data_19744 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase ; _BMRB_accession_number 19744 _BMRB_flat_file_name bmr19744.str _Entry_type original _Submission_date 2014-01-20 _Accession_date 2014-01-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Dimethylarginine Dimethylaminohydrolase, Asymmetric Dimethyarginine, Nitric Oxide, Nitric Oxide Synthases' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Driscoll Paul PCD . 2 Rasheed Masooma MR . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 235 "13C chemical shifts" 486 "15N chemical shifts" 235 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-11 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19742 'Dimethylarginine Dimethylaminohydrolase' 19743 'Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase' stop_ _Original_release_date 2014-04-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24484052 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rasheed Masooma . . 2 Richter Christine . . 3 Chisty Liisa T. . 4 Kirkpatrick John . . 5 Blackledge Martin . . 6 Webb Martin R. . 7 Driscoll Paul C. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 53 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1092 _Page_last 1104 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Pseudomonas aeruginosa Dimethylarginine Dimethylaminohydrolase' _Enzyme_commission_number 3.5.3.18 loop_ _Mol_system_component_name _Mol_label 'Dimethylarginine Dimethylaminohydrolase' $PaDDAH L-citrulline $entity_CIR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; Citrulline residues are generated in proteins as a result of a posttranslational modification reaction conducted by a family of enzymes called peptidylarginine deiminases (PADs), which convert arginine into citrulline. Proteins that normally contain citrulline residues include myelin basic protein (MBP), filaggrin, and several histone proteins. Patients with rheumatoid arthritis often have detectable antibodies against proteins containing citrulline. Therefore, application of antibodies reactive with citrulline, containing proteins is now becoming an important tool to diagnose the rheumatoid arthritis.Whereas, the circulating citrulline concentration in humans,is used as distinctive bio-marker for examining the intestinal functionality. ; save_ ######################## # Monomeric polymers # ######################## save_PaDDAH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PaDDAH _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function ; In mammals, the enzyme dimethylarginine dimethylaminohydrolase (DDAH) is implicated in the regulation of the cellular levels of asymmetric methylarginines, small molecule metabolites that themselves represent a family of endogenous inhibitors of nitric oxide synthase (NOS). The involvement of DDAH function in the regulation of NOS makes this enzyme a potentially attractive therapeutic target. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 254 _Mol_residue_sequence ; MFKHIIARTPARSLVDGLTS SHLGKPDYAKALEQHNAYIE ALQTCDVDITLLPPDERFPD SVFVEDPVLCTSRCAIITRP GAESRRGETEIIEETVQHFY PGKVERIEAPGTVEAGDIMM VGDHFYIGESARTNAEGARQ MIAILEKHGLSGSVVRLEKV LHLKTGLAYLEHNNLLAAGE FVSKPEFQDFNIIEIPEEES YAANCIWVNERVIMPAGYPR TREKIARLGYRVIEVDTSEY RKIDGGVSCMSLRF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 PHE 3 3 LYS 4 4 HIS 5 5 ILE 6 6 ILE 7 7 ALA 8 8 ARG 9 9 THR 10 10 PRO 11 11 ALA 12 12 ARG 13 13 SER 14 14 LEU 15 15 VAL 16 16 ASP 17 17 GLY 18 18 LEU 19 19 THR 20 20 SER 21 21 SER 22 22 HIS 23 23 LEU 24 24 GLY 25 25 LYS 26 26 PRO 27 27 ASP 28 28 TYR 29 29 ALA 30 30 LYS 31 31 ALA 32 32 LEU 33 33 GLU 34 34 GLN 35 35 HIS 36 36 ASN 37 37 ALA 38 38 TYR 39 39 ILE 40 40 GLU 41 41 ALA 42 42 LEU 43 43 GLN 44 44 THR 45 45 CYS 46 46 ASP 47 47 VAL 48 48 ASP 49 49 ILE 50 50 THR 51 51 LEU 52 52 LEU 53 53 PRO 54 54 PRO 55 55 ASP 56 56 GLU 57 57 ARG 58 58 PHE 59 59 PRO 60 60 ASP 61 61 SER 62 62 VAL 63 63 PHE 64 64 VAL 65 65 GLU 66 66 ASP 67 67 PRO 68 68 VAL 69 69 LEU 70 70 CYS 71 71 THR 72 72 SER 73 73 ARG 74 74 CYS 75 75 ALA 76 76 ILE 77 77 ILE 78 78 THR 79 79 ARG 80 80 PRO 81 81 GLY 82 82 ALA 83 83 GLU 84 84 SER 85 85 ARG 86 86 ARG 87 87 GLY 88 88 GLU 89 89 THR 90 90 GLU 91 91 ILE 92 92 ILE 93 93 GLU 94 94 GLU 95 95 THR 96 96 VAL 97 97 GLN 98 98 HIS 99 99 PHE 100 100 TYR 101 101 PRO 102 102 GLY 103 103 LYS 104 104 VAL 105 105 GLU 106 106 ARG 107 107 ILE 108 108 GLU 109 109 ALA 110 110 PRO 111 111 GLY 112 112 THR 113 113 VAL 114 114 GLU 115 115 ALA 116 116 GLY 117 117 ASP 118 118 ILE 119 119 MET 120 120 MET 121 121 VAL 122 122 GLY 123 123 ASP 124 124 HIS 125 125 PHE 126 126 TYR 127 127 ILE 128 128 GLY 129 129 GLU 130 130 SER 131 131 ALA 132 132 ARG 133 133 THR 134 134 ASN 135 135 ALA 136 136 GLU 137 137 GLY 138 138 ALA 139 139 ARG 140 140 GLN 141 141 MET 142 142 ILE 143 143 ALA 144 144 ILE 145 145 LEU 146 146 GLU 147 147 LYS 148 148 HIS 149 149 GLY 150 150 LEU 151 151 SER 152 152 GLY 153 153 SER 154 154 VAL 155 155 VAL 156 156 ARG 157 157 LEU 158 158 GLU 159 159 LYS 160 160 VAL 161 161 LEU 162 162 HIS 163 163 LEU 164 164 LYS 165 165 THR 166 166 GLY 167 167 LEU 168 168 ALA 169 169 TYR 170 170 LEU 171 171 GLU 172 172 HIS 173 173 ASN 174 174 ASN 175 175 LEU 176 176 LEU 177 177 ALA 178 178 ALA 179 179 GLY 180 180 GLU 181 181 PHE 182 182 VAL 183 183 SER 184 184 LYS 185 185 PRO 186 186 GLU 187 187 PHE 188 188 GLN 189 189 ASP 190 190 PHE 191 191 ASN 192 192 ILE 193 193 ILE 194 194 GLU 195 195 ILE 196 196 PRO 197 197 GLU 198 198 GLU 199 199 GLU 200 200 SER 201 201 TYR 202 202 ALA 203 203 ALA 204 204 ASN 205 205 CYS 206 206 ILE 207 207 TRP 208 208 VAL 209 209 ASN 210 210 GLU 211 211 ARG 212 212 VAL 213 213 ILE 214 214 MET 215 215 PRO 216 216 ALA 217 217 GLY 218 218 TYR 219 219 PRO 220 220 ARG 221 221 THR 222 222 ARG 223 223 GLU 224 224 LYS 225 225 ILE 226 226 ALA 227 227 ARG 228 228 LEU 229 229 GLY 230 230 TYR 231 231 ARG 232 232 VAL 233 233 ILE 234 234 GLU 235 235 VAL 236 236 ASP 237 237 THR 238 238 SER 239 239 GLU 240 240 TYR 241 241 ARG 242 242 LYS 243 243 ILE 244 244 ASP 245 245 GLY 246 246 GLY 247 247 VAL 248 248 SER 249 249 CYS 250 250 MET 251 251 SER 252 252 LEU 253 253 ARG 254 254 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 19615 PaDDAH_TM 100.00 254 99.61 99.61 0.00e+00 BMRB 19616 Dimethylarginine_Dimethylaminohydrolase 100.00 254 99.61 99.61 0.00e+00 BMRB 19742 Psuedomonas_aeruginosa_Dimethylarginine_Dimethylaminohydrolase_DDAH 100.00 254 100.00 100.00 0.00e+00 BMRB 19743 Psuedomonas_aeruginosa_Dimethylarginine_Dimethylaminohydrolase 100.00 254 100.00 100.00 0.00e+00 PDB 1H70 "Ddah From Pseudomonas Aeruginosa. C249s Mutant Complexed With Citrulline" 100.00 255 98.82 98.82 0.00e+00 PDB 3BPB "Crystal Structure Of The Dimethylarginine Dimethylaminohydrolase H162g Adduct With S-Methyl-L- Thiocitrulline" 100.00 254 98.82 98.82 0.00e+00 PDB 3RHY "Crystal Structure Of The Dimethylarginine Dimethylaminohydrolase Adduct With 4-Chloro-2-Hydroxymethylpyridine" 100.00 254 99.21 99.21 0.00e+00 DBJ BAK88928 "hypothetical protein NCGM2_2069 [Pseudomonas aeruginosa NCGM2.S1]" 100.00 254 99.21 99.21 0.00e+00 DBJ BAP20511 "hypothetical protein NCGM1900_1389 [Pseudomonas aeruginosa]" 100.00 254 99.21 99.21 0.00e+00 DBJ BAP52091 "hypothetical protein NCGM1984_4129 [Pseudomonas aeruginosa]" 100.00 254 99.21 99.21 0.00e+00 DBJ BAQ41197 "hypothetical protein PA257_4611 [Pseudomonas aeruginosa]" 100.00 254 98.82 98.82 0.00e+00 DBJ BAR69052 "N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa]" 100.00 254 98.82 98.82 0.00e+00 EMBL CAW28868 "putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa LESB58]" 100.00 254 99.21 99.21 0.00e+00 EMBL CCQ86504 "NG,NG-dimethylarginine dimethylaminohydrolase 1 [Pseudomonas aeruginosa 18A]" 100.00 254 98.82 98.82 0.00e+00 EMBL CDH72250 "N(G), N(G)-dimethylargininedimethylaminohydrolase [Pseudomonas aeruginosa MH38]" 100.00 254 99.21 99.21 0.00e+00 EMBL CDH78521 "N(G), N(G)-dimethylargininedimethylaminohydrolase [Pseudomonas aeruginosa MH27]" 100.00 254 99.21 99.21 0.00e+00 EMBL CDI89341 "putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa PA38182]" 100.00 254 99.21 99.21 0.00e+00 GB AAG04584 "hypothetical protein PA1195 [Pseudomonas aeruginosa PAO1]" 100.00 254 99.21 99.21 0.00e+00 GB ABJ10379 "putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa UCBPP-PA14]" 100.00 254 99.21 99.21 0.00e+00 GB AEO76319 "putative dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa M18]" 100.00 254 98.82 98.82 0.00e+00 GB AFM66206 "N-Dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa DK2]" 100.00 254 99.21 99.21 0.00e+00 GB AGI82760 "N-Dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa B136-33]" 100.00 254 99.21 99.21 0.00e+00 REF NP_249886 "hypothetical protein PA1195 [Pseudomonas aeruginosa PAO1]" 100.00 254 99.21 99.21 0.00e+00 REF WP_003082466 "N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa]" 100.00 254 98.82 99.21 0.00e+00 REF WP_003086612 "MULTISPECIES: N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas]" 100.00 254 99.21 99.21 0.00e+00 REF WP_003123128 "N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas aeruginosa]" 100.00 254 98.82 99.21 0.00e+00 REF WP_003133711 "MULTISPECIES: N(G),N(G)-dimethylarginine dimethylaminohydrolase [Pseudomonas]" 100.00 254 98.82 99.21 0.00e+00 SP Q9I4E3 "RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase; Short=DDAH; Short=Dimethylarginine dimethylaminohydrolase; Alt" 100.00 254 99.21 99.21 0.00e+00 stop_ save_ ############# # Ligands # ############# save_CIR _Saveframe_category ligand _Mol_type "non-polymer (L-PEPTIDE LINKING)" _Name_common CITRULLINE _BMRB_code CIR _PDB_code CIR _Molecular_mass 175.186 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? N6 N6 N . 0 . ? C7 C7 C . 0 . ? O7 O7 O . 0 . ? N8 N8 N . 0 . ? HO2 HO2 H . 0 . ? H2 H2 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? HN6 HN6 H . 0 . ? HN81 HN81 H . 0 . ? HN82 HN82 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? SING C2 N2 ? ? SING C2 C3 ? ? SING C2 H2 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 N6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING N6 C7 ? ? SING N6 HN6 ? ? DOUB C7 O7 ? ? SING C7 N8 ? ? SING N8 HN81 ? ? SING N8 HN82 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $PaDDAH g-proteobacteria 208964 Bacteria . Pseudomonas aeruginosa PAO1 PA1195 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 $PaDDAH 'recombinant technology' . Escherichia coli 'BL21 DE3' pPROEX-HTa stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PaDDAH 0.7 uM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR_Analysis _Saveframe_category software _Name CCPNMR_Analysis _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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' 0.1 . M pH 7 . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' 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 'Dimethylarginine Dimethylaminohydrolase' _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 H H 7.610 0.011 1 2 1 1 MET CA C 55.342 0.008 1 3 1 1 MET CB C 35.909 0.345 1 4 1 1 MET N N 120.923 0.125 1 5 2 2 PHE H H 9.531 0.009 1 6 2 2 PHE CA C 55.727 0.062 1 7 2 2 PHE CB C 39.847 0.261 1 8 2 2 PHE N N 119.690 0.124 1 9 3 3 LYS H H 9.611 0.010 1 10 3 3 LYS CA C 56.919 0.256 1 11 3 3 LYS CB C 35.371 0.000 1 12 3 3 LYS N N 120.236 0.142 1 13 4 4 HIS H H 8.724 0.018 1 14 4 4 HIS CA C 54.611 0.257 1 15 4 4 HIS CB C 32.524 0.000 1 16 4 4 HIS N N 119.133 0.091 1 17 5 5 ILE H H 8.081 0.016 1 18 5 5 ILE CA C 56.596 0.337 1 19 5 5 ILE CB C 39.597 0.250 1 20 5 5 ILE N N 115.940 0.129 1 21 6 6 ILE H H 8.533 0.011 1 22 6 6 ILE CA C 60.176 0.236 1 23 6 6 ILE CB C 41.794 0.000 1 24 6 6 ILE N N 125.031 0.090 1 25 7 7 ALA H H 8.949 0.008 1 26 7 7 ALA CA C 50.913 0.268 1 27 7 7 ALA CB C 23.555 0.000 1 28 7 7 ALA N N 128.849 0.077 1 29 8 8 ARG H H 9.862 0.012 1 30 8 8 ARG CA C 55.750 0.321 1 31 8 8 ARG CB C 33.602 0.000 1 32 8 8 ARG N N 121.756 0.138 1 33 9 9 THR H H 7.934 0.010 1 34 9 9 THR CA C 61.832 0.000 1 35 9 9 THR CB C 71.496 0.000 1 36 9 9 THR N N 124.037 0.090 1 37 10 10 PRO CA C 62.040 0.000 1 38 10 10 PRO CB C 33.188 0.250 1 39 11 11 ALA H H 7.935 0.013 1 40 11 11 ALA CA C 50.468 0.227 1 41 11 11 ALA CB C 19.813 0.251 1 42 11 11 ALA N N 125.064 0.103 1 43 12 12 ARG H H 10.376 0.009 1 44 12 12 ARG CA C 59.795 0.000 1 45 12 12 ARG CB C 28.769 0.000 1 46 12 12 ARG N N 124.056 0.071 1 47 13 13 SER H H 8.651 0.015 1 48 13 13 SER CA C 58.442 0.000 1 49 13 13 SER CB C 62.838 0.000 1 50 13 13 SER N N 112.697 0.113 1 51 14 14 LEU H H 8.014 0.015 1 52 14 14 LEU CA C 58.414 0.052 1 53 14 14 LEU CB C 42.803 0.000 1 54 14 14 LEU N N 126.075 0.029 1 55 15 15 VAL H H 6.761 0.016 1 56 15 15 VAL CA C 63.933 0.000 1 57 15 15 VAL CB C 30.945 0.000 1 58 15 15 VAL N N 109.625 0.108 1 59 16 16 ASP H H 8.325 0.019 1 60 16 16 ASP CA C 54.191 0.196 1 61 16 16 ASP CB C 41.375 0.244 1 62 16 16 ASP N N 121.287 0.000 1 63 17 17 GLY H H 8.212 0.007 1 64 17 17 GLY CA C 45.568 0.253 1 65 17 17 GLY N N 109.562 0.193 1 66 18 18 LEU CA C 56.653 0.000 1 67 18 18 LEU CB C 42.287 0.000 1 68 19 19 THR H H 7.940 0.014 1 69 19 19 THR CA C 60.004 0.000 1 70 19 19 THR CB C 69.762 0.000 1 71 19 19 THR N N 111.040 0.056 1 72 20 20 SER CA C 57.800 0.000 1 73 20 20 SER CB C 65.246 0.259 1 74 21 21 SER H H 8.776 0.011 1 75 21 21 SER CA C 58.688 0.000 1 76 21 21 SER CB C 64.704 0.250 1 77 21 21 SER N N 120.634 0.159 1 78 22 22 HIS CA C 55.337 0.015 1 79 22 22 HIS CB C 29.582 0.000 1 80 23 23 LEU H H 8.312 0.013 1 81 23 23 LEU CA C 54.528 0.000 1 82 23 23 LEU CB C 44.516 0.221 1 83 23 23 LEU N N 121.541 0.022 1 84 24 24 GLY H H 8.132 0.010 1 85 24 24 GLY CA C 43.763 0.000 1 86 24 24 GLY N N 108.384 0.079 1 87 25 25 LYS H H 8.415 0.011 1 88 25 25 LYS CA C 53.827 0.000 1 89 25 25 LYS CB C 32.693 0.000 1 90 25 25 LYS N N 118.077 0.076 1 91 26 26 PRO CA C 63.019 0.000 1 92 26 26 PRO CB C 32.815 0.250 1 93 27 27 ASP H H 9.030 0.011 1 94 27 27 ASP CA C 52.418 0.016 1 95 27 27 ASP CB C 43.117 0.310 1 96 27 27 ASP N N 124.645 0.104 1 97 28 28 TYR H H 8.922 0.012 1 98 28 28 TYR CA C 62.419 0.217 1 99 28 28 TYR CB C 38.317 0.000 1 100 28 28 TYR N N 127.555 0.109 1 101 29 29 ALA H H 8.258 0.010 1 102 29 29 ALA CA C 55.595 0.045 1 103 29 29 ALA CB C 18.137 0.008 1 104 29 29 ALA N N 120.489 0.067 1 105 30 30 LYS H H 8.051 0.018 1 106 30 30 LYS CA C 58.595 0.248 1 107 30 30 LYS CB C 31.942 0.250 1 108 30 30 LYS N N 119.211 0.189 1 109 31 31 ALA H H 8.927 0.017 1 110 31 31 ALA CA C 54.754 0.016 1 111 31 31 ALA CB C 17.363 0.000 1 112 31 31 ALA N N 123.050 0.162 1 113 32 32 LEU H H 8.927 0.013 1 114 32 32 LEU CA C 58.696 0.244 1 115 32 32 LEU CB C 41.669 0.242 1 116 32 32 LEU N N 126.216 0.078 1 117 33 33 GLU H H 7.415 0.011 1 118 33 33 GLU CA C 60.171 0.323 1 119 33 33 GLU CB C 29.946 0.000 1 120 33 33 GLU N N 120.124 0.164 1 121 34 34 GLN H H 8.659 0.005 1 122 34 34 GLN CA C 58.969 0.027 1 123 34 34 GLN CB C 27.631 0.000 1 124 34 34 GLN N N 119.787 0.112 1 125 35 35 HIS H H 8.641 0.020 1 126 35 35 HIS CA C 63.232 0.207 1 127 35 35 HIS CB C 30.514 0.000 1 128 35 35 HIS N N 122.794 0.000 1 129 36 36 ASN H H 8.615 0.015 1 130 36 36 ASN CA C 56.459 0.036 1 131 36 36 ASN CB C 38.074 0.230 1 132 36 36 ASN N N 116.261 0.086 1 133 37 37 ALA H H 8.155 0.026 1 134 37 37 ALA CA C 55.095 0.202 1 135 37 37 ALA CB C 17.916 0.101 1 136 37 37 ALA N N 122.240 0.073 1 137 38 38 TYR H H 8.138 0.016 1 138 38 38 TYR CA C 61.269 0.000 1 139 38 38 TYR CB C 38.188 0.400 1 140 38 38 TYR N N 122.983 0.009 1 141 39 39 ILE H H 8.315 0.040 1 142 39 39 ILE CA C 62.408 0.019 1 143 39 39 ILE CB C 35.253 0.400 1 144 39 39 ILE N N 119.304 0.109 1 145 40 40 GLU H H 8.307 0.012 1 146 40 40 GLU CA C 59.770 0.000 1 147 40 40 GLU CB C 28.748 0.000 1 148 40 40 GLU N N 119.122 0.000 1 149 41 41 ALA H H 7.771 0.011 1 150 41 41 ALA CA C 54.864 0.220 1 151 41 41 ALA CB C 18.330 0.280 1 152 41 41 ALA N N 120.448 0.170 1 153 42 42 LEU H H 7.872 0.009 1 154 42 42 LEU CA C 58.199 0.035 1 155 42 42 LEU CB C 41.810 0.229 1 156 42 42 LEU N N 121.017 0.094 1 157 43 43 GLN H H 8.324 0.012 1 158 43 43 GLN CA C 57.470 0.000 1 159 43 43 GLN CB C 28.111 0.000 1 160 43 43 GLN N N 116.656 0.000 1 161 44 44 THR H H 7.429 0.013 1 162 44 44 THR CA C 62.782 0.022 1 163 44 44 THR CB C 69.778 0.214 1 164 44 44 THR N N 108.609 0.077 1 165 45 45 CYS H H 7.626 0.008 1 166 45 45 CYS CA C 59.877 0.000 1 167 45 45 CYS CB C 27.768 0.000 1 168 45 45 CYS N N 117.617 0.103 1 169 46 46 ASP H H 8.086 0.011 1 170 46 46 ASP CA C 56.202 0.276 1 171 46 46 ASP CB C 39.066 0.029 1 172 46 46 ASP N N 115.600 0.136 1 173 47 47 VAL H H 6.608 0.013 1 174 47 47 VAL CA C 58.173 0.000 1 175 47 47 VAL CB C 35.512 0.000 1 176 47 47 VAL N N 105.718 0.000 1 177 48 48 ASP H H 7.889 0.009 1 178 48 48 ASP CA C 52.246 0.035 1 179 48 48 ASP CB C 42.965 0.234 1 180 48 48 ASP N N 119.189 0.001 1 181 49 49 ILE H H 8.549 0.011 1 182 49 49 ILE CA C 60.141 0.000 1 183 49 49 ILE CB C 39.286 0.236 1 184 49 49 ILE N N 120.416 0.129 1 185 50 50 THR H H 8.787 0.009 1 186 50 50 THR CA C 63.326 0.000 1 187 50 50 THR CB C 69.741 0.000 1 188 50 50 THR N N 127.992 0.079 1 189 51 51 LEU H H 8.867 0.010 1 190 51 51 LEU CA C 53.299 0.000 1 191 51 51 LEU CB C 43.554 0.000 1 192 51 51 LEU N N 129.609 0.021 1 193 52 52 LEU H H 9.452 0.020 1 194 52 52 LEU CA C 52.440 0.000 1 195 52 52 LEU CB C 40.918 0.000 1 196 52 52 LEU N N 130.102 0.076 1 197 54 54 PRO CA C 62.016 0.023 1 198 54 54 PRO CB C 32.243 0.400 1 199 55 55 ASP H H 8.159 0.014 1 200 55 55 ASP CA C 53.131 0.000 1 201 55 55 ASP CB C 43.790 0.000 1 202 55 55 ASP N N 119.551 0.005 1 203 56 56 GLU H H 8.659 0.027 1 204 56 56 GLU CA C 57.459 0.000 1 205 56 56 GLU CB C 30.287 0.000 1 206 56 56 GLU N N 121.956 0.029 1 207 57 57 ARG H H 8.308 0.009 1 208 57 57 ARG CA C 58.184 0.000 1 209 57 57 ARG CB C 30.196 0.000 1 210 57 57 ARG N N 116.728 0.023 1 211 58 58 PHE H H 7.521 0.011 1 212 58 58 PHE CA C 55.172 0.000 1 213 58 58 PHE CB C 41.304 0.000 1 214 58 58 PHE N N 113.719 0.077 1 215 59 59 PRO CA C 66.231 0.022 1 216 59 59 PRO CB C 33.647 0.250 1 217 60 60 ASP H H 8.573 0.009 1 218 60 60 ASP CA C 55.406 0.232 1 219 60 60 ASP CB C 44.316 0.228 1 220 60 60 ASP N N 112.307 0.013 1 221 61 61 SER H H 8.359 0.010 1 222 61 61 SER CA C 61.180 0.000 1 223 61 61 SER CB C 64.992 0.000 1 224 61 61 SER N N 112.890 0.102 1 225 62 62 VAL H H 7.024 0.010 1 226 62 62 VAL CA C 62.450 0.000 1 227 62 62 VAL CB C 31.137 0.000 1 228 62 62 VAL N N 120.896 0.099 1 229 63 63 PHE H H 8.249 0.013 1 230 63 63 PHE CA C 54.825 0.016 1 231 63 63 PHE CB C 34.577 0.000 1 232 63 63 PHE N N 125.909 0.030 1 233 64 64 VAL H H 7.411 0.023 1 234 64 64 VAL CA C 62.762 0.047 1 235 64 64 VAL CB C 31.164 0.000 1 236 64 64 VAL N N 114.662 0.074 1 237 65 65 GLU H H 7.654 0.010 1 238 65 65 GLU CA C 58.345 0.000 1 239 65 65 GLU CB C 31.472 0.000 1 240 65 65 GLU N N 117.057 0.029 1 241 66 66 ASP H H 6.880 0.014 1 242 66 66 ASP CA C 59.578 0.000 1 243 66 66 ASP CB C 39.961 0.000 1 244 66 66 ASP N N 109.242 0.026 1 245 67 67 PRO CA C 65.383 0.329 1 246 67 67 PRO CB C 32.628 0.236 1 247 68 68 VAL H H 6.954 0.013 1 248 68 68 VAL CA C 61.145 0.236 1 249 68 68 VAL CB C 35.663 0.000 1 250 68 68 VAL N N 114.405 0.093 1 251 69 69 LEU H H 8.666 0.002 1 252 69 69 LEU CA C 52.993 0.000 1 253 69 69 LEU CB C 45.856 0.287 1 254 69 69 LEU N N 123.063 0.134 1 255 70 70 CYS H H 10.121 0.015 1 256 70 70 CYS CA C 59.555 0.083 1 257 70 70 CYS CB C 28.410 0.261 1 258 70 70 CYS N N 127.182 0.085 1 259 71 71 THR H H 8.199 0.016 1 260 71 71 THR CA C 60.319 0.000 1 261 71 71 THR CB C 72.646 0.265 1 262 71 71 THR N N 115.882 0.118 1 263 72 72 SER H H 10.079 0.008 1 264 72 72 SER CA C 61.131 0.000 1 265 72 72 SER CB C 62.842 0.000 1 266 72 72 SER N N 116.696 0.068 1 267 73 73 ARG H H 7.980 0.011 1 268 73 73 ARG CA C 55.813 0.040 1 269 73 73 ARG CB C 33.520 0.000 1 270 73 73 ARG N N 117.776 0.063 1 271 74 74 CYS H H 7.165 0.012 1 272 74 74 CYS CA C 56.530 0.025 1 273 74 74 CYS CB C 28.440 0.250 1 274 74 74 CYS N N 109.401 0.041 1 275 75 75 ALA H H 8.256 0.010 1 276 75 75 ALA CA C 49.643 0.041 1 277 75 75 ALA CB C 21.263 0.514 1 278 75 75 ALA N N 123.202 0.092 1 279 76 76 ILE H H 9.138 0.012 1 280 76 76 ILE CA C 59.948 0.000 1 281 76 76 ILE CB C 40.472 0.000 1 282 76 76 ILE N N 120.056 0.153 1 283 77 77 ILE H H 9.076 0.008 1 284 77 77 ILE CA C 60.095 0.000 1 285 77 77 ILE CB C 35.697 0.000 1 286 77 77 ILE N N 128.825 0.061 1 287 78 78 THR H H 8.277 0.012 1 288 78 78 THR CA C 60.507 0.005 1 289 78 78 THR CB C 65.366 0.000 1 290 78 78 THR N N 119.143 0.027 1 291 79 79 ARG H H 7.391 0.007 1 292 79 79 ARG CA C 54.782 0.000 1 293 79 79 ARG CB C 30.210 0.000 1 294 79 79 ARG N N 112.406 0.014 1 295 80 80 PRO CA C 64.339 0.016 1 296 80 80 PRO CB C 31.904 0.250 1 297 81 81 GLY H H 9.087 0.009 1 298 81 81 GLY CA C 46.806 0.218 1 299 81 81 GLY N N 112.594 0.053 1 300 82 82 ALA H H 7.496 0.013 1 301 82 82 ALA CA C 51.262 0.000 1 302 82 82 ALA CB C 17.466 0.000 1 303 82 82 ALA N N 122.729 0.060 1 304 83 83 GLU H H 9.193 0.016 1 305 83 83 GLU CA C 60.899 0.000 1 306 83 83 GLU CB C 29.535 0.250 1 307 83 83 GLU N N 128.301 0.000 1 308 84 84 SER H H 8.703 0.016 1 309 84 84 SER CA C 60.688 0.000 1 310 84 84 SER CB C 62.843 0.000 1 311 84 84 SER N N 112.280 0.033 1 312 85 85 ARG H H 7.642 0.011 1 313 85 85 ARG CA C 56.513 0.238 1 314 85 85 ARG CB C 29.787 0.000 1 315 85 85 ARG N N 117.097 0.000 1 316 86 86 ARG H H 7.532 0.011 1 317 86 86 ARG CA C 61.433 0.251 1 318 86 86 ARG CB C 29.504 0.000 1 319 86 86 ARG N N 122.245 0.000 1 320 87 87 GLY H H 9.110 0.014 1 321 87 87 GLY CA C 46.172 0.018 1 322 87 87 GLY N N 103.560 0.061 1 323 88 88 GLU H H 7.558 0.010 1 324 88 88 GLU CA C 58.324 0.030 1 325 88 88 GLU CB C 30.748 0.203 1 326 88 88 GLU N N 119.027 0.057 1 327 89 89 THR H H 7.465 0.011 1 328 89 89 THR CA C 64.359 0.020 1 329 89 89 THR CB C 66.855 0.000 1 330 89 89 THR N N 106.937 0.014 1 331 90 90 GLU H H 6.919 0.014 1 332 90 90 GLU CA C 58.536 0.000 1 333 90 90 GLU CB C 29.591 0.000 1 334 90 90 GLU N N 120.887 0.094 1 335 91 91 ILE H H 6.596 0.014 1 336 91 91 ILE CA C 63.125 0.000 1 337 91 91 ILE CB C 37.970 0.000 1 338 91 91 ILE N N 105.200 0.102 1 339 92 92 ILE H H 7.281 0.013 1 340 92 92 ILE CA C 60.650 0.234 1 341 92 92 ILE CB C 42.464 0.347 1 342 92 92 ILE N N 122.319 0.093 1 343 93 93 GLU H H 7.210 0.012 1 344 93 93 GLU CA C 60.856 0.000 1 345 93 93 GLU CB C 28.965 0.250 1 346 93 93 GLU N N 123.872 0.112 1 347 94 94 GLU H H 9.100 0.013 1 348 94 94 GLU CA C 60.094 0.024 1 349 94 94 GLU CB C 29.700 0.000 1 350 94 94 GLU N N 118.539 0.111 1 351 95 95 THR H H 7.563 0.013 1 352 95 95 THR CA C 67.169 0.030 1 353 95 95 THR CB C 69.173 0.000 1 354 95 95 THR N N 116.347 0.003 1 355 96 96 VAL H H 7.624 0.012 1 356 96 96 VAL CA C 67.607 0.000 1 357 96 96 VAL CB C 31.835 0.204 1 358 96 96 VAL N N 120.071 0.157 1 359 97 97 GLN H H 8.687 0.021 1 360 97 97 GLN CA C 59.118 0.000 1 361 97 97 GLN CB C 28.002 0.000 1 362 97 97 GLN N N 118.276 0.077 1 363 98 98 HIS H H 7.376 0.009 1 364 98 98 HIS CA C 58.901 0.000 1 365 98 98 HIS CB C 28.841 0.250 1 366 98 98 HIS N N 115.617 0.039 1 367 99 99 PHE H H 7.254 0.012 1 368 99 99 PHE CA C 60.851 0.000 1 369 99 99 PHE CB C 41.708 0.250 1 370 99 99 PHE N N 114.603 0.013 1 371 100 100 TYR H H 8.039 0.010 1 372 100 100 TYR CA C 56.459 0.000 1 373 100 100 TYR CB C 38.454 0.250 1 374 100 100 TYR N N 119.524 0.093 1 375 101 101 PRO CA C 65.042 0.000 1 376 101 101 PRO CB C 30.474 0.108 1 377 102 102 GLY H H 8.960 0.015 1 378 102 102 GLY CA C 46.274 0.236 1 379 102 102 GLY N N 113.665 0.083 1 380 103 103 LYS H H 8.301 0.012 1 381 103 103 LYS CA C 54.478 0.224 1 382 103 103 LYS CB C 33.675 0.000 1 383 103 103 LYS N N 121.380 0.197 1 384 104 104 VAL H H 7.828 0.009 1 385 104 104 VAL CA C 62.160 0.029 1 386 104 104 VAL CB C 33.095 0.331 1 387 104 104 VAL N N 119.416 0.059 1 388 105 105 GLU H H 8.963 0.009 1 389 105 105 GLU CA C 54.152 0.000 1 390 105 105 GLU CB C 32.456 0.250 1 391 105 105 GLU N N 129.387 0.116 1 392 106 106 ARG H H 9.006 0.014 1 393 106 106 ARG CA C 55.235 0.000 1 394 106 106 ARG CB C 32.737 0.000 1 395 106 106 ARG N N 116.578 0.068 1 396 107 107 ILE H H 7.598 0.011 1 397 107 107 ILE CA C 57.032 0.000 1 398 107 107 ILE CB C 35.689 0.000 1 399 107 107 ILE N N 120.783 0.042 1 400 108 108 GLU H H 9.485 0.015 1 401 108 108 GLU CA C 54.114 0.000 1 402 108 108 GLU CB C 32.699 0.000 1 403 108 108 GLU N N 126.161 0.051 1 404 109 109 ALA H H 9.196 0.005 1 405 109 109 ALA CA C 52.155 0.000 1 406 109 109 ALA CB C 16.631 0.000 1 407 109 109 ALA N N 126.330 0.105 1 408 110 110 PRO CA C 63.910 0.014 1 409 110 110 PRO CB C 32.692 0.000 1 410 111 111 GLY H H 9.088 0.000 1 411 111 111 GLY CA C 45.854 0.256 1 412 111 111 GLY N N 113.749 0.169 1 413 112 112 THR H H 8.648 0.015 1 414 112 112 THR CA C 59.689 0.000 1 415 112 112 THR CB C 70.103 0.000 1 416 112 112 THR N N 114.671 0.099 1 417 113 113 VAL H H 8.395 0.011 1 418 113 113 VAL CA C 60.050 0.000 1 419 113 113 VAL CB C 38.436 0.000 1 420 113 113 VAL N N 119.029 0.029 1 421 114 114 GLU H H 8.529 0.014 1 422 114 114 GLU CA C 54.734 0.217 1 423 114 114 GLU CB C 31.555 0.285 1 424 114 114 GLU N N 124.526 0.101 1 425 115 115 ALA H H 9.589 0.013 1 426 115 115 ALA CA C 55.036 0.000 1 427 115 115 ALA CB C 17.017 0.000 1 428 115 115 ALA N N 125.881 0.059 1 429 116 116 GLY H H 8.809 0.011 1 430 116 116 GLY CA C 47.617 0.015 1 431 116 116 GLY N N 111.434 0.102 1 432 117 117 ASP H H 8.275 0.009 1 433 117 117 ASP CA C 55.784 0.000 1 434 117 117 ASP CB C 40.901 0.000 1 435 117 117 ASP N N 117.132 0.123 1 436 118 118 ILE H H 7.775 0.005 1 437 118 118 ILE CA C 60.734 0.018 1 438 118 118 ILE CB C 38.675 0.000 1 439 118 118 ILE N N 119.275 0.022 1 440 119 119 MET H H 9.239 0.009 1 441 119 119 MET CA C 53.722 0.000 1 442 119 119 MET CB C 38.224 0.258 1 443 119 119 MET N N 127.670 0.097 1 444 120 120 MET H H 9.320 0.011 1 445 120 120 MET CA C 55.403 0.033 1 446 120 120 MET CB C 34.477 0.000 1 447 120 120 MET N N 130.110 0.051 1 448 121 121 VAL H H 9.280 0.010 1 449 121 121 VAL CA C 60.782 0.288 1 450 121 121 VAL CB C 31.922 0.250 1 451 121 121 VAL N N 104.287 0.018 1 452 122 122 GLY H H 9.426 0.011 1 453 122 122 GLY CA C 47.398 0.001 1 454 122 122 GLY N N 120.639 0.086 1 455 123 123 ASP H H 8.414 0.008 1 456 123 123 ASP CA C 53.836 0.030 1 457 123 123 ASP CB C 41.286 0.000 1 458 123 123 ASP N N 127.065 0.092 1 459 124 124 HIS H H 7.927 0.010 1 460 124 124 HIS CA C 54.506 0.000 1 461 124 124 HIS CB C 33.581 0.000 1 462 124 124 HIS N N 119.241 0.011 1 463 125 125 PHE H H 7.853 0.011 1 464 125 125 PHE CA C 55.826 0.038 1 465 125 125 PHE CB C 39.613 0.000 1 466 125 125 PHE N N 125.180 0.015 1 467 126 126 TYR H H 8.867 0.013 1 468 126 126 TYR CA C 58.311 0.002 1 469 126 126 TYR CB C 39.842 0.260 1 470 126 126 TYR N N 123.094 0.185 1 471 127 127 ILE H H 9.297 0.011 1 472 127 127 ILE CA C 59.904 0.009 1 473 127 127 ILE CB C 40.617 0.169 1 474 127 127 ILE N N 123.288 0.097 1 475 128 128 GLY H H 10.436 0.007 1 476 128 128 GLY CA C 45.580 0.033 1 477 128 128 GLY N N 117.204 0.063 1 478 129 129 GLU H H 8.013 0.011 1 479 129 129 GLU CA C 55.732 0.270 1 480 129 129 GLU CB C 30.880 0.000 1 481 129 129 GLU N N 123.188 0.211 1 482 130 130 SER H H 9.164 0.017 1 483 130 130 SER CA C 56.662 0.012 1 484 130 130 SER CB C 68.538 0.000 1 485 130 130 SER N N 126.329 0.142 1 486 131 131 ALA H H 8.790 0.010 1 487 131 131 ALA CA C 53.714 0.000 1 488 131 131 ALA CB C 18.509 0.250 1 489 131 131 ALA N N 120.094 0.090 1 490 132 132 ARG H H 8.632 0.010 1 491 132 132 ARG CA C 55.126 0.000 1 492 132 132 ARG CB C 31.316 0.000 1 493 132 132 ARG N N 117.225 0.030 1 494 133 133 THR H H 7.801 0.014 1 495 133 133 THR CA C 61.671 0.030 1 496 133 133 THR CB C 69.691 0.000 1 497 133 133 THR N N 121.928 0.000 1 498 134 134 ASN H H 8.193 0.012 1 499 134 134 ASN CA C 49.865 0.025 1 500 134 134 ASN CB C 39.796 0.000 1 501 134 134 ASN N N 120.994 0.009 1 502 135 135 ALA H H 8.484 0.011 1 503 135 135 ALA CA C 55.446 0.000 1 504 135 135 ALA CB C 18.897 0.000 1 505 135 135 ALA N N 121.656 0.072 1 506 136 136 GLU H H 8.564 0.016 1 507 136 136 GLU CA C 57.749 0.030 1 508 136 136 GLU CB C 28.481 0.231 1 509 136 136 GLU N N 119.129 0.092 1 510 137 137 GLY H H 8.884 0.017 1 511 137 137 GLY CA C 47.402 0.320 1 512 137 137 GLY N N 110.504 0.085 1 513 138 138 ALA H H 8.676 0.008 1 514 138 138 ALA CA C 55.725 0.000 1 515 138 138 ALA CB C 17.596 0.000 1 516 138 138 ALA N N 123.387 0.103 1 517 139 139 ARG H H 8.258 0.007 1 518 139 139 ARG CA C 59.810 0.000 1 519 139 139 ARG CB C 29.631 0.250 1 520 139 139 ARG N N 117.557 0.111 1 521 140 140 GLN H H 8.301 0.022 1 522 140 140 GLN CA C 59.419 0.005 1 523 140 140 GLN CB C 30.647 0.250 1 524 140 140 GLN N N 119.432 0.046 1 525 141 141 MET H H 8.320 0.010 1 526 141 141 MET CA C 56.915 0.000 1 527 141 141 MET CB C 30.403 0.248 1 528 141 141 MET N N 117.767 0.112 1 529 142 142 ILE H H 8.376 0.013 1 530 142 142 ILE CA C 66.530 0.042 1 531 142 142 ILE CB C 37.876 0.109 1 532 142 142 ILE N N 119.428 0.069 1 533 143 143 ALA H H 7.678 0.012 1 534 143 143 ALA CA C 55.220 0.000 1 535 143 143 ALA CB C 17.370 0.000 1 536 143 143 ALA N N 120.554 0.024 1 537 144 144 ILE H H 7.939 0.011 1 538 144 144 ILE CA C 65.949 0.280 1 539 144 144 ILE CB C 38.201 0.000 1 540 144 144 ILE N N 120.068 0.113 1 541 145 145 LEU H H 8.378 0.011 1 542 145 145 LEU CA C 58.582 0.000 1 543 145 145 LEU CB C 39.460 0.000 1 544 145 145 LEU N N 119.974 0.089 1 545 146 146 GLU H H 8.655 0.015 1 546 146 146 GLU CA C 59.333 0.047 1 547 146 146 GLU CB C 28.627 0.000 1 548 146 146 GLU N N 118.251 0.216 1 549 147 147 LYS H H 7.772 0.010 1 550 147 147 LYS CA C 59.123 0.001 1 551 147 147 LYS CB C 32.040 0.000 1 552 147 147 LYS N N 122.668 0.028 1 553 148 148 HIS H H 7.369 0.010 1 554 148 148 HIS CA C 56.928 0.278 1 555 148 148 HIS CB C 31.278 0.268 1 556 148 148 HIS N N 115.837 0.024 1 557 149 149 GLY H H 7.937 0.016 1 558 149 149 GLY CA C 46.403 0.264 1 559 149 149 GLY N N 107.815 0.099 1 560 150 150 LEU H H 8.163 0.011 1 561 150 150 LEU CA C 53.091 0.016 1 562 150 150 LEU CB C 43.790 0.000 1 563 150 150 LEU N N 122.098 0.272 1 564 151 151 SER H H 8.456 0.010 1 565 151 151 SER CA C 57.575 0.248 1 566 151 151 SER CB C 66.562 0.303 1 567 151 151 SER N N 111.856 0.092 1 568 152 152 GLY H H 8.588 0.016 1 569 152 152 GLY CA C 46.045 0.285 1 570 152 152 GLY N N 105.043 0.048 1 571 153 153 SER H H 8.365 0.015 1 572 153 153 SER CA C 57.528 0.029 1 573 153 153 SER CB C 65.427 0.259 1 574 153 153 SER N N 113.313 0.103 1 575 154 154 VAL H H 8.545 0.013 1 576 154 154 VAL CA C 61.690 0.244 1 577 154 154 VAL CB C 34.060 0.269 1 578 154 154 VAL N N 120.027 0.150 1 579 155 155 VAL H H 9.247 0.009 1 580 155 155 VAL CA C 60.562 0.034 1 581 155 155 VAL CB C 34.785 0.000 1 582 155 155 VAL N N 129.131 0.097 1 583 156 156 ARG H H 8.802 0.011 1 584 156 156 ARG CA C 56.925 0.000 1 585 156 156 ARG CB C 29.805 0.000 1 586 156 156 ARG N N 127.134 0.094 1 587 157 157 LEU H H 8.154 0.019 1 588 157 157 LEU CA C 54.277 0.046 1 589 157 157 LEU CB C 44.621 0.000 1 590 157 157 LEU N N 121.440 0.080 1 591 158 158 GLU H H 10.667 0.012 1 592 158 158 GLU CA C 57.396 0.000 1 593 158 158 GLU CB C 33.186 0.000 1 594 158 158 GLU N N 120.332 0.070 1 595 159 159 LYS H H 9.594 0.013 1 596 159 159 LYS CA C 57.325 0.272 1 597 159 159 LYS CB C 34.470 0.230 1 598 159 159 LYS N N 118.449 0.105 1 599 160 160 VAL H H 6.990 0.012 1 600 160 160 VAL CA C 59.505 0.000 1 601 160 160 VAL CB C 35.248 0.000 1 602 160 160 VAL N N 109.835 0.099 1 603 161 161 LEU H H 8.083 0.011 1 604 161 161 LEU CA C 57.727 0.000 1 605 161 161 LEU CB C 41.475 0.000 1 606 161 161 LEU N N 120.581 0.020 1 607 162 162 HIS H H 7.061 0.000 1 608 162 162 HIS CA C 51.998 0.008 1 609 162 162 HIS CB C 33.451 0.250 1 610 162 162 HIS N N 105.893 0.000 1 611 163 163 LEU H H 10.232 0.014 1 612 163 163 LEU CA C 59.725 0.321 1 613 163 163 LEU CB C 44.837 0.000 1 614 163 163 LEU N N 124.061 0.103 1 615 164 164 LYS H H 7.266 0.008 1 616 164 164 LYS CA C 58.925 0.000 1 617 164 164 LYS CB C 29.319 0.250 1 618 164 164 LYS N N 107.043 0.088 1 619 165 165 THR H H 8.159 0.019 1 620 165 165 THR CA C 67.040 0.011 1 621 165 165 THR CB C 69.494 0.247 1 622 165 165 THR N N 116.558 0.053 1 623 166 166 GLY H H 7.380 0.013 1 624 166 166 GLY CA C 45.389 0.019 1 625 166 166 GLY N N 104.527 0.052 1 626 167 167 LEU H H 6.492 0.009 1 627 167 167 LEU CA C 53.494 0.009 1 628 167 167 LEU CB C 49.632 0.000 1 629 167 167 LEU N N 120.644 0.011 1 630 168 168 ALA H H 8.038 0.019 1 631 168 168 ALA CA C 52.861 0.249 1 632 168 168 ALA CB C 23.580 0.000 1 633 168 168 ALA N N 119.039 0.150 1 634 169 169 TYR H H 10.038 0.009 1 635 169 169 TYR CA C 57.443 0.018 1 636 169 169 TYR CB C 37.675 0.400 1 637 169 169 TYR N N 123.896 0.007 1 638 170 170 LEU H H 8.628 0.013 1 639 170 170 LEU CA C 52.684 0.000 1 640 170 170 LEU CB C 40.355 0.000 1 641 170 170 LEU N N 129.858 0.072 1 642 171 171 GLU CA C 58.012 0.000 1 643 171 171 GLU CB C 28.020 0.000 1 644 172 172 HIS H H 8.657 0.013 1 645 172 172 HIS CA C 55.710 0.038 1 646 172 172 HIS CB C 26.225 0.331 1 647 172 172 HIS N N 111.723 0.011 1 648 173 173 ASN H H 8.131 0.011 1 649 173 173 ASN CA C 54.975 0.000 1 650 173 173 ASN CB C 40.566 0.000 1 651 173 173 ASN N N 108.880 0.064 1 652 174 174 ASN H H 7.738 0.028 1 653 174 174 ASN CA C 53.553 0.000 1 654 174 174 ASN CB C 39.928 0.250 1 655 174 174 ASN N N 119.327 0.205 1 656 175 175 LEU H H 8.804 0.009 1 657 175 175 LEU CA C 52.816 0.000 1 658 175 175 LEU CB C 47.876 0.000 1 659 175 175 LEU N N 128.508 0.095 1 660 176 176 LEU H H 9.354 0.014 1 661 176 176 LEU CA C 54.292 0.000 1 662 176 176 LEU CB C 41.420 0.000 1 663 176 176 LEU N N 126.739 0.064 1 664 177 177 ALA H H 8.097 0.024 1 665 177 177 ALA CA C 51.017 0.315 1 666 177 177 ALA CB C 23.427 0.400 1 667 177 177 ALA N N 120.832 0.149 1 668 178 178 ALA H H 8.618 0.016 1 669 178 178 ALA CA C 49.266 0.000 1 670 178 178 ALA CB C 23.522 0.000 1 671 178 178 ALA N N 122.010 0.082 1 672 179 179 GLY H H 8.908 0.017 1 673 179 179 GLY CA C 47.496 0.000 1 674 179 179 GLY N N 108.778 0.074 1 675 180 180 GLU H H 9.145 0.018 1 676 180 180 GLU CA C 57.395 0.000 1 677 180 180 GLU CB C 29.506 0.000 1 678 180 180 GLU N N 124.948 0.074 1 679 181 181 PHE H H 7.378 0.013 1 680 181 181 PHE CA C 60.108 0.000 1 681 181 181 PHE CB C 40.748 0.236 1 682 181 181 PHE N N 116.911 0.086 1 683 182 182 VAL H H 6.947 0.008 1 684 182 182 VAL CA C 66.459 0.281 1 685 182 182 VAL CB C 32.041 0.224 1 686 182 182 VAL N N 114.396 0.092 1 687 183 183 SER H H 7.730 0.014 1 688 183 183 SER CA C 57.054 0.000 1 689 183 183 SER CB C 63.848 0.000 1 690 183 183 SER N N 109.349 0.068 1 691 184 184 LYS H H 7.279 0.010 1 692 184 184 LYS CA C 55.151 0.000 1 693 184 184 LYS CB C 31.225 0.000 1 694 184 184 LYS N N 123.734 0.000 1 695 185 185 PRO CA C 65.322 0.022 1 696 185 185 PRO CB C 31.886 0.000 1 697 186 186 GLU H H 10.437 0.013 1 698 186 186 GLU CA C 59.606 0.000 1 699 186 186 GLU CB C 28.078 0.000 1 700 186 186 GLU N N 118.094 0.042 1 701 187 187 PHE H H 7.279 0.030 1 702 187 187 PHE CA C 55.865 0.025 1 703 187 187 PHE CB C 38.634 0.000 1 704 187 187 PHE N N 115.456 0.086 1 705 188 188 GLN H H 7.247 0.006 1 706 188 188 GLN CA C 58.158 0.031 1 707 188 188 GLN CB C 28.812 0.000 1 708 188 188 GLN N N 115.132 0.080 1 709 189 189 ASP H H 8.651 0.013 1 710 189 189 ASP CA C 54.989 0.232 1 711 189 189 ASP CB C 40.309 0.000 1 712 189 189 ASP N N 117.239 0.060 1 713 190 190 PHE H H 7.630 0.013 1 714 190 190 PHE CA C 58.550 0.010 1 715 190 190 PHE CB C 40.277 0.250 1 716 190 190 PHE N N 118.786 0.040 1 717 191 191 ASN H H 8.897 0.008 1 718 191 191 ASN CA C 53.022 0.017 1 719 191 191 ASN CB C 37.370 0.250 1 720 191 191 ASN N N 119.064 0.090 1 721 192 192 ILE H H 8.131 0.016 1 722 192 192 ILE CA C 61.919 0.026 1 723 192 192 ILE CB C 38.286 0.000 1 724 192 192 ILE N N 126.528 0.078 1 725 193 193 ILE H H 9.526 0.009 1 726 193 193 ILE CA C 59.861 0.005 1 727 193 193 ILE CB C 37.330 0.250 1 728 193 193 ILE N N 106.130 0.015 1 729 194 194 GLU H H 8.337 0.012 1 730 194 194 GLU CA C 56.166 0.034 1 731 194 194 GLU CB C 29.719 0.000 1 732 194 194 GLU N N 126.339 0.100 1 733 195 195 ILE H H 8.574 0.014 1 734 195 195 ILE CA C 55.111 0.000 1 735 195 195 ILE CB C 37.072 0.000 1 736 195 195 ILE N N 130.401 0.105 1 737 196 196 PRO CA C 62.468 0.010 1 738 196 196 PRO CB C 32.477 0.250 1 739 197 197 GLU H H 8.906 0.011 1 740 197 197 GLU CA C 60.324 0.000 1 741 197 197 GLU CB C 29.510 0.000 1 742 197 197 GLU N N 123.268 0.102 1 743 198 198 GLU H H 9.779 0.013 1 744 198 198 GLU CA C 58.925 0.025 1 745 198 198 GLU CB C 28.801 0.000 1 746 198 198 GLU N N 117.814 0.077 1 747 199 199 GLU H H 8.072 0.028 1 748 199 199 GLU CA C 55.032 0.018 1 749 199 199 GLU CB C 30.581 0.268 1 750 199 199 GLU N N 118.354 0.197 1 751 200 200 SER H H 7.307 0.044 1 752 200 200 SER CA C 63.129 0.000 1 753 200 200 SER CB C 62.260 0.236 1 754 200 200 SER N N 113.698 0.084 1 755 201 201 TYR H H 8.516 0.016 1 756 201 201 TYR CA C 60.028 0.000 1 757 201 201 TYR CB C 39.384 0.000 1 758 201 201 TYR N N 123.795 0.025 1 759 202 202 ALA H H 7.822 0.010 1 760 202 202 ALA CA C 52.395 0.188 1 761 202 202 ALA CB C 17.132 0.000 1 762 202 202 ALA N N 117.725 0.083 1 763 203 203 ALA H H 7.132 0.012 1 764 203 203 ALA CA C 53.415 0.023 1 765 203 203 ALA CB C 18.709 0.251 1 766 203 203 ALA N N 115.534 0.101 1 767 204 204 ASN H H 6.579 0.010 1 768 204 204 ASN CA C 53.283 0.000 1 769 204 204 ASN CB C 39.537 0.250 1 770 204 204 ASN N N 109.815 0.264 1 771 205 205 CYS H H 6.774 0.010 1 772 205 205 CYS CA C 57.636 0.032 1 773 205 205 CYS CB C 32.847 0.236 1 774 205 205 CYS N N 118.653 0.085 1 775 206 206 ILE H H 8.288 0.008 1 776 206 206 ILE CA C 58.184 0.061 1 777 206 206 ILE CB C 41.429 0.236 1 778 206 206 ILE N N 107.504 0.082 1 779 207 207 TRP H H 8.731 0.014 1 780 207 207 TRP HE1 H 10.626 0.000 1 781 207 207 TRP CA C 56.840 0.031 1 782 207 207 TRP CB C 31.020 0.000 1 783 207 207 TRP N N 124.360 0.000 1 784 207 207 TRP NE1 N 124.632 0.107 1 785 208 208 VAL H H 9.059 0.015 1 786 208 208 VAL CA C 62.178 0.000 1 787 208 208 VAL CB C 33.850 0.000 1 788 208 208 VAL N N 127.160 0.076 1 789 210 210 GLU CA C 59.440 0.346 1 790 210 210 GLU CB C 26.146 0.420 1 791 211 211 ARG H H 7.241 0.014 1 792 211 211 ARG CA C 55.642 0.335 1 793 211 211 ARG CB C 32.195 0.000 1 794 211 211 ARG N N 120.412 0.007 1 795 212 212 VAL H H 8.681 0.009 1 796 212 212 VAL CA C 60.536 0.227 1 797 212 212 VAL CB C 34.519 0.000 1 798 212 212 VAL N N 120.464 0.000 1 799 213 213 ILE H H 8.792 0.010 1 800 213 213 ILE CA C 59.980 0.236 1 801 213 213 ILE CB C 37.826 0.250 1 802 213 213 ILE N N 127.959 0.065 1 803 214 214 MET H H 9.077 0.009 1 804 214 214 MET CA C 51.674 0.000 1 805 214 214 MET CB C 37.149 0.000 1 806 214 214 MET N N 126.483 0.061 1 807 215 215 PRO CA C 61.250 0.000 1 808 215 215 PRO CB C 32.315 0.250 1 809 216 216 ALA H H 7.814 0.014 1 810 216 216 ALA CA C 51.997 0.005 1 811 216 216 ALA CB C 19.685 0.191 1 812 216 216 ALA N N 123.902 0.047 1 813 217 217 GLY H H 8.447 0.014 1 814 217 217 GLY CA C 44.980 0.013 1 815 217 217 GLY N N 109.025 0.035 1 816 218 218 TYR H H 9.293 0.010 1 817 218 218 TYR CA C 56.758 0.000 1 818 218 218 TYR CB C 38.304 0.000 1 819 218 218 TYR N N 122.356 0.012 1 820 219 219 PRO CA C 65.093 0.274 1 821 219 219 PRO CB C 33.010 0.000 1 822 220 220 ARG H H 10.425 0.010 1 823 220 220 ARG CA C 60.022 0.020 1 824 220 220 ARG CB C 29.533 0.269 1 825 220 220 ARG N N 123.956 0.086 1 826 221 221 THR H H 10.312 0.013 1 827 221 221 THR CA C 68.976 0.008 1 828 221 221 THR CB C 68.097 0.320 1 829 221 221 THR N N 123.608 0.075 1 830 222 222 ARG H H 8.375 0.013 1 831 222 222 ARG CA C 60.597 0.033 1 832 222 222 ARG CB C 30.035 0.297 1 833 222 222 ARG N N 121.806 0.084 1 834 223 223 GLU H H 7.729 0.009 1 835 223 223 GLU CA C 59.169 0.000 1 836 223 223 GLU CB C 29.635 0.272 1 837 223 223 GLU N N 116.305 0.054 1 838 224 224 LYS H H 7.576 0.010 1 839 224 224 LYS CA C 60.240 0.263 1 840 224 224 LYS CB C 33.248 0.177 1 841 224 224 LYS N N 117.954 0.099 1 842 225 225 ILE H H 8.062 0.013 1 843 225 225 ILE CA C 65.840 0.204 1 844 225 225 ILE CB C 39.086 0.286 1 845 225 225 ILE N N 117.697 0.183 1 846 226 226 ALA H H 8.910 0.011 1 847 226 226 ALA CA C 55.353 0.247 1 848 226 226 ALA CB C 18.044 0.347 1 849 226 226 ALA N N 127.122 0.000 1 850 227 227 ARG H H 8.035 0.035 1 851 227 227 ARG CA C 58.411 0.040 1 852 227 227 ARG CB C 30.199 0.281 1 853 227 227 ARG N N 117.668 0.135 1 854 228 228 LEU H H 7.493 0.017 1 855 228 228 LEU CA C 55.377 0.269 1 856 228 228 LEU CB C 42.417 0.000 1 857 228 228 LEU N N 118.050 0.063 1 858 229 229 GLY H H 7.846 0.014 1 859 229 229 GLY CA C 44.992 0.025 1 860 229 229 GLY N N 104.802 0.062 1 861 230 230 TYR H H 6.497 0.015 1 862 230 230 TYR CA C 57.757 0.035 1 863 230 230 TYR CB C 39.464 0.000 1 864 230 230 TYR N N 116.463 0.026 1 865 231 231 ARG H H 7.858 0.011 1 866 231 231 ARG CA C 56.093 0.000 1 867 231 231 ARG CB C 30.458 0.000 1 868 231 231 ARG N N 122.453 0.015 1 869 232 232 VAL H H 8.455 0.014 1 870 232 232 VAL CA C 62.225 0.010 1 871 232 232 VAL CB C 32.941 0.000 1 872 232 232 VAL N N 127.059 0.042 1 873 233 233 ILE H H 9.311 0.009 1 874 233 233 ILE CA C 60.932 0.022 1 875 233 233 ILE CB C 41.040 0.250 1 876 233 233 ILE N N 130.513 0.070 1 877 234 234 GLU H H 8.634 0.013 1 878 234 234 GLU CA C 54.807 0.000 1 879 234 234 GLU CB C 33.209 0.202 1 880 234 234 GLU N N 125.251 0.136 1 881 235 235 VAL H H 8.915 0.013 1 882 235 235 VAL CA C 59.395 0.000 1 883 235 235 VAL CB C 33.937 0.000 1 884 235 235 VAL N N 119.090 0.103 1 885 236 236 ASP H H 9.082 0.022 1 886 236 236 ASP CA C 54.382 0.050 1 887 236 236 ASP CB C 37.145 0.000 1 888 236 236 ASP N N 127.099 0.024 1 889 237 237 THR H H 8.252 0.015 1 890 237 237 THR CA C 60.994 0.245 1 891 237 237 THR CB C 68.040 0.000 1 892 237 237 THR N N 115.226 0.076 1 893 238 238 SER H H 8.403 0.007 1 894 238 238 SER CA C 62.530 0.002 1 895 238 238 SER CB C 62.551 0.000 1 896 238 238 SER N N 119.120 0.110 1 897 239 239 GLU H H 9.568 0.011 1 898 239 239 GLU CA C 58.502 0.021 1 899 239 239 GLU CB C 28.651 0.000 1 900 239 239 GLU N N 121.344 0.024 1 901 240 240 TYR H H 7.181 0.010 1 902 240 240 TYR CA C 61.269 0.042 1 903 240 240 TYR CB C 38.093 0.340 1 904 240 240 TYR N N 116.055 0.213 1 905 241 241 ARG H H 8.297 0.011 1 906 241 241 ARG CA C 59.550 0.000 1 907 241 241 ARG CB C 29.210 0.000 1 908 241 241 ARG N N 124.322 0.066 1 909 242 242 LYS H H 6.923 0.008 1 910 242 242 LYS CA C 59.188 0.000 1 911 242 242 LYS CB C 32.194 0.000 1 912 242 242 LYS N N 115.027 0.238 1 913 243 243 ILE H H 7.451 0.012 1 914 243 243 ILE CA C 59.951 0.000 1 915 243 243 ILE CB C 37.239 0.253 1 916 243 243 ILE N N 110.843 0.114 1 917 244 244 ASP H H 7.462 0.001 1 918 244 244 ASP CA C 55.421 0.000 1 919 244 244 ASP CB C 39.492 0.000 1 920 244 244 ASP N N 113.319 0.099 1 921 245 245 GLY H H 8.460 0.011 1 922 245 245 GLY CA C 45.245 0.000 1 923 245 245 GLY N N 104.269 0.053 1 924 246 246 GLY CA C 44.873 0.000 1 925 247 247 VAL H H 8.600 0.000 1 926 247 247 VAL CA C 64.666 0.000 1 927 247 247 VAL CB C 31.948 0.000 1 928 247 247 VAL N N 112.994 0.102 1 929 248 248 SER H H 10.387 0.012 1 930 248 248 SER CA C 61.885 0.000 1 931 248 248 SER CB C 60.719 0.000 1 932 248 248 SER N N 122.386 0.146 1 933 249 249 CYS H H 7.173 0.010 1 934 249 249 CYS CA C 57.368 0.000 1 935 249 249 CYS CB C 28.488 0.250 1 936 249 249 CYS N N 116.623 0.087 1 937 250 250 MET H H 6.375 0.000 1 938 250 250 MET CA C 56.296 0.036 1 939 250 250 MET CB C 36.312 0.250 1 940 250 250 MET N N 115.478 0.000 1 941 251 251 SER H H 7.695 0.016 1 942 251 251 SER CA C 58.470 0.023 1 943 251 251 SER CB C 66.251 0.000 1 944 251 251 SER N N 108.195 0.064 1 945 252 252 LEU H H 8.644 0.011 1 946 252 252 LEU CA C 54.150 0.000 1 947 252 252 LEU CB C 45.099 0.254 1 948 252 252 LEU N N 119.857 0.091 1 949 253 253 ARG H H 9.417 0.015 1 950 253 253 ARG CA C 54.343 0.000 1 951 253 253 ARG CB C 31.231 0.347 1 952 253 253 ARG N N 122.226 0.122 1 953 254 254 PHE H H 8.377 0.011 1 954 254 254 PHE CA C 59.316 0.000 1 955 254 254 PHE CB C 37.806 0.000 1 956 254 254 PHE N N 125.551 0.063 1 stop_ save_