data_17373 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PDZ2 from human SAP97 ; _BMRB_accession_number 17373 _BMRB_flat_file_name bmr17373.str _Entry_type original _Submission_date 2010-12-21 _Accession_date 2010-12-21 _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 Chi Celestine . . 2 Bach Anders . . 3 Engstrom Ake . . 4 Stromgaard Kristian . . 5 Lundstrom Patrik . . 6 Ferguson Neil . . 7 Jemth Per . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 90 "13C chemical shifts" 277 "15N chemical shifts" 90 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-02-01 update BMRB 'update entry citation' 2011-01-18 update BMRB 'update entry citation' 2011-01-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Biophysical Characterization of the Complex between Human Papillomavirus E6 Protein and Synapse-associated Protein 97.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21113079 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chi Celestine N. . 2 Bach Anders . . 3 Engstrom Ake . . 4 Strmgaard Kristian . . 5 Lundstrom Patrik . . 6 Ferguson Neil . . 7 Jemth Per . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3597 _Page_last 3606 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'pdz domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'pdz domain' $SAP97_PDZ2_polypeptide stop_ _System_molecular_weight 10250 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SAP97_PDZ2_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SAP97_PDZ2_polypeptide _Molecular_mass 11678 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; MHHHHHLVPRGSKPVSEKIM EIKLIKGPKGLGFSIAGGVG NQHIPGDNSIYVTKIIEGGA AHKDGKLQIGDKLLAVNNVA LEEVTHEEAVTALKNTSDFV YLKVAKPTS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 299 MET 2 300 HIS 3 301 HIS 4 302 HIS 5 303 HIS 6 304 HIS 7 305 LEU 8 306 VAL 9 307 PRO 10 308 ARG 11 309 GLY 12 310 SER 13 311 LYS 14 312 PRO 15 313 VAL 16 314 SER 17 315 GLU 18 316 LYS 19 317 ILE 20 318 MET 21 319 GLU 22 320 ILE 23 321 LYS 24 322 LEU 25 323 ILE 26 324 LYS 27 325 GLY 28 326 PRO 29 327 LYS 30 328 GLY 31 329 LEU 32 330 GLY 33 331 PHE 34 332 SER 35 333 ILE 36 334 ALA 37 335 GLY 38 336 GLY 39 337 VAL 40 338 GLY 41 339 ASN 42 340 GLN 43 341 HIS 44 342 ILE 45 343 PRO 46 344 GLY 47 345 ASP 48 346 ASN 49 347 SER 50 348 ILE 51 349 TYR 52 350 VAL 53 351 THR 54 352 LYS 55 353 ILE 56 354 ILE 57 355 GLU 58 356 GLY 59 357 GLY 60 358 ALA 61 359 ALA 62 360 HIS 63 361 LYS 64 362 ASP 65 363 GLY 66 364 LYS 67 365 LEU 68 366 GLN 69 367 ILE 70 368 GLY 71 369 ASP 72 370 LYS 73 371 LEU 74 372 LEU 75 373 ALA 76 374 VAL 77 375 ASN 78 376 ASN 79 377 VAL 80 378 ALA 81 379 LEU 82 380 GLU 83 381 GLU 84 382 VAL 85 383 THR 86 384 HIS 87 385 GLU 88 386 GLU 89 387 ALA 90 388 VAL 91 389 THR 92 390 ALA 93 391 LEU 94 392 LYS 95 393 ASN 96 394 THR 97 395 SER 98 396 ASP 99 397 PHE 100 398 VAL 101 399 TYR 102 400 LEU 103 401 LYS 104 402 VAL 105 403 ALA 106 404 LYS 107 405 PRO 108 406 THR 109 407 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-13 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15209 Disks_large_homolog_1 81.65 97 98.88 98.88 1.32e-53 BMRB 17942 hDlg 81.65 97 98.88 98.88 1.32e-53 PDB 2AWU "Synapse Associated Protein 97 Pdz2 Domain Variant C378g" 85.32 105 97.85 98.92 1.45e-55 PDB 2AWX "Synapse Associated Protein 97 Pdz2 Domain Variant C378s" 85.32 105 97.85 100.00 6.60e-56 PDB 2G2L "Crystal Structure Of The Second Pdz Domain Of Sap97 In Complex With A Glur-A C-Terminal Peptide" 85.32 105 97.85 98.92 8.20e-56 PDB 2I0L "X-Ray Crystal Structure Of Sap97 Pdz2 Bound To The C- Terminal Peptide Of Hpv18 E6" 76.15 84 97.59 98.80 1.09e-48 PDB 2M3M "Solution Structure Of A Complex Consisting Of Hdlg/sap-97 Residues 318-406 And Hpv51 Oncoprotein E6 Residues 141-151" 81.65 97 98.88 98.88 1.32e-53 PDB 2OQS "Structure Of The HdlgSAP97 PDZ2 IN COMPLEX WITH HPV-18 Papillomavirus E6 Peptide" 81.65 97 98.88 98.88 1.32e-53 PDB 2X7Z "Crystal Structure Of The Sap97 Pdz2 I342w C378a Mutant Protein Domain" 90.83 99 98.99 98.99 4.82e-61 PDB 4G69 "Structure Of The Human Discs Large 1 Pdz2 - Adenomatous Polyposis Coli Cytoskeletal Polarity Complex" 88.99 100 98.97 98.97 6.58e-60 PDB 4OAJ "Crystal Structure Of The Complex Between Sap97 Pdz2 And 5ht2a Receptor Peptide" 82.57 92 97.78 98.89 3.89e-54 REF XP_012432549 "PREDICTED: disks large homolog 1-like, partial [Taeniopygia guttata]" 72.48 93 97.47 98.73 7.90e-46 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SAP97_PDZ2_polypeptide 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 $SAP97_PDZ2_polypeptide 'recombinant technology' . Escherichia coli . pRSET 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 $SAP97_PDZ2_polypeptide 0.7 mM '[U-100% 15N]' $SAP97_PDZ2_polypeptide 90 % 'natural abundance' $SAP97_PDZ2_polypeptide 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.9 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' HN(CA)CO '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'pdz domain' _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 1 311 13 LYS H H 8.254 0.00 1 2 311 13 LYS C C 174.446 0.00 1 3 311 13 LYS CA C 54.327 0.00 1 4 311 13 LYS CB C 32.761 0.00 1 5 311 13 LYS N N 123.894 0.03 1 6 313 15 VAL C C 176.197 0.00 1 7 313 15 VAL CA C 62.237 0.04 1 8 313 15 VAL CB C 32.977 0.02 1 9 314 16 SER H H 8.337 0.00 1 10 314 16 SER C C 174.026 0.01 1 11 314 16 SER CA C 58.121 0.01 1 12 314 16 SER CB C 63.988 0.03 1 13 314 16 SER N N 119.267 0.01 1 14 315 17 GLU H H 8.259 0.00 1 15 315 17 GLU C C 175.447 0.00 1 16 315 17 GLU CA C 55.989 0.01 1 17 315 17 GLU CB C 31.754 0.02 1 18 315 17 GLU N N 122.218 0.04 1 19 316 18 LYS H H 8.688 0.00 1 20 316 18 LYS C C 174.913 0.00 1 21 316 18 LYS CA C 55.628 0.03 1 22 316 18 LYS CB C 33.826 0.01 1 23 316 18 LYS N N 123.379 0.02 1 24 317 19 ILE H H 8.240 0.00 1 25 317 19 ILE C C 176.230 0.01 1 26 317 19 ILE CA C 59.567 0.02 1 27 317 19 ILE CB C 38.663 0.00 1 28 317 19 ILE N N 124.796 0.01 1 29 318 20 MET H H 9.209 0.00 1 30 318 20 MET C C 173.433 0.00 1 31 318 20 MET CA C 54.381 0.02 1 32 318 20 MET CB C 36.883 0.01 1 33 318 20 MET N N 125.850 0.03 1 34 319 21 GLU H H 8.536 0.00 1 35 319 21 GLU C C 175.655 0.01 1 36 319 21 GLU CA C 55.050 0.03 1 37 319 21 GLU CB C 31.940 0.03 1 38 319 21 GLU N N 123.067 0.01 1 39 320 22 ILE H H 9.060 0.00 1 40 320 22 ILE C C 173.648 0.01 1 41 320 22 ILE CA C 60.558 0.06 1 42 320 22 ILE CB C 42.190 0.03 1 43 320 22 ILE N N 125.824 0.02 1 44 321 23 LYS H H 8.516 0.00 1 45 321 23 LYS C C 175.194 0.00 1 46 321 23 LYS CA C 54.774 0.02 1 47 321 23 LYS CB C 33.836 0.02 1 48 321 23 LYS N N 128.521 0.02 1 49 322 24 LEU H H 8.996 0.00 1 50 322 24 LEU C C 174.914 0.01 1 51 322 24 LEU CA C 52.905 0.02 1 52 322 24 LEU CB C 45.992 0.06 1 53 322 24 LEU N N 125.109 0.02 1 54 323 25 ILE H H 8.268 0.00 1 55 323 25 ILE C C 175.971 0.01 1 56 323 25 ILE CA C 59.716 0.05 1 57 323 25 ILE CB C 38.583 0.02 1 58 323 25 ILE N N 122.047 0.01 1 59 324 26 LYS H H 8.694 0.00 1 60 324 26 LYS C C 176.059 0.01 1 61 324 26 LYS CA C 58.276 0.02 1 62 324 26 LYS CB C 33.525 0.01 1 63 324 26 LYS N N 127.328 0.02 1 64 325 27 GLY H H 7.528 0.00 1 65 325 27 GLY C C 173.687 0.00 1 66 325 27 GLY CA C 44.364 0.00 1 67 325 27 GLY N N 112.105 0.03 1 68 326 28 PRO C C 176.825 0.00 1 69 326 28 PRO CA C 63.116 0.00 1 70 326 28 PRO CB C 32.083 0.00 1 71 327 29 LYS H H 8.211 0.00 1 72 327 29 LYS C C 176.853 0.01 1 73 327 29 LYS CA C 55.459 0.00 1 74 327 29 LYS CB C 32.031 0.01 1 75 327 29 LYS N N 120.241 0.01 1 76 328 30 GLY H H 7.983 0.00 1 77 328 30 GLY C C 175.360 0.00 1 78 328 30 GLY CA C 44.959 0.00 1 79 328 30 GLY N N 106.988 0.01 1 80 329 31 LEU C C 178.174 0.01 1 81 329 31 LEU CA C 56.873 0.02 1 82 329 31 LEU CB C 42.620 0.00 1 83 330 32 GLY H H 8.635 0.00 1 84 330 32 GLY C C 175.858 0.01 1 85 330 32 GLY CA C 47.238 0.01 1 86 330 32 GLY N N 104.290 0.02 1 87 331 33 PHE H H 7.461 0.00 1 88 331 33 PHE C C 172.639 0.00 1 89 331 33 PHE CA C 56.822 0.00 1 90 331 33 PHE CB C 41.239 0.03 1 91 331 33 PHE N N 115.457 0.02 1 92 332 34 SER H H 8.651 0.00 1 93 332 34 SER C C 173.653 0.01 1 94 332 34 SER CA C 56.859 0.02 1 95 332 34 SER CB C 65.240 0.02 1 96 332 34 SER N N 116.238 0.02 1 97 333 35 ILE H H 8.511 0.00 1 98 333 35 ILE C C 175.452 0.01 1 99 333 35 ILE CA C 58.689 0.01 1 100 333 35 ILE CB C 43.371 0.01 1 101 333 35 ILE N N 114.132 0.03 1 102 334 36 ALA H H 9.164 0.00 1 103 334 36 ALA C C 175.740 0.00 1 104 334 36 ALA CA C 51.223 0.01 1 105 334 36 ALA CB C 24.595 0.04 1 106 334 36 ALA N N 122.951 0.01 1 107 335 37 GLY H H 8.473 0.00 1 108 335 37 GLY C C 174.111 0.01 1 109 335 37 GLY CA C 44.505 0.07 1 110 335 37 GLY N N 106.701 0.02 1 111 336 38 GLY H H 6.490 0.00 1 112 336 38 GLY C C 174.698 0.00 1 113 336 38 GLY CA C 43.491 0.01 1 114 336 38 GLY N N 105.977 0.01 1 115 337 39 VAL H H 8.569 0.00 1 116 337 39 VAL C C 178.943 0.00 1 117 337 39 VAL CA C 64.494 0.04 1 118 337 39 VAL CB C 31.962 0.01 1 119 337 39 VAL N N 119.958 0.03 1 120 338 40 GLY H H 9.277 0.00 1 121 338 40 GLY C C 173.774 0.01 1 122 338 40 GLY CA C 45.370 0.03 1 123 338 40 GLY N N 117.851 0.03 1 124 339 41 ASN H H 8.339 0.00 1 125 339 41 ASN C C 174.335 0.01 1 126 339 41 ASN CA C 52.683 0.03 1 127 339 41 ASN CB C 39.871 0.04 1 128 339 41 ASN N N 122.650 0.04 1 129 340 42 GLN H H 8.297 0.00 1 130 340 42 GLN C C 178.167 0.00 1 131 340 42 GLN CA C 58.150 0.01 1 132 340 42 GLN CB C 28.225 0.02 1 133 340 42 GLN N N 117.711 0.05 1 134 341 43 HIS H H 10.095 0.00 1 135 341 43 HIS C C 174.900 0.00 1 136 341 43 HIS CA C 57.712 0.05 1 137 341 43 HIS CB C 32.145 0.03 1 138 341 43 HIS N N 125.312 0.01 1 139 342 44 ILE H H 6.992 0.00 1 140 342 44 ILE C C 173.401 0.00 1 141 342 44 ILE CA C 56.841 0.00 1 142 342 44 ILE CB C 41.213 0.00 1 143 342 44 ILE N N 117.891 0.03 1 144 343 45 PRO C C 177.937 0.00 1 145 343 45 PRO CA C 64.302 0.01 1 146 343 45 PRO CB C 31.642 0.01 1 147 344 46 GLY H H 8.310 0.00 1 148 344 46 GLY C C 172.878 0.01 1 149 344 46 GLY CA C 45.605 0.05 1 150 344 46 GLY N N 112.001 0.01 1 151 345 47 ASP H H 8.158 0.00 1 152 345 47 ASP C C 176.370 0.01 1 153 345 47 ASP CA C 52.554 0.01 1 154 345 47 ASP CB C 43.793 0.03 1 155 345 47 ASP N N 121.999 0.02 1 156 346 48 ASN H H 9.292 0.00 1 157 346 48 ASN C C 176.317 0.19 1 158 346 48 ASN CA C 53.806 0.05 1 159 346 48 ASN CB C 39.171 0.02 1 160 346 48 ASN N N 124.822 0.01 1 161 347 49 SER H H 8.804 0.00 1 162 347 49 SER C C 171.689 0.01 1 163 347 49 SER CA C 60.649 0.05 1 164 347 49 SER CB C 63.166 0.06 1 165 347 49 SER N N 116.269 0.01 1 166 348 50 ILE H H 8.915 0.00 1 167 348 50 ILE C C 175.000 0.01 1 168 348 50 ILE CA C 57.686 0.05 1 169 348 50 ILE CB C 35.402 0.03 1 170 348 50 ILE N N 123.246 0.02 1 171 349 51 TYR H H 8.686 0.00 1 172 349 51 TYR C C 175.848 0.00 1 173 349 51 TYR CA C 56.766 0.01 1 174 349 51 TYR CB C 43.442 0.01 1 175 349 51 TYR N N 123.815 0.04 1 176 350 52 VAL H H 8.740 0.00 1 177 350 52 VAL C C 177.762 0.00 1 178 350 52 VAL CA C 62.973 0.03 1 179 350 52 VAL CB C 32.121 0.03 1 180 350 52 VAL N N 120.272 0.01 1 181 351 53 THR H H 8.755 0.00 1 182 351 53 THR C C 174.727 0.01 1 183 351 53 THR CA C 61.902 0.09 1 184 351 53 THR CB C 69.736 0.06 1 185 351 53 THR N N 118.023 0.01 1 186 352 54 LYS H H 7.192 0.00 1 187 352 54 LYS C C 174.408 0.01 1 188 352 54 LYS CA C 56.889 0.01 1 189 352 54 LYS CB C 36.509 0.01 1 190 352 54 LYS N N 120.751 0.02 1 191 353 55 ILE H H 8.508 0.00 1 192 353 55 ILE C C 175.112 0.01 1 193 353 55 ILE CA C 60.314 0.01 1 194 353 55 ILE CB C 39.496 0.03 1 195 353 55 ILE N N 125.070 0.02 1 196 354 56 ILE H H 7.997 0.00 1 197 354 56 ILE C C 176.571 0.01 1 198 354 56 ILE CA C 60.289 0.01 1 199 354 56 ILE CB C 38.113 0.04 1 200 354 56 ILE N N 126.965 0.02 1 201 355 57 GLU H H 9.097 0.00 1 202 355 57 GLU C C 177.290 0.01 1 203 355 57 GLU CA C 58.314 0.04 1 204 355 57 GLU CB C 28.919 0.04 1 205 355 57 GLU N N 132.067 0.03 1 206 356 58 GLY H H 9.289 0.00 1 207 356 58 GLY C C 174.868 0.02 1 208 356 58 GLY CA C 45.393 0.04 1 209 356 58 GLY N N 115.308 0.01 1 210 357 59 GLY H H 7.683 0.00 1 211 357 59 GLY C C 173.536 0.01 1 212 357 59 GLY CA C 44.674 0.02 1 213 357 59 GLY N N 105.709 0.01 1 214 358 60 ALA H H 8.272 0.00 1 215 358 60 ALA C C 180.793 0.01 1 216 358 60 ALA CA C 55.667 0.02 1 217 358 60 ALA CB C 19.409 0.02 1 218 358 60 ALA N N 119.369 0.04 1 219 359 61 ALA H H 8.165 0.00 1 220 359 61 ALA C C 180.908 0.01 1 221 359 61 ALA CA C 54.796 0.01 1 222 359 61 ALA CB C 18.616 0.00 1 223 359 61 ALA N N 118.630 0.01 1 224 360 62 HIS H H 9.462 0.00 1 225 360 62 HIS C C 177.004 0.01 1 226 360 62 HIS CA C 59.625 0.02 1 227 360 62 HIS CB C 32.651 0.00 1 228 360 62 HIS N N 124.441 0.05 1 229 361 63 LYS H H 8.308 0.00 1 230 361 63 LYS C C 178.425 0.00 1 231 361 63 LYS CA C 59.050 0.01 1 232 361 63 LYS CB C 32.336 0.07 1 233 361 63 LYS N N 118.005 0.05 1 234 362 64 ASP H H 7.561 0.00 1 235 362 64 ASP C C 177.748 0.01 1 236 362 64 ASP CA C 56.918 0.00 1 237 362 64 ASP CB C 44.045 0.03 1 238 362 64 ASP N N 117.164 0.04 1 239 363 65 GLY H H 7.468 0.00 1 240 363 65 GLY C C 174.589 0.01 1 241 363 65 GLY CA C 46.427 0.01 1 242 363 65 GLY N N 103.485 0.01 1 243 364 66 LYS H H 7.861 0.00 1 244 364 66 LYS C C 177.653 0.00 1 245 364 66 LYS CA C 58.604 0.02 1 246 364 66 LYS CB C 33.981 0.02 1 247 364 66 LYS N N 119.907 0.04 1 248 365 67 LEU H H 9.297 0.00 1 249 365 67 LEU C C 174.974 0.00 1 250 365 67 LEU CA C 55.131 0.01 1 251 365 67 LEU CB C 43.789 0.02 1 252 365 67 LEU N N 124.279 0.04 1 253 366 68 GLN H H 8.756 0.00 1 254 366 68 GLN C C 175.163 0.00 1 255 366 68 GLN CA C 53.688 0.03 1 256 366 68 GLN CB C 33.500 0.02 1 257 366 68 GLN N N 123.454 0.04 1 258 367 69 ILE H H 8.386 0.00 1 259 367 69 ILE C C 177.764 0.01 1 260 367 69 ILE CA C 63.598 0.03 1 261 367 69 ILE CB C 37.416 0.03 1 262 367 69 ILE N N 120.265 0.02 1 263 368 70 GLY H H 9.106 0.00 1 264 368 70 GLY C C 174.093 0.01 1 265 368 70 GLY CA C 44.675 0.01 1 266 368 70 GLY N N 116.524 0.04 1 267 369 71 ASP H H 7.872 0.00 1 268 369 71 ASP C C 175.074 0.01 1 269 369 71 ASP CA C 55.773 0.04 1 270 369 71 ASP CB C 40.415 0.01 1 271 369 71 ASP N N 121.979 0.02 1 272 370 72 LYS H H 8.295 0.00 1 273 370 72 LYS C C 176.181 0.00 1 274 370 72 LYS CA C 54.534 0.03 1 275 370 72 LYS CB C 34.933 0.06 1 276 370 72 LYS N N 121.554 0.02 1 277 371 73 LEU H H 8.646 0.00 1 278 371 73 LEU C C 174.592 0.01 1 279 371 73 LEU CA C 54.154 0.06 1 280 371 73 LEU CB C 42.951 0.00 1 281 371 73 LEU N N 126.463 0.02 1 282 372 74 LEU H H 9.016 0.00 1 283 372 74 LEU C C 178.660 0.01 1 284 372 74 LEU CA C 55.743 0.12 1 285 372 74 LEU CB C 43.051 0.04 1 286 372 74 LEU N N 123.743 0.01 1 287 373 75 ALA H H 7.896 0.00 1 288 373 75 ALA C C 175.206 0.01 1 289 373 75 ALA CA C 52.549 0.02 1 290 373 75 ALA CB C 22.382 0.01 1 291 373 75 ALA N N 119.840 0.01 1 292 374 76 VAL H H 8.377 0.00 1 293 374 76 VAL C C 174.719 0.01 1 294 374 76 VAL CA C 59.989 0.04 1 295 374 76 VAL CB C 34.058 0.09 1 296 374 76 VAL N N 118.471 0.01 1 297 375 77 ASN H H 9.989 0.00 1 298 375 77 ASN C C 174.497 0.00 1 299 375 77 ASN CA C 55.141 0.00 1 300 375 77 ASN CB C 36.468 0.00 1 301 375 77 ASN N N 127.729 0.03 1 302 376 78 ASN C C 174.303 0.01 1 303 376 78 ASN CA C 54.294 0.01 1 304 376 78 ASN CB C 38.094 0.01 1 305 377 79 VAL H H 8.542 0.00 1 306 377 79 VAL C C 175.000 0.01 1 307 377 79 VAL CA C 62.817 0.04 1 308 377 79 VAL CB C 31.984 0.01 1 309 377 79 VAL N N 123.884 0.05 1 310 378 80 ALA H H 8.456 0.00 1 311 378 80 ALA C C 177.981 0.00 1 312 378 80 ALA CA C 52.538 0.01 1 313 378 80 ALA CB C 19.646 0.03 1 314 378 80 ALA N N 130.108 0.01 1 315 379 81 LEU H H 8.164 0.00 1 316 379 81 LEU C C 175.800 0.01 1 317 379 81 LEU CA C 52.781 0.14 1 318 379 81 LEU CB C 40.246 0.02 1 319 379 81 LEU N N 122.122 0.04 1 320 380 82 GLU H H 7.087 0.00 1 321 380 82 GLU C C 174.884 0.01 1 322 380 82 GLU CA C 56.498 0.02 1 323 380 82 GLU CB C 31.101 0.01 1 324 380 82 GLU N N 121.066 0.02 1 325 381 83 GLU H H 8.783 0.00 1 326 381 83 GLU C C 175.024 0.01 1 327 381 83 GLU CA C 56.467 0.03 1 328 381 83 GLU CB C 27.693 0.02 1 329 381 83 GLU N N 123.568 0.01 1 330 382 84 VAL H H 8.546 0.00 1 331 382 84 VAL C C 176.579 0.00 1 332 382 84 VAL CA C 58.640 0.02 1 333 382 84 VAL CB C 34.362 0.01 1 334 382 84 VAL N N 113.264 0.01 1 335 383 85 THR H H 8.616 0.00 1 336 383 85 THR C C 175.350 0.00 1 337 383 85 THR CA C 61.223 0.03 1 338 383 85 THR CB C 71.234 0.03 1 339 383 85 THR N N 110.763 0.02 1 340 384 86 HIS H H 9.508 0.00 1 341 384 86 HIS C C 177.155 0.00 1 342 384 86 HIS CA C 61.322 0.07 1 343 384 86 HIS CB C 29.649 0.01 1 344 384 86 HIS N N 121.560 0.03 1 345 385 87 GLU H H 8.717 0.00 1 346 385 87 GLU C C 179.559 0.01 1 347 385 87 GLU CA C 59.957 0.02 1 348 385 87 GLU CB C 29.236 0.10 1 349 385 87 GLU N N 115.915 0.01 1 350 386 88 GLU H H 7.830 0.00 1 351 386 88 GLU C C 179.492 0.00 1 352 386 88 GLU CA C 59.535 0.03 1 353 386 88 GLU CB C 30.058 0.01 1 354 386 88 GLU N N 120.805 0.02 1 355 387 89 ALA H H 7.871 0.01 1 356 387 89 ALA C C 178.174 0.01 1 357 387 89 ALA CA C 55.245 0.11 1 358 387 89 ALA CB C 18.902 0.04 1 359 387 89 ALA N N 123.285 0.03 1 360 388 90 VAL H H 8.291 0.01 1 361 388 90 VAL C C 179.458 0.01 1 362 388 90 VAL CA C 66.861 0.02 1 363 388 90 VAL CB C 31.724 0.01 1 364 388 90 VAL N N 117.045 0.05 1 365 389 91 THR H H 8.292 0.00 1 366 389 91 THR C C 175.578 0.00 1 367 389 91 THR CA C 67.056 0.13 1 368 389 91 THR CB C 68.586 0.04 1 369 389 91 THR N N 117.303 0.09 1 370 390 92 ALA H H 7.861 0.00 1 371 390 92 ALA C C 179.889 0.00 1 372 390 92 ALA CA C 55.093 0.02 1 373 390 92 ALA CB C 17.597 0.03 1 374 390 92 ALA N N 123.479 0.05 1 375 391 93 LEU H H 7.554 0.00 1 376 391 93 LEU C C 179.063 0.00 1 377 391 93 LEU CA C 57.305 0.01 1 378 391 93 LEU CB C 42.090 0.01 1 379 391 93 LEU N N 115.251 0.01 1 380 392 94 LYS H H 8.185 0.00 1 381 392 94 LYS C C 178.190 0.01 1 382 392 94 LYS CA C 58.578 0.01 1 383 392 94 LYS CB C 32.908 0.01 1 384 392 94 LYS N N 121.342 0.01 1 385 393 95 ASN H H 7.764 0.00 1 386 393 95 ASN C C 175.095 0.01 1 387 393 95 ASN CA C 52.874 0.04 1 388 393 95 ASN CB C 37.500 0.01 1 389 393 95 ASN N N 119.433 0.02 1 390 394 96 THR H H 7.518 0.00 1 391 394 96 THR C C 174.866 0.00 1 392 394 96 THR CA C 60.380 0.05 1 393 394 96 THR CB C 72.040 0.05 1 394 394 96 THR N N 109.895 0.02 1 395 395 97 SER H H 8.551 0.00 1 396 395 97 SER C C 173.519 0.00 1 397 395 97 SER CA C 56.969 0.00 1 398 395 97 SER CB C 63.560 0.04 1 399 395 97 SER N N 117.283 0.03 1 400 396 98 ASP H H 8.308 0.00 1 401 396 98 ASP C C 175.090 0.01 1 402 396 98 ASP CA C 57.256 0.04 1 403 396 98 ASP CB C 40.811 0.01 1 404 396 98 ASP N N 117.681 0.04 1 405 397 99 PHE H H 7.841 0.00 1 406 397 99 PHE C C 174.858 0.00 1 407 397 99 PHE CA C 56.166 0.02 1 408 397 99 PHE CB C 40.613 0.02 1 409 397 99 PHE N N 116.934 0.01 1 410 398 100 VAL H H 9.014 0.00 1 411 398 100 VAL C C 173.285 0.01 1 412 398 100 VAL CA C 61.297 0.02 1 413 398 100 VAL CB C 34.803 0.03 1 414 398 100 VAL N N 123.703 0.02 1 415 399 101 TYR H H 8.803 0.00 1 416 399 101 TYR C C 175.631 0.01 1 417 399 101 TYR CA C 56.820 0.01 1 418 399 101 TYR CB C 39.124 0.01 1 419 399 101 TYR N N 125.993 0.04 1 420 400 102 LEU H H 9.440 0.00 1 421 400 102 LEU C C 175.294 0.01 1 422 400 102 LEU CA C 53.130 0.02 1 423 400 102 LEU CB C 44.346 0.01 1 424 400 102 LEU N N 125.627 0.03 1 425 401 103 LYS H H 8.164 0.00 1 426 401 103 LYS C C 175.475 0.01 1 427 401 103 LYS CA C 55.649 0.03 1 428 401 103 LYS CB C 34.623 0.02 1 429 401 103 LYS N N 124.028 0.04 1 430 402 104 VAL H H 9.096 0.00 1 431 402 104 VAL C C 173.348 0.01 1 432 402 104 VAL CA C 59.266 0.08 1 433 402 104 VAL CB C 35.909 0.03 1 434 402 104 VAL N N 123.019 0.02 1 435 403 105 ALA H H 9.086 0.00 1 436 403 105 ALA C C 176.894 0.00 1 437 403 105 ALA CA C 50.013 0.01 1 438 403 105 ALA CB C 21.522 0.04 1 439 403 105 ALA N N 124.472 0.04 1 440 404 106 LYS H H 8.859 0.00 1 441 404 106 LYS C C 174.711 0.00 1 442 404 106 LYS CA C 52.708 0.00 1 443 404 106 LYS CB C 33.018 0.00 1 444 404 106 LYS N N 124.807 0.02 1 445 405 107 PRO C C 177.339 0.00 1 446 405 107 PRO CA C 63.143 0.05 1 447 405 107 PRO CB C 32.306 0.04 1 448 406 108 THR H H 8.252 0.00 1 449 406 108 THR C C 173.817 0.01 1 450 406 108 THR CA C 61.670 0.03 1 451 406 108 THR CB C 69.943 0.03 1 452 406 108 THR N N 114.002 0.01 1 453 407 109 SER H H 7.899 0.00 1 454 407 109 SER C C 178.552 0.00 1 455 407 109 SER CA C 59.932 0.00 1 456 407 109 SER CB C 64.955 0.00 1 457 407 109 SER N N 122.858 0.01 1 stop_ save_