data_5885 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; CHEMICAL SHIFTS OF A FUSED DOCKING DOMAIN FROM THE ERYTHROMYCIN POLYKETIDE SYNTHASE (DEBS), A MODEL FOR THE INTERACTION BETWEEN DEBS 2 AND DEBS 3 ; _BMRB_accession_number 5885 _BMRB_flat_file_name bmr5885.str _Entry_type original _Submission_date 2003-07-29 _Accession_date 2003-07-29 _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 Broadhurst Richard W. . 2 Nietlispach Daniel . . 3 Wheatcroft Michael P. . 4 Leadlay Peter F. . 5 Weissman Kira J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 570 "13C chemical shifts" 391 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-10-06 original author . stop_ _Original_release_date 2003-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Structure of Docking Domains in Modular Polyketide Synthases' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22835172 _PubMed_ID 12954331 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Broadhurst Richard W. . 2 Nietlispach Daniel . . 3 Wheatcroft Michael P. . 4 Leadlay Peter F. . 5 Weissman Kira J. . stop_ _Journal_abbreviation 'Chem. Biol.' _Journal_volume 10 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 723 _Page_last 731 _Year 2003 _Details . loop_ _Keyword NMR 'polyketide synthase' DEBS stop_ save_ ################################## # Molecular system description # ################################## save_system_DOCK23 _Saveframe_category molecular_system _Mol_system_name 'DIMER OF FUSED DOCKING DOMAINS OF DEBS2 AND DEBS3' _Abbreviation_common DOCK23 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DOCK23 subunit 1' $DOCK23 'DOCK23 subunit 2' $DOCK23 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state DIMER _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'DOCK23 subunit 1' 1 'DOCK23 subunit 2' stop_ loop_ _Biological_function 'PORTION OF A MULTIENZYME COMPLEX FOR BIOSYNTHESIS OF 6-deoxyerythronolide B BY SACCHAROPOLYSPORA ERYTHRAEA' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DOCK23 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '6-deoxyerythronolide B synthase' _Abbreviation_common DEBS2/DEBS3 _Molecular_mass . _Mol_thiol_state 'not present' _Details 'N-TERMINAL RESIDUES GLY-1 AND SER-2 ARE CLONING ARTEFACTS. LEU 81 AND MET 82 FORM A LINKER BETWEEN THE C-TERMINAL FRAGMENT OF DEBS2 AND THE N-TERMINAL FRAGMENT OF DEBS3' ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; GSAASPAVDIGDRLDELEKA LEALSAEDGHDDVGQRLESL LRRWNSRRADAPSTSAISED ASDDELFSMLDQRFGGGEDL LMSGDNGMTEEKLRRYLKRT VTELDSVTARLREVEHRAGE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 ALA 4 ALA 5 SER 6 PRO 7 ALA 8 VAL 9 ASP 10 ILE 11 GLY 12 ASP 13 ARG 14 LEU 15 ASP 16 GLU 17 LEU 18 GLU 19 LYS 20 ALA 21 LEU 22 GLU 23 ALA 24 LEU 25 SER 26 ALA 27 GLU 28 ASP 29 GLY 30 HIS 31 ASP 32 ASP 33 VAL 34 GLY 35 GLN 36 ARG 37 LEU 38 GLU 39 SER 40 LEU 41 LEU 42 ARG 43 ARG 44 TRP 45 ASN 46 SER 47 ARG 48 ARG 49 ALA 50 ASP 51 ALA 52 PRO 53 SER 54 THR 55 SER 56 ALA 57 ILE 58 SER 59 GLU 60 ASP 61 ALA 62 SER 63 ASP 64 ASP 65 GLU 66 LEU 67 PHE 68 SER 69 MET 70 LEU 71 ASP 72 GLN 73 ARG 74 PHE 75 GLY 76 GLY 77 GLY 78 GLU 79 ASP 80 LEU 81 LEU 82 MET 83 SER 84 GLY 85 ASP 86 ASN 87 GLY 88 MET 89 THR 90 GLU 91 GLU 92 LYS 93 LEU 94 ARG 95 ARG 96 TYR 97 LEU 98 LYS 99 ARG 100 THR 101 VAL 102 THR 103 GLU 104 LEU 105 ASP 106 SER 107 VAL 108 THR 109 ALA 110 ARG 111 LEU 112 ARG 113 GLU 114 VAL 115 GLU 116 HIS 117 ARG 118 ALA 119 GLY 120 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1PZQ "Structure Of Fused Docking Domains From The Erythromycin Polyketide Synthase (Debs), A Model For The Interaction Between Debs 2" 50.00 60 100.00 100.00 3.83e-31 PDB 1PZR "Structure Of Fused Docking Domains From The Erythromycin Polyketide Synthase (Debs), A Model For The Interaction Between Debs2 " 50.00 60 100.00 100.00 1.54e-32 EMBL CAA44448 "6-deoxyerythronolide B synthase II [Saccharopolyspora erythraea NRRL 2338]" 65.00 3567 100.00 100.00 4.88e-40 EMBL CAM00064 "EryAII Erythromycin polyketide synthase modules 3 and 4 [Saccharopolyspora erythraea NRRL 2338]" 65.00 3567 100.00 100.00 4.88e-40 GB AAA26494 "eryA ORF2 encoding modules 3 & 4 for 6-deoxyerythronolide B formation6-deoxyerythronolide B formation; putative [Saccharopolysp" 65.00 3567 100.00 100.00 4.88e-40 GB AAV39551 "EryAII (morphed) [synthetic construct]" 65.83 3576 98.73 100.00 4.47e-40 GB AAV51821 "EryAII [Saccharopolyspora erythraea]" 65.00 3567 100.00 100.00 4.88e-40 GB EQD87035 "alcohol dehydrogenase [Saccharopolyspora erythraea D]" 65.00 3567 100.00 100.00 4.88e-40 REF WP_011873138 "erythronolide synthase [Saccharopolyspora erythraea]" 65.00 3567 100.00 100.00 4.88e-40 REF WP_037306412 "hypothetical protein [Saccharopolyspora erythraea]" 65.00 845 100.00 100.00 1.65e-40 REF YP_001102990 "EryAII erythromycin polyketide synthase modules 3 and 4 [Saccharopolyspora erythraea NRRL 2338]" 65.00 3567 100.00 100.00 4.88e-40 SP Q03132 "RecName: Full=Erythronolide synthase, modules 3 and 4; AltName: Full=6-deoxyerythronolide B synthase II; AltName: Full=DEBS 2; " 65.00 3567 100.00 100.00 4.88e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $DOCK23 'Streptomyces erythraeus' 1836 Eubacteria . Saccharopolyspora erythraea ERYA 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 _Details $DOCK23 'recombinant technology' . . . . . ; THE DOCK23 CONSTRUCT WAS OVEREXPRESSED AS A FUSION TO GLUTATHIONE S TRANSFERASE IN ESCHERICHIA COLI STRAIN BL21 CODONPLUS USING THE PLASMID PGEX4T-3, INITIALLY PURIFIED BY AFFINITY CHROMATOGRAPHY, CLEAVED WITH THROMBIN AND FINALLY PURIFIED BY GEL FILTRATION ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DOCK23 1.0 mM '[U-100% 13C; U-100% 15N]' NaH2PO4 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DOCK23 0.5 mM '[100% 13C; 100% 15N]' $DOCK23 0.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version 2.7 loop_ _Task 'DATA PROCESSING' stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'MANUAL ASSIGNMENT' stop_ _Details . save_ save_ANSIG2 _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'MANUAL ASSIGNMENT' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label . save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HBHA(CBCACO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CBCACO)NH' _Sample_label . save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNCO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_15N-SEPARATED_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _Sample_label . save_ save_3D_15N-SEPARATED_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED TOCSY' _Sample_label . save_ save_3D_13C-SEPARATED_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _Sample_label . save_ save_3D_HCCH-TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label . save_ save_3D_13C/15N_X-FILTERED_13C-SEPARATED_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C/15N X-FILTERED 13C-SEPARATED NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CBCACO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-SEPARATED TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C/15N X-FILTERED 13C-SEPARATED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 na temperature 298 1 K 'ionic strength' 0.10 0.01 mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemcia_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HBHA(CBCACO)NH' '3D HNCA' '3D HN(CO)CA' '3D HNCO' '3D 15N-SEPARATED NOESY' '3D 15N-SEPARATED TOCSY' '3D 13C-SEPARATED NOESY' '3D HCCH-TOCSY' '3D 13C/15N X-FILTERED 13C-SEPARATED NOESY' stop_ _Sample_conditions_label $condition_set_1 _Chem_shift_reference_set_label $chemcia_shift_reference _Mol_system_component_name 'DOCK23 subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 SER C C 174.218 0.0500 1 2 . 3 ALA H H 8.5170 0.0200 1 3 . 3 ALA N N 125.8270 0.0500 1 4 . 3 ALA C C 177.292 0.0500 1 5 . 4 ALA HA H 4.3565 0.0200 1 6 . 4 ALA HB H 1.3995 0.0200 1 7 . 4 ALA H H 8.3190 0.0200 1 8 . 4 ALA N N 122.9340 0.0500 1 9 . 4 ALA C C 177.503 0.0500 1 10 . 5 SER CB C 63.6810 0.0500 1 11 . 5 SER HA H 4.7810 0.0200 1 12 . 5 SER HB2 H 3.8773 0.0200 1 13 . 5 SER HB3 H 3.8773 0.0200 1 14 . 5 SER H H 8.2750 0.0200 1 15 . 5 SER N N 116.1560 0.0500 1 16 . 6 PRO CA C 63.4160 0.0500 1 17 . 6 PRO CB C 32.0890 0.0500 1 18 . 6 PRO CD C 50.4720 0.0500 1 19 . 6 PRO CG C 27.2460 0.0500 1 20 . 6 PRO HA H 4.4509 0.0200 1 21 . 6 PRO HB2 H 2.3265 0.0200 2 22 . 6 PRO HB3 H 1.9381 0.0200 2 23 . 6 PRO HD2 H 3.8047 0.0200 1 24 . 6 PRO HD3 H 3.8047 0.0200 1 25 . 6 PRO HG2 H 2.0416 0.0200 1 26 . 6 PRO HG3 H 2.0416 0.0200 1 27 . 6 PRO C C 176.577 0.0500 1 28 . 7 ALA CA C 52.7170 0.0500 1 29 . 7 ALA CB C 18.8490 0.0500 1 30 . 7 ALA HA H 4.2860 0.0200 1 31 . 7 ALA HB H 1.3794 0.0200 1 32 . 7 ALA H H 8.3867 0.0200 1 33 . 7 ALA N N 123.4130 0.0500 1 34 . 7 ALA C C 177.704 0.0500 1 35 . 8 VAL CA C 62.2750 0.0500 1 36 . 8 VAL CB C 33.2020 0.0500 1 37 . 8 VAL CG1 C 21.1600 0.0500 1 38 . 8 VAL CG2 C 21.1600 0.0500 1 39 . 8 VAL HA H 4.0795 0.0200 1 40 . 8 VAL HB H 2.0173 0.0200 1 41 . 8 VAL HG1 H 0.9342 0.0200 1 42 . 8 VAL HG2 H 0.9342 0.0200 1 43 . 8 VAL H H 8.0333 0.0200 1 44 . 8 VAL N N 119.5630 0.0500 1 45 . 8 VAL C C 176.033 0.0500 1 46 . 9 ASP CA C 54.1645 0.0500 1 47 . 9 ASP CB C 42.2010 0.0500 1 48 . 9 ASP HA H 4.6887 0.0200 1 49 . 9 ASP HB2 H 2.7698 0.0200 1 50 . 9 ASP HB3 H 2.7698 0.0200 1 51 . 9 ASP H H 8.7084 0.0200 1 52 . 9 ASP N N 125.6120 0.0500 1 53 . 9 ASP C C 177.436 0.0500 1 54 . 10 ILE CA C 61.7900 0.0500 1 55 . 10 ILE CB C 37.7910 0.0500 1 56 . 10 ILE CD1 C 13.9680 0.0500 2 57 . 10 ILE CG1 C 28.8040 0.0500 1 58 . 10 ILE CG2 C 18.3900 0.0500 2 59 . 10 ILE HA H 3.9251 0.0200 1 60 . 10 ILE HB H 1.8322 0.0200 1 61 . 10 ILE HD1 H 0.6947 0.0200 1 62 . 10 ILE HG12 H 1.2280 0.0200 2 63 . 10 ILE HG13 H 1.1093 0.0200 2 64 . 10 ILE HG2 H 0.8050 0.0200 1 65 . 10 ILE H H 8.5083 0.0200 1 66 . 10 ILE N N 122.8180 0.0500 1 67 . 10 ILE C C 176.323 0.0500 1 68 . 11 GLY CA C 47.3960 0.0500 1 69 . 11 GLY HA2 H 3.9120 0.0200 2 70 . 11 GLY HA3 H 3.6445 0.0200 2 71 . 11 GLY H H 8.4790 0.0200 1 72 . 11 GLY N N 110.42 0.0500 1 73 . 11 GLY C C 175.880 0.0500 1 74 . 12 ASP CA C 57.2250 0.0500 1 75 . 12 ASP CB C 40.5700 0.0500 1 76 . 12 ASP HA H 4.4575 0.0200 1 77 . 12 ASP HB2 H 2.8389 0.0200 2 78 . 12 ASP HB3 H 2.7418 0.0200 2 79 . 12 ASP H H 7.5827 0.0200 1 80 . 12 ASP N N 121.0170 0.0500 1 81 . 12 ASP C C 178.881 0.0500 1 82 . 13 ARG CB C 30.5240 0.0500 1 83 . 13 ARG CG C 27.5170 0.0500 1 84 . 13 ARG HA H 4.0040 0.0200 1 85 . 13 ARG HB2 H 1.9120 0.0200 2 86 . 13 ARG HB3 H 1.7488 0.0200 2 87 . 13 ARG HG2 H 1.6397 0.0200 1 88 . 13 ARG HG3 H 1.6397 0.0200 1 89 . 13 ARG H H 7.9056 0.0200 1 90 . 13 ARG N N 118.3040 0.0500 1 91 . 13 ARG C C 180.455 0.0500 1 92 . 14 LEU CA C 58.1490 0.0500 1 93 . 14 LEU CB C 40.7740 0.0500 1 94 . 14 LEU CD1 C 26.4370 0.0500 2 95 . 14 LEU CD2 C 23.7870 0.0500 2 96 . 14 LEU CG C 26.7370 0.0500 1 97 . 14 LEU HA H 3.9527 0.0200 1 98 . 14 LEU HB2 H 2.0495 0.0200 2 99 . 14 LEU HB3 H 1.2063 0.0200 2 100 . 14 LEU HD1 H 0.7445 0.0200 2 101 . 14 LEU HD2 H 0.6396 0.0200 2 102 . 14 LEU HG H 1.6802 0.0200 1 103 . 14 LEU H H 8.4874 0.0200 1 104 . 14 LEU N N 120.8960 0.0500 1 105 . 14 LEU C C 178.143 0.0500 1 106 . 15 ASP CA C 57.6410 0.0500 1 107 . 15 ASP CB C 39.9695 0.0500 1 108 . 15 ASP HA H 4.2958 0.0200 1 109 . 15 ASP HB2 H 3.0238 0.0200 2 110 . 15 ASP HB3 H 2.6873 0.0200 2 111 . 15 ASP H H 8.4105 0.0200 1 112 . 15 ASP N N 121.1470 0.0500 1 113 . 15 ASP C C 179.349 0.0500 1 114 . 16 GLU CA C 59.0340 0.0500 1 115 . 16 GLU CB C 29.8440 0.0500 1 116 . 16 GLU CG C 36.4843 0.0500 1 117 . 16 GLU HA H 4.0091 0.0200 1 118 . 16 GLU HB2 H 2.0577 0.0200 1 119 . 16 GLU HB3 H 2.0577 0.0200 1 120 . 16 GLU HG2 H 2.4630 0.0200 2 121 . 16 GLU HG3 H 2.2700 0.0200 2 122 . 16 GLU H H 8.0893 0.0200 1 123 . 16 GLU N N 118.5470 0.0500 1 124 . 16 GLU C C 179.688 0.0500 1 125 . 17 LEU CA C 57.9700 0.0500 1 126 . 17 LEU CB C 41.4080 0.0500 1 127 . 17 LEU CD1 C 26.8710 0.0500 1 128 . 17 LEU CD2 C 26.8710 0.0500 1 129 . 17 LEU HA H 3.9619 0.0200 1 130 . 17 LEU HB2 H 1.9455 0.0200 1 131 . 17 LEU HB3 H 1.5857 0.0200 1 132 . 17 LEU HD1 H 0.7063 0.0200 1 133 . 17 LEU HD2 H 0.7063 0.0200 1 134 . 17 LEU H H 8.0993 0.0200 1 135 . 17 LEU N N 121.5610 0.0500 1 136 . 17 LEU C C 177.438 0.0500 1 137 . 18 GLU CA C 60.4330 0.0500 1 138 . 18 GLU CB C 29.5450 0.0500 1 139 . 18 GLU CG C 36.1595 0.0500 1 140 . 18 GLU HA H 3.7757 0.0200 1 141 . 18 GLU HB2 H 2.2162 0.0200 1 142 . 18 GLU HB3 H 2.2162 0.0200 1 143 . 18 GLU HG2 H 2.3433 0.0200 2 144 . 18 GLU HG3 H 2.2267 0.0200 2 145 . 18 GLU H H 8.6409 0.0200 1 146 . 18 GLU N N 119.3510 0.0500 1 147 . 18 GLU C C 178.720 0.0500 1 148 . 19 LYS CA C 59.1520 0.0500 1 149 . 19 LYS CB C 32.5030 0.0500 1 150 . 19 LYS CD C 29.3097 0.0500 1 151 . 19 LYS CG C 25.2700 0.0500 1 152 . 19 LYS HA H 4.0538 0.0200 1 153 . 19 LYS HB2 H 1.8964 0.0200 1 154 . 19 LYS HB3 H 1.8964 0.0200 1 155 . 19 LYS HD2 H 1.6763 0.0200 1 156 . 19 LYS HD3 H 1.6763 0.0200 1 157 . 19 LYS HE2 H 2.9512 0.0200 1 158 . 19 LYS HE3 H 2.9512 0.0200 1 159 . 19 LYS HG2 H 1.6300 0.0200 2 160 . 19 LYS HG3 H 1.4877 0.0200 2 161 . 19 LYS H H 7.4963 0.0200 1 162 . 19 LYS N N 116.5500 0.0500 1 163 . 19 LYS C C 179.306 0.0500 1 164 . 20 ALA CA C 54.8670 0.0500 1 165 . 20 ALA CB C 17.9720 0.0500 1 166 . 20 ALA HA H 4.1754 0.0200 1 167 . 20 ALA HB H 1.4269 0.0200 1 168 . 20 ALA H H 7.9912 0.0200 1 169 . 20 ALA N N 122.5550 0.0500 1 170 . 20 ALA C C 180.430 0.0500 1 171 . 21 LEU CA C 57.6650 0.0500 1 172 . 21 LEU CB C 41.1745 0.0500 1 173 . 21 LEU CD1 C 26.8547 0.0500 2 174 . 21 LEU CD2 C 23.4560 0.0500 2 175 . 21 LEU HA H 4.0619 0.0200 1 176 . 21 LEU HB2 H 2.0269 0.0200 2 177 . 21 LEU HB3 H 1.7445 0.0200 2 178 . 21 LEU HD1 H 0.7155 0.0200 2 179 . 21 LEU HD2 H 0.3660 0.0200 2 180 . 21 LEU H H 8.7089 0.0200 1 181 . 21 LEU N N 117.1910 0.0500 1 182 . 21 LEU C C 179.987 0.0500 1 183 . 22 GLU CA C 59.0720 0.0500 1 184 . 22 GLU CB C 29.3830 0.0500 1 185 . 22 GLU CG C 36.1790 0.0500 1 186 . 22 GLU HA H 4.0743 0.0200 1 187 . 22 GLU HB2 H 2.1805 0.0200 1 188 . 22 GLU HB3 H 2.1805 0.0200 1 189 . 22 GLU HG2 H 2.4383 0.0200 1 190 . 22 GLU HG3 H 2.4383 0.0200 1 191 . 22 GLU H H 7.9366 0.0200 1 192 . 22 GLU N N 118.4290 0.0500 1 193 . 22 GLU C C 178.532 0.0500 1 194 . 23 ALA CA C 53.4780 0.0500 1 195 . 23 ALA CB C 18.7700 0.0500 1 196 . 23 ALA HA H 4.3390 0.0200 1 197 . 23 ALA HB H 1.5529 0.0200 1 198 . 23 ALA H H 7.4248 0.0200 1 199 . 23 ALA N N 118.9480 0.0500 1 200 . 23 ALA C C 178.767 0.0500 1 201 . 24 LEU CA C 55.1230 0.0500 1 202 . 24 LEU CB C 43.1290 0.0500 1 203 . 24 LEU CD1 C 25.1180 0.0500 1 204 . 24 LEU CD2 C 25.1180 0.0500 1 205 . 24 LEU HA H 4.3882 0.0200 1 206 . 24 LEU HB2 H 1.9599 0.0200 2 207 . 24 LEU HB3 H 1.6753 0.0200 2 208 . 24 LEU HD1 H 0.7049 0.0200 1 209 . 24 LEU HD2 H 0.7049 0.0200 1 210 . 24 LEU H H 7.6395 0.0200 1 211 . 24 LEU N N 118.2850 0.0500 1 212 . 24 LEU C C 177.773 0.0500 1 213 . 25 SER CA C 59.8540 0.0500 1 214 . 25 SER CB C 63.6520 0.0500 1 215 . 25 SER HA H 4.1768 0.0200 1 216 . 25 SER HB2 H 4.0720 0.0200 2 217 . 25 SER HB3 H 3.9468 0.0200 2 218 . 25 SER H H 8.2972 0.0200 1 219 . 25 SER N N 115.0410 0.0500 1 220 . 25 SER C C 174.736 0.0500 1 221 . 26 ALA CA C 52.7120 0.0500 1 222 . 26 ALA CB C 18.9350 0.0500 1 223 . 26 ALA HA H 4.3346 0.0200 1 224 . 26 ALA HB H 1.2787 0.0200 1 225 . 26 ALA H H 8.1777 0.0200 1 226 . 26 ALA N N 124.2870 0.0500 1 227 . 26 ALA C C 177.606 0.0500 1 228 . 27 GLU CA C 56.2620 0.0500 1 229 . 27 GLU CB C 30.9837 0.0500 1 230 . 27 GLU CG C 36.3150 0.0500 1 231 . 27 GLU HA H 4.3981 0.0200 1 232 . 27 GLU HB2 H 2.2717 0.0200 2 233 . 27 GLU HB3 H 2.1182 0.0200 2 234 . 27 GLU HG2 H 2.4200 0.0200 1 235 . 27 GLU HG3 H 2.4200 0.0200 1 236 . 27 GLU H H 8.0985 0.0200 1 237 . 27 GLU N N 117.3860 0.0500 1 238 . 27 GLU C C 176.273 0.0500 1 239 . 28 ASP CA C 54.4250 0.0500 1 240 . 28 ASP CB C 41.6663 0.0500 1 241 . 28 ASP HA H 4.6514 0.0200 1 242 . 28 ASP HB2 H 2.7354 0.0200 2 243 . 28 ASP HB3 H 2.6626 0.0200 2 244 . 28 ASP H H 8.2496 0.0200 1 245 . 28 ASP N N 120.6260 0.0500 1 246 . 28 ASP C C 176.252 0.0500 1 247 . 29 GLY CA C 45.7040 0.0500 1 248 . 29 GLY HA2 H 3.9690 0.0200 2 249 . 29 GLY HA3 H 3.8173 0.0200 2 250 . 29 GLY H H 8.4487 0.0200 1 251 . 29 GLY N N 126.7990 0.0500 1 252 . 29 GLY C C 174.668 0.0500 1 253 . 30 HIS CB C 27.7040 0.0500 1 254 . 30 HIS CD2 C 121.2130 0.0500 1 255 . 30 HIS CE1 C 137.3680 0.0500 1 256 . 30 HIS HA H 4.8102 0.0200 1 257 . 30 HIS C C 176.034 0.0500 1 258 . 31 ASP CA C 56.7130 0.0500 1 259 . 31 ASP CB C 40.6503 0.0500 1 260 . 31 ASP HA H 4.6851 0.0200 1 261 . 31 ASP HB2 H 2.8404 0.0200 2 262 . 31 ASP HB3 H 2.6955 0.0200 2 263 . 31 ASP H H 8.6760 0.0200 1 264 . 31 ASP N N 119.3820 0.0500 1 265 . 31 ASP C C 176.826 0.0500 1 266 . 32 ASP CA C 55.3090 0.0500 1 267 . 32 ASP CB C 39.8180 0.0500 1 268 . 32 ASP HA H 4.4827 0.0200 1 269 . 32 ASP HB2 H 2.7257 0.0200 1 270 . 32 ASP HB3 H 2.7257 0.0200 1 271 . 32 ASP H H 9.0625 0.0200 1 272 . 32 ASP N N 117.3050 0.0500 1 273 . 32 ASP C C 177.599 0.0500 1 274 . 33 VAL CA C 66.8750 0.0500 1 275 . 33 VAL CB C 31.6790 0.0500 1 276 . 33 VAL CG1 C 23.5900 0.0500 2 277 . 33 VAL CG2 C 19.7780 0.0500 2 278 . 33 VAL HA H 3.1622 0.0200 1 279 . 33 VAL HB H 1.7752 0.0200 1 280 . 33 VAL HG1 H 0.7668 0.0200 2 281 . 33 VAL HG2 H -0.3185 0.0200 2 282 . 33 VAL H H 7.6198 0.0200 1 283 . 33 VAL N N 121.7450 0.0500 1 284 . 33 VAL C C 177.261 0.0500 1 285 . 34 GLY CA C 47.6110 0.0500 1 286 . 34 GLY HA2 H 4.2268 0.0200 2 287 . 34 GLY HA3 H 3.3859 0.0200 2 288 . 34 GLY H H 8.0203 0.0200 1 289 . 34 GLY N N 125.1090 0.0500 1 290 . 34 GLY C C 176.049 0.0500 1 291 . 35 GLN CB C 28.1780 0.0500 1 292 . 35 GLN HA H 4.1580 0.0200 1 293 . 35 GLN HB2 H 2.1646 0.0200 1 294 . 35 GLN HB3 H 2.1646 0.0200 1 295 . 35 GLN HE21 H 7.5690 0.0200 1 296 . 35 GLN HE22 H 6.8870 0.0200 1 297 . 35 GLN HG2 H 2.5280 0.0200 1 298 . 35 GLN HG3 H 2.5280 0.0200 1 299 . 35 GLN H H 7.7734 0.0200 1 300 . 35 GLN N N 119.4290 0.0500 1 301 . 35 GLN NE2 N 111.59 0.0500 1 302 . 35 GLN C C 179.146 0.0500 1 303 . 36 ARG CA C 58.9080 0.0500 1 304 . 36 ARG CB C 29.6740 0.0500 1 305 . 36 ARG CG C 27.2530 0.0500 1 306 . 36 ARG HA H 4.1485 0.0200 1 307 . 36 ARG HB2 H 1.8884 0.0200 1 308 . 36 ARG HB3 H 1.8884 0.0200 1 309 . 36 ARG HD2 H 3.3960 0.0200 1 310 . 36 ARG HD3 H 3.3960 0.0200 1 311 . 36 ARG HG2 H 1.6620 0.0200 1 312 . 36 ARG HG3 H 1.6620 0.0200 1 313 . 36 ARG H H 8.0416 0.0200 1 314 . 36 ARG N N 120.1120 0.0500 1 315 . 36 ARG C C 179.393 0.0500 1 316 . 37 LEU CA C 58.2480 0.0500 1 317 . 37 LEU CB C 42.8100 0.0500 1 318 . 37 LEU CD1 C 22.8650 0.0500 2 319 . 37 LEU CD2 C 25.3500 0.0500 2 320 . 37 LEU CG C 26.5890 0.0500 1 321 . 37 LEU HA H 3.9291 0.0200 1 322 . 37 LEU HB2 H 1.9574 0.0200 1 323 . 37 LEU HB3 H 1.2767 0.0200 1 324 . 37 LEU HD1 H 0.6041 0.0200 2 325 . 37 LEU HD2 H 0.5003 0.0200 2 326 . 37 LEU HG H 1.6356 0.0200 1 327 . 37 LEU H H 8.4268 0.0200 1 328 . 37 LEU N N 119.3430 0.0500 1 329 . 37 LEU C C 178.393 0.0500 1 330 . 38 GLU CA C 60.1810 0.0500 1 331 . 38 GLU CB C 29.4710 0.0500 1 332 . 38 GLU CG C 36.5642 0.0500 1 333 . 38 GLU HA H 3.9064 0.0200 1 334 . 38 GLU HB2 H 2.2355 0.0200 1 335 . 38 GLU HB3 H 2.2355 0.0200 1 336 . 38 GLU HG2 H 2.4170 0.0200 2 337 . 38 GLU HG3 H 2.2800 0.0200 2 338 . 38 GLU H H 8.3996 0.0200 1 339 . 38 GLU N N 118.3180 0.0500 1 340 . 38 GLU C C 179.029 0.0500 1 341 . 39 SER CA C 61.7730 0.0500 1 342 . 39 SER HA H 4.2251 0.0200 1 343 . 39 SER HB2 H 4.1010 0.0200 2 344 . 39 SER HB3 H 3.9190 0.0200 2 345 . 39 SER H H 8.1536 0.0200 1 346 . 39 SER N N 114.7500 0.0500 1 347 . 39 SER C C 177.213 0.0500 1 348 . 40 LEU CA C 58.1110 0.0500 1 349 . 40 LEU CB C 41.7285 0.0500 1 350 . 40 LEU CD1 C 23.8370 0.0500 1 351 . 40 LEU CD2 C 23.8370 0.0500 1 352 . 40 LEU HA H 4.1440 0.0200 1 353 . 40 LEU HB2 H 1.9764 0.0200 2 354 . 40 LEU HB3 H 1.4025 0.0200 2 355 . 40 LEU HD1 H 0.8540 0.0200 1 356 . 40 LEU HD2 H 0.8540 0.0200 1 357 . 40 LEU H H 8.2443 0.0200 1 358 . 40 LEU N N 122.1810 0.0500 1 359 . 40 LEU C C 179.117 0.0500 1 360 . 41 LEU CA C 57.8050 0.0500 1 361 . 41 LEU CB C 42.1812 0.0500 1 362 . 41 LEU CD1 C 26.1890 0.0500 1 363 . 41 LEU CD2 C 26.1890 0.0500 1 364 . 41 LEU HA H 4.1430 0.0200 1 365 . 41 LEU HB2 H 2.0806 0.0200 2 366 . 41 LEU HB3 H 1.4157 0.0200 2 367 . 41 LEU HD1 H 1.0979 0.0200 2 368 . 41 LEU HD2 H 0.9890 0.0200 2 369 . 41 LEU HG H 1.4200 0.0200 1 370 . 41 LEU H H 8.0853 0.0200 1 371 . 41 LEU N N 120.5240 0.0500 1 372 . 41 LEU C C 177.774 0.0500 1 373 . 42 ARG CB C 29.9380 0.0500 1 374 . 42 ARG HA H 4.1130 0.0200 1 375 . 42 ARG HB2 H 2.0280 0.0200 1 376 . 42 ARG HB3 H 2.0280 0.0200 1 377 . 42 ARG H H 8.4825 0.0200 1 378 . 42 ARG N N 118.6470 0.0500 1 379 . 42 ARG C C 180.036 0.0500 1 380 . 43 ARG CB C 29.8320 0.0500 1 381 . 43 ARG CD C 42.9780 0.0500 1 382 . 43 ARG CG C 27.4230 0.0500 1 383 . 43 ARG HA H 4.0905 0.0200 1 384 . 43 ARG HB2 H 2.0580 0.0200 1 385 . 43 ARG HB3 H 2.0580 0.0200 1 386 . 43 ARG HD2 H 3.2500 0.0200 1 387 . 43 ARG HD3 H 3.2500 0.0200 1 388 . 43 ARG HG2 H 1.8070 0.0200 1 389 . 43 ARG HG3 H 1.8070 0.0200 1 390 . 43 ARG H H 8.2327 0.0200 1 391 . 43 ARG N N 119.7270 0.0500 1 392 . 43 ARG C C 178.936 0.0500 1 393 . 44 TRP CA C 60.5090 0.0500 1 394 . 44 TRP CB C 29.3140 0.0500 1 395 . 44 TRP CD1 C 125.9390 0.0500 1 396 . 44 TRP CE3 C 120.7870 0.0500 1 397 . 44 TRP CH2 C 121.9880 0.0500 1 398 . 44 TRP CZ2 C 114.4640 0.0500 1 399 . 44 TRP CZ3 C 123.5680 0.0500 1 400 . 44 TRP HA H 4.3030 0.0200 1 401 . 44 TRP HB2 H 3.4085 0.0200 2 402 . 44 TRP HB3 H 3.3528 0.0200 2 403 . 44 TRP HD1 H 7.1172 0.0200 1 404 . 44 TRP HE1 H 10.4502 0.0200 1 405 . 44 TRP HE3 H 7.5482 0.0200 1 406 . 44 TRP HH2 H 7.2068 0.0200 1 407 . 44 TRP H H 8.5102 0.0200 1 408 . 44 TRP HZ2 H 7.6561 0.0200 1 409 . 44 TRP HZ3 H 6.9430 0.0200 1 410 . 44 TRP N N 121.7210 0.0500 1 411 . 44 TRP NE1 N 128.7590 0.0500 1 412 . 44 TRP C C 178.622 0.0500 1 413 . 45 ASN CA C 55.1830 0.0500 1 414 . 45 ASN CB C 37.9520 0.0500 1 415 . 45 ASN HA H 4.4645 0.0200 1 416 . 45 ASN HB2 H 2.9520 0.0200 2 417 . 45 ASN HB3 H 2.8791 0.0200 2 418 . 45 ASN HD21 H 7.5528 0.0200 1 419 . 45 ASN HD22 H 6.9572 0.0200 1 420 . 45 ASN H H 8.8323 0.0200 1 421 . 45 ASN N N 115.7430 0.0500 1 422 . 45 ASN ND2 N 109.83 0.0500 1 423 . 45 ASN C C 177.997 0.0500 1 424 . 46 SER CA C 60.0680 0.0500 1 425 . 46 SER CB C 63.3800 0.0500 1 426 . 46 SER HA H 4.4473 0.0200 1 427 . 46 SER HB2 H 4.0512 0.0200 1 428 . 46 SER HB3 H 4.0512 0.0200 1 429 . 46 SER H H 7.9915 0.0200 1 430 . 46 SER N N 115.1740 0.0500 1 431 . 46 SER C C 175.393 0.0500 1 432 . 47 ARG CA C 57.6020 0.0500 1 433 . 47 ARG CB C 29.8200 0.0500 1 434 . 47 ARG CG C 26.7430 0.0500 1 435 . 47 ARG HA H 4.1750 0.0200 1 436 . 47 ARG HB2 H 1.6993 0.0200 1 437 . 47 ARG HB3 H 1.6993 0.0200 1 438 . 47 ARG HD2 H 2.8260 0.0200 1 439 . 47 ARG HD3 H 2.8260 0.0200 1 440 . 47 ARG HG2 H 1.5240 0.0200 1 441 . 47 ARG HG3 H 1.5240 0.0200 1 442 . 47 ARG H H 7.4564 0.0200 1 443 . 47 ARG N N 120.4960 0.0500 1 444 . 47 ARG C C 176.788 0.0500 1 445 . 48 ARG CA C 55.7930 0.0500 1 446 . 48 ARG CB C 30.2520 0.0500 1 447 . 48 ARG CD C 42.8682 0.0500 1 448 . 48 ARG CG C 26.8870 0.0500 1 449 . 48 ARG HA H 4.2375 0.0200 1 450 . 48 ARG HB2 H 1.8630 0.0200 2 451 . 48 ARG HB3 H 1.6390 0.0200 2 452 . 48 ARG HD2 H 2.9653 0.0200 1 453 . 48 ARG HD3 H 2.9653 0.0200 1 454 . 48 ARG HG2 H 1.4138 0.0200 1 455 . 48 ARG HG3 H 1.4138 0.0200 1 456 . 48 ARG H H 7.7227 0.0200 1 457 . 48 ARG N N 118.2960 0.0500 1 458 . 48 ARG C C 176.253 0.0500 1 459 . 49 ALA CA C 52.7450 0.0500 1 460 . 49 ALA CB C 19.3530 0.0500 1 461 . 49 ALA HA H 4.2778 0.0200 1 462 . 49 ALA HB H 1.4073 0.0200 1 463 . 49 ALA H H 7.9710 0.0200 1 464 . 49 ALA N N 123.4170 0.0500 1 465 . 49 ALA C C 177.480 0.0500 1 466 . 50 ASP CA C 54.0530 0.0500 1 467 . 50 ASP CB C 41.2295 0.0500 1 468 . 50 ASP HA H 4.5867 0.0200 1 469 . 50 ASP HB2 H 2.6870 0.0200 2 470 . 50 ASP HB3 H 2.6450 0.0200 2 471 . 50 ASP H H 8.1534 0.0200 1 472 . 50 ASP N N 118.3680 0.0500 1 473 . 50 ASP C C 175.564 0.0500 1 474 . 51 ALA CA C 50.5500 0.0500 1 475 . 51 ALA CB C 18.3450 0.0500 1 476 . 51 ALA HA H 4.5937 0.0200 1 477 . 51 ALA HB H 1.3833 0.0200 1 478 . 51 ALA H H 7.9833 0.0200 1 479 . 51 ALA N N 124.5430 0.0500 1 480 . 52 PRO CA C 62.9890 0.0500 1 481 . 52 PRO HA H 4.4855 0.0200 1 482 . 52 PRO HB2 H 2.3370 0.0200 2 483 . 52 PRO HB3 H 1.9540 0.0200 2 484 . 52 PRO C C 177.065 0.0500 1 485 . 53 SER HA H 4.5660 0.0200 1 486 . 53 SER HB2 H 3.9340 0.0200 1 487 . 53 SER HB3 H 3.9340 0.0200 1 488 . 53 SER H H 8.5270 0.0200 1 489 . 53 SER N N 115.9300 0.0500 1 490 . 53 SER C C 174.982 0.0500 1 491 . 54 THR H H 8.2770 0.0200 1 492 . 54 THR N N 115.2270 0.0500 1 493 . 54 THR C C 173.871 0.0500 1 494 . 55 SER H H 8.0190 0.0200 1 495 . 55 SER N N 122.9270 0.0500 1 496 . 56 ALA CA C 51.7470 0.0500 1 497 . 56 ALA HA H 4.1170 0.0200 1 498 . 56 ALA HB H 1.5110 0.0200 1 499 . 57 ILE H H 8.0470 0.0200 1 500 . 57 ILE N N 123.9800 0.0500 1 501 . 59 GLU CA C 56.8580 0.0500 1 502 . 59 GLU HA H 4.3580 0.0200 1 503 . 59 GLU HB2 H 2.1180 0.0200 2 504 . 59 GLU C C 175.919 0.0500 1 505 . 60 ASP CA C 53.7270 0.0500 1 506 . 60 ASP CB C 41.0760 0.0500 1 507 . 60 ASP HA H 4.5960 0.0200 1 508 . 60 ASP HB2 H 2.6980 0.0200 2 509 . 60 ASP HB3 H 2.5850 0.0200 2 510 . 60 ASP H H 8.4115 0.0200 1 511 . 60 ASP N N 120.7490 0.0500 1 512 . 60 ASP C C 175.850 0.0500 1 513 . 61 ALA CA C 52.6780 0.0500 1 514 . 61 ALA CB C 19.2030 0.0500 1 515 . 61 ALA HA H 4.3360 0.0200 1 516 . 61 ALA HB H 1.3784 0.0200 1 517 . 61 ALA H H 8.2780 0.0200 1 518 . 61 ALA N N 124.6790 0.0500 1 519 . 61 ALA C C 178.053 0.0500 1 520 . 62 SER CA C 58.4660 0.0500 1 521 . 62 SER CB C 63.9720 0.0500 1 522 . 62 SER HA H 4.3888 0.0200 1 523 . 62 SER HB2 H 4.0870 0.0200 2 524 . 62 SER HB3 H 3.9317 0.0200 2 525 . 62 SER H H 8.4597 0.0200 1 526 . 62 SER N N 116.0910 0.0500 1 527 . 62 SER C C 175.380 0.0500 1 528 . 63 ASP CA C 56.6540 0.0500 1 529 . 63 ASP CB C 39.6860 0.0500 1 530 . 63 ASP HA H 4.0461 0.0200 1 531 . 63 ASP HB2 H 2.4453 0.0200 2 532 . 63 ASP HB3 H 2.2455 0.0200 2 533 . 63 ASP H H 8.5392 0.0200 1 534 . 63 ASP N N 122.7430 0.0500 1 535 . 63 ASP C C 176.199 0.0500 1 536 . 64 ASP CA C 57.5130 0.0500 1 537 . 64 ASP CB C 40.3157 0.0500 1 538 . 64 ASP HA H 4.3513 0.0200 1 539 . 64 ASP HB2 H 2.6680 0.0200 2 540 . 64 ASP HB3 H 2.5973 0.0200 2 541 . 64 ASP H H 8.0280 0.0200 1 542 . 64 ASP N N 116.8230 0.0500 1 543 . 64 ASP C C 179.052 0.0500 1 544 . 65 GLU CA C 59.1120 0.0500 1 545 . 65 GLU CB C 29.5665 0.0500 1 546 . 65 GLU CG C 36.6105 0.0500 1 547 . 65 GLU HA H 4.0222 0.0200 1 548 . 65 GLU HB2 H 2.0930 0.0200 2 549 . 65 GLU HB3 H 2.0165 0.0200 2 550 . 65 GLU HG2 H 2.3080 0.0200 2 551 . 65 GLU HG3 H 2.2200 0.0200 2 552 . 65 GLU H H 7.8689 0.0200 1 553 . 65 GLU N N 119.9410 0.0500 1 554 . 65 GLU C C 178.519 0.0500 1 555 . 66 LEU CA C 58.0920 0.0500 1 556 . 66 LEU CB C 41.7180 0.0500 1 557 . 66 LEU HA H 4.0843 0.0200 1 558 . 66 LEU HB2 H 1.5210 0.0200 1 559 . 66 LEU HB3 H 1.5210 0.0200 1 560 . 66 LEU HG H 1.5400 0.0200 1 561 . 66 LEU H H 7.7568 0.0200 1 562 . 66 LEU N N 122.2300 0.0500 1 563 . 66 LEU C C 178.453 0.0500 1 564 . 67 PHE CA C 58.8260 0.0500 1 565 . 67 PHE CB C 36.9650 0.0500 1 566 . 67 PHE CD1 C 130.7586 0.0500 1 567 . 67 PHE CD2 C 130.7586 0.0500 1 568 . 67 PHE CE1 C 130.1870 0.0500 1 569 . 67 PHE CE2 C 130.1870 0.0500 1 570 . 67 PHE CZ C 128.0680 0.0500 1 571 . 67 PHE HA H 4.1112 0.0200 1 572 . 67 PHE HB2 H 3.1709 0.0200 2 573 . 67 PHE HB3 H 2.9777 0.0200 2 574 . 67 PHE HD1 H 6.6752 0.0200 1 575 . 67 PHE HD2 H 6.6752 0.0200 1 576 . 67 PHE HE1 H 7.0507 0.0200 1 577 . 67 PHE HE2 H 7.0507 0.0200 1 578 . 67 PHE H H 8.4550 0.0200 1 579 . 67 PHE HZ H 6.9597 0.0200 1 580 . 67 PHE N N 116.5550 0.0500 1 581 . 67 PHE C C 177.788 0.0500 1 582 . 68 SER CA C 61.7690 0.0500 1 583 . 68 SER CB C 62.7580 0.0500 1 584 . 68 SER HA H 4.3372 0.0200 1 585 . 68 SER HB2 H 3.9998 0.0200 1 586 . 68 SER HB3 H 3.9998 0.0200 1 587 . 68 SER H H 8.0576 0.0200 1 588 . 68 SER N N 132.0640 0.0500 1 589 . 68 SER C C 177.344 0.0500 1 590 . 69 MET CA C 59.0080 0.0500 1 591 . 69 MET CB C 31.7080 0.0500 1 592 . 69 MET CG C 31.6780 0.0500 1 593 . 69 MET HA H 4.1346 0.0200 1 594 . 69 MET HB2 H 2.2694 0.0200 1 595 . 69 MET HB3 H 2.2694 0.0200 1 596 . 69 MET HG2 H 2.7392 0.0200 2 597 . 69 MET HG3 H 2.5146 0.0200 2 598 . 69 MET H H 7.9260 0.0200 1 599 . 69 MET N N 121.5990 0.0500 1 600 . 69 MET C C 179.380 0.0500 1 601 . 70 LEU CA C 57.6310 0.0500 1 602 . 70 LEU CB C 40.5830 0.0500 1 603 . 70 LEU CD1 C 26.7470 0.0500 2 604 . 70 LEU CD2 C 21.7200 0.0500 2 605 . 70 LEU HA H 3.7548 0.0200 1 606 . 70 LEU HB2 H 2.0210 0.0200 2 607 . 70 LEU HB3 H 1.3628 0.0200 2 608 . 70 LEU HD1 H 0.9524 0.0200 2 609 . 70 LEU HD2 H 0.8188 0.0200 2 610 . 70 LEU HG H 1.9600 0.0200 1 611 . 70 LEU H H 8.3178 0.0200 1 612 . 70 LEU N N 121.8090 0.0500 1 613 . 70 LEU C C 178.045 0.0500 1 614 . 71 ASP CA C 57.6180 0.0500 1 615 . 71 ASP CB C 40.1067 0.0500 1 616 . 71 ASP HA H 4.4852 0.0200 1 617 . 71 ASP HB2 H 2.9450 0.0200 2 618 . 71 ASP HB3 H 2.6608 0.0200 2 619 . 71 ASP H H 8.9831 0.0200 1 620 . 71 ASP N N 120.3160 0.0500 1 621 . 71 ASP C C 179.685 0.0500 1 622 . 72 GLN CA C 58.2660 0.0500 1 623 . 72 GLN CB C 28.9110 0.0500 1 624 . 72 GLN CG C 34.0100 0.0500 1 625 . 72 GLN HA H 4.0676 0.0200 1 626 . 72 GLN HB2 H 2.1875 0.0200 2 627 . 72 GLN HB3 H 2.0145 0.0200 2 628 . 72 GLN HE21 H 7.4340 0.0200 2 629 . 72 GLN HE22 H 6.8500 0.0200 2 630 . 72 GLN HG2 H 2.5550 0.0200 2 631 . 72 GLN HG3 H 2.4160 0.0200 2 632 . 72 GLN H H 7.6168 0.0200 1 633 . 72 GLN N N 117.1250 0.0500 1 634 . 72 GLN NE2 N 111.83 0.0500 1 635 . 72 GLN C C 178.127 0.0500 1 636 . 73 ARG CA C 58.0950 0.0500 1 637 . 73 ARG CB C 30.4390 0.0500 1 638 . 73 ARG CG C 27.4820 0.0500 1 639 . 73 ARG HA H 4.0762 0.0200 1 640 . 73 ARG HB2 H 1.6281 0.0200 2 641 . 73 ARG HB3 H 1.4748 0.0200 2 642 . 73 ARG HG2 H 1.8090 0.0200 1 643 . 73 ARG HG3 H 1.8090 0.0200 1 644 . 73 ARG H H 7.7760 0.0200 1 645 . 73 ARG N N 119.2960 0.0500 1 646 . 73 ARG C C 178.187 0.0500 1 647 . 74 PHE CA C 55.6060 0.0500 1 648 . 74 PHE CB C 38.8270 0.0500 1 649 . 74 PHE CD1 C 131.0050 0.0500 1 650 . 74 PHE CD2 C 131.0050 0.0500 1 651 . 74 PHE CE1 C 129.0820 0.0500 1 652 . 74 PHE CE2 C 129.0820 0.0500 1 653 . 74 PHE CZ C 130.6045 0.0500 1 654 . 74 PHE HA H 5.0077 0.0200 1 655 . 74 PHE HB2 H 3.4556 0.0200 2 656 . 74 PHE HB3 H 3.1222 0.0200 2 657 . 74 PHE HD1 H 7.1489 0.0200 1 658 . 74 PHE HD2 H 7.1489 0.0200 1 659 . 74 PHE HE1 H 7.3494 0.0200 1 660 . 74 PHE HE2 H 7.3494 0.0200 1 661 . 74 PHE H H 8.3558 0.0200 1 662 . 74 PHE HZ H 7.1900 0.0200 1 663 . 74 PHE N N 115.7460 0.0500 1 664 . 74 PHE C C 177.153 0.0500 1 665 . 75 GLY CA C 45.8370 0.0500 1 666 . 75 GLY HA2 H 4.2540 0.0200 2 667 . 75 GLY HA3 H 4.0355 0.0200 2 668 . 75 GLY H H 7.9742 0.0200 1 669 . 75 GLY N N 127.3020 0.0500 1 670 . 75 GLY C C 174.750 0.0500 1 671 . 76 GLY CA C 45.4800 0.0500 1 672 . 76 GLY HA2 H 4.1290 0.0200 2 673 . 76 GLY HA3 H 3.9750 0.0200 2 674 . 76 GLY H H 8.4573 0.0200 1 675 . 76 GLY N N 127.6520 0.0500 1 676 . 76 GLY C C 174.633 0.0500 1 677 . 77 GLY CA C 45.3120 0.0500 1 678 . 77 GLY HA2 H 4.0045 0.0200 1 679 . 77 GLY HA3 H 4.0045 0.0200 1 680 . 77 GLY H H 8.4150 0.0200 1 681 . 77 GLY N N 127.7410 0.0500 1 682 . 77 GLY C C 174.525 0.0500 1 683 . 78 GLU CA C 57.0640 0.0500 1 684 . 78 GLU CB C 30.0270 0.0500 1 685 . 78 GLU CG C 36.2830 0.0500 1 686 . 78 GLU HA H 4.2436 0.0200 1 687 . 78 GLU HB2 H 2.0590 0.0200 2 688 . 78 GLU HB3 H 1.9387 0.0200 2 689 . 78 GLU HG2 H 2.2413 0.0200 1 690 . 78 GLU HG3 H 2.2413 0.0200 1 691 . 78 GLU H H 8.5040 0.0200 1 692 . 78 GLU N N 120.3590 0.0500 1 693 . 78 GLU C C 176.451 0.0500 1 694 . 79 ASP CA C 54.7260 0.0500 1 695 . 79 ASP CB C 40.6800 0.0500 1 696 . 79 ASP HA H 4.5162 0.0200 1 697 . 79 ASP HB2 H 2.7017 0.0200 2 698 . 79 ASP HB3 H 2.5940 0.0200 2 699 . 79 ASP H H 8.5087 0.0200 1 700 . 79 ASP N N 120.0110 0.0500 1 701 . 79 ASP C C 176.446 0.0500 1 702 . 80 LEU CA C 55.5920 0.0500 1 703 . 80 LEU CB C 41.8540 0.0500 1 704 . 80 LEU HA H 4.2365 0.0200 1 705 . 80 LEU HB2 H 1.5530 0.0200 2 706 . 80 LEU HB3 H 1.5250 0.0200 2 707 . 80 LEU HG H 1.5620 0.0200 1 708 . 80 LEU H H 8.0598 0.0200 1 709 . 80 LEU N N 121.4200 0.0500 1 710 . 80 LEU C C 177.403 0.0500 1 711 . 81 LEU CA C 55.6700 0.0500 1 712 . 81 LEU CB C 41.9260 0.0500 1 713 . 81 LEU HA H 4.2574 0.0200 1 714 . 81 LEU HB2 H 1.6756 0.0200 2 715 . 81 LEU HB3 H 1.5887 0.0200 2 716 . 81 LEU H H 8.0625 0.0200 1 717 . 81 LEU N N 120.6070 0.0500 1 718 . 82 MET HA H 4.4860 0.0200 1 719 . 82 MET HB2 H 2.1110 0.0200 2 720 . 82 MET HB3 H 2.0270 0.0200 2 721 . 82 MET C C 176.221 0.0500 1 722 . 83 SER CA C 58.5930 0.0500 1 723 . 83 SER HA H 4.4163 0.0200 1 724 . 83 SER HB2 H 3.9200 0.0200 1 725 . 83 SER HB3 H 3.9200 0.0200 1 726 . 83 SER H H 8.2310 0.0200 1 727 . 83 SER N N 115.6370 0.0500 1 728 . 83 SER C C 175.040 0.0500 1 729 . 84 GLY CA C 45.3120 0.0500 1 730 . 84 GLY HA2 H 3.9900 0.0200 1 731 . 84 GLY HA3 H 3.9900 0.0200 1 732 . 84 GLY H H 8.4360 0.0200 1 733 . 84 GLY N N 110.24 0.0500 1 734 . 84 GLY C C 173.946 0.0500 1 735 . 85 ASP CB C 41.2170 0.0500 1 736 . 85 ASP HA H 4.6620 0.0200 1 737 . 85 ASP HB2 H 2.6920 0.0200 1 738 . 85 ASP HB3 H 2.6920 0.0200 1 739 . 85 ASP H H 8.2120 0.0200 1 740 . 85 ASP N N 119.8310 0.0500 1 741 . 85 ASP C C 176.308 0.0500 1 742 . 86 ASN CA C 54.2820 0.0500 1 743 . 86 ASN CB C 38.8020 0.0500 1 744 . 86 ASN HA H 4.6898 0.0200 1 745 . 86 ASN HB2 H 2.8600 0.0200 1 746 . 86 ASN HB3 H 2.8600 0.0200 1 747 . 86 ASN HD21 H 7.6480 0.0200 1 748 . 86 ASN HD22 H 6.9650 0.0200 1 749 . 86 ASN H H 8.5070 0.0200 1 750 . 86 ASN N N 118.7390 0.0500 1 751 . 86 ASN ND2 N 112.62 0.0500 1 752 . 86 ASN C C 175.824 0.0500 1 753 . 87 GLY CA C 45.7460 0.0500 1 754 . 87 GLY HA2 H 4.0000 0.0200 1 755 . 87 GLY HA3 H 4.0000 0.0200 1 756 . 87 GLY H H 8.5620 0.0200 1 757 . 87 GLY N N 127.5700 0.0500 1 758 . 87 GLY C C 177.446 0.0500 1 759 . 88 MET CA C 55.3450 0.0500 1 760 . 88 MET CB C 32.3507 0.0500 1 761 . 88 MET CG C 32.3075 0.0500 1 762 . 88 MET HA H 4.6645 0.0200 1 763 . 88 MET HB2 H 2.2635 0.0200 2 764 . 88 MET HB3 H 2.1355 0.0200 2 765 . 88 MET HG2 H 2.6920 0.0200 2 766 . 88 MET HG3 H 2.5652 0.0200 2 767 . 88 MET H H 8.2253 0.0200 1 768 . 88 MET N N 119.4860 0.0500 1 769 . 88 MET C C 176.890 0.0500 1 770 . 89 THR CA C 66.7130 0.0500 1 771 . 89 THR CB C 69.0040 0.0500 1 772 . 89 THR CG2 C 22.3260 0.0500 1 773 . 89 THR HA H 3.9534 0.0200 1 774 . 89 THR HB H 4.2220 0.0200 1 775 . 89 THR HG2 H 1.2918 0.0200 1 776 . 89 THR H H 8.3848 0.0200 1 777 . 89 THR N N 118.9850 0.0500 1 778 . 89 THR C C 175.730 0.0500 1 779 . 90 GLU CA C 60.9410 0.0500 1 780 . 90 GLU CB C 29.8281 0.0500 1 781 . 90 GLU CG C 37.0620 0.0500 1 782 . 90 GLU HA H 3.8232 0.0200 1 783 . 90 GLU HB2 H 2.2598 0.0200 2 784 . 90 GLU HB3 H 2.0393 0.0200 2 785 . 90 GLU HG2 H 2.1665 0.0200 1 786 . 90 GLU HG3 H 2.1665 0.0200 1 787 . 90 GLU H H 9.0826 0.0200 1 788 . 90 GLU N N 120.0810 0.0500 1 789 . 90 GLU C C 176.850 0.0500 1 790 . 91 GLU HA H 4.1593 0.0200 1 791 . 91 GLU H H 7.6180 0.0200 1 792 . 91 GLU N N 116.6360 0.0500 1 793 . 91 GLU C C 178.680 0.0500 1 794 . 92 LYS CA C 60.5900 0.0500 1 795 . 92 LYS CB C 33.0370 0.0500 1 796 . 92 LYS HA H 3.9304 0.0200 1 797 . 92 LYS HB2 H 1.8253 0.0200 2 798 . 92 LYS HB3 H 1.7090 0.0200 2 799 . 92 LYS H H 8.0980 0.0200 1 800 . 92 LYS N N 120.4840 0.0500 1 801 . 92 LYS C C 178.680 0.0500 1 802 . 93 LEU CB C 44.0450 0.0500 1 803 . 93 LEU CD1 C 28.0960 0.0500 2 804 . 93 LEU CG C 27.4480 0.0500 1 805 . 93 LEU HA H 4.1277 0.0200 1 806 . 93 LEU HB2 H 2.2778 0.0200 2 807 . 93 LEU HB3 H 1.3173 0.0200 2 808 . 93 LEU HD1 H 1.0569 0.0200 2 809 . 93 LEU HD2 H 0.9300 0.0200 2 810 . 93 LEU HG H 2.0344 0.0200 1 811 . 93 LEU H H 8.6177 0.0200 1 812 . 93 LEU N N 118.0340 0.0500 1 813 . 93 LEU C C 178.605 0.0500 1 814 . 94 ARG HA H 3.8280 0.0200 1 815 . 94 ARG HG2 H 1.5240 0.0200 1 816 . 94 ARG HG3 H 1.5240 0.0200 1 817 . 94 ARG H H 8.3326 0.0200 1 818 . 94 ARG N N 117.9780 0.0500 1 819 . 94 ARG C C 178.078 0.0500 1 820 . 95 ARG HA H 4.0225 0.0200 1 821 . 95 ARG HB2 H 1.8550 0.0200 1 822 . 95 ARG HB3 H 1.8550 0.0200 1 823 . 95 ARG HG2 H 1.8620 0.0200 2 824 . 95 ARG HG3 H 1.5820 0.0200 2 825 . 95 ARG H H 8.3875 0.0200 1 826 . 95 ARG N N 118.6250 0.0500 1 827 . 95 ARG C C 180.478 0.0500 1 828 . 96 TYR CA C 63.0420 0.0500 1 829 . 96 TYR CB C 38.1500 0.0500 1 830 . 96 TYR CD1 C 132.5050 0.0500 1 831 . 96 TYR CD2 C 132.5050 0.0500 1 832 . 96 TYR CE1 C 118.4737 0.0500 1 833 . 96 TYR CE2 C 118.4737 0.0500 1 834 . 96 TYR HA H 4.1779 0.0200 1 835 . 96 TYR HB2 H 3.2251 0.0200 2 836 . 96 TYR HB3 H 2.9381 0.0200 2 837 . 96 TYR HD1 H 7.2139 0.0200 1 838 . 96 TYR HD2 H 7.2139 0.0200 1 839 . 96 TYR HE1 H 6.6582 0.0200 1 840 . 96 TYR HE2 H 6.6582 0.0200 1 841 . 96 TYR H H 8.8287 0.0200 1 842 . 96 TYR N N 118.4800 0.0500 1 843 . 96 TYR C C 179.519 0.0500 1 844 . 97 LEU CA C 59.0000 0.0500 1 845 . 97 LEU CB C 41.3540 0.0500 1 846 . 97 LEU CD1 C 27.2510 0.0500 1 847 . 97 LEU CD2 C 27.2510 0.0500 1 848 . 97 LEU HA H 4.3064 0.0200 1 849 . 97 LEU HB2 H 2.2631 0.0200 1 850 . 97 LEU HB3 H 1.6333 0.0200 1 851 . 97 LEU HD1 H 1.0221 0.0200 1 852 . 97 LEU HD2 H 1.0221 0.0200 1 853 . 97 LEU HG H 1.6390 0.0200 1 854 . 97 LEU H H 9.2677 0.0200 1 855 . 97 LEU N N 124.7750 0.0500 1 856 . 97 LEU C C 177.683 0.0500 1 857 . 98 LYS CA C 60.6960 0.0500 1 858 . 98 LYS HA H 3.8503 0.0200 1 859 . 98 LYS HB2 H 1.8925 0.0200 1 860 . 98 LYS HB3 H 1.8925 0.0200 1 861 . 98 LYS H H 8.4272 0.0200 1 862 . 98 LYS N N 118.0580 0.0500 1 863 . 98 LYS C C 179.251 0.0500 1 864 . 99 ARG HA H 4.1907 0.0200 1 865 . 99 ARG HB2 H 1.6990 0.0200 1 866 . 99 ARG HB3 H 1.6990 0.0200 1 867 . 99 ARG H H 7.8187 0.0200 1 868 . 99 ARG N N 117.8770 0.0500 1 869 . 99 ARG C C 178.589 0.0500 1 870 . 100 THR CA C 67.7530 0.0500 1 871 . 100 THR CB C 67.8980 0.0500 1 872 . 100 THR CG2 C 22.5470 0.0500 1 873 . 100 THR HA H 4.3533 0.0200 1 874 . 100 THR HB H 3.9695 0.0200 1 875 . 100 THR HG2 H 1.3291 0.0200 1 876 . 100 THR H H 8.5228 0.0200 1 877 . 100 THR N N 118.1340 0.0500 1 878 . 100 THR C C 176.489 0.0500 1 879 . 101 VAL CA C 67.4670 0.0500 1 880 . 101 VAL CB C 31.4110 0.0500 1 881 . 101 VAL CG1 C 24.7480 0.0500 2 882 . 101 VAL CG2 C 21.8240 0.0500 2 883 . 101 VAL HA H 3.5666 0.0200 1 884 . 101 VAL HB H 2.2517 0.0200 1 885 . 101 VAL HG1 H 1.1774 0.0200 2 886 . 101 VAL HG2 H 0.9529 0.0200 2 887 . 101 VAL H H 8.6682 0.0200 1 888 . 101 VAL N N 123.1210 0.0500 1 889 . 101 VAL C C 177.268 0.0500 1 890 . 102 THR CA C 66.8960 0.0500 1 891 . 102 THR CB C 68.5840 0.0500 1 892 . 102 THR CG2 C 21.7015 0.0500 1 893 . 102 THR HA H 4.0410 0.0200 1 894 . 102 THR HB H 4.2957 0.0200 1 895 . 102 THR HG2 H 1.2612 0.0200 1 896 . 102 THR H H 7.8492 0.0200 1 897 . 102 THR N N 115.8620 0.0500 1 898 . 102 THR C C 177.031 0.0500 1 899 . 103 GLU CA C 58.9640 0.0500 1 900 . 103 GLU HA H 4.1932 0.0200 1 901 . 103 GLU HB2 H 2.0240 0.0200 1 902 . 103 GLU HB3 H 2.0240 0.0200 1 903 . 103 GLU HG2 H 2.4570 0.0200 2 904 . 103 GLU HG3 H 2.3150 0.0200 2 905 . 103 GLU H H 7.8134 0.0200 1 906 . 103 GLU N N 122.5440 0.0500 1 907 . 103 GLU C C 178.219 0.0500 1 908 . 104 LEU CA C 58.1680 0.0500 1 909 . 104 LEU CB C 41.8470 0.0500 1 910 . 104 LEU CD1 C 26.1800 0.0500 2 911 . 104 LEU CD2 C 23.0580 0.0500 2 912 . 104 LEU CG C 27.4020 0.0500 1 913 . 104 LEU HA H 4.1554 0.0200 1 914 . 104 LEU HB2 H 2.4038 0.0200 2 915 . 104 LEU HB3 H 1.4968 0.0200 2 916 . 104 LEU HD1 H 1.1055 0.0200 2 917 . 104 LEU HD2 H 0.9838 0.0200 2 918 . 104 LEU HG H 1.6745 0.0200 1 919 . 104 LEU H H 8.9435 0.0200 1 920 . 104 LEU N N 121.0800 0.0500 1 921 . 104 LEU C C 179.991 0.0500 1 922 . 105 ASP CA C 57.8260 0.0500 1 923 . 105 ASP CB C 39.5007 0.0500 1 924 . 105 ASP HA H 4.5076 0.0200 1 925 . 105 ASP HB2 H 2.9189 0.0200 2 926 . 105 ASP HB3 H 2.6896 0.0200 2 927 . 105 ASP H H 9.0481 0.0200 1 928 . 105 ASP N N 123.4150 0.0500 1 929 . 105 ASP C C 179.011 0.0500 1 930 . 106 SER CA C 61.6910 0.0500 1 931 . 106 SER CB C 62.7550 0.0500 1 932 . 106 SER HA H 4.3589 0.0200 1 933 . 106 SER HB2 H 4.0969 0.0200 2 934 . 106 SER HB3 H 4.0958 0.0200 2 935 . 106 SER H H 8.1317 0.0200 1 936 . 106 SER N N 117.0550 0.0500 1 937 . 106 SER C C 177.693 0.0500 1 938 . 107 VAL CA C 66.3770 0.0500 1 939 . 107 VAL CB C 31.7200 0.0500 1 940 . 107 VAL CG1 C 22.5340 0.0500 2 941 . 107 VAL CG2 C 22.2090 0.0500 2 942 . 107 VAL HA H 3.8852 0.0200 1 943 . 107 VAL HB H 2.1032 0.0200 1 944 . 107 VAL HG1 H 1.2189 0.0200 2 945 . 107 VAL HG2 H 1.0954 0.0200 2 946 . 107 VAL H H 8.7596 0.0200 1 947 . 107 VAL N N 120.4020 0.0500 1 948 . 107 VAL C C 177.900 0.0500 1 949 . 108 THR CA C 67.7380 0.0500 1 950 . 108 THR CB C 68.7010 0.0500 1 951 . 108 THR CG2 C 21.0690 0.0500 1 952 . 108 THR HA H 3.8489 0.0200 1 953 . 108 THR HB H 4.4064 0.0200 1 954 . 108 THR HG2 H 1.3239 0.0200 1 955 . 108 THR H H 8.4508 0.0200 1 956 . 108 THR N N 116.6990 0.0500 1 957 . 108 THR C C 176.228 0.0500 1 958 . 109 ALA CA C 55.2767 0.0500 1 959 . 109 ALA CB C 17.8090 0.0500 1 960 . 109 ALA HA H 4.1425 0.0200 1 961 . 109 ALA HB H 1.5713 0.0200 1 962 . 109 ALA H H 7.9484 0.0200 1 963 . 109 ALA N N 123.2760 0.0500 1 964 . 109 ALA C C 180.452 0.0500 1 965 . 110 ARG CA C 58.6280 0.0500 1 966 . 110 ARG CB C 29.8280 0.0500 1 967 . 110 ARG CD C 43.3600 0.0500 1 968 . 110 ARG HA H 4.1600 0.0200 1 969 . 110 ARG HB2 H 2.0495 0.0200 1 970 . 110 ARG HB3 H 2.0495 0.0200 1 971 . 110 ARG HD2 H 3.2473 0.0200 1 972 . 110 ARG HD3 H 3.2473 0.0200 1 973 . 110 ARG HG2 H 1.4830 0.0200 1 974 . 110 ARG HG3 H 1.4830 0.0200 1 975 . 110 ARG H H 7.7794 0.0200 1 976 . 110 ARG N N 119.0710 0.0500 1 977 . 110 ARG C C 178.434 0.0500 1 978 . 111 LEU CA C 58.7510 0.0500 1 979 . 111 LEU CB C 41.5949 0.0500 1 980 . 111 LEU CD1 C 26.4040 0.0500 1 981 . 111 LEU CD2 C 26.4040 0.0500 1 982 . 111 LEU HA H 4.1023 0.0200 1 983 . 111 LEU HB2 H 2.1410 0.0200 2 984 . 111 LEU HB3 H 1.5034 0.0200 2 985 . 111 LEU HD1 H 1.0021 0.0200 1 986 . 111 LEU HD2 H 1.0021 0.0200 1 987 . 111 LEU HG H 1.7170 0.0200 1 988 . 111 LEU H H 8.4697 0.0200 1 989 . 111 LEU N N 120.2590 0.0500 1 990 . 111 LEU C C 177.945 0.0500 1 991 . 112 ARG CA C 59.1080 0.0500 1 992 . 112 ARG CB C 30.0170 0.0500 1 993 . 112 ARG CD C 43.4490 0.0500 1 994 . 112 ARG CG C 27.5807 0.0500 1 995 . 112 ARG HA H 4.1704 0.0200 1 996 . 112 ARG HB2 H 1.9968 0.0200 1 997 . 112 ARG HB3 H 1.9968 0.0200 1 998 . 112 ARG HD2 H 3.2367 0.0200 1 999 . 112 ARG HD3 H 3.2367 0.0200 1 1000 . 112 ARG HG2 H 1.8422 0.0200 2 1001 . 112 ARG HG3 H 1.6850 0.0200 2 1002 . 112 ARG H H 8.1463 0.0200 1 1003 . 112 ARG N N 116.9310 0.0500 1 1004 . 112 ARG C C 178.907 0.0500 1 1005 . 113 GLU CA C 58.8420 0.0500 1 1006 . 113 GLU CB C 29.7970 0.0500 1 1007 . 113 GLU CG C 33.9810 0.0500 1 1008 . 113 GLU HA H 4.1707 0.0200 1 1009 . 113 GLU HB2 H 2.2470 0.0200 1 1010 . 113 GLU HB3 H 2.2470 0.0200 1 1011 . 113 GLU HG2 H 2.5467 0.0200 2 1012 . 113 GLU HG3 H 2.4697 0.0200 2 1013 . 113 GLU H H 7.7110 0.0200 1 1014 . 113 GLU N N 117.6780 0.0500 1 1015 . 113 GLU C C 178.913 0.0500 1 1016 . 114 VAL CA C 64.6960 0.0500 1 1017 . 114 VAL CB C 32.0900 0.0500 1 1018 . 114 VAL CG1 C 21.7310 0.0500 2 1019 . 114 VAL CG2 C 21.7700 0.0500 2 1020 . 114 VAL HA H 3.9892 0.0200 1 1021 . 114 VAL HB H 2.2135 0.0200 1 1022 . 114 VAL HG1 H 1.0836 0.0200 2 1023 . 114 VAL HG2 H 0.9746 0.0200 2 1024 . 114 VAL H H 8.0330 0.0200 1 1025 . 114 VAL N N 116.3180 0.0500 1 1026 . 114 VAL C C 178.062 0.0500 1 1027 . 115 GLU CA C 58.6780 0.0500 1 1028 . 115 GLU CB C 30.1540 0.0500 1 1029 . 115 GLU CG C 37.2644 0.0500 1 1030 . 115 GLU HA H 4.1220 0.0200 1 1031 . 115 GLU HB2 H 1.9850 0.0200 1 1032 . 115 GLU HB3 H 1.9850 0.0200 1 1033 . 115 GLU HG2 H 2.4338 0.0200 2 1034 . 115 GLU HG3 H 2.1355 0.0200 2 1035 . 115 GLU H H 8.4233 0.0200 1 1036 . 115 GLU N N 119.6650 0.0500 1 1037 . 115 GLU C C 177.308 0.0500 1 1038 . 116 HIS CA C 56.4240 0.0500 1 1039 . 116 HIS CB C 28.5960 0.0500 1 1040 . 116 HIS CD2 C 120.0980 0.0500 1 1041 . 116 HIS HA H 4.6413 0.0200 1 1042 . 116 HIS HB2 H 3.3644 0.0200 2 1043 . 116 HIS HB3 H 3.2742 0.0200 2 1044 . 116 HIS HD2 H 7.2787 0.0200 1 1045 . 116 HIS HE1 H 8.4220 0.0200 1 1046 . 116 HIS H H 8.0650 0.0200 1 1047 . 116 HIS N N 117.2170 0.0500 1 1048 . 116 HIS C C 175.353 0.0500 1 1049 . 117 ARG CA C 56.5410 0.0500 1 1050 . 117 ARG CB C 30.6150 0.0500 1 1051 . 117 ARG HA H 4.2938 0.0200 1 1052 . 117 ARG HB2 H 1.9260 0.0200 2 1053 . 117 ARG HB3 H 1.8478 0.0200 2 1054 . 117 ARG HD2 H 3.2440 0.0200 1 1055 . 117 ARG HD3 H 3.2440 0.0200 1 1056 . 117 ARG HG2 H 1.7200 0.0200 1 1057 . 117 ARG HG3 H 1.7200 0.0200 1 1058 . 117 ARG H H 8.1010 0.0200 1 1059 . 117 ARG N N 120.8510 0.0500 1 1060 . 117 ARG C C 176.277 0.0500 1 1061 . 118 ALA CA C 52.7610 0.0500 1 1062 . 118 ALA CB C 19.1040 0.0500 1 1063 . 118 ALA HA H 4.3470 0.0200 1 1064 . 118 ALA HB H 1.4540 0.0200 1 1065 . 118 ALA H H 8.2797 0.0200 1 1066 . 118 ALA N N 123.7870 0.0500 1 1067 . 118 ALA C C 178.096 0.0500 1 1068 . 119 GLY CA C 45.4840 0.0500 1 1069 . 119 GLY HA2 H 3.9922 0.0200 1 1070 . 119 GLY HA3 H 3.9922 0.0200 1 1071 . 119 GLY H H 8.2435 0.0200 1 1072 . 119 GLY N N 127.3420 0.0500 1 1073 . 119 GLY C C 173.361 0.0500 1 1074 . 120 GLU HA H 4.1710 0.0200 1 1075 . 120 GLU HB3 H 1.9260 0.0200 2 1076 . 120 GLU H H 7.8680 0.0200 1 1077 . 120 GLU N N 125.1380 0.0500 1 stop_ save_