data_15710 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Basis of PxxDY Motif Recognition in SH3 Binding ; _BMRB_accession_number 15710 _BMRB_flat_file_name bmr15710.str _Entry_type original _Submission_date 2008-04-02 _Accession_date 2008-04-02 _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 Aitio Olli . . 2 Hellman Maarit . . 3 Kesti Tapio . . 4 Kleino Iivari . . 5 Samuilova Olga . . 6 Tossavainen Helena . . 7 Saksela Kalle . . 8 Permi Perttu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 382 "13C chemical shifts" 235 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-28 original author . stop_ _Original_release_date 2008-08-28 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis of PxxDY motif recognition in SH3 binding' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18644376 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aitio Olli . . 2 Hellman Maarit . . 3 Kesti Tapio . . 4 Kleino Iivari . . 5 Samuilova Olga . . 6 Paakkonen Kimmo . . 7 Tossavainen Helena . . 8 Saksela Kalle . . 9 Permi Perttu . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 382 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 167 _Page_last 178 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Eps8L1SH3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'component 1' $Eps8L1SH3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Eps8L1SH3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Eps8L1SH3 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; GPLGSGALKWVLCNYDFQAR NSSELSVKQRDVLEVLDDSR KWWKVRDPAGQEGYVPYNIL TPYPAAAS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 473 GLY 2 474 PRO 3 475 LEU 4 476 GLY 5 477 SER 6 478 GLY 7 479 ALA 8 480 LEU 9 481 LYS 10 482 TRP 11 483 VAL 12 484 LEU 13 485 CYS 14 486 ASN 15 487 TYR 16 488 ASP 17 489 PHE 18 490 GLN 19 491 ALA 20 492 ARG 21 493 ASN 22 494 SER 23 495 SER 24 496 GLU 25 497 LEU 26 498 SER 27 499 VAL 28 500 LYS 29 501 GLN 30 502 ARG 31 503 ASP 32 504 VAL 33 505 LEU 34 506 GLU 35 507 VAL 36 508 LEU 37 509 ASP 38 510 ASP 39 511 SER 40 512 ARG 41 513 LYS 42 514 TRP 43 515 TRP 44 516 LYS 45 517 VAL 46 518 ARG 47 519 ASP 48 520 PRO 49 521 ALA 50 522 GLY 51 523 GLN 52 524 GLU 53 525 GLY 54 526 TYR 55 527 VAL 56 528 PRO 57 529 TYR 58 530 ASN 59 531 ILE 60 532 LEU 61 533 THR 62 534 PRO 63 535 TYR 64 536 PRO 65 537 ALA 66 538 ALA 67 539 ALA 68 540 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-22 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 2K2M "Structural Basis Of Pxxdy Motif Recognition In Sh3 Binding" 100.00 68 100.00 100.00 2.24e-41 DBJ BAA91041 "unnamed protein product [Homo sapiens]" 85.29 596 98.28 98.28 2.76e-31 DBJ BAC11399 "unnamed protein product [Homo sapiens]" 85.29 723 98.28 98.28 5.64e-31 DBJ BAG59319 "unnamed protein product [Homo sapiens]" 85.29 659 98.28 98.28 4.55e-31 GB AAG03038 "DRC3 [Homo sapiens]" 85.29 437 98.28 98.28 5.13e-31 GB AAG03039 "DRC3 [Homo sapiens]" 85.29 437 98.28 98.28 5.13e-31 GB AAH15763 "EPS8-like 1 [Homo sapiens]" 85.29 596 98.28 98.28 2.74e-31 GB AAL76117 "epidermal growth factor receptor pathway substrate 8 related protein 1 [Homo sapiens]" 85.29 723 98.28 98.28 5.37e-31 GB AAQ15231 "PP10566 [Homo sapiens]" 85.29 723 98.28 98.28 5.59e-31 REF NP_060199 "epidermal growth factor receptor kinase substrate 8-like protein 1 isoform b [Homo sapiens]" 85.29 596 98.28 98.28 2.74e-31 REF NP_573441 "epidermal growth factor receptor kinase substrate 8-like protein 1 isoform a [Homo sapiens]" 85.29 723 98.28 98.28 5.81e-31 REF XP_005259077 "PREDICTED: epidermal growth factor receptor kinase substrate 8-like protein 1 isoform X1 [Homo sapiens]" 85.29 755 98.28 98.28 6.75e-31 REF XP_011525352 "PREDICTED: epidermal growth factor receptor kinase substrate 8-like protein 1 isoform X2 [Homo sapiens]" 85.29 628 98.28 98.28 4.48e-31 SP Q8TE68 "RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 1; Short=EPS8-like protein 1; AltName: Full=Epid" 85.29 723 98.28 98.28 5.81e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Eps8L1SH3 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 $Eps8L1SH3 'recombinant technology' . Escherichia coli . pGEX6P 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 $Eps8L1SH3 0.8 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version . loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . stop_ loop_ _Task 'geometry optimization' 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_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_iHNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D iHNCACB' _Sample_label $sample_1 save_ save_3D_iHNCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D iHNCA' _Sample_label $sample_1 save_ save_3D_HCCH-COSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_1 save_ save_3D_CC(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CC(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_2D_(HB)CB(CGCD)HD_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (HB)CB(CGCD)HD' _Sample_label $sample_1 save_ save_2D_(HB)CB(CGCDCE)HE_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (HB)CB(CGCDCE)HE' _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 pH 7.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; For the 13C axis, we calculated the position of the transmitter using the DSS indirect shift ratio and ended up with this value of 175.571 ppm, in the carbonyl carbon region of the protein 13C spectrum. The midpoint of the aliphatic 13C spectrum is at 118 or 128 ppms from this value, depending on the spectrum. For the 15N axis, we calculated the midpoint of the 15N spectrum from the 1H midpoint using the indirect shift ratio of liquid ammonia, 0.101329118. ; 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 na indirect . . . 0.25144953 water H 1 protons ppm 4.793 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.00 na 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' '2D 1H-13C HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' '3D iHNCACB' '3D iHNCA' '3D HCCH-COSY' '3D CC(CO)NH' '3D H(CCO)NH' '2D (HB)CB(CGCD)HD' '2D (HB)CB(CGCDCE)HE' 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 'component 1' _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 1 474 2 PRO HA H 4.474 0.020 1 2 474 2 PRO HB2 H 2.292 0.020 2 3 474 2 PRO HB3 H 1.937 0.020 2 4 474 2 PRO HD2 H 3.563 0.020 1 5 474 2 PRO HD3 H 3.563 0.020 1 6 474 2 PRO HG2 H 1.995 0.020 1 7 474 2 PRO HG3 H 1.995 0.020 1 8 474 2 PRO CA C 63.244 0.200 1 9 474 2 PRO CB C 32.451 0.200 1 10 474 2 PRO CD C 49.708 0.200 1 11 474 2 PRO CG C 27.256 0.200 1 12 475 3 LEU H H 8.484 0.020 1 13 475 3 LEU HA H 4.331 0.020 1 14 475 3 LEU HB2 H 1.667 0.020 2 15 475 3 LEU HB3 H 1.582 0.020 2 16 475 3 LEU HD1 H 0.861 0.020 1 17 475 3 LEU HD2 H 0.861 0.020 1 18 475 3 LEU CA C 55.502 0.200 1 19 475 3 LEU CB C 42.413 0.200 1 20 475 3 LEU CD1 C 24.798 0.200 2 21 475 3 LEU CD2 C 23.471 0.200 2 22 475 3 LEU CG C 27.067 0.200 1 23 475 3 LEU N N 122.189 0.200 1 24 476 4 GLY H H 8.375 0.020 1 25 476 4 GLY CA C 45.322 0.200 1 26 476 4 GLY N N 110.000 0.200 1 27 478 6 GLY HA2 H 3.982 0.020 1 28 478 6 GLY HA3 H 3.982 0.020 1 29 478 6 GLY CA C 45.336 0.200 1 30 479 7 ALA H H 8.026 0.020 1 31 479 7 ALA HA H 4.314 0.020 1 32 479 7 ALA HB H 1.310 0.020 1 33 479 7 ALA CA C 52.345 0.200 1 34 479 7 ALA CB C 19.795 0.200 1 35 479 7 ALA N N 123.184 0.200 1 36 480 8 LEU H H 8.230 0.020 1 37 480 8 LEU HA H 4.308 0.020 1 38 480 8 LEU HB2 H 1.554 0.020 2 39 480 8 LEU HB3 H 1.334 0.020 2 40 480 8 LEU HD1 H 0.891 0.020 1 41 480 8 LEU HD2 H 0.891 0.020 1 42 480 8 LEU HG H 1.584 0.020 1 43 480 8 LEU CA C 55.216 0.200 1 44 480 8 LEU CB C 42.655 0.200 1 45 480 8 LEU CD1 C 25.185 0.200 2 46 480 8 LEU CD2 C 23.432 0.200 2 47 480 8 LEU CG C 27.340 0.200 1 48 480 8 LEU N N 121.391 0.200 1 49 481 9 LYS H H 8.116 0.020 1 50 481 9 LYS HA H 4.398 0.020 1 51 481 9 LYS HB2 H 1.704 0.020 1 52 481 9 LYS HB3 H 1.704 0.020 1 53 481 9 LYS HD2 H 1.539 0.020 1 54 481 9 LYS HD3 H 1.539 0.020 1 55 481 9 LYS HE2 H 2.785 0.020 1 56 481 9 LYS HE3 H 2.785 0.020 1 57 481 9 LYS HG2 H 1.208 0.020 2 58 481 9 LYS HG3 H 1.062 0.020 2 59 481 9 LYS CA C 56.164 0.200 1 60 481 9 LYS CB C 34.254 0.200 1 61 481 9 LYS CD C 29.297 0.200 1 62 481 9 LYS CE C 42.108 0.200 1 63 481 9 LYS CG C 24.560 0.200 1 64 481 9 LYS N N 120.643 0.200 1 65 482 10 TRP H H 8.341 0.020 1 66 482 10 TRP HA H 5.723 0.020 1 67 482 10 TRP HB2 H 3.246 0.020 2 68 482 10 TRP HB3 H 3.126 0.020 2 69 482 10 TRP HD1 H 7.151 0.020 1 70 482 10 TRP HE1 H 10.103 0.020 1 71 482 10 TRP HE3 H 7.423 0.020 1 72 482 10 TRP HH2 H 7.157 0.020 1 73 482 10 TRP HZ2 H 7.416 0.020 1 74 482 10 TRP HZ3 H 7.110 0.020 1 75 482 10 TRP CA C 55.880 0.200 1 76 482 10 TRP CB C 32.599 0.200 1 77 482 10 TRP CD1 C 126.753 0.200 1 78 482 10 TRP CE3 C 120.437 0.200 1 79 482 10 TRP CH2 C 124.256 0.200 1 80 482 10 TRP CZ2 C 114.378 0.200 1 81 482 10 TRP CZ3 C 121.844 0.200 1 82 482 10 TRP N N 120.701 0.200 1 83 482 10 TRP NE1 N 128.684 0.200 1 84 483 11 VAL H H 9.440 0.020 1 85 483 11 VAL HA H 5.232 0.020 1 86 483 11 VAL HB H 2.206 0.020 1 87 483 11 VAL HG1 H 1.019 0.020 1 88 483 11 VAL HG2 H 0.934 0.020 1 89 483 11 VAL CA C 59.037 0.200 1 90 483 11 VAL CB C 36.491 0.200 1 91 483 11 VAL CG1 C 23.325 0.200 1 92 483 11 VAL CG2 C 20.245 0.200 1 93 483 11 VAL N N 114.496 0.200 1 94 484 12 LEU H H 9.188 0.020 1 95 484 12 LEU HA H 5.031 0.020 1 96 484 12 LEU HB2 H 1.618 0.020 2 97 484 12 LEU HB3 H 1.337 0.020 2 98 484 12 LEU HD1 H 0.780 0.020 2 99 484 12 LEU HD2 H 0.712 0.020 2 100 484 12 LEU HG H 1.333 0.020 1 101 484 12 LEU CA C 52.973 0.200 1 102 484 12 LEU CB C 45.870 0.200 1 103 484 12 LEU CD1 C 26.168 0.200 2 104 484 12 LEU CD2 C 25.416 0.200 2 105 484 12 LEU CG C 27.308 0.200 1 106 484 12 LEU N N 122.079 0.200 1 107 485 13 CYS H H 8.782 0.020 1 108 485 13 CYS HA H 4.680 0.020 1 109 485 13 CYS HB2 H 2.957 0.020 2 110 485 13 CYS HB3 H 2.692 0.020 2 111 485 13 CYS CA C 58.841 0.200 1 112 485 13 CYS CB C 27.210 0.200 1 113 485 13 CYS N N 122.901 0.200 1 114 486 14 ASN H H 9.485 0.020 1 115 486 14 ASN HA H 4.732 0.020 1 116 486 14 ASN HB2 H 2.503 0.020 2 117 486 14 ASN HB3 H 2.364 0.020 2 118 486 14 ASN CA C 54.175 0.200 1 119 486 14 ASN CB C 40.632 0.200 1 120 486 14 ASN N N 127.448 0.200 1 121 487 15 TYR H H 7.576 0.020 1 122 487 15 TYR HA H 4.628 0.020 1 123 487 15 TYR HB2 H 3.169 0.020 2 124 487 15 TYR HB3 H 2.518 0.020 2 125 487 15 TYR HD1 H 7.113 0.020 3 126 487 15 TYR HD2 H 7.113 0.020 3 127 487 15 TYR HE1 H 6.859 0.020 3 128 487 15 TYR HE2 H 6.859 0.020 3 129 487 15 TYR CA C 56.955 0.200 1 130 487 15 TYR CB C 42.916 0.200 1 131 487 15 TYR CD1 C 133.183 0.200 3 132 487 15 TYR CD2 C 133.183 0.200 3 133 487 15 TYR CE1 C 118.041 0.200 3 134 487 15 TYR CE2 C 118.041 0.200 3 135 487 15 TYR N N 116.817 0.200 1 136 488 16 ASP H H 8.323 0.020 1 137 488 16 ASP HA H 4.704 0.020 1 138 488 16 ASP HB2 H 2.722 0.020 2 139 488 16 ASP HB3 H 2.588 0.020 2 140 488 16 ASP CA C 54.910 0.200 1 141 488 16 ASP CB C 41.576 0.200 1 142 488 16 ASP N N 118.946 0.200 1 143 489 17 PHE H H 8.669 0.020 1 144 489 17 PHE HA H 4.697 0.020 1 145 489 17 PHE HB2 H 3.056 0.020 2 146 489 17 PHE HB3 H 2.828 0.020 2 147 489 17 PHE HD1 H 7.565 0.020 3 148 489 17 PHE HD2 H 7.565 0.020 3 149 489 17 PHE HE1 H 7.492 0.020 3 150 489 17 PHE HE2 H 7.492 0.020 3 151 489 17 PHE HZ H 7.720 0.020 2 152 489 17 PHE CA C 58.330 0.200 1 153 489 17 PHE CB C 43.042 0.200 1 154 489 17 PHE CD1 C 132.384 0.200 3 155 489 17 PHE CD2 C 132.384 0.200 3 156 489 17 PHE CE1 C 131.131 0.200 3 157 489 17 PHE CZ C 130.780 0.200 1 158 489 17 PHE N N 122.610 0.200 1 159 490 18 GLN H H 7.579 0.020 1 160 490 18 GLN HA H 4.437 0.020 1 161 490 18 GLN HB2 H 1.748 0.020 1 162 490 18 GLN HB3 H 1.748 0.020 1 163 490 18 GLN HG2 H 2.219 0.020 1 164 490 18 GLN HG3 H 2.219 0.020 1 165 490 18 GLN CA C 53.289 0.200 1 166 490 18 GLN CB C 29.972 0.200 1 167 490 18 GLN CG C 33.733 0.200 1 168 490 18 GLN N N 127.465 0.200 1 169 491 19 ALA H H 8.485 0.020 1 170 491 19 ALA HA H 4.096 0.020 1 171 491 19 ALA HB H 1.385 0.020 1 172 491 19 ALA CA C 53.089 0.200 1 173 491 19 ALA CB C 20.857 0.200 1 174 491 19 ALA N N 127.190 0.200 1 175 492 20 ARG H H 9.439 0.020 1 176 492 20 ARG HA H 4.402 0.020 1 177 492 20 ARG HB2 H 2.034 0.020 2 178 492 20 ARG HB3 H 1.946 0.020 2 179 492 20 ARG HD2 H 3.484 0.020 2 180 492 20 ARG HD3 H 3.323 0.020 2 181 492 20 ARG HG2 H 1.828 0.020 1 182 492 20 ARG HG3 H 1.828 0.020 1 183 492 20 ARG CA C 56.673 0.200 1 184 492 20 ARG CB C 30.509 0.200 1 185 492 20 ARG CD C 42.983 0.200 1 186 492 20 ARG CG C 27.193 0.200 1 187 492 20 ARG N N 120.914 0.200 1 188 493 21 ASN H H 7.571 0.020 1 189 493 21 ASN HA H 4.790 0.020 1 190 493 21 ASN HB2 H 2.949 0.020 1 191 493 21 ASN HB3 H 2.949 0.020 1 192 493 21 ASN CA C 52.070 0.200 1 193 493 21 ASN CB C 40.636 0.200 1 194 493 21 ASN N N 112.659 0.200 1 195 494 22 SER HA H 4.430 0.020 1 196 494 22 SER HB2 H 4.146 0.020 2 197 494 22 SER HB3 H 4.019 0.020 2 198 494 22 SER CA C 60.971 0.200 1 199 494 22 SER CB C 63.403 0.200 1 200 495 23 SER H H 8.630 0.020 1 201 495 23 SER HA H 4.737 0.020 1 202 495 23 SER HB2 H 4.135 0.020 2 203 495 23 SER HB3 H 4.017 0.020 2 204 495 23 SER CA C 59.730 0.200 1 205 495 23 SER CB C 64.042 0.200 1 206 495 23 SER N N 116.744 0.200 1 207 496 24 GLU H H 7.669 0.020 1 208 496 24 GLU HA H 5.374 0.020 1 209 496 24 GLU HB2 H 2.529 0.020 2 210 496 24 GLU HB3 H 2.282 0.020 2 211 496 24 GLU HG2 H 2.471 0.020 2 212 496 24 GLU HG3 H 2.401 0.020 2 213 496 24 GLU CA C 55.502 0.200 1 214 496 24 GLU CB C 33.099 0.200 1 215 496 24 GLU CG C 36.914 0.200 1 216 496 24 GLU N N 123.213 0.200 1 217 497 25 LEU H H 8.058 0.020 1 218 497 25 LEU HA H 4.781 0.020 1 219 497 25 LEU HB2 H 1.614 0.020 2 220 497 25 LEU HB3 H 0.779 0.020 2 221 497 25 LEU HD1 H 0.812 0.020 1 222 497 25 LEU HD2 H 0.643 0.020 1 223 497 25 LEU HG H 1.477 0.020 1 224 497 25 LEU CA C 53.175 0.200 1 225 497 25 LEU CB C 46.385 0.200 1 226 497 25 LEU CD1 C 24.340 0.200 1 227 497 25 LEU CD2 C 26.374 0.200 1 228 497 25 LEU CG C 26.456 0.200 1 229 497 25 LEU N N 122.845 0.200 1 230 498 26 SER H H 8.214 0.020 1 231 498 26 SER HA H 5.172 0.020 1 232 498 26 SER HB2 H 4.061 0.020 2 233 498 26 SER HB3 H 3.896 0.020 2 234 498 26 SER CA C 59.006 0.200 1 235 498 26 SER CB C 63.378 0.200 1 236 498 26 SER N N 119.915 0.200 1 237 499 27 VAL H H 9.026 0.020 1 238 499 27 VAL HA H 4.832 0.020 1 239 499 27 VAL HB H 2.549 0.020 1 240 499 27 VAL HG1 H 1.017 0.020 1 241 499 27 VAL HG2 H 1.161 0.020 1 242 499 27 VAL CA C 59.759 0.200 1 243 499 27 VAL CB C 36.996 0.200 1 244 499 27 VAL CG1 C 23.988 0.200 1 245 499 27 VAL CG2 C 21.477 0.200 1 246 499 27 VAL N N 117.752 0.200 1 247 500 28 LYS H H 9.025 0.020 1 248 500 28 LYS HA H 4.998 0.020 1 249 500 28 LYS HB2 H 1.784 0.020 2 250 500 28 LYS HB3 H 1.736 0.020 2 251 500 28 LYS HD2 H 1.713 0.020 2 252 500 28 LYS HD3 H 1.681 0.020 2 253 500 28 LYS HE2 H 3.050 0.020 1 254 500 28 LYS HE3 H 3.050 0.020 1 255 500 28 LYS HG2 H 1.434 0.020 1 256 500 28 LYS HG3 H 1.434 0.020 1 257 500 28 LYS CA C 53.723 0.200 1 258 500 28 LYS CB C 35.295 0.200 1 259 500 28 LYS CD C 28.906 0.200 1 260 500 28 LYS CE C 42.120 0.200 1 261 500 28 LYS CG C 24.459 0.200 1 262 500 28 LYS N N 122.651 0.200 1 263 501 29 GLN H H 8.812 0.020 1 264 501 29 GLN HA H 3.453 0.020 1 265 501 29 GLN HB2 H 1.886 0.020 2 266 501 29 GLN HB3 H 1.784 0.020 2 267 501 29 GLN HG2 H 2.203 0.020 2 268 501 29 GLN HG3 H 2.170 0.020 2 269 501 29 GLN CA C 58.124 0.200 1 270 501 29 GLN CB C 29.224 0.200 1 271 501 29 GLN CG C 33.987 0.200 1 272 501 29 GLN N N 120.413 0.200 1 273 502 30 ARG H H 9.000 0.020 1 274 502 30 ARG HA H 3.646 0.020 1 275 502 30 ARG HB2 H 2.429 0.020 2 276 502 30 ARG HB3 H 2.073 0.020 2 277 502 30 ARG HD2 H 3.255 0.020 2 278 502 30 ARG HD3 H 3.180 0.020 2 279 502 30 ARG HG2 H 1.616 0.020 1 280 502 30 ARG HG3 H 1.616 0.020 1 281 502 30 ARG CA C 59.698 0.200 1 282 502 30 ARG CB C 27.644 0.200 1 283 502 30 ARG CD C 43.339 0.200 1 284 502 30 ARG CG C 29.035 0.200 1 285 502 30 ARG N N 116.988 0.200 1 286 503 31 ASP H H 8.283 0.020 1 287 503 31 ASP HA H 4.593 0.020 1 288 503 31 ASP HB2 H 3.064 0.020 2 289 503 31 ASP HB3 H 2.452 0.020 2 290 503 31 ASP CA C 56.110 0.200 1 291 503 31 ASP CB C 41.296 0.200 1 292 503 31 ASP N N 121.475 0.200 1 293 504 32 VAL H H 8.050 0.020 1 294 504 32 VAL HA H 4.861 0.020 1 295 504 32 VAL HB H 1.854 0.020 1 296 504 32 VAL HG1 H 0.766 0.020 2 297 504 32 VAL HG2 H 0.737 0.020 2 298 504 32 VAL CA C 61.789 0.200 1 299 504 32 VAL CB C 32.572 0.200 1 300 504 32 VAL CG1 C 21.712 0.200 2 301 504 32 VAL CG2 C 21.760 0.200 2 302 504 32 VAL N N 121.436 0.200 1 303 505 33 LEU H H 9.122 0.020 1 304 505 33 LEU HA H 5.045 0.020 1 305 505 33 LEU HB2 H 1.568 0.020 2 306 505 33 LEU HB3 H 1.349 0.020 2 307 505 33 LEU HD1 H 0.864 0.020 1 308 505 33 LEU HD2 H 0.954 0.020 1 309 505 33 LEU HG H 1.611 0.020 1 310 505 33 LEU CA C 52.931 0.200 1 311 505 33 LEU CB C 45.272 0.200 1 312 505 33 LEU CD1 C 26.900 0.200 1 313 505 33 LEU CD2 C 24.110 0.200 1 314 505 33 LEU N N 125.761 0.200 1 315 506 34 GLU H H 8.487 0.020 1 316 506 34 GLU HA H 4.386 0.020 1 317 506 34 GLU HB2 H 1.692 0.020 1 318 506 34 GLU HB3 H 1.692 0.020 1 319 506 34 GLU HG2 H 1.489 0.020 1 320 506 34 GLU HG3 H 1.489 0.020 1 321 506 34 GLU CA C 54.795 0.200 1 322 506 34 GLU CB C 32.009 0.200 1 323 506 34 GLU CG C 36.085 0.200 1 324 506 34 GLU N N 122.166 0.200 1 325 507 35 VAL H H 8.675 0.020 1 326 507 35 VAL HA H 3.958 0.020 1 327 507 35 VAL HB H 1.887 0.020 1 328 507 35 VAL HG1 H 0.544 0.020 1 329 507 35 VAL HG2 H 1.007 0.020 1 330 507 35 VAL CA C 63.770 0.200 1 331 507 35 VAL CB C 32.446 0.200 1 332 507 35 VAL CG1 C 22.014 0.200 1 333 507 35 VAL CG2 C 24.103 0.200 1 334 507 35 VAL N N 124.509 0.200 1 335 508 36 LEU H H 9.119 0.020 1 336 508 36 LEU HA H 4.443 0.020 1 337 508 36 LEU HB2 H 1.469 0.020 2 338 508 36 LEU HB3 H 1.161 0.020 2 339 508 36 LEU HD1 H 0.646 0.020 1 340 508 36 LEU HD2 H 0.593 0.020 1 341 508 36 LEU HG H 1.392 0.020 1 342 508 36 LEU CA C 55.142 0.200 1 343 508 36 LEU CB C 42.233 0.200 1 344 508 36 LEU CD1 C 25.672 0.200 1 345 508 36 LEU CD2 C 21.867 0.200 1 346 508 36 LEU CG C 27.342 0.200 1 347 508 36 LEU N N 127.447 0.200 1 348 509 37 ASP H H 7.544 0.020 1 349 509 37 ASP HA H 4.623 0.020 1 350 509 37 ASP HB2 H 2.714 0.020 1 351 509 37 ASP HB3 H 2.714 0.020 1 352 509 37 ASP CA C 55.295 0.200 1 353 509 37 ASP CB C 43.281 0.200 1 354 509 37 ASP N N 116.227 0.200 1 355 510 38 ASP H H 8.100 0.020 1 356 510 38 ASP HA H 3.309 0.020 1 357 510 38 ASP HB2 H 1.458 0.020 2 358 510 38 ASP HB3 H 0.717 0.020 2 359 510 38 ASP CA C 51.779 0.200 1 360 510 38 ASP CB C 38.848 0.200 1 361 510 38 ASP N N 128.170 0.200 1 362 511 39 SER H H 8.168 0.020 1 363 511 39 SER HA H 4.134 0.020 1 364 511 39 SER HB2 H 3.975 0.020 1 365 511 39 SER HB3 H 3.975 0.020 1 366 511 39 SER CA C 61.364 0.200 1 367 511 39 SER CB C 64.333 0.200 1 368 511 39 SER N N 114.442 0.200 1 369 512 40 ARG H H 8.168 0.020 1 370 512 40 ARG HA H 4.822 0.020 1 371 512 40 ARG HB2 H 2.273 0.020 2 372 512 40 ARG HB3 H 2.156 0.020 2 373 512 40 ARG HD2 H 3.298 0.020 2 374 512 40 ARG HD3 H 3.254 0.020 2 375 512 40 ARG HG2 H 1.886 0.020 2 376 512 40 ARG HG3 H 1.742 0.020 2 377 512 40 ARG CA C 55.037 0.200 1 378 512 40 ARG CB C 32.208 0.200 1 379 512 40 ARG CD C 43.773 0.200 1 380 512 40 ARG CG C 27.744 0.200 1 381 512 40 ARG N N 122.167 0.200 1 382 513 41 LYS HA H 4.092 0.020 1 383 513 41 LYS HB2 H 1.914 0.020 2 384 513 41 LYS HB3 H 1.884 0.020 2 385 513 41 LYS HD2 H 1.615 0.020 1 386 513 41 LYS HD3 H 1.615 0.020 1 387 513 41 LYS HE2 H 2.959 0.020 1 388 513 41 LYS HE3 H 2.959 0.020 1 389 513 41 LYS HG2 H 1.493 0.020 2 390 513 41 LYS HG3 H 1.276 0.020 2 391 513 41 LYS CA C 58.219 0.200 1 392 513 41 LYS CB C 32.134 0.200 1 393 513 41 LYS CD C 29.178 0.200 1 394 513 41 LYS CE C 42.349 0.200 1 395 513 41 LYS CG C 25.746 0.200 1 396 514 42 TRP H H 7.336 0.020 1 397 514 42 TRP HA H 4.983 0.020 1 398 514 42 TRP HB2 H 3.087 0.020 2 399 514 42 TRP HB3 H 2.952 0.020 2 400 514 42 TRP HD1 H 7.076 0.020 1 401 514 42 TRP HE1 H 10.272 0.020 1 402 514 42 TRP HE3 H 7.156 0.020 1 403 514 42 TRP HH2 H 7.311 0.020 1 404 514 42 TRP HZ2 H 7.480 0.020 1 405 514 42 TRP HZ3 H 7.023 0.020 1 406 514 42 TRP CA C 56.710 0.200 1 407 514 42 TRP CB C 29.879 0.200 1 408 514 42 TRP CD1 C 125.920 0.200 1 409 514 42 TRP CE3 C 119.239 0.200 1 410 514 42 TRP CH2 C 124.730 0.200 1 411 514 42 TRP CZ2 C 114.675 0.200 1 412 514 42 TRP CZ3 C 121.924 0.200 1 413 514 42 TRP N N 119.153 0.200 1 414 514 42 TRP NE1 N 130.105 0.200 1 415 515 43 TRP H H 9.492 0.020 1 416 515 43 TRP HA H 5.395 0.020 1 417 515 43 TRP HB2 H 2.998 0.020 2 418 515 43 TRP HB3 H 2.902 0.020 2 419 515 43 TRP HD1 H 7.210 0.020 1 420 515 43 TRP HE1 H 9.544 0.020 1 421 515 43 TRP HE3 H 7.166 0.020 1 422 515 43 TRP HH2 H 7.289 0.020 1 423 515 43 TRP HZ2 H 7.489 0.020 1 424 515 43 TRP HZ3 H 6.934 0.020 1 425 515 43 TRP CA C 55.294 0.200 1 426 515 43 TRP CB C 30.613 0.200 1 427 515 43 TRP CD1 C 125.109 0.200 1 428 515 43 TRP CE3 C 120.651 0.200 1 429 515 43 TRP CH2 C 124.452 0.200 1 430 515 43 TRP CZ2 C 114.675 0.200 1 431 515 43 TRP CZ3 C 121.924 0.200 1 432 515 43 TRP N N 126.683 0.200 1 433 515 43 TRP NE1 N 130.256 0.200 1 434 516 44 LYS H H 8.851 0.020 1 435 516 44 LYS HA H 4.353 0.020 1 436 516 44 LYS HB2 H 1.636 0.020 2 437 516 44 LYS HB3 H 1.419 0.020 2 438 516 44 LYS HD2 H 1.482 0.020 2 439 516 44 LYS HD3 H 1.423 0.020 2 440 516 44 LYS HE2 H 2.750 0.020 2 441 516 44 LYS HE3 H 2.665 0.020 2 442 516 44 LYS HG2 H 1.104 0.020 2 443 516 44 LYS HG3 H 0.528 0.020 2 444 516 44 LYS CA C 55.760 0.200 1 445 516 44 LYS CB C 33.882 0.200 1 446 516 44 LYS CD C 29.318 0.200 1 447 516 44 LYS CE C 42.139 0.200 1 448 516 44 LYS CG C 26.215 0.200 1 449 516 44 LYS N N 124.422 0.200 1 450 517 45 VAL H H 9.198 0.020 1 451 517 45 VAL HA H 5.490 0.020 1 452 517 45 VAL HB H 2.153 0.020 1 453 517 45 VAL HG1 H 0.919 0.020 1 454 517 45 VAL HG2 H 0.919 0.020 1 455 517 45 VAL CA C 58.988 0.200 1 456 517 45 VAL CB C 36.996 0.200 1 457 517 45 VAL CG1 C 21.608 0.200 2 458 517 45 VAL CG2 C 19.511 0.200 2 459 517 45 VAL N N 122.736 0.200 1 460 518 46 ARG H H 8.881 0.020 1 461 518 46 ARG HA H 5.541 0.020 1 462 518 46 ARG HB2 H 1.756 0.020 2 463 518 46 ARG HB3 H 1.587 0.020 2 464 518 46 ARG HD2 H 3.338 0.020 2 465 518 46 ARG HD3 H 3.274 0.020 2 466 518 46 ARG HE H 7.377 0.020 1 467 518 46 ARG HG2 H 2.013 0.020 2 468 518 46 ARG HG3 H 1.443 0.020 2 469 518 46 ARG CA C 53.957 0.200 1 470 518 46 ARG CB C 35.333 0.200 1 471 518 46 ARG CD C 44.178 0.200 1 472 518 46 ARG CG C 26.768 0.200 1 473 518 46 ARG N N 119.205 0.200 1 474 518 46 ARG NE N 116.324 0.200 1 475 519 47 ASP H H 9.145 0.020 1 476 519 47 ASP HA H 4.979 0.020 1 477 519 47 ASP HB2 H 3.413 0.020 2 478 519 47 ASP HB3 H 2.584 0.020 2 479 519 47 ASP CA C 53.033 0.200 1 480 519 47 ASP CB C 40.853 0.200 1 481 519 47 ASP N N 129.653 0.200 1 482 520 48 PRO HA H 4.526 0.020 1 483 520 48 PRO HB2 H 2.538 0.020 2 484 520 48 PRO HB3 H 1.957 0.020 2 485 520 48 PRO HD2 H 3.979 0.020 2 486 520 48 PRO HD3 H 3.881 0.020 2 487 520 48 PRO HG2 H 2.273 0.020 2 488 520 48 PRO HG3 H 2.212 0.020 2 489 520 48 PRO CA C 65.490 0.200 1 490 520 48 PRO CB C 31.970 0.200 1 491 520 48 PRO CD C 51.925 0.200 1 492 520 48 PRO CG C 28.236 0.200 1 493 521 49 ALA H H 7.900 0.020 1 494 521 49 ALA HA H 4.516 0.020 1 495 521 49 ALA HB H 1.562 0.020 1 496 521 49 ALA CA C 51.892 0.200 1 497 521 49 ALA CB C 18.990 0.200 1 498 521 49 ALA N N 118.719 0.200 1 499 522 50 GLY H H 8.545 0.020 1 500 522 50 GLY HA2 H 4.337 0.020 2 501 522 50 GLY HA3 H 3.546 0.020 2 502 522 50 GLY CA C 45.350 0.200 1 503 522 50 GLY N N 108.677 0.200 1 504 523 51 GLN H H 8.783 0.020 1 505 523 51 GLN HA H 4.324 0.020 1 506 523 51 GLN HB2 H 2.304 0.020 2 507 523 51 GLN HB3 H 2.061 0.020 2 508 523 51 GLN HG2 H 2.524 0.020 2 509 523 51 GLN HG3 H 2.215 0.020 2 510 523 51 GLN CA C 56.030 0.200 1 511 523 51 GLN CB C 29.640 0.200 1 512 523 51 GLN CG C 35.116 0.200 1 513 523 51 GLN N N 122.970 0.200 1 514 524 52 GLU H H 8.404 0.020 1 515 524 52 GLU HA H 5.797 0.020 1 516 524 52 GLU HB2 H 1.841 0.020 2 517 524 52 GLU HB3 H 1.701 0.020 2 518 524 52 GLU HG2 H 2.310 0.020 2 519 524 52 GLU HG3 H 2.012 0.020 2 520 524 52 GLU CA C 53.736 0.200 1 521 524 52 GLU CB C 34.114 0.200 1 522 524 52 GLU CG C 36.454 0.200 1 523 524 52 GLU N N 118.617 0.200 1 524 525 53 GLY H H 8.444 0.020 1 525 525 53 GLY HA2 H 4.044 0.020 1 526 525 53 GLY HA3 H 4.044 0.020 1 527 525 53 GLY CA C 45.524 0.200 1 528 525 53 GLY N N 106.330 0.200 1 529 526 54 TYR H H 8.913 0.020 1 530 526 54 TYR HA H 5.770 0.020 1 531 526 54 TYR HB2 H 3.153 0.020 2 532 526 54 TYR HB3 H 2.907 0.020 2 533 526 54 TYR HD1 H 7.140 0.020 3 534 526 54 TYR HD2 H 7.140 0.020 3 535 526 54 TYR HE1 H 6.938 0.020 3 536 526 54 TYR HE2 H 6.938 0.020 3 537 526 54 TYR CA C 59.049 0.200 1 538 526 54 TYR CB C 41.677 0.200 1 539 526 54 TYR CD1 C 133.007 0.200 3 540 526 54 TYR CD2 C 133.007 0.200 3 541 526 54 TYR CE1 C 118.078 0.200 3 542 526 54 TYR CE2 C 118.078 0.200 3 543 526 54 TYR N N 118.541 0.200 1 544 527 55 VAL H H 9.027 0.020 1 545 527 55 VAL HA H 4.665 0.020 1 546 527 55 VAL HB H 1.781 0.020 1 547 527 55 VAL HG1 H 1.125 0.020 1 548 527 55 VAL HG2 H 0.832 0.020 1 549 527 55 VAL CA C 58.159 0.200 1 550 527 55 VAL CB C 34.495 0.200 1 551 527 55 VAL CG1 C 23.224 0.200 1 552 527 55 VAL CG2 C 21.034 0.200 1 553 527 55 VAL N N 113.437 0.200 1 554 528 56 PRO HA H 3.475 0.020 1 555 528 56 PRO HB2 H 1.389 0.020 2 556 528 56 PRO HB3 H 1.162 0.020 2 557 528 56 PRO HD2 H 2.250 0.020 2 558 528 56 PRO HD3 H 2.148 0.020 2 559 528 56 PRO HG2 H 1.383 0.020 2 560 528 56 PRO HG3 H 0.891 0.020 2 561 528 56 PRO CA C 62.539 0.200 1 562 528 56 PRO CB C 31.250 0.200 1 563 528 56 PRO CD C 49.116 0.200 1 564 528 56 PRO CG C 27.284 0.200 1 565 529 57 TYR H H 7.756 0.020 1 566 529 57 TYR HA H 3.089 0.020 1 567 529 57 TYR HB2 H 1.985 0.020 2 568 529 57 TYR HB3 H 1.541 0.020 2 569 529 57 TYR HD1 H 6.933 0.020 3 570 529 57 TYR HD2 H 6.933 0.020 3 571 529 57 TYR HE1 H 6.725 0.020 3 572 529 57 TYR HE2 H 6.725 0.020 3 573 529 57 TYR CA C 59.515 0.200 1 574 529 57 TYR CB C 35.142 0.200 1 575 529 57 TYR CD1 C 133.217 0.200 1 576 529 57 TYR CD2 C 133.217 0.200 1 577 529 57 TYR CE1 C 117.724 0.200 1 578 529 57 TYR CE2 C 117.724 0.200 1 579 529 57 TYR N N 119.127 0.200 1 580 530 58 ASN H H 7.034 0.020 1 581 530 58 ASN HA H 3.780 0.020 1 582 530 58 ASN HB2 H 2.584 0.020 2 583 530 58 ASN HB3 H 1.723 0.020 2 584 530 58 ASN CA C 54.201 0.200 1 585 530 58 ASN CB C 36.586 0.200 1 586 530 58 ASN N N 113.481 0.200 1 587 531 59 ILE H H 6.586 0.020 1 588 531 59 ILE HA H 4.572 0.020 1 589 531 59 ILE HB H 2.355 0.020 1 590 531 59 ILE HD1 H 0.733 0.020 1 591 531 59 ILE HG12 H 1.318 0.020 2 592 531 59 ILE HG13 H 1.106 0.020 2 593 531 59 ILE HG2 H 0.645 0.020 1 594 531 59 ILE CA C 61.317 0.200 1 595 531 59 ILE CB C 38.091 0.200 1 596 531 59 ILE CD1 C 15.497 0.200 1 597 531 59 ILE CG1 C 24.651 0.200 1 598 531 59 ILE CG2 C 17.089 0.200 1 599 531 59 ILE N N 111.062 0.200 1 600 532 60 LEU H H 7.038 0.020 1 601 532 60 LEU HA H 5.227 0.020 1 602 532 60 LEU HB2 H 1.609 0.020 2 603 532 60 LEU HB3 H 1.039 0.020 2 604 532 60 LEU HD1 H 0.672 0.020 1 605 532 60 LEU HD2 H 0.672 0.020 1 606 532 60 LEU HG H 1.492 0.020 1 607 532 60 LEU CA C 53.315 0.200 1 608 532 60 LEU CB C 43.837 0.200 1 609 532 60 LEU CD1 C 22.937 0.200 2 610 532 60 LEU CD2 C 22.987 0.200 2 611 532 60 LEU CG C 26.144 0.200 1 612 532 60 LEU N N 120.917 0.200 1 613 533 61 THR H H 8.856 0.020 1 614 533 61 THR HA H 4.992 0.020 1 615 533 61 THR HB H 4.120 0.020 1 616 533 61 THR HG2 H 1.301 0.020 1 617 533 61 THR CA C 59.316 0.200 1 618 533 61 THR CB C 71.831 0.200 1 619 533 61 THR CG2 C 21.761 0.200 1 620 533 61 THR N N 116.469 0.200 1 621 534 62 PRO HA H 4.685 0.020 1 622 534 62 PRO HB2 H 2.567 0.020 2 623 534 62 PRO HB3 H 1.997 0.020 2 624 534 62 PRO HD2 H 4.009 0.020 2 625 534 62 PRO HD3 H 3.826 0.020 2 626 534 62 PRO HG2 H 2.255 0.020 2 627 534 62 PRO HG3 H 2.102 0.020 2 628 534 62 PRO CA C 64.349 0.200 1 629 534 62 PRO CB C 32.763 0.200 1 630 534 62 PRO CD C 51.811 0.200 1 631 534 62 PRO CG C 28.212 0.200 1 632 535 63 TYR H H 8.437 0.020 1 633 535 63 TYR HA H 4.964 0.020 1 634 535 63 TYR HB2 H 2.993 0.020 2 635 535 63 TYR HB3 H 2.853 0.020 2 636 535 63 TYR HD1 H 7.076 0.020 3 637 535 63 TYR HD2 H 7.076 0.020 3 638 535 63 TYR HE1 H 6.749 0.020 3 639 535 63 TYR HE2 H 6.749 0.020 3 640 535 63 TYR CA C 55.538 0.200 1 641 535 63 TYR CB C 40.337 0.200 1 642 535 63 TYR CD1 C 132.884 0.200 3 643 535 63 TYR CD2 C 132.884 0.200 3 644 535 63 TYR CE1 C 118.216 0.200 3 645 535 63 TYR CE2 C 118.216 0.200 3 646 535 63 TYR N N 125.786 0.200 1 647 536 64 PRO HA H 4.441 0.020 1 648 536 64 PRO HB2 H 2.177 0.020 2 649 536 64 PRO HB3 H 1.880 0.020 2 650 536 64 PRO HD2 H 3.658 0.020 2 651 536 64 PRO HD3 H 3.067 0.020 2 652 536 64 PRO HG2 H 1.884 0.020 2 653 536 64 PRO HG3 H 1.831 0.020 2 654 536 64 PRO CA C 63.410 0.200 1 655 536 64 PRO CB C 31.771 0.200 1 656 536 64 PRO CD C 50.839 0.200 1 657 536 64 PRO CG C 27.287 0.200 1 658 537 65 ALA H H 7.802 0.020 1 659 537 65 ALA HA H 4.150 0.020 1 660 537 65 ALA HB H 1.287 0.020 1 661 537 65 ALA CA C 52.225 0.200 1 662 537 65 ALA CB C 19.401 0.200 1 663 537 65 ALA N N 123.497 0.200 1 664 538 66 ALA H H 7.876 0.020 1 665 538 66 ALA HA H 4.184 0.020 1 666 538 66 ALA HB H 1.325 0.020 1 667 538 66 ALA CA C 52.225 0.200 1 668 538 66 ALA CB C 19.416 0.200 1 669 538 66 ALA N N 122.547 0.200 1 670 539 67 ALA H H 8.117 0.020 1 671 539 67 ALA HA H 4.349 0.020 1 672 539 67 ALA HB H 1.414 0.020 1 673 539 67 ALA CA C 52.501 0.200 1 674 539 67 ALA CB C 19.520 0.200 1 675 539 67 ALA N N 123.546 0.200 1 676 540 68 SER H H 7.852 0.020 1 677 540 68 SER CA C 59.914 0.200 1 678 540 68 SER CB C 64.945 0.200 1 679 540 68 SER N N 120.675 0.200 1 stop_ save_