data_19297 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of the human C-type lectin DC-SIGNR (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin related) carbohydrate recognition domain in the holo (calcium bound) form. ; _BMRB_accession_number 19297 _BMRB_flat_file_name bmr19297.str _Entry_type original _Submission_date 2013-06-11 _Accession_date 2013-06-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data presented here are for the human C-type lectin DC-SIGNR in the calcium bound (holo) form. DC-SIGNR has been shown to bind high-mannose structures in the presence of calcium. In particular, DC-SIGNR is known to bind oligosaccharides on viral envelope glycoproteins (such as gp120 on HIV) resulting in increased infection of the host. This is the first assignment of the DC-SIGNR carbohydrate recognition domain (CRD) and serves as a starting point for the study of DC-SIGNR CRD/oligosaccharide binding and dynamics by solution NMR. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Probert Fay . . 2 Whittaker Sara B-M . 3 Mitchell Daniel A. . 4 Dixon Ann M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 451 "13C chemical shifts" 431 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-05 update BMRB 'update entry citation' 2013-06-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23788638 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Probert Fay . . 2 Whittaker 'Sara B-M' . . 3 Crispin Max . . 4 Mitchell Daniel A. . 5 Dixon Ann M. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 31 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22745 _Page_last 22757 _Year 2013 _Details . loop_ _Keyword 'C-type lectin' 'glycan binding affinities' gp120 Man9GlcNAc2 'oligosaccharide interactions' 'solution NMR dynamics' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'holo DC-SIGNR CRD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DC-SIGNR CRD' $DC-SIGNR_carbohydrate_recognition_domain 'Ca ion, 1' $entity_CA 'Ca ion, 2' $entity_CA 'Ca ion, 3' $entity_CA stop_ _System_molecular_weight 16200 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Site of carbohydrate recognition and binding in the DC-SIGNR protein' stop_ _Database_query_date . _Details 'DC-SIGNR CRD saturated with calcium to ensure all binding sites occupied.' save_ ######################## # Monomeric polymers # ######################## save_DC-SIGNR_carbohydrate_recognition_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DC-SIGNR_carbohydrate_recognition_domain _Molecular_mass 16194.7 _Mol_thiol_state 'free and disulfide bound' loop_ _Biological_function 'Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; AERLCRHCPKDWTFFQGNCY FMSNSQRNWHDSVTACQEVR AQLVVIKTAEEQNFLQLQTS RSNRFSWMGLSDLNQEGTWQ WVDGSPLSPSFQRYWNSGEP NNSGNEDCAEFSGSGWNDNR CDVDNYWICKKPAACFRDE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 261 ALA 2 262 GLU 3 263 ARG 4 264 LEU 5 265 CYS 6 266 ARG 7 267 HIS 8 268 CYS 9 269 PRO 10 270 LYS 11 271 ASP 12 272 TRP 13 273 THR 14 274 PHE 15 275 PHE 16 276 GLN 17 277 GLY 18 278 ASN 19 279 CYS 20 280 TYR 21 281 PHE 22 282 MET 23 283 SER 24 284 ASN 25 285 SER 26 286 GLN 27 287 ARG 28 288 ASN 29 289 TRP 30 290 HIS 31 291 ASP 32 292 SER 33 293 VAL 34 294 THR 35 295 ALA 36 296 CYS 37 297 GLN 38 298 GLU 39 299 VAL 40 300 ARG 41 301 ALA 42 302 GLN 43 303 LEU 44 304 VAL 45 305 VAL 46 306 ILE 47 307 LYS 48 308 THR 49 309 ALA 50 310 GLU 51 311 GLU 52 312 GLN 53 313 ASN 54 314 PHE 55 315 LEU 56 316 GLN 57 317 LEU 58 318 GLN 59 319 THR 60 320 SER 61 321 ARG 62 322 SER 63 323 ASN 64 324 ARG 65 325 PHE 66 326 SER 67 327 TRP 68 328 MET 69 329 GLY 70 330 LEU 71 331 SER 72 332 ASP 73 333 LEU 74 334 ASN 75 335 GLN 76 336 GLU 77 337 GLY 78 338 THR 79 339 TRP 80 340 GLN 81 341 TRP 82 342 VAL 83 343 ASP 84 344 GLY 85 345 SER 86 346 PRO 87 347 LEU 88 348 SER 89 349 PRO 90 350 SER 91 351 PHE 92 352 GLN 93 353 ARG 94 354 TYR 95 355 TRP 96 356 ASN 97 357 SER 98 358 GLY 99 359 GLU 100 360 PRO 101 361 ASN 102 362 ASN 103 363 SER 104 364 GLY 105 365 ASN 106 366 GLU 107 367 ASP 108 368 CYS 109 369 ALA 110 370 GLU 111 371 PHE 112 372 SER 113 373 GLY 114 374 SER 115 375 GLY 116 376 TRP 117 377 ASN 118 378 ASP 119 379 ASN 120 380 ARG 121 381 CYS 122 382 ASP 123 383 VAL 124 384 ASP 125 385 ASN 126 386 TYR 127 387 TRP 128 388 ILE 129 389 CYS 130 390 LYS 131 391 LYS 132 392 PRO 133 393 ALA 134 394 ALA 135 395 CYS 136 396 PHE 137 397 ARG 138 398 ASP 139 399 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 25046 DC-SIGNR 100.00 139 100.00 100.00 1.34e-97 PDB 1K9J "Complex Of Dc-signr And Glcnac2man3" 100.00 139 100.00 100.00 1.34e-97 PDB 1SL6 "Crystal Structure Of A Fragment Of Dc-signr (containg The Carbohydrate Recognition Domain And Two Repeats Of The Neck) Complexe" 99.28 184 100.00 100.00 2.86e-98 PDB 1XAR "Crystal Structure Of A Fragment Of Dc-Signr (Containing The Carbohydrate Recognition Domain And Two Repeats Of The Neck)" 99.28 184 100.00 100.00 2.86e-98 PDB 1XPH "Structure Of Dc-Signr And A Portion Of Repeat Domain 8" 99.28 150 100.00 100.00 2.64e-97 DBJ BAF84967 "unnamed protein product [Homo sapiens]" 99.28 376 100.00 100.00 1.46e-100 DBJ BAG65307 "unnamed protein product [Homo sapiens]" 99.28 348 100.00 100.00 3.95e-101 GB AAG13815 "probable mannose binding C-type lectin DC-SIGNR [Homo sapiens]" 99.28 399 100.00 100.00 1.03e-100 GB AAG13848 "probable mannose binding C-type lectin DC-SIGNR [Homo sapiens]" 99.28 399 99.28 99.28 1.31e-99 GB AAH38851 "C-type lectin domain family 4, member M [Homo sapiens]" 99.28 399 100.00 100.00 1.03e-100 GB AAI10615 "CLEC4M protein [Homo sapiens]" 99.28 387 100.00 100.00 1.32e-100 GB AAK20998 "L-SIGN [Homo sapiens]" 99.28 376 100.00 100.00 1.46e-100 REF NP_001138376 "C-type lectin domain family 4 member M isoform 2 [Homo sapiens]" 99.28 348 100.00 100.00 4.65e-101 REF NP_001138377 "C-type lectin domain family 4 member M isoform 12 [Homo sapiens]" 99.28 375 100.00 100.00 1.48e-100 REF NP_001138378 "C-type lectin domain family 4 member M isoform 7 [Homo sapiens]" 100.00 263 99.28 99.28 1.87e-99 REF NP_001138379 "C-type lectin domain family 4 member M isoform 11 [Homo sapiens]" 100.00 332 99.28 99.28 1.65e-100 REF NP_001138381 "C-type lectin domain family 4 member M isoform 9 [Homo sapiens]" 99.28 353 100.00 100.00 2.19e-100 SP Q8HY06 "RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; AltName: CD_antigen=CD299" 99.28 376 97.10 98.55 4.90e-98 SP Q9H2X3 "RecName: Full=C-type lectin domain family 4 member M; AltName: Full=CD209 antigen-like protein 1; AltName: Full=DC-SIGN-related" 99.28 399 100.00 100.00 1.03e-100 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $DC-SIGNR_carbohydrate_recognition_domain Human 9606 Eukaryota Metazoa Homo sapiens 'CLEC4M, CD209L, CD209L1, CD299' 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 $DC-SIGNR_carbohydrate_recognition_domain 'recombinant technology' . Escherichia coli BL21(DE3) pT5T stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'holo DC-SIGNR CRD pH 6.8' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DC-SIGNR_carbohydrate_recognition_domain 0.7 mM '[U-100% 13C; U-100% 15N]' HEPES 20 mM '[U-100% 2H]' 'calcium chloride' 4 mM 'natural abundance' 'sodium chloride' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Warwick University' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 800 _Details 'HWB-NMR, University of Birmingham' 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_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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 pH 6.8 . pH pressure 1 . atm temperature 310.15 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'Proton chemical shifts were referenced against external DSS while nitrogen chemical shifts were referenced indirectly to DSS using the absolute frequency ratio.' 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 na indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 1.000000000 DSS N 15 'methyl protons' ppm 0 na indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' parallel 0.10132918 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D CBCA(CO)NH' '3D HN(CA)CO' 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 'DC-SIGNR CRD' _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 1 262 2 GLU C C 175.987 0.000 1 2 262 2 GLU CA C 62.049 0.000 1 3 263 3 ARG H H 8.541 0.01 1 4 263 3 ARG C C 177.536 0.000 1 5 263 3 ARG CA C 58.875 0.094 1 6 263 3 ARG CB C 32.559 0.14 1 7 263 3 ARG N N 122.504 0.052 1 8 264 4 LEU H H 6.692 0.013 1 9 264 4 LEU C C 176.81 0.009 1 10 264 4 LEU CA C 59.557 0.089 1 11 264 4 LEU CB C 42.507 0.063 1 12 264 4 LEU N N 117.859 0.052 1 13 265 5 CYS H H 9.178 0.009 1 14 265 5 CYS C C 173.689 0.014 1 15 265 5 CYS CA C 51.603 0.099 1 16 265 5 CYS CB C 40.6 0.039 1 17 265 5 CYS N N 121.246 0.047 1 18 266 6 ARG H H 9.38 0.01 1 19 266 6 ARG HA H 5.746 0.023 1 20 266 6 ARG HG2 H 1.459 0.438 2 21 266 6 ARG HD2 H 2.065 0.002 2 22 266 6 ARG HD3 H 1.67 0.006 1 23 266 6 ARG C C 175.691 0.062 1 24 266 6 ARG CA C 54.954 0.073 1 25 266 6 ARG CB C 31.026 0.000 1 26 266 6 ARG CG C 25.497 0.000 1 27 266 6 ARG CD C 38.537 0.078 1 28 266 6 ARG N N 123.315 0.047 1 29 267 7 HIS H H 9.234 0.011 1 30 267 7 HIS C C 171.368 0.000 1 31 267 7 HIS CA C 54.423 0.000 1 32 267 7 HIS CB C 34.676 0.000 1 33 267 7 HIS N N 126 0.051 1 34 269 9 PRO C C 176.832 0.000 1 35 269 9 PRO CA C 61.923 0.014 1 36 269 9 PRO CB C 33.106 0.000 1 37 270 10 LYS H H 9.561 0.009 1 38 270 10 LYS C C 176.198 0.009 1 39 270 10 LYS CA C 52.206 0.033 1 40 270 10 LYS CB C 38.057 0.063 1 41 270 10 LYS N N 124.482 0.047 1 42 271 11 ASP H H 11.611 0.013 1 43 271 11 ASP CA C 54.582 0.000 1 44 271 11 ASP N N 127.352 0.056 1 45 272 12 TRP H H 8.623 0.000 1 46 272 12 TRP HA H 5.313 0.005 1 47 272 12 TRP HB2 H 3.661 0.626 2 48 272 12 TRP HB3 H 3.268 0.002 2 49 272 12 TRP C C 176.189 0.000 1 50 272 12 TRP CA C 57.365 0.034 1 51 272 12 TRP CB C 34.059 9.883 1 52 272 12 TRP N N 120.894 0.000 1 53 273 13 THR H H 9.83 0.025 1 54 273 13 THR C C 174.072 0.013 1 55 273 13 THR CA C 62.848 0.08 1 56 273 13 THR CB C 71.851 0.101 1 57 273 13 THR N N 118.956 0.047 1 58 274 14 PHE H H 9.153 0.01 1 59 274 14 PHE HA H 5.56 0.012 1 60 274 14 PHE HB2 H 3.371 0.004 2 61 274 14 PHE HB3 H 3.144 0.009 2 62 274 14 PHE C C 175.225 0.022 1 63 274 14 PHE CA C 58.085 0.077 1 64 274 14 PHE CB C 41.066 0.051 1 65 274 14 PHE N N 128.907 0.047 1 66 275 15 PHE H H 8.836 0.012 1 67 275 15 PHE HA H 3.992 0.004 1 68 275 15 PHE HB2 H 2.284 0.002 2 69 275 15 PHE HB3 H 2.221 0.000 2 70 275 15 PHE C C 174.767 0.004 1 71 275 15 PHE CA C 59.243 0.081 1 72 275 15 PHE CB C 40.982 0.046 1 73 275 15 PHE N N 126.573 0.047 1 74 276 16 GLN H H 8.758 0.007 1 75 276 16 GLN C C 174.454 0.000 1 76 276 16 GLN CA C 56.791 0.139 1 77 276 16 GLN N N 127.147 0.05 1 78 277 17 GLY C C 172.975 0.000 1 79 277 17 GLY CA C 45.605 0.085 1 80 278 18 ASN H H 7.681 0.005 1 81 278 18 ASN HA H 5.397 0.003 1 82 278 18 ASN HB2 H 2.765 0.002 2 83 278 18 ASN HB3 H 2.016 0.004 2 84 278 18 ASN C C 171.439 0.005 1 85 278 18 ASN CA C 52.265 0.049 1 86 278 18 ASN CB C 44.084 0.055 1 87 278 18 ASN N N 118.166 0.05 1 88 279 19 CYS H H 9.557 0.012 1 89 279 19 CYS HA H 5.878 0.006 1 90 279 19 CYS HB2 H 3.16 0.007 2 91 279 19 CYS HB3 H 2.85 0.003 2 92 279 19 CYS C C 174.318 0.013 1 93 279 19 CYS CA C 53.532 0.03 1 94 279 19 CYS CB C 43.123 0.092 1 95 279 19 CYS N N 117.063 0.047 1 96 280 20 TYR H H 10.038 0.011 1 97 280 20 TYR HA H 5.86 0.004 1 98 280 20 TYR HB2 H 2.979 0.007 2 99 280 20 TYR HB3 H 2.826 0.005 2 100 280 20 TYR C C 174.657 0.018 1 101 280 20 TYR CA C 57.26 0.056 1 102 280 20 TYR CB C 41.665 0.058 1 103 280 20 TYR N N 121.246 0.047 1 104 281 21 PHE H H 8.671 0.006 1 105 281 21 PHE HA H 4.275 0.003 1 106 281 21 PHE HB2 H 1.242 0.003 2 107 281 21 PHE HB3 H 1.219 0.000 2 108 281 21 PHE C C 172.971 0.013 1 109 281 21 PHE CA C 55.384 0.048 1 110 281 21 PHE CB C 40.112 0.059 1 111 281 21 PHE N N 125.34 0.047 1 112 282 22 MET H H 7.801 0.007 1 113 282 22 MET HA H 4.494 0.005 1 114 282 22 MET HB2 H 1.631 0.005 2 115 282 22 MET HB3 H 1.744 0.004 2 116 282 22 MET HG2 H 2.385 0.004 1 117 282 22 MET C C 174.543 0.017 1 118 282 22 MET CA C 53.909 0.07 1 119 282 22 MET CB C 32.038 0.083 1 120 282 22 MET CG C 33.273 0.069 1 121 282 22 MET N N 127.057 0.047 1 122 283 23 SER H H 7.847 0.011 1 123 283 23 SER CA C 59.233 0.063 1 124 283 23 SER CB C 62.503 0.000 1 125 283 23 SER N N 119.266 0.05 1 126 284 24 ASN HA H 5.118 0.003 1 127 284 24 ASN HB2 H 2.844 0.003 2 128 284 24 ASN HB3 H 2.993 0.003 2 129 284 24 ASN C C 174.666 0.000 1 130 284 24 ASN CA C 52.471 0.083 1 131 284 24 ASN CB C 39.757 0.038 1 132 285 25 SER H H 7.43 0.303 1 133 285 25 SER HB2 H 4.089 0.005 1 134 285 25 SER C C 171.012 0.027 1 135 285 25 SER CA C 56.839 0.09 1 136 285 25 SER CB C 65.206 0.106 1 137 285 25 SER N N 113.997 1.633 1 138 286 26 GLN H H 8.429 0.005 1 139 286 26 GLN C C 175.987 0.000 1 140 286 26 GLN CA C 54.905 0.05 1 141 286 26 GLN CB C 32.653 0.124 1 142 286 26 GLN N N 116.755 0.047 1 143 287 27 ARG H H 9.683 0.01 1 144 287 27 ARG HA H 4.987 0.005 1 145 287 27 ARG HB2 H 1.726 0.005 2 146 287 27 ARG HB3 H 1.955 0.002 2 147 287 27 ARG HG2 H 1.899 0.004 1 148 287 27 ARG HD2 H 2.662 0.001 1 149 287 27 ARG C C 177.026 0.000 1 150 287 27 ARG CA C 55.657 0.065 1 151 287 27 ARG CB C 37.322 0.05 1 152 287 27 ARG CG C 29.288 0.073 1 153 287 27 ARG CD C 43.627 0.053 1 154 287 27 ARG N N 122.512 0.019 1 155 288 28 ASN H H 9.412 0.006 1 156 288 28 ASN C C 176.903 0.009 1 157 288 28 ASN CA C 49.817 6.111 1 158 288 28 ASN CB C 37.502 0.000 1 159 288 28 ASN N N 120.552 0.047 1 160 289 29 TRP H H 8.326 0.012 1 161 289 29 TRP HA H 2.878 0.007 1 162 289 29 TRP HB2 H 2.647 0.006 2 163 289 29 TRP HB3 H 1.469 0.005 2 164 289 29 TRP C C 177.549 0.014 1 165 289 29 TRP CA C 64.057 0.099 1 166 289 29 TRP CB C 31.291 0.161 1 167 289 29 TRP N N 120.991 0.047 1 168 290 30 HIS H H 7.548 0.051 1 169 290 30 HIS HA H 3.916 0.011 1 170 290 30 HIS HB2 H 3.269 0.003 2 171 290 30 HIS HB3 H 3.14 0.002 2 172 290 30 HIS C C 179.055 0.022 1 173 290 30 HIS CA C 60.3 0.126 1 174 290 30 HIS CB C 29.99 0.096 1 175 290 30 HIS N N 115.584 0.28 1 176 291 31 ASP H H 9 0.009 1 177 291 31 ASP HA H 4.496 0.003 1 178 291 31 ASP HB2 H 2.532 0.002 2 179 291 31 ASP HB3 H 2.453 0.000 2 180 291 31 ASP C C 179.209 0.009 1 181 291 31 ASP CA C 56.116 0.044 1 182 291 31 ASP CB C 39.418 0.037 1 183 291 31 ASP N N 118.362 0.047 1 184 292 32 SER H H 7.997 0.011 1 185 292 32 SER HA H 3.148 0.028 1 186 292 32 SER HB2 H 3.231 0.000 1 187 292 32 SER C C 174.692 0.000 1 188 292 32 SER CA C 63.546 0.415 1 189 292 32 SER CB C 61.974 0.225 1 190 292 32 SER N N 123.636 0.05 1 191 293 33 VAL H H 7.503 0.006 1 192 293 33 VAL HA H 3.276 0.006 1 193 293 33 VAL HB H 2.079 0.009 1 194 293 33 VAL HG1 H 0.793 0.005 1 195 293 33 VAL HG2 H -0.123 0.002 1 196 293 33 VAL C C 180.781 0.004 1 197 293 33 VAL CA C 67.069 0.09 1 198 293 33 VAL CB C 31.606 0.123 1 199 293 33 VAL CG1 C 20.92 0.042 2 200 293 33 VAL CG2 C 22.761 0.03 2 201 293 33 VAL N N 122.919 0.047 1 202 294 34 THR H H 7.484 0.01 1 203 294 34 THR C C 176.009 0.005 1 204 294 34 THR CA C 65.993 0.094 1 205 294 34 THR CB C 68.59 0.164 1 206 294 34 THR N N 114.775 0.05 1 207 295 35 ALA H H 7.941 0.006 1 208 295 35 ALA HA H 4.073 0.007 1 209 295 35 ALA HB H 1.185 0.008 1 210 295 35 ALA C C 181.974 0.036 1 211 295 35 ALA CA C 55.271 0.058 1 212 295 35 ALA CB C 17.713 0.082 1 213 295 35 ALA N N 124.636 0.047 1 214 296 36 CYS H H 7.809 0.006 1 215 296 36 CYS HA H 4.879 0.007 1 216 296 36 CYS HB2 H 2.809 0.004 2 217 296 36 CYS HB3 H 2.696 0.046 2 218 296 36 CYS C C 177.431 0.009 1 219 296 36 CYS CA C 55.386 0.071 1 220 296 36 CYS CB C 36.438 0.046 1 221 296 36 CYS N N 112.44 0.047 1 222 297 37 GLN H H 7.957 0.012 1 223 297 37 GLN HA H 4.391 0.005 1 224 297 37 GLN HB2 H 2.475 0.006 2 225 297 37 GLN HB3 H 2.257 0.004 2 226 297 37 GLN HG2 H 2.73 0.009 2 227 297 37 GLN HG3 H 2.593 0.003 2 228 297 37 GLN C C 180.592 0.009 1 229 297 37 GLN CA C 59.756 0.113 1 230 297 37 GLN CB C 28.145 0.074 1 231 297 37 GLN CG C 34.383 0.05 1 232 297 37 GLN N N 122.831 0.047 1 233 298 38 GLU H H 8.402 0.006 1 234 298 38 GLU HA H 4.185 0.012 1 235 298 38 GLU HB2 H 2.352 0.005 2 236 298 38 GLU HB3 H 2.245 0.005 2 237 298 38 GLU HG2 H 2.695 0.009 2 238 298 38 GLU HG3 H 2.555 0.005 2 239 298 38 GLU C C 178.237 0.005 1 240 298 38 GLU CA C 60.223 0.52 1 241 298 38 GLU CB C 29.183 0.258 1 242 298 38 GLU CG C 37.632 0.051 1 243 298 38 GLU N N 120.013 0.047 1 244 299 39 VAL H H 7.228 0.009 1 245 299 39 VAL HA H 4.773 0.000 1 246 299 39 VAL HB H 2.733 0.003 1 247 299 39 VAL HG1 H 1.308 0.005 2 248 299 39 VAL HG2 H 1.051 0.005 2 249 299 39 VAL C C 174.159 0.014 1 250 299 39 VAL CA C 59.965 0.12 1 251 299 39 VAL CB C 30.328 0.174 1 252 299 39 VAL CG1 C 19.325 0.059 2 253 299 39 VAL CG2 C 25.036 9.901 2 254 299 39 VAL N N 109.71 0.047 1 255 300 40 ARG H H 8.02 0.008 1 256 300 40 ARG HA H 4.021 0.005 1 257 300 40 ARG HB2 H 2.003 0.003 2 258 300 40 ARG HB3 H 2.044 0.000 2 259 300 40 ARG HG2 H 1.674 0.004 1 260 300 40 ARG HD2 H 3.294 0.003 1 261 300 40 ARG C C 174.318 0.004 1 262 300 40 ARG CA C 56.96 0.058 1 263 300 40 ARG CB C 26.434 0.299 1 264 300 40 ARG CG C 27.756 0.075 1 265 300 40 ARG CD C 43.542 0.052 1 266 300 40 ARG N N 115.698 0.047 1 267 301 41 ALA H H 8.257 0.006 1 268 301 41 ALA HA H 4.996 0.018 1 269 301 41 ALA HB H 1.65 0.003 1 270 301 41 ALA C C 174.842 0.009 1 271 301 41 ALA CA C 49.984 0.072 1 272 301 41 ALA CB C 24.594 0.116 1 273 301 41 ALA N N 120.541 0.047 1 274 302 42 GLN H H 8.203 0.008 1 275 302 42 GLN HA H 5.124 0.013 1 276 302 42 GLN HB2 H 2.008 0.004 2 277 302 42 GLN HB3 H 2.189 0.005 2 278 302 42 GLN HG2 H 2.697 0.002 2 279 302 42 GLN HG3 H 2.406 0.008 2 280 302 42 GLN C C 175.67 0.017 1 281 302 42 GLN CA C 54.121 0.067 1 282 302 42 GLN CB C 33.835 0.051 1 283 302 42 GLN CG C 34.968 0.041 1 284 302 42 GLN N N 116.974 0.047 1 285 303 43 LEU H H 9.198 0.019 1 286 303 43 LEU HA H 5.025 0.007 1 287 303 43 LEU HB2 H 1.676 0.003 2 288 303 43 LEU HB3 H 1.089 0.000 2 289 303 43 LEU HG H 0.284 0.005 1 290 303 43 LEU HD1 H 1.221 0.006 1 291 303 43 LEU C C 179.597 0.009 1 292 303 43 LEU CA C 57.774 0.101 1 293 303 43 LEU CB C 42.937 0.129 1 294 303 43 LEU CG C 28.312 0.083 1 295 303 43 LEU CD1 C 24.888 0.105 2 296 303 43 LEU CD2 C 24.042 0.000 2 297 303 43 LEU N N 132.913 0.047 1 298 304 44 VAL H H 8.048 0.005 1 299 304 44 VAL HA H 3.862 0.004 1 300 304 44 VAL HB H 2.203 0.002 1 301 304 44 VAL HG1 H 1.589 0.005 2 302 304 44 VAL HG2 H 1.198 0.006 2 303 304 44 VAL C C 173.19 0.005 1 304 304 44 VAL CA C 65.311 0.042 1 305 304 44 VAL CB C 33.617 0.048 1 306 304 44 VAL CG1 C 19.678 0.035 2 307 304 44 VAL CG2 C 22.799 0.038 2 308 304 44 VAL N N 122.701 0.05 1 309 305 45 VAL H H 7.178 0.007 1 310 305 45 VAL HA H 4.371 0.023 1 311 305 45 VAL HB H 1.939 0.005 1 312 305 45 VAL HG1 H 1.253 0.002 2 313 305 45 VAL HG2 H 1.408 0.004 2 314 305 45 VAL C C 174.578 0.000 1 315 305 45 VAL CA C 60.419 0.107 1 316 305 45 VAL CB C 33 0.221 1 317 305 45 VAL CG1 C 20.443 0.168 2 318 305 45 VAL CG2 C 22.903 0.059 2 319 305 45 VAL N N 127.938 0.047 1 320 306 46 ILE HA H 3.742 0.007 1 321 306 46 ILE HB H 1.813 0.004 1 322 306 46 ILE HG12 H 0.909 0.005 1 323 306 46 ILE HG2 H 1.079 0.002 1 324 306 46 ILE HD1 H 1.339 0.002 1 325 306 46 ILE C C 175.476 0.000 1 326 306 46 ILE CA C 61.318 0.052 1 327 306 46 ILE CB C 37.77 0.066 1 328 306 46 ILE CG1 C 28.41 0.048 1 329 306 46 ILE CG2 C 18.975 0.041 1 330 306 46 ILE CD1 C 15.03 0.027 1 331 307 47 LYS H H 9.286 0.011 1 332 307 47 LYS HA H 4.49 0.012 1 333 307 47 LYS HB2 H 1.995 0.007 2 334 307 47 LYS HB3 H 2.023 0.000 2 335 307 47 LYS HG2 H 1.418 0.123 1 336 307 47 LYS HD2 H 1.509 0.000 1 337 307 47 LYS HE2 H 2.743 0.005 1 338 307 47 LYS C C 177.691 0.022 1 339 307 47 LYS CA C 55.222 0.056 1 340 307 47 LYS CB C 35.142 0.047 1 341 307 47 LYS CG C 24.777 0.107 1 342 307 47 LYS CD C 28.437 0.000 1 343 307 47 LYS CE C 42.249 0.126 1 344 307 47 LYS N N 123.315 0.047 1 345 308 48 THR H H 7.655 0.008 1 346 308 48 THR HA H 5.293 0.01 1 347 308 48 THR HB H 4.953 0.000 1 348 308 48 THR C C 174.49 0.000 1 349 308 48 THR CA C 59.371 0.071 1 350 308 48 THR CB C 73.684 0.101 1 351 308 48 THR N N 107.024 0.047 1 352 309 49 ALA H H 9.312 0.004 1 353 309 49 ALA HA H 4.152 0.003 1 354 309 49 ALA HB H 1.568 0.002 1 355 309 49 ALA C C 180.037 0.009 1 356 309 49 ALA CA C 55.098 0.065 1 357 309 49 ALA CB C 18.471 0.127 1 358 309 49 ALA N N 125.212 0.052 1 359 310 50 GLU H H 9.059 0.007 1 360 310 50 GLU C C 179.333 0.009 1 361 310 50 GLU CA C 60.71 0.037 1 362 310 50 GLU CB C 29.119 0.062 1 363 310 50 GLU N N 117.679 0.047 1 364 311 51 GLU H H 8.261 0.007 1 365 311 51 GLU C C 177.488 0.013 1 366 311 51 GLU CA C 59.678 0.02 1 367 311 51 GLU CB C 30.38 0.000 1 368 311 51 GLU N N 123.447 0.047 1 369 312 52 GLN H H 7.835 0.004 1 370 312 52 GLN HA H 4.327 0.000 1 371 312 52 GLN HG2 H 1.578 0.005 1 372 312 52 GLN C C 176.982 0.009 1 373 312 52 GLN CA C 58.82 0.122 1 374 312 52 GLN CB C 26.168 0.087 1 375 312 52 GLN CG C 32.105 0.059 1 376 312 52 GLN N N 121.273 0.000 1 377 313 53 ASN H H 8.257 0.008 1 378 313 53 ASN C C 177.272 0.035 1 379 313 53 ASN CA C 56.588 0.04 1 380 313 53 ASN CB C 38.389 0.086 1 381 313 53 ASN N N 117.107 0.047 1 382 314 54 PHE H H 7.794 0.008 1 383 314 54 PHE HA H 4.058 0.002 1 384 314 54 PHE HB2 H 2.35 0.003 2 385 314 54 PHE HB3 H 2.392 0.000 2 386 314 54 PHE C C 177.166 0.009 1 387 314 54 PHE CA C 60.524 0.067 1 388 314 54 PHE CB C 39.082 0.104 1 389 314 54 PHE N N 120.497 0.047 1 390 315 55 LEU H H 8.071 0.008 1 391 315 55 LEU HA H 3.156 0.004 1 392 315 55 LEU HB2 H 1.709 0.006 2 393 315 55 LEU HB3 H 0.715 0.006 2 394 315 55 LEU HG H 1.049 0.01 1 395 315 55 LEU HD2 H 0.472 0.002 1 396 315 55 LEU C C 179.104 0.009 1 397 315 55 LEU CA C 57.273 0.074 1 398 315 55 LEU CB C 42.314 0.125 1 399 315 55 LEU CG C 28.419 0.051 1 400 315 55 LEU CD1 C 26.956 0.008 2 401 315 55 LEU CD2 C 22.462 0.045 2 402 315 55 LEU N N 119.969 0.047 1 403 316 56 GLN H H 8.818 0.32 1 404 316 56 GLN HA H 3.667 0.005 1 405 316 56 GLN HB2 H 2.502 0.015 2 406 316 56 GLN HB3 H 2.138 0.000 2 407 316 56 GLN HG2 H 2.361 0.005 1 408 316 56 GLN C C 179.139 0.044 1 409 316 56 GLN CA C 59.015 0.078 1 410 316 56 GLN CB C 28.886 0.057 1 411 316 56 GLN CG C 33.952 0.047 1 412 316 56 GLN N N 122.253 0.28 1 413 317 57 LEU H H 7.716 0.008 1 414 317 57 LEU HA H 4.054 0.005 1 415 317 57 LEU HB2 H 1.583 0.005 2 416 317 57 LEU HB3 H 1.73 0.003 2 417 317 57 LEU HD1 H 0.899 0.013 1 418 317 57 LEU C C 179.201 0.000 1 419 317 57 LEU CA C 57.923 0.059 1 420 317 57 LEU CB C 41.548 0.078 1 421 317 57 LEU CG C 27.122 0.066 1 422 317 57 LEU CD1 C 24.305 0.106 1 423 317 57 LEU N N 119.837 0.047 1 424 318 58 GLN H H 7.632 0.006 1 425 318 58 GLN HA H 3.722 0.009 1 426 318 58 GLN HB2 H 1.777 0.004 2 427 318 58 GLN HB3 H 1.526 0.004 2 428 318 58 GLN HG2 H 1.457 0.002 1 429 318 58 GLN C C 179.483 0.008 1 430 318 58 GLN CA C 58.312 0.101 1 431 318 58 GLN CB C 27.783 0.127 1 432 318 58 GLN CG C 32.985 0.061 1 433 318 58 GLN N N 116.402 0.047 1 434 319 59 THR H H 7.849 0.01 1 435 319 59 THR HA H 3.748 0.003 1 436 319 59 THR HB H 3.657 0.000 1 437 319 59 THR C C 176.903 0.009 1 438 319 59 THR CA C 65.445 0.149 1 439 319 59 THR CB C 68.644 0.000 1 440 319 59 THR N N 111.647 0.047 1 441 320 60 SER H H 8.204 0.009 1 442 320 60 SER HA H 4.326 0.002 1 443 320 60 SER HB2 H 4.136 0.005 1 444 320 60 SER C C 178.153 0.035 1 445 320 60 SER CA C 61.581 0.063 1 446 320 60 SER CB C 63.125 0.055 1 447 320 60 SER N N 118.736 0.047 1 448 321 61 ARG H H 8.104 0.006 1 449 321 61 ARG HA H 4.189 0.004 1 450 321 61 ARG HB2 H 1.868 0.006 2 451 321 61 ARG HB3 H 1.77 0.002 2 452 321 61 ARG HG2 H 1.692 0.004 1 453 321 61 ARG HD2 H 3.15 0.006 1 454 321 61 ARG C C 177.563 0.000 1 455 321 61 ARG CA C 58.64 0.135 1 456 321 61 ARG CB C 30.064 0.067 1 457 321 61 ARG CG C 27.457 0.067 1 458 321 61 ARG CD C 43.617 0.038 1 459 321 61 ARG N N 121.334 0.047 1 460 322 62 SER H H 7.347 0.009 1 461 322 62 SER HA H 5.669 0.007 1 462 322 62 SER HB2 H 3.978 0.007 1 463 322 62 SER C C 173.935 0.000 1 464 322 62 SER CA C 58.529 0.089 1 465 322 62 SER CB C 64.174 0.129 1 466 322 62 SER N N 111.427 0.047 1 467 323 63 ASN H H 7.95 0.007 1 468 323 63 ASN HA H 4.319 0.006 1 469 323 63 ASN HB2 H 3.074 0.015 2 470 323 63 ASN HB3 H 2.709 0.003 2 471 323 63 ASN C C 173.776 0.000 1 472 323 63 ASN CA C 54.278 0.073 1 473 323 63 ASN CB C 37.579 0.038 1 474 323 63 ASN N N 118.604 0.047 1 475 324 64 ARG H H 7.539 0.01 1 476 324 64 ARG HA H 4.439 0.006 1 477 324 64 ARG HB2 H 1.302 0.022 1 478 324 64 ARG HB3 H 1.244 0.007 1 479 324 64 ARG HG2 H 0.935 0.006 1 480 324 64 ARG HD2 H 2.318 0.004 2 481 324 64 ARG HD3 H 1.868 0.007 2 482 324 64 ARG C C 176.005 0.017 1 483 324 64 ARG CA C 55.127 0.085 1 484 324 64 ARG CB C 32.411 0.106 1 485 324 64 ARG CG C 26.364 0.065 1 486 324 64 ARG CD C 43.256 0.167 1 487 324 64 ARG N N 116.49 0.047 1 488 325 65 PHE H H 8.754 0.011 1 489 325 65 PHE HA H 5.153 0.016 1 490 325 65 PHE HB2 H 3.123 0.037 2 491 325 65 PHE HB3 H 3.047 0.004 2 492 325 65 PHE C C 176.356 0.000 1 493 325 65 PHE CA C 56.78 0.067 1 494 325 65 PHE CB C 38.511 0.079 1 495 325 65 PHE N N 125.076 0.047 1 496 326 66 SER H H 7.502 0.007 1 497 326 66 SER HA H 5.363 0.008 1 498 326 66 SER HB2 H 3.662 0.019 1 499 326 66 SER C C 173.812 0.000 1 500 326 66 SER CA C 56.512 0.048 1 501 326 66 SER CB C 67.37 0.157 1 502 326 66 SER N N 113.805 0.047 1 503 327 67 TRP H H 9.988 0.012 1 504 327 67 TRP HA H 5.356 0.002 1 505 327 67 TRP HB2 H 3.626 0.026 1 506 327 67 TRP C C 175.339 0.014 1 507 327 67 TRP CA C 57.32 0.478 1 508 327 67 TRP CB C 34.341 0.048 1 509 327 67 TRP N N 124.946 0.053 1 510 328 68 MET H H 8.466 0.004 1 511 328 68 MET HA H 5.42 0.009 1 512 328 68 MET HB2 H 2.314 0.005 2 513 328 68 MET HB3 H 1.974 0.006 2 514 328 68 MET HG2 H 2.178 0.009 2 515 328 68 MET HG3 H 2.049 0.005 2 516 328 68 MET C C 176.652 0.014 1 517 328 68 MET CA C 53.413 0.06 1 518 328 68 MET CB C 38.015 0.057 1 519 328 68 MET CG C 30.864 0.094 1 520 328 68 MET N N 113.937 0.047 1 521 329 69 GLY H H 9.974 0.009 1 522 329 69 GLY HA2 H 3.753 0.008 1 523 329 69 GLY C C 173.377 0.245 1 524 329 69 GLY CA C 48.84 0.049 1 525 329 69 GLY N N 112.178 0.05 1 526 330 70 LEU H H 8.45 0.006 1 527 330 70 LEU HA H 4.931 0.003 1 528 330 70 LEU HB2 H 1.286 0.003 2 529 330 70 LEU HB3 H 0.558 0.000 2 530 330 70 LEU HG H -0.527 3.541 1 531 330 70 LEU HD1 H -0.33 0.000 1 532 330 70 LEU C C 173.759 0.000 1 533 330 70 LEU CA C 55.07 0.04 1 534 330 70 LEU CB C 46.529 0.053 1 535 330 70 LEU CG C 26.3 0.045 1 536 330 70 LEU CD1 C 22.019 0.055 1 537 330 70 LEU N N 128.336 0.05 1 538 331 71 SER H H 8.631 0.008 1 539 331 71 SER HA H 5.415 0.007 1 540 331 71 SER HB2 H 3.734 0.002 2 541 331 71 SER HB3 H 3.239 0.000 2 542 331 71 SER C C 173.416 0.009 1 543 331 71 SER CA C 58.963 0.056 1 544 331 71 SER CB C 68.014 0.152 1 545 331 71 SER N N 120.629 0.047 1 546 332 72 ASP H H 8.047 0.008 1 547 332 72 ASP HA H 4.596 0.004 1 548 332 72 ASP HB2 H 2.155 0.001 1 549 332 72 ASP C C 176.048 0.018 1 550 332 72 ASP CA C 51.819 0.085 1 551 332 72 ASP CB C 37.629 0.062 1 552 332 72 ASP N N 123.843 0.047 1 553 333 73 LEU H H 6.718 0.017 1 554 333 73 LEU HA H 3.709 0.004 1 555 333 73 LEU HB2 H 1.487 0.007 2 556 333 73 LEU HB3 H 1.347 0.011 2 557 333 73 LEU HG H 0.74 0.091 1 558 333 73 LEU HD1 H 1.039 0.094 1 559 333 73 LEU C C 178.783 0.004 1 560 333 73 LEU CA C 57.373 0.096 1 561 333 73 LEU CB C 44.466 0.067 1 562 333 73 LEU CG C 26.794 0.064 1 563 333 73 LEU CD1 C 25.122 0.054 1 564 333 73 LEU N N 119.396 0.047 1 565 334 74 ASN H H 7.918 0.011 1 566 334 74 ASN HA H 4.438 0.01 1 567 334 74 ASN HB2 H 2.722 0.001 2 568 334 74 ASN HB3 H 2.667 0.004 2 569 334 74 ASN C C 175.503 0.026 1 570 334 74 ASN CA C 56.182 0.113 1 571 334 74 ASN CB C 38.522 0.086 1 572 334 74 ASN N N 115.654 0.047 1 573 335 75 GLN H H 7.823 0.012 1 574 335 75 GLN HA H 4.242 0.022 1 575 335 75 GLN HB2 H 1.914 0.006 2 576 335 75 GLN HB3 H 1.86 0.008 2 577 335 75 GLN HG2 H 2.2 0.003 1 578 335 75 GLN C C 172.394 0.009 1 579 335 75 GLN CA C 55.278 0.045 1 580 335 75 GLN CB C 30.634 0.06 1 581 335 75 GLN CG C 33.891 0.079 1 582 335 75 GLN N N 120.673 0.047 1 583 336 76 GLU H H 8.159 0.01 1 584 336 76 GLU HA H 3.934 0.000 1 585 336 76 GLU HB2 H 1.677 0.004 2 586 336 76 GLU HB3 H 2.281 0.000 2 587 336 76 GLU HG2 H 2.485 0.008 2 588 336 76 GLU HG3 H 1.896 0.000 2 589 336 76 GLU C C 178.259 0.008 1 590 336 76 GLU CA C 57.08 0.062 1 591 336 76 GLU CB C 28.55 0.124 1 592 336 76 GLU CG C 34.324 0.057 1 593 336 76 GLU N N 128.202 0.047 1 594 337 77 GLY H H 10.987 0.014 1 595 337 77 GLY HA2 H 3.77 0.02 1 596 337 77 GLY CA C 45.174 0.047 1 597 337 77 GLY N N 120.765 0.052 1 598 338 78 THR H H 8.586 0.004 1 599 338 78 THR HA H 4.614 0.003 1 600 338 78 THR HB H 4.181 0.005 1 601 338 78 THR C C 172.443 0.013 1 602 338 78 THR CA C 61.822 0.085 1 603 338 78 THR CB C 69.461 0.11 1 604 338 78 THR N N 120.897 0.052 1 605 339 79 TRP H H 8.868 0.009 1 606 339 79 TRP HA H 4.261 0.002 1 607 339 79 TRP HB2 H 3.23 0.008 2 608 339 79 TRP HB3 H 3.006 0.003 2 609 339 79 TRP C C 176.07 0.005 1 610 339 79 TRP CA C 57.915 0.068 1 611 339 79 TRP CB C 29.582 0.061 1 612 339 79 TRP N N 128.862 0.047 1 613 340 80 GLN H H 9.19 0.007 1 614 340 80 GLN HA H 5.001 0.013 1 615 340 80 GLN HB2 H 2.137 0.006 2 616 340 80 GLN HB3 H 1.978 0.006 2 617 340 80 GLN HG2 H 2.522 0.004 2 618 340 80 GLN HG3 H 2.251 0.029 2 619 340 80 GLN C C 176 0.004 1 620 340 80 GLN CA C 54.672 0.039 1 621 340 80 GLN CB C 33.943 0.082 1 622 340 80 GLN CG C 34.235 0.066 1 623 340 80 GLN N N 123.271 0.047 1 624 341 81 TRP H H 9.643 0.007 1 625 341 81 TRP HA H 5.929 0.003 1 626 341 81 TRP HB2 H 3.972 0.003 2 627 341 81 TRP HB3 H 3.59 0.003 2 628 341 81 TRP C C 181.446 0.000 1 629 341 81 TRP CA C 57.412 0.272 1 630 341 81 TRP CB C 34.001 0.853 1 631 341 81 TRP N N 128.598 0.047 1 632 342 82 VAL H H 9.101 0.009 1 633 342 82 VAL HA H 4.433 0.003 1 634 342 82 VAL HB H 2.599 0.003 1 635 342 82 VAL HG1 H 1.243 0.005 2 636 342 82 VAL HG2 H 1.31 0.002 2 637 342 82 VAL C C 176.357 0.026 1 638 342 82 VAL CA C 64.572 0.084 1 639 342 82 VAL CB C 32.297 0.174 1 640 342 82 VAL CG1 C 20.57 0.046 2 641 342 82 VAL CG2 C 22.848 0.089 2 642 342 82 VAL N N 115.126 0.047 1 643 343 83 ASP H H 7.45 0.009 1 644 343 83 ASP HA H 4.81 0.012 1 645 343 83 ASP HB2 H 3.38 0.003 2 646 343 83 ASP HB3 H 2.684 0.008 2 647 343 83 ASP C C 176.991 0.018 1 648 343 83 ASP CA C 53.545 0.064 1 649 343 83 ASP CB C 40.533 0.091 1 650 343 83 ASP N N 117.899 0.047 1 651 344 84 GLY H H 8.646 0.006 1 652 344 84 GLY HA2 H 4.17 0.004 1 653 344 84 GLY C C 174.463 0.009 1 654 344 84 GLY CA C 45.327 0.208 1 655 344 84 GLY N N 109.052 0.05 1 656 345 85 SER H H 8.455 0.005 1 657 345 85 SER HA H 4.874 0.000 1 658 345 85 SER HB2 H 4.276 0.008 2 659 345 85 SER HB3 H 4.114 0.002 2 660 345 85 SER C C 171.901 0.000 1 661 345 85 SER CA C 57.199 0.056 1 662 345 85 SER CB C 63.32 0.08 1 663 345 85 SER N N 119.222 0.05 1 664 346 86 PRO HA H 4.971 0.006 1 665 346 86 PRO HB2 H 2.399 0.202 2 666 346 86 PRO HB3 H 2.114 0.004 2 667 346 86 PRO HG2 H 2.228 0.005 2 668 346 86 PRO HG3 H 2.286 0.005 2 669 346 86 PRO HD2 H 3.799 0.003 2 670 346 86 PRO HD3 H 3.963 0.000 2 671 346 86 PRO C C 177.545 0.000 1 672 346 86 PRO CA C 62.772 0.052 1 673 346 86 PRO CB C 32.659 0.137 1 674 346 86 PRO CG C 27.285 0.082 1 675 346 86 PRO CD C 50.578 0.23 1 676 347 87 LEU H H 8.008 0.008 1 677 347 87 LEU HA H 3.977 0.015 1 678 347 87 LEU HB2 H 1.683 0.003 1 679 347 87 LEU HG H 1.721 0.006 1 680 347 87 LEU HD2 H 0.968 0.003 1 681 347 87 LEU C C 176.753 0.009 1 682 347 87 LEU CA C 55.109 0.245 1 683 347 87 LEU CB C 43.47 0.27 1 684 347 87 LEU CG C 27.164 0.339 1 685 347 87 LEU CD1 C 25.246 0.03 2 686 347 87 LEU CD2 C 23.703 0.087 2 687 347 87 LEU N N 121.642 0.047 1 688 348 88 SER H H 9.072 0.01 1 689 348 88 SER HA H 5.178 0.001 1 690 348 88 SER HB2 H 3.141 0.000 2 691 348 88 SER HB3 H 3.032 0.000 2 692 348 88 SER C C 174.877 0.000 1 693 348 88 SER CA C 56.829 0.063 1 694 348 88 SER CB C 63.841 0.102 1 695 348 88 SER N N 127.101 0.047 1 696 350 90 SER H H 7.802 0.014 1 697 350 90 SER HA H 4.39 0.007 1 698 350 90 SER HB2 H 4.039 0.003 1 699 350 90 SER C C 177.219 0.000 1 700 350 90 SER CA C 60.862 0.161 1 701 350 90 SER CB C 63.032 0.067 1 702 350 90 SER N N 119.946 0.065 1 703 351 91 PHE H H 8.331 0.006 1 704 351 91 PHE HA H 4.589 0.004 1 705 351 91 PHE HB2 H 3.524 0.008 2 706 351 91 PHE HB3 H 3.85 0.004 2 707 351 91 PHE C C 175.471 0.014 1 708 351 91 PHE CA C 57.387 0.06 1 709 351 91 PHE CB C 39.1 0.048 1 710 351 91 PHE N N 120.532 0.05 1 711 352 92 GLN H H 7.544 0.006 1 712 352 92 GLN HA H 4.232 0.01 1 713 352 92 GLN HB2 H 2.316 0.007 2 714 352 92 GLN HB3 H 2.236 0.003 2 715 352 92 GLN HG2 H 2.614 0.003 2 716 352 92 GLN HG3 H 2.411 0.01 2 717 352 92 GLN C C 177.233 0.004 1 718 352 92 GLN CA C 59.06 0.459 1 719 352 92 GLN CB C 29.848 0.635 1 720 352 92 GLN CG C 36.927 0.051 1 721 352 92 GLN N N 117.657 0.047 1 722 353 93 ARG H H 7.064 0.008 1 723 353 93 ARG HA H 4.161 0.036 1 724 353 93 ARG HB2 H 1.586 0.01 2 725 353 93 ARG HB3 H 1.543 0.002 2 726 353 93 ARG HG2 H 0.936 0.009 1 727 353 93 ARG HD2 H 2.918 0.004 1 728 353 93 ARG C C 175.841 0.022 1 729 353 93 ARG CA C 56.442 0.081 1 730 353 93 ARG CB C 29.241 0.083 1 731 353 93 ARG CG C 24.351 0.059 1 732 353 93 ARG CD C 43.446 0.057 1 733 353 93 ARG N N 113.519 0.047 1 734 354 94 TYR H H 6.827 0.011 1 735 354 94 TYR HA H 4.122 0.002 1 736 354 94 TYR HB2 H 1.428 0.001 2 737 354 94 TYR HB3 H 0.335 0.002 2 738 354 94 TYR C C 175.982 0.013 1 739 354 94 TYR CA C 58.365 0.073 1 740 354 94 TYR CB C 34.909 0.073 1 741 354 94 TYR N N 118.274 0.047 1 742 355 95 TRP H H 6.508 0.013 1 743 355 95 TRP HA H 4.492 0.031 1 744 355 95 TRP HB2 H 3.262 0.006 2 745 355 95 TRP HB3 H 2.895 0.004 2 746 355 95 TRP C C 177.704 0.009 1 747 355 95 TRP CA C 57.774 0.105 1 748 355 95 TRP CB C 30.604 0.076 1 749 355 95 TRP N N 117.965 0.047 1 750 356 96 ASN H H 9.995 0.014 1 751 356 96 ASN HB2 H 3.117 0.000 1 752 356 96 ASN C C 175.538 0.000 1 753 356 96 ASN CA C 53.208 0.198 1 754 356 96 ASN CB C 39.19 0.097 1 755 356 96 ASN N N 123.051 0.047 1 756 357 97 SER H H 8.597 0.009 1 757 357 97 SER HA H 4.338 0.000 1 758 357 97 SER HB2 H 3.975 0.006 1 759 357 97 SER C C 175.626 0.000 1 760 357 97 SER CA C 60.527 0.042 1 761 357 97 SER CB C 63.047 0.074 1 762 357 97 SER N N 114.278 0.047 1 763 358 98 GLY C C 173.345 0.000 1 764 358 98 GLY CA C 45.724 0.052 1 765 359 99 GLU H H 8.329 0.01 1 766 359 99 GLU C C 173.944 0.000 1 767 359 99 GLU CA C 52.557 0.000 1 768 359 99 GLU CB C 29.617 0.000 1 769 359 99 GLU N N 118.916 0.052 1 770 362 102 ASN CA C 54.688 0.000 1 771 363 103 SER H H 7.686 0.009 1 772 363 103 SER HA H 4.131 0.002 1 773 363 103 SER HB2 H 3.63 0.003 1 774 363 103 SER C C 174.631 0.000 1 775 363 103 SER CA C 59.519 0.123 1 776 363 103 SER CB C 62.263 0.051 1 777 363 103 SER N N 114.038 0.06 1 778 364 104 GLY H H 8.685 0.009 1 779 364 104 GLY HA2 H 3.971 0.007 1 780 364 104 GLY C C 175.084 0.022 1 781 364 104 GLY CA C 46.822 0.18 1 782 364 104 GLY N N 118.089 0.05 1 783 365 105 ASN H H 7.714 0.008 1 784 365 105 ASN HA H 4.045 0.000 1 785 365 105 ASN HB2 H 2.656 0.002 2 786 365 105 ASN HB3 H 2.609 0.000 2 787 365 105 ASN C C 173.529 0.018 1 788 365 105 ASN CA C 55.363 0.136 1 789 365 105 ASN CB C 36.759 0.051 1 790 365 105 ASN N N 114.478 0.05 1 791 366 106 GLU H H 7.708 0.011 1 792 366 106 GLU HA H 4.11 0.015 1 793 366 106 GLU HB2 H 2.173 0.1 1 794 366 106 GLU HG2 H 2.5 0.001 2 795 366 106 GLU HG3 H 2.011 0.004 2 796 366 106 GLU C C 177.215 0.004 1 797 366 106 GLU CA C 56.092 0.074 1 798 366 106 GLU CB C 31.735 0.071 1 799 366 106 GLU CG C 37.36 0.053 1 800 366 106 GLU N N 123.306 0.05 1 801 367 107 ASP H H 8.078 0.008 1 802 367 107 ASP HA H 5.499 1.417 1 803 367 107 ASP HB2 H 2.787 0.004 2 804 367 107 ASP HB3 H 2.656 0.011 2 805 367 107 ASP C C 174.075 0.018 1 806 367 107 ASP CA C 51.465 0.027 1 807 367 107 ASP CB C 41.554 0.081 1 808 367 107 ASP N N 125.153 0.047 1 809 368 108 CYS H H 8.204 0.007 1 810 368 108 CYS HB2 H 2.466 0.008 2 811 368 108 CYS HB3 H 2.049 0.006 2 812 368 108 CYS C C 172.54 0.005 1 813 368 108 CYS CA C 59.357 0.059 1 814 368 108 CYS CB C 49.141 0.059 1 815 368 108 CYS N N 116.468 0.047 1 816 369 109 ALA H H 8.168 0.009 1 817 369 109 ALA HA H 5.54 0.005 1 818 369 109 ALA HB H 1.167 0.003 1 819 369 109 ALA C C 174.824 0.009 1 820 369 109 ALA CA C 52.054 0.05 1 821 369 109 ALA CB C 21.436 0.058 1 822 369 109 ALA N N 126.529 0.047 1 823 370 110 GLU H H 9.231 0.015 1 824 370 110 GLU HA H 5.67 0.026 1 825 370 110 GLU HB2 H 1.704 0.006 2 826 370 110 GLU HB3 H 1.768 0.001 2 827 370 110 GLU HG2 H 2.45 0.004 2 828 370 110 GLU HG3 H 2.06 0.004 2 829 370 110 GLU C C 175.586 0.013 1 830 370 110 GLU CA C 52.393 0.051 1 831 370 110 GLU CB C 33.544 0.128 1 832 370 110 GLU CG C 35.202 0.054 1 833 370 110 GLU N N 116.975 0.047 1 834 371 111 PHE H H 9.455 0.012 1 835 371 111 PHE HA H 4.046 0.000 1 836 371 111 PHE HB2 H 2.282 0.004 2 837 371 111 PHE HB3 H 2.231 0.000 2 838 371 111 PHE C C 175.74 0.009 1 839 371 111 PHE CA C 59.136 0.132 1 840 371 111 PHE CB C 41.069 0.05 1 841 371 111 PHE N N 121.069 0.047 1 842 372 112 SER H H 8.797 0.01 1 843 372 112 SER C C 174.697 0.022 1 844 372 112 SER CA C 56.416 0.068 1 845 372 112 SER CB C 64.659 0.016 1 846 372 112 SER N N 117.019 0.047 1 847 373 113 GLY H H 8.658 0.011 1 848 373 113 GLY C C 174.886 0.000 1 849 373 113 GLY CA C 47.294 0.038 1 850 373 113 GLY N N 114.907 0.05 1 851 374 114 SER C C 173.838 0.000 1 852 374 114 SER CA C 58.728 0.000 1 853 374 114 SER CB C 64.316 0.000 1 854 375 115 GLY H H 7.656 0.006 1 855 375 115 GLY C C 172.851 0.017 1 856 375 115 GLY CA C 46.609 0.103 1 857 375 115 GLY N N 113.589 0.052 1 858 376 116 TRP H H 8.441 0.01 1 859 376 116 TRP HA H 6.007 0.006 1 860 376 116 TRP HB2 H 2.706 0.002 2 861 376 116 TRP HB3 H 2.552 0.011 2 862 376 116 TRP C C 177.057 0.014 1 863 376 116 TRP CA C 53.021 0.027 1 864 376 116 TRP CB C 32.561 0.1 1 865 376 116 TRP N N 122.392 0.05 1 866 377 117 ASN H H 9.343 0.015 1 867 377 117 ASN HA H 5.597 0.014 1 868 377 117 ASN HB2 H 3.077 0.012 1 869 377 117 ASN C C 175.503 0.036 1 870 377 117 ASN CA C 52.005 0.052 1 871 377 117 ASN CB C 42.441 0.062 1 872 377 117 ASN N N 118.031 0.047 1 873 378 118 ASP H H 9.285 0.01 1 874 378 118 ASP HA H 5.374 0.02 1 875 378 118 ASP HB2 H 2.757 0.005 2 876 378 118 ASP HB3 H 2.012 0.005 2 877 378 118 ASP C C 173.671 0.000 1 878 378 118 ASP CA C 52.379 0.144 1 879 378 118 ASP CB C 43.83 0.625 1 880 378 118 ASP N N 120.677 0.052 1 881 379 119 ASN H H 10.067 0.014 1 882 379 119 ASN HA H 5.477 0.006 1 883 379 119 ASN HB2 H 2.99 0.008 2 884 379 119 ASN HB3 H 2.461 0.000 2 885 379 119 ASN C C 174.67 0.022 1 886 379 119 ASN CA C 49.326 0.062 1 887 379 119 ASN CB C 41.943 0.117 1 888 379 119 ASN N N 125.031 0.046 1 889 380 120 ARG H H 9.618 0.011 1 890 380 120 ARG HB2 H 2.401 0.006 2 891 380 120 ARG HB3 H 2.065 0.003 2 892 380 120 ARG HG2 H 2.142 0.002 2 893 380 120 ARG HG3 H 1.966 0.005 2 894 380 120 ARG HD2 H 3.546 0.005 2 895 380 120 ARG HD3 H 3.447 0.004 2 896 380 120 ARG C C 178.567 0.000 1 897 380 120 ARG CA C 56.737 0.097 1 898 380 120 ARG CB C 31.032 0.07 1 899 380 120 ARG CG C 28.173 0.054 1 900 380 120 ARG CD C 43.852 0.046 1 901 380 120 ARG N N 122.699 0.047 1 902 381 121 CYS H H 8.641 0.01 1 903 381 121 CYS HA H 4.214 0.003 1 904 381 121 CYS HB2 H 3.223 0.01 2 905 381 121 CYS HB3 H 3.021 0.009 2 906 381 121 CYS CA C 58.591 0.057 1 907 381 121 CYS CB C 46.17 0.045 1 908 381 121 CYS N N 119.885 0.052 1 909 382 122 ASP H H 8.635 0.011 1 910 382 122 ASP HA H 4.231 0.596 1 911 382 122 ASP HB2 H 3.058 0.026 2 912 382 122 ASP HB3 H 2.837 0.007 2 913 382 122 ASP C C 176.272 0.005 1 914 382 122 ASP CA C 48.42 6.764 1 915 382 122 ASP CB C 41.725 3.63 1 916 382 122 ASP N N 114.203 0.05 1 917 383 123 VAL H H 7.785 0.009 1 918 383 123 VAL HA H 4.207 0.006 1 919 383 123 VAL HB H 2.497 0.005 1 920 383 123 VAL HG1 H 0.958 0.005 1 921 383 123 VAL HG2 H 1.203 0.003 1 922 383 123 VAL C C 174.005 0.000 1 923 383 123 VAL CA C 63.027 0.105 1 924 383 123 VAL CB C 33.131 0.093 1 925 383 123 VAL CG1 C 21.505 0.109 2 926 383 123 VAL CG2 C 22.186 0.059 2 927 383 123 VAL N N 121.171 0.05 1 928 384 124 ASP H H 7.857 0.019 1 929 384 124 ASP HA H 5.202 0.006 1 930 384 124 ASP HB2 H 2.434 0.1 2 931 384 124 ASP HB3 H 2.158 0.005 2 932 384 124 ASP C C 174.419 0.000 1 933 384 124 ASP CA C 54.24 0.209 1 934 384 124 ASP CB C 41.344 0.26 1 935 384 124 ASP N N 121.206 0.057 1 936 385 125 ASN H H 8.607 0.011 1 937 385 125 ASN HA H 5.237 0.012 1 938 385 125 ASN HB2 H 1.05 0.004 2 939 385 125 ASN HB3 H 2.674 0.01 2 940 385 125 ASN C C 177.012 0.005 1 941 385 125 ASN CA C 50.532 0.043 1 942 385 125 ASN CB C 41.778 0.079 1 943 385 125 ASN N N 123.183 0.047 1 944 386 126 TYR H H 7.257 0.015 1 945 386 126 TYR C C 173.856 0.000 1 946 386 126 TYR CA C 60.301 0.031 1 947 386 126 TYR CB C 37.977 0.000 1 948 386 126 TYR N N 116.446 0.047 1 949 392 132 PRO HA H 5.141 0.008 1 950 392 132 PRO HB2 H 2.544 0.003 2 951 392 132 PRO HB3 H 1.973 0.008 2 952 392 132 PRO HG2 H 2.224 0.003 2 953 392 132 PRO HG3 H 2.137 0.004 2 954 392 132 PRO HD2 H 3.807 0.007 2 955 392 132 PRO HD3 H 3.965 0.005 2 956 392 132 PRO CA C 63.459 0.063 1 957 392 132 PRO CB C 32.453 0.085 1 958 392 132 PRO CG C 28.047 0.082 1 959 392 132 PRO CD C 51.003 0.075 1 960 393 133 ALA H H 7.838 0.01 1 961 393 133 ALA C C 176.634 0.013 1 962 393 133 ALA CA C 52.813 0.068 1 963 393 133 ALA CB C 18.993 0.304 1 964 393 133 ALA N N 123.207 0.05 1 965 394 134 ALA H H 8.847 0.013 1 966 394 134 ALA HB H 1.381 0.003 1 967 394 134 ALA C C 177.123 0.000 1 968 394 134 ALA CA C 51.192 0.059 1 969 394 134 ALA CB C 21.09 0.119 1 970 394 134 ALA N N 123.491 0.047 1 971 397 137 ARG HA H 4.189 0.004 1 972 397 137 ARG HB2 H 1.651 0.004 2 973 397 137 ARG HB3 H 1.775 0.004 2 974 397 137 ARG HG2 H 1.5 0.005 1 975 397 137 ARG HD2 H 3.2 0.005 1 976 397 137 ARG C C 175.546 0.000 1 977 397 137 ARG CA C 56.292 0.109 1 978 397 137 ARG CB C 31.162 0.078 1 979 397 137 ARG CG C 27.113 0.043 1 980 397 137 ARG CD C 43.555 0.054 1 981 398 138 ASP H H 8.365 0.011 1 982 398 138 ASP HA H 5.259 0.007 1 983 398 138 ASP HB2 H 2.781 0.000 2 984 398 138 ASP HB3 H 2.632 0.004 2 985 398 138 ASP C C 175.071 0.009 1 986 398 138 ASP CA C 54.557 0.048 1 987 398 138 ASP CB C 41.252 0.121 1 988 398 138 ASP N N 122.522 0.047 1 989 399 139 GLU H H 7.854 0.008 1 990 399 139 GLU HA H 4.214 0.008 1 991 399 139 GLU HB2 H 2.121 0.005 2 992 399 139 GLU HB3 H 1.972 0.01 2 993 399 139 GLU HG2 H 2.253 0.004 1 994 399 139 GLU C C 180.944 0.000 1 995 399 139 GLU CA C 58.011 0.078 1 996 399 139 GLU CB C 31.606 0.052 1 997 399 139 GLU CG C 36.688 0.022 1 998 399 139 GLU N N 125.781 0.047 1 stop_ save_