data_4373 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89 ; _BMRB_accession_number 4373 _BMRB_flat_file_name bmr4373.str _Entry_type original _Submission_date 1999-07-29 _Accession_date 1999-07-30 _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 Blomberg Niklas . . 2 Sattler Michael . . 3 Nilges Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 577 "13C chemical shifts" 231 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-14 original author . stop_ _Original_release_date 2000-12-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Blomberg, N., Sattler, M., and Nilges, M., "1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89," J. Biomol. NMR 15, 269-270 (1999). ; _Citation_title '1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20142321 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blomberg Niklas . . 2 Sattler Michael . . 3 Nilges Michael . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 15 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 269 _Page_last 270 _Year 1999 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Bartels, C., T. Xia, M. Billeter, P. Guntert, and K. Wutrich, `The program {Xeasy} for computer -supported {NMR} spectral analysis of biological macromolecules', J. Biol. NMR, 6, 1-10 (1994). ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_citation_2 _Saveframe_category citation _Citation_full ; Delaglio, F., S. Greziek, G. Vuister, G. Zhu, J. Pfeifer, and A. Bax, `{NMRP}ipe: a multidimensional spectral processing program based on {UNIX} pipes.' J. Biomol., 6, 277-293 (1995). ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ ################################## # Molecular system description # ################################## save_system_UNC-89_PH_domain _Saveframe_category molecular_system _Mol_system_name 'UNC-89 PH domain' _Abbreviation_common UNC-89 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UNC-89 PH domain' $UNC-89_PH_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UNC-89_PH_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PH domain from C. elegans UNC-89 protein' _Abbreviation_common 'UNC-89 PH domain' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; GRIIRHDAFQVWEGDEPPKL RYVFLFRNKIMFTEQDASTS PPSYTHYSSIRLDKYNIRQH TTDEDTIVLQPQEPGLPSFR IKPKDFETSEYVRKAWLRDI AEEQEKYAAERD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 347 GLY 2 348 ARG 3 349 ILE 4 350 ILE 5 351 ARG 6 352 HIS 7 353 ASP 8 354 ALA 9 355 PHE 10 356 GLN 11 357 VAL 12 358 TRP 13 359 GLU 14 360 GLY 15 361 ASP 16 362 GLU 17 363 PRO 18 364 PRO 19 365 LYS 20 366 LEU 21 367 ARG 22 368 TYR 23 369 VAL 24 370 PHE 25 371 LEU 26 372 PHE 27 373 ARG 28 374 ASN 29 375 LYS 30 376 ILE 31 377 MET 32 378 PHE 33 379 THR 34 380 GLU 35 381 GLN 36 382 ASP 37 383 ALA 38 384 SER 39 385 THR 40 386 SER 41 387 PRO 42 388 PRO 43 389 SER 44 390 TYR 45 391 THR 46 392 HIS 47 393 TYR 48 394 SER 49 395 SER 50 396 ILE 51 397 ARG 52 398 LEU 53 399 ASP 54 400 LYS 55 401 TYR 56 402 ASN 57 403 ILE 58 404 ARG 59 405 GLN 60 406 HIS 61 407 THR 62 408 THR 63 409 ASP 64 410 GLU 65 411 ASP 66 412 THR 67 413 ILE 68 414 VAL 69 415 LEU 70 416 GLN 71 417 PRO 72 418 GLN 73 419 GLU 74 420 PRO 75 421 GLY 76 422 LEU 77 423 PRO 78 424 SER 79 425 PHE 80 426 ARG 81 427 ILE 82 428 LYS 83 429 PRO 84 430 LYS 85 431 ASP 86 432 PHE 87 433 GLU 88 434 THR 89 435 SER 90 436 GLU 91 437 TYR 92 438 VAL 93 439 ARG 94 440 LYS 95 441 ALA 96 442 TRP 97 443 LEU 98 444 ARG 99 445 ASP 100 446 ILE 101 447 ALA 102 448 GLU 103 449 GLU 104 450 GLN 105 451 GLU 106 452 LYS 107 453 TYR 108 454 ALA 109 455 ALA 110 456 GLU 111 457 ARG 112 458 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 1FHO "Solution Structure Of The Ph Domain From The C. Elegans Muscle Protein Unc-89" 100.00 119 100.00 100.00 7.47e-76 EMBL CCD63864 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 6632 100.00 100.00 5.48e-70 EMBL CCD63865 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 8081 100.00 100.00 1.37e-69 EMBL CCD63868 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 5992 100.00 100.00 1.17e-69 EMBL CCD63869 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 7441 100.00 100.00 2.70e-69 EMBL CCD63870 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 7122 100.00 100.00 1.02e-69 GB AAB00542 "UNC-89 [Caenorhabditis elegans]" 100.00 6632 100.00 100.00 5.92e-70 REF NP_001020984 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 6632 100.00 100.00 5.48e-70 REF NP_001020985 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 8081 100.00 100.00 1.37e-69 REF NP_001020988 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 5992 100.00 100.00 1.17e-69 REF NP_001020989 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 7441 100.00 100.00 2.70e-69 REF NP_001020990 "Muscle M-line assembly protein unc-89 [Caenorhabditis elegans]" 100.00 7122 100.00 100.00 1.02e-69 SP O01761 "RecName: Full=Muscle M-line assembly protein unc-89; AltName: Full=Uncoordinated protein 89" 100.00 8081 100.00 100.00 1.37e-69 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $UNC-89_PH_domain 'C. elegans' 6239 Eukaryota Metazoa Caenorhabditis elegans Bristol 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 $UNC-89_PH_domain 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $UNC-89_PH_domain . mM 0.6 0.8 '[U-13C; U-15N]' Pi 5 mM . . . NaCl 50 mM . . . d6-DMSO 16 % . . . stop_ save_ ############################ # Computer software used # ############################ save_XWIN-NMR _Saveframe_category software _Name XWIN-NMR _Version . loop_ _Task Acquisition stop_ _Details . save_ save_Xeasy _Saveframe_category software _Name Xeasy _Version . loop_ _Task 'Spectral analysis' stop_ _Details . _Citation_label $citation_1 save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task Processing stop_ _Details . _Citation_label $citation_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC NOESY' _Sample_label $sample_1 save_ save_1H-15N_HSQC_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC TOCSY' _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_1H-13C_HMQC_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HMQC NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_HNHA-J_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA-J _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_experimental_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.13 0.02 M pH 6.8 0.1 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP C 13 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel_to_Bo 0.25144954 TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel_to_Bo 1.00000000 TSP N 15 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel_to_Bo 0.10132900 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $experimental_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'UNC-89 PH 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 . 2 ARG H H 7.97 . 1 2 . 2 ARG HA H 4.25 . 1 3 . 2 ARG HB2 H 1.79 . 1 4 . 2 ARG HB3 H 1.79 . 1 5 . 2 ARG HG2 H 1.55 . 1 6 . 2 ARG HG3 H 1.55 . 1 7 . 2 ARG HD2 H 3.13 . 1 8 . 2 ARG HD3 H 3.13 . 1 9 . 2 ARG CA C 56.12 . 1 10 . 2 ARG CB C 30.89 . 1 11 . 2 ARG CG C 26.86 . 1 12 . 2 ARG CD C 43.39 . 1 13 . 2 ARG N N 121.07 . 1 14 . 3 ILE H H 8.33 . 1 15 . 3 ILE HA H 3.44 . 1 16 . 3 ILE HB H 1.62 . 1 17 . 3 ILE HG2 H 0.68 . 1 18 . 3 ILE CA C 61.9 . 1 19 . 3 ILE CB C 39.07 . 1 20 . 3 ILE CG2 C 18.91 . 1 21 . 3 ILE N N 125.59 . 1 22 . 4 ILE H H 8.95 . 1 23 . 4 ILE HA H 3.69 . 1 24 . 4 ILE HB H 1.22 . 1 25 . 4 ILE HG12 H 1.4 . 2 26 . 4 ILE HG13 H 0.92 . 2 27 . 4 ILE HG2 H 0.66 . 1 28 . 4 ILE HD1 H 0.58 . 1 29 . 4 ILE CA C 63.32 . 1 30 . 4 ILE CB C 37.82 . 1 31 . 4 ILE CG1 C 28.1 . 1 32 . 4 ILE CG2 C 17.49 . 1 33 . 4 ILE CD1 C 12.37 . 1 34 . 4 ILE N N 131.41 . 1 35 . 5 ARG H H 7.13 . 1 36 . 5 ARG HA H 4.23 . 1 37 . 5 ARG HB2 H 0.97 . 1 38 . 5 ARG HB3 H 0.97 . 1 39 . 5 ARG HG2 H 1.18 . 1 40 . 5 ARG HG3 H 1.18 . 1 41 . 5 ARG CA C 55.69 . 1 42 . 5 ARG CB C 33.18 . 1 43 . 5 ARG N N 116.86 . 1 44 . 6 HIS H H 7.77 . 1 45 . 6 HIS HA H 5.74 . 1 46 . 6 HIS HB2 H 2.58 . 2 47 . 6 HIS HB3 H 2.07 . 2 48 . 6 HIS HD2 H 6.48 . 1 49 . 6 HIS CA C 54.54 . 1 50 . 6 HIS CB C 32.03 . 1 51 . 6 HIS N N 120.34 . 1 52 . 7 ASP H H 8.52 . 1 53 . 7 ASP HA H 4.7 . 1 54 . 7 ASP HB2 H 2.27 . 2 55 . 7 ASP HB3 H 1.98 . 2 56 . 7 ASP CA C 54.33 . 1 57 . 7 ASP N N 121.54 . 1 58 . 8 ALA H H 8.7 . 1 59 . 8 ALA HA H 4.63 . 1 60 . 8 ALA HB H 1.08 . 1 61 . 8 ALA CA C 50.93 . 1 62 . 8 ALA CB C 19.61 . 1 63 . 8 ALA N N 122.51 . 1 64 . 9 PHE H H 8.87 . 1 65 . 9 PHE HA H 4.74 . 1 66 . 9 PHE HB2 H 2.72 . 2 67 . 9 PHE HB3 H 2.18 . 2 68 . 9 PHE HD1 H 6.48 . 1 69 . 9 PHE HD2 H 6.48 . 1 70 . 9 PHE HE1 H 6.25 . 1 71 . 9 PHE HE2 H 6.25 . 1 72 . 9 PHE CA C 56.87 . 1 73 . 9 PHE CB C 42.94 . 1 74 . 9 PHE N N 120.52 . 1 75 . 10 GLN H H 9.26 . 1 76 . 10 GLN HA H 4.34 . 1 77 . 10 GLN HB2 H 1.74 . 2 78 . 10 GLN HB3 H 1.44 . 2 79 . 10 GLN HG2 H 1.92 . 1 80 . 10 GLN HG3 H 1.92 . 1 81 . 10 GLN CA C 56.33 . 1 82 . 10 GLN CB C 30.19 . 1 83 . 10 GLN N N 121.1 . 1 84 . 11 VAL H H 8.88 . 1 85 . 11 VAL HA H 4.97 . 1 86 . 11 VAL HB H 1.94 . 1 87 . 11 VAL HG1 H 0.85 . 1 88 . 11 VAL HG2 H 0.74 . 1 89 . 11 VAL CA C 61.64 . 1 90 . 11 VAL CB C 34.63 . 1 91 . 11 VAL CG1 C 22.08 . 1 92 . 11 VAL CG2 C 21.59 . 1 93 . 11 VAL N N 124.59 . 1 94 . 12 TRP H H 9.83 . 1 95 . 12 TRP HA H 4.5 . 1 96 . 12 TRP HB2 H 3.31 . 2 97 . 12 TRP HB3 H 3.24 . 2 98 . 12 TRP HD1 H 7.44 . 1 99 . 12 TRP HE1 H 10.25 . 1 100 . 12 TRP HE3 H 7.7 . 1 101 . 12 TRP HZ2 H 7.37 . 1 102 . 12 TRP HZ3 H 6.82 . 1 103 . 12 TRP HH2 H 6.91 . 1 104 . 12 TRP CA C 58.72 . 1 105 . 12 TRP N N 132.96 . 1 106 . 12 TRP NE1 N 131.16 . 1 107 . 13 GLU H H 8.69 . 1 108 . 13 GLU HA H 4.57 . 1 109 . 13 GLU HB2 H 1.84 . 2 110 . 13 GLU HB3 H 1.66 . 2 111 . 13 GLU HG2 H 2.08 . 1 112 . 13 GLU HG3 H 2.08 . 1 113 . 13 GLU CA C 54.11 . 1 114 . 13 GLU CB C 31.16 . 1 115 . 13 GLU N N 129.58 . 1 116 . 14 GLY H H 8.51 . 1 117 . 14 GLY HA2 H 3.66 . 2 118 . 14 GLY HA3 H 3.85 . 2 119 . 14 GLY CA C 47.39 . 1 120 . 14 GLY N N 116.05 . 1 121 . 15 ASP H H 9.01 . 1 122 . 15 ASP HA H 4.89 . 1 123 . 15 ASP HB2 H 2.89 . 2 124 . 15 ASP HB3 H 2.47 . 2 125 . 15 ASP CA C 53.89 . 1 126 . 15 ASP CB C 41.24 . 1 127 . 15 ASP N N 128.88 . 1 128 . 16 GLU H H 8.28 . 1 129 . 16 GLU HA H 4.43 . 1 130 . 16 GLU HB2 H 2.29 . 2 131 . 16 GLU HB3 H 2.14 . 2 132 . 16 GLU HG2 H 2.44 . 2 133 . 16 GLU HG3 H 2.29 . 2 134 . 16 GLU CA C 56.05 . 1 135 . 16 GLU CB C 29.21 . 1 136 . 16 GLU CG C 36.45 . 1 137 . 16 GLU N N 122.41 . 1 138 . 18 PRO HA H 4.1 . 1 139 . 18 PRO HB2 H 0.79 . 2 140 . 18 PRO HB3 H -0.29 . 2 141 . 18 PRO CA C 62.21 . 1 142 . 18 PRO CB C 30.5 . 1 143 . 19 LYS H H 8.15 . 1 144 . 19 LYS HA H 4.49 . 1 145 . 19 LYS HB2 H 1.58 . 2 146 . 19 LYS HB3 H 1.43 . 2 147 . 19 LYS HG2 H 1.31 . 1 148 . 19 LYS HG3 H 1.31 . 1 149 . 19 LYS CA C 53.72 . 1 150 . 19 LYS N N 119.32 . 1 151 . 20 LEU H H 8.52 . 1 152 . 20 LEU HA H 4.75 . 1 153 . 20 LEU HB2 H 1.66 . 2 154 . 20 LEU HB3 H 1.53 . 2 155 . 20 LEU HD1 H 0.81 . 1 156 . 20 LEU HD2 H 0.73 . 1 157 . 20 LEU CA C 54.95 . 1 158 . 20 LEU CB C 41.71 . 1 159 . 20 LEU N N 125.61 . 1 160 . 21 ARG H H 9.21 . 1 161 . 21 ARG HA H 5.14 . 1 162 . 21 ARG HB2 H 1.74 . 1 163 . 21 ARG HB3 H 1.74 . 1 164 . 21 ARG CA C 53.41 . 1 165 . 21 ARG CB C 34.45 . 1 166 . 21 ARG N N 126.03 . 1 167 . 22 TYR H H 9.03 . 1 168 . 22 TYR HB2 H 2.86 . 1 169 . 22 TYR HB3 H 2.86 . 1 170 . 22 TYR HD1 H 6.77 . 1 171 . 22 TYR HD2 H 6.77 . 1 172 . 22 TYR HE1 H 6.90 . 1 173 . 22 TYR HE2 H 6.90 . 1 174 . 22 TYR N N 126.02 . 1 175 . 23 VAL H H 8.86 . 1 176 . 23 VAL HA H 4.84 . 1 177 . 23 VAL HB H 1.72 . 1 178 . 23 VAL HG1 H 0.63 . 1 179 . 23 VAL HG2 H 0.19 . 1 180 . 23 VAL CA C 61.62 . 1 181 . 23 VAL CB C 32.82 . 1 182 . 23 VAL CG1 C 23.64 . 1 183 . 23 VAL CG2 C 22.81 . 1 184 . 23 VAL N N 133.17 . 1 185 . 24 PHE H H 9.04 . 1 186 . 24 PHE HA H 5.06 . 1 187 . 24 PHE HB2 H 2.99 . 2 188 . 24 PHE HB3 H 2.5 . 2 189 . 24 PHE HD1 H 7.00 . 1 190 . 24 PHE HD2 H 7.00 . 1 191 . 24 PHE HE1 H 7.11 . 1 192 . 24 PHE HE2 H 7.11 . 1 193 . 24 PHE HZ H 6.03 . 1 194 . 24 PHE CA C 56.4 . 1 195 . 24 PHE CB C 44.21 . 1 196 . 24 PHE N N 124.62 . 1 197 . 25 LEU H H 8.7 . 1 198 . 25 LEU HA H 4.95 . 1 199 . 25 LEU HB2 H 1.18 . 2 200 . 25 LEU HB3 H 0.95 . 2 201 . 25 LEU HG H 0.93 . 1 202 . 25 LEU HD1 H 0.25 . 4 203 . 25 LEU HD2 H 0.25 . 4 204 . 25 LEU CA C 54.02 . 1 205 . 25 LEU CB C 43.67 . 1 206 . 25 LEU CG C 24.32 . 1 207 . 25 LEU CD1 C 26.42 . 4 208 . 25 LEU CD2 C 26.42 . 4 209 . 25 LEU N N 125.65 . 1 210 . 26 PHE H H 9.04 . 1 211 . 26 PHE HA H 4.88 . 1 212 . 26 PHE HB2 H 3.34 . 2 213 . 26 PHE HB3 H 2.74 . 2 214 . 26 PHE HD1 H 7.00 . 1 215 . 26 PHE HD2 H 7.00 . 1 216 . 26 PHE HE1 H 6.96 . 1 217 . 26 PHE HE2 H 6.96 . 1 218 . 26 PHE HZ H 6.63 . 1 219 . 26 PHE N N 126.52 . 1 220 . 28 ASN HA H 4.66 . 1 221 . 29 LYS H H 7.86 . 1 222 . 29 LYS HA H 5.37 . 1 223 . 29 LYS HB2 H 1.71 . 2 224 . 29 LYS HB3 H 1.53 . 2 225 . 29 LYS HG2 H 0.91 . 1 226 . 29 LYS HG3 H 0.91 . 1 227 . 29 LYS HD2 H 0.68 . 1 228 . 29 LYS HD3 H 0.68 . 1 229 . 29 LYS HE2 H 2.65 . 1 230 . 29 LYS HE3 H 2.65 . 1 231 . 29 LYS CA C 56.0 . 1 232 . 29 LYS CB C 36.9 . 1 233 . 29 LYS N N 121.77 . 1 234 . 30 ILE H H 8.14 . 1 235 . 30 ILE HA H 4.98 . 1 236 . 30 ILE HB H 1.08 . 1 237 . 30 ILE HG2 H -0.02 . 1 238 . 30 ILE HD1 H 0.59 . 1 239 . 30 ILE CA C 60.1 . 1 240 . 30 ILE CB C 40.71 . 1 241 . 30 ILE CG2 C 17.89 . 1 242 . 30 ILE CD1 C 13.75 . 1 243 . 30 ILE N N 123.67 . 1 244 . 31 MET H H 9.23 . 1 245 . 31 MET HA H 5.18 . 1 246 . 31 MET HB2 H 2.48 . 2 247 . 31 MET HB3 H 2.31 . 2 248 . 31 MET HG2 H 1.92 . 1 249 . 31 MET HG3 H 1.92 . 1 250 . 31 MET CA C 54.28 . 1 251 . 31 MET CB C 31.71 . 1 252 . 31 MET N N 127.71 . 1 253 . 32 PHE H H 9.56 . 1 254 . 32 PHE HA H 4.8 . 1 255 . 32 PHE HB2 H 3.33 . 2 256 . 32 PHE HB3 H 2.77 . 2 257 . 32 PHE HD1 H 6.83 . 1 258 . 32 PHE HD2 H 6.83 . 1 259 . 32 PHE HE1 H 6.77 . 1 260 . 32 PHE HE2 H 6.77 . 1 261 . 32 PHE N N 125.35 . 1 262 . 33 THR H H 8.58 . 1 263 . 33 THR HA H 5.67 . 1 264 . 33 THR HB H 4.39 . 1 265 . 33 THR HG2 H 1.17 . 1 266 . 33 THR CA C 60.93 . 1 267 . 33 THR CB C 73.09 . 1 268 . 33 THR CG2 C 22.23 . 1 269 . 33 THR N N 115.6 . 1 270 . 34 GLU H H 8.96 . 1 271 . 34 GLU HA H 5.06 . 1 272 . 34 GLU HB2 H 2.19 . 2 273 . 34 GLU HB3 H 2.0 . 2 274 . 34 GLU HG2 H 2.82 . 1 275 . 34 GLU HG3 H 2.82 . 1 276 . 34 GLU CA C 55.13 . 1 277 . 34 GLU CB C 33.38 . 1 278 . 34 GLU N N 120.96 . 1 279 . 35 GLN H H 9.08 . 1 280 . 35 GLN HB2 H 2.03 . 2 281 . 35 GLN HB3 H 2.33 . 2 282 . 35 GLN CB C 31.69 . 1 283 . 35 GLN N N 126.8 . 1 284 . 36 ASP H H 8.9 . 1 285 . 36 ASP HA H 4.7 . 1 286 . 36 ASP HB2 H 2.8 . 2 287 . 36 ASP HB3 H 2.42 . 2 288 . 36 ASP CB C 40.7 . 1 289 . 36 ASP N N 128.74 . 1 290 . 37 ALA H H 8.62 . 1 291 . 37 ALA HA H 4.33 . 1 292 . 37 ALA HB H 1.35 . 1 293 . 37 ALA CA C 51.67 . 1 294 . 37 ALA CB C 18.15 . 1 295 . 37 ALA N N 127.55 . 1 296 . 38 SER H H 8.7 . 1 297 . 38 SER HA H 4.22 . 1 298 . 38 SER HB2 H 3.91 . 2 299 . 38 SER HB3 H 3.83 . 2 300 . 38 SER CA C 60.3 . 1 301 . 38 SER CB C 63.34 . 1 302 . 38 SER N N 116.32 . 1 303 . 39 THR H H 6.97 . 1 304 . 39 THR HA H 4.38 . 1 305 . 39 THR HB H 4.16 . 1 306 . 39 THR CA C 59.68 . 1 307 . 39 THR CB C 68.72 . 1 308 . 39 THR CG2 C 20.5 . 1 309 . 39 THR N N 112.14 . 1 310 . 40 SER H H 8.21 . 1 311 . 40 SER HB2 H 3.70 . 1 312 . 40 SER HB3 H 3.70 . 1 313 . 40 SER CB C 64.68 . 1 314 . 40 SER N N 116.4 . 1 315 . 42 PRO HG2 H 1.90 . 1 316 . 42 PRO HG3 H 1.90 . 1 317 . 42 PRO HD2 H 4.43 . 1 318 . 42 PRO HD3 H 4.43 . 1 319 . 43 SER H H 7.94 . 1 320 . 43 SER HA H 4.61 . 1 321 . 43 SER HB2 H 3.76 . 1 322 . 43 SER HB3 H 3.76 . 1 323 . 43 SER CA C 56.6 . 1 324 . 43 SER CB C 65.42 . 1 325 . 43 SER N N 117.07 . 1 326 . 44 TYR H H 8.59 . 1 327 . 44 TYR HA H 5.19 . 1 328 . 44 TYR HB2 H 2.85 . 1 329 . 44 TYR HB3 H 2.71 . 1 330 . 44 TYR HD1 H 7.00 . 1 331 . 44 TYR HD2 H 7.00 . 1 332 . 44 TYR HE1 H 6.81 . 1 333 . 44 TYR HE2 H 6.81 . 1 334 . 44 TYR CA C 57.65 . 1 335 . 44 TYR CB C 40.3 . 1 336 . 44 TYR N N 120.91 . 1 337 . 47 TYR HA H 4.69 . 1 338 . 47 TYR HB2 H 2.95 . 2 339 . 47 TYR HB3 H 2.76 . 2 340 . 47 TYR HD1 H 6.82 . 1 341 . 47 TYR HD2 H 6.82 . 1 342 . 47 TYR HE1 H 7.13 . 1 343 . 47 TYR HE2 H 7.13 . 1 344 . 47 TYR CA C 59.74 . 1 345 . 47 TYR CB C 39.58 . 1 346 . 48 SER H H 8.88 . 1 347 . 48 SER HA H 4.42 . 1 348 . 48 SER CA C 58.17 . 1 349 . 48 SER N N 120.55 . 1 350 . 49 SER H H 8.69 . 1 351 . 49 SER HA H 5.71 . 1 352 . 49 SER HB2 H 3.79 . 1 353 . 49 SER HB3 H 3.71 . 1 354 . 49 SER CA C 57.78 . 1 355 . 49 SER CB C 66.83 . 1 356 . 49 SER N N 119.3 . 1 357 . 50 ILE H H 8.96 . 1 358 . 50 ILE HA H 4.8 . 1 359 . 50 ILE HB H 1.73 . 1 360 . 50 ILE HG2 H 0.81 . 1 361 . 50 ILE HD1 H -0.05 . 1 362 . 50 ILE CA C 59.02 . 1 363 . 50 ILE CB C 41.1 . 1 364 . 50 ILE CG2 C 18.58 . 1 365 . 50 ILE CD1 C 12.81 . 1 366 . 50 ILE N N 117.41 . 1 367 . 51 ARG H H 8.6 . 1 368 . 51 ARG HA H 4.65 . 1 369 . 51 ARG HB2 H 1.8 . 2 370 . 51 ARG HB3 H 1.73 . 2 371 . 51 ARG HG2 H 2.24 . 1 372 . 51 ARG HG3 H 2.24 . 1 373 . 51 ARG HD2 H 3.1 . 1 374 . 51 ARG HD3 H 3.1 . 1 375 . 51 ARG CA C 54.98 . 1 376 . 51 ARG CB C 31.55 . 1 377 . 51 ARG N N 124.38 . 1 378 . 52 LEU H H 7.38 . 1 379 . 52 LEU HA H 3.93 . 1 380 . 52 LEU HB2 H 1.53 . 2 381 . 52 LEU HB3 H 1.48 . 2 382 . 52 LEU HG H 0.86 . 1 383 . 52 LEU HD1 H 0.72 . 4 384 . 52 LEU HD2 H 0.72 . 4 385 . 52 LEU CA C 57.71 . 1 386 . 52 LEU CB C 41.86 . 1 387 . 52 LEU CG C 25.52 . 1 388 . 52 LEU CD1 C 23.63 . 4 389 . 52 LEU CD2 C 23.63 . 4 390 . 52 LEU N N 123.94 . 1 391 . 53 ASP H H 8.72 . 1 392 . 53 ASP HA H 4.49 . 1 393 . 53 ASP HB2 H 2.8 . 2 394 . 53 ASP HB3 H 2.4 . 2 395 . 53 ASP CA C 55.22 . 1 396 . 53 ASP CB C 39.23 . 1 397 . 53 ASP N N 117.11 . 1 398 . 54 LYS H H 7.35 . 1 399 . 54 LYS HA H 4.49 . 1 400 . 54 LYS HB2 H 1.96 . 1 401 . 54 LYS HB3 H 1.96 . 1 402 . 54 LYS HG2 H 1.49 . 1 403 . 54 LYS HG3 H 1.49 . 1 404 . 54 LYS CA C 54.38 . 1 405 . 54 LYS CB C 32.99 . 1 406 . 54 LYS CG C 24.79 . 1 407 . 54 LYS N N 117.43 . 1 408 . 55 TYR H H 7.67 . 1 409 . 55 TYR HA H 4.8 . 1 410 . 55 TYR HB2 H 2.7 . 2 411 . 55 TYR HB3 H 2.5 . 2 412 . 55 TYR HD1 H 7.05 . 1 413 . 55 TYR HD2 H 7.05 . 1 414 . 55 TYR HE1 H 6.82 . 1 415 . 55 TYR HE2 H 6.82 . 1 416 . 55 TYR CA C 57.85 . 1 417 . 55 TYR CB C 42.97 . 1 418 . 55 TYR N N 119.46 . 1 419 . 56 ASN H H 9.28 . 1 420 . 56 ASN HA H 5.08 . 1 421 . 56 ASN HB2 H 2.70 . 1 422 . 56 ASN HB3 H 2.70 . 1 423 . 56 ASN CA C 52.23 . 1 424 . 56 ASN CB C 40.46 . 1 425 . 56 ASN N N 121.07 . 1 426 . 57 ILE H H 8.97 . 1 427 . 57 ILE HA H 5.27 . 1 428 . 57 ILE HB H 1.75 . 1 429 . 57 ILE HG12 H 1.57 . 2 430 . 57 ILE HG13 H 1.54 . 2 431 . 57 ILE HG2 H 0.82 . 1 432 . 57 ILE HD1 H 1.11 . 1 433 . 57 ILE CA C 60.5 . 1 434 . 57 ILE CB C 39.48 . 1 435 . 57 ILE CG1 C 28.51 . 1 436 . 57 ILE CG2 C 18.14 . 1 437 . 57 ILE N N 127.46 . 1 438 . 58 ARG H H 8.7 . 1 439 . 58 ARG HA H 4.78 . 1 440 . 58 ARG HB2 H 1.98 . 2 441 . 58 ARG HB3 H 1.73 . 2 442 . 58 ARG HG2 H 1.51 . 2 443 . 58 ARG HG3 H 1.4 . 2 444 . 58 ARG HD2 H 3.17 . 1 445 . 58 ARG HD3 H 3.17 . 1 446 . 58 ARG CA C 54.07 . 1 447 . 58 ARG CB C 33.7 . 1 448 . 58 ARG N N 124.73 . 1 449 . 59 GLN H H 8.79 . 1 450 . 59 GLN HA H 4.51 . 1 451 . 59 GLN HB2 H 2.06 . 1 452 . 59 GLN HB3 H 2.06 . 1 453 . 59 GLN CA C 56.06 . 1 454 . 59 GLN CB C 30.34 . 1 455 . 59 GLN N N 122.53 . 1 456 . 60 HIS H H 8.69 . 1 457 . 60 HIS HA H 4.21 . 1 458 . 60 HIS HB2 H 3.7 . 2 459 . 60 HIS HB3 H 2.61 . 2 460 . 60 HIS HD2 H 6.71 . 1 461 . 60 HIS CA C 58.11 . 1 462 . 60 HIS CB C 31.7 . 1 463 . 60 HIS N N 128.44 . 1 464 . 61 THR H H 7.51 . 1 465 . 61 THR HA H 3.95 . 1 466 . 61 THR HB H 4.03 . 1 467 . 61 THR HG2 H 1.14 . 1 468 . 61 THR CA C 64.64 . 1 469 . 61 THR CB C 69.38 . 1 470 . 61 THR CG2 C 22.12 . 1 471 . 61 THR N N 117.5 . 1 472 . 62 THR H H 8.68 . 1 473 . 62 THR HA H 4.52 . 1 474 . 62 THR HB H 4.23 . 1 475 . 62 THR HG2 H 1.12 . 1 476 . 62 THR CA C 62.68 . 1 477 . 62 THR CB C 69.97 . 1 478 . 62 THR CG2 C 21.57 . 1 479 . 62 THR N N 113.62 . 1 480 . 63 ASP H H 8.76 . 1 481 . 63 ASP HA H 4.72 . 1 482 . 63 ASP HB2 H 2.34 . 2 483 . 63 ASP HB3 H 2.16 . 2 484 . 63 ASP CA C 53.3 . 1 485 . 63 ASP CB C 40.72 . 1 486 . 63 ASP N N 126.8 . 1 487 . 64 GLU H H 8.4 . 1 488 . 64 GLU HA H 4.07 . 1 489 . 64 GLU HB2 H 1.95 . 1 490 . 64 GLU HB3 H 1.95 . 1 491 . 64 GLU HG2 H 2.22 . 1 492 . 64 GLU HG3 H 2.22 . 1 493 . 64 GLU CA C 58.6 . 1 494 . 64 GLU CB C 30.12 . 1 495 . 64 GLU CG C 36.49 . 1 496 . 64 GLU N N 124.12 . 1 497 . 65 ASP H H 7.86 . 1 498 . 65 ASP HA H 4.68 . 1 499 . 65 ASP HB2 H 2.8 . 2 500 . 65 ASP HB3 H 2.57 . 2 501 . 65 ASP CB C 41.36 . 1 502 . 65 ASP N N 116.1 . 1 503 . 66 THR H H 7.65 . 1 504 . 66 THR HA H 4.8 . 1 505 . 66 THR HB H 3.97 . 1 506 . 66 THR HG2 H 0.90 . 1 507 . 66 THR CA C 62.66 . 1 508 . 66 THR CB C 69.69 . 1 509 . 66 THR CG2 C 21.71 . 1 510 . 66 THR N N 115.21 . 1 511 . 67 ILE H H 9.21 . 1 512 . 67 ILE HA H 4.34 . 1 513 . 67 ILE HB H 1.66 . 1 514 . 67 ILE HG2 H 0.70 . 1 515 . 67 ILE HD1 H 0.86 . 1 516 . 67 ILE CA C 60.98 . 1 517 . 67 ILE CB C 34.65 . 1 518 . 67 ILE CG2 C 17.65 . 1 519 . 67 ILE N N 128.64 . 1 520 . 68 VAL H H 9.33 . 1 521 . 68 VAL HA H 4.51 . 1 522 . 68 VAL HB H 2.04 . 1 523 . 68 VAL HG1 H 0.98 . 1 524 . 68 VAL HG2 H 0.83 . 1 525 . 68 VAL CA C 61.84 . 1 526 . 68 VAL CB C 33.51 . 1 527 . 68 VAL CG1 C 21.49 . 1 528 . 68 VAL N N 128.8 . 1 529 . 69 LEU H H 8.96 . 1 530 . 69 LEU HA H 4.84 . 1 531 . 69 LEU HB2 H 2.08 . 2 532 . 69 LEU HB3 H 1.43 . 2 533 . 69 LEU HG H 1.55 . 1 534 . 69 LEU HD1 H 0.70 . 1 535 . 69 LEU HD2 H 0.55 . 1 536 . 69 LEU CA C 54.68 . 1 537 . 69 LEU CB C 41.44 . 1 538 . 69 LEU CD1 C 26.34 . 1 539 . 69 LEU CD2 C 27.01 . 1 540 . 69 LEU N N 127.86 . 1 541 . 70 GLN H H 9.03 . 1 542 . 70 GLN HA H 5.25 . 1 543 . 70 GLN HB2 H 2.19 . 2 544 . 70 GLN HB3 H 2.0 . 2 545 . 70 GLN HG2 H 2.70 . 1 546 . 70 GLN HG3 H 2.70 . 1 547 . 70 GLN N N 126.08 . 1 548 . 71 PRO HA H 3.61 . 1 549 . 71 PRO HB2 H 1.97 . 2 550 . 71 PRO HB3 H 1.67 . 2 551 . 71 PRO CA C 62.56 . 1 552 . 71 PRO CB C 33.36 . 1 553 . 72 GLN H H 8.46 . 1 554 . 72 GLN HB2 H 2.14 . 2 555 . 72 GLN HB3 H 2.02 . 2 556 . 72 GLN HG2 H 3.63 . 2 557 . 72 GLN HG3 H 3.60 . 2 558 . 72 GLN N N 118.36 . 1 559 . 73 GLU H H 7.05 . 1 560 . 73 GLU HA H 4.79 . 1 561 . 73 GLU HB2 H 2.02 . 2 562 . 73 GLU HB3 H 1.77 . 2 563 . 73 GLU HG2 H 2.15 . 1 564 . 73 GLU HG3 H 2.15 . 1 565 . 73 GLU CA C 52.58 . 1 566 . 73 GLU CB C 31.81 . 1 567 . 73 GLU N N 117.96 . 1 568 . 74 PRO HD2 H 3.78 . 1 569 . 74 PRO HD3 H 3.78 . 1 570 . 74 PRO CD C 50.42 . 1 571 . 75 GLY HA2 H 4.12 . 2 572 . 75 GLY HA3 H 3.66 . 2 573 . 75 GLY CA C 45.31 . 1 574 . 76 LEU H H 7.03 . 1 575 . 76 LEU HA H 4.8 . 1 576 . 76 LEU HB2 H 1.92 . 2 577 . 76 LEU HB3 H 1.5 . 2 578 . 76 LEU HG H 1.65 . 1 579 . 76 LEU HD1 H 1.01 . 1 580 . 76 LEU HD2 H 0.90 . 1 581 . 76 LEU CB C 42.5 . 1 582 . 76 LEU CG C 27.61 . 1 583 . 76 LEU CD1 C 22.68 . 1 584 . 76 LEU CD2 C 26.39 . 1 585 . 76 LEU N N 122.06 . 1 586 . 77 PRO HA H 4.46 . 1 587 . 77 PRO HB2 H 2.05 . 2 588 . 77 PRO HB3 H 1.35 . 2 589 . 77 PRO HD2 H 3.80 . 1 590 . 77 PRO HD3 H 3.80 . 1 591 . 77 PRO CA C 62.38 . 1 592 . 77 PRO CB C 31.77 . 1 593 . 78 SER H H 8.46 . 1 594 . 78 SER HA H 5.02 . 1 595 . 78 SER CA C 57.27 . 1 596 . 78 SER CB C 65.23 . 1 597 . 78 SER N N 117.2 . 1 598 . 79 PHE H H 8.45 . 1 599 . 79 PHE HA H 5.88 . 1 600 . 79 PHE HB2 H 2.80 . 1 601 . 79 PHE HB3 H 2.80 . 1 602 . 79 PHE HD1 H 6.82 . 1 603 . 79 PHE HD2 H 6.82 . 1 604 . 79 PHE HE1 H 6.28 . 1 605 . 79 PHE HE2 H 6.28 . 1 606 . 79 PHE HZ H 5.88 . 1 607 . 79 PHE CA C 56.53 . 1 608 . 79 PHE CB C 45.07 . 1 609 . 79 PHE CZ C 61.86 . 1 610 . 79 PHE N N 118.08 . 1 611 . 80 ARG H H 8.99 . 1 612 . 80 ARG HA H 5.4 . 1 613 . 80 ARG HB2 H 1.78 . 2 614 . 80 ARG HB3 H 1.53 . 2 615 . 80 ARG HG2 H 1.74 . 1 616 . 80 ARG HG3 H 1.74 . 1 617 . 80 ARG HD2 H 2.81 . 1 618 . 80 ARG HD3 H 2.81 . 1 619 . 80 ARG CA C 55.52 . 1 620 . 80 ARG CB C 33.81 . 1 621 . 80 ARG CG C 28.13 . 1 622 . 80 ARG N N 121.95 . 1 623 . 81 ILE H H 9.44 . 1 624 . 81 ILE HA H 6.08 . 1 625 . 81 ILE HB H 1.45 . 1 626 . 81 ILE HG12 H 0.84 . 1 627 . 81 ILE HG13 H 0.84 . 1 628 . 81 ILE HG2 H 0.74 . 1 629 . 81 ILE HD1 H -0.66 . 1 630 . 81 ILE CA C 59.01 . 1 631 . 81 ILE CB C 40.31 . 1 632 . 81 ILE CG2 C 18.31 . 1 633 . 81 ILE CD1 C 20.09 . 1 634 . 81 ILE N N 117.33 . 1 635 . 82 LYS H H 9.36 . 1 636 . 82 LYS HA H 5.54 . 1 637 . 82 LYS HB2 H 2.03 . 2 638 . 82 LYS HB3 H 1.96 . 2 639 . 82 LYS HG2 H 1.76 . 1 640 . 82 LYS HG3 H 1.76 . 1 641 . 82 LYS HE2 H 2.72 . 1 642 . 82 LYS HE3 H 2.72 . 1 643 . 82 LYS CA C 53.16 . 1 644 . 82 LYS CB C 39.11 . 1 645 . 82 LYS N N 126.54 . 1 646 . 83 PRO HA H 3.57 . 1 647 . 83 PRO HB2 H 2.09 . 2 648 . 83 PRO HB3 H 1.59 . 2 649 . 83 PRO HD2 H 3.60 . 1 650 . 83 PRO HD3 H 3.60 . 1 651 . 83 PRO CA C 63.89 . 1 652 . 83 PRO CB C 32.81 . 1 653 . 84 LYS H H 7.6 . 1 654 . 84 LYS HA H 3.85 . 1 655 . 84 LYS HB2 H 1.4 . 2 656 . 84 LYS HB3 H 1.23 . 2 657 . 84 LYS HG2 H 1.63 . 1 658 . 84 LYS HG3 H 1.63 . 1 659 . 84 LYS CA C 58.62 . 1 660 . 84 LYS CB C 33.5 . 1 661 . 84 LYS CG C 24.38 . 1 662 . 84 LYS N N 124.84 . 1 663 . 85 ASP H H 8.05 . 1 664 . 85 ASP HA H 4.69 . 1 665 . 85 ASP HB2 H 2.69 . 2 666 . 85 ASP HB3 H 2.44 . 2 667 . 85 ASP CA C 53.72 . 1 668 . 85 ASP CB C 41.06 . 1 669 . 85 ASP N N 118.09 . 1 670 . 86 PHE H H 8.59 . 1 671 . 86 PHE HA H 4.31 . 1 672 . 86 PHE HB2 H 3.30 . 2 673 . 86 PHE HB3 H 3.06 . 2 674 . 86 PHE HD1 H 7.25 . 1 675 . 86 PHE HD2 H 7.25 . 1 676 . 86 PHE HE1 H 7.26 . 1 677 . 86 PHE HE2 H 7.26 . 1 678 . 86 PHE CA C 60.45 . 1 679 . 86 PHE CB C 39.13 . 1 680 . 86 PHE N N 127.63 . 1 681 . 87 GLU H H 9.02 . 1 682 . 87 GLU N N 120.14 . 1 683 . 88 THR H H 6.97 . 1 684 . 88 THR HA H 4.68 . 1 685 . 88 THR HB H 4.72 . 1 686 . 88 THR HG2 H 1.08 . 1 687 . 88 THR CA C 60.22 . 1 688 . 88 THR CB C 69.12 . 1 689 . 88 THR N N 131.78 . 1 690 . 89 SER H H 7.14 . 1 691 . 89 SER HA H 4.27 . 1 692 . 89 SER HB2 H 3.87 . 1 693 . 89 SER HB3 H 3.87 . 1 694 . 89 SER CA C 61.82 . 1 695 . 89 SER CB C 62.86 . 1 696 . 89 SER N N 118.56 . 1 697 . 90 GLU H H 8.41 . 1 698 . 90 GLU HA H 4.05 . 1 699 . 90 GLU HB2 H 2.09 . 2 700 . 90 GLU HB3 H 1.83 . 2 701 . 90 GLU CA C 59.66 . 1 702 . 90 GLU CB C 29.23 . 1 703 . 90 GLU N N 121.64 . 1 704 . 91 TYR H H 7.57 . 1 705 . 91 TYR HA H 4.08 . 1 706 . 91 TYR HB2 H 3.11 . 1 707 . 91 TYR HB3 H 3.11 . 1 708 . 91 TYR HD1 H 7.08 . 1 709 . 91 TYR HD2 H 7.08 . 1 710 . 91 TYR CA C 61.07 . 1 711 . 91 TYR CB C 37.97 . 1 712 . 91 TYR N N 119.86 . 1 713 . 92 VAL H H 8.5 . 1 714 . 92 VAL HA H 3.62 . 1 715 . 92 VAL HB H 1.9 . 1 716 . 92 VAL HG1 H 1.09 . 1 717 . 92 VAL HG2 H 0.64 . 1 718 . 92 VAL CA C 67.08 . 1 719 . 92 VAL CB C 35.17 . 1 720 . 92 VAL CG1 C 23.28 . 1 721 . 92 VAL CG2 C 22.07 . 1 722 . 92 VAL N N 121.88 . 1 723 . 93 ARG H H 8.74 . 1 724 . 93 ARG HA H 3.91 . 1 725 . 93 ARG HB2 H 2.05 . 2 726 . 93 ARG HB3 H 1.92 . 2 727 . 93 ARG HG2 H 1.64 . 3 728 . 93 ARG HG3 H 1.64 . 1 729 . 93 ARG HD2 H 2.57 . 1 730 . 93 ARG HD3 H 2.57 . 1 731 . 93 ARG CA C 60.34 . 1 732 . 93 ARG CB C 28.03 . 1 733 . 93 ARG N N 120.75 . 1 734 . 94 LYS H H 8.3 . 1 735 . 94 LYS HA H 3.9 . 1 736 . 94 LYS HB2 H 1.87 . 2 737 . 94 LYS HB3 H 1.74 . 2 738 . 94 LYS HG2 H 1.38 . 3 739 . 94 LYS HG3 H 1.38 . 1 740 . 94 LYS HE2 H 2.95 . 1 741 . 94 LYS HE3 H 2.95 . 1 742 . 94 LYS CA C 60.32 . 1 743 . 94 LYS CB C 32.86 . 1 744 . 94 LYS N N 117.88 . 1 745 . 95 ALA H H 8.3 . 1 746 . 95 ALA HA H 3.91 . 1 747 . 95 ALA HB H 1.20 . 1 748 . 95 ALA CA C 55.24 . 1 749 . 95 ALA CB C 17.34 . 1 750 . 95 ALA N N 124.06 . 1 751 . 96 TRP H H 8.69 . 1 752 . 96 TRP HA H 3.63 . 1 753 . 96 TRP HB2 H 3.23 . 2 754 . 96 TRP HB3 H 2.89 . 2 755 . 96 TRP HD1 H 7.95 . 1 756 . 96 TRP HE1 H 12.16 . 1 757 . 96 TRP HE3 H 7.16 . 1 758 . 96 TRP HZ2 H 6.0 . 1 759 . 96 TRP HZ3 H 6.6 . 1 760 . 96 TRP HH2 H 6.48 . 1 761 . 96 TRP CA C 63.57 . 1 762 . 96 TRP CB C 27.26 . 1 763 . 96 TRP N N 118.74 . 1 764 . 96 TRP NE1 N 135.32 . 1 765 . 97 LEU H H 8.3 . 1 766 . 97 LEU HA H 4.04 . 1 767 . 97 LEU HB2 H 1.9 . 2 768 . 97 LEU HB3 H 1.5 . 2 769 . 97 LEU HD1 H 0.86 . 4 770 . 97 LEU HD2 H 0.86 . 4 771 . 97 LEU CA C 58.65 . 1 772 . 97 LEU CB C 41.29 . 1 773 . 97 LEU CD1 C 22.93 . 4 774 . 97 LEU CD2 C 22.93 . 4 775 . 97 LEU N N 118.34 . 1 776 . 98 ARG H H 7.79 . 1 777 . 98 ARG HA H 4.08 . 1 778 . 98 ARG HB2 H 1.92 . 1 779 . 98 ARG HB3 H 1.92 . 1 780 . 98 ARG HG2 H 1.79 . 1 781 . 98 ARG HG3 H 1.79 . 1 782 . 98 ARG HD2 H 3.17 . 1 783 . 98 ARG HD3 H 3.17 . 1 784 . 98 ARG CA C 59.2 . 1 785 . 98 ARG CB C 30.02 . 1 786 . 98 ARG N N 120.7 . 1 787 . 99 ASP H H 8.2 . 1 788 . 99 ASP HA H 4.41 . 1 789 . 99 ASP HB2 H 2.19 . 1 790 . 99 ASP HB3 H 2.19 . 1 791 . 99 ASP CA C 57.62 . 1 792 . 99 ASP CB C 40.0 . 1 793 . 99 ASP N N 121.94 . 1 794 . 100 ILE H H 8.75 . 1 795 . 100 ILE HA H 3.49 . 1 796 . 100 ILE HB H 1.86 . 1 797 . 100 ILE HG2 H 0.88 . 1 798 . 100 ILE HD1 H 0.93 . 1 799 . 100 ILE CA C 66.22 . 1 800 . 100 ILE CB C 38.24 . 1 801 . 100 ILE CG2 C 17.91 . 1 802 . 100 ILE CD1 C 14.1 . 1 803 . 100 ILE N N 121.22 . 1 804 . 101 ALA H H 7.61 . 1 805 . 101 ALA HA H 4.26 . 1 806 . 101 ALA HB H 1.57 . 1 807 . 101 ALA CA C 55.2 . 1 808 . 101 ALA CB C 17.99 . 1 809 . 101 ALA N N 122.28 . 1 810 . 102 GLU H H 8.08 . 1 811 . 102 GLU HA H 4.12 . 1 812 . 102 GLU HB2 H 2.15 . 1 813 . 102 GLU HB3 H 2.15 . 1 814 . 102 GLU HG2 H 2.42 . 1 815 . 102 GLU HG3 H 2.42 . 1 816 . 102 GLU CB C 25.86 . 1 817 . 102 GLU N N 119.34 . 1 818 . 103 GLU H H 8.18 . 1 819 . 103 GLU HA H 4.09 . 1 820 . 103 GLU HB2 H 2.16 . 2 821 . 103 GLU HB3 H 2.13 . 2 822 . 103 GLU HG2 H 2.42 . 1 823 . 103 GLU HG3 H 2.42 . 1 824 . 103 GLU CA C 58.5 . 1 825 . 103 GLU CB C 29.37 . 1 826 . 103 GLU N N 119.82 . 1 827 . 104 GLN H H 8.53 . 1 828 . 104 GLN HA H 4.21 . 1 829 . 104 GLN HB2 H 2.32 . 2 830 . 104 GLN HB3 H 2.09 . 2 831 . 104 GLN HG2 H 2.61 . 1 832 . 104 GLN HG3 H 2.61 . 1 833 . 104 GLN CA C 58.8 . 1 834 . 104 GLN CB C 28.9 . 1 835 . 104 GLN N N 119.57 . 1 836 . 105 GLU H H 8.03 . 1 837 . 105 GLU HA H 4.12 . 1 838 . 105 GLU HB2 H 2.13 . 1 839 . 105 GLU HB3 H 2.13 . 1 840 . 105 GLU HG2 H 2.39 . 1 841 . 105 GLU HG3 H 2.39 . 1 842 . 105 GLU CA C 58.96 . 1 843 . 105 GLU CB C 29.7 . 1 844 . 105 GLU CG C 36.58 . 1 845 . 105 GLU N N 121.67 . 1 846 . 106 LYS H H 7.94 . 1 847 . 106 LYS HA H 4.1 . 1 848 . 106 LYS HB2 H 2.10 . 1 849 . 106 LYS HB3 H 2.10 . 1 850 . 106 LYS HG2 H 1.54 . 1 851 . 106 LYS HG3 H 1.54 . 1 852 . 106 LYS HD2 H 1.78 . 1 853 . 106 LYS HD3 H 1.78 . 1 854 . 106 LYS HE2 H 2.40 . 1 855 . 106 LYS HE3 H 2.40 . 1 856 . 106 LYS CA C 58.18 . 1 857 . 106 LYS CB C 32.55 . 1 858 . 106 LYS N N 120.28 . 1 859 . 107 TYR H H 7.97 . 1 860 . 107 TYR HA H 4.35 . 1 861 . 107 TYR HB2 H 3.08 . 1 862 . 107 TYR HB3 H 3.08 . 1 863 . 107 TYR HD1 H 7.12 . 1 864 . 107 TYR HD2 H 7.12 . 1 865 . 107 TYR HE1 H 6.36 . 1 866 . 107 TYR HE2 H 6.36 . 1 867 . 107 TYR CA C 59.7 . 1 868 . 107 TYR CB C 38.49 . 1 869 . 107 TYR N N 120.41 . 1 870 . 108 ALA H H 7.76 . 1 871 . 108 ALA HA H 4.12 . 1 872 . 108 ALA HB H 1.44 . 1 873 . 108 ALA CA C 53.25 . 1 874 . 108 ALA CB C 18.82 . 1 875 . 108 ALA N N 123.26 . 1 876 . 109 ALA H H 7.74 . 1 877 . 109 ALA HA H 4.25 . 1 878 . 109 ALA HB H 1.44 . 1 879 . 109 ALA CA C 52.74 . 1 880 . 109 ALA CB C 18.95 . 1 881 . 109 ALA N N 121.32 . 1 882 . 110 GLU H H 7.9 . 1 883 . 110 GLU HA H 4.22 . 1 884 . 110 GLU HB2 H 2.04 . 2 885 . 110 GLU HB3 H 1.94 . 2 886 . 110 GLU HG2 H 2.21 . 1 887 . 110 GLU HG3 H 2.21 . 1 888 . 110 GLU CA C 56.69 . 1 889 . 110 GLU CB C 29.86 . 1 890 . 110 GLU N N 119.57 . 1 891 . 111 ARG H H 7.93 . 1 892 . 111 ARG HA H 4.24 . 1 893 . 111 ARG HB2 H 1.78 . 2 894 . 111 ARG HB3 H 1.75 . 2 895 . 111 ARG HG2 H 2.04 . 1 896 . 111 ARG HG3 H 2.04 . 1 897 . 111 ARG HD2 H 3.11 . 1 898 . 111 ARG HD3 H 3.11 . 1 899 . 111 ARG CB C 30.96 . 1 900 . 111 ARG N N 121.9 . 1 901 . 112 ASP H H 7.86 . 1 902 . 112 ASP HA H 4.27 . 1 903 . 112 ASP HB2 H 2.61 . 1 904 . 112 ASP HB3 H 2.56 . 1 905 . 112 ASP CA C 57.01 . 1 906 . 112 ASP CB C 42.14 . 1 907 . 112 ASP N N 127.61 . 1 stop_ save_