data_15105 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the first Clip domain in PAP2 (CASP Target) ; _BMRB_accession_number 15105 _BMRB_flat_file_name bmr15105.str _Entry_type original _Submission_date 2007-01-22 _Accession_date 2007-01-22 _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 Huang R. D. . 2 Lv Z. Q. . 3 Dai H. E. . 4 Velde D. V. . 5 Prakash O. . . 6 Jiang H. B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 285 "13C chemical shifts" 213 "15N chemical shifts" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-06-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 15106 'Clip, second domain' stop_ _Original_release_date 2008-06-25 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17880110 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang R. D. . 2 Lu Z. Q. . 3 Dai H. E. . 4 Velde D. V. . 5 Prakash O. . . 6 Jiang H. B. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 41 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11431 _Page_last 11439 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'clip monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'clip domain' $Prophenoloxidase_activating_proteinase-2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Prophenoloxidase_activating_proteinase-2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Prophenoloxidase_activating_proteinase-2 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 66 _Mol_residue_sequence ; MHHHHHHAMGQACTLPNNDK GTCKSLLQCDVASKIISKKP RTAQDEKFLRESACGFDGQT PKVCCP ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 ALA 9 MET 10 GLY 11 GLN 12 ALA 13 CYS 14 THR 15 LEU 16 PRO 17 ASN 18 ASN 19 ASP 20 LYS 21 GLY 22 THR 23 CYS 24 LYS 25 SER 26 LEU 27 LEU 28 GLN 29 CYS 30 ASP 31 VAL 32 ALA 33 SER 34 LYS 35 ILE 36 ILE 37 SER 38 LYS 39 LYS 40 PRO 41 ARG 42 THR 43 ALA 44 GLN 45 ASP 46 GLU 47 LYS 48 PHE 49 LEU 50 ARG 51 GLU 52 SER 53 ALA 54 CYS 55 GLY 56 PHE 57 ASP 58 GLY 59 GLN 60 THR 61 PRO 62 LYS 63 VAL 64 CYS 65 CYS 66 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 2IKD "Solution Structure Of The First Clip Domain In Pap2" 100.00 66 100.00 100.00 1.16e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $Prophenoloxidase_activating_proteinase-2 'Tobacco hawkmoth' . . . Manduca sexta PAP-2 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 $Prophenoloxidase_activating_proteinase-2 'recombinant technology' bacteria Escherichia coli M15 pQE60 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details ; 1 mM Dual-Clip domain U-15N,13C, 100 mM phosphate buffer NA, 90% H2O, 10% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Prophenoloxidase_activating_proteinase-2 1.0 mM '[U-100% 13C; U-100% 15N]' 'phosphate buffer' 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_Sparky _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_13C-separated_NOESY _Sample_label $sample save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 8.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 13C-glucose C 13 carbons ppm 0 na indirect . . . 0.251449530 water H 1 protons ppm 0 na indirect . . . 1 '[15N] ammonium chloride' N 15 nitrogen ppm 0 na indirect . . . 0.10132918 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'clip domain' _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 11 11 GLN H H 7.74 . . 2 11 11 GLN HA H 4.29 . . 3 11 11 GLN HB2 H 2.07 . . 4 11 11 GLN HB3 H 1.94 . . 5 11 11 GLN HG2 H 2.34 . . 6 11 11 GLN HE21 H 7.54 . . 7 11 11 GLN HE22 H 6.86 . . 8 11 11 GLN C C 175.2 . . 9 11 11 GLN CA C 55.4 . . 10 11 11 GLN CB C 29.4 . . 11 11 11 GLN CG C 33.6 . . 12 11 11 GLN NE2 N 112.4 . . 13 12 12 ALA H H 8.27 . . 14 12 12 ALA HA H 4.53 . . 15 12 12 ALA HB H 1.42 . . 16 12 12 ALA C C 176.7 . . 17 12 12 ALA CA C 52.9 . . 18 12 12 ALA CB C 19.3 . . 19 12 12 ALA N N 126.3 . . 20 13 13 CYS H H 8.26 . . 21 13 13 CYS HA H 4.89 . . 22 13 13 CYS HB2 H 3.12 . . 23 13 13 CYS HB3 H 3.23 . . 24 13 13 CYS C C 171.8 . . 25 13 13 CYS CA C 54.6 . . 26 13 13 CYS CB C 46.8 . . 27 13 13 CYS N N 117.2 . . 28 14 14 THR H H 8.74 . . 29 14 14 THR HA H 4.64 . . 30 14 14 THR HB H 3.84 . . 31 14 14 THR HG2 H 1.25 . . 32 14 14 THR C C 173.8 . . 33 14 14 THR CA C 61.7 . . 34 14 14 THR CB C 70.2 . . 35 14 14 THR CG2 C 21.8 . . 36 14 14 THR N N 117.8 . . 37 15 15 LEU H H 8.97 . . 38 15 15 LEU HA H 4.19 . . 39 15 15 LEU HB2 H 1.40 . . 40 15 15 LEU HB3 H 1.56 . . 41 15 15 LEU HG H 1.38 . . 42 15 15 LEU HD1 H 0.88 . . 43 15 15 LEU HD2 H 0.76 . . 44 15 15 LEU CA C 54.8 . . 45 15 15 LEU CB C 42.3 . . 46 15 15 LEU CG C 29.7 . . 47 15 15 LEU CD1 C 26.0 . . 48 15 15 LEU CD2 C 26.3 . . 49 15 15 LEU N N 128.7 . . 50 16 16 PRO HA H 4.29 . . 51 16 16 PRO HB2 H 2.36 . . 52 16 16 PRO HB3 H 1.79 . . 53 16 16 PRO HG2 H 1.63 . . 54 16 16 PRO HD2 H 3.38 . . 55 16 16 PRO HD3 H 2.88 . . 56 16 16 PRO CA C 64.6 . . 57 16 16 PRO CB C 31.7 . . 58 16 16 PRO CG C 28.2 . . 59 16 16 PRO CD C 50.6 . . 60 17 17 ASN H H 7.41 . . 61 17 17 ASN HA H 4.60 . . 62 17 17 ASN HB2 H 3.05 . . 63 17 17 ASN HB3 H 2.81 . . 64 17 17 ASN C C 175.7 . . 65 17 17 ASN CA C 52.2 . . 66 17 17 ASN CB C 37.5 . . 67 18 18 ASN H H 8.26 . . 68 18 18 ASN HA H 4.17 . . 69 18 18 ASN HB2 H 3.01 . . 70 18 18 ASN HB3 H 3.06 . . 71 18 18 ASN HD21 H 7.52 . . 72 18 18 ASN HD22 H 6.82 . . 73 18 18 ASN C C 174.6 . . 74 18 18 ASN CA C 55.5 . . 75 18 18 ASN CB C 37.4 . . 76 18 18 ASN N N 111.8 . . 77 18 18 ASN ND2 N 112.9 . . 78 19 19 ASP H H 7.45 . . 79 19 19 ASP HA H 4.72 . . 80 19 19 ASP HB2 H 2.98 . . 81 19 19 ASP HB3 H 2.75 . . 82 19 19 ASP C C 174.7 . . 83 19 19 ASP CA C 54.7 . . 84 19 19 ASP CB C 41.0 . . 85 19 19 ASP N N 119.8 . . 86 20 20 LYS H H 8.63 . . 87 20 20 LYS HA H 4.66 . . 88 20 20 LYS HB2 H 1.92 . . 89 20 20 LYS HB3 H 1.82 . . 90 20 20 LYS HG2 H 1.47 . . 91 20 20 LYS HG3 H 1.53 . . 92 20 20 LYS HD2 H 1.64 . . 93 20 20 LYS HE2 H 2.96 . . 94 20 20 LYS C C 176.8 . . 95 20 20 LYS CA C 56.1 . . 96 20 20 LYS CB C 33.8 . . 97 20 20 LYS CG C 24.9 . . 98 20 20 LYS CD C 28.7 . . 99 20 20 LYS N N 119.5 . . 100 21 21 GLY H H 8.36 . . 101 21 21 GLY HA2 H 4.66 . . 102 21 21 GLY HA3 H 3.66 . . 103 21 21 GLY C C 174.1 . . 104 21 21 GLY CA C 45.5 . . 105 21 21 GLY N N 109.4 . . 106 22 22 THR H H 8.11 . . 107 22 22 THR HA H 4.85 . . 108 22 22 THR HB H 3.72 . . 109 22 22 THR HG2 H 1.02 . . 110 22 22 THR C C 174.2 . . 111 22 22 THR CA C 61.2 . . 112 22 22 THR CB C 71.9 . . 113 22 22 THR CG2 C 22.0 . . 114 22 22 THR N N 113.8 . . 115 23 23 CYS H H 9.03 . . 116 23 23 CYS HA H 4.88 . . 117 23 23 CYS HB2 H 2.94 . . 118 23 23 CYS HB3 H 2.85 . . 119 23 23 CYS C C 173.8 . . 120 23 23 CYS CA C 56.6 . . 121 23 23 CYS CB C 41.1 . . 122 23 23 CYS N N 126.3 . . 123 24 24 LYS H H 8.99 . . 124 24 24 LYS HA H 4.72 . . 125 24 24 LYS HB2 H 1.83 . . 126 24 24 LYS HB3 H 1.55 . . 127 24 24 LYS HG2 H 1.37 . . 128 24 24 LYS HD2 H 1.55 . . 129 24 24 LYS HE2 H 2.85 . . 130 24 24 LYS HE3 H 2.78 . . 131 24 24 LYS C C 174.2 . . 132 24 24 LYS CA C 54.8 . . 133 24 24 LYS CB C 37.2 . . 134 24 24 LYS CG C 23.6 . . 135 24 24 LYS CD C 29.9 . . 136 24 24 LYS CE C 42.0 . . 137 24 24 LYS N N 128.6 . . 138 25 25 SER H H 8.63 . . 139 25 25 SER HA H 4.23 . . 140 25 25 SER HB2 H 3.96 . . 141 25 25 SER HB3 H 3.62 . . 142 25 25 SER C C 176.0 . . 143 25 25 SER CA C 58.6 . . 144 25 25 SER CB C 63.5 . . 145 25 25 SER N N 114.2 . . 146 26 26 LEU H H 8.81 . . 147 26 26 LEU HA H 3.82 . . 148 26 26 LEU HB2 H 1.41 . . 149 26 26 LEU HB3 H 1.56 . . 150 26 26 LEU HG H 1.35 . . 151 26 26 LEU HD1 H 0.79 . . 152 26 26 LEU HD2 H 0.81 . . 153 26 26 LEU C C 178.2 . . 154 26 26 LEU CA C 59.0 . . 155 26 26 LEU CB C 43.1 . . 156 26 26 LEU CD1 C 24.7 . . 157 26 26 LEU N N 128.2 . . 158 27 27 LEU H H 7.64 . . 159 27 27 LEU HA H 4.05 . . 160 27 27 LEU HB2 H 1.58 . . 161 27 27 LEU HG H 1.59 . . 162 27 27 LEU HD1 H 0.90 . . 163 27 27 LEU HD2 H 0.83 . . 164 27 27 LEU C C 178.4 . . 165 27 27 LEU CA C 56.4 . . 166 27 27 LEU CB C 41.3 . . 167 27 27 LEU CG C 27.3 . . 168 27 27 LEU CD1 C 25.1 . . 169 27 27 LEU CD2 C 22.6 . . 170 27 27 LEU N N 113.2 . . 171 28 28 GLN H H 7.55 . . 172 28 28 GLN HA H 4.44 . . 173 28 28 GLN HB2 H 2.32 . . 174 28 28 GLN HB3 H 1.83 . . 175 28 28 GLN HG2 H 2.29 . . 176 28 28 GLN HG3 H 2.22 . . 177 28 28 GLN C C 174.2 . . 178 28 28 GLN CA C 54.7 . . 179 28 28 GLN CB C 29.5 . . 180 28 28 GLN CG C 34.0 . . 181 28 28 GLN N N 115.2 . . 182 29 29 CYS H H 7.70 . . 183 29 29 CYS HA H 5.15 . . 184 29 29 CYS HB2 H 3.25 . . 185 29 29 CYS HB3 H 2.43 . . 186 29 29 CYS CA C 53.8 . . 187 29 29 CYS CB C 39.5 . . 188 29 29 CYS N N 119.6 . . 189 30 30 ASP H H 7.71 . . 190 30 30 ASP HA H 4.29 . . 191 30 30 ASP HB2 H 2.68 . . 192 30 30 ASP HB3 H 2.60 . . 193 30 30 ASP C C 178.4 . . 194 30 30 ASP CA C 58.6 . . 195 30 30 ASP CB C 40.9 . . 196 31 31 VAL H H 8.76 . . 197 31 31 VAL HA H 3.62 . . 198 31 31 VAL HB H 1.82 . . 199 31 31 VAL HG1 H 1.01 . . 200 31 31 VAL HG2 H 0.85 . . 201 31 31 VAL C C 177.0 . . 202 31 31 VAL CA C 66.9 . . 203 31 31 VAL CB C 31.8 . . 204 31 31 VAL CG1 C 23.3 . . 205 31 31 VAL CG2 C 21.0 . . 206 31 31 VAL N N 117.7 . . 207 32 32 ALA H H 6.76 . . 208 32 32 ALA HA H 4.01 . . 209 32 32 ALA HB H 1.40 . . 210 32 32 ALA C C 178.7 . . 211 32 32 ALA CA C 55.4 . . 212 32 32 ALA CB C 19.2 . . 213 32 32 ALA N N 120.1 . . 214 33 33 SER H H 8.22 . . 215 33 33 SER HA H 4.05 . . 216 33 33 SER HB2 H 3.84 . . 217 33 33 SER C C 176.9 . . 218 33 33 SER CA C 62.6 . . 219 33 33 SER CB C 63.6 . . 220 33 33 SER N N 113.1 . . 221 34 34 LYS H H 8.08 . . 222 34 34 LYS HA H 4.00 . . 223 34 34 LYS HB2 H 1.88 . . 224 34 34 LYS HB3 H 1.84 . . 225 34 34 LYS HG2 H 1.56 . . 226 34 34 LYS HD2 H 1.64 . . 227 34 34 LYS HE2 H 2.87 . . 228 34 34 LYS HE3 H 3.07 . . 229 34 34 LYS C C 179.3 . . 230 34 34 LYS CA C 59.5 . . 231 34 34 LYS CB C 32.6 . . 232 34 34 LYS CG C 25.9 . . 233 34 34 LYS CD C 29.2 . . 234 34 34 LYS CE C 42.0 . . 235 34 34 LYS N N 122.6 . . 236 35 35 ILE H H 7.81 . . 237 35 35 ILE HA H 3.46 . . 238 35 35 ILE HB H 1.88 . . 239 35 35 ILE HG12 H 1.90 . . 240 35 35 ILE HG13 H 0.32 . . 241 35 35 ILE HG2 H 0.76 . . 242 35 35 ILE HD1 H 0.46 . . 243 35 35 ILE C C 177.7 . . 244 35 35 ILE CA C 66.0 . . 245 35 35 ILE CB C 37.8 . . 246 35 35 ILE CG1 C 28.4 . . 247 35 35 ILE CG2 C 17.8 . . 248 35 35 ILE CD1 C 13.4 . . 249 35 35 ILE N N 118.9 . . 250 36 36 ILE H H 8.21 . . 251 36 36 ILE HA H 3.67 . . 252 36 36 ILE HB H 1.90 . . 253 36 36 ILE HG12 H 1.24 . . 254 36 36 ILE HG13 H 1.60 . . 255 36 36 ILE HG2 H 0.93 . . 256 36 36 ILE HD1 H 0.80 . . 257 36 36 ILE C C 177.3 . . 258 36 36 ILE CA C 64.4 . . 259 36 36 ILE CB C 37.8 . . 260 36 36 ILE CG1 C 30.5 . . 261 36 36 ILE CG2 C 17.0 . . 262 36 36 ILE CD1 C 14.0 . . 263 36 36 ILE N N 117.2 . . 264 37 37 SER H H 7.37 . . 265 37 37 SER HA H 4.35 . . 266 37 37 SER HB2 H 3.94 . . 267 37 37 SER C C 173.5 . . 268 37 37 SER CA C 59.0 . . 269 37 37 SER CB C 64.2 . . 270 37 37 SER N N 113.5 . . 271 38 38 LYS H H 7.27 . . 272 38 38 LYS HA H 3.92 . . 273 38 38 LYS HB2 H 1.84 . . 274 38 38 LYS HB3 H 1.62 . . 275 38 38 LYS HG2 H 1.21 . . 276 38 38 LYS HG3 H 2.04 . . 277 38 38 LYS HD2 H 2.06 . . 278 38 38 LYS HE2 H 2.53 . . 279 38 38 LYS HE3 H 3.04 . . 280 38 38 LYS C C 175.5 . . 281 38 38 LYS CA C 58.3 . . 282 38 38 LYS CB C 33.4 . . 283 38 38 LYS CG C 24.6 . . 284 38 38 LYS CD C 30.5 . . 285 38 38 LYS CE C 41.4 . . 286 38 38 LYS N N 124.3 . . 287 39 39 LYS H H 8.42 . . 288 39 39 LYS HA H 4.72 . . 289 39 39 LYS HB2 H 1.68 . . 290 39 39 LYS HB3 H 1.42 . . 291 39 39 LYS HG2 H 1.28 . . 292 39 39 LYS HD2 H 1.63 . . 293 39 39 LYS HE2 H 2.97 . . 294 39 39 LYS HE3 H 2.88 . . 295 39 39 LYS CA C 52.7 . . 296 39 39 LYS CB C 34.7 . . 297 39 39 LYS CG C 24.2 . . 298 39 39 LYS CD C 29.3 . . 299 39 39 LYS CE C 42.2 . . 300 39 39 LYS N N 120.6 . . 301 40 40 PRO HA H 4.84 . . 302 40 40 PRO HB2 H 2.27 . . 303 40 40 PRO HB3 H 1.98 . . 304 40 40 PRO HG2 H 1.70 . . 305 40 40 PRO HG3 H 1.76 . . 306 40 40 PRO HD2 H 3.48 . . 307 40 40 PRO HD3 H 3.62 . . 308 40 40 PRO C C 175.8 . . 309 40 40 PRO CA C 63.2 . . 310 40 40 PRO CB C 34.4 . . 311 40 40 PRO CG C 24.1 . . 312 40 40 PRO CD C 50.0 . . 313 41 41 ARG H H 8.33 . . 314 41 41 ARG HA H 4.64 . . 315 41 41 ARG HB2 H 1.89 . . 316 41 41 ARG HG2 H 1.86 . . 317 41 41 ARG HG3 H 1.77 . . 318 41 41 ARG HD2 H 3.44 . . 319 41 41 ARG HD3 H 2.99 . . 320 41 41 ARG C C 177.7 . . 321 41 41 ARG CA C 55.4 . . 322 41 41 ARG CB C 32.0 . . 323 41 41 ARG CG C 28.0 . . 324 41 41 ARG CD C 44.1 . . 325 41 41 ARG N N 119.4 . . 326 42 42 THR H H 9.38 . . 327 42 42 THR HA H 4.48 . . 328 42 42 THR HB H 4.77 . . 329 42 42 THR HG2 H 1.32 . . 330 42 42 THR CA C 60.9 . . 331 42 42 THR CB C 72.3 . . 332 42 42 THR N N 116.1 . . 333 43 43 ALA H H 6.79 . . 334 43 43 ALA HA H 4.10 . . 335 43 43 ALA HB H 1.39 . . 336 43 43 ALA C C 181.1 . . 337 43 43 ALA CA C 55.1 . . 338 43 43 ALA CB C 17.7 . . 339 44 44 GLN H H 8.68 . . 340 44 44 GLN HA H 3.88 . . 341 44 44 GLN HB2 H 1.90 . . 342 44 44 GLN HB3 H 1.65 . . 343 44 44 GLN HG2 H 2.43 . . 344 44 44 GLN HE21 H 7.48 . . 345 44 44 GLN HE22 H 6.81 . . 346 44 44 GLN C C 179.2 . . 347 44 44 GLN CA C 60.7 . . 348 44 44 GLN CB C 26.0 . . 349 44 44 GLN CG C 35.0 . . 350 44 44 GLN N N 118.6 . . 351 44 44 GLN NE2 N 111.4 . . 352 45 45 ASP H H 8.09 . . 353 45 45 ASP HA H 4.10 . . 354 45 45 ASP HB2 H 3.22 . . 355 45 45 ASP HB3 H 2.32 . . 356 45 45 ASP C C 177.7 . . 357 45 45 ASP CA C 58.3 . . 358 45 45 ASP CB C 40.9 . . 359 45 45 ASP N N 124.3 . . 360 46 46 GLU H H 7.91 . . 361 46 46 GLU HA H 3.93 . . 362 46 46 GLU HB2 H 2.20 . . 363 46 46 GLU HB3 H 2.02 . . 364 46 46 GLU HG2 H 2.43 . . 365 46 46 GLU C C 179.2 . . 366 46 46 GLU CA C 59.6 . . 367 46 46 GLU CB C 29.2 . . 368 46 46 GLU CG C 36.4 . . 369 46 46 GLU N N 117.3 . . 370 47 47 LYS H H 8.11 . . 371 47 47 LYS HA H 3.91 . . 372 47 47 LYS HB2 H 1.85 . . 373 47 47 LYS HG2 H 1.36 . . 374 47 47 LYS HD2 H 1.63 . . 375 47 47 LYS HE2 H 3.00 . . 376 47 47 LYS C C 177.1 . . 377 47 47 LYS CA C 59.6 . . 378 47 47 LYS CB C 33.2 . . 379 47 47 LYS CG C 24.6 . . 380 47 47 LYS CD C 29.8 . . 381 47 47 LYS N N 121.3 . . 382 48 48 PHE H H 7.87 . . 383 48 48 PHE HA H 4.08 . . 384 48 48 PHE HB2 H 3.03 . . 385 48 48 PHE C C 178.7 . . 386 48 48 PHE CA C 61.4 . . 387 48 48 PHE CB C 40.4 . . 388 48 48 PHE N N 119.2 . . 389 49 49 LEU H H 8.17 . . 390 49 49 LEU HA H 3.80 . . 391 49 49 LEU HB2 H 1.93 . . 392 49 49 LEU HB3 H 1.38 . . 393 49 49 LEU HG H 1.30 . . 394 49 49 LEU HD1 H 0.81 . . 395 49 49 LEU HD2 H 0.89 . . 396 49 49 LEU C C 180.1 . . 397 49 49 LEU CA C 57.8 . . 398 49 49 LEU CB C 41.8 . . 399 49 49 LEU CD1 C 25.7 . . 400 49 49 LEU CD2 C 22.1 . . 401 49 49 LEU N N 119.4 . . 402 50 50 ARG H H 8.00 . . 403 50 50 ARG HA H 4.04 . . 404 50 50 ARG HB2 H 1.91 . . 405 50 50 ARG HB3 H 1.97 . . 406 50 50 ARG HG2 H 1.59 . . 407 50 50 ARG HG3 H 1.76 . . 408 50 50 ARG HD2 H 3.22 . . 409 50 50 ARG HD3 H 3.20 . . 410 50 50 ARG C C 179.8 . . 411 50 50 ARG CA C 59.7 . . 412 50 50 ARG CB C 30.2 . . 413 50 50 ARG CG C 27.5 . . 414 50 50 ARG CD C 43.6 . . 415 50 50 ARG N N 119.7 . . 416 51 51 GLU H H 8.24 . . 417 51 51 GLU HA H 4.09 . . 418 51 51 GLU HB2 H 1.98 . . 419 51 51 GLU HB3 H 1.85 . . 420 51 51 GLU HG2 H 2.20 . . 421 51 51 GLU HG3 H 2.51 . . 422 51 51 GLU C C 177.0 . . 423 51 51 GLU CA C 57.8 . . 424 51 51 GLU CB C 29.5 . . 425 51 51 GLU CG C 37.2 . . 426 51 51 GLU N N 117.1 . . 427 52 52 SER H H 7.47 . . 428 52 52 SER HA H 4.41 . . 429 52 52 SER HB2 H 3.78 . . 430 52 52 SER HB3 H 3.53 . . 431 52 52 SER C C 173.4 . . 432 52 52 SER CA C 58.9 . . 433 52 52 SER CB C 63.7 . . 434 52 52 SER N N 113.8 . . 435 53 53 ALA H H 6.96 . . 436 53 53 ALA HA H 4.23 . . 437 53 53 ALA HB H 1.49 . . 438 53 53 ALA C C 178.2 . . 439 53 53 ALA CA C 54.0 . . 440 53 53 ALA CB C 19.2 . . 441 53 53 ALA N N 124.9 . . 442 54 54 CYS H H 8.16 . . 443 54 54 CYS HA H 4.94 . . 444 54 54 CYS HB2 H 3.19 . . 445 54 54 CYS C C 172.7 . . 446 54 54 CYS CA C 55.7 . . 447 54 54 CYS CB C 45.8 . . 448 54 54 CYS N N 116.2 . . 449 55 55 GLY H H 7.50 . . 450 55 55 GLY HA2 H 4.33 . . 451 55 55 GLY HA3 H 3.64 . . 452 55 55 GLY C C 176.5 . . 453 55 55 GLY CA C 44.7 . . 454 55 55 GLY N N 108.8 . . 455 56 56 PHE H H 8.70 . . 456 56 56 PHE HA H 4.19 . . 457 56 56 PHE HB2 H 2.33 . . 458 56 56 PHE C C 178.6 . . 459 56 56 PHE CA C 53.6 . . 460 56 56 PHE CB C 37.7 . . 461 56 56 PHE N N 114.6 . . 462 57 57 ASP H H 7.55 . . 463 57 57 ASP HA H 4.55 . . 464 57 57 ASP HB2 H 2.67 . . 465 57 57 ASP HB3 H 2.40 . . 466 57 57 ASP CA C 54.7 . . 467 57 57 ASP CB C 41.1 . . 468 57 57 ASP N N 113.6 . . 469 58 58 GLY H H 8.27 . . 470 58 58 GLY HA2 H 3.57 . . 471 58 58 GLY HA3 H 4.05 . . 472 58 58 GLY CA C 46.4 . . 473 58 58 GLY N N 120.6 . . 474 59 59 GLN HA H 4.33 . . 475 59 59 GLN HB2 H 2.24 . . 476 59 59 GLN HB3 H 1.96 . . 477 59 59 GLN HG2 H 2.30 . . 478 59 59 GLN C C 176.0 . . 479 59 59 GLN CA C 55.9 . . 480 59 59 GLN CB C 29.5 . . 481 59 59 GLN CG C 34.1 . . 482 60 60 THR H H 8.35 . . 483 60 60 THR HA H 4.64 . . 484 60 60 THR HB H 4.32 . . 485 60 60 THR HG2 H 1.37 . . 486 60 60 THR CA C 60.5 . . 487 60 60 THR CB C 70.3 . . 488 60 60 THR CG2 C 21.9 . . 489 60 60 THR N N 119.7 . . 490 61 61 PRO HA H 4.07 . . 491 61 61 PRO HB2 H 2.16 . . 492 61 61 PRO HB3 H 1.70 . . 493 61 61 PRO HG2 H 2.06 . . 494 61 61 PRO HG3 H 2.01 . . 495 61 61 PRO HD2 H 4.12 . . 496 61 61 PRO HD3 H 3.80 . . 497 61 61 PRO C C 175.6 . . 498 61 61 PRO CA C 63.3 . . 499 61 61 PRO CB C 32.3 . . 500 61 61 PRO CG C 27.5 . . 501 61 61 PRO CD C 51.4 . . 502 62 62 LYS H H 8.03 . . 503 62 62 LYS HA H 4.66 . . 504 62 62 LYS HB2 H 1.33 . . 505 62 62 LYS HB3 H 0.96 . . 506 62 62 LYS HE2 H 2.69 . . 507 62 62 LYS C C 176.5 . . 508 62 62 LYS CA C 54.8 . . 509 62 62 LYS CB C 34.9 . . 510 62 62 LYS CG C 25.5 . . 511 62 62 LYS N N 119.2 . . 512 63 63 VAL H H 9.19 . . 513 63 63 VAL HA H 4.61 . . 514 63 63 VAL HB H 1.85 . . 515 63 63 VAL HG1 H 0.66 . . 516 63 63 VAL HG2 H 0.64 . . 517 63 63 VAL C C 173.9 . . 518 63 63 VAL CA C 58.3 . . 519 63 63 VAL CB C 35.5 . . 520 63 63 VAL CG1 C 21.9 . . 521 63 63 VAL CG2 C 19.3 . . 522 63 63 VAL N N 117.1 . . 523 64 64 CYS H H 9.06 . . 524 64 64 CYS HA H 4.32 . . 525 64 64 CYS HB2 H 2.86 . . 526 64 64 CYS HB3 H 2.79 . . 527 64 64 CYS C C 171.6 . . 528 64 64 CYS CA C 56.0 . . 529 64 64 CYS CB C 39.8 . . 530 64 64 CYS N N 123.5 . . 531 65 65 CYS H H 9.02 . . 532 65 65 CYS HA H 5.09 . . 533 65 65 CYS HB2 H 2.70 . . 534 65 65 CYS HB3 H 3.50 . . 535 65 65 CYS CA C 53.4 . . 536 65 65 CYS CB C 43.8 . . 537 65 65 CYS N N 132.0 . . 538 66 66 PRO HA H 4.66 . . 539 66 66 PRO HB2 H 2.42 . . 540 66 66 PRO HB3 H 2.38 . . 541 66 66 PRO HG2 H 2.15 . . 542 66 66 PRO HD2 H 3.73 . . 543 66 66 PRO HD3 H 4.19 . . 544 66 66 PRO C C 176.0 . . 545 66 66 PRO CA C 63.1 . . 546 66 66 PRO CB C 32.1 . . 547 66 66 PRO CG C 27.4 . . 548 66 66 PRO CD C 51.0 . . stop_ save_