data_6965 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N assignment of the soluble domain of the ba3 oxidase subunit II of Thermus thermophilus in the oxidized state ; _BMRB_accession_number 6965 _BMRB_flat_file_name bmr6965.str _Entry_type original _Submission_date 2006-02-01 _Accession_date 2006-02-01 _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 Muresanu Lucia . . 2 Pristovsek Primoz . . 3 Loehr Frank . . 4 Maneg Oliver . . 5 Mukrasch Marco D. . 6 Rueterjans Heinz . . 7 Ludwig Bernd . . 8 Luecke Christian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 713 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-26 original author 'original release' 2006-05-16 update author 'complete the citation saveframe' stop_ loop_ _Related_BMRB_accession_number _Relationship 5819 'same protein in reduced state' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16554303 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Muresanu Lucia . . 2 Pristovsek Primoz . . 3 Loehr Frank . . 4 Maneg Oliver . . 5 Mukrasch Marco D. . 6 Rueterjans Heinz . . 7 Ludwig Bernd . . 8 Luecke Christian . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 281 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14503 _Page_last 14513 _Year 2006 _Details . loop_ _Keyword 'CuA center' 'redox protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Slutter CE, Sanders D, Wittung P, Malmstrom BG, Aasa R, Richards JH, Gray HB, Fee JA. Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus. Biochemistry. 1996 Mar 19;35(11):3387-95. ; _Citation_title 'Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8639488 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Slutter 'C E' E. . 2 Sanders D . . 3 Wittung P . . 4 Malmstrom 'B G' G. . 5 Aasa R . . 6 Richards 'J H' H. . 7 Gray 'H B' B. . 8 Fee 'J A' A. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 35 _Journal_issue 11 _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 3387 _Page_last 3395 _Year 1996 _Details ; Recently, the genes of cytochrome ba3 from thermus thermophilus [Keightley, J.A., et al. (1995) J. Biol. Chem. 270, 20345-20358], a homolog of the heme-copper oxidase family, have been cloned. We report here expression of a truncated gene, encoding the copper A (CuA) domain of cytochrome ba3, that is regulated by a T7 RNA polymerase promoter in Escherichia coli. The CuA-containing domain is purified in high yields as a water-soluble, thermostable, purple-colored protein. Copper analysis by chemical assay, mass spectrometry, X-ray fluorescence, and EPR spin quantification show that this protein contains two copper ions bound in a mixed-valence state, indicating that the CuA site in cytochrome ba3, is a binuclear center. The absorption spectrum of the CuA site, free of the heme interference in cytochrome ba3, is similar to the spectra of other soluble fragments from the aa3-type oxidase of Parachccus denitrificans [Lappalainen, P., et al. (1993) J. Biol Chem. 268, 26416-26421] and the caa3-type oxidase of Bacillus subtilis [von Wachenfeldt, C. et al. (1994) FEBS Lett. 340, 109-113]. There are intense bands at 480 nm (3100 M(-1) cm(-1)) and 530 nm (3200 M(-1) cm(-1)), a band in the near -IR centered at 790 nm (1900 M(-1) cn(-1)), and a weaker band at 363 nm (1300M(-1) cm(-1)). The visible CD spectrum shows a positive-going band at 460 nm and a negative-going band at 527 nm, the opposite signs of which may result from the binuclear nature of the site. The secondary structure prediction from the far-UV CD spectrum indicates that this domain is predominantly beta-sheet, in agreement with the recent X-ray structure reported for the complete P. denitrificans cytochrome aa3 molecule [Iwata, S., et al. (1995) Nature 376, 660-669] and the engineered, purple CyoA protein [Wilmanns, M., et al. (1996) Proc. Natl Acad. Sci. U.S.A. 92, 11955-11959]. However, the thermostability of the fragment described here (Tm approximately 80 degrees C) and the stable binding of copper over a broad pH range (pH 3-9) suggest this protein may be uniquely suitable for detailed physical-chemical study. ; save_ ################################## # Molecular system description # ################################## save_system_CuA _Saveframe_category molecular_system _Mol_system_name 'CuA domain' _Abbreviation_common CuA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CuA domain' $CuA 'COPPER (I) ION, 1' $CU1 'COPPER (II) ION, 2' $CU stop_ _System_molecular_weight 15063 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer protein' stop_ _Database_query_date . _Details ; Upon oxidation, the copper center changes from +2 to +3 oxidation state. Since this charge is shared equally by both copper ions, each copper has a valence of +1.5 in the oxidized form ("mixed valence"). ; save_ ######################## # Monomeric polymers # ######################## save_CuA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CuA domain' _Abbreviation_common CuA _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 136 _Mol_residue_sequence ; MAYTLATHTAGVIPAGKLER VDPTTVRQEGPWADPAQAVV QTGPNQYTVYVLAFAFGYQP NPIEVPQGAEIVFKITSPDV IHGFHVEGTNINVEVLPGEV STVRYTFKRPGEYRIICNQY CGLGHQNMFGTIVVKE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 33 MET 2 34 ALA 3 35 TYR 4 36 THR 5 37 LEU 6 38 ALA 7 39 THR 8 40 HIS 9 41 THR 10 42 ALA 11 43 GLY 12 44 VAL 13 45 ILE 14 46 PRO 15 47 ALA 16 48 GLY 17 49 LYS 18 50 LEU 19 51 GLU 20 52 ARG 21 53 VAL 22 54 ASP 23 55 PRO 24 56 THR 25 57 THR 26 58 VAL 27 59 ARG 28 60 GLN 29 61 GLU 30 62 GLY 31 63 PRO 32 64 TRP 33 65 ALA 34 66 ASP 35 67 PRO 36 68 ALA 37 69 GLN 38 70 ALA 39 71 VAL 40 72 VAL 41 73 GLN 42 74 THR 43 75 GLY 44 76 PRO 45 77 ASN 46 78 GLN 47 79 TYR 48 80 THR 49 81 VAL 50 82 TYR 51 83 VAL 52 84 LEU 53 85 ALA 54 86 PHE 55 87 ALA 56 88 PHE 57 89 GLY 58 90 TYR 59 91 GLN 60 92 PRO 61 93 ASN 62 94 PRO 63 95 ILE 64 96 GLU 65 97 VAL 66 98 PRO 67 99 GLN 68 100 GLY 69 101 ALA 70 102 GLU 71 103 ILE 72 104 VAL 73 105 PHE 74 106 LYS 75 107 ILE 76 108 THR 77 109 SER 78 110 PRO 79 111 ASP 80 112 VAL 81 113 ILE 82 114 HIS 83 115 GLY 84 116 PHE 85 117 HIS 86 118 VAL 87 119 GLU 88 120 GLY 89 121 THR 90 122 ASN 91 123 ILE 92 124 ASN 93 125 VAL 94 126 GLU 95 127 VAL 96 128 LEU 97 129 PRO 98 130 GLY 99 131 GLU 100 132 VAL 101 133 SER 102 134 THR 103 135 VAL 104 136 ARG 105 137 TYR 106 138 THR 107 139 PHE 108 140 LYS 109 141 ARG 110 142 PRO 111 143 GLY 112 144 GLU 113 145 TYR 114 146 ARG 115 147 ILE 116 148 ILE 117 149 CYS 118 150 ASN 119 151 GLN 120 152 TYR 121 153 CYS 122 154 GLY 123 155 LEU 124 156 GLY 125 157 HIS 126 158 GLN 127 159 ASN 128 160 MET 129 161 PHE 130 162 GLY 131 163 THR 132 164 ILE 133 165 VAL 134 166 VAL 135 167 LYS 136 168 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _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 Sep 14 23:21:43 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 1 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CU _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU (COPPER (II) ION)" _BMRB_code . _PDB_code CU _Molecular_mass 63.546 _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 Sep 14 23:20:36 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 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 _Strain _ATCC_number _Gene_mnemonic $CuA 'Thermus thermophilus' 274 Bacteria . Thermus thermophilus HB8 27634 cbaB 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 $CuA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pMA10 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 $CuA 1.2 mM '[U-98% 15N]' 'potassium phosphate' 20 mM . 'potassium hexacyanoferrate (III)' 5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CuA 2.0 mM . 'potassium phosphate' 20 mM . 'potassium hexacyanoferrate (III)' 5 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Task 'data acquisition' 'data processing' stop_ _Details . save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version 2.5.9 loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-1H_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H TROSY' _Sample_label . save_ save_15N-1H_TOCSY-TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H TOCSY-TROSY' _Sample_label . save_ save_15N-1H_NOESY-TROSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H NOESY-TROSY' _Sample_label . save_ save_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CuA 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 35 3 TYR HA H 4.67 0.01 1 2 35 3 TYR HB2 H 3.02 0.01 2 3 35 3 TYR HB3 H 2.98 0.01 2 4 35 3 TYR HD1 H 7.11 0.01 1 5 35 3 TYR HD2 H 7.11 0.01 1 6 35 3 TYR HE1 H 6.80 0.01 1 7 35 3 TYR HE2 H 6.80 0.01 1 8 36 4 THR H H 8.14 0.01 1 9 36 4 THR HA H 4.30 0.01 1 10 36 4 THR HB H 4.10 0.01 1 11 36 4 THR HG2 H 1.15 0.01 1 12 37 5 LEU H H 8.19 0.01 1 13 37 5 LEU HA H 4.31 0.01 1 14 37 5 LEU HB2 H 1.60 0.01 1 15 37 5 LEU HB3 H 1.60 0.01 1 16 37 5 LEU HG H 1.61 0.01 1 17 37 5 LEU HD1 H 0.94 0.01 2 18 37 5 LEU HD2 H 0.89 0.01 2 19 38 6 ALA H H 8.34 0.01 1 20 38 6 ALA HA H 4.36 0.01 1 21 38 6 ALA HB H 1.38 0.01 1 22 39 7 THR H H 8.04 0.01 1 23 39 7 THR HA H 4.29 0.01 1 24 39 7 THR HB H 4.19 0.01 1 25 39 7 THR HG2 H 1.17 0.01 1 26 40 8 HIS H H 8.41 0.01 1 27 40 8 HIS HA H 4.76 0.01 1 28 40 8 HIS HB2 H 3.23 0.01 2 29 40 8 HIS HB3 H 3.16 0.01 2 30 41 9 THR H H 8.18 0.01 1 31 41 9 THR HA H 4.30 0.01 1 32 41 9 THR HB H 4.18 0.01 1 33 41 9 THR HG2 H 1.17 0.01 1 34 42 10 ALA H H 8.41 0.01 1 35 42 10 ALA HA H 4.38 0.01 1 36 42 10 ALA HB H 1.41 0.01 1 37 42 10 ALA N N 126.7 0.1 1 38 43 11 GLY H H 8.37 0.01 9 39 43 11 GLY HA2 H 3.93 0.01 9 40 43 11 GLY HA3 H 3.93 0.01 9 41 43 11 GLY N N 108.8 0.1 9 42 44 12 VAL H H 8.22 0.01 1 43 44 12 VAL HA H 4.12 0.01 1 44 44 12 VAL HB H 2.03 0.01 1 45 44 12 VAL HG1 H 0.91 0.01 2 46 44 12 VAL HG2 H 0.89 0.01 2 47 44 12 VAL N N 119.9 0.1 1 48 45 13 ILE H H 8.37 0.01 1 49 45 13 ILE HA H 4.48 0.01 1 50 45 13 ILE HB H 1.87 0.01 1 51 45 13 ILE HG12 H 1.52 0.01 2 52 45 13 ILE HG13 H 1.20 0.01 2 53 45 13 ILE HG2 H 0.95 0.01 1 54 45 13 ILE HD1 H 0.85 0.01 1 55 45 13 ILE N N 127.3 0.1 1 56 46 14 PRO HA H 4.40 0.01 1 57 46 14 PRO HB2 H 2.30 0.01 2 58 46 14 PRO HB3 H 1.94 0.01 2 59 46 14 PRO HG2 H 2.06 0.01 2 60 46 14 PRO HG3 H 1.98 0.01 2 61 46 14 PRO HD2 H 3.95 0.01 2 62 46 14 PRO HD3 H 3.68 0.01 2 63 47 15 ALA H H 8.39 0.01 1 64 47 15 ALA HA H 4.32 0.01 1 65 47 15 ALA HB H 1.41 0.01 1 66 47 15 ALA N N 124.6 0.1 1 67 48 16 GLY H H 8.40 0.01 1 68 48 16 GLY HA2 H 3.98 0.01 1 69 48 16 GLY HA3 H 3.98 0.01 1 70 48 16 GLY N N 108.1 0.1 1 71 49 17 LYS H H 8.19 0.01 1 72 49 17 LYS HA H 4.38 0.01 1 73 49 17 LYS HB2 H 1.87 0.01 2 74 49 17 LYS HB3 H 1.77 0.01 2 75 49 17 LYS HG2 H 1.45 0.01 2 76 49 17 LYS HG3 H 1.41 0.01 2 77 49 17 LYS HD2 H 1.69 0.01 1 78 49 17 LYS HD3 H 1.69 0.01 1 79 49 17 LYS HE2 H 3.01 0.01 1 80 49 17 LYS HE3 H 3.01 0.01 1 81 49 17 LYS N N 120.8 0.1 1 82 50 18 LEU H H 8.23 0.01 1 83 50 18 LEU HA H 4.43 0.01 1 84 50 18 LEU HB2 H 1.68 0.01 2 85 50 18 LEU HB3 H 1.64 0.01 2 86 50 18 LEU HG H 1.65 0.01 1 87 50 18 LEU HD1 H 0.97 0.01 2 88 50 18 LEU HD2 H 0.93 0.01 2 89 50 18 LEU N N 123.6 0.1 1 90 51 19 GLU H H 8.69 0.01 1 91 51 19 GLU HA H 4.43 0.01 1 92 51 19 GLU HB2 H 2.13 0.01 2 93 51 19 GLU HB3 H 2.00 0.01 2 94 51 19 GLU HG2 H 2.34 0.01 2 95 51 19 GLU HG3 H 2.20 0.01 2 96 51 19 GLU N N 124.2 0.1 1 97 52 20 ARG H H 8.23 0.01 1 98 52 20 ARG HA H 4.96 0.01 1 99 52 20 ARG HB2 H 1.88 0.01 2 100 52 20 ARG HB3 H 1.72 0.01 2 101 52 20 ARG HG2 H 1.68 0.01 2 102 52 20 ARG HG3 H 1.60 0.01 2 103 52 20 ARG HD2 H 3.23 0.01 1 104 52 20 ARG HD3 H 3.23 0.01 1 105 52 20 ARG HE H 7.34 0.01 1 106 52 20 ARG N N 123.0 0.1 1 107 52 20 ARG NE N 85.0 0.1 1 108 53 21 VAL H H 8.09 0.01 1 109 53 21 VAL HA H 4.38 0.01 1 110 53 21 VAL HB H 1.81 0.01 1 111 53 21 VAL HG1 H 0.59 0.01 1 112 53 21 VAL HG2 H 0.40 0.01 1 113 53 21 VAL N N 117.6 0.1 1 114 54 22 ASP H H 8.32 0.01 1 115 54 22 ASP HA H 4.97 0.01 1 116 54 22 ASP HB2 H 3.14 0.01 2 117 54 22 ASP HB3 H 2.49 0.01 2 118 54 22 ASP N N 123.2 0.1 1 119 55 23 PRO HA H 4.30 0.01 9 120 55 23 PRO HB2 H 2.24 0.01 9 121 55 23 PRO HB3 H 2.24 0.01 9 122 55 23 PRO HG2 H 2.06 0.01 9 123 55 23 PRO HG3 H 1.94 0.01 9 124 55 23 PRO HD2 H 4.16 0.01 9 125 55 23 PRO HD3 H 3.99 0.01 9 126 56 24 THR H H 8.43 0.01 1 127 56 24 THR HA H 4.26 0.01 1 128 56 24 THR HB H 4.27 0.01 9 129 56 24 THR HG2 H 1.30 0.01 1 130 56 24 THR N N 108.5 0.1 1 131 57 25 THR H H 7.43 0.01 1 132 57 25 THR HA H 4.74 0.01 1 133 57 25 THR HB H 4.55 0.01 1 134 57 25 THR HG2 H 1.07 0.01 1 135 57 25 THR N N 108.3 0.1 1 136 58 26 VAL H H 7.12 0.01 1 137 58 26 VAL HA H 4.21 0.01 1 138 58 26 VAL HB H 2.05 0.01 1 139 58 26 VAL HG1 H 0.77 0.01 1 140 58 26 VAL HG2 H 0.68 0.01 1 141 58 26 VAL N N 121.8 0.1 1 142 59 27 ARG H H 8.24 0.01 1 143 59 27 ARG HA H 4.26 0.01 1 144 59 27 ARG HB2 H 1.87 0.01 2 145 59 27 ARG HB3 H 1.53 0.01 2 146 59 27 ARG HG2 H 1.39 0.01 1 147 59 27 ARG HG3 H 1.39 0.01 1 148 59 27 ARG HD2 H 2.93 0.01 1 149 59 27 ARG HD3 H 2.93 0.01 1 150 59 27 ARG HE H 7.02 0.01 1 151 59 27 ARG N N 115.4 0.1 1 152 59 27 ARG NE N 84.5 0.1 1 153 60 28 GLN H H 7.78 0.01 1 154 60 28 GLN HA H 4.43 0.01 1 155 60 28 GLN HB2 H 2.08 0.01 1 156 60 28 GLN HB3 H 2.08 0.01 1 157 60 28 GLN HG2 H 2.39 0.01 2 158 60 28 GLN HG3 H 2.26 0.01 2 159 60 28 GLN N N 116.4 0.1 1 160 61 29 GLU H H 8.09 0.01 1 161 61 29 GLU HA H 4.57 0.01 1 162 61 29 GLU HB2 H 2.02 0.01 2 163 61 29 GLU HB3 H 1.92 0.01 2 164 61 29 GLU HG2 H 2.21 0.01 2 165 61 29 GLU HG3 H 2.15 0.01 2 166 61 29 GLU N N 118.2 0.1 1 167 62 30 GLY H H 8.95 0.01 1 168 62 30 GLY HA2 H 4.71 0.01 2 169 62 30 GLY HA3 H 3.81 0.01 2 170 62 30 GLY N N 113.1 0.1 1 171 63 31 PRO HA H 3.68 0.01 1 172 63 31 PRO HB2 H 0.64 0.01 2 173 63 31 PRO HB3 H -0.29 0.01 2 174 63 31 PRO HG2 H 1.28 0.01 2 175 63 31 PRO HG3 H 1.01 0.01 2 176 63 31 PRO HD2 H 3.63 0.01 2 177 63 31 PRO HD3 H 3.45 0.01 2 178 64 32 TRP H H 8.76 0.01 1 179 64 32 TRP HA H 4.32 0.01 1 180 64 32 TRP HB2 H 3.25 0.01 2 181 64 32 TRP HB3 H 2.94 0.01 2 182 64 32 TRP HD1 H 6.79 0.01 1 183 64 32 TRP HE1 H 9.59 0.01 1 184 64 32 TRP HE3 H 7.91 0.01 1 185 64 32 TRP HZ2 H 7.00 0.01 1 186 64 32 TRP HZ3 H 7.04 0.01 1 187 64 32 TRP HH2 H 7.13 0.01 1 188 64 32 TRP N N 117.3 0.1 1 189 64 32 TRP NE1 N 128.5 0.1 1 190 65 33 ALA H H 7.23 0.01 1 191 65 33 ALA HA H 3.93 0.01 1 192 65 33 ALA HB H 1.06 0.01 1 193 65 33 ALA N N 120.1 0.1 1 194 66 34 ASP H H 7.73 0.01 1 195 66 34 ASP HA H 5.22 0.01 1 196 66 34 ASP HB2 H 2.80 0.01 2 197 66 34 ASP HB3 H 2.41 0.01 2 198 66 34 ASP N N 114.6 0.1 1 199 67 35 PRO HA H 4.30 0.01 1 200 67 35 PRO HB2 H 2.23 0.01 2 201 67 35 PRO HB3 H 2.13 0.01 2 202 67 35 PRO HG2 H 2.02 0.01 1 203 67 35 PRO HG3 H 2.02 0.01 1 204 67 35 PRO HD2 H 4.11 0.01 2 205 67 35 PRO HD3 H 3.82 0.01 2 206 68 36 ALA H H 8.18 0.01 1 207 68 36 ALA HA H 4.32 0.01 1 208 68 36 ALA HB H 1.51 0.01 1 209 68 36 ALA N N 119.6 0.1 1 210 69 37 GLN H H 7.75 0.01 1 211 69 37 GLN HA H 4.71 0.01 1 212 69 37 GLN HB2 H 2.47 0.01 2 213 69 37 GLN HB3 H 1.68 0.01 2 214 69 37 GLN HG2 H 2.24 0.01 2 215 69 37 GLN HG3 H 2.13 0.01 2 216 69 37 GLN HE21 H 7.84 0.01 2 217 69 37 GLN HE22 H 6.76 0.01 2 218 69 37 GLN N N 117.0 0.1 1 219 69 37 GLN NE2 N 112.7 0.1 1 220 70 38 ALA H H 7.02 0.01 1 221 70 38 ALA HA H 4.38 0.01 1 222 70 38 ALA HB H 1.79 0.01 1 223 70 38 ALA N N 121.5 0.1 1 224 71 39 VAL H H 7.88 0.01 1 225 71 39 VAL HA H 4.71 0.01 1 226 71 39 VAL HB H 2.19 0.01 1 227 71 39 VAL HG1 H 0.90 0.01 1 228 71 39 VAL HG2 H 1.04 0.01 1 229 71 39 VAL N N 114.0 0.1 1 230 72 40 VAL H H 9.56 0.01 1 231 72 40 VAL HA H 4.43 0.01 1 232 72 40 VAL HB H 2.07 0.01 1 233 72 40 VAL HG1 H 0.92 0.01 1 234 72 40 VAL HG2 H 1.04 0.01 1 235 72 40 VAL N N 129.1 0.1 1 236 73 41 GLN H H 9.17 0.01 1 237 73 41 GLN HA H 4.15 0.01 1 238 73 41 GLN HB2 H 1.85 0.01 2 239 73 41 GLN HB3 H 1.81 0.01 2 240 73 41 GLN HG2 H 2.18 0.01 2 241 73 41 GLN HG3 H 1.99 0.01 2 242 73 41 GLN HE21 H 6.90 0.01 2 243 73 41 GLN HE22 H 6.61 0.01 2 244 73 41 GLN N N 128.8 0.1 1 245 73 41 GLN NE2 N 108.6 0.1 1 246 74 42 THR H H 8.29 0.01 1 247 74 42 THR HA H 4.39 0.01 1 248 74 42 THR HB H 4.44 0.01 1 249 74 42 THR HG2 H 1.12 0.01 1 250 74 42 THR N N 119.3 0.1 1 251 75 43 GLY H H 8.02 0.01 1 252 75 43 GLY HA2 H 4.26 0.01 2 253 75 43 GLY HA3 H 3.81 0.01 2 254 75 43 GLY N N 111.2 0.1 1 255 76 44 PRO HA H 4.17 0.01 9 256 76 44 PRO HB2 H 1.88 0.01 9 257 76 44 PRO HB3 H 1.88 0.01 9 258 76 44 PRO HG2 H 2.12 0.01 9 259 76 44 PRO HG3 H 1.97 0.01 9 260 76 44 PRO HD2 H 3.55 0.01 9 261 76 44 PRO HD3 H 3.55 0.01 9 262 77 45 ASN H H 8.67 0.01 1 263 77 45 ASN HA H 4.88 0.01 1 264 77 45 ASN HB2 H 2.97 0.01 2 265 77 45 ASN HB3 H 2.45 0.01 2 266 77 45 ASN HD21 H 7.65 0.01 2 267 77 45 ASN HD22 H 6.85 0.01 2 268 77 45 ASN N N 117.1 0.1 1 269 77 45 ASN ND2 N 111.5 0.1 1 270 78 46 GLN H H 6.98 0.01 1 271 78 46 GLN HA H 5.61 0.01 1 272 78 46 GLN HB2 H 1.74 0.01 2 273 78 46 GLN HB3 H 1.46 0.01 2 274 78 46 GLN HG2 H 2.24 0.01 1 275 78 46 GLN HG3 H 2.24 0.01 1 276 78 46 GLN HE21 H 7.88 0.01 2 277 78 46 GLN HE22 H 6.80 0.01 2 278 78 46 GLN N N 118.7 0.1 1 279 78 46 GLN NE2 N 113.5 0.1 1 280 79 47 TYR H H 8.92 0.01 1 281 79 47 TYR HA H 5.10 0.01 1 282 79 47 TYR HB2 H 2.52 0.01 1 283 79 47 TYR HB3 H 2.52 0.01 1 284 79 47 TYR HD1 H 6.65 0.01 1 285 79 47 TYR HD2 H 6.65 0.01 1 286 79 47 TYR HE1 H 6.45 0.01 9 287 79 47 TYR HE2 H 6.45 0.01 9 288 79 47 TYR N N 124.7 0.1 1 289 80 48 THR H H 9.62 0.01 1 290 80 48 THR HA H 5.11 0.01 1 291 80 48 THR HB H 3.76 0.01 1 292 80 48 THR HG2 H 0.56 0.01 1 293 80 48 THR N N 121.2 0.1 1 294 81 49 VAL H H 8.75 0.01 1 295 81 49 VAL HA H 5.10 0.01 1 296 81 49 VAL HB H 1.63 0.01 1 297 81 49 VAL HG1 H 0.80 0.01 1 298 81 49 VAL HG2 H 0.56 0.01 1 299 81 49 VAL N N 125.6 0.1 1 300 82 50 TYR H H 9.12 0.01 1 301 82 50 TYR HA H 4.66 0.01 1 302 82 50 TYR HB2 H 2.41 0.01 2 303 82 50 TYR HB3 H 1.31 0.01 2 304 82 50 TYR HD1 H 6.21 0.01 1 305 82 50 TYR HD2 H 6.21 0.01 1 306 82 50 TYR HE1 H 6.21 0.01 9 307 82 50 TYR HE2 H 6.21 0.01 9 308 82 50 TYR N N 129.6 0.1 1 309 83 51 VAL H H 8.74 0.01 1 310 83 51 VAL HA H 5.33 0.01 1 311 83 51 VAL HB H 1.93 0.01 1 312 83 51 VAL HG1 H 1.09 0.01 1 313 83 51 VAL HG2 H 1.09 0.01 1 314 83 51 VAL N N 124.1 0.1 1 315 84 52 LEU H H 9.64 0.01 1 316 84 52 LEU HA H 5.22 0.01 1 317 84 52 LEU HB2 H 1.91 0.01 2 318 84 52 LEU HB3 H 1.70 0.01 2 319 84 52 LEU HG H 1.67 0.01 9 320 84 52 LEU HD1 H 0.56 0.01 1 321 84 52 LEU HD2 H 0.56 0.01 1 322 84 52 LEU N N 128.3 0.1 1 323 85 53 ALA H H 8.69 0.01 1 324 85 53 ALA HA H 4.54 0.01 1 325 85 53 ALA HB H 1.06 0.01 1 326 85 53 ALA N N 130.5 0.1 1 327 86 54 PHE H H 7.68 0.01 1 328 86 54 PHE HA H 5.22 0.01 1 329 86 54 PHE HB2 H 2.98 0.01 2 330 86 54 PHE HB3 H 2.15 0.01 2 331 86 54 PHE HD1 H 6.57 0.01 1 332 86 54 PHE HD2 H 6.57 0.01 1 333 86 54 PHE HE1 H 7.00 0.01 1 334 86 54 PHE HE2 H 7.00 0.01 1 335 86 54 PHE HZ H 7.21 0.01 1 336 86 54 PHE N N 116.9 0.1 1 337 87 55 ALA H H 10.49 0.01 1 338 87 55 ALA HA H 3.65 0.01 1 339 87 55 ALA HB H 0.13 0.01 1 340 87 55 ALA N N 125.5 0.1 1 341 88 56 PHE H H 7.94 0.01 1 342 88 56 PHE HA H 5.39 0.01 1 343 88 56 PHE HB2 H 3.02 0.01 2 344 88 56 PHE HB3 H 2.75 0.01 2 345 88 56 PHE N N 128.4 0.1 1 346 89 57 GLY H H 8.07 0.01 1 347 89 57 GLY HA2 H 3.44 0.01 1 348 89 57 GLY HA3 H 3.44 0.01 1 349 89 57 GLY N N 113.0 0.1 1 350 90 58 TYR H H 8.19 0.01 1 351 90 58 TYR HA H 5.33 0.01 1 352 90 58 TYR HB2 H 2.75 0.01 2 353 90 58 TYR HB3 H 2.52 0.01 2 354 90 58 TYR HD1 H 6.66 0.01 1 355 90 58 TYR HD2 H 6.66 0.01 1 356 90 58 TYR HE1 H 6.29 0.01 1 357 90 58 TYR HE2 H 6.29 0.01 1 358 90 58 TYR N N 113.1 0.1 1 359 91 59 GLN H H 9.23 0.01 1 360 91 59 GLN HA H 4.83 0.01 1 361 91 59 GLN HB2 H 2.24 0.01 1 362 91 59 GLN HB3 H 2.24 0.01 1 363 91 59 GLN HG2 H 2.48 0.01 1 364 91 59 GLN HG3 H 2.48 0.01 1 365 91 59 GLN N N 121.2 0.1 1 366 92 60 PRO HA H 4.76 0.01 9 367 92 60 PRO HB2 H 2.47 0.01 9 368 92 60 PRO HB3 H 2.12 0.01 9 369 92 60 PRO HG2 H 1.99 0.01 9 370 92 60 PRO HG3 H 1.83 0.01 9 371 92 60 PRO HD2 H 4.07 0.01 9 372 92 60 PRO HD3 H 3.49 0.01 9 373 93 61 ASN H H 8.27 0.01 1 374 93 61 ASN HA H 5.12 0.01 1 375 93 61 ASN HB2 H 3.23 0.01 2 376 93 61 ASN HB3 H 3.10 0.01 2 377 93 61 ASN N N 113.2 0.1 1 378 94 62 PRO HA H 5.26 0.01 1 379 94 62 PRO HB2 H 2.23 0.01 2 380 94 62 PRO HB3 H 1.79 0.01 2 381 94 62 PRO HG2 H 1.97 0.01 2 382 94 62 PRO HG3 H 1.82 0.01 2 383 94 62 PRO HD2 H 3.70 0.01 2 384 94 62 PRO HD3 H 3.53 0.01 2 385 95 63 ILE H H 8.36 0.01 1 386 95 63 ILE HA H 4.10 0.01 1 387 95 63 ILE HB H 1.79 0.01 1 388 95 63 ILE HG2 H 0.90 0.01 1 389 95 63 ILE N N 119.9 0.1 1 390 96 64 GLU H H 8.44 0.01 1 391 96 64 GLU HA H 5.50 0.01 1 392 96 64 GLU HB2 H 1.90 0.01 2 393 96 64 GLU HB3 H 1.74 0.01 2 394 96 64 GLU HG2 H 2.07 0.01 2 395 96 64 GLU HG3 H 1.93 0.01 2 396 96 64 GLU N N 128.7 0.1 1 397 97 65 VAL H H 8.48 0.01 1 398 97 65 VAL HA H 4.66 0.01 1 399 97 65 VAL HB H 1.82 0.01 1 400 97 65 VAL HG1 H 0.61 0.01 1 401 97 65 VAL HG2 H 0.45 0.01 1 402 97 65 VAL N N 115.2 0.1 1 403 98 66 PRO HA H 4.68 0.01 1 404 98 66 PRO HB2 H 2.20 0.01 2 405 98 66 PRO HB3 H 1.76 0.01 2 406 98 66 PRO HG2 H 1.59 0.01 9 407 98 66 PRO HG3 H 1.49 0.01 9 408 98 66 PRO HD2 H 3.11 0.01 2 409 98 66 PRO HD3 H 2.72 0.01 2 410 99 67 GLN H H 8.50 0.01 1 411 99 67 GLN HA H 3.91 0.01 1 412 99 67 GLN HB2 H 1.87 0.01 1 413 99 67 GLN HB3 H 1.87 0.01 1 414 99 67 GLN HG2 H 2.38 0.01 2 415 99 67 GLN HG3 H 2.07 0.01 2 416 99 67 GLN HE21 H 7.76 0.01 2 417 99 67 GLN HE22 H 6.70 0.01 2 418 99 67 GLN N N 121.4 0.1 1 419 99 67 GLN NE2 N 109.6 0.1 1 420 100 68 GLY H H 8.74 0.01 1 421 100 68 GLY HA2 H 4.15 0.01 2 422 100 68 GLY HA3 H 3.37 0.01 2 423 100 68 GLY N N 112.2 0.1 1 424 101 69 ALA H H 7.01 0.01 1 425 101 69 ALA HA H 4.54 0.01 1 426 101 69 ALA HB H 1.34 0.01 1 427 101 69 ALA N N 122.3 0.1 1 428 102 70 GLU H H 8.27 0.01 1 429 102 70 GLU HA H 4.32 0.01 1 430 102 70 GLU HB2 H 1.86 0.01 1 431 102 70 GLU HB3 H 1.86 0.01 1 432 102 70 GLU HG2 H 2.07 0.01 2 433 102 70 GLU HG3 H 1.99 0.01 9 434 102 70 GLU N N 123.0 0.1 1 435 103 71 ILE H H 9.13 0.01 1 436 103 71 ILE HA H 4.83 0.01 1 437 103 71 ILE HB H 2.28 0.01 1 438 103 71 ILE HG12 H 2.38 0.01 2 439 103 71 ILE HG13 H 1.24 0.01 2 440 103 71 ILE HG2 H -0.05 0.01 1 441 103 71 ILE HD1 H 0.68 0.01 9 442 103 71 ILE N N 130.4 0.1 1 443 104 72 VAL H H 9.01 0.01 1 444 104 72 VAL HA H 4.38 0.01 1 445 104 72 VAL HB H 2.19 0.01 1 446 104 72 VAL HG1 H 0.66 0.01 2 447 104 72 VAL HG2 H 0.63 0.01 2 448 104 72 VAL N N 127.3 0.1 1 449 105 73 PHE H H 9.54 0.01 1 450 105 73 PHE HA H 4.99 0.01 1 451 105 73 PHE HB2 H 2.99 0.01 2 452 105 73 PHE HB3 H 2.40 0.01 2 453 105 73 PHE HD1 H 7.16 0.01 1 454 105 73 PHE HD2 H 7.16 0.01 1 455 105 73 PHE HE1 H 7.16 0.01 9 456 105 73 PHE HE2 H 7.16 0.01 9 457 105 73 PHE HZ H 7.25 0.01 9 458 105 73 PHE N N 124.8 0.1 1 459 106 74 LYS H H 8.98 0.01 1 460 106 74 LYS HA H 5.11 0.01 1 461 106 74 LYS HB2 H 1.60 0.01 2 462 106 74 LYS HB3 H 1.51 0.01 2 463 106 74 LYS HG2 H 1.10 0.01 2 464 106 74 LYS HG3 H 1.05 0.01 2 465 106 74 LYS HD2 H 1.46 0.01 1 466 106 74 LYS HD3 H 1.46 0.01 1 467 106 74 LYS HE2 H 2.88 0.01 2 468 106 74 LYS HE3 H 2.73 0.01 2 469 106 74 LYS N N 122.9 0.1 1 470 107 75 ILE H H 9.41 0.01 1 471 107 75 ILE HA H 5.78 0.01 1 472 107 75 ILE HB H 1.40 0.01 1 473 107 75 ILE HG12 H 1.23 0.01 2 474 107 75 ILE HG13 H -0.06 0.01 2 475 107 75 ILE HG2 H 0.76 0.01 1 476 107 75 ILE HD1 H -0.23 0.01 1 477 107 75 ILE N N 125.2 0.1 1 478 108 76 THR H H 8.22 0.01 1 479 108 76 THR HA H 4.59 0.01 1 480 108 76 THR HB H 3.50 0.01 1 481 108 76 THR HG1 H 5.53 0.01 1 482 108 76 THR HG2 H -0.46 0.01 1 483 108 76 THR N N 118.9 0.1 1 484 109 77 SER H H 7.14 0.01 1 485 109 77 SER HA H 6.23 0.01 1 486 109 77 SER HB2 H 3.85 0.01 2 487 109 77 SER HB3 H 3.08 0.01 2 488 109 77 SER N N 115.1 0.1 1 489 111 79 ASP H H 8.75 0.01 1 490 111 79 ASP HA H 4.77 0.01 1 491 111 79 ASP HB2 H 2.88 0.01 2 492 111 79 ASP HB3 H 2.63 0.01 2 493 111 79 ASP N N 120.5 0.1 1 494 112 80 VAL H H 11.81 0.01 1 495 112 80 VAL HA H 4.66 0.01 1 496 112 80 VAL HB H 2.42 0.01 1 497 112 80 VAL HG1 H 0.86 0.01 1 498 112 80 VAL HG2 H 0.48 0.01 1 499 112 80 VAL N N 122.0 0.1 1 500 113 81 ILE H H 7.67 0.01 1 501 113 81 ILE HA H 4.49 0.01 1 502 113 81 ILE HB H 1.57 0.01 1 503 113 81 ILE HG2 H 1.09 0.01 1 504 113 81 ILE N N 120.5 0.1 1 505 114 82 HIS H H 8.64 0.01 1 506 114 82 HIS HA H 5.16 0.01 1 507 114 82 HIS HB2 H 2.36 0.01 1 508 114 82 HIS HB3 H 2.36 0.01 1 509 114 82 HIS HD2 H 31.99 0.01 9 510 114 82 HIS HE2 H 24.47 0.01 9 511 114 82 HIS N N 120.8 0.1 1 512 116 84 PHE H H 9.21 0.01 1 513 116 84 PHE HA H 4.43 0.01 1 514 116 84 PHE HB2 H 3.09 0.01 2 515 116 84 PHE HB3 H 2.44 0.01 2 516 116 84 PHE HD1 H 6.67 0.01 1 517 116 84 PHE HD2 H 6.67 0.01 1 518 116 84 PHE HE1 H 6.29 0.01 1 519 116 84 PHE HE2 H 6.29 0.01 1 520 116 84 PHE HZ H 5.93 0.01 1 521 116 84 PHE N N 124.3 0.1 1 522 117 85 HIS H H 8.07 0.01 1 523 117 85 HIS HA H 5.46 0.01 1 524 117 85 HIS HB2 H 3.23 0.01 2 525 117 85 HIS HB3 H 3.08 0.01 2 526 117 85 HIS HD2 H 6.74 0.01 9 527 117 85 HIS N N 126.2 0.1 1 528 118 86 VAL H H 6.33 0.01 1 529 118 86 VAL HA H 4.27 0.01 1 530 118 86 VAL HB H 1.77 0.01 1 531 118 86 VAL HG1 H 0.72 0.01 1 532 118 86 VAL HG2 H 0.16 0.01 1 533 118 86 VAL N N 123.6 0.1 1 534 119 87 GLU H H 8.90 0.01 1 535 119 87 GLU HA H 3.87 0.01 1 536 119 87 GLU HB2 H 2.16 0.01 9 537 119 87 GLU HB3 H 1.98 0.01 2 538 119 87 GLU HG2 H 2.26 0.01 1 539 119 87 GLU HG3 H 2.26 0.01 1 540 119 87 GLU N N 131.1 0.1 1 541 120 88 GLY H H 9.02 0.01 1 542 120 88 GLY HA2 H 4.39 0.01 2 543 120 88 GLY HA3 H 3.84 0.01 2 544 120 88 GLY N N 111.0 0.1 1 545 121 89 THR H H 7.85 0.01 1 546 121 89 THR HA H 4.99 0.01 1 547 121 89 THR HB H 3.65 0.01 1 548 121 89 THR HG2 H 0.76 0.01 1 549 121 89 THR N N 109.4 0.1 1 550 122 90 ASN H H 7.84 0.01 1 551 122 90 ASN HA H 4.96 0.01 1 552 122 90 ASN HB2 H 3.18 0.01 2 553 122 90 ASN HB3 H 2.88 0.01 2 554 122 90 ASN HD21 H 7.63 0.01 2 555 122 90 ASN HD22 H 6.86 0.01 2 556 122 90 ASN N N 115.7 0.1 1 557 122 90 ASN ND2 N 110.4 0.1 1 558 123 91 ILE H H 8.53 0.01 1 559 123 91 ILE HA H 3.81 0.01 1 560 123 91 ILE HB H 1.49 0.01 1 561 123 91 ILE HG12 H 1.01 0.01 9 562 123 91 ILE HG13 H 0.61 0.01 9 563 123 91 ILE HG2 H 0.83 0.01 1 564 123 91 ILE HD1 H 0.19 0.01 9 565 123 91 ILE N N 121.2 0.1 1 566 124 92 ASN H H 9.13 0.01 1 567 124 92 ASN HA H 5.09 0.01 1 568 124 92 ASN HB2 H 2.93 0.01 2 569 124 92 ASN HB3 H 2.54 0.01 2 570 124 92 ASN N N 131.4 0.1 1 571 125 93 VAL H H 8.30 0.01 1 572 125 93 VAL HA H 4.76 0.01 1 573 125 93 VAL HB H 2.24 0.01 1 574 125 93 VAL HG1 H 1.00 0.01 2 575 125 93 VAL HG2 H 0.97 0.01 2 576 125 93 VAL N N 120.5 0.1 1 577 126 94 GLU H H 8.79 0.01 1 578 126 94 GLU HA H 4.70 0.01 1 579 126 94 GLU HB2 H 2.08 0.01 1 580 126 94 GLU HB3 H 2.08 0.01 1 581 126 94 GLU HG2 H 2.35 0.01 1 582 126 94 GLU HG3 H 2.35 0.01 1 583 126 94 GLU N N 126.8 0.1 1 584 127 95 VAL H H 9.02 0.01 9 585 127 95 VAL HA H 4.07 0.01 9 586 127 95 VAL HB H 1.81 0.01 9 587 127 95 VAL HG1 H 0.78 0.01 9 588 127 95 VAL HG2 H 0.68 0.01 9 589 127 95 VAL N N 124.9 0.1 9 590 128 96 LEU H H 9.19 0.01 1 591 128 96 LEU HA H 4.86 0.01 1 592 128 96 LEU HB2 H 1.50 0.01 1 593 128 96 LEU HB3 H 1.50 0.01 1 594 128 96 LEU HG H 1.62 0.01 9 595 128 96 LEU HD1 H 0.93 0.01 9 596 128 96 LEU HD2 H 0.93 0.01 9 597 128 96 LEU N N 128.1 0.1 1 598 129 97 PRO HA H 4.70 0.01 9 599 129 97 PRO HB2 H 1.76 0.01 9 600 129 97 PRO HB3 H 1.76 0.01 9 601 130 98 GLY H H 9.15 0.01 1 602 130 98 GLY HA2 H 4.24 0.01 2 603 130 98 GLY HA3 H 4.02 0.01 2 604 130 98 GLY N N 112.4 0.1 1 605 131 99 GLU H H 7.84 0.01 1 606 131 99 GLU HA H 5.05 0.01 1 607 131 99 GLU HB2 H 1.80 0.01 2 608 131 99 GLU HB3 H 1.73 0.01 2 609 131 99 GLU HG2 H 2.07 0.01 2 610 131 99 GLU HG3 H 1.95 0.01 2 611 131 99 GLU N N 117.8 0.1 1 612 132 100 VAL H H 8.85 0.01 1 613 132 100 VAL HA H 4.52 0.01 1 614 132 100 VAL HB H 2.10 0.01 1 615 132 100 VAL HG1 H 1.06 0.01 2 616 132 100 VAL HG2 H 0.88 0.01 2 617 132 100 VAL N N 126.5 0.1 1 618 133 101 SER H H 9.71 0.01 1 619 133 101 SER HA H 4.94 0.01 1 620 133 101 SER HB2 H 3.90 0.01 2 621 133 101 SER HB3 H 3.74 0.01 2 622 133 101 SER N N 127.3 0.1 1 623 134 102 THR H H 8.89 0.01 1 624 134 102 THR HA H 5.72 0.01 1 625 134 102 THR HB H 3.98 0.01 1 626 134 102 THR HG2 H 1.12 0.01 1 627 134 102 THR N N 121.8 0.1 1 628 135 103 VAL H H 8.85 0.01 1 629 135 103 VAL HA H 4.54 0.01 1 630 135 103 VAL HB H 2.11 0.01 1 631 135 103 VAL HG1 H 1.01 0.01 1 632 135 103 VAL HG2 H 1.01 0.01 1 633 135 103 VAL N N 126.1 0.1 1 634 136 104 ARG H H 8.62 0.01 1 635 136 104 ARG HA H 5.95 0.01 1 636 136 104 ARG HB2 H 1.74 0.01 2 637 136 104 ARG HB3 H 1.68 0.01 2 638 136 104 ARG HG2 H 1.59 0.01 2 639 136 104 ARG HG3 H 1.49 0.01 2 640 136 104 ARG HD2 H 3.13 0.01 1 641 136 104 ARG HD3 H 3.13 0.01 1 642 136 104 ARG HE H 7.20 0.01 1 643 136 104 ARG N N 125.6 0.1 1 644 136 104 ARG NE N 84.7 0.1 1 645 137 105 TYR H H 9.63 0.01 1 646 137 105 TYR HA H 4.38 0.01 1 647 137 105 TYR HB2 H 2.86 0.01 2 648 137 105 TYR HB3 H 2.30 0.01 2 649 137 105 TYR HD1 H 5.99 0.01 1 650 137 105 TYR HD2 H 5.99 0.01 1 651 137 105 TYR HE1 H 6.47 0.01 1 652 137 105 TYR HE2 H 6.47 0.01 1 653 137 105 TYR N N 125.7 0.1 1 654 138 106 THR H H 6.76 0.01 1 655 138 106 THR HA H 4.71 0.01 1 656 138 106 THR HB H 3.53 0.01 1 657 138 106 THR HG2 H 0.78 0.01 1 658 138 106 THR N N 120.7 0.1 1 659 139 107 PHE H H 8.95 0.01 1 660 139 107 PHE HA H 4.43 0.01 1 661 139 107 PHE HB2 H 3.14 0.01 2 662 139 107 PHE HB3 H 2.80 0.01 2 663 139 107 PHE HD1 H 7.15 0.01 1 664 139 107 PHE HD2 H 7.15 0.01 1 665 139 107 PHE HE1 H 7.15 0.01 9 666 139 107 PHE HE2 H 7.15 0.01 9 667 139 107 PHE HZ H 7.20 0.01 9 668 139 107 PHE N N 125.9 0.1 1 669 140 108 LYS H H 8.62 0.01 1 670 140 108 LYS HA H 4.43 0.01 1 671 140 108 LYS HB2 H 1.99 0.01 2 672 140 108 LYS HB3 H 1.74 0.01 2 673 140 108 LYS HG2 H 1.43 0.01 2 674 140 108 LYS HG3 H 1.32 0.01 2 675 140 108 LYS HD2 H 1.64 0.01 1 676 140 108 LYS HD3 H 1.64 0.01 1 677 140 108 LYS HE2 H 2.93 0.01 1 678 140 108 LYS HE3 H 2.93 0.01 1 679 140 108 LYS N N 122.8 0.1 1 680 141 109 ARG H H 7.84 0.01 1 681 141 109 ARG HA H 5.05 0.01 1 682 141 109 ARG HB2 H 1.96 0.01 2 683 141 109 ARG HB3 H 1.79 0.01 2 684 141 109 ARG HG2 H 1.73 0.01 1 685 141 109 ARG HG3 H 1.73 0.01 1 686 141 109 ARG HD2 H 3.30 0.01 2 687 141 109 ARG HD3 H 3.26 0.01 2 688 141 109 ARG HE H 7.24 0.01 1 689 141 109 ARG N N 117.9 0.1 1 690 141 109 ARG NE N 84.3 0.1 9 691 142 110 PRO HA H 4.39 0.01 1 692 142 110 PRO HB2 H 2.06 0.01 1 693 142 110 PRO HB3 H 2.06 0.01 1 694 142 110 PRO HG2 H 1.85 0.01 1 695 142 110 PRO HG3 H 1.85 0.01 1 696 142 110 PRO HD2 H 3.94 0.01 2 697 142 110 PRO HD3 H 3.68 0.01 2 698 143 111 GLY H H 8.68 0.01 1 699 143 111 GLY HA2 H 4.38 0.01 2 700 143 111 GLY HA3 H 3.76 0.01 2 701 143 111 GLY N N 108.1 0.1 1 702 144 112 GLU H H 8.13 0.01 1 703 144 112 GLU HA H 5.22 0.01 1 704 144 112 GLU HB2 H 1.85 0.01 1 705 144 112 GLU HB3 H 1.85 0.01 1 706 144 112 GLU HG2 H 2.24 0.01 2 707 144 112 GLU HG3 H 2.02 0.01 2 708 144 112 GLU N N 118.8 0.1 1 709 145 113 TYR H H 9.69 0.01 1 710 145 113 TYR HA H 4.71 0.01 1 711 145 113 TYR HB2 H 2.64 0.01 2 712 145 113 TYR HB3 H 2.60 0.01 2 713 145 113 TYR HD1 H 7.11 0.01 1 714 145 113 TYR HD2 H 7.11 0.01 1 715 145 113 TYR HE1 H 6.64 0.01 1 716 145 113 TYR HE2 H 6.64 0.01 1 717 145 113 TYR N N 125.2 0.1 1 718 146 114 ARG H H 8.95 0.01 1 719 146 114 ARG HA H 4.66 0.01 1 720 146 114 ARG HB2 H 1.64 0.01 1 721 146 114 ARG HB3 H 1.64 0.01 1 722 146 114 ARG HG2 H 1.79 0.01 2 723 146 114 ARG HG3 H 1.47 0.01 2 724 146 114 ARG HD2 H 2.97 0.01 2 725 146 114 ARG HD3 H 2.91 0.01 2 726 146 114 ARG HE H 7.00 0.01 1 727 146 114 ARG N N 123.4 0.1 1 728 146 114 ARG NE N 83.7 0.1 1 729 147 115 ILE H H 8.30 0.01 1 730 147 115 ILE HA H 4.33 0.01 1 731 147 115 ILE HB H 0.58 0.01 1 732 147 115 ILE HG12 H 1.14 0.01 9 733 147 115 ILE HG13 H -0.03 0.01 9 734 147 115 ILE HG2 H -0.58 0.01 1 735 147 115 ILE HD1 H 0.32 0.01 9 736 147 115 ILE N N 123.7 0.1 1 737 148 116 ILE H H 8.78 0.01 1 738 148 116 ILE HA H 5.09 0.01 1 739 148 116 ILE HB H 1.00 0.01 9 740 148 116 ILE N N 119.8 0.1 1 741 154 122 GLY H H 7.14 0.01 9 742 154 122 GLY HA2 H 5.20 0.01 9 743 154 122 GLY HA3 H 4.38 0.01 9 744 154 122 GLY N N 104.4 0.1 9 745 155 123 LEU H H 7.85 0.01 9 746 155 123 LEU HA H 4.95 0.01 9 747 155 123 LEU HB2 H 3.59 0.01 9 748 155 123 LEU HB3 H 3.59 0.01 9 749 155 123 LEU HG H 1.48 0.01 9 750 155 123 LEU HD1 H 0.79 0.01 9 751 155 123 LEU HD2 H 0.75 0.01 9 752 155 123 LEU N N 109.4 0.1 9 753 156 124 GLY H H 5.70 0.01 1 754 156 124 GLY HA2 H 3.72 0.01 9 755 156 124 GLY HA3 H 0.91 0.01 9 756 156 124 GLY N N 105.3 0.1 1 757 157 125 HIS H H 8.51 0.01 9 758 157 125 HIS HA H 4.55 0.01 9 759 157 125 HIS HB2 H 3.96 0.01 9 760 157 125 HIS HB3 H 1.65 0.01 9 761 157 125 HIS N N 117.6 0.1 9 762 158 126 GLN H H 8.51 0.01 1 763 158 126 GLN HA H 4.17 0.01 1 764 158 126 GLN HB2 H 1.72 0.01 1 765 158 126 GLN HB3 H 1.72 0.01 1 766 158 126 GLN HG2 H 2.17 0.01 2 767 158 126 GLN HG3 H 1.96 0.01 2 768 158 126 GLN N N 122.3 0.1 1 769 159 127 ASN H H 8.44 0.01 1 770 159 127 ASN HA H 4.66 0.01 1 771 159 127 ASN HB2 H 2.80 0.01 1 772 159 127 ASN HB3 H 2.80 0.01 1 773 159 127 ASN N N 117.7 0.1 1 774 160 128 MET H H 7.49 0.01 1 775 160 128 MET HA H 4.38 0.01 1 776 160 128 MET HB2 H 2.15 0.01 2 777 160 128 MET HB3 H 1.74 0.01 2 778 160 128 MET HG2 H 2.48 0.01 2 779 160 128 MET HG3 H 1.38 0.01 2 780 160 128 MET HE H 1.42 0.01 9 781 160 128 MET N N 120.7 0.1 1 782 161 129 PHE H H 8.19 0.01 1 783 161 129 PHE HA H 5.72 0.01 1 784 161 129 PHE HB2 H 3.31 0.01 2 785 161 129 PHE HB3 H 3.14 0.01 2 786 161 129 PHE HD1 H 7.34 0.01 1 787 161 129 PHE HD2 H 7.34 0.01 1 788 161 129 PHE HE1 H 7.44 0.01 1 789 161 129 PHE HE2 H 7.44 0.01 1 790 161 129 PHE HZ H 7.41 0.01 1 791 161 129 PHE N N 121.3 0.1 1 792 162 130 GLY H H 9.19 0.01 1 793 162 130 GLY HA2 H 4.72 0.01 2 794 162 130 GLY HA3 H 3.66 0.01 2 795 162 130 GLY N N 110.2 0.1 1 796 163 131 THR H H 8.05 0.01 1 797 163 131 THR HA H 5.11 0.01 1 798 163 131 THR HB H 3.81 0.01 1 799 163 131 THR HG2 H 1.18 0.01 1 800 163 131 THR N N 115.3 0.1 1 801 164 132 ILE H H 9.19 0.01 1 802 164 132 ILE HA H 4.88 0.01 1 803 164 132 ILE HB H 1.57 0.01 1 804 164 132 ILE HG2 H 0.38 0.01 1 805 164 132 ILE N N 126.7 0.1 1 806 165 133 VAL H H 9.62 0.01 1 807 165 133 VAL HA H 4.42 0.01 1 808 165 133 VAL HB H 1.91 0.01 1 809 165 133 VAL HG1 H 0.90 0.01 2 810 165 133 VAL HG2 H 0.82 0.01 2 811 165 133 VAL N N 129.4 0.1 1 812 166 134 VAL H H 9.07 0.01 1 813 166 134 VAL HA H 4.71 0.01 1 814 166 134 VAL HB H 2.24 0.01 1 815 166 134 VAL HG1 H 0.17 0.01 1 816 166 134 VAL HG2 H 0.73 0.01 1 817 166 134 VAL N N 128.2 0.1 1 818 167 135 LYS H H 8.88 0.01 1 819 167 135 LYS HA H 4.38 0.01 1 820 167 135 LYS HB2 H 1.85 0.01 2 821 167 135 LYS HB3 H 1.62 0.01 2 822 167 135 LYS HG2 H 1.34 0.01 1 823 167 135 LYS HG3 H 1.34 0.01 1 824 167 135 LYS HD2 H 1.55 0.01 1 825 167 135 LYS HD3 H 1.55 0.01 1 826 167 135 LYS HE2 H 2.83 0.01 2 827 167 135 LYS HE3 H 2.79 0.01 2 828 167 135 LYS N N 129.4 0.1 1 829 168 136 GLU H H 8.39 0.01 1 830 168 136 GLU HA H 4.03 0.01 1 831 168 136 GLU HB2 H 1.91 0.01 1 832 168 136 GLU HB3 H 1.91 0.01 1 833 168 136 GLU HG2 H 2.24 0.01 1 834 168 136 GLU HG3 H 2.24 0.01 1 835 168 136 GLU N N 126.9 0.1 1 stop_ save_