data_7216 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for yeast triosephosphate isomerase, TIM ; _BMRB_accession_number 7216 _BMRB_flat_file_name bmr7216.str _Entry_type original _Submission_date 2006-07-06 _Accession_date 2006-07-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'mutation: W90Y W157F' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Loria J. Patrick . 2 Wang Chunyu . . 3 Massi Francesca . . 4 Rance Mark . . 5 Palmer Arthur G. III stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 "13C chemical shifts" 599 "15N chemical shifts" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-08-28 update author 'update chemical shifts' 2006-08-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone 1H, 13C, and 15N Chemical Shift Assignments for yeast triosephosphate isomerase, TIM' _Citation_status 'in preparation' _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Loria J. Patrick . 2 Wang Chunyu . . 3 Massi Francesca . . 4 Rance Mark . . 5 Palmer Arthur G. III stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Triosephosphate isomerase' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Triosephosphate isomerase, chain 1' $TIM 'Triosephosphate isomerase, chain 2' $TIM stop_ _System_molecular_weight 53466 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details 'symmetric dimer' save_ ######################## # Monomeric polymers # ######################## save_TIM _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Triosephosphate isomerase' _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'triose-phosphate isomerase activity' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 248 _Mol_residue_sequence ; MARTFFVGGNFKLNGSKQSI KEIVERLNTASIPENVEVVI CPPATYLDYSVSLVKKPQVT VGAQNAYLKASGAFTGENSV DQIKDVGAKYVILGHSERRS YFHEDDKFIADKTKFALGQG VGVILCIGETLEEKKAGKTL DVVERQLNAVLEEVKDFTNV VVAYEPVWAIGTGLAATPED AQDIHASIRKFLASKLGDKA ASELRILYGGSANGSNAVTF KDKADVDGFLVGGASLKPEF VDIINSRN ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ARG 4 THR 5 PHE 6 PHE 7 VAL 8 GLY 9 GLY 10 ASN 11 PHE 12 LYS 13 LEU 14 ASN 15 GLY 16 SER 17 LYS 18 GLN 19 SER 20 ILE 21 LYS 22 GLU 23 ILE 24 VAL 25 GLU 26 ARG 27 LEU 28 ASN 29 THR 30 ALA 31 SER 32 ILE 33 PRO 34 GLU 35 ASN 36 VAL 37 GLU 38 VAL 39 VAL 40 ILE 41 CYS 42 PRO 43 PRO 44 ALA 45 THR 46 TYR 47 LEU 48 ASP 49 TYR 50 SER 51 VAL 52 SER 53 LEU 54 VAL 55 LYS 56 LYS 57 PRO 58 GLN 59 VAL 60 THR 61 VAL 62 GLY 63 ALA 64 GLN 65 ASN 66 ALA 67 TYR 68 LEU 69 LYS 70 ALA 71 SER 72 GLY 73 ALA 74 PHE 75 THR 76 GLY 77 GLU 78 ASN 79 SER 80 VAL 81 ASP 82 GLN 83 ILE 84 LYS 85 ASP 86 VAL 87 GLY 88 ALA 89 LYS 90 TYR 91 VAL 92 ILE 93 LEU 94 GLY 95 HIS 96 SER 97 GLU 98 ARG 99 ARG 100 SER 101 TYR 102 PHE 103 HIS 104 GLU 105 ASP 106 ASP 107 LYS 108 PHE 109 ILE 110 ALA 111 ASP 112 LYS 113 THR 114 LYS 115 PHE 116 ALA 117 LEU 118 GLY 119 GLN 120 GLY 121 VAL 122 GLY 123 VAL 124 ILE 125 LEU 126 CYS 127 ILE 128 GLY 129 GLU 130 THR 131 LEU 132 GLU 133 GLU 134 LYS 135 LYS 136 ALA 137 GLY 138 LYS 139 THR 140 LEU 141 ASP 142 VAL 143 VAL 144 GLU 145 ARG 146 GLN 147 LEU 148 ASN 149 ALA 150 VAL 151 LEU 152 GLU 153 GLU 154 VAL 155 LYS 156 ASP 157 PHE 158 THR 159 ASN 160 VAL 161 VAL 162 VAL 163 ALA 164 TYR 165 GLU 166 PRO 167 VAL 168 TRP 169 ALA 170 ILE 171 GLY 172 THR 173 GLY 174 LEU 175 ALA 176 ALA 177 THR 178 PRO 179 GLU 180 ASP 181 ALA 182 GLN 183 ASP 184 ILE 185 HIS 186 ALA 187 SER 188 ILE 189 ARG 190 LYS 191 PHE 192 LEU 193 ALA 194 SER 195 LYS 196 LEU 197 GLY 198 ASP 199 LYS 200 ALA 201 ALA 202 SER 203 GLU 204 LEU 205 ARG 206 ILE 207 LEU 208 TYR 209 GLY 210 GLY 211 SER 212 ALA 213 ASN 214 GLY 215 SER 216 ASN 217 ALA 218 VAL 219 THR 220 PHE 221 LYS 222 ASP 223 LYS 224 ALA 225 ASP 226 VAL 227 ASP 228 GLY 229 PHE 230 LEU 231 VAL 232 GLY 233 GLY 234 ALA 235 SER 236 LEU 237 LYS 238 PRO 239 GLU 240 PHE 241 VAL 242 ASP 243 ILE 244 ILE 245 ASN 246 SER 247 ARG 248 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-25 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 16565 WT_yeast_TIM_homodimer 100.00 248 99.19 100.00 3.47e-177 BMRB 16566 WT_yeast_TIM_homodimer 100.00 248 99.19 100.00 3.47e-177 BMRB 17122 TIM 99.60 247 99.60 99.60 1.28e-176 PDB 1I45 "Yeast Triosephosphate Isomerase (Mutant)" 100.00 248 99.60 99.60 1.07e-176 PDB 1NEY "Triosephosphate Isomerase In Complex With Dhap" 99.60 247 99.60 99.60 1.47e-175 PDB 1NF0 "Triosephosphate Isomerase In Complex With Dhap" 99.60 247 99.60 99.60 1.47e-175 PDB 1YPI "Structure Of Yeast Triosephosphate Isomerase At 1.9- Angstroms Resolution" 99.60 247 99.19 100.00 5.27e-176 PDB 2YPI "Crystallographic Analysis Of The Complex Between Triosephosphate Isomerase And 2-Phosphoglycolate At 2.5- Angstroms Resolution." 99.60 247 99.19 100.00 5.27e-176 PDB 3YPI "Electrophilic Catalysis In Triosephosphase Isomerase: The Role Of Histidine-95" 99.60 247 98.79 99.60 7.77e-175 PDB 4FF7 "Structure Of C126s Mutant Of Saccharomyces Cerevisiae Triosephosphate Isomerase" 100.00 248 98.79 99.60 7.75e-176 PDB 7TIM "Structure Of The Triosephosphate Isomerase- Phosphoglycolohydroxamate Complex: An Analogue Of The Intermediate On The Reaction " 99.60 247 99.19 100.00 5.27e-176 DBJ GAA22287 "K7_Tpi1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 248 99.19 100.00 3.47e-177 EMBL CAA89080 "Tpi1p [Saccharomyces cerevisiae]" 100.00 248 99.19 100.00 3.47e-177 EMBL CAY78558 "Tpi1p [Saccharomyces cerevisiae EC1118]" 100.00 248 99.19 100.00 3.47e-177 GB AAA88757 "triose phosphate isomerase [Saccharomyces cerevisiae]" 100.00 248 99.19 100.00 3.47e-177 GB AAS55980 "YDR050C [Saccharomyces cerevisiae]" 100.00 248 99.19 100.00 3.47e-177 GB AHY75046 "Tpi1p [Saccharomyces cerevisiae YJM993]" 100.00 248 99.19 100.00 3.47e-177 GB EDN60396 "triosephosphate isomerase [Saccharomyces cerevisiae YJM789]" 100.00 248 99.19 100.00 3.47e-177 GB EDV08247 "triosephosphate isomerase [Saccharomyces cerevisiae RM11-1a]" 100.00 248 99.19 100.00 3.47e-177 REF NP_010335 "triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288c]" 100.00 248 99.19 100.00 3.47e-177 SP P00942 "RecName: Full=Triosephosphate isomerase; Short=TIM; AltName: Full=Triose-phosphate isomerase [Saccharomyces cerevisiae S288c]" 100.00 248 99.19 100.00 3.47e-177 TPG DAA11897 "TPA: triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288c]" 100.00 248 99.19 100.00 3.47e-177 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TIM 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $TIM 'recombinant technology' 'Escherichia coli' . . . . 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 $TIM 0.9 mM '[U-99% 13C; U-99% 15N; U-80% 2H]' 'Sodium acetate' 10 mM [U-2H] DTT 1 mM . 'Sodium azide' 0.02 % . stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_1H-15N_TROSY _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(CA)CO _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_HN(CO)CACB _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.9 0.1 pH temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 H2O C 13 protons ppm 4.806 internal indirect . . . 0.25144952 $citation_1 $citation_1 H20 H 1 protons ppm 4.806 internal direct . . . 1.0 $citation_1 $citation_1 H2O N 15 protons ppm 4.806 internal indirect . . . 0.10132905 $citation_1 $citation_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '1H-15N TROSY' HNCO HN(CA)CO HNCA HN(CO)CA HNCACB HN(CO)CACB stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'Triosephosphate isomerase, chain 1' _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 4 4 THR H H 9.06 0.02 1 2 4 4 THR C C 173.7 0.1 1 3 4 4 THR CA C 64.0 0.1 1 4 4 4 THR CB C 69.7 0.2 1 5 4 4 THR N N 125.0 0.1 1 6 5 5 PHE H H 8.65 0.02 1 7 5 5 PHE C C 173.0 0.1 1 8 5 5 PHE CA C 57.5 0.1 1 9 5 5 PHE CB C 39.8 0.2 1 10 5 5 PHE N N 131.4 0.1 1 11 6 6 PHE H H 7.53 0.02 1 12 6 6 PHE C C 174.3 0.1 1 13 6 6 PHE CA C 54.8 0.1 1 14 6 6 PHE CB C 41.7 0.2 1 15 6 6 PHE N N 130.3 0.1 1 16 8 8 GLY C C 173.3 0.1 1 17 8 8 GLY CA C 43.7 0.1 1 18 9 9 GLY H H 9.71 0.02 1 19 9 9 GLY C C 171.8 0.1 1 20 9 9 GLY CA C 46.6 0.1 1 21 9 9 GLY N N 113.5 0.1 1 22 10 10 ASN H H 9.16 0.02 1 23 10 10 ASN C C 173.7 0.1 1 24 10 10 ASN CA C 51.3 0.1 1 25 10 10 ASN CB C 37.8 0.2 1 26 10 10 ASN N N 124.3 0.1 1 27 11 11 PHE C C 175.8 0.1 1 28 11 11 PHE CA C 56.4 0.1 1 29 11 11 PHE CB C 37.1 0.2 1 30 12 12 LYS H H 8.00 0.02 1 31 12 12 LYS C C 175.5 0.1 1 32 12 12 LYS CA C 57.4 0.1 1 33 12 12 LYS CB C 30.9 0.2 1 34 12 12 LYS N N 116.7 0.1 1 35 13 13 LEU H H 7.83 0.02 1 36 13 13 LEU C C 174.7 0.1 1 37 13 13 LEU CA C 51.9 0.1 1 38 13 13 LEU CB C 41.6 0.2 1 39 13 13 LEU N N 127.1 0.1 1 40 14 14 ASN H H 7.60 0.02 1 41 14 14 ASN C C 172.8 0.1 1 42 14 14 ASN CA C 52.9 0.1 1 43 14 14 ASN CB C 44.2 0.2 1 44 14 14 ASN N N 117.8 0.1 1 45 15 15 GLY H H 8.30 0.02 1 46 15 15 GLY C C 171.2 0.1 1 47 15 15 GLY CA C 43.3 0.1 1 48 15 15 GLY N N 106.5 0.1 1 49 16 16 SER H H 7.43 0.02 1 50 16 16 SER C C 174.2 0.1 1 51 16 16 SER CA C 55.3 0.1 1 52 16 16 SER CB C 67.1 0.2 1 53 16 16 SER N N 114.3 0.1 1 54 17 17 LYS H H 10.13 0.02 1 55 17 17 LYS C C 179.8 0.1 1 56 17 17 LYS CA C 62.0 0.1 1 57 17 17 LYS CB C 30.8 0.2 1 58 17 17 LYS N N 124.4 0.1 1 59 18 18 GLN H H 8.31 0.02 1 60 18 18 GLN C C 178.6 0.1 1 61 18 18 GLN CA C 58.7 0.1 1 62 18 18 GLN CB C 28.4 0.2 1 63 18 18 GLN N N 118.3 0.1 1 64 19 19 SER H H 8.03 0.02 1 65 19 19 SER C C 177.9 0.1 1 66 19 19 SER CA C 60.6 0.1 1 67 19 19 SER CB C 62.7 0.2 1 68 19 19 SER N N 117.6 0.1 1 69 20 20 ILE H H 8.69 0.02 1 70 20 20 ILE C C 177.3 0.1 1 71 20 20 ILE CA C 65.1 0.1 1 72 20 20 ILE CB C 36.5 0.2 1 73 20 20 ILE N N 125.5 0.1 1 74 21 21 LYS H H 7.79 0.02 1 75 21 21 LYS C C 177.9 0.1 1 76 21 21 LYS CA C 60.0 0.1 1 77 21 21 LYS CB C 31.4 0.2 1 78 21 21 LYS N N 121.6 0.1 1 79 22 22 GLU H H 7.09 0.02 1 80 22 22 GLU C C 179.7 0.1 1 81 22 22 GLU CA C 59.1 0.1 1 82 22 22 GLU CB C 29.4 0.2 1 83 22 22 GLU N N 117.2 0.1 1 84 23 23 ILE H H 7.88 0.02 1 85 23 23 ILE C C 178.8 0.1 1 86 23 23 ILE CA C 64.9 0.1 1 87 23 23 ILE CB C 39.0 0.2 1 88 23 23 ILE N N 120.7 0.1 1 89 27 27 LEU C C 178.1 0.1 1 90 27 27 LEU CA C 57.6 0.1 1 91 27 27 LEU CB C 41.5 0.2 1 92 28 28 ASN H H 8.53 0.02 1 93 28 28 ASN C C 178.2 0.1 1 94 28 28 ASN CA C 54.9 0.1 1 95 28 28 ASN CB C 38.5 0.2 1 96 28 28 ASN N N 115.9 0.1 1 97 29 29 THR H H 7.56 0.02 1 98 29 29 THR C C 174.7 0.1 1 99 29 29 THR CA C 61.8 0.1 1 100 29 29 THR CB C 70.5 0.2 1 101 29 29 THR N N 109.8 0.1 1 102 30 30 ALA H H 7.62 0.02 1 103 30 30 ALA C C 177.1 0.1 1 104 30 30 ALA CA C 51.8 0.1 1 105 30 30 ALA CB C 20.1 0.2 1 106 30 30 ALA N N 127.3 0.1 1 107 31 31 SER H H 8.38 0.02 1 108 31 31 SER C C 174.0 0.1 1 109 31 31 SER CA C 57.4 0.1 1 110 31 31 SER CB C 62.9 0.2 1 111 31 31 SER N N 116.7 0.1 1 112 32 32 ILE H H 7.80 0.02 1 113 32 32 ILE C C 173.5 0.1 1 114 32 32 ILE CA C 57.6 0.1 1 115 32 32 ILE CB C 39.6 0.2 1 116 32 32 ILE N N 124.1 0.1 1 117 33 33 PRO C C 176.9 0.1 1 118 33 33 PRO CA C 62.4 0.1 1 119 33 33 PRO CB C 32.2 0.2 1 120 34 34 GLU H H 8.52 0.02 1 121 34 34 GLU C C 177.2 0.1 1 122 34 34 GLU CA C 57.9 0.1 1 123 34 34 GLU CB C 29.8 0.2 1 124 34 34 GLU N N 118.9 0.1 1 125 35 35 ASN H H 8.16 0.02 1 126 35 35 ASN C C 173.8 0.1 1 127 35 35 ASN CA C 52.1 0.1 1 128 35 35 ASN CB C 37.3 0.2 1 129 35 35 ASN N N 116.2 0.1 1 130 36 36 VAL H H 6.88 0.02 1 131 36 36 VAL C C 173.7 0.1 1 132 36 36 VAL CA C 60.0 0.1 1 133 36 36 VAL CB C 34.6 0.2 1 134 36 36 VAL N N 115.9 0.1 1 135 37 37 GLU H H 8.47 0.02 1 136 37 37 GLU C C 173.3 0.1 1 137 37 37 GLU CA C 55.4 0.1 1 138 37 37 GLU CB C 32.1 0.2 1 139 37 37 GLU N N 126.5 0.1 1 140 38 38 VAL H H 8.13 0.02 1 141 38 38 VAL C C 174.8 0.1 1 142 38 38 VAL CA C 59.4 0.1 1 143 38 38 VAL CB C 33.5 0.2 1 144 38 38 VAL N N 124.2 0.1 1 145 43 43 PRO C C 176.7 0.1 1 146 43 43 PRO CA C 62.9 0.1 1 147 43 43 PRO CB C 32.8 0.2 1 148 44 44 ALA H H 8.41 0.02 1 149 44 44 ALA C C 178.9 0.1 1 150 44 44 ALA CA C 54.6 0.1 1 151 44 44 ALA CB C 17.1 0.2 1 152 44 44 ALA N N 129.7 0.1 1 153 45 45 THR H H 7.49 0.02 1 154 45 45 THR C C 175.0 0.1 1 155 45 45 THR CA C 63.9 0.1 1 156 45 45 THR CB C 69.7 0.2 1 157 45 45 THR N N 111.0 0.1 1 158 46 46 TYR C C 176.6 0.2 1 159 46 46 TYR CA C 56.1 0.1 1 160 46 46 TYR CB C 40.7 0.2 1 161 47 47 LEU H H 7.35 0.02 1 162 47 47 LEU C C 176.5 0.1 1 163 47 47 LEU CA C 59.8 0.1 1 164 47 47 LEU CB C 43.1 0.2 1 165 47 47 LEU N N 126.4 0.1 1 166 48 48 ASP H H 9.04 0.02 1 167 48 48 ASP C C 177.8 0.1 1 168 48 48 ASP CA C 56.5 0.1 1 169 48 48 ASP CB C 41.5 0.2 1 170 48 48 ASP N N 120.2 0.1 1 171 49 49 TYR H H 9.01 0.02 1 172 49 49 TYR C C 178.9 0.1 1 173 49 49 TYR CA C 59.7 0.1 1 174 49 49 TYR CB C 39.6 0.2 1 175 49 49 TYR N N 119.4 0.1 1 176 51 51 VAL C C 179.6 0.1 1 177 51 51 VAL CA C 66.7 0.1 1 178 51 51 VAL CB C 31.3 0.2 1 179 52 52 SER H H 8.00 0.02 1 180 52 52 SER C C 175.3 0.1 1 181 52 52 SER CA C 61.1 0.1 1 182 52 52 SER CB C 63.4 0.2 1 183 52 52 SER N N 115.3 0.1 1 184 53 53 LEU H H 7.13 0.02 1 185 53 53 LEU C C 178.6 0.1 1 186 53 53 LEU CA C 54.9 0.1 1 187 53 53 LEU CB C 45.0 0.2 1 188 53 53 LEU N N 120.8 0.1 1 189 54 54 VAL H H 7.31 0.02 1 190 54 54 VAL C C 177.1 0.1 1 191 54 54 VAL CA C 65.3 0.1 1 192 54 54 VAL CB C 32.2 0.2 1 193 54 54 VAL N N 123.0 0.1 1 194 55 55 LYS H H 8.82 0.02 1 195 55 55 LYS C C 176.1 0.1 1 196 55 55 LYS CA C 54.7 0.1 1 197 55 55 LYS CB C 33.8 0.2 1 198 55 55 LYS N N 127.4 0.1 1 199 56 56 LYS H H 6.84 0.02 1 200 56 56 LYS C C 175.5 0.1 1 201 56 56 LYS CA C 52.3 0.1 1 202 56 56 LYS CB C 34.2 0.2 1 203 56 56 LYS N N 122.7 0.1 1 204 57 57 PRO C C 177.9 0.1 1 205 57 57 PRO CA C 64.5 0.1 1 206 57 57 PRO CB C 31.7 0.2 1 207 58 58 GLN H H 8.79 0.02 1 208 58 58 GLN C C 174.3 0.1 1 209 58 58 GLN CA C 57.9 0.1 1 210 58 58 GLN CB C 28.8 0.2 1 211 58 58 GLN N N 116.2 0.1 1 212 59 59 VAL H H 7.51 0.02 1 213 59 59 VAL C C 174.3 0.1 1 214 59 59 VAL CA C 60.8 0.1 1 215 59 59 VAL CB C 32.0 0.2 1 216 59 59 VAL N N 120.5 0.1 1 217 60 60 THR H H 8.84 0.02 1 218 60 60 THR C C 172.6 0.1 1 219 60 60 THR CA C 59.8 0.1 1 220 60 60 THR CB C 72.5 0.2 1 221 60 60 THR N N 119.7 0.1 1 222 61 61 VAL H H 8.67 0.02 1 223 61 61 VAL C C 175.2 0.1 1 224 61 61 VAL CA C 60.2 0.1 1 225 61 61 VAL CB C 33.6 0.2 1 226 61 61 VAL N N 121.4 0.1 1 227 62 62 GLY H H 8.93 0.02 1 228 62 62 GLY C C 174.6 0.1 1 229 62 62 GLY CA C 44.4 0.1 1 230 62 62 GLY N N 114.2 0.1 1 231 63 63 ALA H H 8.23 0.02 1 232 63 63 ALA C C 178.5 0.1 1 233 63 63 ALA CA C 48.6 0.1 1 234 63 63 ALA CB C 23.0 0.2 1 235 63 63 ALA N N 118.0 0.1 1 236 64 64 GLN H H 9.91 0.02 1 237 64 64 GLN C C 173.6 0.1 1 238 64 64 GLN CA C 57.1 0.1 1 239 64 64 GLN CB C 29.8 0.2 1 240 64 64 GLN N N 117.8 0.1 1 241 65 65 ASN H H 6.63 0.02 1 242 65 65 ASN C C 173.7 0.1 1 243 65 65 ASN CA C 53.3 0.1 1 244 65 65 ASN CB C 40.5 0.2 1 245 65 65 ASN N N 104.8 0.1 1 246 66 66 ALA H H 7.22 0.02 1 247 66 66 ALA C C 174.4 0.1 1 248 66 66 ALA CA C 51.7 0.1 1 249 66 66 ALA CB C 21.6 0.2 1 250 66 66 ALA N N 121.6 0.1 1 251 67 67 TYR H H 7.98 0.02 1 252 67 67 TYR C C 175.5 0.1 1 253 67 67 TYR CA C 56.5 0.1 1 254 67 67 TYR CB C 39.3 0.2 1 255 67 67 TYR N N 115.4 0.1 1 256 68 68 LEU C C 171.2 0.1 1 257 68 68 LEU CA C 53.9 0.1 1 258 68 68 LEU CB C 38.8 0.2 1 259 69 69 LYS H H 5.91 0.02 1 260 69 69 LYS C C 176.8 0.1 1 261 69 69 LYS CA C 53.1 0.1 1 262 69 69 LYS CB C 36.4 0.2 1 263 69 69 LYS N N 112.9 0.1 1 264 70 70 ALA H H 9.05 0.02 1 265 70 70 ALA C C 178.3 0.1 1 266 70 70 ALA CA C 53.1 0.1 1 267 70 70 ALA CB C 20.2 0.2 1 268 70 70 ALA N N 124.1 0.1 1 269 71 71 SER H H 7.61 0.02 1 270 71 71 SER C C 172.9 0.1 1 271 71 71 SER CA C 56.3 0.1 1 272 71 71 SER CB C 66.0 0.2 1 273 71 71 SER N N 111.3 0.1 1 274 72 72 GLY H H 7.89 0.02 1 275 72 72 GLY C C 173.5 0.1 1 276 72 72 GLY CA C 44.1 0.1 1 277 72 72 GLY N N 105.8 0.1 1 278 73 73 ALA H H 7.96 0.02 1 279 73 73 ALA C C 174.2 0.1 1 280 73 73 ALA CA C 50.6 0.1 1 281 73 73 ALA CB C 15.3 0.2 1 282 73 73 ALA N N 129.0 0.1 1 283 74 74 PHE H H 6.68 0.02 1 284 74 74 PHE C C 174.3 0.1 1 285 74 74 PHE CA C 53.8 0.1 1 286 74 74 PHE CB C 39.0 0.2 1 287 74 74 PHE N N 120.4 0.1 1 288 75 75 THR H H 8.81 0.02 1 289 75 75 THR C C 175.8 0.1 1 290 75 75 THR CA C 66.9 0.1 1 291 75 75 THR CB C 70.4 0.2 1 292 75 75 THR N N 119.9 0.1 1 293 76 76 GLY H H 9.39 0.02 1 294 76 76 GLY C C 174.4 0.1 1 295 76 76 GLY CA C 46.0 0.1 1 296 76 76 GLY N N 111.8 0.1 1 297 77 77 GLU H H 7.25 0.02 1 298 77 77 GLU C C 175.6 0.1 1 299 77 77 GLU CA C 54.8 0.1 1 300 77 77 GLU CB C 32.1 0.2 1 301 77 77 GLU N N 121.0 0.1 1 302 78 78 ASN H H 9.39 0.02 1 303 78 78 ASN C C 174.3 0.1 1 304 78 78 ASN CA C 51.0 0.1 1 305 78 78 ASN CB C 38.8 0.2 1 306 78 78 ASN N N 115.5 0.1 1 307 79 79 SER H H 8.21 0.02 1 308 79 79 SER C C 177.4 0.1 1 309 79 79 SER CA C 53.0 0.1 1 310 79 79 SER CB C 64.8 0.2 1 311 79 79 SER N N 115.3 0.1 1 312 80 80 VAL H H 9.84 0.02 1 313 80 80 VAL C C 176.2 0.1 1 314 80 80 VAL CA C 65.5 0.1 1 315 80 80 VAL CB C 31.5 0.2 1 316 80 80 VAL N N 127.0 0.1 1 317 81 81 ASP H H 7.66 0.02 1 318 81 81 ASP C C 179.4 0.1 1 319 81 81 ASP CA C 57.1 0.1 1 320 81 81 ASP CB C 40.6 0.2 1 321 81 81 ASP N N 121.0 0.1 1 322 82 82 GLN H H 6.91 0.02 1 323 82 82 GLN C C 177.5 0.1 1 324 82 82 GLN CA C 57.3 0.1 1 325 82 82 GLN CB C 27.0 0.2 1 326 82 82 GLN N N 121.9 0.1 1 327 83 83 ILE C C 177.2 0.1 1 328 83 83 ILE CA C 65.1 0.1 1 329 83 83 ILE CB C 37.6 0.2 1 330 84 84 LYS H H 7.62 0.02 1 331 84 84 LYS C C 181.0 0.1 1 332 84 84 LYS CA C 58.9 0.1 1 333 84 84 LYS CB C 32.3 0.2 1 334 84 84 LYS N N 119.0 0.1 1 335 85 85 ASP H H 7.75 0.02 1 336 85 85 ASP C C 177.5 0.1 1 337 85 85 ASP CA C 56.9 0.1 1 338 85 85 ASP CB C 42.4 0.2 1 339 85 85 ASP N N 122.2 0.1 1 340 86 86 VAL H H 7.20 0.02 1 341 86 86 VAL C C 175.7 0.1 1 342 86 86 VAL CA C 60.7 0.1 1 343 86 86 VAL CB C 31.0 0.2 1 344 86 86 VAL N N 106.1 0.1 1 345 87 87 GLY H H 7.65 0.02 1 346 87 87 GLY C C 175.2 0.1 1 347 87 87 GLY CA C 45.7 0.1 1 348 87 87 GLY N N 107.0 0.1 1 349 88 88 ALA H H 7.97 0.02 1 350 88 88 ALA C C 178.3 0.1 1 351 88 88 ALA CA C 51.6 0.1 1 352 88 88 ALA CB C 20.0 0.2 1 353 88 88 ALA N N 124.7 0.1 1 354 93 93 LEU C C 176.9 0.1 1 355 93 93 LEU CA C 52.6 0.1 1 356 93 93 LEU CB C 46.0 0.2 1 357 94 94 GLY H H 9.20 0.02 1 358 94 94 GLY C C 173.4 0.1 1 359 94 94 GLY CA C 45.5 0.1 1 360 94 94 GLY N N 107.2 0.1 1 361 95 95 HIS H H 7.56 0.02 1 362 95 95 HIS C C 177.2 0.1 1 363 95 95 HIS CA C 59.8 0.1 1 364 95 95 HIS CB C 32.1 0.2 1 365 95 95 HIS N N 120.1 0.1 1 366 98 98 ARG H H 8.00 0.02 1 367 98 98 ARG C C 177.0 0.1 1 368 98 98 ARG CA C 57.8 0.1 9 369 98 98 ARG CB C 26.7 0.2 1 370 98 98 ARG N N 117.1 0.1 1 371 99 99 ARG H H 7.58 0.02 1 372 99 99 ARG C C 177.8 0.1 1 373 99 99 ARG CA C 58.9 0.1 1 374 99 99 ARG CB C 30.1 0.2 1 375 99 99 ARG N N 117.5 0.1 1 376 100 100 SER H H 7.95 0.02 1 377 100 100 SER C C 176.8 0.1 1 378 100 100 SER CA C 59.0 0.1 1 379 100 100 SER CB C 63.7 0.2 1 380 100 100 SER N N 110.9 0.1 1 381 101 101 TYR H H 7.67 0.02 1 382 101 101 TYR C C 177.1 0.1 1 383 101 101 TYR CA C 59.5 0.1 1 384 101 101 TYR CB C 37.6 0.2 1 385 101 101 TYR N N 118.5 0.1 1 386 102 102 PHE H H 6.53 0.02 1 387 102 102 PHE C C 174.9 0.1 1 388 102 102 PHE CA C 57.4 0.1 1 389 102 102 PHE CB C 38.8 0.2 1 390 102 102 PHE N N 111.9 0.1 1 391 103 103 HIS H H 7.05 0.02 1 392 103 103 HIS C C 174.6 0.1 1 393 103 103 HIS CA C 56.2 0.1 1 394 103 103 HIS CB C 26.3 0.2 1 395 103 103 HIS N N 113.0 0.1 1 396 104 104 GLU H H 7.62 0.02 1 397 104 104 GLU C C 175.1 0.1 1 398 104 104 GLU CA C 58.6 0.1 1 399 104 104 GLU CB C 28.7 0.2 1 400 104 104 GLU N N 119.6 0.1 1 401 105 105 ASP H H 8.12 0.02 1 402 105 105 ASP C C 175.7 0.1 1 403 105 105 ASP CA C 52.3 0.1 1 404 105 105 ASP CB C 42.5 0.2 1 405 105 105 ASP N N 124.8 0.1 1 406 106 106 ASP H H 8.09 0.02 1 407 106 106 ASP C C 178.3 0.1 1 408 106 106 ASP CA C 58.5 0.1 1 409 106 106 ASP CB C 41.5 0.2 9 410 106 106 ASP N N 117.4 0.1 1 411 107 107 LYS H H 7.97 0.02 1 412 107 107 LYS C C 177.4 0.1 1 413 107 107 LYS CA C 58.4 0.1 1 414 107 107 LYS CB C 37.5 0.2 1 415 107 107 LYS N N 120.6 0.1 1 416 108 108 PHE H H 8.15 0.02 9 417 108 108 PHE C C 178.9 0.1 9 418 108 108 PHE CA C 58.4 0.1 9 419 108 108 PHE N N 123.6 0.1 9 420 109 109 ILE C C 179.6 0.1 1 421 109 109 ILE CA C 64.0 0.1 1 422 109 109 ILE CB C 36.8 0.2 1 423 110 110 ALA H H 8.66 0.02 1 424 110 110 ALA C C 178.9 0.1 1 425 110 110 ALA CA C 56.1 0.1 1 426 110 110 ALA CB C 19.3 0.2 1 427 110 110 ALA N N 128.1 0.1 1 428 111 111 ASP H H 8.90 0.02 1 429 111 111 ASP C C 181.2 0.1 1 430 111 111 ASP CA C 57.1 0.1 1 431 111 111 ASP CB C 40.6 0.2 1 432 111 111 ASP N N 120.0 0.1 1 433 117 117 LEU C C 183.1 0.1 1 434 117 117 LEU CA C 56.8 0.1 1 435 117 117 LEU CB C 41.8 0.2 1 436 118 118 GLY H H 7.66 0.02 1 437 118 118 GLY C C 175.5 0.1 1 438 118 118 GLY CA C 46.6 0.1 1 439 118 118 GLY N N 108.5 0.1 1 440 119 119 GLN H H 7.14 0.02 1 441 119 119 GLN C C 176.4 0.1 1 442 119 119 GLN CA C 53.6 0.1 1 443 119 119 GLN CB C 29.5 0.2 1 444 119 119 GLN N N 117.4 0.1 1 445 120 120 GLY H H 7.56 0.02 1 446 120 120 GLY C C 174.5 0.1 1 447 120 120 GLY CA C 46.2 0.1 1 448 120 120 GLY N N 107.0 0.1 1 449 121 121 VAL H H 7.23 0.02 1 450 121 121 VAL C C 174.3 0.1 1 451 121 121 VAL CA C 60.4 0.1 1 452 121 121 VAL CB C 33.3 0.2 1 453 121 121 VAL N N 118.9 0.1 1 454 122 122 GLY H H 7.52 0.02 1 455 122 122 GLY C C 173.4 0.1 1 456 122 122 GLY CA C 45.0 0.1 1 457 122 122 GLY N N 110.2 0.1 1 458 123 123 VAL H H 8.00 0.02 1 459 123 123 VAL C C 175.2 0.1 1 460 123 123 VAL CA C 60.4 0.1 1 461 123 123 VAL CB C 36.9 0.2 1 462 123 123 VAL N N 120.6 0.1 1 463 127 127 ILE C C 174.6 0.1 1 464 127 127 ILE CA C 59.3 0.1 1 465 127 127 ILE CB C 41.6 0.2 1 466 128 128 GLY H H 9.43 0.02 1 467 128 128 GLY C C 172.9 0.1 1 468 128 128 GLY CA C 46.9 0.1 1 469 128 128 GLY N N 108.0 0.1 1 470 129 129 GLU H H 10.02 0.02 1 471 129 129 GLU C C 174.1 0.1 1 472 129 129 GLU CA C 54.3 0.1 1 473 129 129 GLU CB C 30.7 0.2 1 474 129 129 GLU N N 129.5 0.1 1 475 130 130 THR H H 9.10 0.02 1 476 130 130 THR C C 176.3 0.1 1 477 130 130 THR CA C 60.8 0.1 1 478 130 130 THR CB C 72.0 0.2 1 479 130 130 THR N N 112.3 0.1 1 480 131 131 LEU H H 9.10 0.02 1 481 131 131 LEU C C 178.1 0.1 1 482 131 131 LEU CA C 58.8 0.1 1 483 131 131 LEU CB C 41.5 0.2 1 484 131 131 LEU N N 121.6 0.1 1 485 132 132 GLU H H 8.63 0.02 1 486 132 132 GLU C C 180.2 0.1 1 487 132 132 GLU CA C 59.7 0.1 1 488 132 132 GLU CB C 28.8 0.2 1 489 132 132 GLU N N 118.4 0.1 1 490 133 133 GLU H H 7.22 0.02 1 491 133 133 GLU C C 178.3 0.1 1 492 133 133 GLU CA C 58.8 0.1 1 493 133 133 GLU CB C 29.8 0.2 1 494 133 133 GLU N N 120.2 0.1 1 495 134 134 LYS H H 8.71 0.02 1 496 134 134 LYS C C 181.7 0.1 1 497 134 134 LYS CA C 58.7 0.1 1 498 134 134 LYS CB C 32.6 0.2 1 499 134 134 LYS N N 122.9 0.1 1 500 135 135 LYS H H 8.81 0.02 1 501 135 135 LYS C C 177.9 0.1 1 502 135 135 LYS CA C 58.9 0.1 1 503 135 135 LYS CB C 31.8 0.2 1 504 135 135 LYS N N 121.1 0.1 1 505 136 136 ALA H H 7.15 0.02 1 506 136 136 ALA C C 177.5 0.1 1 507 136 136 ALA CA C 51.7 0.1 1 508 136 136 ALA CB C 19.0 0.2 1 509 136 136 ALA N N 119.1 0.1 1 510 137 137 GLY H H 7.86 0.02 1 511 137 137 GLY C C 176.9 0.1 1 512 137 137 GLY CA C 46.3 0.1 1 513 137 137 GLY N N 108.3 0.1 1 514 138 138 LYS H H 7.95 0.02 1 515 138 138 LYS C C 175.3 0.1 1 516 138 138 LYS CA C 54.9 0.1 1 517 138 138 LYS CB C 32.1 0.2 1 518 138 138 LYS N N 117.2 0.1 1 519 140 140 LEU C C 178.3 0.1 1 520 140 140 LEU CA C 57.0 0.1 1 521 140 140 LEU CB C 39.6 0.2 1 522 141 141 ASP H H 7.47 0.02 1 523 141 141 ASP C C 179.6 0.1 1 524 141 141 ASP CA C 57.1 0.1 1 525 141 141 ASP CB C 40.9 0.2 1 526 141 141 ASP N N 119.5 0.1 1 527 142 142 VAL H H 8.25 0.02 1 528 142 142 VAL C C 177.9 0.1 1 529 142 142 VAL CA C 66.6 0.1 1 530 142 142 VAL CB C 31.6 0.2 1 531 142 142 VAL N N 120.5 0.1 1 532 143 143 VAL H H 7.94 0.02 1 533 143 143 VAL C C 178.7 0.1 1 534 143 143 VAL CA C 65.4 0.1 1 535 143 143 VAL CB C 31.0 0.2 1 536 143 143 VAL N N 115.2 0.1 1 537 144 144 GLU H H 8.14 0.02 1 538 144 144 GLU C C 178.2 0.1 1 539 144 144 GLU CA C 59.3 0.1 1 540 144 144 GLU CB C 27.7 0.2 1 541 144 144 GLU N N 118.7 0.1 1 542 145 145 ARG H H 7.65 0.02 1 543 145 145 ARG C C 180.1 0.1 1 544 145 145 ARG CA C 59.7 0.1 1 545 145 145 ARG CB C 29.3 0.2 1 546 145 145 ARG N N 122.2 0.1 1 547 146 146 GLN H H 8.45 0.02 1 548 146 146 GLN C C 180.6 0.1 1 549 146 146 GLN CA C 58.9 0.1 1 550 146 146 GLN CB C 29.0 0.2 1 551 146 146 GLN N N 119.5 0.1 1 552 147 147 LEU C C 179.5 0.1 1 553 147 147 LEU CA C 57.2 0.1 1 554 147 147 LEU CB C 42.6 0.2 1 555 148 148 ASN H H 9.58 0.02 1 556 148 148 ASN C C 178.2 0.1 1 557 148 148 ASN CA C 56.1 0.1 1 558 148 148 ASN CB C 38.2 0.2 1 559 148 148 ASN N N 121.4 0.1 1 560 149 149 ALA H H 7.51 0.02 1 561 149 149 ALA C C 179.7 0.1 1 562 149 149 ALA CA C 54.9 0.1 1 563 149 149 ALA CB C 18.4 0.2 1 564 149 149 ALA N N 119.8 0.1 1 565 150 150 VAL H H 6.88 0.02 1 566 150 150 VAL C C 178.1 0.1 1 567 150 150 VAL CA C 66.1 0.1 1 568 150 150 VAL CB C 31.7 0.2 1 569 150 150 VAL N N 116.8 0.1 1 570 151 151 LEU H H 8.77 0.02 1 571 151 151 LEU C C 178.3 0.1 1 572 151 151 LEU CA C 56.7 0.1 1 573 151 151 LEU CB C 41.7 0.2 1 574 151 151 LEU N N 122.0 0.1 1 575 152 152 GLU H H 7.58 0.02 1 576 152 152 GLU C C 177.8 0.1 1 577 152 152 GLU CA C 58.6 0.1 1 578 152 152 GLU CB C 29.9 0.2 1 579 152 152 GLU N N 117.5 0.1 1 580 153 153 GLU H H 7.37 0.02 1 581 153 153 GLU C C 176.1 0.1 1 582 153 153 GLU CA C 55.4 0.1 1 583 153 153 GLU CB C 31.9 0.2 1 584 153 153 GLU N N 113.5 0.1 1 585 155 155 LYS C C 175.6 0.1 9 586 155 155 LYS CA C 54.6 0.1 1 587 155 155 LYS CB C 32.6 0.2 1 588 156 156 ASP H H 7.12 0.02 1 589 156 156 ASP C C 175.5 0.1 1 590 156 156 ASP CA C 53.0 0.1 1 591 156 156 ASP CB C 42.2 0.2 1 592 156 156 ASP N N 118.1 0.1 1 593 157 157 PHE H H 9.25 0.02 1 594 157 157 PHE C C 176.4 0.1 1 595 157 157 PHE CA C 56.3 0.1 1 596 157 157 PHE CB C 38.0 0.2 1 597 157 157 PHE N N 129.1 0.1 1 598 158 158 THR H H 8.37 0.02 1 599 158 158 THR C C 175.4 0.1 1 600 158 158 THR CA C 67.5 0.1 1 601 158 158 THR CB C 68.9 0.2 1 602 158 158 THR N N 120.2 0.1 1 603 159 159 ASN H H 9.20 0.02 1 604 159 159 ASN C C 172.4 0.1 1 605 159 159 ASN CA C 52.3 0.1 1 606 159 159 ASN CB C 38.8 0.2 1 607 159 159 ASN N N 119.5 0.1 1 608 160 160 VAL H H 7.17 0.02 1 609 160 160 VAL C C 174.9 0.1 1 610 160 160 VAL CA C 60.5 0.1 1 611 160 160 VAL CB C 33.8 0.2 1 612 160 160 VAL N N 119.1 0.1 1 613 162 162 VAL CA C 60.6 0.1 1 614 162 162 VAL CB C 33.6 0.2 1 615 163 163 ALA H H 9.41 0.02 1 616 163 163 ALA CA C 49.3 0.1 1 617 163 163 ALA CB C 21.2 0.1 1 618 163 163 ALA N N 130.2 0.2 1 619 166 166 PRO C C 176.1 0.1 1 620 166 166 PRO CA C 59.5 0.1 1 621 166 166 PRO CB C 28.0 0.2 1 622 167 167 VAL H H 7.86 0.02 1 623 167 167 VAL C C 177.3 0.1 1 624 167 167 VAL CA C 66.6 0.1 1 625 167 167 VAL CB C 30.2 0.2 1 626 167 167 VAL N N 130.8 0.1 1 627 168 168 TRP H H 7.44 0.02 1 628 168 168 TRP C C 174.3 0.1 1 629 168 168 TRP CA C 56.3 0.1 1 630 168 168 TRP CB C 29.2 0.2 1 631 168 168 TRP N N 116.8 0.1 1 632 169 169 ALA H H 7.27 0.02 1 633 169 169 ALA C C 177.1 0.1 1 634 169 169 ALA CA C 51.2 0.1 1 635 169 169 ALA CB C 18.1 0.2 1 636 169 169 ALA N N 124.6 0.1 1 637 170 170 ILE H H 7.42 0.02 1 638 170 170 ILE C C 176.9 0.1 1 639 170 170 ILE CA C 61.3 0.1 1 640 170 170 ILE CB C 37.0 0.2 1 641 170 170 ILE N N 122.1 0.1 1 642 171 171 GLY C C 175.1 0.1 1 643 171 171 GLY CA C 46.3 0.1 1 644 172 172 THR H H 7.25 0.02 1 645 172 172 THR C C 176.2 0.1 1 646 172 172 THR CA C 61.1 0.1 1 647 172 172 THR CB C 71.5 0.2 1 648 172 172 THR N N 108.3 0.1 1 649 173 173 GLY H H 8.52 0.02 1 650 173 173 GLY C C 174.1 0.1 1 651 173 173 GLY CA C 45.2 0.1 1 652 173 173 GLY N N 112.1 0.1 1 653 174 174 LEU H H 7.59 0.02 1 654 174 174 LEU C C 175.6 0.1 1 655 174 174 LEU CA C 54.3 0.1 1 656 174 174 LEU CB C 42.7 0.2 1 657 174 174 LEU N N 122.5 0.1 1 658 175 175 ALA H H 8.24 0.02 1 659 175 175 ALA C C 176.3 0.1 1 660 175 175 ALA CA C 51.2 0.1 1 661 175 175 ALA CB C 21.0 0.2 1 662 175 175 ALA N N 122.8 0.1 1 663 176 176 ALA H H 8.24 0.02 1 664 176 176 ALA C C 178.0 0.1 1 665 176 176 ALA CA C 50.6 0.1 1 666 176 176 ALA CB C 19.9 0.2 1 667 176 176 ALA N N 125.2 0.1 1 668 177 177 THR H H 9.30 0.02 1 669 177 177 THR C C 174.2 0.1 1 670 177 177 THR CA C 59.5 0.1 1 671 177 177 THR CB C 69.8 0.2 1 672 177 177 THR N N 115.6 0.1 1 673 178 178 PRO C C 178.0 0.1 1 674 178 178 PRO CA C 64.8 0.1 1 675 178 178 PRO CB C 31.7 0.2 1 676 179 179 GLU H H 7.76 0.02 1 677 179 179 GLU C C 178.8 0.1 1 678 179 179 GLU CA C 60.4 0.1 1 679 179 179 GLU CB C 28.6 0.2 1 680 179 179 GLU N N 116.8 0.1 1 681 180 180 ASP H H 7.81 0.02 1 682 180 180 ASP C C 179.0 0.1 1 683 180 180 ASP CA C 57.4 0.1 1 684 180 180 ASP CB C 41.1 0.2 1 685 180 180 ASP N N 122.1 0.1 1 686 181 181 ALA H H 7.89 0.02 1 687 181 181 ALA C C 177.2 0.1 1 688 181 181 ALA CA C 54.8 0.1 1 689 181 181 ALA CB C 18.3 0.2 1 690 181 181 ALA N N 121.2 0.1 1 691 182 182 GLN H H 8.01 0.02 1 692 182 182 GLN C C 177.1 0.1 1 693 182 182 GLN CA C 57.5 0.1 9 694 182 182 GLN CB C 26.9 0.2 9 695 182 182 GLN N N 117.2 0.1 1 696 183 183 ASP H H 7.58 0.02 1 697 183 183 ASP C C 179.4 0.1 1 698 183 183 ASP CA C 57.5 0.1 1 699 183 183 ASP CB C 41.5 0.2 9 700 183 183 ASP N N 117.4 0.1 1 701 184 184 ILE H H 7.95 0.02 1 702 184 184 ILE C C 178.5 0.1 1 703 184 184 ILE CA C 62.7 0.1 1 704 184 184 ILE CB C 37.5 0.2 1 705 184 184 ILE N N 120.7 0.1 1 706 185 185 HIS H H 9.43 0.02 1 707 185 185 HIS C C 178.2 0.1 1 708 185 185 HIS CA C 60.6 0.1 1 709 185 185 HIS CB C 29.1 0.2 1 710 185 185 HIS N N 123.2 0.1 1 711 186 186 ALA H H 8.56 0.02 1 712 186 186 ALA C C 181.5 0.1 1 713 186 186 ALA CA C 55.4 0.1 1 714 186 186 ALA CB C 17.6 0.2 1 715 186 186 ALA N N 121.2 0.1 1 716 187 187 SER H H 7.74 0.02 1 717 187 187 SER C C 177.4 0.1 1 718 187 187 SER CA C 62.5 0.1 1 719 187 187 SER CB C 63.1 0.2 1 720 187 187 SER N N 116.8 0.1 1 721 192 192 LEU C C 179.2 0.1 1 722 192 192 LEU CA C 57.5 0.1 1 723 192 192 LEU CB C 40.4 0.2 1 724 193 193 ALA H H 8.80 0.02 1 725 193 193 ALA C C 180.6 0.1 1 726 193 193 ALA CA C 54.3 0.1 1 727 193 193 ALA CB C 17.2 0.2 1 728 193 193 ALA N N 125.1 0.1 1 729 194 194 SER H H 7.37 0.02 1 730 194 194 SER C C 174.6 0.1 1 731 194 194 SER CA C 60.8 0.1 1 732 194 194 SER CB C 63.2 0.2 1 733 194 194 SER N N 115.3 0.1 1 734 195 195 LYS H H 6.76 0.02 1 735 195 195 LYS C C 177.6 0.1 1 736 195 195 LYS CA C 55.7 0.1 1 737 195 195 LYS CB C 33.4 0.2 1 738 195 195 LYS N N 119.8 0.1 1 739 196 196 LEU H H 8.64 0.02 1 740 196 196 LEU C C 178.3 0.1 1 741 196 196 LEU CA C 54.2 0.1 1 742 196 196 LEU CB C 44.3 0.2 1 743 196 196 LEU N N 116.8 0.1 1 744 197 197 GLY H H 7.33 0.02 1 745 197 197 GLY C C 173.8 0.1 1 746 197 197 GLY CA C 44.1 0.1 1 747 197 197 GLY N N 110.1 0.1 1 748 198 198 ASP H H 8.18 0.02 1 749 198 198 ASP C C 178.9 0.1 1 750 198 198 ASP CA C 57.7 0.1 1 751 198 198 ASP CB C 41.3 0.2 1 752 198 198 ASP N N 120.3 0.1 1 753 199 199 LYS H H 8.38 0.02 1 754 199 199 LYS C C 179.6 0.1 1 755 199 199 LYS CA C 59.5 0.1 1 756 199 199 LYS CB C 31.6 0.2 1 757 199 199 LYS N N 122.4 0.1 1 758 200 200 ALA H H 8.43 0.02 1 759 200 200 ALA C C 181.9 0.1 1 760 200 200 ALA CA C 54.5 0.1 1 761 200 200 ALA CB C 18.7 0.2 1 762 200 200 ALA N N 122.3 0.1 1 763 201 201 ALA H H 7.68 0.02 1 764 201 201 ALA C C 178.5 0.1 1 765 201 201 ALA CA C 54.8 0.1 1 766 201 201 ALA CB C 17.8 0.2 1 767 201 201 ALA N N 119.0 0.1 1 768 202 202 SER H H 7.97 0.02 1 769 202 202 SER C C 175.9 0.1 1 770 202 202 SER CA C 60.8 0.1 1 771 202 202 SER CB C 63.4 0.2 1 772 202 202 SER N N 112.9 0.1 1 773 203 203 GLU H H 7.22 0.02 1 774 203 203 GLU C C 176.0 0.1 1 775 203 203 GLU CA C 56.1 0.1 1 776 203 203 GLU CB C 30.7 0.2 1 777 203 203 GLU N N 122.3 0.1 1 778 204 204 LEU H H 6.82 0.02 1 779 204 204 LEU C C 175.2 0.1 1 780 204 204 LEU CA C 54.5 0.1 1 781 204 204 LEU CB C 43.2 0.2 1 782 204 204 LEU N N 123.2 0.1 1 783 205 205 ARG H H 8.83 0.02 1 784 205 205 ARG C C 174.7 0.1 1 785 205 205 ARG CA C 56.7 0.1 1 786 205 205 ARG CB C 29.8 0.2 1 787 205 205 ARG N N 126.6 0.1 1 788 211 211 SER C C 174.6 0.1 1 789 211 211 SER CA C 58.8 0.1 1 790 211 211 SER CB C 62.5 0.2 1 791 212 212 ALA H H 7.64 0.02 1 792 212 212 ALA C C 175.6 0.1 1 793 212 212 ALA CA C 51.0 0.1 1 794 212 212 ALA CB C 20.2 0.2 1 795 212 212 ALA N N 129.5 0.1 1 796 213 213 ASN H H 8.95 0.02 1 797 213 213 ASN C C 174.7 0.1 1 798 213 213 ASN CA C 51.4 0.1 1 799 213 213 ASN CB C 39.9 0.2 1 800 213 213 ASN N N 119.4 0.1 1 801 214 214 GLY H H 9.69 0.02 1 802 214 214 GLY C C 175.3 0.1 1 803 214 214 GLY CA C 47.6 0.1 1 804 214 214 GLY N N 106.0 0.1 1 805 215 215 SER H H 8.22 0.02 1 806 215 215 SER C C 176.0 0.1 1 807 215 215 SER CA C 59.9 0.1 1 808 215 215 SER CB C 64.0 0.2 1 809 215 215 SER N N 115.5 0.1 1 810 216 216 ASN H H 8.12 0.02 1 811 216 216 ASN C C 180.7 0.1 1 812 216 216 ASN CA C 52.1 0.1 1 813 216 216 ASN CB C 39.2 0.2 1 814 216 216 ASN N N 117.3 0.1 1 815 217 217 ALA H H 8.23 0.02 1 816 217 217 ALA C C 181.4 0.1 1 817 217 217 ALA CA C 56.7 0.1 1 818 217 217 ALA CB C 17.4 0.2 1 819 217 217 ALA N N 129.5 0.1 1 820 218 218 VAL H H 8.55 0.02 1 821 218 218 VAL C C 177.8 0.1 1 822 218 218 VAL CA C 64.2 0.1 1 823 218 218 VAL CB C 31.4 0.2 1 824 218 218 VAL N N 117.8 0.1 1 825 219 219 THR H H 7.82 0.02 1 826 219 219 THR C C 175.2 0.1 1 827 219 219 THR CA C 64.0 0.1 1 828 219 219 THR CB C 69.1 0.2 1 829 219 219 THR N N 113.8 0.1 1 830 220 220 PHE H H 7.81 0.02 1 831 220 220 PHE C C 177.5 0.1 1 832 220 220 PHE CA C 57.9 0.1 1 833 220 220 PHE CB C 39.8 0.2 1 834 220 220 PHE N N 118.1 0.1 1 835 221 221 LYS H H 7.67 0.02 1 836 221 221 LYS C C 175.6 0.1 1 837 221 221 LYS CA C 59.7 0.1 1 838 221 221 LYS CB C 32.9 0.2 1 839 221 221 LYS N N 122.9 0.1 1 840 222 222 ASP C C 175.7 0.1 1 841 222 222 ASP CA C 53.4 0.1 1 842 222 222 ASP CB C 40.5 0.2 1 843 223 223 LYS H H 6.96 0.02 1 844 223 223 LYS C C 176.8 0.1 1 845 223 223 LYS CA C 53.2 0.1 1 846 223 223 LYS CB C 28.2 0.2 1 847 223 223 LYS N N 119.1 0.1 1 848 224 224 ALA H H 8.41 0.02 1 849 224 224 ALA C C 178.0 0.1 1 850 224 224 ALA CA C 54.7 0.1 1 851 224 224 ALA CB C 19.5 0.2 1 852 224 224 ALA N N 128.7 0.1 1 853 225 225 ASP H H 9.72 0.02 1 854 225 225 ASP C C 174.8 0.1 1 855 225 225 ASP CA C 54.4 0.1 1 856 225 225 ASP CB C 41.9 0.2 1 857 225 225 ASP N N 113.7 0.1 1 858 226 226 VAL H H 7.51 0.02 1 859 226 226 VAL C C 174.8 0.1 1 860 226 226 VAL CA C 62.1 0.1 1 861 226 226 VAL CB C 30.7 0.2 1 862 226 226 VAL N N 121.0 0.1 1 863 227 227 ASP H H 8.56 0.02 1 864 227 227 ASP C C 173.5 0.1 1 865 227 227 ASP CA C 54.5 0.1 1 866 227 227 ASP CB C 42.5 0.2 1 867 227 227 ASP N N 125.8 0.1 1 868 228 228 GLY H H 7.08 0.02 1 869 228 228 GLY C C 172.4 0.1 1 870 228 228 GLY CA C 44.6 0.1 1 871 228 228 GLY N N 102.0 0.1 1 872 229 229 PHE C C 174.5 0.1 1 873 229 229 PHE CA C 56.2 0.1 1 874 229 229 PHE CB C 46.1 0.2 1 875 230 230 LEU H H 8.08 0.02 1 876 230 230 LEU C C 174.8 0.1 1 877 230 230 LEU CA C 54.1 0.1 1 878 230 230 LEU CB C 42.4 0.2 1 879 230 230 LEU N N 124.6 0.1 1 880 231 231 VAL H H 9.19 0.02 1 881 231 231 VAL C C 175.3 0.1 1 882 231 231 VAL CA C 61.5 0.1 1 883 231 231 VAL CB C 33.5 0.2 1 884 231 231 VAL N N 127.0 0.1 1 885 232 232 GLY H H 8.31 0.02 1 886 232 232 GLY C C 175.8 0.1 1 887 232 232 GLY CA C 44.3 0.1 1 888 232 232 GLY N N 114.8 0.1 1 889 234 234 ALA C C 178.3 0.1 1 890 234 234 ALA CA C 54.3 0.1 1 891 234 234 ALA CB C 17.6 0.2 1 892 235 235 SER H H 8.37 0.02 1 893 235 235 SER C C 173.8 0.1 1 894 235 235 SER CA C 60.6 0.1 1 895 235 235 SER CB C 64.4 0.2 1 896 235 235 SER N N 113.7 0.1 1 897 236 236 LEU H H 6.70 0.02 1 898 236 236 LEU C C 176.9 0.1 1 899 236 236 LEU CA C 53.9 0.1 1 900 236 236 LEU CB C 41.2 0.2 1 901 236 236 LEU N N 117.7 0.1 1 902 237 237 LYS H H 7.20 0.02 1 903 237 237 LYS C C 176.8 0.1 1 904 237 237 LYS CA C 54.0 0.1 1 905 237 237 LYS CB C 34.1 0.2 1 906 237 237 LYS N N 118.5 0.1 1 907 238 238 PRO C C 178.5 0.1 1 908 238 238 PRO CA C 65.8 0.1 1 909 238 238 PRO CB C 31.1 0.2 1 910 239 239 GLU H H 7.88 0.02 1 911 239 239 GLU C C 176.4 0.1 1 912 239 239 GLU CA C 57.2 0.1 1 913 239 239 GLU CB C 29.7 0.2 1 914 239 239 GLU N N 112.9 0.1 1 915 240 240 PHE H H 7.95 0.02 1 916 240 240 PHE C C 178.2 0.1 1 917 240 240 PHE CA C 60.2 0.1 1 918 240 240 PHE CB C 40.2 0.2 1 919 240 240 PHE N N 124.8 0.1 1 920 241 241 VAL H H 7.53 0.02 1 921 241 241 VAL C C 177.4 0.1 1 922 241 241 VAL CA C 66.1 0.1 1 923 241 241 VAL CB C 31.7 0.2 1 924 241 241 VAL N N 114.9 0.1 1 925 242 242 ASP H H 6.90 0.02 1 926 242 242 ASP C C 179.5 0.1 1 927 242 242 ASP CA C 57.1 0.1 1 928 242 242 ASP CB C 40.1 0.2 1 929 242 242 ASP N N 120.3 0.1 1 930 243 243 ILE H H 7.45 0.02 1 931 243 243 ILE C C 179.7 0.1 1 932 243 243 ILE CA C 66.0 0.1 1 933 243 243 ILE CB C 37.6 0.2 1 934 243 243 ILE N N 119.9 0.1 1 935 244 244 ILE H H 7.39 0.02 1 936 244 244 ILE C C 175.3 0.1 1 937 244 244 ILE CA C 65.4 0.1 1 938 244 244 ILE CB C 37.6 0.2 1 939 244 244 ILE N N 123.2 0.1 1 940 245 245 ASN H H 7.31 0.02 1 941 245 245 ASN C C 177.1 0.1 1 942 245 245 ASN CA C 54.1 0.1 1 943 245 245 ASN CB C 39.9 0.2 1 944 245 245 ASN N N 115.0 0.1 1 945 246 246 SER H H 7.44 0.02 1 946 246 246 SER C C 174.8 0.1 1 947 246 246 SER CA C 62.0 0.1 1 948 246 246 SER CB C 64.4 0.2 1 949 246 246 SER N N 115.1 0.1 1 950 247 247 ARG H H 8.09 0.02 1 951 247 247 ARG C C 175.4 0.1 1 952 247 247 ARG CA C 54.8 0.1 1 953 247 247 ARG CB C 29.0 0.2 1 954 247 247 ARG N N 121.2 0.1 1 955 248 248 ASN H H 7.28 0.02 1 956 248 248 ASN C C 180.4 0.1 1 957 248 248 ASN CA C 54.9 0.1 1 958 248 248 ASN CB C 39.3 0.2 1 959 248 248 ASN N N 126.1 0.1 1 stop_ save_