data_5721 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of a aminoglycoside-3'-phosphotransferase from Klebsiella pneumoniae ; _BMRB_accession_number 5721 _BMRB_flat_file_name bmr5721.str _Entry_type original _Submission_date 2003-03-10 _Accession_date 2003-03-10 _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 Stoldt Matthias . . 2 Kupce Eriks . . 3 Gorlach Matthias . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 449 "13C chemical shifts" 709 "15N chemical shifts" 233 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignment of an aminoglycoside-3'-phosphotransferase type IIa ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14739646 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stoldt Matthias . . 2 Kupce Eriks . . 3 Rehm Bernd H.A. . 4 Gorlach Matthias . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 93 _Page_last 94 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_APH _Saveframe_category molecular_system _Mol_system_name APH(3')II _Abbreviation_common APH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'APH(3')II monomer' $APH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_APH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Aminoglycoside-3'-phosphotransferase _Abbreviation_common APH _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 264 _Mol_residue_sequence ; MIEQDGLHAGSPAAWVERLF GYDWAQQTIGCSDAAVFRLS AQGRPVLFVKTDLSGALNEL QDEAARLSWLATTGVPCAAV LDVVTEAGRDWLLLGEVPGQ DLLSSHLAPAEKVSIMADAM RRLHTLDPATCPFDHQAKHR IERARTRMEAGLVDQDDLDE EHQGLAPAELFARLKARMPD GEDLVVTHGDACLPNIMVEN GRFSGFIDCGRLGVADRYQD IALATRDIAEELGGEWADRF LVLYGIAAPDSQRIAFYRLL DEFF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 GLU 4 GLN 5 ASP 6 GLY 7 LEU 8 HIS 9 ALA 10 GLY 11 SER 12 PRO 13 ALA 14 ALA 15 TRP 16 VAL 17 GLU 18 ARG 19 LEU 20 PHE 21 GLY 22 TYR 23 ASP 24 TRP 25 ALA 26 GLN 27 GLN 28 THR 29 ILE 30 GLY 31 CYS 32 SER 33 ASP 34 ALA 35 ALA 36 VAL 37 PHE 38 ARG 39 LEU 40 SER 41 ALA 42 GLN 43 GLY 44 ARG 45 PRO 46 VAL 47 LEU 48 PHE 49 VAL 50 LYS 51 THR 52 ASP 53 LEU 54 SER 55 GLY 56 ALA 57 LEU 58 ASN 59 GLU 60 LEU 61 GLN 62 ASP 63 GLU 64 ALA 65 ALA 66 ARG 67 LEU 68 SER 69 TRP 70 LEU 71 ALA 72 THR 73 THR 74 GLY 75 VAL 76 PRO 77 CYS 78 ALA 79 ALA 80 VAL 81 LEU 82 ASP 83 VAL 84 VAL 85 THR 86 GLU 87 ALA 88 GLY 89 ARG 90 ASP 91 TRP 92 LEU 93 LEU 94 LEU 95 GLY 96 GLU 97 VAL 98 PRO 99 GLY 100 GLN 101 ASP 102 LEU 103 LEU 104 SER 105 SER 106 HIS 107 LEU 108 ALA 109 PRO 110 ALA 111 GLU 112 LYS 113 VAL 114 SER 115 ILE 116 MET 117 ALA 118 ASP 119 ALA 120 MET 121 ARG 122 ARG 123 LEU 124 HIS 125 THR 126 LEU 127 ASP 128 PRO 129 ALA 130 THR 131 CYS 132 PRO 133 PHE 134 ASP 135 HIS 136 GLN 137 ALA 138 LYS 139 HIS 140 ARG 141 ILE 142 GLU 143 ARG 144 ALA 145 ARG 146 THR 147 ARG 148 MET 149 GLU 150 ALA 151 GLY 152 LEU 153 VAL 154 ASP 155 GLN 156 ASP 157 ASP 158 LEU 159 ASP 160 GLU 161 GLU 162 HIS 163 GLN 164 GLY 165 LEU 166 ALA 167 PRO 168 ALA 169 GLU 170 LEU 171 PHE 172 ALA 173 ARG 174 LEU 175 LYS 176 ALA 177 ARG 178 MET 179 PRO 180 ASP 181 GLY 182 GLU 183 ASP 184 LEU 185 VAL 186 VAL 187 THR 188 HIS 189 GLY 190 ASP 191 ALA 192 CYS 193 LEU 194 PRO 195 ASN 196 ILE 197 MET 198 VAL 199 GLU 200 ASN 201 GLY 202 ARG 203 PHE 204 SER 205 GLY 206 PHE 207 ILE 208 ASP 209 CYS 210 GLY 211 ARG 212 LEU 213 GLY 214 VAL 215 ALA 216 ASP 217 ARG 218 TYR 219 GLN 220 ASP 221 ILE 222 ALA 223 LEU 224 ALA 225 THR 226 ARG 227 ASP 228 ILE 229 ALA 230 GLU 231 GLU 232 LEU 233 GLY 234 GLY 235 GLU 236 TRP 237 ALA 238 ASP 239 ARG 240 PHE 241 LEU 242 VAL 243 LEU 244 TYR 245 GLY 246 ILE 247 ALA 248 ALA 249 PRO 250 ASP 251 SER 252 GLN 253 ARG 254 ILE 255 ALA 256 PHE 257 TYR 258 ARG 259 LEU 260 LEU 261 ASP 262 GLU 263 PHE 264 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1ND4 "Crystal Structure Of Aminoglycoside-3'-Phosphotransferase- Iia" 100.00 264 100.00 100.00 0.00e+00 DBJ BAA21468 "neomycin-kanamycin phosphotransferase [Cloning vector pMW218]" 100.00 264 99.62 99.62 0.00e+00 DBJ BAA21470 "neomycin-kanamycin phosphotransferase [Cloning vector pMW219]" 100.00 264 99.62 99.62 0.00e+00 DBJ BAA23653 "neomycin phosphotransferase [Cloning vector pAP3neo]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAA78209 "neomycine phosphotransferase [Dual-tagging gene trap vector pGT1]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAA94847 "neo [Retroviral vector pCXneo]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA03938 "neomycin phosphotransferase [synthetic construct]" 99.62 265 100.00 100.00 0.00e+00 EMBL CAA07593 "aminoglycoside phosphotransferase [Cloning vector pEH1]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA23892 "neomycin phosphotransferase [Escherichia coli]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA54105 "lacZ neomycin phosphotransferase fusion protein [synthetic construct]" 98.48 1311 100.00 100.00 6.08e-175 EMBL CAA54106 "unnamed protein product [synthetic construct]" 99.62 267 100.00 100.00 0.00e+00 GB AAA03699 "neomycin phosphotransferase [Human immunodeficiency virus 1]" 100.00 264 100.00 100.00 0.00e+00 GB AAA56726 "aminoglycoside 3'-phosphotransferase [unidentified cloning vector]" 100.00 264 100.00 100.00 0.00e+00 GB AAA61621 "aminoglycoside phosphotransferase [Cloning vector pKSM711]" 100.00 264 100.00 100.00 0.00e+00 GB AAA61623 "aminoglycoside phosphotransferase [Cloning vector pKSM713]" 100.00 264 100.00 100.00 0.00e+00 GB AAA61626 "aminoglycoside phosphotransferase [Cloning vector pKSM715]" 100.00 264 100.00 100.00 0.00e+00 REF WP_000572405 "MULTISPECIES: aminoglycoside 3'-phosphotransferase [Bacteria]" 100.00 264 100.00 100.00 0.00e+00 REF WP_000572406 "MULTISPECIES: aminoglycoside 3'-phosphotransferase [Bacteria]" 100.00 264 99.62 99.62 0.00e+00 REF WP_004614937 "aminoglycoside 3'-phosphotransferase [Tyzzerella nexilis]" 100.00 264 99.62 99.62 0.00e+00 REF WP_017432000 "hypothetical protein, partial [Staphylococcus aureus]" 73.11 193 100.00 100.00 1.83e-134 REF WP_024031215 "aminoglycoside phosphotransferase, partial [Bacillus vireti]" 62.12 164 98.78 98.78 2.64e-111 SP P00552 "RecName: Full=Aminoglycoside 3'-phosphotransferase; AltName: Full=APH(3')-II; Short=APH(3')II; AltName: Full=Kanamycin kinase, " 100.00 264 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $APH 'Klebsiella pneumoniae' 573 Eubacteria . Klebsiella pneumoniae 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 $APH 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $APH 1.0 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityINOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityINOVA _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityINOVA _Field_strength 900 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 external indirect . . . . DSS N 15 'methyl protons' ppm 0.0 external indirect . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'APH(3')II monomer' _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 . 2 ILE CA C 61.1 0.1 1 2 . 2 ILE CB C 38.0 0.1 1 3 . 2 ILE C C 176.1 0.1 1 4 . 3 GLU N N 126.1 0.1 1 5 . 3 GLU H H 8.51 0.02 1 6 . 3 GLU CA C 56.5 0.1 1 7 . 3 GLU HA H 4.20 0.02 1 8 . 3 GLU CB C 29.7 0.1 1 9 . 3 GLU C C 176.8 0.1 1 10 . 4 GLN N N 122.1 0.1 1 11 . 4 GLN H H 8.35 0.02 1 12 . 4 GLN CA C 55.9 0.1 1 13 . 4 GLN HA H 4.23 0.02 1 14 . 4 GLN CB C 29.0 0.1 1 15 . 4 GLN C C 176.0 0.1 1 16 . 5 ASP N N 121.7 0.1 1 17 . 5 ASP H H 8.24 0.02 1 18 . 5 ASP CA C 54.4 0.1 1 19 . 5 ASP HA H 4.48 0.02 1 20 . 5 ASP CB C 40.8 0.1 1 21 . 5 ASP C C 177.0 0.1 1 22 . 6 GLY N N 109.2 0.1 1 23 . 6 GLY H H 8.13 0.02 1 24 . 6 GLY CA C 45.3 0.1 1 25 . 6 GLY HA2 H 3.84 0.02 1 26 . 6 GLY HA3 H 3.84 0.02 1 27 . 6 GLY C C 174.8 0.1 1 28 . 7 LEU N N 122.2 0.1 1 29 . 7 LEU H H 8.04 0.02 1 30 . 7 LEU CA C 55.6 0.1 1 31 . 7 LEU HA H 4.11 0.02 1 32 . 7 LEU CB C 41.5 0.1 1 33 . 7 LEU C C 177.6 0.1 1 34 . 8 HIS N N 118.9 0.1 1 35 . 8 HIS H H 8.16 0.02 1 36 . 8 HIS CA C 55.3 0.1 1 37 . 8 HIS HA H 4.14 0.02 1 38 . 8 HIS CB C 28.3 0.1 1 39 . 8 HIS C C 174.8 0.1 1 40 . 9 ALA N N 124.3 0.1 1 41 . 9 ALA H H 7.71 0.02 1 42 . 9 ALA CA C 52.8 0.1 1 43 . 9 ALA HA H 3.87 0.02 1 44 . 9 ALA CB C 18.0 0.1 1 45 . 9 ALA C C 177.8 0.1 1 46 . 10 GLY N N 108.3 0.1 1 47 . 10 GLY H H 7.78 0.02 1 48 . 10 GLY CA C 44.5 0.1 1 49 . 10 GLY HA2 H 3.65 0.02 2 50 . 10 GLY HA3 H 3.59 0.02 2 51 . 10 GLY C C 173.0 0.1 1 52 . 11 SER N N 115.1 0.1 1 53 . 11 SER H H 7.11 0.02 1 54 . 11 SER CA C 56.3 0.1 1 55 . 11 SER HA H 2.98 0.02 1 56 . 11 SER CB C 61.8 0.1 1 57 . 12 PRO CA C 62.9 0.1 1 58 . 12 PRO CB C 30.3 0.1 1 59 . 12 PRO C C 178.4 0.1 1 60 . 13 ALA N N 132.9 0.1 1 61 . 13 ALA H H 9.41 0.02 1 62 . 13 ALA CA C 54.7 0.1 1 63 . 13 ALA CB C 17.1 0.1 1 64 . 13 ALA C C 181.2 0.1 1 65 . 14 ALA N N 118.3 0.1 1 66 . 14 ALA H H 8.62 0.02 1 67 . 14 ALA CA C 53.5 0.1 1 68 . 14 ALA HA H 4.09 0.02 1 69 . 14 ALA CB C 18.0 0.1 1 70 . 14 ALA C C 179.2 0.1 1 71 . 15 TRP N N 116.6 0.1 1 72 . 15 TRP H H 7.38 0.02 1 73 . 15 TRP CA C 54.1 0.1 1 74 . 15 TRP HA H 4.84 0.02 1 75 . 15 TRP CB C 29.8 0.1 1 76 . 15 TRP C C 176.5 0.1 1 77 . 16 VAL N N 121.3 0.1 1 78 . 16 VAL H H 7.24 0.02 1 79 . 16 VAL CA C 66.6 0.1 1 80 . 16 VAL HA H 3.60 0.02 1 81 . 16 VAL CB C 31.0 0.1 1 82 . 16 VAL C C 178.3 0.1 1 83 . 17 GLU N N 118.0 0.1 1 84 . 17 GLU H H 8.14 0.02 1 85 . 17 GLU CA C 59.0 0.1 1 86 . 17 GLU HA H 4.09 0.02 1 87 . 17 GLU CB C 28.7 0.1 1 88 . 17 GLU C C 179.9 0.1 1 89 . 18 ARG N N 120.4 0.1 1 90 . 18 ARG H H 8.19 0.02 1 91 . 18 ARG CA C 58.3 0.1 1 92 . 18 ARG HA H 4.09 0.02 1 93 . 18 ARG CB C 29.7 0.1 1 94 . 18 ARG C C 177.9 0.1 1 95 . 19 LEU N N 115.0 0.1 1 96 . 19 LEU H H 7.84 0.02 1 97 . 19 LEU CA C 53.1 0.1 1 98 . 19 LEU HA H 4.59 0.02 1 99 . 19 LEU CB C 39.6 0.1 1 100 . 19 LEU C C 177.2 0.1 1 101 . 20 PHE N N 125.7 0.1 1 102 . 20 PHE H H 7.39 0.02 1 103 . 20 PHE CA C 60.6 0.1 1 104 . 20 PHE HA H 4.27 0.02 1 105 . 20 PHE CB C 38.3 0.1 1 106 . 20 PHE C C 177.3 0.1 1 107 . 21 GLY N N 116.9 0.1 1 108 . 21 GLY H H 8.43 0.02 1 109 . 21 GLY CA C 44.5 0.1 1 110 . 21 GLY HA2 H 3.84 0.02 2 111 . 21 GLY HA3 H 3.15 0.02 2 112 . 21 GLY C C 174.7 0.1 1 113 . 22 TYR N N 119.0 0.1 1 114 . 22 TYR H H 7.69 0.02 1 115 . 22 TYR CA C 59.5 0.1 1 116 . 22 TYR HA H 4.18 0.02 1 117 . 22 TYR CB C 38.0 0.1 1 118 . 22 TYR C C 176.7 0.1 1 119 . 23 ASP N N 123.4 0.1 1 120 . 23 ASP H H 9.05 0.02 1 121 . 23 ASP CA C 53.7 0.1 1 122 . 23 ASP HA H 5.00 0.02 1 123 . 23 ASP CB C 42.4 0.1 1 124 . 23 ASP C C 175.8 0.1 1 125 . 24 TRP N N 124.6 0.1 1 126 . 24 TRP H H 9.08 0.02 1 127 . 24 TRP CA C 56.8 0.1 1 128 . 24 TRP HA H 4.64 0.02 1 129 . 24 TRP CB C 29.1 0.1 1 130 . 24 TRP C C 175.9 0.1 1 131 . 25 ALA N N 126.3 0.1 1 132 . 25 ALA H H 8.78 0.02 1 133 . 25 ALA CA C 50.6 0.1 1 134 . 25 ALA HA H 4.97 0.02 1 135 . 25 ALA CB C 20.1 0.1 1 136 . 25 ALA C C 177.5 0.1 1 137 . 26 GLN N N 129.3 0.1 1 138 . 26 GLN H H 9.47 0.02 1 139 . 26 GLN CA C 57.4 0.1 1 140 . 26 GLN CB C 28.4 0.1 1 141 . 26 GLN C C 176.4 0.1 1 142 . 27 GLN N N 126.6 0.1 1 143 . 27 GLN H H 9.12 0.02 1 144 . 27 GLN CA C 55.6 0.1 1 145 . 27 GLN HA H 4.40 0.02 1 146 . 27 GLN CB C 30.5 0.1 1 147 . 27 GLN C C 176.4 0.1 1 148 . 28 THR N N 112.6 0.1 1 149 . 28 THR H H 7.53 0.02 1 150 . 28 THR CA C 60.7 0.1 1 151 . 28 THR HA H 4.31 0.02 1 152 . 28 THR CB C 69.6 0.1 1 153 . 28 THR C C 174.6 0.1 1 154 . 29 ILE N N 122.9 0.1 1 155 . 29 ILE H H 8.27 0.02 1 156 . 29 ILE CA C 60.7 0.1 1 157 . 29 ILE HA H 4.17 0.02 1 158 . 29 ILE CB C 38.4 0.1 1 159 . 29 ILE C C 176.9 0.1 1 160 . 30 GLY N N 113.8 0.1 1 161 . 30 GLY H H 8.36 0.02 1 162 . 30 GLY CA C 44.9 0.1 1 163 . 30 GLY HA2 H 4.02 0.02 2 164 . 30 GLY HA3 H 3.87 0.02 2 165 . 30 GLY C C 174.2 0.1 1 166 . 31 CYS N N 119.1 0.1 1 167 . 31 CYS H H 8.27 0.02 1 168 . 31 CYS CA C 57.9 0.1 1 169 . 31 CYS HA H 4.58 0.02 1 170 . 31 CYS CB C 27.5 0.1 1 171 . 31 CYS C C 174.6 0.1 1 172 . 32 SER N N 118.8 0.1 1 173 . 32 SER H H 8.08 0.02 1 174 . 32 SER CA C 57.8 0.1 1 175 . 32 SER HA H 4.46 0.02 1 176 . 32 SER CB C 63.6 0.1 1 177 . 32 SER C C 174.2 0.1 1 178 . 33 ASP N N 121.5 0.1 1 179 . 33 ASP H H 8.25 0.02 1 180 . 33 ASP CA C 56.2 0.1 1 181 . 33 ASP HA H 4.48 0.02 1 182 . 33 ASP CB C 41.6 0.1 1 183 . 33 ASP C C 175.6 0.1 1 184 . 34 ALA N N 123.0 0.1 1 185 . 34 ALA H H 7.75 0.02 1 186 . 34 ALA CA C 50.8 0.1 1 187 . 34 ALA HA H 4.86 0.02 1 188 . 34 ALA CB C 18.7 0.1 1 189 . 34 ALA C C 177.0 0.1 1 190 . 35 ALA N N 123.8 0.1 1 191 . 35 ALA H H 8.31 0.02 1 192 . 35 ALA CA C 51.2 0.1 1 193 . 35 ALA HA H 4.51 0.02 1 194 . 35 ALA CB C 22.5 0.1 1 195 . 35 ALA C C 175.5 0.1 1 196 . 36 VAL N N 119.4 0.1 1 197 . 36 VAL H H 7.49 0.02 1 198 . 36 VAL CA C 60.6 0.1 1 199 . 36 VAL HA H 5.11 0.02 1 200 . 36 VAL CB C 34.3 0.1 1 201 . 36 VAL C C 174.9 0.1 1 202 . 37 PHE N N 125.0 0.1 1 203 . 37 PHE H H 9.85 0.02 1 204 . 37 PHE CA C 55.6 0.1 1 205 . 37 PHE HA H 5.29 0.02 1 206 . 37 PHE CB C 43.2 0.1 1 207 . 37 PHE C C 173.8 0.1 1 208 . 38 ARG N N 123.4 0.1 1 209 . 38 ARG H H 8.94 0.02 1 210 . 38 ARG CA C 54.7 0.1 1 211 . 38 ARG HA H 3.16 0.02 1 212 . 38 ARG CB C 32.3 0.1 1 213 . 38 ARG C C 174.7 0.1 1 214 . 39 LEU N N 136.0 0.1 1 215 . 39 LEU H H 9.31 0.02 1 216 . 39 LEU CA C 53.8 0.1 1 217 . 39 LEU HA H 5.27 0.02 1 218 . 39 LEU CB C 41.4 0.1 1 219 . 39 LEU C C 174.8 0.1 1 220 . 40 SER N N 113.8 0.1 1 221 . 40 SER H H 8.34 0.02 1 222 . 40 SER CA C 55.7 0.1 1 223 . 40 SER HA H 5.05 0.02 1 224 . 40 SER CB C 66.7 0.1 1 225 . 40 SER C C 173.3 0.1 1 226 . 41 ALA N N 124.4 0.1 1 227 . 41 ALA H H 8.70 0.02 1 228 . 41 ALA CA C 51.6 0.1 1 229 . 41 ALA HA H 4.23 0.02 1 230 . 41 ALA CB C 20.7 0.1 1 231 . 41 ALA C C 176.6 0.1 1 232 . 42 GLN N N 122.5 0.1 1 233 . 42 GLN H H 8.45 0.02 1 234 . 42 GLN CA C 57.2 0.1 1 235 . 42 GLN HA H 3.92 0.02 1 236 . 42 GLN CB C 27.7 0.1 1 237 . 42 GLN C C 177.9 0.1 1 238 . 43 GLY N N 114.5 0.1 1 239 . 43 GLY H H 8.90 0.02 1 240 . 43 GLY CA C 45.5 0.1 1 241 . 43 GLY HA2 H 3.92 0.02 1 242 . 43 GLY HA3 H 3.92 0.02 1 243 . 43 GLY C C 173.7 0.1 1 244 . 44 ARG N N 119.8 0.1 1 245 . 44 ARG H H 7.53 0.02 1 246 . 44 ARG CA C 53.1 0.1 1 247 . 44 ARG HA H 4.76 0.02 1 248 . 44 ARG CB C 30.3 0.1 1 249 . 45 PRO CA C 62.5 0.1 1 250 . 45 PRO CB C 31.5 0.1 1 251 . 45 PRO C C 176.9 0.1 1 252 . 46 VAL N N 126.5 0.1 1 253 . 46 VAL H H 8.47 0.02 1 254 . 46 VAL CA C 63.0 0.1 1 255 . 46 VAL HA H 4.10 0.02 1 256 . 46 VAL CB C 31.3 0.1 1 257 . 46 VAL C C 174.7 0.1 1 258 . 47 LEU N N 125.2 0.1 1 259 . 47 LEU H H 7.74 0.02 1 260 . 47 LEU CA C 52.0 0.1 1 261 . 47 LEU HA H 4.91 0.02 1 262 . 47 LEU CB C 44.6 0.1 1 263 . 47 LEU C C 174.8 0.1 1 264 . 48 PHE N N 117.5 0.1 1 265 . 48 PHE H H 8.92 0.02 1 266 . 48 PHE CA C 56.2 0.1 1 267 . 48 PHE HA H 5.28 0.02 1 268 . 48 PHE CB C 42.9 0.1 1 269 . 48 PHE C C 174.7 0.1 1 270 . 49 VAL N N 120.5 0.1 1 271 . 49 VAL H H 8.81 0.02 1 272 . 49 VAL CA C 59.6 0.1 1 273 . 49 VAL HA H 5.40 0.02 1 274 . 49 VAL CB C 35.2 0.1 1 275 . 49 VAL C C 176.1 0.1 1 276 . 50 LYS N N 125.2 0.1 1 277 . 50 LYS H H 9.29 0.02 1 278 . 50 LYS CA C 54.5 0.1 1 279 . 50 LYS HA H 5.52 0.02 1 280 . 50 LYS CB C 35.5 0.1 1 281 . 50 LYS C C 175.3 0.1 1 282 . 51 THR N N 115.7 0.1 1 283 . 51 THR H H 8.65 0.02 1 284 . 51 THR CA C 58.2 0.1 1 285 . 51 THR HA H 5.20 0.02 1 286 . 51 THR CB C 69.2 0.1 1 287 . 51 THR C C 171.4 0.1 1 288 . 52 ASP N N 125.1 0.1 1 289 . 52 ASP H H 7.70 0.02 1 290 . 52 ASP CA C 52.3 0.1 1 291 . 52 ASP HA H 4.91 0.02 1 292 . 52 ASP CB C 42.5 0.1 1 293 . 52 ASP C C 175.4 0.1 1 294 . 53 LEU N N 123.2 0.1 1 295 . 53 LEU H H 9.31 0.02 1 296 . 53 LEU CA C 55.4 0.1 1 297 . 53 LEU HA H 5.16 0.02 1 298 . 53 LEU CB C 41.0 0.1 1 299 . 53 LEU C C 178.7 0.1 1 300 . 54 SER N N 119.5 0.1 1 301 . 54 SER H H 8.39 0.02 1 302 . 54 SER CA C 59.2 0.1 1 303 . 54 SER HA H 4.08 0.02 1 304 . 54 SER CB C 62.9 0.1 1 305 . 55 GLY CA C 45.1 0.1 1 306 . 55 GLY C C 174.2 0.1 1 307 . 56 ALA N N 123.2 0.1 1 308 . 56 ALA H H 8.16 0.02 1 309 . 56 ALA CA C 53.6 0.1 1 310 . 56 ALA CB C 18.6 0.1 1 311 . 56 ALA C C 179.0 0.1 1 312 . 57 LEU N N 116.5 0.1 1 313 . 57 LEU H H 8.24 0.02 1 314 . 57 LEU CA C 54.5 0.1 1 315 . 57 LEU HA H 4.28 0.02 1 316 . 57 LEU CB C 40.4 0.1 1 317 . 60 LEU CB C 40.2 0.1 1 318 . 60 LEU C C 179.4 0.1 1 319 . 61 GLN N N 119.3 0.1 1 320 . 61 GLN H H 8.28 0.02 1 321 . 61 GLN CA C 59.0 0.1 1 322 . 61 GLN HA H 4.58 0.02 1 323 . 61 GLN CB C 26.4 0.1 1 324 . 61 GLN C C 180.3 0.1 1 325 . 62 ASP N N 121.2 0.1 1 326 . 62 ASP H H 8.06 0.02 1 327 . 62 ASP CA C 57.0 0.1 1 328 . 62 ASP HA H 4.09 0.02 1 329 . 62 ASP CB C 39.1 0.1 1 330 . 62 ASP C C 179.6 0.1 1 331 . 63 GLU N N 123.2 0.1 1 332 . 63 GLU H H 8.19 0.02 1 333 . 63 GLU CA C 60.3 0.1 1 334 . 63 GLU CB C 28.2 0.1 1 335 . 63 GLU C C 177.3 0.1 1 336 . 64 ALA N N 122.0 0.1 1 337 . 64 ALA H H 8.10 0.02 1 338 . 64 ALA CA C 55.3 0.1 1 339 . 64 ALA HA H 3.90 0.02 1 340 . 64 ALA CB C 17.4 0.1 1 341 . 64 ALA C C 180.0 0.1 1 342 . 65 ALA N N 119.6 0.1 1 343 . 65 ALA H H 7.79 0.02 1 344 . 65 ALA CA C 54.9 0.1 1 345 . 65 ALA HA H 4.18 0.02 1 346 . 65 ALA CB C 17.9 0.1 1 347 . 65 ALA C C 181.8 0.1 1 348 . 66 ARG N N 120.5 0.1 1 349 . 66 ARG H H 7.67 0.02 1 350 . 66 ARG CA C 59.7 0.1 1 351 . 66 ARG HA H 3.81 0.02 1 352 . 66 ARG CB C 28.1 0.1 1 353 . 66 ARG C C 178.7 0.1 1 354 . 67 LEU N N 120.8 0.1 1 355 . 67 LEU H H 8.94 0.02 1 356 . 67 LEU CA C 57.3 0.1 1 357 . 67 LEU CB C 41.7 0.1 1 358 . 68 SER CA C 65.4 0.1 1 359 . 68 SER CB C 66.0 0.1 1 360 . 68 SER C C 176.6 0.1 1 361 . 69 TRP N N 121.0 0.1 1 362 . 69 TRP H H 7.74 0.02 1 363 . 69 TRP CA C 62.2 0.1 1 364 . 69 TRP HA H 4.24 0.02 1 365 . 69 TRP CB C 28.5 0.1 1 366 . 69 TRP C C 179.3 0.1 1 367 . 70 LEU N N 124.7 0.1 1 368 . 70 LEU H H 9.37 0.02 1 369 . 70 LEU CA C 57.2 0.1 1 370 . 70 LEU CB C 40.7 0.1 1 371 . 70 LEU C C 179.8 0.1 1 372 . 71 ALA N N 120.6 0.1 1 373 . 71 ALA H H 7.81 0.02 1 374 . 71 ALA CA C 54.5 0.1 1 375 . 71 ALA HA H 4.10 0.02 1 376 . 71 ALA CB C 17.6 0.1 1 377 . 71 ALA C C 180.7 0.1 1 378 . 72 THR N N 109.3 0.1 1 379 . 72 THR H H 7.47 0.02 1 380 . 72 THR CA C 63.6 0.1 1 381 . 72 THR HA H 4.16 0.02 1 382 . 72 THR CB C 69.4 0.1 1 383 . 72 THR C C 176.0 0.1 1 384 . 73 THR N N 112.3 0.1 1 385 . 73 THR H H 7.27 0.02 1 386 . 73 THR CA C 62.7 0.1 1 387 . 73 THR HA H 4.09 0.02 1 388 . 73 THR CB C 71.2 0.1 1 389 . 73 THR C C 176.5 0.1 1 390 . 74 GLY N N 109.7 0.1 1 391 . 74 GLY H H 7.30 0.02 1 392 . 74 GLY CA C 44.9 0.1 1 393 . 74 GLY HA2 H 4.19 0.02 2 394 . 74 GLY HA3 H 3.56 0.02 2 395 . 74 GLY C C 174.2 0.1 1 396 . 75 VAL N N 125.3 0.1 1 397 . 75 VAL H H 7.57 0.02 1 398 . 75 VAL CA C 60.2 0.1 1 399 . 75 VAL HA H 4.15 0.02 1 400 . 75 VAL CB C 31.8 0.1 1 401 . 76 PRO CA C 62.9 0.1 1 402 . 76 PRO CB C 31.0 0.1 1 403 . 76 PRO C C 175.6 0.1 1 404 . 77 CYS N N 113.4 0.1 1 405 . 77 CYS H H 7.59 0.02 1 406 . 77 CYS CA C 55.6 0.1 1 407 . 77 CYS HA H 4.80 0.02 1 408 . 77 CYS CB C 29.3 0.1 1 409 . 77 CYS C C 172.9 0.1 1 410 . 78 ALA N N 125.6 0.1 1 411 . 78 ALA H H 8.88 0.02 1 412 . 78 ALA CA C 52.9 0.1 1 413 . 78 ALA HA H 3.70 0.02 1 414 . 78 ALA CB C 19.4 0.1 1 415 . 78 ALA C C 177.4 0.1 1 416 . 79 ALA N N 123.2 0.1 1 417 . 79 ALA H H 8.05 0.02 1 418 . 79 ALA CA C 51.3 0.1 1 419 . 79 ALA HA H 4.07 0.02 1 420 . 79 ALA CB C 18.8 0.1 1 421 . 79 ALA C C 178.4 0.1 1 422 . 80 VAL N N 121.9 0.1 1 423 . 80 VAL H H 8.24 0.02 1 424 . 80 VAL CA C 62.1 0.1 1 425 . 80 VAL CB C 30.9 0.1 1 426 . 80 VAL C C 176.5 0.1 1 427 . 81 LEU N N 130.6 0.1 1 428 . 81 LEU H H 8.96 0.02 1 429 . 81 LEU CA C 56.2 0.1 1 430 . 81 LEU HA H 4.29 0.02 1 431 . 81 LEU CB C 40.1 0.1 1 432 . 81 LEU C C 177.9 0.1 1 433 . 82 ASP N N 115.3 0.1 1 434 . 82 ASP H H 7.72 0.02 1 435 . 82 ASP CA C 54.6 0.1 1 436 . 82 ASP HA H 4.87 0.02 1 437 . 82 ASP CB C 43.2 0.1 1 438 . 82 ASP C C 173.9 0.1 1 439 . 83 VAL N N 121.8 0.1 1 440 . 83 VAL H H 7.96 0.02 1 441 . 83 VAL CA C 61.2 0.1 1 442 . 83 VAL HA H 5.26 0.02 1 443 . 83 VAL CB C 34.0 0.1 1 444 . 83 VAL C C 174.8 0.1 1 445 . 84 VAL N N 126.3 0.1 1 446 . 84 VAL H H 9.19 0.02 1 447 . 84 VAL CA C 60.4 0.1 1 448 . 84 VAL HA H 4.54 0.02 1 449 . 84 VAL CB C 36.4 0.1 1 450 . 84 VAL C C 174.2 0.1 1 451 . 85 THR N N 123.3 0.1 1 452 . 85 THR H H 8.43 0.02 1 453 . 85 THR CA C 61.5 0.1 1 454 . 85 THR HA H 5.41 0.02 1 455 . 85 THR CB C 70.7 0.1 1 456 . 85 THR C C 174.6 0.1 1 457 . 86 GLU N N 127.2 0.1 1 458 . 86 GLU H H 9.27 0.02 1 459 . 86 GLU CA C 56.2 0.1 1 460 . 86 GLU HA H 4.45 0.02 1 461 . 86 GLU CB C 33.0 0.1 1 462 . 86 GLU C C 176.0 0.1 1 463 . 87 ALA N N 131.2 0.1 1 464 . 87 ALA H H 9.35 0.02 1 465 . 87 ALA CA C 52.8 0.1 1 466 . 87 ALA CB C 16.7 0.1 1 467 . 87 ALA C C 177.3 0.1 1 468 . 88 GLY N N 104.5 0.1 1 469 . 88 GLY H H 8.57 0.02 1 470 . 88 GLY CA C 45.4 0.1 1 471 . 88 GLY HA2 H 3.55 0.02 2 472 . 88 GLY HA3 H 4.03 0.02 2 473 . 88 GLY C C 174.0 0.1 1 474 . 89 ARG N N 122.3 0.1 1 475 . 89 ARG H H 7.84 0.02 1 476 . 89 ARG CA C 55.2 0.1 1 477 . 89 ARG HA H 4.58 0.02 1 478 . 89 ARG CB C 33.4 0.1 1 479 . 89 ARG C C 173.7 0.1 1 480 . 90 ASP N N 122.3 0.1 1 481 . 90 ASP H H 8.34 0.02 1 482 . 90 ASP CA C 53.1 0.1 1 483 . 90 ASP CB C 43.4 0.1 1 484 . 90 ASP C C 175.9 0.1 1 485 . 91 TRP N N 122.9 0.1 1 486 . 91 TRP H H 9.35 0.02 1 487 . 91 TRP CA C 56.2 0.1 1 488 . 91 TRP HA H 5.18 0.02 1 489 . 91 TRP CB C 31.9 0.1 1 490 . 91 TRP C C 174.1 0.1 1 491 . 92 LEU N N 125.9 0.1 1 492 . 92 LEU H H 9.65 0.02 1 493 . 92 LEU CA C 53.9 0.1 1 494 . 92 LEU HA H 5.25 0.02 1 495 . 92 LEU CB C 45.9 0.1 1 496 . 92 LEU C C 173.4 0.1 1 497 . 93 LEU N N 129.8 0.1 1 498 . 93 LEU H H 8.78 0.02 1 499 . 93 LEU CA C 53.8 0.1 1 500 . 93 LEU HA H 5.00 0.02 1 501 . 93 LEU CB C 42.5 0.1 1 502 . 93 LEU C C 174.6 0.1 1 503 . 94 LEU N N 128.0 0.1 1 504 . 94 LEU H H 9.47 0.02 1 505 . 94 LEU CA C 52.8 0.1 1 506 . 94 LEU HA H 5.34 0.02 1 507 . 94 LEU CB C 45.9 0.1 1 508 . 94 LEU C C 177.1 0.1 1 509 . 95 GLY N N 105.3 0.1 1 510 . 95 GLY H H 8.67 0.02 1 511 . 95 GLY CA C 43.4 0.1 1 512 . 95 GLY HA2 H 3.68 0.02 2 513 . 95 GLY HA3 H 4.38 0.02 2 514 . 95 GLY C C 172.4 0.1 1 515 . 96 GLU N N 117.4 0.1 1 516 . 96 GLU H H 7.92 0.02 1 517 . 96 GLU CA C 55.7 0.1 1 518 . 96 GLU HA H 4.18 0.02 1 519 . 96 GLU CB C 31.1 0.1 1 520 . 96 GLU C C 177.2 0.1 1 521 . 97 VAL N N 129.2 0.1 1 522 . 97 VAL H H 8.08 0.02 1 523 . 97 VAL CA C 59.2 0.1 1 524 . 97 VAL HA H 4.24 0.02 1 525 . 97 VAL CB C 32.2 0.1 1 526 . 98 PRO CA C 63.1 0.1 1 527 . 98 PRO CB C 32.5 0.1 1 528 . 98 PRO C C 175.8 0.1 1 529 . 99 GLY N N 106.4 0.1 1 530 . 99 GLY H H 8.00 0.02 1 531 . 99 GLY CA C 43.6 0.1 1 532 . 99 GLY HA2 H 3.45 0.02 2 533 . 99 GLY HA3 H 4.37 0.02 2 534 . 99 GLY C C 173.8 0.1 1 535 . 100 GLN N N 121.7 0.1 1 536 . 100 GLN H H 8.72 0.02 1 537 . 100 GLN CA C 53.3 0.1 1 538 . 100 GLN HA H 4.57 0.02 1 539 . 100 GLN CB C 32.2 0.1 1 540 . 100 GLN C C 174.0 0.1 1 541 . 101 ASP N N 122.9 0.1 1 542 . 101 ASP H H 8.08 0.02 1 543 . 101 ASP CA C 54.7 0.1 1 544 . 101 ASP HA H 5.07 0.02 1 545 . 101 ASP CB C 42.2 0.1 1 546 . 101 ASP C C 177.5 0.1 1 547 . 102 LEU N N 121.0 0.1 1 548 . 102 LEU H H 8.76 0.02 1 549 . 102 LEU CA C 56.4 0.1 1 550 . 102 LEU CB C 42.1 0.1 1 551 . 102 LEU C C 179.0 0.1 1 552 . 103 LEU N N 120.7 0.1 1 553 . 103 LEU H H 7.45 0.02 1 554 . 103 LEU CA C 58.0 0.1 1 555 . 103 LEU HA H 3.79 0.02 1 556 . 103 LEU CB C 40.1 0.1 1 557 . 103 LEU C C 178.1 0.1 1 558 . 104 SER N N 116.1 0.1 1 559 . 104 SER H H 8.63 0.02 1 560 . 104 SER CA C 60.2 0.1 1 561 . 104 SER HA H 3.95 0.02 1 562 . 104 SER CB C 62.5 0.1 1 563 . 104 SER C C 175.9 0.1 1 564 . 105 SER N N 115.8 0.1 1 565 . 105 SER H H 7.20 0.02 1 566 . 105 SER CA C 59.3 0.1 1 567 . 105 SER HA H 3.81 0.02 1 568 . 105 SER CB C 63.6 0.1 1 569 . 106 HIS CA C 54.7 0.1 1 570 . 106 HIS CB C 27.7 0.1 1 571 . 106 HIS C C 174.5 0.1 1 572 . 107 LEU N N 122.5 0.1 1 573 . 107 LEU H H 7.03 0.02 1 574 . 107 LEU CA C 53.9 0.1 1 575 . 107 LEU HA H 4.17 0.02 1 576 . 107 LEU CB C 44.0 0.1 1 577 . 107 LEU C C 177.3 0.1 1 578 . 108 ALA N N 124.7 0.1 1 579 . 108 ALA H H 8.59 0.02 1 580 . 108 ALA CA C 50.5 0.1 1 581 . 108 ALA HA H 4.31 0.02 1 582 . 108 ALA CB C 16.7 0.1 1 583 . 109 PRO CA C 65.9 0.1 1 584 . 109 PRO CB C 29.3 0.1 1 585 . 109 PRO C C 177.2 0.1 1 586 . 110 ALA N N 115.9 0.1 1 587 . 110 ALA H H 7.71 0.02 1 588 . 110 ALA CA C 55.1 0.1 1 589 . 110 ALA HA H 3.64 0.02 1 590 . 110 ALA CB C 18.2 0.1 1 591 . 110 ALA C C 181.1 0.1 1 592 . 111 GLU N N 116.8 0.1 1 593 . 111 GLU H H 6.83 0.02 1 594 . 111 GLU CA C 58.1 0.1 1 595 . 111 GLU HA H 4.03 0.02 1 596 . 111 GLU CB C 29.5 0.1 1 597 . 111 GLU C C 179.2 0.1 1 598 . 112 LYS N N 118.1 0.1 1 599 . 112 LYS H H 7.82 0.02 1 600 . 112 LYS CA C 61.2 0.1 1 601 . 112 LYS HA H 3.72 0.02 1 602 . 112 LYS CB C 32.0 0.1 1 603 . 112 LYS C C 179.1 0.1 1 604 . 113 VAL N N 111.9 0.1 1 605 . 113 VAL H H 8.04 0.02 1 606 . 113 VAL CA C 66.2 0.1 1 607 . 113 VAL HA H 3.71 0.02 1 608 . 113 VAL CB C 31.0 0.1 1 609 . 113 VAL C C 177.6 0.1 1 610 . 114 SER N N 117.0 0.1 1 611 . 114 SER H H 7.24 0.02 1 612 . 114 SER CA C 61.4 0.1 1 613 . 114 SER HA H 4.16 0.02 1 614 . 114 SER CB C 62.1 0.1 1 615 . 114 SER C C 177.5 0.1 1 616 . 115 ILE N N 122.9 0.1 1 617 . 115 ILE H H 8.02 0.02 1 618 . 115 ILE CA C 64.4 0.1 1 619 . 115 ILE HA H 3.78 0.02 1 620 . 115 ILE CB C 36.8 0.1 1 621 . 115 ILE C C 178.4 0.1 1 622 . 116 MET N N 119.1 0.1 1 623 . 116 MET H H 8.04 0.02 1 624 . 116 MET CA C 58.7 0.1 1 625 . 116 MET HA H 4.46 0.02 1 626 . 116 MET CB C 31.3 0.1 1 627 . 116 MET C C 178.3 0.1 1 628 . 117 ALA N N 121.1 0.1 1 629 . 117 ALA H H 8.41 0.02 1 630 . 117 ALA CA C 56.3 0.1 1 631 . 117 ALA HA H 3.92 0.02 1 632 . 117 ALA CB C 17.1 0.1 1 633 . 117 ALA C C 178.6 0.1 1 634 . 118 ASP N N 119.3 0.1 1 635 . 118 ASP H H 7.89 0.02 1 636 . 118 ASP CA C 57.2 0.1 1 637 . 118 ASP HA H 4.15 0.02 1 638 . 118 ASP CB C 41.0 0.1 1 639 . 118 ASP C C 178.3 0.1 1 640 . 119 ALA N N 121.7 0.1 1 641 . 119 ALA H H 8.30 0.02 1 642 . 119 ALA CA C 54.9 0.1 1 643 . 119 ALA CB C 17.7 0.1 1 644 . 119 ALA C C 179.7 0.1 1 645 . 120 MET N N 114.1 0.1 1 646 . 120 MET H H 7.91 0.02 1 647 . 120 MET CA C 57.1 0.1 1 648 . 120 MET HA H 4.00 0.02 1 649 . 120 MET CB C 34.0 0.1 1 650 . 120 MET C C 177.8 0.1 1 651 . 121 ARG N N 119.2 0.1 1 652 . 121 ARG H H 8.33 0.02 1 653 . 121 ARG CA C 59.7 0.1 1 654 . 121 ARG HA H 3.75 0.02 1 655 . 121 ARG CB C 29.2 0.1 1 656 . 121 ARG C C 179.4 0.1 1 657 . 122 ARG N N 119.2 0.1 1 658 . 122 ARG H H 8.00 0.02 1 659 . 122 ARG CA C 58.7 0.1 1 660 . 122 ARG HA H 3.86 0.02 1 661 . 122 ARG CB C 29.0 0.1 1 662 . 122 ARG C C 179.3 0.1 1 663 . 123 LEU N N 119.5 0.1 1 664 . 123 LEU H H 7.41 0.02 1 665 . 123 LEU CA C 57.4 0.1 1 666 . 123 LEU HA H 4.18 0.02 1 667 . 123 LEU CB C 41.5 0.1 1 668 . 123 LEU C C 179.0 0.1 1 669 . 124 HIS N N 115.3 0.1 1 670 . 124 HIS H H 8.72 0.02 1 671 . 124 HIS CA C 56.4 0.1 1 672 . 124 HIS HA H 4.93 0.02 1 673 . 124 HIS CB C 30.6 0.1 1 674 . 124 HIS C C 177.2 0.1 1 675 . 125 THR N N 112.5 0.1 1 676 . 125 THR H H 7.55 0.02 1 677 . 125 THR CA C 62.5 0.1 1 678 . 125 THR HA H 4.47 0.02 1 679 . 125 THR CB C 69.6 0.1 1 680 . 125 THR C C 175.8 0.1 1 681 . 126 LEU N N 122.9 0.1 1 682 . 126 LEU H H 7.26 0.02 1 683 . 126 LEU CA C 55.3 0.1 1 684 . 126 LEU HA H 4.27 0.02 1 685 . 126 LEU CB C 41.7 0.1 1 686 . 126 LEU C C 177.7 0.1 1 687 . 127 ASP N N 123.8 0.1 1 688 . 127 ASP H H 8.88 0.02 1 689 . 127 ASP CA C 51.6 0.1 1 690 . 127 ASP HA H 4.81 0.02 1 691 . 127 ASP CB C 40.8 0.1 1 692 . 128 PRO C C 177.1 0.1 1 693 . 129 ALA N N 121.9 0.1 1 694 . 129 ALA H H 8.24 0.02 1 695 . 129 ALA CA C 54.0 0.1 1 696 . 129 ALA CB C 17.8 0.1 1 697 . 129 ALA C C 179.4 0.1 1 698 . 130 THR N N 106.0 0.1 1 699 . 130 THR H H 7.47 0.02 1 700 . 130 THR CA C 61.3 0.1 1 701 . 130 THR HA H 4.25 0.02 1 702 . 130 THR CB C 70.0 0.1 1 703 . 130 THR C C 173.9 0.1 1 704 . 131 CYS N N 124.1 0.1 1 705 . 131 CYS H H 7.18 0.02 1 706 . 131 CYS CA C 54.5 0.1 1 707 . 131 CYS HA H 3.81 0.02 1 708 . 131 CYS CB C 29.4 0.1 1 709 . 132 PRO CA C 63.0 0.1 1 710 . 132 PRO CB C 30.7 0.1 1 711 . 132 PRO C C 174.8 0.1 1 712 . 133 PHE N N 120.6 0.1 1 713 . 133 PHE H H 6.17 0.02 1 714 . 133 PHE CA C 56.0 0.1 1 715 . 133 PHE HA H 4.46 0.02 1 716 . 133 PHE CB C 38.8 0.1 1 717 . 133 PHE C C 173.2 0.1 1 718 . 134 ASP N N 126.4 0.1 1 719 . 134 ASP H H 8.70 0.02 1 720 . 134 ASP CA C 54.3 0.1 1 721 . 134 ASP HA H 4.50 0.02 1 722 . 134 ASP CB C 40.5 0.1 1 723 . 134 ASP C C 176.4 0.1 1 724 . 135 HIS N N 122.5 0.1 1 725 . 135 HIS H H 7.94 0.02 1 726 . 135 HIS CA C 55.1 0.1 1 727 . 135 HIS HA H 4.21 0.02 1 728 . 135 HIS CB C 41.6 0.1 1 729 . 135 HIS C C 173.5 0.1 1 730 . 136 GLN N N 115.0 0.1 1 731 . 136 GLN H H 8.00 0.02 1 732 . 136 GLN CA C 57.3 0.1 1 733 . 136 GLN CB C 29.9 0.1 1 734 . 136 GLN C C 177.3 0.1 1 735 . 137 ALA N N 127.9 0.1 1 736 . 137 ALA H H 10.24 0.02 1 737 . 137 ALA CA C 56.5 0.1 1 738 . 137 ALA CB C 16.8 0.1 1 739 . 137 ALA C C 179.9 0.1 1 740 . 138 LYS N N 115.9 0.1 1 741 . 138 LYS H H 9.19 0.02 1 742 . 138 LYS CA C 59.5 0.1 1 743 . 138 LYS CB C 30.8 0.1 1 744 . 138 LYS C C 178.9 0.1 1 745 . 139 HIS N N 118.1 0.1 1 746 . 139 HIS H H 7.14 0.02 1 747 . 139 HIS CA C 56.6 0.1 1 748 . 139 HIS HA H 4.75 0.02 1 749 . 139 HIS CB C 29.8 0.1 1 750 . 139 HIS C C 179.6 0.1 1 751 . 140 ARG N N 121.5 0.1 1 752 . 140 ARG H H 7.87 0.02 1 753 . 140 ARG CA C 56.8 0.1 1 754 . 140 ARG CB C 27.5 0.1 1 755 . 140 ARG C C 179.4 0.1 1 756 . 141 ILE N N 119.6 0.1 1 757 . 141 ILE H H 8.78 0.02 1 758 . 141 ILE CA C 65.4 0.1 1 759 . 141 ILE CB C 37.2 0.1 1 760 . 141 ILE C C 177.6 0.1 1 761 . 142 GLU N N 119.5 0.1 1 762 . 142 GLU H H 6.91 0.02 1 763 . 142 GLU CA C 58.6 0.1 1 764 . 142 GLU HA H 4.07 0.02 1 765 . 142 GLU CB C 28.4 0.1 1 766 . 142 GLU C C 179.2 0.1 1 767 . 143 ARG N N 121.3 0.1 1 768 . 143 ARG H H 7.74 0.02 1 769 . 143 ARG CA C 57.7 0.1 1 770 . 143 ARG HA H 4.11 0.02 1 771 . 143 ARG CB C 28.2 0.1 1 772 . 143 ARG C C 178.3 0.1 1 773 . 144 ALA N N 124.4 0.1 1 774 . 144 ALA H H 8.34 0.02 1 775 . 144 ALA CA C 55.2 0.1 1 776 . 144 ALA HA H 3.35 0.02 1 777 . 144 ALA CB C 16.8 0.1 1 778 . 144 ALA C C 178.7 0.1 1 779 . 145 ARG N N 119.2 0.1 1 780 . 145 ARG H H 7.67 0.02 1 781 . 145 ARG CA C 59.4 0.1 1 782 . 145 ARG HA H 3.26 0.02 1 783 . 145 ARG CB C 28.3 0.1 1 784 . 145 ARG C C 178.7 0.1 1 785 . 146 THR N N 116.7 0.1 1 786 . 146 THR H H 8.02 0.02 1 787 . 146 THR CA C 66.2 0.1 1 788 . 146 THR HA H 3.76 0.02 1 789 . 146 THR CB C 68.2 0.1 1 790 . 146 THR C C 177.7 0.1 1 791 . 147 ARG N N 122.3 0.1 1 792 . 147 ARG H H 8.17 0.02 1 793 . 147 ARG CA C 60.3 0.1 1 794 . 149 GLU C C 177.7 0.1 1 795 . 150 ALA N N 119.8 0.1 1 796 . 150 ALA H H 7.49 0.02 1 797 . 150 ALA CA C 52.0 0.1 1 798 . 150 ALA CB C 18.5 0.1 1 799 . 150 ALA C C 177.8 0.1 1 800 . 151 GLY N N 106.6 0.1 1 801 . 151 GLY H H 7.57 0.02 1 802 . 151 GLY CA C 45.8 0.1 1 803 . 151 GLY HA2 H 3.94 0.02 2 804 . 151 GLY HA3 H 4.05 0.02 2 805 . 151 GLY C C 176.0 0.1 1 806 . 152 LEU N N 117.6 0.1 1 807 . 152 LEU H H 7.59 0.02 1 808 . 152 LEU CA C 54.9 0.1 1 809 . 152 LEU HA H 4.18 0.02 1 810 . 152 LEU CB C 41.5 0.1 1 811 . 152 LEU C C 176.4 0.1 1 812 . 153 VAL N N 120.4 0.1 1 813 . 153 VAL H H 7.69 0.02 1 814 . 153 VAL CA C 61.0 0.1 1 815 . 153 VAL HA H 3.97 0.02 1 816 . 153 VAL CB C 32.7 0.1 1 817 . 153 VAL C C 174.9 0.1 1 818 . 154 ASP N N 130.8 0.1 1 819 . 154 ASP H H 8.88 0.02 1 820 . 154 ASP CA C 53.1 0.1 1 821 . 154 ASP HA H 4.53 0.02 1 822 . 154 ASP CB C 41.7 0.1 1 823 . 154 ASP C C 175.5 0.1 1 824 . 155 GLN N N 124.8 0.1 1 825 . 155 GLN H H 8.60 0.02 1 826 . 155 GLN CA C 58.4 0.1 1 827 . 155 GLN HA H 3.71 0.02 1 828 . 155 GLN CB C 28.7 0.1 1 829 . 155 GLN C C 178.9 0.1 1 830 . 156 ASP N N 116.6 0.1 1 831 . 156 ASP H H 8.35 0.02 1 832 . 156 ASP CA C 55.9 0.1 1 833 . 156 ASP HA H 3.28 0.02 1 834 . 156 ASP CB C 40.0 0.1 1 835 . 156 ASP C C 177.0 0.1 1 836 . 157 ASP N N 118.5 0.1 1 837 . 157 ASP H H 7.63 0.02 1 838 . 157 ASP CA C 54.7 0.1 1 839 . 157 ASP HA H 4.47 0.02 1 840 . 157 ASP CB C 40.8 0.1 1 841 . 157 ASP C C 176.5 0.1 1 842 . 158 LEU N N 120.0 0.1 1 843 . 158 LEU H H 7.04 0.02 1 844 . 158 LEU CA C 53.3 0.1 1 845 . 158 LEU HA H 4.38 0.02 1 846 . 158 LEU CB C 42.5 0.1 1 847 . 158 LEU C C 177.5 0.1 1 848 . 159 ASP N N 120.3 0.1 1 849 . 159 ASP H H 8.06 0.02 1 850 . 159 ASP CA C 54.0 0.1 1 851 . 159 ASP CB C 41.3 0.1 1 852 . 159 ASP C C 177.1 0.1 1 853 . 160 GLU N N 121.3 0.1 1 854 . 160 GLU H H 8.53 0.02 1 855 . 160 GLU CA C 59.6 0.1 1 856 . 160 GLU HA H 3.69 0.02 1 857 . 160 GLU CB C 29.1 0.1 1 858 . 160 GLU C C 178.5 0.1 1 859 . 161 GLU N N 117.7 0.1 1 860 . 161 GLU H H 8.33 0.02 1 861 . 161 GLU CA C 57.8 0.1 1 862 . 161 GLU HA H 3.95 0.02 1 863 . 161 GLU CB C 28.6 0.1 1 864 . 161 GLU C C 177.0 0.1 1 865 . 162 HIS N N 117.1 0.1 1 866 . 162 HIS H H 7.72 0.02 1 867 . 162 HIS CA C 56.0 0.1 1 868 . 162 HIS HA H 4.56 0.02 1 869 . 162 HIS CB C 30.1 0.1 1 870 . 162 HIS C C 174.8 0.1 1 871 . 163 GLN N N 119.6 0.1 1 872 . 163 GLN H H 7.28 0.02 1 873 . 163 GLN CA C 56.9 0.1 1 874 . 163 GLN HA H 3.98 0.02 1 875 . 163 GLN CB C 28.4 0.1 1 876 . 163 GLN C C 177.3 0.1 1 877 . 164 GLY N N 110.1 0.1 1 878 . 164 GLY H H 8.78 0.02 1 879 . 164 GLY CA C 45.4 0.1 1 880 . 164 GLY HA2 H 3.64 0.02 2 881 . 164 GLY HA3 H 3.89 0.02 2 882 . 164 GLY C C 174.5 0.1 1 883 . 165 LEU N N 120.6 0.1 1 884 . 165 LEU H H 7.37 0.02 1 885 . 165 LEU CA C 53.6 0.1 1 886 . 165 LEU HA H 4.40 0.02 1 887 . 165 LEU CB C 42.9 0.1 1 888 . 165 LEU C C 177.0 0.1 1 889 . 166 ALA N N 126.6 0.1 1 890 . 166 ALA H H 8.74 0.02 1 891 . 166 ALA CA C 50.4 0.1 1 892 . 166 ALA HA H 4.51 0.02 1 893 . 166 ALA CB C 16.7 0.1 1 894 . 167 PRO CA C 66.3 0.1 1 895 . 167 PRO CB C 31.5 0.1 1 896 . 167 PRO C C 178.1 0.1 1 897 . 168 ALA N N 117.4 0.1 1 898 . 168 ALA H H 8.64 0.02 1 899 . 168 ALA CA C 55.4 0.1 1 900 . 168 ALA HA H 4.03 0.02 1 901 . 168 ALA CB C 17.7 0.1 1 902 . 168 ALA C C 181.3 0.1 1 903 . 169 GLU N N 118.9 0.1 1 904 . 169 GLU H H 7.20 0.02 1 905 . 169 GLU CA C 58.1 0.1 1 906 . 169 GLU HA H 4.16 0.02 1 907 . 169 GLU CB C 29.3 0.1 1 908 . 169 GLU C C 179.0 0.1 1 909 . 170 LEU N N 122.3 0.1 1 910 . 170 LEU H H 8.21 0.02 1 911 . 170 LEU CA C 58.0 0.1 1 912 . 170 LEU CB C 41.0 0.1 1 913 . 170 LEU C C 178.8 0.1 1 914 . 171 PHE N N 117.2 0.1 1 915 . 171 PHE H H 8.51 0.02 1 916 . 171 PHE CA C 62.2 0.1 1 917 . 171 PHE HA H 3.83 0.02 1 918 . 171 PHE CB C 38.0 0.1 1 919 . 171 PHE C C 177.4 0.1 1 920 . 172 ALA N N 122.5 0.1 1 921 . 172 ALA H H 7.49 0.02 1 922 . 172 ALA CA C 55.1 0.1 1 923 . 172 ALA HA H 3.95 0.02 1 924 . 172 ALA CB C 17.2 0.1 1 925 . 172 ALA C C 181.3 0.1 1 926 . 173 ARG N N 119.7 0.1 1 927 . 173 ARG H H 7.76 0.02 1 928 . 173 ARG CA C 58.9 0.1 1 929 . 173 ARG CB C 29.1 0.1 1 930 . 173 ARG C C 179.1 0.1 1 931 . 174 LEU N N 120.4 0.1 1 932 . 174 LEU H H 7.80 0.02 1 933 . 174 LEU CA C 58.1 0.1 1 934 . 174 LEU HA H 3.82 0.02 1 935 . 174 LEU CB C 41.5 0.1 1 936 . 174 LEU C C 178.9 0.1 1 937 . 175 LYS N N 117.0 0.1 1 938 . 175 LYS H H 7.84 0.02 1 939 . 175 LYS CA C 59.3 0.1 1 940 . 175 LYS HA H 3.67 0.02 1 941 . 175 LYS CB C 31.4 0.1 1 942 . 175 LYS C C 179.3 0.1 1 943 . 176 ALA N N 120.0 0.1 1 944 . 176 ALA H H 7.45 0.02 1 945 . 176 ALA CA C 53.7 0.1 1 946 . 176 ALA HA H 4.03 0.02 1 947 . 176 ALA CB C 17.8 0.1 1 948 . 176 ALA C C 179.0 0.1 1 949 . 177 ARG N N 116.2 0.1 1 950 . 177 ARG H H 7.22 0.02 1 951 . 177 ARG CA C 54.8 0.1 1 952 . 177 ARG HA H 5.33 0.02 1 953 . 177 ARG CB C 30.6 0.1 1 954 . 177 ARG C C 174.8 0.1 1 955 . 178 MET N N 121.4 0.1 1 956 . 178 MET H H 6.83 0.02 1 957 . 178 MET CA C 53.8 0.1 1 958 . 178 MET HA H 2.83 0.02 1 959 . 178 MET CB C 32.5 0.1 1 960 . 179 PRO CA C 62.3 0.1 1 961 . 179 PRO CB C 31.6 0.1 1 962 . 179 PRO C C 175.9 0.1 1 963 . 180 ASP N N 122.0 0.1 1 964 . 180 ASP H H 8.31 0.02 1 965 . 180 ASP CA C 53.9 0.1 1 966 . 180 ASP CB C 40.2 0.1 1 967 . 180 ASP C C 176.3 0.1 1 968 . 181 GLY N N 111.6 0.1 1 969 . 181 GLY H H 7.70 0.02 1 970 . 181 GLY CA C 44.8 0.1 1 971 . 181 GLY HA2 H 3.90 0.02 1 972 . 181 GLY HA3 H 3.90 0.02 1 973 . 181 GLY C C 173.5 0.1 1 974 . 182 GLU N N 121.8 0.1 1 975 . 182 GLU H H 8.26 0.02 1 976 . 182 GLU CA C 55.7 0.1 1 977 . 182 GLU CB C 33.6 0.1 1 978 . 182 GLU C C 174.9 0.1 1 979 . 183 ASP N N 128.0 0.1 1 980 . 183 ASP H H 9.65 0.02 1 981 . 183 ASP CA C 51.9 0.1 1 982 . 183 ASP CB C 39.6 0.1 1 983 . 183 ASP C C 175.2 0.1 1 984 . 184 LEU N N 121.4 0.1 1 985 . 184 LEU H H 7.40 0.02 1 986 . 184 LEU CA C 55.7 0.1 1 987 . 184 LEU HA H 3.93 0.02 1 988 . 184 LEU CB C 40.6 0.1 1 989 . 184 LEU C C 177.1 0.1 1 990 . 185 VAL N N 117.6 0.1 1 991 . 185 VAL H H 8.74 0.02 1 992 . 185 VAL CA C 58.5 0.1 1 993 . 185 VAL HA H 4.51 0.02 1 994 . 185 VAL CB C 36.0 0.1 1 995 . 185 VAL C C 174.6 0.1 1 996 . 186 VAL N N 121.5 0.1 1 997 . 186 VAL H H 9.45 0.02 1 998 . 186 VAL CA C 65.2 0.1 1 999 . 186 VAL HA H 3.48 0.02 1 1000 . 186 VAL CB C 29.3 0.1 1 1001 . 186 VAL C C 173.5 0.1 1 1002 . 187 THR N N 114.5 0.1 1 1003 . 187 THR H H 8.08 0.02 1 1004 . 187 THR CA C 58.1 0.1 1 1005 . 187 THR HA H 4.88 0.02 1 1006 . 187 THR CB C 72.1 0.1 1 1007 . 187 THR C C 173.9 0.1 1 1008 . 188 HIS N N 126.2 0.1 1 1009 . 188 HIS H H 10.46 0.02 1 1010 . 188 HIS CA C 60.9 0.1 1 1011 . 188 HIS HA H 3.44 0.02 1 1012 . 188 HIS CB C 31.0 0.1 1 1013 . 188 HIS C C 176.9 0.1 1 1014 . 189 GLY N N 104.2 0.1 1 1015 . 189 GLY H H 8.61 0.02 1 1016 . 189 GLY CA C 46.1 0.1 1 1017 . 189 GLY HA2 H 3.94 0.02 1 1018 . 189 GLY HA3 H 3.94 0.02 1 1019 . 189 GLY C C 174.3 0.1 1 1020 . 190 ASP N N 127.6 0.1 1 1021 . 190 ASP H H 9.99 0.02 1 1022 . 190 ASP CA C 52.7 0.1 1 1023 . 190 ASP HA H 4.55 0.02 1 1024 . 190 ASP CB C 39.3 0.1 1 1025 . 190 ASP C C 175.8 0.1 1 1026 . 191 ALA N N 126.4 0.1 1 1027 . 191 ALA H H 8.37 0.02 1 1028 . 191 ALA CA C 52.9 0.1 1 1029 . 191 ALA HA H 3.63 0.02 1 1030 . 191 ALA CB C 17.0 0.1 1 1031 . 191 ALA C C 173.6 0.1 1 1032 . 192 CYS N N 115.6 0.1 1 1033 . 192 CYS H H 7.26 0.02 1 1034 . 192 CYS CA C 55.7 0.1 1 1035 . 192 CYS HA H 4.28 0.02 1 1036 . 192 CYS CB C 29.5 0.1 1 1037 . 192 CYS C C 174.2 0.1 1 1038 . 193 LEU N N 122.4 0.1 1 1039 . 193 LEU H H 9.49 0.02 1 1040 . 193 LEU CA C 60.1 0.1 1 1041 . 193 LEU CB C 39.3 0.1 1 1042 . 194 PRO CA C 64.8 0.1 1 1043 . 194 PRO CB C 30.6 0.1 1 1044 . 194 PRO C C 175.3 0.1 1 1045 . 195 ASN N N 112.3 0.1 1 1046 . 195 ASN H H 7.12 0.02 1 1047 . 195 ASN CA C 52.2 0.1 1 1048 . 195 ASN HA H 5.06 0.02 1 1049 . 195 ASN CB C 37.7 0.1 1 1050 . 195 ASN C C 173.5 0.1 1 1051 . 196 ILE N N 121.7 0.1 1 1052 . 196 ILE H H 7.28 0.02 1 1053 . 196 ILE CA C 59.3 0.1 1 1054 . 196 ILE HA H 4.30 0.02 1 1055 . 196 ILE CB C 38.0 0.1 1 1056 . 196 ILE C C 173.9 0.1 1 1057 . 197 MET N N 123.6 0.1 1 1058 . 197 MET H H 8.13 0.02 1 1059 . 197 MET CA C 52.2 0.1 1 1060 . 197 MET HA H 4.88 0.02 1 1061 . 197 MET CB C 31.3 0.1 1 1062 . 197 MET C C 176.4 0.1 1 1063 . 198 VAL N N 118.8 0.1 1 1064 . 198 VAL H H 8.82 0.02 1 1065 . 198 VAL CA C 58.7 0.1 1 1066 . 198 VAL HA H 4.70 0.02 1 1067 . 198 VAL CB C 35.0 0.1 1 1068 . 198 VAL C C 174.7 0.1 1 1069 . 199 GLU N N 125.3 0.1 1 1070 . 199 GLU H H 8.69 0.02 1 1071 . 199 GLU CA C 55.2 0.1 1 1072 . 199 GLU HA H 4.47 0.02 1 1073 . 199 GLU CB C 31.7 0.1 1 1074 . 199 GLU C C 176.3 0.1 1 1075 . 200 ASN N N 128.2 0.1 1 1076 . 200 ASN H H 9.42 0.02 1 1077 . 200 ASN CA C 54.1 0.1 1 1078 . 200 ASN HA H 5.34 0.02 1 1079 . 200 ASN CB C 36.9 0.1 1 1080 . 200 ASN C C 175.7 0.1 1 1081 . 201 GLY N N 103.0 0.1 1 1082 . 201 GLY H H 8.59 0.02 1 1083 . 201 GLY CA C 45.5 0.1 1 1084 . 201 GLY HA2 H 3.16 0.02 2 1085 . 201 GLY HA3 H 3.90 0.02 2 1086 . 201 GLY C C 172.8 0.1 1 1087 . 202 ARG N N 118.3 0.1 1 1088 . 202 ARG H H 7.41 0.02 1 1089 . 202 ARG CA C 53.5 0.1 1 1090 . 202 ARG HA H 4.57 0.02 1 1091 . 202 ARG CB C 33.1 0.1 1 1092 . 202 ARG C C 174.7 0.1 1 1093 . 203 PHE N N 123.3 0.1 1 1094 . 203 PHE H H 8.96 0.02 1 1095 . 203 PHE CA C 58.1 0.1 1 1096 . 203 PHE HA H 4.05 0.02 1 1097 . 203 PHE CB C 38.8 0.1 1 1098 . 203 PHE C C 175.5 0.1 1 1099 . 204 SER N N 123.7 0.1 1 1100 . 204 SER H H 8.98 0.02 1 1101 . 204 SER CA C 56.9 0.1 1 1102 . 204 SER HA H 4.05 0.02 1 1103 . 204 SER CB C 64.4 0.1 1 1104 . 205 GLY CA C 44.7 0.1 1 1105 . 205 GLY C C 171.1 0.1 1 1106 . 206 PHE N N 116.3 0.1 1 1107 . 206 PHE H H 7.28 0.02 1 1108 . 206 PHE CA C 57.1 0.1 1 1109 . 206 PHE HA H 4.19 0.02 1 1110 . 206 PHE CB C 44.0 0.1 1 1111 . 206 PHE C C 175.8 0.1 1 1112 . 207 ILE N N 113.2 0.1 1 1113 . 207 ILE H H 8.12 0.02 1 1114 . 207 ILE CA C 59.4 0.1 1 1115 . 207 ILE HA H 4.44 0.02 1 1116 . 207 ILE CB C 40.8 0.1 1 1117 . 207 ILE C C 174.8 0.1 1 1118 . 208 ASP N N 122.8 0.1 1 1119 . 208 ASP H H 8.53 0.02 1 1120 . 208 ASP CA C 54.9 0.1 1 1121 . 208 ASP CB C 36.9 0.1 1 1122 . 208 ASP C C 176.5 0.1 1 1123 . 209 CYS N N 115.4 0.1 1 1124 . 209 CYS H H 8.10 0.02 1 1125 . 209 CYS CA C 59.4 0.1 1 1126 . 209 CYS HA H 3.75 0.02 1 1127 . 209 CYS CB C 27.4 0.1 1 1128 . 209 CYS C C 175.4 0.1 1 1129 . 210 GLY N N 108.0 0.1 1 1130 . 210 GLY H H 8.65 0.02 1 1131 . 210 GLY CA C 46.5 0.1 1 1132 . 210 GLY HA2 H 3.14 0.02 2 1133 . 210 GLY HA3 H 3.65 0.02 2 1134 . 210 GLY C C 172.1 0.1 1 1135 . 211 ARG N N 117.1 0.1 1 1136 . 211 ARG H H 8.84 0.02 1 1137 . 211 ARG CA C 54.5 0.1 1 1138 . 211 ARG HA H 4.00 0.02 1 1139 . 211 ARG CB C 28.2 0.1 1 1140 . 211 ARG C C 173.8 0.1 1 1141 . 212 LEU N N 125.9 0.1 1 1142 . 212 LEU H H 6.55 0.02 1 1143 . 212 LEU CA C 55.3 0.1 1 1144 . 212 LEU CB C 42.3 0.1 1 1145 . 212 LEU C C 175.5 0.1 1 1146 . 213 GLY N N 109.0 0.1 1 1147 . 213 GLY H H 8.06 0.02 1 1148 . 213 GLY CA C 45.0 0.1 1 1149 . 213 GLY C C 172.3 0.1 1 1150 . 214 VAL N N 124.8 0.1 1 1151 . 214 VAL H H 8.94 0.02 1 1152 . 214 VAL CA C 63.4 0.1 1 1153 . 214 VAL HA H 4.54 0.02 1 1154 . 214 VAL CB C 30.9 0.1 1 1155 . 214 VAL C C 174.8 0.1 1 1156 . 215 ALA N N 129.6 0.1 1 1157 . 215 ALA H H 9.11 0.02 1 1158 . 215 ALA CA C 50.8 0.1 1 1159 . 215 ALA HA H 4.10 0.02 1 1160 . 215 ALA CB C 21.9 0.1 1 1161 . 215 ALA C C 175.6 0.1 1 1162 . 216 ASP N N 120.4 0.1 1 1163 . 216 ASP H H 8.76 0.02 1 1164 . 216 ASP CA C 54.5 0.1 1 1165 . 216 ASP CB C 44.7 0.1 1 1166 . 216 ASP C C 178.7 0.1 1 1167 . 217 ARG N N 124.3 0.1 1 1168 . 217 ARG H H 7.59 0.02 1 1169 . 217 ARG CA C 58.6 0.1 1 1170 . 217 ARG CB C 30.0 0.1 1 1171 . 217 ARG C C 179.1 0.1 1 1172 . 218 TYR N N 121.9 0.1 1 1173 . 218 TYR H H 10.87 0.02 1 1174 . 218 TYR CA C 62.5 0.1 1 1175 . 218 TYR CB C 37.3 0.1 1 1176 . 218 TYR C C 177.1 0.1 1 1177 . 219 GLN N N 123.2 0.1 1 1178 . 219 GLN H H 8.35 0.02 1 1179 . 219 GLN CA C 58.2 0.1 1 1180 . 219 GLN HA H 3.63 0.02 1 1181 . 219 GLN CB C 26.8 0.1 1 1182 . 219 GLN C C 178.4 0.1 1 1183 . 220 ASP N N 114.8 0.1 1 1184 . 220 ASP H H 6.75 0.02 1 1185 . 220 ASP CA C 54.7 0.1 1 1186 . 220 ASP HA H 5.09 0.02 1 1187 . 220 ASP CB C 40.9 0.1 1 1188 . 220 ASP C C 178.2 0.1 1 1189 . 221 ILE N N 118.4 0.1 1 1190 . 221 ILE H H 7.98 0.02 1 1191 . 221 ILE CA C 63.3 0.1 1 1192 . 221 ILE HA H 4.48 0.02 1 1193 . 221 ILE CB C 35.4 0.1 1 1194 . 221 ILE C C 179.2 0.1 1 1195 . 222 ALA N N 122.0 0.1 1 1196 . 222 ALA H H 9.68 0.02 1 1197 . 222 ALA CA C 55.5 0.1 1 1198 . 222 ALA HA H 3.93 0.02 1 1199 . 222 ALA CB C 21.1 0.1 1 1200 . 222 ALA C C 178.4 0.1 1 1201 . 223 LEU N N 119.6 0.1 1 1202 . 223 LEU H H 6.30 0.02 1 1203 . 223 LEU CA C 58.1 0.1 1 1204 . 223 LEU HA H 4.00 0.02 1 1205 . 223 LEU CB C 39.5 0.1 1 1206 . 223 LEU C C 177.8 0.1 1 1207 . 224 ALA N N 123.4 0.1 1 1208 . 224 ALA H H 8.37 0.02 1 1209 . 224 ALA CA C 55.3 0.1 1 1210 . 224 ALA HA H 3.97 0.02 1 1211 . 224 ALA CB C 17.9 0.1 1 1212 . 224 ALA C C 180.5 0.1 1 1213 . 225 THR N N 104.3 0.1 1 1214 . 225 THR H H 7.65 0.02 1 1215 . 225 THR CA C 65.1 0.1 1 1216 . 225 THR HA H 3.56 0.02 1 1217 . 225 THR CB C 68.6 0.1 1 1218 . 225 THR C C 176.7 0.1 1 1219 . 226 ARG N N 123.9 0.1 1 1220 . 226 ARG H H 6.63 0.02 1 1221 . 226 ARG CA C 59.4 0.1 1 1222 . 226 ARG HA H 3.85 0.02 1 1223 . 226 ARG CB C 29.9 0.1 1 1224 . 226 ARG C C 177.8 0.1 1 1225 . 227 ASP N N 120.2 0.1 1 1226 . 227 ASP H H 7.93 0.02 1 1227 . 227 ASP CA C 57.9 0.1 1 1228 . 227 ASP HA H 4.44 0.02 1 1229 . 227 ASP CB C 43.2 0.1 1 1230 . 227 ASP C C 177.7 0.1 1 1231 . 228 ILE N N 116.6 0.1 1 1232 . 228 ILE H H 8.37 0.02 1 1233 . 228 ILE CA C 65.8 0.1 1 1234 . 228 ILE HA H 4.28 0.02 1 1235 . 228 ILE CB C 38.3 0.1 1 1236 . 229 ALA N N 122.1 0.1 1 1237 . 229 ALA H H 8.24 0.02 1 1238 . 229 ALA CA C 54.9 0.1 1 1239 . 229 ALA CB C 17.2 0.1 1 1240 . 229 ALA C C 179.8 0.1 1 1241 . 230 GLU N N 116.4 0.1 1 1242 . 230 GLU H H 7.65 0.02 1 1243 . 230 GLU CA C 58.5 0.1 1 1244 . 230 GLU HA H 3.93 0.02 1 1245 . 230 GLU CB C 29.5 0.1 1 1246 . 230 GLU C C 178.4 0.1 1 1247 . 231 GLU N N 115.6 0.1 1 1248 . 231 GLU H H 8.06 0.02 1 1249 . 231 GLU CA C 57.2 0.1 1 1250 . 231 GLU HA H 4.34 0.02 1 1251 . 231 GLU CB C 29.5 0.1 1 1252 . 231 GLU C C 178.0 0.1 1 1253 . 232 LEU N N 116.4 0.1 1 1254 . 232 LEU H H 8.57 0.02 1 1255 . 232 LEU CA C 54.8 0.1 1 1256 . 232 LEU HA H 4.55 0.02 1 1257 . 232 LEU CB C 41.6 0.1 1 1258 . 232 LEU C C 177.5 0.1 1 1259 . 233 GLY N N 109.7 0.1 1 1260 . 233 GLY H H 7.65 0.02 1 1261 . 233 GLY CA C 44.6 0.1 1 1262 . 233 GLY HA2 H 3.95 0.02 2 1263 . 233 GLY HA3 H 4.82 0.02 2 1264 . 233 GLY C C 176.4 0.1 1 1265 . 234 GLY N N 112.5 0.1 1 1266 . 234 GLY H H 8.91 0.02 1 1267 . 234 GLY CA C 47.9 0.1 1 1268 . 234 GLY HA2 H 4.02 0.02 1 1269 . 234 GLY HA3 H 4.02 0.02 1 1270 . 234 GLY C C 176.5 0.1 1 1271 . 235 GLU N N 122.0 0.1 1 1272 . 235 GLU H H 9.43 0.02 1 1273 . 235 GLU CA C 58.1 0.1 1 1274 . 235 GLU HA H 4.12 0.02 1 1275 . 235 GLU CB C 27.5 0.1 1 1276 . 235 GLU C C 179.1 0.1 1 1277 . 236 TRP N N 122.0 0.1 1 1278 . 236 TRP H H 7.14 0.02 1 1279 . 236 TRP CA C 58.1 0.1 1 1280 . 236 TRP HA H 4.52 0.02 1 1281 . 236 TRP CB C 28.7 0.1 1 1282 . 236 TRP C C 178.3 0.1 1 1283 . 237 ALA N N 126.7 0.1 1 1284 . 237 ALA H H 7.63 0.02 1 1285 . 237 ALA CA C 55.4 0.1 1 1286 . 237 ALA HA H 4.00 0.02 1 1287 . 237 ALA CB C 17.6 0.1 1 1288 . 237 ALA C C 179.2 0.1 1 1289 . 238 ASP N N 118.8 0.1 1 1290 . 238 ASP H H 7.47 0.02 1 1291 . 238 ASP CA C 57.3 0.1 1 1292 . 238 ASP HA H 4.38 0.02 1 1293 . 238 ASP CB C 39.5 0.1 1 1294 . 238 ASP C C 179.3 0.1 1 1295 . 239 ARG N N 120.2 0.1 1 1296 . 239 ARG H H 7.53 0.02 1 1297 . 239 ARG CA C 57.9 0.1 1 1298 . 239 ARG HA H 4.01 0.02 1 1299 . 239 ARG CB C 28.7 0.1 1 1300 . 239 ARG C C 178.3 0.1 1 1301 . 240 PHE N N 119.8 0.1 1 1302 . 240 PHE H H 8.27 0.02 1 1303 . 240 PHE CA C 61.2 0.1 1 1304 . 240 PHE HA H 3.90 0.02 1 1305 . 240 PHE CB C 38.3 0.1 1 1306 . 243 LEU CA C 57.0 0.1 1 1307 . 243 LEU CB C 41.0 0.1 1 1308 . 243 LEU C C 179.6 0.1 1 1309 . 244 TYR N N 120.2 0.1 1 1310 . 244 TYR H H 8.43 0.02 1 1311 . 244 TYR CA C 61.0 0.1 1 1312 . 244 TYR HA H 3.56 0.02 1 1313 . 244 TYR CB C 38.1 0.1 1 1314 . 244 TYR C C 175.3 0.1 1 1315 . 245 GLY N N 104.7 0.1 1 1316 . 245 GLY H H 7.53 0.02 1 1317 . 245 GLY CA C 44.6 0.1 1 1318 . 245 GLY HA2 H 3.48 0.02 2 1319 . 245 GLY HA3 H 4.18 0.02 2 1320 . 245 GLY C C 174.6 0.1 1 1321 . 246 ILE N N 124.3 0.1 1 1322 . 246 ILE H H 8.02 0.02 1 1323 . 246 ILE CA C 60.3 0.1 1 1324 . 246 ILE HA H 4.12 0.02 1 1325 . 246 ILE CB C 39.3 0.1 1 1326 . 246 ILE C C 173.8 0.1 1 1327 . 247 ALA N N 129.6 0.1 1 1328 . 247 ALA H H 8.14 0.02 1 1329 . 247 ALA CA C 52.9 0.1 1 1330 . 247 ALA HA H 4.18 0.02 1 1331 . 247 ALA CB C 18.7 0.1 1 1332 . 247 ALA C C 177.8 0.1 1 1333 . 248 ALA N N 120.9 0.1 1 1334 . 248 ALA H H 7.63 0.02 1 1335 . 248 ALA CA C 48.9 0.1 1 1336 . 248 ALA HA H 4.79 0.02 1 1337 . 248 ALA CB C 18.2 0.1 1 1338 . 253 ARG CA C 60.0 0.1 1 1339 . 253 ARG CB C 30.1 0.1 1 1340 . 253 ARG C C 178.8 0.1 1 1341 . 254 ILE N N 119.8 0.1 1 1342 . 254 ILE H H 8.06 0.02 1 1343 . 254 ILE CA C 65.2 0.1 1 1344 . 254 ILE HA H 3.77 0.02 1 1345 . 254 ILE CB C 36.3 0.1 1 1346 . 254 ILE C C 177.4 0.1 1 1347 . 255 ALA N N 119.2 0.1 1 1348 . 255 ALA H H 7.63 0.02 1 1349 . 255 ALA CA C 54.7 0.1 1 1350 . 255 ALA HA H 4.01 0.02 1 1351 . 255 ALA CB C 17.6 0.1 1 1352 . 255 ALA C C 181.0 0.1 1 1353 . 256 PHE N N 118.9 0.1 1 1354 . 256 PHE H H 7.94 0.02 1 1355 . 256 PHE CA C 61.9 0.1 1 1356 . 256 PHE HA H 3.88 0.02 1 1357 . 256 PHE CB C 38.3 0.1 1 1358 . 256 PHE C C 176.2 0.1 1 1359 . 257 TYR N N 115.1 0.1 1 1360 . 257 TYR H H 7.84 0.02 1 1361 . 257 TYR CA C 63.5 0.1 1 1362 . 257 TYR HA H 3.78 0.02 1 1363 . 257 TYR CB C 37.6 0.1 1 1364 . 257 TYR C C 179.8 0.1 1 1365 . 258 ARG N N 119.5 0.1 1 1366 . 258 ARG H H 7.74 0.02 1 1367 . 258 ARG CA C 60.5 0.1 1 1368 . 258 ARG CB C 29.2 0.1 1 1369 . 258 ARG C C 177.9 0.1 1 1370 . 259 LEU N N 122.8 0.1 1 1371 . 259 LEU H H 7.49 0.02 1 1372 . 259 LEU CA C 57.6 0.1 1 1373 . 259 LEU HA H 4.09 0.02 1 1374 . 259 LEU CB C 40.4 0.1 1 1375 . 259 LEU C C 179.1 0.1 1 1376 . 260 LEU N N 119.7 0.1 1 1377 . 260 LEU H H 8.04 0.02 1 1378 . 260 LEU CA C 57.2 0.1 1 1379 . 260 LEU CB C 40.6 0.1 1 1380 . 260 LEU C C 178.1 0.1 1 1381 . 261 ASP N N 114.2 0.1 1 1382 . 261 ASP H H 7.04 0.02 1 1383 . 261 ASP CA C 56.6 0.1 1 1384 . 261 ASP HA H 4.67 0.02 1 1385 . 261 ASP CB C 42.8 0.1 1 1386 . 261 ASP C C 177.9 0.1 1 1387 . 262 GLU N N 117.5 0.1 1 1388 . 262 GLU H H 7.74 0.02 1 1389 . 262 GLU CA C 57.9 0.1 1 1390 . 262 GLU HA H 3.96 0.02 1 1391 . 262 GLU CB C 27.0 0.1 1 stop_ save_