data_16537 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) ; _BMRB_accession_number 16537 _BMRB_flat_file_name bmr16537.str _Entry_type original _Submission_date 2009-10-04 _Accession_date 2009-10-04 _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 Andersson Fredrik I. . 2 Jackson Sophie E. . 3 Hsu 'Shang-Te Danny' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 295 "13C chemical shifts" 597 "15N chemical shifts" 203 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-20 update BMRB 'update related entry loop' 2010-05-20 update BMRB 'complete entry citation' 2009-12-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17260 'UCHL1 S18Y variant' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20012716 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Andersson Fredrik I. . 2 Jackson Sophie E. . 3 Hsu 'Shang-Te Danny' . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 41 _Page_last 43 _Year 2010 _Details . loop_ _Keyword de-ubiquitination 'knotted protein' 'Parkinson's disease' 'ubiquitin C-terminal hydrolase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name UCH-L1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label UCH-L1 $UCH-L1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'ubiquitin C-terminal hydrolases' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UCH-L1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common UCH-L1 _Molecular_mass . _Mol_thiol_state unknown _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 223 _Mol_residue_sequence ; MQLKPMEINPEMLNKVLSRL GVAGQWRFVDVLGLEEESLG SVPAPACALLLLFPLTAQHE NFRKKQIEELKGQEVSPKVY FMKQTIGNSCGTIGLIHAVA NNQDKLGFEDGSVLKQFLSE TEKMSPEDRAKCFEKNEAIQ AAHDAVAQEGQCRVDDKVNF HFILFNNVDGHLYELDGRMP FPVNHGASSEDTLLKDAAKV CREFTEREQGEVRFSAVALC KAA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 LEU 4 LYS 5 PRO 6 MET 7 GLU 8 ILE 9 ASN 10 PRO 11 GLU 12 MET 13 LEU 14 ASN 15 LYS 16 VAL 17 LEU 18 SER 19 ARG 20 LEU 21 GLY 22 VAL 23 ALA 24 GLY 25 GLN 26 TRP 27 ARG 28 PHE 29 VAL 30 ASP 31 VAL 32 LEU 33 GLY 34 LEU 35 GLU 36 GLU 37 GLU 38 SER 39 LEU 40 GLY 41 SER 42 VAL 43 PRO 44 ALA 45 PRO 46 ALA 47 CYS 48 ALA 49 LEU 50 LEU 51 LEU 52 LEU 53 PHE 54 PRO 55 LEU 56 THR 57 ALA 58 GLN 59 HIS 60 GLU 61 ASN 62 PHE 63 ARG 64 LYS 65 LYS 66 GLN 67 ILE 68 GLU 69 GLU 70 LEU 71 LYS 72 GLY 73 GLN 74 GLU 75 VAL 76 SER 77 PRO 78 LYS 79 VAL 80 TYR 81 PHE 82 MET 83 LYS 84 GLN 85 THR 86 ILE 87 GLY 88 ASN 89 SER 90 CYS 91 GLY 92 THR 93 ILE 94 GLY 95 LEU 96 ILE 97 HIS 98 ALA 99 VAL 100 ALA 101 ASN 102 ASN 103 GLN 104 ASP 105 LYS 106 LEU 107 GLY 108 PHE 109 GLU 110 ASP 111 GLY 112 SER 113 VAL 114 LEU 115 LYS 116 GLN 117 PHE 118 LEU 119 SER 120 GLU 121 THR 122 GLU 123 LYS 124 MET 125 SER 126 PRO 127 GLU 128 ASP 129 ARG 130 ALA 131 LYS 132 CYS 133 PHE 134 GLU 135 LYS 136 ASN 137 GLU 138 ALA 139 ILE 140 GLN 141 ALA 142 ALA 143 HIS 144 ASP 145 ALA 146 VAL 147 ALA 148 GLN 149 GLU 150 GLY 151 GLN 152 CYS 153 ARG 154 VAL 155 ASP 156 ASP 157 LYS 158 VAL 159 ASN 160 PHE 161 HIS 162 PHE 163 ILE 164 LEU 165 PHE 166 ASN 167 ASN 168 VAL 169 ASP 170 GLY 171 HIS 172 LEU 173 TYR 174 GLU 175 LEU 176 ASP 177 GLY 178 ARG 179 MET 180 PRO 181 PHE 182 PRO 183 VAL 184 ASN 185 HIS 186 GLY 187 ALA 188 SER 189 SER 190 GLU 191 ASP 192 THR 193 LEU 194 LEU 195 LYS 196 ASP 197 ALA 198 ALA 199 LYS 200 VAL 201 CYS 202 ARG 203 GLU 204 PHE 205 THR 206 GLU 207 ARG 208 GLU 209 GLN 210 GLY 211 GLU 212 VAL 213 ARG 214 PHE 215 SER 216 ALA 217 VAL 218 ALA 219 LEU 220 CYS 221 LYS 222 ALA 223 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-13 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 BMRB 17260 UCHL1_S18Y_variant 100.00 231 99.55 99.55 1.38e-161 PDB 2ETL "Crystal Structure Of Ubiquitin Carboxy-terminal Hydrolase L1 (uch-l1)" 100.00 228 100.00 100.00 2.00e-162 PDB 2LEN "Solution Structure Of Uchl1 S18y Variant" 100.00 231 99.55 99.55 1.38e-161 PDB 3IFW "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." 100.00 228 99.55 99.55 1.45e-161 PDB 3IRT "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy-Te Hydrolase L1" 100.00 228 99.55 100.00 5.78e-162 PDB 3KVF "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" 100.00 228 99.55 100.00 5.78e-162 PDB 3KW5 "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" 100.00 228 100.00 100.00 2.00e-162 PDB 4DM9 "The Crystal Structure Of Ubiquitin Carboxy-Terminal Hydrolase L1 (Uchl1) Bound To A Tripeptide Fluoromethyl Ketone Z-Vae(Ome)-F" 100.00 228 100.00 100.00 2.00e-162 PDB 4JKJ "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy-terminal Hydrolase L1" 100.00 228 99.55 99.55 1.45e-161 DBJ BAA28214 "PGP9.5 [Equus caballus]" 62.33 139 98.56 99.28 2.98e-95 DBJ BAB33087 "hypothetical protein [Macaca fascicularis]" 63.68 142 98.59 99.30 4.63e-97 DBJ BAD51987 "ubiquitin carboxyl-terminal esterase L1 [Macaca fascicularis]" 100.00 223 98.65 99.55 1.95e-160 DBJ BAE87282 "unnamed protein product [Macaca fascicularis]" 100.00 223 99.10 99.55 3.54e-161 DBJ BAG37761 "unnamed protein product [Homo sapiens]" 100.00 223 99.10 99.10 9.79e-161 EMBL CAA28443 "unnamed protein product [Homo sapiens]" 95.07 212 100.00 100.00 9.54e-154 GB AAD09172 "ubiquitin carboxy-terminal hydrolase L1 [Homo sapiens]" 93.27 208 100.00 100.00 2.18e-150 GB AAH00332 "Ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase) [Homo sapiens]" 100.00 223 100.00 100.00 8.96e-163 GB AAH05117 "Ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase) [Homo sapiens]" 100.00 223 100.00 100.00 8.96e-163 GB AAH06305 "Ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase) [Homo sapiens]" 100.00 223 100.00 100.00 8.96e-163 GB AAY40923 "unknown [Homo sapiens]" 100.00 223 100.00 100.00 8.96e-163 REF NP_004172 "ubiquitin carboxyl-terminal hydrolase isozyme L1 [Homo sapiens]" 100.00 223 100.00 100.00 8.96e-163 REF XP_001097839 "PREDICTED: ubiquitin carboxyl-terminal hydrolase isozyme L1-like [Macaca mulatta]" 100.00 219 97.31 97.76 1.92e-155 REF XP_002745940 "PREDICTED: ubiquitin carboxyl-terminal hydrolase isozyme L1 [Callithrix jacchus]" 100.00 223 99.10 99.55 1.26e-161 REF XP_002814743 "PREDICTED: ubiquitin carboxyl-terminal hydrolase isozyme L1 [Pongo abelii]" 100.00 223 100.00 100.00 8.96e-163 REF XP_003258669 "PREDICTED: ubiquitin carboxyl-terminal hydrolase isozyme L1 isoform X3 [Nomascus leucogenys]" 100.00 223 99.55 100.00 2.37e-162 SP P09936 "RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1; Short=UCH-L1; AltName: Full=Neuron cytoplasmic protein 9.5; Alt" 100.00 223 100.00 100.00 8.96e-163 SP Q60HC8 "RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1; Short=UCH-L1; AltName: Full=Ubiquitin thioesterase L1; Flags: P" 100.00 223 98.65 99.55 1.95e-160 SP Q9GM50 "RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1; Short=UCH-L1; AltName: Full=Neuron cytoplasmic protein 9.5; Alt" 100.00 223 97.31 99.10 2.68e-158 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $UCH-L1 Human 9606 Eukaryota Metazoa Homo sapiens 'The expression of UCH-L1 is specifically located to neurons and it constitutes up to 1-2 % of the total protein content in human brain.' 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 $UCH-L1 'recombinant technology' . Escherichia coli 'Rosetta BL21' pGEX 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 $UCH-L1 . mM 0.2 0.4 '[U-98% 13C; U-98% 15N]' TRIS 50 mM . . 'natural abundance' EDTA 0.5 mM . . 'natural abundance' DTT 5 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_700 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_600 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_800 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' . . M pH 7.6 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water C 13 protons ppm 4.755 internal indirect . . . 0.251449530 water H 1 protons ppm 4.755 internal direct . . . 1.0 water N 15 protons ppm 4.755 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '3D HNCO' '3D HN(CA)CO' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name UCH-L1 _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 1 MET C C 175.4 . 1 2 1 1 MET CA C 54.2 . 1 3 1 1 MET CB C 32.8 . 1 4 2 2 GLN H H 8.351 . 1 5 2 2 GLN C C 174.6 . 1 6 2 2 GLN CA C 55.13 . 1 7 2 2 GLN CB C 31.58 . 1 8 2 2 GLN N N 120.4 . 1 9 3 3 LEU H H 7.668 . 1 10 3 3 LEU HA H 4.501 . 1 11 3 3 LEU C C 176.9 . 1 12 3 3 LEU CA C 53.5 . 1 13 3 3 LEU CB C 41.98 . 1 14 3 3 LEU N N 122.2 . 1 15 4 4 LYS H H 9.587 . 1 16 4 4 LYS C C 174.7 . 1 17 4 4 LYS CA C 55.41 . 1 18 4 4 LYS CB C 32.76 . 1 19 4 4 LYS N N 123 . 1 20 5 5 PRO C C 175.2 . 1 21 5 5 PRO CA C 62.78 . 1 22 5 5 PRO CB C 31.85 . 1 23 6 6 MET H H 8.131 . 1 24 6 6 MET HA H 4.39 . 1 25 6 6 MET C C 174.6 . 1 26 6 6 MET CA C 54.01 . 1 27 6 6 MET CB C 37.25 . 1 28 6 6 MET N N 119.5 . 1 29 7 7 GLU H H 8.623 . 1 30 7 7 GLU C C 174.3 . 1 31 7 7 GLU CA C 56.51 . 1 32 7 7 GLU CB C 29.99 . 1 33 7 7 GLU N N 126.9 . 1 34 8 8 ILE H H 8.025 . 1 35 8 8 ILE HA H 3.336 . 1 36 8 8 ILE C C 176.8 . 1 37 8 8 ILE CA C 61.14 . 1 38 8 8 ILE CB C 42.36 . 1 39 8 8 ILE N N 123 . 1 40 9 9 ASN H H 7.883 . 1 41 9 9 ASN C C 177.9 . 1 42 9 9 ASN CA C 58.98 . 1 43 9 9 ASN CB C 37.14 . 1 44 9 9 ASN N N 121.4 . 1 45 10 10 PRO C C 176 . 1 46 10 10 PRO CA C 66.97 . 1 47 10 10 PRO CB C 31.4 . 1 48 11 11 GLU H H 7.981 . 1 49 11 11 GLU HA H 3.946 . 1 50 11 11 GLU C C 179.9 . 1 51 11 11 GLU CA C 59.88 . 1 52 11 11 GLU CB C 29.11 . 1 53 11 11 GLU N N 117 . 1 54 12 12 MET H H 8.346 . 1 55 12 12 MET C C 179.1 . 1 56 12 12 MET CA C 57.06 . 1 57 12 12 MET CB C 31.9 . 1 58 12 12 MET N N 117.2 . 1 59 13 13 LEU H H 8.098 . 1 60 13 13 LEU C C 179.3 . 1 61 13 13 LEU CA C 57.54 . 1 62 13 13 LEU CB C 42.45 . 1 63 13 13 LEU N N 117.6 . 1 64 14 14 ASN H H 9.023 . 1 65 14 14 ASN C C 179.2 . 1 66 14 14 ASN CA C 56.05 . 1 67 14 14 ASN CB C 37.33 . 1 68 14 14 ASN N N 117.5 . 1 69 15 15 LYS H H 7.718 . 1 70 15 15 LYS HA H 4.116 . 1 71 15 15 LYS C C 179.9 . 1 72 15 15 LYS CA C 60.32 . 1 73 15 15 LYS CB C 33.45 . 1 74 15 15 LYS N N 122.4 . 1 75 16 16 VAL H H 8.018 . 1 76 16 16 VAL HA H 3.363 . 1 77 16 16 VAL C C 177.5 . 1 78 16 16 VAL CA C 68.2 . 1 79 16 16 VAL CB C 30.8 . 1 80 16 16 VAL N N 121.2 . 1 81 17 17 LEU H H 8.656 . 1 82 17 17 LEU C C 178.6 . 1 83 17 17 LEU CA C 58.94 . 1 84 17 17 LEU CB C 42.88 . 1 85 17 17 LEU N N 119.5 . 1 86 18 18 SER H H 7.706 . 1 87 18 18 SER HA H 4.319 . 1 88 18 18 SER C C 179.3 . 1 89 18 18 SER CA C 61.53 . 1 90 18 18 SER CB C 63.15 . 1 91 18 18 SER N N 110.9 . 1 92 19 19 ARG H H 8.266 . 1 93 19 19 ARG C C 178.5 . 1 94 19 19 ARG CA C 58.47 . 1 95 19 19 ARG CB C 30.28 . 1 96 19 19 ARG N N 123 . 1 97 20 20 LEU H H 8.224 . 1 98 20 20 LEU C C 177.2 . 1 99 20 20 LEU CA C 54.81 . 1 100 20 20 LEU CB C 41.21 . 1 101 20 20 LEU N N 115.4 . 1 102 21 21 GLY H H 8.131 . 1 103 21 21 GLY C C 173.2 . 1 104 21 21 GLY CA C 47.29 . 1 105 21 21 GLY N N 109.1 . 1 106 22 22 VAL H H 7.989 . 1 107 22 22 VAL C C 175.3 . 1 108 22 22 VAL CA C 62.73 . 1 109 22 22 VAL CB C 31.4 . 1 110 22 22 VAL N N 121.8 . 1 111 23 23 ALA H H 8.387 . 1 112 23 23 ALA HA H 4.387 . 1 113 23 23 ALA C C 178.2 . 1 114 23 23 ALA CA C 52.3 . 1 115 23 23 ALA CB C 20.42 . 1 116 23 23 ALA N N 132 . 1 117 24 24 GLY H H 8.556 . 1 118 24 24 GLY C C 174.7 . 1 119 24 24 GLY CA C 46.36 . 1 120 24 24 GLY N N 107.3 . 1 121 25 25 GLN C C 174.9 . 1 122 25 25 GLN CA C 57.75 . 1 123 25 25 GLN CB C 29.25 . 1 124 26 26 TRP H H 7.649 . 1 125 26 26 TRP HA H 5.128 . 1 126 26 26 TRP C C 175 . 1 127 26 26 TRP CA C 56.07 . 1 128 26 26 TRP CB C 29.31 . 1 129 26 26 TRP N N 119 . 1 130 27 27 ARG H H 9.07 . 1 131 27 27 ARG HA H 4.284 . 1 132 27 27 ARG C C 175.2 . 1 133 27 27 ARG CA C 53.83 . 1 134 27 27 ARG CB C 34.79 . 1 135 27 27 ARG N N 119.6 . 1 136 28 28 PHE H H 10.29 . 1 137 28 28 PHE C C 177.2 . 1 138 28 28 PHE CA C 58.86 . 1 139 28 28 PHE CB C 40.01 . 1 140 28 28 PHE N N 121 . 1 141 29 29 VAL H H 9.343 . 1 142 29 29 VAL HA H 4.593 . 1 143 29 29 VAL C C 174.9 . 1 144 29 29 VAL CA C 59.59 . 1 145 29 29 VAL CB C 36.25 . 1 146 29 29 VAL N N 116.1 . 1 147 30 30 ASP H H 8.745 . 1 148 30 30 ASP HA H 4.645 . 1 149 30 30 ASP C C 175.2 . 1 150 30 30 ASP CA C 56.18 . 1 151 30 30 ASP CB C 42.74 . 1 152 30 30 ASP N N 122.5 . 1 153 31 31 VAL H H 7.947 . 1 154 31 31 VAL HA H 4.05 . 1 155 31 31 VAL C C 176 . 1 156 31 31 VAL CA C 61.7 . 1 157 31 31 VAL CB C 32.29 . 1 158 31 31 VAL N N 122.5 . 1 159 32 32 LEU H H 8.922 . 1 160 32 32 LEU HA H 4.124 . 1 161 32 32 LEU C C 176.8 . 1 162 32 32 LEU CA C 56.94 . 1 163 32 32 LEU CB C 41.38 . 1 164 32 32 LEU N N 127.9 . 1 165 33 33 GLY H H 7.357 . 1 166 33 33 GLY HA2 H 4.028 . 2 167 33 33 GLY HA3 H 4.028 . 2 168 33 33 GLY C C 171 . 1 169 33 33 GLY CA C 44.8 . 1 170 33 33 GLY N N 105.8 . 1 171 34 34 LEU H H 8.227 . 1 172 34 34 LEU HA H 4.252 . 1 173 34 34 LEU C C 176.9 . 1 174 34 34 LEU CA C 53.66 . 1 175 34 34 LEU CB C 42.93 . 1 176 34 34 LEU N N 115.6 . 1 177 35 35 GLU H H 7.966 . 1 178 35 35 GLU HA H 4.106 . 1 179 35 35 GLU C C 177.7 . 1 180 35 35 GLU CA C 56.49 . 1 181 35 35 GLU CB C 29.33 . 1 182 35 35 GLU N N 117.7 . 1 183 36 36 GLU H H 8.949 . 1 184 36 36 GLU C C 179.2 . 1 185 36 36 GLU CA C 60.74 . 1 186 36 36 GLU CB C 29.5 . 1 187 36 36 GLU N N 122.9 . 1 188 37 37 GLU H H 9.184 . 1 189 37 37 GLU C C 178.4 . 1 190 37 37 GLU CA C 59.31 . 1 191 37 37 GLU CB C 29.02 . 1 192 37 37 GLU N N 117.1 . 1 193 38 38 SER H H 7.593 . 1 194 38 38 SER HA H 4.353 . 1 195 38 38 SER C C 176.5 . 1 196 38 38 SER CA C 60.12 . 1 197 38 38 SER CB C 63.27 . 1 198 38 38 SER N N 115.4 . 1 199 39 39 LEU H H 7.646 . 1 200 39 39 LEU HA H 4.024 . 1 201 39 39 LEU C C 179.1 . 1 202 39 39 LEU CA C 56.94 . 1 203 39 39 LEU CB C 41.17 . 1 204 39 39 LEU N N 121.1 . 1 205 40 40 GLY H H 8.005 . 1 206 40 40 GLY C C 174.2 . 1 207 40 40 GLY CA C 46.74 . 1 208 40 40 GLY N N 105.7 . 1 209 41 41 SER H H 7.424 . 1 210 41 41 SER C C 174.4 . 1 211 41 41 SER CA C 58.71 . 1 212 41 41 SER CB C 63.76 . 1 213 41 41 SER N N 112.9 . 1 214 42 42 VAL H H 7.293 . 1 215 42 42 VAL HA H 4.206 . 1 216 42 42 VAL C C 172.2 . 1 217 42 42 VAL CA C 60.5 . 1 218 42 42 VAL CB C 32.55 . 1 219 42 42 VAL N N 125.9 . 1 220 44 44 ALA N N 123.1 . 1 221 45 45 PRO C C 174.3 . 1 222 45 45 PRO CA C 62.43 . 1 223 45 45 PRO CB C 35.26 . 1 224 46 46 ALA H H 8.47 . 1 225 46 46 ALA HA H 5.437 . 1 226 46 46 ALA C C 177.5 . 1 227 46 46 ALA CA C 50.93 . 1 228 46 46 ALA CB C 22.38 . 1 229 46 46 ALA N N 121.7 . 1 230 47 47 CYS H H 9.022 . 1 231 47 47 CYS HA H 5.061 . 1 232 47 47 CYS C C 173.1 . 1 233 47 47 CYS CA C 56.5 . 1 234 47 47 CYS CB C 30.48 . 1 235 47 47 CYS N N 113.6 . 1 236 48 48 ALA H H 7.412 . 1 237 48 48 ALA C C 175 . 1 238 48 48 ALA CA C 52.81 . 1 239 48 48 ALA CB C 23.18 . 1 240 48 48 ALA N N 121.6 . 1 241 49 49 LEU H H 8.542 . 1 242 49 49 LEU HA H 5.108 . 1 243 49 49 LEU C C 173.8 . 1 244 49 49 LEU CA C 52.81 . 1 245 49 49 LEU CB C 45.86 . 1 246 49 49 LEU N N 123.2 . 1 247 50 50 LEU H H 9.752 . 1 248 50 50 LEU HA H 5.463 . 1 249 50 50 LEU C C 173.6 . 1 250 50 50 LEU CA C 55.86 . 1 251 50 50 LEU CB C 43.58 . 1 252 50 50 LEU N N 127.3 . 1 253 51 51 LEU H H 8.121 . 1 254 51 51 LEU C C 173.6 . 1 255 51 51 LEU CA C 53.64 . 1 256 51 51 LEU CB C 47.07 . 1 257 51 51 LEU N N 122.9 . 1 258 52 52 LEU H H 9.588 . 1 259 52 52 LEU C C 175.8 . 1 260 52 52 LEU CA C 54.29 . 1 261 52 52 LEU CB C 45.14 . 1 262 52 52 LEU N N 130.9 . 1 263 53 53 PHE H H 9.002 . 1 264 53 53 PHE C C 170.9 . 1 265 53 53 PHE N N 122.9 . 1 266 54 54 PRO C C 176.9 . 1 267 55 55 LEU H H 9.587 . 1 268 55 55 LEU C C 174.7 . 1 269 55 55 LEU CA C 55.41 . 1 270 55 55 LEU N N 123 . 1 271 56 56 THR H H 7.459 . 1 272 56 56 THR C C 178.4 . 1 273 56 56 THR CA C 58.95 . 1 274 56 56 THR CB C 66.14 . 1 275 56 56 THR N N 106.7 . 1 276 57 57 ALA H H 8.636 . 1 277 57 57 ALA HA H 3.733 . 1 278 57 57 ALA C C 180.4 . 1 279 57 57 ALA CA C 55.24 . 1 280 57 57 ALA CB C 18.66 . 1 281 57 57 ALA N N 121.6 . 1 282 58 58 GLN H H 7.829 . 1 283 58 58 GLN HA H 4.104 . 1 284 58 58 GLN C C 176.9 . 1 285 58 58 GLN CA C 57.57 . 1 286 58 58 GLN CB C 29.27 . 1 287 58 58 GLN N N 114.8 . 1 288 59 59 HIS H H 7.759 . 1 289 59 59 HIS HA H 4.177 . 1 290 59 59 HIS C C 177.3 . 1 291 59 59 HIS CA C 59.7 . 1 292 59 59 HIS CB C 29.88 . 1 293 59 59 HIS N N 118.6 . 1 294 60 60 GLU H H 8.117 . 1 295 60 60 GLU C C 180.1 . 1 296 60 60 GLU CA C 60.52 . 1 297 60 60 GLU CB C 29.23 . 1 298 60 60 GLU N N 117.7 . 1 299 61 61 ASN H H 8.157 . 1 300 61 61 ASN C C 177.6 . 1 301 61 61 ASN CA C 56.27 . 1 302 61 61 ASN CB C 38.21 . 1 303 61 61 ASN N N 118.9 . 1 304 62 62 PHE H H 8.341 . 1 305 62 62 PHE C C 177.5 . 1 306 62 62 PHE CA C 61.15 . 1 307 62 62 PHE CB C 38.38 . 1 308 62 62 PHE N N 124.2 . 1 309 63 63 ARG H H 8.497 . 1 310 63 63 ARG C C 178.1 . 1 311 63 63 ARG CA C 57.16 . 1 312 63 63 ARG CB C 31.81 . 1 313 63 63 ARG N N 117.7 . 1 314 64 64 LYS H H 7.586 . 1 315 64 64 LYS C C 179.3 . 1 316 64 64 LYS CA C 60.03 . 1 317 64 64 LYS CB C 32.54 . 1 318 64 64 LYS N N 116.8 . 1 319 65 65 LYS H H 7.107 . 1 320 65 65 LYS HA H 3.95 . 1 321 65 65 LYS C C 177.9 . 1 322 65 65 LYS CA C 58.63 . 1 323 65 65 LYS CB C 32.57 . 1 324 65 65 LYS N N 119.1 . 1 325 66 66 GLN H H 8.27 . 1 326 66 66 GLN C C 178.2 . 1 327 66 66 GLN CA C 55.67 . 1 328 66 66 GLN CB C 29.49 . 1 329 66 66 GLN N N 122.3 . 1 330 67 67 ILE H H 8.502 . 1 331 67 67 ILE HA H 3.597 . 1 332 67 67 ILE C C 178 . 1 333 67 67 ILE CA C 65.81 . 1 334 67 67 ILE CB C 38.6 . 1 335 67 67 ILE N N 117 . 1 336 68 68 GLU H H 6.935 . 1 337 68 68 GLU HA H 4.01 . 1 338 68 68 GLU C C 179 . 1 339 68 68 GLU CA C 58.6 . 1 340 68 68 GLU CB C 29.54 . 1 341 68 68 GLU N N 116.4 . 1 342 69 69 GLU H H 7.873 . 1 343 69 69 GLU HA H 4.046 . 1 344 69 69 GLU C C 178.3 . 1 345 69 69 GLU CA C 58.22 . 1 346 69 69 GLU CB C 29.83 . 1 347 69 69 GLU N N 118.1 . 1 348 70 70 LEU H H 7.838 . 1 349 70 70 LEU HA H 4.215 . 1 350 70 70 LEU C C 176.9 . 1 351 70 70 LEU CA C 54.98 . 1 352 70 70 LEU CB C 42.05 . 1 353 70 70 LEU N N 118.2 . 1 354 71 71 LYS H H 7.204 . 1 355 71 71 LYS HA H 3.852 . 1 356 71 71 LYS C C 177.2 . 1 357 71 71 LYS CA C 58.75 . 1 358 71 71 LYS CB C 32.37 . 1 359 71 71 LYS N N 120 . 1 360 72 72 GLY H H 8.583 . 1 361 72 72 GLY C C 177.8 . 1 362 72 72 GLY CA C 45.13 . 1 363 72 72 GLY N N 110.7 . 1 364 73 73 GLN H H 7.572 . 1 365 73 73 GLN HA H 4.135 . 1 366 73 73 GLN C C 175.1 . 1 367 73 73 GLN CA C 55.94 . 1 368 73 73 GLN CB C 28.54 . 1 369 73 73 GLN N N 119.5 . 1 370 74 74 GLU H H 8.602 . 1 371 74 74 GLU HA H 4.249 . 1 372 74 74 GLU C C 175.3 . 1 373 74 74 GLU CA C 54.47 . 1 374 74 74 GLU CB C 30.89 . 1 375 74 74 GLU N N 124 . 1 376 75 75 VAL H H 8.191 . 1 377 75 75 VAL C C 177.8 . 1 378 75 75 VAL CA C 56.73 . 1 379 75 75 VAL CB C 29.22 . 1 380 75 75 VAL N N 120.3 . 1 381 76 76 SER H H 8.734 . 1 382 76 76 SER C C 173.8 . 1 383 76 76 SER CA C 45.74 . 1 384 76 76 SER N N 110.3 . 1 385 77 77 PRO C C 176.5 . 1 386 77 77 PRO CA C 63.65 . 1 387 77 77 PRO CB C 31.95 . 1 388 78 78 LYS H H 8.114 . 1 389 78 78 LYS HA H 3.997 . 1 390 78 78 LYS C C 177.7 . 1 391 78 78 LYS CA C 56.96 . 1 392 78 78 LYS CB C 33.22 . 1 393 78 78 LYS N N 116.5 . 1 394 79 79 VAL H H 7.079 . 1 395 79 79 VAL C C 175 . 1 396 79 79 VAL CA C 54.65 . 1 397 79 79 VAL CB C 31.55 . 1 398 79 79 VAL N N 118.2 . 1 399 80 80 TYR H H 9.562 . 1 400 80 80 TYR HA H 4.063 . 1 401 80 80 TYR C C 173.4 . 1 402 80 80 TYR CA C 58.8 . 1 403 80 80 TYR CB C 38.32 . 1 404 80 80 TYR N N 133.7 . 1 405 81 81 PHE H H 6.822 . 1 406 81 81 PHE C C 171.8 . 1 407 81 81 PHE CA C 55.5 . 1 408 81 81 PHE CB C 43.41 . 1 409 81 81 PHE N N 128.9 . 1 410 82 82 MET H H 11.96 . 1 411 82 82 MET C C 170.6 . 1 412 82 82 MET CA C 53.72 . 1 413 82 82 MET CB C 38.87 . 1 414 82 82 MET N N 133.2 . 1 415 83 83 LYS H H 5.704 . 1 416 83 83 LYS CA C 54.39 . 1 417 83 83 LYS CB C 32.67 . 1 418 83 83 LYS N N 114.4 . 1 419 90 90 CYS H H 7.531 . 1 420 90 90 CYS C C 177.5 . 1 421 90 90 CYS CA C 61.08 . 1 422 90 90 CYS N N 108.9 . 1 423 91 91 GLY H H 9.363 . 1 424 91 91 GLY C C 173.7 . 1 425 91 91 GLY CA C 47.16 . 1 426 91 91 GLY N N 116.5 . 1 427 92 92 THR H H 6.882 . 1 428 92 92 THR C C 176.1 . 1 429 92 92 THR CB C 67.86 . 1 430 92 92 THR N N 122 . 1 431 93 93 ILE H H 8.753 . 1 432 93 93 ILE C C 177.2 . 1 433 93 93 ILE CA C 63.51 . 1 434 93 93 ILE CB C 36.28 . 1 435 93 93 ILE N N 121.2 . 1 436 94 94 GLY H H 7.986 . 1 437 94 94 GLY C C 174.5 . 1 438 94 94 GLY CA C 47.69 . 1 439 94 94 GLY N N 107.6 . 1 440 95 95 LEU H H 7.929 . 1 441 95 95 LEU C C 178.1 . 1 442 95 95 LEU CA C 60.25 . 1 443 95 95 LEU CB C 42.64 . 1 444 95 95 LEU N N 122.2 . 1 445 96 96 ILE H H 8.732 . 1 446 96 96 ILE C C 177.9 . 1 447 96 96 ILE CA C 67.34 . 1 448 96 96 ILE CB C 37.59 . 1 449 96 96 ILE N N 121.3 . 1 450 97 97 HIS H H 9.104 . 1 451 97 97 HIS C C 178.1 . 1 452 97 97 HIS CA C 59.38 . 1 453 97 97 HIS CB C 30.38 . 1 454 97 97 HIS N N 118.2 . 1 455 98 98 ALA H H 8.617 . 1 456 98 98 ALA C C 178.7 . 1 457 98 98 ALA CA C 55.03 . 1 458 98 98 ALA CB C 17.67 . 1 459 98 98 ALA N N 123.3 . 1 460 99 99 VAL H H 8.379 . 1 461 99 99 VAL C C 178.5 . 1 462 99 99 VAL CA C 65.49 . 1 463 99 99 VAL CB C 32.01 . 1 464 99 99 VAL N N 117.7 . 1 465 100 100 ALA H H 9.262 . 1 466 100 100 ALA C C 179.7 . 1 467 100 100 ALA CA C 54.55 . 1 468 100 100 ALA CB C 20.94 . 1 469 100 100 ALA N N 118.6 . 1 470 101 101 ASN H H 7.16 . 1 471 101 101 ASN C C 173.1 . 1 472 101 101 ASN CA C 54.24 . 1 473 101 101 ASN CB C 39.51 . 1 474 101 101 ASN N N 109.5 . 1 475 102 102 ASN H H 7.669 . 1 476 102 102 ASN C C 175.9 . 1 477 102 102 ASN CA C 54.61 . 1 478 102 102 ASN CB C 40.69 . 1 479 102 102 ASN N N 119 . 1 480 103 103 GLN H H 8.302 . 1 481 103 103 GLN HA H 4.566 . 1 482 103 103 GLN C C 175.3 . 1 483 103 103 GLN CA C 59.96 . 1 484 103 103 GLN CB C 29.87 . 1 485 103 103 GLN N N 120.5 . 1 486 104 104 ASP H H 9.098 . 1 487 104 104 ASP HA H 4.38 . 1 488 104 104 ASP C C 176.3 . 1 489 104 104 ASP CA C 54.98 . 1 490 104 104 ASP CB C 39.51 . 1 491 104 104 ASP N N 115.3 . 1 492 105 105 LYS H H 7.411 . 1 493 105 105 LYS HA H 4.332 . 1 494 105 105 LYS C C 175.4 . 1 495 105 105 LYS CA C 56.87 . 1 496 105 105 LYS CB C 34.54 . 1 497 105 105 LYS N N 117.8 . 1 498 106 106 LEU H H 6.998 . 1 499 106 106 LEU HA H 3.904 . 1 500 106 106 LEU C C 175 . 1 501 106 106 LEU CA C 54.99 . 1 502 106 106 LEU CB C 42.92 . 1 503 106 106 LEU N N 119.6 . 1 504 107 107 GLY H H 7.416 . 1 505 107 107 GLY C C 172.2 . 1 506 107 107 GLY CA C 43.74 . 1 507 107 107 GLY N N 106 . 1 508 108 108 PHE H H 8.529 . 1 509 108 108 PHE C C 176.6 . 1 510 108 108 PHE CA C 57.03 . 1 511 108 108 PHE CB C 42.92 . 1 512 108 108 PHE N N 115.7 . 1 513 109 109 GLU H H 9.117 . 1 514 109 109 GLU C C 177.5 . 1 515 109 109 GLU CA C 55.22 . 1 516 109 109 GLU CB C 30.89 . 1 517 109 109 GLU N N 122.1 . 1 518 110 110 ASP H H 9.008 . 1 519 110 110 ASP C C 177.8 . 1 520 110 110 ASP CB C 40.37 . 1 521 110 110 ASP N N 123.9 . 1 522 111 111 GLY H H 8.886 . 1 523 111 111 GLY C C 174.6 . 1 524 111 111 GLY CA C 45.51 . 1 525 111 111 GLY N N 112.933 . 1 526 112 112 SER H H 7.458 . 1 527 112 112 SER C C 177.9 . 1 528 112 112 SER CA C 58.01 . 1 529 112 112 SER CB C 64.53 . 1 530 112 112 SER N N 112.1 . 1 531 113 113 VAL H H 8.971 . 1 532 113 113 VAL C C 178.9 . 1 533 113 113 VAL CA C 64.33 . 1 534 113 113 VAL N N 128.8 . 1 535 114 114 LEU H H 7.839 . 1 536 114 114 LEU C C 176.8 . 1 537 114 114 LEU CA C 57.03 . 1 538 114 114 LEU CB C 42.65 . 1 539 114 114 LEU N N 121.4 . 1 540 115 115 LYS H H 7.883 . 1 541 115 115 LYS C C 177.9 . 1 542 115 115 LYS CA C 58.98 . 1 543 115 115 LYS CB C 31.86 . 1 544 115 115 LYS N N 121.4 . 1 545 116 116 GLN H H 7.094 . 1 546 116 116 GLN HA H 3.882 . 1 547 116 116 GLN C C 177.7 . 1 548 116 116 GLN CA C 59.06 . 1 549 116 116 GLN CB C 28.16 . 1 550 116 116 GLN N N 116.4 . 1 551 117 117 PHE H H 7.69 . 1 552 117 117 PHE C C 179.1 . 1 553 117 117 PHE CA C 61.28 . 1 554 117 117 PHE CB C 39.98 . 1 555 117 117 PHE N N 120.3 . 1 556 118 118 LEU H H 8.796 . 1 557 118 118 LEU C C 178.4 . 1 558 118 118 LEU CA C 57.8 . 1 559 118 118 LEU CB C 39.9 . 1 560 118 118 LEU N N 122.1 . 1 561 119 119 SER H H 8.018 . 1 562 119 119 SER HA H 4.184 . 1 563 119 119 SER C C 177.4 . 1 564 119 119 SER CA C 61.32 . 1 565 119 119 SER CB C 62.82 . 1 566 119 119 SER N N 115 . 1 567 120 120 GLU H H 8.085 . 1 568 120 120 GLU C C 178.9 . 1 569 120 120 GLU CA C 58.97 . 1 570 120 120 GLU CB C 30.14 . 1 571 120 120 GLU N N 120.8 . 1 572 121 121 THR H H 7.409 . 1 573 121 121 THR C C 176.2 . 1 574 121 121 THR CA C 60.79 . 1 575 121 121 THR N N 120.6 . 1 576 122 122 GLU H H 7.309 . 1 577 122 122 GLU HA H 3.995 . 1 578 122 122 GLU C C 177.1 . 1 579 122 122 GLU CA C 60.91 . 1 580 122 122 GLU CB C 30.49 . 1 581 122 122 GLU N N 126.2 . 1 582 123 123 LYS H H 8.815 . 1 583 123 123 LYS C C 175.5 . 1 584 123 123 LYS CA C 54.87 . 1 585 123 123 LYS CB C 31.91 . 1 586 123 123 LYS N N 117.4 . 1 587 124 124 MET H H 6.778 . 1 588 124 124 MET HA H 4.495 . 1 589 124 124 MET C C 174.9 . 1 590 124 124 MET CA C 55.64 . 1 591 124 124 MET CB C 36.63 . 1 592 124 124 MET N N 119 . 1 593 125 125 SER H H 8.977 . 1 594 125 125 SER C C 173.4 . 1 595 125 125 SER CA C 56.44 . 1 596 125 125 SER CB C 62.93 . 1 597 125 125 SER N N 116.4 . 1 598 126 126 PRO C C 179.5 . 1 599 126 126 PRO CA C 66.33 . 1 600 127 127 GLU H H 8.882 . 1 601 127 127 GLU HA H 3.919 . 1 602 127 127 GLU C C 178.8 . 1 603 127 127 GLU CA C 60.19 . 1 604 127 127 GLU CB C 29.1 . 1 605 127 127 GLU N N 116.9 . 1 606 128 128 ASP H H 8.043 . 1 607 128 128 ASP HA H 4.473 . 1 608 128 128 ASP C C 179.7 . 1 609 128 128 ASP CA C 57.51 . 1 610 128 128 ASP CB C 39.08 . 1 611 128 128 ASP N N 124 . 1 612 129 129 ARG H H 8.92 . 1 613 129 129 ARG C C 178.2 . 1 614 129 129 ARG CA C 60.72 . 1 615 129 129 ARG CB C 30.65 . 1 616 129 129 ARG N N 122 . 1 617 130 130 ALA H H 7.335 . 1 618 130 130 ALA C C 179.4 . 1 619 130 130 ALA CA C 55.31 . 1 620 130 130 ALA CB C 19.18 . 1 621 130 130 ALA N N 120.8 . 1 622 131 131 LYS H H 7.62 . 1 623 131 131 LYS C C 179.4 . 1 624 131 131 LYS CA C 59.42 . 1 625 131 131 LYS CB C 31.97 . 1 626 131 131 LYS N N 117.9 . 1 627 132 132 CYS H H 8.11 . 1 628 132 132 CYS C C 178 . 1 629 132 132 CYS CA C 63.38 . 1 630 132 132 CYS CB C 26.69 . 1 631 132 132 CYS N N 117.9 . 1 632 133 133 PHE H H 8.71 . 1 633 133 133 PHE C C 177.5 . 1 634 133 133 PHE CA C 61.5 . 1 635 133 133 PHE CB C 39.5 . 1 636 133 133 PHE N N 123.3 . 1 637 134 134 GLU H H 8.406 . 1 638 134 134 GLU C C 178 . 1 639 134 134 GLU CA C 59.12 . 1 640 134 134 GLU CB C 29.62 . 1 641 134 134 GLU N N 117.5 . 1 642 135 135 LYS H H 7.031 . 1 643 135 135 LYS HA H 4.314 . 1 644 135 135 LYS C C 175.3 . 1 645 135 135 LYS CA C 55.41 . 1 646 135 135 LYS CB C 33.26 . 1 647 135 135 LYS N N 114.5 . 1 648 136 136 ASN H H 7.436 . 1 649 136 136 ASN HA H 4.902 . 1 650 136 136 ASN C C 173.1 . 1 651 136 136 ASN CA C 54.1 . 1 652 136 136 ASN CB C 37.86 . 1 653 136 136 ASN N N 121.5 . 1 654 137 137 GLU H H 8.145 . 1 655 137 137 GLU C C 178.1 . 1 656 137 137 GLU CA C 58.97 . 1 657 137 137 GLU CB C 30.03 . 1 658 137 137 GLU N N 126.7 . 1 659 138 138 ALA H H 8.226 . 1 660 138 138 ALA HA H 4.116 . 1 661 138 138 ALA C C 181.3 . 1 662 138 138 ALA CA C 55.45 . 1 663 138 138 ALA CB C 18.72 . 1 664 138 138 ALA N N 122.3 . 1 665 139 139 ILE H H 8.879 . 1 666 139 139 ILE C C 177.4 . 1 667 139 139 ILE CA C 65.48 . 1 668 139 139 ILE N N 119.9 . 1 669 140 140 GLN H H 7.053 . 1 670 140 140 GLN C C 177.1 . 1 671 140 140 GLN CA C 59.69 . 1 672 140 140 GLN CB C 27.57 . 1 673 140 140 GLN N N 117.8 . 1 674 141 141 ALA H H 8.473 . 1 675 141 141 ALA C C 180.7 . 1 676 141 141 ALA CA C 54.88 . 1 677 141 141 ALA CB C 18.17 . 1 678 141 141 ALA N N 119.4 . 1 679 142 142 ALA H H 7.601 . 1 680 142 142 ALA HA H 4.054 . 1 681 142 142 ALA C C 178.2 . 1 682 142 142 ALA CA C 55.23 . 1 683 142 142 ALA CB C 18.62 . 1 684 142 142 ALA N N 121.7 . 1 685 143 143 HIS H H 7.864 . 1 686 143 143 HIS C C 177.1 . 1 687 143 143 HIS CA C 60.71 . 1 688 143 143 HIS CB C 31.43 . 1 689 143 143 HIS N N 116.5 . 1 690 144 144 ASP H H 8.632 . 1 691 144 144 ASP C C 178.7 . 1 692 144 144 ASP CA C 57.9 . 1 693 144 144 ASP CB C 40.25 . 1 694 144 144 ASP N N 118.6 . 1 695 145 145 ALA H H 8.349 . 1 696 145 145 ALA C C 180.7 . 1 697 145 145 ALA CA C 55.19 . 1 698 145 145 ALA CB C 18.34 . 1 699 145 145 ALA N N 122.2 . 1 700 146 146 VAL H H 7.545 . 1 701 146 146 VAL HA H 3.512 . 1 702 146 146 VAL C C 178.4 . 1 703 146 146 VAL CA C 66.23 . 1 704 146 146 VAL N N 118.8 . 1 705 147 147 ALA H H 9.023 . 1 706 147 147 ALA C C 179.2 . 1 707 147 147 ALA CA C 56.05 . 1 708 147 147 ALA N N 117.5 . 1 709 148 148 GLN H H 8.628 . 1 710 148 148 GLN C C 178.4 . 1 711 148 148 GLN CA C 59.34 . 1 712 148 148 GLN CB C 27.47 . 1 713 148 148 GLN N N 117.6 . 1 714 149 149 GLU H H 7.759 . 1 715 149 149 GLU HA H 4.177 . 1 716 149 149 GLU C C 177.3 . 1 717 149 149 GLU CA C 57.39 . 1 718 149 149 GLU CB C 29.88 . 1 719 149 149 GLU N N 118.6 . 1 720 150 150 GLY H H 7.624 . 1 721 150 150 GLY C C 173 . 1 722 150 150 GLY CA C 45.04 . 1 723 150 150 GLY N N 106.9 . 1 724 151 151 GLN H H 8.311 . 1 725 151 151 GLN C C 175.5 . 1 726 151 151 GLN CA C 55.76 . 1 727 151 151 GLN CB C 29.53 . 1 728 151 151 GLN N N 118.5 . 1 729 152 152 CYS H H 8.435 . 1 730 152 152 CYS CA C 58.82 . 1 731 152 152 CYS CB C 28.04 . 1 732 152 152 CYS N N 120.7 . 1 733 153 153 ARG H H 8.61 . 1 734 153 153 ARG C C 176 . 1 735 153 153 ARG CA C 55.87 . 1 736 153 153 ARG CB C 31.11 . 1 737 153 153 ARG N N 125.4 . 1 738 154 154 VAL H H 8.274 . 1 739 154 154 VAL HA H 4.001 . 1 740 154 154 VAL C C 175.6 . 1 741 154 154 VAL CA C 62.15 . 1 742 154 154 VAL CB C 32.8 . 1 743 154 154 VAL N N 122.1 . 1 744 155 155 ASP H H 8.445 . 1 745 155 155 ASP HA H 4.544 . 1 746 155 155 ASP C C 175.9 . 1 747 155 155 ASP CA C 54.2 . 1 748 155 155 ASP CB C 41.74 . 1 749 155 155 ASP N N 124.8 . 1 750 156 156 ASP H H 8.316 . 1 751 156 156 ASP HA H 4.447 . 1 752 156 156 ASP C C 176.7 . 1 753 156 156 ASP CA C 54.81 . 1 754 156 156 ASP CB C 41.17 . 1 755 156 156 ASP N N 121.8 . 1 756 157 157 LYS H H 8.415 . 1 757 157 157 LYS C C 176.6 . 1 758 157 157 LYS CA C 56.95 . 1 759 157 157 LYS CB C 32.49 . 1 760 157 157 LYS N N 119.3 . 1 761 158 158 VAL H H 7.632 . 1 762 158 158 VAL HA H 3.899 . 1 763 158 158 VAL C C 174.2 . 1 764 158 158 VAL CA C 61.71 . 1 765 158 158 VAL CB C 33.31 . 1 766 158 158 VAL N N 119.3 . 1 767 159 159 ASN H H 8.47 . 1 768 159 159 ASN C C 174 . 1 769 159 159 ASN CA C 52.33 . 1 770 159 159 ASN CB C 39.58 . 1 771 159 159 ASN N N 122.7 . 1 772 160 160 PHE H H 8.428 . 1 773 160 160 PHE HA H 4.685 . 1 774 160 160 PHE C C 174.8 . 1 775 160 160 PHE CA C 57.84 . 1 776 160 160 PHE CB C 40.81 . 1 777 160 160 PHE N N 121.2 . 1 778 161 161 HIS H H 9.303 . 1 779 161 161 HIS C C 171.4 . 1 780 161 161 HIS CA C 53.52 . 1 781 161 161 HIS N N 123.1 . 1 782 162 162 PHE H H 6.542 . 1 783 162 162 PHE C C 174.5 . 1 784 162 162 PHE N N 103.2 . 1 785 163 163 ILE H H 8.43 . 1 786 163 163 ILE C C 172.1 . 1 787 163 163 ILE CA C 59.65 . 1 788 163 163 ILE N N 118.6 . 1 789 164 164 LEU H H 7.262 . 1 790 164 164 LEU C C 173.1 . 1 791 164 164 LEU CA C 53.8 . 1 792 164 164 LEU CB C 45.85 . 1 793 164 164 LEU N N 120.7 . 1 794 165 165 PHE H H 9.387 . 1 795 165 165 PHE C C 174.3 . 1 796 165 165 PHE CA C 57.06 . 1 797 165 165 PHE CB C 41.83 . 1 798 165 165 PHE N N 122.8 . 1 799 166 166 ASN H H 9.282 . 1 800 166 166 ASN HA H 4.764 . 1 801 166 166 ASN C C 173.2 . 1 802 166 166 ASN CA C 52.78 . 1 803 166 166 ASN CB C 44.27 . 1 804 166 166 ASN N N 120.6 . 1 805 167 167 ASN H H 9.213 . 1 806 167 167 ASN C C 176.5 . 1 807 167 167 ASN CA C 53.36 . 1 808 167 167 ASN CB C 42.02 . 1 809 167 167 ASN N N 125.7 . 1 810 168 168 VAL H H 9.358 . 1 811 168 168 VAL HA H 4.262 . 1 812 168 168 VAL C C 175.9 . 1 813 168 168 VAL CA C 62.33 . 1 814 168 168 VAL CB C 35.26 . 1 815 168 168 VAL N N 124.8 . 1 816 169 169 ASP H H 9.593 . 1 817 169 169 ASP HA H 4.279 . 1 818 169 169 ASP CA C 55.1 . 1 819 169 169 ASP CB C 40.77 . 1 820 169 169 ASP N N 128.5 . 1 821 170 170 GLY H H 8.455 . 1 822 170 170 GLY C C 174 . 1 823 170 170 GLY CA C 46.45 . 1 824 170 170 GLY N N 104.1 . 1 825 171 171 HIS H H 7.848 . 1 826 171 171 HIS HA H 4.808 . 1 827 171 171 HIS C C 172.2 . 1 828 171 171 HIS CA C 55.14 . 1 829 171 171 HIS CB C 32.41 . 1 830 171 171 HIS N N 118.8 . 1 831 172 172 LEU H H 8.589 . 1 832 172 172 LEU HA H 4.77 . 1 833 172 172 LEU C C 174 . 1 834 172 172 LEU CA C 55.08 . 1 835 172 172 LEU CB C 42.28 . 1 836 172 172 LEU N N 122.8 . 1 837 173 173 TYR H H 9.204 . 1 838 173 173 TYR HA H 5.675 . 1 839 173 173 TYR C C 174.4 . 1 840 173 173 TYR CA C 57.11 . 1 841 173 173 TYR CB C 42.53 . 1 842 173 173 TYR N N 124.7 . 1 843 174 174 GLU H H 9.193 . 1 844 174 174 GLU C C 176.5 . 1 845 174 174 GLU CA C 53.06 . 1 846 174 174 GLU CB C 34.2 . 1 847 174 174 GLU N N 122.3 . 1 848 175 175 LEU H H 9.882 . 1 849 175 175 LEU C C 174.7 . 1 850 175 175 LEU CA C 55.83 . 1 851 175 175 LEU CB C 42.94 . 1 852 175 175 LEU N N 129 . 1 853 176 176 ASP H H 9.314 . 1 854 176 176 ASP C C 177.3 . 1 855 176 176 ASP CA C 53.24 . 1 856 176 176 ASP CB C 43.52 . 1 857 176 176 ASP N N 128.4 . 1 858 177 177 GLY H H 9.407 . 1 859 177 177 GLY C C 176.5 . 1 860 177 177 GLY CA C 47.6 . 1 861 177 177 GLY N N 112.9 . 1 862 178 178 ARG H H 7.538 . 1 863 178 178 ARG HA H 4.579 . 1 864 178 178 ARG C C 178.3 . 1 865 178 178 ARG CA C 58 . 1 866 178 178 ARG CB C 29.62 . 1 867 178 178 ARG N N 121.7 . 1 868 179 179 MET H H 7.768 . 1 869 179 179 MET C C 177.3 . 1 870 179 179 MET CA C 49.68 . 1 871 179 179 MET N N 118.2 . 1 872 180 180 PRO C C 175.4 . 1 873 180 180 PRO CA C 62.69 . 1 874 180 180 PRO CB C 31.75 . 1 875 181 181 PHE H H 6.711 . 1 876 181 181 PHE HA H 4.372 . 1 877 181 181 PHE C C 173.2 . 1 878 181 181 PHE CA C 52.35 . 1 879 181 181 PHE CB C 37.45 . 1 880 181 181 PHE N N 113.1 . 1 881 182 182 PRO C C 173.8 . 1 882 182 182 PRO CA C 61.88 . 1 883 182 182 PRO CB C 33.6 . 1 884 183 183 VAL H H 8.561 . 1 885 183 183 VAL C C 174.4 . 1 886 183 183 VAL CA C 61.88 . 1 887 183 183 VAL CB C 34.27 . 1 888 183 183 VAL N N 119.8 . 1 889 184 184 ASN H H 8.598 . 1 890 184 184 ASN HA H 4.187 . 1 891 184 184 ASN C C 176 . 1 892 184 184 ASN CA C 52.23 . 1 893 184 184 ASN CB C 38.59 . 1 894 184 184 ASN N N 125.5 . 1 895 185 185 HIS H H 9.498 . 1 896 185 185 HIS HA H 4.617 . 1 897 185 185 HIS C C 175.8 . 1 898 185 185 HIS CA C 57.64 . 1 899 185 185 HIS CB C 31.39 . 1 900 185 185 HIS N N 126.5 . 1 901 186 186 GLY H H 8.856 . 1 902 186 186 GLY C C 172.3 . 1 903 186 186 GLY CA C 43.83 . 1 904 186 186 GLY N N 110 . 1 905 187 187 ALA H H 8.188 . 1 906 187 187 ALA HA H 4.196 . 1 907 187 187 ALA C C 176.9 . 1 908 187 187 ALA CA C 52.92 . 1 909 187 187 ALA CB C 18.79 . 1 910 187 187 ALA N N 120.4 . 1 911 188 188 SER H H 7.941 . 1 912 188 188 SER HA H 4.248 . 1 913 188 188 SER C C 173.1 . 1 914 188 188 SER CA C 57.18 . 1 915 188 188 SER CB C 64.31 . 1 916 188 188 SER N N 116.1 . 1 917 189 189 SER H H 8.251 . 1 918 189 189 SER HA H 4.645 . 1 919 189 189 SER C C 175.5 . 1 920 189 189 SER CA C 60.75 . 1 921 189 189 SER CB C 65.72 . 1 922 189 189 SER N N 117.7 . 1 923 190 190 GLU H H 7.335 . 1 924 190 190 GLU C C 179.4 . 1 925 190 190 GLU CA C 55.31 . 1 926 190 190 GLU N N 120.8 . 1 927 191 191 ASP H H 8.379 . 1 928 191 191 ASP C C 177.5 . 1 929 191 191 ASP CA C 56.02 . 1 930 191 191 ASP CB C 40.92 . 1 931 191 191 ASP N N 115.4 . 1 932 192 192 THR H H 7.527 . 1 933 192 192 THR HA H 4.567 . 1 934 192 192 THR C C 173.4 . 1 935 192 192 THR CA C 61.24 . 1 936 192 192 THR CB C 68.35 . 1 937 192 192 THR N N 108.7 . 1 938 193 193 LEU H H 7.111 . 1 939 193 193 LEU HA H 3.534 . 1 940 193 193 LEU C C 177.6 . 1 941 193 193 LEU CA C 59.16 . 1 942 193 193 LEU CB C 41.52 . 1 943 193 193 LEU N N 124.2 . 1 944 194 194 LEU H H 8.404 . 1 945 194 194 LEU HA H 3.646 . 1 946 194 194 LEU C C 178.1 . 1 947 194 194 LEU CA C 58.95 . 1 948 194 194 LEU CB C 41.29 . 1 949 194 194 LEU N N 115.8 . 1 950 195 195 LYS H H 7.771 . 1 951 195 195 LYS HA H 3.722 . 1 952 195 195 LYS C C 179.3 . 1 953 195 195 LYS CA C 59.47 . 1 954 195 195 LYS CB C 32.55 . 1 955 195 195 LYS N N 117.7 . 1 956 196 196 ASP H H 8.845 . 1 957 196 196 ASP HA H 4.307 . 1 958 196 196 ASP C C 178.6 . 1 959 196 196 ASP CA C 57.19 . 1 960 196 196 ASP CB C 39.93 . 1 961 196 196 ASP N N 122 . 1 962 197 197 ALA H H 9.119 . 1 963 197 197 ALA HA H 3.503 . 1 964 197 197 ALA C C 179.6 . 1 965 197 197 ALA CA C 54.61 . 1 966 197 197 ALA CB C 19.17 . 1 967 197 197 ALA N N 122.4 . 1 968 198 198 ALA H H 8.726 . 1 969 198 198 ALA C C 178.5 . 1 970 198 198 ALA CA C 55.81 . 1 971 198 198 ALA CB C 18.62 . 1 972 198 198 ALA N N 121.5 . 1 973 199 199 LYS H H 7.204 . 1 974 199 199 LYS HA H 3.707 . 1 975 199 199 LYS C C 178.8 . 1 976 199 199 LYS CA C 60.07 . 1 977 199 199 LYS CB C 32.23 . 1 978 199 199 LYS N N 117 . 1 979 200 200 VAL H H 6.639 . 1 980 200 200 VAL HA H 3.505 . 1 981 200 200 VAL C C 179.4 . 1 982 200 200 VAL CA C 65.25 . 1 983 200 200 VAL CB C 30.7 . 1 984 200 200 VAL N N 118.7 . 1 985 201 201 CYS H H 7.929 . 1 986 201 201 CYS C C 177.3 . 1 987 201 201 CYS CA C 64.36 . 1 988 201 201 CYS CB C 27.6 . 1 989 201 201 CYS N N 117.5 . 1 990 202 202 ARG H H 8.447 . 1 991 202 202 ARG C C 179.1 . 1 992 202 202 ARG CA C 59.69 . 1 993 202 202 ARG CB C 29.58 . 1 994 202 202 ARG N N 118.4 . 1 995 203 203 GLU H H 7.519 . 1 996 203 203 GLU HA H 3.856 . 1 997 203 203 GLU C C 179.5 . 1 998 203 203 GLU CA C 59.45 . 1 999 203 203 GLU CB C 28.6 . 1 1000 203 203 GLU N N 119.9 . 1 1001 204 204 PHE H H 7.636 . 1 1002 204 204 PHE CA C 61.37 . 1 1003 204 204 PHE CB C 32.24 . 1 1004 204 204 PHE N N 118.1 . 1 1005 206 206 GLU H H 7.538 . 1 1006 206 206 GLU HA H 4.579 . 1 1007 206 206 GLU C C 178.3 . 1 1008 206 206 GLU CA C 58 . 1 1009 206 206 GLU CB C 29.62 . 1 1010 206 206 GLU N N 121.7 . 1 1011 207 207 ARG H H 7.267 . 1 1012 207 207 ARG C C 176.7 . 1 1013 207 207 ARG CA C 58.98 . 1 1014 207 207 ARG CB C 31.28 . 1 1015 207 207 ARG N N 117 . 1 1016 209 209 GLN C C 177.9 . 1 1017 209 209 GLN CA C 55.35 . 1 1018 210 210 GLY H H 8.403 . 1 1019 210 210 GLY HA2 H 3.968 . 2 1020 210 210 GLY HA3 H 3.968 . 2 1021 210 210 GLY C C 174 . 1 1022 210 210 GLY CA C 45.5 . 1 1023 210 210 GLY N N 110 . 1 1024 211 211 GLU H H 8.732 . 1 1025 211 211 GLU C C 177.9 . 1 1026 211 211 GLU CB C 30.56 . 1 1027 211 211 GLU N N 121.3 . 1 1028 212 212 VAL H H 8.015 . 1 1029 212 212 VAL HA H 4.513 . 1 1030 212 212 VAL C C 176.5 . 1 1031 212 212 VAL CA C 61.13 . 1 1032 212 212 VAL CB C 33.37 . 1 1033 212 212 VAL N N 119 . 1 1034 213 213 ARG H H 8.627 . 1 1035 213 213 ARG HA H 4.458 . 1 1036 213 213 ARG C C 174.1 . 1 1037 213 213 ARG CA C 56.32 . 1 1038 213 213 ARG CB C 30.08 . 1 1039 213 213 ARG N N 126.2 . 1 1040 214 214 PHE H H 8.093 . 1 1041 214 214 PHE HA H 5.262 . 1 1042 214 214 PHE C C 175.9 . 1 1043 214 214 PHE CB C 42.06 . 1 1044 214 214 PHE N N 120.5 . 1 1045 215 215 SER H H 8.918 . 1 1046 215 215 SER C C 171.4 . 1 1047 215 215 SER CA C 56.62 . 1 1048 215 215 SER CB C 65.45 . 1 1049 215 215 SER N N 115.7 . 1 1050 216 216 ALA H H 9.026 . 1 1051 216 216 ALA C C 176.3 . 1 1052 216 216 ALA CA C 50.81 . 1 1053 216 216 ALA CB C 22.19 . 1 1054 216 216 ALA N N 124.1 . 1 1055 217 217 VAL H H 9.007 . 1 1056 217 217 VAL HA H 5.2 . 1 1057 217 217 VAL C C 173.6 . 1 1058 217 217 VAL CA C 59.22 . 1 1059 217 217 VAL CB C 36.58 . 1 1060 217 217 VAL N N 115.1 . 1 1061 218 218 ALA H H 9.178 . 1 1062 218 218 ALA HA H 5.548 . 1 1063 218 218 ALA C C 175.4 . 1 1064 218 218 ALA CA C 50.19 . 1 1065 218 218 ALA CB C 22.52 . 1 1066 218 218 ALA N N 124.1 . 1 1067 219 219 LEU H H 8.075 . 1 1068 219 219 LEU C C 174.7 . 1 1069 219 219 LEU CA C 54.14 . 1 1070 219 219 LEU CB C 43.45 . 1 1071 219 219 LEU N N 124.3 . 1 1072 220 220 CYS H H 8.928 . 1 1073 220 220 CYS HA H 5.623 . 1 1074 220 220 CYS C C 172.6 . 1 1075 220 220 CYS CA C 57.45 . 1 1076 220 220 CYS CB C 32.7 . 1 1077 220 220 CYS N N 124.1 . 1 1078 221 221 LYS H H 7.402 . 1 1079 221 221 LYS HA H 3.376 . 1 1080 221 221 LYS C C 175 . 1 1081 221 221 LYS CA C 55.82 . 1 1082 221 221 LYS CB C 31.25 . 1 1083 221 221 LYS N N 125.1 . 1 1084 222 222 ALA H H 7.917 . 1 1085 222 222 ALA HA H 4.084 . 1 1086 222 222 ALA C C 175.7 . 1 1087 222 222 ALA CA C 52.16 . 1 1088 222 222 ALA CB C 19.86 . 1 1089 222 222 ALA N N 129.7 . 1 1090 223 223 ALA H H 7.79 . 1 1091 223 223 ALA HA H 3.962 . 1 1092 223 223 ALA C C 182 . 1 1093 223 223 ALA CA C 53.52 . 1 1094 223 223 ALA CB C 20.35 . 1 1095 223 223 ALA N N 128.8 . 1 stop_ save_