data_17674 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of FGF1-SSR128129E ; _BMRB_accession_number 17674 _BMRB_flat_file_name bmr17674.str _Entry_type original _Submission_date 2011-05-30 _Accession_date 2011-05-30 _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 Mohan Sepuru K. . 2 Rani Sandhya G. . 3 Yu Chin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 586 "13C chemical shifts" 359 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-19 original author . stop_ _Original_release_date 2012-06-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Interaction of FGF1 with a novel anti-angiogenic drug SSR128129E.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22683470 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mohan Sepuru K. . 2 Rani Sandhya G. . 3 Chiu Ing-Ming . . 4 Yu Chin . . stop_ _Journal_abbreviation 'Arch. Biochem. Biophys.' _Journal_name_full 'Archives of biochemistry and biophysics' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FGF1-SSR128129E _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FGF1 $FGF1 SSR_1 $SSR SSR_2 $SSR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FGF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FGF1 _Molecular_mass 14828.918 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; YKKPKLLYCSNGGHFLRILP DGTVDGTRDRSDQHIQLQLS AESVGEVYIKSTETGQYLAM DTDGLLYGSQTPNEECLFLE RLEENHYNTYISKKHAEKNW FVGLKKNGSCKRGPRTHYGQ KAILFLPLPV ; loop_ _Residue_seq_code _Residue_label 1 TYR 2 LYS 3 LYS 4 PRO 5 LYS 6 LEU 7 LEU 8 TYR 9 CYS 10 SER 11 ASN 12 GLY 13 GLY 14 HIS 15 PHE 16 LEU 17 ARG 18 ILE 19 LEU 20 PRO 21 ASP 22 GLY 23 THR 24 VAL 25 ASP 26 GLY 27 THR 28 ARG 29 ASP 30 ARG 31 SER 32 ASP 33 GLN 34 HIS 35 ILE 36 GLN 37 LEU 38 GLN 39 LEU 40 SER 41 ALA 42 GLU 43 SER 44 VAL 45 GLY 46 GLU 47 VAL 48 TYR 49 ILE 50 LYS 51 SER 52 THR 53 GLU 54 THR 55 GLY 56 GLN 57 TYR 58 LEU 59 ALA 60 MET 61 ASP 62 THR 63 ASP 64 GLY 65 LEU 66 LEU 67 TYR 68 GLY 69 SER 70 GLN 71 THR 72 PRO 73 ASN 74 GLU 75 GLU 76 CYS 77 LEU 78 PHE 79 LEU 80 GLU 81 ARG 82 LEU 83 GLU 84 GLU 85 ASN 86 HIS 87 TYR 88 ASN 89 THR 90 TYR 91 ILE 92 SER 93 LYS 94 LYS 95 HIS 96 ALA 97 GLU 98 LYS 99 ASN 100 TRP 101 PHE 102 VAL 103 GLY 104 LEU 105 LYS 106 LYS 107 ASN 108 GLY 109 SER 110 CYS 111 LYS 112 ARG 113 GLY 114 PRO 115 ARG 116 THR 117 HIS 118 TYR 119 GLY 120 GLN 121 LYS 122 ALA 123 ILE 124 LEU 125 PHE 126 LEU 127 PRO 128 LEU 129 PRO 130 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-22 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 BMRB 15783 FGF-1 100.00 133 100.00 100.00 2.83e-91 BMRB 15960 FGF-1 100.00 133 100.00 100.00 2.83e-91 BMRB 16493 aFGF 99.23 132 100.00 100.00 1.81e-90 BMRB 16494 aFGF 99.23 132 100.00 100.00 1.81e-90 BMRB 16502 aFGF 99.23 132 100.00 100.00 1.81e-90 BMRB 17464 FGF 99.23 132 100.00 100.00 1.81e-90 PDB 1AXM "Heparin-Linked Biologically-Active Dimer Of Fibroblast Growth Factor" 100.00 135 99.23 99.23 4.25e-90 PDB 1DJS "Ligand-binding Portion Of Fibroblast Growth Factor Receptor 2 In Complex With Fgf1" 100.00 135 99.23 99.23 4.25e-90 PDB 1DZC "High Resolution Structure Of Acidic Fibroblast Growth Factor. Mutant Fgf-4-ala-(23-154), 24 Nmr Structures" 96.15 131 100.00 100.00 1.14e-87 PDB 1DZD "High Resolution Structure Of Acidic Fibroblast Growth Factor (27-154), 24 Nmr Structures" 95.38 127 100.00 100.00 1.04e-86 PDB 1E0O "Crystal Structure Of A Ternary Fgf1-Fgfr2-Heparin Complex" 100.00 140 100.00 100.00 8.37e-91 PDB 1EVT "Crystal Structure Of Fgf1 In Complex With The Extracellular Ligand Binding Domain Of Fgf Receptor 1 (Fgfr1)" 100.00 134 100.00 100.00 3.09e-91 PDB 1HKN "A Complex Between Acidic Fibroblast Growth Factor And 5- Amino-2-Naphthalenesulfonate" 100.00 139 100.00 100.00 6.80e-91 PDB 1JQZ "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag." 100.00 146 100.00 100.00 1.22e-90 PDB 1JT3 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Histidine Tag And Leu 73 Replaced By Val (L73v)" 100.00 146 99.23 100.00 3.11e-90 PDB 1JT4 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Val 109 Replaced By Leu (v109l)" 100.00 146 99.23 100.00 4.51e-90 PDB 1JT5 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Leu 73 Replaced By Val And Val 109 R" 100.00 146 98.46 100.00 1.07e-89 PDB 1JT7 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Leu 44 Replaced By Phe And Leu 73 Re" 100.00 146 97.69 99.23 3.36e-89 PDB 1JTC "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Leu 44 Replaced By Phe (L44f)" 100.00 146 99.23 99.23 3.82e-90 PDB 1JY0 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Cys 117 Replaced With Val (C117v)" 100.00 146 99.23 99.23 1.55e-89 PDB 1K5U "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag With His93 Replaced By Gly (H93g)" 100.00 146 99.23 99.23 4.71e-89 PDB 1K5V "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag With Asn106 Replaced By Gly (N106g)" 100.00 146 99.23 99.23 1.42e-89 PDB 1M16 "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag And Leu 44 Replaced With Phe (L44f), Leu" 100.00 146 96.92 98.46 4.18e-88 PDB 1P63 "Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form With Amino Terminal His Tag And Leu111 Replaced With Ile (L111i)" 100.00 144 99.23 100.00 2.72e-90 PDB 1PZZ "Crystal Structure Of Fgf-1, V51n Mutant" 100.00 146 99.23 99.23 1.43e-89 PDB 1Q03 "Crystal Structure Of Fgf-1, S50gV51G MUTANT" 100.00 146 98.46 98.46 1.40e-88 PDB 1Q04 "Crystal Structure Of Fgf-1, S50e/v51n" 100.00 146 98.46 98.46 8.88e-89 PDB 1RG8 "Human Acidic Fibroblast Growth Factor (Hafgf-1) At 1.10 Angstrom Resolution (140 Amino Acid Form)" 100.00 146 100.00 100.00 1.22e-90 PDB 1RML "Nmr Study Of Acid Fibroblast Growth Factor Bound To 1,3,6- Naphthalene Trisulphonate, 26 Structures" 100.00 155 100.00 100.00 3.29e-91 PDB 1RY7 "Crystal Structure Of The 3 Ig Form Of Fgfr3c In Complex With Fgf1" 100.00 155 100.00 100.00 3.29e-91 PDB 1YTO "Crystal Structure Of Gly19 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 145 99.23 99.23 4.77e-88 PDB 1Z2V "Crystal Structure Of Glu60 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 145 99.23 99.23 4.18e-88 PDB 1Z4S "Crystal Structure Of Gly19 And Glu60 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 144 98.46 98.46 1.68e-85 PDB 2AFG "2.0 Angstrom X-Ray Structure Of Human Acidic Fibroblast Growth Factor" 100.00 140 100.00 100.00 8.37e-91 PDB 2AQZ "Crystal Structure Of Fgf-1, S17tN18TG19 DELETION MUTANT" 100.00 145 97.69 98.46 1.12e-86 PDB 2AXM "Heparin-Linked Biologically-Active Dimer Of Fibroblast Growth Factor" 100.00 135 100.00 100.00 3.34e-91 PDB 2ERM "Solution Structure Of A Biologically Active Human Fgf-1 Monomer, Complexed To A Hexasaccharide Heparin-Analogue" 100.00 139 100.00 100.00 6.80e-91 PDB 2HW9 "Crystal Structure Of Lys12cysCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.60 Angstrom Resolution" 100.00 146 98.46 98.46 5.44e-88 PDB 2HWA "Crystal Structure Of Lys12thrCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.65 Angstrom Resolution" 100.00 146 98.46 98.46 8.41e-89 PDB 2HWM "Crystal Structure Of Lys12valCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.60 Angstrom Resolution" 100.00 146 98.46 98.46 1.47e-88 PDB 2HZ9 "Crystal Structure Of Lys12valASN95VALCYS117VAL MUTANT OF Human Acidic Fibroblast Growth Factor At 1.70 Angstrom Resolution" 100.00 146 97.69 97.69 2.59e-87 PDB 2J3P "Crystal Structure Of Rat Fgf1 At 1.4 A" 100.00 134 96.92 97.69 1.60e-88 PDB 2K43 "Acidic Fibroblast Growth Factor Solution Structure In The Fgf-1-C2a Binary Complex: Key Component In The Fibroblast Growthfacto" 100.00 133 100.00 100.00 2.83e-91 PDB 2K4A "Fgf-1-C2a Binary Complex Structure: A Key Component In The Fibroblast Growthfactor Non-Classical Pathway" 100.00 133 100.00 100.00 2.83e-91 PDB 2K8R "Solution Structure Of Human Acidic Fibroblast Growth Factor In Complex With Anti-Angiogenic Drug Inositol Hexaphosphate (Ip6)" 100.00 133 100.00 100.00 2.83e-91 PDB 2KI4 "Fgf1-S100a13 Complex Structure: Key Component In Non-Classic Way Of Fgf1" 100.00 133 100.00 100.00 2.83e-91 PDB 2KI6 "The Fgf1-S100a13-C2a Hetero-Hexameric Complex Structure: A C In The Non-Classical Pathway For Fgf1 Secretion" 100.00 133 100.00 100.00 2.83e-91 PDB 2NTD "Human Fibroblast Growth Factor-1 (140 Amino Acid Form) With Cys117valPRO134CYS MUTATIONS" 100.00 146 98.46 98.46 8.14e-88 PDB 2Q9X "Crystal Structure Of Highly Stable Mutant Q40p/s47i/h93g Of Human Fibroblast Growth Factor-1" 100.00 140 97.69 97.69 2.04e-87 PDB 2RQ9 "Solution Structure Of Human Acidic Fibroblast Growth Factor (Afgf) In The Presence Of A Protein Stabilizer Ndsb-New" 100.00 143 100.00 100.00 3.73e-91 PDB 2UUS "Crystal Structure Of The Rat Fgf1-sucrose Octasulfate (sos) Complex" 100.00 132 96.92 97.69 1.90e-88 PDB 3B9U "Crystal Structure Of L26nD28NH93G MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.69 98.46 2.59e-87 PDB 3BA4 "Crystal Structure Of L26d Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.63e-89 PDB 3BA5 "Crystal Structure Of D28a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.19e-89 PDB 3BA7 "Crystal Structure Of L26nD28A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 98.46 1.40e-88 PDB 3BAD "Crystal Structure Of D70aH93G MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 98.46 4.93e-88 PDB 3BAG "Crystal Structure Of K112nN114A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 98.46 6.40e-89 PDB 3BAH "Crystal Structure Of K112n Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 5.92e-90 PDB 3BAO "Crystal Structure Of L26n Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.37e-89 PDB 3BAQ "Crystal Structure Of L26a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 5.73e-90 PDB 3BAU "Crystal Structure Of K12vL26DD28A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.69 97.69 1.59e-87 PDB 3BAV "Crystal Structure Of L26aD28N MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 99.23 2.39e-89 PDB 3BB2 "Crystal Structure Of L26dD28N MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 99.23 7.54e-89 PDB 3CQA "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ala And Lys101ala" 100.00 144 98.46 98.46 3.08e-89 PDB 3CRG "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ala, Glu82asn And Lys101ala" 100.00 146 97.69 97.69 1.62e-88 PDB 3CRH "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ser And Lys101ala" 100.00 146 98.46 98.46 2.92e-89 PDB 3CRI "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ser, Glu82asn And Lys101ala" 100.00 146 97.69 97.69 1.32e-88 PDB 3CU1 "Crystal Structure Of 2:2:2 Fgfr2d2:fgf1:sos Complex" 100.00 131 100.00 100.00 4.73e-91 PDB 3FGM "Crystal Structure Of L44fC83TC117VF132W MUTANT OF HUMAN Acidic Fibroblast Growth Factor" 100.00 146 96.92 97.69 4.83e-87 PDB 3FJ8 "Crystal Structure Of C117i Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.88e-89 PDB 3FJ9 "Crystal Structure Of F85w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 100.00 8.30e-90 PDB 3FJA "Crystal Structure Of F132w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 100.00 8.30e-90 PDB 3FJB "Crystal Structure Of V31i Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 100.00 2.10e-90 PDB 3FJC "Crystal Structure Of L44w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.01e-89 PDB 3FJD "Crystal Structure Of L44fF132W MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.46 99.23 3.01e-89 PDB 3FJE "Crystal Structure Of C83s Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.65e-89 PDB 3FJF "Crystal Structure Of C83t Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.99e-89 PDB 3FJH "Crystal Structure Of C83a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.18e-89 PDB 3FJI "Crystal Structure Of K12vC83IC117V MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.69 97.69 1.42e-87 PDB 3FJJ "Crystal Structure Of C83v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.55e-89 PDB 3FJK "Crystal Structure Of A66c Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.33e-89 PDB 3HAL "Crystal Structure Of Rabbit Acidic Fibroblast Growth Factor" 100.00 146 97.69 98.46 2.45e-88 PDB 3HOM "Crystal Structure Of Oxidized A66c Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.33e-89 PDB 3JUT "Acidic Fibroblast Growth Factor (Fgf-1) Complexed With Gentisic Acid" 99.23 130 100.00 100.00 3.03e-90 PDB 3K1X "Acidic Fibroblast Growth Factor (Fgf-1) Complexed With Dobes" 99.23 130 100.00 100.00 3.03e-90 PDB 3OJ2 "Crystal Structure Of Fgf1 Complexed With The Ectodomain Of Fgfr2b Harboring The A172f Pfeiffer Syndrome Mutation" 100.00 155 100.00 100.00 3.29e-91 PDB 3OJM "Crystal Structure Of Fgf1 Complexed With The Ectodomain Of Fgfr2b Harboring P253r Apert Mutation" 100.00 155 100.00 100.00 3.29e-91 PDB 3OJV "Crystal Structure Of Fgf1 Complexed With The Ectodomain Of Fgfr1c Exhibiting An Ordered Ligand Specificity-Determining Betac'-B" 100.00 136 100.00 100.00 2.90e-91 PDB 3UD7 "Crystal Structure Analysis Of Fgf1-disaccharide(ni21) Complexes" 100.00 141 100.00 100.00 7.34e-91 PDB 3UD8 "Crystal Structure Analysis Of Fgf1-disaccharide(ni22) Complex" 100.00 141 100.00 100.00 7.34e-91 PDB 3UD9 "Crystal Structure Analysis Of Fgf1-disaccharide(ni23) Complex" 100.00 141 100.00 100.00 7.34e-91 PDB 3UDA "Crystal Structure Analysis Of Fgf1-disaccharide(ni24) Complex" 100.00 141 100.00 100.00 7.34e-91 PDB 4J23 "Low Resolution Crystal Structure Of The Fgfr2d2d3/fgf1/sr128545 Complex" 100.00 138 100.00 100.00 5.29e-91 PDB 4Q91 "Crystal Structure Of C16a/k12v/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.92 96.92 1.87e-86 PDB 4Q9G "Crystal Structure Of K12v/c16s/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.92 96.92 2.46e-86 PDB 4Q9P "Crystal Structure Of C16t/k12v/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.92 96.92 2.51e-86 PDB 4QAL "Crystal Structure Of C117a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.18e-89 PDB 4QBC "Crystal Structure Of C117t Mutant Of Human Acidic Fibroblast Growth Factor In Sodium Formate Buffer" 100.00 146 99.23 99.23 1.99e-89 PDB 4QBV "Crystal Structure Of C117t Mutant Of Human Acidic Fibroblast Growth Factor In Sodium Citrate Buffer" 100.00 146 99.23 99.23 1.53e-89 PDB 4QC4 "Crystal Structure Of C117s Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.23 99.23 1.65e-89 DBJ BAC29035 "unnamed protein product [Mus musculus]" 100.00 155 96.92 97.69 1.29e-88 DBJ BAF82451 "unnamed protein product [Homo sapiens]" 100.00 154 99.23 99.23 1.26e-88 DBJ BAG35227 "unnamed protein product [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 DBJ BAI46827 "fibroblast growth factor 1 [synthetic construct]" 100.00 155 100.00 100.00 3.29e-91 EMBL CAA32448 "unnamed protein product [Rattus norvegicus]" 100.00 155 96.92 97.69 1.29e-88 EMBL CAA36206 "unnamed protein product [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 EMBL CAA42869 "acidic fibroblast growth factor [Sus scrofa]" 100.00 152 97.69 98.46 6.62e-89 EMBL CAA46661 "acidic fibroblast growth factor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 EMBL CAI29610 "hypothetical protein [Pongo abelii]" 100.00 214 100.00 100.00 2.21e-90 GB AAA37618 "acidic fibroblast growth factor [Mus musculus]" 100.00 155 96.92 97.69 1.29e-88 GB AAA52446 "acidic fibroblast growth factor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 GB AAA52638 "heparin-binding growth factor 1, partial [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 GB AAA79245 "beta-endothelial cell growth factor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 GB AAB29057 "acidic fibroblast growth factor, partial [Homo sapiens]" 100.00 154 100.00 100.00 2.62e-91 PRF 1605206A "acidic fibroblast growth factor" 100.00 156 100.00 100.00 2.83e-91 REF NP_000791 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 REF NP_001127073 "fibroblast growth factor 1 [Pongo abelii]" 100.00 214 100.00 100.00 2.21e-90 REF NP_001138364 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 REF NP_001138406 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 REF NP_001138407 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 3.29e-91 SP P05230 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 100.00 100.00 3.29e-91 SP P20002 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 152 97.69 98.46 6.62e-89 SP P34004 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 97.69 97.69 3.37e-89 SP P61148 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 96.92 97.69 1.29e-88 SP P61149 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 96.92 97.69 1.29e-88 stop_ save_ ############# # Ligands # ############# save_SSR _Saveframe_category ligand _Mol_type non-polymer _Name_common "SSR (2-(3-fluoro-2-methylbenzyl)-4-methyl-1-phenyl-3-(piperazin-1-ylcarbonyl)-1H-indol-5-ol)" _BMRB_code . _PDB_code SSR _Molecular_mass 457.539 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 17 10:22:08 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N9 N9 N . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? O16 O16 O . 0 . ? C17 C17 C . 0 . ? N18 N18 N . 0 . ? C19 C19 C . 0 . ? C20 C20 C . 0 . ? N21 N21 N . 0 . ? C22 C22 C . 0 . ? C23 C23 C . 0 . ? O32 O32 O . 0 . ? C35 C35 C . 0 . ? C36 C36 C . 0 . ? C37 C37 C . 0 . ? C38 C38 C . 0 . ? C39 C39 C . 0 . ? C40 C40 C . 0 . ? C46 C46 C . 0 . ? C47 C47 C . 0 . ? C50 C50 C . 0 . ? C51 C51 C . 0 . ? C52 C52 C . 0 . ? C53 C53 C . 0 . ? C54 C54 C . 0 . ? C58 C58 C . 0 . ? F62 F62 F . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H12 H12 H . 0 . ? H12A H12A H . 0 . ? H12B H12B H . 0 . ? HO16 HO16 H . 0 . ? H19 H19 H . 0 . ? H19A H19A H . 0 . ? H20 H20 H . 0 . ? H20A H20A H . 0 . ? HN21 HN21 H . 0 . ? H22 H22 H . 0 . ? H22A H22A H . 0 . ? H23 H23 H . 0 . ? H23A H23A H . 0 . ? H36 H36 H . 0 . ? H37 H37 H . 0 . ? H38 H38 H . 0 . ? H39 H39 H . 0 . ? H40 H40 H . 0 . ? H46 H46 H . 0 . ? H46A H46A H . 0 . ? H52 H52 H . 0 . ? H53 H53 H . 0 . ? H54 H54 H . 0 . ? H58 H58 H . 0 . ? H58A H58A H . 0 . ? H58B H58B H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 C2 ? ? SING C1 C6 ? ? SING C2 C3 ? ? DOUB C3 C4 ? ? SING C3 N9 ? ? SING C4 C5 ? ? SING C4 C11 ? ? DOUB C5 C6 ? ? SING C5 C12 ? ? SING C6 O16 ? ? SING N9 C10 ? ? SING N9 C35 ? ? DOUB C10 C11 ? ? SING C10 C46 ? ? SING C11 C17 ? ? SING C17 N18 ? ? DOUB C17 O32 ? ? SING N18 C19 ? ? SING N18 C23 ? ? SING C19 C20 ? ? SING C20 N21 ? ? SING N21 C22 ? ? SING C22 C23 ? ? DOUB C35 C36 ? ? SING C35 C40 ? ? SING C36 C37 ? ? DOUB C37 C38 ? ? SING C38 C39 ? ? DOUB C39 C40 ? ? SING C46 C47 ? ? DOUB C47 C50 ? ? SING C47 C54 ? ? SING C50 C51 ? ? SING C50 C58 ? ? DOUB C51 C52 ? ? SING C51 F62 ? ? SING C52 C53 ? ? DOUB C53 C54 ? ? SING C1 H1 ? ? SING C2 H2 ? ? SING C12 H12 ? ? SING C12 H12A ? ? SING C12 H12B ? ? SING O16 HO16 ? ? SING C19 H19 ? ? SING C19 H19A ? ? SING C20 H20 ? ? SING C20 H20A ? ? SING N21 HN21 ? ? SING C22 H22 ? ? SING C22 H22A ? ? SING C23 H23 ? ? SING C23 H23A ? ? SING C36 H36 ? ? SING C37 H37 ? ? SING C38 H38 ? ? SING C39 H39 ? ? SING C40 H40 ? ? SING C46 H46 ? ? SING C46 H46A ? ? SING C52 H52 ? ? SING C53 H53 ? ? SING C54 H54 ? ? SING C58 H58 ? ? SING C58 H58A ? ? SING C58 H58B ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic _Details $FGF1 'E. coli' 562 Bacteria . Escherichia coli BL21DE3 FGF 'acidic fibroblast growth factor' 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 $FGF1 'recombinant technology' . Escherichia coli . pET20b $SSR 'chemical synthesis' . chemical synthesis . 'synthetic compound' 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 $FGF1 1.0 mM '[U-100% 13C; U-100% 15N]' $SSR 2.1 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' 'ammonium sulfate' 100 mM 'natural abundance' H2O 90 % 'natural abundance' H2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_13C-Filter_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-Filter NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 TSP C 13 'methyl carbon' ppm 0 internal direct . . . 1 TSP H 1 'methylene protons' ppm 0 internal direct . . . 1 TSP N 15 nitrogen ppm 0 internal direct . . . 1 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HNCACB' '3D HBHA(CO)NH' '3D HN(CO)CA' '3D C(CO)NH' '3D H(CCO)NH' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FGF1 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 TYR HA H 4.696 0.0 . 2 1 1 TYR HB2 H 2.927 0.0 . 3 1 1 TYR HB3 H 3.36 0.0 . 4 1 1 TYR HD1 H 7.1 0.0 . 5 1 1 TYR HD2 H 7.1 0.0 . 6 1 1 TYR HE1 H 6.89 0.0 . 7 1 1 TYR HE2 H 6.89 0.0 . 8 1 1 TYR H H 8.416 0.0 . 9 1 1 TYR C C 174.229 0.0 . 10 1 1 TYR CA C 55.442 0.0 . 11 1 1 TYR N N 120.6 0.0 . 12 2 2 LYS H H 7.955 0.0 . 13 2 2 LYS HA H 4.27 0.0 . 14 2 2 LYS HB2 H 1.89 0.0 . 15 2 2 LYS C C 174.3 0.0 . 16 2 2 LYS CA C 51.913 0.0 . 17 2 2 LYS N N 120.0 0.0 . 18 3 3 LYS H H 8.06 0.0 . 19 3 3 LYS HA H 4.6 0.0 . 20 3 3 LYS HB2 H 1.6 0.0 . 21 3 3 LYS HB3 H 1.77 0.0 . 22 3 3 LYS CA C 51.9 0.0 . 23 3 3 LYS N N 131.14 0.0 . 24 4 4 PRO HA H 4.716 0.0 . 25 4 4 PRO HB3 H 2.171 0.0 . 26 4 4 PRO C C 172.359 0.0 . 27 4 4 PRO CA C 60.687 0.0 . 28 4 4 PRO CB C 30.627 0.0 . 29 5 5 LYS H H 9.357 0.0 . 30 5 5 LYS HA H 5.062 0.0 . 31 5 5 LYS HB2 H 1.507 0.0 . 32 5 5 LYS HB3 H 1.835 0.0 . 33 5 5 LYS C C 171.776 0.0 . 34 5 5 LYS CA C 51.445 0.0 . 35 5 5 LYS CB C 34.945 0.0 . 36 5 5 LYS N N 119.1 0.0 . 37 6 6 LEU H H 8.944 0.0 . 38 6 6 LEU HA H 4.984 0.0 . 39 6 6 LEU HB2 H 1.641 0.0 . 40 6 6 LEU HB3 H 1.806 0.0 . 41 6 6 LEU HD1 H 0.769 0.0 . 42 6 6 LEU HD2 H 0.646 0.0 . 43 6 6 LEU C C 174.676 0.0 . 44 6 6 LEU CA C 50.259 0.0 . 45 6 6 LEU CB C 41.472 0.0 . 46 6 6 LEU N N 117.4 0.0 . 47 7 7 LEU H H 10.297 0.0 . 48 7 7 LEU HA H 5.083 0.0 . 49 7 7 LEU HB2 H 1.335 0.0 . 50 7 7 LEU HB3 H 1.65 0.0 . 51 7 7 LEU HG H 1.46 0.0 . 52 7 7 LEU HD1 H 0.625 0.0 . 53 7 7 LEU HD2 H 0.528 0.0 . 54 7 7 LEU C C 172.29 0.0 . 55 7 7 LEU CA C 53.596 0.0 . 56 7 7 LEU N N 125.0 0.0 . 57 8 8 TYR H H 8.483 0.0 . 58 8 8 TYR HA H 4.592 0.0 . 59 8 8 TYR HB2 H 2.922 0.0 . 60 8 8 TYR HB3 H 3.405 0.0 . 61 8 8 TYR C C 171.27 0.0 . 62 8 8 TYR CA C 54.761 0.0 . 63 8 8 TYR CB C 37.988 0.0 . 64 8 8 TYR N N 125.0 0.0 . 65 9 9 CYS H H 9.235 0.0 . 66 9 9 CYS HA H 4.163 0.0 . 67 9 9 CYS HB2 H 2.52 0.0 . 68 9 9 CYS HB3 H 2.581 0.0 . 69 9 9 CYS C C 172.619 0.0 . 70 9 9 CYS CA C 55.588 0.0 . 71 9 9 CYS CB C 26.864 0.0 . 72 9 9 CYS N N 130.104 0.0 . 73 10 10 SER H H 8.173 0.0 . 74 10 10 SER HA H 3.92 0.0 . 75 10 10 SER HB2 H 3.9 0.0 . 76 10 10 SER C C 172.21 0.0 . 77 10 10 SER CA C 57.853 0.0 . 78 10 10 SER CB C 61.82 0.0 . 79 10 10 SER N N 122.6 0.0 . 80 11 11 ASN H H 7.45 0.0 . 81 11 11 ASN HA H 4.36 0.0 . 82 11 11 ASN CA C 52.43 0.0 . 83 11 11 ASN N N 119.55 0.0 . 84 12 12 GLY H H 7.096 0.0 . 85 12 12 GLY HA3 H 3.927 0.0 . 86 12 12 GLY C C 171.806 0.0 . 87 12 12 GLY CA C 41.915 0.0 . 88 12 12 GLY N N 109.3 0.0 . 89 13 13 GLY H H 7.096 0.0 . 90 13 13 GLY HA2 H 3.598 0.0 . 91 13 13 GLY HA3 H 3.204 0.0 . 92 13 13 GLY C C 170.445 0.0 . 93 13 13 GLY CA C 44.272 0.0 . 94 13 13 GLY N N 109.3 0.0 . 95 14 14 HIS H H 6.302 0.0 . 96 14 14 HIS HA H 4.104 0.0 . 97 14 14 HIS HB2 H 2.488 0.0 . 98 14 14 HIS HB3 H 2.651 0.0 . 99 14 14 HIS C C 171.281 0.0 . 100 14 14 HIS CA C 54.319 0.0 . 101 14 14 HIS CB C 31.792 0.0 . 102 14 14 HIS N N 113.6 0.0 . 103 15 15 PHE H H 9.298 0.0 . 104 15 15 PHE HA H 5.39 0.0 . 105 15 15 PHE HB2 H 2.936 0.0 . 106 15 15 PHE HB3 H 3.547 0.0 . 107 15 15 PHE C C 173.938 0.0 . 108 15 15 PHE CA C 54.273 0.0 . 109 15 15 PHE CB C 37.632 0.0 . 110 15 15 PHE N N 120.7 0.0 . 111 16 16 LEU H H 8.48 0.0 . 112 16 16 LEU HA H 4.394 0.0 . 113 16 16 LEU HB2 H 1.384 0.0 . 114 16 16 LEU HB3 H 1.897 0.0 . 115 16 16 LEU C C 171.758 0.0 . 116 16 16 LEU CA C 54.44 0.0 . 117 16 16 LEU CB C 41.301 0.0 . 118 16 16 LEU N N 124.7 0.0 . 119 17 17 ARG H H 9.339 0.0 . 120 17 17 ARG HA H 4.715 0.0 . 121 17 17 ARG HB2 H 1.236 0.0 . 122 17 17 ARG HB3 H 2.587 0.0 . 123 17 17 ARG HG2 H 1.23 0.0 . 124 17 17 ARG HG3 H 1.503 0.0 . 125 17 17 ARG HD2 H 3.196 0.0 . 126 17 17 ARG HD3 H 3.416 0.0 . 127 17 17 ARG C C 171.302 0.0 . 128 17 17 ARG CA C 53.301 0.0 . 129 17 17 ARG CB C 32.62 0.0 . 130 17 17 ARG N N 126.971 0.0 . 131 18 18 ILE H H 6.989 0.0 . 132 18 18 ILE HA H 4.563 0.0 . 133 18 18 ILE HB H 1.653 0.0 . 134 18 18 ILE HG2 H 0.641 0.0 . 135 18 18 ILE C C 173.747 0.0 . 136 18 18 ILE CA C 57.903 0.0 . 137 18 18 ILE N N 120.966 0.0 . 138 19 19 LEU H H 8.94 0.0 . 139 19 19 LEU CA C 51.419 0.0 . 140 19 19 LEU N N 128.097 0.0 . 141 20 20 PRO HA H 4.319 0.0 . 142 20 20 PRO HB2 H 1.971 0.0 . 143 20 20 PRO HB3 H 2.343 0.0 . 144 20 20 PRO HG2 H 1.939 0.0 . 145 20 20 PRO HD2 H 3.673 0.0 . 146 20 20 PRO C C 173.966 0.0 . 147 20 20 PRO CA C 62.71 0.0 . 148 20 20 PRO CB C 29.518 0.0 . 149 21 21 ASP H H 7.415 0.0 . 150 21 21 ASP HA H 4.513 0.0 . 151 21 21 ASP HB2 H 2.606 0.0 . 152 21 21 ASP HB3 H 3.094 0.0 . 153 21 21 ASP C C 174.57 0.0 . 154 21 21 ASP CA C 51.361 0.0 . 155 21 21 ASP CB C 37.419 0.0 . 156 21 21 ASP N N 114.0 0.0 . 157 22 22 GLY H H 8.404 0.0 . 158 22 22 GLY HA2 H 4.632 0.0 . 159 22 22 GLY HA3 H 3.838 0.0 . 160 22 22 GLY C C 172.565 0.0 . 161 22 22 GLY CA C 43.166 0.0 . 162 22 22 GLY N N 109.1 0.0 . 163 23 23 THR H H 7.894 0.0 . 164 23 23 THR HA H 4.489 0.0 . 165 23 23 THR HB H 4.206 0.0 . 166 23 23 THR HG2 H 1.154 0.0 . 167 23 23 THR C C 170.17 0.0 . 168 23 23 THR CA C 61.304 0.0 . 169 23 23 THR CB C 67.455 0.0 . 170 23 23 THR N N 116.8 0.0 . 171 24 24 VAL H H 7.792 0.0 . 172 24 24 VAL HA H 5.084 0.0 . 173 24 24 VAL HB H 1.601 0.0 . 174 24 24 VAL HG1 H 0.83 0.0 . 175 24 24 VAL C C 171.629 0.0 . 176 24 24 VAL CA C 58.203 0.0 . 177 24 24 VAL CB C 31.847 0.0 . 178 24 24 VAL N N 123.1 0.0 . 179 25 25 ASP H H 8.906 0.0 . 180 25 25 ASP HA H 4.313 0.0 . 181 25 25 ASP HB2 H 2.734 0.0 . 182 25 25 ASP HB3 H 3.018 0.0 . 183 25 25 ASP C C 170.281 0.0 . 184 25 25 ASP CA C 50.847 0.0 . 185 25 25 ASP CB C 38.73 0.0 . 186 25 25 ASP N N 131.2 0.0 . 187 26 26 GLY H H 7.891 0.0 . 188 26 26 GLY HA2 H 5.029 0.0 . 189 26 26 GLY HA3 H 3.015 0.0 . 190 26 26 GLY C C 169.975 0.0 . 191 26 26 GLY CA C 42.057 0.0 . 192 26 26 GLY N N 102.5 0.0 . 193 27 27 THR H H 8.529 0.0 . 194 27 27 THR HA H 5.189 0.0 . 195 27 27 THR HB H 3.986 0.0 . 196 27 27 THR HG2 H 1.344 0.0 . 197 27 27 THR C C 170.554 0.0 . 198 27 27 THR CA C 56.74 0.0 . 199 27 27 THR CB C 67.326 0.0 . 200 27 27 THR N N 112.7 0.0 . 201 28 28 ARG H H 8.993 0.0 . 202 28 28 ARG HA H 4.691 0.0 . 203 28 28 ARG HB2 H 1.744 0.0 . 204 28 28 ARG HB3 H 2.078 0.0 . 205 28 28 ARG C C 173.45 0.0 . 206 28 28 ARG CA C 54.938 0.0 . 207 28 28 ARG CB C 34.26 0.0 . 208 28 28 ARG N N 127.5 0.0 . 209 29 29 ASP H H 8.323 0.0 . 210 29 29 ASP HA H 4.661 0.0 . 211 29 29 ASP HB2 H 2.671 0.0 . 212 29 29 ASP HB3 H 3.222 0.0 . 213 29 29 ASP C C 172.275 0.0 . 214 29 29 ASP CA C 50.779 0.0 . 215 29 29 ASP CB C 38.511 0.0 . 216 29 29 ASP N N 121.0 0.0 . 217 30 30 ARG H H 8.342 0.0 . 218 30 30 ARG HA H 3.592 0.0 . 219 30 30 ARG HB3 H 1.777 0.0 . 220 30 30 ARG HG2 H 1.446 0.0 . 221 30 30 ARG HD2 H 3.124 0.0 . 222 30 30 ARG C C 173.454 0.0 . 223 30 30 ARG CA C 54.924 0.0 . 224 30 30 ARG CB C 28.367 0.0 . 225 30 30 ARG N N 126.1 0.0 . 226 31 31 SER H H 8.379 0.0 . 227 31 31 SER HA H 4.397 0.0 . 228 31 31 SER HB2 H 4.033 0.0 . 229 31 31 SER HB3 H 4.033 0.0 . 230 31 31 SER C C 171.758 0.0 . 231 31 31 SER CA C 55.918 0.0 . 232 31 31 SER CB C 61.807 0.0 . 233 31 31 SER N N 113.6 0.0 . 234 32 32 ASP H H 7.105 0.0 . 235 32 32 ASP HA H 4.276 0.0 . 236 32 32 ASP HB2 H 2.707 0.0 . 237 32 32 ASP HB3 H 2.771 0.0 . 238 32 32 ASP C C 174.497 0.0 . 239 32 32 ASP CA C 53.116 0.0 . 240 32 32 ASP CB C 41.585 0.0 . 241 32 32 ASP N N 125.0 0.0 . 242 33 33 GLN H H 8.775 0.0 . 243 33 33 GLN HA H 4.061 0.0 . 244 33 33 GLN HB2 H 1.643 0.0 . 245 33 33 GLN HB3 H 1.52 0.0 . 246 33 33 GLN HG2 H 2.098 0.0 . 247 33 33 GLN HE21 H 7.36 0.0 . 248 33 33 GLN HE22 H 6.66 0.0 . 249 33 33 GLN C C 174.9 0.0 . 250 33 33 GLN CA C 55.127 0.0 . 251 33 33 GLN CB C 26.601 0.0 . 252 33 33 GLN N N 124.7 0.0 . 253 33 33 GLN NE2 N 112.0 0.0 . 254 34 34 HIS H H 9.681 0.0 . 255 34 34 HIS HA H 4.885 0.0 . 256 34 34 HIS HB2 H 3.037 0.0 . 257 34 34 HIS HB3 H 3.964 0.0 . 258 34 34 HIS C C 172.307 0.0 . 259 34 34 HIS CA C 55.739 0.0 . 260 34 34 HIS CB C 26.065 0.0 . 261 34 34 HIS N N 116.7 0.0 . 262 35 35 ILE H H 6.711 0.0 . 263 35 35 ILE HA H 5.114 0.0 . 264 35 35 ILE HB H 2.427 0.0 . 265 35 35 ILE HG12 H 1.113 0.0 . 266 35 35 ILE HG2 H 0.83 0.0 . 267 35 35 ILE HD1 H 0.54 0.0 . 268 35 35 ILE C C 172.249 0.0 . 269 35 35 ILE CA C 58.395 0.0 . 270 35 35 ILE CB C 35.989 0.0 . 271 35 35 ILE N N 108.6 0.0 . 272 36 36 GLN H H 7.178 0.0 . 273 36 36 GLN HA H 4.261 0.0 . 274 36 36 GLN HB2 H 1.877 0.0 . 275 36 36 GLN HB3 H 2.112 0.0 . 276 36 36 GLN HG2 H 2.082 0.0 . 277 36 36 GLN HE21 H 7.438 0.0 . 278 36 36 GLN HE22 H 6.63 0.0 . 279 36 36 GLN C C 172.952 0.0 . 280 36 36 GLN CA C 55.111 0.0 . 281 36 36 GLN CB C 25.19 0.0 . 282 36 36 GLN N N 120.018 0.0 . 283 36 36 GLN NE2 N 110.1 0.0 . 284 37 37 LEU H H 9.11 0.0 . 285 37 37 LEU HA H 5.315 0.0 . 286 37 37 LEU HB2 H 1.047 0.0 . 287 37 37 LEU HB3 H 1.599 0.0 . 288 37 37 LEU HD1 H 0.72 0.0 . 289 37 37 LEU HD2 H 0.59 0.0 . 290 37 37 LEU C C 172.877 0.0 . 291 37 37 LEU CA C 51.329 0.0 . 292 37 37 LEU CB C 42.165 0.0 . 293 37 37 LEU N N 127.6 0.0 . 294 38 38 GLN H H 9.556 0.0 . 295 38 38 GLN HA H 4.623 0.0 . 296 38 38 GLN HB2 H 1.789 0.0 . 297 38 38 GLN HB3 H 1.874 0.0 . 298 38 38 GLN HG2 H 2.041 0.0 . 299 38 38 GLN C C 172.676 0.0 . 300 38 38 GLN CA C 51.81 0.0 . 301 38 38 GLN CB C 29.259 0.0 . 302 38 38 GLN N N 120.583 0.0 . 303 39 39 LEU H H 8.926 0.0 . 304 39 39 LEU HA H 5.506 0.0 . 305 39 39 LEU HB2 H 1.569 0.0 . 306 39 39 LEU HB3 H 1.668 0.0 . 307 39 39 LEU HD1 H 0.892 0.0 . 308 39 39 LEU HD2 H 0.779 0.0 . 309 39 39 LEU C C 174.601 0.0 . 310 39 39 LEU CA C 53.062 0.0 . 311 39 39 LEU CB C 40.765 0.0 . 312 39 39 LEU N N 131.7 0.0 . 313 40 40 SER H H 8.569 0.0 . 314 40 40 SER HA H 4.676 0.0 . 315 40 40 SER HB2 H 3.809 0.0 . 316 40 40 SER HB3 H 3.873 0.0 . 317 40 40 SER C C 170.046 0.0 . 318 40 40 SER CA C 54.925 0.0 . 319 40 40 SER CB C 59.614 0.0 . 320 40 40 SER N N 115.9 0.0 . 321 41 41 ALA H H 8.357 0.0 . 322 41 41 ALA HA H 5.016 0.0 . 323 41 41 ALA HB H 1.34 0.0 . 324 41 41 ALA C C 175.352 0.0 . 325 41 41 ALA CA C 49.309 0.0 . 326 41 41 ALA CB C 17.456 0.0 . 327 41 41 ALA N N 125.9 0.0 . 328 42 42 GLU H H 8.485 0.0 . 329 42 42 GLU HA H 4.444 0.0 . 330 42 42 GLU HB2 H 1.814 0.0 . 331 42 42 GLU HB3 H 2.2 0.0 . 332 42 42 GLU HG2 H 2.324 0.0 . 333 42 42 GLU HG3 H 2.2 0.0 . 334 42 42 GLU C C 174.014 0.0 . 335 42 42 GLU CA C 54.611 0.0 . 336 42 42 GLU CB C 28.181 0.0 . 337 42 42 GLU N N 125.4 0.0 . 338 43 43 SER H H 8.02 0.0 . 339 43 43 SER HA H 4.516 0.0 . 340 43 43 SER HB2 H 3.722 0.0 . 341 43 43 SER HB3 H 3.814 0.0 . 342 43 43 SER C C 171.119 0.0 . 343 43 43 SER CA C 55.014 0.0 . 344 43 43 SER CB C 61.687 0.0 . 345 43 43 SER N N 113.9 0.0 . 346 44 44 VAL H H 8.113 0.0 . 347 44 44 VAL HA H 3.868 0.0 . 348 44 44 VAL HB H 2.057 0.0 . 349 44 44 VAL HG1 H 1.154 0.0 . 350 44 44 VAL HG2 H 1.082 0.0 . 351 44 44 VAL C C 175.533 0.0 . 352 44 44 VAL CA C 62.838 0.0 . 353 44 44 VAL CB C 28.991 0.0 . 354 44 44 VAL N N 121.1 0.0 . 355 45 45 GLY H H 8.807 0.0 . 356 45 45 GLY HA2 H 4.296 0.0 . 357 45 45 GLY HA3 H 3.995 0.0 . 358 45 45 GLY C C 170.948 0.0 . 359 45 45 GLY CA C 43.553 0.0 . 360 45 45 GLY N N 115.545 0.0 . 361 46 46 GLU H H 7.985 0.0 . 362 46 46 GLU HA H 5.442 0.0 . 363 46 46 GLU HB2 H 1.82 0.0 . 364 46 46 GLU HB3 H 1.842 0.0 . 365 46 46 GLU HG2 H 2.149 0.0 . 366 46 46 GLU HG3 H 2.087 0.0 . 367 46 46 GLU C C 173.583 0.0 . 368 46 46 GLU CA C 52.751 0.0 . 369 46 46 GLU CB C 29.432 0.0 . 370 46 46 GLU N N 121.2 0.0 . 371 47 47 VAL H H 9.56 0.0 . 372 47 47 VAL HA H 5.505 0.0 . 373 47 47 VAL HB H 2.296 0.0 . 374 47 47 VAL HG1 H 0.979 0.0 . 375 47 47 VAL HG2 H 0.871 0.0 . 376 47 47 VAL C C 172.96 0.0 . 377 47 47 VAL CA C 56.846 0.0 . 378 47 47 VAL CB C 33.714 0.0 . 379 47 47 VAL N N 116.4 0.0 . 380 48 48 TYR H H 8.415 0.0 . 381 48 48 TYR HA H 5.29 0.0 . 382 48 48 TYR HB2 H 3.035 0.0 . 383 48 48 TYR HB3 H 3.286 0.0 . 384 48 48 TYR C C 173.423 0.0 . 385 48 48 TYR CA C 54.331 0.0 . 386 48 48 TYR CB C 39.296 0.0 . 387 48 48 TYR N N 117.4 0.0 . 388 49 49 ILE H H 10.532 0.0 . 389 49 49 ILE HA H 4.341 0.0 . 390 49 49 ILE HB H 1.65 0.0 . 391 49 49 ILE HG12 H 1.231 0.0 . 392 49 49 ILE HD1 H -0.17 0.0 . 393 49 49 ILE C C 170.853 0.0 . 394 49 49 ILE CA C 59.573 0.0 . 395 49 49 ILE CB C 40.504 0.0 . 396 49 49 ILE N N 123.1 0.0 . 397 50 50 LYS H H 9.111 0.0 . 398 50 50 LYS HA H 4.991 0.0 . 399 50 50 LYS HB2 H 1.113 0.0 . 400 50 50 LYS HB3 H 1.303 0.0 . 401 50 50 LYS HG2 H 0.861 0.0 . 402 50 50 LYS HG3 H 0.654 0.0 . 403 50 50 LYS HD2 H 1.302 0.0 . 404 50 50 LYS HE2 H 2.6 0.0 . 405 50 50 LYS HE3 H 2.5 0.0 . 406 50 50 LYS C C 173.759 0.0 . 407 50 50 LYS CA C 51.179 0.0 . 408 50 50 LYS CB C 34.816 0.0 . 409 50 50 LYS N N 122.8 0.0 . 410 51 51 SER H H 8.92 0.0 . 411 51 51 SER HA H 4.666 0.0 . 412 51 51 SER HB2 H 3.883 0.0 . 413 51 51 SER HB3 H 3.883 0.0 . 414 51 51 SER C C 175.084 0.0 . 415 51 51 SER CA C 55.043 0.0 . 416 51 51 SER CB C 61.065 0.0 . 417 51 51 SER N N 117.579 0.0 . 418 52 52 THR H H 8.342 0.0 . 419 52 52 THR HA H 3.996 0.0 . 420 52 52 THR HB H 4.193 0.0 . 421 52 52 THR HG2 H 1.446 0.0 . 422 52 52 THR C C 173.566 0.0 . 423 52 52 THR CA C 62.792 0.0 . 424 52 52 THR CB C 65.611 0.0 . 425 52 52 THR N N 123.2 0.0 . 426 53 53 GLU H H 8.312 0.0 . 427 53 53 GLU HA H 4.311 0.0 . 428 53 53 GLU HB2 H 1.912 0.0 . 429 53 53 GLU HB3 H 2.207 0.0 . 430 53 53 GLU C C 175.327 0.0 . 431 53 53 GLU CA C 55.889 0.0 . 432 53 53 GLU CB C 28.359 0.0 . 433 53 53 GLU N N 122.0 0.0 . 434 54 54 THR H H 7.724 0.0 . 435 54 54 THR HA H 4.681 0.0 . 436 54 54 THR HB H 4.528 0.0 . 437 54 54 THR HG2 H 1.184 0.0 . 438 54 54 THR C C 173.942 0.0 . 439 54 54 THR CA C 58.555 0.0 . 440 54 54 THR CB C 69.03 0.0 . 441 54 54 THR N N 103.1 0.0 . 442 55 55 GLY H H 7.643 0.0 . 443 55 55 GLY HA2 H 4.15 0.0 . 444 55 55 GLY HA3 H 3.591 0.0 . 445 55 55 GLY C C 170.694 0.0 . 446 55 55 GLY CA C 43.594 0.0 . 447 55 55 GLY N N 110.7 0.0 . 448 56 56 GLN H H 7.281 0.0 . 449 56 56 GLN HA H 4.311 0.0 . 450 56 56 GLN HB2 H 1.591 0.0 . 451 56 56 GLN HB3 H 1.591 0.0 . 452 56 56 GLN HE21 H 7.02 0.0 . 453 56 56 GLN HE22 H 6.38 0.0 . 454 56 56 GLN C C 172.141 0.0 . 455 56 56 GLN CA C 53.898 0.0 . 456 56 56 GLN CB C 30.456 0.0 . 457 56 56 GLN N N 115.0 0.0 . 458 56 56 GLN NE2 N 106.6 0.0 . 459 57 57 TYR H H 9.254 0.0 . 460 57 57 TYR HA H 4.128 0.0 . 461 57 57 TYR HB2 H 2.811 0.0 . 462 57 57 TYR HB3 H 3.161 0.0 . 463 57 57 TYR C C 173.32 0.0 . 464 57 57 TYR CA C 53.356 0.0 . 465 57 57 TYR CB C 40.466 0.0 . 466 57 57 TYR N N 119.4 0.0 . 467 58 58 LEU H H 9.126 0.0 . 468 58 58 LEU HA H 4.128 0.0 . 469 58 58 LEU HB2 H 1.037 0.0 . 470 58 58 LEU HB3 H 1.939 0.0 . 471 58 58 LEU HG H 1.733 0.0 . 472 58 58 LEU HD1 H 0.435 0.0 . 473 58 58 LEU C C 172.32 0.0 . 474 58 58 LEU CA C 53.256 0.0 . 475 58 58 LEU CB C 40.466 0.0 . 476 58 58 LEU N N 123.6 0.0 . 477 59 59 ALA H H 8.656 0.0 . 478 59 59 ALA HA H 5.124 0.0 . 479 59 59 ALA HB H 0.611 0.0 . 480 59 59 ALA C C 172.722 0.0 . 481 59 59 ALA CA C 48.45 0.0 . 482 59 59 ALA CB C 21.261 0.0 . 483 59 59 ALA N N 126.947 0.0 . 484 60 60 MET H H 7.521 0.0 . 485 60 60 MET HA H 5.527 0.0 . 486 60 60 MET HB2 H 2.192 0.0 . 487 60 60 MET HB3 H 2.385 0.0 . 488 60 60 MET HG2 H 2.785 0.0 . 489 60 60 MET HG3 H 2.2 0.0 . 490 60 60 MET C C 173.753 0.0 . 491 60 60 MET CA C 52.251 0.0 . 492 60 60 MET CB C 35.046 0.0 . 493 60 60 MET N N 116.602 0.0 . 494 61 61 ASP H H 9.159 0.0 . 495 61 61 ASP HA H 5.046 0.0 . 496 61 61 ASP HB2 H 2.87 0.0 . 497 61 61 ASP HB3 H 3.586 0.0 . 498 61 61 ASP C C 175.8 0.0 . 499 61 61 ASP CA C 51.48 0.0 . 500 61 61 ASP CB C 39.346 0.0 . 501 61 61 ASP N N 128.445 0.0 . 502 62 62 THR H H 7.972 0.0 . 503 62 62 THR HA H 4.134 0.0 . 504 62 62 THR HB H 4.503 0.0 . 505 62 62 THR HG2 H 1.662 0.0 . 506 62 62 THR C C 172.355 0.0 . 507 62 62 THR CA C 62.626 0.0 . 508 62 62 THR CB C 66.955 0.0 . 509 62 62 THR N N 107.806 0.0 . 510 63 63 ASP H H 8.333 0.0 . 511 63 63 ASP HA H 4.964 0.0 . 512 63 63 ASP HB2 H 2.769 0.0 . 513 63 63 ASP HB3 H 2.749 0.0 . 514 63 63 ASP C C 174.438 0.0 . 515 63 63 ASP CA C 51.865 0.0 . 516 63 63 ASP CB C 39.182 0.0 . 517 63 63 ASP N N 119.831 0.0 . 518 64 64 GLY H H 8.264 0.0 . 519 64 64 GLY HA2 H 3.652 0.0 . 520 64 64 GLY HA3 H 3.397 0.0 . 521 64 64 GLY C C 171.248 0.0 . 522 64 64 GLY CA C 42.923 0.0 . 523 64 64 GLY N N 109.142 0.0 . 524 65 65 LEU H H 8.636 0.0 . 525 65 65 LEU HA H 4.529 0.0 . 526 65 65 LEU HB2 H 1.567 0.0 . 527 65 65 LEU HB3 H 2.054 0.0 . 528 65 65 LEU HG H 2.447 0.0 . 529 65 65 LEU HD1 H 1.143 0.0 . 530 65 65 LEU HD2 H 0.995 0.0 . 531 65 65 LEU C C 174.507 0.0 . 532 65 65 LEU CA C 52.224 0.0 . 533 65 65 LEU CB C 40.557 0.0 . 534 65 65 LEU N N 123.137 0.0 . 535 66 66 LEU H H 7.431 0.0 . 536 66 66 LEU HA H 5.714 0.0 . 537 66 66 LEU HB2 H 1.434 0.0 . 538 66 66 LEU HB3 H 1.139 0.0 . 539 66 66 LEU HG H 2.164 0.0 . 540 66 66 LEU HD1 H 1.42 0.0 . 541 66 66 LEU HD2 H 1.02 0.0 . 542 66 66 LEU C C 174.07 0.0 . 543 66 66 LEU CA C 51.635 0.0 . 544 66 66 LEU CB C 40.474 0.0 . 545 66 66 LEU N N 124.493 0.0 . 546 67 67 TYR H H 9.237 0.0 . 547 67 67 TYR HA H 5.023 0.0 . 548 67 67 TYR HB2 H 3.111 0.0 . 549 67 67 TYR C C 169.64 0.0 . 550 67 67 TYR CA C 54.076 0.0 . 551 67 67 TYR CB C 38.903 0.0 . 552 67 67 TYR N N 120.36 0.0 . 553 68 68 GLY H H 8.928 0.0 . 554 68 68 GLY HA2 H 4.676 0.0 . 555 68 68 GLY C C 170.551 0.0 . 556 68 68 GLY CA C 41.569 0.0 . 557 68 68 GLY N N 105.646 0.0 . 558 69 69 SER H H 9.608 0.0 . 559 69 69 SER HA H 4.966 0.0 . 560 69 69 SER HB2 H 3.552 0.0 . 561 69 69 SER HB3 H 3.915 0.0 . 562 69 69 SER C C 174.219 0.0 . 563 69 69 SER CA C 53.737 0.0 . 564 69 69 SER CB C 63.042 0.0 . 565 69 69 SER N N 120.1 0.0 . 566 70 70 GLN H H 9.343 0.0 . 567 70 70 GLN HA H 4.286 0.0 . 568 70 70 GLN HB2 H 2.216 0.0 . 569 70 70 GLN HB3 H 2.331 0.0 . 570 70 70 GLN HG2 H 2.539 0.0 . 571 70 70 GLN HG3 H 2.667 0.0 . 572 70 70 GLN HE21 H 7.36 0.0 . 573 70 70 GLN HE22 H 6.86 0.0 . 574 70 70 GLN C C 173.241 0.0 . 575 70 70 GLN CA C 56.139 0.0 . 576 70 70 GLN CB C 27.092 0.0 . 577 70 70 GLN N N 127.339 0.0 . 578 70 70 GLN NE2 N 112.2 0.0 . 579 71 71 THR H H 7.532 0.0 . 580 71 71 THR HA H 4.78 0.0 . 581 71 71 THR HB H 4.15 0.0 . 582 71 71 THR CA C 55.203 0.0 . 583 71 71 THR N N 108.1 0.0 . 584 72 72 PRO HA H 4.173 0.0 . 585 72 72 PRO HB2 H 2.325 0.0 . 586 72 72 PRO HB3 H 1.31 0.0 . 587 72 72 PRO C C 172.92 0.0 . 588 72 72 PRO CA C 60.05 0.0 . 589 72 72 PRO CB C 29.254 0.0 . 590 73 73 ASN H H 7.321 0.0 . 591 73 73 ASN CA C 49.994 0.0 . 592 73 73 ASN N N 119.2 0.0 . 593 74 74 GLU H H 9.03 0.0 . 594 74 74 GLU HA H 4.13 0.0 . 595 74 74 GLU HB2 H 2.12 0.0 . 596 74 74 GLU HB3 H 2.117 0.0 . 597 74 74 GLU HG2 H 2.529 0.0 . 598 74 74 GLU HG3 H 2.529 0.0 . 599 74 74 GLU C C 176.352 0.0 . 600 74 74 GLU CA C 57.131 0.0 . 601 74 74 GLU CB C 27.005 0.0 . 602 75 75 GLU H H 8.574 0.0 . 603 75 75 GLU HA H 4.206 0.0 . 604 75 75 GLU HB2 H 2.468 0.0 . 605 75 75 GLU HB3 H 2.631 0.0 . 606 75 75 GLU HG2 H 2.434 0.0 . 607 75 75 GLU HG3 H 2.621 0.0 . 608 75 75 GLU C C 173.866 0.0 . 609 75 75 GLU CA C 56.343 0.0 . 610 75 75 GLU CB C 26.028 0.0 . 611 75 75 GLU N N 119.2 0.0 . 612 76 76 CYS H H 7.727 0.0 . 613 76 76 CYS HA H 5.426 0.0 . 614 76 76 CYS HB2 H 3.315 0.0 . 615 76 76 CYS HB3 H 3.71 0.0 . 616 76 76 CYS C C 170.849 0.0 . 617 76 76 CYS CA C 55.635 0.0 . 618 76 76 CYS CB C 26.036 0.0 . 619 76 76 CYS N N 113.8 0.0 . 620 77 77 LEU H H 6.241 0.0 . 621 77 77 LEU HA H 4.555 0.0 . 622 77 77 LEU HB2 H 1.163 0.0 . 623 77 77 LEU HB3 H 1.423 0.0 . 624 77 77 LEU HG H 1.27 0.0 . 625 77 77 LEU HD1 H 0.65 0.0 . 626 77 77 LEU HD2 H 0.38 0.0 . 627 77 77 LEU C C 173.882 0.0 . 628 77 77 LEU CA C 51.793 0.0 . 629 77 77 LEU CB C 42.123 0.0 . 630 77 77 LEU N N 118.069 0.0 . 631 78 78 PHE H H 9.067 0.0 . 632 78 78 PHE HA H 5.169 0.0 . 633 78 78 PHE HB2 H 2.804 0.0 . 634 78 78 PHE HB3 H 2.936 0.0 . 635 78 78 PHE C C 171.853 0.0 . 636 78 78 PHE CA C 54.917 0.0 . 637 78 78 PHE CB C 40.597 0.0 . 638 78 78 PHE N N 122.377 0.0 . 639 79 79 LEU H H 9.958 0.0 . 640 79 79 LEU HA H 4.686 0.0 . 641 79 79 LEU HB2 H 1.9 0.0 . 642 79 79 LEU HG H 1.573 0.0 . 643 79 79 LEU HD1 H 0.935 0.0 . 644 79 79 LEU C C 173.055 0.0 . 645 79 79 LEU CA C 51.232 0.0 . 646 79 79 LEU CB C 38.511 0.0 . 647 79 79 LEU N N 122.126 0.0 . 648 80 80 GLU H H 8.347 0.0 . 649 80 80 GLU HA H 4.832 0.0 . 650 80 80 GLU HB2 H 1.926 0.0 . 651 80 80 GLU HB3 H 2.079 0.0 . 652 80 80 GLU C C 173.355 0.0 . 653 80 80 GLU CA C 52.558 0.0 . 654 80 80 GLU CB C 30.892 0.0 . 655 80 80 GLU N N 126.3 0.0 . 656 81 81 ARG H H 8.84 0.0 . 657 81 81 ARG HA H 4.659 0.0 . 658 81 81 ARG HB2 H 1.83 0.0 . 659 81 81 ARG HB3 H 1.84 0.0 . 660 81 81 ARG HG2 H 1.567 0.0 . 661 81 81 ARG HG3 H 1.482 0.0 . 662 81 81 ARG HD2 H 3.19 0.0 . 663 81 81 ARG C C 172.258 0.0 . 664 81 81 ARG CA C 52.288 0.0 . 665 81 81 ARG CB C 36.453 0.0 . 666 81 81 ARG N N 129.522 0.0 . 667 82 82 LEU H H 8.347 0.0 . 668 82 82 LEU HA H 4.875 0.0 . 669 82 82 LEU HB2 H 1.505 0.0 . 670 82 82 LEU HB3 H 1.746 0.0 . 671 82 82 LEU HG H 1.706 0.0 . 672 82 82 LEU HD1 H 0.848 0.0 . 673 82 82 LEU C C 174.567 0.0 . 674 82 82 LEU CA C 52.631 0.0 . 675 82 82 LEU CB C 40.304 0.0 . 676 82 82 LEU N N 125.7 0.0 . 677 83 83 GLU H H 7.204 0.0 . 678 83 83 GLU HA H 4.974 0.0 . 679 83 83 GLU HG2 H 2.208 0.0 . 680 83 83 GLU HG3 H 2.208 0.0 . 681 83 83 GLU C C 174.885 0.0 . 682 83 83 GLU CA C 51.723 0.0 . 683 83 83 GLU CB C 33.703 0.0 . 684 83 83 GLU N N 116.1 0.0 . 685 84 84 GLU H H 8.626 0.0 . 686 84 84 GLU HA H 4.112 0.0 . 687 84 84 GLU HB2 H 2.165 0.0 . 688 84 84 GLU HG2 H 2.355 0.0 . 689 84 84 GLU HG3 H 2.355 0.0 . 690 84 84 GLU C C 174.261 0.0 . 691 84 84 GLU CA C 55.553 0.0 . 692 84 84 GLU CB C 27.117 0.0 . 693 84 84 GLU N N 120.3 0.0 . 694 85 85 ASN H H 8.429 0.0 . 695 85 85 ASN HA H 4.343 0.0 . 696 85 85 ASN HB2 H 2.998 0.0 . 697 85 85 ASN HB3 H 3.092 0.0 . 698 85 85 ASN C C 172.203 0.0 . 699 85 85 ASN CA C 51.788 0.0 . 700 85 85 ASN CB C 35.301 0.0 . 701 85 85 ASN N N 114.8 0.0 . 702 86 86 HIS H H 8.081 0.0 . 703 86 86 HIS HA H 4.26 0.0 . 704 86 86 HIS HB2 H 3.284 0.0 . 705 86 86 HIS HB3 H 3.442 0.0 . 706 86 86 HIS C C 171.039 0.0 . 707 86 86 HIS CA C 55.255 0.0 . 708 86 86 HIS CB C 24.858 0.0 . 709 86 86 HIS N N 108.737 0.0 . 710 87 87 TYR H H 7.632 0.0 . 711 87 87 TYR HA H 4.836 0.0 . 712 87 87 TYR HB2 H 2.959 0.0 . 713 87 87 TYR C C 171.983 0.0 . 714 87 87 TYR CA C 56.163 0.0 . 715 87 87 TYR CB C 38.643 0.0 . 716 87 87 TYR N N 117.738 0.0 . 717 88 88 ASN H H 9.84 0.0 . 718 88 88 ASN HA H 5.837 0.0 . 719 88 88 ASN HB2 H 2.486 0.0 . 720 88 88 ASN HB3 H 2.658 0.0 . 721 88 88 ASN HD21 H 6.72 0.0 . 722 88 88 ASN HD22 H 6.5 0.0 . 723 88 88 ASN C C 172.471 0.0 . 724 88 88 ASN CA C 50.063 0.0 . 725 88 88 ASN CB C 40.242 0.0 . 726 88 88 ASN N N 118.891 0.0 . 727 88 88 ASN ND2 N 106.93 0.0 . 728 89 89 THR H H 8.38 0.0 . 729 89 89 THR HA H 5.127 0.0 . 730 89 89 THR HB H 4.58 0.0 . 731 89 89 THR HG2 H 1.319 0.0 . 732 89 89 THR C C 170.548 0.0 . 733 89 89 THR CA C 57.357 0.0 . 734 89 89 THR CB C 70.868 0.0 . 735 89 89 THR N N 108.521 0.0 . 736 90 90 TYR H H 10.247 0.0 . 737 90 90 TYR HA H 5.472 0.0 . 738 90 90 TYR HB2 H 2.471 0.0 . 739 90 90 TYR C C 172.442 0.0 . 740 90 90 TYR CA C 55.106 0.0 . 741 90 90 TYR CB C 39.047 0.0 . 742 90 90 TYR N N 119.0 0.0 . 743 91 91 ILE H H 8.781 0.0 . 744 91 91 ILE HA H 4.673 0.0 . 745 91 91 ILE HG12 H 1.288 0.0 . 746 91 91 ILE HG2 H 0.631 0.0 . 747 91 91 ILE HD1 H 0.562 0.0 . 748 91 91 ILE C C 172.924 0.0 . 749 91 91 ILE CA C 56.346 0.0 . 750 91 91 ILE CB C 36.627 0.0 . 751 91 91 ILE N N 122.546 0.0 . 752 92 92 SER H H 8.191 0.0 . 753 92 92 SER HA H 4.016 0.0 . 754 92 92 SER HB2 H 3.816 0.0 . 755 92 92 SER C C 172.863 0.0 . 756 92 92 SER CA C 55.781 0.0 . 757 92 92 SER CB C 62.382 0.0 . 758 92 92 SER N N 120.2 0.0 . 759 93 93 LYS H H 7.993 0.0 . 760 93 93 LYS HA H 3.779 0.0 . 761 93 93 LYS HB2 H 1.19 0.0 . 762 93 93 LYS HB3 H 1.766 0.0 . 763 93 93 LYS HG2 H 1.203 0.0 . 764 93 93 LYS HE2 H 2.912 0.0 . 765 93 93 LYS HE3 H 2.657 0.0 . 766 93 93 LYS C C 176.938 0.0 . 767 93 93 LYS CA C 57.942 0.0 . 768 93 93 LYS CB C 30.889 0.0 . 769 93 93 LYS N N 130.618 0.0 . 770 94 94 LYS H H 8.616 0.0 . 771 94 94 LYS HA H 3.851 0.0 . 772 94 94 LYS HB2 H 1.342 0.0 . 773 94 94 LYS HB3 H 1.475 0.0 . 774 94 94 LYS HG2 H 0.948 0.0 . 775 94 94 LYS HG3 H 0.593 0.0 . 776 94 94 LYS HD2 H 1.435 0.0 . 777 94 94 LYS HE2 H 2.919 0.0 . 778 94 94 LYS C C 174.491 0.0 . 779 94 94 LYS CA C 55.868 0.0 . 780 94 94 LYS CB C 30.329 0.0 . 781 94 94 LYS N N 120.044 0.0 . 782 95 95 HIS H H 7.249 0.0 . 783 95 95 HIS HA H 4.604 0.0 . 784 95 95 HIS HB2 H 2.47 0.0 . 785 95 95 HIS HB3 H 2.524 0.0 . 786 95 95 HIS C C 173.734 0.0 . 787 95 95 HIS CA C 51.18 0.0 . 788 95 95 HIS CB C 26.844 0.0 . 789 95 95 HIS N N 114.486 0.0 . 790 96 96 ALA H H 7.104 0.0 . 791 96 96 ALA HA H 4.131 0.0 . 792 96 96 ALA HB H 2.116 0.0 . 793 96 96 ALA C C 178.508 0.0 . 794 96 96 ALA CA C 53.758 0.0 . 795 96 96 ALA CB C 16.578 0.0 . 796 96 96 ALA N N 125.204 0.0 . 797 97 97 GLU H H 8.857 0.0 . 798 97 97 GLU HA H 4.063 0.0 . 799 97 97 GLU HB2 H 1.965 0.0 . 800 97 97 GLU HG2 H 2.278 0.0 . 801 97 97 GLU HG3 H 2.154 0.0 . 802 97 97 GLU C C 174.813 0.0 . 803 97 97 GLU CA C 56.153 0.0 . 804 97 97 GLU CB C 26.241 0.0 . 805 97 97 GLU N N 118.007 0.0 . 806 98 98 LYS H H 7.196 0.0 . 807 98 98 LYS HA H 4.28 0.0 . 808 98 98 LYS HB2 H 1.934 0.0 . 809 98 98 LYS HB3 H 1.735 0.0 . 810 98 98 LYS HG2 H 0.756 0.0 . 811 98 98 LYS HD2 H 1.459 0.0 . 812 98 98 LYS HE2 H 2.278 0.0 . 813 98 98 LYS C C 173.361 0.0 . 814 98 98 LYS CA C 52.852 0.0 . 815 98 98 LYS CB C 29.959 0.0 . 816 98 98 LYS N N 116.241 0.0 . 817 99 99 ASN H H 7.842 0.0 . 818 99 99 ASN HA H 4.562 0.0 . 819 99 99 ASN HB2 H 2.816 0.0 . 820 99 99 ASN HB3 H 2.973 0.0 . 821 99 99 ASN HD21 H 7.4 0.0 . 822 99 99 ASN HD22 H 6.47 0.0 . 823 99 99 ASN C C 170.506 0.0 . 824 99 99 ASN CA C 52.24 0.0 . 825 99 99 ASN CB C 35.289 0.0 . 826 99 99 ASN N N 113.0 0.0 . 827 99 99 ASN ND2 N 112.85 0.0 . 828 100 100 TRP H H 6.369 0.0 . 829 100 100 TRP HA H 4.816 0.0 . 830 100 100 TRP HB2 H 2.92 0.0 . 831 100 100 TRP HB3 H 3.141 0.0 . 832 100 100 TRP C C 171.701 0.0 . 833 100 100 TRP CA C 53.179 0.0 . 834 100 100 TRP CB C 28.228 0.0 . 835 100 100 TRP N N 116.0 0.0 . 836 101 101 PHE H H 8.026 0.0 . 837 101 101 PHE HA H 5.373 0.0 . 838 101 101 PHE HB2 H 2.722 0.0 . 839 101 101 PHE HB3 H 3.456 0.0 . 840 101 101 PHE C C 175.044 0.0 . 841 101 101 PHE CA C 55.472 0.0 . 842 101 101 PHE CB C 39.22 0.0 . 843 101 101 PHE N N 124.185 0.0 . 844 102 102 VAL H H 8.499 0.0 . 845 102 102 VAL HA H 3.939 0.0 . 846 102 102 VAL HB H 2.027 0.0 . 847 102 102 VAL HG1 H 0.508 0.0 . 848 102 102 VAL C C 174.22 0.0 . 849 102 102 VAL CA C 60.975 0.0 . 850 102 102 VAL CB C 30.243 0.0 . 851 102 102 VAL N N 120.282 0.0 . 852 103 103 GLY H H 8.996 0.0 . 853 103 103 GLY HA2 H 4.926 0.0 . 854 103 103 GLY HA3 H 3.18 0.0 . 855 103 103 GLY C C 169.388 0.0 . 856 103 103 GLY CA C 43.802 0.0 . 857 103 103 GLY N N 114.668 0.0 . 858 104 104 LEU H H 8.118 0.0 . 859 104 104 LEU HA H 4.959 0.0 . 860 104 104 LEU HB2 H 2.229 0.0 . 861 104 104 LEU HG H 1.629 0.0 . 862 104 104 LEU HD1 H 0.747 0.0 . 863 104 104 LEU HD2 H 0.631 0.0 . 864 104 104 LEU C C 174.252 0.0 . 865 104 104 LEU CA C 51.207 0.0 . 866 104 104 LEU CB C 43.579 0.0 . 867 104 104 LEU N N 119.1 0.0 . 868 105 105 LYS H H 8.847 0.0 . 869 105 105 LYS HA H 4.215 0.0 . 870 105 105 LYS HB2 H 1.781 0.0 . 871 105 105 LYS HB3 H 2.121 0.0 . 872 105 105 LYS HD2 H 1.737 0.0 . 873 105 105 LYS HD3 H 1.59 0.0 . 874 105 105 LYS HE2 H 3.128 0.0 . 875 105 105 LYS C C 176.404 0.0 . 876 105 105 LYS CA C 54.035 0.0 . 877 105 105 LYS N N 118.9 0.0 . 878 106 106 LYS H H 8.98 0.0 . 879 106 106 LYS HA H 3.624 0.0 . 880 106 106 LYS HB2 H 1.475 0.0 . 881 106 106 LYS HB3 H 1.761 0.0 . 882 106 106 LYS HG2 H 1.536 0.0 . 883 106 106 LYS HE2 H 3.082 0.0 . 884 106 106 LYS C C 174.499 0.0 . 885 106 106 LYS CA C 57.672 0.0 . 886 106 106 LYS CB C 29.78 0.0 . 887 106 106 LYS N N 122.172 0.0 . 888 107 107 ASN H H 7.352 0.0 . 889 107 107 ASN HA H 4.678 0.0 . 890 107 107 ASN HB2 H 2.762 0.0 . 891 107 107 ASN HB3 H 3.318 0.0 . 892 107 107 ASN C C 174.511 0.0 . 893 107 107 ASN CA C 49.523 0.0 . 894 107 107 ASN CB C 35.121 0.0 . 895 107 107 ASN N N 112.743 0.0 . 896 108 108 GLY H H 7.656 0.0 . 897 108 108 GLY HA2 H 3.358 0.0 . 898 108 108 GLY HA3 H 3.171 0.0 . 899 108 108 GLY C C 169.305 0.0 . 900 108 108 GLY CA C 42.207 0.0 . 901 108 108 GLY N N 109.9 0.0 . 902 109 109 SER H H 7.28 0.0 . 903 109 109 SER HA H 4.755 0.0 . 904 109 109 SER HB2 H 3.913 0.0 . 905 109 109 SER HB3 H 3.913 0.0 . 906 109 109 SER C C 171.244 0.0 . 907 109 109 SER CA C 55.139 0.0 . 908 109 109 SER CB C 62.749 0.0 . 909 109 109 SER N N 112.357 0.0 . 910 110 110 CYS H H 9.07 0.0 . 911 110 110 CYS HA H 4.296 0.0 . 912 110 110 CYS HB2 H 3.143 0.0 . 913 110 110 CYS HB3 H 3.217 0.0 . 914 110 110 CYS C C 172.131 0.0 . 915 110 110 CYS CA C 57.858 0.0 . 916 110 110 CYS CB C 37.322 0.0 . 917 110 110 CYS N N 119.883 0.0 . 918 111 111 LYS H H 8.095 0.0 . 919 111 111 LYS HA H 4.38 0.0 . 920 111 111 LYS HB2 H 1.458 0.0 . 921 111 111 LYS HB3 H 1.458 0.0 . 922 111 111 LYS HG2 H 1.134 0.0 . 923 111 111 LYS HD2 H 1.25 0.0 . 924 111 111 LYS C C 172.265 0.0 . 925 111 111 LYS CA C 52.117 0.0 . 926 111 111 LYS CB C 30.98 0.0 . 927 111 111 LYS N N 128.642 0.0 . 928 112 112 ARG H H 8.566 0.0 . 929 112 112 ARG HA H 4.252 0.0 . 930 112 112 ARG HB2 H 1.554 0.0 . 931 112 112 ARG HB3 H 1.554 0.0 . 932 112 112 ARG HG2 H 1.65 0.0 . 933 112 112 ARG HD2 H 3.143 0.0 . 934 112 112 ARG HD3 H 3.143 0.0 . 935 112 112 ARG C C 175.24 0.0 . 936 112 112 ARG CA C 54.295 0.0 . 937 112 112 ARG CB C 28.927 0.0 . 938 112 112 ARG N N 124.7 0.0 . 939 113 113 GLY H H 9.408 0.0 . 940 113 113 GLY HA2 H 3.51 0.0 . 941 113 113 GLY C C 169.61 0.0 . 942 113 113 GLY CA C 44.552 0.0 . 943 113 113 GLY N N 106.636 0.0 . 944 114 114 PRO HA H 4.321 0.0 . 945 114 114 PRO HB2 H 1.892 0.0 . 946 114 114 PRO HB3 H 2.36 0.0 . 947 114 114 PRO HG2 H 1.652 0.0 . 948 114 114 PRO HG3 H 1.505 0.0 . 949 114 114 PRO C C 174.543 0.0 . 950 114 114 PRO CA C 62.529 0.0 . 951 115 115 ARG H H 8.067 0.0 . 952 115 115 ARG HA H 4.508 0.0 . 953 115 115 ARG HB2 H 1.926 0.0 . 954 115 115 ARG HB3 H 2.133 0.0 . 955 115 115 ARG HD2 H 3.205 0.0 . 956 115 115 ARG HD3 H 3.082 0.0 . 957 115 115 ARG C C 174.68 0.0 . 958 115 115 ARG CA C 52.011 0.0 . 959 115 115 ARG CB C 27.143 0.0 . 960 115 115 ARG N N 114.5 0.0 . 961 116 116 THR H H 7.643 0.0 . 962 116 116 THR HA H 5.198 0.0 . 963 116 116 THR HB H 4.104 0.0 . 964 116 116 THR HG2 H 1.118 0.0 . 965 116 116 THR C C 172.573 0.0 . 966 116 116 THR CA C 58.712 0.0 . 967 116 116 THR CB C 70.086 0.0 . 968 116 116 THR N N 111.716 0.0 . 969 117 117 HIS H H 7.091 0.0 . 970 117 117 HIS HA H 4.868 0.0 . 971 117 117 HIS HB2 H 3.222 0.0 . 972 117 117 HIS HB3 H 3.4 0.0 . 973 117 117 HIS C C 170.344 0.0 . 974 117 117 HIS CA C 53.291 0.0 . 975 117 117 HIS CB C 29.133 0.0 . 976 117 117 HIS N N 112.914 0.0 . 977 118 118 TYR H H 9.02 0.0 . 978 118 118 TYR HA H 3.897 0.0 . 979 118 118 TYR HB2 H 2.936 0.0 . 980 118 118 TYR HB3 H 3.089 0.0 . 981 118 118 TYR C C 174.446 0.0 . 982 118 118 TYR CA C 58.801 0.0 . 983 118 118 TYR CB C 34.165 0.0 . 984 118 118 TYR N N 123.051 0.0 . 985 119 119 GLY H H 7.999 0.0 . 986 119 119 GLY HA2 H 4.385 0.0 . 987 119 119 GLY HA3 H 3.296 0.0 . 988 119 119 GLY C C 172.439 0.0 . 989 119 119 GLY CA C 42.599 0.0 . 990 119 119 GLY N N 116.885 0.0 . 991 120 120 GLN H H 7.003 0.0 . 992 120 120 GLN HA H 4.262 0.0 . 993 120 120 GLN HB2 H 2.005 0.0 . 994 120 120 GLN HB3 H 2.118 0.0 . 995 120 120 GLN C C 174.995 0.0 . 996 120 120 GLN CA C 52.617 0.0 . 997 120 120 GLN CB C 27.324 0.0 . 998 120 120 GLN N N 118.266 0.0 . 999 121 121 LYS H H 8.477 0.0 . 1000 121 121 LYS HA H 3.809 0.0 . 1001 121 121 LYS HB2 H 1.443 0.0 . 1002 121 121 LYS HB3 H 1.567 0.0 . 1003 121 121 LYS HG2 H 1.28 0.0 . 1004 121 121 LYS HD2 H 1.56 0.0 . 1005 121 121 LYS C C 172.702 0.0 . 1006 121 121 LYS CA C 56.243 0.0 . 1007 121 121 LYS CB C 29.598 0.0 . 1008 121 121 LYS N N 121.222 0.0 . 1009 122 122 ALA H H 7.526 0.0 . 1010 122 122 ALA HA H 3.947 0.0 . 1011 122 122 ALA HB H 1.143 0.0 . 1012 122 122 ALA C C 172.756 0.0 . 1013 122 122 ALA CA C 52.338 0.0 . 1014 122 122 ALA CB C 18.675 0.0 . 1015 122 122 ALA N N 116.019 0.0 . 1016 123 123 ILE H H 5.794 0.0 . 1017 123 123 ILE HA H 5.184 0.0 . 1018 123 123 ILE HB H 2.232 0.0 . 1019 123 123 ILE HG12 H 1.064 0.0 . 1020 123 123 ILE HG2 H 0.601 0.0 . 1021 123 123 ILE HD1 H -0.126 0.0 . 1022 123 123 ILE C C 172.79 0.0 . 1023 123 123 ILE CA C 57.297 0.0 . 1024 123 123 ILE CB C 35.425 0.0 . 1025 123 123 ILE N N 101.2 0.0 . 1026 124 124 LEU H H 6.716 0.0 . 1027 124 124 LEU HA H 4.597 0.0 . 1028 124 124 LEU HB2 H 0.67 0.0 . 1029 124 124 LEU HB3 H 0.67 0.0 . 1030 124 124 LEU HD1 H 0.407 0.0 . 1031 124 124 LEU HD2 H 0.407 0.0 . 1032 124 124 LEU C C 173.411 0.0 . 1033 124 124 LEU CA C 51.686 0.0 . 1034 124 124 LEU CB C 39.622 0.0 . 1035 124 124 LEU N N 121.554 0.0 . 1036 125 125 PHE H H 9.226 0.0 . 1037 125 125 PHE HA H 5.612 0.0 . 1038 125 125 PHE HB2 H 2.803 0.0 . 1039 125 125 PHE HB3 H 3.178 0.0 . 1040 125 125 PHE C C 172.768 0.0 . 1041 125 125 PHE CA C 54.604 0.0 . 1042 125 125 PHE CB C 41.692 0.0 . 1043 125 125 PHE N N 121.9 0.0 . 1044 126 126 LEU H H 9.932 0.0 . 1045 126 126 LEU CA C 48.875 0.0 . 1046 126 126 LEU N N 125.427 0.0 . 1047 127 127 PRO HA H 5.587 0.0 . 1048 127 127 PRO HB2 H 2.04 0.0 . 1049 127 127 PRO HG2 H 2.386 0.0 . 1050 127 127 PRO C C 174.541 0.0 . 1051 127 127 PRO CA C 58.907 0.0 . 1052 127 127 PRO CB C 28.73 0.0 . 1053 128 128 LEU H H 9.674 0.0 . 1054 128 128 LEU C C 175.96 0.0 . 1055 128 128 LEU CA C 49.523 0.0 . 1056 128 128 LEU N N 129.196 0.0 . 1057 129 129 PRO HA H 4.71 0.0 . 1058 129 129 PRO HB2 H 1.961 0.0 . 1059 129 129 PRO HB3 H 2.355 0.0 . 1060 129 129 PRO HG2 H 2.146 0.0 . 1061 129 129 PRO HD2 H 3.901 0.0 . 1062 129 129 PRO HD3 H 3.654 0.0 . 1063 129 129 PRO C C 174.414 0.0 . 1064 129 129 PRO CA C 60.043 0.0 . 1065 129 129 PRO CB C 29.8 0.0 . 1066 130 130 VAL H H 6.392 0.0 . 1067 130 130 VAL HA H 3.794 0.0 . 1068 130 130 VAL HB H 1.985 0.0 . 1069 130 130 VAL HG1 H 0.832 0.0 . 1070 130 130 VAL HG2 H 0.832 0.0 . 1071 130 130 VAL C C 174.097 0.0 . 1072 130 130 VAL CA C 61.494 0.0 . 1073 130 130 VAL CB C 29.649 0.0 . 1074 130 130 VAL N N 116.125 0.0 . stop_ save_