data_4450 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 15N and 13C Resonnace assignment of the Inhibitory Prodomain of Human Furin ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharjya Surajit . . 2 Xu Ping . . 3 Ni Feng . . stop_ _BMRB_accession_number 4450 _BMRB_flat_file_name bmr4450.str _Entry_type new _Submission_date 1999-11-03 _Accession_date 1999-11-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 454 '13C chemical shifts' 274 '15N chemical shifts' 85 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the inhibitory prodomain of human furin ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharjya Surajit . . 2 Xu Ping . . 3 Ni Feng . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 16 _Journal_issue 3 _Page_first 275 _Page_last 276 _Year 2000 loop_ _Keyword Prodomain Furin 'heteronuclear NMR' stop_ save_ ################################## # Molecular system description # ################################## save_system_pFurin _Saveframe_category molecular_system _Mol_system_name 'Inhibitory Prodomain of Furin' _Abbreviation_common pFurin loop_ _Mol_system_component_name _Mol_label pFurin $pFurin stop_ _System_molecular_weight 12300 _System_physical_state Native _System_oligomer_state Monomer _System_type Simple _System_paramagnetic No _System_thiol_state 'not present' loop_ _Biological_function "Regulation of Furin enzymatic Activity and Transport" stop_ save_ ######################## # Monomeric polymers # ######################## save_pFurin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Prodomain of Furin' _Name_variant . _Abbreviation_common pFurin _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; MASMTGGQQMGRDPQKVFTN TWAVRIPGGPAVANSVARKH GFLXLGQIFGDYYHFWHRGV TKRSLSPHRPRHSRLQREPQ VQWLEQQVAKRRTKRDVAAA LEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 SER 4 MET 5 THR 6 GLY 7 GLY 8 GLN 9 GLN 10 MET 11 GLY 12 ARG 13 ASP 14 PRO 15 GLN 16 LYS 17 VAL 18 PHE 19 THR 20 ASN 21 THR 22 TRP 23 ALA 24 VAL 25 ARG 26 ILE 27 PRO 28 GLY 29 GLY 30 PRO 31 ALA 32 VAL 33 ALA 34 ASN 35 SER 36 VAL 37 ALA 38 ARG 39 LYS 40 HIS 41 GLY 42 PHE 43 LEU 44 BASP 45 LEU 46 GLY 47 GLN 48 ILE 49 PHE 50 GLY 51 ASP 52 TYR 53 TYR 54 HIS 55 PHE 56 TRP 57 HIS 58 ARG 59 GLY 60 VAL 61 THR 62 LYS 63 ARG 64 SER 65 LEU 66 SER 67 PRO 68 HIS 69 ARG 70 PRO 71 ARG 72 HIS 73 SER 74 ARG 75 LEU 76 GLN 77 ARG 78 GLU 79 PRO 80 GLN 81 VAL 82 GLN 83 TRP 84 LEU 85 GLU 86 GLN 87 GLN 88 VAL 89 ALA 90 LYS 91 ARG 92 ARG 93 THR 94 LYS 95 ARG 96 ASP 97 VAL 98 ALA 99 ALA 100 ALA 101 LEU 102 GLU 103 HIS 104 HIS 105 HIS 106 HIS 107 HIS 108 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4449 "antifreeze protein type III" 100.00 134 100.00 100.00 2.10e-87 PDB 1C89 "Nmr Structure Of Intramolecular Dimer Antifreeze Protein Rd3, 40 Sa Structures" 100.00 134 100.00 100.00 2.10e-87 PDB 1C8A "Nmr Structure Of Intramolecular Dimer Antifreeze Protein Rd3, 40 Sa Structures" 100.00 134 100.00 100.00 2.10e-87 PRF 2109220B "antifreeze peptide:ISOTYPE=RD3 [Lycodichthys dearborni]" 100.00 134 100.00 100.00 2.10e-87 SP P35753 "RecName: Full=Ice-structuring protein RD3; Short=ISP RD3; AltName: Full=Antifreeze peptide RD3" 100.00 134 100.00 100.00 2.10e-87 stop_ save_ ###################### # Polymer residues # ###################### save_BASP _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'beta linked aspartate' _Abbreviation_common BASP _Name_IUPAC . _Standard_residue_derivative aspartate loop_ _Mol_label _Residue_seq_code $pFurin 44 stop_ _Mol_paramagnetic no loop_ _Atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons H H . . . . N N . . . . HA H . . . . CA C . . . . C C . . . . "O'" O . . . . "O''" O . . . . "H''" H . . . . HB2 H . . . . HB3 H . . . . CB C . . . . CG C . . . . OD1 O . . . . stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name single H N single N H single N CA single HA CA single CA HA single CA N single CA C single CA CB double C "O'" single C "O''" single C CA double "O'" C single "O''" C single "O''" "H''" single "H''" "O''" single HB2 CB single HB3 CB single CB HB2 single CB HB3 single CB CA single CB CG single CG CB double CG OD1 double OD1 CG stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Details single amide pFurin 44 BASP CG pFurin 45 LEU N ; ASN 44 is deamidated, converting it to ASP 44; the CG of ASP 44 is bound to the N of LEU 45 to form a beta-peptide linkage. ; stop_ loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name pFurin 44 BASP OD2 pFurin 45 LEU H stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $pFurin Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Vendor_name $pFurin 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET24b(+) Novagen stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type Solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $pFurin 0.8 mM . . [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type Solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $pFurin 0.8 mM . . '[U-15N; U-13C]' stop_ save_ ############################# # Purity of the molecules # ############################# save_sample_mol_purity _Saveframe_category sample_mol_purity _Sample_label $sample_1 loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $pFurin 98 % 'SDS gel electrophoresis & mass spectrometry' stop_ save_ ############################ # Computer software used # ############################ save_NMR_PIPE _Saveframe_category software _Name NMR-PIPE loop_ _Task 'FID transformations' stop_ save_ save_NMR_View _Saveframe_category software _Name NMR-View loop_ _Task 'spectral analysis' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 2D (1H-15N) HSQC 2D (1H-1H) NOESY 3D (1H-15N) NOESY-HSQC 3D (1H-15N) TOCSY-HSQC 3D HNCA 3D HN(CO)CA 3D HNCACB 3D CBCA(CO)NH 3D HNCO 3D HN(CA)CO 3D H(CCO)NH-TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_set_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.1 n/a temperature 303 1.0 K 'ionic strength' 0.05 0.5 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_set_1 _Saveframe_category chemical_shift_reference 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 . . . 0.101329 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_set_1 _Chem_shift_reference_set_label $chemical_shift_reference_set_1 _Mol_system_component_name pFurin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 ALA HA H 3.11 . 1 2 2 ALA HB H 1.54 . 1 3 2 ALA C C 178.40 . 1 4 2 ALA CA C 51.80 . 1 5 2 ALA CB C 18.86 . 1 6 3 SER H H 8.63 . 1 7 3 SER HA H 4.53 . 1 8 3 SER HB2 H 3.87 . 1 9 3 SER HB3 H 3.87 . 1 10 3 SER C C 177.73 . 1 11 3 SER CA C 58.20 . 1 12 3 SER CB C 63.65 . 1 13 3 SER N N 115.48 . 1 14 4 MET H H 8.59 . 1 15 4 MET HA H 4.60 . 1 16 4 MET HB2 H 2.59 . 1 17 4 MET HB3 H 2.59 . 1 18 4 MET C C 175.67 . 1 19 4 MET CA C 55.60 . 1 20 4 MET CB C 32.89 . 1 21 4 MET N N 122.55 . 1 22 5 THR H H 8.16 . 1 23 5 THR HA H 4.49 . 1 24 5 THR HB H 4.35 . 1 25 5 THR HG2 H 1.18 . 1 26 5 THR C C 177.00 . 1 27 5 THR CA C 61.85 . 1 28 5 THR CB C 69.92 . 1 29 5 THR N N 114.35 . 1 30 6 GLY H H 8.38 . 1 31 6 GLY HA2 H 4.01 . 1 32 6 GLY HA3 H 4.01 . 1 33 6 GLY C C 177.26 . 1 34 6 GLY CA C 45.47 . 1 35 6 GLY N N 110.98 . 1 36 7 GLY H H 8.25 . 1 37 7 GLY HA2 H 3.97 . 1 38 7 GLY HA3 H 3.97 . 1 39 7 GLY C C 177.82 . 1 40 7 GLY CA C 45.33 . 1 41 7 GLY N N 108.37 . 1 42 8 GLN H H 8.25 . 1 43 8 GLN HA H 4.41 . 1 44 8 GLN HB2 H 2.45 . 1 45 8 GLN HB3 H 2.45 . 1 46 8 GLN HG2 H 2.19 . 2 47 8 GLN HG3 H 2.07 . 2 48 8 GLN C C 176.07 . 1 49 8 GLN CA C 56.00 . 1 50 8 GLN CB C 29.05 . 1 51 8 GLN N N 119.50 . 1 52 9 GLN H H 8.44 . 1 53 9 GLN HA H 4.40 . 1 54 9 GLN HB2 H 2.45 . 1 55 9 GLN HB3 H 2.45 . 1 56 9 GLN HG2 H 2.07 . 2 57 9 GLN HG3 H 2.19 . 2 58 9 GLN C C 176.08 . 1 59 9 GLN CA C 55.97 . 1 60 9 GLN CB C 28.97 . 1 61 9 GLN N N 121.09 . 1 62 10 MET H H 8.59 . 1 63 10 MET HA H 4.48 . 1 64 10 MET HB2 H 2.60 . 1 65 10 MET HB3 H 2.60 . 1 66 10 MET C C 175.42 . 1 67 10 MET CA C 55.89 . 1 68 10 MET CB C 32.89 . 1 69 10 MET N N 122.55 . 1 70 11 GLY H H 8.40 . 1 71 11 GLY HA2 H 3.96 . 1 72 11 GLY HA3 H 3.96 . 1 73 11 GLY C C 178.82 . 1 74 11 GLY CA C 45.22 . 1 75 11 GLY N N 109.95 . 1 76 12 ARG H H 8.07 . 1 77 12 ARG HA H 4.34 . 1 78 12 ARG HB2 H 2.37 . 1 79 12 ARG HB3 H 2.37 . 1 80 12 ARG C C 175.42 . 1 81 12 ARG CA C 55.73 . 1 82 12 ARG CB C 30.62 . 1 83 12 ARG N N 119.74 . 1 84 13 ASP H H 8.42 . 1 85 13 ASP HA H 4.98 . 1 86 13 ASP HB2 H 2.87 . 2 87 13 ASP HB3 H 2.69 . 2 88 13 ASP C C 176.00 . 1 89 13 ASP CA C 51.86 . 1 90 13 ASP CB C 40.12 . 1 91 13 ASP N N 121.36 . 1 92 14 PRO HA H 4.40 . 1 93 14 PRO HB2 H 2.00 . 1 94 14 PRO HB3 H 2.00 . 1 95 14 PRO C C 177.16 . 1 96 14 PRO CA C 63.57 . 1 97 14 PRO CB C 31.87 . 1 98 15 GLN H H 8.32 . 1 99 15 GLN HA H 4.25 . 1 100 15 GLN HB2 H 2.32 . 1 101 15 GLN HB3 H 2.32 . 1 102 15 GLN HG2 H 1.80 . 2 103 15 GLN HG3 H 1.60 . 2 104 15 GLN C C 176.00 . 1 105 15 GLN CA C 56.13 . 1 106 15 GLN CB C 28.97 . 1 107 15 GLN N N 118.58 . 1 108 16 LYS H H 8.20 . 1 109 16 LYS HA H 4.24 . 1 110 16 LYS HB2 H 2.28 . 1 111 16 LYS HB3 H 2.28 . 1 112 16 LYS HG2 H 1.39 . 1 113 16 LYS HG3 H 1.39 . 1 114 16 LYS HD2 H 1.66 . 1 115 16 LYS HD3 H 1.66 . 1 116 16 LYS HE2 H 3.05 . 1 117 16 LYS HE3 H 3.05 . 1 118 16 LYS C C 175.65 . 1 119 16 LYS CA C 56.11 . 1 120 16 LYS CB C 32.89 . 1 121 16 LYS N N 122.14 . 1 122 17 VAL H H 8.04 . 1 123 17 VAL HA H 4.17 . 1 124 17 VAL HB H 2.01 . 1 125 17 VAL HG1 H 0.83 . 1 126 17 VAL HG2 H 0.83 . 1 127 17 VAL C C 176.61 . 2 128 17 VAL CA C 61.87 . 1 129 17 VAL CB C 32.19 . 1 130 17 VAL N N 121.22 . 1 131 18 PHE H H 8.38 . 1 132 18 PHE HA H 4.75 . 1 133 18 PHE HB2 H 3.13 . 1 134 18 PHE HB3 H 2.97 . 1 135 18 PHE C C 176.50 . 1 136 18 PHE CA C 57.51 . 1 137 18 PHE CB C 39.86 . 1 138 18 PHE N N 124.22 . 1 139 19 THR H H 8.01 . 1 140 19 THR HA H 4.45 . 1 141 19 THR HB H 4.15 . 1 142 19 THR HG2 H 1.14 . 1 143 19 THR C C 178.32 . 1 144 19 THR CA C 61.51 . 1 145 19 THR CB C 70.13 . 1 146 19 THR N N 115.58 . 1 147 20 ASN H H 8.30 . 1 148 20 ASN HA H 4.64 . 1 149 20 ASN HB2 H 2.65 . 1 150 20 ASN HB3 H 2.65 . 1 151 20 ASN C C 176.77 . 1 152 20 ASN CA C 53.21 . 1 153 20 ASN CB C 38.73 . 1 154 20 ASN N N 120.60 . 1 155 21 THR H H 7.92 . 1 156 21 THR HA H 4.40 . 1 157 21 THR HB H 4.21 . 1 158 21 THR HG2 H 1.57 . 1 159 21 THR C C 177.91 . 1 160 21 THR CA C 62.24 . 1 161 21 THR CB C 69.14 . 1 162 21 THR N N 113.70 . 1 163 22 TRP H H 7.90 . 1 164 22 TRP HA H 4.66 . 1 165 22 TRP HB2 H 3.27 . 1 166 22 TRP HB3 H 3.27 . 1 167 22 TRP C C 176.40 . 1 168 22 TRP CA C 57.15 . 1 169 22 TRP CB C 29.23 . 1 170 22 TRP N N 121.92 . 1 171 23 ALA H H 7.84 . 1 172 23 ALA HA H 4.29 . 1 173 23 ALA HB H 1.26 . 1 174 23 ALA C C 175.00 . 1 175 23 ALA CA C 52.42 . 1 176 23 ALA CB C 19.03 . 1 177 23 ALA N N 124.31 . 1 178 24 VAL H H 7.78 . 1 179 24 VAL HA H 4.07 . 1 180 24 VAL HB H 2.07 . 1 181 24 VAL HG1 H 0.95 . 1 182 24 VAL HG2 H 0.95 . 1 183 24 VAL C C 176.48 . 1 184 24 VAL CA C 62.10 . 1 185 24 VAL CB C 32.80 . 1 186 24 VAL N N 118.12 . 1 187 25 ARG H H 8.10 . 1 188 25 ARG C C 175.61 . 1 189 25 ARG CA C 56.44 . 1 190 25 ARG CB C 30.45 . 1 191 25 ARG N N 121.23 . 1 192 27 PRO HA H 4.20 . 1 193 27 PRO HB2 H 2.04 . 1 194 27 PRO HB3 H 2.04 . 1 195 27 PRO HG2 H 1.35 . 1 196 27 PRO HG3 H 1.35 . 1 197 27 PRO C C 180.00 . 1 198 27 PRO CA C 61.60 . 1 199 28 GLY H H 8.79 . 1 200 28 GLY HA2 H 4.11 . 1 201 28 GLY HA3 H 4.11 . 1 202 28 GLY C C 177.70 . 1 203 28 GLY CA C 45.36 . 1 204 28 GLY N N 112.37 . 1 205 29 GLY H H 8.36 . 1 206 29 GLY HA2 H 4.07 . 1 207 29 GLY HA3 H 4.07 . 1 208 29 GLY C C 177.89 . 1 209 29 GLY CA C 45.33 . 1 210 29 GLY N N 108.78 . 1 211 30 PRO HA H 4.37 . 1 212 30 PRO HB2 H 2.01 . 1 213 30 PRO HB3 H 2.01 . 1 214 30 PRO C C 178.00 . 1 215 30 PRO CA C 62.03 . 1 216 31 ALA H H 8.20 . 1 217 31 ALA HA H 4.32 . 1 218 31 ALA HB H 1.40 . 1 219 31 ALA C C 175.02 . 1 220 31 ALA CA C 52.58 . 1 221 31 ALA CB C 18.90 . 1 222 31 ALA N N 124.37 . 1 223 32 VAL H H 7.90 . 1 224 32 VAL HA H 4.10 . 1 225 32 VAL HB H 2.07 . 1 226 32 VAL HG1 H 0.95 . 1 227 32 VAL HG2 H 0.95 . 1 228 32 VAL C C 176.00 . 1 229 32 VAL CA C 62.21 . 1 230 32 VAL CB C 32.71 . 1 231 32 VAL N N 118.38 . 1 232 33 ALA H H 8.11 . 1 233 33 ALA HA H 4.27 . 1 234 33 ALA HB H 1.38 . 1 235 33 ALA C C 174.00 . 1 236 33 ALA CA C 53.00 . 1 237 33 ALA CB C 18.91 . 1 238 33 ALA N N 125.60 . 1 239 34 ASN H H 8.17 . 1 240 34 ASN HA H 4.60 . 1 241 34 ASN HB2 H 2.80 . 1 242 34 ASN HB3 H 2.80 . 1 243 34 ASN C C 175.60 . 1 244 34 ASN CA C 53.55 . 1 245 34 ASN CB C 39.46 . 1 246 34 ASN N N 123.90 . 1 247 35 SER H H 8.11 . 1 248 35 SER HA H 4.40 . 1 249 35 SER HB2 H 3.93 . 1 250 35 SER HB3 H 3.93 . 1 251 35 SER C C 177.61 . 1 252 35 SER CA C 58.90 . 1 253 35 SER CB C 63.43 . 1 254 35 SER N N 115.33 . 1 255 36 VAL H H 7.95 . 1 256 36 VAL HA H 4.14 . 1 257 36 VAL HB H 2.06 . 1 258 36 VAL HG1 H 0.92 . 1 259 36 VAL HG2 H 0.92 . 1 260 36 VAL C C 175.96 . 1 261 36 VAL CA C 62.94 . 1 262 36 VAL CB C 32.36 . 1 263 36 VAL N N 121.11 . 1 264 37 ALA H H 8.11 . 1 265 37 ALA HA H 4.23 . 1 266 37 ALA HB H 1.37 . 1 267 37 ALA C C 174.10 . 1 268 37 ALA CA C 52.90 . 1 269 37 ALA CB C 18.91 . 1 270 37 ALA N N 125.83 . 1 271 38 ARG H H 8.04 . 1 272 38 ARG HA H 4.29 . 1 273 38 ARG HB2 H 1.81 . 1 274 38 ARG HB3 H 1.81 . 1 275 38 ARG HG2 H 1.51 . 2 276 38 ARG HG3 H 1.41 . 2 277 38 ARG HD2 H 3.02 . 1 278 38 ARG HD3 H 3.02 . 1 279 38 ARG C C 176.38 . 1 280 38 ARG CA C 56.28 . 1 281 38 ARG CB C 30.55 . 1 282 38 ARG N N 119.24 . 1 283 39 LYS HA H 4.33 . 1 284 39 LYS C C 176.18 . 1 285 39 LYS CA C 55.94 . 1 286 39 LYS CB C 32.97 . 1 287 40 HIS H H 8.37 . 1 288 40 HIS HA H 4.50 . 1 289 40 HIS HB2 H 3.31 . 1 290 40 HIS HB3 H 3.31 . 1 291 40 HIS C C 175.40 . 1 292 40 HIS CA C 55.54 . 1 293 40 HIS CB C 29.03 . 1 294 40 HIS N N 121.31 . 1 295 41 GLY H H 8.40 . 1 296 41 GLY HA2 H 3.95 . 2 297 41 GLY HA3 H 4.15 . 2 298 41 GLY C C 175.43 . 1 299 41 GLY CA C 45.33 . 1 300 41 GLY N N 109.95 . 1 301 42 PHE H H 8.08 . 1 302 42 PHE HA H 4.64 . 1 303 42 PHE HB2 H 3.15 . 1 304 42 PHE HB3 H 3.15 . 1 305 42 PHE C C 175.00 . 1 306 42 PHE CA C 57.63 . 1 307 42 PHE CB C 39.51 . 1 308 42 PHE N N 119.42 . 1 309 43 LEU H H 8.11 . 1 310 43 LEU HA H 4.31 . 1 311 43 LEU HB2 H 1.55 . 1 312 43 LEU HB3 H 1.55 . 1 313 43 LEU HG H 0.87 . 2 314 43 LEU HD1 H 0.87 . 1 315 43 LEU HD2 H 0.87 . 1 316 43 LEU C C 176.80 . 1 317 43 LEU CA C 55.09 . 1 318 43 LEU CB C 42.63 . 1 319 43 LEU N N 122.86 . 1 320 44 BASP HA H 3.79 . 1 321 44 BASP HB2 H 2.54 . 1 322 44 BASP HB3 H 2.54 . 1 323 44 BASP C C 174.00 . 1 324 44 BASP CA C 34.00 . 1 325 44 BASP CB C 29.00 . 1 326 45 LEU H H 8.50 . 1 327 45 LEU HA H 4.42 . 1 328 45 LEU HB2 H 1.55 . 1 329 45 LEU HB3 H 1.55 . 1 330 45 LEU HD1 H 0.88 . 1 331 45 LEU HD2 H 0.88 . 1 332 45 LEU C C 177.36 . 1 333 45 LEU CA C 55.35 . 1 334 45 LEU CB C 42.00 . 1 335 45 LEU N N 123.18 . 1 336 46 GLY H H 8.30 . 1 337 46 GLY HA2 H 3.94 . 1 338 46 GLY HA3 H 3.94 . 1 339 46 GLY C C 174.20 . 1 340 46 GLY CA C 45.53 . 1 341 46 GLY N N 115.30 . 1 342 49 PHE HA H 4.75 . 1 343 49 PHE HB2 H 3.28 . 2 344 49 PHE HB3 H 2.98 . 2 345 49 PHE C C 177.60 . 1 346 49 PHE CA C 58.17 . 1 347 50 GLY H H 8.26 . 1 348 50 GLY HA2 H 3.95 . 1 349 50 GLY HA3 H 3.95 . 1 350 50 GLY C C 172.00 . 1 351 50 GLY CA C 45.17 . 1 352 50 GLY N N 109.29 . 1 353 51 ASP H H 8.09 . 1 354 51 ASP HA H 4.63 . 1 355 51 ASP HB2 H 2.70 . 1 356 51 ASP HB3 H 2.70 . 1 357 51 ASP C C 174.50 . 1 358 51 ASP CA C 52.48 . 1 359 51 ASP CB C 42.19 . 1 360 51 ASP N N 123.54 . 1 361 54 HIS HA H 4.73 . 1 362 54 HIS HB2 H 3.25 . 1 363 54 HIS HB3 H 3.25 . 1 364 54 HIS C C 178.63 . 1 365 54 HIS CA C 55.46 . 1 366 54 HIS CB C 29.11 . 1 367 55 PHE H H 8.35 . 1 368 55 PHE HA H 4.78 . 1 369 55 PHE HB2 H 3.03 . 1 370 55 PHE HB3 H 3.03 . 1 371 55 PHE C C 173.80 . 1 372 55 PHE CA C 57.00 . 1 373 55 PHE N N 125.17 . 1 374 56 TRP H H 8.00 . 1 375 56 TRP HA H 4.63 . 1 376 56 TRP HB2 H 3.33 . 1 377 56 TRP HB3 H 3.33 . 1 378 56 TRP C C 175.40 . 1 379 56 TRP CA C 58.47 . 1 380 56 TRP CB C 28.91 . 1 381 56 TRP N N 121.15 . 1 382 57 HIS H H 7.95 . 1 383 57 HIS HA H 4.60 . 1 384 57 HIS HB2 H 3.20 . 1 385 57 HIS HB3 H 3.20 . 1 386 57 HIS C C 176.66 . 1 387 57 HIS CA C 56.19 . 1 388 57 HIS CB C 29.28 . 1 389 57 HIS N N 122.17 . 1 390 58 ARG H H 8.41 . 1 391 58 ARG HA H 4.24 . 1 392 58 ARG HB2 H 1.60 . 1 393 58 ARG HB3 H 1.60 . 1 394 58 ARG C C 176.40 . 1 395 58 ARG CA C 56.36 . 1 396 58 ARG CB C 33.14 . 1 397 58 ARG N N 123.44 . 1 398 59 GLY H H 8.33 . 1 399 59 GLY HA2 H 3.95 . 1 400 59 GLY HA3 H 3.95 . 1 401 59 GLY C C 175.47 . 1 402 59 GLY CA C 45.14 . 1 403 59 GLY N N 110.07 . 1 404 60 VAL H H 7.95 . 1 405 60 VAL HA H 4.18 . 1 406 60 VAL HB H 1.39 . 2 407 60 VAL HG1 H 0.90 . 1 408 60 VAL HG2 H 0.90 . 1 409 60 VAL C C 175.76 . 1 410 60 VAL CA C 62.18 . 1 411 60 VAL CB C 32.88 . 1 412 60 VAL N N 118.96 . 1 413 61 THR H H 8.19 . 1 414 61 THR HA H 4.37 . 1 415 61 THR HB H 4.17 . 1 416 61 THR HG2 H 1.18 . 1 417 61 THR C C 177.84 . 1 418 61 THR CA C 61.80 . 1 419 61 THR CB C 70.30 . 1 420 61 THR N N 118.23 . 1 421 62 LYS H H 8.30 . 1 422 62 LYS HA H 4.30 . 1 423 62 LYS HB2 H 1.80 . 1 424 62 LYS HB3 H 1.80 . 1 425 62 LYS HG2 H 1.42 . 1 426 62 LYS HG3 H 1.42 . 1 427 62 LYS HD2 H 1.70 . 1 428 62 LYS HD3 H 1.70 . 1 429 62 LYS HE2 H 3.19 . 1 430 62 LYS HE3 H 3.19 . 1 431 62 LYS C C 175.70 . 1 432 62 LYS CA C 56.36 . 1 433 62 LYS CB C 32.96 . 1 434 62 LYS N N 124.10 . 1 435 63 ARG H H 8.30 . 1 436 63 ARG HA H 4.34 . 1 437 63 ARG HB2 H 1.81 . 1 438 63 ARG HB3 H 1.81 . 1 439 63 ARG HG2 H 1.61 . 1 440 63 ARG HG3 H 1.61 . 1 441 63 ARG C C 175.83 . 1 442 63 ARG CA C 56.13 . 1 443 63 ARG CB C 30.70 . 1 444 63 ARG N N 122.33 . 1 445 64 SER H H 8.27 . 1 446 64 SER HA H 4.45 . 1 447 64 SER HB2 H 3.87 . 1 448 64 SER HB3 H 3.87 . 1 449 64 SER C C 177.84 . 1 450 64 SER CA C 58.19 . 1 451 64 SER CB C 63.57 . 1 452 64 SER N N 116.97 . 1 453 65 LEU H H 8.24 . 1 454 65 LEU HA H 4.40 . 1 455 65 LEU HB2 H 1.61 . 1 456 65 LEU HB3 H 1.61 . 1 457 65 LEU HD1 H 0.89 . 1 458 65 LEU HD2 H 0.89 . 1 459 65 LEU C C 175.05 . 1 460 65 LEU CA C 54.93 . 1 461 65 LEU CB C 42.38 . 1 462 65 LEU N N 124.07 . 1 463 66 SER H H 8.29 . 1 464 66 SER HA H 4.75 . 1 465 66 SER HB2 H 3.85 . 1 466 66 SER HB3 H 3.85 . 1 467 66 SER C C 179.42 . 1 468 66 SER CA C 56.22 . 1 469 66 SER CB C 63.32 . 1 470 66 SER N N 117.36 . 1 471 67 PRO HA H 4.33 . 1 472 67 PRO HB2 H 2.26 . 1 473 67 PRO HB3 H 2.26 . 1 474 67 PRO HG2 H 1.93 . 2 475 67 PRO HG3 H 1.88 . 2 476 67 PRO C C 175.42 . 1 477 67 PRO CA C 63.17 . 1 478 67 PRO CB C 31.80 . 1 479 68 HIS H H 8.44 . 1 480 68 HIS HA H 4.69 . 1 481 68 HIS HB2 H 3.21 . 1 482 68 HIS HB3 H 3.21 . 1 483 68 HIS C C 178.06 . 1 484 68 HIS CA C 54.92 . 1 485 68 HIS CB C 28.84 . 1 486 68 HIS N N 118.21 . 1 487 69 ARG H H 8.28 . 1 488 69 ARG HA H 4.64 . 1 489 69 ARG HB2 H 1.83 . 1 490 69 ARG HB3 H 1.83 . 1 491 69 ARG HG2 H 1.73 . 1 492 69 ARG HG3 H 1.73 . 1 493 69 ARG HD2 H 3.22 . 1 494 69 ARG HD3 H 3.22 . 1 495 69 ARG C C 175.38 . 1 496 69 ARG CA C 53.97 . 1 497 69 ARG CB C 30.16 . 1 498 69 ARG N N 123.48 . 1 499 70 PRO HA H 4.33 . 1 500 70 PRO HB2 H 2.36 . 1 501 70 PRO HB3 H 2.36 . 1 502 70 PRO C C 176.00 . 1 503 70 PRO CA C 62.90 . 1 504 70 PRO CB C 31.80 . 1 505 71 ARG H H 8.44 . 1 506 71 ARG HA H 4.27 . 1 507 71 ARG HB2 H 1.75 . 1 508 71 ARG HB3 H 1.75 . 1 509 71 ARG HG2 H 1.60 . 1 510 71 ARG HG3 H 1.60 . 1 511 71 ARG HD2 H 3.18 . 1 512 71 ARG HD3 H 3.18 . 1 513 71 ARG C C 175.80 . 1 514 71 ARG CA C 56.00 . 1 515 71 ARG CB C 30.70 . 1 516 71 ARG N N 121.00 . 1 517 72 HIS H H 8.49 . 1 518 72 HIS HA H 4.66 . 1 519 72 HIS HB2 H 3.27 . 2 520 72 HIS HB3 H 3.21 . 2 521 72 HIS C C 177.87 . 1 522 72 HIS CA C 55.12 . 1 523 72 HIS N N 119.00 . 1 524 73 SER H H 8.31 . 1 525 73 SER HA H 4.46 . 1 526 73 SER HB2 H 3.83 . 1 527 73 SER HB3 H 3.83 . 1 528 73 SER C C 177.73 . 1 529 73 SER CA C 58.22 . 1 530 73 SER CB C 64.00 . 1 531 73 SER N N 117.07 . 1 532 74 ARG H H 8.45 . 1 533 74 ARG HA H 4.36 . 1 534 74 ARG HB2 H 1.83 . 1 535 74 ARG HB3 H 1.83 . 1 536 74 ARG HG2 H 1.65 . 1 537 74 ARG HG3 H 1.65 . 1 538 74 ARG HD2 H 3.21 . 1 539 74 ARG HD3 H 3.21 . 1 540 74 ARG C C 176.00 . 1 541 74 ARG CA C 56.40 . 1 542 74 ARG CB C 30.44 . 1 543 74 ARG N N 123.00 . 1 544 75 LEU H H 8.18 . 1 545 75 LEU HA H 4.31 . 1 546 75 LEU HB2 H 1.60 . 1 547 75 LEU HB3 H 1.60 . 1 548 75 LEU HG H 0.87 . 2 549 75 LEU HD1 H 0.87 . 1 550 75 LEU HD2 H 0.87 . 1 551 75 LEU C C 175.00 . 1 552 75 LEU CA C 55.21 . 1 553 75 LEU CB C 42.21 . 1 554 75 LEU N N 122.65 . 1 555 76 GLN H H 8.24 . 1 556 76 GLN HA H 4.31 . 1 557 76 GLN HB2 H 1.82 . 1 558 76 GLN HB3 H 1.82 . 1 559 76 GLN HG2 H 2.33 . 1 560 76 GLN HG3 H 2.33 . 1 561 76 GLN C C 176.60 . 1 562 76 GLN CA C 55.92 . 1 563 76 GLN CB C 29.34 . 1 564 76 GLN N N 121.15 . 1 565 77 ARG H H 8.25 . 1 566 77 ARG HA H 4.33 . 1 567 77 ARG HB2 H 1.78 . 1 568 77 ARG HB3 H 1.78 . 1 569 77 ARG HG2 H 1.61 . 1 570 77 ARG HG3 H 1.61 . 1 571 77 ARG HD2 H 3.17 . 1 572 77 ARG HD3 H 3.17 . 1 573 77 ARG C C 176.25 . 1 574 77 ARG CA C 56.40 . 1 575 77 ARG CB C 30.52 . 1 576 77 ARG N N 121.90 . 1 577 78 GLU H H 8.35 . 1 578 78 GLU HA H 4.65 . 1 579 78 GLU HB2 H 2.11 . 2 580 78 GLU HB3 H 1.96 . 2 581 78 GLU HG2 H 2.43 . 1 582 78 GLU HG3 H 2.43 . 1 583 78 GLU C C 177.90 . 1 584 78 GLU CA C 54.00 . 1 585 78 GLU CB C 28.76 . 1 586 78 GLU N N 122.34 . 1 587 79 PRO HA H 4.39 . 1 588 79 PRO HB2 H 2.32 . 1 589 79 PRO HB3 H 2.32 . 1 590 79 PRO HG2 H 2.00 . 1 591 79 PRO HG3 H 2.00 . 1 592 79 PRO HD2 H 3.68 . 1 593 79 PRO HD3 H 3.68 . 1 594 79 PRO C C 175.00 . 1 595 79 PRO CA C 63.42 . 1 596 79 PRO CB C 31.78 . 1 597 80 GLN H H 8.42 . 1 598 80 GLN HA H 4.17 . 1 599 80 GLN HB2 H 2.16 . 1 600 80 GLN HB3 H 2.16 . 1 601 80 GLN C C 175.61 . 1 602 80 GLN CA C 56.39 . 1 603 80 GLN CB C 29.00 . 1 604 80 GLN N N 120.25 . 1 605 81 VAL H H 7.92 . 1 606 81 VAL HA H 3.94 . 1 607 81 VAL HB H 2.08 . 1 608 81 VAL HG1 H 0.95 . 1 609 81 VAL HG2 H 0.95 . 1 610 81 VAL C C 175.66 . 1 611 81 VAL CA C 63.34 . 1 612 81 VAL CB C 32.30 . 1 613 81 VAL N N 119.86 . 1 614 82 GLN H H 8.20 . 1 615 82 GLN HA H 4.22 . 1 616 82 GLN HB2 H 2.28 . 1 617 82 GLN HB3 H 2.28 . 1 618 82 GLN C C 175.65 . 1 619 82 GLN CA C 56.89 . 1 620 82 GLN CB C 28.85 . 1 621 82 GLN N N 122.14 . 1 622 83 TRP H H 8.00 . 1 623 83 TRP HA H 4.34 . 1 624 83 TRP HB2 H 3.29 . 1 625 83 TRP HB3 H 3.29 . 1 626 83 TRP C C 175.22 . 1 627 83 TRP CA C 58.50 . 1 628 83 TRP CB C 28.92 . 1 629 83 TRP N N 121.15 . 1 630 84 LEU H H 7.97 . 1 631 84 LEU HA H 4.15 . 1 632 84 LEU HB2 H 1.53 . 1 633 84 LEU HB3 H 1.53 . 1 634 84 LEU HG H 0.85 . 2 635 84 LEU HD1 H 0.85 . 1 636 84 LEU HD2 H 0.85 . 1 637 84 LEU C C 174.13 . 1 638 84 LEU CA C 56.18 . 1 639 84 LEU CB C 42.13 . 1 640 84 LEU N N 121.72 . 1 641 85 GLU H H 8.04 . 1 642 85 GLU HA H 4.15 . 1 643 85 GLU HB2 H 2.07 . 1 644 85 GLU HB3 H 2.07 . 1 645 85 GLU HG2 H 2.39 . 1 646 85 GLU HG3 H 2.39 . 1 647 85 GLU C C 175.00 . 1 648 85 GLU CA C 56.28 . 1 649 85 GLU CB C 28.67 . 1 650 85 GLU N N 119.24 . 1 651 86 GLN H H 8.08 . 1 652 86 GLN HA H 4.28 . 1 653 86 GLN HB2 H 2.18 . 1 654 86 GLN HB3 H 2.18 . 1 655 86 GLN HG2 H 2.35 . 1 656 86 GLN HG3 H 2.35 . 1 657 86 GLN C C 175.00 . 1 658 86 GLN CA C 57.00 . 1 659 86 GLN CB C 28.76 . 1 660 86 GLN N N 119.42 . 1 661 87 GLN H H 8.09 . 1 662 87 GLN HA H 4.28 . 1 663 87 GLN HB2 H 2.18 . 1 664 87 GLN HB3 H 2.18 . 1 665 87 GLN HG2 H 2.35 . 1 666 87 GLN HG3 H 2.35 . 1 667 87 GLN C C 175.76 . 1 668 87 GLN CA C 56.42 . 1 669 87 GLN CB C 28.93 . 1 670 87 GLN N N 120.12 . 1 671 88 VAL H H 8.03 . 1 672 88 VAL HA H 3.94 . 1 673 88 VAL HB H 2.06 . 1 674 88 VAL HG1 H 0.93 . 1 675 88 VAL HG2 H 0.93 . 1 676 88 VAL C C 175.55 . 1 677 88 VAL CA C 63.00 . 1 678 88 VAL CB C 32.22 . 1 679 88 VAL N N 120.30 . 1 680 89 ALA H H 8.08 . 1 681 89 ALA HA H 4.24 . 1 682 89 ALA HB H 1.40 . 1 683 89 ALA C C 173.50 . 1 684 89 ALA CA C 53.10 . 1 685 89 ALA CB C 18.86 . 1 686 89 ALA N N 125.39 . 1 687 90 LYS H H 7.98 . 1 688 90 LYS HA H 4.27 . 1 689 90 LYS HB2 H 1.81 . 1 690 90 LYS HB3 H 1.81 . 1 691 90 LYS HG2 H 1.43 . 1 692 90 LYS HG3 H 1.43 . 1 693 90 LYS HD2 H 1.65 . 1 694 90 LYS HD3 H 1.65 . 1 695 90 LYS HE2 H 2.98 . 1 696 90 LYS HE3 H 2.98 . 1 697 90 LYS C C 175.25 . 1 698 90 LYS CA C 56.67 . 1 699 90 LYS CB C 32.86 . 1 700 90 LYS N N 119.26 . 1 701 91 ARG H H 8.05 . 1 702 91 ARG HA H 4.32 . 1 703 91 ARG HB2 H 1.84 . 1 704 91 ARG HB3 H 1.84 . 1 705 91 ARG HG2 H 1.66 . 1 706 91 ARG HG3 H 1.66 . 1 707 91 ARG C C 175.63 . 1 708 91 ARG CA C 56.56 . 1 709 91 ARG CB C 30.45 . 1 710 91 ARG N N 120.97 . 1 711 92 ARG H H 8.01 . 1 712 92 ARG HA H 4.40 . 1 713 92 ARG HB2 H 1.85 . 1 714 92 ARG HB3 H 1.85 . 1 715 92 ARG HG2 H 1.66 . 1 716 92 ARG HG3 H 1.66 . 1 717 92 ARG HD2 H 3.21 . 1 718 92 ARG HD3 H 3.21 . 1 719 92 ARG C C 175.56 . 1 720 92 ARG CA C 56.33 . 1 721 92 ARG CB C 30.53 . 1 722 92 ARG N N 120.47 . 1 723 93 THR H H 8.14 . 2 724 93 THR HA H 4.39 . 1 725 93 THR HB H 4.27 . 1 726 93 THR HG2 H 1.21 . 1 727 93 THR C C 177.62 . 1 728 93 THR CA C 61.90 . 1 729 93 THR CB C 70.28 . 1 730 93 THR N N 115.11 . 1 731 94 LYS H H 8.29 . 1 732 94 LYS HA H 4.32 . 1 733 94 LYS HB2 H 1.80 . 1 734 94 LYS HB3 H 1.80 . 1 735 94 LYS HG2 H 1.67 . 1 736 94 LYS HG3 H 1.67 . 1 737 94 LYS HD2 H 1.44 . 1 738 94 LYS HD3 H 1.44 . 1 739 94 LYS HE2 H 2.98 . 1 740 94 LYS HE3 H 2.98 . 1 741 94 LYS C C 175.36 . 1 742 94 LYS CA C 56.89 . 1 743 94 LYS CB C 32.86 . 1 744 94 LYS N N 123.20 . 1 745 95 ARG H H 8.05 . 1 746 95 ARG HA H 4.34 . 1 747 95 ARG HB2 H 1.80 . 1 748 95 ARG HB3 H 1.80 . 1 749 95 ARG HG2 H 1.62 . 1 750 95 ARG HG3 H 1.62 . 1 751 95 ARG HD2 H 2.98 . 1 752 95 ARG HD3 H 2.98 . 1 753 95 ARG C C 175.84 . 1 754 95 ARG CA C 56.50 . 1 755 95 ARG CB C 30.43 . 1 756 95 ARG N N 120.97 . 1 757 96 ASP H H 8.32 . 1 758 96 ASP HA H 4.64 . 1 759 96 ASP HB2 H 2.76 . 1 760 96 ASP HB3 H 2.76 . 1 761 96 ASP C C 175.83 . 1 762 96 ASP CA C 54.17 . 1 763 96 ASP CB C 40.00 . 1 764 96 ASP N N 121.76 . 1 765 97 VAL H H 8.01 . 1 766 97 VAL HA H 4.13 . 1 767 97 VAL HB H 2.13 . 1 768 97 VAL HG1 H 0.94 . 1 769 97 VAL HG2 H 0.94 . 1 770 97 VAL C C 175.73 . 1 771 97 VAL CA C 63.25 . 1 772 97 VAL CB C 32.22 . 1 773 97 VAL N N 120.47 . 1 774 98 ALA H H 8.18 . 1 775 98 ALA HA H 4.23 . 1 776 98 ALA HB H 1.41 . 1 777 98 ALA C C 173.79 . 1 778 98 ALA CA C 53.17 . 1 779 98 ALA CB C 18.86 . 1 780 98 ALA N N 125.57 . 1 781 99 ALA H H 8.04 . 1 782 99 ALA HA H 4.24 . 1 783 99 ALA HB H 1.38 . 1 784 99 ALA C C 173.79 . 1 785 99 ALA CA C 53.21 . 1 786 99 ALA CB C 18.86 . 1 787 99 ALA N N 122.10 . 1 788 100 ALA H H 7.98 . 1 789 100 ALA HA H 4.23 . 1 790 100 ALA HB H 1.41 . 1 791 100 ALA C C 173.72 . 1 792 100 ALA CA C 53.13 . 1 793 100 ALA CB C 18.86 . 1 794 100 ALA N N 121.43 . 1 795 101 LEU H H 7.88 . 1 796 101 LEU HA H 4.21 . 1 797 101 LEU HB2 H 1.63 . 1 798 101 LEU HB3 H 1.63 . 1 799 101 LEU HG H 0.87 . 2 800 101 LEU HD1 H 0.87 . 1 801 101 LEU HD2 H 0.87 . 1 802 101 LEU C C 174.47 . 1 803 101 LEU CA C 55.50 . 1 804 101 LEU CB C 42.00 . 1 805 101 LEU N N 119.46 . 1 806 102 GLU H H 7.92 . 1 807 102 GLU HA H 4.20 . 1 808 102 GLU HG2 H 2.30 . 1 809 102 GLU HG3 H 2.30 . 1 810 102 GLU C C 175.90 . 1 811 102 GLU CA C 56.28 . 1 812 102 GLU CB C 29.00 . 1 813 102 GLU N N 119.36 . 1 stop_ save_