data_5044 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical shift assignments for the third Immunoglobulin domain from the neural cell adhesion molecule, N-CAM ; _BMRB_accession_number 5044 _BMRB_flat_file_name bmr5044.str _Entry_type original _Submission_date 2001-06-05 _Accession_date 2001-06-05 _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 Atkins A. R. . 2 Chung J. . . 3 Deechongkit S. . . 4 Little E. B. . 5 Edelman G. M. . 6 Wright P. E. . 7 Cunningham B. A. . 8 Dyson H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 607 "13C chemical shifts" 324 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-14 original author . stop_ _Original_release_date 2001-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the Third Immunoglobulin Domain of the Neural Cell Adhesion Molecule N-CAM: Can Solution Studies Define the Mechanism of Homophilic Binding? ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21363704 _PubMed_ID 11469865 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Atkins A. R. . 2 Chung J. . . 3 Deechongkit S. . . 4 Little E. B. . 5 Edelman G. M. . 6 Wright P. E. . 7 Cunningham B. A. . 8 Dyson H. J. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 311 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 161 _Page_last 172 _Year 2001 _Details . loop_ _Keyword 'Intermediate Immunoglobulin fold' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_DYANA _Saveframe_category citation _Citation_full . _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P. . . 2 Mumenthaler C. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _Journal_issue 1 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ save_ref_SANE _Saveframe_category citation _Citation_full . _Citation_title 'SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11370778 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Duggan 'B. M.' M. . 2 Legge 'G. B.' B. . 3 Dyson 'H. J.' J. . 4 Wright 'P. E.' E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 19 _Journal_issue 4 _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 321 _Page_last 329 _Year 2001 _Details ; A reliable automated approach for assignment of NOESY spectra would allow more rapid determination of protein structures by NMR. In this paper we describe a semi-automated procedure for complete NOESY assignment (SANE, Structure Assisted NOE Evaluation), coupled to an iterative procedure for NMR structure determination where the user is directly involved. Our method is similar to ARIA [Nilges et al. (1997) J. Mol. Biol., 269, 408-422], but is compatible with the molecular dynamics suites AMBER and DYANA. The method is ideal for systems where an initial model or crystal structure is available, but has also been used successfully for ab initio structure determination. Use of this semi-automated iterative approach assists in the identification of errors in the NOE assignments to short-cut the path to an NMR solution structure. ; save_ save_ref_AMBER _Saveframe_category citation _Citation_full . _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 11183777 _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_ref_NMRView _Saveframe_category citation _Citation_full . _Citation_title 'NMRView: A computer program for the visualization and analysis of NMR data' _Citation_status . _Citation_type journal _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_ref_NMRPipe _Saveframe_category citation _Citation_full . _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes' _Citation_status . _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96088118 _PubMed_ID ? 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. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _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 . save_ ################################## # Molecular system description # ################################## save_system_N-CAM _Saveframe_category molecular_system _Mol_system_name 'NEURAL CELL ADHESION MOLECULE' _Abbreviation_common N-CAM _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IgIII $N-CAM_IgIII stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'cell adhesion molecule' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_N-CAM_IgIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Third Immunoglobulin domain of the Neural cell adhesion molecule' _Abbreviation_common 'N-CAM IgIII' _Molecular_mass 11839 _Mol_thiol_state 'all disulfide bound' _Details 'Third immunoglobulin domain' ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; GKDIQVIVNVPPSVRARQST MNATANLSQSVTLACDADGF PEPTMTWTKDGEPIEQEDNE EKYSFNYDGSELIIKKVDKS DEAEYICIAENKAGEQDATI HLKVFAK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 LYS 3 ASP 4 ILE 5 GLN 6 VAL 7 ILE 8 VAL 9 ASN 10 VAL 11 PRO 12 PRO 13 SER 14 VAL 15 ARG 16 ALA 17 ARG 18 GLN 19 SER 20 THR 21 MET 22 ASN 23 ALA 24 THR 25 ALA 26 ASN 27 LEU 28 SER 29 GLN 30 SER 31 VAL 32 THR 33 LEU 34 ALA 35 CYS 36 ASP 37 ALA 38 ASP 39 GLY 40 PHE 41 PRO 42 GLU 43 PRO 44 THR 45 MET 46 THR 47 TRP 48 THR 49 LYS 50 ASP 51 GLY 52 GLU 53 PRO 54 ILE 55 GLU 56 GLN 57 GLU 58 ASP 59 ASN 60 GLU 61 GLU 62 LYS 63 TYR 64 SER 65 PHE 66 ASN 67 TYR 68 ASP 69 GLY 70 SER 71 GLU 72 LEU 73 ILE 74 ILE 75 LYS 76 LYS 77 VAL 78 ASP 79 LYS 80 SER 81 ASP 82 GLU 83 ALA 84 GLU 85 TYR 86 ILE 87 CYS 88 ILE 89 ALA 90 GLU 91 ASN 92 LYS 93 ALA 94 GLY 95 GLU 96 GLN 97 ASP 98 ALA 99 THR 100 ILE 101 HIS 102 LEU 103 LYS 104 VAL 105 PHE 106 ALA 107 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 1IE5 "Nmr Structure Of The Third Immunoglobulin Domain From The Neural Cell Adhesion Molecule" 100.00 107 100.00 100.00 2.21e-72 REF XP_010213927 "PREDICTED: neural cell adhesion molecule 1-like, partial [Tinamus guttatus]" 99.07 407 97.17 100.00 5.07e-66 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $N-CAM_IgIII chicken 9031 Eukaryota Metazoa gallus gallus 'membrane protein' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $N-CAM_IgIII 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pET3d stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $N-CAM_IgIII 1.0 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details . _Citation_label $ref_NMRPipe save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure calculations' stop_ _Details 'Dyana was used to generate starting structures for subsequent refinement in AMBER' _Citation_label $ref_DYANA save_ save_AMBER _Saveframe_category software _Name AMBER _Version 7 loop_ _Task 'structure refinement' stop_ _Details 'restrained molecular dynamics and simulated annealing' _Citation_label $ref_AMBER save_ save_NMRView _Saveframe_category software _Name NMRView _Version 3 loop_ _Task 'data analysis' stop_ _Details 'viewing and annotation of spectra' _Citation_label $ref_NMRView save_ save_SANE _Saveframe_category software _Name SANE _Version 1 loop_ _Task 'noe assignments' stop_ _Details 'Assignment of noe crosspeaks using distance and structural filters' _Citation_label $ref_SANE save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D_13C-separated NOESY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D_15N-separated NOESY' _Sample_label $sample_1 save_ save_HNHB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $sample_1 save_ save_CGCN_4 _Saveframe_category NMR_applied_experiment _Experiment_name CGCN _Sample_label $sample_1 save_ save_CGCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name CGCO _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D_13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D_15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CGCN _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CGCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . mM pH* 6.8 0.2 n/a pressure 1 . atm temperature 298 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name IgIII _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY HA2 H 3.84 0.05 1 2 . 1 GLY HA3 H 3.84 0.05 1 3 . 1 GLY CA C 43.524 0.05 1 4 . 2 LYS HA H 4.328 0.05 1 5 . 2 LYS HB2 H 1.813 0.05 2 6 . 2 LYS HB3 H 1.742 0.05 2 7 . 2 LYS HG2 H 1.403 0.05 1 8 . 2 LYS HG3 H 1.403 0.05 1 9 . 2 LYS HD2 H 1.675 0.05 1 10 . 2 LYS HD3 H 1.675 0.05 1 11 . 2 LYS HE2 H 2.991 0.05 1 12 . 2 LYS HE3 H 2.991 0.05 1 13 . 2 LYS CA C 56.563 0.05 1 14 . 2 LYS CB C 33.231 0.05 1 15 . 2 LYS CG C 24.574 0.05 1 16 . 2 LYS CD C 29.074 0.05 1 17 . 2 LYS CE C 42.163 0.05 1 18 . 3 ASP H H 8.488 0.05 1 19 . 3 ASP HA H 4.596 0.05 1 20 . 3 ASP HB2 H 2.556 0.05 2 21 . 3 ASP HB3 H 2.68 0.05 2 22 . 3 ASP CA C 54.404 0.05 1 23 . 3 ASP CB C 41.112 0.05 1 24 . 3 ASP N N 122.576 0.05 1 25 . 4 ILE H H 8.116 0.05 1 26 . 4 ILE HA H 4.144 0.05 1 27 . 4 ILE HB H 1.84 0.05 1 28 . 4 ILE HG12 H 1.168 0.05 2 29 . 4 ILE HG13 H 1.44 0.05 2 30 . 4 ILE HG2 H 0.882 0.05 1 31 . 4 ILE HD1 H 0.854 0.05 1 32 . 4 ILE CA C 61.062 0.05 1 33 . 4 ILE CB C 38.75 0.05 1 34 . 4 ILE CG1 C 27.218 0.05 1 35 . 4 ILE CG2 C 17.561 0.05 1 36 . 4 ILE CD1 C 13 0.05 1 37 . 4 ILE N N 121.8 0.05 1 38 . 5 GLN H H 8.425 0.05 1 39 . 5 GLN HA H 4.339 0.05 1 40 . 5 GLN HB2 H 1.949 0.05 2 41 . 5 GLN HB3 H 2.029 0.05 2 42 . 5 GLN HG2 H 2.319 0.05 1 43 . 5 GLN HG3 H 2.319 0.05 1 44 . 5 GLN HE21 H 7.567 0.05 2 45 . 5 GLN HE22 H 6.846 0.05 2 46 . 5 GLN CA C 55.661 0.05 1 47 . 5 GLN CB C 29.624 0.05 1 48 . 5 GLN CG C 33.834 0.05 1 49 . 5 GLN N N 125.415 0.05 1 50 . 5 GLN NE2 N 133.301 0.05 1 51 . 6 VAL H H 8.164 0.05 1 52 . 6 VAL HA H 4.044 0.05 1 53 . 6 VAL HB H 1.961 0.05 1 54 . 6 VAL HG1 H 0.837 0.05 2 55 . 6 VAL HG2 H 0.882 0.05 2 56 . 6 VAL CA C 62.31 0.05 1 57 . 6 VAL CB C 32.729 0.05 1 58 . 6 VAL CG1 C 21.114 0.05 2 59 . 6 VAL CG2 C 20.631 0.05 2 60 . 6 VAL N N 123.452 0.05 1 61 . 7 ILE H H 8.226 0.05 1 62 . 7 ILE HA H 4.072 0.05 1 63 . 7 ILE HB H 1.717 0.05 1 64 . 7 ILE HG12 H 1.082 0.05 2 65 . 7 ILE HG13 H 1.403 0.05 2 66 . 7 ILE HG2 H 0.685 0.05 1 67 . 7 ILE HD1 H 0.761 0.05 1 68 . 7 ILE CA C 60.876 0.05 1 69 . 7 ILE CB C 38.465 0.05 1 70 . 7 ILE CG1 C 27.3 0.05 1 71 . 7 ILE CG2 C 17.573 0.05 1 72 . 7 ILE CD1 C 12.512 0.05 1 73 . 7 ILE N N 126.891 0.05 1 74 . 8 VAL H H 7.983 0.05 1 75 . 8 VAL HA H 4.118 0.05 1 76 . 8 VAL HB H 1.973 0.05 1 77 . 8 VAL HG1 H 0.891 0.05 2 78 . 8 VAL HG2 H 0.863 0.05 2 79 . 8 VAL CA C 61.627 0.05 1 80 . 8 VAL CB C 33.23 0.05 1 81 . 8 VAL CG1 C 21.173 0.05 2 82 . 8 VAL CG2 C 20.396 0.05 2 83 . 8 VAL N N 125.938 0.05 1 84 . 9 ASN H H 8.349 0.05 1 85 . 9 ASN HA H 5.019 0.05 1 86 . 9 ASN HB2 H 2.673 0.05 1 87 . 9 ASN HB3 H 2.673 0.05 1 88 . 9 ASN HD21 H 7.478 0.05 1 89 . 9 ASN HD22 H 6.742 0.05 1 90 . 9 ASN CA C 53.267 0.05 1 91 . 9 ASN CB C 39.295 0.05 1 92 . 9 ASN N N 122.741 0.05 1 93 . 9 ASN ND2 N 111.14 0.05 1 94 . 10 VAL H H 9.914 0.05 1 95 . 10 VAL HA H 4.609 0.05 1 96 . 10 VAL HB H 1.974 0.05 1 97 . 10 VAL HG1 H 1.065 0.05 2 98 . 10 VAL HG2 H 0.979 0.05 2 99 . 10 VAL CA C 59.485 0.05 1 100 . 10 VAL CB C 35.708 0.05 1 101 . 10 VAL CG1 C 20.516 0.05 2 102 . 10 VAL CG2 C 20.773 0.05 2 103 . 10 VAL N N 125.32 0.05 1 104 . 11 PRO HA H 4.531 0.05 1 105 . 11 PRO HB2 H 2.001 0.05 2 106 . 11 PRO HB3 H 2.072 0.05 2 107 . 11 PRO HG2 H 2.043 0.05 1 108 . 11 PRO HG3 H 2.043 0.05 1 109 . 11 PRO HD2 H 3.735 0.05 1 110 . 11 PRO HD3 H 3.828 0.05 1 111 . 11 PRO CA C 61.22 0.05 1 112 . 11 PRO CB C 30.482 0.05 1 113 . 11 PRO CG C 27.438 0.05 1 114 . 11 PRO CD C 51.563 0.05 1 115 . 12 PRO HA H 5.005 0.05 1 116 . 12 PRO HB2 H 1.801 0.05 2 117 . 12 PRO HB3 H 1.407 0.05 2 118 . 12 PRO HG2 H 1.44 0.05 2 119 . 12 PRO HG3 H 1.805 0.05 2 120 . 12 PRO HD2 H 2.908 0.05 2 121 . 12 PRO HD3 H 3.786 0.05 2 122 . 12 PRO CA C 62.387 0.05 1 123 . 12 PRO CB C 33.352 0.05 1 124 . 12 PRO CG C 27.987 0.05 1 125 . 12 PRO CD C 49.923 0.05 1 126 . 13 SER H H 8.117 0.05 1 127 . 13 SER HA H 4.662 0.05 1 128 . 13 SER HB2 H 3.739 0.05 1 129 . 13 SER HB3 H 3.739 0.05 1 130 . 13 SER CA C 56.724 0.05 1 131 . 13 SER CB C 65.495 0.05 1 132 . 13 SER N N 115.97 0.05 1 133 . 14 VAL H H 8.695 0.05 1 134 . 14 VAL HA H 5.109 0.05 1 135 . 14 VAL HB H 1.576 0.05 1 136 . 14 VAL HG1 H 0.627 0.05 2 137 . 14 VAL HG2 H 0.712 0.05 2 138 . 14 VAL CA C 59.722 0.05 1 139 . 14 VAL CB C 35.498 0.05 1 140 . 14 VAL CG1 C 20.37 0.05 2 141 . 14 VAL CG2 C 24.421 0.05 2 142 . 14 VAL N N 121.673 0.05 1 143 . 15 ARG H H 8.193 0.05 1 144 . 15 ARG HA H 4.57 0.05 1 145 . 15 ARG HB2 H 1.683 0.05 2 146 . 15 ARG HB3 H 1.796 0.05 2 147 . 15 ARG HG2 H 1.55 0.05 2 148 . 15 ARG HG3 H 1.663 0.05 2 149 . 15 ARG HD2 H 3.2 0.05 1 150 . 15 ARG HD3 H 3.2 0.05 1 151 . 15 ARG HE H 7.241 0.05 1 152 . 15 ARG CA C 54.078 0.05 1 153 . 15 ARG CB C 33.262 0.05 1 154 . 15 ARG CG C 26.02 0.05 1 155 . 15 ARG CD C 43.195 0.05 1 156 . 15 ARG N N 124.899 0.05 1 157 . 15 ARG NE N 85.05 0.05 1 158 . 16 ALA H H 8.977 0.05 1 159 . 16 ALA HA H 4.812 0.05 1 160 . 16 ALA HB H 1.217 0.05 1 161 . 16 ALA CA C 52.026 0.05 1 162 . 16 ALA CB C 19.137 0.05 1 163 . 16 ALA N N 128.004 0.05 1 164 . 17 ARG H H 8.858 0.05 1 165 . 17 ARG HA H 4.058 0.05 1 166 . 17 ARG HB2 H 1.727 0.05 2 167 . 17 ARG HB3 H 1.841 0.05 2 168 . 17 ARG HG2 H 1.481 0.05 1 169 . 17 ARG HG3 H 1.481 0.05 1 170 . 17 ARG HD2 H 3.014 0.05 2 171 . 17 ARG HD3 H 3.22 0.05 2 172 . 17 ARG HE H 8.075 0.05 1 173 . 17 ARG CA C 60.078 0.05 1 174 . 17 ARG CB C 29.863 0.05 1 175 . 17 ARG CG C 27.798 0.05 1 176 . 17 ARG CD C 43.138 0.05 1 177 . 17 ARG N N 126.247 0.05 1 178 . 17 ARG NE N 85.048 0.05 1 179 . 18 GLN H H 7.437 0.05 1 180 . 18 GLN HA H 4.569 0.05 1 181 . 18 GLN HB2 H 2.077 0.05 2 182 . 18 GLN HB3 H 2.148 0.05 2 183 . 18 GLN HG2 H 2.417 0.05 2 184 . 18 GLN HG3 H 2.466 0.05 2 185 . 18 GLN HE21 H 7.666 0.05 1 186 . 18 GLN HE22 H 6.917 0.05 1 187 . 18 GLN CA C 55.823 0.05 1 188 . 18 GLN CB C 31.477 0.05 1 189 . 18 GLN CG C 34.114 0.05 1 190 . 18 GLN N N 115.329 0.05 1 191 . 18 GLN NE2 N 112.5 0.05 1 192 . 19 SER H H 8.825 0.05 1 193 . 19 SER HA H 4.485 0.05 1 194 . 19 SER HB2 H 4.043 0.05 2 195 . 19 SER HB3 H 4.165 0.05 2 196 . 19 SER CA C 61.066 0.05 1 197 . 19 SER CB C 63.868 0.05 1 198 . 19 SER N N 118.843 0.05 1 199 . 20 THR H H 7.877 0.05 1 200 . 20 THR HA H 5.253 0.05 1 201 . 20 THR HB H 4.154 0.05 1 202 . 20 THR HG2 H 1.265 0.05 1 203 . 20 THR CA C 61.316 0.05 1 204 . 20 THR CB C 70.828 0.05 1 205 . 20 THR CG2 C 21.724 0.05 1 206 . 20 THR N N 117.299 0.05 1 207 . 21 MET H H 8.781 0.05 1 208 . 21 MET HA H 4.843 0.05 1 209 . 21 MET HB2 H 1.641 0.05 1 210 . 21 MET HB3 H 1.979 0.05 1 211 . 21 MET HG2 H 2.321 0.05 1 212 . 21 MET HG3 H 2.321 0.05 1 213 . 21 MET HE H 2.12 0.05 1 214 . 21 MET CA C 53.993 0.05 1 215 . 21 MET CB C 36.84 0.05 1 216 . 21 MET CG C 32.155 0.05 1 217 . 21 MET CE C 16.771 0.05 1 218 . 21 MET N N 124.356 0.05 1 219 . 22 ASN H H 8.598 0.05 1 220 . 22 ASN HA H 5.92 0.05 1 221 . 22 ASN HB2 H 2.607 0.05 1 222 . 22 ASN HB3 H 2.607 0.05 1 223 . 22 ASN HD21 H 7.384 0.05 1 224 . 22 ASN HD22 H 6.756 0.05 1 225 . 22 ASN CA C 52.005 0.05 1 226 . 22 ASN CB C 42.406 0.05 1 227 . 22 ASN N N 120.479 0.05 1 228 . 22 ASN ND2 N 113.2 0.05 1 229 . 23 ALA H H 8.642 0.05 1 230 . 23 ALA HA H 4.687 0.05 1 231 . 23 ALA HB H 1.288 0.05 1 232 . 23 ALA CA C 50.95 0.05 1 233 . 23 ALA CB C 23.254 0.05 1 234 . 23 ALA N N 122.674 0.05 1 235 . 24 THR H H 8.472 0.05 1 236 . 24 THR HA H 4.897 0.05 1 237 . 24 THR HB H 3.854 0.05 1 238 . 24 THR HG2 H 1.281 0.05 1 239 . 24 THR CA C 62.011 0.05 1 240 . 24 THR CB C 70.222 0.05 1 241 . 24 THR CG2 C 22.057 0.05 1 242 . 24 THR N N 117.614 0.05 1 243 . 25 ALA H H 8.667 0.05 1 244 . 25 ALA HA H 3.981 0.05 1 245 . 25 ALA HB H 1.36 0.05 1 246 . 25 ALA CA C 52.574 0.05 1 247 . 25 ALA CB C 19.873 0.05 1 248 . 25 ALA N N 128.363 0.05 1 249 . 26 ASN H H 8.063 0.05 1 250 . 26 ASN HA H 4.565 0.05 1 251 . 26 ASN HB2 H 2.954 0.05 2 252 . 26 ASN HB3 H 3.032 0.05 2 253 . 26 ASN HD21 H 7.724 0.05 1 254 . 26 ASN HD22 H 6.975 0.05 1 255 . 26 ASN CA C 55.155 0.05 1 256 . 26 ASN CB C 37.434 0.05 1 257 . 26 ASN N N 112.974 0.05 1 258 . 26 ASN ND2 N 113.48 0.05 1 259 . 27 LEU H H 8.402 0.05 1 260 . 27 LEU HA H 4.508 0.05 1 261 . 27 LEU HB2 H 1.409 0.05 2 262 . 27 LEU HB3 H 1.694 0.05 2 263 . 27 LEU HG H 1.591 0.05 1 264 . 27 LEU HD1 H 0.876 0.05 2 265 . 27 LEU HD2 H 0.895 0.05 2 266 . 27 LEU CA C 54.928 0.05 1 267 . 27 LEU CB C 43.321 0.05 1 268 . 27 LEU CG C 26.586 0.05 1 269 . 27 LEU CD1 C 22.979 0.05 2 270 . 27 LEU CD2 C 25.503 0.05 2 271 . 27 LEU N N 120.32 0.05 1 272 . 28 SER H H 8.839 0.05 1 273 . 28 SER HA H 3.976 0.05 1 274 . 28 SER HB2 H 4.057 0.05 1 275 . 28 SER HB3 H 4.057 0.05 1 276 . 28 SER CA C 59.436 0.05 1 277 . 28 SER CB C 62.269 0.05 1 278 . 28 SER N N 115.772 0.05 1 279 . 29 GLN H H 8.648 0.05 1 280 . 29 GLN HA H 4.366 0.05 1 281 . 29 GLN HB2 H 2.022 0.05 2 282 . 29 GLN HB3 H 2.087 0.05 2 283 . 29 GLN HG2 H 2.383 0.05 1 284 . 29 GLN HG3 H 2.383 0.05 1 285 . 29 GLN HE21 H 7.48 0.05 1 286 . 29 GLN HE22 H 6.947 0.05 1 287 . 29 GLN CA C 56.2 0.05 1 288 . 29 GLN CB C 30.141 0.05 1 289 . 29 GLN CG C 34.264 0.05 1 290 . 29 GLN N N 122.1 0.05 1 291 . 29 GLN NE2 N 112.287 0.05 1 292 . 30 SER H H 8.182 0.05 1 293 . 30 SER HA H 5.556 0.05 1 294 . 30 SER HB2 H 3.638 0.05 1 295 . 30 SER HB3 H 3.638 0.05 1 296 . 30 SER CA C 56.293 0.05 1 297 . 30 SER CB C 65.945 0.05 1 298 . 30 SER N N 115.336 0.05 1 299 . 31 VAL H H 8.696 0.05 1 300 . 31 VAL HA H 4.466 0.05 1 301 . 31 VAL HB H 1.793 0.05 1 302 . 31 VAL HG1 H 0.756 0.05 2 303 . 31 VAL HG2 H 0.747 0.05 2 304 . 31 VAL CA C 60.226 0.05 1 305 . 31 VAL CB C 35.445 0.05 1 306 . 31 VAL CG1 C 21.028 0.05 1 307 . 31 VAL CG2 C 21.457 0.05 1 308 . 31 VAL N N 120.124 0.05 1 309 . 32 THR H H 8.215 0.05 1 310 . 32 THR HA H 4.848 0.05 1 311 . 32 THR HB H 3.836 0.05 1 312 . 32 THR HG2 H 0.882 0.05 1 313 . 32 THR CA C 61.584 0.05 1 314 . 32 THR CB C 69.817 0.05 1 315 . 32 THR CG2 C 21.282 0.05 1 316 . 32 THR N N 121.225 0.05 1 317 . 33 LEU H H 9.435 0.05 1 318 . 33 LEU HA H 4.438 0.05 1 319 . 33 LEU HB2 H 1.208 0.05 1 320 . 33 LEU HB3 H 1.471 0.05 1 321 . 33 LEU HG H 1.439 0.05 1 322 . 33 LEU HD1 H 0.413 0.05 1 323 . 33 LEU HD2 H 0.198 0.05 1 324 . 33 LEU CA C 54.215 0.05 1 325 . 33 LEU CB C 42.56 0.05 1 326 . 33 LEU CG C 28.871 0.05 1 327 . 33 LEU CD1 C 24.986 0.05 1 328 . 33 LEU CD2 C 25.87 0.05 1 329 . 33 LEU N N 132.109 0.05 1 330 . 34 ALA H H 8.178 0.05 1 331 . 34 ALA HA H 5.877 0.05 1 332 . 34 ALA HB H 1.267 0.05 1 333 . 34 ALA CA C 51.347 0.05 1 334 . 34 ALA CB C 23.607 0.05 1 335 . 34 ALA N N 121.823 0.05 1 336 . 35 CYS H H 9.126 0.05 1 337 . 35 CYS HA H 4.94 0.05 1 338 . 35 CYS HB2 H 2.525 0.05 2 339 . 35 CYS HB3 H 2.911 0.05 2 340 . 35 CYS CA C 54.141 0.05 1 341 . 35 CYS CB C 47.196 0.05 1 342 . 35 CYS N N 120.157 0.05 1 343 . 36 ASP H H 8.581 0.05 1 344 . 36 ASP HA H 4.977 0.05 1 345 . 36 ASP HB2 H 2.423 0.05 1 346 . 36 ASP HB3 H 2.594 0.05 1 347 . 36 ASP CA C 53.702 0.05 1 348 . 36 ASP CB C 42.903 0.05 1 349 . 36 ASP N N 120.877 0.05 1 350 . 37 ALA H H 9.134 0.05 1 351 . 37 ALA HA H 5.513 0.05 1 352 . 37 ALA HB H 1.182 0.05 1 353 . 37 ALA CA C 50.082 0.05 1 354 . 37 ALA CB C 23.677 0.05 1 355 . 37 ALA N N 128.167 0.05 1 356 . 38 ASP H H 8.582 0.05 1 357 . 38 ASP HA H 4.958 0.05 1 358 . 38 ASP HB2 H 2.612 0.05 1 359 . 38 ASP HB3 H 2.612 0.05 1 360 . 38 ASP CA C 52.436 0.05 1 361 . 38 ASP CB C 44.2 0.05 1 362 . 38 ASP N N 120.678 0.05 1 363 . 39 GLY H H 7.97 0.05 1 364 . 39 GLY HA2 H 3.464 0.05 2 365 . 39 GLY HA3 H 3.913 0.05 2 366 . 39 GLY CA C 44.497 0.05 1 367 . 39 GLY N N 106.228 0.05 1 368 . 40 PHE H H 8.325 0.05 1 369 . 40 PHE HA H 4.473 0.05 1 370 . 40 PHE HB2 H 2.987 0.05 1 371 . 40 PHE HB3 H 2.987 0.05 1 372 . 40 PHE HD1 H 7.35 0.05 1 373 . 40 PHE HD2 H 7.35 0.05 1 374 . 40 PHE HE1 H 6.93 0.05 1 375 . 40 PHE HE2 H 6.93 0.05 1 376 . 40 PHE CA C 56.918 0.05 1 377 . 40 PHE CB C 42.669 0.05 1 378 . 40 PHE N N 119.795 0.05 1 379 . 41 PRO HA H 3.302 0.05 1 380 . 41 PRO HB2 H 1.751 0.05 2 381 . 41 PRO HB3 H 2.157 0.05 2 382 . 41 PRO HG2 H 1.415 0.05 1 383 . 41 PRO HG3 H 1.415 0.05 1 384 . 41 PRO HD2 H 2.868 0.05 2 385 . 41 PRO HD3 H 3.692 0.05 2 386 . 41 PRO CA C 62.328 0.05 1 387 . 41 PRO CB C 34.309 0.05 1 388 . 41 PRO CG C 26.136 0.05 1 389 . 41 PRO CD C 49.277 0.05 1 390 . 42 GLU H H 8.908 0.05 1 391 . 42 GLU HA H 4.156 0.05 1 392 . 42 GLU HB2 H 2.018 0.05 1 393 . 42 GLU HB3 H 2.018 0.05 1 394 . 42 GLU HG2 H 2.493 0.05 2 395 . 42 GLU HG3 H 2.535 0.05 2 396 . 42 GLU CA C 55.676 0.05 1 397 . 42 GLU CB C 29.224 0.05 1 398 . 42 GLU CG C 36.153 0.05 1 399 . 42 GLU N N 124.207 0.05 1 400 . 43 PRO HA H 4.548 0.05 1 401 . 43 PRO HB2 H 1.702 0.05 1 402 . 43 PRO HB3 H 1.702 0.05 1 403 . 43 PRO HG2 H 1.572 0.05 2 404 . 43 PRO HG3 H 1.76 0.05 2 405 . 43 PRO HD2 H 3.474 0.05 2 406 . 43 PRO HD3 H 3.635 0.05 2 407 . 43 PRO CA C 62.529 0.05 1 408 . 43 PRO CB C 33.289 0.05 1 409 . 43 PRO CG C 27.281 0.05 1 410 . 43 PRO CD C 50.94 0.05 1 411 . 44 THR H H 8.748 0.05 1 412 . 44 THR HA H 4.588 0.05 1 413 . 44 THR HB H 4.194 0.05 1 414 . 44 THR HG2 H 1.2 0.05 1 415 . 44 THR CA C 61.024 0.05 1 416 . 44 THR CB C 70.468 0.05 1 417 . 44 THR CG2 C 21.975 0.05 1 418 . 44 THR N N 114.419 0.05 1 419 . 45 MET H H 8.598 0.05 1 420 . 45 MET HA H 5.739 0.05 1 421 . 45 MET HB2 H 1.738 0.05 1 422 . 45 MET HB3 H 1.93 0.05 1 423 . 45 MET HG2 H 2.069 0.05 2 424 . 45 MET HG3 H 2.233 0.05 2 425 . 45 MET HE H 1.686 0.05 1 426 . 45 MET CA C 53.883 0.05 1 427 . 45 MET CB C 34.726 0.05 1 428 . 45 MET CG C 32.486 0.05 1 429 . 45 MET CE C 16.805 0.05 1 430 . 45 MET N N 123.863 0.05 1 431 . 46 THR H H 8.583 0.05 1 432 . 46 THR HA H 4.608 0.05 1 433 . 46 THR HB H 4.191 0.05 1 434 . 46 THR HG2 H 1.175 0.05 1 435 . 46 THR CA C 60.968 0.05 1 436 . 46 THR CB C 72.134 0.05 1 437 . 46 THR CG2 C 21.989 0.05 1 438 . 46 THR N N 118.219 0.05 1 439 . 47 TRP H H 8.942 0.05 1 440 . 47 TRP HA H 6.007 0.05 1 441 . 47 TRP HB2 H 3.184 0.05 1 442 . 47 TRP HB3 H 2.955 0.05 1 443 . 47 TRP HD1 H 7.169 0.05 1 444 . 47 TRP HE1 H 10.795 0.05 1 445 . 47 TRP HE3 H 6.978 0.05 1 446 . 47 TRP HZ2 H 7.335 0.05 1 447 . 47 TRP HZ3 H 6.71 0.05 1 448 . 47 TRP HH2 H 6.67 0.05 1 449 . 47 TRP CA C 56.538 0.05 1 450 . 47 TRP CB C 33.717 0.05 1 451 . 47 TRP N N 121.075 0.05 1 452 . 47 TRP NE1 N 130.521 0.05 1 453 . 48 THR H H 9.408 0.05 1 454 . 48 THR HA H 5.046 0.05 1 455 . 48 THR HB H 3.615 0.05 1 456 . 48 THR HG2 H 0.859 0.05 1 457 . 48 THR CA C 59.249 0.05 1 458 . 48 THR CB C 72.576 0.05 1 459 . 48 THR CG2 C 20.715 0.05 1 460 . 48 THR N N 111.421 0.05 1 461 . 49 LYS H H 9.086 0.05 1 462 . 49 LYS HA H 4.268 0.05 1 463 . 49 LYS HB2 H 1.385 0.05 2 464 . 49 LYS HB3 H 1.81 0.05 2 465 . 49 LYS HG2 H 1.251 0.05 2 466 . 49 LYS HG3 H 1.333 0.05 2 467 . 49 LYS HD2 H 1.633 0.05 1 468 . 49 LYS HD3 H 1.633 0.05 1 469 . 49 LYS HE2 H 2.946 0.05 1 470 . 49 LYS HE3 H 2.946 0.05 1 471 . 49 LYS CA C 54.592 0.05 1 472 . 49 LYS CB C 35.075 0.05 1 473 . 49 LYS CG C 25.005 0.05 1 474 . 49 LYS CD C 29.778 0.05 1 475 . 49 LYS CE C 42.536 0.05 1 476 . 49 LYS N N 122.112 0.05 1 477 . 50 ASP H H 9.691 0.05 1 478 . 50 ASP HA H 4.438 0.05 1 479 . 50 ASP HB2 H 2.591 0.05 2 480 . 50 ASP HB3 H 3.004 0.05 2 481 . 50 ASP CA C 55.915 0.05 1 482 . 50 ASP CB C 39.792 0.05 1 483 . 50 ASP N N 131.71 0.05 1 484 . 51 GLY H H 8.67 0.05 1 485 . 51 GLY HA2 H 3.494 0.05 2 486 . 51 GLY HA3 H 4.281 0.05 2 487 . 51 GLY CA C 45.04 0.05 1 488 . 51 GLY N N 102.315 0.05 1 489 . 52 GLU H H 7.973 0.05 1 490 . 52 GLU HA H 4.965 0.05 1 491 . 52 GLU HB2 H 2.126 0.05 1 492 . 52 GLU HB3 H 1.988 0.05 1 493 . 52 GLU HG2 H 2.24 0.05 2 494 . 52 GLU HG3 H 2.356 0.05 2 495 . 52 GLU CA C 52.874 0.05 1 496 . 52 GLU CB C 30.628 0.05 1 497 . 52 GLU CG C 35.483 0.05 1 498 . 52 GLU N N 122.569 0.05 1 499 . 53 PRO HA H 4.547 0.05 1 500 . 53 PRO HB2 H 1.873 0.05 2 501 . 53 PRO HB3 H 2.364 0.05 2 502 . 53 PRO HG2 H 1.94 0.05 2 503 . 53 PRO HG3 H 2.154 0.05 2 504 . 53 PRO HD2 H 3.756 0.05 2 505 . 53 PRO HD3 H 3.962 0.05 2 506 . 53 PRO CA C 63.735 0.05 1 507 . 53 PRO CB C 32.425 0.05 1 508 . 53 PRO CG C 27.719 0.05 1 509 . 53 PRO CD C 50.991 0.05 1 510 . 54 ILE H H 8.12 0.05 1 511 . 54 ILE HA H 4.088 0.05 1 512 . 54 ILE HB H 1.67 0.05 1 513 . 54 ILE HG12 H 0.891 0.05 1 514 . 54 ILE HG13 H 1.485 0.05 1 515 . 54 ILE HG2 H 0.237 0.05 1 516 . 54 ILE HD1 H 0.652 0.05 1 517 . 54 ILE CA C 61.227 0.05 1 518 . 54 ILE CB C 38.427 0.05 1 519 . 54 ILE CG1 C 27.198 0.05 1 520 . 54 ILE CG2 C 16.986 0.05 1 521 . 54 ILE CD1 C 13.749 0.05 1 522 . 54 ILE N N 124.39 0.05 1 523 . 55 GLU H H 8.523 0.05 1 524 . 55 GLU HA H 4.487 0.05 1 525 . 55 GLU HB2 H 2.103 0.05 1 526 . 55 GLU HB3 H 1.945 0.05 1 527 . 55 GLU HG2 H 2.289 0.05 1 528 . 55 GLU HG3 H 2.289 0.05 1 529 . 55 GLU CA C 55.258 0.05 1 530 . 55 GLU CB C 30.979 0.05 1 531 . 55 GLU CG C 35.833 0.05 1 532 . 55 GLU N N 127.431 0.05 1 533 . 56 GLN H H 8.592 0.05 1 534 . 56 GLN HA H 4.282 0.05 1 535 . 56 GLN HB2 H 1.892 0.05 2 536 . 56 GLN HB3 H 2.016 0.05 2 537 . 56 GLN HG2 H 2.106 0.05 1 538 . 56 GLN HG3 H 2.309 0.05 1 539 . 56 GLN HE21 H 7.48 0.05 1 540 . 56 GLN HE22 H 6.953 0.05 1 541 . 56 GLN CA C 57.04 0.05 1 542 . 56 GLN CB C 29.207 0.05 1 543 . 56 GLN CG C 33.884 0.05 1 544 . 56 GLN N N 122.56 0.05 1 545 . 56 GLN NE2 N 112.6 0.05 1 546 . 57 GLU H H 8.546 0.05 1 547 . 57 GLU HA H 4.408 0.05 1 548 . 57 GLU HB2 H 2.1 0.05 1 549 . 57 GLU HB3 H 2.1 0.05 1 550 . 57 GLU HG2 H 2.338 0.05 1 551 . 57 GLU HG3 H 2.338 0.05 1 552 . 57 GLU CA C 56.798 0.05 1 553 . 57 GLU CB C 30.493 0.05 1 554 . 57 GLU CG C 36.295 0.05 1 555 . 57 GLU N N 122.193 0.05 1 556 . 58 ASP H H 8.694 0.05 1 557 . 58 ASP HA H 4.555 0.05 1 558 . 58 ASP HB2 H 2.757 0.05 2 559 . 58 ASP HB3 H 2.843 0.05 2 560 . 58 ASP CA C 55.983 0.05 1 561 . 58 ASP CB C 40.556 0.05 1 562 . 58 ASP N N 121.219 0.05 1 563 . 59 ASN H H 8.31 0.05 1 564 . 59 ASN HA H 4.97 0.05 1 565 . 59 ASN HB2 H 2.868 0.05 2 566 . 59 ASN HB3 H 3.056 0.05 2 567 . 59 ASN HD21 H 7.849 0.05 1 568 . 59 ASN HD22 H 7.007 0.05 1 569 . 59 ASN CA C 52.88 0.05 1 570 . 59 ASN CB C 39.287 0.05 1 571 . 59 ASN N N 117.595 0.05 1 572 . 59 ASN ND2 N 113.74 0.05 1 573 . 60 GLU H H 8.715 0.05 1 574 . 60 GLU HA H 4.517 0.05 1 575 . 60 GLU HB2 H 2.028 0.05 2 576 . 60 GLU HB3 H 2.139 0.05 2 577 . 60 GLU HG2 H 2.39 0.05 2 578 . 60 GLU HG3 H 2.436 0.05 2 579 . 60 GLU CA C 57.77 0.05 1 580 . 60 GLU CB C 29.293 0.05 1 581 . 60 GLU CG C 36.841 0.05 1 582 . 60 GLU N N 120.981 0.05 1 583 . 61 GLU H H 8.354 0.05 1 584 . 61 GLU HA H 4.007 0.05 1 585 . 61 GLU HB2 H 1.935 0.05 1 586 . 61 GLU HB3 H 1.935 0.05 1 587 . 61 GLU HG2 H 2.205 0.05 1 588 . 61 GLU HG3 H 2.205 0.05 1 589 . 61 GLU CA C 57.931 0.05 1 590 . 61 GLU CB C 29.282 0.05 1 591 . 61 GLU CG C 36.442 0.05 1 592 . 61 GLU N N 118.103 0.05 1 593 . 62 LYS H H 8.099 0.05 1 594 . 62 LYS HA H 4.251 0.05 1 595 . 62 LYS HB2 H 1.277 0.05 2 596 . 62 LYS HB3 H 1.355 0.05 2 597 . 62 LYS HG2 H -0.148 0.05 1 598 . 62 LYS HG3 H 0.885 0.05 1 599 . 62 LYS HD2 H 1.64 0.05 1 600 . 62 LYS CA C 55.239 0.05 1 601 . 62 LYS CB C 34.492 0.05 1 602 . 62 LYS CG C 23.307 0.05 1 603 . 62 LYS CD C 27.086 0.05 1 604 . 62 LYS N N 120.141 0.05 1 605 . 63 TYR H H 7.91 0.05 1 606 . 63 TYR HA H 5.693 0.05 1 607 . 63 TYR HB2 H 2.46 0.05 1 608 . 63 TYR HB3 H 2.46 0.05 1 609 . 63 TYR HD1 H 6.97 0.05 1 610 . 63 TYR HD2 H 6.97 0.05 1 611 . 63 TYR HE1 H 6.75 0.05 1 612 . 63 TYR HE2 H 6.75 0.05 1 613 . 63 TYR CA C 54.87 0.05 1 614 . 63 TYR CB C 42.138 0.05 1 615 . 63 TYR N N 115.071 0.05 1 616 . 64 SER H H 8.613 0.05 1 617 . 64 SER HA H 4.752 0.05 1 618 . 64 SER HB2 H 3.539 0.05 2 619 . 64 SER HB3 H 3.715 0.05 2 620 . 64 SER CA C 57.411 0.05 1 621 . 64 SER CB C 65.96 0.05 1 622 . 64 SER N N 115.7 0.05 1 623 . 65 PHE H H 8.781 0.05 1 624 . 65 PHE HA H 5.449 0.05 1 625 . 65 PHE HB2 H 3.172 0.05 1 626 . 65 PHE HB3 H 2.967 0.05 1 627 . 65 PHE HD1 H 7.181 0.05 1 628 . 65 PHE HD2 H 7.181 0.05 1 629 . 65 PHE HE1 H 6.99 0.05 1 630 . 65 PHE HE2 H 6.99 0.05 1 631 . 65 PHE CA C 56.628 0.05 1 632 . 65 PHE CB C 42.835 0.05 1 633 . 65 PHE N N 123.973 0.05 1 634 . 66 ASN HD21 H 7.732 0.05 1 635 . 66 ASN HD22 H 6.7 0.05 1 636 . 66 ASN ND2 N 111.9 0.05 1 637 . 68 ASP HA H 4.658 0.05 1 638 . 68 ASP HB2 H 2.419 0.05 2 639 . 68 ASP HB3 H 3.07 0.05 2 640 . 68 ASP CA C 52.822 0.05 1 641 . 68 ASP CB C 40.117 0.05 1 642 . 69 GLY H H 7.714 0.05 1 643 . 69 GLY HA2 H 3.723 0.05 2 644 . 69 GLY HA3 H 4.429 0.05 2 645 . 69 GLY CA C 46.474 0.05 1 646 . 69 GLY N N 109.104 0.05 1 647 . 70 SER H H 8.429 0.05 1 648 . 70 SER HA H 4.558 0.05 1 649 . 70 SER HB2 H 3.979 0.05 1 650 . 70 SER HB3 H 3.979 0.05 1 651 . 70 SER CA C 61.099 0.05 1 652 . 70 SER CB C 63.985 0.05 1 653 . 70 SER N N 116.375 0.05 1 654 . 71 GLU H H 7.977 0.05 1 655 . 71 GLU HA H 5.171 0.05 1 656 . 71 GLU HB2 H 1.622 0.05 1 657 . 71 GLU HB3 H 1.622 0.05 1 658 . 71 GLU HG2 H 2.086 0.05 1 659 . 71 GLU HG3 H 2.086 0.05 1 660 . 71 GLU CA C 54.76 0.05 1 661 . 71 GLU CB C 32.517 0.05 1 662 . 71 GLU CG C 36.709 0.05 1 663 . 71 GLU N N 118.319 0.05 1 664 . 72 LEU H H 8.596 0.05 1 665 . 72 LEU HA H 4.137 0.05 1 666 . 72 LEU HB2 H -0.547 0.05 1 667 . 72 LEU HB3 H 0.211 0.05 1 668 . 72 LEU HG H 0.609 0.05 1 669 . 72 LEU HD1 H -0.17 0.05 2 670 . 72 LEU HD2 H -0.307 0.05 2 671 . 72 LEU CA C 52.775 0.05 1 672 . 72 LEU CB C 42.556 0.05 1 673 . 72 LEU CG C 26.627 0.05 1 674 . 72 LEU CD1 C 25.737 0.05 2 675 . 72 LEU CD2 C 21.848 0.05 2 676 . 72 LEU N N 127.173 0.05 1 677 . 73 ILE H H 8.77 0.05 1 678 . 73 ILE HA H 4.523 0.05 1 679 . 73 ILE HB H 1.518 0.05 1 680 . 73 ILE HG12 H 1 0.05 1 681 . 73 ILE HG13 H 1.441 0.05 1 682 . 73 ILE HG2 H 0.568 0.05 1 683 . 73 ILE HD1 H 0.673 0.05 1 684 . 73 ILE CA C 60.51 0.05 1 685 . 73 ILE CB C 39.118 0.05 1 686 . 73 ILE CG1 C 27.935 0.05 1 687 . 73 ILE CG2 C 17.73 0.05 1 688 . 73 ILE CD1 C 14.124 0.05 1 689 . 73 ILE N N 127.763 0.05 1 690 . 74 ILE H H 8.655 0.05 1 691 . 74 ILE HA H 4.335 0.05 1 692 . 74 ILE HB H 1.485 0.05 1 693 . 74 ILE HG12 H 0.701 0.05 2 694 . 74 ILE HG13 H 1.349 0.05 2 695 . 74 ILE HG2 H 0.653 0.05 1 696 . 74 ILE HD1 H 0.394 0.05 1 697 . 74 ILE CA C 60.766 0.05 1 698 . 74 ILE CB C 38.402 0.05 1 699 . 74 ILE CG1 C 26.703 0.05 1 700 . 74 ILE CG2 C 17.639 0.05 1 701 . 74 ILE CD1 C 13.866 0.05 1 702 . 74 ILE N N 126.982 0.05 1 703 . 75 LYS H H 8.621 0.05 1 704 . 75 LYS HA H 4.319 0.05 1 705 . 75 LYS HB2 H 1.618 0.05 1 706 . 75 LYS HB3 H 1.618 0.05 1 707 . 75 LYS HG2 H 1.153 0.05 2 708 . 75 LYS HG3 H 1.081 0.05 2 709 . 75 LYS HD2 H 1.46 0.05 1 710 . 75 LYS HD3 H 1.46 0.05 1 711 . 75 LYS HE2 H 2.97 0.05 1 712 . 75 LYS HE3 H 2.97 0.05 1 713 . 75 LYS CA C 55.279 0.05 1 714 . 75 LYS CB C 33.987 0.05 1 715 . 75 LYS CG C 26.182 0.05 1 716 . 75 LYS CD C 29.041 0.05 1 717 . 75 LYS CE C 42.218 0.05 1 718 . 75 LYS N N 125.72 0.05 1 719 . 76 LYS H H 8.473 0.05 1 720 . 76 LYS HA H 3.482 0.05 1 721 . 76 LYS HB2 H 1.735 0.05 2 722 . 76 LYS HB3 H 1.6 0.05 2 723 . 76 LYS HG2 H 1.272 0.05 2 724 . 76 LYS HG3 H 1.241 0.05 2 725 . 76 LYS HD2 H 1.621 0.05 1 726 . 76 LYS HD3 H 1.621 0.05 1 727 . 76 LYS HE2 H 2.907 0.05 1 728 . 76 LYS HE3 H 2.907 0.05 1 729 . 76 LYS CA C 56.113 0.05 1 730 . 76 LYS CB C 30.511 0.05 1 731 . 76 LYS CG C 24.522 0.05 1 732 . 76 LYS CD C 29.77 0.05 1 733 . 76 LYS CE C 42.04 0.05 1 734 . 76 LYS N N 118.069 0.05 1 735 . 77 VAL H H 8.178 0.05 1 736 . 77 VAL HA H 3.901 0.05 1 737 . 77 VAL HB H 1.717 0.05 1 738 . 77 VAL HG1 H 0.674 0.05 1 739 . 77 VAL HG2 H 0.74 0.05 1 740 . 77 VAL CA C 63.814 0.05 1 741 . 77 VAL CB C 31.566 0.05 1 742 . 77 VAL CG1 C 22.841 0.05 1 743 . 77 VAL CG2 C 23.483 0.05 1 744 . 77 VAL N N 119.38 0.05 1 745 . 78 ASP H H 9.738 0.05 1 746 . 78 ASP HA H 4.624 0.05 1 747 . 78 ASP HB2 H 2.662 0.05 2 748 . 78 ASP HB3 H 3.102 0.05 2 749 . 78 ASP CA C 52.642 0.05 1 750 . 78 ASP CB C 43.053 0.05 1 751 . 78 ASP N N 129.516 0.05 1 752 . 79 LYS H H 8.934 0.05 1 753 . 79 LYS HA H 3.808 0.05 1 754 . 79 LYS HB2 H 1.768 0.05 2 755 . 79 LYS HB3 H 1.93 0.05 2 756 . 79 LYS HG2 H 1.469 0.05 2 757 . 79 LYS HG3 H 1.54 0.05 2 758 . 79 LYS HD2 H 1.778 0.05 1 759 . 79 LYS HD3 H 1.778 0.05 1 760 . 79 LYS HE2 H 2.966 0.05 1 761 . 79 LYS HE3 H 2.966 0.05 1 762 . 79 LYS CA C 58.766 0.05 1 763 . 79 LYS CB C 32.062 0.05 1 764 . 79 LYS CG C 24.42 0.05 1 765 . 79 LYS CD C 28.809 0.05 1 766 . 79 LYS CE C 42.173 0.05 1 767 . 79 LYS N N 120.146 0.05 1 768 . 80 SER H H 8.639 0.05 1 769 . 80 SER HA H 4.338 0.05 1 770 . 80 SER HB2 H 4.078 0.05 1 771 . 80 SER HB3 H 3.916 0.05 1 772 . 80 SER CA C 60.888 0.05 1 773 . 80 SER CB C 62.857 0.05 1 774 . 80 SER N N 115.7 0.05 1 775 . 81 ASP H H 8.183 0.05 1 776 . 81 ASP HA H 4.57 0.05 1 777 . 81 ASP HB2 H 2.551 0.05 2 778 . 81 ASP HB3 H 2.847 0.05 2 779 . 81 ASP CA C 55.943 0.05 1 780 . 81 ASP CB C 41.544 0.05 1 781 . 81 ASP N N 119.89 0.05 1 782 . 82 GLU H H 7.631 0.05 1 783 . 82 GLU HA H 4.307 0.05 1 784 . 82 GLU HB2 H 2.039 0.05 2 785 . 82 GLU HB3 H 2.333 0.05 2 786 . 82 GLU HG2 H 2.194 0.05 2 787 . 82 GLU HG3 H 3.118 0.05 2 788 . 82 GLU CA C 57.926 0.05 1 789 . 82 GLU CB C 29.622 0.05 1 790 . 82 GLU CG C 36.019 0.05 1 791 . 82 GLU N N 124.646 0.05 1 792 . 83 ALA H H 8.164 0.05 1 793 . 83 ALA HA H 4.625 0.05 1 794 . 83 ALA HB H 1.048 0.05 1 795 . 83 ALA CA C 51.861 0.05 1 796 . 83 ALA CB C 22.035 0.05 1 797 . 83 ALA N N 129.58 0.05 1 798 . 84 GLU H H 8.287 0.05 1 799 . 84 GLU HA H 4.67 0.05 1 800 . 84 GLU HB2 H 1.97 0.05 2 801 . 84 GLU HB3 H 2.15 0.05 2 802 . 84 GLU HG2 H 1.846 0.05 1 803 . 84 GLU HG3 H 1.846 0.05 1 804 . 84 GLU CA C 55.78 0.05 1 805 . 84 GLU CB C 31.266 0.05 1 806 . 84 GLU CG C 37.802 0.05 1 807 . 84 GLU N N 119.442 0.05 1 808 . 85 TYR H H 9.73 0.05 1 809 . 85 TYR HA H 5.595 0.05 1 810 . 85 TYR HB2 H 3.016 0.05 2 811 . 85 TYR HB3 H 3.132 0.05 2 812 . 85 TYR HD1 H 6.97 0.05 1 813 . 85 TYR HD2 H 6.97 0.05 1 814 . 85 TYR HE1 H 6.83 0.05 1 815 . 85 TYR HE2 H 6.83 0.05 1 816 . 85 TYR CA C 56.907 0.05 1 817 . 85 TYR CB C 40.627 0.05 1 818 . 85 TYR N N 131.523 0.05 1 819 . 86 ILE H H 8.627 0.05 1 820 . 86 ILE HA H 5.133 0.05 1 821 . 86 ILE HB H 1.721 0.05 1 822 . 86 ILE HG12 H 1.037 0.05 2 823 . 86 ILE HG13 H 1.338 0.05 2 824 . 86 ILE HG2 H 0.612 0.05 1 825 . 86 ILE HD1 H 0.668 0.05 1 826 . 86 ILE CA C 59.437 0.05 1 827 . 86 ILE CB C 40.352 0.05 1 828 . 86 ILE CG1 C 28.4 0.05 1 829 . 86 ILE CG2 C 17.857 0.05 1 830 . 86 ILE CD1 C 13.661 0.05 1 831 . 86 ILE N N 123.404 0.05 1 832 . 87 CYS H H 8.44 0.05 1 833 . 87 CYS HA H 4.33 0.05 1 834 . 87 CYS HB2 H 2.33 0.05 1 835 . 87 CYS HB3 H 0.524 0.05 1 836 . 87 CYS CA C 51.979 0.05 1 837 . 87 CYS CB C 42.769 0.05 1 838 . 87 CYS N N 123.584 0.05 1 839 . 88 ILE H H 9.005 0.05 1 840 . 88 ILE HA H 4.033 0.05 1 841 . 88 ILE HB H 1.593 0.05 1 842 . 88 ILE HG12 H 0.709 0.05 1 843 . 88 ILE HG13 H 1.217 0.05 1 844 . 88 ILE HG2 H 0.627 0.05 1 845 . 88 ILE HD1 H 0.622 0.05 1 846 . 88 ILE CA C 61.099 0.05 1 847 . 88 ILE CB C 39.359 0.05 1 848 . 88 ILE CG1 C 28.364 0.05 1 849 . 88 ILE CG2 C 18.324 0.05 1 850 . 88 ILE CD1 C 14.954 0.05 1 851 . 88 ILE N N 124.538 0.05 1 852 . 89 ALA H H 9.028 0.05 1 853 . 89 ALA HA H 5.251 0.05 1 854 . 89 ALA HB H 0.979 0.05 1 855 . 89 ALA CA C 49.714 0.05 1 856 . 89 ALA CB C 21.68 0.05 1 857 . 89 ALA N N 131.385 0.05 1 858 . 90 GLU H H 8.65 0.05 1 859 . 90 GLU HA H 5.206 0.05 1 860 . 90 GLU HB2 H 1.854 0.05 1 861 . 90 GLU HB3 H 1.854 0.05 1 862 . 90 GLU HG2 H 2.076 0.05 2 863 . 90 GLU HG3 H 2.173 0.05 2 864 . 90 GLU CA C 54.868 0.05 1 865 . 90 GLU CB C 34.419 0.05 1 866 . 90 GLU CG C 36.451 0.05 1 867 . 90 GLU N N 121.308 0.05 1 868 . 91 ASN H H 9.019 0.05 1 869 . 91 ASN HA H 4.667 0.05 1 870 . 91 ASN HB2 H 2.569 0.05 2 871 . 91 ASN HB3 H 2.958 0.05 2 872 . 91 ASN HD21 H 8.105 0.05 1 873 . 91 ASN HD22 H 6.916 0.05 1 874 . 91 ASN CA C 51.876 0.05 1 875 . 91 ASN CB C 40.793 0.05 1 876 . 91 ASN N N 121.364 0.05 1 877 . 91 ASN ND2 N 108.598 0.05 1 878 . 92 LYS H H 8.22 0.05 1 879 . 92 LYS HA H 4.085 0.05 1 880 . 92 LYS HB2 H 1.774 0.05 2 881 . 92 LYS HB3 H 1.697 0.05 2 882 . 92 LYS HG2 H 1.337 0.05 1 883 . 92 LYS HG3 H 1.337 0.05 1 884 . 92 LYS HD2 H 1.638 0.05 1 885 . 92 LYS HD3 H 1.638 0.05 1 886 . 92 LYS HE2 H 2.907 0.05 1 887 . 92 LYS HE3 H 2.907 0.05 1 888 . 92 LYS CA C 58.101 0.05 1 889 . 92 LYS CB C 32.263 0.05 1 890 . 92 LYS CG C 23.827 0.05 1 891 . 92 LYS CD C 29.021 0.05 1 892 . 92 LYS CE C 41.745 0.05 1 893 . 92 LYS N N 115.078 0.05 1 894 . 93 ALA H H 7.883 0.05 1 895 . 93 ALA HA H 4.533 0.05 1 896 . 93 ALA HB H 1.232 0.05 1 897 . 93 ALA CA C 51.492 0.05 1 898 . 93 ALA CB C 19.868 0.05 1 899 . 93 ALA N N 120.106 0.05 1 900 . 94 GLY H H 7.816 0.05 1 901 . 94 GLY HA2 H 3.96 0.05 2 902 . 94 GLY HA3 H 4.406 0.05 2 903 . 94 GLY CA C 45.989 0.05 1 904 . 94 GLY N N 107.841 0.05 1 905 . 95 GLU H H 8.188 0.05 1 906 . 95 GLU HA H 5.483 0.05 1 907 . 95 GLU HB2 H 1.886 0.05 2 908 . 95 GLU HB3 H 1.91 0.05 2 909 . 95 GLU HG2 H 2.105 0.05 1 910 . 95 GLU HG3 H 2.105 0.05 1 911 . 95 GLU CA C 54.214 0.05 1 912 . 95 GLU CB C 33.086 0.05 1 913 . 95 GLU CG C 34.682 0.05 1 914 . 95 GLU N N 117.73 0.05 1 915 . 96 GLN H H 8.868 0.05 1 916 . 96 GLN HA H 4.338 0.05 1 917 . 96 GLN HB2 H 1.71 0.05 2 918 . 96 GLN HB3 H 1.91 0.05 2 919 . 96 GLN HG2 H 2.532 0.05 2 920 . 96 GLN HG3 H 2.686 0.05 2 921 . 96 GLN HE21 H 7.719 0.05 1 922 . 96 GLN HE22 H 6.891 0.05 1 923 . 96 GLN CA C 56.786 0.05 1 924 . 96 GLN CB C 34.165 0.05 1 925 . 96 GLN CG C 36.085 0.05 1 926 . 96 GLN N N 123.997 0.05 1 927 . 96 GLN NE2 N 112.716 0.05 1 928 . 97 ASP H H 8.07 0.05 1 929 . 97 ASP HA H 5.615 0.05 1 930 . 97 ASP HB2 H 2.344 0.05 2 931 . 97 ASP HB3 H 2.509 0.05 2 932 . 97 ASP CA C 51.906 0.05 1 933 . 97 ASP CB C 44.879 0.05 1 934 . 97 ASP N N 121.312 0.05 1 935 . 98 ALA H H 8.28 0.05 1 936 . 98 ALA HA H 4.715 0.05 1 937 . 98 ALA HB H 1.337 0.05 1 938 . 98 ALA CA C 51.763 0.05 1 939 . 98 ALA CB C 22.536 0.05 1 940 . 98 ALA N N 120.79 0.05 1 941 . 99 THR H H 7.744 0.05 1 942 . 99 THR HA H 5.032 0.05 1 943 . 99 THR HB H 3.83 0.05 1 944 . 99 THR HG2 H 0.95 0.05 1 945 . 99 THR CA C 62.058 0.05 1 946 . 99 THR CB C 70.965 0.05 1 947 . 99 THR CG2 C 21.866 0.05 1 948 . 99 THR N N 112.915 0.05 1 949 . 100 ILE H H 9.84 0.05 1 950 . 100 ILE HA H 4.739 0.05 1 951 . 100 ILE HB H 1.838 0.05 1 952 . 100 ILE HG12 H 1.388 0.05 2 953 . 100 ILE HG13 H 1.571 0.05 2 954 . 100 ILE HG2 H 0.898 0.05 1 955 . 100 ILE HD1 H 1.233 0.05 1 956 . 100 ILE CA C 60.666 0.05 1 957 . 100 ILE CB C 43.184 0.05 1 958 . 100 ILE CG1 C 28.667 0.05 1 959 . 100 ILE CG2 C 17.815 0.05 1 960 . 100 ILE CD1 C 15.832 0.05 1 961 . 100 ILE N N 127.389 0.05 1 962 . 101 HIS H H 8.709 0.05 1 963 . 101 HIS HA H 5.195 0.05 1 964 . 101 HIS HB2 H 3.268 0.05 1 965 . 101 HIS HB3 H 3.268 0.05 1 966 . 101 HIS HD2 H 7.29 0.05 1 967 . 101 HIS HE1 H 8.58 0.05 1 968 . 101 HIS CA C 56.183 0.05 1 969 . 101 HIS CB C 30.678 0.05 1 970 . 101 HIS CD2 C 120.10 0.05 1 971 . 101 HIS CE1 C 136.2 0.05 1 972 . 101 HIS N N 126.03 0.05 1 973 . 102 LEU H H 8.207 0.05 1 974 . 102 LEU HA H 5.126 0.05 1 975 . 102 LEU HB2 H 1.144 0.05 2 976 . 102 LEU HB3 H 2.423 0.05 2 977 . 102 LEU HG H 1.286 0.05 1 978 . 102 LEU HD1 H 0.695 0.05 2 979 . 102 LEU HD2 H 0.684 0.05 2 980 . 102 LEU CA C 53.603 0.05 1 981 . 102 LEU CB C 44.693 0.05 1 982 . 102 LEU CG C 28.236 0.05 1 983 . 102 LEU CD1 C 24.064 0.05 2 984 . 102 LEU CD2 C 26.055 0.05 2 985 . 102 LEU N N 127.713 0.05 1 986 . 103 LYS H H 8.858 0.05 1 987 . 103 LYS HA H 4.516 0.05 1 988 . 103 LYS HB2 H 1.69 0.05 2 989 . 103 LYS HB3 H 1.884 0.05 2 990 . 103 LYS HG2 H 1.211 0.05 2 991 . 103 LYS HG3 H 1.312 0.05 2 992 . 103 LYS HD2 H 1.579 0.05 2 993 . 103 LYS HD3 H 1.618 0.05 2 994 . 103 LYS HE2 H 2.844 0.05 1 995 . 103 LYS HE3 H 2.844 0.05 1 996 . 103 LYS CA C 54.609 0.05 1 997 . 103 LYS CB C 33.836 0.05 1 998 . 103 LYS CG C 24.73 0.05 1 999 . 103 LYS CD C 28.675 0.05 1 1000 . 103 LYS CE C 42.225 0.05 1 1001 . 103 LYS N N 129.472 0.05 1 1002 . 104 VAL H H 9.003 0.05 1 1003 . 104 VAL HA H 4.686 0.05 1 1004 . 104 VAL HB H 1.823 0.05 1 1005 . 104 VAL HG1 H 0.629 0.05 2 1006 . 104 VAL HG2 H 0.54 0.05 2 1007 . 104 VAL CA C 60.437 0.05 1 1008 . 104 VAL CB C 34.311 0.05 1 1009 . 104 VAL CG1 C 20.359 0.05 2 1010 . 104 VAL CG2 C 21.823 0.05 2 1011 . 104 VAL N N 123.376 0.05 1 1012 . 105 PHE H H 8.905 0.05 1 1013 . 105 PHE HA H 4.722 0.05 1 1014 . 105 PHE HB2 H 3.243 0.05 1 1015 . 105 PHE HB3 H 2.988 0.05 1 1016 . 105 PHE HD1 H 7.294 0.05 1 1017 . 105 PHE HD2 H 7.294 0.05 1 1018 . 105 PHE CA C 56.938 0.05 1 1019 . 105 PHE CB C 40.424 0.05 1 1020 . 105 PHE N N 127.439 0.05 1 1021 . 106 ALA H H 8.74 0.05 1 1022 . 106 ALA HA H 4.418 0.05 1 1023 . 106 ALA HB H 1.412 0.05 1 1024 . 106 ALA CA C 52.376 0.05 1 1025 . 106 ALA CB C 20.25 0.05 1 1026 . 106 ALA N N 126.821 0.05 1 1027 . 107 LYS H H 7.881 0.05 1 1028 . 107 LYS HA H 4.06 0.05 1 1029 . 107 LYS HB2 H 1.815 0.05 2 1030 . 107 LYS HB3 H 1.747 0.05 2 1031 . 107 LYS HG2 H 1.407 0.05 1 1032 . 107 LYS HG3 H 1.407 0.05 1 1033 . 107 LYS HD2 H 1.69 0.05 1 1034 . 107 LYS HD3 H 1.69 0.05 1 1035 . 107 LYS HE2 H 3 0.05 1 1036 . 107 LYS HE3 H 3 0.05 1 1037 . 107 LYS CA C 57.817 0.05 1 1038 . 107 LYS CB C 33.642 0.05 1 1039 . 107 LYS CG C 24.637 0.05 1 1040 . 107 LYS CD C 29.419 0.05 1 1041 . 107 LYS CE C 42.45 0.05 1 1042 . 107 LYS N N 124.998 0.05 1 stop_ save_