data_17915 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PFBD: High-throughput Strategy of Backbone fold Determination for small well-folded proteins in less than a day ; _BMRB_accession_number 17915 _BMRB_flat_file_name bmr17915.str _Entry_type original _Submission_date 2011-09-04 _Accession_date 2011-09-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR Method Developments' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumar Dinesh Dr. Jr. 2 Hosur 'Ramakrishna V' Prof. Sr. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 59 "13C chemical shifts" 114 "15N chemical shifts" 59 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-20 update BMRB 'update entry citation' 2011-10-07 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 3433 '1H and 15N assignments and secondary structure of the Src Sh3 domain' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Facile backbone (1H, 15N, 13Ca, and 13C') assignment of 13C/15N-labeled proteins using orthogonal projection planes of HNN and HN(C)N experiments and its automation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22508472 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kumar Dinesh . . 2 Borkar Aditi . . 3 Hosur Ramakrishna V. . stop_ _Journal_abbreviation 'Magn. Reson. Chem.' _Journal_name_full 'Magnetic resonance in chemistry : MRC' _Journal_volume 50 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 357 _Page_last 363 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SH3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SH3 $SH3 LL5_1 $LL5 LL5_2 $LL5 LL5_3 $LL5 LL5_4 $LL5 LL5_5 $LL5 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_SH3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SH3 _Molecular_mass 7229.313 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; MDETGKELVLALYDYQEKSP REVTMKKGDILTLLNSTNKD WWKVEVNDRQGFVPAAYVKK LD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASP 3 3 GLU 4 4 THR 5 5 GLY 6 6 LYS 7 7 GLU 8 8 LEU 9 9 VAL 10 10 LEU 11 11 ALA 12 12 LEU 13 13 TYR 14 14 ASP 15 15 TYR 16 16 GLN 17 17 GLU 18 18 LYS 19 19 SER 20 20 PRO 21 21 ARG 22 22 GLU 23 23 VAL 24 24 THR 25 25 MET 26 26 LYS 27 27 LYS 28 28 GLY 29 29 ASP 30 30 ILE 31 31 LEU 32 32 THR 33 33 LEU 34 34 LEU 35 35 ASN 36 36 SER 37 37 THR 38 38 ASN 39 39 LYS 40 40 ASP 41 41 TRP 42 42 TRP 43 43 LYS 44 44 VAL 45 45 GLU 46 46 VAL 47 47 ASN 48 48 ASP 49 49 ARG 50 50 GLN 51 51 GLY 52 52 PHE 53 53 VAL 54 54 PRO 55 55 ALA 56 56 ALA 57 57 TYR 58 58 VAL 59 59 LYS 60 60 LYS 61 61 LEU 62 62 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-30 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 15013 SPCp41 70.97 77 97.73 97.73 4.45e-22 BMRB 15144 SH3_domain_from_chicken_alpha-spectrin 100.00 62 100.00 100.00 4.13e-36 PDB 1AEY "Alpha-Spectrin Src Homology 3 Domain, Solution Nmr, 15 Structures" 100.00 62 100.00 100.00 4.13e-36 PDB 1BK2 "A-Spectrin Sh3 Domain D48g Mutant" 91.94 57 98.25 98.25 3.95e-31 PDB 1HD3 "A-Spectrin Sh3 Domain F52y Mutant" 100.00 62 98.39 100.00 1.61e-35 PDB 1M8M "Solid-State Mas Nmr Structure Of The A-Spectrin Sh3 Domain" 100.00 62 100.00 100.00 4.13e-36 PDB 1NEG "Crystal Structure Analysis Of N-And C-Terminal Labeled Sh3- Domain Of Alpha-Chicken Spectrin" 96.77 83 100.00 100.00 4.06e-35 PDB 1PWT "Thermodynamic Analysis Of Alpha-Spectrin Sh3 And Two Of Its Circular Permutants With Different Loop Lengths: Discerning The Rea" 95.16 61 100.00 100.00 9.12e-34 PDB 1QKW "Alpha-Spectrin Src Homology 3 Domain, N47g Mutant In The Distal Loop" 98.39 62 98.36 98.36 3.37e-34 PDB 1QKX "Alpha-Spectrin Src Homology 3 Domain, N47a Mutant In The Distal Loop" 98.39 62 98.36 98.36 3.80e-34 PDB 1SHG "Crystal Structure Of A Src-Homology 3 (Sh3) Domain" 100.00 62 100.00 100.00 4.13e-36 PDB 1U06 "Crystal Structure Of Chicken Alpha-Spectrin Sh3 Domain" 100.00 62 100.00 100.00 4.13e-36 PDB 2CDT "Alpha-Spectrin Sh3 Domain A56s Mutant" 100.00 62 98.39 100.00 1.23e-35 PDB 2F2V "Alpha-Spectrin Sh3 Domain A56g Mutant" 100.00 62 98.39 98.39 1.93e-35 PDB 2F2W "Alpha-Spectrin Sh3 Domain R21a Mutant" 100.00 62 98.39 98.39 3.92e-35 PDB 2F2X "Alpha-Spectrin Sh3 Domain R21g Mutant" 100.00 62 98.39 98.39 6.53e-35 PDB 2JM8 "R21a Spc-Sh3 Free" 100.00 62 98.39 98.39 3.92e-35 PDB 2JM9 "R21a Spc-Sh3 Bound" 100.00 62 98.39 98.39 3.92e-35 PDB 2JMA "R21a Spc-Sh3:p41 Complex" 100.00 62 98.39 98.39 3.92e-35 PDB 2JMC "Chimer Between Spc-Sh3 And P41" 70.97 77 97.73 97.73 4.45e-22 PDB 2LJ3 "Pfbd: High-Throughput Strategy Of Backbone Fold Determination For Small Well-Folded Proteins In Less Than A Day" 100.00 63 100.00 100.00 4.24e-36 PDB 2NUZ "Crystal Structure Of Alpha Spectrin Sh3 Domain Measured At Room Temperature" 100.00 62 100.00 100.00 4.13e-36 PDB 3M0P "Crystal Structure Of The R21d Mutant Of Alpha-spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 4." 100.00 62 98.39 98.39 6.97e-35 PDB 3M0Q "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 5." 100.00 62 98.39 98.39 6.97e-35 PDB 3M0R "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 6." 100.00 62 98.39 98.39 6.97e-35 PDB 3M0S "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 7" 91.94 57 98.25 98.25 7.66e-31 PDB 3M0T "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 9." 100.00 62 98.39 98.39 6.97e-35 PDB 3M0U "Crystal Structure Of The R21d Mutant Of Alpha-spectrin Sh3 Domain. Hexagonal Crystal Obtained In Sodium Formate At Ph 6.5" 100.00 62 98.39 98.39 6.97e-35 PDB 3THK "Structure Of Sh3 Chimera With A Type Ii Ligand Linked To The Chain C- Terminal" 95.16 73 100.00 100.00 7.25e-34 PDB 4F16 "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 5" 100.00 62 100.00 100.00 4.13e-36 PDB 4F17 "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 9" 100.00 62 100.00 100.00 4.13e-36 DBJ BAD52438 "non-erythrocytic spectrin alpha [Homo sapiens]" 98.39 2452 100.00 100.00 1.03e-32 DBJ BAD93097 "spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) variant [Homo sapiens]" 98.39 2506 100.00 100.00 1.19e-32 DBJ BAG57892 "unnamed protein product [Homo sapiens]" 98.39 1312 100.00 100.00 9.47e-33 DBJ BAG62120 "unnamed protein product [Homo sapiens]" 98.39 1176 100.00 100.00 7.18e-33 DBJ BAG72795 "spectrin, alpha, non-erythrocytic 1 [synthetic construct]" 98.39 2472 100.00 100.00 1.03e-32 EMBL CAA29435 "unnamed protein product [Xenopus laevis]" 91.94 454 100.00 100.00 5.85e-31 EMBL CAA32663 "spectrin alpha chain, partial [Gallus gallus]" 98.39 2449 100.00 100.00 1.17e-32 EMBL CAA62350 "alphaII spectrin [Rattus norvegicus]" 98.39 2472 100.00 100.00 1.06e-32 EMBL CAB53710 "hypothetical protein [Homo sapiens]" 54.84 1325 100.00 100.00 1.45e-11 EMBL CAF90367 "unnamed protein product [Tetraodon nigroviridis]" 98.39 1589 98.36 98.36 1.80e-29 GB AAA51702 "alpha-fodrin, partial [Homo sapiens]" 98.39 920 100.00 100.00 5.65e-33 GB AAA51790 "nonerythroid alpha-spectrin [Homo sapiens]" 98.39 2472 100.00 100.00 1.04e-32 GB AAA52468 "alpha-fodrin, partial [Homo sapiens]" 98.39 920 100.00 100.00 5.65e-33 GB AAB41498 "alpha II spectrin [Homo sapiens]" 98.39 2477 100.00 100.00 1.04e-32 GB AAB60364 "alpha II spectrin, partial [Homo sapiens]" 98.39 719 100.00 100.00 3.07e-33 REF NP_001036003 "spectrin alpha chain, non-erythrocytic 1 [Gallus gallus]" 98.39 2477 100.00 100.00 1.22e-32 REF NP_001090674 "spectrin alpha chain, non-erythrocytic 1 [Xenopus (Silurana) tropicalis]" 98.39 2471 100.00 100.00 1.23e-32 REF NP_001091958 "spectrin alpha chain, non-erythrocytic 1 [Danio rerio]" 98.39 2480 100.00 100.00 1.47e-32 REF NP_001107628 "spectrin alpha chain, non-erythrocytic 1 [Bos taurus]" 98.39 2472 100.00 100.00 1.06e-32 REF NP_001123910 "spectrin alpha chain, non-erythrocytic 1 isoform 1 [Homo sapiens]" 98.39 2477 100.00 100.00 1.04e-32 SP P07751 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain" 98.39 2477 100.00 100.00 1.22e-32 SP P16086 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain" 98.39 2472 100.00 100.00 1.03e-32 SP P16546 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain" 98.39 2472 100.00 100.00 1.08e-32 SP Q13813 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain; AltN" 98.39 2472 100.00 100.00 1.03e-32 TPG DAA24188 "TPA: spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) [Bos taurus]" 98.39 2472 100.00 100.00 1.06e-32 stop_ save_ ############# # Ligands # ############# save_LL5 _Saveframe_category ligand _Mol_type non-polymer _Name_common "LL5 ((2S)-2-amino-3-methyl-1-{4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidin-1-yl}butan-1-one)" _BMRB_code . _PDB_code LL5 _Molecular_mass 334.436 _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 Mon Sep 26 13:27:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C22 C22 C . 0 . ? C20 C20 C . 0 . ? C21 C21 C . 0 . ? C19 C19 C . 0 . ? N33 N33 N . 0 . ? C7 C7 C . 0 . ? O32 O32 O . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C6 C6 C . 0 . ? C5 C5 C . 0 . ? C4 C4 C . 0 . ? C14 C14 C . 0 . ? N23 N23 N . 0 . ? O26 O26 O . 0 . ? N25 N25 N . 0 . ? C24 C24 C . 0 . ? C27 C27 C . 0 . ? C31 C31 C . 0 . ? C30 C30 C . 0 . ? C29 C29 C . 0 . ? S28 S28 S . 0 . ? H22 H22 H . 0 . ? H22A H22A H . 0 . ? H22B H22B H . 0 . ? H20 H20 H . 0 . ? H21 H21 H . 0 . ? H21A H21A H . 0 . ? H21B H21B H . 0 . ? H19 H19 H . 0 . ? HN33 HN33 H . 0 . ? HN3A HN3A H . 0 . ? H2 H2 H . 0 . ? H2A H2A H . 0 . ? H3 H3 H . 0 . ? H3A H3A H . 0 . ? H6 H6 H . 0 . ? H6A H6A H . 0 . ? H5 H5 H . 0 . ? H5A H5A H . 0 . ? H4 H4 H . 0 . ? H31 H31 H . 0 . ? H30 H30 H . 0 . ? H29 H29 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 SING C22 C20 ? ? SING C22 H22 ? ? SING C22 H22A ? ? SING C22 H22B ? ? SING C20 C19 ? ? SING C20 C21 ? ? SING C20 H20 ? ? SING C21 H21 ? ? SING C21 H21A ? ? SING C21 H21B ? ? SING C7 C19 ? ? SING N33 C19 ? ? SING C19 H19 ? ? SING N33 HN33 ? ? SING N33 HN3A ? ? DOUB O32 C7 ? ? SING C7 N1 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING C3 C2 ? ? SING C2 H2 ? ? SING C2 H2A ? ? SING C4 C3 ? ? SING C3 H3 ? ? SING C3 H3A ? ? SING C5 C6 ? ? SING C6 H6 ? ? SING C6 H6A ? ? SING C5 C4 ? ? SING C5 H5 ? ? SING C5 H5A ? ? SING C14 C4 ? ? SING C4 H4 ? ? SING O26 C14 ? ? DOUB C14 N23 ? ? SING C24 N23 ? ? SING N25 O26 ? ? DOUB N25 C24 ? ? SING C24 C27 ? ? SING S28 C27 ? ? DOUB C27 C31 ? ? SING C30 C31 ? ? SING C31 H31 ? ? DOUB C29 C30 ? ? SING C30 H30 ? ? SING S28 C29 ? ? SING C29 H29 ? ? stop_ _Mol_thiol_state 'not present' _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 $SH3 chicken 9031 Eukaryota Metazoa Gallus Gallus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $SH3 'recombinant technology' . Escherichia coli . pGEX4T1 'Purchased from Cambridge Isotope Lab' 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 $SH3 1.2 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 50 mM 'natural abundance' NaCl 150 mM 'natural abundance' H2O 90 % 'natural abundance' D2O" 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version '3.0 Beta' loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_hNcnH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hNcnH' _Sample_label $sample_1 save_ save_2D_hncNH-G_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hncNH-G' _Sample_label $sample_1 save_ save_2D_hncNH-A_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hncNH-A' _Sample_label $sample_1 save_ save_2D_hncNH-ST_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hncNH-ST' _Sample_label $sample_1 save_ save_2D_cbcacoNH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D cbcacoNH' _Sample_label $sample_1 save_ save_2D_HnCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HnCO' _Sample_label $sample_1 save_ save_2D_hnCOcanH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hnCOcanH' _Sample_label $sample_1 save_ save_2D-HncoCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-HncoCA _Sample_label $sample_1 save_ save_2D_hncoCAnH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D hncoCAnH' _Sample_label $sample_1 save_ save_2D-(HN)NH-G,_A,_ST_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D-(HN)NH-G, A, ST' _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' 50 2 mM pH 6.5 0.1 pH pressure 1 . atm temperature 298 1 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D hNcnH' '2D hncNH-G' '2D hncNH-A' '2D hncNH-ST' '2D cbcacoNH' '2D HnCO' '2D hnCOcanH' 2D-HncoCA '2D hncoCAnH' '2D-(HN)NH-G, A, ST' 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 SH3 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 ASP H H 8.738 0.02 1 2 2 2 ASP C C 175.703 0.30 1 3 2 2 ASP CA C 54.041 0.30 1 4 2 2 ASP N N 123.22 0.30 1 5 3 3 GLU H H 8.57 0.02 1 6 3 3 GLU C C 176.48 0.30 1 7 3 3 GLU CA C 56.128 0.30 1 8 3 3 GLU N N 121.895 0.30 1 9 4 4 THR H H 8.176 0.02 1 10 4 4 THR C C 175.417 0.30 1 11 4 4 THR CA C 62.685 0.30 1 12 4 4 THR N N 114.607 0.30 1 13 5 5 GLY H H 8.344 0.02 1 14 5 5 GLY C C 173.777 0.30 1 15 5 5 GLY CA C 45.56 0.30 1 16 5 5 GLY N N 111.43 0.30 1 17 6 6 LYS H H 7.903 0.02 1 18 6 6 LYS C C 176.049 0.30 1 19 6 6 LYS CA C 55.914 0.30 1 20 6 6 LYS N N 119.85 0.30 1 21 7 7 GLU H H 8.562 0.02 1 22 7 7 GLU C C 174.172 0.30 1 23 7 7 GLU CA C 55.459 0.30 1 24 7 7 GLU N N 123.025 0.30 1 25 8 8 LEU H H 8.292 0.02 1 26 8 8 LEU C C 177.495 0.30 1 27 8 8 LEU CA C 53.425 0.30 1 28 8 8 LEU N N 123.147 0.30 1 29 9 9 VAL H H 9.051 0.02 1 30 9 9 VAL CA C 57.894 0.30 1 31 9 9 VAL N N 111.799 0.30 1 32 10 10 LEU H H 8.864 0.02 1 33 10 10 LEU C C 176.729 0.30 1 34 10 10 LEU CA C 52.489 0.30 1 35 10 10 LEU N N 123.127 0.30 1 36 11 11 ALA H H 8.988 0.02 1 37 11 11 ALA C C 178.406 0.30 1 38 11 11 ALA CA C 52.515 0.30 1 39 11 11 ALA N N 126.907 0.30 1 40 12 12 LEU H H 9.136 0.02 1 41 12 12 LEU C C 175.046 0.30 1 42 12 12 LEU CA C 55.727 0.30 1 43 12 12 LEU N N 127.694 0.30 1 44 13 13 TYR H H 6.979 0.02 1 45 13 13 TYR C C 173.844 0.30 1 46 13 13 TYR CA C 54.656 0.30 1 47 13 13 TYR N N 111.415 0.30 1 48 14 14 ASP H H 8.26 0.02 1 49 14 14 ASP C C 176.14 0.30 1 50 14 14 ASP CA C 54.522 0.30 1 51 14 14 ASP N N 117.591 0.30 1 52 15 15 TYR H H 8.58 0.02 1 53 15 15 TYR C C 172.859 0.30 1 54 15 15 TYR CA C 59.661 0.30 1 55 15 15 TYR N N 119.917 0.30 1 56 16 16 GLN H H 7.45 0.02 1 57 16 16 GLN C C 176.377 0.30 1 58 16 16 GLN CA C 53.666 0.30 1 59 16 16 GLN N N 127.024 0.30 1 60 17 17 GLU H H 7.899 0.02 1 61 17 17 GLU C C 176.14 0.30 1 62 17 17 GLU CA C 56.075 0.30 1 63 17 17 GLU N N 122.837 0.30 1 64 18 18 LYS H H 8.649 0.02 1 65 18 18 LYS C C 176.267 0.30 1 66 18 18 LYS CA C 55.245 0.30 1 67 18 18 LYS N N 120.622 0.30 1 68 19 19 SER H H 7.552 0.02 1 69 19 19 SER CA C 56.824 0.30 1 70 19 19 SER N N 115.184 0.30 1 71 21 21 ARG H H 7.596 0.02 1 72 21 21 ARG C C 176.638 0.30 1 73 21 21 ARG CA C 56.208 0.30 1 74 21 21 ARG N N 113.44 0.30 1 75 22 22 GLU H H 7.746 0.02 1 76 22 22 GLU C C 174.5 0.30 1 77 22 22 GLU CA C 55.352 0.30 1 78 22 22 GLU N N 121.392 0.30 1 79 23 23 VAL H H 7.318 0.02 1 80 23 23 VAL C C 172.337 0.30 1 81 23 23 VAL CA C 59.875 0.30 1 82 23 23 VAL N N 114.115 0.30 1 83 24 24 THR H H 7.324 0.02 1 84 24 24 THR C C 174.451 0.30 1 85 24 24 THR CA C 61.641 0.30 1 86 24 24 THR N N 118.996 0.30 1 87 25 25 MET H H 9.432 0.02 1 88 25 25 MET C C 173.931 0.30 1 89 25 25 MET CA C 54.389 0.30 1 90 25 25 MET N N 121.901 0.30 1 91 26 26 LYS H H 8.634 0.02 1 92 26 26 LYS C C 175.002 0.30 1 93 26 26 LYS CA C 53.666 0.30 1 94 26 26 LYS N N 124.169 0.30 1 95 27 27 LYS H H 8.919 0.02 1 96 27 27 LYS C C 177.318 0.30 1 97 27 27 LYS CA C 58.644 0.30 1 98 27 27 LYS N N 122.603 0.30 1 99 28 28 GLY H H 8.732 0.02 1 100 28 28 GLY C C 174.193 0.30 1 101 28 28 GLY CA C 44.888 0.30 1 102 28 28 GLY N N 115.585 0.30 1 103 29 29 ASP H H 8.388 0.02 1 104 29 29 ASP C C 174.281 0.30 1 105 29 29 ASP CA C 55.486 0.30 1 106 29 29 ASP N N 121.77 0.30 1 107 30 30 ILE H H 8.033 0.02 1 108 30 30 ILE C C 176.356 0.30 1 109 30 30 ILE CA C 60.249 0.30 1 110 30 30 ILE N N 120.469 0.30 1 111 31 31 LEU H H 9.223 0.02 1 112 31 31 LEU C C 175.745 0.30 1 113 31 31 LEU CA C 53.907 0.30 1 114 31 31 LEU N N 127.129 0.30 1 115 32 32 THR H H 8.36 0.02 1 116 32 32 THR C C 173.844 0.30 1 117 32 32 THR CA C 63.247 0.30 1 118 32 32 THR N N 117.055 0.30 1 119 33 33 LEU H H 8.937 0.02 1 120 33 33 LEU C C 174.718 0.30 1 121 33 33 LEU CA C 54.87 0.30 1 122 33 33 LEU N N 128.815 0.30 1 123 34 34 LEU H H 8.929 0.02 1 124 34 34 LEU C C 177.689 0.30 1 125 34 34 LEU CA C 55.218 0.30 1 126 34 34 LEU N N 126.23 0.30 1 127 35 35 ASN H H 7.489 0.02 1 128 35 35 ASN C C 174.565 0.30 1 129 35 35 ASN CA C 54.576 0.30 1 130 35 35 ASN N N 113.879 0.30 1 131 36 36 SER H H 9.086 0.02 1 132 36 36 SER C C 173.503 0.30 1 133 36 36 SER CA C 56.904 0.30 1 134 36 36 SER N N 123.684 0.30 1 135 37 37 THR H H 8.071 0.02 1 136 37 37 THR C C 175.417 0.30 1 137 37 37 THR CA C 65.521 0.30 1 138 37 37 THR N N 115.012 0.30 1 139 38 38 ASN H H 8.595 0.02 1 140 38 38 ASN C C 174.696 0.30 1 141 38 38 ASN CA C 53.479 0.30 1 142 38 38 ASN N N 122.517 0.30 1 143 39 39 LYS H H 8.416 0.02 1 144 39 39 LYS C C 176.444 0.30 1 145 39 39 LYS CA C 58.403 0.30 1 146 39 39 LYS N N 120.851 0.30 1 147 40 40 ASP H H 8.085 0.02 1 148 40 40 ASP C C 176.96 0.30 1 149 40 40 ASP CA C 55.352 0.30 1 150 40 40 ASP N N 114.427 0.30 1 151 41 41 TRP H H 8.096 0.02 1 152 41 41 TRP C C 174.303 0.30 1 153 41 41 TRP CA C 56.208 0.30 1 154 41 41 TRP N N 122.708 0.30 1 155 42 42 TRP H H 9.245 0.02 1 156 42 42 TRP C C 174.303 0.30 1 157 42 42 TRP CA C 53.987 0.30 1 158 42 42 TRP N N 124.707 0.30 1 159 43 43 LYS H H 8.783 0.02 1 160 43 43 LYS C C 175.482 0.30 1 161 43 43 LYS CA C 55.379 0.30 1 162 43 43 LYS N N 124.005 0.30 1 163 44 44 VAL H H 9.287 0.02 1 164 44 44 VAL C C 173.472 0.30 1 165 44 44 VAL CA C 59.072 0.30 1 166 44 44 VAL N N 122.139 0.30 1 167 45 45 GLU H H 8.566 0.02 1 168 45 45 GLU C C 174.827 0.30 1 169 45 45 GLU CA C 54.174 0.30 1 170 45 45 GLU N N 118.524 0.30 1 171 46 46 VAL H H 8.774 0.02 1 172 46 46 VAL C C 174.608 0.30 1 173 46 46 VAL CA C 60.651 0.30 1 174 46 46 VAL N N 124.904 0.30 1 175 47 47 ASN H H 9.356 0.02 1 176 47 47 ASN C C 174.259 0.30 1 177 47 47 ASN CA C 55.245 0.30 1 178 47 47 ASN N N 126.53 0.30 1 179 48 48 ASP H H 8.628 0.02 1 180 48 48 ASP C C 174.521 0.30 1 181 48 48 ASP CA C 54.683 0.30 1 182 48 48 ASP N N 112.42 0.30 1 183 49 49 ARG H H 8.069 0.02 1 184 49 49 ARG C C 174.477 0.30 1 185 49 49 ARG CA C 55.298 0.30 1 186 49 49 ARG N N 120.379 0.30 1 187 50 50 GLN H H 8.432 0.02 1 188 50 50 GLN C C 175.963 0.30 1 189 50 50 GLN CA C 53.425 0.30 1 190 50 50 GLN N N 118.647 0.30 1 191 51 51 GLY H H 8.534 0.02 1 192 51 51 GLY C C 170.479 0.30 1 193 51 51 GLY CA C 45.638 0.30 1 194 51 51 GLY N N 107.028 0.30 1 195 52 52 PHE H H 9.098 0.02 1 196 52 52 PHE C C 175.635 0.30 1 197 52 52 PHE CA C 58.724 0.30 1 198 52 52 PHE N N 119.03 0.30 1 199 53 53 VAL H H 8.942 0.02 1 200 53 53 VAL CA C 58.108 0.30 1 201 53 53 VAL N N 110.897 0.30 1 202 55 55 ALA H H 7.355 0.02 1 203 55 55 ALA C C 178.565 0.30 1 204 55 55 ALA CA C 54.629 0.30 1 205 55 55 ALA N N 129.055 0.30 1 206 56 56 ALA H H 7.75 0.02 1 207 56 56 ALA C C 178.214 0.30 1 208 56 56 ALA CA C 52.943 0.30 1 209 56 56 ALA N N 113.282 0.30 1 210 57 57 TYR H H 7.611 0.02 1 211 57 57 TYR C C 174.565 0.30 1 212 57 57 TYR CA C 56.422 0.30 1 213 57 57 TYR N N 116.083 0.30 1 214 58 58 VAL H H 7.301 0.02 1 215 58 58 VAL C C 173.647 0.30 1 216 58 58 VAL CA C 58.242 0.30 1 217 58 58 VAL N N 110.965 0.30 1 218 59 59 LYS H H 8.515 0.02 1 219 59 59 LYS C C 176.16 0.30 1 220 59 59 LYS CA C 54.041 0.30 1 221 59 59 LYS N N 118.586 0.30 1 222 60 60 LYS H H 9.135 0.02 1 223 60 60 LYS C C 176.793 0.30 1 224 60 60 LYS CA C 58.617 0.30 1 225 60 60 LYS N N 125.734 0.30 1 226 61 61 LEU H H 8.384 0.02 1 227 61 61 LEU C C 174.106 0.30 1 228 61 61 LEU CA C 54.977 0.30 1 229 61 61 LEU N N 125.061 0.30 1 230 62 62 ASP H H 7.923 0.02 1 231 62 62 ASP CA C 56.101 0.30 1 232 62 62 ASP N N 123.073 0.30 1 stop_ save_