data_4580 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H,13C,and 15N assignments of the anti-dansyl antibody Fv fragment ; _BMRB_accession_number 4580 _BMRB_flat_file_name bmr4580.str _Entry_type original _Submission_date 2000-02-01 _Accession_date 2000-02-02 _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 Shindo Kazuyasu . . 2 Masuda Katsyoshi . . 3 Takahashi Hideo . . 4 Arata Yoji . . 5 Shimada Ichio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 223 "13C chemical shifts" 217 "15N chemical shifts" 224 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-09-25 update BMRB 'Entry citation updated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of the anti-dansyl antibody Fv fragment ; _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 Shindo Kazuyasu . . 2 Masuda Katsyoshi . . 3 Takahashi Hideo . . 4 Arata Yoji . . 5 Shimada Ichio . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 357 _Page_last 358 _Year 2000 _Details . loop_ _Keyword 'anti-dansyl antibody' 'heteronuclear NMR' 'resonace assignments' stop_ save_ ################################## # Molecular system description # ################################## save_Fv_fragment _Saveframe_category molecular_system _Mol_system_name 'anti-dansyl Fv fragment' _Abbreviation_common 'Fv fragment' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'VH domain' $VH_domain 'VL domain' $VL_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state heterodimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function antibody stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_VH_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'VH domain' _Abbreviation_common VH _Molecular_mass 12500 _Mol_thiol_state 'all disulfide bound' _Details ; VH domain associates VL domain, forms a heterodimer usually and this dimer is refered as Fv fragment. Residues26-32, 53-59, 102-209 are called H1 region, H2 region, H3 region, respectively and form antigen binding site generally. ; ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; EVKLEESGGGLVQPGGSMKL SCATSGFTFSDAWMDWVRQS PEKGLEWVAEIRNKANNHAT YYAESVKGRFTISRDDSKRR VYLQMNTLRAEDTGIYYCTG IYYHYPWFAYWGQGTLVTVS AEPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLU 2 2 VAL 3 3 LYS 4 4 LEU 5 5 GLU 6 6 GLU 7 7 SER 8 8 GLY 9 9 GLY 10 10 GLY 11 11 LEU 12 12 VAL 13 13 GLN 14 14 PRO 15 15 GLY 16 16 GLY 17 17 SER 18 18 MET 19 19 LYS 20 20 LEU 21 21 SER 22 22 CYS 23 23 ALA 24 24 THR 25 25 SER 26 26 GLY 27 27 PHE 28 28 THR 29 29 PHE 30 30 SER 31 31 ASP 32 32 ALA 33 33 TRP 34 34 MET 35 35 ASP 36 36 TRP 37 37 VAL 38 33 ARG 39 39 GLN 40 40 SER 41 41 PRO 42 42 GLU 43 43 LYS 44 44 GLY 45 45 LEU 46 46 GLU 47 47 TRP 48 48 VAL 49 49 ALA 50 50 GLU 51 51 ILE 52 52 ARG 53 52a ASN 54 52b LYS 55 52c ALA 56 53 ASN 57 54 ASN 58 55 HIS 59 56 ALA 60 57 THR 61 58 TYR 62 59 TYR 63 60 ALA 64 61 GLU 65 62 SER 66 63 VAL 67 64 LYS 68 65 GLY 69 66 ARG 70 67 PHE 71 68 THR 72 69 ILE 73 70 SER 74 71 ARG 75 72 ASP 76 73 ASP 77 74 SER 78 75 LYS 79 76 ARG 80 77 ARG 81 78 VAL 82 79 TYR 83 80 LEU 84 81 GLN 85 82 MET 86 82a ASN 87 82b THR 88 82c LEU 89 83 ARG 90 84 ALA 91 85 GLU 92 86 ASP 93 87 THR 94 88 GLY 95 89 ILE 96 90 TYR 97 91 TYR 98 92 CYS 99 93 THR 100 94 GLY 101 95 ILE 102 96 TYR 103 97 TYR 104 98 HIS 105 99 TYR 106 100 PRO 107 101 TRP 108 102 PHE 109 103 ALA 110 104 TYR 111 105 TRP 112 106 GLY 113 107 GLN 114 108 GLY 115 109 THR 116 110 LEU 117 111 VAL 118 112 THR 119 113 VAL 120 114 SER 121 115 ALA 122 116 GLU 123 117 PRO 124 118 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1DLF "High Resolution Crystal Structure Of The Fv Fragment From An Anti-Dansyl Switch Variant Antibody Igg2a(S) Crystallized At Ph 5." 100.00 124 100.00 100.00 5.70e-87 PDB 1WZ1 "Crystal Structure Of The Fv Fragment Complexed With Dansyl- Lysine" 99.19 123 100.00 100.00 3.69e-86 PDB 2DLF "High Resolution Crystal Structure Of The Fv Fragment From An Anti-Dansyl Switch Variant Antibody Igg2a(S) Crystallized At Ph 6." 100.00 124 100.00 100.00 5.70e-87 stop_ save_ save_VL_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'VL domain' _Abbreviation_common VL _Molecular_mass 12500 _Mol_thiol_state 'all disulfide bond' _Details ; VL domain associates VH domain, forms a heterodimer usually and this dimer is refered as Fv fragment. Residues26-32, 50-52, and 91-96 are called L1 region, L2 region, and L3 region respectively. ; _Residue_count 113 _Mol_residue_sequence ; DVVMTQTPLSLPVSLGNQAS ISCRSSQSLVHSNGNTYLHW YLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKI SRVEAEDLGVYFCSQSTHVP FTFGSGTKLEIKR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 VAL 3 3 VAL 4 4 MET 5 5 THR 6 6 GLN 7 7 THR 8 8 PRO 9 9 LEU 10 10 SER 11 11 LEU 12 12 PRO 13 13 VAL 14 14 SER 15 15 LEU 16 16 GLY 17 17 ASN 18 18 GLN 19 19 ALA 20 20 SER 21 21 ILE 22 22 SER 23 23 CYS 24 24 ARG 25 25 SER 26 26 SER 27 27 GLN 28 27a SER 29 27b LEU 30 27c VAL 31 27d HIS 32 27e SER 33 28 ASN 34 29 GLY 35 30 ASN 36 31 THR 37 32 TYR 38 33 LEU 39 34 HIS 40 35 TRP 41 36 TYR 42 37 LEU 43 38 GLN 44 39 LYS 45 40 PRO 46 41 GLY 47 42 GLN 48 43 SER 49 44 PRO 50 45 LYS 51 46 LEU 52 47 LEU 53 48 ILE 54 49 TYR 55 50 LYS 56 51 VAL 57 52 SER 58 53 ASN 59 54 ARG 60 55 PHE 61 56 SER 62 57 GLY 63 58 VAL 64 59 PRO 65 60 ASP 66 61 ARG 67 62 PHE 68 63 SER 69 64 GLY 70 65 SER 71 66 GLY 72 67 SER 73 68 GLY 74 69 THR 75 70 ASP 76 71 PHE 77 72 THR 78 73 LEU 79 74 LYS 80 75 ILE 81 76 SER 82 77 ARG 83 78 VAL 84 79 GLU 85 80 ALA 86 81 GLU 87 82 ASP 88 83 LEU 89 84 GLY 90 85 VAL 91 86 TYR 92 87 PHE 93 88 CYS 94 89 SER 95 90 GLN 96 91 SER 97 92 THR 98 93 HIS 99 94 VAL 100 95 PRO 101 96 PHE 102 97 THR 103 98 PHE 104 99 GLY 105 100 SER 106 101 GLY 107 102 THR 108 103 LYS 109 104 LEU 110 105 GLU 111 106 ILE 112 107 LYS 113 108 ARG stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 PIR B30577 'Ig kappa chain precursor V region (MRL10) - mouse (fragment)' 99.12 131 98.21 100.00 2.00e-58 PIR PL0257 'Ig kappa chain V region (anti-DNA, DP1VK) - mouse (fragment)' 98.23 111 98.20 100.00 1.39e-57 GenBank AAB22613 'immunoglobulin variable kappa 1 [Mus sp.]' 88.50 104 99.00 100.00 1.03e-51 GenBank AAB28784 'IgM kappa chain variable region; IgM VK [Mus sp.]' 92.04 104 99.04 100.00 2.13e-53 GenBank AAA39066 'immunoglobulin kappa chain' 88.50 120 99.00 100.00 1.63e-51 GenBank AAA85498 'immunoglobulin light chain variable region' 99.12 112 98.21 100.00 4.18e-58 EMBL CAB46118 'immunoglobulin light chain variable region [Mus musculus]' 88.50 119 99.00 100.00 1.31e-51 GenBank AAA39041 'Ig kappa-chain V-region precursor' 88.50 119 99.00 100.00 1.31e-51 PDB 2HKH 'Crystal Structure Of The Fab M75' 100.00 219 98.23 99.12 3.14e-59 DBJ BAA00052 'Ig kappa chain [Mus musculus]' 88.50 119 99.00 100.00 1.31e-51 PDB 2DLF 'High Resolution Crystal Structure Of The Fv Fragment From An Anti-Dansyl Switch Variant Antibody Igg2a(S) Crystallized At Ph 6.75' 100.00 113 100.00 100.00 8.13e-60 PDB 2HKF 'Crystal Structure Of The Complex Fab M75- Peptide' 100.00 219 98.23 99.12 3.14e-59 PDB 1DLF 'High Resolution Crystal Structure Of The Fv Fragment From An Anti-Dansyl Switch Variant Antibody Igg2a(S) Crystallized At Ph 5.25' 100.00 113 100.00 100.00 8.13e-60 PDB 1WZ1 'Crystal Structure Of The Fv Fragment Complexed With Dansyl- Lysine' 100.00 113 100.00 100.00 8.13e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Cell_line _Cell_type _Details $VH_domain Mouse 10090 Eukaryota Metazoa Mus musculus '27-1B10.7 murine-murine hybridoma' 'B-lymphocyte, anti-dansyl monoclonal antibody, IgG2a(s)' ; The Fv fragment, which is a heterodimer composed of VH domain and VL domain, is prepared from IgG2a(s) by a limited proteolytic digestion using clostripin. ; $VL_domain Mouse 10090 Eukaryota Metazoa Mus musculus '27-1B10.7 murine-murine hybridoma' 'B-lymphocyte, anti-dansyl monoclonal antibody, IgG2a(s)' ; The Fv fragment, which is a heterodimer composed of VH domain and VL domain, is prepared from IgG2a(s) by a limited proteolytic digestion using clostripin. ; 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 $VH_domain 'purified from the natural source' . . . . . $VL_domain 'purified from the natural source' . . . . . 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 $VH_domain 1.2 mM '[U-95% 13C; U-95% 15N(except Cys and Trp); [98% 15N]-Cys; [98% 15N]-Trp]' $VL_domain 1.2 mM '[U-95% 13C; U-95% 15N(except Cys and Trp); [98% 15N]-Cys; [98% 15N]-Trp]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task processing stop_ _Details . save_ save_UXNMR _Saveframe_category software _Name UXNMR _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _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_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_15N_edited_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited TOCSY' _Sample_label $sample_1 save_ save_15N_edited_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited NOESY' _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 6.0 0.05 n/a temperature 310 1 K 'ionic strength' 0.35 0.05 M 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 . direct . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'VH domain' _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 GLU CA C 55.5 . 1 2 . 2 VAL H H 8.50 . 1 3 . 2 VAL CA C 63.6 . 1 4 . 2 VAL N N 126.2 . 1 5 . 3 LYS H H 8.50 . 1 6 . 3 LYS CA C 55.9 . 1 7 . 3 LYS N N 128.6 . 1 8 . 4 LEU H H 8.36 . 1 9 . 4 LEU CA C 54.7 . 1 10 . 4 LEU N N 126.9 . 1 11 . 5 GLU H H 8.70 . 1 12 . 5 GLU CA C 56.1 . 1 13 . 5 GLU N N 121.5 . 1 14 . 6 GLU H H 10.55 . 1 15 . 6 GLU CA C 57.3 . 1 16 . 6 GLU N N 131.9 . 1 17 . 7 SER H H 9.24 . 1 18 . 7 SER CA C 58.2 . 1 19 . 7 SER N N 115.4 . 1 20 . 8 GLY H H 9.40 . 1 21 . 8 GLY CA C 45.3 . 1 22 . 8 GLY N N 111.5 . 1 23 . 9 GLY H H 8.33 . 1 24 . 9 GLY CA C 44.7 . 1 25 . 9 GLY N N 109.9 . 1 26 . 10 GLY H H 7.40 . 1 27 . 10 GLY CA C 44.9 . 1 28 . 10 GLY N N 106.6 . 1 29 . 11 LEU H H 7.80 . 1 30 . 11 LEU CA C 54.5 . 1 31 . 11 LEU N N 124.0 . 1 32 . 12 VAL H H 8.92 . 1 33 . 12 VAL CA C 59.7 . 1 34 . 12 VAL N N 125.8 . 1 35 . 13 GLN H H 7.95 . 1 36 . 13 GLN CA C 54.3 . 1 37 . 13 GLN N N 123.9 . 1 38 . 14 PRO CA C 63.7 . 1 39 . 15 GLY H H 9.68 . 1 40 . 15 GLY CA C 45.3 . 1 41 . 15 GLY N N 114.8 . 1 42 . 16 GLY H H 8.48 . 1 43 . 16 GLY CA C 44.7 . 1 44 . 16 GLY N N 108.3 . 1 45 . 17 SER H H 7.84 . 1 46 . 17 SER CA C 56.5 . 1 47 . 17 SER N N 110.6 . 1 48 . 18 MET H H 8.52 . 1 49 . 18 MET CA C 55.3 . 1 50 . 18 MET N N 121.2 . 1 51 . 19 LYS H H 8.18 . 1 52 . 19 LYS CA C 55.0 . 1 53 . 19 LYS N N 125.1 . 1 54 . 20 LEU H H 8.35 . 1 55 . 20 LEU CA C 52.8 . 1 56 . 20 LEU N N 126.5 . 1 57 . 21 SER H H 8.68 . 1 58 . 21 SER CA C 57.0 . 1 59 . 21 SER N N 114.9 . 1 60 . 22 CYS H H 8.89 . 1 61 . 22 CYS N N 124.5 . 1 62 . 23 ALA H H 8.64 . 1 63 . 23 ALA CA C 51.3 . 1 64 . 23 ALA N N 131.0 . 1 65 . 24 THR H H 7.75 . 1 66 . 24 THR CA C 60.3 . 1 67 . 24 THR N N 112.2 . 1 68 . 25 SER H H 8.68 . 1 69 . 25 SER CA C 58.7 . 1 70 . 25 SER N N 113.8 . 1 71 . 26 GLY H H 8.61 . 1 72 . 26 GLY CA C 46.3 . 1 73 . 26 GLY N N 108.6 . 1 74 . 27 PHE H H 7.23 . 1 75 . 27 PHE CA C 55.3 . 1 76 . 27 PHE N N 114.7 . 1 77 . 28 THR H H 8.69 . 1 78 . 28 THR CA C 61.9 . 1 79 . 28 THR N N 119.5 . 1 80 . 29 PHE H H 8.33 . 1 81 . 29 PHE N N 134.6 . 1 82 . 30 SER H H 8.60 . 1 83 . 30 SER CA C 61.3 . 1 84 . 30 SER N N 111.4 . 1 85 . 31 ASP H H 9.32 . 1 86 . 31 ASP CA C 55.3 . 1 87 . 31 ASP N N 127.0 . 1 88 . 32 ALA H H 7.49 . 1 89 . 32 ALA CA C 52.3 . 1 90 . 32 ALA N N 123.3 . 1 91 . 33 TRP H H 8.73 . 1 92 . 33 TRP N N 125.7 . 1 93 . 34 MET H H 8.09 . 1 94 . 34 MET CA C 52.4 . 1 95 . 34 MET N N 118.6 . 1 96 . 35 ASP H H 8.91 . 1 97 . 35 ASP CA C 52.5 . 1 98 . 35 ASP N N 119.7 . 1 99 . 36 TRP H H 8.32 . 1 100 . 36 TRP N N 115.5 . 1 101 . 37 VAL H H 9.22 . 1 102 . 37 VAL CA C 60.7 . 1 103 . 37 VAL N N 125.1 . 1 104 . 38 ARG H H 9.35 . 1 105 . 38 ARG CA C 52.7 . 1 106 . 38 ARG N N 124.4 . 1 107 . 39 GLN H H 9.25 . 1 108 . 39 GLN CA C 54.0 . 1 109 . 39 GLN N N 122.7 . 1 110 . 40 SER H H 8.56 . 1 111 . 40 SER CA C 55.7 . 1 112 . 40 SER N N 123.4 . 1 113 . 41 PRO CA C 65.3 . 1 114 . 42 GLU H H 8.37 . 1 115 . 42 GLU CA C 58.8 . 1 116 . 42 GLU N N 115.0 . 1 117 . 43 LYS H H 7.54 . 1 118 . 43 LYS CA C 55.8 . 1 119 . 43 LYS N N 116.3 . 1 120 . 44 GLY H H 9.03 . 1 121 . 44 GLY CA C 45.7 . 1 122 . 44 GLY N N 116.7 . 1 123 . 45 LEU H H 7.93 . 1 124 . 45 LEU CA C 54.4 . 1 125 . 45 LEU N N 124.4 . 1 126 . 46 GLU H H 9.19 . 1 127 . 46 GLU CA C 54.9 . 1 128 . 46 GLU N N 122.3 . 1 129 . 47 TRP H H 9.81 . 1 130 . 47 TRP N N 129.7 . 1 131 . 48 VAL H H 7.79 . 1 132 . 48 VAL CA C 63.1 . 1 133 . 48 VAL N N 123.3 . 1 134 . 49 ALA H H 6.64 . 1 135 . 49 ALA CA C 51.7 . 1 136 . 49 ALA N N 115.4 . 1 137 . 50 GLU H H 8.96 . 1 138 . 50 GLU CA C 55.3 . 1 139 . 50 GLU N N 120.8 . 1 140 . 51 ILE H H 9.36 . 1 141 . 51 ILE CA C 58.4 . 1 142 . 51 ILE N N 123.4 . 1 143 . 52 ARG H H 8.93 . 1 144 . 52 ARG CA C 56.3 . 1 145 . 52 ARG N N 126.6 . 1 146 . 53 ASN H H 7.01 . 1 147 . 53 ASN CA C 52.3 . 1 148 . 53 ASN N N 115.1 . 1 149 . 54 LYS H H 9.44 . 1 150 . 54 LYS N N 127.8 . 1 151 . 55 ALA H H 8.21 . 1 152 . 55 ALA CA C 54.4 . 1 153 . 55 ALA N N 122.9 . 1 154 . 56 ASN H H 7.24 . 1 155 . 56 ASN CA C 53.3 . 1 156 . 56 ASN N N 115.4 . 1 157 . 57 ASN H H 8.14 . 1 158 . 57 ASN CA C 54.6 . 1 159 . 57 ASN N N 116.6 . 1 160 . 58 HIS H H 8.20 . 1 161 . 58 HIS CA C 56.1 . 1 162 . 58 HIS N N 111.9 . 1 163 . 59 ALA H H 6.79 . 1 164 . 59 ALA CA C 53.8 . 1 165 . 59 ALA N N 118.7 . 1 166 . 60 THR H H 7.66 . 1 167 . 60 THR CA C 58.6 . 1 168 . 60 THR N N 109.4 . 1 169 . 61 TYR H H 8.29 . 1 170 . 61 TYR CA C 57.3 . 1 171 . 61 TYR N N 120.4 . 1 172 . 62 TYR H H 8.66 . 1 173 . 62 TYR CA C 57.1 . 1 174 . 62 TYR N N 117.9 . 1 175 . 63 ALA H H 7.79 . 1 176 . 63 ALA CA C 52.3 . 1 177 . 63 ALA N N 126.1 . 1 178 . 64 GLU H H 9.27 . 1 179 . 64 GLU CA C 59.9 . 1 180 . 64 GLU N N 124.3 . 1 181 . 65 SER H H 8.17 . 1 182 . 65 SER CA C 60.1 . 1 183 . 65 SER N N 110.3 . 1 184 . 66 VAL H H 7.20 . 1 185 . 66 VAL CA C 60.3 . 1 186 . 66 VAL N N 112.3 . 1 187 . 67 LYS H H 7.23 . 1 188 . 67 LYS CA C 58.4 . 1 189 . 67 LYS N N 126.3 . 1 190 . 68 GLY H H 8.08 . 1 191 . 68 GLY CA C 45.4 . 1 192 . 68 GLY N N 109.7 . 1 193 . 69 ARG H H 7.63 . 1 194 . 69 ARG CA C 57.3 . 1 195 . 69 ARG N N 117.8 . 1 196 . 70 PHE H H 7.40 . 1 197 . 70 PHE CA C 52.7 . 1 198 . 70 PHE N N 120.4 . 1 199 . 71 THR H H 9.00 . 1 200 . 71 THR CA C 61.3 . 1 201 . 71 THR N N 113.8 . 1 202 . 72 ILE H H 9.29 . 1 203 . 72 ILE CA C 58.5 . 1 204 . 72 ILE N N 133.0 . 1 205 . 73 SER H H 8.59 . 1 206 . 73 SER CA C 57.7 . 1 207 . 73 SER N N 120.0 . 1 208 . 74 ARG H H 9.12 . 1 209 . 74 ARG CA C 54.7 . 1 210 . 74 ARG N N 117.4 . 1 211 . 75 ASP H H 7.32 . 1 212 . 75 ASP CA C 52.3 . 1 213 . 75 ASP N N 118.7 . 1 214 . 76 ASP H H 7.33 . 1 215 . 76 ASP CA C 57.4 . 1 216 . 76 ASP N N 118.6 . 1 217 . 77 SER H H 8.49 . 1 218 . 77 SER CA C 61.3 . 1 219 . 77 SER N N 117.5 . 1 220 . 78 LYS H H 7.32 . 1 221 . 78 LYS CA C 55.7 . 1 222 . 78 LYS N N 119.3 . 1 223 . 79 ARG H H 7.63 . 1 224 . 79 ARG CA C 55.7 . 1 225 . 79 ARG N N 117.8 . 1 226 . 80 ARG H H 6.98 . 1 227 . 80 ARG CA C 53.8 . 1 228 . 80 ARG N N 116.1 . 1 229 . 81 VAL H H 8.33 . 1 230 . 81 VAL CA C 59.3 . 1 231 . 81 VAL N N 119.1 . 1 232 . 82 TYR H H 8.97 . 1 233 . 82 TYR CA C 56.4 . 1 234 . 82 TYR N N 123.7 . 1 235 . 83 LEU H H 8.64 . 1 236 . 83 LEU CA C 53.7 . 1 237 . 83 LEU N N 123.6 . 1 238 . 84 GLN H H 8.97 . 1 239 . 84 GLN CA C 54.9 . 1 240 . 84 GLN N N 129.3 . 1 241 . 85 MET H H 8.75 . 1 242 . 85 MET CA C 54.7 . 1 243 . 85 MET N N 127.7 . 1 244 . 86 ASN H H 7.81 . 1 245 . 86 ASN CA C 51.7 . 1 246 . 86 ASN N N 121.7 . 1 247 . 87 THR H H 8.27 . 1 248 . 87 THR CA C 61.6 . 1 249 . 87 THR N N 112.5 . 1 250 . 88 LEU H H 8.01 . 1 251 . 88 LEU CA C 56.5 . 1 252 . 88 LEU N N 119.9 . 1 253 . 89 ARG H H 9.56 . 1 254 . 89 ARG CA C 53.8 . 1 255 . 89 ARG N N 121.8 . 1 256 . 90 ALA H H 9.06 . 1 257 . 90 ALA CA C 56.3 . 1 258 . 90 ALA N N 126.2 . 1 259 . 91 GLU H H 9.25 . 1 260 . 91 GLU CA C 58.7 . 1 261 . 91 GLU N N 115.4 . 1 262 . 92 ASP H H 8.49 . 1 263 . 92 ASP CA C 55.3 . 1 264 . 92 ASP N N 119.3 . 1 265 . 93 THR H H 7.74 . 1 266 . 93 THR CA C 64.5 . 1 267 . 93 THR N N 120.3 . 1 268 . 94 GLY H H 9.44 . 1 269 . 94 GLY CA C 45.3 . 1 270 . 94 GLY N N 115.5 . 1 271 . 95 ILE H H 8.34 . 1 272 . 95 ILE CA C 61.0 . 1 273 . 95 ILE N N 121.2 . 1 274 . 96 TYR H H 9.20 . 1 275 . 96 TYR CA C 58.3 . 1 276 . 96 TYR N N 128.3 . 1 277 . 97 TYR H H 9.72 . 1 278 . 97 TYR CA C 56.3 . 1 279 . 97 TYR N N 121.4 . 1 280 . 98 CYS H H 10.74 . 1 281 . 98 CYS N N 124.8 . 1 282 . 99 THR H H 7.96 . 1 283 . 99 THR CA C 59.3 . 1 284 . 99 THR N N 120.2 . 1 285 . 100 GLY H H 8.25 . 1 286 . 100 GLY CA C 46.1 . 1 287 . 100 GLY N N 109.2 . 1 288 . 101 ILE H H 8.80 . 1 289 . 101 ILE N N 114.6 . 1 290 . 102 TYR H H 7.02 . 1 291 . 102 TYR N N 119.1 . 1 292 . 103 TYR H H 8.07 . 1 293 . 103 TYR CA C 62.0 . 1 294 . 103 TYR N N 122.6 . 1 295 . 104 HIS H H 7.55 . 1 296 . 104 HIS N N 113.9 . 1 297 . 105 TYR H H 7.13 . 1 298 . 105 TYR N N 117.7 . 1 299 . 107 TRP N N 122.34 . 1 300 . 108 PHE H H 7.59 . 1 301 . 108 PHE N N 119.3 . 1 302 . 110 TYR H H 7.42 . 1 303 . 110 TYR CA C 56.4 . 1 304 . 110 TYR N N 114.9 . 1 305 . 111 TRP H H 8.89 . 1 306 . 111 TRP N N 125.7 . 1 307 . 112 GLY H H 8.53 . 1 308 . 112 GLY CA C 45.7 . 1 309 . 112 GLY N N 110.8 . 1 310 . 113 GLN H H 8.61 . 1 311 . 113 GLN CA C 57.3 . 1 312 . 113 GLN N N 118.3 . 1 313 . 114 GLY H H 7.69 . 1 314 . 114 GLY CA C 44.3 . 1 315 . 114 GLY N N 108.1 . 1 316 . 115 THR H H 8.31 . 1 317 . 115 THR CA C 59.8 . 1 318 . 115 THR N N 117.2 . 1 319 . 116 LEU H H 8.20 . 1 320 . 116 LEU CA C 56.0 . 1 321 . 116 LEU N N 132.4 . 1 322 . 117 VAL H H 9.04 . 1 323 . 117 VAL CA C 62.3 . 1 324 . 117 VAL N N 130.2 . 1 325 . 118 THR H H 8.30 . 1 326 . 118 THR CA C 62.0 . 1 327 . 118 THR N N 124.5 . 1 328 . 119 VAL H H 8.22 . 1 329 . 119 VAL CA C 60.0 . 1 330 . 119 VAL N N 128.8 . 1 331 . 120 SER H H 8.36 . 1 332 . 120 SER CA C 57.3 . 1 333 . 120 SER N N 120.7 . 1 334 . 121 ALA H H 8.63 . 1 335 . 121 ALA CA C 52.1 . 1 336 . 121 ALA N N 128.4 . 1 337 . 122 GLU H H 8.14 . 1 338 . 122 GLU CA C 54.6 . 1 339 . 122 GLU N N 121.4 . 1 340 . 123 PRO CA C 63.5 . 1 341 . 124 ARG H H 7.79 . 1 342 . 124 ARG CA C 57.3 . 1 343 . 124 ARG N N 127.0 . 1 stop_ save_ save_shift_set_2 _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 'VL domain' _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 CA C 53.4 . 1 2 . 2 VAL H H 9.14 . 1 3 . 2 VAL CA C 64.0 . 1 4 . 2 VAL N N 123.7 . 1 5 . 3 VAL H H 8.43 . 1 6 . 3 VAL CA C 62.7 . 1 7 . 3 VAL N N 132.9 . 1 8 . 4 MET H H 9.00 . 1 9 . 4 MET CA C 52.3 . 1 10 . 4 MET N N 128.7 . 1 11 . 5 THR H H 9.52 . 1 12 . 5 THR CA C 62.3 . 1 13 . 5 THR N N 121.5 . 1 14 . 6 GLN H H 8.92 . 1 15 . 6 GLN CA C 54.7 . 1 16 . 6 GLN N N 128.3 . 1 17 . 7 THR H H 8.41 . 1 18 . 7 THR CA C 59.1 . 1 19 . 7 THR N N 116.1 . 1 20 . 8 PRO CA C 63.4 . 1 21 . 9 LEU H H 8.63 . 1 22 . 9 LEU CA C 57.4 . 1 23 . 9 LEU N N 119.9 . 1 24 . 10 SER H H 7.65 . 1 25 . 10 SER CA C 57.3 . 1 26 . 10 SER N N 114.5 . 1 27 . 11 LEU H H 9.07 . 1 28 . 11 LEU CA C 52.0 . 1 29 . 11 LEU N N 128.7 . 1 30 . 12 PRO CA C 60.9 . 1 31 . 13 VAL H H 9.05 . 1 32 . 13 VAL CA C 59.6 . 1 33 . 13 VAL N N 121.9 . 1 34 . 14 SER H H 8.00 . 1 35 . 14 SER CA C 57.5 . 1 36 . 14 SER N N 119.1 . 1 37 . 15 LEU H H 8.52 . 1 38 . 15 LEU CA C 56.8 . 1 39 . 15 LEU N N 124.0 . 1 40 . 16 GLY H H 9.34 . 1 41 . 16 GLY CA C 45.1 . 1 42 . 16 GLY N N 112.1 . 1 43 . 17 ASN H H 7.68 . 1 44 . 17 ASN CA C 52.3 . 1 45 . 17 ASN N N 120.1 . 1 46 . 18 GLN H H 8.19 . 1 47 . 18 GLN CA C 55.3 . 1 48 . 18 GLN N N 118.4 . 1 49 . 19 ALA H H 8.45 . 1 50 . 19 ALA CA C 51.3 . 1 51 . 19 ALA N N 123.3 . 1 52 . 20 SER H H 7.63 . 1 53 . 20 SER CA C 57.1 . 1 54 . 20 SER N N 115.4 . 1 55 . 21 ILE H H 8.90 . 1 56 . 21 ILE CA C 61.3 . 1 57 . 21 ILE N N 124.6 . 1 58 . 22 SER H H 8.61 . 1 59 . 22 SER CA C 58.0 . 1 60 . 22 SER N N 120.7 . 1 61 . 23 CYS H H 9.23 . 1 62 . 23 CYS N N 125.1 . 1 63 . 24 ARG H H 8.90 . 1 64 . 24 ARG CA C 53.4 . 1 65 . 24 ARG N N 124.6 . 1 66 . 25 SER H H 9.36 . 1 67 . 25 SER CA C 56.3 . 1 68 . 25 SER N N 119.5 . 1 69 . 26 SER H H 8.21 . 1 70 . 26 SER CA C 60.3 . 1 71 . 26 SER N N 115.5 . 1 72 . 27 GLN H H 7.20 . 1 73 . 27 GLN CA C 53.8 . 1 74 . 27 GLN N N 116.8 . 1 75 . 28 SER H H 8.14 . 1 76 . 28 SER CA C 59.3 . 1 77 . 28 SER N N 121.4 . 1 78 . 29 LEU H H 8.51 . 1 79 . 29 LEU CA C 53.7 . 1 80 . 29 LEU N N 125.3 . 1 81 . 30 VAL H H 7.98 . 1 82 . 30 VAL CA C 63.7 . 1 83 . 30 VAL N N 124.8 . 1 84 . 31 HIS H H 9.24 . 1 85 . 31 HIS CA C 57.7 . 1 86 . 31 HIS N N 133.4 . 1 87 . 32 SER H H 7.77 . 1 88 . 32 SER CA C 62.3 . 1 89 . 32 SER N N 127.0 . 1 90 . 33 ASN H H 12.40 . 1 91 . 33 ASN CA C 53.0 . 1 92 . 33 ASN N N 125.5 . 1 93 . 34 GLY H H 8.37 . 1 94 . 34 GLY CA C 49.0 . 1 95 . 34 GLY N N 114.3 . 1 96 . 35 ASN H H 7.63 . 1 97 . 35 ASN CA C 53.3 . 1 98 . 35 ASN N N 122.5 . 1 99 . 36 THR H H 8.40 . 1 100 . 36 THR CA C 61.7 . 1 101 . 36 THR N N 117.1 . 1 102 . 37 TYR H H 6.18 . 1 103 . 37 TYR CA C 57.3 . 1 104 . 37 TYR N N 126.2 . 1 105 . 38 LEU H H 5.94 . 1 106 . 38 LEU CA C 50.8 . 1 107 . 38 LEU N N 126.0 . 1 108 . 39 HIS H H 8.58 . 1 109 . 39 HIS CA C 52.3 . 1 110 . 39 HIS N N 125.6 . 1 111 . 40 TRP H H 9.13 . 1 112 . 40 TRP N N 118.0 . 1 113 . 41 TYR H H 9.66 . 1 114 . 41 TYR CA C 56.7 . 1 115 . 41 TYR N N 120.3 . 1 116 . 42 LEU H H 8.94 . 1 117 . 42 LEU CA C 53.3 . 1 118 . 42 LEU N N 123.4 . 1 119 . 43 GLN H H 9.86 . 1 120 . 43 GLN CA C 54.7 . 1 121 . 43 GLN N N 130.4 . 1 122 . 44 LYS H H 8.70 . 1 123 . 44 LYS CA C 54.7 . 1 124 . 44 LYS N N 132.5 . 1 125 . 45 PRO CA C 64.4 . 1 126 . 46 GLY H H 8.68 . 1 127 . 46 GLY CA C 45.9 . 1 128 . 46 GLY N N 113.8 . 1 129 . 47 GLN H H 8.00 . 1 130 . 47 GLN CA C 53.8 . 1 131 . 47 GLN N N 119.0 . 1 132 . 48 SER H H 8.36 . 1 133 . 48 SER CA C 56.4 . 1 134 . 48 SER N N 116.1 . 1 135 . 49 PRO CA C 63.3 . 1 136 . 50 LYS H H 8.26 . 1 137 . 50 LYS CA C 53.8 . 1 138 . 50 LYS N N 120.3 . 1 139 . 51 LEU H H 8.76 . 1 140 . 51 LEU CA C 56.1 . 1 141 . 51 LEU N N 127.4 . 1 142 . 52 LEU H H 8.67 . 1 143 . 52 LEU CA C 54.6 . 1 144 . 52 LEU N N 126.1 . 1 145 . 53 ILE H H 7.22 . 1 146 . 53 ILE CA C 57.3 . 1 147 . 53 ILE N N 118.6 . 1 148 . 54 TYR H H 9.11 . 1 149 . 54 TYR CA C 53.5 . 1 150 . 54 TYR N N 123.1 . 1 151 . 55 LYS H H 9.49 . 1 152 . 55 LYS CA C 57.7 . 1 153 . 55 LYS N N 121.1 . 1 154 . 56 VAL H H 9.53 . 1 155 . 56 VAL CA C 69.7 . 1 156 . 56 VAL N N 114.6 . 1 157 . 57 SER H H 8.56 . 1 158 . 57 SER CA C 57.7 . 1 159 . 57 SER N N 110.5 . 1 160 . 58 ASN H H 8.39 . 1 161 . 58 ASN CA C 53.3 . 1 162 . 58 ASN N N 120.0 . 1 163 . 59 ARG H H 9.11 . 1 164 . 59 ARG CA C 53.7 . 1 165 . 59 ARG N N 129.8 . 1 166 . 60 PHE H H 8.26 . 1 167 . 60 PHE CA C 57.3 . 1 168 . 60 PHE N N 125.6 . 1 169 . 61 SER H H 6.01 . 1 170 . 61 SER CA C 59.7 . 1 171 . 61 SER N N 119.4 . 1 172 . 62 GLY H H 8.68 . 1 173 . 62 GLY CA C 45.5 . 1 174 . 62 GLY N N 114.9 . 1 175 . 63 VAL H H 7.73 . 1 176 . 63 VAL CA C 60.7 . 1 177 . 63 VAL N N 125.4 . 1 178 . 64 PRO CA C 63.3 . 1 179 . 65 ASP H H 8.44 . 1 180 . 65 ASP CA C 55.7 . 1 181 . 65 ASP N N 118.8 . 1 182 . 66 ARG H H 6.81 . 1 183 . 66 ARG CA C 56.8 . 1 184 . 66 ARG N N 114.6 . 1 185 . 67 PHE H H 7.57 . 1 186 . 67 PHE CA C 58.3 . 1 187 . 67 PHE N N 120.2 . 1 188 . 68 SER H H 8.96 . 1 189 . 68 SER CA C 57.3 . 1 190 . 68 SER N N 116.1 . 1 191 . 69 GLY H H 8.84 . 1 192 . 69 GLY CA C 44.3 . 1 193 . 69 GLY N N 111.2 . 1 194 . 70 SER H H 8.86 . 1 195 . 70 SER CA C 57.4 . 1 196 . 70 SER N N 115.6 . 1 197 . 71 GLY H H 8.49 . 1 198 . 71 GLY CA C 45.0 . 1 199 . 71 GLY N N 108.3 . 1 200 . 72 SER H H 7.45 . 1 201 . 72 SER CA C 57.7 . 1 202 . 72 SER N N 110.4 . 1 203 . 73 GLY H H 8.76 . 1 204 . 73 GLY CA C 49.3 . 1 205 . 73 GLY N N 110.6 . 1 206 . 74 THR H H 7.94 . 1 207 . 74 THR CA C 61.0 . 1 208 . 74 THR N N 117.3 . 1 209 . 75 ASP H H 6.94 . 1 210 . 75 ASP CA C 54.4 . 1 211 . 75 ASP N N 123.2 . 1 212 . 76 PHE H H 8.81 . 1 213 . 76 PHE CA C 57.3 . 1 214 . 76 PHE N N 122.1 . 1 215 . 77 THR H H 8.70 . 1 216 . 77 THR CA C 61.9 . 1 217 . 77 THR N N 118.0 . 1 218 . 78 LEU H H 8.65 . 1 219 . 78 LEU CA C 53.4 . 1 220 . 78 LEU N N 130.2 . 1 221 . 79 LYS H H 8.87 . 1 222 . 79 LYS CA C 54.6 . 1 223 . 79 LYS N N 127.0 . 1 224 . 80 ILE H H 8.54 . 1 225 . 80 ILE CA C 59.8 . 1 226 . 80 ILE N N 124.5 . 1 227 . 81 SER H H 8.91 . 1 228 . 81 SER CA C 60.9 . 1 229 . 81 SER N N 122.3 . 1 230 . 82 ARG H H 6.44 . 1 231 . 82 ARG CA C 55.5 . 1 232 . 82 ARG N N 119.5 . 1 233 . 83 VAL H H 8.29 . 1 234 . 83 VAL CA C 64.3 . 1 235 . 83 VAL N N 124.0 . 1 236 . 84 GLU H H 9.17 . 1 237 . 84 GLU CA C 54.3 . 1 238 . 84 GLU N N 130.1 . 1 239 . 85 ALA H H 9.02 . 1 240 . 85 ALA CA C 55.7 . 1 241 . 85 ALA N N 124.7 . 1 242 . 86 GLU H H 8.37 . 1 243 . 86 GLU CA C 57.7 . 1 244 . 86 GLU N N 114.3 . 1 245 . 87 ASP H H 7.99 . 1 246 . 87 ASP CA C 54.5 . 1 247 . 87 ASP N N 121.1 . 1 248 . 88 LEU H H 7.00 . 1 249 . 88 LEU CA C 56.4 . 1 250 . 88 LEU N N 119.0 . 1 251 . 89 GLY H H 7.48 . 1 252 . 89 GLY CA C 44.7 . 1 253 . 89 GLY N N 109.0 . 1 254 . 90 VAL H H 8.05 . 1 255 . 90 VAL CA C 61.3 . 1 256 . 90 VAL N N 120.9 . 1 257 . 91 TYR H H 8.93 . 1 258 . 91 TYR CA C 57.0 . 1 259 . 91 TYR N N 126.6 . 1 260 . 92 PHE H H 9.82 . 1 261 . 92 PHE CA C 57.0 . 1 262 . 92 PHE N N 122.1 . 1 263 . 93 CYS H H 8.02 . 1 264 . 93 CYS N N 118.0 . 1 265 . 94 SER H H 8.60 . 1 266 . 94 SER CA C 56.3 . 1 267 . 94 SER N N 116.2 . 1 268 . 95 GLN H H 8.24 . 1 269 . 95 GLN CA C 51.4 . 1 270 . 95 GLN N N 122.4 . 1 271 . 96 SER H H 8.88 . 1 272 . 96 SER CA C 55.7 . 1 273 . 96 SER N N 117.3 . 1 274 . 97 THR H H 7.80 . 1 275 . 97 THR CA C 66.5 . 1 276 . 97 THR N N 120.8 . 1 277 . 98 HIS H H 9.43 . 1 278 . 98 HIS CA C 53.8 . 1 279 . 98 HIS N N 122.9 . 1 280 . 99 VAL H H 8.23 . 1 281 . 99 VAL CA C 59.5 . 1 282 . 99 VAL N N 120.3 . 1 283 . 101 PHE H H 7.74 . 1 284 . 101 PHE CA C 55.3 . 1 285 . 101 PHE N N 123.5 . 1 286 . 102 THR H H 7.27 . 1 287 . 102 THR CA C 59.6 . 1 288 . 102 THR N N 108.5 . 1 289 . 103 PHE H H 9.17 . 1 290 . 103 PHE CA C 57.3 . 1 291 . 103 PHE N N 120.4 . 1 292 . 104 GLY H H 9.12 . 1 293 . 104 GLY CA C 45.0 . 1 294 . 104 GLY N N 109.3 . 1 295 . 105 SER H H 8.25 . 1 296 . 105 SER CA C 60.6 . 1 297 . 105 SER N N 111.2 . 1 298 . 106 GLY H H 6.89 . 1 299 . 106 GLY CA C 45.1 . 1 300 . 106 GLY N N 107.8 . 1 301 . 107 THR H H 8.18 . 1 302 . 107 THR CA C 61.7 . 1 303 . 107 THR N N 120.5 . 1 304 . 108 LYS H H 8.36 . 1 305 . 108 LYS CA C 56.1 . 1 306 . 108 LYS N N 129.6 . 1 307 . 109 LEU H H 9.01 . 1 308 . 109 LEU CA C 55.3 . 1 309 . 109 LEU N N 132.8 . 1 310 . 110 GLU H H 8.00 . 1 311 . 110 GLU CA C 54.0 . 1 312 . 110 GLU N N 126.0 . 1 313 . 111 ILE H H 8.16 . 1 314 . 111 ILE CA C 60.0 . 1 315 . 111 ILE N N 122.1 . 1 316 . 112 LYS H H 8.20 . 1 317 . 112 LYS CA C 56.3 . 1 318 . 112 LYS N N 129.4 . 1 319 . 113 ARG H H 8.07 . 1 320 . 113 ARG CA C 57.7 . 1 321 . 113 ARG N N 131.6 . 1 stop_ save_