data_4249 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the DNA- and RPA-binding Domain of the Human Repair Factor XPA ; _BMRB_accession_number 4249 _BMRB_flat_file_name bmr4249.str _Entry_type original _Submission_date 1998-10-17 _Accession_date 1998-10-17 _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 Ikegami Takahisa . . 2 Kuraoka Isao . . 3 Saijo Masafumi . . 4 Kodo Naohiko . . 5 Kyogoku Yoshimasa . . 6 Morikawa Kosuke . . 7 Tanaka Kiyoji . . 8 Shirakawa Masahiro . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 616 "13C chemical shifts" 500 "15N chemical shifts" 120 "coupling constants" 89 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 ; Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., and Shirakawa, M., "Solution Structure of the DNA- and RPA-binding Domain of the Human Repair Factor XPA," Nat. Struct. Biol. 5, 701-706 (1998). ; _Citation_title ; Solution Structure of the DNA- and RPA-binding Domain of the Human Repair Factor XPA ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98363214 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ikegami Takahisa . . 2 Kuraoka Isao . . 3 Saijo Masafumi . . 4 Kodo Naohiko . . 5 Kyogoku Yoshimasa . . 6 Morikawa Kosuke . . 7 Tanaka Kiyoji . . 8 Shirakawa Masahiro . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 5 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 701 _Page_last 706 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Cavanagh, J., Fairbrother, W. J., Palmer III, A. G., and Skelton, N. J. Protein NMR Spectroscopy, p. 176, Academic Press, Inc. (1996). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ save_citation_two _Saveframe_category citation _Citation_full 'Delaglio, F. et al. (1994) J. Biomol. NMR 6, 277-293.' _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_citation_three _Saveframe_category citation _Citation_full 'Garrett, D.S. (1991) J. Magn. Reson. 95, 214-220.' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_XPA _Saveframe_category molecular_system _Mol_system_name 'Human NER factor XPA' _Abbreviation_common XPA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label XPA $XPA Zn $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Involved in the nucleotide excision repair' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_XPA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common XPA _Abbreviation_common XPA _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MEFDYVICEECGKEFMDSYL MNHFDLPTCDNCRDADDKHK LITKTEAKQEYLLKDCDLEK REPPLKFIVKKNPHHSQWGD MKLYLKLQIVKRSLEVWGSQ EALEEAKEVRQENREKMKQK KF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 98 MET 2 99 GLU 3 100 PHE 4 101 ASP 5 102 TYR 6 103 VAL 7 104 ILE 8 105 CYS 9 106 GLU 10 107 GLU 11 108 CYS 12 109 GLY 13 110 LYS 14 111 GLU 15 112 PHE 16 113 MET 17 114 ASP 18 115 SER 19 116 TYR 20 117 LEU 21 118 MET 22 119 ASN 23 120 HIS 24 121 PHE 25 122 ASP 26 123 LEU 27 124 PRO 28 125 THR 29 126 CYS 30 127 ASP 31 128 ASN 32 129 CYS 33 130 ARG 34 131 ASP 35 132 ALA 36 133 ASP 37 134 ASP 38 135 LYS 39 136 HIS 40 137 LYS 41 138 LEU 42 139 ILE 43 140 THR 44 141 LYS 45 142 THR 46 143 GLU 47 144 ALA 48 145 LYS 49 146 GLN 50 147 GLU 51 148 TYR 52 149 LEU 53 150 LEU 54 151 LYS 55 152 ASP 56 153 CYS 57 154 ASP 58 155 LEU 59 156 GLU 60 157 LYS 61 158 ARG 62 159 GLU 63 160 PRO 64 161 PRO 65 162 LEU 66 163 LYS 67 164 PHE 68 165 ILE 69 166 VAL 70 167 LYS 71 168 LYS 72 169 ASN 73 170 PRO 74 171 HIS 75 172 HIS 76 173 SER 77 174 GLN 78 175 TRP 79 176 GLY 80 177 ASP 81 178 MET 82 179 LYS 83 180 LEU 84 181 TYR 85 182 LEU 86 183 LYS 87 184 LEU 88 185 GLN 89 186 ILE 90 187 VAL 91 188 LYS 92 189 ARG 93 190 SER 94 191 LEU 95 192 GLU 96 193 VAL 97 194 TRP 98 195 GLY 99 196 SER 100 197 GLN 101 198 GLU 102 199 ALA 103 200 LEU 104 201 GLU 105 202 GLU 106 203 ALA 107 204 LYS 108 205 GLU 109 206 VAL 110 207 ARG 111 208 GLN 112 209 GLU 113 210 ASN 114 211 ARG 115 212 GLU 116 213 LYS 117 214 MET 118 215 LYS 119 216 GLN 120 217 LYS 121 218 LYS 122 219 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 PDB 1D4U "Interactions Of Human Nucleotide Excision Repair Protein Xpa With Rpa70 And Dna: Chemical Shift Mapping And 15n Nmr Relaxation " 90.98 111 98.20 100.00 1.01e-73 PDB 1XPA "Solution Structure Of The Dna-And Rpa-Binding Domain Of The Human Repair Factor Xpa, Nmr, 1 Structure" 100.00 122 100.00 100.00 2.77e-83 DBJ BAA03403 "XPAC protein [Homo sapiens]" 100.00 273 100.00 100.00 1.48e-83 DBJ BAJ20553 "xeroderma pigmentosum, complementation group A [synthetic construct]" 100.00 273 100.00 100.00 1.48e-83 GB AAA92883 "XPAC, partial [Homo sapiens]" 100.00 215 100.00 100.00 1.47e-82 GB AAH14965 "Xeroderma pigmentosum, complementation group A [Homo sapiens]" 100.00 273 100.00 100.00 1.48e-83 GB AAM18969 "xeroderma pigmentosum, complementation group A [Homo sapiens]" 100.00 273 100.00 100.00 1.48e-83 GB AAV38325 "xeroderma pigmentosum, complementation group A [Homo sapiens]" 100.00 273 100.00 100.00 1.48e-83 GB AAX29766 "xeroderma pigmentosum complementation group A [synthetic construct]" 100.00 274 99.18 99.18 1.34e-82 PRF 1701435A "DNA excision repair gene" 100.00 273 100.00 100.00 1.48e-83 REF NP_000371 "DNA repair protein complementing XP-A cells [Homo sapiens]" 100.00 273 100.00 100.00 1.48e-83 REF XP_001114093 "PREDICTED: DNA repair protein complementing XP-A cells [Macaca mulatta]" 100.00 273 100.00 100.00 1.90e-83 REF XP_001156167 "PREDICTED: DNA repair protein complementing XP-A cells isoform X2 [Pan troglodytes]" 100.00 273 100.00 100.00 1.49e-83 REF XP_002743160 "PREDICTED: DNA repair protein complementing XP-A cells [Callithrix jacchus]" 100.00 272 99.18 99.18 1.94e-82 REF XP_002820062 "PREDICTED: DNA repair protein complementing XP-A cells [Pongo abelii]" 100.00 273 100.00 100.00 1.82e-83 SP P23025 "RecName: Full=DNA repair protein complementing XP-A cells; AltName: Full=Xeroderma pigmentosum group A-complementing protein" 100.00 273 100.00 100.00 1.48e-83 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 15:20:29 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $XPA 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 _Details $XPA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET16b ; E.coli cells of strain BL21(DE3) transformed with the plasmids which carried the central domain of XPA (Met98-Phe219) under the control of T7 phi 10 promoter were used. ; 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 _Isotopic_labeling $system_XPA 1.2 mM '[U-13C; U-15N]' $ZN 0.02 mM . KCl 150 mM . DTT 10 mM . 'Deuterated Tris-HCl' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name NMRPIPE _Version 1.6 loop_ _Task 'Data processing' stop_ _Details . _Citation_label $citation_two save_ save_software_two _Saveframe_category software _Name PIPP _Version 4.0.4 loop_ _Task 'Peak picker' stop_ _Details . _Citation_label $citation_three save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX500 _Field_strength 500 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX800 _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ save_NMR_applied_experiment_one _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details '3D-4D Multi-dimensional experiments' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.3 0.2 n/a pressure 1 . atm temperature 303 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144952 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.10132905 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_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 XPA _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 MET HA H 4.21 . 1 2 . 1 MET HB2 H 2.05 . 2 3 . 1 MET HB3 H 3.15 . 2 4 . 1 MET HG2 H 2.35 . 2 5 . 1 MET HE H 2.00 . 1 6 . 1 MET C C 176.43 . 1 7 . 1 MET CA C 56.92 . 1 8 . 1 MET CB C 28.81 . 1 9 . 1 MET CG C 30.53 . 1 10 . 1 MET CE C 16.83 . 1 11 . 2 GLU HA H 4.15 . 1 12 . 2 GLU HB2 H 1.98 . 2 13 . 2 GLU HG2 H 2.01 . 2 14 . 2 GLU C C 175.38 . 1 15 . 2 GLU CA C 56.49 . 1 16 . 2 GLU CB C 29.99 . 1 17 . 2 GLU CG C 36.11 . 1 18 . 3 PHE H H 7.98 . 1 19 . 3 PHE HA H 4.53 . 1 20 . 3 PHE HB2 H 2.90 . 2 21 . 3 PHE HB3 H 2.67 . 2 22 . 3 PHE HD1 H 7.10 . 3 23 . 3 PHE HE1 H 6.71 . 3 24 . 3 PHE HZ H 7.20 . 1 25 . 3 PHE C C 174.62 . 1 26 . 3 PHE CA C 56.88 . 1 27 . 3 PHE CB C 40.10 . 1 28 . 3 PHE CD1 C 131.90 . 1 29 . 3 PHE N N 120.02 . 1 30 . 4 ASP H H 8.14 . 1 31 . 4 ASP HA H 4.58 . 1 32 . 4 ASP HB2 H 2.54 . 2 33 . 4 ASP HB3 H 2.39 . 2 34 . 4 ASP C C 174.97 . 1 35 . 4 ASP CA C 53.83 . 1 36 . 4 ASP CB C 41.39 . 1 37 . 4 ASP N N 121.73 . 1 38 . 5 TYR H H 7.65 . 1 39 . 5 TYR HA H 4.49 . 1 40 . 5 TYR HB2 H 2.76 . 2 41 . 5 TYR HB3 H 2.65 . 2 42 . 5 TYR HD1 H 6.83 . 3 43 . 5 TYR HE1 H 6.72 . 3 44 . 5 TYR C C 174.91 . 1 45 . 5 TYR CA C 57.46 . 1 46 . 5 TYR CB C 39.84 . 1 47 . 5 TYR N N 118.42 . 1 48 . 6 VAL H H 8.53 . 1 49 . 6 VAL HA H 3.93 . 1 50 . 6 VAL HB H 0.66 . 1 51 . 6 VAL HG1 H 0.62 . 1 52 . 6 VAL HG2 H 0.39 . 1 53 . 6 VAL C C 173.58 . 1 54 . 6 VAL CA C 60.45 . 1 55 . 6 VAL CB C 33.15 . 1 56 . 6 VAL CG1 C 22.99 . 1 57 . 6 VAL CG2 C 20.84 . 1 58 . 6 VAL N N 122.45 . 1 59 . 7 ILE H H 7.84 . 1 60 . 7 ILE HA H 4.26 . 1 61 . 7 ILE HB H 1.74 . 1 62 . 7 ILE HG12 H 1.43 . 2 63 . 7 ILE HG13 H 1.17 . 2 64 . 7 ILE HG2 H 0.69 . 1 65 . 7 ILE HD1 H 0.74 . 1 66 . 7 ILE C C 175.83 . 1 67 . 7 ILE CA C 59.15 . 1 68 . 7 ILE CB C 37.84 . 1 69 . 7 ILE CG1 C 27.47 . 1 70 . 7 ILE CG2 C 17.19 . 1 71 . 7 ILE CD1 C 11.74 . 1 72 . 7 ILE N N 123.78 . 1 73 . 8 CYS H H 8.77 . 1 74 . 8 CYS HA H 4.72 . 1 75 . 8 CYS HB2 H 2.88 . 2 76 . 8 CYS HB3 H 3.54 . 2 77 . 8 CYS C C 178.22 . 1 78 . 8 CYS CA C 59.76 . 1 79 . 8 CYS CB C 30.95 . 1 80 . 8 CYS N N 128.79 . 1 81 . 9 GLU H H 9.43 . 1 82 . 9 GLU HA H 4.21 . 1 83 . 9 GLU HB2 H 2.19 . 2 84 . 9 GLU HG2 H 2.43 . 2 85 . 9 GLU C C 176.12 . 1 86 . 9 GLU CA C 58.28 . 1 87 . 9 GLU CB C 30.10 . 1 88 . 9 GLU CG C 35.90 . 1 89 . 9 GLU N N 131.98 . 1 90 . 10 GLU H H 9.18 . 1 91 . 10 GLU HA H 4.61 . 1 92 . 10 GLU HB2 H 2.28 . 2 93 . 10 GLU HG2 H 2.32 . 2 94 . 10 GLU C C 177.55 . 1 95 . 10 GLU CA C 57.81 . 1 96 . 10 GLU CB C 30.88 . 1 97 . 10 GLU CG C 35.97 . 1 98 . 10 GLU N N 121.79 . 1 99 . 11 CYS H H 8.33 . 1 100 . 11 CYS HA H 4.89 . 1 101 . 11 CYS HB2 H 3.16 . 2 102 . 11 CYS HB3 H 2.73 . 2 103 . 11 CYS C C 177.37 . 1 104 . 11 CYS CA C 59.07 . 1 105 . 11 CYS CB C 32.86 . 1 106 . 11 CYS N N 117.99 . 1 107 . 12 GLY H H 8.04 . 1 108 . 12 GLY HA2 H 4.10 . 2 109 . 12 GLY HA3 H 3.85 . 2 110 . 12 GLY C C 173.51 . 1 111 . 12 GLY CA C 46.18 . 1 112 . 12 GLY N N 113.38 . 1 113 . 13 LYS H H 8.54 . 1 114 . 13 LYS HA H 4.45 . 1 115 . 13 LYS HB2 H 1.87 . 2 116 . 13 LYS HB3 H 2.10 . 2 117 . 13 LYS HG2 H 1.51 . 2 118 . 13 LYS HD2 H 1.72 . 2 119 . 13 LYS HE2 H 3.02 . 2 120 . 13 LYS C C 176.31 . 1 121 . 13 LYS CA C 56.28 . 1 122 . 13 LYS CB C 33.49 . 1 123 . 13 LYS CG C 25.42 . 1 124 . 13 LYS CD C 29.06 . 1 125 . 13 LYS CE C 42.22 . 1 126 . 13 LYS N N 122.59 . 1 127 . 14 GLU H H 8.49 . 1 128 . 14 GLU HA H 4.97 . 1 129 . 14 GLU HB2 H 1.67 . 2 130 . 14 GLU HB3 H 1.50 . 2 131 . 14 GLU HG2 H 2.08 . 2 132 . 14 GLU HG3 H 1.91 . 2 133 . 14 GLU C C 176.99 . 1 134 . 14 GLU CA C 55.78 . 1 135 . 14 GLU CB C 30.68 . 1 136 . 14 GLU CG C 36.70 . 1 137 . 14 GLU N N 122.03 . 1 138 . 15 PHE H H 9.49 . 1 139 . 15 PHE HA H 5.01 . 1 140 . 15 PHE HB2 H 3.06 . 2 141 . 15 PHE HD1 H 7.05 . 3 142 . 15 PHE HE1 H 6.75 . 3 143 . 15 PHE C C 172.12 . 1 144 . 15 PHE CA C 56.24 . 1 145 . 15 PHE CB C 41.57 . 1 146 . 15 PHE CD1 C 133.17 . 1 147 . 15 PHE N N 121.58 . 1 148 . 16 MET H H 8.73 . 1 149 . 16 MET HA H 4.53 . 1 150 . 16 MET HB2 H 1.90 . 2 151 . 16 MET HB3 H 1.96 . 2 152 . 16 MET HG2 H 2.32 . 2 153 . 16 MET HE H 1.82 . 1 154 . 16 MET C C 174.90 . 1 155 . 16 MET CA C 56.32 . 1 156 . 16 MET CB C 34.25 . 1 157 . 16 MET CG C 31.98 . 1 158 . 16 MET CE C 16.72 . 1 159 . 16 MET N N 118.85 . 1 160 . 17 ASP H H 7.94 . 1 161 . 17 ASP HA H 4.96 . 1 162 . 17 ASP HB2 H 2.61 . 2 163 . 17 ASP C C 174.79 . 1 164 . 17 ASP CA C 53.31 . 1 165 . 17 ASP CB C 44.10 . 1 166 . 17 ASP N N 117.53 . 1 167 . 18 SER H H 8.15 . 1 168 . 18 SER HA H 4.89 . 1 169 . 18 SER HB2 H 3.88 . 2 170 . 18 SER C C 172.42 . 1 171 . 18 SER CA C 56.33 . 1 172 . 18 SER CB C 66.09 . 1 173 . 18 SER N N 116.38 . 1 174 . 19 TYR H H 10.47 . 1 175 . 19 TYR HA H 4.29 . 1 176 . 19 TYR HB2 H 2.79 . 2 177 . 19 TYR HB3 H 3.34 . 2 178 . 19 TYR HD1 H 7.04 . 3 179 . 19 TYR HE1 H 6.69 . 3 180 . 19 TYR C C 178.41 . 1 181 . 19 TYR CA C 62.46 . 1 182 . 19 TYR CB C 39.26 . 1 183 . 19 TYR CD1 C 132.84 . 1 184 . 19 TYR CE1 C 118.28 . 1 185 . 19 TYR N N 126.54 . 1 186 . 20 LEU H H 9.15 . 1 187 . 20 LEU HA H 4.30 . 1 188 . 20 LEU HB2 H 1.59 . 2 189 . 20 LEU HG H 1.96 . 1 190 . 20 LEU HD1 H 0.16 . 1 191 . 20 LEU HD2 H 1.12 . 1 192 . 20 LEU C C 179.61 . 1 193 . 20 LEU CA C 57.73 . 1 194 . 20 LEU CB C 40.70 . 1 195 . 20 LEU CG C 25.73 . 1 196 . 20 LEU CD1 C 25.84 . 1 197 . 20 LEU CD2 C 23.60 . 1 198 . 20 LEU N N 119.08 . 1 199 . 21 MET H H 8.27 . 1 200 . 21 MET HA H 4.27 . 1 201 . 21 MET HB2 H 2.38 . 2 202 . 21 MET HG2 H 2.73 . 2 203 . 21 MET HE H 1.94 . 1 204 . 21 MET C C 178.67 . 1 205 . 21 MET CA C 57.82 . 1 206 . 21 MET CB C 32.88 . 1 207 . 21 MET CG C 33.29 . 1 208 . 21 MET CE C 17.86 . 1 209 . 21 MET N N 124.35 . 1 210 . 22 ASN H H 8.56 . 1 211 . 22 ASN HA H 4.19 . 1 212 . 22 ASN HB2 H 2.72 . 2 213 . 22 ASN HB3 H 2.21 . 2 214 . 22 ASN HD21 H 7.04 . 1 215 . 22 ASN C C 177.36 . 1 216 . 22 ASN CA C 56.12 . 1 217 . 22 ASN CB C 38.15 . 1 218 . 22 ASN N N 118.46 . 1 219 . 22 ASN ND2 N 112.65 . 1 220 . 23 HIS H H 7.63 . 1 221 . 23 HIS HA H 4.05 . 1 222 . 23 HIS HB2 H 1.57 . 2 223 . 23 HIS HB3 H 2.05 . 2 224 . 23 HIS HD2 H 7.24 . 1 225 . 23 HIS C C 175.43 . 1 226 . 23 HIS CA C 58.06 . 1 227 . 23 HIS CB C 29.88 . 1 228 . 23 HIS N N 111.72 . 1 229 . 24 PHE H H 7.13 . 1 230 . 24 PHE HA H 4.91 . 1 231 . 24 PHE HB2 H 3.69 . 2 232 . 24 PHE HB3 H 2.86 . 2 233 . 24 PHE HD1 H 7.24 . 3 234 . 24 PHE HE1 H 7.28 . 3 235 . 24 PHE HZ H 6.96 . 1 236 . 24 PHE C C 174.35 . 1 237 . 24 PHE CA C 57.25 . 1 238 . 24 PHE CB C 41.20 . 1 239 . 24 PHE CD1 C 132.86 . 1 240 . 24 PHE N N 112.38 . 1 241 . 25 ASP H H 7.85 . 1 242 . 25 ASP HA H 4.68 . 1 243 . 25 ASP HB2 H 2.94 . 2 244 . 25 ASP C C 174.47 . 1 245 . 25 ASP CA C 55.91 . 1 246 . 25 ASP CB C 39.48 . 1 247 . 25 ASP N N 117.05 . 1 248 . 26 LEU H H 7.70 . 1 249 . 26 LEU HA H 4.85 . 1 250 . 26 LEU HG H 1.58 . 1 251 . 26 LEU HD1 H 0.99 . 1 252 . 26 LEU HD2 H 0.93 . 1 253 . 26 LEU C C 175.34 . 1 254 . 26 LEU CA C 51.56 . 1 255 . 26 LEU CB C 44.71 . 1 256 . 26 LEU CD1 C 25.10 . 1 257 . 26 LEU CD2 C 27.38 . 1 258 . 26 LEU N N 124.21 . 1 259 . 27 PRO HA H 4.86 . 1 260 . 27 PRO HB2 H 2.65 . 2 261 . 27 PRO HG2 H 2.07 . 2 262 . 27 PRO HD2 H 3.68 . 2 263 . 27 PRO HD3 H 3.74 . 2 264 . 27 PRO C C 173.51 . 1 265 . 27 PRO CA C 62.50 . 1 266 . 27 PRO CB C 27.73 . 1 267 . 27 PRO CG C 26.01 . 1 268 . 27 PRO CD C 50.84 . 1 269 . 28 THR H H 8.76 . 1 270 . 28 THR HA H 5.56 . 1 271 . 28 THR HB H 3.38 . 1 272 . 28 THR HG2 H 0.95 . 1 273 . 28 THR C C 174.57 . 1 274 . 28 THR CA C 61.14 . 1 275 . 28 THR CB C 71.80 . 1 276 . 28 THR CG2 C 22.91 . 1 277 . 28 THR N N 123.91 . 1 278 . 29 CYS H H 9.74 . 1 279 . 29 CYS HA H 3.21 . 1 280 . 29 CYS HB2 H 2.02 . 2 281 . 29 CYS HB3 H 2.93 . 2 282 . 29 CYS C C 174.89 . 1 283 . 29 CYS CA C 58.51 . 1 284 . 29 CYS CB C 30.71 . 1 285 . 29 CYS N N 135.89 . 1 286 . 30 ASP H H 8.93 . 1 287 . 30 ASP HA H 4.42 . 1 288 . 30 ASP HB2 H 2.58 . 2 289 . 30 ASP HB3 H 2.69 . 2 290 . 30 ASP C C 178.09 . 1 291 . 30 ASP CA C 57.24 . 1 292 . 30 ASP CB C 40.41 . 1 293 . 30 ASP N N 117.47 . 1 294 . 31 ASN H H 8.50 . 1 295 . 31 ASN HA H 4.56 . 1 296 . 31 ASN HB2 H 2.84 . 2 297 . 31 ASN HB3 H 2.97 . 2 298 . 31 ASN HD21 H 7.00 . 1 299 . 31 ASN HD22 H 7.77 . 1 300 . 31 ASN C C 176.58 . 1 301 . 31 ASN CA C 55.88 . 1 302 . 31 ASN CB C 38.86 . 1 303 . 31 ASN N N 121.18 . 1 304 . 31 ASN ND2 N 115.19 . 1 305 . 32 CYS H H 7.68 . 1 306 . 32 CYS HA H 3.98 . 1 307 . 32 CYS HB2 H 2.57 . 2 308 . 32 CYS HB3 H 2.79 . 2 309 . 32 CYS C C 174.73 . 1 310 . 32 CYS CA C 61.20 . 1 311 . 32 CYS CB C 30.55 . 1 312 . 32 CYS N N 122.09 . 1 313 . 33 ARG H H 6.79 . 1 314 . 33 ARG HA H 3.88 . 1 315 . 33 ARG HB2 H 2.20 . 2 316 . 33 ARG C C 175.14 . 1 317 . 33 ARG CA C 56.28 . 1 318 . 33 ARG CB C 30.32 . 1 319 . 33 ARG N N 121.12 . 1 320 . 34 ASP HA H 4.96 . 1 321 . 34 ASP HB2 H 2.62 . 2 322 . 34 ASP HB3 H 2.99 . 2 323 . 34 ASP C C 176.43 . 1 324 . 34 ASP CA C 51.61 . 1 325 . 34 ASP CB C 41.35 . 1 326 . 35 ALA H H 8.81 . 1 327 . 35 ALA HA H 3.83 . 1 328 . 35 ALA HB H 1.25 . 1 329 . 35 ALA C C 177.14 . 1 330 . 35 ALA CA C 53.74 . 1 331 . 35 ALA CB C 18.75 . 1 332 . 35 ALA N N 126.57 . 1 333 . 36 ASP H H 7.72 . 1 334 . 36 ASP HA H 4.62 . 1 335 . 36 ASP HB2 H 2.53 . 2 336 . 36 ASP HB3 H 2.67 . 2 337 . 36 ASP C C 176.26 . 1 338 . 36 ASP CA C 55.16 . 1 339 . 36 ASP CB C 42.03 . 1 340 . 36 ASP N N 113.66 . 1 341 . 37 ASP H H 7.11 . 1 342 . 37 ASP HA H 4.69 . 1 343 . 37 ASP HB2 H 2.47 . 2 344 . 37 ASP HB3 H 3.07 . 2 345 . 37 ASP C C 176.27 . 1 346 . 37 ASP CA C 55.69 . 1 347 . 37 ASP CB C 41.74 . 1 348 . 37 ASP N N 117.91 . 1 349 . 38 LYS H H 8.10 . 1 350 . 38 LYS HA H 3.64 . 1 351 . 38 LYS HB2 H 1.30 . 2 352 . 38 LYS HB3 H 1.69 . 2 353 . 38 LYS HG2 H 1.09 . 2 354 . 38 LYS HD2 H 1.47 . 2 355 . 38 LYS HD3 H 1.66 . 2 356 . 38 LYS HE2 H 2.80 . 2 357 . 38 LYS C C 178.11 . 1 358 . 38 LYS CA C 60.69 . 1 359 . 38 LYS CB C 33.14 . 1 360 . 38 LYS CG C 24.85 . 1 361 . 38 LYS CD C 29.89 . 1 362 . 38 LYS CE C 41.78 . 1 363 . 38 LYS N N 122.98 . 1 364 . 39 HIS H H 8.52 . 1 365 . 39 HIS HA H 4.78 . 1 366 . 39 HIS HB2 H 2.45 . 2 367 . 39 HIS HB3 H 3.24 . 2 368 . 39 HIS HD2 H 6.50 . 1 369 . 39 HIS HE1 H 7.64 . 1 370 . 39 HIS C C 173.46 . 1 371 . 39 HIS CA C 55.39 . 1 372 . 39 HIS CB C 30.07 . 1 373 . 39 HIS CD2 C 114.44 . 1 374 . 39 HIS N N 114.18 . 1 375 . 40 LYS H H 6.71 . 1 376 . 40 LYS HA H 4.23 . 1 377 . 40 LYS HB2 H 1.43 . 2 378 . 40 LYS HB3 H 1.70 . 2 379 . 40 LYS HG2 H 1.30 . 2 380 . 40 LYS HD2 H 1.49 . 2 381 . 40 LYS HE2 H 3.02 . 2 382 . 40 LYS C C 176.12 . 1 383 . 40 LYS CA C 56.51 . 1 384 . 40 LYS CB C 33.60 . 1 385 . 40 LYS CG C 23.96 . 1 386 . 40 LYS CD C 29.58 . 1 387 . 40 LYS CE C 41.83 . 1 388 . 40 LYS N N 118.23 . 1 389 . 41 LEU H H 8.28 . 1 390 . 41 LEU HA H 5.24 . 1 391 . 41 LEU HB2 H 1.43 . 2 392 . 41 LEU HB3 H 1.78 . 2 393 . 41 LEU HG H 1.87 . 1 394 . 41 LEU HD1 H 1.02 . 1 395 . 41 LEU HD2 H 0.75 . 1 396 . 41 LEU C C 176.91 . 1 397 . 41 LEU CA C 53.31 . 1 398 . 41 LEU CB C 43.40 . 1 399 . 41 LEU CG C 26.71 . 1 400 . 41 LEU CD1 C 26.54 . 1 401 . 41 LEU CD2 C 24.06 . 1 402 . 41 LEU N N 123.68 . 1 403 . 42 ILE H H 9.44 . 1 404 . 42 ILE HA H 4.88 . 1 405 . 42 ILE HB H 1.83 . 1 406 . 42 ILE HG12 H 1.66 . 2 407 . 42 ILE HG13 H 1.17 . 2 408 . 42 ILE HG2 H 0.87 . 1 409 . 42 ILE HD1 H 0.84 . 1 410 . 42 ILE C C 174.16 . 1 411 . 42 ILE CA C 59.06 . 1 412 . 42 ILE CB C 42.53 . 1 413 . 42 ILE CG1 C 26.31 . 1 414 . 42 ILE CG2 C 17.24 . 1 415 . 42 ILE CD1 C 14.15 . 1 416 . 42 ILE N N 118.63 . 1 417 . 43 THR H H 8.77 . 1 418 . 43 THR HA H 4.98 . 1 419 . 43 THR HB H 4.97 . 1 420 . 43 THR HG2 H 1.40 . 1 421 . 43 THR C C 175.91 . 1 422 . 43 THR CA C 61.61 . 1 423 . 43 THR CB C 71.32 . 1 424 . 43 THR CG2 C 22.39 . 1 425 . 43 THR N N 115.71 . 1 426 . 44 LYS H H 8.76 . 1 427 . 44 LYS HA H 3.81 . 1 428 . 44 LYS HB2 H 2.30 . 2 429 . 44 LYS HG2 H 1.59 . 2 430 . 44 LYS HD2 H 1.98 . 2 431 . 44 LYS HE2 H 2.55 . 2 432 . 44 LYS C C 177.77 . 1 433 . 44 LYS CA C 60.44 . 1 434 . 44 LYS CB C 33.56 . 1 435 . 44 LYS CG C 25.64 . 1 436 . 44 LYS CD C 29.95 . 1 437 . 44 LYS CE C 42.59 . 1 438 . 44 LYS N N 122.20 . 1 439 . 45 THR H H 7.84 . 1 440 . 45 THR HA H 3.84 . 1 441 . 45 THR HB H 4.09 . 1 442 . 45 THR HG2 H 1.22 . 1 443 . 45 THR C C 176.25 . 1 444 . 45 THR CA C 66.57 . 1 445 . 45 THR CB C 68.80 . 1 446 . 45 THR CG2 C 21.75 . 1 447 . 45 THR N N 112.62 . 1 448 . 46 GLU H H 7.88 . 1 449 . 46 GLU HA H 4.05 . 1 450 . 46 GLU HB2 H 2.19 . 2 451 . 46 GLU HG2 H 2.25 . 2 452 . 46 GLU C C 178.47 . 1 453 . 46 GLU CA C 59.66 . 1 454 . 46 GLU CB C 29.74 . 1 455 . 46 GLU CG C 37.27 . 1 456 . 46 GLU N N 123.54 . 1 457 . 47 ALA H H 8.74 . 1 458 . 47 ALA HA H 4.06 . 1 459 . 47 ALA HB H 1.34 . 1 460 . 47 ALA C C 179.26 . 1 461 . 47 ALA CA C 55.22 . 1 462 . 47 ALA CB C 18.38 . 1 463 . 47 ALA N N 121.63 . 1 464 . 48 LYS H H 8.17 . 1 465 . 48 LYS HA H 4.04 . 1 466 . 48 LYS HB2 H 1.33 . 2 467 . 48 LYS HB3 H 1.94 . 2 468 . 48 LYS HD2 H 1.71 . 2 469 . 48 LYS HE2 H 2.90 . 2 470 . 48 LYS C C 179.43 . 1 471 . 48 LYS CA C 60.42 . 1 472 . 48 LYS CB C 32.29 . 1 473 . 48 LYS CG C 25.25 . 1 474 . 48 LYS CD C 32.01 . 1 475 . 48 LYS CE C 41.56 . 1 476 . 48 LYS N N 115.12 . 1 477 . 49 GLN H H 7.92 . 1 478 . 49 GLN HA H 4.09 . 1 479 . 49 GLN HB2 H 2.17 . 2 480 . 49 GLN HB3 H 2.08 . 2 481 . 49 GLN HG2 H 2.40 . 2 482 . 49 GLN HE21 H 7.48 . 1 483 . 49 GLN HE22 H 6.82 . 1 484 . 49 GLN C C 177.83 . 1 485 . 49 GLN CA C 58.56 . 1 486 . 49 GLN CB C 29.50 . 1 487 . 49 GLN CG C 33.92 . 1 488 . 49 GLN N N 117.14 . 1 489 . 49 GLN NE2 N 113.02 . 1 490 . 50 GLU H H 8.71 . 1 491 . 50 GLU HA H 3.96 . 1 492 . 50 GLU HB2 H 1.49 . 2 493 . 50 GLU HG2 H 2.03 . 2 494 . 50 GLU C C 177.23 . 1 495 . 50 GLU CA C 57.42 . 1 496 . 50 GLU CB C 29.70 . 1 497 . 50 GLU CG C 35.64 . 1 498 . 50 GLU N N 116.13 . 1 499 . 51 TYR H H 7.19 . 1 500 . 51 TYR HA H 4.40 . 1 501 . 51 TYR HB2 H 2.85 . 2 502 . 51 TYR HB3 H 3.22 . 2 503 . 51 TYR HD1 H 7.14 . 3 504 . 51 TYR HE1 H 6.62 . 3 505 . 51 TYR C C 172.42 . 1 506 . 51 TYR CA C 57.97 . 1 507 . 51 TYR CB C 36.98 . 1 508 . 51 TYR N N 113.78 . 1 509 . 52 LEU H H 6.98 . 1 510 . 52 LEU HA H 4.07 . 1 511 . 52 LEU HB2 H 1.80 . 2 512 . 52 LEU HB3 H 1.85 . 2 513 . 52 LEU HG H 1.26 . 1 514 . 52 LEU HD1 H 0.46 . 1 515 . 52 LEU HD2 H 0.68 . 1 516 . 52 LEU C C 176.13 . 1 517 . 52 LEU CA C 55.63 . 1 518 . 52 LEU CB C 39.25 . 1 519 . 52 LEU CG C 26.48 . 1 520 . 52 LEU CD1 C 26.41 . 1 521 . 52 LEU CD2 C 23.83 . 1 522 . 52 LEU N N 116.03 . 1 523 . 53 LEU H H 7.41 . 1 524 . 53 LEU HA H 4.91 . 1 525 . 53 LEU HB2 H 1.26 . 2 526 . 53 LEU HB3 H 1.33 . 2 527 . 53 LEU HG H 1.75 . 1 528 . 53 LEU HD1 H 0.70 . 1 529 . 53 LEU HD2 H 0.86 . 1 530 . 53 LEU C C 176.30 . 1 531 . 53 LEU CA C 52.82 . 1 532 . 53 LEU CB C 44.97 . 1 533 . 53 LEU CG C 26.85 . 1 534 . 53 LEU CD1 C 27.08 . 1 535 . 53 LEU CD2 C 23.68 . 1 536 . 53 LEU N N 117.84 . 1 537 . 54 LYS H H 9.43 . 1 538 . 54 LYS HA H 4.55 . 1 539 . 54 LYS HG2 H 1.20 . 2 540 . 54 LYS C C 178.51 . 1 541 . 54 LYS CA C 54.42 . 1 542 . 54 LYS CB C 35.61 . 1 543 . 54 LYS N N 121.91 . 1 544 . 56 CYS HA H 4.25 . 1 545 . 56 CYS HB2 H 2.88 . 2 546 . 56 CYS HB3 H 3.07 . 2 547 . 56 CYS C C 176.44 . 1 548 . 56 CYS CA C 60.14 . 1 549 . 56 CYS CB C 26.91 . 1 550 . 57 ASP H H 7.34 . 1 551 . 57 ASP HA H 4.31 . 1 552 . 57 ASP HB2 H 2.87 . 2 553 . 57 ASP HB3 H 3.01 . 2 554 . 57 ASP C C 176.12 . 1 555 . 57 ASP CA C 57.25 . 1 556 . 57 ASP CB C 42.92 . 1 557 . 57 ASP N N 123.69 . 1 558 . 58 LEU H H 7.24 . 1 559 . 58 LEU HA H 4.14 . 1 560 . 58 LEU HB2 H 1.99 . 2 561 . 58 LEU HG H 1.57 . 1 562 . 58 LEU HD1 H 0.53 . 1 563 . 58 LEU HD2 H 0.31 . 1 564 . 58 LEU C C 177.68 . 1 565 . 58 LEU CA C 56.73 . 1 566 . 58 LEU CB C 42.76 . 1 567 . 58 LEU CG C 24.73 . 1 568 . 58 LEU CD1 C 25.02 . 1 569 . 58 LEU CD2 C 23.87 . 1 570 . 58 LEU N N 116.79 . 1 571 . 59 GLU H H 7.99 . 1 572 . 59 GLU HA H 4.50 . 1 573 . 59 GLU HB2 H 1.87 . 2 574 . 59 GLU C C 176.71 . 1 575 . 59 GLU CA C 57.35 . 1 576 . 59 GLU CB C 32.52 . 1 577 . 59 GLU CG C 35.94 . 1 578 . 59 GLU N N 114.66 . 1 579 . 60 LYS H H 7.91 . 1 580 . 60 LYS HA H 4.49 . 1 581 . 60 LYS HB2 H 1.95 . 2 582 . 60 LYS HB3 H 1.89 . 2 583 . 60 LYS HG2 H 1.44 . 2 584 . 60 LYS HG3 H 1.34 . 2 585 . 60 LYS HD2 H 1.63 . 2 586 . 60 LYS HE2 H 2.94 . 2 587 . 60 LYS C C 176.61 . 1 588 . 60 LYS CA C 55.89 . 1 589 . 60 LYS CB C 33.36 . 1 590 . 60 LYS CG C 24.81 . 1 591 . 60 LYS CD C 28.97 . 1 592 . 60 LYS CE C 42.07 . 1 593 . 60 LYS N N 117.24 . 1 594 . 61 ARG H H 6.90 . 1 595 . 61 ARG HA H 4.13 . 1 596 . 61 ARG HB2 H 1.69 . 2 597 . 61 ARG HG2 H 2.18 . 2 598 . 61 ARG HD2 H 3.06 . 2 599 . 61 ARG C C 174.51 . 1 600 . 61 ARG CA C 56.14 . 1 601 . 61 ARG CB C 30.50 . 1 602 . 61 ARG CG C 28.78 . 1 603 . 61 ARG CD C 43.36 . 1 604 . 61 ARG N N 120.67 . 1 605 . 62 GLU H H 8.18 . 1 606 . 62 GLU HA H 4.16 . 1 607 . 62 GLU C C 175.44 . 1 608 . 62 GLU CA C 54.60 . 1 609 . 62 GLU CB C 30.66 . 1 610 . 62 GLU N N 123.08 . 1 611 . 63 PRO HA H 5.03 . 1 612 . 63 PRO HG2 H 1.99 . 2 613 . 63 PRO HD2 H 3.45 . 2 614 . 63 PRO HD3 H 3.54 . 2 615 . 63 PRO CA C 60.80 . 1 616 . 63 PRO CD C 50.17 . 1 617 . 64 PRO HA H 4.45 . 1 618 . 64 PRO HB2 H 2.36 . 2 619 . 64 PRO HG2 H 1.88 . 2 620 . 64 PRO HD2 H 3.64 . 2 621 . 64 PRO HD3 H 3.78 . 2 622 . 64 PRO C C 177.39 . 1 623 . 64 PRO CA C 62.99 . 1 624 . 64 PRO CB C 31.83 . 1 625 . 64 PRO CG C 27.76 . 1 626 . 64 PRO CD C 50.31 . 1 627 . 65 LEU H H 8.11 . 1 628 . 65 LEU HA H 4.58 . 1 629 . 65 LEU HB2 H 1.92 . 2 630 . 65 LEU HB3 H 2.24 . 2 631 . 65 LEU HG H 1.93 . 1 632 . 65 LEU HD1 H 0.89 . 1 633 . 65 LEU HD2 H 0.94 . 1 634 . 65 LEU C C 178.07 . 1 635 . 65 LEU CA C 55.24 . 1 636 . 65 LEU CB C 42.48 . 1 637 . 65 LEU CG C 28.65 . 1 638 . 65 LEU CD1 C 26.06 . 1 639 . 65 LEU CD2 C 23.92 . 1 640 . 65 LEU N N 122.95 . 1 641 . 66 LYS H H 9.62 . 1 642 . 66 LYS HA H 4.28 . 1 643 . 66 LYS HB2 H 2.06 . 2 644 . 66 LYS HB3 H 1.85 . 2 645 . 66 LYS HG2 H 1.26 . 2 646 . 66 LYS HD2 H 1.47 . 2 647 . 66 LYS HE2 H 2.86 . 2 648 . 66 LYS C C 173.92 . 1 649 . 66 LYS CA C 56.23 . 1 650 . 66 LYS CB C 34.42 . 1 651 . 66 LYS CG C 26.27 . 1 652 . 66 LYS CD C 29.16 . 1 653 . 66 LYS CE C 42.17 . 1 654 . 66 LYS N N 125.77 . 1 655 . 67 PHE H H 6.96 . 1 656 . 67 PHE HA H 5.38 . 1 657 . 67 PHE HB2 H 1.75 . 2 658 . 67 PHE HB3 H 2.37 . 2 659 . 67 PHE HD1 H 6.85 . 3 660 . 67 PHE HE1 H 7.32 . 3 661 . 67 PHE HZ H 6.72 . 1 662 . 67 PHE C C 175.49 . 1 663 . 67 PHE CA C 54.67 . 1 664 . 67 PHE CB C 41.14 . 1 665 . 67 PHE N N 112.32 . 1 666 . 68 ILE H H 9.13 . 1 667 . 68 ILE HA H 4.45 . 1 668 . 68 ILE HB H 1.68 . 1 669 . 68 ILE HG12 H 1.30 . 2 670 . 68 ILE HG13 H 0.89 . 2 671 . 68 ILE HG2 H 0.58 . 1 672 . 68 ILE HD1 H 0.56 . 1 673 . 68 ILE C C 174.88 . 1 674 . 68 ILE CA C 59.39 . 1 675 . 68 ILE CB C 41.84 . 1 676 . 68 ILE CG1 C 27.09 . 1 677 . 68 ILE CG2 C 17.81 . 1 678 . 68 ILE CD1 C 14.12 . 1 679 . 68 ILE N N 118.35 . 1 680 . 69 VAL H H 8.44 . 1 681 . 69 VAL HA H 4.88 . 1 682 . 69 VAL HB H 1.96 . 1 683 . 69 VAL HG1 H 0.87 . 1 684 . 69 VAL HG2 H 1.03 . 1 685 . 69 VAL C C 175.96 . 1 686 . 69 VAL CA C 61.29 . 1 687 . 69 VAL CB C 33.32 . 1 688 . 69 VAL CG1 C 21.53 . 1 689 . 69 VAL CG2 C 21.72 . 1 690 . 69 VAL N N 123.59 . 1 691 . 70 LYS H H 8.85 . 1 692 . 70 LYS HA H 4.53 . 1 693 . 70 LYS HB2 H 1.55 . 2 694 . 70 LYS HB3 H 1.78 . 2 695 . 70 LYS HG2 H 1.33 . 2 696 . 70 LYS HD2 H 1.60 . 2 697 . 70 LYS HE2 H 2.90 . 2 698 . 70 LYS C C 175.10 . 1 699 . 70 LYS CA C 54.67 . 1 700 . 70 LYS CB C 35.13 . 1 701 . 70 LYS CG C 24.69 . 1 702 . 70 LYS CD C 29.64 . 1 703 . 70 LYS CE C 42.12 . 1 704 . 70 LYS N N 128.95 . 1 705 . 71 LYS H H 8.47 . 1 706 . 71 LYS HA H 4.30 . 1 707 . 71 LYS HB2 H 1.66 . 2 708 . 71 LYS HG2 H 1.38 . 2 709 . 71 LYS HE2 H 2.92 . 2 710 . 71 LYS C C 176.27 . 1 711 . 71 LYS CA C 56.04 . 1 712 . 71 LYS CB C 32.80 . 1 713 . 71 LYS CG C 24.50 . 1 714 . 71 LYS CD C 29.13 . 1 715 . 71 LYS CE C 41.92 . 1 716 . 71 LYS N N 125.41 . 1 717 . 72 ASN H H 8.76 . 1 718 . 72 ASN HA H 4.84 . 1 719 . 72 ASN HB2 H 2.85 . 2 720 . 72 ASN HB3 H 2.65 . 2 721 . 72 ASN HD21 H 7.01 . 1 722 . 72 ASN HD22 H 7.67 . 1 723 . 72 ASN C C 174.14 . 1 724 . 72 ASN CA C 51.28 . 1 725 . 72 ASN CB C 39.48 . 1 726 . 72 ASN N N 123.37 . 1 727 . 72 ASN ND2 N 114.00 . 1 728 . 73 PRO HD2 H 3.83 . 2 729 . 73 PRO HD3 H 3.98 . 2 730 . 73 PRO CD C 50.95 . 1 731 . 74 HIS HD2 H 6.93 . 1 732 . 74 HIS CB C 31.08 . 1 733 . 75 HIS HA H 3.98 . 1 734 . 75 HIS HB2 H 2.27 . 2 735 . 75 HIS HD2 H 7.25 . 1 736 . 75 HIS C C 178.09 . 1 737 . 75 HIS CA C 58.27 . 1 738 . 75 HIS CB C 29.64 . 1 739 . 77 GLN HA H 4.25 . 1 740 . 77 GLN HB2 H 1.89 . 2 741 . 77 GLN HB3 H 1.81 . 2 742 . 77 GLN HG2 H 2.04 . 2 743 . 77 GLN C C 176.00 . 1 744 . 77 GLN CA C 56.57 . 1 745 . 77 GLN CB C 28.70 . 1 746 . 77 GLN CG C 33.45 . 1 747 . 78 TRP H H 7.92 . 1 748 . 78 TRP HA H 4.75 . 1 749 . 78 TRP HB2 H 3.38 . 2 750 . 78 TRP HB3 H 3.20 . 2 751 . 78 TRP HD1 H 7.16 . 1 752 . 78 TRP HE1 H 10.04 . 1 753 . 78 TRP HE3 H 7.55 . 1 754 . 78 TRP HZ2 H 7.37 . 1 755 . 78 TRP C C 176.78 . 1 756 . 78 TRP CA C 57.01 . 1 757 . 78 TRP CB C 29.74 . 1 758 . 78 TRP N N 120.62 . 1 759 . 78 TRP NE1 N 129.62 . 1 760 . 79 GLY H H 8.14 . 1 761 . 79 GLY HA2 H 3.94 . 2 762 . 79 GLY HA3 H 3.89 . 2 763 . 79 GLY C C 173.58 . 1 764 . 79 GLY CA C 45.33 . 1 765 . 79 GLY N N 109.22 . 1 766 . 80 ASP H H 8.17 . 1 767 . 80 ASP HA H 4.68 . 1 768 . 80 ASP HB2 H 2.50 . 2 769 . 80 ASP C C 176.01 . 1 770 . 80 ASP CA C 54.61 . 1 771 . 80 ASP CB C 41.46 . 1 772 . 80 ASP N N 121.21 . 1 773 . 81 MET H H 8.50 . 1 774 . 81 MET HA H 4.74 . 1 775 . 81 MET HB2 H 2.02 . 2 776 . 81 MET HG2 H 2.53 . 2 777 . 81 MET HE H 2.06 . 1 778 . 81 MET C C 174.35 . 1 779 . 81 MET CA C 54.65 . 1 780 . 81 MET CB C 34.78 . 1 781 . 81 MET CG C 31.72 . 1 782 . 81 MET CE C 16.97 . 1 783 . 81 MET N N 121.18 . 1 784 . 82 LYS H H 8.15 . 1 785 . 82 LYS HA H 4.74 . 1 786 . 82 LYS HB2 H 2.04 . 2 787 . 82 LYS HE2 H 2.33 . 2 788 . 82 LYS C C 174.97 . 1 789 . 82 LYS CA C 56.22 . 1 790 . 82 LYS CB C 34.80 . 1 791 . 82 LYS CG C 26.30 . 1 792 . 82 LYS CE C 41.82 . 1 793 . 82 LYS N N 124.18 . 1 794 . 83 LEU H H 9.21 . 1 795 . 83 LEU HA H 5.07 . 1 796 . 83 LEU HB2 H 1.38 . 2 797 . 83 LEU HG H 1.56 . 1 798 . 83 LEU HD1 H 0.83 . 1 799 . 83 LEU HD2 H 0.76 . 1 800 . 83 LEU C C 174.95 . 1 801 . 83 LEU CA C 53.78 . 1 802 . 83 LEU CB C 44.33 . 1 803 . 83 LEU CG C 26.31 . 1 804 . 83 LEU CD1 C 26.30 . 1 805 . 83 LEU CD2 C 24.79 . 1 806 . 83 LEU N N 123.27 . 1 807 . 84 TYR H H 9.24 . 1 808 . 84 TYR HA H 4.82 . 1 809 . 84 TYR HB2 H 3.09 . 2 810 . 84 TYR HB3 H 2.27 . 2 811 . 84 TYR HD1 H 7.18 . 3 812 . 84 TYR HE1 H 6.45 . 3 813 . 84 TYR C C 174.99 . 1 814 . 84 TYR CA C 56.54 . 1 815 . 84 TYR CB C 42.79 . 1 816 . 84 TYR CE1 C 116.54 . 1 817 . 84 TYR N N 120.34 . 1 818 . 85 LEU H H 9.32 . 1 819 . 85 LEU HA H 4.15 . 1 820 . 85 LEU HB2 H 1.41 . 2 821 . 85 LEU HB3 H 1.15 . 2 822 . 85 LEU HG H 1.04 . 1 823 . 85 LEU HD1 H 0.58 . 1 824 . 85 LEU HD2 H 0.67 . 1 825 . 85 LEU C C 178.26 . 1 826 . 85 LEU CA C 54.47 . 1 827 . 85 LEU CB C 41.57 . 1 828 . 85 LEU CG C 26.33 . 1 829 . 85 LEU CD1 C 26.08 . 1 830 . 85 LEU CD2 C 26.66 . 1 831 . 85 LEU N N 123.65 . 1 832 . 86 LYS H H 8.76 . 1 833 . 86 LYS HA H 3.55 . 1 834 . 86 LYS HG2 H 1.51 . 2 835 . 86 LYS C C 177.59 . 1 836 . 86 LYS CA C 61.59 . 1 837 . 86 LYS CB C 32.35 . 1 838 . 86 LYS CG C 21.83 . 1 839 . 86 LYS CD C 25.58 . 1 840 . 86 LYS CE C 42.35 . 1 841 . 86 LYS N N 132.27 . 1 842 . 87 LEU H H 9.22 . 1 843 . 87 LEU HA H 4.04 . 1 844 . 87 LEU HB2 H 1.65 . 2 845 . 87 LEU HB3 H 1.56 . 2 846 . 87 LEU HG H 1.81 . 1 847 . 87 LEU HD1 H 0.88 . 1 848 . 87 LEU HD2 H 0.97 . 1 849 . 87 LEU C C 179.71 . 1 850 . 87 LEU CA C 58.77 . 1 851 . 87 LEU CB C 42.11 . 1 852 . 87 LEU CG C 25.88 . 1 853 . 87 LEU CD1 C 25.77 . 1 854 . 87 LEU CD2 C 26.19 . 1 855 . 87 LEU N N 117.85 . 1 856 . 88 GLN H H 7.12 . 1 857 . 88 GLN HA H 4.09 . 1 858 . 88 GLN HB2 H 2.33 . 2 859 . 88 GLN HG2 H 2.55 . 2 860 . 88 GLN HE21 H 6.76 . 1 861 . 88 GLN HE22 H 7.49 . 1 862 . 88 GLN C C 178.47 . 1 863 . 88 GLN CA C 58.24 . 1 864 . 88 GLN CB C 27.35 . 1 865 . 88 GLN CG C 35.27 . 1 866 . 88 GLN N N 117.13 . 1 867 . 88 GLN NE2 N 112.35 . 1 868 . 89 ILE H H 7.66 . 1 869 . 89 ILE HA H 3.45 . 1 870 . 89 ILE HB H 2.16 . 1 871 . 89 ILE HG12 H 1.56 . 2 872 . 89 ILE HG13 H 0.88 . 2 873 . 89 ILE HG2 H 0.23 . 1 874 . 89 ILE HD1 H 0.13 . 1 875 . 89 ILE C C 177.27 . 1 876 . 89 ILE CA C 60.90 . 1 877 . 89 ILE CB C 34.27 . 1 878 . 89 ILE CG1 C 25.84 . 1 879 . 89 ILE CG2 C 17.63 . 1 880 . 89 ILE CD1 C 8.89 . 1 881 . 89 ILE N N 124.38 . 1 882 . 90 VAL H H 8.54 . 1 883 . 90 VAL HA H 3.08 . 1 884 . 90 VAL HB H 1.90 . 1 885 . 90 VAL HG1 H 0.89 . 1 886 . 90 VAL HG2 H 0.81 . 1 887 . 90 VAL C C 179.08 . 1 888 . 90 VAL CA C 66.60 . 1 889 . 90 VAL CB C 31.57 . 1 890 . 90 VAL CG1 C 20.77 . 1 891 . 90 VAL CG2 C 22.75 . 1 892 . 90 VAL N N 121.32 . 1 893 . 91 LYS H H 7.16 . 1 894 . 91 LYS HA H 3.97 . 1 895 . 91 LYS HB2 H 1.87 . 2 896 . 91 LYS HB3 H 1.78 . 2 897 . 91 LYS HG2 H 1.33 . 2 898 . 91 LYS HG3 H 1.46 . 2 899 . 91 LYS HD2 H 1.68 . 2 900 . 91 LYS HD3 H 1.55 . 2 901 . 91 LYS HE2 H 2.96 . 2 902 . 91 LYS C C 178.67 . 1 903 . 91 LYS CA C 59.90 . 1 904 . 91 LYS CB C 32.68 . 1 905 . 91 LYS CG C 24.97 . 1 906 . 91 LYS CD C 30.48 . 1 907 . 91 LYS CE C 42.18 . 1 908 . 91 LYS N N 119.28 . 1 909 . 92 ARG H H 7.98 . 1 910 . 92 ARG HA H 4.34 . 1 911 . 92 ARG HB2 H 1.95 . 2 912 . 92 ARG HG2 H 1.23 . 2 913 . 92 ARG HD2 H 3.43 . 2 914 . 92 ARG C C 177.90 . 1 915 . 92 ARG CA C 56.44 . 1 916 . 92 ARG CB C 27.58 . 1 917 . 92 ARG CG C 25.37 . 1 918 . 92 ARG CD C 40.34 . 1 919 . 92 ARG N N 120.02 . 1 920 . 93 SER H H 8.91 . 1 921 . 93 SER HA H 4.29 . 1 922 . 93 SER C C 176.16 . 1 923 . 93 SER CA C 62.74 . 1 924 . 93 SER N N 116.65 . 1 925 . 94 LEU H H 7.81 . 1 926 . 94 LEU HA H 4.13 . 1 927 . 94 LEU HB2 H 1.96 . 2 928 . 94 LEU HB3 H 1.49 . 2 929 . 94 LEU HG H 1.86 . 1 930 . 94 LEU HD1 H 0.91 . 1 931 . 94 LEU HD2 H 0.80 . 1 932 . 94 LEU C C 180.66 . 1 933 . 94 LEU CA C 57.75 . 1 934 . 94 LEU CB C 41.27 . 1 935 . 94 LEU CG C 27.13 . 1 936 . 94 LEU CD1 C 25.07 . 1 937 . 94 LEU CD2 C 22.14 . 1 938 . 94 LEU N N 122.68 . 1 939 . 95 GLU H H 7.87 . 1 940 . 95 GLU HA H 3.99 . 1 941 . 95 GLU HB2 H 2.21 . 2 942 . 95 GLU HG2 H 2.60 . 2 943 . 95 GLU C C 178.74 . 1 944 . 95 GLU CA C 59.09 . 1 945 . 95 GLU CB C 29.57 . 1 946 . 95 GLU CG C 36.47 . 1 947 . 95 GLU N N 121.69 . 1 948 . 96 VAL H H 7.89 . 1 949 . 96 VAL HA H 3.38 . 1 950 . 96 VAL HB H 1.87 . 1 951 . 96 VAL HG1 H 0.10 . 1 952 . 96 VAL HG2 H 0.76 . 1 953 . 96 VAL C C 177.95 . 1 954 . 96 VAL CA C 65.83 . 1 955 . 96 VAL CB C 32.38 . 1 956 . 96 VAL CG1 C 19.90 . 1 957 . 96 VAL CG2 C 21.96 . 1 958 . 96 VAL N N 119.06 . 1 959 . 97 TRP H H 8.58 . 1 960 . 97 TRP HA H 4.39 . 1 961 . 97 TRP HB2 H 3.45 . 2 962 . 97 TRP HB3 H 3.09 . 2 963 . 97 TRP HD1 H 7.65 . 1 964 . 97 TRP HE1 H 9.78 . 1 965 . 97 TRP HE3 H 7.34 . 1 966 . 97 TRP HZ2 H 7.66 . 1 967 . 97 TRP HZ3 H 7.09 . 1 968 . 97 TRP HH2 H 7.13 . 1 969 . 97 TRP C C 177.66 . 1 970 . 97 TRP CA C 58.84 . 1 971 . 97 TRP CB C 30.19 . 1 972 . 97 TRP N N 118.07 . 1 973 . 97 TRP NE1 N 128.53 . 1 974 . 98 GLY H H 8.07 . 1 975 . 98 GLY HA2 H 4.52 . 2 976 . 98 GLY HA3 H 3.70 . 2 977 . 98 GLY C C 174.09 . 1 978 . 98 GLY CA C 46.56 . 1 979 . 98 GLY N N 112.13 . 1 980 . 99 SER H H 7.50 . 1 981 . 99 SER HA H 4.59 . 1 982 . 99 SER HB2 H 4.22 . 2 983 . 99 SER HB3 H 4.25 . 2 984 . 99 SER C C 173.61 . 1 985 . 99 SER CA C 57.17 . 1 986 . 99 SER CB C 65.47 . 1 987 . 99 SER N N 110.64 . 1 988 . 100 GLN H H 9.20 . 1 989 . 100 GLN HA H 3.94 . 1 990 . 100 GLN HB2 H 2.16 . 2 991 . 100 GLN HB3 H 1.93 . 2 992 . 100 GLN HG2 H 2.35 . 2 993 . 100 GLN HE21 H 6.69 . 1 994 . 100 GLN HE22 H 7.74 . 1 995 . 100 GLN C C 177.89 . 1 996 . 100 GLN CA C 58.37 . 1 997 . 100 GLN CB C 27.96 . 1 998 . 100 GLN CG C 33.14 . 1 999 . 100 GLN N N 123.24 . 1 1000 . 100 GLN NE2 N 112.50 . 1 1001 . 101 GLU H H 8.98 . 1 1002 . 101 GLU HA H 3.90 . 1 1003 . 101 GLU HB2 H 1.90 . 2 1004 . 101 GLU HB3 H 2.10 . 2 1005 . 101 GLU HG2 H 2.23 . 2 1006 . 101 GLU HG3 H 2.44 . 2 1007 . 101 GLU C C 178.79 . 1 1008 . 101 GLU CA C 60.53 . 1 1009 . 101 GLU CB C 28.69 . 1 1010 . 101 GLU CG C 37.22 . 1 1011 . 101 GLU N N 119.56 . 1 1012 . 102 ALA H H 8.03 . 1 1013 . 102 ALA HA H 4.18 . 1 1014 . 102 ALA HB H 1.72 . 1 1015 . 102 ALA C C 180.61 . 1 1016 . 102 ALA CA C 54.84 . 1 1017 . 102 ALA CB C 18.95 . 1 1018 . 102 ALA N N 123.42 . 1 1019 . 103 LEU H H 7.28 . 1 1020 . 103 LEU HA H 3.12 . 1 1021 . 103 LEU HB2 H 1.88 . 2 1022 . 103 LEU HB3 H 1.18 . 2 1023 . 103 LEU HG H 1.04 . 1 1024 . 103 LEU HD1 H 0.29 . 1 1025 . 103 LEU HD2 H 0.87 . 1 1026 . 103 LEU C C 177.61 . 1 1027 . 103 LEU CA C 57.83 . 1 1028 . 103 LEU CB C 41.05 . 1 1029 . 103 LEU CG C 25.46 . 1 1030 . 103 LEU CD1 C 22.93 . 1 1031 . 103 LEU CD2 C 25.71 . 1 1032 . 103 LEU N N 122.36 . 1 1033 . 104 GLU H H 8.24 . 1 1034 . 104 GLU HA H 3.67 . 1 1035 . 104 GLU HB2 H 1.93 . 2 1036 . 104 GLU HG2 H 2.25 . 2 1037 . 104 GLU HG3 H 2.36 . 2 1038 . 104 GLU C C 179.82 . 1 1039 . 104 GLU CA C 59.40 . 1 1040 . 104 GLU CB C 28.69 . 1 1041 . 104 GLU CG C 36.29 . 1 1042 . 104 GLU N N 118.23 . 1 1043 . 105 GLU H H 8.03 . 1 1044 . 105 GLU HA H 3.96 . 1 1045 . 105 GLU HB2 H 2.00 . 2 1046 . 105 GLU HG2 H 2.14 . 2 1047 . 105 GLU HG3 H 2.32 . 2 1048 . 105 GLU C C 178.31 . 1 1049 . 105 GLU CA C 59.21 . 1 1050 . 105 GLU CB C 29.36 . 1 1051 . 105 GLU CG C 36.32 . 1 1052 . 105 GLU N N 120.53 . 1 1053 . 106 ALA H H 7.47 . 1 1054 . 106 ALA HA H 3.97 . 1 1055 . 106 ALA HB H 0.86 . 1 1056 . 106 ALA C C 180.47 . 1 1057 . 106 ALA CA C 54.51 . 1 1058 . 106 ALA CB C 18.40 . 1 1059 . 106 ALA N N 122.83 . 1 1060 . 107 LYS H H 7.92 . 1 1061 . 107 LYS HA H 3.72 . 1 1062 . 107 LYS HB2 H 1.71 . 2 1063 . 107 LYS HE2 H 3.13 . 2 1064 . 107 LYS C C 178.62 . 1 1065 . 107 LYS CA C 59.50 . 1 1066 . 107 LYS CB C 32.52 . 1 1067 . 107 LYS CG C 25.76 . 1 1068 . 107 LYS CD C 30.48 . 1 1069 . 107 LYS CE C 41.72 . 1 1070 . 107 LYS N N 118.89 . 1 1071 . 108 GLU H H 7.68 . 1 1072 . 108 GLU HA H 4.04 . 1 1073 . 108 GLU HB2 H 2.07 . 2 1074 . 108 GLU HG2 H 2.18 . 2 1075 . 108 GLU HG3 H 2.31 . 2 1076 . 108 GLU C C 178.43 . 1 1077 . 108 GLU CA C 58.56 . 1 1078 . 108 GLU CB C 29.59 . 1 1079 . 108 GLU CG C 36.17 . 1 1080 . 108 GLU N N 120.50 . 1 1081 . 109 VAL H H 7.81 . 1 1082 . 109 VAL HA H 3.90 . 1 1083 . 109 VAL HB H 2.14 . 1 1084 . 109 VAL HG1 H 0.94 . 1 1085 . 109 VAL HG2 H 1.03 . 1 1086 . 109 VAL C C 177.60 . 1 1087 . 109 VAL CA C 64.31 . 1 1088 . 109 VAL CB C 32.89 . 1 1089 . 109 VAL CG1 C 21.16 . 1 1090 . 109 VAL CG2 C 21.72 . 1 1091 . 109 VAL N N 119.34 . 1 1092 . 110 ARG H H 7.78 . 1 1093 . 110 ARG HA H 4.17 . 1 1094 . 110 ARG HB2 H 1.73 . 2 1095 . 110 ARG HB3 H 1.82 . 2 1096 . 110 ARG HG2 H 2.01 . 2 1097 . 110 ARG HG3 H 2.07 . 2 1098 . 110 ARG HD2 H 3.13 . 2 1099 . 110 ARG C C 177.57 . 1 1100 . 110 ARG CA C 57.42 . 1 1101 . 110 ARG CB C 30.34 . 1 1102 . 110 ARG CG C 27.11 . 1 1103 . 110 ARG CD C 43.48 . 1 1104 . 110 ARG N N 121.34 . 1 1105 . 111 GLN H H 8.03 . 1 1106 . 111 GLN HA H 4.12 . 1 1107 . 111 GLN HB2 H 2.06 . 2 1108 . 111 GLN HG2 H 2.38 . 2 1109 . 111 GLN HE21 H 6.80 . 1 1110 . 111 GLN HE22 H 7.52 . 1 1111 . 111 GLN C C 176.91 . 1 1112 . 111 GLN CA C 57.25 . 1 1113 . 111 GLN CB C 28.77 . 1 1114 . 111 GLN CG C 33.58 . 1 1115 . 111 GLN N N 120.61 . 1 1116 . 111 GLN NE2 N 112.83 . 1 1117 . 112 GLU H H 8.36 . 1 1118 . 112 GLU HA H 4.14 . 1 1119 . 112 GLU HB2 H 1.99 . 2 1120 . 112 GLU HG2 H 2.23 . 2 1121 . 112 GLU C C 177.30 . 1 1122 . 112 GLU CA C 57.74 . 1 1123 . 112 GLU CB C 29.82 . 1 1124 . 112 GLU CG C 36.18 . 1 1125 . 112 GLU N N 121.45 . 1 1126 . 113 ASN H H 8.29 . 1 1127 . 113 ASN HA H 4.61 . 1 1128 . 113 ASN HB2 H 2.82 . 2 1129 . 113 ASN HD21 H 6.92 . 1 1130 . 113 ASN HD22 H 7.58 . 1 1131 . 113 ASN CA C 53.97 . 1 1132 . 113 ASN CB C 38.47 . 1 1133 . 113 ASN N N 119.17 . 1 1134 . 113 ASN ND2 N 113.37 . 1 1135 . 114 ARG H H 8.14 . 1 1136 . 114 ARG HA H 4.17 . 1 1137 . 114 ARG HB2 H 1.87 . 2 1138 . 114 ARG HB3 H 1.83 . 2 1139 . 114 ARG HG2 H 1.61 . 2 1140 . 114 ARG HG3 H 1.69 . 2 1141 . 114 ARG HD2 H 3.17 . 2 1142 . 114 ARG CA C 57.86 . 1 1143 . 114 ARG CB C 30.40 . 1 1144 . 114 ARG CG C 26.23 . 1 1145 . 114 ARG CD C 43.36 . 1 1146 . 114 ARG N N 121.73 . 1 1147 . 115 GLU H H 8.25 . 1 1148 . 115 GLU HA H 4.15 . 1 1149 . 115 GLU HB2 H 1.99 . 2 1150 . 115 GLU HB3 H 2.26 . 2 1151 . 115 GLU HG2 H 2.26 . 2 1152 . 115 GLU C C 177.61 . 1 1153 . 115 GLU CA C 57.68 . 1 1154 . 115 GLU CB C 29.87 . 1 1155 . 115 GLU N N 120.70 . 1 1156 . 116 LYS H H 8.02 . 1 1157 . 116 LYS HA H 4.15 . 1 1158 . 116 LYS HB2 H 1.80 . 2 1159 . 116 LYS HB3 H 1.44 . 2 1160 . 116 LYS HG2 H 2.94 . 2 1161 . 116 LYS HG3 H 2.71 . 2 1162 . 116 LYS C C 177.44 . 1 1163 . 116 LYS CA C 57.36 . 1 1164 . 116 LYS CB C 32.64 . 1 1165 . 116 LYS N N 120.91 . 1 1166 . 117 MET H H 7.98 . 1 1167 . 117 MET HA H 4.37 . 1 1168 . 117 MET HB2 H 2.08 . 2 1169 . 117 MET HG2 H 2.55 . 2 1170 . 117 MET HE H 2.06 . 1 1171 . 117 MET C C 176.62 . 1 1172 . 117 MET CA C 55.95 . 1 1173 . 117 MET CB C 32.56 . 1 1174 . 117 MET CG C 29.60 . 1 1175 . 117 MET CE C 16.97 . 1 1176 . 117 MET N N 119.80 . 1 1177 . 118 LYS H H 7.97 . 1 1178 . 118 LYS HA H 4.22 . 1 1179 . 118 LYS HB2 H 1.78 . 2 1180 . 118 LYS HB3 H 1.62 . 2 1181 . 118 LYS HG2 H 1.39 . 2 1182 . 118 LYS HD2 H 2.91 . 2 1183 . 118 LYS C C 176.62 . 1 1184 . 118 LYS CA C 56.69 . 1 1185 . 118 LYS CB C 32.82 . 1 1186 . 118 LYS N N 121.94 . 1 1187 . 119 GLN H H 8.10 . 1 1188 . 119 GLN HA H 4.25 . 1 1189 . 119 GLN HB2 H 2.06 . 2 1190 . 119 GLN HB3 H 1.96 . 2 1191 . 119 GLN HG2 H 2.34 . 2 1192 . 119 GLN HE21 H 6.74 . 1 1193 . 119 GLN HE22 H 7.25 . 1 1194 . 119 GLN C C 175.74 . 1 1195 . 119 GLN CA C 55.75 . 1 1196 . 119 GLN CB C 29.34 . 1 1197 . 119 GLN CG C 33.71 . 1 1198 . 119 GLN N N 121.09 . 1 1199 . 119 GLN NE2 N 112.68 . 1 1200 . 120 LYS H H 8.16 . 1 1201 . 120 LYS HA H 4.20 . 1 1202 . 120 LYS HB2 H 2.35 . 2 1203 . 120 LYS HG2 H 1.32 . 2 1204 . 120 LYS HD2 H 1.59 . 2 1205 . 120 LYS HE2 H 2.91 . 2 1206 . 120 LYS C C 175.98 . 1 1207 . 120 LYS CA C 56.25 . 1 1208 . 120 LYS CB C 33.07 . 1 1209 . 120 LYS CG C 24.24 . 1 1210 . 120 LYS CE C 41.88 . 1 1211 . 120 LYS N N 123.42 . 1 1212 . 121 LYS H H 8.17 . 1 1213 . 121 LYS HA H 4.23 . 1 1214 . 121 LYS HB2 H 1.60 . 2 1215 . 121 LYS HB3 H 1.65 . 2 1216 . 121 LYS HG2 H 1.30 . 2 1217 . 121 LYS HG3 H 1.32 . 2 1218 . 121 LYS HD2 H 1.60 . 2 1219 . 121 LYS HE2 H 2.92 . 2 1220 . 121 LYS C C 175.13 . 1 1221 . 121 LYS CA C 56.14 . 1 1222 . 121 LYS CB C 33.18 . 1 1223 . 121 LYS CG C 24.46 . 1 1224 . 121 LYS CD C 29.33 . 1 1225 . 121 LYS CE C 42.02 . 1 1226 . 121 LYS N N 123.74 . 1 1227 . 122 PHE H H 7.69 . 1 1228 . 122 PHE HA H 4.39 . 1 1229 . 122 PHE HB2 H 3.13 . 2 1230 . 122 PHE HB3 H 2.92 . 2 1231 . 122 PHE HD1 H 7.31 . 3 1232 . 122 PHE HE1 H 7.49 . 3 1233 . 122 PHE C C 180.22 . 1 1234 . 122 PHE CA C 58.98 . 1 1235 . 122 PHE CB C 40.29 . 1 1236 . 122 PHE N N 126.55 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H . _Mol_system_component_name XPA _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 PHE H 3 PHE HA 10.2 . . . 2 3JHNHA 4 ASP H 4 ASP HA 9.8 . . . 3 3JHNHA 5 TYR H 5 TYR HA 6.3 . . . 4 3JHNHA 6 VAL H 6 VAL HA 8.5 . . . 5 3JHNHA 7 ILE H 7 ILE HA 6.7 . . . 6 3JHNHA 8 CYS H 8 CYS HA 4.1 . . . 7 3JHNHA 9 GLU H 9 GLU HA 5.1 . . . 8 3JHNHA 10 GLU H 10 GLU HA 9.3 . . . 9 3JHNHA 11 CYS H 11 CYS HA 8.3 . . . 10 3JHNHA 13 LYS H 13 LYS HA 6.9 . . . 11 3JHNHA 14 GLU H 14 GLU HA 5.6 . . . 12 3JHNHA 15 PHE H 15 PHE HA 6.6 . . . 13 3JHNHA 16 MET H 16 MET HA 9.0 . . . 14 3JHNHA 18 SER H 18 SER HA 5.1 . . . 15 3JHNHA 19 TYR H 19 TYR HA 2.1 . . . 16 3JHNHA 20 LEU H 20 LEU HA 0.0 . . . 17 3JHNHA 21 MET H 21 MET HA 5.2 . . . 18 3JHNHA 22 ASN H 22 ASN HA 1.9 . . . 19 3JHNHA 23 HIS H 23 HIS HA 6.1 . . . 20 3JHNHA 24 PHE H 24 PHE HA 9.4 . . . 21 3JHNHA 25 ASP H 25 ASP HA 6.3 . . . 22 3JHNHA 26 LEU H 26 LEU HA 8.9 . . . 23 3JHNHA 28 THR H 28 THR HA 7.6 . . . 24 3JHNHA 29 CYS H 29 CYS HA 5.0 . . . 25 3JHNHA 30 ASP H 30 ASP HA 2.3 . . . 26 3JHNHA 32 CYS H 32 CYS HA 7.2 . . . 27 3JHNHA 33 ARG H 33 ARG HA 1.5 . . . 28 3JHNHA 35 ALA H 35 ALA HA 4.0 . . . 29 3JHNHA 36 ASP H 36 ASP HA 6.3 . . . 30 3JHNHA 37 ASP H 37 ASP HA 10.1 . . . 31 3JHNHA 38 LYS H 38 LYS HA 0.0 . . . 32 3JHNHA 39 HIS H 39 HIS HA 7.3 . . . 33 3JHNHA 40 LYS H 40 LYS HA 1.7 . . . 34 3JHNHA 41 LEU H 41 LEU HA 6.8 . . . 35 3JHNHA 42 ILE H 42 ILE HA 8.4 . . . 36 3JHNHA 43 THR H 43 THR HA 5.2 . . . 37 3JHNHA 44 LYS H 44 LYS HA 0.0 . . . 38 3JHNHA 45 THR H 45 THR HA 4.8 . . . 39 3JHNHA 46 GLU H 46 GLU HA 2.7 . . . 40 3JHNHA 47 ALA H 47 ALA HA 1.9 . . . 41 3JHNHA 48 LYS H 48 LYS HA 2.0 . . . 42 3JHNHA 50 GLU H 50 GLU HA 3.4 . . . 43 3JHNHA 51 TYR H 51 TYR HA 7.3 . . . 44 3JHNHA 52 LEU H 52 LEU HA 4.6 . . . 45 3JHNHA 53 LEU H 53 LEU HA 6.9 . . . 46 3JHNHA 54 LYS H 54 LYS HA 8.6 . . . 47 3JHNHA 57 ASP H 57 ASP HA 5.7 . . . 48 3JHNHA 58 LEU H 58 LEU HA 7.9 . . . 49 3JHNHA 59 GLU H 59 GLU HA 8.4 . . . 50 3JHNHA 61 ARG H 61 ARG HA 3.2 . . . 51 3JHNHA 62 GLU H 62 GLU HA 3.0 . . . 52 3JHNHA 65 LEU H 65 LEU HA 6.3 . . . 53 3JHNHA 66 LYS H 66 LYS HA 6.8 . . . 54 3JHNHA 67 PHE H 67 PHE HA 7.2 . . . 55 3JHNHA 68 ILE H 68 ILE HA 8.7 . . . 56 3JHNHA 69 VAL H 69 VAL HA 8.0 . . . 57 3JHNHA 70 LYS H 70 LYS HA 6.7 . . . 58 3JHNHA 71 LYS H 71 LYS HA 5.3 . . . 59 3JHNHA 72 ASN H 72 ASN HA 6.3 . . . 60 3JHNHA 78 TRP H 78 TRP HA 7.0 . . . 61 3JHNHA 80 ASP H 80 ASP HA 3.0 . . . 62 3JHNHA 82 LYS H 82 LYS HA 7.4 . . . 63 3JHNHA 84 TYR H 84 TYR HA 8.3 . . . 64 3JHNHA 85 LEU H 85 LEU HA 5.4 . . . 65 3JHNHA 87 LEU H 87 LEU HA 2.6 . . . 66 3JHNHA 88 GLN H 88 GLN HA 8.0 . . . 67 3JHNHA 89 ILE H 89 ILE HA 3.4 . . . 68 3JHNHA 90 VAL H 90 VAL HA 1.8 . . . 69 3JHNHA 91 LYS H 91 LYS HA 1.8 . . . 70 3JHNHA 93 SER H 93 SER HA 1.9 . . . 71 3JHNHA 94 LEU H 94 LEU HA 2.4 . . . 72 3JHNHA 95 GLU H 95 GLU HA 4.0 . . . 73 3JHNHA 96 VAL H 96 VAL HA 5.8 . . . 74 3JHNHA 97 TRP H 97 TRP HA 5.4 . . . 75 3JHNHA 99 SER H 99 SER HA 3.2 . . . 76 3JHNHA 100 GLN H 100 GLN HA 0.0 . . . 77 3JHNHA 101 GLU H 101 GLU HA 1.9 . . . 78 3JHNHA 102 ALA H 102 ALA HA 2.6 . . . 79 3JHNHA 103 LEU H 103 LEU HA 2.4 . . . 80 3JHNHA 104 GLU H 104 GLU HA 2.1 . . . 81 3JHNHA 106 ALA H 106 ALA HA 2.4 . . . 82 3JHNHA 107 LYS H 107 LYS HA 2.5 . . . 83 3JHNHA 108 GLU H 108 GLU HA 2.8 . . . 84 3JHNHA 109 VAL H 109 VAL HA 3.0 . . . 85 3JHNHA 110 ARG H 110 ARG HA 2.9 . . . 86 3JHNHA 113 ASN H 113 ASN HA 7.7 . . . 87 3JHNHA 114 ARG H 114 ARG HA 3.0 . . . 88 3JHNHA 115 GLU H 115 GLU HA 2.8 . . . 89 3JHNHA 122 PHE H 122 PHE HA 8.6 . . . stop_ save_