data_15425 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Partial chemical shift assignments of the N-terminal deletion mutant KChIP4a(Delta1-42) in its Ca2+- and Mg2+-loaded form ; _BMRB_accession_number 15425 _BMRB_flat_file_name bmr15425.str _Entry_type original _Submission_date 2007-08-09 _Accession_date 2007-08-09 _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 Schwenk Jochen . . 2 Kandias Nikolaos G. . 3 Neubauer Isabel . . 4 Fakler Bernd . . 5 Bentrop Detlef . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 135 "13C chemical shifts" 393 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-03 update BMRB 'complete entry citation' 2007-10-03 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15422 KChIP4a stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Analysis of KChIP4a Reveals Structural Basis for Control of Surface Expression of Kv4 Channel Complexes' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18458082 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwenk Jochen . . 2 Zolles Gerd . . 3 Kandias Nikolaos G. . 4 Neubauer Isabel . . 5 Kalbacher Hubert . . 6 Covarrubias Manuel . . 7 Fakler Bernd . . 8 Bentrop Detlef . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 283 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18937 _Page_last 18946 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name KChIP4a(Delta1-42) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label KChIP4a(Delta1-42) $KChIP4a(Delta1-42) ligand1 $CA ligand2 $CA ligand3 $MG stop_ _System_molecular_weight 23200 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; N-terminal deletion mutant KChIP4a(Delta1-42) with EF-hand 2 loaded with Mg2+ and EF-hands 3 and 4 loaded with Ca2+ ; save_ ######################## # Monomeric polymers # ######################## save_KChIP4a(Delta1-42) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common KChIP4a(Delta1-42) _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'inactivation kinetics' 'recovery from inactivation' 'regulatory subunit of Kv4 channels' 'surface expression' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; GSTMGHHHHHHATVRHRPEA LELLEAQSKFTKKELQILYR GFKNECPSGVVNEETFKEIY SQFFPQGDSTTYAHFLFNAF DTDHNGAVSFEDFIKGLSIL LRGTVQEKLNWAFNLYDINK DGYITKEEMLDIMKAIYDMM GKCTYPVLKEDAPRQHVETF FQKMDKNKDGVVTIDEFIES CQKDENIMRSMQLFENVI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 32 GLY 2 33 SER 3 34 THR 4 35 MET 5 36 GLY 6 37 HIS 7 38 HIS 8 39 HIS 9 40 HIS 10 41 HIS 11 42 HIS 12 43 ALA 13 44 THR 14 45 VAL 15 46 ARG 16 47 HIS 17 48 ARG 18 49 PRO 19 50 GLU 20 51 ALA 21 52 LEU 22 53 GLU 23 54 LEU 24 55 LEU 25 56 GLU 26 57 ALA 27 58 GLN 28 59 SER 29 60 LYS 30 61 PHE 31 62 THR 32 63 LYS 33 64 LYS 34 65 GLU 35 66 LEU 36 67 GLN 37 68 ILE 38 69 LEU 39 70 TYR 40 71 ARG 41 72 GLY 42 73 PHE 43 74 LYS 44 75 ASN 45 76 GLU 46 77 CYS 47 78 PRO 48 79 SER 49 80 GLY 50 81 VAL 51 82 VAL 52 83 ASN 53 84 GLU 54 85 GLU 55 86 THR 56 87 PHE 57 88 LYS 58 89 GLU 59 90 ILE 60 91 TYR 61 92 SER 62 93 GLN 63 94 PHE 64 95 PHE 65 96 PRO 66 97 GLN 67 98 GLY 68 99 ASP 69 100 SER 70 101 THR 71 102 THR 72 103 TYR 73 104 ALA 74 105 HIS 75 106 PHE 76 107 LEU 77 108 PHE 78 109 ASN 79 110 ALA 80 111 PHE 81 112 ASP 82 113 THR 83 114 ASP 84 115 HIS 85 116 ASN 86 117 GLY 87 118 ALA 88 119 VAL 89 120 SER 90 121 PHE 91 122 GLU 92 123 ASP 93 124 PHE 94 125 ILE 95 126 LYS 96 127 GLY 97 128 LEU 98 129 SER 99 130 ILE 100 131 LEU 101 132 LEU 102 133 ARG 103 134 GLY 104 135 THR 105 136 VAL 106 137 GLN 107 138 GLU 108 139 LYS 109 140 LEU 110 141 ASN 111 142 TRP 112 143 ALA 113 144 PHE 114 145 ASN 115 146 LEU 116 147 TYR 117 148 ASP 118 149 ILE 119 150 ASN 120 151 LYS 121 152 ASP 122 153 GLY 123 154 TYR 124 155 ILE 125 156 THR 126 157 LYS 127 158 GLU 128 159 GLU 129 160 MET 130 161 LEU 131 162 ASP 132 163 ILE 133 164 MET 134 165 LYS 135 166 ALA 136 167 ILE 137 168 TYR 138 169 ASP 139 170 MET 140 171 MET 141 172 GLY 142 173 LYS 143 174 CYS 144 175 THR 145 176 TYR 146 177 PRO 147 178 VAL 148 179 LEU 149 180 LYS 150 181 GLU 151 182 ASP 152 183 ALA 153 184 PRO 154 185 ARG 155 186 GLN 156 187 HIS 157 188 VAL 158 189 GLU 159 190 THR 160 191 PHE 161 192 PHE 162 193 GLN 163 194 LYS 164 195 MET 165 196 ASP 166 197 LYS 167 198 ASN 168 199 LYS 169 200 ASP 170 201 GLY 171 202 VAL 172 203 VAL 173 204 THR 174 205 ILE 175 206 ASP 176 207 GLU 177 208 PHE 178 209 ILE 179 210 GLU 180 211 SER 181 212 CYS 182 213 GLN 183 214 LYS 184 215 ASP 185 216 GLU 186 217 ASN 187 218 ILE 188 219 MET 189 220 ARG 190 221 SER 191 222 MET 192 223 GLN 193 224 LEU 194 225 PHE 195 226 GLU 196 227 ASN 197 228 VAL 198 229 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 3DD4 "Structural Basis Of Kchip4a Modulation Of Kv4.3 Slow Inactivation" 94.44 229 100.00 100.00 4.67e-136 DBJ BAC30218 "unnamed protein product [Mus musculus]" 94.44 229 99.47 100.00 1.96e-135 DBJ BAE21645 "unnamed protein product [Mus musculus]" 94.44 188 100.00 100.00 4.73e-136 DBJ BAE28641 "unnamed protein product [Mus musculus]" 94.44 225 100.00 100.00 8.44e-136 DBJ BAE38374 "unnamed protein product [Mus musculus]" 94.44 229 100.00 100.00 4.67e-136 DBJ BAE90434 "unnamed protein product [Macaca fascicularis]" 94.44 250 100.00 100.00 7.82e-137 EMBL CAH90097 "hypothetical protein [Pongo abelii]" 94.44 216 98.93 98.93 6.60e-135 GB AAG36974 "calsenilin-like protein [Homo sapiens]" 94.44 216 100.00 100.00 1.13e-136 GB AAG36976 "calsenilin-like protein [Mus musculus]" 94.44 250 100.00 100.00 1.34e-136 GB AAG36977 "calsenilin-like protein [Homo sapiens]" 94.44 250 100.00 100.00 1.20e-136 GB AAH32520 "Kv channel interacting protein 4 [Homo sapiens]" 94.44 250 100.00 100.00 7.82e-137 GB AAH51130 "Kcnip4 protein [Mus musculus]" 94.44 250 100.00 100.00 1.03e-136 REF NP_001030175 "Kv channel-interacting protein 4 isoform 5 [Homo sapiens]" 94.44 225 100.00 100.00 8.44e-136 REF NP_001030176 "Kv channel-interacting protein 4 isoform 3 [Homo sapiens]" 94.44 188 100.00 100.00 4.73e-136 REF NP_001070403 "Kv channel-interacting protein 4 [Bos taurus]" 94.44 250 99.47 100.00 2.96e-136 REF NP_001127236 "Kv channel-interacting protein 4 [Pongo abelii]" 94.44 216 98.93 98.93 6.60e-135 REF NP_001186171 "Kv channel-interacting protein 4 isoform 1 [Mus musculus]" 94.44 250 100.00 100.00 1.03e-136 SP Q2KI69 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4" 94.44 250 99.47 100.00 2.96e-136 SP Q6PHZ8 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 94.44 250 100.00 100.00 1.03e-136 SP Q6PIL6 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 94.44 250 100.00 100.00 7.82e-137 SP Q8HYN7 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 94.44 250 100.00 100.00 7.82e-137 SP Q99MG9 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 94.44 250 100.00 100.00 1.03e-136 TPG DAA28811 "TPA: kv channel-interacting protein 4 [Bos taurus]" 94.44 250 99.47 100.00 2.96e-136 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 12 11:09:55 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 12 11:09:29 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $KChIP4a(Delta1-42) Mouse 10090 Eukaryota Metazoa Mus musculus 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 $KChIP4a(Delta1-42) 'recombinant technology' . Escherichia coli BL21(DE3) pET30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'All samples contained trace amounts of internal DSS.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $KChIP4a(Delta1-42) 0.25 mM '[U-13C; U-15N; U-2H]' MOPS 10 mM 'natural abundance' DTT 4 mM 'natural abundance' N-octylglucoside 5 mM 'natural abundance' 'magnesium chloride' 2 mM 'natural abundance' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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 pH 7.4 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_ _Software_label $CARA stop_ loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(CO)CACB' '3D HNCO' '3D 1H-15N NOESY' '2D 1H-15N HSQC' 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 KChIP4a(Delta1-42) _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 52 21 LEU C C 178.6 0.2 1 2 52 21 LEU CA C 56.8 0.2 1 3 52 21 LEU CB C 40.2 0.2 1 4 53 22 GLU H H 8.15 0.02 1 5 53 22 GLU C C 179.1 0.2 1 6 53 22 GLU CA C 58.6 0.2 1 7 53 22 GLU CB C 27.9 0.2 1 8 53 22 GLU N N 119.7 0.2 1 9 54 23 LEU H H 7.73 0.02 1 10 54 23 LEU C C 178.9 0.2 1 11 54 23 LEU CA C 56.7 0.2 1 12 54 23 LEU CB C 39.9 0.2 1 13 54 23 LEU N N 121.3 0.2 1 14 55 24 LEU H H 7.70 0.02 1 15 55 24 LEU C C 179.5 0.2 1 16 55 24 LEU CA C 56.4 0.2 1 17 55 24 LEU CB C 40.4 0.2 1 18 55 24 LEU N N 119.3 0.2 1 19 56 25 GLU H H 8.06 0.02 1 20 56 25 GLU C C 176.6 0.2 1 21 56 25 GLU CA C 58.6 0.2 1 22 56 25 GLU CB C 28.7 0.2 1 23 56 25 GLU N N 122.7 0.2 1 24 57 26 ALA H H 7.42 0.02 1 25 57 26 ALA C C 179.0 0.2 1 26 57 26 ALA CA C 53.2 0.2 1 27 57 26 ALA N N 119.7 0.2 1 28 58 27 GLN H H 7.67 0.02 1 29 58 27 GLN CA C 55.3 0.2 1 30 58 27 GLN N N 115.1 0.2 1 31 60 29 LYS C C 176.1 0.2 1 32 60 29 LYS CA C 54.6 0.2 1 33 61 30 PHE H H 7.68 0.02 1 34 61 30 PHE C C 175.8 0.2 1 35 61 30 PHE CA C 56.6 0.2 1 36 61 30 PHE CB C 40.3 0.2 1 37 61 30 PHE N N 119.3 0.2 1 38 62 31 THR H H 9.29 0.02 1 39 62 31 THR C C 175.5 0.2 1 40 62 31 THR CA C 60.1 0.2 1 41 62 31 THR CB C 70.3 0.2 1 42 62 31 THR N N 113.1 0.2 1 43 63 32 LYS H H 8.66 0.02 1 44 63 32 LYS C C 178.6 0.2 1 45 63 32 LYS CA C 60.2 0.2 1 46 63 32 LYS CB C 30.9 0.2 1 47 63 32 LYS N N 121.3 0.2 1 48 64 33 LYS H H 8.09 0.02 1 49 64 33 LYS C C 179.3 0.2 1 50 64 33 LYS CA C 58.9 0.2 1 51 64 33 LYS CB C 31.4 0.2 1 52 64 33 LYS N N 118.3 0.2 1 53 65 34 GLU H H 7.60 0.02 1 54 65 34 GLU C C 179.2 0.2 1 55 65 34 GLU CA C 58.8 0.2 1 56 65 34 GLU CB C 29.2 0.2 1 57 65 34 GLU N N 119.1 0.2 1 58 66 35 LEU H H 8.73 0.02 1 59 66 35 LEU C C 179.0 0.2 1 60 66 35 LEU CA C 57.5 0.2 1 61 66 35 LEU CB C 41.0 0.2 1 62 66 35 LEU N N 118.8 0.2 1 63 67 36 GLN H H 8.09 0.02 1 64 67 36 GLN C C 179.2 0.2 1 65 67 36 GLN CA C 58.9 0.2 1 66 67 36 GLN CB C 27.1 0.2 1 67 67 36 GLN N N 118.6 0.2 1 68 68 37 ILE H H 7.60 0.02 1 69 68 37 ILE C C 179.4 0.2 1 70 68 37 ILE CA C 64.6 0.2 1 71 68 37 ILE CB C 36.9 0.2 1 72 68 37 ILE N N 121.7 0.2 1 73 69 38 LEU H H 8.34 0.02 1 74 69 38 LEU C C 178.5 0.2 1 75 69 38 LEU CA C 57.6 0.2 1 76 69 38 LEU CB C 41.0 0.2 1 77 69 38 LEU N N 121.8 0.2 1 78 70 39 TYR H H 8.95 0.02 1 79 70 39 TYR C C 176.9 0.2 1 80 70 39 TYR CA C 60.6 0.2 1 81 70 39 TYR CB C 36.9 0.2 1 82 70 39 TYR N N 120.4 0.2 1 83 71 40 ARG H H 7.82 0.02 1 84 71 40 ARG C C 179.1 0.2 1 85 71 40 ARG CA C 58.6 0.2 1 86 71 40 ARG CB C 28.6 0.2 1 87 71 40 ARG N N 118.9 0.2 1 88 72 41 GLY H H 7.88 0.02 1 89 72 41 GLY CA C 46.7 0.2 1 90 72 41 GLY N N 105.7 0.2 1 91 78 47 PRO C C 177.5 0.2 1 92 78 47 PRO CA C 65.5 0.2 1 93 79 48 SER H H 7.59 0.02 1 94 79 48 SER C C 176.1 0.2 1 95 79 48 SER CA C 59.0 0.2 1 96 79 48 SER CB C 62.7 0.2 1 97 79 48 SER N N 117.0 0.2 1 98 80 49 GLY H H 8.22 0.02 1 99 80 49 GLY C C 172.5 0.2 1 100 80 49 GLY CA C 45.1 0.2 1 101 80 49 GLY N N 110.0 0.2 1 102 81 50 VAL H H 7.60 0.02 1 103 81 50 VAL N N 118.6 0.2 1 104 82 51 VAL H H 9.30 0.02 1 105 82 51 VAL C C 174.5 0.2 1 106 82 51 VAL CA C 60.1 0.2 1 107 82 51 VAL CB C 33.0 0.2 1 108 82 51 VAL N N 125.1 0.2 1 109 83 52 ASN H H 7.70 0.02 1 110 83 52 ASN C C 174.8 0.2 1 111 83 52 ASN CA C 50.2 0.2 1 112 83 52 ASN CB C 38.5 0.2 1 113 83 52 ASN N N 124.7 0.2 1 114 84 53 GLU H H 8.39 0.02 1 115 84 53 GLU C C 177.9 0.2 1 116 84 53 GLU CA C 59.6 0.2 1 117 84 53 GLU CB C 27.6 0.2 1 118 84 53 GLU N N 122.3 0.2 1 119 85 54 GLU H H 8.27 0.02 1 120 85 54 GLU C C 179.6 0.2 1 121 85 54 GLU CA C 59.3 0.2 1 122 85 54 GLU CB C 27.6 0.2 1 123 85 54 GLU N N 118.6 0.2 1 124 86 55 THR H H 8.12 0.02 1 125 86 55 THR C C 175.9 0.2 1 126 86 55 THR CA C 65.8 0.2 1 127 86 55 THR CB C 67.6 0.2 1 128 86 55 THR N N 117.4 0.2 1 129 87 56 PHE H H 8.53 0.02 1 130 87 56 PHE C C 176.7 0.2 1 131 87 56 PHE CA C 62.0 0.2 1 132 87 56 PHE CB C 39.2 0.2 1 133 87 56 PHE N N 123.1 0.2 1 134 88 57 LYS H H 8.41 0.02 1 135 88 57 LYS CA C 59.9 0.2 1 136 88 57 LYS CB C 30.9 0.2 1 137 88 57 LYS N N 117.6 0.2 1 138 89 58 GLU C C 179.5 0.2 1 139 89 58 GLU CA C 58.9 0.2 1 140 90 59 ILE H H 8.16 0.02 1 141 90 59 ILE C C 178.2 0.2 1 142 90 59 ILE CA C 64.4 0.2 1 143 90 59 ILE CB C 36.9 0.2 1 144 90 59 ILE N N 121.3 0.2 1 145 91 60 TYR H H 8.73 0.02 1 146 91 60 TYR C C 177.6 0.2 1 147 91 60 TYR CA C 62.6 0.2 1 148 91 60 TYR CB C 38.1 0.2 1 149 91 60 TYR N N 121.0 0.2 1 150 92 61 SER H H 7.92 0.02 1 151 92 61 SER C C 175.8 0.2 1 152 92 61 SER CA C 60.6 0.2 1 153 92 61 SER CB C 62.4 0.2 1 154 92 61 SER N N 111.6 0.2 1 155 93 62 GLN H H 7.34 0.02 1 156 93 62 GLN C C 177.7 0.2 1 157 93 62 GLN CA C 56.9 0.2 1 158 93 62 GLN CB C 27.3 0.2 1 159 93 62 GLN N N 119.8 0.2 1 160 94 63 PHE H H 7.37 0.02 1 161 94 63 PHE C C 175.1 0.2 1 162 94 63 PHE CA C 59.1 0.2 1 163 94 63 PHE CB C 39.0 0.2 1 164 94 63 PHE N N 117.3 0.2 1 165 95 64 PHE H H 7.66 0.02 1 166 95 64 PHE CA C 55.0 0.2 1 167 95 64 PHE CB C 38.2 0.2 1 168 95 64 PHE N N 117.1 0.2 1 169 96 65 PRO C C 177.8 0.2 1 170 96 65 PRO CA C 63.8 0.2 1 171 96 65 PRO CB C 31.4 0.2 1 172 97 66 GLN H H 8.60 0.02 1 173 97 66 GLN C C 176.1 0.2 1 174 97 66 GLN CA C 56.3 0.2 1 175 97 66 GLN CB C 28.4 0.2 1 176 97 66 GLN N N 119.8 0.2 1 177 98 67 GLY H H 7.98 0.02 1 178 98 67 GLY CA C 44.4 0.2 1 179 98 67 GLY N N 109.5 0.2 1 180 103 72 TYR C C 177.0 0.2 1 181 103 72 TYR CA C 61.9 0.2 1 182 104 73 ALA H H 8.71 0.02 1 183 104 73 ALA C C 179.1 0.2 1 184 104 73 ALA CA C 54.9 0.2 1 185 104 73 ALA N N 118.9 0.2 1 186 105 74 HIS H H 7.64 0.02 1 187 105 74 HIS C C 176.6 0.2 1 188 105 74 HIS CA C 59.0 0.2 1 189 105 74 HIS CB C 27.1 0.2 1 190 105 74 HIS N N 117.5 0.2 1 191 106 75 PHE H H 7.41 0.02 1 192 106 75 PHE CA C 60.1 0.2 1 193 106 75 PHE CB C 36.9 0.2 1 194 106 75 PHE N N 119.4 0.2 1 195 107 76 LEU H H 8.57 0.02 1 196 107 76 LEU C C 178.0 0.2 1 197 107 76 LEU CA C 57.0 0.2 1 198 107 76 LEU CB C 39.5 0.2 1 199 107 76 LEU N N 121.9 0.2 1 200 108 77 PHE H H 8.54 0.02 1 201 108 77 PHE C C 176.9 0.2 1 202 108 77 PHE CA C 62.0 0.2 1 203 108 77 PHE CB C 37.1 0.2 1 204 108 77 PHE N N 120.6 0.2 1 205 109 78 ASN H H 7.40 0.02 1 206 109 78 ASN C C 176.2 0.2 1 207 109 78 ASN CA C 55.5 0.2 1 208 109 78 ASN CB C 37.8 0.2 1 209 109 78 ASN N N 115.3 0.2 1 210 110 79 ALA H H 7.34 0.02 1 211 110 79 ALA C C 179.0 0.2 1 212 110 79 ALA CA C 53.4 0.2 1 213 110 79 ALA CB C 17.1 0.2 1 214 110 79 ALA N N 121.3 0.2 1 215 111 80 PHE H H 7.54 0.02 1 216 111 80 PHE C C 177.1 0.2 1 217 111 80 PHE CA C 59.0 0.2 1 218 111 80 PHE CB C 39.7 0.2 1 219 111 80 PHE N N 116.2 0.2 1 220 112 81 ASP H H 7.56 0.02 1 221 112 81 ASP CA C 51.4 0.2 1 222 112 81 ASP CB C 38.7 0.2 1 223 112 81 ASP N N 120.8 0.2 1 224 115 84 HIS C C 174.3 0.2 1 225 116 85 ASN H H 8.04 0.02 1 226 116 85 ASN C C 177.1 0.2 1 227 116 85 ASN CA C 51.1 0.2 1 228 116 85 ASN N N 116.7 0.2 1 229 117 86 GLY H H 10.93 0.02 1 230 117 86 GLY C C 173.9 0.2 1 231 117 86 GLY CA C 45.4 0.2 1 232 117 86 GLY N N 114.8 0.2 1 233 118 87 ALA H H 7.70 0.02 1 234 118 87 ALA C C 174.8 0.2 1 235 118 87 ALA CA C 50.7 0.2 1 236 118 87 ALA CB C 21.0 0.2 1 237 118 87 ALA N N 122.4 0.2 1 238 119 88 VAL H H 9.08 0.02 1 239 119 88 VAL C C 173.6 0.2 1 240 119 88 VAL CA C 60.8 0.2 1 241 119 88 VAL N N 129.0 0.2 1 242 120 89 SER H H 9.50 0.02 1 243 120 89 SER C C 175.0 0.2 1 244 120 89 SER CA C 56.1 0.2 1 245 120 89 SER CB C 66.5 0.2 1 246 120 89 SER N N 124.4 0.2 1 247 121 90 PHE H H 8.97 0.02 1 248 121 90 PHE C C 176.6 0.2 1 249 121 90 PHE CA C 61.4 0.2 1 250 121 90 PHE CB C 37.5 0.2 1 251 121 90 PHE N N 121.6 0.2 1 252 122 91 GLU H H 8.91 0.02 1 253 122 91 GLU C C 178.2 0.2 1 254 122 91 GLU CA C 60.1 0.2 1 255 122 91 GLU CB C 28.0 0.2 1 256 122 91 GLU N N 118.7 0.2 1 257 123 92 ASP H H 7.80 0.02 1 258 123 92 ASP C C 179.9 0.2 1 259 123 92 ASP CA C 56.7 0.2 1 260 123 92 ASP CB C 40.7 0.2 1 261 123 92 ASP N N 120.0 0.2 1 262 124 93 PHE H H 8.33 0.02 1 263 124 93 PHE C C 176.0 0.2 1 264 124 93 PHE CA C 59.6 0.2 1 265 124 93 PHE CB C 38.0 0.2 1 266 124 93 PHE N N 122.8 0.2 1 267 125 94 ILE H H 8.41 0.02 1 268 125 94 ILE C C 178.7 0.2 1 269 125 94 ILE CA C 60.8 0.2 1 270 125 94 ILE CB C 33.7 0.2 1 271 125 94 ILE N N 119.2 0.2 1 272 126 95 LYS H H 8.27 0.02 1 273 126 95 LYS C C 179.7 0.2 1 274 126 95 LYS CA C 59.9 0.2 1 275 126 95 LYS CB C 30.9 0.2 1 276 126 95 LYS N N 121.9 0.2 1 277 127 96 GLY H H 7.57 0.02 1 278 127 96 GLY C C 174.6 0.2 1 279 127 96 GLY CA C 46.7 0.2 1 280 127 96 GLY N N 104.7 0.2 1 281 128 97 LEU H H 8.65 0.02 1 282 128 97 LEU C C 178.5 0.2 1 283 128 97 LEU CA C 57.0 0.2 1 284 128 97 LEU CB C 40.8 0.2 1 285 128 97 LEU N N 122.1 0.2 1 286 129 98 SER H H 8.50 0.02 1 287 129 98 SER C C 176.0 0.2 1 288 129 98 SER CA C 61.8 0.2 1 289 129 98 SER N N 113.3 0.2 1 290 130 99 ILE H H 6.65 0.02 1 291 130 99 ILE C C 177.4 0.2 1 292 130 99 ILE CA C 63.4 0.2 1 293 130 99 ILE N N 120.0 0.2 1 294 131 100 LEU H H 7.45 0.02 1 295 131 100 LEU C C 178.0 0.2 1 296 131 100 LEU CA C 57.4 0.2 1 297 131 100 LEU CB C 41.2 0.2 1 298 131 100 LEU N N 117.5 0.2 1 299 132 101 LEU H H 8.37 0.02 1 300 132 101 LEU CA C 55.4 0.2 1 301 132 101 LEU CB C 41.7 0.2 1 302 132 101 LEU N N 112.5 0.2 1 303 133 102 ARG C C 176.2 0.2 1 304 133 102 ARG CA C 54.4 0.2 1 305 133 102 ARG CB C 31.2 0.2 1 306 134 103 GLY H H 7.65 0.02 1 307 134 103 GLY C C 174.5 0.2 1 308 134 103 GLY CA C 44.8 0.2 1 309 134 103 GLY N N 110.2 0.2 1 310 135 104 THR H H 8.95 0.02 1 311 135 104 THR C C 175.5 0.2 1 312 135 104 THR CA C 60.8 0.2 1 313 135 104 THR CB C 70.1 0.2 1 314 135 104 THR N N 112.8 0.2 1 315 136 105 VAL H H 8.64 0.02 1 316 136 105 VAL C C 177.6 0.2 1 317 136 105 VAL CA C 66.8 0.2 1 318 136 105 VAL CB C 30.6 0.2 1 319 136 105 VAL N N 121.4 0.2 1 320 137 106 GLN H H 8.20 0.02 1 321 137 106 GLN C C 178.9 0.2 1 322 137 106 GLN CA C 59.6 0.2 1 323 137 106 GLN CB C 26.8 0.2 1 324 137 106 GLN N N 117.6 0.2 1 325 138 107 GLU H H 7.73 0.02 1 326 138 107 GLU C C 180.4 0.2 1 327 138 107 GLU CA C 58.9 0.2 1 328 138 107 GLU CB C 28.8 0.2 1 329 138 107 GLU N N 120.2 0.2 1 330 139 108 LYS H H 8.58 0.02 1 331 139 108 LYS C C 179.2 0.2 1 332 139 108 LYS CA C 60.3 0.2 1 333 139 108 LYS CB C 31.6 0.2 1 334 139 108 LYS N N 121.1 0.2 1 335 140 109 LEU H H 8.58 0.02 1 336 140 109 LEU C C 178.9 0.2 1 337 140 109 LEU CA C 57.5 0.2 1 338 140 109 LEU CB C 40.8 0.2 1 339 140 109 LEU N N 119.8 0.2 1 340 141 110 ASN H H 8.09 0.02 1 341 141 110 ASN C C 177.1 0.2 1 342 141 110 ASN CA C 56.6 0.2 1 343 141 110 ASN CB C 38.4 0.2 1 344 141 110 ASN N N 118.7 0.2 1 345 142 111 TRP H H 7.97 0.02 1 346 142 111 TRP C C 179.1 0.2 1 347 142 111 TRP CA C 61.6 0.2 1 348 142 111 TRP CB C 29.1 0.2 1 349 142 111 TRP N N 121.9 0.2 1 350 143 112 ALA H H 8.67 0.02 1 351 143 112 ALA C C 177.8 0.2 1 352 143 112 ALA CA C 54.6 0.2 1 353 143 112 ALA CB C 17.1 0.2 1 354 143 112 ALA N N 121.9 0.2 1 355 144 113 PHE H H 8.24 0.02 1 356 144 113 PHE C C 175.8 0.2 1 357 144 113 PHE CA C 61.6 0.2 1 358 144 113 PHE CB C 37.9 0.2 1 359 144 113 PHE N N 118.7 0.2 1 360 145 114 ASN H H 7.18 0.02 1 361 145 114 ASN C C 175.4 0.2 1 362 145 114 ASN CA C 55.1 0.2 1 363 145 114 ASN CB C 37.9 0.2 1 364 145 114 ASN N N 113.9 0.2 1 365 146 115 LEU H H 7.10 0.02 1 366 146 115 LEU C C 177.2 0.2 1 367 146 115 LEU CA C 56.6 0.2 1 368 146 115 LEU CB C 40.0 0.2 1 369 146 115 LEU N N 120.6 0.2 1 370 147 116 TYR H H 7.04 0.02 1 371 147 116 TYR C C 175.4 0.2 1 372 147 116 TYR CA C 58.9 0.2 1 373 147 116 TYR CB C 37.9 0.2 1 374 147 116 TYR N N 114.8 0.2 1 375 148 117 ASP H H 7.36 0.02 1 376 148 117 ASP C C 178.0 0.2 1 377 148 117 ASP CA C 50.8 0.2 1 378 148 117 ASP CB C 37.5 0.2 1 379 148 117 ASP N N 114.9 0.2 1 380 149 118 ILE H H 7.58 0.02 1 381 149 118 ILE C C 178.0 0.2 1 382 149 118 ILE CA C 65.2 0.2 1 383 149 118 ILE CB C 37.8 0.2 1 384 149 118 ILE N N 127.3 0.2 1 385 150 119 ASN H H 7.98 0.02 1 386 150 119 ASN C C 175.0 0.2 1 387 150 119 ASN CA C 51.6 0.2 1 388 150 119 ASN CB C 36.4 0.2 1 389 150 119 ASN N N 114.6 0.2 1 390 151 120 LYS H H 7.71 0.02 1 391 151 120 LYS C C 176.2 0.2 1 392 151 120 LYS CA C 55.4 0.2 1 393 151 120 LYS CB C 26.9 0.2 1 394 151 120 LYS N N 116.1 0.2 1 395 152 121 ASP H H 8.16 0.02 1 396 152 121 ASP C C 177.2 0.2 1 397 152 121 ASP CA C 52.6 0.2 1 398 152 121 ASP CB C 40.0 0.2 1 399 152 121 ASP N N 119.2 0.2 1 400 153 122 GLY H H 10.49 0.02 1 401 153 122 GLY C C 172.8 0.2 1 402 153 122 GLY CA C 44.4 0.2 1 403 153 122 GLY N N 112.9 0.2 1 404 154 123 TYR H H 7.94 0.02 1 405 154 123 TYR C C 175.0 0.2 1 406 154 123 TYR CA C 54.9 0.2 1 407 154 123 TYR CB C 40.0 0.2 1 408 154 123 TYR N N 118.2 0.2 1 409 155 124 ILE H H 9.69 0.02 1 410 155 124 ILE C C 177.2 0.2 1 411 155 124 ILE CA C 60.9 0.2 1 412 155 124 ILE CB C 38.8 0.2 1 413 155 124 ILE N N 126.3 0.2 1 414 156 125 THR H H 8.60 0.02 1 415 156 125 THR C C 175.9 0.2 1 416 156 125 THR CA C 59.1 0.2 1 417 156 125 THR CB C 70.9 0.2 1 418 156 125 THR N N 118.0 0.2 1 419 157 126 LYS H H 8.92 0.02 1 420 157 126 LYS C C 178.4 0.2 1 421 157 126 LYS CA C 59.9 0.2 1 422 157 126 LYS CB C 30.4 0.2 1 423 157 126 LYS N N 123.1 0.2 1 424 158 127 GLU H H 8.29 0.02 1 425 158 127 GLU C C 179.2 0.2 1 426 158 127 GLU CA C 60.0 0.2 1 427 158 127 GLU CB C 27.6 0.2 1 428 158 127 GLU N N 117.7 0.2 1 429 159 128 GLU H H 7.55 0.02 1 430 159 128 GLU C C 178.1 0.2 1 431 159 128 GLU CA C 58.8 0.2 1 432 159 128 GLU CB C 28.1 0.2 1 433 159 128 GLU N N 120.7 0.2 1 434 160 129 MET H H 8.02 0.02 1 435 160 129 MET C C 178.3 0.2 1 436 160 129 MET CA C 58.6 0.2 1 437 160 129 MET CB C 31.4 0.2 1 438 160 129 MET N N 116.5 0.2 1 439 161 130 LEU H H 8.42 0.02 1 440 161 130 LEU C C 178.0 0.2 1 441 161 130 LEU CA C 57.6 0.2 1 442 161 130 LEU CB C 40.2 0.2 1 443 161 130 LEU N N 119.9 0.2 1 444 162 131 ASP H H 7.74 0.02 1 445 162 131 ASP C C 180.1 0.2 1 446 162 131 ASP CA C 57.4 0.2 1 447 162 131 ASP CB C 39.5 0.2 1 448 162 131 ASP N N 121.4 0.2 1 449 163 132 ILE H H 7.75 0.02 1 450 163 132 ILE C C 178.1 0.2 1 451 163 132 ILE CA C 61.9 0.2 1 452 163 132 ILE N N 120.0 0.2 1 453 164 133 MET H H 8.69 0.02 1 454 164 133 MET C C 179.4 0.2 1 455 164 133 MET CA C 57.4 0.2 1 456 164 133 MET CB C 29.8 0.2 1 457 164 133 MET N N 118.9 0.2 1 458 165 134 LYS H H 8.88 0.02 1 459 165 134 LYS C C 178.0 0.2 1 460 165 134 LYS CA C 59.6 0.2 1 461 165 134 LYS CB C 31.2 0.2 1 462 165 134 LYS N N 120.3 0.2 1 463 166 135 ALA H H 7.48 0.02 1 464 166 135 ALA C C 180.9 0.2 1 465 166 135 ALA CA C 54.5 0.2 1 466 166 135 ALA CB C 16.9 0.2 1 467 166 135 ALA N N 121.7 0.2 1 468 167 136 ILE H H 8.45 0.02 1 469 167 136 ILE C C 178.1 0.2 1 470 167 136 ILE CA C 64.8 0.2 1 471 167 136 ILE CB C 36.5 0.2 1 472 167 136 ILE N N 121.0 0.2 1 473 168 137 TYR H H 8.67 0.02 1 474 168 137 TYR C C 179.2 0.2 1 475 168 137 TYR CA C 61.6 0.2 1 476 168 137 TYR CB C 36.4 0.2 1 477 168 137 TYR N N 121.9 0.2 1 478 169 138 ASP H H 8.48 0.02 1 479 169 138 ASP C C 179.0 0.2 1 480 169 138 ASP CA C 56.7 0.2 1 481 169 138 ASP CB C 39.4 0.2 1 482 169 138 ASP N N 120.8 0.2 1 483 170 139 MET H H 7.66 0.02 1 484 170 139 MET C C 176.5 0.2 1 485 170 139 MET CA C 57.9 0.2 1 486 170 139 MET CB C 32.3 0.2 1 487 170 139 MET N N 120.8 0.2 1 488 171 140 MET H H 7.91 0.02 1 489 171 140 MET C C 177.6 0.2 1 490 171 140 MET CA C 55.9 0.2 1 491 171 140 MET CB C 31.6 0.2 1 492 171 140 MET N N 115.9 0.2 1 493 172 141 GLY H H 7.91 0.02 1 494 172 141 GLY CA C 45.5 0.2 1 495 172 141 GLY N N 108.0 0.2 1 496 187 156 HIS C C 178.3 0.2 1 497 187 156 HIS CA C 58.6 0.2 1 498 187 156 HIS CB C 30.2 0.2 1 499 188 157 VAL H H 8.08 0.02 1 500 188 157 VAL C C 177.5 0.2 1 501 188 157 VAL CA C 66.5 0.2 1 502 188 157 VAL CB C 30.4 0.2 1 503 188 157 VAL N N 119.6 0.2 1 504 189 158 GLU H H 8.17 0.02 1 505 189 158 GLU C C 179.6 0.2 1 506 189 158 GLU CA C 59.1 0.2 1 507 189 158 GLU CB C 27.8 0.2 1 508 189 158 GLU N N 119.5 0.2 1 509 190 159 THR H H 8.00 0.02 1 510 190 159 THR C C 176.5 0.2 1 511 190 159 THR CA C 65.7 0.2 1 512 190 159 THR CB C 68.2 0.2 1 513 190 159 THR N N 115.8 0.2 1 514 191 160 PHE H H 8.27 0.02 1 515 191 160 PHE C C 177.8 0.2 1 516 191 160 PHE CA C 60.1 0.2 1 517 191 160 PHE N N 121.6 0.2 1 518 192 161 PHE H H 9.21 0.02 1 519 192 161 PHE C C 177.9 0.2 1 520 192 161 PHE CA C 63.2 0.2 1 521 192 161 PHE CB C 37.8 0.2 1 522 192 161 PHE N N 121.4 0.2 1 523 193 162 GLN H H 7.97 0.02 1 524 193 162 GLN C C 178.4 0.2 1 525 193 162 GLN CA C 58.4 0.2 1 526 193 162 GLN CB C 27.6 0.2 1 527 193 162 GLN N N 116.5 0.2 1 528 194 163 LYS H H 7.29 0.02 1 529 194 163 LYS C C 178.0 0.2 1 530 194 163 LYS CA C 57.9 0.2 1 531 194 163 LYS CB C 31.9 0.2 1 532 194 163 LYS N N 116.8 0.2 1 533 195 164 MET H H 7.78 0.02 1 534 195 164 MET C C 176.9 0.2 1 535 195 164 MET CA C 57.1 0.2 1 536 195 164 MET CB C 34.7 0.2 1 537 195 164 MET N N 116.0 0.2 1 538 196 165 ASP H H 7.75 0.02 1 539 196 165 ASP C C 177.7 0.2 1 540 196 165 ASP CA C 52.1 0.2 1 541 196 165 ASP CB C 37.4 0.2 1 542 196 165 ASP N N 116.3 0.2 1 543 197 166 LYS H H 7.71 0.02 1 544 197 166 LYS C C 177.7 0.2 1 545 197 166 LYS CA C 58.6 0.2 1 546 197 166 LYS CB C 32.0 0.2 1 547 197 166 LYS N N 129.0 0.2 1 548 198 167 ASN H H 7.90 0.02 1 549 198 167 ASN C C 174.7 0.2 1 550 198 167 ASN CA C 51.3 0.2 1 551 198 167 ASN CB C 36.3 0.2 1 552 198 167 ASN N N 113.3 0.2 1 553 199 168 LYS H H 7.64 0.02 1 554 199 168 LYS C C 175.9 0.2 1 555 199 168 LYS CA C 56.9 0.2 1 556 199 168 LYS CB C 27.8 0.2 1 557 199 168 LYS N N 116.0 0.2 1 558 200 169 ASP H H 8.18 0.02 1 559 200 169 ASP C C 178.0 0.2 1 560 200 169 ASP CA C 52.7 0.2 1 561 200 169 ASP CB C 39.8 0.2 1 562 200 169 ASP N N 118.7 0.2 1 563 201 170 GLY H H 10.33 0.02 1 564 201 170 GLY C C 173.3 0.2 1 565 201 170 GLY CA C 45.0 0.2 1 566 201 170 GLY N N 113.1 0.2 1 567 202 171 VAL H H 7.84 0.02 1 568 202 171 VAL C C 174.8 0.2 1 569 202 171 VAL CA C 58.6 0.2 1 570 202 171 VAL CB C 35.7 0.2 1 571 202 171 VAL N N 112.6 0.2 1 572 203 172 VAL H H 9.24 0.02 1 573 203 172 VAL C C 176.7 0.2 1 574 203 172 VAL CA C 60.8 0.2 1 575 203 172 VAL CB C 32.6 0.2 1 576 203 172 VAL N N 126.4 0.2 1 577 204 173 THR H H 8.45 0.02 1 578 204 173 THR C C 177.0 0.2 1 579 204 173 THR CA C 59.9 0.2 1 580 204 173 THR CB C 70.6 0.2 1 581 204 173 THR N N 118.4 0.2 1 582 205 174 ILE H H 8.86 0.02 1 583 205 174 ILE C C 175.5 0.2 1 584 205 174 ILE CA C 63.2 0.2 1 585 205 174 ILE CB C 35.6 0.2 1 586 205 174 ILE N N 123.2 0.2 1 587 206 175 ASP H H 8.03 0.02 1 588 206 175 ASP C C 179.3 0.2 1 589 206 175 ASP CA C 56.1 0.2 1 590 206 175 ASP CB C 39.0 0.2 1 591 206 175 ASP N N 119.8 0.2 1 592 207 176 GLU H H 7.16 0.02 1 593 207 176 GLU C C 179.4 0.2 1 594 207 176 GLU CA C 58.4 0.2 1 595 207 176 GLU CB C 28.6 0.2 1 596 207 176 GLU N N 120.8 0.2 1 597 208 177 PHE H H 8.65 0.02 1 598 208 177 PHE C C 177.0 0.2 1 599 208 177 PHE CA C 61.1 0.2 1 600 208 177 PHE CB C 40.2 0.2 1 601 208 177 PHE N N 123.2 0.2 1 602 209 178 ILE H H 8.87 0.02 1 603 209 178 ILE C C 177.9 0.2 1 604 209 178 ILE CA C 65.3 0.2 1 605 209 178 ILE CB C 36.4 0.2 1 606 209 178 ILE N N 119.2 0.2 1 607 210 179 GLU H H 7.71 0.02 1 608 210 179 GLU C C 179.1 0.2 1 609 210 179 GLU CA C 59.0 0.2 1 610 210 179 GLU CB C 28.7 0.2 1 611 210 179 GLU N N 118.4 0.2 1 612 211 180 SER H H 7.75 0.02 1 613 211 180 SER C C 176.9 0.2 1 614 211 180 SER CA C 61.5 0.2 1 615 211 180 SER CB C 62.7 0.2 1 616 211 180 SER N N 112.8 0.2 1 617 212 181 CYS H H 7.60 0.02 1 618 212 181 CYS C C 176.0 0.2 1 619 212 181 CYS CA C 62.9 0.2 1 620 212 181 CYS N N 118.9 0.2 1 621 213 182 GLN H H 7.81 0.02 1 622 213 182 GLN C C 177.4 0.2 1 623 213 182 GLN CA C 57.6 0.2 1 624 213 182 GLN CB C 27.6 0.2 1 625 213 182 GLN N N 115.4 0.2 1 626 214 183 LYS H H 7.38 0.02 1 627 214 183 LYS C C 176.0 0.2 1 628 214 183 LYS CA C 56.1 0.2 1 629 214 183 LYS CB C 32.4 0.2 1 630 214 183 LYS N N 116.7 0.2 1 631 215 184 ASP H H 7.41 0.02 1 632 215 184 ASP C C 175.4 0.2 1 633 215 184 ASP CA C 52.8 0.2 1 634 215 184 ASP CB C 41.4 0.2 1 635 215 184 ASP N N 120.5 0.2 1 636 216 185 GLU H H 8.90 0.02 1 637 216 185 GLU C C 177.9 0.2 1 638 216 185 GLU CA C 58.1 0.2 1 639 216 185 GLU CB C 28.9 0.2 1 640 216 185 GLU N N 126.2 0.2 1 641 217 186 ASN H H 8.43 0.02 1 642 217 186 ASN C C 178.1 0.2 1 643 217 186 ASN CA C 55.5 0.2 1 644 217 186 ASN CB C 37.8 0.2 1 645 217 186 ASN N N 117.9 0.2 1 646 218 187 ILE H H 7.77 0.02 1 647 218 187 ILE C C 178.1 0.2 1 648 218 187 ILE CA C 64.6 0.2 1 649 218 187 ILE CB C 35.8 0.2 1 650 218 187 ILE N N 123.1 0.2 1 651 219 188 MET H H 8.07 0.02 1 652 219 188 MET CA C 57.9 0.2 1 653 219 188 MET N N 118.8 0.2 1 654 227 196 ASN C C 174.8 0.2 1 655 227 196 ASN CA C 53.1 0.2 1 656 228 197 VAL H H 7.94 0.02 1 657 228 197 VAL C C 174.7 0.2 1 658 228 197 VAL CA C 62.4 0.2 1 659 228 197 VAL N N 119.7 0.2 1 660 229 198 ILE H H 7.46 0.02 1 661 229 198 ILE CA C 62.1 0.2 1 662 229 198 ILE CB C 38.4 0.2 1 663 229 198 ILE N N 126.2 0.2 1 stop_ save_