data_16565 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; apo-WT yeast Triosephosphate Isomerase (TIM) ; _BMRB_accession_number 16565 _BMRB_flat_file_name bmr16565.str _Entry_type original _Submission_date 2009-10-19 _Accession_date 2009-10-19 _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 Xu Yimin . . 2 Lorieau Justin . . 3 McDermott Ann E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 489 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-05 update BMRB 'completed entry citation' 2009-12-03 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16566 'Complex of WT_yeast_TIM with D-glycerol_3-phosphate' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Triosephosphate Isomerase: (15)N and (13)C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19854202 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Yimin . . 2 Lorieau Justin . . 3 McDermott Ann E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 397 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 233 _Page_last 248 _Year 2010 _Details . loop_ _Keyword 'conformational change' 'crystal packing' 'sequential assignment' 'solid-state NMR' 'triosephosphate isomerase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'WT yeast TIM homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'WT TIM chain 1' $WT_yeast_TIM_homodimer 'WT TIM chain 2' $WT_yeast_TIM_homodimer stop_ _System_molecular_weight 26620 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_WT_yeast_TIM_homodimer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common WT_yeast_TIM_homodimer _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 248 _Mol_residue_sequence ; MARTFFVGGNFKLNGSKQSI KEIVERLNTASIPENVEVVI CPPATYLDYSVSLVKKPQVT VGAQNAYLKASGAFTGENSV DQIKDVGAKWVILGHSERRS YFHEDDKFIADKTKFALGQG VGVILCIGETLEEKKAGKTL DVVERQLNAVLEEVKDWTNV 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 TRP 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 TRP 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 2015-09-30 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16566 WT_yeast_TIM_homodimer 100.00 248 100.00 100.00 1.16e-178 BMRB 17122 TIM 99.60 247 98.79 99.60 3.31e-175 PDB 1I45 "Yeast Triosephosphate Isomerase (Mutant)" 100.00 248 98.79 99.60 8.45e-176 PDB 1NEY "Triosephosphate Isomerase In Complex With Dhap" 99.60 247 98.79 99.60 9.05e-175 PDB 1NF0 "Triosephosphate Isomerase In Complex With Dhap" 99.60 247 98.79 99.60 9.05e-175 PDB 1YPI "Structure Of Yeast Triosephosphate Isomerase At 1.9- Angstroms Resolution" 99.60 247 100.00 100.00 1.14e-177 PDB 2YPI "Crystallographic Analysis Of The Complex Between Triosephosphate Isomerase And 2-Phosphoglycolate At 2.5- Angstroms Resolution." 99.60 247 100.00 100.00 1.14e-177 PDB 3YPI "Electrophilic Catalysis In Triosephosphase Isomerase: The Role Of Histidine-95" 99.60 247 99.60 99.60 1.20e-176 PDB 4FF7 "Structure Of C126s Mutant Of Saccharomyces Cerevisiae Triosephosphate Isomerase" 100.00 248 99.60 99.60 1.54e-177 PDB 7TIM "Structure Of The Triosephosphate Isomerase- Phosphoglycolohydroxamate Complex: An Analogue Of The Intermediate On The Reaction " 99.60 247 100.00 100.00 1.14e-177 DBJ GAA22287 "K7_Tpi1p [Saccharomyces cerevisiae Kyokai no. 7]" 100.00 248 100.00 100.00 1.16e-178 EMBL CAA89080 "Tpi1p [Saccharomyces cerevisiae]" 100.00 248 100.00 100.00 1.16e-178 EMBL CAY78558 "Tpi1p [Saccharomyces cerevisiae EC1118]" 100.00 248 100.00 100.00 1.16e-178 GB AAA88757 "triose phosphate isomerase [Saccharomyces cerevisiae]" 100.00 248 100.00 100.00 1.16e-178 GB AAS55980 "YDR050C [Saccharomyces cerevisiae]" 100.00 248 100.00 100.00 1.16e-178 GB AHY75046 "Tpi1p [Saccharomyces cerevisiae YJM993]" 100.00 248 100.00 100.00 1.16e-178 GB AJP37778 "Tpi1p [Saccharomyces cerevisiae YJM1078]" 100.00 248 100.00 100.00 1.16e-178 GB AJU57896 "Tpi1p [Saccharomyces cerevisiae YJM189]" 100.00 248 100.00 100.00 1.16e-178 REF NP_010335 "triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288c]" 100.00 248 100.00 100.00 1.16e-178 SP P00942 "RecName: Full=Triosephosphate isomerase; Short=TIM; AltName: Full=Triose-phosphate isomerase" 100.00 248 100.00 100.00 1.16e-178 TPG DAA11897 "TPA: triose-phosphate isomerase TPI1 [Saccharomyces cerevisiae S288c]" 100.00 248 100.00 100.00 1.16e-178 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WT_yeast_TIM_homodimer 'E. coli' 562 Eubacteria . Escherichia coli 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 $WT_yeast_TIM_homodimer 'recombinant technology' . Escherichia coli . pKK223-3 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type microcrystals _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $WT_yeast_TIM_homodimer 20 mM '[U-100% 13C; U-100% 15N]' Tris-HCl 50 mM 'natural abundance' NaCl 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_13C-13C_DARR_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C DARR' _Sample_label $sample_1 save_ save_2D_15N-13C_DCP_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-13C DCP' _Sample_label $sample_1 save_ save_3D_15N-13C-13C_DCP-DARR_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-13C-13C DCP-DARR' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; The enzyme was concentrated to 200 mg/ml in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, pH 6.8 at 4 C; 40% (w/v) polyethylene glycol (average molecular weight 4000). Buffer was gently added to the protein solution in a sealed pipet tip to reach a final concentration of 15%, and the solution was stored overnight at 4oC to form crystals. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.8 . pH pressure 1 . atm temperature 277 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl carbon' ppm 40.26 internal direct . . . 1.0 DSS N 15 'methyl carbon' ppm 40.26 internal indirect . . . 0.40297969151024825976999280014533 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 13C-13C DARR' '2D 15N-13C DCP' '3D 15N-13C-13C DCP-DARR' 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 'WT TIM 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 C C 173.7 0.2 1 2 4 4 THR CA C 64.2 0.2 1 3 4 4 THR CB C 69.5 0.2 1 4 4 4 THR CG2 C 23.7 0.2 1 5 4 4 THR N N 126.1 0.3 1 6 5 5 PHE C C 172.9 0.2 1 7 5 5 PHE CA C 57.6 0.2 1 8 5 5 PHE CB C 39.9 0.2 1 9 5 5 PHE CG C 139.2 0.2 1 10 5 5 PHE N N 131.2 0.3 1 11 6 6 PHE C C 173.9 0.2 1 12 6 6 PHE CA C 54.7 0.2 1 13 6 6 PHE CB C 41.7 0.2 1 14 6 6 PHE N N 130.9 0.3 1 15 8 8 GLY C C 173.3 0.2 1 16 8 8 GLY CA C 44 0.2 1 17 8 8 GLY N N 111.9 0.3 1 18 9 9 GLY C C 171.5 0.2 1 19 9 9 GLY CA C 46.8 0.2 1 20 9 9 GLY N N 113.6 0.3 1 21 10 10 ASN C C 173.3 0.2 1 22 10 10 ASN CA C 51.4 0.2 1 23 10 10 ASN CB C 37.9 0.2 1 24 10 10 ASN N N 124.2 0.3 1 25 11 11 PHE C C 175.6 0.2 1 26 11 11 PHE CA C 56.5 0.2 1 27 11 11 PHE CB C 37 0.2 1 28 11 11 PHE N N 123.1 0.3 1 29 12 12 LYS C C 175.4 0.2 1 30 12 12 LYS CA C 57.3 0.2 1 31 12 12 LYS CB C 31.2 0.2 1 32 12 12 LYS CG C 26.9 0.2 1 33 12 12 LYS N N 116.5 0.3 1 34 13 13 LEU C C 174.9 0.2 1 35 13 13 LEU CA C 51.7 0.2 1 36 13 13 LEU CB C 41.8 0.2 1 37 13 13 LEU N N 126.9 0.3 1 38 14 14 ASN C C 172.4 0.2 1 39 14 14 ASN CA C 53.1 0.2 1 40 14 14 ASN CB C 44.2 0.2 1 41 14 14 ASN N N 117.7 0.3 1 42 15 15 GLY C C 171.1 0.2 1 43 15 15 GLY CA C 43 0.2 1 44 15 15 GLY N N 106.6 0.3 1 45 16 16 SER C C 174.2 0.2 1 46 16 16 SER CA C 55.2 0.2 1 47 16 16 SER CB C 67 0.2 1 48 16 16 SER N N 114.5 0.3 1 49 17 17 LYS C C 179.6 0.2 1 50 17 17 LYS CA C 62.2 0.2 1 51 17 17 LYS CB C 30.7 0.2 1 52 17 17 LYS N N 124.2 0.3 1 53 18 18 GLN C C 178.3 0.2 1 54 18 18 GLN CA C 59 0.2 1 55 18 18 GLN CB C 28.9 0.2 1 56 18 18 GLN N N 118.3 0.3 1 57 19 19 SER C C 177.5 0.2 1 58 19 19 SER CA C 60.8 0.2 1 59 19 19 SER CB C 62.6 0.2 1 60 19 19 SER N N 117.4 0.3 1 61 20 20 ILE C C 177 0.2 1 62 20 20 ILE CA C 65.3 0.2 1 63 20 20 ILE CB C 36.7 0.2 1 64 20 20 ILE CG2 C 17.5 0.2 1 65 20 20 ILE N N 125.9 0.3 1 66 21 21 LYS C C 177.7 0.2 1 67 21 21 LYS CA C 60.2 0.2 1 68 21 21 LYS CB C 31.1 0.2 1 69 21 21 LYS N N 122.1 0.3 1 70 22 22 GLU C C 179.4 0.2 1 71 22 22 GLU CA C 59.3 0.2 1 72 22 22 GLU CB C 29.9 0.2 1 73 22 22 GLU N N 117.8 0.3 1 74 23 23 ILE C C 178.7 0.2 1 75 23 23 ILE CA C 65.3 0.2 1 76 23 23 ILE CB C 39.1 0.2 1 77 23 23 ILE CG2 C 16 0.2 1 78 23 23 ILE N N 120.5 0.3 1 79 27 27 LEU C C 177.8 0.2 1 80 27 27 LEU CA C 57.7 0.2 1 81 27 27 LEU CB C 41.3 0.2 1 82 27 27 LEU N N 120.5 0.3 1 83 28 28 ASN C C 177.7 0.2 1 84 28 28 ASN CA C 55.2 0.2 1 85 28 28 ASN CB C 38.4 0.2 1 86 28 28 ASN N N 116.5 0.3 1 87 29 29 THR C C 174.5 0.2 1 88 29 29 THR CA C 61.5 0.2 1 89 29 29 THR CB C 70.1 0.2 1 90 29 29 THR CG2 C 21.7 0.2 1 91 29 29 THR N N 109.6 0.3 1 92 30 30 ALA C C 176.8 0.2 1 93 30 30 ALA CA C 52 0.2 1 94 30 30 ALA CB C 20.3 0.2 1 95 30 30 ALA N N 127.6 0.3 1 96 31 31 SER C C 173.9 0.2 1 97 31 31 SER CA C 57.4 0.2 1 98 31 31 SER CB C 62.4 0.2 1 99 31 31 SER N N 116.9 0.3 1 100 32 32 ILE N N 124.1 0.3 1 101 33 33 PRO C C 176.5 0.2 1 102 33 33 PRO CA C 62.4 0.2 1 103 33 33 PRO CB C 32.5 0.2 1 104 34 34 GLU C C 177.3 0.2 1 105 34 34 GLU CA C 57.9 0.2 1 106 34 34 GLU CB C 30.1 0.2 1 107 34 34 GLU N N 119.2 0.3 1 108 35 35 ASN C C 173.3 0.2 1 109 35 35 ASN CA C 52.4 0.2 1 110 35 35 ASN CB C 37.5 0.2 1 111 35 35 ASN N N 115.7 0.3 1 112 36 36 VAL C C 173.5 0.2 1 113 36 36 VAL CA C 60.3 0.2 1 114 36 36 VAL CB C 34.9 0.2 1 115 36 36 VAL N N 115.5 0.3 1 116 37 37 GLU C C 172.8 0.2 1 117 37 37 GLU CA C 55.1 0.2 1 118 37 37 GLU N N 126.3 0.3 1 119 38 38 VAL C C 175 0.2 1 120 38 38 VAL CA C 59.4 0.2 1 121 38 38 VAL CB C 33.4 0.2 1 122 38 38 VAL N N 124 0.3 1 123 44 44 ALA C C 178.7 0.2 1 124 44 44 ALA CA C 54.6 0.2 1 125 44 44 ALA CB C 17.3 0.2 1 126 44 44 ALA N N 130.2 0.3 1 127 45 45 THR CA C 64.4 0.2 1 128 45 45 THR CB C 69.3 0.2 1 129 45 45 THR CG2 C 21.7 0.2 1 130 46 46 TYR C C 176.3 0.2 1 131 46 46 TYR CA C 56.2 0.2 1 132 46 46 TYR CB C 40.5 0.2 1 133 46 46 TYR CG C 129 0.2 1 134 47 47 LEU CA C 60.1 0.2 1 135 47 47 LEU CB C 43.5 0.2 1 136 47 47 LEU N N 126.8 0.3 1 137 49 49 TYR C C 178.8 0.2 1 138 49 49 TYR CA C 60.2 0.2 1 139 49 49 TYR CB C 39.8 0.2 1 140 49 49 TYR N N 119.4 0.3 1 141 51 51 VAL C C 179.7 0.2 1 142 51 51 VAL CA C 67.1 0.2 1 143 51 51 VAL CB C 31.5 0.2 1 144 52 52 SER C C 174.9 0.2 1 145 52 52 SER CA C 61.1 0.2 1 146 52 52 SER CB C 63.2 0.2 1 147 52 52 SER N N 115.1 0.3 1 148 53 53 LEU CA C 54.9 0.2 1 149 53 53 LEU CB C 45.3 0.2 1 150 54 54 VAL C C 176.8 0.2 1 151 54 54 VAL CA C 65.4 0.2 1 152 54 54 VAL CB C 32.4 0.2 1 153 54 54 VAL N N 123.1 0.3 1 154 55 55 LYS C C 175.9 0.2 1 155 55 55 LYS CA C 55.1 0.2 1 156 55 55 LYS CB C 34 0.2 1 157 56 56 LYS C C 175.2 0.2 1 158 56 56 LYS CA C 52.2 0.2 1 159 56 56 LYS CB C 34.4 0.2 1 160 56 56 LYS CG C 26.6 0.2 1 161 57 57 PRO C C 177.5 0.2 1 162 57 57 PRO CA C 64.3 0.2 1 163 57 57 PRO CB C 31.9 0.2 1 164 57 57 PRO N N 117.9 0.3 1 165 59 59 VAL C C 174.4 0.2 1 166 59 59 VAL CA C 60.7 0.2 1 167 59 59 VAL CB C 32.4 0.2 1 168 59 59 VAL N N 120.3 0.3 1 169 60 60 THR C C 172.7 0.2 1 170 60 60 THR CA C 59.7 0.2 1 171 60 60 THR CB C 73.1 0.2 1 172 60 60 THR CG2 C 23.3 0.2 1 173 60 60 THR N N 118.1 0.3 1 174 61 61 VAL C C 175 0.2 1 175 61 61 VAL CA C 60.2 0.2 1 176 61 61 VAL CB C 34 0.2 1 177 61 61 VAL N N 120.7 0.3 1 178 62 62 GLY C C 174.5 0.2 1 179 62 62 GLY CA C 44.8 0.2 1 180 62 62 GLY N N 114.2 0.3 1 181 63 63 ALA C C 178.4 0.2 1 182 63 63 ALA CA C 48.7 0.2 1 183 63 63 ALA CB C 23 0.2 1 184 63 63 ALA N N 117.6 0.3 1 185 64 64 GLN C C 173.5 0.2 1 186 64 64 GLN CA C 57.3 0.2 1 187 64 64 GLN N N 117.7 0.3 1 188 65 65 ASN C C 173.7 0.2 1 189 65 65 ASN CA C 53.4 0.2 1 190 65 65 ASN N N 104.5 0.3 1 191 66 66 ALA C C 174.4 0.2 1 192 66 66 ALA CA C 51.9 0.2 1 193 66 66 ALA CB C 21.7 0.2 1 194 66 66 ALA N N 121.7 0.3 1 195 67 67 TYR CA C 56.4 0.2 1 196 67 67 TYR CB C 39.6 0.2 1 197 67 67 TYR N N 115.3 0.3 1 198 68 68 LEU C C 171.1 0.2 1 199 68 68 LEU CA C 53.8 0.2 1 200 68 68 LEU CB C 38.8 0.2 1 201 69 69 LYS C C 177 0.2 1 202 69 69 LYS CA C 53.5 0.2 1 203 69 69 LYS CB C 36.6 0.2 1 204 69 69 LYS N N 112.2 0.3 1 205 70 70 ALA C C 178.2 0.2 1 206 70 70 ALA CA C 53.2 0.2 1 207 70 70 ALA CB C 20.3 0.2 1 208 70 70 ALA N N 124.1 0.3 1 209 71 71 SER C C 172.9 0.2 1 210 71 71 SER CA C 56.3 0.2 1 211 71 71 SER CB C 65.7 0.2 1 212 71 71 SER N N 111.5 0.3 1 213 72 72 GLY C C 173.3 0.2 1 214 72 72 GLY CA C 44 0.2 1 215 72 72 GLY N N 105.7 0.3 1 216 73 73 ALA C C 174.1 0.2 1 217 73 73 ALA CA C 50.7 0.2 1 218 73 73 ALA CB C 15.4 0.2 1 219 73 73 ALA N N 129.2 0.3 1 220 74 74 PHE C C 174 0.2 1 221 74 74 PHE CA C 53.8 0.2 1 222 74 74 PHE CB C 38.9 0.2 1 223 74 74 PHE N N 120.7 0.3 1 224 75 75 THR C C 175.7 0.2 1 225 75 75 THR CA C 66.9 0.2 1 226 75 75 THR CB C 70.1 0.2 1 227 75 75 THR CG2 C 20.8 0.2 1 228 75 75 THR N N 119.9 0.3 1 229 76 76 GLY C C 174.4 0.2 1 230 76 76 GLY CA C 46.2 0.2 1 231 76 76 GLY N N 111.4 0.3 1 232 77 77 GLU C C 175.2 0.2 1 233 77 77 GLU CA C 54.9 0.2 1 234 77 77 GLU CB C 32.5 0.2 1 235 77 77 GLU N N 121 0.3 1 236 78 78 ASN CA C 51.1 0.2 1 237 78 78 ASN CB C 38.5 0.2 1 238 79 79 SER C C 177.2 0.2 1 239 79 79 SER CA C 52.7 0.2 1 240 79 79 SER CB C 64.6 0.2 1 241 79 79 SER N N 115 0.3 1 242 81 81 ASP C C 178.7 0.2 1 243 81 81 ASP CA C 57.5 0.2 1 244 81 81 ASP CB C 40.9 0.2 1 245 81 81 ASP N N 120.7 0.3 1 246 82 82 GLN C C 177.2 0.2 1 247 82 82 GLN CA C 57.5 0.2 1 248 82 82 GLN CB C 27.2 0.2 1 249 82 82 GLN N N 122.4 0.3 1 250 83 83 ILE C C 176.9 0.2 1 251 83 83 ILE CA C 65 0.2 1 252 83 83 ILE CB C 37.7 0.2 1 253 83 83 ILE N N 119.2 0.3 1 254 85 85 ASP C C 177.3 0.2 1 255 86 86 VAL C C 175.7 0.2 1 256 86 86 VAL CA C 60.6 0.2 1 257 86 86 VAL CB C 31.4 0.2 1 258 86 86 VAL N N 107.1 0.3 1 259 87 87 GLY C C 175.1 0.2 1 260 87 87 GLY CA C 45.6 0.2 1 261 87 87 GLY N N 124.5 0.3 1 262 88 88 ALA C C 178.2 0.2 1 263 88 88 ALA CA C 51.8 0.2 1 264 88 88 ALA CB C 20 0.2 1 265 88 88 ALA N N 106.7 0.3 1 266 93 93 LEU C C 176.7 0.2 1 267 93 93 LEU CA C 53.1 0.2 1 268 93 93 LEU CB C 46.2 0.2 1 269 94 94 GLY C C 173.4 0.2 1 270 94 94 GLY CA C 45.6 0.2 1 271 95 95 HIS CB C 31.8 0.2 1 272 95 95 HIS CD2 C 115.8 0.2 1 273 95 95 HIS CE1 C 137.4 0.2 1 274 95 95 HIS N N 117.5 0.3 1 275 98 98 ARG CA C 57.7 0.2 1 276 98 98 ARG CB C 27 0.2 1 277 99 99 ARG CA C 59.1 0.2 1 278 99 99 ARG CB C 30.1 0.2 1 279 99 99 ARG N N 110.4 0.3 1 280 102 102 PHE C C 174.7 0.2 1 281 102 102 PHE CA C 57.2 0.2 1 282 102 102 PHE CB C 38.8 0.2 1 283 103 103 HIS CA C 56.6 0.2 1 284 103 103 HIS CB C 26.3 0.2 1 285 103 103 HIS CD2 C 118.4 0.2 1 286 103 103 HIS CE1 C 132.8 0.2 1 287 104 104 GLU C C 175.2 0.2 1 288 104 104 GLU CA C 59 0.2 1 289 104 104 GLU CB C 29 0.2 1 290 104 104 GLU CG C 38.2 0.2 1 291 104 104 GLU CD C 182.1 0.2 1 292 104 104 GLU N N 119.6 0.3 1 293 105 105 ASP C C 175.4 0.2 1 294 105 105 ASP CA C 52 0.2 1 295 105 105 ASP CB C 43 0.2 1 296 105 105 ASP N N 124.9 0.3 1 297 107 107 LYS CA C 58.9 0.2 1 298 107 107 LYS CB C 37.8 0.2 1 299 109 109 ILE C C 179.4 0.2 1 300 109 109 ILE CA C 64.3 0.2 1 301 109 109 ILE CB C 36.9 0.2 1 302 110 110 ALA C C 178.5 0.2 1 303 110 110 ALA CA C 56.3 0.2 1 304 110 110 ALA CB C 19.6 0.2 1 305 110 110 ALA N N 127.7 0.3 1 306 111 111 ASP C C 181.4 0.2 1 307 111 111 ASP CA C 57.1 0.2 1 308 111 111 ASP CB C 40.5 0.2 1 309 111 111 ASP N N 120.2 0.3 1 310 117 117 LEU C C 183.1 0.2 1 311 117 117 LEU CA C 56.9 0.2 1 312 117 117 LEU CB C 42.3 0.2 1 313 117 117 LEU N N 116.1 0.3 1 314 118 118 GLY C C 175.4 0.2 1 315 118 118 GLY CA C 46.4 0.2 1 316 118 118 GLY N N 108.8 0.3 1 317 119 119 GLN CA C 53.8 0.2 1 318 119 119 GLN CB C 29.5 0.2 1 319 120 120 GLY C C 174.3 0.2 1 320 120 120 GLY CA C 45.9 0.2 1 321 121 121 VAL C C 174.3 0.2 1 322 121 121 VAL CA C 60.7 0.2 1 323 121 121 VAL CB C 33.7 0.2 1 324 121 121 VAL N N 119.2 0.3 1 325 122 122 GLY C C 173.6 0.2 1 326 122 122 GLY CA C 44.7 0.2 1 327 122 122 GLY N N 110.4 0.3 1 328 123 123 VAL CA C 60.1 0.2 1 329 123 123 VAL CB C 36.8 0.2 1 330 123 123 VAL N N 120.5 0.3 1 331 127 127 ILE C C 174.5 0.2 1 332 127 127 ILE CA C 59.8 0.2 1 333 127 127 ILE CB C 41.8 0.2 1 334 127 127 ILE CG2 C 18.1 0.2 1 335 128 128 GLY C C 172.9 0.2 1 336 128 128 GLY CA C 46.9 0.2 1 337 128 128 GLY N N 106.8 0.3 1 338 129 129 GLU C C 173.7 0.2 1 339 129 129 GLU CA C 54.3 0.2 1 340 129 129 GLU CB C 30.7 0.2 1 341 129 129 GLU N N 129.7 0.3 1 342 130 130 THR C C 176.1 0.2 1 343 130 130 THR CA C 60.8 0.2 1 344 130 130 THR CB C 71.7 0.2 1 345 130 130 THR CG2 C 21.5 0.2 1 346 130 130 THR N N 112.3 0.3 1 347 134 134 LYS C C 181.4 0.2 1 348 135 135 LYS CA C 59 0.2 1 349 135 135 LYS CB C 31.9 0.2 1 350 135 135 LYS N N 121.4 0.3 1 351 136 136 ALA C C 177.2 0.2 1 352 136 136 ALA CA C 51.9 0.2 1 353 136 136 ALA CB C 19.3 0.2 1 354 136 136 ALA N N 118.9 0.3 1 355 137 137 GLY C C 176.7 0.2 1 356 137 137 GLY CA C 46.1 0.2 1 357 137 137 GLY N N 108 0.3 1 358 138 138 LYS C C 175.5 0.2 1 359 138 138 LYS CA C 55.2 0.2 1 360 138 138 LYS CB C 32.3 0.2 1 361 138 138 LYS N N 117 0.3 1 362 142 142 VAL C C 177.7 0.2 1 363 142 142 VAL CA C 67.1 0.2 1 364 142 142 VAL CB C 31.6 0.2 1 365 142 142 VAL N N 120.5 0.3 1 366 146 146 GLN CA C 59.4 0.2 1 367 146 146 GLN CB C 29.4 0.2 1 368 147 147 LEU C C 179.2 0.2 1 369 147 147 LEU CA C 57.7 0.2 1 370 147 147 LEU CB C 42.7 0.2 1 371 147 147 LEU N N 117.3 0.3 1 372 148 148 ASN CA C 56.2 0.2 1 373 148 148 ASN CB C 38.2 0.2 1 374 148 148 ASN N N 121.6 0.3 1 375 149 149 ALA C C 179.3 0.2 1 376 149 149 ALA CA C 55.1 0.2 1 377 149 149 ALA CB C 18.7 0.2 1 378 149 149 ALA N N 120.2 0.3 1 379 150 150 VAL CA C 66 0.2 1 380 150 150 VAL CB C 31.5 0.2 1 381 150 150 VAL N N 116.7 0.3 1 382 151 151 LEU CA C 57.1 0.2 1 383 151 151 LEU CB C 42.1 0.2 1 384 155 155 LYS CA C 55.1 0.2 1 385 155 155 LYS CB C 33 0.2 1 386 158 158 THR C C 175.4 0.2 1 387 158 158 THR CA C 67.5 0.2 1 388 158 158 THR CB C 69 0.2 1 389 158 158 THR CG2 C 21.1 0.2 1 390 158 158 THR N N 120 0.3 1 391 159 159 ASN C C 172 0.2 1 392 159 159 ASN CA C 52 0.2 1 393 159 159 ASN CB C 38.5 0.2 1 394 160 160 VAL N N 119.2 0.3 1 395 163 163 ALA C C 174.8 0.2 1 396 163 163 ALA CA C 49.5 0.2 1 397 163 163 ALA CB C 21.6 0.2 1 398 163 163 ALA N N 130.1 0.3 1 399 164 164 TYR N N 122.6 0.3 1 400 166 166 PRO CA C 59.7 0.2 1 401 166 166 PRO CB C 28.4 0.2 1 402 166 166 PRO N N 140.9 0.3 1 403 167 167 VAL CA C 66.6 0.2 1 404 167 167 VAL N N 131.4 0.3 1 405 168 168 TRP CA C 56.2 0.2 1 406 168 168 TRP CB C 28.9 0.2 1 407 168 168 TRP CD1 C 123.5 0.2 1 408 168 168 TRP CG C 110.1 0.2 1 409 169 169 ALA CA C 51.7 0.2 1 410 169 169 ALA CB C 18.1 0.2 1 411 169 169 ALA N N 124.3 0.3 1 412 170 170 ILE CA C 60.8 0.2 1 413 170 170 ILE CB C 37 0.2 1 414 171 171 GLY C C 175.4 0.2 1 415 171 171 GLY CA C 46.4 0.2 1 416 172 172 THR CA C 60.9 0.2 1 417 172 172 THR CB C 71.2 0.2 1 418 172 172 THR CG2 C 23.6 0.2 1 419 173 173 GLY C C 174.3 0.2 1 420 173 173 GLY CA C 45.4 0.2 1 421 175 175 ALA C C 176.5 0.2 1 422 175 175 ALA CA C 51.6 0.2 1 423 175 175 ALA CB C 21.2 0.2 1 424 176 176 ALA C C 177.8 0.2 1 425 176 176 ALA CA C 50.9 0.2 1 426 176 176 ALA CB C 19.8 0.2 1 427 176 176 ALA N N 125.6 0.3 1 428 177 177 THR C C 174.4 0.2 1 429 177 177 THR CA C 59.2 0.2 1 430 177 177 THR CB C 69.6 0.2 1 431 177 177 THR CG2 C 22.3 0.2 1 432 177 177 THR N N 115.6 0.3 1 433 178 178 PRO C C 177.5 0.2 1 434 178 178 PRO CA C 64.6 0.2 1 435 178 178 PRO CB C 31.9 0.2 1 436 178 178 PRO N N 117.9 0.3 1 437 181 181 ALA CA C 55.1 0.2 1 438 181 181 ALA CB C 18.6 0.2 1 439 181 181 ALA N N 121.2 0.3 1 440 183 183 ASP C C 179.2 0.2 1 441 183 183 ASP CA C 57.9 0.2 1 442 183 183 ASP CB C 41.4 0.2 1 443 183 183 ASP N N 117.4 0.3 1 444 184 184 ILE C C 178.2 0.2 1 445 184 184 ILE CA C 63.2 0.2 1 446 184 184 ILE CB C 37.9 0.2 1 447 184 184 ILE CG1 C 29.1 0.2 1 448 184 184 ILE N N 121.1 0.3 1 449 185 185 HIS CA C 60.7 0.2 1 450 185 185 HIS CB C 28.9 0.2 1 451 185 185 HIS CD2 C 119.5 0.2 1 452 185 185 HIS CG C 129.3 0.2 1 453 185 185 HIS N N 123.2 0.3 1 454 186 186 ALA C C 181.4 0.2 1 455 186 186 ALA CA C 55.7 0.2 1 456 186 186 ALA CB C 17.7 0.2 1 457 186 186 ALA N N 121.4 0.3 1 458 187 187 SER N N 116.8 0.3 1 459 192 192 LEU C C 179.2 0.2 1 460 193 193 ALA C C 180.6 0.2 1 461 193 193 ALA CA C 54.4 0.2 1 462 193 193 ALA CB C 17.3 0.2 1 463 193 193 ALA N N 125 0.3 1 464 196 196 LEU CA C 54.6 0.2 1 465 196 196 LEU CB C 44.5 0.2 1 466 197 197 GLY C C 173.3 0.2 1 467 197 197 GLY CA C 44 0.2 1 468 197 197 GLY N N 109.6 0.3 1 469 198 198 ASP C C 178.7 0.2 1 470 198 198 ASP CA C 57.7 0.2 1 471 198 198 ASP CB C 41.2 0.2 1 472 198 198 ASP N N 120.6 0.3 1 473 199 199 LYS C C 179.5 0.2 1 474 199 199 LYS CA C 59.7 0.2 1 475 199 199 LYS CB C 32 0.2 1 476 200 200 ALA C C 181.9 0.2 1 477 200 200 ALA CA C 54.8 0.2 1 478 200 200 ALA CB C 18.9 0.2 1 479 200 200 ALA N N 122.2 0.3 1 480 201 201 ALA C C 178.4 0.2 1 481 201 201 ALA CA C 54.8 0.2 1 482 201 201 ALA CB C 17.8 0.2 1 483 201 201 ALA N N 119 0.3 1 484 202 202 SER C C 175.9 0.2 1 485 202 202 SER CA C 60.9 0.2 1 486 202 202 SER CB C 63.2 0.2 1 487 202 202 SER N N 112.5 0.3 1 488 203 203 GLU C C 175.7 0.2 1 489 203 203 GLU CA C 56.3 0.2 1 490 203 203 GLU CB C 30.7 0.2 1 491 203 203 GLU N N 122.8 0.3 1 492 204 204 LEU CA C 54.6 0.2 1 493 204 204 LEU CB C 43.7 0.2 1 494 205 205 ARG C C 174.5 0.2 1 495 205 205 ARG CA C 57.2 0.2 1 496 205 205 ARG CB C 29.9 0.2 1 497 209 209 GLY C C 170.1 0.2 1 498 209 209 GLY CA C 44.7 0.2 1 499 209 209 GLY N N 113.4 0.3 1 500 210 210 GLY C C 175.9 0.2 1 501 210 210 GLY CA C 47.9 0.2 1 502 210 210 GLY N N 119.4 0.3 1 503 211 211 SER C C 174.2 0.2 1 504 211 211 SER CA C 59.2 0.2 1 505 211 211 SER CB C 62.3 0.2 1 506 211 211 SER N N 123.2 0.3 1 507 212 212 ALA CA C 51.1 0.2 1 508 212 212 ALA CB C 20.3 0.2 1 509 213 213 ASN C C 174.5 0.2 1 510 213 213 ASN CA C 51.8 0.2 1 511 213 213 ASN CB C 39.6 0.2 1 512 214 214 GLY C C 175.2 0.2 1 513 214 214 GLY CA C 47.3 0.2 1 514 214 214 GLY N N 105 0.3 1 515 215 215 SER C C 175.7 0.2 1 516 215 215 SER CA C 59.9 0.2 1 517 215 215 SER CB C 63.6 0.2 1 518 215 215 SER N N 115.6 0.3 1 519 216 216 ASN C C 180.6 0.2 1 520 216 216 ASN CA C 52.2 0.2 1 521 216 216 ASN CB C 39 0.2 1 522 216 216 ASN N N 117.7 0.3 1 523 217 217 ALA C C 181.3 0.2 1 524 217 217 ALA CA C 57.1 0.2 1 525 217 217 ALA CB C 17.7 0.2 1 526 217 217 ALA N N 129.9 0.3 1 527 218 218 VAL CA C 64.3 0.2 1 528 218 218 VAL N N 117.8 0.3 1 529 219 219 THR C C 175.4 0.2 1 530 219 219 THR CA C 64.3 0.2 1 531 219 219 THR CB C 68.8 0.2 1 532 219 219 THR CG2 C 22.3 0.2 1 533 219 219 THR N N 114 0.3 1 534 223 223 LYS C C 176.6 0.2 1 535 223 223 LYS CA C 53.6 0.2 1 536 223 223 LYS CB C 28.4 0.2 1 537 223 223 LYS N N 119.5 0.3 1 538 224 224 ALA C C 177.8 0.2 1 539 224 224 ALA CA C 54.9 0.2 1 540 224 224 ALA CB C 19.7 0.2 1 541 224 224 ALA N N 129.2 0.3 1 542 225 225 ASP C C 174.4 0.2 1 543 225 225 ASP CA C 54.5 0.2 1 544 225 225 ASP CB C 41.6 0.2 1 545 225 225 ASP N N 113.8 0.3 1 546 226 226 VAL C C 174.4 0.2 1 547 226 226 VAL CA C 62.6 0.2 1 548 226 226 VAL CB C 31.2 0.2 1 549 226 226 VAL N N 121.5 0.3 1 550 227 227 ASP C C 173.2 0.2 1 551 227 227 ASP CA C 54.4 0.2 1 552 227 227 ASP CB C 43 0.2 1 553 227 227 ASP N N 126.2 0.3 1 554 228 228 GLY C C 172.1 0.2 1 555 228 228 GLY CA C 44.7 0.2 1 556 228 228 GLY N N 101.7 0.3 1 557 229 229 PHE C C 174.7 0.2 1 558 229 229 PHE CA C 56.5 0.2 1 559 229 229 PHE CB C 46.1 0.2 1 560 229 229 PHE CG C 138.4 0.2 1 561 229 229 PHE N N 114.1 0.3 1 562 230 230 LEU C C 174.6 0.2 1 563 230 230 LEU CA C 54.4 0.2 1 564 230 230 LEU CB C 42.4 0.2 1 565 230 230 LEU N N 124.6 0.3 1 566 231 231 VAL C C 174.9 0.2 1 567 231 231 VAL CA C 62 0.2 1 568 231 231 VAL CB C 33.7 0.2 1 569 231 231 VAL N N 127.2 0.3 1 570 232 232 GLY C C 175.6 0.2 1 571 232 232 GLY CA C 43.9 0.2 1 572 232 232 GLY N N 115.3 0.3 1 573 233 233 GLY C C 175.4 0.2 1 574 233 233 GLY CA C 44.8 0.2 1 575 233 233 GLY N N 119.3 0.3 1 576 234 234 ALA C C 178.4 0.2 1 577 234 234 ALA CA C 54.6 0.2 1 578 234 234 ALA CB C 17.8 0.2 1 579 234 234 ALA N N 119.6 0.3 1 580 235 235 SER C C 173.4 0.2 1 581 235 235 SER CA C 60.9 0.2 1 582 235 235 SER CB C 64.2 0.2 1 583 235 235 SER N N 114.1 0.3 1 584 236 236 LEU CA C 54.1 0.2 1 585 236 236 LEU CB C 41.4 0.2 1 586 236 236 LEU N N 117.7 0.3 1 587 237 237 LYS C C 176.6 0.2 1 588 237 237 LYS CA C 54.3 0.2 1 589 237 237 LYS CB C 34.3 0.2 1 590 237 237 LYS N N 118.1 0.3 1 591 238 238 PRO C C 178.4 0.2 1 592 238 238 PRO CA C 65.9 0.2 1 593 238 238 PRO CB C 31.5 0.2 1 594 239 239 GLU C C 176.1 0.2 1 595 239 239 GLU CA C 57.3 0.2 1 596 239 239 GLU CB C 30.1 0.2 1 597 239 239 GLU N N 112.6 0.3 1 598 240 240 PHE CA C 60.1 0.2 1 599 240 240 PHE CB C 40.1 0.2 1 600 240 240 PHE N N 124.7 0.3 1 601 241 241 VAL C C 177.2 0.2 1 602 241 241 VAL CA C 66.2 0.2 1 603 241 241 VAL CB C 32.2 0.2 1 604 241 241 VAL N N 114.8 0.3 1 605 243 243 ILE C C 179.8 0.2 1 606 243 243 ILE CA C 66.1 0.2 1 607 243 243 ILE CB C 37.7 0.2 1 608 243 243 ILE CG2 C 17.6 0.2 1 609 243 243 ILE N N 119.5 0.3 1 610 244 244 ILE C C 175.1 0.2 1 611 244 244 ILE CA C 65.6 0.2 1 612 244 244 ILE CB C 37.7 0.2 1 613 244 244 ILE N N 123.2 0.3 1 614 245 245 ASN C C 176.8 0.2 1 615 245 245 ASN CA C 54.1 0.2 1 616 245 245 ASN CB C 39.7 0.2 1 617 245 245 ASN N N 115.1 0.3 1 618 246 246 SER C C 174.7 0.2 1 619 246 246 SER CA C 61.8 0.2 1 620 246 246 SER CB C 64.1 0.2 1 621 246 246 SER N N 115 0.3 1 622 247 247 ARG C C 175.2 0.2 1 623 247 247 ARG CA C 54.8 0.2 1 624 247 247 ARG CB C 29.1 0.2 1 625 247 247 ARG N N 121.5 0.3 1 626 248 248 ASN C C 180.4 0.2 1 627 248 248 ASN CA C 55.2 0.2 1 628 248 248 ASN CB C 39 0.2 1 629 248 248 ASN N N 126.5 0.3 1 stop_ save_