data_5490 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C, 15N Resonance Assigments of the Major Cherry Allergen Pru av 1 Mutant E45W ; _BMRB_accession_number 5490 _BMRB_flat_file_name bmr5490.str _Entry_type original _Submission_date 2002-08-05 _Accession_date 2002-08-05 _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 Neudecker Philipp . . 2 Lehmann Katrin . . 3 Nerkamp Joerg . . 4 Schweimer Kristian . . 5 Sticht Heirich . . 6 Boehm Markus . . 7 Scheurer Stephan . . 8 Vieths Stefan . . 9 Roesch Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 855 "13C chemical shifts" 558 "15N chemical shifts" 156 "coupling constants" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-10-06 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4671 'Pru a 1' stop_ _Original_release_date 2003-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12943529 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Neudecker Philipp . . 2 Lehmann Katrin . . 3 Nerkamp Joerg . . 4 Haase Tanja . . 5 Wangorsch Andrea . . 6 Foetisch Kay . . 7 Hoffmann Silke . . 8 Roesch Paul . . 9 Vieths Stefan . . 10 Scheurer Stephan . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 376 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 97 _Page_last 107 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; K. Schweimer, H. Sticht, J. Nerkamp, M. Boehm, M. Breitenbach, S. Vieths and P. Roesch: NMR Spectroscopy Reveals Common Structural Features of the Birch Pollen Allergen Bet v 1 and the Cherry Allergen Pru a 1 Appl. Magn. Reson. 17, 449-464 (1999) ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; P. Neudecker, K. Schweimer, J. Nerkamp, M. Boehm, S. Scheurer, S. Vieths, H. Sticht and P. Roesch: Sequence-specific 1H, 13C and 15N resonance assignments of the major cherry allergen Pru a 1 J. Biomol. NMR 18, 71-72 (2000) ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 11061231 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full ; P. Neudecker, K. Schweimer, J. Nerkamp, S. Scheurer, S. Vieths, H. Sticht and P. Roesch: Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1 J. Biol. Chem. 276, 22756-22763 (2001) ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 11287426 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_4 _Saveframe_category citation _Citation_full ; P. Neudecker, H. Sticht and P. Roesch: Improving the efficiency of the Gaussian conformational database potential for the refinement of protein and nucleic acid structures J. Biomol. NMR. 21, 373-375 (2001) ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 11824757 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Pru_av_1_E45W _Saveframe_category molecular_system _Mol_system_name 'Pru av 1 E45W' _Abbreviation_common 'Pru av 1 E45W' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pru av 1 E45W' $Pru_av_1_E45W stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pru_av_1_E45W _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Pru av 1' _Name_variant E45W _Abbreviation_common 'Pru av 1 E45W' _Molecular_mass 17586 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; GVFTYESEFTSEIPPPRLFK AFVLDADNLVPKIAPQAIKH SEILWGDGGPGTIKKITFGE GSQYGYVKHKIDSIDKENYS YSYTLIEGDALGDTLEKISY ETKLVASPSGGSIIKSTSHY HTKGNVEIKEEHVKAGKEKA SNLFKLIETYLKGHPDAYN ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 VAL 3 PHE 4 THR 5 TYR 6 GLU 7 SER 8 GLU 9 PHE 10 THR 11 SER 12 GLU 13 ILE 14 PRO 15 PRO 16 PRO 17 ARG 18 LEU 19 PHE 20 LYS 21 ALA 22 PHE 23 VAL 24 LEU 25 ASP 26 ALA 27 ASP 28 ASN 29 LEU 30 VAL 31 PRO 32 LYS 33 ILE 34 ALA 35 PRO 36 GLN 37 ALA 38 ILE 39 LYS 40 HIS 41 SER 42 GLU 43 ILE 44 LEU 45 TRP 46 GLY 47 ASP 48 GLY 49 GLY 50 PRO 51 GLY 52 THR 53 ILE 54 LYS 55 LYS 56 ILE 57 THR 58 PHE 59 GLY 60 GLU 61 GLY 62 SER 63 GLN 64 TYR 65 GLY 66 TYR 67 VAL 68 LYS 69 HIS 70 LYS 71 ILE 72 ASP 73 SER 74 ILE 75 ASP 76 LYS 77 GLU 78 ASN 79 TYR 80 SER 81 TYR 82 SER 83 TYR 84 THR 85 LEU 86 ILE 87 GLU 88 GLY 89 ASP 90 ALA 91 LEU 92 GLY 93 ASP 94 THR 95 LEU 96 GLU 97 LYS 98 ILE 99 SER 100 TYR 101 GLU 102 THR 103 LYS 104 LEU 105 VAL 106 ALA 107 SER 108 PRO 109 SER 110 GLY 111 GLY 112 SER 113 ILE 114 ILE 115 LYS 116 SER 117 THR 118 SER 119 HIS 120 TYR 121 HIS 122 THR 123 LYS 124 GLY 125 ASN 126 VAL 127 GLU 128 ILE 129 LYS 130 GLU 131 GLU 132 HIS 133 VAL 134 LYS 135 ALA 136 GLY 137 LYS 138 GLU 139 LYS 140 ALA 141 SER 142 ASN 143 LEU 144 PHE 145 LYS 146 LEU 147 ILE 148 GLU 149 THR 150 TYR 151 LEU 152 LYS 153 GLY 154 HIS 155 PRO 156 ASP 157 ALA 158 TYR 159 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 4671 Pru_a_1 100.00 159 99.37 99.37 5.57e-107 PDB 1E09 "Solution Structure Of The Major Cherry Allergen Pru Av 1" 100.00 159 99.37 99.37 5.57e-107 PDB 1H2O "Solution Structure Of The Major Cherry Allergen Pru Av 1 Mutant E45w" 100.00 159 100.00 100.00 6.38e-109 EMBL CAM35495 "pru p 1 [Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 GB AAC02632 "cherry-allergen PRUA1 [Prunus avium]" 100.00 160 99.37 99.37 4.06e-107 GB ABB78006 "major allergen Pru p 1 [Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 GB ABW99628 "pathogenesis related protein PR10 [Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 GB ACE80940 "putative allergen Pru p 1.01 [Prunus dulcis x Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 GB EMJ24835 "hypothetical protein PRUPE_ppa012651mg [Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 REF XP_007223636 "hypothetical protein PRUPE_ppa012651mg [Prunus persica]" 100.00 160 97.48 98.74 6.46e-105 SP O24248 "RecName: Full=Major allergen Pru av 1; AltName: Full=Allergen Pru a 1; AltName: Allergen=Pru av 1 [Prunus avium]" 100.00 160 99.37 99.37 4.06e-107 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pru_av_1_E45W 'sweet cherry' 42229 Eukaryota Viridiplantae Prunus avium 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 $Pru_av_1_E45W 'recombinant technology' 'E. coli' Escherichia coli BL21/DE3 plasmid pET11a 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 $Pru_av_1_E45W 0.7 mM '[U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NDEE _Saveframe_category software _Name NDEE _Version . loop_ _Task 'spectral analysis' stop_ _Details 'SpinUp Inc., Dortmund, Germany' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'spectral analysis' stop_ _Details 'Bruce A. Johnson, Merck and Co., Whitehouse Station, NJ' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_1H,15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _Sample_label $sample_1 save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_3D_1H,15N-TOCSY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N-TOCSY-HSQC' _Sample_label $sample_1 save_ save_3D_1H,15N-NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N-NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_1H,15N/1H,15N-HMQC-NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N/1H,15N-HMQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N-TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H,15N/1H,15N-HMQC-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 ; Chemical shifts of residues other than W45, G46, D47, G48, G51, T52, and I53 are identical to those of wild-type Pru av 1. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Pru av 1 E45W' _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 GLY HA2 H 4.03 0.02 2 2 . 1 GLY HA3 H 3.80 0.02 2 3 . 1 GLY C C 172.85 0.20 1 4 . 1 GLY CA C 45.45 0.20 1 5 . 2 VAL H H 7.40 0.02 1 6 . 2 VAL HA H 4.80 0.02 1 7 . 2 VAL HB H 1.59 0.02 1 8 . 2 VAL HG1 H 0.38 0.02 2 9 . 2 VAL HG2 H 0.35 0.02 2 10 . 2 VAL C C 175.05 0.20 1 11 . 2 VAL CA C 60.67 0.20 1 12 . 2 VAL CB C 33.48 0.20 1 13 . 2 VAL CG1 C 21.03 0.20 2 14 . 2 VAL CG2 C 20.50 0.20 2 15 . 2 VAL N N 120.48 0.20 1 16 . 3 PHE H H 8.77 0.02 1 17 . 3 PHE HA H 4.71 0.02 1 18 . 3 PHE HB2 H 3.09 0.02 2 19 . 3 PHE HB3 H 2.88 0.02 2 20 . 3 PHE HD1 H 7.22 0.02 1 21 . 3 PHE HD2 H 7.22 0.02 1 22 . 3 PHE HE1 H 7.34 0.02 1 23 . 3 PHE HE2 H 7.34 0.02 1 24 . 3 PHE C C 174.33 0.20 1 25 . 3 PHE CA C 57.07 0.20 1 26 . 3 PHE CB C 41.92 0.20 1 27 . 3 PHE N N 128.00 0.20 1 28 . 4 THR H H 8.37 0.02 1 29 . 4 THR HA H 5.30 0.02 1 30 . 4 THR HB H 3.62 0.02 1 31 . 4 THR HG2 H 0.96 0.02 1 32 . 4 THR C C 173.21 0.20 1 33 . 4 THR CA C 62.46 0.20 1 34 . 4 THR CB C 70.92 0.20 1 35 . 4 THR CG2 C 22.20 0.20 1 36 . 4 THR N N 123.52 0.20 1 37 . 5 TYR H H 9.01 0.02 1 38 . 5 TYR HA H 4.71 0.02 1 39 . 5 TYR HB2 H 3.06 0.02 2 40 . 5 TYR HB3 H 2.71 0.02 2 41 . 5 TYR HD1 H 7.07 0.02 1 42 . 5 TYR HD2 H 7.07 0.02 1 43 . 5 TYR HE1 H 6.52 0.02 1 44 . 5 TYR HE2 H 6.52 0.02 1 45 . 5 TYR C C 174.46 0.20 1 46 . 5 TYR CA C 57.15 0.20 1 47 . 5 TYR CB C 41.85 0.20 1 48 . 5 TYR N N 125.69 0.20 1 49 . 6 GLU H H 8.74 0.02 1 50 . 6 GLU HA H 5.23 0.02 1 51 . 6 GLU HB2 H 1.99 0.02 2 52 . 6 GLU HB3 H 1.86 0.02 2 53 . 6 GLU HG2 H 2.12 0.02 1 54 . 6 GLU HG3 H 2.12 0.02 1 55 . 6 GLU C C 175.63 0.20 1 56 . 6 GLU CA C 55.20 0.20 1 57 . 6 GLU CB C 32.84 0.20 1 58 . 6 GLU CG C 36.42 0.20 1 59 . 6 GLU N N 124.55 0.20 1 60 . 7 SER H H 8.91 0.02 1 61 . 7 SER HA H 4.70 0.02 1 62 . 7 SER HB2 H 3.65 0.02 1 63 . 7 SER HB3 H 3.65 0.02 1 64 . 7 SER C C 176.05 0.20 1 65 . 7 SER CA C 57.62 0.20 1 66 . 7 SER CB C 66.55 0.20 1 67 . 7 SER N N 117.35 0.20 1 68 . 8 GLU H H 8.22 0.02 1 69 . 8 GLU HA H 5.41 0.02 1 70 . 8 GLU HB2 H 1.78 0.02 1 71 . 8 GLU HB3 H 1.78 0.02 1 72 . 8 GLU HG2 H 2.02 0.02 2 73 . 8 GLU HG3 H 1.94 0.02 2 74 . 8 GLU C C 174.67 0.20 1 75 . 8 GLU CA C 54.74 0.20 1 76 . 8 GLU CB C 33.54 0.20 1 77 . 8 GLU CG C 37.07 0.20 1 78 . 8 GLU N N 122.26 0.20 1 79 . 9 PHE H H 8.67 0.02 1 80 . 9 PHE HA H 5.03 0.02 1 81 . 9 PHE HB2 H 3.16 0.02 2 82 . 9 PHE HB3 H 2.64 0.02 2 83 . 9 PHE HD1 H 6.98 0.02 1 84 . 9 PHE HD2 H 6.98 0.02 1 85 . 9 PHE HE1 H 7.07 0.02 1 86 . 9 PHE HE2 H 7.07 0.02 1 87 . 9 PHE C C 173.94 0.20 1 88 . 9 PHE CA C 55.16 0.20 1 89 . 9 PHE CB C 41.18 0.20 1 90 . 9 PHE N N 122.18 0.20 1 91 . 10 THR H H 8.43 0.02 1 92 . 10 THR HA H 5.03 0.02 1 93 . 10 THR HB H 4.15 0.02 1 94 . 10 THR HG2 H 1.14 0.02 1 95 . 10 THR C C 173.37 0.20 1 96 . 10 THR CA C 60.68 0.20 1 97 . 10 THR CB C 71.32 0.20 1 98 . 10 THR CG2 C 21.66 0.20 1 99 . 10 THR N N 112.36 0.20 1 100 . 11 SER H H 8.61 0.02 1 101 . 11 SER HA H 4.90 0.02 1 102 . 11 SER HB2 H 3.72 0.02 2 103 . 11 SER HB3 H 3.31 0.02 2 104 . 11 SER HG H 6.75 0.02 1 105 . 11 SER C C 175.44 0.20 1 106 . 11 SER CA C 56.06 0.20 1 107 . 11 SER CB C 66.17 0.20 1 108 . 11 SER N N 114.28 0.20 1 109 . 12 GLU H H 9.30 0.02 1 110 . 12 GLU HA H 4.29 0.02 1 111 . 12 GLU HB2 H 2.15 0.02 2 112 . 12 GLU HB3 H 1.81 0.02 2 113 . 12 GLU HG2 H 2.26 0.02 1 114 . 12 GLU HG3 H 2.26 0.02 1 115 . 12 GLU C C 175.93 0.20 1 116 . 12 GLU CA C 57.40 0.20 1 117 . 12 GLU CB C 30.51 0.20 1 118 . 12 GLU CG C 36.78 0.20 1 119 . 12 GLU N N 127.45 0.20 1 120 . 13 ILE H H 8.49 0.02 1 121 . 13 ILE HA H 4.42 0.02 1 122 . 13 ILE HB H 2.15 0.02 1 123 . 13 ILE HG12 H 1.65 0.02 2 124 . 13 ILE HG13 H 1.27 0.02 2 125 . 13 ILE HG2 H 1.09 0.02 1 126 . 13 ILE HD1 H 0.75 0.02 1 127 . 13 ILE CA C 56.48 0.20 1 128 . 13 ILE CB C 36.68 0.20 1 129 . 13 ILE CG1 C 26.71 0.20 1 130 . 13 ILE CG2 C 17.39 0.20 1 131 . 13 ILE CD1 C 9.38 0.20 1 132 . 13 ILE N N 122.31 0.20 1 133 . 16 PRO HA H 3.96 0.02 1 134 . 16 PRO HB2 H 2.42 0.02 2 135 . 16 PRO HB3 H 1.91 0.02 2 136 . 16 PRO HG2 H 2.05 0.02 1 137 . 16 PRO HG3 H 2.05 0.02 1 138 . 16 PRO HD2 H 3.41 0.02 2 139 . 16 PRO HD3 H 3.29 0.02 2 140 . 16 PRO C C 179.32 0.20 1 141 . 16 PRO CA C 66.57 0.20 1 142 . 16 PRO CB C 30.44 0.20 1 143 . 16 PRO CG C 28.22 0.20 1 144 . 16 PRO CD C 49.44 0.20 1 145 . 17 ARG H H 6.59 0.02 1 146 . 17 ARG HA H 4.22 0.02 1 147 . 17 ARG HB2 H 1.81 0.02 2 148 . 17 ARG HB3 H 1.60 0.02 2 149 . 17 ARG HG2 H 1.42 0.02 1 150 . 17 ARG HG3 H 1.42 0.02 1 151 . 17 ARG HD2 H 3.27 0.02 1 152 . 17 ARG HD3 H 3.27 0.02 1 153 . 17 ARG HE H 6.75 0.02 1 154 . 17 ARG C C 177.21 0.20 1 155 . 17 ARG CA C 58.94 0.20 1 156 . 17 ARG CB C 30.88 0.20 1 157 . 17 ARG CG C 28.43 0.20 1 158 . 17 ARG CD C 44.37 0.20 1 159 . 17 ARG CZ C 159.56 0.20 1 160 . 17 ARG N N 115.54 0.20 1 161 . 17 ARG NE N 85.48 0.20 1 162 . 18 LEU H H 7.60 0.02 1 163 . 18 LEU HA H 3.82 0.02 1 164 . 18 LEU HB2 H 1.53 0.02 2 165 . 18 LEU HB3 H 1.25 0.02 2 166 . 18 LEU HG H 1.57 0.02 1 167 . 18 LEU HD1 H 0.83 0.02 2 168 . 18 LEU HD2 H 0.78 0.02 2 169 . 18 LEU C C 178.33 0.20 1 170 . 18 LEU CA C 57.51 0.20 1 171 . 18 LEU CB C 42.03 0.20 1 172 . 18 LEU CG C 27.40 0.20 1 173 . 18 LEU CD1 C 23.50 0.20 2 174 . 18 LEU CD2 C 24.99 0.20 2 175 . 18 LEU N N 118.12 0.20 1 176 . 19 PHE H H 9.19 0.02 1 177 . 19 PHE HA H 3.84 0.02 1 178 . 19 PHE HB2 H 3.17 0.02 2 179 . 19 PHE HB3 H 3.01 0.02 2 180 . 19 PHE HD1 H 7.18 0.02 1 181 . 19 PHE HD2 H 7.18 0.02 1 182 . 19 PHE HE1 H 7.13 0.02 1 183 . 19 PHE HE2 H 7.13 0.02 1 184 . 19 PHE C C 177.80 0.20 1 185 . 19 PHE CA C 62.43 0.20 1 186 . 19 PHE CB C 40.22 0.20 1 187 . 19 PHE N N 118.70 0.20 1 188 . 20 LYS H H 7.56 0.02 1 189 . 20 LYS HA H 3.69 0.02 1 190 . 20 LYS HB2 H 2.04 0.02 2 191 . 20 LYS HB3 H 1.95 0.02 2 192 . 20 LYS HG2 H 1.55 0.02 1 193 . 20 LYS HG3 H 1.55 0.02 1 194 . 20 LYS HD2 H 1.82 0.02 1 195 . 20 LYS HD3 H 1.82 0.02 1 196 . 20 LYS HE2 H 3.01 0.02 1 197 . 20 LYS HE3 H 3.01 0.02 1 198 . 20 LYS C C 176.30 0.20 1 199 . 20 LYS CA C 60.35 0.20 1 200 . 20 LYS CB C 33.26 0.20 1 201 . 20 LYS CG C 26.40 0.20 1 202 . 20 LYS CD C 29.45 0.20 1 203 . 20 LYS N N 117.89 0.20 1 204 . 21 ALA H H 7.04 0.02 1 205 . 21 ALA HA H 3.18 0.02 1 206 . 21 ALA HB H 0.82 0.02 1 207 . 21 ALA C C 175.26 0.20 1 208 . 21 ALA CA C 54.39 0.20 1 209 . 21 ALA CB C 20.59 0.20 1 210 . 21 ALA N N 118.15 0.20 1 211 . 22 PHE H H 8.22 0.02 1 212 . 22 PHE HA H 4.15 0.02 1 213 . 22 PHE HB2 H 2.94 0.02 2 214 . 22 PHE HB3 H 2.80 0.02 2 215 . 22 PHE HD1 H 6.91 0.02 1 216 . 22 PHE HD2 H 6.91 0.02 1 217 . 22 PHE HE1 H 7.14 0.02 1 218 . 22 PHE HE2 H 7.14 0.02 1 219 . 22 PHE C C 174.01 0.20 1 220 . 22 PHE CA C 58.19 0.20 1 221 . 22 PHE CB C 40.29 0.20 1 222 . 22 PHE N N 110.09 0.20 1 223 . 23 VAL H H 7.11 0.02 1 224 . 23 VAL HA H 3.13 0.02 1 225 . 23 VAL HB H 0.79 0.02 1 226 . 23 VAL HG1 H 0.08 0.02 2 227 . 23 VAL HG2 H -0.30 0.02 2 228 . 23 VAL C C 177.64 0.20 1 229 . 23 VAL CA C 63.71 0.20 1 230 . 23 VAL CB C 30.82 0.20 1 231 . 23 VAL CG1 C 21.25 0.20 2 232 . 23 VAL CG2 C 20.16 0.20 2 233 . 23 VAL N N 114.12 0.20 1 234 . 24 LEU H H 7.04 0.02 1 235 . 24 LEU HA H 3.85 0.02 1 236 . 24 LEU HB2 H 2.02 0.02 2 237 . 24 LEU HB3 H 1.46 0.02 2 238 . 24 LEU HG H 1.04 0.02 1 239 . 24 LEU HD1 H 1.20 0.02 2 240 . 24 LEU HD2 H 0.73 0.02 2 241 . 24 LEU C C 178.51 0.20 1 242 . 24 LEU CA C 57.28 0.20 1 243 . 24 LEU CB C 40.35 0.20 1 244 . 24 LEU CG C 25.39 0.20 1 245 . 24 LEU N N 115.24 0.20 1 246 . 25 ASP H H 7.65 0.02 1 247 . 25 ASP HA H 5.35 0.02 1 248 . 25 ASP HB2 H 2.80 0.02 2 249 . 25 ASP HB3 H 2.44 0.02 2 250 . 25 ASP C C 177.47 0.20 1 251 . 25 ASP CA C 53.06 0.20 1 252 . 25 ASP CB C 43.53 0.20 1 253 . 25 ASP N N 117.01 0.20 1 254 . 26 ALA H H 6.38 0.02 1 255 . 26 ALA HA H 3.71 0.02 1 256 . 26 ALA HB H 1.11 0.02 1 257 . 26 ALA C C 178.70 0.20 1 258 . 26 ALA CA C 56.28 0.20 1 259 . 26 ALA CB C 18.93 0.20 1 260 . 26 ALA N N 122.84 0.20 1 261 . 27 ASP H H 8.11 0.02 1 262 . 27 ASP HA H 3.97 0.02 1 263 . 27 ASP HB2 H 2.51 0.02 2 264 . 27 ASP HB3 H 2.32 0.02 2 265 . 27 ASP C C 175.90 0.20 1 266 . 27 ASP CA C 56.77 0.20 1 267 . 27 ASP CB C 39.86 0.20 1 268 . 27 ASP N N 113.49 0.20 1 269 . 28 ASN H H 7.24 0.02 1 270 . 28 ASN HA H 4.67 0.02 1 271 . 28 ASN HB2 H 2.70 0.02 2 272 . 28 ASN HB3 H 2.64 0.02 2 273 . 28 ASN HD21 H 8.26 0.02 2 274 . 28 ASN HD22 H 6.89 0.02 2 275 . 28 ASN C C 176.24 0.20 1 276 . 28 ASN CA C 53.77 0.20 1 277 . 28 ASN CB C 40.06 0.20 1 278 . 28 ASN N N 113.13 0.20 1 279 . 28 ASN ND2 N 116.14 0.20 1 280 . 29 LEU H H 8.16 0.02 1 281 . 29 LEU HA H 4.01 0.02 1 282 . 29 LEU HB2 H 1.68 0.02 2 283 . 29 LEU HB3 H 1.41 0.02 2 284 . 29 LEU HG H 1.04 0.02 1 285 . 29 LEU HD1 H 0.62 0.02 2 286 . 29 LEU HD2 H 0.41 0.02 2 287 . 29 LEU C C 177.95 0.20 1 288 . 29 LEU CA C 57.59 0.20 1 289 . 29 LEU CB C 42.75 0.20 1 290 . 29 LEU CG C 27.10 0.20 1 291 . 29 LEU CD1 C 25.76 0.20 2 292 . 29 LEU CD2 C 22.13 0.20 2 293 . 29 LEU N N 120.79 0.20 1 294 . 30 VAL H H 8.28 0.02 1 295 . 30 VAL HA H 3.45 0.02 1 296 . 30 VAL HB H 2.14 0.02 1 297 . 30 VAL HG1 H 0.91 0.02 2 298 . 30 VAL HG2 H 0.88 0.02 2 299 . 30 VAL CA C 68.85 0.20 1 300 . 30 VAL CB C 28.81 0.20 1 301 . 30 VAL CG1 C 23.65 0.20 2 302 . 30 VAL CG2 C 23.12 0.20 2 303 . 30 VAL N N 116.85 0.20 1 304 . 31 PRO HA H 4.47 0.02 1 305 . 31 PRO HB2 H 2.33 0.02 2 306 . 31 PRO HB3 H 1.58 0.02 2 307 . 31 PRO HG2 H 2.00 0.02 1 308 . 31 PRO HG3 H 2.00 0.02 1 309 . 31 PRO HD2 H 3.36 0.02 2 310 . 31 PRO HD3 H 3.08 0.02 2 311 . 31 PRO C C 177.60 0.20 1 312 . 31 PRO CA C 65.54 0.20 1 313 . 31 PRO CB C 31.24 0.20 1 314 . 31 PRO CG C 28.30 0.20 1 315 . 31 PRO CD C 50.27 0.20 1 316 . 32 LYS H H 6.95 0.02 1 317 . 32 LYS HA H 4.09 0.02 1 318 . 32 LYS HB2 H 1.85 0.02 2 319 . 32 LYS HB3 H 1.53 0.02 2 320 . 32 LYS HG2 H 1.32 0.02 1 321 . 32 LYS HG3 H 1.32 0.02 1 322 . 32 LYS C C 178.15 0.20 1 323 . 32 LYS CA C 58.04 0.20 1 324 . 32 LYS CB C 32.95 0.20 1 325 . 32 LYS N N 112.26 0.20 1 326 . 33 ILE H H 7.41 0.02 1 327 . 33 ILE HA H 4.34 0.02 1 328 . 33 ILE HB H 1.86 0.02 1 329 . 33 ILE HG12 H 1.19 0.02 2 330 . 33 ILE HG13 H 1.05 0.02 2 331 . 33 ILE HG2 H 0.57 0.02 1 332 . 33 ILE HD1 H 0.47 0.02 1 333 . 33 ILE CA C 61.50 0.20 1 334 . 33 ILE CB C 39.55 0.20 1 335 . 33 ILE CG1 C 25.60 0.20 1 336 . 33 ILE CG2 C 18.33 0.20 1 337 . 33 ILE CD1 C 14.14 0.20 1 338 . 33 ILE N N 111.38 0.20 1 339 . 34 ALA H H 8.85 0.02 1 340 . 34 ALA HA H 4.84 0.02 1 341 . 34 ALA HB H 1.15 0.02 1 342 . 34 ALA CA C 50.65 0.20 1 343 . 34 ALA CB C 19.21 0.20 1 344 . 34 ALA N N 124.96 0.20 1 345 . 35 PRO HA H 4.62 0.02 1 346 . 35 PRO HB2 H 2.41 0.02 2 347 . 35 PRO HB3 H 1.94 0.02 2 348 . 35 PRO HG2 H 1.92 0.02 1 349 . 35 PRO HG3 H 1.92 0.02 1 350 . 35 PRO HD2 H 3.60 0.02 2 351 . 35 PRO HD3 H 3.26 0.02 2 352 . 35 PRO C C 177.47 0.20 1 353 . 35 PRO CA C 64.28 0.20 1 354 . 35 PRO CB C 31.42 0.20 1 355 . 35 PRO CG C 27.17 0.20 1 356 . 35 PRO CD C 50.32 0.20 1 357 . 36 GLN H H 8.64 0.02 1 358 . 36 GLN HA H 4.16 0.02 1 359 . 36 GLN HB2 H 2.03 0.02 2 360 . 36 GLN HB3 H 1.96 0.02 2 361 . 36 GLN HG2 H 2.42 0.02 2 362 . 36 GLN HG3 H 2.25 0.02 2 363 . 36 GLN HE21 H 7.55 0.02 2 364 . 36 GLN HE22 H 6.90 0.02 2 365 . 36 GLN C C 175.97 0.20 1 366 . 36 GLN CA C 57.20 0.20 1 367 . 36 GLN CB C 27.52 0.20 1 368 . 36 GLN CG C 33.47 0.20 1 369 . 36 GLN N N 115.89 0.20 1 370 . 36 GLN NE2 N 111.73 0.20 1 371 . 37 ALA H H 8.03 0.02 1 372 . 37 ALA HA H 4.29 0.02 1 373 . 37 ALA HB H 1.34 0.02 1 374 . 37 ALA CA C 53.67 0.20 1 375 . 37 ALA CB C 19.53 0.20 1 376 . 37 ALA N N 123.60 0.20 1 377 . 38 ILE H H 7.37 0.02 1 378 . 38 ILE HA H 4.03 0.02 1 379 . 38 ILE HB H 1.47 0.02 1 380 . 38 ILE HG12 H 1.31 0.02 2 381 . 38 ILE HG13 H 0.92 0.02 2 382 . 38 ILE HG2 H 0.61 0.02 1 383 . 38 ILE HD1 H 0.66 0.02 1 384 . 38 ILE C C 173.04 0.20 1 385 . 38 ILE CA C 61.85 0.20 1 386 . 38 ILE CB C 41.40 0.20 1 387 . 38 ILE CG1 C 27.26 0.20 1 388 . 38 ILE CG2 C 17.00 0.20 1 389 . 38 ILE CD1 C 12.92 0.20 1 390 . 38 ILE N N 116.23 0.20 1 391 . 39 LYS H H 8.76 0.02 1 392 . 39 LYS HA H 4.41 0.02 1 393 . 39 LYS HB2 H 1.69 0.02 2 394 . 39 LYS HB3 H 1.50 0.02 2 395 . 39 LYS HG2 H 1.24 0.02 1 396 . 39 LYS HG3 H 1.24 0.02 1 397 . 39 LYS HE2 H 2.92 0.02 1 398 . 39 LYS HE3 H 2.92 0.02 1 399 . 39 LYS C C 176.60 0.20 1 400 . 39 LYS CA C 57.10 0.20 1 401 . 39 LYS CB C 34.01 0.20 1 402 . 39 LYS CG C 24.86 0.20 1 403 . 39 LYS CD C 29.90 0.20 1 404 . 39 LYS N N 125.37 0.20 1 405 . 40 HIS H H 7.64 0.02 1 406 . 40 HIS HA H 4.65 0.02 1 407 . 40 HIS HB2 H 3.03 0.02 2 408 . 40 HIS HB3 H 2.99 0.02 2 409 . 40 HIS HD2 H 6.86 0.02 1 410 . 40 HIS HE1 H 7.66 0.02 1 411 . 40 HIS C C 172.42 0.20 1 412 . 40 HIS CA C 55.77 0.20 1 413 . 40 HIS CB C 33.23 0.20 1 414 . 40 HIS N N 114.86 0.20 1 415 . 41 SER H H 7.90 0.02 1 416 . 41 SER HA H 5.11 0.02 1 417 . 41 SER HB2 H 3.46 0.02 2 418 . 41 SER HB3 H 3.32 0.02 2 419 . 41 SER C C 172.58 0.20 1 420 . 41 SER CA C 56.36 0.20 1 421 . 41 SER CB C 64.77 0.20 1 422 . 41 SER N N 118.18 0.20 1 423 . 42 GLU H H 8.57 0.02 1 424 . 42 GLU HA H 4.59 0.02 1 425 . 42 GLU HB2 H 2.04 0.02 2 426 . 42 GLU HB3 H 1.88 0.02 2 427 . 42 GLU C C 174.73 0.20 1 428 . 42 GLU CA C 54.30 0.20 1 429 . 42 GLU CB C 33.88 0.20 1 430 . 42 GLU CG C 35.92 0.20 1 431 . 42 GLU N N 123.77 0.20 1 432 . 43 ILE H H 8.84 0.02 1 433 . 43 ILE HA H 4.03 0.02 1 434 . 43 ILE HB H 1.76 0.02 1 435 . 43 ILE HG12 H 1.60 0.02 1 436 . 43 ILE HG13 H 1.60 0.02 1 437 . 43 ILE HG2 H 0.69 0.02 1 438 . 43 ILE HD1 H 0.70 0.02 1 439 . 43 ILE C C 176.26 0.20 1 440 . 43 ILE CA C 62.10 0.20 1 441 . 43 ILE CB C 37.74 0.20 1 442 . 43 ILE CG1 C 28.76 0.20 1 443 . 43 ILE CG2 C 18.09 0.20 1 444 . 43 ILE CD1 C 11.80 0.20 1 445 . 43 ILE N N 125.18 0.20 1 446 . 44 LEU H H 9.13 0.02 1 447 . 44 LEU HA H 4.41 0.02 1 448 . 44 LEU HB2 H 1.60 0.02 1 449 . 44 LEU HB3 H 1.60 0.02 1 450 . 44 LEU C C 177.23 0.20 1 451 . 44 LEU CA C 55.88 0.20 1 452 . 44 LEU CB C 42.56 0.20 1 453 . 44 LEU N N 129.14 0.20 1 454 . 45 TRP H H 7.78 0.02 1 455 . 45 TRP HA H 4.55 0.02 1 456 . 45 TRP HB2 H 3.39 0.02 2 457 . 45 TRP HB3 H 2.96 0.02 2 458 . 45 TRP HD1 H 7.37 0.02 1 459 . 45 TRP HE1 H 10.13 0.02 1 460 . 45 TRP HE3 H 7.66 0.02 1 461 . 45 TRP HZ2 H 7.49 0.02 1 462 . 45 TRP HZ3 H 7.09 0.02 1 463 . 45 TRP HH2 H 7.24 0.02 1 464 . 45 TRP N N 119.59 0.20 1 465 . 45 TRP NE1 N 129.63 0.20 1 466 . 46 GLY H H 7.65 0.02 1 467 . 46 GLY HA2 H 4.41 0.02 2 468 . 46 GLY HA3 H 3.01 0.02 2 469 . 46 GLY N N 113.62 0.20 1 470 . 47 ASP H H 7.65 0.02 1 471 . 47 ASP HA H 4.61 0.02 1 472 . 47 ASP HB2 H 2.97 0.02 2 473 . 47 ASP HB3 H 2.41 0.02 2 474 . 47 ASP N N 115.05 0.20 1 475 . 48 GLY H H 8.68 0.02 1 476 . 48 GLY HA2 H 4.64 0.02 2 477 . 48 GLY HA3 H 3.39 0.02 2 478 . 48 GLY N N 110.66 0.20 1 479 . 49 GLY H H 8.25 0.02 1 480 . 49 GLY HA2 H 4.46 0.02 2 481 . 49 GLY HA3 H 4.00 0.02 2 482 . 49 GLY CA C 43.54 0.20 1 483 . 49 GLY N N 106.83 0.20 1 484 . 50 PRO HA H 3.95 0.02 1 485 . 50 PRO HB2 H 2.32 0.02 2 486 . 50 PRO HB3 H 1.95 0.02 2 487 . 50 PRO HG2 H 1.96 0.02 1 488 . 50 PRO HG3 H 1.96 0.02 1 489 . 50 PRO HD2 H 3.75 0.02 2 490 . 50 PRO HD3 H 3.61 0.02 2 491 . 50 PRO C C 176.52 0.20 1 492 . 50 PRO CA C 64.73 0.20 1 493 . 50 PRO CB C 31.32 0.20 1 494 . 50 PRO CG C 26.43 0.20 1 495 . 50 PRO CD C 49.91 0.20 1 496 . 51 GLY H H 9.48 0.02 1 497 . 51 GLY HA2 H 4.69 0.02 2 498 . 51 GLY HA3 H 3.59 0.02 2 499 . 51 GLY N N 114.77 0.20 1 500 . 52 THR H H 7.98 0.02 1 501 . 52 THR HA H 4.80 0.02 1 502 . 52 THR HB H 4.03 0.02 1 503 . 52 THR HG1 H 6.79 0.02 1 504 . 52 THR HG2 H 1.27 0.02 1 505 . 52 THR N N 117.54 0.20 1 506 . 53 ILE H H 8.96 0.02 1 507 . 53 ILE HA H 5.33 0.02 1 508 . 53 ILE HB H 1.96 0.02 1 509 . 53 ILE HG2 H 0.96 0.02 1 510 . 53 ILE HD1 H 0.85 0.02 1 511 . 53 ILE N N 125.69 0.20 1 512 . 54 LYS H H 9.41 0.02 1 513 . 54 LYS HA H 5.26 0.02 1 514 . 54 LYS HB2 H 1.55 0.02 2 515 . 54 LYS HB3 H 1.47 0.02 2 516 . 54 LYS HG2 H 1.25 0.02 1 517 . 54 LYS HG3 H 1.25 0.02 1 518 . 54 LYS C C 174.30 0.20 1 519 . 54 LYS CA C 54.11 0.20 1 520 . 54 LYS CB C 36.42 0.20 1 521 . 54 LYS CG C 25.33 0.20 1 522 . 54 LYS N N 126.67 0.20 1 523 . 55 LYS H H 9.23 0.02 1 524 . 55 LYS HA H 5.13 0.02 1 525 . 55 LYS HB2 H 1.84 0.02 2 526 . 55 LYS HB3 H 1.44 0.02 2 527 . 55 LYS C C 174.94 0.20 1 528 . 55 LYS CA C 54.82 0.20 1 529 . 55 LYS CB C 35.97 0.20 1 530 . 55 LYS N N 123.50 0.20 1 531 . 56 ILE H H 9.17 0.02 1 532 . 56 ILE HA H 4.62 0.02 1 533 . 56 ILE HB H 1.52 0.02 1 534 . 56 ILE HG12 H 1.07 0.02 2 535 . 56 ILE HG13 H 0.87 0.02 2 536 . 56 ILE HG2 H 0.64 0.02 1 537 . 56 ILE HD1 H 0.35 0.02 1 538 . 56 ILE C C 174.84 0.20 1 539 . 56 ILE CA C 60.52 0.20 1 540 . 56 ILE CB C 39.62 0.20 1 541 . 56 ILE CG1 C 27.87 0.20 1 542 . 56 ILE CG2 C 18.94 0.20 1 543 . 56 ILE CD1 C 13.43 0.20 1 544 . 56 ILE N N 132.34 0.20 1 545 . 57 THR H H 8.78 0.02 1 546 . 57 THR HA H 4.79 0.02 1 547 . 57 THR HB H 3.85 0.02 1 548 . 57 THR HG2 H 1.21 0.02 1 549 . 57 THR C C 175.73 0.20 1 550 . 57 THR CA C 61.33 0.20 1 551 . 57 THR CB C 70.13 0.20 1 552 . 57 THR CG2 C 21.71 0.20 1 553 . 57 THR N N 121.78 0.20 1 554 . 58 PHE H H 8.36 0.02 1 555 . 58 PHE HA H 4.91 0.02 1 556 . 58 PHE HB2 H 3.11 0.02 2 557 . 58 PHE HB3 H 2.93 0.02 2 558 . 58 PHE HD1 H 7.05 0.02 1 559 . 58 PHE HD2 H 7.05 0.02 1 560 . 58 PHE HE1 H 7.15 0.02 1 561 . 58 PHE HE2 H 7.15 0.02 1 562 . 58 PHE C C 174.37 0.20 1 563 . 58 PHE CA C 56.66 0.20 1 564 . 58 PHE CB C 40.98 0.20 1 565 . 58 PHE N N 123.93 0.20 1 566 . 59 GLY H H 8.02 0.02 1 567 . 59 GLY HA2 H 4.10 0.02 2 568 . 59 GLY HA3 H 3.97 0.02 2 569 . 59 GLY C C 173.06 0.20 1 570 . 59 GLY CA C 44.68 0.20 1 571 . 59 GLY N N 105.42 0.20 1 572 . 60 GLU H H 8.15 0.02 1 573 . 60 GLU HA H 4.28 0.02 1 574 . 60 GLU HB2 H 2.01 0.02 2 575 . 60 GLU HB3 H 1.90 0.02 2 576 . 60 GLU HG2 H 2.20 0.02 1 577 . 60 GLU HG3 H 2.20 0.02 1 578 . 60 GLU C C 176.17 0.20 1 579 . 60 GLU CA C 56.49 0.20 1 580 . 60 GLU CB C 30.39 0.20 1 581 . 60 GLU N N 119.05 0.20 1 582 . 61 GLY H H 8.50 0.02 1 583 . 61 GLY HA2 H 4.02 0.02 2 584 . 61 GLY HA3 H 3.83 0.02 2 585 . 61 GLY CA C 45.39 0.20 1 586 . 61 GLY N N 111.03 0.20 1 587 . 63 GLN HG2 H 2.18 0.02 2 588 . 63 GLN HE21 H 7.40 0.02 2 589 . 63 GLN HE22 H 6.73 0.02 2 590 . 63 GLN C C 174.94 0.20 1 591 . 63 GLN CA C 56.12 0.20 1 592 . 63 GLN CB C 28.81 0.20 1 593 . 63 GLN CG C 33.82 0.20 1 594 . 63 GLN NE2 N 112.14 0.20 1 595 . 64 TYR H H 7.76 0.02 1 596 . 64 TYR HA H 4.77 0.02 1 597 . 64 TYR HB2 H 2.87 0.02 2 598 . 64 TYR HB3 H 2.72 0.02 2 599 . 64 TYR HD1 H 6.92 0.02 1 600 . 64 TYR HD2 H 6.92 0.02 1 601 . 64 TYR C C 175.62 0.20 1 602 . 64 TYR CA C 56.95 0.20 1 603 . 64 TYR CB C 39.38 0.20 1 604 . 64 TYR N N 119.37 0.20 1 605 . 65 GLY H H 8.21 0.02 1 606 . 65 GLY HA2 H 4.01 0.02 2 607 . 65 GLY HA3 H 3.65 0.02 2 608 . 65 GLY C C 176.55 0.20 1 609 . 65 GLY CA C 45.13 0.20 1 610 . 65 GLY N N 111.00 0.20 1 611 . 66 TYR H H 7.95 0.02 1 612 . 66 TYR HA H 5.62 0.02 1 613 . 66 TYR HB2 H 2.86 0.02 1 614 . 66 TYR HB3 H 2.86 0.02 1 615 . 66 TYR HD1 H 6.83 0.02 1 616 . 66 TYR HD2 H 6.83 0.02 1 617 . 66 TYR HE1 H 6.71 0.02 1 618 . 66 TYR HE2 H 6.71 0.02 1 619 . 66 TYR C C 174.64 0.20 1 620 . 66 TYR CA C 56.10 0.20 1 621 . 66 TYR CB C 41.65 0.20 1 622 . 66 TYR N N 115.33 0.20 1 623 . 67 VAL H H 8.92 0.02 1 624 . 67 VAL HA H 4.93 0.02 1 625 . 67 VAL HB H 2.29 0.02 1 626 . 67 VAL HG1 H 1.16 0.02 2 627 . 67 VAL HG2 H 0.77 0.02 2 628 . 67 VAL C C 175.26 0.20 1 629 . 67 VAL CA C 59.61 0.20 1 630 . 67 VAL CB C 36.49 0.20 1 631 . 67 VAL CG1 C 23.59 0.20 2 632 . 67 VAL CG2 C 19.25 0.20 2 633 . 67 VAL N N 113.33 0.20 1 634 . 68 LYS H H 8.56 0.02 1 635 . 68 LYS HA H 5.67 0.02 1 636 . 68 LYS HB2 H 1.68 0.02 2 637 . 68 LYS HB3 H 1.65 0.02 2 638 . 68 LYS C C 175.67 0.20 1 639 . 68 LYS CA C 55.31 0.20 1 640 . 68 LYS CB C 36.49 0.20 1 641 . 68 LYS N N 118.58 0.20 1 642 . 69 HIS H H 9.05 0.02 1 643 . 69 HIS HA H 5.91 0.02 1 644 . 69 HIS HB2 H 2.83 0.02 2 645 . 69 HIS HB3 H 2.78 0.02 2 646 . 69 HIS HD2 H 6.83 0.02 1 647 . 69 HIS HE1 H 7.30 0.02 1 648 . 69 HIS C C 174.03 0.20 1 649 . 69 HIS CA C 52.25 0.20 1 650 . 69 HIS CB C 35.83 0.20 1 651 . 69 HIS N N 122.54 0.20 1 652 . 70 LYS H H 9.68 0.02 1 653 . 70 LYS HA H 5.54 0.02 1 654 . 70 LYS HB2 H 1.83 0.02 2 655 . 70 LYS HB3 H 1.50 0.02 2 656 . 70 LYS C C 175.84 0.20 1 657 . 70 LYS CA C 53.80 0.20 1 658 . 70 LYS CB C 35.98 0.20 1 659 . 70 LYS N N 123.68 0.20 1 660 . 71 ILE H H 9.22 0.02 1 661 . 71 ILE HA H 3.95 0.02 1 662 . 71 ILE HB H 2.07 0.02 1 663 . 71 ILE HG12 H 1.58 0.02 2 664 . 71 ILE HG13 H 1.46 0.02 2 665 . 71 ILE HG2 H 0.92 0.02 1 666 . 71 ILE HD1 H 0.84 0.02 1 667 . 71 ILE C C 175.17 0.20 1 668 . 71 ILE CA C 62.30 0.20 1 669 . 71 ILE CB C 36.73 0.20 1 670 . 71 ILE CG1 C 27.59 0.20 1 671 . 71 ILE CG2 C 17.14 0.20 1 672 . 71 ILE CD1 C 11.75 0.20 1 673 . 71 ILE N N 126.68 0.20 1 674 . 72 ASP H H 9.02 0.02 1 675 . 72 ASP HA H 4.91 0.02 1 676 . 72 ASP HB2 H 2.56 0.02 2 677 . 72 ASP HB3 H 2.34 0.02 2 678 . 72 ASP C C 176.23 0.20 1 679 . 72 ASP CA C 56.59 0.20 1 680 . 72 ASP CB C 42.83 0.20 1 681 . 72 ASP N N 130.80 0.20 1 682 . 73 SER H H 8.20 0.02 1 683 . 73 SER HA H 4.59 0.02 1 684 . 73 SER HB2 H 3.81 0.02 2 685 . 73 SER HB3 H 3.78 0.02 2 686 . 73 SER C C 172.32 0.20 1 687 . 73 SER CA C 58.37 0.20 1 688 . 73 SER CB C 64.89 0.20 1 689 . 73 SER N N 112.57 0.20 1 690 . 74 ILE H H 8.53 0.02 1 691 . 74 ILE HA H 4.66 0.02 1 692 . 74 ILE HB H 1.96 0.02 1 693 . 74 ILE HG12 H 1.71 0.02 2 694 . 74 ILE HG13 H 1.22 0.02 2 695 . 74 ILE HG2 H 1.04 0.02 1 696 . 74 ILE HD1 H 0.95 0.02 1 697 . 74 ILE C C 173.69 0.20 1 698 . 74 ILE CA C 62.18 0.20 1 699 . 74 ILE CB C 41.50 0.20 1 700 . 74 ILE CG1 C 28.51 0.20 1 701 . 74 ILE CG2 C 17.32 0.20 1 702 . 74 ILE CD1 C 14.37 0.20 1 703 . 74 ILE N N 122.06 0.20 1 704 . 75 ASP H H 9.06 0.02 1 705 . 75 ASP HA H 5.01 0.02 1 706 . 75 ASP HB2 H 3.11 0.02 2 707 . 75 ASP HB3 H 2.45 0.02 2 708 . 75 ASP C C 176.34 0.20 1 709 . 75 ASP CA C 52.28 0.20 1 710 . 75 ASP CB C 41.58 0.20 1 711 . 75 ASP N N 127.87 0.20 1 712 . 76 LYS H H 8.80 0.02 1 713 . 76 LYS HA H 3.82 0.02 1 714 . 76 LYS HB2 H 1.87 0.02 1 715 . 76 LYS HB3 H 1.87 0.02 1 716 . 76 LYS HG2 H 1.57 0.02 2 717 . 76 LYS HG3 H 1.51 0.02 2 718 . 76 LYS C C 176.69 0.20 1 719 . 76 LYS CA C 58.21 0.20 1 720 . 76 LYS CB C 32.57 0.20 1 721 . 76 LYS CG C 25.95 0.20 1 722 . 76 LYS N N 122.77 0.20 1 723 . 77 GLU H H 8.03 0.02 1 724 . 77 GLU HA H 3.86 0.02 1 725 . 77 GLU HB2 H 1.91 0.02 2 726 . 77 GLU HB3 H 1.86 0.02 2 727 . 77 GLU HG2 H 2.15 0.02 1 728 . 77 GLU HG3 H 2.15 0.02 1 729 . 77 GLU C C 176.32 0.20 1 730 . 77 GLU CA C 57.94 0.20 1 731 . 77 GLU CB C 29.76 0.20 1 732 . 77 GLU CG C 36.68 0.20 1 733 . 77 GLU N N 117.34 0.20 1 734 . 78 ASN H H 7.26 0.02 1 735 . 78 ASN HA H 4.44 0.02 1 736 . 78 ASN HB2 H 2.63 0.02 2 737 . 78 ASN HB3 H 2.24 0.02 2 738 . 78 ASN HD21 H 8.44 0.02 2 739 . 78 ASN HD22 H 6.86 0.02 2 740 . 78 ASN C C 173.57 0.20 1 741 . 78 ASN CA C 51.83 0.20 1 742 . 78 ASN CB C 39.32 0.20 1 743 . 78 ASN N N 113.40 0.20 1 744 . 78 ASN ND2 N 117.23 0.20 1 745 . 79 TYR H H 6.68 0.02 1 746 . 79 TYR HA H 2.82 0.02 1 747 . 79 TYR HB2 H 3.54 0.02 2 748 . 79 TYR HB3 H 2.55 0.02 2 749 . 79 TYR HD1 H 6.43 0.02 1 750 . 79 TYR HD2 H 6.43 0.02 1 751 . 79 TYR HE1 H 6.65 0.02 1 752 . 79 TYR HE2 H 6.65 0.02 1 753 . 79 TYR C C 173.38 0.20 1 754 . 79 TYR CA C 57.59 0.20 1 755 . 79 TYR CB C 35.39 0.20 1 756 . 79 TYR N N 116.50 0.20 1 757 . 80 SER H H 8.15 0.02 1 758 . 80 SER HA H 5.81 0.02 1 759 . 80 SER HB2 H 3.89 0.02 2 760 . 80 SER HB3 H 3.78 0.02 2 761 . 80 SER C C 172.92 0.20 1 762 . 80 SER CA C 56.44 0.20 1 763 . 80 SER CB C 66.66 0.20 1 764 . 80 SER N N 112.06 0.20 1 765 . 81 TYR H H 9.19 0.02 1 766 . 81 TYR HA H 5.47 0.02 1 767 . 81 TYR HB2 H 3.30 0.02 2 768 . 81 TYR HB3 H 2.91 0.02 2 769 . 81 TYR HD1 H 7.13 0.02 1 770 . 81 TYR HD2 H 7.13 0.02 1 771 . 81 TYR HE1 H 6.49 0.02 1 772 . 81 TYR HE2 H 6.49 0.02 1 773 . 81 TYR C C 173.69 0.20 1 774 . 81 TYR CA C 55.91 0.20 1 775 . 81 TYR CB C 43.01 0.20 1 776 . 81 TYR N N 125.08 0.20 1 777 . 82 SER H H 9.18 0.02 1 778 . 82 SER HA H 5.53 0.02 1 779 . 82 SER HB2 H 4.12 0.02 2 780 . 82 SER HB3 H 4.05 0.02 2 781 . 82 SER C C 172.92 0.20 1 782 . 82 SER CA C 56.68 0.20 1 783 . 82 SER CB C 65.69 0.20 1 784 . 82 SER N N 122.78 0.20 1 785 . 83 TYR H H 8.57 0.02 1 786 . 83 TYR HA H 5.33 0.02 1 787 . 83 TYR HB2 H 2.72 0.02 1 788 . 83 TYR HB3 H 2.72 0.02 1 789 . 83 TYR HD1 H 6.06 0.02 1 790 . 83 TYR HD2 H 6.06 0.02 1 791 . 83 TYR HE1 H 5.88 0.02 1 792 . 83 TYR HE2 H 5.88 0.02 1 793 . 83 TYR C C 172.19 0.20 1 794 . 83 TYR CA C 56.64 0.20 1 795 . 83 TYR CB C 40.66 0.20 1 796 . 83 TYR N N 122.13 0.20 1 797 . 84 THR H H 9.55 0.02 1 798 . 84 THR HA H 5.05 0.02 1 799 . 84 THR HB H 3.90 0.02 1 800 . 84 THR HG2 H 0.96 0.02 1 801 . 84 THR C C 173.48 0.20 1 802 . 84 THR CA C 61.84 0.20 1 803 . 84 THR CB C 71.95 0.20 1 804 . 84 THR CG2 C 22.72 0.20 1 805 . 84 THR N N 116.82 0.20 1 806 . 85 LEU H H 9.77 0.02 1 807 . 85 LEU HA H 5.14 0.02 1 808 . 85 LEU HB2 H 2.17 0.02 2 809 . 85 LEU HB3 H 1.82 0.02 2 810 . 85 LEU HG H 1.77 0.02 1 811 . 85 LEU HD1 H 1.28 0.02 2 812 . 85 LEU HD2 H 0.98 0.02 2 813 . 85 LEU C C 175.25 0.20 1 814 . 85 LEU CA C 55.63 0.20 1 815 . 85 LEU CB C 43.41 0.20 1 816 . 85 LEU CG C 28.57 0.20 1 817 . 85 LEU CD1 C 26.33 0.20 2 818 . 85 LEU CD2 C 25.70 0.20 2 819 . 85 LEU N N 130.77 0.20 1 820 . 86 ILE H H 8.04 0.02 1 821 . 86 ILE HA H 4.75 0.02 1 822 . 86 ILE HB H 2.13 0.02 1 823 . 86 ILE HG12 H 1.38 0.02 2 824 . 86 ILE HG13 H 0.91 0.02 2 825 . 86 ILE HG2 H 0.95 0.02 1 826 . 86 ILE HD1 H 0.92 0.02 1 827 . 86 ILE C C 176.07 0.20 1 828 . 86 ILE CA C 61.30 0.20 1 829 . 86 ILE CB C 39.72 0.20 1 830 . 86 ILE CG1 C 26.33 0.20 1 831 . 86 ILE CG2 C 18.90 0.20 1 832 . 86 ILE CD1 C 14.19 0.20 1 833 . 86 ILE N N 117.61 0.20 1 834 . 87 GLU H H 7.57 0.02 1 835 . 87 GLU HA H 4.47 0.02 1 836 . 87 GLU HB2 H 2.24 0.02 2 837 . 87 GLU HB3 H 1.81 0.02 2 838 . 87 GLU HG2 H 2.47 0.02 2 839 . 87 GLU HG3 H 2.25 0.02 2 840 . 87 GLU C C 173.87 0.20 1 841 . 87 GLU CA C 56.92 0.20 1 842 . 87 GLU CB C 34.94 0.20 1 843 . 87 GLU CG C 37.08 0.20 1 844 . 87 GLU N N 121.41 0.20 1 845 . 88 GLY H H 8.77 0.02 1 846 . 88 GLY HA2 H 4.56 0.02 2 847 . 88 GLY HA3 H 3.69 0.02 2 848 . 88 GLY C C 174.08 0.20 1 849 . 88 GLY CA C 45.00 0.20 1 850 . 88 GLY N N 111.78 0.20 1 851 . 89 ASP H H 8.56 0.02 1 852 . 89 ASP HA H 4.34 0.02 1 853 . 89 ASP HB2 H 2.76 0.02 2 854 . 89 ASP HB3 H 2.58 0.02 2 855 . 89 ASP C C 178.03 0.20 1 856 . 89 ASP CA C 57.28 0.20 1 857 . 89 ASP CB C 41.17 0.20 1 858 . 89 ASP N N 121.02 0.20 1 859 . 90 ALA H H 8.24 0.02 1 860 . 90 ALA HA H 4.02 0.02 1 861 . 90 ALA HB H 1.24 0.02 1 862 . 90 ALA C C 178.20 0.20 1 863 . 90 ALA CA C 53.87 0.20 1 864 . 90 ALA CB C 19.08 0.20 1 865 . 90 ALA N N 120.02 0.20 1 866 . 91 LEU H H 7.54 0.02 1 867 . 91 LEU HA H 4.24 0.02 1 868 . 91 LEU HB2 H 1.96 0.02 2 869 . 91 LEU HB3 H 1.74 0.02 2 870 . 91 LEU HG H 1.43 0.02 1 871 . 91 LEU HD1 H 0.77 0.02 2 872 . 91 LEU HD2 H 0.60 0.02 2 873 . 91 LEU C C 177.66 0.20 1 874 . 91 LEU CA C 55.79 0.20 1 875 . 91 LEU CB C 40.24 0.20 1 876 . 91 LEU CG C 27.20 0.20 1 877 . 91 LEU CD1 C 25.12 0.20 2 878 . 91 LEU CD2 C 23.00 0.20 2 879 . 91 LEU N N 114.70 0.20 1 880 . 92 GLY H H 7.59 0.02 1 881 . 92 GLY HA2 H 3.96 0.02 1 882 . 92 GLY HA3 H 3.96 0.02 1 883 . 92 GLY CA C 46.34 0.20 1 884 . 92 GLY N N 105.15 0.20 1 885 . 93 ASP H H 8.79 0.02 1 886 . 93 ASP HA H 4.84 0.02 1 887 . 93 ASP HB2 H 2.73 0.02 1 888 . 93 ASP HB3 H 2.73 0.02 1 889 . 93 ASP C C 177.43 0.20 1 890 . 93 ASP CA C 54.22 0.20 1 891 . 93 ASP CB C 41.43 0.20 1 892 . 93 ASP N N 121.92 0.20 1 893 . 94 THR H H 7.90 0.02 1 894 . 94 THR HA H 4.54 0.02 1 895 . 94 THR HB H 4.38 0.02 1 896 . 94 THR HG2 H 1.23 0.02 1 897 . 94 THR C C 174.18 0.20 1 898 . 94 THR CA C 62.31 0.20 1 899 . 94 THR CB C 70.46 0.20 1 900 . 94 THR CG2 C 22.16 0.20 1 901 . 94 THR N N 107.22 0.20 1 902 . 95 LEU H H 7.63 0.02 1 903 . 95 LEU HA H 5.04 0.02 1 904 . 95 LEU HB2 H 2.05 0.02 2 905 . 95 LEU HB3 H 1.24 0.02 2 906 . 95 LEU HG H 1.75 0.02 1 907 . 95 LEU HD1 H 1.03 0.02 2 908 . 95 LEU HD2 H 0.92 0.02 2 909 . 95 LEU C C 175.67 0.20 1 910 . 95 LEU CA C 53.85 0.20 1 911 . 95 LEU CB C 44.27 0.20 1 912 . 95 LEU CG C 26.36 0.20 1 913 . 95 LEU CD1 C 26.35 0.20 2 914 . 95 LEU CD2 C 24.72 0.20 2 915 . 95 LEU N N 120.43 0.20 1 916 . 96 GLU H H 9.14 0.02 1 917 . 96 GLU HA H 4.18 0.02 1 918 . 96 GLU HB2 H 2.04 0.02 2 919 . 96 GLU HB3 H 1.85 0.02 2 920 . 96 GLU HG2 H 2.20 0.02 1 921 . 96 GLU HG3 H 2.20 0.02 1 922 . 96 GLU C C 175.83 0.20 1 923 . 96 GLU CA C 57.79 0.20 1 924 . 96 GLU CB C 31.65 0.20 1 925 . 96 GLU CG C 36.29 0.20 1 926 . 96 GLU N N 122.88 0.20 1 927 . 97 LYS H H 7.54 0.02 1 928 . 97 LYS HA H 4.73 0.02 1 929 . 97 LYS HB2 H 2.18 0.02 2 930 . 97 LYS HB3 H 1.53 0.02 2 931 . 97 LYS HG2 H 1.53 0.02 1 932 . 97 LYS HG3 H 1.53 0.02 1 933 . 97 LYS C C 174.01 0.20 1 934 . 97 LYS CA C 55.62 0.20 1 935 . 97 LYS CB C 33.48 0.20 1 936 . 97 LYS CG C 22.95 0.20 1 937 . 97 LYS N N 108.65 0.20 1 938 . 98 ILE H H 7.43 0.02 1 939 . 98 ILE HA H 4.84 0.02 1 940 . 98 ILE HB H 1.36 0.02 1 941 . 98 ILE HG12 H 1.36 0.02 2 942 . 98 ILE HG13 H 0.45 0.02 2 943 . 98 ILE HG2 H -0.31 0.02 1 944 . 98 ILE HD1 H 0.66 0.02 1 945 . 98 ILE C C 174.67 0.20 1 946 . 98 ILE CA C 60.76 0.20 1 947 . 98 ILE CB C 41.72 0.20 1 948 . 98 ILE CG1 C 27.19 0.20 1 949 . 98 ILE CG2 C 16.36 0.20 1 950 . 98 ILE CD1 C 14.22 0.20 1 951 . 98 ILE N N 118.03 0.20 1 952 . 99 SER H H 9.10 0.02 1 953 . 99 SER HA H 5.01 0.02 1 954 . 99 SER HB2 H 3.93 0.02 2 955 . 99 SER HB3 H 3.71 0.02 2 956 . 99 SER C C 171.82 0.20 1 957 . 99 SER CA C 57.65 0.20 1 958 . 99 SER CB C 65.38 0.20 1 959 . 99 SER N N 123.16 0.20 1 960 . 100 TYR H H 9.14 0.02 1 961 . 100 TYR HA H 5.21 0.02 1 962 . 100 TYR HB2 H 2.53 0.02 2 963 . 100 TYR HB3 H 1.57 0.02 2 964 . 100 TYR HD1 H 6.52 0.02 1 965 . 100 TYR HD2 H 6.52 0.02 1 966 . 100 TYR HE1 H 6.49 0.02 1 967 . 100 TYR HE2 H 6.49 0.02 1 968 . 100 TYR C C 176.33 0.20 1 969 . 100 TYR CA C 56.89 0.20 1 970 . 100 TYR CB C 41.31 0.20 1 971 . 100 TYR N N 122.36 0.20 1 972 . 101 GLU H H 8.92 0.02 1 973 . 101 GLU HA H 5.00 0.02 1 974 . 101 GLU HB2 H 2.05 0.02 2 975 . 101 GLU HB3 H 2.00 0.02 2 976 . 101 GLU HG2 H 2.13 0.02 1 977 . 101 GLU HG3 H 2.13 0.02 1 978 . 101 GLU CA C 55.67 0.20 1 979 . 101 GLU CB C 33.12 0.20 1 980 . 101 GLU CG C 36.54 0.20 1 981 . 101 GLU N N 121.57 0.20 1 982 . 102 THR H H 9.17 0.02 1 983 . 102 THR HA H 5.49 0.02 1 984 . 102 THR HB H 4.17 0.02 1 985 . 102 THR HG2 H 1.29 0.02 1 986 . 102 THR C C 172.73 0.20 1 987 . 102 THR CA C 61.98 0.20 1 988 . 102 THR CB C 71.78 0.20 1 989 . 102 THR CG2 C 22.24 0.20 1 990 . 102 THR N N 122.66 0.20 1 991 . 103 LYS H H 9.06 0.02 1 992 . 103 LYS HA H 5.34 0.02 1 993 . 103 LYS HB2 H 1.86 0.02 2 994 . 103 LYS HB3 H 1.79 0.02 2 995 . 103 LYS HG2 H 1.42 0.02 1 996 . 103 LYS HG3 H 1.42 0.02 1 997 . 103 LYS HD2 H 1.64 0.02 1 998 . 103 LYS HD3 H 1.64 0.02 1 999 . 103 LYS HE2 H 2.92 0.02 1 1000 . 103 LYS HE3 H 2.92 0.02 1 1001 . 103 LYS C C 174.32 0.20 1 1002 . 103 LYS CA C 55.19 0.20 1 1003 . 103 LYS CB C 36.30 0.20 1 1004 . 103 LYS CG C 24.94 0.20 1 1005 . 103 LYS CD C 28.98 0.20 1 1006 . 103 LYS CE C 42.10 0.20 1 1007 . 103 LYS N N 126.84 0.20 1 1008 . 104 LEU H H 8.44 0.02 1 1009 . 104 LEU HA H 5.36 0.02 1 1010 . 104 LEU HB2 H 2.07 0.02 2 1011 . 104 LEU HB3 H 1.26 0.02 2 1012 . 104 LEU HG H 1.95 0.02 1 1013 . 104 LEU HD1 H 0.90 0.02 2 1014 . 104 LEU HD2 H 1.09 0.02 2 1015 . 104 LEU C C 175.56 0.20 1 1016 . 104 LEU CA C 54.07 0.20 1 1017 . 104 LEU CB C 43.25 0.20 1 1018 . 104 LEU CG C 28.53 0.20 1 1019 . 104 LEU CD1 C 26.68 0.20 2 1020 . 104 LEU CD2 C 26.44 0.20 2 1021 . 104 LEU N N 123.69 0.20 1 1022 . 105 VAL H H 8.88 0.02 1 1023 . 105 VAL HA H 4.39 0.02 1 1024 . 105 VAL HB H 2.06 0.02 1 1025 . 105 VAL HG1 H 0.96 0.02 2 1026 . 105 VAL HG2 H 0.87 0.02 2 1027 . 105 VAL C C 175.05 0.20 1 1028 . 105 VAL CA C 60.01 0.20 1 1029 . 105 VAL CB C 35.23 0.20 1 1030 . 105 VAL CG1 C 21.11 0.20 2 1031 . 105 VAL CG2 C 20.67 0.20 2 1032 . 105 VAL N N 119.98 0.20 1 1033 . 106 ALA H H 8.74 0.02 1 1034 . 106 ALA HA H 4.44 0.02 1 1035 . 106 ALA HB H 1.42 0.02 1 1036 . 106 ALA C C 177.43 0.20 1 1037 . 106 ALA CA C 52.85 0.20 1 1038 . 106 ALA CB C 18.55 0.20 1 1039 . 106 ALA N N 127.71 0.20 1 1040 . 107 SER H H 8.16 0.02 1 1041 . 107 SER HA H 4.85 0.02 1 1042 . 107 SER HB2 H 4.18 0.02 2 1043 . 107 SER HB3 H 3.46 0.02 2 1044 . 107 SER CA C 54.54 0.20 1 1045 . 107 SER CB C 64.22 0.20 1 1046 . 107 SER N N 119.83 0.20 1 1047 . 108 PRO HD2 H 3.88 0.02 2 1048 . 108 PRO CD C 51.02 0.20 1 1049 . 109 SER HA H 4.48 0.02 1 1050 . 109 SER HB2 H 4.10 0.02 2 1051 . 109 SER HB3 H 3.75 0.02 2 1052 . 109 SER C C 174.88 0.20 1 1053 . 109 SER CA C 58.06 0.20 1 1054 . 109 SER CB C 63.40 0.20 1 1055 . 110 GLY H H 7.82 0.02 1 1056 . 110 GLY HA2 H 4.41 0.02 2 1057 . 110 GLY HA3 H 3.78 0.02 2 1058 . 110 GLY C C 174.08 0.20 1 1059 . 110 GLY CA C 45.34 0.20 1 1060 . 110 GLY N N 110.02 0.20 1 1061 . 111 GLY H H 7.35 0.02 1 1062 . 111 GLY HA2 H 3.90 0.02 2 1063 . 111 GLY HA3 H 3.77 0.02 2 1064 . 111 GLY C C 174.68 0.20 1 1065 . 111 GLY CA C 43.93 0.20 1 1066 . 111 GLY N N 108.32 0.20 1 1067 . 112 SER H H 8.71 0.02 1 1068 . 112 SER HA H 5.41 0.02 1 1069 . 112 SER HB2 H 3.34 0.02 1 1070 . 112 SER HB3 H 3.34 0.02 1 1071 . 112 SER HG H 5.72 0.02 1 1072 . 112 SER C C 173.39 0.20 1 1073 . 112 SER CA C 59.02 0.20 1 1074 . 112 SER CB C 67.29 0.20 1 1075 . 112 SER N N 119.15 0.20 1 1076 . 113 ILE H H 9.51 0.02 1 1077 . 113 ILE HA H 4.30 0.02 1 1078 . 113 ILE HB H 1.63 0.02 1 1079 . 113 ILE HG12 H 1.33 0.02 2 1080 . 113 ILE HG13 H 1.00 0.02 2 1081 . 113 ILE HG2 H 0.73 0.02 1 1082 . 113 ILE HD1 H 0.78 0.02 1 1083 . 113 ILE C C 174.81 0.20 1 1084 . 113 ILE CA C 61.18 0.20 1 1085 . 113 ILE CB C 39.00 0.20 1 1086 . 113 ILE CG1 C 27.67 0.20 1 1087 . 113 ILE CG2 C 17.64 0.20 1 1088 . 113 ILE CD1 C 13.30 0.20 1 1089 . 113 ILE N N 125.57 0.20 1 1090 . 114 ILE H H 9.05 0.02 1 1091 . 114 ILE HA H 4.36 0.02 1 1092 . 114 ILE HB H 1.17 0.02 1 1093 . 114 ILE HG12 H 1.02 0.02 2 1094 . 114 ILE HG13 H 0.45 0.02 2 1095 . 114 ILE HG2 H 0.38 0.02 1 1096 . 114 ILE HD1 H 0.06 0.02 1 1097 . 114 ILE C C 174.81 0.20 1 1098 . 114 ILE CA C 61.13 0.20 1 1099 . 114 ILE CB C 38.55 0.20 1 1100 . 114 ILE CG1 C 28.37 0.20 1 1101 . 114 ILE CG2 C 19.19 0.20 1 1102 . 114 ILE CD1 C 15.14 0.20 1 1103 . 114 ILE N N 127.95 0.20 1 1104 . 115 LYS H H 9.01 0.02 1 1105 . 115 LYS HA H 4.84 0.02 1 1106 . 115 LYS HB2 H 1.89 0.02 2 1107 . 115 LYS HB3 H 1.82 0.02 2 1108 . 115 LYS HG2 H 1.36 0.02 1 1109 . 115 LYS HG3 H 1.36 0.02 1 1110 . 115 LYS C C 175.88 0.20 1 1111 . 115 LYS CA C 55.19 0.20 1 1112 . 115 LYS CB C 33.15 0.20 1 1113 . 115 LYS CG C 24.99 0.20 1 1114 . 115 LYS N N 127.21 0.20 1 1115 . 116 SER H H 8.75 0.02 1 1116 . 116 SER HA H 5.55 0.02 1 1117 . 116 SER HB2 H 3.88 0.02 2 1118 . 116 SER HB3 H 3.66 0.02 2 1119 . 116 SER C C 173.79 0.20 1 1120 . 116 SER CA C 56.86 0.20 1 1121 . 116 SER CB C 64.95 0.20 1 1122 . 116 SER N N 121.02 0.20 1 1123 . 117 THR H H 9.41 0.02 1 1124 . 117 THR HA H 4.98 0.02 1 1125 . 117 THR HB H 3.86 0.02 1 1126 . 117 THR HG2 H 0.76 0.02 1 1127 . 117 THR C C 173.31 0.20 1 1128 . 117 THR CA C 62.08 0.20 1 1129 . 117 THR CB C 70.49 0.20 1 1130 . 117 THR CG2 C 22.65 0.20 1 1131 . 117 THR N N 126.20 0.20 1 1132 . 118 SER H H 8.94 0.02 1 1133 . 118 SER HA H 5.06 0.02 1 1134 . 118 SER HB2 H 3.52 0.02 1 1135 . 118 SER HB3 H 3.52 0.02 1 1136 . 118 SER C C 172.35 0.20 1 1137 . 118 SER CA C 55.95 0.20 1 1138 . 118 SER CB C 66.05 0.20 1 1139 . 118 SER N N 121.08 0.20 1 1140 . 119 HIS H H 9.28 0.02 1 1141 . 119 HIS HA H 5.27 0.02 1 1142 . 119 HIS HB2 H 3.15 0.02 2 1143 . 119 HIS HB3 H 2.42 0.02 2 1144 . 119 HIS HD2 H 6.62 0.02 1 1145 . 119 HIS HE1 H 7.67 0.02 1 1146 . 119 HIS C C 174.27 0.20 1 1147 . 119 HIS CA C 53.96 0.20 1 1148 . 119 HIS CB C 31.85 0.20 1 1149 . 119 HIS N N 122.33 0.20 1 1150 . 120 TYR H H 10.04 0.02 1 1151 . 120 TYR HA H 4.48 0.02 1 1152 . 120 TYR HB2 H 3.48 0.02 2 1153 . 120 TYR HB3 H 2.75 0.02 2 1154 . 120 TYR HD1 H 7.19 0.02 1 1155 . 120 TYR HD2 H 7.19 0.02 1 1156 . 120 TYR HE1 H 6.72 0.02 1 1157 . 120 TYR HE2 H 6.72 0.02 1 1158 . 120 TYR C C 174.74 0.20 1 1159 . 120 TYR CA C 58.18 0.20 1 1160 . 120 TYR CB C 39.32 0.20 1 1161 . 120 TYR N N 126.37 0.20 1 1162 . 121 HIS H H 8.22 0.02 1 1163 . 121 HIS HA H 5.14 0.02 1 1164 . 121 HIS HB2 H 3.26 0.02 2 1165 . 121 HIS HB3 H 3.17 0.02 2 1166 . 121 HIS HD2 H 6.82 0.02 1 1167 . 121 HIS HE1 H 7.52 0.02 1 1168 . 121 HIS C C 175.70 0.20 1 1169 . 121 HIS CA C 55.55 0.20 1 1170 . 121 HIS CB C 30.50 0.20 1 1171 . 121 HIS N N 123.98 0.20 1 1172 . 122 THR H H 8.79 0.02 1 1173 . 122 THR HA H 4.88 0.02 1 1174 . 122 THR HB H 4.52 0.02 1 1175 . 122 THR HG1 H 5.85 0.02 1 1176 . 122 THR HG2 H 1.32 0.02 1 1177 . 122 THR C C 174.54 0.20 1 1178 . 122 THR CA C 61.68 0.20 1 1179 . 122 THR CB C 70.66 0.20 1 1180 . 122 THR CG2 C 22.41 0.20 1 1181 . 122 THR N N 116.48 0.20 1 1182 . 123 LYS H H 8.31 0.02 1 1183 . 123 LYS HA H 4.55 0.02 1 1184 . 123 LYS HB2 H 1.81 0.02 2 1185 . 123 LYS HB3 H 1.51 0.02 2 1186 . 123 LYS C C 176.34 0.20 1 1187 . 123 LYS CA C 55.99 0.20 1 1188 . 123 LYS CB C 33.00 0.20 1 1189 . 123 LYS N N 121.00 0.20 1 1190 . 124 GLY H H 8.33 0.02 1 1191 . 124 GLY HA2 H 3.98 0.02 2 1192 . 124 GLY HA3 H 3.84 0.02 2 1193 . 124 GLY CA C 45.31 0.20 1 1194 . 124 GLY N N 109.79 0.20 1 1195 . 125 ASN H H 8.55 0.02 1 1196 . 125 ASN HA H 4.70 0.02 1 1197 . 125 ASN HB2 H 2.93 0.02 2 1198 . 125 ASN HB3 H 2.72 0.02 2 1199 . 125 ASN HD21 H 7.51 0.02 2 1200 . 125 ASN HD22 H 6.80 0.02 2 1201 . 125 ASN C C 174.62 0.20 1 1202 . 125 ASN CA C 53.29 0.20 1 1203 . 125 ASN CB C 37.77 0.20 1 1204 . 125 ASN N N 118.69 0.20 1 1205 . 125 ASN ND2 N 112.06 0.20 1 1206 . 126 VAL H H 7.59 0.02 1 1207 . 126 VAL HA H 4.32 0.02 1 1208 . 126 VAL HB H 2.09 0.02 1 1209 . 126 VAL HG1 H 0.94 0.02 1 1210 . 126 VAL HG2 H 0.94 0.02 1 1211 . 126 VAL C C 174.77 0.20 1 1212 . 126 VAL CA C 60.94 0.20 1 1213 . 126 VAL CB C 34.36 0.20 1 1214 . 126 VAL CG1 C 19.94 0.20 2 1215 . 126 VAL CG2 C 21.42 0.20 2 1216 . 126 VAL N N 118.29 0.20 1 1217 . 127 GLU H H 8.24 0.02 1 1218 . 127 GLU HA H 4.12 0.02 1 1219 . 127 GLU HB2 H 1.85 0.02 2 1220 . 127 GLU HB3 H 1.79 0.02 2 1221 . 127 GLU HG2 H 2.10 0.02 1 1222 . 127 GLU HG3 H 2.10 0.02 1 1223 . 127 GLU C C 175.74 0.20 1 1224 . 127 GLU CA C 55.59 0.20 1 1225 . 127 GLU CB C 30.76 0.20 1 1226 . 127 GLU CG C 36.08 0.20 1 1227 . 127 GLU N N 123.37 0.20 1 1228 . 128 ILE H H 7.24 0.02 1 1229 . 128 ILE HA H 3.97 0.02 1 1230 . 128 ILE HB H 1.30 0.02 1 1231 . 128 ILE HG12 H 1.02 0.02 2 1232 . 128 ILE HG13 H 0.92 0.02 2 1233 . 128 ILE HG2 H 0.33 0.02 1 1234 . 128 ILE HD1 H 0.51 0.02 1 1235 . 128 ILE C C 175.45 0.20 1 1236 . 128 ILE CA C 59.12 0.20 1 1237 . 128 ILE CB C 37.54 0.20 1 1238 . 128 ILE CG1 C 27.30 0.20 1 1239 . 128 ILE CG2 C 17.13 0.20 1 1240 . 128 ILE CD1 C 12.31 0.20 1 1241 . 128 ILE N N 123.56 0.20 1 1242 . 129 LYS H H 8.67 0.02 1 1243 . 129 LYS HA H 4.25 0.02 1 1244 . 129 LYS HB2 H 1.80 0.02 2 1245 . 129 LYS HB3 H 1.43 0.02 2 1246 . 129 LYS HG2 H 1.54 0.02 1 1247 . 129 LYS HG3 H 1.54 0.02 1 1248 . 129 LYS C C 177.46 0.20 1 1249 . 129 LYS CA C 55.55 0.20 1 1250 . 129 LYS CB C 32.79 0.20 1 1251 . 129 LYS CG C 25.00 0.20 1 1252 . 129 LYS N N 127.33 0.20 1 1253 . 130 GLU H H 8.79 0.02 1 1254 . 130 GLU HA H 3.69 0.02 1 1255 . 130 GLU HB2 H 2.02 0.02 2 1256 . 130 GLU HB3 H 1.92 0.02 2 1257 . 130 GLU HG2 H 2.21 0.02 1 1258 . 130 GLU HG3 H 2.21 0.02 1 1259 . 130 GLU C C 178.42 0.20 1 1260 . 130 GLU CA C 59.60 0.20 1 1261 . 130 GLU CB C 29.29 0.20 1 1262 . 130 GLU CG C 36.24 0.20 1 1263 . 130 GLU N N 125.33 0.20 1 1264 . 131 GLU H H 9.16 0.02 1 1265 . 131 GLU HA H 3.93 0.02 1 1266 . 131 GLU HB2 H 1.89 0.02 1 1267 . 131 GLU HB3 H 1.89 0.02 1 1268 . 131 GLU HG2 H 2.08 0.02 1 1269 . 131 GLU HG3 H 2.08 0.02 1 1270 . 131 GLU C C 178.53 0.20 1 1271 . 131 GLU CA C 59.44 0.20 1 1272 . 131 GLU CB C 28.88 0.20 1 1273 . 131 GLU CG C 35.94 0.20 1 1274 . 131 GLU N N 117.27 0.20 1 1275 . 132 HIS H H 7.43 0.02 1 1276 . 132 HIS HA H 4.40 0.02 1 1277 . 132 HIS HB2 H 3.16 0.02 1 1278 . 132 HIS HB3 H 3.16 0.02 1 1279 . 132 HIS HD2 H 6.93 0.02 1 1280 . 132 HIS HE1 H 7.64 0.02 1 1281 . 132 HIS C C 178.25 0.20 1 1282 . 132 HIS CA C 58.61 0.20 1 1283 . 132 HIS CB C 31.36 0.20 1 1284 . 132 HIS N N 119.63 0.20 1 1285 . 133 VAL H H 7.15 0.02 1 1286 . 133 VAL HA H 3.63 0.02 1 1287 . 133 VAL HB H 1.78 0.02 1 1288 . 133 VAL HG1 H 0.16 0.02 2 1289 . 133 VAL HG2 H 0.30 0.02 2 1290 . 133 VAL C C 178.91 0.20 1 1291 . 133 VAL CA C 64.86 0.20 1 1292 . 133 VAL CB C 31.63 0.20 1 1293 . 133 VAL CG1 C 20.53 0.20 2 1294 . 133 VAL CG2 C 20.45 0.20 2 1295 . 133 VAL N N 119.89 0.20 1 1296 . 134 LYS H H 8.14 0.02 1 1297 . 134 LYS HA H 3.87 0.02 1 1298 . 134 LYS HB2 H 1.80 0.02 1 1299 . 134 LYS HB3 H 1.80 0.02 1 1300 . 134 LYS HG2 H 1.40 0.02 1 1301 . 134 LYS HG3 H 1.40 0.02 1 1302 . 134 LYS HD2 H 1.64 0.02 1 1303 . 134 LYS HD3 H 1.64 0.02 1 1304 . 134 LYS HE2 H 2.93 0.02 1 1305 . 134 LYS HE3 H 2.93 0.02 1 1306 . 134 LYS C C 178.47 0.20 1 1307 . 134 LYS CA C 59.71 0.20 1 1308 . 134 LYS CB C 32.49 0.20 1 1309 . 134 LYS CG C 24.99 0.20 1 1310 . 134 LYS CD C 29.10 0.20 1 1311 . 134 LYS CE C 41.86 0.20 1 1312 . 134 LYS N N 120.99 0.20 1 1313 . 135 ALA H H 7.91 0.02 1 1314 . 135 ALA HA H 4.19 0.02 1 1315 . 135 ALA HB H 1.46 0.02 1 1316 . 135 ALA C C 180.75 0.20 1 1317 . 135 ALA CA C 54.97 0.20 1 1318 . 135 ALA CB C 18.04 0.20 1 1319 . 135 ALA N N 121.41 0.20 1 1320 . 136 GLY H H 7.92 0.02 1 1321 . 136 GLY HA2 H 3.99 0.02 2 1322 . 136 GLY HA3 H 3.84 0.02 2 1323 . 136 GLY C C 176.76 0.20 1 1324 . 136 GLY CA C 47.08 0.20 1 1325 . 136 GLY N N 106.00 0.20 1 1326 . 137 LYS H H 7.92 0.02 1 1327 . 137 LYS HA H 4.28 0.02 1 1328 . 137 LYS HB2 H 2.00 0.02 1 1329 . 137 LYS HB3 H 2.00 0.02 1 1330 . 137 LYS HG2 H 1.62 0.02 2 1331 . 137 LYS HG3 H 1.52 0.02 2 1332 . 137 LYS C C 178.80 0.20 1 1333 . 137 LYS CA C 59.61 0.20 1 1334 . 137 LYS CB C 32.60 0.20 1 1335 . 137 LYS CG C 25.10 0.20 1 1336 . 137 LYS N N 124.02 0.20 1 1337 . 138 GLU H H 8.23 0.02 1 1338 . 138 GLU HA H 4.06 0.02 1 1339 . 138 GLU HB2 H 2.06 0.02 1 1340 . 138 GLU HB3 H 2.06 0.02 1 1341 . 138 GLU HG2 H 2.35 0.02 2 1342 . 138 GLU HG3 H 2.24 0.02 2 1343 . 138 GLU C C 178.82 0.20 1 1344 . 138 GLU CA C 59.18 0.20 1 1345 . 138 GLU CB C 29.42 0.20 1 1346 . 138 GLU CG C 36.27 0.20 1 1347 . 138 GLU N N 120.57 0.20 1 1348 . 139 LYS H H 7.99 0.02 1 1349 . 139 LYS HA H 4.00 0.02 1 1350 . 139 LYS HB2 H 1.81 0.02 1 1351 . 139 LYS HB3 H 1.81 0.02 1 1352 . 139 LYS HG2 H 1.53 0.02 2 1353 . 139 LYS HG3 H 1.40 0.02 2 1354 . 139 LYS C C 179.32 0.20 1 1355 . 139 LYS CA C 59.41 0.20 1 1356 . 139 LYS CB C 32.34 0.20 1 1357 . 139 LYS CG C 25.80 0.20 1 1358 . 139 LYS N N 119.36 0.20 1 1359 . 140 ALA H H 7.69 0.02 1 1360 . 140 ALA HA H 3.96 0.02 1 1361 . 140 ALA HB H 1.42 0.02 1 1362 . 140 ALA C C 179.21 0.20 1 1363 . 140 ALA CA C 54.89 0.20 1 1364 . 140 ALA CB C 18.23 0.20 1 1365 . 140 ALA N N 121.90 0.20 1 1366 . 141 SER H H 8.28 0.02 1 1367 . 141 SER HA H 3.78 0.02 1 1368 . 141 SER HB2 H 3.90 0.02 1 1369 . 141 SER HB3 H 3.90 0.02 1 1370 . 141 SER C C 177.12 0.20 1 1371 . 141 SER CA C 61.24 0.20 1 1372 . 141 SER CB C 62.81 0.20 1 1373 . 141 SER N N 113.37 0.20 1 1374 . 142 ASN H H 8.21 0.02 1 1375 . 142 ASN HA H 4.39 0.02 1 1376 . 142 ASN HB2 H 2.88 0.02 2 1377 . 142 ASN HB3 H 2.71 0.02 2 1378 . 142 ASN HD21 H 7.58 0.02 2 1379 . 142 ASN HD22 H 6.95 0.02 2 1380 . 142 ASN C C 177.37 0.20 1 1381 . 142 ASN CA C 56.16 0.20 1 1382 . 142 ASN CB C 38.52 0.20 1 1383 . 142 ASN N N 119.06 0.20 1 1384 . 142 ASN ND2 N 112.47 0.20 1 1385 . 143 LEU H H 7.68 0.02 1 1386 . 143 LEU HA H 4.01 0.02 1 1387 . 143 LEU HB2 H 1.63 0.02 2 1388 . 143 LEU HB3 H 1.53 0.02 2 1389 . 143 LEU HG H 1.42 0.02 1 1390 . 143 LEU HD1 H 0.74 0.02 2 1391 . 143 LEU HD2 H 0.80 0.02 2 1392 . 143 LEU C C 178.56 0.20 1 1393 . 143 LEU CA C 58.04 0.20 1 1394 . 143 LEU CB C 41.02 0.20 1 1395 . 143 LEU CG C 26.98 0.20 1 1396 . 143 LEU CD1 C 24.94 0.20 2 1397 . 143 LEU CD2 C 23.70 0.20 2 1398 . 143 LEU N N 121.07 0.20 1 1399 . 144 PHE H H 8.00 0.02 1 1400 . 144 PHE HA H 3.93 0.02 1 1401 . 144 PHE HB2 H 2.93 0.02 2 1402 . 144 PHE HB3 H 2.76 0.02 2 1403 . 144 PHE HD1 H 6.54 0.02 1 1404 . 144 PHE HD2 H 6.54 0.02 1 1405 . 144 PHE HE1 H 6.50 0.02 1 1406 . 144 PHE HE2 H 6.50 0.02 1 1407 . 144 PHE C C 178.18 0.20 1 1408 . 144 PHE CA C 62.29 0.20 1 1409 . 144 PHE CB C 37.58 0.20 1 1410 . 144 PHE N N 117.23 0.20 1 1411 . 145 LYS H H 8.10 0.02 1 1412 . 145 LYS HA H 4.06 0.02 1 1413 . 145 LYS HB2 H 1.98 0.02 1 1414 . 145 LYS HB3 H 1.98 0.02 1 1415 . 145 LYS C C 179.36 0.20 1 1416 . 145 LYS CA C 59.31 0.20 1 1417 . 145 LYS CB C 31.79 0.20 1 1418 . 145 LYS CG C 24.96 0.20 1 1419 . 145 LYS N N 120.05 0.20 1 1420 . 146 LEU H H 7.97 0.02 1 1421 . 146 LEU HA H 4.11 0.02 1 1422 . 146 LEU HB2 H 1.99 0.02 2 1423 . 146 LEU HB3 H 1.43 0.02 2 1424 . 146 LEU HG H 1.86 0.02 1 1425 . 146 LEU HD1 H 0.88 0.02 1 1426 . 146 LEU HD2 H 0.88 0.02 1 1427 . 146 LEU C C 180.44 0.20 1 1428 . 146 LEU CA C 58.17 0.20 1 1429 . 146 LEU CB C 42.32 0.20 1 1430 . 146 LEU CG C 26.68 0.20 1 1431 . 146 LEU CD1 C 25.49 0.20 2 1432 . 146 LEU CD2 C 23.46 0.20 2 1433 . 146 LEU N N 121.29 0.20 1 1434 . 147 ILE H H 8.18 0.02 1 1435 . 147 ILE HA H 3.51 0.02 1 1436 . 147 ILE HB H 1.85 0.02 1 1437 . 147 ILE HG12 H 1.72 0.02 2 1438 . 147 ILE HG13 H 0.82 0.02 2 1439 . 147 ILE HG2 H 0.71 0.02 1 1440 . 147 ILE HD1 H 0.64 0.02 1 1441 . 147 ILE C C 177.13 0.20 1 1442 . 147 ILE CA C 65.48 0.20 1 1443 . 147 ILE CB C 37.76 0.20 1 1444 . 147 ILE CG1 C 29.52 0.20 1 1445 . 147 ILE CG2 C 17.39 0.20 1 1446 . 147 ILE CD1 C 13.51 0.20 1 1447 . 147 ILE N N 120.97 0.20 1 1448 . 148 GLU H H 8.69 0.02 1 1449 . 148 GLU HA H 3.69 0.02 1 1450 . 148 GLU HB2 H 2.08 0.02 1 1451 . 148 GLU HB3 H 2.08 0.02 1 1452 . 148 GLU HG2 H 2.12 0.02 1 1453 . 148 GLU HG3 H 2.12 0.02 1 1454 . 148 GLU C C 178.08 0.20 1 1455 . 148 GLU CA C 60.45 0.20 1 1456 . 148 GLU CB C 30.16 0.20 1 1457 . 148 GLU CG C 37.14 0.20 1 1458 . 148 GLU N N 121.84 0.20 1 1459 . 149 THR H H 8.42 0.02 1 1460 . 149 THR HA H 3.82 0.02 1 1461 . 149 THR HB H 4.32 0.02 1 1462 . 149 THR HG2 H 1.29 0.02 1 1463 . 149 THR C C 177.13 0.20 1 1464 . 149 THR CA C 67.07 0.20 1 1465 . 149 THR CB C 68.79 0.20 1 1466 . 149 THR CG2 C 21.70 0.20 1 1467 . 149 THR N N 115.26 0.20 1 1468 . 150 TYR H H 7.96 0.02 1 1469 . 150 TYR HA H 4.31 0.02 1 1470 . 150 TYR HB2 H 3.15 0.02 1 1471 . 150 TYR HB3 H 3.15 0.02 1 1472 . 150 TYR HD1 H 6.90 0.02 1 1473 . 150 TYR HD2 H 6.90 0.02 1 1474 . 150 TYR HE1 H 6.35 0.02 1 1475 . 150 TYR HE2 H 6.35 0.02 1 1476 . 150 TYR C C 178.78 0.20 1 1477 . 150 TYR CA C 62.37 0.20 1 1478 . 150 TYR CB C 38.41 0.20 1 1479 . 150 TYR N N 123.60 0.20 1 1480 . 151 LEU H H 8.81 0.02 1 1481 . 151 LEU HA H 3.96 0.02 1 1482 . 151 LEU HB2 H 1.95 0.02 2 1483 . 151 LEU HB3 H 1.35 0.02 2 1484 . 151 LEU HG H 2.10 0.02 1 1485 . 151 LEU HD1 H 0.76 0.02 2 1486 . 151 LEU HD2 H 0.98 0.02 2 1487 . 151 LEU C C 180.26 0.20 1 1488 . 151 LEU CA C 57.84 0.20 1 1489 . 151 LEU CB C 41.05 0.20 1 1490 . 151 LEU CG C 26.94 0.20 1 1491 . 151 LEU CD1 C 27.61 0.20 2 1492 . 151 LEU CD2 C 22.95 0.20 2 1493 . 151 LEU N N 120.40 0.20 1 1494 . 152 LYS H H 8.55 0.02 1 1495 . 152 LYS HA H 4.03 0.02 1 1496 . 152 LYS HB2 H 1.99 0.02 2 1497 . 152 LYS HB3 H 1.82 0.02 2 1498 . 152 LYS HG2 H 1.40 0.02 1 1499 . 152 LYS HG3 H 1.40 0.02 1 1500 . 152 LYS C C 178.42 0.20 1 1501 . 152 LYS CA C 59.33 0.20 1 1502 . 152 LYS CB C 32.15 0.20 1 1503 . 152 LYS CG C 25.45 0.20 1 1504 . 152 LYS CD C 29.56 0.20 1 1505 . 152 LYS N N 119.90 0.20 1 1506 . 153 GLY H H 7.51 0.02 1 1507 . 153 GLY HA2 H 4.01 0.02 2 1508 . 153 GLY HA3 H 3.60 0.02 2 1509 . 153 GLY C C 172.97 0.20 1 1510 . 153 GLY CA C 44.92 0.20 1 1511 . 153 GLY N N 103.74 0.20 1 1512 . 154 HIS H H 7.18 0.02 1 1513 . 154 HIS HA H 4.81 0.02 1 1514 . 154 HIS HB2 H 2.89 0.02 2 1515 . 154 HIS HB3 H 2.44 0.02 2 1516 . 154 HIS HD2 H 6.78 0.02 1 1517 . 154 HIS HE1 H 7.85 0.02 1 1518 . 154 HIS CA C 54.10 0.20 1 1519 . 154 HIS CB C 27.98 0.20 1 1520 . 154 HIS N N 117.57 0.20 1 1521 . 155 PRO HA H 4.35 0.02 1 1522 . 155 PRO HB2 H 2.31 0.02 2 1523 . 155 PRO HB3 H 1.94 0.02 2 1524 . 155 PRO HG2 H 1.90 0.02 1 1525 . 155 PRO HG3 H 1.90 0.02 1 1526 . 155 PRO HD2 H 3.56 0.02 2 1527 . 155 PRO HD3 H 3.25 0.02 2 1528 . 155 PRO C C 176.13 0.20 1 1529 . 155 PRO CA C 64.70 0.20 1 1530 . 155 PRO CB C 32.11 0.20 1 1531 . 155 PRO CG C 26.87 0.20 1 1532 . 155 PRO CD C 50.41 0.20 1 1533 . 156 ASP H H 8.51 0.02 1 1534 . 156 ASP HA H 4.53 0.02 1 1535 . 156 ASP HB2 H 2.64 0.02 2 1536 . 156 ASP HB3 H 2.56 0.02 2 1537 . 156 ASP C C 176.35 0.20 1 1538 . 156 ASP CA C 53.96 0.20 1 1539 . 156 ASP CB C 40.61 0.20 1 1540 . 156 ASP N N 114.51 0.20 1 1541 . 157 ALA H H 7.72 0.02 1 1542 . 157 ALA HA H 4.15 0.02 1 1543 . 157 ALA HB H 1.39 0.02 1 1544 . 157 ALA C C 177.70 0.20 1 1545 . 157 ALA CA C 52.48 0.20 1 1546 . 157 ALA CB C 19.79 0.20 1 1547 . 157 ALA N N 124.26 0.20 1 1548 . 158 TYR H H 8.67 0.02 1 1549 . 158 TYR HA H 4.06 0.02 1 1550 . 158 TYR HB2 H 3.30 0.02 2 1551 . 158 TYR HB3 H 3.02 0.02 2 1552 . 158 TYR HD1 H 6.89 0.02 1 1553 . 158 TYR HD2 H 6.89 0.02 1 1554 . 158 TYR HE1 H 6.75 0.02 1 1555 . 158 TYR HE2 H 6.75 0.02 1 1556 . 158 TYR C C 173.44 0.20 1 1557 . 158 TYR CA C 60.08 0.20 1 1558 . 158 TYR CB C 35.16 0.20 1 1559 . 158 TYR N N 117.87 0.20 1 1560 . 159 ASN H H 7.61 0.02 1 1561 . 159 ASN HA H 4.60 0.02 1 1562 . 159 ASN HB2 H 2.77 0.02 2 1563 . 159 ASN HB3 H 2.50 0.02 2 1564 . 159 ASN HD21 H 7.20 0.02 2 1565 . 159 ASN HD22 H 6.80 0.02 2 1566 . 159 ASN CA C 54.35 0.20 1 1567 . 159 ASN CB C 40.66 0.20 1 1568 . 159 ASN N N 121.61 0.20 1 1569 . 159 ASN ND2 N 112.06 0.20 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details ; Coupling constants of residues other than W45, G46, D47, G48, G51, T52, and I53 are identical to those of wild-type Pru av 1. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'Pru av 1 E45W' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 VAL H 2 VAL HA 9.6 . . 1.0 2 3JHNHA 5 TYR H 5 TYR HA 9.5 . . 1.0 3 3JHNHA 6 GLU H 6 GLU HA 9.1 . . 1.0 4 3JHNHA 7 SER H 7 SER HA 8.6 . . 1.0 5 3JHNHA 8 GLU H 8 GLU HA 8.1 . . 1.0 6 3JHNHA 9 PHE H 9 PHE HA 9.0 . . 1.0 7 3JHNHA 10 THR H 10 THR HA 8.9 . . 1.0 8 3JHNHA 11 SER H 11 SER HA 9.4 . . 1.0 9 3JHNHA 12 GLU H 12 GLU HA 6.8 . . 1.0 10 3JHNHA 13 ILE H 13 ILE HA 6.6 . . 1.0 11 3JHNHA 17 ARG H 17 ARG HA 6.3 . . 1.0 12 3JHNHA 18 LEU H 18 LEU HA 4.4 . . 1.0 13 3JHNHA 19 PHE H 19 PHE HA 4.0 . . 1.0 14 3JHNHA 20 LYS H 20 LYS HA 4.2 . . 1.0 15 3JHNHA 21 ALA H 21 ALA HA 5.9 . . 1.0 16 3JHNHA 22 PHE H 22 PHE HA 6.2 . . 1.0 17 3JHNHA 23 VAL H 23 VAL HA 10.2 . . 1.0 18 3JHNHA 24 LEU H 24 LEU HA 4.8 . . 1.0 19 3JHNHA 27 ASP H 27 ASP HA 4.2 . . 1.0 20 3JHNHA 28 ASN H 28 ASN HA 6.7 . . 1.0 21 3JHNHA 33 ILE H 33 ILE HA 5.7 . . 1.0 22 3JHNHA 36 GLN H 36 GLN HA 6.1 . . 1.0 23 3JHNHA 37 ALA H 37 ALA HA 9.1 . . 1.0 24 3JHNHA 40 HIS H 40 HIS HA 7.0 . . 1.0 25 3JHNHA 41 SER H 41 SER HA 9.1 . . 1.0 26 3JHNHA 42 GLU H 42 GLU HA 9.5 . . 1.0 27 3JHNHA 43 ILE H 43 ILE HA 7.3 . . 1.0 28 3JHNHA 44 LEU H 44 LEU HA 9.2 . . 1.0 29 3JHNHA 47 ASP H 47 ASP HA 9.7 . . 1.0 30 3JHNHA 52 THR H 52 THR HA 3.7 . . 1.0 31 3JHNHA 53 ILE H 53 ILE HA 9.7 . . 1.0 32 3JHNHA 54 LYS H 54 LYS HA 9.2 . . 1.0 33 3JHNHA 55 LYS H 55 LYS HA 8.4 . . 1.0 34 3JHNHA 56 ILE H 56 ILE HA 9.6 . . 1.0 35 3JHNHA 58 PHE H 58 PHE HA 7.6 . . 1.0 36 3JHNHA 60 GLU H 60 GLU HA 6.8 . . 1.0 37 3JHNHA 64 TYR H 64 TYR HA 7.3 . . 1.0 38 3JHNHA 66 TYR H 66 TYR HA 7.4 . . 1.0 39 3JHNHA 67 VAL H 67 VAL HA 8.3 . . 1.0 40 3JHNHA 68 LYS H 68 LYS HA 9.4 . . 1.0 41 3JHNHA 69 HIS H 69 HIS HA 9.2 . . 1.0 42 3JHNHA 70 LYS H 70 LYS HA 9.4 . . 1.0 43 3JHNHA 71 ILE H 71 ILE HA 5.8 . . 1.0 44 3JHNHA 72 ASP H 72 ASP HA 9.6 . . 1.0 45 3JHNHA 73 SER H 73 SER HA 7.1 . . 1.0 46 3JHNHA 76 LYS H 76 LYS HA 5.8 . . 1.0 47 3JHNHA 78 ASN H 78 ASN HA 9.8 . . 1.0 48 3JHNHA 79 TYR H 79 TYR HA 7.0 . . 1.0 49 3JHNHA 80 SER H 80 SER HA 9.1 . . 1.0 50 3JHNHA 81 TYR H 81 TYR HA 8.1 . . 1.0 51 3JHNHA 84 THR H 84 THR HA 9.8 . . 1.0 52 3JHNHA 85 LEU H 85 LEU HA 7.3 . . 1.0 53 3JHNHA 87 GLU H 87 GLU HA 6.4 . . 1.0 54 3JHNHA 89 ASP H 89 ASP HA 3.8 . . 1.0 55 3JHNHA 91 LEU H 91 LEU HA 6.4 . . 1.0 56 3JHNHA 94 THR H 94 THR HA 10.1 . . 1.0 57 3JHNHA 95 LEU H 95 LEU HA 8.2 . . 1.0 58 3JHNHA 96 GLU H 96 GLU HA 8.2 . . 1.0 59 3JHNHA 97 LYS H 97 LYS HA 4.7 . . 1.0 60 3JHNHA 98 ILE H 98 ILE HA 9.5 . . 1.0 61 3JHNHA 99 SER H 99 SER HA 8.9 . . 1.0 62 3JHNHA 100 TYR H 100 TYR HA 8.7 . . 1.0 63 3JHNHA 101 GLU H 101 GLU HA 9.4 . . 1.0 64 3JHNHA 103 LYS H 103 LYS HA 8.8 . . 1.0 65 3JHNHA 104 LEU H 104 LEU HA 9.4 . . 1.0 66 3JHNHA 105 VAL H 105 VAL HA 9.5 . . 1.0 67 3JHNHA 107 SER H 107 SER HA 8.1 . . 1.0 68 3JHNHA 112 SER H 112 SER HA 8.9 . . 1.0 69 3JHNHA 113 ILE H 113 ILE HA 9.1 . . 1.0 70 3JHNHA 115 LYS H 115 LYS HA 9.0 . . 1.0 71 3JHNHA 116 SER H 116 SER HA 9.3 . . 1.0 72 3JHNHA 117 THR H 117 THR HA 9.8 . . 1.0 73 3JHNHA 118 SER H 118 SER HA 9.6 . . 1.0 74 3JHNHA 119 HIS H 119 HIS HA 8.4 . . 1.0 75 3JHNHA 122 THR H 122 THR HA 7.6 . . 1.0 76 3JHNHA 123 LYS H 123 LYS HA 7.4 . . 1.0 77 3JHNHA 127 GLU H 127 GLU HA 6.7 . . 1.0 78 3JHNHA 129 LYS H 129 LYS HA 7.4 . . 1.0 79 3JHNHA 132 HIS H 132 HIS HA 6.8 . . 1.0 80 3JHNHA 133 VAL H 133 VAL HA 7.6 . . 1.0 81 3JHNHA 137 LYS H 137 LYS HA 4.6 . . 1.0 82 3JHNHA 139 LYS H 139 LYS HA 4.8 . . 1.0 83 3JHNHA 141 SER H 141 SER HA 4.0 . . 1.0 84 3JHNHA 142 ASN H 142 ASN HA 4.3 . . 1.0 85 3JHNHA 144 PHE H 144 PHE HA 4.3 . . 1.0 86 3JHNHA 145 LYS H 145 LYS HA 4.2 . . 1.0 87 3JHNHA 148 GLU H 148 GLU HA 3.6 . . 1.0 88 3JHNHA 149 THR H 149 THR HA 3.8 . . 1.0 89 3JHNHA 150 TYR H 150 TYR HA 4.4 . . 1.0 90 3JHNHA 151 LEU H 151 LEU HA 4.7 . . 1.0 91 3JHNHA 152 LYS H 152 LYS HA 4.4 . . 1.0 92 3JHNHA 154 HIS H 154 HIS HA 10.2 . . 1.0 93 3JHNHA 156 ASP H 156 ASP HA 8.4 . . 1.0 94 3JHNHA 157 ALA H 157 ALA HA 6.3 . . 1.0 95 3JHNHA 158 TYR H 158 TYR HA 6.8 . . 1.0 96 3JHNHA 159 ASN H 159 ASN HA 9.3 . . 1.0 stop_ save_