data_4407 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR chemical shift assignment of human GAIP (Galpha Interacting Protein): A regulator of G protein signaling ; _BMRB_accession_number 4407 _BMRB_flat_file_name bmr4407.str _Entry_type original _Submission_date 1999-09-15 _Accession_date 1999-09-16 _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 'de Alba' E. . . 2 'De Vries' L. . . 3 Farquhar M. G. . 4 Tjandra N. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 767 "13C chemical shifts" 452 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-11-11 original author . stop_ _Original_release_date 1999-11-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; de Alba, E., De Vries, L., Farquhar, M., and Tjandra, N., "Solution structure of human GAIP (G alpha interacting protein). A regulator of G protein signaling," J. Mol. Biol. 291, 927-939 (1999). ; _Citation_title ; Solution structure of human GAIP (G alpha interacting protein). A regulator of G protein signaling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99384138 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'de Alba' E. . . 2 'De Vries' L. . . 3 Farquhar M. . . 4 Tjandra N. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 291 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 927 _Page_last 939 _Year 1999 _Details . loop_ _Keyword 'dipolar couplings' GAIP 'G protein' NMR RGS stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full 'J. Mol. Biol. 1999. 291,927-939' _Citation_title 'Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10452897 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'de Alba' E . . 2 'De Vries' L . . 3 Farquhar 'M G' G. . 4 Tjandra N . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 291 _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 927 _Page_last 939 _Year 1999 _Details ; The solution structure of the human protein GAIP (Galpha interacting protein), a regulator of G protein signaling, has been determined by NMR techniques. Dipolar couplings of the oriented protein in two different liquid crystal media have been used in the structure calculation. The solution structure of GAIP is compared to the crystal structure of an homologous protein from rat (RGS4) complexed to the alpha-subunit of a G protein. Some of RGS4 residues involved in the Galpha-RGS binding interface have similar orientations in GAIP (free form), indicating that upon binding these residues do not suffer conformational rearrangements, and therefore, their role does not seem to be restricted to Galpha interaction but also to RGS folding and stability. We suggest that other structural differences between the two proteins may be related to the process of binding as well as to a distinct efficiency in their respective GTPase activating function. ; save_ ################################## # Molecular system description # ################################## save_system_GAIP _Saveframe_category molecular_system _Mol_system_name 'Gaip protein' _Abbreviation_common GAIP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gaip $GAIP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state unknown _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'Regulator of G protein signaling' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GAIP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Gaip protein' _Abbreviation_common GAIP _Molecular_mass 17321 _Mol_thiol_state . _Details ; A 153 residue protein. Only 128 residues correspong to the native sequence of GAIP, the rest are artifacts from protein engineering ; ############################## # Polymer residue sequence # ############################## _Residue_count 153 _Mol_residue_sequence ; GSPGISGGGGGIPSPEEVQS WAQSFDKLMHSPAGRSVFRA FLRTEYSEENMLFWLACEEL KAEANQHVVDEKARLIYEDY VSILSPKEVSLDSRVREGIN KKMQEPSAHTFDDAQLQIYT LMHRDSYPRFLSSPTYRALL PWVDSSSSLIHRD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 PRO 4 GLY 5 ILE 6 SER 7 GLY 8 GLY 9 GLY 10 GLY 11 GLY 12 ILE 13 PRO 14 SER 15 PRO 16 GLU 17 GLU 18 VAL 19 GLN 20 SER 21 TRP 22 ALA 23 GLN 24 SER 25 PHE 26 ASP 27 LYS 28 LEU 29 MET 30 HIS 31 SER 32 PRO 33 ALA 34 GLY 35 ARG 36 SER 37 VAL 38 PHE 39 ARG 40 ALA 41 PHE 42 LEU 43 ARG 44 THR 45 GLU 46 TYR 47 SER 48 GLU 49 GLU 50 ASN 51 MET 52 LEU 53 PHE 54 TRP 55 LEU 56 ALA 57 CYS 58 GLU 59 GLU 60 LEU 61 LYS 62 ALA 63 GLU 64 ALA 65 ASN 66 GLN 67 HIS 68 VAL 69 VAL 70 ASP 71 GLU 72 LYS 73 ALA 74 ARG 75 LEU 76 ILE 77 TYR 78 GLU 79 ASP 80 TYR 81 VAL 82 SER 83 ILE 84 LEU 85 SER 86 PRO 87 LYS 88 GLU 89 VAL 90 SER 91 LEU 92 ASP 93 SER 94 ARG 95 VAL 96 ARG 97 GLU 98 GLY 99 ILE 100 ASN 101 LYS 102 LYS 103 MET 104 GLN 105 GLU 106 PRO 107 SER 108 ALA 109 HIS 110 THR 111 PHE 112 ASP 113 ASP 114 ALA 115 GLN 116 LEU 117 GLN 118 ILE 119 TYR 120 THR 121 LEU 122 MET 123 HIS 124 ARG 125 ASP 126 SER 127 TYR 128 PRO 129 ARG 130 PHE 131 LEU 132 SER 133 SER 134 PRO 135 THR 136 TYR 137 ARG 138 ALA 139 LEU 140 LEU 141 PRO 142 TRP 143 VAL 144 ASP 145 SER 146 SER 147 SER 148 SER 149 LEU 150 ILE 151 HIS 152 ARG 153 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-11 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 1CMZ "Solution Structure Of Gaip (Galpha Interacting Protein): A Regulator Of G Protein Signaling" 99.35 152 100.00 100.00 2.87e-107 EMBL CAG33711 "RGS19 [Homo sapiens]" 84.97 217 97.69 97.69 1.04e-86 GB AAI23822 "Regulator of G-protein signaling 19 [Bos taurus]" 81.70 223 97.60 98.40 1.97e-82 GB EDL07441 "regulator of G-protein signaling 19, isoform CRA_a [Mus musculus]" 50.33 160 98.70 98.70 3.68e-46 GB EDL07445 "regulator of G-protein signaling 19, isoform CRA_e [Mus musculus]" 50.33 103 98.70 98.70 9.29e-47 GB EPY87810 "regulator of G-protein signaling 19-like protein [Camelus ferus]" 83.66 202 97.66 98.44 1.24e-84 REF NP_001070383 "regulator of G-protein signaling 19 [Bos taurus]" 81.70 223 97.60 98.40 1.97e-82 REF XP_003462829 "PREDICTED: regulator of G-protein signaling 19 isoform X1 [Cavia porcellus]" 83.66 264 98.44 99.22 2.48e-85 REF XP_003787844 "PREDICTED: regulator of G-protein signaling 19 isoform X1 [Otolemur garnettii]" 84.97 217 96.92 97.69 2.97e-85 REF XP_005214874 "PREDICTED: regulator of G-protein signaling 19 isoform X1 [Bos taurus]" 81.70 368 97.60 98.40 2.08e-80 REF XP_006045501 "PREDICTED: regulator of G-protein signaling 19 isoform X1 [Bubalus bubalis]" 81.70 221 97.60 98.40 2.35e-82 SP Q08DC7 "RecName: Full=Regulator of G-protein signaling 19; Short=RGS19" 81.70 223 97.60 98.40 1.97e-82 TPG DAA23284 "TPA: regulator of G-protein signaling 19 [Bos taurus]" 81.70 223 97.60 98.40 1.97e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GAIP human 9606 Eukaryota Metazoa homo sapiens 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 $GAIP 'recombinant technology' 'Escherichia coli' Escherichia coli BL21 DE3 plasmid pGEX-2T 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 $GAIP . mM 0.6 1.0 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_CBCACONH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_CBCANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_HBHACONH_3 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label . save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_C-CNOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name C-CNOESY _Sample_label . save_ save_N-CNOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name N-CNOESY _Sample_label . save_ save_H-HNOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name H-HNOESY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name C-CNOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name N-CNOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name H-HNOESY _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' 5 . mM pH 7.2 0.0 n/a temperature 300 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0.0 external direct cylindrical external_to_the_sample parallel_to_Bo 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_chem_shift _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 gaip _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 . 13 PRO HA H 4.60 . 1 2 . 13 PRO HB2 H 2.22 . 2 3 . 13 PRO HB3 H 1.81 . 2 4 . 13 PRO HG2 H 1.97 . 1 5 . 13 PRO HG3 H 1.97 . 1 6 . 13 PRO HD2 H 3.89 . 1 7 . 13 PRO HD3 H 3.89 . 1 8 . 13 PRO CA C 62.53 . 1 9 . 13 PRO CB C 32.17 . 1 10 . 13 PRO CG C 29.22 . 1 11 . 13 PRO CD C 50.34 . 1 12 . 14 SER HA H 4.65 . 1 13 . 14 SER HB2 H 4.35 . 2 14 . 14 SER HB3 H 4.09 . 2 15 . 14 SER H H 8.67 . 1 16 . 14 SER CA C 56.66 . 1 17 . 14 SER CB C 63.35 . 1 18 . 14 SER N N 118.21 . 1 19 . 15 PRO HA H 4.11 . 1 20 . 15 PRO HB2 H 2.19 . 2 21 . 15 PRO HB3 H 1.86 . 2 22 . 15 PRO HG2 H 2.15 . 2 23 . 15 PRO HG3 H 2.02 . 2 24 . 15 PRO HD2 H 3.89 . 1 25 . 15 PRO HD3 H 3.89 . 1 26 . 15 PRO CA C 65.70 . 1 27 . 15 PRO CB C 31.75 . 1 28 . 15 PRO CG C 27.86 . 1 29 . 15 PRO CD C 50.23 . 1 30 . 16 GLU HA H 3.92 . 1 31 . 16 GLU HB2 H 2.04 . 2 32 . 16 GLU HB3 H 1.92 . 2 33 . 16 GLU HG2 H 2.23 . 2 34 . 16 GLU HG3 H 2.37 . 2 35 . 16 GLU H H 8.59 . 1 36 . 16 GLU CA C 60.12 . 1 37 . 16 GLU CB C 28.87 . 1 38 . 16 GLU CG C 36.90 . 1 39 . 16 GLU N N 116.23 . 1 40 . 17 GLU HA H 3.84 . 1 41 . 17 GLU HB2 H 2.14 . 2 42 . 17 GLU HB3 H 1.95 . 2 43 . 17 GLU HG2 H 2.27 . 1 44 . 17 GLU HG3 H 2.27 . 1 45 . 17 GLU H H 7.77 . 1 46 . 17 GLU CA C 59.20 . 1 47 . 17 GLU CB C 29.37 . 1 48 . 17 GLU CG C 36.36 . 1 49 . 17 GLU N N 122.73 . 1 50 . 18 VAL HA H 4.09 . 1 51 . 18 VAL HB H 1.70 . 1 52 . 18 VAL HG1 H 0.48 . 2 53 . 18 VAL HG2 H 0.52 . 2 54 . 18 VAL H H 7.71 . 1 55 . 18 VAL CA C 65.42 . 1 56 . 18 VAL CB C 31.84 . 1 57 . 18 VAL CG1 C 22.11 . 2 58 . 18 VAL CG2 C 22.87 . 2 59 . 18 VAL N N 118.80 . 1 60 . 19 GLN HA H 3.92 . 1 61 . 19 GLN HB2 H 2.04 . 1 62 . 19 GLN HB3 H 2.04 . 1 63 . 19 GLN HG2 H 2.41 . 2 64 . 19 GLN HG3 H 2.28 . 2 65 . 19 GLN H H 8.24 . 1 66 . 19 GLN HE21 H 7.19 . 2 67 . 19 GLN HE22 H 6.79 . 2 68 . 19 GLN CA C 59.30 . 1 69 . 19 GLN CB C 28.61 . 1 70 . 19 GLN CG C 34.21 . 1 71 . 19 GLN N N 119.54 . 1 72 . 19 GLN NE2 N 110.42 . 1 73 . 20 SER HA H 4.27 . 1 74 . 20 SER HB2 H 4.08 . 2 75 . 20 SER HB3 H 4.02 . 2 76 . 20 SER H H 7.79 . 1 77 . 20 SER CA C 61.90 . 1 78 . 20 SER CB C 63.12 . 1 79 . 20 SER N N 117.74 . 1 80 . 21 TRP HA H 4.76 . 1 81 . 21 TRP HB2 H 3.70 . 2 82 . 21 TRP HB3 H 3.40 . 2 83 . 21 TRP HE1 H 10.24 . 1 84 . 21 TRP HD1 H 6.80 . 1 85 . 21 TRP HZ2 H 7.31 . 1 86 . 21 TRP HE3 H 7.79 . 1 87 . 21 TRP HH2 H 6.92 . 1 88 . 21 TRP H H 7.45 . 1 89 . 21 TRP CA C 56.73 . 1 90 . 21 TRP CB C 29.91 . 1 91 . 21 TRP CD1 C 125.68 . 1 92 . 21 TRP CZ2 C 114.14 . 1 93 . 21 TRP CE3 C 119.84 . 1 94 . 21 TRP CH2 C 123.28 . 1 95 . 21 TRP NE1 N 128.92 . 1 96 . 21 TRP N N 122.21 . 1 97 . 22 ALA HA H 4.40 . 1 98 . 22 ALA HB H 1.60 . 1 99 . 22 ALA H H 7.58 . 1 100 . 22 ALA CA C 52.73 . 1 101 . 22 ALA CB C 18.98 . 1 102 . 22 ALA N N 117.62 . 1 103 . 23 GLN HA H 4.35 . 1 104 . 23 GLN HB2 H 2.25 . 1 105 . 23 GLN HB3 H 2.25 . 1 106 . 23 GLN HG2 H 2.46 . 1 107 . 23 GLN HG3 H 2.46 . 1 108 . 23 GLN H H 7.72 . 1 109 . 23 GLN HE21 H 7.48 . 2 110 . 23 GLN HE22 H 6.83 . 2 111 . 23 GLN CA C 56.91 . 1 112 . 23 GLN CB C 29.61 . 1 113 . 23 GLN CG C 34.05 . 1 114 . 23 GLN N N 116.23 . 1 115 . 23 GLN NE2 N 111.31 . 1 116 . 24 SER HA H 4.67 . 1 117 . 24 SER HB2 H 4.08 . 2 118 . 24 SER HB3 H 3.83 . 2 119 . 24 SER H H 7.28 . 1 120 . 24 SER CA C 57.28 . 1 121 . 24 SER CB C 64.46 . 1 122 . 24 SER N N 110.30 . 1 123 . 25 PHE HA H 3.57 . 1 124 . 25 PHE HB2 H 3.13 . 2 125 . 25 PHE HB3 H 3.05 . 2 126 . 25 PHE HE1 H 6.51 . 1 127 . 25 PHE HE2 H 6.51 . 1 128 . 25 PHE HD1 H 5.91 . 1 129 . 25 PHE HD2 H 5.91 . 1 130 . 25 PHE HZ H 5.70 . 1 131 . 25 PHE H H 8.87 . 1 132 . 25 PHE CA C 59.34 . 1 133 . 25 PHE CB C 39.62 . 1 134 . 25 PHE CD1 C 130.58 . 1 135 . 25 PHE CD2 C 130.58 . 1 136 . 25 PHE CZ C 129.12 . 1 137 . 25 PHE N N 128.01 . 1 138 . 26 ASP HA H 3.96 . 1 139 . 26 ASP HB2 H 2.44 . 1 140 . 26 ASP HB3 H 2.44 . 1 141 . 26 ASP H H 7.87 . 1 142 . 26 ASP CA C 56.93 . 1 143 . 26 ASP CB C 40.63 . 1 144 . 26 ASP N N 114.91 . 1 145 . 27 LYS HA H 3.97 . 1 146 . 27 LYS HB2 H 2.13 . 2 147 . 27 LYS HB3 H 1.87 . 2 148 . 27 LYS HG2 H 1.50 . 1 149 . 27 LYS HG3 H 1.50 . 1 150 . 27 LYS HD2 H 1.78 . 1 151 . 27 LYS HD3 H 1.78 . 1 152 . 27 LYS HE2 H 3.08 . 2 153 . 27 LYS HE3 H 3.04 . 2 154 . 27 LYS H H 7.48 . 1 155 . 27 LYS CA C 58.99 . 1 156 . 27 LYS CB C 32.41 . 1 157 . 27 LYS CG C 25.77 . 1 158 . 27 LYS CD C 28.89 . 1 159 . 27 LYS CE C 42.03 . 1 160 . 27 LYS N N 118.09 . 1 161 . 28 LEU HA H 3.31 . 1 162 . 28 LEU HB2 H 1.62 . 2 163 . 28 LEU HB3 H 1.40 . 2 164 . 28 LEU HG H 0.49 . 1 165 . 28 LEU HD1 H 0.15 . 2 166 . 28 LEU HD2 H -0.01 . 2 167 . 28 LEU H H 6.91 . 1 168 . 28 LEU CA C 58.83 . 1 169 . 28 LEU CB C 41.45 . 1 170 . 28 LEU CG C 24.10 . 1 171 . 28 LEU CD1 C 24.39 . 2 172 . 28 LEU CD2 C 25.71 . 2 173 . 28 LEU N N 119.98 . 1 174 . 29 MET HA H 3.67 . 1 175 . 29 MET HB2 H 1.05 . 1 176 . 29 MET HB3 H 1.05 . 1 177 . 29 MET HE H 0.45 . 1 178 . 29 MET H H 7.36 . 1 179 . 29 MET CA C 54.83 . 1 180 . 29 MET CB C 30.32 . 1 181 . 29 MET CE C 14.55 . 1 182 . 29 MET N N 110.51 . 1 183 . 30 HIS HA H 4.45 . 1 184 . 30 HIS HB2 H 3.35 . 2 185 . 30 HIS HB3 H 2.93 . 2 186 . 30 HIS HD2 H 7.02 . 1 187 . 30 HIS H H 7.43 . 1 188 . 30 HIS CA C 57.00 . 1 189 . 30 HIS CB C 30.30 . 1 190 . 30 HIS CD2 C 120.20 . 1 191 . 30 HIS N N 116.42 . 1 192 . 31 SER HA H 5.12 . 1 193 . 31 SER HB2 H 4.34 . 2 194 . 31 SER HB3 H 3.94 . 2 195 . 31 SER H H 7.21 . 1 196 . 31 SER CA C 53.70 . 1 197 . 31 SER CB C 64.74 . 1 198 . 31 SER N N 115.58 . 1 199 . 32 PRO HA H 4.13 . 1 200 . 32 PRO HB2 H 2.41 . 2 201 . 32 PRO HB3 H 2.05 . 2 202 . 32 PRO HG2 H 2.27 . 1 203 . 32 PRO HG3 H 2.27 . 1 204 . 32 PRO HD2 H 4.14 . 1 205 . 32 PRO HD3 H 4.14 . 1 206 . 32 PRO CA C 66.09 . 1 207 . 32 PRO CB C 32.03 . 1 208 . 32 PRO CG C 27.96 . 1 209 . 32 PRO CD C 50.29 . 1 210 . 33 ALA HA H 4.26 . 1 211 . 33 ALA HB H 1.61 . 1 212 . 33 ALA H H 8.16 . 1 213 . 33 ALA CA C 54.93 . 1 214 . 33 ALA CB C 18.94 . 1 215 . 33 ALA N N 120.06 . 1 216 . 34 GLY HA2 H 2.61 . 2 217 . 34 GLY HA3 H 2.03 . 2 218 . 34 GLY H H 8.35 . 1 219 . 34 GLY CA C 46.94 . 1 220 . 34 GLY N N 109.47 . 1 221 . 35 ARG HA H 3.59 . 1 222 . 35 ARG HB2 H 1.97 . 1 223 . 35 ARG HB3 H 1.97 . 1 224 . 35 ARG HG2 H 1.56 . 1 225 . 35 ARG HG3 H 1.56 . 1 226 . 35 ARG HD2 H 2.95 . 1 227 . 35 ARG HD3 H 2.95 . 1 228 . 35 ARG H H 8.72 . 1 229 . 35 ARG CA C 60.81 . 1 230 . 35 ARG CB C 31.57 . 1 231 . 35 ARG CG C 31.22 . 1 232 . 35 ARG N N 119.87 . 1 233 . 36 SER HA H 4.09 . 1 234 . 36 SER HB2 H 4.09 . 1 235 . 36 SER HB3 H 4.09 . 1 236 . 36 SER H H 7.44 . 1 237 . 36 SER CA C 63.00 . 1 238 . 36 SER CB C 63.28 . 1 239 . 36 SER N N 112.86 . 1 240 . 37 VAL HA H 4.00 . 1 241 . 37 VAL HB H 2.17 . 1 242 . 37 VAL HG1 H 1.41 . 2 243 . 37 VAL HG2 H 1.31 . 2 244 . 37 VAL H H 8.02 . 1 245 . 37 VAL CA C 66.13 . 1 246 . 37 VAL CB C 32.01 . 1 247 . 37 VAL CG1 C 22.53 . 2 248 . 37 VAL CG2 C 22.86 . 2 249 . 37 VAL N N 122.91 . 1 250 . 38 PHE HA H 4.02 . 1 251 . 38 PHE HB2 H 2.69 . 2 252 . 38 PHE HB3 H 2.52 . 2 253 . 38 PHE HD1 H 6.46 . 1 254 . 38 PHE HD2 H 6.46 . 1 255 . 38 PHE HE1 H 7.29 . 1 256 . 38 PHE HE2 H 7.29 . 1 257 . 38 PHE H H 8.75 . 1 258 . 38 PHE CA C 59.59 . 1 259 . 38 PHE CB C 39.76 . 1 260 . 38 PHE CD1 C 131.91 . 1 261 . 38 PHE CD2 C 131.91 . 1 262 . 38 PHE CE1 C 131.63 . 1 263 . 38 PHE CE2 C 131.63 . 1 264 . 38 PHE N N 121.47 . 1 265 . 39 ARG HA H 3.59 . 1 266 . 39 ARG HB2 H 2.24 . 2 267 . 39 ARG HB3 H 1.98 . 2 268 . 39 ARG HG2 H 1.98 . 1 269 . 39 ARG HG3 H 1.98 . 1 270 . 39 ARG HD2 H 3.07 . 1 271 . 39 ARG HD3 H 3.07 . 1 272 . 39 ARG H H 8.56 . 1 273 . 39 ARG CA C 60.95 . 1 274 . 39 ARG CB C 30.86 . 1 275 . 39 ARG CG C 29.29 . 1 276 . 39 ARG CD C 43.80 . 1 277 . 39 ARG N N 117.22 . 1 278 . 40 ALA HA H 3.97 . 1 279 . 40 ALA HB H 1.66 . 1 280 . 40 ALA H H 7.56 . 1 281 . 40 ALA CA C 55.68 . 1 282 . 40 ALA CB C 17.47 . 1 283 . 40 ALA N N 120.44 . 1 284 . 41 PHE HA H 4.44 . 1 285 . 41 PHE HB2 H 3.52 . 1 286 . 41 PHE HB3 H 3.52 . 1 287 . 41 PHE HD1 H 6.83 . 1 288 . 41 PHE HD2 H 6.83 . 1 289 . 41 PHE HE1 H 7.22 . 1 290 . 41 PHE HE2 H 7.22 . 1 291 . 41 PHE HZ H 7.15 . 1 292 . 41 PHE H H 8.12 . 1 293 . 41 PHE CA C 61.05 . 1 294 . 41 PHE CB C 39.65 . 1 295 . 41 PHE CD1 C 132.02 . 1 296 . 41 PHE CD2 C 132.02 . 1 297 . 41 PHE CE1 C 131.61 . 1 298 . 41 PHE CE2 C 131.61 . 1 299 . 41 PHE CZ C 131.02 . 1 300 . 41 PHE N N 119.04 . 1 301 . 42 LEU HA H 3.38 . 1 302 . 42 LEU HB2 H 1.65 . 1 303 . 42 LEU HB3 H 1.65 . 1 304 . 42 LEU HG H 1.16 . 1 305 . 42 LEU HD1 H 0.56 . 2 306 . 42 LEU HD2 H 0.44 . 2 307 . 42 LEU H H 8.87 . 1 308 . 42 LEU CA C 57.67 . 1 309 . 42 LEU CB C 40.64 . 1 310 . 42 LEU CG C 25.63 . 1 311 . 42 LEU CD1 C 21.49 . 2 312 . 42 LEU CD2 C 27.39 . 2 313 . 42 LEU N N 122.37 . 1 314 . 43 ARG HA H 3.97 . 1 315 . 43 ARG HB2 H 1.88 . 1 316 . 43 ARG HB3 H 1.88 . 1 317 . 43 ARG HG2 H 1.77 . 2 318 . 43 ARG HG3 H 1.47 . 2 319 . 43 ARG HD2 H 3.27 . 1 320 . 43 ARG HD3 H 3.27 . 1 321 . 43 ARG H H 8.20 . 1 322 . 43 ARG CA C 60.21 . 1 323 . 43 ARG CB C 30.27 . 1 324 . 43 ARG CG C 28.42 . 1 325 . 43 ARG CD C 43.66 . 1 326 . 43 ARG N N 118.15 . 1 327 . 44 THR HA H 4.01 . 1 328 . 44 THR HB H 4.24 . 1 329 . 44 THR HG2 H 1.38 . 1 330 . 44 THR H H 7.47 . 1 331 . 44 THR CA C 64.38 . 1 332 . 44 THR CB C 69.49 . 1 333 . 44 THR CG2 C 21.40 . 1 334 . 44 THR N N 111.11 . 1 335 . 45 GLU HA H 4.29 . 1 336 . 45 GLU HB2 H 2.04 . 2 337 . 45 GLU HB3 H 1.60 . 2 338 . 45 GLU HG2 H 1.64 . 1 339 . 45 GLU HG3 H 1.64 . 1 340 . 45 GLU H H 6.74 . 1 341 . 45 GLU CA C 55.37 . 1 342 . 45 GLU CB C 29.83 . 1 343 . 45 GLU CG C 36.17 . 1 344 . 45 GLU N N 117.43 . 1 345 . 46 TYR HA H 4.32 . 1 346 . 46 TYR HB2 H 3.27 . 2 347 . 46 TYR HB3 H 3.14 . 2 348 . 46 TYR HD1 H 7.06 . 1 349 . 46 TYR HD2 H 7.06 . 1 350 . 46 TYR HE1 H 6.86 . 1 351 . 46 TYR HE2 H 6.86 . 1 352 . 46 TYR H H 7.33 . 1 353 . 46 TYR CA C 59.24 . 1 354 . 46 TYR CB C 35.28 . 1 355 . 46 TYR CD1 C 133.12 . 1 356 . 46 TYR CD2 C 133.12 . 1 357 . 46 TYR CE1 C 117.97 . 1 358 . 46 TYR CE2 C 117.97 . 1 359 . 46 TYR N N 116.51 . 1 360 . 47 SER HA H 5.05 . 1 361 . 47 SER HB2 H 3.81 . 1 362 . 47 SER HB3 H 3.81 . 1 363 . 47 SER H H 8.01 . 1 364 . 47 SER CA C 57.34 . 1 365 . 47 SER CB C 64.65 . 1 366 . 47 SER N N 111.49 . 1 367 . 48 GLU HA H 3.67 . 1 368 . 48 GLU HB2 H 2.09 . 2 369 . 48 GLU HB3 H 1.62 . 2 370 . 48 GLU HG2 H 2.47 . 2 371 . 48 GLU HG3 H 2.33 . 2 372 . 48 GLU H H 8.45 . 1 373 . 48 GLU CA C 58.71 . 1 374 . 48 GLU CB C 30.76 . 1 375 . 48 GLU CG C 36.71 . 1 376 . 48 GLU N N 122.67 . 1 377 . 49 GLU HA H 4.07 . 1 378 . 49 GLU HB2 H 2.14 . 1 379 . 49 GLU HB3 H 2.14 . 1 380 . 49 GLU HG2 H 2.34 . 1 381 . 49 GLU HG3 H 2.34 . 1 382 . 49 GLU H H 9.73 . 1 383 . 49 GLU CA C 60.82 . 1 384 . 49 GLU CB C 28.43 . 1 385 . 49 GLU CG C 37.04 . 1 386 . 49 GLU N N 118.54 . 1 387 . 50 ASN HA H 4.55 . 1 388 . 50 ASN HB2 H 2.82 . 1 389 . 50 ASN HB3 H 2.82 . 1 390 . 50 ASN HD21 H 7.71 . 2 391 . 50 ASN HD22 H 6.89 . 2 392 . 50 ASN H H 7.67 . 1 393 . 50 ASN CA C 56.68 . 1 394 . 50 ASN CB C 38.49 . 1 395 . 50 ASN ND2 N 109.21 . 1 396 . 50 ASN N N 116.60 . 1 397 . 51 MET HA H 4.44 . 1 398 . 51 MET HB2 H 2.10 . 2 399 . 51 MET HB3 H 2.00 . 2 400 . 51 MET HG2 H 2.49 . 1 401 . 51 MET HG3 H 2.49 . 1 402 . 51 MET HE H 2.10 . 1 403 . 51 MET H H 7.06 . 1 404 . 51 MET CA C 56.50 . 1 405 . 51 MET CB C 32.56 . 1 406 . 51 MET CG C 33.60 . 1 407 . 51 MET CE C 18.63 . 1 408 . 51 MET N N 117.51 . 1 409 . 52 LEU HA H 4.01 . 1 410 . 52 LEU HB2 H 2.05 . 2 411 . 52 LEU HB3 H 1.82 . 2 412 . 52 LEU HG H 1.65 . 1 413 . 52 LEU HD1 H 0.77 . 2 414 . 52 LEU HD2 H 0.87 . 2 415 . 52 LEU H H 8.22 . 1 416 . 52 LEU CA C 58.38 . 1 417 . 52 LEU CB C 40.32 . 1 418 . 52 LEU CG C 27.14 . 1 419 . 52 LEU CD1 C 21.36 . 2 420 . 52 LEU CD2 C 25.26 . 2 421 . 52 LEU N N 119.85 . 1 422 . 53 PHE HA H 3.33 . 1 423 . 53 PHE HB2 H 2.91 . 2 424 . 53 PHE HB3 H 2.59 . 2 425 . 53 PHE HD1 H 6.76 . 1 426 . 53 PHE HD2 H 6.76 . 1 427 . 53 PHE HE1 H 6.68 . 1 428 . 53 PHE HE2 H 6.68 . 1 429 . 53 PHE HZ H 6.67 . 1 430 . 53 PHE H H 8.51 . 1 431 . 53 PHE CA C 60.60 . 1 432 . 53 PHE CB C 39.16 . 1 433 . 53 PHE CD1 C 131.65 . 1 434 . 53 PHE CD2 C 131.65 . 1 435 . 53 PHE CE1 C 131.46 . 1 436 . 53 PHE CE2 C 131.46 . 1 437 . 53 PHE CZ C 129.89 . 1 438 . 53 PHE N N 120.18 . 1 439 . 54 TRP HA H 3.45 . 1 440 . 54 TRP HB2 H 3.79 . 2 441 . 54 TRP HB3 H 3.33 . 2 442 . 54 TRP HE1 H 10.64 . 1 443 . 54 TRP HD1 H 7.35 . 1 444 . 54 TRP HZ3 H 6.76 . 1 445 . 54 TRP HH2 H 6.77 . 1 446 . 54 TRP HE3 H 7.30 . 1 447 . 54 TRP HZ2 H 7.17 . 1 448 . 54 TRP H H 8.03 . 1 449 . 54 TRP CA C 65.12 . 1 450 . 54 TRP CB C 29.56 . 1 451 . 54 TRP CD1 C 124.86 . 1 452 . 54 TRP CZ2 C 114.53 . 1 453 . 54 TRP CE3 C 120.18 . 1 454 . 54 TRP CZ3 C 124.82 . 1 455 . 54 TRP CH2 C 121.97 . 1 456 . 54 TRP NE1 N 130.58 . 1 457 . 54 TRP N N 121.57 . 1 458 . 55 LEU HA H 3.65 . 1 459 . 55 LEU HB2 H 1.95 . 2 460 . 55 LEU HB3 H 1.49 . 2 461 . 55 LEU HG H 2.14 . 1 462 . 55 LEU HD1 H 0.90 . 2 463 . 55 LEU HD2 H 1.04 . 2 464 . 55 LEU H H 9.00 . 1 465 . 55 LEU CA C 57.50 . 1 466 . 55 LEU CB C 42.26 . 1 467 . 55 LEU CG C 27.16 . 1 468 . 55 LEU CD1 C 26.15 . 2 469 . 55 LEU CD2 C 23.30 . 2 470 . 55 LEU N N 117.05 . 1 471 . 56 ALA HA H 4.01 . 1 472 . 56 ALA HB H 1.35 . 1 473 . 56 ALA H H 8.02 . 1 474 . 56 ALA CA C 55.14 . 1 475 . 56 ALA CB C 17.75 . 1 476 . 56 ALA N N 123.39 . 1 477 . 57 CYS HA H 3.61 . 1 478 . 57 CYS HB2 H 2.52 . 2 479 . 57 CYS HB3 H 2.03 . 2 480 . 57 CYS H H 7.45 . 1 481 . 57 CYS CA C 63.54 . 1 482 . 57 CYS CB C 25.90 . 1 483 . 57 CYS N N 116.43 . 1 484 . 58 GLU HA H 3.55 . 1 485 . 58 GLU HB2 H 1.55 . 2 486 . 58 GLU HB3 H 1.26 . 2 487 . 58 GLU HG2 H 1.44 . 2 488 . 58 GLU HG3 H 1.06 . 2 489 . 58 GLU H H 7.29 . 1 490 . 58 GLU CA C 58.52 . 1 491 . 58 GLU CB C 29.21 . 1 492 . 58 GLU CG C 34.87 . 1 493 . 58 GLU N N 119.25 . 1 494 . 59 GLU HA H 3.86 . 1 495 . 59 GLU HB2 H 1.99 . 1 496 . 59 GLU HB3 H 1.99 . 1 497 . 59 GLU HG2 H 2.36 . 2 498 . 59 GLU HG3 H 2.09 . 2 499 . 59 GLU H H 7.79 . 1 500 . 59 GLU CA C 59.09 . 1 501 . 59 GLU CB C 29.78 . 1 502 . 59 GLU CG C 36.64 . 1 503 . 59 GLU N N 118.58 . 1 504 . 60 LEU HA H 3.88 . 1 505 . 60 LEU HB2 H 1.98 . 2 506 . 60 LEU HB3 H 1.46 . 2 507 . 60 LEU HG H 1.98 . 1 508 . 60 LEU HD1 H 0.98 . 2 509 . 60 LEU HD2 H 1.09 . 2 510 . 60 LEU H H 7.60 . 1 511 . 60 LEU CA C 57.92 . 1 512 . 60 LEU CB C 42.06 . 1 513 . 60 LEU CG C 29.70 . 1 514 . 60 LEU CD1 C 25.64 . 2 515 . 60 LEU CD2 C 26.41 . 2 516 . 60 LEU N N 120.99 . 1 517 . 61 LYS HA H 3.78 . 1 518 . 61 LYS HB2 H 1.63 . 2 519 . 61 LYS HB3 H 1.52 . 2 520 . 61 LYS HG2 H 1.43 . 2 521 . 61 LYS HG3 H 1.09 . 2 522 . 61 LYS HD2 H 1.44 . 1 523 . 61 LYS HD3 H 1.44 . 1 524 . 61 LYS HE2 H 2.72 . 1 525 . 61 LYS HE3 H 2.72 . 1 526 . 61 LYS H H 7.29 . 1 527 . 61 LYS CA C 58.78 . 1 528 . 61 LYS CB C 32.60 . 1 529 . 61 LYS CG C 25.84 . 1 530 . 61 LYS CD C 29.75 . 1 531 . 61 LYS CE C 41.79 . 1 532 . 61 LYS N N 113.69 . 1 533 . 62 ALA HA H 4.30 . 1 534 . 62 ALA HB H 1.39 . 1 535 . 62 ALA H H 7.09 . 1 536 . 62 ALA CA C 51.77 . 1 537 . 62 ALA CB C 19.27 . 1 538 . 62 ALA N N 119.53 . 1 539 . 63 GLU HA H 4.12 . 1 540 . 63 GLU HB2 H 2.10 . 2 541 . 63 GLU HB3 H 2.01 . 2 542 . 63 GLU HG2 H 2.21 . 1 543 . 63 GLU HG3 H 2.21 . 1 544 . 63 GLU H H 7.75 . 1 545 . 63 GLU CA C 56.86 . 1 546 . 63 GLU CB C 30.04 . 1 547 . 63 GLU CG C 36.67 . 1 548 . 63 GLU N N 122.01 . 1 549 . 64 ALA HA H 4.35 . 1 550 . 64 ALA HB H 1.40 . 1 551 . 64 ALA H H 8.37 . 1 552 . 64 ALA CA C 53.08 . 1 553 . 64 ALA CB C 20.33 . 1 554 . 64 ALA N N 126.12 . 1 555 . 65 ASN HA H 4.89 . 1 556 . 65 ASN HB2 H 3.01 . 2 557 . 65 ASN HB3 H 2.75 . 2 558 . 65 ASN HD21 H 7.80 . 2 559 . 65 ASN HD22 H 7.17 . 2 560 . 65 ASN H H 8.91 . 1 561 . 65 ASN CA C 52.79 . 1 562 . 65 ASN CB C 39.25 . 1 563 . 65 ASN ND2 N 113.18 . 1 564 . 65 ASN N N 117.82 . 1 565 . 66 GLN HA H 3.94 . 1 566 . 66 GLN HB2 H 2.16 . 2 567 . 66 GLN HB3 H 1.97 . 2 568 . 66 GLN HG2 H 2.34 . 1 569 . 66 GLN HG3 H 2.34 . 1 570 . 66 GLN HE21 H 7.78 . 2 571 . 66 GLN HE22 H 6.75 . 2 572 . 66 GLN CA C 58.58 . 1 573 . 66 GLN CB C 28.55 . 1 574 . 66 GLN CG C 33.44 . 1 575 . 66 GLN NE2 N 113.97 . 1 576 . 67 HIS HA H 4.54 . 1 577 . 67 HIS HB2 H 3.23 . 1 578 . 67 HIS HB3 H 3.23 . 1 579 . 67 HIS CA C 58.34 . 1 580 . 67 HIS CB C 29.42 . 1 581 . 68 VAL HA H 4.17 . 1 582 . 68 VAL HB H 2.24 . 1 583 . 68 VAL HG1 H 0.85 . 1 584 . 68 VAL HG2 H 0.85 . 1 585 . 68 VAL H H 7.33 . 1 586 . 68 VAL CA C 63.50 . 1 587 . 68 VAL CB C 31.59 . 1 588 . 68 VAL CG1 C 21.33 . 1 589 . 68 VAL CG2 C 21.33 . 1 590 . 68 VAL N N 118.64 . 1 591 . 69 VAL HA H 3.38 . 1 592 . 69 VAL HB H 2.13 . 1 593 . 69 VAL HG1 H 0.93 . 2 594 . 69 VAL HG2 H 0.72 . 2 595 . 69 VAL H H 7.78 . 1 596 . 69 VAL CA C 66.50 . 1 597 . 69 VAL CB C 31.53 . 1 598 . 69 VAL CG1 C 23.09 . 2 599 . 69 VAL CG2 C 20.86 . 2 600 . 69 VAL N N 121.22 . 1 601 . 70 ASP HA H 4.04 . 1 602 . 70 ASP HB2 H 2.69 . 1 603 . 70 ASP HB3 H 2.69 . 1 604 . 70 ASP H H 8.20 . 1 605 . 70 ASP CA C 58.40 . 1 606 . 70 ASP CB C 40.81 . 1 607 . 70 ASP N N 117.79 . 1 608 . 71 GLU HA H 4.07 . 1 609 . 71 GLU HB2 H 2.10 . 1 610 . 71 GLU HB3 H 2.10 . 1 611 . 71 GLU HG2 H 2.28 . 1 612 . 71 GLU HG3 H 2.28 . 1 613 . 71 GLU H H 7.48 . 1 614 . 71 GLU CA C 59.30 . 1 615 . 71 GLU CB C 30.36 . 1 616 . 71 GLU CG C 36.24 . 1 617 . 71 GLU N N 117.73 . 1 618 . 72 LYS HA H 4.06 . 1 619 . 72 LYS HB2 H 1.89 . 2 620 . 72 LYS HB3 H 1.79 . 2 621 . 72 LYS HG2 H 1.65 . 2 622 . 72 LYS HG3 H 1.45 . 2 623 . 72 LYS HD2 H 1.60 . 1 624 . 72 LYS HD3 H 1.60 . 1 625 . 72 LYS HE2 H 2.86 . 1 626 . 72 LYS HE3 H 2.86 . 1 627 . 72 LYS H H 8.88 . 1 628 . 72 LYS CA C 59.98 . 1 629 . 72 LYS CB C 33.08 . 1 630 . 72 LYS CG C 26.78 . 1 631 . 72 LYS CD C 29.34 . 1 632 . 72 LYS CE C 41.80 . 1 633 . 72 LYS N N 118.93 . 1 634 . 73 ALA HA H 4.29 . 1 635 . 73 ALA HB H 1.62 . 1 636 . 73 ALA H H 9.30 . 1 637 . 73 ALA CA C 55.69 . 1 638 . 73 ALA CB C 18.56 . 1 639 . 73 ALA N N 121.39 . 1 640 . 74 ARG HA H 4.07 . 1 641 . 74 ARG HB2 H 2.00 . 1 642 . 74 ARG HB3 H 2.00 . 1 643 . 74 ARG HG2 H 1.87 . 2 644 . 74 ARG HG3 H 1.65 . 2 645 . 74 ARG HD2 H 3.22 . 1 646 . 74 ARG HD3 H 3.22 . 1 647 . 74 ARG H H 7.70 . 1 648 . 74 ARG CA C 60.18 . 1 649 . 74 ARG CB C 29.53 . 1 650 . 74 ARG CG C 28.33 . 1 651 . 74 ARG CD C 43.09 . 1 652 . 74 ARG N N 116.70 . 1 653 . 75 LEU HA H 4.15 . 1 654 . 75 LEU HB2 H 1.83 . 2 655 . 75 LEU HB3 H 1.69 . 2 656 . 75 LEU HG H 1.79 . 1 657 . 75 LEU HD1 H 0.90 . 2 658 . 75 LEU HD2 H 0.89 . 2 659 . 75 LEU H H 7.76 . 1 660 . 75 LEU CA C 58.30 . 1 661 . 75 LEU CB C 41.75 . 1 662 . 75 LEU CG C 26.78 . 1 663 . 75 LEU CD1 C 25.11 . 2 664 . 75 LEU CD2 C 23.62 . 2 665 . 75 LEU N N 119.75 . 1 666 . 76 ILE HA H 3.80 . 1 667 . 76 ILE HB H 1.67 . 1 668 . 76 ILE HG12 H 2.00 . 2 669 . 76 ILE HG13 H 0.72 . 2 670 . 76 ILE HG2 H 0.21 . 1 671 . 76 ILE HD1 H 0.53 . 1 672 . 76 ILE H H 8.15 . 1 673 . 76 ILE CA C 65.87 . 1 674 . 76 ILE CB C 38.45 . 1 675 . 76 ILE CG1 C 30.04 . 1 676 . 76 ILE CG2 C 17.70 . 1 677 . 76 ILE CD1 C 15.01 . 1 678 . 76 ILE N N 119.45 . 1 679 . 77 TYR HA H 4.06 . 1 680 . 77 TYR HB2 H 3.50 . 1 681 . 77 TYR HB3 H 3.50 . 1 682 . 77 TYR HD1 H 7.14 . 1 683 . 77 TYR HD2 H 7.14 . 1 684 . 77 TYR HE1 H 6.91 . 1 685 . 77 TYR HE2 H 6.91 . 1 686 . 77 TYR H H 8.52 . 1 687 . 77 TYR CA C 62.47 . 1 688 . 77 TYR CB C 39.18 . 1 689 . 77 TYR CD1 C 133.17 . 1 690 . 77 TYR CD2 C 133.17 . 1 691 . 77 TYR CE1 C 118.12 . 1 692 . 77 TYR CE2 C 118.12 . 1 693 . 77 TYR N N 119.51 . 1 694 . 78 GLU HA H 3.90 . 1 695 . 78 GLU HB2 H 2.09 . 1 696 . 78 GLU HB3 H 2.09 . 1 697 . 78 GLU HG2 H 2.62 . 2 698 . 78 GLU HG3 H 2.55 . 2 699 . 78 GLU H H 8.65 . 1 700 . 78 GLU CA C 59.22 . 1 701 . 78 GLU CB C 29.98 . 1 702 . 78 GLU CG C 36.59 . 1 703 . 78 GLU N N 118.09 . 1 704 . 79 ASP HA H 4.45 . 1 705 . 79 ASP HB2 H 2.41 . 2 706 . 79 ASP HB3 H 1.33 . 2 707 . 79 ASP H H 8.27 . 1 708 . 79 ASP CA C 56.54 . 1 709 . 79 ASP CB C 41.37 . 1 710 . 79 ASP N N 116.36 . 1 711 . 80 TYR HA H 4.75 . 1 712 . 80 TYR HB2 H 2.80 . 1 713 . 80 TYR HB3 H 2.80 . 1 714 . 80 TYR HD1 H 7.42 . 1 715 . 80 TYR HD2 H 7.42 . 1 716 . 80 TYR HE1 H 6.84 . 1 717 . 80 TYR HE2 H 6.84 . 1 718 . 80 TYR H H 7.93 . 1 719 . 80 TYR CA C 58.82 . 1 720 . 80 TYR CB C 42.40 . 1 721 . 80 TYR CD1 C 134.49 . 1 722 . 80 TYR CD2 C 134.49 . 1 723 . 80 TYR CE1 C 117.80 . 1 724 . 80 TYR CE2 C 117.80 . 1 725 . 80 TYR N N 112.08 . 1 726 . 81 VAL HA H 3.92 . 1 727 . 81 VAL HB H 1.95 . 1 728 . 81 VAL HG1 H 0.95 . 1 729 . 81 VAL HG2 H 0.95 . 1 730 . 81 VAL H H 7.46 . 1 731 . 81 VAL CA C 63.48 . 1 732 . 81 VAL CB C 32.70 . 1 733 . 81 VAL CG1 C 22.57 . 1 734 . 81 VAL CG2 C 22.57 . 1 735 . 81 VAL N N 116.02 . 1 736 . 82 SER HA H 3.93 . 1 737 . 82 SER HB2 H 3.68 . 2 738 . 82 SER HB3 H 3.52 . 2 739 . 82 SER H H 7.68 . 1 740 . 82 SER CA C 57.85 . 1 741 . 82 SER CB C 63.31 . 1 742 . 82 SER N N 113.42 . 1 743 . 83 ILE HA H 4.05 . 1 744 . 83 ILE HB H 1.89 . 1 745 . 83 ILE HG12 H 1.43 . 2 746 . 83 ILE HG13 H 1.30 . 2 747 . 83 ILE HG2 H 0.93 . 1 748 . 83 ILE HD1 H 0.85 . 1 749 . 83 ILE CA C 62.99 . 1 750 . 83 ILE CB C 38.01 . 1 751 . 83 ILE CG1 C 27.66 . 1 752 . 83 ILE CG2 C 17.08 . 1 753 . 83 ILE CD1 C 13.48 . 1 754 . 84 LEU HA H 4.23 . 1 755 . 84 LEU HB2 H 1.68 . 1 756 . 84 LEU HB3 H 1.68 . 1 757 . 84 LEU HG H 1.55 . 1 758 . 84 LEU HD1 H 0.91 . 2 759 . 84 LEU HD2 H 0.79 . 2 760 . 84 LEU H H 8.23 . 1 761 . 84 LEU CA C 55.28 . 1 762 . 84 LEU CB C 40.82 . 1 763 . 84 LEU CG C 27.09 . 1 764 . 84 LEU CD1 C 25.50 . 2 765 . 84 LEU CD2 C 22.68 . 2 766 . 84 LEU N N 123.46 . 1 767 . 85 SER HA H 4.48 . 1 768 . 85 SER HB2 H 3.85 . 2 769 . 85 SER HB3 H 3.72 . 2 770 . 85 SER H H 7.60 . 1 771 . 85 SER CA C 56.34 . 1 772 . 85 SER CB C 63.11 . 1 773 . 85 SER N N 115.69 . 1 774 . 86 PRO HA H 4.42 . 1 775 . 86 PRO HB2 H 2.29 . 2 776 . 86 PRO HB3 H 1.95 . 2 777 . 86 PRO HG2 H 2.09 . 2 778 . 86 PRO HG3 H 1.96 . 2 779 . 86 PRO HD3 H 4.08 . 2 780 . 86 PRO HD2 H 3.78 . 2 781 . 86 PRO CA C 64.17 . 1 782 . 86 PRO CB C 32.12 . 1 783 . 86 PRO CG C 27.57 . 1 784 . 86 PRO CD C 50.57 . 1 785 . 87 LYS HA H 4.36 . 1 786 . 87 LYS HB2 H 1.69 . 2 787 . 87 LYS HB3 H 1.49 . 2 788 . 87 LYS HG2 H 1.24 . 2 789 . 87 LYS HG3 H 1.11 . 2 790 . 87 LYS HD2 H 1.50 . 2 791 . 87 LYS HD3 H 1.24 . 2 792 . 87 LYS HE2 H 2.85 . 2 793 . 87 LYS HE3 H 2.74 . 2 794 . 87 LYS H H 7.78 . 1 795 . 87 LYS CA C 55.25 . 1 796 . 87 LYS CB C 33.17 . 1 797 . 87 LYS CG C 25.22 . 1 798 . 87 LYS CD C 29.82 . 1 799 . 87 LYS CE C 42.12 . 1 800 . 87 LYS N N 118.88 . 1 801 . 88 GLU HA H 4.13 . 1 802 . 88 GLU HB2 H 1.96 . 2 803 . 88 GLU HB3 H 1.83 . 2 804 . 88 GLU HG2 H 2.08 . 1 805 . 88 GLU HG3 H 2.08 . 1 806 . 88 GLU CA C 56.73 . 1 807 . 88 GLU CB C 30.64 . 1 808 . 88 GLU CG C 35.68 . 1 809 . 89 VAL HA H 4.50 . 1 810 . 89 VAL HB H 1.96 . 1 811 . 89 VAL HG1 H 0.82 . 2 812 . 89 VAL HG2 H 0.47 . 2 813 . 89 VAL H H 8.20 . 1 814 . 89 VAL CA C 59.98 . 1 815 . 89 VAL CB C 33.82 . 1 816 . 89 VAL CG1 C 21.84 . 2 817 . 89 VAL CG2 C 18.75 . 2 818 . 89 VAL N N 120.02 . 1 819 . 90 SER HA H 4.36 . 1 820 . 90 SER HB2 H 3.91 . 2 821 . 90 SER HB3 H 3.71 . 2 822 . 90 SER H H 8.82 . 1 823 . 90 SER CA C 57.93 . 1 824 . 90 SER CB C 62.63 . 1 825 . 90 SER N N 119.77 . 1 826 . 91 LEU HA H 4.77 . 1 827 . 91 LEU HB2 H 1.48 . 1 828 . 91 LEU HB3 H 1.48 . 1 829 . 91 LEU HG H 1.30 . 1 830 . 91 LEU HD1 H 0.86 . 2 831 . 91 LEU HD2 H 0.64 . 2 832 . 91 LEU H H 7.61 . 1 833 . 91 LEU CA C 52.95 . 1 834 . 91 LEU CB C 45.29 . 1 835 . 91 LEU CG C 27.83 . 1 836 . 91 LEU CD1 C 23.99 . 2 837 . 91 LEU CD2 C 26.20 . 2 838 . 91 LEU N N 123.42 . 1 839 . 92 ASP HA H 4.64 . 1 840 . 92 ASP HB2 H 3.02 . 2 841 . 92 ASP HB3 H 2.71 . 2 842 . 92 ASP H H 8.74 . 1 843 . 92 ASP CA C 53.70 . 1 844 . 92 ASP CB C 42.30 . 1 845 . 92 ASP N N 122.80 . 1 846 . 93 SER HA H 4.11 . 1 847 . 93 SER CA C 62.21 . 1 848 . 94 ARG HA H 4.14 . 1 849 . 94 ARG HB2 H 1.97 . 1 850 . 94 ARG HB3 H 1.97 . 1 851 . 94 ARG HD2 H 3.00 . 2 852 . 94 ARG HD3 H 2.70 . 2 853 . 94 ARG H H 8.41 . 1 854 . 94 ARG CA C 59.29 . 1 855 . 94 ARG CB C 29.71 . 1 856 . 94 ARG CD C 42.06 . 1 857 . 94 ARG N N 122.12 . 1 858 . 95 VAL HA H 3.93 . 1 859 . 95 VAL HB H 2.31 . 1 860 . 95 VAL HG1 H 1.04 . 2 861 . 95 VAL HG2 H 1.13 . 2 862 . 95 VAL H H 8.11 . 1 863 . 95 VAL CA C 65.43 . 1 864 . 95 VAL CB C 31.70 . 1 865 . 95 VAL CG1 C 22.05 . 2 866 . 95 VAL CG2 C 23.25 . 2 867 . 95 VAL N N 121.58 . 1 868 . 96 ARG HA H 3.83 . 1 869 . 96 ARG HB2 H 1.96 . 2 870 . 96 ARG HB3 H 1.84 . 2 871 . 96 ARG HG2 H 1.70 . 2 872 . 96 ARG HG3 H 1.53 . 2 873 . 96 ARG HD2 H 3.40 . 2 874 . 96 ARG HD3 H 3.19 . 2 875 . 96 ARG H H 8.23 . 1 876 . 96 ARG CA C 60.99 . 1 877 . 96 ARG CB C 30.30 . 1 878 . 96 ARG CG C 28.82 . 1 879 . 96 ARG CD C 43.32 . 1 880 . 96 ARG N N 120.77 . 1 881 . 97 GLU HA H 4.17 . 1 882 . 97 GLU HB2 H 2.18 . 2 883 . 97 GLU HB3 H 2.10 . 2 884 . 97 GLU HG2 H 2.32 . 2 885 . 97 GLU HG3 H 2.44 . 2 886 . 97 GLU H H 8.33 . 1 887 . 97 GLU CA C 59.31 . 1 888 . 97 GLU CB C 29.53 . 1 889 . 97 GLU CG C 36.15 . 1 890 . 97 GLU N N 118.94 . 1 891 . 98 GLY HA2 H 3.95 . 1 892 . 98 GLY HA3 H 3.95 . 1 893 . 98 GLY H H 7.95 . 1 894 . 98 GLY CA C 47.34 . 1 895 . 98 GLY N N 106.13 . 1 896 . 99 ILE HA H 3.57 . 1 897 . 99 ILE HB H 2.08 . 1 898 . 99 ILE HG12 H 1.95 . 2 899 . 99 ILE HG13 H 1.05 . 2 900 . 99 ILE HG2 H 1.00 . 1 901 . 99 ILE HD1 H 1.09 . 1 902 . 99 ILE H H 7.93 . 1 903 . 99 ILE CA C 65.15 . 1 904 . 99 ILE CB C 38.12 . 1 905 . 99 ILE CG1 C 29.33 . 1 906 . 99 ILE CG2 C 19.52 . 1 907 . 99 ILE CD1 C 15.44 . 1 908 . 99 ILE N N 121.55 . 1 909 . 100 ASN HA H 4.23 . 1 910 . 100 ASN HB2 H 3.06 . 2 911 . 100 ASN HB3 H 2.92 . 2 912 . 100 ASN HD21 H 7.58 . 2 913 . 100 ASN HD22 H 7.01 . 2 914 . 100 ASN H H 8.26 . 1 915 . 100 ASN CA C 56.74 . 1 916 . 100 ASN CB C 38.41 . 1 917 . 100 ASN ND2 N 111.95 . 1 918 . 100 ASN N N 117.91 . 1 919 . 101 LYS HA H 4.13 . 1 920 . 101 LYS HB2 H 1.95 . 1 921 . 101 LYS HB3 H 1.95 . 1 922 . 101 LYS HG2 H 1.59 . 2 923 . 101 LYS HG3 H 1.50 . 2 924 . 101 LYS HD2 H 1.69 . 1 925 . 101 LYS HD3 H 1.69 . 1 926 . 101 LYS HE2 H 3.07 . 1 927 . 101 LYS HE3 H 3.07 . 1 928 . 101 LYS H H 7.60 . 1 929 . 101 LYS CA C 58.77 . 1 930 . 101 LYS CB C 32.61 . 1 931 . 101 LYS CG C 25.05 . 1 932 . 101 LYS CD C 28.77 . 1 933 . 101 LYS CE C 38.25 . 1 934 . 101 LYS N N 117.09 . 1 935 . 102 LYS HA H 4.19 . 1 936 . 102 LYS HB2 H 1.97 . 2 937 . 102 LYS HB3 H 1.71 . 2 938 . 102 LYS HG2 H 1.62 . 2 939 . 102 LYS HG3 H 1.47 . 2 940 . 102 LYS HD2 H 1.69 . 1 941 . 102 LYS HD3 H 1.69 . 1 942 . 102 LYS HE2 H 3.00 . 1 943 . 102 LYS HE3 H 3.00 . 1 944 . 102 LYS H H 7.87 . 1 945 . 102 LYS CA C 58.01 . 1 946 . 102 LYS CB C 33.83 . 1 947 . 102 LYS CG C 26.10 . 1 948 . 102 LYS CD C 29.72 . 1 949 . 102 LYS CE C 42.31 . 1 950 . 102 LYS N N 119.66 . 1 951 . 103 MET HA H 4.31 . 1 952 . 103 MET HB2 H 1.89 . 1 953 . 103 MET HB3 H 1.89 . 1 954 . 103 MET HG2 H 2.41 . 2 955 . 103 MET HG3 H 1.89 . 2 956 . 103 MET HE H 1.76 . 1 957 . 103 MET H H 7.66 . 1 958 . 103 MET CA C 54.49 . 1 959 . 103 MET CB C 29.79 . 1 960 . 103 MET CG C 31.98 . 1 961 . 103 MET CE C 14.61 . 1 962 . 103 MET N N 116.02 . 1 963 . 104 GLN HA H 4.12 . 1 964 . 104 GLN HB2 H 2.11 . 1 965 . 104 GLN HB3 H 2.11 . 1 966 . 104 GLN HG2 H 2.48 . 2 967 . 104 GLN HG3 H 2.40 . 2 968 . 104 GLN HE21 H 7.56 . 2 969 . 104 GLN HE22 H 6.83 . 2 970 . 104 GLN H H 7.50 . 1 971 . 104 GLN CA C 58.11 . 1 972 . 104 GLN CB C 28.80 . 1 973 . 104 GLN CG C 34.27 . 1 974 . 104 GLN NE2 N 111.69 . 1 975 . 104 GLN N N 117.49 . 1 976 . 105 GLU HA H 4.58 . 1 977 . 105 GLU HB2 H 1.95 . 2 978 . 105 GLU HB3 H 1.85 . 2 979 . 105 GLU HG2 H 2.12 . 1 980 . 105 GLU HG3 H 2.12 . 1 981 . 105 GLU H H 7.58 . 1 982 . 105 GLU CA C 53.64 . 1 983 . 105 GLU CB C 30.47 . 1 984 . 105 GLU CG C 36.18 . 1 985 . 105 GLU N N 117.36 . 1 986 . 106 PRO HA H 4.26 . 1 987 . 106 PRO HB2 H 2.14 . 2 988 . 106 PRO HB3 H 1.74 . 2 989 . 106 PRO HG2 H 1.99 . 1 990 . 106 PRO HG3 H 1.99 . 1 991 . 106 PRO HD3 H 3.53 . 2 992 . 106 PRO HD2 H 3.47 . 2 993 . 106 PRO CA C 63.72 . 1 994 . 106 PRO CB C 32.83 . 1 995 . 106 PRO CG C 27.22 . 1 996 . 106 PRO CD C 49.82 . 1 997 . 107 SER HA H 4.76 . 1 998 . 107 SER HB2 H 4.16 . 2 999 . 107 SER HB3 H 3.90 . 2 1000 . 107 SER H H 8.69 . 1 1001 . 107 SER CA C 56.92 . 1 1002 . 107 SER CB C 67.66 . 1 1003 . 107 SER N N 115.46 . 1 1004 . 108 ALA HA H 3.93 . 1 1005 . 108 ALA HB H 1.31 . 1 1006 . 108 ALA H H 8.91 . 1 1007 . 108 ALA CA C 54.09 . 1 1008 . 108 ALA CB C 18.86 . 1 1009 . 108 ALA N N 121.03 . 1 1010 . 109 HIS HA H 4.82 . 1 1011 . 109 HIS HB2 H 2.69 . 1 1012 . 109 HIS HB3 H 2.69 . 1 1013 . 109 HIS H H 7.75 . 1 1014 . 109 HIS CA C 55.40 . 1 1015 . 109 HIS CB C 29.86 . 1 1016 . 109 HIS N N 110.07 . 1 1017 . 110 THR HA H 3.53 . 1 1018 . 110 THR HB H 3.39 . 1 1019 . 110 THR HG2 H 0.40 . 1 1020 . 110 THR H H 7.66 . 1 1021 . 110 THR CA C 67.84 . 1 1022 . 110 THR CB C 70.49 . 1 1023 . 110 THR CG2 C 22.00 . 1 1024 . 110 THR N N 120.14 . 1 1025 . 111 PHE HA H 4.58 . 1 1026 . 111 PHE HB2 H 3.61 . 2 1027 . 111 PHE HB3 H 2.94 . 2 1028 . 111 PHE HD1 H 7.22 . 1 1029 . 111 PHE HD2 H 7.22 . 1 1030 . 111 PHE H H 8.46 . 1 1031 . 111 PHE CA C 57.94 . 1 1032 . 111 PHE CB C 40.36 . 1 1033 . 111 PHE CD1 C 131.68 . 1 1034 . 111 PHE CD2 C 131.68 . 1 1035 . 111 PHE N N 114.01 . 1 1036 . 112 ASP HA H 4.29 . 1 1037 . 112 ASP HB2 H 2.82 . 1 1038 . 112 ASP HB3 H 2.82 . 1 1039 . 112 ASP H H 7.53 . 1 1040 . 112 ASP CA C 58.85 . 1 1041 . 112 ASP CB C 40.01 . 1 1042 . 112 ASP N N 121.23 . 1 1043 . 113 ASP HA H 4.59 . 1 1044 . 113 ASP HB2 H 2.72 . 1 1045 . 113 ASP HB3 H 2.72 . 1 1046 . 113 ASP CA C 57.40 . 1 1047 . 113 ASP CB C 40.10 . 1 1048 . 114 ALA HA H 4.19 . 1 1049 . 114 ALA HB H 1.76 . 1 1050 . 114 ALA H H 8.06 . 1 1051 . 114 ALA CA C 55.07 . 1 1052 . 114 ALA CB C 20.28 . 1 1053 . 114 ALA N N 123.60 . 1 1054 . 115 GLN HA H 3.93 . 1 1055 . 115 GLN HB2 H 2.27 . 2 1056 . 115 GLN HB3 H 2.04 . 2 1057 . 115 GLN HG2 H 2.28 . 1 1058 . 115 GLN HG3 H 2.28 . 1 1059 . 115 GLN H H 9.56 . 1 1060 . 115 GLN CA C 60.51 . 1 1061 . 115 GLN CB C 28.15 . 1 1062 . 115 GLN CG C 28.13 . 1 1063 . 115 GLN N N 118.87 . 1 1064 . 116 LEU HA H 4.46 . 1 1065 . 116 LEU HB2 H 1.97 . 2 1066 . 116 LEU HB3 H 1.83 . 2 1067 . 116 LEU HG H 1.75 . 1 1068 . 116 LEU HD1 H 0.97 . 2 1069 . 116 LEU HD2 H 0.96 . 2 1070 . 116 LEU H H 8.06 . 1 1071 . 116 LEU CA C 58.00 . 1 1072 . 116 LEU CB C 41.67 . 1 1073 . 116 LEU CG C 27.28 . 1 1074 . 116 LEU CD1 C 23.47 . 2 1075 . 116 LEU CD2 C 25.25 . 2 1076 . 116 LEU N N 119.44 . 1 1077 . 117 GLN HA H 4.22 . 1 1078 . 117 GLN HB2 H 2.37 . 1 1079 . 117 GLN HB3 H 2.37 . 1 1080 . 117 GLN HG2 H 2.43 . 2 1081 . 117 GLN HG3 H 2.64 . 2 1082 . 117 GLN HE21 H 7.36 . 2 1083 . 117 GLN HE22 H 6.83 . 2 1084 . 117 GLN H H 8.12 . 1 1085 . 117 GLN CA C 60.18 . 1 1086 . 117 GLN CB C 28.57 . 1 1087 . 117 GLN CG C 34.56 . 1 1088 . 117 GLN NE2 N 109.93 . 1 1089 . 117 GLN N N 121.35 . 1 1090 . 118 ILE HA H 4.21 . 1 1091 . 118 ILE HB H 2.48 . 1 1092 . 118 ILE HG12 H 1.97 . 2 1093 . 118 ILE HG13 H 1.50 . 2 1094 . 118 ILE HG2 H 1.43 . 1 1095 . 118 ILE HD1 H 0.80 . 1 1096 . 118 ILE H H 8.41 . 1 1097 . 118 ILE CA C 61.87 . 1 1098 . 118 ILE CB C 36.57 . 1 1099 . 118 ILE CG1 C 29.06 . 1 1100 . 118 ILE CG2 C 19.79 . 1 1101 . 118 ILE CD1 C 9.71 . 1 1102 . 118 ILE N N 120.68 . 1 1103 . 119 TYR HA H 3.92 . 1 1104 . 119 TYR HB2 H 3.41 . 1 1105 . 119 TYR HB3 H 3.41 . 1 1106 . 119 TYR HD1 H 6.72 . 1 1107 . 119 TYR HD2 H 6.72 . 1 1108 . 119 TYR HE1 H 6.37 . 1 1109 . 119 TYR HE2 H 6.37 . 1 1110 . 119 TYR H H 9.20 . 1 1111 . 119 TYR CA C 63.46 . 1 1112 . 119 TYR CB C 39.43 . 1 1113 . 119 TYR CD1 C 133.27 . 1 1114 . 119 TYR CD2 C 133.27 . 1 1115 . 119 TYR CE1 C 118.12 . 1 1116 . 119 TYR CE2 C 118.12 . 1 1117 . 119 TYR N N 124.17 . 1 1118 . 120 THR HA H 4.04 . 1 1119 . 120 THR HB H 4.50 . 1 1120 . 120 THR HG2 H 1.39 . 1 1121 . 120 THR H H 8.60 . 1 1122 . 120 THR CA C 66.96 . 1 1123 . 120 THR CB C 69.22 . 1 1124 . 120 THR CG2 C 21.42 . 1 1125 . 120 THR N N 113.42 . 1 1126 . 121 LEU HA H 4.14 . 1 1127 . 121 LEU HB2 H 2.06 . 2 1128 . 121 LEU HB3 H 1.88 . 2 1129 . 121 LEU HG H 1.82 . 1 1130 . 121 LEU HD1 H 1.00 . 1 1131 . 121 LEU HD2 H 1.00 . 1 1132 . 121 LEU H H 8.00 . 1 1133 . 121 LEU CA C 58.89 . 1 1134 . 121 LEU CB C 42.42 . 1 1135 . 121 LEU CG C 27.14 . 1 1136 . 121 LEU CD1 C 25.00 . 1 1137 . 121 LEU CD2 C 25.00 . 1 1138 . 121 LEU N N 123.98 . 1 1139 . 122 MET HA H 4.20 . 1 1140 . 122 MET HB2 H 2.55 . 2 1141 . 122 MET HB3 H 1.95 . 2 1142 . 122 MET HG2 H 3.12 . 2 1143 . 122 MET HG3 H 2.53 . 2 1144 . 122 MET HE H 1.88 . 1 1145 . 122 MET H H 8.47 . 1 1146 . 122 MET CA C 60.60 . 1 1147 . 122 MET CB C 35.18 . 1 1148 . 122 MET CG C 32.01 . 1 1149 . 122 MET CE C 16.54 . 1 1150 . 122 MET N N 117.81 . 1 1151 . 123 HIS HA H 2.67 . 1 1152 . 123 HIS HB2 H 3.06 . 2 1153 . 123 HIS HB3 H 2.36 . 2 1154 . 123 HIS H H 8.11 . 1 1155 . 123 HIS CA C 56.96 . 1 1156 . 123 HIS CB C 31.70 . 1 1157 . 123 HIS N N 118.86 . 1 1158 . 124 ARG HA H 3.89 . 1 1159 . 124 ARG HB2 H 1.85 . 1 1160 . 124 ARG HB3 H 1.85 . 1 1161 . 124 ARG HG2 H 1.69 . 2 1162 . 124 ARG HG3 H 1.63 . 2 1163 . 124 ARG HD2 H 3.12 . 1 1164 . 124 ARG HD3 H 3.12 . 1 1165 . 124 ARG H H 8.16 . 1 1166 . 124 ARG CA C 58.30 . 1 1167 . 124 ARG CB C 31.40 . 1 1168 . 124 ARG CG C 26.88 . 1 1169 . 124 ARG CD C 43.53 . 1 1170 . 124 ARG N N 115.08 . 1 1171 . 125 ASP HA H 4.92 . 1 1172 . 125 ASP HB2 H 2.80 . 1 1173 . 125 ASP HB3 H 2.80 . 1 1174 . 125 ASP H H 8.35 . 1 1175 . 125 ASP CA C 56.01 . 1 1176 . 125 ASP CB C 42.50 . 1 1177 . 125 ASP N N 115.15 . 1 1178 . 126 SER HA H 4.65 . 1 1179 . 126 SER HB2 H 4.19 . 1 1180 . 126 SER HB3 H 4.19 . 1 1181 . 126 SER H H 7.46 . 1 1182 . 126 SER CA C 62.26 . 1 1183 . 126 SER CB C 64.29 . 1 1184 . 126 SER N N 113.46 . 1 1185 . 127 TYR HA H 4.53 . 1 1186 . 127 TYR HB2 H 3.45 . 2 1187 . 127 TYR HB3 H 2.63 . 2 1188 . 127 TYR HD1 H 7.42 . 1 1189 . 127 TYR HD2 H 7.42 . 1 1190 . 127 TYR HE1 H 6.84 . 1 1191 . 127 TYR HE2 H 6.84 . 1 1192 . 127 TYR H H 8.70 . 1 1193 . 127 TYR CA C 61.95 . 1 1194 . 127 TYR CB C 35.81 . 1 1195 . 127 TYR CD1 C 134.22 . 1 1196 . 127 TYR CD2 C 134.22 . 1 1197 . 127 TYR CE1 C 117.80 . 1 1198 . 127 TYR CE2 C 117.80 . 1 1199 . 127 TYR N N 122.03 . 1 1200 . 128 PRO HA H 3.83 . 1 1201 . 128 PRO HB2 H 2.21 . 2 1202 . 128 PRO HB3 H 1.75 . 2 1203 . 128 PRO HG2 H 2.02 . 2 1204 . 128 PRO HG3 H 1.95 . 2 1205 . 128 PRO HD2 H 3.33 . 1 1206 . 128 PRO HD3 H 3.33 . 1 1207 . 128 PRO CA C 66.17 . 1 1208 . 128 PRO CB C 30.82 . 1 1209 . 128 PRO CG C 28.94 . 1 1210 . 128 PRO CD C 49.69 . 1 1211 . 129 ARG HA H 4.05 . 1 1212 . 129 ARG HB2 H 2.19 . 1 1213 . 129 ARG HB3 H 2.19 . 1 1214 . 129 ARG HG2 H 1.95 . 2 1215 . 129 ARG HG3 H 1.64 . 2 1216 . 129 ARG HD2 H 3.45 . 1 1217 . 129 ARG HD3 H 3.45 . 1 1218 . 129 ARG H H 6.51 . 1 1219 . 129 ARG CA C 59.38 . 1 1220 . 129 ARG CB C 30.92 . 1 1221 . 129 ARG CG C 29.10 . 1 1222 . 129 ARG CD C 43.31 . 1 1223 . 129 ARG N N 114.41 . 1 1224 . 130 PHE HA H 2.72 . 1 1225 . 130 PHE HB2 H 3.39 . 2 1226 . 130 PHE HB3 H 2.87 . 2 1227 . 130 PHE HD1 H 6.84 . 1 1228 . 130 PHE HD2 H 6.84 . 1 1229 . 130 PHE HE1 H 7.14 . 1 1230 . 130 PHE HE2 H 7.14 . 1 1231 . 130 PHE HZ H 7.29 . 1 1232 . 130 PHE H H 8.41 . 1 1233 . 130 PHE CA C 59.48 . 1 1234 . 130 PHE CB C 38.73 . 1 1235 . 130 PHE CE1 C 130.96 . 1 1236 . 130 PHE CE2 C 130.96 . 1 1237 . 130 PHE CZ C 128.64 . 1 1238 . 130 PHE N N 122.67 . 1 1239 . 131 LEU HA H 3.17 . 1 1240 . 131 LEU HB2 H 1.50 . 2 1241 . 131 LEU HB3 H 1.06 . 2 1242 . 131 LEU HG H 1.06 . 1 1243 . 131 LEU HD1 H 0.39 . 2 1244 . 131 LEU HD2 H -0.01 . 2 1245 . 131 LEU H H 7.37 . 1 1246 . 131 LEU CA C 56.54 . 1 1247 . 131 LEU CB C 41.24 . 1 1248 . 131 LEU CG C 25.60 . 1 1249 . 131 LEU CD1 C 24.77 . 2 1250 . 131 LEU CD2 C 20.21 . 2 1251 . 131 LEU N N 117.20 . 1 1252 . 132 SER HA H 4.52 . 1 1253 . 132 SER HB2 H 3.89 . 1 1254 . 132 SER HB3 H 3.89 . 1 1255 . 132 SER H H 6.95 . 1 1256 . 132 SER CA C 57.83 . 1 1257 . 132 SER CB C 64.36 . 1 1258 . 132 SER N N 110.19 . 1 1259 . 133 SER HA H 4.84 . 1 1260 . 133 SER HB2 H 4.44 . 2 1261 . 133 SER HB3 H 4.24 . 2 1262 . 133 SER H H 7.65 . 1 1263 . 133 SER CA C 57.61 . 1 1264 . 133 SER CB C 64.73 . 1 1265 . 133 SER N N 119.60 . 1 1266 . 134 PRO HA H 4.32 . 1 1267 . 134 PRO HB2 H 2.47 . 2 1268 . 134 PRO HB3 H 2.03 . 2 1269 . 134 PRO HG2 H 2.29 . 2 1270 . 134 PRO HG3 H 2.09 . 2 1271 . 134 PRO HD2 H 4.12 . 1 1272 . 134 PRO HD3 H 4.12 . 1 1273 . 134 PRO CA C 65.01 . 1 1274 . 134 PRO CB C 32.18 . 1 1275 . 134 PRO CG C 28.10 . 1 1276 . 134 PRO CD C 50.92 . 1 1277 . 135 THR HA H 3.89 . 1 1278 . 135 THR HB H 4.27 . 1 1279 . 135 THR HG2 H 1.51 . 1 1280 . 135 THR H H 7.53 . 1 1281 . 135 THR CA C 67.01 . 1 1282 . 135 THR CB C 69.55 . 1 1283 . 135 THR CG2 C 22.39 . 1 1284 . 135 THR N N 112.02 . 1 1285 . 136 TYR HA H 4.11 . 1 1286 . 136 TYR HB2 H 2.40 . 2 1287 . 136 TYR HB3 H 1.58 . 2 1288 . 136 TYR HD1 H 6.91 . 1 1289 . 136 TYR HD2 H 6.91 . 1 1290 . 136 TYR HE1 H 6.88 . 1 1291 . 136 TYR HE2 H 6.88 . 1 1292 . 136 TYR H H 7.15 . 1 1293 . 136 TYR CA C 60.54 . 1 1294 . 136 TYR CB C 39.30 . 1 1295 . 136 TYR CD1 C 132.74 . 1 1296 . 136 TYR CD2 C 132.74 . 1 1297 . 136 TYR CE1 C 117.41 . 1 1298 . 136 TYR CE2 C 117.41 . 1 1299 . 136 TYR N N 118.19 . 1 1300 . 137 ARG HA H 3.49 . 1 1301 . 137 ARG HB2 H 1.80 . 2 1302 . 137 ARG HB3 H 1.69 . 2 1303 . 137 ARG HG2 H 1.77 . 2 1304 . 137 ARG HG3 H 1.58 . 2 1305 . 137 ARG HD2 H 3.04 . 1 1306 . 137 ARG HD3 H 3.04 . 1 1307 . 137 ARG H H 8.14 . 1 1308 . 137 ARG CA C 59.17 . 1 1309 . 137 ARG CB C 29.75 . 1 1310 . 137 ARG CG C 28.23 . 1 1311 . 137 ARG CD C 43.29 . 1 1312 . 137 ARG N N 114.58 . 1 1313 . 138 ALA HA H 4.12 . 1 1314 . 138 ALA HB H 1.44 . 1 1315 . 138 ALA H H 7.87 . 1 1316 . 138 ALA CA C 53.90 . 1 1317 . 138 ALA CB C 18.73 . 1 1318 . 138 ALA N N 118.30 . 1 1319 . 139 LEU HA H 4.15 . 1 1320 . 139 LEU HB2 H 1.73 . 2 1321 . 139 LEU HB3 H 1.48 . 2 1322 . 139 LEU HG H 1.89 . 1 1323 . 139 LEU HD1 H 1.23 . 2 1324 . 139 LEU HD2 H 0.95 . 2 1325 . 139 LEU H H 7.47 . 1 1326 . 139 LEU CA C 54.84 . 1 1327 . 139 LEU CB C 43.02 . 1 1328 . 139 LEU CG C 26.88 . 1 1329 . 139 LEU CD1 C 27.16 . 2 1330 . 139 LEU CD2 C 22.58 . 2 1331 . 139 LEU N N 115.58 . 1 1332 . 140 LEU HA H 4.19 . 1 1333 . 140 LEU HB2 H 1.48 . 2 1334 . 140 LEU HB3 H 1.06 . 2 1335 . 140 LEU HG H 1.18 . 1 1336 . 140 LEU HD1 H 0.66 . 2 1337 . 140 LEU HD2 H 0.52 . 2 1338 . 140 LEU H H 7.00 . 1 1339 . 140 LEU CA C 52.49 . 1 1340 . 140 LEU CB C 41.37 . 1 1341 . 140 LEU CG C 26.22 . 1 1342 . 140 LEU CD1 C 25.40 . 2 1343 . 140 LEU CD2 C 22.83 . 2 1344 . 140 LEU N N 118.63 . 1 stop_ save_