data_16982 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of the D-allose binding protein from Escherichia coli in the apo form ; _BMRB_accession_number 16982 _BMRB_flat_file_name bmr16982.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" 266 "13C chemical shifts" 775 "15N chemical shifts" 266 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 16984 'Complex 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 'D-allose binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'D-allose binding protein' $ALBP 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 16984 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_ #################### # 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 Eubacteria . 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]' 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 Varian _Model DMX _Field_strength 500 _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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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 'D-allose binding protein' _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 175.407 0.4 1 2 1 1 ALA CA C 51.850 0.38 1 3 1 1 ALA CB C 18.334 0.24 1 4 2 2 ALA H H 8.292 0.03 1 5 2 2 ALA C C 176.090 0.4 1 6 2 2 ALA CA C 51.399 0.38 1 7 2 2 ALA CB C 19.293 0.24 1 8 2 2 ALA N N 123.323 0.35 1 9 3 3 GLU H H 8.130 0.03 1 10 3 3 GLU C C 176.737 0.4 1 11 3 3 GLU CA C 58.109 0.38 1 12 3 3 GLU CB C 31.685 0.24 1 13 3 3 GLU N N 117.975 0.35 1 14 4 4 TYR H H 7.794 0.03 1 15 4 4 TYR C C 179.012 0.4 1 16 4 4 TYR CA C 56.592 0.38 1 17 4 4 TYR CB C 41.701 0.24 1 18 4 4 TYR N N 114.226 0.35 1 19 5 5 ALA H H 8.339 0.03 1 20 5 5 ALA C C 176.025 0.4 1 21 5 5 ALA CA C 48.921 0.38 1 22 5 5 ALA CB C 20.548 0.24 1 23 5 5 ALA N N 121.724 0.35 1 24 6 6 VAL H H 8.672 0.03 1 25 6 6 VAL C C 178.214 0.4 1 26 6 6 VAL CA C 59.471 0.38 1 27 6 6 VAL CB C 34.576 0.24 1 28 6 6 VAL N N 118.131 0.35 1 29 7 7 VAL H H 9.155 0.03 1 30 7 7 VAL C C 177.675 0.4 1 31 7 7 VAL CA C 60.477 0.38 1 32 7 7 VAL CB C 32.660 0.24 1 33 7 7 VAL N N 126.757 0.35 1 34 8 8 LEU H H 8.973 0.03 1 35 8 8 LEU CA C 52.339 0.38 1 36 8 8 LEU CB C 42.070 0.24 1 37 8 8 LEU N N 124.550 0.35 1 38 9 9 LYS C C 177.922 0.4 1 39 9 9 LYS CA C 60.088 0.38 1 40 9 9 LYS CB C 31.940 0.24 1 41 10 10 THR H H 6.293 0.03 1 42 10 10 THR C C 181.252 0.4 1 43 10 10 THR CA C 59.140 0.38 1 44 10 10 THR CB C 67.834 0.24 1 45 10 10 THR N N 106.313 0.35 1 46 11 11 LEU H H 8.456 0.03 1 47 11 11 LEU C C 172.914 0.4 1 48 11 11 LEU CA C 54.064 0.38 1 49 11 11 LEU CB C 40.414 0.24 1 50 11 11 LEU N N 121.722 0.35 1 51 12 12 SER H H 8.274 0.03 1 52 12 12 SER C C 179.248 0.4 1 53 12 12 SER CA C 58.305 0.38 1 54 12 12 SER CB C 63.109 0.24 1 55 12 12 SER N N 114.057 0.35 1 56 13 13 ASN H H 7.118 0.03 1 57 13 13 ASN CA C 50.515 0.38 1 58 13 13 ASN CB C 40.864 0.24 1 59 13 13 ASN N N 118.655 0.35 1 60 14 14 PRO C C 175.729 0.4 1 61 14 14 PRO CA C 64.950 0.38 1 62 14 14 PRO CB C 31.570 0.24 1 63 15 15 PHE H H 8.044 0.03 1 64 15 15 PHE C C 176.037 0.4 1 65 15 15 PHE CA C 60.744 0.38 1 66 15 15 PHE CB C 38.684 0.24 1 67 15 15 PHE N N 118.723 0.35 1 68 16 16 TRP H H 7.059 0.03 1 69 16 16 TRP CA C 58.240 0.38 1 70 16 16 TRP CB C 30.040 0.24 1 71 16 16 TRP N N 117.834 0.35 1 72 17 17 VAL H H 7.642 0.03 1 73 17 17 VAL C C 173.564 0.4 1 74 17 17 VAL CA C 66.424 0.38 1 75 17 17 VAL CB C 30.905 0.24 1 76 17 17 VAL N N 121.277 0.35 1 77 18 18 ASP H H 8.394 0.03 1 78 18 18 ASP C C 172.981 0.4 1 79 18 18 ASP CA C 56.636 0.38 1 80 18 18 ASP CB C 39.509 0.24 1 81 18 18 ASP N N 121.611 0.35 1 82 19 19 MET H H 7.550 0.03 1 83 19 19 MET C C 174.849 0.4 1 84 19 19 MET CA C 59.227 0.38 1 85 19 19 MET CB C 31.087 0.24 1 86 19 19 MET N N 120.812 0.35 1 87 20 20 LYS H H 8.163 0.03 1 88 20 20 LYS CA C 59.881 0.38 1 89 20 20 LYS CB C 31.369 0.24 1 90 20 20 LYS N N 119.944 0.35 1 91 21 21 LYS H H 7.773 0.03 1 92 21 21 LYS C C 173.839 0.4 1 93 21 21 LYS CA C 58.701 0.38 1 94 21 21 LYS CB C 31.032 0.24 1 95 21 21 LYS N N 118.945 0.35 1 96 22 22 GLY H H 7.992 0.03 1 97 22 22 GLY CA C 46.544 0.38 1 98 22 22 GLY N N 105.230 0.35 1 99 23 23 ILE H H 8.117 0.03 1 100 23 23 ILE C C 175.410 0.4 1 101 23 23 ILE CA C 65.394 0.38 1 102 23 23 ILE CB C 36.711 0.24 1 103 23 23 ILE N N 121.679 0.35 1 104 24 24 GLU H H 8.431 0.03 1 105 24 24 GLU C C 172.038 0.4 1 106 24 24 GLU CA C 59.510 0.38 1 107 24 24 GLU CB C 28.710 0.24 1 108 24 24 GLU N N 119.687 0.35 1 109 25 25 ASP H H 8.696 0.03 1 110 25 25 ASP C C 173.440 0.4 1 111 25 25 ASP CA C 56.914 0.38 1 112 25 25 ASP CB C 39.287 0.24 1 113 25 25 ASP N N 120.275 0.35 1 114 26 26 GLU H H 7.902 0.03 1 115 26 26 GLU C C 174.202 0.4 1 116 26 26 GLU CA C 57.565 0.38 1 117 26 26 GLU CB C 27.273 0.24 1 118 26 26 GLU N N 122.989 0.35 1 119 27 27 ALA H H 8.789 0.03 1 120 27 27 ALA C C 172.713 0.4 1 121 27 27 ALA CA C 55.205 0.38 1 122 27 27 ALA CB C 16.802 0.24 1 123 27 27 ALA N N 122.578 0.35 1 124 28 28 LYS H H 7.423 0.03 1 125 28 28 LYS C C 172.570 0.4 1 126 28 28 LYS CA C 58.673 0.38 1 127 28 28 LYS CB C 31.052 0.24 1 128 28 28 LYS N N 116.781 0.35 1 129 29 29 THR H H 7.663 0.03 1 130 29 29 THR C C 177.167 0.4 1 131 29 29 THR CA C 65.688 0.38 1 132 29 29 THR CB C 68.038 0.24 1 133 29 29 THR N N 117.723 0.35 1 134 30 30 LEU H H 8.349 0.03 1 135 30 30 LEU C C 174.916 0.4 1 136 30 30 LEU CA C 55.141 0.38 1 137 30 30 LEU CB C 42.325 0.24 1 138 30 30 LEU N N 119.088 0.35 1 139 31 31 GLY H H 8.011 0.03 1 140 31 31 GLY C C 177.212 0.4 1 141 31 31 GLY CA C 46.184 0.38 1 142 31 31 GLY N N 108.954 0.35 1 143 32 32 VAL H H 7.857 0.03 1 144 32 32 VAL C C 178.422 0.4 1 145 32 32 VAL CA C 58.078 0.38 1 146 32 32 VAL CB C 34.009 0.24 1 147 32 32 VAL N N 111.193 0.35 1 148 33 33 SER H H 8.538 0.03 1 149 33 33 SER C C 178.774 0.4 1 150 33 33 SER CA C 55.889 0.38 1 151 33 33 SER CB C 64.652 0.24 1 152 33 33 SER N N 115.703 0.35 1 153 34 34 VAL H H 8.449 0.03 1 154 34 34 VAL C C 179.044 0.4 1 155 34 34 VAL CA C 58.429 0.38 1 156 34 34 VAL CB C 34.817 0.24 1 157 34 34 VAL N N 119.991 0.35 1 158 35 35 ASP H H 8.696 0.03 1 159 35 35 ASP C C 178.398 0.4 1 160 35 35 ASP CA C 52.622 0.38 1 161 35 35 ASP CB C 43.433 0.24 1 162 35 35 ASP N N 127.729 0.35 1 163 36 36 ILE H H 8.261 0.03 1 164 36 36 ILE C C 178.079 0.4 1 165 36 36 ILE CA C 60.248 0.38 1 166 36 36 ILE CB C 37.976 0.24 1 167 36 36 ILE N N 122.292 0.35 1 168 37 37 PHE H H 9.153 0.03 1 169 37 37 PHE C C 178.552 0.4 1 170 37 37 PHE CA C 55.842 0.38 1 171 37 37 PHE CB C 43.948 0.24 1 172 37 37 PHE N N 125.638 0.35 1 173 38 38 ALA H H 8.488 0.03 1 174 38 38 ALA C C 176.317 0.4 1 175 38 38 ALA CA C 50.603 0.38 1 176 38 38 ALA CB C 21.447 0.24 1 177 38 38 ALA N N 120.226 0.35 1 178 39 39 SER H H 7.620 0.03 1 179 39 39 SER CA C 57.192 0.38 1 180 39 39 SER CB C 62.405 0.24 1 181 39 39 SER N N 115.409 0.35 1 182 40 40 PRO CA C 64.440 0.38 1 183 40 40 PRO CB C 31.270 0.24 1 184 41 41 SER H H 7.458 0.03 1 185 41 41 SER CA C 56.471 0.38 1 186 41 41 SER CB C 63.546 0.24 1 187 41 41 SER N N 110.579 0.35 1 188 42 42 GLU CA C 57.464 0.38 1 189 42 42 GLU CB C 28.570 0.24 1 190 43 43 GLY H H 8.304 0.03 1 191 43 43 GLY C C 178.904 0.4 1 192 43 43 GLY CA C 44.540 0.38 1 193 43 43 GLY N N 107.520 0.35 1 194 44 44 ASP H H 7.022 0.03 1 195 44 44 ASP CA C 52.597 0.38 1 196 44 44 ASP CB C 40.072 0.24 1 197 44 44 ASP N N 120.362 0.35 1 198 45 45 PHE H H 7.842 0.03 1 199 45 45 PHE C C 175.027 0.4 1 200 45 45 PHE CA C 59.621 0.38 1 201 45 45 PHE CB C 37.864 0.24 1 202 45 45 PHE N N 123.706 0.35 1 203 46 46 GLN H H 8.519 0.03 1 204 46 46 GLN C C 174.020 0.4 1 205 46 46 GLN CA C 57.793 0.38 1 206 46 46 GLN CB C 27.121 0.24 1 207 46 46 GLN N N 119.599 0.35 1 208 47 47 SER H H 8.222 0.03 1 209 47 47 SER CA C 60.824 0.38 1 210 47 47 SER CB C 61.935 0.24 1 211 47 47 SER N N 116.447 0.35 1 212 48 48 GLN H H 7.676 0.03 1 213 48 48 GLN C C 177.284 0.4 1 214 48 48 GLN CA C 58.959 0.38 1 215 48 48 GLN CB C 27.984 0.24 1 216 48 48 GLN N N 121.363 0.35 1 217 49 49 LEU H H 7.560 0.03 1 218 49 49 LEU CA C 59.198 0.38 1 219 49 49 LEU CB C 40.514 0.24 1 220 49 49 LEU N N 121.219 0.35 1 221 50 50 GLN H H 8.190 0.03 1 222 50 50 GLN C C 174.087 0.4 1 223 50 50 GLN CA C 58.319 0.38 1 224 50 50 GLN CB C 27.564 0.24 1 225 50 50 GLN N N 118.682 0.35 1 226 51 51 LEU H H 7.790 0.03 1 227 51 51 LEU C C 174.776 0.4 1 228 51 51 LEU CA C 57.329 0.38 1 229 51 51 LEU CB C 40.957 0.24 1 230 51 51 LEU N N 120.388 0.35 1 231 52 52 PHE H H 8.362 0.03 1 232 52 52 PHE C C 174.081 0.4 1 233 52 52 PHE CA C 61.800 0.38 1 234 52 52 PHE CB C 39.362 0.24 1 235 52 52 PHE N N 119.130 0.35 1 236 53 53 GLU H H 8.663 0.03 1 237 53 53 GLU C C 173.288 0.4 1 238 53 53 GLU CA C 59.471 0.38 1 239 53 53 GLU CB C 28.700 0.24 1 240 53 53 GLU N N 118.396 0.35 1 241 54 54 ASP H H 8.058 0.03 1 242 54 54 ASP C C 172.890 0.4 1 243 54 54 ASP CA C 57.110 0.38 1 244 54 54 ASP CB C 40.225 0.24 1 245 54 54 ASP N N 119.809 0.35 1 246 55 55 LEU H H 8.101 0.03 1 247 55 55 LEU C C 172.325 0.4 1 248 55 55 LEU CA C 57.225 0.38 1 249 55 55 LEU CB C 39.756 0.24 1 250 55 55 LEU N N 118.211 0.35 1 251 56 56 SER H H 8.214 0.03 1 252 56 56 SER C C 177.637 0.4 1 253 56 56 SER CA C 60.440 0.38 1 254 56 56 SER CB C 62.308 0.24 1 255 56 56 SER N N 113.715 0.35 1 256 57 57 ASN H H 7.479 0.03 1 257 57 57 ASN C C 176.706 0.4 1 258 57 57 ASN CA C 53.096 0.38 1 259 57 57 ASN CB C 38.651 0.24 1 260 57 57 ASN N N 118.441 0.35 1 261 58 58 LYS H H 7.444 0.03 1 262 58 58 LYS C C 175.725 0.4 1 263 58 58 LYS CA C 55.291 0.38 1 264 58 58 LYS CB C 31.311 0.24 1 265 58 58 LYS N N 120.271 0.35 1 266 59 59 ASN H H 7.893 0.03 1 267 59 59 ASN C C 177.050 0.4 1 268 59 59 ASN CA C 53.311 0.38 1 269 59 59 ASN CB C 36.879 0.24 1 270 59 59 ASN N N 115.865 0.35 1 271 60 60 TYR H H 7.458 0.03 1 272 60 60 TYR C C 176.074 0.4 1 273 60 60 TYR CA C 59.589 0.38 1 274 60 60 TYR CB C 37.973 0.24 1 275 60 60 TYR N N 118.111 0.35 1 276 61 61 LYS H H 9.059 0.03 1 277 61 61 LYS C C 174.450 0.4 1 278 61 61 LYS CA C 57.518 0.38 1 279 61 61 LYS CB C 32.593 0.24 1 280 61 61 LYS N N 119.799 0.35 1 281 62 62 GLY H H 7.244 0.03 1 282 62 62 GLY C C 180.577 0.4 1 283 62 62 GLY CA C 46.149 0.38 1 284 62 62 GLY N N 103.375 0.35 1 285 63 63 ILE H H 8.611 0.03 1 286 63 63 ILE C C 177.469 0.4 1 287 63 63 ILE CA C 59.853 0.38 1 288 63 63 ILE CB C 41.671 0.24 1 289 63 63 ILE N N 122.089 0.35 1 290 64 64 ALA H H 8.866 0.03 1 291 64 64 ALA C C 175.218 0.4 1 292 64 64 ALA CA C 48.427 0.38 1 293 64 64 ALA CB C 18.721 0.24 1 294 64 64 ALA N N 128.595 0.35 1 295 65 65 PHE H H 8.955 0.03 1 296 65 65 PHE C C 180.602 0.4 1 297 65 65 PHE CA C 54.914 0.38 1 298 65 65 PHE CB C 42.212 0.24 1 299 65 65 PHE N N 115.861 0.35 1 300 66 66 ALA H H 8.678 0.03 1 301 66 66 ALA CA C 47.305 0.38 1 302 66 66 ALA CB C 21.136 0.24 1 303 66 66 ALA N N 130.574 0.35 1 304 67 67 PRO C C 176.310 0.4 1 305 67 67 PRO CA C 61.810 0.38 1 306 67 67 PRO CB C 31.560 0.24 1 307 68 68 LEU H H 8.605 0.03 1 308 68 68 LEU C C 174.749 0.4 1 309 68 68 LEU CA C 56.430 0.38 1 310 68 68 LEU CB C 42.113 0.24 1 311 68 68 LEU N N 119.255 0.35 1 312 69 69 SER H H 8.271 0.03 1 313 69 69 SER CA C 55.243 0.38 1 314 69 69 SER CB C 66.500 0.24 1 315 69 69 SER N N 113.131 0.35 1 316 70 70 SER C C 175.542 0.4 1 317 70 70 SER CA C 60.590 0.38 1 318 70 70 SER CB C 62.000 0.24 1 319 71 71 VAL H H 7.431 0.03 1 320 71 71 VAL C C 178.201 0.4 1 321 71 71 VAL CA C 61.043 0.38 1 322 71 71 VAL CB C 33.183 0.24 1 323 71 71 VAL N N 111.613 0.35 1 324 72 72 ASN H H 7.937 0.03 1 325 72 72 ASN C C 176.668 0.4 1 326 72 72 ASN CA C 57.517 0.38 1 327 72 72 ASN CB C 36.922 0.24 1 328 72 72 ASN N N 122.499 0.35 1 329 73 73 LEU H H 8.651 0.03 1 330 73 73 LEU C C 176.035 0.4 1 331 73 73 LEU CA C 52.485 0.38 1 332 73 73 LEU CB C 40.557 0.24 1 333 73 73 LEU N N 116.412 0.35 1 334 74 74 VAL H H 7.001 0.03 1 335 74 74 VAL CA C 68.038 0.38 1 336 74 74 VAL CB C 30.452 0.24 1 337 74 74 VAL N N 119.076 0.35 1 338 75 75 MET H H 8.463 0.03 1 339 75 75 MET CA C 58.195 0.38 1 340 75 75 MET CB C 26.936 0.24 1 341 75 75 MET N N 113.324 0.35 1 342 76 76 PRO C C 172.930 0.4 1 343 76 76 PRO CA C 64.960 0.38 1 344 76 76 PRO CB C 30.190 0.24 1 345 77 77 VAL H H 7.723 0.03 1 346 77 77 VAL C C 175.451 0.4 1 347 77 77 VAL CA C 66.502 0.38 1 348 77 77 VAL CB C 29.633 0.24 1 349 77 77 VAL N N 121.156 0.35 1 350 78 78 ALA H H 8.102 0.03 1 351 78 78 ALA CA C 55.973 0.38 1 352 78 78 ALA CB C 17.160 0.24 1 353 78 78 ALA N N 122.406 0.35 1 354 79 79 ARG H H 7.823 0.03 1 355 79 79 ARG CA C 59.422 0.38 1 356 79 79 ARG CB C 29.640 0.24 1 357 79 79 ARG N N 115.817 0.35 1 358 80 80 ALA H H 8.198 0.03 1 359 80 80 ALA C C 173.578 0.4 1 360 80 80 ALA CA C 54.596 0.38 1 361 80 80 ALA CB C 17.556 0.24 1 362 80 80 ALA N N 122.435 0.35 1 363 81 81 TRP H H 8.904 0.03 1 364 81 81 TRP C C 171.750 0.4 1 365 81 81 TRP CA C 62.763 0.38 1 366 81 81 TRP CB C 27.361 0.24 1 367 81 81 TRP N N 123.498 0.35 1 368 82 82 LYS H H 8.237 0.03 1 369 82 82 LYS C C 174.326 0.4 1 370 82 82 LYS CA C 58.961 0.38 1 371 82 82 LYS CB C 32.232 0.24 1 372 82 82 LYS N N 119.957 0.35 1 373 83 83 LYS H H 7.411 0.03 1 374 83 83 LYS C C 175.877 0.4 1 375 83 83 LYS CA C 56.005 0.38 1 376 83 83 LYS CB C 31.948 0.24 1 377 83 83 LYS N N 116.839 0.35 1 378 84 84 GLY H H 7.865 0.03 1 379 84 84 GLY C C 178.725 0.4 1 380 84 84 GLY CA C 44.972 0.38 1 381 84 84 GLY N N 108.002 0.35 1 382 85 85 ILE H H 7.385 0.03 1 383 85 85 ILE C C 178.284 0.4 1 384 85 85 ILE CA C 61.123 0.38 1 385 85 85 ILE CB C 37.368 0.24 1 386 85 85 ILE N N 122.179 0.35 1 387 86 86 TYR H H 7.789 0.03 1 388 86 86 TYR C C 177.024 0.4 1 389 86 86 TYR CA C 58.737 0.38 1 390 86 86 TYR CB C 38.094 0.24 1 391 86 86 TYR N N 125.019 0.35 1 392 87 87 LEU H H 9.488 0.03 1 393 87 87 LEU C C 175.453 0.4 1 394 87 87 LEU CA C 54.109 0.38 1 395 87 87 LEU CB C 46.057 0.24 1 396 87 87 LEU N N 128.181 0.35 1 397 88 88 VAL H H 8.288 0.03 1 398 88 88 VAL C C 179.959 0.4 1 399 88 88 VAL CA C 61.005 0.38 1 400 88 88 VAL CB C 35.203 0.24 1 401 88 88 VAL N N 119.796 0.35 1 402 89 89 ASN H H 8.640 0.03 1 403 89 89 ASN C C 179.852 0.4 1 404 89 89 ASN CA C 50.073 0.38 1 405 89 89 ASN CB C 41.496 0.24 1 406 89 89 ASN N N 126.837 0.35 1 407 90 90 LEU H H 9.157 0.03 1 408 90 90 LEU CA C 53.410 0.38 1 409 90 90 LEU CB C 42.810 0.24 1 410 90 90 LEU N N 127.907 0.35 1 411 91 91 ASP H H 8.921 0.03 1 412 91 91 ASP C C 178.538 0.4 1 413 91 91 ASP CA C 60.460 0.38 1 414 91 91 ASP CB C 42.929 0.24 1 415 91 91 ASP N N 116.712 0.35 1 416 92 92 GLU H H 9.257 0.03 1 417 92 92 GLU C C 177.650 0.4 1 418 92 92 GLU CA C 54.490 0.38 1 419 92 92 GLU CB C 30.917 0.24 1 420 92 92 GLU N N 127.064 0.35 1 421 93 93 LYS H H 8.383 0.03 1 422 93 93 LYS C C 174.817 0.4 1 423 93 93 LYS CA C 57.320 0.38 1 424 93 93 LYS CB C 32.076 0.24 1 425 93 93 LYS N N 129.109 0.35 1 426 94 94 ILE H H 8.816 0.03 1 427 94 94 ILE C C 175.444 0.4 1 428 94 94 ILE CA C 60.956 0.38 1 429 94 94 ILE CB C 39.242 0.24 1 430 94 94 ILE N N 128.541 0.35 1 431 95 95 ASP H H 8.009 0.03 1 432 95 95 ASP C C 176.731 0.4 1 433 95 95 ASP CA C 53.568 0.38 1 434 95 95 ASP CB C 40.199 0.24 1 435 95 95 ASP N N 122.292 0.35 1 436 96 96 MET H H 8.152 0.03 1 437 96 96 MET C C 173.649 0.4 1 438 96 96 MET CA C 56.231 0.38 1 439 96 96 MET CB C 29.774 0.24 1 440 96 96 MET N N 129.210 0.35 1 441 97 97 ASP H H 8.130 0.03 1 442 97 97 ASP C C 173.507 0.4 1 443 97 97 ASP CA C 57.064 0.38 1 444 97 97 ASP CB C 39.942 0.24 1 445 97 97 ASP N N 120.815 0.35 1 446 98 98 ASN H H 8.250 0.03 1 447 98 98 ASN C C 174.448 0.4 1 448 98 98 ASN CA C 55.490 0.38 1 449 98 98 ASN CB C 37.685 0.24 1 450 98 98 ASN N N 119.077 0.35 1 451 99 99 LEU H H 8.512 0.03 1 452 99 99 LEU C C 174.645 0.4 1 453 99 99 LEU CA C 57.982 0.38 1 454 99 99 LEU CB C 40.815 0.24 1 455 99 99 LEU N N 122.814 0.35 1 456 100 100 LYS H H 8.051 0.03 1 457 100 100 LYS C C 170.501 0.4 1 458 100 100 LYS CA C 59.075 0.38 1 459 100 100 LYS CB C 30.522 0.24 1 460 100 100 LYS N N 119.500 0.35 1 461 101 101 LYS H H 7.639 0.03 1 462 101 101 LYS C C 174.431 0.4 1 463 101 101 LYS CA C 58.977 0.38 1 464 101 101 LYS CB C 31.421 0.24 1 465 101 101 LYS N N 120.944 0.35 1 466 102 102 ALA H H 7.555 0.03 1 467 102 102 ALA C C 175.631 0.4 1 468 102 102 ALA CA C 51.849 0.38 1 469 102 102 ALA CB C 18.089 0.24 1 470 102 102 ALA N N 120.496 0.35 1 471 103 103 GLY H H 7.796 0.03 1 472 103 103 GLY C C 179.314 0.4 1 473 103 103 GLY CA C 45.386 0.38 1 474 103 103 GLY N N 106.461 0.35 1 475 104 104 GLY H H 7.442 0.03 1 476 104 104 GLY C C 184.316 0.4 1 477 104 104 GLY CA C 43.135 0.38 1 478 104 104 GLY N N 104.055 0.35 1 479 105 105 ASN H H 6.077 0.03 1 480 105 105 ASN C C 180.753 0.4 1 481 105 105 ASN CA C 49.425 0.38 1 482 105 105 ASN CB C 40.038 0.24 1 483 105 105 ASN N N 111.475 0.35 1 484 106 106 VAL H H 7.886 0.03 1 485 106 106 VAL C C 178.762 0.4 1 486 106 106 VAL CA C 58.462 0.38 1 487 106 106 VAL CB C 34.071 0.24 1 488 106 106 VAL N N 104.999 0.35 1 489 107 107 GLU H H 9.170 0.03 1 490 107 107 GLU C C 173.210 0.4 1 491 107 107 GLU CA C 57.493 0.38 1 492 107 107 GLU CB C 29.423 0.24 1 493 107 107 GLU N N 114.226 0.35 1 494 108 108 ALA H H 7.242 0.03 1 495 108 108 ALA C C 178.477 0.4 1 496 108 108 ALA CA C 50.263 0.38 1 497 108 108 ALA CB C 23.323 0.24 1 498 108 108 ALA N N 111.045 0.35 1 499 109 109 PHE H H 8.799 0.03 1 500 109 109 PHE C C 179.351 0.4 1 501 109 109 PHE CA C 54.034 0.38 1 502 109 109 PHE CB C 41.149 0.24 1 503 109 109 PHE N N 121.838 0.35 1 504 110 110 VAL H H 7.885 0.03 1 505 110 110 VAL C C 178.899 0.4 1 506 110 110 VAL CA C 59.205 0.38 1 507 110 110 VAL CB C 32.872 0.24 1 508 110 110 VAL N N 125.833 0.35 1 509 111 111 THR H H 7.863 0.03 1 510 111 111 THR C C 180.943 0.4 1 511 111 111 THR CA C 59.181 0.38 1 512 111 111 THR CB C 68.347 0.24 1 513 111 111 THR N N 119.907 0.35 1 514 112 112 THR H H 8.221 0.03 1 515 112 112 THR C C 179.111 0.4 1 516 112 112 THR CA C 61.917 0.38 1 517 112 112 THR CB C 69.365 0.24 1 518 112 112 THR N N 119.524 0.35 1 519 113 113 ASP H H 8.863 0.03 1 520 113 113 ASP CA C 52.850 0.38 1 521 113 113 ASP CB C 40.541 0.24 1 522 113 113 ASP N N 124.686 0.35 1 523 114 114 ASN C C 173.404 0.4 1 524 114 114 ASN CA C 56.828 0.38 1 525 114 114 ASN CB C 40.570 0.24 1 526 115 115 VAL H H 8.169 0.03 1 527 115 115 VAL C C 173.920 0.4 1 528 115 115 VAL CA C 65.229 0.38 1 529 115 115 VAL CB C 30.152 0.24 1 530 115 115 VAL N N 122.499 0.35 1 531 116 116 ALA H H 7.043 0.03 1 532 116 116 ALA C C 171.582 0.4 1 533 116 116 ALA CA C 53.597 0.38 1 534 116 116 ALA CB C 17.282 0.24 1 535 116 116 ALA N N 121.833 0.35 1 536 117 117 VAL H H 7.703 0.03 1 537 117 117 VAL C C 175.005 0.4 1 538 117 117 VAL CA C 65.715 0.38 1 539 117 117 VAL CB C 30.642 0.24 1 540 117 117 VAL N N 119.611 0.35 1 541 118 118 GLY H H 7.401 0.03 1 542 118 118 GLY CA C 46.635 0.38 1 543 118 118 GLY N N 105.523 0.35 1 544 119 119 ALA H H 8.112 0.03 1 545 119 119 ALA C C 172.383 0.4 1 546 119 119 ALA CA C 54.473 0.38 1 547 119 119 ALA CB C 17.248 0.24 1 548 119 119 ALA N N 122.123 0.35 1 549 120 120 LYS H H 8.349 0.03 1 550 120 120 LYS C C 174.158 0.4 1 551 120 120 LYS CA C 59.023 0.38 1 552 120 120 LYS CB C 30.448 0.24 1 553 120 120 LYS N N 121.867 0.35 1 554 121 121 GLY H H 7.913 0.03 1 555 121 121 GLY C C 173.889 0.4 1 556 121 121 GLY CA C 47.073 0.38 1 557 121 121 GLY N N 107.028 0.35 1 558 122 122 ALA H H 7.606 0.03 1 559 122 122 ALA C C 173.140 0.4 1 560 122 122 ALA CA C 54.315 0.38 1 561 122 122 ALA CB C 18.434 0.24 1 562 122 122 ALA N N 121.170 0.35 1 563 123 123 SER H H 8.701 0.03 1 564 123 123 SER C C 176.639 0.4 1 565 123 123 SER CA C 61.917 0.38 1 566 123 123 SER CB C 61.835 0.24 1 567 123 123 SER N N 114.247 0.35 1 568 124 124 PHE H H 7.720 0.03 1 569 124 124 PHE C C 175.888 0.4 1 570 124 124 PHE CA C 60.661 0.38 1 571 124 124 PHE CB C 37.959 0.24 1 572 124 124 PHE N N 122.520 0.35 1 573 125 125 ILE H H 7.215 0.03 1 574 125 125 ILE C C 175.927 0.4 1 575 125 125 ILE CA C 65.587 0.38 1 576 125 125 ILE CB C 37.116 0.24 1 577 125 125 ILE N N 119.161 0.35 1 578 126 126 ILE H H 8.718 0.03 1 579 126 126 ILE C C 173.137 0.4 1 580 126 126 ILE CA C 65.547 0.38 1 581 126 126 ILE CB C 37.536 0.24 1 582 126 126 ILE N N 119.339 0.35 1 583 127 127 ASP H H 8.122 0.03 1 584 127 127 ASP C C 172.818 0.4 1 585 127 127 ASP CA C 56.829 0.38 1 586 127 127 ASP CB C 40.125 0.24 1 587 127 127 ASP N N 120.278 0.35 1 588 128 128 LYS H H 7.852 0.03 1 589 128 128 LYS C C 173.161 0.4 1 590 128 128 LYS CA C 56.578 0.38 1 591 128 128 LYS CB C 30.605 0.24 1 592 128 128 LYS N N 118.543 0.35 1 593 129 129 LEU H H 8.145 0.03 1 594 129 129 LEU C C 173.064 0.4 1 595 129 129 LEU CA C 55.720 0.38 1 596 129 129 LEU CB C 39.827 0.24 1 597 129 129 LEU N N 117.607 0.35 1 598 130 130 GLY H H 7.279 0.03 1 599 130 130 GLY CA C 44.976 0.38 1 600 130 130 GLY N N 104.444 0.35 1 601 131 131 ALA H H 8.600 0.03 1 602 131 131 ALA C C 172.689 0.4 1 603 131 131 ALA CA C 54.315 0.38 1 604 131 131 ALA CB C 17.724 0.24 1 605 131 131 ALA N N 124.451 0.35 1 606 132 132 GLU H H 8.470 0.03 1 607 132 132 GLU C C 174.029 0.4 1 608 132 132 GLU CA C 57.778 0.38 1 609 132 132 GLU CB C 28.991 0.24 1 610 132 132 GLU N N 114.454 0.35 1 611 133 133 GLY H H 7.193 0.03 1 612 133 133 GLY C C 179.813 0.4 1 613 133 133 GLY CA C 45.231 0.38 1 614 133 133 GLY N N 103.909 0.35 1 615 134 134 GLY H H 7.920 0.03 1 616 134 134 GLY C C 180.632 0.4 1 617 134 134 GLY CA C 43.842 0.38 1 618 134 134 GLY N N 108.660 0.35 1 619 135 135 GLU H H 8.534 0.03 1 620 135 135 GLU C C 175.388 0.4 1 621 135 135 GLU CA C 54.736 0.38 1 622 135 135 GLU CB C 30.293 0.24 1 623 135 135 GLU N N 119.101 0.35 1 624 136 136 VAL H H 8.849 0.03 1 625 136 136 VAL C C 178.716 0.4 1 626 136 136 VAL CA C 57.741 0.38 1 627 136 136 VAL CB C 35.123 0.24 1 628 136 136 VAL N N 115.022 0.35 1 629 137 137 ALA H H 8.053 0.03 1 630 137 137 ALA C C 177.431 0.4 1 631 137 137 ALA CA C 49.261 0.38 1 632 137 137 ALA CB C 23.612 0.24 1 633 137 137 ALA N N 119.907 0.35 1 634 138 138 ILE H H 8.437 0.03 1 635 138 138 ILE C C 177.841 0.4 1 636 138 138 ILE CA C 59.402 0.38 1 637 138 138 ILE CB C 40.792 0.24 1 638 138 138 ILE N N 119.198 0.35 1 639 139 139 ILE H H 8.858 0.03 1 640 139 139 ILE C C 177.145 0.4 1 641 139 139 ILE CA C 57.126 0.38 1 642 139 139 ILE CB C 34.798 0.24 1 643 139 139 ILE N N 126.984 0.35 1 644 140 140 GLU H H 8.341 0.03 1 645 140 140 GLU C C 174.820 0.4 1 646 140 140 GLU CA C 54.065 0.38 1 647 140 140 GLU CB C 31.086 0.24 1 648 140 140 GLU N N 125.751 0.35 1 649 141 141 GLY H H 8.094 0.03 1 650 141 141 GLY CA C 41.564 0.38 1 651 141 141 GLY N N 104.937 0.35 1 652 142 142 LYS C C 175.899 0.4 1 653 143 143 ALA H H 8.974 0.03 1 654 143 143 ALA CA C 53.303 0.38 1 655 143 143 ALA CB C 17.420 0.24 1 656 143 143 ALA N N 131.864 0.35 1 657 144 144 GLY H H 9.169 0.03 1 658 144 144 GLY CA C 44.762 0.38 1 659 144 144 GLY N N 111.218 0.35 1 660 147 147 SER C C 175.341 0.4 1 661 148 148 GLY C C 174.646 0.4 1 662 149 149 GLU H H 8.832 0.03 1 663 149 149 GLU C C 179.817 0.4 1 664 149 149 GLU CA C 58.596 0.38 1 665 149 149 GLU CB C 28.312 0.24 1 666 149 149 GLU N N 125.265 0.35 1 667 150 150 ALA H H 7.903 0.03 1 668 150 150 ALA C C 172.850 0.4 1 669 150 150 ALA CA C 54.896 0.38 1 670 150 150 ALA CB C 18.559 0.24 1 671 150 150 ALA N N 121.952 0.35 1 672 151 151 ARG H H 7.779 0.03 1 673 151 151 ARG C C 173.364 0.4 1 674 151 151 ARG CA C 59.399 0.38 1 675 151 151 ARG CB C 29.117 0.24 1 676 151 151 ARG N N 117.180 0.35 1 677 152 152 ARG H H 8.210 0.03 1 678 152 152 ARG C C 172.601 0.4 1 679 152 152 ARG CA C 59.626 0.38 1 680 152 152 ARG CB C 28.458 0.24 1 681 152 152 ARG N N 117.862 0.35 1 682 153 153 ASN H H 9.216 0.03 1 683 153 153 ASN C C 174.753 0.4 1 684 153 153 ASN CA C 56.208 0.38 1 685 153 153 ASN CB C 37.358 0.24 1 686 153 153 ASN N N 123.313 0.35 1 687 154 154 GLY H H 8.986 0.03 1 688 154 154 GLY C C 176.918 0.4 1 689 154 154 GLY CA C 47.253 0.38 1 690 154 154 GLY N N 107.550 0.35 1 691 155 155 ALA H H 7.762 0.03 1 692 155 155 ALA C C 174.497 0.4 1 693 155 155 ALA CA C 54.032 0.38 1 694 155 155 ALA CB C 17.447 0.24 1 695 155 155 ALA N N 121.553 0.35 1 696 156 156 THR H H 8.378 0.03 1 697 156 156 THR C C 173.273 0.4 1 698 156 156 THR CA C 67.712 0.38 1 699 156 156 THR CB C 67.305 0.24 1 700 156 156 THR N N 114.145 0.35 1 701 157 157 GLU H H 8.259 0.03 1 702 157 157 GLU C C 173.914 0.4 1 703 157 157 GLU CA C 58.630 0.38 1 704 157 157 GLU CB C 28.231 0.24 1 705 157 157 GLU N N 119.686 0.35 1 706 158 158 ALA H H 7.007 0.03 1 707 158 158 ALA C C 171.369 0.4 1 708 158 158 ALA CA C 54.526 0.38 1 709 158 158 ALA CB C 17.152 0.24 1 710 158 158 ALA N N 120.247 0.35 1 711 159 159 PHE H H 8.253 0.03 1 712 159 159 PHE C C 173.803 0.4 1 713 159 159 PHE CA C 58.520 0.38 1 714 159 159 PHE CB C 37.156 0.24 1 715 159 159 PHE N N 115.930 0.35 1 716 160 160 LYS H H 8.286 0.03 1 717 160 160 LYS C C 174.713 0.4 1 718 160 160 LYS CA C 58.423 0.38 1 719 160 160 LYS CB C 31.488 0.24 1 720 160 160 LYS N N 117.748 0.35 1 721 161 161 LYS H H 7.065 0.03 1 722 161 161 LYS C C 176.850 0.4 1 723 161 161 LYS CA C 56.635 0.38 1 724 161 161 LYS CB C 31.948 0.24 1 725 161 161 LYS N N 115.817 0.35 1 726 162 162 ALA H H 7.389 0.03 1 727 162 162 ALA CA C 50.179 0.38 1 728 162 162 ALA CB C 18.748 0.24 1 729 162 162 ALA N N 124.905 0.35 1 730 163 163 SER H H 8.376 0.03 1 731 163 163 SER C C 177.412 0.4 1 732 163 163 SER CA C 60.930 0.38 1 733 163 163 SER CB C 62.385 0.24 1 734 163 163 SER N N 119.374 0.35 1 735 164 164 GLN H H 9.579 0.03 1 736 164 164 GLN C C 176.983 0.4 1 737 164 164 GLN CA C 55.904 0.38 1 738 164 164 GLN CB C 25.384 0.24 1 739 164 164 GLN N N 120.020 0.35 1 740 165 165 ILE H H 8.105 0.03 1 741 165 165 ILE C C 177.374 0.4 1 742 165 165 ILE CA C 56.811 0.38 1 743 165 165 ILE CB C 34.650 0.24 1 744 165 165 ILE N N 126.158 0.35 1 745 166 166 LYS H H 8.165 0.03 1 746 166 166 LYS C C 178.177 0.4 1 747 166 166 LYS CA C 53.896 0.38 1 748 166 166 LYS CB C 33.521 0.24 1 749 166 166 LYS N N 127.388 0.35 1 750 167 167 LEU H H 8.775 0.03 1 751 167 167 LEU C C 175.318 0.4 1 752 167 167 LEU CA C 53.904 0.38 1 753 167 167 LEU CB C 40.324 0.24 1 754 167 167 LEU N N 129.275 0.35 1 755 168 168 VAL H H 8.716 0.03 1 756 168 168 VAL C C 176.657 0.4 1 757 168 168 VAL CA C 61.315 0.38 1 758 168 168 VAL CB C 31.586 0.24 1 759 168 168 VAL N N 120.833 0.35 1 760 169 169 ALA H H 7.069 0.03 1 761 169 169 ALA CA C 52.076 0.38 1 762 169 169 ALA CB C 21.347 0.24 1 763 169 169 ALA N N 119.651 0.35 1 764 170 170 SER H H 8.306 0.03 1 765 170 170 SER CA C 57.399 0.38 1 766 170 170 SER CB C 62.772 0.24 1 767 170 170 SER N N 119.015 0.35 1 768 171 171 GLN H H 8.322 0.03 1 769 171 171 GLN CA C 51.813 0.38 1 770 171 171 GLN CB C 32.376 0.24 1 771 171 171 GLN N N 123.807 0.35 1 772 172 172 PRO CA C 62.230 0.38 1 773 172 172 PRO CB C 32.500 0.24 1 774 173 173 ALA H H 8.555 0.03 1 775 173 173 ALA C C 173.069 0.4 1 776 173 173 ALA CA C 50.950 0.38 1 777 173 173 ALA CB C 17.734 0.24 1 778 173 173 ALA N N 119.566 0.35 1 779 174 174 ASP H H 7.079 0.03 1 780 174 174 ASP C C 172.940 0.4 1 781 174 174 ASP CA C 56.012 0.38 1 782 174 174 ASP CB C 37.841 0.24 1 783 174 174 ASP N N 111.613 0.35 1 784 175 175 TRP H H 7.558 0.03 1 785 175 175 TRP CA C 56.300 0.38 1 786 175 175 TRP CB C 28.094 0.24 1 787 175 175 TRP N N 109.001 0.35 1 788 176 176 ASP H H 8.045 0.03 1 789 176 176 ASP C C 177.182 0.4 1 790 176 176 ASP CA C 53.390 0.38 1 791 176 176 ASP CB C 44.843 0.24 1 792 176 176 ASP N N 122.179 0.35 1 793 177 177 ARG H H 8.748 0.03 1 794 177 177 ARG C C 175.302 0.4 1 795 177 177 ARG CA C 59.965 0.38 1 796 177 177 ARG CB C 30.966 0.24 1 797 177 177 ARG N N 127.745 0.35 1 798 178 178 ILE H H 7.751 0.03 1 799 178 178 ILE C C 173.301 0.4 1 800 178 178 ILE CA C 62.853 0.38 1 801 178 178 ILE CB C 35.342 0.24 1 802 178 178 ILE N N 119.339 0.35 1 803 179 179 LYS H H 8.845 0.03 1 804 179 179 LYS C C 173.488 0.4 1 805 179 179 LYS CA C 58.861 0.38 1 806 179 179 LYS CB C 30.723 0.24 1 807 179 179 LYS N N 122.179 0.35 1 808 180 180 ALA H H 8.288 0.03 1 809 180 180 ALA CA C 55.235 0.38 1 810 180 180 ALA CB C 18.646 0.24 1 811 180 180 ALA N N 119.566 0.35 1 812 181 181 LEU H H 7.648 0.03 1 813 181 181 LEU C C 172.310 0.4 1 814 181 181 LEU CA C 58.735 0.38 1 815 181 181 LEU CB C 41.074 0.24 1 816 181 181 LEU N N 121.043 0.35 1 817 182 182 ASP H H 8.016 0.03 1 818 182 182 ASP C C 173.361 0.4 1 819 182 182 ASP CA C 57.739 0.38 1 820 182 182 ASP CB C 40.364 0.24 1 821 182 182 ASP N N 123.883 0.35 1 822 183 183 VAL H H 9.118 0.03 1 823 183 183 VAL C C 173.293 0.4 1 824 183 183 VAL CA C 65.911 0.38 1 825 183 183 VAL CB C 31.408 0.24 1 826 183 183 VAL N N 121.440 0.35 1 827 184 184 ALA H H 9.027 0.03 1 828 184 184 ALA C C 173.694 0.4 1 829 184 184 ALA CA C 54.703 0.38 1 830 184 184 ALA CB C 18.868 0.24 1 831 184 184 ALA N N 120.278 0.35 1 832 185 185 THR H H 8.111 0.03 1 833 185 185 THR C C 178.220 0.4 1 834 185 185 THR CA C 67.325 0.38 1 835 185 185 THR CB C 68.154 0.24 1 836 185 185 THR N N 115.501 0.35 1 837 186 186 ASN H H 7.413 0.03 1 838 186 186 ASN C C 174.973 0.4 1 839 186 186 ASN CA C 56.566 0.38 1 840 186 186 ASN CB C 38.406 0.24 1 841 186 186 ASN N N 120.056 0.35 1 842 187 187 VAL H H 8.530 0.03 1 843 187 187 VAL C C 174.025 0.4 1 844 187 187 VAL CA C 66.147 0.38 1 845 187 187 VAL CB C 30.721 0.24 1 846 187 187 VAL N N 121.148 0.35 1 847 188 188 LEU H H 8.389 0.03 1 848 188 188 LEU C C 173.585 0.4 1 849 188 188 LEU CA C 57.011 0.38 1 850 188 188 LEU CB C 40.784 0.24 1 851 188 188 LEU N N 119.191 0.35 1 852 189 189 GLN H H 7.521 0.03 1 853 189 189 GLN C C 174.213 0.4 1 854 189 189 GLN CA C 57.820 0.38 1 855 189 189 GLN CB C 27.807 0.24 1 856 189 189 GLN N N 116.962 0.35 1 857 190 190 ARG H H 7.698 0.03 1 858 190 190 ARG C C 176.123 0.4 1 859 190 190 ARG CA C 56.992 0.38 1 860 190 190 ARG CB C 30.199 0.24 1 861 190 190 ARG N N 116.567 0.35 1 862 191 191 ASN H H 7.743 0.03 1 863 191 191 ASN CA C 51.506 0.38 1 864 191 191 ASN CB C 39.000 0.24 1 865 191 191 ASN N N 116.263 0.35 1 866 192 192 PRO C C 174.496 0.4 1 867 192 192 PRO CA C 63.887 0.38 1 868 192 192 PRO CB C 31.305 0.24 1 869 193 193 ASN H H 9.151 0.03 1 870 193 193 ASN C C 176.943 0.4 1 871 193 193 ASN CA C 52.016 0.38 1 872 193 193 ASN CB C 37.571 0.24 1 873 193 193 ASN N N 116.072 0.35 1 874 194 194 ILE H H 7.525 0.03 1 875 194 194 ILE C C 178.047 0.4 1 876 194 194 ILE CA C 62.404 0.38 1 877 194 194 ILE CB C 37.724 0.24 1 878 194 194 ILE N N 122.376 0.35 1 879 195 195 LYS H H 8.920 0.03 1 880 195 195 LYS C C 174.522 0.4 1 881 195 195 LYS CA C 55.341 0.38 1 882 195 195 LYS CB C 35.500 0.24 1 883 195 195 LYS N N 121.910 0.35 1 884 196 196 ALA H H 7.506 0.03 1 885 196 196 ALA C C 177.826 0.4 1 886 196 196 ALA CA C 51.371 0.38 1 887 196 196 ALA CB C 24.577 0.24 1 888 196 196 ALA N N 119.351 0.35 1 889 197 197 ILE H H 8.854 0.03 1 890 197 197 ILE C C 177.507 0.4 1 891 197 197 ILE CA C 60.122 0.38 1 892 197 197 ILE CB C 40.859 0.24 1 893 197 197 ILE N N 119.474 0.35 1 894 198 198 TYR H H 8.887 0.03 1 895 198 198 TYR CA C 56.391 0.38 1 896 198 198 TYR CB C 39.006 0.24 1 897 198 198 TYR N N 126.377 0.35 1 898 199 199 CYS H H 8.238 0.03 1 899 199 199 CYS C C 179.530 0.4 1 900 199 199 CYS CA C 55.348 0.38 1 901 199 199 CYS CB C 30.862 0.24 1 902 199 199 CYS N N 124.853 0.35 1 903 200 200 ALA H H 7.989 0.03 1 904 200 200 ALA C C 173.022 0.4 1 905 200 200 ALA CA C 52.907 0.38 1 906 200 200 ALA CB C 17.836 0.24 1 907 200 200 ALA N N 119.024 0.35 1 908 201 201 ASN H H 7.135 0.03 1 909 201 201 ASN CA C 52.226 0.38 1 910 201 201 ASN CB C 39.330 0.24 1 911 201 201 ASN N N 110.893 0.35 1 912 202 202 ASP H H 7.803 0.03 1 913 202 202 ASP C C 173.750 0.4 1 914 202 202 ASP CA C 56.647 0.38 1 915 202 202 ASP CB C 41.896 0.24 1 916 202 202 ASP N N 121.857 0.35 1 917 203 203 THR H H 7.810 0.03 1 918 203 203 THR C C 177.230 0.4 1 919 203 203 THR CA C 66.694 0.38 1 920 203 203 THR CB C 67.817 0.24 1 921 203 203 THR N N 117.058 0.35 1 922 204 204 MET H H 7.925 0.03 1 923 204 204 MET C C 174.172 0.4 1 924 204 204 MET CA C 58.912 0.38 1 925 204 204 MET CB C 31.524 0.24 1 926 204 204 MET N N 115.411 0.35 1 927 205 205 ALA H H 7.738 0.03 1 928 205 205 ALA C C 173.874 0.4 1 929 205 205 ALA CA C 55.101 0.38 1 930 205 205 ALA CB C 18.193 0.24 1 931 205 205 ALA N N 121.951 0.35 1 932 206 206 MET H H 8.342 0.03 1 933 206 206 MET CA C 59.460 0.38 1 934 206 206 MET CB C 31.983 0.24 1 935 206 206 MET N N 116.899 0.35 1 936 207 207 GLY H H 7.470 0.03 1 937 207 207 GLY C C 176.703 0.4 1 938 207 207 GLY CA C 46.609 0.38 1 939 207 207 GLY N N 108.666 0.35 1 940 208 208 VAL H H 8.359 0.03 1 941 208 208 VAL C C 174.759 0.4 1 942 208 208 VAL CA C 65.981 0.38 1 943 208 208 VAL CB C 29.342 0.24 1 944 208 208 VAL N N 123.088 0.35 1 945 209 209 ALA H H 8.976 0.03 1 946 209 209 ALA C C 171.749 0.4 1 947 209 209 ALA CA C 54.806 0.38 1 948 209 209 ALA CB C 17.089 0.24 1 949 209 209 ALA N N 121.497 0.35 1 950 210 210 GLN H H 7.390 0.03 1 951 210 210 GLN C C 175.147 0.4 1 952 210 210 GLN CA C 58.040 0.38 1 953 210 210 GLN CB C 27.313 0.24 1 954 210 210 GLN N N 119.452 0.35 1 955 211 211 ALA H H 7.934 0.03 1 956 211 211 ALA C C 171.570 0.4 1 957 211 211 ALA CA C 54.966 0.38 1 958 211 211 ALA CB C 18.470 0.24 1 959 211 211 ALA N N 124.337 0.35 1 960 212 212 VAL H H 8.593 0.03 1 961 212 212 VAL C C 174.605 0.4 1 962 212 212 VAL CA C 66.477 0.38 1 963 212 212 VAL CB C 30.840 0.24 1 964 212 212 VAL N N 119.794 0.35 1 965 213 213 ALA H H 7.968 0.03 1 966 213 213 ALA C C 169.675 0.4 1 967 213 213 ALA CA C 54.477 0.38 1 968 213 213 ALA CB C 17.026 0.24 1 969 213 213 ALA N N 123.738 0.35 1 970 214 214 ASN H H 8.791 0.03 1 971 214 214 ASN C C 176.441 0.4 1 972 214 214 ASN CA C 54.736 0.38 1 973 214 214 ASN CB C 36.722 0.24 1 974 214 214 ASN N N 120.588 0.35 1 975 215 215 ALA H H 7.434 0.03 1 976 215 215 ALA C C 175.154 0.4 1 977 215 215 ALA CA C 51.337 0.38 1 978 215 215 ALA CB C 18.313 0.24 1 979 215 215 ALA N N 119.679 0.35 1 980 216 216 GLY H H 8.139 0.03 1 981 216 216 GLY CA C 45.867 0.38 1 982 216 216 GLY N N 108.248 0.35 1 983 217 217 LYS H H 7.946 0.03 1 984 217 217 LYS C C 176.705 0.4 1 985 217 217 LYS CA C 54.938 0.38 1 986 217 217 LYS CB C 33.351 0.24 1 987 217 217 LYS N N 116.044 0.35 1 988 218 218 THR H H 8.127 0.03 1 989 218 218 THR CA C 66.120 0.38 1 990 218 218 THR CB C 67.565 0.24 1 991 218 218 THR N N 121.270 0.35 1 992 219 219 GLY H H 9.517 0.03 1 993 219 219 GLY CA C 45.087 0.38 1 994 219 219 GLY N N 117.507 0.35 1 995 220 220 LYS H H 8.063 0.03 1 996 220 220 LYS CA C 55.907 0.38 1 997 220 220 LYS CB C 32.438 0.24 1 998 220 220 LYS N N 118.657 0.35 1 999 221 221 VAL H H 7.026 0.03 1 1000 221 221 VAL C C 177.120 0.4 1 1001 221 221 VAL CA C 60.294 0.38 1 1002 221 221 VAL CB C 32.925 0.24 1 1003 221 221 VAL N N 118.657 0.35 1 1004 222 222 LEU H H 8.638 0.03 1 1005 222 222 LEU C C 175.927 0.4 1 1006 222 222 LEU CA C 54.716 0.38 1 1007 222 222 LEU CB C 40.442 0.24 1 1008 222 222 LEU N N 126.117 0.35 1 1009 223 223 VAL H H 8.544 0.03 1 1010 223 223 VAL C C 177.302 0.4 1 1011 223 223 VAL CA C 62.004 0.38 1 1012 223 223 VAL CB C 34.399 0.24 1 1013 223 223 VAL N N 121.674 0.35 1 1014 224 224 VAL H H 8.564 0.03 1 1015 224 224 VAL C C 177.392 0.4 1 1016 224 224 VAL CA C 59.883 0.38 1 1017 224 224 VAL CB C 34.412 0.24 1 1018 224 224 VAL N N 128.086 0.35 1 1019 225 225 GLY H H 8.502 0.03 1 1020 225 225 GLY C C 177.021 0.4 1 1021 225 225 GLY CA C 43.383 0.38 1 1022 225 225 GLY N N 113.090 0.35 1 1023 226 226 THR H H 6.444 0.03 1 1024 226 226 THR C C 181.023 0.4 1 1025 226 226 THR CA C 64.471 0.38 1 1026 226 226 THR CB C 73.950 0.24 1 1027 226 226 THR N N 114.340 0.35 1 1028 227 227 ASP H H 8.786 0.03 1 1029 227 227 ASP C C 173.308 0.4 1 1030 227 227 ASP CA C 61.184 0.38 1 1031 227 227 ASP CB C 40.226 0.24 1 1032 227 227 ASP N N 118.771 0.35 1 1033 228 228 GLY H H 10.024 0.03 1 1034 228 228 GLY C C 176.858 0.4 1 1035 228 228 GLY CA C 46.226 0.38 1 1036 228 228 GLY N N 118.035 0.35 1 1037 229 229 ILE H H 8.902 0.03 1 1038 229 229 ILE CA C 61.347 0.38 1 1039 229 229 ILE CB C 34.360 0.24 1 1040 229 229 ILE N N 118.399 0.35 1 1041 230 230 PRO CA C 66.490 0.38 1 1042 230 230 PRO CB C 30.650 0.24 1 1043 231 231 GLU H H 9.637 0.03 1 1044 231 231 GLU C C 173.486 0.4 1 1045 231 231 GLU CA C 59.678 0.38 1 1046 231 231 GLU CB C 28.751 0.24 1 1047 231 231 GLU N N 116.797 0.35 1 1048 232 232 ALA H H 7.131 0.03 1 1049 232 232 ALA C C 172.993 0.4 1 1050 232 232 ALA CA C 53.892 0.38 1 1051 232 232 ALA CB C 17.699 0.24 1 1052 232 232 ALA N N 120.963 0.35 1 1053 233 233 ARG H H 7.977 0.03 1 1054 233 233 ARG CA C 60.022 0.38 1 1055 233 233 ARG CB C 27.955 0.24 1 1056 233 233 ARG N N 117.511 0.35 1 1057 235 235 MET C C 173.304 0.4 1 1058 236 236 VAL H H 8.368 0.03 1 1059 236 236 VAL C C 172.766 0.4 1 1060 236 236 VAL CA C 64.476 0.38 1 1061 236 236 VAL CB C 30.445 0.24 1 1062 236 236 VAL N N 123.277 0.35 1 1063 237 237 GLU H H 7.843 0.03 1 1064 237 237 GLU C C 174.276 0.4 1 1065 237 237 GLU CA C 58.968 0.38 1 1066 237 237 GLU CB C 28.774 0.24 1 1067 237 237 GLU N N 120.970 0.35 1 1068 238 238 ALA H H 7.680 0.03 1 1069 238 238 ALA C C 172.570 0.4 1 1070 238 238 ALA CA C 51.889 0.38 1 1071 238 238 ALA CB C 18.803 0.24 1 1072 238 238 ALA N N 117.320 0.35 1 1073 239 239 GLY H H 7.868 0.03 1 1074 239 239 GLY C C 174.605 0.4 1 1075 239 239 GLY CA C 45.101 0.38 1 1076 239 239 GLY N N 107.094 0.35 1 1077 240 240 GLN H H 8.199 0.03 1 1078 240 240 GLN C C 176.685 0.4 1 1079 240 240 GLN CA C 56.441 0.38 1 1080 240 240 GLN CB C 29.264 0.24 1 1081 240 240 GLN N N 118.292 0.35 1 1082 241 241 MET H H 7.162 0.03 1 1083 241 241 MET C C 178.512 0.4 1 1084 241 241 MET CA C 54.421 0.38 1 1085 241 241 MET CB C 36.493 0.24 1 1086 241 241 MET N N 115.578 0.35 1 1087 242 242 THR H H 8.770 0.03 1 1088 242 242 THR C C 173.596 0.4 1 1089 242 242 THR CA C 65.596 0.38 1 1090 242 242 THR CB C 68.512 0.24 1 1091 242 242 THR N N 120.101 0.35 1 1092 243 243 ALA H H 7.749 0.03 1 1093 243 243 ALA C C 176.697 0.4 1 1094 243 243 ALA CA C 50.650 0.38 1 1095 243 243 ALA CB C 22.000 0.24 1 1096 243 243 ALA N N 115.619 0.35 1 1097 244 244 THR H H 8.438 0.03 1 1098 244 244 THR C C 181.413 0.4 1 1099 244 244 THR CA C 59.860 0.38 1 1100 244 244 THR CB C 66.769 0.24 1 1101 244 244 THR N N 113.088 0.35 1 1102 245 245 VAL H H 7.676 0.03 1 1103 245 245 VAL C C 178.245 0.4 1 1104 245 245 VAL CA C 61.785 0.38 1 1105 245 245 VAL CB C 30.266 0.24 1 1106 245 245 VAL N N 128.302 0.35 1 1107 246 246 ALA H H 9.512 0.03 1 1108 246 246 ALA C C 174.882 0.4 1 1109 246 246 ALA CA C 50.625 0.38 1 1110 246 246 ALA CB C 20.915 0.24 1 1111 246 246 ALA N N 130.920 0.35 1 1112 247 247 GLN H H 7.699 0.03 1 1113 247 247 GLN C C 177.965 0.4 1 1114 247 247 GLN CA C 55.775 0.38 1 1115 247 247 GLN CB C 30.685 0.24 1 1116 247 247 GLN N N 117.175 0.35 1 1117 248 248 ASN H H 9.326 0.03 1 1118 248 248 ASN CA C 48.798 0.38 1 1119 248 248 ASN CB C 37.789 0.24 1 1120 248 248 ASN N N 117.078 0.35 1 1121 249 249 PRO C C 173.751 0.4 1 1122 249 249 PRO CA C 63.509 0.38 1 1123 249 249 PRO CB C 30.143 0.24 1 1124 250 250 ALA H H 8.131 0.03 1 1125 250 250 ALA C C 173.417 0.4 1 1126 250 250 ALA CA C 55.728 0.38 1 1127 250 250 ALA CB C 17.037 0.24 1 1128 250 250 ALA N N 119.449 0.35 1 1129 251 251 ASP H H 6.763 0.03 1 1130 251 251 ASP C C 172.254 0.4 1 1131 251 251 ASP CA C 55.414 0.38 1 1132 251 251 ASP CB C 40.562 0.24 1 1133 251 251 ASP N N 115.959 0.35 1 1134 252 252 ILE H H 7.692 0.03 1 1135 252 252 ILE C C 174.788 0.4 1 1136 252 252 ILE CA C 65.596 0.38 1 1137 252 252 ILE CB C 37.150 0.24 1 1138 252 252 ILE N N 123.389 0.35 1 1139 253 253 GLY H H 8.052 0.03 1 1140 253 253 GLY C C 177.952 0.4 1 1141 253 253 GLY CA C 47.131 0.38 1 1142 253 253 GLY N N 103.891 0.35 1 1143 254 254 ALA H H 8.510 0.03 1 1144 254 254 ALA C C 175.363 0.4 1 1145 254 254 ALA CA C 55.580 0.38 1 1146 254 254 ALA CB C 18.464 0.24 1 1147 254 254 ALA N N 123.961 0.35 1 1148 255 255 THR H H 8.273 0.03 1 1149 255 255 THR C C 176.170 0.4 1 1150 255 255 THR CA C 66.396 0.38 1 1151 255 255 THR CB C 67.423 0.24 1 1152 255 255 THR N N 113.611 0.35 1 1153 256 256 GLY H H 8.083 0.03 1 1154 256 256 GLY CA C 47.390 0.38 1 1155 256 256 GLY N N 107.628 0.35 1 1156 257 257 LEU H H 7.887 0.03 1 1157 257 257 LEU C C 178.393 0.4 1 1158 257 257 LEU CA C 57.369 0.38 1 1159 257 257 LEU CB C 40.491 0.24 1 1160 257 257 LEU N N 119.820 0.35 1 1161 258 258 LYS H H 8.060 0.03 1 1162 258 258 LYS C C 174.159 0.4 1 1163 258 258 LYS CA C 59.566 0.38 1 1164 258 258 LYS CB C 31.179 0.24 1 1165 258 258 LYS N N 119.034 0.35 1 1166 259 259 LEU H H 8.085 0.03 1 1167 259 259 LEU C C 172.349 0.4 1 1168 259 259 LEU CA C 57.472 0.38 1 1169 259 259 LEU CB C 40.968 0.24 1 1170 259 259 LEU N N 116.346 0.35 1 1171 260 260 MET H H 7.449 0.03 1 1172 260 260 MET C C 176.179 0.4 1 1173 260 260 MET CA C 60.052 0.38 1 1174 260 260 MET CB C 33.514 0.24 1 1175 260 260 MET N N 119.349 0.35 1 1176 261 261 VAL H H 7.769 0.03 1 1177 261 261 VAL C C 173.458 0.4 1 1178 261 261 VAL CA C 64.974 0.38 1 1179 261 261 VAL CB C 30.725 0.24 1 1180 261 261 VAL N N 119.599 0.35 1 1181 262 262 ASP H H 8.540 0.03 1 1182 262 262 ASP C C 172.803 0.4 1 1183 262 262 ASP CA C 56.742 0.38 1 1184 262 262 ASP CB C 39.250 0.24 1 1185 262 262 ASP N N 119.995 0.35 1 1186 263 263 ALA H H 7.745 0.03 1 1187 263 263 ALA C C 177.925 0.4 1 1188 263 263 ALA CA C 54.407 0.38 1 1189 263 263 ALA CB C 16.698 0.24 1 1190 263 263 ALA N N 123.971 0.35 1 1191 264 264 GLU H H 7.547 0.03 1 1192 264 264 GLU C C 172.780 0.4 1 1193 264 264 GLU CA C 58.323 0.38 1 1194 264 264 GLU CB C 27.902 0.24 1 1195 264 264 GLU N N 121.361 0.35 1 1196 265 265 LYS H H 7.569 0.03 1 1197 265 265 LYS C C 172.694 0.4 1 1198 265 265 LYS CA C 57.715 0.38 1 1199 265 265 LYS CB C 31.174 0.24 1 1200 265 265 LYS N N 116.901 0.35 1 1201 266 266 SER H H 7.810 0.03 1 1202 266 266 SER C C 172.814 0.4 1 1203 266 266 SER CA C 60.150 0.38 1 1204 266 266 SER CB C 62.970 0.24 1 1205 266 266 SER N N 115.653 0.35 1 1206 267 267 GLY H H 7.451 0.03 1 1207 267 267 GLY C C 179.203 0.4 1 1208 267 267 GLY CA C 45.816 0.38 1 1209 267 267 GLY N N 109.072 0.35 1 1210 268 268 LYS H H 7.647 0.03 1 1211 268 268 LYS C C 177.210 0.4 1 1212 268 268 LYS CA C 55.007 0.38 1 1213 268 268 LYS CB C 34.648 0.24 1 1214 268 268 LYS N N 120.462 0.35 1 1215 269 269 VAL H H 7.700 0.03 1 1216 269 269 VAL C C 175.589 0.4 1 1217 269 269 VAL CA C 60.303 0.38 1 1218 269 269 VAL CB C 33.082 0.24 1 1219 269 269 VAL N N 118.118 0.35 1 1220 270 270 ILE H H 10.487 0.03 1 1221 270 270 ILE CA C 58.844 0.38 1 1222 270 270 ILE CB C 38.270 0.24 1 1223 270 270 ILE N N 130.401 0.35 1 1224 271 271 PRO C C 174.024 0.4 1 1225 271 271 PRO CA C 62.237 0.38 1 1226 271 271 PRO CB C 32.000 0.24 1 1227 272 272 LEU H H 8.736 0.03 1 1228 272 272 LEU C C 175.571 0.4 1 1229 272 272 LEU CA C 57.179 0.38 1 1230 272 272 LEU CB C 40.811 0.24 1 1231 272 272 LEU N N 121.156 0.35 1 1232 273 273 ASP H H 7.976 0.03 1 1233 273 273 ASP C C 177.002 0.4 1 1234 273 273 ASP CA C 52.957 0.38 1 1235 273 273 ASP CB C 39.644 0.24 1 1236 273 273 ASP N N 110.932 0.35 1 1237 274 274 LYS H H 7.087 0.03 1 1238 274 274 LYS C C 177.148 0.4 1 1239 274 274 LYS CA C 54.627 0.38 1 1240 274 274 LYS CB C 33.720 0.24 1 1241 274 274 LYS N N 121.497 0.35 1 1242 275 275 ALA H H 8.426 0.03 1 1243 275 275 ALA CA C 49.892 0.38 1 1244 275 275 ALA CB C 17.105 0.24 1 1245 275 275 ALA N N 129.458 0.35 1 1246 276 276 PRO C C 175.640 0.4 1 1247 276 276 PRO CA C 61.906 0.38 1 1248 276 276 PRO CB C 31.111 0.24 1 1249 277 277 GLU H H 7.835 0.03 1 1250 277 277 GLU C C 177.056 0.4 1 1251 277 277 GLU CA C 56.362 0.38 1 1252 277 277 GLU CB C 29.339 0.24 1 1253 277 277 GLU N N 121.767 0.35 1 1254 278 278 PHE H H 8.798 0.03 1 1255 278 278 PHE C C 177.559 0.4 1 1256 278 278 PHE CA C 55.119 0.38 1 1257 278 278 PHE CB C 38.700 0.24 1 1258 278 278 PHE N N 126.419 0.35 1 1259 279 279 LYS H H 8.670 0.03 1 1260 279 279 LYS C C 179.138 0.4 1 1261 279 279 LYS CA C 53.218 0.38 1 1262 279 279 LYS CB C 32.943 0.24 1 1263 279 279 LYS N N 126.532 0.35 1 1264 280 280 LEU H H 8.212 0.03 1 1265 280 280 LEU C C 175.118 0.4 1 1266 280 280 LEU CA C 52.150 0.38 1 1267 280 280 LEU CB C 41.816 0.24 1 1268 280 280 LEU N N 124.728 0.35 1 1269 281 281 VAL H H 8.476 0.03 1 1270 281 281 VAL C C 175.597 0.4 1 1271 281 281 VAL CA C 60.798 0.38 1 1272 281 281 VAL CB C 31.792 0.24 1 1273 281 281 VAL N N 124.309 0.35 1 1274 282 282 ASP H H 8.790 0.03 1 1275 282 282 ASP C C 175.934 0.4 1 1276 282 282 ASP CA C 54.829 0.38 1 1277 282 282 ASP CB C 40.751 0.24 1 1278 282 282 ASP N N 128.556 0.35 1 1279 283 283 SER H H 8.269 0.03 1 1280 283 283 SER C C 178.680 0.4 1 1281 283 283 SER CA C 56.845 0.38 1 1282 283 283 SER CB C 64.784 0.24 1 1283 283 283 SER N N 117.066 0.35 1 1284 284 284 ILE H H 8.915 0.03 1 1285 284 284 ILE C C 177.828 0.4 1 1286 284 284 ILE CA C 59.552 0.38 1 1287 284 284 ILE CB C 41.138 0.24 1 1288 284 284 ILE N N 118.261 0.35 1 1289 285 285 LEU H H 8.594 0.03 1 1290 285 285 LEU C C 177.086 0.4 1 1291 285 285 LEU CA C 54.416 0.38 1 1292 285 285 LEU CB C 41.745 0.24 1 1293 285 285 LEU N N 127.358 0.35 1 1294 286 286 VAL H H 8.880 0.03 1 1295 286 286 VAL C C 177.537 0.4 1 1296 286 286 VAL CA C 61.971 0.38 1 1297 286 286 VAL CB C 30.984 0.24 1 1298 286 286 VAL N N 130.196 0.35 1 1299 287 287 THR H H 8.116 0.03 1 1300 287 287 THR C C 178.997 0.4 1 1301 287 287 THR CA C 59.788 0.38 1 1302 287 287 THR CB C 70.582 0.24 1 1303 287 287 THR N N 116.313 0.35 1 1304 288 288 GLN H H 8.113 0.03 1 1305 288 288 GLN CA C 57.971 0.38 1 1306 288 288 GLN CB C 29.255 0.24 1 1307 288 288 GLN N N 125.699 0.35 1 stop_ save_