data_16337 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments for the aminoglycoside phosphotransferase(3')-IIIa ; _BMRB_accession_number 16337 _BMRB_flat_file_name bmr16337.str _Entry_type original _Submission_date 2009-06-08 _Accession_date 2009-06-08 _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 Ozen Can . . 2 Norris Adrianne . . 3 Whittemore Neil . . 4 Steren Carlos . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 217 "13C chemical shifts" 631 "15N chemical shifts" 215 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-20 update BMRB 'complete entry citation' 2009-11-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(3')-IIIa.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19898995 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Serpersu Engin H. . 2 Ozen Can . . 3 Norris Adrianne L. . 4 Steren Carlos . . 5 Whittemore Neil . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9 _Page_last 12 _Year 2010 _Details . loop_ _Keyword NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Complex of APH with antibiotic tobramycin' _Enzyme_commission_number 2.7.1.95 loop_ _Mol_system_component_name _Mol_label enzyme $APH-tobramycin tobramycin $TOY stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 enzyme stop_ _Database_query_date . _Details 'The binary APH-tobramycin complex' save_ ######################## # Monomeric polymers # ######################## save_APH-tobramycin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common APH-tobramycin _Molecular_mass 30.974 _Mol_thiol_state 'all free' loop_ _Biological_function 'Antibiotic resistance by phosphorylation of aminoglycoside antibiotics' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 264 _Mol_residue_sequence ; MAKMRISPELKKLIEKYRCV KDTEGMSPAKVYKLVGENEN LYLKMTDSRYKGTTYDVERE KDMMLWLEGKLPVPKVLHFE RHDGWSNLLMSEADGVLCSE EYEDEQSPEKIIELYAECIR LFHSIDISDCPYTNSLDSRL AELDYLLNNDLADVDCENWE EDTPFKDPRELYDFLKTEKP EEELVFSHGDLGDSNIFVKD GKVSGFIDLGRSGRADKWYD IAFCVRSIREDIGEEQYVEL FFDLLGIKPDWEKIKYYILL DELF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 MET 5 ARG 6 ILE 7 SER 8 PRO 9 GLU 10 LEU 11 LYS 12 LYS 13 LEU 14 ILE 15 GLU 16 LYS 17 TYR 18 ARG 19 CYS 20 VAL 21 LYS 22 ASP 23 THR 24 GLU 25 GLY 26 MET 27 SER 28 PRO 29 ALA 30 LYS 31 VAL 32 TYR 33 LYS 34 LEU 35 VAL 36 GLY 37 GLU 38 ASN 39 GLU 40 ASN 41 LEU 42 TYR 43 LEU 44 LYS 45 MET 46 THR 47 ASP 48 SER 49 ARG 50 TYR 51 LYS 52 GLY 53 THR 54 THR 55 TYR 56 ASP 57 VAL 58 GLU 59 ARG 60 GLU 61 LYS 62 ASP 63 MET 64 MET 65 LEU 66 TRP 67 LEU 68 GLU 69 GLY 70 LYS 71 LEU 72 PRO 73 VAL 74 PRO 75 LYS 76 VAL 77 LEU 78 HIS 79 PHE 80 GLU 81 ARG 82 HIS 83 ASP 84 GLY 85 TRP 86 SER 87 ASN 88 LEU 89 LEU 90 MET 91 SER 92 GLU 93 ALA 94 ASP 95 GLY 96 VAL 97 LEU 98 CYS 99 SER 100 GLU 101 GLU 102 TYR 103 GLU 104 ASP 105 GLU 106 GLN 107 SER 108 PRO 109 GLU 110 LYS 111 ILE 112 ILE 113 GLU 114 LEU 115 TYR 116 ALA 117 GLU 118 CYS 119 ILE 120 ARG 121 LEU 122 PHE 123 HIS 124 SER 125 ILE 126 ASP 127 ILE 128 SER 129 ASP 130 CYS 131 PRO 132 TYR 133 THR 134 ASN 135 SER 136 LEU 137 ASP 138 SER 139 ARG 140 LEU 141 ALA 142 GLU 143 LEU 144 ASP 145 TYR 146 LEU 147 LEU 148 ASN 149 ASN 150 ASP 151 LEU 152 ALA 153 ASP 154 VAL 155 ASP 156 CYS 157 GLU 158 ASN 159 TRP 160 GLU 161 GLU 162 ASP 163 THR 164 PRO 165 PHE 166 LYS 167 ASP 168 PRO 169 ARG 170 GLU 171 LEU 172 TYR 173 ASP 174 PHE 175 LEU 176 LYS 177 THR 178 GLU 179 LYS 180 PRO 181 GLU 182 GLU 183 GLU 184 LEU 185 VAL 186 PHE 187 SER 188 HIS 189 GLY 190 ASP 191 LEU 192 GLY 193 ASP 194 SER 195 ASN 196 ILE 197 PHE 198 VAL 199 LYS 200 ASP 201 GLY 202 LYS 203 VAL 204 SER 205 GLY 206 PHE 207 ILE 208 ASP 209 LEU 210 GLY 211 ARG 212 SER 213 GLY 214 ARG 215 ALA 216 ASP 217 LYS 218 TRP 219 TYR 220 ASP 221 ILE 222 ALA 223 PHE 224 CYS 225 VAL 226 ARG 227 SER 228 ILE 229 ARG 230 GLU 231 ASP 232 ILE 233 GLY 234 GLU 235 GLU 236 GLN 237 TYR 238 VAL 239 GLU 240 LEU 241 PHE 242 PHE 243 ASP 244 LEU 245 LEU 246 GLY 247 ILE 248 LYS 249 PRO 250 ASP 251 TRP 252 GLU 253 LYS 254 ILE 255 LYS 256 TYR 257 TYR 258 ILE 259 LEU 260 LEU 261 ASP 262 GLU 263 LEU 264 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-09 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 1J7I ; Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Apoenzyme ; 100.00 264 100.00 100.00 0.00e+00 PDB 1J7L ; Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Complex ; 100.00 264 100.00 100.00 0.00e+00 PDB 1J7U ; Crystal Structure Of 3',5"-aminoglycoside Phosphotransferase Type Iiia Amppnp Complex ; 100.00 264 100.00 100.00 0.00e+00 PDB 1L8T ; Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A Complex ; 99.62 263 100.00 100.00 0.00e+00 PDB 2B0Q ; Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex ; 99.62 263 100.00 100.00 0.00e+00 PDB 2BKK "Crystal Structure Of Aminoglycoside Phosphotransferase Aph (3')-Iiia In Complex With The Inhibitor Ar_3a" 100.00 264 99.24 99.24 0.00e+00 PDB 3Q2J ; Crystal Structure Of 3',5"-aminoglycoside Phosphotransferase Type Iiia Protein Kinase Inhibitor Cki-7 Complex ; 100.00 264 100.00 100.00 0.00e+00 PDB 3TM0 ; Crystal Structure Of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Butirosin A Complex ; 99.62 263 100.00 100.00 0.00e+00 DBJ BAE98117 "aminoglycoside phosphotransferase [Enterococcus faecalis]" 100.00 264 97.35 98.11 0.00e+00 DBJ BAF75368 "neomycin phosphotransferase II [Shuttle vector pSU7]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAF75370 "neomycin phosphotransferase II [Shuttle vector pSU23]" 100.00 264 100.00 100.00 0.00e+00 DBJ BAF82029 "aminoglycoside phosphotransferase [Staphylococcus aureus]" 98.86 261 100.00 100.00 0.00e+00 DBJ BAG12997 "aminoglycoside phosphotransferase [Binary vector pUB-GW-GFP]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA04791 "aminoglycoside phosphotransferase [synthetic construct]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA24789 "unnamed protein product [Enterococcus faecalis]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA67773 "aph3 [Escherichia coli]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAA85747 "3'5''-aminoglycoside phosphotransferase [synthetic construct]" 100.00 264 100.00 100.00 0.00e+00 EMBL CAC29201 "aminoglycoside phosphotransferase type III [Enterococcus faecalis]" 100.00 264 100.00 100.00 0.00e+00 GB AAA26596 "aminocyclitol-3'-phosphotransferase [Staphylococcus aureus]" 100.00 263 98.48 98.86 0.00e+00 GB AAA98050 "kanamycin resistance protein [Plasmid pIP1433]" 100.00 264 100.00 100.00 0.00e+00 GB AAA98979 "3'5''-aminoglycoside phosphotransferase [synthetic construct]" 98.86 261 100.00 100.00 0.00e+00 GB AAB07765 "3'5'-aminoglycoside phosphotransferase [Staphylococcus aureus]" 100.00 264 100.00 100.00 0.00e+00 GB AAC16050 "aminoglycoside phosphotransferase A3 [Tn917 delivery vector pAJ005]" 100.00 264 100.00 100.00 0.00e+00 PIR I40613 "kanamycin resistance protein - Campylobacter coli plasmid pIP1433" 100.00 264 100.00 100.00 0.00e+00 PRF 1202264A phosphotransferase,aminoglycoside 100.00 264 100.00 100.00 0.00e+00 REF WP_001096887 "MULTISPECIES: aminoglycoside 3'-phosphotransferase [Bacteria]" 100.00 264 100.00 100.00 0.00e+00 REF WP_001637127 "aminoglycoside phosphotransferase APH(3') [Staphylococcus aureus]" 100.00 264 99.62 99.62 0.00e+00 REF WP_002360696 "MULTISPECIES: aminoglycoside phosphotransferase APH(3') [Bacteria]" 98.86 261 100.00 100.00 0.00e+00 REF WP_002409341 "aminoglycoside phosphotransferase APH(3'), partial [Enterococcus faecalis]" 85.61 226 100.00 100.00 6.50e-161 REF WP_002418579 "MULTISPECIES: aminoglycoside phosphotransferase APH(3'), partial [Bacilli]" 82.20 217 100.00 100.00 3.11e-154 SP P0A3Y5 "RecName: Full=Aminoglycoside 3'-phosphotransferase; AltName: Full=APH(3')III; AltName: Full=Kanamycin kinase, type III; AltName" 100.00 264 100.00 100.00 0.00e+00 SP P0A3Y6 "RecName: Full=Aminoglycoside 3'-phosphotransferase; AltName: Full=APH(3')III; AltName: Full=Kanamycin kinase, type III; AltName" 100.00 263 98.48 98.86 0.00e+00 stop_ save_ ############# # Ligands # ############# save_TOY _Saveframe_category ligand _Mol_type non-polymer _Name_common "TOY (TOBRAMYCIN)" _BMRB_code . _PDB_code TOY _Molecular_mass 467.514 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 26 10:14:07 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C11 C11 C . 0 . ? O11 O11 O . 0 . ? C21 C21 C . 0 . ? N21 N21 N . 0 . ? C31 C31 C . 0 . ? C41 C41 C . 0 . ? O41 O41 O . 0 . ? C51 C51 C . 0 . ? O51 O51 O . 0 . ? C61 C61 C . 0 . ? N61 N61 N . 0 . ? C12 C12 C . 0 . ? N12 N12 N . 0 . ? C22 C22 C . 0 . ? C32 C32 C . 0 . ? N32 N32 N . 0 . ? C42 C42 C . 0 . ? C52 C52 C . 0 . ? O52 O52 O . 0 . ? C62 C62 C . 0 . ? O62 O62 O . 0 . ? C13 C13 C . 0 . ? C23 C23 C . 0 . ? O23 O23 O . 0 . ? C33 C33 C . 0 . ? N33 N33 N . 0 . ? C43 C43 C . 0 . ? O43 O43 O . 0 . ? C53 C53 C . 0 . ? O53 O53 O . 0 . ? C63 C63 C . 0 . ? O63 O63 O . 0 . ? H11 H11 H . 0 . ? H21 H21 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? H311 H311 H . 0 . ? H312 H312 H . 0 . ? H41 H41 H . 0 . ? H41O H41O H . 0 . ? H51 H51 H . 0 . ? H611 H611 H . 0 . ? H612 H612 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H12 H12 H . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? H221 H221 H . 0 . ? H222 H222 H . 0 . ? H32 H32 H . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? H42 H42 H . 0 . ? H52 H52 H . 0 . ? H52O H52O H . 0 . ? H62 H62 H . 0 . ? H13 H13 H . 0 . ? H23 H23 H . 0 . ? H23O H23O H . 0 . ? H33 H33 H . 0 . ? HN31 HN31 H . 0 . ? HN32 HN32 H . 0 . ? H43 H43 H . 0 . ? H43O H43O H . 0 . ? H53 H53 H . 0 . ? H631 H631 H . 0 . ? H632 H632 H . 0 . ? H63O H63O H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C11 O11 ? ? SING C11 C21 ? ? SING C11 O51 ? ? SING C11 H11 ? ? SING O11 C42 ? ? SING C21 N21 ? ? SING C21 C31 ? ? SING C21 H21 ? ? SING N21 HN21 ? ? SING N21 HN22 ? ? SING C31 C41 ? ? SING C31 H311 ? ? SING C31 H312 ? ? SING C41 O41 ? ? SING C41 C51 ? ? SING C41 H41 ? ? SING O41 H41O ? ? SING C51 O51 ? ? SING C51 C61 ? ? SING C51 H51 ? ? SING C61 N61 ? ? SING C61 H611 ? ? SING C61 H612 ? ? SING N61 HN61 ? ? SING N61 HN62 ? ? SING C12 N12 ? ? SING C12 C22 ? ? SING C12 C62 ? ? SING C12 H12 ? ? SING N12 HN11 ? ? SING N12 HN12 ? ? SING C22 C32 ? ? SING C22 H221 ? ? SING C22 H222 ? ? SING C32 N32 ? ? SING C32 C42 ? ? SING C32 H32 ? ? SING N32 HN1 ? ? SING N32 HN2 ? ? SING C42 C52 ? ? SING C42 H42 ? ? SING C52 O52 ? ? SING C52 C62 ? ? SING C52 H52 ? ? SING O52 H52O ? ? SING C62 O62 ? ? SING C62 H62 ? ? SING O62 C13 ? ? SING C13 C23 ? ? SING C13 O53 ? ? SING C13 H13 ? ? SING C23 O23 ? ? SING C23 C33 ? ? SING C23 H23 ? ? SING O23 H23O ? ? SING C33 N33 ? ? SING C33 C43 ? ? SING C33 H33 ? ? SING N33 HN31 ? ? SING N33 HN32 ? ? SING C43 O43 ? ? SING C43 C53 ? ? SING C43 H43 ? ? SING O43 H43O ? ? SING C53 O53 ? ? SING C53 C63 ? ? SING C53 H53 ? ? SING C63 O63 ? ? SING C63 H631 ? ? SING C63 H632 ? ? SING O63 H63O ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . 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 $APH-tobramycin 'Streptococcus faecalis' 1351 Bacteria . Enterococcus faecalis IIIa 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-tobramycin 'recombinant technology' . Escherichia coli BL21 pAT21-1 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-tobramycin 250 uM '[U-13C; U-15N; U-2H]' Tris-HCl 25 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 1 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 5 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model DMX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model DMX _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.4 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 protons ppm 0 na indirect . . . 0.251449530 $entry_citation $entry_citation DSS N 15 protons ppm 0 na indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HNCO' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name enzyme _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 2 ALA H H 7.68 0.02 1 2 2 2 ALA C C 173.4 0.30 1 3 2 2 ALA CA C 51.4 0.30 1 4 2 2 ALA CB C 18.5 0.30 1 5 2 2 ALA N N 120.4 0.20 1 6 3 3 LYS H H 9.23 0.02 1 7 3 3 LYS CA C 51.4 0.30 1 8 3 3 LYS CB C 31.7 0.30 1 9 6 6 ILE H H 7.33 0.02 1 10 6 6 ILE C C 173.6 0.30 5 11 6 6 ILE CA C 60.8 0.30 1 12 6 6 ILE CB C 37.3 0.30 1 13 6 6 ILE N N 108.7 0.20 1 14 7 7 SER H H 7.49 0.02 1 15 7 7 SER CA C 53.3 0.30 1 16 7 7 SER CB C 65.3 0.30 1 17 7 7 SER N N 123.9 0.20 1 18 8 8 PRO C C 174.9 0.30 9 19 8 8 PRO CA C 50.9 0.30 9 20 8 8 PRO CB C 33.2 0.30 9 21 9 9 GLU H H 8.09 0.02 9 22 9 9 GLU C C 171.9 0.30 9 23 9 9 GLU CA C 59.5 0.30 9 24 9 9 GLU CB C 38.6 0.30 9 25 9 9 GLU N N 123.1 0.20 9 26 10 10 LEU H H 8.01 0.02 1 27 10 10 LEU C C 172.8 0.30 1 28 10 10 LEU CA C 56.7 0.30 1 29 10 10 LEU CB C 25.2 0.30 9 30 10 10 LEU N N 124.3 0.20 1 31 11 11 LYS H H 8.28 0.02 1 32 11 11 LYS C C 171.9 0.30 1 33 11 11 LYS CA C 59.3 0.30 1 34 11 11 LYS CB C 31.1 0.30 1 35 11 11 LYS N N 119.8 0.20 1 36 12 12 LYS H H 7.35 0.02 1 37 12 12 LYS C C 171.5 0.30 1 38 12 12 LYS CA C 58.0 0.30 1 39 12 12 LYS CB C 31.1 0.30 1 40 12 12 LYS N N 117.2 0.20 1 41 13 13 LEU H H 7.30 0.02 1 42 13 13 LEU C C 175.3 0.30 1 43 13 13 LEU CA C 56.9 0.30 1 44 13 13 LEU CB C 41.3 0.30 9 45 13 13 LEU N N 119.2 0.20 1 46 14 14 ILE H H 8.55 0.02 1 47 14 14 ILE C C 171.1 0.30 1 48 14 14 ILE CA C 55.1 0.30 1 49 14 14 ILE CB C 30.2 0.30 4 50 14 14 ILE N N 123.0 0.20 1 51 15 15 GLU H H 8.97 0.02 1 52 15 15 GLU C C 173.4 0.30 1 53 15 15 GLU CA C 58.2 0.30 1 54 15 15 GLU CB C 28.9 0.30 1 55 15 15 GLU N N 122.5 0.20 1 56 16 16 LYS H H 8.07 0.02 9 57 16 16 LYS C C 175.0 0.30 9 58 16 16 LYS CA C 55.8 0.30 9 59 16 16 LYS CB C 30.2 0.30 9 60 16 16 LYS N N 115.9 0.20 9 61 17 17 TYR H H 7.64 0.02 9 62 17 17 TYR C C 170.3 0.30 9 63 17 17 TYR CA C 57.1 0.30 9 64 17 17 TYR CB C 40.4 0.30 9 65 17 17 TYR N N 119.9 0.20 9 66 18 18 ARG H H 8.81 0.02 1 67 18 18 ARG C C 171.9 0.30 1 68 18 18 ARG CA C 57.8 0.30 1 69 18 18 ARG CB C 30.4 0.30 1 70 18 18 ARG N N 119.3 0.20 1 71 19 19 CYS H H 7.71 0.02 1 72 19 19 CYS C C 176.0 0.30 1 73 19 19 CYS CA C 58.4 0.30 1 74 19 19 CYS N N 121.3 0.20 1 75 20 20 VAL H H 9.52 0.02 1 76 20 20 VAL C C 175.0 0.30 1 77 20 20 VAL CA C 61.0 0.30 1 78 20 20 VAL CB C 32.8 0.30 1 79 20 20 VAL N N 131.0 0.20 1 80 21 21 LYS H H 8.83 0.02 1 81 21 21 LYS CA C 57.0 0.30 1 82 21 21 LYS CB C 32.7 0.30 1 83 21 21 LYS N N 130.0 0.20 1 84 23 23 THR H H 7.93 0.02 9 85 23 23 THR CA C 56.4 0.30 9 86 23 23 THR CB C 62.9 0.30 9 87 23 23 THR N N 117.1 0.20 9 88 24 24 GLU C C 172.9 0.30 1 89 25 25 GLY H H 8.30 0.02 1 90 25 25 GLY C C 176.5 0.30 1 91 25 25 GLY CA C 47.2 0.30 1 92 25 25 GLY N N 105.8 0.20 1 93 26 26 MET H H 8.17 0.02 1 94 26 26 MET C C 175.8 0.30 1 95 26 26 MET CA C 57.2 0.30 1 96 26 26 MET CB C 36.0 0.30 4 97 26 26 MET N N 123.7 0.20 1 98 27 27 SER H H 9.23 0.02 1 99 27 27 SER CA C 57.1 0.30 1 100 27 27 SER CB C 60.6 0.30 1 101 27 27 SER N N 121.8 0.20 1 102 28 28 PRO C C 170.3 0.30 1 103 28 28 PRO CA C 57.6 0.30 1 104 29 29 ALA H H 7.72 0.02 9 105 29 29 ALA CA C 54.8 0.30 9 106 29 29 ALA CB C 17.0 0.30 9 107 29 29 ALA N N 125.1 0.20 9 108 31 31 VAL H H 8.25 0.02 1 109 31 31 VAL C C 176.1 0.30 1 110 31 31 VAL CA C 60.8 0.30 1 111 31 31 VAL CB C 33.4 0.30 1 112 31 31 VAL N N 123.8 0.20 1 113 32 32 TYR H H 9.49 0.02 1 114 32 32 TYR C C 176.2 0.30 1 115 32 32 TYR CA C 55.8 0.30 1 116 32 32 TYR CB C 40.2 0.30 1 117 32 32 TYR N N 125.8 0.20 1 118 33 33 LYS H H 8.97 0.02 1 119 33 33 LYS C C 176.8 0.30 1 120 33 33 LYS CA C 54.8 0.30 1 121 33 33 LYS CB C 33.3 0.30 1 122 33 33 LYS N N 125.5 0.20 1 123 34 34 LEU H H 8.79 0.02 1 124 34 34 LEU C C 175.2 0.30 1 125 34 34 LEU CA C 52.0 0.30 1 126 34 34 LEU CB C 39.1 0.30 4 127 34 34 LEU N N 130.2 0.20 1 128 35 35 VAL H H 9.15 0.02 1 129 35 35 VAL C C 173.8 0.30 1 130 35 35 VAL CA C 62.0 0.30 1 131 35 35 VAL CB C 32.1 0.30 4 132 35 35 VAL N N 125.1 0.20 1 133 36 36 GLY H H 8.47 0.02 1 134 36 36 GLY C C 170.6 0.30 5 135 36 36 GLY CA C 43.4 0.30 1 136 36 36 GLY N N 120.2 0.20 1 137 37 37 GLU H H 8.42 0.02 9 138 37 37 GLU CA C 56.9 0.30 4 139 37 37 GLU CB C 40.4 0.30 9 140 37 37 GLU N N 120.9 0.20 9 141 39 39 GLU C C 173.9 0.30 1 142 40 40 ASN H H 8.32 0.02 1 143 40 40 ASN C C 176.7 0.30 1 144 40 40 ASN CA C 50.8 0.30 1 145 40 40 ASN CB C 40.1 0.30 9 146 40 40 ASN N N 117.1 0.20 1 147 41 41 LEU H H 8.83 0.02 1 148 41 41 LEU C C 175.8 0.30 1 149 41 41 LEU CA C 52.0 0.30 1 150 41 41 LEU CB C 44.0 0.30 1 151 41 41 LEU N N 119.7 0.20 1 152 42 42 TYR H H 8.69 0.02 1 153 42 42 TYR C C 177.1 0.30 1 154 42 42 TYR CA C 57.2 0.30 1 155 42 42 TYR CB C 41.4 0.30 1 156 42 42 TYR N N 116.4 0.20 1 157 43 43 LEU H H 9.04 0.02 1 158 43 43 LEU C C 176.8 0.30 1 159 43 43 LEU CA C 52.3 0.30 1 160 43 43 LEU CB C 45.3 0.30 1 161 43 43 LEU N N 126.2 0.20 1 162 44 44 LYS H H 9.55 0.02 1 163 44 44 LYS C C 175.3 0.30 1 164 44 44 LYS CA C 54.4 0.30 1 165 44 44 LYS CB C 36.3 0.30 4 166 44 44 LYS N N 127.9 0.20 1 167 45 45 MET H H 9.22 0.02 1 168 45 45 MET C C 174.0 0.30 1 169 45 45 MET CA C 54.4 0.30 1 170 45 45 MET CB C 37.5 0.30 1 171 45 45 MET N N 123.3 0.20 1 172 46 46 THR H H 9.39 0.02 1 173 46 46 THR C C 176.6 0.30 1 174 46 46 THR CA C 59.3 0.30 1 175 46 46 THR CB C 72.0 0.30 1 176 46 46 THR N N 112.6 0.20 1 177 47 47 ASP H H 7.70 0.02 1 178 47 47 ASP C C 173.8 0.30 1 179 47 47 ASP CA C 52.0 0.30 1 180 47 47 ASP CB C 39.1 0.30 1 181 47 47 ASP N N 115.9 0.20 1 182 48 48 SER H H 7.40 0.02 1 183 48 48 SER C C 173.5 0.30 1 184 48 48 SER CA C 60.8 0.30 1 185 48 48 SER CB C 67.8 0.30 1 186 48 48 SER N N 123.2 0.20 1 187 49 49 ARG H H 8.68 0.02 1 188 49 49 ARG C C 172.4 0.30 1 189 49 49 ARG CA C 58.3 0.30 1 190 49 49 ARG CB C 28.6 0.30 1 191 49 49 ARG N N 123.6 0.20 1 192 50 50 TYR H H 7.59 0.02 1 193 50 50 TYR C C 174.5 0.30 1 194 50 50 TYR CA C 57.3 0.30 1 195 50 50 TYR CB C 37.5 0.30 1 196 50 50 TYR N N 113.2 0.20 1 197 51 51 LYS H H 7.30 0.02 1 198 51 51 LYS C C 172.6 0.30 1 199 51 51 LYS CA C 57.3 0.30 1 200 51 51 LYS CB C 31.2 0.30 1 201 51 51 LYS N N 125.6 0.20 1 202 52 52 GLY H H 10.0 0.02 1 203 52 52 GLY C C 174.3 0.30 5 204 52 52 GLY CA C 45.4 0.30 1 205 52 52 GLY N N 115.9 0.20 1 206 53 53 THR H H 7.79 0.02 9 207 53 53 THR C C 173.3 0.30 9 208 53 53 THR CA C 58.2 0.30 9 209 53 53 THR CB C 73.0 0.30 5 210 53 53 THR N N 110.9 0.20 9 211 54 54 THR H H 7.68 0.02 1 212 54 54 THR C C 176.2 0.30 1 213 54 54 THR CA C 52.8 0.30 9 214 54 54 THR CB C 74.2 0.30 1 215 54 54 THR N N 120.4 0.20 1 216 55 55 TYR H H 7.86 0.02 1 217 55 55 TYR C C 174.6 0.30 1 218 55 55 TYR CA C 57.3 0.30 1 219 55 55 TYR CB C 38.7 0.30 1 220 55 55 TYR N N 117.0 0.20 1 221 56 56 ASP H H 7.40 0.02 1 222 56 56 ASP C C 170.4 0.30 1 223 56 56 ASP CA C 53.5 0.30 1 224 56 56 ASP CB C 41.0 0.30 1 225 56 56 ASP N N 119.5 0.20 1 226 57 57 VAL H H 8.47 0.02 1 227 57 57 VAL C C 173.5 0.30 5 228 57 57 VAL CA C 64.3 0.30 1 229 57 57 VAL N N 127.8 0.20 1 230 58 58 GLU H H 9.08 0.02 1 231 58 58 GLU C C 172.7 0.30 1 232 58 58 GLU CA C 59.5 0.30 1 233 58 58 GLU CB C 30.4 0.30 4 234 58 58 GLU N N 124.5 0.20 1 235 59 59 ARG H H 7.22 0.02 1 236 59 59 ARG C C 172.2 0.30 1 237 59 59 ARG CA C 58.5 0.30 1 238 59 59 ARG N N 117.3 0.20 1 239 60 60 GLU H H 6.56 0.02 1 240 60 60 GLU C C 173.4 0.30 1 241 60 60 GLU CA C 59.5 0.30 1 242 60 60 GLU CB C 28.4 0.30 1 243 60 60 GLU N N 118.3 0.20 1 244 61 61 LYS H H 8.09 0.02 1 245 61 61 LYS C C 171.2 0.30 5 246 61 61 LYS CA C 59.5 0.30 1 247 61 61 LYS CB C 27.2 0.30 1 248 61 61 LYS N N 120.2 0.20 1 249 62 62 ASP H H 7.77 0.02 1 250 62 62 ASP CA C 57.4 0.30 1 251 62 62 ASP CB C 40.9 0.30 4 252 68 68 GLU C C 173.1 0.30 1 253 69 69 GLY H H 8.45 0.02 1 254 69 69 GLY C C 176.6 0.30 1 255 69 69 GLY CA C 45.4 0.30 1 256 69 69 GLY N N 109.9 0.20 1 257 70 70 LYS H H 8.59 0.02 1 258 70 70 LYS C C 174.8 0.30 1 259 70 70 LYS CA C 56.8 0.30 1 260 70 70 LYS CB C 33.8 0.30 1 261 70 70 LYS N N 121.1 0.20 1 262 71 71 LEU H H 7.84 0.02 1 263 71 71 LEU CA C 51.1 0.30 1 264 71 71 LEU CB C 45.2 0.30 1 265 71 71 LEU N N 117.7 0.20 1 266 74 74 PRO C C 174.7 0.30 9 267 74 74 PRO CA C 62 0.30 1 268 74 74 PRO CB C 36.5 0.30 1 269 75 75 LYS H H 8.05 0.02 1 270 75 75 LYS C C 173.4 0.30 1 271 75 75 LYS CA C 54.3 0.30 1 272 75 75 LYS CB C 32.9 0.30 1 273 75 75 LYS N N 118.1 0.20 1 274 76 76 VAL H H 8.74 0.02 1 275 76 76 VAL C C 174.6 0.30 1 276 76 76 VAL CA C 63.1 0.30 1 277 76 76 VAL CB C 31.1 0.30 1 278 76 76 VAL N N 123.2 0.20 1 279 77 77 LEU H H 9.00 0.02 1 280 77 77 LEU C C 175.0 0.30 1 281 77 77 LEU CA C 55.2 0.30 1 282 77 77 LEU CB C 41.5 0.30 1 283 77 77 LEU N N 130.0 0.20 1 284 78 78 HIS H H 8.84 0.02 1 285 78 78 HIS C C 170.3 0.30 1 286 78 78 HIS CA C 58.2 0.30 1 287 78 78 HIS N N 127.0 0.20 1 288 79 79 PHE H H 8.89 0.02 9 289 79 79 PHE CA C 57.2 0.30 9 290 79 79 PHE CB C 40.9 0.30 4 291 79 79 PHE N N 120.7 0.20 9 292 83 83 ASP C C 175.2 0.30 1 293 84 84 GLY H H 8.35 0.02 1 294 84 84 GLY C C 176.3 0.30 1 295 84 84 GLY CA C 44.9 0.30 1 296 84 84 GLY N N 104.5 0.20 1 297 85 85 TRP H H 8.43 0.02 1 298 85 85 TRP C C 174.2 0.30 1 299 85 85 TRP CA C 57.0 0.30 1 300 85 85 TRP CB C 28.5 0.30 1 301 85 85 TRP N N 123.9 0.20 1 302 86 86 SER H H 9.31 0.02 1 303 86 86 SER C C 179.3 0.30 1 304 86 86 SER CA C 57.0 0.30 1 305 86 86 SER CB C 64.1 0.30 1 306 86 86 SER N N 119.9 0.20 1 307 87 87 ASN H H 8.64 0.02 1 308 87 87 ASN C C 178.2 0.30 1 309 87 87 ASN CA C 51.9 0.30 1 310 87 87 ASN CB C 40.3 0.30 1 311 87 87 ASN N N 121.4 0.20 1 312 88 88 LEU H H 9.30 0.02 1 313 88 88 LEU C C 178.1 0.30 1 314 88 88 LEU CA C 53.3 0.30 1 315 88 88 LEU CB C 46.0 0.30 1 316 88 88 LEU N N 124.9 0.20 1 317 89 89 LEU H H 9.32 0.02 1 318 89 89 LEU C C 175.5 0.30 1 319 89 89 LEU CA C 52.9 0.30 1 320 89 89 LEU CB C 45.0 0.30 4 321 89 89 LEU N N 130.0 0.20 1 322 90 90 MET H H 9.80 0.02 1 323 90 90 MET C C 176.6 0.30 1 324 90 90 MET CA C 53.3 0.30 1 325 90 90 MET CB C 38.0 0.30 1 326 90 90 MET N N 126.6 0.20 1 327 91 91 SER H H 8.23 0.02 1 328 91 91 SER C C 178.8 0.30 1 329 91 91 SER CA C 57.3 0.30 1 330 91 91 SER CB C 64.4 0.30 1 331 91 91 SER N N 114.7 0.20 1 332 92 92 GLU H H 8.23 0.02 1 333 92 92 GLU C C 173.6 0.30 1 334 92 92 GLU CA C 55.1 0.30 1 335 92 92 GLU CB C 30.8 0.30 1 336 92 92 GLU N N 117.3 0.20 1 337 93 93 ALA H H 8.27 0.02 1 338 93 93 ALA C C 175.2 0.30 1 339 93 93 ALA CA C 51.1 0.30 1 340 93 93 ALA CB C 16.2 0.30 1 341 93 93 ALA N N 129.8 0.20 1 342 94 94 ASP H H 8.54 0.02 1 343 94 94 ASP C C 174.1 0.30 1 344 94 94 ASP CA C 53.4 0.30 1 345 94 94 ASP CB C 42.0 0.30 1 346 94 94 ASP N N 121.5 0.20 1 347 95 95 GLY H H 8.00 0.02 1 348 95 95 GLY C C 177.7 0.30 1 349 95 95 GLY CA C 43.5 0.30 1 350 95 95 GLY N N 109.3 0.20 1 351 96 96 VAL H H 8.82 0.02 1 352 96 96 VAL C C 175.5 0.30 1 353 96 96 VAL CA C 59.5 0.30 1 354 96 96 VAL CB C 34.4 0.30 4 355 96 96 VAL N N 120.8 0.20 1 356 97 97 LEU H H 8.54 0.02 1 357 97 97 LEU C C 171.1 0.30 5 358 97 97 LEU CA C 54.7 0.30 1 359 97 97 LEU CB C 42.1 0.30 1 360 97 97 LEU N N 127.9 0.20 1 361 98 98 CYS H H 9.07 0.02 1 362 98 98 CYS C C 175.2 0.30 1 363 98 98 CYS CA C 62.1 0.30 1 364 98 98 CYS CB C 26.0 0.30 4 365 98 98 CYS N N 124.4 0.20 1 366 99 99 SER H H 7.48 0.02 1 367 99 99 SER C C 175.0 0.30 1 368 99 99 SER CA C 59.3 0.30 1 369 99 99 SER CB C 61.3 0.30 1 370 99 99 SER N N 111.6 0.20 1 371 100 100 GLU H H 6.99 0.02 1 372 100 100 GLU C C 172.5 0.30 1 373 100 100 GLU CA C 57.0 0.30 1 374 100 100 GLU CB C 29.1 0.30 1 375 100 100 GLU N N 121.4 0.20 1 376 101 101 GLU H H 8.07 0.02 1 377 101 101 GLU C C 172.8 0.30 1 378 101 101 GLU CA C 57.6 0.30 1 379 101 101 GLU CB C 28.6 0.30 1 380 101 101 GLU N N 122.4 0.20 1 381 102 102 TYR H H 7.59 0.02 1 382 102 102 TYR C C 174.1 0.30 1 383 102 102 TYR CA C 56.1 0.30 1 384 102 102 TYR CB C 36.4 0.30 1 385 102 102 TYR N N 114.7 0.20 1 386 103 103 GLU H H 7.24 0.02 1 387 103 103 GLU C C 173.1 0.30 1 388 103 103 GLU CA C 58.2 0.30 1 389 103 103 GLU CB C 28.8 0.30 1 390 103 103 GLU N N 122.0 0.20 1 391 104 104 ASP H H 7.94 0.02 5 392 104 104 ASP C C 174.2 0.30 5 393 104 104 ASP CA C 52.0 0.30 5 394 104 104 ASP CB C 38.3 0.30 5 395 104 104 ASP N N 115.2 0.20 5 396 105 105 GLU H H 7.39 0.02 1 397 105 105 GLU C C 169.5 0.30 1 398 105 105 GLU CA C 54.5 0.30 1 399 105 105 GLU CB C 28.9 0.30 1 400 105 105 GLU N N 124.9 0.20 1 401 106 106 GLN H H 8.02 0.02 1 402 106 106 GLN C C 172.2 0.30 1 403 106 106 GLN CA C 58.3 0.30 1 404 106 106 GLN CB C 28.1 0.30 1 405 106 106 GLN N N 120.9 0.20 1 406 107 107 SER H H 7.87 0.02 1 407 107 107 SER CA C 64.5 0.30 1 408 107 107 SER CB C 68.9 0.30 1 409 107 107 SER N N 113.5 0.20 1 410 108 108 PRO C C 174.2 0.30 1 411 108 108 PRO CA C 64.8 0.30 1 412 109 109 GLU H H 7.90 0.02 1 413 109 109 GLU C C 176.1 0.30 1 414 109 109 GLU CA C 54.5 0.30 1 415 109 109 GLU CB C 26.6 0.30 1 416 109 109 GLU N N 121.0 0.20 1 417 110 110 LYS H H 6.30 0.02 1 418 110 110 LYS CA C 54.2 0.30 1 419 110 110 LYS CB C 32.3 0.30 1 420 110 110 LYS N N 119.6 0.20 1 421 111 111 ILE C C 176.1 0.30 1 422 112 112 ILE H H 7.47 0.02 1 423 112 112 ILE C C 173.2 0.30 1 424 112 112 ILE CA C 61.8 0.30 1 425 112 112 ILE N N 116.9 0.20 1 426 113 113 GLU H H 7.76 0.02 1 427 113 113 GLU C C 172.9 0.30 5 428 113 113 GLU CA C 59.5 0.30 1 429 113 113 GLU CB C 29.0 0.30 1 430 113 113 GLU N N 117.7 0.20 1 431 114 114 LEU H H 7.77 0.02 1 432 114 114 LEU C C 172.7 0.30 1 433 114 114 LEU CA C 57.4 0.30 1 434 114 114 LEU CB C 40.9 0.30 4 435 114 114 LEU N N 119.9 0.20 1 436 115 115 TYR H H 7.20 0.02 1 437 115 115 TYR C C 173.8 0.30 1 438 115 115 TYR CA C 60.8 0.30 1 439 115 115 TYR CB C 36.6 0.30 1 440 115 115 TYR N N 118.8 0.20 1 441 116 116 ALA H H 8.47 0.02 1 442 116 116 ALA CA C 59.3 0.30 1 443 116 116 ALA CB C 20.5 0.30 1 444 116 116 ALA N N 120.2 0.20 1 445 117 117 GLU H H 8.50 0.02 9 446 117 117 GLU C C 172.6 0.30 9 447 117 117 GLU CA C 55.3 0.30 9 448 117 117 GLU CB C 32.3 0.30 9 449 117 117 GLU N N 120.4 0.20 9 450 118 118 CYS H H 7.55 0.02 9 451 118 118 CYS C C 171.3 0.30 9 452 118 118 CYS CA C 58.1 0.30 9 453 118 118 CYS CB C 28.5 0.30 9 454 118 118 CYS N N 116.0 0.20 9 455 119 119 ILE H H 7.22 0.02 1 456 119 119 ILE C C 172.1 0.30 1 457 119 119 ILE CA C 63.0 0.30 1 458 119 119 ILE CB C 36.0 0.30 1 459 119 119 ILE N N 120.4 0.20 1 460 120 120 ARG H H 8.39 0.02 1 461 120 120 ARG C C 174.9 0.30 1 462 120 120 ARG CA C 57.1 0.30 1 463 120 120 ARG CB C 39.8 0.30 1 464 120 120 ARG N N 122.7 0.20 1 465 121 121 LEU H H 8.34 0.02 1 466 121 121 LEU C C 173.9 0.30 1 467 121 121 LEU CA C 54.7 0.30 1 468 121 121 LEU CB C 42.7 0.30 1 469 121 121 LEU N N 115.7 0.20 1 470 122 122 PHE H H 6.99 0.02 1 471 122 122 PHE CA C 58.3 0.30 1 472 122 122 PHE CB C 28.1 0.30 1 473 122 122 PHE N N 122.9 0.20 1 474 123 123 HIS C C 175.0 0.30 1 475 124 124 SER H H 7.79 0.02 1 476 124 124 SER C C 176.3 0.30 1 477 124 124 SER CA C 59.0 0.30 1 478 124 124 SER CB C 63.8 0.30 1 479 124 124 SER N N 114.4 0.20 1 480 125 125 ILE H H 7.19 0.02 1 481 125 125 ILE C C 174.7 0.30 1 482 125 125 ILE CA C 59.9 0.30 1 483 125 125 ILE CB C 36.6 0.30 1 484 125 125 ILE N N 123.7 0.20 1 485 126 126 ASP H H 8.67 0.02 1 486 126 126 ASP C C 173.4 0.30 1 487 126 126 ASP CA C 53.4 0.30 1 488 126 126 ASP CB C 39.9 0.30 1 489 126 126 ASP N N 128.6 0.20 1 490 127 127 ILE H H 8.26 0.02 1 491 127 127 ILE C C 172.8 0.30 1 492 127 127 ILE CA C 60.5 0.30 1 493 127 127 ILE CB C 36.2 0.30 4 494 127 127 ILE N N 118.0 0.20 1 495 128 128 SER H H 8.96 0.02 1 496 128 128 SER C C 175.7 0.30 1 497 128 128 SER CA C 62.2 0.30 1 498 128 128 SER CB C 61.4 0.30 1 499 128 128 SER N N 122.0 0.20 1 500 129 129 ASP H H 7.99 0.02 1 501 129 129 ASP C C 175.4 0.30 1 502 129 129 ASP CA C 51.3 0.30 1 503 129 129 ASP CB C 39.5 0.30 1 504 129 129 ASP N N 119.0 0.20 1 505 130 130 CYS H H 6.78 0.02 1 506 130 130 CYS CA C 55.9 0.30 1 507 130 130 CYS CB C 26.6 0.30 1 508 130 130 CYS N N 121.3 0.20 1 509 131 131 PRO C C 174.6 0.30 1 510 131 131 PRO CA C 56.9 0.30 9 511 131 131 PRO CB C 32.2 0.30 1 512 132 132 TYR H H 8.53 0.02 9 513 132 132 TYR C C 173.8 0.30 9 514 132 132 TYR CA C 53.6 0.30 9 515 132 132 TYR CB C 41.4 0.30 9 516 132 132 TYR N N 126.9 0.20 9 517 133 133 THR H H 8.28 0.02 1 518 133 133 THR C C 177.6 0.30 1 519 133 133 THR CA C 61.5 0.30 1 520 133 133 THR CB C 68.8 0.30 1 521 133 133 THR N N 116.3 0.20 1 522 134 134 ASN H H 9.40 0.02 1 523 134 134 ASN C C 175.7 0.30 1 524 134 134 ASN CA C 50.7 0.30 1 525 134 134 ASN CB C 36.9 0.30 1 526 134 134 ASN N N 133.2 0.20 1 527 135 135 SER H H 6.69 0.02 1 528 135 135 SER C C 175.2 0.30 1 529 135 135 SER CA C 56.2 0.30 1 530 135 135 SER CB C 63.7 0.30 1 531 135 135 SER N N 111.8 0.20 1 532 136 136 LEU H H 10.40 0.02 1 533 136 136 LEU C C 171.3 0.30 1 534 136 136 LEU CA C 58.3 0.30 1 535 136 136 LEU CB C 41.0 0.30 1 536 136 136 LEU N N 125.3 0.20 1 537 137 137 ASP H H 9.10 0.02 9 538 137 137 ASP C C 171.0 0.30 9 539 137 137 ASP CA C 57.4 0.30 9 540 137 137 ASP CB C 39.3 0.30 9 541 137 137 ASP N N 118.5 0.20 9 542 138 138 SER H H 7.62 0.02 1 543 138 138 SER C C 173.4 0.30 1 544 138 138 SER CA C 60.8 0.30 1 545 138 138 SER CB C 62.3 0.30 1 546 138 138 SER N N 116.7 0.20 1 547 139 139 ARG H H 9.33 0.02 1 548 139 139 ARG C C 170.3 0.30 1 549 139 139 ARG CA C 57.0 0.30 1 550 139 139 ARG CB C 39.4 0.30 1 551 139 139 ARG N N 117.8 0.20 1 552 140 140 LEU H H 7.53 0.02 1 553 140 140 LEU C C 175.8 0.30 1 554 140 140 LEU CA C 55.2 0.30 1 555 140 140 LEU CB C 42.3 0.30 1 556 140 140 LEU N N 117.7 0.20 1 557 141 141 ALA H H 7.97 0.02 1 558 141 141 ALA C C 176.7 0.30 1 559 141 141 ALA CA C 53.6 0.30 1 560 141 141 ALA CB C 18.9 0.30 1 561 141 141 ALA N N 131.4 0.20 1 562 142 142 GLU H H 7.23 0.02 1 563 142 142 GLU C C 175.6 0.30 1 564 142 142 GLU CA C 55.0 0.30 1 565 142 142 GLU CB C 30.1 0.30 1 566 142 142 GLU N N 115.3 0.20 1 567 143 143 LEU H H 8.27 0.02 1 568 143 143 LEU C C 174.5 0.30 1 569 143 143 LEU CA C 55.5 0.30 1 570 143 143 LEU CB C 30.5 0.30 9 571 143 143 LEU N N 122.7 0.20 1 572 144 144 ASP H H 10.40 0.02 1 573 144 144 ASP C C 173.2 0.30 1 574 144 144 ASP CA C 54.9 0.30 1 575 144 144 ASP CB C 34.1 0.30 1 576 144 144 ASP N N 128.3 0.20 1 577 145 145 TYR H H 7.14 0.02 1 578 145 145 TYR C C 172.1 0.30 1 579 145 145 TYR CA C 60.9 0.30 1 580 145 145 TYR CB C 40.3 0.30 1 581 145 145 TYR N N 122.4 0.20 1 582 146 146 LEU H H 8.77 0.02 1 583 146 146 LEU C C 172.1 0.30 1 584 146 146 LEU CA C 58.0 0.30 1 585 146 146 LEU CB C 40.0 0.30 1 586 146 146 LEU N N 121.6 0.20 1 587 147 147 LEU H H 8.53 0.02 1 588 147 147 LEU C C 171.1 0.30 1 589 147 147 LEU CA C 57.0 0.30 1 590 147 147 LEU N N 122.8 0.20 1 591 148 148 ASN H H 7.98 0.02 1 592 148 148 ASN C C 175.0 0.30 1 593 148 148 ASN CA C 54.6 0.30 1 594 148 148 ASN CB C 37.7 0.30 1 595 148 148 ASN N N 117.2 0.20 1 596 149 149 ASN H H 7.13 0.02 1 597 149 149 ASN C C 178.1 0.30 1 598 149 149 ASN CA C 53.1 0.30 1 599 149 149 ASN CB C 38.7 0.30 1 600 149 149 ASN N N 116.3 0.20 1 601 150 150 ASP H H 7.52 0.02 1 602 150 150 ASP C C 174.9 0.30 1 603 150 150 ASP CA C 55.8 0.30 1 604 150 150 ASP CB C 38.4 0.30 1 605 150 150 ASP N N 115.8 0.20 1 606 151 151 LEU H H 8.35 0.02 1 607 151 151 LEU C C 178.2 0.30 5 608 151 151 LEU CA C 53.2 0.30 1 609 151 151 LEU CB C 43.8 0.30 1 610 151 151 LEU N N 115.3 0.20 1 611 152 152 ALA H H 7.48 0.02 1 612 152 152 ALA C C 174.3 0.30 1 613 152 152 ALA CA C 50.6 0.30 1 614 152 152 ALA CB C 19.2 0.30 1 615 152 152 ALA N N 123.8 0.20 1 616 153 153 ASP H H 8.98 0.02 1 617 153 153 ASP C C 175.4 0.30 1 618 153 153 ASP CA C 52.3 0.30 1 619 153 153 ASP CB C 37.9 0.30 1 620 153 153 ASP N N 122.9 0.20 1 621 154 154 VAL H H 7.37 0.02 1 622 154 154 VAL C C 176.3 0.30 1 623 154 154 VAL CA C 60.4 0.30 1 624 154 154 VAL CB C 29.9 0.30 1 625 154 154 VAL N N 113.7 0.20 1 626 155 155 ASP H H 7.11 0.02 1 627 155 155 ASP C C 175.2 0.30 1 628 155 155 ASP CA C 52.2 0.30 1 629 155 155 ASP CB C 40.0 0.30 1 630 155 155 ASP N N 121.4 0.20 1 631 156 156 CYS H H 7.54 0.02 1 632 156 156 CYS CA C 59.3 0.30 1 633 156 156 CYS CB C 26.0 0.30 1 634 156 156 CYS N N 123.6 0.20 1 635 157 157 GLU H H 8.36 0.02 1 636 157 157 GLU C C 171.5 0.30 1 637 157 157 GLU CA C 58.0 0.30 1 638 157 157 GLU CB C 27.7 0.30 1 639 157 157 GLU N N 121.5 0.20 1 640 158 158 ASN H H 7.29 0.02 1 641 158 158 ASN CA C 57.2 0.30 1 642 158 158 ASN CB C 33.6 0.30 4 643 158 158 ASN N N 118.4 0.20 1 644 159 159 TRP C C 177.8 0.30 1 645 160 160 GLU H H 7.53 0.02 1 646 160 160 GLU C C 178.4 0.30 1 647 160 160 GLU CA C 53.3 0.30 1 648 160 160 GLU CB C 32.0 0.30 1 649 160 160 GLU N N 121.9 0.20 1 650 161 161 GLU H H 8.11 0.02 1 651 161 161 GLU C C 174.2 0.30 1 652 161 161 GLU CA C 54.4 0.30 1 653 161 161 GLU CB C 30.1 0.30 1 654 161 161 GLU N N 119.6 0.20 1 655 162 162 ASP H H 9.33 0.02 1 656 162 162 ASP C C 174.9 0.30 1 657 162 162 ASP CA C 55.9 0.30 1 658 162 162 ASP CB C 32.8 0.30 1 659 162 162 ASP N N 126.3 0.20 1 660 163 163 THR H H 8.32 0.02 1 661 163 163 THR CA C 55.0 0.30 1 662 163 163 THR CB C 62.9 0.30 1 663 163 163 THR N N 116.1 0.20 1 664 165 165 PHE C C 174.4 0.30 9 665 166 166 LYS H H 11.70 0.02 9 666 166 166 LYS C C 171.9 0.30 9 667 166 166 LYS CA C 55.4 0.30 9 668 166 166 LYS CB C 29.0 0.30 9 669 166 166 LYS N N 123.8 0.20 9 670 167 167 ASP H H 7.70 0.02 9 671 167 167 ASP CA C 50.3 0.30 9 672 167 167 ASP CB C 43.5 0.30 9 673 167 167 ASP N N 120.5 0.20 9 674 168 168 PRO C C 172.6 0.30 1 675 168 168 PRO CA C 64.1 0.30 1 676 168 168 PRO CB C 32.5 0.30 1 677 169 169 ARG H H 7.93 0.02 1 678 169 169 ARG C C 172.1 0.30 1 679 169 169 ARG CA C 59.0 0.30 1 680 169 169 ARG CB C 28.6 0.30 1 681 169 169 ARG N N 119.1 0.20 1 682 170 170 GLU H H 8.74 0.02 1 683 170 170 GLU C C 171.1 0.30 1 684 170 170 GLU CA C 56.6 0.30 1 685 170 170 GLU CB C 27.3 0.30 1 686 170 170 GLU N N 122.8 0.20 1 687 171 171 LEU H H 9.41 0.02 1 688 171 171 LEU C C 173.2 0.30 1 689 171 171 LEU CA C 57.4 0.30 1 690 171 171 LEU CB C 39.7 0.30 1 691 171 171 LEU N N 119.3 0.20 1 692 172 172 TYR H H 8.21 0.02 1 693 172 172 TYR CA C 60.7 0.30 1 694 172 172 TYR CB C 37.5 0.30 1 695 172 172 TYR N N 120.1 0.20 1 696 173 173 ASP C C 172.9 0.30 1 697 174 174 PHE H H 7.54 0.02 1 698 174 174 PHE C C 171.2 0.30 1 699 174 174 PHE CA C 60.4 0.30 1 700 174 174 PHE CB C 37.8 0.30 1 701 174 174 PHE N N 119.4 0.20 1 702 175 175 LEU H H 7.98 0.02 1 703 175 175 LEU C C 176.2 0.30 1 704 175 175 LEU CA C 59.4 0.30 1 705 175 175 LEU CB C 28.0 0.30 4 706 175 175 LEU N N 118.1 0.20 1 707 176 176 LYS H H 8.02 0.02 1 708 176 176 LYS C C 172.7 0.30 1 709 176 176 LYS CA C 52.5 0.30 1 710 176 176 LYS CB C 40.4 0.30 1 711 176 176 LYS N N 121.4 0.20 1 712 177 177 THR H H 7.90 0.02 1 713 177 177 THR C C 175.6 0.30 1 714 177 177 THR CA C 61.2 0.30 1 715 177 177 THR CB C 62.4 0.30 1 716 177 177 THR N N 116.1 0.20 1 717 178 178 GLU H H 8.35 0.02 1 718 178 178 GLU C C 172.7 0.30 1 719 178 178 GLU CA C 56.6 0.30 1 720 178 178 GLU CB C 29.9 0.30 1 721 178 178 GLU N N 123.2 0.20 1 722 179 179 LYS H H 7.90 0.02 1 723 179 179 LYS CA C 58.1 0.30 1 724 179 179 LYS CB C 31.3 0.30 1 725 179 179 LYS N N 116.6 0.20 1 726 180 180 PRO C C 173.6 0.30 1 727 181 181 GLU H H 8.11 0.02 9 728 181 181 GLU C C 176.4 0.30 9 729 181 181 GLU CA C 59.1 0.30 9 730 181 181 GLU CB C 31.5 0.30 9 731 181 181 GLU N N 116.5 0.20 9 732 182 182 GLU H H 7.19 0.02 9 733 182 182 GLU C C 172.6 0.30 9 734 182 182 GLU CA C 59.9 0.30 9 735 182 182 GLU CB C 36.7 0.30 9 736 182 182 GLU N N 123.7 0.20 9 737 183 183 GLU H H 8.02 0.02 9 738 183 183 GLU C C 173.7 0.30 9 739 183 183 GLU CA C 59.3 0.30 9 740 183 183 GLU CB C 28.3 0.30 9 741 183 183 GLU N N 119.5 0.20 9 742 184 184 LEU H H 7.48 0.02 5 743 184 184 LEU C C 170.1 0.30 5 744 184 184 LEU CA C 57.2 0.30 5 745 184 184 LEU CB C 40.0 0.30 5 746 184 184 LEU N N 122.6 0.20 5 747 185 185 VAL H H 7.98 0.02 9 748 185 185 VAL CA C 61.0 0.30 9 749 185 185 VAL CB C 27.4 0.30 9 750 185 185 VAL N N 121.7 0.20 9 751 188 188 HIS C C 173.6 0.30 1 752 189 189 GLY H H 8.00 0.02 1 753 189 189 GLY C C 175.7 0.30 1 754 189 189 GLY CA C 45.3 0.30 1 755 189 189 GLY N N 104.4 0.20 1 756 190 190 ASP H H 10.70 0.02 1 757 190 190 ASP C C 175.5 0.30 1 758 190 190 ASP CA C 52.9 0.30 1 759 190 190 ASP CB C 40.9 0.30 1 760 190 190 ASP N N 132.3 0.20 1 761 191 191 LEU H H 8.77 0.02 1 762 191 191 LEU C C 173.2 0.30 1 763 191 191 LEU CA C 56.1 0.30 1 764 191 191 LEU CB C 42.5 0.30 1 765 191 191 LEU N N 126.3 0.20 1 766 192 192 GLY H H 8.19 0.02 1 767 192 192 GLY C C 173.9 0.30 9 768 192 192 GLY CA C 44.7 0.30 1 769 192 192 GLY N N 111.7 0.20 1 770 193 193 ASP H H 8.32 0.02 1 771 193 193 ASP C C 176.0 0.30 5 772 193 193 ASP CA C 55.5 0.30 1 773 193 193 ASP CB C 39.0 0.30 1 774 193 193 ASP N N 118.2 0.20 1 775 194 194 SER H H 7.79 0.02 1 776 194 194 SER C C 173.7 0.30 1 777 194 194 SER CA C 58.2 0.30 1 778 194 194 SER CB C 73.0 0.30 5 779 194 194 SER N N 110.9 0.20 1 780 195 195 ASN H H 8.00 0.02 5 781 195 195 ASN C C 178.2 0.30 5 782 195 195 ASN CA C 52.1 0.30 5 783 195 195 ASN CB C 38.9 0.30 5 784 195 195 ASN N N 113.3 0.20 5 785 196 196 ILE H H 6.45 0.02 1 786 196 196 ILE C C 176.6 0.30 1 787 196 196 ILE CA C 60.1 0.30 1 788 196 196 ILE CB C 41.5 0.30 1 789 196 196 ILE N N 116.1 0.20 1 790 197 197 PHE H H 8.65 0.02 1 791 197 197 PHE C C 175.0 0.30 1 792 197 197 PHE CA C 55.8 0.30 1 793 197 197 PHE CB C 40.3 0.30 1 794 197 197 PHE N N 127.0 0.20 1 795 198 198 VAL H H 9.25 0.02 1 796 198 198 VAL C C 174.6 0.30 1 797 198 198 VAL CA C 58.9 0.30 1 798 198 198 VAL CB C 35.2 0.30 1 799 198 198 VAL N N 117.8 0.20 1 800 199 199 LYS H H 8.82 0.02 9 801 199 199 LYS C C 174.3 0.30 9 802 199 199 LYS CA C 56.0 0.30 9 803 199 199 LYS CB C 33.9 0.30 9 804 199 199 LYS N N 123.2 0.20 9 805 200 200 ASP H H 9.56 0.02 1 806 200 200 ASP C C 174.4 0.30 1 807 200 200 ASP CA C 55.1 0.30 1 808 200 200 ASP CB C 38.9 0.30 1 809 200 200 ASP N N 129.4 0.20 1 810 201 201 GLY H H 8.62 0.02 1 811 201 201 GLY C C 177.3 0.30 1 812 201 201 GLY CA C 44.9 0.30 1 813 201 201 GLY N N 103.6 0.20 1 814 202 202 LYS H H 7.54 0.02 1 815 202 202 LYS C C 175.1 0.30 1 816 202 202 LYS CA C 53.2 0.30 1 817 202 202 LYS CB C 34.6 0.30 1 818 202 202 LYS N N 120.6 0.20 1 819 203 203 VAL H H 8.78 0.02 1 820 203 203 VAL C C 173.8 0.30 1 821 203 203 VAL CA C 64.1 0.30 1 822 203 203 VAL CB C 30.7 0.30 4 823 203 203 VAL N N 122.4 0.20 1 824 204 204 SER H H 9.65 0.02 1 825 204 204 SER C C 175.2 0.30 1 826 204 204 SER CA C 57.5 0.30 1 827 204 204 SER CB C 65.1 0.30 1 828 204 204 SER N N 122.2 0.20 1 829 205 205 GLY H H 7.12 0.02 1 830 205 205 GLY C C 174.0 0.30 1 831 205 205 GLY CA C 46.0 0.30 1 832 205 205 GLY N N 111.5 0.20 1 833 206 206 PHE H H 7.65 0.02 1 834 206 206 PHE C C 176.4 0.30 1 835 206 206 PHE CA C 57.0 0.30 1 836 206 206 PHE CB C 43.7 0.30 1 837 206 206 PHE N N 118.6 0.20 1 838 207 207 ILE H H 7.88 0.02 1 839 207 207 ILE C C 171.7 0.30 1 840 207 207 ILE CA C 59.3 0.30 1 841 207 207 ILE CB C 40.9 0.30 1 842 207 207 ILE N N 109.6 0.20 1 843 208 208 ASP H H 8.39 0.02 1 844 208 208 ASP C C 175.2 0.30 1 845 208 208 ASP CA C 54.6 0.30 1 846 208 208 ASP CB C 37.0 0.30 1 847 208 208 ASP N N 118.8 0.20 1 848 209 209 LEU H H 7.63 0.02 1 849 209 209 LEU C C 171.1 0.30 1 850 209 209 LEU CA C 54.4 0.30 1 851 209 209 LEU CB C 41.9 0.30 1 852 209 209 LEU N N 118.6 0.20 1 853 210 210 GLY H H 9.08 0.02 9 854 210 210 GLY CA C 47.3 0.30 9 855 210 210 GLY N N 112.7 0.20 1 856 211 211 ARG C C 175.8 0.30 1 857 212 212 SER H H 7.13 0.02 1 858 212 212 SER C C 176.7 0.30 1 859 212 212 SER CA C 58.1 0.30 1 860 212 212 SER CB C 64.5 0.30 1 861 212 212 SER N N 118.9 0.20 1 862 213 213 GLY H H 7.51 0.02 1 863 213 213 GLY C C 178.6 0.30 1 864 213 213 GLY CA C 43.9 0.30 1 865 213 213 GLY N N 104.2 0.20 1 866 214 214 ARG H H 8.09 0.02 1 867 214 214 ARG C C 174.8 0.30 1 868 214 214 ARG CA C 55.1 0.30 1 869 214 214 ARG CB C 31.1 0.30 1 870 214 214 ARG N N 119.1 0.20 1 871 215 215 ALA H H 9.05 0.02 1 872 215 215 ALA C C 175.2 0.30 1 873 215 215 ALA CA C 51.7 0.30 1 874 215 215 ALA CB C 20.5 0.30 1 875 215 215 ALA N N 123.0 0.20 1 876 216 216 ASP H H 8.77 0.02 1 877 216 216 ASP C C 171.8 0.30 1 878 216 216 ASP CA C 54.8 0.30 1 879 216 216 ASP CB C 45.0 0.30 1 880 216 216 ASP N N 118.0 0.20 1 881 217 217 LYS H H 7.87 0.02 1 882 217 217 LYS CA C 57.8 0.30 1 883 217 217 LYS CB C 32.1 0.30 1 884 217 217 LYS N N 123.4 0.20 1 885 218 218 TRP C C 174.8 0.30 9 886 219 219 TYR H H 6.16 0.02 9 887 219 219 TYR CA C 57.1 0.30 9 888 219 219 TYR CB C 40.8 0.30 9 889 219 219 TYR N N 111.3 0.20 9 890 220 220 ASP C C 170.6 0.30 1 891 221 221 ILE H H 6.70 0.02 1 892 221 221 ILE C C 173.3 0.30 1 893 221 221 ILE CA C 66.2 0.30 1 894 221 221 ILE CB C 37.5 0.30 1 895 221 221 ILE N N 118.2 0.20 1 896 222 222 ALA H H 8.82 0.02 1 897 222 222 ALA C C 174.1 0.30 1 898 222 222 ALA CA C 55.5 0.30 1 899 222 222 ALA CB C 19.6 0.30 1 900 222 222 ALA N N 123.5 0.20 1 901 223 223 PHE H H 7.97 0.02 1 902 223 223 PHE C C 170.9 0.30 1 903 223 223 PHE CA C 61.0 0.30 1 904 223 223 PHE CB C 40.9 0.30 4 905 223 223 PHE N N 119.9 0.20 1 906 224 224 CYS H H 7.91 0.02 1 907 224 224 CYS C C 174.1 0.30 1 908 224 224 CYS CA C 63.3 0.30 1 909 224 224 CYS N N 120.4 0.20 1 910 225 225 VAL H H 8.08 0.02 1 911 225 225 VAL C C 173.8 0.30 1 912 225 225 VAL CA C 67.1 0.30 1 913 225 225 VAL CB C 30.6 0.30 1 914 225 225 VAL N N 120.6 0.20 1 915 226 226 ARG H H 8.37 0.02 1 916 226 226 ARG C C 172.0 0.30 1 917 226 226 ARG CA C 59.3 0.30 1 918 226 226 ARG CB C 29.9 0.30 1 919 226 226 ARG N N 120.3 0.20 1 920 227 227 SER H H 7.82 0.02 1 921 227 227 SER C C 174.2 0.30 1 922 227 227 SER CA C 60.9 0.30 1 923 227 227 SER CB C 61.7 0.30 1 924 227 227 SER N N 115.2 0.20 1 925 228 228 ILE H H 8.61 0.02 1 926 228 228 ILE C C 175.5 0.30 1 927 228 228 ILE CA C 65.4 0.30 1 928 228 228 ILE CB C 37.5 0.30 1 929 228 228 ILE N N 122.9 0.20 1 930 229 229 ARG H H 8.39 0.02 1 931 229 229 ARG C C 173.4 0.30 1 932 229 229 ARG CA C 59.4 0.30 1 933 229 229 ARG CB C 29.1 0.30 1 934 229 229 ARG N N 118.2 0.20 1 935 230 230 GLU H H 7.51 0.02 1 936 230 230 GLU C C 181.4 0.30 1 937 230 230 GLU CA C 57.9 0.30 1 938 230 230 GLU CB C 29.1 0.30 1 939 230 230 GLU N N 118.3 0.20 1 940 231 231 ASP H H 7.67 0.02 1 941 231 231 ASP C C 173.9 0.30 1 942 231 231 ASP CA C 61.2 0.30 9 943 231 231 ASP CB C 36.8 0.30 1 944 231 231 ASP N N 118.6 0.20 1 945 232 232 ILE H H 7.94 0.02 1 946 232 232 ILE C C 172.9 0.30 1 947 232 232 ILE CA C 61.9 0.30 1 948 232 232 ILE CB C 37.7 0.30 1 949 232 232 ILE N N 119.7 0.20 1 950 233 233 GLY H H 8.24 0.02 1 951 233 233 GLY C C 176.4 0.30 1 952 233 233 GLY CA C 46.1 0.30 1 953 233 233 GLY N N 107.8 0.20 1 954 234 234 GLU H H 7.08 0.02 1 955 234 234 GLU CA C 55.5 0.30 1 956 234 234 GLU CB C 31.0 0.30 1 957 234 234 GLU N N 118.2 0.20 1 958 236 236 GLN C C 172.8 0.30 1 959 237 237 TYR H H 7.65 0.02 1 960 237 237 TYR C C 173.3 0.30 1 961 237 237 TYR CA C 61.4 0.30 1 962 237 237 TYR CB C 36.7 0.30 1 963 237 237 TYR N N 119.0 0.20 1 964 238 238 VAL H H 7.60 0.02 1 965 238 238 VAL C C 172.9 0.30 1 966 238 238 VAL CA C 66.6 0.30 1 967 238 238 VAL N N 122.6 0.20 1 968 239 239 GLU H H 7.70 0.02 1 969 239 239 GLU C C 176.1 0.30 1 970 239 239 GLU CA C 59.4 0.30 1 971 239 239 GLU N N 118.6 0.20 1 972 240 240 LEU H H 8.84 0.02 1 973 240 240 LEU C C 174.4 0.30 1 974 240 240 LEU CA C 60.9 0.30 1 975 240 240 LEU CB C 36.9 0.30 4 976 240 240 LEU N N 120.6 0.20 1 977 241 241 PHE H H 7.52 0.02 1 978 241 241 PHE C C 175.4 0.30 1 979 241 241 PHE CA C 63.0 0.30 1 980 241 241 PHE CB C 36.7 0.30 1 981 241 241 PHE N N 115.3 0.20 1 982 242 242 PHE H H 6.63 0.02 1 983 242 242 PHE CA C 57.0 0.30 1 984 242 242 PHE CB C 42.2 0.30 1 985 242 242 PHE N N 116.8 0.20 1 986 243 243 ASP C C 174.1 0.30 1 987 244 244 LEU H H 7.72 0.02 1 988 244 244 LEU C C 173.9 0.30 1 989 244 244 LEU CA C 56.2 0.30 1 990 244 244 LEU CB C 29.1 0.30 1 991 244 244 LEU N N 119.3 0.20 1 992 245 245 LEU H H 8.44 0.02 1 993 245 245 LEU C C 172.6 0.30 1 994 245 245 LEU CA C 55.3 0.30 1 995 245 245 LEU CB C 34.1 0.30 1 996 245 245 LEU N N 121.8 0.20 1 997 246 246 GLY H H 8.00 0.02 1 998 246 246 GLY C C 176.0 0.30 1 999 246 246 GLY CA C 45.6 0.30 1 1000 246 246 GLY N N 108.6 0.20 1 1001 247 247 ILE H H 7.27 0.02 1 1002 247 247 ILE C C 176.5 0.30 1 1003 247 247 ILE CA C 58.6 0.30 1 1004 247 247 ILE CB C 41.3 0.30 1 1005 247 247 ILE N N 114.6 0.20 1 1006 248 248 LYS H H 8.17 0.02 1 1007 248 248 LYS CA C 52.1 0.30 1 1008 248 248 LYS CB C 31.0 0.30 4 1009 248 248 LYS N N 123.7 0.20 1 1010 251 251 TRP C C 173.7 0.30 1 1011 252 252 GLU H H 8.87 0.02 9 1012 252 252 GLU C C 172.8 0.30 9 1013 252 252 GLU CA C 60.6 0.30 9 1014 252 252 GLU CB C 27.6 0.30 9 1015 252 252 GLU N N 118.2 0.20 9 1016 253 253 LYS H H 7.69 0.02 9 1017 253 253 LYS C C 174.2 0.30 9 1018 253 253 LYS CA C 58.1 0.30 9 1019 253 253 LYS CB C 30.2 0.30 9 1020 253 253 LYS N N 117.9 0.20 9 1021 254 254 ILE H H 7.34 0.02 1 1022 254 254 ILE C C 171.1 0.30 1 1023 254 254 ILE CA C 64.3 0.30 1 1024 254 254 ILE N N 118.5 0.20 1 1025 255 255 LYS H H 7.99 0.02 1 1026 255 255 LYS C C 171.6 0.30 1 1027 255 255 LYS CA C 59.4 0.30 1 1028 255 255 LYS CB C 28.0 0.30 4 1029 255 255 LYS N N 118.0 0.20 1 1030 256 256 TYR H H 7.56 0.02 1 1031 256 256 TYR C C 175.0 0.30 1 1032 256 256 TYR CA C 62.9 0.30 1 1033 256 256 TYR CB C 37.1 0.30 1 1034 256 256 TYR N N 119.9 0.20 1 1035 257 257 TYR H H 8.06 0.02 1 1036 257 257 TYR C C 173.1 0.30 1 1037 257 257 TYR CA C 63.9 0.30 1 1038 257 257 TYR CB C 37.6 0.30 1 1039 257 257 TYR N N 116.3 0.20 1 1040 258 258 ILE H H 7.59 0.02 1 1041 258 258 ILE C C 171.3 0.30 1 1042 258 258 ILE CA C 65.4 0.30 1 1043 258 258 ILE CB C 36.4 0.30 1 1044 258 258 ILE N N 119.2 0.20 1 1045 259 259 LEU H H 7.64 0.02 1 1046 259 259 LEU C C 176.9 0.30 5 1047 259 259 LEU CA C 56.9 0.30 1 1048 259 259 LEU CB C 40.2 0.30 1 1049 259 259 LEU N N 120.9 0.20 1 1050 260 260 LEU H H 8.41 0.02 1 1051 260 260 LEU CA C 58.3 0.30 4 1052 260 260 LEU CB C 29.0 0.30 1 1053 260 260 LEU N N 120.8 0.20 1 1054 262 262 GLU C C 176.5 0.30 1 1055 263 263 LEU H H 8.16 0.02 5 1056 263 263 LEU C C 178.2 0.30 5 1057 263 263 LEU CA C 57.2 0.30 5 1058 263 263 LEU CB C 40.7 0.30 5 1059 263 263 LEU N N 121.2 0.20 5 1060 264 264 PHE H H 7.78 0.02 9 1061 264 264 PHE CA C 56.0 0.30 9 1062 264 264 PHE CB C 42.1 0.30 9 1063 264 264 PHE N N 126.8 0.20 9 stop_ loop_ _Atom_shift_assign_ID_ambiguity 37 '252,' '368,' '401,689' '430,801' ',' ',' ',' ',' '738,' '739,' '740,' '741,' '743,' '374,' stop_ save_