data_17740 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N assignment of Hck kinase regulatory segment ; _BMRB_accession_number 17740 _BMRB_flat_file_name bmr17740.str _Entry_type original _Submission_date 2011-06-28 _Accession_date 2011-06-28 _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 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 170 "13C chemical shifts" 482 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-09-01 original author . stop_ _Original_release_date 2011-09-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21365684 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Gronenborn Angela M. . stop_ _Journal_abbreviation Proteins _Journal_name_full Proteins _Journal_volume 79 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1609 _Page_last 1622 _Year 2011 _Details . loop_ _Keyword AIDS Hck HIV Nef SH2 SH3 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Hck _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Hck32L $Hck32L stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hck32L _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hck32L _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Regulatory domain of Hck' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 193 _Mol_residue_sequence ; GIREAGSEDIIVVALYDYEA IHHEDLSFQKGDQMVVLEES GEWWKARSLATRKEGYIPSN YVARVDSLETEEWFFKGISR KDAERQLLAPGNMLGSFMIR DSETTKGSYSLSVRDYDPRQ GDTVKHYKIRTLDNGGFYIS PRSTFSTLQELVDHYKKGND GLCQKLSVPCMSSKPQKPWE KDAWELEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 72 GLY 2 73 ILE 3 74 ARG 4 75 GLU 5 76 ALA 6 77 GLY 7 78 SER 8 79 GLU 9 80 ASP 10 81 ILE 11 82 ILE 12 83 VAL 13 84 VAL 14 85 ALA 15 86 LEU 16 87 TYR 17 88 ASP 18 89 TYR 19 90 GLU 20 91 ALA 21 92 ILE 22 93 HIS 23 94 HIS 24 95 GLU 25 96 ASP 26 97 LEU 27 98 SER 28 99 PHE 29 100 GLN 30 101 LYS 31 102 GLY 32 103 ASP 33 104 GLN 34 105 MET 35 106 VAL 36 107 VAL 37 108 LEU 38 109 GLU 39 110 GLU 40 111 SER 41 112 GLY 42 113 GLU 43 114 TRP 44 115 TRP 45 116 LYS 46 117 ALA 47 118 ARG 48 119 SER 49 120 LEU 50 121 ALA 51 122 THR 52 123 ARG 53 124 LYS 54 125 GLU 55 126 GLY 56 127 TYR 57 128 ILE 58 129 PRO 59 130 SER 60 131 ASN 61 132 TYR 62 133 VAL 63 134 ALA 64 135 ARG 65 136 VAL 66 137 ASP 67 138 SER 68 139 LEU 69 140 GLU 70 141 THR 71 142 GLU 72 143 GLU 73 144 TRP 74 145 PHE 75 146 PHE 76 147 LYS 77 148 GLY 78 149 ILE 79 150 SER 80 151 ARG 81 152 LYS 82 153 ASP 83 154 ALA 84 155 GLU 85 156 ARG 86 157 GLN 87 158 LEU 88 159 LEU 89 160 ALA 90 161 PRO 91 162 GLY 92 163 ASN 93 164 MET 94 165 LEU 95 166 GLY 96 167 SER 97 168 PHE 98 169 MET 99 170 ILE 100 171 ARG 101 172 ASP 102 173 SER 103 174 GLU 104 175 THR 105 176 THR 106 177 LYS 107 178 GLY 108 179 SER 109 180 TYR 110 181 SER 111 182 LEU 112 183 SER 113 184 VAL 114 185 ARG 115 186 ASP 116 187 TYR 117 188 ASP 118 189 PRO 119 190 ARG 120 191 GLN 121 192 GLY 122 193 ASP 123 194 THR 124 195 VAL 125 196 LYS 126 197 HIS 127 198 TYR 128 199 LYS 129 200 ILE 130 201 ARG 131 202 THR 132 203 LEU 133 204 ASP 134 205 ASN 135 206 GLY 136 207 GLY 137 208 PHE 138 209 TYR 139 210 ILE 140 211 SER 141 212 PRO 142 213 ARG 143 214 SER 144 215 THR 145 216 PHE 146 217 SER 147 218 THR 148 219 LEU 149 220 GLN 150 221 GLU 151 222 LEU 152 223 VAL 153 224 ASP 154 225 HIS 155 226 TYR 156 227 LYS 157 228 LYS 158 229 GLY 159 230 ASN 160 231 ASP 161 232 GLY 162 233 LEU 163 234 CYS 164 235 GLN 165 236 LYS 166 237 LEU 167 238 SER 168 239 VAL 169 240 PRO 170 241 CYS 171 242 MET 172 243 SER 173 244 SER 174 245 LYS 175 246 PRO 176 247 GLN 177 248 LYS 178 249 PRO 179 250 TRP 180 251 GLU 181 252 LYS 182 253 ASP 183 254 ALA 184 255 TRP 185 256 GLU 186 257 LEU 187 258 GLU 188 259 HIS 189 260 HIS 190 261 HIS 191 262 HIS 192 263 HIS 193 264 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17819 Hck32L 100.00 193 100.00 100.00 4.33e-141 PDB 1AD5 "Src Family Kinase Hck-Amp-Pnp Complex" 92.75 438 99.44 100.00 1.10e-126 PDB 1QCF "Crystal Structure Of Hck In Complex With A Src Family- Selective Tyrosine Kinase Inhibitor" 91.71 454 99.44 100.00 6.98e-125 PDB 2C0I "Src Family Kinase Hck With Bound Inhibitor A-420983" 91.71 454 99.44 100.00 6.98e-125 PDB 2C0O "Src Family Kinase Hck With Bound Inhibitor A-770041" 91.71 454 99.44 100.00 6.98e-125 PDB 2C0T "Src Family Kinase Hck With Bound Inhibitor A-641359" 91.71 454 99.44 100.00 6.98e-125 PDB 2HCK "Src Family Kinase Hck-Quercetin Complex" 92.75 438 99.44 100.00 1.10e-126 PDB 3HCK "Nmr Ensemble Of The Uncomplexed Human Hck Sh2 Domain, 20 Structures" 55.44 107 99.07 100.00 8.05e-72 PDB 3NHN "Crystal Structure Of The Src-Family Kinase Hck Sh3-Sh2-Linker Regulatory Region" 100.00 193 100.00 100.00 4.33e-141 PDB 3VRY "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 4-amino-5-(4-phenoxyphenyl)-7h-pyrrolo[2,3-d]pyrimidin-7" 91.71 454 99.44 100.00 6.98e-125 PDB 3VRZ "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 1-[4-(4-amino-7-cyclopentyl-7h-pyrrolo[2,3-d]pyrimidin-5" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS0 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor N-[4-(4-amino-7-cyclopentyl-7h-pyrrolo[2,3-d]pyrimidin-5" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS1 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 1-[4-(4-amino-7-cyclopentyl-7h-pyrrolo[2,3-d]pyrimidin-5" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS2 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 7-[cis-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phenox" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS3 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 7-[trans-4-(4-methylpiperazin-1-yl)cyclohexyl]-5-(4-phen" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS4 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 5-(4-phenoxyphenyl)-7-(tetrahydro-2h-pyran-4-yl)-7h-pyrr" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS5 "Crystal Structure Of Hck Complexed With A Pyrrolo-pyrimidine Inhibitor 7-(1-methylpiperidin-4-yl)-5-(4-phenoxyphenyl)-7h-pyrrol" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS6 "Crystal Structure Of Hck Complexed With A Pyrazolo-pyrimidine Inhibitor Tert-butyl {4-[4-amino-1-(propan-2-yl)-1h-pyrazolo[3,4-" 91.71 454 99.44 100.00 6.98e-125 PDB 3VS7 "Crystal Structure Of Hck Complexed With A Pyrazolo-pyrimidine Inhibitor 1-cyclopentyl-3-(1h-pyrrolo[2,3-b]pyridin-5-yl)-1h- Pyr" 91.71 454 99.44 100.00 6.98e-125 PDB 4LUD "Crystal Structure Of Hck In Complex With The Fluorescent Compound Skf86002" 91.71 454 99.44 100.00 6.98e-125 PDB 4LUE "Crystal Structure Of Hck In Complex With 7-[trans-4-(4- Methylpiperazin-1-yl)cyclohexyl]-5-(4-phenoxyphenyl)-7h-pyrrolo[2,3- D]" 91.71 454 99.44 100.00 6.98e-125 DBJ BAB15482 "unnamed protein product [Homo sapiens]" 96.37 505 98.92 99.46 1.45e-129 DBJ BAF82585 "unnamed protein product [Homo sapiens]" 96.37 504 97.85 99.46 1.35e-127 DBJ BAF83617 "unnamed protein product [Homo sapiens]" 96.37 506 99.46 100.00 2.33e-131 DBJ BAG60878 "unnamed protein product [Homo sapiens]" 96.37 505 99.46 100.00 2.49e-131 EMBL CAC44031 "hck protein [Macaca fascicularis]" 96.37 504 97.31 98.92 4.40e-126 GB AAA52643 "protein-tyrosine kinase [Homo sapiens]" 96.37 505 99.46 100.00 1.96e-131 GB AAA52644 "protein-tyrosine kinase [Homo sapiens]" 96.37 505 99.46 100.00 2.49e-131 GB AAH14435 "Hemopoietic cell kinase [Homo sapiens]" 96.37 526 99.46 100.00 7.66e-131 GB AAH94847 "Hemopoietic cell kinase [Homo sapiens]" 96.37 526 99.46 100.00 7.66e-131 GB AAI08931 "Hemopoietic cell kinase [Homo sapiens]" 96.37 526 99.46 100.00 7.66e-131 REF NP_001165600 "tyrosine-protein kinase HCK isoform b [Homo sapiens]" 96.37 505 99.46 100.00 2.49e-131 REF NP_001165601 "tyrosine-protein kinase HCK isoform c [Homo sapiens]" 96.37 525 98.92 99.46 2.00e-128 REF NP_001165602 "tyrosine-protein kinase HCK isoform d [Homo sapiens]" 96.37 504 98.92 99.46 9.68e-129 REF NP_001165603 "tyrosine-protein kinase HCK isoform e [Homo sapiens]" 96.37 506 99.46 100.00 2.33e-131 REF NP_001165604 "tyrosine-protein kinase HCK isoform b [Homo sapiens]" 96.37 505 99.46 100.00 2.49e-131 SP P08631 "RecName: Full=Tyrosine-protein kinase HCK; AltName: Full=Hematopoietic cell kinase; AltName: Full=Hemopoietic cell kinase; AltN" 96.37 526 99.46 100.00 7.66e-131 SP Q95M30 "RecName: Full=Tyrosine-protein kinase HCK; AltName: Full=Hematopoietic cell kinase; AltName: Full=Hemopoietic cell kinase; AltN" 96.37 504 97.31 98.92 4.40e-126 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hck32L 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 _Variant _Vector_name $Hck32L 'recombinant technology' . Escherichia coli BL21 Rosetta2(DE3) pET21 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 $Hck32L 0.3 mM '[U-13C; U-15N; U-2H]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' DTT 10 mM 'natural abundance' HEPES 10 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.02 w/v 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hck32L 0.6 mM '[U-13C; U-15N; U-2H]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' DTT 10 mM 'natural abundance' HEPES 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium azide' 0.02 w/v 'natural abundance' glutamate 50 mM 'natural abundance' arginine 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . http://www.nmr.ch stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details ; CARA is the application for the analysis of NMR spectra and computer aided resonance assignment developed at and used by the group of Prof. Dr. Kurt W thrich, Institute of Molecular Biology and Biophysics, ETH Z rich. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 8.0 . pH pressure 1 . atm temperature 300 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.2 . pH pressure 1 . atm temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 1.000000000 DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical 'separate tube (no insert) not similar to the experimental sample tube' parallel 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCA' '3D HNCO' '3D HN(CO)CA' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Hck32L _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 74 3 ARG H H 8.450 0.02 1 2 74 3 ARG C C 176.147 0.3 1 3 74 3 ARG CA C 55.630 0.3 1 4 74 3 ARG CB C 29.484 0.3 1 5 74 3 ARG N N 124.245 0.3 1 6 75 4 GLU H H 8.502 0.02 1 7 75 4 GLU C C 176.203 0.3 1 8 75 4 GLU CA C 55.685 0.3 1 9 75 4 GLU CB C 29.139 0.3 1 10 75 4 GLU N N 122.440 0.3 1 11 76 5 ALA H H 8.424 0.02 1 12 76 5 ALA C C 178.245 0.3 1 13 76 5 ALA CA C 52.296 0.3 1 14 76 5 ALA CB C 17.992 0.3 1 15 76 5 ALA N N 125.264 0.3 1 16 77 6 GLY H H 8.537 0.02 1 17 77 6 GLY CA C 44.602 0.3 1 18 77 6 GLY N N 108.738 0.3 1 19 78 7 SER H H 8.104 0.02 1 20 78 7 SER C C 174.451 0.3 1 21 78 7 SER CA C 57.656 0.3 1 22 78 7 SER CB C 62.914 0.3 1 23 78 7 SER N N 115.214 0.3 1 24 79 8 GLU H H 8.520 0.02 1 25 79 8 GLU C C 175.954 0.3 1 26 79 8 GLU CA C 55.477 0.3 1 27 79 8 GLU CB C 29.050 0.3 1 28 79 8 GLU N N 122.120 0.3 1 29 80 9 ASP H H 8.172 0.02 1 30 80 9 ASP C C 175.781 0.3 1 31 80 9 ASP CA C 54.011 0.3 1 32 80 9 ASP CB C 40.813 0.3 1 33 80 9 ASP N N 120.870 0.3 1 34 81 10 ILE H H 8.833 0.02 1 35 81 10 ILE C C 174.060 0.3 1 36 81 10 ILE CA C 60.333 0.3 1 37 81 10 ILE CB C 36.515 0.3 1 38 81 10 ILE N N 123.623 0.3 1 39 82 11 ILE H H 8.106 0.02 1 40 82 11 ILE C C 176.628 0.3 1 41 82 11 ILE CA C 58.408 0.3 1 42 82 11 ILE CB C 36.748 0.3 1 43 82 11 ILE N N 127.053 0.3 1 44 83 12 VAL H H 9.161 0.02 1 45 83 12 VAL C C 173.395 0.3 1 46 83 12 VAL CA C 57.129 0.3 1 47 83 12 VAL CB C 34.200 0.3 1 48 83 12 VAL N N 118.423 0.3 1 49 84 13 VAL H H 9.178 0.02 1 50 84 13 VAL C C 174.485 0.3 1 51 84 13 VAL CA C 57.292 0.3 1 52 84 13 VAL CB C 33.441 0.3 1 53 84 13 VAL N N 118.198 0.3 1 54 85 14 ALA H H 8.444 0.02 1 55 85 14 ALA C C 179.086 0.3 1 56 85 14 ALA CA C 51.600 0.3 1 57 85 14 ALA CB C 20.377 0.3 1 58 85 14 ALA N N 126.111 0.3 1 59 86 15 LEU H H 9.418 0.02 1 60 86 15 LEU C C 174.885 0.3 1 61 86 15 LEU CA C 54.852 0.3 1 62 86 15 LEU CB C 41.247 0.3 1 63 86 15 LEU N N 125.809 0.3 1 64 87 16 TYR H H 7.215 0.02 1 65 87 16 TYR C C 173.607 0.3 1 66 87 16 TYR CA C 53.408 0.3 1 67 87 16 TYR CB C 41.734 0.3 1 68 87 16 TYR N N 112.211 0.3 1 69 88 17 ASP H H 8.310 0.02 1 70 88 17 ASP C C 175.668 0.3 1 71 88 17 ASP CA C 53.799 0.3 1 72 88 17 ASP CB C 41.097 0.3 1 73 88 17 ASP N N 117.440 0.3 1 74 89 18 TYR H H 8.580 0.02 1 75 89 18 TYR C C 173.285 0.3 1 76 89 18 TYR CA C 57.633 0.3 1 77 89 18 TYR CB C 40.652 0.3 1 78 89 18 TYR N N 120.427 0.3 1 79 90 19 GLU H H 7.423 0.02 1 80 90 19 GLU C C 173.586 0.3 1 81 90 19 GLU CA C 53.178 0.3 1 82 90 19 GLU CB C 29.112 0.3 1 83 90 19 GLU N N 128.409 0.3 1 84 91 20 ALA H H 7.997 0.02 1 85 91 20 ALA C C 177.879 0.3 1 86 91 20 ALA CA C 52.431 0.3 1 87 91 20 ALA CB C 19.293 0.3 1 88 91 20 ALA N N 125.411 0.3 1 89 92 21 ILE H H 8.433 0.02 1 90 92 21 ILE C C 176.531 0.3 1 91 92 21 ILE CA C 61.050 0.3 1 92 92 21 ILE CB C 38.342 0.3 1 93 92 21 ILE N N 120.384 0.3 1 94 96 25 ASP H H 7.960 0.02 1 95 96 25 ASP C C 175.846 0.3 1 96 96 25 ASP CA C 53.678 0.3 1 97 96 25 ASP CB C 41.734 0.3 1 98 96 25 ASP N N 121.507 0.3 1 99 97 26 LEU H H 8.962 0.02 1 100 97 26 LEU C C 175.222 0.3 1 101 97 26 LEU CA C 53.321 0.3 1 102 97 26 LEU CB C 43.090 0.3 1 103 97 26 LEU N N 123.770 0.3 1 104 98 27 SER H H 7.772 0.02 1 105 98 27 SER C C 174.328 0.3 1 106 98 27 SER CA C 57.689 0.3 1 107 98 27 SER CB C 63.905 0.3 1 108 98 27 SER N N 116.240 0.3 1 109 99 28 PHE H H 8.787 0.02 1 110 99 28 PHE C C 173.611 0.3 1 111 99 28 PHE CA C 55.754 0.3 1 112 99 28 PHE CB C 39.380 0.3 1 113 99 28 PHE N N 116.814 0.3 1 114 100 29 GLN H H 9.045 0.02 1 115 100 29 GLN C C 175.177 0.3 1 116 100 29 GLN CA C 52.955 0.3 1 117 100 29 GLN CB C 31.542 0.3 1 118 100 29 GLN N N 119.882 0.3 1 119 101 30 LYS H H 9.183 0.02 1 120 101 30 LYS C C 177.121 0.3 1 121 101 30 LYS CA C 57.927 0.3 1 122 101 30 LYS CB C 31.381 0.3 1 123 101 30 LYS N N 121.905 0.3 1 124 102 31 GLY H H 8.935 0.02 1 125 102 31 GLY C C 174.486 0.3 1 126 102 31 GLY CA C 44.282 0.3 1 127 102 31 GLY N N 115.166 0.3 1 128 103 32 ASP H H 8.622 0.02 1 129 103 32 ASP C C 175.744 0.3 1 130 103 32 ASP CA C 55.074 0.3 1 131 103 32 ASP CB C 40.244 0.3 1 132 103 32 ASP N N 122.794 0.3 1 133 104 33 GLN H H 8.438 0.02 1 134 104 33 GLN C C 176.779 0.3 1 135 104 33 GLN CA C 54.133 0.3 1 136 104 33 GLN CB C 29.918 0.3 1 137 104 33 GLN N N 118.116 0.3 1 138 105 34 MET H H 9.163 0.02 1 139 105 34 MET C C 173.287 0.3 1 140 105 34 MET CA C 53.822 0.3 1 141 105 34 MET CB C 37.669 0.3 1 142 105 34 MET N N 120.885 0.3 1 143 106 35 VAL H H 8.896 0.02 1 144 106 35 VAL C C 175.900 0.3 1 145 106 35 VAL CA C 59.351 0.3 1 146 106 35 VAL CB C 32.736 0.3 1 147 106 35 VAL N N 119.727 0.3 1 148 107 36 VAL H H 8.774 0.02 1 149 107 36 VAL C C 175.004 0.3 1 150 107 36 VAL CA C 63.212 0.3 1 151 107 36 VAL CB C 31.002 0.3 1 152 107 36 VAL N N 126.448 0.3 1 153 108 37 LEU H H 9.174 0.02 1 154 108 37 LEU C C 177.445 0.3 1 155 108 37 LEU CA C 54.852 0.3 1 156 108 37 LEU CB C 41.192 0.3 1 157 108 37 LEU N N 128.098 0.3 1 158 109 38 GLU H H 7.611 0.02 1 159 109 38 GLU C C 174.264 0.3 1 160 109 38 GLU CA C 55.735 0.3 1 161 109 38 GLU CB C 32.194 0.3 1 162 109 38 GLU N N 117.043 0.3 1 163 110 39 GLU H H 8.640 0.02 1 164 110 39 GLU C C 175.383 0.3 1 165 110 39 GLU CA C 53.646 0.3 1 166 110 39 GLU CB C 28.230 0.3 1 167 110 39 GLU N N 126.316 0.3 1 168 111 40 SER H H 7.757 0.02 1 169 111 40 SER C C 174.656 0.3 1 170 111 40 SER CA C 56.457 0.3 1 171 111 40 SER CB C 62.455 0.3 1 172 111 40 SER N N 117.595 0.3 1 173 112 41 GLY H H 8.478 0.02 1 174 112 41 GLY C C 174.129 0.3 1 175 112 41 GLY CA C 45.435 0.3 1 176 112 41 GLY N N 111.645 0.3 1 177 113 42 GLU H H 8.877 0.02 1 178 113 42 GLU CA C 56.738 0.3 1 179 113 42 GLU CB C 29.209 0.3 1 180 113 42 GLU N N 122.527 0.3 1 181 114 43 TRP H H 7.947 0.02 1 182 114 43 TRP C C 175.328 0.3 1 183 114 43 TRP CA C 55.132 0.3 1 184 114 43 TRP CB C 29.267 0.3 1 185 114 43 TRP N N 120.159 0.3 1 186 115 44 TRP H H 9.069 0.02 1 187 115 44 TRP C C 175.835 0.3 1 188 115 44 TRP CA C 52.649 0.3 1 189 115 44 TRP CB C 30.405 0.3 1 190 115 44 TRP N N 124.176 0.3 1 191 116 45 LYS H H 8.804 0.02 1 192 116 45 LYS C C 175.275 0.3 1 193 116 45 LYS CA C 55.534 0.3 1 194 116 45 LYS CB C 32.790 0.3 1 195 116 45 LYS N N 122.984 0.3 1 196 117 46 ALA H H 9.394 0.02 1 197 117 46 ALA C C 173.737 0.3 1 198 117 46 ALA CA C 50.333 0.3 1 199 117 46 ALA CB C 23.630 0.3 1 200 117 46 ALA N N 130.361 0.3 1 201 118 47 ARG H H 8.845 0.02 1 202 118 47 ARG C C 176.244 0.3 1 203 118 47 ARG CA C 52.775 0.3 1 204 118 47 ARG CB C 32.949 0.3 1 205 118 47 ARG N N 117.395 0.3 1 206 119 48 SER H H 8.970 0.02 1 207 119 48 SER C C 177.319 0.3 1 208 119 48 SER CA C 57.592 0.3 1 209 119 48 SER CB C 62.495 0.3 1 210 119 48 SER N N 119.269 0.3 1 211 120 49 LEU H H 8.690 0.02 1 212 120 49 LEU C C 177.685 0.3 1 213 120 49 LEU CA C 56.619 0.3 1 214 120 49 LEU CB C 39.729 0.3 1 215 120 49 LEU N N 130.128 0.3 1 216 121 50 ALA H H 8.336 0.02 1 217 121 50 ALA C C 179.639 0.3 1 218 121 50 ALA CA C 54.028 0.3 1 219 121 50 ALA CB C 18.534 0.3 1 220 121 50 ALA N N 120.691 0.3 1 221 122 51 THR H H 7.924 0.02 1 222 122 51 THR CA C 60.506 0.3 1 223 122 51 THR CB C 70.726 0.3 1 224 122 51 THR N N 103.905 0.3 1 225 123 52 ARG H H 7.789 0.02 1 226 123 52 ARG C C 174.751 0.3 1 227 123 52 ARG CA C 57.718 0.3 1 228 123 52 ARG CB C 25.844 0.3 1 229 123 52 ARG N N 114.637 0.3 1 230 124 53 LYS H H 7.650 0.02 1 231 124 53 LYS C C 174.826 0.3 1 232 124 53 LYS CA C 56.023 0.3 1 233 124 53 LYS CB C 32.357 0.3 1 234 124 53 LYS N N 119.839 0.3 1 235 125 54 GLU H H 8.467 0.02 1 236 125 54 GLU C C 176.687 0.3 1 237 125 54 GLU CA C 53.334 0.3 1 238 125 54 GLU CB C 32.411 0.3 1 239 125 54 GLU N N 118.993 0.3 1 240 126 55 GLY H H 8.764 0.02 1 241 126 55 GLY C C 171.104 0.3 1 242 126 55 GLY CA C 44.824 0.3 1 243 126 55 GLY N N 107.633 0.3 1 244 127 56 TYR H H 8.950 0.02 1 245 127 56 TYR C C 176.513 0.3 1 246 127 56 TYR CA C 58.465 0.3 1 247 127 56 TYR CB C 39.163 0.3 1 248 127 56 TYR N N 119.347 0.3 1 249 128 57 ILE H H 9.599 0.02 1 250 128 57 ILE C C 172.263 0.3 1 251 128 57 ILE CA C 56.483 0.3 1 252 128 57 ILE CB C 39.458 0.3 1 253 128 57 ILE N N 112.567 0.3 1 254 130 59 SER H H 7.760 0.02 1 255 130 59 SER CA C 60.310 0.3 1 256 130 59 SER N N 121.463 0.3 1 257 131 60 ASN H H 8.154 0.02 1 258 131 60 ASN C C 175.436 0.3 1 259 131 60 ASN CA C 53.110 0.3 1 260 131 60 ASN CB C 35.562 0.3 1 261 131 60 ASN N N 115.280 0.3 1 262 132 61 TYR H H 7.865 0.02 1 263 132 61 TYR C C 174.929 0.3 1 264 132 61 TYR CA C 57.475 0.3 1 265 132 61 TYR CB C 38.209 0.3 1 266 132 61 TYR N N 118.975 0.3 1 267 133 62 VAL H H 7.135 0.02 1 268 133 62 VAL C C 173.467 0.3 1 269 133 62 VAL CA C 57.725 0.3 1 270 133 62 VAL CB C 34.742 0.3 1 271 133 62 VAL N N 108.669 0.3 1 272 134 63 ALA H H 8.414 0.02 1 273 134 63 ALA C C 176.457 0.3 1 274 134 63 ALA CA C 49.586 0.3 1 275 134 63 ALA CB C 22.329 0.3 1 276 134 63 ALA N N 119.874 0.3 1 277 135 64 ARG H H 8.869 0.02 1 278 135 64 ARG C C 177.416 0.3 1 279 135 64 ARG CA C 56.483 0.3 1 280 135 64 ARG CB C 29.213 0.3 1 281 135 64 ARG N N 120.444 0.3 1 282 136 65 VAL H H 8.142 0.02 1 283 136 65 VAL C C 175.452 0.3 1 284 136 65 VAL CA C 63.146 0.3 1 285 136 65 VAL CB C 31.056 0.3 1 286 136 65 VAL N N 121.899 0.3 1 287 137 66 ASP H H 8.585 0.02 1 288 137 66 ASP C C 175.749 0.3 1 289 137 66 ASP CA C 53.919 0.3 1 290 137 66 ASP CB C 39.404 0.3 1 291 137 66 ASP N N 120.669 0.3 1 292 138 67 SER H H 7.949 0.02 1 293 138 67 SER CA C 57.661 0.3 1 294 138 67 SER CB C 64.013 0.3 1 295 138 67 SER N N 114.924 0.3 1 296 139 68 LEU H H 8.492 0.02 1 297 139 68 LEU CA C 56.227 0.3 1 298 139 68 LEU CB C 39.939 0.3 1 299 139 68 LEU N N 124.526 0.3 1 300 140 69 GLU H H 8.169 0.02 1 301 140 69 GLU C C 176.905 0.3 1 302 140 69 GLU CA C 57.700 0.3 1 303 140 69 GLU CB C 28.562 0.3 1 304 140 69 GLU N N 113.570 0.3 1 305 141 70 THR H H 7.416 0.02 1 306 141 70 THR C C 175.139 0.3 1 307 141 70 THR CA C 61.310 0.3 1 308 141 70 THR CB C 68.458 0.3 1 309 141 70 THR N N 107.392 0.3 1 310 142 71 GLU H H 7.618 0.02 1 311 142 71 GLU C C 178.774 0.3 1 312 142 71 GLU CA C 54.619 0.3 1 313 142 71 GLU CB C 26.503 0.3 1 314 142 71 GLU N N 121.999 0.3 1 315 143 72 GLU H H 9.006 0.02 1 316 143 72 GLU C C 176.053 0.3 1 317 143 72 GLU CA C 57.700 0.3 1 318 143 72 GLU CB C 28.841 0.3 1 319 143 72 GLU N N 122.111 0.3 1 320 144 73 TRP H H 6.225 0.02 1 321 144 73 TRP C C 174.820 0.3 1 322 144 73 TRP CA C 52.660 0.3 1 323 144 73 TRP CB C 30.731 0.3 1 324 144 73 TRP N N 108.161 0.3 1 325 145 74 PHE H H 7.449 0.02 1 326 145 74 PHE C C 174.485 0.3 1 327 145 74 PHE CA C 57.201 0.3 1 328 145 74 PHE CB C 38.970 0.3 1 329 145 74 PHE N N 123.260 0.3 1 330 146 75 PHE H H 8.629 0.02 1 331 146 75 PHE C C 173.608 0.3 1 332 146 75 PHE CA C 55.505 0.3 1 333 146 75 PHE CB C 39.349 0.3 1 334 146 75 PHE N N 130.577 0.3 1 335 147 76 LYS H H 7.951 0.02 1 336 147 76 LYS C C 178.017 0.3 1 337 147 76 LYS CA C 55.362 0.3 1 338 147 76 LYS CB C 32.465 0.3 1 339 147 76 LYS N N 121.774 0.3 1 340 148 77 GLY H H 9.273 0.02 1 341 148 77 GLY C C 174.143 0.3 1 342 148 77 GLY CA C 46.223 0.3 1 343 148 77 GLY N N 113.544 0.3 1 344 149 78 ILE H H 7.246 0.02 1 345 149 78 ILE C C 174.917 0.3 1 346 149 78 ILE CA C 58.914 0.3 1 347 149 78 ILE CB C 38.536 0.3 1 348 149 78 ILE N N 117.432 0.3 1 349 150 79 SER H H 9.021 0.02 1 350 150 79 SER C C 174.280 0.3 1 351 150 79 SER CA C 56.511 0.3 1 352 150 79 SER CB C 64.902 0.3 1 353 150 79 SER N N 122.500 0.3 1 354 151 80 ARG H H 8.784 0.02 1 355 151 80 ARG C C 177.801 0.3 1 356 151 80 ARG CA C 59.677 0.3 1 357 151 80 ARG CB C 28.617 0.3 1 358 151 80 ARG N N 121.766 0.3 1 359 152 81 LYS H H 8.242 0.02 1 360 152 81 LYS C C 179.464 0.3 1 361 152 81 LYS CA C 58.402 0.3 1 362 152 81 LYS CB C 31.002 0.3 1 363 152 81 LYS N N 116.715 0.3 1 364 153 82 ASP H H 7.846 0.02 1 365 153 82 ASP C C 178.052 0.3 1 366 153 82 ASP CA C 56.749 0.3 1 367 153 82 ASP CB C 39.349 0.3 1 368 153 82 ASP N N 120.263 0.3 1 369 154 83 ALA H H 8.523 0.02 1 370 154 83 ALA C C 179.391 0.3 1 371 154 83 ALA CA C 54.565 0.3 1 372 154 83 ALA CB C 17.871 0.3 1 373 154 83 ALA N N 123.437 0.3 1 374 155 84 GLU H H 7.797 0.02 1 375 155 84 GLU C C 177.136 0.3 1 376 155 84 GLU CA C 59.057 0.3 1 377 155 84 GLU CB C 27.587 0.3 1 378 155 84 GLU N N 114.571 0.3 1 379 156 85 ARG H H 7.690 0.02 1 380 156 85 ARG C C 179.529 0.3 1 381 156 85 ARG CA C 58.781 0.3 1 382 156 85 ARG CB C 28.942 0.3 1 383 156 85 ARG N N 116.639 0.3 1 384 157 86 GLN H H 8.319 0.02 1 385 157 86 GLN C C 179.024 0.3 1 386 157 86 GLN CA C 58.592 0.3 1 387 157 86 GLN CB C 27.424 0.3 1 388 157 86 GLN N N 116.491 0.3 1 389 158 87 LEU H H 8.078 0.02 1 390 158 87 LEU C C 178.527 0.3 1 391 158 87 LEU CA C 56.673 0.3 1 392 158 87 LEU CB C 42.277 0.3 1 393 158 87 LEU N N 118.777 0.3 1 394 159 88 LEU H H 7.752 0.02 1 395 159 88 LEU C C 176.019 0.3 1 396 159 88 LEU CA C 54.805 0.3 1 397 159 88 LEU CB C 39.709 0.3 1 398 159 88 LEU N N 116.623 0.3 1 399 160 89 ALA H H 7.013 0.02 1 400 160 89 ALA C C 175.360 0.3 1 401 160 89 ALA CA C 50.678 0.3 1 402 160 89 ALA CB C 16.204 0.3 1 403 160 89 ALA N N 124.189 0.3 1 404 162 91 GLY H H 8.328 0.02 1 405 162 91 GLY CA C 44.207 0.3 1 406 162 91 GLY N N 108.997 0.3 1 407 163 92 ASN H H 7.098 0.02 1 408 163 92 ASN C C 172.680 0.3 1 409 163 92 ASN CA C 52.657 0.3 1 410 163 92 ASN CB C 40.325 0.3 1 411 163 92 ASN N N 116.014 0.3 1 412 164 93 MET H H 9.062 0.02 1 413 164 93 MET C C 175.079 0.3 1 414 164 93 MET CA C 53.781 0.3 1 415 164 93 MET CB C 35.013 0.3 1 416 164 93 MET N N 116.798 0.3 1 417 165 94 LEU H H 8.336 0.02 1 418 165 94 LEU C C 179.635 0.3 1 419 165 94 LEU CA C 56.511 0.3 1 420 165 94 LEU CB C 40.379 0.3 1 421 165 94 LEU N N 121.170 0.3 1 422 166 95 GLY H H 8.954 0.02 1 423 166 95 GLY C C 174.729 0.3 1 424 166 95 GLY CA C 45.678 0.3 1 425 166 95 GLY N N 115.062 0.3 1 426 167 96 SER H H 8.567 0.02 1 427 167 96 SER C C 175.182 0.3 1 428 167 96 SER CA C 60.706 0.3 1 429 167 96 SER CB C 62.648 0.3 1 430 167 96 SER N N 120.211 0.3 1 431 168 97 PHE H H 7.613 0.02 1 432 168 97 PHE C C 173.706 0.3 1 433 168 97 PHE CA C 55.516 0.3 1 434 168 97 PHE CB C 43.144 0.3 1 435 168 97 PHE N N 114.572 0.3 1 436 169 98 MET H H 8.784 0.02 1 437 169 98 MET C C 174.064 0.3 1 438 169 98 MET CA C 54.378 0.3 1 439 169 98 MET CB C 37.181 0.3 1 440 169 98 MET N N 113.689 0.3 1 441 170 99 ILE H H 9.490 0.02 1 442 170 99 ILE C C 172.984 0.3 1 443 170 99 ILE CA C 59.730 0.3 1 444 170 99 ILE CB C 37.110 0.3 1 445 170 99 ILE N N 121.688 0.3 1 446 171 100 ARG H H 8.983 0.02 1 447 171 100 ARG C C 175.420 0.3 1 448 171 100 ARG CA C 52.250 0.3 1 449 171 100 ARG CB C 32.726 0.3 1 450 171 100 ARG N N 122.163 0.3 1 451 172 101 ASP H H 8.659 0.02 1 452 172 101 ASP C C 175.922 0.3 1 453 172 101 ASP CA C 53.606 0.3 1 454 172 101 ASP CB C 40.867 0.3 1 455 172 101 ASP N N 120.444 0.3 1 456 173 102 SER H H 8.106 0.02 1 457 173 102 SER C C 175.560 0.3 1 458 173 102 SER CA C 57.213 0.3 1 459 173 102 SER CB C 62.821 0.3 1 460 173 102 SER N N 114.824 0.3 1 461 174 103 GLU H H 8.138 0.02 1 462 174 103 GLU C C 174.459 0.3 1 463 174 103 GLU CA C 53.381 0.3 1 464 174 103 GLU CB C 32.352 0.3 1 465 174 103 GLU N N 121.951 0.3 1 466 178 107 GLY H H 9.132 0.02 1 467 178 107 GLY CA C 44.730 0.3 1 468 178 107 GLY N N 113.306 0.3 1 469 179 108 SER H H 7.636 0.02 1 470 179 108 SER C C 173.404 0.3 1 471 179 108 SER CA C 56.294 0.3 1 472 179 108 SER CB C 63.688 0.3 1 473 179 108 SER N N 114.197 0.3 1 474 180 109 TYR H H 8.840 0.02 1 475 180 109 TYR C C 175.179 0.3 1 476 180 109 TYR CA C 57.129 0.3 1 477 180 109 TYR CB C 41.734 0.3 1 478 180 109 TYR N N 121.662 0.3 1 479 181 110 SER H H 9.219 0.02 1 480 181 110 SER C C 171.659 0.3 1 481 181 110 SER CA C 57.292 0.3 1 482 181 110 SER CB C 65.104 0.3 1 483 181 110 SER N N 115.408 0.3 1 484 182 111 LEU H H 9.457 0.02 1 485 182 111 LEU C C 175.222 0.3 1 486 182 111 LEU CA C 52.734 0.3 1 487 182 111 LEU CB C 43.686 0.3 1 488 182 111 LEU N N 127.113 0.3 1 489 183 112 SER H H 9.219 0.02 1 490 183 112 SER C C 172.649 0.3 1 491 183 112 SER CA C 57.804 0.3 1 492 183 112 SER CB C 64.239 0.3 1 493 183 112 SER N N 124.245 0.3 1 494 184 113 VAL H H 9.050 0.02 1 495 184 113 VAL C C 174.120 0.3 1 496 184 113 VAL CA C 59.582 0.3 1 497 184 113 VAL CB C 35.663 0.3 1 498 184 113 VAL N N 122.489 0.3 1 499 185 114 ARG H H 9.015 0.02 1 500 185 114 ARG C C 173.179 0.3 1 501 185 114 ARG CA C 56.403 0.3 1 502 185 114 ARG CB C 29.863 0.3 1 503 185 114 ARG N N 127.407 0.3 1 504 186 115 ASP H H 9.235 0.02 1 505 186 115 ASP C C 175.409 0.3 1 506 186 115 ASP CA C 51.383 0.3 1 507 186 115 ASP CB C 45.258 0.3 1 508 186 115 ASP N N 129.886 0.3 1 509 187 116 TYR H H 8.605 0.02 1 510 187 116 TYR C C 173.049 0.3 1 511 187 116 TYR CA C 58.132 0.3 1 512 187 116 TYR CB C 40.921 0.3 1 513 187 116 TYR N N 122.612 0.3 1 514 188 117 ASP H H 7.586 0.02 1 515 188 117 ASP C C 173.524 0.3 1 516 188 117 ASP CA C 49.918 0.3 1 517 188 117 ASP CB C 43.757 0.3 1 518 188 117 ASP N N 128.072 0.3 1 519 190 119 ARG H H 8.204 0.02 1 520 190 119 ARG C C 177.373 0.3 1 521 190 119 ARG CA C 56.697 0.3 1 522 190 119 ARG CB C 29.484 0.3 1 523 190 119 ARG N N 115.714 0.3 1 524 191 120 GLN H H 8.383 0.02 1 525 191 120 GLN C C 175.916 0.3 1 526 191 120 GLN CA C 55.538 0.3 1 527 191 120 GLN CB C 30.026 0.3 1 528 191 120 GLN N N 116.271 0.3 1 529 192 121 GLY H H 8.483 0.02 1 530 192 121 GLY C C 173.629 0.3 1 531 192 121 GLY CA C 43.837 0.3 1 532 192 121 GLY N N 109.625 0.3 1 533 193 122 ASP H H 8.351 0.02 1 534 193 122 ASP C C 175.511 0.3 1 535 193 122 ASP CA C 55.108 0.3 1 536 193 122 ASP CB C 40.908 0.3 1 537 193 122 ASP N N 123.347 0.3 1 538 194 123 THR H H 8.166 0.02 1 539 194 123 THR C C 172.010 0.3 1 540 194 123 THR CA C 59.270 0.3 1 541 194 123 THR CB C 71.006 0.3 1 542 194 123 THR N N 114.983 0.3 1 543 195 124 VAL H H 8.237 0.02 1 544 195 124 VAL C C 174.291 0.3 1 545 195 124 VAL CA C 60.056 0.3 1 546 195 124 VAL CB C 34.037 0.3 1 547 195 124 VAL N N 120.150 0.3 1 548 196 125 LYS H H 8.651 0.02 1 549 196 125 LYS CA C 52.820 0.3 1 550 196 125 LYS CB C 34.300 0.3 1 551 196 125 LYS N N 126.298 0.3 1 552 197 126 HIS H H 8.166 0.02 1 553 197 126 HIS C C 175.189 0.3 1 554 197 126 HIS CA C 53.465 0.3 1 555 197 126 HIS CB C 32.736 0.3 1 556 197 126 HIS N N 118.630 0.3 1 557 198 127 TYR H H 9.822 0.02 1 558 198 127 TYR CA C 56.023 0.3 1 559 198 127 TYR CB C 40.217 0.3 1 560 198 127 TYR N N 121.377 0.3 1 561 199 128 LYS H H 8.975 0.02 1 562 199 128 LYS CA C 56.126 0.3 1 563 199 128 LYS CB C 31.549 0.3 1 564 199 128 LYS N N 125.178 0.3 1 565 200 129 ILE H H 8.520 0.02 1 566 200 129 ILE C C 175.813 0.3 1 567 200 129 ILE CA C 60.333 0.3 1 568 200 129 ILE CB C 36.353 0.3 1 569 200 129 ILE N N 126.284 0.3 1 570 201 130 ARG H H 8.828 0.02 1 571 201 130 ARG C C 174.918 0.3 1 572 201 130 ARG CA C 54.025 0.3 1 573 201 130 ARG CB C 30.297 0.3 1 574 201 130 ARG N N 129.489 0.3 1 575 202 131 THR H H 8.025 0.02 1 576 202 131 THR C C 175.878 0.3 1 577 202 131 THR CA C 58.911 0.3 1 578 202 131 THR CB C 70.464 0.3 1 579 202 131 THR N N 109.243 0.3 1 580 203 132 LEU H H 8.178 0.02 1 581 203 132 LEU C C 178.869 0.3 1 582 203 132 LEU CA C 53.034 0.3 1 583 203 132 LEU CB C 42.114 0.3 1 584 203 132 LEU N N 124.072 0.3 1 585 206 135 GLY H H 7.707 0.02 1 586 206 135 GLY C C 173.455 0.3 1 587 206 135 GLY CA C 44.228 0.3 1 588 206 135 GLY N N 108.222 0.3 1 589 207 136 GLY H H 7.802 0.02 1 590 207 136 GLY C C 172.304 0.3 1 591 207 136 GLY CA C 43.919 0.3 1 592 207 136 GLY N N 109.435 0.3 1 593 208 137 PHE H H 9.168 0.02 1 594 208 137 PHE C C 176.095 0.3 1 595 208 137 PHE CA C 56.457 0.3 1 596 208 137 PHE CB C 43.144 0.3 1 597 208 137 PHE N N 117.300 0.3 1 598 209 138 TYR H H 8.968 0.02 1 599 209 138 TYR C C 172.280 0.3 1 600 209 138 TYR CA C 57.617 0.3 1 601 209 138 TYR CB C 39.650 0.3 1 602 209 138 TYR N N 114.849 0.3 1 603 210 139 ILE H H 9.790 0.02 1 604 210 139 ILE C C 176.915 0.3 1 605 210 139 ILE CA C 62.803 0.3 1 606 210 139 ILE CB C 38.699 0.3 1 607 210 139 ILE N N 119.692 0.3 1 608 211 140 SER H H 9.164 0.02 1 609 211 140 SER CA C 53.647 0.3 1 610 211 140 SER CB C 64.338 0.3 1 611 211 140 SER N N 116.816 0.3 1 612 213 142 ARG H H 7.506 0.02 1 613 213 142 ARG C C 176.356 0.3 1 614 213 142 ARG CA C 56.712 0.3 1 615 213 142 ARG CB C 29.267 0.3 1 616 213 142 ARG N N 114.233 0.3 1 617 214 143 SER H H 7.691 0.02 1 618 214 143 SER C C 170.885 0.3 1 619 214 143 SER CA C 56.200 0.3 1 620 214 143 SER CB C 63.742 0.3 1 621 214 143 SER N N 116.342 0.3 1 622 215 144 THR H H 7.653 0.02 1 623 215 144 THR C C 173.196 0.3 1 624 215 144 THR CA C 58.863 0.3 1 625 215 144 THR CB C 69.867 0.3 1 626 215 144 THR N N 113.988 0.3 1 627 216 145 PHE H H 9.028 0.02 1 628 216 145 PHE C C 176.170 0.3 1 629 216 145 PHE CA C 56.099 0.3 1 630 216 145 PHE CB C 43.252 0.3 1 631 216 145 PHE N N 118.440 0.3 1 632 217 146 SER H H 9.463 0.02 1 633 217 146 SER C C 174.308 0.3 1 634 217 146 SER CA C 60.726 0.3 1 635 217 146 SER CB C 62.766 0.3 1 636 217 146 SER N N 117.826 0.3 1 637 218 147 THR H H 7.476 0.02 1 638 218 147 THR C C 174.664 0.3 1 639 218 147 THR CA C 58.494 0.3 1 640 218 147 THR CB C 72.620 0.3 1 641 218 147 THR N N 106.436 0.3 1 642 219 148 LEU H H 8.986 0.02 1 643 219 148 LEU C C 178.466 0.3 1 644 219 148 LEU CA C 56.207 0.3 1 645 219 148 LEU CB C 40.298 0.3 1 646 219 148 LEU N N 121.740 0.3 1 647 220 149 GLN H H 8.856 0.02 1 648 220 149 GLN C C 176.272 0.3 1 649 220 149 GLN CA C 59.471 0.3 1 650 220 149 GLN CB C 26.232 0.3 1 651 220 149 GLN N N 118.051 0.3 1 652 221 150 GLU H H 7.774 0.02 1 653 221 150 GLU C C 178.190 0.3 1 654 221 150 GLU CA C 58.348 0.3 1 655 221 150 GLU CB C 30.080 0.3 1 656 221 150 GLU N N 118.258 0.3 1 657 222 151 LEU H H 6.910 0.02 1 658 222 151 LEU C C 177.239 0.3 1 659 222 151 LEU CA C 58.240 0.3 1 660 222 151 LEU CB C 40.260 0.3 1 661 222 151 LEU N N 123.018 0.3 1 662 223 152 VAL H H 7.853 0.02 1 663 223 152 VAL C C 176.948 0.3 1 664 223 152 VAL CA C 66.196 0.3 1 665 223 152 VAL CB C 30.134 0.3 1 666 223 152 VAL N N 119.701 0.3 1 667 224 153 ASP H H 7.819 0.02 1 668 224 153 ASP C C 178.698 0.3 1 669 224 153 ASP CA C 56.929 0.3 1 670 224 153 ASP CB C 39.891 0.3 1 671 224 153 ASP N N 116.383 0.3 1 672 225 154 HIS H H 7.657 0.02 1 673 225 154 HIS C C 178.752 0.3 1 674 225 154 HIS CA C 59.738 0.3 1 675 225 154 HIS CB C 30.724 0.3 1 676 225 154 HIS N N 118.414 0.3 1 677 226 155 TYR H H 7.523 0.02 1 678 226 155 TYR C C 176.915 0.3 1 679 226 155 TYR CA C 60.418 0.3 1 680 226 155 TYR CB C 36.260 0.3 1 681 226 155 TYR N N 116.629 0.3 1 682 227 156 LYS H H 7.661 0.02 1 683 227 156 LYS C C 178.309 0.3 1 684 227 156 LYS CA C 57.237 0.3 1 685 227 156 LYS CB C 32.357 0.3 1 686 227 156 LYS N N 118.734 0.3 1 687 228 157 LYS H H 7.355 0.02 1 688 228 157 LYS C C 177.604 0.3 1 689 228 157 LYS CA C 57.029 0.3 1 690 228 157 LYS CB C 31.307 0.3 1 691 228 157 LYS N N 117.308 0.3 1 692 229 158 GLY H H 7.098 0.02 1 693 229 158 GLY C C 171.168 0.3 1 694 229 158 GLY CA C 44.355 0.3 1 695 229 158 GLY N N 105.414 0.3 1 696 231 160 ASP H H 8.579 0.02 1 697 231 160 ASP CA C 54.025 0.3 1 698 231 160 ASP CB C 39.946 0.3 1 699 231 160 ASP N N 118.106 0.3 1 700 232 161 GLY H H 8.013 0.02 1 701 232 161 GLY C C 175.317 0.3 1 702 232 161 GLY CA C 44.622 0.3 1 703 232 161 GLY N N 105.414 0.3 1 704 233 162 LEU H H 8.326 0.02 1 705 233 162 LEU C C 177.869 0.3 1 706 233 162 LEU CA C 53.551 0.3 1 707 233 162 LEU CB C 40.921 0.3 1 708 233 162 LEU N N 119.779 0.3 1 709 234 163 CYS H H 7.697 0.02 1 710 234 163 CYS C C 173.608 0.3 1 711 234 163 CYS CA C 57.572 0.3 1 712 234 163 CYS CB C 27.641 0.3 1 713 234 163 CYS N N 115.642 0.3 1 714 235 164 GLN H H 6.927 0.02 1 715 235 164 GLN C C 173.927 0.3 1 716 235 164 GLN CA C 52.660 0.3 1 717 235 164 GLN CB C 31.869 0.3 1 718 235 164 GLN N N 117.191 0.3 1 719 236 165 LYS H H 7.951 0.02 1 720 236 165 LYS C C 176.315 0.3 1 721 236 165 LYS CA C 55.634 0.3 1 722 236 165 LYS CB C 31.436 0.3 1 723 236 165 LYS N N 118.952 0.3 1 724 237 166 LEU H H 7.722 0.02 1 725 237 166 LEU C C 176.674 0.3 1 726 237 166 LEU CA C 54.241 0.3 1 727 237 166 LEU CB C 38.265 0.3 1 728 237 166 LEU N N 124.323 0.3 1 729 238 167 SER H H 8.451 0.02 1 730 238 167 SER C C 174.641 0.3 1 731 238 167 SER CA C 55.991 0.3 1 732 238 167 SER CB C 63.525 0.3 1 733 238 167 SER N N 116.506 0.3 1 734 239 168 VAL H H 8.121 0.02 1 735 239 168 VAL C C 172.554 0.3 1 736 239 168 VAL CA C 57.237 0.3 1 737 239 168 VAL CB C 33.007 0.3 1 738 239 168 VAL N N 117.349 0.3 1 739 241 170 CYS H H 8.564 0.02 1 740 241 170 CYS C C 172.403 0.3 1 741 241 170 CYS CA C 59.189 0.3 1 742 241 170 CYS CB C 26.990 0.3 1 743 241 170 CYS N N 123.355 0.3 1 744 242 171 MET H H 8.651 0.02 1 745 242 171 MET C C 176.591 0.3 1 746 242 171 MET CA C 56.153 0.3 1 747 242 171 MET CB C 31.868 0.3 1 748 242 171 MET N N 128.150 0.3 1 749 243 172 SER H H 8.570 0.02 1 750 243 172 SER CA C 57.405 0.3 1 751 243 172 SER CB C 63.659 0.3 1 752 243 172 SER N N 118.165 0.3 1 753 245 174 LYS H H 8.296 0.02 1 754 245 174 LYS C C 174.286 0.3 1 755 245 174 LYS CA C 53.764 0.3 1 756 245 174 LYS CB C 30.996 0.3 1 757 245 174 LYS N N 123.813 0.3 1 758 247 176 GLN H H 8.408 0.02 1 759 247 176 GLN C C 175.798 0.3 1 760 247 176 GLN CA C 55.177 0.3 1 761 247 176 GLN CB C 28.583 0.3 1 762 247 176 GLN N N 120.360 0.3 1 763 248 177 LYS H H 8.287 0.02 1 764 248 177 LYS C C 174.615 0.3 1 765 248 177 LYS CA C 53.106 0.3 1 766 248 177 LYS CB C 30.460 0.3 1 767 248 177 LYS N N 122.465 0.3 1 768 250 179 TRP H H 7.490 0.02 1 769 250 179 TRP C C 176.265 0.3 1 770 250 179 TRP CA C 56.749 0.3 1 771 250 179 TRP CB C 27.912 0.3 1 772 250 179 TRP N N 117.477 0.3 1 773 251 180 GLU H H 7.845 0.02 1 774 251 180 GLU C C 176.114 0.3 1 775 251 180 GLU CA C 55.862 0.3 1 776 251 180 GLU CB C 29.376 0.3 1 777 251 180 GLU N N 122.353 0.3 1 778 252 181 LYS H H 7.934 0.02 1 779 252 181 LYS C C 176.362 0.3 1 780 252 181 LYS CA C 56.153 0.3 1 781 252 181 LYS CB C 31.815 0.3 1 782 252 181 LYS N N 121.196 0.3 1 783 253 182 ASP H H 8.336 0.02 1 784 253 182 ASP C C 176.383 0.3 1 785 253 182 ASP CA C 54.202 0.3 1 786 253 182 ASP CB C 40.217 0.3 1 787 253 182 ASP N N 120.462 0.3 1 788 254 183 ALA H H 8.069 0.02 1 789 254 183 ALA C C 178.029 0.3 1 790 254 183 ALA CA C 52.620 0.3 1 791 254 183 ALA CB C 17.667 0.3 1 792 254 183 ALA N N 123.018 0.3 1 793 255 184 TRP H H 7.948 0.02 1 794 255 184 TRP C C 176.790 0.3 1 795 255 184 TRP CA C 57.454 0.3 1 796 255 184 TRP CB C 28.291 0.3 1 797 255 184 TRP N N 118.778 0.3 1 798 256 185 GLU H H 8.078 0.02 1 799 256 185 GLU C C 176.631 0.3 1 800 256 185 GLU CA C 56.511 0.3 1 801 256 185 GLU CB C 28.942 0.3 1 802 256 185 GLU N N 120.833 0.3 1 803 257 186 LEU H H 7.874 0.02 1 804 257 186 LEU C C 177.604 0.3 1 805 257 186 LEU CA C 54.944 0.3 1 806 257 186 LEU CB C 40.976 0.3 1 807 257 186 LEU N N 121.109 0.3 1 808 258 187 GLU H H 8.113 0.02 1 809 258 187 GLU C C 176.330 0.3 1 810 258 187 GLU CA C 56.424 0.3 1 811 258 187 GLU CB C 29.105 0.3 1 812 258 187 GLU N N 119.857 0.3 1 813 259 188 HIS H H 8.034 0.02 1 814 259 188 HIS C C 175.231 0.3 1 815 259 188 HIS CA C 56.019 0.3 1 816 259 188 HIS CB C 29.831 0.3 1 817 259 188 HIS N N 119.113 0.3 1 818 264 193 HIS H H 7.792 0.02 1 819 264 193 HIS C C 179.788 0.3 1 820 264 193 HIS CA C 56.943 0.3 1 821 264 193 HIS CB C 30.297 0.3 1 822 264 193 HIS N N 125.619 0.3 1 stop_ save_