data_15422 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Partial chemical shift assignments of KChIP4a in its Ca2+- and Mg2+-loaded form ; _BMRB_accession_number 15422 _BMRB_flat_file_name bmr15422.str _Entry_type original _Submission_date 2007-08-08 _Accession_date 2007-08-08 _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" 161 "13C chemical shifts" 477 "15N chemical shifts" 161 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 15425 'mutant KChIP4a(Delta1-42)' 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 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label KChIP4a $KChIP4a ligand1 $CA ligand2 $CA ligand3 $MG stop_ _System_molecular_weight 27600 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'KChIP4a with EF-hand 2 loaded with Mg2+ and EF-hands 3 and 4 loaded with Ca2+' save_ ######################## # Monomeric polymers # ######################## save_KChIP4a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common KChIP4a _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 237 _Mol_residue_sequence ; MGHHHHHHMNLEGLEMIAVL IVIVLFVKLLEQFGLIEAGL EDSVEDELEMATVRHRPEAL ELLEAQSKFTKKELQILYRG FKNECPSGVVNEETFKEIYS QFFPQGDSTTYAHFLFNAFD TDHNGAVSFEDFIKGLSILL RGTVQEKLNWAFNLYDINKD GYITKEEMLDIMKAIYDMMG KCTYPVLKEDAPRQHVETFF QKMDKNKDGVVTIDEFIESC QKDENIMRSMQLFENVI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -7 MET 2 -6 GLY 3 -5 HIS 4 -4 HIS 5 -3 HIS 6 -2 HIS 7 -1 HIS 8 0 HIS 9 1 MET 10 2 ASN 11 3 LEU 12 4 GLU 13 5 GLY 14 6 LEU 15 7 GLU 16 8 MET 17 9 ILE 18 10 ALA 19 11 VAL 20 12 LEU 21 13 ILE 22 14 VAL 23 15 ILE 24 16 VAL 25 17 LEU 26 18 PHE 27 19 VAL 28 20 LYS 29 21 LEU 30 22 LEU 31 23 GLU 32 24 GLN 33 25 PHE 34 26 GLY 35 27 LEU 36 28 ILE 37 29 GLU 38 30 ALA 39 31 GLY 40 32 LEU 41 33 GLU 42 34 ASP 43 35 SER 44 36 VAL 45 37 GLU 46 38 ASP 47 39 GLU 48 40 LEU 49 41 GLU 50 42 MET 51 43 ALA 52 44 THR 53 45 VAL 54 46 ARG 55 47 HIS 56 48 ARG 57 49 PRO 58 50 GLU 59 51 ALA 60 52 LEU 61 53 GLU 62 54 LEU 63 55 LEU 64 56 GLU 65 57 ALA 66 58 GLN 67 59 SER 68 60 LYS 69 61 PHE 70 62 THR 71 63 LYS 72 64 LYS 73 65 GLU 74 66 LEU 75 67 GLN 76 68 ILE 77 69 LEU 78 70 TYR 79 71 ARG 80 72 GLY 81 73 PHE 82 74 LYS 83 75 ASN 84 76 GLU 85 77 CYS 86 78 PRO 87 79 SER 88 80 GLY 89 81 VAL 90 82 VAL 91 83 ASN 92 84 GLU 93 85 GLU 94 86 THR 95 87 PHE 96 88 LYS 97 89 GLU 98 90 ILE 99 91 TYR 100 92 SER 101 93 GLN 102 94 PHE 103 95 PHE 104 96 PRO 105 97 GLN 106 98 GLY 107 99 ASP 108 100 SER 109 101 THR 110 102 THR 111 103 TYR 112 104 ALA 113 105 HIS 114 106 PHE 115 107 LEU 116 108 PHE 117 109 ASN 118 110 ALA 119 111 PHE 120 112 ASP 121 113 THR 122 114 ASP 123 115 HIS 124 116 ASN 125 117 GLY 126 118 ALA 127 119 VAL 128 120 SER 129 121 PHE 130 122 GLU 131 123 ASP 132 124 PHE 133 125 ILE 134 126 LYS 135 127 GLY 136 128 LEU 137 129 SER 138 130 ILE 139 131 LEU 140 132 LEU 141 133 ARG 142 134 GLY 143 135 THR 144 136 VAL 145 137 GLN 146 138 GLU 147 139 LYS 148 140 LEU 149 141 ASN 150 142 TRP 151 143 ALA 152 144 PHE 153 145 ASN 154 146 LEU 155 147 TYR 156 148 ASP 157 149 ILE 158 150 ASN 159 151 LYS 160 152 ASP 161 153 GLY 162 154 TYR 163 155 ILE 164 156 THR 165 157 LYS 166 158 GLU 167 159 GLU 168 160 MET 169 161 LEU 170 162 ASP 171 163 ILE 172 164 MET 173 165 LYS 174 166 ALA 175 167 ILE 176 168 TYR 177 169 ASP 178 170 MET 179 171 MET 180 172 GLY 181 173 LYS 182 174 CYS 183 175 THR 184 176 TYR 185 177 PRO 186 178 VAL 187 179 LEU 188 180 LYS 189 181 GLU 190 182 ASP 191 183 ALA 192 184 PRO 193 185 ARG 194 186 GLN 195 187 HIS 196 188 VAL 197 189 GLU 198 190 THR 199 191 PHE 200 192 PHE 201 193 GLN 202 194 LYS 203 195 MET 204 196 ASP 205 197 LYS 206 198 ASN 207 199 LYS 208 200 ASP 209 201 GLY 210 202 VAL 211 203 VAL 212 204 THR 213 205 ILE 214 206 ASP 215 207 GLU 216 208 PHE 217 209 ILE 218 210 GLU 219 211 SER 220 212 CYS 221 213 GLN 222 214 LYS 223 215 ASP 224 216 GLU 225 217 ASN 226 218 ILE 227 219 MET 228 220 ARG 229 221 SER 230 222 MET 231 223 GLN 232 224 LEU 233 225 PHE 234 226 GLU 235 227 ASN 236 228 VAL 237 229 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" 96.62 229 100.00 100.00 6.56e-166 DBJ BAC30218 "unnamed protein product [Mus musculus]" 96.62 229 99.56 100.00 1.94e-165 DBJ BAE21645 "unnamed protein product [Mus musculus]" 79.32 188 100.00 100.00 1.20e-136 DBJ BAE28641 "unnamed protein product [Mus musculus]" 82.70 225 100.00 100.00 2.97e-142 DBJ BAE38374 "unnamed protein product [Mus musculus]" 96.62 229 100.00 100.00 6.56e-166 DBJ BAE90434 "unnamed protein product [Macaca fascicularis]" 83.97 250 97.99 99.50 3.40e-143 EMBL CAH90097 "hypothetical protein [Pongo abelii]" 82.70 216 98.98 98.98 2.55e-141 GB AAG36974 "calsenilin-like protein [Homo sapiens]" 82.70 216 100.00 100.00 5.44e-143 GB AAG36976 "calsenilin-like protein [Mus musculus]" 83.97 250 97.99 99.50 3.44e-143 GB AAG36977 "calsenilin-like protein [Homo sapiens]" 83.97 250 97.99 99.50 5.74e-143 GB AAH32520 "Kv channel interacting protein 4 [Homo sapiens]" 83.97 250 97.99 99.50 3.40e-143 GB AAH51130 "Kcnip4 protein [Mus musculus]" 83.97 250 97.99 99.50 3.79e-143 REF NP_001030175 "Kv channel-interacting protein 4 isoform 5 [Homo sapiens]" 82.70 225 100.00 100.00 2.97e-142 REF NP_001030176 "Kv channel-interacting protein 4 isoform 3 [Homo sapiens]" 79.32 188 100.00 100.00 1.20e-136 REF NP_001070403 "Kv channel-interacting protein 4 [Bos taurus]" 83.97 250 97.49 99.50 1.75e-142 REF NP_001127236 "Kv channel-interacting protein 4 [Pongo abelii]" 82.70 216 98.98 98.98 2.55e-141 REF NP_001186171 "Kv channel-interacting protein 4 isoform 1 [Mus musculus]" 83.97 250 97.99 99.50 3.79e-143 SP Q2KI69 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4" 83.97 250 97.49 99.50 1.75e-142 SP Q6PHZ8 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 83.97 250 97.99 99.50 3.79e-143 SP Q6PIL6 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 83.97 250 97.99 99.50 3.40e-143 SP Q8HYN7 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 83.97 250 97.99 99.50 3.40e-143 SP Q99MG9 "RecName: Full=Kv channel-interacting protein 4; Short=KChIP4; AltName: Full=A-type potassium channel modulatory protein 4; AltN" 83.97 250 97.99 99.50 3.79e-143 TPG DAA28811 "TPA: kv channel-interacting protein 4 [Bos taurus]" 83.97 250 97.49 99.50 1.75e-142 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 10:50:12 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 10:51:45 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 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 'recombinant technology' . Escherichia coli BL21(DE3) pET16b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The added N-octylglucoside was necessary to stabilize the monomeric state of the protein. All samples contained trace amounts of internal DSS.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $KChIP4a . mM 0.1 0.25 '[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 _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 18 26 PHE C C 178.8 0.2 1 2 18 26 PHE CA C 58.9 0.2 1 3 19 27 VAL H H 8.08 0.02 1 4 19 27 VAL C C 178.0 0.2 1 5 19 27 VAL CA C 66.8 0.2 1 6 19 27 VAL CB C 30.4 0.2 1 7 19 27 VAL N N 120.5 0.2 1 8 20 28 LYS H H 7.86 0.02 1 9 20 28 LYS CA C 57.7 0.2 1 10 20 28 LYS N N 118.7 0.2 1 11 25 33 PHE C C 176.6 0.2 1 12 25 33 PHE CA C 57.8 0.2 1 13 26 34 GLY H H 7.92 0.02 1 14 26 34 GLY C C 175.2 0.2 1 15 26 34 GLY CA C 45.7 0.2 1 16 26 34 GLY N N 106.5 0.2 1 17 27 35 LEU H H 7.72 0.02 1 18 27 35 LEU C C 177.6 0.2 1 19 27 35 LEU CA C 55.6 0.2 1 20 27 35 LEU CB C 41.0 0.2 1 21 27 35 LEU N N 120.9 0.2 1 22 28 36 ILE H H 7.69 0.02 1 23 28 36 ILE C C 177.0 0.2 1 24 28 36 ILE CA C 61.6 0.2 1 25 28 36 ILE CB C 37.5 0.2 1 26 28 36 ILE N N 119.5 0.2 1 27 29 37 GLU H H 8.28 0.02 1 28 29 37 GLU C C 176.8 0.2 1 29 29 37 GLU CA C 57.0 0.2 1 30 29 37 GLU CB C 29.0 0.2 1 31 29 37 GLU N N 123.4 0.2 1 32 30 38 ALA H H 8.01 0.02 1 33 30 38 ALA C C 178.5 0.2 1 34 30 38 ALA CA C 52.6 0.2 1 35 30 38 ALA CB C 18.4 0.2 1 36 30 38 ALA N N 123.6 0.2 1 37 31 39 GLY H H 8.14 0.02 1 38 31 39 GLY C C 174.5 0.2 1 39 31 39 GLY CA C 44.9 0.2 1 40 31 39 GLY N N 107.6 0.2 1 41 32 40 LEU H H 7.90 0.02 1 42 32 40 LEU C C 177.6 0.2 1 43 32 40 LEU CA C 54.9 0.2 1 44 32 40 LEU CB C 41.1 0.2 1 45 32 40 LEU N N 121.8 0.2 1 46 33 41 GLU H H 8.31 0.02 1 47 33 41 GLU C C 176.4 0.2 1 48 33 41 GLU CA C 56.2 0.2 1 49 33 41 GLU CB C 29.5 0.2 1 50 33 41 GLU N N 121.3 0.2 1 51 34 42 ASP H H 8.21 0.02 1 52 34 42 ASP C C 176.2 0.2 1 53 34 42 ASP CA C 54.1 0.2 1 54 34 42 ASP CB C 40.8 0.2 1 55 34 42 ASP N N 121.7 0.2 1 56 35 43 SER H H 8.15 0.02 1 57 35 43 SER C C 174.7 0.2 1 58 35 43 SER CA C 57.8 0.2 1 59 35 43 SER CB C 63.6 0.2 1 60 35 43 SER N N 116.6 0.2 1 61 36 44 VAL H H 8.12 0.02 1 62 36 44 VAL C C 176.4 0.2 1 63 36 44 VAL CA C 62.1 0.2 1 64 36 44 VAL CB C 31.4 0.2 1 65 36 44 VAL N N 122.4 0.2 1 66 37 45 GLU H H 8.38 0.02 1 67 37 45 GLU C C 176.5 0.2 1 68 37 45 GLU CA C 56.4 0.2 1 69 37 45 GLU CB C 29.5 0.2 1 70 37 45 GLU N N 124.4 0.2 1 71 38 46 ASP H H 8.22 0.02 1 72 38 46 ASP C C 176.7 0.2 1 73 38 46 ASP CA C 54.1 0.2 1 74 38 46 ASP CB C 40.9 0.2 1 75 38 46 ASP N N 122.0 0.2 1 76 39 47 GLU H H 8.31 0.02 1 77 39 47 GLU C C 177.3 0.2 1 78 39 47 GLU CA C 56.9 0.2 1 79 39 47 GLU CB C 29.2 0.2 1 80 39 47 GLU N N 122.0 0.2 1 81 40 48 LEU H H 8.13 0.02 1 82 40 48 LEU C C 178.2 0.2 1 83 40 48 LEU CA C 55.6 0.2 1 84 40 48 LEU CB C 40.9 0.2 1 85 40 48 LEU N N 122.3 0.2 1 86 41 49 GLU H H 8.14 0.02 1 87 41 49 GLU C C 177.3 0.2 1 88 41 49 GLU CA C 56.8 0.2 1 89 41 49 GLU CB C 29.1 0.2 1 90 41 49 GLU N N 121.2 0.2 1 91 42 50 MET H H 8.12 0.02 1 92 42 50 MET C C 176.6 0.2 1 93 42 50 MET CA C 55.6 0.2 1 94 42 50 MET CB C 31.4 0.2 1 95 42 50 MET N N 120.1 0.2 1 96 43 51 ALA H H 8.08 0.02 1 97 43 51 ALA C C 178.2 0.2 1 98 43 51 ALA CA C 52.8 0.2 1 99 43 51 ALA N N 123.6 0.2 1 100 44 52 THR H H 7.84 0.02 1 101 44 52 THR C C 174.9 0.2 1 102 44 52 THR CA C 62.1 0.2 1 103 44 52 THR CB C 69.1 0.2 1 104 44 52 THR N N 112.2 0.2 1 105 45 53 VAL H H 7.82 0.02 1 106 45 53 VAL CA C 62.2 0.2 1 107 45 53 VAL CB C 31.3 0.2 1 108 45 53 VAL N N 121.7 0.2 1 109 49 57 PRO C C 177.6 0.2 1 110 49 57 PRO CA C 63.3 0.2 1 111 49 57 PRO CB C 30.5 0.2 1 112 50 58 GLU H H 8.90 0.02 1 113 50 58 GLU C C 177.3 0.2 1 114 50 58 GLU CA C 57.5 0.2 1 115 50 58 GLU CB C 28.8 0.2 1 116 50 58 GLU N N 121.7 0.2 1 117 51 59 ALA H H 8.11 0.02 1 118 51 59 ALA C C 179.3 0.2 1 119 51 59 ALA CA C 53.3 0.2 1 120 51 59 ALA CB C 17.9 0.2 1 121 51 59 ALA N N 123.1 0.2 1 122 52 60 LEU H H 7.79 0.02 1 123 52 60 LEU C C 178.4 0.2 1 124 52 60 LEU CA C 56.9 0.2 1 125 52 60 LEU CB C 40.5 0.2 1 126 52 60 LEU N N 119.0 0.2 1 127 53 61 GLU H H 8.19 0.02 1 128 53 61 GLU C C 179.2 0.2 1 129 53 61 GLU CA C 58.9 0.2 1 130 53 61 GLU CB C 28.0 0.2 1 131 53 61 GLU N N 119.6 0.2 1 132 54 62 LEU H H 7.69 0.02 1 133 54 62 LEU C C 178.9 0.2 1 134 54 62 LEU CA C 56.7 0.2 1 135 54 62 LEU CB C 40.5 0.2 1 136 54 62 LEU N N 121.3 0.2 1 137 55 63 LEU H H 7.73 0.02 1 138 55 63 LEU C C 179.6 0.2 1 139 55 63 LEU CA C 56.5 0.2 1 140 55 63 LEU CB C 41.2 0.2 1 141 55 63 LEU N N 119.6 0.2 1 142 56 64 GLU H H 8.21 0.02 1 143 56 64 GLU C C 177.5 0.2 1 144 56 64 GLU CA C 58.6 0.2 1 145 56 64 GLU CB C 28.9 0.2 1 146 56 64 GLU N N 122.9 0.2 1 147 57 65 ALA H H 7.39 0.02 1 148 57 65 ALA C C 179.2 0.2 1 149 57 65 ALA CA C 53.3 0.2 1 150 57 65 ALA CB C 18.1 0.2 1 151 57 65 ALA N N 119.5 0.2 1 152 58 66 GLN H H 7.69 0.02 1 153 58 66 GLN C C 175.3 0.2 1 154 58 66 GLN CA C 55.2 0.2 1 155 58 66 GLN CB C 29.2 0.2 1 156 58 66 GLN N N 115.1 0.2 1 157 59 67 SER H H 7.83 0.02 1 158 59 67 SER C C 173.1 0.2 1 159 59 67 SER CA C 57.9 0.2 1 160 59 67 SER CB C 66.0 0.2 1 161 59 67 SER N N 116.1 0.2 1 162 60 68 LYS H H 7.61 0.02 1 163 60 68 LYS C C 176.2 0.2 1 164 60 68 LYS CA C 54.4 0.2 1 165 60 68 LYS CB C 30.3 0.2 1 166 60 68 LYS N N 116.2 0.2 1 167 61 69 PHE H H 7.70 0.02 1 168 61 69 PHE C C 175.8 0.2 1 169 61 69 PHE CA C 56.8 0.2 1 170 61 69 PHE CB C 40.6 0.2 1 171 61 69 PHE N N 119.5 0.2 1 172 62 70 THR H H 9.36 0.02 1 173 62 70 THR C C 175.4 0.2 1 174 62 70 THR CA C 60.1 0.2 1 175 62 70 THR CB C 70.6 0.2 1 176 62 70 THR N N 113.3 0.2 1 177 63 71 LYS H H 8.65 0.02 1 178 63 71 LYS C C 178.4 0.2 1 179 63 71 LYS CA C 60.3 0.2 1 180 63 71 LYS CB C 31.3 0.2 1 181 63 71 LYS N N 120.9 0.2 1 182 64 72 LYS H H 8.13 0.02 1 183 64 72 LYS C C 179.2 0.2 1 184 64 72 LYS CA C 58.9 0.2 1 185 64 72 LYS CB C 31.6 0.2 1 186 64 72 LYS N N 118.4 0.2 1 187 65 73 GLU H H 7.62 0.02 1 188 65 73 GLU C C 179.0 0.2 1 189 65 73 GLU CA C 58.9 0.2 1 190 65 73 GLU CB C 28.8 0.2 1 191 65 73 GLU N N 118.7 0.2 1 192 66 74 LEU H H 8.76 0.02 1 193 66 74 LEU C C 178.8 0.2 1 194 66 74 LEU CA C 57.6 0.2 1 195 66 74 LEU CB C 41.4 0.2 1 196 66 74 LEU N N 118.1 0.2 1 197 67 75 GLN H H 8.13 0.02 1 198 67 75 GLN C C 179.2 0.2 1 199 67 75 GLN CA C 58.9 0.2 1 200 67 75 GLN CB C 27.6 0.2 1 201 67 75 GLN N N 118.8 0.2 1 202 68 76 ILE H H 7.69 0.02 1 203 68 76 ILE C C 178.8 0.2 1 204 68 76 ILE CA C 64.6 0.2 1 205 68 76 ILE CB C 37.0 0.2 1 206 68 76 ILE N N 121.6 0.2 1 207 69 77 LEU H H 8.44 0.02 1 208 69 77 LEU C C 178.5 0.2 1 209 69 77 LEU CA C 57.6 0.2 1 210 69 77 LEU CB C 41.0 0.2 1 211 69 77 LEU N N 120.9 0.2 1 212 70 78 TYR H H 8.89 0.02 1 213 70 78 TYR C C 176.7 0.2 1 214 70 78 TYR CA C 60.9 0.2 1 215 70 78 TYR CB C 37.3 0.2 1 216 70 78 TYR N N 120.1 0.2 1 217 71 79 ARG H H 7.78 0.02 1 218 71 79 ARG C C 179.2 0.2 1 219 71 79 ARG CA C 58.8 0.2 1 220 71 79 ARG CB C 28.9 0.2 1 221 71 79 ARG N N 119.1 0.2 1 222 72 80 GLY H H 7.88 0.02 1 223 72 80 GLY C C 175.2 0.2 1 224 72 80 GLY CA C 46.7 0.2 1 225 72 80 GLY N N 105.9 0.2 1 226 73 81 PHE H H 8.42 0.02 1 227 73 81 PHE C C 176.5 0.2 1 228 73 81 PHE CA C 61.1 0.2 1 229 73 81 PHE CB C 39.4 0.2 1 230 73 81 PHE N N 123.7 0.2 1 231 74 82 LYS H H 8.35 0.02 1 232 74 82 LYS C C 178.2 0.2 1 233 74 82 LYS CA C 56.6 0.2 1 234 74 82 LYS CB C 29.9 0.2 1 235 74 82 LYS N N 118.3 0.2 1 236 75 83 ASN H H 7.35 0.02 1 237 75 83 ASN C C 176.7 0.2 1 238 75 83 ASN CA C 55.0 0.2 1 239 75 83 ASN CB C 38.3 0.2 1 240 75 83 ASN N N 116.4 0.2 1 241 76 84 GLU H H 7.25 0.02 1 242 76 84 GLU C C 176.6 0.2 1 243 76 84 GLU CA C 56.0 0.2 1 244 76 84 GLU CB C 29.7 0.2 1 245 76 84 GLU N N 116.5 0.2 1 246 77 85 CYS H H 8.09 0.02 1 247 77 85 CYS CA C 55.1 0.2 1 248 77 85 CYS CB C 26.6 0.2 1 249 77 85 CYS N N 118.6 0.2 1 250 78 86 PRO C C 177.4 0.2 1 251 78 86 PRO CA C 66.3 0.2 1 252 78 86 PRO CB C 30.2 0.2 1 253 79 87 SER H H 7.50 0.02 1 254 79 87 SER C C 176.2 0.2 1 255 79 87 SER CA C 59.0 0.2 1 256 79 87 SER CB C 62.8 0.2 1 257 79 87 SER N N 116.2 0.2 1 258 80 88 GLY H H 8.22 0.02 1 259 80 88 GLY CA C 45.1 0.2 1 260 80 88 GLY N N 110.2 0.2 1 261 92 100 SER C C 176.1 0.2 1 262 92 100 SER CA C 61.3 0.2 1 263 93 101 GLN H H 7.37 0.02 1 264 93 101 GLN C C 177.5 0.2 1 265 93 101 GLN CA C 57.0 0.2 1 266 93 101 GLN CB C 27.8 0.2 1 267 93 101 GLN N N 118.5 0.2 1 268 94 102 PHE H H 7.21 0.02 1 269 94 102 PHE CA C 59.0 0.2 1 270 94 102 PHE N N 118.4 0.2 1 271 96 104 PRO C C 178.2 0.2 1 272 96 104 PRO CA C 64.3 0.2 1 273 97 105 GLN H H 8.70 0.02 1 274 97 105 GLN C C 176.1 0.2 1 275 97 105 GLN CA C 55.7 0.2 1 276 97 105 GLN CB C 28.3 0.2 1 277 97 105 GLN N N 116.9 0.2 1 278 98 106 GLY H H 7.52 0.02 1 279 98 106 GLY C C 172.7 0.2 1 280 98 106 GLY CA C 43.7 0.2 1 281 98 106 GLY N N 108.3 0.2 1 282 99 107 ASP H H 8.01 0.02 1 283 99 107 ASP CA C 52.4 0.2 1 284 99 107 ASP CB C 41.5 0.2 1 285 99 107 ASP N N 120.0 0.2 1 286 100 108 SER C C 174.1 0.2 1 287 100 108 SER CA C 59.2 0.2 1 288 101 109 THR H H 8.27 0.02 1 289 101 109 THR C C 180.0 0.2 1 290 101 109 THR CA C 67.3 0.2 1 291 101 109 THR N N 117.4 0.2 1 292 102 110 THR H H 8.14 0.02 1 293 102 110 THR C C 176.2 0.2 1 294 102 110 THR CA C 65.8 0.2 1 295 102 110 THR CB C 67.9 0.2 1 296 102 110 THR N N 116.2 0.2 1 297 103 111 TYR H H 9.10 0.02 1 298 103 111 TYR CA C 62.6 0.2 1 299 103 111 TYR N N 123.7 0.2 1 300 104 112 ALA H H 8.54 0.02 1 301 104 112 ALA C C 178.7 0.2 1 302 104 112 ALA CA C 55.0 0.2 1 303 104 112 ALA CB C 17.1 0.2 1 304 104 112 ALA N N 118.3 0.2 1 305 105 113 HIS H H 7.43 0.02 1 306 105 113 HIS C C 176.9 0.2 1 307 105 113 HIS CA C 58.9 0.2 1 308 105 113 HIS CB C 27.4 0.2 1 309 105 113 HIS N N 116.8 0.2 1 310 106 114 PHE H H 7.61 0.02 1 311 106 114 PHE C C 179.0 0.2 1 312 106 114 PHE CA C 58.6 0.2 1 313 106 114 PHE CB C 36.7 0.2 1 314 106 114 PHE N N 119.2 0.2 1 315 107 115 LEU H H 8.62 0.02 1 316 107 115 LEU C C 178.3 0.2 1 317 107 115 LEU CA C 56.8 0.2 1 318 107 115 LEU CB C 40.9 0.2 1 319 107 115 LEU N N 121.9 0.2 1 320 108 116 PHE H H 8.73 0.02 1 321 108 116 PHE CA C 62.4 0.2 1 322 108 116 PHE CB C 38.6 0.2 1 323 108 116 PHE N N 121.0 0.2 1 324 109 117 ASN C C 176.3 0.2 1 325 109 117 ASN CA C 55.3 0.2 1 326 109 117 ASN CB C 38.1 0.2 1 327 110 118 ALA H H 7.34 0.02 1 328 110 118 ALA C C 178.7 0.2 1 329 110 118 ALA CA C 53.3 0.2 1 330 110 118 ALA CB C 17.3 0.2 1 331 110 118 ALA N N 121.0 0.2 1 332 111 119 PHE H H 7.39 0.02 1 333 111 119 PHE C C 176.5 0.2 1 334 111 119 PHE CA C 59.7 0.2 1 335 111 119 PHE CB C 40.7 0.2 1 336 111 119 PHE N N 115.2 0.2 1 337 112 120 ASP H H 7.67 0.02 1 338 112 120 ASP CA C 51.4 0.2 1 339 112 120 ASP N N 120.9 0.2 1 340 116 124 ASN C C 177.2 0.2 1 341 116 124 ASN CA C 51.5 0.2 1 342 117 125 GLY H H 10.86 0.02 1 343 117 125 GLY C C 173.5 0.2 1 344 117 125 GLY CA C 45.3 0.2 1 345 117 125 GLY N N 114.7 0.2 1 346 118 126 ALA H H 7.72 0.02 1 347 118 126 ALA CA C 50.7 0.2 1 348 118 126 ALA CB C 21.5 0.2 1 349 118 126 ALA N N 122.2 0.2 1 350 119 127 VAL H H 9.17 0.02 1 351 119 127 VAL C C 173.7 0.2 1 352 119 127 VAL CA C 60.8 0.2 1 353 119 127 VAL N N 129.1 0.2 1 354 120 128 SER H H 9.28 0.02 1 355 120 128 SER C C 174.9 0.2 1 356 120 128 SER CA C 56.0 0.2 1 357 120 128 SER CB C 66.5 0.2 1 358 120 128 SER N N 123.6 0.2 1 359 121 129 PHE H H 9.08 0.02 1 360 121 129 PHE C C 176.6 0.2 1 361 121 129 PHE CA C 61.3 0.2 1 362 121 129 PHE CB C 37.9 0.2 1 363 121 129 PHE N N 121.3 0.2 1 364 122 130 GLU H H 9.06 0.02 1 365 122 130 GLU C C 178.1 0.2 1 366 122 130 GLU CA C 60.1 0.2 1 367 122 130 GLU CB C 28.1 0.2 1 368 122 130 GLU N N 118.3 0.2 1 369 123 131 ASP H H 7.76 0.02 1 370 123 131 ASP CA C 56.9 0.2 1 371 123 131 ASP CB C 41.2 0.2 1 372 123 131 ASP N N 120.1 0.2 1 373 124 132 PHE C C 176.6 0.2 1 374 124 132 PHE CA C 60.1 0.2 1 375 124 132 PHE CB C 38.4 0.2 1 376 125 133 ILE H H 8.45 0.02 1 377 125 133 ILE C C 178.5 0.2 1 378 125 133 ILE CA C 60.8 0.2 1 379 125 133 ILE CB C 33.7 0.2 1 380 125 133 ILE N N 118.8 0.2 1 381 126 134 LYS H H 8.26 0.02 1 382 126 134 LYS C C 179.4 0.2 1 383 126 134 LYS CA C 60.1 0.2 1 384 126 134 LYS CB C 30.9 0.2 1 385 126 134 LYS N N 122.1 0.2 1 386 127 135 GLY H H 7.52 0.02 1 387 127 135 GLY C C 174.3 0.2 1 388 127 135 GLY CA C 46.7 0.2 1 389 127 135 GLY N N 104.7 0.2 1 390 128 136 LEU H H 8.35 0.02 1 391 128 136 LEU C C 178.2 0.2 1 392 128 136 LEU CA C 57.4 0.2 1 393 128 136 LEU CB C 40.9 0.2 1 394 128 136 LEU N N 121.2 0.2 1 395 129 137 SER H H 8.60 0.02 1 396 129 137 SER C C 176.2 0.2 1 397 129 137 SER CA C 61.5 0.2 1 398 129 137 SER CB C 63.0 0.2 1 399 129 137 SER N N 113.0 0.2 1 400 130 138 ILE H H 6.99 0.02 1 401 130 138 ILE C C 177.5 0.2 1 402 130 138 ILE CA C 63.8 0.2 1 403 130 138 ILE N N 119.8 0.2 1 404 131 139 LEU H H 7.33 0.02 1 405 131 139 LEU C C 177.4 0.2 1 406 131 139 LEU CA C 57.0 0.2 1 407 131 139 LEU CB C 40.8 0.2 1 408 131 139 LEU N N 116.1 0.2 1 409 132 140 LEU H H 8.24 0.02 1 410 132 140 LEU CA C 55.4 0.2 1 411 132 140 LEU CB C 40.8 0.2 1 412 132 140 LEU N N 113.1 0.2 1 413 133 141 ARG C C 176.3 0.2 1 414 133 141 ARG CA C 54.8 0.2 1 415 133 141 ARG CB C 31.2 0.2 1 416 134 142 GLY H H 7.49 0.02 1 417 134 142 GLY C C 174.5 0.2 1 418 134 142 GLY CA C 44.5 0.2 1 419 134 142 GLY N N 110.1 0.2 1 420 135 143 THR H H 8.88 0.02 1 421 135 143 THR C C 176.1 0.2 1 422 135 143 THR CA C 60.7 0.2 1 423 135 143 THR CB C 70.4 0.2 1 424 135 143 THR N N 111.7 0.2 1 425 136 144 VAL H H 8.83 0.02 1 426 136 144 VAL C C 177.6 0.2 1 427 136 144 VAL CA C 66.8 0.2 1 428 136 144 VAL CB C 30.7 0.2 1 429 136 144 VAL N N 121.3 0.2 1 430 137 145 GLN H H 8.29 0.02 1 431 137 145 GLN C C 178.7 0.2 1 432 137 145 GLN CA C 60.3 0.2 1 433 137 145 GLN CB C 26.4 0.2 1 434 137 145 GLN N N 118.3 0.2 1 435 138 146 GLU H H 7.72 0.02 1 436 138 146 GLU C C 180.3 0.2 1 437 138 146 GLU CA C 59.1 0.2 1 438 138 146 GLU CB C 28.6 0.2 1 439 138 146 GLU N N 120.4 0.2 1 440 139 147 LYS H H 8.34 0.02 1 441 139 147 LYS C C 178.8 0.2 1 442 139 147 LYS CA C 60.1 0.2 1 443 139 147 LYS CB C 32.6 0.2 1 444 139 147 LYS N N 120.9 0.2 1 445 140 148 LEU H H 8.54 0.02 1 446 140 148 LEU C C 179.2 0.2 1 447 140 148 LEU CA C 57.1 0.2 1 448 140 148 LEU CB C 41.1 0.2 1 449 140 148 LEU N N 118.6 0.2 1 450 141 149 ASN H H 8.25 0.02 1 451 141 149 ASN C C 177.0 0.2 1 452 141 149 ASN CA C 56.6 0.2 1 453 141 149 ASN CB C 38.7 0.2 1 454 141 149 ASN N N 119.4 0.2 1 455 142 150 TRP H H 7.89 0.02 1 456 142 150 TRP C C 179.3 0.2 1 457 142 150 TRP CA C 62.1 0.2 1 458 142 150 TRP CB C 29.3 0.2 1 459 142 150 TRP N N 122.2 0.2 1 460 143 151 ALA H H 8.64 0.02 1 461 143 151 ALA C C 177.3 0.2 1 462 143 151 ALA CA C 54.6 0.2 1 463 143 151 ALA CB C 18.0 0.2 1 464 143 151 ALA N N 121.2 0.2 1 465 144 152 PHE H H 8.21 0.02 1 466 144 152 PHE C C 175.7 0.2 1 467 144 152 PHE CA C 61.4 0.2 1 468 144 152 PHE CB C 37.7 0.2 1 469 144 152 PHE N N 118.1 0.2 1 470 145 153 ASN H H 7.18 0.02 1 471 145 153 ASN C C 175.3 0.2 1 472 145 153 ASN CA C 55.0 0.2 1 473 145 153 ASN CB C 38.2 0.2 1 474 145 153 ASN N N 114.0 0.2 1 475 146 154 LEU H H 6.97 0.02 1 476 146 154 LEU C C 177.0 0.2 1 477 146 154 LEU CA C 56.8 0.2 1 478 146 154 LEU CB C 39.3 0.2 1 479 146 154 LEU N N 120.4 0.2 1 480 147 155 TYR H H 6.70 0.02 1 481 147 155 TYR C C 175.4 0.2 1 482 147 155 TYR CA C 58.4 0.2 1 483 147 155 TYR CB C 37.8 0.2 1 484 147 155 TYR N N 114.4 0.2 1 485 148 156 ASP H H 7.33 0.02 1 486 148 156 ASP C C 178.0 0.2 1 487 148 156 ASP CA C 50.8 0.2 1 488 148 156 ASP CB C 37.8 0.2 1 489 148 156 ASP N N 114.2 0.2 1 490 149 157 ILE H H 7.56 0.02 1 491 149 157 ILE C C 178.0 0.2 1 492 149 157 ILE CA C 65.1 0.2 1 493 149 157 ILE CB C 38.0 0.2 1 494 149 157 ILE N N 127.3 0.2 1 495 150 158 ASN H H 7.97 0.02 1 496 150 158 ASN C C 175.0 0.2 1 497 150 158 ASN CA C 51.6 0.2 1 498 150 158 ASN CB C 36.8 0.2 1 499 150 158 ASN N N 114.7 0.2 1 500 151 159 LYS H H 7.74 0.02 1 501 151 159 LYS C C 176.2 0.2 1 502 151 159 LYS CA C 55.3 0.2 1 503 151 159 LYS CB C 27.2 0.2 1 504 151 159 LYS N N 116.1 0.2 1 505 152 160 ASP H H 8.15 0.02 1 506 152 160 ASP C C 177.2 0.2 1 507 152 160 ASP CA C 52.6 0.2 1 508 152 160 ASP CB C 40.4 0.2 1 509 152 160 ASP N N 119.1 0.2 1 510 153 161 GLY H H 10.49 0.02 1 511 153 161 GLY C C 172.8 0.2 1 512 153 161 GLY CA C 44.3 0.2 1 513 153 161 GLY N N 112.9 0.2 1 514 154 162 TYR H H 8.02 0.02 1 515 154 162 TYR C C 175.4 0.2 1 516 154 162 TYR CA C 54.9 0.2 1 517 154 162 TYR CB C 40.2 0.2 1 518 154 162 TYR N N 118.3 0.2 1 519 155 163 ILE H H 9.64 0.02 1 520 155 163 ILE C C 177.1 0.2 1 521 155 163 ILE CA C 61.2 0.2 1 522 155 163 ILE CB C 38.9 0.2 1 523 155 163 ILE N N 126.5 0.2 1 524 156 164 THR H H 8.48 0.02 1 525 156 164 THR C C 176.1 0.2 1 526 156 164 THR CA C 59.1 0.2 1 527 156 164 THR CB C 71.2 0.2 1 528 156 164 THR N N 117.8 0.2 1 529 157 165 LYS H H 9.00 0.02 1 530 157 165 LYS C C 178.7 0.2 1 531 157 165 LYS CA C 60.0 0.2 1 532 157 165 LYS CB C 30.7 0.2 1 533 157 165 LYS N N 122.9 0.2 1 534 158 166 GLU H H 8.34 0.02 1 535 158 166 GLU C C 178.9 0.2 1 536 158 166 GLU CA C 59.9 0.2 1 537 158 166 GLU CB C 27.8 0.2 1 538 158 166 GLU N N 118.2 0.2 1 539 159 167 GLU H H 7.52 0.02 1 540 159 167 GLU C C 178.3 0.2 1 541 159 167 GLU CA C 58.9 0.2 1 542 159 167 GLU CB C 27.9 0.2 1 543 159 167 GLU N N 120.3 0.2 1 544 160 168 MET H H 7.76 0.02 1 545 160 168 MET C C 178.6 0.2 1 546 160 168 MET CA C 56.6 0.2 1 547 160 168 MET CB C 30.1 0.2 1 548 160 168 MET N N 116.0 0.2 1 549 161 169 LEU H H 8.52 0.02 1 550 161 169 LEU CA C 57.6 0.2 1 551 161 169 LEU CB C 40.1 0.2 1 552 161 169 LEU N N 121.5 0.2 1 553 164 172 MET C C 179.6 0.2 1 554 165 173 LYS H H 9.07 0.02 1 555 165 173 LYS C C 178.0 0.2 1 556 165 173 LYS CA C 59.6 0.2 1 557 165 173 LYS CB C 31.2 0.2 1 558 165 173 LYS N N 121.8 0.2 1 559 166 174 ALA H H 7.74 0.02 1 560 166 174 ALA C C 181.4 0.2 1 561 166 174 ALA CA C 54.4 0.2 1 562 166 174 ALA CB C 17.4 0.2 1 563 166 174 ALA N N 121.3 0.2 1 564 167 175 ILE H H 8.20 0.02 1 565 167 175 ILE N N 120.7 0.2 1 566 170 178 MET C C 176.0 0.2 1 567 170 178 MET CA C 58.6 0.2 1 568 170 178 MET CB C 27.3 0.2 1 569 171 179 MET H H 8.02 0.02 1 570 171 179 MET C C 177.6 0.2 1 571 171 179 MET CA C 56.1 0.2 1 572 171 179 MET CB C 33.0 0.2 1 573 171 179 MET N N 113.0 0.2 1 574 172 180 GLY H H 8.06 0.02 1 575 172 180 GLY C C 174.1 0.2 1 576 172 180 GLY CA C 46.3 0.2 1 577 172 180 GLY N N 108.7 0.2 1 578 173 181 LYS H H 8.06 0.02 1 579 173 181 LYS CA C 58.6 0.2 1 580 173 181 LYS N N 118.5 0.2 1 581 177 185 PRO C C 175.7 0.2 1 582 177 185 PRO CA C 62.3 0.2 1 583 177 185 PRO CB C 33.0 0.2 1 584 178 186 VAL H H 8.16 0.02 1 585 178 186 VAL C C 176.5 0.2 1 586 178 186 VAL CA C 62.7 0.2 1 587 178 186 VAL CB C 31.5 0.2 1 588 178 186 VAL N N 121.9 0.2 1 589 179 187 LEU H H 8.27 0.02 1 590 179 187 LEU C C 177.2 0.2 1 591 179 187 LEU CA C 54.1 0.2 1 592 179 187 LEU CB C 41.4 0.2 1 593 179 187 LEU N N 126.3 0.2 1 594 180 188 LYS H H 8.45 0.02 1 595 180 188 LYS C C 177.6 0.2 1 596 180 188 LYS CA C 55.9 0.2 1 597 180 188 LYS CB C 32.3 0.2 1 598 180 188 LYS N N 123.3 0.2 1 599 181 189 GLU H H 8.60 0.02 1 600 181 189 GLU C C 176.4 0.2 1 601 181 189 GLU CA C 57.9 0.2 1 602 181 189 GLU N N 119.8 0.2 1 603 182 190 ASP H H 8.05 0.02 1 604 182 190 ASP C C 176.2 0.2 1 605 182 190 ASP CA C 53.5 0.2 1 606 182 190 ASP CB C 40.3 0.2 1 607 182 190 ASP N N 117.6 0.2 1 608 183 191 ALA H H 7.86 0.02 1 609 183 191 ALA CA C 54.9 0.2 1 610 183 191 ALA CB C 16.3 0.2 1 611 183 191 ALA N N 123.3 0.2 1 612 187 195 HIS C C 178.9 0.2 1 613 187 195 HIS CA C 58.9 0.2 1 614 188 196 VAL H H 8.02 0.02 1 615 188 196 VAL C C 177.5 0.2 1 616 188 196 VAL CA C 66.8 0.2 1 617 188 196 VAL CB C 30.2 0.2 1 618 188 196 VAL N N 120.5 0.2 1 619 189 197 GLU H H 8.19 0.02 1 620 189 197 GLU C C 179.9 0.2 1 621 189 197 GLU CA C 59.2 0.2 1 622 189 197 GLU CB C 28.3 0.2 1 623 189 197 GLU N N 120.0 0.2 1 624 190 198 THR H H 8.23 0.02 1 625 190 198 THR C C 176.2 0.2 1 626 190 198 THR CA C 65.9 0.2 1 627 190 198 THR CB C 68.0 0.2 1 628 190 198 THR N N 116.4 0.2 1 629 191 199 PHE H H 8.17 0.02 1 630 191 199 PHE C C 177.2 0.2 1 631 191 199 PHE CA C 60.7 0.2 1 632 191 199 PHE N N 123.8 0.2 1 633 192 200 PHE H H 8.94 0.02 1 634 192 200 PHE CA C 63.1 0.2 1 635 192 200 PHE CB C 38.1 0.2 1 636 192 200 PHE N N 119.0 0.2 1 637 193 201 GLN C C 178.3 0.2 1 638 193 201 GLN CA C 58.5 0.2 1 639 193 201 GLN CB C 27.5 0.2 1 640 194 202 LYS H H 7.49 0.02 1 641 194 202 LYS C C 177.9 0.2 1 642 194 202 LYS CA C 58.1 0.2 1 643 194 202 LYS CB C 32.3 0.2 1 644 194 202 LYS N N 117.0 0.2 1 645 195 203 MET H H 7.70 0.02 1 646 195 203 MET C C 176.6 0.2 1 647 195 203 MET CA C 55.8 0.2 1 648 195 203 MET CB C 34.2 0.2 1 649 195 203 MET N N 114.1 0.2 1 650 196 204 ASP H H 7.71 0.02 1 651 196 204 ASP C C 178.0 0.2 1 652 196 204 ASP CA C 51.9 0.2 1 653 196 204 ASP CB C 38.1 0.2 1 654 196 204 ASP N N 115.4 0.2 1 655 197 205 LYS H H 7.53 0.02 1 656 197 205 LYS C C 177.7 0.2 1 657 197 205 LYS CA C 58.8 0.2 1 658 197 205 LYS CB C 32.3 0.2 1 659 197 205 LYS N N 128.8 0.2 1 660 198 206 ASN H H 7.97 0.02 1 661 198 206 ASN C C 174.8 0.2 1 662 198 206 ASN CA C 51.3 0.2 1 663 198 206 ASN CB C 36.3 0.2 1 664 198 206 ASN N N 113.2 0.2 1 665 199 207 LYS H H 7.66 0.02 1 666 199 207 LYS C C 175.9 0.2 1 667 199 207 LYS CA C 56.9 0.2 1 668 199 207 LYS CB C 28.4 0.2 1 669 199 207 LYS N N 116.0 0.2 1 670 200 208 ASP H H 8.17 0.02 1 671 200 208 ASP C C 178.0 0.2 1 672 200 208 ASP CA C 52.8 0.2 1 673 200 208 ASP CB C 40.4 0.2 1 674 200 208 ASP N N 118.7 0.2 1 675 201 209 GLY H H 10.36 0.02 1 676 201 209 GLY C C 173.3 0.2 1 677 201 209 GLY CA C 45.0 0.2 1 678 201 209 GLY N N 113.3 0.2 1 679 202 210 VAL H H 7.89 0.02 1 680 202 210 VAL C C 174.9 0.2 1 681 202 210 VAL CA C 58.6 0.2 1 682 202 210 VAL CB C 35.8 0.2 1 683 202 210 VAL N N 112.7 0.2 1 684 203 211 VAL H H 9.18 0.02 1 685 203 211 VAL C C 176.5 0.2 1 686 203 211 VAL CA C 60.6 0.2 1 687 203 211 VAL CB C 33.1 0.2 1 688 203 211 VAL N N 126.4 0.2 1 689 204 212 THR H H 8.52 0.02 1 690 204 212 THR C C 176.8 0.2 1 691 204 212 THR CA C 59.9 0.2 1 692 204 212 THR CB C 70.8 0.2 1 693 204 212 THR N N 118.5 0.2 1 694 205 213 ILE H H 8.82 0.02 1 695 205 213 ILE C C 175.5 0.2 1 696 205 213 ILE CA C 62.9 0.2 1 697 205 213 ILE CB C 36.0 0.2 1 698 205 213 ILE N N 123.1 0.2 1 699 206 214 ASP H H 7.97 0.02 1 700 206 214 ASP C C 179.3 0.2 1 701 206 214 ASP CA C 56.2 0.2 1 702 206 214 ASP CB C 39.4 0.2 1 703 206 214 ASP N N 119.8 0.2 1 704 207 215 GLU H H 7.17 0.02 1 705 207 215 GLU C C 178.9 0.2 1 706 207 215 GLU CA C 58.6 0.2 1 707 207 215 GLU CB C 28.7 0.2 1 708 207 215 GLU N N 120.4 0.2 1 709 208 216 PHE H H 8.55 0.02 1 710 208 216 PHE C C 177.3 0.2 1 711 208 216 PHE CA C 60.5 0.2 1 712 208 216 PHE CB C 40.5 0.2 1 713 208 216 PHE N N 122.2 0.2 1 714 209 217 ILE H H 8.93 0.02 1 715 209 217 ILE C C 178.1 0.2 1 716 209 217 ILE CA C 65.1 0.2 1 717 209 217 ILE CB C 36.5 0.2 1 718 209 217 ILE N N 119.3 0.2 1 719 210 218 GLU H H 7.64 0.02 1 720 210 218 GLU C C 179.2 0.2 1 721 210 218 GLU CA C 59.0 0.2 1 722 210 218 GLU CB C 28.6 0.2 1 723 210 218 GLU N N 118.4 0.2 1 724 211 219 SER H H 7.94 0.02 1 725 211 219 SER C C 177.6 0.2 1 726 211 219 SER CA C 61.4 0.2 1 727 211 219 SER CB C 62.9 0.2 1 728 211 219 SER N N 113.0 0.2 1 729 212 220 CYS H H 8.01 0.02 1 730 212 220 CYS C C 176.3 0.2 1 731 212 220 CYS CA C 64.3 0.2 1 732 212 220 CYS CB C 27.9 0.2 1 733 212 220 CYS N N 118.7 0.2 1 734 213 221 GLN H H 7.63 0.02 1 735 213 221 GLN C C 177.5 0.2 1 736 213 221 GLN CA C 57.6 0.2 1 737 213 221 GLN CB C 28.3 0.2 1 738 213 221 GLN N N 113.4 0.2 1 739 214 222 LYS H H 7.03 0.02 1 740 214 222 LYS C C 174.9 0.2 1 741 214 222 LYS CA C 55.4 0.2 1 742 214 222 LYS CB C 31.8 0.2 1 743 214 222 LYS N N 116.1 0.2 1 744 215 223 ASP H H 7.35 0.02 1 745 215 223 ASP C C 174.8 0.2 1 746 215 223 ASP CA C 52.9 0.2 1 747 215 223 ASP CB C 42.6 0.2 1 748 215 223 ASP N N 122.9 0.2 1 749 216 224 GLU H H 8.88 0.02 1 750 216 224 GLU C C 178.8 0.2 1 751 216 224 GLU CA C 58.9 0.2 1 752 216 224 GLU CB C 28.6 0.2 1 753 216 224 GLU N N 126.9 0.2 1 754 217 225 ASN H H 8.22 0.02 1 755 217 225 ASN C C 178.8 0.2 1 756 217 225 ASN CA C 55.9 0.2 1 757 217 225 ASN CB C 37.7 0.2 1 758 217 225 ASN N N 118.2 0.2 1 759 218 226 ILE H H 8.68 0.02 1 760 218 226 ILE C C 179.2 0.2 1 761 218 226 ILE CA C 65.5 0.2 1 762 218 226 ILE CB C 36.7 0.2 1 763 218 226 ILE N N 125.1 0.2 1 764 219 227 MET H H 8.26 0.02 1 765 219 227 MET C C 179.9 0.2 1 766 219 227 MET CA C 56.9 0.2 1 767 219 227 MET CB C 29.7 0.2 1 768 219 227 MET N N 118.5 0.2 1 769 220 228 ARG H H 8.25 0.02 1 770 220 228 ARG C C 179.9 0.2 1 771 220 228 ARG CA C 58.9 0.2 1 772 220 228 ARG CB C 29.2 0.2 1 773 220 228 ARG N N 120.9 0.2 1 774 221 229 SER H H 7.93 0.02 1 775 221 229 SER C C 175.2 0.2 1 776 221 229 SER CA C 61.7 0.2 1 777 221 229 SER N N 117.2 0.2 1 778 222 230 MET H H 7.66 0.02 1 779 222 230 MET C C 178.9 0.2 1 780 222 230 MET CA C 55.7 0.2 1 781 222 230 MET CB C 30.3 0.2 1 782 222 230 MET N N 117.6 0.2 1 783 223 231 GLN H H 7.83 0.02 1 784 223 231 GLN C C 177.4 0.2 1 785 223 231 GLN CA C 57.1 0.2 1 786 223 231 GLN CB C 27.9 0.2 1 787 223 231 GLN N N 119.9 0.2 1 788 224 232 LEU H H 7.51 0.02 1 789 224 232 LEU CA C 56.9 0.2 1 790 224 232 LEU CB C 41.0 0.2 1 791 224 232 LEU N N 120.6 0.2 1 792 227 235 ASN C C 174.8 0.2 1 793 227 235 ASN CA C 53.1 0.2 1 794 227 235 ASN CB C 38.1 0.2 1 795 228 236 VAL H H 8.05 0.02 1 796 228 236 VAL CA C 63.8 0.2 1 797 228 236 VAL N N 119.9 0.2 1 798 229 237 ILE H H 7.42 0.02 1 799 229 237 ILE N N 122.9 0.2 1 stop_ save_