data_17432 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of murine myristoylated msrA ; _BMRB_accession_number 17432 _BMRB_flat_file_name bmr17432.str _Entry_type original _Submission_date 2011-01-27 _Accession_date 2011-01-27 _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 Gruschus James M. . 2 Lim Jungchae . . 3 Piszczek Grzegorz . . 4 Levine Rodney L. . 5 Tjandra Nico . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 421 "13C chemical shifts" 393 "15N chemical shifts" 196 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-08-08 update BMRB 'update entry citation' 2012-01-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22661718 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lim 'Jung Chae' . . 2 Gruschus James M. . 3 Ghesquiere Bart . . 4 Kim Geumsoo . . 5 Piszczek Grzegorz . . 6 Tjandra Nico . . 7 Levine Rodney L. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 287 _Journal_issue 30 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 25589 _Page_last 25595 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Myristoylated msrA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label msrA $msrA 'MYRISTIC ACID' $MYR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_msrA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common msrA _Molecular_mass 23679.752 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 212 _Mol_residue_sequence ; GDSASKVISAEEALPGRTEP IPVTAKHHVSGNRTVEPFPE GTQMAVFGMGCFWGAERKFW VLKGVYSTQVGFAGGHTRNP TYKEVCSEKTGHAEVVRVVY RPEHISFEELLKVFWENHDP TQGMRQGNDFGTQYRSAVYP TSAVQMEAALRSKEEYQKVL SKHNFGPITTDIREGQVFYY AEDYHQQYLSKNPDGYCGLG GTGVSCPMAIKK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 SER 4 ALA 5 SER 6 LYS 7 VAL 8 ILE 9 SER 10 ALA 11 GLU 12 GLU 13 ALA 14 LEU 15 PRO 16 GLY 17 ARG 18 THR 19 GLU 20 PRO 21 ILE 22 PRO 23 VAL 24 THR 25 ALA 26 LYS 27 HIS 28 HIS 29 VAL 30 SER 31 GLY 32 ASN 33 ARG 34 THR 35 VAL 36 GLU 37 PRO 38 PHE 39 PRO 40 GLU 41 GLY 42 THR 43 GLN 44 MET 45 ALA 46 VAL 47 PHE 48 GLY 49 MET 50 GLY 51 CYS 52 PHE 53 TRP 54 GLY 55 ALA 56 GLU 57 ARG 58 LYS 59 PHE 60 TRP 61 VAL 62 LEU 63 LYS 64 GLY 65 VAL 66 TYR 67 SER 68 THR 69 GLN 70 VAL 71 GLY 72 PHE 73 ALA 74 GLY 75 GLY 76 HIS 77 THR 78 ARG 79 ASN 80 PRO 81 THR 82 TYR 83 LYS 84 GLU 85 VAL 86 CYS 87 SER 88 GLU 89 LYS 90 THR 91 GLY 92 HIS 93 ALA 94 GLU 95 VAL 96 VAL 97 ARG 98 VAL 99 VAL 100 TYR 101 ARG 102 PRO 103 GLU 104 HIS 105 ILE 106 SER 107 PHE 108 GLU 109 GLU 110 LEU 111 LEU 112 LYS 113 VAL 114 PHE 115 TRP 116 GLU 117 ASN 118 HIS 119 ASP 120 PRO 121 THR 122 GLN 123 GLY 124 MET 125 ARG 126 GLN 127 GLY 128 ASN 129 ASP 130 PHE 131 GLY 132 THR 133 GLN 134 TYR 135 ARG 136 SER 137 ALA 138 VAL 139 TYR 140 PRO 141 THR 142 SER 143 ALA 144 VAL 145 GLN 146 MET 147 GLU 148 ALA 149 ALA 150 LEU 151 ARG 152 SER 153 LYS 154 GLU 155 GLU 156 TYR 157 GLN 158 LYS 159 VAL 160 LEU 161 SER 162 LYS 163 HIS 164 ASN 165 PHE 166 GLY 167 PRO 168 ILE 169 THR 170 THR 171 ASP 172 ILE 173 ARG 174 GLU 175 GLY 176 GLN 177 VAL 178 PHE 179 TYR 180 TYR 181 ALA 182 GLU 183 ASP 184 TYR 185 HIS 186 GLN 187 GLN 188 TYR 189 LEU 190 SER 191 LYS 192 ASN 193 PRO 194 ASP 195 GLY 196 TYR 197 CYS 198 GLY 199 LEU 200 GLY 201 GLY 202 THR 203 GLY 204 VAL 205 SER 206 CYS 207 PRO 208 MET 209 ALA 210 ILE 211 LYS 212 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-26 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 2L90 "Solution Structure Of Murine Myristoylated Msra" 100.00 212 100.00 100.00 1.63e-156 DBJ BAB22035 "unnamed protein product [Mus musculus]" 100.00 233 99.53 99.53 4.45e-156 DBJ BAB26522 "unnamed protein product [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 DBJ BAC33889 "unnamed protein product [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 GB AAH89311 "Methionine sulfoxide reductase A [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 GB EDL36048 "methionine sulfoxide reductase A, isoform CRA_c [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 REF NP_001240641 "mitochondrial peptide methionine sulfoxide reductase isoform 1 [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 REF NP_001240645 "mitochondrial peptide methionine sulfoxide reductase isoform 4 [Mus musculus]" 88.68 191 100.00 100.00 1.65e-138 REF NP_080598 "mitochondrial peptide methionine sulfoxide reductase isoform 1 [Mus musculus]" 100.00 233 100.00 100.00 1.89e-157 REF XP_006518492 "PREDICTED: mitochondrial peptide methionine sulfoxide reductase isoform X3 [Mus musculus]" 79.72 169 100.00 100.00 3.36e-123 REF XP_011243223 "PREDICTED: mitochondrial peptide methionine sulfoxide reductase isoform X4 [Mus musculus]" 88.68 196 100.00 100.00 1.25e-138 SP Q9D6Y7 "RecName: Full=Mitochondrial peptide methionine sulfoxide reductase; AltName: Full=Peptide-methionine (S)-S-oxide reductase; Sho" 100.00 233 100.00 100.00 1.89e-157 stop_ save_ ############# # Ligands # ############# save_MYR _Saveframe_category ligand _Mol_type non-polymer _Name_common "MYR (MYRISTIC ACID)" _BMRB_code . _PDB_code MYR _Molecular_mass 228.371 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Feb 10 14:19:04 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? HO2 HO2 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H121 H121 H . 0 . ? H122 H122 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H143 H143 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 C7 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING C8 C9 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C9 C10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C11 C12 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C12 C13 ? ? SING C12 H121 ? ? SING C12 H122 ? ? SING C13 C14 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C14 H143 ? ? stop_ _Mol_thiol_state 'not present' _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 $msrA 'house mouse' 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $msrA 'recombinant technology' . . . . pET17b $MYR 'chemical synthesis' . . . . . 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 $msrA 0.3 mM '[U-98% 13C; U-98% 15N]' DTT 5 mM 'natural abundance' TRIS 50 mM 'natural abundance' EDTA 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 300 . K pH 7.0 . pH pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 TSP H 1 'methyl protons' ppm 0 external direct . . . 1.0 TSP C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 TSP N 15 'methyl protons' ppm 0 external 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC aliphatic' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name msrA _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 2 2 ASP CA C 54.8 0.2 1 2 2 2 ASP CB C 40.6 0.2 1 3 3 3 SER H H 8.25 0.02 1 4 3 3 SER CA C 60.567 0.2 1 5 3 3 SER CB C 63.7 0.2 1 6 3 3 SER N N 115.52 0.1 1 7 4 4 ALA H H 8.2 0.02 1 8 4 4 ALA HA H 4.1 0.02 1 9 4 4 ALA CA C 54.322 0.2 1 10 4 4 ALA CB C 18.692 0.2 1 11 4 4 ALA N N 123.5 0.1 1 12 5 5 SER H H 7.92 0.02 1 13 5 5 SER HA H 4.35 0.02 1 14 5 5 SER CA C 59.255 0.2 1 15 5 5 SER CB C 63.333 0.2 1 16 5 5 SER N N 112.06 0.1 1 17 6 6 LYS H H 7.85 0.02 1 18 6 6 LYS HA H 4.29 0.02 1 19 6 6 LYS CA C 56.065 0.2 1 20 6 6 LYS CB C 33.179 0.2 1 21 6 6 LYS N N 120.17 0.1 1 22 7 7 VAL H H 7.7 0.02 1 23 7 7 VAL HA H 4.06 0.02 1 24 7 7 VAL CA C 62.63 0.2 1 25 7 7 VAL CB C 32.081 0.2 1 26 7 7 VAL N N 119.88 0.1 1 27 8 8 ILE H H 7.73 0.02 1 28 8 8 ILE HA H 3.94 0.02 1 29 8 8 ILE CA C 61.435 0.2 1 30 8 8 ILE CB C 39.159 0.2 1 31 8 8 ILE N N 127.46 0.1 1 32 9 9 SER H H 8.04 0.02 1 33 9 9 SER HA H 4.29 0.02 1 34 9 9 SER CA C 57.503 0.2 1 35 9 9 SER CB C 65 0.2 1 36 9 9 SER N N 120.31 0.1 1 37 10 10 ALA H H 8.36 0.02 1 38 10 10 ALA HA H 2.67 0.02 1 39 10 10 ALA CA C 54.322 0.2 1 40 10 10 ALA CB C 18.261 0.2 1 41 10 10 ALA N N 123.19 0.1 1 42 11 11 GLU H H 8.38 0.02 1 43 11 11 GLU HA H 3.9 0.02 1 44 11 11 GLU CA C 59.004 0.2 1 45 11 11 GLU CB C 29 0.2 1 46 11 11 GLU N N 114.46 0.1 1 47 12 12 GLU H H 7.1 0.02 1 48 12 12 GLU HA H 4.22 0.02 1 49 12 12 GLU CA C 55.608 0.2 1 50 12 12 GLU CB C 31.208 0.2 1 51 12 12 GLU N N 116.68 0.1 1 52 13 13 ALA H H 7 0.02 1 53 13 13 ALA HA H 4.33 0.02 1 54 13 13 ALA CA C 51.272 0.2 1 55 13 13 ALA CB C 20.246 0.2 1 56 13 13 ALA N N 121.31 0.1 1 57 14 14 LEU H H 7.65 0.02 1 58 14 14 LEU HA H 4.33 0.02 1 59 14 14 LEU CA C 53.179 0.2 1 60 14 14 LEU CB C 40.496 0.2 1 61 14 14 LEU N N 119.75 0.1 1 62 15 15 PRO HA H 4.39 0.02 1 63 16 16 GLY H H 8.44 0.02 1 64 16 16 GLY HA2 H 4.39 0.02 2 65 16 16 GLY HA3 H 3.44 0.02 2 66 16 16 GLY CA C 45.078 0.2 1 67 16 16 GLY N N 109.28 0.1 1 68 17 17 ARG H H 7.89 0.02 1 69 17 17 ARG HA H 4.89 0.02 1 70 17 17 ARG CA C 54.689 0.2 1 71 17 17 ARG CB C 29.414 0.2 1 72 17 17 ARG N N 117.65 0.1 1 73 18 18 THR H H 8.52 0.02 1 74 18 18 THR HA H 3.97 0.02 1 75 18 18 THR CA C 63.508 0.2 1 76 18 18 THR CB C 69.008 0.2 1 77 18 18 THR N N 112.5 0.1 1 78 19 19 GLU H H 7.72 0.02 1 79 19 19 GLU HA H 4.6 0.02 1 80 19 19 GLU CA C 53.351 0.2 1 81 19 19 GLU CB C 29.749 0.2 1 82 19 19 GLU N N 123.76 0.1 1 83 20 20 PRO HA H 4.46 0.02 1 84 20 20 PRO CA C 61.112 0.2 1 85 20 20 PRO CB C 32.632 0.2 1 86 21 21 ILE H H 8.59 0.02 1 87 21 21 ILE HA H 4.2 0.02 1 88 21 21 ILE CA C 58.71 0.2 1 89 21 21 ILE CB C 38.419 0.2 1 90 21 21 ILE N N 125.25 0.1 1 91 22 22 PRO HA H 4.54 0.02 1 92 22 22 PRO CA C 62.078 0.2 1 93 22 22 PRO CB C 32.107 0.2 1 94 23 23 VAL H H 7.75 0.02 1 95 23 23 VAL HA H 4.5 0.02 1 96 23 23 VAL CA C 59.32 0.2 1 97 23 23 VAL CB C 32.174 0.2 1 98 23 23 VAL N N 113.811 0.1 1 99 24 24 THR H H 8.82 0.02 1 100 24 24 THR HA H 4.09 0.02 1 101 24 24 THR CA C 63.754 0.2 1 102 24 24 THR CB C 68.397 0.2 1 103 24 24 THR N N 119.85 0.1 1 104 25 25 ALA H H 8.34 0.02 1 105 25 25 ALA HA H 4.22 0.02 1 106 25 25 ALA CA C 54.102 0.2 1 107 25 25 ALA CB C 19.705 0.2 1 108 25 25 ALA N N 124.73 0.1 1 109 26 26 LYS H H 6.87 0.02 1 110 26 26 LYS HA H 4.81 0.02 1 111 26 26 LYS CA C 54.21 0.2 1 112 26 26 LYS CB C 35.807 0.2 1 113 26 26 LYS N N 116.3 0.1 1 114 27 27 HIS H H 9.47 0.02 1 115 27 27 HIS HA H 3.93 0.02 1 116 27 27 HIS CA C 58.414 0.2 1 117 27 27 HIS CB C 35.941 0.2 1 118 27 27 HIS N N 127.22 0.1 1 119 28 28 HIS H H 9.03 0.02 1 120 28 28 HIS HA H 3.91 0.02 1 121 28 28 HIS CA C 61.657 0.2 1 122 28 28 HIS CB C 33.648 0.2 1 123 28 28 HIS N N 128.9 0.1 1 124 29 29 VAL H H 8.09 0.02 1 125 29 29 VAL HA H 3.61 0.02 1 126 29 29 VAL CA C 63.919 0.2 1 127 29 29 VAL CB C 32.358 0.2 1 128 29 29 VAL N N 114.64 0.1 1 129 30 30 SER H H 8.32 0.02 1 130 30 30 SER HA H 4.23 0.02 1 131 30 30 SER CA C 58.461 0.2 1 132 30 30 SER CB C 65.451 0.2 1 133 30 30 SER N N 112.04 0.1 1 134 31 31 GLY H H 7.86 0.02 1 135 31 31 GLY HA2 H 4.24 0.02 2 136 31 31 GLY HA3 H 3.75 0.02 2 137 31 31 GLY CA C 45.77 0.2 1 138 31 31 GLY N N 109.7 0.1 1 139 32 32 ASN H H 7.58 0.02 1 140 32 32 ASN HA H 4.71 0.02 1 141 32 32 ASN CA C 52.027 0.2 1 142 32 32 ASN CB C 37.241 0.2 1 143 32 32 ASN N N 118.75 0.1 1 144 33 33 ARG H H 8.04 0.02 1 145 33 33 ARG HA H 4.7 0.02 1 146 33 33 ARG CA C 50.423 0.2 1 147 33 33 ARG CB C 31.614 0.2 1 148 33 33 ARG N N 117.16 0.1 1 149 34 34 THR H H 8.24 0.02 1 150 34 34 THR HA H 4.47 0.02 1 151 34 34 THR CA C 60.839 0.2 1 152 34 34 THR N N 109.318 0.1 1 153 35 35 VAL H H 6.99 0.02 1 154 35 35 VAL HA H 4.25 0.02 1 155 35 35 VAL CA C 58.6 0.2 1 156 35 35 VAL CB C 35.72 0.2 1 157 35 35 VAL N N 116.46 0.1 1 158 36 36 GLU H H 8.22 0.02 1 159 36 36 GLU HA H 3.02 0.02 1 160 36 36 GLU CA C 55.381 0.2 1 161 36 36 GLU CB C 28.652 0.2 1 162 36 36 GLU N N 120.91 0.1 1 163 37 37 PRO HA H 4.47 0.02 1 164 37 37 PRO CA C 61.343 0.2 1 165 37 37 PRO CB C 33.891 0.2 1 166 38 38 PHE H H 8.71 0.02 1 167 38 38 PHE HA H 4.61 0.02 1 168 38 38 PHE CA C 56.51 0.2 1 169 38 38 PHE CB C 37.373 0.2 1 170 38 38 PHE N N 123.87 0.1 1 171 39 39 PRO HA H 4.17 0.02 1 172 39 39 PRO CA C 63.408 0.2 1 173 39 39 PRO CB C 31.698 0.2 1 174 40 40 GLU H H 8.78 0.02 1 175 40 40 GLU HA H 4.02 0.02 1 176 40 40 GLU CA C 57.916 0.2 1 177 40 40 GLU CB C 29.321 0.2 1 178 40 40 GLU N N 124.58 0.1 1 179 41 41 GLY H H 8.8 0.02 1 180 41 41 GLY HA2 H 4.26 0.02 2 181 41 41 GLY CA C 45.141 0.2 1 182 41 41 GLY N N 112.3 0.1 1 183 42 42 THR H H 7.4 0.02 1 184 42 42 THR HA H 4.6 0.02 1 185 42 42 THR CA C 60.257 0.2 1 186 42 42 THR CB C 71.761 0.2 1 187 42 42 THR N N 107.87 0.1 1 188 43 43 GLN H H 8.35 0.02 1 189 43 43 GLN HA H 4.34 0.02 1 190 43 43 GLN CA C 53.427 0.2 1 191 43 43 GLN CB C 32.787 0.2 1 192 43 43 GLN N N 118.88 0.1 1 193 44 44 MET H H 8.29 0.02 1 194 44 44 MET HA H 5.59 0.02 1 195 44 44 MET CA C 53.959 0.2 1 196 44 44 MET CB C 36.822 0.2 1 197 44 44 MET N N 115.81 0.1 1 198 45 45 ALA H H 9.08 0.02 1 199 45 45 ALA HA H 4.84 0.02 1 200 45 45 ALA CA C 49.81 0.2 1 201 45 45 ALA CB C 23.76 0.2 1 202 45 45 ALA N N 125.78 0.1 1 203 46 46 VAL H H 7.81 0.02 1 204 46 46 VAL HA H 4.67 0.02 1 205 46 46 VAL CA C 61.414 0.2 1 206 46 46 VAL CB C 33.375 0.2 1 207 46 46 VAL N N 121.21 0.1 1 208 47 47 PHE H H 8.48 0.02 1 209 47 47 PHE HA H 4.91 0.02 1 210 47 47 PHE CA C 54.948 0.2 1 211 47 47 PHE CB C 44.086 0.2 1 212 47 47 PHE N N 123.15 0.1 1 213 48 48 GLY H H 9.92 0.02 1 214 48 48 GLY HA2 H 5.12 0.02 2 215 48 48 GLY HA3 H 3.41 0.02 2 216 48 48 GLY CA C 45.888 0.2 1 217 48 48 GLY N N 110.503 0.1 1 218 49 49 MET H H 9.46 0.02 1 219 49 49 MET HA H 3.91 0.02 1 220 49 49 MET CA C 53.6 0.2 1 221 49 49 MET CB C 36.4 0.2 1 222 49 49 MET N N 125.4 0.1 1 223 50 50 GLY H H 9.77 0.02 1 224 50 50 GLY HA2 H 4.41 0.02 2 225 50 50 GLY HA3 H 3.78 0.02 2 226 50 50 GLY CA C 43.548 0.2 1 227 50 50 GLY N N 111.3 0.1 1 228 51 51 CYS H H 8.91 0.02 1 229 51 51 CYS HA H 4.38 0.02 1 230 51 51 CYS CA C 59.243 0.2 1 231 51 51 CYS CB C 26.60 0.2 1 232 51 51 CYS N N 124.54 0.1 1 233 52 52 PHE H H 8.54 0.02 1 234 52 52 PHE HA H 4.6 0.02 1 235 52 52 PHE CA C 57.1 0.2 1 236 52 52 PHE CB C 39.3 0.2 1 237 52 52 PHE N N 126.6 0.1 1 238 53 53 TRP H H 8.11 0.02 1 239 53 53 TRP HA H 5.66 0.02 1 240 53 53 TRP CA C 57.218 0.2 1 241 53 53 TRP CB C 29.37 0.2 1 242 53 53 TRP N N 123.42 0.1 1 243 54 54 GLY H H 8.19 0.02 1 244 54 54 GLY HA2 H 4.05 0.02 2 245 54 54 GLY HA3 H 3.78 0.02 2 246 54 54 GLY CA C 46.58 0.2 1 247 54 54 GLY N N 105.146 0.1 1 248 55 55 ALA H H 6.89 0.02 1 249 55 55 ALA HA H 3.91 0.02 1 250 55 55 ALA CA C 54.896 0.2 1 251 55 55 ALA CB C 20.71 0.2 1 252 55 55 ALA N N 121.94 0.1 1 253 56 56 GLU H H 8.41 0.02 1 254 56 56 GLU HA H 3.88 0.02 1 255 56 56 GLU CA C 60.674 0.2 1 256 56 56 GLU CB C 32.917 0.2 1 257 56 56 GLU N N 118.14 0.1 1 258 57 57 ARG H H 6.35 0.02 1 259 57 57 ARG HA H 4.75 0.02 1 260 57 57 ARG CA C 56.539 0.2 1 261 57 57 ARG CB C 31.188 0.2 1 262 57 57 ARG N N 115.46 0.1 1 263 58 58 LYS H H 6.88 0.02 1 264 58 58 LYS HA H 3.57 0.02 1 265 58 58 LYS CA C 56.14 0.2 1 266 58 58 LYS CB C 30.842 0.2 1 267 58 58 LYS N N 114.07 0.1 1 268 59 59 PHE H H 7.04 0.02 1 269 59 59 PHE HA H 4.6 0.02 1 270 59 59 PHE CA C 59.509 0.2 1 271 59 59 PHE CB C 42.287 0.2 1 272 59 59 PHE N N 109.18 0.1 1 273 60 60 TRP H H 7.94 0.02 1 274 60 60 TRP HA H 4.57 0.02 1 275 60 60 TRP CA C 60.4 0.2 1 276 60 60 TRP CB C 25.15 0.2 1 277 60 60 TRP N N 115.3 0.1 1 278 61 61 VAL H H 6.5 0.02 1 279 61 61 VAL HA H 4.42 0.02 1 280 61 61 VAL CA C 61.228 0.2 1 281 61 61 VAL CB C 31.871 0.2 1 282 61 61 VAL N N 110.81 0.1 1 283 62 62 LEU H H 7.18 0.02 1 284 62 62 LEU HA H 4.21 0.02 1 285 62 62 LEU CA C 54.541 0.2 1 286 62 62 LEU CB C 41.866 0.2 1 287 62 62 LEU N N 122.07 0.1 1 288 63 63 LYS H H 8.62 0.02 1 289 63 63 LYS HA H 4.07 0.02 1 290 63 63 LYS CA C 57.563 0.2 1 291 63 63 LYS CB C 31.376 0.2 1 292 63 63 LYS N N 125.89 0.1 1 293 64 64 GLY H H 8.62 0.02 1 294 64 64 GLY HA2 H 4.38 0.02 2 295 64 64 GLY HA3 H 3.7 0.02 2 296 64 64 GLY CA C 46.083 0.2 1 297 64 64 GLY N N 111.17 0.1 1 298 65 65 VAL H H 7.55 0.02 1 299 65 65 VAL HA H 3.93 0.02 1 300 65 65 VAL CA C 64.146 0.2 1 301 65 65 VAL CB C 31.521 0.2 1 302 65 65 VAL N N 120.89 0.1 1 303 66 66 TYR H H 9.53 0.02 1 304 66 66 TYR HA H 4.34 0.02 1 305 66 66 TYR CA C 59.9 0.2 1 306 66 66 TYR CB C 39.5 0.2 1 307 66 66 TYR N N 131.3 0.1 1 308 67 67 SER H H 8.21 0.02 1 309 67 67 SER HA H 4.39 0.02 1 310 67 67 SER CA C 56.685 0.2 1 311 67 67 SER CB C 64.808 0.2 1 312 67 67 SER N N 110.48 0.1 1 313 68 68 THR H H 7 0.02 1 314 68 68 THR HA H 5.6 0.02 1 315 68 68 THR CA C 59.839 0.2 1 316 68 68 THR CB C 71.551 0.2 1 317 68 68 THR N N 111.27 0.1 1 318 69 69 GLN H H 8.83 0.02 1 319 69 69 GLN HA H 4.97 0.02 1 320 69 69 GLN CA C 55.328 0.2 1 321 69 69 GLN CB C 33.823 0.2 1 322 69 69 GLN N N 115.27 0.1 1 323 70 70 VAL H H 9.36 0.02 1 324 70 70 VAL HA H 5.58 0.02 1 325 70 70 VAL CA C 58.585 0.2 1 326 70 70 VAL CB C 34.65 0.2 1 327 70 70 VAL N N 111.08 0.1 1 328 71 71 GLY H H 8.77 0.02 1 329 71 71 GLY HA2 H 3.79 0.02 2 330 71 71 GLY HA3 H 2.91 0.02 2 331 71 71 GLY CA C 46.618 0.2 1 332 71 71 GLY N N 111.44 0.1 1 333 72 72 PHE H H 9.09 0.02 1 334 72 72 PHE HA H 5.99 0.02 1 335 72 72 PHE CA C 53.168 0.2 1 336 72 72 PHE CB C 42.3 0.2 1 337 72 72 PHE N N 123.337 0.1 1 338 73 73 ALA H H 8.85 0.02 1 339 73 73 ALA HA H 4.97 0.02 1 340 73 73 ALA CA C 52.28 0.2 1 341 73 73 ALA CB C 23.796 0.2 1 342 73 73 ALA N N 121.62 0.1 1 343 74 74 GLY H H 9.35 0.02 1 344 74 74 GLY HA2 H 4.4 0.02 2 345 74 74 GLY HA3 H 3.56 0.02 2 346 74 74 GLY CA C 44.084 0.2 1 347 74 74 GLY N N 106.22 0.1 1 348 75 75 GLY H H 9 0.02 1 349 75 75 GLY HA2 H 3.59 0.02 2 350 75 75 GLY HA3 H 1.92 0.02 2 351 75 75 GLY CA C 41.08 0.2 1 352 75 75 GLY N N 112.82 0.1 1 353 76 76 HIS H H 7.68 0.02 1 354 76 76 HIS HA H 4.62 0.02 1 355 76 76 HIS CA C 56.545 0.2 1 356 76 76 HIS CB C 33.799 0.2 1 357 76 76 HIS N N 118.09 0.1 1 358 77 77 THR H H 6.54 0.02 1 359 77 77 THR HA H 3.75 0.02 1 360 77 77 THR CA C 64.128 0.2 1 361 77 77 THR CB C 71.778 0.2 1 362 77 77 THR N N 114.25 0.1 1 363 78 78 ARG H H 8.44 0.02 1 364 78 78 ARG HA H 3.75 0.02 1 365 78 78 ARG CA C 56.835 0.2 1 366 78 78 ARG CB C 30.776 0.2 1 367 78 78 ARG N N 129.36 0.1 1 368 80 80 PRO HA H 4.38 0.02 1 369 80 80 PRO CA C 61.96 0.2 1 370 80 80 PRO CB C 33 0.2 1 371 81 81 THR H H 8.31 0.02 1 372 81 81 THR HA H 4.69 0.02 1 373 81 81 THR CA C 58.746 0.2 1 374 81 81 THR CB C 71.193 0.2 1 375 81 81 THR N N 107.377 0.1 1 376 82 82 TYR H H 11.05 0.02 1 377 82 82 TYR HA H 4.09 0.02 1 378 82 82 TYR CA C 62.9 0.2 1 379 82 82 TYR CB C 38 0.2 1 380 82 82 TYR N N 124.4 0.1 1 381 83 83 LYS H H 8.65 0.02 1 382 83 83 LYS HA H 3.76 0.02 1 383 83 83 LYS CA C 59.711 0.2 1 384 83 83 LYS CB C 32.431 0.2 1 385 83 83 LYS N N 118.6 0.1 1 386 84 84 GLU H H 7.51 0.02 1 387 84 84 GLU HA H 3.72 0.02 1 388 84 84 GLU CA C 58.923 0.2 1 389 84 84 GLU CB C 29.229 0.2 1 390 84 84 GLU N N 117.62 0.1 1 391 85 85 VAL H H 8.46 0.02 1 392 85 85 VAL HA H 3.3 0.02 1 393 85 85 VAL CA C 66.4 0.2 1 394 85 85 VAL CB C 29.2 0.2 1 395 85 85 VAL N N 124.2 0.1 1 396 86 86 CYS H H 8.29 0.02 1 397 86 86 CYS HA H 4.3 0.02 1 398 86 86 CYS CA C 61.857 0.2 1 399 86 86 CYS CB C 26.723 0.2 1 400 86 86 CYS N N 117.68 0.1 1 401 87 87 SER H H 7.23 0.02 1 402 87 87 SER HA H 4.3 0.02 1 403 87 87 SER CA C 60.188 0.2 1 404 87 87 SER CB C 65.342 0.2 1 405 87 87 SER N N 114.085 0.1 1 406 88 88 GLU H H 7.68 0.02 1 407 88 88 GLU HA H 4.05 0.02 1 408 88 88 GLU CA C 61.226 0.2 1 409 88 88 GLU N N 111.038 0.1 1 410 89 89 LYS H H 7.8 0.02 1 411 89 89 LYS HA H 4.42 0.02 1 412 89 89 LYS CA C 56.715 0.2 1 413 89 89 LYS CB C 31.247 0.2 1 414 89 89 LYS N N 116.13 0.1 1 415 90 90 THR H H 8.17 0.02 1 416 90 90 THR HA H 5.29 0.02 1 417 90 90 THR CA C 61.612 0.2 1 418 90 90 THR CB C 71.705 0.2 1 419 90 90 THR N N 105.28 0.1 1 420 91 91 GLY H H 6.63 0.02 1 421 91 91 GLY HA2 H 3.69 0.02 2 422 91 91 GLY HA3 H 3.69 0.02 2 423 91 91 GLY CA C 46.307 0.2 1 424 91 91 GLY N N 108.88 0.1 1 425 92 92 HIS H H 7.95 0.02 1 426 92 92 HIS HA H 4.03 0.02 1 427 92 92 HIS CA C 57.233 0.2 1 428 92 92 HIS CB C 33.551 0.2 1 429 92 92 HIS N N 121.88 0.1 1 430 93 93 ALA H H 9.57 0.02 1 431 93 93 ALA HA H 4.7 0.02 1 432 93 93 ALA CA C 50.292 0.2 1 433 93 93 ALA CB C 20.019 0.2 1 434 93 93 ALA N N 122.02 0.1 1 435 94 94 GLU H H 9.27 0.02 1 436 94 94 GLU HA H 4.64 0.02 1 437 94 94 GLU CA C 57.5 0.2 1 438 94 94 GLU CB C 27.8 0.2 1 439 94 94 GLU N N 120.4 0.1 1 440 95 95 VAL H H 9.59 0.02 1 441 95 95 VAL HA H 5.58 0.02 1 442 95 95 VAL CA C 58.76 0.2 1 443 95 95 VAL CB C 36.746 0.2 1 444 95 95 VAL N N 118.52 0.1 1 445 96 96 VAL H H 9.41 0.02 1 446 96 96 VAL HA H 4.95 0.02 1 447 96 96 VAL CA C 58.899 0.2 1 448 96 96 VAL CB C 35.22 0.2 1 449 96 96 VAL N N 118.86 0.1 1 450 97 97 ARG H H 9.23 0.02 1 451 97 97 ARG HA H 4.98 0.02 1 452 97 97 ARG CA C 54.1 0.2 1 453 97 97 ARG CB C 33.2 0.2 1 454 97 97 ARG N N 125.9 0.1 1 455 98 98 VAL H H 9.23 0.02 1 456 98 98 VAL HA H 4.13 0.02 1 457 98 98 VAL CA C 60.993 0.2 1 458 98 98 VAL CB C 33.219 0.2 1 459 98 98 VAL N N 125.89 0.1 1 460 99 99 VAL H H 8.92 0.02 1 461 99 99 VAL HA H 4.82 0.02 1 462 99 99 VAL CA C 60.974 0.2 1 463 99 99 VAL CB C 31.261 0.2 1 464 99 99 VAL N N 128.01 0.1 1 465 100 100 TYR H H 9.36 0.02 1 466 100 100 TYR HA H 5.5 0.02 1 467 100 100 TYR CA C 54.942 0.2 1 468 100 100 TYR CB C 42.021 0.2 1 469 100 100 TYR N N 125.68 0.1 1 470 101 101 ARG H H 8.53 0.02 1 471 101 101 ARG HA H 4.88 0.02 1 472 101 101 ARG CA C 53.169 0.2 1 473 101 101 ARG CB C 30.274 0.2 1 474 101 101 ARG N N 120.4 0.1 1 475 102 102 PRO HA H 5.31 0.02 1 476 102 102 PRO CA C 63.5 0.1 1 477 102 102 PRO CB C 31.9 0.1 1 478 103 103 GLU H H 9.89 0.02 1 479 103 103 GLU HA H 4.19 0.02 1 480 103 103 GLU CA C 57.667 0.2 1 481 103 103 GLU CB C 27.693 0.2 1 482 103 103 GLU N N 118.6 0.1 1 483 104 104 HIS H H 8.18 0.02 1 484 104 104 HIS HA H 4.9 0.02 1 485 104 104 HIS CA C 55.912 0.2 1 486 104 104 HIS CB C 35.44 0.2 1 487 104 104 HIS N N 119.37 0.1 1 488 105 105 ILE H H 8.45 0.02 1 489 105 105 ILE HA H 4.42 0.02 1 490 105 105 ILE CA C 60.979 0.2 1 491 105 105 ILE CB C 39.928 0.2 1 492 105 105 ILE N N 121.42 0.1 1 493 106 106 SER H H 8.31 0.02 1 494 106 106 SER HA H 4.94 0.02 1 495 106 106 SER CA C 56.095 0.2 1 496 106 106 SER CB C 67.307 0.2 1 497 106 106 SER N N 118.64 0.1 1 498 107 107 PHE H H 9.23 0.02 1 499 107 107 PHE HA H 3.99 0.02 1 500 107 107 PHE CA C 61.4 0.2 1 501 107 107 PHE CB C 38.755 0.2 1 502 107 107 PHE N N 121.08 0.1 1 503 108 108 GLU H H 9.25 0.02 1 504 108 108 GLU HA H 3.73 0.02 1 505 108 108 GLU CA C 61.763 0.2 1 506 108 108 GLU CB C 28.506 0.2 1 507 108 108 GLU N N 117.05 0.1 1 508 109 109 GLU H H 7.85 0.02 1 509 109 109 GLU HA H 3.85 0.02 1 510 109 109 GLU CA C 59.261 0.2 1 511 109 109 GLU CB C 29.805 0.2 1 512 109 109 GLU N N 120.22 0.1 1 513 110 110 LEU H H 7.61 0.02 1 514 110 110 LEU HA H 3.85 0.02 1 515 110 110 LEU CA C 57.867 0.2 1 516 110 110 LEU CB C 41.153 0.2 1 517 110 110 LEU N N 120.44 0.1 1 518 111 111 LEU H H 8.42 0.02 1 519 111 111 LEU HA H 3.46 0.02 1 520 111 111 LEU CA C 56.778 0.2 1 521 111 111 LEU CB C 41.401 0.2 1 522 111 111 LEU N N 118.69 0.1 1 523 112 112 LYS H H 7.41 0.02 1 524 112 112 LYS HA H 3.95 0.02 1 525 112 112 LYS CA C 60.818 0.2 1 526 112 112 LYS CB C 32.954 0.2 1 527 112 112 LYS N N 119.09 0.1 1 528 113 113 VAL H H 6.85 0.02 1 529 113 113 VAL HA H 3.34 0.02 1 530 113 113 VAL CA C 65.759 0.2 1 531 113 113 VAL CB C 32.975 0.2 1 532 113 113 VAL N N 116.77 0.1 1 533 114 114 PHE H H 7.96 0.02 1 534 114 114 PHE HA H 3.92 0.02 1 535 114 114 PHE CA C 60.322 0.2 1 536 114 114 PHE CB C 38 0.2 1 537 114 114 PHE N N 120.97 0.1 1 538 115 115 TRP H H 8.99 0.02 1 539 115 115 TRP HA H 3.84 0.02 1 540 115 115 TRP CA C 59.673 0.2 1 541 115 115 TRP N N 120.696 0.1 1 542 116 116 GLU H H 7.43 0.02 1 543 116 116 GLU HA H 4.06 0.02 1 544 116 116 GLU CA C 57.736 0.2 1 545 116 116 GLU CB C 30.212 0.2 1 546 116 116 GLU N N 106.2 0.1 1 547 117 117 ASN H H 7.29 0.02 1 548 117 117 ASN HA H 4.79 0.02 1 549 117 117 ASN CA C 53.867 0.2 1 550 117 117 ASN CB C 39.584 0.2 1 551 117 117 ASN N N 113.05 0.1 1 552 118 118 HIS H H 7.77 0.02 1 553 118 118 HIS HA H 4.4 0.02 1 554 118 118 HIS CA C 54.5 0.2 1 555 118 118 HIS CB C 30.79 0.2 1 556 118 118 HIS N N 113.8 0.1 1 557 119 119 ASP H H 9.23 0.02 1 558 119 119 ASP HA H 4.82 0.02 1 559 119 119 ASP CA C 50.057 0.2 1 560 119 119 ASP CB C 38.721 0.2 1 561 119 119 ASP N N 120.8 0.1 1 562 120 120 PRO HA H 4.69 0.02 1 563 120 120 PRO CA C 63.98 0.2 1 564 120 120 PRO CB C 31.75 0.2 1 565 121 121 THR H H 8.36 0.02 1 566 121 121 THR HA H 5.02 0.02 1 567 121 121 THR CA C 62.01 0.2 1 568 121 121 THR CB C 70.1 0.2 1 569 121 121 THR N N 110.7 0.1 1 570 122 122 GLN H H 8.23 0.02 1 571 122 122 GLN HA H 4.16 0.02 1 572 122 122 GLN CA C 57.182 0.2 1 573 122 122 GLN N N 121.85 0.1 1 574 123 123 GLY H H 6.95 0.02 1 575 123 123 GLY HA2 H 4.12 0.02 2 576 123 123 GLY HA3 H 3.51 0.02 2 577 123 123 GLY CA C 45.071 0.2 1 578 123 123 GLY N N 110.78 0.1 1 579 124 124 MET H H 9.12 0.02 1 580 124 124 MET HA H 4.56 0.02 1 581 124 124 MET CA C 51.8 0.2 1 582 124 124 MET CB C 29 0.2 1 583 124 124 MET N N 129.2 0.1 1 584 125 125 ARG H H 7.96 0.02 1 585 125 125 ARG HA H 4.46 0.02 1 586 125 125 ARG CA C 55.354 0.2 1 587 125 125 ARG CB C 32.05 0.2 1 588 125 125 ARG N N 120.35 0.1 1 589 126 126 GLN H H 8.72 0.02 1 590 126 126 GLN HA H 4.84 0.02 1 591 126 126 GLN CA C 55.083 0.2 1 592 126 126 GLN CB C 30.078 0.2 1 593 126 126 GLN N N 120.94 0.1 1 594 127 127 GLY H H 10.33 0.02 1 595 127 127 GLY HA2 H 3.92 0.02 2 596 127 127 GLY HA3 H 3.65 0.02 2 597 127 127 GLY CA C 46.969 0.2 1 598 127 127 GLY N N 120.71 0.1 1 599 128 128 ASN H H 9.04 0.02 1 600 128 128 ASN HA H 4.7 0.02 1 601 128 128 ASN CA C 52.939 0.2 1 602 128 128 ASN CB C 39.009 0.2 1 603 128 128 ASN N N 125.49 0.1 1 604 129 129 ASP H H 7.75 0.02 1 605 129 129 ASP HA H 4.52 0.02 1 606 129 129 ASP CA C 53.926 0.2 1 607 129 129 ASP CB C 38.959 0.2 1 608 129 129 ASP N N 120.83 0.1 1 609 130 130 PHE H H 8.82 0.02 1 610 130 130 PHE HA H 4.43 0.02 1 611 130 130 PHE CA C 57.767 0.2 1 612 130 130 PHE CB C 40.795 0.2 1 613 130 130 PHE N N 123.84 0.1 1 614 131 131 GLY H H 8.24 0.02 1 615 131 131 GLY HA2 H 4.83 0.02 2 616 131 131 GLY HA3 H 3.95 0.02 2 617 131 131 GLY CA C 45.01 0.2 1 618 131 131 GLY N N 111.88 0.1 1 619 132 132 THR H H 9.21 0.02 1 620 132 132 THR HA H 4.22 0.02 1 621 132 132 THR CA C 64.355 0.2 1 622 132 132 THR CB C 70.044 0.2 1 623 132 132 THR N N 113.04 0.1 1 624 133 133 GLN H H 10.45 0.02 1 625 133 133 GLN HA H 5.16 0.02 1 626 133 133 GLN CA C 55.8 0.2 1 627 133 133 GLN CB C 27.7 0.2 1 628 133 133 GLN N N 124.5 0.1 1 629 134 134 TYR H H 7.38 0.02 1 630 134 134 TYR HA H 4.87 0.02 1 631 134 134 TYR CA C 56.027 0.2 1 632 134 134 TYR CB C 38.083 0.2 1 633 134 134 TYR N N 119.5 0.1 1 634 135 135 ARG H H 6.7 0.02 1 635 135 135 ARG HA H 4.29 0.02 1 636 135 135 ARG CA C 54.81 0.2 1 637 135 135 ARG CB C 29.798 0.2 1 638 135 135 ARG N N 116.25 0.1 1 639 136 136 SER H H 7.89 0.02 1 640 136 136 SER HA H 4.57 0.02 1 641 136 136 SER CA C 58.689 0.2 1 642 136 136 SER CB C 61.495 0.2 1 643 136 136 SER N N 117.35 0.1 1 644 137 137 ALA H H 10.13 0.02 1 645 137 137 ALA HA H 5.1 0.02 1 646 137 137 ALA CA C 52.6 0.2 1 647 137 137 ALA CB C 22.3 0.2 1 648 137 137 ALA N N 133 0.1 1 649 138 138 VAL H H 8.06 0.02 1 650 138 138 VAL HA H 3.88 0.02 1 651 138 138 VAL CA C 62.23 0.2 1 652 138 138 VAL CB C 34.685 0.2 1 653 138 138 VAL N N 118.52 0.1 1 654 139 139 TYR H H 7.84 0.02 1 655 139 139 TYR HA H 5.97 0.02 1 656 139 139 TYR CA C 62.315 0.2 1 657 139 139 TYR CB C 37.32 0.2 1 658 139 139 TYR N N 124.41 0.1 1 659 140 140 PRO HA H 3.99 0.02 1 660 140 140 PRO CA C 62.6 0.2 1 661 140 140 PRO CB C 34.4 0.2 1 662 141 141 THR H H 8.89 0.02 1 663 141 141 THR HA H 4.51 0.02 1 664 141 141 THR CA C 61.032 0.2 1 665 141 141 THR CB C 69.66 0.2 1 666 141 141 THR N N 113.44 0.1 1 667 142 142 SER H H 7.26 0.02 1 668 142 142 SER HA H 4.69 0.02 1 669 142 142 SER CA C 56.367 0.2 1 670 142 142 SER CB C 66.455 0.2 1 671 142 142 SER N N 113.4 0.1 1 672 143 143 ALA HA H 4.15 0.02 1 673 143 143 ALA CA C 54.82 0.2 1 674 143 143 ALA CB C 18.34 0.2 1 675 144 144 VAL H H 7.79 0.02 1 676 144 144 VAL HA H 3.93 0.02 1 677 144 144 VAL CA C 65.412 0.2 1 678 144 144 VAL CB C 31.743 0.2 1 679 144 144 VAL N N 118.11 0.1 1 680 145 145 GLN H H 7.48 0.02 1 681 145 145 GLN HA H 3.68 0.02 1 682 145 145 GLN CA C 58.488 0.2 1 683 145 145 GLN CB C 29.527 0.2 1 684 145 145 GLN N N 120 0.1 1 685 146 146 MET H H 7.75 0.02 1 686 146 146 MET HA H 4.17 0.02 1 687 146 146 MET CA C 58.54 0.2 1 688 146 146 MET CB C 32.138 0.2 1 689 146 146 MET N N 120.83 0.1 1 690 147 147 GLU H H 7.89 0.02 1 691 147 147 GLU HA H 4.33 0.02 1 692 147 147 GLU CA C 59.646 0.2 1 693 147 147 GLU CB C 29.414 0.2 1 694 147 147 GLU N N 117.69 0.1 1 695 148 148 ALA H H 7.71 0.02 1 696 148 148 ALA HA H 4.3 0.02 1 697 148 148 ALA CA C 54.875 0.2 1 698 148 148 ALA CB C 18.995 0.2 1 699 148 148 ALA N N 119.82 0.1 1 700 149 149 ALA H H 9.25 0.02 1 701 149 149 ALA HA H 4.3 0.02 1 702 149 149 ALA CA C 55.626 0.2 1 703 149 149 ALA CB C 18.399 0.2 1 704 149 149 ALA N N 122.95 0.1 1 705 150 150 LEU H H 8.57 0.02 1 706 150 150 LEU HA H 4.17 0.02 1 707 150 150 LEU CA C 58.345 0.2 1 708 150 150 LEU CB C 41.614 0.2 1 709 150 150 LEU N N 118.52 0.1 1 710 151 151 ARG H H 8.19 0.02 1 711 151 151 ARG HA H 4.24 0.02 1 712 151 151 ARG CA C 59.299 0.2 1 713 151 151 ARG CB C 30.33 0.2 1 714 151 151 ARG N N 119.86 0.1 1 715 152 152 SER H H 8.34 0.02 1 716 152 152 SER HA H 4.27 0.02 1 717 152 152 SER CA C 61.173 0.2 1 718 152 152 SER CB C 62.709 0.2 1 719 152 152 SER N N 114.24 0.1 1 720 153 153 LYS H H 8.23 0.02 1 721 153 153 LYS HA H 3.42 0.02 1 722 153 153 LYS CA C 59.827 0.2 1 723 153 153 LYS CB C 32.307 0.2 1 724 153 153 LYS N N 124.08 0.1 1 725 154 154 GLU H H 7.68 0.02 1 726 154 154 GLU HA H 4.03 0.02 1 727 154 154 GLU CA C 58.905 0.2 1 728 154 154 GLU CB C 29.066 0.2 1 729 154 154 GLU N N 118.51 0.1 1 730 155 155 GLU H H 7.89 0.02 1 731 155 155 GLU HA H 4.05 0.02 1 732 155 155 GLU CA C 58.689 0.2 1 733 155 155 GLU CB C 29.414 0.2 1 734 155 155 GLU N N 117.52 0.1 1 735 156 156 TYR H H 8.77 0.02 1 736 156 156 TYR HA H 4.45 0.02 1 737 156 156 TYR CA C 58.448 0.2 1 738 156 156 TYR CB C 36.199 0.2 1 739 156 156 TYR N N 121.33 0.1 1 740 157 157 GLN H H 8.65 0.02 1 741 157 157 GLN HA H 3.64 0.02 1 742 157 157 GLN CA C 58.327 0.2 1 743 157 157 GLN CB C 29.546 0.2 1 744 157 157 GLN N N 117.87 0.1 1 745 158 158 LYS H H 7.16 0.02 1 746 158 158 LYS HA H 4.02 0.02 1 747 158 158 LYS CA C 59.897 0.2 1 748 158 158 LYS CB C 32.618 0.2 1 749 158 158 LYS N N 115.74 0.1 1 750 159 159 VAL H H 6.97 0.02 1 751 159 159 VAL HA H 4.03 0.02 1 752 159 159 VAL CA C 65 0.2 1 753 159 159 VAL CB C 31.399 0.2 1 754 159 159 VAL N N 114.34 0.1 1 755 160 160 LEU H H 8.45 0.02 1 756 160 160 LEU HA H 3.86 0.02 1 757 160 160 LEU CA C 58.436 0.2 1 758 160 160 LEU CB C 40.7 0.2 1 759 160 160 LEU N N 122.69 0.1 1 760 161 161 SER H H 8.89 0.02 1 761 161 161 SER HA H 4.45 0.02 1 762 161 161 SER CA C 58.321 0.2 1 763 161 161 SER CB C 62.929 0.2 1 764 161 161 SER N N 116.52 0.1 1 765 162 162 LYS H H 7.37 0.02 1 766 162 162 LYS HA H 4.1 0.02 1 767 162 162 LYS CA C 58.226 0.2 1 768 162 162 LYS CB C 31.972 0.2 1 769 162 162 LYS N N 122.31 0.1 1 770 163 163 HIS H H 7.55 0.02 1 771 163 163 HIS HA H 4.54 0.02 1 772 163 163 HIS CA C 56.421 0.2 1 773 163 163 HIS CB C 29.777 0.2 1 774 163 163 HIS N N 116.98 0.1 1 775 164 164 ASN H H 7.82 0.02 1 776 164 164 ASN HA H 4.35 0.02 1 777 164 164 ASN CA C 54.989 0.2 1 778 164 164 ASN CB C 36.478 0.2 1 779 164 164 ASN N N 111.33 0.1 1 780 165 165 PHE H H 7.88 0.02 1 781 165 165 PHE HA H 4.45 0.02 1 782 165 165 PHE CA C 58.689 0.2 1 783 165 165 PHE CB C 41.373 0.2 1 784 165 165 PHE N N 117.17 0.1 1 785 166 166 GLY H H 9.05 0.02 1 786 166 166 GLY HA2 H 4.18 0.02 2 787 166 166 GLY HA3 H 3.92 0.02 2 788 166 166 GLY CA C 44.241 0.2 1 789 166 166 GLY N N 108.208 0.1 1 790 167 167 PRO HA H 4.38 0.02 1 791 167 167 PRO CA C 62.06 0.2 1 792 167 167 PRO CB C 32.38 0.2 1 793 168 168 ILE H H 9.11 0.02 1 794 168 168 ILE HA H 3.94 0.02 1 795 168 168 ILE CA C 63.279 0.2 1 796 168 168 ILE CB C 39.061 0.2 1 797 168 168 ILE N N 122.67 0.1 1 798 169 169 THR H H 10 0.02 1 799 169 169 THR HA H 4.42 0.02 1 800 169 169 THR CA C 61.793 0.2 1 801 169 169 THR CB C 69.228 0.2 1 802 169 169 THR N N 120.521 0.1 1 803 170 170 THR H H 7.69 0.02 1 804 170 170 THR HA H 3.66 0.02 1 805 170 170 THR CA C 65.443 0.2 1 806 170 170 THR CB C 70.055 0.2 1 807 170 170 THR N N 119.18 0.1 1 808 171 171 ASP H H 8.94 0.02 1 809 171 171 ASP HA H 4.56 0.02 1 810 171 171 ASP CA C 52.66 0.2 1 811 171 171 ASP CB C 42.71 0.2 1 812 171 171 ASP N N 129.5 0.1 1 813 172 172 ILE H H 8.1 0.02 1 814 172 172 ILE HA H 5.59 0.02 1 815 172 172 ILE CA C 60.641 0.2 1 816 172 172 ILE CB C 38.027 0.2 1 817 172 172 ILE N N 125.52 0.1 1 818 173 173 ARG H H 7.42 0.02 1 819 173 173 ARG HA H 4.86 0.02 1 820 173 173 ARG CA C 55.549 0.2 1 821 173 173 ARG CB C 38.06 0.2 1 822 173 173 ARG N N 122.72 0.1 1 823 174 174 GLU H H 9.03 0.02 1 824 174 174 GLU HA H 4.38 0.02 1 825 174 174 GLU CA C 56.683 0.2 1 826 174 174 GLU CB C 32.577 0.2 1 827 174 174 GLU N N 121.94 0.1 1 828 175 175 GLY H H 9.08 0.02 1 829 175 175 GLY HA2 H 3.81 0.02 2 830 175 175 GLY HA3 H 3.75 0.02 2 831 175 175 GLY CA C 46.832 0.2 1 832 175 175 GLY N N 109.42 0.1 1 833 176 176 GLN H H 8.74 0.02 1 834 176 176 GLN HA H 4.11 0.02 1 835 176 176 GLN CA C 53.731 0.2 1 836 176 176 GLN CB C 27.983 0.2 1 837 176 176 GLN N N 118.79 0.1 1 838 177 177 VAL H H 7.83 0.02 1 839 177 177 VAL HA H 3.77 0.02 1 840 177 177 VAL CA C 61.814 0.2 1 841 177 177 VAL CB C 33.384 0.2 1 842 177 177 VAL N N 123.46 0.1 1 843 178 178 PHE H H 8.01 0.02 1 844 178 178 PHE HA H 4.35 0.02 1 845 178 178 PHE CA C 57.685 0.2 1 846 178 178 PHE CB C 40.690 0.2 1 847 178 178 PHE N N 124.44 0.1 1 848 179 179 TYR H H 8.21 0.02 1 849 179 179 TYR HA H 4.63 0.02 1 850 179 179 TYR CA C 57.66 0.2 1 851 179 179 TYR CB C 40.715 0.2 1 852 179 179 TYR N N 127.51 0.1 1 853 180 180 TYR H H 8.99 0.02 1 854 180 180 TYR HA H 3.62 0.02 1 855 180 180 TYR CA C 59.673 0.2 1 856 180 180 TYR CB C 38.4 0.2 1 857 180 180 TYR N N 120.69 0.1 1 858 181 181 ALA H H 7.15 0.02 1 859 181 181 ALA HA H 4.56 0.02 1 860 181 181 ALA CA C 49.873 0.2 1 861 181 181 ALA CB C 21.274 0.2 1 862 181 181 ALA N N 119 0.1 1 863 182 182 GLU H H 10.87 0.02 1 864 182 182 GLU HA H 4.02 0.02 1 865 182 182 GLU CA C 59.052 0.2 1 866 182 182 GLU CB C 30.749 0.2 1 867 182 182 GLU N N 117.59 0.1 1 868 183 183 ASP H H 8.71 0.02 1 869 183 183 ASP HA H 4.57 0.02 1 870 183 183 ASP CA C 57.994 0.2 1 871 183 183 ASP CB C 42.564 0.2 1 872 183 183 ASP N N 120.51 0.1 1 873 184 184 TYR H H 7.84 0.02 1 874 184 184 TYR HA H 4.25 0.02 1 875 184 184 TYR CA C 59.644 0.2 1 876 184 184 TYR CB C 36.972 0.2 1 877 184 184 TYR N N 113.04 0.1 1 878 185 185 HIS H H 7.28 0.02 1 879 185 185 HIS HA H 4.43 0.02 1 880 185 185 HIS CA C 58.42 0.2 1 881 185 185 HIS CB C 32.85 0.2 1 882 185 185 HIS N N 115.9 0.1 1 883 186 186 GLN H H 7.57 0.02 1 884 186 186 GLN HA H 3.97 0.02 1 885 186 186 GLN CA C 55.559 0.2 1 886 186 186 GLN CB C 25.729 0.2 1 887 186 186 GLN N N 118.12 0.1 1 888 187 187 GLN H H 10.2 0.02 1 889 187 187 GLN HA H 4.1 0.02 1 890 187 187 GLN CA C 58.3 0.2 1 891 187 187 GLN CB C 26.6 0.2 1 892 187 187 GLN N N 123.5 0.1 1 893 188 188 TYR H H 7.72 0.02 1 894 188 188 TYR CA C 63.7 0.2 1 895 188 188 TYR CB C 39.6 0.2 1 896 188 188 TYR N N 120.4 0.1 1 897 189 189 LEU H H 10.207 0.02 1 898 189 189 LEU HA H 4.25 0.02 1 899 189 189 LEU CA C 55.578 0.2 1 900 189 189 LEU CB C 41.5 0.2 1 901 189 189 LEU N N 115.21 0.1 1 902 190 190 SER H H 7.47 0.02 1 903 190 190 SER HA H 4.34 0.02 1 904 190 190 SER CA C 61.375 0.2 1 905 190 190 SER CB C 59.272 0.2 1 906 190 190 SER N N 113.83 0.1 1 907 191 191 LYS H H 6.77 0.02 1 908 191 191 LYS HA H 3.46 0.02 1 909 191 191 LYS CA C 58.6 0.2 1 910 191 191 LYS CB C 33.2 0.2 1 911 191 191 LYS N N 118.4 0.1 1 912 192 192 ASN H H 7.94 0.02 1 913 192 192 ASN HA H 4.83 0.02 1 914 192 192 ASN CA C 50.1 0.2 1 915 192 192 ASN CB C 38.307 0.2 1 916 192 192 ASN N N 114.21 0.1 1 917 193 193 PRO HA H 4.66 0.02 1 918 193 193 PRO CA C 64.4 0.2 1 919 193 193 PRO CB C 31.9 0.2 1 920 194 194 ASP H H 8.19 0.02 1 921 194 194 ASP HA H 4.85 0.02 1 922 194 194 ASP CA C 53.59 0.2 1 923 194 194 ASP CB C 40.498 0.2 1 924 194 194 ASP N N 116.98 0.1 1 925 195 195 GLY H H 8.057 0.02 1 926 195 195 GLY HA2 H 4.05 0.02 2 927 195 195 GLY HA3 H 3.53 0.02 2 928 195 195 GLY CA C 45.263 0.2 1 929 195 195 GLY N N 107.3 0.1 1 930 196 196 TYR H H 8.27 0.02 1 931 196 196 TYR HA H 4.66 0.02 1 932 196 196 TYR CA C 58.633 0.2 1 933 196 196 TYR CB C 39.47 0.2 1 934 196 196 TYR N N 120.74 0.1 1 935 197 197 CYS H H 8.17 0.02 1 936 197 197 CYS CA C 57.2 0.2 1 937 197 197 CYS CB C 29.3 0.2 1 938 197 197 CYS N N 123.6 0.1 1 939 198 198 GLY H H 8.44 0.02 1 940 198 198 GLY HA2 H 3.96 0.02 2 941 198 198 GLY HA3 H 3.84 0.02 2 942 198 198 GLY CA C 45.078 0.2 1 943 198 198 GLY N N 109.28 0.1 1 944 199 199 LEU H H 8.41 0.02 1 945 199 199 LEU HA H 4.42 0.02 1 946 199 199 LEU CA C 55.103 0.2 1 947 199 199 LEU CB C 43.384 0.2 1 948 199 199 LEU N N 120.84 0.1 1 949 200 200 GLY H H 8.33 0.02 1 950 200 200 GLY HA2 H 3.89 0.02 2 951 200 200 GLY HA3 H 3.88 0.02 2 952 200 200 GLY CA C 44.987 0.2 1 953 200 200 GLY N N 109.89 0.1 1 954 201 201 GLY H H 8.28 0.02 1 955 201 201 GLY HA2 H 3.94 0.02 2 956 201 201 GLY HA3 H 3.69 0.02 2 957 201 201 GLY CA C 43.044 0.2 1 958 201 201 GLY N N 105.82 0.1 1 959 202 202 THR H H 8.49 0.02 1 960 202 202 THR HA H 3.7 0.02 1 961 202 202 THR CA C 63.221 0.2 1 962 202 202 THR CB C 71.5 0.2 1 963 202 202 THR N N 108.63 0.1 1 964 203 203 GLY H H 8.56 0.02 1 965 203 203 GLY HA2 H 4.19 0.02 2 966 203 203 GLY HA3 H 3.45 0.02 2 967 203 203 GLY CA C 44.859 0.2 1 968 203 203 GLY N N 110.3 0.1 1 969 204 204 VAL H H 7.55 0.02 1 970 204 204 VAL HA H 3.77 0.02 1 971 204 204 VAL CA C 61.405 0.2 1 972 204 204 VAL CB C 31.181 0.2 1 973 204 204 VAL N N 121.92 0.1 1 974 205 205 SER H H 8.81 0.02 1 975 205 205 SER HA H 4.19 0.02 1 976 205 205 SER CA C 59.279 0.2 1 977 205 205 SER CB C 63.265 0.2 1 978 205 205 SER N N 127.05 0.1 1 979 206 206 CYS H H 10.58 0.02 1 980 206 206 CYS CA C 63.367 0.2 1 981 206 206 CYS CB C 27.97 0.2 1 982 206 206 CYS N N 127.89 0.1 1 983 207 207 PRO HA H 4.44 0.02 1 984 207 207 PRO CA C 62.8 0.2 1 985 207 207 PRO CB C 31.7 0.2 1 986 208 208 MET H H 8.15 0.02 1 987 208 208 MET HA H 4.47 0.02 1 988 208 208 MET CA C 54.531 0.2 1 989 208 208 MET CB C 33.58 0.2 1 990 208 208 MET N N 120.66 0.1 1 991 209 209 ALA H H 8.55 0.02 1 992 209 209 ALA HA H 4.29 0.02 1 993 209 209 ALA CA C 52.09 0.2 1 994 209 209 ALA CB C 18.827 0.2 1 995 209 209 ALA N N 127.46 0.1 1 996 210 210 ILE H H 8.1 0.02 1 997 210 210 ILE HA H 4.08 0.02 1 998 210 210 ILE CA C 60.672 0.2 1 999 210 210 ILE CB C 38.732 0.2 1 1000 210 210 ILE N N 121.2 0.1 1 1001 211 211 LYS H H 8.39 0.02 1 1002 211 211 LYS HA H 4.31 0.02 1 1003 211 211 LYS CA C 56.217 0.2 1 1004 211 211 LYS CB C 32.974 0.2 1 1005 211 211 LYS N N 127.31 0.1 1 1006 212 212 LYS H H 7.95 0.02 1 1007 212 212 LYS HA H 4.13 0.02 1 1008 212 212 LYS CA C 57.566 0.2 1 1009 212 212 LYS CB C 33.787 0.2 1 1010 212 212 LYS N N 129.49 0.1 1 stop_ save_