data_16984 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of D-allose binding protein from Escherichia coli in the complex form with D-allose ; _BMRB_accession_number 16984 _BMRB_flat_file_name bmr16984.str _Entry_type original _Submission_date 2010-06-08 _Accession_date 2010-06-08 _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 Millet Oscar . . 2 Castano David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 224 "13C chemical shifts" 690 "15N chemical shifts" 224 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-03-24 update BMRB 'update entry citation' 2010-08-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16982 'Apo form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone chemical shifts assignments of D: -allose binding protein in the free form and in complex with D: -allose.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20711759 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Castano David . . 2 Millet Oscar . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 5 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31 _Page_last 34 _Year 2011 _Details . loop_ _Keyword 'bacterial chemotaxis' 'D-allose binding protein' 'hinge motion' 'periplasmic binding protein' 'protein dynamics' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ALBP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ALBP $ALBP D-allose $AOS stop_ _System_molecular_weight 30385 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ALBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ALBP _Molecular_mass 30385 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 288 _Mol_residue_sequence ; AAEYAVVLKTLSNPFWVDMK KGIEDEAKTLGVSVDIFASP SEGDFQSQLQLFEDLSNKNY KGIAFAPLSSVNLVMPVARA WKKGIYLVNLDEKIDMDNLK KAGGNVEAFVTTDNVAVGAK GASFIIDKLGAEGGEVAIIE GKAGNASGEARRNGATEAFK KASQIKLVASQPADWDRIKA LDVATNVLQRNPNIKAIYCA NDTMAMGVAQAVANAGKTGK VLVVGTDGIPEARKMVEAGQ MTATVAQNPADIGATGLKLM VDAEKSGKVIPLDKAPEFKL VDSILVTQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ALA 3 GLU 4 TYR 5 ALA 6 VAL 7 VAL 8 LEU 9 LYS 10 THR 11 LEU 12 SER 13 ASN 14 PRO 15 PHE 16 TRP 17 VAL 18 ASP 19 MET 20 LYS 21 LYS 22 GLY 23 ILE 24 GLU 25 ASP 26 GLU 27 ALA 28 LYS 29 THR 30 LEU 31 GLY 32 VAL 33 SER 34 VAL 35 ASP 36 ILE 37 PHE 38 ALA 39 SER 40 PRO 41 SER 42 GLU 43 GLY 44 ASP 45 PHE 46 GLN 47 SER 48 GLN 49 LEU 50 GLN 51 LEU 52 PHE 53 GLU 54 ASP 55 LEU 56 SER 57 ASN 58 LYS 59 ASN 60 TYR 61 LYS 62 GLY 63 ILE 64 ALA 65 PHE 66 ALA 67 PRO 68 LEU 69 SER 70 SER 71 VAL 72 ASN 73 LEU 74 VAL 75 MET 76 PRO 77 VAL 78 ALA 79 ARG 80 ALA 81 TRP 82 LYS 83 LYS 84 GLY 85 ILE 86 TYR 87 LEU 88 VAL 89 ASN 90 LEU 91 ASP 92 GLU 93 LYS 94 ILE 95 ASP 96 MET 97 ASP 98 ASN 99 LEU 100 LYS 101 LYS 102 ALA 103 GLY 104 GLY 105 ASN 106 VAL 107 GLU 108 ALA 109 PHE 110 VAL 111 THR 112 THR 113 ASP 114 ASN 115 VAL 116 ALA 117 VAL 118 GLY 119 ALA 120 LYS 121 GLY 122 ALA 123 SER 124 PHE 125 ILE 126 ILE 127 ASP 128 LYS 129 LEU 130 GLY 131 ALA 132 GLU 133 GLY 134 GLY 135 GLU 136 VAL 137 ALA 138 ILE 139 ILE 140 GLU 141 GLY 142 LYS 143 ALA 144 GLY 145 ASN 146 ALA 147 SER 148 GLY 149 GLU 150 ALA 151 ARG 152 ARG 153 ASN 154 GLY 155 ALA 156 THR 157 GLU 158 ALA 159 PHE 160 LYS 161 LYS 162 ALA 163 SER 164 GLN 165 ILE 166 LYS 167 LEU 168 VAL 169 ALA 170 SER 171 GLN 172 PRO 173 ALA 174 ASP 175 TRP 176 ASP 177 ARG 178 ILE 179 LYS 180 ALA 181 LEU 182 ASP 183 VAL 184 ALA 185 THR 186 ASN 187 VAL 188 LEU 189 GLN 190 ARG 191 ASN 192 PRO 193 ASN 194 ILE 195 LYS 196 ALA 197 ILE 198 TYR 199 CYS 200 ALA 201 ASN 202 ASP 203 THR 204 MET 205 ALA 206 MET 207 GLY 208 VAL 209 ALA 210 GLN 211 ALA 212 VAL 213 ALA 214 ASN 215 ALA 216 GLY 217 LYS 218 THR 219 GLY 220 LYS 221 VAL 222 LEU 223 VAL 224 VAL 225 GLY 226 THR 227 ASP 228 GLY 229 ILE 230 PRO 231 GLU 232 ALA 233 ARG 234 LYS 235 MET 236 VAL 237 GLU 238 ALA 239 GLY 240 GLN 241 MET 242 THR 243 ALA 244 THR 245 VAL 246 ALA 247 GLN 248 ASN 249 PRO 250 ALA 251 ASP 252 ILE 253 GLY 254 ALA 255 THR 256 GLY 257 LEU 258 LYS 259 LEU 260 MET 261 VAL 262 ASP 263 ALA 264 GLU 265 LYS 266 SER 267 GLY 268 LYS 269 VAL 270 ILE 271 PRO 272 LEU 273 ASP 274 LYS 275 ALA 276 PRO 277 GLU 278 PHE 279 LYS 280 LEU 281 VAL 282 ASP 283 SER 284 ILE 285 LEU 286 VAL 287 THR 288 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-21 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16982 ALBP 100.00 288 100.00 100.00 0.00e+00 PDB 1GUB "Hinge-Bending Motion Of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations" 99.65 288 100.00 100.00 0.00e+00 PDB 1GUD "Hinge-Bending Motion Of D-Allose Binding Protein From Escherichia Coli: Three Open Conformations" 100.00 288 100.00 100.00 0.00e+00 PDB 1RPJ "Crystal Structure Of D-Allose Binding Protein From Escherichia Coli" 100.00 288 100.00 100.00 0.00e+00 DBJ BAE78091 "D-allose transporter subunit [Escherichia coli str. K12 substr. W3110]" 100.00 311 100.00 100.00 0.00e+00 DBJ BAG79910 "D-allose ABC transporter substrate binding component [Escherichia coli SE11]" 100.00 311 99.31 99.65 0.00e+00 DBJ BAI33528 "D-allose-binding periplasmic protein [Escherichia coli O103:H2 str. 12009]" 100.00 311 99.31 100.00 0.00e+00 DBJ BAI57509 "D-allose ABC transporter substrate binding component [Escherichia coli SE15]" 100.00 311 99.65 99.65 0.00e+00 DBJ BAJ45803 "D-allose transporter subunit [Escherichia coli DH1]" 100.00 311 99.65 99.65 0.00e+00 EMBL CAP78562 "D-allose-binding periplasmic protein [Escherichia coli LF82]" 100.00 313 99.65 99.65 0.00e+00 EMBL CAQ34437 "alsB, subunit of D-allose ABC transporter [Escherichia coli BL21(DE3)]" 100.00 311 100.00 100.00 0.00e+00 EMBL CAR05747 "D-allose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli S88]" 100.00 311 99.65 99.65 0.00e+00 EMBL CAR10927 "D-allose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli ED1a]" 100.00 311 98.96 99.31 0.00e+00 EMBL CAR20617 "D-allose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli IAI39]" 100.00 311 99.65 99.65 0.00e+00 GB AAA96987 "ORF_f311 [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 100.00 100.00 0.00e+00 GB AAC77049 "D-allose ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 100.00 100.00 0.00e+00 GB AAN83519 "D-allose-binding periplasmic protein precursor [Escherichia coli CFT073]" 100.00 313 99.65 99.65 0.00e+00 GB ABE10091 "D-allose-binding periplasmic protein precursor [Escherichia coli UTI89]" 100.00 313 99.65 99.65 0.00e+00 GB ABG72275 "D-allose-binding periplasmic protein precursor [Escherichia coli 536]" 100.00 313 99.65 99.65 0.00e+00 REF NP_418512 "D-allose ABC transporter periplasmic binding protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 311 100.00 100.00 0.00e+00 REF WP_001046184 "cytochrome C [Escherichia coli]" 100.00 311 98.96 99.65 0.00e+00 REF WP_001046185 "cytochrome C [Escherichia coli]" 100.00 311 99.65 99.65 0.00e+00 REF WP_001046186 "D-allose-binding periplasmic protein [Escherichia coli]" 100.00 311 99.31 100.00 0.00e+00 REF WP_001046187 "MULTISPECIES: D-allose-binding periplasmic protein [Proteobacteria]" 100.00 311 100.00 100.00 0.00e+00 SP P39265 "RecName: Full=D-allose-binding periplasmic protein; Short=ALBP; Flags: Precursor" 100.00 311 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_AOS _Saveframe_category ligand _Mol_type "non-polymer (D-SACCHARIDE)" _Name_common "AOS (D-ALLOSE)" _BMRB_code . _PDB_code AOS _Molecular_mass 180.156 _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 Mon Dec 5 11:57:26 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? C3 C3 C . 0 . ? O3 O3 O . 0 . ? C4 C4 C . 0 . ? O4 O4 O . 0 . ? C5 C5 C . 0 . ? O5 O5 O . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? HO2 HO2 H . 0 . ? H3 H3 H . 0 . ? HO3 HO3 H . 0 . ? H4 H4 H . 0 . ? HO4 HO4 H . 0 . ? H5 H5 H . 0 . ? HO5 HO5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HO6 HO6 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 DOUB C1 O1 ? ? SING C1 C2 ? ? SING C1 H1 ? ? SING C2 O2 ? ? SING C2 C3 ? ? SING C2 H2 ? ? SING O2 HO2 ? ? SING C3 O3 ? ? SING C3 C4 ? ? SING C3 H3 ? ? SING O3 HO3 ? ? SING C4 O4 ? ? SING C4 C5 ? ? SING C4 H4 ? ? SING O4 HO4 ? ? SING C5 O5 ? ? SING C5 C6 ? ? SING C5 H5 ? ? SING O5 HO5 ? ? SING C6 O6 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING O6 HO6 ? ? 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 $ALBP 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $ALBP 'recombinant technology' . Escherichia coli . pET11d 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 $ALBP 800 uM '[U-100% 13C; U-100% 15N; U-80% 2H]' $AOS 5 mM 'natural abundance' NaCl 150 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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' 150 . mM pH 7.1 . pH pressure 1 . atm temperature 310 . 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 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 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_ _Experiment_label '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D CBCA(CO)NH' 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 ALBP _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 ALA C C 171.429 0.4 1 2 1 1 ALA CA C 48.980 0.20 1 3 1 1 ALA CB C 15.750 0.12 1 4 2 2 ALA H H 8.356 0.03 1 5 2 2 ALA CA C 48.672 0.20 1 6 2 2 ALA CB C 16.675 0.12 1 7 2 2 ALA N N 123.042 0.25 1 8 3 3 GLU H H 8.200 0.03 1 9 3 3 GLU C C 172.754 0.4 1 10 3 3 GLU CA C 54.526 0.20 1 11 3 3 GLU CB C 29.033 0.12 1 12 3 3 GLU N N 117.869 0.25 1 13 4 4 TYR H H 7.833 0.03 1 14 4 4 TYR CA C 53.740 0.20 1 15 4 4 TYR CB C 39.094 0.12 1 16 4 4 TYR N N 113.678 0.25 1 17 5 5 ALA H H 8.398 0.03 1 18 5 5 ALA CA C 46.216 0.20 1 19 5 5 ALA CB C 17.873 0.12 1 20 5 5 ALA N N 121.292 0.25 1 21 6 6 VAL H H 8.841 0.03 1 22 6 6 VAL CA C 56.760 0.20 1 23 6 6 VAL CB C 31.903 0.12 1 24 6 6 VAL N N 117.727 0.25 1 25 7 7 VAL H H 9.259 0.03 1 26 7 7 VAL C C 173.625 0.4 1 27 7 7 VAL CA C 57.903 0.20 1 28 7 7 VAL CB C 30.363 0.12 1 29 7 7 VAL N N 126.856 0.25 1 30 8 8 LEU H H 9.114 0.03 1 31 8 8 LEU CA C 49.282 0.20 1 32 8 8 LEU CB C 39.331 0.12 1 33 8 8 LEU N N 124.648 0.25 1 34 10 10 THR CA C 56.700 0.20 1 35 10 10 THR CB C 65.500 0.12 1 36 11 11 LEU H H 8.173 0.03 1 37 11 11 LEU C C 172.754 0.4 1 38 11 11 LEU CA C 55.267 0.20 1 39 11 11 LEU CB C 44.310 0.12 1 40 11 11 LEU N N 125.228 0.25 1 41 12 12 SER H H 8.074 0.03 1 42 12 12 SER C C 175.820 0.4 1 43 12 12 SER CA C 56.566 0.20 1 44 12 12 SER CB C 60.331 0.12 1 45 12 12 SER N N 113.857 0.25 1 46 13 13 ASN H H 7.088 0.03 1 47 13 13 ASN CA C 55.630 0.20 1 48 13 13 ASN CB C 38.225 0.12 1 49 13 13 ASN N N 120.921 0.25 1 50 14 14 PRO CA C 61.489 0.20 1 51 14 14 PRO CB C 29.871 0.12 1 52 15 15 PHE H H 8.227 0.03 1 53 15 15 PHE CA C 58.400 0.20 1 54 15 15 PHE CB C 36.639 0.12 1 55 15 15 PHE N N 119.690 0.25 1 56 16 16 TRP C C 170.124 0.4 1 57 16 16 TRP CA C 55.056 0.20 1 58 17 17 VAL H H 7.198 0.03 1 59 17 17 VAL C C 169.709 0.4 1 60 17 17 VAL CA C 63.422 0.20 1 61 17 17 VAL CB C 28.151 0.12 1 62 17 17 VAL N N 120.904 0.25 1 63 18 18 ASP H H 7.918 0.03 1 64 18 18 ASP C C 168.813 0.4 1 65 18 18 ASP CA C 53.967 0.20 1 66 18 18 ASP CB C 37.151 0.12 1 67 18 18 ASP N N 120.356 0.25 1 68 19 19 MET H H 7.350 0.03 1 69 19 19 MET C C 171.031 0.4 1 70 19 19 MET CA C 56.581 0.20 1 71 19 19 MET CB C 27.798 0.12 1 72 19 19 MET N N 119.804 0.25 1 73 20 20 LYS H H 8.195 0.03 1 74 20 20 LYS CA C 57.181 0.20 1 75 20 20 LYS CB C 28.932 0.12 1 76 20 20 LYS N N 119.750 0.25 1 77 21 21 LYS H H 7.792 0.03 1 78 21 21 LYS C C 169.693 0.4 1 79 21 21 LYS CA C 56.035 0.20 1 80 21 21 LYS CB C 28.511 0.12 1 81 21 21 LYS N N 118.161 0.25 1 82 22 22 GLY H H 7.901 0.03 1 83 22 22 GLY CA C 43.768 0.20 1 84 22 22 GLY N N 104.356 0.25 1 85 23 23 ILE H H 8.486 0.03 1 86 23 23 ILE CA C 59.003 0.20 1 87 23 23 ILE CB C 36.762 0.12 1 88 23 23 ILE N N 118.985 0.25 1 89 24 24 GLU H H 8.609 0.03 1 90 24 24 GLU C C 167.962 0.4 1 91 24 24 GLU CA C 56.776 0.20 1 92 24 24 GLU CB C 26.085 0.12 1 93 24 24 GLU N N 118.129 0.25 1 94 25 25 ASP H H 8.569 0.03 1 95 25 25 ASP C C 169.231 0.4 1 96 25 25 ASP CA C 54.327 0.20 1 97 25 25 ASP CB C 36.772 0.12 1 98 25 25 ASP N N 119.533 0.25 1 99 26 26 GLU H H 7.930 0.03 1 100 26 26 GLU C C 170.186 0.4 1 101 26 26 GLU CA C 54.946 0.20 1 102 26 26 GLU CB C 24.904 0.12 1 103 26 26 GLU N N 122.594 0.25 1 104 27 27 ALA H H 8.909 0.03 1 105 27 27 ALA C C 168.405 0.4 1 106 27 27 ALA CA C 52.511 0.20 1 107 27 27 ALA CB C 14.159 0.12 1 108 27 27 ALA N N 122.066 0.25 1 109 28 28 LYS H H 7.475 0.03 1 110 28 28 LYS C C 168.374 0.4 1 111 28 28 LYS CA C 55.958 0.20 1 112 28 28 LYS CB C 28.497 0.12 1 113 28 28 LYS N N 116.310 0.25 1 114 29 29 THR H H 7.696 0.03 1 115 29 29 THR CA C 62.879 0.20 1 116 29 29 THR CB C 65.385 0.12 1 117 29 29 THR N N 117.211 0.25 1 118 30 30 LEU H H 8.459 0.03 1 119 30 30 LEU C C 170.571 0.4 1 120 30 30 LEU CA C 52.518 0.20 1 121 30 30 LEU CB C 39.816 0.12 1 122 30 30 LEU N N 118.945 0.25 1 123 31 31 GLY H H 8.077 0.03 1 124 31 31 GLY C C 172.766 0.4 1 125 31 31 GLY CA C 43.383 0.20 1 126 31 31 GLY N N 108.544 0.25 1 127 32 32 VAL H H 8.801 0.03 1 128 32 32 VAL CA C 58.401 0.20 1 129 32 32 VAL CB C 31.868 0.12 1 130 32 32 VAL N N 117.633 0.25 1 131 33 33 SER H H 8.601 0.03 1 132 33 33 SER C C 171.957 0.4 1 133 33 33 SER CA C 53.343 0.20 1 134 33 33 SER CB C 61.924 0.12 1 135 33 33 SER N N 115.871 0.25 1 136 34 34 VAL H H 8.473 0.03 1 137 34 34 VAL C C 174.344 0.4 1 138 34 34 VAL CA C 55.753 0.20 1 139 34 34 VAL CB C 32.316 0.12 1 140 34 34 VAL N N 118.964 0.25 1 141 35 35 ASP H H 8.694 0.03 1 142 35 35 ASP C C 174.063 0.4 1 143 35 35 ASP CA C 49.987 0.20 1 144 35 35 ASP CB C 40.607 0.12 1 145 35 35 ASP N N 127.000 0.25 1 146 36 36 ILE H H 8.306 0.03 1 147 36 36 ILE C C 174.063 0.4 1 148 36 36 ILE CA C 57.436 0.20 1 149 36 36 ILE CB C 35.393 0.12 1 150 36 36 ILE N N 121.468 0.25 1 151 37 37 PHE H H 9.260 0.03 1 152 37 37 PHE C C 174.813 0.4 1 153 37 37 PHE CA C 53.120 0.20 1 154 37 37 PHE CB C 41.308 0.12 1 155 37 37 PHE N N 125.996 0.25 1 156 38 38 ALA H H 8.609 0.03 1 157 38 38 ALA C C 172.759 0.4 1 158 38 38 ALA CA C 48.047 0.20 1 159 38 38 ALA CB C 18.950 0.12 1 160 38 38 ALA N N 119.850 0.25 1 161 39 39 SER H H 7.562 0.03 1 162 39 39 SER CA C 55.368 0.20 1 163 39 39 SER CB C 59.770 0.12 1 164 39 39 SER N N 115.041 0.25 1 165 40 40 PRO C C 171.878 0.4 1 166 40 40 PRO CA C 62.430 0.20 1 167 40 40 PRO CB C 28.770 0.12 1 168 41 41 SER H H 7.600 0.03 1 169 41 41 SER CA C 53.922 0.20 1 170 41 41 SER CB C 63.143 0.12 1 171 41 41 SER N N 109.406 0.25 1 172 42 42 GLU CA C 54.960 0.20 1 173 42 42 GLU CB C 26.560 0.12 1 174 43 43 GLY H H 7.356 0.03 1 175 43 43 GLY C C 173.184 0.4 1 176 43 43 GLY CA C 43.377 0.20 1 177 43 43 GLY N N 102.933 0.25 1 178 44 44 ASP H H 7.903 0.03 1 179 44 44 ASP C C 174.070 0.4 1 180 44 44 ASP CA C 55.385 0.20 1 181 44 44 ASP CB C 31.397 0.12 1 182 44 44 ASP N N 110.806 0.25 1 183 45 45 PHE H H 8.609 0.03 1 184 45 45 PHE C C 174.508 0.4 1 185 45 45 PHE CA C 55.353 0.20 1 186 45 45 PHE CB C 40.530 0.12 1 187 45 45 PHE N N 115.731 0.25 1 188 46 46 GLN H H 9.277 0.03 1 189 46 46 GLN CA C 54.752 0.20 1 190 46 46 GLN CB C 26.907 0.12 1 191 46 46 GLN N N 113.949 0.25 1 192 51 51 LEU H H 8.180 0.03 1 193 51 51 LEU C C 169.311 0.4 1 194 51 51 LEU CA C 54.583 0.20 1 195 51 51 LEU CB C 38.541 0.12 1 196 51 51 LEU N N 120.391 0.25 1 197 52 52 PHE H H 8.484 0.03 1 198 52 52 PHE C C 169.693 0.4 1 199 52 52 PHE CA C 59.004 0.20 1 200 52 52 PHE CB C 36.774 0.12 1 201 52 52 PHE N N 119.235 0.25 1 202 53 53 GLU H H 8.612 0.03 1 203 53 53 GLU C C 169.226 0.4 1 204 53 53 GLU CA C 56.770 0.20 1 205 53 53 GLU CB C 26.095 0.12 1 206 53 53 GLU N N 118.093 0.25 1 207 54 54 ASP H H 8.100 0.03 1 208 54 54 ASP C C 168.821 0.4 1 209 54 54 ASP CA C 54.270 0.20 1 210 54 54 ASP CB C 37.658 0.12 1 211 54 54 ASP N N 119.436 0.25 1 212 55 55 LEU H H 8.201 0.03 1 213 55 55 LEU C C 168.374 0.4 1 214 55 55 LEU CA C 54.512 0.20 1 215 55 55 LEU CB C 37.218 0.12 1 216 55 55 LEU N N 117.834 0.25 1 217 56 56 SER H H 8.202 0.03 1 218 56 56 SER CA C 57.907 0.20 1 219 56 56 SER CB C 59.637 0.12 1 220 56 56 SER N N 113.105 0.25 1 221 58 58 LYS CA C 61.155 0.20 1 222 58 58 LYS CB C 28.766 0.12 1 223 59 59 ASN C C 172.731 0.4 1 224 59 59 ASN CA C 57.790 0.20 1 225 59 59 ASN CB C 34.380 0.12 1 226 60 60 TYR H H 7.600 0.03 1 227 60 60 TYR C C 174.066 0.4 1 228 60 60 TYR CA C 59.528 0.20 1 229 60 60 TYR CB C 35.125 0.12 1 230 60 60 TYR N N 121.900 0.25 1 231 61 61 LYS H H 9.023 0.03 1 232 61 61 LYS CA C 52.492 0.20 1 233 61 61 LYS CB C 32.890 0.12 1 234 61 61 LYS N N 121.514 0.25 1 235 64 64 ALA H H 8.895 0.03 1 236 64 64 ALA CA C 44.784 0.20 1 237 64 64 ALA CB C 19.292 0.12 1 238 64 64 ALA N N 130.460 0.25 1 239 67 67 PRO C C 172.758 0.4 1 240 67 67 PRO CA C 58.720 0.20 1 241 67 67 PRO CB C 29.280 0.12 1 242 68 68 LEU H H 8.950 0.03 1 243 68 68 LEU C C 169.307 0.4 1 244 68 68 LEU CA C 53.801 0.20 1 245 68 68 LEU CB C 40.076 0.12 1 246 68 68 LEU N N 117.245 0.25 1 247 69 69 SER H H 8.455 0.03 1 248 69 69 SER CA C 52.477 0.20 1 249 69 69 SER CB C 63.647 0.12 1 250 69 69 SER N N 113.665 0.25 1 251 70 70 SER CA C 58.310 0.20 1 252 71 71 VAL H H 7.470 0.03 1 253 71 71 VAL C C 170.136 0.4 1 254 71 71 VAL CA C 58.188 0.20 1 255 71 71 VAL CB C 30.724 0.12 1 256 71 71 VAL N N 110.003 0.25 1 257 72 72 ASN H H 8.153 0.03 1 258 72 72 ASN C C 172.318 0.4 1 259 72 72 ASN CA C 54.829 0.20 1 260 72 72 ASN CB C 34.033 0.12 1 261 72 72 ASN N N 122.566 0.25 1 262 73 73 LEU H H 8.642 0.03 1 263 73 73 LEU C C 172.719 0.4 1 264 73 73 LEU CA C 49.867 0.20 1 265 73 73 LEU CB C 37.880 0.12 1 266 73 73 LEU N N 115.605 0.25 1 267 74 74 VAL H H 7.126 0.03 1 268 74 74 VAL C C 172.337 0.4 1 269 74 74 VAL CA C 59.300 0.20 1 270 74 74 VAL CB C 27.894 0.12 1 271 74 74 VAL N N 118.761 0.25 1 272 75 75 MET H H 8.540 0.03 1 273 75 75 MET CA C 55.565 0.20 1 274 75 75 MET CB C 34.680 0.12 1 275 75 75 MET N N 113.062 0.25 1 276 77 77 VAL C C 171.479 0.4 1 277 77 77 VAL CA C 63.630 0.20 1 278 78 78 ALA H H 8.160 0.03 1 279 78 78 ALA C C 168.377 0.4 1 280 78 78 ALA CA C 53.316 0.20 1 281 78 78 ALA CB C 14.561 0.12 1 282 78 78 ALA N N 122.094 0.25 1 283 79 79 ARG H H 7.953 0.03 1 284 79 79 ARG C C 169.231 0.4 1 285 79 79 ARG CA C 56.773 0.20 1 286 79 79 ARG CB C 27.059 0.12 1 287 79 79 ARG N N 115.325 0.25 1 288 80 80 ALA H H 8.242 0.03 1 289 80 80 ALA CA C 51.940 0.20 1 290 80 80 ALA CB C 14.832 0.12 1 291 80 80 ALA N N 122.068 0.25 1 292 81 81 TRP C C 169.345 0.4 1 293 81 81 TRP CB C 37.290 0.12 1 294 82 82 LYS H H 8.328 0.03 1 295 82 82 LYS C C 170.133 0.4 1 296 82 82 LYS CA C 56.290 0.20 1 297 82 82 LYS CB C 29.669 0.12 1 298 82 82 LYS N N 119.433 0.25 1 299 83 83 LYS H H 7.507 0.03 1 300 83 83 LYS C C 171.862 0.4 1 301 83 83 LYS CA C 53.355 0.20 1 302 83 83 LYS CB C 29.462 0.12 1 303 83 83 LYS N N 116.527 0.25 1 304 84 84 GLY H H 7.930 0.03 1 305 84 84 GLY C C 174.508 0.4 1 306 84 84 GLY CA C 42.361 0.20 1 307 84 84 GLY N N 107.714 0.25 1 308 85 85 ILE H H 7.463 0.03 1 309 85 85 ILE C C 174.065 0.4 1 310 85 85 ILE CA C 58.399 0.20 1 311 85 85 ILE CB C 34.784 0.12 1 312 85 85 ILE N N 121.683 0.25 1 313 86 86 TYR H H 7.802 0.03 1 314 86 86 TYR C C 173.022 0.4 1 315 86 86 TYR CA C 56.173 0.20 1 316 86 86 TYR CB C 34.783 0.12 1 317 86 86 TYR N N 124.589 0.25 1 318 87 87 LEU H H 9.571 0.03 1 319 87 87 LEU CA C 51.286 0.20 1 320 87 87 LEU CB C 43.346 0.12 1 321 87 87 LEU N N 127.884 0.25 1 322 88 88 VAL C C 173.139 0.4 1 323 88 88 VAL CA C 57.810 0.20 1 324 88 88 VAL CB C 32.770 0.12 1 325 89 89 ASN H H 8.785 0.03 1 326 89 89 ASN CA C 47.377 0.20 1 327 89 89 ASN CB C 38.377 0.12 1 328 89 89 ASN N N 126.291 0.25 1 329 90 90 LEU H H 9.059 0.03 1 330 90 90 LEU C C 170.569 0.4 1 331 90 90 LEU CA C 50.486 0.20 1 332 90 90 LEU CB C 40.272 0.12 1 333 90 90 LEU N N 127.297 0.25 1 334 91 91 ASP H H 9.669 0.03 1 335 91 91 ASP C C 174.876 0.4 1 336 91 91 ASP CA C 57.999 0.20 1 337 91 91 ASP CB C 40.511 0.12 1 338 91 91 ASP N N 116.180 0.25 1 339 92 92 GLU H H 10.005 0.03 1 340 92 92 GLU C C 172.960 0.4 1 341 92 92 GLU CA C 51.697 0.20 1 342 92 92 GLU CB C 29.023 0.12 1 343 92 92 GLU N N 130.448 0.25 1 344 93 93 LYS H H 8.542 0.03 1 345 93 93 LYS C C 170.908 0.4 1 346 93 93 LYS CA C 55.346 0.20 1 347 93 93 LYS CB C 29.744 0.12 1 348 93 93 LYS N N 128.844 0.25 1 349 94 94 ILE H H 8.894 0.03 1 350 94 94 ILE C C 175.813 0.4 1 351 94 94 ILE CA C 58.388 0.20 1 352 94 94 ILE CB C 36.642 0.12 1 353 94 94 ILE N N 130.737 0.25 1 354 95 95 ASP H H 7.997 0.03 1 355 95 95 ASP C C 172.253 0.4 1 356 95 95 ASP CA C 51.251 0.20 1 357 95 95 ASP CB C 37.758 0.12 1 358 95 95 ASP N N 121.711 0.25 1 359 96 96 MET H H 8.269 0.03 1 360 96 96 MET C C 169.240 0.4 1 361 96 96 MET CA C 53.119 0.20 1 362 96 96 MET CB C 27.154 0.12 1 363 96 96 MET N N 129.321 0.25 1 364 97 97 ASP H H 8.213 0.03 1 365 97 97 ASP C C 173.189 0.4 1 366 97 97 ASP CA C 54.358 0.20 1 367 97 97 ASP CB C 37.297 0.12 1 368 97 97 ASP N N 120.962 0.25 1 369 98 98 ASN H H 8.336 0.03 1 370 98 98 ASN C C 170.126 0.4 1 371 98 98 ASN CA C 52.713 0.20 1 372 98 98 ASN CB C 35.117 0.12 1 373 98 98 ASN N N 119.002 0.25 1 374 99 99 LEU H H 8.649 0.03 1 375 99 99 LEU C C 171.305 0.4 1 376 99 99 LEU CA C 55.326 0.20 1 377 99 99 LEU CB C 38.247 0.12 1 378 99 99 LEU N N 122.429 0.25 1 379 100 100 LYS H H 8.188 0.03 1 380 100 100 LYS C C 166.633 0.4 1 381 100 100 LYS CA C 56.369 0.20 1 382 100 100 LYS CB C 27.880 0.12 1 383 100 100 LYS N N 119.223 0.25 1 384 101 101 LYS H H 7.691 0.03 1 385 101 101 LYS C C 171.140 0.4 1 386 101 101 LYS CA C 56.347 0.20 1 387 101 101 LYS CB C 28.902 0.12 1 388 101 101 LYS N N 120.405 0.25 1 389 102 102 ALA H H 7.629 0.03 1 390 102 102 ALA C C 171.443 0.4 1 391 102 102 ALA CA C 49.255 0.20 1 392 102 102 ALA CB C 15.470 0.12 1 393 102 102 ALA N N 120.108 0.25 1 394 103 103 GLY H H 7.860 0.03 1 395 103 103 GLY C C 175.381 0.4 1 396 103 103 GLY CA C 42.762 0.20 1 397 103 103 GLY N N 106.034 0.25 1 398 104 104 GLY H H 7.516 0.03 1 399 104 104 GLY C C 166.167 0.4 1 400 104 104 GLY CA C 40.312 0.20 1 401 104 104 GLY N N 103.504 0.25 1 402 105 105 ASN H H 6.158 0.03 1 403 105 105 ASN CA C 46.817 0.20 1 404 105 105 ASN CB C 37.577 0.12 1 405 105 105 ASN N N 111.080 0.25 1 406 107 107 GLU C C 170.975 0.4 1 407 108 108 ALA H H 7.355 0.03 1 408 108 108 ALA C C 174.067 0.4 1 409 108 108 ALA CA C 47.391 0.20 1 410 108 108 ALA CB C 20.546 0.12 1 411 108 108 ALA N N 111.067 0.25 1 412 109 109 PHE H H 8.897 0.03 1 413 109 109 PHE CA C 51.094 0.20 1 414 109 109 PHE CB C 38.551 0.12 1 415 109 109 PHE N N 121.115 0.25 1 416 110 110 VAL CA C 56.250 0.20 1 417 110 110 VAL CB C 29.940 0.12 1 418 111 111 THR H H 8.271 0.03 1 419 111 111 THR C C 177.123 0.4 1 420 111 111 THR CA C 56.369 0.20 1 421 111 111 THR CB C 66.223 0.12 1 422 111 111 THR N N 120.924 0.25 1 423 112 112 THR H H 8.419 0.03 1 424 112 112 THR C C 174.066 0.4 1 425 112 112 THR CA C 58.604 0.20 1 426 112 112 THR CB C 65.352 0.12 1 427 112 112 THR N N 121.736 0.25 1 428 113 113 ASP H H 8.542 0.03 1 429 113 113 ASP C C 172.431 0.4 1 430 113 113 ASP CA C 50.479 0.20 1 431 113 113 ASP CB C 35.515 0.12 1 432 113 113 ASP N N 120.717 0.25 1 433 114 114 ASN H H 8.161 0.03 1 434 114 114 ASN C C 171.459 0.4 1 435 114 114 ASN CA C 53.694 0.20 1 436 114 114 ASN CB C 38.458 0.12 1 437 114 114 ASN N N 129.083 0.25 1 438 115 115 VAL H H 7.993 0.03 1 439 115 115 VAL C C 170.122 0.4 1 440 115 115 VAL CA C 62.668 0.20 1 441 115 115 VAL CB C 27.953 0.12 1 442 115 115 VAL N N 123.356 0.25 1 443 116 116 ALA H H 7.341 0.03 1 444 116 116 ALA C C 167.937 0.4 1 445 116 116 ALA CA C 51.078 0.20 1 446 116 116 ALA CB C 14.538 0.12 1 447 116 116 ALA N N 120.659 0.25 1 448 117 117 VAL H H 7.643 0.03 1 449 117 117 VAL C C 171.012 0.4 1 450 117 117 VAL CA C 63.479 0.20 1 451 117 117 VAL CB C 28.132 0.12 1 452 117 117 VAL N N 117.844 0.25 1 453 118 118 GLY H H 7.505 0.03 1 454 118 118 GLY CA C 43.974 0.20 1 455 118 118 GLY N N 103.811 0.25 1 456 119 119 ALA H H 8.286 0.03 1 457 119 119 ALA C C 167.502 0.4 1 458 119 119 ALA CA C 52.099 0.20 1 459 119 119 ALA CB C 14.739 0.12 1 460 119 119 ALA N N 122.113 0.25 1 461 120 120 LYS H H 8.734 0.03 1 462 120 120 LYS C C 170.569 0.4 1 463 120 120 LYS CA C 56.373 0.20 1 464 120 120 LYS CB C 29.449 0.12 1 465 120 120 LYS N N 120.373 0.25 1 466 121 121 GLY H H 7.982 0.03 1 467 121 121 GLY CA C 41.338 0.20 1 468 121 121 GLY N N 102.863 0.25 1 469 126 126 ILE C C 168.840 0.4 1 470 126 126 ILE CA C 62.736 0.20 1 471 126 126 ILE CB C 34.978 0.12 1 472 127 127 ASP H H 8.067 0.03 1 473 127 127 ASP C C 169.267 0.4 1 474 127 127 ASP CA C 54.142 0.20 1 475 127 127 ASP CB C 37.583 0.12 1 476 127 127 ASP N N 119.908 0.25 1 477 128 128 LYS H H 7.912 0.03 1 478 128 128 LYS C C 169.236 0.4 1 479 128 128 LYS CA C 53.856 0.20 1 480 128 128 LYS CB C 28.136 0.12 1 481 128 128 LYS N N 118.083 0.25 1 482 129 129 LEU H H 8.245 0.03 1 483 129 129 LEU C C 169.253 0.4 1 484 129 129 LEU CA C 53.017 0.20 1 485 129 129 LEU CB C 37.349 0.12 1 486 129 129 LEU N N 117.082 0.25 1 487 130 130 GLY H H 7.358 0.03 1 488 130 130 GLY CA C 42.351 0.20 1 489 130 130 GLY N N 104.060 0.25 1 490 131 131 ALA C C 168.813 0.4 1 491 131 131 ALA CA C 51.570 0.20 1 492 131 131 ALA CB C 15.140 0.12 1 493 132 132 GLU H H 8.525 0.03 1 494 132 132 GLU C C 170.128 0.4 1 495 132 132 GLU CA C 55.145 0.20 1 496 132 132 GLU CB C 26.399 0.12 1 497 132 132 GLU N N 114.061 0.25 1 498 133 133 GLY H H 7.245 0.03 1 499 133 133 GLY C C 175.816 0.4 1 500 133 133 GLY CA C 42.577 0.20 1 501 133 133 GLY N N 103.487 0.25 1 502 134 134 GLY H H 8.039 0.03 1 503 134 134 GLY C C 173.619 0.4 1 504 134 134 GLY CA C 41.154 0.20 1 505 134 134 GLY N N 108.536 0.25 1 506 135 135 GLU H H 8.492 0.03 1 507 135 135 GLU CA C 51.900 0.20 1 508 135 135 GLU CB C 27.721 0.12 1 509 135 135 GLU N N 118.679 0.25 1 510 137 137 ALA C C 169.247 0.4 1 511 137 137 ALA CA C 51.400 0.20 1 512 137 137 ALA CB C 16.180 0.12 1 513 138 138 ILE H H 8.737 0.03 1 514 138 138 ILE CA C 59.411 0.20 1 515 138 138 ILE CB C 37.867 0.12 1 516 138 138 ILE N N 113.628 0.25 1 517 139 139 ILE C C 172.731 0.4 1 518 139 139 ILE CA C 54.600 0.20 1 519 139 139 ILE CB C 32.900 0.12 1 520 140 140 GLU H H 8.434 0.03 1 521 140 140 GLU C C 171.453 0.4 1 522 140 140 GLU CA C 51.401 0.20 1 523 140 140 GLU CB C 27.754 0.12 1 524 140 140 GLU N N 125.511 0.25 1 525 141 141 GLY H H 7.491 0.03 1 526 141 141 GLY CA C 39.901 0.20 1 527 141 141 GLY N N 104.789 0.25 1 528 142 142 LYS C C 171.578 0.4 1 529 142 142 LYS CA C 56.660 0.20 1 530 142 142 LYS CB C 29.580 0.12 1 531 143 143 ALA H H 9.163 0.03 1 532 143 143 ALA C C 169.691 0.4 1 533 143 143 ALA CA C 50.804 0.20 1 534 143 143 ALA CB C 14.703 0.12 1 535 143 143 ALA N N 133.950 0.25 1 536 144 144 GLY H H 9.331 0.03 1 537 144 144 GLY C C 173.623 0.4 1 538 144 144 GLY CA C 41.966 0.20 1 539 144 144 GLY N N 111.665 0.25 1 540 145 145 ASN H H 7.745 0.03 1 541 145 145 ASN C C 173.935 0.4 1 542 145 145 ASN CA C 50.187 0.20 1 543 145 145 ASN CB C 34.075 0.12 1 544 145 145 ASN N N 121.409 0.25 1 545 146 146 ALA H H 9.917 0.03 1 546 146 146 ALA C C 167.475 0.4 1 547 146 146 ALA CA C 52.479 0.20 1 548 146 146 ALA CB C 16.219 0.12 1 549 146 146 ALA N N 129.883 0.25 1 550 147 147 SER H H 9.944 0.03 1 551 147 147 SER C C 171.010 0.4 1 552 147 147 SER CA C 58.211 0.20 1 553 147 147 SER CB C 60.301 0.12 1 554 147 147 SER N N 120.023 0.25 1 555 148 148 GLY H H 7.969 0.03 1 556 148 148 GLY C C 171.051 0.4 1 557 148 148 GLY CA C 44.356 0.20 1 558 148 148 GLY N N 107.016 0.25 1 559 149 149 GLU H H 8.878 0.03 1 560 149 149 GLU C C 169.658 0.4 1 561 149 149 GLU CA C 56.270 0.20 1 562 149 149 GLU CB C 26.126 0.12 1 563 149 149 GLU N N 123.791 0.25 1 564 150 150 ALA H H 8.261 0.03 1 565 150 150 ALA CA C 52.099 0.20 1 566 150 150 ALA CB C 16.265 0.12 1 567 150 150 ALA N N 120.774 0.25 1 568 151 151 ARG CA C 56.590 0.20 1 569 152 152 ARG C C 168.824 0.4 1 570 152 152 ARG CA C 56.660 0.20 1 571 152 152 ARG CB C 25.887 0.12 1 572 153 153 ASN H H 9.333 0.03 1 573 153 153 ASN C C 170.566 0.4 1 574 153 153 ASN CA C 53.518 0.20 1 575 153 153 ASN CB C 34.719 0.12 1 576 153 153 ASN N N 123.286 0.25 1 577 154 154 GLY H H 9.138 0.03 1 578 154 154 GLY CA C 44.400 0.20 1 579 154 154 GLY N N 107.457 0.25 1 580 155 155 ALA H H 7.972 0.03 1 581 155 155 ALA C C 172.796 0.4 1 582 155 155 ALA CA C 51.786 0.20 1 583 155 155 ALA CB C 14.169 0.12 1 584 155 155 ALA N N 121.143 0.25 1 585 156 156 THR H H 7.544 0.03 1 586 156 156 THR C C 167.506 0.4 1 587 156 156 THR CA C 64.692 0.20 1 588 156 156 THR CB C 65.569 0.12 1 589 156 156 THR N N 119.689 0.25 1 590 157 157 GLU H H 8.345 0.03 1 591 157 157 GLU C C 170.113 0.4 1 592 157 157 GLU CA C 56.039 0.20 1 593 157 157 GLU CB C 25.710 0.12 1 594 157 157 GLU N N 119.689 0.25 1 595 158 158 ALA H H 6.987 0.03 1 596 158 158 ALA C C 174.939 0.4 1 597 158 158 ALA CA C 51.855 0.20 1 598 158 158 ALA CB C 14.479 0.12 1 599 158 158 ALA N N 119.793 0.25 1 600 159 159 PHE H H 8.478 0.03 1 601 159 159 PHE C C 174.499 0.4 1 602 159 159 PHE CA C 55.582 0.20 1 603 159 159 PHE CB C 34.566 0.12 1 604 159 159 PHE N N 115.650 0.25 1 605 160 160 LYS H H 8.404 0.03 1 606 160 160 LYS C C 170.569 0.4 1 607 160 160 LYS CA C 55.678 0.20 1 608 160 160 LYS CB C 28.970 0.12 1 609 160 160 LYS N N 117.719 0.25 1 610 161 161 LYS H H 7.126 0.03 1 611 161 161 LYS C C 172.721 0.4 1 612 161 161 LYS CA C 53.939 0.20 1 613 161 161 LYS CB C 29.318 0.12 1 614 161 161 LYS N N 115.454 0.25 1 615 162 162 ALA H H 7.465 0.03 1 616 162 162 ALA CA C 47.543 0.20 1 617 162 162 ALA CB C 16.157 0.12 1 618 162 162 ALA N N 124.321 0.25 1 619 163 163 SER C C 173.188 0.4 1 620 163 163 SER CA C 58.300 0.20 1 621 163 163 SER CB C 59.680 0.12 1 622 164 164 GLN H H 9.630 0.03 1 623 164 164 GLN C C 173.179 0.4 1 624 164 164 GLN CA C 53.164 0.20 1 625 164 164 GLN CB C 22.842 0.12 1 626 164 164 GLN N N 119.527 0.25 1 627 165 165 ILE H H 8.106 0.03 1 628 165 165 ILE C C 173.169 0.4 1 629 165 165 ILE CA C 54.214 0.20 1 630 165 165 ILE CB C 32.276 0.12 1 631 165 165 ILE N N 125.433 0.25 1 632 166 166 LYS H H 8.184 0.03 1 633 166 166 LYS C C 174.003 0.4 1 634 166 166 LYS CA C 51.250 0.20 1 635 166 166 LYS CB C 31.247 0.12 1 636 166 166 LYS N N 126.839 0.25 1 637 167 167 LEU H H 8.804 0.03 1 638 167 167 LEU C C 171.014 0.4 1 639 167 167 LEU CA C 51.382 0.20 1 640 167 167 LEU CB C 37.959 0.12 1 641 167 167 LEU N N 128.996 0.25 1 642 168 168 VAL H H 8.846 0.03 1 643 168 168 VAL C C 172.756 0.4 1 644 168 168 VAL CA C 58.454 0.20 1 645 168 168 VAL CB C 29.232 0.12 1 646 168 168 VAL N N 120.102 0.25 1 647 169 169 ALA H H 7.124 0.03 1 648 169 169 ALA CA C 49.478 0.20 1 649 169 169 ALA CB C 18.865 0.12 1 650 169 169 ALA N N 119.453 0.25 1 651 170 170 SER C C 174.064 0.4 1 652 170 170 SER CA C 54.692 0.20 1 653 170 170 SER CB C 60.245 0.12 1 654 171 171 GLN H H 8.410 0.03 1 655 171 171 GLN CA C 49.438 0.20 1 656 171 171 GLN CB C 30.335 0.12 1 657 171 171 GLN N N 123.742 0.25 1 658 172 172 PRO CA C 59.870 0.20 1 659 172 172 PRO CB C 30.054 0.12 1 660 173 173 ALA H H 8.353 0.03 1 661 173 173 ALA C C 168.827 0.4 1 662 173 173 ALA CA C 48.485 0.20 1 663 173 173 ALA CB C 15.002 0.12 1 664 173 173 ALA N N 119.296 0.25 1 665 174 174 ASP H H 7.207 0.03 1 666 174 174 ASP C C 174.932 0.4 1 667 174 174 ASP CA C 53.714 0.20 1 668 174 174 ASP CB C 35.421 0.12 1 669 174 174 ASP N N 111.684 0.25 1 670 175 175 TRP H H 7.656 0.03 1 671 175 175 TRP C C 173.636 0.4 1 672 175 175 TRP CA C 53.345 0.20 1 673 175 175 TRP CB C 25.978 0.12 1 674 175 175 TRP N N 109.425 0.25 1 675 176 176 ASP H H 8.169 0.03 1 676 176 176 ASP C C 173.130 0.4 1 677 176 176 ASP CA C 50.734 0.20 1 678 176 176 ASP CB C 42.150 0.12 1 679 176 176 ASP N N 121.944 0.25 1 680 177 177 ARG H H 8.923 0.03 1 681 177 177 ARG C C 171.026 0.4 1 682 177 177 ARG CA C 57.367 0.20 1 683 177 177 ARG CB C 28.310 0.12 1 684 177 177 ARG N N 127.567 0.25 1 685 178 178 ILE H H 7.824 0.03 1 686 178 178 ILE C C 169.231 0.4 1 687 178 178 ILE CA C 60.135 0.20 1 688 178 178 ILE CB C 32.775 0.12 1 689 178 178 ILE N N 118.860 0.25 1 690 179 179 LYS H H 8.961 0.03 1 691 179 179 LYS C C 171.006 0.4 1 692 179 179 LYS CA C 56.375 0.20 1 693 179 179 LYS CB C 28.283 0.12 1 694 179 179 LYS N N 121.853 0.25 1 695 180 180 ALA H H 8.339 0.03 1 696 180 180 ALA C C 169.682 0.4 1 697 180 180 ALA CA C 52.730 0.20 1 698 180 180 ALA CB C 15.970 0.12 1 699 180 180 ALA N N 119.223 0.25 1 700 181 181 LEU H H 7.824 0.03 1 701 181 181 LEU C C 168.376 0.4 1 702 181 181 LEU CA C 56.095 0.20 1 703 181 181 LEU CB C 38.551 0.12 1 704 181 181 LEU N N 120.584 0.25 1 705 182 182 ASP H H 8.292 0.03 1 706 182 182 ASP C C 169.254 0.4 1 707 182 182 ASP CA C 55.148 0.20 1 708 182 182 ASP CB C 37.660 0.12 1 709 182 182 ASP N N 123.667 0.25 1 710 183 183 VAL H H 9.155 0.03 1 711 183 183 VAL C C 169.253 0.4 1 712 183 183 VAL CA C 63.264 0.20 1 713 183 183 VAL CB C 28.781 0.12 1 714 183 183 VAL N N 121.128 0.25 1 715 184 184 ALA H H 9.098 0.03 1 716 184 184 ALA C C 169.695 0.4 1 717 184 184 ALA CA C 52.099 0.20 1 718 184 184 ALA CB C 16.178 0.12 1 719 184 184 ALA N N 120.085 0.25 1 720 185 185 THR H H 8.278 0.03 1 721 185 185 THR C C 172.231 0.4 1 722 185 185 THR CA C 64.563 0.20 1 723 185 185 THR CB C 65.566 0.12 1 724 185 185 THR N N 115.255 0.25 1 725 186 186 ASN H H 7.547 0.03 1 726 186 186 ASN C C 170.994 0.4 1 727 186 186 ASN CA C 53.927 0.20 1 728 186 186 ASN CB C 35.700 0.12 1 729 186 186 ASN N N 119.844 0.25 1 730 187 187 VAL H H 8.625 0.03 1 731 187 187 VAL CA C 63.626 0.20 1 732 187 187 VAL CB C 28.173 0.12 1 733 187 187 VAL N N 120.746 0.25 1 734 188 188 LEU C C 169.688 0.4 1 735 189 189 GLN H H 7.609 0.03 1 736 189 189 GLN CA C 54.308 0.20 1 737 189 189 GLN CB C 27.530 0.12 1 738 189 189 GLN N N 116.656 0.25 1 739 190 190 ARG H H 8.721 0.03 1 740 190 190 ARG CA C 56.773 0.20 1 741 190 190 ARG CB C 25.918 0.12 1 742 190 190 ARG N N 118.445 0.25 1 743 192 192 PRO C C 170.570 0.4 1 744 193 193 ASN H H 9.165 0.03 1 745 193 193 ASN C C 172.758 0.4 1 746 193 193 ASN CA C 49.381 0.20 1 747 193 193 ASN CB C 34.951 0.12 1 748 193 193 ASN N N 115.713 0.25 1 749 194 194 ILE H H 7.548 0.03 1 750 194 194 ILE C C 171.935 0.4 1 751 194 194 ILE CA C 56.786 0.20 1 752 194 194 ILE CB C 35.417 0.12 1 753 194 194 ILE N N 117.923 0.25 1 754 195 195 LYS H H 9.086 0.03 1 755 195 195 LYS CA C 54.936 0.20 1 756 195 195 LYS CB C 30.118 0.12 1 757 195 195 LYS N N 119.431 0.25 1 758 199 199 CYS C C 175.382 0.4 1 759 199 199 CYS CA C 52.590 0.20 1 760 199 199 CYS CB C 28.080 0.12 1 761 200 200 ALA H H 8.117 0.03 1 762 200 200 ALA C C 171.874 0.4 1 763 200 200 ALA CA C 50.055 0.20 1 764 200 200 ALA CB C 15.499 0.12 1 765 200 200 ALA N N 117.980 0.25 1 766 201 201 ASN H H 7.151 0.03 1 767 201 201 ASN C C 171.846 0.4 1 768 201 201 ASN CA C 49.712 0.20 1 769 201 201 ASN CB C 37.045 0.12 1 770 201 201 ASN N N 110.830 0.25 1 771 202 202 ASP H H 7.603 0.03 1 772 202 202 ASP C C 169.679 0.4 1 773 202 202 ASP CA C 53.928 0.20 1 774 202 202 ASP CB C 39.438 0.12 1 775 202 202 ASP N N 121.366 0.25 1 776 203 203 THR H H 8.170 0.03 1 777 203 203 THR C C 171.006 0.4 1 778 203 203 THR CA C 63.682 0.20 1 779 203 203 THR CB C 65.300 0.12 1 780 203 203 THR N N 117.512 0.25 1 781 204 204 MET H H 7.889 0.03 1 782 204 204 MET CA C 56.366 0.20 1 783 204 204 MET CB C 29.126 0.12 1 784 204 204 MET N N 115.018 0.25 1 785 205 205 ALA H H 8.064 0.03 1 786 205 205 ALA C C 169.691 0.4 1 787 205 205 ALA CA C 52.307 0.20 1 788 205 205 ALA CB C 15.476 0.12 1 789 205 205 ALA N N 121.765 0.25 1 790 206 206 MET H H 8.500 0.03 1 791 206 206 MET C C 168.384 0.4 1 792 206 206 MET CA C 56.736 0.20 1 793 206 206 MET CB C 29.144 0.12 1 794 206 206 MET N N 116.455 0.25 1 795 207 207 GLY H H 7.576 0.03 1 796 207 207 GLY CA C 43.977 0.20 1 797 207 207 GLY N N 108.798 0.25 1 798 208 208 VAL C C 170.554 0.4 1 799 208 208 VAL CA C 63.141 0.20 1 800 208 208 VAL CB C 26.810 0.12 1 801 209 209 ALA H H 9.072 0.03 1 802 209 209 ALA CA C 52.102 0.20 1 803 209 209 ALA CB C 14.182 0.12 1 804 209 209 ALA N N 121.164 0.25 1 805 210 210 GLN H H 7.558 0.03 1 806 210 210 GLN C C 171.041 0.4 1 807 210 210 GLN CA C 55.451 0.20 1 808 210 210 GLN CB C 24.697 0.12 1 809 210 210 GLN N N 119.533 0.25 1 810 211 211 ALA H H 8.024 0.03 1 811 211 211 ALA C C 167.509 0.4 1 812 211 211 ALA CA C 52.303 0.20 1 813 211 211 ALA CB C 15.765 0.12 1 814 211 211 ALA N N 124.054 0.25 1 815 212 212 VAL H H 8.664 0.03 1 816 212 212 VAL C C 170.464 0.4 1 817 212 212 VAL CA C 63.677 0.20 1 818 212 212 VAL CB C 28.316 0.12 1 819 212 212 VAL N N 119.385 0.25 1 820 213 213 ALA H H 8.073 0.03 1 821 213 213 ALA C C 165.751 0.4 1 822 213 213 ALA CA C 51.847 0.20 1 823 213 213 ALA CB C 14.500 0.12 1 824 213 213 ALA N N 123.444 0.25 1 825 214 214 ASN H H 8.881 0.03 1 826 214 214 ASN C C 171.447 0.4 1 827 214 214 ASN CA C 52.089 0.20 1 828 214 214 ASN CB C 34.086 0.12 1 829 214 214 ASN N N 120.388 0.25 1 830 215 215 ALA H H 7.506 0.03 1 831 215 215 ALA C C 170.999 0.4 1 832 215 215 ALA CA C 48.650 0.20 1 833 215 215 ALA CB C 15.688 0.12 1 834 215 215 ALA N N 119.218 0.25 1 835 216 216 GLY H H 8.211 0.03 1 836 216 216 GLY C C 171.437 0.4 1 837 216 216 GLY CA C 43.168 0.20 1 838 216 216 GLY N N 107.975 0.25 1 839 217 217 LYS H H 8.009 0.03 1 840 217 217 LYS C C 169.654 0.4 1 841 217 217 LYS CA C 52.297 0.20 1 842 217 217 LYS CB C 30.773 0.12 1 843 217 217 LYS N N 115.660 0.25 1 844 218 218 THR H H 8.183 0.03 1 845 218 218 THR C C 172.314 0.4 1 846 218 218 THR CA C 63.321 0.20 1 847 218 218 THR CB C 64.926 0.12 1 848 218 218 THR N N 120.416 0.25 1 849 219 219 GLY H H 9.590 0.03 1 850 219 219 GLY C C 174.944 0.4 1 851 219 219 GLY CA C 42.389 0.20 1 852 219 219 GLY N N 117.122 0.25 1 853 220 220 LYS H H 7.711 0.03 1 854 220 220 LYS C C 173.178 0.4 1 855 220 220 LYS CA C 52.336 0.20 1 856 220 220 LYS CB C 32.022 0.12 1 857 220 220 LYS N N 119.996 0.25 1 858 221 221 VAL H H 7.789 0.03 1 859 221 221 VAL C C 175.817 0.4 1 860 221 221 VAL CA C 57.626 0.20 1 861 221 221 VAL CB C 30.443 0.12 1 862 221 221 VAL N N 118.283 0.25 1 863 222 222 LEU H H 8.804 0.03 1 864 222 222 LEU C C 171.875 0.4 1 865 222 222 LEU CA C 52.064 0.20 1 866 222 222 LEU CB C 37.663 0.12 1 867 222 222 LEU N N 125.897 0.25 1 868 223 223 VAL H H 8.501 0.03 1 869 223 223 VAL CA C 59.169 0.20 1 870 223 223 VAL CB C 31.948 0.12 1 871 223 223 VAL N N 121.160 0.25 1 872 224 224 VAL CA C 59.412 0.20 1 873 224 224 VAL CB C 37.872 0.12 1 874 226 226 THR C C 172.334 0.4 1 875 226 226 THR CA C 59.750 0.20 1 876 226 226 THR CB C 69.830 0.12 1 877 227 227 ASP H H 7.671 0.03 1 878 227 227 ASP C C 169.243 0.4 1 879 227 227 ASP CA C 58.209 0.20 1 880 227 227 ASP CB C 35.574 0.12 1 881 227 227 ASP N N 121.510 0.25 1 882 228 228 GLY H H 8.298 0.03 1 883 228 228 GLY CA C 43.304 0.20 1 884 228 228 GLY N N 113.071 0.25 1 885 230 230 PRO C C 168.381 0.4 1 886 230 230 PRO CA C 63.980 0.20 1 887 230 230 PRO CB C 28.650 0.12 1 888 231 231 GLU H H 10.162 0.03 1 889 231 231 GLU C C 169.257 0.4 1 890 231 231 GLU CA C 56.600 0.20 1 891 231 231 GLU CB C 26.518 0.12 1 892 231 231 GLU N N 117.300 0.25 1 893 232 232 ALA H H 7.152 0.03 1 894 232 232 ALA C C 169.244 0.4 1 895 232 232 ALA CA C 51.484 0.20 1 896 232 232 ALA CB C 15.018 0.12 1 897 232 232 ALA N N 120.374 0.25 1 898 233 233 ARG H H 8.037 0.03 1 899 233 233 ARG C C 168.816 0.4 1 900 233 233 ARG CA C 57.370 0.20 1 901 233 233 ARG CB C 25.442 0.12 1 902 233 233 ARG N N 116.824 0.25 1 903 234 234 LYS H H 8.037 0.03 1 904 234 234 LYS C C 168.827 0.4 1 905 234 234 LYS CA C 55.757 0.20 1 906 234 234 LYS CB C 28.134 0.12 1 907 234 234 LYS N N 119.137 0.25 1 908 235 235 MET H H 7.942 0.03 1 909 235 235 MET C C 169.281 0.4 1 910 235 235 MET CA C 56.774 0.20 1 911 235 235 MET CB C 30.210 0.12 1 912 235 235 MET N N 119.383 0.25 1 913 236 236 VAL H H 8.501 0.03 1 914 236 236 VAL C C 168.828 0.4 1 915 236 236 VAL CA C 61.655 0.20 1 916 236 236 VAL CB C 27.869 0.12 1 917 236 236 VAL N N 122.832 0.25 1 918 237 237 GLU H H 7.790 0.03 1 919 237 237 GLU C C 170.126 0.4 1 920 237 237 GLU CA C 56.337 0.20 1 921 237 237 GLU CB C 26.176 0.12 1 922 237 237 GLU N N 120.486 0.25 1 923 238 238 ALA H H 7.836 0.03 1 924 238 238 ALA C C 170.131 0.4 1 925 238 238 ALA CA C 49.255 0.20 1 926 238 238 ALA CB C 16.288 0.12 1 927 238 238 ALA N N 117.131 0.25 1 928 239 239 GLY H H 7.928 0.03 1 929 239 239 GLY C C 169.684 0.4 1 930 239 239 GLY CA C 42.450 0.20 1 931 239 239 GLY N N 106.844 0.25 1 932 240 240 GLN H H 8.363 0.03 1 933 240 240 GLN C C 172.753 0.4 1 934 240 240 GLN CA C 53.927 0.20 1 935 240 240 GLN CB C 26.647 0.12 1 936 240 240 GLN N N 118.681 0.25 1 937 241 241 MET H H 7.350 0.03 1 938 241 241 MET C C 174.491 0.4 1 939 241 241 MET CA C 52.078 0.20 1 940 241 241 MET CB C 34.000 0.12 1 941 241 241 MET N N 115.633 0.25 1 942 242 242 THR H H 8.957 0.03 1 943 242 242 THR C C 174.501 0.4 1 944 242 242 THR CA C 62.784 0.20 1 945 242 242 THR CB C 65.941 0.12 1 946 242 242 THR N N 119.588 0.25 1 947 243 243 ALA H H 7.846 0.03 1 948 243 243 ALA C C 172.328 0.4 1 949 243 243 ALA CA C 48.233 0.20 1 950 243 243 ALA CB C 19.856 0.12 1 951 243 243 ALA N N 115.237 0.25 1 952 244 244 THR H H 8.635 0.03 1 953 244 244 THR C C 171.031 0.4 1 954 244 244 THR CA C 57.588 0.20 1 955 244 244 THR CB C 64.394 0.12 1 956 244 244 THR N N 112.364 0.25 1 957 245 245 VAL H H 7.914 0.03 1 958 245 245 VAL C C 173.985 0.4 1 959 245 245 VAL CA C 59.213 0.20 1 960 245 245 VAL CB C 26.316 0.12 1 961 245 245 VAL N N 121.602 0.25 1 962 246 246 ALA H H 9.398 0.03 1 963 246 246 ALA C C 170.563 0.4 1 964 246 246 ALA CA C 49.865 0.20 1 965 246 246 ALA CB C 16.372 0.12 1 966 246 246 ALA N N 131.425 0.25 1 967 247 247 GLN H H 7.609 0.03 1 968 247 247 GLN C C 174.501 0.4 1 969 247 247 GLN CA C 51.682 0.20 1 970 247 247 GLN CB C 32.369 0.12 1 971 247 247 GLN N N 117.850 0.25 1 972 248 248 ASN H H 9.317 0.03 1 973 248 248 ASN CA C 46.829 0.20 1 974 248 248 ASN CB C 35.155 0.12 1 975 248 248 ASN N N 116.172 0.25 1 976 249 249 PRO C C 169.706 0.4 1 977 249 249 PRO CA C 60.760 0.20 1 978 249 249 PRO CB C 27.360 0.12 1 979 250 250 ALA H H 8.406 0.03 1 980 250 250 ALA C C 169.694 0.4 1 981 250 250 ALA CA C 53.136 0.20 1 982 250 250 ALA CB C 14.236 0.12 1 983 250 250 ALA N N 119.152 0.25 1 984 251 251 ASP H H 7.111 0.03 1 985 251 251 ASP C C 167.939 0.4 1 986 251 251 ASP CA C 53.327 0.20 1 987 251 251 ASP CB C 37.880 0.12 1 988 251 251 ASP N N 116.527 0.25 1 989 252 252 ILE H H 7.865 0.03 1 990 252 252 ILE C C 170.568 0.4 1 991 252 252 ILE CA C 62.696 0.20 1 992 252 252 ILE CB C 35.045 0.12 1 993 252 252 ILE N N 121.683 0.25 1 994 253 253 GLY H H 8.200 0.03 1 995 253 253 GLY C C 174.044 0.4 1 996 253 253 GLY CA C 44.384 0.20 1 997 253 253 GLY N N 102.966 0.25 1 998 254 254 ALA H H 8.710 0.03 1 999 254 254 ALA CA C 52.746 0.20 1 1000 254 254 ALA CB C 15.761 0.12 1 1001 254 254 ALA N N 123.447 0.25 1 1002 255 255 THR H H 8.298 0.03 1 1003 255 255 THR CA C 63.692 0.20 1 1004 255 255 THR CB C 64.861 0.12 1 1005 255 255 THR N N 113.071 0.25 1 1006 256 256 GLY H H 8.133 0.03 1 1007 256 256 GLY CA C 44.621 0.20 1 1008 256 256 GLY N N 107.148 0.25 1 1009 257 257 LEU C C 170.116 0.4 1 1010 257 257 LEU CA C 59.530 0.20 1 1011 257 257 LEU CB C 41.520 0.12 1 1012 258 258 LYS H H 8.779 0.03 1 1013 258 258 LYS CA C 54.492 0.20 1 1014 258 258 LYS CB C 38.163 0.12 1 1015 258 258 LYS N N 120.588 0.25 1 1016 259 259 LEU H H 7.614 0.03 1 1017 259 259 LEU C C 170.139 0.4 1 1018 259 259 LEU CA C 55.084 0.20 1 1019 259 259 LEU CB C 40.320 0.12 1 1020 259 259 LEU N N 116.660 0.25 1 1021 260 260 MET H H 7.786 0.03 1 1022 260 260 MET C C 171.870 0.4 1 1023 260 260 MET CA C 54.345 0.20 1 1024 260 260 MET CB C 27.652 0.12 1 1025 260 260 MET N N 116.295 0.25 1 1026 261 261 VAL H H 7.906 0.03 1 1027 261 261 VAL CA C 58.890 0.20 1 1028 261 261 VAL CB C 36.306 0.12 1 1029 261 261 VAL N N 116.126 0.25 1 1030 262 262 ASP C C 168.714 0.4 1 1031 262 262 ASP CA C 53.970 0.20 1 1032 262 262 ASP CB C 36.740 0.12 1 1033 263 263 ALA H H 7.845 0.03 1 1034 263 263 ALA CA C 51.706 0.20 1 1035 263 263 ALA CB C 14.070 0.12 1 1036 263 263 ALA N N 123.484 0.25 1 1037 264 264 GLU C C 170.131 0.4 1 1038 264 264 GLU CA C 56.700 0.20 1 1039 264 264 GLU CB C 28.600 0.12 1 1040 265 265 LYS H H 8.117 0.03 1 1041 265 265 LYS CA C 54.735 0.20 1 1042 265 265 LYS CB C 38.118 0.12 1 1043 265 265 LYS N N 116.231 0.25 1 1044 267 267 GLY C C 174.074 0.4 1 1045 267 267 GLY CA C 42.449 0.20 1 1046 268 268 LYS H H 8.131 0.03 1 1047 268 268 LYS C C 171.892 0.4 1 1048 268 268 LYS CA C 53.155 0.20 1 1049 268 268 LYS CB C 30.439 0.12 1 1050 268 268 LYS N N 118.378 0.25 1 1051 269 269 VAL H H 7.068 0.03 1 1052 269 269 VAL C C 171.406 0.4 1 1053 269 269 VAL CA C 57.584 0.20 1 1054 269 269 VAL CB C 35.798 0.12 1 1055 269 269 VAL N N 118.474 0.25 1 1056 270 270 ILE H H 10.598 0.03 1 1057 270 270 ILE CA C 56.162 0.20 1 1058 270 270 ILE CB C 37.029 0.12 1 1059 270 270 ILE N N 130.211 0.25 1 1060 271 271 PRO CA C 61.453 0.20 1 1061 271 271 PRO CB C 29.793 0.12 1 1062 272 272 LEU C C 171.447 0.4 1 1063 272 272 LEU CA C 56.300 0.20 1 1064 272 272 LEU CB C 26.880 0.12 1 1065 273 273 ASP H H 8.053 0.03 1 1066 273 273 ASP C C 172.741 0.4 1 1067 273 273 ASP CA C 50.260 0.20 1 1068 273 273 ASP CB C 31.149 0.12 1 1069 273 273 ASP N N 110.666 0.25 1 1070 274 274 LYS H H 7.108 0.03 1 1071 274 274 LYS C C 173.344 0.4 1 1072 274 274 LYS CA C 51.939 0.20 1 1073 274 274 LYS CB C 34.580 0.12 1 1074 274 274 LYS N N 121.200 0.25 1 1075 275 275 ALA H H 8.462 0.03 1 1076 275 275 ALA CA C 47.224 0.20 1 1077 275 275 ALA CB C 18.930 0.12 1 1078 275 275 ALA N N 128.919 0.25 1 1079 276 276 PRO CA C 59.810 0.20 1 1080 276 276 PRO CB C 28.530 0.12 1 1081 277 277 GLU H H 7.912 0.03 1 1082 277 277 GLU C C 173.139 0.4 1 1083 277 277 GLU CA C 53.727 0.20 1 1084 277 277 GLU CB C 29.880 0.12 1 1085 277 277 GLU N N 121.602 0.25 1 1086 278 278 PHE H H 8.731 0.03 1 1087 278 278 PHE C C 173.139 0.4 1 1088 278 278 PHE CA C 52.640 0.20 1 1089 278 278 PHE CB C 37.867 0.12 1 1090 278 278 PHE N N 124.152 0.25 1 1091 279 279 LYS H H 8.412 0.03 1 1092 279 279 LYS C C 174.935 0.4 1 1093 279 279 LYS CA C 50.832 0.20 1 1094 279 279 LYS CB C 31.495 0.12 1 1095 279 279 LYS N N 124.624 0.25 1 1096 280 280 LEU H H 8.119 0.03 1 1097 280 280 LEU C C 171.091 0.4 1 1098 280 280 LEU CA C 49.704 0.20 1 1099 280 280 LEU CB C 41.125 0.12 1 1100 280 280 LEU N N 122.074 0.25 1 1101 281 281 VAL H H 8.555 0.03 1 1102 281 281 VAL C C 172.314 0.4 1 1103 281 281 VAL CA C 58.186 0.20 1 1104 281 281 VAL CB C 29.635 0.12 1 1105 281 281 VAL N N 124.152 0.25 1 1106 282 282 ASP H H 8.556 0.03 1 1107 282 282 ASP C C 172.747 0.4 1 1108 282 282 ASP CA C 52.309 0.20 1 1109 282 282 ASP CB C 38.957 0.12 1 1110 282 282 ASP N N 126.514 0.25 1 1111 283 283 SER H H 8.589 0.03 1 1112 283 283 SER C C 174.522 0.4 1 1113 283 283 SER CA C 53.747 0.20 1 1114 283 283 SER CB C 64.040 0.12 1 1115 283 283 SER N N 114.634 0.25 1 1116 284 284 ILE H H 8.527 0.03 1 1117 284 284 ILE CA C 56.911 0.20 1 1118 284 284 ILE CB C 38.986 0.12 1 1119 284 284 ILE N N 117.280 0.25 1 1120 285 285 LEU H H 8.594 0.03 1 1121 285 285 LEU C C 173.338 0.4 1 1122 285 285 LEU CA C 52.906 0.20 1 1123 285 285 LEU CB C 39.417 0.12 1 1124 285 285 LEU N N 129.737 0.25 1 1125 286 286 VAL H H 9.049 0.03 1 1126 286 286 VAL C C 173.193 0.4 1 1127 286 286 VAL CA C 59.406 0.20 1 1128 286 286 VAL CB C 29.103 0.12 1 1129 286 286 VAL N N 129.735 0.25 1 1130 287 287 THR H H 8.268 0.03 1 1131 287 287 THR C C 174.934 0.4 1 1132 287 287 THR CA C 57.128 0.20 1 1133 287 287 THR CB C 67.884 0.12 1 1134 287 287 THR N N 115.926 0.25 1 1135 288 288 GLN H H 8.909 0.03 1 1136 288 288 GLN CA C 52.078 0.20 1 1137 288 288 GLN CB C 35.318 0.12 1 1138 288 288 GLN N N 125.528 0.25 1 stop_ save_