data_4675 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments of the DNA binding domain of the human forkhead transcription factor AFX ; _BMRB_accession_number 4675 _BMRB_flat_file_name bmr4675.str _Entry_type original _Submission_date 2000-03-01 _Accession_date 2000-03-01 _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 Weigelt Johan . . 2 Climent Isabel . . 3 Dahlman-Wright Karin . . 4 Wikstrom Mats . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 529 "13C chemical shifts" 494 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-07-08 original author . stop_ _Original_release_date 2000-07-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignments of the DNA binding domain of the human forkhead transcription factor AFX ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weigelt Johan . . 2 Climent Isabel . . 3 Dahlman-Wright Karin . . 4 Wikstrom Mats . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 181 _Page_last 182 _Year 2000 _Details . loop_ _Keyword AFX 'DNA binding' 'forkhead domain' 'winged helix' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR, 6, 135-40 (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_AFXdbd _Saveframe_category molecular_system _Mol_system_name 'DNA binding domain of AFX transcription factor' _Abbreviation_common AFX-DBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AFX-DBD $AFX stop_ _System_molecular_weight 16708 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; DNA binding domain (residues 82-207) of the human transcription factor AFX. The construct contain 24 additional (non-native) residues included for purification purposes (his-tag, residues 58-81). ; save_ ######################## # Monomeric polymers # ######################## save_AFX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AFX _Abbreviation_common AFX _Molecular_mass 16708 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 150 _Mol_residue_sequence ; GSSHHHHHHSSGLVPRGSHM LEDPGAVTGPRKGGSRRNAW GNQSYAELISQAIESAPEKR LTLAQIYEWMVRTVPYFKDK GDSNSSAGWKNSIRHNLSLH SKFIKVHNEATGKSSWWMLN PEGGKSGKAPRRRAASMDSS SKLLRGRSKA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 58 GLY 2 59 SER 3 60 SER 4 61 HIS 5 62 HIS 6 63 HIS 7 64 HIS 8 65 HIS 9 66 HIS 10 67 SER 11 68 SER 12 69 GLY 13 70 LEU 14 71 VAL 15 72 PRO 16 73 ARG 17 74 GLY 18 75 SER 19 76 HIS 20 77 MET 21 78 LEU 22 79 GLU 23 80 ASP 24 81 PRO 25 82 GLY 26 83 ALA 27 84 VAL 28 85 THR 29 86 GLY 30 87 PRO 31 88 ARG 32 89 LYS 33 90 GLY 34 91 GLY 35 92 SER 36 93 ARG 37 94 ARG 38 95 ASN 39 96 ALA 40 97 TRP 41 98 GLY 42 99 ASN 43 100 GLN 44 101 SER 45 102 TYR 46 103 ALA 47 104 GLU 48 105 LEU 49 106 ILE 50 107 SER 51 108 GLN 52 109 ALA 53 110 ILE 54 111 GLU 55 112 SER 56 113 ALA 57 114 PRO 58 115 GLU 59 116 LYS 60 117 ARG 61 118 LEU 62 119 THR 63 120 LEU 64 121 ALA 65 122 GLN 66 123 ILE 67 124 TYR 68 125 GLU 69 126 TRP 70 127 MET 71 128 VAL 72 129 ARG 73 130 THR 74 131 VAL 75 132 PRO 76 133 TYR 77 134 PHE 78 135 LYS 79 136 ASP 80 137 LYS 81 138 GLY 82 139 ASP 83 140 SER 84 141 ASN 85 142 SER 86 143 SER 87 144 ALA 88 145 GLY 89 146 TRP 90 147 LYS 91 148 ASN 92 149 SER 93 150 ILE 94 151 ARG 95 152 HIS 96 153 ASN 97 154 LEU 98 155 SER 99 156 LEU 100 157 HIS 101 158 SER 102 159 LYS 103 160 PHE 104 161 ILE 105 162 LYS 106 163 VAL 107 164 HIS 108 165 ASN 109 166 GLU 110 167 ALA 111 168 THR 112 169 GLY 113 170 LYS 114 171 SER 115 172 SER 116 173 TRP 117 174 TRP 118 175 MET 119 176 LEU 120 177 ASN 121 178 PRO 122 179 GLU 123 180 GLY 124 181 GLY 125 182 LYS 126 183 SER 127 184 GLY 128 185 LYS 129 186 ALA 130 187 PRO 131 188 ARG 132 189 ARG 133 190 ARG 134 191 ALA 135 192 ALA 136 193 SER 137 194 MET 138 195 ASP 139 196 SER 140 197 SER 141 198 SER 142 199 LYS 143 200 LEU 144 201 LEU 145 202 ARG 146 203 GLY 147 204 ARG 148 205 SER 149 206 LYS 150 207 ALA 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 1E17 "Solution Structure Of The Dna Binding Domain Of The Human Forkhead Transcription Factor Afx (Foxo4)" 100.00 150 100.00 100.00 5.60e-103 PDB 3L2C "Crystal Structure Of The Dna Binding Domain Of Foxo4 Bound To Dna" 73.33 110 100.00 100.00 6.40e-74 DBJ BAA86199 "forkhead protein [Mus musculus]" 83.33 505 98.40 99.20 5.08e-80 DBJ BAG61928 "unnamed protein product [Homo sapiens]" 84.00 398 100.00 100.00 3.82e-82 DBJ BAG73163 "forkhead box O4 [synthetic construct]" 84.00 505 100.00 100.00 2.84e-82 EMBL CAA63819 "AFX [Homo sapiens]" 84.00 501 99.21 99.21 1.27e-81 EMBL CAA72156 "AFX1 [Homo sapiens]" 84.00 504 100.00 100.00 1.69e-82 GB AAD42108 "forkhead protein AFXH [Mus musculus]" 83.33 505 98.40 99.20 5.08e-80 GB AAI06762 "Forkhead box O4 [Homo sapiens]" 84.00 505 100.00 100.00 2.84e-82 GB AAI39276 "Forkhead box O4 [Mus musculus]" 83.33 505 98.40 99.20 5.08e-80 GB AAI39305 "Forkhead box O4 [Mus musculus]" 83.33 505 98.40 99.20 5.08e-80 GB AAI48035 "FOXO4 protein [Bos taurus]" 83.33 512 99.20 100.00 4.87e-81 REF NP_001094747 "forkhead box protein O4 [Bos taurus]" 83.33 512 99.20 100.00 4.87e-81 REF NP_005929 "forkhead box protein O4 isoform 1 [Homo sapiens]" 84.00 505 100.00 100.00 2.84e-82 REF NP_061259 "forkhead box protein O4 [Mus musculus]" 83.33 505 98.40 99.20 5.08e-80 REF XP_002720130 "PREDICTED: forkhead box protein O4 [Oryctolagus cuniculus]" 84.00 506 99.21 100.00 1.16e-81 REF XP_002763017 "PREDICTED: forkhead box protein O4 [Callithrix jacchus]" 84.00 505 100.00 100.00 3.07e-82 SP P98177 "RecName: Full=Forkhead box protein O4; AltName: Full=Fork head domain transcription factor AFX1" 84.00 505 100.00 100.00 2.84e-82 SP Q9WVH3 "RecName: Full=Forkhead box protein O4; AltName: Full=Afxh; AltName: Full=Fork head domain transcription factor AFX1" 83.33 505 98.40 99.20 5.08e-80 TPG DAA12928 "TPA: forkhead box O4 [Bos taurus]" 83.33 512 99.20 100.00 4.87e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AFX 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 _Vendor_name $AFX 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b Novagen stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AFX 1.5 mM '[U-13C; U-15N]' 'Na phosphate' 20 mM . NaCl 100 mM . EDTA 1 mM . Pefabloc 1 mM . NaN3 0.02 '% w/v' . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Inova' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 pH temperature 304 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_ref_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value _Correction_value_citation_label H2O H 1 protons ppm 4.695 internal direct spherical internal parallel_to_Bo . $ref_1 temperature -0.083 $ref_1 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $ref_1 . . . DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $ref_1 . . . 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chem_ref_1 _Mol_system_component_name AFX-DBD _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 . 12 GLY N N 110.52 0.1 1 2 . 12 GLY H H 8.350 0.01 1 3 . 12 GLY CA C 45.37 0.1 1 4 . 12 GLY C C 173.81 0.1 1 5 . 13 LEU N N 121.58 0.1 1 6 . 13 LEU H H 8.007 0.01 1 7 . 13 LEU CA C 55.11 0.1 1 8 . 13 LEU HA H 4.339 0.01 1 9 . 13 LEU C C 177.04 0.1 1 10 . 13 LEU CB C 42.49 0.1 1 11 . 13 LEU HB3 H 1.522 0.01 2 12 . 13 LEU HB2 H 1.572 0.01 2 13 . 13 LEU CD1 C 24.92 0.1 2 14 . 13 LEU CD2 C 23.57 0.1 2 15 . 14 VAL N N 122.46 0.1 1 16 . 14 VAL H H 8.034 0.01 1 17 . 14 VAL CA C 59.78 0.1 1 18 . 14 VAL HA H 4.369 0.01 1 19 . 14 VAL CB C 32.77 0.1 1 20 . 14 VAL HB H 2.025 0.01 1 21 . 14 VAL CG1 C 21.12 0.1 1 22 . 14 VAL CG2 C 20.41 0.1 1 23 . 15 PRO CA C 63.16 0.1 1 24 . 15 PRO HA H 4.382 0.01 1 25 . 15 PRO C C 176.85 0.1 1 26 . 15 PRO CB C 32.10 0.1 1 27 . 15 PRO CD C 51.12 0.1 1 28 . 15 PRO HD3 H 3.616 0.01 2 29 . 15 PRO HD2 H 3.816 0.01 2 30 . 16 ARG N N 121.78 0.1 1 31 . 16 ARG H H 8.402 0.01 1 32 . 16 ARG CA C 56.44 0.1 1 33 . 16 ARG HA H 4.295 0.01 1 34 . 16 ARG C C 176.99 0.1 1 35 . 16 ARG CB C 30.90 0.1 1 36 . 17 GLY N N 110.24 0.1 1 37 . 17 GLY H H 8.422 0.01 1 38 . 17 GLY CA C 45.37 0.1 1 39 . 17 GLY C C 174.20 0.1 1 40 . 18 SER N N 115.50 0.1 1 41 . 18 SER H H 8.174 0.01 1 42 . 18 SER CA C 58.58 0.1 1 43 . 18 SER HA H 4.385 0.01 1 44 . 18 SER CB C 63.86 0.1 1 45 . 20 MET CA C 55.67 0.1 1 46 . 20 MET HA H 4.391 0.01 1 47 . 20 MET C C 175.80 0.1 1 48 . 20 MET CB C 32.96 0.1 1 49 . 20 MET HB3 H 2.026 0.01 2 50 . 20 MET HB2 H 1.923 0.01 2 51 . 20 MET CG C 32.04 0.1 1 52 . 20 MET HG3 H 2.456 0.01 2 53 . 20 MET HG2 H 2.391 0.01 2 54 . 21 LEU N N 122.83 0.1 1 55 . 21 LEU H H 8.182 0.01 1 56 . 21 LEU CA C 55.24 0.1 1 57 . 21 LEU HA H 4.311 0.01 1 58 . 21 LEU CB C 42.43 0.1 1 59 . 21 LEU HB3 H 1.574 0.01 2 60 . 21 LEU HB2 H 1.607 0.01 2 61 . 22 GLU N N 121.25 0.1 1 62 . 22 GLU H H 8.218 0.01 1 63 . 22 GLU CA C 56.27 0.1 1 64 . 22 GLU HA H 4.241 0.01 1 65 . 22 GLU CB C 30.64 0.1 1 66 . 22 GLU HB3 H 1.983 0.01 2 67 . 22 GLU HB2 H 1.877 0.01 2 68 . 24 PRO CA C 64.04 0.1 1 69 . 24 PRO HA H 4.386 0.01 1 70 . 24 PRO C C 177.71 0.1 1 71 . 24 PRO CB C 32.08 0.1 1 72 . 24 PRO HB3 H 1.950 0.01 2 73 . 24 PRO HB2 H 2.256 0.01 2 74 . 24 PRO CG C 27.20 0.1 1 75 . 24 PRO CD C 50.92 0.1 1 76 . 25 GLY N N 107.74 0.1 1 77 . 25 GLY H H 8.462 0.01 1 78 . 25 GLY CA C 45.36 0.1 1 79 . 25 GLY HA3 H 3.959 0.01 2 80 . 25 GLY HA2 H 3.800 0.01 2 81 . 25 GLY C C 174.14 0.1 1 82 . 26 ALA N N 123.40 0.1 1 83 . 26 ALA H H 7.835 0.01 1 84 . 26 ALA CA C 52.60 0.1 1 85 . 26 ALA HA H 4.320 0.01 1 86 . 26 ALA C C 177.85 0.1 1 87 . 26 ALA CB C 19.31 0.1 1 88 . 27 VAL N N 118.46 0.1 1 89 . 27 VAL H H 7.967 0.01 1 90 . 27 VAL CA C 62.50 0.1 1 91 . 27 VAL HA H 4.154 0.01 1 92 . 27 VAL C C 176.42 0.1 1 93 . 27 VAL CB C 32.66 0.1 1 94 . 27 VAL HB H 2.109 0.01 1 95 . 27 VAL CG1 C 21.45 0.1 2 96 . 27 VAL CG2 C 20.72 0.1 2 97 . 28 THR N N 116.25 0.1 1 98 . 28 THR H H 8.063 0.01 1 99 . 28 THR CA C 61.57 0.1 1 100 . 28 THR HA H 4.387 0.01 1 101 . 28 THR C C 174.69 0.1 1 102 . 28 THR CB C 69.96 0.1 1 103 . 28 THR HB H 4.223 0.01 1 104 . 28 THR CG2 C 21.54 0.1 1 105 . 29 GLY N N 110.97 0.1 1 106 . 29 GLY H H 8.114 0.01 1 107 . 29 GLY CA C 44.74 0.1 1 108 . 30 PRO HB3 H 1.877 0.01 2 109 . 30 PRO HB2 H 2.245 0.01 2 110 . 30 PRO CG C 27.30 0.1 1 111 . 30 PRO CD C 49.92 0.1 1 112 . 30 PRO HD3 H 3.582 0.01 2 113 . 30 PRO HD2 H 3.602 0.01 2 114 . 32 LYS CA C 56.48 0.1 1 115 . 32 LYS C C 177.04 0.1 1 116 . 32 LYS CB C 33.04 0.1 1 117 . 33 GLY N N 110.45 0.1 1 118 . 33 GLY H H 8.436 0.01 1 119 . 33 GLY CA C 45.39 0.1 1 120 . 33 GLY C C 174.63 0.1 1 121 . 34 GLY N N 108.73 0.1 1 122 . 34 GLY H H 8.250 0.01 1 123 . 34 GLY CA C 45.28 0.1 1 124 . 34 GLY C C 174.24 0.1 1 125 . 35 SER N N 115.65 0.1 1 126 . 35 SER H H 8.241 0.01 1 127 . 35 SER CA C 58.39 0.1 1 128 . 35 SER HA H 4.422 0.01 1 129 . 35 SER C C 176.35 0.1 1 130 . 35 SER CB C 63.93 0.1 1 131 . 35 SER HB3 H 3.743 0.01 2 132 . 35 SER HB2 H 3.657 0.01 2 133 . 36 ARG N N 122.79 0.1 1 134 . 36 ARG H H 8.346 0.01 1 135 . 36 ARG CA C 56.04 0.1 1 136 . 36 ARG HA H 4.340 0.01 1 137 . 36 ARG C C 176.12 0.1 1 138 . 36 ARG CB C 30.85 0.1 1 139 . 37 ARG N N 121.72 0.1 1 140 . 37 ARG H H 8.245 0.01 1 141 . 37 ARG CA C 56.72 0.1 1 142 . 37 ARG HA H 4.124 0.01 1 143 . 37 ARG C C 175.79 0.1 1 144 . 37 ARG CB C 30.95 0.1 1 145 . 37 ARG HB3 H 1.651 0.01 2 146 . 37 ARG HB2 H 1.698 0.01 2 147 . 37 ARG CG C 27.14 0.1 1 148 . 37 ARG CD C 43.32 0.1 1 149 . 38 ASN N N 117.97 0.1 1 150 . 38 ASN H H 7.853 0.01 1 151 . 38 ASN CA C 52.16 0.1 1 152 . 38 ASN HA H 4.454 0.01 1 153 . 38 ASN C C 175.20 0.1 1 154 . 38 ASN CB C 39.01 0.1 1 155 . 38 ASN HB3 H 1.420 0.02 2 156 . 38 ASN HB2 H 1.897 0.02 2 157 . 38 ASN ND2 N 113.95 0.1 1 158 . 38 ASN HD21 H 6.823 0.01 1 159 . 38 ASN HD22 H 6.972 0.01 1 160 . 39 ALA N N 123.22 0.1 1 161 . 39 ALA H H 8.162 0.01 1 162 . 39 ALA CA C 53.70 0.1 1 163 . 39 ALA HA H 3.913 0.01 1 164 . 39 ALA C C 177.31 0.1 1 165 . 39 ALA CB C 18.82 0.1 1 166 . 40 TRP N N 113.74 0.1 1 167 . 40 TRP H H 6.948 0.03 1 168 . 40 TRP CA C 56.98 0.1 1 169 . 40 TRP HA H 4.341 0.01 1 170 . 40 TRP C C 175.79 0.1 1 171 . 40 TRP CB C 29.21 0.1 1 172 . 40 TRP HB3 H 2.730 0.01 2 173 . 40 TRP HB2 H 3.069 0.01 2 174 . 40 TRP CD1 C 126.79 0.1 1 175 . 40 TRP HD1 H 6.999 0.01 1 176 . 40 TRP NE1 N 130.80 0.1 1 177 . 40 TRP HE1 H 10.079 0.1 1 178 . 40 TRP HE3 H 6.910 0.01 1 179 . 40 TRP CZ2 C 114.59 0.1 1 180 . 40 TRP HZ2 H 7.062 0.01 1 181 . 40 TRP CZ3 C 122.14 0.1 1 182 . 40 TRP HZ3 H 7.014 0.01 1 183 . 40 TRP CH2 C 124.98 0.1 1 184 . 40 TRP HH2 H 6.931 0.01 1 185 . 41 GLY N N 110.00 0.1 1 186 . 41 GLY H H 7.385 0.02 1 187 . 41 GLY CA C 44.92 0.1 1 188 . 41 GLY HA3 H 3.650 0.01 2 189 . 41 GLY HA2 H 4.236 0.01 2 190 . 41 GLY C C 173.32 0.1 1 191 . 42 ASN N N 118.06 0.1 1 192 . 42 ASN H H 8.418 0.01 1 193 . 42 ASN CA C 53.79 0.1 1 194 . 42 ASN HA H 4.618 0.01 1 195 . 42 ASN C C 175.53 0.1 1 196 . 42 ASN CB C 38.77 0.1 1 197 . 42 ASN HB3 H 2.841 0.01 2 198 . 42 ASN HB2 H 2.710 0.01 2 199 . 42 ASN ND2 N 112.46 0.1 1 200 . 42 ASN HD21 H 6.870 0.01 1 201 . 42 ASN HD22 H 7.526 0.01 1 202 . 43 GLN N N 119.33 0.1 1 203 . 43 GLN H H 8.268 0.01 1 204 . 43 GLN CA C 56.17 0.1 1 205 . 43 GLN HA H 4.446 0.01 1 206 . 43 GLN C C 175.95 0.1 1 207 . 43 GLN CB C 30.32 0.1 1 208 . 43 GLN HB3 H 2.007 0.01 2 209 . 43 GLN HB2 H 1.967 0.01 2 210 . 43 GLN CG C 34.42 0.1 1 211 . 43 GLN NE2 N 111.20 0.1 1 212 . 43 GLN HE21 H 6.806 0.01 1 213 . 43 GLN HE22 H 7.426 0.01 1 214 . 44 SER N N 118.37 0.1 1 215 . 44 SER H H 8.783 0.01 1 216 . 44 SER CA C 57.46 0.1 1 217 . 44 SER HA H 4.646 0.01 1 218 . 44 SER C C 175.82 0.1 1 219 . 44 SER CB C 64.94 0.1 1 220 . 44 SER HB3 H 4.023 0.01 1 221 . 44 SER HB2 H 4.353 0.01 1 222 . 45 TYR N N 119.89 0.1 1 223 . 45 TYR H H 8.828 0.01 1 224 . 45 TYR CA C 63.02 0.1 1 225 . 45 TYR HA H 4.228 0.01 1 226 . 45 TYR C C 178.16 0.1 1 227 . 45 TYR CB C 38.62 0.1 1 228 . 45 TYR HB3 H 2.738 0.01 1 229 . 45 TYR HB2 H 2.960 0.01 1 230 . 46 ALA N N 119.27 0.1 1 231 . 46 ALA H H 8.606 0.01 1 232 . 46 ALA CA C 56.08 0.1 1 233 . 46 ALA HA H 4.038 0.01 1 234 . 46 ALA C C 180.23 0.1 1 235 . 46 ALA CB C 17.62 0.1 1 236 . 47 GLU N N 119.58 0.1 1 237 . 47 GLU H H 7.963 0.01 1 238 . 47 GLU CA C 59.42 0.1 1 239 . 47 GLU HA H 4.055 0.01 1 240 . 47 GLU C C 179.21 0.1 1 241 . 47 GLU CB C 29.75 0.1 1 242 . 47 GLU HB3 H 2.089 0.01 1 243 . 47 GLU HB2 H 2.307 0.01 1 244 . 48 LEU N N 121.19 0.1 1 245 . 48 LEU H H 8.010 0.01 1 246 . 48 LEU CA C 58.22 0.1 1 247 . 48 LEU HA H 4.123 0.01 1 248 . 48 LEU C C 177.93 0.1 1 249 . 48 LEU CB C 42.87 0.1 1 250 . 48 LEU HB3 H 1.517 0.01 1 251 . 48 LEU HB2 H 2.017 0.01 1 252 . 48 LEU CG C 26.90 0.1 1 253 . 48 LEU HG H 1.783 0.01 1 254 . 48 LEU CD1 C 25.88 0.1 1 255 . 48 LEU CD2 C 23.13 0.1 1 256 . 49 ILE N N 117.77 0.1 1 257 . 49 ILE H H 8.492 0.01 1 258 . 49 ILE CA C 65.56 0.1 1 259 . 49 ILE HA H 3.012 0.01 1 260 . 49 ILE C C 177.52 0.1 1 261 . 49 ILE CB C 38.15 0.1 1 262 . 49 ILE HB H 1.496 0.01 1 263 . 49 ILE CG1 C 29.56 0.1 1 264 . 49 ILE HG13 H 1.831 0.01 2 265 . 49 ILE HG12 H 0.401 0.01 2 266 . 49 ILE CG2 C 18.98 0.1 1 267 . 49 ILE CD1 C 15.34 0.1 1 268 . 50 SER N N 113.06 0.1 1 269 . 50 SER H H 7.912 0.01 1 270 . 50 SER CA C 62.95 0.1 1 271 . 50 SER HA H 4.093 0.01 1 272 . 50 SER C C 175.21 0.1 1 273 . 50 SER CB C 62.91 0.1 1 274 . 51 GLN N N 120.54 0.1 1 275 . 51 GLN H H 7.719 0.01 1 276 . 51 GLN CA C 58.88 0.1 1 277 . 51 GLN HA H 3.841 0.01 1 278 . 51 GLN C C 178.34 0.1 1 279 . 51 GLN CB C 28.50 0.1 1 280 . 51 GLN HB3 H 2.123 0.01 2 281 . 51 GLN HB2 H 2.193 0.01 2 282 . 51 GLN CG C 34.31 0.1 1 283 . 51 GLN HG3 H 2.389 0.01 2 284 . 51 GLN HG2 H 2.600 0.01 2 285 . 51 GLN NE2 N 109.81 0.1 1 286 . 51 GLN HE21 H 6.776 0.01 1 287 . 51 GLN HE22 H 7.443 0.01 1 288 . 52 ALA N N 123.79 0.1 1 289 . 52 ALA H H 7.382 0.01 1 290 . 52 ALA CA C 54.77 0.1 1 291 . 52 ALA HA H 2.003 0.01 1 292 . 52 ALA C C 179.52 0.1 1 293 . 52 ALA CB C 16.78 0.1 1 294 . 53 ILE N N 117.72 0.1 1 295 . 53 ILE H H 7.786 0.01 1 296 . 53 ILE CA C 66.16 0.1 1 297 . 53 ILE HA H 3.165 0.01 1 298 . 53 ILE C C 177.75 0.1 1 299 . 53 ILE CB C 38.49 0.1 1 300 . 53 ILE HB H 1.614 0.01 1 301 . 53 ILE CG1 C 30.00 0.1 1 302 . 53 ILE HG13 H 1.677 0.01 2 303 . 53 ILE HG12 H 0.642 0.01 2 304 . 53 ILE CG2 C 18.83 0.1 1 305 . 53 ILE CD1 C 14.30 0.1 1 306 . 54 GLU N N 116.20 0.1 1 307 . 54 GLU H H 8.360 0.01 1 308 . 54 GLU CA C 58.87 0.1 1 309 . 54 GLU HA H 3.897 0.01 1 310 . 54 GLU C C 177.73 0.1 1 311 . 54 GLU CB C 29.83 0.1 1 312 . 54 GLU HB3 H 1.958 0.01 1 313 . 54 GLU HB2 H 2.035 0.01 1 314 . 54 GLU CG C 37.20 0.1 1 315 . 54 GLU HG3 H 2.343 0.01 2 316 . 54 GLU HG2 H 2.226 0.01 2 317 . 55 SER N N 111.69 0.1 1 318 . 55 SER H H 7.373 0.01 1 319 . 55 SER CA C 59.28 0.1 1 320 . 55 SER HA H 4.346 0.01 1 321 . 55 SER C C 173.90 0.1 1 322 . 55 SER CB C 63.97 0.1 1 323 . 56 ALA N N 128.27 0.1 1 324 . 56 ALA H H 7.462 0.01 1 325 . 56 ALA CA C 50.32 0.1 1 326 . 56 ALA HA H 4.707 0.01 1 327 . 56 ALA CB C 18.76 0.1 1 328 . 57 PRO CA C 65.53 0.1 1 329 . 57 PRO HA H 4.319 0.01 1 330 . 57 PRO CB C 31.93 0.1 1 331 . 57 PRO HB3 H 1.971 0.01 2 332 . 57 PRO HB2 H 2.409 0.01 2 333 . 57 PRO CG C 27.91 0.1 1 334 . 57 PRO HG3 H 2.127 0.01 2 335 . 57 PRO HG2 H 2.225 0.01 2 336 . 57 PRO CD C 50.67 0.1 1 337 . 57 PRO HD3 H 3.902 0.01 2 338 . 57 PRO HD2 H 4.045 0.01 2 339 . 58 GLU CA C 56.29 0.1 1 340 . 58 GLU C C 175.85 0.1 1 341 . 59 LYS N N 113.76 0.1 1 342 . 59 LYS H H 8.161 0.01 1 343 . 59 LYS CA C 56.01 0.1 1 344 . 59 LYS HA H 4.244 0.01 1 345 . 59 LYS C C 173.87 0.1 1 346 . 59 LYS CB C 29.12 0.1 1 347 . 59 LYS HB3 H 2.019 0.01 2 348 . 59 LYS HB2 H 1.713 0.01 2 349 . 59 LYS CG C 24.94 0.1 1 350 . 59 LYS HG3 H 1.300 0.01 2 351 . 59 LYS HG2 H 1.395 0.01 2 352 . 59 LYS CD C 28.88 0.1 1 353 . 59 LYS HD3 H 1.606 0.01 2 354 . 59 LYS HD2 H 1.876 0.01 2 355 . 59 LYS CE C 42.68 0.1 1 356 . 59 LYS HE3 H 3.015 0.01 2 357 . 59 LYS HE2 H 3.057 0.01 2 358 . 60 ARG N N 109.68 0.1 1 359 . 60 ARG H H 6.757 0.01 1 360 . 60 ARG CA C 53.93 0.1 1 361 . 60 ARG HA H 5.314 0.01 1 362 . 60 ARG C C 173.82 0.1 1 363 . 60 ARG CB C 32.69 0.1 1 364 . 60 ARG HB3 H 1.619 0.01 1 365 . 60 ARG HB2 H 1.248 0.01 1 366 . 60 ARG CG C 24.33 0.1 1 367 . 60 ARG HG3 H 0.607 0.01 2 368 . 60 ARG HG2 H 1.138 0.01 2 369 . 60 ARG CD C 43.23 0.1 1 370 . 60 ARG HD3 H 1.587 0.01 2 371 . 60 ARG HD2 H 2.130 0.01 2 372 . 60 ARG NE N 84.57 0.1 1 373 . 60 ARG HE H 6.074 0.01 1 374 . 61 LEU N N 120.13 0.1 1 375 . 61 LEU H H 8.617 0.01 1 376 . 61 LEU CA C 54.17 0.1 1 377 . 61 LEU HA H 5.260 0.01 1 378 . 61 LEU C C 177.20 0.1 1 379 . 61 LEU CB C 49.63 0.1 1 380 . 61 LEU HB3 H 1.851 0.01 1 381 . 61 LEU HB2 H 1.427 0.01 1 382 . 61 LEU CG C 27.25 0.1 1 383 . 61 LEU HG H 1.404 0.01 1 384 . 61 LEU CD1 C 27.08 0.1 1 385 . 61 LEU CD2 C 23.89 0.1 1 386 . 62 THR N N 112.50 0.1 1 387 . 62 THR H H 8.892 0.01 1 388 . 62 THR CA C 60.60 0.1 1 389 . 62 THR HA H 4.983 0.01 1 390 . 62 THR C C 175.56 0.1 1 391 . 62 THR CB C 71.14 0.1 1 392 . 62 THR HB H 4.586 0.01 1 393 . 62 THR CG2 C 21.39 0.1 1 394 . 63 LEU N N 122.29 0.1 1 395 . 63 LEU H H 9.309 0.01 1 396 . 63 LEU CA C 58.68 0.1 1 397 . 63 LEU HA H 3.687 0.01 1 398 . 63 LEU C C 177.75 0.1 1 399 . 63 LEU CB C 41.74 0.1 1 400 . 63 LEU HB3 H 1.722 0.01 1 401 . 63 LEU HB2 H 1.503 0.01 1 402 . 63 LEU CG C 26.73 0.1 1 403 . 63 LEU HG H 0.966 0.01 1 404 . 63 LEU CD1 C 23.86 0.1 1 405 . 63 LEU CD2 C 25.65 0.1 1 406 . 64 ALA N N 117.89 0.1 1 407 . 64 ALA H H 8.255 0.01 1 408 . 64 ALA CA C 55.36 0.1 1 409 . 64 ALA HA H 3.927 0.01 1 410 . 64 ALA C C 181.15 0.1 1 411 . 64 ALA CB C 18.28 0.1 1 412 . 65 GLN N N 116.34 0.1 1 413 . 65 GLN H H 7.639 0.01 1 414 . 65 GLN CA C 58.52 0.1 1 415 . 65 GLN HA H 4.177 0.01 1 416 . 65 GLN C C 180.08 0.1 1 417 . 65 GLN CB C 30.50 0.1 1 418 . 65 GLN HB3 H 2.170 0.01 1 419 . 65 GLN HB2 H 2.571 0.01 1 420 . 65 GLN CG C 35.05 0.1 1 421 . 65 GLN NE2 N 110.57 0.1 1 422 . 65 GLN HE21 H 6.809 0.01 1 423 . 65 GLN HE22 H 7.540 0.01 1 424 . 66 ILE N N 124.58 0.1 1 425 . 66 ILE H H 8.352 0.01 1 426 . 66 ILE CA C 66.67 0.1 1 427 . 66 ILE HA H 3.529 0.01 1 428 . 66 ILE C C 177.86 0.1 1 429 . 66 ILE CB C 37.72 0.1 1 430 . 66 ILE HB H 1.958 0.01 1 431 . 66 ILE CG1 C 30.89 0.1 1 432 . 66 ILE HG13 H 0.431 0.01 2 433 . 66 ILE HG12 H 1.899 0.01 2 434 . 66 ILE CG2 C 18.23 0.1 1 435 . 66 ILE CD1 C 13.78 0.1 1 436 . 67 TYR N N 118.38 0.1 1 437 . 67 TYR H H 8.193 0.01 1 438 . 67 TYR CA C 59.31 0.1 1 439 . 67 TYR HA H 4.537 0.01 1 440 . 67 TYR C C 178.24 0.1 1 441 . 67 TYR CB C 36.84 0.1 1 442 . 67 TYR HB3 H 3.258 0.01 2 443 . 67 TYR HB2 H 3.326 0.01 2 444 . 68 GLU N N 117.69 0.1 1 445 . 68 GLU H H 8.138 0.01 1 446 . 68 GLU CA C 59.59 0.1 1 447 . 68 GLU HA H 4.002 0.01 1 448 . 68 GLU C C 178.45 0.1 1 449 . 68 GLU CB C 29.75 0.1 1 450 . 68 GLU HB3 H 2.141 0.01 1 451 . 68 GLU HB2 H 2.200 0.01 1 452 . 68 GLU CG C 36.54 0.1 1 453 . 68 GLU HG3 H 2.324 0.01 2 454 . 68 GLU HG2 H 2.521 0.01 2 455 . 69 TRP N N 120.62 0.1 1 456 . 69 TRP H H 8.247 0.01 1 457 . 69 TRP CA C 62.66 0.1 1 458 . 69 TRP HA H 3.955 0.01 1 459 . 69 TRP C C 179.57 0.1 1 460 . 69 TRP CB C 29.03 0.1 1 461 . 69 TRP HB3 H 3.515 0.01 2 462 . 69 TRP HB2 H 3.296 0.01 2 463 . 69 TRP CD1 C 126.81 0.1 1 464 . 69 TRP HD1 H 7.248 0.01 1 465 . 69 TRP NE1 N 129.03 0.1 1 466 . 69 TRP HE1 H 9.913 0.01 1 467 . 69 TRP CE3 C 119.98 0.1 1 468 . 69 TRP HE3 H 7.215 0.01 1 469 . 69 TRP CZ2 C 114.21 0.1 1 470 . 69 TRP HZ2 H 7.307 0.01 1 471 . 69 TRP CZ3 C 122.22 0.1 1 472 . 69 TRP HZ3 H 6.864 0.01 1 473 . 69 TRP CH2 C 124.70 0.1 1 474 . 69 TRP HH2 H 7.028 0.01 1 475 . 70 MET N N 119.50 0.1 1 476 . 70 MET H H 8.399 0.01 1 477 . 70 MET CA C 58.74 0.1 1 478 . 70 MET HA H 3.919 0.01 1 479 . 70 MET CB C 31.67 0.1 1 480 . 70 MET HB3 H 1.267 0.01 1 481 . 70 MET HB2 H 2.321 0.01 1 482 . 70 MET CG C 33.64 0.1 1 483 . 70 MET HG3 H 2.785 0.01 2 484 . 70 MET HG2 H 2.740 0.01 2 485 . 70 MET CE C 18.20 0.1 1 486 . 71 VAL N N 115.62 0.1 1 487 . 71 VAL H H 7.578 0.01 1 488 . 71 VAL CA C 64.98 0.1 1 489 . 71 VAL HA H 3.413 0.01 1 490 . 71 VAL C C 177.49 0.1 1 491 . 71 VAL CB C 32.09 0.1 1 492 . 71 VAL HB H 2.041 0.01 1 493 . 71 VAL CG1 C 21.57 0.1 1 494 . 71 VAL CG2 C 22.59 0.1 1 495 . 72 ARG N N 116.72 0.1 1 496 . 72 ARG H H 7.668 0.01 1 497 . 72 ARG CA C 57.90 0.1 1 498 . 72 ARG HA H 4.076 0.01 1 499 . 72 ARG C C 178.10 0.1 1 500 . 72 ARG CB C 31.22 0.1 1 501 . 72 ARG HB3 H 1.647 0.01 2 502 . 72 ARG HB2 H 1.743 0.01 2 503 . 72 ARG CG C 27.65 0.1 1 504 . 72 ARG HG3 H 1.526 0.01 2 505 . 72 ARG HG2 H 1.640 0.01 2 506 . 72 ARG CD C 43.48 0.1 1 507 . 72 ARG NE N 112.91 0.1 1 508 . 72 ARG HE H 7.382 0.01 1 509 . 73 THR N N 112.00 0.1 1 510 . 73 THR H H 7.506 0.01 1 511 . 73 THR CA C 64.47 0.1 1 512 . 73 THR HA H 3.877 0.01 1 513 . 73 THR C C 174.18 0.1 1 514 . 73 THR CB C 69.75 0.1 1 515 . 73 THR HB H 2.758 0.01 1 516 . 73 THR CG2 C 21.13 0.1 1 517 . 74 VAL N N 124.31 0.1 1 518 . 74 VAL H H 7.972 0.01 1 519 . 74 VAL CA C 60.01 0.1 1 520 . 74 VAL HA H 4.254 0.01 1 521 . 74 VAL CB C 32.29 0.1 1 522 . 74 VAL HB H 2.327 0.01 1 523 . 74 VAL CG1 C 21.77 0.1 1 524 . 74 VAL CG2 C 21.66 0.1 1 525 . 75 PRO CA C 66.10 0.1 1 526 . 75 PRO HA H 4.025 0.01 1 527 . 75 PRO C C 177.68 0.1 1 528 . 75 PRO CB C 31.99 0.1 1 529 . 75 PRO HB3 H 1.903 0.01 2 530 . 75 PRO HB2 H 2.290 0.01 2 531 . 75 PRO CG C 27.41 0.1 1 532 . 75 PRO HG3 H 1.903 0.01 2 533 . 75 PRO HG2 H 2.046 0.01 2 534 . 75 PRO CD C 51.11 0.1 1 535 . 75 PRO HD3 H 3.685 0.01 2 536 . 75 PRO HD2 H 3.984 0.01 2 537 . 76 TYR N N 115.61 0.1 1 538 . 76 TYR H H 7.824 0.01 1 539 . 76 TYR CA C 60.45 0.1 1 540 . 76 TYR HA H 4.008 0.01 1 541 . 76 TYR C C 175.60 0.1 1 542 . 76 TYR CB C 39.17 0.1 1 543 . 76 TYR HB3 H 2.072 0.01 1 544 . 76 TYR HB2 H 2.987 0.01 1 545 . 77 PHE N N 113.89 0.1 1 546 . 77 PHE H H 7.406 0.01 1 547 . 77 PHE CA C 58.38 0.1 1 548 . 77 PHE HA H 3.880 0.01 1 549 . 77 PHE C C 176.00 0.1 1 550 . 77 PHE CB C 38.16 0.1 1 551 . 77 PHE HB3 H 2.313 0.01 1 552 . 77 PHE HB2 H 2.423 0.01 1 553 . 77 PHE CZ C 129.54 0.1 1 554 . 77 PHE HZ H 6.498 0.01 1 555 . 78 LYS N N 120.13 0.1 1 556 . 78 LYS H H 7.490 0.01 1 557 . 78 LYS CA C 58.76 0.1 1 558 . 78 LYS HA H 4.205 0.01 1 559 . 78 LYS C C 177.49 0.1 1 560 . 78 LYS CB C 32.88 0.1 1 561 . 78 LYS HB3 H 1.771 0.01 2 562 . 78 LYS HB2 H 1.942 0.01 2 563 . 78 LYS CG C 24.60 0.1 1 564 . 78 LYS CD C 29.16 0.1 1 565 . 78 LYS CE C 41.95 0.1 1 566 . 79 ASP N N 117.15 0.1 1 567 . 79 ASP H H 8.094 0.01 1 568 . 79 ASP CA C 54.06 0.1 1 569 . 79 ASP HA H 4.694 0.01 1 570 . 79 ASP C C 176.74 0.1 1 571 . 79 ASP CB C 40.71 0.1 1 572 . 79 ASP HB3 H 2.619 0.01 2 573 . 79 ASP HB2 H 2.772 0.01 2 574 . 80 LYS N N 119.63 0.1 1 575 . 80 LYS H H 7.763 0.01 1 576 . 80 LYS CA C 55.56 0.1 1 577 . 80 LYS HA H 4.612 0.01 1 578 . 80 LYS C C 177.24 0.1 1 579 . 80 LYS CB C 32.68 0.1 1 580 . 80 LYS HB3 H 2.147 0.01 1 581 . 80 LYS HB2 H 1.614 0.01 1 582 . 80 LYS CG C 24.88 0.1 1 583 . 80 LYS HG3 H 1.213 0.01 2 584 . 80 LYS HG2 H 1.350 0.01 2 585 . 80 LYS CD C 28.66 0.1 1 586 . 80 LYS HD3 H 1.594 0.01 2 587 . 80 LYS HD2 H 1.250 0.01 2 588 . 80 LYS CE C 42.21 0.1 1 589 . 80 LYS HE3 H 2.853 0.01 2 590 . 80 LYS HE2 H 2.687 0.01 2 591 . 81 GLY N N 108.27 0.1 1 592 . 81 GLY H H 8.476 0.01 1 593 . 81 GLY CA C 46.30 0.1 1 594 . 81 GLY HA3 H 4.169 0.01 2 595 . 81 GLY HA2 H 3.937 0.01 2 596 . 81 GLY C C 174.41 0.1 1 597 . 82 ASP N N 119.51 0.1 1 598 . 82 ASP H H 8.167 0.01 1 599 . 82 ASP CA C 53.74 0.1 1 600 . 82 ASP HA H 4.718 0.01 1 601 . 82 ASP C C 176.84 0.1 1 602 . 82 ASP CB C 41.39 0.1 1 603 . 82 ASP HB3 H 2.804 0.01 2 604 . 82 ASP HB2 H 2.732 0.01 2 605 . 83 SER N N 116.44 0.1 1 606 . 83 SER H H 8.442 0.01 1 607 . 83 SER CA C 60.21 0.1 1 608 . 83 SER HA H 4.208 0.01 1 609 . 83 SER C C 175.38 0.1 1 610 . 83 SER CB C 63.42 0.1 1 611 . 84 ASN N N 119.99 0.1 1 612 . 84 ASN H H 8.494 0.01 1 613 . 84 ASN CA C 54.62 0.1 1 614 . 84 ASN HA H 4.647 0.01 1 615 . 84 ASN C C 176.65 0.1 1 616 . 84 ASN CB C 38.76 0.1 1 617 . 84 ASN ND2 N 113.43 0.1 1 618 . 84 ASN HD21 H 6.925 0.01 1 619 . 84 ASN HD22 H 7.661 0.01 1 620 . 85 SER N N 115.88 0.1 1 621 . 85 SER H H 8.292 0.01 1 622 . 85 SER CA C 59.86 0.1 1 623 . 85 SER C C 175.46 0.1 1 624 . 85 SER CB C 63.70 0.1 1 625 . 86 SER N N 116.07 0.1 1 626 . 86 SER H H 8.122 0.01 1 627 . 86 SER CA C 59.23 0.1 1 628 . 86 SER HA H 4.279 0.01 1 629 . 86 SER C C 174.41 0.1 1 630 . 86 SER CB C 64.05 0.1 1 631 . 86 SER HB3 H 3.553 0.01 2 632 . 86 SER HB2 H 3.937 0.01 2 633 . 87 ALA N N 124.01 0.1 1 634 . 87 ALA H H 7.579 0.01 1 635 . 87 ALA CA C 54.08 0.1 1 636 . 87 ALA HA H 4.012 0.01 1 637 . 87 ALA C C 179.21 0.1 1 638 . 87 ALA CB C 18.89 0.1 1 639 . 88 GLY N N 106.88 0.1 1 640 . 88 GLY H H 8.240 0.01 1 641 . 88 GLY CA C 47.02 0.1 1 642 . 88 GLY HA3 H 3.888 0.01 2 643 . 88 GLY HA2 H 3.996 0.01 2 644 . 88 GLY C C 176.68 0.1 1 645 . 89 TRP N N 122.72 0.1 1 646 . 89 TRP H H 8.104 0.01 1 647 . 89 TRP CA C 59.50 0.1 1 648 . 89 TRP HA H 4.531 0.01 1 649 . 89 TRP C C 178.63 0.1 1 650 . 89 TRP CB C 28.79 0.1 1 651 . 89 TRP HB3 H 3.467 0.01 2 652 . 89 TRP HB2 H 3.348 0.01 2 653 . 89 TRP CD1 C 127.57 0.1 1 654 . 89 TRP HD1 H 7.548 0.01 1 655 . 89 TRP NE1 N 129.11 0.1 1 656 . 89 TRP HE1 H 10.114 0.1 1 657 . 89 TRP CZ2 C 114.25 0.1 1 658 . 89 TRP HZ2 H 7.211 0.01 1 659 . 89 TRP CZ3 C 121.25 0.1 1 660 . 89 TRP HZ3 H 6.739 0.01 1 661 . 89 TRP CH2 C 124.10 0.1 1 662 . 89 TRP HH2 H 7.078 0.01 1 663 . 90 LYS N N 122.04 0.1 1 664 . 90 LYS H H 7.365 0.01 1 665 . 90 LYS CA C 60.77 0.1 1 666 . 90 LYS HA H 3.348 0.01 1 667 . 90 LYS C C 179.77 0.1 1 668 . 90 LYS CB C 32.90 0.1 1 669 . 90 LYS HB3 H 1.149 0.01 2 670 . 90 LYS HB2 H 1.204 0.01 2 671 . 91 ASN N N 119.04 0.1 1 672 . 91 ASN H H 7.781 0.01 1 673 . 91 ASN CA C 56.22 0.1 1 674 . 91 ASN HA H 4.341 0.01 1 675 . 91 ASN C C 177.85 0.1 1 676 . 91 ASN CB C 38.06 0.1 1 677 . 91 ASN HB3 H 2.812 0.01 2 678 . 91 ASN HB2 H 2.786 0.01 2 679 . 91 ASN ND2 N 113.44 0.1 1 680 . 91 ASN HD21 H 6.903 0.01 1 681 . 91 ASN HD22 H 7.617 0.01 1 682 . 92 SER N N 117.47 0.1 1 683 . 92 SER H H 8.097 0.01 1 684 . 92 SER CA C 62.58 0.1 1 685 . 92 SER HA H 4.217 0.01 1 686 . 92 SER C C 177.63 0.1 1 687 . 92 SER CB C 62.56 0.1 1 688 . 92 SER HB3 H 3.782 0.01 1 689 . 92 SER HB2 H 3.327 0.01 1 690 . 93 ILE N N 124.57 0.1 1 691 . 93 ILE H H 8.179 0.01 1 692 . 93 ILE CA C 64.83 0.1 1 693 . 93 ILE HA H 3.469 0.01 1 694 . 93 ILE C C 176.51 0.1 1 695 . 93 ILE CB C 36.84 0.1 1 696 . 93 ILE HB H 2.258 0.01 1 697 . 93 ILE CG1 C 29.10 0.1 1 698 . 93 ILE HG13 H 1.311 0.01 2 699 . 93 ILE HG12 H 1.796 0.01 2 700 . 93 ILE CG2 C 16.88 0.1 1 701 . 93 ILE CD1 C 13.19 0.1 1 702 . 94 ARG N N 118.75 0.1 1 703 . 94 ARG H H 7.753 0.01 1 704 . 94 ARG CA C 60.31 0.1 1 705 . 94 ARG HA H 3.629 0.01 1 706 . 94 ARG C C 178.86 0.1 1 707 . 94 ARG CB C 29.92 0.1 1 708 . 94 ARG CG C 28.00 0.1 1 709 . 94 ARG HG3 H 1.823 0.01 2 710 . 94 ARG HG2 H 1.535 0.01 2 711 . 94 ARG CD C 43.35 0.1 1 712 . 95 HIS N N 117.52 0.1 1 713 . 95 HIS H H 8.361 0.01 1 714 . 95 HIS CA C 59.17 0.1 1 715 . 95 HIS HA H 4.341 0.01 1 716 . 95 HIS C C 177.69 0.1 1 717 . 95 HIS CB C 30.42 0.1 1 718 . 95 HIS CD2 C 119.52 0.1 1 719 . 95 HIS HD2 H 6.946 0.01 1 720 . 96 ASN N N 117.50 0.1 1 721 . 96 ASN H H 7.930 0.01 1 722 . 96 ASN CA C 57.70 0.1 1 723 . 96 ASN HA H 4.253 0.01 1 724 . 96 ASN C C 176.99 0.1 1 725 . 96 ASN CB C 40.74 0.1 1 726 . 96 ASN HB3 H 2.243 0.01 1 727 . 96 ASN HB2 H 2.719 0.01 1 728 . 96 ASN ND2 N 112.92 0.1 1 729 . 96 ASN HD21 H 7.590 0.01 1 730 . 96 ASN HD22 H 7.525 0.01 1 731 . 97 LEU N N 119.65 0.1 1 732 . 97 LEU H H 7.803 0.01 1 733 . 97 LEU CA C 57.57 0.1 1 734 . 97 LEU HA H 3.704 0.01 1 735 . 97 LEU C C 176.92 0.1 1 736 . 97 LEU CB C 40.60 0.1 1 737 . 97 LEU HB3 H -0.131 0.01 1 738 . 97 LEU HB2 H 1.033 0.01 1 739 . 97 LEU CG C 25.73 0.1 1 740 . 97 LEU HG H 0.871 0.01 1 741 . 97 LEU CD1 C 25.32 0.1 1 742 . 97 LEU CD2 C 21.72 0.1 1 743 . 98 SER N N 109.57 0.1 1 744 . 98 SER H H 7.126 0.01 1 745 . 98 SER CA C 60.13 0.1 1 746 . 98 SER HA H 4.418 0.01 1 747 . 98 SER C C 175.01 0.1 1 748 . 98 SER CB C 63.99 0.1 1 749 . 98 SER HB3 H 3.989 0.01 2 750 . 98 SER HB2 H 4.017 0.01 2 751 . 99 LEU N N 121.02 0.1 1 752 . 99 LEU H H 7.430 0.01 1 753 . 99 LEU CA C 55.63 0.1 1 754 . 99 LEU HA H 4.288 0.01 1 755 . 99 LEU CB C 43.24 0.1 1 756 . 99 LEU HB3 H 1.313 0.01 1 757 . 99 LEU HB2 H 1.558 0.01 1 758 . 99 LEU CG C 26.53 0.1 1 759 . 99 LEU HG H 1.412 0.01 1 760 . 99 LEU CD1 C 24.53 0.1 1 761 . 99 LEU CD2 C 23.78 0.1 1 762 . 100 HIS CA C 56.94 0.1 1 763 . 100 HIS HA H 4.767 0.01 1 764 . 100 HIS CB C 30.69 0.1 1 765 . 100 HIS HB3 H 3.226 0.01 1 766 . 100 HIS HB2 H 3.299 0.01 1 767 . 101 SER CA C 59.82 0.1 1 768 . 101 SER C C 174.55 0.1 1 769 . 101 SER CB C 62.95 0.1 1 770 . 102 LYS N N 119.22 0.1 1 771 . 102 LYS H H 7.770 0.01 1 772 . 102 LYS CA C 57.51 0.1 1 773 . 102 LYS HA H 4.112 0.01 1 774 . 102 LYS C C 175.54 0.1 1 775 . 102 LYS CB C 32.85 0.1 1 776 . 102 LYS HB3 H 1.008 0.01 2 777 . 102 LYS HB2 H 1.424 0.01 2 778 . 102 LYS CG C 24.22 0.1 1 779 . 102 LYS HG3 H 0.670 0.01 2 780 . 102 LYS HG2 H 0.855 0.01 2 781 . 102 LYS CD C 28.94 0.1 1 782 . 102 LYS HD3 H 1.345 0.01 2 783 . 102 LYS HD2 H 1.312 0.01 2 784 . 102 LYS CE C 41.55 0.1 1 785 . 103 PHE N N 118.69 0.1 1 786 . 103 PHE H H 7.971 0.01 1 787 . 103 PHE CA C 55.89 0.1 1 788 . 103 PHE HA H 5.649 0.01 1 789 . 103 PHE C C 174.76 0.1 1 790 . 103 PHE CB C 41.56 0.1 1 791 . 103 PHE CZ C 129.23 0.1 1 792 . 103 PHE HZ H 7.453 0.01 1 793 . 104 ILE N N 119.07 0.1 1 794 . 104 ILE H H 9.284 0.01 1 795 . 104 ILE CA C 59.52 0.1 1 796 . 104 ILE HA H 4.729 0.01 1 797 . 104 ILE C C 172.75 0.1 1 798 . 104 ILE CB C 42.20 0.1 1 799 . 104 ILE HB H 1.680 0.01 1 800 . 104 ILE CG1 C 27.27 0.1 1 801 . 104 ILE HG13 H 0.919 0.01 2 802 . 104 ILE HG12 H 1.433 0.01 2 803 . 104 ILE CG2 C 17.70 0.1 1 804 . 104 ILE CD1 C 13.92 0.1 1 805 . 105 LYS N N 125.52 0.1 1 806 . 105 LYS H H 8.013 0.01 1 807 . 105 LYS CA C 54.58 0.1 1 808 . 105 LYS HA H 4.235 0.01 1 809 . 105 LYS C C 176.52 0.1 1 810 . 105 LYS CB C 32.90 0.1 1 811 . 105 LYS HB3 H 0.953 0.01 1 812 . 105 LYS HB2 H 0.471 0.01 1 813 . 105 LYS CG C 24.37 0.1 1 814 . 105 LYS HG3 H 0.173 0.01 2 815 . 105 LYS HG2 H 0.398 0.01 2 816 . 105 LYS CD C 29.18 0.1 1 817 . 105 LYS HD3 H 1.279 0.01 2 818 . 105 LYS HD2 H 1.315 0.01 2 819 . 105 LYS CE C 41.62 0.1 1 820 . 106 VAL N N 126.41 0.1 1 821 . 106 VAL H H 8.978 0.01 1 822 . 106 VAL CA C 61.14 0.1 1 823 . 106 VAL HA H 4.143 0.01 1 824 . 106 VAL C C 174.76 0.1 1 825 . 106 VAL CB C 34.73 0.1 1 826 . 106 VAL HB H 1.859 0.01 1 827 . 106 VAL CG1 C 21.09 0.1 1 828 . 106 VAL CG2 C 21.00 0.1 1 829 . 107 HIS N N 124.05 0.1 1 830 . 107 HIS H H 8.473 0.01 1 831 . 107 HIS CA C 56.36 0.1 1 832 . 107 HIS HA H 4.465 0.01 1 833 . 107 HIS C C 174.12 0.1 1 834 . 107 HIS CB C 30.55 0.1 1 835 . 107 HIS HB3 H 3.023 0.01 2 836 . 107 HIS HB2 H 2.978 0.01 2 837 . 107 HIS HD2 H 6.961 0.01 1 838 . 107 HIS HE1 H 7.254 0.01 1 839 . 108 ASN N N 122.95 0.1 1 840 . 108 ASN H H 8.356 0.01 1 841 . 108 ASN CA C 52.60 0.1 1 842 . 108 ASN HA H 4.501 0.01 1 843 . 108 ASN C C 175.13 0.1 1 844 . 108 ASN CB C 38.97 0.1 1 845 . 108 ASN HB3 H 2.597 0.01 1 846 . 108 ASN HB2 H 2.126 0.02 1 847 . 108 ASN ND2 N 112.02 0.1 1 848 . 108 ASN HD21 H 6.472 0.01 1 849 . 108 ASN HD22 H 6.940 0.01 1 850 . 109 GLU N N 123.55 0.1 1 851 . 109 GLU H H 8.705 0.01 1 852 . 109 GLU CA C 57.98 0.1 1 853 . 109 GLU HA H 4.061 0.01 1 854 . 109 GLU C C 176.93 0.1 1 855 . 109 GLU CB C 29.70 0.1 1 856 . 109 GLU HB3 H 2.102 0.01 1 857 . 109 GLU HB2 H 1.992 0.01 1 858 . 109 GLU CG C 36.39 0.1 1 859 . 110 ALA N N 122.37 0.1 1 860 . 110 ALA H H 8.270 0.01 1 861 . 110 ALA CA C 52.96 0.1 1 862 . 110 ALA HA H 4.318 0.01 1 863 . 110 ALA C C 178.14 0.1 1 864 . 110 ALA CB C 19.02 0.1 1 865 . 111 THR N N 111.73 0.1 1 866 . 111 THR H H 7.806 0.01 1 867 . 111 THR CA C 62.42 0.1 1 868 . 111 THR HA H 4.195 0.01 1 869 . 111 THR C C 175.71 0.1 1 870 . 111 THR CB C 69.52 0.1 1 871 . 111 THR HB H 4.171 0.01 1 872 . 111 THR CG2 C 21.41 0.1 1 873 . 112 GLY N N 111.89 0.1 1 874 . 112 GLY H H 8.334 0.01 1 875 . 112 GLY CA C 45.75 0.1 1 876 . 112 GLY HA3 H 4.070 0.01 2 877 . 112 GLY HA2 H 3.788 0.01 2 878 . 112 GLY C C 174.37 0.1 1 879 . 113 LYS N N 119.50 0.1 1 880 . 113 LYS H H 7.866 0.01 1 881 . 113 LYS CA C 55.66 0.1 1 882 . 113 LYS HA H 4.402 0.01 1 883 . 113 LYS C C 176.60 0.1 1 884 . 113 LYS CB C 33.32 0.1 1 885 . 113 LYS HB3 H 1.641 0.01 2 886 . 113 LYS HB2 H 1.781 0.01 2 887 . 113 LYS CG C 25.07 0.1 1 888 . 113 LYS HG3 H 1.362 0.01 2 889 . 113 LYS HG2 H 1.272 0.01 2 890 . 113 LYS CD C 28.63 0.1 1 891 . 113 LYS CE C 42.08 0.1 1 892 . 114 SER N N 116.08 0.1 1 893 . 114 SER H H 8.070 0.01 1 894 . 114 SER CA C 58.42 0.1 1 895 . 114 SER HA H 4.425 0.01 1 896 . 114 SER C C 173.34 0.1 1 897 . 114 SER CB C 63.93 0.1 1 898 . 114 SER HB3 H 3.659 0.01 2 899 . 114 SER HB2 H 3.743 0.01 2 900 . 115 SER N N 116.90 0.1 1 901 . 115 SER H H 8.145 0.01 1 902 . 115 SER CA C 58.89 0.1 1 903 . 115 SER HA H 4.285 0.01 1 904 . 115 SER C C 173.16 0.1 1 905 . 115 SER CB C 64.02 0.1 1 906 . 115 SER HB3 H 3.431 0.01 1 907 . 115 SER HB2 H 3.341 0.01 1 908 . 116 TRP N N 120.49 0.1 1 909 . 116 TRP H H 8.346 0.01 1 910 . 116 TRP CA C 56.38 0.1 1 911 . 116 TRP HA H 4.661 0.01 1 912 . 116 TRP C C 174.43 0.1 1 913 . 116 TRP CB C 32.54 0.1 1 914 . 116 TRP HB3 H 2.864 0.01 1 915 . 116 TRP HB2 H 2.952 0.01 1 916 . 116 TRP CD1 C 126.60 0.1 1 917 . 116 TRP HD1 H 6.931 0.01 1 918 . 116 TRP NE1 N 129.92 0.1 1 919 . 116 TRP HE1 H 10.234 0.1 1 920 . 116 TRP CE3 C 119.97 0.1 1 921 . 116 TRP HE3 H 7.211 0.01 1 922 . 116 TRP CZ2 C 114.84 0.1 1 923 . 116 TRP HZ2 H 7.433 0.01 1 924 . 116 TRP CZ3 C 122.58 0.1 1 925 . 116 TRP HZ3 H 7.261 0.01 1 926 . 116 TRP CH2 C 124.74 0.1 1 927 . 116 TRP HH2 H 7.223 0.01 1 928 . 117 TRP N N 121.76 0.1 1 929 . 117 TRP H H 9.173 0.01 1 930 . 117 TRP CA C 56.86 0.1 1 931 . 117 TRP HA H 5.312 0.01 1 932 . 117 TRP C C 175.35 0.1 1 933 . 117 TRP CB C 31.01 0.1 1 934 . 117 TRP HB3 H 2.846 0.01 1 935 . 117 TRP HB2 H 2.961 0.01 1 936 . 117 TRP CD1 C 125.48 0.1 1 937 . 117 TRP HD1 H 6.874 0.01 1 938 . 117 TRP NE1 N 126.85 0.1 1 939 . 117 TRP HE1 H 9.758 0.01 1 940 . 117 TRP CE3 C 120.62 0.1 1 941 . 117 TRP HE3 H 7.317 0.01 1 942 . 117 TRP CZ2 C 114.04 0.1 1 943 . 117 TRP HZ2 H 7.324 0.01 1 944 . 117 TRP CZ3 C 122.61 0.1 1 945 . 117 TRP HZ3 H 6.961 0.01 1 946 . 117 TRP CH2 C 124.21 0.1 1 947 . 117 TRP HH2 H 7.016 0.01 1 948 . 118 MET N N 117.74 0.1 1 949 . 118 MET H H 9.195 0.01 1 950 . 118 MET CA C 54.30 0.1 1 951 . 118 MET HA H 5.057 0.01 1 952 . 118 MET C C 174.84 0.1 1 953 . 118 MET CB C 38.08 0.1 1 954 . 118 MET HB3 H 2.323 0.01 1 955 . 118 MET HB2 H 2.013 0.01 1 956 . 118 MET CG C 31.93 0.1 1 957 . 118 MET HG3 H 2.758 0.01 2 958 . 118 MET HG2 H 2.274 0.01 2 959 . 119 LEU N N 120.72 0.1 1 960 . 119 LEU H H 9.167 0.01 1 961 . 119 LEU CA C 54.83 0.1 1 962 . 119 LEU HA H 4.909 0.01 1 963 . 119 LEU C C 177.49 0.1 1 964 . 119 LEU CB C 41.97 0.1 1 965 . 119 LEU HB3 H 1.443 0.01 1 966 . 119 LEU HB2 H 1.702 0.01 1 967 . 119 LEU CG C 27.98 0.1 1 968 . 119 LEU HG H 1.776 0.01 1 969 . 119 LEU CD1 C 25.50 0.1 1 970 . 119 LEU CD2 C 24.41 0.1 1 971 . 120 ASN N N 121.54 0.1 1 972 . 120 ASN H H 8.580 0.01 1 973 . 120 ASN CA C 50.63 0.1 1 974 . 120 ASN HA H 4.668 0.01 1 975 . 120 ASN CB C 39.19 0.1 1 976 . 120 ASN HB3 H 2.398 0.01 2 977 . 120 ASN HB2 H 2.950 0.01 2 978 . 120 ASN ND2 N 112.02 0.1 1 979 . 120 ASN HD21 H 7.040 0.01 1 980 . 120 ASN HD22 H 7.645 0.01 1 981 . 121 PRO CA C 64.03 0.1 1 982 . 121 PRO HA H 4.403 0.01 1 983 . 121 PRO C C 177.31 0.1 1 984 . 121 PRO CB C 32.24 0.1 1 985 . 121 PRO HB3 H 2.000 0.01 2 986 . 121 PRO HB2 H 2.285 0.01 2 987 . 121 PRO CG C 27.14 0.1 1 988 . 121 PRO CD C 51.23 0.1 1 989 . 121 PRO HD3 H 3.913 0.01 2 990 . 121 PRO HD2 H 4.031 0.01 2 991 . 122 GLU N N 118.95 0.1 1 992 . 122 GLU H H 8.002 0.01 1 993 . 122 GLU CA C 56.59 0.1 1 994 . 122 GLU HA H 4.238 0.01 1 995 . 122 GLU C C 177.18 0.1 1 996 . 122 GLU CB C 29.94 0.1 1 997 . 122 GLU HB3 H 1.875 0.01 1 998 . 122 GLU HB2 H 2.071 0.01 1 999 . 122 GLU CG C 36.48 0.1 1 1000 . 122 GLU HG3 H 2.259 0.01 2 1001 . 122 GLU HG2 H 2.182 0.01 2 1002 . 123 GLY N N 108.73 0.1 1 1003 . 123 GLY H H 8.084 0.01 1 1004 . 123 GLY CA C 45.75 0.1 1 1005 . 123 GLY HA3 H 3.907 0.01 2 1006 . 123 GLY HA2 H 3.937 0.01 2 1007 . 123 GLY C C 174.78 0.1 1 1008 . 124 GLY N N 108.50 0.1 1 1009 . 124 GLY H H 8.159 0.01 1 1010 . 124 GLY CA C 45.47 0.1 1 1011 . 124 GLY HA3 H 3.914 0.01 2 1012 . 124 GLY HA2 H 3.969 0.01 2 1013 . 124 GLY C C 174.47 0.1 1 1014 . 125 LYS N N 120.56 0.1 1 1015 . 125 LYS H H 8.116 0.01 1 1016 . 125 LYS CA C 56.49 0.1 1 1017 . 125 LYS HA H 4.335 0.01 1 1018 . 125 LYS C C 176.92 0.1 1 1019 . 125 LYS CB C 32.99 0.1 1 1020 . 126 SER N N 116.32 0.1 1 1021 . 126 SER H H 8.300 0.01 1 1022 . 126 SER CA C 58.64 0.1 1 1023 . 126 SER C C 175.11 0.1 1 1024 . 126 SER CB C 63.82 0.1 1 1025 . 127 GLY N N 110.77 0.1 1 1026 . 127 GLY H H 8.331 0.01 1 1027 . 127 GLY CA C 45.42 0.1 1 1028 . 128 LYS N N 120.44 0.1 1 1029 . 128 LYS H H 8.065 0.01 1 1030 . 128 LYS CA C 55.93 0.1 1 1031 . 128 LYS HA H 4.317 0.01 1 1032 . 128 LYS C C 176.04 0.1 1 1033 . 128 LYS CB C 33.22 0.1 1 1034 . 129 ALA N N 126.47 0.1 1 1035 . 129 ALA H H 8.241 0.01 1 1036 . 129 ALA CA C 50.58 0.1 1 1037 . 129 ALA HA H 4.557 0.01 1 1038 . 129 ALA CB C 18.24 0.1 1 1039 . 133 ARG N N 123.16 0.1 1 1040 . 133 ARG H H 8.394 0.01 1 1041 . 133 ARG CA C 56.08 0.1 1 1042 . 133 ARG HA H 4.291 0.01 1 1043 . 133 ARG C C 175.92 0.1 1 1044 . 133 ARG CB C 30.99 0.1 1 1045 . 134 ALA N N 125.93 0.1 1 1046 . 134 ALA H H 8.337 0.01 1 1047 . 134 ALA CA C 52.48 0.1 1 1048 . 134 ALA HA H 4.280 0.01 1 1049 . 134 ALA C C 177.41 0.1 1 1050 . 134 ALA CB C 19.34 0.1 1 1051 . 135 ALA N N 123.56 0.1 1 1052 . 135 ALA H H 8.292 0.01 1 1053 . 135 ALA CA C 52.59 0.1 1 1054 . 135 ALA HA H 4.301 0.01 1 1055 . 135 ALA C C 177.82 0.1 1 1056 . 135 ALA CB C 19.27 0.1 1 1057 . 136 SER N N 114.67 0.1 1 1058 . 136 SER H H 8.205 0.01 1 1059 . 136 SER CA C 58.37 0.1 1 1060 . 136 SER HA H 4.410 0.01 1 1061 . 136 SER C C 174.74 0.1 1 1062 . 136 SER CB C 63.80 0.1 1 1063 . 137 MET N N 122.03 0.1 1 1064 . 137 MET H H 8.343 0.01 1 1065 . 137 MET CA C 55.64 0.1 1 1066 . 137 MET HA H 4.495 0.01 1 1067 . 137 MET C C 175.94 0.1 1 1068 . 137 MET CB C 32.98 0.1 1 1069 . 137 MET HB3 H 2.109 0.01 2 1070 . 137 MET HB2 H 1.997 0.01 2 1071 . 137 MET CG C 32.12 0.1 1 1072 . 137 MET HG3 H 2.515 0.01 2 1073 . 137 MET HG2 H 2.590 0.01 2 1074 . 138 ASP N N 121.46 0.1 1 1075 . 138 ASP H H 8.263 0.01 1 1076 . 138 ASP CA C 54.40 0.1 1 1077 . 138 ASP HA H 4.629 0.01 1 1078 . 138 ASP C C 176.61 0.1 1 1079 . 138 ASP CB C 41.44 0.1 1 1080 . 138 ASP HB3 H 2.713 0.01 2 1081 . 138 ASP HB2 H 2.668 0.01 2 1082 . 139 SER N N 116.88 0.1 1 1083 . 139 SER H H 8.340 0.01 1 1084 . 139 SER CA C 59.04 0.1 1 1085 . 139 SER HA H 4.413 0.01 1 1086 . 139 SER C C 175.21 0.1 1 1087 . 139 SER CB C 63.66 0.1 1 1088 . 140 SER N N 117.75 0.1 1 1089 . 140 SER H H 8.381 0.01 1 1090 . 140 SER CA C 59.39 0.1 1 1091 . 140 SER HA H 4.412 0.01 1 1092 . 140 SER C C 175.17 0.1 1 1093 . 140 SER CB C 63.60 0.1 1 1094 . 141 SER N N 117.50 0.1 1 1095 . 141 SER H H 8.190 0.01 1 1096 . 141 SER CA C 59.14 0.1 1 1097 . 141 SER HA H 4.380 0.01 1 1098 . 141 SER C C 175.10 0.1 1 1099 . 141 SER CB C 63.53 0.1 1 1100 . 142 LYS N N 122.77 0.1 1 1101 . 142 LYS H H 8.146 0.01 1 1102 . 142 LYS CA C 56.99 0.1 1 1103 . 142 LYS HA H 4.236 0.01 1 1104 . 142 LYS C C 176.77 0.1 1 1105 . 142 LYS CB C 32.75 0.1 1 1106 . 142 LYS HB3 H 1.764 0.01 2 1107 . 142 LYS HB2 H 1.851 0.01 2 1108 . 142 LYS CG C 25.00 0.1 1 1109 . 142 LYS HG3 H 1.393 0.01 2 1110 . 142 LYS HG2 H 1.446 0.01 2 1111 . 142 LYS CD C 29.03 0.1 1 1112 . 142 LYS CE C 42.05 0.1 1 1113 . 143 LEU N N 121.39 0.1 1 1114 . 143 LEU H H 7.942 0.01 1 1115 . 143 LEU CA C 55.52 0.1 1 1116 . 143 LEU HA H 4.285 0.01 1 1117 . 143 LEU C C 177.35 0.1 1 1118 . 143 LEU CB C 42.25 0.1 1 1119 . 143 LEU HB3 H 1.565 0.01 2 1120 . 143 LEU HB2 H 1.632 0.01 2 1121 . 143 LEU CD1 C 24.91 0.1 1 1122 . 143 LEU CD2 C 23.52 0.1 1 1123 . 144 LEU N N 122.16 0.1 1 1124 . 144 LEU H H 7.991 0.01 1 1125 . 144 LEU CA C 55.32 0.1 1 1126 . 144 LEU HA H 4.313 0.01 1 1127 . 144 LEU CB C 42.21 0.1 1 1128 . 144 LEU HB2 H 1.656 0.01 2 1129 . 145 ARG N N 121.17 0.1 1 1130 . 145 ARG H H 8.145 0.01 1 1131 . 145 ARG CA C 56.36 0.1 1 1132 . 145 ARG HA H 4.303 0.01 1 1133 . 145 ARG C C 176.83 0.1 1 1134 . 145 ARG CB C 30.68 0.1 1 1135 . 145 ARG HB3 H 1.862 0.01 2 1136 . 145 ARG HB2 H 1.752 0.01 2 1137 . 146 GLY N N 109.57 0.1 1 1138 . 146 GLY H H 8.324 0.01 1 1139 . 146 GLY CA C 45.41 0.1 1 1140 . 146 GLY C C 174.06 0.1 1 1141 . 147 ARG N N 120.36 0.1 1 1142 . 147 ARG H H 8.115 0.01 1 1143 . 147 ARG CA C 56.02 0.1 1 1144 . 147 ARG HA H 4.389 0.01 1 1145 . 147 ARG C C 176.40 0.1 1 1146 . 147 ARG CB C 30.94 0.1 1 1147 . 148 SER N N 117.08 0.1 1 1148 . 148 SER H H 8.329 0.01 1 1149 . 148 SER CA C 58.50 0.1 1 1150 . 148 SER C C 174.22 0.1 1 1151 . 148 SER CB C 63.86 0.1 1 1152 . 149 LYS N N 123.45 0.1 1 1153 . 149 LYS H H 8.261 0.01 1 1154 . 149 LYS CA C 56.34 0.1 1 1155 . 149 LYS HA H 4.320 0.01 1 1156 . 149 LYS C C 175.12 0.1 1 1157 . 149 LYS CB C 33.20 0.1 1 1158 . 150 ALA N N 131.00 0.1 1 1159 . 150 ALA H H 7.936 0.01 1 1160 . 150 ALA CA C 53.88 0.1 1 1161 . 150 ALA HA H 4.091 0.01 1 1162 . 150 ALA CB C 20.22 0.1 1 stop_ save_