data_4952 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The UBX Domain: A Widespread Ubquitin-like Module ; _BMRB_accession_number 4952 _BMRB_flat_file_name bmr4952.str _Entry_type original _Submission_date 2001-02-01 _Accession_date 2001-02-01 _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 Buchberger Alex . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 431 "13C chemical shifts" 283 "15N chemical shifts" 87 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-09 original author . stop_ _Original_release_date 2001-03-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The UBX Domain: A Widespread Ubquitin-like Module' _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Buchberger Alex . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_faf1 _Saveframe_category molecular_system _Mol_system_name 'UBX domain of fas accociated factor 1' _Abbreviation_common faf1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ubx domain' $faf1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state momomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_faf1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'fas accociated factor 1' _Abbreviation_common faf1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; GSEAIRLSLEQALPPEPKEE NAEPVSKLRIRTPSGEFLER RFLASNKLQIVFDFVASKGF PWDEYKLLSTFPRRDVTQLD PNKSLLEVKLFPQETLFLEA KE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 GLU 4 ALA 5 ILE 6 ARG 7 LEU 8 SER 9 LEU 10 GLU 11 GLN 12 ALA 13 LEU 14 PRO 15 PRO 16 GLU 17 PRO 18 LYS 19 GLU 20 GLU 21 ASN 22 ALA 23 GLU 24 PRO 25 VAL 26 SER 27 LYS 28 LEU 29 ARG 30 ILE 31 ARG 32 THR 33 PRO 34 SER 35 GLY 36 GLU 37 PHE 38 LEU 39 GLU 40 ARG 41 ARG 42 PHE 43 LEU 44 ALA 45 SER 46 ASN 47 LYS 48 LEU 49 GLN 50 ILE 51 VAL 52 PHE 53 ASP 54 PHE 55 VAL 56 ALA 57 SER 58 LYS 59 GLY 60 PHE 61 PRO 62 TRP 63 ASP 64 GLU 65 TYR 66 LYS 67 LEU 68 LEU 69 SER 70 THR 71 PHE 72 PRO 73 ARG 74 ARG 75 ASP 76 VAL 77 THR 78 GLN 79 LEU 80 ASP 81 PRO 82 ASN 83 LYS 84 SER 85 LEU 86 LEU 87 GLU 88 VAL 89 LYS 90 LEU 91 PHE 92 PRO 93 GLN 94 GLU 95 THR 96 LEU 97 PHE 98 LEU 99 GLU 100 ALA 101 LYS 102 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1H8C "Ubx Domain From Human Faf1" 80.39 82 100.00 100.00 1.06e-49 PDB 3QC8 "Crystal Structure Of Faf1 Ubx Domain In Complex With P97VCP N DOMAIN Reveals The Conserved Fcisp Touch-Turn Motif Of Ubx Domain" 78.43 84 100.00 100.00 5.79e-48 PDB 3QCA "Crystal Structure Of Faf1 Ubx Domain In Complex With P97VCP N DOMAIN Reveals The Conserved Fcisp Touch-Turn Motif Of Ubx Domain" 78.43 84 100.00 100.00 5.79e-48 PDB 3QQ8 "Crystal Structure Of P97-N In Complex With Faf1-Ubx" 81.37 85 100.00 100.00 1.47e-50 PDB 3QX1 "Crystal Structure Of Faf1 Ubx Domain" 80.39 84 97.56 98.78 1.83e-48 PDB 3R3M "Crystal Structure Of The Faf1 Ubx Domain" 81.37 85 100.00 100.00 1.47e-50 DBJ BAF85529 "unnamed protein product [Homo sapiens]" 98.04 650 100.00 100.00 9.44e-59 DBJ BAG11065 "FAS-associated factor 1 [synthetic construct]" 98.04 650 100.00 100.00 8.10e-59 DBJ BAG52940 "unnamed protein product [Homo sapiens]" 72.55 464 98.65 100.00 1.33e-41 DBJ BAG57107 "unnamed protein product [Homo sapiens]" 98.04 408 100.00 100.00 6.11e-61 EMBL CAB63755 "hypothetical protein [Homo sapiens]" 98.04 554 100.00 100.00 1.96e-59 EMBL CAB67705 "Fas-associated factor, FAF1 [Homo sapiens]" 98.04 650 100.00 100.00 8.10e-59 GB AAA92091 "FAF1 [Mus musculus]" 98.04 649 97.00 99.00 7.13e-57 GB AAD27713 "CGI-03 protein [Homo sapiens]" 98.04 650 100.00 100.00 8.10e-59 GB AAD51876 "Fas associated factor 1 [Homo sapiens]" 98.04 490 100.00 100.00 1.45e-59 GB AAD51886 "fas-associated factor 1 [Homo sapiens]" 98.04 650 100.00 100.00 9.64e-59 GB AAH04970 "Fas (TNFRSF6) associated factor 1 [Homo sapiens]" 98.04 650 100.00 100.00 8.10e-59 REF NP_001039783 "FAS-associated factor 1 [Bos taurus]" 98.04 650 98.00 99.00 1.36e-56 REF NP_001252796 "FAS-associated factor 1 [Macaca mulatta]" 98.04 650 99.00 100.00 5.38e-58 REF NP_008982 "FAS-associated factor 1 [Homo sapiens]" 98.04 650 100.00 100.00 8.10e-59 REF NP_032009 "FAS-associated factor 1 [Mus musculus]" 98.04 649 97.00 99.00 8.23e-57 REF XP_001137725 "PREDICTED: FAS-associated factor 1 [Pan troglodytes]" 98.04 650 100.00 100.00 7.77e-59 SP P54731 "RecName: Full=FAS-associated factor 1 [Mus musculus]" 98.04 649 97.00 99.00 8.23e-57 SP Q9UNN5 "RecName: Full=FAS-associated factor 1; Short=hFAF1; AltName: Full=UBX domain-containing protein 12; AltName: Full=UBX domain-co" 98.04 650 100.00 100.00 8.10e-59 TPG DAA31193 "TPA: Fas (TNFRSF6) associated factor 1 [Bos taurus]" 98.04 650 98.00 99.00 1.36e-56 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $faf1 human 9606 Eukaryota Metazoa Homo sapien 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 $faf1 '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 _Isotopic_labeling $faf1 5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.2 n/a temperature 310 0.5 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_citation_label _Correction_value_citation_label . C 13 . ppm . . . . . . $entry_citation $entry_citation . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_set_1. _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ubx 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 . 3 GLU HA H 4.18 0.015 1 2 . 3 GLU HB2 H 1.97 0.015 1 3 . 3 GLU HB3 H 1.97 0.015 1 4 . 3 GLU C C 174.62 0.15 1 5 . 3 GLU CA C 55.58 0.15 1 6 . 3 GLU CB C 27.44 0.15 1 7 . 4 ALA H H 8.14 0.015 1 8 . 4 ALA HA H 4.17 0.015 1 9 . 4 ALA HB H 1.35 0.015 1 10 . 4 ALA C C 176.65 0.15 1 11 . 4 ALA CA C 51.38 0.15 1 12 . 4 ALA CB C 16.71 0.15 1 13 . 4 ALA N N 123.27 0.2 1 14 . 5 ILE H H 7.75 0.015 1 15 . 5 ILE HA H 3.95 0.015 1 16 . 5 ILE HB H 1.84 0.015 1 17 . 5 ILE HG12 H 1.45 0.015 2 18 . 5 ILE HG13 H 1.14 0.015 2 19 . 5 ILE HG2 H 0.83 0.015 1 20 . 5 ILE HD1 H 0.76 0.015 1 21 . 5 ILE C C 174.78 0.15 1 22 . 5 ILE CA C 60.19 0.15 1 23 . 5 ILE CB C 35.98 0.15 1 24 . 5 ILE CD1 C 10.65 0.15 1 25 . 5 ILE N N 119.15 0.2 1 26 . 6 ARG H H 8.09 0.015 1 27 . 6 ARG HA H 4.12 0.015 1 28 . 6 ARG HB2 H 1.82 0.015 2 29 . 6 ARG HB3 H 1.17 0.015 2 30 . 6 ARG C C 173.23 0.15 1 31 . 6 ARG CA C 55.55 0.15 1 32 . 6 ARG CB C 28.27 0.15 1 33 . 6 ARG N N 123.33 0.2 1 34 . 7 LEU H H 8.17 0.015 1 35 . 7 LEU HA H 4.22 0.015 1 36 . 7 LEU HB2 H 1.59 0.015 1 37 . 7 LEU HB3 H 1.59 0.015 1 38 . 7 LEU C C 176.03 0.15 1 39 . 7 LEU CA C 54.08 0.15 1 40 . 7 LEU CB C 40.11 0.15 1 41 . 7 LEU N N 121.53 0.2 1 42 . 8 SER H H 8.04 0.015 1 43 . 8 SER HA H 4.33 0.015 1 44 . 8 SER HB2 H 3.89 0.015 1 45 . 8 SER HB3 H 3.89 0.015 1 46 . 8 SER C C 173.68 0.15 1 47 . 8 SER CA C 57.34 0.15 1 48 . 8 SER CB C 61.16 0.15 1 49 . 8 SER N N 115.59 0.2 1 50 . 9 LEU H H 8.06 0.015 1 51 . 9 LEU HA H 4.21 0.015 1 52 . 9 LEU HB2 H 1.72 0.015 2 53 . 9 LEU HB3 H 1.52 0.015 2 54 . 9 LEU C C 176.40 0.15 1 55 . 9 LEU CA C 54.31 0.15 1 56 . 9 LEU CB C 40.15 0.15 1 57 . 9 LEU N N 123.06 0.2 1 58 . 10 GLU H H 8.27 0.015 1 59 . 10 GLU HA H 4.07 0.015 1 60 . 10 GLU HB2 H 2.06 0.015 1 61 . 10 GLU HB3 H 2.06 0.015 1 62 . 10 GLU HG2 H 2.29 0.015 1 63 . 10 GLU HG3 H 2.29 0.015 1 64 . 10 GLU C C 175.70 0.15 1 65 . 10 GLU CA C 56.14 0.15 1 66 . 10 GLU CB C 27.89 0.15 1 67 . 10 GLU N N 119.56 0.2 1 68 . 11 GLN H H 8.05 0.015 1 69 . 11 GLN HA H 4.19 0.015 1 70 . 11 GLN HB2 H 2.05 0.015 1 71 . 11 GLN HB3 H 2.05 0.015 1 72 . 11 GLN HG2 H 2.38 0.015 1 73 . 11 GLN HG3 H 2.38 0.015 1 74 . 11 GLN C C 173.69 0.15 1 75 . 11 GLN CA C 54.36 0.15 1 76 . 11 GLN CB C 27.04 0.15 1 77 . 11 GLN N N 118.15 0.2 1 78 . 12 ALA H H 7.78 0.015 1 79 . 12 ALA HA H 4.32 0.015 1 80 . 12 ALA HB H 1.42 0.015 1 81 . 12 ALA C C 175.42 0.15 1 82 . 12 ALA CA C 49.89 0.15 1 83 . 12 ALA CB C 17.28 0.15 1 84 . 12 ALA N N 122.44 0.2 1 85 . 13 LEU H H 7.66 0.015 1 86 . 13 LEU HA H 4.59 0.015 1 87 . 13 LEU HB2 H 1.71 0.015 2 88 . 13 LEU HB3 H 1.46 0.015 2 89 . 13 LEU CA C 51.07 0.15 1 90 . 13 LEU N N 121.32 0.2 1 91 . 17 PRO HA H 4.37 0.015 1 92 . 17 PRO HB2 H 2.14 0.015 2 93 . 17 PRO HB3 H 1.79 0.015 2 94 . 17 PRO C C 174.34 0.15 1 95 . 17 PRO CA C 60.43 0.15 1 96 . 17 PRO CB C 29.95 0.15 1 97 . 18 LYS H H 8.39 0.015 1 98 . 18 LYS HA H 4.17 0.015 1 99 . 18 LYS HB2 H 1.91 0.015 2 100 . 18 LYS HB3 H 1.70 0.015 2 101 . 18 LYS C C 174.75 0.15 1 102 . 18 LYS CA C 53.92 0.15 1 103 . 18 LYS CB C 30.98 0.15 1 104 . 18 LYS N N 121.49 0.2 1 105 . 19 GLU H H 8.57 0.015 1 106 . 19 GLU HA H 3.96 0.015 1 107 . 19 GLU HB2 H 1.92 0.015 1 108 . 19 GLU HB3 H 1.92 0.015 1 109 . 19 GLU HG2 H 2.16 0.015 1 110 . 19 GLU HG3 H 2.16 0.015 1 111 . 19 GLU C C 174.79 0.15 1 112 . 19 GLU CA C 56.29 0.15 1 113 . 19 GLU CB C 27.82 0.15 1 114 . 19 GLU N N 120.67 0.2 1 115 . 20 GLU H H 8.32 0.015 1 116 . 20 GLU HA H 4.20 0.015 1 117 . 20 GLU HB2 H 1.94 0.015 1 118 . 20 GLU HB3 H 1.94 0.015 1 119 . 20 GLU C C 173.61 0.15 1 120 . 20 GLU CA C 54.33 0.15 1 121 . 20 GLU CB C 26.99 0.15 1 122 . 20 GLU N N 118.26 0.2 1 123 . 21 ASN H H 7.96 0.015 1 124 . 21 ASN HA H 4.58 0.015 1 125 . 21 ASN HB2 H 2.84 0.015 2 126 . 21 ASN HB3 H 2.74 0.015 2 127 . 21 ASN C C 172.71 0.15 1 128 . 21 ASN CA C 51.56 0.15 1 129 . 21 ASN CB C 38.02 0.15 1 130 . 21 ASN N N 120.95 0.2 1 131 . 22 ALA H H 8.38 0.015 1 132 . 22 ALA HA H 4.23 0.015 1 133 . 22 ALA HB H 1.39 0.015 1 134 . 22 ALA C C 175.79 0.15 1 135 . 22 ALA CA C 51.22 0.15 1 136 . 22 ALA CB C 17.13 0.15 1 137 . 22 ALA N N 124.79 0.2 1 138 . 23 GLU H H 8.02 0.015 1 139 . 23 GLU HA H 4.58 0.015 1 140 . 23 GLU HB2 H 1.79 0.015 1 141 . 23 GLU HB3 H 1.79 0.015 1 142 . 23 GLU HG2 H 2.20 0.015 1 143 . 23 GLU HG3 H 2.20 0.015 1 144 . 23 GLU CA C 52.23 0.15 1 145 . 23 GLU N N 118.69 0.2 1 146 . 24 PRO HA H 4.29 0.015 1 147 . 24 PRO HB2 H 2.28 0.015 2 148 . 24 PRO HB3 H 1.78 0.015 2 149 . 24 PRO C C 176.80 0.15 1 150 . 24 PRO CA C 61.50 0.15 1 151 . 24 PRO CB C 29.66 0.15 1 152 . 25 VAL H H 8.53 0.015 1 153 . 25 VAL HA H 4.72 0.015 1 154 . 25 VAL HB H 1.99 0.015 1 155 . 25 VAL HG1 H 0.94 0.015 2 156 . 25 VAL HG2 H 0.85 0.015 2 157 . 25 VAL C C 172.74 0.15 1 158 . 25 VAL CA C 59.01 0.15 1 159 . 25 VAL CB C 33.84 0.15 1 160 . 25 VAL N N 123.87 0.2 1 161 . 26 SER H H 9.31 0.015 1 162 . 26 SER HA H 5.07 0.015 1 163 . 26 SER HB2 H 3.60 0.015 1 164 . 26 SER HB3 H 3.60 0.015 1 165 . 26 SER C C 171.35 0.15 1 166 . 26 SER CA C 55.44 0.15 1 167 . 26 SER CB C 63.30 0.15 1 168 . 26 SER N N 120.10 0.2 1 169 . 27 LYS H H 8.42 0.015 1 170 . 27 LYS HA H 4.54 0.015 1 171 . 27 LYS HB2 H 1.85 0.015 2 172 . 27 LYS HB3 H 1.59 0.015 2 173 . 27 LYS C C 172.81 0.15 1 174 . 27 LYS CA C 53.60 0.15 1 175 . 27 LYS CB C 30.10 0.15 1 176 . 27 LYS N N 125.56 0.2 1 177 . 28 LEU H H 8.42 0.015 1 178 . 28 LEU HA H 5.27 0.015 1 179 . 28 LEU HB2 H 1.89 0.015 2 180 . 28 LEU HB3 H 1.14 0.015 2 181 . 28 LEU HG H 1.66 0.015 1 182 . 28 LEU HD1 H 0.64 0.015 2 183 . 28 LEU HD2 H 0.69 0.015 2 184 . 28 LEU C C 174.86 0.15 1 185 . 28 LEU CA C 51.03 0.15 1 186 . 28 LEU CB C 41.93 0.15 1 187 . 28 LEU N N 124.05 0.2 1 188 . 29 ARG H H 8.17 0.015 1 189 . 29 ARG HA H 5.22 0.015 1 190 . 29 ARG HB2 H 1.75 0.015 1 191 . 29 ARG HB3 H 1.75 0.015 1 192 . 29 ARG C C 174.49 0.15 1 193 . 29 ARG CA C 52.48 0.15 1 194 . 29 ARG CB C 30.79 0.15 1 195 . 29 ARG N N 121.53 0.2 1 196 . 30 ILE H H 9.55 0.015 1 197 . 30 ILE HA H 4.80 0.015 1 198 . 30 ILE HB H 1.75 0.015 1 199 . 30 ILE HG12 H 1.49 0.015 1 200 . 30 ILE HG13 H 1.49 0.015 1 201 . 30 ILE HG2 H 0.48 0.015 1 202 . 30 ILE HD1 H 0.89 0.015 1 203 . 30 ILE C C 172.29 0.15 1 204 . 30 ILE CA C 57.54 0.15 1 205 . 30 ILE CB C 39.13 0.15 1 206 . 30 ILE CD1 C 12.15 0.15 1 207 . 30 ILE N N 123.83 0.2 1 208 . 31 ARG H H 9.14 0.015 1 209 . 31 ARG HA H 4.14 0.015 1 210 . 31 ARG HB2 H 1.70 0.015 2 211 . 31 ARG HB3 H 1.10 0.015 2 212 . 31 ARG C C 174.36 0.15 1 213 . 31 ARG CA C 53.32 0.15 1 214 . 31 ARG CB C 29.17 0.15 1 215 . 31 ARG N N 129.55 0.2 1 216 . 32 THR H H 8.89 0.015 1 217 . 32 THR HA H 4.17 0.015 1 218 . 32 THR HB H 4.26 0.015 1 219 . 32 THR HG2 H 0.88 0.015 1 220 . 32 THR CA C 58.34 0.15 1 221 . 32 THR CB C 65.30 0.15 1 222 . 32 THR CG2 C 19.34 0.15 1 223 . 32 THR N N 119.59 0.2 1 224 . 34 SER HA H 4.44 0.015 1 225 . 34 SER HB2 H 4.05 0.015 1 226 . 34 SER HB3 H 3.86 0.015 1 227 . 34 SER C C 173.27 0.15 1 228 . 34 SER CA C 56.33 0.15 1 229 . 34 SER CB C 61.39 0.15 1 230 . 35 GLY H H 8.10 0.015 1 231 . 35 GLY HA2 H 4.24 0.015 1 232 . 35 GLY HA3 H 3.15 0.015 1 233 . 35 GLY C C 171.76 0.15 1 234 . 35 GLY CA C 42.84 0.15 1 235 . 35 GLY N N 110.11 0.2 1 236 . 36 GLU H H 7.16 0.015 1 237 . 36 GLU HA H 4.28 0.015 1 238 . 36 GLU HB2 H 1.77 0.015 2 239 . 36 GLU HB3 H 1.97 0.015 2 240 . 36 GLU HG2 H 2.14 0.015 1 241 . 36 GLU HG3 H 2.14 0.015 1 242 . 36 GLU C C 173.22 0.15 1 243 . 36 GLU CA C 53.51 0.15 1 244 . 36 GLU CB C 28.20 0.15 1 245 . 36 GLU N N 119.28 0.2 1 246 . 37 PHE H H 8.87 0.015 1 247 . 37 PHE HA H 5.23 0.015 1 248 . 37 PHE HB2 H 2.88 0.015 2 249 . 37 PHE HB3 H 2.58 0.015 2 250 . 37 PHE HD1 H 7.07 0.015 1 251 . 37 PHE HD2 H 7.07 0.015 1 252 . 37 PHE HE1 H 7.22 0.015 1 253 . 37 PHE HE2 H 7.22 0.015 1 254 . 37 PHE HZ H 7.31 0.015 1 255 . 37 PHE C C 172.99 0.15 1 256 . 37 PHE CA C 55.66 0.15 1 257 . 37 PHE CB C 39.01 0.15 1 258 . 37 PHE N N 119.38 0.2 1 259 . 38 LEU H H 9.52 0.015 1 260 . 38 LEU HA H 4.71 0.015 1 261 . 38 LEU HB2 H 1.95 0.015 1 262 . 38 LEU HB3 H 1.57 0.015 1 263 . 38 LEU C C 174.37 0.15 1 264 . 38 LEU CA C 51.26 0.15 1 265 . 38 LEU CB C 41.18 0.15 1 266 . 38 LEU N N 123.81 0.2 1 267 . 39 GLU H H 8.76 0.015 1 268 . 39 GLU HA H 5.37 0.015 1 269 . 39 GLU HB2 H 1.93 0.015 1 270 . 39 GLU HB3 H 1.93 0.015 1 271 . 39 GLU HG2 H 2.11 0.015 1 272 . 39 GLU HG3 H 2.11 0.015 1 273 . 39 GLU C C 172.81 0.15 1 274 . 39 GLU CA C 53.31 0.15 1 275 . 39 GLU N N 122.07 0.2 1 276 . 40 ARG H H 8.42 0.015 1 277 . 40 ARG HA H 4.09 0.015 1 278 . 40 ARG HB2 H 0.94 0.015 2 279 . 40 ARG HB3 H 0.71 0.015 2 280 . 40 ARG C C 170.94 0.15 1 281 . 40 ARG CA C 53.45 0.15 1 282 . 40 ARG CB C 31.55 0.15 1 283 . 40 ARG N N 124.04 0.2 1 284 . 41 ARG H H 8.80 0.015 1 285 . 41 ARG HA H 5.08 0.015 1 286 . 41 ARG HB2 H 1.65 0.015 1 287 . 41 ARG HB3 H 1.40 0.015 1 288 . 41 ARG C C 173.18 0.15 1 289 . 41 ARG CA C 52.65 0.15 1 290 . 41 ARG CB C 29.81 0.15 1 291 . 41 ARG N N 123.03 0.2 1 292 . 42 PHE H H 8.93 0.015 1 293 . 42 PHE HA H 4.68 0.015 1 294 . 42 PHE HB2 H 3.17 0.015 2 295 . 42 PHE HB3 H 2.23 0.015 2 296 . 42 PHE HD1 H 7.09 0.015 1 297 . 42 PHE HD2 H 7.09 0.015 1 298 . 42 PHE HE1 H 6.85 0.015 1 299 . 42 PHE HE2 H 6.85 0.015 1 300 . 42 PHE HZ H 6.57 0.015 1 301 . 42 PHE C C 173.97 0.15 1 302 . 42 PHE CA C 53.88 0.15 1 303 . 42 PHE CB C 41.37 0.15 1 304 . 42 PHE N N 117.82 0.2 1 305 . 43 LEU H H 8.50 0.015 1 306 . 43 LEU HA H 4.45 0.015 1 307 . 43 LEU HB2 H 1.65 0.015 1 308 . 43 LEU HB3 H 1.65 0.015 1 309 . 43 LEU C C 176.37 0.15 1 310 . 43 LEU CA C 53.99 0.15 1 311 . 43 LEU CB C 39.15 0.15 1 312 . 43 LEU N N 123.01 0.2 1 313 . 44 ALA H H 8.64 0.015 1 314 . 44 ALA HA H 4.07 0.015 1 315 . 44 ALA HB H 1.03 0.015 1 316 . 44 ALA C C 174.05 0.15 1 317 . 44 ALA CA C 52.05 0.15 1 318 . 44 ALA CB C 16.31 0.15 1 319 . 44 ALA N N 126.61 0.2 1 320 . 45 SER H H 7.80 0.015 1 321 . 45 SER HA H 4.16 0.015 1 322 . 45 SER HB2 H 3.99 0.015 2 323 . 45 SER HB3 H 3.72 0.015 2 324 . 45 SER C C 173.72 0.15 1 325 . 45 SER CA C 55.84 0.15 1 326 . 45 SER CB C 61.54 0.15 1 327 . 45 SER N N 106.5 0.2 1 328 . 46 ASN H H 7.93 0.015 1 329 . 46 ASN HA H 4.46 0.015 1 330 . 46 ASN HB2 H 2.99 0.015 2 331 . 46 ASN HB3 H 2.64 0.015 2 332 . 46 ASN C C 171.78 0.15 1 333 . 46 ASN CA C 51.62 0.15 1 334 . 46 ASN CB C 37.48 0.15 1 335 . 46 ASN N N 121.11 0.2 1 336 . 47 LYS H H 8.01 0.015 1 337 . 47 LYS HA H 4.06 0.015 1 338 . 47 LYS HB2 H 2.21 0.015 1 339 . 47 LYS HB3 H 1.60 0.015 1 340 . 47 LYS C C 175.23 0.15 1 341 . 47 LYS CA C 53.64 0.15 1 342 . 47 LYS CB C 30.68 0.15 1 343 . 47 LYS N N 116.85 0.2 1 344 . 48 LEU H H 8.71 0.015 1 345 . 48 LEU HA H 3.46 0.015 1 346 . 48 LEU HB2 H 1.31 0.015 2 347 . 48 LEU HB3 H 1.12 0.015 2 348 . 48 LEU C C 175.46 0.15 1 349 . 48 LEU N N 123.75 0.2 1 350 . 49 GLN H H 8.31 0.015 1 351 . 49 GLN HA H 3.26 0.015 1 352 . 49 GLN HB2 H 2.11 0.015 2 353 . 49 GLN HB3 H 1.51 0.015 2 354 . 49 GLN C C 174.12 0.15 1 355 . 49 GLN CA C 55.91 0.15 1 356 . 49 GLN CB C 27.32 0.15 1 357 . 49 GLN N N 115.97 0.2 1 358 . 50 ILE H H 7.80 0.015 1 359 . 50 ILE HA H 3.93 0.015 1 360 . 50 ILE HB H 2.02 0.015 1 361 . 50 ILE HD1 H 0.86 0.015 1 362 . 50 ILE C C 176.69 0.15 1 363 . 50 ILE CA C 61.32 0.15 1 364 . 50 ILE CB C 34.38 0.15 1 365 . 50 ILE CD1 C 9.54 0.15 1 366 . 50 ILE N N 116.0 0.2 1 367 . 51 VAL H H 7.18 0.015 1 368 . 51 VAL HA H 3.37 0.015 1 369 . 51 VAL HB H 1.87 0.015 1 370 . 51 VAL HG1 H 0.55 0.015 2 371 . 51 VAL HG2 H -0.04 0.015 2 372 . 51 VAL C C 176.26 0.15 1 373 . 51 VAL CA C 63.68 0.15 1 374 . 51 VAL CB C 28.52 0.15 1 375 . 51 VAL N N 120.83 0.2 1 376 . 52 PHE H H 7.27 0.015 1 377 . 52 PHE HA H 4.54 0.015 1 378 . 52 PHE HB2 H 3.14 0.015 2 379 . 52 PHE HB3 H 3.13 0.015 2 380 . 52 PHE HD1 H 6.63 0.015 1 381 . 52 PHE HD2 H 6.63 0.015 1 382 . 52 PHE HE1 H 6.95 0.015 1 383 . 52 PHE HE2 H 6.95 0.015 1 384 . 52 PHE HZ H 7.44 0.015 1 385 . 52 PHE C C 177.14 0.15 1 386 . 52 PHE CA C 55.29 0.15 1 387 . 52 PHE CB C 33.29 0.15 1 388 . 52 PHE N N 119.67 0.2 1 389 . 53 ASP H H 9.15 0.015 1 390 . 53 ASP HA H 4.50 0.015 1 391 . 53 ASP HB2 H 2.95 0.015 2 392 . 53 ASP HB3 H 2.72 0.015 2 393 . 53 ASP C C 177.14 0.15 1 394 . 53 ASP CA C 55.45 0.15 1 395 . 53 ASP CB C 37.88 0.15 1 396 . 53 ASP N N 122.37 0.2 1 397 . 54 PHE H H 8.57 0.015 1 398 . 54 PHE HA H 4.47 0.015 1 399 . 54 PHE HB2 H 3.53 0.015 1 400 . 54 PHE HB3 H 3.53 0.015 1 401 . 54 PHE C C 176.51 0.15 1 402 . 54 PHE CA C 58.64 0.15 1 403 . 54 PHE CB C 36.52 0.15 1 404 . 54 PHE N N 121.62 0.2 1 405 . 55 VAL H H 8.66 0.015 1 406 . 55 VAL HA H 3.36 0.015 1 407 . 55 VAL HB H 2.37 0.015 1 408 . 55 VAL HG1 H 1.31 0.015 2 409 . 55 VAL HG2 H 1.06 0.015 2 410 . 55 VAL C C 174.57 0.15 1 411 . 55 VAL CA C 64.87 0.15 1 412 . 55 VAL CB C 29.66 0.15 1 413 . 55 VAL N N 116.89 0.2 1 414 . 56 ALA H H 8.54 0.015 1 415 . 56 ALA HA H 3.75 0.015 1 416 . 56 ALA HB H 1.68 0.015 1 417 . 56 ALA C C 180.02 0.15 1 418 . 56 ALA CA C 53.65 0.15 1 419 . 56 ALA CB C 16.16 0.15 1 420 . 56 ALA N N 123.50 0.2 1 421 . 57 SER H H 8.45 0.015 1 422 . 57 SER HA H 4.20 0.015 1 423 . 57 SER HB2 H 3.95 0.015 1 424 . 57 SER HB3 H 3.95 0.015 1 425 . 57 SER C C 172.51 0.15 1 426 . 57 SER CA C 59.95 0.15 1 427 . 57 SER CB C 59.95 0.15 1 428 . 57 SER N N 117.09 0.2 1 429 . 58 LYS H H 6.95 0.015 1 430 . 58 LYS HA H 4.32 0.015 1 431 . 58 LYS HB2 H 2.01 0.015 2 432 . 58 LYS HB3 H 1.67 0.015 2 433 . 58 LYS C C 173.23 0.15 1 434 . 58 LYS CA C 51.40 0.15 1 435 . 58 LYS CB C 29.32 0.15 1 436 . 58 LYS N N 119.23 0.2 1 437 . 59 GLY H H 7.58 0.015 1 438 . 59 GLY HA2 H 3.77 0.015 2 439 . 59 GLY HA3 H 3.35 0.015 2 440 . 59 GLY C C 171.00 0.15 1 441 . 59 GLY CA C 42.30 0.15 1 442 . 59 GLY N N 104.31 0.2 1 443 . 60 PHE H H 7.52 0.015 1 444 . 60 PHE HA H 4.76 0.015 1 445 . 60 PHE HB2 H 2.42 0.015 2 446 . 60 PHE HB3 H 1.99 0.015 2 447 . 60 PHE HD1 H 6.08 0.015 1 448 . 60 PHE HD2 H 6.08 0.015 1 449 . 60 PHE CA C 52.47 0.15 1 450 . 60 PHE CD1 C 130.13 0.15 1 451 . 60 PHE CD2 C 130.13 0.15 1 452 . 60 PHE CE1 C 128.73 0.15 1 453 . 60 PHE CE2 C 128.73 0.15 1 454 . 60 PHE N N 118.75 0.2 1 455 . 62 TRP HA H 4.44 0.015 1 456 . 62 TRP HB2 H 3.05 0.015 1 457 . 62 TRP HB3 H 3.05 0.015 1 458 . 62 TRP HD1 H 6.91 0.015 1 459 . 62 TRP HE1 H 9.92 0.015 1 460 . 62 TRP HE3 H 7.42 0.015 1 461 . 62 TRP HZ2 H 7.55 0.015 1 462 . 62 TRP HZ3 H 6.97 0.015 1 463 . 62 TRP HH2 H 7.19 0.015 1 464 . 62 TRP C C 173.58 0.15 1 465 . 62 TRP CA C 57.69 0.15 1 466 . 62 TRP CB C 26.19 0.15 1 467 . 62 TRP CD1 C 125.08 0.15 1 468 . 62 TRP CE3 C 118.80 0.15 1 469 . 62 TRP CZ2 C 112.49 0.15 1 470 . 62 TRP CZ3 C 120.00 0.15 1 471 . 62 TRP CH2 C 122.58 0.15 1 472 . 62 TRP NE1 N 129.16 0.2 1 473 . 63 ASP H H 8.08 0.015 1 474 . 63 ASP HA H 4.13 0.015 1 475 . 63 ASP HB2 H 2.44 0.015 1 476 . 63 ASP HB3 H 2.15 0.015 1 477 . 63 ASP C C 174.36 0.15 1 478 . 63 ASP CA C 52.50 0.15 1 479 . 63 ASP N N 114.60 0.2 1 480 . 64 GLU H H 7.63 0.015 1 481 . 64 GLU HA H 4.23 0.015 1 482 . 64 GLU HB2 H 1.83 0.015 1 483 . 64 GLU HB3 H 1.83 0.015 1 484 . 64 GLU HG2 H 2.00 0.015 1 485 . 64 GLU HG3 H 2.00 0.015 1 486 . 64 GLU C C 173.42 0.15 1 487 . 64 GLU CA C 54.30 0.15 1 488 . 64 GLU CB C 31.24 0.15 1 489 . 64 GLU N N 116.35 0.2 1 490 . 65 TYR H H 7.66 0.015 1 491 . 65 TYR HA H 4.74 0.015 1 492 . 65 TYR HB2 H 2.80 0.015 2 493 . 65 TYR HB3 H 2.35 0.015 2 494 . 65 TYR HD1 H 6.94 0.015 1 495 . 65 TYR HD2 H 6.94 0.015 1 496 . 65 TYR HE1 H 7.00 0.015 1 497 . 65 TYR HE2 H 7.00 0.015 1 498 . 65 TYR C C 172.29 0.15 1 499 . 65 TYR CA C 56.11 0.15 1 500 . 65 TYR CB C 40.24 0.15 1 501 . 65 TYR CD1 C 116.44 0.15 1 502 . 65 TYR CD2 C 116.44 0.15 1 503 . 65 TYR CE1 C 131.17 0.15 1 504 . 65 TYR CE2 C 131.17 0.15 1 505 . 65 TYR N N 117.93 0.2 1 506 . 66 LYS H H 9.12 0.015 1 507 . 66 LYS HA H 4.44 0.015 1 508 . 66 LYS HB2 H 1.54 0.015 1 509 . 66 LYS HB3 H 1.54 0.015 1 510 . 66 LYS C C 172.87 0.15 1 511 . 66 LYS CA C 52.46 0.15 1 512 . 66 LYS CB C 33.18 0.15 1 513 . 66 LYS N N 118.25 0.2 1 514 . 67 LEU H H 7.82 0.015 1 515 . 67 LEU HA H 4.92 0.015 1 516 . 67 LEU HB2 H 1.72 0.015 2 517 . 67 LEU HB3 H 1.35 0.015 2 518 . 67 LEU C C 172.24 0.15 1 519 . 67 LEU CA C 51.26 0.15 1 520 . 67 LEU CB C 43.16 0.15 1 521 . 67 LEU N N 122.45 0.2 1 522 . 68 LEU H H 9.14 0.015 1 523 . 68 LEU HA H 5.38 0.015 1 524 . 68 LEU HB2 H 1.85 0.015 2 525 . 68 LEU HB3 H 1.45 0.015 2 526 . 68 LEU C C 175.45 0.15 1 527 . 68 LEU CA C 51.68 0.15 1 528 . 68 LEU CB C 41.92 0.15 1 529 . 68 LEU N N 125.16 0.2 1 530 . 69 SER H H 8.83 0.015 1 531 . 69 SER HA H 4.91 0.015 1 532 . 69 SER HB2 H 4.44 0.015 2 533 . 69 SER HB3 H 3.58 0.015 2 534 . 69 SER C C 172.08 0.15 1 535 . 69 SER CA C 55.42 0.15 1 536 . 69 SER CB C 63.18 0.15 1 537 . 69 SER N N 115.17 0.2 1 538 . 70 THR H H 8.66 0.015 1 539 . 70 THR HA H 4.23 0.015 1 540 . 70 THR HB H 4.23 0.015 1 541 . 70 THR HG2 H 1.15 0.015 1 542 . 70 THR C C 172.49 0.15 1 543 . 70 THR CA C 62.69 0.15 1 544 . 70 THR CB C 67.68 0.15 1 545 . 70 THR CG2 C 19.76 0.15 1 546 . 70 THR N N 113.65 0.2 1 547 . 71 PHE H H 8.34 0.015 1 548 . 71 PHE HA H 4.59 0.015 1 549 . 71 PHE HB2 H 3.03 0.015 1 550 . 71 PHE HB3 H 3.03 0.015 1 551 . 71 PHE CA C 54.48 0.15 1 552 . 71 PHE N N 119.59 0.2 1 553 . 73 ARG HA H 4.21 0.015 1 554 . 73 ARG HB2 H 1.73 0.015 1 555 . 73 ARG HB3 H 1.73 0.015 1 556 . 73 ARG C C 173.53 0.15 1 557 . 73 ARG CA C 54.42 0.15 1 558 . 73 ARG CB C 27.34 0.15 1 559 . 74 ARG H H 7.85 0.015 1 560 . 74 ARG HA H 4.51 0.015 1 561 . 74 ARG HB2 H 1.74 0.015 1 562 . 74 ARG HB3 H 1.74 0.015 1 563 . 74 ARG C C 171.50 0.15 1 564 . 74 ARG CA C 52.39 0.15 1 565 . 74 ARG CB C 30.22 0.15 1 566 . 74 ARG N N 124.42 0.2 1 567 . 75 ASP H H 8.40 0.015 1 568 . 75 ASP HA H 4.95 0.015 1 569 . 75 ASP HB2 H 2.86 0.015 2 570 . 75 ASP HB3 H 2.36 0.015 2 571 . 75 ASP C C 175.90 0.15 1 572 . 75 ASP CA C 50.57 0.15 1 573 . 75 ASP CB C 37.88 0.15 1 574 . 75 ASP N N 124.42 0.2 1 575 . 76 VAL H H 9.42 0.015 1 576 . 76 VAL HA H 3.81 0.015 1 577 . 76 VAL HB H 2.25 0.015 1 578 . 76 VAL HG1 H 1.05 0.015 1 579 . 76 VAL HG2 H 1.05 0.015 1 580 . 76 VAL C C 175.16 0.15 1 581 . 76 VAL CA C 62.80 0.15 1 582 . 76 VAL CB C 29.44 0.15 1 583 . 76 VAL N N 126.64 0.2 1 584 . 77 THR H H 8.38 0.015 1 585 . 77 THR HA H 4.24 0.015 1 586 . 77 THR HB H 4.22 0.015 1 587 . 77 THR HG2 H 1.13 0.015 1 588 . 77 THR C C 174.17 0.15 1 589 . 77 THR CA C 61.70 0.15 1 590 . 77 THR CB C 66.84 0.15 1 591 . 77 THR CG2 C 21.50 0.15 1 592 . 77 THR N N 108.51 0.2 1 593 . 78 GLN H H 7.40 0.015 1 594 . 78 GLN HA H 4.42 0.015 1 595 . 78 GLN HB2 H 2.39 0.015 2 596 . 78 GLN HB3 H 1.87 0.015 2 597 . 78 GLN HG2 H 2.23 0.015 1 598 . 78 GLN HG3 H 2.23 0.015 1 599 . 78 GLN C C 174.20 0.15 1 600 . 78 GLN CA C 53.23 0.15 1 601 . 78 GLN CB C 26.88 0.15 1 602 . 78 GLN N N 117.61 0.2 1 603 . 79 LEU H H 7.36 0.015 1 604 . 79 LEU HA H 4.37 0.015 1 605 . 79 LEU HB2 H 1.99 0.015 2 606 . 79 LEU HB3 H 1.23 0.015 2 607 . 79 LEU C C 173.23 0.15 1 608 . 79 LEU CA C 51.76 0.15 1 609 . 79 LEU CB C 40.14 0.15 1 610 . 79 LEU N N 120.04 0.2 1 611 . 80 ASP H H 7.84 0.015 1 612 . 80 ASP HA H 4.58 0.015 1 613 . 80 ASP HB2 H 2.63 0.015 1 614 . 80 ASP HB3 H 2.63 0.015 1 615 . 80 ASP CA C 49.39 0.15 1 616 . 80 ASP N N 120.44 0.2 1 617 . 81 PRO HA H 3.96 0.015 1 618 . 81 PRO HB2 H 1.93 0.015 1 619 . 81 PRO HB3 H 1.93 0.015 1 620 . 81 PRO C C 174.17 0.15 1 621 . 81 PRO CA C 61.33 0.15 1 622 . 81 PRO CB C 29.87 0.15 1 623 . 82 ASN H H 8.45 0.015 1 624 . 82 ASN HA H 4.56 0.015 1 625 . 82 ASN HB2 H 2.72 0.015 1 626 . 82 ASN HB3 H 2.72 0.015 1 627 . 82 ASN C C 174.28 0.15 1 628 . 82 ASN CA C 51.54 0.15 1 629 . 82 ASN CB C 37.34 0.15 1 630 . 82 ASN N N 113.29 0.2 1 631 . 83 LYS H H 7.52 0.015 1 632 . 83 LYS HA H 4.25 0.015 1 633 . 83 LYS HB2 H 1.66 0.015 1 634 . 83 LYS HB3 H 1.66 0.015 1 635 . 83 LYS C C 173.18 0.15 1 636 . 83 LYS CA C 53.90 0.15 1 637 . 83 LYS CB C 32.30 0.15 1 638 . 83 LYS N N 120.80 0.2 1 639 . 84 SER H H 8.80 0.015 1 640 . 84 SER HA H 4.84 0.015 1 641 . 84 SER HB2 H 4.22 0.015 1 642 . 84 SER HB3 H 3.77 0.015 1 643 . 84 SER C C 173.18 0.15 1 644 . 84 SER CA C 54.59 0.15 1 645 . 84 SER CB C 64.05 0.15 1 646 . 84 SER N N 115.65 0.2 1 647 . 85 LEU H H 7.92 0.015 1 648 . 85 LEU HA H 3.79 0.015 1 649 . 85 LEU HB2 H 1.98 0.015 2 650 . 85 LEU HB3 H 1.52 0.015 2 651 . 85 LEU C C 177.78 0.15 1 652 . 85 LEU CA C 56.35 0.15 1 653 . 85 LEU CB C 37.18 0.15 1 654 . 85 LEU N N 118.34 0.2 1 655 . 86 LEU H H 7.76 0.015 1 656 . 86 LEU HA H 3.68 0.015 1 657 . 86 LEU HB2 H 2.01 0.015 1 658 . 86 LEU HB3 H 2.01 0.015 1 659 . 86 LEU HG H 1.34 0.015 1 660 . 86 LEU HD1 H 1.16 0.015 1 661 . 86 LEU HD2 H 0.29 0.015 1 662 . 86 LEU C C 178.52 0.15 1 663 . 86 LEU CA C 56.12 0.15 1 664 . 86 LEU CB C 40.14 0.15 1 665 . 86 LEU CD1 C 24.41 0.15 1 666 . 86 LEU CD2 C 22.06 0.15 1 667 . 86 LEU N N 117.04 0.2 1 668 . 87 GLU H H 7.84 0.015 1 669 . 87 GLU HA H 3.90 0.015 1 670 . 87 GLU HB2 H 2.33 0.015 2 671 . 87 GLU HB3 H 1.97 0.015 2 672 . 87 GLU C C 176.90 0.15 1 673 . 87 GLU CA C 57.32 0.15 1 674 . 87 GLU CB C 28.04 0.15 1 675 . 87 GLU N N 120.44 0.2 1 676 . 88 VAL H H 7.65 0.015 1 677 . 88 VAL HA H 4.48 0.015 1 678 . 88 VAL HB H 2.46 0.015 1 679 . 88 VAL HG1 H 0.91 0.015 1 680 . 88 VAL HG2 H 0.91 0.015 1 681 . 88 VAL C C 172.07 0.15 1 682 . 88 VAL CA C 58.74 0.15 1 683 . 88 VAL CB C 28.14 0.15 1 684 . 88 VAL N N 109.15 0.2 1 685 . 89 LYS H H 7.67 0.015 1 686 . 89 LYS HA H 3.88 0.015 1 687 . 89 LYS HB2 H 2.12 0.015 1 688 . 89 LYS HB3 H 2.12 0.015 1 689 . 89 LYS C C 174.25 0.15 1 690 . 89 LYS CA C 55.75 0.15 1 691 . 89 LYS CB C 26.21 0.15 1 692 . 89 LYS N N 114.91 0.2 1 693 . 90 LEU H H 8.37 0.015 1 694 . 90 LEU HA H 4.58 0.015 1 695 . 90 LEU HB2 H 1.40 0.015 1 696 . 90 LEU HB3 H 1.40 0.015 1 697 . 90 LEU C C 173.07 0.15 1 698 . 90 LEU CA C 49.88 0.15 1 699 . 90 LEU CB C 38.20 0.15 1 700 . 90 LEU N N 122.58 0.2 1 701 . 91 PHE H H 7.27 0.015 1 702 . 91 PHE HA H 4.55 0.015 1 703 . 91 PHE HB2 H 2.99 0.015 2 704 . 91 PHE HB3 H 2.41 0.015 2 705 . 91 PHE CA C 53.39 0.15 1 706 . 91 PHE N N 117.66 0.2 1 707 . 92 PRO HA H 3.87 0.015 1 708 . 92 PRO HB2 H 1.83 0.015 2 709 . 92 PRO HB3 H 1.22 0.015 2 710 . 92 PRO C C 173.47 0.15 1 711 . 92 PRO CA C 62.23 0.15 1 712 . 92 PRO CB C 31.45 0.15 1 713 . 93 GLN H H 7.22 0.015 1 714 . 93 GLN HA H 5.33 0.015 1 715 . 93 GLN HB2 H 2.02 0.015 1 716 . 93 GLN HB3 H 2.02 0.015 1 717 . 93 GLN HG2 H 2.17 0.015 1 718 . 93 GLN HG3 H 2.17 0.015 1 719 . 93 GLN C C 171.58 0.15 1 720 . 93 GLN CA C 52.67 0.15 1 721 . 93 GLN CB C 28.72 0.15 1 722 . 93 GLN N N 119.64 0.2 1 723 . 94 GLU H H 7.82 0.015 1 724 . 94 GLU HA H 4.88 0.015 1 725 . 94 GLU HB2 H 1.90 0.015 2 726 . 94 GLU HB3 H 1.62 0.015 2 727 . 94 GLU HG2 H 2.26 0.015 1 728 . 94 GLU HG3 H 2.26 0.015 1 729 . 94 GLU C C 172.55 0.15 1 730 . 94 GLU CA C 53.23 0.15 1 731 . 94 GLU CB C 32.06 0.15 1 732 . 94 GLU N N 121.38 0.2 1 733 . 95 THR H H 9.06 0.015 1 734 . 95 THR HA H 5.32 0.015 1 735 . 95 THR HB H 3.97 0.015 1 736 . 95 THR HG2 H 1.00 0.015 1 737 . 95 THR C C 171.25 0.15 1 738 . 95 THR CA C 59.57 0.15 1 739 . 95 THR CB C 67.96 0.15 1 740 . 95 THR CG2 C 19.70 0.15 1 741 . 95 THR N N 121.20 0.2 1 742 . 96 LEU H H 9.27 0.015 1 743 . 96 LEU HA H 5.33 0.015 1 744 . 96 LEU HB2 H 1.49 0.015 2 745 . 96 LEU HB3 H 1.37 0.015 2 746 . 96 LEU C C 172.99 0.15 1 747 . 96 LEU CA C 50.38 0.15 1 748 . 96 LEU CB C 43.73 0.15 1 749 . 96 LEU N N 125.63 0.2 1 750 . 97 PHE H H 9.43 0.015 1 751 . 97 PHE HA H 4.82 0.015 1 752 . 97 PHE HB3 H 3.04 0.015 1 753 . 97 PHE HB2 H 2.88 0.015 1 754 . 97 PHE C C 176.92 0.15 1 755 . 97 PHE CA C 54.60 0.15 1 756 . 97 PHE CB C 39.16 0.15 1 757 . 97 PHE N N 118.56 0.2 1 758 . 98 LEU H H 8.02 0.015 1 759 . 98 LEU HA H 5.16 0.015 1 760 . 98 LEU HB2 H 1.55 0.015 2 761 . 98 LEU HB3 H 0.75 0.015 2 762 . 98 LEU HG H 1.10 0.015 1 763 . 98 LEU HD1 H 0.59 0.015 2 764 . 98 LEU HD2 H -0.25 0.015 2 765 . 98 LEU C C 174.78 0.15 1 766 . 98 LEU CA C 52.26 0.15 1 767 . 98 LEU CB C 42.37 0.15 1 768 . 98 LEU N N 122.50 0.2 1 769 . 99 GLU H H 8.28 0.015 1 770 . 99 GLU HA H 4.63 0.015 1 771 . 99 GLU HB2 H 1.86 0.015 2 772 . 99 GLU HB3 H 1.78 0.015 2 773 . 99 GLU HG2 H 2.16 0.015 1 774 . 99 GLU HG3 H 2.16 0.015 1 775 . 99 GLU C C 172.74 0.15 1 776 . 99 GLU CA C 52.80 0.15 1 777 . 99 GLU CB C 32.30 0.15 1 778 . 99 GLU N N 120.51 0.2 1 779 . 100 ALA H H 9.18 0.015 1 780 . 100 ALA HA H 3.87 0.015 1 781 . 100 ALA HB H 1.30 0.015 1 782 . 100 ALA C C 175.73 0.15 1 783 . 100 ALA CA C 51.29 0.15 1 784 . 100 ALA CB C 16.41 0.15 1 785 . 100 ALA N N 128.40 0.2 1 786 . 101 LYS H H 7.73 0.015 1 787 . 101 LYS HA H 3.91 0.015 1 788 . 101 LYS HB2 H 1.65 0.015 2 789 . 101 LYS HB3 H 1.25 0.015 2 790 . 101 LYS C C 173.27 0.15 1 791 . 101 LYS CA C 55.46 0.15 1 792 . 101 LYS CB C 30.91 0.15 1 793 . 101 LYS N N 121.31 0.2 1 794 . 102 GLU H H 7.85 0.015 1 795 . 102 GLU HA H 4.01 0.015 1 796 . 102 GLU HB2 H 1.92 0.015 2 797 . 102 GLU HB3 H 1.76 0.015 2 798 . 102 GLU HG2 H 2.06 0.015 1 799 . 102 GLU HG3 H 2.06 0.015 1 800 . 102 GLU CA C 55.72 0.15 1 801 . 102 GLU N N 126.24 0.2 1 stop_ save_