data_5474 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of the 298 amino acid catalytic domain of protein tyrosine phosphatase 1B (PTP1B) ; _BMRB_accession_number 5474 _BMRB_flat_file_name bmr5474.str _Entry_type original _Submission_date 2002-07-24 _Accession_date 2002-07-24 _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 Meier Sebastian . . 2 Li Yu-Chin . . 3 Koehn James . . 4 Vlattas Isidoros . . 5 Wareing James . . 6 Jahnke Wolfgang . . 7 Wennogle Lawrence P. . 8 Grzesiek Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 218 "13C chemical shifts" 697 "15N chemical shifts" 218 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-03 update author 'update 11 nitrogen chemical shifts' 2003-01-06 update author 'update the experimental source' 2002-11-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignment of the 298 amino acid catalytic domain of protein tyrosine phosphatase 1B (PTP1B) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Meier Sebastian . . 2 Li Yu-Chin . . 3 Koehn James . . 4 Vlattas Isidoros . . 5 Wareing James . . 6 Jahnke Wolfgang . . 7 Wennogle Lawrence P. . 8 Grzesiek Stephan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 165 _Page_last 166 _Year 2002 _Details . loop_ _Keyword obesity diabetes 'heteronuclear NMR' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_1 _Saveframe_category citation _Citation_full ; Barford, D., Flint, A.J., Tonks,N.K. (1994) Science, 263, 1397-1404. ; _Citation_title 'Crystal structure of human protein tyrosine phosphatase 1B.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8128219 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Barford D. . . 2 Flint A.J. J. . 3 Tonks N.K. K. . stop_ _Journal_abbreviation Science _Journal_name_full 'Science (New York, N.Y.)' _Journal_volume 263 _Journal_issue 5152 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1397 _Page_last 1404 _Year 1994 _Details ; Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation. ; save_ ################################## # Molecular system description # ################################## save_system_ptp1b _Saveframe_category molecular_system _Mol_system_name 'protein tyrosine phosphatase 1B' _Abbreviation_common ptp1b _Enzyme_commission_number 3.1.3.48 loop_ _Mol_system_component_name _Mol_label 'protein tyrosine phosphatase 1B' $ptp1b 'DADEXLIP-amide,(X=phenylalanine-p-difluoromethyl phosphonate)' $DADEXLIP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'protein tyrosine phosphatase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ptp1b _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'protein tyrosine phosphatase 1B' _Abbreviation_common PTP1B _Molecular_mass 34672 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 298 _Mol_residue_sequence ; MEMEKEFEQIDKSGSWAAIY QDIRHEASDFPCRVAKLPKN KNRNRYRDVSPFDHSRIKLH QEDNDYINASLIKMEEAQRS YILTQGPLPNTCGHFWEMVW EQKSRGVVMLNRVMEKGSLK CAQYWPQKEEKEMIFEDTNL KLTLISEDIKSYYTVRQLEL ENLTTQETREILHFHYTTWP DFGVPESPASFLNFLFKVRE SGSLSPEHGPVVVHCSAGIG RSGTFCLADTCLLLMDKRKD PSSVDIKKVLLEMRKFRMGL IQTADQLRFSYLAVIEGAKF IMGDSSVQDQWKELSHED ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 MET 4 GLU 5 LYS 6 GLU 7 PHE 8 GLU 9 GLN 10 ILE 11 ASP 12 LYS 13 SER 14 GLY 15 SER 16 TRP 17 ALA 18 ALA 19 ILE 20 TYR 21 GLN 22 ASP 23 ILE 24 ARG 25 HIS 26 GLU 27 ALA 28 SER 29 ASP 30 PHE 31 PRO 32 CYS 33 ARG 34 VAL 35 ALA 36 LYS 37 LEU 38 PRO 39 LYS 40 ASN 41 LYS 42 ASN 43 ARG 44 ASN 45 ARG 46 TYR 47 ARG 48 ASP 49 VAL 50 SER 51 PRO 52 PHE 53 ASP 54 HIS 55 SER 56 ARG 57 ILE 58 LYS 59 LEU 60 HIS 61 GLN 62 GLU 63 ASP 64 ASN 65 ASP 66 TYR 67 ILE 68 ASN 69 ALA 70 SER 71 LEU 72 ILE 73 LYS 74 MET 75 GLU 76 GLU 77 ALA 78 GLN 79 ARG 80 SER 81 TYR 82 ILE 83 LEU 84 THR 85 GLN 86 GLY 87 PRO 88 LEU 89 PRO 90 ASN 91 THR 92 CYS 93 GLY 94 HIS 95 PHE 96 TRP 97 GLU 98 MET 99 VAL 100 TRP 101 GLU 102 GLN 103 LYS 104 SER 105 ARG 106 GLY 107 VAL 108 VAL 109 MET 110 LEU 111 ASN 112 ARG 113 VAL 114 MET 115 GLU 116 LYS 117 GLY 118 SER 119 LEU 120 LYS 121 CYS 122 ALA 123 GLN 124 TYR 125 TRP 126 PRO 127 GLN 128 LYS 129 GLU 130 GLU 131 LYS 132 GLU 133 MET 134 ILE 135 PHE 136 GLU 137 ASP 138 THR 139 ASN 140 LEU 141 LYS 142 LEU 143 THR 144 LEU 145 ILE 146 SER 147 GLU 148 ASP 149 ILE 150 LYS 151 SER 152 TYR 153 TYR 154 THR 155 VAL 156 ARG 157 GLN 158 LEU 159 GLU 160 LEU 161 GLU 162 ASN 163 LEU 164 THR 165 THR 166 GLN 167 GLU 168 THR 169 ARG 170 GLU 171 ILE 172 LEU 173 HIS 174 PHE 175 HIS 176 TYR 177 THR 178 THR 179 TRP 180 PRO 181 ASP 182 PHE 183 GLY 184 VAL 185 PRO 186 GLU 187 SER 188 PRO 189 ALA 190 SER 191 PHE 192 LEU 193 ASN 194 PHE 195 LEU 196 PHE 197 LYS 198 VAL 199 ARG 200 GLU 201 SER 202 GLY 203 SER 204 LEU 205 SER 206 PRO 207 GLU 208 HIS 209 GLY 210 PRO 211 VAL 212 VAL 213 VAL 214 HIS 215 CYS 216 SER 217 ALA 218 GLY 219 ILE 220 GLY 221 ARG 222 SER 223 GLY 224 THR 225 PHE 226 CYS 227 LEU 228 ALA 229 ASP 230 THR 231 CYS 232 LEU 233 LEU 234 LEU 235 MET 236 ASP 237 LYS 238 ARG 239 LYS 240 ASP 241 PRO 242 SER 243 SER 244 VAL 245 ASP 246 ILE 247 LYS 248 LYS 249 VAL 250 LEU 251 LEU 252 GLU 253 MET 254 ARG 255 LYS 256 PHE 257 ARG 258 MET 259 GLY 260 LEU 261 ILE 262 GLN 263 THR 264 ALA 265 ASP 266 GLN 267 LEU 268 ARG 269 PHE 270 SER 271 TYR 272 LEU 273 ALA 274 VAL 275 ILE 276 GLU 277 GLY 278 ALA 279 LYS 280 PHE 281 ILE 282 MET 283 GLY 284 ASP 285 SER 286 SER 287 VAL 288 GLN 289 ASP 290 GLN 291 TRP 292 LYS 293 GLU 294 LEU 295 SER 296 HIS 297 GLU 298 ASP 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 SWISS-PROT P18031 'Tyrosine-protein phosphatase non-receptor type 1 (Protein-tyrosine phosphatase 1B) (PTP-1B)' 100.00 435 100.00 100.00 2.52e-177 REF XP_001096412 'PREDICTED: protein tyrosine phosphatase, non-receptor type 1 isoform 4 [Macaca mulatta]' 100.00 432 100.00 100.00 2.30e-177 REF XP_001096290 'PREDICTED: protein tyrosine phosphatase, non-receptor type 1 isoform 3 [Macaca mulatta]' 100.00 435 100.00 100.00 1.52e-177 REF XP_001096168 'PREDICTED: protein tyrosine phosphatase, non-receptor type 1 isoform 2 [Macaca mulatta]' 100.00 432 100.00 100.00 2.30e-177 REF XP_001096053 'PREDICTED: protein tyrosine phosphatase, non-receptor type 1 isoform 1 [Macaca mulatta]' 100.00 432 100.00 100.00 2.30e-177 REF NP_002818 'protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 GenBank AAP35398 'protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 GenBank AAH18164 'Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 GenBank AAH15660 'Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 GenBank AAA60223 'phosphotyrosyl-protein phosphatase (EC 3.1.3.48)' 100.00 435 100.00 100.00 2.52e-177 GenBank AAA60157 'non-receptor tyrosine phosphatase 1' 100.00 435 100.00 100.00 2.52e-177 EMBL CAI23215 'protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 EMBL CAH90487 'hypothetical protein [Pongo abelii]' 100.00 435 99.33 99.66 1.81e-176 EMBL CAC00618 'protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 DBJ BAG61697 'unnamed protein product [Homo sapiens]' 75.50 362 100.00 100.00 2.67e-131 DBJ BAG38152 'unnamed protein product [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 DBJ BAG11007 'protein tyrosine phosphatase, non-receptor type 1 [synthetic construct]' 100.00 435 100.00 100.00 2.52e-177 DBJ BAF83327 'unnamed protein product [Homo sapiens]' 100.00 435 100.00 100.00 2.52e-177 PDB 3CWE 'Ptp1b In Complex With A Phosphonic Acid Inhibitor' 94.97 290 100.00 100.00 9.54e-169 PDB 2VEY 'Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 2VEX 'Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 2VEW 'Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 2VEV 'Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 2VEU 'Crystal Structure Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 2QBS 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 100.00 100.00 9.35e-178 PDB 2QBR 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 100.00 100.00 9.35e-178 PDB 2QBQ 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 100.00 100.00 9.35e-178 PDB 2QBP 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 100.00 100.00 9.35e-178 PDB 2NTA 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 99.66 100.00 2.08e-177 PDB 2NT7 'Crystal Structure Of Ptp1b-Inhibitor Complex' 100.00 299 99.66 100.00 2.08e-177 PDB 2HNQ 'Crystal Structure Of Human Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2HNP 'Crystal Structure Of Human Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2HB1 'Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor' 100.00 299 100.00 100.00 9.35e-178 PDB 2H4K 'Crystal Structure Of Ptp1b With A Monocyclic Thiophene Inhibitor' 100.00 299 100.00 100.00 9.35e-178 PDB 2H4G 'Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor' 100.00 299 100.00 100.00 9.35e-178 PDB 2FJN 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2' 100.00 310 100.00 100.00 7.34e-178 PDB 2FJM 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2' 100.00 310 99.66 100.00 1.53e-177 PDB 2F71 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F70 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6Z 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6Y 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6W 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6V 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6T 'Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors' 100.00 298 100.00 100.00 8.25e-178 PDB 2F6F 'The Structure Of The S295f Mutant Of Human Ptp1b' 100.00 302 99.66 99.66 4.42e-177 PDB 2CNI 'Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2CNH 'Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2CNG 'Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2CNF 'Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 2CNE 'Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b' 99.66 304 100.00 100.00 5.22e-177 PDB 2CMC 'Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics' 99.66 304 100.00 100.00 5.22e-177 PDB 2CMB 'Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics' 99.66 304 100.00 100.00 5.22e-177 PDB 2CMA 'Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics' 99.66 327 100.00 100.00 1.98e-176 PDB 2CM8 'Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics' 100.00 321 100.00 100.00 2.25e-177 PDB 2CM7 'Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics' 100.00 321 100.00 100.00 2.25e-177 PDB 2CM3 'Structure Of Protein Tyrosine Phosphatase 1b (C2)' 99.66 304 100.00 100.00 5.22e-177 PDB 2CM2 'Structure Of Protein Tyrosine Phosphatase 1b (P212121)' 99.66 304 100.00 100.00 5.22e-177 PDB 2BGE 'Structure-Based Design Of Protein Tyrosine Phosphatase-1b Inhibitors' 100.00 321 100.00 100.00 2.25e-177 PDB 2BGD 'Structure-Based Design Of Protein Tyrosine Phosphatase-1b Inhibitors' 100.00 321 100.00 100.00 2.25e-177 PDB 2B4S 'Crystal Structure Of A Complex Between Ptp1b And The Insulin Receptor Tyrosine Kinase' 100.00 298 99.66 99.66 4.76e-177 PDB 2B07 'Crystal Structure Of Ptp1b With Tricyclic Thiophene Inhibitor.' 100.00 299 100.00 100.00 9.35e-178 PDB 2AZR 'Crystal Structure Of Ptp1b With Bicyclic Thiophene Inhibitor' 100.00 299 100.00 100.00 9.35e-178 PDB 1XBO 'Ptp1b Complexed With Isoxazole Carboxylic Acid' 100.00 321 100.00 100.00 2.25e-177 PDB 1WAX 'Protein Tyrosine Phosphatase 1b With Active Site Inhibitor' 100.00 321 100.00 100.00 2.25e-177 PDB 1T4J 'Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b' 100.00 298 100.00 100.00 8.25e-178 PDB 1T49 'Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b' 100.00 298 100.00 100.00 8.25e-178 PDB 1T48 'Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b' 100.00 298 100.00 100.00 8.25e-178 PDB 1SUG '1.95 A Structure Of Apo Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 1QXK 'Monoacid-Based, Cell Permeable, Selective Inhibitors Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 1Q6T 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 11' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q6S 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 9' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q6P 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 6' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q6N 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 4' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q6M 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 3' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q6J 'The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2' 100.00 310 100.00 100.00 7.34e-178 PDB 1Q1M 'A Highly Efficient Approach To A Selective And Cell Active Ptp1b Inhibitors' 100.00 321 100.00 100.00 2.25e-177 PDB 1PYN 'Dual-Site Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Using A Linked Fragment Strategy And A Malonate Head On The First Site' 100.00 321 100.00 100.00 2.25e-177 PDB 1PXH 'Crystal Structure Of Protein Tyrosine Phosphatase 1b With Potent And Selective Bidentate Inhibitor Compound 2' 100.00 321 100.00 100.00 2.25e-177 PDB 1PTY 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Phosphotyrosine Molecules' 100.00 321 99.66 99.66 2.23e-176 PDB 1PTV 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine' 100.00 321 98.99 99.66 1.11e-175 PDB 1PTU 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Hexa-Peptide (Dadepyl-Nh2)' 100.00 321 99.33 99.66 3.93e-176 PDB 1PTT 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Tetra-Peptide (Ac-Depyl-Nh2)' 100.00 321 99.33 99.66 3.93e-176 PDB 1PH0 'Non-Carboxylic Acid-Containing Inhibitor Of Ptp1b Targeting The Second Phosphotyrosine Site' 100.00 321 100.00 100.00 2.25e-177 PDB 1PA1 'Crystal Structure Of The C215d Mutant Of Protein Tyrosine Phosphatase 1b' 100.00 310 99.66 99.66 1.79e-176 PDB 1ONZ 'Oxalyl-Aryl-Amino Benzoic Acid Inhibitors Of Ptp1b, Compound 8b' 100.00 321 100.00 100.00 2.25e-177 PDB 1ONY 'Oxalyl-Aryl-Amino Benzoic Acid Inhibitors Of Ptp1b, Compound 17' 100.00 321 100.00 100.00 2.25e-177 PDB 1OEV 'Oxidation State Of Protein Tyrosine Phosphatase 1b' 100.00 321 99.66 99.66 3.71e-176 PDB 1OEU 'Oxidation State Of Protein Tyrosine Phosphatase 1b' 100.00 321 99.66 99.66 3.71e-176 PDB 1OET 'Oxidation State Of Protein Tyrosine Phosphatase 1b' 100.00 321 99.66 99.66 3.71e-176 PDB 1OES 'Oxidation State Of Protein Tyrosine Phosphatase 1b' 100.00 321 100.00 100.00 2.25e-177 PDB 1OEO 'Ptp1b With The Catalytic Cysteine Oxidized To Sulfonic Acid' 100.00 321 99.66 99.66 3.71e-176 PDB 1OEM 'Ptp1b With The Catalytic Cysteine Oxidized To A Sulfenyl- Amide Bond' 100.00 321 100.00 100.00 2.25e-177 PDB 1NZ7 'Potent, Selective Inhibitors Of Protein Tyrosine Phosphatase 1b Using A Second Phosphotyrosine Binding Site, Complexed With Compound 19.' 100.00 321 100.00 100.00 2.25e-177 PDB 1NWL 'Crystal Structure Of The Ptp1b Complexed With Sp7343-Sp7964, A Ptyr Mimetic' 100.00 298 98.99 98.99 8.33e-175 PDB 1NWE 'Ptp1b R47c Modified At C47 With N-[4-(2-{2-[3-(2-Bromo- Acetylamino)-Propionylamino]-3-Hydroxy-Propionylamino}- Ethyl)-Phenyl]-Oxalamic Acid' 100.00 298 98.99 98.99 8.33e-175 PDB 1NO6 'Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 5 Using A Linked-Fragment Strategy' 100.00 321 100.00 100.00 2.25e-177 PDB 1NNY 'Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 23 Using A Linked-Fragment Strategy' 100.00 321 100.00 100.00 2.25e-177 PDB 1NL9 'Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 12 Using A Linked-Fragment Strategy' 100.00 321 100.00 100.00 2.25e-177 PDB 1LQF 'Structure Of Ptp1b In Complex With A Peptidic Bisphosphonate Inhibitor' 94.97 295 100.00 100.00 1.27e-168 PDB 1L8G 'Crystal Structure Of Ptp1b Complexed With 7-(1,1-Dioxo-1h- Benzo[d]isothiazol-3-Yloxymethyl)-2-(Oxalyl-Amino)-4,7- Dihydro-5h-Thieno[2,3-C]pyran-3-Carboxylic Acid' 100.00 321 99.33 100.00 1.64e-176 PDB 1KAV 'Human Tyrosine Phosphatase 1b Complexed With An Inhibitor' 100.00 298 100.00 100.00 8.25e-178 PDB 1KAK 'Human Tyrosine Phosphatase 1b Complexed With An Inhibitor' 100.00 298 100.00 100.00 8.25e-178 PDB 1JF7 'Human Ptp1b Catalytic Domain Complexed With Pnu177836' 100.00 298 100.00 100.00 8.25e-178 PDB 1I57 'Crystal Structure Of Apo Human Ptp1b (C215s) Mutant' 100.00 310 99.66 99.66 9.44e-177 PDB 1G7G 'Human Ptp1b Catalytic Domain Complexes With Pnu179326' 100.00 298 100.00 100.00 8.25e-178 PDB 1G7F 'Human Ptp1b Catalytic Domain Complexed With Pnu177496' 100.00 298 99.66 100.00 2.65e-177 PDB 1G1H 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Bis-Phosphorylated Peptide (Etd(Ptr)(Ptr) Rkggkgll) From The Insulin Receptor Kinase' 100.00 298 99.66 99.66 4.76e-177 PDB 1G1G 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Mono-Phosphorylated Peptide (Etdy(Ptr) Rkggkgll) From The Insulin Receptor Kinase' 100.00 298 99.66 99.66 4.76e-177 PDB 1G1F 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Tri-Phosphorylated Peptide (Rdi(Ptr) Etd(Ptr)(Ptr)rk) From The Insulin Receptor Kinase' 100.00 298 99.66 99.66 4.76e-177 PDB 1EEO 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Acetyl-E-L-E-F-Ptyr-M-D-Y-E-Nh2' 100.00 321 99.66 99.66 2.23e-176 PDB 1EEN 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Acetyl-D-A-D-Bpa-Ptyr-L-I-P-Q-Q-G' 100.00 321 99.66 99.66 2.23e-176 PDB 1ECV 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 5-Iodo-2-(Oxalyl-Amino)-Benzoic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1C88 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino)-4,5,6,7-Tetrahydro- Thieno[2,3-C]pyridine-3-Carboxylic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1C87 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino-4,7-Dihydro-5h-Thieno[2,3- C]pyran-3-Carboxylic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1C86 'Crystal Structure Of Protein Tyrosine Phosphatase 1b (R47v, D48n) Complexed With 2-(Oxalyl-Amino-4,7-Dihydro-5h- Thieno[2,3-C]pyran-3-Carboxylic Acid' 100.00 298 98.66 99.66 5.92e-176 PDB 1C85 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino)-Benzoic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1C84 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 3-(Oxalyl-Amino)-Naphthalene-2-Carboxlic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1C83 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 6-(Oxalyl-Amino)-1h-Indole-5-Carboxylic Acid' 100.00 298 99.33 100.00 6.48e-177 PDB 1BZJ 'Human Ptp1b Complexed With Tpicooh' 99.33 297 100.00 100.00 1.22e-176 PDB 1BZH 'Cyclic Peptide Inhibitor Of Human Ptp1b' 100.00 298 99.33 100.00 7.11e-177 PDB 1BZC 'Human Ptp1b Catalytic Domain Complexed With Tpi' 100.00 321 99.33 100.00 1.92e-176 PDB 1AAX 'Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Bis(Para-Phosphophenyl)methane (Bppm) Molecules' 100.00 321 99.66 99.66 2.59e-176 PDB 1A5Y 'Protein Tyrosine Phosphatase 1b Cysteinyl-Phosphate Intermediate' 100.00 330 98.66 99.33 2.07e-174 stop_ save_ save_DADEXLIP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DADEXLIP-amide,(X=phenylalanine-p-difluoromethyl phosphonate)' _Molecular_mass 34672 _Mol_thiol_state 'all free' _Details . _Residue_count 8 _Mol_residue_sequence DADEXLIP loop_ _Residue_seq_code _Residue_label 1 ASP 2 ALA 3 ASP 4 GLU 5 X 6 LEU 7 ILE 8 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ptp1b Human 9606 Eukaryota Metazoa Homo sapiens 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 _Details $ptp1b 'recombinant technology' 'E. coli' Escherichia coli BL21 'pET 19-b' ; human hippocampal cDNA library (Clonetech). Human PTP-1B (1-298) was cloned from a human hippocampal cDNA library (Clonetech) using PCR and placed into a pET 19-b vector (Novagen) at the Nco1 restriction site. E. coli strain BL21 (DE3) was transformed, individual colonies picked, inoculated into 5 ml LB-ampicillin medium and grown at 37?C overnight. This culture was diluted 1:100 in a total volume of 50 ml and allowed to grow to an OD600 of 0.6. IPTG (0.1 mM) was added and the culture was incubated with shaking for another 4 h at 37?C. Cells were collected by centrifugation and lysis performed by re-suspending the pellet into 5 ml of ice-cold buffer containing 50 mM TRIS pH.7.6, 150 mM NaCl, 5 mM DTT, 0.1% Triton-X100, 100 ?M PMSF, 100 ?g/ml DNase 1, 2 mM MgCl2, and 100 ?g/ml lysozyme. The suspension was sonicated on ice with 4 x 10 sec bursts of a Branson sonication probe. After leaving at 4?C for 30 min, the sonicate was centrifuged at 35,000g for 20 min and the supernatant collected. The supernatant was buffer exchanged and purified on a cation exchange POROS 20SP column followed by an anion exchange Source 30Q (Pharmacia) column, using linear NaCl gradient elutions. The cation exchange buffer was 50 mM MES, 75 mM NaCl, 5 mM DTT, pH 6.5 and Anion Exchange Buffer was 50 mM TRIS, 50 mM NaCl, 5 mM DTT, pH 8.0. Enzyme was pooled, adjusted to 1 mg/ml (in a buffer of 50 mM NaCl, 50 mM TRIS, 3 mM DTT, pH 7.5) and frozen at -80 C. As judged by SDS-polyacrylamide gel electrophoresis, preparations approached 98% purity. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ptp1b 0.5 mM '[U-100% 15N; U-100% 13C]' $DADEXLIP 1 mM . H2O 30 % . D2O 70 % . stop_ save_ ############################ # Computer software used # ############################ save_nmrPIPE _Saveframe_category software _Name nmrPIPE _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CO)CA_TROSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CA TROSY' _Sample_label $sample_1 save_ save_HN(CA)CO_TROSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CA)CO TROSY' _Sample_label $sample_1 save_ save_HN(CO)CACB_TROSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CACB TROSY' _Sample_label $sample_1 save_ save_HNCACB_TROSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCACB TROSY' _Sample_label $sample_1 save_ save_HNCA_TROSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCA TROSY' _Sample_label $sample_1 save_ save_HNCO_TROSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCO TROSY' _Sample_label $sample_1 save_ save_15N-edited_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CA TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CA)CO TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CACB TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCACB TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCA TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCO TROSY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details 'Standard and TROSY versions of each experiment were performed.' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 n/a temperature 293 1 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 DSS H 1 'methyl protons' ppm 0.0 . direct . . . 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'protein tyrosine phosphatase 1B' _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 MET C C 178.24 . 1 2 . 1 MET CA C 57.80 . 1 3 . 1 MET CB C 31.46 . 1 4 . 2 GLU N N 120.30 . 1 5 . 2 GLU H H 7.83 . 1 6 . 2 GLU C C 178.34 . 1 7 . 2 GLU CA C 57.86 . 1 8 . 2 GLU CB C 28.99 . 1 9 . 3 MET N N 121.24 . 1 10 . 3 MET H H 8.81 . 1 11 . 3 MET C C 178.16 . 1 12 . 3 MET CA C 59.56 . 1 13 . 3 MET CB C 32.72 . 1 14 . 4 GLU N N 118.07 . 1 15 . 4 GLU H H 8.55 . 1 16 . 4 GLU C C 178.70 . 1 17 . 4 GLU CA C 59.49 . 1 18 . 4 GLU CB C 29.00 . 1 19 . 5 LYS N N 119.35 . 1 20 . 5 LYS H H 7.27 . 1 21 . 5 LYS C C 179.39 . 1 22 . 5 LYS CA C 58.11 . 1 23 . 5 LYS CB C 31.07 . 1 24 . 6 GLU N N 121.49 . 1 25 . 6 GLU H H 8.25 . 1 26 . 6 GLU C C 177.84 . 1 27 . 6 GLU CA C 59.20 . 1 28 . 6 GLU CB C 28.98 . 1 29 . 7 PHE N N 118.13 . 1 30 . 7 PHE H H 8.50 . 1 31 . 7 PHE C C 176.49 . 1 32 . 7 PHE CA C 61.74 . 1 33 . 7 PHE CB C 39.28 . 1 34 . 8 GLU N N 116.92 . 1 35 . 8 GLU H H 7.91 . 1 36 . 8 GLU C C 176.51 . 1 37 . 8 GLU CA C 58.87 . 1 38 . 8 GLU CB C 28.97 . 1 39 . 9 GLN N N 117.90 . 1 40 . 9 GLN H H 7.70 . 1 41 . 9 GLN C C 179.23 . 1 42 . 9 GLN CA C 58.32 . 1 43 . 9 GLN CB C 27.40 . 1 44 . 10 ILE N N 121.95 . 1 45 . 10 ILE H H 8.01 . 1 46 . 10 ILE C C 178.34 . 1 47 . 10 ILE CA C 64.27 . 1 48 . 10 ILE CB C 37.02 . 1 49 . 11 ASP N N 118.84 . 1 50 . 11 ASP H H 8.34 . 1 51 . 11 ASP C C 180.35 . 1 52 . 11 ASP CA C 57.00 . 1 53 . 11 ASP CB C 41.43 . 1 54 . 12 LYS N N 117.11 . 1 55 . 12 LYS H H 8.25 . 1 56 . 12 LYS C C 178.41 . 1 57 . 12 LYS CA C 58.29 . 1 58 . 12 LYS CB C 31.31 . 1 59 . 13 SER N N 110.64 . 1 60 . 13 SER H H 7.40 . 1 61 . 13 SER C C 174.05 . 1 62 . 13 SER CA C 58.15 . 1 63 . 13 SER CB C 63.50 . 1 64 . 14 GLY N N 112.27 . 1 65 . 14 GLY H H 7.73 . 1 66 . 14 GLY C C 176.97 . 1 67 . 14 GLY CA C 46.40 . 1 68 . 15 SER N N 110.78 . 1 69 . 15 SER H H 7.66 . 1 70 . 15 SER C C 174.00 . 1 71 . 15 SER CA C 58.18 . 1 72 . 15 SER CB C 62.77 . 1 73 . 16 TRP N N 120.96 . 1 74 . 16 TRP H H 7.02 . 1 75 . 16 TRP C C 177.68 . 1 76 . 16 TRP CA C 59.94 . 1 77 . 16 TRP CB C 28.33 . 1 78 . 17 ALA N N 118.75 . 1 79 . 17 ALA H H 8.61 . 1 80 . 17 ALA C C 180.15 . 1 81 . 17 ALA CA C 55.04 . 1 82 . 17 ALA CB C 16.91 . 1 83 . 18 ALA N N 122.04 . 1 84 . 18 ALA H H 7.59 . 1 85 . 18 ALA C C 180.19 . 1 86 . 18 ALA CA C 54.60 . 1 87 . 18 ALA CB C 17.19 . 1 88 . 19 ILE N N 118.50 . 1 89 . 19 ILE H H 7.81 . 1 90 . 19 ILE C C 178.74 . 1 91 . 19 ILE CA C 62.83 . 1 92 . 19 ILE CB C 36.42 . 1 93 . 20 TYR N N 119.47 . 1 94 . 20 TYR H H 8.52 . 1 95 . 20 TYR C C 177.06 . 1 96 . 20 TYR CA C 61.49 . 1 97 . 20 TYR CB C 38.01 . 1 98 . 21 GLN N N 117.57 . 1 99 . 21 GLN H H 8.07 . 1 100 . 21 GLN C C 177.97 . 1 101 . 21 GLN CA C 58.09 . 1 102 . 21 GLN CB C 26.91 . 1 103 . 22 ASP N N 119.86 . 1 104 . 22 ASP H H 7.71 . 1 105 . 22 ASP C C 178.92 . 1 106 . 22 ASP CA C 57.21 . 1 107 . 22 ASP CB C 39.28 . 1 108 . 23 ILE N N 119.69 . 1 109 . 23 ILE H H 7.52 . 1 110 . 23 ILE C C 177.24 . 1 111 . 23 ILE CA C 64.46 . 1 112 . 23 ILE CB C 36.36 . 1 113 . 24 ARG N N 116.76 . 1 114 . 24 ARG H H 7.59 . 1 115 . 24 ARG C C 179.34 . 1 116 . 24 ARG CA C 59.34 . 1 117 . 24 ARG CB C 28.98 . 1 118 . 25 HIS N N 116.22 . 1 119 . 25 HIS H H 8.05 . 1 120 . 25 HIS C C 176.68 . 1 121 . 25 HIS CA C 57.80 . 1 122 . 25 HIS CB C 29.69 . 1 123 . 26 GLU N N 116.99 . 1 124 . 26 GLU H H 7.73 . 1 125 . 26 GLU C C 176.59 . 1 126 . 26 GLU CA C 55.97 . 1 127 . 26 GLU CB C 30.01 . 1 128 . 27 ALA N N 122.52 . 1 129 . 27 ALA H H 7.34 . 1 130 . 27 ALA C C 177.40 . 1 131 . 27 ALA CA C 52.37 . 1 132 . 27 ALA CB C 18.47 . 1 133 . 28 SER N N 116.61 . 1 134 . 28 SER H H 7.88 . 1 135 . 28 SER C C 172.53 . 1 136 . 28 SER CA C 58.91 . 1 137 . 28 SER CB C 64.19 . 1 138 . 29 ASP N N 121.71 . 1 139 . 29 ASP H H 7.99 . 1 140 . 29 ASP C C 173.61 . 1 141 . 29 ASP CA C 53.13 . 1 142 . 29 ASP CB C 42.80 . 1 143 . 30 PHE N N 118.84 . 1 144 . 30 PHE H H 6.56 . 1 145 . 30 PHE C C 173.10 . 1 146 . 30 PHE CA C 54.78 . 1 147 . 30 PHE CB C 40.28 . 1 148 . 31 PRO C C 177.07 . 1 149 . 31 PRO CA C 63.77 . 1 150 . 31 PRO CB C 31.91 . 1 151 . 32 CYS N N 125.42 . 1 152 . 32 CYS H H 9.04 . 1 153 . 32 CYS C C 174.49 . 1 154 . 32 CYS CA C 56.01 . 1 155 . 32 CYS CB C 28.25 . 1 156 . 33 ARG N N 121.03 . 1 157 . 33 ARG H H 9.36 . 1 158 . 33 ARG C C 180.97 . 1 159 . 33 ARG CA C 59.29 . 1 160 . 33 ARG CB C 29.69 . 1 161 . 34 VAL N N 121.09 . 1 162 . 34 VAL H H 9.59 . 1 163 . 34 VAL C C 179.54 . 1 164 . 34 VAL CA C 66.56 . 1 165 . 34 VAL CB C 30.09 . 1 166 . 35 ALA N N 120.87 . 1 167 . 35 ALA H H 8.36 . 1 168 . 35 ALA C C 178.13 . 1 169 . 35 ALA CA C 54.17 . 1 170 . 35 ALA CB C 20.18 . 1 171 . 36 LYS N N 110.04 . 1 172 . 36 LYS H H 6.66 . 1 173 . 36 LYS C C 176.78 . 1 174 . 36 LYS CA C 54.53 . 1 175 . 36 LYS CB C 31.74 . 1 176 . 37 LEU N N 123.00 . 1 177 . 37 LEU H H 7.38 . 1 178 . 37 LEU C C 177.94 . 1 179 . 37 LEU CA C 53.57 . 1 180 . 37 LEU CB C 40.08 . 1 181 . 39 LYS C C 176.00 . 1 182 . 39 LYS CA C 57.31 . 1 183 . 39 LYS CB C 30.21 . 1 184 . 40 ASN N N 116.11 . 1 185 . 40 ASN H H 7.63 . 1 186 . 40 ASN C C 176.71 . 1 187 . 40 ASN CA C 52.45 . 1 188 . 40 ASN CB C 38.72 . 1 189 . 41 LYS N N 122.89 . 1 190 . 41 LYS H H 7.26 . 1 191 . 41 LYS C C 179.23 . 1 192 . 41 LYS CA C 60.27 . 1 193 . 41 LYS CB C 31.74 . 1 194 . 42 ASN C C 175.55 . 1 195 . 42 ASN CA C 52.55 . 1 196 . 42 ASN CB C 36.20 . 1 197 . 43 ARG N N 114.77 . 1 198 . 43 ARG H H 7.75 . 1 199 . 43 ARG C C 176.21 . 1 200 . 43 ARG CA C 55.73 . 1 201 . 43 ARG CB C 30.49 . 1 202 . 44 ASN N N 119.35 . 1 203 . 44 ASN H H 7.41 . 1 204 . 44 ASN C C 172.93 . 1 205 . 44 ASN CA C 52.10 . 1 206 . 44 ASN CB C 40.36 . 1 207 . 45 ARG N N 125.83 . 1 208 . 45 ARG H H 9.10 . 1 209 . 45 ARG C C 174.82 . 1 210 . 45 ARG CA C 58.53 . 1 211 . 45 ARG CB C 29.90 . 1 212 . 46 TYR N N 116.19 . 1 213 . 46 TYR H H 9.43 . 1 214 . 46 TYR C C 177.20 . 1 215 . 46 TYR CA C 54.73 . 1 216 . 46 TYR CB C 40.41 . 1 217 . 47 ARG N N 120.80 . 1 218 . 47 ARG H H 9.00 . 1 219 . 47 ARG C C 175.68 . 1 220 . 47 ARG CA C 56.80 . 1 221 . 47 ARG CB C 29.41 . 1 222 . 48 ASP N N 114.33 . 1 223 . 48 ASP H H 9.10 . 1 224 . 48 ASP C C 175.24 . 1 225 . 48 ASP CA C 51.95 . 1 226 . 48 ASP CB C 39.37 . 1 227 . 49 VAL N N 117.56 . 1 228 . 49 VAL H H 6.64 . 1 229 . 49 VAL C C 175.41 . 1 230 . 49 VAL CA C 62.13 . 1 231 . 49 VAL CB C 32.74 . 1 232 . 50 SER N N 122.00 . 1 233 . 50 SER H H 7.55 . 1 234 . 50 SER C C 170.50 . 1 235 . 50 SER CA C 55.26 . 1 236 . 50 SER CB C 64.44 . 1 237 . 51 PRO C C 175.75 . 1 238 . 51 PRO CA C 61.33 . 1 239 . 51 PRO CB C 31.29 . 1 240 . 52 PHE N N 123.49 . 1 241 . 52 PHE H H 6.93 . 1 242 . 52 PHE C C 178.15 . 1 243 . 52 PHE CA C 55.02 . 1 244 . 52 PHE CB C 38.50 . 1 245 . 53 ASP N N 123.79 . 1 246 . 53 ASP H H 9.22 . 1 247 . 53 ASP C C 180.19 . 1 248 . 53 ASP CA C 58.48 . 1 249 . 53 ASP CB C 40.03 . 1 250 . 54 HIS N N 114.70 . 1 251 . 54 HIS H H 8.90 . 1 252 . 54 HIS C C 175.81 . 1 253 . 54 HIS CA C 58.76 . 1 254 . 54 HIS CB C 29.68 . 1 255 . 55 SER N N 107.55 . 1 256 . 55 SER H H 6.24 . 1 257 . 55 SER C C 174.11 . 1 258 . 55 SER CA C 55.10 . 1 259 . 55 SER CB C 63.09 . 1 260 . 56 ARG N N 122.35 . 1 261 . 56 ARG H H 7.12 . 1 262 . 56 ARG C C 175.57 . 1 263 . 56 ARG CA C 55.24 . 1 264 . 56 ARG CB C 27.65 . 1 265 . 57 ILE N N 121.61 . 1 266 . 57 ILE H H 7.08 . 1 267 . 57 ILE C C 175.08 . 1 268 . 57 ILE CA C 56.79 . 1 269 . 57 ILE CB C 35.42 . 1 270 . 58 LYS N N 126.35 . 1 271 . 58 LYS H H 8.36 . 1 272 . 58 LYS C C 177.75 . 1 273 . 58 LYS CA C 54.57 . 1 274 . 58 LYS CB C 32.14 . 1 275 . 59 LEU N N 124.62 . 1 276 . 59 LEU H H 9.15 . 1 277 . 59 LEU C C 178.97 . 1 278 . 59 LEU CA C 53.58 . 1 279 . 59 LEU CB C 41.44 . 1 280 . 60 HIS N N 123.59 . 1 281 . 60 HIS H H 9.40 . 1 282 . 60 HIS C C 174.72 . 1 283 . 60 HIS CA C 53.60 . 1 284 . 60 HIS CB C 27.19 . 1 285 . 61 GLN N N 119.02 . 1 286 . 61 GLN H H 7.31 . 1 287 . 61 GLN C C 175.67 . 1 288 . 61 GLN CA C 54.10 . 1 289 . 61 GLN CB C 30.77 . 1 290 . 62 GLU N N 120.66 . 1 291 . 62 GLU H H 8.36 . 1 292 . 62 GLU C C 177.53 . 1 293 . 62 GLU CA C 57.50 . 1 294 . 62 GLU CB C 29.66 . 1 295 . 63 ASP N N 117.76 . 1 296 . 63 ASP H H 8.25 . 1 297 . 63 ASP C C 176.64 . 1 298 . 63 ASP CA C 56.10 . 1 299 . 63 ASP CB C 40.34 . 1 300 . 64 ASN N N 113.31 . 1 301 . 64 ASN H H 7.31 . 1 302 . 64 ASN C C 174.44 . 1 303 . 64 ASN CA C 53.05 . 1 304 . 64 ASN CB C 37.45 . 1 305 . 65 ASP N N 125.24 . 1 306 . 65 ASP H H 8.03 . 1 307 . 65 ASP C C 178.37 . 1 308 . 65 ASP CA C 52.68 . 1 309 . 65 ASP CB C 41.16 . 1 310 . 66 TYR N N 117.93 . 1 311 . 66 TYR H H 7.90 . 1 312 . 66 TYR C C 174.98 . 1 313 . 66 TYR CA C 60.51 . 1 314 . 66 TYR CB C 38.46 . 1 315 . 67 ILE N N 124.53 . 1 316 . 67 ILE H H 7.55 . 1 317 . 67 ILE C C 172.77 . 1 318 . 67 ILE CA C 58.33 . 1 319 . 67 ILE CB C 41.00 . 1 320 . 68 ASN N N 124.84 . 1 321 . 68 ASN H H 8.03 . 1 322 . 68 ASN C C 172.99 . 1 323 . 68 ASN CA C 52.06 . 1 324 . 68 ASN CB C 35.50 . 1 325 . 69 ALA N N 128.10 . 1 326 . 69 ALA H H 7.62 . 1 327 . 69 ALA C C 175.43 . 1 328 . 69 ALA CA C 51.27 . 1 329 . 69 ALA CB C 22.28 . 1 330 . 70 SER N N 116.20 . 1 331 . 70 SER H H 8.97 . 1 332 . 70 SER C C 170.86 . 1 333 . 70 SER CA C 57.10 . 1 334 . 70 SER CB C 66.55 . 1 335 . 71 LEU N N 125.92 . 1 336 . 71 LEU H H 8.85 . 1 337 . 71 LEU C C 175.03 . 1 338 . 71 LEU CA C 53.55 . 1 339 . 71 LEU CB C 41.32 . 1 340 . 72 ILE N N 128.01 . 1 341 . 72 ILE H H 9.38 . 1 342 . 72 ILE C C 173.81 . 1 343 . 72 ILE CA C 59.96 . 1 344 . 72 ILE CB C 36.20 . 1 345 . 73 LYS C C 174.05 . 1 346 . 73 LYS CA C 54.53 . 1 347 . 73 LYS CB C 32.67 . 1 348 . 74 MET N N 123.41 . 1 349 . 74 MET H H 8.07 . 1 350 . 74 MET C C 176.93 . 1 351 . 74 MET CA C 51.76 . 1 352 . 74 MET CB C 28.64 . 1 353 . 75 GLU N N 125.47 . 1 354 . 75 GLU H H 8.29 . 1 355 . 75 GLU C C 179.22 . 1 356 . 75 GLU CA C 59.86 . 1 357 . 75 GLU CB C 28.84 . 1 358 . 76 GLU C C 177.84 . 1 359 . 76 GLU CA C 58.55 . 1 360 . 76 GLU CB C 28.24 . 1 361 . 77 ALA N N 116.80 . 1 362 . 77 ALA H H 7.36 . 1 363 . 77 ALA C C 174.78 . 1 364 . 77 ALA CA C 52.29 . 1 365 . 77 ALA CB C 18.28 . 1 366 . 78 GLN N N 110.64 . 1 367 . 78 GLN H H 7.58 . 1 368 . 78 GLN C C 174.31 . 1 369 . 78 GLN CA C 55.81 . 1 370 . 78 GLN CB C 25.47 . 1 371 . 79 ARG N N 117.59 . 1 372 . 79 ARG H H 7.14 . 1 373 . 79 ARG C C 173.75 . 1 374 . 79 ARG CA C 54.81 . 1 375 . 79 ARG CB C 33.65 . 1 376 . 80 SER N N 118.78 . 1 377 . 80 SER H H 7.64 . 1 378 . 80 SER C C 170.40 . 1 379 . 80 SER CA C 56.03 . 1 380 . 80 SER CB C 65.71 . 1 381 . 81 TYR N N 116.27 . 1 382 . 81 TYR H H 8.45 . 1 383 . 81 TYR C C 174.97 . 1 384 . 81 TYR CA C 54.79 . 1 385 . 81 TYR CB C 43.01 . 1 386 . 82 ILE N N 122.24 . 1 387 . 82 ILE H H 9.26 . 1 388 . 82 ILE C C 174.02 . 1 389 . 82 ILE CA C 59.97 . 1 390 . 82 ILE CB C 38.18 . 1 391 . 83 LEU N N 128.34 . 1 392 . 83 LEU H H 8.54 . 1 393 . 83 LEU C C 176.86 . 1 394 . 83 LEU CA C 53.64 . 1 395 . 83 LEU CB C 43.16 . 1 396 . 84 THR N N 115.21 . 1 397 . 84 THR H H 8.40 . 1 398 . 84 THR C C 169.61 . 1 399 . 84 THR CA C 57.16 . 1 400 . 84 THR CB C 71.24 . 1 401 . 85 GLN N N 115.49 . 1 402 . 85 GLN H H 6.24 . 1 403 . 85 GLN C C 175.03 . 1 404 . 85 GLN CA C 51.98 . 1 405 . 85 GLN CB C 27.90 . 1 406 . 86 GLY N N 112.05 . 1 407 . 86 GLY H H 8.80 . 1 408 . 86 GLY C C 173.31 . 1 409 . 86 GLY CA C 44.58 . 1 410 . 87 PRO C C 175.59 . 1 411 . 87 PRO CA C 63.44 . 1 412 . 87 PRO CB C 31.47 . 1 413 . 88 LEU N N 122.42 . 1 414 . 88 LEU H H 7.73 . 1 415 . 88 LEU C C 176.58 . 1 416 . 88 LEU CA C 52.71 . 1 417 . 88 LEU CB C 41.42 . 1 418 . 89 PRO C C 177.04 . 1 419 . 89 PRO CA C 65.65 . 1 420 . 89 PRO CB C 30.52 . 1 421 . 90 ASN N N 106.15 . 1 422 . 90 ASN H H 8.45 . 1 423 . 90 ASN C C 176.27 . 1 424 . 90 ASN CA C 53.45 . 1 425 . 90 ASN CB C 36.65 . 1 426 . 91 THR N N 111.00 . 1 427 . 91 THR H H 7.98 . 1 428 . 91 THR C C 174.65 . 1 429 . 91 THR CA C 60.22 . 1 430 . 91 THR CB C 68.90 . 1 431 . 92 CYS N N 120.62 . 1 432 . 92 CYS H H 7.44 . 1 433 . 92 CYS C C 175.71 . 1 434 . 92 CYS CA C 63.59 . 1 435 . 92 CYS CB C 27.69 . 1 436 . 93 GLY N N 107.82 . 1 437 . 93 GLY H H 8.19 . 1 438 . 93 GLY C C 178.06 . 1 439 . 93 GLY CA C 47.21 . 1 440 . 94 HIS N N 123.07 . 1 441 . 94 HIS H H 7.34 . 1 442 . 94 HIS C C 176.56 . 1 443 . 94 HIS CA C 56.52 . 1 444 . 94 HIS CB C 31.86 . 1 445 . 95 PHE N N 118.68 . 1 446 . 95 PHE H H 8.15 . 1 447 . 95 PHE C C 175.71 . 1 448 . 95 PHE CA C 61.62 . 1 449 . 95 PHE CB C 37.51 . 1 450 . 96 TRP N N 117.10 . 1 451 . 96 TRP H H 8.17 . 1 452 . 96 TRP C C 177.37 . 1 453 . 96 TRP CA C 54.55 . 1 454 . 96 TRP CB C 29.66 . 1 455 . 104 SER C C 172.73 . 1 456 . 104 SER CA C 60.88 . 1 457 . 104 SER CB C 63.03 . 1 458 . 105 ARG N N 122.70 . 1 459 . 105 ARG H H 9.34 . 1 460 . 105 ARG C C 174.21 . 1 461 . 105 ARG CA C 54.50 . 1 462 . 105 ARG CB C 31.37 . 1 463 . 106 GLY N N 102.02 . 1 464 . 106 GLY H H 7.17 . 1 465 . 106 GLY CA C 43.20 . 1 466 . 121 CYS C C 172.28 . 1 467 . 121 CYS CA C 58.47 . 1 468 . 122 ALA N N 126.17 . 1 469 . 122 ALA H H 7.80 . 1 470 . 122 ALA C C 176.41 . 1 471 . 122 ALA CA C 51.66 . 1 472 . 122 ALA CB C 18.29 . 1 473 . 123 GLN N N 119.97 . 1 474 . 123 GLN H H 8.32 . 1 475 . 123 GLN C C 174.53 . 1 476 . 123 GLN CA C 54.99 . 1 477 . 123 GLN CB C 25.80 . 1 478 . 124 TYR N N 121.46 . 1 479 . 124 TYR H H 6.51 . 1 480 . 124 TYR C C 171.12 . 1 481 . 124 TYR CA C 55.98 . 1 482 . 125 TRP N N 119.42 . 1 483 . 125 TRP H H 6.47 . 1 484 . 125 TRP C C 171.93 . 1 485 . 125 TRP CA C 54.94 . 1 486 . 125 TRP CB C 30.51 . 1 487 . 132 GLU C C 175.04 . 1 488 . 132 GLU CA C 53.63 . 1 489 . 132 GLU CB C 32.41 . 1 490 . 133 MET N N 120.36 . 1 491 . 133 MET H H 8.78 . 1 492 . 133 MET C C 172.71 . 1 493 . 133 MET CA C 54.77 . 1 494 . 133 MET CB C 37.73 . 1 495 . 134 ILE N N 121.41 . 1 496 . 134 ILE H H 8.09 . 1 497 . 134 ILE C C 174.87 . 1 498 . 134 ILE CA C 59.55 . 1 499 . 134 ILE CB C 39.25 . 1 500 . 135 PHE N N 127.10 . 1 501 . 135 PHE H H 8.83 . 1 502 . 135 PHE C C 176.00 . 1 503 . 135 PHE CA C 56.20 . 1 504 . 135 PHE CB C 37.14 . 1 505 . 136 GLU N N 123.47 . 1 506 . 136 GLU H H 8.89 . 1 507 . 136 GLU C C 177.57 . 1 508 . 136 GLU CA C 58.68 . 1 509 . 136 GLU CB C 29.03 . 1 510 . 137 ASP N N 115.71 . 1 511 . 137 ASP H H 8.99 . 1 512 . 137 ASP C C 178.31 . 1 513 . 137 ASP CA C 55.38 . 1 514 . 137 ASP CB C 37.93 . 1 515 . 138 THR N N 107.37 . 1 516 . 138 THR H H 7.37 . 1 517 . 138 THR C C 173.84 . 1 518 . 138 THR CA C 60.05 . 1 519 . 138 THR CB C 68.27 . 1 520 . 139 ASN N N 120.39 . 1 521 . 139 ASN H H 7.89 . 1 522 . 139 ASN C C 172.89 . 1 523 . 139 ASN CA C 53.22 . 1 524 . 139 ASN CB C 37.21 . 1 525 . 140 LEU N N 116.38 . 1 526 . 140 LEU H H 7.33 . 1 527 . 140 LEU C C 173.98 . 1 528 . 140 LEU CA C 53.12 . 1 529 . 141 LYS C C 173.00 . 1 530 . 141 LYS CA C 53.84 . 1 531 . 142 LEU N N 128.93 . 1 532 . 142 LEU H H 9.06 . 1 533 . 142 LEU CA C 52.09 . 1 534 . 143 THR C C 174.14 . 1 535 . 143 THR CA C 60.93 . 1 536 . 143 THR CB C 70.69 . 1 537 . 144 LEU N N 127.19 . 1 538 . 144 LEU H H 8.88 . 1 539 . 144 LEU C C 174.41 . 1 540 . 144 LEU CA C 54.86 . 1 541 . 144 LEU CB C 42.05 . 1 542 . 145 ILE N N 128.87 . 1 543 . 145 ILE H H 8.81 . 1 544 . 145 ILE C C 176.81 . 1 545 . 145 ILE CA C 60.65 . 1 546 . 145 ILE CB C 35.82 . 1 547 . 146 SER N N 110.67 . 1 548 . 146 SER H H 7.73 . 1 549 . 146 SER C C 172.05 . 1 550 . 146 SER CA C 57.38 . 1 551 . 146 SER CB C 64.91 . 1 552 . 147 GLU N N 119.51 . 1 553 . 147 GLU H H 8.51 . 1 554 . 147 GLU C C 173.23 . 1 555 . 147 GLU CA C 55.39 . 1 556 . 147 GLU CB C 33.62 . 1 557 . 148 ASP N N 126.19 . 1 558 . 148 ASP H H 8.78 . 1 559 . 148 ASP C C 174.37 . 1 560 . 148 ASP CA C 52.82 . 1 561 . 148 ASP CB C 41.44 . 1 562 . 149 ILE N N 126.28 . 1 563 . 149 ILE H H 8.46 . 1 564 . 149 ILE C C 176.05 . 1 565 . 149 ILE CA C 61.68 . 1 566 . 149 ILE CB C 38.06 . 1 567 . 150 LYS N N 128.24 . 1 568 . 150 LYS H H 8.11 . 1 569 . 150 LYS C C 177.63 . 1 570 . 150 LYS CA C 53.00 . 1 571 . 150 LYS CB C 31.61 . 1 572 . 151 SER N N 115.04 . 1 573 . 151 SER H H 8.46 . 1 574 . 151 SER C C 175.90 . 1 575 . 151 SER CA C 61.30 . 1 576 . 152 TYR C C 172.91 . 1 577 . 152 TYR CA C 54.89 . 1 578 . 152 TYR CB C 37.72 . 1 579 . 153 TYR N N 114.14 . 1 580 . 153 TYR H H 6.37 . 1 581 . 153 TYR C C 172.54 . 1 582 . 153 TYR CA C 55.64 . 1 583 . 153 TYR CB C 39.04 . 1 584 . 154 THR N N 116.22 . 1 585 . 154 THR H H 9.26 . 1 586 . 154 THR C C 172.95 . 1 587 . 154 THR CA C 60.60 . 1 588 . 154 THR CB C 72.94 . 1 589 . 155 VAL N N 126.05 . 1 590 . 155 VAL H H 8.70 . 1 591 . 155 VAL C C 175.55 . 1 592 . 155 VAL CA C 60.34 . 1 593 . 156 ARG C C 174.25 . 1 594 . 156 ARG CA C 53.85 . 1 595 . 157 GLN N N 120.23 . 1 596 . 157 GLN H H 8.07 . 1 597 . 157 GLN CA C 54.66 . 1 598 . 157 GLN CB C 32.05 . 1 599 . 161 GLU C C 174.81 . 1 600 . 161 GLU CA C 53.02 . 1 601 . 161 GLU CB C 32.51 . 1 602 . 162 ASN N N 123.60 . 1 603 . 162 ASN H H 8.13 . 1 604 . 162 ASN C C 175.85 . 1 605 . 162 ASN CA C 51.37 . 1 606 . 162 ASN CB C 37.16 . 1 607 . 163 LEU N N 125.02 . 1 608 . 163 LEU H H 8.17 . 1 609 . 163 LEU C C 178.36 . 1 610 . 163 LEU CA C 56.33 . 1 611 . 163 LEU CB C 39.98 . 1 612 . 164 THR N N 114.32 . 1 613 . 164 THR H H 8.15 . 1 614 . 164 THR C C 175.69 . 1 615 . 164 THR CA C 64.64 . 1 616 . 164 THR CB C 68.02 . 1 617 . 165 THR N N 108.56 . 1 618 . 165 THR H H 6.94 . 1 619 . 165 THR C C 175.66 . 1 620 . 165 THR CA C 61.39 . 1 621 . 165 THR CB C 69.65 . 1 622 . 166 GLN N N 115.96 . 1 623 . 166 GLN H H 8.29 . 1 624 . 166 GLN C C 174.88 . 1 625 . 166 GLN CA C 57.49 . 1 626 . 166 GLN CB C 25.43 . 1 627 . 167 GLU N N 118.71 . 1 628 . 167 GLU H H 7.35 . 1 629 . 167 GLU C C 175.23 . 1 630 . 167 GLU CA C 55.81 . 1 631 . 167 GLU CB C 32.60 . 1 632 . 168 THR N N 112.96 . 1 633 . 168 THR H H 8.39 . 1 634 . 168 THR C C 174.44 . 1 635 . 168 THR CA C 59.17 . 1 636 . 168 THR CB C 71.35 . 1 637 . 176 TYR C C 176.68 . 1 638 . 176 TYR CA C 57.30 . 1 639 . 177 THR N N 115.36 . 1 640 . 177 THR H H 8.07 . 1 641 . 177 THR C C 176.44 . 1 642 . 177 THR CA C 63.09 . 1 643 . 177 THR CB C 68.45 . 1 644 . 178 THR N N 109.20 . 1 645 . 178 THR H H 6.79 . 1 646 . 178 THR CA C 59.70 . 1 647 . 180 PRO C C 176.63 . 1 648 . 180 PRO CA C 62.15 . 1 649 . 180 PRO CB C 32.53 . 1 650 . 181 ASP N N 120.13 . 1 651 . 181 ASP H H 8.77 . 1 652 . 181 ASP C C 176.26 . 1 653 . 181 ASP CA C 55.00 . 1 654 . 181 ASP CB C 38.96 . 1 655 . 182 PHE N N 114.86 . 1 656 . 182 PHE H H 8.14 . 1 657 . 182 PHE C C 174.70 . 1 658 . 182 PHE CA C 60.50 . 1 659 . 183 GLY N N 107.45 . 1 660 . 183 GLY H H 8.02 . 1 661 . 183 GLY C C 173.83 . 1 662 . 183 GLY CA C 43.00 . 1 663 . 184 VAL N N 112.78 . 1 664 . 184 VAL H H 8.29 . 1 665 . 184 VAL C C 171.52 . 1 666 . 184 VAL CA C 57.76 . 1 667 . 184 VAL CB C 31.75 . 1 668 . 188 PRO C C 177.17 . 1 669 . 188 PRO CA C 65.32 . 1 670 . 188 PRO CB C 30.16 . 1 671 . 189 ALA N N 117.31 . 1 672 . 189 ALA H H 8.03 . 1 673 . 189 ALA C C 179.25 . 1 674 . 189 ALA CA C 55.26 . 1 675 . 189 ALA CB C 18.40 . 1 676 . 190 SER N N 113.88 . 1 677 . 190 SER H H 8.04 . 1 678 . 190 SER C C 177.63 . 1 679 . 190 SER CA C 61.00 . 1 680 . 191 PHE N N 123.15 . 1 681 . 191 PHE H H 7.38 . 1 682 . 191 PHE C C 175.60 . 1 683 . 191 PHE CA C 61.14 . 1 684 . 192 LEU N N 120.23 . 1 685 . 192 LEU H H 8.90 . 1 686 . 192 LEU C C 177.98 . 1 687 . 192 LEU CA C 56.88 . 1 688 . 192 LEU CB C 39.45 . 1 689 . 193 ASN N N 116.21 . 1 690 . 193 ASN H H 8.35 . 1 691 . 193 ASN C C 176.92 . 1 692 . 193 ASN CA C 56.56 . 1 693 . 193 ASN CB C 38.98 . 1 694 . 194 PHE N N 116.89 . 1 695 . 194 PHE H H 7.15 . 1 696 . 194 PHE C C 178.24 . 1 697 . 194 PHE CA C 61.11 . 1 698 . 194 PHE CB C 35.83 . 1 699 . 195 LEU N N 122.45 . 1 700 . 195 LEU H H 7.61 . 1 701 . 195 LEU C C 179.73 . 1 702 . 195 LEU CA C 57.80 . 1 703 . 198 VAL C C 181.36 . 1 704 . 198 VAL CA C 65.41 . 1 705 . 198 VAL CB C 29.64 . 1 706 . 199 ARG N N 119.82 . 1 707 . 199 ARG H H 8.38 . 1 708 . 199 ARG C C 180.12 . 1 709 . 199 ARG CA C 59.62 . 1 710 . 199 ARG CB C 30.08 . 1 711 . 200 GLU N N 119.80 . 1 712 . 200 GLU H H 8.52 . 1 713 . 200 GLU C C 177.45 . 1 714 . 200 GLU CA C 58.11 . 1 715 . 200 GLU CB C 28.71 . 1 716 . 201 SER N N 111.69 . 1 717 . 201 SER H H 7.29 . 1 718 . 201 SER C C 175.21 . 1 719 . 201 SER CA C 59.84 . 1 720 . 201 SER CB C 65.50 . 1 721 . 202 GLY N N 109.40 . 1 722 . 202 GLY H H 7.56 . 1 723 . 202 GLY C C 175.97 . 1 724 . 202 GLY CA C 45.55 . 1 725 . 203 SER N N 113.35 . 1 726 . 203 SER H H 7.76 . 1 727 . 203 SER C C 171.72 . 1 728 . 203 SER CA C 62.53 . 1 729 . 203 SER CB C 62.20 . 1 730 . 204 LEU N N 115.67 . 1 731 . 204 LEU H H 8.17 . 1 732 . 204 LEU C C 176.60 . 1 733 . 204 LEU CA C 53.33 . 1 734 . 204 LEU CB C 39.59 . 1 735 . 205 SER N N 115.26 . 1 736 . 205 SER H H 7.23 . 1 737 . 205 SER C C 175.00 . 1 738 . 205 SER CA C 56.46 . 1 739 . 205 SER CB C 62.98 . 1 740 . 206 PRO C C 176.72 . 1 741 . 206 PRO CA C 64.13 . 1 742 . 206 PRO CB C 30.70 . 1 743 . 207 GLU N N 117.04 . 1 744 . 207 GLU H H 8.15 . 1 745 . 207 GLU C C 176.05 . 1 746 . 207 GLU CA C 57.09 . 1 747 . 207 GLU CB C 28.21 . 1 748 . 208 HIS N N 118.60 . 1 749 . 208 HIS H H 7.38 . 1 750 . 208 HIS C C 175.23 . 1 751 . 208 HIS CA C 53.77 . 1 752 . 208 HIS CB C 33.26 . 1 753 . 209 GLY N N 103.81 . 1 754 . 209 GLY H H 7.22 . 1 755 . 209 GLY C C 171.09 . 1 756 . 209 GLY CA C 43.90 . 1 757 . 217 ALA C C 178.14 . 1 758 . 217 ALA CA C 51.00 . 1 759 . 218 GLY N N 113.30 . 1 760 . 218 GLY H H 9.00 . 1 761 . 218 GLY C C 175.81 . 1 762 . 218 GLY CA C 47.00 . 1 763 . 222 SER C C 176.46 . 1 764 . 222 SER CA C 63.82 . 1 765 . 223 GLY N N 104.01 . 1 766 . 223 GLY H H 6.24 . 1 767 . 223 GLY C C 173.49 . 1 768 . 223 GLY CA C 47.20 . 1 769 . 224 THR N N 119.68 . 1 770 . 224 THR H H 7.44 . 1 771 . 224 THR C C 173.52 . 1 772 . 224 THR CA C 67.31 . 1 773 . 225 PHE N N 118.75 . 1 774 . 225 PHE H H 8.15 . 1 775 . 225 PHE C C 175.71 . 1 776 . 225 PHE CA C 61.92 . 1 777 . 225 PHE CB C 39.98 . 1 778 . 226 CYS N N 114.32 . 1 779 . 226 CYS H H 7.66 . 1 780 . 226 CYS C C 176.13 . 1 781 . 226 CYS CA C 62.90 . 1 782 . 226 CYS CB C 26.36 . 1 783 . 227 LEU N N 120.56 . 1 784 . 227 LEU H H 8.34 . 1 785 . 227 LEU C C 179.17 . 1 786 . 227 LEU CA C 57.59 . 1 787 . 227 LEU CB C 40.90 . 1 788 . 228 ALA N N 118.74 . 1 789 . 228 ALA H H 7.63 . 1 790 . 228 ALA C C 178.56 . 1 791 . 228 ALA CA C 54.82 . 1 792 . 228 ALA CB C 16.87 . 1 793 . 229 ASP N N 113.46 . 1 794 . 229 ASP H H 7.33 . 1 795 . 229 ASP C C 178.24 . 1 796 . 229 ASP CA C 58.27 . 1 797 . 229 ASP CB C 40.34 . 1 798 . 230 THR N N 114.50 . 1 799 . 230 THR H H 8.55 . 1 800 . 230 THR C C 176.80 . 1 801 . 230 THR CA C 68.05 . 1 802 . 230 THR CB C 65.61 . 1 803 . 231 CYS N N 117.38 . 1 804 . 231 CYS H H 8.37 . 1 805 . 231 CYS C C 176.90 . 1 806 . 231 CYS CA C 65.52 . 1 807 . 231 CYS CB C 27.17 . 1 808 . 232 LEU N N 117.52 . 1 809 . 232 LEU H H 7.79 . 1 810 . 232 LEU C C 180.40 . 1 811 . 232 LEU CA C 57.52 . 1 812 . 232 LEU CB C 40.50 . 1 813 . 233 LEU N N 121.78 . 1 814 . 233 LEU H H 7.84 . 1 815 . 233 LEU C C 180.28 . 1 816 . 233 LEU CA C 57.44 . 1 817 . 233 LEU CB C 41.38 . 1 818 . 234 LEU N N 118.56 . 1 819 . 234 LEU H H 8.35 . 1 820 . 234 LEU C C 178.90 . 1 821 . 234 LEU CA C 57.38 . 1 822 . 234 LEU CB C 41.43 . 1 823 . 235 MET N N 116.36 . 1 824 . 235 MET H H 7.81 . 1 825 . 235 MET C C 177.03 . 1 826 . 235 MET CA C 58.66 . 1 827 . 235 MET CB C 32.05 . 1 828 . 236 ASP N N 116.48 . 1 829 . 236 ASP H H 7.18 . 1 830 . 236 ASP C C 177.53 . 1 831 . 236 ASP CA C 55.74 . 1 832 . 236 ASP CB C 41.91 . 1 833 . 237 LYS N N 116.61 . 1 834 . 237 LYS H H 7.88 . 1 835 . 237 LYS C C 178.50 . 1 836 . 237 LYS CA C 57.66 . 1 837 . 237 LYS CB C 32.19 . 1 838 . 238 ARG N N 115.56 . 1 839 . 238 ARG H H 7.86 . 1 840 . 238 ARG C C 176.01 . 1 841 . 238 ARG CA C 56.02 . 1 842 . 238 ARG CB C 30.44 . 1 843 . 239 LYS N N 117.24 . 1 844 . 239 LYS H H 7.90 . 1 845 . 239 LYS C C 176.10 . 1 846 . 239 LYS CA C 56.20 . 1 847 . 239 LYS CB C 29.82 . 1 848 . 240 ASP N N 112.71 . 1 849 . 240 ASP H H 7.28 . 1 850 . 240 ASP C C 175.10 . 1 851 . 240 ASP CA C 50.70 . 1 852 . 240 ASP CB C 40.83 . 1 853 . 241 PRO C C 177.15 . 1 854 . 241 PRO CA C 64.40 . 1 855 . 242 SER N N 112.14 . 1 856 . 242 SER H H 8.06 . 1 857 . 242 SER C C 174.63 . 1 858 . 242 SER CA C 59.90 . 1 859 . 242 SER CB C 62.84 . 1 860 . 243 SER N N 114.35 . 1 861 . 243 SER H H 7.54 . 1 862 . 243 SER C C 174.27 . 1 863 . 243 SER CA C 58.73 . 1 864 . 243 SER CB C 64.19 . 1 865 . 244 VAL N N 122.84 . 1 866 . 244 VAL H H 7.18 . 1 867 . 244 VAL C C 173.25 . 1 868 . 244 VAL CA C 62.99 . 1 869 . 244 VAL CB C 31.38 . 1 870 . 245 ASP N N 128.85 . 1 871 . 245 ASP H H 8.31 . 1 872 . 245 ASP C C 175.80 . 1 873 . 245 ASP CA C 51.30 . 1 874 . 245 ASP CB C 40.88 . 1 875 . 246 ILE N N 125.36 . 1 876 . 246 ILE H H 8.41 . 1 877 . 246 ILE C C 176.64 . 1 878 . 246 ILE CA C 65.47 . 1 879 . 246 ILE CB C 37.05 . 1 880 . 247 LYS N N 116.77 . 1 881 . 247 LYS H H 7.78 . 1 882 . 247 LYS C C 177.87 . 1 883 . 247 LYS CA C 59.98 . 1 884 . 247 LYS CB C 30.04 . 1 885 . 248 LYS N N 116.77 . 1 886 . 248 LYS H H 7.12 . 1 887 . 248 LYS C C 180.49 . 1 888 . 248 LYS CA C 58.80 . 1 889 . 248 LYS CB C 31.76 . 1 890 . 249 VAL N N 120.97 . 1 891 . 249 VAL H H 8.07 . 1 892 . 249 VAL C C 177.87 . 1 893 . 249 VAL CA C 65.91 . 1 894 . 249 VAL CB C 30.50 . 1 895 . 250 LEU N N 120.38 . 1 896 . 250 LEU H H 8.32 . 1 897 . 250 LEU C C 179.17 . 1 898 . 250 LEU CA C 57.66 . 1 899 . 250 LEU CB C 39.95 . 1 900 . 251 LEU N N 118.04 . 1 901 . 251 LEU H H 8.08 . 1 902 . 251 LEU C C 179.66 . 1 903 . 251 LEU CA C 57.80 . 1 904 . 251 LEU CB C 40.52 . 1 905 . 252 GLU N N 120.22 . 1 906 . 252 GLU H H 7.82 . 1 907 . 252 GLU C C 179.50 . 1 908 . 252 GLU CA C 59.14 . 1 909 . 252 GLU CB C 28.28 . 1 910 . 253 MET N N 118.71 . 1 911 . 253 MET H H 8.56 . 1 912 . 253 MET C C 179.31 . 1 913 . 253 MET CA C 60.36 . 1 914 . 253 MET CB C 33.39 . 1 915 . 254 ARG N N 116.34 . 1 916 . 254 ARG H H 8.45 . 1 917 . 254 ARG C C 177.22 . 1 918 . 254 ARG CA C 57.66 . 1 919 . 254 ARG CB C 29.74 . 1 920 . 255 LYS N N 118.30 . 1 921 . 255 LYS H H 7.56 . 1 922 . 255 LYS C C 176.21 . 1 923 . 255 LYS CA C 58.63 . 1 924 . 255 LYS CB C 31.07 . 1 925 . 256 PHE N N 111.84 . 1 926 . 256 PHE H H 8.14 . 1 927 . 256 PHE C C 177.47 . 1 928 . 256 PHE CA C 58.92 . 1 929 . 256 PHE CB C 40.73 . 1 930 . 257 ARG N N 119.78 . 1 931 . 257 ARG H H 7.34 . 1 932 . 257 ARG C C 171.49 . 1 933 . 257 ARG CA C 56.49 . 1 934 . 257 ARG CB C 31.72 . 1 935 . 258 MET N N 120.30 . 1 936 . 258 MET H H 8.02 . 1 937 . 258 MET C C 175.98 . 1 938 . 258 MET CA C 54.66 . 1 939 . 258 MET CB C 31.89 . 1 940 . 259 GLY N N 99.71 . 1 941 . 259 GLY H H 8.74 . 1 942 . 259 GLY C C 174.20 . 1 943 . 259 GLY CA C 46.34 . 1 944 . 260 LEU N N 113.82 . 1 945 . 260 LEU H H 6.26 . 1 946 . 260 LEU C C 180.23 . 1 947 . 260 LEU CA C 54.94 . 1 948 . 260 LEU CB C 39.95 . 1 949 . 261 ILE N N 115.54 . 1 950 . 261 ILE H H 8.27 . 1 951 . 261 ILE C C 176.61 . 1 952 . 261 ILE CA C 67.28 . 1 953 . 261 ILE CB C 32.41 . 1 954 . 262 GLN N N 126.10 . 1 955 . 262 GLN H H 8.64 . 1 956 . 262 GLN C C 174.44 . 1 957 . 262 GLN CA C 56.61 . 1 958 . 262 GLN CB C 33.50 . 1 959 . 263 THR N N 106.50 . 1 960 . 263 THR H H 6.83 . 1 961 . 263 THR C C 173.28 . 1 962 . 263 THR CA C 57.48 . 1 963 . 263 THR CB C 71.87 . 1 964 . 264 ALA N N 122.80 . 1 965 . 264 ALA H H 8.52 . 1 966 . 264 ALA C C 178.72 . 1 967 . 264 ALA CA C 53.93 . 1 968 . 264 ALA CB C 16.87 . 1 969 . 265 ASP N N 115.83 . 1 970 . 265 ASP H H 7.68 . 1 971 . 265 ASP C C 179.46 . 1 972 . 265 ASP CA C 56.08 . 1 973 . 265 ASP CB C 39.52 . 1 974 . 266 GLN N N 121.18 . 1 975 . 266 GLN H H 7.88 . 1 976 . 266 GLN C C 178.87 . 1 977 . 266 GLN CA C 58.71 . 1 978 . 266 GLN CB C 27.19 . 1 979 . 267 LEU N N 121.97 . 1 980 . 267 LEU H H 7.33 . 1 981 . 267 LEU C C 177.64 . 1 982 . 267 LEU CA C 57.81 . 1 983 . 267 LEU CB C 40.44 . 1 984 . 268 ARG N N 120.37 . 1 985 . 268 ARG H H 7.90 . 1 986 . 268 ARG C C 177.62 . 1 987 . 268 ARG CA C 58.93 . 1 988 . 268 ARG CB C 28.28 . 1 989 . 269 PHE N N 117.15 . 1 990 . 269 PHE H H 8.21 . 1 991 . 269 PHE C C 175.79 . 1 992 . 269 PHE CA C 61.60 . 1 993 . 269 PHE CB C 38.94 . 1 994 . 270 SER N N 115.64 . 1 995 . 270 SER H H 8.02 . 1 996 . 270 SER C C 175.53 . 1 997 . 270 SER CA C 63.56 . 1 998 . 271 TYR N N 119.36 . 1 999 . 271 TYR H H 7.47 . 1 1000 . 271 TYR C C 177.77 . 1 1001 . 271 TYR CA C 61.68 . 1 1002 . 271 TYR CB C 40.05 . 1 1003 . 272 LEU N N 117.02 . 1 1004 . 272 LEU H H 7.48 . 1 1005 . 272 LEU C C 179.35 . 1 1006 . 272 LEU CA C 57.15 . 1 1007 . 272 LEU CB C 40.89 . 1 1008 . 273 ALA N N 118.69 . 1 1009 . 273 ALA H H 8.47 . 1 1010 . 273 ALA C C 178.98 . 1 1011 . 273 ALA CA C 54.49 . 1 1012 . 273 ALA CB C 16.72 . 1 1013 . 274 VAL N N 118.01 . 1 1014 . 274 VAL H H 7.73 . 1 1015 . 274 VAL C C 177.23 . 1 1016 . 274 VAL CA C 66.17 . 1 1017 . 274 VAL CB C 30.00 . 1 1018 . 275 ILE N N 119.80 . 1 1019 . 275 ILE H H 8.35 . 1 1020 . 275 ILE C C 178.57 . 1 1021 . 275 ILE CA C 65.44 . 1 1022 . 275 ILE CB C 37.50 . 1 1023 . 276 GLU N N 117.42 . 1 1024 . 276 GLU H H 7.90 . 1 1025 . 276 GLU C C 179.68 . 1 1026 . 276 GLU CA C 58.19 . 1 1027 . 276 GLU CB C 27.90 . 1 1028 . 277 GLY N N 108.02 . 1 1029 . 277 GLY H H 8.67 . 1 1030 . 277 GLY C C 175.75 . 1 1031 . 277 GLY CA C 47.10 . 1 1032 . 278 ALA N N 123.93 . 1 1033 . 278 ALA H H 8.49 . 1 1034 . 278 ALA C C 179.22 . 1 1035 . 278 ALA CA C 54.36 . 1 1036 . 278 ALA CB C 17.61 . 1 1037 . 279 LYS N N 115.32 . 1 1038 . 279 LYS H H 7.46 . 1 1039 . 279 LYS C C 179.01 . 1 1040 . 279 LYS CA C 58.84 . 1 1041 . 279 LYS CB C 31.90 . 1 1042 . 280 PHE N N 117.13 . 1 1043 . 280 PHE H H 7.42 . 1 1044 . 280 PHE C C 178.22 . 1 1045 . 280 PHE CA C 59.26 . 1 1046 . 280 PHE CB C 39.19 . 1 1047 . 281 ILE N N 118.61 . 1 1048 . 281 ILE H H 7.69 . 1 1049 . 281 ILE C C 177.62 . 1 1050 . 281 ILE CA C 62.33 . 1 1051 . 281 ILE CB C 36.59 . 1 1052 . 282 MET N N 116.13 . 1 1053 . 282 MET H H 8.03 . 1 1054 . 282 MET C C 177.01 . 1 1055 . 282 MET CA C 54.98 . 1 1056 . 282 MET CB C 30.77 . 1 1057 . 283 GLY N N 106.37 . 1 1058 . 283 GLY H H 7.35 . 1 1059 . 283 GLY C C 173.83 . 1 1060 . 283 GLY CA C 45.10 . 1 1061 . 284 ASP N N 119.95 . 1 1062 . 284 ASP H H 7.80 . 1 1063 . 284 ASP C C 176.41 . 1 1064 . 284 ASP CA C 53.01 . 1 1065 . 284 ASP CB C 40.19 . 1 1066 . 285 SER N N 117.97 . 1 1067 . 285 SER H H 8.17 . 1 1068 . 285 SER C C 175.80 . 1 1069 . 285 SER CA C 59.63 . 1 1070 . 285 SER CB C 62.61 . 1 1071 . 286 SER N N 117.82 . 1 1072 . 286 SER H H 8.32 . 1 1073 . 286 SER C C 176.06 . 1 1074 . 286 SER CA C 59.87 . 1 1075 . 286 SER CB C 62.53 . 1 1076 . 287 VAL N N 120.77 . 1 1077 . 287 VAL H H 7.33 . 1 1078 . 287 VAL C C 176.09 . 1 1079 . 287 VAL CA C 63.34 . 1 1080 . 287 VAL CB C 30.81 . 1 1081 . 288 GLN N N 119.46 . 1 1082 . 288 GLN H H 7.45 . 1 1083 . 288 GLN C C 177.80 . 1 1084 . 288 GLN CA C 57.40 . 1 1085 . 288 GLN CB C 27.20 . 1 1086 . 289 ASP N N 119.34 . 1 1087 . 289 ASP H H 7.70 . 1 1088 . 289 ASP C C 178.18 . 1 1089 . 289 ASP CA C 55.94 . 1 1090 . 289 ASP CB C 39.72 . 1 1091 . 290 GLN N N 119.63 . 1 1092 . 290 GLN H H 7.45 . 1 1093 . 290 GLN C C 177.77 . 1 1094 . 290 GLN CA C 57.35 . 1 1095 . 290 GLN CB C 27.51 . 1 1096 . 291 TRP N N 119.45 . 1 1097 . 291 TRP H H 8.00 . 1 1098 . 291 TRP C C 178.24 . 1 1099 . 291 TRP CA C 57.50 . 1 1100 . 291 TRP CB C 27.85 . 1 1101 . 292 LYS N N 119.91 . 1 1102 . 292 LYS H H 7.60 . 1 1103 . 292 LYS C C 178.26 . 1 1104 . 292 LYS CA C 58.34 . 1 1105 . 292 LYS CB C 31.70 . 1 1106 . 293 GLU N N 120.30 . 1 1107 . 293 GLU H H 7.83 . 1 1108 . 293 GLU C C 178.34 . 1 1109 . 293 GLU CA C 57.86 . 1 1110 . 293 GLU CB C 29.00 . 1 1111 . 294 LEU N N 119.68 . 1 1112 . 294 LEU H H 8.18 . 1 1113 . 294 LEU C C 178.05 . 1 1114 . 294 LEU CA C 55.50 . 1 1115 . 294 LEU CB C 41.34 . 1 1116 . 295 SER N N 113.95 . 1 1117 . 295 SER H H 7.84 . 1 1118 . 295 SER C C 174.05 . 1 1119 . 295 SER CA C 58.74 . 1 1120 . 295 SER CB C 63.12 . 1 1121 . 296 HIS C C 175.35 . 1 1122 . 296 HIS CA C 55.67 . 1 1123 . 296 HIS CB C 27.64 . 1 1124 . 297 GLU N N 120.13 . 1 1125 . 297 GLU H H 8.20 . 1 1126 . 297 GLU C C 175.08 . 1 1127 . 297 GLU CA C 57.05 . 1 1128 . 297 GLU CB C 29.91 . 1 1129 . 298 ASP N N 124.73 . 1 1130 . 298 ASP H H 7.82 . 1 1131 . 298 ASP C C 180.82 . 1 1132 . 298 ASP CA C 55.63 . 1 1133 . 298 ASP CB C 41.81 . 1 stop_ save_