data_15303 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C resonance assignments for bb' domains of human protein disulfide isomerase (PDI) ; _BMRB_accession_number 15303 _BMRB_flat_file_name bmr15303.str _Entry_type original _Submission_date 2007-06-13 _Accession_date 2007-06-13 _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 Denisov Alexey . . 2 Maattanen Pekka . . 3 Thomas David . . 4 Gehring Kalle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 935 "13C chemical shifts" 685 "15N chemical shifts" 223 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-31 update author 'correct entry citation' 2008-04-22 update author 'complete entry citation' 2007-08-08 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4156 'b domain of human PDI' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title "1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase" _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636846 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Denisov 'Alexey Yu' . . 2 Maattanen Pekka . . 3 Sprules Tara . . 4 Thomas David Y. . 5 Gehring Kalle . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 129 _Page_last 130 _Year 2007 _Details . loop_ _Keyword 'disulfide bonds' 'endoplasmic reticulum' NMR PDI 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bb-PDI monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'bb-PDI monomer, major conformer' $bb-PDI 'bb-PDI monomer, minor conformer' $bb-PDI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bb-PDI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common bb-PDI _Molecular_mass 25500 _Mol_thiol_state 'all free' loop_ _Biological_function 'protein folding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 228 _Mol_residue_sequence ; GPLGSPAATTLPDGAAAESL VESSEVAVIGFFKDVESDSA KQFLQAAEAIDDIPFGITSN SDVFSKYQLDKDGVVLFKKF DEGRNNFEGEVTKENLLDFI KHNQLPLVIEFTEQTAPKIF GGEIKTHILLFLPKSVSDYD GKLSNFKTAAESFKGKILFI FIDSDHTDNQRILEFFGLKK EECPAVRLITLEEEMTKYKP ESEELTAERITEFCHRFLEG KIKPHLMS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 LEU 4 GLY 5 SER 6 PRO 7 ALA 8 ALA 9 THR 10 THR 11 LEU 12 PRO 13 ASP 14 GLY 15 ALA 16 ALA 17 ALA 18 GLU 19 SER 20 LEU 21 VAL 22 GLU 23 SER 24 SER 25 GLU 26 VAL 27 ALA 28 VAL 29 ILE 30 GLY 31 PHE 32 PHE 33 LYS 34 ASP 35 VAL 36 GLU 37 SER 38 ASP 39 SER 40 ALA 41 LYS 42 GLN 43 PHE 44 LEU 45 GLN 46 ALA 47 ALA 48 GLU 49 ALA 50 ILE 51 ASP 52 ASP 53 ILE 54 PRO 55 PHE 56 GLY 57 ILE 58 THR 59 SER 60 ASN 61 SER 62 ASP 63 VAL 64 PHE 65 SER 66 LYS 67 TYR 68 GLN 69 LEU 70 ASP 71 LYS 72 ASP 73 GLY 74 VAL 75 VAL 76 LEU 77 PHE 78 LYS 79 LYS 80 PHE 81 ASP 82 GLU 83 GLY 84 ARG 85 ASN 86 ASN 87 PHE 88 GLU 89 GLY 90 GLU 91 VAL 92 THR 93 LYS 94 GLU 95 ASN 96 LEU 97 LEU 98 ASP 99 PHE 100 ILE 101 LYS 102 HIS 103 ASN 104 GLN 105 LEU 106 PRO 107 LEU 108 VAL 109 ILE 110 GLU 111 PHE 112 THR 113 GLU 114 GLN 115 THR 116 ALA 117 PRO 118 LYS 119 ILE 120 PHE 121 GLY 122 GLY 123 GLU 124 ILE 125 LYS 126 THR 127 HIS 128 ILE 129 LEU 130 LEU 131 PHE 132 LEU 133 PRO 134 LYS 135 SER 136 VAL 137 SER 138 ASP 139 TYR 140 ASP 141 GLY 142 LYS 143 LEU 144 SER 145 ASN 146 PHE 147 LYS 148 THR 149 ALA 150 ALA 151 GLU 152 SER 153 PHE 154 LYS 155 GLY 156 LYS 157 ILE 158 LEU 159 PHE 160 ILE 161 PHE 162 ILE 163 ASP 164 SER 165 ASP 166 HIS 167 THR 168 ASP 169 ASN 170 GLN 171 ARG 172 ILE 173 LEU 174 GLU 175 PHE 176 PHE 177 GLY 178 LEU 179 LYS 180 LYS 181 GLU 182 GLU 183 CYS 184 PRO 185 ALA 186 VAL 187 ARG 188 LEU 189 ILE 190 THR 191 LEU 192 GLU 193 GLU 194 GLU 195 MET 196 THR 197 LYS 198 TYR 199 LYS 200 PRO 201 GLU 202 SER 203 GLU 204 GLU 205 LEU 206 THR 207 ALA 208 GLU 209 ARG 210 ILE 211 THR 212 GLU 213 PHE 214 CYS 215 HIS 216 ARG 217 PHE 218 LEU 219 GLU 220 GLY 221 LYS 222 ILE 223 LYS 224 PRO 225 HIS 226 LEU 227 MET 228 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 15974 "b-b'-x" 97.81 236 100.00 100.00 3.48e-157 BMRB 15998 "b'-x" 56.14 140 100.00 100.00 3.57e-85 PDB 2K18 "Solution Structure Of Bb' Domains Of Human Protein Disulfide Isomerase" 100.00 228 100.00 100.00 2.12e-161 PDB 3BJ5 "Alternative Conformations Of The X Region Of Human Protein Disulphide- Isomerase Modulate Exposure Of The Substrate Binding B' " 56.58 147 98.45 99.22 1.81e-84 PDB 3UEM "Crystal Structure Of Human Pdi Bb'a' Domains" 100.00 361 98.68 98.68 3.45e-154 PDB 4EKZ "Crystal Structure Of Reduced Hpdi (abb'xa')" 97.81 482 100.00 100.00 9.56e-154 PDB 4EL1 "Crystal Structure Of Oxidized Hpdi (abb'xa')" 97.81 482 100.00 100.00 9.56e-154 PDB 4JU5 "Crystal Structure Of The Dimeric Form Of The Bb' Domains Of Human Protein Disulfide Isomerase" 100.00 238 100.00 100.00 1.96e-161 DBJ BAE79726 "protein disulfide isomerase [Macaca fuscata]" 97.81 510 99.10 100.00 2.22e-152 DBJ BAE87231 "unnamed protein product [Macaca fascicularis]" 97.81 510 97.76 99.55 3.06e-150 DBJ BAE88032 "unnamed protein product [Macaca fascicularis]" 84.21 336 97.40 98.96 2.93e-127 DBJ BAG37999 "unnamed protein product [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 DBJ BAG60277 "unnamed protein product [Homo sapiens]" 97.81 492 99.55 99.55 2.97e-153 EMBL CAA28775 "unnamed protein product [Homo sapiens]" 97.81 508 100.00 100.00 1.63e-153 EMBL CAH93050 "hypothetical protein [Pongo abelii]" 97.81 508 99.10 99.55 1.47e-152 GB AAA61169 "thyroid hormone binding protein precursor [Homo sapiens]" 97.81 508 99.55 99.55 1.17e-152 GB AAC13652 "prolyl 4-hydroxylase beta-subunit [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 GB AAH10859 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 GB AAH29617 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 GB AAH71892 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 REF NP_000909 "protein disulfide-isomerase precursor [Homo sapiens]" 97.81 508 100.00 100.00 7.20e-154 REF NP_001126805 "protein disulfide-isomerase precursor [Pongo abelii]" 97.81 508 99.10 99.55 1.47e-152 REF NP_001233358 "protein disulfide-isomerase precursor [Pan troglodytes]" 97.81 508 99.55 99.55 6.01e-153 REF XP_002764185 "PREDICTED: protein disulfide-isomerase isoform X2 [Callithrix jacchus]" 97.81 510 97.31 99.10 3.13e-150 REF XP_003282223 "PREDICTED: protein disulfide-isomerase isoform X1 [Nomascus leucogenys]" 97.81 505 97.76 98.21 5.32e-148 SP P07237 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 97.81 508 100.00 100.00 7.20e-154 SP Q2HWU2 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Prolyl 4-hydroxylase subunit beta; Flags: Precursor" 97.81 510 99.10 100.00 2.22e-152 SP Q5R5B6 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 97.81 508 99.10 99.55 1.47e-152 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $bb-PDI Human 9606 Eukaryota Metazoa Homo sapiens 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 $bb-PDI 'recombinant technology' . Escherichia coli BL21 pGEX-6P-1 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 $bb-PDI 2 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 25 mM 'natural abundance' 'sodium chloride' 70 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' DTT 5 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $bb-PDI 2 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 25 mM 'natural abundance' 'sodium chloride' 70 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' DTT 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.0 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details ; Extra peaks of second (minor) form of PDI-bb were found just for few N- and C-terminal residues which is probably result of cis-trans isomerization for Pro-6 and Pro-224 residues. Additional 15N and 1H backbone amide chemical shifts are corresponding to (in ppm): LEU-3 (121.4, 8.51), GLY-4 (109.4, 8.19), SER-5 (115.4, 7.83), ILE-222 (118.9, 7.63), LYS-223 (125.5, 8.08), HIS-225 (119.0, 8.33), LEU-226 (123.2, 8.03), MET-227 (121.2, 8.28). ; loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D 1H-15N NOESY' '3D HNCO' 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 'bb-PDI monomer, major conformer' _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 2 2 PRO C C 176.9 0.20 1 2 2 2 PRO CA C 63.0 0.20 1 3 2 2 PRO CB C 32.1 0.20 1 4 3 3 LEU H H 8.51 0.01 1 5 3 3 LEU HA H 4.32 0.01 1 6 3 3 LEU HB2 H 1.65 0.01 2 7 3 3 LEU HD1 H 0.91 0.01 2 8 3 3 LEU C C 177.9 0.20 1 9 3 3 LEU CA C 55.5 0.20 1 10 3 3 LEU CB C 42.0 0.20 1 11 3 3 LEU N N 122.4 0.25 1 12 4 4 GLY H H 8.45 0.01 1 13 4 4 GLY HA2 H 3.90 0.01 2 14 4 4 GLY HA3 H 4.02 0.01 2 15 4 4 GLY C C 173.8 0.20 1 16 4 4 GLY CA C 45.1 0.20 1 17 4 4 GLY N N 110.2 0.25 1 18 5 5 SER H H 8.04 0.01 1 19 5 5 SER HA H 4.01 0.01 1 20 5 5 SER HB2 H 3.85 0.01 2 21 5 5 SER CA C 56.3 0.20 1 22 5 5 SER CB C 63.3 0.20 1 23 5 5 SER N N 116.9 0.25 1 24 6 6 PRO HA H 4.45 0.01 1 25 6 6 PRO HB2 H 2.33 0.01 2 26 6 6 PRO HB3 H 2.03 0.01 2 27 6 6 PRO C C 176.7 0.20 1 28 6 6 PRO CA C 63.0 0.20 1 29 6 6 PRO CB C 32.0 0.20 1 30 7 7 ALA H H 8.56 0.01 1 31 7 7 ALA HA H 4.10 0.01 1 32 7 7 ALA HB H 1.23 0.01 1 33 7 7 ALA C C 176.6 0.20 1 34 7 7 ALA CA C 53.4 0.20 1 35 7 7 ALA CB C 19.6 0.20 1 36 7 7 ALA N N 123.6 0.25 1 37 8 8 ALA H H 7.41 0.01 1 38 8 8 ALA HA H 4.68 0.01 1 39 8 8 ALA HB H 1.00 0.01 1 40 8 8 ALA C C 175.9 0.20 1 41 8 8 ALA CA C 50.1 0.20 1 42 8 8 ALA CB C 21.3 0.20 1 43 8 8 ALA N N 116.2 0.25 1 44 9 9 THR H H 8.67 0.01 1 45 9 9 THR HA H 4.33 0.01 1 46 9 9 THR HB H 4.01 0.01 1 47 9 9 THR HG2 H 1.28 0.01 1 48 9 9 THR C C 174.4 0.20 1 49 9 9 THR CA C 62.6 0.20 1 50 9 9 THR CB C 70.1 0.20 1 51 9 9 THR N N 119.9 0.25 1 52 10 10 THR H H 9.00 0.01 1 53 10 10 THR HA H 4.58 0.01 1 54 10 10 THR HB H 4.09 0.01 1 55 10 10 THR HG2 H 1.21 0.01 1 56 10 10 THR C C 174.1 0.20 1 57 10 10 THR CA C 63.9 0.20 1 58 10 10 THR CB C 68.5 0.20 1 59 10 10 THR N N 125.9 0.25 1 60 11 11 LEU H H 9.01 0.01 1 61 11 11 LEU HA H 4.97 0.01 1 62 11 11 LEU HB2 H 1.91 0.01 2 63 11 11 LEU HD1 H 0.68 0.01 2 64 11 11 LEU HG H 1.65 0.01 1 65 11 11 LEU CA C 50.2 0.20 1 66 11 11 LEU CB C 41.7 0.20 1 67 11 11 LEU N N 127.2 0.25 1 68 12 12 PRO HA H 4.52 0.01 1 69 12 12 PRO HB2 H 2.42 0.01 2 70 12 12 PRO HB3 H 2.03 0.01 2 71 12 12 PRO C C 175.3 0.20 1 72 12 12 PRO CA C 63.9 0.20 1 73 12 12 PRO CB C 32.7 0.20 1 74 13 13 ASP H H 7.11 0.01 1 75 13 13 ASP HA H 4.42 0.01 1 76 13 13 ASP HB2 H 3.02 0.01 2 77 13 13 ASP HB3 H 2.87 0.01 2 78 13 13 ASP C C 175.4 0.20 1 79 13 13 ASP CA C 52.3 0.20 1 80 13 13 ASP CB C 42.0 0.20 1 81 13 13 ASP N N 112.1 0.25 1 82 14 14 GLY H H 9.12 0.01 1 83 14 14 GLY HA2 H 3.61 0.01 2 84 14 14 GLY HA3 H 4.01 0.01 2 85 14 14 GLY C C 175.1 0.20 1 86 14 14 GLY CA C 47.4 0.20 1 87 14 14 GLY N N 106.6 0.25 1 88 15 15 ALA H H 8.05 0.01 1 89 15 15 ALA HA H 4.17 0.01 1 90 15 15 ALA HB H 1.41 0.01 1 91 15 15 ALA C C 180.5 0.20 1 92 15 15 ALA CA C 54.8 0.20 1 93 15 15 ALA CB C 17.6 0.20 1 94 15 15 ALA N N 125.1 0.25 1 95 16 16 ALA H H 8.26 0.01 1 96 16 16 ALA HA H 4.17 0.01 1 97 16 16 ALA HB H 1.65 0.01 1 98 16 16 ALA C C 180.5 0.20 1 99 16 16 ALA CA C 54.5 0.20 1 100 16 16 ALA CB C 18.6 0.20 1 101 16 16 ALA N N 121.6 0.25 1 102 17 17 ALA H H 7.60 0.01 1 103 17 17 ALA HA H 3.99 0.01 1 104 17 17 ALA HB H 1.53 0.01 1 105 17 17 ALA C C 177.2 0.20 1 106 17 17 ALA CA C 55.4 0.20 1 107 17 17 ALA CB C 18.7 0.20 1 108 17 17 ALA N N 120.6 0.25 1 109 18 18 GLU H H 8.45 0.01 1 110 18 18 GLU HA H 3.79 0.01 1 111 18 18 GLU HB2 H 2.01 0.01 2 112 18 18 GLU HG2 H 2.21 0.01 2 113 18 18 GLU HG3 H 2.38 0.01 2 114 18 18 GLU C C 178.8 0.20 1 115 18 18 GLU CA C 59.2 0.20 1 116 18 18 GLU CB C 29.5 0.20 1 117 18 18 GLU N N 117.1 0.25 1 118 19 19 SER H H 7.92 0.01 1 119 19 19 SER HA H 4.15 0.01 1 120 19 19 SER HB2 H 3.94 0.01 2 121 19 19 SER C C 176.8 0.20 1 122 19 19 SER CA C 61.3 0.20 1 123 19 19 SER CB C 62.4 0.20 1 124 19 19 SER N N 112.8 0.25 1 125 20 20 LEU H H 7.46 0.01 1 126 20 20 LEU HA H 4.02 0.01 1 127 20 20 LEU HB2 H 1.84 0.01 2 128 20 20 LEU HD1 H 0.85 0.01 2 129 20 20 LEU HD2 H 0.70 0.01 2 130 20 20 LEU HG H 1.56 0.01 1 131 20 20 LEU C C 179.2 0.20 1 132 20 20 LEU CA C 58.4 0.20 1 133 20 20 LEU CB C 41.6 0.20 1 134 20 20 LEU N N 123.0 0.25 1 135 21 21 VAL H H 7.98 0.01 1 136 21 21 VAL HA H 3.09 0.01 1 137 21 21 VAL HB H 1.76 0.01 1 138 21 21 VAL HG1 H 0.53 0.01 2 139 21 21 VAL HG2 H 0.10 0.01 2 140 21 21 VAL C C 177.6 0.20 1 141 21 21 VAL CA C 66.8 0.20 1 142 21 21 VAL CB C 31.6 0.20 1 143 21 21 VAL N N 119.5 0.25 1 144 22 22 GLU H H 8.18 0.01 1 145 22 22 GLU HA H 4.04 0.01 1 146 22 22 GLU HB2 H 2.03 0.01 2 147 22 22 GLU HG2 H 2.32 0.01 2 148 22 22 GLU C C 178.7 0.20 1 149 22 22 GLU CA C 58.0 0.20 1 150 22 22 GLU CB C 29.5 0.20 1 151 22 22 GLU N N 114.8 0.25 1 152 23 23 SER H H 7.57 0.01 1 153 23 23 SER HA H 4.36 0.01 1 154 23 23 SER HB2 H 4.10 0.01 2 155 23 23 SER HB3 H 4.04 0.01 2 156 23 23 SER C C 173.7 0.20 1 157 23 23 SER CA C 59.8 0.20 1 158 23 23 SER CB C 64.0 0.20 1 159 23 23 SER N N 112.5 0.25 1 160 24 24 SER H H 7.08 0.01 1 161 24 24 SER HA H 4.80 0.01 1 162 24 24 SER HB2 H 3.63 0.01 2 163 24 24 SER HB3 H 3.54 0.01 2 164 24 24 SER C C 172.8 0.20 1 165 24 24 SER CA C 57.2 0.20 1 166 24 24 SER CB C 65.4 0.20 1 167 24 24 SER N N 115.4 0.25 1 168 25 25 GLU H H 8.70 0.01 1 169 25 25 GLU HA H 3.97 0.01 1 170 25 25 GLU HB2 H 2.22 0.01 2 171 25 25 GLU HB3 H 2.30 0.01 2 172 25 25 GLU HG2 H 2.49 0.01 2 173 25 25 GLU C C 175.7 0.20 1 174 25 25 GLU CA C 59.9 0.20 1 175 25 25 GLU CB C 30.3 0.20 1 176 25 25 GLU N N 124.5 0.25 1 177 26 26 VAL H H 7.32 0.01 1 178 26 26 VAL HA H 5.00 0.01 1 179 26 26 VAL HB H 1.91 0.01 1 180 26 26 VAL HG1 H 1.18 0.01 2 181 26 26 VAL HG2 H 0.89 0.01 2 182 26 26 VAL C C 174.3 0.20 1 183 26 26 VAL CA C 60.5 0.20 1 184 26 26 VAL CB C 35.7 0.20 1 185 26 26 VAL N N 113.5 0.25 1 186 27 27 ALA H H 9.13 0.01 1 187 27 27 ALA HA H 4.82 0.01 1 188 27 27 ALA HB H 1.18 0.01 1 189 27 27 ALA C C 175.0 0.20 1 190 27 27 ALA CA C 51.2 0.20 1 191 27 27 ALA CB C 23.0 0.20 1 192 27 27 ALA N N 127.2 0.25 1 193 28 28 VAL H H 7.98 0.01 1 194 28 28 VAL HA H 5.08 0.01 1 195 28 28 VAL HB H 1.20 0.01 1 196 28 28 VAL HG1 H 0.85 0.01 2 197 28 28 VAL HG2 H 0.55 0.01 2 198 28 28 VAL C C 174.6 0.20 1 199 28 28 VAL CA C 60.8 0.20 1 200 28 28 VAL CB C 34.3 0.20 1 201 28 28 VAL N N 120.1 0.25 1 202 29 29 ILE H H 9.08 0.01 1 203 29 29 ILE HA H 4.78 0.01 1 204 29 29 ILE HB H 1.43 0.01 1 205 29 29 ILE HD1 H -0.45 0.01 1 206 29 29 ILE HG2 H 0.84 0.01 1 207 29 29 ILE C C 173.3 0.20 1 208 29 29 ILE CA C 60.0 0.20 1 209 29 29 ILE CB C 40.3 0.20 1 210 29 29 ILE N N 124.3 0.25 1 211 30 30 GLY H H 8.61 0.01 1 212 30 30 GLY HA2 H 1.91 0.01 2 213 30 30 GLY HA3 H 3.96 0.01 2 214 30 30 GLY C C 169.3 0.20 1 215 30 30 GLY CA C 44.5 0.20 1 216 30 30 GLY N N 115.8 0.25 1 217 31 31 PHE H H 8.47 0.01 1 218 31 31 PHE HA H 4.20 0.01 1 219 31 31 PHE HB2 H 2.06 0.01 2 220 31 31 PHE HB3 H 0.53 0.01 2 221 31 31 PHE C C 172.8 0.20 1 222 31 31 PHE CA C 55.0 0.20 1 223 31 31 PHE CB C 36.5 0.20 1 224 31 31 PHE N N 127.8 0.25 1 225 32 32 PHE H H 8.20 0.01 1 226 32 32 PHE HA H 4.98 0.01 1 227 32 32 PHE HB2 H 2.90 0.01 2 228 32 32 PHE HB3 H 2.27 0.01 2 229 32 32 PHE C C 174.4 0.20 1 230 32 32 PHE CA C 55.7 0.20 1 231 32 32 PHE CB C 42.9 0.20 1 232 32 32 PHE N N 116.9 0.25 1 233 33 33 LYS H H 9.42 0.01 1 234 33 33 LYS HA H 4.02 0.01 1 235 33 33 LYS HB2 H 1.96 0.01 2 236 33 33 LYS HB3 H 1.81 0.01 2 237 33 33 LYS HG2 H 1.55 0.01 2 238 33 33 LYS HG3 H 1.39 0.01 2 239 33 33 LYS C C 176.7 0.20 1 240 33 33 LYS CA C 58.9 0.20 1 241 33 33 LYS CB C 31.9 0.20 1 242 33 33 LYS N N 124.7 0.25 1 243 34 34 ASP H H 8.92 0.01 1 244 34 34 ASP HA H 5.02 0.01 1 245 34 34 ASP HB2 H 2.93 0.01 2 246 34 34 ASP HB3 H 2.57 0.01 2 247 34 34 ASP C C 177.8 0.20 1 248 34 34 ASP CA C 51.7 0.20 1 249 34 34 ASP CB C 41.8 0.20 1 250 34 34 ASP N N 117.3 0.25 1 251 35 35 VAL H H 8.56 0.01 1 252 35 35 VAL HA H 3.79 0.01 1 253 35 35 VAL HB H 2.38 0.01 1 254 35 35 VAL HG1 H 1.03 0.01 2 255 35 35 VAL HG2 H 0.98 0.01 2 256 35 35 VAL C C 174.5 0.20 1 257 35 35 VAL CA C 63.9 0.20 1 258 35 35 VAL CB C 30.5 0.20 1 259 35 35 VAL N N 120.7 0.25 1 260 36 36 GLU H H 8.25 0.01 1 261 36 36 GLU HA H 4.39 0.01 1 262 36 36 GLU HB2 H 1.91 0.01 2 263 36 36 GLU HG2 H 2.10 0.01 2 264 36 36 GLU HG3 H 2.29 0.01 2 265 36 36 GLU C C 176.6 0.20 1 266 36 36 GLU CA C 54.8 0.20 1 267 36 36 GLU CB C 29.2 0.20 1 268 36 36 GLU N N 117.2 0.25 1 269 37 37 SER H H 7.56 0.01 1 270 37 37 SER HA H 4.30 0.01 1 271 37 37 SER HB2 H 4.20 0.01 2 272 37 37 SER HB3 H 4.42 0.01 2 273 37 37 SER C C 174.0 0.20 1 274 37 37 SER CA C 58.1 0.20 1 275 37 37 SER CB C 65.4 0.20 1 276 37 37 SER N N 116.1 0.25 1 277 38 38 ASP H H 8.92 0.01 1 278 38 38 ASP HA H 4.29 0.01 1 279 38 38 ASP HB2 H 2.72 0.01 2 280 38 38 ASP C C 179.2 0.20 1 281 38 38 ASP CA C 58.1 0.20 1 282 38 38 ASP CB C 40.1 0.20 1 283 38 38 ASP N N 121.4 0.25 1 284 39 39 SER H H 8.50 0.01 1 285 39 39 SER HA H 4.05 0.01 1 286 39 39 SER HB2 H 3.91 0.01 2 287 39 39 SER C C 174.5 0.20 1 288 39 39 SER CA C 61.5 0.20 1 289 39 39 SER CB C 62.4 0.20 1 290 39 39 SER N N 114.2 0.25 1 291 40 40 ALA H H 6.97 0.01 1 292 40 40 ALA HA H 2.38 0.01 1 293 40 40 ALA HB H 0.94 0.01 1 294 40 40 ALA C C 179.6 0.20 1 295 40 40 ALA CA C 54.5 0.20 1 296 40 40 ALA CB C 18.6 0.20 1 297 40 40 ALA N N 125.7 0.25 1 298 41 41 LYS H H 8.04 0.01 1 299 41 41 LYS HA H 3.83 0.01 1 300 41 41 LYS HB2 H 1.92 0.01 2 301 41 41 LYS HB3 H 1.78 0.01 2 302 41 41 LYS HG2 H 1.57 0.01 2 303 41 41 LYS HG3 H 1.33 0.01 2 304 41 41 LYS C C 180.5 0.20 1 305 41 41 LYS CA C 60.0 0.20 1 306 41 41 LYS CB C 31.9 0.20 1 307 41 41 LYS N N 115.8 0.25 1 308 42 42 GLN H H 7.87 0.01 1 309 42 42 GLN HA H 3.78 0.01 1 310 42 42 GLN HB2 H 1.78 0.01 2 311 42 42 GLN HB3 H 2.17 0.01 2 312 42 42 GLN HG2 H 2.65 0.01 2 313 42 42 GLN C C 177.8 0.20 1 314 42 42 GLN CA C 58.6 0.20 1 315 42 42 GLN CB C 28.6 0.20 1 316 42 42 GLN N N 119.1 0.25 1 317 43 43 PHE H H 7.71 0.01 1 318 43 43 PHE HA H 3.85 0.01 1 319 43 43 PHE HB2 H 2.74 0.01 2 320 43 43 PHE HB3 H 3.28 0.01 2 321 43 43 PHE C C 176.2 0.20 1 322 43 43 PHE CA C 61.3 0.20 1 323 43 43 PHE CB C 39.0 0.20 1 324 43 43 PHE N N 120.0 0.25 1 325 44 44 LEU H H 8.36 0.01 1 326 44 44 LEU HA H 3.58 0.01 1 327 44 44 LEU HB2 H 1.86 0.01 2 328 44 44 LEU HD1 H 0.87 0.01 2 329 44 44 LEU HG H 1.39 0.01 1 330 44 44 LEU C C 179.4 0.20 1 331 44 44 LEU CA C 57.4 0.20 1 332 44 44 LEU CB C 40.9 0.20 1 333 44 44 LEU N N 119.5 0.25 1 334 45 45 GLN H H 7.66 0.01 1 335 45 45 GLN HA H 3.90 0.01 1 336 45 45 GLN HB2 H 1.89 0.01 2 337 45 45 GLN HB3 H 2.09 0.01 2 338 45 45 GLN HG2 H 2.31 0.01 2 339 45 45 GLN HG3 H 2.59 0.01 2 340 45 45 GLN C C 179.3 0.20 1 341 45 45 GLN CA C 58.7 0.20 1 342 45 45 GLN CB C 28.7 0.20 1 343 45 45 GLN N N 117.7 0.25 1 344 46 46 ALA H H 7.63 0.01 1 345 46 46 ALA HA H 3.74 0.01 1 346 46 46 ALA HB H 1.28 0.01 1 347 46 46 ALA C C 177.1 0.20 1 348 46 46 ALA CA C 55.3 0.20 1 349 46 46 ALA CB C 17.5 0.20 1 350 46 46 ALA N N 123.7 0.25 1 351 47 47 ALA H H 7.33 0.01 1 352 47 47 ALA HA H 1.79 0.01 1 353 47 47 ALA HB H 0.44 0.01 1 354 47 47 ALA C C 178.6 0.20 1 355 47 47 ALA CA C 53.2 0.20 1 356 47 47 ALA CB C 17.7 0.20 1 357 47 47 ALA N N 118.1 0.25 1 358 48 48 GLU H H 7.02 0.01 1 359 48 48 GLU HA H 3.84 0.01 1 360 48 48 GLU HB2 H 1.91 0.01 2 361 48 48 GLU HG2 H 2.17 0.01 2 362 48 48 GLU HG3 H 2.32 0.01 2 363 48 48 GLU C C 177.1 0.20 1 364 48 48 GLU CA C 57.3 0.20 1 365 48 48 GLU CB C 29.9 0.20 1 366 48 48 GLU N N 112.9 0.25 1 367 49 49 ALA H H 7.25 0.01 1 368 49 49 ALA HA H 4.25 0.01 1 369 49 49 ALA HB H 1.48 0.01 1 370 49 49 ALA C C 176.9 0.20 1 371 49 49 ALA CA C 52.6 0.20 1 372 49 49 ALA CB C 20.1 0.20 1 373 49 49 ALA N N 119.8 0.25 1 374 50 50 ILE H H 7.03 0.01 1 375 50 50 ILE HA H 4.37 0.01 1 376 50 50 ILE HB H 1.96 0.01 1 377 50 50 ILE HD1 H 0.95 0.01 1 378 50 50 ILE HG12 H 1.49 0.01 2 379 50 50 ILE HG13 H 1.26 0.01 2 380 50 50 ILE HG2 H 1.19 0.01 1 381 50 50 ILE C C 174.3 0.20 1 382 50 50 ILE CA C 59.7 0.20 1 383 50 50 ILE CB C 39.4 0.20 1 384 50 50 ILE N N 119.3 0.25 1 385 51 51 ASP H H 8.39 0.01 1 386 51 51 ASP HA H 4.83 0.01 1 387 51 51 ASP HB2 H 2.67 0.01 2 388 51 51 ASP C C 177.5 0.20 1 389 51 51 ASP CA C 54.3 0.20 1 390 51 51 ASP CB C 42.2 0.20 1 391 51 51 ASP N N 123.2 0.25 1 392 52 52 ASP H H 8.53 0.01 1 393 52 52 ASP HA H 4.57 0.01 1 394 52 52 ASP HB2 H 2.65 0.01 2 395 52 52 ASP HB3 H 2.88 0.01 2 396 52 52 ASP C C 175.0 0.20 1 397 52 52 ASP CA C 54.6 0.20 1 398 52 52 ASP CB C 40.2 0.20 1 399 52 52 ASP N N 116.0 0.25 1 400 53 53 ILE H H 7.15 0.01 1 401 53 53 ILE HA H 4.57 0.01 1 402 53 53 ILE HB H 1.63 0.01 1 403 53 53 ILE HD1 H 0.60 0.01 1 404 53 53 ILE HG12 H 1.42 0.01 2 405 53 53 ILE HG13 H 1.17 0.01 2 406 53 53 ILE HG2 H 0.97 0.01 1 407 53 53 ILE CA C 57.7 0.20 1 408 53 53 ILE CB C 42.0 0.20 1 409 53 53 ILE N N 119.3 0.25 1 410 54 54 PRO C C 175.1 0.20 1 411 54 54 PRO CA C 62.7 0.20 1 412 54 54 PRO CB C 32.5 0.20 1 413 55 55 PHE H H 8.78 0.01 1 414 55 55 PHE HA H 5.84 0.01 1 415 55 55 PHE HB2 H 2.60 0.01 2 416 55 55 PHE HB3 H 3.23 0.01 2 417 55 55 PHE C C 176.9 0.20 1 418 55 55 PHE CA C 55.6 0.20 1 419 55 55 PHE CB C 42.0 0.20 1 420 55 55 PHE N N 119.9 0.25 1 421 56 56 GLY H H 9.51 0.01 1 422 56 56 GLY HA2 H 3.35 0.01 2 423 56 56 GLY HA3 H 5.62 0.01 2 424 56 56 GLY C C 170.8 0.20 1 425 56 56 GLY CA C 43.4 0.20 1 426 56 56 GLY N N 109.0 0.25 1 427 57 57 ILE H H 8.93 0.01 1 428 57 57 ILE HA H 5.57 0.01 1 429 57 57 ILE HB H 1.70 0.01 1 430 57 57 ILE HD1 H 0.88 0.01 1 431 57 57 ILE HG12 H 1.16 0.01 2 432 57 57 ILE HG2 H 1.02 0.01 1 433 57 57 ILE C C 172.0 0.20 1 434 57 57 ILE CA C 58.4 0.20 1 435 57 57 ILE CB C 42.9 0.20 1 436 57 57 ILE N N 120.8 0.25 1 437 58 58 THR H H 8.66 0.01 1 438 58 58 THR HA H 4.96 0.01 1 439 58 58 THR HB H 3.90 0.01 1 440 58 58 THR HG2 H 0.71 0.01 1 441 58 58 THR C C 170.0 0.20 1 442 58 58 THR CA C 60.1 0.20 1 443 58 58 THR CB C 72.1 0.20 1 444 58 58 THR N N 121.2 0.25 1 445 59 59 SER H H 8.71 0.01 1 446 59 59 SER HA H 5.20 0.01 1 447 59 59 SER HB2 H 4.04 0.01 2 448 59 59 SER HB3 H 4.21 0.01 2 449 59 59 SER C C 173.9 0.20 1 450 59 59 SER CA C 56.7 0.20 1 451 59 59 SER CB C 65.7 0.20 1 452 59 59 SER N N 119.9 0.25 1 453 60 60 ASN H H 8.03 0.01 1 454 60 60 ASN HA H 4.79 0.01 1 455 60 60 ASN HB2 H 2.85 0.01 2 456 60 60 ASN CA C 53.2 0.20 1 457 60 60 ASN CB C 39.5 0.20 1 458 60 60 ASN N N 122.2 0.25 1 459 61 61 SER HB2 H 3.84 0.01 2 460 61 61 SER C C 175.9 0.20 1 461 61 61 SER CA C 62.5 0.20 1 462 61 61 SER CB C 62.5 0.20 1 463 62 62 ASP H H 8.63 0.01 1 464 62 62 ASP HA H 4.53 0.01 1 465 62 62 ASP HB2 H 2.80 0.01 2 466 62 62 ASP HB3 H 2.71 0.01 2 467 62 62 ASP C C 179.0 0.20 1 468 62 62 ASP CA C 57.4 0.20 1 469 62 62 ASP CB C 40.0 0.20 1 470 62 62 ASP N N 122.2 0.25 1 471 63 63 VAL H H 8.03 0.01 1 472 63 63 VAL HA H 3.75 0.01 1 473 63 63 VAL HB H 2.65 0.01 1 474 63 63 VAL HG1 H 1.18 0.01 2 475 63 63 VAL HG2 H 0.77 0.01 2 476 63 63 VAL C C 177.9 0.20 1 477 63 63 VAL CA C 65.8 0.20 1 478 63 63 VAL CB C 30.7 0.20 1 479 63 63 VAL N N 122.4 0.25 1 480 64 64 PHE H H 7.98 0.01 1 481 64 64 PHE HA H 4.20 0.01 1 482 64 64 PHE HB2 H 3.54 0.01 2 483 64 64 PHE HB3 H 3.12 0.01 2 484 64 64 PHE C C 178.8 0.20 1 485 64 64 PHE CA C 61.7 0.20 1 486 64 64 PHE CB C 37.5 0.20 1 487 64 64 PHE N N 120.1 0.25 1 488 65 65 SER H H 8.09 0.01 1 489 65 65 SER HA H 4.21 0.01 1 490 65 65 SER HB2 H 4.00 0.01 2 491 65 65 SER C C 177.8 0.20 1 492 65 65 SER CA C 61.6 0.20 1 493 65 65 SER CB C 62.3 0.20 1 494 65 65 SER N N 112.1 0.25 1 495 66 66 LYS H H 7.65 0.01 1 496 66 66 LYS HA H 3.87 0.01 1 497 66 66 LYS HB2 H 1.88 0.01 2 498 66 66 LYS HG2 H 1.18 0.01 2 499 66 66 LYS HG3 H 0.19 0.01 2 500 66 66 LYS C C 176.7 0.20 1 501 66 66 LYS CA C 58.9 0.20 1 502 66 66 LYS CB C 32.7 0.20 1 503 66 66 LYS N N 124.1 0.25 1 504 67 67 TYR H H 7.04 0.01 1 505 67 67 TYR HA H 4.64 0.01 1 506 67 67 TYR HB2 H 3.26 0.01 2 507 67 67 TYR HB3 H 2.36 0.01 2 508 67 67 TYR C C 173.6 0.20 1 509 67 67 TYR CA C 58.4 0.20 1 510 67 67 TYR CB C 37.7 0.20 1 511 67 67 TYR N N 113.8 0.25 1 512 68 68 GLN H H 7.85 0.01 1 513 68 68 GLN HA H 3.83 0.01 1 514 68 68 GLN HB2 H 2.17 0.01 2 515 68 68 GLN HG2 H 2.34 0.01 2 516 68 68 GLN C C 174.7 0.20 1 517 68 68 GLN CA C 57.4 0.20 1 518 68 68 GLN CB C 25.0 0.20 1 519 68 68 GLN N N 113.7 0.25 1 520 69 69 LEU H H 8.07 0.01 1 521 69 69 LEU HA H 4.53 0.01 1 522 69 69 LEU HB2 H 1.54 0.01 2 523 69 69 LEU HD1 H 0.08 0.01 2 524 69 69 LEU HD2 H -0.18 0.01 2 525 69 69 LEU HG H 0.98 0.01 1 526 69 69 LEU C C 176.8 0.20 1 527 69 69 LEU CA C 54.9 0.20 1 528 69 69 LEU CB C 43.2 0.20 1 529 69 69 LEU N N 120.8 0.25 1 530 70 70 ASP H H 8.58 0.01 1 531 70 70 ASP HA H 4.65 0.01 1 532 70 70 ASP HB2 H 2.72 0.01 2 533 70 70 ASP HB3 H 2.54 0.01 2 534 70 70 ASP C C 174.8 0.20 1 535 70 70 ASP CA C 53.2 0.20 1 536 70 70 ASP CB C 41.6 0.20 1 537 70 70 ASP N N 120.4 0.25 1 538 71 71 LYS H H 7.72 0.01 1 539 71 71 LYS HA H 4.55 0.01 1 540 71 71 LYS HB2 H 2.04 0.01 2 541 71 71 LYS HB3 H 1.81 0.01 2 542 71 71 LYS HG2 H 1.39 0.01 2 543 71 71 LYS C C 173.1 0.20 1 544 71 71 LYS CA C 54.3 0.20 1 545 71 71 LYS CB C 34.1 0.20 1 546 71 71 LYS N N 117.3 0.25 1 547 72 72 ASP H H 7.78 0.01 1 548 72 72 ASP HA H 4.65 0.01 1 549 72 72 ASP HB2 H 2.61 0.01 2 550 72 72 ASP HB3 H 2.79 0.01 2 551 72 72 ASP C C 177.6 0.20 1 552 72 72 ASP CA C 54.5 0.20 1 553 72 72 ASP CB C 41.5 0.20 1 554 72 72 ASP N N 116.9 0.25 1 555 73 73 GLY H H 8.66 0.01 1 556 73 73 GLY HA2 H 3.89 0.01 2 557 73 73 GLY C C 169.7 0.20 1 558 73 73 GLY CA C 45.5 0.20 1 559 73 73 GLY N N 107.4 0.25 1 560 74 74 VAL H H 8.49 0.01 1 561 74 74 VAL HA H 4.84 0.01 1 562 74 74 VAL HB H 1.60 0.01 1 563 74 74 VAL HG1 H 0.89 0.01 2 564 74 74 VAL C C 173.5 0.20 1 565 74 74 VAL CA C 61.3 0.20 1 566 74 74 VAL CB C 35.5 0.20 1 567 74 74 VAL N N 117.9 0.25 1 568 75 75 VAL H H 8.93 0.01 1 569 75 75 VAL HA H 4.58 0.01 1 570 75 75 VAL HB H 1.71 0.01 1 571 75 75 VAL HG1 H 0.71 0.01 2 572 75 75 VAL HG2 H -0.03 0.01 2 573 75 75 VAL C C 172.7 0.20 1 574 75 75 VAL CA C 61.1 0.20 1 575 75 75 VAL CB C 35.6 0.20 1 576 75 75 VAL N N 126.9 0.25 1 577 76 76 LEU H H 8.69 0.01 1 578 76 76 LEU HA H 4.98 0.01 1 579 76 76 LEU HB2 H 1.60 0.01 2 580 76 76 LEU HD1 H 0.52 0.01 2 581 76 76 LEU HG H 1.45 0.01 1 582 76 76 LEU C C 173.4 0.20 1 583 76 76 LEU CA C 54.2 0.20 1 584 76 76 LEU CB C 46.0 0.20 1 585 76 76 LEU N N 128.0 0.25 1 586 77 77 PHE H H 9.60 0.01 1 587 77 77 PHE HA H 4.93 0.01 1 588 77 77 PHE HB2 H 3.10 0.01 2 589 77 77 PHE HB3 H 2.65 0.01 2 590 77 77 PHE C C 173.8 0.20 1 591 77 77 PHE CA C 56.8 0.20 1 592 77 77 PHE CB C 42.1 0.20 1 593 77 77 PHE N N 126.5 0.25 1 594 78 78 LYS H H 8.41 0.01 1 595 78 78 LYS HA H 5.41 0.01 1 596 78 78 LYS HB2 H 1.32 0.01 2 597 78 78 LYS HB3 H 1.18 0.01 2 598 78 78 LYS HG2 H 1.00 0.01 2 599 78 78 LYS HG3 H 0.65 0.01 2 600 78 78 LYS C C 176.6 0.20 1 601 78 78 LYS CA C 53.5 0.20 1 602 78 78 LYS CB C 34.6 0.20 1 603 78 78 LYS N N 115.8 0.25 1 604 79 79 LYS H H 8.01 0.01 1 605 79 79 LYS HA H 4.37 0.01 1 606 79 79 LYS HB2 H 2.24 0.01 2 607 79 79 LYS HB3 H 1.76 0.01 2 608 79 79 LYS HG2 H 1.48 0.01 2 609 79 79 LYS C C 175.0 0.20 1 610 79 79 LYS CA C 56.0 0.20 1 611 79 79 LYS CB C 31.9 0.20 1 612 79 79 LYS N N 121.4 0.25 1 613 80 80 PHE H H 6.62 0.01 1 614 80 80 PHE HA H 4.88 0.01 1 615 80 80 PHE HB2 H 3.37 0.01 2 616 80 80 PHE C C 174.0 0.20 1 617 80 80 PHE CA C 54.4 0.20 1 618 80 80 PHE CB C 40.4 0.20 1 619 80 80 PHE N N 113.5 0.25 1 620 81 81 ASP H H 8.98 0.01 1 621 81 81 ASP HA H 4.27 0.01 1 622 81 81 ASP HB2 H 3.00 0.01 2 623 81 81 ASP HB3 H 2.90 0.01 2 624 81 81 ASP C C 176.6 0.20 1 625 81 81 ASP CA C 56.0 0.20 1 626 81 81 ASP CB C 40.2 0.20 1 627 81 81 ASP N N 117.7 0.25 1 628 82 82 GLU H H 10.32 0.01 1 629 82 82 GLU HA H 4.34 0.01 1 630 82 82 GLU HB2 H 2.23 0.01 2 631 82 82 GLU HG2 H 2.54 0.01 2 632 82 82 GLU C C 178.7 0.20 1 633 82 82 GLU CA C 58.2 0.20 1 634 82 82 GLU CB C 28.6 0.20 1 635 82 82 GLU N N 123.9 0.25 1 636 83 83 GLY H H 7.78 0.01 1 637 83 83 GLY HA2 H 4.15 0.01 2 638 83 83 GLY HA3 H 4.29 0.01 2 639 83 83 GLY C C 174.4 0.20 1 640 83 83 GLY CA C 46.6 0.20 1 641 83 83 GLY N N 109.2 0.25 1 642 84 84 ARG H H 7.20 0.01 1 643 84 84 ARG HA H 5.21 0.01 1 644 84 84 ARG HB2 H 1.69 0.01 2 645 84 84 ARG HB3 H 1.57 0.01 2 646 84 84 ARG HG2 H 1.16 0.01 2 647 84 84 ARG C C 174.0 0.20 1 648 84 84 ARG CA C 55.0 0.20 1 649 84 84 ARG CB C 32.5 0.20 1 650 84 84 ARG N N 121.0 0.25 1 651 85 85 ASN H H 9.27 0.01 1 652 85 85 ASN HA H 5.00 0.01 1 653 85 85 ASN HB2 H 2.77 0.01 2 654 85 85 ASN HB3 H 2.19 0.01 2 655 85 85 ASN C C 172.9 0.20 1 656 85 85 ASN CA C 53.8 0.20 1 657 85 85 ASN CB C 43.6 0.20 1 658 85 85 ASN N N 121.6 0.25 1 659 86 86 ASN H H 9.15 0.01 1 660 86 86 ASN HA H 5.00 0.01 1 661 86 86 ASN HB2 H 2.72 0.01 2 662 86 86 ASN C C 174.4 0.20 1 663 86 86 ASN CA C 52.4 0.20 1 664 86 86 ASN CB C 38.6 0.20 1 665 86 86 ASN N N 123.2 0.25 1 666 87 87 PHE H H 8.38 0.01 1 667 87 87 PHE HA H 3.46 0.01 1 668 87 87 PHE HB2 H 2.62 0.01 2 669 87 87 PHE HB3 H 1.60 0.01 2 670 87 87 PHE C C 174.6 0.20 1 671 87 87 PHE CA C 59.0 0.20 1 672 87 87 PHE CB C 39.0 0.20 1 673 87 87 PHE N N 124.9 0.25 1 674 88 88 GLU H H 7.45 0.01 1 675 88 88 GLU HA H 4.27 0.01 1 676 88 88 GLU HB2 H 1.80 0.01 2 677 88 88 GLU HB3 H 1.55 0.01 2 678 88 88 GLU HG2 H 2.00 0.01 2 679 88 88 GLU C C 173.9 0.20 1 680 88 88 GLU CA C 54.8 0.20 1 681 88 88 GLU CB C 31.7 0.20 1 682 88 88 GLU N N 128.6 0.25 1 683 89 89 GLY H H 7.05 0.01 1 684 89 89 GLY HA2 H 3.70 0.01 2 685 89 89 GLY HA3 H 3.84 0.01 2 686 89 89 GLY C C 172.6 0.20 1 687 89 89 GLY CA C 43.4 0.20 1 688 89 89 GLY N N 108.6 0.25 1 689 90 90 GLU H H 8.45 0.01 1 690 90 90 GLU HA H 4.29 0.01 1 691 90 90 GLU HB2 H 1.88 0.01 2 692 90 90 GLU HG2 H 2.17 0.01 2 693 90 90 GLU HG3 H 2.29 0.01 2 694 90 90 GLU C C 177.4 0.20 1 695 90 90 GLU CA C 56.2 0.20 1 696 90 90 GLU CB C 29.9 0.20 1 697 90 90 GLU N N 120.4 0.25 1 698 91 91 VAL H H 9.14 0.01 1 699 91 91 VAL HA H 3.73 0.01 1 700 91 91 VAL HB H 2.27 0.01 1 701 91 91 VAL HG1 H 1.21 0.01 2 702 91 91 VAL HG2 H 0.89 0.01 2 703 91 91 VAL C C 173.6 0.20 1 704 91 91 VAL CA C 64.4 0.20 1 705 91 91 VAL CB C 29.8 0.20 1 706 91 91 VAL N N 126.5 0.25 1 707 92 92 THR H H 7.21 0.01 1 708 92 92 THR HA H 4.63 0.01 1 709 92 92 THR HB H 4.52 0.01 1 710 92 92 THR HG2 H 1.11 0.01 1 711 92 92 THR C C 174.1 0.20 1 712 92 92 THR CA C 58.0 0.20 1 713 92 92 THR CB C 72.4 0.20 1 714 92 92 THR N N 117.9 0.25 1 715 93 93 LYS H H 9.36 0.01 1 716 93 93 LYS HA H 3.68 0.01 1 717 93 93 LYS HB2 H 1.91 0.01 2 718 93 93 LYS HB3 H 1.76 0.01 2 719 93 93 LYS HG2 H 1.10 0.01 2 720 93 93 LYS C C 177.1 0.20 1 721 93 93 LYS CA C 60.7 0.20 1 722 93 93 LYS CB C 32.1 0.20 1 723 93 93 LYS N N 124.1 0.25 1 724 94 94 GLU H H 9.12 0.01 1 725 94 94 GLU HA H 3.90 0.01 1 726 94 94 GLU HB2 H 2.01 0.01 2 727 94 94 GLU HG2 H 2.28 0.01 2 728 94 94 GLU HG3 H 2.48 0.01 2 729 94 94 GLU C C 179.1 0.20 1 730 94 94 GLU CA C 60.7 0.20 1 731 94 94 GLU CB C 28.7 0.20 1 732 94 94 GLU N N 116.6 0.25 1 733 95 95 ASN H H 8.02 0.01 1 734 95 95 ASN HA H 4.65 0.01 1 735 95 95 ASN HB2 H 3.20 0.01 2 736 95 95 ASN HB3 H 3.12 0.01 2 737 95 95 ASN C C 179.7 0.20 1 738 95 95 ASN CA C 55.3 0.20 1 739 95 95 ASN CB C 37.5 0.20 1 740 95 95 ASN N N 118.1 0.25 1 741 96 96 LEU H H 8.55 0.01 1 742 96 96 LEU HA H 3.96 0.01 1 743 96 96 LEU HB2 H 2.00 0.01 2 744 96 96 LEU HB3 H 1.48 0.01 2 745 96 96 LEU HD1 H 0.76 0.01 2 746 96 96 LEU HD2 H 0.14 0.01 2 747 96 96 LEU HG H 1.02 0.01 1 748 96 96 LEU C C 178.4 0.20 1 749 96 96 LEU CA C 57.5 0.20 1 750 96 96 LEU CB C 42.2 0.20 1 751 96 96 LEU N N 121.6 0.25 1 752 97 97 LEU H H 8.50 0.01 1 753 97 97 LEU HA H 4.01 0.01 1 754 97 97 LEU HB2 H 1.93 0.01 2 755 97 97 LEU HD1 H 0.89 0.01 2 756 97 97 LEU HG H 1.54 0.01 1 757 97 97 LEU C C 179.2 0.20 1 758 97 97 LEU CA C 58.9 0.20 1 759 97 97 LEU CB C 40.9 0.20 1 760 97 97 LEU N N 120.1 0.25 1 761 98 98 ASP H H 7.66 0.01 1 762 98 98 ASP HA H 4.41 0.01 1 763 98 98 ASP HB2 H 2.85 0.01 2 764 98 98 ASP HB3 H 2.72 0.01 2 765 98 98 ASP C C 177.8 0.20 1 766 98 98 ASP CA C 57.7 0.20 1 767 98 98 ASP CB C 41.1 0.20 1 768 98 98 ASP N N 118.7 0.25 1 769 99 99 PHE H H 7.90 0.01 1 770 99 99 PHE HA H 4.53 0.01 1 771 99 99 PHE HB2 H 3.75 0.01 2 772 99 99 PHE HB3 H 3.43 0.01 2 773 99 99 PHE C C 177.6 0.20 1 774 99 99 PHE CA C 60.4 0.20 1 775 99 99 PHE CB C 39.8 0.20 1 776 99 99 PHE N N 120.8 0.25 1 777 100 100 ILE H H 8.78 0.01 1 778 100 100 ILE HA H 3.12 0.01 1 779 100 100 ILE HB H 2.15 0.01 1 780 100 100 ILE HD1 H 0.75 0.01 1 781 100 100 ILE HG12 H 1.80 0.01 2 782 100 100 ILE HG2 H 0.95 0.01 1 783 100 100 ILE C C 177.4 0.20 1 784 100 100 ILE CA C 65.5 0.20 1 785 100 100 ILE CB C 38.5 0.20 1 786 100 100 ILE N N 121.4 0.25 1 787 101 101 LYS H H 8.21 0.01 1 788 101 101 LYS HA H 4.20 0.01 1 789 101 101 LYS HB2 H 1.97 0.01 2 790 101 101 LYS HB3 H 1.85 0.01 2 791 101 101 LYS HG2 H 1.58 0.01 2 792 101 101 LYS HG3 H 1.45 0.01 2 793 101 101 LYS C C 179.4 0.20 1 794 101 101 LYS CA C 59.3 0.20 1 795 101 101 LYS CB C 31.8 0.20 1 796 101 101 LYS N N 117.9 0.25 1 797 102 102 HIS H H 7.87 0.01 1 798 102 102 HIS HA H 4.42 0.01 1 799 102 102 HIS HB2 H 3.17 0.01 2 800 102 102 HIS C C 175.9 0.20 1 801 102 102 HIS CA C 58.4 0.20 1 802 102 102 HIS CB C 30.1 0.20 1 803 102 102 HIS N N 113.9 0.25 1 804 103 103 ASN H H 7.27 0.01 1 805 103 103 ASN HA H 4.84 0.01 1 806 103 103 ASN HB2 H 2.58 0.01 2 807 103 103 ASN HB3 H 1.90 0.01 2 808 103 103 ASN C C 174.5 0.20 1 809 103 103 ASN CA C 54.4 0.20 1 810 103 103 ASN CB C 41.1 0.20 1 811 103 103 ASN N N 113.9 0.25 1 812 104 104 GLN H H 7.65 0.01 1 813 104 104 GLN HA H 4.25 0.01 1 814 104 104 GLN HB2 H 2.04 0.01 2 815 104 104 GLN HG2 H 2.31 0.01 2 816 104 104 GLN HG3 H 2.54 0.01 2 817 104 104 GLN C C 173.8 0.20 1 818 104 104 GLN CA C 57.4 0.20 1 819 104 104 GLN CB C 28.9 0.20 1 820 104 104 GLN N N 115.0 0.25 1 821 105 105 LEU H H 7.50 0.01 1 822 105 105 LEU HA H 4.72 0.01 1 823 105 105 LEU HB2 H 1.64 0.01 2 824 105 105 LEU HD1 H 0.89 0.01 2 825 105 105 LEU CA C 51.8 0.20 1 826 105 105 LEU CB C 42.1 0.20 1 827 105 105 LEU N N 119.7 0.25 1 828 106 106 PRO HA H 4.38 0.01 1 829 106 106 PRO C C 175.6 0.20 1 830 106 106 PRO CA C 61.7 0.20 1 831 106 106 PRO CB C 31.8 0.20 1 832 107 107 LEU H H 9.44 0.01 1 833 107 107 LEU HA H 3.98 0.01 1 834 107 107 LEU HB2 H 1.71 0.01 2 835 107 107 LEU HB3 H 1.57 0.01 2 836 107 107 LEU HD1 H 0.85 0.01 2 837 107 107 LEU C C 177.1 0.20 1 838 107 107 LEU CA C 57.8 0.20 1 839 107 107 LEU CB C 42.7 0.20 1 840 107 107 LEU N N 123.4 0.25 1 841 108 108 VAL H H 7.73 0.01 1 842 108 108 VAL HA H 5.01 0.01 1 843 108 108 VAL HB H 2.07 0.01 1 844 108 108 VAL HG1 H 0.89 0.01 2 845 108 108 VAL C C 174.8 0.20 1 846 108 108 VAL CA C 59.4 0.20 1 847 108 108 VAL CB C 34.4 0.20 1 848 108 108 VAL N N 109.7 0.25 1 849 109 109 ILE H H 8.70 0.01 1 850 109 109 ILE HA H 4.21 0.01 1 851 109 109 ILE HB H 1.74 0.01 1 852 109 109 ILE HD1 H 0.80 0.01 1 853 109 109 ILE HG12 H 1.58 0.01 2 854 109 109 ILE HG2 H 0.91 0.01 1 855 109 109 ILE C C 173.5 0.20 1 856 109 109 ILE CA C 59.9 0.20 1 857 109 109 ILE CB C 41.6 0.20 1 858 109 109 ILE N N 124.5 0.25 1 859 110 110 GLU H H 8.41 0.01 1 860 110 110 GLU HA H 3.43 0.01 1 861 110 110 GLU HB2 H 1.74 0.01 2 862 110 110 GLU HB3 H 1.54 0.01 2 863 110 110 GLU C C 176.0 0.20 1 864 110 110 GLU CA C 54.7 0.20 1 865 110 110 GLU CB C 29.8 0.20 1 866 110 110 GLU N N 128.2 0.25 1 867 111 111 PHE H H 8.68 0.01 1 868 111 111 PHE HA H 3.85 0.01 1 869 111 111 PHE HB2 H 2.82 0.01 2 870 111 111 PHE HB3 H 2.46 0.01 2 871 111 111 PHE C C 173.6 0.20 1 872 111 111 PHE CA C 59.5 0.20 1 873 111 111 PHE CB C 40.2 0.20 1 874 111 111 PHE N N 128.8 0.25 1 875 112 112 THR H H 7.31 0.01 1 876 112 112 THR HA H 4.50 0.01 1 877 112 112 THR HB H 4.22 0.01 1 878 112 112 THR HG2 H 1.03 0.01 1 879 112 112 THR C C 173.7 0.20 1 880 112 112 THR CA C 59.2 0.20 1 881 112 112 THR CB C 73.5 0.20 1 882 112 112 THR N N 119.8 0.25 1 883 113 113 GLU H H 8.93 0.01 1 884 113 113 GLU HA H 3.89 0.01 1 885 113 113 GLU HB2 H 2.02 0.01 2 886 113 113 GLU HG2 H 2.28 0.01 2 887 113 113 GLU HG3 H 2.37 0.01 2 888 113 113 GLU C C 178.1 0.20 1 889 113 113 GLU CA C 59.1 0.20 1 890 113 113 GLU CB C 29.2 0.20 1 891 113 113 GLU N N 120.1 0.25 1 892 114 114 GLN H H 7.94 0.01 1 893 114 114 GLN HA H 4.13 0.01 1 894 114 114 GLN HB2 H 2.01 0.01 2 895 114 114 GLN HG2 H 2.40 0.01 2 896 114 114 GLN C C 177.8 0.20 1 897 114 114 GLN CA C 58.2 0.20 1 898 114 114 GLN CB C 28.6 0.20 1 899 114 114 GLN N N 114.8 0.25 1 900 115 115 THR H H 7.50 0.01 1 901 115 115 THR HA H 4.18 0.01 1 902 115 115 THR HB H 3.86 0.01 1 903 115 115 THR HG2 H 1.18 0.01 1 904 115 115 THR C C 175.8 0.20 1 905 115 115 THR CA C 61.9 0.20 1 906 115 115 THR CB C 69.4 0.20 1 907 115 115 THR N N 109.0 0.25 1 908 116 116 ALA H H 7.77 0.01 1 909 116 116 ALA HA H 3.84 0.01 1 910 116 116 ALA HB H 1.33 0.01 1 911 116 116 ALA CA C 56.8 0.20 1 912 116 116 ALA CB C 16.1 0.20 1 913 116 116 ALA N N 125.5 0.25 1 914 117 117 PRO HA H 4.37 0.01 1 915 117 117 PRO C C 179.5 0.20 1 916 117 117 PRO CA C 65.8 0.20 1 917 117 117 PRO CB C 30.8 0.20 1 918 118 118 LYS H H 7.26 0.01 1 919 118 118 LYS HA H 4.14 0.01 1 920 118 118 LYS HB2 H 1.87 0.01 2 921 118 118 LYS HG2 H 1.60 0.01 2 922 118 118 LYS HG3 H 1.44 0.01 2 923 118 118 LYS C C 178.3 0.20 1 924 118 118 LYS CA C 57.5 0.20 1 925 118 118 LYS CB C 32.2 0.20 1 926 118 118 LYS N N 115.8 0.25 1 927 119 119 ILE H H 7.69 0.01 1 928 119 119 ILE HA H 3.44 0.01 1 929 119 119 ILE HB H 1.44 0.01 1 930 119 119 ILE HD1 H 0.13 0.01 1 931 119 119 ILE HG12 H 0.75 0.01 2 932 119 119 ILE HG2 H 0.62 0.01 1 933 119 119 ILE C C 177.5 0.20 1 934 119 119 ILE CA C 64.4 0.20 1 935 119 119 ILE CB C 38.7 0.20 1 936 119 119 ILE N N 119.3 0.25 1 937 120 120 PHE H H 8.04 0.01 1 938 120 120 PHE HA H 4.31 0.01 1 939 120 120 PHE HB2 H 3.27 0.01 2 940 120 120 PHE HB3 H 2.79 0.01 2 941 120 120 PHE C C 176.8 0.20 1 942 120 120 PHE CA C 58.9 0.20 1 943 120 120 PHE CB C 38.4 0.20 1 944 120 120 PHE N N 115.8 0.25 1 945 121 121 GLY H H 7.66 0.01 1 946 121 121 GLY HA2 H 3.83 0.01 2 947 121 121 GLY HA3 H 4.35 0.01 2 948 121 121 GLY C C 174.7 0.20 1 949 121 121 GLY CA C 45.3 0.20 1 950 121 121 GLY N N 106.8 0.25 1 951 122 122 GLY H H 7.62 0.01 1 952 122 122 GLY HA2 H 4.00 0.01 2 953 122 122 GLY HA3 H 4.32 0.01 2 954 122 122 GLY C C 173.8 0.20 1 955 122 122 GLY CA C 44.8 0.20 1 956 122 122 GLY N N 108.4 0.25 1 957 123 123 GLU H H 8.49 0.01 1 958 123 123 GLU HA H 4.16 0.01 1 959 123 123 GLU HB2 H 2.00 0.01 2 960 123 123 GLU HB3 H 2.12 0.01 2 961 123 123 GLU HG2 H 2.33 0.01 2 962 123 123 GLU C C 177.7 0.20 1 963 123 123 GLU CA C 57.9 0.20 1 964 123 123 GLU CB C 30.4 0.20 1 965 123 123 GLU N N 117.7 0.25 1 966 124 124 ILE H H 7.89 0.01 1 967 124 124 ILE HA H 4.09 0.01 1 968 124 124 ILE HB H 1.83 0.01 1 969 124 124 ILE HD1 H 0.81 0.01 1 970 124 124 ILE HG12 H 1.59 0.01 2 971 124 124 ILE HG2 H 0.92 0.01 1 972 124 124 ILE C C 176.7 0.20 1 973 124 124 ILE CA C 62.0 0.20 1 974 124 124 ILE CB C 37.5 0.20 1 975 124 124 ILE N N 119.9 0.25 1 976 125 125 LYS H H 8.60 0.01 1 977 125 125 LYS HA H 4.59 0.01 1 978 125 125 LYS HB2 H 1.80 0.01 2 979 125 125 LYS HG2 H 1.57 0.01 2 980 125 125 LYS C C 174.4 0.20 1 981 125 125 LYS CA C 55.6 0.20 1 982 125 125 LYS CB C 33.0 0.20 1 983 125 125 LYS N N 125.5 0.25 1 984 126 126 THR H H 6.86 0.01 1 985 126 126 THR HA H 4.94 0.01 1 986 126 126 THR HB H 4.06 0.01 1 987 126 126 THR HG2 H 0.91 0.01 1 988 126 126 THR C C 172.0 0.20 1 989 126 126 THR CA C 62.1 0.20 1 990 126 126 THR CB C 69.7 0.20 1 991 126 126 THR N N 116.2 0.25 1 992 127 127 HIS H H 8.87 0.01 1 993 127 127 HIS HA H 5.47 0.01 1 994 127 127 HIS HB2 H 2.81 0.01 2 995 127 127 HIS C C 173.6 0.20 1 996 127 127 HIS CA C 53.7 0.20 1 997 127 127 HIS CB C 35.3 0.20 1 998 127 127 HIS N N 125.9 0.25 1 999 128 128 ILE H H 9.20 0.01 1 1000 128 128 ILE HA H 4.89 0.01 1 1001 128 128 ILE HB H 1.39 0.01 1 1002 128 128 ILE HD1 H -0.24 0.01 1 1003 128 128 ILE HG2 H 0.92 0.01 1 1004 128 128 ILE C C 171.1 0.20 1 1005 128 128 ILE CA C 58.9 0.20 1 1006 128 128 ILE CB C 40.2 0.20 1 1007 128 128 ILE N N 122.6 0.25 1 1008 129 129 LEU H H 9.07 0.01 1 1009 129 129 LEU HA H 5.04 0.01 1 1010 129 129 LEU HB2 H 1.17 0.01 2 1011 129 129 LEU HD1 H 0.82 0.01 2 1012 129 129 LEU HD2 H 0.55 0.01 2 1013 129 129 LEU HG H 1.07 0.01 1 1014 129 129 LEU C C 174.3 0.20 1 1015 129 129 LEU CA C 53.4 0.20 1 1016 129 129 LEU CB C 43.6 0.20 1 1017 129 129 LEU N N 128.8 0.25 1 1018 130 130 LEU H H 8.68 0.01 1 1019 130 130 LEU HA H 4.64 0.01 1 1020 130 130 LEU HB2 H 0.85 0.01 2 1021 130 130 LEU HD1 H 0.14 0.01 2 1022 130 130 LEU HD2 H -0.13 0.01 2 1023 130 130 LEU HG H 0.53 0.01 1 1024 130 130 LEU C C 174.4 0.20 1 1025 130 130 LEU CA C 52.7 0.20 1 1026 130 130 LEU CB C 41.6 0.20 1 1027 130 130 LEU N N 123.2 0.25 1 1028 131 131 PHE H H 9.10 0.01 1 1029 131 131 PHE HA H 4.63 0.01 1 1030 131 131 PHE HB2 H 3.11 0.01 2 1031 131 131 PHE HB3 H 2.81 0.01 2 1032 131 131 PHE C C 173.6 0.20 1 1033 131 131 PHE CA C 56.8 0.20 1 1034 131 131 PHE CB C 39.2 0.20 1 1035 131 131 PHE N N 127.5 0.25 1 1036 132 132 LEU H H 9.00 0.01 1 1037 132 132 LEU HA H 5.02 0.01 1 1038 132 132 LEU HB2 H 1.98 0.01 2 1039 132 132 LEU HD1 H 0.69 0.01 2 1040 132 132 LEU HD2 H 0.15 0.01 2 1041 132 132 LEU CA C 50.7 0.20 1 1042 132 132 LEU CB C 44.4 0.20 1 1043 132 132 LEU N N 127.1 0.25 1 1044 133 133 PRO HA H 4.77 0.01 1 1045 133 133 PRO C C 179.1 0.20 1 1046 133 133 PRO CA C 62.3 0.20 1 1047 133 133 PRO CB C 31.6 0.20 1 1048 134 134 LYS H H 8.30 0.01 1 1049 134 134 LYS HA H 4.07 0.01 1 1050 134 134 LYS HB2 H 1.88 0.01 2 1051 134 134 LYS HB3 H 1.72 0.01 2 1052 134 134 LYS HG2 H 1.52 0.01 2 1053 134 134 LYS C C 176.7 0.20 1 1054 134 134 LYS CA C 58.9 0.20 1 1055 134 134 LYS CB C 32.0 0.20 1 1056 134 134 LYS N N 123.9 0.25 1 1057 135 135 SER H H 7.61 0.01 1 1058 135 135 SER HA H 4.25 0.01 1 1059 135 135 SER HB2 H 3.77 0.01 2 1060 135 135 SER C C 175.2 0.20 1 1061 135 135 SER CA C 58.2 0.20 1 1062 135 135 SER CB C 63.3 0.20 1 1063 135 135 SER N N 108.2 0.25 1 1064 136 136 VAL H H 7.50 0.01 1 1065 136 136 VAL HA H 4.21 0.01 1 1066 136 136 VAL HB H 2.25 0.01 1 1067 136 136 VAL HG1 H 1.22 0.01 2 1068 136 136 VAL HG2 H 1.08 0.01 2 1069 136 136 VAL C C 175.1 0.20 1 1070 136 136 VAL CA C 61.9 0.20 1 1071 136 136 VAL CB C 32.6 0.20 1 1072 136 136 VAL N N 122.8 0.25 1 1073 137 137 SER H H 8.45 0.01 1 1074 137 137 SER HA H 4.30 0.01 1 1075 137 137 SER HB2 H 3.91 0.01 2 1076 137 137 SER C C 175.2 0.20 1 1077 137 137 SER CA C 59.7 0.20 1 1078 137 137 SER CB C 63.0 0.20 1 1079 137 137 SER N N 120.8 0.25 1 1080 138 138 ASP H H 8.98 0.01 1 1081 138 138 ASP HA H 4.63 0.01 1 1082 138 138 ASP HB2 H 2.79 0.01 2 1083 138 138 ASP HB3 H 2.51 0.01 2 1084 138 138 ASP C C 174.8 0.20 1 1085 138 138 ASP CA C 54.0 0.20 1 1086 138 138 ASP CB C 39.3 0.20 1 1087 138 138 ASP N N 122.4 0.25 1 1088 139 139 TYR H H 7.62 0.01 1 1089 139 139 TYR HA H 3.53 0.01 1 1090 139 139 TYR HB2 H 3.21 0.01 2 1091 139 139 TYR HB3 H 2.93 0.01 2 1092 139 139 TYR C C 176.4 0.20 1 1093 139 139 TYR CA C 62.8 0.20 1 1094 139 139 TYR CB C 39.1 0.20 1 1095 139 139 TYR N N 120.5 0.25 1 1096 140 140 ASP H H 8.69 0.01 1 1097 140 140 ASP HA H 4.21 0.01 1 1098 140 140 ASP HB2 H 2.64 0.01 2 1099 140 140 ASP C C 179.3 0.20 1 1100 140 140 ASP CA C 57.2 0.20 1 1101 140 140 ASP CB C 40.4 0.20 1 1102 140 140 ASP N N 115.2 0.25 1 1103 141 141 GLY H H 7.80 0.01 1 1104 141 141 GLY HA2 H 3.80 0.01 2 1105 141 141 GLY HA3 H 4.07 0.01 2 1106 141 141 GLY C C 176.8 0.20 1 1107 141 141 GLY CA C 47.0 0.20 1 1108 141 141 GLY N N 110.3 0.25 1 1109 142 142 LYS H H 8.01 0.01 1 1110 142 142 LYS HA H 4.03 0.01 1 1111 142 142 LYS HB2 H 1.73 0.01 2 1112 142 142 LYS HG2 H 1.46 0.01 2 1113 142 142 LYS C C 179.0 0.20 1 1114 142 142 LYS CA C 59.7 0.20 1 1115 142 142 LYS CB C 33.0 0.20 1 1116 142 142 LYS N N 123.2 0.25 1 1117 143 143 LEU H H 8.09 0.01 1 1118 143 143 LEU HA H 3.76 0.01 1 1119 143 143 LEU HB2 H 1.51 0.01 2 1120 143 143 LEU HD1 H 0.37 0.01 2 1121 143 143 LEU HD2 H 0.14 0.01 2 1122 143 143 LEU HG H 0.81 0.01 1 1123 143 143 LEU C C 179.0 0.20 1 1124 143 143 LEU CA C 57.5 0.20 1 1125 143 143 LEU CB C 40.6 0.20 1 1126 143 143 LEU N N 120.0 0.25 1 1127 144 144 SER H H 8.35 0.01 1 1128 144 144 SER HA H 4.12 0.01 1 1129 144 144 SER HB2 H 4.06 0.01 2 1130 144 144 SER C C 177.3 0.20 1 1131 144 144 SER CA C 61.9 0.20 1 1132 144 144 SER CB C 62.3 0.20 1 1133 144 144 SER N N 114.6 0.25 1 1134 145 145 ASN H H 7.98 0.01 1 1135 145 145 ASN HA H 4.46 0.01 1 1136 145 145 ASN HB2 H 3.17 0.01 2 1137 145 145 ASN HB3 H 2.56 0.01 2 1138 145 145 ASN C C 176.3 0.20 1 1139 145 145 ASN CA C 56.6 0.20 1 1140 145 145 ASN CB C 38.6 0.20 1 1141 145 145 ASN N N 121.6 0.25 1 1142 146 146 PHE H H 7.71 0.01 1 1143 146 146 PHE HA H 4.37 0.01 1 1144 146 146 PHE HB2 H 3.31 0.01 2 1145 146 146 PHE HB3 H 3.17 0.01 2 1146 146 146 PHE C C 176.2 0.20 1 1147 146 146 PHE CA C 61.5 0.20 1 1148 146 146 PHE CB C 40.5 0.20 1 1149 146 146 PHE N N 121.8 0.25 1 1150 147 147 LYS H H 8.51 0.01 1 1151 147 147 LYS HA H 3.62 0.01 1 1152 147 147 LYS HB2 H 1.96 0.01 2 1153 147 147 LYS HB3 H 1.86 0.01 2 1154 147 147 LYS HG2 H 1.48 0.01 2 1155 147 147 LYS C C 178.2 0.20 1 1156 147 147 LYS CA C 59.6 0.20 1 1157 147 147 LYS CB C 32.4 0.20 1 1158 147 147 LYS N N 117.7 0.25 1 1159 148 148 THR H H 8.28 0.01 1 1160 148 148 THR HA H 3.87 0.01 1 1161 148 148 THR HB H 4.23 0.01 1 1162 148 148 THR HG2 H 1.14 0.01 1 1163 148 148 THR C C 177.2 0.20 1 1164 148 148 THR CA C 66.6 0.20 1 1165 148 148 THR CB C 68.2 0.20 1 1166 148 148 THR N N 116.2 0.25 1 1167 149 149 ALA H H 7.57 0.01 1 1168 149 149 ALA HA H 4.03 0.01 1 1169 149 149 ALA HB H 1.65 0.01 1 1170 149 149 ALA C C 177.7 0.20 1 1171 149 149 ALA CA C 54.9 0.20 1 1172 149 149 ALA CB C 18.7 0.20 1 1173 149 149 ALA N N 124.0 0.25 1 1174 150 150 ALA H H 7.36 0.01 1 1175 150 150 ALA HA H 1.86 0.01 1 1176 150 150 ALA HB H 0.66 0.01 1 1177 150 150 ALA C C 180.6 0.20 1 1178 150 150 ALA CA C 53.9 0.20 1 1179 150 150 ALA CB C 19.5 0.20 1 1180 150 150 ALA N N 119.7 0.25 1 1181 151 151 GLU H H 7.05 0.01 1 1182 151 151 GLU HA H 3.68 0.01 1 1183 151 151 GLU HB2 H 2.06 0.01 2 1184 151 151 GLU HG2 H 2.26 0.01 2 1185 151 151 GLU HG3 H 2.50 0.01 2 1186 151 151 GLU C C 178.5 0.20 1 1187 151 151 GLU CA C 59.0 0.20 1 1188 151 151 GLU CB C 30.0 0.20 1 1189 151 151 GLU N N 114.2 0.25 1 1190 152 152 SER H H 7.51 0.01 1 1191 152 152 SER HA H 4.16 0.01 1 1192 152 152 SER HB2 H 3.16 0.01 2 1193 152 152 SER HB3 H 3.53 0.01 2 1194 152 152 SER C C 173.4 0.20 1 1195 152 152 SER CA C 60.6 0.20 1 1196 152 152 SER CB C 63.5 0.20 1 1197 152 152 SER N N 111.9 0.25 1 1198 153 153 PHE H H 7.24 0.01 1 1199 153 153 PHE HA H 4.75 0.01 1 1200 153 153 PHE HB2 H 2.59 0.01 2 1201 153 153 PHE HB3 H 3.61 0.01 2 1202 153 153 PHE C C 174.6 0.20 1 1203 153 153 PHE CA C 57.2 0.20 1 1204 153 153 PHE CB C 41.3 0.20 1 1205 153 153 PHE N N 115.8 0.25 1 1206 154 154 LYS H H 7.32 0.01 1 1207 154 154 LYS HA H 4.38 0.01 1 1208 154 154 LYS HB2 H 1.65 0.01 2 1209 154 154 LYS HB3 H 1.77 0.01 2 1210 154 154 LYS HG2 H 1.34 0.01 2 1211 154 154 LYS HG3 H 1.50 0.01 2 1212 154 154 LYS C C 178.2 0.20 1 1213 154 154 LYS CA C 58.5 0.20 1 1214 154 154 LYS CB C 31.9 0.20 1 1215 154 154 LYS N N 124.0 0.25 1 1216 155 155 GLY H H 9.72 0.01 1 1217 155 155 GLY HA2 H 3.62 0.01 2 1218 155 155 GLY HA3 H 4.29 0.01 2 1219 155 155 GLY C C 173.2 0.20 1 1220 155 155 GLY CA C 45.5 0.20 1 1221 155 155 GLY N N 115.4 0.25 1 1222 156 156 LYS H H 8.40 0.01 1 1223 156 156 LYS HA H 4.63 0.01 1 1224 156 156 LYS HB2 H 1.85 0.01 2 1225 156 156 LYS HB3 H 1.98 0.01 2 1226 156 156 LYS HG2 H 1.49 0.01 2 1227 156 156 LYS C C 175.0 0.20 1 1228 156 156 LYS CA C 57.1 0.20 1 1229 156 156 LYS CB C 35.8 0.20 1 1230 156 156 LYS N N 118.7 0.25 1 1231 157 157 ILE H H 7.89 0.01 1 1232 157 157 ILE HA H 4.33 0.01 1 1233 157 157 ILE HB H 1.60 0.01 1 1234 157 157 ILE HD1 H 0.40 0.01 1 1235 157 157 ILE HG2 H 0.89 0.01 1 1236 157 157 ILE C C 175.0 0.20 1 1237 157 157 ILE CA C 60.4 0.20 1 1238 157 157 ILE CB C 43.6 0.20 1 1239 157 157 ILE N N 116.6 0.25 1 1240 158 158 LEU H H 8.30 0.01 1 1241 158 158 LEU HA H 4.84 0.01 1 1242 158 158 LEU HB2 H 1.57 0.01 2 1243 158 158 LEU HB3 H 1.75 0.01 2 1244 158 158 LEU HD1 H 0.82 0.01 2 1245 158 158 LEU HD2 H 0.97 0.01 2 1246 158 158 LEU C C 175.0 0.20 1 1247 158 158 LEU CA C 54.5 0.20 1 1248 158 158 LEU CB C 43.3 0.20 1 1249 158 158 LEU N N 129.8 0.25 1 1250 159 159 PHE H H 9.31 0.01 1 1251 159 159 PHE HA H 4.89 0.01 1 1252 159 159 PHE HB2 H 2.22 0.01 2 1253 159 159 PHE HB3 H 3.52 0.01 2 1254 159 159 PHE C C 178.5 0.20 1 1255 159 159 PHE CA C 56.6 0.20 1 1256 159 159 PHE CB C 39.1 0.20 1 1257 159 159 PHE N N 130.0 0.25 1 1258 160 160 ILE H H 9.13 0.01 1 1259 160 160 ILE HA H 5.47 0.01 1 1260 160 160 ILE HB H 1.72 0.01 1 1261 160 160 ILE HD1 H 0.82 0.01 1 1262 160 160 ILE HG2 H 0.92 0.01 1 1263 160 160 ILE C C 174.5 0.20 1 1264 160 160 ILE CA C 58.7 0.20 1 1265 160 160 ILE CB C 42.0 0.20 1 1266 160 160 ILE N N 124.1 0.25 1 1267 161 161 PHE H H 8.92 0.01 1 1268 161 161 PHE HA H 5.78 0.01 1 1269 161 161 PHE HB2 H 2.64 0.01 2 1270 161 161 PHE HB3 H 2.85 0.01 2 1271 161 161 PHE C C 172.8 0.20 1 1272 161 161 PHE CA C 54.5 0.20 1 1273 161 161 PHE CB C 42.7 0.20 1 1274 161 161 PHE N N 122.6 0.25 1 1275 162 162 ILE H H 8.78 0.01 1 1276 162 162 ILE HA H 4.31 0.01 1 1277 162 162 ILE HD1 H 0.48 0.01 1 1278 162 162 ILE HG2 H 1.15 0.01 1 1279 162 162 ILE C C 174.0 0.20 1 1280 162 162 ILE CA C 59.6 0.20 1 1281 162 162 ILE CB C 42.3 0.20 1 1282 162 162 ILE N N 121.4 0.25 1 1283 163 163 ASP H H 8.41 0.01 1 1284 163 163 ASP HA H 5.37 0.01 1 1285 163 163 ASP HB2 H 2.80 0.01 2 1286 163 163 ASP HB3 H 3.05 0.01 2 1287 163 163 ASP C C 178.3 0.20 1 1288 163 163 ASP CA C 52.6 0.20 1 1289 163 163 ASP CB C 40.5 0.20 1 1290 163 163 ASP N N 123.8 0.25 1 1291 164 164 SER H H 7.47 0.01 1 1292 164 164 SER HA H 3.99 0.01 1 1293 164 164 SER HB2 H 3.59 0.01 2 1294 164 164 SER HB3 H 4.44 0.01 2 1295 164 164 SER C C 173.9 0.20 1 1296 164 164 SER CA C 60.5 0.20 1 1297 164 164 SER CB C 64.5 0.20 1 1298 164 164 SER N N 124.0 0.25 1 1299 165 165 ASP H H 8.36 0.01 1 1300 165 165 ASP HA H 4.67 0.01 1 1301 165 165 ASP HB2 H 2.70 0.01 2 1302 165 165 ASP HB3 H 3.33 0.01 2 1303 165 165 ASP C C 177.4 0.20 1 1304 165 165 ASP CA C 55.6 0.20 1 1305 165 165 ASP CB C 41.3 0.20 1 1306 165 165 ASP N N 119.3 0.25 1 1307 166 166 HIS H H 7.26 0.01 1 1308 166 166 HIS HA H 4.40 0.01 1 1309 166 166 HIS HB2 H 3.18 0.01 2 1310 166 166 HIS CA C 58.3 0.20 1 1311 166 166 HIS CB C 31.9 0.20 1 1312 166 166 HIS N N 121.4 0.25 1 1313 167 167 THR HA H 4.05 0.01 1 1314 167 167 THR HB H 4.16 0.01 1 1315 167 167 THR HG2 H 1.29 0.01 1 1316 167 167 THR C C 176.8 0.20 1 1317 167 167 THR CA C 66.0 0.20 1 1318 167 167 THR CB C 68.6 0.20 1 1319 168 168 ASP H H 11.03 0.01 1 1320 168 168 ASP HA H 4.64 0.01 1 1321 168 168 ASP HB2 H 2.62 0.01 2 1322 168 168 ASP HB3 H 2.80 0.01 2 1323 168 168 ASP C C 177.5 0.20 1 1324 168 168 ASP CA C 56.8 0.20 1 1325 168 168 ASP CB C 39.8 0.20 1 1326 168 168 ASP N N 124.9 0.25 1 1327 169 169 ASN H H 7.97 0.01 1 1328 169 169 ASN HA H 5.26 0.01 1 1329 169 169 ASN HB2 H 2.73 0.01 2 1330 169 169 ASN HB3 H 2.88 0.01 2 1331 169 169 ASN C C 176.1 0.20 1 1332 169 169 ASN CA C 52.7 0.20 1 1333 169 169 ASN CB C 38.6 0.20 1 1334 169 169 ASN N N 114.6 0.25 1 1335 170 170 GLN H H 7.66 0.01 1 1336 170 170 GLN HA H 4.02 0.01 1 1337 170 170 GLN HB2 H 2.27 0.01 2 1338 170 170 GLN HG2 H 2.54 0.01 2 1339 170 170 GLN C C 178.1 0.20 1 1340 170 170 GLN CA C 59.5 0.20 1 1341 170 170 GLN CB C 28.0 0.20 1 1342 170 170 GLN N N 121.4 0.25 1 1343 171 171 ARG H H 8.57 0.01 1 1344 171 171 ARG HA H 4.25 0.01 1 1345 171 171 ARG HB2 H 1.94 0.01 2 1346 171 171 ARG HG2 H 1.67 0.01 2 1347 171 171 ARG C C 178.7 0.20 1 1348 171 171 ARG CA C 58.7 0.20 1 1349 171 171 ARG CB C 29.1 0.20 1 1350 171 171 ARG N N 117.5 0.25 1 1351 172 172 ILE H H 7.70 0.01 1 1352 172 172 ILE HA H 4.01 0.01 1 1353 172 172 ILE HB H 1.96 0.01 1 1354 172 172 ILE HD1 H 0.96 0.01 1 1355 172 172 ILE HG2 H 1.43 0.01 1 1356 172 172 ILE C C 177.6 0.20 1 1357 172 172 ILE CA C 63.3 0.20 1 1358 172 172 ILE CB C 37.0 0.20 1 1359 172 172 ILE N N 121.0 0.25 1 1360 173 173 LEU H H 7.40 0.01 1 1361 173 173 LEU HA H 3.74 0.01 1 1362 173 173 LEU HB2 H 1.78 0.01 2 1363 173 173 LEU HD1 H 0.60 0.01 2 1364 173 173 LEU HD2 H 0.87 0.01 2 1365 173 173 LEU HG H 1.46 0.01 1 1366 173 173 LEU C C 179.5 0.20 1 1367 173 173 LEU CA C 60.5 0.20 1 1368 173 173 LEU CB C 40.5 0.20 1 1369 173 173 LEU N N 121.4 0.25 1 1370 174 174 GLU H H 8.03 0.01 1 1371 174 174 GLU HA H 4.00 0.01 1 1372 174 174 GLU HB2 H 2.10 0.01 2 1373 174 174 GLU HB3 H 2.26 0.01 2 1374 174 174 GLU HG2 H 2.44 0.01 2 1375 174 174 GLU C C 180.2 0.20 1 1376 174 174 GLU CA C 59.2 0.20 1 1377 174 174 GLU CB C 29.3 0.20 1 1378 174 174 GLU N N 117.2 0.25 1 1379 175 175 PHE H H 8.00 0.01 1 1380 175 175 PHE HA H 4.15 0.01 1 1381 175 175 PHE HB2 H 3.11 0.01 2 1382 175 175 PHE HB3 H 3.23 0.01 2 1383 175 175 PHE C C 176.4 0.20 1 1384 175 175 PHE CA C 60.8 0.20 1 1385 175 175 PHE CB C 38.7 0.20 1 1386 175 175 PHE N N 122.0 0.25 1 1387 176 176 PHE H H 7.51 0.01 1 1388 176 176 PHE HA H 4.11 0.01 1 1389 176 176 PHE HB2 H 2.61 0.01 2 1390 176 176 PHE HB3 H 3.21 0.01 2 1391 176 176 PHE C C 175.0 0.20 1 1392 176 176 PHE CA C 59.3 0.20 1 1393 176 176 PHE CB C 40.0 0.20 1 1394 176 176 PHE N N 113.1 0.25 1 1395 177 177 GLY H H 8.03 0.01 1 1396 177 177 GLY HA2 H 3.85 0.01 2 1397 177 177 GLY C C 173.9 0.20 1 1398 177 177 GLY CA C 46.5 0.20 1 1399 177 177 GLY N N 110.9 0.25 1 1400 178 178 LEU H H 7.73 0.01 1 1401 178 178 LEU HA H 4.44 0.01 1 1402 178 178 LEU HB2 H 1.02 0.01 2 1403 178 178 LEU HD1 H -0.13 0.01 2 1404 178 178 LEU HD2 H 0.35 0.01 2 1405 178 178 LEU HG H 0.86 0.01 1 1406 178 178 LEU C C 175.8 0.20 1 1407 178 178 LEU CA C 53.5 0.20 1 1408 178 178 LEU CB C 45.9 0.20 1 1409 178 178 LEU N N 120.7 0.25 1 1410 179 179 LYS H H 8.17 0.01 1 1411 179 179 LYS HA H 4.53 0.01 1 1412 179 179 LYS HB3 H 2.07 0.01 2 1413 179 179 LYS HG2 H 1.44 0.01 2 1414 179 179 LYS C C 178.5 0.20 1 1415 179 179 LYS CA C 54.0 0.20 1 1416 179 179 LYS CB C 34.1 0.20 1 1417 179 179 LYS N N 119.5 0.25 1 1418 180 180 LYS H H 9.11 0.01 1 1419 180 180 LYS HA H 3.82 0.01 1 1420 180 180 LYS HB2 H 1.75 0.01 2 1421 180 180 LYS HB3 H 1.91 0.01 2 1422 180 180 LYS HG2 H 1.53 0.01 2 1423 180 180 LYS C C 179.6 0.20 1 1424 180 180 LYS CA C 60.9 0.20 1 1425 180 180 LYS CB C 32.1 0.20 1 1426 180 180 LYS N N 124.2 0.25 1 1427 181 181 GLU H H 9.46 0.01 1 1428 181 181 GLU HA H 4.22 0.01 1 1429 181 181 GLU HB2 H 2.07 0.01 2 1430 181 181 GLU HG2 H 2.29 0.01 2 1431 181 181 GLU C C 176.7 0.20 1 1432 181 181 GLU CA C 58.7 0.20 1 1433 181 181 GLU CB C 28.3 0.20 1 1434 181 181 GLU N N 116.6 0.25 1 1435 182 182 GLU H H 7.66 0.01 1 1436 182 182 GLU HA H 4.32 0.01 1 1437 182 182 GLU HB2 H 2.07 0.01 2 1438 182 182 GLU HG2 H 2.22 0.01 2 1439 182 182 GLU C C 174.9 0.20 1 1440 182 182 GLU CA C 55.7 0.20 1 1441 182 182 GLU CB C 30.6 0.20 1 1442 182 182 GLU N N 118.3 0.25 1 1443 183 183 CYS H H 7.09 0.01 1 1444 183 183 CYS HA H 4.27 0.01 1 1445 183 183 CYS HB2 H 2.54 0.01 2 1446 183 183 CYS HB3 H 3.00 0.01 2 1447 183 183 CYS CA C 58.2 0.20 1 1448 183 183 CYS CB C 27.4 0.20 1 1449 183 183 CYS N N 117.7 0.25 1 1450 184 184 PRO HA H 5.37 0.01 1 1451 184 184 PRO C C 174.3 0.20 1 1452 184 184 PRO CA C 61.5 0.20 1 1453 184 184 PRO CB C 36.0 0.20 1 1454 185 185 ALA H H 8.37 0.01 1 1455 185 185 ALA HA H 4.79 0.01 1 1456 185 185 ALA HB H 1.39 0.01 1 1457 185 185 ALA C C 174.8 0.20 1 1458 185 185 ALA CA C 51.6 0.20 1 1459 185 185 ALA CB C 23.4 0.20 1 1460 185 185 ALA N N 123.0 0.25 1 1461 186 186 VAL H H 8.66 0.01 1 1462 186 186 VAL HA H 5.71 0.01 1 1463 186 186 VAL HB H 1.70 0.01 1 1464 186 186 VAL HG1 H 0.81 0.01 2 1465 186 186 VAL C C 176.5 0.20 1 1466 186 186 VAL CA C 59.3 0.20 1 1467 186 186 VAL CB C 35.3 0.20 1 1468 186 186 VAL N N 117.9 0.25 1 1469 187 187 ARG H H 8.91 0.01 1 1470 187 187 ARG HA H 5.00 0.01 1 1471 187 187 ARG HB2 H 1.72 0.01 2 1472 187 187 ARG HG2 H 1.39 0.01 2 1473 187 187 ARG C C 172.6 0.20 1 1474 187 187 ARG CA C 53.0 0.20 1 1475 187 187 ARG CB C 35.9 0.20 1 1476 187 187 ARG N N 123.0 0.25 1 1477 188 188 LEU H H 8.79 0.01 1 1478 188 188 LEU HA H 5.42 0.01 1 1479 188 188 LEU HB2 H 1.38 0.01 2 1480 188 188 LEU HD1 H -0.44 0.01 2 1481 188 188 LEU HD2 H -0.24 0.01 2 1482 188 188 LEU HG H 1.18 0.01 1 1483 188 188 LEU C C 174.6 0.20 1 1484 188 188 LEU CA C 54.3 0.20 1 1485 188 188 LEU CB C 47.3 0.20 1 1486 188 188 LEU N N 124.7 0.25 1 1487 189 189 ILE H H 9.59 0.01 1 1488 189 189 ILE HA H 5.88 0.01 1 1489 189 189 ILE HB H 1.96 0.01 1 1490 189 189 ILE HD1 H 0.92 0.01 1 1491 189 189 ILE HG2 H 1.15 0.01 1 1492 189 189 ILE C C 173.5 0.20 1 1493 189 189 ILE CA C 58.4 0.20 1 1494 189 189 ILE CB C 43.0 0.20 1 1495 189 189 ILE N N 121.8 0.25 1 1496 190 190 THR H H 8.75 0.01 1 1497 190 190 THR HA H 5.36 0.01 1 1498 190 190 THR HB H 4.32 0.01 1 1499 190 190 THR HG2 H 1.40 0.01 1 1500 190 190 THR C C 174.3 0.20 1 1501 190 190 THR CA C 58.8 0.20 1 1502 190 190 THR CB C 70.4 0.20 1 1503 190 190 THR N N 114.2 0.25 1 1504 191 191 LEU H H 8.61 0.01 1 1505 191 191 LEU HA H 4.64 0.01 1 1506 191 191 LEU HB2 H 1.82 0.01 2 1507 191 191 LEU HD1 H 0.89 0.01 2 1508 191 191 LEU HG H 1.65 0.01 1 1509 191 191 LEU C C 176.4 0.20 1 1510 191 191 LEU CA C 54.5 0.20 1 1511 191 191 LEU CB C 42.3 0.20 1 1512 191 191 LEU N N 125.5 0.25 1 1513 192 192 GLU H H 7.54 0.01 1 1514 192 192 GLU HA H 4.51 0.01 1 1515 192 192 GLU HB2 H 2.09 0.01 2 1516 192 192 GLU HG2 H 2.29 0.01 2 1517 192 192 GLU C C 176.1 0.20 1 1518 192 192 GLU CA C 56.3 0.20 1 1519 192 192 GLU CB C 29.8 0.20 1 1520 192 192 GLU N N 123.4 0.25 1 1521 193 193 GLU H H 8.49 0.01 1 1522 193 193 GLU HA H 4.15 0.01 1 1523 193 193 GLU HB2 H 2.12 0.01 2 1524 193 193 GLU HG2 H 2.30 0.01 2 1525 193 193 GLU C C 176.7 0.20 1 1526 193 193 GLU CA C 59.2 0.20 1 1527 193 193 GLU CB C 29.0 0.20 1 1528 193 193 GLU N N 122.4 0.25 1 1529 194 194 GLU H H 7.99 0.01 1 1530 194 194 GLU HA H 4.46 0.01 1 1531 194 194 GLU HB2 H 1.90 0.01 2 1532 194 194 GLU HB3 H 2.08 0.01 2 1533 194 194 GLU HG2 H 2.21 0.01 2 1534 194 194 GLU C C 175.7 0.20 1 1535 194 194 GLU CA C 54.9 0.20 1 1536 194 194 GLU CB C 31.4 0.20 1 1537 194 194 GLU N N 116.2 0.25 1 1538 195 195 MET H H 8.76 0.01 1 1539 195 195 MET HA H 5.05 0.01 1 1540 195 195 MET HB2 H 2.05 0.01 2 1541 195 195 MET HB3 H 2.18 0.01 2 1542 195 195 MET HG2 H 2.42 0.01 2 1543 195 195 MET HG3 H 2.63 0.01 2 1544 195 195 MET C C 175.9 0.20 1 1545 195 195 MET CA C 56.0 0.20 1 1546 195 195 MET CB C 33.2 0.20 1 1547 195 195 MET N N 123.0 0.25 1 1548 196 196 THR H H 8.40 0.01 1 1549 196 196 THR HA H 4.40 0.01 1 1550 196 196 THR HB H 4.14 0.01 1 1551 196 196 THR HG2 H 1.12 0.01 1 1552 196 196 THR C C 172.0 0.20 1 1553 196 196 THR CA C 62.9 0.20 1 1554 196 196 THR CB C 69.8 0.20 1 1555 196 196 THR N N 122.0 0.25 1 1556 197 197 LYS H H 8.53 0.01 1 1557 197 197 LYS HA H 5.42 0.01 1 1558 197 197 LYS HB2 H 1.89 0.01 2 1559 197 197 LYS HG2 H 1.41 0.01 2 1560 197 197 LYS C C 174.7 0.20 1 1561 197 197 LYS CA C 55.0 0.20 1 1562 197 197 LYS CB C 35.6 0.20 1 1563 197 197 LYS N N 123.9 0.25 1 1564 198 198 TYR H H 9.54 0.01 1 1565 198 198 TYR HA H 4.88 0.01 1 1566 198 198 TYR HB2 H 2.88 0.01 2 1567 198 198 TYR HB3 H 2.99 0.01 2 1568 198 198 TYR C C 174.4 0.20 1 1569 198 198 TYR CA C 57.7 0.20 1 1570 198 198 TYR CB C 41.7 0.20 1 1571 198 198 TYR N N 117.9 0.25 1 1572 199 199 LYS H H 9.29 0.01 1 1573 199 199 LYS HA H 5.07 0.01 1 1574 199 199 LYS HB2 H 1.49 0.01 2 1575 199 199 LYS HG2 H 1.34 0.01 2 1576 199 199 LYS HG3 H 1.18 0.01 2 1577 199 199 LYS CA C 52.5 0.20 1 1578 199 199 LYS CB C 35.4 0.20 1 1579 199 199 LYS N N 122.6 0.25 1 1580 200 200 PRO HA H 4.12 0.01 1 1581 200 200 PRO C C 176.7 0.20 1 1582 200 200 PRO CA C 62.0 0.20 1 1583 200 200 PRO CB C 31.2 0.20 1 1584 201 201 GLU H H 9.01 0.01 1 1585 201 201 GLU HA H 4.11 0.01 1 1586 201 201 GLU HB2 H 2.02 0.01 2 1587 201 201 GLU HB3 H 2.19 0.01 2 1588 201 201 GLU HG2 H 2.38 0.01 2 1589 201 201 GLU C C 176.1 0.20 1 1590 201 201 GLU CA C 57.6 0.20 1 1591 201 201 GLU CB C 30.4 0.20 1 1592 201 201 GLU N N 119.7 0.25 1 1593 202 202 SER H H 7.57 0.01 1 1594 202 202 SER HA H 4.65 0.01 1 1595 202 202 SER HB2 H 3.69 0.01 2 1596 202 202 SER HB3 H 3.96 0.01 2 1597 202 202 SER C C 174.4 0.20 1 1598 202 202 SER CA C 56.4 0.20 1 1599 202 202 SER CB C 65.1 0.20 1 1600 202 202 SER N N 111.9 0.25 1 1601 203 203 GLU H H 8.79 0.01 1 1602 203 203 GLU HA H 4.37 0.01 1 1603 203 203 GLU HB2 H 1.87 0.01 2 1604 203 203 GLU HG2 H 2.27 0.01 2 1605 203 203 GLU C C 176.1 0.20 1 1606 203 203 GLU CA C 56.2 0.20 1 1607 203 203 GLU CB C 29.5 0.20 1 1608 203 203 GLU N N 122.8 0.25 1 1609 204 204 GLU H H 8.03 0.01 1 1610 204 204 GLU HA H 4.11 0.01 1 1611 204 204 GLU HB2 H 1.96 0.01 2 1612 204 204 GLU HG2 H 2.28 0.01 2 1613 204 204 GLU C C 176.3 0.20 1 1614 204 204 GLU CA C 57.3 0.20 1 1615 204 204 GLU CB C 31.1 0.20 1 1616 204 204 GLU N N 120.7 0.25 1 1617 205 205 LEU H H 8.69 0.01 1 1618 205 205 LEU HA H 4.58 0.01 1 1619 205 205 LEU HB2 H 1.68 0.01 2 1620 205 205 LEU HD1 H 0.68 0.01 2 1621 205 205 LEU HD2 H 0.76 0.01 2 1622 205 205 LEU HG H 1.54 0.01 1 1623 205 205 LEU C C 176.3 0.20 1 1624 205 205 LEU CA C 53.1 0.20 1 1625 205 205 LEU CB C 41.1 0.20 1 1626 205 205 LEU N N 125.5 0.25 1 1627 206 206 THR H H 6.80 0.01 1 1628 206 206 THR HA H 4.37 0.01 1 1629 206 206 THR HB H 4.72 0.01 1 1630 206 206 THR HG2 H 1.28 0.01 1 1631 206 206 THR C C 175.2 0.20 1 1632 206 206 THR CA C 59.4 0.20 1 1633 206 206 THR CB C 70.4 0.20 1 1634 206 206 THR N N 108.2 0.25 1 1635 207 207 ALA H H 9.32 0.01 1 1636 207 207 ALA HA H 4.01 0.01 1 1637 207 207 ALA HB H 1.55 0.01 1 1638 207 207 ALA C C 180.8 0.20 1 1639 207 207 ALA CA C 56.0 0.20 1 1640 207 207 ALA CB C 18.2 0.20 1 1641 207 207 ALA N N 125.3 0.25 1 1642 208 208 GLU H H 9.39 0.01 1 1643 208 208 GLU HA H 4.05 0.01 1 1644 208 208 GLU HB2 H 1.96 0.01 2 1645 208 208 GLU HB3 H 2.10 0.01 2 1646 208 208 GLU HG2 H 2.35 0.01 2 1647 208 208 GLU C C 179.1 0.20 1 1648 208 208 GLU CA C 60.2 0.20 1 1649 208 208 GLU CB C 29.1 0.20 1 1650 208 208 GLU N N 118.5 0.25 1 1651 209 209 ARG H H 7.70 0.01 1 1652 209 209 ARG HA H 4.23 0.01 1 1653 209 209 ARG HB2 H 1.96 0.01 2 1654 209 209 ARG HG2 H 1.76 0.01 2 1655 209 209 ARG C C 180.0 0.20 1 1656 209 209 ARG CA C 57.9 0.20 1 1657 209 209 ARG CB C 30.1 0.20 1 1658 209 209 ARG N N 119.7 0.25 1 1659 210 210 ILE H H 8.54 0.01 1 1660 210 210 ILE HA H 3.95 0.01 1 1661 210 210 ILE HB H 1.95 0.01 1 1662 210 210 ILE HD1 H 0.91 0.01 1 1663 210 210 ILE HG2 H 1.12 0.01 1 1664 210 210 ILE C C 178.0 0.20 1 1665 210 210 ILE CA C 65.4 0.20 1 1666 210 210 ILE CB C 38.3 0.20 1 1667 210 210 ILE N N 122.0 0.25 1 1668 211 211 THR H H 8.62 0.01 1 1669 211 211 THR HA H 4.04 0.01 1 1670 211 211 THR HB H 4.44 0.01 1 1671 211 211 THR HG2 H 1.48 0.01 1 1672 211 211 THR C C 175.3 0.20 1 1673 211 211 THR CA C 67.8 0.20 1 1674 211 211 THR CB C 68.3 0.20 1 1675 211 211 THR N N 117.1 0.25 1 1676 212 212 GLU H H 8.05 0.01 1 1677 212 212 GLU HA H 4.28 0.01 1 1678 212 212 GLU HB2 H 2.28 0.01 2 1679 212 212 GLU HG2 H 2.44 0.01 2 1680 212 212 GLU C C 177.2 0.20 1 1681 212 212 GLU CA C 59.7 0.20 1 1682 212 212 GLU CB C 30.3 0.20 1 1683 212 212 GLU N N 121.6 0.25 1 1684 213 213 PHE H H 7.89 0.01 1 1685 213 213 PHE HA H 4.62 0.01 1 1686 213 213 PHE HB2 H 3.37 0.01 2 1687 213 213 PHE HB3 H 3.58 0.01 2 1688 213 213 PHE C C 176.3 0.20 1 1689 213 213 PHE CA C 59.3 0.20 1 1690 213 213 PHE CB C 38.7 0.20 1 1691 213 213 PHE N N 119.7 0.25 1 1692 214 214 CYS H H 7.70 0.01 1 1693 214 214 CYS HA H 3.26 0.01 1 1694 214 214 CYS HB2 H 1.03 0.01 2 1695 214 214 CYS HB3 H 2.41 0.01 2 1696 214 214 CYS C C 177.0 0.20 1 1697 214 214 CYS CA C 64.5 0.20 1 1698 214 214 CYS CB C 27.4 0.20 1 1699 214 214 CYS N N 116.0 0.25 1 1700 215 215 HIS H H 8.64 0.01 1 1701 215 215 HIS HA H 4.50 0.01 1 1702 215 215 HIS HB2 H 3.19 0.01 2 1703 215 215 HIS HB3 H 3.33 0.01 2 1704 215 215 HIS C C 178.1 0.20 1 1705 215 215 HIS CA C 60.3 0.20 1 1706 215 215 HIS CB C 30.3 0.20 1 1707 215 215 HIS N N 118.1 0.25 1 1708 216 216 ARG H H 8.73 0.01 1 1709 216 216 ARG HA H 3.92 0.01 1 1710 216 216 ARG HB2 H 2.04 0.01 2 1711 216 216 ARG HG2 H 1.73 0.01 2 1712 216 216 ARG C C 179.1 0.20 1 1713 216 216 ARG CA C 59.8 0.20 1 1714 216 216 ARG CB C 30.1 0.20 1 1715 216 216 ARG N N 118.7 0.25 1 1716 217 217 PHE H H 8.39 0.01 1 1717 217 217 PHE HA H 3.97 0.01 1 1718 217 217 PHE HB2 H 2.30 0.01 2 1719 217 217 PHE HB3 H 2.70 0.01 2 1720 217 217 PHE C C 179.2 0.20 1 1721 217 217 PHE CA C 60.7 0.20 1 1722 217 217 PHE CB C 37.8 0.20 1 1723 217 217 PHE N N 120.6 0.25 1 1724 218 218 LEU H H 8.25 0.01 1 1725 218 218 LEU HA H 3.50 0.01 1 1726 218 218 LEU HB2 H 1.96 0.01 2 1727 218 218 LEU HB3 H 2.13 0.01 2 1728 218 218 LEU HD1 H 0.96 0.01 2 1729 218 218 LEU HD2 H 1.07 0.01 2 1730 218 218 LEU HG H 1.49 0.01 1 1731 218 218 LEU C C 178.8 0.20 1 1732 218 218 LEU CA C 57.4 0.20 1 1733 218 218 LEU CB C 41.3 0.20 1 1734 218 218 LEU N N 123.5 0.25 1 1735 219 219 GLU H H 7.77 0.01 1 1736 219 219 GLU HA H 4.20 0.01 1 1737 219 219 GLU HB2 H 1.98 0.01 2 1738 219 219 GLU HB3 H 2.14 0.01 2 1739 219 219 GLU HG2 H 2.25 0.01 2 1740 219 219 GLU HG3 H 2.43 0.01 2 1741 219 219 GLU C C 176.8 0.20 1 1742 219 219 GLU CA C 56.2 0.20 1 1743 219 219 GLU CB C 30.6 0.20 1 1744 219 219 GLU N N 116.4 0.25 1 1745 220 220 GLY H H 7.72 0.01 1 1746 220 220 GLY HA2 H 3.89 0.01 2 1747 220 220 GLY HA3 H 3.96 0.01 2 1748 220 220 GLY C C 176.3 0.20 1 1749 220 220 GLY CA C 46.3 0.20 1 1750 220 220 GLY N N 108.6 0.25 1 1751 221 221 LYS H H 8.00 0.01 1 1752 221 221 LYS HA H 4.32 0.01 1 1753 221 221 LYS HB2 H 2.13 0.01 2 1754 221 221 LYS HG2 H 1.36 0.01 2 1755 221 221 LYS HG3 H 1.55 0.01 2 1756 221 221 LYS C C 175.9 0.20 1 1757 221 221 LYS CA C 56.1 0.20 1 1758 221 221 LYS CB C 33.7 0.20 1 1759 221 221 LYS N N 116.6 0.25 1 1760 222 222 ILE H H 7.91 0.01 1 1761 222 222 ILE HA H 4.57 0.01 1 1762 222 222 ILE HB H 2.06 0.01 1 1763 222 222 ILE HD1 H 1.02 0.01 1 1764 222 222 ILE HG12 H 1.34 0.01 2 1765 222 222 ILE HG2 H 1.18 0.01 1 1766 222 222 ILE C C 175.4 0.20 1 1767 222 222 ILE CA C 59.2 0.20 1 1768 222 222 ILE CB C 38.8 0.20 1 1769 222 222 ILE N N 118.9 0.25 1 1770 223 223 LYS H H 8.76 0.01 1 1771 223 223 LYS HA H 4.57 0.01 1 1772 223 223 LYS HB2 H 1.81 0.01 2 1773 223 223 LYS HB3 H 2.02 0.01 2 1774 223 223 LYS CA C 54.3 0.20 1 1775 223 223 LYS CB C 32.0 0.20 1 1776 223 223 LYS N N 127.7 0.25 1 1777 224 224 PRO C C 175.9 0.20 1 1778 224 224 PRO CA C 63.0 0.20 1 1779 224 224 PRO CB C 32.3 0.20 1 1780 225 225 HIS H H 8.77 0.01 1 1781 225 225 HIS C C 174.7 0.20 1 1782 225 225 HIS CA C 55.8 0.20 1 1783 225 225 HIS CB C 31.1 0.20 1 1784 225 225 HIS N N 121.8 0.25 1 1785 226 226 LEU H H 8.16 0.01 1 1786 226 226 LEU C C 176.4 0.20 1 1787 226 226 LEU CA C 54.5 0.20 1 1788 226 226 LEU CB C 42.3 0.20 1 1789 226 226 LEU N N 127.0 0.25 1 1790 227 227 MET H H 7.98 0.01 1 1791 227 227 MET C C 175.1 0.20 1 1792 227 227 MET CA C 55.4 0.20 1 1793 227 227 MET CB C 33.0 0.20 1 1794 227 227 MET N N 120.8 0.25 1 1795 228 228 SER H H 7.86 0.01 1 1796 228 228 SER CA C 59.9 0.20 1 1797 228 228 SER CB C 64.6 0.20 1 1798 228 228 SER N N 122.3 0.25 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details ; Extra peaks of second (minor) form of PDI-bb were found just for few N- and C-terminal residues which is probably result of cis-trans isomerization for Pro-6 and Pro-224 residues. Additional 15N and 1H backbone amide chemical shifts are corresponding to (in ppm): LEU-3 (121.4, 8.51), GLY-4 (109.4, 8.19), SER-5 (115.4, 7.83), ILE-222 (118.9, 7.63), LYS-223 (125.5, 8.08), HIS-225 (119.0, 8.33), LEU-226 (123.2, 8.03), MET-227 (121.2, 8.28). ; loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '3D 1H-15N NOESY' '3D HNCO' 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 'bb-PDI monomer, minor conformer' _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 2 2 PRO C C 176.9 0.20 1 2 2 2 PRO CA C 63.3 0.20 1 3 2 2 PRO CB C 32.2 0.20 1 4 3 3 LEU H H 8.51 0.01 1 5 3 3 LEU C C 177.7 0.20 1 6 3 3 LEU CA C 55.3 0.20 1 7 3 3 LEU CB C 42.1 0.20 1 8 3 3 LEU N N 121.4 0.25 1 9 4 4 GLY H H 8.19 0.01 1 10 4 4 GLY C C 172.9 0.20 1 11 4 4 GLY CA C 45.2 0.20 1 12 4 4 GLY N N 109.4 0.25 1 13 5 5 SER H H 7.83 0.01 1 14 5 5 SER CA C 55.5 0.20 1 15 5 5 SER CB C 64.1 0.20 1 16 5 5 SER N N 115.4 0.25 1 17 221 221 LYS C C 176.8 0.20 1 18 221 221 LYS CA C 56.1 0.20 1 19 221 221 LYS CB C 32.5 0.20 1 20 222 222 ILE H H 7.63 0.01 1 21 222 222 ILE C C 175.8 0.20 1 22 222 222 ILE CA C 61.3 0.20 1 23 222 222 ILE CB C 38.5 0.20 1 24 222 222 ILE N N 118.9 0.25 1 25 223 223 LYS H H 8.08 0.01 1 26 223 223 LYS CA C 54.3 0.20 1 27 223 223 LYS CB C 32.4 0.20 1 28 223 223 LYS N N 125.5 0.25 1 29 224 224 PRO C C 176.7 0.20 1 30 224 224 PRO CA C 63.4 0.20 1 31 224 224 PRO CB C 31.8 0.20 1 32 225 225 HIS H H 8.33 0.01 1 33 225 225 HIS C C 175.0 0.20 1 34 225 225 HIS CA C 56.1 0.20 1 35 225 225 HIS CB C 30.3 0.20 1 36 225 225 HIS N N 119.0 0.25 1 37 226 226 LEU H H 8.03 0.01 1 38 226 226 LEU C C 176.8 0.20 1 39 226 226 LEU CA C 55.0 0.20 1 40 226 226 LEU CB C 42.3 0.20 1 41 226 226 LEU N N 123.2 0.25 1 42 227 227 MET H H 8.28 0.01 1 43 227 227 MET CA C 55.3 0.20 1 44 227 227 MET CB C 32.9 0.20 1 45 227 227 MET N N 121.2 0.25 1 stop_ save_