data_5040 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-1--a Protein Inhibitor of Protein Phosphatase-1 ; _BMRB_accession_number 5040 _BMRB_flat_file_name bmr5040.str _Entry_type original _Submission_date 2001-06-05 _Accession_date 2001-06-05 _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 Chyan Chia-lin . . 2 Tang Tzu-Chun . . 3 Chen Yi-chen . . 4 Liu Hsin-tzu . . 5 Lin Fang-Min . . 6 Liu Chen-Kung . . 7 Hsieh Meng-Juei . . 8 Shiao Ming-Shi . . 9 Huang Hsien-bin . . 10 Lin Ta-Hsien . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 550 "13C chemical shifts" 492 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-01-23 original author . stop_ _Original_release_date 2002-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-1--a Protein Inhibitor of Protein Phosphatase-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21631522 _PubMed_ID 11775747 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chyan Chia-lin . . 2 Tang Tzu-Chun . . 3 Chen Yi-chen . . 4 Liu Hsin-tzu . . 5 Lin Fang-Min . . 6 Liu Chen-Kung . . 7 Hsieh Meng-Juei . . 8 Shiao Ming-Shi . . 9 Huang Hsien-bin . . 10 Lin Ta-Hsien . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 287 _Page_last 288 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_I1(I29T) _Saveframe_category molecular_system _Mol_system_name 'I1(I29T) monomer' _Abbreviation_common I1(I29T) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'I1(I29T) mononer' $I1(I29T)_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_I1(I29T)_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'protein phosphatase inhibitor 1(I29T)' _Abbreviation_common I1(I29T) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 171 _Mol_residue_sequence ; MEQDNSPRKIQFTVPLLEPH LDPEAAEQTRRRRPTPATLV LTSDQSSPEIDEDRIPNPHL KSTLAMSPRQRKKMTRITPT MKELQMMVEHHLGQQQQGEE PEGAAESTGTQESRPPGIPD TEVESRLGTSGTAKKTAECI PKTHERGSKEPSTKEPSTHI PPLDSKGANSV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 GLN 4 ASP 5 ASN 6 SER 7 PRO 8 ARG 9 LYS 10 ILE 11 GLN 12 PHE 13 THR 14 VAL 15 PRO 16 LEU 17 LEU 18 GLU 19 PRO 20 HIS 21 LEU 22 ASP 23 PRO 24 GLU 25 ALA 26 ALA 27 GLU 28 GLN 29 THR 30 ARG 31 ARG 32 ARG 33 ARG 34 PRO 35 THR 36 PRO 37 ALA 38 THR 39 LEU 40 VAL 41 LEU 42 THR 43 SER 44 ASP 45 GLN 46 SER 47 SER 48 PRO 49 GLU 50 ILE 51 ASP 52 GLU 53 ASP 54 ARG 55 ILE 56 PRO 57 ASN 58 PRO 59 HIS 60 LEU 61 LYS 62 SER 63 THR 64 LEU 65 ALA 66 MET 67 SER 68 PRO 69 ARG 70 GLN 71 ARG 72 LYS 73 LYS 74 MET 75 THR 76 ARG 77 ILE 78 THR 79 PRO 80 THR 81 MET 82 LYS 83 GLU 84 LEU 85 GLN 86 MET 87 MET 88 VAL 89 GLU 90 HIS 91 HIS 92 LEU 93 GLY 94 GLN 95 GLN 96 GLN 97 GLN 98 GLY 99 GLU 100 GLU 101 PRO 102 GLU 103 GLY 104 ALA 105 ALA 106 GLU 107 SER 108 THR 109 GLY 110 THR 111 GLN 112 GLU 113 SER 114 ARG 115 PRO 116 PRO 117 GLY 118 ILE 119 PRO 120 ASP 121 THR 122 GLU 123 VAL 124 GLU 125 SER 126 ARG 127 LEU 128 GLY 129 THR 130 SER 131 GLY 132 THR 133 ALA 134 LYS 135 LYS 136 THR 137 ALA 138 GLU 139 CYS 140 ILE 141 PRO 142 LYS 143 THR 144 HIS 145 GLU 146 ARG 147 GLY 148 SER 149 LYS 150 GLU 151 PRO 152 SER 153 THR 154 LYS 155 GLU 156 PRO 157 SER 158 THR 159 HIS 160 ILE 161 PRO 162 PRO 163 LEU 164 ASP 165 SER 166 LYS 167 GLY 168 ALA 169 ASN 170 SER 171 VAL 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 DBJ BAE90004 "unnamed protein product [Macaca fascicularis]" 100.00 171 97.08 97.66 2.60e-112 EMBL CAG33284 "PPP1R1A [Homo sapiens]" 100.00 171 99.42 99.42 2.40e-116 GB AAB02402 "protein phosphatase-1 inhibitor [Homo sapiens]" 100.00 171 99.42 99.42 2.40e-116 GB AAH22470 "Protein phosphatase 1, regulatory (inhibitor) subunit 1A [Homo sapiens]" 100.00 171 98.83 99.42 1.46e-115 GB AAL48320 "inhibitor-1 [Canis lupus familiaris]" 100.00 171 98.83 98.83 1.74e-115 GB AAL48321 "inhibitor-1 [Homo sapiens]" 100.00 171 98.83 98.83 1.56e-115 GB AAV38794 "protein phosphatase 1, regulatory (inhibitor) subunit 1A [synthetic construct]" 100.00 172 98.83 98.83 4.96e-115 REF NP_001003062 "protein phosphatase 1 regulatory subunit 1A [Canis lupus familiaris]" 100.00 171 98.83 98.83 1.74e-115 REF NP_001253895 "protein phosphatase 1 regulatory subunit 1A [Macaca mulatta]" 100.00 171 97.08 97.66 2.60e-112 REF NP_001271621 "uncharacterized protein LOC101925798 [Macaca fascicularis]" 100.00 171 97.08 97.66 2.60e-112 REF NP_006732 "protein phosphatase 1 regulatory subunit 1A [Homo sapiens]" 100.00 171 99.42 99.42 2.40e-116 REF XP_003807647 "PREDICTED: protein phosphatase 1 regulatory subunit 1A, partial [Pan paniscus]" 91.81 157 98.73 98.73 1.37e-103 SP Q13522 "RecName: Full=Protein phosphatase 1 regulatory subunit 1A; AltName: Full=Protein phosphatase inhibitor 1; Short=I-1; Short=IPP-" 100.00 171 98.83 98.83 6.37e-115 SP Q8WMS3 "RecName: Full=Protein phosphatase 1 regulatory subunit 1A; AltName: Full=Protein phosphatase inhibitor 1; Short=I-1; Short=IPP-" 100.00 171 98.83 98.83 1.74e-115 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 $I1(I29T)_monomer 'E. coli' 562 Bacteria . Escherichia coli BL21(DE3) 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 $I1(I29T)_monomer 'recombinant technology' . . . . plasmid pET28a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $I1(I29T)_monomer . mM 1.0 1.5 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_aurelia _Saveframe_category software _Name AURELIA _Version 2.5 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details ; It is equipped with a 5 mm inverse triple resonance (1H/13C/BB), Z-axis gradient probe. ; save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_15N-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.2 n/a temperature 293 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_cs_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'I1(I29T) mononer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU HA H 4.05 0.01 1 2 . 2 GLU HB2 H 1.77 0.01 1 3 . 2 GLU HB3 H 1.64 0.01 1 4 . 2 GLU C C 176.1 0.2 1 5 . 2 GLU CA C 56.6 0.2 1 6 . 2 GLU CB C 30.0 0.2 1 7 . 3 GLN H H 8.63 0.01 1 8 . 3 GLN HA H 4.01 0.01 1 9 . 3 GLN HB2 H 1.79 0.01 1 10 . 3 GLN HB3 H 1.69 0.01 1 11 . 3 GLN C C 175.5 0.2 1 12 . 3 GLN CA C 55.6 0.2 1 13 . 3 GLN CB C 29.4 0.2 1 14 . 3 GLN N N 121.3 0.2 1 15 . 4 ASP H H 8.44 0.01 1 16 . 4 ASP HA H 4.29 0.01 1 17 . 4 ASP HB2 H 1.79 0.01 1 18 . 4 ASP HB3 H 1.69 0.01 1 19 . 4 ASP C C 176.0 0.2 1 20 . 4 ASP CA C 54.1 0.2 1 21 . 4 ASP CB C 41.0 0.2 1 22 . 4 ASP N N 121.8 0.2 1 23 . 5 ASN H H 8.5 0.01 1 24 . 5 ASN HA H 4.5 0.01 1 25 . 5 ASN HB2 H 2.60 0.01 1 26 . 5 ASN HB3 H 2.50 0.01 1 27 . 5 ASN C C 175.1 0.2 1 28 . 5 ASN CA C 52.8 0.2 1 29 . 5 ASN CB C 38.6 0.2 1 30 . 5 ASN N N 120.3 0.2 1 31 . 6 SER H H 8.2 0.01 1 32 . 6 SER HA H 4.4 0.01 1 33 . 6 SER HB2 H 3.6 0.01 2 34 . 6 SER C C 172.7 0.2 1 35 . 6 SER CA C 56.9 0.2 1 36 . 6 SER CB C 62.9 0.2 1 37 . 6 SER N N 117.5 0.2 1 38 . 7 PRO HA H 4.1 0.01 1 39 . 7 PRO HB2 H 2.00 0.01 1 40 . 7 PRO HB3 H 1.60 0.01 1 41 . 7 PRO C C 176.9 0.2 1 42 . 7 PRO CA C 63.4 0.2 1 43 . 7 PRO CB C 31.8 0.2 1 44 . 8 ARG H H 8.35 0.01 1 45 . 8 ARG HA H 3.99 0.01 1 46 . 8 ARG HB2 H 1.49 0.01 2 47 . 8 ARG C C 176.2 0.2 1 48 . 8 ARG CA C 55.7 0.2 1 49 . 8 ARG CB C 30.8 0.2 1 50 . 8 ARG N N 121.06 0.2 1 51 . 9 LYS H H 8.32 0.01 1 52 . 9 LYS HA H 4.01 0.01 1 53 . 9 LYS HB2 H 1.47 0.01 2 54 . 9 LYS C C 176.4 0.2 1 55 . 9 LYS CA C 56.1 0.2 1 56 . 9 LYS CB C 32.8 0.2 1 57 . 9 LYS N N 123.0 0.2 1 58 . 10 ILE H H 8.18 0.01 1 59 . 10 ILE HA H 3.79 0.01 1 60 . 10 ILE HB H 1.48 0.01 1 61 . 10 ILE C C 175.8 0.2 1 62 . 10 ILE CA C 60.9 0.2 1 63 . 10 ILE CB C 38.5 0.2 1 64 . 10 ILE N N 122.7 0.2 1 65 . 11 GLN H H 8.38 0.01 1 66 . 11 GLN HA H 4.02 0.01 1 67 . 11 GLN HB2 H 1.59 0.01 1 68 . 11 GLN HB3 H 1.67 0.01 1 69 . 11 GLN C C 175.2 0.2 1 70 . 11 GLN CA C 55.3 0.2 1 71 . 11 GLN CB C 29.5 0.2 1 72 . 11 GLN N N 124.1 0.2 1 73 . 12 PHE H H 8.3 0.01 1 74 . 12 PHE HA H 4.41 0.01 1 75 . 12 PHE HB2 H 2.85 0.01 1 76 . 12 PHE HB3 H 2.71 0.01 1 77 . 12 PHE C C 175.5 0.2 1 78 . 12 PHE CA C 57.2 0.2 1 79 . 12 PHE CB C 39.6 0.2 1 80 . 12 PHE N N 122.9 0.2 1 81 . 13 THR H H 8.14 0.01 1 82 . 13 THR HA H 4.02 0.01 1 83 . 13 THR HB H 3.79 0.01 1 84 . 13 THR C C 173.6 0.2 1 85 . 13 THR CA C 61.3 0.2 1 86 . 13 THR CB C 69.8 0.2 1 87 . 13 THR N N 116.9 0.2 1 88 . 14 VAL H H 8.17 0.01 1 89 . 14 VAL HA H 4.04 0.01 1 90 . 14 VAL HB H 1.79 0.01 1 91 . 14 VAL C C 177.7 0.2 1 92 . 14 VAL CA C 59.7 0.2 1 93 . 14 VAL CB C 32.4 0.2 1 94 . 14 VAL N N 123.8 0.2 1 95 . 15 PRO HA H 4.08 0.01 1 96 . 15 PRO HB2 H 1.97 0.01 1 97 . 15 PRO HB3 H 1.56 0.01 1 98 . 15 PRO C C 176.5 0.2 1 99 . 15 PRO CA C 63.0 0.2 1 100 . 15 PRO CB C 31.9 0.2 1 101 . 16 LEU H H 8.26 0.01 1 102 . 16 LEU HA H 4.01 0.01 1 103 . 16 LEU HB2 H 1.28 0.01 2 104 . 16 LEU C C 177.1 0.2 1 105 . 16 LEU CA C 54.9 0.2 1 106 . 16 LEU CB C 42.2 0.2 1 107 . 16 LEU N N 122.5 0.2 1 108 . 17 LEU H H 8.21 0.01 1 109 . 17 LEU HA H 4.08 0.01 1 110 . 17 LEU HB2 H 1.28 0.01 2 111 . 17 LEU C C 176.8 0.2 1 112 . 17 LEU CA C 54.5 0.2 1 113 . 17 LEU CB C 42.2 0.2 1 114 . 17 LEU N N 123.3 0.2 1 115 . 18 GLU H H 8.29 0.01 1 116 . 18 GLU HA H 4.27 0.01 1 117 . 18 GLU HB2 H 1.72 0.01 1 118 . 18 GLU HB3 H 1.58 0.01 1 119 . 18 GLU C C 174.3 0.2 1 120 . 18 GLU CA C 54.1 0.2 1 121 . 18 GLU CB C 29.7 0.2 1 122 . 18 GLU N N 123.2 0.2 1 123 . 19 PRO HA H 4.07 0.01 1 124 . 19 PRO HB2 H 1.94 0.01 1 125 . 19 PRO HB3 H 1.52 0.01 1 126 . 19 PRO C C 176.6 0.2 1 127 . 19 PRO CA C 63.1 0.2 1 128 . 19 PRO CB C 31.9 0.2 1 129 . 20 HIS H H 8.58 0.01 1 130 . 20 HIS HA H 4.35 0.01 1 131 . 20 HIS HB2 H 2.88 0.01 2 132 . 20 HIS C C 174.2 0.2 1 133 . 20 HIS CA C 55.3 0.2 1 134 . 20 HIS CB C 29.2 0.2 1 135 . 20 HIS N N 118.8 0.2 1 136 . 21 LEU H H 8.25 0.01 1 137 . 21 LEU HA H 4.06 0.01 1 138 . 21 LEU HB2 H 1.24 0.01 2 139 . 21 LEU C C 176.4 0.2 1 140 . 21 LEU CA C 54.6 0.2 1 141 . 21 LEU CB C 42.6 0.2 1 142 . 21 LEU N N 124.2 0.2 1 143 . 22 ASP H H 8.4 0.2 1 144 . 22 ASP HA H 4.08 0.01 1 145 . 22 ASP HB2 H 2.51 0.01 1 146 . 22 ASP HB3 H 2.31 0.01 1 147 . 22 ASP C C 174.9 0.2 1 148 . 22 ASP CA C 52.0 0.2 1 149 . 22 ASP CB C 41.1 0.2 1 150 . 22 ASP N N 123.1 0.2 1 151 . 23 PRO HA H 4.07 0.01 1 152 . 23 PRO HB2 H 2.04 0.01 1 153 . 23 PRO HB3 H 1.70 0.01 1 154 . 23 PRO C C 178.0 0.2 1 155 . 23 PRO CA C 64.2 0.2 1 156 . 23 PRO CB C 32.0 0.2 1 157 . 24 GLU H H 8.45 0.01 1 158 . 24 GLU HA H 3.93 0.01 1 159 . 24 GLU HB2 H 1.80 0.01 1 160 . 24 GLU HB3 H 1.70 0.01 1 161 . 24 GLU C C 177.3 0.2 1 162 . 24 GLU CA C 57.2 0.2 1 163 . 24 GLU CB C 29.4 0.2 1 164 . 24 GLU N N 118.8 0.2 1 165 . 25 ALA H H 7.96 0.01 1 166 . 25 ALA HA H 3.93 0.01 1 167 . 25 ALA HB H 1.16 0.01 1 168 . 25 ALA C C 178.8 0.2 1 169 . 25 ALA CA C 53.3 0.2 1 170 . 25 ALA CB C 18.7 0.2 1 171 . 25 ALA N N 123.6 0.2 1 172 . 26 ALA H H 8.23 0.01 1 173 . 26 ALA HA H 3.89 0.01 1 174 . 26 ALA HB H 1.13 0.01 1 175 . 26 ALA C C 179.0 0.2 1 176 . 26 ALA CA C 53.4 0.2 1 177 . 26 ALA CB C 18.6 0.2 1 178 . 26 ALA N N 122.2 0.2 1 179 . 27 GLU H H 8.24 0.01 1 180 . 27 GLU HA H 3.89 0.01 1 181 . 27 GLU HB2 H 1.76 0.01 2 182 . 27 GLU C C 177.7 0.2 1 183 . 27 GLU CA C 57.5 0.2 1 184 . 27 GLU CB C 29.2 0.2 1 185 . 27 GLU N N 119.2 0.2 1 186 . 28 GLN H H 8.24 0.01 1 187 . 28 GLN HA H 3.90 0.01 1 188 . 28 GLN HB2 H 1.83 0.01 2 189 . 28 GLN C C 177.4 0.2 1 190 . 28 GLN CA C 57.2 0.2 1 191 . 28 GLN CB C 28.6 0.2 1 192 . 28 GLN N N 119.2 0.2 1 193 . 29 THR H H 8 0.01 1 194 . 29 THR HA H 3.95 0.01 1 195 . 29 THR HB H 3.88 0.01 1 196 . 29 THR C C 175.3 0.2 1 197 . 29 THR CA C 63.4 0.2 1 198 . 29 THR CB C 69.1 0.2 1 199 . 29 THR N N 113.3 0.2 1 200 . 30 ARG H H 8.02 0.01 1 201 . 30 ARG HA H 3.96 0.01 1 202 . 30 ARG HB2 H 1.54 0.01 2 203 . 30 ARG C C 176.7 0.2 1 204 . 30 ARG CA C 56.9 0.2 1 205 . 30 ARG CB C 30.3 0.2 1 206 . 30 ARG N N 122.1 0.2 1 207 . 31 ARG H H 8.08 0.01 1 208 . 31 ARG HA H 3.98 0.01 1 209 . 31 ARG HB2 H 1.51 0.01 2 210 . 31 ARG C C 176.3 0.2 1 211 . 31 ARG CA C 56.2 0.2 1 212 . 31 ARG CB C 30.5 0.2 1 213 . 31 ARG N N 120.3 0.2 1 214 . 32 ARG H H 8.15 0.01 1 215 . 32 ARG HA H 4.02 0.01 1 216 . 32 ARG HB2 H 1.55 0.01 1 217 . 32 ARG HB3 H 1.49 0.01 1 218 . 32 ARG C C 176.0 0.2 1 219 . 32 ARG CA C 55.8 0.2 1 220 . 32 ARG CB C 30.7 0.2 1 221 . 32 ARG N N 121.5 0.2 1 222 . 33 ARG H H 8.34 0.01 1 223 . 33 ARG HA H 4.32 0.01 1 224 . 33 ARG HB2 H 1.51 0.01 2 225 . 33 ARG C C 174.1 0.2 1 226 . 33 ARG CA C 53.8 0.2 1 227 . 33 ARG CB C 30.1 0.2 1 228 . 33 ARG N N 123.6 0.2 1 229 . 34 PRO HA H 4.19 0.01 1 230 . 34 PRO HB2 H 1.99 0.01 1 231 . 34 PRO HB3 H 1.59 0.01 1 232 . 34 PRO C C 176.7 0.2 1 233 . 34 PRO CA C 62.9 0.2 1 234 . 34 PRO CB C 31.9 0.2 1 235 . 35 THR H H 8.34 0.01 1 236 . 35 THR HA H 4.27 0.01 1 237 . 35 THR HB H 3.87 0.01 1 238 . 35 THR C C 172.9 0.2 1 239 . 35 THR CA C 59.9 0.2 1 240 . 35 THR CB C 69.6 0.2 1 241 . 35 THR N N 117.2 0.2 1 242 . 36 PRO HA H 4.07 0.01 1 243 . 36 PRO HB2 H 2.03 0.01 1 244 . 36 PRO HB3 H 1.64 0.01 1 245 . 36 PRO C C 176.7 0.2 1 246 . 36 PRO CA C 63.1 0.2 1 247 . 36 PRO CB C 32.1 0.2 1 248 . 37 ALA H H 8.43 0.01 1 249 . 37 ALA HA H 4.02 0.01 1 250 . 37 ALA HB H 1.11 0.01 1 251 . 37 ALA C C 178.0 0.2 1 252 . 37 ALA CA C 52.6 0.2 1 253 . 37 ALA CB C 19.0 0.2 1 254 . 37 ALA N N 123.9 0.2 1 255 . 38 THR H H 8.03 0.01 1 256 . 38 THR HA H 3.98 0.01 1 257 . 38 THR HB H 3.88 0.01 1 258 . 38 THR C C 174.2 0.2 1 259 . 38 THR CA C 61.6 0.2 1 260 . 38 THR CB C 69.4 0.2 1 261 . 38 THR N N 113.0 0.2 1 262 . 39 LEU H H 8.19 0.01 1 263 . 39 LEU HA H 4.08 0.01 1 264 . 39 LEU HB2 H 1.30 0.01 2 265 . 39 LEU C C 176.7 0.2 1 266 . 39 LEU CA C 55.1 0.2 1 267 . 39 LEU CB C 42.4 0.2 1 268 . 39 LEU N N 124.8 0.2 1 269 . 40 VAL H H 8.14 0.01 1 270 . 40 VAL HA H 3.79 0.01 1 271 . 40 VAL HB H 1.74 0.01 1 272 . 40 VAL C C 175.9 0.2 1 273 . 40 VAL CA C 62.0 0.2 1 274 . 40 VAL CB C 32.5 0.2 1 275 . 40 VAL N N 122.3 0.2 1 276 . 41 LEU H H 8.42 0.01 1 277 . 41 LEU HA H 4.19 0.01 1 278 . 41 LEU HB2 H 1.37 0.01 1 279 . 41 LEU HB3 H 1.30 0.01 1 280 . 41 LEU C C 177.5 0.2 1 281 . 41 LEU CA C 54.8 0.2 1 282 . 41 LEU CB C 42.3 0.2 1 283 . 41 LEU N N 126.6 0.2 1 284 . 42 THR H H 8.17 0.01 1 285 . 42 THR HA H 4.11 0.01 1 286 . 42 THR HB H 4.00 0.01 1 287 . 42 THR C C 174.6 0.2 1 288 . 42 THR CA C 61.3 0.2 1 289 . 42 THR CB C 69.7 0.2 1 290 . 42 THR N N 114.4 0.2 1 291 . 43 SER H H 8.36 0.01 1 292 . 43 SER HA H 4.17 0.01 1 293 . 43 SER HB2 H 3.61 0.01 1 294 . 43 SER HB3 H 3.56 0.01 1 295 . 43 SER C C 174.3 0.2 1 296 . 43 SER CA C 58.2 0.2 1 297 . 43 SER CB C 63.7 0.2 1 298 . 43 SER N N 117.3 0.2 1 299 . 44 ASP H H 8.4 0.01 1 300 . 44 ASP HA H 4.32 0.01 1 301 . 44 ASP HB2 H 2.40 0.01 2 302 . 44 ASP C C 176.2 0.2 1 303 . 44 ASP CA C 54.3 0.2 1 304 . 44 ASP CB C 40.8 0.2 1 305 . 44 ASP N N 122.1 0.2 1 306 . 45 GLN H H 8.29 0.01 1 307 . 45 GLN HA H 4.07 0.01 1 308 . 45 GLN HB2 H 1.89 0.01 1 309 . 45 GLN HB3 H 1.69 0.01 1 310 . 45 GLN C C 178.2 0.2 1 311 . 45 GLN CA C 55.7 0.2 1 312 . 45 GLN CB C 29.2 0.2 1 313 . 45 GLN N N 120.2 0.2 1 314 . 46 SER H H 8.34 0.01 1 315 . 46 SER HA H 4.16 0.01 1 316 . 46 SER HB2 H 3.57 0.01 2 317 . 46 SER C C 174.1 0.2 1 318 . 46 SER CA C 58.4 0.2 1 319 . 46 SER CB C 63.7 0.2 1 320 . 46 SER N N 116.8 0.2 1 321 . 47 SER H H 8.34 0.01 1 322 . 47 SER HA H 4.49 0.01 1 323 . 47 SER HB2 H 3.56 0.01 2 324 . 47 SER C C 172.7 0.2 1 325 . 47 SER CA C 56.3 0.2 1 326 . 47 SER CB C 63.3 0.2 1 327 . 47 SER N N 118.7 0.2 1 328 . 48 PRO HA H 3.98 0.01 1 329 . 48 PRO HB2 H 1.98 0.01 1 330 . 48 PRO HB3 H 1.63 0.01 1 331 . 48 PRO C C 176.8 0.2 1 332 . 48 PRO CA C 63.4 0.2 1 333 . 48 PRO CB C 32.0 0.2 1 334 . 49 GLU H H 8.51 0.01 1 335 . 49 GLU HA H 3.97 0.01 1 336 . 49 GLU HB2 H 1.72 0.01 1 337 . 49 GLU HB3 H 1.61 0.01 1 338 . 49 GLU C C 176.4 0.2 1 339 . 49 GLU CA C 56.7 0.2 1 340 . 49 GLU CB C 29.7 0.2 1 341 . 49 GLU N N 120.6 0.2 1 342 . 50 ILE H H 8.13 0.01 1 343 . 50 ILE HA H 3.88 0.01 1 344 . 50 ILE HB H 1.57 0.01 1 345 . 50 ILE C C 175.75 0.2 1 346 . 50 ILE CA C 60.9 0.2 1 347 . 50 ILE CB C 38.9 0.2 1 348 . 50 ILE N N 121.2 0.2 1 349 . 51 ASP H H 8.38 0.01 1 350 . 51 ASP HA H 4.32 0.01 1 351 . 51 ASP HB2 H 2.43 0.01 1 352 . 51 ASP HB3 H 2.30 0.01 1 353 . 51 ASP C C 175.2 0.2 1 354 . 51 ASP CA C 54.2 0.2 1 355 . 51 ASP CB C 41.1 0.2 1 356 . 51 ASP N N 124.4 0.2 1 357 . 52 GLU H H 8.47 0.01 1 358 . 52 GLU HA H 3.90 0.01 1 359 . 52 GLU HB2 H 1.77 0.01 1 360 . 52 GLU HB3 H 1.66 0.01 1 361 . 52 GLU C C 176.4 0.2 1 362 . 52 GLU CA C 57.2 0.2 1 363 . 52 GLU CB C 30.0 0.2 1 364 . 52 GLU N N 121.8 0.2 1 365 . 53 ASP H H 8.39 0.01 1 366 . 53 ASP HA H 4.29 0.01 1 367 . 53 ASP HB2 H 2.41 0.01 1 368 . 53 ASP HB3 H 2.35 0.01 1 369 . 53 ASP C C 176.3 0.2 1 370 . 53 ASP CA C 54.6 0.2 1 371 . 53 ASP CB C 40.7 0.2 1 372 . 53 ASP N N 119.9 0.2 1 373 . 54 ARG H H 8.02 0.01 1 374 . 54 ARG HA H 4.01 0.01 1 375 . 54 ARG HB2 H 1.46 0.01 1 376 . 54 ARG HB3 H 1.58 0.01 1 377 . 54 ARG C C 176.0 0.2 1 378 . 54 ARG CA C 56.0 0.2 1 379 . 54 ARG CB C 30.5 0.2 1 380 . 54 ARG N N 119.9 0.2 1 381 . 55 ILE H H 8 0.01 1 382 . 55 ILE HA H 4.12 0.01 1 383 . 55 ILE HB H 1.59 0.01 1 384 . 55 ILE C C 174.5 0.2 1 385 . 55 ILE CA C 58.7 0.2 1 386 . 55 ILE CB C 38.2 0.2 1 387 . 55 ILE N N 122.4 0.2 1 388 . 56 PRO HA H 4.07 0.01 1 389 . 56 PRO HB2 H 1.95 0.01 1 390 . 56 PRO HB3 H 1.55 0.01 1 391 . 56 PRO C C 176.2 0.2 1 392 . 56 PRO CA C 63.1 0.2 1 393 . 56 PRO CB C 31.8 0.2 1 394 . 57 ASN H H 8.46 0.01 1 395 . 57 ASN HA H 4.63 0.01 1 396 . 57 ASN HB2 H 2.54 0.01 1 397 . 57 ASN HB3 H 2.48 0.01 1 398 . 57 ASN C C 174.0 0.2 1 399 . 57 ASN CA C 51.0 0.2 1 400 . 57 ASN CB C 38.9 0.2 1 401 . 57 ASN N N 119.5 0.2 1 402 . 58 PRO HA H 4.07 0.01 1 403 . 58 PRO HB2 H 1.76 0.01 1 404 . 58 PRO HB3 H 1.65 0.01 1 405 . 58 PRO C C 177.0 0.2 1 406 . 58 PRO CA C 63.5 0.2 1 407 . 58 PRO CB C 30.0 0.2 1 408 . 59 HIS H H 8.4 0.01 1 409 . 59 HIS HA H 4.33 0.01 1 410 . 59 HIS HB2 H 2.85 0.01 1 411 . 59 HIS HB3 H 2.96 0.01 1 412 . 59 HIS C C 175.1 0.2 1 413 . 59 HIS CA C 55.7 0.2 1 414 . 59 HIS CB C 28.9 0.2 1 415 . 59 HIS N N 117.3 0.2 1 416 . 60 LEU H H 7.83 0.01 1 417 . 60 LEU HA H 4.03 0.01 1 418 . 60 LEU HB2 H 1.33 0.01 2 419 . 60 LEU C C 177.2 0.2 1 420 . 60 LEU CA C 55.2 0.2 1 421 . 60 LEU CB C 42.2 0.2 1 422 . 60 LEU N N 121.7 0.2 1 423 . 61 LYS H H 8.31 0.01 1 424 . 61 LYS HA H 4.00 0.01 1 425 . 61 LYS HB2 H 1.56 0.01 1 426 . 61 LYS HB3 H 1.48 0.01 1 427 . 61 LYS C C 176.8 0.2 1 428 . 61 LYS CA C 57.5 0.2 1 429 . 61 LYS CB C 32.9 0.2 1 430 . 61 LYS N N 121.9 0.2 1 431 . 62 SER H H 8.29 0.01 1 432 . 62 SER HA H 4.19 0.01 1 433 . 62 SER HB2 H 3.63 0.01 1 434 . 62 SER HB3 H 3.57 0.01 1 435 . 62 SER C C 175.1 0.2 1 436 . 62 SER CA C 58.3 0.2 1 437 . 62 SER CB C 63.4 0.2 1 438 . 62 SER N N 116.3 0.2 1 439 . 63 THR H H 8.19 0.01 1 440 . 63 THR HA H 4.06 0.01 1 441 . 63 THR HB H 3.92 0.01 1 442 . 63 THR C C 174.8 0.2 1 443 . 63 THR CA C 62.0 0.2 1 444 . 63 THR CB C 69.5 0.2 1 445 . 63 THR N N 116.0 0.2 1 446 . 64 LEU H H 8.13 0.01 1 447 . 64 LEU HA H 4.02 0.01 1 448 . 64 LEU HB2 H 1.31 0.01 2 449 . 64 LEU C C 177.1 0.2 1 450 . 64 LEU CA C 55.3 0.2 1 451 . 64 LEU CB C 42.1 0.2 1 452 . 64 LEU N N 123.7 0.2 1 453 . 65 ALA H H 8.17 0.01 1 454 . 65 ALA HA H 4.01 0.01 1 455 . 65 ALA HB H 1.08 0.01 1 456 . 65 ALA C C 177.5 0.2 1 457 . 65 ALA CA C 52.3 0.2 1 458 . 65 ALA CB C 19.0 0.2 1 459 . 65 ALA N N 124.1 0.2 1 460 . 66 MET H H 8.14 0.01 1 461 . 66 MET HA H 4.19 0.01 1 462 . 66 MET HB2 H 1.75 0.01 1 463 . 66 MET HB3 H 1.70 0.01 1 464 . 66 MET C C 175.9 0.2 1 465 . 66 MET CA C 55.2 0.2 1 466 . 66 MET CB C 33.2 0.2 1 467 . 66 MET N N 118.9 0.2 1 468 . 67 SER H H 8.37 0.01 1 469 . 67 SER HA H 4.47 0.01 1 470 . 67 SER HB2 H 3.61 0.01 1 471 . 67 SER C C 173.0 0.2 1 472 . 67 SER CA C 56.4 0.2 1 473 . 67 SER CB C 63.1 0.2 1 474 . 67 SER N N 118.7 0.2 1 475 . 68 PRO HA H 4.09 0.01 1 476 . 68 PRO HB2 H 2.04 0.01 1 477 . 68 PRO HB3 H 1.64 0.01 1 478 . 68 PRO C C 177.4 0.2 1 479 . 68 PRO CA C 63.9 0.2 1 480 . 68 PRO CB C 32.0 0.2 1 481 . 69 ARG H H 8.35 0.01 1 482 . 69 ARG HA H 3.93 0.01 1 483 . 69 ARG HB2 H 1.52 0.01 2 484 . 69 ARG C C 176.8 0.2 1 485 . 69 ARG CA C 56.8 0.2 1 486 . 69 ARG CB C 30.3 0.2 1 487 . 69 ARG N N 119.7 0.2 1 488 . 70 GLN H H 8.22 0.01 1 489 . 70 GLN HA H 3.99 0.01 1 490 . 70 GLN HB2 H 1.77 0.01 2 491 . 70 GLN C C 176.3 0.2 1 492 . 70 GLN CA C 56.0 0.2 1 493 . 70 GLN CB C 29.3 0.2 1 494 . 70 GLN N N 120.7 0.2 1 495 . 71 ARG H H 8.38 0.01 1 496 . 71 ARG HA H 3.98 0.01 1 497 . 71 ARG HB2 H 1.76 0.01 2 498 . 71 ARG C C 176.6 0.2 1 499 . 71 ARG CA C 56.4 0.2 1 500 . 71 ARG CB C 30.6 0.2 1 501 . 71 ARG N N 122.2 0.2 1 502 . 72 LYS H H 8.37 0.01 1 503 . 72 LYS HA H 4.05 0.01 1 504 . 72 LYS HB2 H 2.01 0.01 1 505 . 72 LYS HB3 H 1.64 0.01 1 506 . 72 LYS C C 176.6 0.2 1 507 . 72 LYS CA C 55.9 0.2 1 508 . 72 LYS CB C 29.3 0.2 1 509 . 72 LYS N N 122.2 0.2 1 510 . 73 LYS H H 8.51 0.01 1 511 . 73 LYS HA H 3.98 0.01 1 512 . 73 LYS HB2 H 2.01 0.01 1 513 . 73 LYS HB3 H 1.52 0.01 1 514 . 73 LYS C C 176.4 0.2 1 515 . 73 LYS CA C 56.4 0.2 1 516 . 73 LYS CB C 30.2 0.2 1 517 . 73 LYS N N 122.2 0.2 1 518 . 74 MET H H 8.41 0.01 1 519 . 74 MET HA H 4.03 0.01 1 520 . 74 MET HB2 H 1.79 0.01 1 521 . 74 MET HB3 H 1.69 0.01 1 522 . 74 MET C C 176.2 0.2 1 523 . 74 MET CA C 55.2 0.2 1 524 . 74 MET CB C 32.8 0.2 1 525 . 74 MET N N 121.8 0.2 1 526 . 75 THR H H 8.18 0.01 1 527 . 75 THR HA H 4.17 0.01 1 528 . 75 THR HB H 3.87 0.01 1 529 . 75 THR C C 174.0 0.2 1 530 . 75 THR CA C 61.7 0.2 1 531 . 75 THR CB C 69.6 0.2 1 532 . 75 THR N N 116.3 0.2 1 533 . 76 ARG H H 8.37 0.01 1 534 . 76 ARG HA H 4.10 0.01 1 535 . 76 ARG HB2 H 1.52 0.01 1 536 . 76 ARG HB3 H 1.45 0.01 1 537 . 76 ARG C C 175.8 0.2 1 538 . 76 ARG CA C 55.9 0.2 1 539 . 76 ARG CB C 30.7 0.2 1 540 . 76 ARG N N 123.8 0.2 1 541 . 77 ILE H H 8.32 0.01 1 542 . 77 ILE HA H 3.96 0.01 1 543 . 77 ILE HB H 1.54 0.01 1 544 . 77 ILE C C 176.1 0.2 1 545 . 77 ILE CA C 60.6 0.2 1 546 . 77 ILE CB C 32.6 0.2 1 547 . 77 ILE N N 122.9 0.2 1 548 . 78 THR H H 8.26 0.01 1 549 . 78 THR HA H 4.33 0.01 1 550 . 78 THR HB H 3.91 0.01 1 551 . 78 THR C C 172.8 0.2 1 552 . 78 THR CA C 59.7 0.2 1 553 . 78 THR CB C 69.3 0.2 1 554 . 78 THR N N 121.1 0.2 1 555 . 79 PRO HA H 4.24 0.01 1 556 . 79 PRO HB2 H 2.01 0.01 1 557 . 79 PRO HB3 H 1.63 0.01 1 558 . 79 PRO C C 177.2 0.2 1 559 . 79 PRO CA C 63.2 0.2 1 560 . 79 PRO CB C 32.1 0.2 1 561 . 80 THR H H 8.36 0.01 1 562 . 80 THR HA H 4.03 0.01 1 563 . 80 THR HB H 4.04 0.01 1 564 . 80 THR C C 175.0 0.2 1 565 . 80 THR CA C 61.6 0.2 1 566 . 80 THR CB C 70.0 0.2 1 567 . 80 THR N N 113.1 0.2 1 568 . 81 MET H H 8.51 0.01 1 569 . 81 MET HA H 4.02 0.01 1 570 . 81 MET HB2 H 1.10 0.01 2 571 . 81 MET C C 177.6 0.2 1 572 . 81 MET CA C 57.3 0.2 1 573 . 81 MET CB C 32.1 0.2 1 574 . 81 MET N N 121.0 0.2 1 575 . 82 LYS H H 8.29 0.01 1 576 . 82 LYS HA H 3.85 0.01 1 577 . 82 LYS HB2 H 1.51 0.01 1 578 . 82 LYS HB3 H 1.52 0.01 1 579 . 82 LYS C C 177.9 0.2 1 580 . 82 LYS CA C 58.1 0.2 1 581 . 82 LYS CB C 32.4 0.2 1 582 . 82 LYS N N 120.5 0.2 1 583 . 83 GLU H H 8.08 0.01 1 584 . 83 GLU HA H 3.79 0.01 1 585 . 83 GLU HB2 H 1.84 0.01 1 586 . 83 GLU HB3 H 1.75 0.01 1 587 . 83 GLU C C 178.2 0.2 1 588 . 83 GLU CA C 58.2 0.2 1 589 . 83 GLU CB C 29.6 0.2 1 590 . 83 GLU N N 120.1 0.2 1 591 . 84 LEU H H 8.22 0.01 1 592 . 84 LEU HA H 3.92 0.01 1 593 . 84 LEU HB2 H 1.49 0.01 1 594 . 84 LEU HB3 H 1.32 0.01 1 595 . 84 LEU C C 178.5 0.2 1 596 . 84 LEU CA C 56.6 0.2 1 597 . 84 LEU CB C 41.8 0.2 1 598 . 84 LEU N N 121.1 0.2 1 599 . 85 GLN H H 8.17 0.01 1 600 . 85 GLN HA H 3.85 0.01 1 601 . 85 GLN HB2 H 1.82 0.01 2 602 . 85 GLN C C 177.2 0.2 1 603 . 85 GLN CA C 57.1 0.2 1 604 . 85 GLN CB C 28.4 0.2 1 605 . 85 GLN N N 119.1 0.2 1 606 . 86 MET H H 8.05 0.01 1 607 . 86 MET HA H 4.07 0.01 1 608 . 86 MET HB2 H 1.83 0.01 2 609 . 86 MET C C 177.1 0.2 1 610 . 86 MET CA C 56.6 0.2 1 611 . 86 MET CB C 32.4 0.2 1 612 . 86 MET N N 118.9 0.2 1 613 . 87 MET H H 8.08 0.01 1 614 . 87 MET HA H 4.07 0.01 1 615 . 87 MET HB2 H 1.84 0.01 2 616 . 87 MET C C 176.3 0.2 1 617 . 87 MET CA C 56.8 0.2 1 618 . 87 MET CB C 32.5 0.2 1 619 . 87 MET N N 119.9 0.2 1 620 . 88 VAL H H 7.98 0.01 1 621 . 88 VAL HA H 3.69 0.01 1 622 . 88 VAL HB H 1.80 0.01 1 623 . 88 VAL C C 176.8 0.2 1 624 . 88 VAL CA C 63.4 0.2 1 625 . 88 VAL CB C 32.5 0.2 1 626 . 88 VAL N N 119.9 0.2 1 627 . 89 GLU H H 8.28 0.01 1 628 . 89 GLU HA H 3.85 0.01 1 629 . 89 GLU HB2 H 1.63 0.01 2 630 . 89 GLU C C 176.6 0.2 1 631 . 89 GLU CA C 57.1 0.2 1 632 . 89 GLU CB C 29.8 0.2 1 633 . 89 GLU N N 122.4 0.2 1 634 . 90 HIS H H 8.29 0.01 1 635 . 90 HIS HA H 4.33 0.01 1 636 . 90 HIS HB2 H 2.87 0.01 1 637 . 90 HIS HB3 H 2.85 0.01 1 638 . 90 HIS C C 174.6 0.2 1 639 . 90 HIS CA C 55.6 0.2 1 640 . 90 HIS CB C 29.4 0.2 1 641 . 90 HIS N N 118.5 0.2 1 642 . 92 LEU H H 8.41 0.01 1 643 . 92 LEU HA H 4.03 0.01 1 644 . 92 LEU HB2 H 1.33 0.01 1 645 . 92 LEU HB3 H 1.25 0.01 1 646 . 92 LEU C C 177.9 0.2 1 647 . 92 LEU CA C 55.3 0.2 1 648 . 92 LEU CB C 42.2 0.2 1 649 . 92 LEU N N 122.4 0.2 1 650 . 93 GLY H H 8.5 0.01 1 651 . 93 GLY HA2 H 3.66 0.01 2 652 . 93 GLY C C 174.2 0.2 1 653 . 93 GLY CA C 45.3 0.2 1 654 . 93 GLY N N 109.5 0.2 1 655 . 94 GLN H H 8.22 0.01 1 656 . 94 GLN HA H 4.03 0.01 1 657 . 94 GLN HB2 H 1.80 0.01 1 658 . 94 GLN HB3 H 1.69 0.01 1 659 . 94 GLN C C 176.1 0.2 1 660 . 94 GLN CA C 55.8 0.2 1 661 . 94 GLN CB C 29.3 0.2 1 662 . 94 GLN N N 119.6 0.2 1 663 . 95 GLN H H 8.53 0.01 1 664 . 95 GLN HA H 4.02 0.01 1 665 . 95 GLN HB2 H 1.80 0.01 1 666 . 95 GLN HB3 H 1.69 0.01 1 667 . 95 GLN C C 176.0 0.2 1 668 . 95 GLN CA C 55.9 0.2 1 669 . 95 GLN CB C 29.2 0.2 1 670 . 95 GLN N N 121.6 0.2 1 671 . 96 GLN H H 8.53 0.01 1 672 . 96 GLN HA H 4.03 0.01 1 673 . 96 GLN HB2 H 1.75 0.01 2 674 . 96 GLN C C 175.8 0.2 1 675 . 96 GLN CA C 55.6 0.2 1 676 . 96 GLN CB C 29.3 0.2 1 677 . 96 GLN N N 121.8 0.2 1 678 . 97 GLN H H 8.55 0.01 1 679 . 97 GLN HA H 4.05 0.01 1 680 . 97 GLN HB2 H 1.77 0.01 2 681 . 97 GLN C C 176.3 0.2 1 682 . 97 GLN CA C 55.9 0.2 1 683 . 97 GLN CB C 29.3 0.2 1 684 . 97 GLN N N 121.8 0.2 1 685 . 98 GLY H H 8.52 0.01 1 686 . 98 GLY HA2 H 3.69 0.01 2 687 . 98 GLY C C 173.8 0.2 1 688 . 98 GLY CA C 45.1 0.2 1 689 . 98 GLY N N 110.6 0.2 1 690 . 99 GLU H H 8.28 0.01 1 691 . 99 GLU HA H 4.04 0.01 1 692 . 99 GLU HB2 H 1.76 0.01 1 693 . 99 GLU HB3 H 1.6 0.01 1 694 . 99 GLU C C 176.3 0.2 1 695 . 99 GLU CA C 56.0 0.2 1 696 . 99 GLU CB C 30.4 0.2 1 697 . 99 GLU N N 120.1 0.2 1 698 . 100 GLU H H 8.54 0.01 1 699 . 100 GLU HA H 4.28 0.01 1 700 . 100 GLU HB2 H 1.67 0.01 1 701 . 100 GLU HB3 H 1.6 0.01 1 702 . 100 GLU C C 174.6 0.2 1 703 . 100 GLU CA C 54.3 0.2 1 704 . 100 GLU CB C 29.4 0.2 1 705 . 100 GLU N N 123.1 0.2 1 706 . 101 PRO HA H 4.12 0.01 1 707 . 101 PRO HB2 H 1.99 0.01 1 708 . 101 PRO HB3 H 1.63 0.01 1 709 . 101 PRO C C 177.0 0.2 1 710 . 101 PRO CA C 63.1 0.2 1 711 . 101 PRO CB C 32.0 0.2 1 712 . 102 GLU H H 8.61 0.01 1 713 . 102 GLU HA H 3.95 0.01 1 714 . 102 GLU HB2 H 1.75 0.01 1 715 . 102 GLU HB3 H 1.67 0.01 1 716 . 102 GLU C C 177.1 0.2 1 717 . 102 GLU CA C 56.8 0.2 1 718 . 102 GLU CB C 30.0 0.2 1 719 . 102 GLU N N 121.3 0.2 1 720 . 103 GLY H H 8.48 0.01 1 721 . 103 GLY HA2 H 3.65 0.01 2 722 . 103 GLY C C 173.8 0.2 1 723 . 103 GLY CA C 45.2 0.2 1 724 . 103 GLY N N 110.3 0.2 1 725 . 104 ALA H H 8.17 0.01 1 726 . 104 ALA HA H 4.02 0.01 1 727 . 104 ALA HB H 1.09 0.01 1 728 . 104 ALA C C 177.7 0.2 1 729 . 104 ALA CA C 52.2 0.2 1 730 . 104 ALA CB C 19.2 0.2 1 731 . 104 ALA N N 123.9 0.2 1 732 . 105 ALA H H 8.37 0.01 1 733 . 105 ALA HA H 4.00 0.01 1 734 . 105 ALA HB H 1.10 0.01 1 735 . 105 ALA C C 178.0 0.2 1 736 . 105 ALA CA C 52.5 0.2 1 737 . 105 ALA CB C 19.1 0.2 1 738 . 105 ALA N N 123.4 0.2 1 739 . 106 GLU H H 8.43 0.01 1 740 . 106 GLU HA H 3.99 0.01 1 741 . 106 GLU HB2 H 1.78 0.01 1 742 . 106 GLU HB3 H 1.67 0.01 1 743 . 106 GLU C C 176.7 0.2 1 744 . 106 GLU CA C 56.6 0.2 1 745 . 106 GLU CB C 30.1 0.2 1 746 . 106 GLU N N 119.9 0.2 1 747 . 107 SER H H 8.4 0.01 1 748 . 107 SER HA H 4.24 0.01 1 749 . 107 SER HB2 H 3.60 0.01 2 750 . 107 SER C C 175.0 0.2 1 751 . 107 SER CA C 58.2 0.2 1 752 . 107 SER CB C 63.6 0.2 1 753 . 107 SER N N 116.7 0.2 1 754 . 108 THR H H 8.27 0.01 1 755 . 108 THR HA H 4.09 0.01 1 756 . 108 THR HB H 4.00 0.01 1 757 . 108 THR C C 175.3 0.2 1 758 . 108 THR CA C 62.0 0.2 1 759 . 108 THR CB C 69.6 0.2 1 760 . 108 THR N N 115.5 0.2 1 761 . 109 GLY H H 8.45 0.01 1 762 . 109 GLY HA2 H 3.75 0.01 2 763 . 109 GLY C C 174.4 0.2 1 764 . 109 GLY CA C 45.4 0.2 1 765 . 109 GLY N N 110.9 0.2 1 766 . 110 THR H H 8.13 0.01 1 767 . 110 THR HA H 4.07 0.01 1 768 . 110 THR HB H 3.95 0.01 1 769 . 110 THR C C 174.4 0.2 1 770 . 110 THR CA C 61.8 0.2 1 771 . 110 THR CB C 69.6 0.2 1 772 . 110 THR N N 113.6 0.2 1 773 . 111 GLN H H 8.54 0.01 1 774 . 111 GLN HA H 4.05 0.01 1 775 . 111 GLN HB2 H 1.83 0.01 1 776 . 111 GLN HB3 H 1.70 0.01 1 777 . 111 GLN C C 176.0 0.2 1 778 . 111 GLN CA C 55.9 0.2 1 779 . 111 GLN CB C 29.2 0.2 1 780 . 111 GLN N N 122.6 0.2 1 781 . 112 GLU H H 8.51 0.01 1 782 . 112 GLU HA H 4.00 0.01 1 783 . 112 GLU HB2 H 1.75 0.01 1 784 . 112 GLU HB3 H 1.65 0.01 1 785 . 112 GLU C C 176.4 0.2 1 786 . 112 GLU CA C 56.6 0.2 1 787 . 112 GLU CB C 30.1 0.2 1 788 . 112 GLU N N 122.2 0.2 1 789 . 113 SER H H 8.39 0.01 1 790 . 113 SER HA H 4.15 0.01 1 791 . 113 SER HB2 H 3.55 0.01 2 792 . 113 SER C C 174.0 0.2 1 793 . 113 SER CA C 58.1 0.2 1 794 . 113 SER CB C 63.5 0.2 1 795 . 113 SER N N 117.5 0.2 1 796 . 114 ARG H H 8.34 0.01 1 797 . 114 ARG HA H 4.37 0.01 1 798 . 114 ARG HB2 H 1.52 0.01 1 799 . 114 ARG HB3 H 1.42 0.01 1 800 . 114 ARG C C 173.7 0.2 1 801 . 114 ARG CA C 53.8 0.2 1 802 . 114 ARG CB C 30.2 0.2 1 803 . 114 ARG N N 124.1 0.2 1 804 . 116 PRO HA H 4.13 0.01 1 805 . 116 PRO HB2 H 2.00 0.01 1 806 . 116 PRO HB3 H 1.64 0.01 1 807 . 116 PRO C C 177.5 0.2 1 808 . 116 PRO CA C 63.1 0.2 1 809 . 116 PRO CB C 31.9 0.2 1 810 . 117 GLY H H 8.42 0.01 1 811 . 117 GLY HA2 H 3.62 0.01 2 812 . 117 GLY C C 173.7 0.2 1 813 . 117 GLY CA C 45.1 0.2 1 814 . 117 GLY N N 108.6 0.2 1 815 . 118 ILE H H 7.97 0.01 1 816 . 118 ILE HA H 4.20 0.01 1 817 . 118 ILE HB H 1.58 0.01 1 818 . 118 ILE C C 174.6 0.2 1 819 . 118 ILE CA C 58.4 0.2 1 820 . 118 ILE CB C 38.3 0.2 1 821 . 118 ILE N N 121.5 0.2 1 822 . 119 PRO HA H 4.15 0.01 1 823 . 119 PRO HB2 H 2.00 0.01 1 824 . 119 PRO HB3 H 1.63 0.01 1 825 . 119 PRO C C 176.8 0.2 1 826 . 119 PRO CA C 63.3 0.2 1 827 . 119 PRO CB C 32.0 0.2 1 828 . 120 ASP H H 8.51 0.01 1 829 . 120 ASP HA H 4.29 0.01 1 830 . 120 ASP HB2 H 2.45 0.01 1 831 . 120 ASP HB3 H 2.35 0.01 1 832 . 120 ASP C C 176.7 0.2 1 833 . 120 ASP CA C 54.6 0.2 1 834 . 120 ASP CB C 40.8 0.2 1 835 . 120 ASP N N 120.8 0.2 1 836 . 121 THR H H 8.04 0.01 1 837 . 121 THR HA H 3.98 0.01 1 838 . 121 THR HB H 3.9 0.01 1 839 . 121 THR C C 175.0 0.2 1 840 . 121 THR CA C 62.0 0.2 1 841 . 121 THR CB C 69.4 0.2 1 842 . 121 THR N N 113.1 0.2 1 843 . 122 GLU H H 8.39 0.01 1 844 . 122 GLU HA H 4.28 0.01 1 845 . 122 GLU HB2 H 1.80 0.01 1 846 . 122 GLU HB3 H 1.69 0.01 1 847 . 122 GLU C C 176.9 0.2 1 848 . 122 GLU CA C 56.7 0.2 1 849 . 122 GLU CB C 29.8 0.2 1 850 . 122 GLU N N 122.9 0.2 1 851 . 123 VAL H H 8.03 0.01 1 852 . 123 VAL HA H 3.68 0.01 1 853 . 123 VAL HB H 1.75 0.01 1 854 . 123 VAL C C 176.7 0.2 1 855 . 123 VAL CA C 63.2 0.2 1 856 . 123 VAL CB C 32.5 0.2 1 857 . 123 VAL N N 120.6 0.2 1 858 . 124 GLU H H 8.4 0.01 1 859 . 124 GLU HA H 3.92 0.01 1 860 . 124 GLU HB2 H 1.73 0.01 2 861 . 124 GLU C C 174.2 0.2 1 862 . 124 GLU CA C 57.1 0.2 1 863 . 124 GLU CB C 29.7 0.2 1 864 . 124 GLU N N 120.6 0.2 1 865 . 125 SER H H 8.31 0.01 1 866 . 125 SER HA H 4.10 0.01 1 867 . 125 SER HB2 H 3.61 0.01 2 868 . 125 SER C C 175.1 0.2 1 869 . 125 SER CA C 58.7 0.2 1 870 . 125 SER CB C 63.4 0.2 1 871 . 125 SER N N 116.4 0.2 1 872 . 126 ARG H H 8.29 0.01 1 873 . 126 ARG HA H 4.05 0.01 1 874 . 126 ARG HB2 H 1.61 0.01 1 875 . 126 ARG HB3 H 1.52 0.01 1 876 . 126 ARG C C 176.6 0.2 1 877 . 126 ARG CA C 56.3 0.2 1 878 . 126 ARG CB C 30.4 0.2 1 879 . 126 ARG N N 122.4 0.2 1 880 . 127 LEU H H 8.17 0.01 1 881 . 127 LEU HA H 4.04 0.01 1 882 . 127 LEU HB2 H 1.41 0.01 1 883 . 127 LEU HB3 H 1.30 0.01 1 884 . 127 LEU C C 178.1 0.2 1 885 . 127 LEU CA C 55.4 0.2 1 886 . 127 LEU CB C 42.1 0.2 1 887 . 127 LEU N N 121.8 0.2 1 888 . 128 GLY H H 8.35 0.01 1 889 . 128 GLY HA2 H 3.73 0.01 2 890 . 128 GLY C C 174.6 0.2 1 891 . 128 GLY CA C 45.4 0.2 1 892 . 128 GLY N N 109.0 0.2 1 893 . 129 THR H H 8.09 0.01 1 894 . 129 THR HA H 4.13 0.01 1 895 . 129 THR HB H 4.01 0.01 1 896 . 129 THR C C 175.0 0.2 1 897 . 129 THR CA C 61.7 0.2 1 898 . 129 THR CB C 69.6 0.2 1 899 . 129 THR N N 112.7 0.2 1 900 . 130 SER H H 8.43 0.01 1 901 . 130 SER HA H 4.19 0.01 1 902 . 130 SER HB2 H 3.62 0.01 2 903 . 130 SER C C 175.2 0.2 1 904 . 130 SER CA C 58.5 0.2 1 905 . 130 SER CB C 63.6 0.2 1 906 . 130 SER N N 117.8 0.2 1 907 . 131 GLY H H 8.5 0.01 1 908 . 131 GLY HA2 H 3.73 0.01 1 909 . 131 GLY HA3 H 3.73 0.01 1 910 . 131 GLY C C 174.4 0.2 1 911 . 131 GLY CA C 45.5 0.2 1 912 . 131 GLY N N 110.7 0.2 1 913 . 132 THR H H 8.07 0.01 1 914 . 132 THR HA H 4.02 0.01 1 915 . 132 THR HB H 3.92 0.01 1 916 . 132 THR C C 174.4 0.2 1 917 . 132 THR CA C 61.8 0.2 1 918 . 132 THR CB C 69.6 0.2 1 919 . 132 THR N N 113.5 0.2 1 920 . 133 ALA H H 8.31 0.01 1 921 . 133 ALA HA H 4.02 0.01 1 922 . 133 ALA HB H 1.10 0.01 1 923 . 133 ALA C C 177.7 0.2 1 924 . 133 ALA CA C 52.6 0.2 1 925 . 133 ALA CB C 19.0 0.2 1 926 . 133 ALA N N 126.5 0.2 1 927 . 134 LYS H H 8.29 0.01 1 928 . 134 LYS HA H 3.98 0.01 1 929 . 134 LYS HB2 H 1.49 0.01 2 930 . 134 LYS C C 176.6 0.2 1 931 . 134 LYS CA C 56.2 0.2 1 932 . 134 LYS CB C 32.9 0.2 1 933 . 134 LYS N N 120.89 0.2 1 934 . 135 LYS H H 8.42 0.01 1 935 . 135 LYS HA H 4.08 0.01 1 936 . 135 LYS HB2 H 1.56 0.01 1 937 . 135 LYS HB3 H 1.47 0.01 1 938 . 135 LYS C C 176.8 0.2 1 939 . 135 LYS CA C 56.3 0.2 1 940 . 135 LYS CB C 33.0 0.2 1 941 . 135 LYS N N 123.0 0.2 1 942 . 136 THR H H 8.19 0.01 1 943 . 136 THR HA H 4.00 0.01 1 944 . 136 THR HB H 3.93 0.01 1 945 . 136 THR C C 176.8 0.2 1 946 . 136 THR CA C 61.9 0.2 1 947 . 136 THR CB C 69.6 0.2 1 948 . 136 THR N N 116.0 0.2 1 949 . 137 ALA H H 8.39 0.01 1 950 . 137 ALA HA H 4.02 0.01 1 951 . 137 ALA HB H 1.11 0.01 1 952 . 137 ALA C C 177.7 0.2 1 953 . 137 ALA CA C 52.6 0.2 1 954 . 137 ALA CB C 19.1 0.2 1 955 . 137 ALA N N 126.0 0.2 1 956 . 138 GLU H H 8.39 0.01 1 957 . 138 GLU HA H 3.97 0.01 1 958 . 138 GLU HB2 H 1.74 0.01 1 959 . 138 GLU HB3 H 1.64 0.01 1 960 . 138 GLU C C 176.2 0.2 1 961 . 138 GLU CA C 54.6 0.2 1 962 . 138 GLU CB C 30.2 0.2 1 963 . 138 GLU N N 120.0 0.2 1 964 . 139 CYS H H 8.4 0.01 1 965 . 139 CYS HA H 4.21 0.01 1 966 . 139 CYS HB2 H 2.60 0.01 2 967 . 139 CYS C C 174.2 0.2 1 968 . 139 CYS CA C 58.3 0.2 1 969 . 139 CYS CB C 27.7 0.2 1 970 . 139 CYS N N 120.5 0.2 1 971 . 140 ILE H H 8.25 0.01 1 972 . 140 ILE HA H 4.17 0.01 1 973 . 140 ILE HB H 1.57 0.01 1 974 . 140 ILE C C 174.4 0.2 1 975 . 140 ILE CA C 58.7 0.2 1 976 . 140 ILE CB C 38.3 0.2 1 977 . 140 ILE N N 125.3 0.2 1 978 . 141 PRO HA H 4.11 0.01 1 979 . 141 PRO HB2 H 2.00 0.01 1 980 . 141 PRO HB3 H 1.58 0.01 1 981 . 141 PRO C C 176.8 0.2 1 982 . 141 PRO CA C 63.0 0.2 1 983 . 141 PRO CB C 32.0 0.2 1 984 . 142 LYS H H 8.51 0.01 1 985 . 142 LYS HA H 4.05 0.01 1 986 . 142 LYS HB2 H 1.53 0.01 1 987 . 142 LYS HB3 H 1.46 0.01 1 988 . 142 LYS C C 176.9 0.2 1 989 . 142 LYS CA C 56.2 0.2 1 990 . 142 LYS CB C 32.6 0.2 1 991 . 142 LYS N N 122.0 0.2 1 992 . 143 THR H H 8.11 0.01 1 993 . 143 THR HA H 3.99 0.01 1 994 . 143 THR HB H 3.89 0.01 1 995 . 143 THR C C 174.3 0.2 1 996 . 143 THR CA C 61.4 0.2 1 997 . 143 THR CB C 69.6 0.2 1 998 . 143 THR N N 114.5 0.2 1 999 . 144 HIS H H 8.5 0.01 1 1000 . 144 HIS HA H 4.39 0.01 1 1001 . 144 HIS HB2 H 2.89 0.01 1 1002 . 144 HIS HB3 H 2.83 0.01 1 1003 . 144 HIS C C 174.7 0.2 1 1004 . 144 HIS CA C 55.5 0.2 1 1005 . 144 HIS CB C 29.7 0.2 1 1006 . 144 HIS N N 120.5 0.2 1 1007 . 145 GLU H H 8.49 0.01 1 1008 . 145 GLU HA H 3.99 0.01 1 1009 . 145 GLU HB2 H 1.73 0.01 1 1010 . 145 GLU HB3 H 1.63 0.01 1 1011 . 145 GLU C C 176.5 0.2 1 1012 . 145 GLU CA C 56.5 0.2 1 1013 . 145 GLU CB C 30.0 0.2 1 1014 . 145 GLU N N 122.6 0.2 1 1015 . 146 ARG H H 8.6 0.01 1 1016 . 146 ARG HA H 4.02 0.01 1 1017 . 146 ARG HB2 H 1.59 0.01 1 1018 . 146 ARG HB3 H 1.50 0.01 1 1019 . 146 ARG C C 176.9 0.2 1 1020 . 146 ARG CA C 56.4 0.2 1 1021 . 146 ARG CB C 30.4 0.2 1 1022 . 146 ARG N N 122.6 0.2 1 1023 . 147 GLY H H 8.56 0.01 1 1024 . 147 GLY HA2 H 3.70 0.01 2 1025 . 147 GLY C C 174.1 0.2 1 1026 . 147 GLY CA C 45.2 0.2 1 1027 . 147 GLY N N 110.2 0.2 1 1028 . 148 SER H H 8.23 0.01 1 1029 . 148 SER HA H 4.15 0.01 1 1030 . 148 SER HB2 H 3.56 0.01 2 1031 . 148 SER C C 174.5 0.2 1 1032 . 148 SER CA C 58.3 0.2 1 1033 . 148 SER CB C 63.8 0.2 1 1034 . 148 SER N N 115.6 0.2 1 1035 . 149 LYS H H 8.44 0.01 1 1036 . 149 LYS HA H 4.06 0.01 1 1037 . 149 LYS HB2 H 1.55 0.01 1 1038 . 149 LYS HB3 H 1.44 0.01 1 1039 . 149 LYS C C 176.3 0.2 1 1040 . 149 LYS CA C 55.7 0.2 1 1041 . 149 LYS CB C 32.8 0.2 1 1042 . 149 LYS N N 123.0 0.2 1 1043 . 150 GLU H H 8.4 0.01 1 1044 . 150 GLU HA H 4.26 0.01 1 1045 . 150 GLU HB2 H 1.75 0.01 2 1046 . 150 GLU C C 174.6 0.2 1 1047 . 150 GLU CA C 54.4 0.2 1 1048 . 150 GLU CB C 29.3 0.2 1 1049 . 150 GLU N N 123.5 0.2 1 1050 . 151 PRO HA H 4.15 0.01 1 1051 . 151 PRO HB2 H 2.02 0.01 1 1052 . 151 PRO HB3 H 1.66 0.01 1 1053 . 151 PRO C C 177.0 0.2 1 1054 . 151 PRO CA C 63.1 0.2 1 1055 . 151 PRO CB C 31.9 0.2 1 1056 . 152 SER H H 8.51 0.01 1 1057 . 152 SER HA H 4.19 0.01 1 1058 . 152 SER HB2 H 3.61 0.01 1 1059 . 152 SER HB3 H 3.60 0.01 1 1060 . 152 SER C C 174.9 0.2 1 1061 . 152 SER CA C 58.3 0.2 1 1062 . 152 SER CB C 63.5 0.2 1 1063 . 152 SER N N 116.1 0.2 1 1064 . 153 THR H H 8.18 0.01 1 1065 . 153 THR HA H 4.06 0.01 1 1066 . 153 THR HB H 3.94 0.01 1 1067 . 153 THR C C 174.2 0.2 1 1068 . 153 THR CA C 61.6 0.2 1 1069 . 153 THR CB C 69.5 0.2 1 1070 . 153 THR N N 115.7 0.2 1 1071 . 154 LYS H H 8.32 0.01 1 1072 . 154 LYS HA H 4.04 0.01 1 1073 . 154 LYS HB2 H 1.53 0.01 1 1074 . 154 LYS HB3 H 1.43 0.01 1 1075 . 154 LYS C C 176.2 0.2 1 1076 . 154 LYS CA C 56.0 0.2 1 1077 . 154 LYS CB C 32.8 0.2 1 1078 . 154 LYS N N 123.6 0.2 1 1079 . 155 GLU H H 8.43 0.01 1 1080 . 155 GLU HA H 4.27 0.01 1 1081 . 155 GLU HB2 H 1.75 0.01 1 1082 . 155 GLU HB3 H 1.60 0.01 1 1083 . 155 GLU C C 174.6 0.2 1 1084 . 155 GLU CA C 54.2 0.2 1 1085 . 155 GLU CB C 29.4 0.2 1 1086 . 155 GLU N N 123.7 0.2 1 1087 . 156 PRO HA H 4.15 0.01 1 1088 . 156 PRO HB2 H 2.02 0.01 1 1089 . 156 PRO HB3 H 1.65 0.01 1 1090 . 156 PRO C C 177.0 0.2 1 1091 . 156 PRO CA C 63.0 0.2 1 1092 . 156 PRO CB C 31.9 0.2 1 1093 . 157 SER H H 8.5 0.01 1 1094 . 157 SER HA H 4.18 0.01 1 1095 . 157 SER HB2 H 3.58 0.01 1 1096 . 157 SER HB3 H 3.59 0.01 1 1097 . 157 SER C C 174.8 0.2 1 1098 . 157 SER CA C 58.1 0.2 1 1099 . 157 SER CB C 63.6 0.2 1 1100 . 157 SER N N 115.9 0.2 1 1101 . 158 THR H H 8.1 0.01 1 1102 . 158 THR HA H 4.02 0.01 1 1103 . 158 THR HB H 3.91 0.01 1 1104 . 158 THR C C 174.2 0.2 1 1105 . 158 THR CA C 61.7 0.2 1 1106 . 158 THR CB C 69.5 0.2 1 1107 . 158 THR N N 115.2 0.2 1 1108 . 159 HIS H H 8.46 0.01 1 1109 . 159 HIS HA H 4.39 0.01 1 1110 . 159 HIS HB2 H 2.85 0.01 2 1111 . 159 HIS C C 174.1 0.2 1 1112 . 159 HIS CA C 55.3 0.2 1 1113 . 159 HIS CB C 29.3 0.2 1 1114 . 159 HIS N N 121.4 0.2 1 1115 . 160 ILE H H 8.22 0.01 1 1116 . 160 ILE HA H 4.13 0.01 1 1117 . 160 ILE HB H 1.52 0.01 1 1118 . 160 ILE C C 174.0 0.2 1 1119 . 160 ILE CA C 58.5 0.2 1 1120 . 160 ILE CB C 38.4 0.2 1 1121 . 160 ILE N N 124.9 0.2 1 1122 . 162 PRO HA H 4.15 0.01 1 1123 . 162 PRO HB2 H 2.00 0.01 1 1124 . 162 PRO HB3 H 1.64 0.01 1 1125 . 162 PRO C C 177.0 0.2 1 1126 . 162 PRO CA C 62.6 0.2 1 1127 . 162 PRO CB C 31.9 0.2 1 1128 . 163 LEU H H 8.34 0.01 1 1129 . 163 LEU HA H 3.99 0.01 1 1130 . 163 LEU HB2 H 1.30 0.01 2 1131 . 163 LEU C C 177.3 0.2 1 1132 . 163 LEU CA C 55.4 0.2 1 1133 . 163 LEU CB C 42.3 0.2 1 1134 . 163 LEU N N 122.3 0.2 1 1135 . 164 ASP H H 8.36 0.01 1 1136 . 164 ASP HA H 4.32 0.01 1 1137 . 164 ASP HB2 H 2.40 0.01 2 1138 . 164 ASP C C 176.4 0.2 1 1139 . 164 ASP CA C 53.9 0.2 1 1140 . 164 ASP CB C 41.1 0.2 1 1141 . 164 ASP N N 120.9 0.2 1 1142 . 165 SER H H 8.26 0.01 1 1143 . 165 SER HA H 4.10 0.01 1 1144 . 165 SER HB2 H 3.62 0.01 1 1145 . 165 SER HB3 H 3.56 0.01 1 1146 . 165 SER C C 174.9 0.2 1 1147 . 165 SER CA C 58.6 0.2 1 1148 . 165 SER CB C 63.4 0.2 1 1149 . 165 SER N N 116.6 0.2 1 1150 . 166 LYS H H 8.4 0.01 1 1151 . 166 LYS HA H 4.02 0.01 1 1152 . 166 LYS HB2 H 1.54 0.01 2 1153 . 166 LYS C C 177.2 0.2 1 1154 . 166 LYS CA C 56.5 0.2 1 1155 . 166 LYS CB C 32.40 0.2 1 1156 . 166 LYS N N 122.9 0.2 1 1157 . 167 GLY H H 8.35 0.01 1 1158 . 167 GLY HA2 H 3.64 0.01 2 1159 . 167 GLY C C 174.0 0.2 1 1160 . 167 GLY CA C 45.2 0.2 1 1161 . 167 GLY N N 109.4 0.2 1 1162 . 168 ALA H H 8.26 0.01 1 1163 . 168 ALA HA H 4.01 0.01 1 1164 . 168 ALA HB H 1.09 0.01 1 1165 . 168 ALA C C 177.6 0.2 1 1166 . 168 ALA CA C 52.6 0.2 1 1167 . 168 ALA CB C 19.0 0.2 1 1168 . 168 ALA N N 123.6 0.2 1 1169 . 169 ASN H H 8.47 0.01 1 1170 . 169 ASN HA H 4.46 0.01 1 1171 . 169 ASN HB2 H 2.57 0.01 1 1172 . 169 ASN HB3 H 2.47 0.01 1 1173 . 169 ASN C C 175.1 0.2 1 1174 . 169 ASN CA C 53.0 0.2 1 1175 . 169 ASN CB C 38.7 0.2 1 1176 . 169 ASN N N 117.3 0.2 1 1177 . 170 SER H H 8.18 0.01 1 1178 . 170 SER HA H 4.19 0.01 1 1179 . 170 SER HB2 H 3.57 0.01 2 1180 . 170 SER C C 173.5 0.2 1 1181 . 170 SER CA C 58.2 0.2 1 1182 . 170 SER CB C 63.6 0.2 1 1183 . 170 SER N N 116.3 0.2 1 1184 . 171 VAL H H 7.77 0.01 1 1185 . 171 VAL HA H 3.77 0.01 1 1186 . 171 VAL HB H 1.80 0.01 1 1187 . 171 VAL C C 173.0 0.2 1 1188 . 171 VAL CA C 63.6 0.2 1 1189 . 171 VAL CB C 33.0 0.2 1 1190 . 171 VAL N N 125.2 0.2 1 stop_ save_