data_15783 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; acidic fibroblast growth factor solution structure in the FGF-1-C2A binary complex: key component in the fibroblast growthfactor non-classical pathway ; _BMRB_accession_number 15783 _BMRB_flat_file_name bmr15783.str _Entry_type original _Submission_date 2008-05-28 _Accession_date 2008-05-28 _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 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" 598 "13C chemical shifts" 364 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-16 update BMRB 'update entry citation' 2009-10-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15785 C2A stop_ save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19723500 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Anbazhagan Veerappan . . 2 Wang Han-Min . . 3 Lu Ching-Song . . 4 Yu Chin . . stop_ _Journal_abbreviation 'Arch. Biochem. Biophys.' _Journal_name_full 'Archives of biochemistry and biophysics' _Journal_volume 490 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 158 _Page_last 162 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FGF-1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FGF-1 $FGF-1 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_FGF-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FGF-1 _Molecular_mass 15118.163 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 133 _Mol_residue_sequence ; YKKPKLLYCSNGGHFLRILP DGTVDGTRDRSDQHIQLQLS AESVGEVYIKSTETGQYLAM DTDGLLYGSQTPNEECLFLE RLEENHYNTYISKKHAEKNW FVGLKKNGSCKRGPRTHYGQ KAILFLPLPVSSD ; 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 131 SER 132 SER 133 ASP 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 15960 FGF-1 100.00 133 100.00 100.00 1.51e-93 BMRB 16493 aFGF 99.25 132 100.00 100.00 1.38e-92 BMRB 16494 aFGF 99.25 132 100.00 100.00 1.38e-92 BMRB 16502 aFGF 99.25 132 100.00 100.00 1.38e-92 BMRB 17464 FGF 99.25 132 100.00 100.00 1.38e-92 BMRB 17674 FGF1 97.74 130 100.00 100.00 2.90e-91 PDB 1AXM "Heparin-Linked Biologically-Active Dimer Of Fibroblast Growth Factor" 100.00 135 99.25 99.25 2.43e-92 PDB 1DJS "Ligand-binding Portion Of Fibroblast Growth Factor Receptor 2 In Complex With Fgf1" 100.00 135 99.25 99.25 2.43e-92 PDB 1DZC "High Resolution Structure Of Acidic Fibroblast Growth Factor. Mutant Fgf-4-ala-(23-154), 24 Nmr Structures" 96.24 131 100.00 100.00 7.19e-90 PDB 1DZD "High Resolution Structure Of Acidic Fibroblast Growth Factor (27-154), 24 Nmr Structures" 95.49 127 100.00 100.00 7.28e-89 PDB 1E0O "Crystal Structure Of A Ternary Fgf1-Fgfr2-Heparin Complex" 100.00 140 100.00 100.00 4.94e-93 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 1.57e-93 PDB 1HKN "A Complex Between Acidic Fibroblast Growth Factor And 5- Amino-2-Naphthalenesulfonate" 100.00 139 100.00 100.00 4.48e-93 PDB 1JQZ "Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form With Amino Terminal His Tag." 100.00 146 100.00 100.00 7.84e-93 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 99.25 100.00 1.92e-92 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 99.25 100.00 2.69e-92 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 98.50 100.00 6.89e-92 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 97.74 99.25 2.03e-91 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 99.25 99.25 2.28e-92 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 99.25 99.25 8.47e-92 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 99.25 99.25 2.85e-91 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 99.25 99.25 7.68e-92 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 96.99 98.50 2.45e-90 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 99.25 100.00 1.41e-92 PDB 1PZZ "Crystal Structure Of Fgf-1, V51n Mutant" 100.00 146 99.25 99.25 9.98e-92 PDB 1Q03 "Crystal Structure Of Fgf-1, S50gV51G MUTANT" 100.00 146 98.50 98.50 7.20e-91 PDB 1Q04 "Crystal Structure Of Fgf-1, S50e/v51n" 100.00 146 98.50 98.50 4.31e-91 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 7.84e-93 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 1.63e-93 PDB 1RY7 "Crystal Structure Of The 3 Ig Form Of Fgfr3c In Complex With Fgf1" 100.00 155 100.00 100.00 1.63e-93 PDB 1YTO "Crystal Structure Of Gly19 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 145 99.25 99.25 2.58e-90 PDB 1Z2V "Crystal Structure Of Glu60 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 145 99.25 99.25 2.70e-90 PDB 1Z4S "Crystal Structure Of Gly19 And Glu60 Deletion Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 144 98.50 98.50 1.08e-87 PDB 2AFG "2.0 Angstrom X-Ray Structure Of Human Acidic Fibroblast Growth Factor" 100.00 140 100.00 100.00 4.94e-93 PDB 2AQZ "Crystal Structure Of Fgf-1, S17tN18TG19 DELETION MUTANT" 100.00 145 97.74 98.50 5.20e-89 PDB 2AXM "Heparin-Linked Biologically-Active Dimer Of Fibroblast Growth Factor" 100.00 135 100.00 100.00 2.40e-93 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 4.48e-93 PDB 2HW9 "Crystal Structure Of Lys12cysCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.60 Angstrom Resolution" 100.00 146 98.50 98.50 3.11e-90 PDB 2HWA "Crystal Structure Of Lys12thrCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.65 Angstrom Resolution" 100.00 146 98.50 98.50 5.08e-91 PDB 2HWM "Crystal Structure Of Lys12valCYS117VAL MUTANT OF HUMAN Acidic Fibroblast Growth Factor At 1.60 Angstrom Resolution" 100.00 146 98.50 98.50 9.57e-91 PDB 2HZ9 "Crystal Structure Of Lys12valASN95VALCYS117VAL MUTANT OF Human Acidic Fibroblast Growth Factor At 1.70 Angstrom Resolution" 100.00 146 97.74 97.74 1.40e-89 PDB 2J3P "Crystal Structure Of Rat Fgf1 At 1.4 A" 100.00 134 96.99 97.74 9.13e-91 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 1.51e-93 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 1.51e-93 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 1.51e-93 PDB 2KI4 "Fgf1-S100a13 Complex Structure: Key Component In Non-Classic Way Of Fgf1" 100.00 133 100.00 100.00 1.51e-93 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 1.51e-93 PDB 2NTD "Human Fibroblast Growth Factor-1 (140 Amino Acid Form) With Cys117valPRO134CYS MUTATIONS" 100.00 146 98.50 98.50 4.09e-90 PDB 2Q9X "Crystal Structure Of Highly Stable Mutant Q40p/s47i/h93g Of Human Fibroblast Growth Factor-1" 100.00 140 97.74 97.74 1.07e-89 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 2.30e-93 PDB 2UUS "Crystal Structure Of The Rat Fgf1-sucrose Octasulfate (sos) Complex" 98.50 132 96.95 97.71 2.79e-89 PDB 3B9U "Crystal Structure Of L26nD28NH93G MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.74 98.50 1.47e-89 PDB 3BA4 "Crystal Structure Of L26d Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 1.16e-91 PDB 3BA5 "Crystal Structure Of D28a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 6.45e-92 PDB 3BA7 "Crystal Structure Of L26nD28A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 98.50 1.00e-90 PDB 3BAD "Crystal Structure Of D70aH93G MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 98.50 2.91e-90 PDB 3BAG "Crystal Structure Of K112nN114A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 98.50 3.66e-91 PDB 3BAH "Crystal Structure Of K112n Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 3.46e-92 PDB 3BAO "Crystal Structure Of L26n Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 8.85e-92 PDB 3BAQ "Crystal Structure Of L26a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 3.46e-92 PDB 3BAU "Crystal Structure Of K12vL26DD28A MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.74 97.74 1.00e-89 PDB 3BAV "Crystal Structure Of L26aD28N MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 99.25 1.67e-91 PDB 3BB2 "Crystal Structure Of L26dD28N MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 99.25 4.81e-91 PDB 3CQA "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ala And Lys101ala" 100.00 144 98.50 98.50 1.48e-91 PDB 3CRG "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ala, Glu82asn And Lys101ala" 100.00 146 97.74 97.74 1.15e-90 PDB 3CRH "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ser And Lys101ala" 100.00 146 98.50 98.50 2.03e-91 PDB 3CRI "Crystal Structure Of Human Fibroblast Growth Factor-1 With Mutations Glu81ser, Glu82asn And Lys101ala" 100.00 146 97.74 97.74 1.04e-90 PDB 3CU1 "Crystal Structure Of 2:2:2 Fgfr2d2:fgf1:sos Complex" 97.74 131 100.00 100.00 3.38e-91 PDB 3FGM "Crystal Structure Of L44fC83TC117VF132W MUTANT OF HUMAN Acidic Fibroblast Growth Factor" 100.00 146 96.99 97.74 3.12e-89 PDB 3FJ8 "Crystal Structure Of C117i Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 1.09e-91 PDB 3FJ9 "Crystal Structure Of F85w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 100.00 5.78e-92 PDB 3FJA "Crystal Structure Of F132w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 100.00 5.78e-92 PDB 3FJB "Crystal Structure Of V31i Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 100.00 1.28e-92 PDB 3FJC "Crystal Structure Of L44w Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 6.31e-92 PDB 3FJD "Crystal Structure Of L44fF132W MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 98.50 99.25 1.92e-91 PDB 3FJE "Crystal Structure Of C83s Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 8.95e-92 PDB 3FJF "Crystal Structure Of C83t Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 9.35e-92 PDB 3FJH "Crystal Structure Of C83a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 6.45e-92 PDB 3FJI "Crystal Structure Of K12vC83IC117V MUTANT OF HUMAN ACIDIC Fibroblast Growth Factor" 100.00 146 97.74 97.74 1.01e-89 PDB 3FJJ "Crystal Structure Of C83v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 8.47e-92 PDB 3FJK "Crystal Structure Of A66c Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 7.19e-92 PDB 3HAL "Crystal Structure Of Rabbit Acidic Fibroblast Growth Factor" 100.00 146 97.74 98.50 1.67e-90 PDB 3HOM "Crystal Structure Of Oxidized A66c Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 7.19e-92 PDB 3JUT "Acidic Fibroblast Growth Factor (Fgf-1) Complexed With Gentisic Acid" 97.74 130 100.00 100.00 5.11e-91 PDB 3K1X "Acidic Fibroblast Growth Factor (Fgf-1) Complexed With Dobes" 97.74 130 100.00 100.00 5.11e-91 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 1.63e-93 PDB 3OJM "Crystal Structure Of Fgf1 Complexed With The Ectodomain Of Fgfr2b Harboring P253r Apert Mutation" 100.00 155 100.00 100.00 1.63e-93 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 1.79e-93 PDB 3UD7 "Crystal Structure Analysis Of Fgf1-disaccharide(ni21) Complexes" 100.00 141 100.00 100.00 3.48e-93 PDB 3UD8 "Crystal Structure Analysis Of Fgf1-disaccharide(ni22) Complex" 100.00 141 100.00 100.00 3.48e-93 PDB 3UD9 "Crystal Structure Analysis Of Fgf1-disaccharide(ni23) Complex" 100.00 141 100.00 100.00 3.48e-93 PDB 3UDA "Crystal Structure Analysis Of Fgf1-disaccharide(ni24) Complex" 100.00 141 100.00 100.00 3.48e-93 PDB 4J23 "Low Resolution Crystal Structure Of The Fgfr2d2d3/fgf1/sr128545 Complex" 100.00 138 100.00 100.00 2.77e-93 PDB 4Q91 "Crystal Structure Of C16a/k12v/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.99 96.99 1.11e-88 PDB 4Q9G "Crystal Structure Of K12v/c16s/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.99 96.99 1.50e-88 PDB 4Q9P "Crystal Structure Of C16t/k12v/c117v/p134v Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 96.99 96.99 1.47e-88 PDB 4QAL "Crystal Structure Of C117a Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 6.45e-92 PDB 4QBC "Crystal Structure Of C117t Mutant Of Human Acidic Fibroblast Growth Factor In Sodium Formate Buffer" 100.00 146 99.25 99.25 9.35e-92 PDB 4QBV "Crystal Structure Of C117t Mutant Of Human Acidic Fibroblast Growth Factor In Sodium Citrate Buffer" 100.00 146 99.25 99.25 8.47e-92 PDB 4QC4 "Crystal Structure Of C117s Mutant Of Human Acidic Fibroblast Growth Factor" 100.00 146 99.25 99.25 8.95e-92 DBJ BAC29035 "unnamed protein product [Mus musculus]" 100.00 155 96.99 97.74 6.63e-91 DBJ BAF82451 "unnamed protein product [Homo sapiens]" 100.00 154 99.25 99.25 7.72e-91 DBJ BAG35227 "unnamed protein product [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 DBJ BAI46827 "fibroblast growth factor 1 [synthetic construct]" 100.00 155 100.00 100.00 1.63e-93 EMBL CAA32448 "unnamed protein product [Rattus norvegicus]" 100.00 155 96.99 97.74 6.63e-91 EMBL CAA36206 "unnamed protein product [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 EMBL CAA42869 "acidic fibroblast growth factor [Sus scrofa]" 97.74 152 97.69 98.46 5.63e-89 EMBL CAA46661 "acidic fibroblast growth factor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 EMBL CAI29610 "hypothetical protein [Pongo abelii]" 100.00 214 100.00 100.00 1.30e-92 GB AAA37618 "acidic fibroblast growth factor [Mus musculus]" 100.00 155 96.99 97.74 6.63e-91 GB AAA52446 "acidic fibroblast growth factor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 GB AAA52638 "heparin-binding growth factor 1, partial [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 GB AAA79245 "beta-endothelial cell growth factor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 GB AAB29057 "acidic fibroblast growth factor, partial [Homo sapiens]" 99.25 154 100.00 100.00 1.18e-92 PRF 1605206A "acidic fibroblast growth factor" 100.00 156 100.00 100.00 1.26e-93 REF NP_000791 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 REF NP_001127073 "fibroblast growth factor 1 [Pongo abelii]" 100.00 214 100.00 100.00 1.30e-92 REF NP_001138364 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 REF NP_001138406 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 REF NP_001138407 "fibroblast growth factor 1 isoform 1 precursor [Homo sapiens]" 100.00 155 100.00 100.00 1.63e-93 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 1.63e-93 SP P20002 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 97.74 152 97.69 98.46 5.63e-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 97.74 97.74 2.30e-91 SP P61148 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 96.99 97.74 6.63e-91 SP P61149 "RecName: Full=Fibroblast growth factor 1; Short=FGF-1; AltName: Full=Acidic fibroblast growth factor; Short=aFGF; AltName: Full" 100.00 155 96.99 97.74 6.63e-91 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FGF-1 Human 9606 Eukaryota Metazoa Homo spiens 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 $FGF-1 'recombinant technology' . Escherichia coli BL21(DE3) pET20 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details '25mM Phosphate buffer; 90%H20, 10% D20' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FGF-1 1.0 mM 'natural abundance' 'Phosphate buffer' 25 mM . H2O 90 % 'natural abundance' D2O 10 % . 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AV600 _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AV800 _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label $sample 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' 50 . mM pH 6.0 . 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set _Saveframe_category assigned_chemical_shifts _Details 'Derived from the file: /home/krishna/FGF/run30/data/15N/15N.ppm' loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label 3D_15N-separated_NOESY stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FGF-1 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 TYR H H 8.416 0.0 . 2 1 1 TYR N N 120.6 0.0 . 3 1 1 TYR CA C 55.442 0.0 . 4 1 1 TYR C C 174.229 0.0 . 5 1 1 TYR HA H 4.696 0.0 . 6 1 1 TYR HB3 H 3.36 0.0 . 7 1 1 TYR HB2 H 2.927 0.0 . 8 1 1 TYR HD1 H 7.1 0.0 . 9 1 1 TYR HD2 H 7.1 0.0 . 10 1 1 TYR HE1 H 6.89 0.0 . 11 1 1 TYR HE2 H 6.89 0.0 . 12 2 2 LYS H H 7.955 0.0 . 13 2 2 LYS N N 120.0 0.0 . 14 2 2 LYS CA C 51.913 0.0 . 15 2 2 LYS C C 174.3 0.0 . 16 2 2 LYS HA H 4.27 0.0 . 17 2 2 LYS HB2 H 1.89 0.0 . 18 3 3 LYS H H 7.96 0.0 . 19 3 3 LYS N N 119.64 0.0 . 20 3 3 LYS CA C 51.9 0.0 . 21 3 3 LYS HA H 4.6 0.0 . 22 3 3 LYS HB3 H 1.77 0.0 . 23 3 3 LYS HB2 H 1.6 0.0 . 24 4 4 PRO CA C 60.687 0.0 . 25 4 4 PRO C C 172.359 0.0 . 26 4 4 PRO CB C 30.627 0.0 . 27 4 4 PRO HA H 4.716 0.0 . 28 4 4 PRO HB3 H 2.171 0.0 . 29 5 5 LYS H H 9.357 0.0 . 30 5 5 LYS N N 119.1 0.0 . 31 5 5 LYS CA C 51.445 0.0 . 32 5 5 LYS CB C 34.945 0.0 . 33 5 5 LYS C C 171.776 0.0 . 34 5 5 LYS HA H 5.062 0.0 . 35 5 5 LYS HB3 H 1.835 0.0 . 36 5 5 LYS HB2 H 1.507 0.0 . 37 6 6 LEU H H 8.944 0.0 . 38 6 6 LEU N N 117.4 0.0 . 39 6 6 LEU CA C 50.259 0.0 . 40 6 6 LEU CB C 41.472 0.0 . 41 6 6 LEU C C 174.676 0.0 . 42 6 6 LEU HA H 4.984 0.0 . 43 6 6 LEU HB3 H 1.806 0.0 . 44 6 6 LEU HB2 H 1.641 0.0 . 45 6 6 LEU HD1 H 0.769 0.0 . 46 6 6 LEU HD2 H 0.646 0.0 . 47 7 7 LEU H H 10.297 0.0 . 48 7 7 LEU N N 125.0 0.0 . 49 7 7 LEU CA C 53.596 0.0 . 50 7 7 LEU C C 172.29 0.0 . 51 7 7 LEU HA H 5.083 0.0 . 52 7 7 LEU HB3 H 1.65 0.0 . 53 7 7 LEU HB2 H 1.335 0.0 . 54 7 7 LEU HD1 H 0.625 0.0 . 55 7 7 LEU HD2 H 0.528 0.0 . 56 7 7 LEU HG H 1.46 0.0 . 57 8 8 TYR H H 8.483 0.0 . 58 8 8 TYR N N 125.0 0.0 . 59 8 8 TYR CA C 54.761 0.0 . 60 8 8 TYR CB C 37.988 0.0 . 61 8 8 TYR C C 171.27 0.0 . 62 8 8 TYR HA H 4.592 0.0 . 63 8 8 TYR HB3 H 3.405 0.0 . 64 8 8 TYR HB2 H 2.922 0.0 . 65 9 9 CYS H H 9.235 0.0 . 66 9 9 CYS N N 130.104 0.0 . 67 9 9 CYS CA C 55.588 0.0 . 68 9 9 CYS CB C 26.864 0.0 . 69 9 9 CYS C C 172.619 0.0 . 70 9 9 CYS HA H 4.163 0.0 . 71 9 9 CYS HB2 H 2.52 0.0 . 72 9 9 CYS HB3 H 2.581 0.0 . 73 10 10 SER H H 8.173 0.0 . 74 10 10 SER N N 122.6 0.0 . 75 10 10 SER CA C 57.853 0.0 . 76 10 10 SER CB C 61.82 0.0 . 77 10 10 SER C C 172.21 0.0 . 78 10 10 SER HA H 3.92 0.0 . 79 10 10 SER HB2 H 3.9 0.0 . 80 11 11 ASN H H 7.45 0.0 . 81 11 11 ASN N N 119.55 0.0 . 82 11 11 ASN CA C 52.43 0.0 . 83 11 11 ASN HA H 4.36 0.0 . 84 11 11 ASN HB2 H 4.36 0.0 . 85 12 12 GLY C C 171.806 0.0 . 86 12 12 GLY CA C 41.915 0.0 . 87 12 12 GLY HA3 H 3.927 0.0 . 88 12 12 GLY H H 7.096 0.0 . 89 12 12 GLY N N 109.3 0.0 . 90 13 13 GLY H H 7.096 0.0 . 91 13 13 GLY N N 109.3 0.0 . 92 13 13 GLY CA C 44.272 0.0 . 93 13 13 GLY C C 170.445 0.0 . 94 13 13 GLY HA2 H 3.598 0.0 . 95 13 13 GLY HA3 H 3.204 0.0 . 96 14 14 HIS H H 6.302 0.0 . 97 14 14 HIS N N 113.6 0.0 . 98 14 14 HIS CA C 54.319 0.0 . 99 14 14 HIS CB C 31.792 0.0 . 100 14 14 HIS C C 171.281 0.0 . 101 14 14 HIS HA H 4.104 0.0 . 102 14 14 HIS HB3 H 2.651 0.0 . 103 14 14 HIS HB2 H 2.488 0.0 . 104 15 15 PHE H H 9.298 0.0 . 105 15 15 PHE N N 120.7 0.0 . 106 15 15 PHE CA C 54.273 0.0 . 107 15 15 PHE CB C 37.632 0.0 . 108 15 15 PHE C C 173.938 0.0 . 109 15 15 PHE HA H 5.39 0.0 . 110 15 15 PHE HB3 H 3.547 0.0 . 111 15 15 PHE HB2 H 2.936 0.0 . 112 16 16 LEU H H 8.48 0.0 . 113 16 16 LEU N N 124.7 0.0 . 114 16 16 LEU CA C 54.44 0.0 . 115 16 16 LEU C C 171.758 0.0 . 116 16 16 LEU CB C 41.301 0.0 . 117 16 16 LEU HA H 4.394 0.0 . 118 16 16 LEU HB3 H 1.897 0.0 . 119 16 16 LEU HB2 H 1.384 0.0 . 120 17 17 ARG H H 9.339 0.0 . 121 17 17 ARG N N 126.971 0.0 . 122 17 17 ARG CA C 53.301 0.0 . 123 17 17 ARG CB C 32.62 0.0 . 124 17 17 ARG C C 171.302 0.0 . 125 17 17 ARG HA H 4.715 0.0 . 126 17 17 ARG HB3 H 2.587 0.0 . 127 17 17 ARG HB2 H 1.236 0.0 . 128 17 17 ARG HG3 H 1.503 0.0 . 129 17 17 ARG HG2 H 1.23 0.0 . 130 17 17 ARG HD3 H 3.416 0.0 . 131 17 17 ARG HD2 H 3.196 0.0 . 132 18 18 ILE H H 6.989 0.0 . 133 18 18 ILE N N 120.966 0.0 . 134 18 18 ILE CA C 57.903 0.0 . 135 18 18 ILE C C 173.747 0.0 . 136 18 18 ILE HA H 4.563 0.0 . 137 18 18 ILE HB H 1.653 0.0 . 138 18 18 ILE HG2 H 0.641 0.0 . 139 19 19 LEU H H 8.94 0.0 . 140 19 19 LEU N N 128.097 0.0 . 141 19 19 LEU CA C 51.419 0.0 . 142 20 20 PRO CA C 62.71 0.0 . 143 20 20 PRO CB C 29.518 0.0 . 144 20 20 PRO C C 173.966 0.0 . 145 20 20 PRO HA H 4.319 0.0 . 146 20 20 PRO HB3 H 2.343 0.0 . 147 20 20 PRO HB2 H 1.971 0.0 . 148 20 20 PRO HG2 H 1.939 0.0 . 149 20 20 PRO HD2 H 3.673 0.0 . 150 21 21 ASP H H 7.415 0.0 . 151 21 21 ASP N N 114.0 0.0 . 152 21 21 ASP CA C 51.361 0.0 . 153 21 21 ASP CB C 37.419 0.0 . 154 21 21 ASP C C 174.57 0.0 . 155 21 21 ASP HA H 4.513 0.0 . 156 21 21 ASP HB3 H 3.094 0.0 . 157 21 21 ASP HB2 H 2.606 0.0 . 158 22 22 GLY H H 8.404 0.0 . 159 22 22 GLY N N 109.1 0.0 . 160 22 22 GLY CA C 43.166 0.0 . 161 22 22 GLY C C 172.565 0.0 . 162 22 22 GLY HA3 H 4.632 0.0 . 163 22 22 GLY HA2 H 3.838 0.0 . 164 23 23 THR H H 7.894 0.0 . 165 23 23 THR N N 116.8 0.0 . 166 23 23 THR CA C 61.304 0.0 . 167 23 23 THR CB C 67.455 0.0 . 168 23 23 THR C C 170.17 0.0 . 169 23 23 THR HA H 4.489 0.0 . 170 23 23 THR HB H 4.206 0.0 . 171 23 23 THR HG2 H 1.154 0.0 . 172 24 24 VAL H H 7.792 0.0 . 173 24 24 VAL N N 123.1 0.0 . 174 24 24 VAL CA C 58.203 0.0 . 175 24 24 VAL CB C 31.847 0.0 . 176 24 24 VAL C C 171.629 0.0 . 177 24 24 VAL HA H 5.084 0.0 . 178 24 24 VAL HB H 1.601 0.0 . 179 24 24 VAL HG1 H 0.83 0.0 . 180 25 25 ASP H H 8.906 0.0 . 181 25 25 ASP N N 131.2 0.0 . 182 25 25 ASP CA C 50.847 0.0 . 183 25 25 ASP CB C 38.73 0.0 . 184 25 25 ASP C C 170.281 0.0 . 185 25 25 ASP HA H 4.313 0.0 . 186 25 25 ASP HB3 H 3.018 0.0 . 187 25 25 ASP HB2 H 2.734 0.0 . 188 26 26 GLY H H 7.891 0.0 . 189 26 26 GLY N N 102.5 0.0 . 190 26 26 GLY CA C 42.057 0.0 . 191 26 26 GLY C C 169.975 0.0 . 192 26 26 GLY HA3 H 5.529 0.0 . 193 26 26 GLY HA2 H 3.015 0.0 . 194 27 27 THR H H 8.529 0.0 . 195 27 27 THR N N 112.7 0.0 . 196 27 27 THR CA C 56.74 0.0 . 197 27 27 THR CB C 67.326 0.0 . 198 27 27 THR C C 170.554 0.0 . 199 27 27 THR HA H 5.189 0.0 . 200 27 27 THR HB H 3.986 0.0 . 201 27 27 THR HG2 H 1.344 0.0 . 202 28 28 ARG H H 8.993 0.0 . 203 28 28 ARG N N 127.5 0.0 . 204 28 28 ARG CA C 54.938 0.0 . 205 28 28 ARG CB C 37.26 0.0 . 206 28 28 ARG C C 173.45 0.0 . 207 28 28 ARG HA H 4.691 0.0 . 208 28 28 ARG HB3 H 2.078 0.0 . 209 28 28 ARG HB2 H 1.744 0.0 . 210 29 29 ASP H H 8.323 0.0 . 211 29 29 ASP N N 121.0 0.0 . 212 29 29 ASP CA C 50.779 0.0 . 213 29 29 ASP C C 172.275 0.0 . 214 29 29 ASP HA H 4.661 0.0 . 215 29 29 ASP HB3 H 3.222 0.0 . 216 29 29 ASP HB2 H 2.671 0.0 . 217 30 30 ARG H H 8.342 0.0 . 218 30 30 ARG N N 126.1 0.0 . 219 30 30 ARG CA C 54.924 0.0 . 220 30 30 ARG CB C 28.367 0.0 . 221 30 30 ARG C C 173.454 0.0 . 222 30 30 ARG HA H 3.592 0.0 . 223 30 30 ARG HB3 H 1.777 0.0 . 224 30 30 ARG HG2 H 1.446 0.0 . 225 30 30 ARG HD2 H 3.124 0.0 . 226 31 31 SER H H 8.379 0.0 . 227 31 31 SER N N 113.6 0.0 . 228 31 31 SER CA C 55.918 0.0 . 229 31 31 SER CB C 61.807 0.0 . 230 31 31 SER C C 171.758 0.0 . 231 31 31 SER HA H 4.397 0.0 . 232 31 31 SER HB3 H 4.033 0.0 . 233 31 31 SER HB2 H 4.033 0.0 . 234 32 32 ASP H H 7.105 0.0 . 235 32 32 ASP N N 125.0 0.0 . 236 32 32 ASP CA C 53.116 0.0 . 237 32 32 ASP CB C 41.585 0.0 . 238 32 32 ASP C C 174.497 0.0 . 239 32 32 ASP HA H 4.276 0.0 . 240 32 32 ASP HB3 H 2.771 0.0 . 241 32 32 ASP HB2 H 2.707 0.0 . 242 33 33 GLN H H 8.775 0.0 . 243 33 33 GLN N N 124.7 0.0 . 244 33 33 GLN CA C 55.127 0.0 . 245 33 33 GLN CB C 26.601 0.0 . 246 33 33 GLN C C 174.9 0.0 . 247 33 33 GLN HA H 4.061 0.0 . 248 33 33 GLN HB3 H 1.643 0.0 . 249 33 33 GLN HB2 H 1.52 0.0 . 250 33 33 GLN HG2 H 2.098 0.0 . 251 33 33 GLN NE2 N 112.0 0.0 . 252 33 33 GLN HE21 H 7.36 0.0 . 253 33 33 GLN HE22 H 6.66 0.0 . 254 34 34 HIS H H 9.681 0.0 . 255 34 34 HIS N N 116.7 0.0 . 256 34 34 HIS CA C 55.739 0.0 . 257 34 34 HIS CB C 26.065 0.0 . 258 34 34 HIS C C 172.307 0.0 . 259 34 34 HIS HA H 4.885 0.0 . 260 34 34 HIS HB3 H 3.964 0.0 . 261 34 34 HIS HB2 H 3.037 0.0 . 262 35 35 ILE H H 6.711 0.0 . 263 35 35 ILE N N 108.6 0.0 . 264 35 35 ILE CA C 58.395 0.0 . 265 35 35 ILE CB C 35.989 0.0 . 266 35 35 ILE C C 172.249 0.0 . 267 35 35 ILE HA H 5.114 0.0 . 268 35 35 ILE HB H 2.427 0.0 . 269 35 35 ILE HG2 H 0.83 0.0 . 270 35 35 ILE HG12 H 1.113 0.0 . 271 35 35 ILE HD1 H 0.54 0.0 . 272 36 36 GLN H H 7.148 0.0 . 273 36 36 GLN N N 120.018 0.0 . 274 36 36 GLN CA C 55.111 0.0 . 275 36 36 GLN CB C 25.19 0.0 . 276 36 36 GLN C C 172.952 0.0 . 277 36 36 GLN HA H 4.261 0.0 . 278 36 36 GLN HB3 H 2.112 0.0 . 279 36 36 GLN HB2 H 1.877 0.0 . 280 36 36 GLN NE2 N 110.1 0.0 . 281 36 36 GLN HE21 H 7.438 0.0 . 282 36 36 GLN HE22 H 6.63 0.0 . 283 36 36 GLN HG2 H 2.082 0.0 . 284 37 37 LEU H H 9.11 0.0 . 285 37 37 LEU N N 127.6 0.0 . 286 37 37 LEU CA C 51.329 0.0 . 287 37 37 LEU CB C 42.165 0.0 . 288 37 37 LEU C C 172.877 0.0 . 289 37 37 LEU HA H 5.315 0.0 . 290 37 37 LEU HB3 H 1.599 0.0 . 291 37 37 LEU HB2 H 1.047 0.0 . 292 37 37 LEU HD1 H 0.72 0.0 . 293 37 37 LEU HD2 H 0.59 0.0 . 294 38 38 GLN H H 9.556 0.0 . 295 38 38 GLN N N 120.583 0.0 . 296 38 38 GLN CA C 51.81 0.0 . 297 38 38 GLN CB C 29.259 0.0 . 298 38 38 GLN C C 172.676 0.0 . 299 38 38 GLN HA H 4.623 0.0 . 300 38 38 GLN HB3 H 1.874 0.0 . 301 38 38 GLN HB2 H 1.789 0.0 . 302 38 38 GLN HG2 H 2.041 0.0 . 303 39 39 LEU H H 8.926 0.0 . 304 39 39 LEU N N 131.7 0.0 . 305 39 39 LEU CA C 53.062 0.0 . 306 39 39 LEU C C 174.601 0.0 . 307 39 39 LEU HA H 5.506 0.0 . 308 39 39 LEU HB3 H 1.668 0.0 . 309 39 39 LEU HB2 H 1.569 0.0 . 310 39 39 LEU HD1 H 0.892 0.0 . 311 39 39 LEU HD2 H 0.779 0.0 . 312 40 40 SER H H 8.569 0.0 . 313 40 40 SER N N 115.9 0.0 . 314 40 40 SER CA C 54.925 0.0 . 315 40 40 SER CB C 46.694 0.0 . 316 40 40 SER C C 170.046 0.0 . 317 40 40 SER HA H 4.676 0.0 . 318 40 40 SER HB3 H 3.873 0.0 . 319 40 40 SER HB2 H 3.809 0.0 . 320 41 41 ALA H H 8.357 0.0 . 321 41 41 ALA N N 125.9 0.0 . 322 41 41 ALA CA C 49.309 0.0 . 323 41 41 ALA CB C 27.376 0.0 . 324 41 41 ALA C C 175.352 0.0 . 325 41 41 ALA HA H 5.016 0.0 . 326 41 41 ALA HB H 1.34 0.0 . 327 42 42 GLU H H 8.485 0.0 . 328 42 42 GLU N N 125.4 0.0 . 329 42 42 GLU CA C 54.611 0.0 . 330 42 42 GLU CB C 28.181 0.0 . 331 42 42 GLU C C 174.014 0.0 . 332 42 42 GLU HA H 4.444 0.0 . 333 42 42 GLU HB3 H 2.2 0.0 . 334 42 42 GLU HB2 H 1.814 0.0 . 335 42 42 GLU HG3 H 2.324 0.0 . 336 42 42 GLU HG2 H 2.2 0.0 . 337 43 43 SER H H 8.02 0.0 . 338 43 43 SER N N 113.9 0.0 . 339 43 43 SER CA C 55.014 0.0 . 340 43 43 SER CB C 61.687 0.0 . 341 43 43 SER C C 171.119 0.0 . 342 43 43 SER HA H 4.516 0.0 . 343 43 43 SER HB3 H 3.814 0.0 . 344 43 43 SER HB2 H 3.722 0.0 . 345 44 44 VAL H H 8.113 0.0 . 346 44 44 VAL N N 121.1 0.0 . 347 44 44 VAL CA C 62.838 0.0 . 348 44 44 VAL CB C 28.991 0.0 . 349 44 44 VAL C C 175.533 0.0 . 350 44 44 VAL HA H 3.868 0.0 . 351 44 44 VAL HB H 2.057 0.0 . 352 44 44 VAL HG1 H 1.154 0.0 . 353 44 44 VAL HG2 H 1.082 0.0 . 354 45 45 GLY H H 8.807 0.0 . 355 45 45 GLY N N 115.545 0.0 . 356 45 45 GLY CA C 43.553 0.0 . 357 45 45 GLY C C 170.948 0.0 . 358 45 45 GLY HA3 H 4.296 0.0 . 359 45 45 GLY HA2 H 3.995 0.0 . 360 46 46 GLU H H 7.985 0.0 . 361 46 46 GLU N N 121.2 0.0 . 362 46 46 GLU CA C 52.751 0.0 . 363 46 46 GLU CB C 29.432 0.0 . 364 46 46 GLU C C 173.583 0.0 . 365 46 46 GLU HA H 5.442 0.0 . 366 46 46 GLU HB3 H 1.842 0.0 . 367 46 46 GLU HB2 H 1.82 0.0 . 368 46 46 GLU HG3 H 2.149 0.0 . 369 46 46 GLU HG2 H 2.087 0.0 . 370 47 47 VAL H H 9.56 0.0 . 371 47 47 VAL N N 116.4 0.0 . 372 47 47 VAL CA C 56.846 0.0 . 373 47 47 VAL CB C 33.714 0.0 . 374 47 47 VAL C C 172.96 0.0 . 375 47 47 VAL HA H 5.505 0.0 . 376 47 47 VAL HB H 2.296 0.0 . 377 47 47 VAL HG1 H 0.979 0.0 . 378 47 47 VAL HG2 H 0.871 0.0 . 379 48 48 TYR H H 8.415 0.0 . 380 48 48 TYR N N 117.4 0.0 . 381 48 48 TYR CA C 54.331 0.0 . 382 48 48 TYR CB C 39.296 0.0 . 383 48 48 TYR C C 173.423 0.0 . 384 48 48 TYR HA H 5.29 0.0 . 385 48 48 TYR HB3 H 3.286 0.0 . 386 48 48 TYR HB2 H 3.035 0.0 . 387 49 49 ILE H H 10.532 0.0 . 388 49 49 ILE N N 123.1 0.0 . 389 49 49 ILE CA C 59.573 0.0 . 390 49 49 ILE CB C 40.504 0.0 . 391 49 49 ILE C C 170.853 0.0 . 392 49 49 ILE HA H 4.341 0.0 . 393 49 49 ILE HB H 1.65 0.0 . 394 49 49 ILE HG13 H 1.231 0.0 . 395 49 49 ILE HG12 H 0.487 0.0 . 396 49 49 ILE HD1 H -0.17 0.0 . 397 50 50 LYS H H 8.511 0.0 . 398 50 50 LYS N N 125.8 0.0 . 399 50 50 LYS CA C 51.179 0.0 . 400 50 50 LYS CB C 34.816 0.0 . 401 50 50 LYS C C 173.759 0.0 . 402 50 50 LYS HA H 4.991 0.0 . 403 50 50 LYS HB3 H 1.303 0.0 . 404 50 50 LYS HB2 H 1.113 0.0 . 405 50 50 LYS HG3 H 0.861 0.0 . 406 50 50 LYS HG2 H 0.399 0.0 . 407 50 50 LYS HD2 H 1.302 0.0 . 408 50 50 LYS HE3 H 2.6 0.0 . 409 50 50 LYS HE2 H 2.5 0.0 . 410 51 51 SER H H 8.92 0.0 . 411 51 51 SER N N 117.579 0.0 . 412 51 51 SER CA C 55.043 0.0 . 413 51 51 SER CB C 61.065 0.0 . 414 51 51 SER C C 175.084 0.0 . 415 51 51 SER HA H 4.666 0.0 . 416 51 51 SER HB3 H 3.883 0.0 . 417 51 51 SER HB2 H 3.883 0.0 . 418 52 52 THR H H 8.342 0.0 . 419 52 52 THR N N 123.2 0.0 . 420 52 52 THR CA C 62.792 0.0 . 421 52 52 THR CB C 65.611 0.0 . 422 52 52 THR C C 173.566 0.0 . 423 52 52 THR HA H 3.996 0.0 . 424 52 52 THR HB H 4.193 0.0 . 425 52 52 THR HG2 H 1.446 0.0 . 426 53 53 GLU H H 8.312 0.0 . 427 53 53 GLU N N 122.0 0.0 . 428 53 53 GLU CA C 55.889 0.0 . 429 53 53 GLU CB C 28.359 0.0 . 430 53 53 GLU C C 175.327 0.0 . 431 53 53 GLU HA H 4.311 0.0 . 432 53 53 GLU HB3 H 2.207 0.0 . 433 53 53 GLU HB2 H 1.912 0.0 . 434 54 54 THR H H 7.724 0.0 . 435 54 54 THR N N 103.1 0.0 . 436 54 54 THR CA C 58.555 0.0 . 437 54 54 THR CB C 69.03 0.0 . 438 54 54 THR C C 173.942 0.0 . 439 54 54 THR HA H 4.681 0.0 . 440 54 54 THR HB H 4.528 0.0 . 441 54 54 THR HG2 H 1.184 0.0 . 442 55 55 GLY H H 7.643 0.0 . 443 55 55 GLY N N 110.7 0.0 . 444 55 55 GLY CA C 43.594 0.0 . 445 55 55 GLY HA3 H 4.15 0.0 . 446 55 55 GLY HA2 H 3.591 0.0 . 447 55 55 GLY C C 170.694 0.0 . 448 56 56 GLN H H 7.211 0.0 . 449 56 56 GLN N N 115.7 0.0 . 450 56 56 GLN CA C 53.898 0.0 . 451 56 56 GLN CB C 30.456 0.0 . 452 56 56 GLN C C 172.141 0.0 . 453 56 56 GLN HA H 4.311 0.0 . 454 56 56 GLN HB2 H 1.591 0.0 . 455 56 56 GLN HB3 H 1.591 0.0 . 456 56 56 GLN NE2 N 106.6 0.0 . 457 56 56 GLN HE21 H 7.02 0.0 . 458 56 56 GLN HE22 H 6.38 0.0 . 459 57 57 TYR H H 9.254 0.0 . 460 57 57 TYR N N 119.4 0.0 . 461 57 57 TYR CA C 53.356 0.0 . 462 57 57 TYR CB C 40.466 0.0 . 463 57 57 TYR C C 173.32 0.0 . 464 57 57 TYR HA H 4.128 0.0 . 465 57 57 TYR HB3 H 3.161 0.0 . 466 57 57 TYR HB2 H 2.811 0.0 . 467 58 58 LEU H H 9.126 0.0 . 468 58 58 LEU N N 123.6 0.0 . 469 58 58 LEU CA C 53.256 0.0 . 470 58 58 LEU CB C 40.466 0.0 . 471 58 58 LEU C C 172.32 0.0 . 472 58 58 LEU HA H 4.128 0.0 . 473 58 58 LEU HB3 H 1.939 0.0 . 474 58 58 LEU HB2 H 1.037 0.0 . 475 58 58 LEU HD1 H 0.435 0.0 . 476 58 58 LEU HG H 1.733 0.0 . 477 59 59 ALA H H 8.656 0.0 . 478 59 59 ALA N N 126.947 0.0 . 479 59 59 ALA CA C 48.45 0.0 . 480 59 59 ALA CB C 21.261 0.0 . 481 59 59 ALA C C 172.722 0.0 . 482 59 59 ALA HA H 5.124 0.0 . 483 59 59 ALA HB H 0.611 0.0 . 484 60 60 MET H H 7.521 0.0 . 485 60 60 MET N N 116.602 0.0 . 486 60 60 MET CA C 52.251 0.0 . 487 60 60 MET CB C 35.046 0.0 . 488 60 60 MET C C 173.753 0.0 . 489 60 60 MET HA H 5.527 0.0 . 490 60 60 MET HB3 H 2.385 0.0 . 491 60 60 MET HB2 H 2.192 0.0 . 492 60 60 MET HG3 H 2.785 0.0 . 493 60 60 MET HG2 H 2.2 0.0 . 494 61 61 ASP H H 9.159 0.0 . 495 61 61 ASP N N 128.445 0.0 . 496 61 61 ASP CA C 51.48 0.0 . 497 61 61 ASP CB C 39.346 0.0 . 498 61 61 ASP C C 175.8 0.0 . 499 61 61 ASP HA H 5.046 0.0 . 500 61 61 ASP HB3 H 3.586 0.0 . 501 61 61 ASP HB2 H 2.87 0.0 . 502 62 62 THR H H 7.972 0.0 . 503 62 62 THR N N 107.806 0.0 . 504 62 62 THR CA C 62.626 0.0 . 505 62 62 THR CB C 66.955 0.0 . 506 62 62 THR C C 172.355 0.0 . 507 62 62 THR HA H 4.134 0.0 . 508 62 62 THR HB H 4.503 0.0 . 509 62 62 THR HG2 H 1.662 0.0 . 510 63 63 ASP H H 8.333 0.0 . 511 63 63 ASP N N 119.831 0.0 . 512 63 63 ASP CA C 51.865 0.0 . 513 63 63 ASP CB C 39.182 0.0 . 514 63 63 ASP C C 174.438 0.0 . 515 63 63 ASP HA H 4.964 0.0 . 516 63 63 ASP HB3 H 2.749 0.0 . 517 63 63 ASP HB2 H 2.769 0.0 . 518 64 64 GLY H H 8.264 0.0 . 519 64 64 GLY N N 109.142 0.0 . 520 64 64 GLY CA C 42.923 0.0 . 521 64 64 GLY C C 171.248 0.0 . 522 64 64 GLY HA3 H 3.652 0.0 . 523 64 64 GLY HA2 H 3.397 0.0 . 524 65 65 LEU H H 8.636 0.0 . 525 65 65 LEU N N 123.137 0.0 . 526 65 65 LEU CA C 52.224 0.0 . 527 65 65 LEU CB C 40.557 0.0 . 528 65 65 LEU C C 174.507 0.0 . 529 65 65 LEU HA H 4.529 0.0 . 530 65 65 LEU HB3 H 2.054 0.0 . 531 65 65 LEU HB2 H 1.567 0.0 . 532 65 65 LEU HD1 H 1.143 0.0 . 533 65 65 LEU HD2 H 0.995 0.0 . 534 65 65 LEU HG H 2.447 0.0 . 535 66 66 LEU H H 7.431 0.0 . 536 66 66 LEU N N 124.493 0.0 . 537 66 66 LEU CA C 51.635 0.0 . 538 66 66 LEU CB C 40.474 0.0 . 539 66 66 LEU C C 174.07 0.0 . 540 66 66 LEU HA H 5.714 0.0 . 541 66 66 LEU HB3 H 1.139 0.0 . 542 66 66 LEU HB2 H 1.434 0.0 . 543 66 66 LEU HD1 H 1.42 0.0 . 544 66 66 LEU HD2 H 1.02 0.0 . 545 66 66 LEU HG H 2.164 0.0 . 546 67 67 TYR H H 9.237 0.0 . 547 67 67 TYR N N 120.36 0.0 . 548 67 67 TYR CA C 54.076 0.0 . 549 67 67 TYR CB C 38.903 0.0 . 550 67 67 TYR C C 169.64 0.0 . 551 67 67 TYR HA H 5.023 0.0 . 552 67 67 TYR HB2 H 3.111 0.0 . 553 68 68 GLY H H 8.928 0.0 . 554 68 68 GLY N N 105.646 0.0 . 555 68 68 GLY CA C 41.569 0.0 . 556 68 68 GLY C C 170.551 0.0 . 557 68 68 GLY HA2 H 4.676 0.0 . 558 69 69 SER H H 9.608 0.0 . 559 69 69 SER N N 120.1 0.0 . 560 69 69 SER CA C 53.737 0.0 . 561 69 69 SER CB C 63.042 0.0 . 562 69 69 SER C C 174.219 0.0 . 563 69 69 SER HA H 4.966 0.0 . 564 69 69 SER HB3 H 3.915 0.0 . 565 69 69 SER HB2 H 3.552 0.0 . 566 70 70 GLN H H 9.343 0.0 . 567 70 70 GLN N N 127.339 0.0 . 568 70 70 GLN CA C 56.139 0.0 . 569 70 70 GLN CB C 27.092 0.0 . 570 70 70 GLN C C 173.241 0.0 . 571 70 70 GLN HA H 4.286 0.0 . 572 70 70 GLN HB3 H 2.331 0.0 . 573 70 70 GLN HB2 H 2.216 0.0 . 574 70 70 GLN NE2 N 112.2 0.0 . 575 70 70 GLN HE21 H 7.36 0.0 . 576 70 70 GLN HE22 H 6.86 0.0 . 577 70 70 GLN HG3 H 2.667 0.0 . 578 70 70 GLN HG2 H 2.539 0.0 . 579 71 71 THR H H 7.532 0.0 . 580 71 71 THR N N 108.1 0.0 . 581 71 71 THR CA C 55.203 0.0 . 582 71 71 THR HA H 4.78 0.0 . 583 71 71 THR HB H 4.15 0.0 . 584 72 72 PRO CA C 60.05 0.0 . 585 72 72 PRO CB C 26.678 0.0 . 586 72 72 PRO C C 172.92 0.0 . 587 72 72 PRO HA H 4.173 0.0 . 588 72 72 PRO HB3 H 1.31 0.0 . 589 72 72 PRO HB2 H 0.325 0.0 . 590 73 73 ASN H H 7.321 0.0 . 591 73 73 ASN N N 119.2 0.0 . 592 73 73 ASN CA C 49.994 0.0 . 593 74 74 GLU H H 9.03 0.0 . 594 74 74 GLU CA C 57.131 0.0 . 595 74 74 GLU CB C 27.005 0.0 . 596 74 74 GLU C C 176.352 0.0 . 597 74 74 GLU HA H 4.13 0.0 . 598 74 74 GLU HB3 H 2.117 0.0 . 599 74 74 GLU HB2 H 2.12 0.0 . 600 74 74 GLU HG2 H 2.529 0.0 . 601 74 74 GLU HG3 H 2.529 0.0 . 602 75 75 GLU H H 8.574 0.0 . 603 75 75 GLU N N 119.2 0.0 . 604 75 75 GLU CA C 56.343 0.0 . 605 75 75 GLU CB C 26.028 0.0 . 606 75 75 GLU C C 173.866 0.0 . 607 75 75 GLU HA H 4.206 0.0 . 608 75 75 GLU HB3 H 2.631 0.0 . 609 75 75 GLU HB2 H 2.468 0.0 . 610 75 75 GLU HG3 H 2.621 0.0 . 611 75 75 GLU HG2 H 2.434 0.0 . 612 76 76 CYS H H 7.727 0.0 . 613 76 76 CYS N N 113.8 0.0 . 614 76 76 CYS CA C 55.635 0.0 . 615 76 76 CYS CB C 26.036 0.0 . 616 76 76 CYS C C 170.849 0.0 . 617 76 76 CYS HA H 5.426 0.0 . 618 76 76 CYS HB3 H 3.71 0.0 . 619 76 76 CYS HB2 H 3.315 0.0 . 620 77 77 LEU H H 6.241 0.0 . 621 77 77 LEU N N 118.069 0.0 . 622 77 77 LEU CA C 51.793 0.0 . 623 77 77 LEU CB C 42.123 0.0 . 624 77 77 LEU C C 173.882 0.0 . 625 77 77 LEU HA H 4.555 0.0 . 626 77 77 LEU HB3 H 1.423 0.0 . 627 77 77 LEU HB2 H 1.163 0.0 . 628 77 77 LEU HD1 H 0.65 0.0 . 629 77 77 LEU HD2 H 0.38 0.0 . 630 77 77 LEU HG H 1.27 0.0 . 631 78 78 PHE H H 9.067 0.0 . 632 78 78 PHE N N 122.377 0.0 . 633 78 78 PHE CA C 54.917 0.0 . 634 78 78 PHE CB C 40.597 0.0 . 635 78 78 PHE C C 171.853 0.0 . 636 78 78 PHE HA H 5.169 0.0 . 637 78 78 PHE HB3 H 2.936 0.0 . 638 78 78 PHE HB2 H 2.804 0.0 . 639 79 79 LEU H H 9.958 0.0 . 640 79 79 LEU N N 122.126 0.0 . 641 79 79 LEU CA C 51.232 0.0 . 642 79 79 LEU CB C 38.511 0.0 . 643 79 79 LEU C C 173.055 0.0 . 644 79 79 LEU HA H 4.686 0.0 . 645 79 79 LEU HB2 H 1.9 0.0 . 646 79 79 LEU HD1 H 0.935 0.0 . 647 79 79 LEU HG H 1.573 0.0 . 648 80 80 GLU H H 8.347 0.0 . 649 80 80 GLU N N 126.3 0.0 . 650 80 80 GLU CA C 52.558 0.0 . 651 80 80 GLU CB C 30.892 0.0 . 652 80 80 GLU C C 173.355 0.0 . 653 80 80 GLU HA H 4.832 0.0 . 654 80 80 GLU HB3 H 2.079 0.0 . 655 80 80 GLU HB2 H 1.926 0.0 . 656 81 81 ARG H H 8.84 0.0 . 657 81 81 ARG N N 129.522 0.0 . 658 81 81 ARG CA C 52.288 0.0 . 659 81 81 ARG CB C 38.588 0.0 . 660 81 81 ARG C C 172.258 0.0 . 661 81 81 ARG HA H 4.659 0.0 . 662 81 81 ARG HB3 H 1.84 0.0 . 663 81 81 ARG HB2 H 1.83 0.0 . 664 81 81 ARG HG3 H 1.567 0.0 . 665 81 81 ARG HG2 H 1.482 0.0 . 666 81 81 ARG HD2 H 3.19 0.0 . 667 82 82 LEU H H 8.347 0.0 . 668 82 82 LEU N N 125.7 0.0 . 669 82 82 LEU CA C 52.631 0.0 . 670 82 82 LEU CB C 40.304 0.0 . 671 82 82 LEU C C 174.567 0.0 . 672 82 82 LEU HA H 4.875 0.0 . 673 82 82 LEU HB3 H 1.746 0.0 . 674 82 82 LEU HB2 H 1.505 0.0 . 675 82 82 LEU HD1 H 0.848 0.0 . 676 82 82 LEU HG H 1.706 0.0 . 677 83 83 GLU H H 9.064 0.0 . 678 83 83 GLU N N 125.6 0.0 . 679 83 83 GLU CA C 51.723 0.0 . 680 83 83 GLU CB C 43.703 0.0 . 681 83 83 GLU C C 174.885 0.0 . 682 83 83 GLU HA H 4.974 0.0 . 683 83 83 GLU HG2 H 2.208 0.0 . 684 83 83 GLU HG3 H 2.208 0.0 . 685 84 84 GLU H H 8.806 0.0 . 686 84 84 GLU N N 120.3 0.0 . 687 84 84 GLU CA C 55.553 0.0 . 688 84 84 GLU CB C 27.117 0.0 . 689 84 84 GLU C C 174.261 0.0 . 690 84 84 GLU HA H 4.112 0.0 . 691 84 84 GLU HB2 H 2.165 0.0 . 692 84 84 GLU HG3 H 2.355 0.0 . 693 84 84 GLU HG2 H 2.355 0.0 . 694 85 85 ASN H H 8.429 0.0 . 695 85 85 ASN N N 114.8 0.0 . 696 85 85 ASN CA C 51.788 0.0 . 697 85 85 ASN CB C 35.301 0.0 . 698 85 85 ASN C C 172.203 0.0 . 699 85 85 ASN HA H 4.343 0.0 . 700 85 85 ASN HB3 H 3.092 0.0 . 701 85 85 ASN HB2 H 2.998 0.0 . 702 86 86 HIS H H 8.081 0.0 . 703 86 86 HIS N N 108.737 0.0 . 704 86 86 HIS CA C 55.255 0.0 . 705 86 86 HIS CB C 24.858 0.0 . 706 86 86 HIS C C 171.039 0.0 . 707 86 86 HIS HA H 4.26 0.0 . 708 86 86 HIS HB3 H 3.442 0.0 . 709 86 86 HIS HB2 H 3.284 0.0 . 710 87 87 TYR H H 7.592 0.0 . 711 87 87 TYR N N 117.738 0.0 . 712 87 87 TYR CA C 56.163 0.0 . 713 87 87 TYR CB C 38.643 0.0 . 714 87 87 TYR C C 171.983 0.0 . 715 87 87 TYR HA H 4.836 0.0 . 716 87 87 TYR HB2 H 2.959 0.0 . 717 88 88 ASN H H 9.84 0.0 . 718 88 88 ASN N N 118.891 0.0 . 719 88 88 ASN CA C 50.063 0.0 . 720 88 88 ASN CB C 40.242 0.0 . 721 88 88 ASN C C 172.471 0.0 . 722 88 88 ASN HA H 5.837 0.0 . 723 88 88 ASN HB3 H 2.658 0.0 . 724 88 88 ASN HB2 H 2.486 0.0 . 725 88 88 ASN ND2 N 106.93 0.0 . 726 88 88 ASN HD21 H 6.72 0.0 . 727 88 88 ASN HD22 H 6.5 0.0 . 728 89 89 THR H H 8.38 0.0 . 729 89 89 THR N N 108.521 0.0 . 730 89 89 THR CA C 57.357 0.0 . 731 89 89 THR CB C 70.868 0.0 . 732 89 89 THR C C 170.548 0.0 . 733 89 89 THR HA H 5.127 0.0 . 734 89 89 THR HB H 4.58 0.0 . 735 89 89 THR HG2 H 1.319 0.0 . 736 90 90 TYR H H 10.247 0.0 . 737 90 90 TYR N N 119.0 0.0 . 738 90 90 TYR CA C 55.106 0.0 . 739 90 90 TYR CB C 39.047 0.0 . 740 90 90 TYR C C 172.442 0.0 . 741 90 90 TYR HA H 5.472 0.0 . 742 90 90 TYR HB2 H 2.471 0.0 . 743 91 91 ILE H H 8.781 0.0 . 744 91 91 ILE N N 122.546 0.0 . 745 91 91 ILE CA C 56.346 0.0 . 746 91 91 ILE CB C 36.627 0.0 . 747 91 91 ILE C C 172.924 0.0 . 748 91 91 ILE HA H 4.673 0.0 . 749 91 91 ILE HG13 H 1.288 0.0 . 750 91 91 ILE HG12 H 0.036 0.0 . 751 91 91 ILE HG2 H 0.631 0.0 . 752 91 91 ILE HD1 H 0.562 0.0 . 753 92 92 SER H H 8.191 0.0 . 754 92 92 SER N N 120.2 0.0 . 755 92 92 SER CA C 55.781 0.0 . 756 92 92 SER CB C 62.382 0.0 . 757 92 92 SER C C 172.863 0.0 . 758 92 92 SER HA H 4.016 0.0 . 759 92 92 SER HB2 H 3.816 0.0 . 760 93 93 LYS H H 7.993 0.0 . 761 93 93 LYS N N 130.618 0.0 . 762 93 93 LYS CA C 57.942 0.0 . 763 93 93 LYS CB C 30.889 0.0 . 764 93 93 LYS C C 176.938 0.0 . 765 93 93 LYS HA H 3.779 0.0 . 766 93 93 LYS HB3 H 1.766 0.0 . 767 93 93 LYS HB2 H 1.19 0.0 . 768 93 93 LYS HG2 H 1.203 0.0 . 769 93 93 LYS HE3 H 2.912 0.0 . 770 93 93 LYS HE2 H 2.657 0.0 . 771 94 94 LYS H H 8.616 0.0 . 772 94 94 LYS N N 120.044 0.0 . 773 94 94 LYS CA C 55.868 0.0 . 774 94 94 LYS CB C 30.329 0.0 . 775 94 94 LYS C C 174.491 0.0 . 776 94 94 LYS HA H 3.851 0.0 . 777 94 94 LYS HB3 H 1.475 0.0 . 778 94 94 LYS HB2 H 1.342 0.0 . 779 94 94 LYS HG3 H 0.948 0.0 . 780 94 94 LYS HG2 H 0.593 0.0 . 781 94 94 LYS HD2 H 1.435 0.0 . 782 94 94 LYS HE2 H 2.919 0.0 . 783 95 95 HIS H H 7.249 0.0 . 784 95 95 HIS N N 114.486 0.0 . 785 95 95 HIS CA C 51.18 0.0 . 786 95 95 HIS CB C 26.844 0.0 . 787 95 95 HIS C C 173.734 0.0 . 788 95 95 HIS HA H 4.604 0.0 . 789 95 95 HIS HB3 H 2.524 0.0 . 790 95 95 HIS HB2 H 2.47 0.0 . 791 96 96 ALA H H 7.104 0.0 . 792 96 96 ALA N N 125.204 0.0 . 793 96 96 ALA CA C 53.758 0.0 . 794 96 96 ALA CB C 16.578 0.0 . 795 96 96 ALA C C 178.508 0.0 . 796 96 96 ALA HA H 4.131 0.0 . 797 96 96 ALA HB H 2.116 0.0 . 798 97 97 GLU H H 8.857 0.0 . 799 97 97 GLU N N 118.007 0.0 . 800 97 97 GLU CA C 56.153 0.0 . 801 97 97 GLU CB C 26.241 0.0 . 802 97 97 GLU C C 174.813 0.0 . 803 97 97 GLU HA H 4.063 0.0 . 804 97 97 GLU HB2 H 1.965 0.0 . 805 97 97 GLU HG3 H 2.278 0.0 . 806 97 97 GLU HG2 H 2.154 0.0 . 807 98 98 LYS H H 7.116 0.0 . 808 98 98 LYS N N 116.241 0.0 . 809 98 98 LYS CA C 52.852 0.0 . 810 98 98 LYS CB C 29.959 0.0 . 811 98 98 LYS C C 173.361 0.0 . 812 98 98 LYS HA H 4.28 0.0 . 813 98 98 LYS HB3 H 1.735 0.0 . 814 98 98 LYS HB2 H 0.756 0.0 . 815 98 98 LYS HG2 H 0.431 0.0 . 816 98 98 LYS HD2 H 1.459 0.0 . 817 98 98 LYS HE2 H 2.278 0.0 . 818 99 99 ASN H H 7.842 0.0 . 819 99 99 ASN N N 113.0 0.0 . 820 99 99 ASN CA C 52.24 0.0 . 821 99 99 ASN CB C 35.289 0.0 . 822 99 99 ASN C C 170.506 0.0 . 823 99 99 ASN HA H 3.772 0.0 . 824 99 99 ASN HB3 H 2.973 0.0 . 825 99 99 ASN HB2 H 2.816 0.0 . 826 99 99 ASN ND2 N 112.85 0.0 . 827 99 99 ASN HD21 H 7.4 0.0 . 828 99 99 ASN HD22 H 6.47 0.0 . 829 100 100 TRP H H 6.369 0.0 . 830 100 100 TRP N N 116.0 0.0 . 831 100 100 TRP CA C 53.179 0.0 . 832 100 100 TRP CB C 28.228 0.0 . 833 100 100 TRP C C 171.701 0.0 . 834 100 100 TRP HA H 4.816 0.0 . 835 100 100 TRP HB3 H 3.141 0.0 . 836 100 100 TRP HB2 H 2.92 0.0 . 837 101 101 PHE H H 8.026 0.0 . 838 101 101 PHE N N 124.185 0.0 . 839 101 101 PHE CA C 55.472 0.0 . 840 101 101 PHE CB C 39.22 0.0 . 841 101 101 PHE C C 175.044 0.0 . 842 101 101 PHE HA H 5.373 0.0 . 843 101 101 PHE HB3 H 3.456 0.0 . 844 101 101 PHE HB2 H 2.722 0.0 . 845 102 102 VAL H H 8.499 0.0 . 846 102 102 VAL N N 120.282 0.0 . 847 102 102 VAL CA C 60.975 0.0 . 848 102 102 VAL CB C 30.243 0.0 . 849 102 102 VAL C C 174.22 0.0 . 850 102 102 VAL HA H 3.939 0.0 . 851 102 102 VAL HB H 2.027 0.0 . 852 102 102 VAL HG1 H 0.508 0.0 . 853 103 103 GLY H H 8.996 0.0 . 854 103 103 GLY N N 114.668 0.0 . 855 103 103 GLY CA C 43.802 0.0 . 856 103 103 GLY C C 169.388 0.0 . 857 103 103 GLY HA2 H 5.275 0.0 . 858 103 103 GLY HA3 H 3.18 0.0 . 859 104 104 LEU H H 8.118 0.0 . 860 104 104 LEU N N 119.1 0.0 . 861 104 104 LEU CA C 51.207 0.0 . 862 104 104 LEU CB C 43.579 0.0 . 863 104 104 LEU C C 174.252 0.0 . 864 104 104 LEU HA H 4.959 0.0 . 865 104 104 LEU HB2 H 2.229 0.0 . 866 104 104 LEU HD1 H 0.747 0.0 . 867 104 104 LEU HD2 H 0.631 0.0 . 868 104 104 LEU HG H 1.629 0.0 . 869 105 105 LYS H H 8.847 0.0 . 870 105 105 LYS N N 118.9 0.0 . 871 105 105 LYS CA C 54.035 0.0 . 872 105 105 LYS C C 176.404 0.0 . 873 105 105 LYS HA H 4.215 0.0 . 874 105 105 LYS HB3 H 2.121 0.0 . 875 105 105 LYS HB2 H 1.781 0.0 . 876 105 105 LYS HD3 H 1.737 0.0 . 877 105 105 LYS HD2 H 1.59 0.0 . 878 105 105 LYS HE2 H 3.128 0.0 . 879 106 106 LYS H H 8.98 0.0 . 880 106 106 LYS N N 122.172 0.0 . 881 106 106 LYS CA C 57.672 0.0 . 882 106 106 LYS CB C 29.78 0.0 . 883 106 106 LYS C C 174.499 0.0 . 884 106 106 LYS HA H 3.624 0.0 . 885 106 106 LYS HB3 H 1.761 0.0 . 886 106 106 LYS HB2 H 1.475 0.0 . 887 106 106 LYS HG2 H 1.536 0.0 . 888 106 106 LYS HE2 H 3.082 0.0 . 889 107 107 ASN H H 7.352 0.0 . 890 107 107 ASN N N 112.743 0.0 . 891 107 107 ASN CA C 49.523 0.0 . 892 107 107 ASN CB C 35.121 0.0 . 893 107 107 ASN C C 174.511 0.0 . 894 107 107 ASN HA H 4.678 0.0 . 895 107 107 ASN HB3 H 3.318 0.0 . 896 107 107 ASN HB2 H 2.762 0.0 . 897 108 108 GLY H H 7.656 0.0 . 898 108 108 GLY N N 109.9 0.0 . 899 108 108 GLY CA C 42.207 0.0 . 900 108 108 GLY C C 169.305 0.0 . 901 108 108 GLY HA3 H 3.358 0.0 . 902 108 108 GLY HA2 H 2.111 0.0 . 903 109 109 SER H H 7.28 0.0 . 904 109 109 SER N N 112.357 0.0 . 905 109 109 SER CA C 55.139 0.0 . 906 109 109 SER CB C 62.749 0.0 . 907 109 109 SER C C 171.244 0.0 . 908 109 109 SER HA H 4.755 0.0 . 909 109 109 SER HB2 H 3.913 0.0 . 910 109 109 SER HB3 H 3.913 0.0 . 911 110 110 CYS H H 9.07 0.0 . 912 110 110 CYS N N 119.883 0.0 . 913 110 110 CYS CA C 57.858 0.0 . 914 110 110 CYS CB C 37.322 0.0 . 915 110 110 CYS C C 172.131 0.0 . 916 110 110 CYS HA H 4.296 0.0 . 917 110 110 CYS HB3 H 3.217 0.0 . 918 110 110 CYS HB2 H 3.143 0.0 . 919 111 111 LYS H H 8.095 0.0 . 920 111 111 LYS N N 128.642 0.0 . 921 111 111 LYS CA C 52.117 0.0 . 922 111 111 LYS CB C 30.98 0.0 . 923 111 111 LYS C C 172.265 0.0 . 924 111 111 LYS HA H 4.38 0.0 . 925 111 111 LYS HB2 H 1.458 0.0 . 926 111 111 LYS HB3 H 1.458 0.0 . 927 111 111 LYS HD2 H 1.25 0.0 . 928 111 111 LYS HG2 H 1.134 0.0 . 929 112 112 ARG H H 8.566 0.0 . 930 112 112 ARG N N 124.7 0.0 . 931 112 112 ARG CA C 54.295 0.0 . 932 112 112 ARG CB C 28.927 0.0 . 933 112 112 ARG C C 175.24 0.0 . 934 112 112 ARG HA H 4.252 0.0 . 935 112 112 ARG HB3 H 1.554 0.0 . 936 112 112 ARG HB2 H 1.554 0.0 . 937 112 112 ARG HD2 H 3.143 0.0 . 938 112 112 ARG HD3 H 3.143 0.0 . 939 112 112 ARG HG2 H 1.65 0.0 . 940 113 113 GLY H H 9.408 0.0 . 941 113 113 GLY N N 106.636 0.0 . 942 113 113 GLY CA C 44.552 0.0 . 943 113 113 GLY C C 169.61 0.0 . 944 113 113 GLY HA2 H 1.51 0.0 . 945 114 114 PRO CA C 62.529 0.0 . 946 114 114 PRO C C 174.543 0.0 . 947 114 114 PRO HA H 4.321 0.0 . 948 114 114 PRO HB3 H 2.36 0.0 . 949 114 114 PRO HB2 H 1.892 0.0 . 950 114 114 PRO HG3 H 1.652 0.0 . 951 114 114 PRO HG2 H 1.505 0.0 . 952 115 115 ARG H H 8.067 0.0 . 953 115 115 ARG N N 114.5 0.0 . 954 115 115 ARG CA C 52.011 0.0 . 955 115 115 ARG CB C 27.143 0.0 . 956 115 115 ARG C C 174.68 0.0 . 957 115 115 ARG HA H 4.508 0.0 . 958 115 115 ARG HB3 H 2.133 0.0 . 959 115 115 ARG HB2 H 1.926 0.0 . 960 115 115 ARG HD3 H 3.205 0.0 . 961 115 115 ARG HD2 H 3.082 0.0 . 962 116 116 THR H H 7.643 0.0 . 963 116 116 THR N N 111.716 0.0 . 964 116 116 THR CA C 58.712 0.0 . 965 116 116 THR CB C 70.086 0.0 . 966 116 116 THR C C 172.573 0.0 . 967 116 116 THR HA H 5.198 0.0 . 968 116 116 THR HB H 4.104 0.0 . 969 116 116 THR HG2 H 1.118 0.0 . 970 117 117 HIS H H 7.091 0.0 . 971 117 117 HIS N N 112.914 0.0 . 972 117 117 HIS CA C 53.291 0.0 . 973 117 117 HIS CB C 29.133 0.0 . 974 117 117 HIS C C 170.344 0.0 . 975 117 117 HIS HA H 4.868 0.0 . 976 117 117 HIS HB3 H 3.4 0.0 . 977 117 117 HIS HB2 H 3.222 0.0 . 978 118 118 TYR H H 9.02 0.0 . 979 118 118 TYR N N 123.051 0.0 . 980 118 118 TYR CA C 58.801 0.0 . 981 118 118 TYR CB C 29.959 0.0 . 982 118 118 TYR C C 174.446 0.0 . 983 118 118 TYR HA H 3.897 0.0 . 984 118 118 TYR HB3 H 3.089 0.0 . 985 118 118 TYR HB2 H 2.936 0.0 . 986 119 119 GLY H H 7.999 0.0 . 987 119 119 GLY N N 116.885 0.0 . 988 119 119 GLY CA C 42.599 0.0 . 989 119 119 GLY C C 172.439 0.0 . 990 119 119 GLY HA3 H 4.385 0.0 . 991 119 119 GLY HA2 H 3.296 0.0 . 992 120 120 GLN H H 7.003 0.0 . 993 120 120 GLN N N 118.266 0.0 . 994 120 120 GLN CA C 52.617 0.0 . 995 120 120 GLN CB C 27.324 0.0 . 996 120 120 GLN C C 174.995 0.0 . 997 120 120 GLN HA H 4.262 0.0 . 998 120 120 GLN HB3 H 2.118 0.0 . 999 120 120 GLN HB2 H 2.005 0.0 . 1000 121 121 LYS H H 8.477 0.0 . 1001 121 121 LYS N N 121.222 0.0 . 1002 121 121 LYS CA C 56.243 0.0 . 1003 121 121 LYS CB C 29.598 0.0 . 1004 121 121 LYS C C 172.702 0.0 . 1005 121 121 LYS HA H 3.809 0.0 . 1006 121 121 LYS HB3 H 1.567 0.0 . 1007 121 121 LYS HB2 H 1.443 0.0 . 1008 121 121 LYS HD2 H 1.56 0.0 . 1009 121 121 LYS HG2 H 1.28 0.0 . 1010 122 122 ALA H H 7.526 0.0 . 1011 122 122 ALA N N 116.019 0.0 . 1012 122 122 ALA CA C 52.338 0.0 . 1013 122 122 ALA CB C 18.675 0.0 . 1014 122 122 ALA C C 172.756 0.0 . 1015 122 122 ALA HA H 3.947 0.0 . 1016 122 122 ALA HB H 1.143 0.0 . 1017 123 123 ILE H H 5.794 0.0 . 1018 123 123 ILE N N 101.2 0.0 . 1019 123 123 ILE CA C 57.297 0.0 . 1020 123 123 ILE CB C 35.425 0.0 . 1021 123 123 ILE C C 172.79 0.0 . 1022 123 123 ILE HA H 5.184 0.0 . 1023 123 123 ILE HB H 2.232 0.0 . 1024 123 123 ILE HG12 H 1.064 0.0 . 1025 123 123 ILE HG2 H 0.601 0.0 . 1026 123 123 ILE HD1 H -0.126 0.0 . 1027 124 124 LEU H H 6.716 0.0 . 1028 124 124 LEU N N 121.554 0.0 . 1029 124 124 LEU CA C 51.686 0.0 . 1030 124 124 LEU CB C 39.622 0.0 . 1031 124 124 LEU C C 173.411 0.0 . 1032 124 124 LEU HA H 4.597 0.0 . 1033 124 124 LEU HB3 H 0.67 0.0 . 1034 124 124 LEU HB2 H 0.67 0.0 . 1035 124 124 LEU HD1 H 0.407 0.0 . 1036 124 124 LEU HD2 H 0.407 0.0 . 1037 125 125 PHE H H 9.226 0.0 . 1038 125 125 PHE N N 121.9 0.0 . 1039 125 125 PHE CA C 54.604 0.0 . 1040 125 125 PHE CB C 41.692 0.0 . 1041 125 125 PHE C C 172.768 0.0 . 1042 125 125 PHE HA H 5.612 0.0 . 1043 125 125 PHE HB3 H 3.178 0.0 . 1044 125 125 PHE HB2 H 2.803 0.0 . 1045 126 126 LEU H H 9.932 0.0 . 1046 126 126 LEU N N 125.427 0.0 . 1047 126 126 LEU CA C 48.875 0.0 . 1048 127 127 PRO CA C 58.907 0.0 . 1049 127 127 PRO CB C 28.73 0.0 . 1050 127 127 PRO C C 174.541 0.0 . 1051 127 127 PRO HA H 5.587 0.0 . 1052 127 127 PRO HB2 H 2.04 0.0 . 1053 127 127 PRO HG2 H 2.386 0.0 . 1054 128 128 LEU H H 9.674 0.0 . 1055 128 128 LEU N N 129.196 0.0 . 1056 128 128 LEU CA C 49.523 0.0 . 1057 128 128 LEU C C 175.96 0.0 . 1058 129 129 PRO CA C 60.043 0.0 . 1059 129 129 PRO CB C 29.8 0.0 . 1060 129 129 PRO C C 174.414 0.0 . 1061 129 129 PRO HA H 4.71 0.0 . 1062 129 129 PRO HB3 H 2.355 0.0 . 1063 129 129 PRO HB2 H 1.961 0.0 . 1064 129 129 PRO HD3 H 3.901 0.0 . 1065 129 129 PRO HD2 H 3.654 0.0 . 1066 129 129 PRO HG2 H 2.146 0.0 . 1067 130 130 VAL H H 7.992 0.0 . 1068 130 130 VAL N N 118.275 0.0 . 1069 130 130 VAL CA C 61.494 0.0 . 1070 130 130 VAL CB C 29.649 0.0 . 1071 130 130 VAL C C 174.097 0.0 . 1072 130 130 VAL HA H 3.794 0.0 . 1073 130 130 VAL HB H 1.985 0.0 . 1074 130 130 VAL HG1 H 0.832 0.0 . 1075 130 130 VAL HG2 H 0.832 0.0 . 1076 131 131 SER H H 7.844 0.0 . 1077 131 131 SER N N 115.853 0.0 . 1078 131 131 SER CA C 55.233 0.0 . 1079 131 131 SER CB C 61.375 0.0 . 1080 131 131 SER C C 173.574 0.0 . 1081 131 131 SER HA H 4.218 0.0 . 1082 131 131 SER HB3 H 3.153 0.0 . 1083 131 131 SER HB2 H 3.153 0.0 . 1084 132 132 SER H H 8.196 0.0 . 1085 132 132 SER N N 118.1 0.0 . 1086 132 132 SER CA C 56.021 0.0 . 1087 132 132 SER CB C 61.848 0.0 . 1088 132 132 SER C C 170.997 0.0 . 1089 132 132 SER HA H 4.484 0.0 . 1090 132 132 SER HB3 H 3.873 0.0 . 1091 132 132 SER HB2 H 3.873 0.0 . 1092 133 133 ASP H H 7.926 0.0 . 1093 133 133 ASP N N 127.281 0.0 . 1094 133 133 ASP CA C 53.567 0.0 . stop_ save_