data_5090 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: 1H(N), 15N, 13CO, 13C[agr], 13C[bgr] Assignment and Secondary Structure of a 20 kDa [agr]-L-fucosidase from Pea using TROSY ; _BMRB_accession_number 5090 _BMRB_flat_file_name bmr5090.str _Entry_type original _Submission_date 2001-07-19 _Accession_date 2001-07-24 _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 Codina Anna . . 2 Gairi Margarida . . 3 Tarrago Teresa . . 4 Viguera 'Ana Rosa' . . 5 Feliz Miguel . . 6 Ludevid Dolors . . 7 Giralt Ernest . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 156 "13C chemical shifts" 505 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H(N), 15N, 13CO, 13C[agr], 13C[bgr] Assignment and Secondary Structure of a 20 kDa [agr]-L-fucosidase from Pea using TROSY ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21986772 _PubMed_ID 11991358 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Codina Anna . . 2 Gairi Margarida . . 3 Tarrago Teresa . . 4 Viguera 'Ana Rosa' . . 5 Feliz Miguel . . 6 Ludevid Dolors . . 7 Giralt Ernest . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 295 _Page_last 296 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_Fuc _Saveframe_category molecular_system _Mol_system_name alfa-L-fucosidase _Abbreviation_common Fuc _Enzyme_commission_number 3.2.1.51 loop_ _Mol_system_component_name _Mol_label alfa-L-fucosidase $alfa-L-fucosidase stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_alfa-L-fucosidase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pea alfa-L-fucosidase' _Abbreviation_common Fuc _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 195 _Mol_residue_sequence ; GSHMEDVEQVLDINGNPIFP GVQYFILPAIRGPAGGGVRL GRTGDLTCPVTVLQDRQEVK YGLPVKFVIPEISPGIIFTG TPIEIEYAKKPNCAKSSKWL VFVDNVIQKACVGIGGPENY PGVQTLSGLFKIEKHESGFG YKLGFCVKGSPTCLDVGRFD NDEDGRRLNLTEHESFQVVF IQAEANDAEFIKSVV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 GLU 6 ASP 7 VAL 8 GLU 9 GLN 10 VAL 11 LEU 12 ASP 13 ILE 14 ASN 15 GLY 16 ASN 17 PRO 18 ILE 19 PHE 20 PRO 21 GLY 22 VAL 23 GLN 24 TYR 25 PHE 26 ILE 27 LEU 28 PRO 29 ALA 30 ILE 31 ARG 32 GLY 33 PRO 34 ALA 35 GLY 36 GLY 37 GLY 38 VAL 39 ARG 40 LEU 41 GLY 42 ARG 43 THR 44 GLY 45 ASP 46 LEU 47 THR 48 CYS 49 PRO 50 VAL 51 THR 52 VAL 53 LEU 54 GLN 55 ASP 56 ARG 57 GLN 58 GLU 59 VAL 60 LYS 61 TYR 62 GLY 63 LEU 64 PRO 65 VAL 66 LYS 67 PHE 68 VAL 69 ILE 70 PRO 71 GLU 72 ILE 73 SER 74 PRO 75 GLY 76 ILE 77 ILE 78 PHE 79 THR 80 GLY 81 THR 82 PRO 83 ILE 84 GLU 85 ILE 86 GLU 87 TYR 88 ALA 89 LYS 90 LYS 91 PRO 92 ASN 93 CYS 94 ALA 95 LYS 96 SER 97 SER 98 LYS 99 TRP 100 LEU 101 VAL 102 PHE 103 VAL 104 ASP 105 ASN 106 VAL 107 ILE 108 GLN 109 LYS 110 ALA 111 CYS 112 VAL 113 GLY 114 ILE 115 GLY 116 GLY 117 PRO 118 GLU 119 ASN 120 TYR 121 PRO 122 GLY 123 VAL 124 GLN 125 THR 126 LEU 127 SER 128 GLY 129 LEU 130 PHE 131 LYS 132 ILE 133 GLU 134 LYS 135 HIS 136 GLU 137 SER 138 GLY 139 PHE 140 GLY 141 TYR 142 LYS 143 LEU 144 GLY 145 PHE 146 CYS 147 VAL 148 LYS 149 GLY 150 SER 151 PRO 152 THR 153 CYS 154 LEU 155 ASP 156 VAL 157 GLY 158 ARG 159 PHE 160 ASP 161 ASN 162 ASP 163 GLU 164 ASP 165 GLY 166 ARG 167 ARG 168 LEU 169 ASN 170 LEU 171 THR 172 GLU 173 HIS 174 GLU 175 SER 176 PHE 177 GLN 178 VAL 179 VAL 180 PHE 181 ILE 182 GLN 183 ALA 184 GLU 185 ALA 186 ASN 187 ASP 188 ALA 189 GLU 190 PHE 191 ILE 192 LYS 193 SER 194 VAL 195 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 EMBL CAA57931 "alpha-fucosidase [Pisum sativum]" 97.95 217 98.43 98.43 4.85e-132 SP Q41015 "RecName: Full=Kunitz-type trypsin inhibitor-like 1 protein; AltName: Full=Protease inhibitor from pea 1; Flags: Precursor [Pisu" 97.95 217 98.43 98.43 4.85e-132 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $alfa-L-fucosidase Pea 3888 Eukaryota Viridiplantae Pisum sativum 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 $alfa-L-fucosidase 'recombinant technology' . . . . . 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 $alfa-L-fucosidase . mM 0.8 1.0 '[U-99% 13C; U-99% 15N; U-85% 2H]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.7 0.1 n/a temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Chemical shift assignment were made based on TROSY experiments performed with a deuterated sample. Isotopic efect were corrected with a factor of +0.23 ppm in case of 15N (Gardner et al., 1996) and according to the number of deuterons one and two bond away from the 13Ca and 13Cb nucleus (Venters et al., 1996). TROSY effect were corrected based on a JHN of 93 Hz. The chemical shifts 620-624 correspond to a Ser that has a previous Pro. Instead of Ser150 it could be Ser2 but this last assignment is not provable because Ser2 is in the floppy N-terminus of the protein. ; 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 0.0 internal direct . . . 1.0 TSP N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 TSP C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 ; Chemical shift assignment were made based on TROSY experiments performed with a deuterated sample. Isotopic efect were corrected with a factor of +0.23 ppm in case of 15N (Gardner et al., 1996) and according to the number of deuterons one and two bond away from the 13Ca and 13Cb nucleus (Venters et al., 1996). TROSY effect were corrected based on a JHN of 93 Hz. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name alfa-L-fucosidase _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 . 3 HIS C C 177.05 0.02 1 2 . 3 HIS CA C 48.3 0.03 1 3 . 4 MET H H 8.355 0.01 1 4 . 4 MET N N 122.754 0.05 1 5 . 4 MET C C 175.97 0.02 1 6 . 4 MET CA C 55.28 0.03 1 7 . 4 MET CB C 33.19 0.06 1 8 . 5 GLU H H 8.353 0.01 1 9 . 5 GLU N N 121.374 0.05 1 10 . 5 GLU C C 176.18 0.02 1 11 . 5 GLU CA C 56.86 0.03 1 12 . 5 GLU CB C 30.61 0.06 1 13 . 6 ASP H H 8.412 0.01 1 14 . 6 ASP N N 121.008 0.05 1 15 . 6 ASP C C 175.80 0.02 1 16 . 6 ASP CA C 54.75 0.03 1 17 . 6 ASP CB C 41.84 0.06 1 18 . 7 VAL H H 7.835 0.01 1 19 . 7 VAL N N 118.422 0.05 1 20 . 7 VAL C C 175.32 0.02 1 21 . 7 VAL CA C 61.99 0.03 1 22 . 7 VAL CB C 33.71 0.06 1 23 . 8 GLU H H 8.245 0.01 1 24 . 8 GLU N N 121.608 0.05 1 25 . 8 GLU C C 175.77 0.02 1 26 . 8 GLU CA C 55 0.03 1 27 . 8 GLU CB C 33.68 0.06 1 28 . 9 GLN H H 8.873 0.01 1 29 . 9 GLN N N 122.429 0.05 1 30 . 9 GLN C C 176.3 0.02 1 31 . 9 GLN CA C 57.5 0.03 1 32 . 9 GLN CB C 29.19 0.06 1 33 . 10 VAL H H 7.832 0.01 1 34 . 10 VAL N N 126.463 0.05 1 35 . 10 VAL C C 173.62 0.02 1 36 . 10 VAL CA C 64.23 0.03 1 37 . 10 VAL CB C 31.38 0.06 1 38 . 11 LEU H H 7.386 0.01 1 39 . 11 LEU N N 125.122 0.05 1 40 . 11 LEU C C 176.5 0.02 1 41 . 11 LEU CA C 52.97 0.03 1 42 . 11 LEU CB C 45.68 0.06 1 43 . 12 ASP H H 9.033 0.01 1 44 . 12 ASP N N 118.218 0.05 1 45 . 12 ASP C C 180.36 0.02 1 46 . 12 ASP CA C 53 0.03 1 47 . 12 ASP CB C 42.66 0.06 1 48 . 13 ILE H H 8.502 0.01 1 49 . 13 ILE N N 115.688 0.05 1 50 . 13 ILE C C 176.63 0.02 1 51 . 13 ILE CA C 64.04 0.03 1 52 . 13 ILE CB C 39.74 0.06 1 53 . 14 ASN H H 8.328 0.01 1 54 . 14 ASN N N 119.318 0.05 1 55 . 14 ASN C C 175.69 0.02 1 56 . 14 ASN CA C 53.53 0.03 1 57 . 14 ASN CB C 40.6 0.06 1 58 . 15 GLY H H 8.541 0.01 1 59 . 15 GLY N N 108.397 0.05 1 60 . 15 GLY C C 173.43 0.02 1 61 . 15 GLY CA C 45.71 0.03 1 62 . 16 ASN H H 8.424 0.01 1 63 . 16 ASN N N 120.747 0.05 1 64 . 16 ASN C C 172.34 0.02 1 65 . 16 ASN CA C 51.05 0.03 1 66 . 16 ASN CB C 39.15 0.06 1 67 . 17 PRO C C 175.43 0.02 1 68 . 17 PRO CA C 62.96 0.03 1 69 . 17 PRO CB C 32.26 0.06 1 70 . 18 ILE H H 7.569 0.01 1 71 . 18 ILE N N 117.884 0.05 1 72 . 18 ILE C C 174.94 0.02 1 73 . 18 ILE CA C 59.21 0.03 1 74 . 18 ILE CB C 37.38 0.06 1 75 . 19 PHE H H 7.981 0.01 1 76 . 19 PHE N N 123.153 0.05 1 77 . 19 PHE C C 174.88 0.02 1 78 . 19 PHE CA C 55.01 0.03 1 79 . 19 PHE CB C 42.11 0.06 1 80 . 20 PRO C C 177.10 0.02 1 81 . 20 PRO CA C 63.54 0.03 1 82 . 20 PRO CB C 33 0.06 1 83 . 21 GLY H H 8.586 0.01 1 84 . 21 GLY N N 111.492 0.05 1 85 . 21 GLY C C 173.1 0.02 1 86 . 21 GLY CA C 46.14 0.03 1 87 . 22 VAL H H 7.446 0.01 1 88 . 22 VAL N N 123.153 0.05 1 89 . 22 VAL C C 174.51 0.02 1 90 . 22 VAL CA C 62.08 0.03 1 91 . 22 VAL CB C 33.77 0.06 1 92 . 23 GLN H H 8.23 0.01 1 93 . 23 GLN N N 123.372 0.05 1 94 . 23 GLN C C 175.92 0.02 1 95 . 23 GLN CA C 56.02 0.03 1 96 . 23 GLN CB C 30.45 0.06 1 97 . 24 TYR H H 9.471 0.01 1 98 . 24 TYR N N 121.352 0.05 1 99 . 24 TYR C C 175.34 0.02 1 100 . 24 TYR CA C 58.3 0.03 1 101 . 24 TYR CB C 43.57 0.06 1 102 . 25 PHE H H 9.807 0.01 1 103 . 25 PHE N N 119.221 0.05 1 104 . 25 PHE C C 176.05 0.02 1 105 . 25 PHE CA C 57.4 0.03 1 106 . 25 PHE CB C 41.79 0.06 1 107 . 26 ILE H H 8.825 0.01 1 108 . 26 ILE N N 121.261 0.05 1 109 . 26 ILE C C 173.92 0.02 1 110 . 26 ILE CA C 61.82 0.03 1 111 . 26 ILE CB C 39.59 0.06 1 112 . 27 LEU H H 8.122 0.01 1 113 . 27 LEU N N 125.778 0.05 1 114 . 27 LEU C C 173.71 0.02 9 115 . 27 LEU CA C 50.6 0.03 1 116 . 27 LEU CB C 44.19 0.06 1 117 . 28 PRO C C 177.24 0.02 1 118 . 28 PRO CA C 62.38 0.03 1 119 . 28 PRO CB C 32.62 0.06 1 120 . 29 ALA H H 7.853 0.01 1 121 . 29 ALA N N 123.142 0.05 1 122 . 29 ALA C C 177.14 0.02 1 123 . 29 ALA CA C 54.25 0.03 1 124 . 29 ALA CB C 19.42 0.06 1 125 . 33 PRO C C 177.62 0.02 1 126 . 33 PRO CA C 64.41 0.03 1 127 . 33 PRO CB C 32.56 0.06 1 128 . 34 ALA H H 8.595 0.01 1 129 . 34 ALA N N 122.905 0.05 1 130 . 34 ALA C C 178.55 0.02 1 131 . 34 ALA CA C 54.24 0.03 1 132 . 34 ALA CB C 20.21 0.06 1 133 . 35 GLY H H 8.186 0.01 1 134 . 35 GLY N N 104.795 0.05 1 135 . 35 GLY C C 172.48 0.02 1 136 . 35 GLY CA C 45.08 0.03 1 137 . 36 GLY H H 8.21 0.01 1 138 . 36 GLY N N 110.685 0.05 1 139 . 36 GLY C C 174.94 0.02 1 140 . 36 GLY CA C 44.6 0.03 1 141 . 37 GLY H H 8.806 0.01 1 142 . 37 GLY N N 107.404 0.05 1 143 . 37 GLY C C 173.43 0.02 1 144 . 37 GLY CA C 44.49 0.03 1 145 . 38 VAL H H 8.07 0.01 1 146 . 38 VAL N N 109.81 0.05 1 147 . 38 VAL C C 174.53 0.02 1 148 . 38 VAL CA C 60.37 0.03 1 149 . 38 VAL CB C 33.51 0.06 1 150 . 39 ARG H H 9.39 0.01 1 151 . 39 ARG N N 119.216 0.05 1 152 . 39 ARG C C 176.13 0.02 1 153 . 39 ARG CA C 55.18 0.03 1 154 . 39 ARG CB C 28.86 0.06 1 155 . 40 LEU H H 8.076 0.01 1 156 . 40 LEU N N 125.343 0.05 1 157 . 40 LEU C C 177.49 0.02 1 158 . 40 LEU CA C 54.28 0.03 1 159 . 40 LEU CB C 47.81 0.06 1 160 . 41 GLY H H 8.598 0.01 1 161 . 41 GLY N N 106.102 0.05 1 162 . 41 GLY C C 169.9 0.02 1 163 . 41 GLY CA C 45.25 0.03 1 164 . 42 ARG H H 8.542 0.01 1 165 . 42 ARG N N 120.31 0.05 1 166 . 42 ARG C C 176.41 0.02 1 167 . 42 ARG CA C 55.53 0.03 1 168 . 42 ARG CB C 32.18 0.06 1 169 . 43 THR H H 8.083 0.01 1 170 . 43 THR N N 114.783 0.05 1 171 . 43 THR C C 173.67 0.02 1 172 . 43 THR CA C 60.12 0.03 1 173 . 43 THR CB C 73.08 0.06 1 174 . 44 GLY H H 9.074 0.01 1 175 . 44 GLY N N 107.185 0.05 1 176 . 44 GLY C C 175.39 0.02 1 177 . 44 GLY CA C 47.19 0.03 1 178 . 45 ASP H H 8.808 0.01 1 179 . 45 ASP N N 126.09 0.05 1 180 . 45 ASP C C 177.12 0.02 1 181 . 45 ASP CA C 53.51 0.03 1 182 . 45 ASP CB C 41.66 0.06 1 183 . 46 LEU H H 8.144 0.01 1 184 . 46 LEU N N 122.29 0.05 1 185 . 46 LEU C C 178.44 0.02 1 186 . 46 LEU CA C 56.07 0.03 1 187 . 46 LEU CB C 41.09 0.06 1 188 . 47 THR C C 173.68 0.02 1 189 . 47 THR CA C 62.62 0.03 1 190 . 47 THR CB C 69.55 0.06 1 191 . 48 CYS H H 7.815 0.01 9 192 . 48 CYS N N 123.372 0.05 9 193 . 48 CYS C C 172.55 0.02 9 194 . 48 CYS CA C 51.05 0.03 9 195 . 48 CYS CB C 42.23 0.06 9 196 . 49 PRO C C 172.05 0.02 1 197 . 49 PRO CA C 62.33 0.03 1 198 . 49 PRO CB C 28.49 0.06 1 199 . 50 VAL H H 7.893 0.01 1 200 . 50 VAL N N 113.31 0.05 1 201 . 50 VAL C C 175.11 0.02 1 202 . 50 VAL CA C 60.34 0.03 1 203 . 50 VAL CB C 32.9 0.06 1 204 . 51 THR H H 8.334 0.01 1 205 . 51 THR N N 119.946 0.05 1 206 . 51 THR C C 173.43 0.02 1 207 . 51 THR CA C 64.56 0.03 1 208 . 51 THR CB C 68.21 0.06 1 209 . 52 VAL H H 8.149 0.01 1 210 . 52 VAL N N 127.747 0.05 1 211 . 52 VAL C C 174.61 0.02 1 212 . 52 VAL CA C 64.04 0.03 1 213 . 52 VAL CB C 30.7 0.06 1 214 . 53 LEU H H 7.434 0.01 1 215 . 53 LEU N N 125.341 0.05 1 216 . 53 LEU C C 175.68 0.02 1 217 . 53 LEU CA C 51.72 0.03 1 218 . 53 LEU CB C 47.43 0.06 1 219 . 54 GLN H H 9.945 0.01 1 220 . 54 GLN N N 123.712 0.05 1 221 . 54 GLN C C 175.85 0.02 1 222 . 54 GLN CA C 55.06 0.03 1 223 . 54 GLN CB C 26.57 0.06 1 224 . 55 ASP H H 9.239 0.01 1 225 . 55 ASP N N 130.558 0.05 1 226 . 55 ASP C C 176.75 0.02 1 227 . 55 ASP CA C 55.64 0.03 1 228 . 55 ASP CB C 45.31 0.06 1 229 . 56 ARG H H 9.175 0.01 1 230 . 56 ARG N N 122.889 0.05 1 231 . 56 ARG C C 177.45 0.02 1 232 . 56 ARG CA C 58.08 0.03 1 233 . 56 ARG CB C 30.45 0.06 1 234 . 57 GLN H H 9.756 0.01 1 235 . 57 GLN N N 120.779 0.05 1 236 . 57 GLN C C 175.94 0.02 1 237 . 57 GLN CA C 55.73 0.03 1 238 . 57 GLN CB C 30.58 0.06 1 239 . 58 GLU H H 8.886 0.01 1 240 . 58 GLU N N 123.462 0.05 1 241 . 58 GLU C C 176.02 0.02 1 242 . 58 GLU CA C 58.63 0.03 1 243 . 58 GLU CB C 29.63 0.06 1 244 . 59 VAL H H 6.976 0.01 1 245 . 59 VAL N N 108.642 0.05 1 246 . 59 VAL C C 175.62 0.02 1 247 . 59 VAL CA C 61.96 0.03 1 248 . 59 VAL CB C 31.66 0.06 1 249 . 60 LYS H H 7.516 0.01 1 250 . 60 LYS N N 121.564 0.05 1 251 . 60 LYS C C 175.51 0.02 1 252 . 60 LYS CA C 54.4 0.03 1 253 . 60 LYS CB C 31.16 0.06 1 254 . 61 TYR H H 8.449 0.01 1 255 . 61 TYR N N 123.933 0.05 1 256 . 61 TYR C C 175.44 0.02 1 257 . 61 TYR CA C 58 0.03 1 258 . 61 TYR CB C 36.35 0.06 1 259 . 62 GLY H H 8.103 0.01 1 260 . 62 GLY N N 105.612 0.05 1 261 . 62 GLY C C 173.17 0.02 1 262 . 62 GLY CA C 44.52 0.03 1 263 . 63 LEU H H 9.824 0.01 1 264 . 63 LEU N N 124.466 0.05 1 265 . 63 LEU C C 174.26 0.02 1 266 . 63 LEU CA C 51.43 0.03 1 267 . 63 LEU CB C 44.78 0.06 1 268 . 64 PRO C C 177.10 0.02 1 269 . 64 PRO CA C 61.75 0.03 1 270 . 64 PRO CB C 33 0.06 1 271 . 65 VAL H H 9.569 0.01 1 272 . 65 VAL N N 115.834 0.05 1 273 . 65 VAL C C 174.86 0.02 1 274 . 65 VAL CA C 58.39 0.03 1 275 . 65 VAL CB C 35.24 0.06 1 276 . 66 LYS H H 8.552 0.01 1 277 . 66 LYS N N 115.716 0.05 1 278 . 66 LYS C C 173.96 0.02 1 279 . 66 LYS CA C 54.83 0.03 1 280 . 66 LYS CB C 36.82 0.06 1 281 . 67 PHE H H 9.452 0.01 1 282 . 67 PHE N N 120.31 0.05 1 283 . 67 PHE C C 176.117 0.02 1 284 . 67 PHE CA C 56.23 0.03 1 285 . 67 PHE CB C 41.58 0.06 1 286 . 68 VAL H H 8.88 0.01 1 287 . 68 VAL N N 122.657 0.05 1 288 . 68 VAL C C 175.21 0.02 1 289 . 68 VAL CA C 61.41 0.03 1 290 . 68 VAL CB C 36.36 0.06 1 291 . 69 ILE H H 8.608 0.01 1 292 . 69 ILE N N 126.318 0.05 1 293 . 69 ILE C C 175.48 0.02 1 294 . 69 ILE CA C 58.5 0.03 1 295 . 69 ILE CB C 39.33 0.06 1 296 . 75 GLY C C 171.99 0.02 1 297 . 75 GLY CA C 46.22 0.03 1 298 . 76 ILE H H 7.074 0.01 1 299 . 76 ILE N N 118.122 0.05 1 300 . 76 ILE C C 173.77 0.02 1 301 . 76 ILE CA C 59.79 0.03 1 302 . 76 ILE CB C 42.22 0.06 1 303 . 77 ILE H H 8.06 0.01 1 304 . 77 ILE N N 123.153 0.05 1 305 . 77 ILE C C 174.53 0.02 1 306 . 77 ILE CA C 62.06 0.03 1 307 . 77 ILE CB C 37.29 0.06 1 308 . 78 PHE H H 7.892 0.01 1 309 . 78 PHE N N 126.872 0.05 1 310 . 78 PHE C C 177.55 0.02 1 311 . 78 PHE CA C 56.77 0.03 1 312 . 78 PHE CB C 41.83 0.06 1 313 . 79 THR H H 9.214 0.01 1 314 . 79 THR N N 114.344 0.05 1 315 . 79 THR C C 176.56 0.02 1 316 . 79 THR CA C 62.05 0.03 1 317 . 79 THR CB C 69.01 0.06 1 318 . 80 GLY H H 8.878 0.01 1 319 . 80 GLY N N 110.839 0.05 1 320 . 80 GLY C C 174.3 0.02 1 321 . 80 GLY CA C 46.15 0.03 1 322 . 81 THR H H 7.81 0.01 1 323 . 81 THR N N 121.185 0.05 1 324 . 81 THR C C 172.04 0.02 1 325 . 81 THR CA C 62.55 0.03 1 326 . 81 THR CB C 71.02 0.06 1 327 . 82 PRO C C 176.55 0.02 1 328 . 82 PRO CA C 63.25 0.03 1 329 . 82 PRO CB C 33.23 0.06 1 330 . 83 ILE H H 8.854 0.01 1 331 . 83 ILE N N 117.196 0.05 1 332 . 83 ILE C C 175.23 0.02 1 333 . 83 ILE CA C 59.76 0.03 1 334 . 83 ILE CB C 43.96 0.06 1 335 . 84 GLU H H 9.008 0.01 1 336 . 84 GLU N N 117.549 0.05 1 337 . 84 GLU C C 175.4 0.02 1 338 . 84 GLU CA C 54.73 0.03 1 339 . 84 GLU CB C 32.35 0.06 1 340 . 85 ILE H H 8.644 0.01 1 341 . 85 ILE N N 121.082 0.05 1 342 . 85 ILE C C 173.77 0.02 1 343 . 85 ILE CA C 60.78 0.03 1 344 . 85 ILE CB C 40.2 0.06 1 345 . 86 GLU H H 8.362 0.01 1 346 . 86 GLU N N 122.06 0.05 1 347 . 86 GLU C C 176.8 0.02 1 348 . 86 GLU CA C 53.55 0.03 1 349 . 86 GLU CB C 33.67 0.06 1 350 . 87 TYR H H 8.213 0.01 1 351 . 87 TYR N N 118.651 0.05 1 352 . 87 TYR C C 178.04 0.02 1 353 . 87 TYR CA C 57.91 0.03 1 354 . 87 TYR CB C 40.86 0.06 1 355 . 88 ALA H H 8.859 0.01 1 356 . 88 ALA N N 122.193 0.05 1 357 . 88 ALA C C 176.44 0.02 1 358 . 88 ALA CA C 53.94 0.03 1 359 . 88 ALA CB C 19.77 0.06 1 360 . 89 LYS H H 7.547 0.01 1 361 . 89 LYS N N 115.247 0.05 1 362 . 89 LYS C C 173.39 0.02 1 363 . 89 LYS CA C 54.88 0.03 1 364 . 89 LYS CB C 36.35 0.06 1 365 . 90 LYS H H 8.287 0.01 1 366 . 90 LYS N N 116.81 0.05 1 367 . 90 LYS CA C 53.2 0.03 1 368 . 90 LYS CB C 33.96 0.06 1 369 . 93 CYS C C 174.37 0.02 1 370 . 93 CYS CA C 55.68 0.03 1 371 . 93 CYS CB C 40.84 0.06 1 372 . 94 ALA H H 7.722 0.01 1 373 . 94 ALA N N 125.997 0.05 1 374 . 94 ALA C C 177.23 0.02 1 375 . 94 ALA CA C 51.26 0.03 1 376 . 94 ALA CB C 20.17 0.06 1 377 . 95 LYS H H 9.147 0.01 1 378 . 95 LYS N N 121.214 0.05 1 379 . 95 LYS C C 176.32 0.02 1 380 . 95 LYS CA C 57.38 0.03 1 381 . 95 LYS CB C 32.54 0.06 1 382 . 96 SER H H 7.149 0.01 1 383 . 96 SER N N 107.77 0.05 1 384 . 96 SER C C 173.93 0.02 1 385 . 96 SER CA C 56.43 0.03 1 386 . 96 SER CB C 65.59 0.06 1 387 . 97 SER C C 173.68 0.02 1 388 . 97 SER CA C 58.52 0.03 1 389 . 97 SER CB C 64.52 0.06 1 390 . 98 LYS H H 8.235 0.01 1 391 . 98 LYS N N 123.81 0.05 1 392 . 98 LYS C C 177.26 0.02 1 393 . 98 LYS CA C 57.38 0.03 1 394 . 98 LYS CB C 33.28 0.06 1 395 . 99 TRP H H 9.864 0.01 1 396 . 99 TRP N N 126.334 0.05 1 397 . 99 TRP C C 176.26 0.02 1 398 . 99 TRP CA C 57.54 0.03 1 399 . 99 TRP CB C 31.71 0.06 1 400 . 100 LEU H H 10.199 0.01 1 401 . 100 LEU N N 123.347 0.05 1 402 . 100 LEU C C 174.73 0.02 1 403 . 100 LEU CA C 53.94 0.03 1 404 . 100 LEU CB C 44.35 0.06 1 405 . 101 VAL H H 7.546 0.01 1 406 . 101 VAL N N 118.341 0.05 1 407 . 101 VAL C C 173.72 0.02 1 408 . 101 VAL CA C 60.44 0.03 1 409 . 101 VAL CB C 35.15 0.06 1 410 . 102 PHE H H 9.469 0.01 1 411 . 102 PHE N N 125.341 0.05 1 412 . 102 PHE C C 172.74 0.02 1 413 . 102 PHE CA C 54.14 0.03 1 414 . 102 PHE CB C 42.91 0.06 1 415 . 103 VAL H H 8.588 0.01 1 416 . 103 VAL N N 122.278 0.05 1 417 . 103 VAL C C 174.34 0.02 1 418 . 103 VAL CA C 63.14 0.03 1 419 . 103 VAL CB C 31.76 0.06 1 420 . 104 ASP H H 8.286 0.01 1 421 . 104 ASP N N 127.966 0.05 1 422 . 104 ASP C C 177.04 0.02 1 423 . 104 ASP CA C 53.55 0.03 1 424 . 104 ASP CB C 43.59 0.06 1 425 . 105 ASN H H 8.881 0.01 1 426 . 105 ASN N N 124.004 0.05 1 427 . 105 ASN C C 175.96 0.02 1 428 . 105 ASN CA C 55.14 0.03 1 429 . 105 ASN CB C 39.35 0.06 1 430 . 106 VAL H H 8.662 0.01 1 431 . 106 VAL N N 121.544 0.05 1 432 . 106 VAL C C 178.18 0.02 1 433 . 106 VAL CA C 66.08 0.03 1 434 . 106 VAL CB C 32.18 0.06 1 435 . 107 ILE H H 7.031 0.01 1 436 . 107 ILE N N 108.217 0.05 1 437 . 107 ILE C C 175.14 0.02 1 438 . 107 ILE CA C 60.81 0.03 1 439 . 107 ILE CB C 38.85 0.06 1 440 . 108 GLN H H 7.862 0.01 1 441 . 108 GLN N N 118.315 0.05 1 442 . 108 GLN C C 175.3 0.02 1 443 . 108 GLN CA C 56.74 0.03 1 444 . 108 GLN CB C 25.66 0.06 1 445 . 109 LYS H H 7.163 0.01 1 446 . 109 LYS N N 113.809 0.05 1 447 . 109 LYS C C 174.13 0.02 1 448 . 109 LYS CA C 53.69 0.03 1 449 . 109 LYS CB C 37.28 0.06 1 450 . 111 CYS H H 8.727 0.01 1 451 . 111 CYS N N 120.54 0.05 1 452 . 111 CYS C C 171.78 0.02 1 453 . 111 CYS CA C 57.15 0.03 1 454 . 111 CYS CB C 31.71 0.06 1 455 . 112 VAL H H 8.417 0.01 1 456 . 112 VAL N N 120.966 0.05 1 457 . 112 VAL C C 176.67 0.02 1 458 . 112 VAL CA C 62.55 0.03 1 459 . 112 VAL CB C 32.39 0.06 1 460 . 113 GLY H H 8.82 0.01 1 461 . 113 GLY N N 116.709 0.05 1 462 . 113 GLY C C 172.07 0.02 1 463 . 113 GLY CA C 44.98 0.03 1 464 . 114 ILE H H 9.181 0.01 1 465 . 114 ILE N N 110.904 0.05 1 466 . 114 ILE C C 177.31 0.02 1 467 . 114 ILE CA C 60.07 0.03 1 468 . 114 ILE CB C 40.93 0.06 1 469 . 115 GLY H H 7.509 0.01 1 470 . 115 GLY N N 103.254 0.05 1 471 . 115 GLY C C 173 0.02 1 472 . 115 GLY CA C 45.69 0.03 1 473 . 116 GLY H H 8.499 0.01 1 474 . 116 GLY N N 109.591 0.05 1 475 . 116 GLY C C 171.69 0.02 1 476 . 116 GLY CA C 44.1 0.03 1 477 . 118 GLU C C 178.14 0.02 1 478 . 118 GLU CA C 59.17 0.03 1 479 . 118 GLU CB C 29.3 0.06 1 480 . 119 ASN H H 8.649 0.01 1 481 . 119 ASN N N 114.603 0.05 1 482 . 119 ASN C C 172.08 0.02 1 483 . 119 ASN CA C 55.49 0.03 1 484 . 119 ASN CB C 42 0.06 1 485 . 120 TYR H H 7.505 0.01 1 486 . 120 TYR N N 116.591 0.05 1 487 . 120 TYR C C 172.5 0.02 1 488 . 120 TYR CA C 55.32 0.03 1 489 . 120 TYR CB C 40.27 0.06 1 490 . 122 GLY C C 173.80 0.02 1 491 . 122 GLY CA C 45.98 0.03 1 492 . 123 VAL H H 7.948 0.01 1 493 . 123 VAL N N 122.935 0.05 1 494 . 123 VAL C C 174.73 0.02 1 495 . 123 VAL CA C 61.25 0.03 1 496 . 123 VAL CB C 35.58 0.06 1 497 . 124 GLN H H 9.195 0.01 1 498 . 124 GLN N N 127.091 0.05 1 499 . 124 GLN C C 175.41 0.02 1 500 . 124 GLN CA C 56.22 0.03 1 501 . 124 GLN CB C 30.07 0.06 1 502 . 125 THR H H 8.253 0.01 1 503 . 125 THR N N 114.862 0.05 1 504 . 125 THR C C 174.27 0.02 1 505 . 125 THR CA C 59.96 0.03 1 506 . 125 THR CB C 71.42 0.06 1 507 . 126 LEU H H 8.896 0.01 1 508 . 126 LEU N N 121.403 0.05 1 509 . 126 LEU C C 176.76 0.02 1 510 . 126 LEU CA C 53.64 0.03 1 511 . 126 LEU CB C 44.2 0.06 1 512 . 127 SER H H 8.745 0.01 1 513 . 127 SER N N 118.341 0.05 1 514 . 127 SER C C 174.08 0.02 1 515 . 127 SER CA C 57.59 0.03 1 516 . 127 SER CB C 65.2 0.06 1 517 . 128 GLY H H 8.438 0.01 1 518 . 128 GLY N N 111.997 0.05 1 519 . 128 GLY C C 170.92 0.02 1 520 . 128 GLY CA C 46.04 0.03 1 521 . 129 LEU H H 7.015 0.01 1 522 . 129 LEU N N 118.778 0.05 1 523 . 129 LEU C C 175.4 0.02 1 524 . 129 LEU CA C 53.68 0.03 1 525 . 129 LEU CB C 46.49 0.06 1 526 . 130 PHE H H 8.568 0.01 1 527 . 130 PHE N N 118.314 0.05 1 528 . 130 PHE C C 175.01 0.02 1 529 . 130 PHE CA C 58.13 0.03 1 530 . 130 PHE CB C 43.5 0.06 1 531 . 131 LYS H H 8.596 0.01 1 532 . 131 LYS N N 113.747 0.05 1 533 . 131 LYS C C 173.39 0.02 1 534 . 131 LYS CA C 56.22 0.03 1 535 . 131 LYS CB C 36.34 0.06 1 536 . 132 ILE H H 9.713 0.01 1 537 . 132 ILE N N 122.06 0.05 1 538 . 132 ILE C C 175.8 0.02 1 539 . 132 ILE CA C 60.65 0.03 1 540 . 132 ILE CB C 40.47 0.06 1 541 . 133 GLU H H 9.079 0.01 1 542 . 133 GLU N N 123.731 0.05 1 543 . 133 GLU C C 176.36 0.02 1 544 . 133 GLU CA C 53.71 0.03 1 545 . 133 GLU CB C 34.14 0.06 1 546 . 134 LYS H H 9.452 0.01 1 547 . 134 LYS N N 121.336 0.05 1 548 . 134 LYS C C 176.63 0.02 1 549 . 134 LYS CA C 57.59 0.03 1 550 . 134 LYS CB C 32.28 0.06 1 551 . 135 HIS H H 8.377 0.01 1 552 . 135 HIS N N 124.776 0.05 1 553 . 135 HIS C C 177.75 0.02 1 554 . 135 HIS CA C 60.57 0.03 1 555 . 135 HIS CB C 31.76 0.06 1 556 . 136 GLU H H 9.394 0.01 1 557 . 136 GLU N N 128.439 0.05 1 558 . 136 GLU C C 176.99 0.02 1 559 . 136 GLU CA C 59.95 0.03 1 560 . 136 GLU CB C 28.21 0.06 1 561 . 137 SER H H 8.96 0.01 1 562 . 137 SER N N 118.356 0.05 1 563 . 137 SER C C 176.47 0.02 1 564 . 137 SER CA C 60.95 0.03 1 565 . 137 SER CB C 65.04 0.06 1 566 . 138 GLY H H 8.227 0.01 1 567 . 138 GLY N N 110.047 0.05 1 568 . 138 GLY C C 172.8 0.02 1 569 . 138 GLY CA C 45.05 0.03 1 570 . 139 PHE H H 8.043 0.01 1 571 . 139 PHE N N 121.622 0.05 1 572 . 139 PHE C C 174.22 0.02 1 573 . 139 PHE CA C 56.78 0.03 1 574 . 139 PHE CB C 41.32 0.06 1 575 . 140 GLY H H 7.992 0.01 1 576 . 140 GLY N N 111.997 0.05 1 577 . 140 GLY C C 172.47 0.02 1 578 . 140 GLY CA C 43.42 0.03 1 579 . 141 TYR H H 9.05 0.01 1 580 . 141 TYR N N 117.028 0.05 1 581 . 141 TYR C C 173.12 0.02 1 582 . 141 TYR CA C 58.46 0.03 1 583 . 141 TYR CB C 43.76 0.06 1 584 . 142 LYS H H 9.493 0.01 1 585 . 142 LYS N N 115.935 0.05 1 586 . 142 LYS C C 174.44 0.02 1 587 . 142 LYS CA C 54.86 0.03 1 588 . 142 LYS CB C 36.76 0.06 1 589 . 143 LEU H H 10.484 0.01 1 590 . 143 LEU N N 122.06 0.05 1 591 . 143 LEU C C 176.81 0.02 1 592 . 143 LEU CA C 53.62 0.03 1 593 . 143 LEU CB C 44.25 0.06 1 594 . 144 GLY H H 9.012 0.01 1 595 . 144 GLY N N 107.507 0.05 1 596 . 144 GLY C C 171.25 0.02 1 597 . 144 GLY CA C 44.27 0.03 1 598 . 145 PHE H H 9.345 0.01 1 599 . 145 PHE N N 118.997 0.05 1 600 . 145 PHE C C 173.97 0.02 1 601 . 145 PHE CA C 57.61 0.03 1 602 . 145 PHE CB C 44.49 0.06 1 603 . 146 CYS H H 8.489 0.01 1 604 . 146 CYS N N 127.31 0.05 1 605 . 146 CYS C C 174.09 0.02 1 606 . 146 CYS CA C 54 0.03 1 607 . 146 CYS CB C 45.68 0.06 1 608 . 147 VAL H H 8.888 0.01 1 609 . 147 VAL N N 128.622 0.05 1 610 . 147 VAL C C 176.5 0.02 1 611 . 147 VAL CA C 63.12 0.03 1 612 . 147 VAL CB C 32.78 0.06 1 613 . 148 LYS H H 8.784 0.01 1 614 . 148 LYS N N 129.694 0.05 1 615 . 148 LYS C C 177.79 0.02 1 616 . 148 LYS CA C 58.69 0.03 1 617 . 148 LYS CB C 32.61 0.06 1 618 . 149 GLY C C 173.99 0.02 1 619 . 149 GLY CA C 45.28 0.03 1 620 . 150 SER H H 7.975 0.01 5 621 . 150 SER N N 116.372 0.05 5 622 . 150 SER C C 174.26 0.02 5 623 . 150 SER CA C 55.64 0.03 5 624 . 150 SER CB C 65.52 0.06 5 625 . 151 PRO C C 176.53 0.02 1 626 . 151 PRO CA C 64.07 0.03 1 627 . 151 PRO CB C 32.46 0.06 1 628 . 152 THR H H 7.67 0.01 9 629 . 152 THR N N 112.449 0.05 9 630 . 152 THR C C 174.07 0.02 9 631 . 152 THR CA C 61.14 0.03 9 632 . 152 THR CB C 71.03 0.06 9 633 . 153 CYS C C 172.93 0.02 1 634 . 153 CYS CA C 56.98 0.03 1 635 . 153 CYS CB C 50.21 0.06 1 636 . 154 LEU H H 8.794 0.01 1 637 . 154 LEU N N 123.591 0.05 1 638 . 154 LEU C C 175.73 0.02 1 639 . 154 LEU CA C 54.17 0.03 1 640 . 154 LEU CB C 46.49 0.06 1 641 . 155 ASP H H 8.181 0.01 1 642 . 155 ASP N N 120.446 0.05 1 643 . 155 ASP C C 174.82 0.02 1 644 . 155 ASP CA C 54.78 0.03 1 645 . 155 ASP CB C 43.33 0.06 1 646 . 156 VAL H H 8.59 0.01 1 647 . 156 VAL N N 118.997 0.05 1 648 . 156 VAL C C 177.25 0.02 1 649 . 156 VAL CA C 62.29 0.03 1 650 . 156 VAL CB C 32.15 0.06 1 651 . 157 GLY H H 9.802 0.01 1 652 . 157 GLY N N 120.591 0.05 1 653 . 157 GLY C C 171.33 0.02 1 654 . 157 GLY CA C 44.18 0.03 1 655 . 158 ARG H H 8.354 0.01 1 656 . 158 ARG N N 115.06 0.05 1 657 . 158 ARG C C 177.04 0.02 1 658 . 158 ARG CA C 54.64 0.03 1 659 . 158 ARG CB C 35.97 0.06 1 660 . 159 PHE H H 8.462 0.01 1 661 . 159 PHE N N 120.538 0.05 1 662 . 159 PHE CA C 57.95 0.03 1 663 . 159 PHE CB C 42.66 0.06 1 664 . 160 ASP C C 173.43 0.02 1 665 . 160 ASP CA C 53.57 0.03 1 666 . 160 ASP CB C 41.83 0.06 1 667 . 161 ASN H H 9.311 0.01 1 668 . 161 ASN N N 126.872 0.05 1 669 . 161 ASN C C 175.07 0.02 1 670 . 161 ASN CA C 52.1 0.03 1 671 . 161 ASN CB C 41.15 0.06 1 672 . 162 ASP H H 9.056 0.01 1 673 . 162 ASP N N 114.963 0.05 1 674 . 162 ASP C C 176.06 0.02 1 675 . 162 ASP CA C 56.29 0.03 1 676 . 162 ASP CB C 40.15 0.06 1 677 . 163 GLU H H 7.347 0.01 1 678 . 163 GLU N N 114.814 0.05 1 679 . 163 GLU C C 177 0.02 1 680 . 163 GLU CA C 55.8 0.03 1 681 . 163 GLU CB C 27.9 0.06 1 682 . 164 ASP C C 176.26 0.02 1 683 . 164 ASP CA C 56.95 0.03 1 684 . 164 ASP CB C 41.37 0.06 1 685 . 165 GLY H H 7.088 0.01 1 686 . 165 GLY N N 103.146 0.05 1 687 . 165 GLY C C 172.08 0.02 1 688 . 165 GLY CA C 43.57 0.03 1 689 . 166 ARG H H 8.888 0.01 1 690 . 166 ARG N N 118.997 0.05 1 691 . 166 ARG C C 176.25 0.02 1 692 . 166 ARG CA C 57.25 0.03 1 693 . 166 ARG CB C 31.89 0.06 1 694 . 167 ARG H H 8.619 0.01 1 695 . 167 ARG N N 118.557 0.05 1 696 . 167 ARG C C 175.81 0.02 1 697 . 167 ARG CA C 56.01 0.03 1 698 . 168 LEU H H 8.788 0.01 1 699 . 168 LEU N N 121.94 0.05 1 700 . 168 LEU C C 175.74 0.02 1 701 . 168 LEU CA C 54.4 0.03 1 702 . 168 LEU CB C 42.42 0.06 1 703 . 169 ASN H H 8.452 0.01 1 704 . 169 ASN N N 118.934 0.05 1 705 . 169 ASN C C 174.04 0.02 1 706 . 169 ASN CA C 51 0.03 1 707 . 169 ASN CB C 43.14 0.06 1 708 . 170 LEU H H 8.514 0.01 1 709 . 170 LEU N N 119.216 0.05 1 710 . 170 LEU C C 177.77 0.02 1 711 . 170 LEU CA C 54.51 0.03 1 712 . 170 LEU CB C 40.45 0.06 1 713 . 171 THR H H 9.416 0.01 1 714 . 171 THR N N 119.148 0.05 1 715 . 171 THR C C 171.11 0.02 1 716 . 171 THR CA C 59.94 0.03 1 717 . 171 THR CB C 71.33 0.06 1 718 . 174 GLU C C 176.37 0.02 1 719 . 174 GLU CA C 57.72 0.03 1 720 . 174 GLU CB C 30.08 0.06 1 721 . 175 SER H H 8.597 0.01 1 722 . 175 SER N N 120.254 0.05 1 723 . 175 SER C C 174.45 0.02 1 724 . 175 SER CA C 58.88 0.03 1 725 . 175 SER CB C 65.88 0.06 1 726 . 176 PHE H H 9.291 0.01 1 727 . 176 PHE N N 121.841 0.05 1 728 . 176 PHE C C 173.08 0.02 1 729 . 176 PHE CA C 54.25 0.03 1 730 . 176 PHE CB C 39.14 0.06 1 731 . 177 GLN H H 8.52 0.01 1 732 . 177 GLN N N 131.68 0.05 1 733 . 177 GLN C C 175.58 0.02 1 734 . 177 GLN CA C 55.34 0.03 1 735 . 177 GLN CB C 29.29 0.06 1 736 . 178 VAL H H 9.24 0.01 1 737 . 178 VAL N N 124.053 0.05 1 738 . 178 VAL C C 174.58 0.02 1 739 . 178 VAL CA C 59.75 0.03 1 740 . 178 VAL CB C 36.7 0.06 1 741 . 179 VAL H H 8.538 0.01 1 742 . 179 VAL N N 111.56 0.05 1 743 . 179 VAL C C 172.96 0.02 1 744 . 179 VAL CA C 59.18 0.03 1 745 . 179 VAL CB C 36.44 0.06 1 746 . 180 PHE H H 8.38 0.01 1 747 . 180 PHE N N 116.372 0.05 1 748 . 180 PHE C C 175.18 0.02 1 749 . 180 PHE CA C 56.2 0.03 1 750 . 180 PHE CB C 42.81 0.06 1 751 . 181 ILE H H 8.916 0.01 1 752 . 181 ILE N N 121.4 0.05 1 753 . 181 ILE C C 175.8 0.02 1 754 . 181 ILE CA C 59.94 0.03 1 755 . 181 ILE CB C 42.28 0.06 1 756 . 182 GLN H H 9.917 0.01 1 757 . 182 GLN N N 129.773 0.05 1 758 . 182 GLN C C 176.12 0.02 1 759 . 182 GLN CA C 58.52 0.03 1 760 . 182 GLN CB C 28.82 0.06 1 761 . 183 ALA H H 8.244 0.01 1 762 . 183 ALA N N 129.483 0.05 1 763 . 183 ALA C C 177.41 0.02 1 764 . 183 ALA CA C 52.76 0.03 1 765 . 183 ALA CB C 19.38 0.06 1 766 . 184 GLU H H 8.37 0.01 1 767 . 184 GLU N N 120.307 0.05 1 768 . 184 GLU C C 175.99 0.02 1 769 . 184 GLU CA C 56.17 0.03 1 770 . 184 GLU CB C 30.89 0.06 1 771 . 185 ALA H H 8.316 0.01 1 772 . 185 ALA N N 124.655 0.05 1 773 . 185 ALA C C 177.51 0.02 1 774 . 185 ALA CA C 52.91 0.03 1 775 . 185 ALA CB C 19.63 0.06 1 776 . 186 ASN C C 175.12 0.02 1 777 . 186 ASN CA C 53.7 0.03 1 778 . 187 ASP H H 8.327 0.01 1 779 . 187 ASP N N 121.098 0.05 1 780 . 187 ASP C C 176.37 0.02 1 781 . 187 ASP CA C 55.11 0.03 1 782 . 187 ASP CB C 42.11 0.06 1 783 . 188 ALA H H 8.219 0.01 1 784 . 188 ALA N N 123.838 0.05 1 785 . 188 ALA C C 175.37 0.02 1 786 . 188 ALA CA C 53.52 0.03 1 787 . 188 ALA CB C 19.67 0.06 1 788 . 189 GLU H H 8.258 0.01 1 789 . 189 GLU N N 118.5 0.05 1 790 . 189 GLU C C 176.66 0.02 1 791 . 189 GLU CA C 57.14 0.03 1 792 . 189 GLU CB C 30.35 0.06 1 793 . 190 PHE H H 8.041 0.01 1 794 . 190 PHE N N 120.335 0.05 1 795 . 190 PHE C C 175.8 0.02 1 796 . 190 PHE CA C 58.43 0.03 1 797 . 190 PHE CB C 40.08 0.06 1 798 . 191 ILE H H 7.952 0.01 1 799 . 191 ILE N N 122.5 0.05 1 800 . 191 ILE C C 175.93 0.02 1 801 . 191 ILE CA C 61.19 0.03 1 802 . 191 ILE CB C 38.77 0.06 1 803 . 192 LYS H H 8.192 0.01 1 804 . 192 LYS N N 124.958 0.05 1 805 . 192 LYS C C 176.56 0.02 1 806 . 192 LYS CA C 56.8 0.03 1 807 . 192 LYS CB C 33.38 0.06 1 808 . 194 VAL H H 8.146 0.01 1 809 . 194 VAL N N 122.06 0.05 1 810 . 194 VAL C C 175.32 0.02 1 811 . 194 VAL CA C 62.62 0.03 1 812 . 194 VAL CB C 33.3 0.06 1 813 . 195 VAL H H 7.688 0.01 1 814 . 195 VAL N N 127.016 0.05 1 815 . 195 VAL C C 180.97 0.02 1 816 . 195 VAL CA C 63.85 0.03 1 817 . 195 VAL CB C 33.89 0.06 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 624 '623,622,621,620' stop_ save_