data_4974 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Rapid Protein fold Determination using Secondary Chemical Shifts and Cross- hydrogen bond 15N-13C' Scalar Couplings (3hbJNC') ; _BMRB_accession_number 4974 _BMRB_flat_file_name bmr4974.str _Entry_type original _Submission_date 2001-03-19 _Accession_date 2001-03-19 _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 Bonvin Alexandre M.J.J. . 2 Houben Klaartje . . 3 Guenneugues Marc . . 4 Kaptein Robert . . 5 Boelens Rolf . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 389 "13C chemical shifts" 269 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-10-17 original author . stop_ _Original_release_date 2001-10-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Rapid Protein fold Determination using Secondary Chemical Shifts and Cross- hydrogen bond 15N-13C' Scalar Couplings (3hbJNC') ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21631514 _PubMed_ID 11775739 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bonvin Alexandre M.J.J. . 2 Houben Klaartje . . 3 Guenneugues Marc . . 4 Kaptein Robert . . 5 Boelens Rolf . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 221 _Page_last 233 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_CI2 _Saveframe_category molecular_system _Mol_system_name 'Chymotrypsin Inhibitor 2' _Abbreviation_common CI2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Chymotrypsin Inhibitor II' $ci2_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ci2_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Chymotrypsin Inhibitor 2' _Abbreviation_common ci2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; LKTEWPELVGKSVEEAKKVI LQDKPEAQIIVLPVGTIVTM EYRIDRVRLFVDKLDNIAQV VRVG ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 LYS 3 THR 4 GLU 5 TRP 6 PRO 7 GLU 8 LEU 9 VAL 10 GLY 11 LYS 12 SER 13 VAL 14 GLU 15 GLU 16 ALA 17 LYS 18 LYS 19 VAL 20 ILE 21 LEU 22 GLN 23 ASP 24 LYS 25 PRO 26 GLU 27 ALA 28 GLN 29 ILE 30 ILE 31 VAL 32 LEU 33 PRO 34 VAL 35 GLY 36 THR 37 ILE 38 VAL 39 THR 40 MET 41 GLU 42 TYR 43 ARG 44 ILE 45 ASP 46 ARG 47 VAL 48 ARG 49 LEU 50 PHE 51 VAL 52 ASP 53 LYS 54 LEU 55 ASP 56 ASN 57 ILE 58 ALA 59 GLN 60 VAL 61 VAL 62 ARG 63 VAL 64 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1869 BSPI-2 100.00 83 98.44 98.44 1.32e-34 BMRB 1870 BSPI-2 100.00 65 98.44 98.44 1.22e-34 BMRB 1871 BSPI-2 100.00 83 98.44 98.44 1.32e-34 BMRB 1872 BSPI-2 100.00 65 98.44 98.44 1.22e-34 PDB 1CIQ "Complex Of Two Fragments Of Ci2, Residues 1-40 And 41-64" 62.50 40 97.50 100.00 4.30e-17 PDB 1CIR "Complex Of Two Fragments Of Ci2 [(1-40)(Dot)(41-64)]" 60.94 40 97.44 100.00 3.50e-16 PDB 1CQ4 "Ci2 Mutant With Tetraglutamine (mgqqqqgm) Replacing Met59" 62.50 47 97.50 100.00 3.33e-17 PDB 3CI2 "Refinement Of The Three-Dimensional Solution Structure Of Barley Serine Proteinase Inhibitor 2 And Comparison With The Structur" 100.00 66 98.44 98.44 1.18e-34 EMBL CAA28988 "unnamed protein product [Hordeum vulgare subsp. vulgare]" 100.00 84 98.44 98.44 9.98e-35 GB ABW71682 "chymotrypsin inhibitor-2 [Hordeum vulgare subsp. vulgare]" 100.00 84 98.44 98.44 9.98e-35 GB ABW71687 "chymotrypsin inhibitor-2 [Hordeum vulgare subsp. spontaneum]" 100.00 84 98.44 98.44 9.98e-35 GB ABW71691 "chymotrypsin inhibitor-2 [Hordeum vulgare subsp. spontaneum]" 100.00 84 98.44 98.44 9.98e-35 GB ABW71693 "chymotrypsin inhibitor-2 [Hordeum vulgare subsp. spontaneum]" 100.00 84 98.44 98.44 9.98e-35 GB ABW71694 "chymotrypsin inhibitor-2 [Hordeum vulgare subsp. spontaneum]" 100.00 84 98.44 98.44 9.98e-35 SP P01053 "RecName: Full=Subtilisin-chymotrypsin inhibitor-2A; Short=CI-2A [Hordeum vulgare]" 100.00 84 98.44 98.44 9.98e-35 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ci2_monomer Barley 4513 Eukaryota Viridiplantae Hordeum vulgare 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 $ci2_monomer 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ci2_monomer 2 mM '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.6 0.1 n/a temperature 303 1.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS 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 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Chymotrypsin Inhibitor II' _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 LEU CA C 54.963 0.10 1 2 . 1 LEU HA H 4.185 0.02 1 3 . 1 LEU CB C 33.162 0.10 1 4 . 1 LEU HB2 H 2.191 0.02 2 5 . 1 LEU CG C 30.542 0.10 1 6 . 1 LEU HG H 2.592 0.02 1 7 . 1 LEU C C 171.525 0.10 1 8 . 2 LYS N N 127.601 0.10 1 9 . 2 LYS H H 8.796 0.02 1 10 . 2 LYS CA C 56.536 0.10 1 11 . 2 LYS HA H 4.271 0.02 1 12 . 2 LYS CB C 33.909 0.10 1 13 . 2 LYS HB3 H 1.470 0.02 2 14 . 2 LYS HB2 H 1.559 0.02 2 15 . 2 LYS CG C 25.110 0.10 1 16 . 2 LYS HG3 H 0.694 0.02 2 17 . 2 LYS HG2 H 1.004 0.02 2 18 . 2 LYS CD C 29.837 0.10 1 19 . 2 LYS HD3 H 1.391 0.02 2 20 . 2 LYS HD2 H 1.490 0.02 2 21 . 2 LYS CE C 41.922 0.10 1 22 . 2 LYS HE3 H 2.382 0.02 2 23 . 2 LYS HE2 H 2.521 0.02 2 24 . 2 LYS HZ H 7.752 0.02 1 25 . 2 LYS C C 175.289 0.10 1 26 . 3 THR N N 112.746 0.10 1 27 . 3 THR H H 8.466 0.02 1 28 . 3 THR CA C 60.940 0.10 1 29 . 3 THR HA H 4.325 0.02 1 30 . 3 THR CB C 70.469 0.10 1 31 . 3 THR HB H 4.564 0.02 1 32 . 3 THR CG2 C 21.788 0.10 1 33 . 3 THR HG2 H 1.122 0.02 1 34 . 3 THR C C 173.010 0.10 1 35 . 4 GLU N N 117.087 0.10 1 36 . 4 GLU H H 6.719 0.02 1 37 . 4 GLU CA C 55.083 0.10 1 38 . 4 GLU HA H 5.352 0.02 1 39 . 4 GLU CB C 33.009 0.10 1 40 . 4 GLU HB3 H 1.812 0.02 2 41 . 4 GLU HB2 H 2.132 0.02 2 42 . 4 GLU CG C 34.539 0.10 1 43 . 4 GLU HG3 H 2.248 0.02 1 44 . 4 GLU HG2 H 2.248 0.02 1 45 . 4 GLU C C 174.794 0.10 1 46 . 5 TRP N N 119.125 0.10 1 47 . 5 TRP H H 8.283 0.02 1 48 . 5 TRP CA C 56.483 0.10 1 49 . 5 TRP HA H 5.170 0.02 1 50 . 5 TRP CB C 32.098 0.10 1 51 . 5 TRP HB3 H 2.917 0.02 2 52 . 5 TRP HB2 H 3.084 0.02 2 53 . 5 TRP HD1 H 7.126 0.02 1 54 . 5 TRP NE1 N 131.982 0.10 1 55 . 5 TRP HE1 H 11.503 0.02 2 56 . 5 TRP HZ2 H 7.176 0.02 2 57 . 5 TRP HH2 H 7.599 0.02 1 58 . 5 TRP HZ3 H 7.874 0.02 2 59 . 5 TRP HE3 H 7.317 0.02 2 60 . 5 TRP C C 174.345 0.10 1 61 . 6 PRO HA H 4.350 0.02 1 62 . 6 PRO HB2 H 2.351 0.02 2 63 . 6 PRO HG2 H 2.120 0.02 2 64 . 6 PRO HD3 H 3.279 0.02 2 65 . 6 PRO HD2 H 3.891 0.02 2 66 . 7 GLU N N 120.525 0.10 1 67 . 7 GLU H H 10.733 0.02 1 68 . 7 GLU CA C 57.790 0.10 1 69 . 7 GLU HA H 4.405 0.02 1 70 . 7 GLU CB C 27.964 0.10 1 71 . 7 GLU HB3 H 2.161 0.02 1 72 . 7 GLU HB2 H 2.161 0.02 1 73 . 7 GLU CG C 35.184 0.10 1 74 . 7 GLU HG3 H 2.560 0.02 1 75 . 7 GLU HG2 H 2.560 0.02 1 76 . 7 GLU C C 176.842 0.10 1 77 . 8 LEU N N 119.217 0.10 1 78 . 8 LEU H H 7.890 0.02 1 79 . 8 LEU CA C 54.351 0.10 1 80 . 8 LEU HA H 4.422 0.02 1 81 . 8 LEU CB C 42.508 0.10 1 82 . 8 LEU HB3 H 1.582 0.02 2 83 . 8 LEU HB2 H 1.935 0.02 2 84 . 8 LEU CG C 27.375 0.10 1 85 . 8 LEU HG H 1.555 0.02 1 86 . 8 LEU CD1 C 25.851 0.10 2 87 . 8 LEU HD1 H 0.829 0.02 4 88 . 8 LEU CD2 C 22.414 0.10 2 89 . 8 LEU HD2 H 0.829 0.02 4 90 . 8 LEU C C 176.977 0.10 1 91 . 9 VAL N N 119.840 0.10 1 92 . 9 VAL H H 7.162 0.02 1 93 . 9 VAL CA C 66.329 0.10 1 94 . 9 VAL HA H 3.306 0.02 1 95 . 9 VAL CB C 30.827 0.10 1 96 . 9 VAL HB H 2.017 0.02 1 97 . 9 VAL CG2 C 21.109 0.10 2 98 . 9 VAL HG2 H 0.893 0.02 4 99 . 9 VAL CG1 C 23.796 0.10 2 100 . 9 VAL HG1 H 1.007 0.02 4 101 . 9 VAL C C 177.124 0.10 1 102 . 10 GLY N N 116.800 0.10 1 103 . 10 GLY H H 9.121 0.02 1 104 . 10 GLY CA C 45.011 0.10 1 105 . 10 GLY HA3 H 3.683 0.02 2 106 . 10 GLY HA2 H 4.398 0.02 2 107 . 10 GLY C C 173.817 0.10 1 108 . 11 LYS N N 119.375 0.10 1 109 . 11 LYS H H 7.808 0.02 1 110 . 11 LYS CA C 54.103 0.10 1 111 . 11 LYS HA H 4.581 0.02 1 112 . 11 LYS CB C 32.690 0.10 1 113 . 11 LYS HB3 H 1.924 0.02 2 114 . 11 LYS HB2 H 2.082 0.02 2 115 . 11 LYS CG C 25.798 0.10 1 116 . 11 LYS HG3 H 1.357 0.02 2 117 . 11 LYS HG2 H 1.460 0.02 2 118 . 11 LYS CD C 28.468 0.10 1 119 . 11 LYS HD3 H 1.642 0.02 1 120 . 11 LYS HD2 H 1.642 0.02 1 121 . 11 LYS CE C 42.635 0.10 1 122 . 11 LYS HE3 H 3.041 0.02 1 123 . 11 LYS HE2 H 3.041 0.02 1 124 . 11 LYS C C 175.225 0.10 1 125 . 12 SER N N 115.953 0.10 1 126 . 12 SER H H 8.563 0.02 1 127 . 12 SER CA C 58.071 0.10 1 128 . 12 SER HA H 4.977 0.02 1 129 . 12 SER CB C 65.290 0.10 1 130 . 12 SER HB3 H 4.100 0.02 2 131 . 12 SER HB2 H 4.456 0.02 2 132 . 12 SER C C 176.047 0.10 1 133 . 13 VAL N N 121.788 0.10 1 134 . 13 VAL H H 8.360 0.02 1 135 . 13 VAL CA C 66.366 0.10 1 136 . 13 VAL HA H 3.609 0.02 1 137 . 13 VAL CB C 31.737 0.10 1 138 . 13 VAL HB H 2.029 0.02 1 139 . 13 VAL CG2 C 21.122 0.10 2 140 . 13 VAL HG2 H 0.943 0.02 4 141 . 13 VAL CG1 C 24.335 0.10 2 142 . 13 VAL HG1 H 0.943 0.02 4 143 . 13 VAL C C 176.747 0.10 1 144 . 14 GLU N N 119.108 0.10 1 145 . 14 GLU H H 8.312 0.02 1 146 . 14 GLU CA C 59.715 0.10 1 147 . 14 GLU HA H 3.948 0.02 1 148 . 14 GLU CB C 28.772 0.10 1 149 . 14 GLU HB3 H 2.032 0.02 1 150 . 14 GLU HB2 H 2.032 0.02 1 151 . 14 GLU CG C 35.849 0.10 1 152 . 14 GLU HG3 H 2.376 0.02 1 153 . 14 GLU HG2 H 2.376 0.02 1 154 . 14 GLU C C 179.388 0.10 1 155 . 15 GLU N N 120.860 0.10 1 156 . 15 GLU H H 7.670 0.02 1 157 . 15 GLU CA C 58.795 0.10 1 158 . 15 GLU HA H 4.019 0.02 1 159 . 15 GLU CB C 29.506 0.10 1 160 . 15 GLU HB3 H 2.022 0.02 2 161 . 15 GLU HB2 H 2.196 0.02 2 162 . 15 GLU CG C 35.680 0.10 1 163 . 15 GLU HG3 H 2.247 0.02 2 164 . 15 GLU HG2 H 2.330 0.02 2 165 . 15 GLU C C 178.269 0.10 1 166 . 16 ALA N N 120.692 0.10 1 167 . 16 ALA H H 8.427 0.02 1 168 . 16 ALA CA C 54.616 0.10 1 169 . 16 ALA HA H 4.049 0.02 1 170 . 16 ALA CB C 19.388 0.10 1 171 . 16 ALA HB H 1.385 0.02 1 172 . 16 ALA C C 178.732 0.10 1 173 . 17 LYS N N 116.508 0.10 1 174 . 17 LYS H H 8.516 0.02 1 175 . 17 LYS CA C 60.721 0.10 1 176 . 17 LYS HA H 3.464 0.02 1 177 . 17 LYS CB C 32.713 0.10 1 178 . 17 LYS HB3 H 1.621 0.02 2 179 . 17 LYS HB2 H 1.723 0.02 2 180 . 17 LYS CG C 26.506 0.10 1 181 . 17 LYS HG3 H 1.128 0.02 1 182 . 17 LYS HG2 H 1.128 0.02 1 183 . 17 LYS CD C 29.868 0.10 1 184 . 17 LYS HD3 H 1.568 0.02 1 185 . 17 LYS HD2 H 1.568 0.02 1 186 . 17 LYS CE C 41.292 0.10 1 187 . 17 LYS HE3 H 2.655 0.02 2 188 . 17 LYS HE2 H 2.732 0.02 2 189 . 17 LYS C C 176.889 0.10 1 190 . 18 LYS N N 116.031 0.10 1 191 . 18 LYS H H 6.969 0.02 1 192 . 18 LYS CA C 59.372 0.10 1 193 . 18 LYS HA H 3.852 0.02 1 194 . 18 LYS CB C 32.435 0.10 1 195 . 18 LYS HB3 H 1.895 0.02 1 196 . 18 LYS HB2 H 1.895 0.02 1 197 . 18 LYS CG C 25.130 0.10 1 198 . 18 LYS HG3 H 1.349 0.02 2 199 . 18 LYS HG2 H 1.582 0.02 2 200 . 18 LYS CD C 29.556 0.10 1 201 . 18 LYS HD3 H 1.681 0.02 1 202 . 18 LYS HD2 H 1.681 0.02 1 203 . 18 LYS CE C 41.923 0.10 1 204 . 18 LYS HE3 H 2.956 0.02 1 205 . 18 LYS HE2 H 2.956 0.02 1 206 . 18 LYS C C 179.222 0.10 1 207 . 19 VAL N N 119.867 0.10 1 208 . 19 VAL H H 7.434 0.02 1 209 . 19 VAL CA C 66.166 0.10 1 210 . 19 VAL HA H 3.595 0.02 1 211 . 19 VAL CB C 32.368 0.10 1 212 . 19 VAL HB H 1.977 0.02 1 213 . 19 VAL CG2 C 22.455 0.10 1 214 . 19 VAL HG2 H 1.045 0.02 4 215 . 19 VAL CG1 C 22.455 0.10 1 216 . 19 VAL HG1 H 1.078 0.02 4 217 . 19 VAL C C 178.040 0.10 1 218 . 20 ILE N N 120.109 0.10 1 219 . 20 ILE H H 8.126 0.02 1 220 . 20 ILE CA C 65.353 0.10 1 221 . 20 ILE HA H 2.958 0.02 1 222 . 20 ILE CB C 37.045 0.10 1 223 . 20 ILE HB H 1.204 0.02 1 224 . 20 ILE CG1 C 27.830 0.10 2 225 . 20 ILE HG13 H -1.078 0.02 9 226 . 20 ILE HG12 H 0.682 0.02 9 227 . 20 ILE CD1 C 14.373 0.10 1 228 . 20 ILE HD1 H -0.086 0.02 1 229 . 20 ILE CG2 C 16.918 0.10 2 230 . 20 ILE HG2 H 0.099 0.02 4 231 . 20 ILE C C 177.403 0.10 1 232 . 21 LEU N N 116.524 0.10 1 233 . 21 LEU H H 7.924 0.02 1 234 . 21 LEU CA C 56.717 0.10 1 235 . 21 LEU HA H 4.091 0.02 1 236 . 21 LEU CB C 41.208 0.10 1 237 . 21 LEU HB3 H 1.377 0.02 2 238 . 21 LEU HB2 H 1.758 0.02 2 239 . 21 LEU CG C 27.627 0.10 1 240 . 21 LEU HG H 1.651 0.02 1 241 . 21 LEU CD1 C 25.324 0.10 2 242 . 21 LEU HD1 H 0.920 0.02 4 243 . 21 LEU CD2 C 23.417 0.10 2 244 . 21 LEU HD2 H 0.819 0.02 4 245 . 21 LEU C C 179.475 0.10 1 246 . 22 GLN N N 118.388 0.10 1 247 . 22 GLN H H 7.307 0.02 1 248 . 22 GLN CA C 58.262 0.10 1 249 . 22 GLN HA H 4.112 0.02 1 250 . 22 GLN CB C 28.515 0.10 1 251 . 22 GLN HB3 H 2.231 0.02 2 252 . 22 GLN HB2 H 2.300 0.02 2 253 . 22 GLN CG C 34.149 0.10 1 254 . 22 GLN HG3 H 2.453 0.02 2 255 . 22 GLN HG2 H 2.536 0.02 2 256 . 22 GLN CD C 180.662 0.10 1 257 . 22 GLN NE2 N 112.312 0.10 1 258 . 22 GLN HE21 H 7.558 0.02 2 259 . 22 GLN HE22 H 6.839 0.02 2 260 . 22 GLN C C 177.657 0.10 1 261 . 23 ASP N N 118.878 0.10 1 262 . 23 ASP H H 7.611 0.02 1 263 . 23 ASP CA C 56.324 0.10 1 264 . 23 ASP HA H 4.696 0.02 1 265 . 23 ASP CB C 42.918 0.10 1 266 . 23 ASP HB3 H 2.996 0.02 2 267 . 23 ASP HB2 H 3.071 0.02 2 268 . 23 ASP C C 176.728 0.10 1 269 . 24 LYS N N 124.627 0.10 1 270 . 24 LYS H H 9.142 0.02 1 271 . 24 LYS CA C 53.872 0.10 1 272 . 24 LYS HA H 4.737 0.02 1 273 . 24 LYS CB C 33.949 0.10 1 274 . 24 LYS HB3 H 1.611 0.02 2 275 . 24 LYS HB2 H 2.094 0.02 2 276 . 24 LYS CG C 26.638 0.10 1 277 . 24 LYS HG3 H 1.029 0.02 2 278 . 24 LYS HG2 H 1.692 0.02 2 279 . 24 LYS CD C 30.361 0.10 1 280 . 24 LYS HD3 H 1.369 0.02 2 281 . 24 LYS HD2 H 2.007 0.02 2 282 . 24 LYS CE C 43.055 0.10 1 283 . 24 LYS HE3 H 3.164 0.02 2 284 . 24 LYS HE2 H 2.656 0.02 2 285 . 24 LYS C C 171.667 0.10 1 286 . 25 PRO HA H 4.703 0.02 1 287 . 25 PRO HB2 H 2.471 0.02 2 288 . 25 PRO HG3 H 1.957 0.02 2 289 . 25 PRO HG2 H 2.084 0.02 2 290 . 25 PRO HD3 H 3.442 0.02 2 291 . 25 PRO HD2 H 3.753 0.02 2 292 . 26 GLU N N 118.398 0.10 1 293 . 26 GLU H H 9.477 0.02 1 294 . 26 GLU CA C 55.558 0.10 1 295 . 26 GLU HA H 4.453 0.02 1 296 . 26 GLU CB C 28.006 0.10 1 297 . 26 GLU HB3 H 2.088 0.02 1 298 . 26 GLU HB2 H 2.088 0.02 1 299 . 26 GLU CG C 35.864 0.10 1 300 . 26 GLU HG3 H 2.455 0.02 1 301 . 26 GLU HG2 H 2.455 0.02 1 302 . 26 GLU C C 175.902 0.10 1 303 . 27 ALA N N 123.765 0.10 1 304 . 27 ALA H H 8.017 0.02 1 305 . 27 ALA CA C 52.919 0.10 1 306 . 27 ALA HA H 4.183 0.02 1 307 . 27 ALA CB C 19.007 0.10 1 308 . 27 ALA HB H 1.145 0.02 1 309 . 27 ALA C C 177.080 0.10 1 310 . 28 GLN N N 123.984 0.10 1 311 . 28 GLN H H 8.969 0.02 1 312 . 28 GLN CA C 54.101 0.10 1 313 . 28 GLN HA H 4.380 0.02 1 314 . 28 GLN CB C 28.276 0.10 1 315 . 28 GLN HB3 H 1.818 0.02 2 316 . 28 GLN HB2 H 1.923 0.02 2 317 . 28 GLN CG C 33.198 0.10 1 318 . 28 GLN HG3 H 2.183 0.02 2 319 . 28 GLN HG2 H 2.319 0.02 2 320 . 28 GLN CD C 180.274 0.10 1 321 . 28 GLN NE2 N 113.510 0.10 1 322 . 28 GLN HE21 H 7.359 0.02 2 323 . 28 GLN HE22 H 6.734 0.02 2 324 . 28 GLN C C 174.521 0.10 1 325 . 29 ILE N N 126.811 0.10 1 326 . 29 ILE H H 8.331 0.02 1 327 . 29 ILE CA C 60.288 0.10 1 328 . 29 ILE HA H 4.740 0.02 1 329 . 29 ILE CB C 37.879 0.10 1 330 . 29 ILE HB H 1.674 0.02 1 331 . 29 ILE CG1 C 28.400 0.10 2 332 . 29 ILE HG13 H 0.801 0.02 9 333 . 29 ILE HG12 H 1.403 0.02 9 334 . 29 ILE CD1 C 13.432 0.10 1 335 . 29 ILE HD1 H 0.648 0.02 1 336 . 29 ILE CG2 C 17.333 0.10 2 337 . 29 ILE HG2 H 0.655 0.02 4 338 . 29 ILE C C 175.958 0.10 1 339 . 30 ILE N N 129.977 0.10 1 340 . 30 ILE H H 7.905 0.02 1 341 . 30 ILE CA C 58.699 0.10 1 342 . 30 ILE HA H 4.422 0.02 1 343 . 30 ILE CB C 40.915 0.10 1 344 . 30 ILE HB H 1.555 0.02 1 345 . 30 ILE CG1 C 27.132 0.10 2 346 . 30 ILE HG13 H 1.100 0.02 9 347 . 30 ILE HG12 H 1.319 0.02 9 348 . 30 ILE CD1 C 12.387 0.10 1 349 . 30 ILE HD1 H 0.753 0.02 1 350 . 30 ILE CG2 C 16.732 0.10 2 351 . 30 ILE HG2 H 0.820 0.02 4 352 . 30 ILE C C 173.302 0.10 1 353 . 31 VAL N N 129.088 0.10 1 354 . 31 VAL H H 8.494 0.02 1 355 . 31 VAL CA C 61.695 0.10 1 356 . 31 VAL HA H 4.684 0.02 1 357 . 31 VAL CB C 32.503 0.10 1 358 . 31 VAL HB H 1.902 0.02 1 359 . 31 VAL HG2 H 0.838 0.02 4 360 . 31 VAL CG1 C 22.395 0.10 2 361 . 31 VAL HG1 H 0.838 0.02 4 362 . 31 VAL C C 175.490 0.10 1 363 . 32 LEU N N 130.156 0.10 1 364 . 32 LEU H H 9.127 0.02 1 365 . 32 LEU CA C 51.807 0.10 1 366 . 32 LEU HA H 5.002 0.02 1 367 . 32 LEU CB C 45.486 0.10 1 368 . 32 LEU HB3 H 1.225 0.02 2 369 . 32 LEU HB2 H 1.338 0.02 2 370 . 32 LEU CG C 23.788 0.10 1 371 . 32 LEU HG H 0.772 0.02 1 372 . 32 LEU CD1 C 26.558 0.10 1 373 . 32 LEU HD1 H 1.262 0.02 4 374 . 32 LEU CD2 C 26.558 0.10 1 375 . 32 LEU HD2 H 0.552 0.02 4 376 . 33 PRO HB3 H 2.520 0.02 2 377 . 33 PRO HB2 H 1.807 0.02 2 378 . 33 PRO HG3 H 2.023 0.02 2 379 . 33 PRO HG2 H 2.114 0.02 2 380 . 33 PRO HD3 H 3.653 0.02 2 381 . 33 PRO HD2 H 3.894 0.02 2 382 . 34 VAL N N 126.315 0.10 1 383 . 34 VAL H H 8.959 0.02 1 384 . 34 VAL CA C 64.149 0.10 1 385 . 34 VAL HA H 4.043 0.02 1 386 . 34 VAL CB C 32.107 0.10 1 387 . 34 VAL HB H 1.777 0.02 1 388 . 34 VAL CG2 C 19.758 0.10 2 389 . 34 VAL HG2 H 0.957 0.02 4 390 . 34 VAL CG1 C 21.803 0.10 2 391 . 34 VAL HG1 H 0.957 0.02 4 392 . 34 VAL C C 174.714 0.10 1 393 . 35 GLY N N 116.564 0.10 1 394 . 35 GLY H H 8.971 0.02 1 395 . 35 GLY CA C 44.518 0.10 1 396 . 35 GLY HA3 H 3.540 0.02 2 397 . 35 GLY HA2 H 4.359 0.02 2 398 . 35 GLY C C 174.654 0.10 1 399 . 36 THR N N 118.596 0.10 1 400 . 36 THR H H 7.621 0.02 1 401 . 36 THR CA C 64.752 0.10 1 402 . 36 THR HA H 4.048 0.02 1 403 . 36 THR CB C 69.706 0.10 1 404 . 36 THR HB H 4.105 0.02 1 405 . 36 THR CG2 C 21.790 0.10 1 406 . 36 THR HG2 H 1.341 0.02 1 407 . 36 THR C C 173.264 0.10 1 408 . 37 ILE N N 129.707 0.10 1 409 . 37 ILE H H 8.591 0.02 1 410 . 37 ILE CA C 61.437 0.10 1 411 . 37 ILE HA H 4.077 0.02 1 412 . 37 ILE CB C 37.298 0.10 1 413 . 37 ILE HB H 1.857 0.02 1 414 . 37 ILE CG1 C 27.818 0.10 2 415 . 37 ILE HG13 H 1.318 0.02 9 416 . 37 ILE HG12 H 1.642 0.02 9 417 . 37 ILE CD1 C 11.963 0.10 1 418 . 37 ILE HD1 H 0.886 0.02 1 419 . 37 ILE CG2 C 17.064 0.10 2 420 . 37 ILE HG2 H 0.905 0.02 4 421 . 37 ILE C C 176.099 0.10 1 422 . 38 VAL N N 121.112 0.10 1 423 . 38 VAL H H 8.083 0.02 1 424 . 38 VAL CA C 58.905 0.10 1 425 . 38 VAL HA H 4.825 0.02 1 426 . 38 VAL CB C 34.952 0.10 1 427 . 38 VAL HB H 2.359 0.02 1 428 . 38 VAL CG2 C 18.376 0.10 2 429 . 38 VAL HG2 H 0.958 0.02 4 430 . 38 VAL CG1 C 22.438 0.10 2 431 . 38 VAL HG1 H 0.958 0.02 4 432 . 38 VAL C C 176.284 0.10 1 433 . 39 THR N N 112.898 0.10 1 434 . 39 THR H H 7.981 0.02 1 435 . 39 THR CA C 61.693 0.10 1 436 . 39 THR HA H 4.441 0.02 1 437 . 39 THR CB C 68.903 0.10 1 438 . 39 THR HB H 4.617 0.02 1 439 . 39 THR CG2 C 22.180 0.10 1 440 . 39 THR HG2 H 1.301 0.02 1 441 . 39 THR C C 176.112 0.10 1 442 . 40 MET N N 118.412 0.10 1 443 . 40 MET H H 8.541 0.02 1 444 . 40 MET CA C 55.717 0.10 1 445 . 40 MET HA H 4.611 0.02 1 446 . 40 MET CB C 32.378 0.10 1 447 . 40 MET HB3 H 1.994 0.02 2 448 . 40 MET HB2 H 2.330 0.02 2 449 . 40 MET CG C 30.492 0.10 1 450 . 40 MET HG3 H 2.563 0.02 2 451 . 40 MET HG2 H 2.730 0.02 2 452 . 40 MET C C 176.530 0.10 1 453 . 41 GLU N N 124.786 0.10 1 454 . 41 GLU H H 8.565 0.02 1 455 . 41 GLU CA C 57.023 0.10 1 456 . 41 GLU HA H 4.307 0.02 1 457 . 41 GLU CB C 28.962 0.10 1 458 . 41 GLU HB3 H 2.013 0.02 2 459 . 41 GLU HB2 H 2.158 0.02 2 460 . 41 GLU CG C 35.869 0.10 1 461 . 41 GLU HG3 H 2.413 0.02 1 462 . 41 GLU HG2 H 2.413 0.02 1 463 . 41 GLU C C 174.199 0.10 1 464 . 42 TYR N N 126.134 0.10 1 465 . 42 TYR H H 8.646 0.02 1 466 . 42 TYR CA C 57.631 0.10 1 467 . 42 TYR HA H 4.880 0.02 1 468 . 42 TYR CB C 39.909 0.10 1 469 . 42 TYR HB3 H 2.945 0.02 2 470 . 42 TYR HB2 H 3.029 0.02 2 471 . 42 TYR HD1 H 7.322 0.02 2 472 . 42 TYR HE1 H 6.685 0.02 2 473 . 42 TYR HE2 H 6.601 0.02 2 474 . 42 TYR HD2 H 7.173 0.02 2 475 . 42 TYR C C 175.678 0.10 1 476 . 43 ARG N N 132.043 0.10 1 477 . 43 ARG H H 8.837 0.02 1 478 . 43 ARG CA C 54.136 0.10 1 479 . 43 ARG HA H 4.506 0.02 1 480 . 43 ARG CB C 32.153 0.10 1 481 . 43 ARG HB3 H 1.459 0.02 2 482 . 43 ARG HB2 H 1.753 0.02 2 483 . 43 ARG CG C 27.135 0.10 1 484 . 43 ARG HG3 H 1.544 0.02 1 485 . 43 ARG HG2 H 1.544 0.02 1 486 . 43 ARG CD C 43.227 0.10 1 487 . 43 ARG HD3 H 3.097 0.02 2 488 . 43 ARG HD2 H 3.147 0.02 2 489 . 43 ARG NE N 85.943 0.10 1 490 . 43 ARG HE H 7.880 0.02 1 491 . 43 ARG C C 175.261 0.10 1 492 . 44 ILE N N 122.476 0.10 1 493 . 44 ILE H H 8.046 0.02 1 494 . 44 ILE CA C 62.746 0.10 1 495 . 44 ILE HA H 3.677 0.02 1 496 . 44 ILE CB C 39.157 0.10 1 497 . 44 ILE HB H 1.885 0.02 1 498 . 44 ILE CG1 C 28.701 0.10 2 499 . 44 ILE HG13 H 1.357 0.02 9 500 . 44 ILE HG12 H 1.603 0.02 9 501 . 44 ILE CD1 C 14.384 0.10 1 502 . 44 ILE HD1 H 1.001 0.02 1 503 . 44 ILE CG2 C 16.386 0.10 2 504 . 44 ILE HG2 H 0.949 0.02 4 505 . 44 ILE C C 174.213 0.10 1 506 . 45 ASP N N 116.494 0.10 1 507 . 45 ASP H H 8.330 0.02 1 508 . 45 ASP CA C 53.187 0.10 1 509 . 45 ASP HA H 4.372 0.02 1 510 . 45 ASP CB C 40.398 0.10 1 511 . 45 ASP HB3 H 2.675 0.02 2 512 . 45 ASP HB2 H 2.799 0.02 2 513 . 45 ASP C C 173.962 0.10 1 514 . 46 ARG N N 123.709 0.10 1 515 . 46 ARG H H 7.288 0.02 1 516 . 46 ARG CA C 55.337 0.10 1 517 . 46 ARG HA H 4.961 0.02 1 518 . 46 ARG CB C 34.173 0.10 1 519 . 46 ARG HB3 H 1.246 0.02 2 520 . 46 ARG HB2 H 2.246 0.02 2 521 . 46 ARG CG C 25.806 0.10 1 522 . 46 ARG HG3 H 1.483 0.02 2 523 . 46 ARG HG2 H 1.660 0.02 2 524 . 46 ARG CD C 44.564 0.10 1 525 . 46 ARG HD3 H 3.015 0.02 1 526 . 46 ARG HD2 H 3.015 0.02 1 527 . 46 ARG NE N 83.984 0.10 1 528 . 46 ARG HE H 9.259 0.02 1 529 . 46 ARG C C 174.377 0.10 1 530 . 47 VAL N N 123.164 0.10 1 531 . 47 VAL H H 8.117 0.02 1 532 . 47 VAL CA C 62.026 0.10 1 533 . 47 VAL HA H 4.394 0.02 1 534 . 47 VAL CB C 35.207 0.10 1 535 . 47 VAL HB H 1.633 0.02 1 536 . 47 VAL HG2 H 0.567 0.02 4 537 . 47 VAL CG1 C 21.749 0.10 2 538 . 47 VAL HG1 H 0.706 0.02 4 539 . 47 VAL C C 174.911 0.10 1 540 . 48 ARG N N 126.552 0.10 1 541 . 48 ARG H H 9.012 0.02 1 542 . 48 ARG CA C 55.564 0.10 1 543 . 48 ARG HA H 4.662 0.02 1 544 . 48 ARG CB C 31.082 0.10 1 545 . 48 ARG HB3 H 0.861 0.02 2 546 . 48 ARG HB2 H 1.825 0.02 2 547 . 48 ARG CG C 29.184 0.10 1 548 . 48 ARG HG3 H 1.223 0.02 2 549 . 48 ARG HG2 H 1.618 0.02 2 550 . 48 ARG CD C 43.929 0.10 1 551 . 48 ARG HD3 H 2.916 0.02 2 552 . 48 ARG HD2 H 3.313 0.02 2 553 . 48 ARG NE N 83.438 0.10 1 554 . 48 ARG HE H 7.677 0.02 1 555 . 48 ARG C C 175.457 0.10 1 556 . 49 LEU N N 124.208 0.10 1 557 . 49 LEU H H 9.062 0.02 1 558 . 49 LEU CA C 52.236 0.10 1 559 . 49 LEU HA H 4.795 0.02 1 560 . 49 LEU CB C 42.199 0.10 1 561 . 49 LEU HB3 H 0.968 0.02 2 562 . 49 LEU HB2 H 1.756 0.02 2 563 . 49 LEU CG C 23.305 0.10 1 564 . 49 LEU HG H 0.635 0.02 1 565 . 49 LEU CD1 C 26.490 0.10 2 566 . 49 LEU HD1 H 1.470 0.02 4 567 . 49 LEU HD2 H 0.619 0.02 4 568 . 49 LEU C C 174.054 0.10 1 569 . 50 PHE N N 123.524 0.10 1 570 . 50 PHE H H 9.089 0.02 1 571 . 50 PHE CA C 56.369 0.10 1 572 . 50 PHE HA H 5.697 0.02 1 573 . 50 PHE CB C 40.410 0.10 1 574 . 50 PHE HB3 H 2.601 0.02 2 575 . 50 PHE HB2 H 2.870 0.02 2 576 . 50 PHE HD1 H 7.239 0.02 2 577 . 50 PHE C C 177.269 0.10 1 578 . 51 VAL N N 115.505 0.10 1 579 . 51 VAL H H 8.742 0.02 1 580 . 51 VAL CA C 58.591 0.10 1 581 . 51 VAL HA H 5.355 0.02 1 582 . 51 VAL CB C 35.987 0.10 1 583 . 51 VAL HB H 2.068 0.02 1 584 . 51 VAL CG2 C 17.738 0.10 2 585 . 51 VAL HG2 H 0.620 0.02 4 586 . 51 VAL CG1 C 21.807 0.10 2 587 . 51 VAL HG1 H 0.827 0.02 4 588 . 51 VAL C C 176.943 0.10 1 589 . 52 ASP N N 124.248 0.10 1 590 . 52 ASP H H 8.816 0.02 1 591 . 52 ASP CA C 52.249 0.10 1 592 . 52 ASP HA H 4.744 0.02 1 593 . 52 ASP CB C 41.649 0.10 1 594 . 52 ASP HB3 H 2.648 0.02 2 595 . 52 ASP HB2 H 3.455 0.02 2 596 . 52 ASP C C 178.294 0.10 1 597 . 53 LYS N N 116.797 0.10 1 598 . 53 LYS H H 8.239 0.02 1 599 . 53 LYS CA C 58.270 0.10 1 600 . 53 LYS HA H 4.181 0.02 1 601 . 53 LYS CB C 32.015 0.10 1 602 . 53 LYS HB3 H 1.923 0.02 1 603 . 53 LYS HB2 H 1.923 0.02 1 604 . 53 LYS CG C 25.088 0.10 1 605 . 53 LYS HG3 H 1.532 0.02 1 606 . 53 LYS HG2 H 1.532 0.02 1 607 . 53 LYS CD C 29.177 0.10 1 608 . 53 LYS HD3 H 1.738 0.02 1 609 . 53 LYS HD2 H 1.738 0.02 1 610 . 53 LYS CE C 41.975 0.10 1 611 . 53 LYS HE2 H 3.026 0.02 2 612 . 53 LYS NZ N 33.324 0.10 1 613 . 53 LYS HZ H 7.566 0.02 1 614 . 53 LYS C C 176.970 0.10 1 615 . 54 LEU N N 121.712 0.10 1 616 . 54 LEU H H 8.033 0.02 1 617 . 54 LEU CA C 54.270 0.10 1 618 . 54 LEU HA H 4.424 0.02 1 619 . 54 LEU CB C 41.265 0.10 1 620 . 54 LEU HB3 H 1.719 0.02 2 621 . 54 LEU HB2 H 1.817 0.02 2 622 . 54 LEU CG C 27.396 0.10 1 623 . 54 LEU HG H 1.543 0.02 1 624 . 54 LEU CD1 C 25.202 0.10 2 625 . 54 LEU HD1 H 0.917 0.02 4 626 . 54 LEU CD2 C 23.111 0.10 2 627 . 54 LEU HD2 H 0.844 0.02 4 628 . 54 LEU C C 176.152 0.10 1 629 . 55 ASP N N 115.553 0.10 1 630 . 55 ASP H H 8.279 0.02 1 631 . 55 ASP CA C 55.230 0.10 1 632 . 55 ASP HA H 4.194 0.02 1 633 . 55 ASP CB C 37.971 0.10 1 634 . 55 ASP HB3 H 2.917 0.02 2 635 . 55 ASP HB2 H 3.317 0.02 2 636 . 55 ASP C C 173.255 0.10 1 637 . 56 ASN N N 115.294 0.10 1 638 . 56 ASN H H 8.223 0.02 1 639 . 56 ASN CA C 51.258 0.10 1 640 . 56 ASN HA H 5.405 0.02 1 641 . 56 ASN CB C 39.888 0.10 1 642 . 56 ASN HB3 H 2.011 0.02 2 643 . 56 ASN HB2 H 3.001 0.02 2 644 . 56 ASN CG C 175.786 0.10 1 645 . 56 ASN ND2 N 114.840 0.10 1 646 . 56 ASN HD21 H 8.028 0.02 2 647 . 56 ASN HD22 H 6.676 0.02 2 648 . 56 ASN C C 176.288 0.10 1 649 . 57 ILE N N 120.432 0.10 1 650 . 57 ILE H H 9.135 0.02 1 651 . 57 ILE CA C 60.626 0.10 1 652 . 57 ILE HA H 3.989 0.02 1 653 . 57 ILE CB C 34.706 0.10 1 654 . 57 ILE HB H 2.584 0.02 1 655 . 57 ILE CG1 C 27.874 0.10 2 656 . 57 ILE HG13 H 1.177 0.02 9 657 . 57 ILE HG12 H 1.750 0.02 9 658 . 57 ILE CD1 C 12.139 0.10 1 659 . 57 ILE HD1 H 0.705 0.02 1 660 . 57 ILE CG2 C 20.446 0.10 2 661 . 57 ILE HG2 H 1.066 0.02 4 662 . 57 ILE C C 178.616 0.10 1 663 . 58 ALA N N 132.557 0.10 1 664 . 58 ALA H H 9.569 0.02 1 665 . 58 ALA CA C 52.562 0.10 1 666 . 58 ALA HA H 4.665 0.02 1 667 . 58 ALA CB C 21.778 0.10 1 668 . 58 ALA HB H 1.431 0.02 1 669 . 58 ALA C C 176.258 0.10 1 670 . 59 GLN N N 115.000 0.10 1 671 . 59 GLN H H 7.302 0.02 1 672 . 59 GLN CA C 53.512 0.10 1 673 . 59 GLN HA H 4.755 0.02 1 674 . 59 GLN CB C 33.549 0.10 1 675 . 59 GLN HB3 H 1.977 0.02 2 676 . 59 GLN HB2 H 2.114 0.02 2 677 . 59 GLN CG C 31.779 0.10 1 678 . 59 GLN HG3 H 2.177 0.02 2 679 . 59 GLN HG2 H 2.306 0.02 2 680 . 59 GLN CD C 179.088 0.10 1 681 . 59 GLN NE2 N 113.117 0.10 1 682 . 59 GLN HE21 H 7.404 0.02 2 683 . 59 GLN HE22 H 6.486 0.02 2 684 . 59 GLN C C 175.328 0.10 1 685 . 60 VAL N N 126.410 0.10 1 686 . 60 VAL H H 8.941 0.02 1 687 . 60 VAL CA C 62.562 0.10 1 688 . 60 VAL HA H 3.604 0.02 1 689 . 60 VAL CB C 32.892 0.10 1 690 . 60 VAL HB H 2.112 0.02 1 691 . 60 VAL CG2 C 20.210 0.10 2 692 . 60 VAL HG2 H 0.871 0.02 4 693 . 60 VAL CG1 C 22.346 0.10 2 694 . 60 VAL HG1 H 1.178 0.02 4 695 . 60 VAL C C 174.630 0.10 1 696 . 62 ARG N N 123.861 0.10 1 697 . 62 ARG H H 9.342 0.02 1 698 . 62 ARG CA C 54.763 0.10 1 699 . 62 ARG HA H 5.732 0.02 1 700 . 62 ARG CB C 34.716 0.10 1 701 . 62 ARG HB3 H 2.002 0.02 2 702 . 62 ARG HB2 H 2.079 0.02 2 703 . 62 ARG CG C 27.150 0.10 1 704 . 62 ARG HG3 H 1.843 0.02 1 705 . 62 ARG HG2 H 1.843 0.02 1 706 . 62 ARG CD C 43.924 0.10 1 707 . 62 ARG HD3 H 3.347 0.02 1 708 . 62 ARG HD2 H 3.347 0.02 1 709 . 62 ARG NE N 86.279 0.10 1 710 . 62 ARG HE H 7.345 0.02 1 711 . 62 ARG C C 175.431 0.10 1 712 . 63 VAL N N 123.007 0.10 1 713 . 63 VAL H H 8.517 0.02 1 714 . 63 VAL CA C 62.843 0.10 1 715 . 63 VAL HA H 4.666 0.02 1 716 . 63 VAL CB C 33.131 0.10 1 717 . 63 VAL HB H 2.219 0.02 1 718 . 63 VAL HG2 H 1.166 0.02 4 719 . 63 VAL CG1 C 23.071 0.10 2 720 . 63 VAL HG1 H 1.309 0.02 4 721 . 63 VAL C C 176.178 0.10 1 722 . 64 GLY N N 122.817 0.10 1 723 . 64 GLY H H 8.784 0.02 1 724 . 64 GLY CA C 47.239 0.10 1 725 . 64 GLY HA3 H 3.053 0.02 2 726 . 64 GLY HA2 H 4.271 0.02 2 727 . 64 GLY C C 180.523 0.10 1 stop_ save_