data_5204 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignments for CRT(189-261) ; _BMRB_accession_number 5204 _BMRB_flat_file_name bmr5204.str _Entry_type original _Submission_date 2001-11-09 _Accession_date 2001-11-09 _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 Ellgaard Lars . . 2 Bettendorff Pascal . . 3 Braun Daniel . . 4 Herrmann Torsten . . 5 Fiorito Francesco . . 6 Guentert Peter . . 7 Helenius Ari . . 8 Wuethrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 474 "13C chemical shifts" 258 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-10-17 update author 'correction of citation.' 2002-09-12 original author 'original release.' stop_ loop_ _Related_BMRB_accession_number _Relationship 4878 'Calreticulin P-domain' 5205 'Calreticulin P-domain fragment 221-256' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Structures of 36 and 73-residue Fragments of the Calreticulin P-domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12270713 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ellgaard Lars . . 2 Bettendorff Pascal . . 3 Braun Daniel . . 4 Herrmann Torsten . . 5 Fiorito Francesco . . 6 Jelesarov Ilian . . 7 Guentert Peter . . 8 Helenius Ari . . 9 Wuethrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 322 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 773 _Page_last 784 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_CRT(189-261) _Saveframe_category molecular_system _Mol_system_name 'Calreticulin P-domain fragment 189-261' _Abbreviation_common CRT(189-261) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CRT(189-261) $CRT(189-261) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CRT(189-261) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Calreticulin P-domain fragment' _Abbreviation_common CRT(189-261) _Molecular_mass . _Mol_thiol_state 'not present' _Details 'proline rich' ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; SKKIKDPDAAKPEDWDERAK IDDPTDSKPEDWDKPEHIPD PDAKKPEDWDEEMDGEWEPP VIQNPEYKGEWKPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 188 SER 2 189 LYS 3 190 LYS 4 191 ILE 5 192 LYS 6 193 ASP 7 194 PRO 8 195 ASP 9 196 ALA 10 197 ALA 11 198 LYS 12 199 PRO 13 200 GLU 14 201 ASP 15 202 TRP 16 203 ASP 17 204 GLU 18 205 ARG 19 206 ALA 20 207 LYS 21 208 ILE 22 209 ASP 23 210 ASP 24 211 PRO 25 212 THR 26 213 ASP 27 214 SER 28 215 LYS 29 216 PRO 30 217 GLU 31 218 ASP 32 219 TRP 33 220 ASP 34 221 LYS 35 222 PRO 36 223 GLU 37 224 HIS 38 225 ILE 39 226 PRO 40 227 ASP 41 228 PRO 42 229 ASP 43 230 ALA 44 231 LYS 45 232 LYS 46 233 PRO 47 234 GLU 48 235 ASP 49 236 TRP 50 237 ASP 51 238 GLU 52 239 GLU 53 240 MET 54 241 ASP 55 242 GLY 56 243 GLU 57 244 TRP 58 245 GLU 59 246 PRO 60 247 PRO 61 248 VAL 62 249 ILE 63 250 GLN 64 251 ASN 65 252 PRO 66 253 GLU 67 254 TYR 68 255 LYS 69 256 GLY 70 257 GLU 71 258 TRP 72 259 LYS 73 260 PRO 74 261 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 17224 CRT 98.65 100 98.63 100.00 1.81e-38 BMRB 4878 CRT 98.65 100 100.00 100.00 1.28e-38 PDB 1HHN "Calreticulin P-Domain" 98.65 101 100.00 100.00 1.31e-38 PDB 1K9C "Solution Structure Of Calreticulin P-Domain Subdomain (Residues 189-261)" 98.65 74 100.00 100.00 1.09e-38 DBJ BAA11345 "calreticulin [Rattus norvegicus]" 98.65 416 100.00 100.00 3.58e-39 DBJ BAB86913 "calreticulin [Bos taurus]" 98.65 417 98.63 100.00 1.72e-38 DBJ BAC35852 "unnamed protein product [Mus musculus]" 98.65 416 100.00 100.00 4.36e-39 DBJ BAD96780 "calreticulin precursor variant [Homo sapiens]" 98.65 406 98.63 100.00 1.44e-38 DBJ BAE01267 "unnamed protein product [Macaca fascicularis]" 98.65 417 98.63 100.00 1.14e-38 EMBL CAA33053 "calreticulin precursor protein [Mus musculus]" 98.65 416 100.00 100.00 4.36e-39 EMBL CAA37446 "precursor (AA -17 to 399) [Rattus norvegicus]" 98.65 416 100.00 100.00 3.58e-39 EMBL CAA55890 "calreticulin [Rattus norvegicus]" 98.65 416 100.00 100.00 3.58e-39 EMBL CAG33351 "CALR [Homo sapiens]" 98.65 417 98.63 100.00 1.14e-38 GB AAA31188 "calreticulin precursor [Oryctolagus cuniculus]" 98.65 418 98.63 100.00 1.36e-38 GB AAA36582 "Ro ribonucleoprotein autoantigen (Ro/SS-A) precursor [Homo sapiens]" 98.65 417 98.63 100.00 1.14e-38 GB AAA37569 "calregulin [Mus musculus]" 98.65 416 100.00 100.00 4.36e-39 GB AAA51916 "calreticulin [Homo sapiens]" 98.65 417 98.63 100.00 1.14e-38 GB AAB20096 "calreticulin [rabbits, sketetal muscle, Peptide, 401 aa]" 98.65 401 98.63 100.00 1.06e-38 REF NP_001075704 "calreticulin precursor [Oryctolagus cuniculus]" 98.65 418 98.63 100.00 1.36e-38 REF NP_001167604 "calreticulin precursor [Sus scrofa]" 98.65 417 98.63 98.63 1.26e-38 REF NP_001231051 "calreticulin precursor [Cricetulus griseus]" 98.65 417 100.00 100.00 3.27e-39 REF NP_001248060 "calreticulin precursor [Macaca mulatta]" 98.65 417 98.63 100.00 1.14e-38 REF NP_001274539 "calreticulin precursor [Macaca fascicularis]" 98.65 417 98.63 100.00 1.14e-38 SP P14211 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 98.65 416 100.00 100.00 4.36e-39 SP P15253 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 98.65 418 98.63 100.00 1.36e-38 SP P18418 "RecName: Full=Calreticulin; AltName: Full=CALBP; AltName: Full=CRP55; AltName: Full=Calcium-binding protein 3; Short=CABP3; Alt" 98.65 416 100.00 100.00 3.58e-39 SP P27797 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 98.65 417 98.63 100.00 1.14e-38 SP P28491 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 98.65 417 98.63 98.63 1.26e-38 TPG DAA28020 "TPA: calreticulin precursor [Bos taurus]" 98.65 417 98.63 100.00 1.46e-38 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CRT(189-261) Rat 10116 Eukaryota Metazoa Rattus norvegicus 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 $CRT(189-261) 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CRT(189-261) 3 mM '[U-15N; U-13C]' 'sodium phosphate buffer' 50 mM . CaCl2 10 mM . D20 25 ul . H20 275 ul . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_1H-13C-1H_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_3D_13C-1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _Sample_label . save_ save_3D_COMBINED_1H-1H-13C/15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D COMBINED 1H-1H-13C/15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D COMBINED 1H-1H-13C/15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 293.4 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CRT(189-261) _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 SER CA C 58.3 0.2 1 2 . 1 SER HA H 4.47 0.02 1 3 . 1 SER CB C 64.1 0.2 1 4 . 1 SER HB2 H 3.83 0.02 1 5 . 1 SER HB3 H 3.83 0.02 1 6 . 2 LYS N N 123.7 0.2 1 7 . 2 LYS H H 8.48 0.02 1 8 . 2 LYS CA C 56.2 0.2 1 9 . 2 LYS HA H 4.26 0.02 1 10 . 2 LYS CB C 33.0 0.2 1 11 . 2 LYS HB2 H 1.79 0.02 2 12 . 2 LYS HB3 H 1.71 0.02 2 13 . 2 LYS CG C 24.7 0.2 1 14 . 2 LYS HG2 H 1.42 0.02 2 15 . 2 LYS HG3 H 1.40 0.02 2 16 . 2 LYS CD C 28.9 0.2 1 17 . 2 LYS HD2 H 1.63 0.02 1 18 . 2 LYS HD3 H 1.63 0.02 1 19 . 2 LYS CE C 42.3 0.2 1 20 . 2 LYS HE2 H 2.93 0.02 1 21 . 2 LYS HE3 H 2.93 0.02 1 22 . 3 LYS N N 123.6 0.2 1 23 . 3 LYS H H 8.30 0.02 1 24 . 3 LYS CA C 56.2 0.2 1 25 . 3 LYS HA H 4.26 0.02 1 26 . 3 LYS CB C 32.8 0.2 1 27 . 3 LYS HB2 H 1.74 0.02 2 28 . 3 LYS HB3 H 1.68 0.02 2 29 . 3 LYS CG C 24.7 0.2 1 30 . 3 LYS HG2 H 1.39 0.02 2 31 . 3 LYS HG3 H 1.36 0.02 2 32 . 3 LYS CD C 28.9 0.2 1 33 . 3 LYS HD2 H 1.64 0.02 1 34 . 3 LYS HD3 H 1.64 0.02 1 35 . 3 LYS CE C 42.3 0.2 1 36 . 3 LYS HE2 H 2.94 0.02 1 37 . 3 LYS HE3 H 2.94 0.02 1 38 . 4 ILE N N 123.0 0.2 1 39 . 4 ILE H H 8.17 0.02 1 40 . 4 ILE CA C 60.9 0.2 1 41 . 4 ILE HA H 4.11 0.02 1 42 . 4 ILE CB C 38.8 0.2 1 43 . 4 ILE HB H 1.80 0.02 1 44 . 4 ILE HG2 H 0.86 0.02 1 45 . 4 ILE CG2 C 17.5 0.2 1 46 . 4 ILE CG1 C 27.1 0.2 1 47 . 4 ILE HG12 H 1.43 0.02 2 48 . 4 ILE HG13 H 1.15 0.02 2 49 . 4 ILE HD1 H 0.82 0.02 1 50 . 4 ILE CD1 C 12.7 0.2 1 51 . 5 LYS N N 126.0 0.2 1 52 . 5 LYS H H 8.37 0.02 1 53 . 5 LYS CA C 56.2 0.2 1 54 . 5 LYS HA H 4.26 0.02 1 55 . 5 LYS CB C 32.7 0.2 1 56 . 5 LYS HB2 H 1.70 0.02 1 57 . 5 LYS HB3 H 1.70 0.02 1 58 . 5 LYS CG C 24.4 0.2 1 59 . 5 LYS HG2 H 1.39 0.02 1 60 . 5 LYS HG3 H 1.39 0.02 1 61 . 5 LYS CD C 29.1 0.2 1 62 . 5 LYS HD2 H 1.63 0.02 1 63 . 5 LYS HD3 H 1.63 0.02 1 64 . 5 LYS CE C 42.0 0.2 1 65 . 5 LYS HE2 H 2.94 0.02 1 66 . 5 LYS HE3 H 2.94 0.02 1 67 . 6 ASP N N 123.7 0.2 1 68 . 6 ASP H H 8.36 0.02 1 69 . 6 ASP CA C 51.8 0.2 1 70 . 6 ASP HA H 4.80 0.02 1 71 . 6 ASP CB C 40.8 0.2 1 72 . 6 ASP HB2 H 2.73 0.02 2 73 . 6 ASP HB3 H 2.50 0.02 2 74 . 7 PRO CD C 50.8 0.2 1 75 . 7 PRO CA C 63.7 0.2 1 76 . 7 PRO HA H 4.33 0.02 1 77 . 7 PRO CB C 32.0 0.2 1 78 . 7 PRO HB2 H 2.25 0.02 2 79 . 7 PRO HB3 H 1.91 0.02 2 80 . 7 PRO CG C 27.1 0.2 1 81 . 7 PRO HG2 H 1.97 0.02 1 82 . 7 PRO HG3 H 1.97 0.02 1 83 . 7 PRO HD2 H 3.81 0.02 2 84 . 7 PRO HD3 H 3.77 0.02 2 85 . 8 ASP N N 119.4 0.2 1 86 . 8 ASP H H 8.35 0.02 1 87 . 8 ASP CA C 54.3 0.2 1 88 . 8 ASP HA H 4.55 0.02 1 89 . 8 ASP CB C 40.9 0.2 1 90 . 8 ASP HB2 H 2.69 0.02 2 91 . 8 ASP HB3 H 2.55 0.02 2 92 . 9 ALA N N 124.0 0.2 1 93 . 9 ALA H H 7.87 0.02 1 94 . 9 ALA CA C 52.4 0.2 1 95 . 9 ALA HA H 4.21 0.02 1 96 . 9 ALA HB H 1.36 0.02 1 97 . 9 ALA CB C 19.4 0.2 1 98 . 10 ALA N N 123.0 0.2 1 99 . 10 ALA H H 8.16 0.02 1 100 . 10 ALA CA C 52.4 0.2 1 101 . 10 ALA HA H 4.24 0.02 1 102 . 10 ALA HB H 1.34 0.02 1 103 . 10 ALA CB C 19.1 0.2 1 104 . 11 LYS N N 122.0 0.2 1 105 . 11 LYS H H 8.21 0.02 1 106 . 11 LYS CA C 54.1 0.2 1 107 . 11 LYS HA H 4.50 0.02 1 108 . 11 LYS CB C 32.5 0.2 1 109 . 11 LYS HB2 H 1.62 0.02 2 110 . 11 LYS HB3 H 1.70 0.02 2 111 . 11 LYS CG C 24.2 0.2 1 112 . 11 LYS HG2 H 1.31 0.02 1 113 . 11 LYS HG3 H 1.31 0.02 1 114 . 11 LYS CD C 28.9 0.2 1 115 . 11 LYS HD2 H 1.50 0.02 2 116 . 11 LYS HD3 H 1.45 0.02 2 117 . 11 LYS CE C 42.0 0.2 1 118 . 11 LYS HE2 H 2.83 0.02 1 119 . 11 LYS HE3 H 2.83 0.02 1 120 . 12 PRO CD C 50.5 0.2 1 121 . 12 PRO CA C 63.2 0.2 1 122 . 12 PRO HA H 4.28 0.02 1 123 . 12 PRO CB C 32.0 0.2 1 124 . 12 PRO HB2 H 2.25 0.02 2 125 . 12 PRO HB3 H 1.89 0.02 2 126 . 12 PRO CG C 27.6 0.2 1 127 . 12 PRO HG2 H 1.99 0.02 1 128 . 12 PRO HG3 H 1.99 0.02 1 129 . 12 PRO HD2 H 3.73 0.02 2 130 . 12 PRO HD3 H 3.54 0.02 2 131 . 13 GLU N N 120.6 0.2 1 132 . 13 GLU H H 8.71 0.02 1 133 . 13 GLU CA C 57.3 0.2 1 134 . 13 GLU HA H 4.12 0.02 1 135 . 13 GLU CB C 29.7 0.2 1 136 . 13 GLU HB2 H 1.88 0.02 2 137 . 13 GLU HB3 H 1.83 0.02 2 138 . 13 GLU CG C 36.2 0.2 1 139 . 13 GLU HG2 H 2.22 0.02 1 140 . 13 GLU HG3 H 2.22 0.02 1 141 . 14 ASP N N 120.0 0.2 1 142 . 14 ASP H H 8.28 0.02 1 143 . 14 ASP CA C 53.9 0.2 1 144 . 14 ASP HA H 4.55 0.02 1 145 . 14 ASP CB C 40.2 0.2 1 146 . 14 ASP HB2 H 2.65 0.02 2 147 . 14 ASP HB3 H 2.62 0.02 2 148 . 15 TRP N N 121.2 0.2 1 149 . 15 TRP H H 7.90 0.02 1 150 . 15 TRP CA C 58.0 0.2 1 151 . 15 TRP HA H 4.48 0.02 1 152 . 15 TRP CB C 29.4 0.2 1 153 . 15 TRP HB2 H 3.26 0.02 1 154 . 15 TRP HB3 H 3.26 0.02 1 155 . 15 TRP CD1 C 126.7 0.2 1 156 . 15 TRP NE1 N 129.4 0.2 1 157 . 15 TRP HD1 H 7.24 0.02 1 158 . 15 TRP CZ2 C 114.4 0.2 1 159 . 15 TRP HE1 H 10.15 0.02 1 160 . 15 TRP CH2 C 124.1 0.2 1 161 . 15 TRP HZ2 H 7.45 0.02 1 162 . 15 TRP HH2 H 7.19 0.02 1 163 . 16 ASP N N 121.7 0.2 1 164 . 16 ASP H H 8.06 0.02 1 165 . 16 ASP CA C 54.3 0.2 1 166 . 16 ASP HA H 4.41 0.02 1 167 . 16 ASP CB C 40.9 0.2 1 168 . 16 ASP HB2 H 2.46 0.02 2 169 . 16 ASP HB3 H 2.40 0.02 2 170 . 17 GLU N N 121.6 0.2 1 171 . 17 GLU H H 8.10 0.02 1 172 . 17 GLU CA C 57.1 0.2 1 173 . 17 GLU HA H 4.04 0.02 1 174 . 17 GLU CB C 29.6 0.2 1 175 . 17 GLU HB2 H 2.01 0.02 2 176 . 17 GLU HB3 H 1.91 0.02 2 177 . 17 GLU CG C 36.2 0.2 1 178 . 17 GLU HG2 H 2.19 0.02 1 179 . 17 GLU HG3 H 2.19 0.02 1 180 . 18 ARG N N 120.5 0.2 1 181 . 18 ARG H H 8.08 0.02 1 182 . 18 ARG CA C 56.3 0.2 1 183 . 18 ARG HA H 4.16 0.02 1 184 . 18 ARG CB C 30.4 0.2 1 185 . 18 ARG HB2 H 1.79 0.02 2 186 . 18 ARG HB3 H 1.72 0.02 2 187 . 18 ARG CG C 26.9 0.2 1 188 . 18 ARG HG2 H 1.57 0.02 1 189 . 18 ARG HG3 H 1.57 0.02 1 190 . 18 ARG CD C 43.3 0.2 1 191 . 18 ARG HD2 H 3.07 0.02 1 192 . 18 ARG HD3 H 3.07 0.02 1 193 . 18 ARG NE N 85.1 0.2 1 194 . 18 ARG HE H 7.20 0.02 1 195 . 19 ALA N N 123.8 0.2 1 196 . 19 ALA H H 8.03 0.02 1 197 . 19 ALA CA C 52.7 0.2 1 198 . 19 ALA HA H 4.19 0.02 1 199 . 19 ALA HB H 1.30 0.02 1 200 . 19 ALA CB C 19.0 0.2 1 201 . 20 LYS N N 120.4 0.2 1 202 . 20 LYS H H 8.05 0.02 1 203 . 20 LYS CA C 56.1 0.2 1 204 . 20 LYS HA H 4.26 0.02 1 205 . 20 LYS CB C 33.0 0.2 1 206 . 20 LYS HB2 H 1.73 0.02 2 207 . 20 LYS HB3 H 1.68 0.02 2 208 . 20 LYS CG C 24.7 0.2 1 209 . 20 LYS HG2 H 1.40 0.02 2 210 . 20 LYS HG3 H 1.34 0.02 2 211 . 20 LYS CD C 28.9 0.2 1 212 . 20 LYS HD2 H 1.63 0.02 1 213 . 20 LYS HD3 H 1.63 0.02 1 214 . 20 LYS CE C 42.3 0.2 1 215 . 20 LYS HE2 H 2.93 0.02 1 216 . 20 LYS HE3 H 2.93 0.02 1 217 . 21 ILE N N 122.0 0.2 1 218 . 21 ILE H H 8.06 0.02 1 219 . 21 ILE CA C 61.1 0.2 1 220 . 21 ILE HA H 4.13 0.02 1 221 . 21 ILE CB C 38.8 0.2 1 222 . 21 ILE HB H 1.82 0.02 1 223 . 21 ILE HG2 H 0.87 0.02 1 224 . 21 ILE CG2 C 17.4 0.2 1 225 . 21 ILE CG1 C 27.1 0.2 1 226 . 21 ILE HG12 H 1.42 0.02 2 227 . 21 ILE HG13 H 1.14 0.02 2 228 . 21 ILE HD1 H 0.83 0.02 1 229 . 21 ILE CD1 C 12.7 0.2 1 230 . 22 ASP N N 124.4 0.2 1 231 . 22 ASP H H 8.35 0.02 1 232 . 22 ASP CA C 54.1 0.2 1 233 . 22 ASP HA H 4.55 0.02 1 234 . 22 ASP CB C 41.1 0.2 1 235 . 22 ASP HB2 H 2.62 0.02 2 236 . 22 ASP HB3 H 2.54 0.02 2 237 . 23 ASP N N 122.0 0.2 1 238 . 23 ASP H H 8.23 0.02 1 239 . 23 ASP CA C 52.2 0.2 1 240 . 23 ASP HA H 4.85 0.02 1 241 . 23 ASP CB C 41.2 0.2 1 242 . 23 ASP HB2 H 2.76 0.02 2 243 . 23 ASP HB3 H 2.50 0.02 2 244 . 24 PRO CD C 50.8 0.2 1 245 . 24 PRO CA C 63.7 0.2 1 246 . 24 PRO HA H 4.48 0.02 1 247 . 24 PRO CB C 32.0 0.2 1 248 . 24 PRO HB2 H 2.26 0.02 2 249 . 24 PRO HB3 H 1.99 0.02 2 250 . 24 PRO CG C 27.1 0.2 1 251 . 24 PRO HG2 H 1.99 0.02 1 252 . 24 PRO HG3 H 1.99 0.02 1 253 . 24 PRO HD2 H 3.81 0.02 2 254 . 24 PRO HD3 H 3.77 0.02 2 255 . 25 THR N N 113.4 0.2 1 256 . 25 THR H H 8.35 0.02 1 257 . 25 THR CA C 62.5 0.2 1 258 . 25 THR HA H 4.26 0.02 1 259 . 25 THR CB C 69.7 0.2 1 260 . 25 THR HB H 4.24 0.02 1 261 . 25 THR HG2 H 1.20 0.02 1 262 . 25 THR CG2 C 21.6 0.2 1 263 . 26 ASP N N 122.6 0.2 1 264 . 26 ASP H H 8.17 0.02 1 265 . 26 ASP CA C 54.2 0.2 1 266 . 26 ASP HA H 4.66 0.02 1 267 . 26 ASP CB C 41.2 0.2 1 268 . 26 ASP HB2 H 2.72 0.02 2 269 . 26 ASP HB3 H 2.64 0.02 2 270 . 27 SER N N 115.8 0.2 1 271 . 27 SER H H 8.08 0.02 1 272 . 27 SER CA C 58.0 0.2 1 273 . 27 SER HA H 4.37 0.02 1 274 . 27 SER CB C 64.1 0.2 1 275 . 27 SER HB2 H 3.78 0.02 1 276 . 27 SER HB3 H 3.78 0.02 1 277 . 28 LYS N N 125.0 0.2 1 278 . 28 LYS H H 8.14 0.02 1 279 . 28 LYS CA C 54.0 0.2 1 280 . 28 LYS HA H 3.79 0.02 1 281 . 28 LYS CB C 32.4 0.2 1 282 . 28 LYS HB2 H 1.50 0.02 2 283 . 28 LYS HB3 H 1.25 0.02 2 284 . 28 LYS CG C 24.1 0.2 1 285 . 28 LYS HG2 H 1.21 0.02 2 286 . 28 LYS HG3 H 0.95 0.02 2 287 . 28 LYS CD C 29.1 0.2 1 288 . 28 LYS HD2 H 1.46 0.02 1 289 . 28 LYS HD3 H 1.46 0.02 1 290 . 28 LYS CE C 42.0 0.2 1 291 . 28 LYS HE2 H 2.82 0.02 1 292 . 28 LYS HE3 H 2.82 0.02 1 293 . 29 PRO CD C 50.5 0.2 1 294 . 29 PRO CA C 63.2 0.2 1 295 . 29 PRO HA H 4.21 0.02 1 296 . 29 PRO CB C 32.3 0.2 1 297 . 29 PRO HB2 H 2.23 0.02 2 298 . 29 PRO HB3 H 1.88 0.02 2 299 . 29 PRO CG C 27.6 0.2 1 300 . 29 PRO HG2 H 2.00 0.02 2 301 . 29 PRO HG3 H 1.91 0.02 2 302 . 29 PRO HD2 H 3.52 0.02 2 303 . 29 PRO HD3 H 3.21 0.02 2 304 . 30 GLU N N 121.0 0.2 1 305 . 30 GLU H H 8.72 0.02 1 306 . 30 GLU CA C 57.6 0.2 1 307 . 30 GLU HA H 4.08 0.02 1 308 . 30 GLU CB C 29.7 0.2 1 309 . 30 GLU HB2 H 1.84 0.02 1 310 . 30 GLU HB3 H 1.84 0.02 1 311 . 30 GLU CG C 36.2 0.2 1 312 . 30 GLU HG2 H 2.21 0.02 1 313 . 30 GLU HG3 H 2.21 0.02 1 314 . 31 ASP N N 118.8 0.2 1 315 . 31 ASP H H 8.32 0.02 1 316 . 31 ASP CA C 54.1 0.2 1 317 . 31 ASP HA H 4.57 0.02 1 318 . 31 ASP CB C 40.6 0.2 1 319 . 31 ASP HB2 H 2.65 0.02 1 320 . 31 ASP HB3 H 2.65 0.02 1 321 . 32 TRP N N 119.8 0.2 1 322 . 32 TRP H H 7.66 0.02 1 323 . 32 TRP CA C 58.5 0.2 1 324 . 32 TRP HA H 4.35 0.02 1 325 . 32 TRP CB C 29.7 0.2 1 326 . 32 TRP HB2 H 3.18 0.02 1 327 . 32 TRP HB3 H 3.18 0.02 1 328 . 32 TRP CD1 C 126.9 0.2 1 329 . 32 TRP NE1 N 129.4 0.2 1 330 . 32 TRP HD1 H 7.32 0.02 1 331 . 32 TRP CZ2 C 114.4 0.2 1 332 . 32 TRP HE1 H 10.03 0.02 1 333 . 32 TRP CH2 C 124.1 0.2 1 334 . 32 TRP HZ2 H 7.39 0.02 1 335 . 32 TRP HH2 H 7.21 0.02 1 336 . 33 ASP N N 119.6 0.2 1 337 . 33 ASP H H 8.19 0.02 1 338 . 33 ASP CA C 54.3 0.2 1 339 . 33 ASP HA H 4.48 0.02 1 340 . 33 ASP CB C 40.5 0.2 1 341 . 33 ASP HB2 H 2.40 0.02 1 342 . 33 ASP HB3 H 2.40 0.02 1 343 . 34 LYS N N 122.8 0.2 1 344 . 34 LYS H H 7.79 0.02 1 345 . 34 LYS CA C 53.4 0.2 1 346 . 34 LYS HA H 4.53 0.02 1 347 . 34 LYS CB C 33.0 0.2 1 348 . 34 LYS HB2 H 1.64 0.02 2 349 . 34 LYS HB3 H 1.56 0.02 2 350 . 34 LYS CG C 24.4 0.2 1 351 . 34 LYS HG2 H 1.33 0.02 2 352 . 34 LYS HG3 H 1.28 0.02 2 353 . 34 LYS CD C 28.8 0.2 1 354 . 34 LYS HD2 H 1.63 0.02 2 355 . 34 LYS HD3 H 1.54 0.02 2 356 . 34 LYS CE C 42.3 0.2 1 357 . 34 LYS HE2 H 2.89 0.02 1 358 . 34 LYS HE3 H 2.89 0.02 1 359 . 35 PRO CD C 50.3 0.2 1 360 . 35 PRO CA C 62.7 0.2 1 361 . 35 PRO HA H 4.37 0.02 1 362 . 35 PRO CB C 31.9 0.2 1 363 . 35 PRO HB2 H 2.26 0.02 2 364 . 35 PRO HB3 H 1.94 0.02 2 365 . 35 PRO CG C 27.3 0.2 1 366 . 35 PRO HG2 H 1.94 0.02 1 367 . 35 PRO HG3 H 1.94 0.02 1 368 . 35 PRO HD2 H 3.71 0.02 2 369 . 35 PRO HD3 H 3.49 0.02 2 370 . 36 GLU N N 121.8 0.2 1 371 . 36 GLU H H 8.49 0.02 1 372 . 36 GLU CA C 58.1 0.2 1 373 . 36 GLU HA H 3.46 0.02 1 374 . 36 GLU CB C 29.8 0.2 1 375 . 36 GLU HB2 H 1.53 0.02 2 376 . 36 GLU HB3 H 1.45 0.02 2 377 . 36 GLU CG C 35.7 0.2 1 378 . 36 GLU HG2 H 1.63 0.02 2 379 . 36 GLU HG3 H 1.46 0.02 2 380 . 37 HIS N N 115.8 0.2 1 381 . 37 HIS H H 8.02 0.02 1 382 . 37 HIS CA C 54.2 0.2 1 383 . 37 HIS HA H 5.07 0.02 1 384 . 37 HIS CB C 31.3 0.2 1 385 . 37 HIS HB2 H 2.92 0.02 2 386 . 37 HIS HB3 H 2.85 0.02 2 387 . 37 HIS CD2 C 118.8 0.2 1 388 . 37 HIS HD2 H 6.83 0.02 1 389 . 38 ILE N N 117.8 0.2 1 390 . 38 ILE H H 8.57 0.02 1 391 . 38 ILE CA C 58.2 0.2 1 392 . 38 ILE HA H 4.66 0.02 1 393 . 38 ILE CB C 39.7 0.2 1 394 . 38 ILE HB H 1.87 0.02 1 395 . 38 ILE HG2 H 0.85 0.02 1 396 . 38 ILE CG2 C 17.9 0.2 1 397 . 38 ILE CG1 C 25.6 0.2 1 398 . 38 ILE HG12 H 1.41 0.02 2 399 . 38 ILE HG13 H 0.76 0.02 2 400 . 38 ILE HD1 H 0.83 0.02 1 401 . 38 ILE CD1 C 13.2 0.2 1 402 . 39 PRO CD C 50.5 0.2 1 403 . 39 PRO CA C 62.5 0.2 1 404 . 39 PRO HA H 4.34 0.02 1 405 . 39 PRO CB C 31.8 0.2 1 406 . 39 PRO HB2 H 2.08 0.02 2 407 . 39 PRO HB3 H 1.70 0.02 2 408 . 39 PRO CG C 27.6 0.2 1 409 . 39 PRO HG2 H 2.01 0.02 2 410 . 39 PRO HG3 H 1.88 0.02 2 411 . 39 PRO HD2 H 3.72 0.02 2 412 . 39 PRO HD3 H 3.58 0.02 2 413 . 40 ASP N N 123.2 0.2 1 414 . 40 ASP H H 8.55 0.02 1 415 . 40 ASP CA C 51.9 0.2 1 416 . 40 ASP HA H 4.53 0.02 1 417 . 40 ASP CB C 41.6 0.2 1 418 . 40 ASP HB2 H 2.76 0.02 2 419 . 40 ASP HB3 H 2.44 0.02 2 420 . 41 PRO CD C 51.0 0.2 1 421 . 41 PRO CA C 63.9 0.2 1 422 . 41 PRO HA H 4.37 0.02 1 423 . 41 PRO CB C 32.3 0.2 1 424 . 41 PRO HB2 H 2.26 0.02 2 425 . 41 PRO HB3 H 1.97 0.02 2 426 . 41 PRO CG C 26.6 0.2 1 427 . 41 PRO HG2 H 2.01 0.02 2 428 . 41 PRO HG3 H 1.93 0.02 2 429 . 41 PRO HD2 H 4.01 0.02 2 430 . 41 PRO HD3 H 3.92 0.02 2 431 . 42 ASP N N 118.2 0.2 1 432 . 42 ASP H H 8.34 0.02 1 433 . 42 ASP CA C 54.3 0.2 1 434 . 42 ASP HA H 4.69 0.02 1 435 . 42 ASP CB C 41.5 0.2 1 436 . 42 ASP HB2 H 2.74 0.02 2 437 . 42 ASP HB3 H 2.55 0.02 2 438 . 43 ALA N N 123.4 0.2 1 439 . 43 ALA H H 7.32 0.02 1 440 . 43 ALA CA C 52.7 0.2 1 441 . 43 ALA HA H 4.31 0.02 1 442 . 43 ALA HB H 1.54 0.02 1 443 . 43 ALA CB C 19.8 0.2 1 444 . 44 LYS N N 121.4 0.2 1 445 . 44 LYS H H 8.30 0.02 1 446 . 44 LYS CA C 54.4 0.2 1 447 . 44 LYS HA H 4.29 0.02 1 448 . 44 LYS CB C 34.4 0.2 1 449 . 44 LYS HB2 H 1.60 0.02 2 450 . 44 LYS HB3 H 1.53 0.02 2 451 . 44 LYS CG C 24.3 0.2 1 452 . 44 LYS HG2 H 1.30 0.02 1 453 . 44 LYS HG3 H 1.30 0.02 1 454 . 44 LYS CD C 28.9 0.2 1 455 . 44 LYS HD2 H 1.57 0.02 1 456 . 44 LYS HD3 H 1.57 0.02 1 457 . 44 LYS CE C 42.3 0.2 1 458 . 44 LYS HE2 H 2.91 0.02 1 459 . 44 LYS HE3 H 2.91 0.02 1 460 . 45 LYS N N 127.2 0.2 1 461 . 45 LYS H H 7.90 0.02 1 462 . 45 LYS HA H 4.27 0.02 1 463 . 45 LYS CB C 32.5 0.2 1 464 . 45 LYS HB2 H 1.07 0.02 2 465 . 45 LYS HB3 H 0.57 0.02 2 466 . 45 LYS CG C 23.1 0.2 1 467 . 45 LYS HG2 H 0.96 0.02 2 468 . 45 LYS HG3 H 0.21 0.02 2 469 . 45 LYS CD C 29.4 0.2 1 470 . 45 LYS HD2 H 1.41 0.02 2 471 . 45 LYS HD3 H 1.34 0.02 2 472 . 45 LYS CE C 41.6 0.2 1 473 . 45 LYS HE2 H 2.82 0.02 2 474 . 45 LYS HE3 H 2.75 0.02 2 475 . 46 PRO CD C 50.8 0.2 1 476 . 46 PRO CA C 63.2 0.2 1 477 . 46 PRO HA H 4.25 0.02 1 478 . 46 PRO CB C 32.7 0.2 1 479 . 46 PRO HB2 H 2.43 0.02 2 480 . 46 PRO HB3 H 2.01 0.02 2 481 . 46 PRO CG C 27.8 0.2 1 482 . 46 PRO HG2 H 2.21 0.02 2 483 . 46 PRO HG3 H 2.01 0.02 2 484 . 46 PRO HD2 H 3.28 0.02 2 485 . 46 PRO HD3 H 2.69 0.02 2 486 . 47 GLU N N 122.9 0.2 1 487 . 47 GLU H H 8.89 0.02 1 488 . 47 GLU CA C 58.5 0.2 1 489 . 47 GLU HA H 4.00 0.02 1 490 . 47 GLU CB C 29.5 0.2 1 491 . 47 GLU HB2 H 1.99 0.02 2 492 . 47 GLU HB3 H 1.94 0.02 2 493 . 47 GLU CG C 36.2 0.2 1 494 . 47 GLU HG2 H 2.29 0.02 1 495 . 47 GLU HG3 H 2.29 0.02 1 496 . 48 ASP N N 115.6 0.2 1 497 . 48 ASP H H 8.29 0.02 1 498 . 48 ASP CA C 52.9 0.2 1 499 . 48 ASP HA H 4.61 0.02 1 500 . 48 ASP CB C 40.0 0.2 1 501 . 48 ASP HB2 H 2.82 0.02 2 502 . 48 ASP HB3 H 2.59 0.02 2 503 . 49 TRP N N 122.0 0.2 1 504 . 49 TRP H H 7.49 0.02 1 505 . 49 TRP CA C 58.5 0.2 1 506 . 49 TRP HA H 4.13 0.02 1 507 . 49 TRP CB C 29.7 0.2 1 508 . 49 TRP HB2 H 3.16 0.02 2 509 . 49 TRP HB3 H 2.97 0.02 2 510 . 49 TRP CD1 C 125.9 0.2 1 511 . 49 TRP CE3 C 120.2 0.2 1 512 . 49 TRP NE1 N 129.8 0.2 1 513 . 49 TRP HD1 H 7.05 0.02 1 514 . 49 TRP HE3 H 7.55 0.02 1 515 . 49 TRP CZ3 C 121.8 0.2 1 516 . 49 TRP CZ2 C 115.1 0.2 1 517 . 49 TRP HE1 H 10.53 0.02 1 518 . 49 TRP HZ3 H 7.29 0.02 1 519 . 49 TRP CH2 C 124.3 0.2 1 520 . 49 TRP HZ2 H 7.26 0.02 1 521 . 49 TRP HH2 H 7.32 0.02 1 522 . 50 ASP N N 129.4 0.2 1 523 . 50 ASP H H 8.51 0.02 1 524 . 50 ASP CA C 52.7 0.2 1 525 . 50 ASP HA H 4.74 0.02 1 526 . 50 ASP CB C 41.8 0.2 1 527 . 50 ASP HB2 H 2.63 0.02 2 528 . 50 ASP HB3 H 2.33 0.02 2 529 . 51 GLU N N 125.2 0.2 1 530 . 51 GLU H H 8.94 0.02 1 531 . 51 GLU CA C 58.8 0.2 1 532 . 51 GLU HA H 4.28 0.02 1 533 . 51 GLU CB C 29.5 0.2 1 534 . 51 GLU HB2 H 2.08 0.02 2 535 . 51 GLU HB3 H 2.01 0.02 2 536 . 51 GLU CG C 36.9 0.2 1 537 . 51 GLU HG2 H 2.47 0.02 1 538 . 51 GLU HG3 H 2.47 0.02 1 539 . 52 GLU N N 118.8 0.2 1 540 . 52 GLU H H 8.17 0.02 1 541 . 52 GLU CA C 58.8 0.2 1 542 . 52 GLU HA H 4.04 0.02 1 543 . 52 GLU CB C 29.5 0.2 1 544 . 52 GLU HB2 H 2.02 0.02 1 545 . 52 GLU HB3 H 2.02 0.02 1 546 . 52 GLU CG C 36.2 0.2 1 547 . 52 GLU HG2 H 2.28 0.02 2 548 . 52 GLU HG3 H 2.22 0.02 2 549 . 53 MET N N 116.2 0.2 1 550 . 53 MET H H 7.50 0.02 1 551 . 53 MET CA C 55.9 0.2 1 552 . 53 MET HA H 4.41 0.02 1 553 . 53 MET CB C 33.4 0.2 1 554 . 53 MET HB2 H 1.84 0.02 2 555 . 53 MET HB3 H 1.72 0.02 2 556 . 53 MET CG C 31.9 0.2 1 557 . 53 MET HG2 H 2.44 0.02 2 558 . 53 MET HG3 H 2.35 0.02 2 559 . 53 MET HE H 1.98 0.02 1 560 . 53 MET CE C 16.8 0.2 1 561 . 54 ASP N N 117.6 0.2 1 562 . 54 ASP H H 8.46 0.02 1 563 . 54 ASP CA C 55.0 0.2 1 564 . 54 ASP HA H 4.57 0.02 1 565 . 54 ASP CB C 41.2 0.2 1 566 . 54 ASP HB2 H 1.96 0.02 2 567 . 54 ASP HB3 H 1.55 0.02 2 568 . 55 GLY N N 108.8 0.2 1 569 . 55 GLY H H 7.66 0.02 1 570 . 55 GLY CA C 44.5 0.2 1 571 . 55 GLY HA2 H 4.23 0.02 2 572 . 55 GLY HA3 H 3.92 0.02 2 573 . 56 GLU N N 119.9 0.2 1 574 . 56 GLU H H 8.50 0.02 1 575 . 56 GLU CA C 56.6 0.2 1 576 . 56 GLU HA H 4.41 0.02 1 577 . 56 GLU CB C 30.1 0.2 1 578 . 56 GLU HB2 H 2.00 0.02 2 579 . 56 GLU HB3 H 1.95 0.02 2 580 . 56 GLU CG C 36.0 0.2 1 581 . 56 GLU HG2 H 2.34 0.02 2 582 . 56 GLU HG3 H 2.27 0.02 2 583 . 57 TRP N N 128.0 0.2 1 584 . 57 TRP H H 9.01 0.02 1 585 . 57 TRP CA C 59.2 0.2 1 586 . 57 TRP HA H 3.91 0.02 1 587 . 57 TRP CB C 28.0 0.2 1 588 . 57 TRP HB2 H 2.66 0.02 2 589 . 57 TRP HB3 H 1.63 0.02 2 590 . 57 TRP CD1 C 126.3 0.2 1 591 . 57 TRP CE3 C 119.6 0.02 1 592 . 57 TRP NE1 N 130.0 0.2 1 593 . 57 TRP HD1 H 5.67 0.02 1 594 . 57 TRP HE3 H 6.99 0.02 1 595 . 57 TRP CZ3 C 121.2 0.2 1 596 . 57 TRP CZ2 C 113.2 0.2 1 597 . 57 TRP HE1 H 9.95 0.02 1 598 . 57 TRP HZ3 H 6.89 0.02 1 599 . 57 TRP CH2 C 123.3 0.2 1 600 . 57 TRP HZ2 H 7.11 0.02 1 601 . 57 TRP HH2 H 6.84 0.02 1 602 . 58 GLU N N 127.2 0.2 1 603 . 58 GLU H H 7.07 0.02 1 604 . 58 GLU CA C 52.4 0.2 1 605 . 58 GLU HA H 4.18 0.02 1 606 . 58 GLU CB C 31.1 0.2 1 607 . 58 GLU HB2 H 1.64 0.02 2 608 . 58 GLU HB3 H 1.49 0.02 2 609 . 58 GLU CG C 35.3 0.2 1 610 . 58 GLU HG2 H 1.95 0.02 1 611 . 58 GLU HG3 H 1.95 0.02 1 612 . 59 PRO CD C 50.1 0.2 1 613 . 59 PRO CA C 60.6 0.2 1 614 . 59 PRO HA H 3.70 0.02 1 615 . 59 PRO CB C 30.9 0.2 1 616 . 59 PRO HB2 H 2.14 0.02 2 617 . 59 PRO HB3 H 1.67 0.02 2 618 . 59 PRO CG C 26.9 0.2 1 619 . 59 PRO HG2 H 1.82 0.02 2 620 . 59 PRO HG3 H 1.81 0.02 2 621 . 59 PRO HD2 H 3.32 0.02 2 622 . 59 PRO HD3 H 3.08 0.02 2 623 . 60 PRO CD C 50.5 0.2 1 624 . 60 PRO CA C 62.5 0.2 1 625 . 60 PRO HA H 4.35 0.02 1 626 . 60 PRO CB C 32.3 0.2 1 627 . 60 PRO HB2 H 2.25 0.02 2 628 . 60 PRO HB3 H 1.88 0.02 2 629 . 60 PRO CG C 27.1 0.2 1 630 . 60 PRO HG2 H 2.03 0.02 1 631 . 60 PRO HG3 H 2.03 0.02 1 632 . 60 PRO HD2 H 3.64 0.02 2 633 . 60 PRO HD3 H 3.43 0.02 2 634 . 61 VAL N N 116.4 0.2 1 635 . 61 VAL H H 8.03 0.02 1 636 . 61 VAL CA C 61.1 0.2 1 637 . 61 VAL HA H 4.42 0.02 1 638 . 61 VAL CB C 33.4 0.2 1 639 . 61 VAL HB H 1.83 0.02 1 640 . 61 VAL HG1 H 0.67 0.02 2 641 . 61 VAL HG2 H 0.68 0.02 2 642 . 61 VAL CG1 C 19.5 0.2 1 643 . 61 VAL CG2 C 21.2 0.2 1 644 . 62 ILE N N 120.4 0.2 1 645 . 62 ILE H H 8.80 0.02 1 646 . 62 ILE CA C 59.9 0.2 1 647 . 62 ILE HA H 4.51 0.02 1 648 . 62 ILE CB C 41.1 0.2 1 649 . 62 ILE HB H 1.90 0.02 1 650 . 62 ILE HG2 H 0.85 0.02 1 651 . 62 ILE CG2 C 17.7 0.2 1 652 . 62 ILE CG1 C 26.3 0.2 1 653 . 62 ILE HG12 H 1.31 0.02 2 654 . 62 ILE HG13 H 0.93 0.02 2 655 . 62 ILE HD1 H 0.85 0.02 1 656 . 62 ILE CD1 C 13.4 0.2 1 657 . 63 GLN N N 121.8 0.2 1 658 . 63 GLN H H 8.53 0.02 1 659 . 63 GLN CA C 56.2 0.2 1 660 . 63 GLN HA H 4.18 0.02 1 661 . 63 GLN CB C 29.0 0.2 1 662 . 63 GLN HB2 H 1.92 0.02 1 663 . 63 GLN HB3 H 1.92 0.02 1 664 . 63 GLN CG C 33.9 0.2 1 665 . 63 GLN HG2 H 2.28 0.02 1 666 . 63 GLN HG3 H 2.28 0.02 1 667 . 63 GLN NE2 N 112.2 0.2 1 668 . 63 GLN HE21 H 7.52 0.02 2 669 . 63 GLN HE22 H 6.86 0.02 2 670 . 64 ASN N N 123.2 0.2 1 671 . 64 ASN H H 8.49 0.02 1 672 . 64 ASN CA C 50.5 0.2 1 673 . 64 ASN HA H 4.68 0.02 1 674 . 64 ASN CB C 39.6 0.2 1 675 . 64 ASN HB2 H 3.07 0.02 2 676 . 64 ASN HB3 H 2.48 0.02 2 677 . 64 ASN ND2 N 112.8 0.2 1 678 . 64 ASN HD21 H 8.18 0.02 2 679 . 64 ASN HD22 H 7.47 0.02 2 680 . 65 PRO CD C 51.3 0.2 1 681 . 65 PRO CA C 64.1 0.2 1 682 . 65 PRO HA H 4.39 0.02 1 683 . 65 PRO CB C 32.3 0.2 1 684 . 65 PRO HB2 H 2.32 0.02 2 685 . 65 PRO HB3 H 1.93 0.02 2 686 . 65 PRO CG C 27.3 0.2 1 687 . 65 PRO HG2 H 2.02 0.02 1 688 . 65 PRO HG3 H 2.02 0.02 1 689 . 65 PRO HD2 H 4.07 0.02 2 690 . 65 PRO HD3 H 3.92 0.02 2 691 . 66 GLU N N 115.0 0.2 1 692 . 66 GLU H H 7.69 0.02 1 693 . 66 GLU CA C 56.2 0.2 1 694 . 66 GLU HA H 4.16 0.02 1 695 . 66 GLU CB C 30.1 0.2 1 696 . 66 GLU HB2 H 2.04 0.02 2 697 . 66 GLU HB3 H 1.74 0.02 2 698 . 66 GLU CG C 36.6 0.2 1 699 . 66 GLU HG2 H 2.24 0.02 2 700 . 66 GLU HG3 H 2.11 0.02 2 701 . 67 TYR N N 120.4 0.2 1 702 . 67 TYR H H 7.69 0.02 1 703 . 67 TYR CA C 58.4 0.2 1 704 . 67 TYR HA H 4.28 0.02 1 705 . 67 TYR CB C 38.6 0.2 1 706 . 67 TYR HB2 H 3.00 0.02 1 707 . 67 TYR HB3 H 3.00 0.02 1 708 . 67 TYR HD1 H 7.06 0.02 1 709 . 67 TYR HD2 H 7.06 0.02 1 710 . 67 TYR HE1 H 6.80 0.02 1 711 . 67 TYR HE2 H 6.80 0.02 1 712 . 67 TYR CD1 C 133.1 0.2 1 713 . 67 TYR CE1 C 117.9 0.2 1 714 . 68 LYS N N 126.4 0.2 1 715 . 68 LYS H H 8.25 0.02 1 716 . 68 LYS CA C 55.7 0.2 1 717 . 68 LYS HA H 4.14 0.02 1 718 . 68 LYS CB C 33.0 0.2 1 719 . 68 LYS HB2 H 1.60 0.02 2 720 . 68 LYS HB3 H 1.21 0.02 2 721 . 68 LYS CG C 24.2 0.2 1 722 . 68 LYS HG2 H 1.16 0.02 2 723 . 68 LYS HG3 H 1.10 0.02 2 724 . 68 LYS CD C 28.4 0.2 1 725 . 68 LYS HD2 H 1.31 0.02 2 726 . 68 LYS HD3 H 1.28 0.02 2 727 . 68 LYS CE C 42.1 0.2 1 728 . 68 LYS HE2 H 2.76 0.02 1 729 . 68 LYS HE3 H 2.76 0.02 1 730 . 69 GLY N N 106.7 0.2 1 731 . 69 GLY H H 6.23 0.02 1 732 . 69 GLY CA C 44.8 0.2 1 733 . 69 GLY HA2 H 3.88 0.02 2 734 . 69 GLY HA3 H 3.68 0.02 2 735 . 70 GLU N N 120.7 0.2 1 736 . 70 GLU H H 8.40 0.02 1 737 . 70 GLU CA C 56.4 0.2 1 738 . 70 GLU HA H 4.33 0.02 1 739 . 70 GLU CB C 30.4 0.2 1 740 . 70 GLU HB2 H 1.96 0.02 2 741 . 70 GLU HB3 H 1.88 0.02 2 742 . 70 GLU CG C 36.0 0.2 1 743 . 70 GLU HG2 H 2.24 0.02 2 744 . 70 GLU HG3 H 2.18 0.02 2 745 . 71 TRP N N 125.2 0.2 1 746 . 71 TRP H H 8.57 0.02 1 747 . 71 TRP CA C 57.9 0.2 1 748 . 71 TRP HA H 4.29 0.02 1 749 . 71 TRP CB C 29.0 0.2 1 750 . 71 TRP HB2 H 3.03 0.02 2 751 . 71 TRP HB3 H 2.73 0.02 2 752 . 71 TRP CD1 C 126.5 0.2 1 753 . 71 TRP CE3 C 120.1 0.2 1 754 . 71 TRP NE1 N 129.4 0.2 1 755 . 71 TRP HD1 H 6.71 0.02 1 756 . 71 TRP HE3 H 7.14 0.02 1 757 . 71 TRP CZ3 C 121.2 0.2 1 758 . 71 TRP CZ2 C 114.0 0.2 1 759 . 71 TRP HE1 H 9.99 0.02 1 760 . 71 TRP HZ3 H 6.93 0.02 1 761 . 71 TRP CH2 C 123.9 0.2 1 762 . 71 TRP HZ2 H 7.32 0.02 1 763 . 71 TRP HH2 H 7.08 0.02 1 764 . 72 LYS N N 125.8 0.2 1 765 . 72 LYS H H 7.46 0.02 1 766 . 72 LYS CA C 53.4 0.2 1 767 . 72 LYS HA H 4.26 0.02 1 768 . 72 LYS CB C 33.1 0.2 1 769 . 72 LYS HB2 H 1.55 0.02 2 770 . 72 LYS HB3 H 1.39 0.02 2 771 . 72 LYS CG C 24.1 0.2 1 772 . 72 LYS HG2 H 1.18 0.02 1 773 . 72 LYS HG3 H 1.18 0.02 1 774 . 72 LYS CE C 42.0 0.2 1 775 . 72 LYS HE2 H 2.87 0.02 1 776 . 72 LYS HE3 H 2.87 0.02 1 777 . 73 PRO CD C 50.3 0.2 1 778 . 73 PRO CA C 63.0 0.2 1 779 . 73 PRO HA H 4.02 0.02 1 780 . 73 PRO CB C 32.0 0.2 1 781 . 73 PRO HB2 H 2.17 0.02 2 782 . 73 PRO HB3 H 1.85 0.02 2 783 . 73 PRO CG C 27.1 0.2 1 784 . 73 PRO HG2 H 1.86 0.02 1 785 . 73 PRO HG3 H 1.86 0.02 1 786 . 73 PRO HD2 H 3.37 0.02 2 787 . 73 PRO HD3 H 3.22 0.02 2 788 . 74 ARG N N 126.0 0.2 1 789 . 74 ARG H H 7.85 0.02 1 790 . 74 ARG CA C 57.3 0.2 1 791 . 74 ARG HA H 4.03 0.02 1 792 . 74 ARG CB C 31.3 0.2 1 793 . 74 ARG HB2 H 1.76 0.02 2 794 . 74 ARG HB3 H 1.65 0.02 2 795 . 74 ARG CG C 27.1 0.2 1 796 . 74 ARG HG2 H 1.54 0.02 1 797 . 74 ARG HG3 H 1.54 0.02 1 798 . 74 ARG CD C 43.5 0.2 1 799 . 74 ARG HD2 H 3.12 0.02 1 800 . 74 ARG HD3 H 3.12 0.02 1 801 . 74 ARG NE N 85.1 0.2 1 802 . 74 ARG HE H 7.04 0.02 1 stop_ save_