data_5065 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Quail Cysteine and Glycine-rich Protein, NMR, 15 Minimized Model Structures ; _BMRB_accession_number 5065 _BMRB_flat_file_name bmr5065.str _Entry_type original _Submission_date 2001-06-29 _Accession_date 2001-06-29 _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 Schuler Wolfgang . . 2 Kloiber Karin . . 3 Matt Theresia . . 4 Bister Klaus . . 5 Konrat Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 296 "13C chemical shifts" 231 "15N chemical shifts" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-14 original author . stop_ _Original_release_date 2001-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Application of Cross-correlated NMR Spin Relaxation to the Zinc-finger Protein CRP2(LIM2): Evidence for Collective Motions in LIM Domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21466850 _PubMed_ID 11583159 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schuler Wolfgang . . 2 Kloiber Karin . . 3 Matt Theresia . . 4 Bister Klaus . . 5 Konrat Robert . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9596 _Page_last 9604 _Year 2001 _Details . loop_ _Keyword 'LIM domain containing proteins' 'metal-binding protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Konrat R, Weiskirchen R, Krautler B, Bister K. Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2. J Biol Chem. 1997 May 2;272(18):12001-7. ; _Citation_title 'Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9115265 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Konrat R . . 2 Weiskirchen R . . 3 Krautler B . . 4 Bister K . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 272 _Journal_issue 18 _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 12001 _Page_last 12007 _Year 1997 _Details ; Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3) are implicated in diverse processes linked to cellular differentiation and growth control. CRP proteins contain two LIM domains, each formed by two zinc-binding modules of the CCHC and CCCC type, respectively. The solution structure of the carboxyl-terminal LIM domain (LIM2) from recombinant quail CRP2 was determined by multidimensional homo- and heteronuclear magnetic resonance spectroscopy. The folding topology retains both independent zinc binding modules (CCHC and CCCC). Each module consists of two orthogonally arranged antiparallel beta-sheets, and the carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N magnetic relaxation data indicate that the modules differ in terms of conformational flexibility. They pack together via a hydrophobic core region. In addition, Arg122 in the CCHC module and Glu155 in the CCCC module are linked by an intermodular hydrogen bond and/or salt bridge. These residues are absolutely conserved in the CRP family of LIM proteins, and their interaction might contribute to the relative orientation of the two zinc-binding modules in CRP LIM2 domains. The global fold of quail CRP2 LIM2 is very similar to that of the carboxyl-terminal LIM domain of the related but functionally distinct CRP family member CRP1, analyzed recently. The carboxyl-terminal CCCC module is structurally related to the DNA-binding domain of the erythroid transcription factor GATA-1. In the two zinc-binding modules of quail CRP2 LIM2, flexible loop regions made up of conserved amino acid residues are located on the same side of the LIM2 domain and may cooperate in macromolecular recognition. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Konrat R, Krautler B, Weiskirchen R, Bister K. Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. J Biol Chem. 1998 Sep 4;273(36):23233-40. ; _Citation_title 'Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9722554 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Konrat R . . 2 Krautler B . . 3 Weiskirchen R . . 4 Bister K . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 273 _Journal_issue 36 _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 23233 _Page_last 23240 _Year 1998 _Details ; Members of the cysteine- and glycine-rich protein family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control, and pathogenesis. Here we report the solution structure of full-length recombinant quail CRP2 as determined by multi-dimensional triple-resonance NMR spectroscopy. The structural analysis revealed that the global fold of the two LIM domains in the context of the full-length protein is identical to the recently determined solution structures of the isolated individual LIM domains of quail CRP2. There is no preference in relative spatial orientation of the two domains. This supports the view that the two LIM domains are independent structural and presumably functional modules of CRP proteins. This is also reflected by the dynamic properties of CRP2 probed by 15N relaxation values (T1, T2, and nuclear Overhauser effect). A model-free analysis revealed local variations in mobility along the backbone of the two LIM domains in the native protein, similar to those observed for the isolated domains. Interestingly, fast and slow motions observed in the 58-amino acid linker region between the two LIM domains endow extensive motional freedom to CRP2. The dynamic analysis indicates independent backbone mobility of the two LIM domains and rules out correlated LIM domain motion in full-length CRP2. The finding that the LIM domains in a protein encompassing multiple LIM motifs are structurally and dynamically independent from each other supports the notion that these proteins may function as adaptor molecules arranging two or more protein constituents into a macromolecular complex. ; save_ ################################## # Molecular system description # ################################## save_system_CRP2(LIM2) _Saveframe_category molecular_system _Mol_system_name 'CYSTEINE-RICH PROTEIN 2' _Abbreviation_common CRP2(LIM2) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYSTEINE-RICH PROTEIN' $CRP2(LIM2) 'ZINC ION, I' $ZN 'ZINC ION, II' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CRP2(LIM2) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CYSTEINE-RICH PROTEIN CRP2(LIM2)' _Abbreviation_common CRP2(LIM2) _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; MDRGERLGIKPESSPSPHRP TTNPNTSKFAQKFGGAEKCS RCGDSVYAAEKVIGAGKPWH KNCFRCAKCGKSLESTTLTE KEGEIYCKGCYAKNFGPKGF GYGQGAGALVHAQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 82 MET 2 83 ASP 3 84 ARG 4 85 GLY 5 86 GLU 6 87 ARG 7 88 LEU 8 89 GLY 9 90 ILE 10 91 LYS 11 92 PRO 12 93 GLU 13 94 SER 14 95 SER 15 96 PRO 16 97 SER 17 98 PRO 18 99 HIS 19 100 ARG 20 101 PRO 21 102 THR 22 103 THR 23 104 ASN 24 105 PRO 25 106 ASN 26 107 THR 27 108 SER 28 109 LYS 29 110 PHE 30 111 ALA 31 112 GLN 32 113 LYS 33 114 PHE 34 115 GLY 35 116 GLY 36 117 ALA 37 118 GLU 38 119 LYS 39 120 CYS 40 121 SER 41 122 ARG 42 123 CYS 43 124 GLY 44 125 ASP 45 126 SER 46 127 VAL 47 128 TYR 48 129 ALA 49 130 ALA 50 131 GLU 51 132 LYS 52 133 VAL 53 134 ILE 54 135 GLY 55 136 ALA 56 137 GLY 57 138 LYS 58 139 PRO 59 140 TRP 60 141 HIS 61 142 LYS 62 143 ASN 63 144 CYS 64 145 PHE 65 146 ARG 66 147 CYS 67 148 ALA 68 149 LYS 69 150 CYS 70 151 GLY 71 152 LYS 72 153 SER 73 154 LEU 74 155 GLU 75 156 SER 76 157 THR 77 158 THR 78 159 LEU 79 160 THR 80 161 GLU 81 162 LYS 82 163 GLU 83 164 GLY 84 165 GLU 85 166 ILE 86 167 TYR 87 168 CYS 88 169 LYS 89 170 GLY 90 171 CYS 91 172 TYR 92 173 ALA 93 174 LYS 94 175 ASN 95 176 PHE 96 177 GLY 97 178 PRO 98 179 LYS 99 180 GLY 100 181 PHE 101 182 GLY 102 183 TYR 103 184 GLY 104 185 GLN 105 186 GLY 106 187 ALA 107 188 GLY 108 189 ALA 109 190 LEU 110 191 VAL 111 192 HIS 112 193 ALA 113 194 GLN 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 PDB 1QLI 'Quail Cysteine And Glycine-Rich Protein, Nmr, Minimized Average Structure' 100.00 113 100.00 100.00 6.49e-60 PDB 1IBI 'Quail Cysteine And Glycine-Rich Protein, Nmr, 15 Minimized Model Structures' 100.00 113 100.00 100.00 6.49e-60 PDB 1CXX 'Mutant R122a Of Quail Cysteine And Glycine-Rich Protein, Nmr, Minimized Structure' 100.00 113 99.12 99.12 3.94e-59 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 15:35:03 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $CRP2(LIM2) 'Japanese Quail' 93934 Eukaryota Metazoa Coturnix japonica CSRP2 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 $CRP2(LIM2) 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)PLYSS plasmid PET3D-QCRP2(LIM2) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CRP2(LIM2) . mM 1.0 2.0 '[U-13C; U-15N]' H2O 90 % . . . D2O 10 % . . [U-2H] 'potassium phosphate' 20 mM . . . KCl 50 mM . . . dithiothreitol 0.5 mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CRP2(LIM2) . mM 1.0 2.0 [U-15N] H2O 90 % . . . D2O 10 % . . [U-2H] 'potassium phosphate' 20 mM . . . KCl 50 mM . . . dithiothreitol 0.5 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 'v6.1 Rev.B' loop_ _Task collection stop_ _Details 'Varian Associates, Inc.' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 'v1.8 Rev 2001.030.21.27' loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version v3.3 loop_ _Task 'data analysis' stop_ _Details 'Kraulis, P.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task 'structure solution' stop_ _Details 'Brunger, A.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details 'Brunger, A.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model UNITYPLUS _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label . save_ save_3D_CCH-TOCSY-NNH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCH-TOCSY-NNH' _Sample_label . save_ save_3D_13C-NOESY-HSQC_(CA-centered)_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-HSQC (CA-centered)' _Sample_label . save_ save_3D_13C-NOESY-HSQC_(methyl-centered)_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-HSQC (methyl-centered)' _Sample_label . save_ save_3D_15N-NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCH-TOCSY-NNH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-HSQC (CA-centered)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-NOESY-HSQC (methyl-centered)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 70.5 . mM pH 7.2 0.2 n/a pressure 1 . atm temperature 299 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'CYSTEINE-RICH PROTEIN' _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 . 37 GLU HA H 4.24 0.03 1 2 . 37 GLU HB2 H 1.80 0.03 2 3 . 37 GLU HB3 H 1.59 0.03 2 4 . 37 GLU HG2 H 2.13 0.03 2 5 . 37 GLU HG3 H 2.05 0.03 2 6 . 37 GLU CA C 55.58 0.50 1 7 . 37 GLU CB C 31.50 0.50 1 8 . 37 GLU CG C 37.05 0.50 1 9 . 38 LYS H H 8.27 0.03 1 10 . 38 LYS HA H 4.23 0.03 1 11 . 38 LYS HB2 H 1.46 0.03 2 12 . 38 LYS HB3 H 1.30 0.03 2 13 . 38 LYS HG2 H 1.50 0.03 2 14 . 38 LYS HG3 H 1.22 0.03 2 15 . 38 LYS HD2 H 1.50 0.03 1 16 . 38 LYS HD3 H 1.50 0.03 1 17 . 38 LYS HE2 H 2.94 0.03 1 18 . 38 LYS HE3 H 2.94 0.03 1 19 . 38 LYS CA C 54.02 0.50 1 20 . 38 LYS C C 175.11 0.50 1 21 . 38 LYS CB C 33.38 0.50 1 22 . 38 LYS CG C 24.32 0.50 1 23 . 38 LYS CD C 28.34 0.50 1 24 . 38 LYS CE C 42.14 0.50 1 25 . 38 LYS N N 121.06 0.25 1 26 . 39 CYS H H 8.33 0.03 1 27 . 39 CYS HA H 3.60 0.03 1 28 . 39 CYS HB2 H 3.32 0.03 2 29 . 39 CYS HB3 H 2.05 0.03 2 30 . 39 CYS CA C 59.05 0.50 1 31 . 39 CYS C C 177.71 0.50 1 32 . 39 CYS CB C 31.06 0.50 1 33 . 39 CYS N N 124.88 0.25 1 34 . 40 SER H H 8.09 0.03 1 35 . 40 SER HA H 3.84 0.03 1 36 . 40 SER HB2 H 2.81 0.03 2 37 . 40 SER HB3 H 1.62 0.03 2 38 . 40 SER CA C 61.34 0.50 1 39 . 40 SER C C 172.43 0.50 1 40 . 40 SER CB C 61.76 0.50 1 41 . 40 SER N N 125.83 0.25 1 42 . 41 ARG H H 8.97 0.03 1 43 . 41 ARG HA H 4.78 0.03 1 44 . 41 ARG HB2 H 2.62 0.03 2 45 . 41 ARG HB3 H 2.38 0.03 2 46 . 41 ARG HG2 H 2.25 0.03 2 47 . 41 ARG HG3 H 1.63 0.03 2 48 . 41 ARG HD2 H 3.51 0.03 1 49 . 41 ARG HD3 H 3.51 0.03 1 50 . 41 ARG CA C 56.26 0.50 1 51 . 41 ARG C C 176.09 0.50 1 52 . 41 ARG CB C 29.82 0.50 1 53 . 41 ARG CG C 25.08 0.50 1 54 . 41 ARG CD C 40.62 0.50 1 55 . 41 ARG N N 123.64 0.25 1 56 . 42 CYS H H 7.99 0.03 1 57 . 42 CYS HA H 4.94 0.03 1 58 . 42 CYS HB2 H 3.40 0.03 2 59 . 42 CYS HB3 H 3.02 0.03 2 60 . 42 CYS CA C 58.77 0.50 1 61 . 42 CYS C C 176.60 0.50 1 62 . 42 CYS CB C 31.90 0.50 1 63 . 42 CYS N N 116.18 0.25 1 64 . 43 GLY H H 7.73 0.03 1 65 . 43 GLY HA2 H 4.22 0.03 2 66 . 43 GLY HA3 H 3.74 0.03 2 67 . 43 GLY CA C 46.19 0.50 1 68 . 43 GLY C C 172.61 0.50 1 69 . 43 GLY N N 112.49 0.25 1 70 . 44 ASP H H 8.43 0.03 1 71 . 44 ASP HA H 5.12 0.03 1 72 . 44 ASP HB2 H 2.99 0.03 2 73 . 44 ASP HB3 H 2.90 0.03 2 74 . 44 ASP CA C 52.97 0.50 1 75 . 44 ASP C C 176.35 0.50 1 76 . 44 ASP CB C 42.42 0.50 1 77 . 44 ASP N N 122.75 0.25 1 78 . 45 SER H H 8.75 0.03 1 79 . 45 SER HA H 4.38 0.03 1 80 . 45 SER HB2 H 3.64 0.03 2 81 . 45 SER HB3 H 3.42 0.03 2 82 . 45 SER CA C 59.85 0.50 1 83 . 45 SER C C 173.29 0.50 1 84 . 45 SER CB C 63.93 0.50 1 85 . 45 SER N N 117.24 0.25 1 86 . 46 VAL H H 8.65 0.03 1 87 . 46 VAL HA H 4.31 0.03 1 88 . 46 VAL HB H 0.92 0.03 1 89 . 46 VAL HG1 H 0.42 0.03 1 90 . 46 VAL HG2 H 0.42 0.03 1 91 . 46 VAL CA C 58.75 0.50 1 92 . 46 VAL C C 173.48 0.50 1 93 . 46 VAL CB C 33.83 0.50 1 94 . 46 VAL CG1 C 19.36 0.50 2 95 . 46 VAL CG2 C 21.51 0.50 2 96 . 46 VAL N N 124.55 0.25 1 97 . 47 TYR H H 8.97 0.03 1 98 . 47 TYR HA H 4.62 0.03 1 99 . 47 TYR HB2 H 3.32 0.03 2 100 . 47 TYR HB3 H 2.88 0.03 2 101 . 47 TYR HD1 H 7.23 0.03 1 102 . 47 TYR HD2 H 7.23 0.03 1 103 . 47 TYR HE1 H 6.82 0.03 1 104 . 47 TYR HE2 H 6.82 0.03 1 105 . 47 TYR CA C 57.37 0.50 1 106 . 47 TYR C C 176.67 0.50 1 107 . 47 TYR CB C 38.71 0.50 1 108 . 47 TYR CD1 C 133.15 0.50 1 109 . 47 TYR CD2 C 133.15 0.50 1 110 . 47 TYR CE1 C 118.22 0.50 1 111 . 47 TYR CE2 C 118.22 0.50 1 112 . 47 TYR N N 129.18 0.25 1 113 . 48 ALA H H 8.58 0.03 1 114 . 48 ALA HA H 3.87 0.03 1 115 . 48 ALA HB H 1.50 0.03 1 116 . 48 ALA CA C 56.21 0.50 1 117 . 48 ALA C C 179.74 0.50 1 118 . 48 ALA CB C 18.60 0.50 1 119 . 48 ALA N N 123.50 0.25 1 120 . 49 ALA H H 8.43 0.03 1 121 . 49 ALA HA H 4.21 0.03 1 122 . 49 ALA HB H 1.49 0.03 1 123 . 49 ALA CA C 54.27 0.50 1 124 . 49 ALA C C 178.28 0.50 1 125 . 49 ALA CB C 18.52 0.50 1 126 . 49 ALA N N 117.46 0.25 1 127 . 50 GLU H H 7.67 0.03 1 128 . 50 GLU HA H 4.58 0.03 1 129 . 50 GLU HB2 H 2.55 0.03 2 130 . 50 GLU HB3 H 2.30 0.03 2 131 . 50 GLU HG2 H 2.44 0.03 2 132 . 50 GLU HG3 H 2.38 0.03 2 133 . 50 GLU CA C 55.35 0.50 1 134 . 50 GLU C C 174.46 0.50 1 135 . 50 GLU CB C 30.96 0.50 1 136 . 50 GLU CG C 36.70 0.50 1 137 . 50 GLU N N 114.73 0.25 1 138 . 51 LYS H H 7.13 0.03 1 139 . 51 LYS HA H 4.37 0.03 1 140 . 51 LYS HB2 H 1.77 0.03 2 141 . 51 LYS HB3 H 1.56 0.03 2 142 . 51 LYS HD2 H 1.55 0.03 2 143 . 51 LYS HD3 H 1.46 0.03 2 144 . 51 LYS HE2 H 2.75 0.03 2 145 . 51 LYS HE3 H 2.65 0.03 2 146 . 51 LYS HG2 H 1.10 0.03 1 147 . 51 LYS HG3 H 1.10 0.03 1 148 . 51 LYS CA C 57.05 0.50 1 149 . 51 LYS C C 175.60 0.50 1 150 . 51 LYS CB C 33.89 0.50 1 151 . 51 LYS CG C 24.65 0.50 1 152 . 51 LYS CD C 29.54 0.50 1 153 . 51 LYS CE C 41.37 0.50 1 154 . 51 LYS N N 121.56 0.25 1 155 . 52 VAL H H 8.97 0.03 1 156 . 52 VAL HA H 4.29 0.03 1 157 . 52 VAL HB H 1.55 0.03 1 158 . 52 VAL HG1 H 0.33 0.03 2 159 . 52 VAL HG2 H 0.44 0.03 2 160 . 52 VAL CA C 60.10 0.50 1 161 . 52 VAL C C 173.18 0.50 1 162 . 52 VAL CB C 34.88 0.50 1 163 . 52 VAL CG1 C 20.40 0.50 2 164 . 52 VAL CG2 C 20.30 0.50 2 165 . 52 VAL N N 125.47 0.25 1 166 . 53 ILE H H 8.16 0.03 1 167 . 53 ILE HA H 5.00 0.03 1 168 . 53 ILE HB H 1.78 0.03 1 169 . 53 ILE HG12 H 1.35 0.03 1 170 . 53 ILE HG13 H 1.16 0.03 1 171 . 53 ILE HG2 H 0.73 0.03 1 172 . 53 ILE HD1 H 0.65 0.03 1 173 . 53 ILE CA C 58.35 0.50 1 174 . 53 ILE C C 176.42 0.50 1 175 . 53 ILE CB C 37.58 0.50 1 176 . 53 ILE CG1 C 26.83 0.50 1 177 . 53 ILE CG2 C 16.75 0.50 1 178 . 53 ILE CD1 C 10.99 0.50 1 179 . 53 ILE N N 124.94 0.25 1 180 . 54 GLY H H 9.01 0.03 1 181 . 54 GLY CA C 45.33 0.50 1 182 . 54 GLY C C 173.35 0.50 1 183 . 54 GLY N N 112.72 0.25 1 184 . 55 ALA H H 9.79 0.03 1 185 . 55 ALA HA H 4.13 0.03 1 186 . 55 ALA HB H 1.49 0.03 1 187 . 55 ALA CA C 53.00 0.50 1 188 . 55 ALA C C 176.81 0.50 1 189 . 55 ALA CB C 16.78 0.50 1 190 . 55 ALA N N 129.68 0.25 1 191 . 56 GLY H H 8.67 0.03 1 192 . 56 GLY HA2 H 4.06 0.03 2 193 . 56 GLY HA3 H 3.59 0.03 2 194 . 56 GLY CA C 45.02 0.50 1 195 . 56 GLY C C 173.70 0.50 1 196 . 56 GLY N N 103.14 0.25 1 197 . 57 LYS H H 8.01 0.03 1 198 . 57 LYS CA C 52.29 0.50 1 199 . 57 LYS C C 177.47 0.50 1 200 . 57 LYS N N 123.93 0.25 1 201 . 58 PRO HA H 5.08 0.03 1 202 . 58 PRO HB2 H 1.80 0.03 2 203 . 58 PRO HB3 H 1.29 0.03 2 204 . 58 PRO HG2 H 2.12 0.03 2 205 . 58 PRO HG3 H 1.83 0.03 2 206 . 58 PRO HD2 H 3.59 0.03 2 207 . 58 PRO HD3 H 3.46 0.03 2 208 . 58 PRO CA C 61.63 0.50 1 209 . 58 PRO C C 176.74 0.50 1 210 . 58 PRO CB C 32.86 0.50 1 211 . 58 PRO CG C 26.04 0.50 1 212 . 58 PRO CD C 49.79 0.50 1 213 . 59 TRP H H 8.75 0.03 1 214 . 59 TRP HA H 5.41 0.03 1 215 . 59 TRP HB2 H 3.32 0.03 2 216 . 59 TRP HB3 H 2.55 0.03 2 217 . 59 TRP HD1 H 7.30 0.03 1 218 . 59 TRP HE1 H 10.17 0.03 1 219 . 59 TRP HE3 H 7.46 0.03 1 220 . 59 TRP HZ2 H 7.10 0.03 1 221 . 59 TRP HZ3 H 7.01 0.03 1 222 . 59 TRP HH2 H 7.26 0.03 1 223 . 59 TRP CA C 54.89 0.50 1 224 . 59 TRP C C 177.20 0.50 1 225 . 59 TRP CB C 31.96 0.50 1 226 . 59 TRP CD1 C 130.43 0.50 1 227 . 59 TRP CE3 C 119.67 0.50 1 228 . 59 TRP CZ2 C 113.81 0.50 1 229 . 59 TRP CZ3 C 121.86 0.50 1 230 . 59 TRP CH2 C 124.56 0.50 1 231 . 59 TRP N N 119.21 0.25 1 232 . 59 TRP NE1 N 131.22 0.25 1 233 . 60 HIS H H 8.90 0.03 1 234 . 60 HIS HA H 4.81 0.03 1 235 . 60 HIS HB2 H 3.73 0.03 2 236 . 60 HIS HB3 H 3.60 0.03 2 237 . 60 HIS HD2 H 7.44 0.03 1 238 . 60 HIS HE1 H 7.20 0.03 1 239 . 60 HIS CA C 59.19 0.50 1 240 . 60 HIS C C 178.77 0.50 1 241 . 60 HIS CB C 30.51 0.50 1 242 . 60 HIS CD2 C 118.82 0.50 1 243 . 60 HIS N N 120.56 0.25 1 244 . 61 LYS H H 9.32 0.03 1 245 . 61 LYS HA H 3.95 0.03 1 246 . 61 LYS HB2 H 1.96 0.03 2 247 . 61 LYS HB3 H 1.86 0.03 2 248 . 61 LYS HG2 H 1.43 0.03 1 249 . 61 LYS HG3 H 1.43 0.03 1 250 . 61 LYS HE2 H 2.97 0.03 1 251 . 61 LYS HE3 H 2.97 0.03 1 252 . 61 LYS CA C 60.88 0.50 1 253 . 61 LYS C C 179.95 0.50 1 254 . 61 LYS CB C 31.83 0.50 1 255 . 61 LYS CG C 25.66 0.50 1 256 . 61 LYS CD C 29.39 0.50 1 257 . 61 LYS CE C 42.14 0.50 1 258 . 61 LYS N N 127.13 0.25 1 259 . 62 ASN H H 9.26 0.03 1 260 . 62 ASN HA H 4.70 0.03 1 261 . 62 ASN HB2 H 2.94 0.03 2 262 . 62 ASN HB3 H 2.86 0.03 2 263 . 62 ASN CA C 54.72 0.50 1 264 . 62 ASN C C 175.97 0.50 1 265 . 62 ASN CB C 38.19 0.50 1 266 . 62 ASN N N 114.66 0.25 1 267 . 63 CYS H H 7.70 0.03 1 268 . 63 CYS HA H 4.43 0.03 1 269 . 63 CYS HB2 H 3.55 0.03 2 270 . 63 CYS HB3 H 3.33 0.03 2 271 . 63 CYS CA C 60.15 0.50 1 272 . 63 CYS C C 173.58 0.50 1 273 . 63 CYS CB C 31.64 0.50 1 274 . 63 CYS N N 117.31 0.25 1 275 . 64 PHE H H 7.35 0.03 1 276 . 64 PHE HA H 4.13 0.03 1 277 . 64 PHE HB2 H 3.31 0.03 2 278 . 64 PHE HB3 H 2.60 0.03 2 279 . 64 PHE HD1 H 6.38 0.03 1 280 . 64 PHE HD2 H 6.38 0.03 1 281 . 64 PHE CA C 56.49 0.50 1 282 . 64 PHE HE1 H 6.64 0.03 1 283 . 64 PHE HE2 H 6.64 0.03 1 284 . 64 PHE C C 173.23 0.50 1 285 . 64 PHE CB C 36.67 0.50 1 286 . 64 PHE CD1 C 132.35 0.50 1 287 . 64 PHE CD2 C 132.35 0.50 1 288 . 64 PHE N N 124.01 0.25 1 289 . 65 ARG H H 7.63 0.03 1 290 . 65 ARG HA H 4.73 0.03 1 291 . 65 ARG HB2 H 1.26 0.03 2 292 . 65 ARG HB3 H 1.07 0.03 2 293 . 65 ARG HG2 H 1.21 0.03 2 294 . 65 ARG HG3 H 1.13 0.03 2 295 . 65 ARG HD2 H 3.20 0.03 2 296 . 65 ARG HD3 H 3.09 0.03 2 297 . 65 ARG CA C 52.70 0.50 1 298 . 65 ARG C C 173.95 0.50 1 299 . 65 ARG CB C 34.78 0.50 1 300 . 65 ARG CG C 27.59 0.50 1 301 . 65 ARG CD C 43.30 0.50 1 302 . 65 ARG N N 122.29 0.25 1 303 . 66 CYS H H 8.73 0.03 1 304 . 66 CYS HA H 3.82 0.03 1 305 . 66 CYS HB2 H 3.32 0.03 2 306 . 66 CYS HB3 H 2.76 0.03 2 307 . 66 CYS CA C 59.83 0.50 1 308 . 66 CYS C C 177.19 0.50 1 309 . 66 CYS CB C 30.89 0.50 1 310 . 66 CYS N N 123.85 0.25 1 311 . 67 ALA H H 8.86 0.03 1 312 . 67 ALA HA H 3.87 0.03 1 313 . 67 ALA HB H 1.21 0.03 1 314 . 67 ALA CA C 54.80 0.50 1 315 . 67 ALA C C 177.49 0.50 1 316 . 67 ALA CB C 18.23 0.50 1 317 . 67 ALA N N 133.93 0.25 1 318 . 68 LYS H H 8.98 0.03 1 319 . 68 LYS HA H 4.64 0.03 1 320 . 68 LYS HB2 H 2.40 0.03 2 321 . 68 LYS HB3 H 2.17 0.03 2 322 . 68 LYS HG2 H 1.52 0.03 1 323 . 68 LYS HG3 H 1.52 0.03 1 324 . 68 LYS CA C 56.69 0.50 1 325 . 68 LYS C C 176.98 0.50 1 326 . 68 LYS CB C 33.65 0.50 1 327 . 68 LYS CG C 25.21 0.50 1 328 . 68 LYS CD C 28.25 0.50 1 329 . 68 LYS CE C 42.04 0.50 1 330 . 68 LYS N N 118.75 0.25 1 331 . 69 CYS H H 8.41 0.03 1 332 . 69 CYS HA H 4.94 0.03 1 333 . 69 CYS HB2 H 3.28 0.03 2 334 . 69 CYS HB3 H 2.67 0.03 2 335 . 69 CYS CA C 59.19 0.50 1 336 . 69 CYS C C 177.14 0.50 1 337 . 69 CYS CB C 32.83 0.50 1 338 . 69 CYS N N 118.57 0.25 1 339 . 70 GLY H H 7.84 0.03 1 340 . 70 GLY HA2 H 4.19 0.03 2 341 . 70 GLY HA3 H 3.72 0.03 2 342 . 70 GLY CA C 46.19 0.50 1 343 . 70 GLY C C 173.21 0.50 1 344 . 70 GLY N N 112.67 0.25 1 345 . 71 LYS H H 8.60 0.03 1 346 . 71 LYS HA H 4.17 0.03 1 347 . 71 LYS HB2 H 1.82 0.03 2 348 . 71 LYS HB3 H 1.69 0.03 2 349 . 71 LYS HG2 H 1.41 0.03 1 350 . 71 LYS HG3 H 1.41 0.03 1 351 . 71 LYS HE2 H 2.97 0.03 1 352 . 71 LYS HE3 H 2.97 0.03 1 353 . 71 LYS CA C 57.23 0.50 1 354 . 71 LYS C C 176.54 0.50 1 355 . 71 LYS CB C 33.43 0.50 1 356 . 71 LYS CG C 24.78 0.50 1 357 . 71 LYS CD C 29.44 0.50 1 358 . 71 LYS CE C 41.91 0.50 1 359 . 71 LYS N N 125.02 0.25 1 360 . 72 SER H H 8.75 0.03 1 361 . 72 SER HA H 4.17 0.03 1 362 . 72 SER HB2 H 3.95 0.03 2 363 . 72 SER HB3 H 3.88 0.03 2 364 . 72 SER CA C 60.24 0.50 1 365 . 72 SER C C 174.20 0.50 1 366 . 72 SER CB C 63.06 0.50 1 367 . 72 SER N N 120.12 0.25 1 368 . 73 LEU H H 7.69 0.03 1 369 . 73 LEU HA H 4.34 0.03 1 370 . 73 LEU HB2 H 0.72 0.03 2 371 . 73 LEU HB3 H 0.38 0.03 2 372 . 73 LEU HG H 1.24 0.03 1 373 . 73 LEU HD1 H -0.07 0.03 2 374 . 73 LEU HD2 H 0.50 0.03 2 375 . 73 LEU CA C 53.30 0.50 1 376 . 73 LEU CB C 43.21 0.50 1 377 . 73 LEU CG C 26.14 0.50 1 378 . 73 LEU CD1 C 25.57 0.50 2 379 . 73 LEU CD2 C 22.20 0.50 2 380 . 73 LEU N N 124.90 0.25 1 381 . 74 GLU H H 7.51 0.03 1 382 . 74 GLU CA C 55.21 0.50 1 383 . 74 GLU N N 116.82 0.25 1 384 . 76 THR HA H 4.46 0.03 1 385 . 76 THR HB H 4.23 0.03 1 386 . 76 THR HG2 H 1.28 0.03 1 387 . 76 THR CA C 62.06 0.50 1 388 . 76 THR C C 175.37 0.50 1 389 . 76 THR CB C 69.29 0.50 1 390 . 76 THR CG2 C 21.70 0.50 1 391 . 77 THR H H 7.62 0.03 1 392 . 77 THR HA H 4.54 0.03 1 393 . 77 THR HB H 4.48 0.03 1 394 . 77 THR HG2 H 1.17 0.03 1 395 . 77 THR CA C 61.03 0.50 1 396 . 77 THR C C 173.61 0.50 1 397 . 77 THR CB C 69.75 0.50 1 398 . 77 THR CG2 C 22.29 0.50 1 399 . 77 THR N N 111.72 0.25 1 400 . 78 LEU H H 7.38 0.03 1 401 . 78 LEU HA H 4.61 0.03 1 402 . 78 LEU HG H 1.64 0.03 1 403 . 78 LEU HD1 H 0.69 0.03 2 404 . 78 LEU HD2 H 0.78 0.03 2 405 . 78 LEU HB2 H 1.51 0.03 1 406 . 78 LEU HB3 H 1.51 0.03 1 407 . 78 LEU CA C 54.79 0.50 1 408 . 78 LEU C C 175.61 0.50 1 409 . 78 LEU CB C 44.54 0.50 1 410 . 78 LEU CG C 26.28 0.50 1 411 . 78 LEU CD1 C 25.38 0.50 2 412 . 78 LEU CD2 C 27.93 0.50 2 413 . 78 LEU N N 122.41 0.25 1 414 . 79 THR H H 8.72 0.03 1 415 . 79 THR HA H 4.37 0.03 1 416 . 79 THR HB H 3.45 0.03 1 417 . 79 THR HG2 H 0.58 0.03 1 418 . 79 THR CA C 61.72 0.50 1 419 . 79 THR C C 171.95 0.50 1 420 . 79 THR CB C 71.13 0.50 1 421 . 79 THR CG2 C 22.11 0.50 1 422 . 79 THR N N 118.09 0.25 1 423 . 80 GLU H H 8.50 0.03 1 424 . 80 GLU HA H 5.46 0.03 1 425 . 80 GLU HB2 H 2.02 0.03 2 426 . 80 GLU HB3 H 1.86 0.03 2 427 . 80 GLU HG2 H 2.18 0.03 1 428 . 80 GLU HG3 H 2.18 0.03 1 429 . 80 GLU CA C 54.42 0.50 1 430 . 80 GLU C C 175.27 0.50 1 431 . 80 GLU CB C 32.38 0.50 1 432 . 80 GLU CG C 35.99 0.50 1 433 . 80 GLU N N 124.90 0.25 1 434 . 81 LYS H H 9.02 0.03 1 435 . 81 LYS HA H 4.40 0.03 1 436 . 81 LYS CA C 56.39 0.50 1 437 . 81 LYS C C 175.68 0.50 1 438 . 81 LYS N N 123.83 0.25 1 439 . 82 GLU HA H 4.76 0.03 1 440 . 82 GLU HB2 H 2.23 0.03 2 441 . 82 GLU CA C 56.91 0.50 1 442 . 82 GLU C C 175.81 0.50 1 443 . 82 GLU CB C 27.78 0.50 1 444 . 82 GLU CG C 36.87 0.50 1 445 . 83 GLY H H 9.09 0.03 1 446 . 83 GLY HA2 H 4.25 0.03 2 447 . 83 GLY HA3 H 3.77 0.03 2 448 . 83 GLY CA C 45.61 0.50 1 449 . 83 GLY C C 172.96 0.50 1 450 . 83 GLY N N 106.46 0.25 1 451 . 84 GLU H H 7.95 0.03 1 452 . 84 GLU HA H 5.07 0.03 1 453 . 84 GLU HB2 H 1.96 0.03 2 454 . 84 GLU HB3 H 1.90 0.03 2 455 . 84 GLU HG2 H 2.34 0.03 2 456 . 84 GLU HG3 H 2.20 0.03 2 457 . 84 GLU CA C 53.41 0.50 1 458 . 84 GLU C C 174.64 0.50 1 459 . 84 GLU CB C 33.17 0.50 1 460 . 84 GLU CG C 36.68 0.50 1 461 . 84 GLU N N 122.78 0.25 1 462 . 85 ILE H H 8.84 0.03 1 463 . 85 ILE HA H 4.95 0.03 1 464 . 85 ILE HB H 1.14 0.03 1 465 . 85 ILE HG12 H 0.99 0.03 1 466 . 85 ILE HG13 H 0.51 0.03 1 467 . 85 ILE HG2 H 0.53 0.03 1 468 . 85 ILE HD1 H -0.77 0.03 1 469 . 85 ILE CA C 59.63 0.50 1 470 . 85 ILE C C 173.12 0.50 1 471 . 85 ILE CB C 40.56 0.50 1 472 . 85 ILE CG1 C 23.80 0.50 1 473 . 85 ILE CG2 C 18.31 0.50 1 474 . 85 ILE CD1 C 12.93 0.50 1 475 . 85 ILE N N 114.84 0.25 1 476 . 86 TYR H H 8.23 0.03 1 477 . 86 TYR HA H 5.66 0.03 1 478 . 86 TYR HB2 H 3.36 0.03 2 479 . 86 TYR HB3 H 2.82 0.03 2 480 . 86 TYR HD1 H 7.08 0.03 1 481 . 86 TYR HD2 H 7.08 0.03 1 482 . 86 TYR HE1 H 6.84 0.03 1 483 . 86 TYR HE2 H 6.84 0.03 1 484 . 86 TYR CA C 56.23 0.50 1 485 . 86 TYR C C 176.20 0.50 1 486 . 86 TYR CB C 43.73 0.50 1 487 . 86 TYR CD1 C 133.17 0.50 1 488 . 86 TYR CD2 C 133.17 0.50 1 489 . 86 TYR N N 118.22 0.25 1 490 . 87 CYS H H 9.69 0.03 1 491 . 87 CYS HA H 5.03 0.03 1 492 . 87 CYS HB2 H 3.48 0.03 2 493 . 87 CYS HB3 H 2.79 0.03 2 494 . 87 CYS CA C 57.40 0.50 1 495 . 87 CYS C C 175.91 0.50 1 496 . 87 CYS CB C 30.99 0.50 1 497 . 87 CYS N N 120.71 0.25 1 498 . 88 LYS H H 8.58 0.03 1 499 . 88 LYS HA H 3.96 0.03 1 500 . 88 LYS HB2 H 1.85 0.03 1 501 . 88 LYS HB3 H 1.85 0.03 1 502 . 88 LYS HG2 H 1.44 0.03 1 503 . 88 LYS HG3 H 1.44 0.03 1 504 . 88 LYS HD2 H 1.68 0.03 1 505 . 88 LYS HD3 H 1.68 0.03 1 506 . 88 LYS HE2 H 3.01 0.03 1 507 . 88 LYS HE3 H 3.01 0.03 1 508 . 88 LYS CA C 59.78 0.50 1 509 . 88 LYS C C 179.70 0.50 1 510 . 88 LYS CB C 32.12 0.50 1 511 . 88 LYS CG C 25.32 0.50 1 512 . 88 LYS CD C 29.24 0.50 1 513 . 88 LYS CE C 42.04 0.50 1 514 . 88 LYS N N 120.75 0.25 1 515 . 89 GLY H H 8.50 0.03 1 516 . 89 GLY HA2 H 4.05 0.03 2 517 . 89 GLY HA3 H 3.90 0.03 2 518 . 89 GLY CA C 46.76 0.50 1 519 . 89 GLY C C 176.85 0.50 1 520 . 89 GLY N N 109.66 0.25 1 521 . 90 CYS H H 9.18 0.03 1 522 . 90 CYS HA H 3.94 0.03 1 523 . 90 CYS HB2 H 3.20 0.03 2 524 . 90 CYS HB3 H 2.77 0.03 2 525 . 90 CYS CA C 64.69 0.50 1 526 . 90 CYS C C 178.59 0.50 1 527 . 90 CYS CB C 29.71 0.50 1 528 . 90 CYS N N 127.03 0.25 1 529 . 91 TYR H H 8.83 0.03 1 530 . 91 TYR HA H 3.74 0.03 1 531 . 91 TYR HB2 H 3.13 0.03 1 532 . 91 TYR HB3 H 3.13 0.03 1 533 . 91 TYR HD1 H 6.83 0.03 1 534 . 91 TYR HD2 H 6.83 0.03 1 535 . 91 TYR HE1 H 6.84 0.03 1 536 . 91 TYR HE2 H 6.84 0.03 1 537 . 91 TYR CA C 61.84 0.50 1 538 . 91 TYR C C 177.10 0.50 1 539 . 91 TYR CB C 38.33 0.50 1 540 . 91 TYR CD1 C 133.27 0.50 1 541 . 91 TYR CD2 C 133.27 0.50 1 542 . 91 TYR N N 122.67 0.25 1 543 . 92 ALA H H 8.02 0.03 1 544 . 92 ALA HA H 4.06 0.03 1 545 . 92 ALA HB H 1.56 0.03 1 546 . 92 ALA CA C 54.66 0.50 1 547 . 92 ALA C C 174.64 0.50 1 548 . 92 ALA CB C 18.04 0.50 1 549 . 92 ALA N N 121.09 0.25 1 550 . 93 LYS H H 7.51 0.03 1 551 . 93 LYS HA H 3.95 0.03 1 552 . 93 LYS HB2 H 1.74 0.03 1 553 . 93 LYS HB3 H 1.74 0.03 1 554 . 93 LYS HD2 H 1.70 0.03 2 555 . 93 LYS HD3 H 1.62 0.03 2 556 . 93 LYS HG2 H 1.45 0.03 1 557 . 93 LYS HG3 H 1.45 0.03 1 558 . 93 LYS HE2 H 2.93 0.03 1 559 . 93 LYS HE3 H 2.93 0.03 1 560 . 93 LYS CA C 58.15 0.50 1 561 . 93 LYS C C 177.09 0.50 1 562 . 93 LYS CB C 32.99 0.50 1 563 . 93 LYS CG C 25.16 0.50 1 564 . 93 LYS CD C 29.15 0.50 1 565 . 93 LYS CE C 42.18 0.50 1 566 . 93 LYS N N 116.27 0.25 1 567 . 94 ASN H H 7.43 0.03 1 568 . 94 ASN HA H 3.89 0.03 1 569 . 94 ASN HB2 H 2.80 0.03 2 570 . 94 ASN HB3 H 2.68 0.03 2 571 . 94 ASN CA C 54.76 0.50 1 572 . 94 ASN C C 175.16 0.50 1 573 . 94 ASN CB C 39.08 0.50 1 574 . 94 ASN N N 114.76 0.25 1 575 . 95 PHE H H 8.05 0.03 1 576 . 95 PHE CA C 56.15 0.50 1 577 . 95 PHE C C 175.75 0.50 1 578 . 95 PHE CB C 39.09 0.50 1 579 . 95 PHE N N 117.33 0.25 1 580 . 96 GLY H H 7.56 0.03 1 581 . 96 GLY CA C 44.70 0.50 1 582 . 96 GLY C C 171.48 0.50 1 583 . 96 GLY N N 109.52 0.25 1 stop_ save_