data_4077 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, 15N Assignments and Secondary Structure of the FK506 Binding Protein When Bound to Ascomycin ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Robert X. . 2 Nettesheim David . . 3 Olejniczak Edward T. . 4 Meadows Robert . . 5 Gemmecker Gerd . . 6 Fesik Stephen W. . stop_ _BMRB_accession_number 4077 _BMRB_flat_file_name bmr4077.str _Entry_type reformat _Submission_date 1997-12-07 _Accession_date 1997-12-07 _Entry_origination BMRB _NMR_STAR_version 2.1 _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' 626 '13C chemical shifts' 470 '15N chemical shifts' 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-15 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Xu, R. X, Nettesheim, D., Olejniczak, E. T., Meadows, R., Gemmecker, G., and Fesik, S. W., "1H, 13C, 15N Assignments and Secondary Structure of the FK506 Binding Protein when Bound to Ascomycin," Biopolymers 33, 535-550 (1993). ; _Citation_title ; 1H, 13C, 15N Assignments and Secondary Structure of the FK506 Binding Protein When Bound to Ascomycin ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 93222455 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Robert X. . 2 Nettesheim David . . 3 Olejniczak Edward T. . 4 Meadows Robert . . 5 Gemmecker Gerd . . 6 Fesik Stephen W. . stop_ _Journal_abbreviation Biopolymers _Journal_volume 33 _Journal_issue 4 _Page_first 535 _Page_last 550 _Year 1993 loop_ _Keyword NMR 'FK506 Binding Protein' 'peptidyl prolyl cis/trans isomerase (PPIase)' stop_ save_ ################################## # Molecular system description # ################################## save_FKBP-ascomycin-complex _Saveframe_category molecular_system _Mol_system_name "FK 506 Binding Protein bound to Ascomycin" _Abbreviation_common FKBP-ascomycin-complex loop_ _Mol_system_component_name _Mol_label FKBP $FKBP ascomycin $ascomycin stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully reduced' loop_ _Biological_function ; 'The complex elicits the immunosuppressant activity by binding to and modulating the effects of protein in T-cell activation' ; stop_ _Details ; FK506 Binding Protein (FKBP) from human T-cells is a peptidyl prolyl cis/trans isomerase that is inhibited by ascomycin, an FK506 analogue. ; save_ ######################## # Monomeric polymers # ######################## save_FKBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "FK 506 Binding Protein" _Abbreviation_common FKBP _Molecular_mass 11800 ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; GVQVETISPGDGRTFPKRGQ TCVVHYTGMLEDGKKFDSSR DRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDY AYGATGHPGIIPPHATLVFD VELLKLE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 VAL 3 3 GLN 4 4 VAL 5 5 GLU 6 6 THR 7 7 ILE 8 8 SER 9 9 PRO 10 10 GLY 11 11 ASP 12 12 GLY 13 13 ARG 14 14 THR 15 15 PHE 16 16 PRO 17 17 LYS 18 18 ARG 19 19 GLY 20 20 GLN 21 21 THR 22 22 CYS 23 23 VAL 24 24 VAL 25 25 HIS 26 26 TYR 27 27 THR 28 28 GLY 29 29 MET 30 30 LEU 31 31 GLU 32 32 ASP 33 33 GLY 34 34 LYS 35 35 LYS 36 36 PHE 37 37 ASP 38 38 SER 39 39 SER 40 40 ARG 41 41 ASP 42 42 ARG 43 43 ASN 44 44 LYS 45 45 PRO 46 46 PHE 47 47 LYS 48 48 PHE 49 49 MET 50 50 LEU 51 51 GLY 52 52 LYS 53 53 GLN 54 54 GLU 55 55 VAL 56 56 ILE 57 57 ARG 58 58 GLY 59 59 TRP 60 60 GLU 61 61 GLU 62 62 GLY 63 63 VAL 64 64 ALA 65 65 GLN 66 66 MET 67 67 SER 68 68 VAL 69 69 GLY 70 70 GLN 71 71 ARG 72 72 ALA 73 73 LYS 74 74 LEU 75 75 THR 76 76 ILE 77 77 SER 78 78 PRO 79 79 ASP 80 80 TYR 81 81 ALA 82 82 TYR 83 83 GLY 84 84 ALA 85 85 THR 86 86 GLY 87 87 HIS 88 88 PRO 89 89 GLY 90 90 ILE 91 91 ILE 92 92 PRO 93 93 PRO 94 94 HIS 95 95 ALA 96 96 THR 97 97 LEU 98 98 VAL 99 99 PHE 100 100 ASP 101 101 VAL 102 102 GLU 103 103 LEU 104 104 LEU 105 105 LYS 106 106 LEU 107 107 GLU 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 4076 "Outer Surface Protein A" 100.00 257 100.00 100.00 4.05e-171 PDB 1FJ1 "Lyme Disease Antigen Ospa In Complex With Neutralizing Antibody Fab La-2" 100.00 257 99.61 99.61 1.38e-170 PDB 1OSP "Crystal Structure Of Outer Surface Protein A Of Borrelia Burgdorferi Complexed With A Murine Monoclonal Antibody Fab" 100.00 257 99.61 99.61 1.38e-170 EMBL CAA32579 "ospA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA34487 "unnamed protein product [Borrelia burgdorferi ZS7]" 100.00 273 98.44 98.44 4.25e-167 EMBL CAA49314 "0spA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA56467 "ospA [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 EMBL CAA59729 "outer surface protein A [Borrelia burgdorferi 297]" 100.00 273 99.22 99.22 1.18e-168 GB AAA20947 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 GB AAA20949 "OspA, partial [Borrelia burgdorferi]" 97.28 250 99.20 99.20 6.94e-164 GB AAA20951 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 GB AAA20953 "OspA, partial [Borrelia burgdorferi]" 97.28 250 98.80 99.20 3.10e-163 GB AAA20955 "OspA, partial [Borrelia burgdorferi]" 97.28 250 100.00 100.00 9.13e-166 REF NP_045688 "outer surface protein A [Borrelia burgdorferi B31]" 100.00 273 99.61 99.61 5.76e-170 REF WP_010258120 "outer surface protein A (ospA) [Borrelia burgdorferi]" 100.00 273 99.22 99.22 1.18e-168 REF WP_010890378 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 99.61 99.61 5.76e-170 REF WP_012615002 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 98.44 98.44 4.25e-167 REF WP_012665570 "outer surface protein A [Borrelia burgdorferi]" 100.00 273 98.83 98.83 6.93e-168 SP B7IZU3 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 98.44 98.44 4.25e-167 SP C6C2D6 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 98.83 98.83 6.93e-168 SP P0CL66 "RecName: Full=Outer surface protein A; Flags: Precursor" 100.00 273 99.61 99.61 5.76e-170 stop_ save_ ############# # Ligands # ############# save_ascomycin _Saveframe_category ligand _Mol_type non-polymer _Name_common ascomycin _Mol_empirical_formula ? _Molecular_mass ? _Mol_charge ? _Mol_paramagnetic no save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Cell_line _Cell_type $FKBP Human 9606 Eukaryota Metazoa Homo sapiens 'Jurket T cell' 'T cell' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Gene_source $FKBP 'recombinant technology' 'E. coli' Escherichia coli 'natural source' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FKBP-ascomycin-complex 3 mM '[U-15N]' 'Potassium phosphate' 50 mM . 'Sodium choloride' 100 mM . 'dithiothreitol-d10' 5 mM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FKBP-ascomycin-complex 3 mM '[U-13C; U-15N]' 'Potassium phosphate' 50 mM . 'Sodium choloride' 100 mM . 'dithiothreitol-d10' 5 mM . stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method H2O H 1 protons ppm 4.74 . TSP C 13 'methyl protons' ppm 0.00 external (NH4)NO3 N 15 ? ppm 119.4 . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_FKBP-ascomycin-complex _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name FKBP 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 1 GLY HA2 H 3.24 . 2 2 1 GLY HA3 H 2.70 . 2 3 1 GLY C C 169.7 . 1 4 1 GLY CA C 42.2 . 1 5 2 VAL H H 8.58 . 1 6 2 VAL HA H 5.27 . 1 7 2 VAL HB H 1.89 . 1 8 2 VAL HG1 H 1.00 . 2 9 2 VAL HG2 H 0.87 . 2 10 2 VAL C C 173.6 . 1 11 2 VAL CA C 58.4 . 1 12 2 VAL CB C 35.4 . 1 13 2 VAL CG1 C 18.7 . 2 14 2 VAL CG2 C 22.6 . 2 15 2 VAL N N 120.0 . 1 16 3 GLN H H 8.59 . 1 17 3 GLN HA H 4.72 . 1 18 3 GLN HB2 H 2.13 . 2 19 3 GLN HB3 H 1.99 . 2 20 3 GLN HG2 H 2.33 . 1 21 3 GLN HG3 H 2.33 . 1 22 3 GLN C C 175.6 . 1 23 3 GLN CA C 54.0 . 1 24 3 GLN CB C 31.8 . 1 25 3 GLN CG C 34.1 . 1 26 3 GLN N N 126.9 . 1 27 4 VAL H H 8.85 . 1 28 4 VAL HA H 4.58 . 1 29 4 VAL HB H 2.05 . 1 30 4 VAL HG1 H 0.67 . 2 31 4 VAL HG2 H 0.80 . 2 32 4 VAL C C 176.3 . 1 33 4 VAL CA C 62.1 . 1 34 4 VAL CB C 33.4 . 1 35 4 VAL CG1 C 20.8 . 2 36 4 VAL CG2 C 21.4 . 2 37 4 VAL N N 124.8 . 1 38 5 GLU H H 9.04 . 1 39 5 GLU HA H 4.80 . 1 40 5 GLU HB2 H 2.13 . 2 41 5 GLU HB3 H 1.98 . 2 42 5 GLU HG2 H 2.25 . 1 43 5 GLU HG3 H 2.17 . 2 44 5 GLU C C 176.6 . 1 45 5 GLU CA C 54.3 . 1 46 5 GLU CB C 33.1 . 1 47 5 GLU CG C 36.8 . 1 48 5 GLU N N 128.0 . 1 49 6 THR H H 9.16 . 1 50 6 THR HA H 3.93 . 1 51 6 THR HB H 4.10 . 1 52 6 THR HG2 H 1.14 . 1 53 6 THR C C 174.2 . 1 54 6 THR CA C 66.8 . 1 55 6 THR CB C 68.8 . 1 56 6 THR CG2 C 22.6 . 1 57 6 THR N N 123.7 . 1 58 7 ILE H H 9.36 . 1 59 7 ILE HA H 4.11 . 1 60 7 ILE HB H 1.35 . 1 61 7 ILE HG12 H 1.58 . 2 62 7 ILE HG13 H 1.09 . 2 63 7 ILE HG2 H 0.91 . 1 64 7 ILE HD1 H 0.75 . 1 65 7 ILE C C 176.5 . 1 66 7 ILE CA C 63.4 . 1 67 7 ILE CB C 39.6 . 1 68 7 ILE CG1 C 28.1 . 1 69 7 ILE CG2 C 16.9 . 1 70 7 ILE CD1 C 13.5 . 1 71 7 ILE N N 128.9 . 1 72 8 SER H H 8.33 . 1 73 8 SER HA H 5.04 . 1 74 8 SER HB2 H 3.92 . 2 75 8 SER HB3 H 3.81 . 2 76 8 SER CA C 55.5 . 1 77 8 SER CB C 64.7 . 1 78 8 SER N N 114.0 . 1 79 9 PRO HA H 4.37 . 1 80 9 PRO HB2 H 2.34 . 2 81 9 PRO HB3 H 2.13 . 2 82 9 PRO HG2 H 2.08 . 1 83 9 PRO HG3 H 2.08 . 1 84 9 PRO HD2 H 3.85 . 2 85 9 PRO HD3 H 3.77 . 2 86 9 PRO C C 178.5 . 1 87 9 PRO CA C 63.9 . 1 88 9 PRO CB C 33.1 . 1 89 9 PRO CG C 27.4 . 1 90 9 PRO CD C 51.4 . 1 91 10 GLY H H 8.47 . 1 92 10 GLY HA2 H 4.17 . 2 93 10 GLY HA3 H 3.55 . 2 94 10 GLY C C 174.9 . 1 95 10 GLY CA C 44.3 . 1 96 10 GLY N N 107.2 . 1 97 11 ASP H H 8.04 . 1 98 11 ASP HA H 4.33 . 1 99 11 ASP HB2 H 3.02 . 2 100 11 ASP HB3 H 2.77 . 2 101 11 ASP C C 179.1 . 1 102 11 ASP CA C 54.8 . 1 103 11 ASP CB C 39.6 . 1 104 11 ASP N N 118.2 . 1 105 12 GLY H H 8.67 . 1 106 12 GLY HA2 H 4.05 . 2 107 12 GLY HA3 H 3.50 . 2 108 12 GLY C C 174.1 . 1 109 12 GLY CA C 46.1 . 1 110 12 GLY N N 107.6 . 1 111 13 ARG H H 8.53 . 1 112 13 ARG HA H 4.74 . 1 113 13 ARG HB2 H 1.78 . 2 114 13 ARG HB3 H 1.58 . 2 115 13 ARG HG2 H 1.58 . 2 116 13 ARG HG3 H 1.47 . 2 117 13 ARG HD2 H 3.20 . 1 118 13 ARG HD3 H 3.20 . 1 119 13 ARG C C 175.7 . 1 120 13 ARG CA C 56.8 . 1 121 13 ARG CB C 34.7 . 1 122 13 ARG CG C 27.1 . 1 123 13 ARG CD C 43.3 . 1 124 13 ARG N N 117.2 . 1 125 14 THR H H 10.27 . 1 126 14 THR HA H 4.24 . 1 127 14 THR HB H 4.28 . 1 128 14 THR HG2 H 1.13 . 1 129 14 THR C C 173.3 . 1 130 14 THR CA C 62.1 . 1 131 14 THR CB C 66.2 . 1 132 14 THR CG2 C 22.7 . 1 133 14 THR N N 124.7 . 1 134 15 PHE H H 8.11 . 1 135 15 PHE HA H 5.26 . 1 136 15 PHE HB2 H 3.13 . 2 137 15 PHE HB3 H 2.64 . 2 138 15 PHE HD1 H 7.08 . 1 139 15 PHE HD2 H 7.08 . 1 140 15 PHE HE1 H 7.15 . 1 141 15 PHE HE2 H 7.15 . 1 142 15 PHE CA C 54.8 . 1 143 15 PHE CB C 39.9 . 1 144 15 PHE CD1 C 132.7 . 1 145 15 PHE CD2 C 132.7 . 1 146 15 PHE CE1 C 130.8 . 1 147 15 PHE CE2 C 130.8 . 1 148 15 PHE N N 124.1 . 1 149 16 PRO HA H 4.40 . 1 150 16 PRO HB2 H 2.08 . 2 151 16 PRO HB3 H 1.71 . 2 152 16 PRO HG2 H 2.13 . 2 153 16 PRO HG3 H 1.85 . 2 154 16 PRO HD2 H 4.26 . 2 155 16 PRO HD3 H 4.10 . 2 156 16 PRO C C 176.3 . 1 157 16 PRO CA C 63.1 . 1 158 16 PRO CB C 33.6 . 1 159 16 PRO CG C 28.7 . 1 160 16 PRO CD C 51.6 . 1 161 17 LYS H H 8.48 . 1 162 17 LYS HA H 4.64 . 1 163 17 LYS HB2 H 1.86 . 2 164 17 LYS HB3 H 1.57 . 2 165 17 LYS HG2 H 1.53 . 1 166 17 LYS HG3 H 1.53 . 1 167 17 LYS HD2 H 1.71 . 2 168 17 LYS HD3 H 1.64 . 2 169 17 LYS HE2 H 3.04 . 1 170 17 LYS HE3 H 3.04 . 1 171 17 LYS C C 176.9 . 1 172 17 LYS CA C 53.7 . 1 173 17 LYS CB C 34.9 . 1 174 17 LYS CG C 25.0 . 1 175 17 LYS CD C 28.9 . 1 176 17 LYS CE C 42.8 . 1 177 17 LYS N N 120.7 . 1 178 18 ARG H H 8.44 . 1 179 18 ARG HA H 3.70 . 1 180 18 ARG HB2 H 1.82 . 1 181 18 ARG HB3 H 1.82 . 1 182 18 ARG HG2 H 1.79 . 2 183 18 ARG HG3 H 1.54 . 2 184 18 ARG HD2 H 3.27 . 1 185 18 ARG HD3 H 3.27 . 1 186 18 ARG CA C 58.9 . 1 187 18 ARG CB C 30.0 . 1 188 18 ARG CG C 28.4 . 1 189 18 ARG CD C 43.5 . 1 190 18 ARG N N 119.9 . 1 191 19 GLY H H 8.87 . 1 192 19 GLY HA2 H 4.42 . 2 193 19 GLY HA3 H 3.67 . 2 194 19 GLY C C 174.9 . 1 195 19 GLY CA C 45.1 . 1 196 19 GLY N N 112.1 . 1 197 20 GLN H H 8.13 . 1 198 20 GLN HA H 4.53 . 1 199 20 GLN HB2 H 2.29 . 2 200 20 GLN HB3 H 1.94 . 2 201 20 GLN HG2 H 2.34 . 2 202 20 GLN HG3 H 2.30 . 2 203 20 GLN C C 175.7 . 1 204 20 GLN CA C 56.3 . 1 205 20 GLN CB C 31.0 . 1 206 20 GLN CG C 36.0 . 1 207 20 GLN N N 118.2 . 1 208 21 THR H H 8.73 . 1 209 21 THR HA H 4.50 . 1 210 21 THR HB H 3.95 . 1 211 21 THR HG2 H 0.87 . 1 212 21 THR C C 174.7 . 1 213 21 THR CA C 63.1 . 1 214 21 THR CB C 69.1 . 1 215 21 THR CG2 C 21.6 . 1 216 21 THR N N 118.9 . 1 217 22 CYS H H 8.83 . 1 218 22 CYS HA H 4.40 . 1 219 22 CYS HB2 H 2.18 . 2 220 22 CYS HB3 H 2.00 . 2 221 22 CYS C C 173.6 . 1 222 22 CYS CA C 58.2 . 1 223 22 CYS CB C 29.4 . 1 224 22 CYS N N 125.2 . 1 225 23 VAL H H 8.13 . 1 226 23 VAL HA H 4.66 . 1 227 23 VAL HB H 2.08 . 1 228 23 VAL HG1 H 0.80 . 2 229 23 VAL HG2 H 0.67 . 2 230 23 VAL C C 176.6 . 1 231 23 VAL CA C 62.1 . 1 232 23 VAL CB C 31.8 . 1 233 23 VAL CG1 C 21.6 . 2 234 23 VAL CG2 C 20.0 . 2 235 23 VAL N N 122.9 . 1 236 24 VAL H H 9.66 . 1 237 24 VAL HA H 5.93 . 1 238 24 VAL HB H 2.55 . 1 239 24 VAL HG1 H 1.05 . 2 240 24 VAL HG2 H 1.54 . 2 241 24 VAL C C 176.5 . 1 242 24 VAL CA C 58.7 . 1 243 24 VAL CB C 36.5 . 1 244 24 VAL CG1 C 21.9 . 2 245 24 VAL CG2 C 21.4 . 2 246 24 VAL N N 118.8 . 1 247 25 HIS H H 8.49 . 1 248 25 HIS HA H 5.87 . 1 249 25 HIS HB2 H 2.89 . 2 250 25 HIS HB3 H 2.77 . 2 251 25 HIS HD2 H 7.00 . 1 252 25 HIS HE1 H 7.14 . 1 253 25 HIS C C 177.1 . 1 254 25 HIS CA C 54.8 . 1 255 25 HIS CB C 36.0 . 1 256 25 HIS CD2 C 117.4 . 1 257 25 HIS CE1 C 136.3 . 1 258 25 HIS N N 117.6 . 1 259 26 TYR H H 10.09 . 1 260 26 TYR HA H 6.70 . 1 261 26 TYR HB2 H 3.40 . 2 262 26 TYR HB3 H 3.24 . 2 263 26 TYR HD1 H 7.17 . 3 264 26 TYR HD2 H 7.07 . 3 265 26 TYR HE1 H 6.92 . 3 266 26 TYR HE2 H 6.35 . 3 267 26 TYR C C 174.7 . 1 268 26 TYR CA C 56.1 . 1 269 26 TYR CB C 45.1 . 1 270 26 TYR CD1 C 132.3 . 2 271 26 TYR CD2 C 132.1 . 2 272 26 TYR CE1 C 117.4 . 2 273 26 TYR CE2 C 118.4 . 2 274 26 TYR N N 117.8 . 1 275 27 THR H H 9.07 . 1 276 27 THR HA H 4.83 . 1 277 27 THR HB H 4.11 . 1 278 27 THR HG2 H 1.32 . 1 279 27 THR C C 174.1 . 1 280 27 THR CA C 63.1 . 1 281 27 THR CB C 72.0 . 1 282 27 THR CG2 C 22.1 . 1 283 27 THR N N 116.5 . 1 284 28 GLY H H 9.30 . 1 285 28 GLY HA2 H 4.20 . 2 286 28 GLY HA3 H 2.42 . 2 287 28 GLY CA C 45.6 . 1 288 28 GLY N N 114.3 . 1 289 29 MET H H 9.09 . 1 290 29 MET HA H 5.22 . 1 291 29 MET HB2 H 1.99 . 2 292 29 MET HB3 H 1.87 . 2 293 29 MET HG2 H 2.40 . 2 294 29 MET HG3 H 2.07 . 2 295 29 MET HE H 1.94 . 1 296 29 MET C C 176.4 . 1 297 29 MET CA C 54.5 . 1 298 29 MET CB C 38.1 . 1 299 29 MET CG C 32.0 . 1 300 29 MET CE C 16.3 . 1 301 29 MET N N 124.7 . 1 302 30 LEU H H 8.41 . 1 303 30 LEU HA H 4.85 . 1 304 30 LEU HB2 H 2.23 . 2 305 30 LEU HB3 H 1.97 . 2 306 30 LEU HG H 1.99 . 1 307 30 LEU HD1 H 1.08 . 2 308 30 LEU HD2 H 0.88 . 2 309 30 LEU C C 179.9 . 1 310 30 LEU CA C 54.2 . 1 311 30 LEU CB C 41.7 . 1 312 30 LEU CG C 28.1 . 1 313 30 LEU CD1 C 26.1 . 2 314 30 LEU CD2 C 23.2 . 2 315 30 LEU N N 118.7 . 1 316 31 GLU H H 8.88 . 1 317 31 GLU HA H 3.84 . 1 318 31 GLU HB2 H 2.12 . 1 319 31 GLU HB3 H 2.12 . 1 320 31 GLU HG2 H 2.33 . 1 321 31 GLU HG3 H 2.27 . 2 322 31 GLU C C 177.1 . 1 323 31 GLU CA C 59.7 . 1 324 31 GLU CB C 30.0 . 1 325 31 GLU CG C 36.5 . 1 326 31 GLU N N 119.8 . 1 327 32 ASP H H 7.93 . 1 328 32 ASP HA H 4.46 . 1 329 32 ASP HB2 H 3.01 . 2 330 32 ASP HB3 H 2.64 . 2 331 32 ASP C C 177.8 . 1 332 32 ASP CA C 53.7 . 1 333 32 ASP CB C 40.1 . 1 334 32 ASP N N 114.8 . 1 335 33 GLY H H 8.28 . 1 336 33 GLY HA2 H 4.30 . 2 337 33 GLY HA3 H 3.67 . 2 338 33 GLY C C 174.9 . 1 339 33 GLY CA C 45.1 . 1 340 33 GLY N N 107.7 . 1 341 34 LYS H H 7.87 . 1 342 34 LYS HA H 4.18 . 1 343 34 LYS HB2 H 1.96 . 2 344 34 LYS HB3 H 1.83 . 2 345 34 LYS HG2 H 1.49 . 2 346 34 LYS HG3 H 1.36 . 2 347 34 LYS HD2 H 1.79 . 2 348 34 LYS HD3 H 1.74 . 2 349 34 LYS HE2 H 3.04 . 1 350 34 LYS HE3 H 3.04 . 1 351 34 LYS C C 177.0 . 1 352 34 LYS CA C 57.1 . 1 353 34 LYS CB C 32.8 . 1 354 34 LYS CG C 25.0 . 1 355 34 LYS CD C 29.4 . 1 356 34 LYS CE C 42.2 . 1 357 34 LYS N N 120.8 . 1 358 35 LYS H H 8.58 . 1 359 35 LYS HA H 4.53 . 1 360 35 LYS HB2 H 1.77 . 1 361 35 LYS HB3 H 1.77 . 1 362 35 LYS HG2 H 1.46 . 2 363 35 LYS HG3 H 1.15 . 2 364 35 LYS HD2 H 1.66 . 1 365 35 LYS HD3 H 1.66 . 1 366 35 LYS HE2 H 2.95 . 2 367 35 LYS HE3 H 2.84 . 2 368 35 LYS C C 176.3 . 1 369 35 LYS CA C 56.6 . 1 370 35 LYS CB C 33.1 . 1 371 35 LYS CG C 24.7 . 1 372 35 LYS CD C 30.0 . 1 373 35 LYS CE C 41.2 . 1 374 35 LYS N N 127.3 . 1 375 36 PHE H H 8.51 . 1 376 36 PHE HA H 5.17 . 1 377 36 PHE HB2 H 3.36 . 2 378 36 PHE HB3 H 2.73 . 2 379 36 PHE HD1 H 6.99 . 1 380 36 PHE HD2 H 6.99 . 1 381 36 PHE HE1 H 7.06 . 1 382 36 PHE HE2 H 7.06 . 1 383 36 PHE HZ H 6.65 . 1 384 36 PHE C C 175.6 . 1 385 36 PHE CA C 56.3 . 1 386 36 PHE CB C 41.2 . 1 387 36 PHE CD1 C 132.3 . 1 388 36 PHE CD2 C 132.3 . 1 389 36 PHE CE1 C 131.3 . 1 390 36 PHE CE2 C 131.3 . 1 391 36 PHE CZ C 129.5 . 1 392 36 PHE N N 120.6 . 1 393 37 ASP H H 7.03 . 1 394 37 ASP HA H 4.91 . 1 395 37 ASP HB2 H 3.61 . 2 396 37 ASP HB3 H 2.63 . 2 397 37 ASP C C 175.7 . 1 398 37 ASP CA C 54.8 . 1 399 37 ASP CB C 44.4 . 1 400 37 ASP N N 117.7 . 1 401 38 SER H H 8.45 . 1 402 38 SER HA H 4.87 . 1 403 38 SER HB2 H 4.12 . 2 404 38 SER HB3 H 3.65 . 2 405 38 SER C C 176.3 . 1 406 38 SER CA C 57.1 . 1 407 38 SER CB C 65.2 . 1 408 38 SER N N 118.0 . 1 409 39 SER H H 8.43 . 1 410 39 SER HA H 4.05 . 1 411 39 SER HB2 H 5.03 . 2 412 39 SER HB3 H 3.64 . 2 413 39 SER C C 177.8 . 1 414 39 SER CA C 61.8 . 1 415 39 SER CB C 61.8 . 1 416 39 SER N N 124.5 . 1 417 40 ARG H H 7.81 . 1 418 40 ARG HA H 3.63 . 1 419 40 ARG HB2 H 1.49 . 2 420 40 ARG HB3 H 1.45 . 2 421 40 ARG HG2 H 1.05 . 2 422 40 ARG HG3 H 0.60 . 2 423 40 ARG HD2 H 2.90 . 2 424 40 ARG HD3 H 2.75 . 2 425 40 ARG C C 180.7 . 1 426 40 ARG CA C 58.9 . 1 427 40 ARG CB C 28.9 . 1 428 40 ARG CG C 29.2 . 1 429 40 ARG CD C 42.8 . 1 430 40 ARG N N 122.9 . 1 431 41 ASP H H 7.10 . 1 432 41 ASP HA H 4.36 . 1 433 41 ASP HB2 H 2.82 . 2 434 41 ASP HB3 H 2.73 . 2 435 41 ASP CA C 56.6 . 1 436 41 ASP CB C 40.4 . 1 437 41 ASP N N 117.8 . 1 438 42 ARG H H 6.79 . 1 439 42 ARG HA H 4.54 . 1 440 42 ARG HB2 H 2.05 . 1 441 42 ARG HB3 H 2.05 . 1 442 42 ARG HG2 H 1.74 . 1 443 42 ARG HG3 H 1.74 . 1 444 42 ARG HD2 H 3.49 . 2 445 42 ARG HD3 H 3.23 . 2 446 42 ARG C C 175.7 . 1 447 42 ARG CA C 55.8 . 1 448 42 ARG CB C 31.5 . 1 449 42 ARG CG C 28.9 . 1 450 42 ARG CD C 43.5 . 1 451 42 ARG N N 112.9 . 1 452 43 ASN H H 7.78 . 1 453 43 ASN HA H 4.44 . 1 454 43 ASN HB2 H 3.24 . 2 455 43 ASN HB3 H 2.71 . 2 456 43 ASN C C 174.9 . 1 457 43 ASN CA C 54.0 . 1 458 43 ASN CB C 37.8 . 1 459 43 ASN N N 115.5 . 1 460 44 LYS H H 7.48 . 1 461 44 LYS HA H 4.95 . 1 462 44 LYS HB2 H 1.84 . 2 463 44 LYS HB3 H 1.70 . 2 464 44 LYS HG2 H 1.52 . 1 465 44 LYS HG3 H 1.52 . 1 466 44 LYS HD2 H 1.82 . 1 467 44 LYS HD3 H 1.82 . 1 468 44 LYS HE2 H 3.13 . 1 469 44 LYS HE3 H 3.13 . 1 470 44 LYS CA C 53.4 . 1 471 44 LYS CB C 35.7 . 1 472 44 LYS CG C 24.5 . 1 473 44 LYS CD C 29.7 . 1 474 44 LYS CE C 42.2 . 1 475 44 LYS N N 114.8 . 1 476 45 PRO HA H 4.06 . 1 477 45 PRO HB2 H 1.45 . 1 478 45 PRO HB3 H 1.45 . 1 479 45 PRO HG2 H 1.78 . 2 480 45 PRO HG3 H 1.29 . 2 481 45 PRO HD2 H 3.67 . 1 482 45 PRO HD3 H 3.67 . 1 483 45 PRO C C 175.6 . 1 484 45 PRO CA C 63.1 . 1 485 45 PRO CB C 32.6 . 1 486 45 PRO CG C 26.8 . 1 487 45 PRO CD C 50.8 . 1 488 46 PHE H H 9.15 . 1 489 46 PHE HA H 4.98 . 1 490 46 PHE HB2 H 3.65 . 2 491 46 PHE HB3 H 3.11 . 2 492 46 PHE HD1 H 7.32 . 1 493 46 PHE HD2 H 7.32 . 1 494 46 PHE HE1 H 6.89 . 1 495 46 PHE HE2 H 6.89 . 1 496 46 PHE HZ H 6.75 . 1 497 46 PHE C C 173.6 . 1 498 46 PHE CA C 56.8 . 1 499 46 PHE CB C 42.2 . 1 500 46 PHE CD1 C 130.9 . 1 501 46 PHE CD2 C 130.9 . 1 502 46 PHE CE1 C 131.3 . 1 503 46 PHE CE2 C 131.3 . 1 504 46 PHE CZ C 129.9 . 1 505 46 PHE N N 123.6 . 1 506 47 LYS H H 7.27 . 1 507 47 LYS HA H 5.61 . 1 508 47 LYS HB2 H 1.53 . 2 509 47 LYS HB3 H 1.29 . 2 510 47 LYS HG2 H 1.34 . 2 511 47 LYS HG3 H 1.10 . 2 512 47 LYS HD2 H 1.53 . 1 513 47 LYS HD3 H 1.53 . 1 514 47 LYS HE2 H 2.89 . 2 515 47 LYS HE3 H 2.68 . 2 516 47 LYS C C 175.0 . 1 517 47 LYS CA C 54.0 . 1 518 47 LYS CB C 35.7 . 1 519 47 LYS CG C 25.8 . 1 520 47 LYS CD C 30.0 . 1 521 47 LYS CE C 41.7 . 1 522 47 LYS N N 124.1 . 1 523 48 PHE H H 8.11 . 1 524 48 PHE HA H 4.74 . 1 525 48 PHE HB2 H 2.95 . 2 526 48 PHE HB3 H 2.89 . 2 527 48 PHE HD1 H 7.15 . 1 528 48 PHE HD2 H 7.15 . 1 529 48 PHE HE1 H 7.36 . 1 530 48 PHE HE2 H 7.36 . 1 531 48 PHE HZ H 7.22 . 1 532 48 PHE C C 172.0 . 1 533 48 PHE CA C 55.2 . 1 534 48 PHE CB C 41.7 . 1 535 48 PHE CD1 C 133.0 . 1 536 48 PHE CD2 C 133.0 . 1 537 48 PHE CE1 C 130.7 . 1 538 48 PHE CE2 C 130.7 . 1 539 48 PHE CZ C 128.0 . 1 540 48 PHE N N 115.7 . 1 541 49 MET H H 9.10 . 1 542 49 MET HA H 4.70 . 1 543 49 MET HB2 H 1.87 . 2 544 49 MET HB3 H 1.83 . 2 545 49 MET HG2 H 2.18 . 1 546 49 MET HG3 H 2.18 . 1 547 49 MET HE H 2.05 . 1 548 49 MET C C 176.6 . 1 549 49 MET CA C 54.5 . 1 550 49 MET CB C 34.1 . 1 551 49 MET CG C 32.8 . 1 552 49 MET CE C 16.7 . 1 553 49 MET N N 121.9 . 1 554 50 LEU H H 8.38 . 1 555 50 LEU HA H 4.33 . 1 556 50 LEU HB2 H 1.93 . 2 557 50 LEU HB3 H 1.26 . 2 558 50 LEU HG H 1.71 . 1 559 50 LEU HD1 H 1.14 . 2 560 50 LEU HD2 H 0.79 . 2 561 50 LEU C C 178.8 . 1 562 50 LEU CA C 56.8 . 1 563 50 LEU CB C 42.2 . 1 564 50 LEU CG C 27.4 . 1 565 50 LEU CD1 C 25.0 . 2 566 50 LEU CD2 C 26.0 . 2 567 50 LEU N N 129.9 . 1 568 51 GLY H H 10.74 . 1 569 51 GLY HA2 H 4.31 . 2 570 51 GLY HA3 H 3.85 . 2 571 51 GLY C C 175.5 . 1 572 51 GLY CA C 45.6 . 1 573 51 GLY N N 118.3 . 1 574 52 LYS H H 7.71 . 1 575 52 LYS HA H 4.49 . 1 576 52 LYS HB2 H 2.13 . 2 577 52 LYS HB3 H 1.76 . 2 578 52 LYS HG2 H 1.60 . 2 579 52 LYS HG3 H 1.40 . 2 580 52 LYS HD2 H 2.13 . 1 581 52 LYS HD3 H 2.13 . 1 582 52 LYS HE2 H 3.06 . 2 583 52 LYS HE3 H 3.00 . 2 584 52 LYS C C 176.3 . 1 585 52 LYS CA C 55.0 . 1 586 52 LYS CB C 33.6 . 1 587 52 LYS CG C 25.5 . 1 588 52 LYS CD C 33.6 . 1 589 52 LYS CE C 42.8 . 1 590 52 LYS N N 118.9 . 1 591 53 GLN H H 8.99 . 1 592 53 GLN HA H 4.06 . 1 593 53 GLN HB2 H 2.31 . 1 594 53 GLN HB3 H 2.31 . 1 595 53 GLN HG2 H 2.31 . 1 596 53 GLN HG3 H 2.31 . 1 597 53 GLN C C 176.7 . 1 598 53 GLN CA C 57.0 . 1 599 53 GLN CB C 26.3 . 1 600 53 GLN CG C 34.9 . 1 601 53 GLN N N 115.8 . 1 602 54 GLU H H 9.22 . 1 603 54 GLU HA H 4.35 . 1 604 54 GLU HB2 H 2.22 . 2 605 54 GLU HB3 H 2.09 . 2 606 54 GLU HG2 H 2.37 . 1 607 54 GLU HG3 H 2.33 . 2 608 54 GLU CA C 57.4 . 1 609 54 GLU CB C 31.3 . 1 610 54 GLU CG C 37.3 . 1 611 54 GLU N N 116.8 . 1 612 55 VAL H H 6.98 . 1 613 55 VAL HA H 4.91 . 1 614 55 VAL HB H 1.42 . 1 615 55 VAL HG1 H 0.30 . 2 616 55 VAL HG2 H 0.65 . 2 617 55 VAL C C 176.4 . 1 618 55 VAL CA C 57.4 . 1 619 55 VAL CB C 36.8 . 1 620 55 VAL CG1 C 22.4 . 2 621 55 VAL CG2 C 19.26 . 2 622 55 VAL N N 106.1 . 1 623 56 ILE H H 6.96 . 1 624 56 ILE HA H 4.01 . 1 625 56 ILE HB H 2.33 . 1 626 56 ILE HG12 H 1.39 . 2 627 56 ILE HG13 H 0.75 . 2 628 56 ILE HG2 H 0.23 . 1 629 56 ILE HD1 H 0.92 . 1 630 56 ILE C C 177.8 . 1 631 56 ILE CA C 61.8 . 1 632 56 ILE CB C 38.6 . 1 633 56 ILE CG1 C 25.8 . 2 634 56 ILE CG2 C 18.5 . 2 635 56 ILE CD1 C 14.0 . 1 636 56 ILE N N 108.6 . 1 637 57 ARG H H 8.78 . 1 638 57 ARG HA H 4.03 . 1 639 57 ARG HB2 H 1.82 . 2 640 57 ARG HB3 H 1.38 . 2 641 57 ARG HG2 H 1.63 . 2 642 57 ARG HG3 H 1.14 . 2 643 57 ARG HD2 H 2.81 . 2 644 57 ARG HD3 H 2.08 . 2 645 57 ARG C C 179.9 . 1 646 57 ARG CA C 60.2 . 1 647 57 ARG CB C 30.7 . 1 648 57 ARG CG C 27.1 . 1 649 57 ARG CD C 43.5 . 1 650 57 ARG N N 125.4 . 1 651 58 GLY H H 9.72 . 1 652 58 GLY HA2 H 4.02 . 2 653 58 GLY HA3 H 3.87 . 2 654 58 GLY C C 176.5 . 1 655 58 GLY CA C 47.7 . 1 656 58 GLY N N 100.1 . 1 657 59 TRP H H 7.80 . 1 658 59 TRP HA H 4.07 . 1 659 59 TRP HB2 H 3.01 . 2 660 59 TRP HB3 H 2.66 . 2 661 59 TRP HD1 H 6.21 . 1 662 59 TRP HE3 H 6.72 . 1 663 59 TRP HZ2 H 6.29 . 1 664 59 TRP HZ3 H 7.00 . 1 665 59 TRP HH2 H 6.73 . 1 666 59 TRP C C 177.8 . 1 667 59 TRP CA C 62.3 . 1 668 59 TRP CB C 28.1 . 1 669 59 TRP CD1 C 120.9 . 1 670 59 TRP CE3 C 120.2 . 1 671 59 TRP CZ2 C 112.4 . 3 672 59 TRP CZ3 C 120.9 . 3 673 59 TRP CH2 C 124.1 . 1 674 59 TRP N N 118.7 . 1 675 60 GLU H H 7.41 . 1 676 60 GLU HA H 4.21 . 1 677 60 GLU HB2 H 2.20 . 1 678 60 GLU HB3 H 2.20 . 1 679 60 GLU HG2 H 2.42 . 1 680 60 GLU HG3 H 2.25 . 2 681 60 GLU C C 179.3 . 1 682 60 GLU CA C 60.5 . 1 683 60 GLU CB C 30.0 . 1 684 60 GLU CG C 36.2 . 1 685 60 GLU N N 118.7 . 1 686 61 GLU H H 8.19 . 1 687 61 GLU HA H 4.28 . 1 688 61 GLU HB2 H 2.21 . 2 689 61 GLU HB3 H 1.91 . 2 690 61 GLU HG2 H 2.47 . 1 691 61 GLU HG3 H 2.29 . 2 692 61 GLU C C 179.9 . 1 693 61 GLU CA C 58.2 . 1 694 61 GLU CB C 30.5 . 1 695 61 GLU CG C 37.3 . 1 696 61 GLU N N 111.3 . 1 697 62 GLY H H 7.72 . 1 698 62 GLY HA2 H 3.75 . 2 699 62 GLY HA3 H 3.63 . 2 700 62 GLY C C 175.0 . 1 701 62 GLY CA C 47.4 . 1 702 62 GLY N N 106.6 . 1 703 63 VAL H H 8.79 . 1 704 63 VAL HA H 3.75 . 1 705 63 VAL HB H 2.27 . 1 706 63 VAL HG1 H 1.10 . 2 707 63 VAL HG2 H 0.73 . 2 708 63 VAL C C 177.9 . 1 709 63 VAL CA C 66.0 . 1 710 63 VAL CB C 31.0 . 1 711 63 VAL CG1 C 22.7 . 2 712 63 VAL CG2 C 23.7 . 2 713 63 VAL N N 120.0 . 1 714 64 ALA H H 6.56 . 1 715 64 ALA HA H 4.06 . 1 716 64 ALA HB H 1.60 . 1 717 64 ALA C C 178.5 . 1 718 64 ALA CA C 54.8 . 1 719 64 ALA CB C 19.0 . 1 720 64 ALA N N 114.8 . 1 721 65 GLN H H 7.07 . 1 722 65 GLN HA H 4.38 . 1 723 65 GLN HB2 H 2.43 . 2 724 65 GLN HB3 H 2.15 . 2 725 65 GLN HG2 H 2.57 . 2 726 65 GLN HG3 H 2.41 . 2 727 65 GLN C C 176.4 . 1 728 65 GLN CA C 55.8 . 1 729 65 GLN CB C 30.2 . 1 730 65 GLN CG C 34.7 . 1 731 65 GLN N N 111.2 . 1 732 66 MET H H 7.89 . 1 733 66 MET HA H 4.82 . 1 734 66 MET HB2 H 2.15 . 2 735 66 MET HB3 H 1.99 . 2 736 66 MET HG2 H 2.67 . 2 737 66 MET HG3 H 1.93 . 2 738 66 MET HE H 1.85 . 1 739 66 MET C C 173.4 . 1 740 66 MET CA C 55.3 . 1 741 66 MET CB C 35.7 . 1 742 66 MET CG C 31.8 . 1 743 66 MET CE C 17.70 . 1 744 66 MET N N 121.3 . 1 745 67 SER H H 8.21 . 1 746 67 SER HA H 4.87 . 1 747 67 SER HB2 H 3.76 . 2 748 67 SER HB3 H 2.41 . 2 749 67 SER C C 176.9 . 1 750 67 SER CA C 54.8 . 1 751 67 SER CB C 66.2 . 1 752 67 SER N N 107.1 . 1 753 68 VAL H H 7.70 . 1 754 68 VAL HA H 3.16 . 1 755 68 VAL HB H 1.86 . 1 756 68 VAL HG1 H 0.91 . 2 757 68 VAL HG2 H 0.93 . 2 758 68 VAL C C 177.0 . 1 759 68 VAL CA C 67.3 . 1 760 68 VAL CB C 31.8 . 1 761 68 VAL CG1 C 21.6 . 2 762 68 VAL CG2 C 23.4 . 2 763 68 VAL N N 118.4 . 1 764 69 GLY H H 8.84 . 1 765 69 GLY HA2 H 4.43 . 2 766 69 GLY HA3 H 3.87 . 2 767 69 GLY C C 174.8 . 1 768 69 GLY CA C 44.6 . 1 769 69 GLY N N 116.1 . 1 770 70 GLN H H 8.63 . 1 771 70 GLN HA H 4.08 . 1 772 70 GLN HB2 H 2.23 . 1 773 70 GLN HB3 H 2.23 . 1 774 70 GLN HG2 H 2.97 . 2 775 70 GLN HG3 H 2.20 . 2 776 70 GLN C C 174.3 . 1 777 70 GLN CA C 56.1 . 1 778 70 GLN CB C 30.5 . 1 779 70 GLN CG C 33.6 . 1 780 70 GLN N N 122.5 . 1 781 71 ARG H H 8.85 . 1 782 71 ARG HA H 5.71 . 1 783 71 ARG HB2 H 1.88 . 2 784 71 ARG HB3 H 1.62 . 2 785 71 ARG HG2 H 1.62 . 2 786 71 ARG HG3 H 1.46 . 2 787 71 ARG HD2 H 3.02 . 2 788 71 ARG HD3 H 2.95 . 2 789 71 ARG C C 176.4 . 1 790 71 ARG CA C 54.2 . 1 791 71 ARG CB C 33.9 . 1 792 71 ARG CG C 27.7 . 1 793 71 ARG CD C 44.6 . 1 794 71 ARG N N 124.0 . 1 795 72 ALA H H 9.98 . 1 796 72 ALA HA H 5.19 . 1 797 72 ALA HB H 1.29 . 1 798 72 ALA C C 174.0 . 1 799 72 ALA CA C 51.1 . 1 800 72 ALA CB C 23.7 . 1 801 72 ALA N N 130.4 . 1 802 73 LYS H H 9.25 . 1 803 73 LYS HA H 5.28 . 1 804 73 LYS HB2 H 1.79 . 2 805 73 LYS HB3 H 1.67 . 2 806 73 LYS HG2 H 1.33 . 2 807 73 LYS HG3 H 1.20 . 2 808 73 LYS HD2 H 1.65 . 1 809 73 LYS HD3 H 1.65 . 1 810 73 LYS HE2 H 2.82 . 1 811 73 LYS HE3 H 2.82 . 1 812 73 LYS C C 176.9 . 1 813 73 LYS CA C 54.8 . 1 814 73 LYS CB C 34.7 . 1 815 73 LYS CG C 25.8 . 1 816 73 LYS CD C 29.7 . 1 817 73 LYS CE C 42.0 . 1 818 73 LYS N N 119.8 . 1 819 74 LEU H H 9.97 . 1 820 74 LEU HA H 5.45 . 1 821 74 LEU HB2 H 1.76 . 2 822 74 LEU HB3 H 1.27 . 2 823 74 LEU HG H 1.56 . 1 824 74 LEU HD1 H 0.45 . 2 825 74 LEU HD2 H 0.48 . 2 826 74 LEU C C 176.9 . 1 827 74 LEU CA C 53.7 . 1 828 74 LEU CB C 44.1 . 1 829 74 LEU CG C 28.7 . 1 830 74 LEU CD1 C 24.7 . 2 831 74 LEU CD2 C 25.0 . 2 832 74 LEU N N 129.2 . 1 833 75 THR H H 8.88 . 1 834 75 THR HA H 5.13 . 1 835 75 THR HB H 4.04 . 1 836 75 THR HG2 H 1.11 . 1 837 75 THR C C 176.3 . 1 838 75 THR CA C 63.6 . 1 839 75 THR CB C 69.1 . 1 840 75 THR CG2 C 21.1 . 1 841 75 THR N N 120.8 . 1 842 76 ILE H H 9.98 . 1 843 76 ILE HA H 4.64 . 1 844 76 ILE HB H 1.92 . 1 845 76 ILE HG12 H 0.86 . 1 846 76 ILE HG13 H 0.86 . 1 847 76 ILE HG2 H 1.25 . 1 848 76 ILE HD1 H 1.06 . 1 849 76 ILE C C 174.8 . 1 850 76 ILE CA C 61.5 . 1 851 76 ILE CB C 41.7 . 1 852 76 ILE CG1 C 27.9 . 1 853 76 ILE CG2 C 21.6 . 1 854 76 ILE CD1 C 15.9 . 1 855 76 ILE N N 128.9 . 1 856 77 SER H H 8.37 . 1 857 77 SER HA H 4.77 . 1 858 77 SER HB2 H 4.44 . 2 859 77 SER HB3 H 3.98 . 2 860 77 SER CA C 57.9 . 1 861 77 SER CB C 61.8 . 1 862 77 SER N N 121.4 . 1 863 78 PRO HA H 4.55 . 1 864 78 PRO HB2 H 2.16 . 1 865 78 PRO HB3 H 2.16 . 1 866 78 PRO HG2 H 2.09 . 2 867 78 PRO HG3 H 1.82 . 2 868 78 PRO HD2 H 3.88 . 1 869 78 PRO HD3 H 3.88 . 1 870 78 PRO C C 180.7 . 1 871 78 PRO CA C 66.2 . 1 872 78 PRO CB C 31.3 . 1 873 78 PRO CG C 28.1 . 1 874 78 PRO CD C 50.1 . 1 875 79 ASP H H 9.53 . 1 876 79 ASP HA H 4.50 . 1 877 79 ASP HB2 H 2.88 . 2 878 79 ASP HB3 H 2.79 . 2 879 79 ASP C C 177.1 . 1 880 79 ASP CA C 55.3 . 1 881 79 ASP CB C 38.3 . 1 882 79 ASP N N 113.8 . 1 883 80 TYR H H 8.18 . 1 884 80 TYR HA H 4.50 . 1 885 80 TYR HB2 H 3.05 . 2 886 80 TYR HB3 H 2.86 . 2 887 80 TYR HD1 H 6.72 . 1 888 80 TYR HD2 H 6.72 . 1 889 80 TYR HE1 H 6.86 . 1 890 80 TYR HE2 H 6.86 . 1 891 80 TYR C C 174.1 . 1 892 80 TYR CA C 57.8 . 1 893 80 TYR CB C 39.4 . 1 894 80 TYR CD1 C 130.6 . 1 895 80 TYR CD2 C 130.6 . 1 896 80 TYR CE1 C 118.8 . 1 897 80 TYR CE2 C 118.8 . 1 898 80 TYR N N 122.8 . 1 899 81 ALA H H 7.97 . 1 900 81 ALA HA H 4.38 . 1 901 81 ALA HB H 1.53 . 1 902 81 ALA C C 176.5 . 1 903 81 ALA CA C 52.2 . 1 904 81 ALA CB C 19.3 . 1 905 81 ALA N N 125.0 . 1 906 82 TYR H H 9.28 . 1 907 82 TYR HA H 4.27 . 1 908 82 TYR HB2 H 3.24 . 2 909 82 TYR HB3 H 2.78 . 2 910 82 TYR HD1 H 7.25 . 1 911 82 TYR HD2 H 7.25 . 1 912 82 TYR HE1 H 6.58 . 1 913 82 TYR HE2 H 6.58 . 1 914 82 TYR C C 177.0 . 1 915 82 TYR CA C 59.5 . 1 916 82 TYR CB C 37.8 . 1 917 82 TYR CD1 C 133.4 . 1 918 82 TYR CD2 C 133.4 . 1 919 82 TYR CE1 C 117.0 . 1 920 82 TYR CE2 C 117.0 . 1 921 82 TYR N N 121.1 . 1 922 83 GLY H H 8.75 . 1 923 83 GLY HA2 H 3.91 . 2 924 83 GLY HA3 H 3.65 . 2 925 83 GLY CA C 46.9 . 1 926 83 GLY N N 108.0 . 1 927 84 ALA HA H 3.33 . 1 928 84 ALA HB H 1.50 . 1 929 84 ALA C C 177.9 . 1 930 84 ALA CA C 53.4 . 1 931 84 ALA CB C 19.3 . 1 932 85 THR H H 7.88 . 1 933 85 THR HA H 4.07 . 1 934 85 THR HB H 4.31 . 1 935 85 THR HG2 H 1.27 . 1 936 85 THR C C 177.9 . 1 937 85 THR CA C 64.6 . 1 938 85 THR CB C 69.6 . 1 939 85 THR CG2 C 22.1 . 1 940 85 THR N N 109.1 . 1 941 86 GLY H H 7.36 . 1 942 86 GLY HA2 H 3.84 . 2 943 86 GLY HA3 H 3.47 . 2 944 86 GLY C C 172.7 . 1 945 86 GLY CA C 45.1 . 1 946 86 GLY N N 106.1 . 1 947 87 HIS H H 8.82 . 1 948 87 HIS HA H 4.90 . 1 949 87 HIS HB2 H 2.35 . 2 950 87 HIS HB3 H 1.71 . 2 951 87 HIS HD2 H 6.53 . 1 952 87 HIS HE1 H 7.81 . 1 953 87 HIS CA C 54.2 . 1 954 87 HIS CB C 32.3 . 1 955 87 HIS CD2 C 119.5 . 1 956 87 HIS CE1 C 138.4 . 1 957 87 HIS N N 121.0 . 1 958 88 PRO HA H 4.11 . 1 959 88 PRO HB2 H 2.18 . 2 960 88 PRO HB3 H 1.82 . 2 961 88 PRO HG2 H 1.87 . 1 962 88 PRO HG3 H 1.87 . 1 963 88 PRO HD2 H 3.43 . 2 964 88 PRO HD3 H 2.80 . 2 965 88 PRO CA C 65.2 . 1 966 88 PRO CB C 32.1 . 1 967 88 PRO CG C 27.1 . 1 968 88 PRO CD C 51.4 . 1 969 89 GLY H H 8.58 . 1 970 89 GLY HA2 H 4.28 . 2 971 89 GLY HA3 H 3.64 . 2 972 89 GLY C C 174.9 . 1 973 89 GLY CA C 45.9 . 1 974 89 GLY N N 112.4 . 1 975 90 ILE H H 8.06 . 1 976 90 ILE HA H 4.34 . 1 977 90 ILE HB H 1.44 . 1 978 90 ILE HG12 H 1.59 . 2 979 90 ILE HG13 H 1.07 . 2 980 90 ILE HG2 H 0.80 . 1 981 90 ILE HD1 H 0.94 . 1 982 90 ILE C C 174.3 . 1 983 90 ILE CA C 63.4 . 1 984 90 ILE CB C 42.5 . 1 985 90 ILE CG1 C 27.4 . 2 986 90 ILE CG2 C 18.0 . 2 987 90 ILE CD1 C 13.8 . 1 988 90 ILE N N 116.9 . 1 989 91 ILE H H 8.17 . 1 990 91 ILE HA H 4.59 . 1 991 91 ILE HB H 1.42 . 1 992 91 ILE HG12 H 0.54 . 1 993 91 ILE HG13 H 0.54 . 1 994 91 ILE HG2 H 0.96 . 1 995 91 ILE HD1 H -0.30 . 1 996 91 ILE CA C 55.3 . 1 997 91 ILE CB C 39.4 . 1 998 91 ILE CG1 C 26.1 . 2 999 91 ILE CG2 C 18.0 . 2 1000 91 ILE CD1 C 10.1 . 1 1001 91 ILE N N 118.5 . 1 1002 92 PRO HA H 4.79 . 1 1003 92 PRO HB2 H 2.41 . 2 1004 92 PRO HB3 H 1.98 . 2 1005 92 PRO HG2 H 2.02 . 1 1006 92 PRO HG3 H 2.02 . 1 1007 92 PRO HD2 H 3.85 . 2 1008 92 PRO HD3 H 3.42 . 2 1009 92 PRO CA C 62.1 . 1 1010 92 PRO CB C 31.3 . 1 1011 92 PRO CG C 26.8 . 1 1012 92 PRO CD C 51.9 . 1 1013 93 PRO HA H 3.65 . 1 1014 93 PRO HB2 H 2.24 . 2 1015 93 PRO HB3 H 1.58 . 2 1016 93 PRO HG2 H 2.07 . 2 1017 93 PRO HG3 H 1.70 . 2 1018 93 PRO HD2 H 3.79 . 2 1019 93 PRO HD3 H 3.50 . 2 1020 93 PRO C C 176.4 . 1 1021 93 PRO CA C 63.9 . 1 1022 93 PRO CB C 33.4 . 1 1023 93 PRO CG C 28.1 . 1 1024 93 PRO CD C 51.1 . 1 1025 94 HIS H H 8.02 . 1 1026 94 HIS HA H 3.86 . 1 1027 94 HIS HB2 H 3.27 . 2 1028 94 HIS HB3 H 3.24 . 2 1029 94 HIS HD2 H 7.02 . 1 1030 94 HIS HE1 H 7.98 . 1 1031 94 HIS C C 174.3 . 1 1032 94 HIS CA C 57.1 . 1 1033 94 HIS CB C 28.1 . 1 1034 94 HIS CD2 C 119.5 . 1 1035 94 HIS CE1 C 138.1 . 1 1036 94 HIS N N 115.1 . 1 1037 95 ALA H H 7.74 . 1 1038 95 ALA HA H 4.55 . 1 1039 95 ALA HB H 1.31 . 1 1040 95 ALA C C 177.9 . 1 1041 95 ALA CA C 52.7 . 1 1042 95 ALA CB C 20.6 . 1 1043 95 ALA N N 121.3 . 1 1044 96 THR H H 8.50 . 1 1045 96 THR HA H 4.69 . 1 1046 96 THR HB H 4.02 . 1 1047 96 THR HG2 H 1.08 . 1 1048 96 THR C C 174.8 . 1 1049 96 THR CA C 63.9 . 1 1050 96 THR CB C 69.6 . 1 1051 96 THR CG2 C 21.1 . 1 1052 96 THR N N 122.8 . 1 1053 97 LEU H H 8.74 . 1 1054 97 LEU HA H 5.19 . 1 1055 97 LEU HB2 H 1.86 . 2 1056 97 LEU HB3 H 1.52 . 2 1057 97 LEU HG H 1.92 . 1 1058 97 LEU HD1 H 1.31 . 2 1059 97 LEU HD2 H 0.93 . 2 1060 97 LEU C C 175.7 . 1 1061 97 LEU CA C 53.2 . 1 1062 97 LEU CB C 46.9 . 1 1063 97 LEU CG C 27.6 . 1 1064 97 LEU CD1 C 27.6 . 2 1065 97 LEU CD2 C 24.2 . 2 1066 97 LEU N N 124.1 . 1 1067 98 VAL H H 8.72 . 1 1068 98 VAL HA H 5.32 . 1 1069 98 VAL HB H 1.79 . 1 1070 98 VAL HG1 H 0.86 . 2 1071 98 VAL HG2 H 0.93 . 2 1072 98 VAL C C 176.3 . 1 1073 98 VAL CA C 60.8 . 1 1074 98 VAL CB C 34.4 . 1 1075 98 VAL CG1 C 21.6 . 2 1076 98 VAL CG2 C 21.1 . 2 1077 98 VAL N N 121.3 . 1 1078 99 PHE H H 9.67 . 1 1079 99 PHE HA H 5.96 . 1 1080 99 PHE HB2 H 2.99 . 2 1081 99 PHE HB3 H 2.84 . 2 1082 99 PHE HD1 H 7.48 . 1 1083 99 PHE HD2 H 7.48 . 1 1084 99 PHE HE1 H 7.33 . 1 1085 99 PHE HE2 H 7.33 . 1 1086 99 PHE HZ H 7.50 . 1 1087 99 PHE C C 174.9 . 1 1088 99 PHE CA C 55.3 . 1 1089 99 PHE CB C 43.8 . 1 1090 99 PHE CD1 C 132.0 . 1 1091 99 PHE CD2 C 132.0 . 1 1092 99 PHE CE1 C 131.6 . 1 1093 99 PHE CE2 C 131.6 . 1 1094 99 PHE CZ C 130.6 . 1 1095 99 PHE N N 121.4 . 1 1096 100 ASP H H 8.99 . 1 1097 100 ASP HA H 5.20 . 1 1098 100 ASP HB2 H 2.93 . 2 1099 100 ASP HB3 H 2.50 . 2 1100 100 ASP C C 177.1 . 1 1101 100 ASP CA C 52.9 . 1 1102 100 ASP CB C 42.8 . 1 1103 100 ASP N N 124.4 . 1 1104 101 VAL H H 9.56 . 1 1105 101 VAL HA H 5.06 . 1 1106 101 VAL HB H 1.67 . 1 1107 101 VAL HG1 H 0.55 . 2 1108 101 VAL HG2 H 0.53 . 2 1109 101 VAL C C 173.6 . 1 1110 101 VAL CA C 61.5 . 1 1111 101 VAL CB C 35.4 . 1 1112 101 VAL CG1 C 21.4 . 2 1113 101 VAL CG2 C 22.8 . 2 1114 101 VAL N N 125.5 . 1 1115 102 GLU H H 9.17 . 1 1116 102 GLU HA H 5.43 . 1 1117 102 GLU HB2 H 2.10 . 2 1118 102 GLU HB3 H 1.64 . 2 1119 102 GLU HG2 H 2.04 . 1 1120 102 GLU HG3 H 1.88 . 2 1121 102 GLU C C 175.7 . 1 1122 102 GLU CA C 54.2 . 1 1123 102 GLU CB C 34.13 . 1 1124 102 GLU CG C 36.2 . 1 1125 102 GLU N N 127.3 . 1 1126 103 LEU H H 8.62 . 1 1127 103 LEU HA H 4.69 . 1 1128 103 LEU HB2 H 2.33 . 2 1129 103 LEU HB3 H 1.07 . 2 1130 103 LEU HG H 1.40 . 1 1131 103 LEU HD1 H 0.84 . 2 1132 103 LEU HD2 H 0.67 . 2 1133 103 LEU C C 174.9 . 1 1134 103 LEU CA C 54.5 . 1 1135 103 LEU CB C 41.7 . 1 1136 103 LEU CG C 28.7 . 1 1137 103 LEU CD1 C 23.7 . 2 1138 103 LEU CD2 C 26.3 . 2 1139 103 LEU N N 127.7 . 1 1140 104 LEU H H 9.09 . 1 1141 104 LEU HA H 4.23 . 1 1142 104 LEU HB2 H 1.56 . 2 1143 104 LEU HB3 H 1.48 . 2 1144 104 LEU HG H 1.79 . 1 1145 104 LEU HD1 H 0.72 . 2 1146 104 LEU HD2 H 0.86 . 2 1147 104 LEU C C 178.7 . 1 1148 104 LEU CA C 57.4 . 1 1149 104 LEU CB C 42.8 . 1 1150 104 LEU CG C 27.4 . 1 1151 104 LEU CD1 C 26.3 . 2 1152 104 LEU CD2 C 22.7 . 2 1153 104 LEU N N 128.1 . 1 1154 105 LYS H H 7.69 . 1 1155 105 LYS HA H 4.40 . 1 1156 105 LYS HB2 H 1.84 . 2 1157 105 LYS HB3 H 1.72 . 2 1158 105 LYS HG2 H 1.26 . 2 1159 105 LYS HG3 H 1.19 . 2 1160 105 LYS HD2 H 1.73 . 2 1161 105 LYS HD3 H 1.63 . 2 1162 105 LYS HE2 H 2.96 . 2 1163 105 LYS HE3 H 2.90 . 2 1164 105 LYS C C 173.2 . 1 1165 105 LYS CA C 55.5 . 1 1166 105 LYS CB C 35.4 . 1 1167 105 LYS CG C 24.2 . 1 1168 105 LYS CD C 29.4 . 1 1169 105 LYS CE C 42.2 . 1 1170 105 LYS N N 111.2 . 1 1171 106 LEU H H 8.23 . 1 1172 106 LEU HA H 5.29 . 1 1173 106 LEU HB2 H 1.58 . 2 1174 106 LEU HB3 H 1.23 . 2 1175 106 LEU HG H 1.40 . 1 1176 106 LEU HD1 H 0.68 . 2 1177 106 LEU HD2 H 0.88 . 2 1178 106 LEU C C 176.9 . 1 1179 106 LEU CA C 53.2 . 1 1180 106 LEU CB C 44.3 . 1 1181 106 LEU CG C 27.1 . 1 1182 106 LEU CD1 C 26.1 . 1 1183 106 LEU CD2 C 26.1 . 1 1184 106 LEU N N 119.6 . 1 1185 107 GLU H H 9.02 . 1 1186 107 GLU HA H 4.33 . 1 1187 107 GLU HB2 H 2.01 . 2 1188 107 GLU HB3 H 1.74 . 2 1189 107 GLU HG2 H 2.03 . 1 1190 107 GLU HG3 H 1.95 . 2 1191 107 GLU CA C 56.8 . 1 1192 107 GLU CB C 32.8 . 1 1193 107 GLU CG C 37.0 . 1 1194 107 GLU N N 126.2 . 1 stop_ save_