data_5862 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of death domain of TRADD ; _BMRB_accession_number 5862 _BMRB_flat_file_name bmr5862.str _Entry_type original _Submission_date 2003-07-08 _Accession_date 2003-07-08 _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 Tsao Desiree 'H. H.' . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 580 "13C chemical shifts" 381 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-13 original author . stop_ _Original_release_date 2004-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the death doamin of TRADD ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14872135 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tsao Desiree 'H. H.' . 2 Hum Wah-Tung . . 3 Hsu Sang . . 4 Mcguire Michelle . . 5 Malakian Karl . . 6 Lin Lih-Ling . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 407 _Page_last 408 _Year 2004 _Details . loop_ _Keyword TNF TRADD 'NMR assignments' stop_ save_ ################################## # Molecular system description # ################################## save_system_TRADD-DD _Saveframe_category molecular_system _Mol_system_name 'TRADD death domain' _Abbreviation_common TRADD-DD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'death domain of TRADD-DD' $TRADD-DD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function Self-association 'binding to TNFR1-DD' 'Rip-DD and FADD-DD' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TRADD-DD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TRADD death domain' _Abbreviation_common TRADD-DD _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; MPPPAQTFLFQGQPVVNRPL SLKDQQTFARSVGLKWRKVG RSLQRGCRALRDPALDSLAY EYEREGLYEQAFQLLRRFVQ AEGRRATLQRLVEALEENEL TSLAEDLLGLTDPNGGLAHH HHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 PRO 4 PRO 5 ALA 6 GLN 7 THR 8 PHE 9 LEU 10 PHE 11 GLN 12 GLY 13 GLN 14 PRO 15 VAL 16 VAL 17 ASN 18 ARG 19 PRO 20 LEU 21 SER 22 LEU 23 LYS 24 ASP 25 GLN 26 GLN 27 THR 28 PHE 29 ALA 30 ARG 31 SER 32 VAL 33 GLY 34 LEU 35 LYS 36 TRP 37 ARG 38 LYS 39 VAL 40 GLY 41 ARG 42 SER 43 LEU 44 GLN 45 ARG 46 GLY 47 CYS 48 ARG 49 ALA 50 LEU 51 ARG 52 ASP 53 PRO 54 ALA 55 LEU 56 ASP 57 SER 58 LEU 59 ALA 60 TYR 61 GLU 62 TYR 63 GLU 64 ARG 65 GLU 66 GLY 67 LEU 68 TYR 69 GLU 70 GLN 71 ALA 72 PHE 73 GLN 74 LEU 75 LEU 76 ARG 77 ARG 78 PHE 79 VAL 80 GLN 81 ALA 82 GLU 83 GLY 84 ARG 85 ARG 86 ALA 87 THR 88 LEU 89 GLN 90 ARG 91 LEU 92 VAL 93 GLU 94 ALA 95 LEU 96 GLU 97 GLU 98 ASN 99 GLU 100 LEU 101 THR 102 SER 103 LEU 104 ALA 105 GLU 106 ASP 107 LEU 108 LEU 109 GLY 110 LEU 111 THR 112 ASP 113 PRO 114 ASN 115 GLY 116 GLY 117 LEU 118 ALA 119 HIS 120 HIS 121 HIS 122 HIS 123 HIS 124 HIS 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 DBJ BAG38020 "unnamed protein product [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 DBJ BAG52211 "unnamed protein product [Homo sapiens]" 94.35 252 100.00 100.00 8.74e-75 DBJ BAJ20315 "TNFRSF1A-associated via death domain [synthetic construct]" 94.35 312 100.00 100.00 2.64e-74 EMBL CAC38018 "TNFRSF1A-associated via death domain, TRADD [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 GB AAA98482 "tumor necrosis factor receptor type 1 associated protein, partial [Homo sapiens]" 94.35 328 100.00 100.00 5.68e-74 GB AAH04491 "TNFRSF1A-associated via death domain [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 GB AAP35580 "TNFRSF1A-associated via death domain [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 GB AAP36466 "Homo sapiens TNFRSF1A-associated via death domain [synthetic construct]" 94.35 313 100.00 100.00 2.41e-74 GB AAS68637 "TNFRSF1A-associated via death domain [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 REF NP_003780 "tumor necrosis factor receptor type 1-associated DEATH domain protein [Homo sapiens]" 94.35 312 100.00 100.00 2.64e-74 REF XP_002802576 "PREDICTED: tumor necrosis factor receptor type 1-associated DEATH domain protein-like [Macaca mulatta]" 94.35 248 99.15 100.00 1.02e-74 REF XP_003262922 "PREDICTED: tumor necrosis factor receptor type 1-associated DEATH domain protein [Nomascus leucogenys]" 94.35 311 99.15 100.00 7.40e-74 REF XP_003812258 "PREDICTED: LOW QUALITY PROTEIN: tumor necrosis factor receptor type 1-associated DEATH domain protein [Pan paniscus]" 94.35 312 100.00 100.00 2.64e-74 REF XP_003917062 "PREDICTED: tumor necrosis factor receptor type 1-associated DEATH domain protein [Papio anubis]" 94.35 308 99.15 100.00 3.90e-74 SP Q15628 "RecName: Full=Tumor necrosis factor receptor type 1-associated DEATH domain protein; Short=TNFR1-associated DEATH domain protei" 94.35 312 100.00 100.00 2.64e-74 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRADD-DD 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 _Vector_name $TRADD-DD 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TRADD-DD . mM 0.6 1.1 [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TRADD-DD . mM 0.6 1.1 '[U-15N; U-13C]' 'Sodium Acetate' 10 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_1H-15N_NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_CC(CO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH-TOCSY _Sample_label . save_ save_HCC(CO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 0.15 n/a temperature 303 1 K 'ionic strength' 0.010 0.0001 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'death domain of TRADD-DD' _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 . 4 PRO CA C 62.9800 0.3 1 2 . 4 PRO HA H 4.4400 0.01 1 3 . 4 PRO CB C 32.1100 0.3 1 4 . 4 PRO HB2 H 2.3500 0.01 1 5 . 4 PRO HB3 H 1.9400 0.01 1 6 . 4 PRO CG C 27.0500 0.3 1 7 . 4 PRO CD C 50.6900 0.3 1 8 . 4 PRO HD2 H 3.8600 0.01 1 9 . 5 ALA H H 8.4100 0.01 1 10 . 5 ALA N N 124.4200 0.25 1 11 . 5 ALA CA C 52.4000 0.3 1 12 . 5 ALA HA H 4.3700 0.01 1 13 . 5 ALA CB C 19.6600 0.3 1 14 . 5 ALA HB H 1.4700 0.01 1 15 . 6 GLN H H 8.6500 0.01 1 16 . 6 GLN N N 120.7100 0.25 1 17 . 6 GLN CA C 56.4600 0.3 1 18 . 6 GLN HA H 4.5000 0.01 1 19 . 6 GLN CB C 29.7600 0.3 1 20 . 6 GLN HB2 H 2.3100 0.01 1 21 . 6 GLN HB3 H 2.1200 0.01 1 22 . 6 GLN CG C 34.1300 0.3 1 23 . 6 GLN HG2 H 2.5000 0.01 1 24 . 6 GLN NE2 N 112.4000 0.25 1 25 . 6 GLN HE21 H 6.9100 0.01 2 26 . 6 GLN HE22 H 7.5400 0.01 2 27 . 7 THR H H 8.0800 0.01 1 28 . 7 THR N N 112.7000 0.25 1 29 . 7 THR CA C 59.8800 0.3 1 30 . 7 THR HA H 5.4400 0.01 1 31 . 7 THR CB C 63.8100 0.3 1 32 . 7 THR HB H 3.9900 0.01 1 33 . 7 THR CG2 C 21.6400 0.3 1 34 . 7 THR HG2 H 1.0500 0.01 1 35 . 8 PHE H H 9.0600 0.01 1 36 . 8 PHE N N 119.2000 0.25 1 37 . 8 PHE CA C 55.3500 0.3 1 38 . 8 PHE HA H 4.9800 0.01 1 39 . 8 PHE CB C 41.2600 0.3 1 40 . 8 PHE HB2 H 3.1800 0.01 1 41 . 8 PHE HB3 H 2.9300 0.01 1 42 . 8 PHE CD1 C 133.4700 0.3 1 43 . 8 PHE HD1 H 7.0700 0.01 1 44 . 8 PHE CD2 C 133.4700 0.3 1 45 . 8 PHE HD2 H 7.0700 0.01 1 46 . 8 PHE CE1 C 130.3000 0.3 1 47 . 8 PHE HE1 H 7.0500 0.01 1 48 . 8 PHE CE2 C 130.3000 0.3 1 49 . 8 PHE HE2 H 7.0500 0.01 1 50 . 8 PHE CZ C 128.3000 0.3 1 51 . 8 PHE HZ H 6.8300 0.01 1 52 . 9 LEU H H 8.5700 0.01 1 53 . 9 LEU N N 120.0700 0.25 1 54 . 9 LEU CA C 54.1100 0.3 1 55 . 9 LEU HA H 4.7500 0.01 1 56 . 9 LEU CB C 44.1900 0.3 1 57 . 9 LEU HB2 H 1.7800 0.01 1 58 . 9 LEU HB3 H 1.1000 0.01 1 59 . 9 LEU CG C 27.2500 0.3 1 60 . 9 LEU CD1 C 25.0000 0.3 2 61 . 9 LEU HD1 H 0.8000 0.01 2 62 . 9 LEU CD2 C 23.0800 0.3 2 63 . 9 LEU HD2 H 0.5500 0.01 2 64 . 9 LEU HG H 1.5300 0.01 1 65 . 10 PHE H H 8.9900 0.01 1 66 . 10 PHE N N 123.6500 0.25 1 67 . 10 PHE CA C 57.4300 0.3 1 68 . 10 PHE HA H 4.7400 0.01 1 69 . 10 PHE CB C 42.0200 0.3 1 70 . 10 PHE HB2 H 2.7900 0.01 1 71 . 10 PHE HB3 H 2.7100 0.01 1 72 . 10 PHE CD1 C 132.5000 0.3 1 73 . 10 PHE HD1 H 7.1900 0.01 1 74 . 10 PHE CD2 C 132.5000 0.3 1 75 . 10 PHE HD2 H 7.1900 0.01 1 76 . 10 PHE CE1 C 131.1000 0.3 1 77 . 10 PHE HE1 H 7.1000 0.01 1 78 . 10 PHE CE2 C 131.1000 0.3 1 79 . 10 PHE HE2 H 7.1000 0.01 1 80 . 10 PHE CZ C 129.2000 0.3 1 81 . 10 PHE HZ H 7.0100 0.01 1 82 . 11 GLN H H 9.1400 0.01 1 83 . 11 GLN N N 126.4400 0.25 1 84 . 11 GLN CA C 56.4700 0.3 1 85 . 11 GLN HA H 3.5500 0.01 1 86 . 11 GLN CB C 25.8500 0.3 1 87 . 11 GLN HB2 H 1.9100 0.01 1 88 . 11 GLN HB3 H 1.6600 0.01 1 89 . 11 GLN CG C 33.4000 0.3 1 90 . 11 GLN HG2 H 1.4900 0.01 1 91 . 11 GLN HG3 H 1.1600 0.01 1 92 . 11 GLN NE2 N 110.8000 0.25 1 93 . 11 GLN HE21 H 6.7600 0.01 2 94 . 11 GLN HE22 H 6.9800 0.01 2 95 . 12 GLY H H 8.3700 0.01 1 96 . 12 GLY N N 102.3100 0.25 1 97 . 12 GLY CA C 45.5000 0.3 1 98 . 12 GLY HA2 H 4.1500 0.01 1 99 . 12 GLY HA3 H 3.5000 0.01 1 100 . 13 GLN H H 7.9200 0.01 1 101 . 13 GLN N N 120.5100 0.25 1 102 . 13 GLN CA C 52.1300 0.3 1 103 . 13 GLN HA H 4.9400 0.01 1 104 . 13 GLN CB C 30.6800 0.3 1 105 . 13 GLN HB2 H 2.1300 0.01 1 106 . 13 GLN CG C 33.3000 0.3 1 107 . 13 GLN HG2 H 2.3400 0.01 1 108 . 13 GLN NE2 N 111.9000 0.25 1 109 . 13 GLN HE21 H 6.8900 0.01 2 110 . 13 GLN HE22 H 7.4700 0.01 2 111 . 14 PRO CA C 62.6100 0.3 1 112 . 14 PRO HA H 4.6600 0.01 1 113 . 14 PRO CB C 31.6900 0.3 1 114 . 14 PRO HB2 H 2.0300 0.01 1 115 . 14 PRO HB3 H 1.7900 0.01 1 116 . 14 PRO HG2 H 2.1800 0.01 1 117 . 14 PRO HG3 H 2.3500 0.01 1 118 . 14 PRO CD C 51.0900 0.3 1 119 . 14 PRO HD2 H 3.7500 0.01 1 120 . 15 VAL H H 9.0100 0.01 1 121 . 15 VAL N N 124.2800 0.25 1 122 . 15 VAL CA C 60.2900 0.3 1 123 . 15 VAL HA H 4.1700 0.01 1 124 . 15 VAL CB C 34.4700 0.3 1 125 . 15 VAL HB H 0.9800 0.01 1 126 . 15 VAL CG1 C 22.8100 0.3 1 127 . 15 VAL HG1 H 0.7600 0.01 1 128 . 15 VAL CG2 C 20.6600 0.3 1 129 . 15 VAL HG2 H 0.3800 0.01 1 130 . 16 VAL H H 8.1900 0.01 1 131 . 16 VAL N N 123.9200 0.25 1 132 . 16 VAL CA C 63.9000 0.3 1 133 . 16 VAL HA H 3.9600 0.01 1 134 . 16 VAL CB C 32.2200 0.3 1 135 . 16 VAL HB H 1.9800 0.01 1 136 . 16 VAL CG1 C 22.3000 0.3 2 137 . 16 VAL HG1 H 1.0000 0.01 2 138 . 16 VAL CG2 C 21.5000 0.3 2 139 . 16 VAL HG2 H 1.0500 0.01 2 140 . 17 ASN H H 8.6900 0.01 1 141 . 17 ASN N N 125.0100 0.25 1 142 . 17 ASN CA C 51.5200 0.3 1 143 . 17 ASN HA H 5.1200 0.01 1 144 . 17 ASN CB C 39.7700 0.3 1 145 . 17 ASN HB2 H 2.6600 0.01 1 146 . 17 ASN HB3 H 3.0700 0.01 1 147 . 17 ASN ND2 N 110.1000 0.25 1 148 . 17 ASN HD21 H 6.3700 0.01 2 149 . 17 ASN HD22 H 7.8500 0.01 2 150 . 18 ARG H H 7.6300 0.01 1 151 . 18 ARG N N 116.2000 0.25 1 152 . 18 ARG CA C 54.0400 0.3 1 153 . 18 ARG HA H 4.9400 0.01 1 154 . 18 ARG CB C 28.7200 0.3 1 155 . 18 ARG HB2 H 1.6300 0.01 1 156 . 18 ARG HB3 H 2.1800 0.01 1 157 . 18 ARG HD2 H 3.6500 0.01 1 158 . 19 PRO CA C 62.7100 0.3 1 159 . 19 PRO HA H 4.5000 0.01 1 160 . 19 PRO HB2 H 2.0300 0.01 1 161 . 19 PRO CG C 32.5000 0.3 1 162 . 19 PRO HG2 H 1.8300 0.01 1 163 . 19 PRO HG3 H 2.4100 0.01 1 164 . 19 PRO CD C 49.0100 0.3 1 165 . 19 PRO HD2 H 3.8300 0.01 1 166 . 19 PRO HD3 H 3.6300 0.01 1 167 . 20 LEU H H 8.0500 0.01 1 168 . 20 LEU N N 121.4000 0.25 1 169 . 20 LEU CA C 55.1400 0.3 1 170 . 20 LEU HA H 4.5000 0.01 1 171 . 20 LEU CB C 43.2900 0.3 1 172 . 20 LEU HB2 H 1.6200 0.01 1 173 . 20 LEU HB3 H 1.2100 0.01 1 174 . 20 LEU CG C 27.4000 0.3 1 175 . 20 LEU CD1 C 24.2500 0.3 2 176 . 20 LEU HD1 H 0.8500 0.01 2 177 . 20 LEU CD2 C 26.9200 0.3 2 178 . 20 LEU HD2 H 0.7900 0.01 2 179 . 20 LEU HG H 1.5500 0.01 1 180 . 21 SER H H 9.8700 0.01 1 181 . 21 SER N N 121.3400 0.25 1 182 . 21 SER CA C 55.8800 0.3 1 183 . 21 SER HA H 4.7900 0.01 1 184 . 21 SER CB C 67.6200 0.3 1 185 . 21 SER HB2 H 4.3900 0.01 1 186 . 21 SER HB3 H 3.9300 0.01 1 187 . 22 LEU H H 8.8000 0.01 1 188 . 22 LEU N N 123.2400 0.25 1 189 . 22 LEU CA C 58.4200 0.3 1 190 . 22 LEU HA H 4.2400 0.01 1 191 . 22 LEU CB C 41.4000 0.3 1 192 . 22 LEU HB2 H 1.7400 0.01 1 193 . 22 LEU CG C 27.5700 0.3 1 194 . 22 LEU CD1 C 24.9400 0.3 2 195 . 22 LEU HD1 H 0.9700 0.01 2 196 . 22 LEU CD2 C 23.6200 0.3 2 197 . 22 LEU HD2 H 1.1500 0.01 2 198 . 22 LEU HG H 1.6300 0.01 1 199 . 23 LYS H H 8.1400 0.01 1 200 . 23 LYS N N 119.3900 0.25 1 201 . 23 LYS CA C 59.6000 0.3 1 202 . 23 LYS HA H 4.2000 0.01 1 203 . 23 LYS CB C 32.1900 0.3 1 204 . 23 LYS HB2 H 1.8700 0.01 1 205 . 23 LYS HB3 H 1.7900 0.01 1 206 . 23 LYS CG C 24.6800 0.3 1 207 . 23 LYS HG2 H 1.5000 0.01 1 208 . 23 LYS CD C 30.2900 0.3 1 209 . 23 LYS CE C 42.5900 0.3 1 210 . 23 LYS HE2 H 3.0200 0.01 1 211 . 24 ASP H H 7.9800 0.01 1 212 . 24 ASP N N 120.5600 0.25 1 213 . 24 ASP CA C 57.7700 0.3 1 214 . 24 ASP HA H 4.1800 0.01 1 215 . 24 ASP CB C 41.9100 0.3 1 216 . 24 ASP HB2 H 3.0600 0.01 1 217 . 24 ASP HB3 H 2.3600 0.01 1 218 . 25 GLN H H 7.7800 0.01 1 219 . 25 GLN N N 116.9200 0.25 1 220 . 25 GLN CA C 59.3200 0.3 1 221 . 25 GLN HA H 3.8700 0.01 1 222 . 25 GLN CB C 29.4100 0.3 1 223 . 25 GLN HB2 H 1.9200 0.01 1 224 . 25 GLN HB3 H 2.4300 0.01 1 225 . 26 GLN H H 8.6000 0.01 1 226 . 26 GLN N N 118.0300 0.25 1 227 . 26 GLN CA C 59.4000 0.3 1 228 . 26 GLN HA H 4.2600 0.01 1 229 . 26 GLN CB C 28.9100 0.3 1 230 . 26 GLN HB2 H 2.4200 0.01 1 231 . 26 GLN HB3 H 2.0900 0.01 1 232 . 26 GLN CG C 34.1700 0.3 1 233 . 26 GLN HG2 H 2.3900 0.01 1 234 . 26 GLN HG3 H 2.8000 0.01 1 235 . 26 GLN NE2 N 110.4200 0.25 1 236 . 26 GLN HE21 H 6.8100 0.01 2 237 . 26 GLN HE22 H 7.1600 0.01 2 238 . 27 THR H H 8.6200 0.01 1 239 . 27 THR N N 117.5300 0.25 1 240 . 27 THR CA C 67.1300 0.3 1 241 . 27 THR HA H 3.8900 0.01 1 242 . 27 THR CB C 68.4500 0.3 1 243 . 27 THR HB H 4.2800 0.01 1 244 . 27 THR CG2 C 21.8000 0.3 1 245 . 27 THR HG2 H 1.1500 0.01 1 246 . 28 PHE H H 8.4000 0.01 1 247 . 28 PHE N N 120.4000 0.25 1 248 . 28 PHE CA C 61.4100 0.3 1 249 . 28 PHE HA H 4.1700 0.01 1 250 . 28 PHE CB C 39.8900 0.3 1 251 . 28 PHE HB2 H 3.3400 0.01 1 252 . 28 PHE HB3 H 3.0000 0.01 1 253 . 28 PHE CD1 C 132.8000 0.3 1 254 . 28 PHE HD1 H 7.0400 0.01 1 255 . 28 PHE CD2 C 132.8000 0.3 1 256 . 28 PHE CE1 C 131.5000 0.3 1 257 . 28 PHE HE2 H 7.4200 0.01 1 258 . 28 PHE CZ C 128.4000 0.3 1 259 . 28 PHE HZ H 7.0500 0.01 1 260 . 29 ALA H H 8.3000 0.01 1 261 . 29 ALA N N 120.7700 0.25 1 262 . 29 ALA CA C 54.7800 0.3 1 263 . 29 ALA HA H 3.6700 0.01 1 264 . 29 ALA CB C 18.5000 0.3 1 265 . 29 ALA HB H 1.1500 0.01 1 266 . 30 ARG H H 8.1500 0.01 1 267 . 30 ARG N N 114.4600 0.25 1 268 . 30 ARG CA C 58.6000 0.3 1 269 . 30 ARG HA H 4.4100 0.01 1 270 . 30 ARG CB C 31.0700 0.3 1 271 . 30 ARG HB2 H 2.1300 0.01 1 272 . 30 ARG HB3 H 2.0200 0.01 1 273 . 30 ARG CG C 28.2600 0.3 1 274 . 30 ARG HG2 H 1.8400 0.01 1 275 . 30 ARG CD C 43.2700 0.3 1 276 . 30 ARG HD2 H 3.2800 0.01 1 277 . 31 SER H H 7.1400 0.01 1 278 . 31 SER N N 110.2200 0.25 1 279 . 31 SER CA C 59.8000 0.3 1 280 . 31 SER HA H 4.7400 0.01 1 281 . 31 SER CB C 66.0000 0.3 1 282 . 31 SER HB2 H 3.8800 0.01 1 283 . 31 SER HB3 H 3.7400 0.01 1 284 . 32 VAL H H 7.9500 0.01 1 285 . 32 VAL N N 121.0000 0.25 1 286 . 32 VAL CA C 64.4500 0.3 1 287 . 32 VAL HA H 3.6900 0.01 1 288 . 32 VAL CB C 31.0900 0.3 1 289 . 32 VAL HB H 1.2400 0.01 1 290 . 32 VAL CG1 C 21.7000 0.3 2 291 . 32 VAL HG1 H 0.4600 0.01 2 292 . 32 VAL CG2 C 22.3000 0.3 2 293 . 32 VAL HG2 H 0.6100 0.01 2 294 . 33 GLY H H 8.0100 0.01 1 295 . 33 GLY N N 111.3700 0.25 1 296 . 33 GLY CA C 46.9300 0.3 1 297 . 33 GLY HA2 H 3.7000 0.01 1 298 . 33 GLY HA3 H 4.0200 0.01 1 299 . 34 LEU H H 9.1100 0.01 1 300 . 34 LEU N N 124.9800 0.25 1 301 . 34 LEU CA C 57.5400 0.3 1 302 . 34 LEU HA H 4.2300 0.01 1 303 . 34 LEU CB C 42.4200 0.3 1 304 . 34 LEU HB2 H 1.7900 0.01 1 305 . 34 LEU HB3 H 1.8600 0.01 1 306 . 34 LEU CD1 C 24.5000 0.3 2 307 . 34 LEU HD1 H 1.0500 0.01 2 308 . 35 LYS H H 7.6600 0.01 1 309 . 35 LYS N N 116.1600 0.25 1 310 . 35 LYS CA C 57.6900 0.3 1 311 . 35 LYS HA H 4.2900 0.01 1 312 . 35 LYS CB C 32.6400 0.3 1 313 . 35 LYS HB2 H 2.0300 0.01 1 314 . 35 LYS CG C 27.2000 0.3 1 315 . 35 LYS HG2 H 1.7700 0.01 1 316 . 35 LYS HG3 H 1.4800 0.01 1 317 . 35 LYS HE2 H 3.1000 0.01 1 318 . 36 TRP H H 8.0600 0.01 1 319 . 36 TRP N N 121.1200 0.25 1 320 . 36 TRP CA C 61.1000 0.3 1 321 . 36 TRP HA H 3.9800 0.01 1 322 . 36 TRP CB C 27.3600 0.3 1 323 . 36 TRP HB2 H 3.3900 0.01 1 324 . 36 TRP HB3 H 3.3100 0.01 1 325 . 36 TRP CD1 C 127.4000 0.3 1 326 . 36 TRP HD1 H 7.6800 0.01 1 327 . 36 TRP NE1 N 129.7300 0.25 1 328 . 36 TRP HE1 H 9.9500 0.01 1 329 . 36 TRP CE3 C 119.5000 0.3 1 330 . 36 TRP HE3 H 7.3600 0.01 1 331 . 36 TRP CZ2 C 114.4700 0.3 1 332 . 36 TRP HZ2 H 7.3500 0.01 1 333 . 36 TRP CZ3 C 121.2000 0.3 1 334 . 36 TRP HZ3 H 6.9300 0.01 1 335 . 36 TRP CH2 C 124.0000 0.3 1 336 . 36 TRP HH2 H 7.3300 0.01 1 337 . 37 ARG H H 6.0100 0.01 1 338 . 37 ARG N N 121.3100 0.25 1 339 . 37 ARG CA C 59.7500 0.3 1 340 . 37 ARG HA H 3.0700 0.01 1 341 . 37 ARG CB C 29.5400 0.3 1 342 . 37 ARG HB2 H 1.2500 0.01 1 343 . 37 ARG HB3 H 0.6900 0.01 1 344 . 37 ARG CG C 27.7000 0.3 1 345 . 37 ARG HG2 H 0.4900 0.01 1 346 . 37 ARG CD C 42.7500 0.3 1 347 . 37 ARG HD2 H 2.7200 0.01 1 348 . 38 LYS H H 7.2000 0.01 1 349 . 38 LYS N N 119.4700 0.25 1 350 . 38 LYS CA C 59.3700 0.3 1 351 . 38 LYS HA H 3.9100 0.01 1 352 . 38 LYS CB C 31.7500 0.3 1 353 . 38 LYS HB2 H 2.0200 0.01 1 354 . 38 LYS HB3 H 1.7200 0.01 1 355 . 38 LYS CG C 25.3800 0.3 1 356 . 38 LYS HG2 H 1.5500 0.01 1 357 . 38 LYS HG3 H 1.4100 0.01 1 358 . 38 LYS HE2 H 3.0200 0.01 1 359 . 39 VAL H H 7.6500 0.01 1 360 . 39 VAL N N 119.1100 0.25 1 361 . 39 VAL CA C 66.9900 0.3 1 362 . 39 VAL HA H 3.5500 0.01 1 363 . 39 VAL CB C 31.5800 0.3 1 364 . 39 VAL HB H 2.2500 0.01 1 365 . 39 VAL CG1 C 21.3000 0.3 1 366 . 39 VAL HG1 H 0.8500 0.01 1 367 . 39 VAL CG2 C 24.2000 0.3 1 368 . 39 VAL HG2 H 1.0100 0.01 1 369 . 40 GLY H H 8.6900 0.01 1 370 . 40 GLY N N 106.8700 0.25 1 371 . 40 GLY CA C 49.0000 0.3 1 372 . 40 GLY HA2 H 3.6400 0.01 1 373 . 41 ARG H H 8.1100 0.01 1 374 . 41 ARG N N 120.7900 0.25 1 375 . 41 ARG CA C 59.6200 0.3 1 376 . 41 ARG HA H 4.0400 0.01 1 377 . 41 ARG CB C 29.5600 0.3 1 378 . 41 ARG HB2 H 1.9200 0.01 1 379 . 41 ARG CD C 43.2700 0.3 1 380 . 41 ARG HD2 H 3.5600 0.01 1 381 . 42 SER H H 7.7300 0.01 1 382 . 42 SER N N 117.1100 0.25 1 383 . 42 SER CA C 63.6400 0.3 1 384 . 42 SER HA H 4.3100 0.01 1 385 . 42 SER CB C 62.7500 0.3 1 386 . 42 SER HB2 H 3.9900 0.01 1 387 . 43 LEU H H 8.0200 0.01 1 388 . 43 LEU N N 120.2700 0.25 1 389 . 43 LEU CA C 56.3300 0.3 1 390 . 43 LEU HA H 4.0100 0.01 1 391 . 43 LEU CB C 41.6700 0.3 1 392 . 43 LEU HB2 H 1.6300 0.01 1 393 . 43 LEU HB3 H 0.8800 0.01 1 394 . 43 LEU CG C 25.9000 0.3 1 395 . 43 LEU CD1 C 24.1800 0.3 1 396 . 43 LEU HD1 H -0.1500 0.01 1 397 . 43 LEU CD2 C 21.3300 0.3 1 398 . 43 LEU HD2 H 0.1000 0.01 1 399 . 43 LEU HG H 1.4400 0.01 1 400 . 44 GLN H H 8.0500 0.01 1 401 . 44 GLN N N 117.7200 0.25 1 402 . 44 GLN CA C 58.3600 0.3 1 403 . 44 GLN HA H 4.0300 0.01 1 404 . 44 GLN CB C 28.9700 0.3 1 405 . 44 GLN HB2 H 2.2900 0.01 1 406 . 44 GLN HB3 H 2.0100 0.01 1 407 . 44 GLN CG C 34.6100 0.3 1 408 . 44 GLN HG2 H 2.6100 0.01 1 409 . 44 GLN HG3 H 2.7900 0.01 1 410 . 45 ARG H H 7.2300 0.01 1 411 . 45 ARG N N 117.9400 0.25 1 412 . 45 ARG CA C 59.4700 0.3 1 413 . 45 ARG HA H 4.0600 0.01 1 414 . 45 ARG CB C 29.8200 0.3 1 415 . 45 ARG HB2 H 1.9000 0.01 1 416 . 45 ARG CD C 43.7700 0.3 1 417 . 45 ARG HD2 H 3.2700 0.01 1 418 . 46 GLY H H 7.6000 0.01 1 419 . 46 GLY N N 105.2100 0.25 1 420 . 46 GLY CA C 45.1200 0.3 1 421 . 46 GLY HA2 H 4.4400 0.01 1 422 . 46 GLY HA3 H 3.7500 0.01 1 423 . 47 CYS H H 7.3600 0.01 1 424 . 47 CYS N N 121.0500 0.25 1 425 . 47 CYS CA C 57.1500 0.3 1 426 . 47 CYS HA H 4.9000 0.01 1 427 . 47 CYS CB C 27.9100 0.3 1 428 . 47 CYS HB2 H 2.7700 0.01 1 429 . 48 ARG H H 9.1000 0.01 1 430 . 48 ARG N N 130.7700 0.25 1 431 . 48 ARG CA C 59.5300 0.3 1 432 . 48 ARG HA H 4.0600 0.01 1 433 . 48 ARG CB C 29.7700 0.3 1 434 . 48 ARG HB2 H 1.9200 0.01 1 435 . 48 ARG CD C 43.4800 0.3 1 436 . 48 ARG HD2 H 3.2600 0.01 1 437 . 49 ALA H H 8.3700 0.01 1 438 . 49 ALA N N 120.7900 0.25 1 439 . 49 ALA CA C 54.1900 0.3 1 440 . 49 ALA HA H 4.2600 0.01 1 441 . 49 ALA CB C 19.3300 0.3 1 442 . 49 ALA HB H 1.4000 0.01 1 443 . 50 LEU H H 7.4700 0.01 1 444 . 50 LEU N N 114.7100 0.25 1 445 . 50 LEU CA C 53.6400 0.3 1 446 . 50 LEU HA H 4.4400 0.01 1 447 . 50 LEU CB C 42.9600 0.3 1 448 . 50 LEU HB2 H 1.5400 0.01 1 449 . 50 LEU HB3 H 1.8200 0.01 1 450 . 50 LEU CG C 27.7000 0.3 1 451 . 50 LEU CD1 C 26.6200 0.3 1 452 . 50 LEU HD1 H 0.8500 0.01 1 453 . 50 LEU CD2 C 22.6900 0.3 1 454 . 50 LEU HD2 H 0.8200 0.01 1 455 . 50 LEU HG H 1.6800 0.01 1 456 . 51 ARG H H 7.4700 0.01 1 457 . 51 ARG N N 120.2400 0.25 1 458 . 51 ARG CA C 57.3600 0.3 1 459 . 51 ARG HA H 4.0600 0.01 1 460 . 51 ARG CB C 30.5000 0.3 1 461 . 51 ARG HB3 H 2.0000 0.01 1 462 . 51 ARG CG C 30.9100 0.3 1 463 . 51 ARG CD C 44.3400 0.3 1 464 . 51 ARG HD2 H 3.2600 0.01 1 465 . 52 ASP H H 8.8600 0.01 1 466 . 52 ASP N N 124.6700 0.25 1 467 . 52 ASP CA C 54.5900 0.3 1 468 . 52 ASP HA H 4.8600 0.01 1 469 . 52 ASP CB C 39.1600 0.3 1 470 . 52 ASP HB2 H 2.5300 0.01 1 471 . 52 ASP HB3 H 2.8100 0.01 1 472 . 53 PRO CA C 64.6100 0.3 1 473 . 53 PRO HA H 5.0500 0.01 1 474 . 53 PRO CB C 32.6700 0.3 1 475 . 53 PRO HB2 H 2.1100 0.01 1 476 . 53 PRO HB3 H 2.7300 0.01 1 477 . 53 PRO CG C 24.8000 0.3 1 478 . 53 PRO HG2 H 1.7000 0.01 1 479 . 53 PRO HG3 H 2.0200 0.01 1 480 . 53 PRO CD C 49.9000 0.3 1 481 . 53 PRO HD2 H 3.5800 0.01 1 482 . 53 PRO HD3 H 3.5000 0.01 1 483 . 54 ALA H H 9.2900 0.01 1 484 . 54 ALA N N 126.6200 0.25 1 485 . 54 ALA CA C 56.4400 0.3 1 486 . 54 ALA HA H 4.1700 0.01 1 487 . 54 ALA CB C 19.6900 0.3 1 488 . 54 ALA HB H 1.5000 0.01 1 489 . 55 LEU H H 7.9400 0.01 1 490 . 55 LEU N N 114.6200 0.25 1 491 . 55 LEU CA C 58.2300 0.3 1 492 . 55 LEU HA H 4.3000 0.01 1 493 . 55 LEU CB C 40.4700 0.3 1 494 . 55 LEU HB2 H 2.0600 0.01 1 495 . 55 LEU HB3 H 1.4100 0.01 1 496 . 55 LEU CG C 27.1000 0.3 1 497 . 55 LEU CD1 C 25.9000 0.3 1 498 . 55 LEU HD1 H 0.8700 0.01 1 499 . 55 LEU CD2 C 24.0400 0.3 1 500 . 55 LEU HD2 H 0.9100 0.01 1 501 . 55 LEU HG H 1.8700 0.01 1 502 . 56 ASP H H 7.7000 0.01 1 503 . 56 ASP N N 119.3000 0.25 1 504 . 56 ASP CA C 57.3700 0.3 1 505 . 56 ASP HA H 4.4500 0.01 1 506 . 56 ASP CB C 40.6100 0.3 1 507 . 56 ASP HB2 H 2.7400 0.01 1 508 . 57 SER H H 8.5000 0.01 1 509 . 57 SER N N 115.9600 0.25 1 510 . 57 SER CA C 61.7000 0.3 1 511 . 57 SER HA H 4.4000 0.01 1 512 . 57 SER CB C 62.7900 0.3 1 513 . 57 SER HB2 H 4.0400 0.01 1 514 . 58 LEU H H 8.1000 0.01 1 515 . 58 LEU N N 123.2500 0.25 1 516 . 58 LEU CA C 58.7300 0.3 1 517 . 58 LEU HA H 4.2600 0.01 1 518 . 58 LEU CB C 43.2900 0.3 1 519 . 58 LEU HB2 H 1.6700 0.01 1 520 . 58 LEU HB3 H 2.2100 0.01 1 521 . 58 LEU CG C 27.1000 0.3 1 522 . 58 LEU CD1 C 24.5800 0.3 2 523 . 58 LEU HD1 H 0.9300 0.01 2 524 . 58 LEU CD2 C 26.4000 0.3 2 525 . 58 LEU HD2 H 0.9000 0.01 2 526 . 58 LEU HG H 1.9200 0.01 1 527 . 59 ALA H H 8.1000 0.01 1 528 . 59 ALA N N 120.2000 0.25 1 529 . 59 ALA CA C 55.3700 0.3 1 530 . 59 ALA HA H 4.1500 0.01 1 531 . 59 ALA CB C 18.5400 0.3 1 532 . 59 ALA HB H 1.8000 0.01 1 533 . 60 TYR H H 8.0100 0.01 1 534 . 60 TYR N N 115.7300 0.25 1 535 . 60 TYR CA C 60.5200 0.3 1 536 . 60 TYR HA H 4.3900 0.01 1 537 . 60 TYR CB C 38.6600 0.3 1 538 . 60 TYR HB2 H 3.1800 0.01 1 539 . 60 TYR HB3 H 3.2500 0.01 1 540 . 60 TYR CD1 C 133.2000 0.3 1 541 . 60 TYR HD2 H 7.1800 0.01 1 542 . 60 TYR CE1 C 118.1000 0.3 1 543 . 60 TYR HE2 H 6.8500 0.01 1 544 . 61 GLU H H 8.5900 0.01 1 545 . 61 GLU N N 119.4800 0.25 1 546 . 61 GLU CA C 58.8600 0.3 1 547 . 61 GLU HA H 3.7600 0.01 1 548 . 61 GLU CB C 29.1500 0.3 1 549 . 61 GLU HB2 H 2.0000 0.01 1 550 . 61 GLU HB3 H 1.5800 0.01 1 551 . 61 GLU CG C 33.9200 0.3 1 552 . 61 GLU HG2 H 2.1900 0.01 1 553 . 62 TYR H H 7.4400 0.01 1 554 . 62 TYR N N 112.6500 0.25 1 555 . 62 TYR CA C 58.0100 0.3 1 556 . 62 TYR HA H 5.0000 0.01 1 557 . 62 TYR CB C 38.2800 0.3 1 558 . 62 TYR HB2 H 2.4400 0.01 1 559 . 62 TYR HB3 H 3.2200 0.01 1 560 . 62 TYR CD1 C 133.4000 0.3 1 561 . 62 TYR HD2 H 7.2400 0.01 1 562 . 62 TYR CE1 C 117.9800 0.3 1 563 . 62 TYR HE2 H 6.7500 0.01 1 564 . 63 GLU H H 7.4700 0.01 1 565 . 63 GLU N N 122.4100 0.25 1 566 . 63 GLU CA C 60.1100 0.3 1 567 . 63 GLU HA H 3.9400 0.01 1 568 . 63 GLU CB C 28.9100 0.3 1 569 . 63 GLU HB2 H 2.4900 0.01 1 570 . 63 GLU HB3 H 2.1200 0.01 1 571 . 63 GLU CG C 34.4600 0.3 1 572 . 64 ARG H H 8.6700 0.01 1 573 . 64 ARG N N 117.2800 0.25 1 574 . 64 ARG CA C 58.2800 0.3 1 575 . 64 ARG HA H 4.1200 0.01 1 576 . 64 ARG CB C 29.6200 0.3 1 577 . 64 ARG HB2 H 1.8400 0.01 1 578 . 64 ARG HG2 H 2.1900 0.01 1 579 . 64 ARG CD C 43.5500 0.3 1 580 . 64 ARG HD2 H 3.2200 0.01 1 581 . 65 GLU H H 8.0000 0.01 1 582 . 65 GLU N N 117.6400 0.25 1 583 . 65 GLU CA C 58.2400 0.3 1 584 . 65 GLU HA H 4.3400 0.01 1 585 . 65 GLU CB C 29.7900 0.3 1 586 . 65 GLU HB2 H 2.1700 0.01 1 587 . 65 GLU HB3 H 2.3300 0.01 1 588 . 65 GLU CG C 36.0900 0.3 1 589 . 65 GLU HG2 H 2.4800 0.01 1 590 . 65 GLU HG3 H 2.6900 0.01 1 591 . 66 GLY H H 7.6500 0.01 1 592 . 66 GLY N N 106.9800 0.25 1 593 . 66 GLY CA C 44.7200 0.3 1 594 . 66 GLY HA2 H 3.8900 0.01 1 595 . 66 GLY HA3 H 4.5600 0.01 1 596 . 67 LEU H H 8.2000 0.01 1 597 . 67 LEU N N 118.7600 0.25 1 598 . 67 LEU CA C 58.4700 0.3 1 599 . 67 LEU HA H 4.0400 0.01 1 600 . 67 LEU CB C 43.0000 0.3 1 601 . 67 LEU HB2 H 1.4700 0.01 1 602 . 67 LEU HB3 H 1.8300 0.01 1 603 . 67 LEU CG C 27.5000 0.3 1 604 . 67 LEU CD1 C 25.7900 0.3 2 605 . 67 LEU HD1 H 1.0500 0.01 2 606 . 67 LEU CD2 C 24.1000 0.3 2 607 . 67 LEU HD2 H 1.0700 0.01 2 608 . 68 TYR H H 8.4800 0.01 1 609 . 68 TYR N N 119.2800 0.25 1 610 . 68 TYR CA C 61.1500 0.3 1 611 . 68 TYR HA H 4.1100 0.01 1 612 . 68 TYR CB C 37.7000 0.3 1 613 . 68 TYR HB2 H 3.0500 0.01 1 614 . 68 TYR CD1 C 133.3000 0.3 1 615 . 68 TYR HD2 H 6.8100 0.01 1 616 . 68 TYR CE1 C 117.7000 0.3 1 617 . 68 TYR HE2 H 6.6100 0.01 1 618 . 69 GLU H H 7.5700 0.01 1 619 . 69 GLU N N 118.9000 0.25 1 620 . 69 GLU CA C 58.7000 0.3 1 621 . 69 GLU HA H 3.8900 0.01 1 622 . 69 GLU CB C 27.5600 0.3 1 623 . 69 GLU HB2 H 1.9000 0.01 1 624 . 69 GLU HB3 H 2.1600 0.01 1 625 . 69 GLU HG2 H 2.5000 0.01 1 626 . 69 GLU HG3 H 2.6900 0.01 1 627 . 70 GLN H H 7.7700 0.01 1 628 . 70 GLN N N 117.0800 0.25 1 629 . 70 GLN CA C 59.8000 0.3 1 630 . 70 GLN HA H 3.0800 0.01 1 631 . 70 GLN CB C 27.3000 0.3 1 632 . 70 GLN HB2 H 1.4500 0.01 1 633 . 70 GLN HB3 H 1.7600 0.01 1 634 . 70 GLN CG C 30.5000 0.3 1 635 . 70 GLN HG2 H 1.7900 0.01 1 636 . 71 ALA H H 7.2900 0.01 1 637 . 71 ALA N N 117.8000 0.25 1 638 . 71 ALA CA C 55.2000 0.3 1 639 . 71 ALA HA H 3.5900 0.01 1 640 . 71 ALA CB C 20.0600 0.3 1 641 . 71 ALA HB H 1.2900 0.01 1 642 . 72 PHE H H 8.6700 0.01 1 643 . 72 PHE N N 118.5000 0.25 1 644 . 72 PHE CA C 61.8000 0.3 1 645 . 72 PHE HA H 3.7900 0.01 1 646 . 72 PHE CB C 39.9000 0.3 1 647 . 72 PHE HB2 H 2.7200 0.01 1 648 . 72 PHE HB3 H 2.5000 0.01 1 649 . 72 PHE CD1 C 131.4000 0.3 1 650 . 72 PHE HD2 H 6.8300 0.01 1 651 . 72 PHE CE1 C 130.9000 0.3 1 652 . 72 PHE HE2 H 7.2000 0.01 1 653 . 72 PHE CZ C 128.5000 0.3 1 654 . 72 PHE HZ H 7.1700 0.01 1 655 . 73 GLN H H 8.5400 0.01 1 656 . 73 GLN N N 116.7000 0.25 1 657 . 73 GLN CA C 57.8000 0.3 1 658 . 73 GLN HA H 3.6600 0.01 1 659 . 73 GLN CB C 26.8000 0.3 1 660 . 73 GLN HB2 H 1.2500 0.01 1 661 . 73 GLN HB3 H 1.3900 0.01 1 662 . 73 GLN CG C 29.4400 0.3 1 663 . 73 GLN HG2 H 1.6900 0.01 1 664 . 73 GLN HG3 H 1.4400 0.01 1 665 . 74 LEU H H 7.8300 0.01 1 666 . 74 LEU N N 121.4000 0.25 1 667 . 74 LEU CA C 58.9000 0.3 1 668 . 74 LEU HA H 3.9300 0.01 1 669 . 74 LEU CB C 40.6000 0.3 1 670 . 74 LEU HB2 H 2.4200 0.01 1 671 . 74 LEU HB3 H 1.6700 0.01 1 672 . 74 LEU CG C 27.5500 0.3 1 673 . 74 LEU CD1 C 26.9000 0.3 2 674 . 74 LEU HD1 H 1.1800 0.01 2 675 . 74 LEU CD2 C 24.9300 0.3 2 676 . 74 LEU HD2 H 1.0400 0.01 2 677 . 75 LEU H H 7.0600 0.01 1 678 . 75 LEU N N 115.1000 0.25 1 679 . 75 LEU CA C 56.5000 0.3 1 680 . 75 LEU HA H 4.0800 0.01 1 681 . 75 LEU CB C 40.8000 0.3 1 682 . 75 LEU HB2 H 1.6700 0.01 1 683 . 75 LEU HB3 H 1.2200 0.01 1 684 . 75 LEU CG C 27.0000 0.3 1 685 . 75 LEU CD1 C 27.5000 0.3 1 686 . 75 LEU HD1 H 0.4000 0.01 1 687 . 75 LEU CD2 C 22.3700 0.3 1 688 . 75 LEU HD2 H 0.2000 0.01 1 689 . 75 LEU HG H 1.5800 0.01 1 690 . 76 ARG H H 8.4300 0.01 1 691 . 76 ARG N N 121.1000 0.25 1 692 . 76 ARG CA C 59.5000 0.3 1 693 . 76 ARG HA H 3.7100 0.01 1 694 . 76 ARG CB C 29.3000 0.3 1 695 . 76 ARG HB2 H 1.4300 0.01 1 696 . 76 ARG HB3 H 1.6800 0.01 1 697 . 76 ARG HG2 H 1.2600 0.01 1 698 . 76 ARG CD C 44.6900 0.3 1 699 . 76 ARG HD2 H 2.9900 0.01 1 700 . 76 ARG HD3 H 2.9000 0.01 1 701 . 77 ARG H H 8.2000 0.01 1 702 . 77 ARG N N 118.5000 0.25 1 703 . 77 ARG CA C 58.7000 0.3 1 704 . 77 ARG HA H 4.0600 0.01 1 705 . 77 ARG CB C 29.2700 0.3 1 706 . 77 ARG HB2 H 1.9900 0.01 1 707 . 77 ARG HB3 H 1.9300 0.01 1 708 . 77 ARG CG C 29.0000 0.3 1 709 . 77 ARG HG2 H 2.1800 0.01 1 710 . 77 ARG CD C 43.0400 0.3 1 711 . 77 ARG HD2 H 3.2100 0.01 1 712 . 78 PHE H H 7.8700 0.01 1 713 . 78 PHE N N 120.1000 0.25 1 714 . 78 PHE CA C 60.4300 0.3 1 715 . 78 PHE HA H 4.3600 0.01 1 716 . 78 PHE CB C 40.1200 0.3 1 717 . 78 PHE HB2 H 3.1000 0.01 1 718 . 78 PHE HB3 H 3.3000 0.01 1 719 . 78 PHE CD1 C 131.9000 0.3 1 720 . 78 PHE HD2 H 7.1500 0.01 1 721 . 78 PHE CE1 C 130.9000 0.3 1 722 . 78 PHE HE2 H 7.1000 0.01 1 723 . 78 PHE CZ C 128.5000 0.3 1 724 . 78 PHE HZ H 7.0100 0.01 1 725 . 79 VAL H H 8.6500 0.01 1 726 . 79 VAL N N 118.8000 0.25 1 727 . 79 VAL CA C 66.1500 0.3 1 728 . 79 VAL HA H 3.2700 0.01 1 729 . 79 VAL CB C 31.7400 0.3 1 730 . 79 VAL HB H 2.0200 0.01 1 731 . 79 VAL CG1 C 23.3000 0.3 2 732 . 79 VAL HG1 H 0.9200 0.01 2 733 . 79 VAL CG2 C 17.8200 0.3 2 734 . 79 VAL HG2 H 0.9600 0.01 2 735 . 80 GLN H H 8.4300 0.01 1 736 . 80 GLN N N 120.5700 0.25 1 737 . 80 GLN CA C 59.0400 0.3 1 738 . 80 GLN HA H 3.9200 0.01 1 739 . 80 GLN CB C 28.6700 0.3 1 740 . 80 GLN HB2 H 2.1200 0.01 1 741 . 80 GLN CG C 34.0200 0.3 1 742 . 81 ALA H H 7.8000 0.01 1 743 . 81 ALA N N 118.6700 0.25 1 744 . 81 ALA CA C 54.4900 0.3 1 745 . 81 ALA HA H 4.1800 0.01 1 746 . 81 ALA CB C 20.1900 0.3 1 747 . 81 ALA HB H 1.4300 0.01 1 748 . 82 GLU H H 7.9900 0.01 1 749 . 82 GLU N N 113.2000 0.25 1 750 . 82 GLU CA C 55.6400 0.3 1 751 . 82 GLU HA H 4.2300 0.01 1 752 . 82 GLU CB C 31.6000 0.3 1 753 . 82 GLU HB2 H 1.6200 0.01 1 754 . 82 GLU HB3 H 1.2900 0.01 1 755 . 82 GLU CG C 37.0000 0.3 1 756 . 82 GLU HG2 H 1.8100 0.01 1 757 . 82 GLU HG3 H 2.1500 0.01 1 758 . 83 GLY H H 8.4100 0.01 1 759 . 83 GLY N N 112.3900 0.25 1 760 . 83 GLY CA C 46.9500 0.3 1 761 . 83 GLY HA2 H 3.8300 0.01 1 762 . 84 ARG H H 9.1000 0.01 1 763 . 84 ARG N N 127.3000 0.25 1 764 . 84 ARG CA C 58.1500 0.3 1 765 . 84 ARG HA H 4.0500 0.01 1 766 . 84 ARG CB C 29.6700 0.3 1 767 . 84 ARG HB2 H 1.8600 0.01 1 768 . 84 ARG CD C 43.5400 0.3 1 769 . 84 ARG HD2 H 3.2300 0.01 1 770 . 85 ARG H H 7.8500 0.01 1 771 . 85 ARG N N 114.3500 0.25 1 772 . 85 ARG CA C 56.6100 0.3 1 773 . 85 ARG HA H 4.2300 0.01 1 774 . 85 ARG CB C 29.3600 0.3 1 775 . 85 ARG HB2 H 1.9800 0.01 1 776 . 85 ARG CD C 43.4800 0.3 1 777 . 85 ARG HD2 H 3.2800 0.01 1 778 . 86 ALA H H 7.9800 0.01 1 779 . 86 ALA N N 127.0600 0.25 1 780 . 86 ALA CA C 51.0000 0.3 1 781 . 86 ALA HA H 4.0300 0.01 1 782 . 86 ALA CB C 17.6500 0.3 1 783 . 86 ALA HB H 0.9400 0.01 1 784 . 87 THR H H 7.0500 0.01 1 785 . 87 THR N N 111.8000 0.25 1 786 . 87 THR CA C 59.8400 0.3 1 787 . 87 THR HA H 4.7100 0.01 1 788 . 87 THR CB C 71.8700 0.3 1 789 . 87 THR HB H 4.0000 0.01 1 790 . 87 THR CG2 C 22.3000 0.3 1 791 . 87 THR HG2 H 1.0600 0.01 1 792 . 88 LEU H H 8.8800 0.01 1 793 . 88 LEU N N 120.7900 0.25 1 794 . 88 LEU CA C 57.8900 0.3 1 795 . 88 LEU HA H 4.0300 0.01 1 796 . 88 LEU CB C 43.8400 0.3 1 797 . 88 LEU HB2 H 2.1500 0.01 1 798 . 88 LEU HB3 H 1.6200 0.01 1 799 . 88 LEU CD1 C 26.3500 0.3 2 800 . 88 LEU HD1 H 0.8500 0.01 1 801 . 88 LEU CD2 C 22.5500 0.3 2 802 . 88 LEU HD2 H 0.8500 0.01 1 803 . 89 GLN H H 8.2600 0.01 1 804 . 89 GLN N N 116.7500 0.25 1 805 . 89 GLN CA C 59.5400 0.3 1 806 . 89 GLN HA H 2.6500 0.01 1 807 . 89 GLN CB C 28.3200 0.3 1 808 . 89 GLN HB2 H 0.9300 0.01 1 809 . 89 GLN HB3 H 1.4100 0.01 1 810 . 89 GLN CG C 32.0900 0.3 1 811 . 89 GLN HG2 H 1.6800 0.01 1 812 . 89 GLN HG3 H 1.3400 0.01 1 813 . 89 GLN NE2 N 110.7000 0.25 1 814 . 89 GLN HE21 H 6.6600 0.01 2 815 . 89 GLN HE22 H 7.4500 0.01 2 816 . 90 ARG H H 7.1200 0.01 1 817 . 90 ARG N N 115.3000 0.25 1 818 . 90 ARG CA C 58.9000 0.3 1 819 . 90 ARG HA H 3.9400 0.01 1 820 . 90 ARG CB C 31.3900 0.3 1 821 . 90 ARG HB2 H 1.9400 0.01 1 822 . 90 ARG CG C 28.6500 0.3 1 823 . 90 ARG CD C 45.3600 0.3 1 824 . 90 ARG HD2 H 3.4000 0.01 1 825 . 90 ARG HD3 H 3.5600 0.01 1 826 . 91 LEU H H 7.5200 0.01 1 827 . 91 LEU N N 118.4000 0.25 1 828 . 91 LEU CA C 57.6500 0.3 1 829 . 91 LEU HA H 3.9900 0.01 1 830 . 91 LEU CB C 42.7200 0.3 1 831 . 91 LEU HB2 H 1.9700 0.01 1 832 . 91 LEU HB3 H 1.1500 0.01 1 833 . 91 LEU CG C 24.5000 0.3 1 834 . 91 LEU CD1 C 22.7000 0.3 1 835 . 91 LEU HD1 H 0.4400 0.01 1 836 . 91 LEU CD2 C 27.5200 0.3 1 837 . 91 LEU HD2 H 0.6500 0.01 1 838 . 91 LEU HG H 1.1300 0.01 1 839 . 92 VAL H H 8.9600 0.01 1 840 . 92 VAL N N 118.9300 0.25 1 841 . 92 VAL CA C 67.8800 0.3 1 842 . 92 VAL HA H 3.4400 0.01 1 843 . 92 VAL CB C 31.1400 0.3 1 844 . 92 VAL HB H 2.1200 0.01 1 845 . 92 VAL CG1 C 27.1000 0.3 1 846 . 92 VAL HG1 H 0.8700 0.01 1 847 . 92 VAL CG2 C 22.4800 0.3 1 848 . 92 VAL HG2 H 1.0200 0.01 1 849 . 93 GLU H H 8.3900 0.01 1 850 . 93 GLU N N 119.4700 0.25 1 851 . 93 GLU CA C 59.9600 0.3 1 852 . 93 GLU HA H 4.1700 0.01 1 853 . 93 GLU CB C 28.9600 0.3 1 854 . 93 GLU HB2 H 2.0500 0.01 1 855 . 93 GLU CG C 34.5000 0.3 1 856 . 94 ALA H H 7.2400 0.01 1 857 . 94 ALA N N 120.9200 0.25 1 858 . 94 ALA CA C 55.0500 0.3 1 859 . 94 ALA HA H 4.1700 0.01 1 860 . 94 ALA CB C 18.8300 0.3 1 861 . 94 ALA HB H 1.4500 0.01 1 862 . 95 LEU H H 8.5400 0.01 1 863 . 95 LEU N N 119.7500 0.25 1 864 . 95 LEU CA C 58.4600 0.3 1 865 . 95 LEU HA H 4.0900 0.01 1 866 . 95 LEU CB C 40.0800 0.3 1 867 . 95 LEU HB2 H 2.2300 0.01 1 868 . 95 LEU HB3 H 1.6600 0.01 1 869 . 95 LEU CG C 26.8200 0.3 1 870 . 95 LEU CD1 C 26.8400 0.3 1 871 . 95 LEU HD1 H 0.8600 0.01 1 872 . 95 LEU CD2 C 24.2100 0.3 1 873 . 95 LEU HD2 H 1.1000 0.01 1 874 . 95 LEU HG H 2.1500 0.01 1 875 . 96 GLU H H 8.9400 0.01 1 876 . 96 GLU N N 121.3100 0.25 1 877 . 96 GLU CA C 59.8000 0.3 1 878 . 96 GLU HA H 4.0200 0.01 1 879 . 96 GLU CB C 29.8000 0.3 1 880 . 96 GLU HB2 H 2.4000 0.01 1 881 . 96 GLU HB3 H 2.2300 0.01 1 882 . 96 GLU CG C 35.0700 0.3 1 883 . 96 GLU HG2 H 2.7600 0.01 1 884 . 96 GLU HG3 H 2.5500 0.01 1 885 . 97 GLU H H 7.9800 0.01 1 886 . 97 GLU N N 118.7000 0.25 1 887 . 97 GLU CA C 58.4000 0.3 1 888 . 97 GLU HA H 4.2200 0.01 1 889 . 97 GLU CB C 29.8000 0.3 1 890 . 97 GLU HB2 H 2.1600 0.01 1 891 . 97 GLU CG C 36.4800 0.3 1 892 . 97 GLU HG2 H 2.5500 0.01 1 893 . 98 ASN H H 7.1500 0.01 1 894 . 98 ASN N N 114.8000 0.25 1 895 . 98 ASN CA C 53.8000 0.3 1 896 . 98 ASN HA H 4.9500 0.01 1 897 . 98 ASN CB C 40.9000 0.3 1 898 . 98 ASN HB2 H 2.3100 0.01 1 899 . 98 ASN HB3 H 2.8800 0.01 1 900 . 99 GLU H H 7.9600 0.01 1 901 . 99 GLU N N 112.5000 0.25 1 902 . 99 GLU CA C 57.9000 0.3 1 903 . 99 GLU HA H 4.1100 0.01 1 904 . 99 GLU CB C 26.4600 0.3 1 905 . 99 GLU HB2 H 2.2500 0.01 1 906 . 99 GLU CG C 36.0300 0.3 1 907 . 100 LEU H H 8.0600 0.01 1 908 . 100 LEU N N 120.9000 0.25 1 909 . 100 LEU CA C 53.4200 0.3 1 910 . 100 LEU HA H 5.0100 0.01 1 911 . 100 LEU CB C 41.4400 0.3 1 912 . 100 LEU HB2 H 1.8100 0.01 1 913 . 100 LEU HB3 H 1.7100 0.01 1 914 . 100 LEU CG C 25.9000 0.3 1 915 . 100 LEU CD1 C 23.8300 0.3 1 916 . 100 LEU HD1 H 0.9900 0.01 1 917 . 100 LEU CD2 C 28.3500 0.3 1 918 . 100 LEU HD2 H 0.8700 0.01 1 919 . 100 LEU HG H 1.7000 0.01 1 920 . 101 THR H H 7.6800 0.01 1 921 . 101 THR N N 116.7200 0.25 1 922 . 101 THR CA C 67.3000 0.3 1 923 . 101 THR HA H 3.8300 0.01 1 924 . 101 THR CB C 68.3000 0.3 1 925 . 101 THR HB H 4.1700 0.01 1 926 . 101 THR CG2 C 23.2200 0.3 1 927 . 101 THR HG2 H 1.3500 0.01 1 928 . 102 SER H H 8.7500 0.01 1 929 . 102 SER N N 117.0000 0.25 1 930 . 102 SER CA C 61.8500 0.3 1 931 . 102 SER HA H 4.2700 0.01 1 932 . 102 SER CB C 68.3000 0.3 1 933 . 102 SER HB2 H 3.9500 0.01 1 934 . 103 LEU H H 7.4100 0.01 1 935 . 103 LEU N N 124.5600 0.25 1 936 . 103 LEU CA C 57.4700 0.3 1 937 . 103 LEU HA H 4.3700 0.01 1 938 . 103 LEU CB C 41.7700 0.3 1 939 . 103 LEU HB2 H 1.7200 0.01 1 940 . 103 LEU HB3 H 1.9700 0.01 1 941 . 103 LEU CG C 28.2100 0.3 1 942 . 103 LEU CD1 C 25.6600 0.3 2 943 . 103 LEU HD1 H 0.9900 0.01 2 944 . 103 LEU CD2 C 23.9200 0.3 2 945 . 103 LEU HD2 H 1.0500 0.01 2 946 . 103 LEU HG H 1.7500 0.01 1 947 . 104 ALA H H 7.7900 0.01 1 948 . 104 ALA N N 121.1000 0.25 1 949 . 104 ALA CA C 55.8300 0.3 1 950 . 104 ALA HA H 3.7800 0.01 1 951 . 104 ALA CB C 18.3300 0.3 1 952 . 104 ALA HB H 1.4900 0.01 1 953 . 105 GLU H H 8.3800 0.01 1 954 . 105 GLU N N 115.2600 0.25 1 955 . 105 GLU CA C 60.1800 0.3 1 956 . 105 GLU HA H 3.6600 0.01 1 957 . 105 GLU CB C 28.4500 0.3 1 958 . 105 GLU HB2 H 2.4200 0.01 1 959 . 105 GLU HB3 H 2.0700 0.01 1 960 . 105 GLU CG C 35.0000 0.3 1 961 . 106 ASP H H 7.8400 0.01 1 962 . 106 ASP N N 119.8300 0.25 1 963 . 106 ASP CA C 57.0800 0.3 1 964 . 106 ASP HA H 4.4700 0.01 1 965 . 106 ASP CB C 40.3800 0.3 1 966 . 106 ASP HB2 H 2.8600 0.01 1 967 . 106 ASP HB3 H 3.0400 0.01 1 968 . 107 LEU H H 8.2300 0.01 1 969 . 107 LEU N N 120.2000 0.25 1 970 . 107 LEU CA C 57.8000 0.3 1 971 . 107 LEU HA H 4.0600 0.01 1 972 . 107 LEU CB C 42.5000 0.3 1 973 . 107 LEU HB2 H 1.8900 0.01 1 974 . 107 LEU HB3 H 1.3700 0.01 1 975 . 107 LEU CG C 24.0600 0.3 1 976 . 107 LEU CD1 C 27.4700 0.3 1 977 . 107 LEU HD1 H 0.8100 0.01 1 978 . 107 LEU CD2 C 24.9600 0.3 1 979 . 107 LEU HD2 H 0.9700 0.01 1 980 . 108 LEU H H 7.7200 0.01 1 981 . 108 LEU N N 116.2000 0.25 1 982 . 108 LEU CA C 55.4200 0.3 1 983 . 108 LEU HA H 4.1500 0.01 1 984 . 108 LEU CB C 42.6900 0.3 1 985 . 108 LEU HB2 H 1.5100 0.01 1 986 . 108 LEU HB3 H 1.6100 0.01 1 987 . 108 LEU CG C 27.0300 0.3 1 988 . 108 LEU CD1 C 25.6300 0.3 2 989 . 108 LEU HD1 H 0.2100 0.01 2 990 . 108 LEU CD2 C 24.1300 0.3 2 991 . 108 LEU HD2 H 0.7800 0.01 2 992 . 108 LEU HG H 1.6700 0.01 1 993 . 109 GLY H H 7.8700 0.01 1 994 . 109 GLY N N 108.3000 0.25 1 995 . 109 GLY CA C 46.4600 0.3 1 996 . 109 GLY HA2 H 4.0300 0.01 1 997 . 110 LEU H H 8.0100 0.01 1 998 . 110 LEU N N 119.3600 0.25 1 999 . 110 LEU CA C 54.8000 0.3 1 1000 . 110 LEU HA H 4.4400 0.01 1 1001 . 110 LEU CB C 42.7000 0.3 1 1002 . 110 LEU HB2 H 1.6200 0.01 1 1003 . 110 LEU CG C 26.7500 0.3 1 1004 . 110 LEU CD1 C 26.2900 0.3 2 1005 . 110 LEU HD1 H 0.8800 0.01 2 1006 . 110 LEU CD2 C 22.7500 0.3 2 1007 . 110 LEU HD2 H 0.8600 0.01 2 1008 . 110 LEU HG H 1.5600 0.01 1 1009 . 111 THR H H 7.7700 0.01 1 1010 . 111 THR N N 112.6500 0.25 1 1011 . 111 THR CA C 61.5000 0.3 1 1012 . 111 THR HA H 4.2800 0.01 1 1013 . 111 THR CB C 69.9000 0.3 1 1014 . 111 THR HB H 4.1700 0.01 1 1015 . 111 THR CG2 C 22.1600 0.3 1 1016 . 111 THR HG2 H 1.1300 0.01 1 1017 . 112 ASP H H 8.3200 0.01 1 1018 . 112 ASP N N 123.7200 0.25 1 1019 . 112 ASP CA C 52.0700 0.3 1 1020 . 112 ASP HA H 4.9000 0.01 1 1021 . 112 ASP CB C 41.5900 0.3 1 1022 . 112 ASP HB2 H 2.8000 0.01 1 1023 . 112 ASP HB3 H 2.6600 0.01 1 1024 . 113 PRO CA C 64.2000 0.3 1 1025 . 113 PRO HA H 4.4200 0.01 1 1026 . 113 PRO CB C 32.1000 0.3 1 1027 . 113 PRO HB2 H 2.3100 0.01 1 1028 . 113 PRO HB3 H 1.9600 0.01 1 1029 . 113 PRO CD C 51.2000 0.3 1 1030 . 113 PRO HD2 H 3.8600 0.01 1 1031 . 114 ASN H H 8.4900 0.01 1 1032 . 114 ASN N N 116.7800 0.25 1 1033 . 114 ASN CA C 53.5000 0.3 1 1034 . 114 ASN HA H 4.7600 0.01 1 1035 . 114 ASN CB C 39.0300 0.3 1 1036 . 114 ASN HB2 H 2.7700 0.01 1 1037 . 114 ASN HB3 H 2.8900 0.01 1 1038 . 114 ASN ND2 N 113.9000 0.25 1 1039 . 114 ASN HD21 H 6.9400 0.01 2 1040 . 114 ASN HD22 H 7.7300 0.01 2 1041 . 115 GLY H H 8.0800 0.01 1 1042 . 115 GLY N N 108.7000 0.25 1 1043 . 115 GLY CA C 46.0200 0.3 1 1044 . 115 GLY HA2 H 3.9600 0.01 1 1045 . 116 GLY H H 8.2900 0.01 1 1046 . 116 GLY N N 108.6000 0.25 1 1047 . 116 GLY CA C 45.7500 0.3 1 1048 . 116 GLY HA2 H 3.9600 0.01 1 1049 . 117 LEU H H 8.1100 0.01 1 1050 . 117 LEU N N 121.4000 0.25 1 1051 . 117 LEU CA C 55.8100 0.3 1 1052 . 117 LEU HA H 4.2200 0.01 1 1053 . 117 LEU CB C 42.2300 0.3 1 1054 . 117 LEU HB2 H 1.5800 0.01 1 1055 . 117 LEU CG C 26.6700 0.3 1 1056 . 117 LEU CD1 C 24.6400 0.3 2 1057 . 117 LEU HD1 H 0.8700 0.01 1 1058 . 117 LEU CD2 C 23.5800 0.3 2 1059 . 117 LEU HD2 H 0.8700 0.01 1 1060 . 118 ALA H H 8.1000 0.01 1 1061 . 118 ALA N N 122.6000 0.25 1 1062 . 118 ALA CA C 53.0100 0.3 1 1063 . 118 ALA HA H 4.1600 0.01 1 1064 . 118 ALA CB C 18.9100 0.3 1 1065 . 118 ALA HB H 1.2600 0.01 1 1066 . 119 HIS H H 8.1800 0.01 1 1067 . 119 HIS N N 115.8000 0.25 1 1068 . 119 HIS CA C 55.3000 0.3 1 1069 . 119 HIS HA H 4.5900 0.01 1 1070 . 119 HIS CB C 28.7200 0.3 1 1071 . 119 HIS HB2 H 3.1600 0.01 1 1072 . 120 HIS H H 8.2900 0.01 1 1073 . 120 HIS N N 118.3900 0.25 1 1074 . 120 HIS CA C 55.3900 0.3 1 1075 . 120 HIS CB C 29.1600 0.3 1 1076 . 121 HIS H H 7.3300 0.01 1 1077 . 121 HIS N N 119.8500 0.25 1 1078 . 121 HIS CA C 59.4500 0.3 1 1079 . 121 HIS CB C 31.8300 0.3 1 1080 . 122 HIS H H 7.7400 0.01 1 1081 . 122 HIS N N 119.0000 0.25 1 1082 . 122 HIS CA C 66.9800 0.3 1 1083 . 122 HIS CB C 31.5800 0.3 1 stop_ save_