data_5615 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H/13C/15N assignment of the C-terminal domain of the E. amylovora response regulator RcsB ; _BMRB_accession_number 5615 _BMRB_flat_file_name bmr5615.str _Entry_type original _Submission_date 2002-12-04 _Accession_date 2002-12-04 _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 Pristovsek Primoz . . 2 SenGupta Kaushik . . 3 Loehr Frank . . 4 SenGupta Soma . . 5 Bernhard Frank . . 6 Rueterjans Heinz . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 528 "13C chemical shifts" 375 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-12-11 original author . stop_ _Original_release_date 2003-12-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12740396 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pristovsek Primoz . . 2 SenGupta Kaushik . . 3 Loehr Frank . . 4 Schafer B. . . 5 Trebra M. W. . 6 Rueterjans Heinz . . 7 Bernhard Frank . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 278 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17752 _Page_last 17759 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Pristovsek P, Ruterjans H, Jerala R. Semiautomatic sequence-specific assignment of proteins based on the tertiary structure--the program st2nmr. J Comput Chem. 2002 Feb;23(3):335-40. ; _Citation_title 'Semiautomatic sequence-specific assignment of proteins based on the tertiary structure--the program st2nmr.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11908496 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pristovsek Primoz . . 2 Ruterjans Heinz . . 3 Jerala Roman . . stop_ _Journal_abbreviation . _Journal_name_full 'Journal of computational chemistry' _Journal_volume 23 _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 335 _Page_last 340 _Year 2002 _Details ; The sequence-specific assignment of resonances is still the most time-consuming procedure that is necessary as the first step in high-resolution NMR studies of proteins. In many cases a reliable three-dimensional (3D) structure of the protein is available, for example, from X-ray spectroscopy or homology modeling. Here we introduce the st2nmr program that uses the 3D structure and Nuclear Overhauser Effect spectroscopy (NOESY) peak list(s) to evaluate and optimize trial sequence-specific assignments of spin systems derived from correlation spectra to residues of the protein. A distance-dependent target function that scores trial assignments based on the presence of expected NOESY crosspeaks is optimized in a Monte Carlo fashion. The performance of the program st2nmr is tested on real NMR data of an alpha-helical (cytochrome c) and beta-sheet (lipocalin) protein using homology models and/or X-ray structures; it succeeded in completely reproducing the correct sequence-specific assignments in most cases using 2D and/or 15N/13C Nuclear Overhauser Effect (NOE) data. Additionally to amino acid residues the program can also handle ligands that are bound to the protein, such as heme, and can be used as a complementary tool to fully automated assignment procedures. ; save_ ################################## # Molecular system description # ################################## save_system_C-RcsB _Saveframe_category molecular_system _Mol_system_name C-RcsB _Abbreviation_common RcsB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RcsB monomer' $C-RcsB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'response regulator' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C-RcsB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'response regulator' _Abbreviation_common RcsB _Molecular_mass 10989 _Mol_thiol_state 'not present' _Details 'contains His-tag' ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; MRGSHHHHHHGSYTPESVAK LLEKISAGGYGDKRLSPKES EVLRLFAEGFLVTEIAKKLN RSIKTISSQKKSAMMKLGVD NDIALLNYLSSVSMTPVDK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 TYR 14 THR 15 PRO 16 GLU 17 SER 18 VAL 19 ALA 20 LYS 21 LEU 22 LEU 23 GLU 24 LYS 25 ILE 26 SER 27 ALA 28 GLY 29 GLY 30 TYR 31 GLY 32 ASP 33 LYS 34 ARG 35 LEU 36 SER 37 PRO 38 LYS 39 GLU 40 SER 41 GLU 42 VAL 43 LEU 44 ARG 45 LEU 46 PHE 47 ALA 48 GLU 49 GLY 50 PHE 51 LEU 52 VAL 53 THR 54 GLU 55 ILE 56 ALA 57 LYS 58 LYS 59 LEU 60 ASN 61 ARG 62 SER 63 ILE 64 LYS 65 THR 66 ILE 67 SER 68 SER 69 GLN 70 LYS 71 LYS 72 SER 73 ALA 74 MET 75 MET 76 LYS 77 LEU 78 GLY 79 VAL 80 ASP 81 ASN 82 ASP 83 ILE 84 ALA 85 LEU 86 LEU 87 ASN 88 TYR 89 LEU 90 SER 91 SER 92 VAL 93 SER 94 MET 95 THR 96 PRO 97 VAL 98 ASP 99 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1P4W "Solution Structure Of The Dna-Binding Domain Of The Erwinia Amylovora Rcsb Protein" 100.00 99 100.00 100.00 5.58e-64 DBJ BAN97122 "hypothetical protein E05_23560 [Plautia stali symbiont]" 87.88 630 97.70 97.70 6.21e-45 DBJ GAJ89526 "colanic acid biosynthesis two-component response regulator RcsB [Erwinia amylovora NBRC 12687]" 87.88 215 100.00 100.00 5.38e-52 EMBL CAA70978 "rcsB [Erwinia amylovora]" 87.88 215 100.00 100.00 5.38e-52 EMBL CAO96276 "Regulator of capsule synthesis B component [Erwinia tasmaniensis Et1/99]" 87.88 215 97.70 100.00 1.08e-50 EMBL CAX55067 "RcsB protein [Erwinia pyrifoliae Ep1/96]" 87.88 215 97.70 98.85 6.91e-51 EMBL CAY73751 "activator of exoploysaccharide synthesis [Erwinia pyrifoliae DSM 12163]" 87.88 215 97.70 98.85 6.91e-51 EMBL CBA21538 "activator of exoploysaccharide synthesis [Erwinia amylovora CFBP1430]" 87.88 215 100.00 100.00 5.38e-52 GB ADP13087 "transcriptional regulator RcsB [Erwinia sp. Ejp617]" 87.88 215 97.70 98.85 6.91e-51 GB ADU69998 "two component transcriptional regulator, LuxR family [Pantoea sp. At-9b]" 87.88 216 97.70 97.70 1.50e-49 GB AIX73097 "transcriptional regulator [Pantoea sp. PSNIH2]" 84.85 217 98.81 98.81 9.78e-49 GB EKV53357 "activator of exoploysaccharide synthesis [Erwinia amylovora ACW56400]" 87.88 215 100.00 100.00 5.38e-52 GB EOS96240 "transcriptional regulator RcsB [Erwinia tracheiphila PSU-1]" 87.88 216 97.70 97.70 5.54e-50 REF WP_004158545 "transcriptional regulator [Erwinia amylovora]" 87.88 215 100.00 100.00 5.38e-52 REF WP_004172989 "activator of exoploysaccharide synthesis [Erwinia amylovora]" 87.88 227 100.00 100.00 5.60e-52 REF WP_012440971 "MULTISPECIES: transcriptional regulator [Erwinia]" 87.88 215 97.70 100.00 1.08e-50 REF WP_012667617 "MULTISPECIES: transcriptional regulator [Erwinia]" 87.88 215 97.70 98.85 6.91e-51 REF WP_013509853 "MULTISPECIES: transcriptional regulator [Pantoea]" 87.88 216 97.70 97.70 1.50e-49 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $C-RcsB 'Erwinia amylovora' 552 Eubacteria . Erwinia Amylovora stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $C-RcsB 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $C-RcsB . mM 0.8 1.2 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 loop_ _Task processing visualisation stop_ _Details . save_ save_st2nmr _Saveframe_category software _Name st2nmr _Version 1.05 loop_ _Task 'semi-automated sequence-specific assignment' stop_ _Details 'In-house developed software for sequence-specific assignment.' _Citation_label $ref-1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.3 n/a temperature 289 0.1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RcsB monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ARG HA H 4.38 0.01 1 2 . 2 ARG HB2 H 1.85 0.01 1 3 . 2 ARG HB3 H 1.85 0.01 1 4 . 2 ARG HG2 H 1.66 0.01 1 5 . 2 ARG HG3 H 1.66 0.01 1 6 . 2 ARG HD2 H 3.19 0.01 1 7 . 2 ARG HD3 H 3.19 0.01 1 8 . 2 ARG C C 176.6 0.1 1 9 . 2 ARG CA C 56.6 0.1 1 10 . 2 ARG CB C 30.7 0.1 1 11 . 2 ARG CG C 27.1 0.1 1 12 . 2 ARG CD C 43.5 0.1 1 13 . 3 GLY H H 8.78 0.01 1 14 . 3 GLY HA2 H 4.00 0.01 2 15 . 3 GLY HA3 H 4.03 0.01 2 16 . 3 GLY C C 174.1 0.1 1 17 . 3 GLY CA C 45.2 0.1 1 18 . 3 GLY N N 111.4 0.1 1 19 . 4 SER H H 8.32 0.01 1 20 . 4 SER HA H 4.43 0.01 1 21 . 4 SER HB2 H 3.80 0.01 1 22 . 4 SER HB3 H 3.80 0.01 1 23 . 4 SER C C 174.5 0.1 1 24 . 4 SER CA C 58.5 0.1 1 25 . 4 SER CB C 63.9 0.1 1 26 . 4 SER N N 115.6 0.1 1 27 . 5 HIS H H 8.71 0.01 1 28 . 5 HIS HA H 4.60 0.01 1 29 . 5 HIS HB2 H 3.09 0.01 2 30 . 5 HIS HB3 H 3.00 0.01 2 31 . 5 HIS HD2 H 7.01 0.01 1 32 . 5 HIS HE1 H 8.10 0.01 1 33 . 5 HIS C C 174.6 0.1 1 34 . 5 HIS CA C 56.9 0.1 1 35 . 5 HIS CB C 30.0 0.1 1 36 . 5 HIS N N 120.9 0.1 1 37 . 10 HIS HA H 4.66 0.01 1 38 . 10 HIS HB2 H 3.23 0.01 2 39 . 10 HIS HB3 H 3.12 0.01 2 40 . 10 HIS C C 175.2 0.1 1 41 . 10 HIS CA C 56.0 0.1 1 42 . 10 HIS CB C 30.0 0.1 1 43 . 11 GLY H H 8.58 0.01 1 44 . 11 GLY HA2 H 4.00 0.01 1 45 . 11 GLY HA3 H 3.96 0.01 1 46 . 11 GLY C C 173.9 0.1 1 47 . 11 GLY CA C 45.3 0.1 1 48 . 11 GLY N N 110.6 0.1 1 49 . 12 SER H H 8.35 0.01 1 50 . 12 SER HA H 4.47 0.01 1 51 . 12 SER HB2 H 3.78 0.01 1 52 . 12 SER HB3 H 3.78 0.01 1 53 . 12 SER C C 174.0 0.1 1 54 . 12 SER CA C 58.4 0.1 1 55 . 12 SER CB C 63.9 0.1 1 56 . 12 SER N N 115.9 0.1 1 57 . 13 TYR H H 8.27 0.01 1 58 . 13 TYR HA H 4.69 0.01 1 59 . 13 TYR HB2 H 2.97 0.01 2 60 . 13 TYR HB3 H 2.88 0.01 2 61 . 13 TYR HD1 H 6.99 0.01 1 62 . 13 TYR HD2 H 6.99 0.01 1 63 . 13 TYR HE1 H 6.70 0.01 1 64 . 13 TYR HE2 H 6.70 0.01 1 65 . 13 TYR C C 175.4 0.1 1 66 . 13 TYR CA C 57.7 0.1 1 67 . 13 TYR CB C 39.2 0.1 1 68 . 13 TYR N N 122.2 0.1 1 69 . 15 PRO HA H 4.33 0.01 1 70 . 15 PRO HB2 H 2.40 0.01 2 71 . 15 PRO HB3 H 1.95 0.01 2 72 . 15 PRO HG2 H 2.13 0.01 2 73 . 15 PRO HG3 H 2.04 0.01 2 74 . 15 PRO HD2 H 3.76 0.01 1 75 . 15 PRO HD3 H 3.76 0.01 1 76 . 15 PRO C C 178.3 0.1 1 77 . 15 PRO CA C 64.4 0.1 1 78 . 15 PRO CB C 32.1 0.1 1 79 . 15 PRO CG C 27.9 0.1 1 80 . 15 PRO CD C 50.9 0.1 1 81 . 16 GLU H H 8.78 0.01 1 82 . 16 GLU HA H 4.17 0.01 1 83 . 16 GLU HB2 H 2.04 0.01 1 84 . 16 GLU HB3 H 2.04 0.01 1 85 . 16 GLU HG2 H 2.35 0.01 1 86 . 16 GLU HG3 H 2.35 0.01 1 87 . 16 GLU C C 177.9 0.1 1 88 . 16 GLU CA C 58.8 0.1 1 89 . 16 GLU CB C 29.5 0.1 1 90 . 16 GLU CG C 36.7 0.1 1 91 . 16 GLU N N 119.4 0.1 1 92 . 17 SER H H 8.29 0.01 1 93 . 17 SER HA H 4.31 0.01 1 94 . 17 SER C C 176.6 0.1 1 95 . 17 SER CA C 60.3 0.1 1 96 . 17 SER CB C 63.1 0.1 1 97 . 17 SER N N 116.8 0.1 1 98 . 18 VAL H H 8.12 0.01 1 99 . 18 VAL HA H 3.80 0.01 1 100 . 18 VAL HB H 2.13 0.01 1 101 . 18 VAL HG1 H 0.95 0.01 1 102 . 18 VAL HG2 H 0.98 0.01 1 103 . 18 VAL C C 176.9 0.1 1 104 . 18 VAL CA C 65.4 0.1 1 105 . 18 VAL CB C 31.8 0.1 1 106 . 18 VAL CG1 C 21.5 0.1 1 107 . 18 VAL CG2 C 22.7 0.1 1 108 . 18 VAL N N 123.6 0.1 1 109 . 19 ALA H H 8.17 0.01 1 110 . 19 ALA HA H 4.08 0.01 1 111 . 19 ALA HB H 1.47 0.01 1 112 . 19 ALA C C 180.2 0.1 1 113 . 19 ALA CA C 55.0 0.1 1 114 . 19 ALA CB C 18.2 0.1 1 115 . 19 ALA N N 123.2 0.1 1 116 . 20 LYS H H 7.94 0.01 1 117 . 20 LYS HA H 4.14 0.01 1 118 . 20 LYS HB2 H 1.90 0.01 2 119 . 20 LYS HB3 H 1.71 0.01 2 120 . 20 LYS HG2 H 1.59 0.01 1 121 . 20 LYS HG3 H 1.59 0.01 1 122 . 20 LYS HD2 H 1.51 0.01 1 123 . 20 LYS HD3 H 1.51 0.01 1 124 . 20 LYS HE2 H 2.99 0.01 1 125 . 20 LYS HE3 H 2.99 0.01 1 126 . 20 LYS C C 178.7 0.1 1 127 . 20 LYS CA C 58.3 0.1 1 128 . 20 LYS CB C 32.2 0.1 1 129 . 20 LYS CG C 25.0 0.1 1 130 . 20 LYS CD C 28.8 0.1 1 131 . 20 LYS CE C 42.1 0.1 1 132 . 20 LYS N N 117.9 0.1 1 133 . 21 LEU H H 7.92 0.01 1 134 . 21 LEU HA H 4.21 0.01 1 135 . 21 LEU HB2 H 1.78 0.01 2 136 . 21 LEU HB3 H 1.66 0.01 2 137 . 21 LEU HG H 1.42 0.01 1 138 . 21 LEU HD1 H 0.92 0.01 1 139 . 21 LEU HD2 H 0.92 0.01 1 140 . 21 LEU C C 178.6 0.1 1 141 . 21 LEU CA C 57.6 0.1 1 142 . 21 LEU CB C 41.8 0.1 1 143 . 21 LEU CG C 27.0 0.1 1 144 . 21 LEU CD1 C 24.5 0.1 1 145 . 21 LEU CD2 C 24.5 0.1 1 146 . 21 LEU N N 122.3 0.1 1 147 . 22 LEU H H 8.35 0.01 1 148 . 22 LEU HA H 4.09 0.01 1 149 . 22 LEU HB2 H 1.83 0.01 1 150 . 22 LEU HB3 H 1.56 0.01 1 151 . 22 LEU HG H 1.56 0.01 1 152 . 22 LEU HD1 H 0.87 0.01 1 153 . 22 LEU HD2 H 0.90 0.01 1 154 . 22 LEU C C 179.3 0.1 1 155 . 22 LEU CA C 57.1 0.1 1 156 . 22 LEU CB C 41.2 0.1 1 157 . 22 LEU CG C 27.2 0.1 1 158 . 22 LEU CD1 C 24.9 0.1 1 159 . 22 LEU CD2 C 23.0 0.1 1 160 . 22 LEU N N 119.2 0.1 1 161 . 23 GLU H H 8.02 0.01 1 162 . 23 GLU HA H 4.11 0.01 1 163 . 23 GLU HB2 H 2.26 0.01 1 164 . 23 GLU HB3 H 2.14 0.01 1 165 . 23 GLU HG2 H 2.42 0.01 1 166 . 23 GLU HG3 H 2.42 0.01 1 167 . 23 GLU C C 178.2 0.1 1 168 . 23 GLU CA C 58.8 0.1 1 169 . 23 GLU CB C 29.9 0.1 1 170 . 23 GLU CG C 36.3 0.1 1 171 . 23 GLU N N 120.5 0.1 1 172 . 24 LYS H H 7.93 0.01 1 173 . 24 LYS HA H 4.20 0.01 1 174 . 24 LYS C C 178.8 0.1 1 175 . 24 LYS CA C 58.6 0.1 1 176 . 24 LYS CB C 32.6 0.1 1 177 . 24 LYS N N 120.5 0.1 1 178 . 25 ILE HA H 4.00 0.01 1 179 . 25 ILE HB H 1.97 0.01 1 180 . 25 ILE HG12 H 1.66 0.01 2 181 . 25 ILE HG13 H 1.55 0.01 2 182 . 25 ILE HG2 H 0.94 0.01 1 183 . 25 ILE HD1 H 0.85 0.01 1 184 . 25 ILE C C 177.7 0.1 1 185 . 25 ILE CA C 63.2 0.1 1 186 . 25 ILE CB C 38.3 0.1 1 187 . 25 ILE CG1 C 27.9 0.1 1 188 . 25 ILE CG2 C 17.5 0.1 1 189 . 25 ILE CD1 C 14.0 0.1 1 190 . 26 SER H H 8.19 0.01 1 191 . 26 SER HA H 4.42 0.01 1 192 . 26 SER HB2 H 3.95 0.01 1 193 . 26 SER HB3 H 3.95 0.01 1 194 . 26 SER C C 174.9 0.1 1 195 . 26 SER CA C 59.9 0.1 1 196 . 26 SER CB C 63.7 0.1 1 197 . 26 SER N N 117.1 0.1 1 198 . 27 ALA H H 7.99 0.01 1 199 . 27 ALA HA H 4.37 0.01 1 200 . 27 ALA HB H 1.51 0.01 1 201 . 27 ALA C C 178.4 0.1 1 202 . 27 ALA CA C 53.0 0.1 1 203 . 27 ALA CB C 19.1 0.1 1 204 . 27 ALA N N 124.3 0.1 1 205 . 28 GLY H H 8.17 0.01 1 206 . 28 GLY HA2 H 4.00 0.01 1 207 . 28 GLY HA3 H 4.04 0.01 1 208 . 28 GLY C C 174.8 0.1 1 209 . 28 GLY CA C 45.7 0.1 1 210 . 28 GLY N N 106.4 0.1 1 211 . 29 GLY H H 8.19 0.01 1 212 . 29 GLY HA2 H 3.94 0.01 2 213 . 29 GLY HA3 H 3.95 0.01 2 214 . 29 GLY C C 173.7 0.1 1 215 . 29 GLY CA C 45.3 0.1 1 216 . 29 GLY N N 108.2 0.1 1 217 . 30 TYR H H 8.19 0.01 1 218 . 30 TYR HA H 4.58 0.01 1 219 . 30 TYR HB2 H 3.06 0.01 1 220 . 30 TYR HB3 H 2.99 0.01 1 221 . 30 TYR HD1 H 7.10 0.01 1 222 . 30 TYR HD2 H 7.10 0.01 1 223 . 30 TYR HE1 H 6.82 0.01 1 224 . 30 TYR HE2 H 6.82 0.01 1 225 . 30 TYR C C 176.3 0.1 1 226 . 30 TYR CA C 57.9 0.1 1 227 . 30 TYR CB C 39.2 0.1 1 228 . 30 TYR N N 119.3 0.1 1 229 . 31 GLY H H 8.43 0.01 1 230 . 31 GLY HA2 H 3.95 0.01 2 231 . 31 GLY HA3 H 3.84 0.01 2 232 . 31 GLY C C 174.4 0.1 1 233 . 31 GLY CA C 45.7 0.1 1 234 . 31 GLY N N 110.9 0.1 1 235 . 32 ASP H H 8.41 0.01 1 236 . 32 ASP HA H 4.49 0.01 1 237 . 32 ASP HB2 H 2.75 0.01 1 238 . 32 ASP HB3 H 2.75 0.01 1 239 . 32 ASP C C 176.7 0.1 1 240 . 32 ASP CA C 55.0 0.1 1 241 . 32 ASP CB C 41.1 0.1 1 242 . 32 ASP N N 121.6 0.1 1 243 . 33 LYS H H 8.31 0.01 1 244 . 33 LYS HA H 4.33 0.01 1 245 . 33 LYS HB2 H 1.98 0.01 2 246 . 33 LYS HB3 H 1.83 0.01 2 247 . 33 LYS HG2 H 1.53 0.01 1 248 . 33 LYS HG3 H 1.53 0.01 1 249 . 33 LYS HD2 H 1.74 0.01 1 250 . 33 LYS HD3 H 1.74 0.01 1 251 . 33 LYS HE2 H 3.05 0.01 1 252 . 33 LYS HE3 H 3.05 0.01 1 253 . 33 LYS C C 176.0 0.1 1 254 . 33 LYS CA C 56.1 0.1 1 255 . 33 LYS CB C 32.5 0.1 1 256 . 33 LYS CG C 24.9 0.1 1 257 . 33 LYS CD C 28.9 0.1 1 258 . 33 LYS CE C 42.4 0.1 1 259 . 33 LYS N N 120.8 0.1 1 260 . 34 ARG H H 8.07 0.01 1 261 . 34 ARG HA H 4.26 0.01 1 262 . 34 ARG HB2 H 1.77 0.01 2 263 . 34 ARG HB3 H 1.64 0.01 2 264 . 34 ARG HG2 H 1.64 0.01 1 265 . 34 ARG HG3 H 1.64 0.01 1 266 . 34 ARG HD2 H 3.19 0.01 2 267 . 34 ARG HD3 H 3.13 0.01 2 268 . 34 ARG HE H 7.41 0.01 1 269 . 34 ARG C C 177.1 0.1 1 270 . 34 ARG CA C 56.4 0.1 1 271 . 34 ARG CB C 30.8 0.1 1 272 . 34 ARG N N 119.2 0.1 1 273 . 34 ARG NE N 105.9 0.1 1 274 . 35 LEU H H 8.45 0.01 1 275 . 35 LEU HA H 4.38 0.01 1 276 . 35 LEU HB2 H 1.54 0.01 1 277 . 35 LEU HB3 H 1.54 0.01 1 278 . 35 LEU HD1 H 0.91 0.01 2 279 . 35 LEU HD2 H 0.84 0.01 2 280 . 35 LEU C C 177.4 0.1 1 281 . 35 LEU CA C 54.9 0.1 1 282 . 35 LEU CB C 42.7 0.1 1 283 . 35 LEU CG C 27.6 0.1 1 284 . 35 LEU CD1 C 26.5 0.1 1 285 . 35 LEU CD2 C 24.5 0.1 1 286 . 35 LEU N N 123.7 0.1 1 287 . 36 SER H H 9.48 0.01 1 288 . 36 SER HA H 4.91 0.01 1 289 . 36 SER C C 173.8 0.1 1 290 . 36 SER CA C 56.2 0.1 1 291 . 36 SER CB C 63.6 0.1 1 292 . 36 SER N N 122.1 0.1 1 293 . 37 PRO HA H 4.38 0.01 1 294 . 37 PRO HB2 H 2.45 0.01 2 295 . 37 PRO HB3 H 1.97 0.01 2 296 . 37 PRO HG2 H 2.23 0.01 2 297 . 37 PRO HG3 H 2.07 0.01 2 298 . 37 PRO HD2 H 3.99 0.01 1 299 . 37 PRO HD3 H 3.99 0.01 1 300 . 37 PRO C C 179.7 0.1 1 301 . 37 PRO CA C 65.9 0.1 1 302 . 37 PRO CB C 32.0 0.1 1 303 . 37 PRO CG C 28.1 0.1 1 304 . 37 PRO CD C 50.2 0.1 1 305 . 38 LYS H H 7.84 0.01 1 306 . 38 LYS HA H 4.31 0.01 1 307 . 38 LYS HB2 H 1.63 0.01 1 308 . 38 LYS HB3 H 1.63 0.01 1 309 . 38 LYS HG2 H 1.44 0.01 1 310 . 38 LYS HG3 H 1.44 0.01 1 311 . 38 LYS HD2 H 1.44 0.01 1 312 . 38 LYS HD3 H 1.44 0.01 1 313 . 38 LYS HE2 H 2.97 0.01 1 314 . 38 LYS HE3 H 2.97 0.01 1 315 . 38 LYS C C 179.5 0.1 1 316 . 38 LYS CA C 59.1 0.1 1 317 . 38 LYS CB C 32.8 0.1 1 318 . 38 LYS CG C 26.1 0.1 1 319 . 38 LYS CD C 29.1 0.1 1 320 . 38 LYS CE C 42.3 0.1 1 321 . 38 LYS N N 115.6 0.1 1 322 . 39 GLU H H 7.63 0.01 1 323 . 39 GLU HA H 3.62 0.01 1 324 . 39 GLU HB2 H 2.26 0.01 1 325 . 39 GLU HB3 H 1.75 0.01 1 326 . 39 GLU HG2 H 2.68 0.01 2 327 . 39 GLU HG3 H 2.54 0.01 2 328 . 39 GLU C C 178.7 0.1 1 329 . 39 GLU CA C 59.3 0.1 1 330 . 39 GLU CB C 30.6 0.1 1 331 . 39 GLU CG C 36.4 0.1 1 332 . 39 GLU N N 118.8 0.1 1 333 . 40 SER H H 8.66 0.01 1 334 . 40 SER HA H 3.97 0.01 1 335 . 40 SER HB2 H 3.99 0.01 1 336 . 40 SER HB3 H 3.99 0.01 1 337 . 40 SER C C 176.1 0.1 1 338 . 40 SER CA C 59.3 0.1 1 339 . 40 SER CB C 62.6 0.1 1 340 . 40 SER N N 113.8 0.1 1 341 . 41 GLU H H 7.76 0.01 1 342 . 41 GLU HA H 4.10 0.01 1 343 . 41 GLU HB2 H 2.17 0.01 2 344 . 41 GLU HB3 H 2.08 0.01 2 345 . 41 GLU HG2 H 2.32 0.01 1 346 . 41 GLU HG3 H 2.32 0.01 1 347 . 41 GLU C C 178.2 0.1 1 348 . 41 GLU CA C 59.1 0.1 1 349 . 41 GLU CB C 30.2 0.1 1 350 . 41 GLU CG C 36.2 0.1 1 351 . 41 GLU N N 120.3 0.1 1 352 . 42 VAL H H 7.28 0.01 1 353 . 42 VAL HA H 3.48 0.01 1 354 . 42 VAL HB H 2.16 0.01 1 355 . 42 VAL HG1 H 0.97 0.01 1 356 . 42 VAL HG2 H 1.16 0.01 1 357 . 42 VAL C C 177.5 0.1 1 358 . 42 VAL CA C 67.4 0.1 1 359 . 42 VAL CB C 32.1 0.1 1 360 . 42 VAL CG1 C 21.2 0.1 1 361 . 42 VAL CG2 C 24.5 0.1 1 362 . 42 VAL N N 118.2 0.1 1 363 . 43 LEU H H 8.14 0.01 1 364 . 43 LEU HA H 4.06 0.01 1 365 . 43 LEU HB2 H 1.90 0.01 2 366 . 43 LEU HB3 H 1.59 0.01 2 367 . 43 LEU HG H 1.59 0.01 1 368 . 43 LEU HD1 H 0.89 0.01 2 369 . 43 LEU HD2 H 0.80 0.01 2 370 . 43 LEU C C 178.4 0.1 1 371 . 43 LEU CA C 58.1 0.1 1 372 . 43 LEU CB C 41.2 0.1 1 373 . 43 LEU CG C 27.2 0.1 1 374 . 43 LEU CD1 C 26.1 0.1 1 375 . 43 LEU CD2 C 24.0 0.1 1 376 . 43 LEU N N 117.7 0.1 1 377 . 44 ARG H H 8.53 0.01 1 378 . 44 ARG HA H 3.88 0.01 1 379 . 44 ARG HB2 H 1.94 0.01 2 380 . 44 ARG HB3 H 1.90 0.01 2 381 . 44 ARG HG2 H 1.66 0.01 2 382 . 44 ARG HG3 H 1.56 0.01 2 383 . 44 ARG HD2 H 3.25 0.01 2 384 . 44 ARG HD3 H 3.14 0.01 2 385 . 44 ARG HE H 7.58 0.01 1 386 . 44 ARG C C 178.6 0.1 1 387 . 44 ARG CA C 59.9 0.1 1 388 . 44 ARG CB C 29.8 0.1 1 389 . 44 ARG CG C 27.9 0.1 1 390 . 44 ARG CD C 43.4 0.1 1 391 . 44 ARG N N 119.2 0.1 1 392 . 44 ARG NE N 126.2 0.1 1 393 . 45 LEU H H 7.53 0.01 1 394 . 45 LEU HA H 4.30 0.01 1 395 . 45 LEU HB2 H 1.90 0.01 2 396 . 45 LEU HB3 H 1.23 0.01 2 397 . 45 LEU HD1 H 0.78 0.01 1 398 . 45 LEU HD2 H 0.66 0.01 1 399 . 45 LEU C C 179.5 0.1 1 400 . 45 LEU CA C 57.7 0.1 1 401 . 45 LEU CB C 42.5 0.1 1 402 . 45 LEU CD1 C 27.2 0.1 1 403 . 45 LEU CD2 C 23.2 0.1 1 404 . 45 LEU N N 117.2 0.1 1 405 . 46 PHE H H 8.70 0.01 1 406 . 46 PHE HA H 4.61 0.01 1 407 . 46 PHE HB2 H 3.16 0.01 2 408 . 46 PHE HB3 H 3.09 0.01 2 409 . 46 PHE HD1 H 7.18 0.01 1 410 . 46 PHE HD2 H 7.18 0.01 1 411 . 46 PHE HE1 H 7.24 0.01 1 412 . 46 PHE HE2 H 7.24 0.01 1 413 . 46 PHE C C 179.9 0.1 1 414 . 46 PHE CA C 61.7 0.1 1 415 . 46 PHE CB C 39.4 0.1 1 416 . 46 PHE N N 122.1 0.1 1 417 . 47 ALA H H 8.88 0.01 1 418 . 47 ALA HA H 3.95 0.01 1 419 . 47 ALA HB H 1.59 0.01 1 420 . 47 ALA C C 178.8 0.1 1 421 . 47 ALA CA C 54.6 0.1 1 422 . 47 ALA CB C 18.3 0.1 1 423 . 47 ALA N N 123.1 0.1 1 424 . 48 GLU H H 7.67 0.01 1 425 . 48 GLU HA H 4.17 0.01 1 426 . 48 GLU HB2 H 2.32 0.01 2 427 . 48 GLU HB3 H 2.31 0.01 2 428 . 48 GLU HG2 H 2.68 0.01 1 429 . 48 GLU HG3 H 2.68 0.01 1 430 . 48 GLU C C 176.4 0.1 1 431 . 48 GLU CA C 56.9 0.1 1 432 . 48 GLU CB C 30.3 0.1 1 433 . 48 GLU CG C 37.1 0.1 1 434 . 48 GLU N N 116.3 0.1 1 435 . 49 GLY H H 7.70 0.01 1 436 . 49 GLY HA2 H 4.05 0.01 1 437 . 49 GLY HA3 H 3.51 0.01 1 438 . 49 GLY C C 174.7 0.1 1 439 . 49 GLY CA C 45.1 0.1 1 440 . 49 GLY N N 105.7 0.1 1 441 . 50 PHE H H 7.51 0.01 1 442 . 50 PHE HA H 4.53 0.01 1 443 . 50 PHE HB2 H 2.93 0.01 2 444 . 50 PHE HB3 H 2.55 0.01 2 445 . 50 PHE HD1 H 7.45 0.01 1 446 . 50 PHE HD2 H 7.45 0.01 1 447 . 50 PHE HE1 H 7.41 0.01 1 448 . 50 PHE HE2 H 7.41 0.01 1 449 . 50 PHE HZ H 7.28 0.01 1 450 . 50 PHE C C 175.6 0.1 1 451 . 50 PHE CA C 58.7 0.1 1 452 . 50 PHE CB C 39.6 0.1 1 453 . 50 PHE N N 118.9 0.1 1 454 . 51 LEU H H 9.09 0.01 1 455 . 51 LEU HA H 4.63 0.01 1 456 . 51 LEU HB2 H 1.92 0.01 2 457 . 51 LEU HB3 H 1.70 0.01 2 458 . 51 LEU HG H 1.70 0.01 1 459 . 51 LEU HD1 H 0.98 0.01 2 460 . 51 LEU HD2 H 0.96 0.01 2 461 . 51 LEU C C 180.0 0.1 1 462 . 51 LEU CA C 53.8 0.1 1 463 . 51 LEU CB C 43.3 0.1 1 464 . 51 LEU CG C 27.5 0.1 1 465 . 51 LEU CD1 C 25.5 0.1 1 466 . 51 LEU CD2 C 22.5 0.1 1 467 . 51 LEU N N 121.2 0.1 1 468 . 52 VAL H H 9.25 0.01 1 469 . 52 VAL HA H 3.67 0.01 1 470 . 52 VAL HB H 2.30 0.01 1 471 . 52 VAL HG1 H 1.17 0.01 1 472 . 52 VAL HG2 H 1.05 0.01 1 473 . 52 VAL C C 177.0 0.1 1 474 . 52 VAL CA C 68.1 0.1 1 475 . 52 VAL CB C 31.4 0.1 1 476 . 52 VAL CG1 C 22.7 0.1 1 477 . 52 VAL CG2 C 21.0 0.1 1 478 . 52 VAL N N 121.5 0.1 1 479 . 53 THR H H 7.84 0.01 1 480 . 53 THR HA H 3.92 0.01 1 481 . 53 THR HB H 4.23 0.01 1 482 . 53 THR HG2 H 1.38 0.01 1 483 . 53 THR C C 177.2 0.1 1 484 . 53 THR CA C 65.0 0.1 1 485 . 53 THR CB C 68.0 0.1 1 486 . 53 THR CG2 C 23.0 0.1 1 487 . 53 THR N N 108.9 0.1 1 488 . 54 GLU H H 6.99 0.01 1 489 . 54 GLU HA H 4.23 0.01 1 490 . 54 GLU HB2 H 2.18 0.01 1 491 . 54 GLU HB3 H 2.18 0.01 1 492 . 54 GLU HG2 H 2.68 0.01 2 493 . 54 GLU HG3 H 2.42 0.01 2 494 . 54 GLU C C 179.1 0.1 1 495 . 54 GLU CA C 58.4 0.1 1 496 . 54 GLU CB C 30.4 0.1 1 497 . 54 GLU CG C 37.4 0.1 1 498 . 54 GLU N N 121.8 0.1 1 499 . 55 ILE H H 8.70 0.01 1 500 . 55 ILE HA H 3.26 0.01 1 501 . 55 ILE HB H 1.92 0.01 1 502 . 55 ILE HG12 H 0.92 0.01 1 503 . 55 ILE HG13 H 0.92 0.01 1 504 . 55 ILE HG2 H 0.92 0.01 1 505 . 55 ILE HD1 H 0.71 0.01 1 506 . 55 ILE C C 176.8 0.1 1 507 . 55 ILE CA C 66.5 0.1 1 508 . 55 ILE CB C 38.1 0.1 1 509 . 55 ILE CG1 C 29.5 0.1 1 510 . 55 ILE CG2 C 18.7 0.1 1 511 . 55 ILE CD1 C 12.8 0.1 1 512 . 55 ILE N N 122.1 0.1 1 513 . 56 ALA H H 8.23 0.01 1 514 . 56 ALA HA H 3.78 0.01 1 515 . 56 ALA HB H 1.52 0.01 1 516 . 56 ALA C C 179.3 0.1 1 517 . 56 ALA CA C 56.3 0.1 1 518 . 56 ALA CB C 18.3 0.1 1 519 . 56 ALA N N 121.2 0.1 1 520 . 57 LYS H H 7.04 0.01 1 521 . 57 LYS HA H 4.16 0.01 1 522 . 57 LYS HB2 H 1.95 0.01 1 523 . 57 LYS HB3 H 1.75 0.01 1 524 . 57 LYS HG2 H 1.61 0.01 1 525 . 57 LYS HG3 H 1.61 0.01 1 526 . 57 LYS HD2 H 1.56 0.01 1 527 . 57 LYS HD3 H 1.56 0.01 1 528 . 57 LYS HE2 H 3.02 0.01 1 529 . 57 LYS HE3 H 3.02 0.01 1 530 . 57 LYS C C 179.5 0.1 1 531 . 57 LYS CA C 58.8 0.1 1 532 . 57 LYS CB C 32.4 0.1 1 533 . 57 LYS CG C 24.9 0.1 1 534 . 57 LYS CD C 29.2 0.1 1 535 . 57 LYS CE C 42.4 0.1 1 536 . 57 LYS N N 115.7 0.1 1 537 . 58 LYS H H 8.18 0.01 1 538 . 58 LYS HA H 3.94 0.01 1 539 . 58 LYS HB2 H 1.71 0.01 1 540 . 58 LYS HB3 H 1.71 0.01 1 541 . 58 LYS HG2 H 1.42 0.01 1 542 . 58 LYS HG3 H 1.42 0.01 1 543 . 58 LYS HD2 H 1.33 0.01 2 544 . 58 LYS HD3 H 1.20 0.01 2 545 . 58 LYS HE2 H 2.32 0.01 2 546 . 58 LYS HE3 H 2.23 0.01 2 547 . 58 LYS C C 178.4 0.1 1 548 . 58 LYS CA C 59.2 0.1 1 549 . 58 LYS CB C 32.9 0.1 1 550 . 58 LYS CG C 24.7 0.1 1 551 . 58 LYS CD C 29.5 0.1 1 552 . 58 LYS CE C 40.9 0.1 1 553 . 58 LYS N N 119.4 0.1 1 554 . 59 LEU H H 8.18 0.01 1 555 . 59 LEU HA H 4.36 0.01 1 556 . 59 LEU HB2 H 1.45 0.01 1 557 . 59 LEU HB3 H 1.45 0.01 1 558 . 59 LEU HG H 1.59 0.01 1 559 . 59 LEU HD1 H 0.67 0.01 2 560 . 59 LEU HD2 H 0.69 0.01 2 561 . 59 LEU C C 176.1 0.1 1 562 . 59 LEU CA C 53.9 0.1 1 563 . 59 LEU CB C 41.2 0.1 1 564 . 59 LEU CD1 C 26.6 0.1 1 565 . 59 LEU CD2 C 21.7 0.1 1 566 . 59 LEU N N 113.8 0.1 1 567 . 60 ASN H H 7.88 0.01 1 568 . 60 ASN HA H 4.38 0.01 1 569 . 60 ASN HB2 H 3.23 0.01 1 570 . 60 ASN HB3 H 2.64 0.01 1 571 . 60 ASN HD21 H 7.60 0.01 2 572 . 60 ASN HD22 H 6.85 0.01 2 573 . 60 ASN C C 174.4 0.1 1 574 . 60 ASN CA C 54.0 0.1 1 575 . 60 ASN CB C 37.1 0.1 1 576 . 60 ASN N N 118.6 0.1 1 577 . 60 ASN ND2 N 112.1 0.1 1 578 . 61 ARG H H 8.23 0.01 1 579 . 61 ARG HA H 4.77 0.01 1 580 . 61 ARG HB2 H 1.80 0.01 2 581 . 61 ARG HB3 H 1.42 0.01 2 582 . 61 ARG HG2 H 1.66 0.01 2 583 . 61 ARG HG3 H 1.42 0.01 2 584 . 61 ARG HD2 H 3.37 0.01 2 585 . 61 ARG HD3 H 3.02 0.01 2 586 . 61 ARG C C 174.6 0.1 1 587 . 61 ARG CA C 54.1 0.1 1 588 . 61 ARG CB C 35.0 0.1 1 589 . 61 ARG CG C 27.9 0.1 1 590 . 61 ARG CD C 44.4 0.1 1 591 . 61 ARG N N 116.0 0.1 1 592 . 62 SER H H 8.81 0.01 1 593 . 62 SER HA H 4.43 0.01 1 594 . 62 SER HB2 H 4.07 0.01 1 595 . 62 SER HB3 H 4.07 0.01 1 596 . 62 SER C C 175.2 0.1 1 597 . 62 SER CA C 57.5 0.1 1 598 . 62 SER CB C 64.9 0.1 1 599 . 62 SER N N 115.8 0.1 1 600 . 63 ILE H H 8.88 0.01 1 601 . 63 ILE HA H 3.53 0.01 1 602 . 63 ILE HB H 1.82 0.01 1 603 . 63 ILE HG12 H 1.71 0.01 2 604 . 63 ILE HG13 H 1.04 0.01 2 605 . 63 ILE HG2 H 1.01 0.01 1 606 . 63 ILE HD1 H 0.92 0.01 1 607 . 63 ILE C C 178.4 0.1 1 608 . 63 ILE CA C 65.7 0.1 1 609 . 63 ILE CB C 38.1 0.1 1 610 . 63 ILE CG1 C 29.7 0.1 1 611 . 63 ILE CG2 C 17.3 0.1 1 612 . 63 ILE CD1 C 14.0 0.1 1 613 . 63 ILE N N 122.0 0.1 1 614 . 64 LYS H H 8.40 0.01 1 615 . 64 LYS HA H 4.06 0.01 1 616 . 64 LYS HB2 H 1.87 0.01 2 617 . 64 LYS HB3 H 1.82 0.01 2 618 . 64 LYS HG2 H 1.71 0.01 2 619 . 64 LYS HG3 H 1.49 0.01 2 620 . 64 LYS HD2 H 1.42 0.01 1 621 . 64 LYS HD3 H 1.42 0.01 1 622 . 64 LYS HE2 H 2.99 0.01 1 623 . 64 LYS HE3 H 2.99 0.01 1 624 . 64 LYS C C 179.3 0.1 1 625 . 64 LYS CA C 59.7 0.1 1 626 . 64 LYS CB C 32.3 0.1 1 627 . 64 LYS CG C 25.2 0.1 1 628 . 64 LYS CD C 29.5 0.1 1 629 . 64 LYS CE C 42.1 0.1 1 630 . 64 LYS N N 121.2 0.1 1 631 . 65 THR H H 8.18 0.01 1 632 . 65 THR HA H 3.94 0.01 1 633 . 65 THR HB H 3.80 0.01 1 634 . 65 THR HG2 H 1.20 0.01 1 635 . 65 THR C C 176.1 0.1 1 636 . 65 THR CA C 66.9 0.1 1 637 . 65 THR CB C 67.6 0.1 1 638 . 65 THR CG2 C 22.2 0.1 1 639 . 65 THR N N 119.4 0.1 1 640 . 66 ILE H H 8.43 0.01 1 641 . 66 ILE HA H 3.86 0.01 1 642 . 66 ILE HB H 2.21 0.01 1 643 . 66 ILE HG12 H 1.82 0.01 1 644 . 66 ILE HG13 H 1.82 0.01 1 645 . 66 ILE HG2 H 1.00 0.01 1 646 . 66 ILE HD1 H 0.73 0.01 1 647 . 66 ILE C C 178.4 0.1 1 648 . 66 ILE CA C 62.0 0.1 1 649 . 66 ILE CB C 35.0 0.1 1 650 . 66 ILE CG1 C 26.5 0.1 1 651 . 66 ILE CG2 C 19.2 0.1 1 652 . 66 ILE CD1 C 11.8 0.1 1 653 . 66 ILE N N 120.6 0.1 1 654 . 67 SER H H 8.92 0.01 1 655 . 67 SER HA H 4.08 0.01 1 656 . 67 SER HB2 H 3.97 0.01 1 657 . 67 SER HB3 H 3.97 0.01 1 658 . 67 SER C C 178.4 0.1 1 659 . 67 SER CA C 62.6 0.1 1 660 . 67 SER CB C 62.6 0.1 1 661 . 67 SER N N 115.2 0.1 1 662 . 68 SER H H 8.17 0.01 1 663 . 68 SER HA H 4.27 0.01 1 664 . 68 SER HB2 H 4.14 0.01 1 665 . 68 SER HB3 H 4.14 0.01 1 666 . 68 SER C C 177.1 0.1 1 667 . 68 SER CA C 62.1 0.1 1 668 . 68 SER CB C 62.1 0.1 1 669 . 68 SER N N 118.3 0.1 1 670 . 69 GLN H H 8.51 0.01 1 671 . 69 GLN HA H 4.32 0.01 1 672 . 69 GLN HB2 H 2.47 0.01 2 673 . 69 GLN HB3 H 1.56 0.01 2 674 . 69 GLN HG2 H 2.69 0.01 2 675 . 69 GLN HG3 H 2.47 0.01 2 676 . 69 GLN HE21 H 7.42 0.01 2 677 . 69 GLN HE22 H 5.86 0.01 2 678 . 69 GLN C C 177.9 0.1 1 679 . 69 GLN CA C 58.9 0.1 1 680 . 69 GLN CB C 27.9 0.1 1 681 . 69 GLN CG C 34.4 0.1 1 682 . 69 GLN N N 124.2 0.1 1 683 . 69 GLN NE2 N 107.7 0.1 1 684 . 70 LYS H H 8.80 0.01 1 685 . 70 LYS HA H 3.71 0.01 1 686 . 70 LYS HB2 H 2.16 0.01 2 687 . 70 LYS HB3 H 1.95 0.01 2 688 . 70 LYS HG2 H 1.57 0.01 2 689 . 70 LYS HG3 H 1.20 0.01 2 690 . 70 LYS HD2 H 0.92 0.01 2 691 . 70 LYS HD3 H 0.73 0.01 2 692 . 70 LYS C C 177.6 0.1 1 693 . 70 LYS CA C 60.0 0.1 1 694 . 70 LYS CB C 32.3 0.1 1 695 . 70 LYS CG C 24.9 0.1 1 696 . 70 LYS CD C 29.9 0.1 1 697 . 70 LYS CE C 40.9 0.1 1 698 . 70 LYS N N 119.8 0.1 1 699 . 71 LYS H H 8.10 0.01 1 700 . 71 LYS HA H 4.03 0.01 1 701 . 71 LYS HB2 H 1.95 0.01 1 702 . 71 LYS HB3 H 1.71 0.01 1 703 . 71 LYS HG2 H 1.54 0.01 1 704 . 71 LYS HG3 H 1.54 0.01 1 705 . 71 LYS HD2 H 1.45 0.01 1 706 . 71 LYS HD3 H 1.45 0.01 1 707 . 71 LYS HE2 H 2.99 0.01 1 708 . 71 LYS HE3 H 2.99 0.01 1 709 . 71 LYS C C 179.0 0.1 1 710 . 71 LYS CA C 59.7 0.1 1 711 . 71 LYS CB C 32.4 0.1 1 712 . 71 LYS CG C 24.9 0.1 1 713 . 71 LYS CD C 29.2 0.1 1 714 . 71 LYS CE C 42.1 0.1 1 715 . 71 LYS N N 118.5 0.1 1 716 . 72 SER H H 8.44 0.01 1 717 . 72 SER HA H 4.19 0.01 1 718 . 72 SER HB2 H 4.04 0.01 1 719 . 72 SER HB3 H 4.04 0.01 1 720 . 72 SER C C 177.4 0.1 1 721 . 72 SER CA C 61.1 0.1 1 722 . 72 SER CB C 62.2 0.1 1 723 . 72 SER N N 115.0 0.1 1 724 . 73 ALA H H 8.12 0.01 1 725 . 73 ALA HA H 3.83 0.01 1 726 . 73 ALA HB H 1.49 0.01 1 727 . 73 ALA C C 179.1 0.1 1 728 . 73 ALA CA C 55.0 0.1 1 729 . 73 ALA CB C 19.2 0.1 1 730 . 73 ALA N N 122.7 0.1 1 731 . 74 MET H H 8.38 0.01 1 732 . 74 MET HA H 3.59 0.01 1 733 . 74 MET HB2 H 2.13 0.01 2 734 . 74 MET HB3 H 1.97 0.01 2 735 . 74 MET HG2 H 2.83 0.01 1 736 . 74 MET HG3 H 2.83 0.01 1 737 . 74 MET C C 178.8 0.1 1 738 . 74 MET CA C 60.3 0.1 1 739 . 74 MET CB C 33.2 0.1 1 740 . 74 MET CG C 33.2 0.1 1 741 . 74 MET N N 115.3 0.1 1 742 . 75 MET H H 8.12 0.01 1 743 . 75 MET HA H 4.21 0.01 1 744 . 75 MET HB2 H 2.76 0.01 2 745 . 75 MET HB3 H 2.61 0.01 2 746 . 75 MET HG2 H 2.25 0.01 1 747 . 75 MET HG3 H 2.25 0.01 1 748 . 75 MET C C 178.8 0.1 1 749 . 75 MET CA C 58.6 0.1 1 750 . 75 MET CB C 32.2 0.1 1 751 . 75 MET CG C 32.2 0.1 1 752 . 75 MET N N 118.5 0.1 1 753 . 76 LYS H H 7.98 0.01 1 754 . 76 LYS HA H 3.97 0.01 1 755 . 76 LYS HB2 H 1.83 0.01 1 756 . 76 LYS HB3 H 1.83 0.01 1 757 . 76 LYS HG2 H 1.31 0.01 1 758 . 76 LYS HG3 H 1.31 0.01 1 759 . 76 LYS HD2 H 1.31 0.01 1 760 . 76 LYS HD3 H 1.31 0.01 1 761 . 76 LYS HE2 H 2.99 0.01 1 762 . 76 LYS HE3 H 2.99 0.01 1 763 . 76 LYS C C 178.5 0.1 1 764 . 76 LYS CA C 60.0 0.1 1 765 . 76 LYS CB C 32.8 0.1 1 766 . 76 LYS CG C 27.2 0.1 1 767 . 76 LYS CD C 30.5 0.1 1 768 . 76 LYS CE C 42.2 0.1 1 769 . 76 LYS N N 120.9 0.1 1 770 . 77 LEU H H 7.70 0.01 1 771 . 77 LEU HA H 4.11 0.01 1 772 . 77 LEU HB2 H 1.55 0.01 1 773 . 77 LEU HB3 H 1.55 0.01 1 774 . 77 LEU HG H 1.09 0.01 1 775 . 77 LEU HD1 H 0.56 0.01 1 776 . 77 LEU HD2 H 0.65 0.01 1 777 . 77 LEU C C 177.0 0.1 1 778 . 77 LEU CA C 55.0 0.1 1 779 . 77 LEU CB C 42.7 0.1 1 780 . 77 LEU CD1 C 25.5 0.1 1 781 . 77 LEU CD2 C 22.0 0.1 1 782 . 77 LEU N N 116.3 0.1 1 783 . 78 GLY H H 7.84 0.01 1 784 . 78 GLY HA2 H 3.97 0.01 1 785 . 78 GLY HA3 H 3.85 0.01 1 786 . 78 GLY C C 174.8 0.1 1 787 . 78 GLY CA C 46.3 0.1 1 788 . 78 GLY N N 107.8 0.1 1 789 . 79 VAL H H 7.75 0.01 1 790 . 79 VAL HA H 4.68 0.01 1 791 . 79 VAL HB H 1.99 0.01 1 792 . 79 VAL HG1 H 0.78 0.01 1 793 . 79 VAL HG2 H 0.77 0.01 1 794 . 79 VAL C C 176.0 0.1 1 795 . 79 VAL CA C 59.0 0.1 1 796 . 79 VAL CB C 34.2 0.1 1 797 . 79 VAL CG1 C 21.8 0.1 1 798 . 79 VAL CG2 C 19.7 0.1 1 799 . 79 VAL N N 112.0 0.1 1 800 . 80 ASP H H 8.64 0.01 1 801 . 80 ASP HA H 4.66 0.01 1 802 . 80 ASP HB2 H 2.79 0.01 2 803 . 80 ASP HB3 H 2.55 0.01 2 804 . 80 ASP C C 175.7 0.1 1 805 . 80 ASP CA C 54.1 0.1 1 806 . 80 ASP CB C 42.3 0.1 1 807 . 80 ASP N N 119.2 0.1 1 808 . 81 ASN H H 8.30 0.01 1 809 . 81 ASN HB2 H 2.99 0.01 1 810 . 81 ASN HB3 H 2.90 0.01 1 811 . 81 ASN HD21 H 7.88 0.01 2 812 . 81 ASN HD22 H 6.97 0.01 2 813 . 81 ASN N N 117.4 0.1 1 814 . 81 ASN ND2 N 116.9 0.1 1 815 . 82 ASP HA H 4.20 0.01 1 816 . 82 ASP HB2 H 2.83 0.01 2 817 . 82 ASP HB3 H 2.75 0.01 2 818 . 82 ASP C C 177.7 0.1 1 819 . 82 ASP CA C 55.3 0.1 1 820 . 82 ASP CB C 40.6 0.1 1 821 . 83 ILE H H 8.15 0.01 1 822 . 83 ILE HA H 3.83 0.01 1 823 . 83 ILE HB H 1.97 0.01 1 824 . 83 ILE HG12 H 1.65 0.01 2 825 . 83 ILE HG13 H 1.28 0.01 2 826 . 83 ILE HG2 H 1.28 0.01 1 827 . 83 ILE HD1 H 0.94 0.01 1 828 . 83 ILE C C 178.4 0.1 1 829 . 83 ILE CA C 64.4 0.1 1 830 . 83 ILE CB C 37.6 0.1 1 831 . 83 ILE CG1 C 28.9 0.1 1 832 . 83 ILE CG2 C 17.2 0.1 1 833 . 83 ILE CD1 C 12.5 0.1 1 834 . 83 ILE N N 122.7 0.1 1 835 . 84 ALA H H 8.31 0.01 1 836 . 84 ALA HA H 4.28 0.01 1 837 . 84 ALA HB H 1.57 0.01 1 838 . 84 ALA C C 181.3 0.1 1 839 . 84 ALA CA C 54.8 0.1 1 840 . 84 ALA CB C 18.8 0.1 1 841 . 84 ALA N N 122.9 0.1 1 842 . 85 LEU H H 8.24 0.01 1 843 . 85 LEU HA H 4.18 0.01 1 844 . 85 LEU HB2 H 2.30 0.01 2 845 . 85 LEU HB3 H 1.47 0.01 2 846 . 85 LEU HG H 1.47 0.01 1 847 . 85 LEU HD1 H 0.68 0.01 1 848 . 85 LEU HD2 H 0.90 0.01 1 849 . 85 LEU C C 177.4 0.1 1 850 . 85 LEU CA C 58.4 0.1 1 851 . 85 LEU CB C 41.6 0.1 1 852 . 85 LEU CD1 C 25.7 0.1 1 853 . 85 LEU CD2 C 23.0 0.1 1 854 . 85 LEU N N 120.0 0.1 1 855 . 86 LEU H H 8.54 0.01 1 856 . 86 LEU HA H 4.14 0.01 1 857 . 86 LEU HB2 H 1.92 0.01 2 858 . 86 LEU HB3 H 1.66 0.01 2 859 . 86 LEU HG H 1.66 0.01 1 860 . 86 LEU HD1 H 0.88 0.01 2 861 . 86 LEU HD2 H 0.84 0.01 2 862 . 86 LEU C C 180.1 0.1 1 863 . 86 LEU CA C 58.2 0.1 1 864 . 86 LEU CB C 41.1 0.1 1 865 . 86 LEU CG C 25.0 0.1 1 866 . 86 LEU CD1 C 25.0 0.1 1 867 . 86 LEU CD2 C 23.5 0.1 1 868 . 86 LEU N N 120.1 0.1 1 869 . 87 ASN H H 8.57 0.01 1 870 . 87 ASN HA H 4.51 0.01 1 871 . 87 ASN HB2 H 2.90 0.01 1 872 . 87 ASN HB3 H 2.90 0.01 1 873 . 87 ASN HD21 H 7.73 0.01 2 874 . 87 ASN HD22 H 6.99 0.01 2 875 . 87 ASN C C 177.8 0.1 1 876 . 87 ASN CA C 56.0 0.1 1 877 . 87 ASN CB C 38.2 0.1 1 878 . 87 ASN N N 118.8 0.1 1 879 . 87 ASN ND2 N 112.1 0.1 1 880 . 88 TYR H H 8.33 0.01 1 881 . 88 TYR HA H 4.25 0.01 1 882 . 88 TYR HB2 H 3.33 0.01 1 883 . 88 TYR HB3 H 3.23 0.01 1 884 . 88 TYR HD1 H 6.97 0.01 1 885 . 88 TYR HD2 H 6.97 0.01 1 886 . 88 TYR HE1 H 6.74 0.01 1 887 . 88 TYR HE2 H 6.74 0.01 1 888 . 88 TYR C C 178.2 0.1 1 889 . 88 TYR CA C 61.4 0.1 1 890 . 88 TYR CB C 38.3 0.1 1 891 . 88 TYR N N 122.8 0.1 1 892 . 89 LEU H H 8.55 0.01 1 893 . 89 LEU HA H 3.97 0.01 1 894 . 89 LEU HB2 H 1.99 0.01 2 895 . 89 LEU HB3 H 1.52 0.01 2 896 . 89 LEU HG H 1.99 0.01 1 897 . 89 LEU HD1 H 0.90 0.01 2 898 . 89 LEU HD2 H 0.91 0.01 2 899 . 89 LEU C C 178.4 0.1 1 900 . 89 LEU CA C 57.2 0.1 1 901 . 89 LEU CB C 41.4 0.1 1 902 . 89 LEU CG C 26.5 0.1 1 903 . 89 LEU CD1 C 26.5 0.1 1 904 . 89 LEU CD2 C 22.3 0.1 1 905 . 89 LEU N N 118.4 0.1 1 906 . 90 SER H H 8.04 0.01 1 907 . 90 SER HA H 4.38 0.01 1 908 . 90 SER HB2 H 4.02 0.01 1 909 . 90 SER HB3 H 4.02 0.01 1 910 . 90 SER C C 175.4 0.1 1 911 . 90 SER CA C 60.2 0.1 1 912 . 90 SER CB C 63.6 0.1 1 913 . 90 SER N N 112.8 0.1 1 914 . 91 SER H H 7.83 0.01 1 915 . 91 SER HA H 4.40 0.01 1 916 . 91 SER HB2 H 3.95 0.01 1 917 . 91 SER HB3 H 3.95 0.01 1 918 . 91 SER C C 175.1 0.1 1 919 . 91 SER CA C 59.9 0.1 1 920 . 91 SER CB C 63.8 0.1 1 921 . 91 SER N N 116.9 0.1 1 922 . 92 VAL H H 7.70 0.01 1 923 . 92 VAL HA H 4.12 0.01 1 924 . 92 VAL HB H 2.04 0.01 1 925 . 92 VAL HG1 H 0.81 0.01 1 926 . 92 VAL HG2 H 0.79 0.01 1 927 . 92 VAL C C 176.2 0.1 1 928 . 92 VAL CA C 62.7 0.1 1 929 . 92 VAL CB C 32.1 0.1 1 930 . 92 VAL CG1 C 21.3 0.1 1 931 . 92 VAL CG2 C 20.6 0.1 1 932 . 92 VAL N N 119.6 0.1 1 933 . 93 SER H H 8.09 0.01 1 934 . 93 SER HA H 4.42 0.01 1 935 . 93 SER HB2 H 3.81 0.01 1 936 . 93 SER HB3 H 3.81 0.01 1 937 . 93 SER C C 174.6 0.1 1 938 . 93 SER CA C 58.7 0.1 1 939 . 93 SER CB C 63.9 0.1 1 940 . 93 SER N N 117.4 0.1 1 941 . 94 MET H H 8.31 0.01 1 942 . 94 MET HA H 4.57 0.01 1 943 . 94 MET HB2 H 2.13 0.01 2 944 . 94 MET HB3 H 2.02 0.01 2 945 . 94 MET HG2 H 2.63 0.01 2 946 . 94 MET HG3 H 2.52 0.01 2 947 . 94 MET C C 176.1 0.1 1 948 . 94 MET CA C 55.3 0.1 1 949 . 94 MET CB C 32.8 0.1 1 950 . 94 MET CG C 32.1 0.1 1 951 . 94 MET N N 122.0 0.1 1 952 . 95 THR H H 8.19 0.01 1 953 . 95 THR HA H 4.14 0.01 1 954 . 95 THR CA C 60.2 0.1 1 955 . 95 THR CB C 69.8 0.1 1 956 . 95 THR N N 118.1 0.1 1 957 . 96 PRO HA H 4.50 0.01 1 958 . 96 PRO HB2 H 2.31 0.01 2 959 . 96 PRO HB3 H 1.94 0.01 2 960 . 96 PRO HG2 H 2.06 0.01 1 961 . 96 PRO HG3 H 2.06 0.01 1 962 . 96 PRO HD2 H 3.88 0.01 2 963 . 96 PRO HD3 H 3.71 0.01 2 964 . 96 PRO C C 176.8 0.1 1 965 . 96 PRO CA C 63.2 0.1 1 966 . 96 PRO CB C 32.1 0.1 1 967 . 96 PRO CG C 27.5 0.1 1 968 . 96 PRO CD C 51.1 0.1 1 969 . 97 VAL H H 8.32 0.01 1 970 . 97 VAL HA H 4.14 0.01 1 971 . 97 VAL HB H 2.10 0.01 1 972 . 97 VAL HG1 H 0.97 0.01 2 973 . 97 VAL HG2 H 0.96 0.01 2 974 . 97 VAL C C 175.8 0.1 1 975 . 97 VAL CA C 62.1 0.1 1 976 . 97 VAL CB C 32.8 0.1 1 977 . 97 VAL CG1 C 21.2 0.1 1 978 . 97 VAL CG2 C 20.5 0.1 1 979 . 97 VAL N N 120.1 0.1 1 980 . 98 ASP H H 8.46 0.01 1 981 . 98 ASP HA H 4.64 0.01 1 982 . 98 ASP HB2 H 2.71 0.01 2 983 . 98 ASP HB3 H 2.63 0.01 2 984 . 98 ASP C C 175.0 0.1 1 985 . 98 ASP CA C 54.4 0.1 1 986 . 98 ASP CB C 41.2 0.1 1 987 . 98 ASP N N 124.3 0.1 1 988 . 99 LYS H H 7.89 0.01 1 989 . 99 LYS HA H 4.16 0.01 1 990 . 99 LYS HB2 H 1.80 0.01 2 991 . 99 LYS HB3 H 1.69 0.01 2 992 . 99 LYS C C 181.2 0.1 1 993 . 99 LYS CA C 57.7 0.1 1 994 . 99 LYS CB C 33.8 0.1 1 995 . 99 LYS N N 126.4 0.1 1 stop_ save_