data_4878 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-dimensional Structure Topology of the Calreticulin P-domain based on NMR Assignment ; _BMRB_accession_number 4878 _BMRB_flat_file_name bmr4878.str _Entry_type original _Submission_date 2000-10-24 _Accession_date 2000-10-24 _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 Riek Roland . . 3 Braun Daniel . . 4 Herrmann Torsten . . 5 Helenius Ari . . 6 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 615 "13C chemical shifts" 328 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-12 original author . stop_ _Original_release_date 2001-03-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Three-dimensional Structure Topology of the Calreticulin P-domain based on NMR Assignment ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11163798 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ellgaard Lars . . 2 Riek Roland . . 3 Braun Daniel . . 4 Herrmann Torsten . . 5 Helenius Ari . . 6 Wuthrich Kurt . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 488 _Journal_issue 1-2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 69 _Page_last 73 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_CRT _Saveframe_category molecular_system _Mol_system_name 'Calreticulin P-domain' _Abbreviation_common CRT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CRT $CRT 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Calreticulin _Abbreviation_common CRT _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; KKIKDPDAAKPEDWDERAKI DDPTDSKPEDWDKPEHIPDP DAKKPEDWDEEMDGEWEPPV IQNPEYKGEWKPRQIDNPDY KGTWIHPEIDNPEYSPDANI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 189 LYS 2 190 LYS 3 191 ILE 4 192 LYS 5 193 ASP 6 194 PRO 7 195 ASP 8 196 ALA 9 197 ALA 10 198 LYS 11 199 PRO 12 200 GLU 13 201 ASP 14 202 TRP 15 203 ASP 16 204 GLU 17 205 ARG 18 206 ALA 19 207 LYS 20 208 ILE 21 209 ASP 22 210 ASP 23 211 PRO 24 212 THR 25 213 ASP 26 214 SER 27 215 LYS 28 216 PRO 29 217 GLU 30 218 ASP 31 219 TRP 32 220 ASP 33 221 LYS 34 222 PRO 35 223 GLU 36 224 HIS 37 225 ILE 38 226 PRO 39 227 ASP 40 228 PRO 41 229 ASP 42 230 ALA 43 231 LYS 44 232 LYS 45 233 PRO 46 234 GLU 47 235 ASP 48 236 TRP 49 237 ASP 50 238 GLU 51 239 GLU 52 240 MET 53 241 ASP 54 242 GLY 55 243 GLU 56 244 TRP 57 245 GLU 58 246 PRO 59 247 PRO 60 248 VAL 61 249 ILE 62 250 GLN 63 251 ASN 64 252 PRO 65 253 GLU 66 254 TYR 67 255 LYS 68 256 GLY 69 257 GLU 70 258 TRP 71 259 LYS 72 260 PRO 73 261 ARG 74 262 GLN 75 263 ILE 76 264 ASP 77 265 ASN 78 266 PRO 79 267 ASP 80 268 TYR 81 269 LYS 82 270 GLY 83 271 THR 84 272 TRP 85 273 ILE 86 274 HIS 87 275 PRO 88 276 GLU 89 277 ILE 90 278 ASP 91 279 ASN 92 280 PRO 93 281 GLU 94 282 TYR 95 283 SER 96 284 PRO 97 285 ASP 98 286 ALA 99 287 ASN 100 288 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 83.00 100 98.80 100.00 9.00e-46 BMRB 5204 CRT(189-261) 73.00 74 100.00 100.00 1.72e-38 PDB 1HHN "Calreticulin P-Domain" 100.00 101 100.00 100.00 7.18e-59 PDB 1K9C "Solution Structure Of Calreticulin P-Domain Subdomain (Residues 189-261)" 73.00 74 100.00 100.00 2.84e-38 DBJ BAA11345 "calreticulin [Rattus norvegicus]" 100.00 416 100.00 100.00 4.68e-60 DBJ BAC35852 "unnamed protein product [Mus musculus]" 100.00 416 100.00 100.00 7.18e-60 DBJ BAD96780 "calreticulin precursor variant [Homo sapiens]" 100.00 406 97.00 99.00 1.51e-57 DBJ BAE01267 "unnamed protein product [Macaca fascicularis]" 100.00 417 97.00 99.00 1.33e-57 DBJ BAE22866 "unnamed protein product [Mus musculus]" 100.00 368 100.00 100.00 1.54e-60 EMBL CAA33053 "calreticulin precursor protein [Mus musculus]" 100.00 416 100.00 100.00 7.18e-60 EMBL CAA37446 "precursor (AA -17 to 399) [Rattus norvegicus]" 100.00 416 100.00 100.00 4.68e-60 EMBL CAA55890 "calreticulin [Rattus norvegicus]" 100.00 416 100.00 100.00 4.68e-60 EMBL CAG33351 "CALR [Homo sapiens]" 100.00 417 97.00 99.00 1.32e-57 GB AAA31188 "calreticulin precursor [Oryctolagus cuniculus]" 100.00 418 99.00 100.00 1.73e-59 GB AAA36582 "Ro ribonucleoprotein autoantigen (Ro/SS-A) precursor [Homo sapiens]" 100.00 417 97.00 99.00 1.32e-57 GB AAA37569 "calregulin [Mus musculus]" 100.00 416 100.00 100.00 7.18e-60 GB AAA51916 "calreticulin [Homo sapiens]" 100.00 417 97.00 99.00 1.32e-57 GB AAB20096 "calreticulin [rabbits, sketetal muscle, Peptide, 401 aa]" 100.00 401 99.00 100.00 1.51e-59 REF NP_001075704 "calreticulin precursor [Oryctolagus cuniculus]" 100.00 418 99.00 100.00 1.73e-59 REF NP_001167604 "calreticulin precursor [Sus scrofa]" 100.00 417 98.00 99.00 6.67e-59 REF NP_001231051 "calreticulin precursor [Cricetulus griseus]" 100.00 417 100.00 100.00 5.87e-60 REF NP_001248060 "calreticulin precursor [Macaca mulatta]" 100.00 417 97.00 99.00 1.33e-57 REF NP_001274539 "calreticulin precursor [Macaca fascicularis]" 100.00 417 97.00 99.00 1.33e-57 SP P14211 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 100.00 416 100.00 100.00 7.18e-60 SP P15253 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 100.00 418 99.00 100.00 1.73e-59 SP P18418 "RecName: Full=Calreticulin; AltName: Full=CALBP; AltName: Full=CRP55; AltName: Full=Calcium-binding protein 3; Short=CABP3; Alt" 100.00 416 100.00 100.00 4.68e-60 SP P27797 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 100.00 417 97.00 99.00 1.32e-57 SP P28491 "RecName: Full=Calreticulin; AltName: Full=CRP55; AltName: Full=Calregulin; AltName: Full=Endoplasmic reticulum resident protein" 100.00 417 98.00 99.00 6.67e-59 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 'Norway 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 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_CRT100 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CRT . mM 1.5 3 '{U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_15N_resolved_1H,1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N resolved 1H,1H NOESY' _Sample_label . save_ save_13C_resolved_1H,1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '13C resolved 1H,1H NOESY' _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N resolved 1H,1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '13C resolved 1H,1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.2 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 external direct external . . 1.0 DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 external 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_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $CRT100 stop_ _Sample_conditions_label $Cond1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name CRT _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 LYS N N 123.2 . 1 2 . 1 LYS H H 8.49 . 1 3 . 1 LYS CA C 56.8 . 1 4 . 1 LYS HA H 4.15 . 1 5 . 1 LYS CB C 33.0 . 1 6 . 1 LYS HB2 H 1.75 . 2 7 . 1 LYS HB3 H 1.66 . 2 8 . 1 LYS CG C 24.8 . 1 9 . 1 LYS HG2 H 1.34 . 2 10 . 1 LYS HG3 H 1.25 . 2 11 . 1 LYS CD C 29.0 . 1 12 . 1 LYS HD2 H 1.59 . 1 13 . 1 LYS HD3 H 1.59 . 1 14 . 1 LYS HE2 H 2.91 . 1 15 . 1 LYS HE3 H 2.91 . 1 16 . 2 LYS N N 121.8 . 1 17 . 2 LYS H H 8.31 . 1 18 . 2 LYS CA C 55.6 . 1 19 . 2 LYS HA H 4.48 . 1 20 . 2 LYS CB C 33.5 . 1 21 . 2 LYS HB2 H 1.67 . 1 22 . 2 LYS HB3 H 1.67 . 1 23 . 2 LYS CG C 24.8 . 1 24 . 2 LYS HG2 H 1.38 . 2 25 . 2 LYS HG3 H 1.30 . 2 26 . 2 LYS CE C 41.9 . 1 27 . 2 LYS HE2 H 2.90 . 1 28 . 2 LYS HE3 H 2.90 . 1 29 . 3 ILE N N 120.4 . 1 30 . 3 ILE H H 8.37 . 1 31 . 3 ILE CA C 60.3 . 1 32 . 3 ILE HA H 4.26 . 1 33 . 3 ILE CB C 39.8 . 1 34 . 3 ILE HB H 1.82 . 1 35 . 3 ILE HG2 H 0.84 . 1 36 . 3 ILE CG2 C 17.5 . 1 37 . 3 ILE CG1 C 26.7 . 1 38 . 3 ILE HG12 H 1.38 . 2 39 . 3 ILE HG13 H 1.01 . 2 40 . 3 ILE HD1 H 0.82 . 1 41 . 3 ILE CD1 C 13.0 . 1 42 . 4 LYS N N 124.2 . 1 43 . 4 LYS H H 8.37 . 1 44 . 4 LYS CA C 56.2 . 1 45 . 4 LYS HA H 4.15 . 1 46 . 4 LYS CB C 32.6 . 1 47 . 4 LYS HB2 H 1.58 . 1 48 . 4 LYS HB3 H 1.58 . 1 49 . 4 LYS CG C 24.8 . 1 50 . 4 LYS HG2 H 1.33 . 2 51 . 4 LYS HG3 H 1.23 . 2 52 . 4 LYS CD C 28.9 . 1 53 . 4 LYS HD2 H 1.49 . 1 54 . 4 LYS HD3 H 1.49 . 1 55 . 4 LYS CE C 41.9 . 1 56 . 4 LYS HE2 H 2.88 . 1 57 . 4 LYS HE3 H 2.88 . 1 58 . 5 ASP N N 123.0 . 1 59 . 5 ASP H H 8.46 . 1 60 . 5 ASP CA C 52.1 . 1 61 . 5 ASP HA H 4.69 . 1 62 . 5 ASP CB C 41.4 . 1 63 . 5 ASP HB2 H 2.77 . 2 64 . 5 ASP HB3 H 2.47 . 2 65 . 6 PRO CD C 50.9 . 1 66 . 6 PRO CA C 63.8 . 1 67 . 6 PRO HA H 4.38 . 1 68 . 6 PRO CB C 32.0 . 1 69 . 6 PRO HB2 H 2.27 . 2 70 . 6 PRO HB3 H 1.92 . 2 71 . 6 PRO CG C 27.1 . 1 72 . 6 PRO HG2 H 1.97 . 1 73 . 6 PRO HG3 H 1.97 . 1 74 . 6 PRO HD2 H 3.90 . 2 75 . 6 PRO HD3 H 3.85 . 2 76 . 7 ASP N N 118.5 . 1 77 . 7 ASP H H 8.35 . 1 78 . 7 ASP CA C 54.2 . 1 79 . 7 ASP HA H 4.63 . 1 80 . 7 ASP CB C 41.4 . 1 81 . 7 ASP HB2 H 2.73 . 2 82 . 7 ASP HB3 H 2.55 . 2 83 . 8 ALA N N 123.4 . 1 84 . 8 ALA H H 7.68 . 1 85 . 8 ALA CA C 52.3 . 1 86 . 8 ALA HA H 4.29 . 1 87 . 8 ALA HB H 1.36 . 1 88 . 8 ALA CB C 19.7 . 1 89 . 9 ALA N N 122.4 . 1 90 . 9 ALA H H 8.03 . 1 91 . 9 ALA CA C 51.5 . 1 92 . 9 ALA HA H 4.18 . 1 93 . 9 ALA HB H 1.24 . 1 94 . 9 ALA CB C 20.1 . 1 95 . 10 LYS N N 123.0 . 1 96 . 10 LYS H H 7.88 . 1 97 . 10 LYS CB C 32.0 . 1 98 . 10 LYS HB2 H 1.29 . 2 99 . 10 LYS HB3 H 0.95 . 2 100 . 10 LYS CG C 23.2 . 1 101 . 10 LYS HG2 H 1.13 . 2 102 . 10 LYS HG3 H 0.64 . 2 103 . 10 LYS CD C 28.9 . 1 104 . 10 LYS HD2 H 1.47 . 2 105 . 10 LYS HD3 H 1.40 . 2 106 . 10 LYS CE C 41.5 . 1 107 . 10 LYS HE2 H 2.88 . 2 108 . 10 LYS HE3 H 2.81 . 2 109 . 11 PRO CD C 50.5 . 1 110 . 11 PRO CA C 63.0 . 1 111 . 11 PRO HA H 4.26 . 1 112 . 11 PRO CB C 32.4 . 1 113 . 11 PRO HB2 H 2.34 . 2 114 . 11 PRO HB3 H 1.95 . 2 115 . 11 PRO HD2 H 3.34 . 2 116 . 11 PRO HD3 H 2.91 . 2 117 . 12 GLU N N 122.0 . 1 118 . 12 GLU H H 8.84 . 1 119 . 12 GLU CA C 58.0 . 1 120 . 12 GLU HA H 4.03 . 1 121 . 12 GLU CB C 29.4 . 1 122 . 12 GLU HB2 H 1.94 . 1 123 . 12 GLU HB3 H 1.94 . 1 124 . 12 GLU CG C 36.1 . 1 125 . 12 GLU HG2 H 2.26 . 1 126 . 12 GLU HG3 H 2.26 . 1 127 . 13 ASP N N 116.7 . 1 128 . 13 ASP H H 8.26 . 1 129 . 13 ASP CA C 53.3 . 1 130 . 13 ASP HA H 4.57 . 1 131 . 13 ASP CB C 40.0 . 1 132 . 13 ASP HB2 H 2.79 . 2 133 . 13 ASP HB3 H 2.59 . 2 134 . 14 TRP N N 121.8 . 1 135 . 14 TRP H H 7.65 . 1 136 . 14 TRP CA C 58.0 . 1 137 . 14 TRP HA H 4.28 . 1 138 . 14 TRP CB C 28.9 . 1 139 . 14 TRP HB2 H 3.13 . 1 140 . 14 TRP HB3 H 3.13 . 1 141 . 14 TRP CD1 C 126.4 . 1 142 . 14 TRP CE3 C 120.6 . 1 143 . 14 TRP NE1 N 129.6 . 1 144 . 14 TRP HD1 H 7.07 . 1 145 . 14 TRP HE3 H 7.58 . 1 146 . 14 TRP CZ3 C 122.3 . 1 147 . 14 TRP CZ2 C 115.1 . 1 148 . 14 TRP HE1 H 10.11 . 1 149 . 14 TRP HZ3 H 7.21 . 1 150 . 14 TRP CH2 C 125.0 . 1 151 . 14 TRP HZ2 H 7.29 . 1 152 . 14 TRP HH2 H 7.21 . 1 153 . 15 ASP N N 125.8 . 1 154 . 15 ASP H H 7.90 . 1 155 . 15 ASP CA C 53.9 . 1 156 . 15 ASP HA H 4.56 . 1 157 . 15 ASP CB C 41.0 . 1 158 . 15 ASP HB2 H 2.77 . 2 159 . 15 ASP HB3 H 2.44 . 2 160 . 16 GLU N N 123.2 . 1 161 . 16 GLU H H 8.68 . 1 162 . 16 GLU CA C 56.0 . 1 163 . 16 GLU HA H 4.51 . 1 164 . 16 GLU CB C 30.4 . 1 165 . 16 GLU HB2 H 2.36 . 2 166 . 16 GLU HB3 H 2.06 . 2 167 . 16 GLU CG C 37.3 . 1 168 . 16 GLU HG2 H 2.46 . 1 169 . 16 GLU HG3 H 2.46 . 1 170 . 17 ARG CA C 55.2 . 1 171 . 17 ARG HA H 4.32 . 1 172 . 17 ARG HB2 H 1.84 . 2 173 . 17 ARG HB3 H 1.66 . 2 174 . 17 ARG HG2 H 1.74 . 1 175 . 17 ARG HG3 H 1.74 . 1 176 . 17 ARG CD C 43.5 . 1 177 . 17 ARG HD2 H 3.24 . 2 178 . 17 ARG HD3 H 3.10 . 2 179 . 17 ARG NE N 84.2 . 1 180 . 17 ARG HE H 7.83 . 1 181 . 18 ALA N N 127.2 . 1 182 . 18 ALA H H 8.32 . 1 183 . 18 ALA HA H 2.95 . 1 184 . 18 ALA HB H 0.93 . 1 185 . 18 ALA CB C 18.3 . 1 186 . 19 LYS N N 115.9 . 1 187 . 19 LYS H H 7.76 . 1 188 . 19 LYS CA C 53.4 . 1 189 . 19 LYS HA H 4.97 . 1 190 . 19 LYS CB C 35.9 . 1 191 . 19 LYS HB2 H 1.60 . 2 192 . 19 LYS HB3 H 1.45 . 2 193 . 19 LYS CG C 24.8 . 1 194 . 19 LYS HG2 H 1.25 . 2 195 . 19 LYS HG3 H 1.12 . 2 196 . 19 LYS CD C 29.0 . 1 197 . 19 LYS HD2 H 1.43 . 2 198 . 19 LYS HD3 H 1.26 . 2 199 . 19 LYS CE C 42.1 . 1 200 . 19 LYS HE2 H 2.75 . 1 201 . 19 LYS HE3 H 2.75 . 1 202 . 20 ILE N N 113.1 . 1 203 . 20 ILE H H 8.59 . 1 204 . 20 ILE CA C 58.9 . 1 205 . 20 ILE HA H 4.53 . 1 206 . 20 ILE CB C 42.7 . 1 207 . 20 ILE HB H 1.91 . 1 208 . 20 ILE HG2 H 0.69 . 1 209 . 20 ILE CG2 C 17.9 . 1 210 . 20 ILE CG1 C 25.7 . 1 211 . 20 ILE HG12 H 1.25 . 1 212 . 20 ILE HG13 H 1.25 . 1 213 . 20 ILE HD1 H 0.83 . 1 214 . 20 ILE CD1 C 13.6 . 1 215 . 21 ASP N N 120.6 . 1 216 . 21 ASP H H 8.31 . 1 217 . 21 ASP CA C 54.4 . 1 218 . 21 ASP HA H 4.36 . 1 219 . 21 ASP CB C 40.6 . 1 220 . 21 ASP HB2 H 2.43 . 2 221 . 21 ASP HB3 H 2.27 . 2 222 . 22 ASP N N 121.6 . 1 223 . 22 ASP H H 8.71 . 1 224 . 22 ASP CA C 50.9 . 1 225 . 22 ASP HA H 4.52 . 1 226 . 22 ASP CB C 40.8 . 1 227 . 22 ASP HB2 H 2.42 . 1 228 . 22 ASP HB3 H 2.42 . 1 229 . 23 PRO CD C 51.1 . 1 230 . 23 PRO CA C 64.0 . 1 231 . 23 PRO HA H 4.52 . 1 232 . 23 PRO CB C 32.2 . 1 233 . 23 PRO HB2 H 2.34 . 2 234 . 23 PRO HB3 H 2.06 . 2 235 . 23 PRO CG C 26.7 . 1 236 . 23 PRO HG2 H 1.97 . 1 237 . 23 PRO HG3 H 1.97 . 1 238 . 23 PRO HD2 H 4.25 . 2 239 . 23 PRO HD3 H 4.01 . 2 240 . 24 THR N N 108.8 . 1 241 . 24 THR H H 8.43 . 1 242 . 24 THR CA C 61.9 . 1 243 . 24 THR HA H 4.37 . 1 244 . 24 THR CB C 69.7 . 1 245 . 24 THR HB H 4.34 . 1 246 . 24 THR HG2 H 1.20 . 1 247 . 24 THR CG2 C 21.8 . 1 248 . 25 ASP N N 123.4 . 1 249 . 25 ASP H H 7.42 . 1 250 . 25 ASP CA C 53.6 . 1 251 . 25 ASP HA H 4.87 . 1 252 . 25 ASP CB C 42.4 . 1 253 . 25 ASP HB2 H 2.93 . 2 254 . 25 ASP HB3 H 2.45 . 2 255 . 26 SER N N 117.3 . 1 256 . 26 SER H H 8.29 . 1 257 . 26 SER CA C 57.4 . 1 258 . 26 SER HA H 4.33 . 1 259 . 26 SER CB C 65.0 . 1 260 . 26 SER HB2 H 3.63 . 2 261 . 26 SER HB3 H 3.51 . 2 262 . 27 LYS N N 127.0 . 1 263 . 27 LYS H H 7.67 . 1 264 . 27 LYS CB C 32.6 . 1 265 . 27 LYS HB2 H 0.95 . 2 266 . 27 LYS HB3 H 0.12 . 2 267 . 28 PRO CA C 62.8 . 1 268 . 28 PRO HA H 4.31 . 1 269 . 28 PRO CB C 32.8 . 1 270 . 28 PRO HB2 H 2.48 . 2 271 . 28 PRO HB3 H 2.03 . 2 272 . 29 GLU N N 122.2 . 1 273 . 29 GLU H H 8.91 . 1 274 . 29 GLU CA C 58.3 . 1 275 . 29 GLU HA H 4.01 . 1 276 . 29 GLU CB C 29.6 . 1 277 . 29 GLU HB2 H 2.01 . 2 278 . 29 GLU HB3 H 1.96 . 2 279 . 29 GLU CG C 35.9 . 1 280 . 29 GLU HG2 H 2.29 . 1 281 . 29 GLU HG3 H 2.29 . 1 282 . 30 ASP N N 116.5 . 1 283 . 30 ASP H H 8.38 . 1 284 . 30 ASP CA C 52.9 . 1 285 . 30 ASP HA H 4.70 . 1 286 . 30 ASP CB C 40.0 . 1 287 . 30 ASP HB2 H 2.81 . 2 288 . 30 ASP HB3 H 2.56 . 2 289 . 31 TRP N N 118.9 . 1 290 . 31 TRP H H 7.42 . 1 291 . 31 TRP CA C 60.7 . 1 292 . 31 TRP HA H 3.93 . 1 293 . 31 TRP CB C 30.4 . 1 294 . 31 TRP HB2 H 3.20 . 2 295 . 31 TRP HB3 H 2.89 . 2 296 . 31 TRP CD1 C 127.5 . 1 297 . 31 TRP CE3 C 120.6 . 1 298 . 31 TRP NE1 N 129.4 . 1 299 . 31 TRP HD1 H 7.52 . 1 300 . 31 TRP HE3 H 7.56 . 1 301 . 31 TRP CZ2 C 115.4 . 1 302 . 31 TRP HE1 H 9.92 . 1 303 . 31 TRP CH2 C 124.7 . 1 304 . 31 TRP HZ2 H 7.25 . 1 305 . 31 TRP HH2 H 7.26 . 1 306 . 31 TRP CZ3 C 122.3 . 1 307 . 31 TRP HZ3 H 7.29 . 1 308 . 32 ASP N N 116.5 . 1 309 . 32 ASP H H 8.58 . 1 310 . 32 ASP CA C 55.8 . 1 311 . 32 ASP HA H 4.50 . 1 312 . 32 ASP CB C 40.4 . 1 313 . 32 ASP HB2 H 2.62 . 1 314 . 32 ASP HB3 H 2.62 . 1 315 . 33 LYS N N 124.0 . 1 316 . 33 LYS H H 7.92 . 1 317 . 33 LYS CA C 52.1 . 1 318 . 33 LYS HA H 4.71 . 1 319 . 33 LYS CG C 24.2 . 1 320 . 33 LYS HG2 H 1.28 . 1 321 . 33 LYS HG3 H 1.28 . 1 322 . 33 LYS CD C 28.1 . 1 323 . 33 LYS HD2 H 1.70 . 2 324 . 33 LYS HD3 H 1.51 . 2 325 . 33 LYS CE C 42.5 . 1 326 . 33 LYS HE2 H 2.89 . 1 327 . 33 LYS HE3 H 2.89 . 1 328 . 34 PRO CD C 49.9 . 1 329 . 34 PRO CA C 62.6 . 1 330 . 34 PRO HA H 4.35 . 1 331 . 34 PRO CB C 31.8 . 1 332 . 34 PRO HB2 H 2.35 . 2 333 . 34 PRO HB3 H 1.95 . 2 334 . 34 PRO CG C 27.7 . 1 335 . 34 PRO HG2 H 2.02 . 2 336 . 34 PRO HG3 H 1.95 . 2 337 . 34 PRO HD2 H 3.72 . 2 338 . 34 PRO HD3 H 3.42 . 2 339 . 35 GLU N N 122.8 . 1 340 . 35 GLU H H 8.53 . 1 341 . 35 GLU CA C 58.9 . 1 342 . 35 GLU HA H 3.02 . 1 343 . 35 GLU CB C 29.8 . 1 344 . 35 GLU HB2 H 1.28 . 2 345 . 35 GLU HB3 H 1.19 . 2 346 . 35 GLU CG C 35.3 . 1 347 . 35 GLU HG2 H 1.14 . 2 348 . 35 GLU HG3 H 1.01 . 2 349 . 36 HIS N N 113.3 . 1 350 . 36 HIS H H 7.83 . 1 351 . 36 HIS CA C 54.4 . 1 352 . 36 HIS HA H 5.32 . 1 353 . 36 HIS CB C 32.0 . 1 354 . 36 HIS HB2 H 2.83 . 2 355 . 36 HIS HB3 H 2.72 . 2 356 . 36 HIS CD2 C 119.2 . 1 357 . 36 HIS CE1 C 136.9 . 1 358 . 36 HIS HD2 H 6.69 . 1 359 . 36 HIS HE1 H 7.95 . 1 360 . 37 ILE N N 114.5 . 1 361 . 37 ILE H H 8.73 . 1 362 . 37 ILE CA C 58.1 . 1 363 . 37 ILE HA H 4.80 . 1 364 . 37 ILE CB C 40.2 . 1 365 . 37 ILE HB H 1.92 . 1 366 . 37 ILE HG2 H 0.82 . 1 367 . 37 ILE CG2 C 18.5 . 1 368 . 37 ILE CG1 C 25.7 . 1 369 . 37 ILE HG12 H 1.40 . 1 370 . 37 ILE HG13 H 1.40 . 1 371 . 37 ILE HD1 H 0.84 . 1 372 . 37 ILE CD1 C 13.6 . 1 373 . 38 PRO CD C 49.9 . 1 374 . 38 PRO CA C 62.3 . 1 375 . 38 PRO HA H 4.36 . 1 376 . 38 PRO CB C 31.6 . 1 377 . 38 PRO HB2 H 2.02 . 2 378 . 38 PRO HB3 H 1.64 . 2 379 . 38 PRO CG C 27.7 . 1 380 . 38 PRO HG2 H 2.03 . 2 381 . 38 PRO HG3 H 1.87 . 2 382 . 38 PRO HD2 H 3.71 . 2 383 . 38 PRO HD3 H 3.57 . 2 384 . 39 ASP N N 123.2 . 1 385 . 39 ASP H H 8.62 . 1 386 . 39 ASP CA C 51.7 . 1 387 . 39 ASP HA H 4.41 . 1 388 . 39 ASP CB C 42.1 . 1 389 . 39 ASP HB2 H 2.77 . 2 390 . 39 ASP HB3 H 2.41 . 2 391 . 40 PRO CD C 50.9 . 1 392 . 40 PRO CA C 63.8 . 1 393 . 40 PRO HA H 4.38 . 1 394 . 40 PRO CB C 32.2 . 1 395 . 40 PRO HB2 H 2.27 . 2 396 . 40 PRO HB3 H 2.00 . 2 397 . 40 PRO CG C 26.5 . 1 398 . 40 PRO HG2 H 2.02 . 2 399 . 40 PRO HG3 H 1.92 . 2 400 . 40 PRO HD2 H 4.09 . 2 401 . 40 PRO HD3 H 3.98 . 2 402 . 41 ASP N N 117.5 . 1 403 . 41 ASP H H 8.34 . 1 404 . 41 ASP CA C 54.0 . 1 405 . 41 ASP HA H 4.73 . 1 406 . 41 ASP CB C 41.7 . 1 407 . 41 ASP HB2 H 2.75 . 2 408 . 41 ASP HB3 H 2.55 . 2 409 . 42 ALA N N 123.0 . 1 410 . 42 ALA H H 7.08 . 1 411 . 42 ALA CA C 52.3 . 1 412 . 42 ALA HA H 4.33 . 1 413 . 42 ALA HB H 1.59 . 1 414 . 42 ALA CB C 20.1 . 1 415 . 43 LYS N N 121.6 . 1 416 . 43 LYS H H 8.40 . 1 417 . 43 LYS CA C 54.0 . 1 418 . 43 LYS HA H 4.31 . 1 419 . 43 LYS CB C 34.9 . 1 420 . 43 LYS HB2 H 1.54 . 2 421 . 43 LYS HB3 H 1.48 . 2 422 . 43 LYS CG C 24.2 . 1 423 . 43 LYS HG2 H 1.28 . 1 424 . 43 LYS HG3 H 1.28 . 1 425 . 43 LYS CD C 28.7 . 1 426 . 43 LYS HD2 H 1.57 . 1 427 . 43 LYS HD3 H 1.57 . 1 428 . 43 LYS CE C 42.1 . 1 429 . 43 LYS HE2 H 2.92 . 1 430 . 43 LYS HE3 H 2.92 . 1 431 . 44 LYS N N 127.4 . 1 432 . 44 LYS H H 7.84 . 1 433 . 44 LYS CA C 53.5 . 1 434 . 44 LYS HA H 1.89 . 1 435 . 44 LYS CB C 32.4 . 1 436 . 44 LYS HB2 H 0.94 . 2 437 . 44 LYS HB3 H 0.34 . 2 438 . 44 LYS CG C 22.6 . 1 439 . 44 LYS HG2 H 0.89 . 2 440 . 44 LYS HG3 H -0.02 . 2 441 . 44 LYS CD C 29.6 . 1 442 . 44 LYS HD2 H 1.41 . 2 443 . 44 LYS HD3 H 1.30 . 2 444 . 44 LYS CE C 41.4 . 1 445 . 44 LYS HE2 H 2.81 . 2 446 . 44 LYS HE3 H 2.73 . 2 447 . 45 PRO CD C 50.7 . 1 448 . 45 PRO CA C 63.0 . 1 449 . 45 PRO HA H 4.25 . 1 450 . 45 PRO CB C 32.8 . 1 451 . 45 PRO HB2 H 2.48 . 2 452 . 45 PRO HB3 H 2.06 . 2 453 . 45 PRO CG C 27.9 . 1 454 . 45 PRO HG2 H 2.30 . 2 455 . 45 PRO HG3 H 2.06 . 2 456 . 45 PRO HD2 H 3.27 . 2 457 . 45 PRO HD3 H 2.54 . 2 458 . 46 GLU N N 123.2 . 1 459 . 46 GLU H H 8.93 . 1 460 . 46 GLU CA C 58.7 . 1 461 . 46 GLU HA H 3.97 . 1 462 . 46 GLU CB C 29.4 . 1 463 . 46 GLU HB2 H 2.01 . 2 464 . 46 GLU HB3 H 1.96 . 2 465 . 46 GLU CG C 36.3 . 1 466 . 46 GLU HG2 H 2.30 . 1 467 . 46 GLU HG3 H 2.30 . 1 468 . 47 ASP N N 114.9 . 1 469 . 47 ASP H H 8.31 . 1 470 . 47 ASP CA C 52.5 . 1 471 . 47 ASP HA H 4.62 . 1 472 . 47 ASP CB C 39.6 . 1 473 . 47 ASP HB2 H 2.86 . 2 474 . 47 ASP HB3 H 2.58 . 2 475 . 48 TRP N N 122.0 . 1 476 . 48 TRP H H 7.43 . 1 477 . 48 TRP CA C 58.7 . 1 478 . 48 TRP HA H 4.05 . 1 479 . 48 TRP CB C 29.6 . 1 480 . 48 TRP HB2 H 3.17 . 2 481 . 48 TRP HB3 H 2.92 . 2 482 . 48 TRP CD1 C 126.1 . 1 483 . 48 TRP CE3 C 120.4 . 1 484 . 48 TRP NE1 N 129.6 . 1 485 . 48 TRP HD1 H 7.01 . 1 486 . 48 TRP HE3 H 7.55 . 1 487 . 48 TRP CZ3 C 122.3 . 1 488 . 48 TRP CZ2 C 115.8 . 1 489 . 48 TRP HE1 H 10.62 . 1 490 . 48 TRP HZ3 H 7.33 . 1 491 . 48 TRP CH2 C 125.0 . 1 492 . 48 TRP HZ2 H 7.23 . 1 493 . 48 TRP HH2 H 7.35 . 1 494 . 49 ASP N N 130.0 . 1 495 . 49 ASP H H 8.59 . 1 496 . 49 ASP CA C 52.3 . 1 497 . 49 ASP HA H 4.78 . 1 498 . 49 ASP CB C 41.7 . 1 499 . 49 ASP HB2 H 2.66 . 2 500 . 49 ASP HB3 H 2.31 . 2 501 . 50 GLU N N 125.4 . 1 502 . 50 GLU H H 9.08 . 1 503 . 50 GLU CA C 58.9 . 1 504 . 50 GLU HA H 4.33 . 1 505 . 50 GLU CB C 29.4 . 1 506 . 50 GLU HB2 H 2.12 . 2 507 . 50 GLU HB3 H 2.02 . 2 508 . 50 GLU CG C 37.1 . 1 509 . 50 GLU HG2 H 2.56 . 2 510 . 50 GLU HG3 H 2.51 . 2 511 . 51 GLU N N 118.3 . 1 512 . 51 GLU H H 8.15 . 1 513 . 51 GLU CA C 58.7 . 1 514 . 51 GLU HA H 4.01 . 1 515 . 51 GLU CB C 29.4 . 1 516 . 51 GLU HB2 H 2.02 . 1 517 . 51 GLU HB3 H 2.02 . 1 518 . 51 GLU CG C 36.3 . 1 519 . 51 GLU HG2 H 2.29 . 2 520 . 51 GLU HG3 H 2.22 . 2 521 . 52 MET N N 115.3 . 1 522 . 52 MET H H 7.37 . 1 523 . 52 MET CA C 55.8 . 1 524 . 52 MET HA H 4.42 . 1 525 . 52 MET CB C 33.3 . 1 526 . 52 MET HB2 H 1.82 . 2 527 . 52 MET HB3 H 1.67 . 2 528 . 52 MET CG C 31.8 . 1 529 . 52 MET HG2 H 2.44 . 2 530 . 52 MET HG3 H 2.34 . 2 531 . 52 MET HE H 1.99 . 1 532 . 52 MET CE C 16.7 . 1 533 . 53 ASP N N 116.7 . 1 534 . 53 ASP H H 8.49 . 1 535 . 53 ASP CA C 54.8 . 1 536 . 53 ASP HA H 4.55 . 1 537 . 53 ASP CB C 41.2 . 1 538 . 53 ASP HB2 H 1.84 . 2 539 . 53 ASP HB3 H 1.37 . 2 540 . 54 GLY N N 108.2 . 1 541 . 54 GLY H H 7.56 . 1 542 . 54 GLY CA C 44.3 . 1 543 . 54 GLY HA3 H 4.29 . 2 544 . 54 GLY HA2 H 3.93 . 2 545 . 55 GLU N N 119.5 . 1 546 . 55 GLU H H 8.55 . 1 547 . 55 GLU CA C 56.6 . 1 548 . 55 GLU HA H 4.43 . 1 549 . 55 GLU CB C 30.0 . 1 550 . 55 GLU HB2 H 1.99 . 1 551 . 55 GLU HB3 H 1.99 . 1 552 . 55 GLU CG C 35.9 . 1 553 . 55 GLU HG2 H 2.36 . 2 554 . 55 GLU HG3 H 2.29 . 2 555 . 56 TRP N N 128.4 . 1 556 . 56 TRP H H 9.16 . 1 557 . 56 TRP CA C 59.3 . 1 558 . 56 TRP HA H 3.77 . 1 559 . 56 TRP CB C 27.3 . 1 560 . 56 TRP HB2 H 2.55 . 2 561 . 56 TRP HB3 H 1.30 . 2 562 . 56 TRP NE1 N 129.8 . 1 563 . 56 TRP HD1 H 5.29 . 1 564 . 56 TRP CZ3 C 121.7 . 1 565 . 56 TRP CZ2 C 113.2 . 1 566 . 56 TRP HE1 H 9.95 . 1 567 . 56 TRP HZ3 H 6.87 . 1 568 . 56 TRP CH2 C 123.8 . 1 569 . 56 TRP HZ2 H 7.03 . 1 570 . 56 TRP HH2 H 6.74 . 1 571 . 57 GLU N N 127.4 . 1 572 . 57 GLU H H 6.93 . 1 573 . 57 GLU CA C 52.1 . 1 574 . 57 GLU HA H 4.14 . 1 575 . 57 GLU CB C 31.0 . 1 576 . 57 GLU HB2 H 1.60 . 2 577 . 57 GLU HB3 H 1.46 . 2 578 . 57 GLU CG C 35.3 . 1 579 . 57 GLU HG2 H 1.93 . 1 580 . 57 GLU HG3 H 1.93 . 1 581 . 58 PRO CD C 49.8 . 1 582 . 58 PRO CA C 60.3 . 1 583 . 58 PRO HA H 3.57 . 1 584 . 58 PRO CB C 30.8 . 1 585 . 58 PRO HB2 H 2.13 . 2 586 . 58 PRO HB3 H 1.65 . 2 587 . 58 PRO CG C 26.9 . 1 588 . 58 PRO HG2 H 1.81 . 2 589 . 58 PRO HG3 H 1.74 . 2 590 . 58 PRO HD2 H 3.29 . 2 591 . 58 PRO HD3 H 3.01 . 2 592 . 59 PRO CD C 50.5 . 1 593 . 59 PRO CA C 62.3 . 1 594 . 59 PRO HA H 4.37 . 1 595 . 59 PRO CB C 32.2 . 1 596 . 59 PRO HB2 H 2.27 . 2 597 . 59 PRO HB3 H 1.91 . 2 598 . 59 PRO CG C 27.1 . 1 599 . 59 PRO HG2 H 2.05 . 1 600 . 59 PRO HG3 H 2.05 . 1 601 . 59 PRO HD2 H 3.65 . 2 602 . 59 PRO HD3 H 3.37 . 2 603 . 60 VAL N N 114.5 . 1 604 . 60 VAL H H 8.00 . 1 605 . 60 VAL CA C 60.3 . 1 606 . 60 VAL HA H 4.65 . 1 607 . 60 VAL CB C 33.7 . 1 608 . 60 VAL HB H 1.77 . 1 609 . 60 VAL HG1 H 0.57 . 2 610 . 60 VAL HG2 H 0.62 . 2 611 . 60 VAL CG1 C 19.1 . 1 612 . 60 VAL CG2 C 21.2 . 1 613 . 61 ILE N N 117.9 . 1 614 . 61 ILE H H 9.10 . 1 615 . 61 ILE CA C 59.1 . 1 616 . 61 ILE HA H 4.73 . 1 617 . 61 ILE CB C 42.5 . 1 618 . 61 ILE HB H 1.99 . 1 619 . 61 ILE HG2 H 0.87 . 1 620 . 61 ILE CG2 C 17.9 . 1 621 . 61 ILE CG1 C 25.7 . 1 622 . 61 ILE HG12 H 1.25 . 1 623 . 61 ILE HG13 H 1.25 . 1 624 . 61 ILE HD1 H 0.88 . 1 625 . 61 ILE CD1 C 14.0 . 1 626 . 62 GLN N N 120.2 . 1 627 . 62 GLN H H 8.57 . 1 628 . 62 GLN CA C 56.2 . 1 629 . 62 GLN HA H 4.16 . 1 630 . 62 GLN CB C 28.7 . 1 631 . 62 GLN HB2 H 1.97 . 1 632 . 62 GLN HB3 H 1.97 . 1 633 . 62 GLN CG C 33.9 . 1 634 . 62 GLN HG2 H 2.32 . 1 635 . 62 GLN HG3 H 2.32 . 1 636 . 62 GLN NE2 N 111.9 . 1 637 . 62 GLN HE21 H 7.60 . 2 638 . 62 GLN HE22 H 6.92 . 2 639 . 63 ASN N N 124.0 . 1 640 . 63 ASN H H 8.49 . 1 641 . 63 ASN CA C 50.1 . 1 642 . 63 ASN HA H 4.57 . 1 643 . 63 ASN HB2 H 1.94 . 1 644 . 63 ASN HB3 H 1.94 . 1 645 . 63 ASN ND2 N 112.7 . 1 646 . 63 ASN HD21 H 8.65 . 2 647 . 63 ASN HD22 H 7.88 . 2 648 . 64 PRO CD C 51.1 . 1 649 . 64 PRO CA C 64.4 . 1 650 . 64 PRO HA H 4.42 . 1 651 . 64 PRO CB C 32.4 . 1 652 . 64 PRO HB2 H 2.40 . 2 653 . 64 PRO HB3 H 1.95 . 2 654 . 64 PRO CG C 27.1 . 1 655 . 64 PRO HG2 H 2.04 . 1 656 . 64 PRO HG3 H 2.04 . 1 657 . 64 PRO HD2 H 4.26 . 2 658 . 64 PRO HD3 H 4.05 . 2 659 . 65 GLU N N 112.3 . 1 660 . 65 GLU H H 7.21 . 1 661 . 65 GLU CA C 55.8 . 1 662 . 65 GLU HA H 4.11 . 1 663 . 65 GLU CB C 30.4 . 1 664 . 65 GLU HB2 H 2.10 . 2 665 . 65 GLU HB3 H 1.64 . 2 666 . 65 GLU CG C 36.9 . 1 667 . 65 GLU HG2 H 2.26 . 2 668 . 65 GLU HG3 H 2.10 . 2 669 . 66 TYR N N 119.1 . 1 670 . 66 TYR H H 7.45 . 1 671 . 66 TYR CA C 58.9 . 1 672 . 66 TYR HA H 4.15 . 1 673 . 66 TYR CB C 38.2 . 1 674 . 66 TYR HB2 H 3.09 . 2 675 . 66 TYR HB3 H 3.00 . 2 676 . 66 TYR HD1 H 7.19 . 1 677 . 66 TYR HD2 H 7.19 . 1 678 . 66 TYR HE1 H 6.91 . 1 679 . 66 TYR HE2 H 6.91 . 1 680 . 66 TYR CD1 C 134.5 . 1 681 . 66 TYR CE1 C 118.6 . 1 682 . 67 LYS N N 127.6 . 1 683 . 67 LYS H H 8.59 . 1 684 . 67 LYS CA C 55.4 . 1 685 . 67 LYS HA H 4.01 . 1 686 . 67 LYS CB C 33.1 . 1 687 . 67 LYS HB2 H 1.31 . 2 688 . 67 LYS HB3 H 0.50 . 2 689 . 67 LYS CG C 24.0 . 1 690 . 67 LYS HG2 H 0.89 . 2 691 . 67 LYS HG3 H 0.79 . 2 692 . 67 LYS CD C 27.9 . 1 693 . 67 LYS HD2 H 0.76 . 2 694 . 67 LYS HD3 H 0.67 . 2 695 . 67 LYS CE C 41.7 . 1 696 . 67 LYS HE2 H 2.48 . 1 697 . 67 LYS HE3 H 2.48 . 1 698 . 68 GLY H H 5.05 . 1 699 . 68 GLY CA C 44.5 . 1 700 . 68 GLY HA3 H 4.05 . 2 701 . 68 GLY HA2 H 3.50 . 2 702 . 69 GLU N N 122.4 . 1 703 . 69 GLU H H 8.72 . 1 704 . 69 GLU CA C 56.4 . 1 705 . 69 GLU HA H 4.45 . 1 706 . 69 GLU CB C 30.2 . 1 707 . 69 GLU HB2 H 1.97 . 1 708 . 69 GLU HB3 H 1.97 . 1 709 . 69 GLU CG C 35.9 . 1 710 . 69 GLU HG2 H 2.35 . 2 711 . 69 GLU HG3 H 2.27 . 2 712 . 70 TRP N N 128.4 . 1 713 . 70 TRP H H 9.02 . 1 714 . 70 TRP CA C 59.5 . 1 715 . 70 TRP HA H 3.62 . 1 716 . 70 TRP HB2 H 2.54 . 2 717 . 70 TRP HB3 H 1.36 . 2 718 . 70 TRP NE1 N 130.3 . 1 719 . 70 TRP HD1 H 5.02 . 1 720 . 70 TRP CZ3 C 121.7 . 1 721 . 70 TRP CZ2 C 114.3 . 1 722 . 70 TRP HE1 H 9.80 . 1 723 . 70 TRP HZ3 H 6.80 . 1 724 . 70 TRP CH2 C 124.0 . 1 725 . 70 TRP HZ2 H 6.96 . 1 726 . 70 TRP HH2 H 6.72 . 1 727 . 71 LYS N N 126.6 . 1 728 . 71 LYS H H 6.60 . 1 729 . 71 LYS CA C 52.1 . 1 730 . 71 LYS HA H 3.98 . 1 731 . 71 LYS CB C 33.9 . 1 732 . 71 LYS HB2 H 1.38 . 2 733 . 71 LYS HB3 H 1.21 . 2 734 . 71 LYS CG C 23.8 . 1 735 . 71 LYS HG2 H 1.13 . 1 736 . 71 LYS HG3 H 1.13 . 1 737 . 71 LYS CD C 28.9 . 1 738 . 71 LYS HD2 H 1.51 . 2 739 . 71 LYS HD3 H 1.47 . 2 740 . 71 LYS CE C 41.9 . 1 741 . 71 LYS HE2 H 2.81 . 1 742 . 71 LYS HE3 H 2.81 . 1 743 . 72 PRO CD C 49.9 . 1 744 . 72 PRO CA C 61.3 . 1 745 . 72 PRO HA H 3.83 . 1 746 . 72 PRO CB C 32.8 . 1 747 . 72 PRO HB2 H 2.25 . 2 748 . 72 PRO HB3 H 1.75 . 2 749 . 72 PRO CG C 26.7 . 1 750 . 72 PRO HG2 H 1.78 . 2 751 . 72 PRO HG3 H 1.58 . 2 752 . 72 PRO HD2 H 3.12 . 2 753 . 72 PRO HD3 H 2.85 . 2 754 . 73 ARG N N 122.6 . 1 755 . 73 ARG H H 9.28 . 1 756 . 73 ARG CA C 56.0 . 1 757 . 73 ARG HA H 4.09 . 1 758 . 73 ARG CB C 30.6 . 1 759 . 73 ARG HB2 H 1.90 . 2 760 . 73 ARG HB3 H 1.71 . 2 761 . 73 ARG CG C 27.5 . 1 762 . 73 ARG HG2 H 1.60 . 1 763 . 73 ARG HG3 H 1.60 . 1 764 . 73 ARG CD C 43.5 . 1 765 . 73 ARG HD2 H 3.20 . 2 766 . 73 ARG HD3 H 3.13 . 2 767 . 73 ARG NE N 84.4 . 1 768 . 73 ARG HE H 7.65 . 1 769 . 74 GLN N N 118.7 . 1 770 . 74 GLN H H 8.39 . 1 771 . 74 GLN CA C 53.8 . 1 772 . 74 GLN HA H 4.96 . 1 773 . 74 GLN CB C 31.4 . 1 774 . 74 GLN HB2 H 1.83 . 2 775 . 74 GLN HB3 H 1.69 . 2 776 . 74 GLN CG C 34.1 . 1 777 . 74 GLN HG2 H 2.13 . 1 778 . 74 GLN HG3 H 2.13 . 1 779 . 74 GLN NE2 N 114.3 . 1 780 . 74 GLN HE21 H 7.29 . 2 781 . 74 GLN HE22 H 7.08 . 2 782 . 75 ILE N N 116.7 . 1 783 . 75 ILE H H 9.06 . 1 784 . 75 ILE CA C 58.9 . 1 785 . 75 ILE HA H 4.61 . 1 786 . 75 ILE CB C 42.1 . 1 787 . 75 ILE HB H 1.94 . 1 788 . 75 ILE HG2 H 0.82 . 1 789 . 75 ILE CG2 C 18.1 . 1 790 . 75 ILE CG1 C 25.7 . 1 791 . 75 ILE HG12 H 1.26 . 1 792 . 75 ILE HG13 H 1.26 . 1 793 . 75 ILE HD1 H 0.86 . 1 794 . 75 ILE CD1 C 13.8 . 1 795 . 76 ASP N N 120.4 . 1 796 . 76 ASP H H 8.42 . 1 797 . 76 ASP CA C 55.3 . 1 798 . 76 ASP HA H 4.48 . 1 799 . 76 ASP CB C 40.6 . 1 800 . 76 ASP HB2 H 2.56 . 2 801 . 76 ASP HB3 H 2.38 . 2 802 . 77 ASN N N 120.2 . 1 803 . 77 ASN H H 8.10 . 1 804 . 77 ASN CA C 49.8 . 1 805 . 77 ASN HA H 4.63 . 1 806 . 77 ASN ND2 N 113.1 . 1 807 . 77 ASN HD21 H 8.55 . 2 808 . 77 ASN HD22 H 7.42 . 2 809 . 78 PRO CD C 51.1 . 1 810 . 78 PRO CA C 64.4 . 1 811 . 78 PRO HA H 4.39 . 1 812 . 78 PRO CB C 32.6 . 1 813 . 78 PRO HB2 H 2.32 . 2 814 . 78 PRO HB3 H 1.95 . 2 815 . 78 PRO HD2 H 4.21 . 2 816 . 78 PRO HD3 H 3.97 . 2 817 . 79 ASP N N 115.3 . 1 818 . 79 ASP H H 7.32 . 1 819 . 79 ASP CA C 54.1 . 1 820 . 79 ASP HA H 4.67 . 1 821 . 79 ASP CB C 41.4 . 1 822 . 79 ASP HB2 H 2.89 . 2 823 . 79 ASP HB3 H 2.42 . 2 824 . 80 TYR N N 120.2 . 1 825 . 80 TYR H H 7.29 . 1 826 . 80 TYR CA C 58.0 . 1 827 . 80 TYR HA H 4.26 . 1 828 . 80 TYR CB C 38.8 . 1 829 . 80 TYR HB2 H 3.20 . 2 830 . 80 TYR HB3 H 2.91 . 2 831 . 80 TYR HD1 H 6.99 . 1 832 . 80 TYR HD2 H 6.99 . 1 833 . 80 TYR HE1 H 6.76 . 1 834 . 80 TYR HE2 H 6.76 . 1 835 . 80 TYR CD1 C 133.6 . 1 836 . 80 TYR CE1 C 118.3 . 1 837 . 81 LYS N N 127.0 . 1 838 . 81 LYS H H 8.39 . 1 839 . 81 LYS CA C 55.0 . 1 840 . 81 LYS HA H 4.05 . 1 841 . 81 LYS CB C 32.4 . 1 842 . 81 LYS HB2 H 1.19 . 2 843 . 81 LYS HB3 H 0.82 . 2 844 . 81 LYS CG C 24.6 . 1 845 . 81 LYS HG2 H 1.04 . 1 846 . 81 LYS HG3 H 1.04 . 1 847 . 81 LYS CD C 28.5 . 1 848 . 81 LYS HD2 H 1.20 . 1 849 . 81 LYS HD3 H 1.20 . 1 850 . 81 LYS CE C 41.9 . 1 851 . 81 LYS HE2 H 2.69 . 1 852 . 81 LYS HE3 H 2.69 . 1 853 . 82 GLY CA C 44.5 . 1 854 . 82 GLY HA3 H 3.95 . 2 855 . 82 GLY HA2 H 3.47 . 2 856 . 83 THR N N 114.5 . 1 857 . 83 THR H H 8.20 . 1 858 . 83 THR CA C 62.6 . 1 859 . 83 THR HA H 4.36 . 1 860 . 83 THR CB C 69.7 . 1 861 . 83 THR HB H 4.05 . 1 862 . 83 THR HG2 H 1.20 . 1 863 . 83 THR CG2 C 21.8 . 1 864 . 84 TRP N N 127.0 . 1 865 . 84 TRP H H 8.89 . 1 866 . 84 TRP CA C 58.3 . 1 867 . 84 TRP HA H 4.15 . 1 868 . 84 TRP CB C 28.3 . 1 869 . 84 TRP HB2 H 2.94 . 1 870 . 84 TRP HB3 H 2.94 . 1 871 . 84 TRP NE1 N 129.2 . 1 872 . 84 TRP HD1 H 6.16 . 1 873 . 84 TRP CZ3 C 121.8 . 1 874 . 84 TRP CZ2 C 114.1 . 1 875 . 84 TRP HE1 H 9.95 . 1 876 . 84 TRP HZ3 H 6.81 . 1 877 . 84 TRP CH2 C 123.9 . 1 878 . 84 TRP HZ2 H 7.13 . 1 879 . 84 TRP HH2 H 6.71 . 1 880 . 85 ILE N N 125.6 . 1 881 . 85 ILE H H 7.43 . 1 882 . 85 ILE CA C 59.7 . 1 883 . 85 ILE HA H 3.78 . 1 884 . 85 ILE CB C 38.2 . 1 885 . 85 ILE HB H 1.48 . 1 886 . 85 ILE HG2 H 0.61 . 1 887 . 85 ILE CG2 C 16.9 . 1 888 . 85 ILE CG1 C 26.7 . 1 889 . 85 ILE HG12 H 1.21 . 2 890 . 85 ILE HG13 H 0.94 . 2 891 . 85 ILE HD1 H 0.68 . 1 892 . 85 ILE CD1 C 12.2 . 1 893 . 86 HIS N N 125.4 . 1 894 . 86 HIS H H 8.09 . 1 895 . 86 HIS CB C 29.6 . 1 896 . 86 HIS HB2 H 2.96 . 2 897 . 86 HIS HB3 H 2.86 . 2 898 . 86 HIS CD2 C 119.3 . 1 899 . 86 HIS CE1 C 137.3 . 1 900 . 86 HIS HD2 H 7.31 . 1 901 . 86 HIS HE1 H 8.20 . 1 902 . 87 PRO CD C 50.9 . 1 903 . 87 PRO CA C 63.2 . 1 904 . 87 PRO HA H 4.29 . 1 905 . 87 PRO CB C 32.4 . 1 906 . 87 PRO HB2 H 2.22 . 2 907 . 87 PRO HB3 H 1.86 . 2 908 . 87 PRO CG C 27.1 . 1 909 . 87 PRO HG2 H 1.93 . 1 910 . 87 PRO HG3 H 1.93 . 1 911 . 87 PRO HD2 H 3.58 . 2 912 . 87 PRO HD3 H 3.37 . 2 913 . 88 GLU N N 120.6 . 1 914 . 88 GLU H H 8.67 . 1 915 . 88 GLU CA C 55.8 . 1 916 . 88 GLU HA H 4.48 . 1 917 . 88 GLU CB C 30.8 . 1 918 . 88 GLU HB2 H 1.91 . 2 919 . 88 GLU HB3 H 1.83 . 2 920 . 88 GLU CG C 36.1 . 1 921 . 88 GLU HG2 H 2.26 . 2 922 . 88 GLU HG3 H 2.06 . 2 923 . 89 ILE N N 119.1 . 1 924 . 89 ILE H H 8.37 . 1 925 . 89 ILE CA C 60.3 . 1 926 . 89 ILE HA H 4.26 . 1 927 . 89 ILE CB C 39.8 . 1 928 . 89 ILE HB H 1.85 . 1 929 . 89 ILE HG2 H 0.84 . 1 930 . 89 ILE CG2 C 17.5 . 1 931 . 89 ILE CG1 C 26.7 . 1 932 . 89 ILE HG12 H 1.35 . 2 933 . 89 ILE HG13 H 1.00 . 2 934 . 89 ILE HD1 H 0.82 . 1 935 . 89 ILE CD1 C 13.0 . 1 936 . 90 ASP N N 122.6 . 1 937 . 90 ASP H H 8.35 . 1 938 . 90 ASP CA C 54.4 . 1 939 . 90 ASP HA H 4.56 . 1 940 . 90 ASP CB C 41.0 . 1 941 . 90 ASP HB2 H 2.62 . 2 942 . 90 ASP HB3 H 2.49 . 2 943 . 91 ASN N N 119.9 . 1 944 . 91 ASN H H 8.31 . 1 945 . 91 ASN CA C 50.9 . 1 946 . 91 ASN HA H 4.83 . 1 947 . 91 ASN CB C 39.0 . 1 948 . 91 ASN HB2 H 2.90 . 2 949 . 91 ASN HB3 H 2.58 . 2 950 . 91 ASN ND2 N 112.7 . 1 951 . 91 ASN HD21 H 7.76 . 2 952 . 91 ASN HD22 H 7.08 . 2 953 . 92 PRO CD C 50.7 . 1 954 . 92 PRO CA C 63.6 . 1 955 . 92 PRO HA H 4.39 . 1 956 . 92 PRO CB C 32.0 . 1 957 . 92 PRO HB2 H 2.27 . 2 958 . 92 PRO HB3 H 1.90 . 2 959 . 92 PRO CG C 27.1 . 1 960 . 92 PRO HG2 H 1.99 . 1 961 . 92 PRO HG3 H 1.99 . 1 962 . 92 PRO HD2 H 3.85 . 2 963 . 92 PRO HD3 H 3.78 . 2 964 . 93 GLU N N 118.5 . 1 965 . 93 GLU H H 8.14 . 1 966 . 93 GLU CA C 56.2 . 1 967 . 93 GLU HA H 4.19 . 1 968 . 93 GLU CB C 29.8 . 1 969 . 93 GLU HB2 H 1.97 . 2 970 . 93 GLU HB3 H 1.82 . 2 971 . 93 GLU CG C 36.1 . 1 972 . 93 GLU HG2 H 2.19 . 2 973 . 93 GLU HG3 H 2.12 . 2 974 . 94 TYR N N 120.8 . 1 975 . 94 TYR H H 7.90 . 1 976 . 94 TYR CA C 57.8 . 1 977 . 94 TYR HA H 4.47 . 1 978 . 94 TYR CB C 38.8 . 1 979 . 94 TYR HB2 H 2.97 . 1 980 . 94 TYR HB3 H 2.97 . 1 981 . 94 TYR HD1 H 7.04 . 1 982 . 94 TYR HD2 H 7.04 . 1 983 . 94 TYR HE1 H 6.75 . 1 984 . 94 TYR HE2 H 6.75 . 1 985 . 94 TYR CD1 C 133.2 . 1 986 . 94 TYR CE1 C 118.2 . 1 987 . 95 SER N N 120.2 . 1 988 . 95 SER H H 7.95 . 1 989 . 95 SER CA C 55.2 . 1 990 . 95 SER HA H 4.64 . 1 991 . 95 SER CB C 63.6 . 1 992 . 95 SER HB2 H 3.71 . 1 993 . 95 SER HB3 H 3.71 . 1 994 . 96 PRO CD C 50.5 . 1 995 . 96 PRO CA C 63.2 . 1 996 . 96 PRO HA H 4.32 . 1 997 . 96 PRO CB C 32.0 . 1 998 . 96 PRO HB2 H 2.26 . 2 999 . 96 PRO HB3 H 1.93 . 2 1000 . 96 PRO CG C 27.1 . 1 1001 . 96 PRO HG2 H 1.95 . 1 1002 . 96 PRO HG3 H 1.95 . 1 1003 . 96 PRO HD2 H 3.65 . 2 1004 . 96 PRO HD3 H 3.49 . 2 1005 . 97 ASP N N 119.3 . 1 1006 . 97 ASP H H 8.18 . 1 1007 . 97 ASP CA C 54.2 . 1 1008 . 97 ASP HA H 4.50 . 1 1009 . 97 ASP CB C 41.0 . 1 1010 . 97 ASP HB2 H 2.68 . 2 1011 . 97 ASP HB3 H 2.54 . 2 1012 . 98 ALA N N 123.8 . 1 1013 . 98 ALA H H 8.05 . 1 1014 . 98 ALA CA C 52.7 . 1 1015 . 98 ALA HA H 4.26 . 1 1016 . 98 ALA HB H 1.36 . 1 1017 . 98 ALA CB C 19.7 . 1 1018 . 99 ASN N N 117.9 . 1 1019 . 99 ASN H H 8.42 . 1 1020 . 99 ASN CA C 53.3 . 1 1021 . 99 ASN HA H 4.70 . 1 1022 . 99 ASN CB C 38.8 . 1 1023 . 99 ASN HB2 H 2.83 . 2 1024 . 99 ASN HB3 H 2.69 . 2 1025 . 99 ASN ND2 N 113.3 . 1 1026 . 99 ASN HD21 H 7.62 . 2 1027 . 99 ASN HD22 H 6.89 . 2 1028 . 100 ILE N N 124.4 . 1 1029 . 100 ILE H H 7.56 . 1 1030 . 100 ILE CA C 62.6 . 1 1031 . 100 ILE HA H 4.05 . 1 1032 . 100 ILE CB C 39.6 . 1 1033 . 100 ILE HB H 1.81 . 1 1034 . 100 ILE CG1 C 27.1 . 1 1035 . 100 ILE HG12 H 1.36 . 2 1036 . 100 ILE HG13 H 1.09 . 2 1037 . 100 ILE HD1 H 0.84 . 1 1038 . 100 ILE CD1 C 13.6 . 1 stop_ save_