data_16838 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments of the extracellular domain of tissue factor ; _BMRB_accession_number 16838 _BMRB_flat_file_name bmr16838.str _Entry_type original _Submission_date 2010-04-06 _Accession_date 2010-04-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'extracellular domain of Tissue Factor' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boettcher John M. . 2 Clay Mary . . 3 LaHood Benjamin J . 4 Morrissey James H. . 5 Rienstra Chad M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 204 "13C chemical shifts" 543 "15N chemical shifts" 204 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-10-05 update BMRB 'Update entry citation' 2010-06-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 13C and 15N resonance assignments of the extracellular domain of tissue factor.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20526825 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boettcher John M. . 2 Clay Mary C. . 3 LaHood Benjamin J. . 4 Morrissey James H. . 5 Rienstra Chad M. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183 _Page_last 185 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'soluble tissue factor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'soluble tissue factor' $soluble_tissue_factor stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_soluble_tissue_factor _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common soluble_tissue_factor _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Tissue factor initiates the blood coagulation cascade upon forming a complex with factor VIIa' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 229 _Mol_residue_sequence ; ATTNTVAAYNLTWKSTNFKT ILEWEPKPVNQVYTVQISTK SGDWKSKCFYTTDTECDLTD EIVKDVKQTYLARVFSYPAG NVESTGSAGEPLYENSPEFT PYLETNLGQPTIQSFEQVGT KVNVTVEDERTLVRRNNTFL SLRDVFGKDLIYTLYYWKSS SSGKKTAKTNTNEFLIDVDK GENYCFSVQAVIPSRTVNRK STDSPVECMGQEKGEFREGG AAGHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 THR 3 4 THR 4 5 ASN 5 6 THR 6 7 VAL 7 8 ALA 8 9 ALA 9 10 TYR 10 11 ASN 11 12 LEU 12 13 THR 13 14 TRP 14 15 LYS 15 16 SER 16 17 THR 17 18 ASN 18 19 PHE 19 20 LYS 20 21 THR 21 22 ILE 22 23 LEU 23 24 GLU 24 25 TRP 25 26 GLU 26 27 PRO 27 28 LYS 28 29 PRO 29 30 VAL 30 31 ASN 31 32 GLN 32 33 VAL 33 34 TYR 34 35 THR 35 36 VAL 36 37 GLN 37 38 ILE 38 39 SER 39 40 THR 40 41 LYS 41 42 SER 42 43 GLY 43 44 ASP 44 45 TRP 45 46 LYS 46 47 SER 47 48 LYS 48 49 CYS 49 50 PHE 50 51 TYR 51 52 THR 52 53 THR 53 54 ASP 54 55 THR 55 56 GLU 56 57 CYS 57 58 ASP 58 59 LEU 59 60 THR 60 61 ASP 61 62 GLU 62 63 ILE 63 64 VAL 64 65 LYS 65 66 ASP 66 67 VAL 67 68 LYS 68 69 GLN 69 70 THR 70 71 TYR 71 72 LEU 72 73 ALA 73 74 ARG 74 75 VAL 75 76 PHE 76 77 SER 77 78 TYR 78 79 PRO 79 80 ALA 80 81 GLY 81 82 ASN 82 83 VAL 83 84 GLU 84 85 SER 85 86 THR 86 87 GLY 87 88 SER 88 89 ALA 89 90 GLY 90 91 GLU 91 92 PRO 92 93 LEU 93 94 TYR 94 95 GLU 95 96 ASN 96 97 SER 97 98 PRO 98 99 GLU 99 100 PHE 100 101 THR 101 102 PRO 102 103 TYR 103 104 LEU 104 105 GLU 105 106 THR 106 107 ASN 107 108 LEU 108 109 GLY 109 110 GLN 110 111 PRO 111 112 THR 112 113 ILE 113 114 GLN 114 115 SER 115 116 PHE 116 117 GLU 117 118 GLN 118 119 VAL 119 120 GLY 120 121 THR 121 122 LYS 122 123 VAL 123 124 ASN 124 125 VAL 125 126 THR 126 127 VAL 127 128 GLU 128 129 ASP 129 130 GLU 130 131 ARG 131 132 THR 132 133 LEU 133 134 VAL 134 135 ARG 135 136 ARG 136 137 ASN 137 138 ASN 138 139 THR 139 140 PHE 140 141 LEU 141 142 SER 142 143 LEU 143 144 ARG 144 145 ASP 145 146 VAL 146 147 PHE 147 148 GLY 148 149 LYS 149 150 ASP 150 151 LEU 151 152 ILE 152 153 TYR 153 154 THR 154 155 LEU 155 156 TYR 156 157 TYR 157 158 TRP 158 159 LYS 159 160 SER 160 161 SER 161 162 SER 162 163 SER 163 164 GLY 164 165 LYS 165 166 LYS 166 167 THR 167 168 ALA 168 169 LYS 169 170 THR 170 171 ASN 171 172 THR 172 173 ASN 173 174 GLU 174 175 PHE 175 176 LEU 176 177 ILE 177 178 ASP 178 179 VAL 179 180 ASP 180 181 LYS 181 182 GLY 182 183 GLU 183 184 ASN 184 185 TYR 185 186 CYS 186 187 PHE 187 188 SER 188 189 VAL 189 190 GLN 190 191 ALA 191 192 VAL 192 193 ILE 193 194 PRO 194 195 SER 195 196 ARG 196 197 THR 197 198 VAL 198 199 ASN 199 200 ARG 200 201 LYS 201 202 SER 202 203 THR 203 204 ASP 204 205 SER 205 206 PRO 206 207 VAL 207 208 GLU 208 209 CYS 209 210 MET 210 211 GLY 211 212 GLN 212 213 GLU 213 214 LYS 214 215 GLY 215 216 GLU 216 217 PHE 217 218 ARG 218 219 GLU 219 220 GLY 220 221 GLY 221 222 ALA 222 223 ALA 223 224 GLY 224 225 HIS 225 226 HIS 226 227 HIS 227 228 HIS 228 229 HIS 229 230 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-24 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 1AHW "A Complex Of Extracellular Domain Of Tissue Factor With An Inhibitory Fab (5g9)" 95.20 219 99.54 99.54 2.38e-157 PDB 1BOY "Extracellular Region Of Human Tissue Factor" 95.20 219 99.54 99.54 2.38e-157 PDB 1DAN "Complex Of Active Site Inhibited Human Blood Coagulation Factor Viia With Human Recombinant Soluble Tissue Factor" 52.84 121 100.00 100.00 2.83e-81 PDB 1FAK "Human Tissue Factor Complexed With Coagulation Factor Viia Inhibited With A Bpti-Mutant" 89.96 206 100.00 100.00 1.62e-148 PDB 1J9C "Crystal Structure Of Tissue Factor-Factor Viia Complex" 91.27 210 99.52 99.52 8.65e-150 PDB 1JPS "Crystal Structure Of Tissue Factor In Complex With Humanized Fab D3h44" 95.20 219 99.54 99.54 2.38e-157 PDB 1O5D "Dissecting And Designing Inhibitor Selectivity Determinants At The S1 Site Using An Artificial Ala190 Protease (Ala190 Upa)" 95.20 218 99.54 99.54 3.56e-157 PDB 1TFH "Extracellular Domain Of Human Tissue Factor" 95.20 219 99.54 99.54 2.38e-157 PDB 1UJ3 "Crystal Structure Of A Humanized Fab Fragment Of Anti- Tissue-Factor Antibody In Complex With Tissue Factor" 89.52 205 100.00 100.00 7.98e-148 PDB 1W0Y "Tf7a_3771 Complex" 91.27 210 99.52 99.52 8.65e-150 PDB 1W2K "Tf7a_4380 Complex" 91.27 210 99.52 99.52 8.65e-150 PDB 1WQV "Human Factor Viia-Tissue Factor Complexed With Propylsulfonamide-D- Thr-Met-P-Aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 1WSS "Human Factor Viia-tissue Factor In Complex With Peptide-mimetic Inhibitor That Has Two Charged Groups In P2 And P4" 94.76 218 99.54 99.54 1.43e-156 PDB 1WTG "Human Factor Viia-Tissue Factor Complexed With Ethylsulfonamide-D-Biphenylalanine-Gln-P-Aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 1WUN "Human Factor Viia-Tissue Factor Complexed With Ethylsulfonamide-D-Trp-Gln-P-Aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 1WV7 "Human Factor Viia-tissue Factor Complexed With Ethylsulfonamide-d-5-propoxy-trp-gln-p-aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 1Z6J "Crystal Structure Of A Ternary Complex Of Factor Viia/tissue Factor/pyrazinone Inhibitor" 91.70 211 99.52 99.52 1.17e-150 PDB 2A2Q "Complex Of Active-Site Inhibited Human Coagulation Factor Viia With Human Soluble Tissue Factor In The Presence Of Ca2+, Mg2+, " 89.52 205 100.00 100.00 7.98e-148 PDB 2AEI "Crystal Structure Of A Ternary Complex Of Factor ViiaTISSUE FACTOR And 2-[[6-[3-(Aminoiminomethyl)phenoxy]-3,5-Difluro-4-[(1-Me" 91.70 211 99.52 99.52 1.17e-150 PDB 2AER "Crystal Structure Of Benzamidine-Factor ViiaSOLUBLE TISSUE Factor Complex" 89.52 206 100.00 100.00 6.72e-148 PDB 2B7D "Factor Viia Inhibitors: Chemical Optimization, Preclinical Pharmacokinetics, Pharmacodynamics, And Efficacy In A Baboon Thrombo" 95.20 218 99.54 99.54 3.56e-157 PDB 2B8O "Crystal Structure Of Glu-gly-arg-chloromethyl Ketone-factor Viia/soluble Tissue Factor Complex" 89.52 205 100.00 100.00 7.98e-148 PDB 2EC9 "Crystal Structure Analysis Of Human Factor Viia , Souluble Tissue Factor Complexed With Bcx-3607" 52.40 120 100.00 100.00 2.24e-80 PDB 2F9B "Discovery Of Novel Heterocyclic Factor Viia Inhibitors" 95.20 218 99.54 99.54 3.56e-157 PDB 2FIR "Crystal Structure Of Dfpr-ViiaSTF" 89.52 205 100.00 100.00 7.98e-148 PDB 2FLB "Discovery Of A Novel Hydroxy Pyrazole Based Factor Ixa Inhibitor" 95.20 218 99.54 99.54 3.56e-157 PDB 2FLR "Novel 5-azaindole Factor Viia Inhibitors" 95.20 218 99.54 99.54 3.56e-157 PDB 2PUQ "Crystal Structure Of Active Site Inhibited Coagulation Factor Viia In Complex With Soluble Tissue Factor" 89.08 204 100.00 100.00 1.24e-146 PDB 2ZP0 "Human Factor Viia-Tissue Factor Complexed With Benzylsulfonamide-D- Ile-Gln-P-Aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 2ZWL "Human Factor Viia-Tissue Factor Complexed With Highly Selective Peptide Inhibitor" 94.76 218 99.54 99.54 1.43e-156 PDB 2ZZU "Human Factor Viia-Tissue Factor Complexed With Ethylsulfonamide-D-5- (3-Carboxybenzyloxy)-Trp-Gln-P-Aminobenzamidine" 94.76 218 99.54 99.54 1.43e-156 PDB 3ELA "Crystal Structure Of Active Site Inhibited Coagulation Factor Viia Mutant In Complex With Soluble Tissue Factor" 90.83 209 99.52 99.52 1.07e-148 PDB 3TH2 "Mg2+ Is Required For Optimal Folding Of The Gamma-carboxyglutamic Acid (gla) Domains Of Vitamin K-dependent Clotting Factors At" 89.52 205 100.00 100.00 7.98e-148 PDB 3TH3 "Mg2+ Is Required For Optimal Folding Of The Gamma-Carboxyglutamic Acid (Gla) Domains Of Vitamin K-Dependent Clotting Factors At" 89.52 205 100.00 100.00 7.98e-148 PDB 3TH4 "Mg2+ Is Required For Optimal Folding Of The Gamma-carboxyglutamic Acid (gla) Domains Of Vitamin K-dependent Clotting Factors At" 89.52 205 100.00 100.00 7.98e-148 PDB 4IBL "Rubidium Sites In Blood Coagulation Factor Viia" 95.20 219 99.54 99.54 2.38e-157 DBJ BAG35522 "unnamed protein product [Homo sapiens]" 95.20 295 99.08 99.08 1.49e-155 DBJ BAI46540 "coagulation factor III [synthetic construct]" 95.20 295 99.54 99.54 2.66e-156 EMBL CAG46591 "F3 [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 GB AAA36734 "tissue factor precursor [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 GB AAA61150 "tissue factor versions 1 and 2 precursor [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 GB AAA61151 "tissue factor precursor [Homo sapiens]" 95.20 295 99.54 99.54 2.00e-156 GB AAA61152 "tissue factor [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 GB AAH11029 "Coagulation factor III (thromboplastin, tissue factor) [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 REF NP_001171567 "tissue factor isoform 2 precursor [Homo sapiens]" 72.05 238 99.39 99.39 6.84e-114 REF NP_001984 "tissue factor isoform 1 precursor [Homo sapiens]" 95.20 295 99.54 99.54 2.66e-156 REF XP_001156332 "PREDICTED: tissue factor isoform X2 [Pan troglodytes]" 72.05 238 98.18 99.39 2.10e-113 REF XP_001156450 "PREDICTED: tissue factor isoform X1 [Pan troglodytes]" 95.20 295 98.17 99.08 9.57e-155 REF XP_003808492 "PREDICTED: tissue factor isoform X1 [Pan paniscus]" 95.20 295 98.17 99.08 7.13e-155 SP P13726 "RecName: Full=Tissue factor; Short=TF; AltName: Full=Coagulation factor III; AltName: Full=Thromboplastin; AltName: CD_antigen=" 95.20 295 99.54 99.54 2.66e-156 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $soluble_tissue_factor 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 $soluble_tissue_factor 'recombinant technology' . Escherichia coli . pJH677 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM protein sample in a 50 mM phosphate buffer, pH 6.5 and 50 mM NaCl' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $soluble_tissue_factor 1 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate buffer' 50 mM 'natural abundance' NaCl 50 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 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _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_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 90 . mM pH 6.5 . pH pressure 1 . atm temperature 308 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HNCO' '3D HN(CO)CA' '3D HN(CA)CO' 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 'soluble tissue factor' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 1 ALA CA C 52.971 0.2 1 2 3 2 THR H H 7.069 0.050 1 3 3 2 THR C C 173.263 0.2 1 4 3 2 THR CA C 62.072 0.2 1 5 3 2 THR N N 118.361 0.2 1 6 4 3 THR H H 9.404 0.050 1 7 4 3 THR C C 174.134 0.2 1 8 4 3 THR CA C 61.195 0.2 1 9 4 3 THR CB C 66.611 0.2 1 10 4 3 THR N N 125.552 0.2 1 11 5 4 ASN H H 8.481 0.050 1 12 5 4 ASN C C 174.854 0.2 1 13 5 4 ASN CA C 52.683 0.2 1 14 5 4 ASN CB C 38.742 0.2 1 15 5 4 ASN N N 120.841 0.2 1 16 6 5 THR H H 7.828 0.050 1 17 6 5 THR C C 173.548 0.2 1 18 6 5 THR CA C 60.822 0.2 1 19 6 5 THR CB C 70.065 0.2 1 20 6 5 THR N N 113.819 0.2 1 21 7 6 VAL H H 9.155 0.050 1 22 7 6 VAL C C 176.279 0.2 1 23 7 6 VAL CA C 60.225 0.2 1 24 7 6 VAL CB C 33.991 0.2 1 25 7 6 VAL N N 120.606 0.2 1 26 8 7 ALA H H 8.67 0.050 1 27 8 7 ALA C C 176.19 0.2 1 28 8 7 ALA CA C 51.554 0.2 1 29 8 7 ALA CB C 18.881 0.2 1 30 8 7 ALA N N 129.815 0.2 1 31 9 8 ALA H H 8.699 0.050 1 32 9 8 ALA C C 175.62 0.2 1 33 9 8 ALA CA C 50.757 0.2 1 34 9 8 ALA N N 122.891 0.2 1 35 10 9 TYR H H 8.54 0.050 1 36 10 9 TYR C C 173.472 0.2 1 37 10 9 TYR CA C 55.227 0.2 1 38 10 9 TYR CB C 39.083 0.2 1 39 10 9 TYR N N 113.171 0.2 1 40 11 10 ASN H H 8.897 0.050 1 41 11 10 ASN C C 175.131 0.2 1 42 11 10 ASN CA C 53.072 0.2 1 43 11 10 ASN CB C 35.925 0.2 1 44 11 10 ASN N N 116.184 0.2 1 45 12 11 LEU H H 7.97 0.050 1 46 12 11 LEU C C 177.204 0.2 1 47 12 11 LEU CA C 57.342 0.2 1 48 12 11 LEU CB C 40.859 0.2 1 49 12 11 LEU N N 121.178 0.2 1 50 13 12 THR H H 9.218 0.050 1 51 13 12 THR C C 171.768 0.2 1 52 13 12 THR CA C 60.91 0.2 1 53 13 12 THR CB C 72.027 0.2 1 54 13 12 THR N N 118.811 0.2 1 55 14 13 TRP H H 8.592 0.050 1 56 14 13 TRP C C 175.558 0.2 1 57 14 13 TRP CA C 55.722 0.2 1 58 14 13 TRP CB C 28.547 0.2 1 59 14 13 TRP N N 125.506 0.2 1 60 15 14 LYS H H 9.147 0.050 1 61 15 14 LYS C C 174.448 0.2 1 62 15 14 LYS CA C 55.322 0.2 1 63 15 14 LYS N N 116.423 0.2 1 64 16 15 SER C C 176.282 0.2 1 65 16 15 SER CA C 56.387 0.2 1 66 17 16 THR H H 8.207 0.050 1 67 17 16 THR C C 173.544 0.2 1 68 17 16 THR CA C 60.221 0.2 1 69 17 16 THR CB C 72.095 0.2 1 70 17 16 THR N N 114.085 0.2 1 71 18 17 ASN H H 8.774 0.050 1 72 18 17 ASN C C 175.133 0.2 1 73 18 17 ASN CA C 51.003 0.2 1 74 18 17 ASN CB C 40.985 0.2 1 75 18 17 ASN N N 125.72 0.2 1 76 19 18 PHE H H 8.684 0.050 1 77 19 18 PHE C C 174.94 0.2 1 78 19 18 PHE CA C 61.007 0.2 1 79 19 18 PHE N N 126.373 0.2 1 80 20 19 LYS H H 8.178 0.050 1 81 20 19 LYS C C 176.561 0.2 1 82 20 19 LYS CA C 54.278 0.2 1 83 20 19 LYS N N 120.811 0.2 1 84 21 20 THR H H 9.059 0.050 1 85 21 20 THR C C 173.67 0.2 1 86 21 20 THR CA C 59.255 0.2 1 87 21 20 THR N N 121.585 0.2 1 88 22 21 ILE H H 8.732 0.050 1 89 22 21 ILE N N 118.907 0.2 1 90 23 22 LEU C C 176.734 0.2 1 91 23 22 LEU CA C 53.454 0.2 1 92 24 23 GLU H H 9.005 0.050 1 93 24 23 GLU C C 174.532 0.2 1 94 24 23 GLU CA C 54.043 0.2 1 95 24 23 GLU CB C 32.489 0.2 1 96 24 23 GLU N N 121.057 0.2 1 97 25 24 TRP H H 7.422 0.050 1 98 25 24 TRP C C 171.917 0.2 1 99 25 24 TRP CA C 56.576 0.2 1 100 25 24 TRP CB C 29.982 0.2 1 101 25 24 TRP N N 116.93 0.2 1 102 26 25 GLU H H 8.135 0.050 1 103 26 25 GLU C C 172.155 0.2 1 104 26 25 GLU CA C 53.165 0.2 1 105 26 25 GLU CB C 31.444 0.2 1 106 26 25 GLU N N 117.286 0.2 1 107 27 26 PRO C C 175.401 0.2 1 108 27 26 PRO CA C 63.453 0.2 1 109 28 27 LYS H H 8.072 0.050 1 110 28 27 LYS C C 177.074 0.2 1 111 28 27 LYS N N 128.108 0.2 1 112 29 28 PRO C C 177.552 0.2 1 113 29 28 PRO CA C 63.237 0.2 1 114 29 28 PRO CB C 30.568 0.2 1 115 30 29 VAL H H 8.533 0.050 1 116 30 29 VAL C C 176.635 0.2 1 117 30 29 VAL CA C 62.329 0.2 1 118 30 29 VAL CB C 31.956 0.2 1 119 30 29 VAL N N 126.57 0.2 1 120 31 30 ASN H H 8.085 0.050 1 121 31 30 ASN C C 175.256 0.2 1 122 31 30 ASN CA C 53.94 0.2 1 123 31 30 ASN CB C 42.433 0.2 1 124 31 30 ASN N N 122.065 0.2 1 125 32 31 GLN H H 9.184 0.050 1 126 32 31 GLN C C 174.385 0.2 1 127 32 31 GLN CA C 57.68 0.2 1 128 32 31 GLN N N 123.36 0.2 1 129 33 32 VAL H H 8.25 0.050 1 130 33 32 VAL C C 174.251 0.2 1 131 33 32 VAL CA C 57.877 0.2 1 132 33 32 VAL CB C 34.815 0.2 1 133 33 32 VAL N N 125.937 0.2 1 134 34 33 TYR H H 8.359 0.050 1 135 34 33 TYR C C 175.63 0.2 1 136 34 33 TYR CA C 57.277 0.2 1 137 34 33 TYR CB C 41.259 0.2 1 138 34 33 TYR N N 116.988 0.2 1 139 35 34 THR H H 9.549 0.050 1 140 35 34 THR C C 172.133 0.2 1 141 35 34 THR CA C 60.712 0.2 1 142 35 34 THR N N 117.365 0.2 1 143 36 35 VAL H H 8.731 0.050 1 144 36 35 VAL C C 175.09 0.2 1 145 36 35 VAL CA C 60.437 0.2 1 146 36 35 VAL CB C 33.566 0.2 1 147 36 35 VAL N N 126.286 0.2 1 148 37 36 GLN H H 8.593 0.050 1 149 37 36 GLN C C 174.939 0.2 1 150 37 36 GLN CA C 55.116 0.2 1 151 37 36 GLN N N 122.268 0.2 1 152 38 37 ILE H H 9.061 0.050 1 153 38 37 ILE C C 172.124 0.2 1 154 38 37 ILE CA C 58.091 0.2 1 155 38 37 ILE N N 112.262 0.2 1 156 39 38 SER H H 9.15 0.050 1 157 39 38 SER C C 173.861 0.2 1 158 39 38 SER CA C 56.848 0.2 1 159 39 38 SER CB C 65.453 0.2 1 160 39 38 SER N N 120.977 0.2 1 161 40 39 THR H H 8 0.050 1 162 40 39 THR C C 176.455 0.2 1 163 40 39 THR CA C 60.245 0.2 1 164 40 39 THR CB C 69.96 0.2 1 165 40 39 THR N N 109.949 0.2 1 166 41 40 LYS H H 8.149 0.050 1 167 41 40 LYS C C 177.148 0.2 1 168 41 40 LYS CA C 58.603 0.2 1 169 41 40 LYS CB C 30.631 0.2 1 170 41 40 LYS N N 119.657 0.2 1 171 42 41 SER H H 7.961 0.050 1 172 42 41 SER C C 174.533 0.2 1 173 42 41 SER CA C 58.32 0.2 1 174 42 41 SER N N 112.962 0.2 1 175 43 42 GLY H H 7.772 0.050 1 176 43 42 GLY C C 173.104 0.2 1 177 43 42 GLY CA C 44.193 0.2 1 178 43 42 GLY N N 110.657 0.2 1 179 44 43 ASP H H 8.055 0.050 1 180 44 43 ASP C C 175.585 0.2 1 181 44 43 ASP CA C 52.624 0.2 1 182 44 43 ASP CB C 41.084 0.2 1 183 44 43 ASP N N 118.841 0.2 1 184 45 44 TRP H H 8.064 0.050 1 185 45 44 TRP C C 176.853 0.2 1 186 45 44 TRP CA C 57.098 0.2 1 187 45 44 TRP CB C 30.494 0.2 1 188 45 44 TRP N N 120.604 0.2 1 189 46 45 LYS H H 9.226 0.050 1 190 46 45 LYS C C 176.772 0.2 1 191 46 45 LYS CA C 54.326 0.2 1 192 46 45 LYS CB C 34.269 0.2 1 193 46 45 LYS N N 123.09 0.2 1 194 47 46 SER H H 8.931 0.050 1 195 47 46 SER C C 175.49 0.2 1 196 47 46 SER CA C 61.448 0.2 1 197 47 46 SER CB C 66.256 0.2 1 198 47 46 SER N N 120.313 0.2 1 199 48 47 LYS H H 8.562 0.050 1 200 48 47 LYS C C 176.115 0.2 1 201 48 47 LYS CA C 56.803 0.2 1 202 48 47 LYS N N 127.863 0.2 1 203 49 48 CYS H H 8.792 0.050 1 204 49 48 CYS C C 176.05 0.2 1 205 49 48 CYS N N 122.286 0.2 1 206 50 49 PHE H H 8.723 0.050 1 207 50 49 PHE N N 129.17 0.2 1 208 51 50 TYR H H 8.588 0.050 1 209 51 50 TYR C C 174.363 0.2 1 210 51 50 TYR CA C 57.684 0.2 1 211 51 50 TYR CB C 40.563 0.2 1 212 51 50 TYR N N 121.065 0.2 1 213 52 51 THR H H 9.545 0.050 1 214 52 51 THR C C 174.298 0.2 1 215 52 51 THR CA C 59.83 0.2 1 216 52 51 THR N N 113.811 0.2 1 217 53 52 THR H H 8.249 0.050 1 218 53 52 THR C C 174.44 0.2 1 219 53 52 THR CA C 61.328 0.2 1 220 53 52 THR CB C 68.589 0.2 1 221 53 52 THR N N 114.49 0.2 1 222 54 53 ASP H H 9.967 0.050 1 223 54 53 ASP C C 174.417 0.2 1 224 54 53 ASP CA C 56.022 0.2 1 225 54 53 ASP N N 128.143 0.2 1 226 55 54 THR H H 8.794 0.050 1 227 55 54 THR C C 171.735 0.2 1 228 55 54 THR CA C 58.223 0.2 1 229 55 54 THR CB C 68.365 0.2 1 230 55 54 THR N N 127.739 0.2 1 231 56 55 GLU H H 6.144 0.050 1 232 56 55 GLU C C 175.536 0.2 1 233 56 55 GLU CA C 53.207 0.2 1 234 56 55 GLU CB C 32.686 0.2 1 235 56 55 GLU N N 112.541 0.2 1 236 57 56 CYS H H 8.903 0.050 1 237 57 56 CYS C C 172.636 0.2 1 238 57 56 CYS CA C 54.167 0.2 1 239 57 56 CYS CB C 43.678 0.2 1 240 57 56 CYS N N 117.178 0.2 1 241 58 57 ASP H H 9.168 0.050 1 242 58 57 ASP C C 176.272 0.2 1 243 58 57 ASP CA C 54.903 0.2 1 244 58 57 ASP CB C 39.727 0.2 1 245 58 57 ASP N N 130.279 0.2 1 246 59 58 LEU H H 8.632 0.050 1 247 59 58 LEU N N 122.407 0.2 1 248 60 59 THR H H 7.393 0.050 1 249 60 59 THR C C 174.387 0.2 1 250 60 59 THR CA C 68.288 0.2 1 251 60 59 THR N N 121.524 0.2 1 252 61 60 ASP H H 8.712 0.050 1 253 61 60 ASP C C 177.143 0.2 1 254 61 60 ASP CA C 56.503 0.2 1 255 61 60 ASP CB C 39.305 0.2 1 256 61 60 ASP N N 115.418 0.2 1 257 62 61 GLU H H 7.426 0.050 1 258 62 61 GLU C C 178.012 0.2 1 259 62 61 GLU CA C 56.822 0.2 1 260 62 61 GLU N N 115.512 0.2 1 261 63 62 ILE H H 8.07 0.050 1 262 63 62 ILE C C 178.232 0.2 1 263 63 62 ILE N N 107.748 0.2 1 264 64 63 VAL H H 8.139 0.050 1 265 64 63 VAL C C 177.823 0.2 1 266 64 63 VAL CA C 62.727 0.2 1 267 64 63 VAL N N 107.144 0.2 1 268 65 64 LYS H H 7.387 0.050 1 269 65 64 LYS C C 178.334 0.2 1 270 65 64 LYS CA C 58.801 0.2 1 271 65 64 LYS N N 121.944 0.2 1 272 66 65 ASP H H 6.783 0.050 1 273 66 65 ASP C C 178.584 0.2 1 274 66 65 ASP CA C 54.392 0.2 1 275 66 65 ASP CB C 40.071 0.2 1 276 66 65 ASP N N 110.522 0.2 1 277 67 66 VAL C C 175.355 0.2 1 278 67 66 VAL CA C 63.133 0.2 1 279 68 67 LYS H H 8.214 0.050 1 280 68 67 LYS C C 176.635 0.2 1 281 68 67 LYS CA C 56.18 0.2 1 282 68 67 LYS CB C 31.266 0.2 1 283 68 67 LYS N N 118.319 0.2 1 284 69 68 GLN H H 6.803 0.050 1 285 69 68 GLN C C 172.125 0.2 1 286 69 68 GLN CA C 54.601 0.2 1 287 69 68 GLN CB C 28.832 0.2 1 288 69 68 GLN N N 119.566 0.2 1 289 70 69 THR H H 7.847 0.050 1 290 70 69 THR C C 173.376 0.2 1 291 70 69 THR CA C 61.836 0.2 1 292 70 69 THR CB C 69.528 0.2 1 293 70 69 THR N N 114.95 0.2 1 294 71 70 TYR H H 9.065 0.050 1 295 71 70 TYR C C 174.056 0.2 1 296 71 70 TYR CA C 57.193 0.2 1 297 71 70 TYR N N 126.68 0.2 1 298 72 71 LEU H H 8.774 0.050 1 299 72 71 LEU C C 174.058 0.2 1 300 72 71 LEU CA C 54.213 0.2 1 301 72 71 LEU CB C 45.256 0.2 1 302 72 71 LEU N N 119.514 0.2 1 303 73 72 ALA H H 8.776 0.050 1 304 73 72 ALA C C 174.603 0.2 1 305 73 72 ALA CA C 49.817 0.2 1 306 73 72 ALA N N 122.18 0.2 1 307 74 73 ARG H H 8.933 0.050 1 308 74 73 ARG C C 174.694 0.2 1 309 74 73 ARG CA C 54.253 0.2 1 310 74 73 ARG N N 125.787 0.2 1 311 75 74 VAL H H 8.111 0.050 1 312 75 74 VAL C C 174.261 0.2 1 313 75 74 VAL CA C 58.665 0.2 1 314 75 74 VAL N N 115.584 0.2 1 315 76 75 PHE H H 9.262 0.050 1 316 76 75 PHE C C 176.748 0.2 1 317 76 75 PHE CA C 56.082 0.2 1 318 76 75 PHE CB C 41.678 0.2 1 319 76 75 PHE N N 117.21 0.2 1 320 79 78 PRO C C 176.044 0.2 1 321 79 78 PRO CA C 62.361 0.2 1 322 80 79 ALA H H 7.627 0.050 1 323 80 79 ALA C C 177.73 0.2 1 324 80 79 ALA CA C 51.675 0.2 1 325 80 79 ALA CB C 18.835 0.2 1 326 80 79 ALA N N 123.038 0.2 1 327 81 80 GLY H H 8.311 0.050 1 328 81 80 GLY C C 174.307 0.2 1 329 81 80 GLY CA C 44.895 0.2 1 330 81 80 GLY N N 107.147 0.2 1 331 82 81 ASN H H 8.155 0.050 1 332 82 81 ASN C C 175.138 0.2 1 333 82 81 ASN CA C 52.922 0.2 1 334 82 81 ASN CB C 38.123 0.2 1 335 82 81 ASN N N 118.831 0.2 1 336 83 82 VAL H H 7.907 0.050 1 337 83 82 VAL C C 176.239 0.2 1 338 83 82 VAL CA C 62.086 0.2 1 339 83 82 VAL CB C 31.775 0.2 1 340 83 82 VAL N N 119.112 0.2 1 341 84 83 GLU H H 8.348 0.050 1 342 84 83 GLU C C 176.732 0.2 1 343 84 83 GLU CA C 56.499 0.2 1 344 84 83 GLU CB C 29.172 0.2 1 345 84 83 GLU N N 122.586 0.2 1 346 85 84 SER H H 8.196 0.050 1 347 85 84 SER C C 174.993 0.2 1 348 85 84 SER CA C 58.096 0.2 1 349 85 84 SER CB C 63.038 0.2 1 350 85 84 SER N N 115.871 0.2 1 351 86 85 THR H H 8.093 0.050 1 352 86 85 THR C C 174.623 0.2 1 353 86 85 THR CA C 61.607 0.2 1 354 86 85 THR CB C 69.195 0.2 1 355 86 85 THR N N 114.72 0.2 1 356 87 86 GLY H H 8.309 0.050 1 357 87 86 GLY C C 175.179 0.2 1 358 87 86 GLY CA C 45.178 0.2 1 359 87 86 GLY N N 110.69 0.2 1 360 88 87 SER H H 8.137 0.050 1 361 88 87 SER CA C 57.846 0.2 1 362 88 87 SER N N 115.715 0.2 1 363 89 88 ALA H H 8.307 0.050 1 364 89 88 ALA C C 177.983 0.2 1 365 89 88 ALA CA C 52.181 0.2 1 366 89 88 ALA N N 125.664 0.2 1 367 90 89 GLY H H 8.13 0.050 1 368 90 89 GLY C C 173.918 0.2 1 369 90 89 GLY CA C 44.414 0.2 1 370 90 89 GLY N N 107.411 0.2 1 371 91 90 GLU H H 8.231 0.050 1 372 91 90 GLU C C 174.454 0.2 1 373 91 90 GLU CA C 53.912 0.2 1 374 91 90 GLU CB C 28.969 0.2 1 375 91 90 GLU N N 121.715 0.2 1 376 92 91 PRO C C 177.051 0.2 1 377 92 91 PRO CA C 62.242 0.2 1 378 92 91 PRO CB C 31.796 0.2 1 379 93 92 LEU H H 8.396 0.050 1 380 93 92 LEU C C 175.307 0.2 1 381 93 92 LEU CA C 53.869 0.2 1 382 93 92 LEU N N 126.346 0.2 1 383 94 93 TYR H H 7.584 0.050 1 384 94 93 TYR C C 173.167 0.2 1 385 94 93 TYR CA C 55.099 0.2 1 386 94 93 TYR CB C 39.859 0.2 1 387 94 93 TYR N N 115.353 0.2 1 388 95 94 GLU H H 7.63 0.050 1 389 95 94 GLU C C 174.424 0.2 1 390 95 94 GLU CA C 53.242 0.2 1 391 95 94 GLU N N 118.195 0.2 1 392 96 95 ASN H H 9.297 0.050 1 393 96 95 ASN C C 175.541 0.2 1 394 96 95 ASN CA C 52.293 0.2 1 395 96 95 ASN CB C 40.587 0.2 1 396 96 95 ASN N N 123.106 0.2 1 397 97 96 SER H H 9.21 0.050 1 398 97 96 SER C C 171.327 0.2 1 399 97 96 SER CA C 57.558 0.2 1 400 97 96 SER CB C 62.891 0.2 1 401 97 96 SER N N 118.316 0.2 1 402 98 97 PRO C C 179.328 0.2 1 403 98 97 PRO CA C 62.713 0.2 1 404 99 98 GLU H H 9.103 0.050 1 405 99 98 GLU C C 176.222 0.2 1 406 99 98 GLU CA C 57.172 0.2 1 407 99 98 GLU CB C 29.595 0.2 1 408 99 98 GLU N N 126.667 0.2 1 409 100 99 PHE H H 8.683 0.050 1 410 100 99 PHE N N 111.95 0.2 1 411 101 100 THR H H 8.184 0.050 1 412 101 100 THR C C 170.587 0.2 1 413 101 100 THR CA C 61.103 0.2 1 414 101 100 THR CB C 71.249 0.2 1 415 101 100 THR N N 115.882 0.2 1 416 102 101 PRO C C 177.803 0.2 1 417 102 101 PRO CA C 65.194 0.2 1 418 103 102 TYR H H 8.811 0.050 1 419 103 102 TYR C C 176.05 0.2 1 420 103 102 TYR CA C 62.541 0.2 1 421 103 102 TYR N N 113.495 0.2 1 422 104 103 LEU H H 6.589 0.050 1 423 104 103 LEU C C 176.999 0.2 1 424 104 103 LEU CA C 54.773 0.2 1 425 104 103 LEU CB C 43.544 0.2 1 426 104 103 LEU N N 112.573 0.2 1 427 105 104 GLU H H 7.152 0.050 1 428 105 104 GLU C C 177.674 0.2 1 429 105 104 GLU CA C 56.39 0.2 1 430 105 104 GLU N N 111.969 0.2 1 431 106 105 THR H H 8.455 0.050 1 432 106 105 THR C C 173.213 0.2 1 433 106 105 THR CA C 64.122 0.2 1 434 106 105 THR CB C 68.289 0.2 1 435 106 105 THR N N 116.27 0.2 1 436 107 106 ASN H H 8.707 0.050 1 437 107 106 ASN C C 174.612 0.2 1 438 107 106 ASN CA C 54.325 0.2 1 439 107 106 ASN CB C 37.837 0.2 1 440 107 106 ASN N N 127.265 0.2 1 441 108 107 LEU H H 8.77 0.050 1 442 108 107 LEU C C 177.502 0.2 1 443 108 107 LEU CA C 53.313 0.2 1 444 108 107 LEU CB C 41.484 0.2 1 445 108 107 LEU N N 122.828 0.2 1 446 109 108 GLY H H 8.658 0.050 1 447 109 108 GLY C C 172.984 0.2 1 448 109 108 GLY CA C 44.122 0.2 1 449 109 108 GLY N N 110.516 0.2 1 450 110 109 GLN H H 8.159 0.050 1 451 110 109 GLN C C 174.3 0.2 1 452 110 109 GLN CA C 54.182 0.2 1 453 110 109 GLN CB C 29.46 0.2 1 454 110 109 GLN N N 121.747 0.2 1 455 111 110 PRO C C 174.421 0.2 1 456 111 110 PRO CA C 62.065 0.2 1 457 112 111 THR H H 8.364 0.050 1 458 112 111 THR C C 173.978 0.2 1 459 112 111 THR CA C 61.449 0.2 1 460 112 111 THR CB C 71.5 0.2 1 461 112 111 THR N N 111.716 0.2 1 462 113 112 ILE H H 9.061 0.050 1 463 113 112 ILE C C 174.756 0.2 1 464 113 112 ILE CA C 62.581 0.2 1 465 113 112 ILE CB C 36.996 0.2 1 466 113 112 ILE N N 125.919 0.2 1 467 114 113 GLN H H 9.157 0.050 1 468 114 113 GLN C C 175.532 0.2 1 469 114 113 GLN CA C 57.338 0.2 1 470 114 113 GLN N N 131.392 0.2 1 471 115 114 SER H H 7.605 0.050 1 472 115 114 SER C C 171.49 0.2 1 473 115 114 SER CA C 57.1 0.2 1 474 115 114 SER CB C 64.479 0.2 1 475 115 114 SER N N 108.639 0.2 1 476 116 115 PHE H H 7.817 0.050 1 477 116 115 PHE C C 174.005 0.2 1 478 116 115 PHE CA C 55.453 0.2 1 479 116 115 PHE CB C 40.729 0.2 1 480 116 115 PHE N N 115.813 0.2 1 481 117 116 GLU H H 8.524 0.050 1 482 117 116 GLU C C 174.125 0.2 1 483 117 116 GLU CA C 54.852 0.2 1 484 117 116 GLU N N 119.643 0.2 1 485 118 117 GLN H H 9.022 0.050 1 486 118 117 GLN C C 174.916 0.2 1 487 118 117 GLN CA C 55.001 0.2 1 488 118 117 GLN CB C 28.873 0.2 1 489 118 117 GLN N N 125.982 0.2 1 490 119 118 VAL H H 8.785 0.050 1 491 119 118 VAL C C 176.454 0.2 1 492 119 118 VAL CA C 60.624 0.2 1 493 119 118 VAL CB C 32.106 0.2 1 494 119 118 VAL N N 128.322 0.2 1 495 120 119 GLY H H 8.977 0.050 1 496 120 119 GLY CA C 46.782 0.2 1 497 120 119 GLY N N 117.483 0.2 1 498 121 120 THR C C 172.87 0.2 1 499 121 120 THR CA C 61.128 0.2 1 500 122 121 LYS H H 7.793 0.050 1 501 122 121 LYS C C 176.003 0.2 1 502 122 121 LYS CA C 53.901 0.2 1 503 122 121 LYS CB C 34.964 0.2 1 504 122 121 LYS N N 119.866 0.2 1 505 123 122 VAL H H 8.855 0.050 1 506 123 122 VAL C C 171.705 0.2 1 507 123 122 VAL CA C 60.574 0.2 1 508 123 122 VAL CB C 33.748 0.2 1 509 123 122 VAL N N 120.72 0.2 1 510 124 123 ASN H H 9.028 0.050 1 511 124 123 ASN C C 174.829 0.2 1 512 124 123 ASN CA C 53.61 0.2 1 513 124 123 ASN N N 128.481 0.2 1 514 125 124 VAL H H 9.48 0.050 1 515 125 124 VAL C C 175.06 0.2 1 516 125 124 VAL CA C 61.23 0.2 1 517 125 124 VAL N N 125.492 0.2 1 518 126 125 THR H H 8.786 0.050 1 519 126 125 THR C C 173.666 0.2 1 520 126 125 THR CA C 61.13 0.2 1 521 126 125 THR CB C 70.25 0.2 1 522 126 125 THR N N 121.448 0.2 1 523 127 126 VAL H H 9.128 0.050 1 524 127 126 VAL C C 175.438 0.2 1 525 127 126 VAL CA C 61.253 0.2 1 526 127 126 VAL CB C 32.972 0.2 1 527 127 126 VAL N N 127.063 0.2 1 528 128 127 GLU C C 176.181 0.2 1 529 128 127 GLU CA C 56.823 0.2 1 530 129 128 ASP H H 8.838 0.050 1 531 129 128 ASP C C 175.167 0.2 1 532 129 128 ASP CA C 52.941 0.2 1 533 129 128 ASP CB C 39.544 0.2 1 534 129 128 ASP N N 127.92 0.2 1 535 130 129 GLU H H 7.61 0.050 1 536 130 129 GLU C C 175.159 0.2 1 537 130 129 GLU CA C 55.782 0.2 1 538 130 129 GLU CB C 30.611 0.2 1 539 130 129 GLU N N 124.292 0.2 1 540 131 130 ARG H H 8.56 0.050 1 541 131 130 ARG C C 177.069 0.2 1 542 131 130 ARG CA C 55.733 0.2 1 543 131 130 ARG CB C 32.094 0.2 1 544 131 130 ARG N N 120.285 0.2 1 545 132 131 THR H H 8.515 0.050 1 546 132 131 THR C C 173.435 0.2 1 547 132 131 THR CA C 60.145 0.2 1 548 132 131 THR N N 115.347 0.2 1 549 133 132 LEU H H 8.116 0.050 1 550 133 132 LEU C C 176.871 0.2 1 551 133 132 LEU CA C 53.983 0.2 1 552 133 132 LEU CB C 40.658 0.2 1 553 133 132 LEU N N 116.165 0.2 1 554 134 133 VAL H H 8.427 0.050 1 555 134 133 VAL C C 174.202 0.2 1 556 134 133 VAL CA C 63.487 0.2 1 557 134 133 VAL CB C 29.934 0.2 1 558 134 133 VAL N N 120.582 0.2 1 559 135 134 ARG H H 7.599 0.050 1 560 135 134 ARG C C 176.431 0.2 1 561 135 134 ARG CA C 54.108 0.2 1 562 135 134 ARG CB C 32.848 0.2 1 563 135 134 ARG N N 126.351 0.2 1 564 136 135 ARG H H 8.428 0.050 1 565 136 135 ARG C C 175.693 0.2 1 566 136 135 ARG CA C 55.285 0.2 1 567 136 135 ARG CB C 32.352 0.2 1 568 136 135 ARG N N 123.239 0.2 1 569 138 137 ASN H H 8.871 0.050 1 570 138 137 ASN C C 173.766 0.2 1 571 138 137 ASN CA C 53.741 0.2 1 572 138 137 ASN N N 117.036 0.2 1 573 139 138 THR H H 7.671 0.050 1 574 139 138 THR C C 172.696 0.2 1 575 139 138 THR CA C 60.547 0.2 1 576 139 138 THR CB C 70.778 0.2 1 577 139 138 THR N N 114.345 0.2 1 578 140 139 PHE H H 8.495 0.050 1 579 140 139 PHE C C 176.051 0.2 1 580 140 139 PHE CA C 58.221 0.2 1 581 140 139 PHE CB C 38.738 0.2 1 582 140 139 PHE N N 122.375 0.2 1 583 141 140 LEU H H 8.883 0.050 1 584 141 140 LEU C C 178.252 0.2 1 585 141 140 LEU CA C 53.65 0.2 1 586 141 140 LEU CB C 41.734 0.2 1 587 141 140 LEU N N 123.301 0.2 1 588 142 141 SER H H 10.033 0.050 1 589 142 141 SER C C 174.76 0.2 1 590 142 141 SER CA C 56.681 0.2 1 591 142 141 SER CB C 64.562 0.2 1 592 142 141 SER N N 122.615 0.2 1 593 143 142 LEU H H 8.191 0.050 1 594 143 142 LEU C C 174.889 0.2 1 595 143 142 LEU CA C 56.802 0.2 1 596 143 142 LEU CB C 46.148 0.2 1 597 143 142 LEU N N 116.065 0.2 1 598 144 143 ARG H H 8.609 0.050 1 599 144 143 ARG C C 179.707 0.2 1 600 144 143 ARG CA C 58.306 0.2 1 601 144 143 ARG N N 120.988 0.2 1 602 145 144 ASP H H 8.105 0.050 1 603 145 144 ASP C C 178.323 0.2 1 604 145 144 ASP CA C 57.01 0.2 1 605 145 144 ASP CB C 40.716 0.2 1 606 145 144 ASP N N 121.225 0.2 1 607 146 145 VAL H H 7.914 0.050 1 608 146 145 VAL C C 177.473 0.2 1 609 146 145 VAL CA C 65.517 0.2 1 610 146 145 VAL CB C 31.633 0.2 1 611 146 145 VAL N N 118.163 0.2 1 612 147 146 PHE H H 8.399 0.050 1 613 147 146 PHE C C 177.565 0.2 1 614 147 146 PHE CA C 59.752 0.2 1 615 147 146 PHE N N 114.729 0.2 1 616 148 147 GLY H H 8.569 0.050 1 617 148 147 GLY C C 176.333 0.2 1 618 148 147 GLY CA C 46.691 0.2 1 619 148 147 GLY N N 110.299 0.2 1 620 149 148 LYS H H 8.664 0.050 1 621 149 148 LYS C C 176.869 0.2 1 622 149 148 LYS CA C 56.75 0.2 1 623 149 148 LYS CB C 31.078 0.2 1 624 149 148 LYS N N 123.994 0.2 1 625 150 149 ASP H H 8.301 0.050 1 626 150 149 ASP C C 174.976 0.2 1 627 150 149 ASP CA C 55.379 0.2 1 628 150 149 ASP CB C 39.409 0.2 1 629 150 149 ASP N N 118.813 0.2 1 630 151 150 LEU H H 6.941 0.050 1 631 151 150 LEU C C 174.858 0.2 1 632 151 150 LEU CA C 53.927 0.2 1 633 151 150 LEU CB C 43.869 0.2 1 634 151 150 LEU N N 118.727 0.2 1 635 152 151 ILE H H 7.521 0.050 1 636 152 151 ILE C C 172.594 0.2 1 637 152 151 ILE CA C 57.041 0.2 1 638 152 151 ILE N N 114.454 0.2 1 639 153 152 TYR H H 8.603 0.050 1 640 153 152 TYR C C 177.958 0.2 1 641 153 152 TYR CA C 55.462 0.2 1 642 153 152 TYR N N 112.327 0.2 1 643 154 153 THR H H 8.386 0.050 1 644 154 153 THR N N 116.33 0.2 1 645 155 154 LEU C C 174.293 0.2 1 646 155 154 LEU CA C 54.424 0.2 1 647 156 155 TYR H H 9.078 0.050 1 648 156 155 TYR C C 174.246 0.2 1 649 156 155 TYR CA C 55.615 0.2 1 650 156 155 TYR CB C 42.114 0.2 1 651 156 155 TYR N N 119.349 0.2 1 652 157 156 TYR H H 8.398 0.050 1 653 157 156 TYR C C 176.098 0.2 1 654 157 156 TYR CA C 54.341 0.2 1 655 157 156 TYR CB C 42.675 0.2 1 656 157 156 TYR N N 124.286 0.2 1 657 158 157 TRP H H 8.154 0.050 1 658 158 157 TRP C C 174.451 0.2 1 659 158 157 TRP CA C 58.401 0.2 1 660 158 157 TRP N N 121.902 0.2 1 661 159 158 LYS H H 7.448 0.050 1 662 159 158 LYS C C 177.5 0.2 1 663 159 158 LYS CA C 53.555 0.2 1 664 159 158 LYS N N 109.958 0.2 1 665 160 159 SER H H 9.01 0.050 1 666 160 159 SER C C 174.66 0.2 1 667 160 159 SER CA C 57.731 0.2 1 668 160 159 SER CB C 66.532 0.2 1 669 160 159 SER N N 118.37 0.2 1 670 161 160 SER H H 7.654 0.050 1 671 161 160 SER C C 172.034 0.2 1 672 161 160 SER CA C 57.97 0.2 1 673 161 160 SER CB C 65.549 0.2 1 674 161 160 SER N N 104.899 0.2 1 675 162 161 SER H H 8.622 0.050 1 676 162 161 SER CA C 55.125 0.2 1 677 162 161 SER N N 117.871 0.2 1 678 163 162 SER C C 174.506 0.2 1 679 163 162 SER CA C 57.648 0.2 1 680 163 162 SER CB C 66.404 0.2 1 681 164 163 GLY H H 8.3 0.050 1 682 164 163 GLY C C 173.987 0.2 1 683 164 163 GLY CA C 45.029 0.2 1 684 164 163 GLY N N 110.675 0.2 1 685 165 164 LYS H H 8.198 0.050 1 686 165 164 LYS C C 176.134 0.2 1 687 165 164 LYS CA C 55.903 0.2 1 688 165 164 LYS N N 120.443 0.2 1 689 166 165 LYS H H 8.695 0.050 1 690 166 165 LYS C C 174.905 0.2 1 691 166 165 LYS CA C 54.76 0.2 1 692 166 165 LYS CB C 33.272 0.2 1 693 166 165 LYS N N 124.369 0.2 1 694 167 166 THR H H 7.913 0.050 1 695 167 166 THR C C 174.766 0.2 1 696 167 166 THR CA C 59.072 0.2 1 697 167 166 THR CB C 72.277 0.2 1 698 167 166 THR N N 108.213 0.2 1 699 168 167 ALA H H 9.03 0.050 1 700 168 167 ALA C C 175.037 0.2 1 701 168 167 ALA CA C 50.847 0.2 1 702 168 167 ALA CB C 22.557 0.2 1 703 168 167 ALA N N 125.444 0.2 1 704 169 168 LYS H H 8.762 0.050 1 705 169 168 LYS C C 175.913 0.2 1 706 169 168 LYS CA C 55.08 0.2 1 707 169 168 LYS CB C 35.908 0.2 1 708 169 168 LYS N N 118.765 0.2 1 709 170 169 THR H H 8.816 0.050 1 710 170 169 THR C C 170.726 0.2 1 711 170 169 THR CA C 58.886 0.2 1 712 170 169 THR CB C 70.14 0.2 1 713 170 169 THR N N 114.774 0.2 1 714 171 170 ASN H H 8.388 0.050 1 715 171 170 ASN C C 175.494 0.2 1 716 171 170 ASN CA C 52.428 0.2 1 717 171 170 ASN N N 122.42 0.2 1 718 172 171 THR H H 8.545 0.050 1 719 172 171 THR C C 172.165 0.2 1 720 172 171 THR CA C 59.808 0.2 1 721 172 171 THR CB C 68.3 0.2 1 722 172 171 THR N N 113.748 0.2 1 723 173 172 ASN H H 8.238 0.050 1 724 173 172 ASN C C 173.287 0.2 1 725 173 172 ASN CA C 51.898 0.2 1 726 173 172 ASN CB C 37.312 0.2 1 727 173 172 ASN N N 117.274 0.2 1 728 174 173 GLU H H 7.866 0.050 1 729 174 173 GLU C C 174.099 0.2 1 730 174 173 GLU CA C 54.391 0.2 1 731 174 173 GLU CB C 33.348 0.2 1 732 174 173 GLU N N 116.544 0.2 1 733 175 174 PHE H H 7.987 0.050 1 734 175 174 PHE C C 175.336 0.2 1 735 175 174 PHE N N 104.768 0.2 1 736 176 175 LEU C C 176.149 0.2 1 737 176 175 LEU CA C 54.062 0.2 1 738 177 176 ILE H H 8.681 0.050 1 739 177 176 ILE C C 174.237 0.2 1 740 177 176 ILE CA C 58.334 0.2 1 741 177 176 ILE N N 120.923 0.2 1 742 178 177 ASP H H 8.149 0.050 1 743 178 177 ASP C C 175.686 0.2 1 744 178 177 ASP CA C 54.113 0.2 1 745 178 177 ASP CB C 41.794 0.2 1 746 178 177 ASP N N 121.897 0.2 1 747 179 178 VAL H H 8.296 0.050 1 748 179 178 VAL C C 175.031 0.2 1 749 179 178 VAL CA C 59.2 0.2 1 750 179 178 VAL CB C 34.45 0.2 1 751 179 178 VAL N N 115.387 0.2 1 752 180 179 ASP H H 8.135 0.050 1 753 180 179 ASP C C 176.508 0.2 1 754 180 179 ASP CA C 53.767 0.2 1 755 180 179 ASP CB C 40.793 0.2 1 756 180 179 ASP N N 121.249 0.2 1 757 181 180 LYS H H 8.498 0.050 1 758 181 180 LYS C C 177.639 0.2 1 759 181 180 LYS CA C 57.207 0.2 1 760 181 180 LYS CB C 31.777 0.2 1 761 181 180 LYS N N 122.948 0.2 1 762 182 181 GLY H H 8.756 0.050 1 763 182 181 GLY C C 173.758 0.2 1 764 182 181 GLY CA C 45.381 0.2 1 765 182 181 GLY N N 111.838 0.2 1 766 183 182 GLU H H 7.344 0.050 1 767 183 182 GLU C C 174.974 0.2 1 768 183 182 GLU CA C 54.583 0.2 1 769 183 182 GLU CB C 31.232 0.2 1 770 183 182 GLU N N 117.893 0.2 1 771 184 183 ASN H H 8.651 0.050 1 772 184 183 ASN C C 174.227 0.2 1 773 184 183 ASN CA C 52.587 0.2 1 774 184 183 ASN CB C 39.033 0.2 1 775 184 183 ASN N N 119.993 0.2 1 776 185 184 TYR H H 7.892 0.050 1 777 185 184 TYR C C 174.404 0.2 1 778 185 184 TYR CA C 56.654 0.2 1 779 185 184 TYR CB C 41.632 0.2 1 780 185 184 TYR N N 122.602 0.2 1 781 186 185 CYS H H 9.54 0.050 1 782 186 185 CYS C C 175.941 0.2 1 783 186 185 CYS CA C 55.81 0.2 1 784 186 185 CYS N N 128.746 0.2 1 785 187 186 PHE H H 9.296 0.050 1 786 187 186 PHE C C 175.654 0.2 1 787 187 186 PHE CA C 55.97 0.2 1 788 187 186 PHE N N 126.728 0.2 1 789 188 187 SER H H 8.381 0.050 1 790 188 187 SER C C 172.178 0.2 1 791 188 187 SER CA C 58.162 0.2 1 792 188 187 SER CB C 64.689 0.2 1 793 188 187 SER N N 114.982 0.2 1 794 189 188 VAL H H 8.907 0.050 1 795 189 188 VAL C C 174.512 0.2 1 796 189 188 VAL CA C 58.947 0.2 1 797 189 188 VAL CB C 35.756 0.2 1 798 189 188 VAL N N 119.182 0.2 1 799 190 189 GLN H H 9.159 0.050 1 800 190 189 GLN C C 174.504 0.2 1 801 190 189 GLN CA C 54.563 0.2 1 802 190 189 GLN N N 122.87 0.2 1 803 191 190 ALA H H 8.88 0.050 1 804 191 190 ALA C C 175.704 0.2 1 805 191 190 ALA CA C 50.612 0.2 1 806 191 190 ALA N N 128.805 0.2 1 807 192 191 VAL H H 8.748 0.050 1 808 192 191 VAL C C 173.99 0.2 1 809 192 191 VAL CA C 59.953 0.2 1 810 192 191 VAL N N 120.448 0.2 1 811 193 192 ILE H H 8.475 0.050 1 812 193 192 ILE C C 175.334 0.2 1 813 193 192 ILE CA C 56.811 0.2 1 814 193 192 ILE N N 125.037 0.2 1 815 194 193 PRO C C 177.257 0.2 1 816 194 193 PRO CA C 64.206 0.2 1 817 195 194 SER H H 8.255 0.050 1 818 195 194 SER C C 176.221 0.2 1 819 195 194 SER CA C 58.874 0.2 1 820 195 194 SER CB C 62.262 0.2 1 821 195 194 SER N N 109.021 0.2 1 822 196 195 ARG H H 7.754 0.050 1 823 196 195 ARG C C 176.779 0.2 1 824 196 195 ARG CA C 57.463 0.2 1 825 196 195 ARG CB C 31.564 0.2 1 826 196 195 ARG N N 122.496 0.2 1 827 197 196 THR H H 9.39 0.050 1 828 197 196 THR C C 170.254 0.2 1 829 197 196 THR CA C 63.423 0.2 1 830 197 196 THR CB C 71.67 0.2 1 831 197 196 THR N N 128.062 0.2 1 832 198 197 VAL H H 9.236 0.050 1 833 198 197 VAL C C 173.975 0.2 1 834 198 197 VAL CA C 61.245 0.2 1 835 198 197 VAL N N 128.35 0.2 1 836 199 198 ASN H H 8.728 0.050 1 837 199 198 ASN C C 173.134 0.2 1 838 199 198 ASN CA C 54.023 0.2 1 839 199 198 ASN CB C 41.441 0.2 1 840 199 198 ASN N N 123.803 0.2 1 841 200 199 ARG CA C 56.111 0.2 1 842 201 200 LYS H H 9.049 0.050 1 843 201 200 LYS C C 175.539 0.2 1 844 201 200 LYS CA C 54.376 0.2 1 845 201 200 LYS N N 121.135 0.2 1 846 202 201 SER H H 8.842 0.050 1 847 202 201 SER C C 174.534 0.2 1 848 202 201 SER CA C 55.231 0.2 1 849 202 201 SER CB C 63.925 0.2 1 850 202 201 SER N N 119.67 0.2 1 851 203 202 THR H H 8.295 0.050 1 852 203 202 THR C C 175.344 0.2 1 853 203 202 THR CA C 61.715 0.2 1 854 203 202 THR CB C 70.933 0.2 1 855 203 202 THR N N 125.917 0.2 1 856 204 203 ASP H H 8.224 0.050 1 857 204 203 ASP C C 177.536 0.2 1 858 204 203 ASP CA C 54.855 0.2 1 859 204 203 ASP CB C 41.068 0.2 1 860 204 203 ASP N N 122.512 0.2 1 861 205 204 SER H H 9.35 0.050 1 862 205 204 SER C C 171.361 0.2 1 863 205 204 SER CA C 57.656 0.2 1 864 205 204 SER CB C 62.779 0.2 1 865 205 204 SER N N 117.208 0.2 1 866 206 205 PRO C C 174.645 0.2 1 867 206 205 PRO CA C 62.854 0.2 1 868 207 206 VAL H H 8.017 0.050 1 869 207 206 VAL C C 173.344 0.2 1 870 207 206 VAL CA C 59.142 0.2 1 871 207 206 VAL CB C 34.128 0.2 1 872 207 206 VAL N N 118.465 0.2 1 873 208 207 GLU H H 8.928 0.050 1 874 208 207 GLU C C 175.127 0.2 1 875 208 207 GLU CA C 53.7 0.2 1 876 208 207 GLU N N 122.176 0.2 1 877 209 208 CYS H H 8.652 0.050 1 878 209 208 CYS C C 174.228 0.2 1 879 209 208 CYS CA C 55.028 0.2 1 880 209 208 CYS CB C 48.125 0.2 1 881 209 208 CYS N N 117.739 0.2 1 882 210 209 MET H H 8.587 0.050 1 883 210 209 MET C C 176.301 0.2 1 884 210 209 MET CA C 56.393 0.2 1 885 210 209 MET CB C 36.12 0.2 1 886 210 209 MET N N 120.738 0.2 1 887 211 210 GLY H H 8.613 0.050 1 888 211 210 GLY CA C 45.133 0.2 1 889 211 210 GLY N N 108.722 0.2 1 890 212 211 GLN H H 8.034 0.050 1 891 212 211 GLN C C 175.344 0.2 1 892 212 211 GLN CA C 55.21 0.2 1 893 212 211 GLN CB C 29.151 0.2 1 894 212 211 GLN N N 118.898 0.2 1 895 213 212 GLU H H 8.574 0.050 1 896 213 212 GLU C C 176.472 0.2 1 897 213 212 GLU CA C 56.297 0.2 1 898 213 212 GLU CB C 29.845 0.2 1 899 213 212 GLU N N 122.644 0.2 1 900 214 213 LYS H H 8.425 0.050 1 901 214 213 LYS C C 177.058 0.2 1 902 214 213 LYS CA C 56.117 0.2 1 903 214 213 LYS CB C 32.242 0.2 1 904 214 213 LYS N N 122.308 0.2 1 905 215 214 GLY H H 8.377 0.050 1 906 215 214 GLY C C 174.622 0.2 1 907 215 214 GLY CA C 44.825 0.2 1 908 215 214 GLY N N 109.577 0.2 1 909 216 215 GLU H H 8.104 0.050 1 910 216 215 GLU C C 176.151 0.2 1 911 216 215 GLU CA C 56.014 0.2 1 912 216 215 GLU CB C 29.814 0.2 1 913 216 215 GLU N N 120.63 0.2 1 914 217 216 PHE H H 8.273 0.050 1 915 217 216 PHE C C 175.549 0.2 1 916 217 216 PHE CA C 57.318 0.2 1 917 217 216 PHE N N 121.181 0.2 1 918 218 217 ARG H H 8.083 0.050 1 919 218 217 ARG C C 175.895 0.2 1 920 218 217 ARG CA C 55.383 0.2 1 921 218 217 ARG N N 123.05 0.2 1 922 219 218 GLU H H 8.352 0.050 1 923 219 218 GLU C C 176.92 0.2 1 924 219 218 GLU CA C 56.395 0.2 1 925 219 218 GLU N N 122.002 0.2 1 926 220 219 GLY H H 8.417 0.050 1 927 220 219 GLY C C 174.854 0.2 1 928 220 219 GLY CA C 45.032 0.2 1 929 220 219 GLY N N 110.083 0.2 1 930 221 220 GLY H H 8.212 0.050 1 931 221 220 GLY CA C 44.822 0.2 1 932 221 220 GLY N N 108.629 0.2 1 933 222 221 ALA H H 8.177 0.050 1 934 222 221 ALA C C 177.854 0.2 1 935 222 221 ALA CA C 52.175 0.2 1 936 222 221 ALA N N 123.671 0.2 1 937 223 222 ALA H H 8.187 0.050 1 938 223 222 ALA C C 178.343 0.2 1 939 223 222 ALA N N 122.24 0.2 1 940 224 223 GLY H H 8.164 0.050 1 941 224 223 GLY CA C 44.86 0.2 1 942 224 223 GLY N N 110.593 0.2 1 943 225 224 HIS H H 8.264 0.050 1 944 225 224 HIS N N 121.073 0.2 1 945 226 225 HIS C C 174.526 0.2 1 946 226 225 HIS CA C 54.985 0.2 1 947 227 226 HIS H H 8.365 0.050 1 948 227 226 HIS CA C 55.538 0.2 1 949 227 226 HIS N N 119.237 0.2 1 950 228 227 HIS H H 8.032 0.050 1 951 228 227 HIS N N 125.112 0.2 1 stop_ save_