data_18307 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human APOBEC2 chemical shifts ; _BMRB_accession_number 18307 _BMRB_flat_file_name bmr18307.str _Entry_type original _Submission_date 2012-03-01 _Accession_date 2012-03-01 _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 Krzysiak Troy C. . 2 Jung Jinwon . . 3 Thompson James . . 4 Baker David . . 5 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" 198 "13C chemical shifts" 387 "15N chemical shifts" 198 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-03-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 18306 'A2POBEC2 41-224' stop_ _Original_release_date 2012-03-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'APOBEC2 is a Monomer in Solution: Implications for APOBEC3G Models' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22339232 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krzysiak Troy C. . 2 Jung Jinwon . . 3 Thompson James . . 4 Baker David . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 51 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2008 _Page_last 2017 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'A2POBEC2 1-224' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'A2POBEC2 1-224' $APOBEC2_1-224 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_APOBEC2_1-224 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common APOBEC2_1-224 _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 227 _Mol_residue_sequence ; SEFMAQKEEAAVATEAASQN GEDLENLDDPEKLKELIELP PFEIVTGERLPANFFKFQFR NVEYSSGRNKTFLCYVVEAQ GKGGQVQASRGYLEDEHAAA HAEEAFFNTILPAFDPALRY NVTWYVSSSPCAACADRIIK TLSKTKNLRLLILVGRLFMW EEPEIQAALKKLKEAGCKLR IMKPQDFEYVWQNFVEQEEG ESKAFQPWEDIQENFLYYEE KLADILK ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLU 3 PHE 4 MET 5 ALA 6 GLN 7 LYS 8 GLU 9 GLU 10 ALA 11 ALA 12 VAL 13 ALA 14 THR 15 GLU 16 ALA 17 ALA 18 SER 19 GLN 20 ASN 21 GLY 22 GLU 23 ASP 24 LEU 25 GLU 26 ASN 27 LEU 28 ASP 29 ASP 30 PRO 31 GLU 32 LYS 33 LEU 34 LYS 35 GLU 36 LEU 37 ILE 38 GLU 39 LEU 40 PRO 41 PRO 42 PHE 43 GLU 44 ILE 45 VAL 46 THR 47 GLY 48 GLU 49 ARG 50 LEU 51 PRO 52 ALA 53 ASN 54 PHE 55 PHE 56 LYS 57 PHE 58 GLN 59 PHE 60 ARG 61 ASN 62 VAL 63 GLU 64 TYR 65 SER 66 SER 67 GLY 68 ARG 69 ASN 70 LYS 71 THR 72 PHE 73 LEU 74 CYS 75 TYR 76 VAL 77 VAL 78 GLU 79 ALA 80 GLN 81 GLY 82 LYS 83 GLY 84 GLY 85 GLN 86 VAL 87 GLN 88 ALA 89 SER 90 ARG 91 GLY 92 TYR 93 LEU 94 GLU 95 ASP 96 GLU 97 HIS 98 ALA 99 ALA 100 ALA 101 HIS 102 ALA 103 GLU 104 GLU 105 ALA 106 PHE 107 PHE 108 ASN 109 THR 110 ILE 111 LEU 112 PRO 113 ALA 114 PHE 115 ASP 116 PRO 117 ALA 118 LEU 119 ARG 120 TYR 121 ASN 122 VAL 123 THR 124 TRP 125 TYR 126 VAL 127 SER 128 SER 129 SER 130 PRO 131 CYS 132 ALA 133 ALA 134 CYS 135 ALA 136 ASP 137 ARG 138 ILE 139 ILE 140 LYS 141 THR 142 LEU 143 SER 144 LYS 145 THR 146 LYS 147 ASN 148 LEU 149 ARG 150 LEU 151 LEU 152 ILE 153 LEU 154 VAL 155 GLY 156 ARG 157 LEU 158 PHE 159 MET 160 TRP 161 GLU 162 GLU 163 PRO 164 GLU 165 ILE 166 GLN 167 ALA 168 ALA 169 LEU 170 LYS 171 LYS 172 LEU 173 LYS 174 GLU 175 ALA 176 GLY 177 CYS 178 LYS 179 LEU 180 ARG 181 ILE 182 MET 183 LYS 184 PRO 185 GLN 186 ASP 187 PHE 188 GLU 189 TYR 190 VAL 191 TRP 192 GLN 193 ASN 194 PHE 195 VAL 196 GLU 197 GLN 198 GLU 199 GLU 200 GLY 201 GLU 202 SER 203 LYS 204 ALA 205 PHE 206 GLN 207 PRO 208 TRP 209 GLU 210 ASP 211 ILE 212 GLN 213 GLU 214 ASN 215 PHE 216 LEU 217 TYR 218 TYR 219 GLU 220 GLU 221 LYS 222 LEU 223 ALA 224 ASP 225 ILE 226 LEU 227 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 18306 APOBEC2_41-224 81.06 187 100.00 100.00 2.14e-132 PDB 2NYT "The Apobec2 Crystal Structure And Functional Implications For Aid" 81.06 190 100.00 100.00 1.83e-132 DBJ BAD97181 "apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 variant [Homo sapiens]" 98.68 224 99.55 99.55 2.12e-161 DBJ BAG36096 "unnamed protein product [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 EMBL CAH90732 "hypothetical protein [Pongo abelii]" 98.68 224 98.66 98.66 4.52e-159 GB AAD45360 "APOBEC-2 protein [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 GB AAH47767 "Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 GB AAH69688 "Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 GB AAH69764 "Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2 [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 GB AAT44388 "Apobec2 [Pongo pygmaeus]" 98.68 224 98.66 98.66 4.52e-159 REF NP_001125408 "probable C->U-editing enzyme APOBEC-2 [Pongo abelii]" 98.68 224 98.66 98.66 4.52e-159 REF NP_006780 "C->U-editing enzyme APOBEC-2 [Homo sapiens]" 98.68 224 100.00 100.00 5.12e-162 REF XP_001117195 "PREDICTED: probable C->U-editing enzyme APOBEC-2 [Macaca mulatta]" 98.68 224 98.21 98.66 1.07e-159 REF XP_003266357 "PREDICTED: probable C->U-editing enzyme APOBEC-2 [Nomascus leucogenys]" 98.68 224 99.55 99.55 2.05e-161 REF XP_003897628 "PREDICTED: probable C->U-editing enzyme APOBEC-2 [Papio anubis]" 98.68 224 98.21 98.66 1.07e-159 SP Q694B4 "RecName: Full=Probable C->U-editing enzyme APOBEC-2; AltName: Full=mRNA(cytosine(6666)) deaminase 2" 98.68 224 98.66 98.66 4.52e-159 SP Q9Y235 "RecName: Full=C->U-editing enzyme APOBEC-2; AltName: Full=mRNA(cytosine(6666)) deaminase 2" 98.68 224 100.00 100.00 5.12e-162 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $APOBEC2_1-224 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $APOBEC2_1-224 'recombinant technology' . Escherichia coli . 'pET41a modified' 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 HEPES 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 5 mM 'natural abundance' $APOBEC2_1-224 1 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _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' 50 . mM pH 7.0 . pH pressure 1 . atm temperature 310 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HN(COCA)CB' 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 'A2POBEC2 1-224' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 5 ALA H H 8.126 0.020 1 2 2 5 ALA CA C 52.109 0.3 1 3 2 5 ALA CB C 18.111 0.3 1 4 2 5 ALA N N 125.152 0.3 1 5 3 6 GLN H H 8.254 0.020 1 6 3 6 GLN CA C 55.380 0.3 1 7 3 6 GLN CB C 28.439 0.3 1 8 3 6 GLN N N 119.415 0.3 1 9 4 7 LYS H H 8.262 0.020 1 10 4 7 LYS CA C 55.937 0.3 1 11 4 7 LYS CB C 32.028 0.3 1 12 4 7 LYS N N 122.608 0.3 1 13 5 8 GLU H H 8.430 0.020 1 14 5 8 GLU CA C 56.164 0.3 1 15 5 8 GLU CB C 29.203 0.3 1 16 5 8 GLU N N 122.298 0.3 1 17 6 9 GLU H H 8.389 0.020 1 18 6 9 GLU CA C 56.157 0.3 1 19 6 9 GLU CB C 29.230 0.3 1 20 6 9 GLU N N 122.147 0.3 1 21 7 10 ALA H H 8.227 0.020 1 22 7 10 ALA CA C 51.996 0.3 1 23 7 10 ALA CB C 18.183 0.3 1 24 7 10 ALA N N 124.748 0.3 1 25 8 11 ALA H H 8.146 0.020 1 26 8 11 ALA CA C 52.002 0.3 1 27 8 11 ALA CB C 18.255 0.3 1 28 8 11 ALA N N 123.157 0.3 1 29 9 12 VAL H H 7.960 0.020 1 30 9 12 VAL CA C 61.582 0.3 1 31 9 12 VAL CB C 31.813 0.3 1 32 9 12 VAL N N 118.931 0.3 1 33 10 13 ALA H H 8.301 0.020 1 34 10 13 ALA CA C 52.089 0.3 1 35 10 13 ALA CB C 18.183 0.3 1 36 10 13 ALA N N 127.400 0.3 1 37 11 14 THR H H 8.050 0.020 1 38 11 14 THR CA C 61.582 0.3 1 39 11 14 THR CB C 69.186 0.3 1 40 11 14 THR N N 113.515 0.3 1 41 12 15 GLU H H 8.349 0.020 1 42 12 15 GLU CA C 56.171 0.3 1 43 12 15 GLU CB C 29.203 0.3 1 44 12 15 GLU N N 122.904 0.3 1 45 14 17 ALA H H 8.170 0.020 1 46 14 17 ALA CA C 52.140 0.3 1 47 14 17 ALA CB C 18.227 0.3 1 48 14 17 ALA N N 122.924 0.3 1 49 15 18 SER H H 8.168 0.020 1 50 15 18 SER CA C 57.924 0.3 1 51 15 18 SER CB C 63.591 0.3 1 52 15 18 SER N N 114.609 0.3 1 53 16 19 GLN H H 8.351 0.020 1 54 16 19 GLN CA C 55.483 0.3 1 55 16 19 GLN CB C 28.441 0.3 1 56 16 19 GLN N N 121.698 0.3 1 57 17 20 ASN H H 8.442 0.020 1 58 17 20 ASN CA C 53.033 0.3 1 59 17 20 ASN CB C 38.484 0.3 1 60 17 20 ASN N N 119.479 0.3 1 61 18 21 GLY H H 8.334 0.020 1 62 18 21 GLY CA C 45.088 0.3 1 63 18 21 GLY N N 109.235 0.3 1 64 20 23 ASP H H 8.364 0.020 1 65 20 23 ASP CA C 53.953 0.3 1 66 20 23 ASP CB C 40.081 0.3 1 67 20 23 ASP N N 120.770 0.3 1 68 21 24 LEU H H 8.074 0.020 1 69 21 24 LEU CA C 54.936 0.3 1 70 21 24 LEU CB C 41.098 0.3 1 71 21 24 LEU N N 122.121 0.3 1 72 22 25 GLU H H 8.260 0.020 1 73 22 25 GLU CA C 56.379 0.3 1 74 22 25 GLU CB C 29.205 0.3 1 75 22 25 GLU N N 120.231 0.3 1 76 23 26 ASN H H 8.286 0.020 1 77 23 26 ASN CA C 52.875 0.3 1 78 23 26 ASN CB C 38.197 0.3 1 79 23 26 ASN N N 118.937 0.3 1 80 24 27 LEU H H 8.127 0.020 1 81 24 27 LEU CA C 54.847 0.3 1 82 24 27 LEU CB C 41.106 0.3 1 83 24 27 LEU N N 122.506 0.3 1 84 25 28 ASP H H 8.196 0.020 1 85 25 28 ASP CA C 53.860 0.3 1 86 25 28 ASP CB C 40.636 0.3 1 87 25 28 ASP N N 120.322 0.3 1 88 26 29 ASP H H 7.967 0.020 1 89 26 29 ASP CA C 51.539 0.3 1 90 26 29 ASP CB C 40.923 0.3 1 91 26 29 ASP N N 120.913 0.3 1 92 28 31 GLU H H 8.381 0.020 1 93 28 31 GLU CA C 56.921 0.3 1 94 28 31 GLU CB C 28.441 0.3 1 95 28 31 GLU N N 117.925 0.3 1 96 29 32 LYS H H 7.740 0.020 1 97 29 32 LYS CA C 56.456 0.3 1 98 29 32 LYS CB C 31.382 0.3 1 99 29 32 LYS N N 119.614 0.3 1 100 30 33 LEU H H 7.871 0.020 1 101 30 33 LEU CA C 55.270 0.3 1 102 30 33 LEU CB C 40.708 0.3 1 103 30 33 LEU N N 120.881 0.3 1 104 31 34 LYS H H 7.934 0.020 1 105 31 34 LYS CA C 56.481 0.3 1 106 31 34 LYS CB C 31.797 0.3 1 107 31 34 LYS N N 120.536 0.3 1 108 32 35 GLU H H 8.073 0.020 1 109 32 35 GLU CA C 56.273 0.3 1 110 32 35 GLU CB C 29.208 0.3 1 111 32 35 GLU N N 120.173 0.3 1 112 33 36 LEU H H 8.015 0.020 1 113 33 36 LEU CA C 54.845 0.3 1 114 33 36 LEU CB C 41.106 0.3 1 115 33 36 LEU N N 122.248 0.3 1 116 34 37 ILE H H 7.911 0.020 1 117 34 37 ILE CA C 60.552 0.3 1 118 34 37 ILE CB C 37.766 0.3 1 119 34 37 ILE N N 121.025 0.3 1 120 35 38 GLU H H 8.244 0.020 1 121 35 38 GLU CA C 55.556 0.3 1 122 35 38 GLU CB C 29.445 0.3 1 123 35 38 GLU N N 124.462 0.3 1 124 36 39 LEU H H 8.171 0.020 1 125 36 39 LEU CA C 52.328 0.3 1 126 36 39 LEU CB C 40.636 0.3 1 127 36 39 LEU N N 125.034 0.3 1 128 39 42 PHE H H 8.004 0.020 1 129 39 42 PHE CA C 57.148 0.3 1 130 39 42 PHE CB C 39.129 0.3 1 131 39 42 PHE N N 119.968 0.3 1 132 40 43 GLU H H 8.083 0.020 1 133 40 43 GLU CA C 55.413 0.3 1 134 40 43 GLU CB C 29.947 0.3 1 135 40 43 GLU N N 123.050 0.3 1 136 41 44 ILE H H 8.098 0.020 1 137 41 44 ILE CA C 60.225 0.3 1 138 41 44 ILE CB C 38.053 0.3 1 139 41 44 ILE N N 122.393 0.3 1 140 42 45 VAL H H 8.319 0.020 1 141 42 45 VAL CA C 61.797 0.3 1 142 42 45 VAL CB C 32.068 0.3 1 143 42 45 VAL N N 127.097 0.3 1 144 43 46 THR H H 8.286 0.020 1 145 43 46 THR CA C 60.662 0.3 1 146 43 46 THR CB C 69.585 0.3 1 147 43 46 THR N N 118.979 0.3 1 148 44 47 GLY H H 8.232 0.020 1 149 44 47 GLY CA C 44.536 0.3 1 150 44 47 GLY N N 111.355 0.3 1 151 45 48 GLU H H 8.456 0.020 1 152 45 48 GLU CA C 57.064 0.3 1 153 45 48 GLU CB C 29.876 0.3 1 154 45 48 GLU N N 120.708 0.3 1 155 46 49 ARG H H 8.261 0.020 1 156 46 49 ARG CA C 54.845 0.3 1 157 46 49 ARG CB C 32.055 0.3 1 158 46 49 ARG N N 118.715 0.3 1 159 47 50 LEU H H 8.523 0.020 1 160 47 50 LEU CA C 52.048 0.3 1 161 47 50 LEU CB C 41.497 0.3 1 162 47 50 LEU N N 123.160 0.3 1 163 49 52 ALA H H 8.529 0.020 1 164 49 52 ALA CA C 55.341 0.3 1 165 49 52 ALA CB C 18.040 0.3 1 166 49 52 ALA N N 126.593 0.3 1 167 50 53 ASN H H 9.185 0.020 1 168 50 53 ASN CA C 55.772 0.3 1 169 50 53 ASN CB C 36.403 0.3 1 170 50 53 ASN N N 114.625 0.3 1 171 51 54 PHE H H 7.269 0.020 1 172 51 54 PHE CA C 57.813 0.3 1 173 51 54 PHE CB C 36.701 0.3 1 174 51 54 PHE N N 118.139 0.3 1 175 52 55 PHE H H 7.878 0.020 1 176 52 55 PHE CA C 61.471 0.3 1 177 52 55 PHE CB C 38.556 0.3 1 178 52 55 PHE N N 119.655 0.3 1 179 53 56 LYS H H 8.512 0.020 1 180 53 56 LYS CA C 59.358 0.3 1 181 53 56 LYS CB C 31.669 0.3 1 182 53 56 LYS N N 115.964 0.3 1 183 54 57 PHE H H 7.494 0.020 1 184 54 57 PHE CA C 58.928 0.3 1 185 54 57 PHE CB C 39.488 0.3 1 186 54 57 PHE N N 113.434 0.3 1 187 55 58 GLN H H 8.246 0.020 1 188 55 58 GLN CA C 56.848 0.3 1 189 55 58 GLN CB C 27.724 0.3 1 190 55 58 GLN N N 114.798 0.3 1 191 56 59 PHE H H 8.052 0.020 1 192 56 59 PHE CA C 58.282 0.3 1 193 56 59 PHE CB C 38.699 0.3 1 194 56 59 PHE N N 117.000 0.3 1 195 58 61 ASN H H 7.061 0.020 1 196 58 61 ASN CA C 60.377 0.3 1 197 58 61 ASN CB C 32.458 0.3 1 198 58 61 ASN N N 113.512 0.3 1 199 59 62 VAL H H 8.531 0.020 1 200 59 62 VAL CA C 56.760 0.3 1 201 59 62 VAL CB C 28.871 0.3 1 202 59 62 VAL N N 122.994 0.3 1 203 60 63 GLU H H 7.935 0.020 1 204 60 63 GLU CA C 56.516 0.3 1 205 60 63 GLU CB C 30.521 0.3 1 206 60 63 GLU N N 120.523 0.3 1 207 62 65 SER H H 6.886 0.020 1 208 62 65 SER CA C 56.130 0.3 1 209 62 65 SER CB C 65.097 0.3 1 210 62 65 SER N N 111.049 0.3 1 211 63 66 SER H H 7.530 0.020 1 212 63 66 SER CA C 57.995 0.3 1 213 63 66 SER CB C 61.582 0.3 1 214 63 66 SER N N 115.659 0.3 1 215 65 68 ARG H H 8.266 0.020 1 216 65 68 ARG CA C 56.280 0.3 1 217 65 68 ARG CB C 29.206 0.3 1 218 65 68 ARG N N 120.255 0.3 1 219 66 69 ASN H H 8.261 0.020 1 220 66 69 ASN CA C 57.482 0.3 1 221 66 69 ASN CB C 38.627 0.3 1 222 66 69 ASN N N 120.729 0.3 1 223 67 70 LYS H H 8.110 0.020 1 224 67 70 LYS CA C 55.544 0.3 1 225 67 70 LYS CB C 32.099 0.3 1 226 67 70 LYS N N 122.468 0.3 1 227 69 72 PHE H H 7.922 0.020 1 228 69 72 PHE CA C 56.704 0.3 1 229 69 72 PHE CB C 42.070 0.3 1 230 69 72 PHE N N 122.633 0.3 1 231 70 73 LEU H H 9.116 0.020 1 232 70 73 LEU CA C 54.122 0.3 1 233 70 73 LEU CB C 45.729 0.3 1 234 70 73 LEU N N 126.976 0.3 1 235 71 74 CYS H H 9.429 0.020 1 236 71 74 CYS CA C 57.479 0.3 1 237 71 74 CYS CB C 26.935 0.3 1 238 71 74 CYS N N 125.472 0.3 1 239 72 75 TYR H H 8.997 0.020 1 240 72 75 TYR CA C 54.629 0.3 1 241 72 75 TYR CB C 42.396 0.3 1 242 72 75 TYR N N 120.907 0.3 1 243 73 76 VAL H H 9.333 0.020 1 244 73 76 VAL CA C 61.805 0.3 1 245 73 76 VAL CB C 34.323 0.3 1 246 73 76 VAL N N 118.330 0.3 1 247 74 77 VAL H H 9.671 0.020 1 248 74 77 VAL CA C 61.529 0.3 1 249 74 77 VAL CB C 33.104 0.3 1 250 74 77 VAL N N 126.855 0.3 1 251 75 78 GLU H H 8.776 0.020 1 252 75 78 GLU CA C 54.767 0.3 1 253 75 78 GLU CB C 31.167 0.3 1 254 75 78 GLU N N 126.199 0.3 1 255 76 79 ALA H H 8.934 0.020 1 256 76 79 ALA CA C 49.746 0.3 1 257 76 79 ALA CB C 20.192 0.3 1 258 76 79 ALA N N 128.192 0.3 1 259 77 80 GLN H H 8.908 0.020 1 260 77 80 GLN CA C 54.404 0.3 1 261 77 80 GLN CB C 30.808 0.3 1 262 77 80 GLN N N 122.667 0.3 1 263 78 81 GLY H H 8.656 0.020 1 264 78 81 GLY CA C 43.767 0.3 1 265 78 81 GLY N N 112.975 0.3 1 266 79 82 LYS H H 8.682 0.020 1 267 79 82 LYS CA C 57.520 0.3 1 268 79 82 LYS CB C 31.167 0.3 1 269 79 82 LYS N N 121.944 0.3 1 270 81 84 GLY H H 8.023 0.020 1 271 81 84 GLY CA C 44.541 0.3 1 272 81 84 GLY N N 107.075 0.3 1 273 82 85 GLN H H 7.900 0.020 1 274 82 85 GLN CA C 55.772 0.3 1 275 82 85 GLN CB C 28.082 0.3 1 276 82 85 GLN N N 120.305 0.3 1 277 83 86 VAL H H 8.468 0.020 1 278 83 86 VAL CA C 61.080 0.3 1 279 83 86 VAL CB C 33.247 0.3 1 280 83 86 VAL N N 123.603 0.3 1 281 84 87 GLN H H 8.569 0.020 1 282 84 87 GLN CA C 54.409 0.3 1 283 84 87 GLN CB C 30.163 0.3 1 284 84 87 GLN N N 125.194 0.3 1 285 85 88 ALA H H 8.898 0.020 1 286 85 88 ALA CA C 50.320 0.3 1 287 85 88 ALA CB C 21.339 0.3 1 288 85 88 ALA N N 128.429 0.3 1 289 86 89 SER H H 9.098 0.020 1 290 86 89 SER CA C 56.991 0.3 1 291 86 89 SER CB C 65.743 0.3 1 292 86 89 SER N N 116.123 0.3 1 293 87 90 ARG H H 8.580 0.020 1 294 87 90 ARG CA C 54.122 0.3 1 295 87 90 ARG CB C 33.319 0.3 1 296 87 90 ARG N N 119.898 0.3 1 297 88 91 GLY H H 7.344 0.020 1 298 88 91 GLY CA C 45.084 0.3 1 299 88 91 GLY N N 108.109 0.3 1 300 89 92 TYR H H 8.757 0.020 1 301 89 92 TYR CA C 55.286 0.3 1 302 89 92 TYR CB C 42.924 0.3 1 303 89 92 TYR N N 117.659 0.3 1 304 90 93 LEU H H 9.424 0.020 1 305 90 93 LEU CA C 53.316 0.3 1 306 90 93 LEU CB C 46.303 0.3 1 307 90 93 LEU N N 122.017 0.3 1 308 91 94 GLU H H 8.318 0.020 1 309 91 94 GLU CA C 53.199 0.3 1 310 91 94 GLU CB C 32.530 0.3 1 311 91 94 GLU N N 118.479 0.3 1 312 92 95 ASP H H 7.427 0.020 1 313 92 95 ASP CA C 54.193 0.3 1 314 92 95 ASP CB C 41.640 0.3 1 315 92 95 ASP N N 120.659 0.3 1 316 96 99 ALA H H 8.384 0.020 1 317 96 99 ALA CA C 50.954 0.3 1 318 96 99 ALA CB C 18.255 0.3 1 319 96 99 ALA N N 121.466 0.3 1 320 97 100 ALA H H 7.546 0.020 1 321 97 100 ALA CA C 51.667 0.3 1 322 97 100 ALA CB C 18.064 0.3 1 323 97 100 ALA N N 123.600 0.3 1 324 98 101 HIS H H 8.767 0.020 1 325 98 101 HIS CA C 53.690 0.3 1 326 98 101 HIS CB C 31.813 0.3 1 327 98 101 HIS N N 121.195 0.3 1 328 100 103 GLU H H 11.759 0.020 1 329 100 103 GLU CA C 60.233 0.3 1 330 100 103 GLU CB C 26.372 0.3 1 331 100 103 GLU N N 117.810 0.3 1 332 101 104 GLU H H 6.655 0.020 1 333 101 104 GLU CA C 59.358 0.3 1 334 101 104 GLU CB C 28.728 0.3 1 335 101 104 GLU N N 114.217 0.3 1 336 102 105 ALA H H 8.210 0.020 1 337 102 105 ALA CA C 54.517 0.3 1 338 102 105 ALA CB C 17.179 0.3 1 339 102 105 ALA N N 121.648 0.3 1 340 103 106 PHE H H 8.503 0.020 1 341 103 106 PHE CA C 62.303 0.3 1 342 103 106 PHE CB C 37.695 0.3 1 343 103 106 PHE N N 120.089 0.3 1 344 104 107 PHE H H 7.071 0.020 1 345 104 107 PHE CA C 60.255 0.3 1 346 104 107 PHE CB C 38.197 0.3 1 347 104 107 PHE N N 116.562 0.3 1 348 105 108 ASN H H 8.156 0.020 1 349 105 108 ASN CA C 54.085 0.3 1 350 105 108 ASN CB C 38.269 0.3 1 351 105 108 ASN N N 115.041 0.3 1 352 106 109 THR H H 7.987 0.020 1 353 106 109 THR CA C 62.802 0.3 1 354 106 109 THR CB C 70.477 0.3 1 355 106 109 THR N N 108.763 0.3 1 356 107 110 ILE H H 7.091 0.020 1 357 107 110 ILE CA C 60.147 0.3 1 358 107 110 ILE CB C 32.960 0.3 1 359 107 110 ILE N N 122.201 0.3 1 360 108 111 LEU H H 6.736 0.020 1 361 108 111 LEU CA C 51.611 0.3 1 362 108 111 LEU CB C 41.712 0.3 1 363 108 111 LEU N N 117.687 0.3 1 364 110 113 ALA H H 6.849 0.020 1 365 110 113 ALA CA C 50.392 0.3 1 366 110 113 ALA CB C 20.192 0.3 1 367 110 113 ALA N N 118.889 0.3 1 368 111 114 PHE H H 8.336 0.020 1 369 111 114 PHE CA C 55.987 0.3 1 370 111 114 PHE CB C 39.345 0.3 1 371 111 114 PHE N N 118.246 0.3 1 372 112 115 ASP H H 8.954 0.020 1 373 112 115 ASP CA C 51.252 0.3 1 374 112 115 ASP CB C 41.640 0.3 1 375 112 115 ASP N N 128.253 0.3 1 376 114 117 ALA H H 8.870 0.020 1 377 114 117 ALA CA C 52.087 0.3 1 378 114 117 ALA CB C 18.398 0.3 1 379 114 117 ALA N N 119.824 0.3 1 380 115 118 LEU H H 7.722 0.020 1 381 115 118 LEU CA C 52.980 0.3 1 382 115 118 LEU CB C 42.674 0.3 1 383 115 118 LEU N N 118.569 0.3 1 384 116 119 ARG H H 8.292 0.020 1 385 116 119 ARG CA C 54.845 0.3 1 386 116 119 ARG CB C 30.306 0.3 1 387 116 119 ARG N N 118.954 0.3 1 388 117 120 TYR H H 8.897 0.020 1 389 117 120 TYR CA C 57.485 0.3 1 390 117 120 TYR CB C 40.576 0.3 1 391 117 120 TYR N N 121.682 0.3 1 392 118 121 ASN H H 9.350 0.020 1 393 118 121 ASN CA C 52.400 0.3 1 394 118 121 ASN CB C 39.488 0.3 1 395 118 121 ASN N N 124.405 0.3 1 396 119 122 VAL H H 9.147 0.020 1 397 119 122 VAL CA C 60.711 0.3 1 398 119 122 VAL CB C 32.960 0.3 1 399 119 122 VAL N N 127.461 0.3 1 400 120 123 THR H H 9.274 0.020 1 401 120 123 THR CA C 61.380 0.3 1 402 120 123 THR CB C 70.362 0.3 1 403 120 123 THR N N 125.434 0.3 1 404 121 124 TRP H H 9.284 0.020 1 405 121 124 TRP CA C 52.211 0.3 1 406 121 124 TRP CB C 33.175 0.3 1 407 121 124 TRP N N 125.673 0.3 1 408 122 125 TYR H H 9.528 0.020 1 409 122 125 TYR CA C 56.593 0.3 1 410 122 125 TYR CB C 37.838 0.3 1 411 122 125 TYR N N 121.243 0.3 1 412 123 126 VAL H H 9.351 0.020 1 413 123 126 VAL CA C 57.695 0.3 1 414 123 126 VAL CB C 34.383 0.3 1 415 123 126 VAL N N 118.801 0.3 1 416 124 127 SER H H 8.640 0.020 1 417 124 127 SER CA C 61.197 0.3 1 418 124 127 SER N N 119.441 0.3 1 419 128 131 CYS H H 8.275 0.020 1 420 128 131 CYS CA C 57.067 0.3 1 421 128 131 CYS CB C 28.467 0.3 1 422 128 131 CYS N N 117.281 0.3 1 423 129 132 ALA H H 8.594 0.020 1 424 129 132 ALA CA C 55.399 0.3 1 425 129 132 ALA CB C 16.820 0.3 1 426 129 132 ALA N N 120.499 0.3 1 427 130 133 ALA H H 8.224 0.020 1 428 130 133 ALA CA C 54.962 0.3 1 429 130 133 ALA CB C 17.681 0.3 1 430 130 133 ALA N N 123.189 0.3 1 431 131 134 CYS H H 8.973 0.020 1 432 131 134 CYS CA C 65.491 0.3 1 433 131 134 CYS CB C 28.943 0.3 1 434 131 134 CYS N N 123.819 0.3 1 435 132 135 ALA H H 8.732 0.020 1 436 132 135 ALA CA C 55.483 0.3 1 437 132 135 ALA CB C 16.964 0.3 1 438 132 135 ALA N N 120.647 0.3 1 439 133 136 ASP H H 7.789 0.020 1 440 133 136 ASP CA C 57.582 0.3 1 441 133 136 ASP CB C 40.923 0.3 1 442 133 136 ASP N N 116.438 0.3 1 443 134 137 ARG H H 7.556 0.020 1 444 134 137 ARG CA C 58.011 0.3 1 445 134 137 ARG CB C 27.652 0.3 1 446 134 137 ARG N N 118.809 0.3 1 447 135 138 ILE H H 8.538 0.020 1 448 135 138 ILE CA C 65.817 0.3 1 449 135 138 ILE CB C 37.336 0.3 1 450 135 138 ILE N N 122.202 0.3 1 451 136 139 ILE H H 8.724 0.020 1 452 136 139 ILE CA C 66.061 0.3 1 453 136 139 ILE CB C 37.264 0.3 1 454 136 139 ILE N N 120.496 0.3 1 455 137 140 LYS H H 8.339 0.020 1 456 137 140 LYS CA C 59.343 0.3 1 457 137 140 LYS CB C 31.167 0.3 1 458 137 140 LYS N N 120.141 0.3 1 459 138 141 THR H H 7.691 0.020 1 460 138 141 THR CA C 67.023 0.3 1 461 138 141 THR CB C 67.680 0.3 1 462 138 141 THR N N 116.385 0.3 1 463 139 142 LEU H H 8.690 0.020 1 464 139 142 LEU CA C 57.589 0.3 1 465 139 142 LEU CB C 39.990 0.3 1 466 139 142 LEU N N 122.447 0.3 1 467 140 143 SER H H 8.116 0.020 1 468 140 143 SER CA C 60.793 0.3 1 469 140 143 SER CB C 62.945 0.3 1 470 140 143 SER N N 111.706 0.3 1 471 141 144 LYS H H 7.075 0.020 1 472 141 144 LYS CA C 55.630 0.3 1 473 141 144 LYS CB C 32.817 0.3 1 474 141 144 LYS N N 116.621 0.3 1 475 142 145 THR H H 7.473 0.020 1 476 142 145 THR CA C 60.434 0.3 1 477 142 145 THR CB C 67.608 0.3 1 478 142 145 THR N N 118.148 0.3 1 479 143 146 LYS H H 8.538 0.020 1 480 143 146 LYS CA C 56.942 0.3 1 481 143 146 LYS CB C 30.665 0.3 1 482 143 146 LYS N N 123.142 0.3 1 483 144 147 ASN H H 9.060 0.020 1 484 144 147 ASN CA C 52.325 0.3 1 485 144 147 ASN CB C 35.184 0.3 1 486 144 147 ASN N N 114.606 0.3 1 487 145 148 LEU H H 7.233 0.020 1 488 145 148 LEU CA C 53.902 0.3 1 489 145 148 LEU CB C 43.146 0.3 1 490 145 148 LEU N N 121.257 0.3 1 491 146 149 ARG H H 8.549 0.020 1 492 146 149 ARG CA C 54.115 0.3 1 493 146 149 ARG CB C 30.880 0.3 1 494 146 149 ARG N N 126.599 0.3 1 495 147 150 LEU H H 8.917 0.020 1 496 147 150 LEU CA C 53.046 0.3 1 497 147 150 LEU CB C 45.585 0.3 1 498 147 150 LEU N N 126.492 0.3 1 499 148 151 LEU H H 8.337 0.020 1 500 148 151 LEU CA C 53.234 0.3 1 501 148 151 LEU CB C 43.362 0.3 1 502 148 151 LEU N N 130.772 0.3 1 503 149 152 ILE H H 8.925 0.020 1 504 149 152 ILE CA C 60.666 0.3 1 505 149 152 ILE CB C 38.555 0.3 1 506 149 152 ILE N N 124.583 0.3 1 507 150 153 LEU H H 9.161 0.020 1 508 150 153 LEU CA C 53.021 0.3 1 509 150 153 LEU CB C 40.994 0.3 1 510 150 153 LEU N N 128.483 0.3 1 511 151 154 VAL H H 8.739 0.020 1 512 151 154 VAL CA C 58.279 0.3 1 513 151 154 VAL CB C 33.247 0.3 1 514 151 154 VAL N N 116.786 0.3 1 515 152 155 GLY H H 9.253 0.020 1 516 152 155 GLY CA C 48.156 0.3 1 517 152 155 GLY N N 115.230 0.3 1 518 153 156 ARG H H 6.854 0.020 1 519 153 156 ARG CA C 53.642 0.3 1 520 153 156 ARG CB C 32.602 0.3 1 521 153 156 ARG N N 112.102 0.3 1 522 155 158 PHE H H 8.383 0.020 1 523 155 158 PHE CA C 56.274 0.3 1 524 155 158 PHE CB C 40.349 0.3 1 525 155 158 PHE N N 125.735 0.3 1 526 156 159 MET H H 8.741 0.020 1 527 156 159 MET CA C 56.152 0.3 1 528 156 159 MET CB C 29.230 0.3 1 529 156 159 MET N N 122.719 0.3 1 530 157 160 TRP H H 6.536 0.020 1 531 157 160 TRP CA C 58.282 0.3 1 532 157 160 TRP CB C 28.584 0.3 1 533 157 160 TRP N N 112.228 0.3 1 534 158 161 GLU H H 8.020 0.020 1 535 158 161 GLU CA C 56.776 0.3 1 536 158 161 GLU CB C 28.082 0.3 1 537 158 161 GLU N N 117.889 0.3 1 538 159 162 GLU H H 7.743 0.020 1 539 159 162 GLU CA C 52.974 0.3 1 540 159 162 GLU CB C 28.233 0.3 1 541 159 162 GLU N N 121.085 0.3 1 542 161 164 GLU H H 9.427 0.020 1 543 161 164 GLU CA C 59.117 0.3 1 544 161 164 GLU CB C 28.226 0.3 1 545 161 164 GLU N N 116.809 0.3 1 546 162 165 ILE H H 7.203 0.020 1 547 162 165 ILE CA C 60.988 0.3 1 548 162 165 ILE CB C 34.323 0.3 1 549 162 165 ILE N N 121.428 0.3 1 550 163 166 GLN H H 7.979 0.020 1 551 163 166 GLN CA C 59.890 0.3 1 552 163 166 GLN CB C 25.930 0.3 1 553 163 166 GLN N N 119.012 0.3 1 554 164 167 ALA H H 8.153 0.020 1 555 164 167 ALA CA C 54.405 0.3 1 556 164 167 ALA CB C 17.294 0.3 1 557 164 167 ALA N N 117.802 0.3 1 558 165 168 ALA H H 7.587 0.020 1 559 165 168 ALA CA C 54.738 0.3 1 560 165 168 ALA CB C 17.027 0.3 1 561 165 168 ALA N N 121.121 0.3 1 562 166 169 LEU H H 8.487 0.020 1 563 166 169 LEU CA C 57.793 0.3 1 564 166 169 LEU CB C 39.990 0.3 1 565 166 169 LEU N N 116.725 0.3 1 566 167 170 LYS H H 7.739 0.020 1 567 167 170 LYS CA C 59.789 0.3 1 568 167 170 LYS CB C 31.382 0.3 1 569 167 170 LYS N N 118.058 0.3 1 570 168 171 LYS H H 8.254 0.020 1 571 168 171 LYS CA C 59.100 0.3 1 572 168 171 LYS CB C 31.597 0.3 1 573 168 171 LYS N N 119.763 0.3 1 574 169 172 LEU H H 8.414 0.020 1 575 169 172 LEU CA C 58.036 0.3 1 576 169 172 LEU CB C 40.564 0.3 1 577 169 172 LEU N N 122.303 0.3 1 578 170 173 LYS H H 7.593 0.020 1 579 170 173 LYS CA C 58.693 0.3 1 580 170 173 LYS CB C 31.007 0.3 1 581 170 173 LYS N N 120.455 0.3 1 582 171 174 GLU H H 8.416 0.020 1 583 171 174 GLU CA C 58.577 0.3 1 584 171 174 GLU CB C 28.418 0.3 1 585 171 174 GLU N N 121.427 0.3 1 586 172 175 ALA H H 7.768 0.020 1 587 172 175 ALA CA C 51.885 0.3 1 588 172 175 ALA CB C 18.398 0.3 1 589 172 175 ALA N N 119.337 0.3 1 590 173 176 GLY H H 7.837 0.020 1 591 173 176 GLY CA C 44.316 0.3 1 592 173 176 GLY N N 104.243 0.3 1 593 174 177 CYS H H 7.911 0.020 1 594 174 177 CYS CA C 58.918 0.3 1 595 174 177 CYS CB C 27.365 0.3 1 596 174 177 CYS N N 122.344 0.3 1 597 175 178 LYS H H 8.193 0.020 1 598 175 178 LYS CA C 55.198 0.3 1 599 175 178 LYS CB C 32.386 0.3 1 600 175 178 LYS N N 129.489 0.3 1 601 176 179 LEU H H 8.067 0.020 1 602 176 179 LEU CA C 53.659 0.3 1 603 176 179 LEU CB C 44.581 0.3 1 604 176 179 LEU N N 125.708 0.3 1 605 177 180 ARG H H 8.743 0.020 1 606 177 180 ARG CA C 54.206 0.3 1 607 177 180 ARG CB C 33.462 0.3 1 608 177 180 ARG N N 120.556 0.3 1 609 178 181 ILE H H 8.746 0.020 1 610 178 181 ILE CA C 57.481 0.3 1 611 178 181 ILE CB C 34.644 0.3 1 612 178 181 ILE N N 120.916 0.3 1 613 179 182 MET H H 8.798 0.020 1 614 179 182 MET CA C 57.482 0.3 1 615 179 182 MET CB C 34.377 0.3 1 616 179 182 MET N N 125.191 0.3 1 617 180 183 LYS H H 9.480 0.020 1 618 180 183 LYS CA C 53.620 0.3 1 619 180 183 LYS CB C 30.736 0.3 1 620 180 183 LYS N N 123.515 0.3 1 621 182 185 GLN H H 8.747 0.020 1 622 182 185 GLN CA C 58.498 0.3 1 623 182 185 GLN CB C 27.293 0.3 1 624 182 185 GLN N N 113.569 0.3 1 625 183 186 ASP H H 8.053 0.020 1 626 183 186 ASP CA C 57.033 0.3 1 627 183 186 ASP CB C 40.349 0.3 1 628 183 186 ASP N N 120.268 0.3 1 629 184 187 PHE H H 7.586 0.020 1 630 184 187 PHE CA C 62.730 0.3 1 631 184 187 PHE CB C 38.484 0.3 1 632 184 187 PHE N N 117.831 0.3 1 633 185 188 GLU H H 7.485 0.020 1 634 185 188 GLU CA C 58.928 0.3 1 635 185 188 GLU CB C 28.082 0.3 1 636 185 188 GLU N N 118.959 0.3 1 637 186 189 TYR H H 7.694 0.020 1 638 186 189 TYR CA C 61.726 0.3 1 639 186 189 TYR CB C 37.551 0.3 1 640 186 189 TYR N N 120.232 0.3 1 641 187 190 VAL H H 7.934 0.020 1 642 187 190 VAL CA C 65.817 0.3 1 643 187 190 VAL CB C 29.947 0.3 1 644 187 190 VAL N N 120.720 0.3 1 645 188 191 TRP H H 8.176 0.020 1 646 188 191 TRP CA C 59.678 0.3 1 647 188 191 TRP CB C 28.226 0.3 1 648 188 191 TRP N N 121.121 0.3 1 649 189 192 GLN H H 8.225 0.020 1 650 189 192 GLN CA C 57.814 0.3 1 651 189 192 GLN CB C 28.169 0.3 1 652 189 192 GLN N N 112.786 0.3 1 653 190 193 ASN H H 7.529 0.020 1 654 190 193 ASN CA C 54.622 0.3 1 655 190 193 ASN CB C 40.062 0.3 1 656 190 193 ASN N N 111.975 0.3 1 657 191 194 PHE H H 8.512 0.020 1 658 191 194 PHE CA C 57.708 0.3 1 659 191 194 PHE CB C 40.421 0.3 1 660 191 194 PHE N N 113.110 0.3 1 661 192 195 VAL H H 6.523 0.020 1 662 192 195 VAL CA C 60.937 0.3 1 663 192 195 VAL CB C 30.665 0.3 1 664 192 195 VAL N N 118.699 0.3 1 665 193 196 GLU H H 8.393 0.020 1 666 193 196 GLU CA C 54.983 0.3 1 667 193 196 GLU CB C 29.517 0.3 1 668 193 196 GLU N N 129.361 0.3 1 669 194 197 GLN H H 8.311 0.020 1 670 194 197 GLN CA C 55.058 0.3 1 671 194 197 GLN CB C 28.298 0.3 1 672 194 197 GLN N N 126.087 0.3 1 673 195 198 GLU H H 8.741 0.020 1 674 195 198 GLU CA C 56.059 0.3 1 675 195 198 GLU CB C 29.466 0.3 1 676 195 198 GLU N N 122.447 0.3 1 677 196 199 GLU H H 8.583 0.020 1 678 196 199 GLU CA C 57.169 0.3 1 679 196 199 GLU CB C 28.441 0.3 1 680 196 199 GLU N N 121.427 0.3 1 681 197 200 GLY H H 8.474 0.020 1 682 197 200 GLY CA C 44.969 0.3 1 683 197 200 GLY N N 110.302 0.3 1 684 198 201 GLU H H 7.866 0.020 1 685 198 201 GLU CA C 55.494 0.3 1 686 198 201 GLU CB C 30.019 0.3 1 687 198 201 GLU N N 119.956 0.3 1 688 199 202 SER H H 8.487 0.020 1 689 199 202 SER CA C 57.708 0.3 1 690 199 202 SER CB C 63.017 0.3 1 691 199 202 SER N N 116.637 0.3 1 692 200 203 LYS H H 8.703 0.020 1 693 200 203 LYS CA C 55.628 0.3 1 694 200 203 LYS CB C 32.458 0.3 1 695 200 203 LYS N N 124.125 0.3 1 696 201 204 ALA H H 8.182 0.020 1 697 201 204 ALA CA C 51.252 0.3 1 698 201 204 ALA CB C 18.327 0.3 1 699 201 204 ALA N N 124.235 0.3 1 700 202 205 PHE H H 8.608 0.020 1 701 202 205 PHE CA C 56.489 0.3 1 702 202 205 PHE CB C 38.556 0.3 1 703 202 205 PHE N N 121.749 0.3 1 704 203 206 GLN H H 7.075 0.020 1 705 203 206 GLN CA C 50.535 0.3 1 706 203 206 GLN CB C 28.011 0.3 1 707 203 206 GLN N N 128.185 0.3 1 708 206 209 GLU H H 9.139 0.020 1 709 206 209 GLU CA C 58.904 0.3 1 710 206 209 GLU CB C 28.441 0.3 1 711 206 209 GLU N N 120.758 0.3 1 712 207 210 ASP H H 8.774 0.020 1 713 207 210 ASP CA C 53.416 0.3 1 714 207 210 ASP CB C 38.197 0.3 1 715 207 210 ASP N N 115.581 0.3 1 716 208 211 ILE H H 7.323 0.020 1 717 208 211 ILE CA C 65.036 0.3 1 718 208 211 ILE CB C 36.977 0.3 1 719 208 211 ILE N N 119.811 0.3 1 720 209 212 GLN H H 8.369 0.020 1 721 209 212 GLN CA C 58.239 0.3 1 722 209 212 GLN CB C 27.137 0.3 1 723 209 212 GLN N N 123.050 0.3 1 724 210 213 GLU H H 8.884 0.020 1 725 210 213 GLU CA C 60.291 0.3 1 726 210 213 GLU CB C 27.724 0.3 1 727 210 213 GLU N N 121.190 0.3 1 728 211 214 ASN H H 8.634 0.020 1 729 211 214 ASN CA C 55.413 0.3 1 730 211 214 ASN CB C 37.479 0.3 1 731 211 214 ASN N N 118.335 0.3 1 732 212 215 PHE H H 7.538 0.020 1 733 212 215 PHE CA C 60.332 0.3 1 734 212 215 PHE CB C 37.049 0.3 1 735 212 215 PHE N N 122.248 0.3 1 736 213 216 LEU H H 8.071 0.020 1 737 213 216 LEU CA C 57.185 0.3 1 738 213 216 LEU CB C 40.636 0.3 1 739 213 216 LEU N N 120.056 0.3 1 740 214 217 TYR H H 7.825 0.020 1 741 214 217 TYR CA C 60.589 0.3 1 742 214 217 TYR CB C 37.264 0.3 1 743 214 217 TYR N N 119.969 0.3 1 744 215 218 TYR H H 8.067 0.020 1 745 215 218 TYR CA C 61.760 0.3 1 746 215 218 TYR CB C 37.125 0.3 1 747 215 218 TYR N N 116.625 0.3 1 748 216 219 GLU H H 9.186 0.020 1 749 216 219 GLU CA C 59.513 0.3 1 750 216 219 GLU CB C 28.154 0.3 1 751 216 219 GLU N N 122.646 0.3 1 752 217 220 GLU H H 7.560 0.020 1 753 217 220 GLU CA C 58.678 0.3 1 754 217 220 GLU CB C 28.166 0.3 1 755 217 220 GLU N N 119.235 0.3 1 756 218 221 LYS H H 7.222 0.020 1 757 218 221 LYS CA C 56.704 0.3 1 758 218 221 LYS CB C 29.302 0.3 1 759 218 221 LYS N N 116.206 0.3 1 760 219 222 LEU H H 8.534 0.020 1 761 219 222 LEU CA C 57.063 0.3 1 762 219 222 LEU CB C 39.918 0.3 1 763 219 222 LEU N N 118.703 0.3 1 764 220 223 ALA H H 7.849 0.020 1 765 220 223 ALA CA C 54.337 0.3 1 766 220 223 ALA CB C 16.748 0.3 1 767 220 223 ALA N N 119.470 0.3 1 768 221 224 ASP H H 7.504 0.020 1 769 221 224 ASP CA C 56.592 0.3 1 770 221 224 ASP CB C 40.564 0.3 1 771 221 224 ASP N N 116.415 0.3 1 772 222 225 ILE H H 7.741 0.020 1 773 222 225 ILE CA C 64.067 0.3 1 774 222 225 ILE CB C 37.910 0.3 1 775 222 225 ILE N N 119.025 0.3 1 776 223 226 LEU H H 7.916 0.020 1 777 223 226 LEU CA C 54.541 0.3 1 778 223 226 LEU CB C 40.205 0.3 1 779 223 226 LEU N N 115.968 0.3 1 780 224 227 LYS H H 7.166 0.020 1 781 224 227 LYS CA C 58.713 0.3 1 782 224 227 LYS CB C 31.597 0.3 1 783 224 227 LYS N N 124.831 0.3 1 stop_ save_