data_5507 #Corrected using PDB structure: 2B9AA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 11 C CA 50.73 59.16 # 90 E CA 53.35 59.67 #114 P CA 56.05 65.25 #121 A CA 55.66 50.17 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted #105 R N 105.94 116.37 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 0.36 N/A N/A -0.07 0.07 # #bmr5507.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5507.str file): #HA CA CB CO N HN #N/A +0.36 N/A N/A -0.07 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.15 N/A N/A +/-0.33 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.925 N/A N/A 0.900 0.755 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.748 N/A N/A 1.654 0.270 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Kai . . 2 Kelly Jeffery . . 3 Wemmer David . . stop_ _BMRB_accession_number 5507 _BMRB_flat_file_name bmr5507.str _Entry_type new _Submission_date 2002-08-25 _Accession_date 2002-08-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 121 '15N chemical shifts' 121 '13C chemical shifts' 128 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 22090787 _PubMed_ID 12095258 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Kai . . 2 Kelly Jeffery . . 3 Wemmer David . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 320 _Journal_issue 4 _Page_first 821 _Page_last 832 _Year 2002 loop_ _Keyword "transthyretin" "amyloid" "hydrogen exchange" "NMR spectroscopy" "protection factor" stop_ save_ ################################## # Molecular system description # ################################## save_system_TTR _Saveframe_category molecular_system _Mol_system_name "Transthyretin Tetramer" _Abbreviation_common TTR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "TTR subunit 1" $TTR "TTR subunit 2" $TTR "TTR subunit 3" $TTR "TTR subunit 4" $TTR stop_ _System_physical_state native _System_oligomer_state tetramer _System_paramagnetic no _System_thiol_state "all free" loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "TTR subunit 1" 1 "TTR subunit 2" 1 "TTR subunit 3" 1 "TTR subunit 4" stop_ save_ ######################## # Monomeric polymers # ######################## save_TTR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Transthyretin _Name_variant . _Abbreviation_common TTR _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; MGPTGTGESKCPLMVKVLDA VRGSPAINVAVHVFRKAADD TWEPFASGKTSESGELHGLT TEEEFVEGIYKVEIDTKSYW KALGISPFHEHAEVVFTAND SGPRRYTIAALLSPYSYSTT AVVTNPKE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 PRO 4 THR 5 GLY 6 THR 7 GLY 8 GLU 9 SER 10 LYS 11 CYS 12 PRO 13 LEU 14 MET 15 VAL 16 LYS 17 VAL 18 LEU 19 ASP 20 ALA 21 VAL 22 ARG 23 GLY 24 SER 25 PRO 26 ALA 27 ILE 28 ASN 29 VAL 30 ALA 31 VAL 32 HIS 33 VAL 34 PHE 35 ARG 36 LYS 37 ALA 38 ALA 39 ASP 40 ASP 41 THR 42 TRP 43 GLU 44 PRO 45 PHE 46 ALA 47 SER 48 GLY 49 LYS 50 THR 51 SER 52 GLU 53 SER 54 GLY 55 GLU 56 LEU 57 HIS 58 GLY 59 LEU 60 THR 61 THR 62 GLU 63 GLU 64 GLU 65 PHE 66 VAL 67 GLU 68 GLY 69 ILE 70 TYR 71 LYS 72 VAL 73 GLU 74 ILE 75 ASP 76 THR 77 LYS 78 SER 79 TYR 80 TRP 81 LYS 82 ALA 83 LEU 84 GLY 85 ILE 86 SER 87 PRO 88 PHE 89 HIS 90 GLU 91 HIS 92 ALA 93 GLU 94 VAL 95 VAL 96 PHE 97 THR 98 ALA 99 ASN 100 ASP 101 SER 102 GLY 103 PRO 104 ARG 105 ARG 106 TYR 107 THR 108 ILE 109 ALA 110 ALA 111 LEU 112 LEU 113 SER 114 PRO 115 TYR 116 SER 117 TYR 118 SER 119 THR 120 THR 121 ALA 122 VAL 123 VAL 124 THR 125 ASN 126 PRO 127 LYS 128 GLU stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1F86 "A Chain A, Transthyretin Thr119met ProteinStabilisation" 111.30 115 99 99 8e-61 PDB 1FH2 "A Chain A, Transthyretin Stability As A KeyFactor In Amyloidogenesis" 110.34 116 98 98 5e-58 PDB 1QAB "B Chain B, The Structure Of Human RetinolBinding Protein With Its Carrier Protein TransthyretinReveals Interaction With The Carboxy Terminus Of Rbp" 108.47 118 99 100 4e-63 PDB 1DVQ "A Chain A, Crystal Structure Of HumanTransthyretin" 103.23 124 99 100 7e-67 PDB 1DVS "A Chain A, Crystal Structure Of HumanTransthyretin In Complex With Resveratrol" 103.23 124 99 100 7e-67 PDB 1DVT "A Chain A, Crystal Structure Of HumanTransthyretin In Complex With Flurbiprofen" 103.23 124 99 100 7e-67 PDB 1DVU "A Chain A, Crystal Structure Of HumanTransthyretin In Complex WithDibenzofuran-4,6-Dicarboxylic Acid" 103.23 124 99 100 7e-67 PDB 1DVX "A Chain A, Crystal Structure Of HumanTransthyretin In Complex With Diclofenac" 103.23 124 99 100 7e-67 PDB 1DVY "A Chain A, Crystal Structure Of TransthyretinIn Complex With N-(M- Trifluoromethylphenyl)Phenoxazine-4,6-Dicarboxylic Acid" 103.23 124 99 100 7e-67 PDB 1DVZ "A Chain A, Crystal Structure Of HumanTransthyretin In Complex With O- TrifluoromethylphenylAnthranilic Acid" 103.23 124 99 100 7e-67 PDB 1QAB "A Chain A, The Structure Of Human RetinolBinding Protein With Its Carrier Protein TransthyretinReveals Interaction With The Carboxy Terminus Of Rbp" 103.23 124 99 100 7e-67 PDB 1BZ8 "A Chain A, Transthyretin (Del Val122)" 101.59 126 99 99 2e-67 PDB 1BM7 "A Chain A, Human Transthyretin (Prealbumin)Complex With Flufenamic Acid(2-[[3-(Trifluoromethyl)phenyl]amino] Benzoic Acid)" 100.79 127 100 100 3e-69 PDB 1BMZ "A Chain A, Human Transthyretin (Prealbumin)" 100.79 127 100 100 3e-69 PDB 1E3F "A Chain A, Structure Of Human TransthyretinComplexed With Bromophenols: A New Mode Of Binding" 100.79 127 100 100 3e-69 PDB 1E4H "A Chain A, Structure Of Human TransthyretinComplexed With Bromophenols: A New Mode Of Binding" 100.79 127 100 100 3e-69 PDB 1E5A "A Chain A, Structure Of Human TransthyretinComplexed With Bromophenols: A New Mode Of Binding" 100.79 127 100 100 3e-69 PDB 1F41 "A Chain A, Crystal Structure Of HumanTransthyretin At 1.5a Resolution" 100.79 127 100 100 3e-69 PDB 1ICT "A Chain A, Monoclinic Form Of HumanTransthyretin Complexed With Thyroxine (T4)" 100.79 127 100 100 3e-69 PDB 1KED "A Chain A, Human Transthyretin (Also CalledPrealbumin) Complex With 3, 3',5,5'-TetraiodothyroaceticAcid (T4ac)" 100.79 127 100 100 3e-69 PDB 1TTA "A Chain A, Transthyretin (Formerly Prealbumin)" 100.79 127 100 100 3e-69 PDB 1TYR "A Chain A, Transthyretin Complex With RetinoicAcid" 100.79 127 100 100 3e-69 PDB 2ROX "A Chain A, Transthyretin (Also CalledPrealbumin) Complex With Thyroxine (T4)" 100.79 127 100 100 3e-69 PDB 2ROY "A Chain A, Transthyretin (Also CalledPrealbumin) Complex With3',5'-Dinitro-N-Acetyl-L-Thyronine" 100.79 127 100 100 3e-69 PDB 1BZD "A Chain A, Tertiary Structures Of ThreeAmyloidogenic Transthyretin Variants And ImplicationsFor Amyloid Fibril Formation" 100.79 127 99 99 2e-68 PDB 1BZE "A Chain A, Tertiary Structures Of ThreeAmyloidogenic Transthyretin Variants And ImplicationsFor Amyloid Fibril Formation" 100.79 127 99 99 2e-68 PDB 1ETB "1 Chain 1, The X-Ray Crystal StructureRefinements Of Normal Human Transthyretin And TheAmyloidogenic Val 30-->met Variant" 100.79 127 99 99 10e-69 PDB 1FHN "A Chain A, Transthyretin Stability As A KeyFactor In Amyloidogenesis" 100.79 127 99 99 2e-68 PDB 1III "A Chain A, Crystal Structure Of TheTransthyretin Mutant Ttr Y114c- Data Collected At RoomTemperature" 100.79 127 99 99 4e-68 PDB 1IIK "A Chain A, Crystal Structure Of TheTransthyretin Mutant Ttr Y114c- Data Collected At CryoTemperature" 100.79 127 99 99 4e-68 PDB 1RLB "A Chain A, Retinol Binding Protein ComplexedWith Transthyretin" 100.79 127 99 100 8e-69 PDB 1THA "A Chain A, Transthyretin (Also CalledPrealbumin) Complex With 3,3'-Diiodo-L-Thyronine" 100.79 127 99 100 8e-69 PDB 1THC "A Chain A, Transthyretin (Also CalledPrealbumin) Complex With3',5'-Dibromo-2',4,4',6-Tetra-Hydroxyaurone" 100.79 127 99 100 8e-69 PDB 1TLM "A Chain A, Transthyretin (Also CalledPrealbumin) Complex With Milrinone" 100.79 127 99 100 8e-69 PDB 1TSH "A Chain A, Tertiary Structures Of ThreeAmyloidogenic Transthyretin Variants And ImplicationsFor Amyloid Fibril Formation" 100.79 127 99 99 10e-69 PDB 1TTB "A Chain A, Transthyretin (Formerly Prealbumin)Mutant With Ala 109 Replaced By Thr (A109t)" 100.79 127 99 99 10e-69 PDB 1TTC "A Chain A, Transthyretin (Formerly Prealbumin)Mutant With Val 30 Replaced By Met (V30m)" 100.79 127 99 100 8e-69 PDB 1TTR "A Chain A, Transthyretin - V122ICARDIOMYOPATHIC MUTANT" 100.79 127 99 100 4e-69 PDB 2PAB "A Chain A, Prealbumin (Human Plasma)" 100.79 127 99 100 8e-69 PDB 2TRH "A Chain A, Tertiary Structures Of ThreeAmyloidogenic Transthyretin Variants And ImplicationsFor Amyloid Fibril Formation" 100.79 127 99 99 8e-68 PDB 2TRY "A Chain A, Tertiary Structures Of ThreeAmyloidogenic Transthyretin Variants And ImplicationsFor Amyloid Fibril Formation" 100.79 127 99 99 2e-68 PDB 5TTR "A Chain A, Leu 55 Pro Transthyretin CrystalStructure" 100.79 127 99 99 2e-68 PDB 1GKO "A Chain A, An Engineered Transthyretin MonomerThat Is Non-Amyloidogenic - Unless Partially Denatured" 100.79 127 98 99 3e-68 PDB 1IJN "A Chain A, Crystal Structure Of TheTransthyretin Mutant Ttr C10aY114C" 100.79 127 98 98 4e-67 PDB 1G1O "A Chain A, Crystal Structure Of The HighlyAmyloidogenic Transthyretin Mutant Ttr G53sE54DL55S" 100.79 127 98 98 2e-67 PDB 1ETA "1 Chain 1, The X-Ray Crystal StructureRefinements Of Normal Human Transthyretin And TheAmyloidogenic Val 30-->met Variant To 1.7 AngstromsResolution" 100.00 128 99 99 8e-68 DBJ BAA00059.1 "prealbumin [Homo sapiens]" 87.07 147 99 100 8e-69 EMBL CAA42087.1 "transthyretin [Homo sapiens]" 87.07 147 100 100 3e-69 EMBL CAG33189.1 "TTR [Homo sapiens]" 87.07 147 99 100 8e-69 GenBank AAA60011.1 prealbumin 87.07 147 100 100 3e-69 GenBank AAA60012.1 prealbumin 87.07 147 100 100 3e-69 GenBank AAA60013.1 "prealbumin precursor" 87.07 147 100 100 3e-69 GenBank AAA73473.1 "transthyretin precursor [Homo sapiens]" 87.07 147 100 100 3e-69 GenBank AAD45014.1 "transthyretin precursor [Homo sapiens]" 87.07 147 100 100 3e-69 PIR VBHU "transthyretin precursor [validated] - human" 87.07 147 100 100 3e-69 PRF 0908191A "prealbumin,thyroxine binding" 100.79 127 100 100 3e-69 PRF 1101213A "protein,amyloid fibril" 100.79 127 100 100 3e-69 PRF 1008142A "prealbumin variant" 100.79 127 98 99 1e-67 PRF 1709210A transthyretin 87.07 147 100 100 3e-69 REF NP_000362.1 "transthyretin; prealbumin [Homosapiens]" 87.07 147 100 100 3e-69 SWISS-PROT P02766 "TTHY_HUMAN Transthyretin precursor (Prealbumin)(TBPA) (TTR) (ATTR)" 87.07 147 100 100 3e-69 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TTR 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 $TTR 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TTR . mM 0.3 1.2 . stop_ save_ ############################ # Computer software used # ############################ save_XEasy _Saveframe_category software _Name XEasy _Version 2.1 loop_ _Task "data processing" "peak assignments" stop_ save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HSQC HNCA HNCACB 1H-15N NOESY ; save_ ####################### # Sample conditions # ####################### save_Native_State _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.75 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_cs _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Native_State _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "TTR subunit 1" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET CA C 53.86 0.000 1 2 2 GLY N N 108.64 0.250 1 3 2 GLY H H 8.43 0.049 1 4 2 GLY CA C 46.43 0.000 1 5 3 PRO CA C 63.38 0.000 1 6 4 THR N N 113.43 0.142 1 7 4 THR H H 8.16 0.010 1 8 4 THR CA C 61.86 0.000 1 9 5 GLY N N 110.74 0.017 1 10 5 GLY H H 8.28 0.005 1 11 5 GLY CA C 45.42 0.000 1 12 6 THR N N 112.78 0.070 1 13 6 THR H H 8.03 0.002 1 14 6 THR CA C 61.81 0.000 1 15 7 GLY N N 110.96 0.221 1 16 7 GLY H H 8.38 0.051 1 17 7 GLY CA C 45.38 0.000 1 18 8 GLU N N 120.36 0.041 1 19 8 GLU H H 8.13 0.003 1 20 8 GLU CA C 56.41 0.000 1 21 9 SER N N 116.57 0.054 1 22 9 SER H H 8.24 0.005 1 23 9 SER CA C 58.61 0.000 1 24 10 LYS N N 122.42 0.025 1 25 10 LYS H H 8.29 0.005 1 26 10 LYS CA C 55.35 0.000 1 27 11 CYS N N 119.10 0.041 1 28 11 CYS H H 8.16 0.005 1 29 11 CYS CA C 50.73 0.000 1 30 12 PRO CA C 64.56 0.000 1 31 13 LEU N N 115.64 0.084 1 32 13 LEU H H 6.82 0.039 1 33 13 LEU CA C 53.69 0.047 1 34 14 MET N N 126.73 0.055 1 35 14 MET H H 8.60 0.004 1 36 14 MET CA C 54.82 0.000 1 37 15 VAL N N 121.85 0.213 1 38 15 VAL H H 7.50 0.051 1 39 15 VAL CA C 59.86 0.000 1 40 16 LYS N N 127.24 0.002 1 41 16 LYS H H 8.60 0.018 1 42 16 LYS CA C 55.24 0.000 1 43 17 VAL N N 123.66 0.189 1 44 17 VAL H H 9.08 0.002 1 45 17 VAL CA C 60.90 0.000 1 46 18 LEU N N 126.04 0.084 1 47 18 LEU H H 8.59 0.038 1 48 18 LEU CA C 54.01 0.000 1 49 19 ASP N N 121.35 0.024 1 50 19 ASP H H 8.76 0.007 1 51 19 ASP CA C 53.43 0.000 1 52 20 ALA N N 127.88 0.050 1 53 20 ALA H H 9.05 0.003 1 54 20 ALA CA C 53.82 0.000 1 55 21 VAL N N 120.63 0.004 1 56 21 VAL H H 9.74 0.022 1 57 21 VAL CA C 65.56 0.000 1 58 22 ARG N N 116.57 0.011 1 59 22 ARG H H 8.40 0.028 1 60 22 ARG CA C 55.46 0.000 1 61 23 GLY N N 109.16 0.036 1 62 23 GLY H H 7.44 0.002 1 63 23 GLY CA C 46.91 0.000 1 64 24 SER N N 111.32 0.046 1 65 24 SER H H 7.37 0.016 1 66 24 SER CA C 55.42 0.000 1 67 25 PRO CA C 62.93 0.000 1 68 26 ALA N N 126.99 0.082 1 69 26 ALA H H 8.15 0.031 1 70 26 ALA CA C 50.62 0.000 1 71 27 ILE N N 126.94 0.009 1 72 27 ILE H H 7.84 0.000 1 73 27 ILE CA C 61.83 0.000 1 74 28 ASN N N 122.14 0.006 1 75 28 ASN H H 7.77 0.005 1 76 28 ASN CA C 54.38 0.000 1 77 29 VAL N N 119.73 0.003 1 78 29 VAL H H 8.32 0.009 1 79 29 VAL CA C 61.76 0.000 1 80 30 ALA N N 130.62 0.000 1 81 30 ALA H H 9.17 0.005 1 82 30 ALA CA C 52.80 0.000 1 83 31 VAL N N 121.95 0.088 1 84 31 VAL H H 8.46 0.006 1 85 31 VAL CA C 60.27 0.000 1 86 32 HIS N N 123.53 0.006 1 87 32 HIS H H 9.01 0.003 1 88 32 HIS CA C 54.97 0.000 1 89 33 VAL N N 122.16 0.072 1 90 33 VAL H H 9.23 0.002 1 91 33 VAL CA C 59.81 0.000 1 92 34 PHE N N 128.13 0.109 1 93 34 PHE H H 9.89 0.003 1 94 34 PHE CA C 56.17 0.000 1 95 35 ARG N N 122.64 0.007 1 96 35 ARG H H 9.51 0.004 1 97 35 ARG CA C 54.37 0.000 1 98 36 LYS N N 129.95 0.029 1 99 36 LYS H H 8.59 0.001 1 100 36 LYS CA C 57.09 0.000 1 101 37 ALA N N 131.33 0.001 1 102 37 ALA H H 8.75 0.009 1 103 37 ALA CA C 51.06 0.000 1 104 38 ALA N N 121.94 0.072 1 105 38 ALA H H 8.30 0.008 1 106 38 ALA CA C 53.91 0.000 1 107 39 ASP N N 115.65 0.095 1 108 39 ASP H H 7.75 0.000 1 109 39 ASP CA C 53.36 0.000 1 110 40 ASP N N 113.25 0.024 1 111 40 ASP H H 7.93 0.002 1 112 40 ASP CA C 55.94 0.000 1 113 41 THR N N 110.85 0.030 1 114 41 THR H H 7.27 0.001 1 115 41 THR CA C 61.37 0.000 1 116 42 TRP N N 120.01 0.111 1 117 42 TRP H H 8.36 0.013 1 118 42 TRP CA C 55.52 0.000 1 119 42 TRP NE1 N 129.01 0.000 1 120 42 TRP HE1 H 9.89 0.000 1 121 43 GLU N N 126.06 0.082 1 122 43 GLU H H 9.29 0.007 1 123 43 GLU CA C 52.96 0.000 1 124 44 PRO CA C 64.51 0.000 1 125 45 PHE N N 124.86 0.047 1 126 45 PHE H H 8.80 0.001 1 127 45 PHE CA C 59.17 0.000 1 128 46 ALA N N 118.34 0.020 1 129 46 ALA H H 7.87 0.007 1 130 46 ALA CA C 52.24 0.000 1 131 47 SER N N 113.15 0.029 1 132 47 SER H H 8.55 0.000 1 133 47 SER CA C 57.64 0.000 1 134 48 GLY N N 106.01 0.029 1 135 48 GLY H H 8.33 0.004 1 136 48 GLY CA C 45.55 0.000 1 137 49 LYS N N 120.00 0.071 1 138 49 LYS H H 8.45 0.002 1 139 49 LYS CA C 53.86 0.000 1 140 50 THR N N 111.36 0.047 1 141 50 THR H H 8.65 0.005 1 142 50 THR CA C 61.89 0.000 1 143 51 SER N N 118.08 0.141 1 144 51 SER H H 8.60 0.005 1 145 51 SER CA C 57.07 0.000 1 146 52 GLU N N 118.50 0.093 1 147 52 GLU H H 9.07 0.006 1 148 52 GLU CA C 59.13 0.000 1 149 53 SER N N 111.38 0.067 1 150 53 SER H H 8.07 0.005 1 151 53 SER CA C 57.50 0.000 1 152 54 GLY N N 111.97 0.000 1 153 54 GLY H H 8.57 0.000 1 154 54 GLY CA C 45.37 0.000 1 155 55 GLU N N 115.15 0.024 1 156 55 GLU H H 7.20 0.004 1 157 55 GLU CA C 54.37 0.000 1 158 56 LEU N N 123.64 0.017 1 159 56 LEU H H 8.67 0.009 1 160 56 LEU CA C 53.93 0.000 1 161 57 HIS N N 124.14 0.016 1 162 57 HIS H H 8.67 0.000 1 163 57 HIS CA C 53.97 0.000 1 164 58 GLY N N 108.89 0.000 1 165 58 GLY H H 9.08 0.003 1 166 58 GLY CA C 46.51 0.000 1 167 59 LEU N N 119.38 0.005 1 168 59 LEU H H 8.06 0.010 1 169 59 LEU CA C 57.00 0.003 1 170 60 THR N N 109.39 0.194 1 171 60 THR H H 7.80 0.058 1 172 60 THR CA C 59.17 0.000 1 173 61 THR N N 111.12 0.008 1 174 61 THR H H 8.38 0.000 1 175 61 THR CA C 59.58 0.000 1 176 62 GLU N N 121.26 0.039 1 177 62 GLU H H 9.24 0.004 1 178 62 GLU CA C 60.03 0.000 1 179 63 GLU N N 115.84 0.001 1 180 63 GLU H H 8.67 0.008 1 181 63 GLU CA C 59.13 0.000 1 182 64 GLU N N 115.25 0.024 1 183 64 GLU H H 7.22 0.001 1 184 64 GLU CA C 56.99 0.000 1 185 65 PHE N N 123.66 0.037 1 186 65 PHE H H 7.80 0.003 1 187 65 PHE CA C 54.38 0.000 1 188 66 VAL N N 115.08 0.000 1 189 66 VAL H H 7.17 0.004 1 190 66 VAL CA C 60.18 0.000 1 191 67 GLU N N 121.70 0.000 1 192 67 GLU H H 8.54 0.006 1 193 67 GLU CA C 56.60 0.000 1 194 68 GLY N N 110.91 0.035 1 195 68 GLY H H 7.92 0.006 1 196 68 GLY CA C 44.65 0.000 1 197 69 ILE N N 120.51 0.004 1 198 69 ILE H H 8.31 0.001 1 199 69 ILE CA C 60.76 0.000 1 200 70 TYR N N 124.78 0.004 1 201 70 TYR H H 8.65 0.000 1 202 70 TYR CA C 56.46 0.000 1 203 71 LYS N N 118.49 0.000 1 204 71 LYS H H 8.71 0.001 1 205 71 LYS CA C 53.52 0.000 1 206 72 VAL N N 127.27 0.088 1 207 72 VAL H H 9.65 0.004 1 208 72 VAL CA C 61.33 0.000 1 209 73 GLU N N 128.10 0.066 1 210 73 GLU H H 9.66 0.003 1 211 73 GLU CA C 54.99 0.000 1 212 74 ILE N N 126.23 0.002 1 213 74 ILE H H 9.16 0.009 1 214 74 ILE CA C 60.22 0.000 1 215 75 ASP N N 128.64 0.007 1 216 75 ASP H H 8.95 0.008 1 217 75 ASP CA C 53.44 0.000 1 218 76 THR N N 117.30 0.049 1 219 76 THR H H 8.18 0.004 1 220 76 THR CA C 64.42 0.000 1 221 77 LYS N N 124.42 0.000 1 222 77 LYS H H 7.52 0.002 1 223 77 LYS CA C 60.31 0.000 1 224 78 SER N N 112.86 0.000 1 225 78 SER H H 8.18 0.013 1 226 78 SER CA C 61.75 0.000 1 227 79 TYR N N 121.07 0.000 1 228 79 TYR H H 6.78 0.000 1 229 79 TYR CA C 61.11 0.000 1 230 80 TRP N N 117.23 0.000 1 231 80 TRP H H 7.78 0.000 1 232 80 TRP CA C 59.16 0.000 1 233 80 TRP NE1 N 126.55 0.000 1 234 80 TRP HE1 H 10.19 0.000 1 235 81 LYS N N 118.22 0.000 1 236 81 LYS H H 8.72 0.002 1 237 81 LYS CA C 59.67 0.000 1 238 82 ALA N N 122.04 0.000 1 239 82 ALA H H 7.53 0.006 1 240 82 ALA CA C 54.40 0.000 1 241 83 LEU N N 117.43 0.000 1 242 83 LEU H H 7.28 0.001 1 243 83 LEU CA C 54.51 0.000 1 244 84 GLY N N 107.34 0.015 1 245 84 GLY H H 7.94 0.005 1 246 84 GLY CA C 45.50 0.000 1 247 85 ILE N N 122.71 0.047 1 248 85 ILE H H 7.92 0.001 1 249 85 ILE CA C 59.70 0.000 1 250 86 SER N N 121.73 0.000 1 251 86 SER H H 8.39 0.001 1 252 86 SER CA C 54.92 0.000 1 253 87 PRO CA C 61.29 0.000 1 254 88 PHE N N 115.82 0.000 1 255 88 PHE H H 7.33 0.008 1 256 88 PHE CA C 60.26 0.000 1 257 89 HIS N N 112.86 0.108 1 258 89 HIS H H 7.63 0.002 1 259 89 HIS CA C 58.13 0.000 1 260 90 GLU N N 122.47 0.000 1 261 90 GLU H H 8.36 0.002 1 262 90 GLU CA C 53.35 0.000 1 263 91 HIS N N 116.59 0.060 1 264 91 HIS H H 8.09 0.000 1 265 91 HIS CA C 54.37 0.000 1 266 92 ALA N N 120.14 0.013 1 267 92 ALA H H 8.51 0.002 1 268 92 ALA CA C 51.69 0.000 1 269 93 GLU N N 121.01 0.044 1 270 93 GLU H H 8.14 0.002 1 271 93 GLU CA C 54.41 0.000 1 272 94 VAL N N 122.28 0.071 1 273 94 VAL H H 8.91 0.006 1 274 94 VAL CA C 61.38 0.000 1 275 95 VAL N N 127.95 0.057 1 276 95 VAL H H 9.29 0.014 1 277 95 VAL CA C 61.06 0.000 1 278 96 PHE N N 124.62 0.085 1 279 96 PHE H H 9.02 0.001 1 280 96 PHE CA C 56.03 0.000 1 281 97 THR N N 118.18 0.000 1 282 97 THR H H 8.52 0.000 1 283 97 THR CA C 62.95 0.000 1 284 98 ALA N N 129.36 0.047 1 285 98 ALA H H 9.14 0.004 1 286 98 ALA CA C 50.07 0.000 1 287 99 ASN N N 111.88 0.071 1 288 99 ASN H H 8.63 0.003 1 289 99 ASN CA C 54.44 0.000 1 290 100 ASP N N 117.05 0.025 1 291 100 ASP H H 8.89 0.006 1 292 100 ASP CA C 55.43 0.000 1 293 101 SER N N 117.23 0.000 1 294 101 SER H H 8.79 0.005 1 295 101 SER CA C 57.23 0.000 1 296 102 GLY N N 109.95 0.030 1 297 102 GLY H H 7.15 0.004 1 298 102 GLY CA C 43.47 0.000 1 299 103 PRO CA C 54.37 0.000 1 300 104 ARG N N 121.16 0.013 1 301 104 ARG H H 8.87 0.026 1 302 104 ARG CA C 58.11 0.002 1 303 105 ARG N N 105.94 0.013 1 304 105 ARG H H 7.27 0.000 1 305 105 ARG CA C 54.42 0.056 1 306 106 TYR N N 121.13 0.000 1 307 106 TYR H H 8.81 0.024 1 308 106 TYR CA C 57.99 0.000 1 309 107 THR N N 120.53 0.000 1 310 107 THR H H 8.86 0.002 1 311 107 THR CA C 61.85 0.000 1 312 108 ILE N N 126.97 0.055 1 313 108 ILE H H 8.80 0.011 1 314 108 ILE CA C 58.51 0.000 1 315 109 ALA N N 128.29 0.078 1 316 109 ALA H H 8.12 0.000 1 317 109 ALA CA C 50.69 0.000 1 318 110 ALA N N 125.07 0.051 1 319 110 ALA H H 9.03 0.006 1 320 110 ALA CA C 48.62 0.000 1 321 111 LEU N N 124.65 0.131 1 322 111 LEU H H 8.79 0.000 1 323 111 LEU CA C 53.95 0.000 1 324 112 LEU N N 124.28 0.066 1 325 112 LEU H H 9.08 0.000 1 326 112 LEU CA C 55.47 0.000 1 327 113 SER N N 116.89 0.019 1 328 113 SER H H 9.08 0.012 1 329 113 SER CA C 58.11 0.000 1 330 114 PRO CA C 56.05 0.000 1 331 115 TYR N N 113.86 0.047 1 332 115 TYR H H 8.23 0.001 1 333 115 TYR CA C 58.60 0.000 1 334 116 SER N N 111.58 0.050 1 335 116 SER H H 7.46 0.001 1 336 116 SER CA C 57.33 0.000 1 337 117 TYR N N 120.40 0.038 1 338 117 TYR H H 8.33 0.016 1 339 117 TYR CA C 55.19 0.000 1 340 118 SER N N 113.74 0.079 1 341 118 SER H H 8.44 0.003 1 342 118 SER CA C 57.86 0.000 1 343 119 THR N N 121.96 0.025 1 344 119 THR H H 8.39 0.001 1 345 119 THR CA C 63.51 0.000 1 346 120 THR N N 116.27 0.003 1 347 120 THR H H 8.89 0.006 1 348 120 THR CA C 58.61 0.000 1 349 121 ALA N N 122.16 0.094 1 350 121 ALA H H 8.32 0.000 1 351 121 ALA CA C 55.66 0.000 1 352 122 VAL N N 120.55 0.024 1 353 122 VAL H H 8.13 0.000 1 354 122 VAL CA C 61.11 0.000 1 355 123 VAL N N 128.36 0.055 1 356 123 VAL H H 8.33 0.003 1 357 123 VAL CA C 60.83 0.000 1 358 124 THR N N 119.86 0.039 1 359 124 THR H H 8.71 0.001 1 360 124 THR CA C 60.32 0.000 1 361 125 ASN N N 121.62 0.057 1 362 125 ASN H H 8.69 0.004 1 363 125 ASN CA C 50.53 0.000 1 364 126 PRO CA C 63.44 0.000 1 365 127 LYS N N 120.23 0.011 1 366 127 LYS H H 7.98 0.007 1 367 127 LYS CA C 56.14 0.000 1 368 128 GLU N N 126.50 0.024 1 369 128 GLU H H 7.65 0.000 1 370 128 GLU CA C 57.99 0.000 1 stop_ save_