data_5572 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect ; _BMRB_accession_number 5572 _BMRB_flat_file_name bmr5572.str _Entry_type original _Submission_date 2002-11-04 _Accession_date 2002-11-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Graether Steffen P . 2 Kuiper Michael J . 3 Gagne Stephane M . 4 Walker Virginia K . 5 Jia Zongchao . . 6 Sykes Brian D . 7 Davies Peter L . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 423 "13C chemical shifts" 226 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-27 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5573 'Spruce budworm antifreeze protein (5 C)' stop_ _Original_release_date 2002-12-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20372205 _PubMed_ID 10917537 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Graether Steffen P . 2 Kuiper Michael J . 3 Gagne Stephane M . 4 Walker Virginia K . 5 Jia Zongchao . . 6 Sykes Brian D . 7 Davies Peter L . stop_ _Journal_abbreviation Nature _Journal_volume 406 _Journal_issue 6793 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 325 _Page_last 328 _Year 2000 _Details . loop_ _Keyword antifreeze beta-helix ice stop_ save_ ################################## # Molecular system description # ################################## save_system_sbwAFP _Saveframe_category molecular_system _Mol_system_name 'spruce budworm antifreeze protein' _Abbreviation_common sbwAFP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label sbwAFP $sbwAFP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound' loop_ _Biological_function 'ice growth inhibition' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_sbwAFP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'spruce budworm antifreeze protein' _Name_variant 'Choristoneura fumiferana antifreeze protein' _Abbreviation_common sbwAFP _Molecular_mass . _Mol_thiol_state 'disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 90 _Mol_residue_sequence ; DGSCTNTNSQLSANSKCEKS TLTNCYVDKSEVYGTTCTGS RFDGVTITTSTSTGSRISGP GCKISTCIITGGVPAPSAAC KISGCTFSAN ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 GLY 3 SER 4 CYS 5 THR 6 ASN 7 THR 8 ASN 9 SER 10 GLN 11 LEU 12 SER 13 ALA 14 ASN 15 SER 16 LYS 17 CYS 18 GLU 19 LYS 20 SER 21 THR 22 LEU 23 THR 24 ASN 25 CYS 26 TYR 27 VAL 28 ASP 29 LYS 30 SER 31 GLU 32 VAL 33 TYR 34 GLY 35 THR 36 THR 37 CYS 38 THR 39 GLY 40 SER 41 ARG 42 PHE 43 ASP 44 GLY 45 VAL 46 THR 47 ILE 48 THR 49 THR 50 SER 51 THR 52 SER 53 THR 54 GLY 55 SER 56 ARG 57 ILE 58 SER 59 GLY 60 PRO 61 GLY 62 CYS 63 LYS 64 ILE 65 SER 66 THR 67 CYS 68 ILE 69 ILE 70 THR 71 GLY 72 GLY 73 VAL 74 PRO 75 ALA 76 PRO 77 SER 78 ALA 79 ALA 80 CYS 81 LYS 82 ILE 83 SER 84 GLY 85 CYS 86 THR 87 PHE 88 SER 89 ALA 90 ASN 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 BMRB 5573 sbwAFP 100.00 90 100.00 100.00 1.05e-53 PDB 1EWW "Solution Structure Of Spruce Budworm Antifreeze Protein At 30 Degrees Celsius" 100.00 90 100.00 100.00 1.05e-53 PDB 1L0S "Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 337" 100.00 90 97.78 98.89 7.62e-52 PDB 1N4I "Solution Structure Of Spruce Budworm Antifreeze Protein At 5 Degrees Celsius" 100.00 90 100.00 100.00 1.05e-53 GB AAG32660 "thermal hysteresis protein precursor [Choristoneura fumiferana]" 100.00 108 100.00 100.00 2.80e-54 GB AAG33032 "thermal hysteresis protein [synthetic construct]" 100.00 91 100.00 100.00 9.63e-54 GB AAG33033 "PR-S/thermal hysteresis protein fusion protein [synthetic construct]" 100.00 115 100.00 100.00 7.65e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $sbwAFP 'Spruce budworm' 7141 Eukaryota Metazoa Choristoneura fumiferana 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 $sbwAFP '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 $sbwAFP 18 mM '[U-15N; U-13C]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.25 n/a temperature 303 0.1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name sbwAFP _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 ASP H H 8.47 0.03 1 2 . 1 ASP HA H 5.22 0.03 1 3 . 1 ASP HB2 H 3.26 0.03 1 4 . 1 ASP HB3 H 3.26 0.03 1 5 . 1 ASP CA C 54.66 0.50 1 6 . 1 ASP CB C 41.68 0.50 1 7 . 1 ASP N N 121.11 0.50 1 8 . 2 GLY H H 8.57 0.03 1 9 . 2 GLY HA2 H 4.73 0.03 1 10 . 2 GLY HA3 H 4.12 0.03 1 11 . 2 GLY CA C 45.87 0.50 1 12 . 2 GLY N N 110.31 0.50 1 13 . 3 SER H H 8.64 0.03 1 14 . 3 SER HA H 4.61 0.03 1 15 . 3 SER HB2 H 4.17 0.03 1 16 . 3 SER HB3 H 3.94 0.03 1 17 . 3 SER CA C 58.28 0.50 1 18 . 3 SER CB C 64.03 0.50 1 19 . 3 SER N N 115.38 0.50 1 20 . 4 CYS H H 8.37 0.03 1 21 . 4 CYS HA H 4.42 0.03 1 22 . 4 CYS HB2 H 1.77 0.03 1 23 . 4 CYS HB3 H 1.77 0.03 1 24 . 4 CYS CA C 56.17 0.50 1 25 . 4 CYS CB C 30.70 0.50 1 26 . 4 CYS N N 122.83 0.50 1 27 . 5 THR H H 7.42 0.03 1 28 . 5 THR HA H 5.45 0.03 1 29 . 5 THR HB H 4.00 0.03 1 30 . 5 THR HG2 H 3.65 0.03 1 31 . 5 THR CA C 58.21 0.50 1 32 . 5 THR CB C 68.20 0.50 1 33 . 5 THR CG2 C 20.49 0.50 1 34 . 5 THR N N 110.56 0.50 1 35 . 6 ASN H H 8.94 0.03 1 36 . 6 ASN HA H 5.10 0.03 1 37 . 6 ASN HB2 H 3.02 0.03 1 38 . 6 ASN HB3 H 2.40 0.03 1 39 . 6 ASN HD21 H 7.45 0.03 1 40 . 6 ASN HD22 H 6.12 0.03 1 41 . 6 ASN CA C 52.17 0.50 1 42 . 6 ASN CB C 39.88 0.50 1 43 . 6 ASN N N 127.03 0.50 1 44 . 6 ASN ND2 N 108.76 0.50 1 45 . 7 THR H H 9.01 0.03 1 46 . 7 THR HA H 4.49 0.03 1 47 . 7 THR HB H 4.10 0.03 1 48 . 7 THR HG2 H 1.25 0.03 1 49 . 7 THR CA C 61.89 0.50 1 50 . 7 THR CB C 69.30 0.50 1 51 . 7 THR CG2 C 21.30 0.50 1 52 . 7 THR N N 122.78 0.50 1 53 . 8 ASN H H 8.40 0.03 1 54 . 8 ASN HA H 4.41 0.03 1 55 . 8 ASN HB2 H 3.30 0.03 1 56 . 8 ASN HB3 H 2.64 0.03 1 57 . 8 ASN HD21 H 7.58 0.03 1 58 . 8 ASN HD22 H 6.91 0.03 1 59 . 8 ASN CA C 54.37 0.50 1 60 . 8 ASN CB C 37.91 0.50 1 61 . 8 ASN N N 119.48 0.50 1 62 . 8 ASN ND2 N 112.68 0.50 1 63 . 9 SER H H 8.42 0.03 1 64 . 9 SER HA H 5.27 0.03 1 65 . 9 SER HB2 H 3.40 0.03 1 66 . 9 SER HB3 H 3.40 0.03 1 67 . 9 SER CA C 57.87 0.50 1 68 . 9 SER CB C 65.61 0.50 1 69 . 9 SER N N 110.24 0.50 1 70 . 10 GLN H H 8.21 0.03 1 71 . 10 GLN HA H 4.51 0.03 1 72 . 10 GLN HB2 H 1.88 0.03 1 73 . 10 GLN HB3 H 1.88 0.03 1 74 . 10 GLN HG2 H 2.23 0.03 1 75 . 10 GLN HG3 H 2.23 0.03 1 76 . 10 GLN HE21 H 7.35 0.03 1 77 . 10 GLN HE22 H 6.71 0.03 1 78 . 10 GLN CA C 54.68 0.50 1 79 . 10 GLN CB C 30.47 0.50 1 80 . 10 GLN CG C 33.65 0.50 1 81 . 10 GLN N N 123.05 0.50 1 82 . 10 GLN NE2 N 111.31 0.50 1 83 . 11 LEU H H 8.56 0.03 1 84 . 11 LEU HA H 4.76 0.03 1 85 . 11 LEU HB2 H 1.75 0.03 1 86 . 11 LEU HB3 H 0.99 0.03 1 87 . 11 LEU HG H 1.46 0.03 1 88 . 11 LEU HD1 H 0.70 0.03 1 89 . 11 LEU HD2 H 0.81 0.03 1 90 . 11 LEU CA C 53.44 0.50 1 91 . 11 LEU CB C 43.63 0.50 1 92 . 11 LEU CG C 27.27 0.50 1 93 . 11 LEU CD1 C 24.98 0.50 1 94 . 11 LEU CD2 C 26.56 0.50 1 95 . 11 LEU N N 127.66 0.50 1 96 . 12 SER H H 8.39 0.03 1 97 . 12 SER HA H 4.41 0.03 1 98 . 12 SER HB2 H 4.36 0.03 1 99 . 12 SER HB3 H 4.22 0.03 1 100 . 12 SER CA C 58.71 0.50 1 101 . 12 SER CB C 64.77 0.50 1 102 . 12 SER N N 122.18 0.50 1 103 . 13 ALA H H 8.85 0.03 1 104 . 13 ALA HA H 4.28 0.03 1 105 . 13 ALA HB H 1.51 0.03 1 106 . 13 ALA CA C 54.43 0.50 1 107 . 13 ALA CB C 18.27 0.50 1 108 . 13 ALA N N 123.78 0.50 1 109 . 14 ASN H H 7.64 0.03 1 110 . 14 ASN HA H 4.71 0.03 1 111 . 14 ASN HB2 H 3.27 0.03 1 112 . 14 ASN HB3 H 2.81 0.03 1 113 . 14 ASN HD21 H 7.75 0.03 1 114 . 14 ASN HD22 H 7.32 0.03 1 115 . 14 ASN CA C 52.05 0.50 1 116 . 14 ASN CB C 37.60 0.50 1 117 . 14 ASN N N 111.32 0.50 1 118 . 14 ASN ND2 N 113.83 0.50 1 119 . 15 SER H H 7.58 0.03 1 120 . 15 SER HA H 5.21 0.03 1 121 . 15 SER HB2 H 3.92 0.03 1 122 . 15 SER HB3 H 3.60 0.03 1 123 . 15 SER CA C 59.51 0.50 1 124 . 15 SER CB C 66.20 0.50 1 125 . 15 SER N N 116.51 0.50 1 126 . 16 LYS H H 8.56 0.03 1 127 . 16 LYS HA H 4.71 0.03 1 128 . 16 LYS HB2 H 1.56 0.03 1 129 . 16 LYS HB3 H 1.56 0.03 1 130 . 16 LYS HG2 H 1.36 0.03 1 131 . 16 LYS HG3 H 1.36 0.03 1 132 . 16 LYS HD2 H 1.80 0.03 1 133 . 16 LYS HD3 H 1.80 0.03 1 134 . 16 LYS HE2 H 2.99 0.03 1 135 . 16 LYS HE3 H 2.99 0.03 1 136 . 16 LYS CA C 54.78 0.50 1 137 . 16 LYS CB C 36.35 0.50 1 138 . 16 LYS CG C 25.03 0.50 1 139 . 16 LYS CD C 36.33 0.50 1 140 . 16 LYS CE C 42.26 0.50 1 141 . 16 LYS N N 121.18 0.50 1 142 . 17 CYS H H 8.87 0.03 1 143 . 17 CYS HA H 5.27 0.03 1 144 . 17 CYS HB2 H 3.11 0.03 1 145 . 17 CYS HB3 H 3.11 0.03 1 146 . 17 CYS CA C 55.76 0.50 1 147 . 17 CYS CB C 44.58 0.50 1 148 . 17 CYS N N 123.02 0.50 1 149 . 18 GLU H H 8.94 0.03 1 150 . 18 GLU HA H 4.72 0.03 1 151 . 18 GLU HB2 H 2.11 0.03 1 152 . 18 GLU HB3 H 2.11 0.03 1 153 . 18 GLU HG2 H 2.33 0.03 1 154 . 18 GLU HG3 H 2.33 0.03 1 155 . 18 GLU CA C 55.92 0.50 1 156 . 18 GLU CB C 34.28 0.50 1 157 . 18 GLU CG C 36.37 0.50 1 158 . 18 GLU N N 126.69 0.50 1 159 . 19 LYS H H 8.29 0.03 1 160 . 19 LYS HA H 4.29 0.03 1 161 . 19 LYS HB2 H 1.41 0.03 1 162 . 19 LYS HB3 H 1.41 0.03 1 163 . 19 LYS CA C 60.99 0.50 1 164 . 19 LYS CB C 38.79 0.50 1 165 . 19 LYS N N 125.39 0.50 1 166 . 20 SER H H 8.30 0.03 1 167 . 20 SER HA H 4.55 0.03 1 168 . 20 SER HB2 H 3.86 0.03 1 169 . 20 SER HB3 H 3.86 0.03 1 170 . 20 SER CA C 58.19 0.50 1 171 . 20 SER CB C 64.10 0.50 1 172 . 20 SER N N 119.45 0.50 1 173 . 21 THR H H 8.18 0.03 1 174 . 21 THR HA H 4.45 0.03 1 175 . 21 THR HB H 3.83 0.03 1 176 . 21 THR HG2 H 1.17 0.03 1 177 . 21 THR CA C 61.87 0.50 1 178 . 21 THR CB C 69.84 0.50 1 179 . 21 THR N N 115.61 0.50 1 180 . 22 LEU H H 8.39 0.03 1 181 . 22 LEU HA H 4.01 0.03 1 182 . 22 LEU HB2 H 0.84 0.03 1 183 . 22 LEU HB3 H 0.84 0.03 1 184 . 22 LEU CA C 55.69 0.50 1 185 . 22 LEU CB C 41.63 0.50 1 186 . 22 LEU N N 111.22 0.50 1 187 . 23 THR H H 8.22 0.03 1 188 . 23 THR HA H 4.68 0.03 1 189 . 23 THR HB H 4.39 0.03 1 190 . 23 THR CA C 61.09 0.50 1 191 . 23 THR CB C 69.72 0.50 1 192 . 23 THR N N 118.62 0.50 1 193 . 24 ASN H H 8.58 0.03 1 194 . 24 ASN HA H 4.56 0.03 1 195 . 24 ASN HB2 H 3.09 0.03 1 196 . 24 ASN HB3 H 2.90 0.03 1 197 . 24 ASN HD21 H 7.69 0.03 1 198 . 24 ASN HD22 H 6.83 0.03 1 199 . 24 ASN CA C 54.45 0.50 1 200 . 24 ASN CB C 36.76 0.50 1 201 . 24 ASN N N 123.09 0.50 1 202 . 24 ASN ND2 N 112.69 0.50 1 203 . 25 CYS H H 8.46 0.03 1 204 . 25 CYS HA H 5.73 0.03 1 205 . 25 CYS HB2 H 3.15 0.03 1 206 . 25 CYS HB3 H 2.19 0.03 1 207 . 25 CYS CA C 55.52 0.50 1 208 . 25 CYS CB C 49.41 0.50 1 209 . 25 CYS N N 112.20 0.50 1 210 . 26 TYR H H 8.14 0.03 1 211 . 26 TYR HA H 4.83 0.03 1 212 . 26 TYR HB2 H 2.87 0.03 1 213 . 26 TYR HB3 H 2.87 0.03 1 214 . 26 TYR HD1 H 7.01 0.03 3 215 . 26 TYR HE1 H 6.72 0.03 3 216 . 26 TYR CA C 57.69 0.50 1 217 . 26 TYR CB C 40.80 0.50 1 218 . 26 TYR N N 122.94 0.50 1 219 . 27 VAL H H 8.62 0.03 1 220 . 27 VAL HA H 4.72 0.03 1 221 . 27 VAL HB H 2.13 0.03 1 222 . 27 VAL HG1 H 0.63 0.03 1 223 . 27 VAL HG2 H 1.00 0.03 1 224 . 27 VAL CA C 61.95 0.50 1 225 . 27 VAL CB C 34.79 0.50 1 226 . 27 VAL CG1 C 20.87 0.50 1 227 . 27 VAL CG2 C 23.01 0.50 1 228 . 27 VAL N N 126.67 0.50 1 229 . 28 ASP H H 8.90 0.03 1 230 . 28 ASP HA H 5.21 0.03 1 231 . 28 ASP HB2 H 2.75 0.03 1 232 . 28 ASP HB3 H 2.50 0.03 1 233 . 28 ASP CA C 53.10 0.50 1 234 . 28 ASP CB C 45.28 0.50 1 235 . 28 ASP N N 127.01 0.50 1 236 . 29 LYS H H 8.46 0.03 1 237 . 29 LYS HA H 3.68 0.03 1 238 . 29 LYS HB2 H 2.01 0.03 1 239 . 29 LYS HB3 H 1.70 0.03 1 240 . 29 LYS HG2 H 1.44 0.03 1 241 . 29 LYS HG3 H 1.36 0.03 1 242 . 29 LYS HD2 H 1.66 0.03 1 243 . 29 LYS HD3 H 1.66 0.03 1 244 . 29 LYS HE2 H 2.99 0.03 1 245 . 29 LYS HE3 H 2.99 0.03 1 246 . 29 LYS CA C 57.05 0.50 1 247 . 29 LYS CB C 31.18 0.50 1 248 . 29 LYS CG C 25.33 0.50 1 249 . 29 LYS CD C 29.59 0.50 1 250 . 29 LYS CE C 42.11 0.50 1 251 . 29 LYS N N 128.53 0.50 1 252 . 30 SER H H 8.04 0.03 1 253 . 30 SER HA H 5.56 0.03 1 254 . 30 SER HB2 H 3.91 0.03 1 255 . 30 SER HB3 H 3.32 0.03 1 256 . 30 SER CA C 58.50 0.50 1 257 . 30 SER CB C 69.03 0.50 1 258 . 30 SER N N 112.21 0.50 1 259 . 31 GLU H H 9.18 0.03 1 260 . 31 GLU HA H 4.79 0.03 1 261 . 31 GLU HB2 H 2.07 0.03 1 262 . 31 GLU HB3 H 1.93 0.03 1 263 . 31 GLU HG2 H 2.25 0.03 1 264 . 31 GLU HG3 H 2.08 0.03 1 265 . 31 GLU CA C 55.39 0.50 1 266 . 31 GLU CB C 32.52 0.50 1 267 . 31 GLU CG C 36.15 0.50 1 268 . 31 GLU N N 121.77 0.50 1 269 . 32 VAL H H 8.16 0.03 1 270 . 32 VAL HA H 4.44 0.03 1 271 . 32 VAL HB H 2.09 0.03 1 272 . 32 VAL HG1 H 0.88 0.03 1 273 . 32 VAL HG2 H 1.02 0.03 1 274 . 32 VAL CA C 61.06 0.50 1 275 . 32 VAL CB C 34.13 0.50 1 276 . 32 VAL CG1 C 21.42 0.50 1 277 . 32 VAL CG2 C 20.92 0.50 1 278 . 32 VAL N N 124.00 0.50 1 279 . 33 TYR H H 8.83 0.03 1 280 . 33 TYR HA H 5.67 0.03 1 281 . 33 TYR HB2 H 3.12 0.03 1 282 . 33 TYR HB3 H 2.98 0.03 1 283 . 33 TYR HD1 H 7.04 0.03 3 284 . 33 TYR HE1 H 6.69 0.03 3 285 . 33 TYR CA C 55.87 0.50 1 286 . 33 TYR CB C 41.41 0.50 1 287 . 33 TYR N N 124.95 0.50 1 288 . 34 GLY H H 8.17 0.03 1 289 . 34 GLY HA2 H 4.48 0.03 1 290 . 34 GLY HA3 H 3.81 0.03 1 291 . 34 GLY CA C 48.80 0.50 1 292 . 34 GLY N N 118.93 0.50 1 293 . 35 THR H H 8.60 0.03 1 294 . 35 THR HA H 5.49 0.03 1 295 . 35 THR HB H 3.65 0.03 1 296 . 35 THR HG2 H 0.92 0.03 1 297 . 35 THR CA C 62.69 0.50 1 298 . 35 THR CB C 12.65 0.50 1 299 . 35 THR CG2 C 20.05 0.50 1 300 . 35 THR N N 117.99 0.50 1 301 . 36 THR H H 8.38 0.03 1 302 . 36 THR HA H 4.76 0.03 1 303 . 36 THR HB H 4.18 0.03 1 304 . 36 THR HG2 H 1.15 0.03 1 305 . 36 THR CA C 62.16 0.50 1 306 . 36 THR CB C 60.19 0.50 1 307 . 36 THR CG2 C 21.70 0.50 1 308 . 36 THR N N 119.15 0.50 1 309 . 37 CYS H H 8.28 0.03 1 310 . 37 CYS HA H 4.29 0.03 1 311 . 37 CYS HB2 H 1.88 0.03 1 312 . 37 CYS HB3 H 0.89 0.03 1 313 . 37 CYS CA C 60.95 0.50 1 314 . 37 CYS CB C 38.91 0.50 1 315 . 37 CYS N N 124.17 0.50 1 316 . 38 THR H H 8.30 0.03 1 317 . 38 THR HA H 4.50 0.03 1 318 . 38 THR HB H 4.24 0.03 1 319 . 38 THR CA C 61.35 0.50 1 320 . 38 THR CB C 70.81 0.50 1 321 . 38 THR N N 118.49 0.50 1 322 . 39 GLY H H 9.34 0.03 1 323 . 39 GLY HA2 H 4.37 0.03 1 324 . 39 GLY HA3 H 4.07 0.03 1 325 . 39 GLY CA C 48.66 0.50 1 326 . 39 GLY N N 120.24 0.50 1 327 . 40 SER H H 7.31 0.03 1 328 . 40 SER HA H 5.58 0.03 1 329 . 40 SER HB2 H 4.01 0.03 1 330 . 40 SER HB3 H 3.85 0.03 1 331 . 40 SER CA C 57.24 0.50 1 332 . 40 SER CB C 68.64 0.50 1 333 . 40 SER N N 111.27 0.50 1 334 . 41 ARG H H 8.68 0.03 1 335 . 41 ARG HA H 5.48 0.03 1 336 . 41 ARG HB2 H 1.78 0.03 1 337 . 41 ARG HB3 H 1.64 0.03 1 338 . 41 ARG HG2 H 1.61 0.03 1 339 . 41 ARG HG3 H 1.51 0.03 1 340 . 41 ARG HD2 H 3.03 0.03 1 341 . 41 ARG HD3 H 2.87 0.03 1 342 . 41 ARG CA C 54.24 0.50 1 343 . 41 ARG CB C 33.63 0.50 1 344 . 41 ARG CG C 28.23 0.50 1 345 . 41 ARG CD C 43.32 0.50 1 346 . 41 ARG N N 121.81 0.50 1 347 . 42 PHE H H 9.25 0.03 1 348 . 42 PHE HA H 5.74 0.03 1 349 . 42 PHE HB2 H 3.24 0.03 1 350 . 42 PHE HB3 H 3.24 0.03 1 351 . 42 PHE HD1 H 7.07 0.03 3 352 . 42 PHE HE1 H 7.17 0.03 3 353 . 42 PHE HZ H 6.79 0.03 1 354 . 42 PHE CA C 52.20 0.50 1 355 . 42 PHE CB C 41.52 0.50 1 356 . 42 PHE N N 124.60 0.50 1 357 . 43 ASP H H 8.16 0.03 1 358 . 43 ASP HA H 5.60 0.03 1 359 . 43 ASP HB2 H 2.75 0.03 1 360 . 43 ASP HB3 H 2.51 0.03 1 361 . 43 ASP CA C 52.73 0.50 1 362 . 43 ASP CB C 43.33 0.50 1 363 . 43 ASP N N 122.93 0.50 1 364 . 44 GLY H H 7.82 0.03 1 365 . 44 GLY HA2 H 4.41 0.03 1 366 . 44 GLY HA3 H 3.87 0.03 1 367 . 44 GLY CA C 48.58 0.50 1 368 . 44 GLY N N 114.88 0.50 1 369 . 45 VAL H H 7.74 0.03 1 370 . 45 VAL HA H 4.36 0.03 1 371 . 45 VAL HB H 1.57 0.03 1 372 . 45 VAL HG1 H 0.34 0.03 1 373 . 45 VAL HG2 H 0.50 0.03 1 374 . 45 VAL CA C 60.39 0.50 1 375 . 45 VAL CB C 36.06 0.50 1 376 . 45 VAL CG1 C 21.64 0.50 1 377 . 45 VAL CG2 C 21.84 0.50 1 378 . 45 VAL N N 118.24 0.50 1 379 . 46 THR H H 8.80 0.03 1 380 . 46 THR HA H 5.17 0.03 1 381 . 46 THR HB H 4.09 0.03 1 382 . 46 THR HG2 H 1.29 0.03 1 383 . 46 THR CA C 62.28 0.50 1 384 . 46 THR CB C 69.79 0.50 1 385 . 46 THR CG2 C 20.76 0.50 1 386 . 46 THR N N 124.32 0.50 1 387 . 47 ILE H H 9.12 0.03 1 388 . 47 ILE HA H 5.51 0.03 1 389 . 47 ILE HB H 1.08 0.03 1 390 . 47 ILE HG12 H 0.72 0.03 1 391 . 47 ILE HG13 H 0.72 0.03 1 392 . 47 ILE HG2 H 0.88 0.03 1 393 . 47 ILE HD1 H 0.40 0.03 1 394 . 47 ILE CA C 57.72 0.50 1 395 . 47 ILE CB C 41.26 0.50 1 396 . 47 ILE CG1 C 15.54 0.50 1 397 . 47 ILE CD1 C 13.31 0.50 1 398 . 47 ILE N N 126.21 0.50 1 399 . 48 THR H H 8.40 0.03 1 400 . 48 THR HA H 5.92 0.03 1 401 . 48 THR HB H 4.07 0.03 1 402 . 48 THR HG2 H 1.34 0.03 1 403 . 48 THR CA C 59.28 0.50 1 404 . 48 THR CB C 71.05 0.50 1 405 . 48 THR CG2 C 21.62 0.50 1 406 . 48 THR N N 119.87 0.50 1 407 . 49 THR H H 8.69 0.03 1 408 . 49 THR HA H 4.38 0.03 1 409 . 49 THR HB H 4.46 0.03 1 410 . 49 THR HG2 H 1.44 0.03 1 411 . 49 THR CA C 61.94 0.50 1 412 . 49 THR CB C 67.49 0.50 1 413 . 49 THR CG2 C 23.48 0.50 1 414 . 49 THR N N 122.47 0.50 1 415 . 50 SER H H 7.46 0.03 1 416 . 50 SER HA H 5.55 0.03 1 417 . 50 SER HB2 H 3.26 0.03 1 418 . 50 SER HB3 H 3.26 0.03 1 419 . 50 SER CA C 58.30 0.50 1 420 . 50 SER CB C 68.80 0.50 1 421 . 50 SER N N 113.19 0.50 1 422 . 51 THR H H 8.76 0.03 1 423 . 51 THR HA H 5.34 0.03 1 424 . 51 THR HB H 4.00 0.03 1 425 . 51 THR HG2 H 1.19 0.03 1 426 . 51 THR CA C 61.75 0.50 1 427 . 51 THR CB C 72.03 0.50 1 428 . 51 THR CG2 C 22.70 0.50 1 429 . 51 THR N N 117.54 0.50 1 430 . 52 SER H H 8.86 0.03 1 431 . 52 SER HA H 5.67 0.03 1 432 . 52 SER HB2 H 3.91 0.03 1 433 . 52 SER HB3 H 3.45 0.03 1 434 . 52 SER CA C 56.07 0.50 1 435 . 52 SER CB C 65.77 0.50 1 436 . 52 SER N N 118.52 0.50 1 437 . 53 THR H H 9.33 0.03 1 438 . 53 THR HA H 5.61 0.03 1 439 . 53 THR HB H 4.02 0.03 1 440 . 53 THR HG2 H 1.25 0.03 1 441 . 53 THR CA C 60.55 0.50 1 442 . 53 THR CB C 70.83 0.50 1 443 . 53 THR CG2 C 21.83 0.50 1 444 . 53 THR N N 126.78 0.50 1 445 . 54 GLY H H 8.63 0.03 1 446 . 54 GLY HA2 H 4.46 0.03 1 447 . 54 GLY HA3 H 4.07 0.03 1 448 . 54 GLY CA C 49.02 0.50 1 449 . 54 GLY N N 118.39 0.50 1 450 . 55 SER H H 7.96 0.03 1 451 . 55 SER HA H 5.29 0.03 1 452 . 55 SER HB2 H 3.77 0.03 1 453 . 55 SER HB3 H 3.58 0.03 1 454 . 55 SER CA C 58.26 0.50 1 455 . 55 SER CB C 67.17 0.50 1 456 . 55 SER N N 111.74 0.50 1 457 . 56 ARG H H 9.53 0.03 1 458 . 56 ARG HA H 5.14 0.03 1 459 . 56 ARG HB2 H 1.84 0.03 1 460 . 56 ARG HB3 H 1.67 0.03 1 461 . 56 ARG HG2 H 1.49 0.03 1 462 . 56 ARG HG3 H 1.37 0.03 1 463 . 56 ARG HD2 H 3.11 0.03 1 464 . 56 ARG HD3 H 3.11 0.03 1 465 . 56 ARG CA C 55.73 0.50 1 466 . 56 ARG CB C 30.96 0.50 1 467 . 56 ARG CG C 28.18 0.50 1 468 . 56 ARG CD C 43.78 0.50 1 469 . 56 ARG N N 126.75 0.50 1 470 . 57 ILE H H 9.13 0.03 1 471 . 57 ILE HA H 4.78 0.03 1 472 . 57 ILE HB H 1.80 0.03 1 473 . 57 ILE HG12 H 0.92 0.03 1 474 . 57 ILE HG13 H 0.92 0.03 1 475 . 57 ILE HG2 H 1.20 0.03 1 476 . 57 ILE HD1 H 0.68 0.03 1 477 . 57 ILE CA C 60.80 0.50 1 478 . 57 ILE CB C 40.80 0.50 1 479 . 57 ILE CG1 C 14.24 0.50 1 480 . 57 ILE CG2 C 26.31 0.50 1 481 . 57 ILE CD1 C 20.34 0.50 1 482 . 57 ILE N N 124.61 0.50 1 483 . 58 SER H H 8.70 0.03 1 484 . 58 SER HA H 5.68 0.03 1 485 . 58 SER HB2 H 3.88 0.03 1 486 . 58 SER HB3 H 3.71 0.03 1 487 . 58 SER CA C 56.72 0.50 1 488 . 58 SER CB C 66.38 0.50 1 489 . 58 SER N N 121.22 0.50 1 490 . 59 GLY H H 8.56 0.03 1 491 . 59 GLY HA2 H 4.42 0.03 1 492 . 59 GLY HA3 H 3.88 0.03 1 493 . 59 GLY CA C 43.59 0.50 1 494 . 59 GLY N N 111.31 0.50 1 495 . 60 PRO HA H 4.98 0.03 1 496 . 60 PRO HB2 H 2.49 0.03 1 497 . 60 PRO HB3 H 2.12 0.03 1 498 . 60 PRO HG2 H 1.92 0.03 1 499 . 60 PRO HG3 H 1.92 0.03 1 500 . 60 PRO HD2 H 3.60 0.03 1 501 . 60 PRO HD3 H 3.52 0.03 1 502 . 60 PRO CA C 63.70 0.50 1 503 . 60 PRO CB C 34.60 0.50 1 504 . 60 PRO CG C 25.27 0.50 1 505 . 60 PRO CD C 50.65 0.50 1 506 . 61 GLY H H 9.05 0.03 1 507 . 61 GLY HA2 H 3.99 0.03 1 508 . 61 GLY HA3 H 3.76 0.03 1 509 . 61 GLY CA C 46.36 0.50 1 510 . 61 GLY N N 108.99 0.50 1 511 . 62 CYS H H 7.34 0.03 1 512 . 62 CYS HA H 5.08 0.03 1 513 . 62 CYS HB2 H 3.35 0.03 1 514 . 62 CYS HB3 H 2.58 0.03 1 515 . 62 CYS CA C 55.22 0.50 1 516 . 62 CYS CB C 37.78 0.50 1 517 . 62 CYS N N 117.50 0.50 1 518 . 63 LYS H H 9.45 0.03 1 519 . 63 LYS HA H 5.31 0.03 1 520 . 63 LYS HB2 H 1.76 0.03 1 521 . 63 LYS HB3 H 1.76 0.03 1 522 . 63 LYS HG2 H 1.39 0.03 1 523 . 63 LYS HG3 H 1.31 0.03 1 524 . 63 LYS HD2 H 1.63 0.03 1 525 . 63 LYS HD3 H 1.63 0.03 1 526 . 63 LYS HE2 H 2.91 0.03 1 527 . 63 LYS HE3 H 2.91 0.03 1 528 . 63 LYS CA C 55.39 0.50 1 529 . 63 LYS CB C 35.19 0.50 1 530 . 63 LYS CG C 24.96 0.50 1 531 . 63 LYS CD C 29.47 0.50 1 532 . 63 LYS CE C 42.25 0.50 1 533 . 63 LYS N N 110.10 0.50 1 534 . 64 ILE H H 8.79 0.03 1 535 . 64 ILE HA H 5.00 0.03 1 536 . 64 ILE HB H 1.32 0.03 1 537 . 64 ILE HG12 H 0.88 0.03 1 538 . 64 ILE HG13 H 0.88 0.03 1 539 . 64 ILE HG2 H 1.11 0.03 1 540 . 64 ILE HD1 H 0.86 0.03 1 541 . 64 ILE CA C 60.21 0.50 1 542 . 64 ILE CB C 43.04 0.50 1 543 . 64 ILE CG1 C 17.69 0.50 1 544 . 64 ILE CG2 C 28.99 0.50 1 545 . 64 ILE CD1 C 16.36 0.50 1 546 . 64 ILE N N 123.83 0.50 1 547 . 65 SER H H 9.14 0.03 1 548 . 65 SER HA H 5.31 0.03 1 549 . 65 SER HB2 H 3.71 0.03 1 550 . 65 SER HB3 H 3.71 0.03 1 551 . 65 SER CA C 56.03 0.50 1 552 . 65 SER CB C 65.15 0.50 1 553 . 65 SER N N 122.43 0.50 1 554 . 66 THR H H 7.87 0.03 1 555 . 66 THR HA H 4.25 0.03 1 556 . 66 THR HB H 4.57 0.03 1 557 . 66 THR HG2 H 1.27 0.03 1 558 . 66 THR CA C 61.73 0.50 1 559 . 66 THR CB C 65.33 0.50 1 560 . 66 THR CG2 C 23.71 0.50 1 561 . 66 THR N N 117.44 0.50 1 562 . 67 CYS H H 8.29 0.03 1 563 . 67 CYS HA H 5.29 0.03 1 564 . 67 CYS HB2 H 2.84 0.03 1 565 . 67 CYS HB3 H 2.45 0.03 1 566 . 67 CYS CA C 55.67 0.50 1 567 . 67 CYS CB C 25.70 0.50 1 568 . 67 CYS N N 116.34 0.50 1 569 . 68 ILE H H 8.29 0.03 1 570 . 68 ILE HA H 4.68 0.03 1 571 . 68 ILE CA C 57.61 0.50 1 572 . 68 ILE CB C 39.66 0.50 1 573 . 68 ILE N N 120.96 0.50 1 574 . 69 ILE H H 8.16 0.03 1 575 . 69 ILE HA H 4.59 0.03 1 576 . 69 ILE HB H 2.66 0.03 1 577 . 69 ILE CA C 54.22 0.50 1 578 . 69 ILE CB C 41.23 0.50 1 579 . 69 ILE N N 122.20 0.50 1 580 . 70 THR H H 9.35 0.03 1 581 . 70 THR HA H 5.52 0.03 1 582 . 70 THR HB H 4.04 0.03 1 583 . 70 THR HG2 H 1.26 0.03 1 584 . 70 THR CA C 61.29 0.50 1 585 . 70 THR CB C 58.83 0.50 1 586 . 70 THR CG2 C 22.04 0.50 1 587 . 70 THR N N 127.49 0.50 1 588 . 71 GLY H H 8.77 0.03 1 589 . 71 GLY HA2 H 4.30 0.03 1 590 . 71 GLY HA3 H 3.88 0.03 1 591 . 71 GLY CA C 47.54 0.50 1 592 . 71 GLY N N 118.41 0.50 1 593 . 72 GLY H H 8.61 0.03 1 594 . 72 GLY HA2 H 4.07 0.03 1 595 . 72 GLY HA3 H 3.19 0.03 1 596 . 72 GLY CA C 44.92 0.50 1 597 . 72 GLY N N 125.00 0.50 1 598 . 73 VAL H H 7.45 0.03 1 599 . 73 VAL HA H 4.34 0.03 1 600 . 73 VAL HB H 2.16 0.03 1 601 . 73 VAL HG1 H 0.86 0.03 1 602 . 73 VAL HG2 H 0.61 0.03 1 603 . 73 VAL CA C 59.35 0.50 1 604 . 73 VAL CB C 34.29 0.50 1 605 . 73 VAL CG1 C 20.60 0.50 1 606 . 73 VAL CG2 C 18.15 0.50 1 607 . 73 VAL N N 119.69 0.50 1 608 . 74 PRO HA H 4.51 0.03 1 609 . 74 PRO HB2 H 2.15 0.03 1 610 . 74 PRO HB3 H 2.04 0.03 1 611 . 74 PRO HD2 H 3.93 0.03 1 612 . 74 PRO HD3 H 3.66 0.03 1 613 . 74 PRO CA C 63.05 0.50 1 614 . 74 PRO CB C 27.66 0.50 1 615 . 75 ALA H H 8.33 0.03 1 616 . 75 ALA HA H 4.58 0.03 1 617 . 75 ALA HB H 1.37 0.03 1 618 . 75 ALA CA C 50.41 0.50 1 619 . 75 ALA CB C 18.25 0.50 1 620 . 75 ALA N N 125.36 0.50 1 621 . 76 PRO HA H 4.51 0.03 1 622 . 76 PRO HB2 H 2.17 0.03 1 623 . 76 PRO HB3 H 2.01 0.03 1 624 . 76 PRO HD2 H 3.93 0.03 1 625 . 76 PRO HD3 H 3.66 0.03 1 626 . 76 PRO CA C 63.08 0.50 1 627 . 76 PRO CB C 31.22 0.50 1 628 . 76 PRO CD C 50.47 0.50 1 629 . 77 SER H H 8.13 0.03 1 630 . 77 SER HA H 4.56 0.03 1 631 . 77 SER HB2 H 4.25 0.03 1 632 . 77 SER HB3 H 3.73 0.03 1 633 . 77 SER CA C 57.50 0.50 1 634 . 77 SER CB C 64.83 0.50 1 635 . 77 SER N N 118.33 0.50 1 636 . 78 ALA H H 8.98 0.03 1 637 . 78 ALA HA H 4.25 0.03 1 638 . 78 ALA HB H 1.48 0.03 1 639 . 78 ALA CA C 54.48 0.50 1 640 . 78 ALA CB C 18.43 0.50 1 641 . 78 ALA N N 128.83 0.50 1 642 . 79 ALA H H 7.92 0.03 1 643 . 79 ALA HA H 4.30 0.03 1 644 . 79 ALA HB H 1.45 0.03 1 645 . 79 ALA CA C 52.48 0.50 1 646 . 79 ALA CB C 20.13 0.50 1 647 . 79 ALA N N 117.81 0.50 1 648 . 80 CYS H H 7.06 0.03 1 649 . 80 CYS HA H 5.02 0.03 1 650 . 80 CYS HB2 H 3.70 0.03 1 651 . 80 CYS HB3 H 2.86 0.03 1 652 . 80 CYS CA C 55.74 0.50 1 653 . 80 CYS CB C 38.18 0.50 1 654 . 80 CYS N N 115.93 0.50 1 655 . 81 LYS H H 8.97 0.03 1 656 . 81 LYS HA H 4.76 0.03 1 657 . 81 LYS HB2 H 1.78 0.03 1 658 . 81 LYS HB3 H 1.78 0.03 1 659 . 81 LYS HG2 H 1.65 0.03 1 660 . 81 LYS HG3 H 1.65 0.03 1 661 . 81 LYS HD2 H 1.45 0.03 1 662 . 81 LYS HD3 H 1.45 0.03 1 663 . 81 LYS HE2 H 2.97 0.03 1 664 . 81 LYS HE3 H 2.97 0.03 1 665 . 81 LYS CA C 54.70 0.50 1 666 . 81 LYS CB C 34.25 0.50 1 667 . 81 LYS CG C 28.95 0.50 1 668 . 81 LYS CD C 24.05 0.50 1 669 . 81 LYS CE C 42.37 0.50 1 670 . 81 LYS N N 109.80 0.50 1 671 . 82 ILE H H 8.34 0.03 1 672 . 82 ILE HA H 4.95 0.03 1 673 . 82 ILE HB H 1.67 0.03 1 674 . 82 ILE HG12 H 1.07 0.03 1 675 . 82 ILE HG13 H 1.07 0.03 1 676 . 82 ILE HG2 H 1.79 0.03 1 677 . 82 ILE HD1 H 0.87 0.03 1 678 . 82 ILE CA C 60.66 0.50 1 679 . 82 ILE CB C 42.71 0.50 1 680 . 82 ILE CG1 C 18.71 0.50 1 681 . 82 ILE CG2 C 28.89 0.50 1 682 . 82 ILE CD1 C 14.44 0.50 1 683 . 82 ILE N N 124.28 0.50 1 684 . 83 SER H H 8.95 0.03 1 685 . 83 SER HA H 4.75 0.03 1 686 . 83 SER HB2 H 3.84 0.03 1 687 . 83 SER HB3 H 3.84 0.03 1 688 . 83 SER CA C 57.54 0.50 1 689 . 83 SER CB C 65.08 0.50 1 690 . 83 SER N N 121.03 0.50 1 691 . 84 GLY H H 8.83 0.03 1 692 . 84 GLY HA2 H 4.17 0.03 1 693 . 84 GLY HA3 H 3.87 0.03 1 694 . 84 GLY CA C 46.86 0.50 1 695 . 84 GLY N N 113.16 0.50 1 696 . 85 CYS H H 7.72 0.03 1 697 . 85 CYS HA H 5.07 0.03 1 698 . 85 CYS HB2 H 2.42 0.03 1 699 . 85 CYS HB3 H 2.09 0.03 1 700 . 85 CYS CA C 55.56 0.50 1 701 . 85 CYS CB C 48.00 0.50 1 702 . 85 CYS N N 115.59 0.50 1 703 . 86 THR H H 8.71 0.03 1 704 . 86 THR HA H 4.42 0.03 1 705 . 86 THR HB H 4.00 0.03 1 706 . 86 THR HG2 H 1.21 0.03 1 707 . 86 THR CA C 61.92 0.50 1 708 . 86 THR CB C 70.53 0.50 1 709 . 86 THR CG2 C 21.39 0.50 1 710 . 86 THR N N 118.17 0.50 1 711 . 87 PHE H H 8.91 0.03 1 712 . 87 PHE HA H 5.62 0.03 1 713 . 87 PHE HB2 H 3.41 0.03 1 714 . 87 PHE HB3 H 2.91 0.03 1 715 . 87 PHE HD1 H 7.20 0.03 3 716 . 87 PHE HE1 H 7.04 0.03 3 717 . 87 PHE CA C 57.22 0.50 1 718 . 87 PHE CB C 44.77 0.50 1 719 . 87 PHE N N 123.11 0.50 1 720 . 88 SER H H 9.00 0.03 1 721 . 88 SER HA H 4.82 0.03 1 722 . 88 SER HB2 H 4.04 0.03 1 723 . 88 SER HB3 H 4.04 0.03 1 724 . 88 SER CA C 58.01 0.50 1 725 . 88 SER CB C 65.81 0.50 1 726 . 88 SER N N 112.77 0.50 1 727 . 89 ALA H H 8.81 0.03 1 728 . 89 ALA HA H 4.31 0.03 1 729 . 89 ALA HB H 1.48 0.03 1 730 . 89 ALA CA C 53.23 0.50 1 731 . 89 ALA CB C 18.96 0.50 1 732 . 89 ALA N N 125.74 0.50 1 733 . 90 ASN H H 7.64 0.03 1 734 . 90 ASN HA H 4.67 0.03 1 735 . 90 ASN HB2 H 2.49 0.03 1 736 . 90 ASN HB3 H 2.08 0.03 1 737 . 90 ASN HD21 H 7.09 0.03 1 738 . 90 ASN HD22 H 6.59 0.03 1 739 . 90 ASN CA C 53.93 0.50 1 740 . 90 ASN CB C 42.35 0.50 1 741 . 90 ASN N N 124.78 0.50 1 742 . 90 ASN ND2 N 111.68 0.50 1 stop_ save_