data_4452 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Solution structure of Type II Antifreeze Protein Reveals a New Member of the Lectin Family ; _BMRB_accession_number 4452 _BMRB_flat_file_name bmr4452.str _Entry_type original _Submission_date 1999-11-08 _Accession_date 1999-11-08 _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 Gronwald W. . . 2 Loewen M. C. . 3 Lix B. . . 4 Daugulis A. J. . 5 Sonnichsen F. D. . 6 Davies P. L. . 7 Sykes B. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 558 "15N chemical shifts" 120 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-01-12 original author . stop_ _Original_release_date 2000-01-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Solution Structure of Type II Antifreeze Protein Reveals a New Member of the Lectin Family ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98206886 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gronwald W. . . 2 Loewen M. C. . 3 Lix B. . . 4 Daugulis A. J. . 5 Sonnichsen F. D. . 6 Davies P. L. . 7 Sykes B. D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4712 _Page_last 4721 _Year 1998 _Details . loop_ _Keyword 'recombinant sea raven protein' 'solution backbone fold' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full 'Brunger, A.T., Kuriyan, J. and Karplus, M. (1987) Science, 235, 458-460' _Citation_title 'Crystallographic R Factor Refinement by Molecular Dynamics.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17810339 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brunger . T. . 2 Kuriyan . . . 3 Karplus . . . stop_ _Journal_abbreviation Science _Journal_name_full 'Science (New York, N.Y.)' _Journal_volume 235 _Journal_issue 4787 _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 458 _Page_last 460 _Year 1987 _Details ; Molecular dynamics was used to refine macromolecular structures by incorporating the difference between the observed crystallographic structure factor amplitude and that calculated from an assumed atomic model into the total energy of the system. The method has a radius of convergence that is larger than that of conventional restrained least-squares refinement. Test cases showed that the need for manual corrections during refinement of macromolecular crystal structures is reduced. In crambin, the dynamics calculation moved residues that were misplaced by more than 3 angstroms into the correct positions without human intervention. ; save_ save_ref2 _Saveframe_category citation _Citation_full 'Varian, palo Alto, CA' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref3 _Saveframe_category citation _Citation_full ; Delagio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) J. Biomol. NMR, 6, 277-293 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref4 _Saveframe_category citation _Citation_full ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore G.M. (1991) J. Magn. Reson., 95, 214-220. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref5 _Saveframe_category citation _Citation_full ; Gronwald, W., Loewen, M.C., Lix, B., Daugulis, A.J., Sonnichsen,F.D., Davies, P.L. and Sykes, B.D. (1998) Biochemistry, 37, 4712-4721 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_SRAFP _Saveframe_category molecular_system _Mol_system_name 'sea raven Type II antifreeze protein' _Abbreviation_common SRAFP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SRAFP $SRAFP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disufide bound' loop_ _Biological_function 'antifreeze activity' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SRAFP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'sea raven Type II antifreeze protein' _Abbreviation_common SRAFP _Molecular_mass 13993 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; QRAGPNCPAGWQPLGDRCIY YETTAMTWALAETNCMKLGG HLASIHSQEEHSFIQTLNAG VVWIGGSACLQAGAWTWSDG TPMNFRSWCSTKPDDVLAAC CMQMTAAADQCWDDLPCPAS HKSVCAMTF ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 ARG 3 ALA 4 GLY 5 PRO 6 ASN 7 CYS 8 PRO 9 ALA 10 GLY 11 TRP 12 GLN 13 PRO 14 LEU 15 GLY 16 ASP 17 ARG 18 CYS 19 ILE 20 TYR 21 TYR 22 GLU 23 THR 24 THR 25 ALA 26 MET 27 THR 28 TRP 29 ALA 30 LEU 31 ALA 32 GLU 33 THR 34 ASN 35 CYS 36 MET 37 LYS 38 LEU 39 GLY 40 GLY 41 HIS 42 LEU 43 ALA 44 SER 45 ILE 46 HIS 47 SER 48 GLN 49 GLU 50 GLU 51 HIS 52 SER 53 PHE 54 ILE 55 GLN 56 THR 57 LEU 58 ASN 59 ALA 60 GLY 61 VAL 62 VAL 63 TRP 64 ILE 65 GLY 66 GLY 67 SER 68 ALA 69 CYS 70 LEU 71 GLN 72 ALA 73 GLY 74 ALA 75 TRP 76 THR 77 TRP 78 SER 79 ASP 80 GLY 81 THR 82 PRO 83 MET 84 ASN 85 PHE 86 ARG 87 SER 88 TRP 89 CYS 90 SER 91 THR 92 LYS 93 PRO 94 ASP 95 ASP 96 VAL 97 LEU 98 ALA 99 ALA 100 CYS 101 CYS 102 MET 103 GLN 104 MET 105 THR 106 ALA 107 ALA 108 ALA 109 ASP 110 GLN 111 CYS 112 TRP 113 ASP 114 ASP 115 LEU 116 PRO 117 CYS 118 PRO 119 ALA 120 SER 121 HIS 122 LYS 123 SER 124 VAL 125 CYS 126 ALA 127 MET 128 THR 129 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 2AFP "The Solution Structure Of Type Ii Antifreeze Protein Reveals A New Member Of The Lectin Family" 100.00 129 100.00 100.00 2.09e-89 GB AAA49617 "antifreeze polypeptide (AFP) precursor [Hemitripterus americanus]" 100.00 195 99.22 99.22 1.16e-89 GB AAA49618 "antifreeze protein [Hemitripterus americanus]" 100.00 163 100.00 100.00 2.38e-90 SP P05140 "RecName: Full=Type-2 ice-structuring protein; AltName: Full=Type II antifreeze protein; Short=AFP; Flags: Precursor" 100.00 163 99.22 99.22 4.06e-89 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $SRAFP 'Sea raven' 8094 Eukaryota Metazoa Hemitripterus americanus blood 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 $SRAFP 'recombinant technology' 'Pichia Pastoris' Pichia Pastoris . . 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 $SRAFP . mM 0.5 1.2 [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task 'structure calculation' stop_ _Details . _Citation_label $ref1 save_ save_VNMR _Saveframe_category software _Name VNMR _Version 5.1 loop_ _Task ; Acquisition and processing of NMR spectra ; stop_ _Details . _Citation_label $ref2 save_ save_NMRPIPE _Saveframe_category software _Name NMRPipe _Version . loop_ _Task ; Processing of NMR spectra ; stop_ _Details . _Citation_label $ref3 save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Task 'Analysis of NMR spectra' stop_ _Details . _Citation_label $ref4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D-DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-DQF-COSY _Sample_label $sample_1 save_ save_2D-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _Sample_label $sample_1 save_ save_2D-NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label $sample_1 save_ save_3D-TOCSY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TOCSY-HSQC _Sample_label $sample_1 save_ save_3D-NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NOESY-HSQC _Sample_label $sample_1 save_ save_3D-HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNHA _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TOCSY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details ; spectra were also measured at 25 and 45 deg Celsius. However, the reported assignments were taken from the spectra measured at 35 deg Celsius ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.1 n/a temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 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_afp2.shift.ascii _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name SRAFP _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 GLN N N 122.7130 . 1 2 . 1 GLN H H 8.3840 . 1 3 . 1 GLN HA H 4.2870 . 1 4 . 1 GLN HB3 H 2.0390 . 2 5 . 1 GLN HB2 H 1.8700 . 2 6 . 1 GLN HG3 H 2.3120 . 2 7 . 1 GLN HG2 H 2.0450 . 2 8 . 2 ARG N N 123.0640 . 1 9 . 2 ARG H H 8.2570 . 1 10 . 2 ARG HA H 4.2840 . 1 11 . 2 ARG HB3 H 1.8440 . 2 12 . 2 ARG HB2 H 1.7650 . 2 13 . 2 ARG HG2 H 1.6390 . 1 14 . 2 ARG HG3 H 1.6390 . 1 15 . 3 ALA N N 126.8610 . 1 16 . 3 ALA H H 8.2730 . 1 17 . 3 ALA HA H 4.5730 . 1 18 . 3 ALA HB H 1.3030 . 1 19 . 6 ASN N N 125.2380 . 1 20 . 6 ASN H H 8.2460 . 1 21 . 6 ASN HA H 4.4600 . 1 22 . 6 ASN HB3 H 3.2570 . 2 23 . 6 ASN HB2 H 3.1410 . 2 24 . 7 CYS N N 120.6930 . 1 25 . 7 CYS H H 8.2540 . 1 26 . 7 CYS HA H 4.5910 . 1 27 . 9 ALA N N 123.0580 . 1 28 . 9 ALA H H 8.3520 . 1 29 . 9 ALA HA H 4.2740 . 1 30 . 9 ALA HB H 1.4750 . 1 31 . 10 GLY N N 111.6360 . 1 32 . 10 GLY H H 8.9250 . 1 33 . 10 GLY HA3 H 4.5770 . 2 34 . 10 GLY HA2 H 3.7990 . 2 35 . 11 TRP N N 121.5180 . 1 36 . 11 TRP H H 8.5850 . 1 37 . 11 TRP HA H 5.2330 . 1 38 . 11 TRP HB3 H 3.4240 . 2 39 . 11 TRP HB2 H 3.1620 . 2 40 . 11 TRP HD1 H 7.2820 . 1 41 . 11 TRP HE1 H 10.1160 . 1 42 . 11 TRP HE3 H 7.0000 . 1 43 . 11 TRP HZ2 H 7.0780 . 1 44 . 11 TRP HZ3 H 6.5810 . 1 45 . 11 TRP HH2 H 6.4020 . 1 46 . 12 GLN N N 119.4900 . 1 47 . 12 GLN H H 9.6320 . 1 48 . 12 GLN HA H 5.2330 . 1 49 . 12 GLN HB3 H 2.4270 . 2 50 . 12 GLN HB2 H 2.0180 . 2 51 . 14 LEU N N 122.6080 . 1 52 . 14 LEU H H 8.3880 . 1 53 . 14 LEU HA H 4.0920 . 1 54 . 14 LEU HB2 H 1.4470 . 1 55 . 14 LEU HB3 H 1.4470 . 1 56 . 14 LEU HD1 H 0.8060 . 1 57 . 14 LEU HD2 H 0.8060 . 1 58 . 15 GLY N N 120.4680 . 1 59 . 15 GLY H H 9.1310 . 1 60 . 15 GLY HA3 H 3.9480 . 2 61 . 15 GLY HA2 H 3.6200 . 2 62 . 16 ASP N N 126.6950 . 1 63 . 16 ASP H H 8.6980 . 1 64 . 16 ASP HA H 4.7640 . 1 65 . 16 ASP HB3 H 2.8040 . 2 66 . 16 ASP HB2 H 2.6970 . 2 67 . 17 ARG N N 118.4720 . 1 68 . 17 ARG H H 8.0860 . 1 69 . 17 ARG HA H 5.1210 . 1 70 . 17 ARG HB3 H 1.9750 . 2 71 . 17 ARG HB2 H 1.7630 . 2 72 . 18 CYS N N 115.4440 . 1 73 . 18 CYS H H 8.3460 . 1 74 . 18 CYS HA H 5.6600 . 1 75 . 18 CYS HB3 H 3.1670 . 2 76 . 18 CYS HB2 H 2.8560 . 2 77 . 19 ILE N N 121.5620 . 1 78 . 19 ILE H H 10.2040 . 1 79 . 19 ILE HA H 5.6630 . 1 80 . 19 ILE HB H 2.0720 . 1 81 . 19 ILE HG13 H 0.9350 . 2 82 . 19 ILE HG12 H 0.9840 . 2 83 . 19 ILE HD1 H 0.8500 . 1 84 . 19 ILE HG2 H 0.9190 . 1 85 . 20 TYR N N 126.0990 . 1 86 . 20 TYR H H 8.4090 . 1 87 . 20 TYR HA H 4.4020 . 1 88 . 20 TYR HB3 H 0.8630 . 2 89 . 20 TYR HB2 H 0.3130 . 2 90 . 20 TYR HD1 H 5.9100 . 1 91 . 20 TYR HD2 H 5.9100 . 1 92 . 20 TYR HE1 H 6.5570 . 1 93 . 20 TYR HE2 H 6.5570 . 1 94 . 21 TYR N N 129.2960 . 1 95 . 21 TYR H H 7.8690 . 1 96 . 21 TYR HA H 4.8980 . 1 97 . 21 TYR HB3 H 2.7970 . 2 98 . 21 TYR HB2 H 2.6680 . 2 99 . 21 TYR HD1 H 6.8960 . 1 100 . 21 TYR HD2 H 6.8960 . 1 101 . 21 TYR HE1 H 6.5430 . 1 102 . 21 TYR HE2 H 6.5430 . 1 103 . 22 GLU N N 131.3220 . 1 104 . 22 GLU H H 8.7180 . 1 105 . 22 GLU HA H 4.0230 . 1 106 . 22 GLU HB3 H 2.5420 . 2 107 . 22 GLU HB2 H 1.6600 . 2 108 . 23 THR N N 115.3920 . 1 109 . 23 THR H H 7.4140 . 1 110 . 23 THR HA H 3.7330 . 1 111 . 23 THR HB H 5.6630 . 1 112 . 23 THR HG2 H 0.5710 . 1 113 . 24 THR N N 123.0810 . 1 114 . 24 THR H H 9.3770 . 1 115 . 24 THR HA H 4.1530 . 1 116 . 24 THR HB H 4.0360 . 1 117 . 24 THR HG2 H 1.1370 . 1 118 . 25 ALA N N 131.3200 . 1 119 . 25 ALA H H 8.5990 . 1 120 . 25 ALA HA H 3.8770 . 1 121 . 25 ALA HB H 1.1290 . 1 122 . 26 MET N N 121.0440 . 1 123 . 26 MET H H 8.5430 . 1 124 . 26 MET HA H 4.9650 . 1 125 . 26 MET HB3 H 2.2540 . 2 126 . 26 MET HB2 H 2.1230 . 2 127 . 26 MET HG3 H 2.7000 . 2 128 . 26 MET HG2 H 2.4890 . 2 129 . 27 THR N N 111.7910 . 1 130 . 27 THR H H 7.3800 . 1 131 . 27 THR HA H 5.2670 . 1 132 . 27 THR HB H 5.4600 . 1 133 . 27 THR HG2 H 1.5510 . 1 134 . 28 TRP N N 122.0000 . 1 135 . 28 TRP H H 7.9760 . 1 136 . 28 TRP HA H 4.4090 . 1 137 . 28 TRP HB2 H 2.9940 . 1 138 . 28 TRP HB3 H 2.9940 . 1 139 . 28 TRP HD1 H 6.8700 . 1 140 . 28 TRP HE1 H 10.3630 . 1 141 . 28 TRP HZ2 H 7.0980 . 1 142 . 29 ALA N N 115.9540 . 1 143 . 29 ALA H H 8.9200 . 1 144 . 29 ALA HA H 4.0300 . 1 145 . 29 ALA HB H 1.5450 . 1 146 . 30 LEU N N 119.4980 . 1 147 . 30 LEU H H 7.6870 . 1 148 . 30 LEU HA H 4.1270 . 1 149 . 30 LEU HB3 H 1.8620 . 2 150 . 30 LEU HB2 H 1.5440 . 2 151 . 30 LEU HG H 1.6710 . 1 152 . 30 LEU HD1 H 1.0450 . 2 153 . 30 LEU HD2 H 0.9250 . 2 154 . 31 ALA N N 126.7390 . 1 155 . 31 ALA H H 8.9740 . 1 156 . 31 ALA HA H 4.4810 . 1 157 . 31 ALA HB H 1.5280 . 1 158 . 32 GLU N N 122.6142 . 1 159 . 32 GLU H H 8.3200 . 1 160 . 32 GLU HA H 4.1050 . 1 161 . 32 GLU HG2 H 2.4170 . 1 162 . 32 GLU HG3 H 2.4170 . 1 163 . 33 THR N N 116.9260 . 1 164 . 33 THR H H 8.0610 . 1 165 . 33 THR HA H 3.9500 . 1 166 . 33 THR HB H 4.2930 . 1 167 . 33 THR HG2 H 1.2910 . 1 168 . 34 ASN N N 122.5840 . 1 169 . 34 ASN H H 8.8200 . 1 170 . 34 ASN HA H 4.2870 . 1 171 . 34 ASN HB3 H 3.1050 . 2 172 . 34 ASN HB2 H 2.6390 . 2 173 . 35 CYS N N 114.8860 . 1 174 . 35 CYS H H 8.4980 . 1 175 . 35 CYS HA H 4.3370 . 1 176 . 35 CYS HB3 H 2.7990 . 2 177 . 35 CYS HB2 H 2.5280 . 2 178 . 36 MET N N 122.0740 . 1 179 . 36 MET H H 8.4450 . 1 180 . 36 MET HA H 4.3580 . 1 181 . 36 MET HB2 H 2.0530 . 1 182 . 36 MET HB3 H 2.0530 . 1 183 . 36 MET HG2 H 2.2600 . 1 184 . 36 MET HG3 H 2.2600 . 1 185 . 37 LYS N N 124.6470 . 1 186 . 37 LYS H H 8.4540 . 1 187 . 37 LYS HA H 4.0130 . 1 188 . 37 LYS HB2 H 2.0410 . 1 189 . 37 LYS HB3 H 2.0410 . 1 190 . 37 LYS HG2 H 1.6320 . 1 191 . 37 LYS HG3 H 1.6320 . 1 192 . 38 LEU N N 117.4440 . 1 193 . 38 LEU H H 7.4580 . 1 194 . 38 LEU HA H 4.2390 . 1 195 . 38 LEU HB3 H 1.9020 . 2 196 . 38 LEU HB2 H 1.7670 . 2 197 . 38 LEU HD1 H 0.7130 . 2 198 . 38 LEU HD2 H 0.4550 . 2 199 . 39 GLY N N 104.5940 . 1 200 . 39 GLY H H 7.6090 . 1 201 . 39 GLY HA3 H 4.3200 . 2 202 . 39 GLY HA2 H 3.6800 . 2 203 . 40 GLY N N 109.6210 . 1 204 . 40 GLY H H 8.5700 . 1 205 . 40 GLY HA3 H 4.6390 . 2 206 . 40 GLY HA2 H 3.8510 . 2 207 . 41 HIS N N 119.4840 . 1 208 . 41 HIS H H 8.5350 . 1 209 . 41 HIS HA H 4.6460 . 1 210 . 41 HIS HB3 H 3.6640 . 2 211 . 41 HIS HB2 H 3.1310 . 2 212 . 42 LEU N N 124.6510 . 1 213 . 42 LEU H H 9.4800 . 1 214 . 42 LEU HA H 4.9670 . 1 215 . 42 LEU HB3 H 1.2810 . 2 216 . 42 LEU HB2 H 0.8220 . 2 217 . 42 LEU HG H 1.0350 . 1 218 . 42 LEU HD1 H 0.0030 . 2 219 . 42 LEU HD2 H -0.0110 . 2 220 . 43 ALA N N 123.6070 . 1 221 . 43 ALA H H 9.2680 . 1 222 . 43 ALA HA H 3.8970 . 1 223 . 43 ALA HB H 1.0340 . 1 224 . 44 SER N N 113.3050 . 1 225 . 44 SER H H 6.5640 . 1 226 . 44 SER HA H 2.7580 . 1 227 . 45 ILE HA H 4.3310 . 1 228 . 45 ILE HB H 1.9900 . 1 229 . 45 ILE HG12 H 1.3130 . 1 230 . 45 ILE HG13 H 1.3130 . 1 231 . 45 ILE HD1 H 0.7080 . 1 232 . 46 HIS N N 123.1000 . 1 233 . 46 HIS H H 9.8720 . 1 234 . 46 HIS HA H 4.9690 . 1 235 . 46 HIS HB3 H 3.7410 . 2 236 . 46 HIS HB2 H 2.9960 . 2 237 . 47 SER N N 112.3050 . 1 238 . 47 SER H H 7.0480 . 1 239 . 47 SER HA H 3.9660 . 1 240 . 48 GLN N N 119.5500 . 1 241 . 48 GLN H H 7.5800 . 1 242 . 48 GLN HA H 4.0440 . 1 243 . 48 GLN HB3 H 2.2080 . 2 244 . 48 GLN HG3 H 2.4540 . 2 245 . 48 GLN HG2 H 2.0150 . 2 246 . 48 GLN HB2 H 1.8990 . 2 247 . 49 GLU N N 119.9990 . 1 248 . 49 GLU H H 8.5630 . 1 249 . 49 GLU HA H 4.0450 . 1 250 . 49 GLU HB2 H 1.9270 . 2 251 . 49 GLU HB3 H 2.0580 . 2 252 . 49 GLU HG2 H 2.2800 . 1 253 . 49 GLU HG3 H 2.2800 . 1 254 . 50 GLU N N 122.0200 . 1 255 . 50 GLU H H 8.8920 . 1 256 . 50 GLU HA H 4.6820 . 1 257 . 50 GLU HB2 H 2.0260 . 1 258 . 50 GLU HB3 H 2.0260 . 1 259 . 51 HIS N N 120.0090 . 1 260 . 51 HIS H H 7.5710 . 1 261 . 51 HIS HA H 4.0640 . 1 262 . 51 HIS HB3 H 3.3760 . 2 263 . 51 HIS HB2 H 3.1460 . 2 264 . 51 HIS HD2 H 7.5530 . 1 265 . 52 SER N N 112.8180 . 1 266 . 52 SER H H 9.0400 . 1 267 . 52 SER HA H 4.3090 . 1 268 . 52 SER HB2 H 4.0110 . 1 269 . 52 SER HB3 H 4.0110 . 1 270 . 53 PHE N N 122.1260 . 1 271 . 53 PHE H H 8.0460 . 1 272 . 53 PHE HA H 4.2750 . 1 273 . 53 PHE HB3 H 3.2720 . 2 274 . 53 PHE HB2 H 3.1180 . 2 275 . 53 PHE HD1 H 7.0530 . 1 276 . 53 PHE HD2 H 7.0530 . 1 277 . 53 PHE HE1 H 7.1540 . 1 278 . 53 PHE HE2 H 7.1540 . 1 279 . 54 ILE N N 120.5300 . 1 280 . 54 ILE H H 7.9420 . 1 281 . 54 ILE HA H 3.3760 . 1 282 . 54 ILE HB H 1.8910 . 1 283 . 54 ILE HG13 H 1.7260 . 2 284 . 54 ILE HG12 H 1.3450 . 2 285 . 54 ILE HD1 H 0.7990 . 1 286 . 54 ILE HG2 H 0.7190 . 1 287 . 55 GLN N N 119.4760 . 1 288 . 55 GLN H H 7.8370 . 1 289 . 55 GLN HA H 4.1860 . 1 290 . 55 GLN HB2 H 2.1510 . 1 291 . 55 GLN HB3 H 2.1510 . 1 292 . 55 GLN HG2 H 2.2440 . 1 293 . 55 GLN HG3 H 2.2440 . 1 294 . 55 GLN NE2 N 109.5520 . 1 295 . 55 GLN HE21 H 6.8450 . 2 296 . 55 GLN HE22 H 6.6860 . 2 297 . 56 THR N N 110.2980 . 1 298 . 56 THR H H 7.5730 . 1 299 . 56 THR HA H 4.0620 . 1 300 . 56 THR HB H 4.1670 . 1 301 . 56 THR HG2 H 1.3290 . 1 302 . 57 LEU N N 119.4720 . 1 303 . 57 LEU H H 7.2360 . 1 304 . 57 LEU HA H 3.8580 . 1 305 . 57 LEU HB2 H 1.4460 . 1 306 . 57 LEU HB3 H 1.4460 . 1 307 . 57 LEU HD1 H 0.8340 . 2 308 . 57 LEU HD2 H 0.5360 . 2 309 . 58 ASN N N 114.8770 . 1 310 . 58 ASN H H 7.6980 . 1 311 . 58 ASN HA H 4.3110 . 1 312 . 58 ASN HB3 H 2.9480 . 2 313 . 58 ASN HB2 H 2.5460 . 2 314 . 58 ASN ND2 N 112.2160 . 1 315 . 58 ASN HD21 H 7.3320 . 2 316 . 58 ASN HD22 H 6.6120 . 2 317 . 59 ALA N N 121.5520 . 1 318 . 59 ALA H H 8.7450 . 1 319 . 59 ALA HA H 3.8840 . 1 320 . 59 ALA HB H 0.7720 . 1 321 . 60 GLY N N 107.1170 . 1 322 . 60 GLY H H 7.9790 . 1 323 . 60 GLY HA3 H 3.9210 . 2 324 . 60 GLY HA2 H 3.4510 . 2 325 . 61 VAL N N 121.0470 . 1 326 . 61 VAL H H 7.8230 . 1 327 . 61 VAL HA H 4.0610 . 1 328 . 61 VAL HB H 1.6400 . 1 329 . 61 VAL HG1 H 0.8350 . 2 330 . 61 VAL HG2 H 0.0040 . 2 331 . 62 VAL N N 117.5350 . 1 332 . 62 VAL H H 7.6050 . 1 333 . 62 VAL HA H 4.7300 . 1 334 . 62 VAL HB H 1.8760 . 1 335 . 63 TRP N N 121.5540 . 1 336 . 63 TRP H H 9.3140 . 1 337 . 63 TRP HA H 5.6550 . 1 338 . 63 TRP HB3 H 3.5780 . 2 339 . 63 TRP HB2 H 3.0840 . 2 340 . 63 TRP HD1 H 7.1970 . 1 341 . 63 TRP HE1 H 10.3620 . 1 342 . 63 TRP HE3 H 8.6380 . 1 343 . 63 TRP HZ2 H 8.5980 . 1 344 . 63 TRP HZ3 H 6.9600 . 1 345 . 63 TRP HH2 H 7.3300 . 1 346 . 64 ILE N N 112.8180 . 1 347 . 64 ILE H H 8.1970 . 1 348 . 64 ILE HA H 4.9430 . 1 349 . 64 ILE HD1 H 0.0090 . 1 350 . 64 ILE HG2 H 0.2570 . 1 351 . 65 GLY N N 104.0790 . 1 352 . 65 GLY H H 8.9560 . 1 353 . 65 GLY HA3 H 4.3830 . 2 354 . 65 GLY HA2 H 4.2660 . 2 355 . 66 GLY N N 113.3290 . 1 356 . 66 GLY H H 7.5810 . 1 357 . 66 GLY HA3 H 5.3030 . 2 358 . 66 GLY HA2 H 3.4880 . 2 359 . 67 SER N N 116.2000 . 1 360 . 67 SER H H 8.9360 . 1 361 . 67 SER HA H 5.2950 . 1 362 . 68 ALA N N 126.6980 . 1 363 . 68 ALA H H 7.9630 . 1 364 . 68 ALA HA H 4.3360 . 1 365 . 68 ALA HB H -0.6170 . 1 366 . 69 CYS N N 115.4940 . 1 367 . 69 CYS H H 8.2670 . 1 368 . 69 CYS HA H 4.4680 . 1 369 . 69 CYS HB3 H 3.1870 . 2 370 . 69 CYS HB2 H 2.4650 . 2 371 . 70 LEU N N 121.6350 . 1 372 . 70 LEU H H 7.9670 . 1 373 . 70 LEU HA H 4.4090 . 1 374 . 70 LEU HB2 H 1.5830 . 1 375 . 70 LEU HB3 H 1.5830 . 1 376 . 70 LEU HD1 H 0.8270 . 1 377 . 70 LEU HD2 H 0.8270 . 1 378 . 71 GLN N N 119.0100 . 1 379 . 71 GLN H H 7.7650 . 1 380 . 71 GLN HA H 4.2760 . 1 381 . 71 GLN HB3 H 2.1910 . 2 382 . 71 GLN HB2 H 1.8210 . 2 383 . 72 ALA N N 128.2650 . 1 384 . 72 ALA H H 8.5600 . 1 385 . 72 ALA HA H 3.9970 . 1 386 . 72 ALA HB H 1.2340 . 1 387 . 73 GLY N N 110.2000 . 1 388 . 73 GLY H H 9.0300 . 1 389 . 73 GLY HA2 H 3.7630 . 2 390 . 73 GLY HA3 H 3.9910 . 2 391 . 74 ALA N N 125.6680 . 1 392 . 74 ALA H H 7.4570 . 1 393 . 74 ALA HA H 4.6870 . 1 394 . 74 ALA HB H 1.1880 . 1 395 . 75 TRP N N 123.1000 . 1 396 . 75 TRP H H 7.5820 . 1 397 . 75 TRP HA H 4.3320 . 1 398 . 75 TRP HB3 H 3.1250 . 2 399 . 75 TRP HB2 H 2.8800 . 2 400 . 75 TRP HD1 H 7.3350 . 1 401 . 75 TRP HE1 H 11.2890 . 1 402 . 75 TRP HE3 H 7.0000 . 1 403 . 75 TRP HZ2 H 7.7740 . 1 404 . 75 TRP HZ3 H 6.6260 . 1 405 . 75 TRP HH2 H 6.7570 . 1 406 . 76 THR N N 113.8440 . 1 407 . 76 THR H H 8.9090 . 1 408 . 76 THR HA H 4.6910 . 1 409 . 76 THR HB H 4.3920 . 1 410 . 77 TRP N N 121.0410 . 1 411 . 77 TRP H H 8.9990 . 1 412 . 77 TRP HA H 5.5820 . 1 413 . 77 TRP HB3 H 3.6880 . 2 414 . 77 TRP HB2 H 3.2680 . 2 415 . 77 TRP HD1 H 7.4780 . 1 416 . 77 TRP HE3 H 7.3250 . 1 417 . 77 TRP HZ2 H 7.8890 . 1 418 . 77 TRP HZ3 H 6.9340 . 1 419 . 77 TRP HH2 H 6.3200 . 1 420 . 78 SER N N 123.0850 . 1 421 . 78 SER H H 9.6720 . 1 422 . 78 SER HA H 4.4010 . 1 423 . 79 ASP N N 118.9810 . 1 424 . 79 ASP H H 7.9880 . 1 425 . 79 ASP HA H 3.4900 . 1 426 . 79 ASP HB2 H 3.1660 . 1 427 . 79 ASP HB3 H 3.1660 . 1 428 . 80 GLY N N 107.6780 . 1 429 . 80 GLY H H 8.1920 . 1 430 . 80 GLY HA3 H 4.1820 . 2 431 . 80 GLY HA2 H 4.0760 . 2 432 . 81 THR N N 113.8440 . 1 433 . 81 THR H H 8.1560 . 1 434 . 81 THR HA H 4.6010 . 1 435 . 81 THR HB H 4.6870 . 1 436 . 81 THR HG2 H 1.0900 . 1 437 . 83 MET N N 124.1330 . 1 438 . 83 MET H H 8.8690 . 1 439 . 83 MET HA H 5.5210 . 1 440 . 83 MET HB3 H 2.3630 . 2 441 . 83 MET HB2 H 1.8370 . 2 442 . 83 MET HG3 H 2.6110 . 2 443 . 83 MET HG2 H 2.4790 . 2 444 . 84 ASN N N 122.0370 . 1 445 . 84 ASN H H 9.0690 . 1 446 . 84 ASN HA H 4.8580 . 1 447 . 84 ASN HB3 H 3.2730 . 2 448 . 84 ASN HB2 H 2.8570 . 2 449 . 84 ASN ND2 N 115.1260 . 1 450 . 84 ASN HD21 H 8.0070 . 2 451 . 84 ASN HD22 H 7.5760 . 2 452 . 85 PHE N N 124.1330 . 1 453 . 85 PHE H H 8.8750 . 1 454 . 85 PHE HA H 4.6590 . 1 455 . 85 PHE HB3 H 3.0620 . 2 456 . 85 PHE HB2 H 2.9040 . 2 457 . 85 PHE HE1 H 6.8380 . 1 458 . 85 PHE HE2 H 6.8380 . 1 459 . 86 ARG N N 123.0990 . 1 460 . 86 ARG H H 7.3070 . 1 461 . 86 ARG HA H 4.2290 . 1 462 . 86 ARG HB3 H 1.5080 . 2 463 . 86 ARG HB2 H 1.3400 . 2 464 . 86 ARG HG2 H 1.6320 . 1 465 . 86 ARG HG3 H 1.6320 . 1 466 . 86 ARG HD2 H 3.2200 . 1 467 . 86 ARG HD3 H 3.2200 . 1 468 . 87 SER N N 112.0920 . 1 469 . 87 SER H H 2.9640 . 1 470 . 87 SER HA H 3.6890 . 1 471 . 88 TRP N N 121.1570 . 1 472 . 88 TRP H H 7.0270 . 1 473 . 88 TRP HA H 4.5280 . 1 474 . 88 TRP HB3 H 3.1710 . 2 475 . 88 TRP HB2 H 2.6910 . 2 476 . 88 TRP HD1 H 7.0430 . 1 477 . 88 TRP HE1 H 9.9570 . 1 478 . 88 TRP HE3 H 7.4790 . 1 479 . 88 TRP HH2 H 5.4890 . 1 480 . 89 CYS N N 122.5920 . 1 481 . 89 CYS H H 10.1650 . 1 482 . 89 CYS HB3 H 3.1340 . 2 483 . 89 CYS HB2 H 2.4620 . 2 484 . 90 SER N N 116.8500 . 1 485 . 90 SER H H 8.9120 . 1 486 . 90 SER HA H 4.2930 . 1 487 . 91 THR N N 121.0390 . 1 488 . 91 THR H H 8.3260 . 1 489 . 91 THR HA H 4.4250 . 1 490 . 91 THR HB H 4.5750 . 1 491 . 92 LYS N N 120.6790 . 1 492 . 92 LYS H H 8.1490 . 1 493 . 92 LYS HA H 4.2120 . 1 494 . 92 LYS HB3 H 2.3390 . 2 495 . 92 LYS HB2 H 1.7820 . 2 496 . 94 ASP N N 118.9060 . 1 497 . 94 ASP H H 7.8740 . 1 498 . 94 ASP HA H 4.6850 . 1 499 . 94 ASP HB3 H 2.6280 . 2 500 . 94 ASP HB2 H 2.5050 . 2 501 . 95 ASP N N 119.4950 . 1 502 . 95 ASP H H 8.2100 . 1 503 . 95 ASP HA H 4.8490 . 1 504 . 95 ASP HB3 H 2.9450 . 2 505 . 95 ASP HB2 H 2.7190 . 2 506 . 96 VAL HA H 4.2480 . 1 507 . 96 VAL HB H 2.0680 . 1 508 . 97 LEU N N 128.7530 . 1 509 . 97 LEU H H 8.6270 . 1 510 . 97 LEU HA H 3.8330 . 1 511 . 97 LEU HB3 H 1.5970 . 2 512 . 97 LEU HB2 H 1.5070 . 2 513 . 97 LEU HG H 1.2310 . 1 514 . 97 LEU HD1 H 0.9250 . 2 515 . 97 LEU HD2 H 0.8350 . 2 516 . 98 ALA N N 116.4230 . 1 517 . 98 ALA H H 7.6950 . 1 518 . 98 ALA HA H 4.1550 . 1 519 . 98 ALA HB H 1.3990 . 1 520 . 99 ALA N N 124.1630 . 1 521 . 99 ALA H H 7.6140 . 1 522 . 99 ALA HA H 4.4760 . 1 523 . 99 ALA HB H 1.1660 . 1 524 . 100 CYS N N 112.8070 . 1 525 . 100 CYS H H 7.6640 . 1 526 . 100 CYS HA H 5.2660 . 1 527 . 100 CYS HB3 H 2.7770 . 2 528 . 100 CYS HB2 H 3.1180 . 2 529 . 101 CYS N N 118.4910 . 1 530 . 101 CYS H H 8.3460 . 1 531 . 101 CYS HA H 4.8350 . 1 532 . 101 CYS HB3 H 2.7760 . 2 533 . 101 CYS HB2 H 2.3620 . 2 534 . 102 MET N N 124.1300 . 1 535 . 102 MET H H 8.3030 . 1 536 . 102 MET HA H 4.8510 . 1 537 . 102 MET HG3 H 2.7580 . 2 538 . 102 MET HG2 H 2.6210 . 2 539 . 102 MET HB3 H 2.1460 . 2 540 . 102 MET HB2 H 2.0250 . 2 541 . 103 GLN N N 121.5780 . 1 542 . 103 GLN H H 8.9040 . 1 543 . 103 GLN HA H 5.5630 . 1 544 . 103 GLN HB2 H 1.6040 . 2 545 . 103 GLN HB3 H 1.8740 . 2 546 . 104 MET N N 120.0550 . 1 547 . 104 MET H H 8.6630 . 1 548 . 104 MET HA H 4.4220 . 1 549 . 104 MET HB3 H 1.9140 . 2 550 . 104 MET HB2 H 1.8500 . 2 551 . 104 MET HG3 H 2.4460 . 2 552 . 104 MET HG2 H 2.8410 . 2 553 . 105 THR N N 111.3200 . 1 554 . 105 THR H H 7.6670 . 1 555 . 105 THR HA H 4.2860 . 1 556 . 105 THR HB H 4.5690 . 1 557 . 105 THR HG2 H 1.5810 . 1 558 . 106 ALA N N 118.4270 . 1 559 . 106 ALA H H 8.3310 . 1 560 . 106 ALA HA H 4.5450 . 1 561 . 106 ALA HB H 1.3480 . 1 562 . 107 ALA N N 120.0090 . 1 563 . 107 ALA H H 7.0930 . 1 564 . 107 ALA HA H 4.3530 . 1 565 . 107 ALA HB H 1.6260 . 1 566 . 108 ALA N N 124.5500 . 1 567 . 108 ALA H H 8.8460 . 1 568 . 108 ALA HA H 4.7040 . 1 569 . 108 ALA HB H 1.4430 . 1 570 . 109 ASP N N 112.8200 . 1 571 . 109 ASP H H 7.9250 . 1 572 . 109 ASP HA H 4.5860 . 1 573 . 109 ASP HB3 H 2.9560 . 2 574 . 109 ASP HB2 H 2.4940 . 2 575 . 110 GLN N N 115.4000 . 1 576 . 110 GLN H H 8.2510 . 1 577 . 110 GLN HA H 4.0650 . 1 578 . 110 GLN HB2 H 1.8990 . 1 579 . 110 GLN HB3 H 1.8990 . 1 580 . 110 GLN HG2 H 2.3360 . 1 581 . 110 GLN HG3 H 2.3360 . 1 582 . 111 CYS N N 109.7360 . 1 583 . 111 CYS H H 6.7890 . 1 584 . 111 CYS HA H 4.3450 . 1 585 . 111 CYS HB3 H 3.2150 . 2 586 . 111 CYS HB2 H 3.1390 . 2 587 . 112 TRP N N 121.5550 . 1 588 . 112 TRP H H 8.7990 . 1 589 . 112 TRP HA H 5.9060 . 1 590 . 112 TRP HB3 H 2.5190 . 2 591 . 112 TRP HB2 H 2.4390 . 2 592 . 112 TRP HD1 H 7.4790 . 1 593 . 112 TRP HE1 H 10.5980 . 1 594 . 112 TRP HE3 H 7.4820 . 1 595 . 112 TRP HZ2 H 7.8880 . 1 596 . 112 TRP HZ3 H 5.0620 . 1 597 . 112 TRP HH2 H 6.3770 . 1 598 . 113 ASP N N 119.5050 . 1 599 . 113 ASP H H 9.0080 . 1 600 . 113 ASP HA H 5.1730 . 1 601 . 113 ASP HB3 H 2.6300 . 2 602 . 113 ASP HB2 H 2.4270 . 2 603 . 114 ASP H H 10.6580 . 1 604 . 114 ASP HA H 5.5350 . 1 605 . 114 ASP HB3 H 3.6220 . 2 606 . 114 ASP HB2 H 3.2080 . 2 607 . 115 LEU H H 10.1180 . 1 608 . 115 LEU HA H 5.0780 . 1 609 . 115 LEU HB3 H 2.1100 . 2 610 . 115 LEU HB2 H 1.5720 . 2 611 . 115 LEU HG H 1.8360 . 1 612 . 115 LEU HD1 H 0.9860 . 2 613 . 115 LEU HD2 H 0.7630 . 2 614 . 117 CYS N N 125.2960 . 1 615 . 117 CYS H H 8.8600 . 1 616 . 117 CYS HA H 4.8910 . 1 617 . 119 ALA N N 121.5440 . 1 618 . 119 ALA H H 8.1300 . 1 619 . 119 ALA HA H 4.3200 . 1 620 . 119 ALA HB H 1.7170 . 1 621 . 120 SER N N 114.8610 . 1 622 . 120 SER H H 7.8850 . 1 623 . 120 SER HA H 4.3000 . 1 624 . 120 SER HB3 H 3.5570 . 2 625 . 120 SER HB2 H 3.4350 . 2 626 . 121 HIS N N 122.0700 . 1 627 . 121 HIS H H 8.9360 . 1 628 . 121 HIS HA H 4.9300 . 1 629 . 121 HIS HB3 H 2.9040 . 2 630 . 121 HIS HB2 H 1.6850 . 2 631 . 122 LYS N N 123.6290 . 1 632 . 122 LYS H H 8.7060 . 1 633 . 122 LYS HA H 4.2810 . 1 634 . 122 LYS HB3 H 2.5200 . 2 635 . 122 LYS HB2 H 2.0490 . 2 636 . 122 LYS HG3 H 1.6520 . 2 637 . 122 LYS HG2 H 1.5230 . 2 638 . 122 LYS HD2 H 1.9350 . 1 639 . 122 LYS HD3 H 1.9350 . 1 640 . 123 SER N N 109.7390 . 1 641 . 123 SER H H 8.7290 . 1 642 . 123 SER HA H 5.3890 . 1 643 . 123 SER HB3 H 3.8480 . 2 644 . 123 SER HB2 H 3.7400 . 2 645 . 124 VAL N N 114.6310 . 1 646 . 124 VAL H H 7.1990 . 1 647 . 124 VAL HA H 5.3910 . 1 648 . 124 VAL HB H 1.8420 . 1 649 . 124 VAL HG1 H 0.8240 . 1 650 . 124 VAL HG2 H 0.8240 . 1 651 . 125 CYS N N 123.1000 . 1 652 . 125 CYS H H 9.5990 . 1 653 . 125 CYS HA H 5.6410 . 1 654 . 125 CYS HB3 H 3.0930 . 2 655 . 125 CYS HB2 H 2.4270 . 2 656 . 126 ALA N N 120.4420 . 1 657 . 126 ALA H H 9.5130 . 1 658 . 126 ALA HA H 6.0890 . 1 659 . 126 ALA HB H 1.5110 . 1 660 . 127 MET N N 120.4920 . 1 661 . 127 MET H H 9.1160 . 1 662 . 127 MET HA H 4.8210 . 1 663 . 127 MET HB3 H 1.7110 . 2 664 . 127 MET HB2 H 1.5080 . 2 665 . 128 THR N N 116.9320 . 1 666 . 128 THR H H 8.4480 . 1 667 . 128 THR HA H 4.4990 . 1 668 . 128 THR HB H 4.0170 . 1 669 . 128 THR HG2 H 1.1090 . 1 670 . 129 PHE N N 123.0980 . 1 671 . 129 PHE H H 8.6460 . 1 672 . 129 PHE HA H 4.4930 . 1 673 . 129 PHE HB3 H 2.9820 . 2 674 . 129 PHE HB2 H 2.7330 . 2 675 . 129 PHE HD1 H 7.2390 . 1 676 . 129 PHE HD2 H 7.2390 . 1 677 . 129 PHE HE1 H 7.1130 . 3 678 . 129 PHE HE2 H 7.0060 . 3 stop_ save_