data_5753 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Towards an Understanding of the Poliovirus Replication Complex: The Solution Structure of the Soluble Domain of the Poliovirus 3A Protein ; _BMRB_accession_number 5753 _BMRB_flat_file_name bmr5753.str _Entry_type original _Submission_date 2003-03-21 _Accession_date 2003-03-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Strauss D. M. . 2 Glustrom L. W. . 3 Wuttke D. S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 328 "13C chemical shifts" 253 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-08 original author . stop_ _Original_release_date 2003-08-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Towards an Understanding of the Poliovirus Replication Complex: The Solution Structure of the Soluble Domain of the Poliovirus 3A Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22708502 _PubMed_ID 12823963 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Strauss D. M. . 2 Glustrom L. W. . 3 Wuttke D. S. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 330 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 225 _Page_last 234 _Year 2003 _Details . loop_ _Keyword 'Poliovirus 3A protein' picornavirus 'symmetric dimer structure' 'unfolded domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_3A-N _Saveframe_category molecular_system _Mol_system_name 'Genome polyprotein [Core protein P3A]' _Abbreviation_common 3A-N _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label '3A monomer, chain A' $3A-N '3A monomer, chain B' $3A-N stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 '3A monomer, chain A' 1 '3A monomer, chain B' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_3A-N _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Poliovirus 3A' _Abbreviation_common 3A-N _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; MGPLQYKDLKIDIKTSPPPE CINDLLQAVDSQEVRDYCEK KGWIVNITSQVQTERNINRA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 PRO 4 LEU 5 GLN 6 TYR 7 LYS 8 ASP 9 LEU 10 LYS 11 ILE 12 ASP 13 ILE 14 LYS 15 THR 16 SER 17 PRO 18 PRO 19 PRO 20 GLU 21 CYS 22 ILE 23 ASN 24 ASP 25 LEU 26 LEU 27 GLN 28 ALA 29 VAL 30 ASP 31 SER 32 GLN 33 GLU 34 VAL 35 ARG 36 ASP 37 TYR 38 CYS 39 GLU 40 LYS 41 LYS 42 GLY 43 TRP 44 ILE 45 VAL 46 ASN 47 ILE 48 THR 49 SER 50 GLN 51 VAL 52 GLN 53 THR 54 GLU 55 ARG 56 ASN 57 ILE 58 ASN 59 ARG 60 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1NG7 "The Solution Structure Of The Soluble Domain Of Poliovirus 3a Protein" 100.00 60 100.00 100.00 2.23e-35 EMBL CAA24445 "unnamed protein product [Human poliovirus 1]" 98.33 2221 100.00 100.00 2.69e-31 EMBL CAA24446 "unnamed protein product [Human poliovirus 1]" 98.33 2207 100.00 100.00 3.55e-32 EMBL CAA24456 "unnamed protein product [Human poliovirus 1]" 98.33 752 100.00 100.00 5.33e-33 EMBL CAA24461 "polyprotein [Human poliovirus 1 Mahoney]" 98.33 2209 100.00 100.00 3.01e-32 EMBL CAA24465 "polyprotein [Human poliovirus 1 strain Sabin]" 98.33 2209 100.00 100.00 3.01e-32 GB AAA46911 "P3-1b polyprotein precursor, partial [Human poliovirus 1]" 98.33 757 100.00 100.00 5.32e-33 GB AAA46914 "viral protein precursor [Human poliovirus 3]" 98.33 2206 98.31 98.31 1.32e-30 GB AAL75970 "polyprotein [Human poliovirus 1]" 98.33 2209 98.31 100.00 4.65e-32 GB AAM09803 "polyprotein [Human poliovirus 1]" 98.33 2209 100.00 100.00 2.90e-32 GB AAM09805 "polyprotein [Human poliovirus 1]" 98.33 2209 100.00 100.00 2.73e-32 PRF 0707268A polyprotein 98.33 2221 100.00 100.00 2.69e-31 PRF 0908283A "protein P3-9" 98.33 109 100.00 100.00 5.29e-35 REF NP_041277 "genome polyprotein [Enterovirus C]" 98.33 2209 100.00 100.00 3.01e-32 REF NP_740474 "protein 3A [Human enterovirus C]" 98.33 87 100.00 100.00 2.91e-35 REF YP_007353733 "protein 3AB [Human enterovirus C]" 98.33 109 100.00 100.00 5.29e-35 SP P03300 "RecName: Full=Genome polyprotein; Contains: RecName: Full=P1; Contains: RecName: Full=Capsid protein VP0; AltName: Full=VP4-VP2" 98.33 2209 100.00 100.00 3.01e-32 SP P03301 "RecName: Full=Genome polyprotein; Contains: RecName: Full=P3; Contains: RecName: Full=Protein 3AB; Contains: RecName: Full=P1; " 98.33 2209 100.00 100.00 3.01e-32 SP P03302 "RecName: Full=Genome polyprotein; Contains: RecName: Full=P3; Contains: RecName: Full=Protein 3AB; Contains: RecName: Full=P1; " 98.33 2206 98.31 98.31 1.32e-30 SP P06209 "RecName: Full=Genome polyprotein; Contains: RecName: Full=P3; Contains: RecName: Full=Protein 3AB; Contains: RecName: Full=P1; " 98.33 2206 98.31 100.00 7.03e-32 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $3A-N Poliovirus 138953 Viruses . Enterovirus poliovirus 'type 1' 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 $3A-N 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3A-N 1.5 mM '[U-95% 13C; U-99% 15N]' 'potassium phosphate' 20 mM . NaCl 50 mM . D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $3A-N 2.0 mM '[U-95% 13C;U-99% 15N]' 'potassium phosphate' 20 mM . NaCl 50 mM . H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1a loop_ _Task collection stop_ _Details Varian save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.0 loop_ _Task processing stop_ _Details Delaglio save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'data analysis' stop_ _Details Kraulis save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task refinement stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_select/filter_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated select/filter NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated select/filter NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 298 0.2 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 DSS P 31 'methyl protons' ppm 0.0 . indirect . . . 0.404808636 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '3A monomer, chain A' _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 MET N N 126.64 0.00 1 2 . 1 MET CA C 55.58 0.07 1 3 . 1 MET HA H 3.911 0.009 1 4 . 1 MET C C 175.45 0.00 1 5 . 1 MET CB C 34.11 0.01 1 6 . 1 MET HB2 H 2.048 0.009 1 7 . 1 MET CG C 31.27 0.00 1 8 . 1 MET HG2 H 2.594 0.009 1 9 . 1 MET CE C 16.84 0.00 1 10 . 1 MET HE H 2.061 0.003 1 11 . 2 GLY N N 111.94 0.01 1 12 . 2 GLY CA C 44.50 0.11 1 13 . 2 GLY HA2 H 4.086 0.011 1 14 . 2 GLY HA3 H 4.155 0.005 1 15 . 3 PRO N N 111.56 0.00 1 16 . 3 PRO CA C 63.30 0.12 1 17 . 3 PRO HA H 4.380 0.008 1 18 . 3 PRO C C 177.19 0.00 1 19 . 3 PRO CB C 32.23 0.20 1 20 . 3 PRO HB2 H 1.876 0.016 1 21 . 3 PRO HB3 H 2.251 0.007 1 22 . 3 PRO CG C 27.26 0.21 1 23 . 3 PRO HG2 H 1.981 0.010 1 24 . 3 PRO CD C 49.83 0.06 1 25 . 3 PRO HD2 H 3.606 0.005 1 26 . 4 LEU H H 8.309 0.003 1 27 . 4 LEU N N 121.79 0.03 1 28 . 4 LEU CA C 55.34 0.04 1 29 . 4 LEU HA H 4.262 0.027 1 30 . 4 LEU C C 177.21 0.04 1 31 . 4 LEU CB C 42.12 0.15 1 32 . 4 LEU HB2 H 1.444 0.010 1 33 . 4 LEU HB3 H 1.602 0.013 1 34 . 4 LEU CG C 27.15 0.00 1 35 . 4 LEU CD1 C 24.31 0.00 1 36 . 4 LEU HD1 H 0.865 0.019 1 37 . 4 LEU HG H 1.588 0.020 1 38 . 5 GLN H H 8.199 0.003 1 39 . 5 GLN N N 120.63 0.09 1 40 . 5 GLN CA C 55.68 0.16 1 41 . 5 GLN HA H 4.269 0.007 1 42 . 5 GLN C C 175.58 0.02 1 43 . 5 GLN CB C 29.63 0.08 1 44 . 5 GLN HB2 H 1.894 0.007 1 45 . 5 GLN HB3 H 1.962 0.005 1 46 . 5 GLN CG C 33.85 0.00 1 47 . 5 GLN HG2 H 2.217 0.005 1 48 . 6 TYR H H 8.126 0.011 1 49 . 6 TYR N N 121.16 0.02 1 50 . 6 TYR CA C 58.08 0.07 1 51 . 6 TYR HA H 4.489 0.007 1 52 . 6 TYR C C 175.72 0.00 1 53 . 6 TYR CB C 38.78 0.10 1 54 . 6 TYR HB2 H 2.939 0.000 1 55 . 6 TYR HB3 H 3.016 0.007 1 56 . 6 TYR HD1 H 7.061 0.032 1 57 . 6 TYR HE1 H 6.794 0.022 1 58 . 7 LYS H H 8.071 0.008 1 59 . 7 LYS N N 122.27 0.10 1 60 . 7 LYS CA C 56.54 0.12 1 61 . 7 LYS HA H 4.186 0.011 1 62 . 7 LYS C C 175.67 0.02 1 63 . 7 LYS CB C 33.11 0.06 1 64 . 7 LYS HB2 H 1.708 0.005 1 65 . 7 LYS HB3 H 1.713 0.013 1 66 . 7 LYS CG C 24.58 0.04 1 67 . 7 LYS HG2 H 1.307 0.006 1 68 . 7 LYS CD C 28.95 0.00 1 69 . 7 LYS HD2 H 1.629 0.005 1 70 . 7 LYS CE C 41.84 0.02 1 71 . 7 LYS HE2 H 2.943 0.005 1 72 . 8 ASP H H 8.185 0.005 1 73 . 8 ASP N N 120.97 0.04 1 74 . 8 ASP CA C 54.32 0.06 1 75 . 8 ASP HA H 4.526 0.008 1 76 . 8 ASP C C 175.88 0.05 1 77 . 8 ASP CB C 41.20 0.12 1 78 . 8 ASP HB2 H 2.562 0.008 1 79 . 8 ASP HB3 H 2.706 0.011 1 80 . 9 LEU H H 8.006 0.004 1 81 . 9 LEU N N 122.61 0.06 1 82 . 9 LEU CA C 55.25 0.05 1 83 . 9 LEU HA H 4.263 0.008 1 84 . 9 LEU C C 177.03 0.03 1 85 . 9 LEU CB C 42.39 0.08 1 86 . 9 LEU HB2 H 1.580 0.009 1 87 . 9 LEU CG C 27.10 0.05 1 88 . 9 LEU CD1 C 24.04 0.00 1 89 . 9 LEU HD1 H 0.824 0.006 1 90 . 9 LEU CD2 C 24.83 0.00 1 91 . 9 LEU HD2 H 0.857 0.012 1 92 . 9 LEU HG H 1.583 0.005 1 93 . 10 LYS H H 8.290 0.013 1 94 . 10 LYS N N 122.19 0.13 1 95 . 10 LYS CA C 56.07 0.10 1 96 . 10 LYS HA H 4.294 0.014 1 97 . 10 LYS C C 176.09 0.09 1 98 . 10 LYS CB C 32.51 0.14 1 99 . 10 LYS HB2 H 1.764 0.008 1 100 . 10 LYS CG C 24.73 0.09 1 101 . 10 LYS HG2 H 1.377 0.013 1 102 . 10 LYS HG3 H 1.380 0.003 1 103 . 10 LYS CD C 29.09 0.24 1 104 . 10 LYS HD2 H 1.644 0.009 1 105 . 10 LYS CE C 41.80 0.18 1 106 . 10 LYS HE2 H 2.956 0.009 1 107 . 11 ILE H H 7.982 0.008 1 108 . 11 ILE N N 121.57 0.07 1 109 . 11 ILE CA C 60.90 0.09 1 110 . 11 ILE HA H 4.148 0.006 1 111 . 11 ILE C C 175.56 0.04 1 112 . 11 ILE CB C 39.12 0.20 1 113 . 11 ILE HB H 1.800 0.006 1 114 . 11 ILE CG2 C 17.52 0.06 1 115 . 11 ILE HG2 H 0.843 0.006 1 116 . 11 ILE CG1 C 27.21 0.15 1 117 . 11 ILE HG12 H 1.124 0.019 1 118 . 11 ILE HG13 H 1.394 0.005 1 119 . 11 ILE CD1 C 12.96 0.21 1 120 . 11 ILE HD1 H 0.803 0.003 1 121 . 12 ASP H H 8.384 0.006 1 122 . 12 ASP N N 124.84 0.08 1 123 . 12 ASP CA C 54.06 0.06 1 124 . 12 ASP HA H 4.616 0.008 1 125 . 12 ASP C C 175.70 0.09 1 126 . 12 ASP CB C 41.41 0.07 1 127 . 12 ASP HB2 H 2.519 0.013 1 128 . 12 ASP HB3 H 2.665 0.007 1 129 . 13 ILE H H 7.987 0.014 1 130 . 13 ILE N N 121.43 0.07 1 131 . 13 ILE CA C 61.08 0.04 1 132 . 13 ILE HA H 4.140 0.009 1 133 . 13 ILE C C 176.02 0.03 1 134 . 14 LYS H H 8.400 0.002 1 135 . 14 LYS N N 125.53 0.04 1 136 . 14 LYS CA C 56.09 0.05 1 137 . 14 LYS HA H 4.411 0.013 1 138 . 14 LYS C C 176.53 0.02 1 139 . 14 LYS CB C 32.83 0.11 1 140 . 14 LYS HB2 H 1.805 0.018 1 141 . 14 LYS HB3 H 1.590 0.298 1 142 . 14 LYS CG C 24.76 0.08 1 143 . 14 LYS HG2 H 1.445 0.145 1 144 . 14 LYS HG3 H 1.434 0.000 1 145 . 14 LYS CD C 28.87 0.04 1 146 . 14 LYS HD2 H 1.664 0.013 1 147 . 14 LYS CE C 42.13 0.00 1 148 . 14 LYS HE2 H 2.984 0.002 1 149 . 15 THR H H 8.053 0.006 1 150 . 15 THR N N 114.64 0.07 1 151 . 15 THR CA C 61.18 0.08 1 152 . 15 THR HA H 4.651 0.016 1 153 . 15 THR C C 174.32 0.02 1 154 . 15 THR CB C 70.47 0.07 1 155 . 15 THR HB H 4.164 0.008 1 156 . 15 THR CG2 C 22.02 0.06 1 157 . 15 THR HG2 H 1.141 0.007 1 158 . 16 SER H H 8.487 0.009 1 159 . 16 SER N N 117.57 0.07 1 160 . 16 SER CA C 56.42 0.08 1 161 . 16 SER HA H 4.964 0.009 1 162 . 16 SER C C 171.40 0.00 1 163 . 16 SER CB C 64.33 0.05 1 164 . 16 SER HB2 H 3.925 0.011 1 165 . 17 PRO N N 115.07 0.02 1 166 . 17 PRO CA C 61.54 0.08 1 167 . 17 PRO HA H 4.810 0.009 1 168 . 17 PRO C C 174.04 0.00 1 169 . 17 PRO CB C 30.68 0.14 1 170 . 17 PRO HB2 H 1.793 0.015 1 171 . 17 PRO HB3 H 2.319 0.010 1 172 . 17 PRO CG C 26.87 0.09 1 173 . 17 PRO HG2 H 1.826 0.012 1 174 . 17 PRO CD C 50.17 0.20 1 175 . 17 PRO HD2 H 3.556 0.025 1 176 . 17 PRO HD3 H 3.925 0.046 1 177 . 18 PRO N N 112.16 0.00 1 178 . 18 PRO CA C 60.53 0.03 1 179 . 18 PRO HA H 3.499 0.013 1 180 . 18 PRO CB C 30.01 0.07 1 181 . 18 PRO HB2 H 1.356 0.009 1 182 . 18 PRO HB3 H 1.567 0.067 1 183 . 18 PRO HG2 H 1.838 0.001 1 184 . 18 PRO CD C 49.25 0.07 1 185 . 18 PRO HD2 H 1.856 0.020 1 186 . 18 PRO HD3 H 2.550 0.009 1 187 . 19 PRO CA C 62.26 0.15 1 188 . 19 PRO HA H 4.343 0.035 1 189 . 19 PRO C C 177.55 0.01 1 190 . 19 PRO CB C 32.64 0.08 1 191 . 19 PRO HB2 H 1.987 0.008 1 192 . 19 PRO HB3 H 2.415 0.004 1 193 . 19 PRO CG C 26.51 0.10 1 194 . 19 PRO HG2 H 1.976 0.010 1 195 . 19 PRO HG3 H 2.003 0.011 1 196 . 19 PRO CD C 49.25 0.00 1 197 . 19 PRO HD2 H 3.349 0.001 1 198 . 20 GLU H H 8.927 0.016 1 199 . 20 GLU N N 125.52 0.05 1 200 . 20 GLU CA C 60.23 0.07 1 201 . 20 GLU HA H 3.926 0.008 1 202 . 20 GLU C C 177.88 0.00 1 203 . 20 GLU CB C 29.42 0.15 1 204 . 20 GLU HB2 H 2.055 0.010 1 205 . 20 GLU HB3 H 2.321 0.008 1 206 . 20 GLU CG C 36.09 0.00 1 207 . 20 GLU HG2 H 2.302 0.023 1 208 . 21 CYS H H 8.555 0.008 1 209 . 21 CYS N N 112.82 0.16 1 210 . 21 CYS CA C 59.91 0.12 1 211 . 21 CYS HA H 4.523 0.010 1 212 . 21 CYS C C 177.41 0.01 1 213 . 21 CYS CB C 26.86 0.13 1 214 . 21 CYS HB2 H 2.894 0.009 1 215 . 21 CYS HB3 H 3.136 0.010 1 216 . 22 ILE H H 7.173 0.008 1 217 . 22 ILE N N 123.16 0.04 1 218 . 22 ILE CA C 61.20 0.08 1 219 . 22 ILE HA H 3.889 0.013 1 220 . 22 ILE C C 176.47 0.03 1 221 . 22 ILE CB C 35.44 0.09 1 222 . 22 ILE HB H 1.843 0.010 1 223 . 22 ILE CG2 C 17.59 0.02 1 224 . 22 ILE HG2 H 0.853 0.007 1 225 . 22 ILE CG1 C 27.16 0.05 1 226 . 22 ILE HG12 H 1.137 0.015 1 227 . 22 ILE HG13 H 1.355 0.014 1 228 . 22 ILE CD1 C 9.67 0.11 1 229 . 22 ILE HD1 H 0.712 0.010 1 230 . 23 ASN H H 7.915 0.012 1 231 . 23 ASN N N 120.67 0.04 1 232 . 23 ASN CA C 57.14 0.07 1 233 . 23 ASN HA H 4.307 0.010 1 234 . 23 ASN C C 177.86 0.04 1 235 . 23 ASN CB C 38.60 0.11 1 236 . 23 ASN HB2 H 2.535 0.008 1 237 . 23 ASN HB3 H 2.895 0.007 1 238 . 23 ASN ND2 N 112.90 0.02 1 239 . 23 ASN HD22 H 6.713 0.022 1 240 . 23 ASN HD21 H 7.696 0.008 1 241 . 24 ASP H H 8.270 0.008 1 242 . 24 ASP N N 117.50 0.04 1 243 . 24 ASP CA C 57.34 0.16 1 244 . 24 ASP HA H 4.277 0.010 1 245 . 24 ASP C C 178.40 0.01 1 246 . 24 ASP CB C 40.45 0.09 1 247 . 24 ASP HB2 H 2.741 0.010 1 248 . 25 LEU H H 7.152 0.006 1 249 . 25 LEU N N 122.99 0.03 1 250 . 25 LEU CA C 58.98 0.17 1 251 . 25 LEU HA H 3.456 0.008 1 252 . 25 LEU C C 178.05 0.04 1 253 . 25 LEU CB C 42.04 0.17 1 254 . 25 LEU HB2 H 1.892 0.033 1 255 . 25 LEU HB3 H 1.911 0.021 1 256 . 25 LEU CG C 27.11 0.32 1 257 . 25 LEU CD1 C 26.24 0.13 1 258 . 25 LEU HD1 H 0.687 0.041 1 259 . 25 LEU CD2 C 26.78 0.13 1 260 . 25 LEU HD2 H 0.712 0.008 1 261 . 25 LEU HG H 1.175 0.010 1 262 . 26 LEU H H 8.356 0.008 1 263 . 26 LEU N N 118.30 0.11 1 264 . 26 LEU CA C 56.97 0.12 1 265 . 26 LEU HA H 4.087 0.013 1 266 . 26 LEU C C 178.36 0.05 1 267 . 26 LEU CB C 42.15 0.13 1 268 . 26 LEU HB2 H 1.451 0.018 1 269 . 26 LEU HB3 H 1.951 0.010 1 270 . 26 LEU CG C 27.27 0.12 1 271 . 26 LEU CD1 C 24.05 0.13 1 272 . 26 LEU HD1 H 0.949 0.014 1 273 . 26 LEU CD2 C 26.57 0.14 1 274 . 26 LEU HD2 H 0.950 0.014 1 275 . 26 LEU HG H 1.750 0.011 1 276 . 27 GLN H H 7.400 0.008 1 277 . 27 GLN N N 113.99 0.07 1 278 . 27 GLN CA C 56.91 0.11 1 279 . 27 GLN HA H 4.101 0.011 1 280 . 27 GLN C C 176.52 0.02 1 281 . 27 GLN CB C 28.73 0.07 1 282 . 27 GLN HB2 H 2.032 0.014 1 283 . 27 GLN HB3 H 2.182 0.010 1 284 . 27 GLN CG C 33.94 0.10 1 285 . 27 GLN HG2 H 2.471 0.015 1 286 . 27 GLN HG3 H 2.513 0.009 1 287 . 27 GLN NE2 N 112.14 0.02 1 288 . 27 GLN HE22 H 6.877 0.006 1 289 . 27 GLN HE21 H 7.158 0.001 1 290 . 28 ALA H H 7.423 0.004 1 291 . 28 ALA N N 120.48 0.06 1 292 . 28 ALA CA C 53.19 0.16 1 293 . 28 ALA HA H 4.391 0.012 1 294 . 28 ALA C C 177.57 0.03 1 295 . 28 ALA CB C 22.12 0.12 1 296 . 28 ALA HB H 1.476 0.008 1 297 . 29 VAL H H 8.122 0.008 1 298 . 29 VAL N N 118.60 0.07 1 299 . 29 VAL CA C 61.18 0.10 1 300 . 29 VAL HA H 4.096 0.017 1 301 . 29 VAL C C 173.69 0.03 1 302 . 29 VAL CB C 33.54 0.05 1 303 . 29 VAL HB H 1.892 0.010 1 304 . 29 VAL CG1 C 21.08 0.17 1 305 . 29 VAL HG1 H 0.668 0.011 1 306 . 29 VAL CG2 C 21.70 0.10 1 307 . 29 VAL HG2 H 0.681 0.007 1 308 . 30 ASP H H 8.579 0.009 1 309 . 30 ASP N N 125.63 0.04 1 310 . 30 ASP CA C 52.92 0.09 1 311 . 30 ASP HA H 4.633 0.008 1 312 . 30 ASP C C 175.37 0.01 1 313 . 30 ASP CB C 40.31 0.09 1 314 . 30 ASP HB2 H 2.518 0.007 1 315 . 30 ASP HB3 H 2.761 0.019 1 316 . 31 SER H H 7.385 0.010 1 317 . 31 SER N N 116.01 0.06 1 318 . 31 SER CA C 56.05 0.28 1 319 . 31 SER HA H 4.711 0.015 1 320 . 31 SER C C 175.30 0.00 1 321 . 31 SER CB C 64.05 0.09 1 322 . 31 SER HB2 H 3.444 0.079 1 323 . 31 SER HB3 H 3.862 0.015 1 324 . 31 SER HG H 7.382 0.000 1 325 . 32 GLN H H 9.351 0.008 1 326 . 32 GLN N N 131.41 0.13 1 327 . 32 GLN CA C 58.34 0.12 1 328 . 32 GLN HA H 3.819 0.008 1 329 . 32 GLN C C 177.25 0.04 1 330 . 32 GLN CB C 28.29 0.17 1 331 . 32 GLN HB2 H 1.997 0.023 1 332 . 32 GLN HB3 H 2.211 0.008 1 333 . 32 GLN CG C 33.13 0.11 1 334 . 32 GLN HG2 H 2.431 0.011 1 335 . 32 GLN NE2 N 116.91 0.01 1 336 . 32 GLN HE22 H 7.070 0.009 1 337 . 32 GLN HE21 H 8.047 0.011 1 338 . 33 GLU H H 8.789 0.011 1 339 . 33 GLU N N 118.23 0.06 1 340 . 33 GLU CA C 60.09 0.12 1 341 . 33 GLU HA H 4.162 0.010 1 342 . 33 GLU C C 180.19 0.02 1 343 . 33 GLU CB C 29.45 0.27 1 344 . 33 GLU HB2 H 1.955 0.015 1 345 . 33 GLU CG C 37.07 0.16 1 346 . 33 GLU HG2 H 2.405 0.027 1 347 . 33 GLU HG3 H 2.421 0.003 1 348 . 34 VAL H H 7.622 0.016 1 349 . 34 VAL N N 119.92 0.03 1 350 . 34 VAL CA C 66.50 0.07 1 351 . 34 VAL HA H 3.629 0.011 1 352 . 34 VAL C C 178.00 0.04 1 353 . 34 VAL CB C 31.90 0.27 1 354 . 34 VAL HB H 2.196 0.013 1 355 . 34 VAL CG1 C 21.88 0.10 1 356 . 34 VAL HG1 H 0.929 0.004 1 357 . 34 VAL CG2 C 23.32 0.74 1 358 . 34 VAL HG2 H 0.928 0.020 1 359 . 35 ARG H H 7.909 0.008 1 360 . 35 ARG N N 121.71 0.06 1 361 . 35 ARG CA C 61.77 0.17 1 362 . 35 ARG HA H 3.872 0.010 1 363 . 35 ARG C C 178.58 0.03 1 364 . 35 ARG CB C 29.81 0.10 1 365 . 35 ARG HB2 H 1.913 0.023 1 366 . 35 ARG HB3 H 1.911 0.007 1 367 . 35 ARG CG C 21.84 0.07 1 368 . 35 ARG HG2 H 0.918 0.013 1 369 . 35 ARG CD C 43.49 0.07 1 370 . 35 ARG HD2 H 3.141 0.000 1 371 . 35 ARG HD3 H 3.332 0.008 1 372 . 35 ARG NE N 83.03 0.07 1 373 . 35 ARG HE H 7.332 0.007 1 374 . 36 ASP H H 8.995 0.007 1 375 . 36 ASP N N 120.04 0.04 1 376 . 36 ASP CA C 57.58 0.07 1 377 . 36 ASP HA H 4.362 0.014 1 378 . 36 ASP C C 178.49 0.03 1 379 . 36 ASP CB C 40.57 0.12 1 380 . 36 ASP HB2 H 2.640 0.012 1 381 . 36 ASP HB3 H 2.780 0.018 1 382 . 37 TYR H H 7.709 0.013 1 383 . 37 TYR N N 121.47 0.03 1 384 . 37 TYR CA C 61.77 0.09 1 385 . 37 TYR HA H 4.016 0.014 1 386 . 37 TYR C C 177.35 0.05 1 387 . 37 TYR CB C 38.25 0.09 1 388 . 37 TYR HB2 H 3.061 0.025 1 389 . 37 TYR HB3 H 3.319 0.020 1 390 . 37 TYR CD1 C 133.73 0.00 1 391 . 37 TYR HD1 H 7.106 0.015 1 392 . 37 TYR CE1 C 117.57 0.06 1 393 . 37 TYR HE1 H 6.750 0.015 1 394 . 38 CYS H H 8.245 0.020 1 395 . 38 CYS N N 116.34 0.06 1 396 . 38 CYS CA C 64.02 0.13 1 397 . 38 CYS HA H 4.060 0.018 1 398 . 38 CYS C C 176.71 0.03 1 399 . 38 CYS CB C 27.00 0.09 1 400 . 38 CYS HB2 H 2.901 0.012 1 401 . 38 CYS HB3 H 3.450 0.021 1 402 . 39 GLU H H 8.488 0.008 1 403 . 39 GLU N N 121.03 0.05 1 404 . 39 GLU CA C 59.69 0.16 1 405 . 39 GLU HA H 4.124 0.010 1 406 . 39 GLU C C 180.67 0.03 1 407 . 39 GLU CB C 29.49 0.13 1 408 . 39 GLU HB2 H 2.130 0.013 1 409 . 39 GLU CG C 36.64 0.09 1 410 . 39 GLU HG2 H 2.394 0.011 1 411 . 39 GLU HG3 H 2.402 0.009 1 412 . 40 LYS H H 7.796 0.008 1 413 . 40 LYS N N 121.18 0.05 1 414 . 40 LYS CA C 58.91 0.20 1 415 . 40 LYS HA H 3.895 0.010 1 416 . 40 LYS C C 178.40 0.03 1 417 . 40 LYS CB C 31.94 0.13 1 418 . 40 LYS HB2 H 1.732 0.017 1 419 . 40 LYS CG C 25.49 0.06 1 420 . 40 LYS HG2 H 1.343 0.011 1 421 . 40 LYS HG3 H 1.476 0.008 1 422 . 40 LYS CD C 28.95 0.07 1 423 . 40 LYS HD2 H 1.550 0.011 1 424 . 40 LYS HD3 H 1.548 0.000 1 425 . 40 LYS CE C 41.86 0.07 1 426 . 40 LYS HE2 H 2.869 0.009 1 427 . 41 LYS H H 6.949 0.006 1 428 . 41 LYS N N 116.84 0.09 1 429 . 41 LYS CA C 54.59 0.07 1 430 . 41 LYS HA H 3.588 0.010 1 431 . 41 LYS C C 175.98 0.02 1 432 . 41 LYS CB C 30.52 0.09 1 433 . 41 LYS HB2 H 0.047 0.020 1 434 . 41 LYS HB3 H 0.531 0.017 1 435 . 41 LYS CG C 23.07 0.09 1 436 . 41 LYS HG2 H 0.070 0.010 1 437 . 41 LYS HG3 H 0.373 0.020 1 438 . 41 LYS CD C 26.93 0.12 1 439 . 41 LYS HD2 H 0.917 0.016 1 440 . 41 LYS HD3 H 0.935 0.006 1 441 . 41 LYS CE C 41.59 0.09 1 442 . 41 LYS HE2 H 2.419 0.009 1 443 . 41 LYS HE3 H 2.541 0.015 1 444 . 42 GLY H H 7.520 0.008 1 445 . 42 GLY N N 111.98 12.00 1 446 . 42 GLY CA C 45.29 0.11 1 447 . 42 GLY HA2 H 3.952 0.011 1 448 . 42 GLY C C 174.24 0.02 1 449 . 42 GLY HA3 H 3.630 0.036 1 450 . 43 TRP H H 7.658 0.008 1 451 . 43 TRP N N 120.04 0.03 1 452 . 43 TRP CA C 54.08 0.05 1 453 . 43 TRP HA H 5.517 0.017 1 454 . 43 TRP C C 175.62 0.00 1 455 . 43 TRP CB C 30.02 0.16 1 456 . 43 TRP HB2 H 2.798 0.015 1 457 . 43 TRP HB3 H 3.110 0.001 1 458 . 43 TRP HD1 H 6.957 0.011 1 459 . 43 TRP NE1 N 129.08 0.01 1 460 . 43 TRP HE1 H 10.043 0.002 1 461 . 43 TRP HE3 H 7.404 0.005 1 462 . 43 TRP HZ2 H 7.509 0.013 1 463 . 43 TRP HZ3 H 7.490 0.018 1 464 . 43 TRP HH2 H 7.202 0.011 1 465 . 44 ILE H H 8.000 0.011 1 466 . 44 ILE N N 120.51 0.04 1 467 . 44 ILE CA C 60.47 0.10 1 468 . 44 ILE HA H 4.127 0.010 1 469 . 44 ILE C C 175.30 0.03 1 470 . 44 ILE CB C 39.55 0.09 1 471 . 44 ILE HB H 1.654 0.009 1 472 . 44 ILE CG2 C 17.46 0.08 1 473 . 44 ILE HG2 H 0.824 0.012 1 474 . 44 ILE CG1 C 27.39 0.05 1 475 . 44 ILE HG12 H 1.034 0.006 1 476 . 44 ILE HG13 H 1.391 0.013 1 477 . 44 ILE CD1 C 13.03 0.03 1 478 . 44 ILE HD1 H 0.813 0.020 1 479 . 45 VAL H H 8.322 0.009 1 480 . 45 VAL N N 124.36 0.05 1 481 . 45 VAL CA C 61.55 0.13 1 482 . 45 VAL HA H 4.141 0.016 1 483 . 45 VAL C C 175.13 0.05 1 484 . 45 VAL CB C 33.13 0.07 1 485 . 45 VAL HB H 2.071 0.008 1 486 . 45 VAL CG1 C 21.28 0.00 1 487 . 45 VAL HG1 H 0.898 0.006 1 488 . 45 VAL CG2 C 20.73 0.03 1 489 . 45 VAL HG2 H 0.913 0.018 1 490 . 46 ASN H H 8.629 0.011 1 491 . 46 ASN N N 123.94 0.06 1 492 . 46 ASN CA C 52.82 0.06 1 493 . 46 ASN HA H 4.774 0.009 1 494 . 46 ASN C C 174.76 0.02 1 495 . 46 ASN CB C 39.18 0.15 1 496 . 46 ASN HB2 H 2.640 0.009 1 497 . 46 ASN HB3 H 2.769 0.013 1 498 . 46 ASN ND2 N 112.49 0.04 1 499 . 46 ASN HD22 H 6.781 0.007 1 500 . 46 ASN HD21 H 7.582 0.002 1 501 . 47 ILE H H 8.264 0.009 1 502 . 47 ILE N N 122.35 0.06 1 503 . 47 ILE CA C 61.01 0.08 1 504 . 47 ILE HA H 4.247 0.007 1 505 . 47 ILE C C 176.42 0.02 1 506 . 47 ILE CB C 38.61 0.05 1 507 . 47 ILE HB H 1.870 0.013 1 508 . 47 ILE CG2 C 17.68 0.07 1 509 . 47 ILE HG2 H 0.861 0.006 1 510 . 47 ILE CG1 C 27.38 0.42 1 511 . 47 ILE HG12 H 1.160 0.009 1 512 . 47 ILE HG13 H 1.400 0.005 1 513 . 47 ILE CD1 C 13.00 0.00 1 514 . 47 ILE HD1 H 0.812 0.017 1 515 . 48 THR H H 8.285 0.003 1 516 . 48 THR N N 118.34 0.05 1 517 . 48 THR CA C 61.99 0.17 1 518 . 48 THR HA H 4.322 0.007 1 519 . 48 THR C C 174.58 0.01 1 520 . 48 THR CB C 69.64 0.24 1 521 . 48 THR HB H 4.208 0.012 1 522 . 48 THR CG2 C 21.81 0.19 1 523 . 48 THR HG2 H 1.167 0.005 1 524 . 49 SER H H 8.244 0.008 1 525 . 49 SER N N 117.92 0.07 1 526 . 49 SER CA C 58.44 0.10 1 527 . 49 SER HA H 4.419 0.006 1 528 . 49 SER C C 174.51 0.02 1 529 . 49 SER CB C 63.78 0.11 1 530 . 49 SER HB2 H 3.835 0.015 1 531 . 49 SER HB3 H 3.856 0.001 1 532 . 50 GLN H H 8.373 0.007 1 533 . 50 GLN N N 122.41 0.09 1 534 . 50 GLN CA C 56.02 0.04 1 535 . 50 GLN HA H 4.334 0.006 1 536 . 50 GLN C C 176.03 0.01 1 537 . 50 GLN CB C 29.45 0.02 1 538 . 50 GLN HB2 H 2.069 0.007 1 539 . 50 GLN HB3 H 2.084 0.000 1 540 . 50 GLN CG C 33.73 0.02 1 541 . 50 GLN HG2 H 2.331 0.002 1 542 . 50 GLN NE2 N 112.32 0.01 1 543 . 50 GLN HE22 H 6.826 0.000 1 544 . 50 GLN HE21 H 7.498 0.000 1 545 . 51 VAL H H 8.090 0.003 1 546 . 51 VAL N N 121.11 0.02 1 547 . 51 VAL CA C 62.67 0.07 1 548 . 51 VAL HA H 4.045 0.011 1 549 . 51 VAL C C 176.25 0.03 1 550 . 51 VAL CB C 32.61 0.04 1 551 . 51 VAL HB H 2.027 0.007 1 552 . 51 VAL HG1 H 0.908 0.010 1 553 . 51 VAL CG2 C 20.92 0.01 1 554 . 51 VAL HG2 H 0.908 0.000 1 555 . 51 VAL CG1 C 20.95 0.19 1 556 . 52 GLN H H 8.459 0.006 1 557 . 52 GLN N N 124.14 0.07 1 558 . 52 GLN CA C 55.98 0.04 1 559 . 52 GLN HA H 4.373 0.011 1 560 . 52 GLN C C 176.20 0.02 1 561 . 52 GLN CB C 29.45 0.05 1 562 . 52 GLN HB2 H 1.965 0.015 1 563 . 52 GLN HB3 H 2.096 0.006 1 564 . 52 GLN CG C 33.79 0.12 1 565 . 52 GLN HG2 H 2.333 0.011 1 566 . 52 GLN NE2 N 112.33 0.04 1 567 . 52 GLN HE22 H 6.826 0.000 1 568 . 52 GLN HE21 H 7.498 0.000 1 569 . 53 THR H H 8.153 0.003 1 570 . 53 THR N N 115.69 0.10 1 571 . 53 THR CA C 62.26 0.07 1 572 . 53 THR HA H 4.256 0.006 1 573 . 53 THR C C 174.67 0.01 1 574 . 53 THR CB C 69.76 0.07 1 575 . 53 THR HB H 4.192 0.011 1 576 . 53 THR CG2 C 21.62 0.03 1 577 . 53 THR HG2 H 1.175 0.015 1 578 . 54 GLU H H 8.411 0.004 1 579 . 54 GLU N N 123.09 0.08 1 580 . 54 GLU CA C 56.84 0.05 1 581 . 54 GLU HA H 4.247 0.009 1 582 . 54 GLU C C 176.44 0.02 1 583 . 54 GLU CB C 30.11 0.12 1 584 . 54 GLU HB2 H 1.942 0.033 1 585 . 54 GLU HB3 H 2.021 0.009 1 586 . 54 GLU CG C 36.38 0.08 1 587 . 54 GLU HG2 H 2.238 0.006 1 588 . 55 ARG H H 8.277 0.002 1 589 . 55 ARG N N 121.56 0.08 1 590 . 55 ARG CA C 56.23 0.07 1 591 . 55 ARG HA H 4.275 0.003 1 592 . 55 ARG C C 175.99 0.00 1 593 . 55 ARG CB C 30.74 0.08 1 594 . 55 ARG HB2 H 1.729 0.008 1 595 . 55 ARG HB3 H 1.803 0.010 1 596 . 55 ARG CG C 27.15 0.00 1 597 . 55 ARG HG2 H 1.593 0.010 1 598 . 55 ARG CD C 42.55 0.00 1 599 . 55 ARG HD2 H 3.158 0.004 1 600 . 56 ASN H H 8.428 0.006 1 601 . 56 ASN N N 119.77 0.04 1 602 . 56 ASN CA C 53.29 0.06 1 603 . 56 ASN HA H 4.686 0.006 1 604 . 56 ASN C C 175.16 0.02 1 605 . 56 ASN CB C 38.88 0.20 1 606 . 56 ASN HB2 H 2.728 0.017 1 607 . 56 ASN HB3 H 2.804 0.009 1 608 . 57 ILE H H 8.010 0.007 1 609 . 57 ILE N N 120.55 0.03 1 610 . 57 ILE CA C 61.31 0.16 1 611 . 57 ILE HA H 4.132 0.005 1 612 . 57 ILE C C 175.80 0.02 1 613 . 57 ILE CB C 38.81 0.06 1 614 . 57 ILE HB H 1.849 0.007 1 615 . 57 ILE CG2 C 17.62 0.03 1 616 . 57 ILE HG2 H 0.849 0.008 1 617 . 57 ILE CG1 C 27.15 0.01 1 618 . 57 ILE HG12 H 1.128 0.008 1 619 . 57 ILE HG13 H 1.396 0.002 1 620 . 57 ILE CD1 C 13.04 0.07 1 621 . 57 ILE HD1 H 0.806 0.005 1 622 . 58 ASN H H 8.440 0.004 1 623 . 58 ASN N N 122.15 0.05 1 624 . 58 ASN CA C 53.31 0.04 1 625 . 58 ASN HA H 4.689 0.006 1 626 . 58 ASN C C 174.73 0.02 1 627 . 58 ASN CB C 38.95 0.00 1 628 . 58 ASN HB2 H 2.722 0.000 1 629 . 58 ASN HB3 H 2.807 0.000 1 630 . 59 ARG H H 8.180 0.004 1 631 . 59 ARG N N 122.25 0.02 1 632 . 59 ARG CA C 55.92 0.07 1 633 . 59 ARG HA H 4.312 0.013 1 634 . 59 ARG C C 174.79 0.03 1 635 . 59 ARG CB C 30.85 0.09 1 636 . 59 ARG HB2 H 1.710 0.006 1 637 . 59 ARG HB3 H 1.852 0.008 1 638 . 59 ARG CG C 27.00 0.16 1 639 . 59 ARG HG2 H 1.609 0.009 1 640 . 59 ARG CD C 43.19 0.08 1 641 . 59 ARG HD2 H 3.158 0.008 1 642 . 60 ALA H H 7.954 0.003 1 643 . 60 ALA N N 131.24 0.19 1 644 . 60 ALA CA C 51.44 13.49 1 645 . 60 ALA HA H 4.091 0.004 1 646 . 60 ALA C C 182.45 0.00 1 647 . 60 ALA CB C 20.22 0.08 1 648 . 60 ALA HB H 1.300 0.008 1 stop_ save_