data_4168 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Receptor Binding Domain of Human Alpha-2-macroglobulin ; _BMRB_accession_number 4168 _BMRB_flat_file_name bmr4168.str _Entry_type original _Submission_date 1998-07-24 _Accession_date 1998-07-24 _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 Huang Wen . . 2 Dolmer Klavs . . 3 Liao Xiubei . . 4 Gettins Peter G.W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 271 "13C chemical shifts" 138 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-27 original author . stop_ _Original_release_date 2000-03-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Localization of Basic Residues Required for Receptor Binding to the Single Alpha-helix of the Receptor Binding Domain of Human Alpha-2-macroglobulin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99081553 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Huang Wen . . 2 Dolmer Klavs . . 3 Liao Xiubei . . 4 Gettins Peter G.W. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 7 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2602 _Page_last 2612 _Year 1998 _Details . loop_ _Keyword alpha-2-macroglobulin receptor 'receptor binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_RBD _Saveframe_category molecular_system _Mol_system_name 'Alpha-2-macroglobulin receptor binding domain' _Abbreviation_common RBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RBD $RBD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'receptor binding domain' stop_ _Database_query_date . _Details 'This is the first NMR study of any domain from human alpha-2-macroglobulin' save_ ######################## # Monomeric polymers # ######################## save_RBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Alpha-2-macroglobulin receptor binding domain' _Abbreviation_common RBD _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 138 _Mol_residue_sequence ; EEFPFALGVQTLPQTCDEPK AHTSFQISLSVSYTGSRSAS NMAIVDVKMVSGFIPLKPTV KMLERSNHVSRTEVSSNHVL IYLDKVSNQTLSLFFTVLQD VPVRDLKPAIVKVYDYYETD EFAIAEYNAPCSKDLGNA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1314 GLU 2 1315 GLU 3 1316 PHE 4 1317 PRO 5 1318 PHE 6 1319 ALA 7 1320 LEU 8 1321 GLY 9 1322 VAL 10 1323 GLN 11 1324 THR 12 1325 LEU 13 1326 PRO 14 1327 GLN 15 1328 THR 16 1329 CYS 17 1330 ASP 18 1331 GLU 19 1332 PRO 20 1333 LYS 21 1334 ALA 22 1335 HIS 23 1336 THR 24 1337 SER 25 1338 PHE 26 1339 GLN 27 1340 ILE 28 1341 SER 29 1342 LEU 30 1343 SER 31 1344 VAL 32 1345 SER 33 1346 TYR 34 1347 THR 35 1348 GLY 36 1349 SER 37 1350 ARG 38 1351 SER 39 1352 ALA 40 1353 SER 41 1354 ASN 42 1355 MET 43 1356 ALA 44 1357 ILE 45 1358 VAL 46 1359 ASP 47 1360 VAL 48 1361 LYS 49 1362 MET 50 1363 VAL 51 1364 SER 52 1365 GLY 53 1366 PHE 54 1367 ILE 55 1368 PRO 56 1369 LEU 57 1370 LYS 58 1371 PRO 59 1372 THR 60 1373 VAL 61 1374 LYS 62 1375 MET 63 1376 LEU 64 1377 GLU 65 1378 ARG 66 1379 SER 67 1380 ASN 68 1381 HIS 69 1382 VAL 70 1383 SER 71 1384 ARG 72 1385 THR 73 1386 GLU 74 1387 VAL 75 1388 SER 76 1389 SER 77 1390 ASN 78 1391 HIS 79 1392 VAL 80 1393 LEU 81 1394 ILE 82 1395 TYR 83 1396 LEU 84 1397 ASP 85 1398 LYS 86 1399 VAL 87 1400 SER 88 1401 ASN 89 1402 GLN 90 1403 THR 91 1404 LEU 92 1405 SER 93 1406 LEU 94 1407 PHE 95 1408 PHE 96 1409 THR 97 1410 VAL 98 1411 LEU 99 1412 GLN 100 1413 ASP 101 1414 VAL 102 1415 PRO 103 1416 VAL 104 1417 ARG 105 1418 ASP 106 1419 LEU 107 1420 LYS 108 1421 PRO 109 1422 ALA 110 1423 ILE 111 1424 VAL 112 1425 LYS 113 1426 VAL 114 1427 TYR 115 1428 ASP 116 1429 TYR 117 1430 TYR 118 1431 GLU 119 1432 THR 120 1433 ASP 121 1434 GLU 122 1435 PHE 123 1436 ALA 124 1437 ILE 125 1438 ALA 126 1439 GLU 127 1440 TYR 128 1441 ASN 129 1442 ALA 130 1443 PRO 131 1444 CYS 132 1445 SER 133 1446 LYS 134 1447 ASP 135 1448 LEU 136 1449 GLY 137 1450 ASN 138 1451 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-20 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1BV8 "Receptor Domain From Alpha-2-Macroglobulin" 99.28 138 100.00 100.00 4.01e-95 PDB 4ACQ "Alpha-2 Macroglobulin" 100.00 1451 100.00 100.00 2.80e-86 DBJ BAD92851 "alpha 2 macroglobulin variant [Homo sapiens]" 100.00 1482 100.00 100.00 4.37e-86 DBJ BAG10847 "alpha-2-macroglobulin precursor [synthetic construct]" 100.00 1474 100.00 100.00 3.51e-86 EMBL CAH18188 "hypothetical protein [Homo sapiens]" 100.00 1474 100.00 100.00 3.31e-86 EMBL CAH93278 "hypothetical protein [Pongo abelii]" 100.00 1474 99.28 100.00 1.03e-85 GB AAA51551 "alpha-2-macroglobulin precursor [Homo sapiens]" 100.00 1474 100.00 100.00 3.31e-86 GB AAA51552 "alpha-2-macroglobulin, partial [Homo sapiens]" 100.00 643 100.00 100.00 1.81e-90 GB AAH40071 "Alpha-2-macroglobulin [Homo sapiens]" 100.00 1474 100.00 100.00 3.31e-86 GB AAQ13498 "FWP007 [Homo sapiens]" 100.00 267 100.00 100.00 2.51e-95 GB AAT02228 "alpha 2 macroglobulin [Homo sapiens]" 100.00 1499 100.00 100.00 4.51e-86 PRF 1009174A "macroglobulin alpha2" 100.00 1450 100.00 100.00 2.79e-86 REF NP_000005 "alpha-2-macroglobulin precursor [Homo sapiens]" 100.00 1474 100.00 100.00 3.51e-86 REF NP_001126929 "alpha-2-macroglobulin precursor [Pongo abelii]" 100.00 1474 99.28 100.00 1.03e-85 REF XP_001139819 "PREDICTED: alpha-2-macroglobulin isoform X2 [Pan troglodytes]" 100.00 1474 100.00 100.00 3.44e-86 REF XP_003265499 "PREDICTED: alpha-2-macroglobulin isoform X1 [Nomascus leucogenys]" 100.00 1474 99.28 100.00 1.10e-85 REF XP_003804581 "PREDICTED: alpha-2-macroglobulin isoform X3 [Pan paniscus]" 100.00 1474 99.28 99.28 9.51e-86 SP P01023 "RecName: Full=Alpha-2-macroglobulin; Short=Alpha-2-M; AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing pro" 100.00 1474 100.00 100.00 3.73e-86 SP Q5R4N8 "RecName: Full=Alpha-2-macroglobulin; Short=Alpha-2-M; Flags: Precursor" 100.00 1474 99.28 100.00 1.03e-85 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RBD 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 $RBD 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $RBD . mM 0.9 1.2 '[U-95% 13C; U-90%15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $sample_one save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_one save_ save_NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label $sample_one save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_one save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_one save_ save_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.4 0.02 M pH 5.1 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 . C 13 . . . . . . . . . H 1 . . . . . . . . . N 15 . . . . . . . . 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_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name RBD _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 GLU H H 8.28 0.02 1 2 . 1 GLU HA H 4.17 0.02 1 3 . 1 GLU CA C 56.0 0.24 1 4 . 1 GLU N N 121.3 0.05 1 5 . 2 GLU H H 8.37 0.02 1 6 . 2 GLU HA H 4.20 0.02 1 7 . 2 GLU CA C 56.0 0.24 1 8 . 2 GLU N N 121.5 0.05 1 9 . 3 PHE H H 8.28 0.02 1 10 . 3 PHE HA H 4.44 0.02 1 11 . 3 PHE CA C 56.4 0.24 1 12 . 3 PHE N N 121.3 0.05 1 13 . 4 PRO HA H 4.71 0.02 1 14 . 4 PRO CA C 62.9 0.24 1 15 . 5 PHE H H 8.46 0.02 1 16 . 5 PHE HA H 5.05 0.02 1 17 . 5 PHE CA C 56.6 0.24 1 18 . 5 PHE N N 120.4 0.05 1 19 . 6 ALA H H 8.73 0.02 1 20 . 6 ALA HA H 4.49 0.02 1 21 . 6 ALA CA C 50.9 0.24 1 22 . 6 ALA N N 124.2 0.05 1 23 . 7 LEU H H 8.36 0.02 1 24 . 7 LEU HA H 5.25 0.02 1 25 . 7 LEU CA C 53.0 0.24 1 26 . 7 LEU N N 125.0 0.05 1 27 . 8 GLY H H 9.17 0.02 1 28 . 8 GLY HA2 H 4.57 0.02 1 29 . 8 GLY HA3 H 3.59 0.02 1 30 . 8 GLY CA C 44.1 0.24 1 31 . 8 GLY N N 115.1 0.05 1 32 . 9 VAL H H 8.57 0.02 1 33 . 9 VAL HA H 4.92 0.02 1 34 . 9 VAL CA C 60.2 0.24 1 35 . 9 VAL N N 120.7 0.05 1 36 . 10 GLN H H 8.84 0.02 1 37 . 10 GLN HA H 4.79 0.02 1 38 . 10 GLN CA C 53.6 0.24 1 39 . 10 GLN N N 125.1 0.05 1 40 . 11 THR H H 8.62 0.02 1 41 . 11 THR HA H 5.34 0.02 1 42 . 11 THR CA C 59.7 0.24 1 43 . 11 THR N N 110.4 0.05 1 44 . 12 LEU H H 8.79 0.02 1 45 . 12 LEU HA H 4.64 0.02 1 46 . 12 LEU CA C 51.9 0.24 1 47 . 12 LEU N N 120.5 0.05 1 48 . 13 PRO HA H 4.89 0.02 1 49 . 13 PRO CA C 63.3 0.24 1 50 . 14 GLN H H 8.99 0.02 1 51 . 14 GLN HA H 4.05 0.02 1 52 . 14 GLN CA C 57.7 0.24 1 53 . 14 GLN N N 118.1 0.05 1 54 . 15 THR H H 7.39 0.02 1 55 . 15 THR HA H 4.52 0.02 1 56 . 15 THR CA C 59.0 0.24 1 57 . 15 THR N N 107.0 0.05 1 58 . 16 CYS H H 8.51 0.02 1 59 . 16 CYS HA H 4.69 0.02 1 60 . 16 CYS CA C 56.1 0.24 1 61 . 16 CYS N N 120.6 0.05 1 62 . 17 ASP H H 8.18 0.02 1 63 . 17 ASP HA H 4.46 0.02 1 64 . 17 ASP CA C 54.9 0.24 1 65 . 17 ASP N N 122.2 0.05 1 66 . 18 GLU H H 7.61 0.02 1 67 . 18 GLU HA H 4.82 0.02 1 68 . 18 GLU CA C 53.6 0.24 1 69 . 18 GLU N N 117.1 0.05 1 70 . 19 PRO HA H 4.31 0.02 1 71 . 19 PRO CA C 65.9 0.24 1 72 . 20 LYS H H 8.80 0.02 1 73 . 20 LYS HA H 4.25 0.02 1 74 . 20 LYS CA C 58.6 0.24 1 75 . 20 LYS N N 117.4 0.05 1 76 . 21 ALA H H 7.91 0.02 1 77 . 21 ALA HA H 4.58 0.02 1 78 . 21 ALA CA C 53.9 0.24 1 79 . 21 ALA N N 120.3 0.05 1 80 . 22 HIS H H 7.95 0.02 1 81 . 22 HIS HA H 4.17 0.02 1 82 . 22 HIS CA C 58.3 0.24 1 83 . 22 HIS N N 110.6 0.05 1 84 . 23 THR H H 7.86 0.02 1 85 . 23 THR HA H 4.56 0.02 1 86 . 23 THR CA C 61.6 0.24 1 87 . 23 THR N N 104.4 0.05 1 88 . 24 SER H H 8.39 0.02 1 89 . 24 SER HA H 5.22 0.02 1 90 . 24 SER CA C 58.2 0.24 1 91 . 24 SER N N 116.1 0.05 1 92 . 25 PHE H H 8.06 0.02 1 93 . 25 PHE HA H 4.98 0.02 1 94 . 25 PHE CA C 56.6 0.24 1 95 . 25 PHE N N 115.4 0.05 1 96 . 26 GLN H H 9.01 0.02 1 97 . 26 GLN HA H 5.13 0.02 1 98 . 26 GLN CA C 53.9 0.24 1 99 . 26 GLN N N 115.1 0.05 1 100 . 27 ILE H H 8.57 0.02 1 101 . 27 ILE HA H 3.84 0.02 1 102 . 27 ILE CA C 60.9 0.24 1 103 . 27 ILE N N 123.6 0.05 1 104 . 28 SER H H 8.60 0.02 1 105 . 28 SER HA H 4.93 0.02 1 106 . 28 SER CA C 55.2 0.24 1 107 . 28 SER N N 120.0 0.05 1 108 . 29 LEU H H 9.41 0.02 1 109 . 29 LEU HA H 5.15 0.02 1 110 . 29 LEU CA C 53.1 0.24 1 111 . 29 LEU N N 126.6 0.05 1 112 . 30 SER H H 9.01 0.02 1 113 . 30 SER HA H 5.41 0.02 1 114 . 30 SER CA C 56.4 0.24 1 115 . 30 SER N N 118.3 0.05 1 116 . 31 VAL H H 8.94 0.02 1 117 . 31 VAL HA H 5.31 0.02 1 118 . 31 VAL CA C 60.0 0.24 1 119 . 31 VAL N N 122.9 0.05 1 120 . 32 SER H H 8.58 0.02 1 121 . 32 SER HA H 4.62 0.02 1 122 . 32 SER CA C 57.5 0.24 1 123 . 32 SER N N 117.4 0.05 1 124 . 33 TYR H H 8.54 0.02 1 125 . 33 TYR HA H 4.70 0.02 1 126 . 33 TYR CA C 57.2 0.24 1 127 . 33 TYR N N 123.1 0.05 1 128 . 34 THR H H 7.90 0.02 1 129 . 34 THR HA H 4.12 0.02 1 130 . 34 THR CA C 60.2 0.24 1 131 . 34 THR N N 117.80 0.05 1 132 . 35 GLY H H 5.16 0.02 1 133 . 35 GLY HA2 H 3.32 0.02 1 134 . 35 GLY HA3 H 4.04 0.02 1 135 . 35 GLY CA C 44.8 0.24 1 136 . 35 GLY N N 107.6 0.05 1 137 . 36 SER H H 8.71 0.02 1 138 . 36 SER HA H 4.23 0.02 1 139 . 36 SER CA C 59.5 0.24 1 140 . 36 SER N N 112.9 0.05 1 141 . 37 ARG H H 7.86 0.02 1 142 . 37 ARG HA H 4.45 0.02 1 143 . 37 ARG CA C 56.1 0.24 1 144 . 37 ARG N N 120.5 0.05 1 145 . 38 SER H H 8.54 0.02 1 146 . 38 SER HA H 4.11 0.02 1 147 . 38 SER CA C 60.9 0.24 1 148 . 38 SER N N 114.3 0.05 1 149 . 39 ALA H H 7.51 0.02 1 150 . 39 ALA HA H 4.18 0.02 1 151 . 39 ALA CA C 51.3 0.24 1 152 . 39 ALA N N 119.6 0.05 1 153 . 40 SER H H 8.37 0.02 1 154 . 40 SER HA H 3.99 0.02 1 155 . 40 SER CA C 57.6 0.24 1 156 . 40 SER N N 114.3 0.05 1 157 . 41 ASN H H 8.38 0.02 1 158 . 41 ASN HA H 4.71 0.02 1 159 . 41 ASN CA C 54.5 0.24 1 160 . 41 ASN N N 121.8 0.05 1 161 . 42 MET H H 8.05 0.02 1 162 . 42 MET HA H 4.88 0.02 1 163 . 42 MET CA C 56.6 0.24 1 164 . 42 MET N N 118.8 0.05 1 165 . 43 ALA H H 8.63 0.02 1 166 . 43 ALA HA H 5.01 0.02 1 167 . 43 ALA CA C 50.1 0.24 1 168 . 43 ALA N N 126.9 0.05 1 169 . 44 ILE H H 8.41 0.02 1 170 . 44 ILE HA H 4.26 0.02 1 171 . 44 ILE CA C 56.2 0.24 1 172 . 44 ILE N N 120.0 0.05 1 173 . 45 VAL H H 8.87 0.02 1 174 . 45 VAL HA H 4.47 0.02 1 175 . 45 VAL CA C 60.2 0.24 1 176 . 45 VAL N N 124.1 0.05 1 177 . 46 ASP H H 9.49 0.02 1 178 . 46 ASP HA H 5.24 0.02 1 179 . 46 ASP CA C 51.9 0.24 1 180 . 46 ASP N N 126.8 0.05 1 181 . 47 VAL H H 9.63 0.02 1 182 . 47 VAL HA H 4.28 0.02 1 183 . 47 VAL CA C 61.1 0.24 1 184 . 47 VAL N N 125.7 0.05 1 185 . 48 LYS H H 8.32 0.02 1 186 . 48 LYS HA H 4.56 0.02 1 187 . 48 LYS CA C 52.7 0.24 1 188 . 48 LYS N N 124.4 0.05 1 189 . 49 MET H H 8.37 0.02 1 190 . 49 MET HA H 4.41 0.02 1 191 . 49 MET CA C 54.2 0.24 1 192 . 49 MET N N 122.2 0.05 1 193 . 50 VAL H H 8.43 0.02 1 194 . 50 VAL HA H 3.84 0.02 1 195 . 50 VAL CA C 62.7 0.24 1 196 . 50 VAL N N 125.0 0.05 1 197 . 51 SER H H 8.62 0.02 1 198 . 51 SER HA H 4.21 0.02 1 199 . 51 SER CA C 60.5 0.24 1 200 . 51 SER N N 120.7 0.05 1 201 . 52 GLY H H 8.48 0.02 1 202 . 52 GLY HA2 H 3.81 0.02 1 203 . 52 GLY HA3 H 4.41 0.02 1 204 . 52 GLY CA C 45.7 0.24 1 205 . 52 GLY N N 111.1 0.05 1 206 . 53 PHE H H 8.62 0.02 1 207 . 53 PHE HA H 5.15 0.02 1 208 . 53 PHE CA C 57.5 0.24 1 209 . 53 PHE N N 119.2 0.05 1 210 . 54 ILE H H 9.24 0.02 1 211 . 54 ILE HA H 4.99 0.02 1 212 . 54 ILE CA C 57.4 0.24 1 213 . 54 ILE N N 112.9 0.05 1 214 . 55 PRO HA H 4.75 0.02 1 215 . 55 PRO CA C 62.1 0.24 1 216 . 56 LEU H H 8.71 0.02 1 217 . 56 LEU HA H 4.14 0.02 1 218 . 56 LEU CA C 53.7 0.24 1 219 . 56 LEU N N 122.2 0.05 1 220 . 57 LYS H H 8.45 0.02 1 221 . 57 LYS HA H 4.98 0.02 1 222 . 57 LYS CA C 55.0 0.24 1 223 . 57 LYS N N 121.5 0.05 1 224 . 58 PRO HA H 4.41 0.02 1 225 . 58 PRO CA C 66.2 0.24 1 226 . 59 THR H H 7.66 0.02 1 227 . 59 THR HA H 4.41 0.02 1 228 . 59 THR CA C 64.1 0.24 1 229 . 59 THR N N 104.8 0.05 1 230 . 60 VAL H H 7.31 0.02 1 231 . 60 VAL HA H 3.50 0.02 1 232 . 60 VAL CA C 65.1 0.24 1 233 . 60 VAL N N 123.4 0.05 1 234 . 61 LYS H H 7.81 0.02 1 235 . 61 LYS HA H 3.91 0.02 1 236 . 61 LYS CA C 57.6 0.24 1 237 . 61 LYS N N 118.0 0.05 1 238 . 62 MET H H 7.57 0.02 1 239 . 62 MET HA H 4.13 0.02 1 240 . 62 MET CA C 57.8 0.24 1 241 . 62 MET N N 115.8 0.05 1 242 . 63 LEU H H 7.78 0.02 1 243 . 63 LEU HA H 4.09 0.02 1 244 . 63 LEU CA C 57.1 0.24 1 245 . 63 LEU N N 118.8 0.05 1 246 . 64 GLU H H 7.55 0.02 1 247 . 64 GLU HA H 3.76 0.02 1 248 . 64 GLU CA C 57.7 0.24 1 249 . 64 GLU N N 113.0 0.05 1 250 . 65 ARG H H 7.46 0.02 1 251 . 65 ARG HA H 4.13 0.02 1 252 . 65 ARG CA C 57.4 0.24 1 253 . 65 ARG N N 115.9 0.05 1 254 . 66 SER H H 7.67 0.02 1 255 . 66 SER HA H 4.42 0.02 1 256 . 66 SER CA C 57.9 0.24 1 257 . 66 SER N N 112.9 0.05 1 258 . 67 ASN H H 9.09 0.02 1 259 . 67 ASN HA H 4.46 0.02 1 260 . 67 ASN CA C 54.9 0.24 1 261 . 67 ASN N N 125.7 0.05 1 262 . 68 HIS H H 8.48 0.02 1 263 . 68 HIS HA H 4.66 0.02 1 264 . 68 HIS CA C 56.4 0.24 1 265 . 68 HIS N N 113.2 0.05 1 266 . 69 VAL H H 7.25 0.02 1 267 . 69 VAL HA H 4.64 0.02 1 268 . 69 VAL CA C 60.9 0.24 1 269 . 69 VAL N N 119.1 0.05 1 270 . 70 SER H H 8.89 0.02 1 271 . 70 SER HA H 4.37 0.02 1 272 . 70 SER CA C 59.0 0.24 1 273 . 70 SER N N 121.8 0.05 1 274 . 71 ARG H H 7.51 0.02 1 275 . 71 ARG HA H 4.33 0.02 1 276 . 71 ARG CA C 55.6 0.24 1 277 . 71 ARG N N 116.9 0.05 1 278 . 72 THR H H 7.94 0.02 1 279 . 72 THR HA H 5.31 0.02 1 280 . 72 THR CA C 59.5 0.24 1 281 . 72 THR N N 112.5 0.05 1 282 . 73 GLU H H 9.17 0.02 1 283 . 73 GLU HA H 4.66 0.02 1 284 . 73 GLU CA C 55.3 0.24 1 285 . 73 GLU N N 118.9 0.05 1 286 . 74 VAL H H 8.81 0.02 1 287 . 74 VAL HA H 4.59 0.02 1 288 . 74 VAL CA C 61.6 0.24 1 289 . 74 VAL N N 122.8 0.05 1 290 . 75 SER H H 8.64 0.02 1 291 . 75 SER HA H 4.79 0.02 1 292 . 75 SER CA C 56.3 0.24 1 293 . 75 SER N N 122.3 0.05 1 294 . 76 SER H H 8.92 0.02 1 295 . 76 SER HA H 4.66 0.02 1 296 . 76 SER CA C 60.4 0.24 1 297 . 76 SER N N 116.1 0.05 1 298 . 77 ASN H H 8.59 0.02 1 299 . 77 ASN HA H 4.73 0.02 1 300 . 77 ASN CA C 53.2 0.24 1 301 . 77 ASN N N 114.7 0.05 1 302 . 78 HIS H H 8.09 0.02 1 303 . 78 HIS HA H 5.46 0.02 1 304 . 78 HIS CA C 54.8 0.24 1 305 . 78 HIS N N 115.7 0.05 1 306 . 79 VAL H H 8.79 0.02 1 307 . 79 VAL HA H 4.41 0.02 1 308 . 79 VAL CA C 61.5 0.24 1 309 . 79 VAL N N 120.2 0.05 1 310 . 80 LEU H H 9.03 0.02 1 311 . 80 LEU HA H 5.39 0.02 1 312 . 80 LEU CA C 53.2 0.24 1 313 . 80 LEU N N 126.0 0.05 1 314 . 81 ILE H H 9.15 0.02 1 315 . 81 ILE HA H 4.19 0.02 1 316 . 81 ILE CA C 60.6 0.24 1 317 . 81 ILE N N 121.9 0.05 1 318 . 82 TYR H H 8.66 0.02 1 319 . 82 TYR HA H 4.63 0.02 1 320 . 82 TYR CA C 57.4 0.24 1 321 . 82 TYR N N 127.1 0.05 1 322 . 83 LEU H H 9.29 0.02 1 323 . 83 LEU HA H 5.43 0.02 1 324 . 83 LEU CA C 52.4 0.24 1 325 . 83 LEU N N 123.0 0.05 1 326 . 84 ASP H H 8.74 0.02 1 327 . 84 ASP HA H 4.75 0.02 1 328 . 84 ASP CA C 53.7 0.24 1 329 . 84 ASP N N 120.8 0.05 1 330 . 85 LYS H H 8.17 0.02 1 331 . 85 LYS HA H 3.88 0.02 1 332 . 85 LYS CA C 56.9 0.24 1 333 . 85 LYS N N 119.3 0.05 1 334 . 86 VAL H H 8.38 0.02 1 335 . 86 VAL HA H 3.89 0.02 1 336 . 86 VAL CA C 62.6 0.24 1 337 . 86 VAL N N 122.6 0.05 1 338 . 87 SER H H 9.31 0.02 1 339 . 87 SER HA H 5.02 0.02 1 340 . 87 SER CA C 56.5 0.24 1 341 . 87 SER N N 124.1 0.05 1 342 . 88 ASN H H 8.72 0.02 1 343 . 88 ASN HA H 4.71 0.02 1 344 . 88 ASN CA C 54.6 0.24 1 345 . 88 ASN N N 117.6 0.05 1 346 . 89 GLN H H 7.84 0.02 1 347 . 89 GLN HA H 4.29 0.02 1 348 . 89 GLN CA C 55.2 0.24 1 349 . 89 GLN N N 119.8 0.05 1 350 . 90 THR H H 8.37 0.02 1 351 . 90 THR HA H 4.03 0.02 1 352 . 90 THR CA C 64.4 0.24 1 353 . 90 THR N N 120.6 0.05 1 354 . 91 LEU H H 9.32 0.02 1 355 . 91 LEU HA H 4.56 0.02 1 356 . 91 LEU CA C 53.7 0.24 1 357 . 91 LEU N N 130.8 0.05 1 358 . 92 SER H H 8.46 0.02 1 359 . 92 SER HA H 5.41 0.02 1 360 . 92 SER CA C 56.7 0.24 1 361 . 92 SER N N 118.8 0.05 1 362 . 93 LEU H H 8.66 0.02 1 363 . 93 LEU HA H 4.74 0.02 1 364 . 93 LEU CA C 53.3 0.24 1 365 . 93 LEU N N 124.2 0.05 1 366 . 94 PHE H H 7.77 0.02 1 367 . 94 PHE HA H 5.93 0.02 1 368 . 94 PHE CA C 55.5 0.24 1 369 . 94 PHE N N 117.7 0.05 1 370 . 95 PHE H H 8.17 0.02 1 371 . 95 PHE HA H 4.87 0.02 1 372 . 95 PHE CA C 57.5 0.24 1 373 . 95 PHE N N 112.7 0.05 1 374 . 96 THR H H 8.75 0.02 1 375 . 96 THR HA H 4.73 0.02 1 376 . 96 THR CA C 63.1 0.24 1 377 . 96 THR N N 114.5 0.05 1 378 . 97 VAL H H 8.66 0.02 1 379 . 97 VAL HA H 5.02 0.02 1 380 . 97 VAL CA C 58.8 0.24 1 381 . 97 VAL N N 118.1 0.05 1 382 . 98 LEU H H 9.43 0.02 1 383 . 98 LEU HA H 5.20 0.02 1 384 . 98 LEU CA C 53.2 0.24 1 385 . 98 LEU N N 119.8 0.05 1 386 . 99 GLN H H 8.78 0.02 1 387 . 99 GLN HA H 5.64 0.02 1 388 . 99 GLN CA C 56.5 0.24 1 389 . 99 GLN N N 122.5 0.05 1 390 . 100 ASP H H 9.20 0.02 1 391 . 100 ASP HA H 4.69 0.02 1 392 . 100 ASP CA C 55.0 0.24 1 393 . 100 ASP N N 130.9 0.05 1 394 . 101 VAL H H 7.83 0.02 1 395 . 101 VAL HA H 4.46 0.02 1 396 . 101 VAL CA C 58.3 0.24 1 397 . 101 VAL N N 115.8 0.05 1 398 . 102 PRO HA H 4.17 0.02 1 399 . 102 PRO CA C 62.6 0.24 1 400 . 103 VAL H H 7.71 0.02 1 401 . 103 VAL HA H 4.09 0.02 1 402 . 103 VAL CA C 61.5 0.24 1 403 . 103 VAL N N 125.1 0.05 1 404 . 104 ARG H H 8.45 0.02 1 405 . 104 ARG HA H 4.19 0.02 1 406 . 104 ARG CA C 57.3 0.24 1 407 . 104 ARG N N 124.6 0.05 1 408 . 105 ASP H H 8.09 0.02 1 409 . 105 ASP HA H 4.62 0.02 1 410 . 105 ASP CA C 53.2 0.24 1 411 . 105 ASP N N 118.7 0.05 1 412 . 106 LEU H H 8.22 0.02 1 413 . 106 LEU HA H 4.26 0.02 1 414 . 106 LEU CA C 54.8 0.24 1 415 . 106 LEU N N 122.5 0.05 1 416 . 107 LYS H H 8.18 0.02 1 417 . 107 LYS HA H 4.59 0.02 1 418 . 107 LYS CA C 53.6 0.24 1 419 . 107 LYS N N 124.0 0.05 1 420 . 108 PRO HA H 4.26 0.02 1 421 . 108 PRO CA C 62.7 0.24 1 422 . 109 ALA H H 8.36 0.02 1 423 . 109 ALA HA H 4.60 0.02 1 424 . 109 ALA CA C 49.7 0.24 1 425 . 109 ALA N N 123.8 0.05 1 426 . 110 ILE H H 7.14 0.02 1 427 . 110 ILE HA H 4.77 0.02 1 428 . 110 ILE CA C 59.8 0.24 1 429 . 110 ILE N N 115.8 0.05 1 430 . 111 VAL H H 9.11 0.02 1 431 . 111 VAL HA H 4.93 0.02 1 432 . 111 VAL CA C 60.4 0.24 1 433 . 111 VAL N N 125.6 0.05 1 434 . 112 LYS H H 8.71 0.02 1 435 . 112 LYS HA H 5.45 0.02 1 436 . 112 LYS CA C 53.8 0.24 1 437 . 112 LYS N N 125.7 0.05 1 438 . 113 VAL H H 8.79 0.02 1 439 . 113 VAL HA H 5.67 0.02 1 440 . 113 VAL CA C 57.5 0.24 1 441 . 113 VAL N N 122.5 0.05 1 442 . 114 TYR H H 8.37 0.02 1 443 . 114 TYR HA H 4.21 0.02 1 444 . 114 TYR CA C 56.9 0.24 1 445 . 114 TYR N N 121.4 0.05 1 446 . 115 ASP H H 8.70 0.02 1 447 . 115 ASP HA H 3.86 0.02 1 448 . 115 ASP CA C 52.9 0.24 1 449 . 115 ASP N N 121.5 0.05 1 450 . 116 TYR H H 8.19 0.02 1 451 . 116 TYR HA H 4.67 0.02 1 452 . 116 TYR CA C 61.1 0.24 1 453 . 116 TYR N N 122.1 0.05 1 454 . 117 TYR H H 8.32 0.02 1 455 . 117 TYR HA H 4.57 0.02 1 456 . 117 TYR CA C 52.7 0.24 1 457 . 117 TYR N N 127.3 0.05 1 458 . 118 GLU H H 8.39 0.02 1 459 . 118 GLU HA H 4.76 0.02 1 460 . 118 GLU CA C 56.0 0.24 1 461 . 118 GLU N N 120.6 0.05 1 462 . 119 THR H H 8.17 0.02 1 463 . 119 THR HA H 4.03 0.02 1 464 . 119 THR CA C 61.2 0.24 1 465 . 119 THR N N 113.2 0.05 1 466 . 120 ASP H H 8.07 0.02 1 467 . 120 ASP HA H 4.41 0.02 1 468 . 120 ASP CA C 55.5 0.24 1 469 . 120 ASP N N 127.2 0.05 1 470 . 121 GLU H H 8.31 0.02 1 471 . 121 GLU HA H 3.76 0.02 1 472 . 121 GLU CA C 56.0 0.24 1 473 . 121 GLU N N 112.6 0.05 1 474 . 122 PHE H H 7.84 0.02 1 475 . 122 PHE HA H 4.82 0.02 1 476 . 122 PHE CA C 59.0 0.24 1 477 . 122 PHE N N 111.9 0.05 1 478 . 123 ALA H H 9.06 0.02 1 479 . 123 ALA HA H 4.29 0.02 1 480 . 123 ALA CA C 50.8 0.24 1 481 . 123 ALA N N 123.4 0.05 1 482 . 124 ILE H H 8.54 0.02 1 483 . 124 ILE HA H 5.38 0.02 1 484 . 124 ILE CA C 59.3 0.24 1 485 . 124 ILE N N 120.3 0.05 1 486 . 125 ALA H H 9.27 0.02 1 487 . 125 ALA HA H 4.69 0.02 1 488 . 125 ALA CA C 51.4 0.24 1 489 . 125 ALA N N 127.2 0.05 1 490 . 126 GLU H H 8.45 0.02 1 491 . 126 GLU HA H 5.47 0.02 1 492 . 126 GLU CA C 54.4 0.24 1 493 . 126 GLU N N 117.4 0.05 1 494 . 127 TYR H H 8.75 0.02 1 495 . 127 TYR HA H 4.75 0.02 1 496 . 127 TYR CA C 55.9 0.24 1 497 . 127 TYR N N 117.5 0.05 1 498 . 128 ASN H H 8.27 0.02 1 499 . 128 ASN HA H 4.62 0.02 1 500 . 128 ASN CA C 50.1 0.24 1 501 . 128 ASN N N 115.5 0.05 1 502 . 129 ALA H H 8.67 0.02 1 503 . 129 ALA HA H 3.30 0.02 1 504 . 129 ALA CA C 50.0 0.24 1 505 . 129 ALA N N 123.6 0.05 1 506 . 130 PRO HA H 3.97 0.02 1 507 . 130 PRO CA C 64.3 0.24 1 508 . 131 CYS H H 8.14 0.02 1 509 . 131 CYS HA H 4.70 0.02 1 510 . 131 CYS CA C 54.3 0.24 1 511 . 131 CYS N N 111.5 0.05 1 512 . 132 SER H H 7.53 0.02 1 513 . 132 SER HA H 4.16 0.02 1 514 . 132 SER CA C 60.0 0.24 1 515 . 132 SER N N 115.3 0.05 1 516 . 133 LYS H H 8.15 0.02 1 517 . 133 LYS CA C 55.9 0.24 1 518 . 133 LYS N N 121.4 0.05 1 519 . 134 ASP H H 8.15 0.02 1 520 . 134 ASP HA H 4.57 0.02 1 521 . 134 ASP CA C 54.2 0.24 1 522 . 134 ASP N N 121.4 0.05 1 523 . 135 LEU H H 8.29 0.02 1 524 . 135 LEU HA H 4.27 0.02 1 525 . 135 LEU CA C 55.3 0.24 1 526 . 135 LEU N N 122.5 0.05 1 527 . 136 GLY H H 8.42 0.02 1 528 . 136 GLY HA2 H 3.88 0.02 1 529 . 136 GLY HA3 H 3.88 0.02 1 530 . 136 GLY CA C 45.4 0.24 1 531 . 136 GLY N N 108.3 0.05 1 532 . 137 ASN H H 8.20 0.02 1 533 . 137 ASN HA H 4.70 0.02 1 534 . 137 ASN CA C 53.0 0.24 1 535 . 137 ASN N N 118.4 0.05 1 536 . 138 ALA H H 7.90 0.02 1 537 . 138 ALA HA H 4.05 0.02 1 538 . 138 ALA CA C 53.8 0.24 1 539 . 138 ALA N N 129.1 0.05 1 stop_ save_