data_5182 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Extracellular Ligand-Binding Domain of Ionotropic Glutamate Receptor 2 ; _BMRB_accession_number 5182 _BMRB_flat_file_name bmr5182.str _Entry_type original _Submission_date 2001-10-17 _Accession_date 2001-10-17 _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 McFeeters Robert L . 2 Swapna G.V.T. . . 3 Montelione Gaetano T . 4 Oswald Robert E . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 246 "13C chemical shifts" 740 "15N chemical shifts" 246 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-10-17 original BMRB . stop_ _Original_release_date 2001-10-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Semi-automated Backbone Resonance Assignments of the Extracellular Ligand-binding Domain of an Ionotropic Glutamate Receptor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21986773 _PubMed_ID 11991359 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McFeeters Robert L . 2 Swapna G.V.T. . . 3 Montelione Gaetano T . 4 Oswald Robert E . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 297 _Page_last 298 _Year 2002 _Details . loop_ _Keyword automated 'ionotropic glutamate receptor' 'large protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_glur2_s1s2 _Saveframe_category molecular_system _Mol_system_name 'GluR2 Extracellular Ligand-Binding Domain' _Abbreviation_common 'glur2 s1s2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gluR2 s1s2' $glur2_s1s2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_glur2_s1s2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ionotropic glutamate receptor 2' _Abbreviation_common iGluR2 _Molecular_mass 29184 _Mol_thiol_state 'disulfide bound and free' _Details 'flop isoform' ############################## # Polymer residue sequence # ############################## _Residue_count 263 _Mol_residue_sequence ; GANKTVVVTTILESPYVMMK KNHEMLEGNERYEGYCVDLA AEIAKHCGFKYKLTIVGDGK YGARDADTKIWNGMVGELVY GKADIAIAPLTITLVREEVI DFSKPFMSLGISIMIKKGTP IESAEDLSKQTEIAYGTLDS GSTKEFFRRSKIAVFDKMWT YMRSAEPSVFVRTTAEGVAR VRKSKGKYAYLLESTMNEYI EQRKPCDTMKVGGNLDSKGY GIATPKGSSLGNAVNLAVLK LNEQGLLDKLKNKWWYDKGE CGS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 ASN 4 LYS 5 THR 6 VAL 7 VAL 8 VAL 9 THR 10 THR 11 ILE 12 LEU 13 GLU 14 SER 15 PRO 16 TYR 17 VAL 18 MET 19 MET 20 LYS 21 LYS 22 ASN 23 HIS 24 GLU 25 MET 26 LEU 27 GLU 28 GLY 29 ASN 30 GLU 31 ARG 32 TYR 33 GLU 34 GLY 35 TYR 36 CYS 37 VAL 38 ASP 39 LEU 40 ALA 41 ALA 42 GLU 43 ILE 44 ALA 45 LYS 46 HIS 47 CYS 48 GLY 49 PHE 50 LYS 51 TYR 52 LYS 53 LEU 54 THR 55 ILE 56 VAL 57 GLY 58 ASP 59 GLY 60 LYS 61 TYR 62 GLY 63 ALA 64 ARG 65 ASP 66 ALA 67 ASP 68 THR 69 LYS 70 ILE 71 TRP 72 ASN 73 GLY 74 MET 75 VAL 76 GLY 77 GLU 78 LEU 79 VAL 80 TYR 81 GLY 82 LYS 83 ALA 84 ASP 85 ILE 86 ALA 87 ILE 88 ALA 89 PRO 90 LEU 91 THR 92 ILE 93 THR 94 LEU 95 VAL 96 ARG 97 GLU 98 GLU 99 VAL 100 ILE 101 ASP 102 PHE 103 SER 104 LYS 105 PRO 106 PHE 107 MET 108 SER 109 LEU 110 GLY 111 ILE 112 SER 113 ILE 114 MET 115 ILE 116 LYS 117 LYS 118 GLY 119 THR 120 PRO 121 ILE 122 GLU 123 SER 124 ALA 125 GLU 126 ASP 127 LEU 128 SER 129 LYS 130 GLN 131 THR 132 GLU 133 ILE 134 ALA 135 TYR 136 GLY 137 THR 138 LEU 139 ASP 140 SER 141 GLY 142 SER 143 THR 144 LYS 145 GLU 146 PHE 147 PHE 148 ARG 149 ARG 150 SER 151 LYS 152 ILE 153 ALA 154 VAL 155 PHE 156 ASP 157 LYS 158 MET 159 TRP 160 THR 161 TYR 162 MET 163 ARG 164 SER 165 ALA 166 GLU 167 PRO 168 SER 169 VAL 170 PHE 171 VAL 172 ARG 173 THR 174 THR 175 ALA 176 GLU 177 GLY 178 VAL 179 ALA 180 ARG 181 VAL 182 ARG 183 LYS 184 SER 185 LYS 186 GLY 187 LYS 188 TYR 189 ALA 190 TYR 191 LEU 192 LEU 193 GLU 194 SER 195 THR 196 MET 197 ASN 198 GLU 199 TYR 200 ILE 201 GLU 202 GLN 203 ARG 204 LYS 205 PRO 206 CYS 207 ASP 208 THR 209 MET 210 LYS 211 VAL 212 GLY 213 GLY 214 ASN 215 LEU 216 ASP 217 SER 218 LYS 219 GLY 220 TYR 221 GLY 222 ILE 223 ALA 224 THR 225 PRO 226 LYS 227 GLY 228 SER 229 SER 230 LEU 231 GLY 232 ASN 233 ALA 234 VAL 235 ASN 236 LEU 237 ALA 238 VAL 239 LEU 240 LYS 241 LEU 242 ASN 243 GLU 244 GLN 245 GLY 246 LEU 247 LEU 248 ASP 249 LYS 250 LEU 251 LYS 252 ASN 253 LYS 254 TRP 255 TRP 256 TYR 257 ASP 258 LYS 259 GLY 260 GLU 261 CYS 262 GLY 263 SER stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 15492 S1S2 100.00 263 100.00 100.00 4.54e-152 BMRB 15493 S1S2 100.00 263 100.00 100.00 4.54e-152 BMRB 15494 S1S2 100.00 263 100.00 100.00 4.54e-152 BMRB 15495 S1S2 100.00 263 100.00 100.00 4.54e-152 BMRB 15496 S1S2 100.00 263 100.00 100.00 4.54e-152 PDB 1FTJ 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Glutamate At 1.9 Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1FTK 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2i) In Complex With Kainate At 1.6 A Resolution' 100.76 279 98.11 98.11 1.01e-148 PDB 1FTL 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With The Antagonist Dnqx At 1.8 A Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1FTM 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Ampa At 1.7 Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1FTO 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In The Apo State At 2.0 A Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1FW0 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Kainate At 2.0 A Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1GR2 'Structure Of A Glutamate Receptor Ligand Binding Core (Glur2) Complexed With Kainate' 100.76 279 98.11 98.11 1.01e-148 PDB 1LB8 'Crystal Structure Of The Non-Desensitizing Glur2 Ligand Binding Core Mutant (S1s2j-L483y) In Complex With Ampa At 2.3 Resolution' 100.00 263 99.62 99.62 2.64e-151 PDB 1LB9 ; Crystal Structure Of The Non-Desensitizing Glur2 Ligand Binding Core Mutant (S1s2j-L483y) In Complex With Antagonist Dnqx At 2.3 A Resolution ; 100.00 263 99.62 99.62 2.64e-151 PDB 1LBB 'Crystal Structure Of The Glur2 Ligand Binding Domain Mutant (S1s2j-N754d) In Complex With Kainate At 2.1 A Resolution' 100.00 263 99.62 100.00 1.67e-151 PDB 1LBC ; Crystal Structure Of Glur2 Ligand Binding Core (S1s2j- N775s) In Complex With Cyclothiazide (Ctz) As Well As Glutamate At 1.8 A Resolution ; 100.00 263 99.62 100.00 1.70e-151 PDB 1M5B 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With 2-Me-Tet-Ampa At 1.85 A Resolution.' 100.00 263 100.00 100.00 4.54e-152 PDB 1M5C 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Br-Hibo At 1.65 A Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1M5D 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j- Y702f) In Complex With Br-Hibo At 1.73 A Resolution' 100.00 263 99.62 100.00 9.87e-152 PDB 1M5E 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Acpa At 1.46 A Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1M5F 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j- Y702f) In Complex With Acpa At 1.95 A Resolution' 100.00 263 99.62 100.00 9.87e-152 PDB 1MM6 ; Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Quisqualate In A Non Zinc Crystal Form At 2.15 Angstroms Resolution ; 100.00 263 100.00 100.00 4.54e-152 PDB 1MM7 ; Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Quisqualate In A Zinc Crystal Form At 1.65 Angstroms Resolution ; 100.00 263 100.00 100.00 4.54e-152 PDB 1MQD ; X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Des-Me-Ampa At 1.46 A Resolution. Crystallization In The Presence Of Lithium Sulfate. ; 99.24 261 100.00 100.00 5.15e-151 PDB 1MQG 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Iodo-Willardiine At 2.15 Angstroms Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1MQH 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Bromo-Willardiine At 1.8 Angstroms Resolution' 100.00 263 99.62 99.62 2.69e-151 PDB 1MQI 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Fluoro-Willardiine At 1.35 Angstroms Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1MQJ 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Willardiine At 1.65 Angstroms Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 1MS7 ; X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Des-Me-Ampa At 1.97 A Resolution, Crystallization In The Presence Of Zinc Acetate ; 100.00 263 100.00 100.00 4.54e-152 PDB 1MXU ; Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Bromo-Willardiine (Control For The Crystal Titration Experiments) ; 100.00 263 100.00 100.00 4.54e-152 PDB 1MXV 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 10 Mm Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MXW 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 1 Mm Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MXX 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 100 Um Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MXY 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 10 Um Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MXZ 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 1 Um Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MY0 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 100 Nm Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MY1 'Crystal Titration Experiments (Ampa Co-Crystals Soaked In 10 Nm Brw)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MY2 'Crystal Titration Experiment (Ampa Complex Control)' 100.00 263 100.00 100.00 4.54e-152 PDB 1MY3 'Crystal Structure Of Glutamate Receptor Ligand-Binding Core In Complex With Bromo-Willardiine In The Zn Crystal Form' 100.00 263 100.00 100.00 4.54e-152 PDB 1MY4 'Crystal Structure Of Glutamate Receptor Ligand-Binding Core In Complex With Iodo-Willardiine In The Zn Crystal Form' 100.00 263 100.00 100.00 4.54e-152 PDB 1N0T 'X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With The Antagonist (S)-Atpo At 2.1 A Resolution.' 100.00 263 100.00 100.00 4.54e-152 PDB 1NNK ; X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Atpa At 1.85 A Resolution. Crystallization With Zinc Ions. ; 100.00 263 100.00 100.00 4.54e-152 PDB 1NNP ; X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Atpa At 1.9 A Resolution. Crystallization Without Zinc Ions. ; 100.00 263 100.00 100.00 4.54e-152 PDB 1P1N 'Glur2 Ligand Binding Core (S1s2j) Mutant L650t In Complex With Kainate' 100.00 263 99.62 99.62 1.86e-151 PDB 1P1O 'Crystal Structure Of The Glur2 Ligand-Binding Core (S1s2j) Mutant L650t In Complex With Quisqualate' 100.00 263 99.62 99.62 1.86e-151 PDB 1P1Q 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) L650t Mutant In Complex With Ampa' 100.00 263 99.62 99.62 1.86e-151 PDB 1P1U 'Crystal Structure Of The Glur2 Ligand-Binding Core (S1s2j) L650t Mutant In Complex With Ampa (Ammonium Sulfate Crystal Form)' 100.00 263 99.62 99.62 1.86e-151 PDB 1P1W 'Crystal Structure Of The Glur2 Ligand-Binding Core (S1s2j) With The L483y And L650t Mutations And In Complex With Ampa' 100.00 263 99.24 99.24 1.07e-150 PDB 1SYH 'X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Cpw399 At 1.85 A Resolution.' 100.00 263 100.00 100.00 4.54e-152 PDB 1SYI 'X-Ray Structure Of The Y702f Mutant Of The Glur2 Ligand- Binding Core (S1s2j) In Complex With (S)-Cpw399 At 2.1 A Resolution.' 100.00 263 99.62 100.00 9.87e-152 PDB 1WVJ 'Exploring The Glur2 Ligand-Binding Core In Complex With The Bicyclic Ampa Analogue (S)-4-Ahcp' 100.00 263 100.00 100.00 4.54e-152 PDB 1XHY 'X-Ray Structure Of The Y702f Mutant Of The Glur2 Ligand- Binding Core (S1s2j) In Complex With Kainate At 1.85 A Resolution' 100.00 263 99.62 100.00 9.87e-152 PDB 2AIX 'X-Ray Structure Of The Glur2 Ligand-Binding Core (S1s2j) In Complex With (S)-Thio-Atpa At 2.2 A Resolution.' 100.00 263 100.00 100.00 4.54e-152 PDB 2AL4 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Quisqualate And Cx614.' 100.00 263 100.00 100.00 4.54e-152 PDB 2AL5 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With Fluoro-Willardiine And Aniracetam' 100.00 263 100.00 100.00 4.54e-152 PDB 2ANJ ; Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j- Y450w) Mutant In Complex With The Partial Agonist Kainic Acid At 2.1 A Resolution ; 100.00 263 99.62 100.00 2.04e-151 PDB 2CMO 'The Structure Of A Mixed Glur2 Ligand-Binding Core Dimer In Complex With (S)-Glutamate And The Antagonist (S)-Ns1209' 100.00 263 100.00 100.00 4.54e-152 PDB 2GFE 'Crystal Structure Of The Glur2 A476e S673d Ligand Binding Core Mutant At 1.54 Angstroms Resolution' 99.62 262 99.24 99.24 1.99e-150 PDB 2I3V ; Measurement Of Conformational Changes Accompanying Desensitization In An Ionotropic Glutamate Receptor: Structure Of G725c Mutant ; 98.48 259 99.61 99.61 6.04e-149 PDB 2I3W ; Measurement Of Conformational Changes Accompanying Desensitization In An Ionotropic Glutamate Receptor: Structure Of S729c Mutant ; 98.48 259 99.61 99.61 4.70e-149 PDB 2P2A 'X-Ray Structure Of The Glur2 Ligand Binding Core (S1s2j) In Complex With 2-Bn-Tet-Ampa At 2.26a Resolution' 100.00 263 100.00 100.00 4.54e-152 PDB 2UXA 'Crystal Structure Of The Glur2-Flip Ligand Binding Domain, RG UNEDITED' 98.86 262 98.08 98.85 2.50e-147 PDB 3B6Q 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) Mutant T686a In Complex With Glutamate At 2.0 Resolution' 98.10 260 99.61 99.61 1.11e-148 PDB 3B6T 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) T686a Mutant In Complex With Quisqualate At 2.1 Resolution' 100.00 263 99.62 99.62 1.66e-151 PDB 3B6W 'Crystal Structure Of The Glur2 Ligand Binding Core (S1s2j) T686s Mutant In Complex With Glutamate At 1.7 Resolution' 100.00 263 99.62 100.00 9.55e-152 PDB 3B7D 'Crystal Structure Of The Glur2 Ligand Binding Core (Hs1s2j) In Complex With Cnqx At 2.5 A Resolution' 99.24 261 100.00 100.00 5.15e-151 PDB 3BBR ; Crystal Structure Of The Iglur2 Ligand Binding Core (S1s2j- N775s) In Complex With A Dimeric Positive Modulator As Well As Glutamate At 2.25 A Resolution ; 100.00 267 99.62 100.00 1.97e-151 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $glur2_s1s2 Rat 10116 Eukaryota Metazoa Rattus norvegicus brain 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 $glur2_s1s2 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $glur2_s1s2 . mM 0.45 0.65 '[U-98% 13C; U-98% 15N; U-95% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_nmrDraw _Saveframe_category software _Name nmrDraw _Version . loop_ _Task processing stop_ _Details . save_ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . loop_ _Task processing stop_ _Details . save_ save_Sparky _Saveframe_category software _Name Sparky _Version . loop_ _Task visualization stop_ _Details . save_ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version . loop_ _Task 'automatic sequence assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 n/a temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCACB HN(CO)CACB HNCO HN(CA)CO '1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'gluR2 s1s2' _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 . 1 GLY H H 7.71 0.01 1 2 . 1 GLY C C 169.96 0.1 1 3 . 1 GLY CA C 43.08 0.1 1 4 . 1 GLY N N 120.66 0.1 1 5 . 2 ALA H H 8.55 0.01 1 6 . 2 ALA C C 177.52 0.1 1 7 . 2 ALA CA C 52.26 0.1 1 8 . 2 ALA CB C 18.83 0.1 1 9 . 2 ALA N N 124.26 0.1 1 10 . 3 ASN H H 8.52 0.01 1 11 . 3 ASN C C 174.82 0.1 1 12 . 3 ASN CA C 53.05 0.1 1 13 . 3 ASN CB C 38.44 0.1 1 14 . 3 ASN N N 119.36 0.1 1 15 . 4 LYS H H 8.15 0.01 1 16 . 4 LYS C C 176.42 0.1 1 17 . 4 LYS CA C 55.87 0.1 1 18 . 4 LYS CB C 32.70 0.1 1 19 . 4 LYS N N 122.44 0.1 1 20 . 5 THR H H 8.39 0.01 1 21 . 5 THR C C 173.88 0.1 1 22 . 5 THR CA C 62.93 0.1 1 23 . 5 THR CB C 68.63 0.1 1 24 . 5 THR N N 121.70 0.1 1 25 . 6 VAL H H 8.68 0.01 1 26 . 6 VAL C C 174.74 0.1 1 27 . 6 VAL CA C 62.18 0.1 1 28 . 6 VAL CB C 32.21 0.1 1 29 . 6 VAL N N 130.04 0.1 1 30 . 7 VAL H H 9.79 0.01 1 31 . 7 VAL C C 175.90 0.1 1 32 . 7 VAL CA C 63.31 0.1 1 33 . 7 VAL CB C 31.85 0.1 1 34 . 7 VAL N N 130.82 0.1 1 35 . 8 VAL H H 8.65 0.01 1 36 . 8 VAL C C 176.38 0.1 1 37 . 8 VAL CA C 59.26 0.1 1 38 . 8 VAL CB C 32.67 0.1 1 39 . 8 VAL N N 131.28 0.1 1 40 . 9 THR H H 8.98 0.01 1 41 . 9 THR C C 171.48 0.1 1 42 . 9 THR CA C 59.66 0.1 1 43 . 9 THR CB C 68.03 0.1 1 44 . 9 THR N N 124.94 0.1 1 45 . 10 THR H H 7.83 0.01 1 46 . 10 THR C C 169.96 0.1 1 47 . 10 THR CA C 60.94 0.1 1 48 . 10 THR CB C 68.23 0.1 1 49 . 10 THR N N 124.56 0.1 1 50 . 11 ILE H H 7.81 0.01 1 51 . 11 ILE C C 172.20 0.1 1 52 . 11 ILE CA C 58.57 0.1 1 53 . 11 ILE CB C 42.37 0.1 1 54 . 11 ILE N N 120.20 0.1 1 55 . 12 LEU H H 7.83 0.01 1 56 . 12 LEU C C 174.86 0.1 1 57 . 12 LEU CA C 54.80 0.1 1 58 . 12 LEU CB C 39.01 0.1 1 59 . 12 LEU N N 124.89 0.1 1 60 . 13 GLU H H 7.78 0.01 1 61 . 13 GLU C C 176.56 0.1 1 62 . 13 GLU CA C 54.56 0.1 1 63 . 13 GLU CB C 33.02 0.1 1 64 . 13 GLU N N 128.80 0.1 1 65 . 14 SER H H 9.54 0.01 1 66 . 14 SER C C 170.80 0.1 1 67 . 14 SER CA C 58.46 0.1 1 68 . 14 SER CB C 62.09 0.1 1 69 . 14 SER N N 132.05 0.1 1 70 . 15 PRO C C 173.87 0.1 1 71 . 15 PRO CA C 63.45 0.1 1 72 . 15 PRO CB C 32.43 0.1 1 73 . 16 TYR H H 8.25 0.01 1 74 . 16 TYR C C 176.93 0.1 1 75 . 16 TYR CA C 62.07 0.1 1 76 . 16 TYR CB C 37.15 0.1 1 77 . 16 TYR N N 124.89 0.1 1 78 . 17 VAL H H 7.94 0.01 1 79 . 17 VAL C C 174.08 0.1 1 80 . 17 VAL CA C 63.72 0.1 1 81 . 17 VAL CB C 33.70 0.1 1 82 . 17 VAL N N 118.28 0.1 1 83 . 18 MET H H 9.33 0.01 1 84 . 18 MET C C 175.19 0.1 1 85 . 18 MET CA C 53.34 0.1 1 86 . 18 MET CB C 35.50 0.1 1 87 . 18 MET N N 126.17 0.1 1 88 . 19 MET H H 8.75 0.01 1 89 . 19 MET C C 177.77 0.1 1 90 . 19 MET CA C 54.53 0.1 1 91 . 19 MET CB C 30.53 0.1 1 92 . 19 MET N N 120.28 0.1 1 93 . 20 LYS H H 8.52 0.01 1 94 . 20 LYS C C 177.70 0.1 1 95 . 20 LYS CA C 57.06 0.1 1 96 . 20 LYS CB C 33.40 0.1 1 97 . 20 LYS N N 126.61 0.1 1 98 . 21 LYS H H 8.86 0.01 1 99 . 21 LYS C C 177.52 0.1 1 100 . 21 LYS CA C 58.22 0.1 1 101 . 21 LYS CB C 31.29 0.1 1 102 . 21 LYS N N 124.10 0.1 1 103 . 22 ASN H H 8.73 0.01 1 104 . 22 ASN C C 176.18 0.1 1 105 . 22 ASN CA C 52.99 0.1 1 106 . 22 ASN CB C 36.43 0.1 1 107 . 22 ASN N N 117.06 0.1 1 108 . 23 HIS H H 7.63 0.01 1 109 . 23 HIS C C 175.55 0.1 1 110 . 23 HIS CA C 58.38 0.1 1 111 . 23 HIS CB C 28.25 0.1 1 112 . 23 HIS N N 115.49 0.1 1 113 . 24 GLU H H 8.69 0.01 1 114 . 24 GLU C C 177.23 0.1 1 115 . 24 GLU CA C 58.65 0.1 1 116 . 24 GLU CB C 28.11 0.1 1 117 . 24 GLU N N 121.14 0.1 1 118 . 25 MET H H 7.85 0.01 1 119 . 25 MET C C 175.49 0.1 1 120 . 25 MET CA C 54.63 0.1 1 121 . 25 MET CB C 31.72 0.1 1 122 . 25 MET N N 116.70 0.1 1 123 . 26 LEU H H 7.45 0.01 1 124 . 26 LEU C C 175.02 0.1 1 125 . 26 LEU CA C 53.20 0.1 1 126 . 26 LEU CB C 43.47 0.1 1 127 . 26 LEU N N 122.18 0.1 1 128 . 27 GLU H H 8.33 0.01 1 129 . 27 GLU C C 177.07 0.1 1 130 . 27 GLU CA C 54.12 0.1 1 131 . 27 GLU CB C 32.51 0.1 1 132 . 27 GLU N N 118.42 0.1 1 133 . 28 GLY H H 8.82 0.01 1 134 . 28 GLY C C 177.28 0.1 1 135 . 28 GLY CA C 46.12 0.1 1 136 . 28 GLY N N 109.73 0.1 1 137 . 29 ASN H H 9.49 0.01 1 138 . 29 ASN C C 176.31 0.1 1 139 . 29 ASN CA C 55.14 0.1 1 140 . 29 ASN CB C 36.90 0.1 1 141 . 29 ASN N N 125.54 0.1 1 142 . 30 GLU H H 7.83 0.01 1 143 . 30 GLU C C 176.20 0.1 1 144 . 30 GLU CA C 57.17 0.1 1 145 . 30 GLU CB C 28.95 0.1 1 146 . 30 GLU N N 116.53 0.1 1 147 . 31 ARG H H 6.87 0.01 1 148 . 31 ARG C C 174.37 0.1 1 149 . 31 ARG CA C 58.32 0.1 1 150 . 31 ARG CB C 30.63 0.1 1 151 . 31 ARG N N 114.81 0.1 1 152 . 32 TYR H H 6.86 0.01 1 153 . 32 TYR C C 173.98 0.1 1 154 . 32 TYR CA C 55.50 0.1 1 155 . 32 TYR CB C 42.27 0.1 1 156 . 32 TYR N N 114.30 0.1 1 157 . 33 GLU H H 9.19 0.01 1 158 . 33 GLU C C 172.95 0.1 1 159 . 33 GLU CA C 53.56 0.1 1 160 . 33 GLU CB C 32.58 0.1 1 161 . 33 GLU N N 116.33 0.1 1 162 . 34 GLY H H 8.26 0.01 1 163 . 34 GLY C C 174.33 0.1 1 164 . 34 GLY CA C 42.07 0.1 1 165 . 34 GLY N N 109.32 0.1 1 166 . 35 TYR H H 7.34 0.01 1 167 . 35 TYR C C 178.28 0.1 1 168 . 35 TYR CA C 62.61 0.1 1 169 . 35 TYR CB C 39.49 0.1 1 170 . 35 TYR N N 119.47 0.1 1 171 . 36 CYS H H 10.20 0.01 1 172 . 36 CYS C C 175.50 0.1 1 173 . 36 CYS CA C 63.86 0.1 1 174 . 36 CYS CB C 27.05 0.1 1 175 . 36 CYS N N 114.50 0.1 1 176 . 37 VAL H H 6.66 0.01 1 177 . 37 VAL C C 178.68 0.1 1 178 . 37 VAL CA C 66.21 0.1 1 179 . 37 VAL CB C 30.40 0.1 1 180 . 37 VAL N N 124.19 0.1 1 181 . 38 ASP H H 8.08 0.01 1 182 . 38 ASP C C 179.20 0.1 1 183 . 38 ASP CA C 57.03 0.1 1 184 . 38 ASP CB C 40.63 0.1 1 185 . 38 ASP N N 123.24 0.1 1 186 . 39 LEU H H 8.30 0.01 1 187 . 39 LEU C C 177.84 0.1 1 188 . 39 LEU CA C 57.52 0.1 1 189 . 39 LEU CB C 41.37 0.1 1 190 . 39 LEU N N 120.74 0.1 1 191 . 40 ALA H H 7.98 0.01 1 192 . 40 ALA C C 177.87 0.1 1 193 . 40 ALA CA C 55.25 0.1 1 194 . 40 ALA CB C 16.93 0.1 1 195 . 40 ALA N N 120.67 0.1 1 196 . 41 ALA H H 7.24 0.01 1 197 . 41 ALA C C 181.44 0.1 1 198 . 41 ALA CA C 55.07 0.1 1 199 . 41 ALA CB C 17.46 0.1 1 200 . 41 ALA N N 118.70 0.1 1 201 . 42 GLU H H 7.66 0.01 1 202 . 42 GLU C C 180.16 0.1 1 203 . 42 GLU CA C 58.30 0.1 1 204 . 42 GLU CB C 29.17 0.1 1 205 . 42 GLU N N 118.30 0.1 1 206 . 43 ILE H H 8.61 0.01 1 207 . 43 ILE C C 177.64 0.1 1 208 . 43 ILE CA C 64.20 0.1 1 209 . 43 ILE CB C 36.18 0.1 1 210 . 43 ILE N N 122.02 0.1 1 211 . 44 ALA H H 8.21 0.01 1 212 . 44 ALA C C 180.12 0.1 1 213 . 44 ALA CA C 55.27 0.1 1 214 . 44 ALA CB C 19.68 0.1 1 215 . 44 ALA N N 123.48 0.1 1 216 . 45 LYS H H 7.55 0.01 1 217 . 45 LYS C C 179.18 0.1 1 218 . 45 LYS CA C 58.63 0.1 1 219 . 45 LYS CB C 31.60 0.1 1 220 . 45 LYS N N 118.15 0.1 1 221 . 46 HIS H H 7.63 0.01 1 222 . 46 HIS C C 177.20 0.1 1 223 . 46 HIS CA C 59.33 0.1 1 224 . 46 HIS CB C 29.77 0.1 1 225 . 46 HIS N N 117.28 0.1 1 226 . 47 CYS H H 8.08 0.01 1 227 . 47 CYS C C 175.23 0.1 1 228 . 47 CYS CA C 60.39 0.1 1 229 . 47 CYS CB C 29.33 0.1 1 230 . 47 CYS N N 114.74 0.1 1 231 . 48 GLY H H 7.90 0.01 1 232 . 48 GLY C C 174.00 0.1 1 233 . 48 GLY CA C 46.42 0.1 1 234 . 48 GLY N N 109.81 0.1 1 235 . 49 PHE H H 7.11 0.01 1 236 . 49 PHE C C 174.80 0.1 1 237 . 49 PHE CA C 54.19 0.1 1 238 . 49 PHE CB C 40.58 0.1 1 239 . 49 PHE N N 114.55 0.1 1 240 . 50 LYS H H 8.81 0.01 1 241 . 50 LYS C C 176.48 0.1 1 242 . 50 LYS CA C 54.92 0.1 1 243 . 50 LYS CB C 33.17 0.1 1 244 . 50 LYS N N 121.92 0.1 1 245 . 51 TYR H H 8.41 0.01 1 246 . 51 TYR C C 173.95 0.1 1 247 . 51 TYR CA C 55.53 0.1 1 248 . 51 TYR CB C 41.91 0.1 1 249 . 51 TYR N N 117.62 0.1 1 250 . 52 LYS H H 8.81 0.01 1 251 . 52 LYS C C 175.56 0.1 1 252 . 52 LYS CA C 54.18 0.1 1 253 . 52 LYS CB C 35.08 0.1 1 254 . 52 LYS N N 122.88 0.1 1 255 . 53 LEU H H 8.76 0.01 1 256 . 53 LEU C C 176.23 0.1 1 257 . 53 LEU CA C 55.02 0.1 1 258 . 53 LEU CB C 41.77 0.1 1 259 . 53 LEU N N 125.90 0.1 1 260 . 54 THR H H 8.68 0.01 1 261 . 54 THR C C 171.11 0.1 1 262 . 54 THR CA C 59.85 0.1 1 263 . 54 THR CB C 70.87 0.1 1 264 . 54 THR N N 120.07 0.1 1 265 . 55 ILE H H 8.10 0.01 1 266 . 55 ILE C C 176.76 0.1 1 267 . 55 ILE CA C 57.22 0.1 1 268 . 55 ILE CB C 34.37 0.1 1 269 . 55 ILE N N 123.43 0.1 1 270 . 56 VAL H H 8.78 0.01 1 271 . 56 VAL C C 177.51 0.1 1 272 . 56 VAL CA C 60.99 0.1 1 273 . 56 VAL CB C 30.27 0.1 1 274 . 56 VAL N N 131.26 0.1 1 275 . 57 GLY H H 8.92 0.01 1 276 . 57 GLY C C 175.51 0.1 1 277 . 57 GLY CA C 48.00 0.1 1 278 . 57 GLY N N 119.18 0.1 1 279 . 58 ASP H H 7.85 0.01 1 280 . 58 ASP C C 178.31 0.1 1 281 . 58 ASP CA C 52.29 0.1 1 282 . 58 ASP CB C 40.31 0.1 1 283 . 58 ASP N N 117.32 0.1 1 284 . 59 GLY H H 7.39 0.01 1 285 . 59 GLY C C 173.84 0.1 1 286 . 59 GLY CA C 46.17 0.1 1 287 . 59 GLY N N 106.30 0.1 1 288 . 60 LYS H H 7.82 0.01 1 289 . 60 LYS C C 175.54 0.1 1 290 . 60 LYS CA C 54.87 0.1 1 291 . 60 LYS CB C 34.78 0.1 1 292 . 60 LYS N N 120.39 0.1 1 293 . 61 TYR H H 8.38 0.01 1 294 . 61 TYR C C 177.89 0.1 1 295 . 61 TYR CA C 61.99 0.1 1 296 . 61 TYR CB C 38.37 0.1 1 297 . 61 TYR N N 119.84 0.1 1 298 . 62 GLY H H 7.89 0.01 1 299 . 62 GLY C C 172.87 0.1 1 300 . 62 GLY CA C 46.70 0.1 1 301 . 62 GLY N N 103.08 0.1 1 302 . 63 ALA H H 9.05 0.01 1 303 . 63 ALA C C 174.17 0.1 1 304 . 63 ALA CA C 51.10 0.1 1 305 . 63 ALA CB C 22.05 0.1 1 306 . 63 ALA N N 133.93 0.1 1 307 . 64 ARG H H 7.67 0.01 1 308 . 64 ARG C C 175.95 0.1 1 309 . 64 ARG CA C 53.80 0.1 1 310 . 64 ARG CB C 29.57 0.1 1 311 . 64 ARG N N 122.95 0.1 1 312 . 65 ASP H H 7.80 0.01 1 313 . 65 ASP C C 175.94 0.1 1 314 . 65 ASP CA C 54.81 0.1 1 315 . 65 ASP CB C 42.65 0.1 1 316 . 65 ASP N N 130.51 0.1 1 317 . 66 ALA H H 8.68 0.01 1 318 . 66 ALA C C 178.22 0.1 1 319 . 66 ALA CA C 54.60 0.1 1 320 . 66 ALA CB C 18.46 0.1 1 321 . 66 ALA N N 129.83 0.1 1 322 . 67 ASP H H 8.39 0.01 1 323 . 67 ASP C C 177.88 0.1 1 324 . 67 ASP CA C 56.04 0.1 1 325 . 67 ASP CB C 41.34 0.1 1 326 . 67 ASP N N 116.32 0.1 1 327 . 68 THR C C 175.89 0.1 1 328 . 68 THR CB C 69.91 0.1 1 329 . 68 THR CA C 62.11 0.1 1 330 . 69 LYS H H 7.80 0.01 1 331 . 69 LYS C C 174.84 0.1 1 332 . 69 LYS CA C 57.32 0.1 1 333 . 69 LYS CB C 28.40 0.1 1 334 . 69 LYS N N 114.96 0.1 1 335 . 70 ILE H H 7.30 0.01 1 336 . 70 ILE C C 178.05 0.1 1 337 . 70 ILE CA C 59.95 0.1 1 338 . 70 ILE CB C 38.23 0.1 1 339 . 70 ILE N N 120.12 0.1 1 340 . 71 TRP H H 8.61 0.01 1 341 . 71 TRP C C 175.53 0.1 1 342 . 71 TRP CA C 57.84 0.1 1 343 . 71 TRP CB C 30.13 0.1 1 344 . 71 TRP N N 130.00 0.1 1 345 . 72 ASN H H 8.17 0.01 1 346 . 72 ASN C C 176.54 0.1 1 347 . 72 ASN CA C 49.98 0.1 1 348 . 72 ASN CB C 39.30 0.1 1 349 . 72 ASN N N 121.17 0.1 1 350 . 73 GLY H H 10.02 0.01 1 351 . 73 GLY C C 176.70 0.1 1 352 . 73 GLY CA C 46.22 0.1 1 353 . 73 GLY N N 107.35 0.1 1 354 . 74 MET H H 7.65 0.01 1 355 . 74 MET C C 178.04 0.1 1 356 . 74 MET CA C 59.10 0.1 1 357 . 74 MET CB C 34.25 0.1 1 358 . 74 MET N N 124.40 0.1 1 359 . 75 VAL H H 7.43 0.01 1 360 . 75 VAL C C 177.30 0.1 1 361 . 75 VAL CA C 67.06 0.1 1 362 . 75 VAL CB C 30.95 0.1 1 363 . 75 VAL N N 115.06 0.1 1 364 . 76 GLY H H 7.75 0.01 1 365 . 76 GLY C C 174.38 0.1 1 366 . 76 GLY CA C 46.97 0.1 1 367 . 76 GLY N N 106.97 0.1 1 368 . 77 GLU H H 7.59 0.01 1 369 . 77 GLU C C 178.80 0.1 1 370 . 77 GLU CA C 60.29 0.1 1 371 . 77 GLU CB C 28.17 0.1 1 372 . 77 GLU N N 119.46 0.1 1 373 . 78 LEU H H 7.23 0.01 1 374 . 78 LEU C C 179.25 0.1 1 375 . 78 LEU CA C 56.62 0.1 1 376 . 78 LEU CB C 41.78 0.1 1 377 . 78 LEU N N 117.28 0.1 1 378 . 79 VAL H H 8.09 0.01 1 379 . 79 VAL C C 178.50 0.1 1 380 . 79 VAL CA C 65.48 0.1 1 381 . 79 VAL CB C 31.41 0.1 1 382 . 79 VAL N N 120.20 0.1 1 383 . 80 TYR H H 8.14 0.01 1 384 . 80 TYR C C 177.14 0.1 1 385 . 80 TYR CA C 56.44 0.1 1 386 . 80 TYR CB C 35.96 0.1 1 387 . 80 TYR N N 115.44 0.1 1 388 . 81 GLY H H 7.18 0.01 1 389 . 81 GLY C C 175.20 0.1 1 390 . 81 GLY CA C 47.02 0.1 1 391 . 81 GLY N N 107.28 0.1 1 392 . 82 LYS H H 8.57 0.01 1 393 . 82 LYS C C 175.78 0.1 1 394 . 82 LYS CA C 55.98 0.1 1 395 . 82 LYS CB C 32.21 0.1 1 396 . 82 LYS N N 119.13 0.1 1 397 . 83 ALA H H 7.40 0.01 1 398 . 83 ALA C C 174.55 0.1 1 399 . 83 ALA CA C 50.45 0.1 1 400 . 83 ALA CB C 21.65 0.1 1 401 . 83 ALA N N 119.98 0.1 1 402 . 84 ASP H H 8.65 0.01 1 403 . 84 ASP C C 175.15 0.1 1 404 . 84 ASP CA C 55.97 0.1 1 405 . 84 ASP CB C 43.60 0.1 1 406 . 84 ASP N N 118.45 0.1 1 407 . 85 ILE H H 7.56 0.01 1 408 . 85 ILE C C 172.35 0.1 1 409 . 85 ILE CA C 59.16 0.1 1 410 . 85 ILE CB C 40.06 0.1 1 411 . 85 ILE N N 114.90 0.1 1 412 . 86 ALA H H 9.34 0.01 1 413 . 86 ALA C C 177.68 0.1 1 414 . 86 ALA CA C 50.19 0.1 1 415 . 86 ALA CB C 21.17 0.1 1 416 . 86 ALA N N 129.27 0.1 1 417 . 87 ILE H H 7.31 0.01 1 418 . 87 ILE C C 172.30 0.1 1 419 . 87 ILE CA C 61.66 0.1 1 420 . 87 ILE CB C 36.55 0.1 1 421 . 87 ILE N N 123.71 0.1 1 422 . 88 ALA H H 9.18 0.01 1 423 . 88 ALA C C 174.33 0.1 1 424 . 88 ALA CA C 50.84 0.1 1 425 . 88 ALA CB C 21.31 0.1 1 426 . 88 ALA N N 131.57 0.1 1 427 . 89 PRO C C 171.55 0.1 1 428 . 89 PRO CA C 60.07 0.1 1 429 . 89 PRO CB C 25.54 0.1 1 430 . 90 LEU H H 7.76 0.01 1 431 . 90 LEU C C 174.74 0.1 1 432 . 90 LEU CA C 52.85 0.1 1 433 . 90 LEU CB C 43.98 0.1 1 434 . 90 LEU N N 126.69 0.1 1 435 . 91 THR H H 9.18 0.01 1 436 . 91 THR C C 173.65 0.1 1 437 . 91 THR CA C 63.40 0.1 1 438 . 91 THR CB C 68.23 0.1 1 439 . 91 THR N N 125.11 0.1 1 440 . 92 ILE H H 8.11 0.01 1 441 . 92 ILE C C 175.77 0.1 1 442 . 92 ILE CA C 62.25 0.1 1 443 . 92 ILE CB C 36.55 0.1 1 444 . 92 ILE N N 128.41 0.1 1 445 . 93 THR H H 6.31 0.01 1 446 . 93 THR C C 173.96 0.1 1 447 . 93 THR CA C 57.82 0.1 1 448 . 93 THR CB C 71.45 0.1 1 449 . 93 THR N N 117.67 0.1 1 450 . 94 LEU H H 8.50 0.01 1 451 . 94 LEU C C 180.17 0.1 1 452 . 94 LEU CA C 55.05 0.1 1 453 . 94 LEU CB C 40.96 0.1 1 454 . 94 LEU N N 124.93 0.1 1 455 . 95 VAL H H 7.96 0.01 1 456 . 95 VAL C C 179.20 0.1 1 457 . 95 VAL CA C 65.17 0.1 1 458 . 95 VAL CB C 30.98 0.1 1 459 . 95 VAL N N 117.06 0.1 1 460 . 96 ARG H H 7.40 0.01 1 461 . 96 ARG C C 178.05 0.1 1 462 . 96 ARG CA C 58.88 0.1 1 463 . 96 ARG CB C 30.73 0.1 1 464 . 96 ARG N N 119.03 0.1 1 465 . 97 GLU H H 8.27 0.01 1 466 . 97 GLU C C 176.80 0.1 1 467 . 97 GLU CA C 57.58 0.1 1 468 . 97 GLU CB C 28.76 0.1 1 469 . 97 GLU N N 119.89 0.1 1 470 . 98 GLU H H 7.17 0.01 1 471 . 98 GLU C C 178.33 0.1 1 472 . 98 GLU CA C 58.70 0.1 1 473 . 98 GLU CB C 30.00 0.1 1 474 . 98 GLU N N 116.29 0.1 1 475 . 99 VAL H H 7.56 0.01 1 476 . 99 VAL C C 174.58 0.1 1 477 . 99 VAL CA C 61.17 0.1 1 478 . 99 VAL CB C 33.56 0.1 1 479 . 99 VAL N N 107.29 0.1 1 480 . 100 ILE H H 7.97 0.01 1 481 . 100 ILE C C 172.58 0.1 1 482 . 100 ILE CA C 59.87 0.1 1 483 . 100 ILE CB C 40.65 0.1 1 484 . 100 ILE N N 118.52 0.1 1 485 . 101 ASP H H 8.36 0.01 1 486 . 101 ASP C C 175.45 0.1 1 487 . 101 ASP CA C 52.52 0.1 1 488 . 101 ASP CB C 42.35 0.1 1 489 . 101 ASP N N 118.51 0.1 1 490 . 102 PHE H H 8.64 0.01 1 491 . 102 PHE C C 176.87 0.1 1 492 . 102 PHE CA C 56.45 0.1 1 493 . 102 PHE CB C 43.24 0.1 1 494 . 102 PHE N N 117.12 0.1 1 495 . 103 SER H H 8.72 0.01 1 496 . 103 SER C C 175.13 0.1 1 497 . 103 SER CA C 58.10 0.1 1 498 . 103 SER CB C 66.64 0.1 1 499 . 103 SER N N 116.24 0.1 1 500 . 104 LYS H H 8.46 0.01 1 501 . 104 LYS CA C 54.62 0.1 1 502 . 104 LYS CB C 30.40 0.1 1 503 . 104 LYS N N 119.45 0.1 1 504 . 105 PRO C C 177.90 0.1 1 505 . 105 PRO CA C 62.30 0.1 1 506 . 105 PRO CB C 31.47 0.1 1 507 . 106 PHE H H 8.30 0.01 1 508 . 106 PHE C C 173.90 0.1 1 509 . 106 PHE CA C 55.01 0.1 1 510 . 106 PHE CB C 39.41 0.1 1 511 . 106 PHE N N 115.86 0.1 1 512 . 107 MET H H 6.78 0.01 1 513 . 107 MET C C 173.12 0.1 1 514 . 107 MET CA C 56.02 0.1 1 515 . 107 MET CB C 36.03 0.1 1 516 . 107 MET N N 120.33 0.1 1 517 . 108 SER H H 8.09 0.01 1 518 . 108 SER C C 172.70 0.1 1 519 . 108 SER CA C 57.17 0.1 1 520 . 108 SER CB C 64.18 0.1 1 521 . 108 SER N N 120.08 0.1 1 522 . 109 LEU H H 8.08 0.01 1 523 . 109 LEU C C 174.30 0.1 1 524 . 109 LEU CA C 54.79 0.1 1 525 . 109 LEU CB C 40.86 0.1 1 526 . 109 LEU N N 119.87 0.1 1 527 . 110 GLY H H 7.89 0.01 1 528 . 110 GLY C C 172.90 0.1 1 529 . 110 GLY CA C 44.93 0.1 1 530 . 110 GLY N N 105.46 0.1 1 531 . 111 ILE H H 9.25 0.01 1 532 . 111 ILE C C 173.35 0.1 1 533 . 111 ILE CA C 64.36 0.1 1 534 . 111 ILE CB C 37.25 0.1 1 535 . 111 ILE N N 124.86 0.1 1 536 . 112 SER H H 8.88 0.01 1 537 . 112 SER C C 170.85 0.1 1 538 . 112 SER CA C 56.63 0.1 1 539 . 112 SER CB C 68.22 0.1 1 540 . 112 SER N N 122.48 0.1 1 541 . 113 ILE H H 8.31 0.01 1 542 . 113 ILE C C 175.25 0.1 1 543 . 113 ILE CA C 60.85 0.1 1 544 . 113 ILE CB C 39.05 0.1 1 545 . 113 ILE N N 118.78 0.1 1 546 . 114 MET H H 9.45 0.01 1 547 . 114 MET C C 174.70 0.1 1 548 . 114 MET CA C 54.20 0.1 1 549 . 114 MET CB C 36.77 0.1 1 550 . 114 MET N N 131.02 0.1 1 551 . 115 ILE H H 8.40 0.01 1 552 . 115 ILE C C 175.95 0.1 1 553 . 115 ILE CA C 58.08 0.1 1 554 . 115 ILE CB C 41.41 0.1 1 555 . 115 ILE N N 117.41 0.1 1 556 . 116 LYS H H 8.69 0.01 1 557 . 116 LYS C C 177.94 0.1 1 558 . 116 LYS CA C 55.17 0.1 1 559 . 116 LYS CB C 32.43 0.1 1 560 . 116 LYS N N 123.18 0.1 1 561 . 117 LYS H H 8.65 0.01 1 562 . 117 LYS C C 176.96 0.1 1 563 . 117 LYS CA C 59.84 0.1 1 564 . 117 LYS CB C 31.67 0.1 1 565 . 117 LYS N N 130.93 0.1 1 566 . 118 GLY H H 8.72 0.01 1 567 . 118 GLY C C 174.83 0.1 1 568 . 118 GLY CA C 44.38 0.1 1 569 . 118 GLY N N 113.51 0.1 1 570 . 123 SER C C 174.04 0.1 1 571 . 123 SER CA C 56.43 0.1 1 572 . 123 SER CB C 66.08 0.1 1 573 . 124 ALA H H 9.25 0.01 1 574 . 124 ALA C C 178.47 0.1 1 575 . 124 ALA CA C 54.91 0.1 1 576 . 124 ALA CB C 16.98 0.1 1 577 . 124 ALA N N 124.01 0.1 1 578 . 125 GLU H H 8.56 0.01 1 579 . 125 GLU C C 179.88 0.1 1 580 . 125 GLU CA C 59.78 0.1 1 581 . 125 GLU CB C 28.00 0.1 1 582 . 125 GLU N N 118.52 0.1 1 583 . 126 ASP H H 7.91 0.01 1 584 . 126 ASP C C 179.42 0.1 1 585 . 126 ASP CA C 57.02 0.1 1 586 . 126 ASP CB C 40.59 0.1 1 587 . 126 ASP N N 120.21 0.1 1 588 . 127 LEU C C 178.92 0.1 1 589 . 127 LEU CA C 57.20 0.1 1 590 . 127 LEU CB C 39.96 0.1 1 591 . 128 SER H H 7.98 0.01 1 592 . 128 SER C C 174.88 0.1 1 593 . 128 SER CA C 60.79 0.1 1 594 . 128 SER CB C 63.53 0.1 1 595 . 128 SER N N 112.27 0.1 1 596 . 129 LYS H H 7.03 0.01 1 597 . 129 LYS C C 174.77 0.1 1 598 . 129 LYS CA C 56.29 0.1 1 599 . 129 LYS CB C 32.75 0.1 1 600 . 129 LYS N N 120.80 0.1 1 601 . 130 GLN H H 7.67 0.01 1 602 . 130 GLN C C 174.18 0.1 1 603 . 130 GLN CA C 53.26 0.1 1 604 . 130 GLN CB C 30.55 0.1 1 605 . 130 GLN N N 116.86 0.1 1 606 . 131 THR H H 8.54 0.01 1 607 . 131 THR C C 174.30 0.1 1 608 . 131 THR CA C 60.81 0.1 1 609 . 131 THR CB C 70.14 0.1 1 610 . 131 THR N N 107.18 0.1 1 611 . 132 GLU H H 7.36 0.01 1 612 . 132 GLU C C 176.60 0.1 1 613 . 132 GLU CA C 58.87 0.1 1 614 . 132 GLU CB C 30.09 0.1 1 615 . 132 GLU N N 125.53 0.1 1 616 . 133 ILE H H 9.72 0.01 1 617 . 133 ILE C C 176.14 0.1 1 618 . 133 ILE CA C 60.62 0.1 1 619 . 133 ILE CB C 37.43 0.1 1 620 . 133 ILE N N 122.78 0.1 1 621 . 134 ALA H H 7.89 0.01 1 622 . 134 ALA C C 175.31 0.1 1 623 . 134 ALA CA C 51.23 0.1 1 624 . 134 ALA CB C 20.63 0.1 1 625 . 134 ALA N N 130.79 0.1 1 626 . 135 TYR H H 6.35 0.01 1 627 . 135 TYR C C 172.92 0.1 1 628 . 135 TYR CA C 54.25 0.1 1 629 . 135 TYR CB C 38.61 0.1 1 630 . 135 TYR N N 112.32 0.1 1 631 . 136 GLY H H 6.67 0.01 1 632 . 136 GLY C C 171.13 0.1 1 633 . 136 GLY CA C 44.56 0.1 1 634 . 136 GLY N N 101.37 0.1 1 635 . 137 THR H H 6.34 0.01 1 636 . 137 THR CA C 60.29 0.1 1 637 . 137 THR CB C 71.95 0.1 1 638 . 137 THR N N 105.35 0.1 1 639 . 138 LEU C C 180.19 0.1 1 640 . 138 LEU CA C 55.65 0.1 1 641 . 138 LEU CB C 41.65 0.1 1 642 . 139 ASP H H 9.48 0.01 1 643 . 139 ASP C C 177.25 0.1 1 644 . 139 ASP CA C 55.17 0.1 1 645 . 139 ASP CB C 41.40 0.1 1 646 . 139 ASP N N 128.60 0.1 1 647 . 140 SER H H 7.79 0.01 1 648 . 140 SER C C 172.40 0.1 1 649 . 140 SER CA C 58.87 0.1 1 650 . 140 SER CB C 60.88 0.1 1 651 . 140 SER N N 111.94 0.1 1 652 . 141 GLY H H 6.88 0.01 1 653 . 141 GLY C C 175.06 0.1 1 654 . 141 GLY CA C 43.99 0.1 1 655 . 141 GLY N N 104.90 0.1 1 656 . 142 SER H H 9.38 0.01 1 657 . 142 SER C C 178.58 0.1 1 658 . 142 SER CA C 60.84 0.1 1 659 . 142 SER CB C 63.29 0.1 1 660 . 142 SER N N 117.06 0.1 1 661 . 143 THR H H 9.04 0.01 1 662 . 143 THR C C 176.11 0.1 1 663 . 143 THR CA C 67.78 0.1 1 664 . 143 THR CB C 65.57 0.1 1 665 . 143 THR N N 129.69 0.1 1 666 . 144 LYS H H 9.61 0.01 1 667 . 144 LYS C C 178.44 0.1 1 668 . 144 LYS CA C 60.96 0.1 1 669 . 144 LYS CB C 31.95 0.1 1 670 . 144 LYS N N 125.19 0.1 1 671 . 145 GLU H H 7.01 0.01 1 672 . 145 GLU C C 177.92 0.1 1 673 . 145 GLU CA C 57.90 0.1 1 674 . 145 GLU CB C 29.40 0.1 1 675 . 145 GLU N N 114.66 0.1 1 676 . 146 PHE H H 7.95 0.01 1 677 . 146 PHE C C 177.92 0.1 1 678 . 146 PHE CA C 60.64 0.1 1 679 . 146 PHE CB C 37.95 0.1 1 680 . 146 PHE N N 120.84 0.1 1 681 . 147 PHE H H 7.31 0.01 1 682 . 147 PHE C C 175.74 0.1 1 683 . 147 PHE CA C 63.10 0.1 1 684 . 147 PHE CB C 39.59 0.1 1 685 . 147 PHE N N 117.03 0.1 1 686 . 148 ARG H H 7.42 0.01 1 687 . 148 ARG C C 177.03 0.1 1 688 . 148 ARG CA C 57.66 0.1 1 689 . 148 ARG CB C 29.23 0.1 1 690 . 148 ARG N N 119.66 0.1 1 691 . 149 ARG H H 7.04 0.01 1 692 . 149 ARG C C 177.10 0.1 1 693 . 149 ARG CA C 54.87 0.1 1 694 . 149 ARG CB C 29.95 0.1 1 695 . 149 ARG N N 112.36 0.1 1 696 . 150 SER H H 6.86 0.01 1 697 . 150 SER C C 176.45 0.1 1 698 . 150 SER CA C 60.24 0.1 1 699 . 150 SER CB C 62.89 0.1 1 700 . 150 SER N N 115.22 0.1 1 701 . 151 LYS H H 8.75 0.01 1 702 . 151 LYS C C 176.95 0.1 1 703 . 151 LYS CA C 54.80 0.1 1 704 . 151 LYS CB C 31.39 0.1 1 705 . 151 LYS N N 125.68 0.1 1 706 . 152 ILE H H 8.05 0.01 1 707 . 152 ILE C C 177.51 0.1 1 708 . 152 ILE CA C 60.38 0.1 1 709 . 152 ILE CB C 36.73 0.1 1 710 . 152 ILE N N 125.37 0.1 1 711 . 153 ALA H H 8.63 0.01 1 712 . 153 ALA C C 180.33 0.1 1 713 . 153 ALA CA C 56.38 0.1 1 714 . 153 ALA CB C 17.61 0.1 1 715 . 153 ALA N N 132.59 0.1 1 716 . 154 VAL H H 8.02 0.01 1 717 . 154 VAL C C 176.58 0.1 1 718 . 154 VAL CA C 65.83 0.1 1 719 . 154 VAL CB C 30.83 0.1 1 720 . 154 VAL N N 117.14 0.1 1 721 . 155 PHE H H 6.25 0.01 1 722 . 155 PHE C C 178.14 0.1 1 723 . 155 PHE CA C 57.40 0.1 1 724 . 155 PHE CB C 35.28 0.1 1 725 . 155 PHE N N 120.60 0.1 1 726 . 156 ASP H H 8.76 0.01 1 727 . 156 ASP C C 179.44 0.1 1 728 . 156 ASP CA C 56.75 0.1 1 729 . 156 ASP CB C 40.83 0.1 1 730 . 156 ASP N N 122.89 0.1 1 731 . 157 LYS H H 8.41 0.01 1 732 . 157 LYS C C 180.20 0.1 1 733 . 157 LYS CA C 59.66 0.1 1 734 . 157 LYS CB C 31.53 0.1 1 735 . 157 LYS N N 123.17 0.1 1 736 . 158 MET H H 8.06 0.01 1 737 . 158 MET C C 178.45 0.1 1 738 . 158 MET CA C 58.55 0.1 1 739 . 158 MET CB C 33.74 0.1 1 740 . 158 MET N N 119.72 0.1 1 741 . 159 TRP H H 9.25 0.01 1 742 . 159 TRP C C 176.57 0.1 1 743 . 159 TRP CA C 59.50 0.1 1 744 . 159 TRP CB C 30.15 0.1 1 745 . 159 TRP N N 122.73 0.1 1 746 . 160 THR H H 8.62 0.01 1 747 . 160 THR C C 176.64 0.1 1 748 . 160 THR CA C 66.78 0.1 1 749 . 160 THR CB C 68.24 0.1 1 750 . 160 THR N N 114.55 0.1 1 751 . 161 TYR H H 7.62 0.01 1 752 . 161 TYR C C 177.36 0.1 1 753 . 161 TYR CA C 60.67 0.1 1 754 . 161 TYR CB C 36.98 0.1 1 755 . 161 TYR N N 122.02 0.1 1 756 . 162 MET H H 8.54 0.01 1 757 . 162 MET C C 177.77 0.1 1 758 . 162 MET CA C 59.52 0.1 1 759 . 162 MET CB C 33.68 0.1 1 760 . 162 MET N N 120.70 0.1 1 761 . 163 ARG H H 8.29 0.01 1 762 . 163 ARG C C 177.01 0.1 1 763 . 163 ARG CA C 57.72 0.1 1 764 . 163 ARG CB C 27.85 0.1 1 765 . 163 ARG N N 114.77 0.1 1 766 . 164 SER H H 6.68 0.01 1 767 . 164 SER C C 173.91 0.1 1 768 . 164 SER CA C 57.60 0.1 1 769 . 164 SER CB C 64.39 0.1 1 770 . 164 SER N N 112.20 0.1 1 771 . 165 ALA H H 6.78 0.01 1 772 . 165 ALA C C 176.77 0.1 1 773 . 165 ALA CA C 53.34 0.1 1 774 . 165 ALA CB C 18.23 0.1 1 775 . 165 ALA N N 127.20 0.1 1 776 . 166 GLU H H 8.06 0.01 1 777 . 166 GLU C C 174.90 0.1 1 778 . 166 GLU CA C 53.03 0.1 1 779 . 166 GLU CB C 32.03 0.1 1 780 . 166 GLU N N 122.72 0.1 1 781 . 169 VAL C C 175.02 0.1 1 782 . 169 VAL CA C 61.63 0.1 1 783 . 169 VAL CB C 31.26 0.1 1 784 . 170 PHE H H 7.82 0.01 1 785 . 170 PHE C C 176.12 0.1 1 786 . 170 PHE CA C 57.49 0.1 1 787 . 170 PHE CB C 39.53 0.1 1 788 . 170 PHE N N 122.31 0.1 1 789 . 171 VAL H H 7.97 0.01 1 790 . 171 VAL C C 175.98 0.1 1 791 . 171 VAL CA C 58.96 0.1 1 792 . 171 VAL CB C 34.42 0.1 1 793 . 171 VAL N N 112.87 0.1 1 794 . 172 ARG H H 8.77 0.01 1 795 . 172 ARG C C 177.95 0.1 1 796 . 172 ARG CA C 57.96 0.1 1 797 . 172 ARG CB C 31.08 0.1 1 798 . 172 ARG N N 119.63 0.1 1 799 . 173 THR H H 7.18 0.01 1 800 . 173 THR C C 174.22 0.1 1 801 . 173 THR CA C 59.03 0.1 1 802 . 173 THR CB C 73.18 0.1 1 803 . 173 THR N N 106.99 0.1 1 804 . 174 THR H H 9.22 0.01 1 805 . 174 THR C C 176.91 0.1 1 806 . 174 THR CA C 65.63 0.1 1 807 . 174 THR CB C 67.72 0.1 1 808 . 174 THR N N 122.53 0.1 1 809 . 175 ALA H H 8.62 0.01 1 810 . 175 ALA C C 180.76 0.1 1 811 . 175 ALA CA C 54.97 0.1 1 812 . 175 ALA CB C 17.43 0.1 1 813 . 175 ALA N N 121.94 0.1 1 814 . 176 GLU H H 7.93 0.01 1 815 . 176 GLU C C 179.60 0.1 1 816 . 176 GLU CA C 58.87 0.1 1 817 . 176 GLU CB C 29.62 0.1 1 818 . 176 GLU N N 120.84 0.1 1 819 . 177 GLY H H 7.74 0.01 1 820 . 177 GLY C C 174.51 0.1 1 821 . 177 GLY CA C 47.15 0.1 1 822 . 177 GLY N N 110.72 0.1 1 823 . 178 VAL H H 8.21 0.01 1 824 . 178 VAL C C 178.33 0.1 1 825 . 178 VAL CA C 65.71 0.1 1 826 . 178 VAL CB C 31.33 0.1 1 827 . 178 VAL N N 121.77 0.1 1 828 . 179 ALA H H 8.08 0.01 1 829 . 179 ALA C C 179.90 0.1 1 830 . 179 ALA CA C 54.74 0.1 1 831 . 179 ALA CB C 17.26 0.1 1 832 . 179 ALA N N 121.71 0.1 1 833 . 180 ARG H H 7.78 0.01 1 834 . 180 ARG C C 180.23 0.1 1 835 . 180 ARG CA C 59.49 0.1 1 836 . 180 ARG CB C 29.15 0.1 1 837 . 180 ARG N N 120.21 0.1 1 838 . 181 VAL H H 8.15 0.01 1 839 . 181 VAL C C 179.60 0.1 1 840 . 181 VAL CA C 66.31 0.1 1 841 . 181 VAL CB C 31.49 0.1 1 842 . 181 VAL N N 123.25 0.1 1 843 . 182 ARG H H 8.13 0.01 1 844 . 182 ARG C C 179.71 0.1 1 845 . 182 ARG CA C 60.51 0.1 1 846 . 182 ARG CB C 29.66 0.1 1 847 . 182 ARG N N 118.37 0.1 1 848 . 183 LYS H H 8.58 0.01 1 849 . 183 LYS C C 178.14 0.1 1 850 . 183 LYS CA C 57.41 0.1 1 851 . 183 LYS CB C 32.15 0.1 1 852 . 183 LYS N N 119.15 0.1 1 853 . 184 SER H H 7.48 0.01 1 854 . 184 SER C C 176.36 0.1 1 855 . 184 SER CA C 59.55 0.1 1 856 . 184 SER CB C 63.55 0.1 1 857 . 184 SER N N 112.92 0.1 1 858 . 185 LYS H H 8.53 0.01 1 859 . 185 LYS C C 175.68 0.1 1 860 . 185 LYS CA C 57.57 0.1 1 861 . 185 LYS CB C 29.23 0.1 1 862 . 185 LYS N N 119.82 0.1 1 863 . 186 GLY H H 8.13 0.01 1 864 . 186 GLY C C 175.11 0.1 1 865 . 186 GLY CA C 45.28 0.1 1 866 . 186 GLY N N 105.15 0.1 1 867 . 187 LYS H H 7.32 0.01 1 868 . 187 LYS C C 175.18 0.1 1 869 . 187 LYS CA C 55.38 0.1 1 870 . 187 LYS CB C 30.43 0.1 1 871 . 187 LYS N N 116.15 0.1 1 872 . 188 TYR H H 7.63 0.01 1 873 . 188 TYR C C 173.28 0.1 1 874 . 188 TYR CA C 57.32 0.1 1 875 . 188 TYR CB C 41.64 0.1 1 876 . 188 TYR N N 122.55 0.1 1 877 . 189 ALA H H 8.71 0.01 1 878 . 189 ALA C C 172.70 0.1 1 879 . 189 ALA CA C 50.02 0.1 1 880 . 189 ALA CB C 20.95 0.1 1 881 . 189 ALA N N 134.25 0.1 1 882 . 190 TYR H H 8.27 0.01 1 883 . 190 TYR C C 173.40 0.1 1 884 . 190 TYR CA C 54.49 0.1 1 885 . 190 TYR CB C 42.85 0.1 1 886 . 190 TYR N N 120.43 0.1 1 887 . 191 LEU H H 8.05 0.01 1 888 . 191 LEU C C 173.87 0.1 1 889 . 191 LEU CA C 53.11 0.1 1 890 . 191 LEU CB C 40.31 0.1 1 891 . 191 LEU N N 129.96 0.1 1 892 . 192 LEU H H 8.40 0.01 1 893 . 192 LEU C C 176.01 0.1 1 894 . 192 LEU CA C 53.89 0.1 1 895 . 192 LEU CB C 41.14 0.1 1 896 . 192 LEU N N 122.00 0.1 1 897 . 193 GLU H H 9.91 0.01 1 898 . 193 GLU C C 179.29 0.1 1 899 . 193 GLU CA C 57.19 0.1 1 900 . 193 GLU CB C 28.64 0.1 1 901 . 193 GLU N N 124.94 0.1 1 902 . 194 SER H H 9.77 0.01 1 903 . 194 SER C C 174.97 0.1 1 904 . 194 SER CA C 62.18 0.1 1 905 . 194 SER CB C 61.23 0.1 1 906 . 194 SER N N 120.83 0.1 1 907 . 195 THR H H 7.32 0.01 1 908 . 195 THR C C 177.93 0.1 1 909 . 195 THR CA C 62.38 0.1 1 910 . 195 THR CB C 67.04 0.1 1 911 . 195 THR N N 112.08 0.1 1 912 . 196 MET H H 7.25 0.01 1 913 . 196 MET C C 177.42 0.1 1 914 . 196 MET CA C 60.08 0.1 1 915 . 196 MET CB C 32.32 0.1 1 916 . 196 MET N N 122.62 0.1 1 917 . 197 ASN H H 8.17 0.01 1 918 . 197 ASN C C 177.04 0.1 1 919 . 197 ASN CA C 55.87 0.1 1 920 . 197 ASN CB C 39.42 0.1 1 921 . 197 ASN N N 119.03 0.1 1 922 . 198 GLU H H 8.96 0.01 1 923 . 198 GLU C C 178.65 0.1 1 924 . 198 GLU CA C 58.70 0.1 1 925 . 198 GLU CB C 29.30 0.1 1 926 . 198 GLU N N 116.41 0.1 1 927 . 199 TYR H H 7.25 0.01 1 928 . 199 TYR C C 177.10 0.1 1 929 . 199 TYR CA C 61.41 0.1 1 930 . 199 TYR CB C 37.61 0.1 1 931 . 199 TYR N N 118.14 0.1 1 932 . 200 ILE H H 7.71 0.01 1 933 . 200 ILE C C 179.22 0.1 1 934 . 200 ILE CA C 62.63 0.1 1 935 . 200 ILE CB C 36.96 0.1 1 936 . 200 ILE N N 119.63 0.1 1 937 . 201 GLU H H 8.24 0.01 1 938 . 201 GLU C C 176.33 0.1 1 939 . 201 GLU CA C 58.21 0.1 1 940 . 201 GLU CB C 29.15 0.1 1 941 . 201 GLU N N 119.72 0.1 1 942 . 202 GLN H H 6.90 0.01 1 943 . 202 GLN C C 174.71 0.1 1 944 . 202 GLN CA C 54.52 0.1 1 945 . 202 GLN CB C 28.25 0.1 1 946 . 202 GLN N N 112.62 0.1 1 947 . 203 ARG H H 7.45 0.01 1 948 . 203 ARG C C 176.55 0.1 1 949 . 203 ARG CA C 53.19 0.1 1 950 . 203 ARG CB C 32.13 0.1 1 951 . 203 ARG N N 120.56 0.1 1 952 . 204 LYS H H 9.07 0.01 1 953 . 204 LYS C C 176.44 0.1 1 954 . 204 LYS CA C 56.02 0.1 1 955 . 204 LYS CB C 30.74 0.1 1 956 . 204 LYS N N 123.66 0.1 1 957 . 206 CYS C C 175.85 0.1 1 958 . 206 CYS CA C 56.00 0.1 1 959 . 207 ASP H H 8.65 0.01 1 960 . 207 ASP C C 176.40 0.1 1 961 . 207 ASP CA C 53.08 0.1 1 962 . 207 ASP CB C 40.86 0.1 1 963 . 207 ASP N N 117.46 0.1 1 964 . 208 THR H H 7.77 0.01 1 965 . 208 THR C C 173.30 0.1 1 966 . 208 THR CA C 59.79 0.1 1 967 . 208 THR CB C 72.15 0.1 1 968 . 208 THR N N 111.59 0.1 1 969 . 209 MET H H 8.91 0.01 1 970 . 209 MET C C 173.23 0.1 1 971 . 209 MET CA C 54.53 0.1 1 972 . 209 MET CB C 36.46 0.1 1 973 . 209 MET N N 116.65 0.1 1 974 . 210 LYS H H 8.15 0.01 1 975 . 210 LYS C C 176.72 0.1 1 976 . 210 LYS CA C 54.43 0.1 1 977 . 210 LYS CB C 32.80 0.1 1 978 . 210 LYS N N 124.87 0.1 1 979 . 211 VAL H H 7.91 0.01 1 980 . 211 VAL C C 175.81 0.1 1 981 . 211 VAL CA C 59.61 0.1 1 982 . 211 VAL CB C 33.96 0.1 1 983 . 211 VAL N N 122.78 0.1 1 984 . 212 GLY H H 8.55 0.01 1 985 . 212 GLY C C 174.15 0.1 1 986 . 212 GLY CA C 44.88 0.1 1 987 . 212 GLY N N 113.57 0.1 1 988 . 213 GLY H H 8.06 0.01 1 989 . 213 GLY C C 174.18 0.1 1 990 . 213 GLY CA C 43.70 0.1 1 991 . 213 GLY N N 107.54 0.1 1 992 . 214 ASN H H 8.52 0.01 1 993 . 214 ASN C C 177.79 0.1 1 994 . 214 ASN CA C 51.81 0.1 1 995 . 214 ASN CB C 37.48 0.1 1 996 . 214 ASN N N 120.73 0.1 1 997 . 215 LEU H H 9.28 0.01 1 998 . 215 LEU C C 175.15 0.1 1 999 . 215 LEU CA C 56.00 0.1 1 1000 . 215 LEU CB C 40.74 0.1 1 1001 . 215 LEU N N 121.98 0.1 1 1002 . 216 ASP H H 7.38 0.01 1 1003 . 216 ASP C C 174.23 0.1 1 1004 . 216 ASP CA C 52.04 0.1 1 1005 . 216 ASP CB C 40.33 0.1 1 1006 . 216 ASP N N 117.01 0.1 1 1007 . 217 SER H H 7.68 0.01 1 1008 . 217 SER C C 173.12 0.1 1 1009 . 217 SER CA C 57.31 0.1 1 1010 . 217 SER CB C 63.44 0.1 1 1011 . 217 SER N N 111.58 0.1 1 1012 . 218 LYS H H 8.95 0.01 1 1013 . 218 LYS C C 173.67 0.1 1 1014 . 218 LYS CA C 54.92 0.1 1 1015 . 218 LYS CB C 33.13 0.1 1 1016 . 218 LYS N N 126.29 0.1 1 1017 . 219 GLY H H 7.76 0.01 1 1018 . 219 GLY C C 172.02 0.1 1 1019 . 219 GLY CA C 44.37 0.1 1 1020 . 219 GLY N N 106.69 0.1 1 1021 . 220 TYR H H 7.09 0.01 1 1022 . 220 TYR C C 172.02 0.1 1 1023 . 220 TYR CA C 52.67 0.1 1 1024 . 220 TYR CB C 39.71 0.1 1 1025 . 220 TYR N N 117.64 0.1 1 1026 . 221 GLY H H 8.14 0.01 1 1027 . 221 GLY C C 172.75 0.1 1 1028 . 221 GLY CA C 43.73 0.1 1 1029 . 221 GLY N N 105.05 0.1 1 1030 . 222 ILE H H 8.76 0.01 1 1031 . 222 ILE C C 172.70 0.1 1 1032 . 222 ILE CA C 60.67 0.1 1 1033 . 222 ILE CB C 36.19 0.1 1 1034 . 222 ILE N N 121.14 0.1 1 1035 . 223 ALA H H 7.91 0.01 1 1036 . 223 ALA C C 175.31 0.1 1 1037 . 223 ALA CA C 49.75 0.1 1 1038 . 223 ALA CB C 23.61 0.1 1 1039 . 223 ALA N N 131.02 0.1 1 1040 . 224 THR H H 8.66 0.01 1 1041 . 224 THR C C 170.80 0.1 1 1042 . 224 THR CA C 57.54 0.1 1 1043 . 224 THR CB C 68.89 0.1 1 1044 . 224 THR N N 112.11 0.1 1 1045 . 225 PRO C C 176.90 0.1 1 1046 . 225 PRO CA C 62.08 0.1 1 1047 . 225 PRO CB C 30.98 0.1 1 1048 . 226 LYS H H 8.61 0.01 1 1049 . 226 LYS C C 179.01 0.1 1 1050 . 226 LYS CA C 56.86 0.1 1 1051 . 226 LYS CB C 30.47 0.1 1 1052 . 226 LYS N N 122.92 0.1 1 1053 . 227 GLY H H 9.11 0.01 1 1054 . 227 GLY C C 174.76 0.1 1 1055 . 227 GLY CA C 44.93 0.1 1 1056 . 227 GLY N N 114.33 0.1 1 1057 . 228 SER H H 7.65 0.01 1 1058 . 228 SER C C 178.21 0.1 1 1059 . 228 SER CA C 57.76 0.1 1 1060 . 228 SER CB C 63.44 0.1 1 1061 . 228 SER N N 114.62 0.1 1 1062 . 229 SER H H 9.30 0.01 1 1063 . 229 SER C C 175.86 0.1 1 1064 . 229 SER CA C 60.43 0.1 1 1065 . 229 SER CB C 62.35 0.1 1 1066 . 229 SER N N 126.96 0.1 1 1067 . 230 LEU H H 8.27 0.01 1 1068 . 230 LEU C C 177.98 0.1 1 1069 . 230 LEU CA C 55.82 0.1 1 1070 . 230 LEU CB C 42.35 0.1 1 1071 . 230 LEU N N 123.01 0.1 1 1072 . 231 GLY H H 7.31 0.01 1 1073 . 231 GLY C C 176.26 0.1 1 1074 . 231 GLY CA C 47.91 0.1 1 1075 . 231 GLY N N 104.14 0.1 1 1076 . 232 ASN H H 8.34 0.01 1 1077 . 232 ASN C C 177.20 0.1 1 1078 . 232 ASN CA C 56.63 0.1 1 1079 . 232 ASN CB C 38.13 0.1 1 1080 . 232 ASN N N 121.50 0.1 1 1081 . 233 ALA H H 7.90 0.01 1 1082 . 233 ALA C C 180.90 0.1 1 1083 . 233 ALA CA C 54.91 0.1 1 1084 . 233 ALA CB C 17.74 0.1 1 1085 . 233 ALA N N 122.73 0.1 1 1086 . 234 VAL H H 8.35 0.01 1 1087 . 234 VAL C C 177.36 0.1 1 1088 . 234 VAL CA C 65.69 0.1 1 1089 . 234 VAL CB C 30.88 0.1 1 1090 . 234 VAL N N 117.27 0.1 1 1091 . 235 ASN H H 7.90 0.01 1 1092 . 235 ASN C C 177.56 0.1 1 1093 . 235 ASN CA C 56.92 0.1 1 1094 . 235 ASN CB C 38.40 0.1 1 1095 . 235 ASN N N 120.10 0.1 1 1096 . 236 LEU H H 7.77 0.01 1 1097 . 236 LEU C C 179.68 0.1 1 1098 . 236 LEU CA C 57.64 0.1 1 1099 . 236 LEU CB C 40.51 0.1 1 1100 . 236 LEU N N 118.48 0.1 1 1101 . 237 ALA H H 7.79 0.01 1 1102 . 237 ALA C C 178.82 0.1 1 1103 . 237 ALA CA C 54.86 0.1 1 1104 . 237 ALA CB C 18.34 0.1 1 1105 . 237 ALA N N 121.53 0.1 1 1106 . 238 VAL H H 8.22 0.01 1 1107 . 238 VAL C C 177.77 0.1 1 1108 . 238 VAL CA C 67.78 0.1 1 1109 . 238 VAL CB C 30.97 0.1 1 1110 . 238 VAL N N 119.21 0.1 1 1111 . 239 LEU H H 7.87 0.01 1 1112 . 239 LEU C C 180.23 0.1 1 1113 . 239 LEU CA C 58.12 0.1 1 1114 . 239 LEU CB C 40.78 0.1 1 1115 . 239 LEU N N 119.80 0.1 1 1116 . 240 LYS H H 7.93 0.01 1 1117 . 240 LYS C C 178.97 0.1 1 1118 . 240 LYS CA C 58.17 0.1 1 1119 . 240 LYS CB C 30.58 0.1 1 1120 . 240 LYS N N 121.29 0.1 1 1121 . 241 LEU H H 8.48 0.01 1 1122 . 241 LEU C C 180.21 0.1 1 1123 . 241 LEU CA C 57.58 0.1 1 1124 . 241 LEU CB C 40.45 0.1 1 1125 . 241 LEU N N 119.89 0.1 1 1126 . 242 ASN H H 8.43 0.01 1 1127 . 242 ASN C C 179.55 0.1 1 1128 . 242 ASN CA C 56.07 0.1 1 1129 . 242 ASN CB C 38.83 0.1 1 1130 . 242 ASN N N 118.42 0.1 1 1131 . 243 GLU H H 8.33 0.01 1 1132 . 243 GLU C C 178.47 0.1 1 1133 . 243 GLU CA C 59.11 0.1 1 1134 . 243 GLU CB C 29.02 0.1 1 1135 . 243 GLU N N 122.84 0.1 1 1136 . 244 GLN H H 8.03 0.01 1 1137 . 244 GLN C C 176.75 0.1 1 1138 . 244 GLN CA C 56.06 0.1 1 1139 . 244 GLN CB C 29.17 0.1 1 1140 . 244 GLN N N 115.32 0.1 1 1141 . 245 GLY H H 7.86 0.01 1 1142 . 245 GLY C C 176.06 0.1 1 1143 . 245 GLY CA C 45.40 0.1 1 1144 . 245 GLY N N 108.11 0.1 1 1145 . 246 LEU H H 7.81 0.01 1 1146 . 246 LEU C C 179.04 0.1 1 1147 . 246 LEU CA C 57.18 0.1 1 1148 . 246 LEU CB C 41.45 0.1 1 1149 . 246 LEU N N 121.57 0.1 1 1150 . 247 LEU H H 7.30 0.01 1 1151 . 247 LEU C C 180.58 0.1 1 1152 . 247 LEU CA C 58.03 0.1 1 1153 . 247 LEU CB C 38.18 0.1 1 1154 . 247 LEU N N 117.17 0.1 1 1155 . 248 ASP H H 7.79 0.01 1 1156 . 248 ASP C C 178.42 0.1 1 1157 . 248 ASP CA C 57.30 0.1 1 1158 . 248 ASP CB C 40.28 0.1 1 1159 . 248 ASP N N 121.78 0.1 1 1160 . 249 LYS H H 7.56 0.01 1 1161 . 249 LYS C C 180.28 0.1 1 1162 . 249 LYS CA C 59.72 0.1 1 1163 . 249 LYS CB C 31.88 0.1 1 1164 . 249 LYS N N 120.90 0.1 1 1165 . 250 LEU H H 8.50 0.01 1 1166 . 250 LEU C C 179.67 0.1 1 1167 . 250 LEU CA C 57.57 0.1 1 1168 . 250 LEU CB C 42.46 0.1 1 1169 . 250 LEU N N 120.52 0.1 1 1170 . 251 LYS H H 8.16 0.01 1 1171 . 251 LYS C C 178.80 0.1 1 1172 . 251 LYS CA C 59.49 0.1 1 1173 . 251 LYS CB C 30.94 0.1 1 1174 . 251 LYS N N 122.41 0.1 1 1175 . 252 ASN H H 8.17 0.01 1 1176 . 252 ASN C C 177.02 0.1 1 1177 . 252 ASN CA C 56.51 0.1 1 1178 . 252 ASN CB C 37.81 0.1 1 1179 . 252 ASN N N 118.56 0.1 1 1180 . 253 LYS H H 8.00 0.01 1 1181 . 253 LYS C C 178.05 0.1 1 1182 . 253 LYS CA C 58.94 0.1 1 1183 . 253 LYS CB C 32.70 0.1 1 1184 . 253 LYS N N 119.71 0.1 1 1185 . 254 TRP H H 7.69 0.01 1 1186 . 254 TRP C C 175.70 0.1 1 1187 . 254 TRP CA C 58.62 0.1 1 1188 . 254 TRP CB C 30.30 0.1 1 1189 . 254 TRP N N 116.09 0.1 1 1190 . 255 TRP H H 8.90 0.01 1 1191 . 255 TRP C C 177.18 0.1 1 1192 . 255 TRP CA C 60.78 0.1 1 1193 . 255 TRP CB C 30.03 0.1 1 1194 . 255 TRP N N 121.02 0.1 1 1195 . 256 TYR H H 7.19 0.01 1 1196 . 256 TYR C C 176.85 0.1 1 1197 . 256 TYR CA C 58.88 0.1 1 1198 . 256 TYR CB C 38.33 0.1 1 1199 . 256 TYR N N 119.19 0.1 1 1200 . 257 ASP H H 8.50 0.01 1 1201 . 257 ASP C C 176.40 0.1 1 1202 . 257 ASP CA C 55.07 0.1 1 1203 . 257 ASP CB C 40.34 0.1 1 1204 . 257 ASP N N 123.94 0.1 1 1205 . 258 LYS H H 8.00 0.01 1 1206 . 258 LYS C C 176.82 0.1 1 1207 . 258 LYS CA C 55.34 0.1 1 1208 . 258 LYS CB C 31.60 0.1 1 1209 . 258 LYS N N 120.70 0.1 1 1210 . 259 GLY H H 8.17 0.01 1 1211 . 259 GLY C C 175.70 0.1 1 1212 . 259 GLY CA C 46.11 0.1 1 1213 . 259 GLY N N 109.34 0.1 1 1214 . 260 GLU H H 8.46 0.01 1 1215 . 260 GLU C C 177.20 0.1 1 1216 . 260 GLU CA C 56.84 0.1 1 1217 . 260 GLU CB C 31.10 0.1 1 1218 . 260 GLU N N 120.31 0.1 1 1219 . 261 CYS H H 8.36 0.01 1 1220 . 261 CYS C C 175.91 0.1 1 1221 . 261 CYS CA C 53.30 0.1 1 1222 . 261 CYS CB C 39.14 0.1 1 1223 . 261 CYS N N 117.64 0.1 1 1224 . 262 GLY H H 8.26 0.01 1 1225 . 262 GLY C C 173.40 0.1 1 1226 . 262 GLY CA C 45.23 0.1 1 1227 . 262 GLY N N 111.53 0.1 1 1228 . 263 SER H H 7.89 0.01 1 1229 . 263 SER C C 178.82 0.1 1 1230 . 263 SER CA C 59.57 0.1 1 1231 . 263 SER CB C 64.47 0.1 1 1232 . 263 SER N N 121.98 0.1 1 stop_ save_