data_5736 #Corrected using PDB structure: 1ZYIA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 98 E CA 62.71 54.92 #101 E CA 64.07 57.69 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 68 P CB 37.66 32.51 # 75 V CB 30.52 35.53 # 80 N CB 38.74 45.78 #101 E CB 35.91 29.92 #137 C CB 26.56 31.76 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 33 E N 134.68 122.50 # 42 G N 108.18 118.95 # 67 Y N 119.20 131.69 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 47 Y H 9.77 7.73 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A -0.53 0.05 -0.27 0.37 -0.04 # #bmr5736.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5736.str file): #HA CA CB CO N HN #N/A -0.24 -0.24 -0.27 +0.37 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.18 +/-0.23 +/-0.17 +/-0.50 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.935 0.988 0.811 0.694 0.509 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.918 1.119 0.793 2.390 0.346 # #*Note: CA and CB offsets differences were greater than 0.5ppm, # Please check for possible misassignment or deuterate effects ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific resonance assignments of ICln, an ion channel cloned from epithelial cells ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schedlbauer Andreas . . 2 Kontaxis Georg . . 3 Konig Matthias . . 4 Furst Johannes . . 5 Botta Guido . . 6 Paulmichl Markus . . 7 Konrat Robert . . stop_ _BMRB_accession_number 5736 _BMRB_flat_file_name bmr5736.str _Entry_type new _Submission_date 2003-03-14 _Accession_date 2003-03-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 114 '13C chemical shifts' 349 '15N chemical shifts' 110 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Sequence-specific Resonance Assignments of ICln, an ion channel cloned from epithelial Cells ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 22874490 _PubMed_ID 14512740 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schedlbauer Andreas . . 2 Kontaxis Georg . . 3 Konig Matthias . . 4 Furst Johannes . . 5 Jakab Martin . . 6 Ritter Markus . . 7 Garavaglia Lisa . . 8 Botta Guido . . 9 Meyer Giuliano . . 10 Paulmichl Markus . . 11 Konrat Robert . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 27 _Journal_issue 4 _Page_first 399 _Page_last 400 _Year 2003 loop_ _Keyword "swelling dependent ion channel" "chloride channel" "NMR assignments" "protein structure" stop_ save_ ################################## # Molecular system description # ################################## save_system_ICln _Saveframe_category molecular_system _Mol_system_name ICln _Abbreviation_common ICln _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "ICln monomer" $ICln stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function "swelling dependent in channel" stop_ save_ ######################## # Monomeric polymers # ######################## save_ICln _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ICln _Name_variant . _Abbreviation_common ICln _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; MHHHHHHLEMSFLKSFPPPG SAEGLRQQQPETEAVLNGKG LGTGTLYIAESRLSWLDGSG LGFSLEYPTISLHAVSRDLN AYPREHLYVMVNAKFGEESK ESVAEEEDSDDDVEPIAEFR FVPSDKSALEAMFTAMCECQ ALHPDPEDEDSDDYDGEEYD VEAHEQGQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 LEU 9 GLU 10 MET 11 SER 12 PHE 13 LEU 14 LYS 15 SER 16 PHE 17 PRO 18 PRO 19 PRO 20 GLY 21 SER 22 ALA 23 GLU 24 GLY 25 LEU 26 ARG 27 GLN 28 GLN 29 GLN 30 PRO 31 GLU 32 THR 33 GLU 34 ALA 35 VAL 36 LEU 37 ASN 38 GLY 39 LYS 40 GLY 41 LEU 42 GLY 43 THR 44 GLY 45 THR 46 LEU 47 TYR 48 ILE 49 ALA 50 GLU 51 SER 52 ARG 53 LEU 54 SER 55 TRP 56 LEU 57 ASP 58 GLY 59 SER 60 GLY 61 LEU 62 GLY 63 PHE 64 SER 65 LEU 66 GLU 67 TYR 68 PRO 69 THR 70 ILE 71 SER 72 LEU 73 HIS 74 ALA 75 VAL 76 SER 77 ARG 78 ASP 79 LEU 80 ASN 81 ALA 82 TYR 83 PRO 84 ARG 85 GLU 86 HIS 87 LEU 88 TYR 89 VAL 90 MET 91 VAL 92 ASN 93 ALA 94 LYS 95 PHE 96 GLY 97 GLU 98 GLU 99 SER 100 LYS 101 GLU 102 SER 103 VAL 104 ALA 105 GLU 106 GLU 107 GLU 108 ASP 109 SER 110 ASP 111 ASP 112 ASP 113 VAL 114 GLU 115 PRO 116 ILE 117 ALA 118 GLU 119 PHE 120 ARG 121 PHE 122 VAL 123 PRO 124 SER 125 ASP 126 LYS 127 SER 128 ALA 129 LEU 130 GLU 131 ALA 132 MET 133 PHE 134 THR 135 ALA 136 MET 137 CYS 138 GLU 139 CYS 140 GLN 141 ALA 142 LEU 143 HIS 144 PRO 145 ASP 146 PRO 147 GLU 148 ASP 149 GLU 150 ASP 151 SER 152 ASP 153 ASP 154 TYR 155 ASP 156 GLY 157 GLU 158 GLU 159 TYR 160 ASP 161 VAL 162 GLU 163 ALA 164 HIS 165 GLU 166 GLN 167 GLY 168 GLN stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-28 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 EMBL CAA46447.1 "chloride channel [Canis familiaris]" 71.49 235 100 100 1e-88 PIR S23401 "chloride channel protein - dog" 71.49 235 99 100 3e-88 PRF 1808296A "Cl channel" 71.49 235 99 99 2e-87 SWISS-PROT P35521 "ICLN_CANFA Methylosome subunit pICln (Chlorideconductance regulatory protein ICln) (I(Cln)) (Chloridechannel, nucleotide sensitive 1A)" 71.49 235 100 100 1e-88 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 $ICln Dog 9615 Eukaryota Metazoa Canis familiaris kidney 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 $ICln 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_max_value _Isotopic_labeling $ICln . mM 1 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N HSQC 3D HNCO 3D HNCACB 3D CBCACONH ; save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "ICln monomer" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 12 PHE N N 119.77 0.10 . 2 12 PHE H H 7.77 0.01 . 3 12 PHE CA C 47.07 0.10 . 4 12 PHE CB C 39.16 0.10 . 5 12 PHE C C 174.70 0.10 . 6 13 LEU N N 121.11 0.10 . 7 13 LEU H H 7.56 0.01 . 8 13 LEU CA C 54.53 0.10 . 10 13 LEU C C 176.30 0.10 . 11 14 LYS N N 121.54 0.10 . 12 14 LYS H H 9.40 0.01 . 13 14 LYS CA C 54.66 0.10 . 14 14 LYS CB C 36.60 0.10 . 15 14 LYS C C 174.85 0.10 . 16 15 SER N N 115.60 0.10 . 17 15 SER H H 8.61 0.01 . 18 15 SER CA C 57.45 0.10 . 19 15 SER CB C 63.79 0.10 . 20 15 SER C C 174.26 0.10 . 21 16 PHE N N 122.21 0.10 . 22 16 PHE H H 6.82 0.01 . 23 16 PHE CA C 54.83 0.10 . 24 16 PHE CB C 37.24 0.10 . 25 19 PRO CA C 62.49 0.10 . 26 19 PRO CB C 32.26 0.10 . 27 19 PRO C C 175.10 0.10 . 28 20 GLY N N 109.29 0.10 . 29 20 GLY H H 8.66 0.01 . 30 20 GLY CA C 44.07 0.10 . 31 22 ALA CA C 54.27 0.10 . 32 22 ALA CB C 17.86 0.10 . 33 22 ALA C C 178.14 0.10 . 34 23 GLU N N 116.56 0.10 . 35 23 GLU H H 7.49 0.01 . 36 23 GLU CA C 56.88 0.10 . 37 23 GLU CB C 29.56 0.10 . 39 24 GLY N N 108.60 0.10 . 40 24 GLY H H 8.02 0.01 . 41 24 GLY CA C 47.07 0.10 . 42 24 GLY C C 175.69 0.10 . 43 25 LEU N N 121.50 0.10 . 44 25 LEU H H 7.61 0.01 . 45 25 LEU CA C 57.10 0.10 . 46 25 LEU CB C 41.79 0.10 . 47 25 LEU C C 175.74 0.10 . 48 26 ARG N N 127.16 0.10 . 49 26 ARG H H 9.00 0.01 . 50 26 ARG CA C 62.85 0.10 . 51 26 ARG CB C 31.81 0.10 . 52 26 ARG C C 175.28 0.10 . 53 27 GLN N N 119.16 0.10 . 54 27 GLN H H 7.77 0.01 . 55 27 GLN CA C 55.91 0.10 . 57 27 GLN C C 172.35 0.10 . 58 28 GLN N N 124.93 0.10 . 59 28 GLN H H 8.64 0.01 . 60 28 GLN CA C 53.03 0.10 . 61 28 GLN CB C 32.10 0.10 . 62 30 PRO CA C 62.34 0.10 . 63 30 PRO CB C 33.33 0.10 . 64 30 PRO C C 174.09 0.10 . 65 31 GLU N N 116.87 0.10 . 66 31 GLU H H 8.94 0.01 . 67 31 GLU CA C 56.75 0.10 . 69 31 GLU C C 175.35 0.10 . 70 32 THR N N 116.23 0.10 . 71 32 THR H H 9.75 0.01 . 72 32 THR CA C 62.23 0.10 . 73 32 THR CB C 69.62 0.10 . 74 32 THR C C 175.78 0.10 . 75 33 GLU N N 134.68 0.10 . 76 33 GLU H H 8.92 0.01 . 77 33 GLU CA C 55.77 0.10 . 79 33 GLU C C 175.40 0.10 . 80 34 ALA N N 125.99 0.10 . 81 34 ALA H H 7.72 0.01 . 82 34 ALA CA C 50.17 0.10 . 83 34 ALA CB C 19.20 0.10 . 84 35 VAL N N 123.54 0.10 . 85 35 VAL H H 8.36 0.01 . 86 35 VAL CA C 60.44 0.10 . 87 35 VAL CB C 34.05 0.10 . 88 35 VAL C C 174.00 0.10 . 89 36 LEU N N 128.22 0.10 . 90 36 LEU H H 8.56 0.01 . 91 36 LEU CA C 52.52 0.10 . 92 36 LEU CB C 43.73 0.10 . 93 36 LEU C C 175.27 0.10 . 94 37 ASN N N 129.17 0.10 . 95 37 ASN H H 9.40 0.01 . 96 37 ASN CA C 53.73 0.10 . 97 37 ASN CB C 36.67 0.10 . 98 37 ASN C C 177.68 0.10 . 99 38 GLY N N 102.77 0.10 . 100 38 GLY H H 8.41 0.01 . 101 38 GLY CA C 45.32 0.10 . 102 38 GLY C C 173.25 0.10 . 103 39 LYS N N 123.77 0.10 . 104 39 LYS H H 8.01 0.01 . 105 39 LYS CA C 54.57 0.10 . 106 39 LYS CB C 33.34 0.10 . 107 39 LYS C C 175.06 0.10 . 108 40 GLY N N 114.33 0.10 . 109 40 GLY H H 8.90 0.01 . 110 40 GLY CA C 46.79 0.10 . 111 40 GLY C C 174.42 0.10 . 112 41 LEU N N 124.93 0.10 . 113 41 LEU H H 9.27 0.01 . 114 41 LEU CA C 54.30 0.10 . 115 41 LEU CB C 42.91 0.10 . 116 41 LEU C C 175.96 0.10 . 117 42 GLY N N 108.18 0.10 . 118 42 GLY H H 8.26 0.01 . 119 42 GLY CA C 43.57 0.10 . 120 42 GLY C C 172.08 0.10 . 121 43 THR N N 114.11 0.10 . 122 43 THR H H 8.66 0.01 . 123 43 THR CA C 62.66 0.10 . 124 43 THR CB C 69.92 0.10 . 125 43 THR C C 173.57 0.10 . 126 44 GLY N N 114.96 0.10 . 127 44 GLY H H 8.27 0.01 . 128 44 GLY CA C 45.64 0.10 . 129 44 GLY C C 171.00 0.10 . 130 45 THR N N 118.99 0.10 . 131 45 THR H H 8.15 0.01 . 132 45 THR CA C 60.66 0.10 . 133 45 THR CB C 70.43 0.10 . 134 45 THR C C 171.41 0.10 . 135 46 LEU N N 126.41 0.10 . 136 46 LEU H H 8.04 0.01 . 137 46 LEU CA C 52.92 0.10 . 138 46 LEU CB C 45.61 0.10 . 139 46 LEU C C 173.53 0.10 . 140 47 TYR N N 125.78 0.10 . 141 47 TYR H H 9.81 0.01 . 142 47 TYR CA C 57.24 0.10 . 144 47 TYR C C 174.92 0.10 . 145 48 ILE N N 124.29 0.10 . 146 48 ILE H H 9.05 0.01 . 147 48 ILE CA C 61.41 0.10 . 148 48 ILE CB C 37.37 0.10 . 149 48 ILE C C 173.49 0.10 . 150 49 ALA N N 128.75 0.10 . 151 49 ALA H H 7.32 0.01 . 152 49 ALA CA C 48.95 0.10 . 154 49 ALA C C 175.89 0.10 . 155 50 GLU N N 122.11 0.10 . 156 50 GLU H H 8.60 0.01 . 157 50 GLU CA C 60.16 0.10 . 158 50 GLU CB C 29.30 0.10 . 159 50 GLU C C 177.45 0.10 . 160 51 SER N N 109.03 0.10 . 161 51 SER H H 8.01 0.01 . 162 51 SER CA C 60.44 0.10 . 164 51 SER C C 174.64 0.10 . 165 52 ARG N N 115.71 0.10 . 166 52 ARG H H 7.24 0.01 . 167 52 ARG CA C 54.92 0.10 . 168 52 ARG CB C 30.06 0.10 . 169 52 ARG C C 172.56 0.10 . 170 53 LEU N N 123.02 0.10 . 171 53 LEU H H 7.65 0.01 . 172 53 LEU CA C 53.88 0.10 . 173 53 LEU CB C 44.05 0.10 . 174 53 LEU C C 176.10 0.10 . 175 54 SER N N 119.42 0.10 . 176 54 SER H H 9.21 0.01 . 177 54 SER CA C 57.90 0.10 . 178 54 SER CB C 66.87 0.10 . 179 54 SER C C 170.16 0.10 . 180 55 TRP N N 126.08 0.10 . 181 55 TRP H H 8.78 0.01 . 182 55 TRP CA C 56.46 0.10 . 183 55 TRP CB C 32.23 0.10 . 184 55 TRP C C 174.00 0.10 . 185 56 LEU N N 125.14 0.10 . 186 56 LEU H H 7.50 0.01 . 187 56 LEU CA C 53.32 0.10 . 188 56 LEU CB C 48.32 0.10 . 191 57 ASP H H 8.95 0.01 . 192 57 ASP CA C 52.24 0.10 . 193 57 ASP CB C 40.82 0.10 . 194 57 ASP C C 177.64 0.10 . 195 58 GLY N N 105.82 0.10 . 196 58 GLY H H 8.47 0.01 . 197 58 GLY CA C 46.53 0.10 . 198 58 GLY C C 174.96 0.10 . 199 59 SER N N 117.51 0.10 . 200 59 SER H H 8.80 0.01 . 201 59 SER CA C 57.83 0.10 . 202 59 SER CB C 64.21 0.10 . 203 59 SER C C 174.16 0.10 . 204 60 GLY N N 110.82 0.10 . 205 60 GLY H H 8.03 0.01 . 206 60 GLY CA C 45.79 0.10 . 207 60 GLY C C 172.27 0.10 . 208 61 LEU N N 122.38 0.10 . 209 61 LEU H H 7.97 0.01 . 210 61 LEU CA C 52.83 0.10 . 211 61 LEU CB C 44.12 0.10 . 214 62 GLY H H 9.19 0.01 . 215 62 GLY CA C 47.12 0.10 . 216 62 GLY C C 172.03 0.10 . 217 63 PHE N N 117.08 0.10 . 218 63 PHE H H 9.03 0.01 . 219 63 PHE CA C 56.10 0.10 . 220 63 PHE CB C 41.79 0.10 . 221 63 PHE C C 172.17 0.10 . 222 64 SER N N 114.11 0.10 . 223 64 SER H H 8.74 0.01 . 224 64 SER CA C 56.63 0.10 . 225 64 SER CB C 66.38 0.10 . 226 64 SER C C 172.10 0.10 . 227 65 LEU N N 121.54 0.10 . 228 65 LEU H H 9.16 0.01 . 229 65 LEU CA C 52.48 0.10 . 230 65 LEU CB C 44.63 0.10 . 232 66 GLU N N 120.26 0.10 . 233 66 GLU H H 8.73 0.01 . 234 66 GLU CA C 54.61 0.10 . 235 66 GLU CB C 30.40 0.10 . 238 67 TYR H H 7.35 0.01 . 239 67 TYR CA C 53.33 0.10 . 240 67 TYR CB C 40.50 0.10 . 241 68 PRO CA C 65.53 0.10 . 242 68 PRO CB C 37.37 0.10 . 243 68 PRO C C 176.72 0.10 . 244 69 THR N N 104.87 0.10 . 245 69 THR H H 7.57 0.01 . 246 69 THR CA C 61.89 0.10 . 247 69 THR CB C 69.77 0.10 . 248 69 THR C C 173.55 0.10 . 249 70 ILE N N 123.66 0.10 . 250 70 ILE H H 7.82 0.01 . 251 70 ILE CA C 62.02 0.10 . 252 70 ILE CB C 38.12 0.10 . 253 70 ILE C C 175.47 0.10 . 254 71 SER N N 125.56 0.10 . 255 71 SER H H 8.92 0.01 . 256 71 SER CA C 58.93 0.10 . 257 71 SER CB C 64.11 0.10 . 260 72 LEU H H 7.65 0.01 . 261 72 LEU CA C 55.82 0.10 . 262 72 LEU CB C 45.82 0.10 . 263 73 HIS H H 8.13 0.01 . 264 73 HIS CA C 55.10 0.10 . 265 73 HIS CB C 34.72 0.10 . 266 73 HIS C C 173.26 0.10 . 267 74 ALA N N 122.17 0.10 . 268 74 ALA H H 9.34 0.01 . 269 74 ALA CA C 52.07 0.10 . 270 74 ALA CB C 22.70 0.10 . 271 74 ALA C C 177.47 0.10 . 272 75 VAL N N 120.08 0.10 . 273 75 VAL H H 8.40 0.01 . 274 75 VAL CA C 56.64 0.10 . 275 75 VAL CB C 30.23 0.10 . 276 75 VAL C C 176.31 0.10 . 277 76 SER N N 117.53 0.10 . 278 76 SER H H 8.45 0.01 . 279 76 SER CA C 58.22 0.10 . 280 76 SER CB C 63.47 0.10 . 281 77 ARG N N 124.29 0.10 . 282 77 ARG H H 8.43 0.01 . 283 77 ARG CA C 56.45 0.10 . 284 77 ARG CB C 32.70 0.10 . 285 78 ASP CA C 53.30 0.10 . 286 78 ASP CB C 40.49 0.10 . 287 78 ASP C C 176.73 0.10 . 288 79 LEU N N 127.16 0.10 . 289 79 LEU H H 8.65 0.01 . 290 79 LEU CA C 55.34 0.10 . 291 79 LEU CB C 39.58 0.10 . 292 79 LEU C C 175.87 0.10 . 293 80 ASN N N 116.66 0.10 . 294 80 ASN H H 8.34 0.01 . 295 80 ASN CA C 54.68 0.10 . 296 80 ASN CB C 38.45 0.10 . 297 80 ASN C C 175.87 0.10 . 298 81 ALA N N 123.02 0.10 . 299 81 ALA H H 7.54 0.01 . 300 81 ALA CA C 53.41 0.10 . 301 81 ALA CB C 19.20 0.10 . 302 81 ALA C C 177.24 0.10 . 303 82 TYR N N 118.35 0.10 . 304 82 TYR H H 7.54 0.01 . 305 82 TYR CA C 56.94 0.10 . 306 82 TYR CB C 41.47 0.10 . 307 83 PRO CA C 65.22 0.10 . 308 83 PRO CB C 31.77 0.10 . 311 84 ARG H H 7.00 0.01 . 312 84 ARG CA C 54.38 0.10 . 313 84 ARG CB C 35.68 0.10 . 314 84 ARG C C 175.52 0.10 . 315 85 GLU N N 127.48 0.10 . 316 85 GLU H H 9.88 0.01 . 317 85 GLU CA C 58.10 0.10 . 321 86 HIS H H 8.73 0.01 . 326 87 LEU H H 8.92 0.01 . 327 87 LEU CA C 53.82 0.10 . 328 87 LEU CB C 44.94 0.10 . 329 87 LEU C C 173.90 0.10 . 330 88 TYR N N 132.56 0.10 . 331 88 TYR H H 9.72 0.01 . 332 88 TYR CA C 56.71 0.10 . 333 88 TYR CB C 40.70 0.10 . 336 89 VAL H H 8.93 0.01 . 337 89 VAL CA C 61.28 0.10 . 338 89 VAL CB C 36.17 0.10 . 339 89 VAL C C 172.75 0.10 . 340 90 MET N N 127.69 0.10 . 341 90 MET H H 9.00 0.01 . 342 90 MET CA C 53.48 0.10 . 343 90 MET CB C 32.49 0.10 . 346 91 VAL H H 9.06 0.01 . 347 91 VAL CA C 60.32 0.10 . 348 91 VAL CB C 35.71 0.10 . 349 91 VAL C C 174.80 0.10 . 350 92 ASN N N 126.41 0.10 . 351 92 ASN H H 9.11 0.01 . 352 92 ASN CA C 52.23 0.10 . 353 92 ASN CB C 37.99 0.10 . 354 92 ASN C C 173.55 0.10 . 355 93 ALA N N 123.45 0.10 . 356 93 ALA H H 7.87 0.01 . 357 93 ALA CA C 51.88 0.10 . 358 93 ALA CB C 21.03 0.10 . 359 93 ALA C C 174.64 0.10 . 360 94 LYS N N 118.78 0.10 . 361 94 LYS H H 8.11 0.01 . 364 95 PHE H H 8.36 0.01 . 369 96 GLY H H 8.33 0.01 . 375 99 SER H H 8.85 0.01 . 382 101 GLU H H 9.14 0.01 . 385 102 SER CA C 58.16 0.10 . 386 102 SER CB C 63.68 0.10 . 387 102 SER C C 174.19 0.10 . 388 103 VAL N N 121.92 0.10 . 389 103 VAL H H 8.14 0.01 . 390 103 VAL CA C 61.79 0.10 . 391 103 VAL CB C 32.58 0.10 . 394 104 ALA H H 8.36 0.01 . 398 105 GLU N N 118.46 0.10 . 399 105 GLU H H 8.25 0.01 . 400 112 ASP C C 175.63 0.10 . 401 113 VAL N N 120.05 0.10 . 402 113 VAL H H 7.88 0.01 . 403 113 VAL CA C 61.80 0.10 . 404 113 VAL CB C 32.80 0.10 . 405 113 VAL C C 175.73 0.10 . 406 114 GLU N N 126.95 0.10 . 407 114 GLU H H 8.50 0.01 . 408 114 GLU CA C 54.11 0.10 . 409 114 GLU CB C 29.74 0.10 . 410 116 ILE N N 119.62 0.10 . 411 116 ILE H H 7.90 0.01 . 412 116 ILE CA C 59.89 0.10 . 413 116 ILE CB C 40.85 0.10 . 414 116 ILE C C 174.83 0.10 . 415 117 ALA N N 129.38 0.10 . 416 117 ALA H H 8.97 0.01 . 417 117 ALA CA C 50.82 0.10 . 418 117 ALA CB C 21.45 0.10 . 419 117 ALA C C 174.55 0.10 . 420 118 GLU H H 8.23 0.01 . 421 118 GLU CA C 54.91 0.10 . 422 118 GLU CB C 32.44 0.10 . 423 118 GLU C C 174.51 0.10 . 424 119 PHE N N 126.41 0.10 . 425 119 PHE H H 9.37 0.01 . 426 119 PHE CA C 56.42 0.10 . 427 119 PHE CB C 42.00 0.10 . 428 119 PHE C C 174.73 0.10 . 429 120 ARG N N 117.51 0.10 . 430 120 ARG H H 8.63 0.01 . 431 120 ARG CA C 53.96 0.10 . 432 120 ARG CB C 31.95 0.10 . 433 120 ARG C C 174.25 0.10 . 434 121 PHE N N 120.69 0.10 . 435 121 PHE H H 9.45 0.01 . 436 121 PHE CA C 56.17 0.10 . 437 121 PHE CB C 40.38 0.10 . 438 121 PHE C C 175.29 0.10 . 439 122 VAL N N 126.95 0.10 . 440 122 VAL H H 9.55 0.01 . 441 122 VAL CA C 58.65 0.10 . 442 122 VAL CB C 32.67 0.10 . 443 123 PRO CA C 62.53 0.10 . 444 123 PRO CB C 31.42 0.10 . 445 123 PRO C C 176.07 0.10 . 446 124 SER N N 119.20 0.10 . 447 124 SER H H 8.71 0.01 . 448 124 SER CA C 63.08 0.10 . 449 124 SER CB C 60.88 0.10 . 450 124 SER C C 174.64 0.10 . 451 125 ASP N N 117.93 0.10 . 452 125 ASP H H 7.62 0.01 . 453 125 ASP CA C 51.64 0.10 . 454 125 ASP CB C 40.07 0.10 . 455 125 ASP C C 174.93 0.10 . 456 126 LYS N N 123.66 0.10 . 457 126 LYS H H 8.56 0.01 . 458 126 LYS CA C 58.06 0.10 . 459 126 LYS CB C 31.54 0.10 . 462 127 SER H H 8.53 0.01 . 463 127 SER CA C 60.72 0.10 . 464 127 SER CB C 62.88 0.10 . 465 127 SER C C 174.90 0.10 . 466 128 ALA N N 124.08 0.10 . 467 128 ALA H H 7.46 0.01 . 468 128 ALA CA C 52.85 0.10 . 469 128 ALA CB C 19.40 0.10 . 470 128 ALA C C 177.51 0.10 . 471 129 LEU N N 117.08 0.10 . 472 129 LEU H H 7.20 0.01 . 473 129 LEU CA C 58.71 0.10 . 474 129 LEU CB C 41.63 0.10 . 475 129 LEU C C 177.88 0.10 . 476 130 GLU N N 118.46 0.10 . 477 130 GLU H H 8.32 0.01 . 478 130 GLU CA C 60.64 0.10 . 479 130 GLU CB C 28.32 0.10 . 480 130 GLU C C 178.66 0.10 . 481 131 ALA N N 124.19 0.10 . 482 131 ALA H H 8.32 0.01 . 483 131 ALA CA C 55.15 0.10 . 484 131 ALA CB C 17.83 0.10 . 485 131 ALA C C 181.13 0.10 . 486 132 MET N N 118.99 0.10 . 487 132 MET H H 8.31 0.01 . 488 132 MET CA C 59.20 0.10 . 489 132 MET CB C 35.40 0.10 . 492 133 PHE H H 8.57 0.01 . 497 134 THR H H 8.92 0.01 . 502 135 ALA H H 7.99 0.01 . 503 135 ALA CA C 55.16 0.10 . 504 135 ALA CB C 18.22 0.10 . 505 135 ALA C C 179.18 0.10 . 506 136 MET N N 117.93 0.10 . 507 136 MET H H 8.11 0.01 . 508 136 MET CA C 59.57 0.10 . 509 136 MET CB C 31.71 0.10 . 512 137 CYS H H 7.97 0.01 . 515 138 GLU H H 8.12 0.01 . 520 139 CYS H H 7.87 0.01 . 525 140 GLN H H 8.10 0.01 . 530 141 ALA H H 7.25 0.01 . 535 142 LEU H H 7.20 0.01 . 540 143 HIS H H 7.74 0.01 . 543 146 PRO CA C 63.38 0.10 . 544 146 PRO CB C 32.09 0.10 . 547 147 GLU H H 8.57 0.01 . 550 155 ASP CA C 53.92 0.10 . 551 155 ASP CB C 41.26 0.10 . 552 155 ASP C C 176.04 0.10 . 553 156 GLY N N 109.03 0.10 . 554 156 GLY H H 7.60 0.01 . 555 156 GLY CA C 45.28 0.10 . 558 157 GLU H H 7.91 0.01 . 565 163 ALA H H 8.10 0.01 . 572 167 GLY H H 8.49 0.01 . stop_ save_