data_4158 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Nuclear Magnetic Resonance Chemical Shifts of the Cytotoxic Ribonuclease Alpha-sarcin ; _BMRB_accession_number 4158 _BMRB_flat_file_name bmr4158.str _Entry_type original _Submission_date 1998-07-03 _Accession_date 1998-07-03 _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 Rico Manuel . . 2 Bruix Marta . . 3 Santoro Jorge . . 4 Campos-Olivas Ramon . . 5 Perez-Canadillas Jose M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 814 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-08 original author . stop_ _Original_release_date 2000-03-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H and 15N Nuclear Magnetic Resonance Assignment and Secondary Structure of the Cytotoxic Ribonuclease Alpha-sarcin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96303820 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Campos-Olivas Ramon . . 2 Bruix Marta . . 3 Santoro Jorge . . 4 'Martinez del Pozo' Alvaro . . 5 Lacadena Javier . . 6 Gavilanes Jose . . 7 Rico Manuel . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 5 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 969 _Page_last 972 _Year 1996 _Details . loop_ _Keyword 'alpha Sarcin' 'nuclear magnetic resonance' 'protein structure' ribonuclease 'ribosome-inactivating protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR 6, 135-140 (1995) ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ save_citation_two _Saveframe_category citation _Citation_full . _Citation_title ; Campos-Olivas, R., "Estructura y Dinamica de Proteinas por Resonancia Magnetica Nuclear: Proteina Antifungica y Alpha Sarcina," Thesis, 85-142, Universidad Complutense de Madrid (1997) ; _Citation_status . _Citation_type . _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_ ################################## # Molecular system description # ################################## save_system_alpha_sar _Saveframe_category molecular_system _Mol_system_name 'Ribonuclease alpha-sarcin' _Abbreviation_common alpha_sarcin _Enzyme_commission_number 3.1.27.10 loop_ _Mol_system_component_name _Mol_label 'alpha sarcin' $alpha_sar stop_ _System_molecular_weight 16981 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'Cytotoxic endoribonuclease' 'Ribosome Inactivating Protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_alpha_sar _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ribonuclease alpha-sarcin' _Abbreviation_common alpha_sar _Molecular_mass 16981 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 150 _Mol_residue_sequence ; AVTWTCLNDQKNPKTNKYET KRLLYNQNKAESNSHHAPLS DGKTGSSYPHWFTNGYDGDG KLPKGRTPIKFGKSDCDRPP KHSKDGNGKTDHYLLEFPTF PDGHDYKFDSKKPKENPGPA RVIYTYPNKVFCGIIAHTKE NQGELKLCSH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 VAL 3 THR 4 TRP 5 THR 6 CYS 7 LEU 8 ASN 9 ASP 10 GLN 11 LYS 12 ASN 13 PRO 14 LYS 15 THR 16 ASN 17 LYS 18 TYR 19 GLU 20 THR 21 LYS 22 ARG 23 LEU 24 LEU 25 TYR 26 ASN 27 GLN 28 ASN 29 LYS 30 ALA 31 GLU 32 SER 33 ASN 34 SER 35 HIS 36 HIS 37 ALA 38 PRO 39 LEU 40 SER 41 ASP 42 GLY 43 LYS 44 THR 45 GLY 46 SER 47 SER 48 TYR 49 PRO 50 HIS 51 TRP 52 PHE 53 THR 54 ASN 55 GLY 56 TYR 57 ASP 58 GLY 59 ASP 60 GLY 61 LYS 62 LEU 63 PRO 64 LYS 65 GLY 66 ARG 67 THR 68 PRO 69 ILE 70 LYS 71 PHE 72 GLY 73 LYS 74 SER 75 ASP 76 CYS 77 ASP 78 ARG 79 PRO 80 PRO 81 LYS 82 HIS 83 SER 84 LYS 85 ASP 86 GLY 87 ASN 88 GLY 89 LYS 90 THR 91 ASP 92 HIS 93 TYR 94 LEU 95 LEU 96 GLU 97 PHE 98 PRO 99 THR 100 PHE 101 PRO 102 ASP 103 GLY 104 HIS 105 ASP 106 TYR 107 LYS 108 PHE 109 ASP 110 SER 111 LYS 112 LYS 113 PRO 114 LYS 115 GLU 116 ASN 117 PRO 118 GLY 119 PRO 120 ALA 121 ARG 122 VAL 123 ILE 124 TYR 125 THR 126 TYR 127 PRO 128 ASN 129 LYS 130 VAL 131 PHE 132 CYS 133 GLY 134 ILE 135 ILE 136 ALA 137 HIS 138 THR 139 LYS 140 GLU 141 ASN 142 GLN 143 GLY 144 GLU 145 LEU 146 LYS 147 LEU 148 CYS 149 SER 150 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 PDB 1DE3 "Solution Structure Of The Cytotoxic Ribonuclease Alpha- Sarcin" 99.33 150 100.00 100.00 1.29e-104 DBJ BAA02863 "alpha sarcin precursor [Aspergillus giganteus]" 100.00 177 100.00 100.00 1.46e-106 EMBL CAA37471 "alpha-sarcin [synthetic construct]" 100.00 150 100.00 100.00 1.99e-105 EMBL CAA43180 "alpha-sarcin [Aspergillus giganteus]" 100.00 177 100.00 100.00 1.46e-106 GB AAB66603 "a-sarcin precursor [Penicillium daleae]" 100.00 177 98.00 100.00 6.92e-105 GB AAB66605 "a-sarcin precursor [Talaromyces aculeatus]" 100.00 177 98.00 100.00 6.92e-105 GB ACA34736 "ribotoxin, partial [Aspergillus clavatonanicus]" 94.00 144 100.00 100.00 2.90e-98 SP P00655 "RecName: Full=Ribonuclease alpha-sarcin; AltName: Full=rRNA endonuclease; Flags: Precursor" 100.00 177 100.00 100.00 1.46e-106 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Cell_type _Secretion $alpha_sar 'Aspergillus giganteus' 5060 Eukaryota Fungi Aspergillus giganteus 'MDH 18894' mycelia extracellular stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $alpha_sar 'recombinant technology' 'E. coli' Escherichia coli RB791 plasmid pINPGaS cDNA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $alpha_sar 1.5 mM [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.1 n/a temperature 306 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Correction_value _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0 internal direct . . . . . TSP N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 $citation_one 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'alpha sarcin' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 4.30 0.01 1 2 . 1 ALA HB H 1.57 0.01 1 3 . 2 VAL H H 8.76 0.01 1 4 . 2 VAL HA H 4.16 0.01 1 5 . 2 VAL HB H 2.08 0.01 1 6 . 2 VAL HG1 H 0.91 0.01 1 7 . 2 VAL HG2 H 1.06 0.01 1 8 . 2 VAL N N 124.0 0.1 1 9 . 3 THR H H 8.53 0.01 1 10 . 3 THR HA H 5.31 0.01 1 11 . 3 THR HB H 4.05 0.01 1 12 . 3 THR HG2 H 1.27 0.01 1 13 . 3 THR N N 125.8 0.1 1 14 . 4 TRP H H 10.24 0.01 1 15 . 4 TRP HA H 5.56 0.01 1 16 . 4 TRP HB2 H 3.21 0.01 2 17 . 4 TRP HB3 H 3.15 0.01 2 18 . 4 TRP HD1 H 7.26 0.01 1 19 . 4 TRP HE1 H 11.32 0.01 1 20 . 4 TRP HE3 H 7.40 0.01 1 21 . 4 TRP HZ2 H 7.46 0.01 1 22 . 4 TRP HZ3 H 7.38 0.01 1 23 . 4 TRP HH2 H 7.48 0.01 1 24 . 4 TRP N N 132.3 0.1 1 25 . 4 TRP NE1 N 134.7 0.1 1 26 . 5 THR H H 9.63 0.01 1 27 . 5 THR HA H 5.47 0.01 1 28 . 5 THR HB H 4.02 0.01 1 29 . 5 THR HG2 H 1.16 0.01 1 30 . 6 CYS H H 10.26 0.01 1 31 . 6 CYS HA H 5.39 0.01 1 32 . 6 CYS HB2 H 2.97 0.01 1 33 . 6 CYS HB3 H 2.97 0.01 1 34 . 6 CYS N N 129.0 0.1 1 35 . 7 LEU H H 8.91 0.01 1 36 . 7 LEU HA H 5.00 0.01 1 37 . 7 LEU HB2 H 1.89 0.01 2 38 . 7 LEU HB3 H 1.38 0.01 2 39 . 7 LEU HG H 1.79 0.01 1 40 . 7 LEU HD1 H 0.98 0.01 1 41 . 7 LEU HD2 H 0.86 0.01 1 42 . 7 LEU N N 125.4 0.1 1 43 . 8 ASN H H 8.94 0.01 1 44 . 8 ASN HA H 5.00 0.01 1 45 . 8 ASN HB2 H 2.55 0.01 2 46 . 8 ASN HB3 H 2.45 0.01 2 47 . 8 ASN HD21 H 8.40 0.01 1 48 . 8 ASN HD22 H 7.39 0.01 1 49 . 8 ASN N N 122.8 0.1 1 50 . 8 ASN ND2 N 113.4 0.1 1 51 . 9 ASP H H 9.05 0.01 1 52 . 9 ASP HA H 5.51 0.01 1 53 . 9 ASP HB2 H 2.81 0.01 2 54 . 9 ASP HB3 H 2.46 0.01 2 55 . 9 ASP N N 131.4 0.1 1 56 . 10 GLN H H 9.07 0.01 1 57 . 10 GLN HA H 4.91 0.01 1 58 . 10 GLN HB2 H 2.23 0.01 2 59 . 10 GLN HB3 H 1.81 0.01 2 60 . 10 GLN HG2 H 2.54 0.01 2 61 . 10 GLN HG3 H 2.50 0.01 2 62 . 10 GLN HE21 H 8.10 0.01 1 63 . 10 GLN HE22 H 6.92 0.01 1 64 . 10 GLN N N 122.1 0.1 1 65 . 10 GLN NE2 N 111.8 0.1 1 66 . 11 LYS H H 9.09 0.01 1 67 . 11 LYS HA H 3.57 0.01 1 68 . 11 LYS HB2 H 1.43 0.01 2 69 . 11 LYS HB3 H 1.10 0.01 2 70 . 11 LYS HG2 H 0.70 0.01 2 71 . 11 LYS HG3 H 0.55 0.01 2 72 . 11 LYS HD2 H 1.36 0.01 2 73 . 11 LYS HE2 H 2.71 0.01 2 74 . 11 LYS N N 127.6 0.1 1 75 . 12 ASN H H 8.70 0.01 1 76 . 12 ASN HA H 4.96 0.01 1 77 . 12 ASN HB2 H 3.44 0.01 2 78 . 12 ASN HB3 H 2.67 0.01 2 79 . 12 ASN HD21 H 8.18 0.01 1 80 . 12 ASN HD22 H 7.21 0.01 1 81 . 12 ASN N N 130.3 0.1 1 82 . 12 ASN ND2 N 116.6 0.1 1 83 . 13 PRO HA H 3.63 0.01 1 84 . 13 PRO HB2 H 2.40 0.01 2 85 . 13 PRO HB3 H 2.07 0.01 2 86 . 13 PRO HG2 H 2.13 0.01 2 87 . 13 PRO HG3 H 2.07 0.01 2 88 . 13 PRO HD2 H 4.09 0.01 2 89 . 13 PRO HD3 H 3.92 0.01 2 90 . 14 LYS H H 8.34 0.01 1 91 . 14 LYS HA H 4.35 0.01 1 92 . 14 LYS HB2 H 1.96 0.01 2 93 . 14 LYS HB3 H 1.77 0.01 2 94 . 14 LYS HG2 H 1.57 0.01 2 95 . 14 LYS HG3 H 1.46 0.01 2 96 . 14 LYS N N 117.7 0.1 1 97 . 15 THR H H 7.34 0.01 1 98 . 15 THR HA H 4.41 0.01 1 99 . 15 THR HB H 4.40 0.01 1 100 . 15 THR HG2 H 1.17 0.01 1 101 . 15 THR N N 106.9 0.1 1 102 . 16 ASN H H 8.62 0.01 1 103 . 16 ASN HA H 4.19 0.01 1 104 . 16 ASN HB2 H 3.15 0.01 2 105 . 16 ASN HB3 H 2.87 0.01 2 106 . 16 ASN HD21 H 7.47 0.01 1 107 . 16 ASN HD22 H 6.81 0.01 1 108 . 16 ASN N N 113.4 0.1 1 109 . 16 ASN ND2 N 118.0 0.1 1 110 . 17 LYS H H 7.56 0.01 1 111 . 17 LYS HA H 4.66 0.01 1 112 . 17 LYS HB2 H 1.92 0.01 2 113 . 17 LYS HB3 H 1.70 0.01 2 114 . 17 LYS HG2 H 1.52 0.01 2 115 . 17 LYS HG3 H 1.45 0.01 2 116 . 17 LYS N N 117.8 0.1 1 117 . 18 TYR H H 8.84 0.01 1 118 . 18 TYR HA H 4.53 0.01 1 119 . 18 TYR HB2 H 2.94 0.01 2 120 . 18 TYR HB3 H 2.70 0.01 2 121 . 18 TYR HD1 H 6.98 0.01 1 122 . 18 TYR HD2 H 6.98 0.01 1 123 . 18 TYR HE1 H 6.82 0.01 1 124 . 18 TYR HE2 H 6.82 0.01 1 125 . 18 TYR N N 121.6 0.1 1 126 . 19 GLU H H 8.90 0.01 1 127 . 19 GLU HA H 4.82 0.01 1 128 . 19 GLU HB2 H 2.13 0.01 2 129 . 19 GLU HB3 H 2.02 0.01 2 130 . 19 GLU HG2 H 2.37 0.01 2 131 . 19 GLU HG3 H 2.29 0.01 2 132 . 19 GLU N N 122.7 0.1 1 133 . 20 THR H H 8.89 0.01 1 134 . 20 THR HA H 4.57 0.01 1 135 . 20 THR HB H 3.95 0.01 1 136 . 20 THR HG2 H 1.25 0.01 1 137 . 20 THR N N 122.3 0.1 1 138 . 21 LYS H H 9.03 0.01 1 139 . 21 LYS HA H 4.68 0.01 1 140 . 21 LYS HB2 H 2.07 0.01 2 141 . 21 LYS HB3 H 1.90 0.01 2 142 . 21 LYS HG2 H 1.59 0.01 2 143 . 21 LYS HG3 H 1.54 0.01 2 144 . 21 LYS N N 131.6 0.1 1 145 . 22 ARG H H 8.43 0.01 1 146 . 22 ARG HA H 4.81 0.01 1 147 . 22 ARG HB2 H 1.78 0.01 2 148 . 22 ARG HG2 H 1.63 0.01 2 149 . 22 ARG HD2 H 3.23 0.01 2 150 . 22 ARG HE H 7.31 0.01 1 151 . 22 ARG N N 123.3 0.1 1 152 . 22 ARG NE N 84.6 0.1 1 153 . 23 LEU H H 9.08 0.01 1 154 . 23 LEU HA H 4.61 0.01 1 155 . 23 LEU HB2 H 1.94 0.01 2 156 . 23 LEU HB3 H 1.48 0.01 2 157 . 23 LEU HG H 1.53 0.01 1 158 . 23 LEU HD1 H 0.95 0.01 2 159 . 23 LEU N N 129.6 0.1 1 160 . 24 LEU H H 8.11 0.01 1 161 . 24 LEU HA H 5.48 0.01 1 162 . 24 LEU HB2 H 1.64 0.01 2 163 . 24 LEU HB3 H 1.31 0.01 2 164 . 24 LEU HG H 1.72 0.01 1 165 . 24 LEU HD1 H 0.93 0.01 1 166 . 24 LEU HD2 H 0.88 0.01 1 167 . 24 LEU N N 125.3 0.1 1 168 . 25 TYR H H 9.47 0.01 1 169 . 25 TYR HA H 4.71 0.01 1 170 . 25 TYR HB2 H 2.73 0.01 2 171 . 25 TYR HB3 H 2.71 0.01 2 172 . 25 TYR HD1 H 6.92 0.01 1 173 . 25 TYR HD2 H 6.92 0.01 1 174 . 25 TYR HE1 H 6.36 0.01 1 175 . 25 TYR HE2 H 6.36 0.01 1 176 . 25 TYR HH H 9.08 0.01 1 177 . 25 TYR N N 120.2 0.1 1 178 . 26 ASN H H 9.93 0.01 1 179 . 26 ASN HA H 5.01 0.01 1 180 . 26 ASN HB2 H 3.01 0.01 2 181 . 26 ASN HB3 H 2.95 0.01 2 182 . 26 ASN HD21 H 7.93 0.01 1 183 . 26 ASN HD22 H 7.15 0.01 1 184 . 26 ASN N N 126.4 0.1 1 185 . 26 ASN ND2 N 114.4 0.1 1 186 . 27 GLN H H 9.28 0.01 1 187 . 27 GLN HA H 3.54 0.01 1 188 . 27 GLN HB2 H 2.41 0.01 2 189 . 27 GLN HB3 H 2.25 0.01 2 190 . 27 GLN HG2 H 1.91 0.01 2 191 . 27 GLN HG3 H 1.38 0.01 2 192 . 27 GLN HE21 H 7.28 0.01 1 193 . 27 GLN HE22 H 6.67 0.01 1 194 . 27 GLN N N 128.4 0.1 1 195 . 27 GLN NE2 N 113.9 0.1 1 196 . 28 ASN H H 8.25 0.01 1 197 . 28 ASN HA H 4.34 0.01 1 198 . 28 ASN HB2 H 3.06 0.01 2 199 . 28 ASN HB3 H 2.89 0.01 2 200 . 28 ASN HD21 H 7.76 0.01 1 201 . 28 ASN HD22 H 7.11 0.01 1 202 . 28 ASN N N 117.3 0.1 1 203 . 28 ASN ND2 N 114.2 0.1 1 204 . 29 LYS H H 7.83 0.01 1 205 . 29 LYS HA H 4.13 0.01 1 206 . 29 LYS HB2 H 2.37 0.01 2 207 . 29 LYS HB3 H 1.98 0.01 2 208 . 29 LYS HG2 H 1.58 0.01 2 209 . 29 LYS HD2 H 1.86 0.01 2 210 . 29 LYS HD3 H 1.80 0.01 2 211 . 29 LYS N N 122.3 0.1 1 212 . 30 ALA H H 7.94 0.01 1 213 . 30 ALA HA H 4.36 0.01 1 214 . 30 ALA HB H 1.34 0.01 1 215 . 30 ALA N N 124.3 0.1 1 216 . 31 GLU H H 8.62 0.01 1 217 . 31 GLU HA H 3.73 0.01 1 218 . 31 GLU HB2 H 1.90 0.01 2 219 . 31 GLU HB3 H 1.85 0.01 2 220 . 31 GLU HG2 H 2.18 0.01 2 221 . 31 GLU HG3 H 2.01 0.01 2 222 . 31 GLU N N 118.5 0.1 1 223 . 32 SER H H 8.11 0.01 1 224 . 32 SER HA H 3.90 0.01 1 225 . 32 SER HB2 H 4.04 0.01 2 226 . 32 SER HB3 H 3.97 0.01 2 227 . 32 SER N N 119.2 0.1 1 228 . 33 ASN H H 8.40 0.01 1 229 . 33 ASN HA H 4.64 0.01 1 230 . 33 ASN HB2 H 3.37 0.01 2 231 . 33 ASN HB3 H 3.30 0.01 2 232 . 33 ASN HD21 H 8.29 0.01 1 233 . 33 ASN HD22 H 6.80 0.01 1 234 . 33 ASN N N 120.2 0.1 1 235 . 33 ASN ND2 N 112.0 0.1 1 236 . 34 SER H H 7.58 0.01 1 237 . 34 SER HA H 3.30 0.01 1 238 . 34 SER HB2 H 3.12 0.01 2 239 . 34 SER HB3 H 1.92 0.01 2 240 . 34 SER N N 111.5 0.1 1 241 . 35 HIS H H 7.57 0.01 1 242 . 35 HIS HA H 4.26 0.01 1 243 . 35 HIS HB2 H 3.43 0.01 2 244 . 35 HIS HB3 H 3.27 0.01 2 245 . 35 HIS HD2 H 7.02 0.01 1 246 . 35 HIS HE1 H 8.26 0.01 1 247 . 35 HIS N N 121.2 0.1 1 248 . 36 HIS H H 7.89 0.01 1 249 . 36 HIS HA H 4.71 0.01 1 250 . 36 HIS HB2 H 3.50 0.01 2 251 . 36 HIS HB3 H 3.35 0.01 2 252 . 36 HIS HD2 H 7.29 0.01 1 253 . 36 HIS HE1 H 8.50 0.01 1 254 . 36 HIS N N 117.4 0.1 1 255 . 37 ALA H H 6.87 0.01 1 256 . 37 ALA HA H 3.95 0.01 1 257 . 37 ALA HB H 0.37 0.01 1 258 . 37 ALA N N 123.8 0.1 1 259 . 38 PRO HA H 4.32 0.01 1 260 . 38 PRO HB2 H 1.71 0.01 2 261 . 38 PRO HB3 H 1.58 0.01 2 262 . 38 PRO HD2 H 2.54 0.01 2 263 . 38 PRO HD3 H 2.47 0.01 2 264 . 39 LEU H H 8.65 0.01 1 265 . 39 LEU HA H 4.60 0.01 1 266 . 39 LEU HB2 H 2.12 0.01 2 267 . 39 LEU HB3 H 1.42 0.01 2 268 . 39 LEU HG H 1.67 0.01 1 269 . 39 LEU HD1 H 0.98 0.01 1 270 . 39 LEU HD2 H 0.98 0.01 1 271 . 39 LEU N N 125.8 0.1 1 272 . 40 SER H H 7.53 0.01 1 273 . 40 SER HA H 4.58 0.01 1 274 . 40 SER HB2 H 3.84 0.01 2 275 . 40 SER HB3 H 3.74 0.01 2 276 . 40 SER N N 119.0 0.1 1 277 . 41 ASP H H 8.33 0.01 1 278 . 41 ASP HA H 5.18 0.01 1 279 . 41 ASP HB2 H 2.89 0.01 2 280 . 41 ASP HB3 H 2.81 0.01 2 281 . 41 ASP N N 118.8 0.1 1 282 . 42 GLY H H 9.22 0.01 1 283 . 42 GLY HA2 H 4.24 0.01 2 284 . 42 GLY HA3 H 4.15 0.01 1 285 . 42 GLY N N 113.1 0.1 1 286 . 43 LYS HA H 4.63 0.01 1 287 . 43 LYS HB2 H 2.11 0.01 2 288 . 43 LYS HB3 H 1.77 0.01 2 289 . 43 LYS HG2 H 1.43 0.01 2 290 . 43 LYS HD2 H 1.58 0.01 2 291 . 43 LYS N N 119.6 0.1 1 292 . 44 THR H H 7.50 0.01 1 293 . 44 THR HA H 4.71 0.01 1 294 . 44 THR HB H 5.17 0.01 1 295 . 44 THR HG2 H 1.58 0.01 1 296 . 44 THR N N 110.4 0.1 1 297 . 45 GLY H H 9.68 0.01 1 298 . 45 GLY HA2 H 3.98 0.01 2 299 . 45 GLY HA3 H 3.84 0.01 2 300 . 45 GLY N N 109.4 0.1 1 301 . 46 SER H H 8.36 0.01 1 302 . 46 SER HA H 4.60 0.01 1 303 . 46 SER HB2 H 4.31 0.01 2 304 . 46 SER HB3 H 4.33 0.01 2 305 . 46 SER N N 113.2 0.1 1 306 . 47 SER H H 7.94 0.01 1 307 . 47 SER HA H 4.12 0.01 1 308 . 47 SER HB2 H 3.90 0.01 2 309 . 47 SER HB3 H 3.95 0.01 2 310 . 47 SER N N 113.2 0.1 1 311 . 48 TYR H H 8.86 0.01 1 312 . 48 TYR HA H 4.85 0.01 1 313 . 48 TYR HB2 H 3.07 0.01 2 314 . 48 TYR HD1 H 7.05 0.01 1 315 . 48 TYR HD2 H 7.05 0.01 1 316 . 48 TYR HE1 H 6.77 0.01 1 317 . 48 TYR HE2 H 6.77 0.01 1 318 . 48 TYR N N 121.6 0.1 1 319 . 49 PRO HA H 5.79 0.01 1 320 . 49 PRO HB2 H 3.02 0.01 2 321 . 49 PRO HB3 H 2.60 0.01 2 322 . 49 PRO HG2 H 2.30 0.01 2 323 . 49 PRO HG3 H 2.85 0.01 2 324 . 49 PRO HD2 H 4.00 0.01 2 325 . 49 PRO HD3 H 3.67 0.01 2 326 . 50 HIS H H 7.94 0.01 1 327 . 50 HIS HA H 5.49 0.01 1 328 . 50 HIS HB2 H 3.98 0.01 2 329 . 50 HIS HB3 H 3.61 0.01 2 330 . 50 HIS HD2 H 7.15 0.01 1 331 . 50 HIS HE1 H 7.87 0.01 1 332 . 50 HIS N N 109.6 0.1 1 333 . 51 TRP H H 9.55 0.01 1 334 . 51 TRP HA H 5.37 0.01 1 335 . 51 TRP HB2 H 3.20 0.01 2 336 . 51 TRP HB3 H 2.75 0.01 2 337 . 51 TRP HD1 H 8.06 0.01 1 338 . 51 TRP HE1 H 9.61 0.01 1 339 . 51 TRP HE3 H 6.93 0.01 1 340 . 51 TRP HZ2 H 6.77 0.01 1 341 . 51 TRP HZ3 H 6.79 0.01 1 342 . 51 TRP HH2 H 6.91 0.01 1 343 . 51 TRP N N 124.4 0.1 1 344 . 51 TRP NE1 N 128.2 0.1 1 345 . 52 PHE H H 9.33 0.01 1 346 . 52 PHE HA H 5.05 0.01 1 347 . 52 PHE HB2 H 2.94 0.01 2 348 . 52 PHE HB3 H 2.68 0.01 2 349 . 52 PHE HD1 H 7.28 0.01 1 350 . 52 PHE HD2 H 7.28 0.01 1 351 . 52 PHE HE1 H 7.23 0.01 3 352 . 52 PHE HE2 H 7.28 0.01 3 353 . 52 PHE HZ H 7.21 0.01 1 354 . 52 PHE N N 134.5 0.1 1 355 . 53 THR H H 7.93 0.01 1 356 . 53 THR HA H 2.68 0.01 1 357 . 53 THR HB H 4.20 0.01 1 358 . 53 THR HG2 H -0.51 0.01 1 359 . 54 ASN H H 6.04 0.01 1 360 . 54 ASN HA H 3.71 0.01 1 361 . 54 ASN HB2 H 3.61 0.01 2 362 . 54 ASN HB3 H 2.11 0.01 2 363 . 54 ASN HD21 H 8.19 0.01 1 364 . 54 ASN HD22 H 8.19 0.01 1 365 . 54 ASN N N 116.0 0.1 1 366 . 54 ASN ND2 N 110.0 0.1 1 367 . 55 GLY H H 7.48 0.01 1 368 . 55 GLY HA2 H 3.84 0.01 2 369 . 55 GLY HA3 H 3.18 0.01 2 370 . 55 GLY N N 100.4 0.1 1 371 . 56 TYR H H 7.29 0.01 1 372 . 56 TYR HA H 4.60 0.01 1 373 . 56 TYR HB2 H 3.45 0.01 2 374 . 56 TYR HB3 H 3.12 0.01 2 375 . 56 TYR HD1 H 7.24 0.01 1 376 . 56 TYR HD2 H 7.24 0.01 1 377 . 56 TYR HE1 H 6.90 0.01 1 378 . 56 TYR HE2 H 6.90 0.01 1 379 . 56 TYR N N 119.6 0.1 1 380 . 57 ASP H H 8.52 0.01 1 381 . 57 ASP HA H 5.09 0.01 1 382 . 57 ASP HB2 H 3.35 0.01 2 383 . 57 ASP HB3 H 2.96 0.01 2 384 . 57 ASP N N 117.8 0.1 1 385 . 58 GLY H H 8.94 0.01 1 386 . 58 GLY HA2 H 4.15 0.01 2 387 . 58 GLY HA3 H 3.99 0.01 2 388 . 58 GLY N N 105.0 0.1 1 389 . 59 ASP H H 8.23 0.01 1 390 . 59 ASP HA H 4.95 0.01 1 391 . 59 ASP HB2 H 2.96 0.01 2 392 . 59 ASP HB3 H 2.89 0.01 2 393 . 59 ASP N N 118.8 0.1 1 394 . 60 GLY H H 8.33 0.01 1 395 . 60 GLY HA2 H 4.31 0.01 2 396 . 60 GLY HA3 H 3.62 0.01 2 397 . 60 GLY N N 111.2 0.1 1 398 . 61 LYS H H 8.29 0.01 1 399 . 61 LYS HA H 4.59 0.01 1 400 . 61 LYS HB2 H 1.84 0.01 2 401 . 61 LYS HB3 H 1.53 0.01 2 402 . 61 LYS HG2 H 1.48 0.01 2 403 . 61 LYS HG3 H 1.39 0.01 2 404 . 61 LYS N N 122.6 0.1 1 405 . 62 LEU H H 8.54 0.01 1 406 . 62 LEU HA H 4.83 0.01 1 407 . 62 LEU HB2 H 1.72 0.01 2 408 . 62 LEU HG H 1.30 0.01 1 409 . 62 LEU HD1 H 0.21 0.01 1 410 . 62 LEU HD2 H 0.46 0.01 1 411 . 62 LEU N N 126.6 0.1 1 412 . 63 PRO HA H 4.44 0.01 1 413 . 63 PRO HB2 H 2.38 0.01 2 414 . 63 PRO HG2 H 1.97 0.01 2 415 . 63 PRO HG3 H 1.94 0.01 2 416 . 63 PRO HD2 H 4.05 0.01 2 417 . 63 PRO HD3 H 3.57 0.01 2 418 . 64 LYS H H 8.29 0.01 1 419 . 64 LYS HA H 4.09 0.01 1 420 . 64 LYS HB2 H 1.85 0.01 2 421 . 64 LYS HB3 H 1.79 0.01 2 422 . 64 LYS HG2 H 1.56 0.01 2 423 . 64 LYS HG3 H 1.48 0.01 2 424 . 64 LYS N N 122.6 0.1 1 425 . 65 GLY H H 8.73 0.01 1 426 . 65 GLY HA2 H 4.23 0.01 2 427 . 65 GLY HA3 H 3.72 0.01 2 428 . 65 GLY N N 113.2 0.1 1 429 . 66 ARG H H 7.47 0.01 1 430 . 66 ARG HA H 4.53 0.01 1 431 . 66 ARG HB2 H 1.68 0.01 2 432 . 66 ARG HG2 H 1.50 0.01 2 433 . 66 ARG HD2 H 3.15 0.01 2 434 . 66 ARG HD3 H 3.10 0.01 2 435 . 66 ARG HE H 7.16 0.01 1 436 . 66 ARG N N 121.0 0.1 1 437 . 66 ARG NE N 84.8 0.1 1 438 . 67 THR H H 8.61 0.01 1 439 . 67 THR HA H 4.72 0.01 1 440 . 67 THR HB H 4.02 0.01 1 441 . 67 THR HG2 H 1.19 0.01 1 442 . 67 THR N N 120.0 0.1 1 443 . 68 PRO HA H 4.22 0.01 1 444 . 68 PRO HB2 H 2.57 0.01 2 445 . 68 PRO HB3 H 2.00 0.01 2 446 . 68 PRO HG2 H 1.95 0.01 2 447 . 68 PRO HG3 H 1.89 0.01 2 448 . 68 PRO HD2 H 3.75 0.01 2 449 . 68 PRO HD3 H 3.66 0.01 2 450 . 69 ILE H H 9.20 0.01 1 451 . 69 ILE HA H 3.70 0.01 1 452 . 69 ILE HB H 1.53 0.01 1 453 . 69 ILE HG12 H 1.88 0.01 2 454 . 69 ILE HG13 H 1.12 0.01 2 455 . 69 ILE HG2 H 0.83 0.01 1 456 . 69 ILE HD1 H 0.05 0.01 1 457 . 69 ILE N N 125.0 0.1 1 458 . 70 LYS H H 8.30 0.01 1 459 . 70 LYS HA H 4.44 0.01 1 460 . 70 LYS HB2 H 1.81 0.01 2 461 . 70 LYS HB3 H 1.72 0.01 2 462 . 70 LYS HG2 H 1.48 0.01 2 463 . 70 LYS HG3 H 1.32 0.01 2 464 . 70 LYS N N 131.0 0.1 1 465 . 71 PHE H H 10.96 0.01 1 466 . 71 PHE HA H 4.53 0.01 1 467 . 71 PHE HB2 H 3.26 0.01 2 468 . 71 PHE HB3 H 2.78 0.01 2 469 . 71 PHE HD1 H 7.24 0.01 1 470 . 71 PHE HD2 H 7.24 0.01 1 471 . 71 PHE HE1 H 6.94 0.01 1 472 . 71 PHE HE2 H 6.94 0.01 1 473 . 71 PHE HZ H 6.88 0.01 1 474 . 71 PHE N N 127.2 0.1 1 475 . 72 GLY H H 9.98 0.01 1 476 . 72 GLY HA2 H 4.30 0.01 2 477 . 72 GLY HA3 H 3.78 0.01 2 478 . 72 GLY N N 112.5 0.1 1 479 . 73 LYS H H 7.08 0.01 1 480 . 73 LYS HA H 4.84 0.01 1 481 . 73 LYS HB2 H 1.99 0.01 2 482 . 73 LYS HB3 H 1.93 0.01 2 483 . 73 LYS HG2 H 1.57 0.01 2 484 . 73 LYS N N 117.9 0.1 1 485 . 74 SER H H 9.43 0.01 1 486 . 74 SER HA H 4.21 0.01 1 487 . 74 SER HB2 H 4.01 0.01 1 488 . 74 SER HB3 H 4.01 0.01 1 489 . 74 SER N N 126.3 0.1 1 490 . 75 ASP H H 8.96 0.01 1 491 . 75 ASP HA H 4.40 0.01 1 492 . 75 ASP HB2 H 2.65 0.01 2 493 . 75 ASP HB3 H 2.45 0.01 2 494 . 75 ASP N N 118.4 0.1 1 495 . 76 CYS H H 7.15 0.01 1 496 . 76 CYS HA H 4.42 0.01 1 497 . 76 CYS HB2 H 3.29 0.01 2 498 . 76 CYS HB3 H 2.63 0.01 2 499 . 76 CYS N N 113.1 0.1 1 500 . 77 ASP H H 7.89 0.01 1 501 . 77 ASP HA H 5.00 0.01 1 502 . 77 ASP HB2 H 3.00 0.01 2 503 . 77 ASP HB3 H 2.53 0.01 2 504 . 77 ASP N N 119.2 0.1 1 505 . 78 ARG H H 7.52 0.01 1 506 . 78 ARG HA H 4.88 0.01 1 507 . 78 ARG HB2 H 2.02 0.01 2 508 . 78 ARG HB3 H 1.86 0.01 2 509 . 78 ARG HG2 H 1.82 0.01 2 510 . 78 ARG HG3 H 1.73 0.01 2 511 . 78 ARG HD2 H 3.07 0.01 1 512 . 78 ARG HD3 H 3.07 0.01 1 513 . 78 ARG HE H 6.98 0.01 1 514 . 78 ARG N N 123.3 0.1 1 515 . 78 ARG NE N 84.4 0.1 1 516 . 79 PRO HA H 3.75 0.01 1 517 . 79 PRO HB2 H 2.68 0.01 2 518 . 79 PRO HB3 H 2.48 0.01 2 519 . 79 PRO HG2 H 2.37 0.01 2 520 . 79 PRO HG3 H 2.16 0.01 2 521 . 79 PRO HD2 H 4.15 0.01 2 522 . 79 PRO HD3 H 3.69 0.01 2 523 . 80 PRO HA H 4.95 0.01 1 524 . 80 PRO HB2 H 1.87 0.01 2 525 . 80 PRO HG2 H 2.28 0.01 2 526 . 80 PRO HD2 H 3.32 0.01 2 527 . 81 LYS H H 8.35 0.01 1 528 . 81 LYS HA H 4.41 0.01 1 529 . 81 LYS HB2 H 1.71 0.01 2 530 . 81 LYS HB3 H 1.43 0.01 2 531 . 81 LYS HG2 H 1.48 0.01 2 532 . 81 LYS HG3 H 1.31 0.01 2 533 . 81 LYS HD2 H 1.26 0.01 2 534 . 81 LYS N N 118.2 0.1 1 535 . 82 HIS H H 9.36 0.01 1 536 . 82 HIS HA H 4.08 0.01 1 537 . 82 HIS HB2 H 1.87 0.01 2 538 . 82 HIS HB3 H 1.33 0.01 2 539 . 82 HIS HD2 H 3.46 0.01 1 540 . 82 HIS HE1 H 7.99 0.01 1 541 . 82 HIS N N 127.6 0.1 1 542 . 83 SER H H 8.85 0.01 1 543 . 83 SER HA H 4.31 0.01 1 544 . 83 SER HB2 H 3.99 0.01 2 545 . 83 SER HB3 H 3.84 0.01 2 546 . 83 SER N N 125.6 0.1 1 547 . 84 LYS H H 8.37 0.01 1 548 . 84 LYS HA H 3.93 0.01 1 549 . 84 LYS HB2 H 1.86 0.01 2 550 . 84 LYS HB3 H 1.72 0.01 2 551 . 84 LYS HD2 H 1.47 0.01 2 552 . 84 LYS HD3 H 1.40 0.01 2 553 . 84 LYS N N 122.8 0.1 1 554 . 85 ASP H H 8.25 0.01 1 555 . 85 ASP HA H 3.85 0.01 1 556 . 85 ASP HB2 H 2.80 0.01 2 557 . 85 ASP HB3 H 2.77 0.01 2 558 . 85 ASP N N 116.8 0.1 1 559 . 86 GLY H H 7.76 0.01 1 560 . 86 GLY HA2 H 3.75 0.01 2 561 . 86 GLY HA3 H 2.77 0.01 2 562 . 86 GLY N N 107.6 0.1 1 563 . 87 ASN H H 7.37 0.01 1 564 . 87 ASN HA H 5.09 0.01 1 565 . 87 ASN HB2 H 2.93 0.01 2 566 . 87 ASN HB3 H 2.62 0.01 2 567 . 87 ASN HD21 H 7.45 0.01 1 568 . 87 ASN HD22 H 6.91 0.01 1 569 . 87 ASN N N 116.7 0.1 1 570 . 87 ASN ND2 N 111.4 0.1 1 571 . 88 GLY H H 8.01 0.01 1 572 . 88 GLY HA2 H 4.07 0.01 2 573 . 88 GLY HA3 H 3.70 0.01 2 574 . 88 GLY N N 110.3 0.1 1 575 . 89 LYS H H 8.94 0.01 1 576 . 89 LYS HA H 4.17 0.01 1 577 . 89 LYS HB2 H 2.00 0.01 2 578 . 89 LYS HB3 H 1.97 0.01 2 579 . 89 LYS HG2 H 1.65 0.01 2 580 . 89 LYS HG3 H 1.59 0.01 2 581 . 89 LYS N N 126.4 0.1 1 582 . 90 THR H H 8.20 0.01 1 583 . 90 THR HA H 4.70 0.01 1 584 . 90 THR HB H 4.79 0.01 1 585 . 90 THR HG2 H 1.21 0.01 1 586 . 90 THR N N 106.7 0.1 1 587 . 91 ASP H H 7.24 0.01 1 588 . 91 ASP HA H 4.39 0.01 1 589 . 91 ASP HB2 H 2.89 0.01 2 590 . 91 ASP HB3 H 2.76 0.01 2 591 . 91 ASP N N 123.8 0.1 1 592 . 92 HIS H H 8.78 0.01 1 593 . 92 HIS HA H 5.21 0.01 1 594 . 92 HIS HB2 H 3.48 0.01 2 595 . 92 HIS HB3 H 3.30 0.01 2 596 . 92 HIS HD2 H 7.62 0.01 1 597 . 92 HIS HE1 H 8.88 0.01 1 598 . 92 HIS N N 115.8 0.1 1 599 . 93 TYR H H 8.11 0.01 1 600 . 93 TYR HA H 4.95 0.01 1 601 . 93 TYR HB2 H 3.36 0.01 2 602 . 93 TYR HB3 H 3.18 0.01 2 603 . 93 TYR HD1 H 7.15 0.01 1 604 . 93 TYR HD2 H 7.15 0.01 1 605 . 93 TYR HE1 H 6.27 0.01 1 606 . 93 TYR HE2 H 6.27 0.01 1 607 . 93 TYR N N 119.8 0.1 1 608 . 94 LEU H H 9.47 0.01 1 609 . 94 LEU HA H 4.96 0.01 1 610 . 94 LEU HB2 H 2.96 0.01 2 611 . 94 LEU HB3 H 1.40 0.01 2 612 . 94 LEU HG H 2.22 0.01 1 613 . 94 LEU HD1 H 1.27 0.01 1 614 . 94 LEU HD2 H 0.96 0.01 1 615 . 94 LEU N N 119.0 0.1 1 616 . 95 LEU H H 9.50 0.01 1 617 . 95 LEU HA H 4.93 0.01 1 618 . 95 LEU HB2 H 0.62 0.01 2 619 . 95 LEU HG H 1.53 0.01 1 620 . 95 LEU HD1 H 0.94 0.01 1 621 . 95 LEU HD2 H 1.09 0.01 1 622 . 95 LEU N N 125.7 0.1 1 623 . 96 GLU H H 8.29 0.01 1 624 . 96 GLU HA H 5.77 0.01 1 625 . 96 GLU HB2 H 1.86 0.01 2 626 . 96 GLU HB3 H 1.66 0.01 2 627 . 96 GLU HG2 H 2.44 0.01 2 628 . 96 GLU HG3 H 1.96 0.01 2 629 . 96 GLU N N 111.4 0.1 1 630 . 97 PHE H H 8.43 0.01 1 631 . 97 PHE HA H 5.13 0.01 1 632 . 97 PHE HB2 H 3.67 0.01 2 633 . 97 PHE HB3 H 2.94 0.01 2 634 . 97 PHE HD1 H 7.23 0.01 1 635 . 97 PHE HD2 H 7.23 0.01 1 636 . 97 PHE HE1 H 7.80 0.01 1 637 . 97 PHE HE2 H 7.80 0.01 1 638 . 97 PHE HZ H 8.15 0.01 1 639 . 97 PHE N N 122.6 0.1 1 640 . 98 PRO HA H 4.11 0.01 1 641 . 98 PRO HB2 H 2.28 0.01 2 642 . 98 PRO HB3 H 0.62 0.01 2 643 . 98 PRO HG2 H -0.39 0.01 2 644 . 98 PRO HG3 H -0.90 0.01 2 645 . 98 PRO HD2 H 2.56 0.01 2 646 . 98 PRO HD3 H 1.03 0.01 2 647 . 99 THR H H 6.71 0.01 1 648 . 99 THR HA H 4.50 0.01 1 649 . 99 THR HB H 3.76 0.01 1 650 . 99 THR HG1 H 5.27 0.01 1 651 . 99 THR HG2 H 0.56 0.01 1 652 . 99 THR N N 117.0 0.1 1 653 . 100 PHE H H 9.91 0.01 1 654 . 100 PHE HA H 5.80 0.01 1 655 . 100 PHE HB2 H 3.47 0.01 2 656 . 100 PHE HB3 H 2.67 0.01 2 657 . 100 PHE HD1 H 7.12 0.01 1 658 . 100 PHE HD2 H 7.12 0.01 1 659 . 100 PHE HE1 H 7.10 0.01 3 660 . 100 PHE HE2 H 7.12 0.01 3 661 . 100 PHE HZ H 7.51 0.01 3 662 . 100 PHE N N 125.5 0.1 1 663 . 101 PRO HA H 4.21 0.01 1 664 . 101 PRO HB3 H 2.13 0.01 2 665 . 101 PRO HG2 H 2.13 0.01 2 666 . 101 PRO HG3 H 1.93 0.01 2 667 . 101 PRO HD2 H 4.57 0.01 2 668 . 101 PRO HD3 H 4.10 0.01 2 669 . 102 ASP H H 8.29 0.01 1 670 . 102 ASP HA H 4.53 0.01 1 671 . 102 ASP HB2 H 3.22 0.01 2 672 . 102 ASP HB3 H 2.85 0.01 2 673 . 102 ASP N N 114.0 0.1 1 674 . 103 GLY H H 8.60 0.01 1 675 . 103 GLY HA2 H 4.34 0.01 2 676 . 103 GLY HA3 H 4.16 0.01 2 677 . 103 GLY N N 110.2 0.1 1 678 . 104 HIS H H 8.68 0.01 1 679 . 104 HIS HA H 4.60 0.01 1 680 . 104 HIS HB2 H 3.46 0.01 2 681 . 104 HIS HB3 H 3.10 0.01 2 682 . 104 HIS HD2 H 6.98 0.01 1 683 . 104 HIS HE1 H 6.65 0.01 1 684 . 104 HIS N N 121.8 0.1 1 685 . 105 ASP H H 9.16 0.01 1 686 . 105 ASP HA H 4.84 0.01 1 687 . 105 ASP HB2 H 3.09 0.01 2 688 . 105 ASP HB3 H 2.83 0.01 2 689 . 105 ASP N N 124.4 0.1 1 690 . 106 TYR H H 9.46 0.01 1 691 . 106 TYR HA H 4.19 0.01 1 692 . 106 TYR HB2 H 2.86 0.01 1 693 . 106 TYR HB3 H 2.86 0.01 1 694 . 106 TYR N N 129.5 0.1 1 695 . 107 LYS H H 8.20 0.01 1 696 . 107 LYS HA H 4.32 0.01 1 697 . 107 LYS HB2 H 1.72 0.01 2 698 . 107 LYS HG2 H 1.53 0.01 2 699 . 107 LYS HG3 H 1.42 0.01 2 700 . 107 LYS N N 130.1 0.1 1 701 . 108 PHE H H 8.03 0.01 1 702 . 108 PHE HA H 4.82 0.01 1 703 . 108 PHE HB2 H 4.32 0.01 2 704 . 108 PHE HB3 H 3.44 0.01 2 705 . 108 PHE HD1 H 7.71 0.01 1 706 . 108 PHE HD2 H 7.71 0.01 1 707 . 108 PHE HE1 H 7.73 0.01 1 708 . 108 PHE HE2 H 7.73 0.01 1 709 . 108 PHE HZ H 7.66 0.01 1 710 . 108 PHE N N 126.5 0.1 1 711 . 109 ASP H H 8.91 0.01 1 712 . 109 ASP HA H 5.38 0.01 1 713 . 109 ASP HB2 H 2.79 0.01 2 714 . 109 ASP HB3 H 2.55 0.01 2 715 . 109 ASP N N 125.8 0.1 1 716 . 110 SER H H 7.45 0.01 1 717 . 110 SER HA H 4.24 0.01 1 718 . 110 SER HB2 H 4.03 0.01 1 719 . 110 SER HB3 H 4.03 0.01 1 720 . 110 SER N N 116.8 0.1 1 721 . 111 LYS H H 7.97 0.01 1 722 . 111 LYS HA H 4.32 0.01 1 723 . 111 LYS HB2 H 1.85 0.01 2 724 . 111 LYS HB3 H 1.72 0.01 2 725 . 111 LYS HG2 H 1.42 0.01 2 726 . 111 LYS HD2 H 1.65 0.01 2 727 . 111 LYS N N 119.2 0.1 1 728 . 112 LYS H H 8.19 0.01 1 729 . 112 LYS HA H 4.23 0.01 1 730 . 112 LYS N N 121.5 0.1 1 731 . 113 PRO HA H 4.49 0.01 1 732 . 113 PRO HB2 H 2.05 0.01 2 733 . 113 PRO HB3 H 2.27 0.01 2 734 . 114 LYS H H 8.39 0.01 1 735 . 114 LYS HA H 4.11 0.01 1 736 . 114 LYS HB2 H 1.87 0.01 2 737 . 114 LYS HB3 H 1.63 0.01 2 738 . 114 LYS N N 122.2 0.1 1 739 . 115 GLU H H 9.11 0.01 1 740 . 115 GLU HA H 4.11 0.01 1 741 . 115 GLU HB2 H 1.84 0.01 2 742 . 115 GLU HB3 H 1.43 0.01 2 743 . 115 GLU HG2 H 2.51 0.01 2 744 . 115 GLU HG3 H 2.37 0.01 2 745 . 115 GLU N N 128.6 0.1 1 746 . 116 ASN H H 9.15 0.01 1 747 . 116 ASN HA H 4.94 0.01 1 748 . 116 ASN HB2 H 3.15 0.01 2 749 . 116 ASN HB3 H 3.10 0.01 2 750 . 116 ASN HD21 H 7.83 0.01 2 751 . 116 ASN HD22 H 7.09 0.01 2 752 . 116 ASN N N 132.0 0.1 1 753 . 116 ASN ND2 N 114.0 0.1 1 754 . 117 PRO HA H 4.37 0.01 1 755 . 117 PRO HB2 H 1.63 0.01 2 756 . 117 PRO HG2 H 2.22 0.01 2 757 . 117 PRO HD2 H 4.31 0.01 2 758 . 117 PRO HD3 H 4.14 0.01 2 759 . 118 GLY H H 8.36 0.01 1 760 . 118 GLY HA2 H 4.19 0.01 2 761 . 118 GLY HA3 H 3.99 0.01 2 762 . 118 GLY N N 104.8 0.1 1 763 . 119 PRO HA H 4.54 0.01 1 764 . 119 PRO HB2 H 2.64 0.01 2 765 . 119 PRO HB3 H 1.92 0.01 2 766 . 119 PRO HG2 H 2.03 0.01 2 767 . 119 PRO HG3 H 1.36 0.01 2 768 . 120 ALA H H 9.12 0.01 1 769 . 120 ALA HA H 5.26 0.01 1 770 . 120 ALA HB H 1.08 0.01 1 771 . 120 ALA N N 125.0 0.1 1 772 . 121 ARG H H 9.13 0.01 1 773 . 121 ARG HA H 4.61 0.01 1 774 . 121 ARG HB2 H 1.40 0.01 2 775 . 121 ARG HB3 H 1.23 0.01 2 776 . 121 ARG N N 119.0 0.1 1 777 . 121 ARG NE N 84.8 0.1 1 778 . 122 VAL H H 9.16 0.01 1 779 . 122 VAL HA H 4.55 0.01 1 780 . 122 VAL HB H 1.85 0.01 1 781 . 122 VAL HG1 H 1.25 0.01 1 782 . 122 VAL HG2 H 1.03 0.01 1 783 . 122 VAL N N 121.9 0.1 1 784 . 123 ILE H H 8.21 0.01 1 785 . 123 ILE HA H 5.31 0.01 1 786 . 123 ILE HB H 1.31 0.01 1 787 . 123 ILE HG12 H 1.28 0.01 2 788 . 123 ILE HG13 H 1.65 0.01 2 789 . 123 ILE HG2 H 0.55 0.01 1 790 . 123 ILE HD1 H 0.05 0.01 1 791 . 123 ILE N N 128.6 0.1 1 792 . 124 TYR H H 8.42 0.01 1 793 . 124 TYR HA H 5.56 0.01 1 794 . 124 TYR HB2 H 2.96 0.01 2 795 . 124 TYR HB3 H 2.42 0.01 2 796 . 124 TYR HD1 H 6.70 0.01 1 797 . 124 TYR HD2 H 6.70 0.01 1 798 . 124 TYR HE1 H 6.56 0.01 1 799 . 124 TYR HE2 H 6.56 0.01 1 800 . 124 TYR HH H 9.03 0.01 2 801 . 124 TYR N N 127.0 0.1 1 802 . 125 THR H H 8.73 0.01 1 803 . 125 THR HA H 4.66 0.01 1 804 . 125 THR HB H 4.38 0.01 1 805 . 125 THR HG1 H 5.72 0.01 1 806 . 125 THR HG2 H 1.08 0.01 1 807 . 125 THR N N 110.5 0.1 1 808 . 126 TYR HA H 4.66 0.01 1 809 . 126 TYR HB2 H 2.10 0.01 2 810 . 126 TYR HB3 H 1.64 0.01 2 811 . 126 TYR HD1 H 6.53 0.01 1 812 . 126 TYR HD2 H 6.53 0.01 1 813 . 126 TYR HE1 H 6.72 0.01 1 814 . 126 TYR HE2 H 6.72 0.01 1 815 . 126 TYR N N 121.9 0.1 1 816 . 127 PRO HA H 3.57 0.01 1 817 . 127 PRO HB2 H 1.94 0.01 2 818 . 127 PRO HB3 H 1.58 0.01 2 819 . 127 PRO HG2 H 1.73 0.01 2 820 . 127 PRO HD2 H 3.70 0.01 2 821 . 127 PRO HD3 H 3.57 0.01 2 822 . 128 ASN H H 7.42 0.01 1 823 . 128 ASN HA H 4.57 0.01 1 824 . 128 ASN HB2 H 2.89 0.01 2 825 . 128 ASN HB3 H 2.78 0.01 2 826 . 128 ASN HD21 H 7.69 0.01 1 827 . 128 ASN HD22 H 7.17 0.01 1 828 . 128 ASN N N 117.8 0.1 1 829 . 128 ASN ND2 N 116.0 0.1 1 830 . 129 LYS H H 8.49 0.01 1 831 . 129 LYS HA H 4.49 0.01 1 832 . 129 LYS HB2 H 2.10 0.01 2 833 . 129 LYS HG2 H 1.58 0.01 2 834 . 129 LYS HG3 H 1.21 0.01 2 835 . 129 LYS N N 119.0 0.1 1 836 . 130 VAL H H 8.23 0.01 1 837 . 130 VAL HA H 3.80 0.01 1 838 . 130 VAL HB H 2.09 0.01 1 839 . 130 VAL HG1 H 1.08 0.01 2 840 . 130 VAL HG2 H 0.91 0.01 2 841 . 130 VAL N N 123.4 0.1 1 842 . 131 PHE H H 8.76 0.01 1 843 . 131 PHE HA H 4.19 0.01 1 844 . 131 PHE HB2 H 3.33 0.01 2 845 . 131 PHE HB3 H 2.87 0.01 2 846 . 131 PHE HD1 H 7.02 0.01 4 847 . 131 PHE HD2 H 7.02 0.01 4 848 . 131 PHE HE1 H 7.02 0.01 4 849 . 131 PHE HE2 H 7.02 0.01 4 850 . 131 PHE HZ H 6.16 0.01 1 851 . 131 PHE N N 128.9 0.1 1 852 . 132 CYS H H 8.36 0.01 1 853 . 132 CYS HA H 4.62 0.01 1 854 . 132 CYS HB2 H 1.58 0.01 2 855 . 132 CYS HB3 H 1.48 0.01 2 856 . 132 CYS N N 124.7 0.1 1 857 . 133 GLY H H 6.32 0.01 1 858 . 133 GLY HA2 H 3.54 0.01 2 859 . 133 GLY HA3 H 3.15 0.01 2 860 . 133 GLY N N 104.1 0.1 1 861 . 134 ILE H H 5.13 0.01 1 862 . 134 ILE HA H 4.59 0.01 1 863 . 134 ILE HB H 0.80 0.01 1 864 . 134 ILE HG12 H 0.21 0.01 2 865 . 134 ILE HG2 H 0.15 0.01 1 866 . 134 ILE HD1 H 0.25 0.01 1 867 . 134 ILE N N 119.2 0.1 1 868 . 135 ILE H H 8.27 0.01 1 869 . 135 ILE HA H 5.27 0.01 1 870 . 135 ILE HB H 1.37 0.01 1 871 . 135 ILE HG12 H 0.80 0.01 2 872 . 135 ILE HG13 H 0.53 0.01 2 873 . 135 ILE HG2 H 0.70 0.01 1 874 . 135 ILE HD1 H 0.02 0.01 1 875 . 135 ILE N N 119.2 0.1 1 876 . 136 ALA H H 8.89 0.01 1 877 . 136 ALA HA H 5.26 0.01 1 878 . 136 ALA HB H 1.36 0.01 1 879 . 136 ALA N N 119.8 0.1 1 880 . 137 HIS H H 8.85 0.01 1 881 . 137 HIS HA H 4.85 0.01 1 882 . 137 HIS HB2 H 3.64 0.01 2 883 . 137 HIS HB3 H 3.08 0.01 2 884 . 137 HIS HD2 H 7.14 0.01 1 885 . 137 HIS HE1 H 8.87 0.01 1 886 . 137 HIS N N 123.2 0.1 1 887 . 138 THR H H 8.26 0.01 1 888 . 138 THR HA H 4.56 0.01 1 889 . 138 THR HB H 4.40 0.01 1 890 . 138 THR HG2 H 1.42 0.01 1 891 . 138 THR N N 114.0 0.1 1 892 . 139 LYS H H 8.00 0.01 1 893 . 139 LYS HA H 4.83 0.01 1 894 . 139 LYS HB2 H 1.66 0.01 2 895 . 139 LYS N N 126.2 0.1 1 896 . 140 GLU H H 9.10 0.01 1 897 . 140 GLU HA H 4.02 0.01 1 898 . 140 GLU HB2 H 2.37 0.01 2 899 . 140 GLU HB3 H 2.24 0.01 2 900 . 140 GLU HG2 H 2.74 0.01 2 901 . 140 GLU HG3 H 2.63 0.01 2 902 . 140 GLU N N 125.7 0.1 1 903 . 141 ASN H H 8.12 0.01 1 904 . 141 ASN HA H 4.85 0.01 1 905 . 141 ASN HB2 H 2.93 0.01 2 906 . 141 ASN HB3 H 2.70 0.01 2 907 . 141 ASN HD21 H 7.36 0.01 1 908 . 141 ASN HD22 H 6.88 0.01 1 909 . 141 ASN N N 120.4 0.1 1 910 . 141 ASN ND2 N 111.6 0.1 1 911 . 142 GLN H H 8.26 0.01 1 912 . 142 GLN HA H 4.42 0.01 1 913 . 142 GLN HB2 H 2.20 0.01 2 914 . 142 GLN HB3 H 2.12 0.01 2 915 . 142 GLN HG2 H 2.34 0.01 2 916 . 142 GLN HG3 H 2.27 0.01 2 917 . 142 GLN HE21 H 7.50 0.01 1 918 . 142 GLN HE22 H 6.90 0.01 1 919 . 142 GLN N N 118.9 0.1 1 920 . 142 GLN NE2 N 112.8 0.1 1 921 . 143 GLY H H 8.61 0.01 1 922 . 143 GLY HA2 H 4.42 0.01 2 923 . 143 GLY HA3 H 3.97 0.01 2 924 . 143 GLY N N 109.5 0.1 1 925 . 144 GLU H H 8.67 0.01 1 926 . 144 GLU HA H 4.32 0.01 1 927 . 144 GLU HB2 H 2.08 0.01 2 928 . 144 GLU HG2 H 2.41 0.01 2 929 . 144 GLU N N 124.0 0.1 1 930 . 145 LEU H H 8.37 0.01 1 931 . 145 LEU HA H 4.42 0.01 1 932 . 145 LEU HB2 H 1.62 0.01 2 933 . 145 LEU HB3 H 0.96 0.01 2 934 . 145 LEU HG H 1.07 0.01 1 935 . 145 LEU HD1 H 0.76 0.01 1 936 . 145 LEU HD2 H 0.10 0.01 1 937 . 145 LEU N N 123.5 0.1 1 938 . 146 LYS H H 8.14 0.01 1 939 . 146 LYS HA H 4.60 0.01 1 940 . 146 LYS HB2 H 1.89 0.01 2 941 . 146 LYS HB3 H 1.71 0.01 2 942 . 146 LYS HG2 H 1.42 0.01 2 943 . 146 LYS HG3 H 1.36 0.01 2 944 . 146 LYS N N 121.2 0.1 1 945 . 147 LEU H H 8.69 0.01 1 946 . 147 LEU HA H 4.35 0.01 1 947 . 147 LEU HB2 H 1.96 0.01 2 948 . 147 LEU HB3 H 1.31 0.01 2 949 . 147 LEU HG H 2.54 0.01 1 950 . 147 LEU HD1 H 1.16 0.01 1 951 . 147 LEU HD2 H 1.11 0.01 1 952 . 147 LEU N N 125.1 0.1 1 953 . 148 CYS H H 8.80 0.01 1 954 . 148 CYS HA H 5.09 0.01 1 955 . 148 CYS HB2 H 3.80 0.01 1 956 . 148 CYS HB3 H 3.35 0.01 1 957 . 148 CYS N N 127.7 0.1 1 958 . 149 SER H H 8.77 0.01 1 959 . 149 SER HA H 4.76 0.01 1 960 . 149 SER HB2 H 4.07 0.01 2 961 . 149 SER N N 116.7 0.1 1 962 . 150 HIS H H 7.88 0.01 1 963 . 150 HIS HA H 4.49 0.01 1 964 . 150 HIS HB2 H 2.30 0.01 2 965 . 150 HIS HB3 H 1.47 0.01 2 966 . 150 HIS HD2 H 6.17 0.01 1 967 . 150 HIS HE1 H 8.53 0.01 1 968 . 150 HIS N N 123.3 0.1 1 stop_ save_