data_4037 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli ; _BMRB_accession_number 4037 _BMRB_flat_file_name bmr4037.str _Entry_type original _Submission_date 1997-06-26 _Accession_date 1997-06-26 _Entry_origination BMRB _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 Clubb Robert T. . 2 Thanabal Venkataraman . . 3 Fejzo Jasna . . 4 Ferguson Stephen B. . 5 Zydowsky Lynne . . 6 Baker C. Hunter . 7 Walsh Christopher T. . 8 Wagner Gerhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 323 "13C chemical shifts" 328 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-07-05 version_update BMRB 'converted to NMR-STAR 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Clubb, R. T., Thanabal, V., Fejzo, J., Ferguson, S. B., Zydowsky, L., Baker, C. H., Walsh, C. T., and Wagner, G., "Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli," Biochemistry 32, 6391-6401 (1993). ; _Citation_title ; Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 93298762 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Clubb Robert T. . 2 Thanabal Venkataraman . . 3 Fejzo Jasna . . 4 Ferguson Stephen B. . 5 Zydowsky Lynne . . 6 Baker C. Hunter . 7 Walsh Christopher T. . 8 Wagner Gerhard . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 32 _Journal_issue 25 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6391 _Page_last 6401 _Year 1993 _Details . loop_ _Keyword NMR 'Peptidyl-Prolyl Isomerase' cyclophilin stop_ save_ ################################## # Molecular system description # ################################## save_system_eCyP _Saveframe_category molecular_system _Mol_system_name 'periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase' _Abbreviation_common eCyP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label eCyP $eCyP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_eCyP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'periplasmic cyclophilin type cys-trans peptidyl-prolyl isomerase' _Abbreviation_common eCyP _Molecular_mass 18244 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; AAKGDPHVLLTTSAGNIELE LDKQKAPVSVQNFVDYVNSG FYNNTTFHRVIPGFMIQGGG FTEQMQQKKPNPPIKNEADN GLRNTRGTIAMARTADKDSA TSQFFINVADNAFLDHGQRD FGYAVFGKVVKGMDVADKIS QVPTHDVGPYQNVPSKPVVI LSAKVLP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 ALA 2 1 ALA 3 2 LYS 4 3 GLY 5 4 ASP 6 5 PRO 7 6 HIS 8 7 VAL 9 8 LEU 10 9 LEU 11 10 THR 12 11 THR 13 12 SER 14 13 ALA 15 14 GLY 16 15 ASN 17 16 ILE 18 17 GLU 19 18 LEU 20 19 GLU 21 20 LEU 22 21 ASP 23 22 LYS 24 23 GLN 25 24 LYS 26 25 ALA 27 26 PRO 28 27 VAL 29 28 SER 30 29 VAL 31 30 GLN 32 31 ASN 33 32 PHE 34 33 VAL 35 34 ASP 36 35 TYR 37 36 VAL 38 37 ASN 39 38 SER 40 39 GLY 41 40 PHE 42 41 TYR 43 42 ASN 44 43 ASN 45 44 THR 46 45 THR 47 46 PHE 48 47 HIS 49 48 ARG 50 49 VAL 51 50 ILE 52 51 PRO 53 52 GLY 54 53 PHE 55 54 MET 56 55 ILE 57 56 GLN 58 57 GLY 59 58 GLY 60 59 GLY 61 60 PHE 62 61 THR 63 62 GLU 64 63 GLN 65 64 MET 66 65 GLN 67 66 GLN 68 67 LYS 69 68 LYS 70 69 PRO 71 70 ASN 72 71 PRO 73 72 PRO 74 73 ILE 75 74 LYS 76 75 ASN 77 76 GLU 78 77 ALA 79 78 ASP 80 79 ASN 81 80 GLY 82 81 LEU 83 82 ARG 84 83 ASN 85 84 THR 86 85 ARG 87 86 GLY 88 87 THR 89 88 ILE 90 89 ALA 91 90 MET 92 91 ALA 93 92 ARG 94 93 THR 95 94 ALA 96 95 ASP 97 96 LYS 98 97 ASP 99 98 SER 100 99 ALA 101 100 THR 102 101 SER 103 102 GLN 104 103 PHE 105 104 PHE 106 105 ILE 107 106 ASN 108 107 VAL 109 108 ALA 110 109 ASP 111 110 ASN 112 111 ALA 113 112 PHE 114 113 LEU 115 114 ASP 116 115 HIS 117 116 GLY 118 117 GLN 119 118 ARG 120 119 ASP 121 120 PHE 122 121 GLY 123 122 TYR 124 123 ALA 125 124 VAL 126 125 PHE 127 126 GLY 128 127 LYS 129 128 VAL 130 129 VAL 131 130 LYS 132 131 GLY 133 132 MET 134 133 ASP 135 134 VAL 136 135 ALA 137 136 ASP 138 137 LYS 139 138 ILE 140 139 SER 141 140 GLN 142 141 VAL 143 142 PRO 144 143 THR 145 144 HIS 146 145 ASP 147 146 VAL 148 147 GLY 149 148 PRO 150 149 TYR 151 150 GLN 152 151 ASN 153 152 VAL 154 153 PRO 155 154 SER 156 155 LYS 157 156 PRO 158 157 VAL 159 158 VAL 160 159 ILE 161 160 LEU 162 161 SER 163 162 ALA 164 163 LYS 165 164 VAL 166 165 LEU 167 166 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 1CLH "Three-Dimensional Solution Structure Of Escherichia Coli Periplasmic Cyclophilin" 99.40 166 100.00 100.00 1.08e-116 PDB 1J2A "Structure Of E. Coli Cyclophilin B K163t Mutant" 99.40 166 99.40 99.40 6.19e-116 PDB 1V9T "Structure Of E. Coli Cyclophilin B K163t Mutant Bound To Succinyl-Ala- Pro-Ala-P-Nitroanilide" 99.40 166 99.40 99.40 6.19e-116 PDB 1VAI "Structure Of E. Coli Cyclophilin B K163t Mutant Bound To N- Acetyl-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin" 99.40 166 99.40 99.40 6.19e-116 DBJ BAB37637 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli O157:H7 str. Sakai]" 100.00 190 100.00 100.00 4.81e-118 DBJ BAE77927 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli str. K12 substr. W3110]" 100.00 190 100.00 100.00 4.81e-118 DBJ BAG79149 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli SE11]" 100.00 190 100.00 100.00 4.81e-118 DBJ BAI27622 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli O26:H11 str. 11368]" 100.00 190 100.00 100.00 4.81e-118 DBJ BAI32792 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli O103:H2 str. 12009]" 100.00 190 100.00 100.00 4.81e-118 EMBL CAD08141 "peptidyl-prolyl cis-trans isomerase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 190 97.01 98.80 6.39e-115 EMBL CAP77816 "Peptidyl-prolyl cis-trans isomerase A [Escherichia coli LF82]" 100.00 190 100.00 100.00 4.81e-118 EMBL CAQ33683 "peptidyl-prolyl cis-trans isomerase A (rotamase A) [Escherichia coli BL21(DE3)]" 100.00 190 99.40 100.00 2.62e-117 EMBL CAQ90814 "peptidyl-prolyl cis-trans isomerase A (rotamase A) [Escherichia fergusonii ATCC 35469]" 100.00 190 98.20 99.40 4.16e-116 EMBL CAR00303 "peptidyl-prolyl cis-trans isomerase A (rotamase A) [Escherichia coli IAI1]" 100.00 190 100.00 100.00 4.81e-118 GB AAA23451 "peptidyl-prolyl cis-trans isomerase a [Escherichia coli]" 100.00 190 100.00 100.00 4.81e-118 GB AAA23772 "ORF190 [Escherichia coli]" 100.00 190 100.00 100.00 4.81e-118 GB AAA24261 "protein of unknown function (utu), partial [Escherichia coli]" 92.22 154 100.00 100.00 3.19e-107 GB AAA58160 "peptidyl-prolyl cis-trans isomerase a [Escherichia coli str. K-12 substr. MG1655]" 100.00 190 100.00 100.00 4.81e-118 GB AAC76388 "peptidyl-prolyl cis-trans isomerase A (rotamase A) [Escherichia coli str. K-12 substr. MG1655]" 100.00 190 100.00 100.00 4.81e-118 PIR AI1001 "peptidylprolyl isomerase (EC 5.2.1.8) - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 190 97.01 98.80 6.39e-115 REF NP_312241 "peptidyl-prolyl cis-trans isomerase A [Escherichia coli O157:H7 str. Sakai]" 100.00 190 100.00 100.00 4.81e-118 REF NP_417822 "peptidyl-prolyl cis-trans isomerase A (rotamase A) [Escherichia coli str. K-12 substr. MG1655]" 100.00 190 100.00 100.00 4.81e-118 REF NP_458430 "peptidyl-prolyl cis-trans isomerase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 190 97.01 98.80 6.39e-115 REF NP_462375 "peptidyl-prolyl cis-trans isomerase A [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 190 97.01 98.80 7.77e-115 REF NP_709138 "peptidyl-prolyl cis-trans isomerase A [Shigella flexneri 2a str. 301]" 100.00 193 100.00 100.00 3.53e-118 SP P0AFL3 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Rotamase A; Fla" 100.00 190 100.00 100.00 4.81e-118 SP P0AFL4 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Rotamase A; Fla" 100.00 190 100.00 100.00 4.81e-118 SP P0AFL5 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Rotamase A; Fla" 100.00 190 100.00 100.00 4.81e-118 SP P20753 "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Rotamase A; Flags: Precursor" 100.00 190 97.01 98.80 7.77e-115 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $eCyP 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $eCyP 'recombinant technology' E.coli Escherichia coli . plasmid pJLEC-2B stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $eCyP . mM 0.2 2.0 [U-15N] phosphate_buffer 50 mM . . . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $eCyP . mM 0.2 2.0 [U-13C;U-15N] phosphate_buffer 50 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX500 _Field_strength 500MHz _Details . save_ save_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX600 _Field_strength 600MHz _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_one _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 TSP H 1 methyl ppm 0.0 . . . . . dioxane C 13 methyl ppm 67.8 external . . . . NH4NO2 N 15 nitrogen ppm 376.25 . . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name eCyP _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 ALA HA H 4.02 . 1 2 . 1 ALA C C 172.4 . 1 3 . 1 ALA CA C 50.1 . 1 4 . 2 ALA H H 8.06 . 1 5 . 2 ALA HA H 4.41 . 1 6 . 2 ALA C C 176.3 . 1 7 . 2 ALA CA C 50.5 . 1 8 . 2 ALA N N 127.1 . 1 9 . 3 LYS H H 8.46 . 1 10 . 3 LYS HA H 4.26 . 1 11 . 3 LYS C C 175.9 . 1 12 . 3 LYS CA C 55.2 . 1 13 . 3 LYS N N 124.5 . 1 14 . 4 GLY HA2 H 3.95 . 1 15 . 4 GLY HA3 H 3.95 . 1 16 . 4 GLY C C 172.7 . 1 17 . 4 GLY CA C 43.3 . 1 18 . 4 GLY N N 114.3 . 1 19 . 5 ASP H H 8.12 . 1 20 . 5 ASP HA H 5.13 . 1 21 . 5 ASP C C 173.9 . 1 22 . 5 ASP CA C 51.6 . 1 23 . 5 ASP N N 127.2 . 1 24 . 6 PRO HA H 4.62 . 1 25 . 6 PRO C C 175.0 . 1 26 . 6 PRO CA C 61.4 . 1 27 . 7 HIS H H 9.51 . 1 28 . 7 HIS HA H 6.01 . 1 29 . 7 HIS C C 173.3 . 1 30 . 7 HIS CA C 52.1 . 1 31 . 7 HIS N N 123.2 . 1 32 . 8 VAL H H 8.65 . 1 33 . 8 VAL HA H 5.05 . 1 34 . 8 VAL C C 172.0 . 1 35 . 8 VAL CA C 58.1 . 1 36 . 8 VAL N N 123.7 . 1 37 . 9 LEU H H 9.30 . 1 38 . 9 LEU HA H 5.07 . 1 39 . 9 LEU C C 174.9 . 1 40 . 9 LEU CA C 51.6 . 1 41 . 9 LEU N N 132.2 . 1 42 . 10 LEU H H 9.83 . 1 43 . 10 LEU HA H 4.96 . 1 44 . 10 LEU C C 173.7 . 1 45 . 10 LEU CA C 51.6 . 1 46 . 10 LEU N N 132.0 . 1 47 . 11 THR H H 9.13 . 1 48 . 11 THR HA H 4.82 . 1 49 . 11 THR C C 173.6 . 1 50 . 11 THR CA C 60.7 . 1 51 . 11 THR N N 127.1 . 1 52 . 12 THR H H 7.97 . 1 53 . 12 THR HA H 6.14 . 1 54 . 12 THR C C 175.6 . 1 55 . 12 THR CA C 57.8 . 1 56 . 12 THR N N 120.8 . 1 57 . 13 SER H H 9.62 . 1 58 . 13 SER HA H 4.24 . 1 59 . 13 SER C C 172.4 . 1 60 . 13 SER CA C 59.3 . 1 61 . 13 SER N N 120.6 . 1 62 . 14 ALA H H 8.28 . 1 63 . 14 ALA HA H 4.62 . 1 64 . 14 ALA C C 174.1 . 1 65 . 14 ALA CA C 49.7 . 1 66 . 14 ALA N N 126.1 . 1 67 . 15 GLY H H 7.37 . 1 68 . 15 GLY HA2 H 3.80 . 2 69 . 15 GLY HA3 H 4.67 . 2 70 . 15 GLY C C 173.5 . 1 71 . 15 GLY CA C 42.1 . 1 72 . 15 GLY N N 109.9 . 1 73 . 16 ASN H H 9.06 . 1 74 . 16 ASN HA H 5.79 . 1 75 . 16 ASN C C 173.7 . 1 76 . 16 ASN CA C 51.0 . 1 77 . 16 ASN N N 125.7 . 1 78 . 17 ILE H H 8.99 . 1 79 . 17 ILE HA H 4.60 . 1 80 . 17 ILE C C 172.6 . 1 81 . 17 ILE CA C 59.1 . 1 82 . 17 ILE N N 123.6 . 1 83 . 18 GLU H H 9.19 . 1 84 . 18 GLU HA H 5.39 . 1 85 . 18 GLU C C 173.8 . 1 86 . 18 GLU CA C 52.9 . 1 87 . 18 GLU N N 132.2 . 1 88 . 19 LEU H H 9.54 . 1 89 . 19 LEU HA H 5.11 . 1 90 . 19 LEU C C 174.5 . 1 91 . 19 LEU CA C 51.1 . 1 92 . 19 LEU N N 130.0 . 1 93 . 20 GLU H H 9.01 . 1 94 . 20 GLU HA H 4.46 . 1 95 . 20 GLU C C 174.2 . 1 96 . 20 GLU CA C 53.8 . 1 97 . 20 GLU N N 124.6 . 1 98 . 21 LEU H H 8.73 . 1 99 . 21 LEU HA H 4.76 . 1 100 . 21 LEU C C 172.3 . 1 101 . 21 LEU CA C 52.3 . 1 102 . 21 LEU N N 132.5 . 1 103 . 22 ASP H H 8.16 . 1 104 . 22 ASP HA H 4.58 . 1 105 . 22 ASP C C 173.3 . 1 106 . 22 ASP CA C 50.8 . 1 107 . 22 ASP N N 125.3 . 1 108 . 23 LYS H H 7.94 . 1 109 . 23 LYS HA H 3.75 . 1 110 . 23 LYS C C 175.9 . 1 111 . 23 LYS CA C 57.2 . 1 112 . 23 LYS N N 128.1 . 1 113 . 24 GLN H H 8.61 . 1 114 . 24 GLN HA H 4.09 . 1 115 . 24 GLN C C 177.3 . 1 116 . 24 GLN CA C 56.7 . 1 117 . 24 GLN N N 118.8 . 1 118 . 25 LYS H H 7.67 . 1 119 . 25 LYS HA H 4.41 . 1 120 . 25 LYS C C 176.0 . 1 121 . 25 LYS CA C 54.5 . 1 122 . 25 LYS N N 118.4 . 1 123 . 26 ALA H H 8.12 . 1 124 . 26 ALA HA H 4.89 . 1 125 . 26 ALA C C 171.0 . 1 126 . 26 ALA CA C 48.3 . 1 127 . 26 ALA N N 127.9 . 1 128 . 27 PRO HA H 4.34 . 1 129 . 27 PRO C C 180.3 . 1 130 . 27 PRO CA C 64.8 . 1 131 . 28 VAL H H 9.99 . 1 132 . 28 VAL HA H 3.63 . 1 133 . 28 VAL C C 178.3 . 1 134 . 28 VAL CA C 65.0 . 1 135 . 28 VAL N N 126.3 . 1 136 . 29 SER H H 9.74 . 1 137 . 29 SER HA H 3.96 . 1 138 . 29 SER C C 176.7 . 1 139 . 29 SER CA C 60.1 . 1 140 . 29 SER N N 123.9 . 1 141 . 30 VAL H H 9.29 . 1 142 . 30 VAL HA H 3.51 . 1 143 . 30 VAL C C 175.0 . 1 144 . 30 VAL CA C 67.0 . 1 145 . 30 VAL N N 126.3 . 1 146 . 31 GLN H H 7.69 . 1 147 . 31 GLN HA H 3.86 . 1 148 . 31 GLN C C 175.7 . 1 149 . 31 GLN CA C 57.0 . 1 150 . 31 GLN N N 121.9 . 1 151 . 32 ASN H H 7.93 . 1 152 . 32 ASN HA H 4.12 . 1 153 . 32 ASN C C 173.7 . 1 154 . 32 ASN CA C 55.1 . 1 155 . 32 ASN N N 119.1 . 1 156 . 33 PHE H H 7.83 . 1 157 . 33 PHE HA H 4.48 . 1 158 . 33 PHE C C 176.6 . 1 159 . 33 PHE CA C 60.7 . 1 160 . 33 PHE N N 121.7 . 1 161 . 34 VAL H H 8.91 . 1 162 . 34 VAL HA H 3.40 . 1 163 . 34 VAL C C 176.0 . 1 164 . 34 VAL CA C 65.2 . 1 165 . 34 VAL N N 120.4 . 1 166 . 35 ASP H H 8.39 . 1 167 . 35 ASP HA H 4.40 . 1 168 . 35 ASP C C 179.4 . 1 169 . 35 ASP CA C 56.0 . 1 170 . 35 ASP N N 125.0 . 1 171 . 36 TYR H H 7.50 . 1 172 . 36 TYR HA H 3.94 . 1 173 . 36 TYR C C 177.1 . 1 174 . 36 TYR CA C 60.8 . 1 175 . 36 TYR N N 124.1 . 1 176 . 37 VAL H H 8.47 . 1 177 . 37 VAL HA H 3.56 . 1 178 . 37 VAL C C 179.6 . 1 179 . 37 VAL CA C 64.8 . 1 180 . 37 VAL N N 122.9 . 1 181 . 38 ASN H H 9.34 . 1 182 . 38 ASN HA H 4.53 . 1 183 . 38 ASN C C 176.0 . 1 184 . 38 ASN CA C 53.8 . 1 185 . 38 ASN N N 121.8 . 1 186 . 39 SER H H 7.94 . 1 187 . 39 SER HA H 4.54 . 1 188 . 39 SER C C 174.1 . 1 189 . 39 SER CA C 57.5 . 1 190 . 39 SER N N 116.6 . 1 191 . 40 GLY H H 7.93 . 1 192 . 40 GLY HA2 H 3.96 . 2 193 . 40 GLY HA3 H 4.34 . 2 194 . 40 GLY C C 174.4 . 1 195 . 40 GLY CA C 44.2 . 1 196 . 40 GLY N N 113.7 . 1 197 . 41 PHE H H 8.11 . 1 198 . 41 PHE HA H 3.76 . 1 199 . 41 PHE C C 175.3 . 1 200 . 41 PHE CA C 60.2 . 1 201 . 41 PHE N N 124.8 . 1 202 . 42 TYR H H 7.42 . 1 203 . 42 TYR HA H 4.49 . 1 204 . 42 TYR C C 175.6 . 1 205 . 42 TYR CA C 56.3 . 1 206 . 42 TYR N N 113.5 . 1 207 . 43 ASN H H 7.38 . 1 208 . 43 ASN HA H 4.06 . 1 209 . 43 ASN C C 174.6 . 1 210 . 43 ASN CA C 53.0 . 1 211 . 43 ASN N N 125.7 . 1 212 . 44 ASN H H 9.54 . 1 213 . 44 ASN HA H 4.13 . 1 214 . 44 ASN C C 174.7 . 1 215 . 44 ASN CA C 54.0 . 1 216 . 44 ASN N N 120.8 . 1 217 . 45 THR H H 7.86 . 1 218 . 45 THR HA H 5.00 . 1 219 . 45 THR C C 172.7 . 1 220 . 45 THR CA C 60.2 . 1 221 . 45 THR N N 111.4 . 1 222 . 46 THR H H 7.97 . 1 223 . 46 THR HA H 5.52 . 1 224 . 46 THR C C 177.8 . 1 225 . 46 THR CA C 58.2 . 1 226 . 46 THR N N 108.4 . 1 227 . 47 PHE H H 8.26 . 1 228 . 47 PHE HA H 5.06 . 1 229 . 47 PHE C C 173.6 . 1 230 . 47 PHE CA C 58.1 . 1 231 . 47 PHE N N 123.0 . 1 232 . 48 HIS H H 7.83 . 1 233 . 48 HIS HA H 4.56 . 1 234 . 48 HIS C C 171.9 . 1 235 . 48 HIS CA C 55.2 . 1 236 . 48 HIS N N 124.7 . 1 237 . 49 ARG H H 6.97 . 1 238 . 49 ARG HA H 4.72 . 1 239 . 49 ARG C C 172.6 . 1 240 . 49 ARG CA C 53.8 . 1 241 . 49 ARG N N 126.3 . 1 242 . 50 VAL H H 8.82 . 1 243 . 50 VAL HA H 4.82 . 1 244 . 50 VAL C C 171.7 . 1 245 . 50 VAL CA C 58.0 . 1 246 . 50 VAL N N 125.0 . 1 247 . 51 ILE H H 8.23 . 1 248 . 51 ILE HA H 4.86 . 1 249 . 51 ILE C C 171.9 . 1 250 . 51 ILE CA C 55.8 . 1 251 . 51 ILE N N 125.6 . 1 252 . 52 PRO HA H 4.06 . 1 253 . 52 PRO C C 176.5 . 1 254 . 52 PRO CA C 61.7 . 1 255 . 53 GLY H H 9.29 . 1 256 . 53 GLY HA2 H 3.66 . 2 257 . 53 GLY HA3 H 3.96 . 2 258 . 53 GLY C C 171.8 . 1 259 . 53 GLY CA C 43.7 . 1 260 . 53 GLY N N 112.6 . 1 261 . 54 PHE H H 7.78 . 1 262 . 54 PHE HA H 5.29 . 1 263 . 54 PHE C C 173.1 . 1 264 . 54 PHE CA C 55.4 . 1 265 . 54 PHE N N 119.9 . 1 266 . 55 MET H H 8.21 . 1 267 . 55 MET HA H 5.16 . 1 268 . 55 MET C C 171.4 . 1 269 . 55 MET CA C 53.3 . 1 270 . 55 MET N N 119.9 . 1 271 . 56 ILE H H 7.92 . 1 272 . 56 ILE HA H 4.87 . 1 273 . 56 ILE C C 171.4 . 1 274 . 56 ILE CA C 58.1 . 1 275 . 56 ILE N N 113.1 . 1 276 . 57 GLN H H 9.12 . 1 277 . 57 GLN HA H 5.43 . 1 278 . 57 GLN C C 173.2 . 1 279 . 57 GLN CA C 52.0 . 1 280 . 57 GLN N N 130.0 . 1 281 . 58 GLY H H 8.29 . 2 282 . 58 GLY HA2 H 3.03 . 2 283 . 58 GLY HA3 H 5.21 . 1 284 . 58 GLY C C 171.4 . 1 285 . 58 GLY CA C 44.3 . 1 286 . 58 GLY N N 113.9 . 1 287 . 59 GLY H H 7.47 . 1 288 . 59 GLY C C 172.3 . 1 289 . 59 GLY CA C 45.1 . 1 290 . 59 GLY N N 106.0 . 1 291 . 60 GLY H H 9.82 . 1 292 . 60 GLY HA2 H 3.21 . 2 293 . 60 GLY HA3 H 4.61 . 2 294 . 60 GLY C C 169.9 . 1 295 . 60 GLY CA C 44.1 . 1 296 . 60 GLY N N 109.0 . 1 297 . 61 PHE H H 9.68 . 1 298 . 61 PHE HA H 5.22 . 1 299 . 61 PHE C C 175.5 . 1 300 . 61 PHE CA C 55.4 . 1 301 . 61 PHE N N 124.6 . 1 302 . 62 THR H H 8.58 . 1 303 . 62 THR HA H 4.74 . 1 304 . 62 THR C C 175.2 . 1 305 . 62 THR CA C 58.8 . 1 306 . 62 THR N N 113.4 . 1 307 . 63 GLU H H 9.51 . 1 308 . 63 GLU HA H 3.98 . 1 309 . 63 GLU C C 175.6 . 1 310 . 63 GLU CA C 57.7 . 1 311 . 63 GLU N N 122.7 . 1 312 . 64 GLN H H 7.56 . 1 313 . 64 GLN HA H 4.36 . 1 314 . 64 GLN C C 173.3 . 1 315 . 64 GLN CA C 54.0 . 1 316 . 64 GLN N N 120.1 . 1 317 . 65 MET H H 8.35 . 1 318 . 65 MET HA H 4.16 . 1 319 . 65 MET C C 173.8 . 1 320 . 65 MET CA C 54.0 . 1 321 . 65 MET N N 117.9 . 1 322 . 66 GLN H H 7.08 . 1 323 . 66 GLN HA H 4.56 . 1 324 . 66 GLN C C 174.1 . 1 325 . 66 GLN CA C 52.6 . 1 326 . 66 GLN N N 118.9 . 1 327 . 67 GLN H H 8.86 . 1 328 . 67 GLN HA H 3.63 . 1 329 . 67 GLN C C 175.1 . 1 330 . 67 GLN CA C 54.0 . 1 331 . 67 GLN N N 128.9 . 1 332 . 68 LYS H H 7.65 . 1 333 . 68 LYS HA H 4.12 . 1 334 . 68 LYS C C 174.6 . 1 335 . 68 LYS CA C 54.8 . 1 336 . 68 LYS N N 130.2 . 1 337 . 69 LYS H H 8.56 . 1 338 . 69 LYS HA H 4.54 . 1 339 . 69 LYS C C 173.4 . 1 340 . 69 LYS CA C 52.9 . 1 341 . 69 LYS N N 129.6 . 1 342 . 70 PRO HA H 4.81 . 1 343 . 70 PRO C C 174.8 . 1 344 . 70 PRO CA C 60.8 . 1 345 . 71 ASN H H 8.51 . 1 346 . 71 ASN HA H 4.93 . 1 347 . 71 ASN C C 171.3 . 1 348 . 71 ASN CA C 50.8 . 1 349 . 71 ASN N N 121.4 . 1 350 . 73 PRO HA H 5.01 . 1 351 . 73 PRO C C 175.9 . 1 352 . 73 PRO CA C 60.8 . 1 353 . 74 ILE H H 8.19 . 1 354 . 74 ILE HA H 4.56 . 1 355 . 74 ILE C C 173.9 . 1 356 . 74 ILE CA C 57.4 . 1 357 . 74 ILE N N 113.9 . 1 358 . 75 LYS H H 7.84 . 1 359 . 75 LYS HA H 3.86 . 1 360 . 75 LYS C C 174.3 . 1 361 . 75 LYS CA C 54.1 . 1 362 . 75 LYS N N 124.5 . 1 363 . 76 ASN H H 8.49 . 1 364 . 76 ASN HA H 4.41 . 1 365 . 76 ASN C C 175.8 . 1 366 . 76 ASN CA C 51.9 . 1 367 . 76 ASN N N 125.9 . 1 368 . 77 GLU H H 7.96 . 1 369 . 77 GLU HA H 4.67 . 1 370 . 77 GLU C C 173.8 . 1 371 . 77 GLU CA C 54.9 . 1 372 . 77 GLU N N 131.1 . 1 373 . 78 ALA H H 9.36 . 1 374 . 78 ALA HA H 4.63 . 1 375 . 78 ALA C C 175.4 . 1 376 . 78 ALA CA C 52.7 . 1 377 . 78 ALA N N 123.5 . 1 378 . 79 ASP H H 8.17 . 1 379 . 79 ASP HA H 3.60 . 1 380 . 79 ASP C C 174.3 . 1 381 . 79 ASP CA C 51.3 . 1 382 . 79 ASP N N 117.4 . 1 383 . 80 ASN H H 8.16 . 1 384 . 80 ASN HA H 4.38 . 1 385 . 80 ASN C C 174.9 . 1 386 . 80 ASN CA C 52.0 . 1 387 . 80 ASN N N 121.8 . 1 388 . 81 GLY H H 8.18 . 1 389 . 81 GLY HA2 H 3.59 . 2 390 . 81 GLY HA3 H 4.23 . 2 391 . 81 GLY C C 173.6 . 1 392 . 81 GLY CA C 43.8 . 1 393 . 81 GLY N N 111.8 . 1 394 . 82 LEU H H 7.89 . 1 395 . 82 LEU HA H 4.49 . 1 396 . 82 LEU C C 175.6 . 1 397 . 82 LEU CA C 53.0 . 1 398 . 82 LEU N N 124.2 . 1 399 . 83 ARG H H 8.08 . 1 400 . 83 ARG HA H 4.70 . 1 401 . 83 ARG C C 175.4 . 1 402 . 83 ARG CA C 53.7 . 1 403 . 83 ARG N N 125.2 . 1 404 . 84 ASN H H 11.26 . 1 405 . 84 ASN HA H 4.68 . 1 406 . 84 ASN C C 175.4 . 1 407 . 84 ASN CA C 52.8 . 1 408 . 84 ASN N N 129.8 . 1 409 . 85 THR H H 8.27 . 1 410 . 85 THR HA H 4.42 . 1 411 . 85 THR C C 174.3 . 1 412 . 85 THR CA C 59.0 . 1 413 . 85 THR N N 117.0 . 1 414 . 86 ARG H H 9.24 . 1 415 . 86 ARG HA H 3.26 . 1 416 . 86 ARG C C 174.3 . 1 417 . 86 ARG CA C 57.1 . 1 418 . 86 ARG N N 126.2 . 1 419 . 87 GLY H H 9.0 . 1 420 . 87 GLY C C 172.1 . 1 421 . 87 GLY CA C 43.6 . 1 422 . 87 GLY N N 117.9 . 1 423 . 88 THR H H 7.85 . 1 424 . 88 THR HA H 4.71 . 1 425 . 88 THR C C 171.3 . 1 426 . 88 THR CA C 59.5 . 1 427 . 88 THR N N 113.1 . 1 428 . 89 ILE H H 7.20 . 1 429 . 89 ILE HA H 5.11 . 1 430 . 89 ILE C C 169.4 . 1 431 . 89 ILE CA C 55.6 . 1 432 . 89 ILE N N 121.1 . 1 433 . 90 ALA H H 8.54 . 1 434 . 90 ALA HA H 5.49 . 1 435 . 90 ALA C C 176.0 . 1 436 . 90 ALA CA C 48.4 . 1 437 . 90 ALA N N 132.9 . 1 438 . 91 MET H H 8.26 . 1 439 . 91 MET HA H 5.61 . 1 440 . 91 MET C C 176.6 . 1 441 . 91 MET CA C 50.8 . 1 442 . 91 MET N N 118.7 . 1 443 . 92 ALA H H 8.53 . 1 444 . 92 ALA HA H 4.83 . 1 445 . 92 ALA C C 174.6 . 1 446 . 92 ALA CA C 49.7 . 1 447 . 92 ALA N N 129.6 . 1 448 . 93 ARG H H 8.03 . 1 449 . 93 ARG HA H 4.75 . 1 450 . 93 ARG C C 174.6 . 1 451 . 93 ARG CA C 53.5 . 1 452 . 93 ARG N N 115.6 . 1 453 . 94 THR H H 8.12 . 1 454 . 94 THR HA H 4.66 . 1 455 . 94 THR C C 172.3 . 1 456 . 94 THR CA C 59.2 . 1 457 . 94 THR N N 114.8 . 1 458 . 95 ALA H H 8.00 . 1 459 . 95 ALA HA H 4.01 . 1 460 . 95 ALA C C 177.5 . 1 461 . 95 ALA CA C 53.9 . 1 462 . 95 ALA N N 123.8 . 1 463 . 96 ASP H H 8.23 . 1 464 . 96 ASP HA H 4.56 . 1 465 . 96 ASP C C 176.7 . 1 466 . 96 ASP CA C 52.4 . 1 467 . 96 ASP N N 119.6 . 1 468 . 97 LYS HA H 3.78 . 1 469 . 97 LYS C C 176.1 . 1 470 . 97 LYS CA C 58.4 . 1 471 . 98 ASP H H 8.57 . 1 472 . 98 ASP HA H 5.04 . 1 473 . 98 ASP C C 173.2 . 1 474 . 98 ASP CA C 53.1 . 1 475 . 98 ASP N N 126.0 . 1 476 . 99 SER H H 6.75 . 1 477 . 99 SER HA H 4.49 . 1 478 . 99 SER C C 174.6 . 1 479 . 99 SER CA C 56.7 . 1 480 . 99 SER N N 111.2 . 1 481 . 100 ALA H H 8.88 . 1 482 . 100 ALA HA H 4.41 . 1 483 . 100 ALA C C 175.0 . 1 484 . 100 ALA CA C 52.7 . 1 485 . 100 ALA N N 133.0 . 1 486 . 101 THR H H 9.17 . 1 487 . 101 THR HA H 4.89 . 1 488 . 101 THR C C 171.6 . 1 489 . 101 THR CA C 57.7 . 1 490 . 101 THR N N 113.9 . 1 491 . 102 SER H H 8.80 . 1 492 . 102 SER HA H 4.37 . 1 493 . 102 SER C C 175.0 . 1 494 . 102 SER CA C 56.1 . 1 495 . 102 SER N N 116.5 . 1 496 . 103 GLN H H 8.21 . 1 497 . 103 GLN HA H 4.88 . 1 498 . 103 GLN C C 173.0 . 1 499 . 103 GLN CA C 55.7 . 1 500 . 103 GLN N N 125.7 . 1 501 . 104 PHE H H 7.99 . 1 502 . 104 PHE HA H 6.04 . 1 503 . 104 PHE C C 171.4 . 1 504 . 104 PHE CA C 52.6 . 1 505 . 104 PHE N N 121.4 . 1 506 . 105 PHE H H 9.77 . 1 507 . 105 PHE HA H 5.93 . 1 508 . 105 PHE C C 171.4 . 1 509 . 105 PHE CA C 53.6 . 1 510 . 105 PHE N N 119.4 . 1 511 . 106 ILE H H 9.03 . 1 512 . 106 ILE HA H 4.87 . 1 513 . 106 ILE C C 175.5 . 1 514 . 106 ILE CA C 57.2 . 1 515 . 106 ILE N N 121.7 . 1 516 . 107 ASN H H 8.74 . 1 517 . 107 ASN HA H 4.63 . 1 518 . 107 ASN C C 175.3 . 1 519 . 107 ASN CA C 53.6 . 1 520 . 107 ASN N N 129.3 . 1 521 . 108 VAL H H 8.13 . 1 522 . 108 VAL HA H 4.57 . 1 523 . 108 VAL C C 171.9 . 1 524 . 108 VAL CA C 59.1 . 1 525 . 108 VAL N N 121.1 . 1 526 . 109 ALA H H 7.75 . 1 527 . 109 ALA HA H 4.49 . 1 528 . 109 ALA C C 171.7 . 1 529 . 109 ALA CA C 48.8 . 1 530 . 109 ALA N N 129.4 . 1 531 . 110 ASP H H 8.31 . 1 532 . 110 ASP HA H 4.61 . 1 533 . 110 ASP C C 173.4 . 1 534 . 110 ASP CA C 52.8 . 1 535 . 110 ASP N N 120.0 . 1 536 . 111 ASN H H 8.29 . 1 537 . 111 ASN HA H 4.93 . 1 538 . 111 ASN C C 173.3 . 1 539 . 111 ASN CA C 49.6 . 1 540 . 111 ASN N N 132.7 . 1 541 . 112 ALA H H 7.96 . 1 542 . 112 ALA HA H 4.21 . 1 543 . 112 ALA C C 177.5 . 1 544 . 112 ALA CA C 53.1 . 1 545 . 112 ALA N N 127.9 . 1 546 . 113 PHE H H 7.16 . 1 547 . 113 PHE HA H 4.49 . 1 548 . 113 PHE C C 174.6 . 1 549 . 113 PHE CA C 55.4 . 1 550 . 113 PHE N N 115.0 . 1 551 . 114 LEU H H 7.27 . 1 552 . 114 LEU HA H 4.61 . 1 553 . 114 LEU C C 174.3 . 1 554 . 114 LEU CA C 52.9 . 1 555 . 114 LEU N N 124.2 . 1 556 . 115 ASP H H 7.38 . 1 557 . 115 ASP HA H 5.04 . 1 558 . 115 ASP C C 176.6 . 1 559 . 115 ASP CA C 53.1 . 1 560 . 115 ASP N N 121.0 . 1 561 . 116 HIS H H 8.65 . 1 562 . 116 HIS HA H 4.01 . 1 563 . 116 HIS C C 174.1 . 1 564 . 116 HIS CA C 55.9 . 1 565 . 116 HIS N N 123.3 . 1 566 . 117 GLY H H 7.52 . 1 567 . 117 GLY HA2 H 3.61 . 2 568 . 117 GLY HA3 H 4.21 . 2 569 . 117 GLY CA C 43.4 . 1 570 . 117 GLY N N 117.8 . 1 571 . 118 GLN H H 8.22 . 1 572 . 118 GLN HA H 4.06 . 1 573 . 118 GLN C C 175.7 . 1 574 . 118 GLN CA C 56.2 . 1 575 . 118 GLN N N 122.4 . 1 576 . 119 ARG H H 8.46 . 1 577 . 119 ARG HA H 4.31 . 1 578 . 119 ARG C C 174.3 . 1 579 . 119 ARG CA C 55.5 . 1 580 . 119 ARG N N 120.3 . 1 581 . 120 ASP H H 7.65 . 1 582 . 120 ASP HA H 4.75 . 1 583 . 120 ASP C C 173.4 . 1 584 . 120 ASP CA C 52.1 . 1 585 . 120 ASP N N 121.8 . 1 586 . 121 PHE HA H 4.07 . 1 587 . 121 PHE C C 175.9 . 1 588 . 121 PHE CA C 59.2 . 1 589 . 122 GLY H H 8.65 . 1 590 . 122 GLY HA2 H 3.96 . 1 591 . 122 GLY HA3 H 3.96 . 1 592 . 122 GLY C C 172.5 . 1 593 . 122 GLY CA C 43.0 . 1 594 . 122 GLY N N 105.4 . 1 595 . 123 TYR H H 8.32 . 1 596 . 123 TYR HA H 5.28 . 1 597 . 123 TYR C C 174.1 . 1 598 . 123 TYR CA C 56.0 . 1 599 . 123 TYR N N 123.6 . 1 600 . 124 ALA H H 9.40 . 1 601 . 124 ALA HA H 4.21 . 1 602 . 124 ALA C C 174.0 . 1 603 . 124 ALA CA C 51.3 . 1 604 . 124 ALA N N 130.8 . 1 605 . 125 VAL H H 9.65 . 1 606 . 125 VAL HA H 4.32 . 1 607 . 125 VAL C C 174.7 . 1 608 . 125 VAL CA C 60.6 . 1 609 . 125 VAL N N 132.3 . 1 610 . 126 PHE H H 8.16 . 1 611 . 126 PHE HA H 4.97 . 1 612 . 126 PHE C C 172.0 . 1 613 . 126 PHE CA C 52.9 . 1 614 . 126 PHE N N 119.9 . 1 615 . 127 GLY H H 7.18 . 1 616 . 127 GLY HA2 H 3.85 . 2 617 . 127 GLY HA3 H 4.00 . 2 618 . 127 GLY C C 170.4 . 1 619 . 127 GLY CA C 44.8 . 1 620 . 127 GLY N N 109.3 . 1 621 . 128 LYS H H 8.61 . 1 622 . 128 LYS HA H 5.06 . 1 623 . 128 LYS C C 172.5 . 1 624 . 128 LYS CA C 52.8 . 1 625 . 128 LYS N N 120.8 . 1 626 . 129 VAL H H 9.14 . 1 627 . 129 VAL HA H 4.06 . 1 628 . 129 VAL C C 175.5 . 1 629 . 129 VAL CA C 61.3 . 1 630 . 129 VAL N N 126.9 . 1 631 . 130 VAL H H 8.91 . 1 632 . 130 VAL HA H 4.52 . 1 633 . 130 VAL C C 174.6 . 1 634 . 130 VAL CA C 59.7 . 1 635 . 130 VAL N N 126.3 . 1 636 . 131 LYS H H 7.69 . 1 637 . 131 LYS HA H 4.56 . 1 638 . 131 LYS C C 174.4 . 1 639 . 131 LYS CA C 55.4 . 1 640 . 131 LYS N N 124.9 . 1 641 . 132 GLY H H 8.91 . 1 642 . 132 GLY C C 175.3 . 1 643 . 132 GLY CA C 44.5 . 1 644 . 132 GLY N N 114.9 . 1 645 . 133 MET H H 9.00 . 1 646 . 133 MET HA H 4.61 . 1 647 . 133 MET C C 176.2 . 1 648 . 133 MET CA C 54.8 . 1 649 . 133 MET N N 125.8 . 1 650 . 134 ASP H H 8.96 . 1 651 . 134 ASP HA H 4.39 . 1 652 . 134 ASP C C 177.5 . 1 653 . 134 ASP CA C 54.5 . 1 654 . 134 ASP N N 118.6 . 1 655 . 135 VAL H H 7.30 . 1 656 . 135 VAL HA H 3.44 . 1 657 . 135 VAL C C 176.1 . 1 658 . 135 VAL CA C 64.2 . 1 659 . 135 VAL N N 127.9 . 1 660 . 136 ALA H H 7.64 . 1 661 . 136 ALA HA H 3.68 . 1 662 . 136 ALA C C 177.7 . 1 663 . 136 ALA CA C 53.8 . 1 664 . 136 ALA N N 125.2 . 1 665 . 137 ASP H H 8.49 . 1 666 . 137 ASP HA H 4.33 . 1 667 . 137 ASP C C 178.9 . 1 668 . 137 ASP CA C 55.6 . 1 669 . 137 ASP N N 120.5 . 1 670 . 138 LYS H H 7.91 . 1 671 . 138 LYS HA H 3.88 . 1 672 . 138 LYS C C 178.9 . 1 673 . 138 LYS CA C 58.5 . 1 674 . 138 LYS N N 126.6 . 1 675 . 139 ILE H H 8.60 . 1 676 . 139 ILE HA H 3.48 . 1 677 . 139 ILE C C 175.2 . 1 678 . 139 ILE CA C 64.0 . 1 679 . 139 ILE N N 124.5 . 1 680 . 140 SER H H 7.80 . 1 681 . 140 SER HA H 3.86 . 1 682 . 140 SER C C 171.8 . 1 683 . 140 SER CA C 60.0 . 1 684 . 140 SER N N 115.1 . 1 685 . 141 GLN H H 7.03 . 1 686 . 141 GLN HA H 4.31 . 1 687 . 141 GLN C C 175.2 . 1 688 . 141 GLN CA C 54.0 . 1 689 . 141 GLN N N 120.6 . 1 690 . 142 VAL H H 7.29 . 1 691 . 142 VAL HA H 4.41 . 1 692 . 142 VAL C C 172.2 . 1 693 . 142 VAL CA C 59.3 . 1 694 . 142 VAL N N 120.8 . 1 695 . 143 PRO HA H 4.49 . 1 696 . 143 PRO C C 176.9 . 1 697 . 143 PRO CA C 63.0 . 1 698 . 144 THR H H 8.43 . 1 699 . 144 THR HA H 5.13 . 1 700 . 144 THR C C 172.7 . 1 701 . 144 THR CA C 58.0 . 1 702 . 144 THR N N 115.6 . 1 703 . 145 HIS H H 9.40 . 1 704 . 145 HIS HA H 4.93 . 1 705 . 145 HIS C C 170.6 . 1 706 . 145 HIS CA C 51.6 . 1 707 . 145 HIS N N 118.6 . 1 708 . 146 ASP H H 8.21 . 1 709 . 146 ASP HA H 5.27 . 1 710 . 146 ASP C C 175.1 . 1 711 . 146 ASP CA C 51.8 . 1 712 . 146 ASP N N 121.9 . 1 713 . 147 VAL H H 8.55 . 1 714 . 147 VAL HA H 3.98 . 1 715 . 147 VAL C C 173.7 . 1 716 . 147 VAL CA C 59.7 . 1 717 . 147 VAL N N 125.5 . 1 718 . 148 GLY H H 8.77 . 1 719 . 148 GLY CA C 43.0 . 1 720 . 148 GLY N N 120.7 . 1 721 . 149 PRO HA H 4.36 . 1 722 . 149 PRO C C 174.3 . 1 723 . 149 PRO CA C 61.5 . 1 724 . 150 TYR H H 8.11 . 1 725 . 150 TYR HA H 4.46 . 1 726 . 150 TYR C C 173.3 . 1 727 . 150 TYR CA C 56.2 . 1 728 . 150 TYR N N 126.3 . 1 729 . 151 GLN H H 8.36 . 1 730 . 151 GLN HA H 4.89 . 1 731 . 151 GLN C C 175.0 . 1 732 . 151 GLN CA C 52.5 . 1 733 . 151 GLN N N 123.7 . 1 734 . 152 ASN H H 9.31 . 1 735 . 152 ASN HA H 3.97 . 1 736 . 152 ASN C C 171.3 . 1 737 . 152 ASN CA C 54.2 . 1 738 . 152 ASN N N 117.9 . 1 739 . 153 VAL H H 8.26 . 1 740 . 153 VAL HA H 4.56 . 1 741 . 153 VAL C C 174.9 . 1 742 . 153 VAL CA C 57.5 . 1 743 . 153 VAL N N 122.8 . 1 744 . 154 PRO HA H 4.41 . 1 745 . 154 PRO C C 175.5 . 1 746 . 154 PRO CA C 62.7 . 1 747 . 155 SER H H 8.77 . 1 748 . 155 SER HA H 3.47 . 1 749 . 155 SER C C 172.9 . 1 750 . 155 SER CA C 59.5 . 1 751 . 155 SER N N 125.4 . 1 752 . 156 LYS H H 7.96 . 1 753 . 156 LYS HA H 4.81 . 1 754 . 156 LYS C C 171.9 . 1 755 . 156 LYS CA C 50.9 . 1 756 . 156 LYS N N 126.6 . 1 757 . 157 PRO HA H 4.33 . 1 758 . 157 PRO C C 175.3 . 1 759 . 157 PRO CA C 62.0 . 1 760 . 158 VAL H H 9.61 . 1 761 . 158 VAL HA H 4.02 . 1 762 . 158 VAL C C 173.2 . 1 763 . 158 VAL CA C 60.6 . 1 764 . 158 VAL N N 129.8 . 1 765 . 159 VAL H H 8.29 . 1 766 . 159 VAL HA H 4.16 . 1 767 . 159 VAL C C 175.4 . 1 768 . 159 VAL CA C 60.3 . 1 769 . 159 VAL N N 129.8 . 1 770 . 160 ILE H H 9.47 . 1 771 . 160 ILE HA H 3.89 . 1 772 . 160 ILE C C 172.6 . 1 773 . 160 ILE CA C 60.9 . 1 774 . 160 ILE N N 130.6 . 1 775 . 161 LEU H H 8.84 . 1 776 . 161 LEU HA H 4.03 . 1 777 . 161 LEU C C 177.1 . 1 778 . 161 LEU CA C 55.7 . 1 779 . 161 LEU N N 134.6 . 1 780 . 162 SER H H 7.72 . 1 781 . 162 SER HA H 4.48 . 1 782 . 162 SER C C 170.3 . 1 783 . 162 SER CA C 55.5 . 1 784 . 162 SER N N 110.9 . 1 785 . 163 ALA H H 7.96 . 1 786 . 163 ALA HA H 5.55 . 1 787 . 163 ALA C C 173.7 . 1 788 . 163 ALA CA C 48.6 . 1 789 . 163 ALA N N 128.4 . 1 790 . 164 LYS H H 8.26 . 1 791 . 164 LYS HA H 4.66 . 1 792 . 164 LYS C C 173.3 . 1 793 . 164 LYS CA C 53.2 . 1 794 . 164 LYS N N 121.9 . 1 795 . 165 VAL H H 9.03 . 1 796 . 165 VAL HA H 4.49 . 1 797 . 165 VAL C C 175.1 . 1 798 . 165 VAL CA C 61.1 . 1 799 . 165 VAL N N 128.7 . 1 800 . 166 LEU H H 8.61 . 1 801 . 166 LEU HA H 4.60 . 1 802 . 166 LEU C C 172.9 . 1 803 . 166 LEU CA C 51.2 . 1 804 . 166 LEU N N 133.9 . 1 stop_ save_