data_4217 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The 3D structure of the streptomyces metalloproteinase inhibitor, SMPI, isolated from streptomyces nigrescens TK-23 ; _BMRB_accession_number 4217 _BMRB_flat_file_name bmr4217.str _Entry_type original _Submission_date 1998-06-10 _Accession_date 1998-06-10 _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 Tate S. . . 2 Ohno A. . . 3 Seeram S. S. . 4 Hiraga K. . . 5 Oda K. . . 6 Kainosho M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 519 "13C chemical shifts" 191 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-04 original author . stop_ _Original_release_date 2000-04-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of the streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98407984 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ohno A. . . 2 Tate S. . . 3 Seeram S. S. . 4 Hiraga K. . . 5 Oda K. . . 6 Swindells M. B. . 7 Kainosho M. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 282 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 421 _Page_last 433 _Year 1998 _Details . loop_ _Keyword 'metalloproteinase inhibitor' stop_ save_ ################################## # Molecular system description # ################################## save_system_SMPI _Saveframe_category molecular_system _Mol_system_name 'streptomyces metalloproteinase inhibitor' _Abbreviation_common SMPI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SMPI $SMPI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SMPI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'metalloproteinase inhibitor' _Name_variant 'Sakstar variant' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; APSCPAGSLCTYSGTGLSGA RTVIPASDMEKAGTDGVKLP ASARSFANGTHFTLRYGPAR KVTCVRFPCYQYATVGKVAP GAQLRSLPSPGATVTVGQDL GD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 PRO 3 3 SER 4 4 CYS 5 5 PRO 6 6 ALA 7 7 GLY 8 8 SER 9 9 LEU 10 10 CYS 11 11 THR 12 12 TYR 13 13 SER 14 14 GLY 15 15 THR 16 16 GLY 17 17 LEU 18 18 SER 19 19 GLY 20 20 ALA 21 21 ARG 22 22 THR 23 23 VAL 24 24 ILE 25 25 PRO 26 26 ALA 27 27 SER 28 28 ASP 29 29 MET 30 30 GLU 31 31 LYS 32 32 ALA 33 33 GLY 34 34 THR 35 35 ASP 36 36 GLY 37 37 VAL 38 38 LYS 39 39 LEU 40 40 PRO 41 41 ALA 42 42 SER 43 43 ALA 44 44 ARG 45 45 SER 46 46 PHE 47 47 ALA 48 48 ASN 49 49 GLY 50 50 THR 51 51 HIS 52 52 PHE 53 53 THR 54 54 LEU 55 55 ARG 56 56 TYR 57 57 GLY 58 58 PRO 59 59 ALA 60 60 ARG 61 61 LYS 62 62 VAL 63 63 THR 64 64 CYS 65 65 VAL 66 66 ARG 67 67 PHE 68 68 PRO 69 69 CYS 70 70 TYR 71 71 GLN 72 72 TYR 73 73 ALA 74 74 THR 75 75 VAL 76 76 GLY 77 77 LYS 78 78 VAL 79 79 ALA 80 80 PRO 81 81 GLY 82 82 ALA 83 83 GLN 84 84 LEU 85 85 ARG 86 86 SER 87 87 LEU 88 88 PRO 89 89 SER 90 90 PRO 91 91 GLY 92 92 ALA 93 93 THR 94 94 VAL 95 95 THR 96 96 VAL 97 97 GLY 98 98 GLN 99 99 ASP 100 100 LEU 101 101 GLY 102 102 ASP 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 PDB 1BHU "The 3d Structure Of The Streptomyces Metalloproteinase Inhibitor, Smpi, Isolated From Streptomyces Nigrescens Tk- 23, Nmr, Mini" 100.00 102 100.00 100.00 2.46e-65 DBJ BAA00574 "metalloprotease inhibitor precursor [Streptomyces nigrescens]" 100.00 131 100.00 100.00 1.24e-65 PRF 1102216A "inhibitor,metallo proteinase [Streptomyces nigrescens]" 100.00 102 100.00 100.00 2.46e-65 SP P01077 "RecName: Full=Metalloproteinase inhibitor; Flags: Precursor" 100.00 131 100.00 100.00 1.24e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Organelle _Details $SMPI 'Streptomyces nigrescens' 1920 Bacteria . Streptomyces nigrescens TK-23 'c-Myc and Max are nuclear proteins' ; Prepared as a T7 RNA polymerase transcript from chemically synthesized DNA promoter & template. A UNCG tetra-loop was used to connect nucleotides 593 and 646 (E. coli). ; 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 $SMPI 'recombinant technology' 'Escherichia coli' Escherichia coli . . 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 $SMPI . mM . 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_ ############################# # NMR applied experiments # ############################# save_Heteronuclear_multi-dimensional_experiment_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Heteronuclear multi-dimensional experiment' _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name 'Heteronuclear multi-dimensional experiment' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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_citation_label _Correction_value_citation_label . C 13 . ppm . . . . . . $entry_citation $entry_citation . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $entry_citation $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name SMPI _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 ALA H H 8.29 . 1 2 . 1 ALA HA H 4.59 . 1 3 . 1 ALA HB H 1.30 . 1 4 . 1 ALA CA C 48.88 . 1 5 . 1 ALA CB C 16.92 . 1 6 . 1 ALA N N 128.33 . 1 7 . 2 PRO HA H 4.40 . 1 8 . 2 PRO HB2 H 1.80 . 1 9 . 2 PRO HB3 H 2.21 . 1 10 . 2 PRO HG2 H 1.93 . 1 11 . 2 PRO HG3 H 1.93 . 1 12 . 2 PRO HD2 H 3.74 . 1 13 . 2 PRO HD3 H 3.56 . 1 14 . 2 PRO CA C 61.42 . 1 15 . 2 PRO CB C 30.56 . 1 16 . 3 SER H H 8.42 . 1 17 . 3 SER HA H 4.33 . 1 18 . 3 SER HB2 H 3.81 . 1 19 . 3 SER HB3 H 3.98 . 1 20 . 3 SER CA C 56.53 . 1 21 . 3 SER CB C 62.26 . 1 22 . 3 SER N N 117.89 . 1 23 . 4 CYS H H 8.32 . 1 24 . 4 CYS HA H 5.14 . 1 25 . 4 CYS HB2 H 2.69 . 1 26 . 4 CYS HB3 H 2.98 . 1 27 . 4 CYS CA C 50.18 . 1 28 . 4 CYS CB C 30.90 . 1 29 . 4 CYS N N 125.01 . 1 30 . 5 PRO HA H 4.24 . 1 31 . 5 PRO HB2 H 2.23 . 1 32 . 5 PRO HB3 H 1.76 . 1 33 . 5 PRO HG2 H 1.89 . 1 34 . 5 PRO HG3 H 1.91 . 1 35 . 5 PRO HD2 H 3.75 . 1 36 . 5 PRO HD3 H 3.42 . 1 37 . 5 PRO CA C 61.33 . 1 38 . 5 PRO CB C 30.65 . 1 39 . 6 ALA H H 8.11 . 1 40 . 6 ALA HA H 4.25 . 1 41 . 6 ALA HB H 1.33 . 1 42 . 6 ALA CA C 51.57 . 1 43 . 6 ALA CB C 16.81 . 1 44 . 6 ALA N N 125.06 . 1 45 . 7 GLY H H 8.48 . 1 46 . 7 GLY HA2 H 3.71 . 1 47 . 7 GLY HA3 H 4.24 . 1 48 . 7 GLY CA C 44.18 . 1 49 . 7 GLY N N 111.87 . 1 50 . 8 SER H H 7.30 . 1 51 . 8 SER HA H 4.90 . 1 52 . 8 SER HB2 H 3.51 . 1 53 . 8 SER HB3 H 3.65 . 1 54 . 8 SER CA C 56.63 . 1 55 . 8 SER CB C 64.37 . 1 56 . 8 SER N N 115.62 . 1 57 . 9 LEU H H 8.95 . 1 58 . 9 LEU HA H 4.87 . 1 59 . 9 LEU HB2 H 1.15 . 1 60 . 9 LEU HB3 H 1.83 . 1 61 . 9 LEU HG H 0.48 . 1 62 . 9 LEU HD1 H 1.24 . 1 63 . 9 LEU HD2 H 1.22 . 1 64 . 9 LEU CA C 52.20 . 1 65 . 9 LEU CB C 42.92 . 1 66 . 9 LEU N N 124.61 . 1 67 . 10 CYS H H 8.72 . 1 68 . 10 CYS HA H 5.73 . 1 69 . 10 CYS HB2 H 2.78 . 1 70 . 10 CYS HB3 H 2.99 . 1 71 . 10 CYS CA C 54.10 . 1 72 . 10 CYS CB C 44.27 . 1 73 . 10 CYS N N 123.59 . 1 74 . 11 THR H H 9.03 . 1 75 . 11 THR HA H 5.06 . 1 76 . 11 THR HB H 4.23 . 1 77 . 11 THR HG2 H 0.93 . 1 78 . 11 THR CA C 58.31 . 1 79 . 11 THR CB C 67.92 . 1 80 . 11 THR N N 116.70 . 1 81 . 12 TYR H H 8.23 . 1 82 . 12 TYR HA H 5.49 . 1 83 . 12 TYR HB2 H 3.50 . 1 84 . 12 TYR HB3 H 2.68 . 1 85 . 12 TYR HD1 H 6.62 . 1 86 . 12 TYR HD2 H 6.62 . 1 87 . 12 TYR HE1 H 6.56 . 1 88 . 12 TYR HE2 H 6.56 . 1 89 . 12 TYR CA C 54.89 . 1 90 . 12 TYR CB C 38.62 . 1 91 . 12 TYR N N 120.35 . 1 92 . 13 SER H H 8.50 . 1 93 . 13 SER HA H 4.89 . 1 94 . 13 SER HB2 H 3.81 . 1 95 . 13 SER HB3 H 4.31 . 1 96 . 13 SER CA C 57.88 . 1 97 . 13 SER CB C 62.14 . 1 98 . 13 SER N N 117.90 . 1 99 . 14 GLY H H 8.16 . 1 100 . 14 GLY HA2 H 3.56 . 1 101 . 14 GLY HA3 H 4.62 . 1 102 . 14 GLY CA C 41.27 . 1 103 . 14 GLY N N 111.59 . 1 104 . 15 THR H H 8.41 . 1 105 . 15 THR HA H 4.34 . 1 106 . 15 THR HB H 4.16 . 1 107 . 15 THR HG2 H 1.20 . 1 108 . 15 THR CA C 60.85 . 1 109 . 15 THR CB C 67.82 . 1 110 . 15 THR N N 114.10 . 1 111 . 16 GLY H H 9.77 . 1 112 . 16 GLY HA2 H 3.37 . 1 113 . 16 GLY HA3 H 3.71 . 1 114 . 16 GLY CA C 45.69 . 1 115 . 16 GLY N N 111.38 . 1 116 . 17 LEU H H 7.94 . 1 117 . 17 LEU HA H 2.88 . 1 118 . 17 LEU HB2 H 1.58 . 1 119 . 17 LEU HB3 H 0.23 . 1 120 . 17 LEU HG H 0.92 . 1 121 . 17 LEU HD1 H 0.55 . 1 122 . 17 LEU HD2 H 0.47 . 1 123 . 17 LEU CA C 53.45 . 1 124 . 17 LEU CB C 34.68 . 1 125 . 17 LEU N N 113.90 . 1 126 . 18 SER H H 6.38 . 1 127 . 18 SER HA H 4.52 . 1 128 . 18 SER HB2 H 3.67 . 1 129 . 18 SER HB3 H 3.80 . 1 130 . 18 SER CA C 55.13 . 1 131 . 18 SER CB C 64.71 . 1 132 . 18 SER N N 113.48 . 1 133 . 19 GLY H H 8.23 . 1 134 . 19 GLY HA2 H 4.14 . 1 135 . 19 GLY HA3 H 3.60 . 1 136 . 19 GLY CA C 43.11 . 1 137 . 19 GLY N N 107.01 . 1 138 . 20 ALA H H 8.20 . 1 139 . 20 ALA HA H 4.29 . 1 140 . 20 ALA HB H 1.30 . 1 141 . 20 ALA CA C 50.55 . 1 142 . 20 ALA CB C 18.17 . 1 143 . 20 ALA N N 125.18 . 1 144 . 21 ARG H H 8.63 . 1 145 . 21 ARG HA H 4.82 . 1 146 . 21 ARG HB2 H 1.52 . 1 147 . 21 ARG HB3 H 1.79 . 1 148 . 21 ARG HG2 H 0.96 . 1 149 . 21 ARG HG3 H 0.96 . 1 150 . 21 ARG HD2 H 3.17 . 1 151 . 21 ARG HD3 H 3.25 . 1 152 . 21 ARG CA C 52.88 . 1 153 . 21 ARG CB C 31.86 . 1 154 . 21 ARG N N 126.93 . 1 155 . 22 THR H H 8.97 . 1 156 . 22 THR HA H 4.38 . 1 157 . 22 THR HB H 4.06 . 1 158 . 22 THR HG2 H 1.01 . 1 159 . 22 THR CA C 60.81 . 1 160 . 22 THR CB C 68.46 . 1 161 . 22 THR N N 126.87 . 1 162 . 23 VAL H H 8.63 . 1 163 . 23 VAL HA H 4.42 . 1 164 . 23 VAL HB H 1.90 . 1 165 . 23 VAL HG1 H 0.81 . 1 166 . 23 VAL HG2 H 0.77 . 1 167 . 23 VAL CA C 60.70 . 1 168 . 23 VAL CB C 31.71 . 1 169 . 23 VAL N N 127.57 . 1 170 . 24 ILE H H 9.42 . 1 171 . 24 ILE HA H 4.57 . 1 172 . 24 ILE HB H 1.78 . 1 173 . 24 ILE HG12 H 1.00 . 1 174 . 24 ILE HG13 H 1.00 . 1 175 . 24 ILE HG2 H 0.93 . 1 176 . 24 ILE HD1 H 0.63 . 1 177 . 24 ILE CA C 56.72 . 1 178 . 24 ILE CB C 39.12 . 1 179 . 24 ILE N N 132.62 . 1 180 . 25 PRO HA H 4.46 . 1 181 . 25 PRO HB2 H 2.35 . 1 182 . 25 PRO HB3 H 2.05 . 1 183 . 25 PRO HG2 H 2.16 . 1 184 . 25 PRO HG3 H 2.16 . 1 185 . 25 PRO HD2 H 3.56 . 1 186 . 25 PRO HD3 H 3.79 . 1 187 . 25 PRO CA C 61.43 . 1 188 . 25 PRO CB C 30.95 . 1 189 . 26 ALA H H 8.36 . 1 190 . 26 ALA HA H 3.94 . 1 191 . 26 ALA HB H 1.47 . 1 192 . 26 ALA CA C 54.24 . 1 193 . 26 ALA CB C 17.30 . 1 194 . 26 ALA N N 124.80 . 1 195 . 27 SER H H 8.55 . 1 196 . 27 SER HA H 4.29 . 1 197 . 27 SER HB2 H 3.93 . 1 198 . 27 SER HB3 H 3.98 . 1 199 . 27 SER CA C 59.42 . 1 200 . 27 SER CB C 60.41 . 1 201 . 27 SER N N 112.19 . 1 202 . 28 ASP H H 7.60 . 1 203 . 28 ASP HA H 4.45 . 1 204 . 28 ASP HB2 H 2.46 . 1 205 . 28 ASP HB3 H 2.85 . 1 206 . 28 ASP CA C 55.92 . 1 207 . 28 ASP CB C 37.78 . 1 208 . 28 ASP N N 124.43 . 1 209 . 29 MET H H 7.34 . 1 210 . 29 MET HA H 4.17 . 1 211 . 29 MET HB2 H 1.93 . 1 212 . 29 MET HB3 H 2.38 . 1 213 . 29 MET HG2 H 2.34 . 1 214 . 29 MET HG3 H 2.34 . 1 215 . 29 MET CA C 56.89 . 1 216 . 29 MET CB C 29.93 . 1 217 . 29 MET N N 119.96 . 1 218 . 30 GLU H H 8.29 . 1 219 . 30 GLU HA H 3.95 . 1 220 . 30 GLU HB2 H 2.09 . 1 221 . 30 GLU HB3 H 2.09 . 1 222 . 30 GLU HG2 H 2.36 . 1 223 . 30 GLU HG3 H 2.36 . 1 224 . 30 GLU CA C 57.80 . 1 225 . 30 GLU CB C 28.22 . 1 226 . 30 GLU N N 123.08 . 1 227 . 31 LYS H H 7.96 . 1 228 . 31 LYS HA H 4.04 . 1 229 . 31 LYS HB2 H 1.87 . 1 230 . 31 LYS HB3 H 1.87 . 1 231 . 31 LYS HG2 H 1.50 . 1 232 . 31 LYS HG3 H 1.58 . 1 233 . 31 LYS HD2 H 1.68 . 1 234 . 31 LYS HD3 H 1.68 . 1 235 . 31 LYS HE2 H 2.96 . 1 236 . 31 LYS HE3 H 2.96 . 1 237 . 31 LYS CA C 57.80 . 1 238 . 31 LYS CB C 31.12 . 1 239 . 31 LYS N N 119.58 . 1 240 . 32 ALA H H 7.22 . 1 241 . 32 ALA HA H 4.25 . 1 242 . 32 ALA HB H 1.40 . 1 243 . 32 ALA CA C 51.84 . 1 244 . 32 ALA CB C 18.12 . 1 245 . 32 ALA N N 120.55 . 1 246 . 33 GLY H H 7.26 . 1 247 . 33 GLY HA2 H 4.06 . 1 248 . 33 GLY HA3 H 4.16 . 1 249 . 33 GLY CA C 45.27 . 1 250 . 33 GLY N N 104.49 . 1 251 . 34 THR H H 9.14 . 1 252 . 34 THR HA H 4.37 . 1 253 . 34 THR HB H 4.19 . 1 254 . 34 THR HG2 H 1.15 . 1 255 . 34 THR CA C 62.14 . 1 256 . 34 THR CB C 66.37 . 1 257 . 34 THR N N 120.74 . 1 258 . 35 ASP H H 8.17 . 1 259 . 35 ASP HA H 4.58 . 1 260 . 35 ASP HB2 H 2.76 . 1 261 . 35 ASP HB3 H 3.07 . 1 262 . 35 ASP CA C 55.90 . 1 263 . 35 ASP CB C 39.41 . 1 264 . 35 ASP N N 122.52 . 1 265 . 36 GLY H H 6.58 . 1 266 . 36 GLY HA2 H 3.64 . 1 267 . 36 GLY HA3 H 3.79 . 1 268 . 36 GLY CA C 42.63 . 1 269 . 36 GLY N N 101.57 . 1 270 . 37 VAL H H 9.05 . 1 271 . 37 VAL HA H 4.18 . 1 272 . 37 VAL HB H 1.77 . 1 273 . 37 VAL HG1 H 0.72 . 1 274 . 37 VAL HG2 H 0.69 . 1 275 . 37 VAL CA C 58.89 . 1 276 . 37 VAL CB C 33.02 . 1 277 . 37 VAL N N 118.77 . 1 278 . 38 LYS H H 8.34 . 1 279 . 38 LYS HA H 4.39 . 1 280 . 38 LYS HB2 H 1.60 . 1 281 . 38 LYS HB3 H 1.60 . 1 282 . 38 LYS HG2 H 1.33 . 1 283 . 38 LYS HG3 H 1.42 . 1 284 . 38 LYS CA C 54.86 . 1 285 . 38 LYS CB C 31.00 . 1 286 . 38 LYS N N 128.10 . 1 287 . 39 LEU H H 8.48 . 1 288 . 39 LEU HA H 4.25 . 1 289 . 39 LEU HB2 H 1.89 . 1 290 . 39 LEU HB3 H 1.08 . 1 291 . 39 LEU HG H 1.56 . 1 292 . 39 LEU HD1 H 0.54 . 1 293 . 39 LEU HD2 H 0.43 . 1 294 . 39 LEU CA C 51.23 . 1 295 . 39 LEU CB C 37.96 . 1 296 . 39 LEU N N 125.38 . 1 297 . 40 PRO HA H 4.36 . 1 298 . 40 PRO HB2 H 1.87 . 1 299 . 40 PRO HB3 H 2.33 . 1 300 . 40 PRO HG2 H 1.78 . 1 301 . 40 PRO HG3 H 1.97 . 1 302 . 40 PRO HD2 H 3.68 . 1 303 . 40 PRO HD3 H 3.32 . 1 304 . 40 PRO CA C 61.15 . 1 305 . 40 PRO CB C 30.71 . 1 306 . 41 ALA H H 8.59 . 1 307 . 41 ALA HA H 4.06 . 1 308 . 41 ALA HB H 1.40 . 1 309 . 41 ALA CA C 52.90 . 1 310 . 41 ALA CB C 16.77 . 1 311 . 41 ALA N N 126.86 . 1 312 . 42 SER H H 7.56 . 1 313 . 42 SER HA H 4.12 . 1 314 . 42 SER HB2 H 3.81 . 1 315 . 42 SER HB3 H 3.90 . 1 316 . 42 SER CA C 56.06 . 1 317 . 42 SER CB C 62.12 . 1 318 . 42 SER N N 109.27 . 1 319 . 43 ALA H H 7.50 . 1 320 . 43 ALA HA H 4.23 . 1 321 . 43 ALA HB H 1.32 . 1 322 . 43 ALA CA C 51.81 . 1 323 . 43 ALA CB C 17.82 . 1 324 . 43 ALA N N 124.48 . 1 325 . 44 ARG H H 9.36 . 1 326 . 44 ARG HA H 4.53 . 1 327 . 44 ARG HB2 H 1.85 . 1 328 . 44 ARG HB3 H 1.19 . 1 329 . 44 ARG HG2 H 1.56 . 1 330 . 44 ARG HG3 H 1.43 . 1 331 . 44 ARG HD2 H 3.26 . 1 332 . 44 ARG HD3 H 3.26 . 1 333 . 44 ARG CA C 53.57 . 1 334 . 44 ARG CB C 31.42 . 1 335 . 44 ARG N N 121.08 . 1 336 . 45 SER H H 8.16 . 1 337 . 45 SER HA H 4.46 . 1 338 . 45 SER HB2 H 4.10 . 1 339 . 45 SER HB3 H 4.10 . 1 340 . 45 SER CA C 57.28 . 1 341 . 45 SER CB C 63.11 . 1 342 . 45 SER N N 110.02 . 1 343 . 46 PHE H H 8.52 . 1 344 . 46 PHE HA H 5.74 . 1 345 . 46 PHE HB2 H 3.01 . 1 346 . 46 PHE HB3 H 3.20 . 1 347 . 46 PHE HD1 H 6.79 . 1 348 . 46 PHE HD2 H 6.79 . 1 349 . 46 PHE HE1 H 7.10 . 1 350 . 46 PHE HE2 H 7.10 . 1 351 . 46 PHE HZ H 6.80 . 1 352 . 46 PHE CA C 55.91 . 1 353 . 46 PHE CB C 40.14 . 1 354 . 46 PHE N N 114.03 . 1 355 . 47 ALA H H 9.72 . 1 356 . 47 ALA HA H 4.77 . 1 357 . 47 ALA HB H 1.57 . 1 358 . 47 ALA CA C 49.45 . 1 359 . 47 ALA CB C 21.18 . 1 360 . 47 ALA N N 123.71 . 1 361 . 48 ASN H H 8.83 . 1 362 . 48 ASN HA H 4.92 . 1 363 . 48 ASN HB2 H 3.61 . 1 364 . 48 ASN HB3 H 2.23 . 1 365 . 48 ASN HD22 H 8.15 . 1 366 . 48 ASN HD21 H 6.50 . 1 367 . 48 ASN CA C 49.71 . 1 368 . 48 ASN CB C 36.99 . 1 369 . 48 ASN N N 120.79 . 1 370 . 48 ASN ND2 N 115.06 . 1 371 . 49 GLY H H 8.12 . 1 372 . 49 GLY HA2 H 3.81 . 1 373 . 49 GLY HA3 H 4.50 . 1 374 . 49 GLY CA C 44.80 . 1 375 . 49 GLY N N 117.38 . 1 376 . 50 THR H H 7.69 . 1 377 . 50 THR HA H 4.31 . 1 378 . 50 THR HB H 3.79 . 1 379 . 50 THR HG2 H 0.85 . 1 380 . 50 THR CA C 59.43 . 1 381 . 50 THR CB C 68.19 . 1 382 . 50 THR N N 113.13 . 1 383 . 51 HIS H H 7.99 . 1 384 . 51 HIS HA H 4.73 . 1 385 . 51 HIS HB2 H 2.97 . 1 386 . 51 HIS HB3 H 3.27 . 1 387 . 51 HIS HD2 H 6.96 . 4 388 . 51 HIS HE1 H 9.44 . 4 389 . 51 HIS CA C 52.87 . 1 390 . 51 HIS CB C 27.16 . 1 391 . 51 HIS N N 113.99 . 1 392 . 52 PHE H H 8.33 . 1 393 . 52 PHE HA H 5.07 . 1 394 . 52 PHE HB2 H 2.97 . 1 395 . 52 PHE HB3 H 3.14 . 1 396 . 52 PHE HD1 H 6.80 . 1 397 . 52 PHE HD2 H 6.80 . 1 398 . 52 PHE HE1 H 7.29 . 1 399 . 52 PHE HE2 H 7.29 . 1 400 . 52 PHE HZ H 7.18 . 1 401 . 52 PHE CA C 53.08 . 1 402 . 52 PHE CB C 39.27 . 1 403 . 52 PHE N N 121.10 . 1 404 . 53 THR H H 8.82 . 1 405 . 53 THR HA H 4.37 . 1 406 . 53 THR HB H 4.21 . 1 407 . 53 THR HG2 H 1.15 . 1 408 . 53 THR CA C 62.67 . 1 409 . 53 THR CB C 67.25 . 1 410 . 53 THR N N 120.79 . 1 411 . 54 LEU H H 8.56 . 1 412 . 54 LEU HA H 5.29 . 1 413 . 54 LEU HB2 H 1.56 . 1 414 . 54 LEU HB3 H 1.39 . 1 415 . 54 LEU HG H 1.76 . 1 416 . 54 LEU HD1 H 0.71 . 1 417 . 54 LEU HD2 H 0.66 . 1 418 . 54 LEU CA C 50.84 . 1 419 . 54 LEU CB C 42.21 . 1 420 . 54 LEU N N 127.57 . 1 421 . 55 ARG H H 9.25 . 1 422 . 55 ARG HA H 4.96 . 1 423 . 55 ARG HB2 H 1.81 . 1 424 . 55 ARG HB3 H 2.05 . 1 425 . 55 ARG HG2 H 0.95 . 1 426 . 55 ARG HG3 H 0.95 . 1 427 . 55 ARG HD2 H 2.43 . 1 428 . 55 ARG HD3 H 2.84 . 1 429 . 55 ARG CA C 52.90 . 1 430 . 55 ARG CB C 32.63 . 1 431 . 55 ARG N N 122.92 . 1 432 . 56 TYR H H 7.83 . 1 433 . 56 TYR HA H 5.87 . 1 434 . 56 TYR HB2 H 2.77 . 1 435 . 56 TYR HB3 H 2.77 . 1 436 . 56 TYR HD1 H 6.64 . 1 437 . 56 TYR HD2 H 6.64 . 1 438 . 56 TYR HE1 H 6.43 . 1 439 . 56 TYR HE2 H 6.43 . 1 440 . 56 TYR CA C 53.97 . 1 441 . 56 TYR CB C 41.43 . 1 442 . 56 TYR N N 114.77 . 1 443 . 57 GLY H H 8.90 . 1 444 . 57 GLY HA2 H 3.71 . 1 445 . 57 GLY HA3 H 5.47 . 1 446 . 57 GLY CA C 44.10 . 1 447 . 57 GLY N N 108.65 . 1 448 . 58 PRO HA H 4.72 . 1 449 . 58 PRO HB2 H 2.23 . 1 450 . 58 PRO HB3 H 1.98 . 1 451 . 58 PRO HG2 H 2.02 . 1 452 . 58 PRO HG3 H 2.13 . 1 453 . 58 PRO HD2 H 3.86 . 1 454 . 58 PRO HD3 H 3.44 . 1 455 . 58 PRO CA C 61.29 . 1 456 . 58 PRO CB C 30.77 . 1 457 . 59 ALA H H 8.27 . 1 458 . 59 ALA HA H 4.32 . 1 459 . 59 ALA HB H 1.44 . 1 460 . 59 ALA CA C 51.66 . 1 461 . 59 ALA CB C 17.99 . 1 462 . 59 ALA N N 125.42 . 1 463 . 60 ARG H H 7.93 . 1 464 . 60 ARG HA H 4.39 . 1 465 . 60 ARG HB2 H 1.59 . 1 466 . 60 ARG HB3 H 1.70 . 1 467 . 60 ARG HG2 H 1.29 . 1 468 . 60 ARG HG3 H 1.38 . 1 469 . 60 ARG CA C 53.95 . 1 470 . 60 ARG CB C 30.54 . 1 471 . 60 ARG N N 122.19 . 1 472 . 61 LYS H H 8.24 . 1 473 . 61 LYS HA H 4.65 . 1 474 . 61 LYS HB2 H 1.70 . 1 475 . 61 LYS HB3 H 1.66 . 1 476 . 61 LYS HG2 H 1.31 . 1 477 . 61 LYS HG3 H 1.41 . 1 478 . 61 LYS HE2 H 2.95 . 1 479 . 61 LYS HE3 H 2.95 . 1 480 . 61 LYS CA C 54.24 . 1 481 . 61 LYS CB C 30.77 . 1 482 . 61 LYS N N 125.56 . 1 483 . 62 VAL H H 8.42 . 1 484 . 62 VAL HA H 4.51 . 1 485 . 62 VAL HB H 1.93 . 1 486 . 62 VAL HG2 H 0.75 . 2 487 . 62 VAL CA C 58.70 . 1 488 . 62 VAL CB C 34.61 . 1 489 . 62 VAL N N 124.59 . 1 490 . 63 THR H H 8.26 . 1 491 . 63 THR HA H 4.46 . 1 492 . 63 THR HB H 4.01 . 1 493 . 63 THR HG2 H 1.14 . 1 494 . 63 THR CA C 60.02 . 1 495 . 63 THR CB C 68.17 . 1 496 . 63 THR N N 121.17 . 1 497 . 64 CYS H H 8.67 . 1 498 . 64 CYS HA H 4.91 . 1 499 . 64 CYS HB2 H 3.25 . 1 500 . 64 CYS HB3 H 2.77 . 1 501 . 64 CYS CA C 53.39 . 1 502 . 64 CYS CB C 39.82 . 1 503 . 64 CYS N N 123.91 . 1 504 . 65 VAL H H 8.42 . 1 505 . 65 VAL HA H 4.15 . 1 506 . 65 VAL HB H 2.15 . 1 507 . 65 VAL HG2 H 0.86 . 2 508 . 65 VAL CA C 61.01 . 1 509 . 65 VAL CB C 30.95 . 1 510 . 65 VAL N N 119.43 . 1 511 . 66 ARG H H 7.32 . 1 512 . 66 ARG HA H 4.51 . 1 513 . 66 ARG HB2 H 1.71 . 1 514 . 66 ARG HB3 H 1.79 . 1 515 . 66 ARG HG2 H 1.35 . 1 516 . 66 ARG HG3 H 1.48 . 1 517 . 66 ARG HD2 H 3.18 . 1 518 . 66 ARG HD3 H 3.10 . 1 519 . 66 ARG CA C 52.97 . 1 520 . 66 ARG CB C 30.89 . 1 521 . 66 ARG N N 118.95 . 1 522 . 67 PHE H H 8.16 . 1 523 . 67 PHE HA H 4.40 . 1 524 . 67 PHE HB2 H 2.82 . 1 525 . 67 PHE HB3 H 2.96 . 1 526 . 67 PHE HD1 H 7.21 . 1 527 . 67 PHE HD2 H 7.21 . 1 528 . 67 PHE HE1 H 7.33 . 1 529 . 67 PHE HE2 H 7.33 . 1 530 . 67 PHE HZ H 7.28 . 1 531 . 67 PHE CA C 53.21 . 1 532 . 67 PHE CB C 39.10 . 1 533 . 67 PHE N N 123.48 . 1 534 . 68 PRO HA H 4.55 . 1 535 . 68 PRO HB2 H 2.36 . 1 536 . 68 PRO HB3 H 2.06 . 1 537 . 68 PRO HG2 H 1.98 . 1 538 . 68 PRO HG3 H 1.98 . 1 539 . 68 PRO HD2 H 3.88 . 1 540 . 68 PRO HD3 H 3.74 . 1 541 . 68 PRO CA C 50.12 . 1 542 . 68 PRO CB C 31.64 . 1 543 . 69 CYS H H 8.52 . 1 544 . 69 CYS HA H 4.76 . 1 545 . 69 CYS HB2 H 3.02 . 1 546 . 69 CYS HB3 H 2.77 . 1 547 . 69 CYS CA C 49.97 . 1 548 . 69 CYS CB C 35.39 . 1 549 . 69 CYS N N 126.37 . 1 550 . 70 TYR H H 7.25 . 1 551 . 70 TYR HA H 4.44 . 1 552 . 70 TYR HB2 H 1.93 . 1 553 . 70 TYR HB3 H 2.27 . 1 554 . 70 TYR HD1 H 6.98 . 1 555 . 70 TYR HD2 H 6.98 . 1 556 . 70 TYR HE1 H 6.89 . 1 557 . 70 TYR HE2 H 6.89 . 1 558 . 70 TYR CA C 57.99 . 1 559 . 70 TYR CB C 36.88 . 1 560 . 70 TYR N N 124.76 . 1 561 . 71 GLN H H 8.16 . 1 562 . 71 GLN HA H 4.57 . 1 563 . 71 GLN HB2 H 2.75 . 1 564 . 71 GLN HB3 H 2.14 . 1 565 . 71 GLN HG2 H 2.65 . 1 566 . 71 GLN HG3 H 2.42 . 1 567 . 71 GLN HE22 H 7.22 . 1 568 . 71 GLN HE21 H 6.88 . 1 569 . 71 GLN CA C 52.04 . 1 570 . 71 GLN CB C 25.39 . 1 571 . 71 GLN N N 124.00 . 1 572 . 71 GLN NE2 N 118.31 . 1 573 . 72 TYR H H 6.99 . 1 574 . 72 TYR HA H 4.87 . 1 575 . 72 TYR HB2 H 2.91 . 1 576 . 72 TYR HB3 H 2.38 . 1 577 . 72 TYR HD1 H 6.36 . 1 578 . 72 TYR HD2 H 6.36 . 1 579 . 72 TYR HE1 H 6.16 . 1 580 . 72 TYR HE2 H 6.16 . 1 581 . 72 TYR CA C 54.00 . 1 582 . 72 TYR CB C 36.80 . 1 583 . 72 TYR N N 117.06 . 1 584 . 73 ALA H H 8.56 . 1 585 . 73 ALA HA H 4.25 . 1 586 . 73 ALA HB H 1.20 . 1 587 . 73 ALA CA C 48.83 . 1 588 . 73 ALA CB C 17.85 . 1 589 . 73 ALA N N 126.86 . 1 590 . 74 THR H H 8.11 . 1 591 . 74 THR HA H 3.89 . 1 592 . 74 THR HB H 3.84 . 1 593 . 74 THR HG2 H 0.86 . 1 594 . 74 THR CA C 62.35 . 1 595 . 74 THR CB C 67.23 . 1 596 . 74 THR N N 118.76 . 1 597 . 75 VAL H H 9.59 . 1 598 . 75 VAL HA H 3.99 . 1 599 . 75 VAL HB H 1.89 . 1 600 . 75 VAL HG1 H 0.96 . 1 601 . 75 VAL HG2 H 0.91 . 1 602 . 75 VAL CA C 61.00 . 1 603 . 75 VAL CB C 30.76 . 1 604 . 75 VAL N N 130.09 . 1 605 . 76 GLY H H 6.76 . 1 606 . 76 GLY HA2 H 3.64 . 1 607 . 76 GLY HA3 H 4.01 . 1 608 . 76 GLY CA C 43.03 . 1 609 . 76 GLY N N 107.93 . 1 610 . 77 LYS H H 8.06 . 1 611 . 77 LYS HA H 5.55 . 1 612 . 77 LYS HB2 H 1.55 . 1 613 . 77 LYS HB3 H 1.49 . 1 614 . 77 LYS HG2 H 1.07 . 1 615 . 77 LYS HG3 H 1.26 . 1 616 . 77 LYS CA C 52.99 . 1 617 . 77 LYS CB C 35.73 . 1 618 . 77 LYS N N 116.77 . 1 619 . 78 VAL H H 9.37 . 1 620 . 78 VAL HA H 4.41 . 1 621 . 78 VAL HB H 1.99 . 1 622 . 78 VAL HG1 H 0.99 . 1 623 . 78 VAL HG2 H 0.94 . 1 624 . 78 VAL CA C 59.67 . 1 625 . 78 VAL CB C 33.40 . 1 626 . 78 VAL N N 122.86 . 1 627 . 79 ALA H H 8.84 . 1 628 . 79 ALA HA H 4.56 . 1 629 . 79 ALA HB H 1.47 . 1 630 . 79 ALA CA C 50.11 . 1 631 . 79 ALA CB C 15.69 . 1 632 . 79 ALA N N 133.77 . 1 633 . 80 PRO HA H 4.09 . 1 634 . 80 PRO HB2 H 2.26 . 1 635 . 80 PRO HB3 H 1.78 . 1 636 . 80 PRO CA C 63.25 . 1 637 . 80 PRO CB C 30.16 . 1 638 . 81 GLY H H 8.31 . 1 639 . 81 GLY HA2 H 3.81 . 1 640 . 81 GLY HA3 H 4.17 . 1 641 . 81 GLY CA C 44.66 . 1 642 . 81 GLY N N 116.10 . 1 643 . 82 ALA H H 8.04 . 1 644 . 82 ALA HA H 4.65 . 1 645 . 82 ALA HB H 1.61 . 1 646 . 82 ALA CA C 49.48 . 1 647 . 82 ALA CB C 19.57 . 1 648 . 82 ALA N N 124.25 . 1 649 . 83 GLN H H 8.11 . 1 650 . 83 GLN HA H 4.83 . 1 651 . 83 GLN HB2 H 1.95 . 1 652 . 83 GLN HB3 H 1.91 . 1 653 . 83 GLN HG2 H 2.22 . 1 654 . 83 GLN HG3 H 2.08 . 1 655 . 83 GLN HE22 H 7.37 . 1 656 . 83 GLN HE21 H 6.56 . 1 657 . 83 GLN CA C 52.33 . 1 658 . 83 GLN CB C 30.47 . 1 659 . 83 GLN N N 115.33 . 1 660 . 83 GLN NE2 N 112.23 . 1 661 . 84 LEU H H 8.57 . 1 662 . 84 LEU HA H 4.50 . 1 663 . 84 LEU HB2 H 0.25 . 1 664 . 84 LEU HB3 H 0.54 . 1 665 . 84 LEU HG H 0.88 . 1 666 . 84 LEU HD1 H 0.04 . 2 667 . 84 LEU CA C 51.99 . 1 668 . 84 LEU CB C 41.08 . 1 669 . 84 LEU N N 124.79 . 1 670 . 85 ARG H H 8.66 . 1 671 . 85 ARG HA H 3.69 . 1 672 . 85 ARG HB2 H 1.75 . 1 673 . 85 ARG HB3 H 1.87 . 1 674 . 85 ARG HG2 H 1.34 . 1 675 . 85 ARG HG3 H 1.63 . 1 676 . 85 ARG HD2 H 3.12 . 1 677 . 85 ARG HD3 H 3.21 . 1 678 . 85 ARG CA C 58.43 . 1 679 . 85 ARG CB C 29.15 . 1 680 . 85 ARG N N 125.37 . 1 681 . 86 SER H H 7.24 . 1 682 . 86 SER HA H 4.85 . 1 683 . 86 SER HB2 H 3.71 . 1 684 . 86 SER HB3 H 3.71 . 1 685 . 86 SER CA C 55.54 . 1 686 . 86 SER CB C 62.49 . 1 687 . 86 SER N N 111.20 . 1 688 . 87 LEU H H 8.19 . 1 689 . 87 LEU HA H 4.38 . 1 690 . 87 LEU HB2 H 1.48 . 1 691 . 87 LEU HB3 H 1.48 . 1 692 . 87 LEU HG H 1.27 . 1 693 . 87 LEU HD1 H 0.66 . 1 694 . 87 LEU HD2 H 0.60 . 1 695 . 87 LEU CA C 51.06 . 1 696 . 87 LEU CB C 40.63 . 1 697 . 87 LEU N N 126.78 . 1 698 . 88 PRO HA H 4.79 . 1 699 . 88 PRO HB2 H 2.13 . 1 700 . 88 PRO HB3 H 2.32 . 1 701 . 88 PRO HG2 H 1.94 . 1 702 . 88 PRO HG3 H 1.94 . 1 703 . 88 PRO CA C 62.01 . 1 704 . 88 PRO CB C 30.48 . 1 705 . 89 SER H H 7.99 . 1 706 . 89 SER HA H 4.53 . 1 707 . 89 SER HB2 H 3.74 . 1 708 . 89 SER HB3 H 3.81 . 1 709 . 89 SER CA C 54.51 . 1 710 . 89 SER CB C 61.48 . 1 711 . 89 SER N N 113.99 . 1 712 . 90 PRO HA H 4.37 . 1 713 . 90 PRO HB2 H 1.93 . 1 714 . 90 PRO HB3 H 2.22 . 1 715 . 90 PRO HG2 H 2.02 . 1 716 . 90 PRO HG3 H 2.02 . 1 717 . 90 PRO HD2 H 3.67 . 1 718 . 90 PRO HD3 H 3.64 . 1 719 . 90 PRO CA C 62.20 . 1 720 . 90 PRO CB C 30.24 . 1 721 . 91 GLY H H 8.62 . 1 722 . 91 GLY HA2 H 3.69 . 1 723 . 91 GLY HA3 H 4.14 . 1 724 . 91 GLY CA C 44.71 . 1 725 . 91 GLY N N 112.94 . 1 726 . 92 ALA H H 7.95 . 1 727 . 92 ALA HA H 4.53 . 1 728 . 92 ALA HB H 1.40 . 1 729 . 92 ALA CA C 50.18 . 1 730 . 92 ALA CB C 18.42 . 1 731 . 92 ALA N N 123.92 . 1 732 . 93 THR H H 8.16 . 1 733 . 93 THR HA H 4.30 . 1 734 . 93 THR HB H 4.14 . 1 735 . 93 THR HG2 H 1.13 . 1 736 . 93 THR CA C 60.86 . 1 737 . 93 THR CB C 67.91 . 1 738 . 93 THR N N 115.10 . 1 739 . 94 VAL H H 8.67 . 1 740 . 94 VAL HA H 3.89 . 1 741 . 94 VAL HB H 1.98 . 1 742 . 94 VAL HG1 H 0.91 . 1 743 . 94 VAL HG2 H 0.85 . 1 744 . 94 VAL CA C 61.28 . 1 745 . 94 VAL CB C 31.84 . 1 746 . 94 VAL N N 129.13 . 1 747 . 95 THR H H 8.70 . 1 748 . 95 THR HA H 4.71 . 1 749 . 95 THR HB H 3.60 . 1 750 . 95 THR HG2 H 0.56 . 1 751 . 95 THR CA C 60.25 . 1 752 . 95 THR CB C 68.90 . 1 753 . 95 THR N N 126.57 . 1 754 . 96 VAL H H 8.54 . 1 755 . 96 VAL HA H 5.01 . 1 756 . 96 VAL HB H 1.47 . 1 757 . 96 VAL HG1 H 0.53 . 1 758 . 96 VAL HG2 H 0.49 . 1 759 . 96 VAL CA C 56.86 . 1 760 . 96 VAL CB C 33.36 . 1 761 . 96 VAL N N 122.36 . 1 762 . 97 GLY H H 8.61 . 1 763 . 97 GLY HA2 H 3.79 . 1 764 . 97 GLY HA3 H 4.67 . 1 765 . 97 GLY CA C 42.90 . 1 766 . 97 GLY N N 110.70 . 1 767 . 98 GLN H H 9.16 . 1 768 . 98 GLN HA H 3.94 . 1 769 . 98 GLN HB2 H 1.59 . 1 770 . 98 GLN HB3 H 1.32 . 1 771 . 98 GLN HG2 H 1.76 . 1 772 . 98 GLN HG3 H 1.76 . 1 773 . 98 GLN HE22 H 6.29 . 1 774 . 98 GLN HE21 H 5.95 . 1 775 . 98 GLN CA C 54.99 . 1 776 . 98 GLN CB C 27.90 . 1 777 . 98 GLN N N 122.13 . 1 778 . 98 GLN NE2 N 108.77 . 1 779 . 99 ASP H H 8.50 . 1 780 . 99 ASP HA H 4.32 . 1 781 . 99 ASP HB2 H 2.84 . 1 782 . 99 ASP HB3 H 2.12 . 1 783 . 99 ASP CA C 53.98 . 1 784 . 99 ASP CB C 39.43 . 1 785 . 99 ASP N N 123.77 . 1 786 . 100 LEU H H 8.32 . 1 787 . 100 LEU HA H 4.55 . 1 788 . 100 LEU HB2 H 1.74 . 1 789 . 100 LEU HB3 H 1.39 . 1 790 . 100 LEU HG H 1.50 . 1 791 . 100 LEU HD1 H 0.77 . 1 792 . 100 LEU HD2 H 0.82 . 1 793 . 100 LEU CA C 52.60 . 1 794 . 100 LEU CB C 40.74 . 1 795 . 100 LEU N N 133.26 . 1 796 . 101 GLY H H 8.06 . 1 797 . 101 GLY HA2 H 3.75 . 1 798 . 101 GLY HA3 H 4.43 . 1 799 . 101 GLY CA C 42.20 . 1 800 . 101 GLY N N 110.06 . 1 801 . 102 ASP H H 8.09 . 1 802 . 102 ASP HA H 4.70 . 1 803 . 102 ASP HB2 H 2.37 . 1 804 . 102 ASP HB3 H 2.76 . 1 805 . 102 ASP CA C 54.41 . 1 806 . 102 ASP CB C 41.49 . 1 807 . 102 ASP N N 124.94 . 1 stop_ save_