data_4171 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and C beta Assignments of the Anti-gp120 Antibody Fv Fragment Complexed with an Antigenic Peptide ; _BMRB_accession_number 4171 _BMRB_flat_file_name bmr4171.str _Entry_type original _Submission_date 1998-08-03 _Accession_date 1998-08-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The assignment are reported for the Fv complexed with an antigenic peptide comprising the full epitope of the V3 loop of gp120 (HIV-1). Only the backbone chemical shifts of the isotope- labelled Fv are submitted. The unlabeled peptide is being currently assigned and investigated by isotope-filtering NMR techniques. The Fv consists of two non-covalently linked chains marked in this submission by segments L (light chain) and H (heavy chain). The chemical shifts of the two chains are given in separate loops. The numbering of the residues for the whole Fv may be either sequential (1-231) or chain-specific: 1-112 for the light chain and 1-119 for the heavy chain. The second type of numbering is submitted as the author sequence code. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tugarinov Vitali . . 2 Levy Rina . . 3 Dahan-Shokoroy Adi . . 4 Anglister Jacob . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 449 "13C chemical shifts" 431 "15N chemical shifts" 208 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-02 original author . stop_ _Original_release_date 2000-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone and C beta Assignments of the Anti-gp120 Antibody Fv Fragment Complexed with an Antigenic Peptide ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99169966 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tugarinov Vitali . . 2 Levy Rina . . 3 Dahan-Shokoroy Adi . . 4 Anglister Jacob . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 13 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 193 _Page_last 194 _Year 1999 _Details . loop_ _Keyword 'anti-gp120 antibody' 'Heteronuclear NMR' 'Resonance Assignments' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Zvi, A., Kustanovich, I., Levy, R., Matsushita, M., Richalet-Secordel, P., Regenmortel, M. H. V., and Anglister, J., "Mapping of the Antigenic Determinant Recognized by an Anti-Gp120 HIV Neutralizing Antibody by Two-Dimensional NMR. Eur. J. Biochem. 119: 178-187 (1995). ; _Citation_title 'NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7538073 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zvi A . . 2 Kustanovich I . . 3 Feigelson D . . 4 Levy R . . 5 Eisenstein M . . 6 Matsushita S . . 7 Richalet-Secordel P . . 8 Regenmortel 'M H' H. . 9 Anglister J . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 229 _Journal_issue 1 _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 178 _Page_last 187 _Year 1995 _Details ; The 24-amino-acid peptide RP135 (NNTRKSIRIQRGPGRAFVTIGKIG) corresponds in its amino acid sequence to the principal neutralizing determinant of the human immunodeficiency virus type-1, IIIB isolate (HIV-1IIIB, residues 308-331 of the envelope glycoprotein gp120). In order to map the antigenic determinant recognized by 0.5 beta, the complex of RP135 with an anti-gp120 HIV neutralizing antibody, 0.5 beta, which cross reacts with the peptide, was studied by using two-dimensional NMR spectroscopy. A combination of homonuclear Hartmann Hahn two-dimensional experiment and roating-frame Overhauser enhancement spectroscopy of the Fab/peptide complex measured in H2O was used to eliminate the resonances of the Fab and the tightly bound peptide residues and to obtain sequential assignments for those parts of the peptide which retain considerable mobility upon binding. In this manner, a total of 14 residues (Ser6-Thr19) were shown to be part of the antigenic determinant recognized by the antibody 0.5 beta. Lys5 and Ile20 were found to retain considerable mobility in the bound peptide while their amide protons undergo significant change in chemical shift upon binding. This observation suggests that these two residues are at the boundaries of the determinant recognized by the antibody. Competitive binding experiments using truncated peptides strongly support the NMR observations. ; save_ ################################## # Molecular system description # ################################## save_system_0.5bFv _Saveframe_category molecular_system _Mol_system_name '0.5b antibody Fv - V3 antigen' _Abbreviation_common 0.5bFv/P1053 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FvL $FvL FvH $FvH stop_ _System_molecular_weight 27872 _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details 'System MW is the MW of the labeled Fv + unlabeled peptide' save_ ######################## # Monomeric polymers # ######################## save_FvL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'light chain' _Abbreviation_common FvL _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; DIVLTQSPASLAVSLGQRAT ISCKASQSVDYDGDSYMNWY QQKPGQPPKLLIYAASNLES GIPARFSGSGSRTDFTLNIH PVEEEDAATYYCQQSNEDPF TFGSGTKLEIKR ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 ILE 3 VAL 4 LEU 5 THR 6 GLN 7 SER 8 PRO 9 ALA 10 SER 11 LEU 12 ALA 13 VAL 14 SER 15 LEU 16 GLY 17 GLN 18 ARG 19 ALA 20 THR 21 ILE 22 SER 23 CYS 24 LYS 25 ALA 26 SER 27 GLN 28 SER 29 VAL 30 ASP 31 TYR 32 ASP 33 GLY 34 ASP 35 SER 36 TYR 37 MET 38 ASN 39 TRP 40 TYR 41 GLN 42 GLN 43 LYS 44 PRO 45 GLY 46 GLN 47 PRO 48 PRO 49 LYS 50 LEU 51 LEU 52 ILE 53 TYR 54 ALA 55 ALA 56 SER 57 ASN 58 LEU 59 GLU 60 SER 61 GLY 62 ILE 63 PRO 64 ALA 65 ARG 66 PHE 67 SER 68 GLY 69 SER 70 GLY 71 SER 72 ARG 73 THR 74 ASP 75 PHE 76 THR 77 LEU 78 ASN 79 ILE 80 HIS 81 PRO 82 VAL 83 GLU 84 GLU 85 GLU 86 ASP 87 ALA 88 ALA 89 THR 90 TYR 91 TYR 92 CYS 93 GLN 94 GLN 95 SER 96 ASN 97 GLU 98 ASP 99 PRO 100 PHE 101 THR 102 PHE 103 GLY 104 SER 105 GLY 106 THR 107 LYS 108 LEU 109 GLU 110 ILE 111 LYS 112 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1IQW "Crystal Structure Of The Fab Fragment Of The Mouse Anti- Human Fas Antibody Hfe7a" 100.00 218 97.32 97.32 4.31e-72 PDB 1QNZ "Nmr Structure Of The 0.5b Anti-hiv Antibody Complex With The Gp120 V3 Peptide" 100.00 112 100.00 100.00 1.72e-76 DBJ BAH95819 "immunoglobulin light chain variable region [Mus musculus]" 86.61 97 96.91 96.91 1.63e-61 EMBL CAA75909 "variable region of immunoglobulin kappa light chain [Mus musculus]" 88.39 119 98.99 98.99 1.79e-64 EMBL CAA80931 "immunoglobulin kappa light chain [Mus musculus]" 80.36 90 98.89 98.89 5.76e-58 EMBL CAA80933 "immunoglobulin kappa light chain [Mus musculus]" 78.57 88 98.86 98.86 1.01e-56 EMBL CAA80935 "immunoglobulin kappa light chain [Mus musculus]" 75.89 85 98.82 98.82 1.17e-54 EMBL CAA80937 "immunoglobulin kappa light chain [Mus musculus]" 77.68 87 98.85 98.85 5.23e-56 GB AAA39088 "immunoglobulin light chain, partial [Mus musculus domesticus]" 99.11 111 100.00 100.00 1.53e-75 GB AAA51113 "IgK, partial [Mus musculus domesticus]" 100.00 117 97.32 98.21 1.26e-73 GB AAA68538 "immunoglobulin kappa light chain, variable region, partial [Mus musculus]" 67.86 76 97.37 97.37 1.79e-46 GB AAA68560 "immunoglobulin kappa light chain variable region, partial [Mus musculus]" 86.61 97 96.91 97.94 3.39e-62 GB AAA83114 "Ig kappa chain, partial [Mus musculus]" 84.82 95 97.89 98.95 4.82e-61 PIR S42193 "Ig kappa chain V region - mouse (fragment)" 72.32 81 97.53 97.53 8.05e-51 SP P01665 "RecName: Full=Ig kappa chain V-III region PC 7043" 99.11 111 99.10 99.10 3.39e-74 SP P01667 "RecName: Full=Ig kappa chain V-III region PC 6308" 99.11 111 97.30 98.20 1.18e-72 stop_ save_ save_FvH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'heavy chain' _Abbreviation_common FvH _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 119 _Mol_residue_sequence ; QVQLQQSGAELVKPGASVKM SCKAFGYTFTTYPIEWMKQN HGKSLEWIGNFHPYSDDTNY NEKFKGKAKLTVEKSSSTVY LEFSRLTSDDSAVYYCAIHY GSAYAMDYWGQGTSVTVSS ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 VAL 3 GLN 4 LEU 5 GLN 6 GLN 7 SER 8 GLY 9 ALA 10 GLU 11 LEU 12 VAL 13 LYS 14 PRO 15 GLY 16 ALA 17 SER 18 VAL 19 LYS 20 MET 21 SER 22 CYS 23 LYS 24 ALA 25 PHE 26 GLY 27 TYR 28 THR 29 PHE 30 THR 31 THR 32 TYR 33 PRO 34 ILE 35 GLU 36 TRP 37 MET 38 LYS 39 GLN 40 ASN 41 HIS 42 GLY 43 LYS 44 SER 45 LEU 46 GLU 47 TRP 48 ILE 49 GLY 50 ASN 51 PHE 52 HIS 53 PRO 54 TYR 55 SER 56 ASP 57 ASP 58 THR 59 ASN 60 TYR 61 ASN 62 GLU 63 LYS 64 PHE 65 LYS 66 GLY 67 LYS 68 ALA 69 LYS 70 LEU 71 THR 72 VAL 73 GLU 74 LYS 75 SER 76 SER 77 SER 78 THR 79 VAL 80 TYR 81 LEU 82 GLU 83 PHE 84 SER 85 ARG 86 LEU 87 THR 88 SER 89 ASP 90 ASP 91 SER 92 ALA 93 VAL 94 TYR 95 TYR 96 CYS 97 ALA 98 ILE 99 HIS 100 TYR 101 GLY 102 SER 103 ALA 104 TYR 105 ALA 106 MET 107 ASP 108 TYR 109 TRP 110 GLY 111 GLN 112 GLY 113 THR 114 SER 115 VAL 116 THR 117 VAL 118 SER 119 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FvL mouse 10090 Eukaryota Metazoa Mus musculus $FvH mouse 10090 Eukaryota Metazoa Mus musculus 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 $FvL 'recombinant technology' 'E. coli' Escherichia coli . plasmid pTb11 $FvH 'recombinant technology' 'E. coli' Escherichia coli . plasmid pTb11 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 $FvL 0.6 mM '[U-95% 13C; U-95% 15N]' $FvH 0.6 mM '[U-95% 13C; U-95% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600.13 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500.13 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.05 n/a temperature 310 0.05 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 _Indirect_shift_ratio TSP C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144954 H20 H 1 protons ppm 0.00 . indirect . . . . TSP N 15 'methyl protons' ppm 0.00 . indirect . . . 0.10132914 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 FvL _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 ASP HA H 4.49 0.02 1 2 . 1 ASP C C 172.6 0.15 1 3 . 1 ASP CA C 53.2 0.15 1 4 . 2 ILE H H 8.90 0.02 1 5 . 2 ILE HA H 3.79 0.02 1 6 . 2 ILE C C 175.1 0.15 1 7 . 2 ILE CA C 63.0 0.15 1 8 . 2 ILE N N 122.5 0.15 1 9 . 3 VAL H H 8.62 0.02 1 10 . 3 VAL HA H 4.11 0.02 1 11 . 3 VAL C C 176.1 0.15 1 12 . 3 VAL CA C 62.4 0.15 1 13 . 3 VAL N N 131.2 0.15 1 14 . 4 LEU H H 9.14 0.02 1 15 . 4 LEU HA H 5.32 0.02 1 16 . 4 LEU C C 176.6 0.15 1 17 . 4 LEU CA C 53.1 0.15 1 18 . 4 LEU N N 130.1 0.15 1 19 . 5 THR H H 9.44 0.02 1 20 . 5 THR HA H 4.59 0.02 1 21 . 5 THR CA C 61.7 0.15 1 22 . 5 THR N N 120.2 0.15 1 23 . 6 GLN C C 174.9 0.15 1 24 . 6 GLN CA C 54.6 0.15 1 25 . 7 SER H H 8.77 0.02 1 26 . 7 SER HA H 4.64 0.02 1 27 . 7 SER CA C 55.5 0.15 1 28 . 7 SER N N 117.9 0.15 1 29 . 9 ALA HA H 4.60 0.02 1 30 . 9 ALA C C 178.9 0.15 1 31 . 9 ALA CA C 54.7 0.15 1 32 . 10 SER H H 7.77 0.02 1 33 . 10 SER HA H 5.24 0.02 1 34 . 10 SER C C 171.9 0.15 1 35 . 10 SER CA C 56.8 0.15 1 36 . 10 SER N N 110.9 0.15 1 37 . 11 LEU H H 8.92 0.02 1 38 . 11 LEU HA H 4.64 0.02 1 39 . 11 LEU C C 173.0 0.15 1 40 . 11 LEU CA C 54.7 0.15 1 41 . 11 LEU N N 124.9 0.15 1 42 . 12 ALA H H 8.48 0.02 1 43 . 12 ALA HA H 5.48 0.02 1 44 . 12 ALA C C 176.5 0.15 1 45 . 12 ALA CA C 50.2 0.15 1 46 . 12 ALA N N 128.1 0.15 1 47 . 13 VAL H H 8.46 0.02 1 48 . 13 VAL HA H 4.62 0.02 1 49 . 13 VAL C C 174.6 0.15 1 50 . 13 VAL CA C 59.1 0.15 1 51 . 13 VAL N N 118.8 0.15 1 52 . 14 SER H H 8.53 0.02 1 53 . 14 SER HA H 4.78 0.02 1 54 . 14 SER C C 173.7 0.15 1 55 . 14 SER CA C 58.5 0.15 1 56 . 14 SER N N 120.5 0.15 1 57 . 15 LEU H H 8.43 0.02 1 58 . 15 LEU HA H 3.72 0.02 1 59 . 15 LEU C C 178.6 0.15 1 60 . 15 LEU CA C 56.6 0.15 1 61 . 15 LEU N N 121.4 0.15 1 62 . 16 GLY H H 8.80 0.02 1 63 . 16 GLY HA2 H 3.58 0.02 1 64 . 16 GLY HA3 H 4.34 0.02 1 65 . 16 GLY C C 173.9 0.15 1 66 . 16 GLY CA C 45.2 0.15 1 67 . 16 GLY N N 110.7 0.15 1 68 . 17 GLN H H 7.53 0.02 1 69 . 17 GLN HA H 4.56 0.02 1 70 . 17 GLN C C 173.5 0.15 1 71 . 17 GLN CA C 55.0 0.15 1 72 . 17 GLN N N 117.6 0.15 1 73 . 18 ARG H H 7.97 0.02 1 74 . 18 ARG HA H 5.21 0.02 1 75 . 18 ARG C C 175.2 0.15 1 76 . 18 ARG CA C 54.8 0.15 1 77 . 18 ARG N N 118.8 0.15 1 78 . 19 ALA H H 9.05 0.02 1 79 . 19 ALA HA H 4.71 0.02 1 80 . 19 ALA C C 175.5 0.15 1 81 . 19 ALA CA C 50.2 0.15 1 82 . 19 ALA N N 127.9 0.15 1 83 . 20 THR H H 7.78 0.02 1 84 . 20 THR HA H 4.94 0.02 1 85 . 20 THR C C 172.7 0.15 1 86 . 20 THR CA C 62.1 0.15 1 87 . 20 THR N N 117.6 0.15 1 88 . 21 ILE H H 9.04 0.02 1 89 . 21 ILE HA H 4.38 0.02 1 90 . 21 ILE C C 174.0 0.15 1 91 . 21 ILE CA C 61.0 0.15 1 92 . 21 ILE N N 127.6 0.15 1 93 . 22 SER H H 9.00 0.02 1 94 . 22 SER HA H 5.56 0.02 1 95 . 22 SER C C 174.0 0.15 1 96 . 22 SER CA C 57.8 0.15 1 97 . 22 SER N N 120.1 0.15 1 98 . 23 CYS H H 9.30 0.02 1 99 . 23 CYS HA H 5.23 0.02 1 100 . 23 CYS C C 171.8 0.15 1 101 . 23 CYS CA C 56.5 0.15 1 102 . 23 CYS N N 123.4 0.15 1 103 . 24 LYS H H 8.83 0.02 1 104 . 24 LYS HA H 5.66 0.02 1 105 . 24 LYS C C 175.3 0.15 1 106 . 24 LYS CA C 54.0 0.15 1 107 . 24 LYS N N 127.7 0.15 1 108 . 25 ALA H H 9.47 0.02 1 109 . 25 ALA HA H 5.35 0.02 1 110 . 25 ALA C C 178.1 0.15 1 111 . 25 ALA CA C 50.0 0.15 1 112 . 25 ALA N N 128.0 0.15 1 113 . 26 SER H H 8.46 0.02 1 114 . 26 SER HA H 4.14 0.02 1 115 . 26 SER C C 173.4 0.15 1 116 . 26 SER CA C 60.5 0.15 1 117 . 26 SER N N 114.4 0.15 1 118 . 27 GLN H H 7.34 0.02 1 119 . 27 GLN HA H 4.43 0.02 1 120 . 27 GLN C C 172.7 0.15 1 121 . 27 GLN CA C 53.8 0.15 1 122 . 27 GLN N N 116.9 0.15 1 123 . 28 SER H H 8.30 0.02 1 124 . 28 SER HA H 4.00 0.02 1 125 . 28 SER C C 176.3 0.15 1 126 . 28 SER CA C 57.9 0.15 1 127 . 28 SER N N 110.7 0.15 1 128 . 29 VAL H H 8.26 0.02 1 129 . 29 VAL HA H 4.53 0.02 1 130 . 29 VAL C C 176.3 0.15 1 131 . 29 VAL CA C 59.8 0.15 1 132 . 29 VAL N N 116.5 0.15 1 133 . 30 ASP H H 8.15 0.02 1 134 . 30 ASP HA H 5.67 0.02 1 135 . 30 ASP C C 176.8 0.15 1 136 . 30 ASP CA C 54.3 0.15 1 137 . 30 ASP N N 127.3 0.15 1 138 . 31 TYR H H 9.52 0.02 1 139 . 31 TYR HA H 4.55 0.02 1 140 . 31 TYR C C 176.5 0.15 1 141 . 31 TYR CA C 59.1 0.15 1 142 . 31 TYR N N 122.4 0.15 1 143 . 32 ASP H H 8.86 0.02 1 144 . 32 ASP HA H 4.03 0.02 1 145 . 32 ASP C C 174.9 0.15 1 146 . 32 ASP CA C 54.7 0.15 1 147 . 32 ASP N N 130.6 0.15 1 148 . 33 GLY H H 8.43 0.02 1 149 . 33 GLY HA2 H 3.57 0.02 1 150 . 33 GLY HA3 H 4.20 0.02 1 151 . 33 GLY C C 175.6 0.15 1 152 . 33 GLY CA C 45.5 0.15 1 153 . 33 GLY N N 103.2 0.15 1 154 . 34 ASP H H 7.89 0.02 1 155 . 34 ASP HA H 5.09 0.02 1 156 . 34 ASP C C 175.1 0.15 1 157 . 34 ASP CA C 52.9 0.15 1 158 . 34 ASP N N 118.9 0.15 1 159 . 35 SER H H 9.01 0.02 1 160 . 35 SER HA H 5.03 0.02 1 161 . 35 SER C C 174.2 0.15 1 162 . 35 SER CA C 58.0 0.15 1 163 . 35 SER N N 117.3 0.15 1 164 . 36 TYR H H 8.30 0.02 1 165 . 36 TYR HA H 3.98 0.02 1 166 . 36 TYR C C 174.1 0.15 1 167 . 36 TYR CA C 58.4 0.15 1 168 . 36 TYR N N 128.6 0.15 1 169 . 37 MET H H 7.04 0.02 1 170 . 37 MET HA H 4.87 0.02 1 171 . 37 MET C C 173.0 0.15 1 172 . 37 MET CA C 52.6 0.15 1 173 . 37 MET N N 120.2 0.15 1 174 . 38 ASN H H 9.09 0.02 1 175 . 38 ASN HA H 5.25 0.02 1 176 . 38 ASN C C 173.2 0.15 1 177 . 38 ASN CA C 50.7 0.15 1 178 . 38 ASN N N 125.1 0.15 1 179 . 39 TRP H H 8.74 0.02 1 180 . 39 TRP HA H 5.61 0.02 1 181 . 39 TRP C C 175.3 0.15 1 182 . 39 TRP CA C 55.7 0.15 1 183 . 39 TRP N N 115.4 0.15 1 184 . 40 TYR H H 9.53 0.02 1 185 . 40 TYR HA H 5.36 0.02 1 186 . 40 TYR C C 174.2 0.15 1 187 . 40 TYR CA C 56.3 0.15 1 188 . 40 TYR N N 118.0 0.15 1 189 . 41 GLN H H 9.31 0.02 1 190 . 41 GLN HA H 4.36 0.02 1 191 . 41 GLN C C 174.0 0.15 1 192 . 41 GLN CA C 53.5 0.15 1 193 . 41 GLN N N 122.0 0.15 1 194 . 42 GLN H H 9.67 0.02 1 195 . 42 GLN HA H 4.83 0.02 1 196 . 42 GLN C C 174.6 0.15 1 197 . 42 GLN CA C 55.0 0.15 1 198 . 42 GLN N N 127.9 0.15 1 199 . 43 LYS H H 8.75 0.02 1 200 . 43 LYS HA H 4.61 0.02 1 201 . 43 LYS CA C 54.2 0.15 1 202 . 43 LYS N N 132.2 0.15 1 203 . 45 GLY HA2 H 3.79 0.02 1 204 . 45 GLY HA3 H 4.11 0.02 1 205 . 45 GLY C C 173.9 0.15 1 206 . 45 GLY CA C 45.2 0.15 1 207 . 46 GLN H H 7.93 0.02 1 208 . 46 GLN HA H 4.92 0.02 1 209 . 46 GLN CA C 53.1 0.15 1 210 . 46 GLN N N 119.8 0.15 1 211 . 48 PRO HA H 3.82 0.02 1 212 . 48 PRO C C 172.6 0.15 1 213 . 48 PRO CA C 62.3 0.15 1 214 . 49 LYS H H 8.80 0.02 1 215 . 49 LYS HA H 4.35 0.02 1 216 . 49 LYS C C 176.0 0.15 1 217 . 49 LYS CA C 54.0 0.15 1 218 . 49 LYS N N 120.6 0.15 1 219 . 50 LEU H H 8.89 0.02 1 220 . 50 LEU HA H 3.76 0.02 1 221 . 50 LEU C C 174.6 0.15 1 222 . 50 LEU CA C 56.5 0.15 1 223 . 50 LEU N N 129.1 0.15 1 224 . 51 LEU H H 8.52 0.02 1 225 . 51 LEU HA H 4.54 0.02 1 226 . 51 LEU C C 175.3 0.15 1 227 . 51 LEU CA C 55.0 0.15 1 228 . 51 LEU N N 123.1 0.15 1 229 . 52 ILE H H 6.93 0.02 1 230 . 52 ILE HA H 5.01 0.02 1 231 . 52 ILE C C 174.1 0.15 1 232 . 52 ILE CA C 57.5 0.15 1 233 . 52 ILE N N 115.8 0.15 1 234 . 53 TYR H H 9.02 0.02 1 235 . 53 TYR HA H 5.75 0.02 1 236 . 53 TYR C C 174.5 0.15 1 237 . 53 TYR CA C 53.0 0.15 1 238 . 53 TYR N N 121.9 0.15 1 239 . 54 ALA H H 8.10 0.02 1 240 . 54 ALA HA H 4.20 0.02 1 241 . 54 ALA C C 179.2 0.15 1 242 . 54 ALA CA C 53.0 0.15 1 243 . 54 ALA N N 123.3 0.15 1 244 . 55 ALA H H 9.23 0.02 1 245 . 55 ALA HA H 3.45 0.02 1 246 . 55 ALA C C 179.5 0.15 1 247 . 55 ALA CA C 57.4 0.15 1 248 . 55 ALA N N 115.3 0.15 1 249 . 56 SER H H 8.55 0.02 1 250 . 56 SER HA H 4.57 0.02 1 251 . 56 SER C C 174.7 0.15 1 252 . 56 SER CA C 57.7 0.15 1 253 . 56 SER N N 110.0 0.15 1 254 . 57 ASN H H 7.76 0.02 1 255 . 57 ASN HA H 4.58 0.02 1 256 . 57 ASN C C 172.3 0.15 1 257 . 57 ASN CA C 53.1 0.15 1 258 . 57 ASN N N 121.9 0.15 1 259 . 58 LEU H H 8.50 0.02 1 260 . 58 LEU HA H 4.35 0.02 1 261 . 58 LEU C C 177.6 0.15 1 262 . 58 LEU CA C 55.5 0.15 1 263 . 58 LEU N N 125.9 0.15 1 264 . 59 GLU H H 8.03 0.02 1 265 . 59 GLU HA H 4.86 0.02 1 266 . 59 GLU C C 176.0 0.15 1 267 . 59 GLU CA C 55.8 0.15 1 268 . 59 GLU N N 127.8 0.15 1 269 . 60 SER H H 8.58 0.02 1 270 . 60 SER HA H 4.22 0.02 1 271 . 60 SER C C 172.1 0.15 1 272 . 60 SER CA C 60.2 0.15 1 273 . 60 SER N N 119.8 0.15 1 274 . 61 GLY H H 8.74 0.02 1 275 . 61 GLY HA2 H 3.68 0.02 1 276 . 61 GLY HA3 H 4.24 0.02 1 277 . 61 GLY C C 174.0 0.15 1 278 . 61 GLY CA C 45.2 0.15 1 279 . 61 GLY N N 114.0 0.15 1 280 . 62 ILE H H 7.75 0.02 1 281 . 62 ILE HA H 4.52 0.02 1 282 . 62 ILE CA C 55.4 0.15 1 283 . 62 ILE N N 124.3 0.15 1 284 . 63 PRO HA H 4.56 0.02 1 285 . 63 PRO C C 176.5 0.15 1 286 . 63 PRO CA C 63.2 0.15 1 287 . 64 ALA H H 8.30 0.02 1 288 . 64 ALA HA H 4.35 0.02 1 289 . 64 ALA C C 176.7 0.15 1 290 . 64 ALA CA C 53.5 0.15 1 291 . 64 ALA N N 120.6 0.15 1 292 . 65 ARG H H 6.79 0.02 1 293 . 65 ARG HA H 4.23 0.02 1 294 . 65 ARG C C 175.7 0.15 1 295 . 65 ARG CA C 56.7 0.15 1 296 . 65 ARG N N 113.8 0.15 1 297 . 66 PHE H H 7.64 0.02 1 298 . 66 PHE HA H 4.81 0.02 1 299 . 66 PHE C C 174.1 0.15 1 300 . 66 PHE CA C 57.8 0.15 1 301 . 66 PHE N N 118.9 0.15 1 302 . 67 SER H H 8.75 0.02 1 303 . 67 SER HA H 4.60 0.02 1 304 . 67 SER C C 172.6 0.15 1 305 . 67 SER CA C 57.3 0.15 1 306 . 67 SER N N 112.0 0.15 1 307 . 68 GLY H H 8.89 0.02 1 308 . 68 GLY HA2 H 3.80 0.02 1 309 . 68 GLY HA3 H 5.22 0.02 1 310 . 68 GLY C C 172.6 0.15 1 311 . 68 GLY CA C 44.3 0.15 1 312 . 68 GLY N N 110.7 0.15 1 313 . 69 SER H H 8.73 0.02 1 314 . 69 SER HA H 4.83 0.02 1 315 . 69 SER C C 173.9 0.15 1 316 . 69 SER CA C 57.0 0.15 1 317 . 69 SER N N 113.5 0.15 1 318 . 70 GLY H H 8.38 0.02 1 319 . 70 GLY HA2 H 3.55 0.02 1 320 . 70 GLY HA3 H 5.00 0.02 1 321 . 70 GLY C C 171.7 0.15 1 322 . 70 GLY CA C 45.1 0.15 1 323 . 70 GLY N N 110.3 0.15 1 324 . 71 SER H H 6.85 0.02 1 325 . 71 SER HA H 4.44 0.02 1 326 . 71 SER C C 173.4 0.15 1 327 . 71 SER CA C 58.2 0.15 1 328 . 71 SER N N 107.7 0.15 1 329 . 72 ARG H H 9.17 0.02 1 330 . 72 ARG HA H 3.88 0.02 1 331 . 72 ARG C C 173.4 0.15 1 332 . 72 ARG CA C 60.8 0.15 1 333 . 72 ARG N N 117.9 0.15 1 334 . 73 THR H H 7.82 0.02 1 335 . 73 THR HA H 4.88 0.02 1 336 . 73 THR C C 173.6 0.15 1 337 . 73 THR CA C 61.1 0.15 1 338 . 73 THR N N 110.2 0.15 1 339 . 74 ASP H H 7.29 0.02 1 340 . 74 ASP HA H 5.32 0.02 1 341 . 74 ASP C C 173.2 0.15 1 342 . 74 ASP CA C 54.9 0.15 1 343 . 74 ASP N N 122.6 0.15 1 344 . 75 PHE H H 8.65 0.02 1 345 . 75 PHE HA H 5.27 0.02 1 346 . 75 PHE C C 175.7 0.15 1 347 . 75 PHE CA C 57.3 0.15 1 348 . 75 PHE N N 120.6 0.15 1 349 . 76 THR H H 8.93 0.02 1 350 . 76 THR HA H 5.43 0.02 1 351 . 76 THR C C 171.7 0.15 1 352 . 76 THR CA C 61.2 0.15 1 353 . 76 THR N N 115.7 0.15 1 354 . 77 LEU H H 8.71 0.02 1 355 . 77 LEU HA H 4.37 0.02 1 356 . 77 LEU C C 173.9 0.15 1 357 . 77 LEU CA C 53.0 0.15 1 358 . 77 LEU N N 126.9 0.15 1 359 . 78 ASN H H 8.99 0.02 1 360 . 78 ASN HA H 5.51 0.02 1 361 . 78 ASN C C 173.8 0.15 1 362 . 78 ASN CA C 51.6 0.15 1 363 . 78 ASN N N 124.2 0.15 1 364 . 79 ILE H H 8.62 0.02 1 365 . 79 ILE HA H 4.32 0.02 1 366 . 79 ILE C C 175.7 0.15 1 367 . 79 ILE CA C 60.0 0.15 1 368 . 79 ILE N N 120.7 0.15 1 369 . 80 HIS H H 8.58 0.02 1 370 . 80 HIS HA H 4.80 0.02 1 371 . 80 HIS CA C 53.6 0.15 1 372 . 80 HIS N N 123.4 0.15 1 373 . 81 PRO HA H 4.12 0.02 1 374 . 81 PRO C C 175.3 0.15 1 375 . 81 PRO CA C 62.6 0.15 1 376 . 82 VAL H H 8.05 0.02 1 377 . 82 VAL HA H 3.77 0.02 1 378 . 82 VAL C C 175.9 0.15 1 379 . 82 VAL CA C 63.8 0.15 1 380 . 82 VAL N N 119.1 0.15 1 381 . 83 GLU H H 8.99 0.02 1 382 . 83 GLU HA H 4.63 0.02 1 383 . 83 GLU C C 176.8 0.15 1 384 . 83 GLU CA C 54.4 0.15 1 385 . 83 GLU N N 128.6 0.15 1 386 . 84 GLU H H 8.96 0.02 1 387 . 84 GLU HA H 3.74 0.02 1 388 . 84 GLU C C 178.9 0.15 1 389 . 84 GLU CA C 60.4 0.15 1 390 . 84 GLU N N 121.2 0.15 1 391 . 85 GLU H H 8.41 0.02 1 392 . 85 GLU HA H 4.31 0.02 1 393 . 85 GLU C C 175.7 0.15 1 394 . 85 GLU CA C 57.2 0.15 1 395 . 85 GLU N N 113.6 0.15 1 396 . 86 ASP H H 7.94 0.02 1 397 . 86 ASP HA H 4.58 0.02 1 398 . 86 ASP C C 177.5 0.15 1 399 . 86 ASP CA C 54.7 0.15 1 400 . 86 ASP N N 118.9 0.15 1 401 . 87 ALA H H 7.16 0.02 1 402 . 87 ALA HA H 4.32 0.02 1 403 . 87 ALA C C 175.9 0.15 1 404 . 87 ALA CA C 54.2 0.15 1 405 . 87 ALA N N 123.9 0.15 1 406 . 88 ALA H H 8.24 0.02 1 407 . 88 ALA HA H 4.44 0.02 1 408 . 88 ALA C C 174.9 0.15 1 409 . 88 ALA CA C 51.7 0.15 1 410 . 88 ALA N N 126.0 0.15 1 411 . 89 THR H H 8.01 0.02 1 412 . 89 THR HA H 5.14 0.02 1 413 . 89 THR C C 172.6 0.15 1 414 . 89 THR CA C 62.4 0.15 1 415 . 89 THR N N 114.4 0.15 1 416 . 90 TYR H H 8.92 0.02 1 417 . 90 TYR HA H 5.35 0.02 1 418 . 90 TYR C C 176.6 0.15 1 419 . 90 TYR CA C 56.9 0.15 1 420 . 90 TYR N N 124.0 0.15 1 421 . 91 TYR H H 9.38 0.02 1 422 . 91 TYR HA H 5.56 0.02 1 423 . 91 TYR C C 175.6 0.15 1 424 . 91 TYR CA C 57.9 0.15 1 425 . 91 TYR N N 120.4 0.15 1 426 . 92 CYS H H 7.40 0.02 1 427 . 92 CYS HA H 5.30 0.02 1 428 . 92 CYS C C 173.4 0.15 1 429 . 92 CYS CA C 53.1 0.15 1 430 . 92 CYS N N 116.0 0.15 1 431 . 93 GLN H H 8.18 0.02 1 432 . 93 GLN HA H 4.65 0.02 1 433 . 93 GLN C C 172.5 0.15 1 434 . 93 GLN CA C 55.0 0.15 1 435 . 93 GLN N N 122.7 0.15 1 436 . 94 GLN H H 8.31 0.02 1 437 . 94 GLN HA H 5.49 0.02 1 438 . 94 GLN C C 174.8 0.15 1 439 . 94 GLN CA C 51.9 0.15 1 440 . 94 GLN N N 124.1 0.15 1 441 . 95 SER H H 7.96 0.02 1 442 . 95 SER HA H 3.12 0.02 1 443 . 95 SER C C 173.1 0.15 1 444 . 95 SER CA C 53.9 0.15 1 445 . 95 SER N N 114.2 0.15 1 446 . 96 ASN H H 8.62 0.02 1 447 . 96 ASN HA H 3.78 0.02 1 448 . 96 ASN C C 173.5 0.15 1 449 . 96 ASN CA C 57.0 0.15 1 450 . 96 ASN N N 122.5 0.15 1 451 . 97 GLU H H 8.30 0.02 1 452 . 97 GLU HA H 4.38 0.02 1 453 . 97 GLU C C 175.0 0.15 1 454 . 97 GLU CA C 54.3 0.15 1 455 . 97 GLU N N 115.2 0.15 1 456 . 98 ASP H H 8.32 0.02 1 457 . 98 ASP HA H 4.27 0.02 1 458 . 98 ASP CA C 52.7 0.15 1 459 . 98 ASP N N 121.9 0.15 1 460 . 99 PRO HA H 4.67 0.02 1 461 . 99 PRO C C 174.5 0.15 1 462 . 99 PRO CA C 61.1 0.15 1 463 . 100 PHE H H 7.88 0.02 1 464 . 100 PHE HA H 4.23 0.02 1 465 . 100 PHE C C 175.4 0.15 1 466 . 100 PHE CA C 55.0 0.15 1 467 . 100 PHE N N 123.6 0.15 1 468 . 101 THR H H 7.04 0.02 1 469 . 101 THR HA H 5.15 0.02 1 470 . 101 THR C C 172.6 0.15 1 471 . 101 THR CA C 58.8 0.15 1 472 . 101 THR N N 107.6 0.15 1 473 . 102 PHE H H 9.00 0.02 1 474 . 102 PHE HA H 5.24 0.02 1 475 . 102 PHE C C 178.0 0.15 1 476 . 102 PHE CA C 56.4 0.15 1 477 . 102 PHE N N 117.9 0.15 1 478 . 103 GLY H H 9.26 0.02 1 479 . 103 GLY HA2 H 4.45 0.02 1 480 . 103 GLY HA3 H 4.57 0.02 1 481 . 103 GLY C C 174.2 0.15 1 482 . 103 GLY CA C 44.6 0.15 1 483 . 103 GLY N N 108.0 0.15 1 484 . 104 SER H H 8.02 0.02 1 485 . 104 SER HA H 4.65 0.02 1 486 . 104 SER C C 175.4 0.15 1 487 . 104 SER CA C 60.9 0.15 1 488 . 104 SER N N 110.9 0.15 1 489 . 105 GLY H H 7.04 0.02 1 490 . 105 GLY HA2 H 3.68 0.02 1 491 . 105 GLY HA3 H 4.11 0.02 1 492 . 105 GLY C C 172.6 0.15 1 493 . 105 GLY CA C 45.6 0.15 1 494 . 105 GLY N N 107.6 0.15 1 495 . 106 THR H H 8.02 0.02 1 496 . 106 THR HA H 4.84 0.02 1 497 . 106 THR C C 173.8 0.15 1 498 . 106 THR CA C 61.7 0.15 1 499 . 106 THR N N 118.2 0.15 1 500 . 107 LYS H H 8.40 0.02 1 501 . 107 LYS HA H 4.64 0.02 1 502 . 107 LYS C C 173.4 0.15 1 503 . 107 LYS CA C 56.5 0.15 1 504 . 107 LYS N N 129.7 0.15 1 505 . 108 LEU H H 9.13 0.02 1 506 . 108 LEU HA H 5.28 0.02 1 507 . 108 LEU C C 175.3 0.15 1 508 . 108 LEU CA C 54.7 0.15 1 509 . 108 LEU N N 130.9 0.15 1 510 . 109 GLU H H 9.10 0.02 1 511 . 109 GLU HA H 4.73 0.02 1 512 . 109 GLU C C 173.8 0.15 1 513 . 109 GLU CA C 54.0 0.15 1 514 . 109 GLU N N 126.8 0.15 1 515 . 110 ILE H H 8.48 0.02 1 516 . 110 ILE HA H 4.83 0.02 1 517 . 110 ILE C C 176.7 0.15 1 518 . 110 ILE CA C 58.1 0.15 1 519 . 110 ILE N N 121.0 0.15 1 520 . 111 LYS H H 8.27 0.02 1 521 . 111 LYS HA H 4.31 0.02 1 522 . 111 LYS C C 174.7 0.15 1 523 . 111 LYS CA C 55.5 0.15 1 524 . 111 LYS N N 129.4 0.15 1 525 . 112 ARG H H 8.11 0.02 1 526 . 112 ARG HA H 4.19 0.02 1 527 . 112 ARG CA C 57.2 0.15 1 528 . 112 ARG N N 130.2 0.15 1 stop_ save_ save_assigned_chemical_shifts_two _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 FvH _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 GLN HA H 4.29 0.02 1 2 . 1 GLN C C 176.8 0.15 1 3 . 1 GLN CA C 59.1 0.15 1 4 . 2 VAL H H 7.44 0.02 1 5 . 2 VAL HA H 3.76 0.02 1 6 . 2 VAL C C 175.6 0.15 1 7 . 2 VAL CA C 63.9 0.15 1 8 . 2 VAL N N 122.6 0.15 1 9 . 3 GLN H H 8.33 0.02 1 10 . 3 GLN HA H 4.47 0.02 1 11 . 3 GLN C C 173.3 0.15 1 12 . 3 GLN CA C 55.6 0.15 1 13 . 3 GLN N N 124.9 0.15 1 14 . 4 LEU H H 8.47 0.02 1 15 . 4 LEU HA H 5.03 0.02 1 16 . 4 LEU C C 175.7 0.15 1 17 . 4 LEU CA C 53.4 0.15 1 18 . 4 LEU N N 123.8 0.15 1 19 . 5 GLN H H 9.19 0.02 1 20 . 5 GLN HA H 4.91 0.02 1 21 . 5 GLN C C 176.4 0.15 1 22 . 5 GLN CA C 54.5 0.15 1 23 . 5 GLN N N 121.7 0.15 1 24 . 6 GLN H H 9.68 0.02 1 25 . 6 GLN HA H 5.58 0.02 1 26 . 6 GLN C C 176.2 0.15 1 27 . 6 GLN CA C 55.6 0.15 1 28 . 6 GLN N N 127.9 0.15 1 29 . 7 SER H H 7.65 0.02 1 30 . 7 SER HA H 4.41 0.02 1 31 . 7 SER C C 176.0 0.15 1 32 . 7 SER CA C 58.3 0.15 1 33 . 7 SER N N 113.8 0.15 1 34 . 8 GLY H H 8.59 0.02 1 35 . 8 GLY HA2 H 4.06 0.02 1 36 . 8 GLY HA3 H 4.06 0.02 1 37 . 8 GLY C C 172.2 0.15 1 38 . 8 GLY N N 107.2 0.15 1 39 . 9 ALA H H 7.99 0.02 1 40 . 9 ALA HA H 4.67 0.02 1 41 . 9 ALA C C 178.5 0.15 1 42 . 9 ALA CA C 53.1 0.15 1 43 . 9 ALA N N 118.9 0.15 1 44 . 10 GLU H H 8.48 0.02 1 45 . 10 GLU HA H 4.81 0.02 1 46 . 10 GLU C C 175.0 0.15 1 47 . 10 GLU CA C 55.1 0.15 1 48 . 10 GLU N N 118.5 0.15 1 49 . 11 LEU H H 8.56 0.02 1 50 . 11 LEU HA H 5.26 0.02 1 51 . 11 LEU C C 176.0 0.15 1 52 . 11 LEU CA C 54.7 0.15 1 53 . 11 LEU N N 128.0 0.15 1 54 . 12 VAL H H 8.77 0.02 1 55 . 12 VAL HA H 4.72 0.02 1 56 . 12 VAL C C 173.7 0.15 1 57 . 12 VAL CA C 59.1 0.15 1 58 . 12 VAL N N 120.7 0.15 1 59 . 13 LYS H H 7.96 0.02 1 60 . 13 LYS HA H 4.79 0.02 1 61 . 13 LYS CA C 53.7 0.15 1 62 . 13 LYS N N 121.1 0.15 1 63 . 14 PRO HA H 3.90 0.02 1 64 . 14 PRO C C 178.1 0.15 1 65 . 14 PRO CA C 63.4 0.15 1 66 . 15 GLY H H 9.72 0.02 1 67 . 15 GLY HA2 H 3.70 0.02 1 68 . 15 GLY HA3 H 4.19 0.02 1 69 . 15 GLY C C 173.9 0.15 1 70 . 15 GLY CA C 45.2 0.15 1 71 . 15 GLY N N 112.9 0.15 1 72 . 16 ALA H H 7.62 0.02 1 73 . 16 ALA HA H 4.54 0.02 1 74 . 16 ALA C C 174.3 0.15 1 75 . 16 ALA CA C 51.6 0.15 1 76 . 16 ALA N N 123.7 0.15 1 77 . 17 SER H H 7.70 0.02 1 78 . 17 SER HA H 5.29 0.02 1 79 . 17 SER C C 173.0 0.15 1 80 . 17 SER CA C 56.5 0.15 1 81 . 17 SER N N 110.1 0.15 1 82 . 18 VAL H H 8.37 0.02 1 83 . 18 VAL HA H 4.52 0.02 1 84 . 18 VAL C C 171.6 0.15 1 85 . 18 VAL CA C 59.6 0.15 1 86 . 18 VAL N N 117.5 0.15 1 87 . 19 LYS H H 8.46 0.02 1 88 . 19 LYS HA H 4.94 0.02 1 89 . 19 LYS C C 174.3 0.15 1 90 . 19 LYS CA C 55.6 0.15 1 91 . 19 LYS N N 127.2 0.15 1 92 . 20 MET H H 8.93 0.02 1 93 . 20 MET HA H 4.65 0.02 1 94 . 20 MET C C 174.5 0.15 1 95 . 20 MET CA C 54.6 0.15 1 96 . 20 MET N N 127.3 0.15 1 97 . 21 SER H H 9.11 0.02 1 98 . 21 SER HA H 5.14 0.02 1 99 . 21 SER C C 174.4 0.15 1 100 . 21 SER CA C 56.8 0.15 1 101 . 21 SER N N 113.2 0.15 1 102 . 22 CYS H H 8.79 0.02 1 103 . 22 CYS HA H 4.69 0.02 1 104 . 22 CYS C C 171.3 0.15 1 105 . 22 CYS CA C 56.8 0.15 1 106 . 22 CYS N N 123.3 0.15 1 107 . 23 LYS H H 9.11 0.02 1 108 . 23 LYS HA H 4.80 0.02 1 109 . 23 LYS C C 175.3 0.15 1 110 . 23 LYS CA C 55.6 0.15 1 111 . 23 LYS N N 129.0 0.15 1 112 . 24 ALA H H 8.80 0.02 1 113 . 24 ALA HA H 5.27 0.02 1 114 . 24 ALA C C 176.4 0.15 1 115 . 24 ALA CA C 51.4 0.15 1 116 . 24 ALA N N 133.4 0.15 1 117 . 25 PHE H H 8.74 0.02 1 118 . 25 PHE HA H 4.60 0.02 1 119 . 25 PHE C C 173.8 0.15 1 120 . 25 PHE CA C 58.1 0.15 1 121 . 25 PHE N N 113.1 0.15 1 122 . 26 GLY H H 8.52 0.02 1 123 . 26 GLY HA2 H 3.56 0.02 1 124 . 26 GLY HA3 H 4.39 0.02 1 125 . 26 GLY C C 173.3 0.15 1 126 . 26 GLY CA C 45.5 0.15 1 127 . 26 GLY N N 106.1 0.15 1 128 . 27 TYR H H 7.27 0.02 1 129 . 27 TYR HA H 4.94 0.02 1 130 . 27 TYR CA C 55.7 0.15 1 131 . 27 TYR N N 113.4 0.15 1 132 . 29 PHE HA H 4.36 0.02 1 133 . 29 PHE C C 176.1 0.15 1 134 . 29 PHE CA C 60.2 0.15 1 135 . 30 THR H H 7.67 0.02 1 136 . 30 THR HA H 4.63 0.02 1 137 . 30 THR C C 173.8 0.15 1 138 . 30 THR CA C 62.6 0.15 1 139 . 30 THR N N 100.3 0.15 1 140 . 31 THR H H 7.88 0.02 1 141 . 31 THR HA H 4.16 0.02 1 142 . 31 THR C C 172.9 0.15 1 143 . 31 THR CA C 65.7 0.15 1 144 . 31 THR N N 113.8 0.15 1 145 . 32 TYR H H 6.72 0.02 1 146 . 32 TYR HA H 4.92 0.02 1 147 . 32 TYR CA C 54.8 0.15 1 148 . 32 TYR N N 114.7 0.15 1 149 . 33 PRO HA H 4.62 0.02 1 150 . 33 PRO C C 175.8 0.15 1 151 . 33 PRO CA C 61.9 0.15 1 152 . 34 ILE H H 8.50 0.02 1 153 . 34 ILE HA H 4.51 0.02 1 154 . 34 ILE C C 175.4 0.15 1 155 . 34 ILE CA C 61.2 0.15 1 156 . 34 ILE N N 120.1 0.15 1 157 . 35 GLU H H 8.95 0.02 1 158 . 35 GLU HA H 4.82 0.02 1 159 . 35 GLU C C 176.3 0.15 1 160 . 35 GLU CA C 53.7 0.15 1 161 . 35 GLU N N 124.4 0.15 1 162 . 36 TRP H H 8.50 0.02 1 163 . 36 TRP HA H 5.69 0.02 1 164 . 36 TRP C C 175.6 0.15 1 165 . 36 TRP CA C 56.0 0.15 1 166 . 36 TRP N N 117.1 0.15 1 167 . 37 MET H H 9.57 0.02 1 168 . 37 MET HA H 5.36 0.02 1 169 . 37 MET C C 173.8 0.15 1 170 . 37 MET CA C 54.5 0.15 1 171 . 37 MET N N 121.0 0.15 1 172 . 38 LYS H H 9.18 0.02 1 173 . 38 LYS HA H 4.49 0.02 1 174 . 38 LYS C C 174.5 0.15 1 175 . 38 LYS CA C 54.3 0.15 1 176 . 38 LYS N N 119.5 0.15 1 177 . 39 GLN H H 9.13 0.02 1 178 . 39 GLN HA H 4.81 0.02 1 179 . 39 GLN C C 175.4 0.15 1 180 . 39 GLN CA C 54.6 0.15 1 181 . 39 GLN N N 125.8 0.15 1 182 . 40 ASN H H 9.21 0.02 1 183 . 40 ASN HA H 4.49 0.02 1 184 . 40 ASN CA C 54.2 0.15 1 185 . 40 ASN N N 130.3 0.15 1 186 . 42 GLY HA2 H 3.59 0.02 1 187 . 42 GLY HA3 H 4.28 0.02 1 188 . 42 GLY C C 174.2 0.15 1 189 . 42 GLY CA C 45.7 0.15 1 190 . 43 LYS H H 8.08 0.02 1 191 . 43 LYS HA H 4.77 0.02 1 192 . 43 LYS C C 175.4 0.15 1 193 . 43 LYS CA C 54.5 0.15 1 194 . 43 LYS N N 119.1 0.15 1 195 . 44 SER H H 7.83 0.02 1 196 . 44 SER HA H 4.41 0.02 1 197 . 44 SER C C 173.7 0.15 1 198 . 44 SER CA C 56.5 0.15 1 199 . 44 SER N N 111.8 0.15 1 200 . 45 LEU H H 7.00 0.02 1 201 . 45 LEU HA H 4.69 0.02 1 202 . 45 LEU C C 175.8 0.15 1 203 . 45 LEU CA C 56.2 0.15 1 204 . 45 LEU N N 119.8 0.15 1 205 . 46 GLU H H 8.88 0.02 1 206 . 46 GLU HA H 4.84 0.02 1 207 . 46 GLU C C 175.0 0.15 1 208 . 46 GLU CA C 55.2 0.15 1 209 . 46 GLU N N 117.7 0.15 1 210 . 47 TRP H H 9.90 0.02 1 211 . 47 TRP HA H 4.81 0.02 1 212 . 47 TRP C C 174.6 0.15 1 213 . 47 TRP CA C 59.3 0.15 1 214 . 47 TRP N N 126.5 0.15 1 215 . 48 ILE H H 9.10 0.02 1 216 . 48 ILE HA H 3.86 0.02 1 217 . 48 ILE C C 174.7 0.15 1 218 . 48 ILE CA C 62.8 0.15 1 219 . 48 ILE N N 128.4 0.15 1 220 . 49 GLY H H 6.11 0.02 1 221 . 49 GLY HA2 H 2.67 0.02 1 222 . 49 GLY HA3 H 3.50 0.02 1 223 . 49 GLY C C 170.3 0.15 1 224 . 49 GLY CA C 45.8 0.15 1 225 . 49 GLY N N 102.8 0.15 1 226 . 50 ASN H H 8.79 0.02 1 227 . 50 ASN HA H 4.22 0.02 1 228 . 50 ASN C C 172.3 0.15 1 229 . 50 ASN CA C 51.0 0.15 1 230 . 50 ASN N N 113.1 0.15 1 231 . 51 PHE H H 8.03 0.02 1 232 . 51 PHE HA H 4.73 0.02 1 233 . 51 PHE C C 173.9 0.15 1 234 . 51 PHE CA C 56.1 0.15 1 235 . 51 PHE N N 116.8 0.15 1 236 . 52 HIS H H 8.35 0.02 1 237 . 52 HIS HA H 4.85 0.02 1 238 . 52 HIS CA C 53.5 0.15 1 239 . 52 HIS N N 130.3 0.15 1 240 . 53 PRO HA H 4.66 0.02 1 241 . 53 PRO C C 176.2 0.15 1 242 . 53 PRO CA C 62.9 0.15 1 243 . 54 TYR H H 8.47 0.02 1 244 . 54 TYR HA H 4.10 0.02 1 245 . 54 TYR C C 176.6 0.15 1 246 . 54 TYR CA C 62.5 0.15 1 247 . 54 TYR N N 120.4 0.15 1 248 . 55 SER H H 6.81 0.02 1 249 . 55 SER HA H 4.25 0.02 1 250 . 55 SER C C 173.9 0.15 1 251 . 55 SER CA C 56.5 0.15 1 252 . 55 SER N N 107.0 0.15 1 253 . 56 ASP H H 8.40 0.02 1 254 . 56 ASP HA H 4.01 0.02 1 255 . 56 ASP C C 173.7 0.15 1 256 . 56 ASP CA C 56.1 0.15 1 257 . 56 ASP N N 120.1 0.15 1 258 . 57 ASP H H 7.03 0.02 1 259 . 57 ASP HA H 4.84 0.02 1 260 . 57 ASP C C 176.1 0.15 1 261 . 57 ASP CA C 53.5 0.15 1 262 . 57 ASP N N 115.9 0.15 1 263 . 58 THR H H 8.38 0.02 1 264 . 58 THR HA H 4.78 0.02 1 265 . 58 THR C C 173.6 0.15 1 266 . 58 THR CA C 59.0 0.15 1 267 . 58 THR N N 110.5 0.15 1 268 . 59 ASN H H 7.59 0.02 1 269 . 59 ASN HA H 4.89 0.02 1 270 . 59 ASN C C 173.6 0.15 1 271 . 59 ASN CA C 52.2 0.15 1 272 . 59 ASN N N 118.4 0.15 1 273 . 60 TYR H H 8.55 0.02 1 274 . 60 TYR HA H 4.88 0.02 1 275 . 60 TYR C C 176.6 0.15 1 276 . 60 TYR CA C 57.4 0.15 1 277 . 60 TYR N N 118.8 0.15 1 278 . 61 ASN H H 8.61 0.02 1 279 . 61 ASN HA H 4.92 0.02 1 280 . 61 ASN C C 177.8 0.15 1 281 . 61 ASN CA C 53.1 0.15 1 282 . 61 ASN N N 121.6 0.15 1 283 . 62 GLU H H 9.98 0.02 1 284 . 62 GLU HA H 3.97 0.02 1 285 . 62 GLU C C 177.9 0.15 1 286 . 62 GLU CA C 59.9 0.15 1 287 . 62 GLU N N 132.0 0.15 1 288 . 63 LYS H H 7.93 0.02 1 289 . 63 LYS HA H 3.97 0.02 1 290 . 63 LYS C C 177.0 0.15 1 291 . 63 LYS CA C 58.5 0.15 1 292 . 63 LYS N N 115.0 0.15 1 293 . 64 PHE H H 8.04 0.02 1 294 . 64 PHE HA H 4.72 0.02 1 295 . 64 PHE C C 175.3 0.15 1 296 . 64 PHE CA C 57.6 0.15 1 297 . 64 PHE N N 113.3 0.15 1 298 . 65 LYS H H 7.40 0.02 1 299 . 65 LYS HA H 3.70 0.02 1 300 . 65 LYS C C 175.5 0.15 1 301 . 65 LYS CA C 58.9 0.15 1 302 . 65 LYS N N 122.8 0.15 1 303 . 66 GLY H H 8.28 0.02 1 304 . 66 GLY HA2 H 3.68 0.02 1 305 . 66 GLY HA3 H 4.00 0.02 1 306 . 66 GLY C C 173.7 0.15 1 307 . 66 GLY CA C 45.6 0.15 1 308 . 66 GLY N N 108.5 0.15 1 309 . 67 LYS H H 7.47 0.02 1 310 . 67 LYS HA H 4.20 0.02 1 311 . 67 LYS C C 174.5 0.15 1 312 . 67 LYS CA C 56.5 0.15 1 313 . 67 LYS N N 119.4 0.15 1 314 . 68 ALA H H 7.40 0.02 1 315 . 68 ALA HA H 4.93 0.02 1 316 . 68 ALA C C 175.5 0.15 1 317 . 68 ALA CA C 50.1 0.15 1 318 . 68 ALA N N 119.1 0.15 1 319 . 69 LYS H H 8.41 0.02 1 320 . 69 LYS HA H 4.72 0.02 1 321 . 69 LYS C C 175.4 0.15 1 322 . 69 LYS CA C 55.8 0.15 1 323 . 69 LYS N N 119.5 0.15 1 324 . 70 LEU H H 8.28 0.02 1 325 . 70 LEU HA H 5.48 0.02 1 326 . 70 LEU C C 175.4 0.15 1 327 . 70 LEU CA C 53.6 0.15 1 328 . 70 LEU N N 130.1 0.15 1 329 . 71 THR H H 8.42 0.02 1 330 . 71 THR HA H 4.43 0.02 1 331 . 71 THR C C 172.2 0.15 1 332 . 71 THR CA C 59.9 0.15 1 333 . 71 THR N N 111.8 0.15 1 334 . 72 VAL H H 8.34 0.02 1 335 . 72 VAL HA H 5.12 0.02 1 336 . 72 VAL C C 172.9 0.15 1 337 . 72 VAL CA C 58.8 0.15 1 338 . 72 VAL N N 117.1 0.15 1 339 . 73 GLU H H 8.87 0.02 1 340 . 73 GLU HA H 4.73 0.02 1 341 . 73 GLU C C 173.4 0.15 1 342 . 73 GLU CA C 55.5 0.15 1 343 . 73 GLU N N 127.3 0.15 1 344 . 74 LYS H H 7.81 0.02 1 345 . 74 LYS HA H 4.15 0.02 1 346 . 74 LYS CA C 54.8 0.15 1 347 . 74 LYS N N 116.3 0.15 1 348 . 75 SER HA H 4.22 0.02 1 349 . 75 SER C C 175.1 0.15 1 350 . 75 SER CA C 61.2 0.15 1 351 . 76 SER H H 7.29 0.02 1 352 . 76 SER HA H 4.68 0.02 1 353 . 76 SER C C 174.8 0.15 1 354 . 76 SER CA C 56.8 0.15 1 355 . 76 SER N N 113.6 0.15 1 356 . 77 SER H H 7.54 0.02 1 357 . 77 SER HA H 2.18 0.02 1 358 . 77 SER C C 171.5 0.15 1 359 . 77 SER CA C 58.1 0.15 1 360 . 77 SER N N 116.3 0.15 1 361 . 78 THR H H 7.27 0.02 1 362 . 78 THR HA H 4.96 0.02 1 363 . 78 THR C C 172.7 0.15 1 364 . 78 THR CA C 61.5 0.15 1 365 . 78 THR N N 111.4 0.15 1 366 . 79 VAL H H 8.49 0.02 1 367 . 79 VAL HA H 4.66 0.02 1 368 . 79 VAL C C 173.5 0.15 1 369 . 79 VAL CA C 60.3 0.15 1 370 . 79 VAL N N 124.1 0.15 1 371 . 80 TYR H H 8.87 0.02 1 372 . 80 TYR HA H 5.42 0.02 1 373 . 80 TYR C C 174.1 0.15 1 374 . 80 TYR CA C 56.1 0.15 1 375 . 80 TYR N N 125.2 0.15 1 376 . 81 LEU H H 8.17 0.02 1 377 . 81 LEU HA H 4.36 0.02 1 378 . 81 LEU C C 173.9 0.15 1 379 . 81 LEU CA C 53.2 0.15 1 380 . 81 LEU N N 121.5 0.15 1 381 . 82 GLU H H 8.75 0.02 1 382 . 82 GLU HA H 5.41 0.02 1 383 . 82 GLU C C 174.7 0.15 1 384 . 82 GLU CA C 53.7 0.15 1 385 . 82 GLU N N 127.0 0.15 1 386 . 83 PHE H H 8.73 0.02 1 387 . 83 PHE HA H 5.28 0.02 1 388 . 83 PHE C C 175.1 0.15 1 389 . 83 PHE CA C 56.6 0.15 1 390 . 83 PHE N N 129.2 0.15 1 391 . 84 SER H H 8.18 0.02 1 392 . 84 SER HA H 4.75 0.02 1 393 . 84 SER C C 172.2 0.15 1 394 . 84 SER CA C 57.8 0.15 1 395 . 84 SER N N 118.1 0.15 1 396 . 85 ARG H H 8.30 0.02 1 397 . 85 ARG HA H 3.58 0.02 1 398 . 85 ARG C C 176.3 0.15 1 399 . 85 ARG CA C 56.0 0.15 1 400 . 85 ARG N N 117.3 0.15 1 401 . 86 LEU H H 8.00 0.02 1 402 . 86 LEU HA H 4.41 0.02 1 403 . 86 LEU C C 178.6 0.15 1 404 . 86 LEU CA C 56.2 0.15 1 405 . 86 LEU N N 117.5 0.15 1 406 . 87 THR H H 9.45 0.02 1 407 . 87 THR HA H 4.78 0.02 1 408 . 87 THR CA C 59.4 0.15 1 409 . 87 THR N N 113.3 0.15 1 410 . 89 ASP HA H 4.64 0.02 1 411 . 89 ASP C C 176.1 0.15 1 412 . 89 ASP CA C 56.0 0.15 1 413 . 90 ASP H H 8.25 0.02 1 414 . 90 ASP HA H 4.62 0.02 1 415 . 90 ASP C C 176.4 0.15 1 416 . 90 ASP CA C 54.7 0.15 1 417 . 90 ASP N N 117.7 0.15 1 418 . 91 SER H H 7.37 0.02 1 419 . 91 SER HA H 4.76 0.02 1 420 . 91 SER C C 173.0 0.15 1 421 . 91 SER CA C 59.1 0.15 1 422 . 91 SER N N 118.0 0.15 1 423 . 92 ALA H H 8.68 0.02 1 424 . 92 ALA HA H 4.21 0.02 1 425 . 92 ALA C C 174.2 0.15 1 426 . 92 ALA CA C 51.6 0.15 1 427 . 92 ALA N N 129.6 0.15 1 428 . 93 VAL H H 7.65 0.02 1 429 . 93 VAL HA H 4.55 0.02 1 430 . 93 VAL C C 174.1 0.15 1 431 . 93 VAL CA C 61.7 0.15 1 432 . 93 VAL N N 118.1 0.15 1 433 . 94 TYR H H 8.64 0.02 1 434 . 94 TYR HA H 5.17 0.02 1 435 . 94 TYR C C 176.7 0.15 1 436 . 94 TYR CA C 56.3 0.15 1 437 . 94 TYR N N 125.1 0.15 1 438 . 95 TYR H H 9.42 0.02 1 439 . 95 TYR HA H 5.28 0.02 1 440 . 95 TYR C C 174.7 0.15 1 441 . 95 TYR CA C 58.1 0.15 1 442 . 95 TYR N N 122.1 0.15 1 443 . 96 CYS H H 7.13 0.02 1 444 . 96 CYS HA H 5.30 0.02 1 445 . 96 CYS C C 171.9 0.15 1 446 . 96 CYS CA C 52.2 0.15 1 447 . 96 CYS N N 113.6 0.15 1 448 . 97 ALA H H 8.34 0.02 1 449 . 97 ALA HA H 4.52 0.02 1 450 . 97 ALA C C 175.0 0.15 1 451 . 97 ALA CA C 51.9 0.15 1 452 . 97 ALA N N 121.2 0.15 1 453 . 98 ILE H H 8.00 0.02 1 454 . 98 ILE HA H 5.04 0.02 1 455 . 98 ILE CA C 59.6 0.15 1 456 . 98 ILE N N 109.3 0.15 1 457 . 99 HIS HA H 4.97 0.02 1 458 . 99 HIS C C 173.3 0.15 1 459 . 99 HIS CA C 54.6 0.15 1 460 . 100 TYR H H 10.61 0.02 1 461 . 100 TYR HA H 4.26 0.02 1 462 . 100 TYR C C 179.4 0.15 1 463 . 100 TYR CA C 59.8 0.15 1 464 . 100 TYR N N 125.7 0.15 1 465 . 101 GLY H H 11.32 0.02 1 466 . 101 GLY HA2 H 3.67 0.02 1 467 . 101 GLY HA3 H 3.84 0.02 1 468 . 101 GLY C C 173.6 0.15 1 469 . 101 GLY CA C 46.2 0.15 1 470 . 101 GLY N N 113.4 0.15 1 471 . 102 SER H H 7.87 0.02 1 472 . 102 SER HA H 4.57 0.02 1 473 . 102 SER CA C 57.2 0.15 1 474 . 102 SER N N 115.2 0.15 1 475 . 103 ALA H H 8.05 0.02 1 476 . 103 ALA HA H 4.00 0.02 1 477 . 103 ALA C C 178.5 0.15 1 478 . 103 ALA CA C 51.7 0.15 1 479 . 103 ALA N N 115.5 0.15 1 480 . 104 TYR H H 7.85 0.02 1 481 . 104 TYR HA H 3.97 0.02 1 482 . 104 TYR C C 177.7 0.15 1 483 . 104 TYR CA C 60.9 0.15 1 484 . 104 TYR N N 109.3 0.15 1 485 . 105 ALA H H 6.73 0.02 1 486 . 105 ALA HA H 4.81 0.02 1 487 . 105 ALA C C 173.6 0.15 1 488 . 105 ALA CA C 51.9 0.15 1 489 . 105 ALA N N 119.6 0.15 1 490 . 106 MET H H 6.65 0.02 1 491 . 106 MET HA H 4.30 0.02 1 492 . 106 MET C C 174.0 0.15 1 493 . 106 MET CA C 55.6 0.15 1 494 . 106 MET N N 118.6 0.15 1 495 . 107 ASP H H 10.26 0.02 1 496 . 107 ASP HA H 4.55 0.02 1 497 . 107 ASP C C 176.5 0.15 1 498 . 107 ASP CA C 53.3 0.15 1 499 . 107 ASP N N 122.3 0.15 1 500 . 108 TYR H H 7.46 0.02 1 501 . 108 TYR HA H 4.92 0.02 1 502 . 108 TYR C C 172.9 0.15 1 503 . 108 TYR CA C 59.1 0.15 1 504 . 108 TYR N N 119.4 0.15 1 505 . 109 TRP H H 8.74 0.02 1 506 . 109 TRP HA H 4.89 0.02 1 507 . 109 TRP C C 178.3 0.15 1 508 . 109 TRP CA C 56.3 0.15 1 509 . 109 TRP N N 121.2 0.15 1 510 . 110 GLY H H 9.20 0.02 1 511 . 110 GLY HA2 H 4.25 0.02 1 512 . 110 GLY HA3 H 4.62 0.02 1 513 . 110 GLY C C 172.4 0.15 1 514 . 110 GLY CA C 44.8 0.15 1 515 . 110 GLY N N 110.4 0.15 1 516 . 111 GLN H H 8.40 0.02 1 517 . 111 GLN HA H 4.48 0.02 1 518 . 111 GLN C C 177.3 0.15 1 519 . 111 GLN CA C 57.4 0.15 1 520 . 111 GLN N N 112.7 0.15 1 521 . 112 GLY H H 7.73 0.02 1 522 . 112 GLY HA2 H 3.43 0.02 1 523 . 112 GLY HA3 H 3.67 0.02 1 524 . 112 GLY C C 172.7 0.15 1 525 . 112 GLY CA C 45.0 0.15 1 526 . 112 GLY N N 109.9 0.15 1 527 . 113 THR H H 8.62 0.02 1 528 . 113 THR HA H 4.31 0.02 1 529 . 113 THR C C 173.9 0.15 1 530 . 113 THR CA C 63.0 0.15 1 531 . 113 THR N N 121.4 0.15 1 532 . 114 SER H H 8.96 0.02 1 533 . 114 SER HA H 4.82 0.02 1 534 . 114 SER C C 173.3 0.15 1 535 . 114 SER CA C 58.0 0.15 1 536 . 114 SER N N 122.9 0.15 1 537 . 115 VAL H H 9.12 0.02 1 538 . 115 VAL HA H 4.76 0.02 1 539 . 115 VAL C C 175.7 0.15 1 540 . 115 VAL CA C 61.7 0.15 1 541 . 115 VAL N N 128.8 0.15 1 542 . 116 THR H H 8.70 0.02 1 543 . 116 THR HA H 4.46 0.02 1 544 . 116 THR C C 172.1 0.15 1 545 . 116 THR CA C 62.3 0.15 1 546 . 116 THR N N 124.6 0.15 1 547 . 117 VAL H H 8.44 0.02 1 548 . 117 VAL HA H 4.63 0.02 1 549 . 117 VAL C C 176.1 0.15 1 550 . 117 VAL CA C 60.4 0.15 1 551 . 117 VAL N N 128.7 0.15 1 552 . 118 SER H H 8.79 0.02 1 553 . 118 SER HA H 4.50 0.02 1 554 . 118 SER C C 173.1 0.15 1 555 . 118 SER CA C 57.9 0.15 1 556 . 118 SER N N 122.6 0.15 1 557 . 119 SER H H 8.06 0.02 1 558 . 119 SER HA H 4.23 0.02 1 559 . 119 SER CA C 60.7 0.15 1 560 . 119 SER N N 123.4 0.15 1 stop_ save_