data_5009 #Corrected using PDB structure: 1SCEB # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 39 R HA 4.31 5.01 # 40 H HA 5.71 4.94 # 84 M HA 3.39 4.33 # 91 E HA 4.95 4.20 # 98 K HA 5.94 4.80 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.06 -0.30 -0.33 -0.05 0.06 -0.15 # #bmr5009.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5009.str file): #HA CA CB CO N HN #N/A -0.31 -0.31 -0.05 +0.06 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.16 +/-0.15 +/-0.17 +/-0.40 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.846 0.955 0.995 0.788 0.792 0.551 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.148 0.805 0.705 0.824 1.888 0.363 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H,13C and 15N backbone resonances of p13suc1 proteins -- PA90 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Odaert Benoit . . 2 Landrieu Isabelle . . 3 Dijkstra Klaas . . 4 Schuurman-wolters Gea . . 5 Casteels Peter . . 6 Wieruszeski Jean-Michel . . 7 Scheek Ruud M. . 8 Lippens Guy . . stop_ _BMRB_accession_number 5009 _BMRB_flat_file_name bmr5009.str _Entry_type new _Submission_date 2001-05-09 _Accession_date 2001-05-09 _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' 710 '13C chemical shifts' 524 '15N chemical shifts' 120 stop_ loop_ _Related_BMRB_accession_number _Relationship 5008 "wild type" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Odaert Benoit . . 2 Landrieu Isabelle . . 3 Dijkstra Klaas . . 4 Schuurman-Wolters Gea . . 5 Casteels Peter . . 6 Wieruszeski Jean-Michel . . 7 Scheek Ruud M. . 8 Lippens Guy . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_name_full . _Journal_volume 23 _Journal_issue 2 _Page_first 155 _Page_last 156 _Year 2002 loop_ _Keyword "Cell division" "domain swapping" "protein folding" "p13suc1" "NMR spectroscopy" stop_ save_ ################################## # Molecular system description # ################################## save_system_suc1 _Saveframe_category molecular_system _Mol_system_name p13suc1 _Abbreviation_common suc1 loop_ _Mol_system_component_name _Mol_label "p13 P90A mutant" $P13PA90 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' save_ ######################## # Monomeric polymers # ######################## save_P13PA90 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common suc1 _Name_variant 'p13suc1 P90A mutant' _Abbreviation_common suc1 _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; MSKSGVPRLLTASERERLEP FIDQIHYSPRYADDEYEYRH VMLPKAMLKAIPTDYFNPET GTLRILQEEEWRGLGITQSL GWEMYEVHVAEPHILLFKRE KDYQMKFSQQRGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LYS 4 SER 5 GLY 6 VAL 7 PRO 8 ARG 9 LEU 10 LEU 11 THR 12 ALA 13 SER 14 GLU 15 ARG 16 GLU 17 ARG 18 LEU 19 GLU 20 PRO 21 PHE 22 ILE 23 ASP 24 GLN 25 ILE 26 HIS 27 TYR 28 SER 29 PRO 30 ARG 31 TYR 32 ALA 33 ASP 34 ASP 35 GLU 36 TYR 37 GLU 38 TYR 39 ARG 40 HIS 41 VAL 42 MET 43 LEU 44 PRO 45 LYS 46 ALA 47 MET 48 LEU 49 LYS 50 ALA 51 ILE 52 PRO 53 THR 54 ASP 55 TYR 56 PHE 57 ASN 58 PRO 59 GLU 60 THR 61 GLY 62 THR 63 LEU 64 ARG 65 ILE 66 LEU 67 GLN 68 GLU 69 GLU 70 GLU 71 TRP 72 ARG 73 GLY 74 LEU 75 GLY 76 ILE 77 THR 78 GLN 79 SER 80 LEU 81 GLY 82 TRP 83 GLU 84 MET 85 TYR 86 GLU 87 VAL 88 HIS 89 VAL 90 ALA 91 GLU 92 PRO 93 HIS 94 ILE 95 LEU 96 LEU 97 PHE 98 LYS 99 ARG 100 GLU 101 LYS 102 ASP 103 TYR 104 GLN 105 MET 106 LYS 107 PHE 108 SER 109 GLN 110 GLN 111 ARG 112 GLY 113 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-06 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1PUC "P13suc1 In A Strand-Exchanged Dimer" 107.62 105 99 99 2e-56 PDB 1SCE "A Chain A, Mol_id: 1; Molecule: Suc1; Chain: A,B, C, D; Engineered: Yes" 100.89 112 98 98 3e-59 EMBL CAA21308.1 "cyclin-dependent kinases regulatorysubunit; involved in the regulation of CDK activity(PMID 3289755); involved in regulation of mitotic cellcycle (PMID 3289755); similar to S. cerevisiae YBR135W[Schizosaccharomyces pombe]" 100.00 113 99 99 3e-61 GenBank AAA35346.1 "cell division protein" 100.00 113 99 99 3e-61 PIR A26722 "cell division control protein Suc1+ - fissionyeast (Schizosaccharomyces pombe)" 100.00 113 99 99 3e-61 REF NP_595431.1 "cyclin-dependent kinases regulatorysubunit [Schizosaccharomyces pombe]" 100.00 113 99 99 3e-61 SWISS-PROT P08463 "CKS1_SCHPO Cyclin-dependent kinases regulatorysubunit (P13)" 100.00 113 99 99 3e-61 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $P13PA90 'fission yeast' 4896 Eukaryota Fungi Schizosaccharomyces pombe 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 $P13PA90 'recombinat technology' 'E. coli' Escherichia coli BL21(DE3) pRK172 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_min_value _Concentration_max_value _Isotopic_labeling $P13PA90 . mM 1.0 2.0 "[U-15N]" stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $P13PA90 . mM 1.0 2.0 "[U-13C; U-15N]" stop_ save_ ############################ # Computer software used # ############################ save_SNARF _Saveframe_category software _Name SNARF _Version v0.8.9 _Details "Frans van Hoesel." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; HNCA/HNcaCO HNCO/HNcaCO CBCANH/CBCAcoNH CONCOCAH 15N NOESY/TOCSY 13C NOESY/ HCCH TOCSY 15N HSQC 13C HSQC aromatic ; save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 na temperature 293 0.5 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 $sample_2 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "p13 P90A mutant" 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 2 SER HA H 4.13 . . 2 2 SER HB2 H 4.01 . . 3 2 SER HB3 H 4.01 . . 4 2 SER CA C 57.50 . . 5 2 SER CB C 63.72 . . 6 3 LYS H H 8.07 . . 7 3 LYS HA H 4.48 . . 8 3 LYS HB2 H 1.94 . . 9 3 LYS HB3 H 1.86 . . 10 3 LYS HG2 H 1.53 . . 11 3 LYS HG3 H 1.53 . . 12 3 LYS HD2 H 1.76 . . 13 3 LYS HD3 H 1.76 . . 14 3 LYS HE2 H 3.07 . . 15 3 LYS HE3 H 3.07 . . 16 3 LYS C C 176.57 . . 17 3 LYS CA C 56.42 . . 18 3 LYS CB C 32.76 . . 19 3 LYS CG C 24.54 . . 20 3 LYS CD C 28.93 . . 21 3 LYS CE C 41.92 . . 22 3 LYS N N 122.15 . . 23 4 SER H H 8.52 . . 24 4 SER HA H 4.51 . . 25 4 SER HB2 H 3.92 . . 26 4 SER HB3 H 3.92 . . 27 4 SER C C 174.81 . . 28 4 SER CA C 58.47 . . 30 4 SER N N 117.13 . . 31 5 GLY H H 8.39 . . 32 5 GLY HA2 H 4.01 . . 33 5 GLY HA3 H 4.01 . . 34 5 GLY C C 173.55 . . 35 5 GLY CA C 44.92 . . 36 5 GLY N N 110.77 . . 37 6 VAL H H 8.09 . . 38 6 VAL HA H 4.48 . . 39 6 VAL HB H 2.12 . . 40 6 VAL HG1 H 1.01 . . 41 6 VAL HG2 H 0.95 . . 42 6 VAL C C 174.66 . . 43 6 VAL CA C 59.53 . . 44 6 VAL CB C 32.06 . . 45 6 VAL CG1 C 20.86 . . 46 6 VAL CG2 C 19.77 . . 47 6 VAL N N 120.50 . . 48 7 PRO HA H 4.25 . . 49 7 PRO HB2 H 1.94 . . 50 7 PRO HB3 H 1.68 . . 51 7 PRO HG2 H 2.01 . . 52 7 PRO HG3 H 1.96 . . 53 7 PRO HD2 H 3.89 . . 54 7 PRO HD3 H 3.79 . . 55 7 PRO C C 174.67 . . 56 7 PRO CA C 62.55 . . 57 7 PRO CB C 32.76 . . 58 7 PRO CG C 26.85 . . 59 7 PRO CD C 50.48 . . 60 7 PRO N N 139.57 . . 61 8 ARG H H 9.83 . . 62 8 ARG HA H 4.51 . . 63 8 ARG HB2 H 2.15 . . 64 8 ARG HB3 H 1.63 . . 65 8 ARG HG2 H 1.81 . . 66 8 ARG HG3 H 1.72 . . 67 8 ARG HD2 H 3.12 . . 68 8 ARG HD3 H 2.98 . . 69 8 ARG C C 175.14 . . 70 8 ARG CA C 55.40 . . 71 8 ARG CB C 30.26 . . 72 8 ARG CG C 27.86 . . 73 8 ARG CD C 42.02 . . 74 8 ARG N N 127.39 . . 75 9 LEU H H 8.62 . . 76 9 LEU HA H 4.58 . . 77 9 LEU HB2 H 1.67 . . 78 9 LEU HB3 H 1.59 . . 79 9 LEU HG H 1.67 . . 80 9 LEU HD1 H 0.96 . . 81 9 LEU HD2 H 0.78 . . 82 9 LEU C C 177.74 . . 83 9 LEU CA C 53.71 . . 84 9 LEU CB C 41.41 . . 85 9 LEU CG C 27.05 . . 86 9 LEU CD1 C 24.90 . . 87 9 LEU CD2 C 22.35 . . 88 9 LEU N N 127.05 . . 89 10 LEU H H 8.68 . . 90 10 LEU HA H 4.57 . . 91 10 LEU HB2 H 1.75 . . 92 10 LEU HB3 H 1.62 . . 93 10 LEU HG H 2.00 . . 94 10 LEU HD1 H 0.81 . . 95 10 LEU HD2 H 0.67 . . 96 10 LEU C C 179.36 . . 97 10 LEU CA C 54.51 . . 98 10 LEU CB C 42.66 . . 99 10 LEU CG C 26.57 . . 100 10 LEU CD1 C 27.01 . . 101 10 LEU CD2 C 23.70 . . 102 10 LEU N N 122.36 . . 103 11 THR H H 9.52 . . 104 11 THR HA H 4.49 . . 105 11 THR HB H 4.79 . . 106 11 THR HG2 H 1.37 . . 107 11 THR C C 175.41 . . 108 11 THR CA C 60.53 . . 109 11 THR CB C 70.80 . . 110 11 THR CG2 C 21.41 . . 111 11 THR N N 114.82 . . 112 12 ALA H H 9.00 . . 113 12 ALA HA H 4.13 . . 114 12 ALA HB H 1.54 . . 115 12 ALA C C 180.86 . . 116 12 ALA CA C 55.48 . . 117 12 ALA CB C 17.56 . . 118 12 ALA N N 123.04 . . 119 13 SER H H 8.53 . . 120 13 SER HA H 4.30 . . 121 13 SER HB2 H 3.92 . . 122 13 SER HB3 H 3.92 . . 123 13 SER C C 177.60 . . 124 13 SER CA C 60.93 . . 125 13 SER CB C 62.16 . . 126 13 SER N N 112.76 . . 127 14 GLU H H 7.63 . . 128 14 GLU HA H 3.98 . . 129 14 GLU HB2 H 2.48 . . 130 14 GLU HB3 H 1.91 . . 131 14 GLU HG2 H 2.30 . . 132 14 GLU HG3 H 2.30 . . 133 14 GLU C C 179.90 . . 134 14 GLU CA C 58.83 . . 135 14 GLU CB C 30.36 . . 136 14 GLU CG C 36.44 . . 137 14 GLU N N 122.45 . . 138 15 ARG H H 8.64 . . 139 15 ARG HA H 4.01 . . 140 15 ARG HB2 H 2.07 . . 141 15 ARG HB3 H 1.93 . . 142 15 ARG HG2 H 1.79 . . 143 15 ARG HG3 H 1.79 . . 144 15 ARG HD2 H 3.34 . . 145 15 ARG HD3 H 3.34 . . 146 15 ARG C C 179.40 . . 147 15 ARG CA C 59.29 . . 148 15 ARG CB C 29.36 . . 149 15 ARG CG C 27.85 . . 150 15 ARG CD C 42.61 . . 151 15 ARG N N 119.03 . . 152 16 GLU H H 8.22 . . 153 16 GLU HA H 4.16 . . 154 16 GLU HB2 H 2.26 . . 155 16 GLU HB3 H 2.16 . . 156 16 GLU HG2 H 2.49 . . 157 16 GLU HG3 H 2.32 . . 158 16 GLU C C 179.07 . . 159 16 GLU CA C 59.39 . . 160 16 GLU CB C 29.37 . . 161 16 GLU CG C 36.18 . . 162 16 GLU N N 119.95 . . 163 17 ARG H H 7.32 . . 164 17 ARG HA H 4.24 . . 165 17 ARG HB2 H 2.12 . . 166 17 ARG HB3 H 2.12 . . 167 17 ARG HG2 H 2.00 . . 168 17 ARG HG3 H 1.89 . . 169 17 ARG HD2 H 3.42 . . 170 17 ARG HD3 H 3.36 . . 171 17 ARG C C 176.85 . . 172 17 ARG CA C 57.71 . . 173 17 ARG CB C 30.56 . . 174 17 ARG CG C 27.52 . . 175 17 ARG CD C 43.57 . . 176 17 ARG N N 115.85 . . 177 18 LEU H H 7.44 . . 178 18 LEU HA H 4.74 . . 179 18 LEU HB2 H 2.05 . . 180 18 LEU HB3 H 1.72 . . 181 18 LEU HG H 2.00 . . 182 18 LEU HD1 H 0.98 . . 183 18 LEU HD2 H 0.91 . . 184 18 LEU C C 177.53 . . 185 18 LEU CA C 54.86 . . 186 18 LEU CB C 42.20 . . 187 18 LEU CG C 26.68 . . 188 18 LEU CD1 C 27.16 . . 189 18 LEU CD2 C 24.61 . . 190 18 LEU N N 114.82 . . 191 19 GLU H H 7.62 . . 192 19 GLU HA H 4.19 . . 193 19 GLU HB2 H 2.17 . . 194 19 GLU HB3 H 2.25 . . 195 19 GLU HG2 H 2.41 . . 196 19 GLU HG3 H 2.54 . . 197 19 GLU C C 174.92 . . 198 19 GLU CA C 60.53 . . 199 19 GLU CB C 27.50 . . 200 19 GLU CG C 36.01 . . 201 19 GLU N N 120.40 . . 202 20 PRO HA H 4.33 . . 203 20 PRO HB2 H 2.12 . . 204 20 PRO HB3 H 0.75 . . 205 20 PRO HG2 H 1.81 . . 206 20 PRO HG3 H 1.63 . . 207 20 PRO HD2 H 3.74 . . 208 20 PRO HD3 H 3.29 . . 209 20 PRO C C 176.85 . . 210 20 PRO CA C 64.84 . . 211 20 PRO CB C 31.12 . . 212 20 PRO CG C 27.59 . . 213 20 PRO CD C 50.52 . . 214 20 PRO N N 132.99 . . 215 21 PHE H H 7.77 . . 216 21 PHE HA H 4.62 . . 217 21 PHE HB2 H 3.47 . . 218 21 PHE HB3 H 3.10 . . 219 21 PHE HD1 H 7.36 . . 220 21 PHE HD2 H 7.36 . . 221 21 PHE HE1 H 7.36 . . 222 21 PHE HE2 H 7.36 . . 223 21 PHE HZ H 7.26 . . 224 21 PHE C C 177.48 . . 225 21 PHE CA C 58.27 . . 226 21 PHE CB C 40.93 . . 227 21 PHE CD1 C 131.60 . . 228 21 PHE CD2 C 131.60 . . 229 21 PHE CE1 C 130.66 . . 230 21 PHE CE2 C 130.66 . . 231 21 PHE CZ C 129.11 . . 232 21 PHE N N 111.96 . . 233 22 ILE H H 7.39 . . 234 22 ILE HA H 3.76 . . 235 22 ILE HB H 2.04 . . 236 22 ILE HG12 H 1.90 . . 237 22 ILE HG13 H 1.54 . . 238 22 ILE HG2 H 1.13 . . 239 22 ILE HD1 H 0.98 . . 240 22 ILE C C 178.22 . . 241 22 ILE CA C 65.66 . . 242 22 ILE CB C 37.47 . . 243 22 ILE CG1 C 28.60 . . 244 22 ILE CG2 C 16.95 . . 245 22 ILE CD1 C 12.76 . . 246 22 ILE N N 117.77 . . 247 23 ASP H H 8.72 . . 248 23 ASP HA H 4.72 . . 249 23 ASP HB2 H 2.81 . . 250 23 ASP HB3 H 2.81 . . 251 23 ASP C C 176.61 . . 252 23 ASP CA C 55.40 . . 253 23 ASP CB C 39.98 . . 254 23 ASP N N 117.80 . . 255 24 GLN H H 7.89 . . 256 24 GLN HA H 4.49 . . 257 24 GLN HB2 H 2.60 . . 258 24 GLN HB3 H 2.22 . . 259 24 GLN HG2 H 2.48 . . 260 24 GLN HG3 H 2.48 . . 261 24 GLN HE21 H 7.66 . . 262 24 GLN HE22 H 6.86 . . 263 24 GLN C C 175.85 . . 264 24 GLN CA C 55.07 . . 265 24 GLN CB C 29.85 . . 266 24 GLN CG C 33.90 . . 267 24 GLN N N 116.09 . . 268 24 GLN NE2 N 112.53 . . 269 25 ILE H H 7.35 . . 270 25 ILE HA H 3.95 . . 271 25 ILE HB H 1.84 . . 272 25 ILE HG12 H 2.19 . . 273 25 ILE HG13 H 0.89 . . 274 25 ILE HG2 H 0.41 . . 275 25 ILE HD1 H 0.89 . . 276 25 ILE C C 175.00 . . 277 25 ILE CA C 63.85 . . 278 25 ILE CB C 38.15 . . 279 25 ILE CG1 C 28.85 . . 280 25 ILE CG2 C 17.32 . . 281 25 ILE CD1 C 13.71 . . 282 25 ILE N N 122.13 . . 283 26 HIS H H 8.38 . . 284 26 HIS HA H 5.11 . . 285 26 HIS HB2 H 3.25 . . 286 26 HIS HB3 H 3.12 . . 287 26 HIS HD2 H 7.12 . . 288 26 HIS HE1 H 7.98 . . 289 26 HIS C C 172.68 . . 290 26 HIS CA C 54.27 . . 291 26 HIS CB C 32.53 . . 292 26 HIS CD2 C 118.23 . . 293 26 HIS N N 125.79 . . 294 27 TYR H H 8.65 . . 295 27 TYR HA H 4.63 . . 296 27 TYR HB2 H 2.75 . . 297 27 TYR HB3 H 2.54 . . 298 27 TYR HD1 H 6.76 . . 299 27 TYR HD2 H 6.76 . . 300 27 TYR HE1 H 6.45 . . 301 27 TYR HE2 H 6.45 . . 302 27 TYR C C 175.57 . . 303 27 TYR CA C 56.41 . . 304 27 TYR CB C 39.76 . . 305 27 TYR CD1 C 132.84 . . 306 27 TYR CD2 C 132.84 . . 307 27 TYR CE1 C 117.29 . . 308 27 TYR CE2 C 117.29 . . 309 27 TYR N N 123.04 . . 310 28 SER H H 8.85 . . 311 28 SER HA H 4.74 . . 312 28 SER HB2 H 4.34 . . 313 28 SER HB3 H 3.54 . . 314 28 SER C C 171.81 . . 315 28 SER CA C 57.66 . . 316 28 SER CB C 62.37 . . 317 28 SER N N 121.25 . . 318 29 PRO HA H 4.73 . . 319 29 PRO HB2 H 2.54 . . 320 29 PRO HB3 H 1.92 . . 321 29 PRO HG2 H 2.19 . . 322 29 PRO HG3 H 2.13 . . 323 29 PRO HD2 H 4.01 . . 324 29 PRO HD3 H 3.77 . . 325 29 PRO C C 177.00 . . 326 29 PRO CA C 62.82 . . 327 29 PRO CB C 32.01 . . 328 29 PRO CG C 27.54 . . 329 29 PRO CD C 50.33 . . 330 29 PRO N N 134.54 . . 331 30 ARG H H 8.74 . . 332 30 ARG HA H 5.21 . . 333 30 ARG HB2 H 1.98 . . 334 30 ARG HB3 H 1.98 . . 335 30 ARG HG2 H 1.89 . . 336 30 ARG HG3 H 1.84 . . 337 30 ARG HD2 H 3.35 . . 338 30 ARG HD3 H 3.35 . . 339 30 ARG C C 176.38 . . 340 30 ARG CA C 55.61 . . 341 30 ARG CB C 31.99 . . 342 30 ARG CG C 26.95 . . 343 30 ARG CD C 43.97 . . 344 30 ARG N N 122.71 . . 345 31 TYR H H 8.93 . . 346 31 TYR HA H 5.11 . . 347 31 TYR HB2 H 3.19 . . 348 31 TYR HB3 H 3.19 . . 349 31 TYR HD1 H 7.06 . . 350 31 TYR HD2 H 7.06 . . 351 31 TYR HE1 H 6.49 . . 352 31 TYR HE2 H 6.49 . . 353 31 TYR C C 173.16 . . 354 31 TYR CA C 56.53 . . 355 31 TYR CB C 39.84 . . 356 31 TYR CD1 C 133.77 . . 357 31 TYR CD2 C 133.77 . . 358 31 TYR CE1 C 117.60 . . 359 31 TYR CE2 C 117.60 . . 360 31 TYR N N 120.73 . . 361 32 ALA H H 8.77 . . 362 32 ALA HA H 5.65 . . 363 32 ALA HB H 1.60 . . 364 32 ALA C C 177.77 . . 365 32 ALA CA C 51.98 . . 366 32 ALA CB C 23.27 . . 367 32 ALA N N 121.44 . . 368 33 ASP H H 9.00 . . 369 33 ASP HA H 5.01 . . 370 33 ASP HB2 H 3.56 . . 371 33 ASP HB3 H 2.98 . . 372 33 ASP C C 175.88 . . 373 33 ASP CA C 52.65 . . 374 33 ASP CB C 41.53 . . 375 33 ASP N N 122.55 . . 376 34 ASP H H 8.46 . . 377 34 ASP HA H 4.53 . . 378 34 ASP HB2 H 2.82 . . 379 34 ASP HB3 H 2.75 . . 380 34 ASP C C 176.46 . . 381 34 ASP CA C 56.57 . . 382 34 ASP CB C 40.58 . . 383 34 ASP N N 115.82 . . 384 35 GLU H H 8.67 . . 385 35 GLU HA H 4.35 . . 386 35 GLU HB2 H 1.86 . . 387 35 GLU HB3 H 1.66 . . 388 35 GLU HG2 H 2.07 . . 389 35 GLU HG3 H 1.92 . . 390 35 GLU C C 175.46 . . 391 35 GLU CA C 57.60 . . 392 35 GLU CB C 33.71 . . 393 35 GLU CG C 36.59 . . 394 35 GLU N N 118.05 . . 395 36 TYR H H 9.18 . . 396 36 TYR HA H 4.86 . . 397 36 TYR HB2 H 2.39 . . 398 36 TYR HB3 H 2.30 . . 399 36 TYR HD1 H 6.93 . . 400 36 TYR HD2 H 6.93 . . 401 36 TYR HE1 H 6.76 . . 402 36 TYR HE2 H 6.76 . . 403 36 TYR C C 174.08 . . 404 36 TYR CA C 57.68 . . 405 36 TYR CB C 41.73 . . 406 36 TYR CD1 C 133.15 . . 407 36 TYR CD2 C 133.15 . . 408 36 TYR CE1 C 117.60 . . 409 36 TYR CE2 C 117.60 . . 410 36 TYR N N 120.09 . . 411 37 GLU H H 8.68 . . 412 37 GLU HA H 5.11 . . 413 37 GLU HB2 H 1.95 . . 414 37 GLU HB3 H 1.84 . . 415 37 GLU HG2 H 2.13 . . 416 37 GLU HG3 H 2.07 . . 417 37 GLU C C 174.20 . . 418 37 GLU CA C 53.95 . . 419 37 GLU CB C 33.66 . . 420 37 GLU CG C 36.84 . . 421 37 GLU N N 115.14 . . 422 38 TYR H H 9.12 . . 423 38 TYR HA H 5.74 . . 424 38 TYR HB2 H 2.95 . . 425 38 TYR HB3 H 1.45 . . 426 38 TYR HD1 H 6.88 . . 427 38 TYR HD2 H 6.88 . . 428 38 TYR HE1 H 6.36 . . 429 38 TYR HE2 H 6.36 . . 430 38 TYR C C 175.15 . . 431 38 TYR CA C 57.07 . . 432 38 TYR CB C 42.58 . . 433 38 TYR CD1 C 133.46 . . 434 38 TYR CD2 C 133.46 . . 435 38 TYR CE1 C 116.67 . . 436 38 TYR CE2 C 116.67 . . 437 38 TYR N N 116.96 . . 438 39 ARG H H 8.40 . . 439 39 ARG HA H 4.37 . . 440 39 ARG HB2 H 1.41 . . 441 39 ARG HB3 H 1.34 . . 442 39 ARG C C 173.56 . . 443 39 ARG CA C 56.19 . . 444 39 ARG CB C 31.48 . . 445 39 ARG N N 115.57 . . 446 40 HIS H H 9.00 . . 447 40 HIS HA H 5.78 . . 448 40 HIS HB2 H 3.04 . . 449 40 HIS HB3 H 2.93 . . 450 40 HIS HD2 H 6.83 . . 451 40 HIS HE1 H 7.88 . . 452 40 HIS C C 174.15 . . 453 40 HIS CA C 53.70 . . 454 40 HIS CB C 32.41 . . 455 40 HIS CD2 C 118.85 . . 456 40 HIS CE1 C 137.97 . . 457 40 HIS N N 120.73 . . 458 41 VAL H H 9.36 . . 459 41 VAL HA H 4.44 . . 460 41 VAL HB H 1.89 . . 461 41 VAL HG1 H 0.45 . . 462 41 VAL HG2 H 0.41 . . 463 41 VAL C C 173.78 . . 464 41 VAL CA C 60.93 . . 465 41 VAL CB C 34.31 . . 466 41 VAL CG1 C 20.87 . . 467 41 VAL CG2 C 21.80 . . 468 41 VAL N N 123.37 . . 469 42 MET H H 9.19 . . 470 42 MET HA H 5.10 . . 471 42 MET HB2 H 2.15 . . 472 42 MET HB3 H 1.93 . . 473 42 MET HG2 H 2.48 . . 474 42 MET HG3 H 2.34 . . 475 42 MET HE H 2.01 . . 476 42 MET C C 175.45 . . 477 42 MET CA C 54.24 . . 478 42 MET CB C 34.68 . . 479 42 MET CG C 32.06 . . 480 42 MET CE C 16.96 . . 481 42 MET N N 126.24 . . 482 43 LEU H H 9.39 . . 483 43 LEU HA H 4.66 . . 484 43 LEU HB2 H 1.72 . . 485 43 LEU HB3 H 1.60 . . 486 43 LEU HG H 1.86 . . 487 43 LEU HD1 H 0.84 . . 488 43 LEU HD2 H 0.84 . . 489 43 LEU C C 174.71 . . 490 43 LEU CA C 52.02 . . 491 43 LEU CB C 39.82 . . 492 43 LEU CG C 26.30 . . 493 43 LEU CD1 C 25.20 . . 494 43 LEU CD2 C 21.73 . . 495 43 LEU N N 127.08 . . 496 44 PRO HA H 4.61 . . 497 44 PRO HB2 H 2.52 . . 498 44 PRO HB3 H 1.91 . . 499 44 PRO HG2 H 2.36 . . 500 44 PRO HG3 H 2.36 . . 501 44 PRO HD2 H 3.72 . . 502 44 PRO HD3 H 3.59 . . 503 44 PRO C C 178.78 . . 504 44 PRO CA C 62.25 . . 505 44 PRO CB C 31.07 . . 506 44 PRO CG C 28.83 . . 507 44 PRO CD C 49.37 . . 508 44 PRO N N 133.35 . . 509 45 LYS H H 8.69 . . 510 45 LYS HA H 3.60 . . 511 45 LYS HB2 H 1.70 . . 512 45 LYS HB3 H 1.59 . . 513 45 LYS HG2 H 1.25 . . 514 45 LYS HG3 H 0.93 . . 515 45 LYS HD2 H 1.49 . . 516 45 LYS HD3 H 1.49 . . 517 45 LYS HE2 H 2.58 . . 518 45 LYS HE3 H 2.58 . . 519 45 LYS C C 179.87 . . 520 45 LYS CA C 60.83 . . 521 45 LYS CB C 31.67 . . 522 45 LYS CG C 25.78 . . 523 45 LYS CD C 28.94 . . 524 45 LYS CE C 41.40 . . 525 45 LYS N N 126.12 . . 526 46 ALA H H 8.86 . . 527 46 ALA HA H 4.03 . . 528 46 ALA HB H 1.47 . . 529 46 ALA C C 178.83 . . 530 46 ALA CA C 53.93 . . 531 46 ALA CB C 18.67 . . 532 46 ALA N N 118.88 . . 533 47 MET H H 7.51 . . 534 47 MET HA H 2.69 . . 535 47 MET HB2 H 1.99 . . 536 47 MET HB3 H 1.29 . . 537 47 MET HG2 H 2.37 . . 538 47 MET HG3 H 2.30 . . 539 47 MET HE H 2.30 . . 540 47 MET C C 177.79 . . 541 47 MET CA C 57.62 . . 542 47 MET CB C 33.08 . . 543 47 MET CG C 33.08 . . 544 47 MET CE C 19.04 . . 545 47 MET N N 116.76 . . 546 48 LEU H H 7.16 . . 547 48 LEU HA H 3.99 . . 548 48 LEU HB2 H 1.90 . . 549 48 LEU HB3 H 1.75 . . 550 48 LEU HG H 1.80 . . 551 48 LEU HD1 H 1.04 . . 552 48 LEU HD2 H 0.98 . . 553 48 LEU C C 178.68 . . 554 48 LEU CA C 57.99 . . 555 48 LEU CB C 40.99 . . 556 48 LEU CG C 28.04 . . 557 48 LEU CD1 C 24.93 . . 558 48 LEU CD2 C 23.07 . . 559 48 LEU N N 114.98 . . 560 49 LYS H H 6.89 . . 561 49 LYS HA H 4.15 . . 562 49 LYS HB2 H 1.95 . . 563 49 LYS HB3 H 1.81 . . 564 49 LYS HG2 H 1.49 . . 565 49 LYS HG3 H 1.49 . . 566 49 LYS HD2 H 1.69 . . 567 49 LYS HD3 H 1.69 . . 568 49 LYS HE2 H 3.00 . . 569 49 LYS HE3 H 3.00 . . 570 49 LYS C C 176.21 . . 571 49 LYS CA C 57.09 . . 572 49 LYS CB C 31.87 . . 573 49 LYS CG C 24.55 . . 574 49 LYS CD C 28.58 . . 575 49 LYS CE C 41.71 . . 576 49 LYS N N 113.08 . . 577 50 ALA H H 7.46 . . 578 50 ALA HA H 4.51 . . 579 50 ALA HB H 1.47 . . 580 50 ALA C C 175.91 . . 581 50 ALA CA C 51.13 . . 582 50 ALA CB C 20.29 . . 583 50 ALA N N 119.95 . . 584 51 ILE H H 7.02 . . 585 51 ILE HA H 4.10 . . 586 51 ILE HB H 2.06 . . 587 51 ILE HG12 H 2.27 . . 588 51 ILE HG13 H 0.87 . . 589 51 ILE HG2 H 1.01 . . 590 51 ILE HD1 H 0.87 . . 591 51 ILE C C 173.46 . . 592 51 ILE CA C 59.98 . . 593 51 ILE CB C 39.83 . . 594 51 ILE CG1 C 29.34 . . 595 51 ILE CG2 C 17.57 . . 596 51 ILE CD1 C 14.34 . . 597 51 ILE N N 122.34 . . 598 52 PRO HA H 4.48 . . 599 52 PRO HB2 H 2.37 . . 600 52 PRO HB3 H 1.82 . . 601 52 PRO HG2 H 1.70 . . 602 52 PRO HG3 H 1.70 . . 603 52 PRO HD2 H 3.92 . . 604 52 PRO HD3 H 3.06 . . 605 52 PRO C C 177.48 . . 606 52 PRO CA C 63.39 . . 607 52 PRO CB C 32.69 . . 608 52 PRO CG C 28.97 . . 609 52 PRO CD C 50.55 . . 610 52 PRO N N 139.09 . . 611 53 THR H H 8.60 . . 612 53 THR HA H 4.16 . . 613 53 THR HB H 4.27 . . 614 53 THR HG2 H 1.37 . . 615 53 THR C C 176.33 . . 616 53 THR CA C 65.61 . . 617 53 THR CB C 68.80 . . 618 53 THR CG2 C 21.82 . . 619 53 THR N N 115.01 . . 620 54 ASP H H 8.82 . . 621 54 ASP HA H 4.73 . . 622 54 ASP HB2 H 2.75 . . 623 54 ASP HB3 H 2.69 . . 624 54 ASP C C 176.46 . . 625 54 ASP CA C 55.21 . . 626 54 ASP CB C 39.46 . . 627 54 ASP N N 117.43 . . 628 55 TYR H H 8.22 . . 629 55 TYR HA H 4.27 . . 630 55 TYR HB2 H 3.04 . . 631 55 TYR HB3 H 2.87 . . 632 55 TYR HD1 H 6.90 . . 633 55 TYR HD2 H 6.90 . . 634 55 TYR HE1 H 6.71 . . 635 55 TYR HE2 H 6.71 . . 636 55 TYR C C 173.45 . . 637 55 TYR CA C 58.43 . . 638 55 TYR CB C 36.59 . . 639 55 TYR CD1 C 133.46 . . 640 55 TYR CD2 C 133.46 . . 641 55 TYR CE1 C 117.29 . . 642 55 TYR CE2 C 117.29 . . 643 55 TYR N N 119.93 . . 644 56 PHE H H 7.94 . . 645 56 PHE HA H 4.74 . . 646 56 PHE HB2 H 3.13 . . 647 56 PHE HB3 H 2.64 . . 648 56 PHE HD1 H 7.10 . . 649 56 PHE HD2 H 7.10 . . 650 56 PHE HE1 H 7.26 . . 651 56 PHE HE2 H 7.26 . . 652 56 PHE HZ H 7.47 . . 653 56 PHE C C 175.29 . . 654 56 PHE CA C 57.71 . . 655 56 PHE CB C 40.04 . . 656 56 PHE CD1 C 131.60 . . 657 56 PHE CD2 C 131.60 . . 658 56 PHE CE1 C 130.97 . . 659 56 PHE CE2 C 130.97 . . 660 56 PHE CZ C 129.26 . . 661 56 PHE N N 116.78 . . 662 57 ASN H H 9.35 . . 663 57 ASN HA H 5.07 . . 664 57 ASN HB2 H 3.53 . . 665 57 ASN HB3 H 2.42 . . 666 57 ASN HD21 H 7.78 . . 667 57 ASN HD22 H 7.46 . . 668 57 ASN C C 175.05 . . 669 57 ASN CA C 49.71 . . 670 57 ASN CB C 38.93 . . 671 57 ASN N N 121.53 . . 672 57 ASN ND2 N 113.71 . . 673 58 PRO HA H 4.45 . . 674 58 PRO HB2 H 2.43 . . 675 58 PRO HB3 H 2.10 . . 676 58 PRO HG2 H 2.16 . . 677 58 PRO HG3 H 2.16 . . 678 58 PRO HD2 H 4.21 . . 679 58 PRO HD3 H 4.06 . . 680 58 PRO C C 177.88 . . 681 58 PRO CA C 63.97 . . 682 58 PRO CB C 32.04 . . 683 58 PRO CG C 26.78 . . 684 58 PRO CD C 50.84 . . 685 58 PRO N N 138.47 . . 686 59 GLU H H 8.24 . . 687 59 GLU HA H 4.26 . . 688 59 GLU HB2 H 2.16 . . 689 59 GLU HB3 H 2.16 . . 690 59 GLU HG2 H 2.40 . . 691 59 GLU HG3 H 2.31 . . 692 59 GLU C C 177.88 . . 693 59 GLU CA C 58.17 . . 694 59 GLU CB C 29.98 . . 695 59 GLU CG C 36.62 . . 696 59 GLU N N 115.65 . . 697 60 THR H H 7.23 . . 698 60 THR HA H 4.56 . . 699 60 THR HB H 4.35 . . 700 60 THR HG2 H 1.16 . . 701 60 THR C C 176.63 . . 702 60 THR CA C 61.11 . . 704 60 THR CG2 C 21.46 . . 705 60 THR N N 104.96 . . 706 61 GLY H H 8.57 . . 707 61 GLY HA2 H 4.21 . . 708 61 GLY HA3 H 3.89 . . 709 61 GLY C C 174.36 . . 710 61 GLY CA C 45.68 . . 711 61 GLY N N 110.14 . . 712 62 THR H H 7.87 . . 713 62 THR HA H 4.86 . . 714 62 THR HB H 4.51 . . 715 62 THR HG2 H 1.13 . . 716 62 THR C C 173.90 . . 717 62 THR CA C 59.59 . . 718 62 THR CB C 71.95 . . 719 62 THR CG2 C 20.83 . . 720 62 THR N N 109.61 . . 721 63 LEU H H 9.21 . . 722 63 LEU HA H 4.00 . . 723 63 LEU HB2 H 1.54 . . 724 63 LEU HB3 H 1.41 . . 725 63 LEU HG H 1.66 . . 726 63 LEU HD1 H 0.67 . . 727 63 LEU HD2 H 0.19 . . 728 63 LEU C C 177.59 . . 729 63 LEU CA C 56.21 . . 730 63 LEU CB C 42.67 . . 731 63 LEU CG C 26.88 . . 732 63 LEU CD1 C 26.14 . . 733 63 LEU CD2 C 23.83 . . 734 63 LEU N N 122.81 . . 735 64 ARG H H 8.25 . . 736 64 ARG HA H 4.30 . . 737 64 ARG HB2 H 1.80 . . 738 64 ARG HB3 H 1.49 . . 739 64 ARG HG2 H 1.35 . . 740 64 ARG HG3 H 1.24 . . 741 64 ARG HD2 H 3.21 . . 742 64 ARG HD3 H 3.10 . . 743 64 ARG C C 172.91 . . 744 64 ARG CA C 54.55 . . 745 64 ARG CB C 30.82 . . 746 64 ARG CG C 27.34 . . 747 64 ARG CD C 43.16 . . 748 64 ARG N N 119.33 . . 749 65 ILE H H 7.78 . . 750 65 ILE HA H 3.63 . . 751 65 ILE HB H 1.97 . . 752 65 ILE HG12 H 1.43 . . 753 65 ILE HG13 H 1.43 . . 754 65 ILE HG2 H 0.76 . . 755 65 ILE HD1 H 0.57 . . 756 65 ILE C C 176.71 . . 757 65 ILE CA C 61.12 . . 758 65 ILE CB C 33.93 . . 759 65 ILE CG1 C 26.65 . . 760 65 ILE CG2 C 17.79 . . 761 65 ILE CD1 C 9.77 . . 762 65 ILE N N 114.25 . . 763 66 LEU H H 7.97 . . 764 66 LEU HA H 4.51 . . 765 66 LEU HB2 H 2.13 . . 766 66 LEU HB3 H 1.80 . . 767 66 LEU HG H 0.84 . . 768 66 LEU HD1 H 0.88 . . 769 66 LEU HD2 H 0.52 . . 770 66 LEU C C 177.18 . . 771 66 LEU CA C 53.70 . . 772 66 LEU CB C 42.20 . . 773 66 LEU CG C 25.73 . . 774 66 LEU CD1 C 26.05 . . 775 66 LEU CD2 C 22.01 . . 776 66 LEU N N 132.52 . . 777 67 GLN H H 9.41 . . 778 67 GLN HA H 4.57 . . 779 67 GLN HB2 H 2.50 . . 780 67 GLN HB3 H 1.67 . . 781 67 GLN HG2 H 2.57 . . 782 67 GLN HG3 H 2.50 . . 783 67 GLN HE21 H 7.70 . . 784 67 GLN HE22 H 6.73 . . 785 67 GLN C C 177.46 . . 786 67 GLN CA C 54.93 . . 787 67 GLN CB C 30.13 . . 788 67 GLN CG C 34.18 . . 789 67 GLN N N 120.97 . . 790 67 GLN NE2 N 111.94 . . 791 68 GLU H H 9.40 . . 792 68 GLU HA H 2.69 . . 793 68 GLU HB2 H 2.19 . . 794 68 GLU HB3 H 1.86 . . 795 68 GLU HG2 H 1.78 . . 796 68 GLU HG3 H 1.78 . . 797 68 GLU C C 176.96 . . 798 68 GLU CA C 59.95 . . 799 68 GLU CB C 28.61 . . 800 68 GLU CG C 35.45 . . 801 68 GLU N N 125.26 . . 802 69 GLU H H 9.52 . . 803 69 GLU HA H 3.71 . . 804 69 GLU HB2 H 1.95 . . 805 69 GLU HB3 H 1.69 . . 806 69 GLU HG2 H 2.36 . . 807 69 GLU HG3 H 2.31 . . 808 69 GLU C C 180.07 . . 809 69 GLU CA C 59.68 . . 810 69 GLU CB C 29.58 . . 811 69 GLU CG C 36.82 . . 812 69 GLU N N 114.62 . . 813 70 GLU H H 7.38 . . 814 70 GLU HA H 4.36 . . 815 70 GLU HB2 H 2.82 . . 816 70 GLU HB3 H 1.79 . . 817 70 GLU HG2 H 2.51 . . 818 70 GLU HG3 H 2.04 . . 819 70 GLU C C 178.77 . . 820 70 GLU CA C 57.38 . . 821 70 GLU CB C 30.56 . . 822 70 GLU CG C 36.65 . . 823 70 GLU N N 114.49 . . 824 71 TRP H H 8.38 . . 825 71 TRP HA H 4.61 . . 826 71 TRP HB2 H 3.65 . . 827 71 TRP HB3 H 3.32 . . 828 71 TRP HD1 H 7.18 . . 829 71 TRP HE1 H 10.96 . . 830 71 TRP HE3 H 7.35 . . 831 71 TRP HZ2 H 7.96 . . 832 71 TRP HZ3 H 7.25 . . 833 71 TRP HH2 H 7.21 . . 834 71 TRP C C 180.00 . . 835 71 TRP CA C 60.05 . . 836 71 TRP CB C 27.97 . . 837 71 TRP CZ2 C 115.12 . . 838 71 TRP CH2 C 123.82 . . 839 71 TRP N N 115.86 . . 840 71 TRP NE1 N 130.66 . . 841 72 ARG H H 8.44 . . 842 72 ARG HA H 4.80 . . 843 72 ARG HB2 H 1.63 . . 844 72 ARG HB3 H 1.48 . . 845 72 ARG HG2 H 0.97 . . 846 72 ARG HG3 H 0.87 . . 847 72 ARG HD2 H 3.16 . . 848 72 ARG HD3 H 2.81 . . 849 72 ARG C C 181.61 . . 850 72 ARG CA C 59.95 . . 852 72 ARG CG C 29.40 . . 853 72 ARG CD C 42.73 . . 854 72 ARG N N 122.88 . . 855 73 GLY H H 7.42 . . 856 73 GLY HA2 H 4.01 . . 857 73 GLY HA3 H 4.01 . . 858 73 GLY C C 174.16 . . 859 73 GLY CA C 45.10 . . 860 73 GLY N N 107.90 . . 861 74 LEU H H 7.18 . . 862 74 LEU HA H 4.21 . . 863 74 LEU HB2 H 2.16 . . 864 74 LEU HB3 H 1.66 . . 865 74 LEU HG H 2.16 . . 866 74 LEU HD1 H 0.84 . . 867 74 LEU HD2 H 0.81 . . 868 74 LEU C C 174.38 . . 869 74 LEU CA C 54.84 . . 871 74 LEU CG C 26.92 . . 872 74 LEU CD1 C 25.73 . . 873 74 LEU CD2 C 23.59 . . 874 74 LEU N N 116.54 . . 875 75 GLY H H 7.47 . . 876 75 GLY HA2 H 4.45 . . 877 75 GLY HA3 H 3.62 . . 878 75 GLY C C 174.46 . . 879 75 GLY CA C 43.97 . . 880 75 GLY N N 98.95 . . 881 76 ILE H H 7.19 . . 882 76 ILE HA H 4.16 . . 883 76 ILE HB H 2.31 . . 884 76 ILE HG12 H 1.78 . . 885 76 ILE HG13 H 0.91 . . 886 76 ILE HG2 H 0.69 . . 887 76 ILE HD1 H 1.07 . . 888 76 ILE C C 175.21 . . 889 76 ILE CA C 61.86 . . 890 76 ILE CB C 37.92 . . 891 76 ILE CG1 C 28.36 . . 892 76 ILE CG2 C 18.36 . . 893 76 ILE CD1 C 14.37 . . 894 76 ILE N N 120.76 . . 895 77 THR H H 8.78 . . 896 77 THR HA H 4.68 . . 897 77 THR HB H 4.01 . . 898 77 THR HG2 H 1.16 . . 899 77 THR C C 172.72 . . 900 77 THR CA C 60.81 . . 901 77 THR CB C 69.65 . . 902 77 THR CG2 C 20.41 . . 903 77 THR N N 123.82 . . 904 78 GLN H H 7.32 . . 905 78 GLN HA H 4.57 . . 906 78 GLN HB2 H 1.96 . . 907 78 GLN HB3 H 1.84 . . 908 78 GLN HG2 H 1.69 . . 909 78 GLN HG3 H 1.69 . . 910 78 GLN HE21 H 7.55 . . 911 78 GLN HE22 H 6.89 . . 912 78 GLN C C 175.03 . . 913 78 GLN CA C 53.65 . . 914 78 GLN CB C 31.28 . . 915 78 GLN CG C 31.96 . . 916 78 GLN N N 119.02 . . 917 78 GLN NE2 N 112.90 . . 918 79 SER H H 9.18 . . 919 79 SER HA H 4.52 . . 920 79 SER HB2 H 4.21 . . 921 79 SER HB3 H 4.21 . . 922 79 SER C C 173.35 . . 923 79 SER CA C 59.13 . . 924 79 SER CB C 63.71 . . 925 79 SER N N 117.17 . . 926 80 LEU H H 8.12 . . 927 80 LEU HA H 4.31 . . 928 80 LEU HB2 H 1.78 . . 929 80 LEU HB3 H 1.65 . . 930 80 LEU HG H 1.80 . . 931 80 LEU HD1 H 1.01 . . 932 80 LEU HD2 H 0.98 . . 933 80 LEU C C 177.55 . . 934 80 LEU CA C 56.23 . . 936 80 LEU CG C 27.08 . . 937 80 LEU CD1 C 24.81 . . 938 80 LEU CD2 C 23.34 . . 939 80 LEU N N 119.06 . . 940 81 GLY H H 8.80 . . 941 81 GLY HA2 H 3.36 . . 942 81 GLY HA3 H 3.32 . . 943 81 GLY C C 174.57 . . 944 81 GLY CA C 44.51 . . 945 81 GLY N N 110.09 . . 946 82 TRP H H 7.07 . . 947 82 TRP HA H 4.44 . . 948 82 TRP HB2 H 2.90 . . 949 82 TRP HB3 H 2.90 . . 950 82 TRP HD1 H 7.54 . . 951 82 TRP HE1 H 10.16 . . 952 82 TRP HZ2 H 7.10 . . 953 82 TRP HZ3 H 6.74 . . 954 82 TRP HH2 H 6.63 . . 955 82 TRP C C 176.36 . . 956 82 TRP CA C 57.91 . . 957 82 TRP CB C 30.78 . . 958 82 TRP CZ2 C 113.56 . . 959 82 TRP CZ3 C 121.65 . . 960 82 TRP CH2 C 122.58 . . 961 82 TRP N N 119.40 . . 962 82 TRP NE1 N 130.16 . . 963 83 GLU H H 9.54 . . 964 83 GLU HA H 5.18 . . 965 83 GLU HB2 H 2.22 . . 966 83 GLU HB3 H 2.13 . . 967 83 GLU HG2 H 2.45 . . 968 83 GLU HG3 H 2.38 . . 969 83 GLU C C 175.73 . . 970 83 GLU CA C 54.27 . . 971 83 GLU CB C 32.64 . . 972 83 GLU CG C 35.49 . . 973 83 GLU N N 120.70 . . 974 84 MET H H 9.20 . . 975 84 MET HA H 3.45 . . 976 84 MET HB2 H 2.07 . . 977 84 MET HB3 H 1.18 . . 978 84 MET HG2 H 1.93 . . 979 84 MET HG3 H 1.75 . . 980 84 MET HE H 1.88 . . 981 84 MET C C 175.05 . . 982 84 MET CA C 56.53 . . 983 84 MET CB C 31.38 . . 984 84 MET CG C 33.36 . . 985 84 MET CE C 20.07 . . 986 84 MET N N 126.86 . . 987 85 TYR H H 8.75 . . 988 85 TYR HA H 5.07 . . 989 85 TYR HB2 H 3.19 . . 990 85 TYR HB3 H 2.63 . . 991 85 TYR HD1 H 7.02 . . 992 85 TYR HD2 H 7.02 . . 993 85 TYR HE1 H 6.78 . . 994 85 TYR HE2 H 6.78 . . 995 85 TYR C C 173.35 . . 996 85 TYR CA C 56.55 . . 997 85 TYR CB C 41.14 . . 998 85 TYR CD1 C 133.15 . . 999 85 TYR CD2 C 133.15 . . 1000 85 TYR CE1 C 117.92 . . 1001 85 TYR CE2 C 117.92 . . 1002 85 TYR N N 122.95 . . 1003 86 GLU H H 7.12 . . 1004 86 GLU HA H 4.38 . . 1005 86 GLU HB2 H 1.60 . . 1006 86 GLU HB3 H 1.36 . . 1007 86 GLU HG2 H 1.98 . . 1008 86 GLU HG3 H 1.98 . . 1009 86 GLU C C 173.10 . . 1010 86 GLU CA C 55.97 . . 1011 86 GLU CB C 34.32 . . 1012 86 GLU CG C 36.60 . . 1013 86 GLU N N 120.22 . . 1014 87 VAL H H 8.11 . . 1015 87 VAL HA H 4.11 . . 1016 87 VAL HB H 1.89 . . 1017 87 VAL HG1 H 0.91 . . 1018 87 VAL HG2 H 0.81 . . 1019 87 VAL C C 174.66 . . 1020 87 VAL CA C 61.70 . . 1021 87 VAL CB C 34.17 . . 1022 87 VAL CG1 C 20.79 . . 1023 87 VAL CG2 C 21.47 . . 1024 87 VAL N N 120.02 . . 1025 88 HIS H H 9.29 . . 1026 88 HIS HA H 4.69 . . 1027 88 HIS HB2 H 3.33 . . 1028 88 HIS HB3 H 2.89 . . 1029 88 HIS HD2 H 6.96 . . 1030 88 HIS HE1 H 7.98 . . 1031 88 HIS C C 176.39 . . 1032 88 HIS CA C 55.42 . . 1033 88 HIS CB C 30.68 . . 1034 88 HIS CD2 C 118.23 . . 1035 88 HIS N N 126.89 . . 1036 89 VAL H H 8.39 . . 1037 89 VAL HA H 3.66 . . 1038 89 VAL HB H 2.09 . . 1039 89 VAL HG1 H 1.07 . . 1040 89 VAL HG2 H 0.99 . . 1041 89 VAL C C 176.35 . . 1042 89 VAL CA C 64.90 . . 1043 89 VAL CB C 31.68 . . 1044 89 VAL CG1 C 21.20 . . 1045 89 VAL CG2 C 20.32 . . 1046 89 VAL N N 123.59 . . 1047 90 ALA H H 8.81 . . 1048 90 ALA HA H 4.37 . . 1049 90 ALA HB H 1.51 . . 1050 90 ALA C C 178.27 . . 1051 90 ALA CA C 53.03 . . 1052 90 ALA CB C 19.42 . . 1053 90 ALA N N 120.71 . . 1054 91 GLU H H 7.50 . . 1055 91 GLU HA H 5.01 . . 1056 91 GLU HB2 H 1.80 . . 1057 91 GLU HB3 H 1.73 . . 1058 91 GLU HG2 H 2.15 . . 1059 91 GLU HG3 H 2.15 . . 1060 91 GLU C C 173.82 . . 1061 91 GLU CA C 52.86 . . 1062 91 GLU CB C 30.88 . . 1063 91 GLU CG C 34.91 . . 1064 91 GLU N N 114.98 . . 1065 92 PRO HA H 4.46 . . 1066 92 PRO HB2 H 2.35 . . 1067 92 PRO HB3 H 2.22 . . 1068 92 PRO HG2 H 2.13 . . 1069 92 PRO HG3 H 1.98 . . 1070 92 PRO HD2 H 3.94 . . 1071 92 PRO HD3 H 3.68 . . 1072 92 PRO C C 173.96 . . 1073 92 PRO CA C 64.51 . . 1074 92 PRO CB C 31.88 . . 1075 92 PRO CG C 26.93 . . 1076 92 PRO CD C 49.68 . . 1077 92 PRO N N 135.72 . . 1078 93 HIS H H 9.02 . . 1079 93 HIS HA H 4.57 . . 1080 93 HIS HB2 H 3.91 . . 1081 93 HIS HB3 H 2.53 . . 1082 93 HIS HD2 H 7.15 . . 1083 93 HIS HE1 H 8.00 . . 1084 93 HIS C C 172.85 . . 1085 93 HIS CA C 55.37 . . 1086 93 HIS CB C 29.52 . . 1087 93 HIS N N 114.10 . . 1088 94 ILE H H 7.52 . . 1089 94 ILE HA H 4.60 . . 1090 94 ILE HB H 1.68 . . 1091 94 ILE HG12 H 0.44 . . 1092 94 ILE HG13 H 0.20 . . 1093 94 ILE HG2 H 0.57 . . 1094 94 ILE HD1 H 0.54 . . 1095 94 ILE C C 173.86 . . 1096 94 ILE CA C 61.06 . . 1097 94 ILE CB C 37.07 . . 1098 94 ILE CG1 C 26.66 . . 1099 94 ILE CG2 C 16.94 . . 1100 94 ILE CD1 C 12.61 . . 1101 94 ILE N N 120.42 . . 1102 95 LEU H H 9.34 . . 1103 95 LEU HA H 4.58 . . 1104 95 LEU HB2 H 1.84 . . 1105 95 LEU HB3 H 1.29 . . 1106 95 LEU HG H 1.70 . . 1107 95 LEU HD1 H 0.84 . . 1108 95 LEU HD2 H 0.78 . . 1109 95 LEU C C 175.26 . . 1110 95 LEU CA C 54.08 . . 1111 95 LEU CB C 44.22 . . 1112 95 LEU CG C 29.14 . . 1113 95 LEU CD1 C 24.33 . . 1114 95 LEU CD2 C 24.63 . . 1115 95 LEU N N 128.44 . . 1116 96 LEU H H 8.33 . . 1117 96 LEU HA H 4.89 . . 1118 96 LEU HB2 H 1.46 . . 1119 96 LEU HB3 H 1.07 . . 1120 96 LEU HG H 1.29 . . 1121 96 LEU HD1 H 0.63 . . 1122 96 LEU HD2 H 0.52 . . 1123 96 LEU C C 175.29 . . 1124 96 LEU CA C 55.43 . . 1125 96 LEU CB C 41.11 . . 1126 96 LEU CG C 28.58 . . 1127 96 LEU CD1 C 24.88 . . 1128 96 LEU CD2 C 23.89 . . 1129 96 LEU N N 123.14 . . 1130 97 PHE H H 9.09 . . 1131 97 PHE HA H 5.66 . . 1132 97 PHE HB2 H 3.00 . . 1133 97 PHE HB3 H 2.78 . . 1134 97 PHE HD1 H 6.75 . . 1135 97 PHE HD2 H 6.75 . . 1136 97 PHE HE1 H 5.88 . . 1137 97 PHE HE2 H 5.88 . . 1138 97 PHE HZ H 6.12 . . 1139 97 PHE C C 174.90 . . 1140 97 PHE CA C 56.32 . . 1141 97 PHE CB C 43.64 . . 1142 97 PHE CD1 C 131.13 . . 1143 97 PHE CD2 C 131.13 . . 1144 97 PHE CE1 C 130.35 . . 1145 97 PHE CE2 C 130.35 . . 1146 97 PHE CZ C 127.55 . . 1147 97 PHE N N 122.33 . . 1148 98 LYS H H 9.58 . . 1149 98 LYS HA H 6.01 . . 1150 98 LYS HB2 H 1.47 . . 1151 98 LYS HB3 H 1.20 . . 1152 98 LYS HG2 H 0.99 . . 1153 98 LYS HG3 H 0.80 . . 1154 98 LYS HD2 H 0.16 . . 1155 98 LYS HD3 H -0.01 . . 1156 98 LYS HE2 H 2.04 . . 1157 98 LYS HE3 H 2.04 . . 1158 98 LYS C C 174.42 . . 1159 98 LYS CA C 54.28 . . 1160 98 LYS CB C 37.44 . . 1161 98 LYS CG C 22.89 . . 1162 98 LYS CD C 28.64 . . 1163 98 LYS CE C 41.22 . . 1164 98 LYS N N 117.97 . . 1165 99 ARG H H 8.80 . . 1166 99 ARG HA H 4.54 . . 1167 99 ARG HB2 H 0.68 . . 1168 99 ARG HB3 H 0.36 . . 1169 99 ARG HG2 H 0.74 . . 1170 99 ARG HG3 H 0.58 . . 1171 99 ARG HD2 H 2.67 . . 1172 99 ARG HD3 H 2.51 . . 1173 99 ARG C C 174.52 . . 1174 99 ARG CA C 54.83 . . 1175 99 ARG CB C 33.16 . . 1176 99 ARG CG C 24.22 . . 1177 99 ARG CD C 42.88 . . 1178 99 ARG N N 120.14 . . 1179 100 GLU H H 9.12 . . 1180 100 GLU HA H 3.89 . . 1181 100 GLU HB2 H 2.04 . . 1182 100 GLU HB3 H 1.95 . . 1183 100 GLU HG2 H 2.31 . . 1184 100 GLU HG3 H 2.31 . . 1185 100 GLU C C 176.85 . . 1186 100 GLU CA C 57.68 . . 1187 100 GLU CB C 29.71 . . 1188 100 GLU CG C 36.60 . . 1189 100 GLU N N 125.96 . . 1190 101 LYS H H 8.00 . . 1191 101 LYS HA H 3.85 . . 1192 101 LYS HB2 H 1.57 . . 1193 101 LYS HB3 H 1.39 . . 1194 101 LYS HG2 H 1.21 . . 1195 101 LYS HG3 H 1.21 . . 1196 101 LYS HD2 H 1.64 . . 1197 101 LYS HD3 H 1.46 . . 1198 101 LYS HE2 H 2.88 . . 1199 101 LYS HE3 H 2.88 . . 1200 101 LYS C C 176.58 . . 1201 101 LYS CA C 58.13 . . 1202 101 LYS CB C 32.06 . . 1203 101 LYS CG C 25.15 . . 1204 101 LYS CD C 29.14 . . 1205 101 LYS CE C 41.74 . . 1206 101 LYS N N 123.21 . . 1207 102 ASP H H 8.52 . . 1208 102 ASP HA H 4.60 . . 1209 102 ASP HB2 H 2.75 . . 1210 102 ASP HB3 H 2.66 . . 1211 102 ASP C C 176.11 . . 1212 102 ASP CA C 53.88 . . 1213 102 ASP CB C 39.43 . . 1214 102 ASP N N 118.59 . . 1215 103 TYR H H 7.58 . . 1216 103 TYR HA H 3.95 . . 1217 103 TYR HB2 H 3.22 . . 1218 103 TYR HB3 H 2.84 . . 1219 103 TYR HD1 H 6.97 . . 1220 103 TYR HD2 H 6.97 . . 1221 103 TYR HE1 H 6.67 . . 1222 103 TYR HE2 H 6.67 . . 1223 103 TYR C C 176.46 . . 1224 103 TYR CA C 61.10 . . 1225 103 TYR CB C 38.34 . . 1226 103 TYR CD1 C 132.84 . . 1227 103 TYR CD2 C 132.84 . . 1228 103 TYR CE1 C 118.23 . . 1229 103 TYR CE2 C 118.23 . . 1230 103 TYR N N 119.63 . . 1231 104 GLN H H 8.46 . . 1232 104 GLN HA H 4.01 . . 1233 104 GLN HB2 H 2.01 . . 1234 104 GLN HB3 H 1.94 . . 1235 104 GLN HG2 H 2.29 . . 1236 104 GLN HG3 H 2.29 . . 1237 104 GLN HE21 H 7.56 . . 1238 104 GLN HE22 H 6.91 . . 1239 104 GLN C C 177.00 . . 1240 104 GLN CA C 57.13 . . 1241 104 GLN CB C 28.60 . . 1242 104 GLN CG C 33.70 . . 1243 104 GLN N N 118.40 . . 1244 104 GLN NE2 N 111.84 . . 1245 105 MET H H 7.91 . . 1246 105 MET HA H 4.30 . . 1247 105 MET HB2 H 2.06 . . 1248 105 MET HB3 H 2.06 . . 1249 105 MET HG2 H 2.60 . . 1250 105 MET HG3 H 2.51 . . 1251 105 MET HE H 2.07 . . 1252 105 MET C C 177.21 . . 1253 105 MET CA C 56.54 . . 1254 105 MET CB C 32.03 . . 1255 105 MET CG C 31.78 . . 1256 105 MET CE C 16.97 . . 1257 105 MET N N 118.81 . . 1258 106 LYS H H 7.85 . . 1259 106 LYS HA H 4.07 . . 1260 106 LYS HB2 H 1.49 . . 1261 106 LYS HB3 H 1.49 . . 1262 106 LYS HG2 H 1.25 . . 1263 106 LYS HG3 H 1.14 . . 1264 106 LYS HD2 H 1.51 . . 1265 106 LYS HD3 H 1.51 . . 1266 106 LYS HE2 H 2.85 . . 1267 106 LYS HE3 H 2.85 . . 1268 106 LYS C C 177.18 . . 1269 106 LYS CA C 57.36 . . 1270 106 LYS CB C 32.45 . . 1271 106 LYS CG C 24.57 . . 1272 106 LYS CD C 28.92 . . 1273 106 LYS CE C 41.76 . . 1274 106 LYS N N 119.94 . . 1275 107 PHE H H 8.02 . . 1276 107 PHE HA H 4.59 . . 1277 107 PHE HB2 H 3.16 . . 1278 107 PHE HB3 H 2.77 . . 1279 107 PHE HD1 H 7.10 . . 1280 107 PHE HD2 H 7.10 . . 1281 107 PHE HE1 H 7.27 . . 1282 107 PHE HE2 H 7.27 . . 1283 107 PHE HZ H 7.27 . . 1284 107 PHE C C 176.27 . . 1285 107 PHE CA C 57.97 . . 1286 107 PHE CB C 38.88 . . 1287 107 PHE CD1 C 131.60 . . 1288 107 PHE CD2 C 131.60 . . 1289 107 PHE CE1 C 130.97 . . 1290 107 PHE CE2 C 130.97 . . 1291 107 PHE CZ C 129.42 . . 1292 107 PHE N N 118.71 . . 1293 108 SER H H 8.01 . . 1294 108 SER HA H 4.40 . . 1295 108 SER HB2 H 3.92 . . 1296 108 SER HB3 H 3.92 . . 1297 108 SER C C 174.82 . . 1298 108 SER CA C 58.83 . . 1299 108 SER CB C 63.38 . . 1300 108 SER N N 115.68 . . 1301 109 GLN H H 8.30 . . 1302 109 GLN HA H 4.33 . . 1303 109 GLN HB2 H 2.16 . . 1304 109 GLN HB3 H 2.03 . . 1305 109 GLN HG2 H 2.41 . . 1306 109 GLN HG3 H 2.41 . . 1307 109 GLN HE21 H 6.88 . . 1308 109 GLN HE22 H 7.54 . . 1309 109 GLN C C 176.09 . . 1310 109 GLN CA C 55.96 . . 1311 109 GLN CB C 29.02 . . 1312 109 GLN CG C 33.72 . . 1313 109 GLN N N 121.33 . . 1314 109 GLN NE2 N 112.02 . . 1315 110 GLN H H 8.30 . . 1316 110 GLN HA H 4.33 . . 1317 110 GLN HB2 H 2.16 . . 1318 110 GLN HB3 H 2.04 . . 1319 110 GLN HG2 H 2.41 . . 1320 110 GLN HG3 H 2.41 . . 1321 110 GLN HE21 H 6.89 . . 1322 110 GLN HE22 H 7.54 . . 1323 110 GLN C C 176.06 . . 1324 110 GLN CA C 55.88 . . 1325 110 GLN CB C 29.18 . . 1326 110 GLN CG C 33.56 . . 1327 110 GLN N N 120.54 . . 1328 110 GLN NE2 N 112.26 . . 1329 111 ARG H H 8.38 . . 1330 111 ARG HA H 4.39 . . 1331 111 ARG HB2 H 1.92 . . 1332 111 ARG HB3 H 1.81 . . 1333 111 ARG HG2 H 1.66 . . 1334 111 ARG HG3 H 1.66 . . 1335 111 ARG HD2 H 3.22 . . 1336 111 ARG HD3 H 3.22 . . 1337 111 ARG C C 176.71 . . 1338 111 ARG CA C 55.96 . . 1340 111 ARG CG C 26.89 . . 1341 111 ARG CD C 43.03 . . 1342 111 ARG N N 122.04 . . 1343 112 GLY H H 8.45 . . 1344 112 GLY HA2 H 4.01 . . 1345 112 GLY HA3 H 4.01 . . 1346 112 GLY C C 173.61 . . 1347 112 GLY CA C 45.11 . . 1348 112 GLY N N 110.35 . . 1349 113 GLY H H 8.01 . . 1350 113 GLY HA2 H 3.80 . . 1351 113 GLY HA3 H 3.80 . . stop_ save_