data_4156 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure in Solution of the b Domain of Protein Disulfide Isomerase ; _BMRB_accession_number 4156 _BMRB_flat_file_name bmr4156.str _Entry_type original _Submission_date 1998-07-02 _Accession_date 1998-07-02 _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 Kemmink J. . . 2 Dijkstra K. . . 3 Mariani M. . . 4 Scheek R. M. . 5 Penka E. . . 6 Nilges M. . . 7 Darby N. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 635 "13C chemical shifts" 469 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-06 original author . stop_ _Original_release_date 1999-08-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R.M., Penka, E., Nilges, M., and Darby, N.J., "The Structure in Solution of the b Domain of Protein Disulfide Isomerase," J. Biomol. NMR 13, 357-368 (1999). ; _Citation_title ; The Structure in Solution of the b Domain of Protein Disulfide Isomerase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99309858 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kemmink J. . . 2 Dijkstra K. . . 3 Mariani M. . . 4 Scheek R. M. . 5 Penka E. . . 6 Nilges M. . . 7 Darby N. J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 13 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 357 _Page_last 368 _Year 1999 _Details . loop_ _Keyword 'electron transport' 'endoplasmic reticulum' isomerase 'redox-active center' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_PDI _Saveframe_category molecular_system _Mol_system_name 'Protein Disulfide Isomerase' _Abbreviation_common PDI _Enzyme_commission_number 5.3.4.1 loop_ _Mol_system_component_name _Mol_label PDI $PDI stop_ _System_molecular_weight 12062 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'disulfide bond formation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PDI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Protein Disulfide Isomerase' _Abbreviation_common PDI _Molecular_mass 12062 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; AATTLPDGAAAESLVESSEV AVIGFFKDVESDSAKQFLQA AEAIDDIPFGITSNSDVFSK YQLDKDGVVLFKKFDEGRNN FEGEVTKENLLDFIKHNQLP LVIEFTEQTA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 119 ALA 2 120 ALA 3 121 THR 4 122 THR 5 123 LEU 6 124 PRO 7 125 ASP 8 126 GLY 9 127 ALA 10 128 ALA 11 129 ALA 12 130 GLU 13 131 SER 14 132 LEU 15 133 VAL 16 134 GLU 17 135 SER 18 136 SER 19 137 GLU 20 138 VAL 21 139 ALA 22 140 VAL 23 141 ILE 24 142 GLY 25 143 PHE 26 144 PHE 27 145 LYS 28 146 ASP 29 147 VAL 30 148 GLU 31 149 SER 32 150 ASP 33 151 SER 34 152 ALA 35 153 LYS 36 154 GLN 37 155 PHE 38 156 LEU 39 157 GLN 40 158 ALA 41 159 ALA 42 160 GLU 43 161 ALA 44 162 ILE 45 163 ASP 46 164 ASP 47 165 ILE 48 166 PRO 49 167 PHE 50 168 GLY 51 169 ILE 52 170 THR 53 171 SER 54 172 ASN 55 173 SER 56 174 ASP 57 175 VAL 58 176 PHE 59 177 SER 60 178 LYS 61 179 TYR 62 180 GLN 63 181 LEU 64 182 ASP 65 183 LYS 66 184 ASP 67 185 GLY 68 186 VAL 69 187 VAL 70 188 LEU 71 189 PHE 72 190 LYS 73 191 LYS 74 192 PHE 75 193 ASP 76 194 GLU 77 195 GLY 78 196 ARG 79 197 ASN 80 198 ASN 81 199 PHE 82 200 GLU 83 201 GLY 84 202 GLU 85 203 VAL 86 204 THR 87 205 LYS 88 206 GLU 89 207 ASN 90 208 LEU 91 209 LEU 92 210 ASP 93 211 PHE 94 212 ILE 95 213 LYS 96 214 HIS 97 215 ASN 98 216 GLN 99 217 LEU 100 218 PRO 101 219 LEU 102 220 VAL 103 221 ILE 104 222 GLU 105 223 PHE 106 224 THR 107 225 GLU 108 226 GLN 109 227 THR 110 228 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 15303 bb-PDI 100.00 228 100.00 100.00 7.43e-69 BMRB 15974 "b-b'-x" 100.00 236 100.00 100.00 1.35e-68 PDB 1BJX "Human Protein Disulfide Isomerase, Nmr, 24 Structures" 100.00 110 100.00 100.00 1.99e-70 PDB 2BJX "Protein Disulfide Isomerase" 100.00 110 100.00 100.00 1.99e-70 PDB 2K18 "Solution Structure Of Bb' Domains Of Human Protein Disulfide Isomerase" 100.00 228 100.00 100.00 7.43e-69 PDB 3UEM "Crystal Structure Of Human Pdi Bb'a' Domains" 99.09 361 100.00 100.00 2.44e-66 PDB 4EKZ "Crystal Structure Of Reduced Hpdi (abb'xa')" 100.00 482 100.00 100.00 3.68e-66 PDB 4EL1 "Crystal Structure Of Oxidized Hpdi (abb'xa')" 100.00 482 100.00 100.00 3.68e-66 PDB 4JU5 "Crystal Structure Of The Dimeric Form Of The Bb' Domains Of Human Protein Disulfide Isomerase" 100.00 238 100.00 100.00 1.19e-68 DBJ BAE79726 "protein disulfide isomerase [Macaca fuscata]" 100.00 510 99.09 100.00 6.36e-65 DBJ BAE87231 "unnamed protein product [Macaca fascicularis]" 100.00 510 99.09 100.00 4.77e-65 DBJ BAE88032 "unnamed protein product [Macaca fascicularis]" 100.00 336 98.18 99.09 2.35e-66 DBJ BAG37999 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 DBJ BAG58932 "unnamed protein product [Homo sapiens]" 97.27 242 99.07 100.00 1.05e-66 EMBL CAA28775 "unnamed protein product [Homo sapiens]" 100.00 508 100.00 100.00 7.71e-66 EMBL CAH93050 "hypothetical protein [Pongo abelii]" 100.00 508 98.18 99.09 8.21e-65 GB AAA61169 "thyroid hormone binding protein precursor [Homo sapiens]" 100.00 508 99.09 99.09 1.44e-64 GB AAC13652 "prolyl 4-hydroxylase beta-subunit [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 GB AAH10859 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 GB AAH29617 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 GB AAH71892 "Prolyl 4-hydroxylase, beta polypeptide [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 REF NP_000909 "protein disulfide-isomerase precursor [Homo sapiens]" 100.00 508 100.00 100.00 6.04e-66 REF NP_001126805 "protein disulfide-isomerase precursor [Pongo abelii]" 100.00 508 98.18 99.09 8.21e-65 REF NP_001233358 "protein disulfide-isomerase precursor [Pan troglodytes]" 100.00 508 100.00 100.00 6.17e-66 REF XP_002764185 "PREDICTED: protein disulfide-isomerase isoform X2 [Callithrix jacchus]" 100.00 510 97.27 100.00 2.44e-64 REF XP_003282223 "PREDICTED: protein disulfide-isomerase isoform X1 [Nomascus leucogenys]" 100.00 505 97.27 97.27 6.42e-62 SP P07237 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 100.00 100.00 6.04e-66 SP Q2HWU2 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Prolyl 4-hydroxylase subunit beta; Flags: Precursor" 100.00 510 99.09 100.00 6.36e-65 SP Q5R5B6 "RecName: Full=Protein disulfide-isomerase; Short=PDI; AltName: Full=Cellular thyroid hormone-binding protein; AltName: Full=Pro" 100.00 508 98.18 99.09 8.21e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $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_type _Vector_name $PDI 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PDI . mM 1 2 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'UNITY INOVA' _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 0.001 na pH 6.5 0.1 na temperature 300 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 _Indirect_shift_ratio_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_one DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 $citation_one DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one 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_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name PDI _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 ALA HA H 3.83 . 1 2 . 1 ALA HB H 1.53 . 1 3 . 1 ALA C C 173.7 . 1 4 . 1 ALA CA C 51.8 . 1 5 . 1 ALA CB C 19.8 . 1 6 . 2 ALA H H 8.79 . 1 7 . 2 ALA HA H 4.76 . 1 8 . 2 ALA HB H 1.12 . 1 9 . 2 ALA C C 177.0 . 1 10 . 2 ALA CA C 51.8 . 1 11 . 2 ALA CB C 19.2 . 1 12 . 2 ALA N N 124.3 . 1 13 . 3 THR H H 8.83 . 1 14 . 3 THR HA H 4.52 . 1 15 . 3 THR HB H 4.09 . 1 16 . 3 THR HG2 H 1.32 . 1 17 . 3 THR C C 174.2 . 1 18 . 3 THR CA C 62.2 . 1 19 . 3 THR CB C 70.9 . 1 20 . 3 THR CG2 C 21.3 . 1 21 . 3 THR N N 121.9 . 1 22 . 4 THR H H 9.03 . 1 23 . 4 THR HA H 4.65 . 1 24 . 4 THR HB H 4.12 . 1 25 . 4 THR HG2 H 1.21 . 1 26 . 4 THR CA C 64.0 . 1 27 . 4 THR CB C 69.2 . 1 28 . 4 THR CG2 C 21.1 . 1 29 . 4 THR N N 126.5 . 1 30 . 5 LEU H H 9.11 . 1 31 . 5 LEU HA H 5.06 . 1 32 . 5 LEU HB2 H 1.98 . 1 33 . 5 LEU HB3 H 1.10 . 1 34 . 5 LEU HG H 1.88 . 1 35 . 5 LEU HD1 H 0.74 . 1 36 . 5 LEU HD2 H 0.70 . 1 37 . 5 LEU CA C 50.5 . 1 38 . 5 LEU CB C 42.0 . 1 39 . 5 LEU CG C 25.2 . 1 40 . 5 LEU CD1 C 23.1 . 1 41 . 5 LEU CD2 C 27.2 . 1 42 . 5 LEU N N 128.7 . 1 43 . 6 PRO HA H 4.56 . 1 44 . 6 PRO HB2 H 2.46 . 1 45 . 6 PRO HB3 H 2.04 . 1 46 . 6 PRO HG2 H 2.06 . 1 47 . 6 PRO HG3 H 2.06 . 1 48 . 6 PRO HD2 H 4.05 . 2 49 . 6 PRO HD3 H 3.78 . 2 50 . 6 PRO C C 175.5 . 1 51 . 6 PRO CA C 64.3 . 1 52 . 6 PRO CB C 32.9 . 1 53 . 6 PRO CG C 27.0 . 1 54 . 6 PRO CD C 52.1 . 1 55 . 7 ASP H H 7.15 . 1 56 . 7 ASP HA H 4.46 . 1 57 . 7 ASP HB2 H 3.07 . 1 58 . 7 ASP HB3 H 2.93 . 1 59 . 7 ASP C C 175.5 . 1 60 . 7 ASP CA C 52.8 . 1 61 . 7 ASP CB C 42.2 . 1 62 . 7 ASP N N 113.8 . 1 63 . 8 GLY H H 9.19 . 1 64 . 8 GLY HA2 H 4.03 . 2 65 . 8 GLY HA3 H 3.66 . 2 66 . 8 GLY C C 175.1 . 1 67 . 8 GLY CA C 47.5 . 1 68 . 8 GLY N N 108.4 . 1 69 . 9 ALA H H 8.11 . 1 70 . 9 ALA HA H 4.22 . 1 71 . 9 ALA HB H 1.44 . 1 72 . 9 ALA C C 180.6 . 1 73 . 9 ALA CA C 55.0 . 1 74 . 9 ALA CB C 17.7 . 1 75 . 9 ALA N N 126.9 . 1 76 . 10 ALA H H 8.29 . 1 77 . 10 ALA HA H 4.23 . 1 78 . 10 ALA HB H 1.68 . 1 79 . 10 ALA C C 180.7 . 1 80 . 10 ALA CA C 54.8 . 1 81 . 10 ALA CB C 18.7 . 1 82 . 10 ALA N N 123.1 . 1 83 . 11 ALA H H 7.67 . 1 84 . 11 ALA HA H 4.01 . 1 85 . 11 ALA HB H 1.54 . 1 86 . 11 ALA C C 177.2 . 1 87 . 11 ALA CA C 55.9 . 1 88 . 11 ALA CB C 18.7 . 1 89 . 11 ALA N N 122.4 . 1 90 . 12 GLU H H 8.53 . 1 91 . 12 GLU HA H 3.84 . 1 92 . 12 GLU HB2 H 2.06 . 1 93 . 12 GLU HB3 H 2.06 . 1 94 . 12 GLU HG2 H 2.40 . 2 95 . 12 GLU HG3 H 2.26 . 2 96 . 12 GLU C C 178.9 . 1 97 . 12 GLU CA C 59.6 . 1 98 . 12 GLU CB C 29.5 . 1 99 . 12 GLU CG C 36.4 . 1 100 . 12 GLU N N 118.9 . 1 101 . 13 SER H H 7.97 . 1 102 . 13 SER HA H 4.22 . 1 103 . 13 SER HB2 H 3.98 . 1 104 . 13 SER HB3 H 3.93 . 1 105 . 13 SER C C 176.8 . 1 106 . 13 SER CA C 61.7 . 1 107 . 13 SER CB C 63.1 . 1 108 . 13 SER N N 114.4 . 1 109 . 14 LEU H H 7.52 . 1 110 . 14 LEU HA H 4.07 . 1 111 . 14 LEU HB2 H 1.61 . 1 112 . 14 LEU HB3 H 1.87 . 1 113 . 14 LEU HG H 1.36 . 1 114 . 14 LEU HD1 H 0.88 . 1 115 . 14 LEU HD2 H 0.71 . 1 116 . 14 LEU C C 179.2 . 1 117 . 14 LEU CA C 58.9 . 1 118 . 14 LEU CB C 41.9 . 1 119 . 14 LEU CG C 27.2 . 1 120 . 14 LEU CD1 C 24.7 . 1 121 . 14 LEU CD2 C 26.5 . 1 122 . 14 LEU N N 124.7 . 1 123 . 15 VAL H H 8.03 . 1 124 . 15 VAL HA H 3.15 . 1 125 . 15 VAL HB H 1.78 . 1 126 . 15 VAL HG1 H 0.54 . 1 127 . 15 VAL HG2 H 0.16 . 1 128 . 15 VAL C C 177.7 . 1 129 . 15 VAL CA C 67.0 . 1 130 . 15 VAL CB C 31.4 . 1 131 . 15 VAL CG1 C 21.1 . 1 132 . 15 VAL CG2 C 22.0 . 1 133 . 15 VAL N N 121.1 . 1 134 . 16 GLU H H 8.21 . 1 135 . 16 GLU HA H 4.08 . 1 136 . 16 GLU HB2 H 2.07 . 1 137 . 16 GLU HB3 H 2.07 . 1 138 . 16 GLU HG2 H 2.38 . 1 139 . 16 GLU HG3 H 2.38 . 1 140 . 16 GLU C C 178.6 . 1 141 . 16 GLU CA C 58.5 . 1 142 . 16 GLU CB C 29.4 . 1 143 . 16 GLU CG C 36.1 . 1 144 . 16 GLU N N 116.7 . 1 145 . 17 SER H H 7.60 . 1 146 . 17 SER HA H 4.40 . 1 147 . 17 SER HB2 H 4.14 . 2 148 . 17 SER HB3 H 4.08 . 2 149 . 17 SER C C 173.8 . 1 150 . 17 SER CA C 60.1 . 1 151 . 17 SER CB C 64.7 . 1 152 . 17 SER N N 114.2 . 1 153 . 18 SER H H 7.15 . 1 154 . 18 SER HA H 4.86 . 1 155 . 18 SER HB2 H 3.70 . 1 156 . 18 SER HB3 H 3.59 . 1 157 . 18 SER C C 172.8 . 1 158 . 18 SER CA C 57.6 . 1 159 . 18 SER CB C 65.8 . 1 160 . 18 SER N N 117.3 . 1 161 . 19 GLU H H 8.79 . 1 162 . 19 GLU HA H 3.96 . 1 163 . 19 GLU HB2 H 2.30 . 2 164 . 19 GLU HB3 H 2.21 . 2 165 . 19 GLU HG2 H 2.51 . 1 166 . 19 GLU HG3 H 2.51 . 1 167 . 19 GLU C C 176.0 . 1 168 . 19 GLU CA C 60.3 . 1 169 . 19 GLU CB C 30.3 . 1 170 . 19 GLU CG C 37.0 . 1 171 . 19 GLU N N 126.2 . 1 172 . 20 VAL H H 7.42 . 1 173 . 20 VAL HA H 5.08 . 1 174 . 20 VAL HB H 1.95 . 1 175 . 20 VAL HG1 H 1.17 . 1 176 . 20 VAL HG2 H 0.90 . 1 177 . 20 VAL CA C 60.8 . 1 178 . 20 VAL CB C 35.8 . 1 179 . 20 VAL CG1 C 22.6 . 1 180 . 20 VAL CG2 C 21.5 . 1 181 . 20 VAL N N 115.5 . 1 182 . 21 ALA H H 9.09 . 1 183 . 21 ALA HA H 4.86 . 1 184 . 21 ALA HB H 1.21 . 1 185 . 21 ALA C C 175.0 . 1 186 . 21 ALA CA C 51.3 . 1 187 . 21 ALA CB C 22.7 . 1 188 . 21 ALA N N 128.6 . 1 189 . 22 VAL H H 8.11 . 1 190 . 22 VAL HA H 5.13 . 1 191 . 22 VAL HB H 1.28 . 1 192 . 22 VAL HG1 H 0.85 . 1 193 . 22 VAL HG2 H 0.53 . 1 194 . 22 VAL C C 174.7 . 1 195 . 22 VAL CA C 61.0 . 1 196 . 22 VAL CB C 34.5 . 1 197 . 22 VAL CG1 C 22.6 . 1 198 . 22 VAL CG2 C 21.6 . 1 199 . 22 VAL N N 121.9 . 1 200 . 23 ILE H H 9.17 . 1 201 . 23 ILE HA H 4.86 . 1 202 . 23 ILE HB H 1.47 . 1 203 . 23 ILE HG12 H 1.44 . 2 204 . 23 ILE HG13 H 0.50 . 2 205 . 23 ILE HG2 H -0.42 . 1 206 . 23 ILE HD1 H 0.28 . 1 207 . 23 ILE C C 173.4 . 1 208 . 23 ILE CA C 60.5 . 1 209 . 23 ILE CB C 40.5 . 1 210 . 23 ILE CG1 C 28.1 . 1 211 . 23 ILE CG2 C 16.9 . 1 212 . 23 ILE CD1 C 12.4 . 1 213 . 23 ILE N N 126.1 . 1 214 . 24 GLY H H 8.27 . 1 215 . 24 GLY HA2 H 4.01 . 2 216 . 24 GLY HA3 H 1.93 . 2 217 . 24 GLY C C 169.2 . 1 218 . 24 GLY CA C 44.7 . 1 219 . 24 GLY N N 117.6 . 1 220 . 25 PHE H H 8.57 . 1 221 . 25 PHE HA H 4.25 . 1 222 . 25 PHE HB2 H 2.13 . 1 223 . 25 PHE HB3 H 0.59 . 1 224 . 25 PHE HD1 H 6.38 . 1 225 . 25 PHE HD2 H 6.38 . 1 226 . 25 PHE HE1 H 6.98 . 1 227 . 25 PHE HE2 H 6.98 . 1 228 . 25 PHE HZ H 6.56 . 1 229 . 25 PHE CA C 55.3 . 1 230 . 25 PHE CB C 36.8 . 1 231 . 25 PHE CD1 C 133.3 . 1 232 . 25 PHE CD2 C 133.3 . 1 233 . 25 PHE CE1 C 130.4 . 1 234 . 25 PHE CE2 C 130.4 . 1 235 . 25 PHE CZ C 127.7 . 1 236 . 25 PHE N N 129.8 . 1 237 . 26 PHE H H 8.26 . 1 238 . 26 PHE HA H 5.01 . 1 239 . 26 PHE HB2 H 2.33 . 1 240 . 26 PHE HB3 H 2.92 . 1 241 . 26 PHE HD1 H 7.00 . 1 242 . 26 PHE HD2 H 7.00 . 1 243 . 26 PHE HE1 H 6.63 . 1 244 . 26 PHE HE2 H 6.63 . 1 245 . 26 PHE HZ H 6.61 . 1 246 . 26 PHE C C 174.4 . 1 247 . 26 PHE CA C 56.1 . 1 248 . 26 PHE CB C 43.2 . 1 249 . 26 PHE CD1 C 132.2 . 1 250 . 26 PHE CD2 C 132.2 . 1 251 . 26 PHE CE1 C 129.9 . 1 252 . 26 PHE CE2 C 129.9 . 1 253 . 26 PHE CZ C 128.4 . 1 254 . 26 PHE N N 118.7 . 1 255 . 27 LYS H H 9.48 . 1 256 . 27 LYS HA H 4.07 . 1 257 . 27 LYS HB2 H 1.86 . 1 258 . 27 LYS HB3 H 2.01 . 1 259 . 27 LYS HG2 H 1.59 . 2 260 . 27 LYS HG3 H 1.40 . 2 261 . 27 LYS HD2 H 1.55 . 1 262 . 27 LYS HD3 H 1.55 . 1 263 . 27 LYS HE2 H 2.68 . 2 264 . 27 LYS HE3 H 2.50 . 2 265 . 27 LYS C C 176.7 . 1 266 . 27 LYS CA C 59.0 . 1 267 . 27 LYS CB C 32.1 . 1 268 . 27 LYS CG C 25.0 . 1 269 . 27 LYS CD C 28.5 . 1 270 . 27 LYS CE C 41.7 . 1 271 . 27 LYS N N 126.5 . 1 272 . 28 ASP H H 9.00 . 1 273 . 28 ASP HA H 5.08 . 1 274 . 28 ASP HB2 H 2.97 . 2 275 . 28 ASP HB3 H 2.60 . 2 276 . 28 ASP C C 177.8 . 1 277 . 28 ASP CA C 52.0 . 1 278 . 28 ASP CB C 42.1 . 1 279 . 28 ASP N N 119.1 . 1 280 . 29 VAL H H 8.66 . 1 281 . 29 VAL HA H 3.82 . 1 282 . 29 VAL HB H 2.39 . 1 283 . 29 VAL HG1 H 1.07 . 1 284 . 29 VAL HG2 H 0.99 . 1 285 . 29 VAL CA C 64.3 . 1 286 . 29 VAL CB C 30.7 . 1 287 . 29 VAL CG1 C 21.4 . 1 288 . 29 VAL CG2 C 19.0 . 1 289 . 29 VAL N N 122.6 . 1 290 . 30 GLU H H 8.29 . 1 291 . 30 GLU HA H 4.41 . 1 292 . 30 GLU HB2 H 1.95 . 1 293 . 30 GLU HB3 H 2.31 . 1 294 . 30 GLU HG2 H 2.33 . 2 295 . 30 GLU HG3 H 2.13 . 2 296 . 30 GLU C C 176.7 . 1 297 . 30 GLU CA C 55.2 . 1 298 . 30 GLU CB C 29.3 . 1 299 . 30 GLU CG C 36.5 . 1 300 . 30 GLU N N 118.8 . 1 301 . 31 SER H H 7.62 . 1 302 . 31 SER HA H 4.33 . 1 303 . 31 SER HB2 H 4.47 . 1 304 . 31 SER HB3 H 4.21 . 1 305 . 31 SER C C 173.9 . 1 306 . 31 SER CA C 58.5 . 1 307 . 31 SER CB C 65.8 . 1 308 . 31 SER N N 118.0 . 1 309 . 32 ASP H H 8.99 . 1 310 . 32 ASP HA H 4.34 . 1 311 . 32 ASP HB2 H 2.75 . 1 312 . 32 ASP HB3 H 2.75 . 1 313 . 32 ASP C C 179.3 . 1 314 . 32 ASP CA C 58.4 . 1 315 . 32 ASP CB C 40.4 . 1 316 . 32 ASP N N 123.3 . 1 317 . 33 SER H H 8.59 . 1 318 . 33 SER HA H 4.12 . 1 319 . 33 SER HB2 H 3.95 . 1 320 . 33 SER HB3 H 3.95 . 1 321 . 33 SER C C 174.7 . 1 322 . 33 SER CA C 62.0 . 1 323 . 33 SER CB C 62.6 . 1 324 . 33 SER N N 115.9 . 1 325 . 34 ALA H H 7.03 . 1 326 . 34 ALA HA H 2.39 . 1 327 . 34 ALA HB H 0.98 . 1 328 . 34 ALA C C 179.7 . 1 329 . 34 ALA CA C 54.8 . 1 330 . 34 ALA CB C 19.0 . 1 331 . 34 ALA N N 127.4 . 1 332 . 35 LYS H H 8.14 . 1 333 . 35 LYS HA H 3.85 . 1 334 . 35 LYS HB2 H 1.94 . 1 335 . 35 LYS HB3 H 1.79 . 1 336 . 35 LYS HG2 H 1.61 . 2 337 . 35 LYS HG3 H 1.37 . 2 338 . 35 LYS HD2 H 1.63 . 1 339 . 35 LYS HD3 H 1.63 . 1 340 . 35 LYS HE2 H 2.97 . 1 341 . 35 LYS HE3 H 2.97 . 1 342 . 35 LYS C C 180.5 . 1 343 . 35 LYS CA C 60.4 . 1 344 . 35 LYS CB C 32.2 . 1 345 . 35 LYS CG C 26.1 . 1 346 . 35 LYS CD C 29.4 . 1 347 . 35 LYS CE C 42.4 . 1 348 . 35 LYS N N 117.5 . 1 349 . 36 GLN H H 7.91 . 1 350 . 36 GLN HA H 3.83 . 1 351 . 36 GLN HB2 H 2.22 . 1 352 . 36 GLN HB3 H 1.81 . 1 353 . 36 GLN HG2 H 2.70 . 1 354 . 36 GLN HG3 H 2.70 . 1 355 . 36 GLN HE21 H 7.92 . 2 356 . 36 GLN HE22 H 6.97 . 2 357 . 36 GLN C C 178.0 . 1 358 . 36 GLN CA C 58.8 . 1 359 . 36 GLN CB C 28.7 . 1 360 . 36 GLN CG C 33.8 . 1 361 . 36 GLN N N 120.8 . 1 362 . 36 GLN NE2 N 117.4 . 1 363 . 37 PHE H H 7.78 . 1 364 . 37 PHE HA H 3.87 . 1 365 . 37 PHE HB2 H 2.80 . 1 366 . 37 PHE HB3 H 3.28 . 1 367 . 37 PHE HD1 H 7.13 . 1 368 . 37 PHE HD2 H 7.13 . 1 369 . 37 PHE HE1 H 7.21 . 1 370 . 37 PHE HE2 H 7.21 . 1 371 . 37 PHE HZ H 7.72 . 1 372 . 37 PHE C C 176.2 . 1 373 . 37 PHE CA C 61.8 . 1 374 . 37 PHE CB C 39.3 . 1 375 . 37 PHE CD1 C 132.0 . 1 376 . 37 PHE CD2 C 132.0 . 1 377 . 37 PHE CE1 C 131.3 . 1 378 . 37 PHE CE2 C 131.3 . 1 379 . 37 PHE CZ C 131.6 . 1 380 . 37 PHE N N 122.0 . 1 381 . 38 LEU H H 8.58 . 1 382 . 38 LEU HA H 3.66 . 1 383 . 38 LEU HB2 H 1.89 . 1 384 . 38 LEU HB3 H 1.43 . 1 385 . 38 LEU HG H 1.92 . 1 386 . 38 LEU HD1 H 0.91 . 1 387 . 38 LEU HD2 H 0.89 . 1 388 . 38 LEU C C 180.0 . 1 389 . 38 LEU CA C 57.9 . 1 390 . 38 LEU CB C 41.2 . 1 391 . 38 LEU CG C 26.9 . 1 392 . 38 LEU CD1 C 22.7 . 1 393 . 38 LEU CD2 C 25.4 . 1 394 . 38 LEU N N 121.2 . 1 395 . 39 GLN H H 7.80 . 1 396 . 39 GLN HA H 3.98 . 1 397 . 39 GLN HB2 H 2.13 . 1 398 . 39 GLN HB3 H 1.97 . 1 399 . 39 GLN HG2 H 2.60 . 2 400 . 39 GLN HG3 H 2.32 . 2 401 . 39 GLN HE21 H 7.12 . 2 402 . 39 GLN HE22 H 6.78 . 2 403 . 39 GLN C C 179.7 . 1 404 . 39 GLN CA C 59.1 . 1 405 . 39 GLN CB C 28.7 . 1 406 . 39 GLN CG C 34.5 . 1 407 . 39 GLN N N 119.6 . 1 408 . 39 GLN NE2 N 112.1 . 1 409 . 40 ALA H H 7.78 . 1 410 . 40 ALA HA H 3.76 . 1 411 . 40 ALA HB H 1.31 . 1 412 . 40 ALA C C 177.4 . 1 413 . 40 ALA CA C 55.9 . 1 414 . 40 ALA CB C 17.4 . 1 415 . 40 ALA N N 126.0 . 1 416 . 41 ALA H H 7.39 . 1 417 . 41 ALA HA H 1.97 . 1 418 . 41 ALA HB H 0.51 . 1 419 . 41 ALA C C 178.8 . 1 420 . 41 ALA CA C 53.2 . 1 421 . 41 ALA CB C 18.3 . 1 422 . 41 ALA N N 118.7 . 1 423 . 42 GLU H H 7.01 . 1 424 . 42 GLU HA H 3.99 . 1 425 . 42 GLU HB2 H 1.94 . 1 426 . 42 GLU HB3 H 2.03 . 1 427 . 42 GLU HG2 H 2.40 . 2 428 . 42 GLU HG3 H 2.22 . 2 429 . 42 GLU C C 176.9 . 1 430 . 42 GLU CA C 57.4 . 1 431 . 42 GLU CB C 30.0 . 1 432 . 42 GLU CG C 36.5 . 1 433 . 42 GLU N N 115.3 . 1 434 . 43 ALA H H 7.33 . 1 435 . 43 ALA HA H 4.33 . 1 436 . 43 ALA HB H 1.49 . 1 437 . 43 ALA C C 176.9 . 1 438 . 43 ALA CA C 52.9 . 1 439 . 43 ALA CB C 20.1 . 1 440 . 43 ALA N N 121.9 . 1 441 . 44 ILE H H 7.04 . 1 442 . 44 ILE HA H 4.41 . 1 443 . 44 ILE HB H 1.93 . 1 444 . 44 ILE HG12 H 1.56 . 2 445 . 44 ILE HG13 H 1.21 . 2 446 . 44 ILE HG2 H 1.17 . 1 447 . 44 ILE HD1 H 0.97 . 1 448 . 44 ILE C C 174.4 . 1 449 . 44 ILE CA C 60.2 . 1 450 . 44 ILE CB C 39.9 . 1 451 . 44 ILE CG1 C 27.0 . 1 452 . 44 ILE CG2 C 18.6 . 1 453 . 44 ILE CD1 C 13.5 . 1 454 . 44 ILE N N 120.4 . 1 455 . 45 ASP H H 8.42 . 1 456 . 45 ASP HA H 4.84 . 1 457 . 45 ASP HB2 H 2.71 . 2 458 . 45 ASP HB3 H 2.66 . 2 459 . 45 ASP C C 177.4 . 1 460 . 45 ASP CA C 54.7 . 1 461 . 45 ASP CB C 41.9 . 1 462 . 45 ASP N N 124.5 . 1 463 . 46 ASP H H 8.60 . 1 464 . 46 ASP HA H 4.57 . 1 465 . 46 ASP HB2 H 2.86 . 2 466 . 46 ASP HB3 H 2.70 . 2 467 . 46 ASP C C 175.2 . 1 468 . 46 ASP CA C 55.1 . 1 469 . 46 ASP CB C 40.4 . 1 470 . 46 ASP N N 117.7 . 1 471 . 47 ILE H H 7.22 . 1 472 . 47 ILE HA H 4.64 . 1 473 . 47 ILE HB H 1.71 . 1 474 . 47 ILE HG12 H 1.40 . 2 475 . 47 ILE HG13 H 1.01 . 2 476 . 47 ILE HG2 H 0.64 . 1 477 . 47 ILE HD1 H 0.64 . 1 478 . 47 ILE CA C 57.9 . 1 479 . 47 ILE CB C 41.7 . 1 480 . 47 ILE CG1 C 26.7 . 1 481 . 47 ILE CG2 C 16.6 . 1 482 . 47 ILE CD1 C 13.2 . 1 483 . 47 ILE N N 120.6 . 1 484 . 48 PRO HA H 4.69 . 1 485 . 48 PRO HB2 H 2.30 . 2 486 . 48 PRO HB3 H 1.88 . 2 487 . 48 PRO HG2 H 2.29 . 2 488 . 48 PRO HG3 H 2.09 . 2 489 . 48 PRO HD2 H 4.43 . 2 490 . 48 PRO HD3 H 3.84 . 2 491 . 48 PRO CA C 63.3 . 1 492 . 48 PRO CB C 32.7 . 1 493 . 48 PRO CG C 27.5 . 1 494 . 48 PRO CD C 51.0 . 1 495 . 49 PHE H H 8.66 . 1 496 . 49 PHE HA H 5.93 . 1 497 . 49 PHE HB2 H 3.12 . 2 498 . 49 PHE HB3 H 2.61 . 2 499 . 49 PHE HD1 H 7.22 . 1 500 . 49 PHE HD2 H 7.22 . 1 501 . 49 PHE HE1 H 6.93 . 1 502 . 49 PHE HE2 H 6.93 . 1 503 . 49 PHE HZ H 6.81 . 1 504 . 49 PHE C C 176.8 . 1 505 . 49 PHE CA C 55.8 . 1 506 . 49 PHE CB C 42.9 . 1 507 . 49 PHE CD1 C 132.9 . 1 508 . 49 PHE CD2 C 132.9 . 1 509 . 49 PHE CE1 C 130.2 . 1 510 . 49 PHE CE2 C 130.2 . 1 511 . 49 PHE CZ C 128.4 . 1 512 . 49 PHE N N 122.0 . 1 513 . 50 GLY H H 9.63 . 1 514 . 50 GLY HA2 H 5.72 . 2 515 . 50 GLY HA3 H 3.37 . 2 516 . 50 GLY C C 171.0 . 1 517 . 50 GLY CA C 43.6 . 1 518 . 50 GLY N N 110.7 . 1 519 . 51 ILE H H 8.93 . 1 520 . 51 ILE HA H 5.62 . 1 521 . 51 ILE HB H 1.76 . 1 522 . 51 ILE HG12 H 1.76 . 2 523 . 51 ILE HG13 H 1.17 . 2 524 . 51 ILE HG2 H 0.96 . 1 525 . 51 ILE HD1 H 1.06 . 1 526 . 51 ILE C C 172.0 . 1 527 . 51 ILE CA C 58.6 . 1 528 . 51 ILE CB C 43.3 . 1 529 . 51 ILE CG1 C 28.9 . 1 530 . 51 ILE CG2 C 15.0 . 1 531 . 51 ILE CD1 C 14.9 . 1 532 . 51 ILE N N 122.5 . 1 533 . 52 THR H H 8.74 . 1 534 . 52 THR HA H 5.02 . 1 535 . 52 THR HB H 3.93 . 1 536 . 52 THR HG2 H 0.72 . 1 537 . 52 THR C C 170.0 . 1 538 . 52 THR CA C 60.5 . 1 539 . 52 THR CB C 72.9 . 1 540 . 52 THR CG2 C 19.5 . 1 541 . 52 THR N N 123.2 . 1 542 . 53 SER H H 8.77 . 1 543 . 53 SER HA H 5.25 . 1 544 . 53 SER HB2 H 4.23 . 2 545 . 53 SER HB3 H 4.06 . 2 546 . 53 SER C C 173.9 . 1 547 . 53 SER CA C 57.0 . 1 548 . 53 SER CB C 66.1 . 1 549 . 53 SER N N 121.6 . 1 550 . 54 ASN H H 8.06 . 1 551 . 54 ASN HA H 4.85 . 1 552 . 54 ASN HB2 H 2.91 . 1 553 . 54 ASN HB3 H 2.91 . 1 554 . 54 ASN HD21 H 8.06 . 2 555 . 54 ASN HD22 H 7.72 . 2 556 . 54 ASN C C 177.5 . 1 557 . 54 ASN CA C 53.4 . 1 558 . 54 ASN CB C 39.5 . 1 559 . 54 ASN N N 124.0 . 1 560 . 54 ASN ND2 N 114.6 . 1 561 . 55 SER H H 9.49 . 1 562 . 55 SER C C 176.1 . 1 563 . 55 SER N N 127.5 . 1 564 . 56 ASP H H 8.71 . 1 565 . 56 ASP HA H 4.60 . 1 566 . 56 ASP HB2 H 2.81 . 2 567 . 56 ASP HB3 H 2.72 . 2 568 . 56 ASP C C 179.0 . 1 569 . 56 ASP CA C 57.5 . 1 570 . 56 ASP CB C 40.1 . 1 571 . 56 ASP N N 123.9 . 1 572 . 57 VAL H H 8.09 . 1 573 . 57 VAL HA H 3.78 . 1 574 . 57 VAL HB H 2.67 . 1 575 . 57 VAL HG1 H 1.22 . 1 576 . 57 VAL HG2 H 0.83 . 1 577 . 57 VAL C C 177.9 . 1 578 . 57 VAL CA C 66.1 . 1 579 . 57 VAL CB C 30.8 . 1 580 . 57 VAL CG1 C 23.7 . 1 581 . 57 VAL CG2 C 22.8 . 1 582 . 57 VAL N N 124.0 . 1 583 . 58 PHE H H 8.01 . 1 584 . 58 PHE HA H 4.24 . 1 585 . 58 PHE HB2 H 3.58 . 2 586 . 58 PHE HB3 H 3.17 . 2 587 . 58 PHE HD1 H 7.15 . 1 588 . 58 PHE HD2 H 7.15 . 1 589 . 58 PHE HE1 H 7.00 . 1 590 . 58 PHE HE2 H 7.00 . 1 591 . 58 PHE HZ H 6.28 . 1 592 . 58 PHE C C 178.8 . 1 593 . 58 PHE CA C 62.2 . 1 594 . 58 PHE CB C 37.8 . 1 595 . 58 PHE CD1 C 132.3 . 1 596 . 58 PHE CD2 C 132.3 . 1 597 . 58 PHE CE1 C 130.9 . 1 598 . 58 PHE CE2 C 130.9 . 1 599 . 58 PHE CZ C 129.0 . 1 600 . 58 PHE N N 121.9 . 1 601 . 59 SER H H 8.12 . 1 602 . 59 SER HA H 4.26 . 1 603 . 59 SER HB2 H 4.03 . 1 604 . 59 SER HB3 H 4.03 . 1 605 . 59 SER C C 177.8 . 1 606 . 59 SER CA C 62.0 . 1 607 . 59 SER CB C 63.0 . 1 608 . 59 SER N N 113.8 . 1 609 . 60 LYS H H 7.70 . 1 610 . 60 LYS HA H 3.89 . 1 611 . 60 LYS HB2 H 1.94 . 2 612 . 60 LYS HB3 H 1.89 . 2 613 . 60 LYS HG2 H 1.18 . 2 614 . 60 LYS HG3 H 0.27 . 2 615 . 60 LYS HD2 H 1.60 . 2 616 . 60 LYS HD3 H 1.42 . 2 617 . 60 LYS HE2 H 3.08 . 2 618 . 60 LYS HE3 H 2.79 . 2 619 . 60 LYS C C 176.7 . 1 620 . 60 LYS CA C 59.2 . 1 621 . 60 LYS CB C 33.0 . 1 622 . 60 LYS CG C 24.0 . 1 623 . 60 LYS CD C 30.3 . 1 624 . 60 LYS CE C 42.2 . 1 625 . 60 LYS N N 125.8 . 1 626 . 61 TYR H H 7.09 . 1 627 . 61 TYR HA H 4.67 . 1 628 . 61 TYR HB2 H 2.39 . 1 629 . 61 TYR HB3 H 3.29 . 1 630 . 61 TYR HD1 H 7.47 . 1 631 . 61 TYR HD2 H 7.47 . 1 632 . 61 TYR HE1 H 6.58 . 1 633 . 61 TYR HE2 H 6.58 . 1 634 . 61 TYR C C 173.4 . 1 635 . 61 TYR CA C 58.7 . 1 636 . 61 TYR CB C 37.9 . 1 637 . 61 TYR CD1 C 133.3 . 1 638 . 61 TYR CD2 C 133.3 . 1 639 . 61 TYR CE1 C 117.2 . 1 640 . 61 TYR CE2 C 117.2 . 1 641 . 61 TYR N N 115.6 . 1 642 . 62 GLN H H 7.89 . 1 643 . 62 GLN HA H 3.85 . 1 644 . 62 GLN HB2 H 2.41 . 2 645 . 62 GLN HB3 H 2.22 . 2 646 . 62 GLN HG2 H 2.35 . 2 647 . 62 GLN HG3 H 2.22 . 2 648 . 62 GLN HE21 H 7.52 . 2 649 . 62 GLN HE22 H 6.68 . 2 650 . 62 GLN C C 174.7 . 1 651 . 62 GLN CA C 57.5 . 1 652 . 62 GLN CB C 25.3 . 1 653 . 62 GLN CG C 34.8 . 1 654 . 62 GLN N N 115.3 . 1 655 . 62 GLN NE2 N 114.3 . 1 656 . 63 LEU H H 8.12 . 1 657 . 63 LEU HA H 4.57 . 1 658 . 63 LEU HB2 H 1.57 . 1 659 . 63 LEU HB3 H 1.06 . 1 660 . 63 LEU HG H 1.01 . 1 661 . 63 LEU HD1 H 0.13 . 1 662 . 63 LEU HD2 H -0.15 . 1 663 . 63 LEU CA C 55.2 . 1 664 . 63 LEU CB C 43.5 . 1 665 . 63 LEU CG C 28.5 . 1 666 . 63 LEU CD1 C 23.8 . 1 667 . 63 LEU CD2 C 23.9 . 1 668 . 63 LEU N N 122.6 . 1 669 . 64 ASP H H 8.66 . 1 670 . 64 ASP HA H 4.67 . 1 671 . 64 ASP HB2 H 2.77 . 2 672 . 64 ASP HB3 H 2.57 . 2 673 . 64 ASP C C 174.7 . 1 674 . 64 ASP CA C 53.4 . 1 675 . 64 ASP CB C 41.7 . 1 676 . 64 ASP N N 122.2 . 1 677 . 65 LYS H H 7.76 . 1 678 . 65 LYS HA H 4.60 . 1 679 . 65 LYS HB2 H 2.06 . 2 680 . 65 LYS HB3 H 1.85 . 2 681 . 65 LYS HG2 H 1.42 . 1 682 . 65 LYS HG3 H 1.42 . 1 683 . 65 LYS HD2 H 1.71 . 1 684 . 65 LYS HD3 H 1.71 . 1 685 . 65 LYS HE2 H 3.05 . 1 686 . 65 LYS HE3 H 3.05 . 1 687 . 65 LYS C C 173.2 . 1 688 . 65 LYS CA C 54.7 . 1 689 . 65 LYS CB C 34.5 . 1 690 . 65 LYS CG C 22.6 . 1 691 . 65 LYS CD C 29.2 . 1 692 . 65 LYS CE C 42.2 . 1 693 . 65 LYS N N 119.0 . 1 694 . 66 ASP H H 7.86 . 1 695 . 66 ASP HA H 4.71 . 1 696 . 66 ASP HB2 H 2.82 . 2 697 . 66 ASP HB3 H 2.63 . 2 698 . 66 ASP C C 177.7 . 1 699 . 66 ASP CA C 54.8 . 1 700 . 66 ASP CB C 41.7 . 1 701 . 66 ASP N N 118.8 . 1 702 . 67 GLY H H 8.68 . 1 703 . 67 GLY HA2 H 3.94 . 1 704 . 67 GLY HA3 H 3.94 . 1 705 . 67 GLY C C 169.7 . 1 706 . 67 GLY CA C 45.8 . 1 707 . 67 GLY N N 109.1 . 1 708 . 68 VAL H H 8.63 . 1 709 . 68 VAL HA H 4.88 . 1 710 . 68 VAL HB H 1.71 . 1 711 . 68 VAL HG1 H 0.93 . 1 712 . 68 VAL HG2 H 0.99 . 1 713 . 68 VAL C C 173.7 . 1 714 . 68 VAL CA C 61.6 . 1 715 . 68 VAL CB C 35.5 . 1 716 . 68 VAL CG1 C 22.2 . 1 717 . 68 VAL CG2 C 21.8 . 1 718 . 68 VAL N N 119.9 . 1 719 . 69 VAL H H 9.02 . 1 720 . 69 VAL HA H 4.60 . 1 721 . 69 VAL HB H 1.77 . 1 722 . 69 VAL HG1 H 0.74 . 1 723 . 69 VAL HG2 H 0.00 . 1 724 . 69 VAL C C 172.8 . 1 725 . 69 VAL CA C 61.6 . 1 726 . 69 VAL CB C 36.1 . 1 727 . 69 VAL CG1 C 22.3 . 1 728 . 69 VAL CG2 C 22.7 . 1 729 . 69 VAL N N 128.8 . 1 730 . 70 LEU H H 8.76 . 1 731 . 70 LEU HA H 5.05 . 1 732 . 70 LEU HB2 H 1.67 . 2 733 . 70 LEU HB3 H 1.50 . 2 734 . 70 LEU HG H 1.51 . 1 735 . 70 LEU HD1 H 0.58 . 1 736 . 70 LEU HD2 H 0.51 . 1 737 . 70 LEU C C 173.6 . 1 738 . 70 LEU CA C 54.5 . 1 739 . 70 LEU CB C 46.1 . 1 740 . 70 LEU CG C 27.6 . 1 741 . 70 LEU CD1 C 26.4 . 1 742 . 70 LEU CD2 C 28.0 . 1 743 . 70 LEU N N 129.8 . 1 744 . 71 PHE H H 9.68 . 1 745 . 71 PHE HA H 4.97 . 1 746 . 71 PHE HB2 H 2.72 . 1 747 . 71 PHE HB3 H 3.14 . 1 748 . 71 PHE HD1 H 7.17 . 9 749 . 71 PHE HD2 H 7.17 . 9 750 . 71 PHE HE1 H 7.01 . 9 751 . 71 PHE HE2 H 7.01 . 9 752 . 71 PHE C C 173.9 . 1 753 . 71 PHE CA C 57.4 . 1 754 . 71 PHE CB C 42.3 . 1 755 . 71 PHE N N 128.6 . 1 756 . 72 LYS H H 8.44 . 1 757 . 72 LYS HA H 5.40 . 1 758 . 72 LYS HB2 H 0.99 . 1 759 . 72 LYS HB3 H 1.44 . 1 760 . 72 LYS HG2 H 1.09 . 2 761 . 72 LYS HG3 H 0.83 . 2 762 . 72 LYS HD2 H 1.41 . 2 763 . 72 LYS HD3 H 1.28 . 2 764 . 72 LYS HE2 H 2.70 . 2 765 . 72 LYS HE3 H 2.62 . 2 766 . 72 LYS C C 176.6 . 1 767 . 72 LYS CA C 54.0 . 1 768 . 72 LYS CB C 35.1 . 1 769 . 72 LYS CG C 23.1 . 1 770 . 72 LYS CD C 30.0 . 1 771 . 72 LYS CE C 42.7 . 1 772 . 72 LYS N N 118.2 . 1 773 . 73 LYS H H 8.19 . 1 774 . 73 LYS HA H 4.34 . 1 775 . 73 LYS HB2 H 1.85 . 1 776 . 73 LYS HB3 H 2.19 . 1 777 . 73 LYS HG2 H 1.70 . 2 778 . 73 LYS HG3 H 1.48 . 2 779 . 73 LYS HD2 H 1.74 . 2 780 . 73 LYS HD3 H 1.66 . 2 781 . 73 LYS HE2 H 3.08 . 2 782 . 73 LYS HE3 H 3.01 . 2 783 . 73 LYS C C 175.4 . 1 784 . 73 LYS CA C 56.5 . 1 785 . 73 LYS CB C 32.1 . 1 786 . 73 LYS CG C 25.8 . 1 787 . 73 LYS CD C 29.6 . 1 788 . 73 LYS CE C 42.4 . 1 789 . 73 LYS N N 123.2 . 1 790 . 74 PHE H H 6.93 . 1 791 . 74 PHE HA H 4.82 . 1 792 . 74 PHE HB2 H 3.15 . 1 793 . 74 PHE HB3 H 3.31 . 1 794 . 74 PHE HD1 H 7.17 . 9 795 . 74 PHE HD2 H 7.17 . 9 796 . 74 PHE C C 174.2 . 1 797 . 74 PHE CA C 55.6 . 1 798 . 74 PHE CB C 40.0 . 1 799 . 74 PHE N N 116.0 . 1 800 . 75 ASP H H 8.89 . 1 801 . 75 ASP HA H 4.37 . 1 802 . 75 ASP HB2 H 2.80 . 1 803 . 75 ASP HB3 H 2.98 . 1 804 . 75 ASP C C 176.5 . 1 805 . 75 ASP CA C 56.0 . 1 806 . 75 ASP CB C 40.6 . 1 807 . 75 ASP N N 119.6 . 1 808 . 76 GLU H H 9.66 . 1 809 . 76 GLU HA H 4.35 . 1 810 . 76 GLU HB2 H 2.26 . 2 811 . 76 GLU HB3 H 2.19 . 2 812 . 76 GLU HG2 H 2.51 . 1 813 . 76 GLU HG3 H 2.51 . 1 814 . 76 GLU C C 178.4 . 1 815 . 76 GLU CA C 58.4 . 1 816 . 76 GLU CB C 29.1 . 1 817 . 76 GLU CG C 36.4 . 1 818 . 76 GLU N N 124.4 . 1 819 . 77 GLY H H 7.91 . 1 820 . 77 GLY HA2 H 4.29 . 2 821 . 77 GLY HA3 H 4.12 . 2 822 . 77 GLY C C 174.0 . 1 823 . 77 GLY CA C 46.5 . 1 824 . 77 GLY N N 110.0 . 1 825 . 78 ARG H H 7.41 . 1 826 . 78 ARG HA H 5.19 . 1 827 . 78 ARG HB2 H 1.66 . 2 828 . 78 ARG HB3 H 1.59 . 2 829 . 78 ARG HG2 H 1.25 . 1 830 . 78 ARG HG3 H 1.25 . 1 831 . 78 ARG HD2 H 3.09 . 1 832 . 78 ARG HD3 H 3.09 . 1 833 . 78 ARG C C 174.4 . 1 834 . 78 ARG CA C 55.1 . 1 835 . 78 ARG CB C 32.7 . 1 836 . 78 ARG CG C 25.9 . 1 837 . 78 ARG CD C 44.3 . 1 838 . 78 ARG N N 122.1 . 1 839 . 79 ASN H H 9.23 . 1 840 . 79 ASN HA H 5.05 . 1 841 . 79 ASN HB2 H 2.33 . 1 842 . 79 ASN HB3 H 2.81 . 1 843 . 79 ASN HD21 H 7.30 . 2 844 . 79 ASN HD22 H 7.14 . 2 845 . 79 ASN C C 173.1 . 1 846 . 79 ASN CA C 53.7 . 1 847 . 79 ASN CB C 43.3 . 1 848 . 79 ASN N N 123.3 . 1 849 . 79 ASN ND2 N 110.8 . 1 850 . 80 ASN H H 9.19 . 1 851 . 80 ASN HA H 5.03 . 1 852 . 80 ASN HB2 H 2.71 . 1 853 . 80 ASN HB3 H 2.71 . 1 854 . 80 ASN HD21 H 7.57 . 2 855 . 80 ASN HD22 H 6.74 . 2 856 . 80 ASN C C 174.5 . 1 857 . 80 ASN CA C 53.0 . 1 858 . 80 ASN CB C 39.0 . 1 859 . 80 ASN N N 125.2 . 1 860 . 80 ASN ND2 N 114.0 . 1 861 . 81 PHE H H 8.47 . 1 862 . 81 PHE HA H 3.52 . 1 863 . 81 PHE HB2 H 2.63 . 2 864 . 81 PHE HB3 H 1.75 . 2 865 . 81 PHE HD1 H 6.47 . 1 866 . 81 PHE HD2 H 6.47 . 1 867 . 81 PHE HE1 H 6.95 . 1 868 . 81 PHE HE2 H 6.95 . 1 869 . 81 PHE HZ H 7.27 . 1 870 . 81 PHE C C 174.7 . 1 871 . 81 PHE CA C 58.9 . 1 872 . 81 PHE CB C 39.4 . 1 873 . 81 PHE CD1 C 131.4 . 1 874 . 81 PHE CD2 C 131.4 . 1 875 . 81 PHE CE1 C 131.4 . 1 876 . 81 PHE CE2 C 131.4 . 1 877 . 81 PHE CZ C 129.8 . 1 878 . 81 PHE N N 126.5 . 1 879 . 82 GLU H H 7.51 . 1 880 . 82 GLU HA H 4.33 . 1 881 . 82 GLU HB2 H 1.60 . 1 882 . 82 GLU HB3 H 1.83 . 1 883 . 82 GLU HG2 H 2.08 . 2 884 . 82 GLU HG3 H 2.02 . 2 885 . 82 GLU C C 173.9 . 1 886 . 82 GLU CA C 55.2 . 1 887 . 82 GLU CB C 31.8 . 1 888 . 82 GLU CG C 36.0 . 1 889 . 82 GLU N N 130.4 . 1 890 . 83 GLY H H 7.12 . 1 891 . 83 GLY HA2 H 3.86 . 2 892 . 83 GLY HA3 H 3.73 . 2 893 . 83 GLY CA C 43.6 . 1 894 . 83 GLY N N 110.2 . 1 895 . 84 GLU H H 8.52 . 1 896 . 84 GLU HA H 4.34 . 1 897 . 84 GLU HB2 H 1.92 . 1 898 . 84 GLU HB3 H 1.92 . 1 899 . 84 GLU HG2 H 2.35 . 2 900 . 84 GLU HG3 H 2.20 . 2 901 . 84 GLU C C 177.5 . 1 902 . 84 GLU CA C 56.5 . 1 903 . 84 GLU CB C 30.1 . 1 904 . 84 GLU CG C 36.2 . 1 905 . 84 GLU N N 122.1 . 1 906 . 85 VAL H H 9.21 . 1 907 . 85 VAL HA H 3.77 . 1 908 . 85 VAL HB H 2.31 . 1 909 . 85 VAL HG1 H 1.25 . 1 910 . 85 VAL HG2 H 0.91 . 1 911 . 85 VAL C C 173.7 . 1 912 . 85 VAL CA C 64.7 . 1 913 . 85 VAL CB C 30.1 . 1 914 . 85 VAL CG1 C 21.3 . 1 915 . 85 VAL CG2 C 23.1 . 1 916 . 85 VAL N N 128.4 . 1 917 . 86 THR H H 7.26 . 1 918 . 86 THR HA H 4.68 . 1 919 . 86 THR HB H 4.55 . 1 920 . 86 THR HG2 H 1.14 . 1 921 . 86 THR C C 174.2 . 1 922 . 86 THR CA C 58.4 . 1 923 . 86 THR CB C 72.9 . 1 924 . 86 THR CG2 C 21.8 . 1 925 . 86 THR N N 119.5 . 1 926 . 87 LYS H H 9.44 . 1 927 . 87 LYS HA H 3.73 . 1 928 . 87 LYS HB2 H 1.95 . 2 929 . 87 LYS HB3 H 1.81 . 2 930 . 87 LYS HG2 H 1.19 . 2 931 . 87 LYS HG3 H 1.11 . 2 932 . 87 LYS HD2 H 1.63 . 1 933 . 87 LYS HD3 H 1.63 . 1 934 . 87 LYS HE2 H 2.89 . 2 935 . 87 LYS HE3 H 2.75 . 2 936 . 87 LYS C C 177.1 . 1 937 . 87 LYS CA C 61.1 . 1 938 . 87 LYS CB C 32.3 . 1 939 . 87 LYS CG C 24.3 . 1 940 . 87 LYS CD C 29.9 . 1 941 . 87 LYS CE C 42.0 . 1 942 . 87 LYS N N 125.9 . 1 943 . 88 GLU H H 9.15 . 1 944 . 88 GLU HA H 3.95 . 1 945 . 88 GLU HB2 H 2.03 . 1 946 . 88 GLU HB3 H 2.03 . 1 947 . 88 GLU HG2 H 2.51 . 2 948 . 88 GLU HG3 H 2.30 . 2 949 . 88 GLU C C 179.2 . 1 950 . 88 GLU CA C 61.0 . 1 951 . 88 GLU CB C 28.5 . 1 952 . 88 GLU CG C 37.0 . 1 953 . 88 GLU N N 118.4 . 1 954 . 89 ASN H H 8.11 . 1 955 . 89 ASN HA H 4.70 . 1 956 . 89 ASN HB2 H 3.26 . 2 957 . 89 ASN HB3 H 3.15 . 2 958 . 89 ASN HD21 H 8.34 . 2 959 . 89 ASN HD22 H 7.30 . 2 960 . 89 ASN C C 179.8 . 1 961 . 89 ASN CA C 55.6 . 1 962 . 89 ASN CB C 37.6 . 1 963 . 89 ASN N N 120.0 . 1 964 . 89 ASN ND2 N 113.3 . 1 965 . 90 LEU H H 8.64 . 1 966 . 90 LEU HA H 4.01 . 1 967 . 90 LEU HB2 H 2.02 . 2 968 . 90 LEU HB3 H 1.11 . 2 969 . 90 LEU HG H 1.52 . 1 970 . 90 LEU HD1 H 0.78 . 1 971 . 90 LEU HD2 H 0.21 . 1 972 . 90 LEU CA C 58.0 . 1 973 . 90 LEU CB C 42.4 . 1 974 . 90 LEU CG C 26.9 . 1 975 . 90 LEU CD1 C 27.0 . 1 976 . 90 LEU CD2 C 22.7 . 1 977 . 90 LEU N N 123.5 . 1 978 . 91 LEU H H 8.52 . 1 979 . 91 LEU HA H 4.09 . 1 980 . 91 LEU HB2 H 1.61 . 1 981 . 91 LEU HB3 H 1.95 . 1 982 . 91 LEU HG H 1.94 . 1 983 . 91 LEU HD1 H 0.94 . 1 984 . 91 LEU HD2 H 0.90 . 1 985 . 91 LEU C C 179.2 . 1 986 . 91 LEU CA C 58.9 . 1 987 . 91 LEU CB C 40.9 . 1 988 . 91 LEU CG C 27.4 . 1 989 . 91 LEU CD1 C 23.3 . 1 990 . 91 LEU CD2 C 25.3 . 1 991 . 91 LEU N N 121.8 . 1 992 . 92 ASP H H 7.79 . 1 993 . 92 ASP HA H 4.48 . 1 994 . 92 ASP HB2 H 2.89 . 2 995 . 92 ASP HB3 H 2.78 . 2 996 . 92 ASP C C 178.1 . 1 997 . 92 ASP CA C 58.0 . 1 998 . 92 ASP CB C 41.4 . 1 999 . 92 ASP N N 120.6 . 1 1000 . 93 PHE H H 8.00 . 1 1001 . 93 PHE HA H 4.63 . 1 1002 . 93 PHE HB2 H 3.77 . 2 1003 . 93 PHE HB3 H 3.49 . 2 1004 . 93 PHE HD1 H 7.41 . 1 1005 . 93 PHE HD2 H 7.41 . 1 1006 . 93 PHE C C 177.8 . 1 1007 . 93 PHE CA C 60.6 . 1 1008 . 93 PHE CB C 40.0 . 1 1009 . 93 PHE CD1 C 132.8 . 1 1010 . 93 PHE CD2 C 132.8 . 1 1011 . 93 PHE N N 123.1 . 1 1012 . 94 ILE H H 8.79 . 1 1013 . 94 ILE HA H 3.15 . 1 1014 . 94 ILE HB H 1.86 . 1 1015 . 94 ILE HG12 H 2.14 . 2 1016 . 94 ILE HG13 H 0.90 . 2 1017 . 94 ILE HG2 H 0.77 . 1 1018 . 94 ILE HD1 H 0.98 . 1 1019 . 94 ILE C C 177.6 . 1 1020 . 94 ILE CA C 65.9 . 1 1021 . 94 ILE CB C 38.7 . 1 1022 . 94 ILE CG1 C 29.8 . 1 1023 . 94 ILE CG2 C 17.3 . 1 1024 . 94 ILE CD1 C 15.1 . 1 1025 . 94 ILE N N 123.3 . 1 1026 . 95 LYS H H 8.24 . 1 1027 . 95 LYS HA H 4.26 . 1 1028 . 95 LYS HB2 H 1.98 . 2 1029 . 95 LYS HB3 H 1.86 . 2 1030 . 95 LYS HG2 H 1.58 . 2 1031 . 95 LYS HG3 H 1.48 . 2 1032 . 95 LYS HD2 H 1.71 . 1 1033 . 95 LYS HD3 H 1.71 . 1 1034 . 95 LYS HE2 H 2.99 . 2 1035 . 95 LYS HE3 H 2.93 . 2 1036 . 95 LYS C C 179.5 . 1 1037 . 95 LYS CA C 59.3 . 1 1038 . 95 LYS CB C 32.1 . 1 1039 . 95 LYS CG C 25.4 . 1 1040 . 95 LYS CD C 29.1 . 1 1041 . 95 LYS CE C 42.4 . 1 1042 . 95 LYS N N 119.7 . 1 1043 . 96 HIS H H 7.93 . 1 1044 . 96 HIS HA H 4.49 . 1 1045 . 96 HIS HB2 H 3.30 . 1 1046 . 96 HIS HB3 H 3.30 . 1 1047 . 96 HIS HD2 H 7.26 . 1 1048 . 96 HIS HE1 H 8.56 . 1 1049 . 96 HIS C C 175.6 . 1 1050 . 96 HIS CA C 58.3 . 1 1051 . 96 HIS CB C 29.1 . 1 1052 . 96 HIS CD2 C 120.2 . 1 1053 . 96 HIS CE1 C 137.0 . 1 1054 . 96 HIS N N 115.4 . 1 1055 . 97 ASN H H 7.44 . 1 1056 . 97 ASN HA H 4.82 . 1 1057 . 97 ASN HB2 H 2.03 . 1 1058 . 97 ASN HB3 H 2.57 . 1 1059 . 97 ASN HD21 H 7.07 . 2 1060 . 97 ASN HD22 H 6.90 . 2 1061 . 97 ASN C C 174.2 . 1 1062 . 97 ASN CA C 54.8 . 1 1063 . 97 ASN CB C 41.8 . 1 1064 . 97 ASN N N 116.9 . 1 1065 . 97 ASN ND2 N 117.9 . 1 1066 . 98 GLN H H 7.63 . 1 1067 . 98 GLN HA H 4.32 . 1 1068 . 98 GLN HB2 H 2.29 . 2 1069 . 98 GLN HB3 H 2.07 . 2 1070 . 98 GLN HG2 H 2.47 . 2 1071 . 98 GLN HG3 H 2.23 . 2 1072 . 98 GLN HE21 H 7.30 . 2 1073 . 98 GLN HE22 H 6.84 . 2 1074 . 98 GLN C C 174.1 . 1 1075 . 98 GLN CA C 57.1 . 1 1076 . 98 GLN CB C 29.6 . 1 1077 . 98 GLN CG C 33.9 . 1 1078 . 98 GLN N N 117.2 . 1 1079 . 98 GLN NE2 N 111.2 . 1 1080 . 99 LEU H H 7.59 . 1 1081 . 99 LEU HA H 4.67 . 1 1082 . 99 LEU HB2 H 1.42 . 1 1083 . 99 LEU HB3 H 1.60 . 1 1084 . 99 LEU HG H 1.61 . 1 1085 . 99 LEU HD1 H 0.92 . 1 1086 . 99 LEU HD2 H 0.89 . 1 1087 . 99 LEU CA C 52.5 . 1 1088 . 99 LEU CB C 42.4 . 1 1089 . 99 LEU CG C 27.0 . 1 1090 . 99 LEU CD1 C 25.4 . 1 1091 . 99 LEU CD2 C 23.2 . 1 1092 . 99 LEU N N 122.2 . 1 1093 . 100 PRO HA H 4.39 . 1 1094 . 100 PRO HB2 H 1.84 . 2 1095 . 100 PRO HB3 H 1.65 . 2 1096 . 100 PRO HG2 H 1.72 . 2 1097 . 100 PRO HG3 H 1.11 . 2 1098 . 100 PRO HD2 H 3.39 . 1 1099 . 100 PRO HD3 H 3.39 . 1 1100 . 100 PRO C C 176.6 . 1 1101 . 100 PRO CA C 62.5 . 1 1102 . 100 PRO CB C 31.8 . 1 1103 . 100 PRO CG C 26.6 . 1 1104 . 100 PRO CD C 50.6 . 1 1105 . 101 LEU H H 9.23 . 1 1106 . 101 LEU HA H 4.24 . 1 1107 . 101 LEU HB2 H 1.53 . 1 1108 . 101 LEU HB3 H 1.68 . 1 1109 . 101 LEU HG H 1.69 . 1 1110 . 101 LEU HD1 H 0.95 . 1 1111 . 101 LEU HD2 H 0.91 . 1 1112 . 101 LEU C C 177.5 . 1 1113 . 101 LEU CA C 55.9 . 1 1114 . 101 LEU CB C 42.6 . 1 1115 . 101 LEU CG C 27.2 . 1 1116 . 101 LEU CD1 C 24.8 . 1 1117 . 101 LEU CD2 C 24.0 . 1 1118 . 101 LEU N N 126.7 . 1 1119 . 102 VAL H H 8.27 . 1 1120 . 102 VAL HA H 4.10 . 1 1121 . 102 VAL HB H 2.01 . 1 1122 . 102 VAL HG1 H 0.93 . 1 1123 . 102 VAL HG2 H 0.87 . 1 1124 . 102 VAL C C 175.6 . 1 1125 . 102 VAL CA C 62.5 . 1 1126 . 102 VAL CB C 32.9 . 1 1127 . 102 VAL CG1 C 20.8 . 1 1128 . 102 VAL CG2 C 21.1 . 1 1129 . 102 VAL N N 124.8 . 1 1130 . 103 ILE H H 8.29 . 1 1131 . 103 ILE HA H 4.16 . 1 1132 . 103 ILE HB H 1.80 . 1 1133 . 103 ILE HG12 H 1.42 . 2 1134 . 103 ILE HG13 H 1.15 . 2 1135 . 103 ILE HG2 H 0.81 . 1 1136 . 103 ILE HD1 H 0.85 . 1 1137 . 103 ILE C C 175.7 . 1 1138 . 103 ILE CA C 61.0 . 1 1139 . 103 ILE CB C 38.7 . 1 1140 . 103 ILE CG1 C 27.2 . 1 1141 . 103 ILE CG2 C 17.6 . 1 1142 . 103 ILE CD1 C 12.6 . 1 1143 . 103 ILE N N 128.2 . 1 1144 . 104 GLU H H 8.43 . 1 1145 . 104 GLU HA H 4.31 . 1 1146 . 104 GLU HB2 H 1.91 . 1 1147 . 104 GLU HB3 H 1.91 . 1 1148 . 104 GLU HG2 H 2.20 . 2 1149 . 104 GLU HG3 H 2.13 . 2 1150 . 104 GLU C C 175.6 . 1 1151 . 104 GLU CA C 56.3 . 1 1152 . 104 GLU CB C 30.4 . 1 1153 . 104 GLU CG C 36.1 . 1 1154 . 104 GLU N N 127.4 . 1 1155 . 105 PHE H H 8.42 . 1 1156 . 105 PHE HA H 4.73 . 1 1157 . 105 PHE HB2 H 3.15 . 2 1158 . 105 PHE HB3 H 3.06 . 2 1159 . 105 PHE HD1 H 7.27 . 1 1160 . 105 PHE HD2 H 7.27 . 1 1161 . 105 PHE HE1 H 7.37 . 1 1162 . 105 PHE HE2 H 7.37 . 1 1163 . 105 PHE HZ H 7.32 . 1 1164 . 105 PHE C C 175.6 . 1 1165 . 105 PHE CA C 58.0 . 1 1166 . 105 PHE CB C 40.0 . 1 1167 . 105 PHE CD1 C 132.0 . 1 1168 . 105 PHE CD2 C 132.0 . 1 1169 . 105 PHE CE1 C 131.6 . 1 1170 . 105 PHE CE2 C 131.6 . 1 1171 . 105 PHE CZ C 130.0 . 1 1172 . 105 PHE N N 124.3 . 1 1173 . 106 THR H H 8.10 . 1 1174 . 106 THR HA H 4.33 . 1 1175 . 106 THR HB H 4.15 . 1 1176 . 106 THR HG2 H 1.18 . 1 1177 . 106 THR C C 173.8 . 1 1178 . 106 THR CA C 61.8 . 1 1179 . 106 THR CB C 70.4 . 1 1180 . 106 THR CG2 C 21.0 . 1 1181 . 106 THR N N 118.8 . 1 1182 . 107 GLU H H 8.41 . 1 1183 . 107 GLU HA H 4.30 . 1 1184 . 107 GLU HB2 H 2.07 . 2 1185 . 107 GLU HB3 H 1.95 . 2 1186 . 107 GLU HG2 H 2.29 . 1 1187 . 107 GLU HG3 H 2.29 . 1 1188 . 107 GLU C C 176.1 . 1 1189 . 107 GLU CA C 56.6 . 1 1190 . 107 GLU CB C 30.6 . 1 1191 . 107 GLU CG C 36.3 . 1 1192 . 107 GLU N N 125.3 . 1 1193 . 108 GLN H H 8.52 . 1 1194 . 108 GLN HA H 4.44 . 1 1195 . 108 GLN HB2 H 2.16 . 2 1196 . 108 GLN HB3 H 2.01 . 2 1197 . 108 GLN HG2 H 2.40 . 1 1198 . 108 GLN HG3 H 2.40 . 1 1199 . 108 GLN HE21 H 7.60 . 2 1200 . 108 GLN HE22 H 6.87 . 2 1201 . 108 GLN CA C 56.1 . 1 1202 . 108 GLN CB C 29.6 . 1 1203 . 108 GLN CG C 33.9 . 1 1204 . 108 GLN N N 123.9 . 1 1205 . 108 GLN NE2 N 114.4 . 1 1206 . 109 THR H H 8.29 . 1 1207 . 109 THR HA H 4.40 . 1 1208 . 109 THR HB H 4.30 . 1 1209 . 109 THR HG2 H 1.25 . 1 1210 . 109 THR C C 173.3 . 1 1211 . 109 THR CA C 62.1 . 1 1212 . 109 THR CB C 70.3 . 1 1213 . 109 THR CG2 C 20.6 . 1 1214 . 109 THR N N 118.3 . 1 1215 . 110 ALA H H 8.06 . 1 1216 . 110 ALA HA H 4.19 . 1 1217 . 110 ALA HB H 1.36 . 1 1218 . 110 ALA CA C 54.2 . 1 1219 . 110 ALA CB C 20.1 . 1 1220 . 110 ALA N N 133.9 . 1 stop_ save_