data_5522 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to Editor: 1H, 15N and 13C resonance assignments of the repeated domain of human beta ig-h3 ; _BMRB_accession_number 5522 _BMRB_flat_file_name bmr5522.str _Entry_type original _Submission_date 2002-09-12 _Accession_date 2002-09-12 _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 Park Sangho . . 2 Ahn Hee-Chul . . 3 Kim Jung-Eun . . 4 Kim In-San . . 5 Lee Bong-Jin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 220 "13C chemical shifts" 400 "15N chemical shifts" 131 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-23 original author . stop_ _Original_release_date 2002-12-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to Editor: Backbone 1H, 15N, and 13C resonance assignments of the repeated domain of human beta ig-h3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Park Sangho . . 2 Ahn Hee-Chul . . 3 Kim Jung-Eun . . 4 Kim In-San . . 5 Lee Bong-Jin . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 367 _Page_last 368 _Year 2002 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Kim JE, Kim SJ, Lee BH, Park RW, Kim KS, Kim IS, Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-beta-induced gene, betaig-h3 J Biol Chem. 2000 Oct 6;275(40):30907-15 ; _Citation_title 'Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-beta-induced gene, betaig-h3.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10906123 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'J E' E. . 2 Kim 'S J' J. . 3 Lee 'B H' H. . 4 Park 'R W' W. . 5 Kim 'K S' S. . 6 Kim 'I S' S. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 275 _Journal_issue 40 _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 30907 _Page_last 30915 _Year 2000 _Details ; betaig-h3 is a transforming growth factor-beta-inducible cell adhesion molecule that has four characteristic homologous repeated domains. We made recombinant betaig-h3 proteins, which were highly active in mediating human corneal epithelial (HCE) cell adhesion and spreading. The 2nd and the 4th repeated domains were sufficient to mediate HCE cell adhesion. A sequence analysis showed that aspartic acid (Asp) and isoleucine (Ile) of the 2nd and the 4th domains are highly conserved in many fasciclin 1 homologous (fas-1) domains. Substitution mutational study identified these two amino acids are essential for cell adhesion. Synthetic peptides containing Asp and Ile, NKDIL and EPDIM derived from the 2nd and the 4th domains, respectively, almost completely blocked cell adhesion mediated by not only wild type betaig-h3 but also each of the 2nd and the 4th domains. These peptides alone were fully active in mediating cell adhesion. In addition, we demonstrated the functional receptor for betaig-h3 is alpha(3)beta(1) integrin. These results, therefore, establish the essential motifs within the 2nd and the 4th domains of betaig-h3, which interact with alpha(3)beta(1) integrin to mediate HCE cell adhesion to betaig-h3 and suggest that other proteins containing Asp-Ile in their fas-1 domains could possibly function as cell adhesion molecules. ; save_ ################################## # Molecular system description # ################################## save_system_beta_ig-h3_4th_domain _Saveframe_category molecular_system _Mol_system_name '4th fas-1 domain of beta ig-h3' _Abbreviation_common 'beta ig-h3 4th domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '4th fas-1 domain of beta ig-h3' $beta_ig-h3_4th_domain 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_beta_ig-h3_4th_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '4th fas-1 domain of human beta ig-h3' _Abbreviation_common 'beta ig-h3 4th domain' _Molecular_mass . _Mol_thiol_state 'not present' _Details ; The molecule has 6 and 7 extra vector-derived amino acids at the N- and C-terminus respectively. These are excluded from resonance assignments. ; ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; GSMAISLTPPMGTVMDVLKG DNRFSMLVAAIQSAGLTETL NREGVYTVFAPTNEAFRALP PRERSRLLGDAKELANILKY HIGDEILVSGGIGALVRLKS LQGDKLEVSLKNNVVSVNKE PVAEPDIMATNGVVHVITNV LQPPANEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 MET 4 ALA 5 ILE 6 SER 7 LEU 8 THR 9 PRO 10 PRO 11 MET 12 GLY 13 THR 14 VAL 15 MET 16 ASP 17 VAL 18 LEU 19 LYS 20 GLY 21 ASP 22 ASN 23 ARG 24 PHE 25 SER 26 MET 27 LEU 28 VAL 29 ALA 30 ALA 31 ILE 32 GLN 33 SER 34 ALA 35 GLY 36 LEU 37 THR 38 GLU 39 THR 40 LEU 41 ASN 42 ARG 43 GLU 44 GLY 45 VAL 46 TYR 47 THR 48 VAL 49 PHE 50 ALA 51 PRO 52 THR 53 ASN 54 GLU 55 ALA 56 PHE 57 ARG 58 ALA 59 LEU 60 PRO 61 PRO 62 ARG 63 GLU 64 ARG 65 SER 66 ARG 67 LEU 68 LEU 69 GLY 70 ASP 71 ALA 72 LYS 73 GLU 74 LEU 75 ALA 76 ASN 77 ILE 78 LEU 79 LYS 80 TYR 81 HIS 82 ILE 83 GLY 84 ASP 85 GLU 86 ILE 87 LEU 88 VAL 89 SER 90 GLY 91 GLY 92 ILE 93 GLY 94 ALA 95 LEU 96 VAL 97 ARG 98 LEU 99 LYS 100 SER 101 LEU 102 GLN 103 GLY 104 ASP 105 LYS 106 LEU 107 GLU 108 VAL 109 SER 110 LEU 111 LYS 112 ASN 113 ASN 114 VAL 115 VAL 116 SER 117 VAL 118 ASN 119 LYS 120 GLU 121 PRO 122 VAL 123 ALA 124 GLU 125 PRO 126 ASP 127 ILE 128 MET 129 ALA 130 THR 131 ASN 132 GLY 133 VAL 134 VAL 135 HIS 136 VAL 137 ILE 138 THR 139 ASN 140 VAL 141 LEU 142 GLN 143 PRO 144 PRO 145 ALA 146 ASN 147 GLU 148 HIS 149 HIS 150 HIS 151 HIS 152 HIS 153 HIS 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 11311 "FAS1 domain" 86.93 146 100.00 100.00 4.94e-89 BMRB 18466 Wild-type_FAS1-4 86.93 135 100.00 100.00 5.99e-89 BMRB 18467 FAS1-4_R555W 86.27 135 99.24 99.24 4.14e-87 PDB 1X3B "Solution Structure Of The Fas1 Domain Of Human Transforming Growth Factor-Beta Induced Protein Ig-H3" 86.93 146 100.00 100.00 4.94e-89 PDB 2LTB "Wild-type Fas1-4" 86.93 135 100.00 100.00 5.99e-89 PDB 2LTC "Fas1-4, R555w" 86.27 135 99.24 99.24 4.14e-87 PDB 2VXP "The Fourth Fas1 Domain Structure Of Human Bigh3" 86.27 132 100.00 100.00 6.33e-88 GB AAC24944 "BIGH3 [Homo sapiens]" 94.77 212 97.24 97.93 3.01e-94 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $beta_ig-h3_4th_domain Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $beta_ig-h3_4th_domain 'recombinant technology' 'E. coli' Escherichia coli . . 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 $beta_ig-h3_4th_domain 1.0 mM '[U-90% 2H; U-15N; U-13C]' 'sodium phosphate' 20 mM . 'sodium azide' 1 mM . 'deuterium oxide' 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta_ig-h3_4th_domain 1.0 mM [U-15N] 'sodium phosphate' 20 mM . 'deuterium oxide' 10 % . 'sodium azide' 1.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XwinNMR _Saveframe_category software _Name xwinnmr _Version 2.6 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . 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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_1H-1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _Sample_label . save_ save_1H-1H-15N_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N TOCSY' _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 HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 298 0.05 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '4th fas-1 domain of beta ig-h3' _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 . 7 LEU H H 8.38 0.02 1 2 . 7 LEU HA H 4.11 0.02 1 3 . 7 LEU C C 177.36 0.1 1 4 . 7 LEU CA C 55.26 0.1 1 5 . 7 LEU CB C 42.28 0.1 1 6 . 7 LEU N N 124.74 0.1 1 7 . 8 THR H H 8.14 0.02 1 8 . 8 THR HA H 4.55 0.02 1 9 . 8 THR C C 172.40 0.1 1 10 . 8 THR CA C 59.80 0.1 1 11 . 8 THR CB C 70.02 0.1 1 12 . 8 THR N N 117.43 0.1 1 13 . 10 PRO C C 176.77 0.1 1 14 . 10 PRO CA C 62.73 0.1 1 15 . 10 PRO CB C 32.08 0.1 1 16 . 11 MET H H 8.46 0.02 1 17 . 11 MET C C 176.05 0.1 1 18 . 11 MET CA C 56.02 0.1 1 19 . 11 MET CB C 34.22 0.1 1 20 . 11 MET N N 120.12 0.1 1 21 . 12 GLY H H 8.01 0.02 1 22 . 12 GLY C C 173.87 0.1 1 23 . 12 GLY CA C 44.58 0.1 1 24 . 12 GLY N N 109.11 0.1 1 25 . 13 THR H H 9.31 0.02 1 26 . 13 THR HA H 4.31 0.02 1 27 . 13 THR C C 176.41 0.1 1 28 . 13 THR CA C 62.06 0.1 1 29 . 13 THR CB C 73.34 0.1 1 30 . 13 THR N N 111.96 0.1 1 31 . 14 VAL H H 9.88 0.02 1 32 . 14 VAL C C 177.18 0.1 1 33 . 14 VAL CA C 67.06 0.1 1 34 . 14 VAL CB C 31.48 0.1 1 35 . 14 VAL N N 118.00 0.1 1 36 . 15 MET H H 6.95 0.02 1 37 . 15 MET HA H 4.30 0.02 1 38 . 15 MET C C 178.25 0.1 1 39 . 15 MET CA C 56.09 0.1 1 40 . 15 MET CB C 30.66 0.1 1 41 . 15 MET N N 113.97 0.1 1 42 . 16 ASP H H 7.41 0.02 1 43 . 16 ASP C C 179.80 0.1 1 44 . 16 ASP CA C 58.17 0.1 1 45 . 16 ASP CB C 40.47 0.1 1 46 . 16 ASP N N 120.12 0.1 1 47 . 17 VAL H H 8.12 0.02 1 48 . 17 VAL C C 179.15 0.1 1 49 . 17 VAL CA C 66.05 0.1 1 50 . 17 VAL CB C 31.39 0.1 1 51 . 17 VAL N N 121.10 0.1 1 52 . 18 LEU H H 7.83 0.02 1 53 . 18 LEU C C 179.23 0.1 1 54 . 18 LEU CA C 57.34 0.1 1 55 . 18 LEU CB C 41.71 0.1 1 56 . 18 LEU N N 116.90 0.1 1 57 . 19 LYS H H 8.36 0.02 1 58 . 19 LYS C C 178.16 0.1 1 59 . 19 LYS CA C 59.11 0.1 1 60 . 19 LYS CB C 32.55 0.1 1 61 . 19 LYS N N 114.59 0.1 1 62 . 20 GLY H H 7.58 0.02 1 63 . 20 GLY C C 172.63 0.1 1 64 . 20 GLY CA C 45.54 0.1 1 65 . 20 GLY N N 104.49 0.1 1 66 . 21 ASP H H 7.04 0.02 1 67 . 21 ASP HA H 4.97 0.02 1 68 . 21 ASP C C 176.56 0.1 1 69 . 21 ASP CA C 52.68 0.1 1 70 . 21 ASP CB C 44.04 0.1 1 71 . 21 ASP N N 119.89 0.1 1 72 . 22 ASN H H 8.98 0.02 1 73 . 22 ASN HA H 4.71 0.02 1 74 . 22 ASN C C 176.87 0.1 1 75 . 22 ASN CA C 55.96 0.1 1 76 . 22 ASN CB C 38.30 0.1 1 77 . 22 ASN N N 125.47 0.1 1 78 . 23 ARG H H 8.59 0.02 1 79 . 23 ARG HA H 4.09 0.02 1 80 . 23 ARG C C 176.36 0.1 1 81 . 23 ARG CA C 58.04 0.1 1 82 . 23 ARG CB C 30.48 0.1 1 83 . 23 ARG N N 118.73 0.1 1 84 . 24 PHE H H 7.60 0.02 1 85 . 24 PHE C C 176.68 0.1 1 86 . 24 PHE CA C 56.28 0.1 1 87 . 24 PHE CB C 38.47 0.1 1 88 . 24 PHE N N 113.15 0.1 1 89 . 25 SER H H 7.51 0.02 1 90 . 25 SER C C 178.67 0.1 1 91 . 25 SER CA C 62.76 0.1 1 92 . 25 SER CB C 61.72 0.1 1 93 . 25 SER N N 116.51 0.1 1 94 . 26 MET H H 9.28 0.02 1 95 . 26 MET HA H 3.91 0.02 1 96 . 26 MET C C 178.25 0.1 1 97 . 26 MET CA C 59.44 0.1 1 98 . 26 MET CB C 31.45 0.1 1 99 . 26 MET N N 124.15 0.1 1 100 . 27 LEU H H 8.62 0.02 1 101 . 27 LEU HA H 3.87 0.02 1 102 . 27 LEU C C 178.29 0.1 1 103 . 27 LEU CA C 58.12 0.1 1 104 . 27 LEU CB C 41.04 0.1 1 105 . 27 LEU N N 123.82 0.1 1 106 . 28 VAL H H 9.05 0.02 1 107 . 28 VAL C C 178.30 0.1 1 108 . 28 VAL CA C 67.75 0.1 1 109 . 28 VAL CB C 31.68 0.1 1 110 . 28 VAL N N 118.71 0.1 1 111 . 29 ALA H H 7.46 0.02 1 112 . 29 ALA C C 180.37 0.1 1 113 . 29 ALA CA C 55.07 0.1 1 114 . 29 ALA CB C 17.69 0.1 1 115 . 29 ALA N N 121.93 0.1 1 116 . 30 ALA H H 8.23 0.02 1 117 . 30 ALA HA H 4.06 0.02 1 118 . 30 ALA C C 178.82 0.1 1 119 . 30 ALA CA C 55.00 0.1 1 120 . 30 ALA CB C 17.91 0.1 1 121 . 30 ALA N N 123.23 0.1 1 122 . 31 ILE H H 8.89 0.02 1 123 . 31 ILE C C 178.02 0.1 1 124 . 31 ILE CA C 65.89 0.1 1 125 . 31 ILE CB C 38.34 0.1 1 126 . 31 ILE N N 120.12 0.1 1 127 . 32 GLN H H 7.84 0.02 1 128 . 32 GLN HA H 4.17 0.02 1 129 . 32 GLN C C 180.34 0.1 1 130 . 32 GLN CA C 58.56 0.1 1 131 . 32 GLN CB C 27.44 0.1 1 132 . 32 GLN N N 118.83 0.1 1 133 . 33 SER H H 8.38 0.02 1 134 . 33 SER HA H 4.07 0.02 1 135 . 33 SER C C 175.74 0.1 1 136 . 33 SER CA C 61.84 0.1 1 137 . 33 SER CB C 63.60 0.1 1 138 . 33 SER N N 118.06 0.1 1 139 . 34 ALA H H 8.26 0.02 1 140 . 34 ALA HA H 4.03 0.02 1 141 . 34 ALA C C 177.02 0.1 1 142 . 34 ALA CA C 52.21 0.1 1 143 . 34 ALA CB C 19.96 0.1 1 144 . 34 ALA N N 119.20 0.1 1 145 . 35 GLY H H 7.77 0.02 1 146 . 35 GLY C C 176.69 0.1 1 147 . 35 GLY CA C 46.50 0.1 1 148 . 35 GLY N N 105.92 0.1 1 149 . 36 LEU H H 8.08 0.02 1 150 . 36 LEU HA H 4.42 0.02 1 151 . 36 LEU C C 175.85 0.1 1 152 . 36 LEU CA C 54.91 0.1 1 153 . 36 LEU CB C 45.03 0.1 1 154 . 36 LEU N N 118.31 0.1 1 155 . 37 THR H H 7.58 0.02 1 156 . 37 THR HA H 4.71 0.02 1 157 . 37 THR C C 175.53 0.1 1 158 . 37 THR CA C 66.72 0.1 1 159 . 37 THR CB C 69.01 0.1 1 160 . 37 THR N N 117.98 0.1 1 161 . 38 GLU H H 8.28 0.02 1 162 . 38 GLU C C 179.50 0.1 1 163 . 38 GLU CA C 59.75 0.1 1 164 . 38 GLU CB C 28.43 0.1 1 165 . 38 GLU N N 117.50 0.1 1 166 . 39 THR H H 7.69 0.02 1 167 . 39 THR HA H 3.69 0.02 1 168 . 39 THR C C 175.97 0.1 1 169 . 39 THR CA C 67.13 0.1 1 170 . 39 THR CB C 69.48 0.1 1 171 . 39 THR N N 116.05 0.1 1 172 . 40 LEU H H 7.08 0.02 1 173 . 40 LEU HA H 3.87 0.02 1 174 . 40 LEU C C 176.26 0.1 1 175 . 40 LEU CA C 55.67 0.1 1 176 . 40 LEU CB C 41.34 0.1 1 177 . 40 LEU N N 116.46 0.1 1 178 . 41 ASN H H 7.71 0.02 1 179 . 41 ASN HA H 4.98 0.02 1 180 . 41 ASN C C 174.84 0.1 1 181 . 41 ASN CA C 52.22 0.1 1 182 . 41 ASN CB C 41.07 0.1 1 183 . 41 ASN N N 118.61 0.1 1 184 . 42 ARG H H 7.25 0.02 1 185 . 42 ARG HA H 4.49 0.02 1 186 . 42 ARG C C 175.44 0.1 1 187 . 42 ARG CA C 55.65 0.1 1 188 . 42 ARG CB C 32.64 0.1 1 189 . 42 ARG N N 119.50 0.1 1 190 . 43 GLU H H 8.51 0.02 1 191 . 43 GLU C C 176.38 0.1 1 192 . 43 GLU CA C 57.85 0.1 1 193 . 43 GLU CB C 29.57 0.1 1 194 . 43 GLU N N 119.98 0.1 1 195 . 44 GLY H H 7.94 0.02 1 196 . 44 GLY C C 170.61 0.1 1 197 . 44 GLY CA C 44.84 0.1 1 198 . 44 GLY N N 110.77 0.1 1 199 . 45 VAL H H 7.16 0.02 1 200 . 45 VAL HA H 4.07 0.02 1 201 . 45 VAL C C 173.11 0.1 1 202 . 45 VAL CA C 59.42 0.1 1 203 . 45 VAL CB C 33.74 0.1 1 204 . 45 VAL N N 114.79 0.1 1 205 . 46 TYR H H 7.50 0.02 1 206 . 46 TYR HA H 5.12 0.02 1 207 . 46 TYR C C 176.18 0.1 1 208 . 46 TYR CA C 56.76 0.1 1 209 . 46 TYR CB C 42.55 0.1 1 210 . 46 TYR N N 117.18 0.1 1 211 . 47 THR H H 7.88 0.02 1 212 . 47 THR HA H 4.76 0.02 1 213 . 47 THR C C 173.51 0.1 1 214 . 47 THR CA C 62.23 0.1 1 215 . 47 THR CB C 71.19 0.1 1 216 . 47 THR N N 116.82 0.1 1 217 . 48 VAL H H 9.17 0.02 1 218 . 48 VAL HA H 4.52 0.02 1 219 . 48 VAL C C 174.14 0.1 1 220 . 48 VAL CA C 61.28 0.1 1 221 . 48 VAL CB C 33.85 0.1 1 222 . 48 VAL N N 126.63 0.1 1 223 . 49 PHE H H 9.05 0.02 1 224 . 49 PHE HA H 5.29 0.02 1 225 . 49 PHE C C 173.57 0.1 1 226 . 49 PHE CA C 57.83 0.1 1 227 . 49 PHE CB C 38.57 0.1 1 228 . 49 PHE N N 128.29 0.1 1 229 . 50 ALA H H 8.64 0.02 1 230 . 50 ALA HA H 4.51 0.02 1 231 . 50 ALA C C 174.33 0.1 1 232 . 50 ALA CA C 49.09 0.1 1 233 . 50 ALA CB C 22.87 0.1 1 234 . 50 ALA N N 125.79 0.1 1 235 . 51 PRO C C 177.81 0.1 1 236 . 51 PRO CA C 60.94 0.1 1 237 . 51 PRO CB C 31.42 0.1 1 238 . 52 THR H H 7.75 0.02 1 239 . 52 THR HA H 4.31 0.02 1 240 . 52 THR C C 176.57 0.1 1 241 . 52 THR CA C 60.94 0.1 1 242 . 52 THR CB C 71.84 0.1 1 243 . 52 THR N N 111.85 0.1 1 244 . 53 ASN H H 8.88 0.02 1 245 . 53 ASN C C 178.39 0.1 1 246 . 53 ASN CA C 56.36 0.1 1 247 . 53 ASN CB C 37.27 0.1 1 248 . 53 ASN N N 118.78 0.1 1 249 . 54 GLU H H 8.27 0.02 1 250 . 54 GLU C C 178.30 0.1 1 251 . 54 GLU CA C 59.77 0.1 1 252 . 54 GLU CB C 29.12 0.1 1 253 . 54 GLU N N 118.18 0.1 1 254 . 55 ALA H H 7.46 0.02 1 255 . 55 ALA C C 180.50 0.1 1 256 . 55 ALA CA C 55.07 0.1 1 257 . 55 ALA CB C 19.62 0.1 1 258 . 55 ALA N N 121.93 0.1 1 259 . 56 PHE H H 7.32 0.02 1 260 . 56 PHE HA H 3.95 0.02 1 261 . 56 PHE C C 178.76 0.1 1 262 . 56 PHE CA C 62.09 0.1 1 263 . 56 PHE CB C 40.01 0.1 1 264 . 56 PHE N N 114.98 0.1 1 265 . 57 ARG H H 8.25 0.02 1 266 . 57 ARG C C 176.48 0.1 1 267 . 57 ARG CA C 58.99 0.1 1 268 . 57 ARG CB C 30.34 0.1 1 269 . 57 ARG N N 118.80 0.1 1 270 . 58 ALA H H 7.40 0.02 1 271 . 58 ALA HA H 4.19 0.02 1 272 . 58 ALA C C 178.80 0.1 1 273 . 58 ALA CA C 52.74 0.1 1 274 . 58 ALA CB C 18.96 0.1 1 275 . 58 ALA N N 118.67 0.1 1 276 . 59 LEU H H 7.09 0.02 1 277 . 59 LEU HA H 4.51 0.02 1 278 . 59 LEU C C 174.48 0.1 1 279 . 59 LEU CA C 53.29 0.1 1 280 . 59 LEU CB C 42.16 0.1 1 281 . 59 LEU N N 119.48 0.1 1 282 . 61 PRO C C 179.18 0.1 1 283 . 61 PRO CA C 66.52 0.1 1 284 . 61 PRO CB C 31.82 0.1 1 285 . 62 ARG H H 8.96 0.02 1 286 . 62 ARG HA H 4.71 0.02 1 287 . 62 ARG C C 179.12 0.1 1 288 . 62 ARG CA C 59.42 0.1 1 289 . 62 ARG CB C 29.50 0.1 1 290 . 62 ARG N N 116.83 0.1 1 291 . 63 GLU H H 7.51 0.02 1 292 . 63 GLU HA H 4.28 0.02 1 293 . 63 GLU C C 178.51 0.1 1 294 . 63 GLU CA C 58.42 0.1 1 295 . 63 GLU CB C 29.69 0.1 1 296 . 63 GLU N N 119.48 0.1 1 297 . 64 ARG H H 8.50 0.02 1 298 . 64 ARG C C 178.04 0.1 1 299 . 64 ARG CA C 60.22 0.1 1 300 . 64 ARG CB C 29.82 0.1 1 301 . 64 ARG N N 120.15 0.1 1 302 . 65 SER H H 8.17 0.02 1 303 . 65 SER HA H 4.11 0.02 1 304 . 65 SER C C 177.21 0.1 1 305 . 65 SER CA C 61.65 0.1 1 306 . 65 SER CB C 63.55 0.1 1 307 . 65 SER N N 111.72 0.1 1 308 . 66 ARG H H 7.57 0.02 1 309 . 66 ARG HA H 4.07 0.02 1 310 . 66 ARG C C 178.30 0.1 1 311 . 66 ARG CA C 59.05 0.1 1 312 . 66 ARG CB C 30.35 0.1 1 313 . 66 ARG N N 122.23 0.1 1 314 . 67 LEU H H 8.02 0.02 1 315 . 67 LEU HA H 4.03 0.02 1 316 . 67 LEU C C 177.42 0.1 1 317 . 67 LEU CA C 57.84 0.1 1 318 . 67 LEU CB C 42.35 0.1 1 319 . 67 LEU N N 117.63 0.1 1 320 . 68 LEU H H 7.78 0.02 1 321 . 68 LEU HA H 4.23 0.02 1 322 . 68 LEU C C 179.07 0.1 1 323 . 68 LEU CA C 56.19 0.1 1 324 . 68 LEU CB C 40.97 0.1 1 325 . 68 LEU N N 111.69 0.1 1 326 . 69 GLY H H 7.54 0.02 1 327 . 69 GLY C C 173.34 0.1 1 328 . 69 GLY CA C 45.54 0.1 1 329 . 69 GLY N N 104.41 0.1 1 330 . 70 ASP H H 7.24 0.02 1 331 . 70 ASP HA H 4.86 0.02 1 332 . 70 ASP C C 174.90 0.1 1 333 . 70 ASP CA C 52.62 0.1 1 334 . 70 ASP CB C 42.19 0.1 1 335 . 70 ASP N N 120.60 0.1 1 336 . 71 ALA H H 8.68 0.02 1 337 . 71 ALA HA H 4.68 0.02 1 338 . 71 ALA C C 180.20 0.1 1 339 . 71 ALA CA C 55.72 0.1 1 340 . 71 ALA CB C 18.79 0.1 1 341 . 71 ALA N N 126.79 0.1 1 342 . 72 LYS H H 8.13 0.02 1 343 . 72 LYS C C 179.71 0.1 1 344 . 72 LYS CA C 59.30 0.1 1 345 . 72 LYS CB C 31.69 0.1 1 346 . 72 LYS N N 117.94 0.1 1 347 . 73 GLU H H 7.83 0.02 1 348 . 73 GLU HA H 4.26 0.02 1 349 . 73 GLU C C 179.46 0.1 1 350 . 73 GLU CA C 58.43 0.1 1 351 . 73 GLU CB C 29.23 0.1 1 352 . 73 GLU N N 121.49 0.1 1 353 . 74 LEU H H 8.76 0.02 1 354 . 74 LEU HA H 4.02 0.02 1 355 . 74 LEU C C 178.60 0.1 1 356 . 74 LEU CA C 58.06 0.1 1 357 . 74 LEU CB C 41.24 0.1 1 358 . 74 LEU N N 120.75 0.1 1 359 . 75 ALA H H 8.04 0.02 1 360 . 75 ALA HA H 3.88 0.02 1 361 . 75 ALA C C 178.96 0.1 1 362 . 75 ALA CA C 55.98 0.1 1 363 . 75 ALA CB C 18.13 0.1 1 364 . 75 ALA N N 118.71 0.1 1 365 . 76 ASN H H 7.43 0.02 1 366 . 76 ASN HA H 4.40 0.02 1 367 . 76 ASN C C 176.58 0.1 1 368 . 76 ASN CA C 57.21 0.1 1 369 . 76 ASN CB C 39.32 0.1 1 370 . 76 ASN N N 115.11 0.1 1 371 . 77 ILE H H 8.03 0.02 1 372 . 77 ILE HA H 3.84 0.02 1 373 . 77 ILE C C 179.83 0.1 1 374 . 77 ILE CA C 64.09 0.1 1 375 . 77 ILE CB C 37.74 0.1 1 376 . 77 ILE N N 116.61 0.1 1 377 . 78 LEU H H 8.99 0.02 1 378 . 78 LEU HA H 4.05 0.02 1 379 . 78 LEU C C 179.85 0.1 1 380 . 78 LEU CA C 58.55 0.1 1 381 . 78 LEU CB C 41.68 0.1 1 382 . 78 LEU N N 120.88 0.1 1 383 . 79 LYS H H 8.53 0.02 1 384 . 79 LYS HA H 3.86 0.02 1 385 . 79 LYS C C 177.87 0.1 1 386 . 79 LYS CA C 60.85 0.1 1 387 . 79 LYS CB C 32.38 0.1 1 388 . 79 LYS N N 116.08 0.1 1 389 . 80 TYR H H 7.59 0.02 1 390 . 80 TYR C C 172.07 0.1 1 391 . 80 TYR CA C 59.10 0.1 1 392 . 80 TYR CB C 39.03 0.1 1 393 . 80 TYR N N 119.37 0.1 1 394 . 81 HIS H H 7.51 0.02 1 395 . 81 HIS HA H 4.07 0.02 1 396 . 81 HIS C C 173.83 0.1 1 397 . 81 HIS CA C 59.01 0.1 1 398 . 81 HIS CB C 28.20 0.1 1 399 . 81 HIS N N 108.93 0.1 1 400 . 82 ILE H H 7.28 0.02 1 401 . 82 ILE HA H 5.13 0.02 1 402 . 82 ILE C C 175.79 0.1 1 403 . 82 ILE CA C 59.63 0.1 1 404 . 82 ILE CB C 40.53 0.1 1 405 . 82 ILE N N 117.44 0.1 1 406 . 83 GLY H H 10.18 0.02 1 407 . 83 GLY C C 174.03 0.1 1 408 . 83 GLY CA C 44.00 0.1 1 409 . 83 GLY N N 111.51 0.1 1 410 . 84 ASP H H 8.35 0.02 1 411 . 84 ASP C C 174.79 0.1 1 412 . 84 ASP CA C 53.91 0.1 1 413 . 84 ASP CB C 40.87 0.1 1 414 . 84 ASP N N 120.40 0.1 1 415 . 85 GLU H H 7.25 0.02 1 416 . 85 GLU HA H 4.42 0.02 1 417 . 85 GLU C C 175.39 0.1 1 418 . 85 GLU CA C 54.49 0.1 1 419 . 85 GLU CB C 33.15 0.1 1 420 . 85 GLU N N 114.01 0.1 1 421 . 86 ILE H H 8.49 0.02 1 422 . 86 ILE HA H 3.53 0.02 1 423 . 86 ILE C C 174.90 0.1 1 424 . 86 ILE CA C 62.48 0.1 1 425 . 86 ILE CB C 38.39 0.1 1 426 . 86 ILE N N 120.79 0.1 1 427 . 87 LEU H H 7.99 0.02 1 428 . 87 LEU HA H 4.75 0.02 1 429 . 87 LEU C C 174.23 0.1 1 430 . 87 LEU CA C 54.00 0.1 1 431 . 87 LEU CB C 43.81 0.1 1 432 . 87 LEU N N 132.51 0.1 1 433 . 88 VAL H H 7.95 0.02 1 434 . 88 VAL HA H 4.72 0.02 1 435 . 88 VAL C C 178.50 0.1 1 436 . 88 VAL CA C 59.59 0.1 1 437 . 88 VAL CB C 33.40 0.1 1 438 . 88 VAL N N 118.34 0.1 1 439 . 89 SER H H 11.06 0.02 1 440 . 89 SER C C 177.24 0.1 1 441 . 89 SER CA C 62.94 0.1 1 442 . 89 SER CB C 61.99 0.1 1 443 . 89 SER N N 121.50 0.1 1 444 . 90 GLY H H 8.27 0.02 1 445 . 90 GLY C C 174.80 0.1 1 446 . 90 GLY CA C 46.09 0.1 1 447 . 90 GLY N N 107.26 0.1 1 448 . 91 GLY H H 8.23 0.02 1 449 . 91 GLY C C 174.46 0.1 1 450 . 91 GLY CA C 44.60 0.1 1 451 . 91 GLY N N 107.77 0.1 1 452 . 92 ILE H H 7.31 0.02 1 453 . 92 ILE HA H 3.79 0.02 1 454 . 92 ILE C C 175.77 0.1 1 455 . 92 ILE CA C 62.99 0.1 1 456 . 92 ILE CB C 39.05 0.1 1 457 . 92 ILE N N 120.93 0.1 1 458 . 93 GLY H H 7.91 0.02 1 459 . 93 GLY C C 173.21 0.1 1 460 . 93 GLY CA C 45.57 0.1 1 461 . 93 GLY N N 111.62 0.1 1 462 . 94 ALA H H 8.30 0.02 1 463 . 94 ALA HA H 4.31 0.02 1 464 . 94 ALA C C 177.62 0.1 1 465 . 94 ALA CA C 54.41 0.1 1 466 . 94 ALA CB C 19.69 0.1 1 467 . 94 ALA N N 124.88 0.1 1 468 . 95 LEU H H 7.80 0.02 1 469 . 95 LEU HA H 4.66 0.02 1 470 . 95 LEU C C 175.56 0.1 1 471 . 95 LEU CA C 56.21 0.1 1 472 . 95 LEU CB C 43.49 0.1 1 473 . 95 LEU N N 118.33 0.1 1 474 . 96 VAL H H 9.52 0.02 1 475 . 96 VAL HA H 4.27 0.02 1 476 . 96 VAL C C 174.17 0.1 1 477 . 96 VAL CA C 61.44 0.1 1 478 . 96 VAL CB C 35.60 0.1 1 479 . 96 VAL N N 127.92 0.1 1 480 . 97 ARG H H 8.63 0.02 1 481 . 97 ARG HA H 5.20 0.02 1 482 . 97 ARG C C 175.02 0.1 1 483 . 97 ARG CA C 54.92 0.1 1 484 . 97 ARG CB C 29.98 0.1 1 485 . 97 ARG N N 125.13 0.1 1 486 . 98 LEU H H 8.81 0.02 1 487 . 98 LEU HA H 4.51 0.02 1 488 . 98 LEU C C 175.10 0.1 1 489 . 98 LEU CA C 53.27 0.1 1 490 . 98 LEU CB C 45.65 0.1 1 491 . 98 LEU N N 127.69 0.1 1 492 . 99 LYS H H 9.43 0.02 1 493 . 99 LYS HA H 3.97 0.02 1 494 . 99 LYS C C 174.48 0.1 1 495 . 99 LYS CA C 58.52 0.1 1 496 . 99 LYS CB C 32.35 0.1 1 497 . 99 LYS N N 129.27 0.1 1 498 . 100 SER H H 7.89 0.02 1 499 . 100 SER C C 178.17 0.1 1 500 . 100 SER CA C 58.40 0.1 1 501 . 100 SER CB C 67.68 0.1 1 502 . 100 SER N N 121.46 0.1 1 503 . 101 LEU H H 9.26 0.02 1 504 . 101 LEU HA H 4.23 0.02 1 505 . 101 LEU C C 178.44 0.1 1 506 . 101 LEU CA C 57.53 0.1 1 507 . 101 LEU CB C 41.16 0.1 1 508 . 101 LEU N N 121.06 0.1 1 509 . 102 GLN H H 7.60 0.02 1 510 . 102 GLN C C 176.26 0.1 1 511 . 102 GLN CA C 56.02 0.1 1 512 . 102 GLN CB C 27.49 0.1 1 513 . 102 GLN N N 118.50 0.1 1 514 . 103 GLY H H 7.61 0.02 1 515 . 103 GLY C C 174.55 0.1 1 516 . 103 GLY CA C 45.58 0.1 1 517 . 103 GLY N N 109.18 0.1 1 518 . 104 ASP H H 8.91 0.02 1 519 . 104 ASP HA H 4.89 0.02 1 520 . 104 ASP C C 177.50 0.1 1 521 . 104 ASP CA C 54.88 0.1 1 522 . 104 ASP CB C 41.96 0.1 1 523 . 104 ASP N N 120.48 0.1 1 524 . 105 LYS H H 9.12 0.02 1 525 . 105 LYS HA H 5.06 0.02 1 526 . 105 LYS C C 177.27 0.1 1 527 . 105 LYS CA C 56.19 0.1 1 528 . 105 LYS CB C 33.89 0.1 1 529 . 105 LYS N N 118.76 0.1 1 530 . 106 LEU H H 9.43 0.02 1 531 . 106 LEU HA H 4.32 0.02 1 532 . 106 LEU C C 176.02 0.1 1 533 . 106 LEU CA C 56.32 0.1 1 534 . 106 LEU CB C 44.94 0.1 1 535 . 106 LEU N N 126.52 0.1 1 536 . 107 GLU H H 8.32 0.02 1 537 . 107 GLU C C 175.11 0.1 1 538 . 107 GLU CA C 55.67 0.1 1 539 . 107 GLU CB C 30.35 0.1 1 540 . 107 GLU N N 121.00 0.1 1 541 . 108 VAL H H 9.32 0.02 1 542 . 108 VAL HA H 5.00 0.02 1 543 . 108 VAL C C 173.82 0.1 1 544 . 108 VAL CA C 61.21 0.1 1 545 . 108 VAL CB C 32.77 0.1 1 546 . 108 VAL N N 130.57 0.1 1 547 . 109 SER H H 9.02 0.02 1 548 . 109 SER HA H 4.89 0.02 1 549 . 109 SER C C 171.98 0.1 1 550 . 109 SER CA C 56.72 0.1 1 551 . 109 SER CB C 67.73 0.1 1 552 . 109 SER N N 119.85 0.1 1 553 . 110 LEU H H 7.89 0.02 1 554 . 110 LEU HA H 5.00 0.02 1 555 . 110 LEU C C 175.78 0.1 1 556 . 110 LEU CA C 54.41 0.1 1 557 . 110 LEU CB C 44.87 0.1 1 558 . 110 LEU N N 122.87 0.1 1 559 . 111 LYS H H 8.32 0.02 1 560 . 111 LYS C C 176.32 0.1 1 561 . 111 LYS CA C 55.75 0.1 1 562 . 111 LYS CB C 34.66 0.1 1 563 . 111 LYS N N 126.28 0.1 1 564 . 112 ASN H H 9.57 0.02 1 565 . 112 ASN HA H 4.71 0.02 1 566 . 112 ASN C C 174.20 0.1 1 567 . 112 ASN CA C 55.26 0.1 1 568 . 112 ASN CB C 37.24 0.1 1 569 . 112 ASN N N 126.58 0.1 1 570 . 113 ASN H H 8.67 0.02 1 571 . 113 ASN HA H 4.10 0.02 1 572 . 113 ASN C C 173.95 0.1 1 573 . 113 ASN CA C 55.19 0.1 1 574 . 113 ASN CB C 38.13 0.1 1 575 . 113 ASN N N 108.72 0.1 1 576 . 114 VAL H H 7.88 0.02 1 577 . 114 VAL C C 176.46 0.1 1 578 . 114 VAL CA C 62.14 0.1 1 579 . 114 VAL CB C 34.33 0.1 1 580 . 114 VAL N N 121.4 0.1 1 581 . 115 VAL H H 9.45 0.02 1 582 . 115 VAL HA H 4.56 0.02 1 583 . 115 VAL C C 174.77 0.1 1 584 . 115 VAL CA C 61.86 0.1 1 585 . 115 VAL CB C 32.13 0.1 1 586 . 115 VAL N N 133.17 0.1 1 587 . 116 SER H H 9.11 0.02 1 588 . 116 SER HA H 5.34 0.02 1 589 . 116 SER C C 172.04 0.1 1 590 . 116 SER CA C 57.17 0.1 1 591 . 116 SER CB C 66.81 0.1 1 592 . 116 SER N N 120.43 0.1 1 593 . 117 VAL H H 9.17 0.02 1 594 . 117 VAL HA H 4.79 0.02 1 595 . 117 VAL C C 173.99 0.1 1 596 . 117 VAL CA C 57.55 0.1 1 597 . 117 VAL CB C 33.91 0.1 1 598 . 117 VAL N N 120.92 0.1 1 599 . 118 ASN H H 9.78 0.02 1 600 . 118 ASN HA H 4.20 0.02 1 601 . 118 ASN C C 175.30 0.1 1 602 . 118 ASN CA C 54.02 0.1 1 603 . 118 ASN CB C 35.96 0.1 1 604 . 118 ASN N N 128.11 0.1 1 605 . 119 LYS H H 8.26 0.02 1 606 . 119 LYS HA H 3.58 0.02 1 607 . 119 LYS C C 175.69 0.1 1 608 . 119 LYS CA C 58.57 0.1 1 609 . 119 LYS CB C 30.44 0.1 1 610 . 119 LYS N N 106.74 0.1 1 611 . 120 GLU H H 8.53 0.02 1 612 . 120 GLU HA H 4.67 0.02 1 613 . 120 GLU C C 174.30 0.1 1 614 . 120 GLU CA C 52.99 0.1 1 615 . 120 GLU CB C 29.15 0.1 1 616 . 120 GLU N N 125.06 0.1 1 617 . 121 PRO C C 177.60 0.1 1 618 . 121 PRO CA C 62.90 0.1 1 619 . 121 PRO CB C 31.91 0.1 1 620 . 122 VAL H H 9.20 0.02 1 621 . 122 VAL HA H 4.28 0.02 1 622 . 122 VAL C C 176.60 0.1 1 623 . 122 VAL CA C 62.22 0.1 1 624 . 122 VAL CB C 32.15 0.1 1 625 . 122 VAL N N 124.75 0.1 1 626 . 123 ALA H H 8.89 0.02 1 627 . 123 ALA HA H 4.34 0.02 1 628 . 123 ALA C C 178.45 0.1 1 629 . 123 ALA CA C 54.10 0.1 1 630 . 123 ALA CB C 19.70 0.1 1 631 . 123 ALA N N 132.27 0.1 1 632 . 124 GLU H H 6.86 0.02 1 633 . 124 GLU HA H 4.81 0.02 1 634 . 124 GLU C C 171.95 0.1 1 635 . 124 GLU CA C 53.66 0.1 1 636 . 124 GLU CB C 31.52 0.1 1 637 . 124 GLU N N 114.83 0.1 1 638 . 125 PRO C C 177.16 0.1 1 639 . 125 PRO CA C 62.10 0.1 1 640 . 125 PRO CB C 33.74 0.1 1 641 . 126 ASP H H 9.69 0.02 1 642 . 126 ASP HA H 3.81 0.02 1 643 . 126 ASP C C 175.00 0.1 1 644 . 126 ASP CA C 54.98 0.1 1 645 . 126 ASP CB C 37.72 0.1 1 646 . 126 ASP N N 114.26 0.1 1 647 . 127 ILE H H 8.71 0.02 1 648 . 127 ILE HA H 3.99 0.02 1 649 . 127 ILE C C 176.01 0.1 1 650 . 127 ILE CA C 62.82 0.1 1 651 . 127 ILE CB C 36.78 0.1 1 652 . 127 ILE N N 120.89 0.1 1 653 . 128 MET H H 8.12 0.02 1 654 . 128 MET HA H 4.55 0.02 1 655 . 128 MET C C 174.84 0.1 1 656 . 128 MET CA C 54.98 0.1 1 657 . 128 MET CB C 31.12 0.1 1 658 . 128 MET N N 125.39 0.1 1 659 . 129 ALA H H 8.41 0.02 1 660 . 129 ALA HA H 4.82 0.02 1 661 . 129 ALA C C 177.87 0.1 1 662 . 129 ALA CA C 50.08 0.1 1 663 . 129 ALA CB C 23.23 0.1 1 664 . 129 ALA N N 122.25 0.1 1 665 . 130 THR H H 9.19 0.02 1 666 . 130 THR HA H 3.95 0.02 1 667 . 130 THR C C 176.29 0.1 1 668 . 130 THR CA C 64.58 0.1 1 669 . 130 THR CB C 68.58 0.1 1 670 . 130 THR N N 110.98 0.1 1 671 . 131 ASN H H 7.93 0.02 1 672 . 131 ASN HA H 5.04 0.02 1 673 . 131 ASN C C 173.39 0.1 1 674 . 131 ASN CA C 51.32 0.1 1 675 . 131 ASN CB C 37.11 0.1 1 676 . 131 ASN N N 117.17 0.1 1 677 . 132 GLY H H 6.87 0.02 1 678 . 132 GLY C C 170.03 0.1 1 679 . 132 GLY CA C 46.61 0.1 1 680 . 132 GLY N N 102.56 0.1 1 681 . 133 VAL H H 8.46 0.02 1 682 . 133 VAL C C 170.95 0.1 1 683 . 133 VAL CA C 58.69 0.1 1 684 . 133 VAL CB C 34.79 0.1 1 685 . 133 VAL N N 120.06 0.1 1 686 . 134 VAL H H 9.11 0.02 1 687 . 134 VAL HA H 4.57 0.02 1 688 . 134 VAL C C 173.02 0.1 1 689 . 134 VAL CA C 60.55 0.1 1 690 . 134 VAL CB C 34.36 0.1 1 691 . 134 VAL N N 127.34 0.1 1 692 . 135 HIS H H 8.71 0.02 1 693 . 135 HIS HA H 5.47 0.02 1 694 . 135 HIS C C 175.76 0.1 1 695 . 135 HIS CA C 53.28 0.1 1 696 . 135 HIS CB C 34.19 0.1 1 697 . 135 HIS N N 123.88 0.1 1 698 . 136 VAL H H 8.83 0.02 1 699 . 136 VAL HA H 4.44 0.02 1 700 . 136 VAL C C 176.43 0.1 1 701 . 136 VAL CA C 64.76 0.1 1 702 . 136 VAL CB C 33.15 0.1 1 703 . 136 VAL N N 124.62 0.1 1 704 . 137 ILE H H 8.62 0.02 1 705 . 137 ILE HA H 5.12 0.02 1 706 . 137 ILE C C 175.18 0.1 1 707 . 137 ILE CA C 60.29 0.1 1 708 . 137 ILE CB C 42.51 0.1 1 709 . 137 ILE N N 120.87 0.1 1 710 . 138 THR H H 9.33 0.02 1 711 . 138 THR HA H 4.62 0.02 1 712 . 138 THR C C 173.16 0.1 1 713 . 138 THR CA C 61.12 0.1 1 714 . 138 THR CB C 69.15 0.1 1 715 . 138 THR N N 108.31 0.1 1 716 . 139 ASN H H 7.36 0.02 1 717 . 139 ASN HA H 4.78 0.02 1 718 . 139 ASN C C 172.30 0.1 1 719 . 139 ASN CA C 52.70 0.1 1 720 . 139 ASN CB C 43.15 0.1 1 721 . 139 ASN N N 117.47 0.1 1 722 . 140 VAL H H 8.14 0.02 1 723 . 140 VAL C C 176.84 0.1 1 724 . 140 VAL CA C 62.46 0.1 1 725 . 140 VAL CB C 32.21 0.1 1 726 . 140 VAL N N 118.12 0.1 1 727 . 141 LEU H H 10.88 0.02 1 728 . 141 LEU HA H 4.16 0.02 1 729 . 141 LEU C C 175.71 0.1 1 730 . 141 LEU CA C 55.15 0.1 1 731 . 141 LEU CB C 41.25 0.1 1 732 . 141 LEU N N 131.54 0.1 1 733 . 142 GLN H H 7.81 0.02 1 734 . 142 GLN HA H 4.73 0.02 1 735 . 142 GLN C C 173.22 0.1 1 736 . 142 GLN CA C 52.13 0.1 1 737 . 142 GLN CB C 30.90 0.1 1 738 . 142 GLN N N 115.23 0.1 1 739 . 144 PRO C C 176.79 0.1 1 740 . 144 PRO CA C 63.08 0.1 1 741 . 144 PRO CB C 32.21 0.1 1 742 . 145 ALA H H 8.38 0.02 1 743 . 145 ALA C C 177.80 0.1 1 744 . 145 ALA CA C 52.74 0.1 1 745 . 145 ALA CB C 19.33 0.1 1 746 . 145 ALA N N 123.81 0.1 1 747 . 146 ASN H H 8.29 0.02 1 748 . 146 ASN C C 175.55 0.1 1 749 . 146 ASN CA C 53.25 0.1 1 750 . 146 ASN CB C 38.85 0.1 1 751 . 146 ASN N N 117.89 0.1 1 stop_ save_