data_4098 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Resonance Assignments and Secondary Structure of Apo Liver Fatty Acid-Binding Protein ; _BMRB_accession_number 4098 _BMRB_flat_file_name bmr4098.str _Entry_type original _Submission_date 1998-01-22 _Accession_date 1998-01-22 _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 Wang Hsin . . 2 He Yan . . 3 Hsu 'Kuo Tung' . . 4 Magliocca Joseph F. . 5 Storch Judith . . 6 Stark Ruth E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 572 "13C chemical shifts" 485 "15N chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-12-21 original author . stop_ _Original_release_date 1998-12-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Wang, H., He, Y., Hsu, K.T., Magliocca, J.F., Storch, J., and Stark, R. E., "1H, 15N and 13C Resonance Assignments and Secondary Structure of Apo Liver Fatty Acid-Binding Protein," J. Biomol. NMR 12, 197-199 (1998). ; _Citation_title ; 1H, 15N and 13C Resonance Assignments and Secondary Structure of Apo Liver Fatty Acid-Binding Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98399498 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Hsin . . 2 He Yan . . 3 Hsu 'Kuo Tung' . . 4 Magliocca Joseph F. . 5 Storch Judith . . 6 Stark Ruth E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 197 _Page_last 199 _Year 1998 _Details . loop_ _Keyword 3D_NMR 'chemical-shift index' FABP 'Fatty Acid-Binding Protein' 'isotopic enrichment' 'resonance assignments' 'secondary structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johnson B. A. . 2 Blevins R. A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 4 _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 603 _Page_last 614 _Year 1994 _Details . save_ save_citation_two _Saveframe_category citation _Citation_full 'Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G. Pfeifer, J. and Bax, A (1995) J. Biomol. NMR 6, 277-293.' _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_ save_citation_three _Saveframe_category citation _Citation_full 'Zimmerman, D. E. and Montelione, G. T. (1995) Curr. Opin. Struct. Biol. 5, 664-673.' _Citation_title 'Automated analysis of nuclear magnetic resonance assignments for proteins.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8574703 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zimmerman 'D E' E. . 2 Montelione 'G T' T. . stop_ _Journal_abbreviation 'Curr. Opin. Struct. Biol.' _Journal_name_full 'Current opinion in structural biology' _Journal_volume 5 _Journal_issue 5 _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 664 _Page_last 673 _Year 1995 _Details ; Recent developments in protein NMR technology provide spectral data that are highly amendable to analysis by computer software systems. Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to establish sequential links and sequence-specific assignments. The most advanced systems provide automated analysis of complete backbone and extensive side-chain resonance assignments for proteins of 50-150 amino acids. ; save_ save_citation_four _Saveframe_category citation _Citation_full 'Garrett, D. S., Powers, R., Gronenborn, A. M. and Clore, G. M. (1991) J. Mag. Reson. 95, 214-220.' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Garrett D. S. . 2 Powers R. . . 3 Gronenborn A. M. . 4 Clore G. M. . stop_ _Journal_abbreviation 'J. Mag. Reson.' _Journal_name_full . _Journal_volume 95 _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 214 _Page_last 220 _Year 1991 _Details . save_ save_citation_NMR_Pulse_Sequence_Reference _Saveframe_category citation _Citation_full ; Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc. 114, 6291-6293. Wittekind, M. and Mueller, L. (1993) J. Magn. Reson. Ser. B, 101, 201-205. Muhandiram, D.R. and Kay, L.E. (1994) J. Magn. Reson. Ser. B, 103, 203-216. Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson. 89, 496-514. Kay, L.E. (1993) J. Am. Chem. Soc. 115, 2055-2057. Logan, T.M., Olejniczak, E.T., Xu, R.X. and Fesik, S. (1993) J. Biomol. NMR 3, 225-231. Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR 3, 185-204. Bax, A., Clore, G.M., and Gronenborn, A.M. (1990) J. Magn. Reson. 88, 425-431. Kay, L.E., Keifer, P. and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665. Kay, L.E., Marion, D. and Bax, A. (1989) J. Magn. Reson. 84, 72-84. Zhang, O., Kay, L.E., Olivier, J.P. and Forman-Kay, J.D. (1994) J. Biomol. NMR 4, 845-858. ; _Citation_title 'Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7812156 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang O . . 2 Kay 'L E' E. . 3 Olivier 'J P' P. . 4 Forman-Kay 'J D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 4 _Journal_issue 6 _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 845 _Page_last 858 _Year 1994 _Details ; The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples of the SH3 in near physiological buffer exhibiting an approximately 1:1 ratio of the two states. NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment. ; save_ ################################## # Molecular system description # ################################## save_system_apo-LFABP _Saveframe_category molecular_system _Mol_system_name 'Liver Fatty Acid-Binding Protein' _Abbreviation_common apo-LFABP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label apo-LFABP $apo-LFABP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'cellular growth and differentiation' stop_ _Database_query_date . _Details ; Intracellular transport proteins for fatty acid (FA) LFABP has been detected in abundance in tissues from liver, intestinal epithelia, adipose deposits, myocardium, kidney Up to 5% of the soluble protein in liver and in tips of the villi in the jejunum (small intestine). Implicated in key processes of cellular growth and differentiation. ; save_ ######################## # Monomeric polymers # ######################## save_apo-LFABP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Liver Fatty Acid-Binding Protein' _Abbreviation_common apo-LFABP _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 127 _Mol_residue_sequence ; MNFSGKYQVQSQENFEPFMK AMGLPEDLIQKGKDIKGVSE IVHEGKKVKLTITYGSKVIH NEFTLGEECELETMTGEKVK AVVKMEGDNKMVTTFKGIKS VTEFNGDTITNTMTLGDIVY KRVSKRI ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 PHE 4 SER 5 GLY 6 LYS 7 TYR 8 GLN 9 VAL 10 GLN 11 SER 12 GLN 13 GLU 14 ASN 15 PHE 16 GLU 17 PRO 18 PHE 19 MET 20 LYS 21 ALA 22 MET 23 GLY 24 LEU 25 PRO 26 GLU 27 ASP 28 LEU 29 ILE 30 GLN 31 LYS 32 GLY 33 LYS 34 ASP 35 ILE 36 LYS 37 GLY 38 VAL 39 SER 40 GLU 41 ILE 42 VAL 43 HIS 44 GLU 45 GLY 46 LYS 47 LYS 48 VAL 49 LYS 50 LEU 51 THR 52 ILE 53 THR 54 TYR 55 GLY 56 SER 57 LYS 58 VAL 59 ILE 60 HIS 61 ASN 62 GLU 63 PHE 64 THR 65 LEU 66 GLY 67 GLU 68 GLU 69 CYS 70 GLU 71 LEU 72 GLU 73 THR 74 MET 75 THR 76 GLY 77 GLU 78 LYS 79 VAL 80 LYS 81 ALA 82 VAL 83 VAL 84 LYS 85 MET 86 GLU 87 GLY 88 ASP 89 ASN 90 LYS 91 MET 92 VAL 93 THR 94 THR 95 PHE 96 LYS 97 GLY 98 ILE 99 LYS 100 SER 101 VAL 102 THR 103 GLU 104 PHE 105 ASN 106 GLY 107 ASP 108 THR 109 ILE 110 THR 111 ASN 112 THR 113 MET 114 THR 115 LEU 116 GLY 117 ASP 118 ILE 119 VAL 120 TYR 121 LYS 122 ARG 123 VAL 124 SER 125 LYS 126 ARG 127 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15429 LFABP-apo 100.00 127 100.00 100.00 1.87e-84 BMRB 15433 LFABP 100.00 127 100.00 100.00 1.87e-84 BMRB 15434 LFABP 100.00 127 100.00 100.00 1.87e-84 PDB 1LFO "Liver Fatty Acid Binding Protein-Oleate Complex" 100.00 128 99.21 99.21 7.15e-83 PDB 2JU3 "Solution-State Nmr Structures Of Apo-Lfabp (Liver Fatty Acid-Binding Protein)" 100.00 127 100.00 100.00 1.87e-84 PDB 2JU7 "Solution-State Structures Of Oleate-Liganded Lfabp, Protein Only" 100.00 127 100.00 100.00 1.87e-84 PDB 2JU8 "Solution-State Structures Of Oleate-Liganded Lfabp, Major Form Of 1:2 Protein-Ligand Complex" 100.00 127 100.00 100.00 1.87e-84 EMBL CAA24545 "unnamed protein product [Rattus norvegicus]" 100.00 127 100.00 100.00 1.87e-84 GB AAA41134 "liver fatty acid binding protein p14, partial [Rattus norvegicus]" 80.31 102 100.00 100.00 6.02e-65 GB AAA41135 "fatty acid binding protein (FABP) [Rattus norvegicus]" 100.00 127 100.00 100.00 1.87e-84 GB AAA41140 "liver fatty acid binding protein [Rattus norvegicus]" 100.00 127 100.00 100.00 1.87e-84 GB AAA42119 "sterol carrier protein, partial [Rattus sp.]" 74.02 94 100.00 100.00 4.06e-57 GB AAB19788 "fatty-acid-binding protein [synthetic construct]" 100.00 127 100.00 100.00 1.87e-84 PRF 1202232B "protein,fatty acid binding" 100.00 127 100.00 100.00 1.87e-84 REF NP_036688 "fatty acid-binding protein, liver [Rattus norvegicus]" 100.00 127 100.00 100.00 1.87e-84 SP P02692 "RecName: Full=Fatty acid-binding protein, liver; AltName: Full=Fatty acid-binding protein 1; AltName: Full=Liver-type fatty aci" 100.00 127 100.00 100.00 1.87e-84 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $apo-LFABP Rat 10116 Eukaryota Metazoa Rattus norvegicus liver stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $apo-LFABP 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS plasmid pET-11d 'native (cDNA obtained from Drs. Alan Kleinfeld and Ron Ogata")' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $apo-LFABP 1.3 mM '[U-99% 13C; U-98% 15N]' phosphate 20 mM . D2O 5 % . H2O 95 % . NaCl 100 mM . EDTA 50 uM . sodium_azide 0.02 % . bovine_lung_aprotinin 0.01 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $apo-LFABP . mM 1.0 1.3 '[U-98% 15N]' phosphate 20 mM . . . D2O 5 % . . . H2O 95 % . . . NaCl 100 mM . . . EDTA 50 uM . . . sodium_azide 0.02 % . . . bovine_lung_aprotinin 0.01 % . . . stop_ save_ ############################ # Computer software used # ############################ save_software_NMRVIEW _Saveframe_category software _Name NMRView _Version 3.1 loop_ _Task 'The majority of assignments were completed by using NMRVIEW' stop_ _Details . _Citation_label $citation_one save_ save_software_NMRPIPE _Saveframe_category software _Name NMRPipe _Version 3.1 loop_ _Task 'All data were processed with NMRPIPE and then converted to NMRVIEW format for analysis' stop_ _Details . _Citation_label $citation_two save_ save_software_AUTOASSIGN _Saveframe_category software _Name AutoAssign _Version 3.1 loop_ _Task ; Preliminary sequential backbone assignments were obtained using AUTOASSIGN program at Rutgers University with CBCA(CO)NH and HNCACB data ; stop_ _Details . _Citation_label $citation_three save_ save_software_PIPP _Saveframe_category software _Name PIPP _Version 3.1 _Details . _Citation_label $citation_four save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Unity _Model Inova-600 _Field_strength 600 _Details '3 channels with z-gradient' save_ save_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 600 _Field_strength 600 _Details '3 channels with z-gradient' save_ ############################# # NMR applied experiments # ############################# save_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACOHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACOHA _Sample_label . save_ save_H(CCO)NH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label . save_ save_C(CO)NH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _Sample_label . save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_15N-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_TOCSY-HSQC(15N)_8 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY-HSQC(15N) _Sample_label . save_ save_NOESY-HSQC(15N)_9 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC(15N) _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACOHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY-HSQC(15N) _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC(15N) _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.13 .01 M pH 6.0 0.1 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details '2.9M NH4Cl in 1M HCl' 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 DSS C 13 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo NH4 N 15 . ppm 24.93 external direct cylindrical external_to_the_sample parallel_to_Bo 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_two stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name apo-LFABP _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 ASN CA C 52.30 . 1 2 . 2 ASN HA H 4.81 . 1 3 . 2 ASN CB C 40.40 . 1 4 . 2 ASN HB3 H 2.83 . 2 5 . 2 ASN HB2 H 2.57 . 2 6 . 2 ASN C C 176.00 . 1 7 . 3 PHE N N 131.80 . 2 8 . 3 PHE H H 11.46 . 1 9 . 3 PHE CA C 56.90 . 1 10 . 3 PHE HA H 4.53 . 1 11 . 3 PHE CB C 38.70 . 1 12 . 3 PHE HB3 H 3.07 . 2 13 . 3 PHE HB2 H 2.45 . 2 14 . 3 PHE C C 177.00 . 1 15 . 4 SER N N 118.30 . 1 16 . 4 SER H H 8.70 . 1 17 . 4 SER CA C 61.10 . 1 18 . 4 SER HA H 4.43 . 1 19 . 4 SER CB C 64.40 . 1 20 . 4 SER HB3 H 4.13 . 2 21 . 4 SER HB2 H 4.00 . 2 22 . 4 SER C C 174.20 . 1 23 . 5 GLY N N 113.00 . 1 24 . 5 GLY H H 9.10 . 1 25 . 5 GLY CA C 45.40 . 1 26 . 5 GLY HA3 H 3.96 . 2 27 . 5 GLY HA2 H 3.78 . 2 28 . 5 GLY C C 170.10 . 1 29 . 6 LYS N N 122.50 . 1 30 . 6 LYS H H 8.19 . 1 31 . 6 LYS CA C 55.50 . 1 32 . 6 LYS HA H 5.20 . 1 33 . 6 LYS CB C 34.90 . 1 34 . 6 LYS HB3 H 1.64 . 2 35 . 6 LYS CG C 26.20 . 1 36 . 6 LYS HG3 H 1.44 . 2 37 . 6 LYS HG2 H 1.25 . 2 38 . 6 LYS CD C 29.80 . 1 39 . 6 LYS HD3 H 1.64 . 2 40 . 6 LYS CE C 42.30 . 1 41 . 6 LYS HE3 H 2.89 . 2 42 . 6 LYS C C 174.80 . 1 43 . 7 TYR N N 122.20 . 1 44 . 7 TYR H H 9.13 . 1 45 . 7 TYR CA C 56.00 . 1 46 . 7 TYR HA H 5.23 . 1 47 . 7 TYR CB C 42.10 . 1 48 . 7 TYR HB3 H 2.68 . 2 49 . 7 TYR HB2 H 2.48 . 2 50 . 7 TYR C C 174.80 . 1 51 . 8 GLN N N 125.00 . 1 52 . 8 GLN H H 9.22 . 1 53 . 8 GLN CA C 54.30 . 1 54 . 8 GLN HA H 5.21 . 1 55 . 8 GLN CB C 32.60 . 1 56 . 8 GLN HB3 H 2.04 . 2 57 . 8 GLN CG C 33.90 . 1 58 . 8 GLN HG3 H 2.38 . 2 59 . 8 GLN HG2 H 2.24 . 2 60 . 8 GLN C C 176.20 . 1 61 . 9 VAL N N 132.30 . 1 62 . 9 VAL H H 8.75 . 1 63 . 9 VAL CA C 65.20 . 1 64 . 9 VAL HA H 4.10 . 1 65 . 9 VAL CB C 33.00 . 1 66 . 9 VAL HB H 1.93 . 1 67 . 9 VAL CG2 C 23.20 . 2 68 . 9 VAL HG2 H 0.98 . 2 69 . 9 VAL CG1 C 21.40 . 2 70 . 9 VAL HG1 H 0.86 . 2 71 . 9 VAL C C 175.30 . 1 72 . 10 GLN N N 128.30 . 1 73 . 10 GLN H H 10.05 . 1 74 . 10 GLN CA C 56.00 . 1 75 . 10 GLN HA H 4.53 . 1 76 . 10 GLN CB C 32.10 . 1 77 . 10 GLN HB3 H 2.19 . 2 78 . 10 GLN HB2 H 1.97 . 2 79 . 10 GLN CG C 34.50 . 1 80 . 10 GLN HG3 H 2.41 . 2 81 . 10 GLN C C 176.00 . 1 82 . 11 SER N N 114.10 . 1 83 . 11 SER H H 7.96 . 1 84 . 11 SER CA C 57.60 . 1 85 . 11 SER HA H 4.75 . 1 86 . 11 SER CB C 65.30 . 1 87 . 11 SER HB3 H 3.85 . 2 88 . 11 SER C C 172.20 . 1 89 . 12 GLN N N 120.80 . 1 90 . 12 GLN H H 8.59 . 1 91 . 12 GLN CA C 54.90 . 1 92 . 12 GLN HA H 5.46 . 1 93 . 12 GLN CB C 33.50 . 1 94 . 12 GLN HB3 H 2.24 . 2 95 . 12 GLN CG C 34.40 . 1 96 . 12 GLN HG3 H 2.48 . 2 97 . 12 GLN HG2 H 2.40 . 2 98 . 12 GLN C C 174.40 . 1 99 . 13 GLU N N 123.80 . 1 100 . 13 GLU H H 9.12 . 1 101 . 13 GLU CA C 55.20 . 1 102 . 13 GLU HA H 4.88 . 1 103 . 13 GLU CB C 33.90 . 1 104 . 13 GLU HB3 H 2.13 . 2 105 . 13 GLU HB2 H 1.91 . 2 106 . 13 GLU CG C 36.30 . 1 107 . 13 GLU HG3 H 2.30 . 2 108 . 13 GLU C C 175.70 . 1 109 . 14 ASN N N 118.10 . 1 110 . 14 ASN H H 9.24 . 1 111 . 14 ASN CA C 55.00 . 1 112 . 14 ASN HA H 4.55 . 1 113 . 14 ASN CB C 36.20 . 1 114 . 14 ASN HB3 H 3.73 . 2 115 . 14 ASN HB2 H 3.13 . 2 116 . 14 ASN C C 174.60 . 1 117 . 15 PHE N N 121.30 . 1 118 . 15 PHE H H 8.68 . 1 119 . 15 PHE CA C 62.70 . 1 120 . 15 PHE HA H 3.86 . 1 121 . 15 PHE CB C 40.50 . 1 122 . 15 PHE HB3 H 3.17 . 2 123 . 15 PHE HB2 H 2.33 . 2 124 . 15 PHE C C 176.30 . 1 125 . 16 GLU N N 118.70 . 1 126 . 16 GLU H H 9.60 . 1 127 . 16 GLU CA C 62.40 . 1 128 . 16 GLU HA H 3.86 . 1 129 . 16 GLU CB C 27.00 . 1 130 . 16 GLU HB3 H 2.24 . 2 131 . 16 GLU CG C 37.70 . 1 132 . 16 GLU HG3 H 2.31 . 2 133 . 16 GLU C C 175.30 . 1 134 . 17 PRO CA C 65.60 . 1 135 . 17 PRO HA H 4.25 . 1 136 . 17 PRO CB C 31.00 . 1 137 . 17 PRO HB3 H 2.35 . 2 138 . 17 PRO HB2 H 1.77 . 2 139 . 17 PRO CG C 28.20 . 1 140 . 17 PRO HG3 H 2.14 . 2 141 . 17 PRO CD C 49.70 . 1 142 . 17 PRO HD2 H 3.74 . 2 143 . 17 PRO HD3 H 3.66 . 2 144 . 17 PRO C C 179.60 . 1 145 . 18 PHE N N 120.50 . 1 146 . 18 PHE H H 7.41 . 1 147 . 18 PHE CA C 62.40 . 1 148 . 18 PHE HA H 3.96 . 1 149 . 18 PHE CB C 40.60 . 1 150 . 18 PHE HB3 H 3.04 . 2 151 . 18 PHE HB2 H 2.89 . 2 152 . 18 PHE C C 176.10 . 1 153 . 19 MET N N 117.80 . 1 154 . 19 MET H H 8.31 . 1 155 . 19 MET CA C 56.80 . 1 156 . 19 MET HA H 3.95 . 1 157 . 19 MET CB C 31.60 . 1 158 . 19 MET HB3 H 1.40 . 2 159 . 19 MET CG C 32.90 . 1 160 . 19 MET HG3 H 1.86 . 2 161 . 19 MET HG2 H 1.49 . 2 162 . 19 MET C C 179.50 . 1 163 . 20 LYS N N 122.20 . 1 164 . 20 LYS H H 8.27 . 1 165 . 20 LYS CA C 59.50 . 1 166 . 20 LYS HA H 3.97 . 1 167 . 20 LYS CB C 32.40 . 1 168 . 20 LYS HB3 H 1.79 . 2 169 . 20 LYS CG C 25.60 . 1 170 . 20 LYS HG3 H 1.49 . 2 171 . 20 LYS HG2 H 1.34 . 2 172 . 20 LYS CD C 29.40 . 1 173 . 20 LYS HD3 H 1.65 . 2 174 . 20 LYS CE C 42.20 . 1 175 . 20 LYS HE3 H 2.94 . 2 176 . 20 LYS C C 180.70 . 1 177 . 21 ALA N N 125.90 . 1 178 . 21 ALA H H 7.62 . 1 179 . 21 ALA CA C 54.70 . 1 180 . 21 ALA HA H 4.04 . 1 181 . 21 ALA CB C 18.10 . 1 182 . 21 ALA HB H 1.33 . 1 183 . 21 ALA C C 179.50 . 1 184 . 22 MET N N 117.40 . 1 185 . 22 MET H H 7.51 . 1 186 . 22 MET CA C 55.50 . 1 187 . 22 MET HA H 4.16 . 1 188 . 22 MET CB C 33.20 . 1 189 . 22 MET HB3 H 1.87 . 2 190 . 22 MET CG C 32.50 . 1 191 . 22 MET HG3 H 2.05 . 2 192 . 22 MET C C 176.50 . 1 193 . 23 GLY N N 108.10 . 1 194 . 23 GLY H H 7.63 . 1 195 . 23 GLY CA C 45.30 . 1 196 . 23 GLY HA3 H 4.15 . 2 197 . 23 GLY HA2 H 3.69 . 2 198 . 23 GLY C C 175.00 . 1 199 . 24 LEU N N 125.60 . 1 200 . 24 LEU H H 7.54 . 1 201 . 24 LEU CA C 53.80 . 1 202 . 24 LEU HA H 4.40 . 1 203 . 24 LEU CB C 41.90 . 1 204 . 24 LEU HB3 H 1.41 . 2 205 . 24 LEU HB2 H 1.20 . 2 206 . 24 LEU CG C 28.40 . 1 207 . 24 LEU HG H 1.66 . 1 208 . 24 LEU CD1 C 25.20 . 2 209 . 24 LEU HD1 H 0.85 . 2 210 . 24 LEU CD2 C 25.20 . 2 211 . 24 LEU HD2 H 0.77 . 2 212 . 24 LEU C C 174.30 . 1 213 . 25 PRO CA C 62.80 . 1 214 . 25 PRO HA H 4.47 . 1 215 . 25 PRO CB C 32.90 . 1 216 . 25 PRO HB3 H 2.45 . 2 217 . 25 PRO HB2 H 2.08 . 2 218 . 25 PRO CG C 28.10 . 1 219 . 25 PRO HG3 H 2.13 . 2 220 . 25 PRO CD C 51.00 . 1 221 . 25 PRO HD2 H 4.00 . 2 222 . 25 PRO HD3 H 3.52 . 2 223 . 25 PRO C C 177.90 . 1 224 . 26 GLU N N 124.30 . 1 225 . 26 GLU H H 8.75 . 1 226 . 26 GLU CA C 60.10 . 1 227 . 26 GLU HA H 3.87 . 1 228 . 26 GLU CB C 30.00 . 1 229 . 26 GLU HB3 H 2.07 . 2 230 . 26 GLU CG C 36.30 . 1 231 . 26 GLU HG3 H 2.35 . 2 232 . 26 GLU C C 178.30 . 1 233 . 27 ASP N N 118.60 . 1 234 . 27 ASP H H 8.87 . 1 235 . 27 ASP CA C 57.10 . 1 236 . 27 ASP HA H 4.38 . 1 237 . 27 ASP CB C 40.10 . 1 238 . 27 ASP HB3 H 2.66 . 2 239 . 27 ASP C C 178.50 . 1 240 . 28 LEU N N 121.70 . 1 241 . 28 LEU H H 7.19 . 1 242 . 28 LEU CA C 57.20 . 1 243 . 28 LEU HA H 4.24 . 1 244 . 28 LEU CB C 42.00 . 1 245 . 28 LEU HB3 H 1.81 . 2 246 . 28 LEU HB2 H 1.62 . 2 247 . 28 LEU CG C 27.40 . 1 248 . 28 LEU HG H 1.75 . 1 249 . 28 LEU CD1 C 25.10 . 2 250 . 28 LEU HD1 H 0.99 . 2 251 . 28 LEU CD2 C 23.80 . 2 252 . 28 LEU HD2 H 0.91 . 2 253 . 28 LEU C C 180.30 . 1 254 . 29 ILE N N 124.20 . 1 255 . 29 ILE H H 7.83 . 1 256 . 29 ILE CA C 66.10 . 1 257 . 29 ILE HA H 3.65 . 1 258 . 29 ILE CB C 38.00 . 1 259 . 29 ILE HB H 2.04 . 1 260 . 29 ILE CG1 C 29.50 . 2 261 . 29 ILE HG12 H 1.70 . 2 262 . 29 ILE HG13 H 0.46 . 2 263 . 29 ILE CD1 C 13.70 . 1 264 . 29 ILE HD1 H 0.67 . 1 265 . 29 ILE CG2 C 18.10 . 2 266 . 29 ILE HG2 H 0.94 . 1 267 . 29 ILE C C 177.80 . 1 268 . 30 GLN N N 119.30 . 1 269 . 30 GLN H H 8.23 . 1 270 . 30 GLN CA C 58.70 . 1 271 . 30 GLN HA H 4.00 . 1 272 . 30 GLN CB C 28.30 . 1 273 . 30 GLN HB3 H 2.16 . 2 274 . 30 GLN CG C 33.80 . 1 275 . 30 GLN HG3 H 2.52 . 2 276 . 30 GLN C C 178.70 . 1 277 . 31 LYS N N 118.80 . 1 278 . 31 LYS H H 7.70 . 1 279 . 31 LYS CA C 58.50 . 1 280 . 31 LYS HA H 4.22 . 1 281 . 31 LYS CB C 33.30 . 1 282 . 31 LYS HB3 H 1.90 . 2 283 . 31 LYS CG C 25.80 . 1 284 . 31 LYS HG3 H 1.65 . 2 285 . 31 LYS HG2 H 1.53 . 2 286 . 31 LYS CD C 29.30 . 1 287 . 31 LYS HD3 H 1.69 . 2 288 . 31 LYS CE C 42.40 . 1 289 . 31 LYS HE3 H 3.00 . 2 290 . 31 LYS C C 178.60 . 1 291 . 32 GLY N N 107.70 . 1 292 . 32 GLY H H 7.93 . 1 293 . 32 GLY CA C 46.20 . 1 294 . 32 GLY HA3 H 4.15 . 2 295 . 32 GLY HA2 H 3.81 . 2 296 . 32 GLY C C 175.50 . 1 297 . 33 LYS N N 121.60 . 1 298 . 33 LYS H H 7.55 . 1 299 . 33 LYS CA C 58.90 . 1 300 . 33 LYS HA H 3.37 . 1 301 . 33 LYS CB C 32.40 . 1 302 . 33 LYS HB3 H 1.86 . 2 303 . 33 LYS CG C 24.30 . 1 304 . 33 LYS HG3 H 1.51 . 2 305 . 33 LYS CD C 29.80 . 1 306 . 33 LYS HD3 H 1.43 . 2 307 . 33 LYS HE3 H 3.06 . 2 308 . 33 LYS C C 176.10 . 1 309 . 34 ASP N N 119.30 . 1 310 . 34 ASP H H 7.87 . 1 311 . 34 ASP CA C 54.40 . 1 312 . 34 ASP HA H 4.79 . 1 313 . 34 ASP CB C 41.80 . 1 314 . 34 ASP HB3 H 2.83 . 2 315 . 34 ASP HB2 H 2.50 . 2 316 . 34 ASP C C 176.00 . 1 317 . 35 ILE N N 122.60 . 1 318 . 35 ILE H H 7.23 . 1 319 . 35 ILE CA C 61.50 . 1 320 . 35 ILE HA H 3.95 . 1 321 . 35 ILE CB C 38.30 . 1 322 . 35 ILE HB H 1.76 . 1 323 . 35 ILE CG1 C 27.60 . 2 324 . 35 ILE HG13 H 1.52 . 2 325 . 35 ILE HG12 H 1.12 . 2 326 . 35 ILE CD1 C 13.00 . 1 327 . 35 ILE HD1 H 0.77 . 1 328 . 35 ILE CG2 C 17.30 . 2 329 . 35 ILE HG2 H 0.74 . 1 330 . 35 ILE C C 176.30 . 1 331 . 36 LYS N N 130.90 . 1 332 . 36 LYS H H 8.65 . 1 333 . 36 LYS CA C 55.70 . 1 334 . 36 LYS HA H 4.30 . 1 335 . 36 LYS CB C 32.00 . 1 336 . 36 LYS HB3 H 1.82 . 2 337 . 36 LYS CG C 24.90 . 1 338 . 36 LYS HG3 H 1.28 . 2 339 . 36 LYS CD C 29.30 . 1 340 . 36 LYS HD3 H 1.65 . 2 341 . 36 LYS HE3 H 3.01 . 2 342 . 36 LYS C C 176.10 . 1 343 . 37 GLY N N 113.60 . 1 344 . 37 GLY H H 8.11 . 1 345 . 37 GLY CA C 45.60 . 1 346 . 37 GLY HA3 H 3.97 . 2 347 . 37 GLY HA2 H 3.67 . 2 348 . 37 GLY C C 174.30 . 1 349 . 39 SER CA C 57.20 . 1 350 . 39 SER HA H 5.37 . 1 351 . 39 SER CB C 65.70 . 1 352 . 39 SER HB3 H 3.76 . 2 353 . 39 SER C C 172.90 . 1 354 . 40 GLU N N 126.20 . 1 355 . 40 GLU H H 9.39 . 1 356 . 40 GLU CA C 55.40 . 1 357 . 40 GLU HA H 5.33 . 1 358 . 40 GLU CB C 33.00 . 1 359 . 40 GLU HB3 H 1.94 . 2 360 . 40 GLU CG C 37.00 . 1 361 . 40 GLU HG3 H 2.22 . 2 362 . 40 GLU HG2 H 2.07 . 2 363 . 40 GLU C C 175.10 . 1 364 . 41 ILE N N 127.70 . 1 365 . 41 ILE H H 9.56 . 1 366 . 41 ILE CA C 60.60 . 1 367 . 41 ILE HA H 5.07 . 1 368 . 41 ILE CB C 40.90 . 1 369 . 41 ILE HB H 2.26 . 1 370 . 41 ILE CG1 C 27.80 . 2 371 . 41 ILE HG13 H 1.74 . 2 372 . 41 ILE HG12 H 1.07 . 2 373 . 41 ILE CD1 C 13.60 . 1 374 . 41 ILE HD1 H 0.87 . 1 375 . 41 ILE CG2 C 17.80 . 1 376 . 41 ILE HG2 H 0.81 . 1 377 . 41 ILE C C 176.30 . 1 378 . 42 VAL N N 132.50 . 1 379 . 42 VAL H H 9.35 . 1 380 . 42 VAL CA C 63.10 . 1 381 . 42 VAL HA H 4.23 . 1 382 . 42 VAL CB C 33.50 . 1 383 . 42 VAL HB H 2.09 . 1 384 . 42 VAL CG2 C 20.80 . 2 385 . 42 VAL HG2 H 0.97 . 2 386 . 42 VAL CG1 C 20.80 . 2 387 . 42 VAL HG1 H 0.83 . 2 388 . 42 VAL C C 173.80 . 1 389 . 43 HIS N N 133.70 . 1 390 . 43 HIS H H 8.95 . 1 391 . 43 HIS CA C 53.00 . 1 392 . 43 HIS HA H 5.53 . 1 393 . 43 HIS CB C 34.70 . 1 394 . 43 HIS HB3 H 3.34 . 2 395 . 43 HIS HB2 H 2.53 . 2 396 . 43 HIS C C 174.10 . 1 397 . 44 GLU N N 132.50 . 1 398 . 44 GLU H H 8.95 . 1 399 . 44 GLU CA C 54.80 . 1 400 . 44 GLU HA H 4.38 . 1 401 . 44 GLU CB C 31.90 . 1 402 . 44 GLU HB3 H 1.90 . 2 403 . 44 GLU HB2 H 1.85 . 2 404 . 44 GLU CG C 36.20 . 1 405 . 44 GLU HG3 H 2.07 . 2 406 . 44 GLU C C 175.80 . 1 407 . 45 GLY N N 119.30 . 1 408 . 45 GLY H H 8.59 . 1 409 . 45 GLY CA C 47.40 . 1 410 . 45 GLY HA3 H 4.01 . 2 411 . 45 GLY HA2 H 3.56 . 2 412 . 45 GLY C C 174.40 . 1 413 . 46 LYS N N 127.90 . 1 414 . 46 LYS H H 8.89 . 1 415 . 46 LYS CA C 56.50 . 1 416 . 46 LYS HA H 4.60 . 1 417 . 46 LYS CB C 33.70 . 1 418 . 46 LYS HB3 H 2.27 . 2 419 . 46 LYS HB2 H 1.87 . 2 420 . 46 LYS CG C 25.80 . 1 421 . 46 LYS HG3 H 1.62 . 2 422 . 46 LYS HG2 H 1.57 . 2 423 . 46 LYS CD C 29.80 . 1 424 . 46 LYS HD3 H 1.79 . 2 425 . 46 LYS CE C 42.80 . 1 426 . 46 LYS HE3 H 3.05 . 2 427 . 46 LYS C C 175.10 . 1 428 . 47 LYS N N 122.50 . 1 429 . 47 LYS H H 8.19 . 1 430 . 47 LYS CA C 56.20 . 1 431 . 47 LYS HA H 4.79 . 1 432 . 47 LYS CB C 33.70 . 1 433 . 47 LYS HB3 H 1.94 . 2 434 . 47 LYS HB2 H 1.69 . 2 435 . 47 LYS CG C 25.20 . 1 436 . 47 LYS HG3 H 1.45 . 2 437 . 47 LYS HG2 H 1.29 . 2 438 . 47 LYS CD C 29.20 . 1 439 . 47 LYS HD3 H 1.68 . 2 440 . 47 LYS CE C 41.00 . 1 441 . 47 LYS HE3 H 2.96 . 2 442 . 47 LYS C C 177.90 . 1 443 . 48 VAL N N 127.00 . 1 444 . 48 VAL H H 8.74 . 1 445 . 48 VAL CA C 61.10 . 1 446 . 48 VAL HA H 4.59 . 1 447 . 48 VAL CB C 33.90 . 1 448 . 48 VAL HB H 1.80 . 1 449 . 48 VAL CG2 C 22.00 . 2 450 . 48 VAL HG2 H 0.67 . 2 451 . 48 VAL CG1 C 22.00 . 2 452 . 48 VAL HG1 H 0.48 . 2 453 . 48 VAL C C 174.20 . 1 454 . 49 LYS N N 127.20 . 1 455 . 49 LYS H H 8.80 . 1 456 . 49 LYS CA C 55.30 . 1 457 . 49 LYS HA H 4.81 . 1 458 . 49 LYS CB C 34.40 . 1 459 . 49 LYS HB3 H 2.17 . 2 460 . 49 LYS CG C 25.00 . 1 461 . 49 LYS HG3 H 1.79 . 2 462 . 49 LYS CD C 31.80 . 1 463 . 49 LYS HD3 H 1.98 . 2 464 . 49 LYS HD2 H 1.90 . 2 465 . 49 LYS CE C 42.10 . 1 466 . 49 LYS HE3 H 3.83 . 2 467 . 49 LYS C C 174.90 . 1 468 . 50 LEU N N 128.00 . 1 469 . 50 LEU H H 9.11 . 1 470 . 50 LEU CA C 53.40 . 1 471 . 50 LEU HA H 5.34 . 1 472 . 50 LEU CB C 46.70 . 1 473 . 50 LEU HB3 H 1.68 . 2 474 . 50 LEU HB2 H 1.49 . 2 475 . 50 LEU CG C 27.30 . 1 476 . 50 LEU HG H 1.17 . 1 477 . 50 LEU HD1 H 0.94 . 2 478 . 50 LEU C C 175.80 . 1 479 . 51 THR N N 125.30 . 1 480 . 51 THR H H 9.10 . 1 481 . 51 THR CA C 62.10 . 1 482 . 51 THR HA H 5.27 . 1 483 . 51 THR CB C 71.00 . 1 484 . 51 THR HB H 4.12 . 1 485 . 51 THR CG2 C 22.10 . 1 486 . 51 THR HG2 H 1.09 . 1 487 . 51 THR C C 173.60 . 1 488 . 54 TYR CA C 56.70 . 1 489 . 54 TYR HA H 4.77 . 1 490 . 54 TYR CB C 39.90 . 1 491 . 54 TYR HB3 H 2.97 . 2 492 . 54 TYR HB2 H 2.82 . 2 493 . 54 TYR C C 176.10 . 1 494 . 55 GLY N N 117.00 . 1 495 . 55 GLY H H 8.94 . 1 496 . 55 GLY CA C 47.50 . 1 497 . 55 GLY HA3 H 4.12 . 2 498 . 55 GLY HA2 H 3.68 . 2 499 . 55 GLY C C 174.10 . 1 500 . 56 SER N N 123.60 . 1 501 . 56 SER H H 8.67 . 1 502 . 56 SER CA C 58.70 . 1 503 . 56 SER HA H 4.41 . 1 504 . 56 SER CB C 63.90 . 1 505 . 56 SER HB3 H 4.07 . 2 506 . 56 SER HB2 H 3.82 . 2 507 . 56 SER C C 173.80 . 1 508 . 57 LYS N N 126.10 . 1 509 . 57 LYS H H 7.94 . 1 510 . 57 LYS CA C 55.60 . 1 511 . 57 LYS HA H 4.56 . 1 512 . 57 LYS CB C 34.10 . 1 513 . 57 LYS HB3 H 2.05 . 2 514 . 57 LYS HB2 H 1.89 . 2 515 . 57 LYS CG C 25.00 . 1 516 . 57 LYS HG3 H 1.45 . 2 517 . 57 LYS CD C 29.20 . 1 518 . 57 LYS HD3 H 1.76 . 2 519 . 57 LYS CE C 42.40 . 1 520 . 57 LYS HE3 H 2.94 . 2 521 . 57 LYS C C 174.30 . 1 522 . 58 VAL N N 128.00 . 1 523 . 58 VAL H H 8.45 . 1 524 . 58 VAL CA C 61.70 . 1 525 . 58 VAL HA H 4.11 . 1 526 . 58 VAL CB C 33.70 . 1 527 . 58 VAL HB H 1.92 . 1 528 . 58 VAL CG2 C 21.50 . 2 529 . 58 VAL HG2 H 0.93 . 2 530 . 58 VAL CG1 C 21.50 . 2 531 . 58 VAL HG1 H 0.68 . 2 532 . 58 VAL C C 175.80 . 1 533 . 59 ILE N N 130.10 . 1 534 . 59 ILE H H 9.16 . 1 535 . 59 ILE CA C 60.00 . 1 536 . 59 ILE CB C 40.50 . 1 537 . 60 HIS CA C 54.80 . 1 538 . 60 HIS HA H 5.60 . 1 539 . 60 HIS CB C 31.00 . 1 540 . 60 HIS HB3 H 3.28 . 2 541 . 60 HIS HB2 H 3.06 . 2 542 . 60 HIS C C 173.40 . 1 543 . 61 ASN N N 124.10 . 1 544 . 61 ASN H H 8.83 . 1 545 . 61 ASN CA C 52.80 . 1 546 . 61 ASN HA H 5.34 . 1 547 . 61 ASN CB C 44.50 . 1 548 . 61 ASN HB3 H 2.60 . 2 549 . 61 ASN HB2 H 2.49 . 2 550 . 61 ASN C C 173.50 . 1 551 . 62 GLU N N 123.00 . 1 552 . 62 GLU H H 8.88 . 1 553 . 62 GLU CA C 55.20 . 1 554 . 62 GLU HA H 5.19 . 1 555 . 62 GLU CB C 32.40 . 1 556 . 62 GLU HB3 H 2.04 . 2 557 . 62 GLU CG C 36.20 . 1 558 . 62 GLU HG3 H 2.26 . 2 559 . 62 GLU HG2 H 2.11 . 2 560 . 62 GLU C C 174.30 . 1 561 . 63 PHE N N 121.30 . 1 562 . 63 PHE H H 8.51 . 1 563 . 63 PHE CA C 55.80 . 1 564 . 63 PHE HA H 5.13 . 1 565 . 63 PHE CB C 41.20 . 1 566 . 63 PHE HB3 H 3.32 . 2 567 . 63 PHE HB2 H 3.25 . 2 568 . 63 PHE C C 173.20 . 1 569 . 64 THR N N 119.90 . 1 570 . 64 THR H H 8.70 . 1 571 . 64 THR CA C 61.40 . 1 572 . 64 THR HA H 5.03 . 1 573 . 64 THR CB C 70.40 . 1 574 . 64 THR HB H 3.94 . 1 575 . 64 THR CG2 C 22.50 . 1 576 . 64 THR HG2 H 1.24 . 1 577 . 64 THR C C 175.50 . 1 578 . 65 LEU N N 131.90 . 1 579 . 65 LEU H H 9.62 . 1 580 . 65 LEU CA C 57.00 . 1 581 . 65 LEU HA H 4.43 . 1 582 . 65 LEU CB C 42.30 . 1 583 . 65 LEU HB3 H 1.90 . 2 584 . 65 LEU HB2 H 1.63 . 2 585 . 65 LEU CG C 26.40 . 1 586 . 65 LEU HG H 0.95 . 1 587 . 65 LEU CD1 C 25.00 . 2 588 . 65 LEU HD1 H 0.94 . 2 589 . 65 LEU CD2 C 24.00 . 2 590 . 65 LEU HD2 H 0.94 . 2 591 . 65 LEU C C 178.00 . 1 592 . 66 GLY N N 111.10 . 1 593 . 66 GLY H H 9.45 . 1 594 . 66 GLY CA C 45.80 . 1 595 . 66 GLY HA3 H 4.42 . 2 596 . 66 GLY HA2 H 3.46 . 2 597 . 66 GLY C C 173.60 . 1 598 . 67 GLU N N 121.40 . 1 599 . 67 GLU H H 7.91 . 1 600 . 67 GLU CA C 54.30 . 1 601 . 67 GLU HA H 4.83 . 1 602 . 67 GLU CB C 32.50 . 1 603 . 67 GLU HB3 H 2.18 . 2 604 . 67 GLU HB2 H 1.92 . 2 605 . 67 GLU CG C 36.10 . 1 606 . 67 GLU HG3 H 2.26 . 2 607 . 67 GLU C C 175.50 . 1 608 . 68 GLU N N 126.90 . 1 609 . 68 GLU H H 8.94 . 1 610 . 68 GLU CA C 58.00 . 1 611 . 68 GLU HA H 4.43 . 1 612 . 68 GLU CB C 30.50 . 1 613 . 68 GLU HB3 H 2.03 . 2 614 . 68 GLU HB2 H 1.98 . 2 615 . 68 GLU CG C 37.70 . 1 616 . 68 GLU HG3 H 2.16 . 2 617 . 68 GLU C C 175.90 . 1 618 . 69 CYS N N 126.00 . 1 619 . 69 CYS H H 9.30 . 1 620 . 69 CYS CA C 56.40 . 1 621 . 69 CYS HA H 5.17 . 1 622 . 69 CYS CB C 32.50 . 1 623 . 69 CYS HB3 H 3.45 . 2 624 . 69 CYS HB2 H 3.09 . 2 625 . 69 CYS C C 172.40 . 1 626 . 70 GLU N N 121.60 . 1 627 . 70 GLU H H 8.38 . 1 628 . 70 GLU CA C 55.80 . 1 629 . 70 GLU HA H 5.00 . 1 630 . 70 GLU CB C 32.00 . 1 631 . 70 GLU HB3 H 1.92 . 2 632 . 70 GLU CG C 37.80 . 1 633 . 70 GLU HG3 H 2.17 . 2 634 . 70 GLU HG2 H 1.99 . 2 635 . 70 GLU C C 175.40 . 1 636 . 71 LEU N N 128.70 . 1 637 . 71 LEU H H 9.06 . 1 638 . 71 LEU CA C 53.40 . 1 639 . 71 LEU HA H 4.59 . 1 640 . 71 LEU CB C 44.70 . 1 641 . 71 LEU HB3 H 1.15 . 2 642 . 71 LEU HB2 H 1.05 . 2 643 . 71 LEU CG C 26.50 . 1 644 . 71 LEU HG H 1.33 . 1 645 . 71 LEU CD1 C 25.20 . 2 646 . 71 LEU HD1 H 0.30 . 2 647 . 71 LEU CD2 C 23.80 . 2 648 . 71 LEU HD2 H 0.42 . 2 649 . 71 LEU C C 175.60 . 1 650 . 72 GLU N N 126.00 . 1 651 . 72 GLU H H 9.47 . 1 652 . 72 GLU CA C 55.80 . 1 653 . 72 GLU CB C 31.10 . 1 654 . 74 MET CA C 58.70 . 1 655 . 74 MET HA H 3.93 . 1 656 . 74 MET CB C 32.40 . 1 657 . 74 MET HB3 H 2.39 . 2 658 . 74 MET CG C 32.80 . 1 659 . 74 MET C C 175.90 . 1 660 . 75 THR N N 106.80 . 1 661 . 75 THR H H 7.48 . 1 662 . 75 THR CA C 61.60 . 1 663 . 75 THR HA H 4.25 . 1 664 . 75 THR CB C 68.70 . 1 665 . 75 THR HB H 3.87 . 1 666 . 75 THR HG2 H 1.11 . 1 667 . 75 THR C C 175.80 . 1 668 . 76 GLY N N 112.60 . 1 669 . 76 GLY H H 7.90 . 1 670 . 76 GLY CA C 45.20 . 1 671 . 76 GLY HA3 H 4.39 . 2 672 . 76 GLY HA2 H 3.91 . 2 673 . 76 GLY C C 173.90 . 1 674 . 77 GLU N N 123.00 . 1 675 . 77 GLU H H 7.35 . 1 676 . 77 GLU CA C 56.20 . 1 677 . 77 GLU HA H 4.25 . 1 678 . 77 GLU CB C 30.90 . 1 679 . 77 GLU HB3 H 1.82 . 2 680 . 77 GLU CG C 36.40 . 1 681 . 77 GLU HG3 H 2.23 . 2 682 . 77 GLU HG2 H 2.12 . 2 683 . 77 GLU C C 175.50 . 1 684 . 78 LYS N N 125.80 . 1 685 . 78 LYS H H 8.51 . 1 686 . 78 LYS CA C 54.90 . 1 687 . 78 LYS HA H 5.31 . 1 688 . 78 LYS CB C 33.50 . 1 689 . 78 LYS HB3 H 1.75 . 2 690 . 78 LYS HB2 H 1.53 . 2 691 . 78 LYS CG C 25.50 . 1 692 . 78 LYS HG3 H 1.51 . 2 693 . 78 LYS HG2 H 1.29 . 2 694 . 78 LYS CD C 29.10 . 1 695 . 78 LYS HD3 H 1.61 . 2 696 . 78 LYS CE C 42.50 . 1 697 . 78 LYS HE3 H 3.01 . 2 698 . 78 LYS C C 176.50 . 1 699 . 79 VAL N N 120.80 . 1 700 . 79 VAL H H 8.95 . 1 701 . 79 VAL CA C 58.90 . 1 702 . 79 VAL HA H 4.68 . 1 703 . 79 VAL CB C 35.30 . 1 704 . 79 VAL HB H 2.08 . 1 705 . 79 VAL CG2 C 22.10 . 2 706 . 79 VAL HG2 H 0.80 . 2 707 . 79 VAL CG1 C 19.90 . 2 708 . 79 VAL HG1 H 0.52 . 2 709 . 79 VAL C C 174.20 . 1 710 . 80 LYS N N 124.80 . 1 711 . 80 LYS H H 8.30 . 1 712 . 80 LYS CA C 55.70 . 1 713 . 80 LYS HA H 5.07 . 1 714 . 80 LYS CB C 33.00 . 1 715 . 80 LYS HB3 H 1.81 . 2 716 . 80 LYS HB2 H 1.71 . 2 717 . 80 LYS CG C 25.30 . 1 718 . 80 LYS HG3 H 1.40 . 2 719 . 80 LYS CD C 29.10 . 1 720 . 80 LYS HD3 H 1.63 . 2 721 . 80 LYS CE C 41.70 . 1 722 . 80 LYS HE3 H 2.99 . 2 723 . 80 LYS C C 176.40 . 1 724 . 81 ALA N N 128.70 . 1 725 . 81 ALA H H 8.94 . 1 726 . 81 ALA CA C 51.50 . 1 727 . 81 ALA HA H 4.84 . 1 728 . 81 ALA CB C 23.40 . 1 729 . 81 ALA HB H 1.25 . 1 730 . 81 ALA C C 174.90 . 1 731 . 82 VAL N N 120.10 . 1 732 . 82 VAL H H 8.39 . 1 733 . 82 VAL CA C 61.90 . 1 734 . 82 VAL HA H 4.29 . 1 735 . 82 VAL CB C 34.40 . 1 736 . 82 VAL HB H 1.93 . 1 737 . 82 VAL CG2 C 21.00 . 2 738 . 82 VAL HG2 H 0.88 . 2 739 . 82 VAL CG1 C 20.80 . 2 740 . 82 VAL HG1 H 0.72 . 2 741 . 82 VAL C C 176.10 . 1 742 . 83 VAL N N 136.40 . 1 743 . 83 VAL H H 9.74 . 1 744 . 83 VAL CA C 61.50 . 1 745 . 83 VAL HA H 4.50 . 1 746 . 83 VAL CB C 31.50 . 1 747 . 83 VAL HB H 1.57 . 1 748 . 83 VAL CG2 C 22.00 . 2 749 . 83 VAL HG2 H 0.59 . 2 750 . 83 VAL CG1 C 18.70 . 2 751 . 83 VAL HG1 H -0.10 . 2 752 . 83 VAL C C 174.90 . 1 753 . 84 LYS N N 127.30 . 1 754 . 84 LYS H H 8.89 . 1 755 . 84 LYS CA C 54.60 . 1 756 . 84 LYS HA H 4.94 . 1 757 . 84 LYS CB C 36.60 . 1 758 . 84 LYS HB3 H 1.79 . 2 759 . 84 LYS HB2 H 1.70 . 2 760 . 84 LYS CG C 25.30 . 1 761 . 84 LYS HG3 H 1.36 . 2 762 . 84 LYS CD C 29.70 . 1 763 . 84 LYS HD3 H 1.70 . 2 764 . 84 LYS CE C 42.30 . 1 765 . 84 LYS HE3 H 2.96 . 2 766 . 84 LYS C C 175.60 . 1 767 . 85 MET N N 121.70 . 1 768 . 85 MET H H 8.77 . 1 769 . 85 MET CA C 54.20 . 1 770 . 85 MET HA H 5.49 . 1 771 . 85 MET CB C 32.30 . 1 772 . 85 MET HB3 H 2.38 . 2 773 . 85 MET HB2 H 2.02 . 2 774 . 85 MET CG C 32.40 . 1 775 . 85 MET HG3 H 2.80 . 2 776 . 85 MET HG2 H 2.62 . 2 777 . 85 MET C C 177.30 . 1 778 . 86 GLU N N 128.50 . 1 779 . 86 GLU H H 8.66 . 1 780 . 86 GLU CA C 55.90 . 1 781 . 86 GLU HA H 4.61 . 1 782 . 86 GLU CB C 32.30 . 1 783 . 86 GLU HB3 H 1.92 . 2 784 . 86 GLU HB2 H 1.76 . 2 785 . 86 GLU CG C 36.80 . 1 786 . 86 GLU HG3 H 2.18 . 2 787 . 86 GLU HG2 H 2.12 . 2 788 . 86 GLU C C 175.90 . 1 789 . 87 GLY N N 115.00 . 1 790 . 87 GLY H H 8.47 . 1 791 . 87 GLY CA C 45.70 . 1 792 . 87 GLY HA3 H 4.22 . 2 793 . 87 GLY HA2 H 3.82 . 2 794 . 87 GLY C C 173.90 . 1 795 . 88 ASP N N 120.20 . 1 796 . 88 ASP H H 8.56 . 1 797 . 88 ASP CA C 55.30 . 1 798 . 88 ASP HA H 4.75 . 1 799 . 88 ASP CB C 42.00 . 1 800 . 88 ASP HB3 H 2.73 . 2 801 . 88 ASP C C 178.00 . 1 802 . 89 ASN N N 116.00 . 1 803 . 89 ASN H H 8.15 . 1 804 . 89 ASN CA C 53.30 . 1 805 . 89 ASN HA H 5.17 . 1 806 . 89 ASN CB C 40.00 . 1 807 . 89 ASN HB3 H 3.80 . 2 808 . 89 ASN HB2 H 2.85 . 2 809 . 89 ASN C C 174.30 . 1 810 . 90 LYS N N 119.60 . 1 811 . 90 LYS H H 7.37 . 1 812 . 90 LYS CA C 55.00 . 1 813 . 90 LYS HA H 5.95 . 1 814 . 90 LYS CB C 36.50 . 1 815 . 90 LYS HB3 H 2.15 . 2 816 . 90 LYS HB2 H 1.59 . 2 817 . 90 LYS CG C 25.30 . 1 818 . 90 LYS HG3 H 1.19 . 2 819 . 90 LYS CD C 29.70 . 1 820 . 90 LYS HD3 H 1.56 . 2 821 . 90 LYS CE C 44.90 . 1 822 . 90 LYS HE3 H 2.89 . 2 823 . 90 LYS C C 175.50 . 1 824 . 91 MET N N 122.50 . 1 825 . 91 MET H H 8.89 . 1 826 . 91 MET CA C 55.30 . 1 827 . 91 MET HA H 5.29 . 1 828 . 91 MET CB C 32.50 . 1 829 . 91 MET HB3 H 2.12 . 2 830 . 91 MET HB2 H 2.05 . 2 831 . 91 MET HG3 H 1.74 . 2 832 . 91 MET C C 175.10 . 1 833 . 92 VAL CA C 60.60 . 1 834 . 92 VAL HA H 5.30 . 1 835 . 92 VAL CB C 35.80 . 1 836 . 92 VAL HB H 2.03 . 1 837 . 92 VAL CG2 C 21.10 . 2 838 . 92 VAL HG2 H 0.95 . 2 839 . 92 VAL C C 178.30 . 1 840 . 93 THR N N 121.60 . 1 841 . 93 THR H H 8.87 . 1 842 . 93 THR CA C 61.30 . 1 843 . 93 THR HA H 4.84 . 1 844 . 93 THR CB C 69.30 . 1 845 . 93 THR HB H 4.10 . 1 846 . 93 THR CG2 C 18.20 . 1 847 . 93 THR HG2 H 0.95 . 1 848 . 93 THR C C 172.00 . 1 849 . 94 THR N N 119.60 . 1 850 . 94 THR H H 8.03 . 1 851 . 94 THR CA C 59.80 . 1 852 . 94 THR HA H 5.46 . 1 853 . 94 THR CB C 71.50 . 1 854 . 94 THR HB H 4.04 . 1 855 . 94 THR CG2 C 21.10 . 1 856 . 94 THR HG2 H 1.10 . 1 857 . 94 THR C C 173.20 . 1 858 . 95 PHE N N 122.90 . 1 859 . 95 PHE H H 8.09 . 1 860 . 95 PHE CA C 56.10 . 1 861 . 95 PHE HA H 4.86 . 1 862 . 95 PHE CB C 39.90 . 1 863 . 95 PHE HB3 H 3.28 . 2 864 . 95 PHE HB2 H 2.74 . 2 865 . 95 PHE C C 173.60 . 1 866 . 96 LYS N N 121.30 . 1 867 . 96 LYS H H 9.40 . 1 868 . 96 LYS CA C 56.50 . 1 869 . 96 LYS HA H 3.93 . 1 870 . 96 LYS CB C 30.40 . 1 871 . 96 LYS HB3 H 2.18 . 2 872 . 96 LYS HB2 H 1.87 . 2 873 . 96 LYS CG C 25.40 . 1 874 . 96 LYS HG3 H 1.67 . 2 875 . 96 LYS HG2 H 1.59 . 2 876 . 96 LYS CD C 28.90 . 1 877 . 96 LYS HD3 H 1.79 . 2 878 . 96 LYS HD2 H 1.71 . 2 879 . 96 LYS CE C 41.70 . 1 880 . 96 LYS HE3 H 3.03 . 2 881 . 96 LYS C C 175.70 . 1 882 . 97 GLY N N 106.90 . 1 883 . 97 GLY H H 8.43 . 1 884 . 97 GLY CA C 45.50 . 1 885 . 97 GLY HA3 H 4.04 . 2 886 . 97 GLY HA2 H 3.54 . 2 887 . 97 GLY C C 173.70 . 1 888 . 98 ILE N N 125.50 . 1 889 . 98 ILE H H 8.38 . 1 890 . 98 ILE CA C 60.40 . 1 891 . 98 ILE HA H 4.42 . 1 892 . 98 ILE CB C 39.20 . 1 893 . 98 ILE HB H 1.50 . 1 894 . 98 ILE CG1 C 28.00 . 2 895 . 98 ILE HG13 H 1.48 . 2 896 . 98 ILE CD1 C 18.00 . 1 897 . 98 ILE HD1 H 0.68 . 1 898 . 98 ILE CG2 C 18.20 . 1 899 . 98 ILE HG2 H 0.77 . 1 900 . 98 ILE C C 175.90 . 1 901 . 99 LYS N N 128.80 . 1 902 . 99 LYS H H 8.12 . 1 903 . 99 LYS CA C 55.50 . 1 904 . 99 LYS HA H 4.76 . 1 905 . 99 LYS CB C 34.10 . 1 906 . 99 LYS HB3 H 1.84 . 2 907 . 99 LYS HB2 H 1.71 . 2 908 . 99 LYS CG C 25.40 . 1 909 . 99 LYS HG3 H 1.44 . 2 910 . 99 LYS HG2 H 1.30 . 2 911 . 99 LYS CD C 29.50 . 1 912 . 99 LYS HD3 H 1.63 . 2 913 . 99 LYS CE C 42.40 . 1 914 . 99 LYS HE3 H 2.84 . 2 915 . 99 LYS C C 175.70 . 1 916 . 100 SER N N 124.40 . 1 917 . 100 SER H H 8.97 . 1 918 . 100 SER CA C 55.80 . 1 919 . 100 SER HA H 5.47 . 1 920 . 100 SER CB C 64.40 . 1 921 . 100 SER HB3 H 3.80 . 2 922 . 100 SER HB2 H 3.42 . 2 923 . 100 SER C C 173.60 . 1 924 . 101 VAL N N 130.50 . 1 925 . 101 VAL H H 9.02 . 1 926 . 101 VAL CA C 61.70 . 1 927 . 101 VAL HA H 4.71 . 1 928 . 101 VAL CB C 35.00 . 1 929 . 101 VAL HB H 2.00 . 1 930 . 101 VAL CG2 C 21.10 . 2 931 . 101 VAL HG2 H 0.89 . 2 932 . 101 VAL CG1 C 21.20 . 2 933 . 101 VAL HG1 H 0.73 . 2 934 . 101 VAL C C 175.80 . 1 935 . 102 THR N N 128.80 . 1 936 . 102 THR H H 9.18 . 1 937 . 102 THR CA C 61.90 . 1 938 . 102 THR HA H 5.01 . 1 939 . 102 THR CB C 69.90 . 1 940 . 102 THR HB H 3.83 . 1 941 . 102 THR CG2 C 25.50 . 1 942 . 102 THR HG2 H 0.99 . 1 943 . 102 THR C C 172.20 . 1 944 . 103 GLU N N 129.80 . 1 945 . 103 GLU H H 9.11 . 1 946 . 103 GLU CA C 54.40 . 1 947 . 103 GLU HA H 5.06 . 1 948 . 103 GLU CB C 33.40 . 1 949 . 103 GLU HB3 H 1.71 . 2 950 . 103 GLU CG C 37.00 . 1 951 . 103 GLU HG3 H 2.08 . 2 952 . 103 GLU HG2 H 2.01 . 2 953 . 103 GLU C C 174.40 . 1 954 . 104 PHE N N 128.20 . 1 955 . 104 PHE H H 8.79 . 1 956 . 104 PHE CA C 57.30 . 1 957 . 104 PHE HA H 4.58 . 1 958 . 104 PHE CB C 40.40 . 1 959 . 104 PHE HB3 H 2.93 . 2 960 . 104 PHE HB2 H 2.77 . 2 961 . 104 PHE C C 175.10 . 1 962 . 105 ASN N N 125.70 . 1 963 . 105 ASN H H 8.29 . 1 964 . 105 ASN CA C 52.40 . 1 965 . 105 ASN HA H 5.04 . 1 966 . 105 ASN CB C 40.40 . 1 967 . 105 ASN HB3 H 2.84 . 2 968 . 105 ASN HB2 H 2.58 . 2 969 . 105 ASN C C 175.30 . 1 970 . 106 GLY CA C 47.80 . 1 971 . 106 GLY HA3 H 4.23 . 2 972 . 106 GLY HA2 H 3.60 . 2 973 . 106 GLY C C 174.40 . 1 974 . 107 ASP N N 128.70 . 1 975 . 107 ASP H H 8.77 . 1 976 . 107 ASP CA C 54.50 . 1 977 . 107 ASP HA H 4.82 . 1 978 . 107 ASP CB C 41.70 . 1 979 . 107 ASP HB3 H 2.98 . 2 980 . 107 ASP HB2 H 2.91 . 2 981 . 107 ASP C C 175.20 . 1 982 . 108 THR N N 114.30 . 1 983 . 108 THR H H 7.77 . 1 984 . 108 THR CA C 61.00 . 1 985 . 108 THR HA H 5.37 . 1 986 . 108 THR CB C 71.90 . 1 987 . 108 THR HB H 4.12 . 1 988 . 108 THR CG2 C 21.30 . 1 989 . 108 THR HG2 H 1.17 . 1 990 . 108 THR C C 173.60 . 1 991 . 110 THR CA C 61.60 . 1 992 . 110 THR HA H 5.04 . 1 993 . 110 THR CB C 70.60 . 1 994 . 110 THR HB H 3.93 . 1 995 . 110 THR CG2 C 21.40 . 1 996 . 110 THR HG2 H 1.05 . 1 997 . 110 THR C C 173.80 . 1 998 . 111 ASN N N 129.80 . 1 999 . 111 ASN H H 9.31 . 1 1000 . 111 ASN CA C 52.00 . 1 1001 . 111 ASN HA H 5.72 . 1 1002 . 111 ASN CB C 43.00 . 1 1003 . 111 ASN HB3 H 2.59 . 2 1004 . 111 ASN HB2 H 2.49 . 2 1005 . 111 ASN C C 173.60 . 1 1006 . 112 THR N N 122.40 . 1 1007 . 112 THR H H 9.08 . 1 1008 . 112 THR CA C 60.80 . 1 1009 . 112 THR HA H 5.09 . 1 1010 . 112 THR CB C 70.40 . 1 1011 . 112 THR HB H 3.86 . 1 1012 . 112 THR CG2 C 22.10 . 1 1013 . 112 THR HG2 H 1.00 . 1 1014 . 112 THR C C 174.10 . 1 1015 . 113 MET N N 127.90 . 1 1016 . 113 MET H H 9.19 . 1 1017 . 113 MET CA C 54.80 . 1 1018 . 113 MET HA H 5.45 . 1 1019 . 113 MET CB C 37.30 . 1 1020 . 113 MET HB3 H 1.90 . 2 1021 . 113 MET HB2 H 1.76 . 2 1022 . 113 MET CG C 33.20 . 1 1023 . 113 MET HG3 H 2.56 . 2 1024 . 113 MET HG2 H 2.36 . 2 1025 . 113 MET C C 174.00 . 1 1026 . 114 THR N N 120.50 . 1 1027 . 114 THR H H 8.81 . 1 1028 . 114 THR CA C 61.60 . 1 1029 . 114 THR HA H 5.31 . 1 1030 . 114 THR CB C 70.80 . 1 1031 . 114 THR HB H 4.00 . 1 1032 . 114 THR CG2 C 22.30 . 1 1033 . 114 THR HG2 H 1.20 . 1 1034 . 114 THR C C 173.60 . 1 1035 . 115 LEU N N 132.20 . 1 1036 . 115 LEU H H 8.92 . 1 1037 . 115 LEU CA C 54.20 . 1 1038 . 115 LEU HA H 4.69 . 1 1039 . 115 LEU CB C 44.90 . 1 1040 . 115 LEU HB3 H 1.73 . 2 1041 . 115 LEU HB2 H 1.30 . 2 1042 . 115 LEU CG C 27.70 . 1 1043 . 115 LEU HG H 1.41 . 1 1044 . 115 LEU CD1 C 26.00 . 2 1045 . 115 LEU HD1 H 0.53 . 2 1046 . 115 LEU CD2 C 23.20 . 2 1047 . 115 LEU HD2 H 0.70 . 2 1048 . 115 LEU C C 176.20 . 1 1049 . 116 GLY N N 119.70 . 1 1050 . 116 GLY H H 9.06 . 1 1051 . 116 GLY CA C 47.60 . 1 1052 . 116 GLY HA3 H 3.96 . 2 1053 . 116 GLY HA2 H 3.63 . 2 1054 . 116 GLY C C 174.40 . 1 1055 . 117 ASP N N 128.20 . 1 1056 . 117 ASP H H 8.64 . 1 1057 . 117 ASP CA C 54.10 . 1 1058 . 117 ASP HA H 4.64 . 1 1059 . 117 ASP CB C 41.10 . 1 1060 . 117 ASP HB3 H 2.72 . 2 1061 . 117 ASP HB2 H 2.62 . 2 1062 . 117 ASP C C 175.80 . 1 1063 . 118 ILE N N 124.50 . 1 1064 . 118 ILE H H 8.31 . 1 1065 . 118 ILE CA C 61.70 . 1 1066 . 118 ILE HA H 4.09 . 1 1067 . 118 ILE CB C 39.10 . 1 1068 . 118 ILE HB H 2.26 . 1 1069 . 118 ILE CG1 C 27.30 . 2 1070 . 118 ILE HG13 H 1.72 . 2 1071 . 118 ILE HG12 H 1.09 . 2 1072 . 118 ILE CD1 C 18.10 . 1 1073 . 118 ILE HD1 H 1.00 . 1 1074 . 118 ILE CG2 C 13.80 . 1 1075 . 118 ILE HG2 H 0.82 . 1 1076 . 118 ILE C C 174.40 . 1 1077 . 119 VAL N N 129.30 . 1 1078 . 119 VAL H H 8.34 . 1 1079 . 119 VAL CA C 61.50 . 1 1080 . 119 VAL HA H 4.69 . 1 1081 . 119 VAL CB C 32.70 . 1 1082 . 119 VAL HB H 2.00 . 1 1083 . 119 VAL CG2 C 21.50 . 2 1084 . 119 VAL HG2 H 0.74 . 2 1085 . 119 VAL CG1 C 20.20 . 2 1086 . 119 VAL HG1 H 0.89 . 2 1087 . 119 VAL C C 176.20 . 1 1088 . 120 TYR N N 133.20 . 1 1089 . 120 TYR H H 9.24 . 1 1090 . 120 TYR CA C 54.80 . 1 1091 . 120 TYR HA H 5.25 . 1 1092 . 120 TYR CB C 39.80 . 1 1093 . 120 TYR HB3 H 2.58 . 2 1094 . 120 TYR HB2 H 2.10 . 2 1095 . 120 TYR C C 174.10 . 1 1096 . 121 LYS N N 131.90 . 1 1097 . 121 LYS H H 8.10 . 1 1098 . 121 LYS CA C 54.60 . 1 1099 . 121 LYS HA H 5.12 . 1 1100 . 121 LYS CB C 37.20 . 1 1101 . 121 LYS HB3 H 1.55 . 2 1102 . 121 LYS HB2 H 1.47 . 2 1103 . 121 LYS CG C 25.40 . 1 1104 . 121 LYS HG3 H 1.24 . 2 1105 . 121 LYS HG2 H 1.10 . 2 1106 . 121 LYS CD C 29.70 . 1 1107 . 121 LYS HD3 H 1.47 . 2 1108 . 121 LYS CE C 41.90 . 1 1109 . 121 LYS HE3 H 2.71 . 2 1110 . 121 LYS C C 174.40 . 1 1111 . 123 VAL CA C 61.90 . 1 1112 . 123 VAL HA H 4.91 . 1 1113 . 123 VAL CB C 33.70 . 1 1114 . 123 VAL HB H 2.08 . 1 1115 . 123 VAL CG2 C 21.00 . 2 1116 . 123 VAL HG2 H 0.90 . 2 1117 . 123 VAL C C 176.10 . 1 1118 . 124 SER N N 125.00 . 1 1119 . 124 SER H H 9.35 . 1 1120 . 124 SER CA C 57.60 . 1 1121 . 124 SER HA H 5.47 . 1 1122 . 124 SER CB C 65.70 . 1 1123 . 124 SER HB3 H 3.52 . 2 1124 . 124 SER HB2 H 3.45 . 2 1125 . 124 SER C C 171.60 . 1 1126 . 125 LYS N N 125.00 . 1 1127 . 125 LYS H H 8.76 . 1 1128 . 125 LYS CA C 54.20 . 1 1129 . 125 LYS HA H 5.45 . 1 1130 . 125 LYS CB C 36.60 . 1 1131 . 125 LYS HB3 H 1.90 . 2 1132 . 125 LYS HB2 H 1.77 . 2 1133 . 125 LYS CG C 24.90 . 1 1134 . 125 LYS HG3 H 1.54 . 2 1135 . 125 LYS CD C 29.30 . 1 1136 . 125 LYS HD3 H 1.72 . 2 1137 . 125 LYS CE C 42.40 . 1 1138 . 125 LYS HE3 H 2.99 . 2 1139 . 125 LYS C C 175.60 . 1 1140 . 126 ARG N N 129.30 . 1 1141 . 126 ARG H H 8.88 . 1 1142 . 126 ARG CA C 57.60 . 1 1143 . 126 ARG HA H 4.28 . 1 1144 . 126 ARG CB C 31.60 . 1 1145 . 126 ARG HB3 H 1.77 . 2 1146 . 126 ARG CG C 27.30 . 1 1147 . 126 ARG HG3 H 1.66 . 2 1148 . 126 ARG HG2 H 1.41 . 2 1149 . 126 ARG CD C 43.80 . 1 1150 . 126 ARG HD3 H 3.39 . 2 1151 . 126 ARG HD2 H 3.18 . 2 1152 . 126 ARG C C 175.80 . 1 1153 . 127 ILE N N 132.20 . 1 1154 . 127 ILE H H 8.40 . 1 1155 . 127 ILE CA C 63.00 . 1 1156 . 127 ILE HA H 4.21 . 1 1157 . 127 ILE CB C 40.20 . 1 1158 . 127 ILE HB H 1.86 . 1 1159 . 127 ILE CG1 C 27.30 . 2 1160 . 127 ILE HG13 H 1.29 . 2 1161 . 127 ILE HG12 H 0.87 . 2 1162 . 127 ILE CD1 C 14.60 . 1 1163 . 127 ILE HD1 H 0.84 . 1 1164 . 127 ILE CG2 C 18.70 . 1 1165 . 127 ILE HG2 H 0.93 . 1 1166 . 127 ILE C C 180.90 . 1 stop_ save_