data_5709 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C resonance assignments of the TPR domain of hSGT ; _BMRB_accession_number 5709 _BMRB_flat_file_name bmr5709.str _Entry_type original _Submission_date 2003-02-26 _Accession_date 2003-02-26 _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 Cheng Jya-Wei . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 336 "13C chemical shifts" 342 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-12 original author . stop_ _Original_release_date 2003-06-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N and 13C Resonance Assignments of the TPR Domain of hSGT ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22699292 _PubMed_ID 12815268 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pai Ming-Tao . . 2 Yang Chih-Sheng . . 3 Tzeng Shiou-Ru . . 4 Wang Chung . . 5 Cheng Jya-Wei . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 26 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 381 _Page_last 382 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_TPR _Saveframe_category molecular_system _Mol_system_name 'TPR domain of hSGT' _Abbreviation_common TPR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TPR monomer' $TPR_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TPR_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Tetratricopeptide repeat' _Abbreviation_common TPR _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 118 _Mol_residue_sequence ; AERLKTEGNEQMKVENFEAA VHFYGKAIELNPANAVYFCN RAAAYSKLGNYAGAVQDCER AICIDPAYSKAYGRMGLALS SLNKHVEAVAYYKKALELDP DNETYKSNLKIAELKLRE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 91 ALA 2 92 GLU 3 93 ARG 4 94 LEU 5 95 LYS 6 96 THR 7 97 GLU 8 98 GLY 9 99 ASN 10 100 GLU 11 101 GLN 12 102 MET 13 103 LYS 14 104 VAL 15 105 GLU 16 106 ASN 17 107 PHE 18 108 GLU 19 109 ALA 20 110 ALA 21 111 VAL 22 112 HIS 23 113 PHE 24 114 TYR 25 115 GLY 26 116 LYS 27 117 ALA 28 118 ILE 29 119 GLU 30 120 LEU 31 121 ASN 32 122 PRO 33 123 ALA 34 124 ASN 35 125 ALA 36 126 VAL 37 127 TYR 38 128 PHE 39 129 CYS 40 130 ASN 41 131 ARG 42 132 ALA 43 133 ALA 44 134 ALA 45 135 TYR 46 136 SER 47 137 LYS 48 138 LEU 49 139 GLY 50 140 ASN 51 141 TYR 52 142 ALA 53 143 GLY 54 144 ALA 55 145 VAL 56 146 GLN 57 147 ASP 58 148 CYS 59 149 GLU 60 150 ARG 61 151 ALA 62 152 ILE 63 153 CYS 64 154 ILE 65 155 ASP 66 156 PRO 67 157 ALA 68 158 TYR 69 159 SER 70 160 LYS 71 161 ALA 72 162 TYR 73 163 GLY 74 164 ARG 75 165 MET 76 166 GLY 77 167 LEU 78 168 ALA 79 169 LEU 80 170 SER 81 171 SER 82 172 LEU 83 173 ASN 84 174 LYS 85 175 HIS 86 176 VAL 87 177 GLU 88 178 ALA 89 179 VAL 90 180 ALA 91 181 TYR 92 182 TYR 93 183 LYS 94 184 LYS 95 185 ALA 96 186 LEU 97 187 GLU 98 188 LEU 99 189 ASP 100 190 PRO 101 191 ASP 102 192 ASN 103 193 GLU 104 194 THR 105 195 TYR 106 196 LYS 107 197 SER 108 198 ASN 109 199 LEU 110 200 LYS 111 201 ILE 112 202 ALA 113 203 GLU 114 204 LEU 115 205 LYS 116 206 LEU 117 207 ARG 118 208 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 2VYI "Crystal Structure Of The Tpr Domain Of Human Sgt" 100.00 131 100.00 100.00 1.71e-78 DBJ BAE01321 "unnamed protein product [Macaca fascicularis]" 100.00 313 100.00 100.00 1.85e-78 DBJ BAG57017 "unnamed protein product [Homo sapiens]" 100.00 291 100.00 100.00 2.06e-77 DBJ BAG73729 "small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha [synthetic construct]" 100.00 313 100.00 100.00 1.92e-78 EMBL CAA11565 "small glutamine-rich tetratricopeptide (SGT) [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 EMBL CAB39725 "small glutamine-rich tetratricopeptide repeat containing protein [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 EMBL CAB43297 "hypothetical protein [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 EMBL CAG38548 "SGTA [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 EMBL CAG47077 "SGTA [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 GB AAD13117 "small glutamine-rich tetratricopeptide (SGT) [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 GB AAH00390 "Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 GB AAH02989 "Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 GB AAH05165 "Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 GB AAH08885 "Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 PIR T08782 "hypothetical protein DKFZp586N1020.1 - human (fragment)" 100.00 349 100.00 100.00 6.00e-78 REF NP_001181661 "small glutamine-rich tetratricopeptide repeat-containing protein alpha [Macaca mulatta]" 100.00 313 100.00 100.00 2.16e-78 REF NP_003012 "small glutamine-rich tetratricopeptide repeat-containing protein alpha [Homo sapiens]" 100.00 313 100.00 100.00 1.92e-78 REF XP_001914923 "PREDICTED: small glutamine-rich tetratricopeptide repeat-containing protein alpha-like [Equus caballus]" 64.41 166 98.68 100.00 3.36e-47 REF XP_002761612 "PREDICTED: small glutamine-rich tetratricopeptide repeat-containing protein alpha [Callithrix jacchus]" 100.00 313 100.00 100.00 1.38e-78 REF XP_002923601 "PREDICTED: small glutamine-rich tetratricopeptide repeat-containing protein alpha-like [Ailuropoda melanoleuca]" 100.00 313 97.46 98.31 5.45e-77 SP O43765 "RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha; AltName: Full=Alpha-SGT; AltName: Full=Vp" 100.00 313 100.00 100.00 1.92e-78 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TPR_monomer Human 9606 Eukaryota Metazoa Homo sapiens 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 $TPR_monomer '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 $TPR_monomer . mM 0.5 1.5 '[U-95% 13C; U-90% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'TPR monomer' _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 . 1 ALA N N 122.54 0.05 1 2 . 1 ALA H H 8.29 0.03 1 3 . 1 ALA HA H 3.87 0.03 1 4 . 1 ALA HB H 1.75 0.03 1 5 . 1 ALA CA C 55.41 0.05 1 6 . 1 ALA CB C 18.21 0.05 1 7 . 1 ALA C C 178.65 0.05 1 8 . 2 GLU N N 115.79 0.05 1 9 . 2 GLU H H 7.87 0.03 1 10 . 2 GLU HA H 4.03 0.03 1 11 . 2 GLU CA C 58.19 0.05 1 12 . 2 GLU CB C 29.66 0.05 1 13 . 2 GLU C C 179.00 0.05 1 14 . 3 ARG N N 123.41 0.05 1 15 . 3 ARG H H 7.94 0.03 1 16 . 3 ARG CA C 59.34 0.05 1 17 . 3 ARG CB C 29.30 0.05 1 18 . 3 ARG C C 179.06 0.05 1 19 . 4 LEU N N 122.23 0.05 1 20 . 4 LEU H H 7.95 0.03 1 21 . 4 LEU HA H 4.48 0.03 1 22 . 4 LEU HB2 H 2.91 0.03 1 23 . 4 LEU CA C 57.88 0.05 1 24 . 4 LEU CB C 40.95 0.05 1 25 . 4 LEU C C 178.37 0.05 1 26 . 5 LYS N N 121.06 0.05 1 27 . 5 LYS H H 8.37 0.03 1 28 . 5 LYS HA H 3.60 0.03 1 29 . 5 LYS CA C 59.45 0.05 1 30 . 5 LYS CB C 29.64 0.05 1 31 . 5 LYS C C 177.75 0.05 1 32 . 6 THR N N 117.76 0.05 1 33 . 6 THR H H 8.26 0.03 1 34 . 6 THR HA H 4.22 0.03 1 35 . 6 THR CA C 67.07 0.05 1 36 . 7 GLU N N 122.38 0.05 1 37 . 7 GLU H H 7.89 0.03 1 38 . 7 GLU HA H 3.69 0.03 1 39 . 7 GLU CA C 58.89 0.05 1 40 . 7 GLU CB C 27.40 0.05 1 41 . 7 GLU C C 179.47 0.05 1 42 . 8 GLY N N 107.85 0.05 1 43 . 8 GLY H H 8.28 0.03 1 44 . 8 GLY HA2 H 3.16 0.03 1 45 . 8 GLY HA3 H 2.86 0.03 1 46 . 8 GLY CA C 47.97 0.05 1 47 . 8 GLY C C 174.34 0.05 1 48 . 9 ASN N N 121.46 0.05 1 49 . 9 ASN H H 8.69 0.03 1 50 . 9 ASN HA H 4.25 0.03 1 51 . 9 ASN HB2 H 3.33 0.03 1 52 . 9 ASN HB3 H 2.92 0.03 1 53 . 9 ASN CA C 55.35 0.05 1 54 . 9 ASN CB C 36.69 0.05 1 55 . 9 ASN C C 174.37 0.05 1 56 . 10 GLU N N 122.11 0.05 1 57 . 10 GLU H H 8.24 0.03 1 58 . 10 GLU HA H 4.02 0.03 1 59 . 10 GLU HB2 H 2.22 0.03 1 60 . 10 GLU CA C 58.67 0.05 1 61 . 10 GLU CB C 28.23 0.05 1 62 . 11 GLN N N 118.30 0.05 1 63 . 11 GLN H H 7.82 0.03 1 64 . 11 GLN HA H 4.08 0.03 1 65 . 11 GLN CA C 56.76 0.05 1 66 . 11 GLN CB C 26.16 0.05 1 67 . 11 GLN C C 178.60 0.05 1 68 . 12 MET N N 118.95 0.05 1 69 . 12 MET H H 8.21 0.03 1 70 . 12 MET HA H 4.06 0.03 1 71 . 12 MET CA C 57.10 0.05 1 72 . 12 MET CB C 30.20 0.05 1 73 . 12 MET C C 180.37 0.05 1 74 . 13 LYS N N 119.70 0.05 1 75 . 13 LYS H H 7.52 0.03 1 76 . 13 LYS HA H 3.98 0.03 1 77 . 13 LYS HB2 H 1.95 0.03 1 78 . 13 LYS CA C 59.00 0.05 1 79 . 13 LYS CB C 32.22 0.05 1 80 . 13 LYS C C 177.87 0.05 1 81 . 14 VAL N N 108.40 0.05 1 82 . 14 VAL H H 6.92 0.03 1 83 . 14 VAL HA H 4.37 0.03 1 84 . 14 VAL HB H 2.51 0.03 1 85 . 14 VAL CA C 59.87 0.05 1 86 . 14 VAL C C 174.25 0.05 1 87 . 15 GLU N N 114.21 0.05 1 88 . 15 GLU H H 7.47 0.03 1 89 . 15 GLU HA H 4.05 0.03 1 90 . 15 GLU HB2 H 2.68 0.03 1 91 . 15 GLU HB3 H 2.08 0.03 1 92 . 15 GLU CA C 56.50 0.05 1 93 . 15 GLU CB C 25.05 0.05 1 94 . 15 GLU C C 173.94 0.05 1 95 . 16 ASN N N 118.26 0.05 1 96 . 16 ASN H H 7.92 0.03 1 97 . 16 ASN HA H 4.85 0.03 1 98 . 16 ASN HB2 H 3.38 0.03 1 99 . 16 ASN HB3 H 2.45 0.03 1 100 . 16 ASN CA C 49.91 0.05 1 101 . 16 ASN CB C 38.38 0.05 1 102 . 16 ASN C C 175.62 0.05 1 103 . 17 PHE N N 120.41 0.05 1 104 . 17 PHE H H 7.02 0.03 1 105 . 17 PHE HA H 4.20 0.03 1 106 . 17 PHE HB2 H 2.77 0.03 1 107 . 17 PHE CA C 59.90 0.05 1 108 . 17 PHE CB C 37.82 0.05 1 109 . 17 PHE C C 177.51 0.05 1 110 . 18 GLU N N 118.80 0.05 1 111 . 18 GLU H H 9.06 0.03 1 112 . 18 GLU HA H 3.89 0.03 1 113 . 18 GLU HB2 H 1.99 0.03 1 114 . 18 GLU CA C 59.56 0.05 1 115 . 18 GLU CB C 28.74 0.05 1 116 . 18 GLU C C 179.00 0.05 1 117 . 19 ALA N N 121.99 0.05 1 118 . 19 ALA H H 7.45 0.03 1 119 . 19 ALA HA H 3.99 0.03 1 120 . 19 ALA HB H 1.29 0.03 1 121 . 19 ALA CA C 54.07 0.05 1 122 . 19 ALA CB C 17.98 0.05 1 123 . 19 ALA C C 179.30 0.05 1 124 . 20 ALA N N 120.52 0.05 1 125 . 20 ALA H H 7.92 0.03 1 126 . 20 ALA HA H 3.66 0.03 1 127 . 20 ALA HB H 1.42 0.03 1 128 . 20 ALA CA C 55.89 0.05 1 129 . 20 ALA CB C 17.76 0.05 1 130 . 20 ALA C C 177.52 0.05 1 131 . 21 VAL N N 116.24 0.05 1 132 . 21 VAL H H 8.11 0.03 1 133 . 21 VAL HA H 3.11 0.03 1 134 . 21 VAL HB H 2.18 0.03 1 135 . 21 VAL CA C 67.74 0.05 1 136 . 21 VAL CB C 31.54 0.05 1 137 . 21 VAL C C 178.52 0.05 1 138 . 22 HIS N N 119.64 0.05 1 139 . 22 HIS H H 7.42 0.03 1 140 . 22 HIS HA H 4.09 0.03 1 141 . 22 HIS HB2 H 2.90 0.03 1 142 . 22 HIS CA C 59.00 0.05 1 143 . 22 HIS CB C 28.74 0.05 1 144 . 22 HIS C C 177.60 0.05 1 145 . 23 PHE N N 119.03 0.05 1 146 . 23 PHE H H 8.10 0.03 1 147 . 23 PHE HA H 3.81 0.03 1 148 . 23 PHE HB2 H 3.16 0.03 1 149 . 23 PHE CA C 62.81 0.05 1 150 . 23 PHE CB C 37.73 0.05 1 151 . 23 PHE C C 178.21 0.05 1 152 . 24 TYR N N 116.74 0.05 1 153 . 24 TYR H H 8.80 0.03 1 154 . 24 TYR HA H 4.20 0.03 1 155 . 24 TYR CA C 58.44 0.05 1 156 . 24 TYR CB C 37.03 0.05 1 157 . 24 TYR C C 178.13 0.05 1 158 . 25 GLY N N 105.20 0.05 1 159 . 25 GLY H H 8.30 0.03 1 160 . 25 GLY HA2 H 3.64 0.03 1 161 . 25 GLY CA C 47.07 0.05 1 162 . 25 GLY C C 176.21 0.05 1 163 . 26 LYS N N 122.22 0.05 1 164 . 26 LYS H H 7.57 0.03 1 165 . 26 LYS HA H 3.93 0.03 1 166 . 26 LYS HB2 H 1.81 0.03 1 167 . 26 LYS CA C 57.77 0.05 1 168 . 26 LYS CB C 31.54 0.05 1 169 . 26 LYS C C 178.34 0.05 1 170 . 27 ALA N N 123.92 0.05 1 171 . 27 ALA H H 7.77 0.03 1 172 . 27 ALA HA H 3.71 0.03 1 173 . 27 ALA HB H 0.83 0.03 1 174 . 27 ALA CA C 55.41 0.05 1 175 . 27 ALA CB C 15.85 0.05 1 176 . 27 ALA C C 178.34 0.05 1 177 . 28 ILE N N 118.52 0.05 1 178 . 28 ILE H H 7.80 0.03 1 179 . 28 ILE HA H 3.42 0.03 1 180 . 28 ILE CA C 64.16 0.05 1 181 . 28 ILE CB C 38.60 0.05 1 182 . 28 ILE C C 176.67 0.05 1 183 . 29 GLU N N 117.07 0.05 1 184 . 29 GLU H H 7.47 0.03 1 185 . 29 GLU HA H 3.83 0.03 1 186 . 29 GLU HB2 H 2.02 0.03 1 187 . 29 GLU CA C 58.66 0.05 1 188 . 29 GLU CB C 29.37 0.05 1 189 . 29 GLU C C 178.49 0.05 1 190 . 30 LEU N N 116.45 0.05 1 191 . 30 LEU H H 7.12 0.03 1 192 . 30 LEU HA H 4.16 0.03 1 193 . 30 LEU HB2 H 1.46 0.03 1 194 . 30 LEU CA C 55.75 0.05 1 195 . 30 LEU CB C 43.20 0.05 1 196 . 30 LEU C C 177.39 0.05 1 197 . 31 ASN N N 114.14 0.05 1 198 . 31 ASN H H 8.23 0.03 1 199 . 31 ASN HA H 5.05 0.03 1 200 . 31 ASN CA C 50.10 0.05 1 201 . 31 ASN CB C 43.25 0.05 1 202 . 31 ASN C C 174.43 0.05 1 203 . 32 PRO HA H 4.76 0.03 1 204 . 32 PRO HB2 H 2.39 0.03 1 205 . 32 PRO CA C 63.04 0.05 1 206 . 32 PRO CB C 31.00 0.05 1 207 . 32 PRO C C 175.51 0.05 1 208 . 33 ALA N N 122.22 0.05 1 209 . 33 ALA H H 7.52 0.03 1 210 . 33 ALA HA H 4.52 0.03 1 211 . 33 ALA HB H 1.33 0.03 1 212 . 33 ALA CA C 50.26 0.05 1 213 . 33 ALA CB C 18.21 0.05 1 214 . 33 ALA C C 175.05 0.05 1 215 . 34 ASN N N 118.04 0.05 1 216 . 34 ASN H H 7.55 0.03 1 217 . 34 ASN HA H 4.56 0.03 1 218 . 34 ASN HB2 H 2.31 0.03 1 219 . 34 ASN HB3 H 1.85 0.03 1 220 . 34 ASN CA C 51.72 0.05 1 221 . 34 ASN CB C 39.05 0.05 1 222 . 34 ASN C C 174.82 0.05 1 223 . 35 ALA N N 127.67 0.05 1 224 . 35 ALA H H 9.03 0.03 1 225 . 35 ALA HA H 3.89 0.03 1 226 . 35 ALA HB H 1.36 0.03 1 227 . 35 ALA CA C 55.19 0.05 1 228 . 35 ALA CB C 19.44 0.05 1 229 . 35 ALA C C 178.52 0.05 1 230 . 36 VAL N N 116.06 0.05 1 231 . 36 VAL H H 7.68 0.03 1 232 . 36 VAL HA H 3.52 0.03 1 233 . 36 VAL CA C 65.05 0.05 1 234 . 36 VAL CB C 30.87 0.05 1 235 . 36 VAL C C 178.24 0.05 1 236 . 37 TYR N N 117.47 0.05 1 237 . 37 TYR H H 6.93 0.03 1 238 . 37 TYR HA H 4.04 0.03 1 239 . 37 TYR HB2 H 2.82 0.03 1 240 . 37 TYR CA C 57.43 0.05 1 241 . 37 TYR CB C 36.03 0.05 1 242 . 37 TYR C C 177.97 0.05 1 243 . 38 PHE N N 115.36 0.05 1 244 . 38 PHE H H 6.77 0.03 1 245 . 38 PHE HA H 4.01 0.03 1 246 . 38 PHE HB2 H 3.02 0.03 1 247 . 38 PHE CA C 62.23 0.05 1 248 . 38 PHE CB C 39.65 0.05 1 249 . 38 PHE C C 177.12 0.05 1 250 . 39 CYS N N 119.03 0.05 1 251 . 39 CYS H H 8.10 0.03 1 252 . 39 CYS HA H 3.92 0.03 1 253 . 39 CYS HB2 H 3.24 0.03 1 254 . 39 CYS HB3 H 2.83 0.03 1 255 . 39 CYS CA C 62.37 0.05 1 256 . 39 CYS CB C 26.96 0.05 1 257 . 39 CYS C C 176.53 0.05 1 258 . 40 ASN N N 119.97 0.05 1 259 . 40 ASN H H 8.67 0.03 1 260 . 40 ASN HA H 4.10 0.03 1 261 . 40 ASN CA C 55.08 0.05 1 262 . 40 ASN CB C 35.02 0.05 1 263 . 40 ASN C C 177.01 0.05 1 264 . 41 ARG N N 122.39 0.05 1 265 . 41 ARG H H 7.82 0.03 1 266 . 41 ARG HA H 3.66 0.03 1 267 . 41 ARG HB2 H 2.74 0.03 1 268 . 41 ARG CA C 61.08 0.05 1 269 . 41 ARG CB C 28.74 0.05 1 270 . 41 ARG C C 177.12 0.05 1 271 . 42 ALA N N 120.83 0.05 1 272 . 42 ALA H H 8.51 0.03 1 273 . 42 ALA HA H 4.13 0.03 1 274 . 42 ALA HB H 1.71 0.03 1 275 . 42 ALA CA C 55.53 0.05 1 276 . 42 ALA CB C 19.33 0.05 1 277 . 42 ALA C C 180.00 0.05 1 278 . 43 ALA N N 120.98 0.05 1 279 . 43 ALA H H 7.73 0.03 1 280 . 43 ALA HA H 3.94 0.03 1 281 . 43 ALA HB H 1.50 0.03 1 282 . 43 ALA CA C 54.97 0.05 1 283 . 43 ALA CB C 17.42 0.05 1 284 . 43 ALA C C 179.65 0.05 1 285 . 44 ALA N N 122.54 0.05 1 286 . 44 ALA H H 7.52 0.03 1 287 . 44 ALA HA H 3.81 0.03 1 288 . 44 ALA HB H 1.72 0.03 1 289 . 44 ALA CA C 55.53 0.05 1 290 . 44 ALA CB C 18.77 0.05 1 291 . 44 ALA C C 178.71 0.05 1 292 . 45 TYR N N 116.59 0.05 1 293 . 45 TYR H H 9.08 0.03 1 294 . 45 TYR HA H 4.38 0.03 1 295 . 45 TYR HB2 H 3.53 0.03 1 296 . 45 TYR HB3 H 2.86 0.03 1 297 . 45 TYR CA C 58.33 0.05 1 298 . 45 TYR CB C 36.36 0.05 1 299 . 45 TYR C C 179.67 0.05 1 300 . 46 SER N N 115.90 0.05 1 301 . 46 SER H H 8.38 0.03 1 302 . 46 SER HA H 3.91 0.03 1 303 . 46 SER CA C 57.96 0.05 1 304 . 46 SER CB C 62.12 0.05 1 305 . 46 SER C C 176.78 0.05 1 306 . 47 LYS N N 121.79 0.05 1 307 . 47 LYS H H 7.28 0.03 1 308 . 47 LYS HA H 3.73 0.03 1 309 . 47 LYS CA C 56.55 0.05 1 310 . 47 LYS CB C 29.67 0.05 1 311 . 47 LYS C C 178.02 0.05 1 312 . 48 LEU N N 117.40 0.05 1 313 . 48 LEU H H 7.15 0.03 1 314 . 48 LEU HA H 4.24 0.03 1 315 . 48 LEU HB2 H 1.82 0.03 1 316 . 48 LEU CA C 54.74 0.05 1 317 . 48 LEU CB C 42.86 0.05 1 318 . 48 LEU C C 176.80 0.05 1 319 . 49 GLY N N 107.70 0.05 1 320 . 49 GLY H H 7.50 0.03 1 321 . 49 GLY HA2 H 3.94 0.03 1 322 . 49 GLY HA3 H 2.95 0.03 1 323 . 49 GLY CA C 44.37 0.05 1 324 . 49 GLY C C 172.90 0.05 1 325 . 50 ASN N N 119.50 0.05 1 326 . 50 ASN H H 7.97 0.03 1 327 . 50 ASN HA H 4.74 0.03 1 328 . 50 ASN HB2 H 2.51 0.03 1 329 . 50 ASN CA C 49.14 0.05 1 330 . 50 ASN C C 175.19 0.05 1 331 . 51 TYR N N 121.90 0.05 1 332 . 51 TYR H H 7.05 0.03 1 333 . 51 TYR HA H 3.99 0.03 1 334 . 51 TYR HB2 H 3.09 0.03 1 335 . 51 TYR HB3 H 2.56 0.03 1 336 . 51 TYR CA C 60.23 0.05 1 337 . 51 TYR CB C 37.03 0.05 1 338 . 51 TYR C C 177.28 0.05 1 339 . 52 ALA N N 121.37 0.05 1 340 . 52 ALA H H 8.83 0.03 1 341 . 52 ALA HA H 3.93 0.03 1 342 . 52 ALA HB H 1.31 0.03 1 343 . 52 ALA CA C 54.85 0.05 1 344 . 52 ALA CB C 17.31 0.05 1 345 . 52 ALA C C 180.39 0.05 1 346 . 53 GLY N N 106.76 0.05 1 347 . 53 GLY H H 7.34 0.03 1 348 . 53 GLY HA2 H 3.46 0.03 1 349 . 53 GLY HA3 H 2.61 0.03 1 350 . 53 GLY CA C 46.51 0.05 1 351 . 53 GLY C C 175.54 0.05 1 352 . 54 ALA N N 123.79 0.05 1 353 . 54 ALA H H 7.50 0.03 1 354 . 54 ALA HA H 4.18 0.03 1 355 . 54 ALA HB H 1.56 0.03 1 356 . 54 ALA CA C 55.41 0.05 1 357 . 54 ALA CB C 18.09 0.05 1 358 . 54 ALA C C 178.78 0.05 1 359 . 55 VAL N N 119.27 0.05 1 360 . 55 VAL H H 8.33 0.03 1 361 . 55 VAL HA H 3.45 0.03 1 362 . 55 VAL HB H 2.07 0.03 1 363 . 55 VAL CA C 66.17 0.05 1 364 . 55 VAL CB C 31.40 0.05 1 365 . 55 VAL C C 177.36 0.05 1 366 . 56 GLN N N 117.15 0.05 1 367 . 56 GLN H H 7.38 0.03 1 368 . 56 GLN HA H 3.93 0.03 1 369 . 56 GLN HB2 H 2.06 0.03 1 370 . 56 GLN CA C 58.51 0.05 1 371 . 56 GLN CB C 28.29 0.05 1 372 . 56 GLN C C 178.91 0.05 1 373 . 57 ASP N N 121.30 0.05 1 374 . 57 ASP H H 7.90 0.03 1 375 . 57 ASP HA H 4.63 0.03 1 376 . 57 ASP HB2 H 3.20 0.03 1 377 . 57 ASP CA C 57.43 0.05 1 378 . 57 ASP CB C 40.19 0.05 1 379 . 57 ASP C C 179.21 0.05 1 380 . 58 CYS N N 119.42 0.05 1 381 . 58 CYS H H 8.50 0.03 1 382 . 58 CYS HA H 3.85 0.03 1 383 . 58 CYS HB2 H 2.38 0.03 1 384 . 58 CYS CA C 65.16 0.05 1 385 . 58 CYS CB C 26.90 0.05 1 386 . 58 CYS C C 176.14 0.05 1 387 . 59 GLU N N 119.97 0.05 1 388 . 59 GLU H H 8.39 0.03 1 389 . 59 GLU HA H 3.61 0.03 1 390 . 59 GLU HB2 H 1.97 0.03 1 391 . 59 GLU CA C 59.23 0.05 1 392 . 59 GLU CB C 29.08 0.05 1 393 . 59 GLU C C 178.91 0.05 1 394 . 60 ARG N N 118.87 0.05 1 395 . 60 ARG H H 7.32 0.03 1 396 . 60 ARG HA H 3.62 0.03 1 397 . 60 ARG HB2 H 1.33 0.03 1 398 . 60 ARG CA C 58.10 0.05 1 399 . 60 ARG CB C 28.29 0.05 1 400 . 60 ARG C C 177.89 0.05 1 401 . 61 ALA N N 120.44 0.05 1 402 . 61 ALA H H 7.98 0.03 1 403 . 61 ALA HA H 3.69 0.03 1 404 . 61 ALA HB H 1.52 0.03 1 405 . 61 ALA CA C 55.53 0.05 1 406 . 61 ALA CB C 18.88 0.05 1 407 . 61 ALA C C 177.65 0.05 1 408 . 62 ILE N N 116.69 0.05 1 409 . 62 ILE H H 7.87 0.03 1 410 . 62 ILE HA H 3.40 0.03 1 411 . 62 ILE HB H 1.50 0.03 1 412 . 62 ILE CA C 63.82 0.05 1 413 . 62 ILE CB C 38.00 0.05 1 414 . 62 ILE C C 176.82 0.05 1 415 . 63 CYS N N 116.92 0.05 1 416 . 63 CYS H H 7.36 0.03 1 417 . 63 CYS HA H 3.95 0.03 1 418 . 63 CYS HB2 H 2.84 0.03 1 419 . 63 CYS CA C 62.14 0.05 1 420 . 63 CYS CB C 26.16 0.05 1 421 . 63 CYS C C 176.62 0.05 1 422 . 64 ILE N N 119.11 0.05 1 423 . 64 ILE H H 7.56 0.03 1 424 . 64 ILE HA H 3.59 0.03 1 425 . 64 ILE HB H 1.63 0.03 1 426 . 64 ILE CA C 63.71 0.05 1 427 . 64 ILE CB C 38.46 0.05 1 428 . 64 ILE C C 176.17 0.05 1 429 . 65 ASP N N 115.98 0.05 1 430 . 65 ASP H H 8.40 0.03 1 431 . 65 ASP CA C 50.10 0.05 1 432 . 65 ASP CB C 42.00 0.05 1 433 . 65 ASP C C 172.70 0.05 1 434 . 66 PRO HA H 4.72 0.03 1 435 . 66 PRO HB2 H 2.42 0.03 1 436 . 66 PRO HB3 H 1.99 0.03 1 437 . 66 PRO CA C 62.70 0.05 1 438 . 66 PRO CB C 31.99 0.05 1 439 . 66 PRO C C 177.86 0.05 1 440 . 67 ALA N N 123.25 0.05 1 441 . 67 ALA H H 8.25 0.03 1 442 . 67 ALA HA H 4.62 0.03 1 443 . 67 ALA HB H 1.49 0.03 1 444 . 67 ALA CA C 51.04 0.05 1 445 . 67 ALA CB C 18.32 0.05 1 446 . 67 ALA C C 176.15 0.05 1 447 . 68 TYR N N 122.23 0.05 1 448 . 68 TYR H H 7.69 0.03 1 449 . 68 TYR HA H 4.85 0.03 1 450 . 68 TYR CA C 55.53 0.05 1 451 . 68 TYR CB C 36.03 0.05 1 452 . 68 TYR C C 175.71 0.05 1 453 . 69 SER N N 125.66 0.05 1 454 . 69 SER H H 8.53 0.03 1 455 . 69 SER HA H 4.05 0.03 1 456 . 69 SER CA C 61.69 0.05 1 457 . 69 SER CB C 63.35 0.05 1 458 . 69 SER C C 175.66 0.05 1 459 . 70 LYS N N 119.42 0.05 1 460 . 70 LYS H H 7.39 0.03 1 461 . 70 LYS HA H 4.10 0.03 1 462 . 70 LYS HB2 H 1.44 0.03 1 463 . 70 LYS CA C 58.33 0.05 1 464 . 70 LYS CB C 32.33 0.05 1 465 . 70 LYS C C 177.97 0.05 1 466 . 71 ALA N N 118.87 0.05 1 467 . 71 ALA H H 7.02 0.03 1 468 . 71 ALA HA H 4.02 0.03 1 469 . 71 ALA HB H 1.21 0.03 1 470 . 71 ALA CA C 54.85 0.05 1 471 . 71 ALA CB C 18.88 0.05 1 472 . 71 ALA C C 178.58 0.05 1 473 . 72 TYR N N 115.90 0.05 1 474 . 72 TYR H H 7.07 0.03 1 475 . 72 TYR HA H 3.73 0.03 1 476 . 72 TYR CA C 61.58 0.05 1 477 . 72 TYR CB C 37.15 0.05 1 478 . 72 TYR C C 177.76 0.05 1 479 . 73 GLY N N 105.24 0.05 1 480 . 73 GLY H H 7.79 0.03 1 481 . 73 GLY HA2 H 3.89 0.03 1 482 . 73 GLY HA3 H 2.64 0.03 1 483 . 73 GLY CA C 47.18 0.05 1 484 . 73 GLY C C 175.19 0.05 1 485 . 74 ARG N N 121.12 0.05 1 486 . 74 ARG H H 8.24 0.05 1 487 . 74 ARG HA H 3.97 0.03 1 488 . 74 ARG CA C 57.33 0.05 1 489 . 74 ARG CB C 28.00 0.05 1 490 . 74 ARG C C 177.47 0.05 1 491 . 75 MET N N 122.36 0.05 1 492 . 75 MET H H 7.80 0.03 1 493 . 75 MET HA H 3.74 0.03 1 494 . 75 MET CA C 57.99 0.05 1 495 . 75 MET CB C 31.88 0.05 1 496 . 75 MET C C 177.65 0.05 1 497 . 76 GLY N N 105.35 0.05 1 498 . 76 GLY H H 7.81 0.03 1 499 . 76 GLY HA2 H 3.03 0.03 1 500 . 76 GLY HA3 H 2.40 0.03 1 501 . 76 GLY CA C 47.18 0.05 1 502 . 76 GLY C C 174.06 0.05 1 503 . 77 LEU N N 122.39 0.05 1 504 . 77 LEU H H 7.50 0.03 1 505 . 77 LEU HA H 4.19 0.03 1 506 . 77 LEU HB2 H 1.60 0.03 1 507 . 77 LEU CA C 57.54 0.05 1 508 . 77 LEU CB C 42.19 0.05 1 509 . 77 LEU C C 179.97 0.05 1 510 . 78 ALA N N 124.26 0.05 1 511 . 78 ALA H H 8.09 0.03 1 512 . 78 ALA HA H 3.79 0.03 1 513 . 78 ALA HB H 1.38 0.03 1 514 . 78 ALA CA C 54.90 0.05 1 515 . 78 ALA CB C 18.09 0.05 1 516 . 78 ALA C C 178.52 0.05 1 517 . 79 LEU N N 116.98 0.05 1 518 . 79 LEU H H 8.41 0.03 1 519 . 79 LEU HA H 3.72 0.03 1 520 . 79 LEU CA C 57.32 0.05 1 521 . 79 LEU CB C 40.62 0.05 1 522 . 79 LEU C C 180.08 0.05 1 523 . 80 SER N N 117.86 0.05 1 524 . 80 SER H H 8.65 0.03 1 525 . 80 SER HA H 3.97 0.03 1 526 . 80 SER CA C 62.92 0.05 1 527 . 80 SER CB C 61.61 0.05 1 528 . 80 SER C C 177.91 0.05 1 529 . 81 SER N N 120.20 0.05 1 530 . 81 SER H H 7.69 0.03 1 531 . 81 SER HA H 4.80 0.03 1 532 . 81 SER HB2 H 3.89 0.03 1 533 . 81 SER CA C 60.92 0.05 1 534 . 81 SER C C 174.21 0.05 1 535 . 82 LEU N N 120.59 0.05 1 536 . 82 LEU H H 7.03 0.03 1 537 . 82 LEU HA H 4.12 0.03 1 538 . 82 LEU HB2 H 1.60 0.03 1 539 . 82 LEU CA C 54.18 0.05 1 540 . 82 LEU CB C 42.41 0.05 1 541 . 82 LEU C C 175.08 0.05 1 542 . 83 ASN N N 113.87 0.05 1 543 . 83 ASN H H 7.79 0.03 1 544 . 83 ASN HA H 3.70 0.03 1 545 . 83 ASN HB2 H 2.96 0.03 1 546 . 83 ASN CA C 54.14 0.05 1 547 . 83 ASN CB C 36.40 0.05 1 548 . 83 ASN C C 174.05 0.05 1 549 . 84 LYS N N 121.60 0.05 1 550 . 84 LYS H H 7.90 0.03 1 551 . 84 LYS HA H 4.48 0.03 1 552 . 84 LYS HB2 H 1.82 0.03 1 553 . 84 LYS CA C 53.73 0.05 1 554 . 84 LYS CB C 29.73 0.05 1 555 . 84 LYS C C 176.10 0.05 1 556 . 85 HIS N N 118.10 0.05 1 557 . 85 HIS H H 6.85 0.03 1 558 . 85 HIS HA H 4.06 0.03 1 559 . 85 HIS HB2 H 2.98 0.03 1 560 . 85 HIS CA C 60.07 0.05 1 561 . 85 HIS CB C 30.87 0.05 1 562 . 85 HIS C C 177.45 0.05 1 563 . 86 VAL N N 119.07 0.05 1 564 . 86 VAL H H 8.28 0.03 1 565 . 86 VAL HA H 3.58 0.03 1 566 . 86 VAL HB H 2.01 0.03 1 567 . 86 VAL CA C 66.17 0.05 1 568 . 86 VAL CB C 30.98 0.05 1 569 . 86 VAL C C 178.39 0.05 1 570 . 87 GLU N N 121.37 0.05 1 571 . 87 GLU H H 8.72 0.03 1 572 . 87 GLU HA H 4.00 0.03 1 573 . 87 GLU HB2 H 1.32 0.03 1 574 . 87 GLU CA C 59.45 0.05 1 575 . 87 GLU CB C 29.19 0.05 1 576 . 87 GLU C C 178.30 0.05 1 577 . 88 ALA N N 120.75 0.05 1 578 . 88 ALA H H 8.27 0.03 1 579 . 88 ALA HA H 3.77 0.03 1 580 . 88 ALA HB H 1.47 0.03 1 581 . 88 ALA CA C 55.64 0.05 1 582 . 88 ALA CB C 18.00 0.05 1 583 . 88 ALA C C 178.87 0.05 1 584 . 89 VAL N N 115.18 0.05 1 585 . 89 VAL H H 7.85 0.03 1 586 . 89 VAL HA H 3.54 0.03 1 587 . 89 VAL HB H 2.19 0.03 1 588 . 89 VAL CA C 67.29 0.05 1 589 . 89 VAL CB C 31.34 0.05 1 590 . 89 VAL C C 176.58 0.05 1 591 . 90 ALA N N 119.43 0.05 1 592 . 90 ALA H H 7.23 0.03 1 593 . 90 ALA HA H 3.88 0.03 1 594 . 90 ALA HB H 1.28 0.03 1 595 . 90 ALA CA C 54.85 0.05 1 596 . 90 ALA CB C 17.65 0.05 1 597 . 90 ALA C C 180.83 0.05 1 598 . 91 TYR N N 117.07 0.05 1 599 . 91 TYR H H 7.57 0.03 1 600 . 91 TYR HA H 3.94 0.03 1 601 . 91 TYR CA C 63.60 0.05 1 602 . 91 TYR CB C 36.81 0.05 1 603 . 91 TYR C C 177.89 0.05 1 604 . 92 TYR N N 118.86 0.05 1 605 . 92 TYR H H 8.54 0.03 1 606 . 92 TYR HA H 4.13 0.03 1 607 . 92 TYR HB2 H 2.93 0.03 1 608 . 92 TYR CA C 60.79 0.05 1 609 . 92 TYR CB C 38.72 0.05 1 610 . 92 TYR C C 178.54 0.05 1 611 . 93 LYS N N 117.62 0.05 1 612 . 93 LYS H H 8.54 0.03 1 613 . 93 LYS HA H 3.82 0.03 1 614 . 93 LYS HB2 H 1.75 0.03 1 615 . 93 LYS CA C 60.32 0.05 1 616 . 93 LYS CB C 31.77 0.05 1 617 . 93 LYS C C 179.00 0.05 1 618 . 94 LYS N N 120.42 0.05 1 619 . 94 LYS H H 7.33 0.03 1 620 . 94 LYS HA H 3.81 0.03 1 621 . 94 LYS HB2 H 1.26 0.03 1 622 . 94 LYS CA C 57.54 0.05 1 623 . 94 LYS CB C 31.21 0.05 1 624 . 94 LYS C C 177.73 0.05 1 625 . 95 ALA N N 121.05 0.05 1 626 . 95 ALA H H 8.03 0.03 1 627 . 95 ALA HA H 3.55 0.03 1 628 . 95 ALA HB H 0.09 0.03 1 629 . 95 ALA CA C 54.97 0.05 1 630 . 95 ALA CB C 16.86 0.05 1 631 . 95 ALA C C 178.82 0.05 1 632 . 96 LEU N N 115.83 0.05 1 633 . 96 LEU H H 7.70 0.03 1 634 . 96 LEU HA H 4.14 0.03 1 635 . 96 LEU HB2 H 1.60 0.03 1 636 . 96 LEU CA C 55.86 0.05 1 637 . 96 LEU CB C 42.46 0.05 1 638 . 96 LEU C C 178.36 0.05 1 639 . 97 GLU N N 119.73 0.03 1 640 . 97 GLU H H 7.71 0.03 1 641 . 97 GLU HA H 3.85 0.03 1 642 . 97 GLU HB2 H 2.03 0.03 1 643 . 97 GLU CA C 58.78 0.05 1 644 . 97 GLU CB C 29.30 0.05 1 645 . 97 GLU C C 178.52 0.05 1 646 . 98 LEU N N 116.29 0.05 1 647 . 98 LEU H H 7.14 0.03 1 648 . 98 LEU HA H 4.20 0.03 1 649 . 98 LEU HB2 H 1.61 0.03 1 650 . 98 LEU CA C 55.75 0.05 1 651 . 98 LEU CB C 43.20 0.05 1 652 . 98 LEU C C 176.65 0.05 1 653 . 99 ASP N N 120.44 0.05 1 654 . 99 ASP H H 8.14 0.03 1 655 . 99 ASP HA H 5.02 0.03 1 656 . 99 ASP CA C 51.27 0.05 1 657 . 99 ASP CB C 40.73 0.05 1 658 . 99 ASP C C 177.17 0.05 1 659 . 100 PRO HA H 4.72 0.03 1 660 . 100 PRO HB2 H 2.28 0.03 1 661 . 100 PRO HB3 H 1.82 0.03 1 662 . 100 PRO CA C 64.58 0.05 1 663 . 100 PRO CB C 32.24 0.05 1 664 . 100 PRO C C 175.51 0.05 1 665 . 101 ASP N N 115.69 0.05 1 666 . 101 ASP H H 8.22 0.03 1 667 . 101 ASP HA H 4.60 0.03 1 668 . 101 ASP HB2 H 2.81 0.03 1 669 . 101 ASP HB3 H 2.48 0.03 1 670 . 101 ASP CA C 53.25 0.05 1 671 . 101 ASP CB C 40.55 0.05 1 672 . 101 ASP C C 175.45 0.05 1 673 . 102 ASN N N 119.46 0.05 1 674 . 102 ASN H H 7.19 0.03 1 675 . 102 ASN HA H 4.16 0.03 1 676 . 102 ASN HB2 H 2.65 0.03 1 677 . 102 ASN HB3 H 2.29 0.03 1 678 . 102 ASN CA C 54.07 0.05 1 679 . 102 ASN CB C 38.38 0.05 1 680 . 102 ASN C C 175.30 0.05 1 681 . 103 GLU N N 128.37 0.05 1 682 . 103 GLU H H 8.78 0.03 1 683 . 103 GLU HA H 3.79 0.03 1 684 . 103 GLU HB2 H 1.98 0.03 1 685 . 103 GLU CA C 58.66 0.05 1 686 . 103 GLU CB C 29.19 0.05 1 687 . 103 GLU C C 178.54 0.05 1 688 . 104 THR N N 118.33 0.05 1 689 . 104 THR H H 7.98 0.03 1 690 . 104 THR HA H 3.93 0.03 1 691 . 104 THR CA C 65.73 0.05 1 692 . 104 THR CB C 67.41 0.05 1 693 . 104 THR C C 176.99 0.05 1 694 . 105 TYR N N 121.21 0.05 1 695 . 105 TYR H H 7.61 0.03 1 696 . 105 TYR HA H 4.31 0.03 1 697 . 105 TYR HB2 H 3.09 0.03 1 698 . 105 TYR CA C 57.10 0.05 1 699 . 105 TYR CB C 35.35 0.05 1 700 . 105 TYR C C 177.99 0.05 1 701 . 106 LYS N N 118.52 0.05 1 702 . 106 LYS H H 7.83 0.03 1 703 . 106 LYS HA H 3.69 0.03 1 704 . 106 LYS HB2 H 1.82 0.03 1 705 . 106 LYS CA C 60.35 0.05 1 706 . 106 LYS CB C 32.55 0.05 1 707 . 106 LYS C C 178.91 0.05 1 708 . 107 SER N N 115.00 0.05 1 709 . 107 SER H H 8.11 0.03 1 710 . 107 SER HA H 3.93 0.03 1 711 . 107 SER CA C 60.66 0.05 1 712 . 107 SER CB C 62.23 0.05 1 713 . 107 SER C C 176.40 0.05 1 714 . 108 ASN N N 120.06 0.05 1 715 . 108 ASN H H 8.20 0.03 1 716 . 108 ASN HA H 4.21 0.03 1 717 . 108 ASN HB2 H 2.26 0.03 1 718 . 108 ASN CA C 55.53 0.05 1 719 . 108 ASN CB C 36.92 0.05 1 720 . 108 ASN C C 177.38 0.05 1 721 . 109 LEU N N 122.23 0.05 1 722 . 109 LEU H H 7.92 0.03 1 723 . 109 LEU HA H 3.77 0.03 1 724 . 109 LEU HB2 H 1.85 0.03 1 725 . 109 LEU HB3 H 1.24 0.03 1 726 . 109 LEU CA C 58.05 0.05 1 727 . 109 LEU CB C 40.96 0.05 1 728 . 109 LEU C C 176.54 0.05 1 729 . 110 LYS N N 118.25 0.05 1 730 . 110 LYS H H 7.35 0.03 1 731 . 110 LYS HA H 3.99 0.03 1 732 . 110 LYS HB2 H 1.85 0.03 1 733 . 110 LYS CA C 58.89 0.05 1 734 . 110 LYS CB C 31.54 0.05 1 735 . 110 LYS C C 178.95 0.05 1 736 . 111 ILE N N 118.01 0.05 1 737 . 111 ILE H H 7.51 0.03 1 738 . 111 ILE HA H 3.96 0.03 1 739 . 111 ILE CA C 64.27 0.05 1 740 . 111 ILE CB C 37.82 0.05 1 741 . 111 ILE C C 177.71 0.05 1 742 . 112 ALA N N 122.87 0.05 1 743 . 112 ALA H H 7.67 0.03 1 744 . 112 ALA HA H 3.98 0.03 1 745 . 112 ALA HB H 1.58 0.03 1 746 . 112 ALA CA C 55.08 0.05 1 747 . 112 ALA CB C 18.66 0.05 1 748 . 112 ALA C C 179.41 0.05 1 749 . 113 GLU N N 116.07 0.05 1 750 . 113 GLU H H 8.56 0.03 1 751 . 113 GLU HA H 3.80 0.03 1 752 . 113 GLU HB2 H 2.11 0.03 1 753 . 113 GLU HB3 H 1.94 0.03 1 754 . 113 GLU CA C 59.43 0.05 1 755 . 113 GLU CB C 29.43 0.05 1 756 . 113 GLU C C 179.87 0.05 1 757 . 114 LEU N N 119.96 0.05 1 758 . 114 LEU H H 7.73 0.03 1 759 . 114 LEU HA H 3.98 0.03 1 760 . 114 LEU HB2 H 1.82 0.03 1 761 . 114 LEU HB3 H 1.55 0.03 1 762 . 114 LEU CA C 57.10 0.05 1 763 . 114 LEU CB C 41.41 0.05 1 764 . 114 LEU C C 179.58 0.05 1 765 . 115 LYS N N 118.79 0.05 1 766 . 115 LYS H H 7.63 0.03 1 767 . 115 LYS HA H 3.90 0.03 1 768 . 115 LYS HB2 H 1.58 0.03 1 769 . 115 LYS HB3 H 1.27 0.03 1 770 . 115 LYS CA C 56.76 0.05 1 771 . 115 LYS CB C 30.87 0.05 1 772 . 115 LYS C C 177.80 0.05 1 773 . 116 LEU N N 117.23 0.05 1 774 . 116 LEU H H 7.33 0.03 1 775 . 116 LEU HA H 4.16 0.03 1 776 . 116 LEU HB2 H 1.76 0.03 1 777 . 116 LEU HB3 H 1.63 0.03 1 778 . 116 LEU CA C 55.41 0.05 1 779 . 116 LEU CB C 41.52 0.05 1 780 . 116 LEU C C 177.14 0.05 1 781 . 117 ARG N N 118.47 0.05 1 782 . 117 ARG H H 7.46 0.03 1 783 . 117 ARG HA H 4.29 0.03 1 784 . 117 ARG HB2 H 1.85 0.03 1 785 . 117 ARG CA C 55.53 0.05 1 786 . 117 ARG CB C 30.53 0.05 1 787 . 117 ARG C C 175.14 0.05 1 788 . 118 GLU N N 126.60 0.05 1 789 . 118 GLU H H 7.58 0.03 1 790 . 118 GLU HA H 3.95 0.03 1 791 . 118 GLU CA C 58.10 0.05 1 792 . 118 GLU CB C 30.53 0.05 1 793 . 118 GLU C C 180.93 0.05 1 stop_ save_