data_16471 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for IQGAP1 (401-533) ; _BMRB_accession_number 16471 _BMRB_flat_file_name bmr16471.str _Entry_type original _Submission_date 2009-08-27 _Accession_date 2009-08-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'IQGAP1 residues 401-533' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Matthew J. . 2 Ikura Mitsu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 115 "13C chemical shifts" 237 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-05 update BMRB 'completed entry citation' 2010-01-28 original BMRB 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20075861 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Matthew J. . 2 Hardy 'W. Rod' . . 3 Li Guang-Yao . . 4 Goudreault Marilyn . . 5 Hersch Steven . . 6 Metalnikov Pavel . . 7 Starostine Andrei . . 8 Pawson Tony . . 9 Ikura Mitsuhiko . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 29 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 884 _Page_last 896 _Year 2010 _Details . loop_ _Keyword ErbB2 IQGAP1 'PTB Domain' PTP-PEST ShcA stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'IQGAP1 (401-533)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ShcA PTB Domain Ligand' $IQGAP1_(401-533) stop_ _System_molecular_weight 14888 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Isotopically labeled IQGAP1 (401-533)' save_ ######################## # Monomeric polymers # ######################## save_IQGAP1_(401-533) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IQGAP1_(401-533) _Molecular_mass 14888 _Mol_thiol_state unknown loop_ _Biological_function 'cytoskeletal regulator' 'multidomain scaffold protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; KGIAEKTVLELMNPEAQLPQ VYPFAADLYQKELATLQQQS PEHSLTHPELTVAVEMLSSV ALINRALESGDMTTVWKQLS SSVTGLTNIEEENCQRYLDE LMKLKAQAHAENNAFITWND IQACVDHVNLVVH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 401 LYS 2 402 GLY 3 403 ILE 4 404 ALA 5 405 GLU 6 406 LYS 7 407 THR 8 408 VAL 9 409 LEU 10 410 GLU 11 411 LEU 12 412 MET 13 413 ASN 14 414 PRO 15 415 GLU 16 416 ALA 17 417 GLN 18 418 LEU 19 419 PRO 20 420 GLN 21 421 VAL 22 422 TYR 23 423 PRO 24 424 PHE 25 425 ALA 26 426 ALA 27 427 ASP 28 428 LEU 29 429 TYR 30 430 GLN 31 431 LYS 32 432 GLU 33 433 LEU 34 434 ALA 35 435 THR 36 436 LEU 37 437 GLN 38 438 GLN 39 439 GLN 40 440 SER 41 441 PRO 42 442 GLU 43 443 HIS 44 444 SER 45 445 LEU 46 446 THR 47 447 HIS 48 448 PRO 49 449 GLU 50 450 LEU 51 451 THR 52 452 VAL 53 453 ALA 54 454 VAL 55 455 GLU 56 456 MET 57 457 LEU 58 458 SER 59 459 SER 60 460 VAL 61 461 ALA 62 462 LEU 63 463 ILE 64 464 ASN 65 465 ARG 66 466 ALA 67 467 LEU 68 468 GLU 69 469 SER 70 470 GLY 71 471 ASP 72 472 MET 73 473 THR 74 474 THR 75 475 VAL 76 476 TRP 77 477 LYS 78 478 GLN 79 479 LEU 80 480 SER 81 481 SER 82 482 SER 83 483 VAL 84 484 THR 85 485 GLY 86 486 LEU 87 487 THR 88 488 ASN 89 489 ILE 90 490 GLU 91 491 GLU 92 492 GLU 93 493 ASN 94 494 CYS 95 495 GLN 96 496 ARG 97 497 TYR 98 498 LEU 99 499 ASP 100 500 GLU 101 501 LEU 102 502 MET 103 503 LYS 104 504 LEU 105 505 LYS 106 506 ALA 107 507 GLN 108 508 ALA 109 509 HIS 110 510 ALA 111 511 GLU 112 512 ASN 113 513 ASN 114 514 ALA 115 515 PHE 116 516 ILE 117 517 THR 118 518 TRP 119 519 ASN 120 520 ASP 121 521 ILE 122 522 GLN 123 523 ALA 124 524 CYS 125 525 VAL 126 526 ASP 127 527 HIS 128 528 VAL 129 529 ASN 130 530 LEU 131 531 VAL 132 532 VAL 133 533 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 DBJ BAC97854 "mKIAA0051 protein [Mus musculus]" 100.00 1681 100.00 100.00 2.90e-83 DBJ BAE37174 "unnamed protein product [Mus musculus]" 100.00 539 100.00 100.00 2.25e-87 DBJ BAE37805 "unnamed protein product [Mus musculus]" 100.00 586 100.00 100.00 5.00e-87 GB AAF60344 "IQ motif containing GTPase activating protein 1 [Mus musculus]" 100.00 1657 100.00 100.00 2.88e-83 GB AAH22105 "Iqgap1 protein, partial [Mus musculus]" 100.00 943 100.00 100.00 2.05e-84 GB AAH37685 "Iqgap1 protein, partial [Mus musculus]" 100.00 939 100.00 100.00 2.22e-84 GB AAH46385 "IQ motif containing GTPase activating protein 1 [Mus musculus]" 100.00 1657 100.00 100.00 2.93e-83 GB EDL06977 "IQ motif containing GTPase activating protein 1, isoform CRA_c [Mus musculus]" 100.00 1657 100.00 100.00 2.88e-83 REF NP_001101959 "ras GTPase-activating-like protein IQGAP1 [Rattus norvegicus]" 100.00 1657 97.74 98.50 1.32e-81 REF NP_057930 "ras GTPase-activating-like protein IQGAP1 [Mus musculus]" 100.00 1657 100.00 100.00 2.88e-83 REF XP_003513458 "PREDICTED: ras GTPase-activating-like protein IQGAP1 isoform X1 [Cricetulus griseus]" 100.00 1657 97.74 98.50 1.64e-81 REF XP_005077870 "PREDICTED: ras GTPase-activating-like protein IQGAP1 [Mesocricetus auratus]" 100.00 1657 96.99 98.50 3.34e-81 REF XP_005357708 "PREDICTED: ras GTPase-activating-like protein IQGAP1 [Microtus ochrogaster]" 100.00 1659 96.99 98.50 4.12e-81 SP Q9JKF1 "RecName: Full=Ras GTPase-activating-like protein IQGAP1" 100.00 1657 100.00 100.00 2.88e-83 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $IQGAP1_(401-533) Mouse 10090 Eukaryota Metazoa Mus musculus IQGAP1 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 $IQGAP1_(401-533) 'recombinant technology' . Escherichia coli . pGEX4T2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'IQGAP1 (401-533)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IQGAP1_(401-533) 200 uM '[U-13C; U-15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' NaCl 100 mM '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_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 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' 150 . mM pH 7.5 . pH pressure 1 . atm temperature 303 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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 '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' 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 'ShcA PTB Domain Ligand' _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 1 401 1 LYS H H 8.434 . 1 2 401 1 LYS CA C 56.69 . 1 3 401 1 LYS CB C 33.24 . 1 4 401 1 LYS N N 122 . 1 5 402 2 GLY H H 8.48 . 1 6 402 2 GLY CA C 45.32 . 1 7 402 2 GLY N N 109.89 . 1 8 403 3 ILE H H 7.931 . 1 9 403 3 ILE CA C 61.18 . 1 10 403 3 ILE CB C 38.65 . 1 11 403 3 ILE N N 119.959 . 1 12 404 4 ALA H H 8.397 . 1 13 404 4 ALA CA C 52.69 . 1 14 404 4 ALA CB C 19.13 . 1 15 404 4 ALA N N 127.509 . 1 16 405 5 GLU H H 8.323 . 1 17 405 5 GLU CA C 57.04 . 1 18 405 5 GLU CB C 30.22 . 1 19 405 5 GLU N N 120.331 . 1 20 406 6 LYS H H 8.359 . 1 21 406 6 LYS CA C 59.69 . 1 22 406 6 LYS CB C 33.17 . 1 23 406 6 LYS N N 122.65 . 1 24 407 7 THR H H 8.226 . 1 25 407 7 THR CA C 62.52 . 1 26 407 7 THR CB C 69.96 . 1 27 407 7 THR N N 115.833 . 1 28 408 8 VAL H H 8.153 . 1 29 408 8 VAL CA C 63.29 . 1 30 408 8 VAL CB C 32.54 . 1 31 408 8 VAL N N 121.897 . 1 32 409 9 LEU H H 8.117 . 1 33 409 9 LEU CA C 55.78 . 1 34 409 9 LEU CB C 42.16 . 1 35 409 9 LEU N N 124.103 . 1 36 410 10 GLU H H 8.191 . 1 37 410 10 GLU CA C 57.18 . 1 38 410 10 GLU CB C 30.22 . 1 39 410 10 GLU N N 120.866 . 1 40 411 11 LEU H H 8.035 . 1 41 411 11 LEU CA C 55.36 . 1 42 411 11 LEU CB C 42.37 . 1 43 411 11 LEU N N 121.734 . 1 44 412 12 MET H H 8.098 . 1 45 412 12 MET CA C 55.43 . 1 46 412 12 MET CB C 32.96 . 1 47 412 12 MET N N 119.932 . 1 48 414 14 PRO CA C 64.06 . 1 49 414 14 PRO CB C 32.05 . 1 50 415 15 GLU H H 8.415 . 1 51 415 15 GLU CA C 56.97 . 1 52 415 15 GLU CB C 29.66 . 1 53 415 15 GLU N N 119.096 . 1 54 416 16 ALA H H 7.972 . 1 55 416 16 ALA CA C 52.34 . 1 56 416 16 ALA CB C 19.34 . 1 57 416 16 ALA N N 123.689 . 1 58 417 17 GLN H H 8.129 . 1 59 417 17 GLN CA C 55.36 . 1 60 417 17 GLN CB C 29.38 . 1 61 417 17 GLN N N 118.763 . 1 62 418 18 LEU H H 8.223 . 1 63 418 18 LEU CA C 53.32 . 1 64 418 18 LEU CB C 41.59 . 1 65 418 18 LEU N N 124.665 . 1 66 419 19 PRO CA C 65.68 . 1 67 419 19 PRO CB C 31.91 . 1 68 420 20 GLN H H 8.539 . 1 69 420 20 GLN CA C 59.08 . 1 70 420 20 GLN CB C 29.17 . 1 71 420 20 GLN N N 121.128 . 1 72 421 21 VAL H H 8 . 1 73 421 21 VAL CA C 62.17 . 1 74 421 21 VAL CB C 33.03 . 1 75 421 21 VAL N N 120.912 . 1 76 422 22 TYR H H 8.291 . 1 77 422 22 TYR CA C 55.57 . 1 78 422 22 TYR CB C 38.37 . 1 79 422 22 TYR N N 124.721 . 1 80 423 23 PRO CA C 62.87 . 1 81 423 23 PRO CB C 33.66 . 1 82 424 24 PHE H H 8.267 . 1 83 424 24 PHE CA C 57.67 . 1 84 424 24 PHE CB C 39.07 . 1 85 424 24 PHE N N 122.19 . 1 86 425 25 ALA H H 8.07 . 1 87 425 25 ALA CA C 52.69 . 1 88 425 25 ALA CB C 19.27 . 1 89 425 25 ALA N N 125.153 . 1 90 427 27 ASP H H 8.255 . 1 91 427 27 ASP CA C 55.08 . 1 92 427 27 ASP CB C 40.82 . 1 93 427 27 ASP N N 118.073 . 1 94 428 28 LEU H H 7.851 . 1 95 428 28 LEU CA C 56.34 . 1 96 428 28 LEU CB C 42.02 . 1 97 428 28 LEU N N 121.357 . 1 98 429 29 TYR H H 8.001 . 1 99 429 29 TYR CA C 59.01 . 1 100 429 29 TYR CB C 38.37 . 1 101 429 29 TYR N N 119.536 . 1 102 430 30 GLN H H 8.098 . 1 103 430 30 GLN CA C 56.97 . 1 104 430 30 GLN CB C 28.89 . 1 105 430 30 GLN N N 119.932 . 1 106 432 32 GLU H H 8.403 . 1 107 432 32 GLU CA C 57.6 . 1 108 432 32 GLU CB C 29.66 . 1 109 432 32 GLU N N 120.823 . 1 110 433 33 LEU H H 8.153 . 1 111 433 33 LEU CA C 56.13 . 1 112 433 33 LEU CB C 41.95 . 1 113 433 33 LEU N N 121.897 . 1 114 434 34 ALA H H 8.083 . 1 115 434 34 ALA CA C 53.67 . 1 116 434 34 ALA CB C 18.78 . 1 117 434 34 ALA N N 122.77 . 1 118 435 35 THR H H 7.91 . 1 119 435 35 THR CA C 63.08 . 1 120 435 35 THR CB C 69.33 . 1 121 435 35 THR N N 112.826 . 1 122 436 36 LEU H H 7.988 . 1 123 436 36 LEU CA C 56.06 . 1 124 436 36 LEU CB C 42.09 . 1 125 436 36 LEU N N 123.298 . 1 126 437 37 GLN H H 8.22 . 1 127 437 37 GLN CA C 56.41 . 1 128 437 37 GLN CB C 29.17 . 1 129 437 37 GLN N N 119.62 . 1 130 440 40 SER H H 8.103 . 1 131 440 40 SER CA C 55.64 . 1 132 440 40 SER CB C 64.13 . 1 133 440 40 SER N N 116.733 . 1 134 441 41 PRO CA C 63.78 . 1 135 441 41 PRO CB C 31.98 . 1 136 442 42 GLU H H 8.536 . 1 137 442 42 GLU CA C 57.25 . 1 138 442 42 GLU CB C 29.73 . 1 139 442 42 GLU N N 119.643 . 1 140 444 44 SER H H 8.156 . 1 141 444 44 SER CA C 58.66 . 1 142 444 44 SER CB C 63.71 . 1 143 444 44 SER N N 116.376 . 1 144 445 45 LEU H H 8.289 . 1 145 445 45 LEU CA C 55.43 . 1 146 445 45 LEU CB C 42.37 . 1 147 445 45 LEU N N 123.616 . 1 148 446 46 THR H H 8.026 . 1 149 446 46 THR CA C 61.68 . 1 150 446 46 THR CB C 69.82 . 1 151 446 46 THR N N 113.506 . 1 152 448 48 PRO CA C 64.06 . 1 153 448 48 PRO CB C 31.98 . 1 154 449 49 GLU H H 8.9 . 1 155 449 49 GLU CA C 57.25 . 1 156 449 49 GLU CB C 29.8 . 1 157 449 49 GLU N N 120.18 . 1 158 450 50 LEU H H 8.22 . 1 159 450 50 LEU CA C 55.71 . 1 160 450 50 LEU CB C 42.23 . 1 161 450 50 LEU N N 122.891 . 1 162 451 51 THR H H 8.025 . 1 163 451 51 THR CA C 63.36 . 1 164 451 51 THR CB C 69.33 . 1 165 451 51 THR N N 114.779 . 1 166 452 52 VAL H H 7.851 . 1 167 452 52 VAL CA C 63.57 . 1 168 452 52 VAL CB C 32.33 . 1 169 452 52 VAL N N 121.357 . 1 170 453 53 ALA H H 8.039 . 1 171 453 53 ALA CA C 53.67 . 1 172 453 53 ALA CB C 18.92 . 1 173 453 53 ALA N N 125.661 . 1 174 454 54 VAL H H 8.207 . 1 175 454 54 VAL CA C 65.54 . 1 176 454 54 VAL CB C 31.91 . 1 177 454 54 VAL N N 119.192 . 1 178 457 57 LEU H H 8.157 . 1 179 457 57 LEU CA C 57.67 . 1 180 457 57 LEU CB C 41.46 . 1 181 457 57 LEU N N 120.171 . 1 182 458 58 SER H H 8.57 . 1 183 458 58 SER CA C 61.04 . 1 184 458 58 SER CB C 62.66 . 1 185 458 58 SER N N 116.571 . 1 186 459 59 SER H H 7.898 . 1 187 459 59 SER CA C 60.83 . 1 188 459 59 SER CB C 62.52 . 1 189 459 59 SER N N 117.131 . 1 190 460 60 VAL H H 8.313 . 1 191 460 60 VAL CA C 66.94 . 1 192 460 60 VAL CB C 31.69 . 1 193 460 60 VAL N N 119.722 . 1 194 461 61 ALA H H 8.563 . 1 195 461 61 ALA CA C 56.34 . 1 196 461 61 ALA CB C 17.73 . 1 197 461 61 ALA N N 126.425 . 1 198 462 62 LEU H H 8.069 . 1 199 462 62 LEU CA C 58.17 . 1 200 462 62 LEU CB C 41.53 . 1 201 462 62 LEU N N 120.92 . 1 202 463 63 ILE H H 8.724 . 1 203 463 63 ILE CA C 66.83 . 1 204 463 63 ILE CB C 37.74 . 1 205 463 63 ILE N N 120.042 . 1 206 464 64 ASN H H 8.016 . 1 207 464 64 ASN CA C 58.87 . 1 208 464 64 ASN CB C 40.47 . 1 209 464 64 ASN N N 117.898 . 1 210 465 65 ARG H H 8.083 . 1 211 465 65 ARG CA C 59.15 . 1 212 465 65 ARG CB C 30.36 . 1 213 465 65 ARG N N 118.263 . 1 214 466 66 ALA H H 8.846 . 1 215 466 66 ALA CA C 54.87 . 1 216 466 66 ALA CB C 18.29 . 1 217 466 66 ALA N N 123.753 . 1 218 467 67 LEU H H 8.453 . 1 219 467 67 LEU CA C 57.81 . 1 220 467 67 LEU CB C 42.58 . 1 221 467 67 LEU N N 119.44 . 1 222 468 68 GLU H H 7.687 . 1 223 468 68 GLU CA C 58.94 . 1 224 468 68 GLU CB C 29.31 . 1 225 468 68 GLU N N 118.019 . 1 226 469 69 SER H H 7.91 . 1 227 469 69 SER CA C 58.66 . 1 228 469 69 SER CB C 64.13 . 1 229 469 69 SER N N 111.621 . 1 230 470 70 GLY H H 7.78 . 1 231 470 70 GLY CA C 46.3 . 1 232 470 70 GLY N N 111.271 . 1 233 471 71 ASP H H 8.454 . 1 234 471 71 ASP CA C 51.71 . 1 235 471 71 ASP CB C 38.99 . 1 236 471 71 ASP N N 120.717 . 1 237 472 72 MET H H 8.153 . 1 238 472 72 MET CA C 56.48 . 1 239 472 72 MET CB C 31.63 . 1 240 472 72 MET N N 121.897 . 1 241 473 73 THR H H 8.369 . 1 242 473 73 THR CA C 66.52 . 1 243 473 73 THR CB C 68.2 . 1 244 473 73 THR N N 117.469 . 1 245 474 74 THR H H 7.599 . 1 246 474 74 THR CA C 66.59 . 1 247 474 74 THR CB C 67.78 . 1 248 474 74 THR N N 120.922 . 1 249 476 76 TRP H H 8.454 . 1 250 476 76 TRP CA C 55.49 . 1 251 476 76 TRP CB C 29.59 . 1 252 476 76 TRP N N 120.717 . 1 253 477 77 LYS H H 8 . 1 254 477 77 LYS CA C 59.22 . 1 255 477 77 LYS CB C 33.17 . 1 256 477 77 LYS N N 120.912 . 1 257 478 78 GLN H H 8.098 . 1 258 478 78 GLN CA C 58.94 . 1 259 478 78 GLN CB C 29.17 . 1 260 478 78 GLN N N 119.932 . 1 261 479 79 LEU H H 8.884 . 1 262 479 79 LEU CA C 58.09 . 1 263 479 79 LEU CB C 42.3 . 1 264 479 79 LEU N N 122.002 . 1 265 480 80 SER H H 7.206 . 1 266 480 80 SER CA C 57.95 . 1 267 480 80 SER CB C 63.5 . 1 268 480 80 SER N N 106.455 . 1 269 481 81 SER H H 6.914 . 1 270 481 81 SER CA C 57.46 . 1 271 481 81 SER CB C 63.43 . 1 272 481 81 SER N N 116.51 . 1 273 483 83 VAL H H 7.847 . 1 274 483 83 VAL CA C 64.2 . 1 275 483 83 VAL CB C 31.63 . 1 276 483 83 VAL N N 119.728 . 1 277 484 84 THR H H 7.348 . 1 278 484 84 THR CA C 63.92 . 1 279 484 84 THR CB C 67.64 . 1 280 484 84 THR N N 114.907 . 1 281 485 85 GLY H H 7.574 . 1 282 485 85 GLY CA C 46.93 . 1 283 485 85 GLY N N 104.628 . 1 284 486 86 LEU H H 7.905 . 1 285 486 86 LEU CA C 54.59 . 1 286 486 86 LEU CB C 42.37 . 1 287 486 86 LEU N N 119.239 . 1 288 487 87 THR H H 9.51 . 1 289 487 87 THR CA C 60.56 . 1 290 487 87 THR CB C 71.4 . 1 291 487 87 THR N N 114.19 . 1 292 488 88 ASN H H 8.564 . 1 293 488 88 ASN CA C 54.28 . 1 294 488 88 ASN CB C 36.54 . 1 295 488 88 ASN N N 112.641 . 1 296 489 89 ILE H H 7.902 . 1 297 489 89 ILE CA C 60.55 . 1 298 489 89 ILE CB C 34.78 . 1 299 489 89 ILE N N 117.768 . 1 300 490 90 GLU H H 9.069 . 1 301 490 90 GLU CA C 54.3 . 1 302 490 90 GLU CB C 30.08 . 1 303 490 90 GLU N N 130.971 . 1 304 491 91 GLU H H 9.229 . 1 305 491 91 GLU CA C 60.69 . 1 306 491 91 GLU CB C 29.66 . 1 307 491 91 GLU N N 127.975 . 1 308 492 92 GLU H H 9.476 . 1 309 492 92 GLU CA C 58.77 . 1 310 492 92 GLU CB C 29.17 . 1 311 492 92 GLU N N 117.988 . 1 312 493 93 ASN H H 7.777 . 1 313 493 93 ASN CA C 51.99 . 1 314 493 93 ASN CB C 38.44 . 1 315 493 93 ASN N N 115.64 . 1 316 494 94 CYS H H 7.143 . 1 317 494 94 CYS CA C 62.66 . 1 318 494 94 CYS CB C 26.29 . 1 319 494 94 CYS N N 118.55 . 1 320 495 95 GLN H H 8.312 . 1 321 495 95 GLN CA C 58.79 . 1 322 495 95 GLN CB C 28.12 . 1 323 495 95 GLN N N 116.395 . 1 324 496 96 ARG H H 7.271 . 1 325 496 96 ARG CA C 58.94 . 1 326 496 96 ARG CB C 30.22 . 1 327 496 96 ARG N N 117.169 . 1 328 497 97 TYR H H 8.224 . 1 329 497 97 TYR CA C 59.36 . 1 330 497 97 TYR CB C 37.95 . 1 331 497 97 TYR N N 117.756 . 1 332 498 98 LEU H H 8.016 . 1 333 498 98 LEU CA C 58.87 . 1 334 498 98 LEU CB C 40.47 . 1 335 498 98 LEU N N 117.898 . 1 336 499 99 ASP H H 8.471 . 1 337 499 99 ASP CA C 57.42 . 1 338 499 99 ASP CB C 40.61 . 1 339 499 99 ASP N N 118.416 . 1 340 501 101 LEU H H 8.806 . 1 341 501 101 LEU CA C 57.88 . 1 342 501 101 LEU CB C 42.37 . 1 343 501 101 LEU N N 122.954 . 1 344 502 102 MET H H 8.258 . 1 345 502 102 MET CA C 58.17 . 1 346 502 102 MET CB C 32.05 . 1 347 502 102 MET N N 118.073 . 1 348 503 103 LYS H H 7.61 . 1 349 503 103 LYS CA C 59.57 . 1 350 503 103 LYS CB C 32.33 . 1 351 503 103 LYS N N 121.339 . 1 352 504 104 LEU H H 8.259 . 1 353 504 104 LEU CA C 57.53 . 1 354 504 104 LEU CB C 42.09 . 1 355 504 104 LEU N N 121.448 . 1 356 505 105 LYS H H 8.47 . 1 357 505 105 LYS CA C 57.53 . 1 358 505 105 LYS CB C 31.77 . 1 359 505 105 LYS N N 119.583 . 1 360 506 106 ALA H H 7.824 . 1 361 506 106 ALA CA C 54.73 . 1 362 506 106 ALA CB C 18.08 . 1 363 506 106 ALA N N 121.14 . 1 364 507 107 GLN H H 8.001 . 1 365 507 107 GLN CA C 57.74 . 1 366 507 107 GLN CB C 28.54 . 1 367 507 107 GLN N N 119.536 . 1 368 508 108 ALA H H 8.24 . 1 369 508 108 ALA CA C 54.66 . 1 370 508 108 ALA CB C 17.94 . 1 371 508 108 ALA N N 123.342 . 1 372 509 109 HIS H H 8.299 . 1 373 509 109 HIS CA C 59.08 . 1 374 509 109 HIS CB C 30.5 . 1 375 509 109 HIS N N 118.418 . 1 376 510 110 ALA H H 7.988 . 1 377 510 110 ALA CA C 54.09 . 1 378 510 110 ALA CB C 18.43 . 1 379 510 110 ALA N N 123.298 . 1 380 511 111 GLU H H 7.99 . 1 381 511 111 GLU CA C 55.92 . 1 382 511 111 GLU CB C 29.38 . 1 383 511 111 GLU N N 117.494 . 1 384 512 112 ASN H H 8.051 . 1 385 512 112 ASN CA C 53.88 . 1 386 512 112 ASN CB C 37.88 . 1 387 512 112 ASN N N 115.356 . 1 388 513 113 ASN H H 8.313 . 1 389 513 113 ASN CA C 53.04 . 1 390 513 113 ASN CB C 38.65 . 1 391 513 113 ASN N N 117.364 . 1 392 514 114 ALA H H 8.22 . 1 393 514 114 ALA CA C 53.39 . 1 394 514 114 ALA CB C 19.41 . 1 395 514 114 ALA N N 122.891 . 1 396 515 115 PHE H H 7.893 . 1 397 515 115 PHE CA C 56.97 . 1 398 515 115 PHE CB C 40.82 . 1 399 515 115 PHE N N 118.489 . 1 400 516 116 ILE H H 8.741 . 1 401 516 116 ILE CA C 60.34 . 1 402 516 116 ILE CB C 38.86 . 1 403 516 116 ILE N N 121.574 . 1 404 517 117 THR H H 9.1 . 1 405 517 117 THR CA C 60.83 . 1 406 517 117 THR CB C 72.42 . 1 407 517 117 THR N N 115.082 . 1 408 518 118 TRP H H 9.524 . 1 409 518 118 TRP CA C 63.57 . 1 410 518 118 TRP CB C 29.73 . 1 411 518 118 TRP N N 120.669 . 1 412 519 119 ASN H H 8.518 . 1 413 519 119 ASN CA C 57.18 . 1 414 519 119 ASN CB C 38.51 . 1 415 519 119 ASN N N 114.514 . 1 416 520 120 ASP H H 7.766 . 1 417 520 120 ASP CA C 57.32 . 1 418 520 120 ASP CB C 41.01 . 1 419 520 120 ASP N N 120.778 . 1 420 521 121 ILE H H 8.069 . 1 421 521 121 ILE CA C 65.89 . 1 422 521 121 ILE CB C 37.45 . 1 423 521 121 ILE N N 120.92 . 1 424 522 122 GLN H H 8.22 . 1 425 522 122 GLN CA C 58.24 . 1 426 522 122 GLN CB C 27.69 . 1 427 522 122 GLN N N 119.62 . 1 428 523 123 ALA H H 8.001 . 1 429 523 123 ALA CA C 55.22 . 1 430 523 123 ALA CB C 17.94 . 1 431 523 123 ALA N N 119.536 . 1 432 524 124 CYS H H 7.748 . 1 433 524 124 CYS CA C 62.66 . 1 434 524 124 CYS CB C 26.64 . 1 435 524 124 CYS N N 120.279 . 1 436 525 125 VAL H H 8 . 1 437 525 125 VAL CA C 66.09 . 1 438 525 125 VAL CB C 32.05 . 1 439 525 125 VAL N N 120.912 . 1 440 526 126 ASP H H 8.37 . 1 441 526 126 ASP CA C 57.25 . 1 442 526 126 ASP CB C 40.05 . 1 443 526 126 ASP N N 118.186 . 1 444 528 128 VAL H H 8.595 . 1 445 528 128 VAL CA C 66.33 . 1 446 528 128 VAL CB C 31.49 . 1 447 528 128 VAL N N 120.613 . 1 448 529 129 ASN H H 8.407 . 1 449 529 129 ASN CA C 54.37 . 1 450 529 129 ASN CB C 37.46 . 1 451 529 129 ASN N N 115.71 . 1 452 530 130 LEU H H 7.48 . 1 453 530 130 LEU CA C 56.55 . 1 454 530 130 LEU CB C 43 . 1 455 530 130 LEU N N 119.325 . 1 456 531 131 VAL H H 7.763 . 1 457 531 131 VAL CA C 63.08 . 1 458 531 131 VAL CB C 32.19 . 1 459 531 131 VAL N N 119.021 . 1 460 532 132 VAL H H 7.905 . 1 461 532 132 VAL CA C 62.66 . 1 462 532 132 VAL CB C 32.33 . 1 463 532 132 VAL N N 122.729 . 1 464 533 133 HIS H H 7.794 . 1 465 533 133 HIS CA C 57.39 . 1 466 533 133 HIS CB C 30.93 . 1 467 533 133 HIS N N 127.983 . 1 stop_ save_