data_PB ############################# # Protein Blocks Annotation # ############################# ####################################################################################### # PB encoding by Protein Blocks Expert 2.0 server (http://www.bo-protscience.fr/pbe/) # # Reference: Biophys Rev. 2010 Aug;2(3):137-147. Epub 2010 Aug 5. # # : Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W119-23. # ####################################################################################### save_PB_annotation_1 _PB_list.Sf_category PB_list _PB_list.ID 1 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpccddfbhbacdfklmmmmmmmmmccezz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 1 A . 1 MET . 1 7260 1 1 1 1 2 ASN 1 A . 2 ASN . 1 7260 1 1 1 1 3 LYS 1 A . 3 LYS . 1 7260 1 1 1 1 4 ASP 1 A . 4 ASP . 1 7260 1 1 1 1 5 LYS 1 A . 5 LYS . 1 7260 1 1 1 1 6 LEU 1 A . 6 LEU . 1 7260 1 1 1 1 7 ARG 1 A . 7 ARG m 1 7260 1 1 1 1 8 TYR 1 A . 8 TYR m 1 7260 1 1 1 1 9 ALA 1 A . 9 ALA m 1 7260 1 1 1 1 10 ILE 1 A . 10 ILE m 1 7260 1 1 1 1 11 LEU 1 A . 11 LEU m 1 7260 1 1 1 1 12 LYS 1 A . 12 LYS m 1 7260 1 1 1 1 13 GLU 1 A . 13 GLU m 1 7260 1 1 1 1 14 ILE 1 A . 14 ILE m 1 7260 1 1 1 1 15 PHE 1 A . 15 PHE m 1 7260 1 1 1 1 16 GLU 1 A . 16 GLU n 1 7260 1 1 1 1 17 GLY 1 A . 17 GLY o 1 7260 1 1 1 1 18 ASN 1 A . 18 ASN p 1 7260 1 1 1 1 19 THR 1 A . 19 THR a 1 7260 1 1 1 1 20 PRO 1 A . 20 PRO a 1 7260 1 1 1 1 21 LEU 1 A . 21 LEU d 1 7260 1 1 1 1 22 SER 1 A . 22 SER f 1 7260 1 1 1 1 23 GLU 1 A . 23 GLU k 1 7260 1 1 1 1 24 ASN 1 A . 24 ASN l 1 7260 1 1 1 1 25 ASP 1 A . 25 ASP n 1 7260 1 1 1 1 26 ILE 1 A . 26 ILE o 1 7260 1 1 1 1 27 GLY 1 A . 27 GLY p 1 7260 1 1 1 1 28 VAL 1 A . 28 VAL a 1 7260 1 1 1 1 29 THR 1 A . 29 THR f 1 7260 1 1 1 1 30 GLU 1 A . 30 GLU k 1 7260 1 1 1 1 31 ASP 1 A . 31 ASP l 1 7260 1 1 1 1 32 GLN 1 A . 32 GLN m 1 7260 1 1 1 1 33 PHE 1 A . 33 PHE m 1 7260 1 1 1 1 34 ASP 1 A . 34 ASP m 1 7260 1 1 1 1 35 ASP 1 A . 35 ASP m 1 7260 1 1 1 1 36 ALA 1 A . 36 ALA m 1 7260 1 1 1 1 37 VAL 1 A . 37 VAL m 1 7260 1 1 1 1 38 ASN 1 A . 38 ASN m 1 7260 1 1 1 1 39 PHE 1 A . 39 PHE m 1 7260 1 1 1 1 40 LEU 1 A . 40 LEU m 1 7260 1 1 1 1 41 LYS 1 A . 41 LYS m 1 7260 1 1 1 1 42 ARG 1 A . 42 ARG n 1 7260 1 1 1 1 43 GLU 1 A . 43 GLU o 1 7260 1 1 1 1 44 GLY 1 A . 44 GLY p 1 7260 1 1 1 1 45 TYR 1 A . 45 TYR a 1 7260 1 1 1 1 46 ILE 1 A . 46 ILE g 1 7260 1 1 1 1 47 ILE 1 A . 47 ILE h 1 7260 1 1 1 1 48 GLY 1 A . 48 GLY i 1 7260 1 1 1 1 49 VAL 1 A . 49 VAL a 1 7260 1 1 1 1 50 HIS 1 A . 50 HIS c 1 7260 1 1 1 1 51 TYR 1 A . 51 TYR f 1 7260 1 1 1 1 52 SER 1 A . 52 SER k 1 7260 1 1 1 1 53 ASP 1 A . 53 ASP l 1 7260 1 1 1 1 54 ASP 1 A . 54 ASP p 1 7260 1 1 1 1 55 ARG 1 A . 55 ARG c 1 7260 1 1 1 1 56 PRO 1 A . 56 PRO c 1 7260 1 1 1 1 57 HIS 1 A . 57 HIS d 1 7260 1 1 1 1 58 LEU 1 A . 58 LEU d 1 7260 1 1 1 1 59 TYR 1 A . 59 TYR f 1 7260 1 1 1 1 60 LYS 1 A . 60 LYS b 1 7260 1 1 1 1 61 LEU 1 A . 61 LEU h 1 7260 1 1 1 1 62 GLY 1 A . 62 GLY b 1 7260 1 1 1 1 63 PRO 1 A . 63 PRO a 1 7260 1 1 1 1 64 GLU 1 A . 64 GLU c 1 7260 1 1 1 1 65 LEU 1 A . 65 LEU d 1 7260 1 1 1 1 66 THR 1 A . 66 THR f 1 7260 1 1 1 1 67 GLU 1 A . 67 GLU k 1 7260 1 1 1 1 68 LYS 1 A . 68 LYS l 1 7260 1 1 1 1 69 GLY 1 A . 69 GLY m 1 7260 1 1 1 1 70 GLU 1 A . 70 GLU m 1 7260 1 1 1 1 71 ASN 1 A . 71 ASN m 1 7260 1 1 1 1 72 TYR 1 A . 72 TYR m 1 7260 1 1 1 1 73 LEU 1 A . 73 LEU m 1 7260 1 1 1 1 74 LYS 1 A . 74 LYS m 1 7260 1 1 1 1 75 GLU 1 A . 75 GLU m 1 7260 1 1 1 1 76 ASN 1 A . 76 ASN m 1 7260 1 1 1 1 77 GLY 1 A . 77 GLY m 1 7260 1 1 1 1 78 THR 1 A . 78 THR c 1 7260 1 1 1 1 79 TRP 1 A . 79 TRP c 1 7260 1 1 1 1 80 SER 1 A . 80 SER e 1 7260 1 1 1 1 81 LYS 1 A . 81 LYS . 1 7260 1 1 1 1 82 ALA 1 A . 82 ALA . 1 7260 1 1 1 1 83 TYR 1 A . 83 TYR . 1 7260 1 1 1 1 84 LYS 1 A . 84 LYS . 1 7260 1 1 1 1 85 THR 1 A . 85 THR . 1 7260 1 1 1 1 86 ILE 1 A . 86 ILE . 1 7260 1 1 1 1 87 LYS 1 A . 87 LYS . 1 7260 1 1 1 1 88 GLU 1 A . 88 GLU . 1 7260 1 1 1 1 89 ILE 1 A . 89 ILE . 1 7260 1 1 1 1 90 LYS 1 A . 90 LYS . 1 7260 1 1 1 1 91 ASP 1 A . 91 ASP . 1 7260 1 1 1 1 92 TRP 1 A . 92 TRP . 1 7260 1 1 1 1 93 ILE 1 A . 93 ILE . 1 7260 1 1 1 1 94 LYS 1 A . 94 LYS . 1 7260 1 1 1 1 95 LEU 1 A . 95 LEU . 1 7260 1 1 1 1 96 GLU 1 A . 96 GLU . 1 7260 1 1 1 1 97 HIS 1 A . 97 HIS . 1 7260 1 1 1 1 98 HIS 1 A . 98 HIS . 1 7260 1 1 1 1 99 HIS 1 A . 99 HIS . 1 7260 1 1 1 1 100 HIS 1 A . 100 HIS . 1 7260 1 1 1 1 101 HIS 1 A . 101 HIS . 1 7260 1 1 1 1 102 HIS 1 A . 102 HIS . 1 7260 1 stop_ save_ save_PB_annotation_2 _PB_list.Sf_category PB_list _PB_list.ID 2 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopacdfklnopafklmmmmmmmmmmnopaghiacdfkbccddfblcacdfklmmmmmmmmgojfzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 2 A . 1 MET . 1 7260 2 1 1 1 2 ASN 2 A . 2 ASN . 1 7260 2 1 1 1 3 LYS 2 A . 3 LYS . 1 7260 2 1 1 1 4 ASP 2 A . 4 ASP . 1 7260 2 1 1 1 5 LYS 2 A . 5 LYS . 1 7260 2 1 1 1 6 LEU 2 A . 6 LEU . 1 7260 2 1 1 1 7 ARG 2 A . 7 ARG m 1 7260 2 1 1 1 8 TYR 2 A . 8 TYR m 1 7260 2 1 1 1 9 ALA 2 A . 9 ALA m 1 7260 2 1 1 1 10 ILE 2 A . 10 ILE m 1 7260 2 1 1 1 11 LEU 2 A . 11 LEU m 1 7260 2 1 1 1 12 LYS 2 A . 12 LYS m 1 7260 2 1 1 1 13 GLU 2 A . 13 GLU m 1 7260 2 1 1 1 14 ILE 2 A . 14 ILE m 1 7260 2 1 1 1 15 PHE 2 A . 15 PHE m 1 7260 2 1 1 1 16 GLU 2 A . 16 GLU n 1 7260 2 1 1 1 17 GLY 2 A . 17 GLY o 1 7260 2 1 1 1 18 ASN 2 A . 18 ASN p 1 7260 2 1 1 1 19 THR 2 A . 19 THR a 1 7260 2 1 1 1 20 PRO 2 A . 20 PRO c 1 7260 2 1 1 1 21 LEU 2 A . 21 LEU d 1 7260 2 1 1 1 22 SER 2 A . 22 SER f 1 7260 2 1 1 1 23 GLU 2 A . 23 GLU k 1 7260 2 1 1 1 24 ASN 2 A . 24 ASN l 1 7260 2 1 1 1 25 ASP 2 A . 25 ASP n 1 7260 2 1 1 1 26 ILE 2 A . 26 ILE o 1 7260 2 1 1 1 27 GLY 2 A . 27 GLY p 1 7260 2 1 1 1 28 VAL 2 A . 28 VAL a 1 7260 2 1 1 1 29 THR 2 A . 29 THR f 1 7260 2 1 1 1 30 GLU 2 A . 30 GLU k 1 7260 2 1 1 1 31 ASP 2 A . 31 ASP l 1 7260 2 1 1 1 32 GLN 2 A . 32 GLN m 1 7260 2 1 1 1 33 PHE 2 A . 33 PHE m 1 7260 2 1 1 1 34 ASP 2 A . 34 ASP m 1 7260 2 1 1 1 35 ASP 2 A . 35 ASP m 1 7260 2 1 1 1 36 ALA 2 A . 36 ALA m 1 7260 2 1 1 1 37 VAL 2 A . 37 VAL m 1 7260 2 1 1 1 38 ASN 2 A . 38 ASN m 1 7260 2 1 1 1 39 PHE 2 A . 39 PHE m 1 7260 2 1 1 1 40 LEU 2 A . 40 LEU m 1 7260 2 1 1 1 41 LYS 2 A . 41 LYS m 1 7260 2 1 1 1 42 ARG 2 A . 42 ARG n 1 7260 2 1 1 1 43 GLU 2 A . 43 GLU o 1 7260 2 1 1 1 44 GLY 2 A . 44 GLY p 1 7260 2 1 1 1 45 TYR 2 A . 45 TYR a 1 7260 2 1 1 1 46 ILE 2 A . 46 ILE g 1 7260 2 1 1 1 47 ILE 2 A . 47 ILE h 1 7260 2 1 1 1 48 GLY 2 A . 48 GLY i 1 7260 2 1 1 1 49 VAL 2 A . 49 VAL a 1 7260 2 1 1 1 50 HIS 2 A . 50 HIS c 1 7260 2 1 1 1 51 TYR 2 A . 51 TYR d 1 7260 2 1 1 1 52 SER 2 A . 52 SER f 1 7260 2 1 1 1 53 ASP 2 A . 53 ASP k 1 7260 2 1 1 1 54 ASP 2 A . 54 ASP b 1 7260 2 1 1 1 55 ARG 2 A . 55 ARG c 1 7260 2 1 1 1 56 PRO 2 A . 56 PRO c 1 7260 2 1 1 1 57 HIS 2 A . 57 HIS d 1 7260 2 1 1 1 58 LEU 2 A . 58 LEU d 1 7260 2 1 1 1 59 TYR 2 A . 59 TYR f 1 7260 2 1 1 1 60 LYS 2 A . 60 LYS b 1 7260 2 1 1 1 61 LEU 2 A . 61 LEU l 1 7260 2 1 1 1 62 GLY 2 A . 62 GLY c 1 7260 2 1 1 1 63 PRO 2 A . 63 PRO a 1 7260 2 1 1 1 64 GLU 2 A . 64 GLU c 1 7260 2 1 1 1 65 LEU 2 A . 65 LEU d 1 7260 2 1 1 1 66 THR 2 A . 66 THR f 1 7260 2 1 1 1 67 GLU 2 A . 67 GLU k 1 7260 2 1 1 1 68 LYS 2 A . 68 LYS l 1 7260 2 1 1 1 69 GLY 2 A . 69 GLY m 1 7260 2 1 1 1 70 GLU 2 A . 70 GLU m 1 7260 2 1 1 1 71 ASN 2 A . 71 ASN m 1 7260 2 1 1 1 72 TYR 2 A . 72 TYR m 1 7260 2 1 1 1 73 LEU 2 A . 73 LEU m 1 7260 2 1 1 1 74 LYS 2 A . 74 LYS m 1 7260 2 1 1 1 75 GLU 2 A . 75 GLU m 1 7260 2 1 1 1 76 ASN 2 A . 76 ASN m 1 7260 2 1 1 1 77 GLY 2 A . 77 GLY g 1 7260 2 1 1 1 78 THR 2 A . 78 THR o 1 7260 2 1 1 1 79 TRP 2 A . 79 TRP j 1 7260 2 1 1 1 80 SER 2 A . 80 SER f 1 7260 2 1 1 1 81 LYS 2 A . 81 LYS . 1 7260 2 1 1 1 82 ALA 2 A . 82 ALA . 1 7260 2 1 1 1 83 TYR 2 A . 83 TYR . 1 7260 2 1 1 1 84 LYS 2 A . 84 LYS . 1 7260 2 1 1 1 85 THR 2 A . 85 THR . 1 7260 2 1 1 1 86 ILE 2 A . 86 ILE . 1 7260 2 1 1 1 87 LYS 2 A . 87 LYS . 1 7260 2 1 1 1 88 GLU 2 A . 88 GLU . 1 7260 2 1 1 1 89 ILE 2 A . 89 ILE . 1 7260 2 1 1 1 90 LYS 2 A . 90 LYS . 1 7260 2 1 1 1 91 ASP 2 A . 91 ASP . 1 7260 2 1 1 1 92 TRP 2 A . 92 TRP . 1 7260 2 1 1 1 93 ILE 2 A . 93 ILE . 1 7260 2 1 1 1 94 LYS 2 A . 94 LYS . 1 7260 2 1 1 1 95 LEU 2 A . 95 LEU . 1 7260 2 1 1 1 96 GLU 2 A . 96 GLU . 1 7260 2 1 1 1 97 HIS 2 A . 97 HIS . 1 7260 2 1 1 1 98 HIS 2 A . 98 HIS . 1 7260 2 1 1 1 99 HIS 2 A . 99 HIS . 1 7260 2 1 1 1 100 HIS 2 A . 100 HIS . 1 7260 2 1 1 1 101 HIS 2 A . 101 HIS . 1 7260 2 1 1 1 102 HIS 2 A . 102 HIS . 1 7260 2 stop_ save_ save_PB_annotation_3 _PB_list.Sf_category PB_list _PB_list.ID 3 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopacdfklnopafklmmmmmmmmmmnopaghiacfkopacddfbhpacdfklmmmmmmmmnmopzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 3 A . 1 MET . 1 7260 3 1 1 1 2 ASN 3 A . 2 ASN . 1 7260 3 1 1 1 3 LYS 3 A . 3 LYS . 1 7260 3 1 1 1 4 ASP 3 A . 4 ASP . 1 7260 3 1 1 1 5 LYS 3 A . 5 LYS . 1 7260 3 1 1 1 6 LEU 3 A . 6 LEU . 1 7260 3 1 1 1 7 ARG 3 A . 7 ARG m 1 7260 3 1 1 1 8 TYR 3 A . 8 TYR m 1 7260 3 1 1 1 9 ALA 3 A . 9 ALA m 1 7260 3 1 1 1 10 ILE 3 A . 10 ILE m 1 7260 3 1 1 1 11 LEU 3 A . 11 LEU m 1 7260 3 1 1 1 12 LYS 3 A . 12 LYS m 1 7260 3 1 1 1 13 GLU 3 A . 13 GLU m 1 7260 3 1 1 1 14 ILE 3 A . 14 ILE m 1 7260 3 1 1 1 15 PHE 3 A . 15 PHE m 1 7260 3 1 1 1 16 GLU 3 A . 16 GLU n 1 7260 3 1 1 1 17 GLY 3 A . 17 GLY o 1 7260 3 1 1 1 18 ASN 3 A . 18 ASN p 1 7260 3 1 1 1 19 THR 3 A . 19 THR a 1 7260 3 1 1 1 20 PRO 3 A . 20 PRO c 1 7260 3 1 1 1 21 LEU 3 A . 21 LEU d 1 7260 3 1 1 1 22 SER 3 A . 22 SER f 1 7260 3 1 1 1 23 GLU 3 A . 23 GLU k 1 7260 3 1 1 1 24 ASN 3 A . 24 ASN l 1 7260 3 1 1 1 25 ASP 3 A . 25 ASP n 1 7260 3 1 1 1 26 ILE 3 A . 26 ILE o 1 7260 3 1 1 1 27 GLY 3 A . 27 GLY p 1 7260 3 1 1 1 28 VAL 3 A . 28 VAL a 1 7260 3 1 1 1 29 THR 3 A . 29 THR f 1 7260 3 1 1 1 30 GLU 3 A . 30 GLU k 1 7260 3 1 1 1 31 ASP 3 A . 31 ASP l 1 7260 3 1 1 1 32 GLN 3 A . 32 GLN m 1 7260 3 1 1 1 33 PHE 3 A . 33 PHE m 1 7260 3 1 1 1 34 ASP 3 A . 34 ASP m 1 7260 3 1 1 1 35 ASP 3 A . 35 ASP m 1 7260 3 1 1 1 36 ALA 3 A . 36 ALA m 1 7260 3 1 1 1 37 VAL 3 A . 37 VAL m 1 7260 3 1 1 1 38 ASN 3 A . 38 ASN m 1 7260 3 1 1 1 39 PHE 3 A . 39 PHE m 1 7260 3 1 1 1 40 LEU 3 A . 40 LEU m 1 7260 3 1 1 1 41 LYS 3 A . 41 LYS m 1 7260 3 1 1 1 42 ARG 3 A . 42 ARG n 1 7260 3 1 1 1 43 GLU 3 A . 43 GLU o 1 7260 3 1 1 1 44 GLY 3 A . 44 GLY p 1 7260 3 1 1 1 45 TYR 3 A . 45 TYR a 1 7260 3 1 1 1 46 ILE 3 A . 46 ILE g 1 7260 3 1 1 1 47 ILE 3 A . 47 ILE h 1 7260 3 1 1 1 48 GLY 3 A . 48 GLY i 1 7260 3 1 1 1 49 VAL 3 A . 49 VAL a 1 7260 3 1 1 1 50 HIS 3 A . 50 HIS c 1 7260 3 1 1 1 51 TYR 3 A . 51 TYR f 1 7260 3 1 1 1 52 SER 3 A . 52 SER k 1 7260 3 1 1 1 53 ASP 3 A . 53 ASP o 1 7260 3 1 1 1 54 ASP 3 A . 54 ASP p 1 7260 3 1 1 1 55 ARG 3 A . 55 ARG a 1 7260 3 1 1 1 56 PRO 3 A . 56 PRO c 1 7260 3 1 1 1 57 HIS 3 A . 57 HIS d 1 7260 3 1 1 1 58 LEU 3 A . 58 LEU d 1 7260 3 1 1 1 59 TYR 3 A . 59 TYR f 1 7260 3 1 1 1 60 LYS 3 A . 60 LYS b 1 7260 3 1 1 1 61 LEU 3 A . 61 LEU h 1 7260 3 1 1 1 62 GLY 3 A . 62 GLY p 1 7260 3 1 1 1 63 PRO 3 A . 63 PRO a 1 7260 3 1 1 1 64 GLU 3 A . 64 GLU c 1 7260 3 1 1 1 65 LEU 3 A . 65 LEU d 1 7260 3 1 1 1 66 THR 3 A . 66 THR f 1 7260 3 1 1 1 67 GLU 3 A . 67 GLU k 1 7260 3 1 1 1 68 LYS 3 A . 68 LYS l 1 7260 3 1 1 1 69 GLY 3 A . 69 GLY m 1 7260 3 1 1 1 70 GLU 3 A . 70 GLU m 1 7260 3 1 1 1 71 ASN 3 A . 71 ASN m 1 7260 3 1 1 1 72 TYR 3 A . 72 TYR m 1 7260 3 1 1 1 73 LEU 3 A . 73 LEU m 1 7260 3 1 1 1 74 LYS 3 A . 74 LYS m 1 7260 3 1 1 1 75 GLU 3 A . 75 GLU m 1 7260 3 1 1 1 76 ASN 3 A . 76 ASN m 1 7260 3 1 1 1 77 GLY 3 A . 77 GLY n 1 7260 3 1 1 1 78 THR 3 A . 78 THR m 1 7260 3 1 1 1 79 TRP 3 A . 79 TRP o 1 7260 3 1 1 1 80 SER 3 A . 80 SER p 1 7260 3 1 1 1 81 LYS 3 A . 81 LYS . 1 7260 3 1 1 1 82 ALA 3 A . 82 ALA . 1 7260 3 1 1 1 83 TYR 3 A . 83 TYR . 1 7260 3 1 1 1 84 LYS 3 A . 84 LYS . 1 7260 3 1 1 1 85 THR 3 A . 85 THR . 1 7260 3 1 1 1 86 ILE 3 A . 86 ILE . 1 7260 3 1 1 1 87 LYS 3 A . 87 LYS . 1 7260 3 1 1 1 88 GLU 3 A . 88 GLU . 1 7260 3 1 1 1 89 ILE 3 A . 89 ILE . 1 7260 3 1 1 1 90 LYS 3 A . 90 LYS . 1 7260 3 1 1 1 91 ASP 3 A . 91 ASP . 1 7260 3 1 1 1 92 TRP 3 A . 92 TRP . 1 7260 3 1 1 1 93 ILE 3 A . 93 ILE . 1 7260 3 1 1 1 94 LYS 3 A . 94 LYS . 1 7260 3 1 1 1 95 LEU 3 A . 95 LEU . 1 7260 3 1 1 1 96 GLU 3 A . 96 GLU . 1 7260 3 1 1 1 97 HIS 3 A . 97 HIS . 1 7260 3 1 1 1 98 HIS 3 A . 98 HIS . 1 7260 3 1 1 1 99 HIS 3 A . 99 HIS . 1 7260 3 1 1 1 100 HIS 3 A . 100 HIS . 1 7260 3 1 1 1 101 HIS 3 A . 101 HIS . 1 7260 3 1 1 1 102 HIS 3 A . 102 HIS . 1 7260 3 stop_ save_ save_PB_annotation_4 _PB_list.Sf_category PB_list _PB_list.ID 4 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacehiaacddfblpacdfklmmmmmmmmmpcczz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 4 A . 1 MET . 1 7260 4 1 1 1 2 ASN 4 A . 2 ASN . 1 7260 4 1 1 1 3 LYS 4 A . 3 LYS . 1 7260 4 1 1 1 4 ASP 4 A . 4 ASP . 1 7260 4 1 1 1 5 LYS 4 A . 5 LYS . 1 7260 4 1 1 1 6 LEU 4 A . 6 LEU . 1 7260 4 1 1 1 7 ARG 4 A . 7 ARG m 1 7260 4 1 1 1 8 TYR 4 A . 8 TYR m 1 7260 4 1 1 1 9 ALA 4 A . 9 ALA m 1 7260 4 1 1 1 10 ILE 4 A . 10 ILE m 1 7260 4 1 1 1 11 LEU 4 A . 11 LEU m 1 7260 4 1 1 1 12 LYS 4 A . 12 LYS m 1 7260 4 1 1 1 13 GLU 4 A . 13 GLU m 1 7260 4 1 1 1 14 ILE 4 A . 14 ILE m 1 7260 4 1 1 1 15 PHE 4 A . 15 PHE m 1 7260 4 1 1 1 16 GLU 4 A . 16 GLU n 1 7260 4 1 1 1 17 GLY 4 A . 17 GLY o 1 7260 4 1 1 1 18 ASN 4 A . 18 ASN p 1 7260 4 1 1 1 19 THR 4 A . 19 THR a 1 7260 4 1 1 1 20 PRO 4 A . 20 PRO a 1 7260 4 1 1 1 21 LEU 4 A . 21 LEU d 1 7260 4 1 1 1 22 SER 4 A . 22 SER f 1 7260 4 1 1 1 23 GLU 4 A . 23 GLU k 1 7260 4 1 1 1 24 ASN 4 A . 24 ASN l 1 7260 4 1 1 1 25 ASP 4 A . 25 ASP n 1 7260 4 1 1 1 26 ILE 4 A . 26 ILE o 1 7260 4 1 1 1 27 GLY 4 A . 27 GLY p 1 7260 4 1 1 1 28 VAL 4 A . 28 VAL a 1 7260 4 1 1 1 29 THR 4 A . 29 THR f 1 7260 4 1 1 1 30 GLU 4 A . 30 GLU k 1 7260 4 1 1 1 31 ASP 4 A . 31 ASP l 1 7260 4 1 1 1 32 GLN 4 A . 32 GLN m 1 7260 4 1 1 1 33 PHE 4 A . 33 PHE m 1 7260 4 1 1 1 34 ASP 4 A . 34 ASP m 1 7260 4 1 1 1 35 ASP 4 A . 35 ASP m 1 7260 4 1 1 1 36 ALA 4 A . 36 ALA m 1 7260 4 1 1 1 37 VAL 4 A . 37 VAL m 1 7260 4 1 1 1 38 ASN 4 A . 38 ASN m 1 7260 4 1 1 1 39 PHE 4 A . 39 PHE m 1 7260 4 1 1 1 40 LEU 4 A . 40 LEU m 1 7260 4 1 1 1 41 LYS 4 A . 41 LYS m 1 7260 4 1 1 1 42 ARG 4 A . 42 ARG n 1 7260 4 1 1 1 43 GLU 4 A . 43 GLU o 1 7260 4 1 1 1 44 GLY 4 A . 44 GLY p 1 7260 4 1 1 1 45 TYR 4 A . 45 TYR a 1 7260 4 1 1 1 46 ILE 4 A . 46 ILE g 1 7260 4 1 1 1 47 ILE 4 A . 47 ILE h 1 7260 4 1 1 1 48 GLY 4 A . 48 GLY i 1 7260 4 1 1 1 49 VAL 4 A . 49 VAL a 1 7260 4 1 1 1 50 HIS 4 A . 50 HIS c 1 7260 4 1 1 1 51 TYR 4 A . 51 TYR e 1 7260 4 1 1 1 52 SER 4 A . 52 SER h 1 7260 4 1 1 1 53 ASP 4 A . 53 ASP i 1 7260 4 1 1 1 54 ASP 4 A . 54 ASP a 1 7260 4 1 1 1 55 ARG 4 A . 55 ARG a 1 7260 4 1 1 1 56 PRO 4 A . 56 PRO c 1 7260 4 1 1 1 57 HIS 4 A . 57 HIS d 1 7260 4 1 1 1 58 LEU 4 A . 58 LEU d 1 7260 4 1 1 1 59 TYR 4 A . 59 TYR f 1 7260 4 1 1 1 60 LYS 4 A . 60 LYS b 1 7260 4 1 1 1 61 LEU 4 A . 61 LEU l 1 7260 4 1 1 1 62 GLY 4 A . 62 GLY p 1 7260 4 1 1 1 63 PRO 4 A . 63 PRO a 1 7260 4 1 1 1 64 GLU 4 A . 64 GLU c 1 7260 4 1 1 1 65 LEU 4 A . 65 LEU d 1 7260 4 1 1 1 66 THR 4 A . 66 THR f 1 7260 4 1 1 1 67 GLU 4 A . 67 GLU k 1 7260 4 1 1 1 68 LYS 4 A . 68 LYS l 1 7260 4 1 1 1 69 GLY 4 A . 69 GLY m 1 7260 4 1 1 1 70 GLU 4 A . 70 GLU m 1 7260 4 1 1 1 71 ASN 4 A . 71 ASN m 1 7260 4 1 1 1 72 TYR 4 A . 72 TYR m 1 7260 4 1 1 1 73 LEU 4 A . 73 LEU m 1 7260 4 1 1 1 74 LYS 4 A . 74 LYS m 1 7260 4 1 1 1 75 GLU 4 A . 75 GLU m 1 7260 4 1 1 1 76 ASN 4 A . 76 ASN m 1 7260 4 1 1 1 77 GLY 4 A . 77 GLY m 1 7260 4 1 1 1 78 THR 4 A . 78 THR p 1 7260 4 1 1 1 79 TRP 4 A . 79 TRP c 1 7260 4 1 1 1 80 SER 4 A . 80 SER c 1 7260 4 1 1 1 81 LYS 4 A . 81 LYS . 1 7260 4 1 1 1 82 ALA 4 A . 82 ALA . 1 7260 4 1 1 1 83 TYR 4 A . 83 TYR . 1 7260 4 1 1 1 84 LYS 4 A . 84 LYS . 1 7260 4 1 1 1 85 THR 4 A . 85 THR . 1 7260 4 1 1 1 86 ILE 4 A . 86 ILE . 1 7260 4 1 1 1 87 LYS 4 A . 87 LYS . 1 7260 4 1 1 1 88 GLU 4 A . 88 GLU . 1 7260 4 1 1 1 89 ILE 4 A . 89 ILE . 1 7260 4 1 1 1 90 LYS 4 A . 90 LYS . 1 7260 4 1 1 1 91 ASP 4 A . 91 ASP . 1 7260 4 1 1 1 92 TRP 4 A . 92 TRP . 1 7260 4 1 1 1 93 ILE 4 A . 93 ILE . 1 7260 4 1 1 1 94 LYS 4 A . 94 LYS . 1 7260 4 1 1 1 95 LEU 4 A . 95 LEU . 1 7260 4 1 1 1 96 GLU 4 A . 96 GLU . 1 7260 4 1 1 1 97 HIS 4 A . 97 HIS . 1 7260 4 1 1 1 98 HIS 4 A . 98 HIS . 1 7260 4 1 1 1 99 HIS 4 A . 99 HIS . 1 7260 4 1 1 1 100 HIS 4 A . 100 HIS . 1 7260 4 1 1 1 101 HIS 4 A . 101 HIS . 1 7260 4 1 1 1 102 HIS 4 A . 102 HIS . 1 7260 4 stop_ save_ save_PB_annotation_5 _PB_list.Sf_category PB_list _PB_list.ID 5 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnomaghiacehlaccddfbhjacdfklmmmmmmmmmgoizz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 5 A . 1 MET . 1 7260 5 1 1 1 2 ASN 5 A . 2 ASN . 1 7260 5 1 1 1 3 LYS 5 A . 3 LYS . 1 7260 5 1 1 1 4 ASP 5 A . 4 ASP . 1 7260 5 1 1 1 5 LYS 5 A . 5 LYS . 1 7260 5 1 1 1 6 LEU 5 A . 6 LEU . 1 7260 5 1 1 1 7 ARG 5 A . 7 ARG m 1 7260 5 1 1 1 8 TYR 5 A . 8 TYR m 1 7260 5 1 1 1 9 ALA 5 A . 9 ALA m 1 7260 5 1 1 1 10 ILE 5 A . 10 ILE m 1 7260 5 1 1 1 11 LEU 5 A . 11 LEU m 1 7260 5 1 1 1 12 LYS 5 A . 12 LYS m 1 7260 5 1 1 1 13 GLU 5 A . 13 GLU m 1 7260 5 1 1 1 14 ILE 5 A . 14 ILE m 1 7260 5 1 1 1 15 PHE 5 A . 15 PHE m 1 7260 5 1 1 1 16 GLU 5 A . 16 GLU n 1 7260 5 1 1 1 17 GLY 5 A . 17 GLY o 1 7260 5 1 1 1 18 ASN 5 A . 18 ASN p 1 7260 5 1 1 1 19 THR 5 A . 19 THR a 1 7260 5 1 1 1 20 PRO 5 A . 20 PRO a 1 7260 5 1 1 1 21 LEU 5 A . 21 LEU d 1 7260 5 1 1 1 22 SER 5 A . 22 SER f 1 7260 5 1 1 1 23 GLU 5 A . 23 GLU k 1 7260 5 1 1 1 24 ASN 5 A . 24 ASN l 1 7260 5 1 1 1 25 ASP 5 A . 25 ASP n 1 7260 5 1 1 1 26 ILE 5 A . 26 ILE o 1 7260 5 1 1 1 27 GLY 5 A . 27 GLY p 1 7260 5 1 1 1 28 VAL 5 A . 28 VAL a 1 7260 5 1 1 1 29 THR 5 A . 29 THR f 1 7260 5 1 1 1 30 GLU 5 A . 30 GLU k 1 7260 5 1 1 1 31 ASP 5 A . 31 ASP l 1 7260 5 1 1 1 32 GLN 5 A . 32 GLN m 1 7260 5 1 1 1 33 PHE 5 A . 33 PHE m 1 7260 5 1 1 1 34 ASP 5 A . 34 ASP m 1 7260 5 1 1 1 35 ASP 5 A . 35 ASP m 1 7260 5 1 1 1 36 ALA 5 A . 36 ALA m 1 7260 5 1 1 1 37 VAL 5 A . 37 VAL m 1 7260 5 1 1 1 38 ASN 5 A . 38 ASN m 1 7260 5 1 1 1 39 PHE 5 A . 39 PHE m 1 7260 5 1 1 1 40 LEU 5 A . 40 LEU m 1 7260 5 1 1 1 41 LYS 5 A . 41 LYS m 1 7260 5 1 1 1 42 ARG 5 A . 42 ARG n 1 7260 5 1 1 1 43 GLU 5 A . 43 GLU o 1 7260 5 1 1 1 44 GLY 5 A . 44 GLY m 1 7260 5 1 1 1 45 TYR 5 A . 45 TYR a 1 7260 5 1 1 1 46 ILE 5 A . 46 ILE g 1 7260 5 1 1 1 47 ILE 5 A . 47 ILE h 1 7260 5 1 1 1 48 GLY 5 A . 48 GLY i 1 7260 5 1 1 1 49 VAL 5 A . 49 VAL a 1 7260 5 1 1 1 50 HIS 5 A . 50 HIS c 1 7260 5 1 1 1 51 TYR 5 A . 51 TYR e 1 7260 5 1 1 1 52 SER 5 A . 52 SER h 1 7260 5 1 1 1 53 ASP 5 A . 53 ASP l 1 7260 5 1 1 1 54 ASP 5 A . 54 ASP a 1 7260 5 1 1 1 55 ARG 5 A . 55 ARG c 1 7260 5 1 1 1 56 PRO 5 A . 56 PRO c 1 7260 5 1 1 1 57 HIS 5 A . 57 HIS d 1 7260 5 1 1 1 58 LEU 5 A . 58 LEU d 1 7260 5 1 1 1 59 TYR 5 A . 59 TYR f 1 7260 5 1 1 1 60 LYS 5 A . 60 LYS b 1 7260 5 1 1 1 61 LEU 5 A . 61 LEU h 1 7260 5 1 1 1 62 GLY 5 A . 62 GLY j 1 7260 5 1 1 1 63 PRO 5 A . 63 PRO a 1 7260 5 1 1 1 64 GLU 5 A . 64 GLU c 1 7260 5 1 1 1 65 LEU 5 A . 65 LEU d 1 7260 5 1 1 1 66 THR 5 A . 66 THR f 1 7260 5 1 1 1 67 GLU 5 A . 67 GLU k 1 7260 5 1 1 1 68 LYS 5 A . 68 LYS l 1 7260 5 1 1 1 69 GLY 5 A . 69 GLY m 1 7260 5 1 1 1 70 GLU 5 A . 70 GLU m 1 7260 5 1 1 1 71 ASN 5 A . 71 ASN m 1 7260 5 1 1 1 72 TYR 5 A . 72 TYR m 1 7260 5 1 1 1 73 LEU 5 A . 73 LEU m 1 7260 5 1 1 1 74 LYS 5 A . 74 LYS m 1 7260 5 1 1 1 75 GLU 5 A . 75 GLU m 1 7260 5 1 1 1 76 ASN 5 A . 76 ASN m 1 7260 5 1 1 1 77 GLY 5 A . 77 GLY m 1 7260 5 1 1 1 78 THR 5 A . 78 THR g 1 7260 5 1 1 1 79 TRP 5 A . 79 TRP o 1 7260 5 1 1 1 80 SER 5 A . 80 SER i 1 7260 5 1 1 1 81 LYS 5 A . 81 LYS . 1 7260 5 1 1 1 82 ALA 5 A . 82 ALA . 1 7260 5 1 1 1 83 TYR 5 A . 83 TYR . 1 7260 5 1 1 1 84 LYS 5 A . 84 LYS . 1 7260 5 1 1 1 85 THR 5 A . 85 THR . 1 7260 5 1 1 1 86 ILE 5 A . 86 ILE . 1 7260 5 1 1 1 87 LYS 5 A . 87 LYS . 1 7260 5 1 1 1 88 GLU 5 A . 88 GLU . 1 7260 5 1 1 1 89 ILE 5 A . 89 ILE . 1 7260 5 1 1 1 90 LYS 5 A . 90 LYS . 1 7260 5 1 1 1 91 ASP 5 A . 91 ASP . 1 7260 5 1 1 1 92 TRP 5 A . 92 TRP . 1 7260 5 1 1 1 93 ILE 5 A . 93 ILE . 1 7260 5 1 1 1 94 LYS 5 A . 94 LYS . 1 7260 5 1 1 1 95 LEU 5 A . 95 LEU . 1 7260 5 1 1 1 96 GLU 5 A . 96 GLU . 1 7260 5 1 1 1 97 HIS 5 A . 97 HIS . 1 7260 5 1 1 1 98 HIS 5 A . 98 HIS . 1 7260 5 1 1 1 99 HIS 5 A . 99 HIS . 1 7260 5 1 1 1 100 HIS 5 A . 100 HIS . 1 7260 5 1 1 1 101 HIS 5 A . 101 HIS . 1 7260 5 1 1 1 102 HIS 5 A . 102 HIS . 1 7260 5 stop_ save_ save_PB_annotation_6 _PB_list.Sf_category PB_list _PB_list.ID 6 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacehjaccddfbopacdfklmmmmmmmmnnopzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 6 A . 1 MET . 1 7260 6 1 1 1 2 ASN 6 A . 2 ASN . 1 7260 6 1 1 1 3 LYS 6 A . 3 LYS . 1 7260 6 1 1 1 4 ASP 6 A . 4 ASP . 1 7260 6 1 1 1 5 LYS 6 A . 5 LYS . 1 7260 6 1 1 1 6 LEU 6 A . 6 LEU . 1 7260 6 1 1 1 7 ARG 6 A . 7 ARG m 1 7260 6 1 1 1 8 TYR 6 A . 8 TYR m 1 7260 6 1 1 1 9 ALA 6 A . 9 ALA m 1 7260 6 1 1 1 10 ILE 6 A . 10 ILE m 1 7260 6 1 1 1 11 LEU 6 A . 11 LEU m 1 7260 6 1 1 1 12 LYS 6 A . 12 LYS m 1 7260 6 1 1 1 13 GLU 6 A . 13 GLU m 1 7260 6 1 1 1 14 ILE 6 A . 14 ILE m 1 7260 6 1 1 1 15 PHE 6 A . 15 PHE m 1 7260 6 1 1 1 16 GLU 6 A . 16 GLU n 1 7260 6 1 1 1 17 GLY 6 A . 17 GLY o 1 7260 6 1 1 1 18 ASN 6 A . 18 ASN p 1 7260 6 1 1 1 19 THR 6 A . 19 THR a 1 7260 6 1 1 1 20 PRO 6 A . 20 PRO a 1 7260 6 1 1 1 21 LEU 6 A . 21 LEU d 1 7260 6 1 1 1 22 SER 6 A . 22 SER f 1 7260 6 1 1 1 23 GLU 6 A . 23 GLU k 1 7260 6 1 1 1 24 ASN 6 A . 24 ASN l 1 7260 6 1 1 1 25 ASP 6 A . 25 ASP n 1 7260 6 1 1 1 26 ILE 6 A . 26 ILE o 1 7260 6 1 1 1 27 GLY 6 A . 27 GLY p 1 7260 6 1 1 1 28 VAL 6 A . 28 VAL a 1 7260 6 1 1 1 29 THR 6 A . 29 THR f 1 7260 6 1 1 1 30 GLU 6 A . 30 GLU k 1 7260 6 1 1 1 31 ASP 6 A . 31 ASP l 1 7260 6 1 1 1 32 GLN 6 A . 32 GLN m 1 7260 6 1 1 1 33 PHE 6 A . 33 PHE m 1 7260 6 1 1 1 34 ASP 6 A . 34 ASP m 1 7260 6 1 1 1 35 ASP 6 A . 35 ASP m 1 7260 6 1 1 1 36 ALA 6 A . 36 ALA m 1 7260 6 1 1 1 37 VAL 6 A . 37 VAL m 1 7260 6 1 1 1 38 ASN 6 A . 38 ASN m 1 7260 6 1 1 1 39 PHE 6 A . 39 PHE m 1 7260 6 1 1 1 40 LEU 6 A . 40 LEU m 1 7260 6 1 1 1 41 LYS 6 A . 41 LYS m 1 7260 6 1 1 1 42 ARG 6 A . 42 ARG n 1 7260 6 1 1 1 43 GLU 6 A . 43 GLU o 1 7260 6 1 1 1 44 GLY 6 A . 44 GLY p 1 7260 6 1 1 1 45 TYR 6 A . 45 TYR a 1 7260 6 1 1 1 46 ILE 6 A . 46 ILE g 1 7260 6 1 1 1 47 ILE 6 A . 47 ILE h 1 7260 6 1 1 1 48 GLY 6 A . 48 GLY i 1 7260 6 1 1 1 49 VAL 6 A . 49 VAL a 1 7260 6 1 1 1 50 HIS 6 A . 50 HIS c 1 7260 6 1 1 1 51 TYR 6 A . 51 TYR e 1 7260 6 1 1 1 52 SER 6 A . 52 SER h 1 7260 6 1 1 1 53 ASP 6 A . 53 ASP j 1 7260 6 1 1 1 54 ASP 6 A . 54 ASP a 1 7260 6 1 1 1 55 ARG 6 A . 55 ARG c 1 7260 6 1 1 1 56 PRO 6 A . 56 PRO c 1 7260 6 1 1 1 57 HIS 6 A . 57 HIS d 1 7260 6 1 1 1 58 LEU 6 A . 58 LEU d 1 7260 6 1 1 1 59 TYR 6 A . 59 TYR f 1 7260 6 1 1 1 60 LYS 6 A . 60 LYS b 1 7260 6 1 1 1 61 LEU 6 A . 61 LEU o 1 7260 6 1 1 1 62 GLY 6 A . 62 GLY p 1 7260 6 1 1 1 63 PRO 6 A . 63 PRO a 1 7260 6 1 1 1 64 GLU 6 A . 64 GLU c 1 7260 6 1 1 1 65 LEU 6 A . 65 LEU d 1 7260 6 1 1 1 66 THR 6 A . 66 THR f 1 7260 6 1 1 1 67 GLU 6 A . 67 GLU k 1 7260 6 1 1 1 68 LYS 6 A . 68 LYS l 1 7260 6 1 1 1 69 GLY 6 A . 69 GLY m 1 7260 6 1 1 1 70 GLU 6 A . 70 GLU m 1 7260 6 1 1 1 71 ASN 6 A . 71 ASN m 1 7260 6 1 1 1 72 TYR 6 A . 72 TYR m 1 7260 6 1 1 1 73 LEU 6 A . 73 LEU m 1 7260 6 1 1 1 74 LYS 6 A . 74 LYS m 1 7260 6 1 1 1 75 GLU 6 A . 75 GLU m 1 7260 6 1 1 1 76 ASN 6 A . 76 ASN m 1 7260 6 1 1 1 77 GLY 6 A . 77 GLY n 1 7260 6 1 1 1 78 THR 6 A . 78 THR n 1 7260 6 1 1 1 79 TRP 6 A . 79 TRP o 1 7260 6 1 1 1 80 SER 6 A . 80 SER p 1 7260 6 1 1 1 81 LYS 6 A . 81 LYS . 1 7260 6 1 1 1 82 ALA 6 A . 82 ALA . 1 7260 6 1 1 1 83 TYR 6 A . 83 TYR . 1 7260 6 1 1 1 84 LYS 6 A . 84 LYS . 1 7260 6 1 1 1 85 THR 6 A . 85 THR . 1 7260 6 1 1 1 86 ILE 6 A . 86 ILE . 1 7260 6 1 1 1 87 LYS 6 A . 87 LYS . 1 7260 6 1 1 1 88 GLU 6 A . 88 GLU . 1 7260 6 1 1 1 89 ILE 6 A . 89 ILE . 1 7260 6 1 1 1 90 LYS 6 A . 90 LYS . 1 7260 6 1 1 1 91 ASP 6 A . 91 ASP . 1 7260 6 1 1 1 92 TRP 6 A . 92 TRP . 1 7260 6 1 1 1 93 ILE 6 A . 93 ILE . 1 7260 6 1 1 1 94 LYS 6 A . 94 LYS . 1 7260 6 1 1 1 95 LEU 6 A . 95 LEU . 1 7260 6 1 1 1 96 GLU 6 A . 96 GLU . 1 7260 6 1 1 1 97 HIS 6 A . 97 HIS . 1 7260 6 1 1 1 98 HIS 6 A . 98 HIS . 1 7260 6 1 1 1 99 HIS 6 A . 99 HIS . 1 7260 6 1 1 1 100 HIS 6 A . 100 HIS . 1 7260 6 1 1 1 101 HIS 6 A . 101 HIS . 1 7260 6 1 1 1 102 HIS 6 A . 102 HIS . 1 7260 6 stop_ save_ save_PB_annotation_7 _PB_list.Sf_category PB_list _PB_list.ID 7 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacehjacfbiaklcdcdfklmmmmmmmmnopfzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 7 A . 1 MET . 1 7260 7 1 1 1 2 ASN 7 A . 2 ASN . 1 7260 7 1 1 1 3 LYS 7 A . 3 LYS . 1 7260 7 1 1 1 4 ASP 7 A . 4 ASP . 1 7260 7 1 1 1 5 LYS 7 A . 5 LYS . 1 7260 7 1 1 1 6 LEU 7 A . 6 LEU . 1 7260 7 1 1 1 7 ARG 7 A . 7 ARG m 1 7260 7 1 1 1 8 TYR 7 A . 8 TYR m 1 7260 7 1 1 1 9 ALA 7 A . 9 ALA m 1 7260 7 1 1 1 10 ILE 7 A . 10 ILE m 1 7260 7 1 1 1 11 LEU 7 A . 11 LEU m 1 7260 7 1 1 1 12 LYS 7 A . 12 LYS m 1 7260 7 1 1 1 13 GLU 7 A . 13 GLU m 1 7260 7 1 1 1 14 ILE 7 A . 14 ILE m 1 7260 7 1 1 1 15 PHE 7 A . 15 PHE m 1 7260 7 1 1 1 16 GLU 7 A . 16 GLU n 1 7260 7 1 1 1 17 GLY 7 A . 17 GLY o 1 7260 7 1 1 1 18 ASN 7 A . 18 ASN p 1 7260 7 1 1 1 19 THR 7 A . 19 THR a 1 7260 7 1 1 1 20 PRO 7 A . 20 PRO a 1 7260 7 1 1 1 21 LEU 7 A . 21 LEU d 1 7260 7 1 1 1 22 SER 7 A . 22 SER f 1 7260 7 1 1 1 23 GLU 7 A . 23 GLU k 1 7260 7 1 1 1 24 ASN 7 A . 24 ASN l 1 7260 7 1 1 1 25 ASP 7 A . 25 ASP n 1 7260 7 1 1 1 26 ILE 7 A . 26 ILE o 1 7260 7 1 1 1 27 GLY 7 A . 27 GLY p 1 7260 7 1 1 1 28 VAL 7 A . 28 VAL a 1 7260 7 1 1 1 29 THR 7 A . 29 THR f 1 7260 7 1 1 1 30 GLU 7 A . 30 GLU k 1 7260 7 1 1 1 31 ASP 7 A . 31 ASP l 1 7260 7 1 1 1 32 GLN 7 A . 32 GLN m 1 7260 7 1 1 1 33 PHE 7 A . 33 PHE m 1 7260 7 1 1 1 34 ASP 7 A . 34 ASP m 1 7260 7 1 1 1 35 ASP 7 A . 35 ASP m 1 7260 7 1 1 1 36 ALA 7 A . 36 ALA m 1 7260 7 1 1 1 37 VAL 7 A . 37 VAL m 1 7260 7 1 1 1 38 ASN 7 A . 38 ASN m 1 7260 7 1 1 1 39 PHE 7 A . 39 PHE m 1 7260 7 1 1 1 40 LEU 7 A . 40 LEU m 1 7260 7 1 1 1 41 LYS 7 A . 41 LYS m 1 7260 7 1 1 1 42 ARG 7 A . 42 ARG n 1 7260 7 1 1 1 43 GLU 7 A . 43 GLU o 1 7260 7 1 1 1 44 GLY 7 A . 44 GLY p 1 7260 7 1 1 1 45 TYR 7 A . 45 TYR a 1 7260 7 1 1 1 46 ILE 7 A . 46 ILE g 1 7260 7 1 1 1 47 ILE 7 A . 47 ILE h 1 7260 7 1 1 1 48 GLY 7 A . 48 GLY i 1 7260 7 1 1 1 49 VAL 7 A . 49 VAL a 1 7260 7 1 1 1 50 HIS 7 A . 50 HIS c 1 7260 7 1 1 1 51 TYR 7 A . 51 TYR e 1 7260 7 1 1 1 52 SER 7 A . 52 SER h 1 7260 7 1 1 1 53 ASP 7 A . 53 ASP j 1 7260 7 1 1 1 54 ASP 7 A . 54 ASP a 1 7260 7 1 1 1 55 ARG 7 A . 55 ARG c 1 7260 7 1 1 1 56 PRO 7 A . 56 PRO f 1 7260 7 1 1 1 57 HIS 7 A . 57 HIS b 1 7260 7 1 1 1 58 LEU 7 A . 58 LEU i 1 7260 7 1 1 1 59 TYR 7 A . 59 TYR a 1 7260 7 1 1 1 60 LYS 7 A . 60 LYS k 1 7260 7 1 1 1 61 LEU 7 A . 61 LEU l 1 7260 7 1 1 1 62 GLY 7 A . 62 GLY c 1 7260 7 1 1 1 63 PRO 7 A . 63 PRO d 1 7260 7 1 1 1 64 GLU 7 A . 64 GLU c 1 7260 7 1 1 1 65 LEU 7 A . 65 LEU d 1 7260 7 1 1 1 66 THR 7 A . 66 THR f 1 7260 7 1 1 1 67 GLU 7 A . 67 GLU k 1 7260 7 1 1 1 68 LYS 7 A . 68 LYS l 1 7260 7 1 1 1 69 GLY 7 A . 69 GLY m 1 7260 7 1 1 1 70 GLU 7 A . 70 GLU m 1 7260 7 1 1 1 71 ASN 7 A . 71 ASN m 1 7260 7 1 1 1 72 TYR 7 A . 72 TYR m 1 7260 7 1 1 1 73 LEU 7 A . 73 LEU m 1 7260 7 1 1 1 74 LYS 7 A . 74 LYS m 1 7260 7 1 1 1 75 GLU 7 A . 75 GLU m 1 7260 7 1 1 1 76 ASN 7 A . 76 ASN m 1 7260 7 1 1 1 77 GLY 7 A . 77 GLY n 1 7260 7 1 1 1 78 THR 7 A . 78 THR o 1 7260 7 1 1 1 79 TRP 7 A . 79 TRP p 1 7260 7 1 1 1 80 SER 7 A . 80 SER f 1 7260 7 1 1 1 81 LYS 7 A . 81 LYS . 1 7260 7 1 1 1 82 ALA 7 A . 82 ALA . 1 7260 7 1 1 1 83 TYR 7 A . 83 TYR . 1 7260 7 1 1 1 84 LYS 7 A . 84 LYS . 1 7260 7 1 1 1 85 THR 7 A . 85 THR . 1 7260 7 1 1 1 86 ILE 7 A . 86 ILE . 1 7260 7 1 1 1 87 LYS 7 A . 87 LYS . 1 7260 7 1 1 1 88 GLU 7 A . 88 GLU . 1 7260 7 1 1 1 89 ILE 7 A . 89 ILE . 1 7260 7 1 1 1 90 LYS 7 A . 90 LYS . 1 7260 7 1 1 1 91 ASP 7 A . 91 ASP . 1 7260 7 1 1 1 92 TRP 7 A . 92 TRP . 1 7260 7 1 1 1 93 ILE 7 A . 93 ILE . 1 7260 7 1 1 1 94 LYS 7 A . 94 LYS . 1 7260 7 1 1 1 95 LEU 7 A . 95 LEU . 1 7260 7 1 1 1 96 GLU 7 A . 96 GLU . 1 7260 7 1 1 1 97 HIS 7 A . 97 HIS . 1 7260 7 1 1 1 98 HIS 7 A . 98 HIS . 1 7260 7 1 1 1 99 HIS 7 A . 99 HIS . 1 7260 7 1 1 1 100 HIS 7 A . 100 HIS . 1 7260 7 1 1 1 101 HIS 7 A . 101 HIS . 1 7260 7 1 1 1 102 HIS 7 A . 102 HIS . 1 7260 7 stop_ save_ save_PB_annotation_8 _PB_list.Sf_category PB_list _PB_list.ID 8 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpacddfbhpacdfklmmmmmmmmnopazz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 8 A . 1 MET . 1 7260 8 1 1 1 2 ASN 8 A . 2 ASN . 1 7260 8 1 1 1 3 LYS 8 A . 3 LYS . 1 7260 8 1 1 1 4 ASP 8 A . 4 ASP . 1 7260 8 1 1 1 5 LYS 8 A . 5 LYS . 1 7260 8 1 1 1 6 LEU 8 A . 6 LEU . 1 7260 8 1 1 1 7 ARG 8 A . 7 ARG m 1 7260 8 1 1 1 8 TYR 8 A . 8 TYR m 1 7260 8 1 1 1 9 ALA 8 A . 9 ALA m 1 7260 8 1 1 1 10 ILE 8 A . 10 ILE m 1 7260 8 1 1 1 11 LEU 8 A . 11 LEU m 1 7260 8 1 1 1 12 LYS 8 A . 12 LYS m 1 7260 8 1 1 1 13 GLU 8 A . 13 GLU m 1 7260 8 1 1 1 14 ILE 8 A . 14 ILE m 1 7260 8 1 1 1 15 PHE 8 A . 15 PHE m 1 7260 8 1 1 1 16 GLU 8 A . 16 GLU n 1 7260 8 1 1 1 17 GLY 8 A . 17 GLY o 1 7260 8 1 1 1 18 ASN 8 A . 18 ASN p 1 7260 8 1 1 1 19 THR 8 A . 19 THR a 1 7260 8 1 1 1 20 PRO 8 A . 20 PRO a 1 7260 8 1 1 1 21 LEU 8 A . 21 LEU d 1 7260 8 1 1 1 22 SER 8 A . 22 SER f 1 7260 8 1 1 1 23 GLU 8 A . 23 GLU k 1 7260 8 1 1 1 24 ASN 8 A . 24 ASN l 1 7260 8 1 1 1 25 ASP 8 A . 25 ASP n 1 7260 8 1 1 1 26 ILE 8 A . 26 ILE o 1 7260 8 1 1 1 27 GLY 8 A . 27 GLY p 1 7260 8 1 1 1 28 VAL 8 A . 28 VAL a 1 7260 8 1 1 1 29 THR 8 A . 29 THR f 1 7260 8 1 1 1 30 GLU 8 A . 30 GLU k 1 7260 8 1 1 1 31 ASP 8 A . 31 ASP l 1 7260 8 1 1 1 32 GLN 8 A . 32 GLN m 1 7260 8 1 1 1 33 PHE 8 A . 33 PHE m 1 7260 8 1 1 1 34 ASP 8 A . 34 ASP m 1 7260 8 1 1 1 35 ASP 8 A . 35 ASP m 1 7260 8 1 1 1 36 ALA 8 A . 36 ALA m 1 7260 8 1 1 1 37 VAL 8 A . 37 VAL m 1 7260 8 1 1 1 38 ASN 8 A . 38 ASN m 1 7260 8 1 1 1 39 PHE 8 A . 39 PHE m 1 7260 8 1 1 1 40 LEU 8 A . 40 LEU m 1 7260 8 1 1 1 41 LYS 8 A . 41 LYS m 1 7260 8 1 1 1 42 ARG 8 A . 42 ARG n 1 7260 8 1 1 1 43 GLU 8 A . 43 GLU o 1 7260 8 1 1 1 44 GLY 8 A . 44 GLY p 1 7260 8 1 1 1 45 TYR 8 A . 45 TYR a 1 7260 8 1 1 1 46 ILE 8 A . 46 ILE g 1 7260 8 1 1 1 47 ILE 8 A . 47 ILE h 1 7260 8 1 1 1 48 GLY 8 A . 48 GLY i 1 7260 8 1 1 1 49 VAL 8 A . 49 VAL a 1 7260 8 1 1 1 50 HIS 8 A . 50 HIS c 1 7260 8 1 1 1 51 TYR 8 A . 51 TYR f 1 7260 8 1 1 1 52 SER 8 A . 52 SER k 1 7260 8 1 1 1 53 ASP 8 A . 53 ASP l 1 7260 8 1 1 1 54 ASP 8 A . 54 ASP p 1 7260 8 1 1 1 55 ARG 8 A . 55 ARG a 1 7260 8 1 1 1 56 PRO 8 A . 56 PRO c 1 7260 8 1 1 1 57 HIS 8 A . 57 HIS d 1 7260 8 1 1 1 58 LEU 8 A . 58 LEU d 1 7260 8 1 1 1 59 TYR 8 A . 59 TYR f 1 7260 8 1 1 1 60 LYS 8 A . 60 LYS b 1 7260 8 1 1 1 61 LEU 8 A . 61 LEU h 1 7260 8 1 1 1 62 GLY 8 A . 62 GLY p 1 7260 8 1 1 1 63 PRO 8 A . 63 PRO a 1 7260 8 1 1 1 64 GLU 8 A . 64 GLU c 1 7260 8 1 1 1 65 LEU 8 A . 65 LEU d 1 7260 8 1 1 1 66 THR 8 A . 66 THR f 1 7260 8 1 1 1 67 GLU 8 A . 67 GLU k 1 7260 8 1 1 1 68 LYS 8 A . 68 LYS l 1 7260 8 1 1 1 69 GLY 8 A . 69 GLY m 1 7260 8 1 1 1 70 GLU 8 A . 70 GLU m 1 7260 8 1 1 1 71 ASN 8 A . 71 ASN m 1 7260 8 1 1 1 72 TYR 8 A . 72 TYR m 1 7260 8 1 1 1 73 LEU 8 A . 73 LEU m 1 7260 8 1 1 1 74 LYS 8 A . 74 LYS m 1 7260 8 1 1 1 75 GLU 8 A . 75 GLU m 1 7260 8 1 1 1 76 ASN 8 A . 76 ASN m 1 7260 8 1 1 1 77 GLY 8 A . 77 GLY n 1 7260 8 1 1 1 78 THR 8 A . 78 THR o 1 7260 8 1 1 1 79 TRP 8 A . 79 TRP p 1 7260 8 1 1 1 80 SER 8 A . 80 SER a 1 7260 8 1 1 1 81 LYS 8 A . 81 LYS . 1 7260 8 1 1 1 82 ALA 8 A . 82 ALA . 1 7260 8 1 1 1 83 TYR 8 A . 83 TYR . 1 7260 8 1 1 1 84 LYS 8 A . 84 LYS . 1 7260 8 1 1 1 85 THR 8 A . 85 THR . 1 7260 8 1 1 1 86 ILE 8 A . 86 ILE . 1 7260 8 1 1 1 87 LYS 8 A . 87 LYS . 1 7260 8 1 1 1 88 GLU 8 A . 88 GLU . 1 7260 8 1 1 1 89 ILE 8 A . 89 ILE . 1 7260 8 1 1 1 90 LYS 8 A . 90 LYS . 1 7260 8 1 1 1 91 ASP 8 A . 91 ASP . 1 7260 8 1 1 1 92 TRP 8 A . 92 TRP . 1 7260 8 1 1 1 93 ILE 8 A . 93 ILE . 1 7260 8 1 1 1 94 LYS 8 A . 94 LYS . 1 7260 8 1 1 1 95 LEU 8 A . 95 LEU . 1 7260 8 1 1 1 96 GLU 8 A . 96 GLU . 1 7260 8 1 1 1 97 HIS 8 A . 97 HIS . 1 7260 8 1 1 1 98 HIS 8 A . 98 HIS . 1 7260 8 1 1 1 99 HIS 8 A . 99 HIS . 1 7260 8 1 1 1 100 HIS 8 A . 100 HIS . 1 7260 8 1 1 1 101 HIS 8 A . 101 HIS . 1 7260 8 1 1 1 102 HIS 8 A . 102 HIS . 1 7260 8 stop_ save_ save_PB_annotation_9 _PB_list.Sf_category PB_list _PB_list.ID 9 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnomaghiacehlbacddfbhpacdfklmmmmmmmmnonozz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 9 A . 1 MET . 1 7260 9 1 1 1 2 ASN 9 A . 2 ASN . 1 7260 9 1 1 1 3 LYS 9 A . 3 LYS . 1 7260 9 1 1 1 4 ASP 9 A . 4 ASP . 1 7260 9 1 1 1 5 LYS 9 A . 5 LYS . 1 7260 9 1 1 1 6 LEU 9 A . 6 LEU . 1 7260 9 1 1 1 7 ARG 9 A . 7 ARG m 1 7260 9 1 1 1 8 TYR 9 A . 8 TYR m 1 7260 9 1 1 1 9 ALA 9 A . 9 ALA m 1 7260 9 1 1 1 10 ILE 9 A . 10 ILE m 1 7260 9 1 1 1 11 LEU 9 A . 11 LEU m 1 7260 9 1 1 1 12 LYS 9 A . 12 LYS m 1 7260 9 1 1 1 13 GLU 9 A . 13 GLU m 1 7260 9 1 1 1 14 ILE 9 A . 14 ILE m 1 7260 9 1 1 1 15 PHE 9 A . 15 PHE m 1 7260 9 1 1 1 16 GLU 9 A . 16 GLU n 1 7260 9 1 1 1 17 GLY 9 A . 17 GLY o 1 7260 9 1 1 1 18 ASN 9 A . 18 ASN p 1 7260 9 1 1 1 19 THR 9 A . 19 THR a 1 7260 9 1 1 1 20 PRO 9 A . 20 PRO a 1 7260 9 1 1 1 21 LEU 9 A . 21 LEU d 1 7260 9 1 1 1 22 SER 9 A . 22 SER f 1 7260 9 1 1 1 23 GLU 9 A . 23 GLU k 1 7260 9 1 1 1 24 ASN 9 A . 24 ASN l 1 7260 9 1 1 1 25 ASP 9 A . 25 ASP n 1 7260 9 1 1 1 26 ILE 9 A . 26 ILE o 1 7260 9 1 1 1 27 GLY 9 A . 27 GLY p 1 7260 9 1 1 1 28 VAL 9 A . 28 VAL a 1 7260 9 1 1 1 29 THR 9 A . 29 THR f 1 7260 9 1 1 1 30 GLU 9 A . 30 GLU k 1 7260 9 1 1 1 31 ASP 9 A . 31 ASP l 1 7260 9 1 1 1 32 GLN 9 A . 32 GLN m 1 7260 9 1 1 1 33 PHE 9 A . 33 PHE m 1 7260 9 1 1 1 34 ASP 9 A . 34 ASP m 1 7260 9 1 1 1 35 ASP 9 A . 35 ASP m 1 7260 9 1 1 1 36 ALA 9 A . 36 ALA m 1 7260 9 1 1 1 37 VAL 9 A . 37 VAL m 1 7260 9 1 1 1 38 ASN 9 A . 38 ASN m 1 7260 9 1 1 1 39 PHE 9 A . 39 PHE m 1 7260 9 1 1 1 40 LEU 9 A . 40 LEU m 1 7260 9 1 1 1 41 LYS 9 A . 41 LYS m 1 7260 9 1 1 1 42 ARG 9 A . 42 ARG n 1 7260 9 1 1 1 43 GLU 9 A . 43 GLU o 1 7260 9 1 1 1 44 GLY 9 A . 44 GLY m 1 7260 9 1 1 1 45 TYR 9 A . 45 TYR a 1 7260 9 1 1 1 46 ILE 9 A . 46 ILE g 1 7260 9 1 1 1 47 ILE 9 A . 47 ILE h 1 7260 9 1 1 1 48 GLY 9 A . 48 GLY i 1 7260 9 1 1 1 49 VAL 9 A . 49 VAL a 1 7260 9 1 1 1 50 HIS 9 A . 50 HIS c 1 7260 9 1 1 1 51 TYR 9 A . 51 TYR e 1 7260 9 1 1 1 52 SER 9 A . 52 SER h 1 7260 9 1 1 1 53 ASP 9 A . 53 ASP l 1 7260 9 1 1 1 54 ASP 9 A . 54 ASP b 1 7260 9 1 1 1 55 ARG 9 A . 55 ARG a 1 7260 9 1 1 1 56 PRO 9 A . 56 PRO c 1 7260 9 1 1 1 57 HIS 9 A . 57 HIS d 1 7260 9 1 1 1 58 LEU 9 A . 58 LEU d 1 7260 9 1 1 1 59 TYR 9 A . 59 TYR f 1 7260 9 1 1 1 60 LYS 9 A . 60 LYS b 1 7260 9 1 1 1 61 LEU 9 A . 61 LEU h 1 7260 9 1 1 1 62 GLY 9 A . 62 GLY p 1 7260 9 1 1 1 63 PRO 9 A . 63 PRO a 1 7260 9 1 1 1 64 GLU 9 A . 64 GLU c 1 7260 9 1 1 1 65 LEU 9 A . 65 LEU d 1 7260 9 1 1 1 66 THR 9 A . 66 THR f 1 7260 9 1 1 1 67 GLU 9 A . 67 GLU k 1 7260 9 1 1 1 68 LYS 9 A . 68 LYS l 1 7260 9 1 1 1 69 GLY 9 A . 69 GLY m 1 7260 9 1 1 1 70 GLU 9 A . 70 GLU m 1 7260 9 1 1 1 71 ASN 9 A . 71 ASN m 1 7260 9 1 1 1 72 TYR 9 A . 72 TYR m 1 7260 9 1 1 1 73 LEU 9 A . 73 LEU m 1 7260 9 1 1 1 74 LYS 9 A . 74 LYS m 1 7260 9 1 1 1 75 GLU 9 A . 75 GLU m 1 7260 9 1 1 1 76 ASN 9 A . 76 ASN m 1 7260 9 1 1 1 77 GLY 9 A . 77 GLY n 1 7260 9 1 1 1 78 THR 9 A . 78 THR o 1 7260 9 1 1 1 79 TRP 9 A . 79 TRP n 1 7260 9 1 1 1 80 SER 9 A . 80 SER o 1 7260 9 1 1 1 81 LYS 9 A . 81 LYS . 1 7260 9 1 1 1 82 ALA 9 A . 82 ALA . 1 7260 9 1 1 1 83 TYR 9 A . 83 TYR . 1 7260 9 1 1 1 84 LYS 9 A . 84 LYS . 1 7260 9 1 1 1 85 THR 9 A . 85 THR . 1 7260 9 1 1 1 86 ILE 9 A . 86 ILE . 1 7260 9 1 1 1 87 LYS 9 A . 87 LYS . 1 7260 9 1 1 1 88 GLU 9 A . 88 GLU . 1 7260 9 1 1 1 89 ILE 9 A . 89 ILE . 1 7260 9 1 1 1 90 LYS 9 A . 90 LYS . 1 7260 9 1 1 1 91 ASP 9 A . 91 ASP . 1 7260 9 1 1 1 92 TRP 9 A . 92 TRP . 1 7260 9 1 1 1 93 ILE 9 A . 93 ILE . 1 7260 9 1 1 1 94 LYS 9 A . 94 LYS . 1 7260 9 1 1 1 95 LEU 9 A . 95 LEU . 1 7260 9 1 1 1 96 GLU 9 A . 96 GLU . 1 7260 9 1 1 1 97 HIS 9 A . 97 HIS . 1 7260 9 1 1 1 98 HIS 9 A . 98 HIS . 1 7260 9 1 1 1 99 HIS 9 A . 99 HIS . 1 7260 9 1 1 1 100 HIS 9 A . 100 HIS . 1 7260 9 1 1 1 101 HIS 9 A . 101 HIS . 1 7260 9 1 1 1 102 HIS 9 A . 102 HIS . 1 7260 9 stop_ save_ save_PB_annotation_10 _PB_list.Sf_category PB_list _PB_list.ID 10 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpacddfbhjacdfklmmmmmmmmmmnozz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 10 A . 1 MET . 1 7260 10 1 1 1 2 ASN 10 A . 2 ASN . 1 7260 10 1 1 1 3 LYS 10 A . 3 LYS . 1 7260 10 1 1 1 4 ASP 10 A . 4 ASP . 1 7260 10 1 1 1 5 LYS 10 A . 5 LYS . 1 7260 10 1 1 1 6 LEU 10 A . 6 LEU . 1 7260 10 1 1 1 7 ARG 10 A . 7 ARG m 1 7260 10 1 1 1 8 TYR 10 A . 8 TYR m 1 7260 10 1 1 1 9 ALA 10 A . 9 ALA m 1 7260 10 1 1 1 10 ILE 10 A . 10 ILE m 1 7260 10 1 1 1 11 LEU 10 A . 11 LEU m 1 7260 10 1 1 1 12 LYS 10 A . 12 LYS m 1 7260 10 1 1 1 13 GLU 10 A . 13 GLU m 1 7260 10 1 1 1 14 ILE 10 A . 14 ILE m 1 7260 10 1 1 1 15 PHE 10 A . 15 PHE m 1 7260 10 1 1 1 16 GLU 10 A . 16 GLU n 1 7260 10 1 1 1 17 GLY 10 A . 17 GLY o 1 7260 10 1 1 1 18 ASN 10 A . 18 ASN p 1 7260 10 1 1 1 19 THR 10 A . 19 THR a 1 7260 10 1 1 1 20 PRO 10 A . 20 PRO a 1 7260 10 1 1 1 21 LEU 10 A . 21 LEU d 1 7260 10 1 1 1 22 SER 10 A . 22 SER f 1 7260 10 1 1 1 23 GLU 10 A . 23 GLU k 1 7260 10 1 1 1 24 ASN 10 A . 24 ASN l 1 7260 10 1 1 1 25 ASP 10 A . 25 ASP n 1 7260 10 1 1 1 26 ILE 10 A . 26 ILE o 1 7260 10 1 1 1 27 GLY 10 A . 27 GLY p 1 7260 10 1 1 1 28 VAL 10 A . 28 VAL a 1 7260 10 1 1 1 29 THR 10 A . 29 THR f 1 7260 10 1 1 1 30 GLU 10 A . 30 GLU k 1 7260 10 1 1 1 31 ASP 10 A . 31 ASP l 1 7260 10 1 1 1 32 GLN 10 A . 32 GLN m 1 7260 10 1 1 1 33 PHE 10 A . 33 PHE m 1 7260 10 1 1 1 34 ASP 10 A . 34 ASP m 1 7260 10 1 1 1 35 ASP 10 A . 35 ASP m 1 7260 10 1 1 1 36 ALA 10 A . 36 ALA m 1 7260 10 1 1 1 37 VAL 10 A . 37 VAL m 1 7260 10 1 1 1 38 ASN 10 A . 38 ASN m 1 7260 10 1 1 1 39 PHE 10 A . 39 PHE m 1 7260 10 1 1 1 40 LEU 10 A . 40 LEU m 1 7260 10 1 1 1 41 LYS 10 A . 41 LYS m 1 7260 10 1 1 1 42 ARG 10 A . 42 ARG n 1 7260 10 1 1 1 43 GLU 10 A . 43 GLU o 1 7260 10 1 1 1 44 GLY 10 A . 44 GLY p 1 7260 10 1 1 1 45 TYR 10 A . 45 TYR a 1 7260 10 1 1 1 46 ILE 10 A . 46 ILE g 1 7260 10 1 1 1 47 ILE 10 A . 47 ILE h 1 7260 10 1 1 1 48 GLY 10 A . 48 GLY i 1 7260 10 1 1 1 49 VAL 10 A . 49 VAL a 1 7260 10 1 1 1 50 HIS 10 A . 50 HIS c 1 7260 10 1 1 1 51 TYR 10 A . 51 TYR f 1 7260 10 1 1 1 52 SER 10 A . 52 SER k 1 7260 10 1 1 1 53 ASP 10 A . 53 ASP l 1 7260 10 1 1 1 54 ASP 10 A . 54 ASP p 1 7260 10 1 1 1 55 ARG 10 A . 55 ARG a 1 7260 10 1 1 1 56 PRO 10 A . 56 PRO c 1 7260 10 1 1 1 57 HIS 10 A . 57 HIS d 1 7260 10 1 1 1 58 LEU 10 A . 58 LEU d 1 7260 10 1 1 1 59 TYR 10 A . 59 TYR f 1 7260 10 1 1 1 60 LYS 10 A . 60 LYS b 1 7260 10 1 1 1 61 LEU 10 A . 61 LEU h 1 7260 10 1 1 1 62 GLY 10 A . 62 GLY j 1 7260 10 1 1 1 63 PRO 10 A . 63 PRO a 1 7260 10 1 1 1 64 GLU 10 A . 64 GLU c 1 7260 10 1 1 1 65 LEU 10 A . 65 LEU d 1 7260 10 1 1 1 66 THR 10 A . 66 THR f 1 7260 10 1 1 1 67 GLU 10 A . 67 GLU k 1 7260 10 1 1 1 68 LYS 10 A . 68 LYS l 1 7260 10 1 1 1 69 GLY 10 A . 69 GLY m 1 7260 10 1 1 1 70 GLU 10 A . 70 GLU m 1 7260 10 1 1 1 71 ASN 10 A . 71 ASN m 1 7260 10 1 1 1 72 TYR 10 A . 72 TYR m 1 7260 10 1 1 1 73 LEU 10 A . 73 LEU m 1 7260 10 1 1 1 74 LYS 10 A . 74 LYS m 1 7260 10 1 1 1 75 GLU 10 A . 75 GLU m 1 7260 10 1 1 1 76 ASN 10 A . 76 ASN m 1 7260 10 1 1 1 77 GLY 10 A . 77 GLY m 1 7260 10 1 1 1 78 THR 10 A . 78 THR m 1 7260 10 1 1 1 79 TRP 10 A . 79 TRP n 1 7260 10 1 1 1 80 SER 10 A . 80 SER o 1 7260 10 1 1 1 81 LYS 10 A . 81 LYS . 1 7260 10 1 1 1 82 ALA 10 A . 82 ALA . 1 7260 10 1 1 1 83 TYR 10 A . 83 TYR . 1 7260 10 1 1 1 84 LYS 10 A . 84 LYS . 1 7260 10 1 1 1 85 THR 10 A . 85 THR . 1 7260 10 1 1 1 86 ILE 10 A . 86 ILE . 1 7260 10 1 1 1 87 LYS 10 A . 87 LYS . 1 7260 10 1 1 1 88 GLU 10 A . 88 GLU . 1 7260 10 1 1 1 89 ILE 10 A . 89 ILE . 1 7260 10 1 1 1 90 LYS 10 A . 90 LYS . 1 7260 10 1 1 1 91 ASP 10 A . 91 ASP . 1 7260 10 1 1 1 92 TRP 10 A . 92 TRP . 1 7260 10 1 1 1 93 ILE 10 A . 93 ILE . 1 7260 10 1 1 1 94 LYS 10 A . 94 LYS . 1 7260 10 1 1 1 95 LEU 10 A . 95 LEU . 1 7260 10 1 1 1 96 GLU 10 A . 96 GLU . 1 7260 10 1 1 1 97 HIS 10 A . 97 HIS . 1 7260 10 1 1 1 98 HIS 10 A . 98 HIS . 1 7260 10 1 1 1 99 HIS 10 A . 99 HIS . 1 7260 10 1 1 1 100 HIS 10 A . 100 HIS . 1 7260 10 1 1 1 101 HIS 10 A . 101 HIS . 1 7260 10 1 1 1 102 HIS 10 A . 102 HIS . 1 7260 10 stop_ save_ save_PB_annotation_11 _PB_list.Sf_category PB_list _PB_list.ID 11 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfehpacddfbhpacdfklmmmmmmmmpgcjzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 11 A . 1 MET . 1 7260 11 1 1 1 2 ASN 11 A . 2 ASN . 1 7260 11 1 1 1 3 LYS 11 A . 3 LYS . 1 7260 11 1 1 1 4 ASP 11 A . 4 ASP . 1 7260 11 1 1 1 5 LYS 11 A . 5 LYS . 1 7260 11 1 1 1 6 LEU 11 A . 6 LEU . 1 7260 11 1 1 1 7 ARG 11 A . 7 ARG m 1 7260 11 1 1 1 8 TYR 11 A . 8 TYR m 1 7260 11 1 1 1 9 ALA 11 A . 9 ALA m 1 7260 11 1 1 1 10 ILE 11 A . 10 ILE m 1 7260 11 1 1 1 11 LEU 11 A . 11 LEU m 1 7260 11 1 1 1 12 LYS 11 A . 12 LYS m 1 7260 11 1 1 1 13 GLU 11 A . 13 GLU m 1 7260 11 1 1 1 14 ILE 11 A . 14 ILE m 1 7260 11 1 1 1 15 PHE 11 A . 15 PHE m 1 7260 11 1 1 1 16 GLU 11 A . 16 GLU n 1 7260 11 1 1 1 17 GLY 11 A . 17 GLY o 1 7260 11 1 1 1 18 ASN 11 A . 18 ASN p 1 7260 11 1 1 1 19 THR 11 A . 19 THR a 1 7260 11 1 1 1 20 PRO 11 A . 20 PRO a 1 7260 11 1 1 1 21 LEU 11 A . 21 LEU d 1 7260 11 1 1 1 22 SER 11 A . 22 SER f 1 7260 11 1 1 1 23 GLU 11 A . 23 GLU k 1 7260 11 1 1 1 24 ASN 11 A . 24 ASN l 1 7260 11 1 1 1 25 ASP 11 A . 25 ASP n 1 7260 11 1 1 1 26 ILE 11 A . 26 ILE o 1 7260 11 1 1 1 27 GLY 11 A . 27 GLY p 1 7260 11 1 1 1 28 VAL 11 A . 28 VAL a 1 7260 11 1 1 1 29 THR 11 A . 29 THR f 1 7260 11 1 1 1 30 GLU 11 A . 30 GLU k 1 7260 11 1 1 1 31 ASP 11 A . 31 ASP l 1 7260 11 1 1 1 32 GLN 11 A . 32 GLN m 1 7260 11 1 1 1 33 PHE 11 A . 33 PHE m 1 7260 11 1 1 1 34 ASP 11 A . 34 ASP m 1 7260 11 1 1 1 35 ASP 11 A . 35 ASP m 1 7260 11 1 1 1 36 ALA 11 A . 36 ALA m 1 7260 11 1 1 1 37 VAL 11 A . 37 VAL m 1 7260 11 1 1 1 38 ASN 11 A . 38 ASN m 1 7260 11 1 1 1 39 PHE 11 A . 39 PHE m 1 7260 11 1 1 1 40 LEU 11 A . 40 LEU m 1 7260 11 1 1 1 41 LYS 11 A . 41 LYS m 1 7260 11 1 1 1 42 ARG 11 A . 42 ARG n 1 7260 11 1 1 1 43 GLU 11 A . 43 GLU o 1 7260 11 1 1 1 44 GLY 11 A . 44 GLY p 1 7260 11 1 1 1 45 TYR 11 A . 45 TYR a 1 7260 11 1 1 1 46 ILE 11 A . 46 ILE g 1 7260 11 1 1 1 47 ILE 11 A . 47 ILE h 1 7260 11 1 1 1 48 GLY 11 A . 48 GLY i 1 7260 11 1 1 1 49 VAL 11 A . 49 VAL a 1 7260 11 1 1 1 50 HIS 11 A . 50 HIS c 1 7260 11 1 1 1 51 TYR 11 A . 51 TYR f 1 7260 11 1 1 1 52 SER 11 A . 52 SER e 1 7260 11 1 1 1 53 ASP 11 A . 53 ASP h 1 7260 11 1 1 1 54 ASP 11 A . 54 ASP p 1 7260 11 1 1 1 55 ARG 11 A . 55 ARG a 1 7260 11 1 1 1 56 PRO 11 A . 56 PRO c 1 7260 11 1 1 1 57 HIS 11 A . 57 HIS d 1 7260 11 1 1 1 58 LEU 11 A . 58 LEU d 1 7260 11 1 1 1 59 TYR 11 A . 59 TYR f 1 7260 11 1 1 1 60 LYS 11 A . 60 LYS b 1 7260 11 1 1 1 61 LEU 11 A . 61 LEU h 1 7260 11 1 1 1 62 GLY 11 A . 62 GLY p 1 7260 11 1 1 1 63 PRO 11 A . 63 PRO a 1 7260 11 1 1 1 64 GLU 11 A . 64 GLU c 1 7260 11 1 1 1 65 LEU 11 A . 65 LEU d 1 7260 11 1 1 1 66 THR 11 A . 66 THR f 1 7260 11 1 1 1 67 GLU 11 A . 67 GLU k 1 7260 11 1 1 1 68 LYS 11 A . 68 LYS l 1 7260 11 1 1 1 69 GLY 11 A . 69 GLY m 1 7260 11 1 1 1 70 GLU 11 A . 70 GLU m 1 7260 11 1 1 1 71 ASN 11 A . 71 ASN m 1 7260 11 1 1 1 72 TYR 11 A . 72 TYR m 1 7260 11 1 1 1 73 LEU 11 A . 73 LEU m 1 7260 11 1 1 1 74 LYS 11 A . 74 LYS m 1 7260 11 1 1 1 75 GLU 11 A . 75 GLU m 1 7260 11 1 1 1 76 ASN 11 A . 76 ASN m 1 7260 11 1 1 1 77 GLY 11 A . 77 GLY p 1 7260 11 1 1 1 78 THR 11 A . 78 THR g 1 7260 11 1 1 1 79 TRP 11 A . 79 TRP c 1 7260 11 1 1 1 80 SER 11 A . 80 SER j 1 7260 11 1 1 1 81 LYS 11 A . 81 LYS . 1 7260 11 1 1 1 82 ALA 11 A . 82 ALA . 1 7260 11 1 1 1 83 TYR 11 A . 83 TYR . 1 7260 11 1 1 1 84 LYS 11 A . 84 LYS . 1 7260 11 1 1 1 85 THR 11 A . 85 THR . 1 7260 11 1 1 1 86 ILE 11 A . 86 ILE . 1 7260 11 1 1 1 87 LYS 11 A . 87 LYS . 1 7260 11 1 1 1 88 GLU 11 A . 88 GLU . 1 7260 11 1 1 1 89 ILE 11 A . 89 ILE . 1 7260 11 1 1 1 90 LYS 11 A . 90 LYS . 1 7260 11 1 1 1 91 ASP 11 A . 91 ASP . 1 7260 11 1 1 1 92 TRP 11 A . 92 TRP . 1 7260 11 1 1 1 93 ILE 11 A . 93 ILE . 1 7260 11 1 1 1 94 LYS 11 A . 94 LYS . 1 7260 11 1 1 1 95 LEU 11 A . 95 LEU . 1 7260 11 1 1 1 96 GLU 11 A . 96 GLU . 1 7260 11 1 1 1 97 HIS 11 A . 97 HIS . 1 7260 11 1 1 1 98 HIS 11 A . 98 HIS . 1 7260 11 1 1 1 99 HIS 11 A . 99 HIS . 1 7260 11 1 1 1 100 HIS 11 A . 100 HIS . 1 7260 11 1 1 1 101 HIS 11 A . 101 HIS . 1 7260 11 1 1 1 102 HIS 11 A . 102 HIS . 1 7260 11 stop_ save_ save_PB_annotation_12 _PB_list.Sf_category PB_list _PB_list.ID 12 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacehjaccddfblpacdfklmmmmmmmmnnnozz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 12 A . 1 MET . 1 7260 12 1 1 1 2 ASN 12 A . 2 ASN . 1 7260 12 1 1 1 3 LYS 12 A . 3 LYS . 1 7260 12 1 1 1 4 ASP 12 A . 4 ASP . 1 7260 12 1 1 1 5 LYS 12 A . 5 LYS . 1 7260 12 1 1 1 6 LEU 12 A . 6 LEU . 1 7260 12 1 1 1 7 ARG 12 A . 7 ARG m 1 7260 12 1 1 1 8 TYR 12 A . 8 TYR m 1 7260 12 1 1 1 9 ALA 12 A . 9 ALA m 1 7260 12 1 1 1 10 ILE 12 A . 10 ILE m 1 7260 12 1 1 1 11 LEU 12 A . 11 LEU m 1 7260 12 1 1 1 12 LYS 12 A . 12 LYS m 1 7260 12 1 1 1 13 GLU 12 A . 13 GLU m 1 7260 12 1 1 1 14 ILE 12 A . 14 ILE m 1 7260 12 1 1 1 15 PHE 12 A . 15 PHE m 1 7260 12 1 1 1 16 GLU 12 A . 16 GLU n 1 7260 12 1 1 1 17 GLY 12 A . 17 GLY o 1 7260 12 1 1 1 18 ASN 12 A . 18 ASN p 1 7260 12 1 1 1 19 THR 12 A . 19 THR a 1 7260 12 1 1 1 20 PRO 12 A . 20 PRO a 1 7260 12 1 1 1 21 LEU 12 A . 21 LEU d 1 7260 12 1 1 1 22 SER 12 A . 22 SER f 1 7260 12 1 1 1 23 GLU 12 A . 23 GLU k 1 7260 12 1 1 1 24 ASN 12 A . 24 ASN l 1 7260 12 1 1 1 25 ASP 12 A . 25 ASP n 1 7260 12 1 1 1 26 ILE 12 A . 26 ILE o 1 7260 12 1 1 1 27 GLY 12 A . 27 GLY p 1 7260 12 1 1 1 28 VAL 12 A . 28 VAL a 1 7260 12 1 1 1 29 THR 12 A . 29 THR f 1 7260 12 1 1 1 30 GLU 12 A . 30 GLU k 1 7260 12 1 1 1 31 ASP 12 A . 31 ASP l 1 7260 12 1 1 1 32 GLN 12 A . 32 GLN m 1 7260 12 1 1 1 33 PHE 12 A . 33 PHE m 1 7260 12 1 1 1 34 ASP 12 A . 34 ASP m 1 7260 12 1 1 1 35 ASP 12 A . 35 ASP m 1 7260 12 1 1 1 36 ALA 12 A . 36 ALA m 1 7260 12 1 1 1 37 VAL 12 A . 37 VAL m 1 7260 12 1 1 1 38 ASN 12 A . 38 ASN m 1 7260 12 1 1 1 39 PHE 12 A . 39 PHE m 1 7260 12 1 1 1 40 LEU 12 A . 40 LEU m 1 7260 12 1 1 1 41 LYS 12 A . 41 LYS m 1 7260 12 1 1 1 42 ARG 12 A . 42 ARG n 1 7260 12 1 1 1 43 GLU 12 A . 43 GLU o 1 7260 12 1 1 1 44 GLY 12 A . 44 GLY p 1 7260 12 1 1 1 45 TYR 12 A . 45 TYR a 1 7260 12 1 1 1 46 ILE 12 A . 46 ILE g 1 7260 12 1 1 1 47 ILE 12 A . 47 ILE h 1 7260 12 1 1 1 48 GLY 12 A . 48 GLY i 1 7260 12 1 1 1 49 VAL 12 A . 49 VAL a 1 7260 12 1 1 1 50 HIS 12 A . 50 HIS c 1 7260 12 1 1 1 51 TYR 12 A . 51 TYR e 1 7260 12 1 1 1 52 SER 12 A . 52 SER h 1 7260 12 1 1 1 53 ASP 12 A . 53 ASP j 1 7260 12 1 1 1 54 ASP 12 A . 54 ASP a 1 7260 12 1 1 1 55 ARG 12 A . 55 ARG c 1 7260 12 1 1 1 56 PRO 12 A . 56 PRO c 1 7260 12 1 1 1 57 HIS 12 A . 57 HIS d 1 7260 12 1 1 1 58 LEU 12 A . 58 LEU d 1 7260 12 1 1 1 59 TYR 12 A . 59 TYR f 1 7260 12 1 1 1 60 LYS 12 A . 60 LYS b 1 7260 12 1 1 1 61 LEU 12 A . 61 LEU l 1 7260 12 1 1 1 62 GLY 12 A . 62 GLY p 1 7260 12 1 1 1 63 PRO 12 A . 63 PRO a 1 7260 12 1 1 1 64 GLU 12 A . 64 GLU c 1 7260 12 1 1 1 65 LEU 12 A . 65 LEU d 1 7260 12 1 1 1 66 THR 12 A . 66 THR f 1 7260 12 1 1 1 67 GLU 12 A . 67 GLU k 1 7260 12 1 1 1 68 LYS 12 A . 68 LYS l 1 7260 12 1 1 1 69 GLY 12 A . 69 GLY m 1 7260 12 1 1 1 70 GLU 12 A . 70 GLU m 1 7260 12 1 1 1 71 ASN 12 A . 71 ASN m 1 7260 12 1 1 1 72 TYR 12 A . 72 TYR m 1 7260 12 1 1 1 73 LEU 12 A . 73 LEU m 1 7260 12 1 1 1 74 LYS 12 A . 74 LYS m 1 7260 12 1 1 1 75 GLU 12 A . 75 GLU m 1 7260 12 1 1 1 76 ASN 12 A . 76 ASN m 1 7260 12 1 1 1 77 GLY 12 A . 77 GLY n 1 7260 12 1 1 1 78 THR 12 A . 78 THR n 1 7260 12 1 1 1 79 TRP 12 A . 79 TRP n 1 7260 12 1 1 1 80 SER 12 A . 80 SER o 1 7260 12 1 1 1 81 LYS 12 A . 81 LYS . 1 7260 12 1 1 1 82 ALA 12 A . 82 ALA . 1 7260 12 1 1 1 83 TYR 12 A . 83 TYR . 1 7260 12 1 1 1 84 LYS 12 A . 84 LYS . 1 7260 12 1 1 1 85 THR 12 A . 85 THR . 1 7260 12 1 1 1 86 ILE 12 A . 86 ILE . 1 7260 12 1 1 1 87 LYS 12 A . 87 LYS . 1 7260 12 1 1 1 88 GLU 12 A . 88 GLU . 1 7260 12 1 1 1 89 ILE 12 A . 89 ILE . 1 7260 12 1 1 1 90 LYS 12 A . 90 LYS . 1 7260 12 1 1 1 91 ASP 12 A . 91 ASP . 1 7260 12 1 1 1 92 TRP 12 A . 92 TRP . 1 7260 12 1 1 1 93 ILE 12 A . 93 ILE . 1 7260 12 1 1 1 94 LYS 12 A . 94 LYS . 1 7260 12 1 1 1 95 LEU 12 A . 95 LEU . 1 7260 12 1 1 1 96 GLU 12 A . 96 GLU . 1 7260 12 1 1 1 97 HIS 12 A . 97 HIS . 1 7260 12 1 1 1 98 HIS 12 A . 98 HIS . 1 7260 12 1 1 1 99 HIS 12 A . 99 HIS . 1 7260 12 1 1 1 100 HIS 12 A . 100 HIS . 1 7260 12 1 1 1 101 HIS 12 A . 101 HIS . 1 7260 12 1 1 1 102 HIS 12 A . 102 HIS . 1 7260 12 stop_ save_ save_PB_annotation_13 _PB_list.Sf_category PB_list _PB_list.ID 13 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacdfklccddfbhiacdfklmmmmmmmmnmmizz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 13 A . 1 MET . 1 7260 13 1 1 1 2 ASN 13 A . 2 ASN . 1 7260 13 1 1 1 3 LYS 13 A . 3 LYS . 1 7260 13 1 1 1 4 ASP 13 A . 4 ASP . 1 7260 13 1 1 1 5 LYS 13 A . 5 LYS . 1 7260 13 1 1 1 6 LEU 13 A . 6 LEU . 1 7260 13 1 1 1 7 ARG 13 A . 7 ARG m 1 7260 13 1 1 1 8 TYR 13 A . 8 TYR m 1 7260 13 1 1 1 9 ALA 13 A . 9 ALA m 1 7260 13 1 1 1 10 ILE 13 A . 10 ILE m 1 7260 13 1 1 1 11 LEU 13 A . 11 LEU m 1 7260 13 1 1 1 12 LYS 13 A . 12 LYS m 1 7260 13 1 1 1 13 GLU 13 A . 13 GLU m 1 7260 13 1 1 1 14 ILE 13 A . 14 ILE m 1 7260 13 1 1 1 15 PHE 13 A . 15 PHE m 1 7260 13 1 1 1 16 GLU 13 A . 16 GLU n 1 7260 13 1 1 1 17 GLY 13 A . 17 GLY o 1 7260 13 1 1 1 18 ASN 13 A . 18 ASN p 1 7260 13 1 1 1 19 THR 13 A . 19 THR a 1 7260 13 1 1 1 20 PRO 13 A . 20 PRO a 1 7260 13 1 1 1 21 LEU 13 A . 21 LEU d 1 7260 13 1 1 1 22 SER 13 A . 22 SER f 1 7260 13 1 1 1 23 GLU 13 A . 23 GLU k 1 7260 13 1 1 1 24 ASN 13 A . 24 ASN l 1 7260 13 1 1 1 25 ASP 13 A . 25 ASP n 1 7260 13 1 1 1 26 ILE 13 A . 26 ILE o 1 7260 13 1 1 1 27 GLY 13 A . 27 GLY p 1 7260 13 1 1 1 28 VAL 13 A . 28 VAL a 1 7260 13 1 1 1 29 THR 13 A . 29 THR f 1 7260 13 1 1 1 30 GLU 13 A . 30 GLU k 1 7260 13 1 1 1 31 ASP 13 A . 31 ASP l 1 7260 13 1 1 1 32 GLN 13 A . 32 GLN m 1 7260 13 1 1 1 33 PHE 13 A . 33 PHE m 1 7260 13 1 1 1 34 ASP 13 A . 34 ASP m 1 7260 13 1 1 1 35 ASP 13 A . 35 ASP m 1 7260 13 1 1 1 36 ALA 13 A . 36 ALA m 1 7260 13 1 1 1 37 VAL 13 A . 37 VAL m 1 7260 13 1 1 1 38 ASN 13 A . 38 ASN m 1 7260 13 1 1 1 39 PHE 13 A . 39 PHE m 1 7260 13 1 1 1 40 LEU 13 A . 40 LEU m 1 7260 13 1 1 1 41 LYS 13 A . 41 LYS m 1 7260 13 1 1 1 42 ARG 13 A . 42 ARG n 1 7260 13 1 1 1 43 GLU 13 A . 43 GLU o 1 7260 13 1 1 1 44 GLY 13 A . 44 GLY p 1 7260 13 1 1 1 45 TYR 13 A . 45 TYR a 1 7260 13 1 1 1 46 ILE 13 A . 46 ILE g 1 7260 13 1 1 1 47 ILE 13 A . 47 ILE h 1 7260 13 1 1 1 48 GLY 13 A . 48 GLY i 1 7260 13 1 1 1 49 VAL 13 A . 49 VAL a 1 7260 13 1 1 1 50 HIS 13 A . 50 HIS c 1 7260 13 1 1 1 51 TYR 13 A . 51 TYR d 1 7260 13 1 1 1 52 SER 13 A . 52 SER f 1 7260 13 1 1 1 53 ASP 13 A . 53 ASP k 1 7260 13 1 1 1 54 ASP 13 A . 54 ASP l 1 7260 13 1 1 1 55 ARG 13 A . 55 ARG c 1 7260 13 1 1 1 56 PRO 13 A . 56 PRO c 1 7260 13 1 1 1 57 HIS 13 A . 57 HIS d 1 7260 13 1 1 1 58 LEU 13 A . 58 LEU d 1 7260 13 1 1 1 59 TYR 13 A . 59 TYR f 1 7260 13 1 1 1 60 LYS 13 A . 60 LYS b 1 7260 13 1 1 1 61 LEU 13 A . 61 LEU h 1 7260 13 1 1 1 62 GLY 13 A . 62 GLY i 1 7260 13 1 1 1 63 PRO 13 A . 63 PRO a 1 7260 13 1 1 1 64 GLU 13 A . 64 GLU c 1 7260 13 1 1 1 65 LEU 13 A . 65 LEU d 1 7260 13 1 1 1 66 THR 13 A . 66 THR f 1 7260 13 1 1 1 67 GLU 13 A . 67 GLU k 1 7260 13 1 1 1 68 LYS 13 A . 68 LYS l 1 7260 13 1 1 1 69 GLY 13 A . 69 GLY m 1 7260 13 1 1 1 70 GLU 13 A . 70 GLU m 1 7260 13 1 1 1 71 ASN 13 A . 71 ASN m 1 7260 13 1 1 1 72 TYR 13 A . 72 TYR m 1 7260 13 1 1 1 73 LEU 13 A . 73 LEU m 1 7260 13 1 1 1 74 LYS 13 A . 74 LYS m 1 7260 13 1 1 1 75 GLU 13 A . 75 GLU m 1 7260 13 1 1 1 76 ASN 13 A . 76 ASN m 1 7260 13 1 1 1 77 GLY 13 A . 77 GLY n 1 7260 13 1 1 1 78 THR 13 A . 78 THR m 1 7260 13 1 1 1 79 TRP 13 A . 79 TRP m 1 7260 13 1 1 1 80 SER 13 A . 80 SER i 1 7260 13 1 1 1 81 LYS 13 A . 81 LYS . 1 7260 13 1 1 1 82 ALA 13 A . 82 ALA . 1 7260 13 1 1 1 83 TYR 13 A . 83 TYR . 1 7260 13 1 1 1 84 LYS 13 A . 84 LYS . 1 7260 13 1 1 1 85 THR 13 A . 85 THR . 1 7260 13 1 1 1 86 ILE 13 A . 86 ILE . 1 7260 13 1 1 1 87 LYS 13 A . 87 LYS . 1 7260 13 1 1 1 88 GLU 13 A . 88 GLU . 1 7260 13 1 1 1 89 ILE 13 A . 89 ILE . 1 7260 13 1 1 1 90 LYS 13 A . 90 LYS . 1 7260 13 1 1 1 91 ASP 13 A . 91 ASP . 1 7260 13 1 1 1 92 TRP 13 A . 92 TRP . 1 7260 13 1 1 1 93 ILE 13 A . 93 ILE . 1 7260 13 1 1 1 94 LYS 13 A . 94 LYS . 1 7260 13 1 1 1 95 LEU 13 A . 95 LEU . 1 7260 13 1 1 1 96 GLU 13 A . 96 GLU . 1 7260 13 1 1 1 97 HIS 13 A . 97 HIS . 1 7260 13 1 1 1 98 HIS 13 A . 98 HIS . 1 7260 13 1 1 1 99 HIS 13 A . 99 HIS . 1 7260 13 1 1 1 100 HIS 13 A . 100 HIS . 1 7260 13 1 1 1 101 HIS 13 A . 101 HIS . 1 7260 13 1 1 1 102 HIS 13 A . 102 HIS . 1 7260 13 stop_ save_ save_PB_annotation_14 _PB_list.Sf_category PB_list _PB_list.ID 14 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfbdcdcddfbhpacdfklmmmmmmmmmgopzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 14 A . 1 MET . 1 7260 14 1 1 1 2 ASN 14 A . 2 ASN . 1 7260 14 1 1 1 3 LYS 14 A . 3 LYS . 1 7260 14 1 1 1 4 ASP 14 A . 4 ASP . 1 7260 14 1 1 1 5 LYS 14 A . 5 LYS . 1 7260 14 1 1 1 6 LEU 14 A . 6 LEU . 1 7260 14 1 1 1 7 ARG 14 A . 7 ARG m 1 7260 14 1 1 1 8 TYR 14 A . 8 TYR m 1 7260 14 1 1 1 9 ALA 14 A . 9 ALA m 1 7260 14 1 1 1 10 ILE 14 A . 10 ILE m 1 7260 14 1 1 1 11 LEU 14 A . 11 LEU m 1 7260 14 1 1 1 12 LYS 14 A . 12 LYS m 1 7260 14 1 1 1 13 GLU 14 A . 13 GLU m 1 7260 14 1 1 1 14 ILE 14 A . 14 ILE m 1 7260 14 1 1 1 15 PHE 14 A . 15 PHE m 1 7260 14 1 1 1 16 GLU 14 A . 16 GLU n 1 7260 14 1 1 1 17 GLY 14 A . 17 GLY o 1 7260 14 1 1 1 18 ASN 14 A . 18 ASN p 1 7260 14 1 1 1 19 THR 14 A . 19 THR a 1 7260 14 1 1 1 20 PRO 14 A . 20 PRO a 1 7260 14 1 1 1 21 LEU 14 A . 21 LEU d 1 7260 14 1 1 1 22 SER 14 A . 22 SER f 1 7260 14 1 1 1 23 GLU 14 A . 23 GLU k 1 7260 14 1 1 1 24 ASN 14 A . 24 ASN l 1 7260 14 1 1 1 25 ASP 14 A . 25 ASP n 1 7260 14 1 1 1 26 ILE 14 A . 26 ILE o 1 7260 14 1 1 1 27 GLY 14 A . 27 GLY p 1 7260 14 1 1 1 28 VAL 14 A . 28 VAL a 1 7260 14 1 1 1 29 THR 14 A . 29 THR f 1 7260 14 1 1 1 30 GLU 14 A . 30 GLU k 1 7260 14 1 1 1 31 ASP 14 A . 31 ASP l 1 7260 14 1 1 1 32 GLN 14 A . 32 GLN m 1 7260 14 1 1 1 33 PHE 14 A . 33 PHE m 1 7260 14 1 1 1 34 ASP 14 A . 34 ASP m 1 7260 14 1 1 1 35 ASP 14 A . 35 ASP m 1 7260 14 1 1 1 36 ALA 14 A . 36 ALA m 1 7260 14 1 1 1 37 VAL 14 A . 37 VAL m 1 7260 14 1 1 1 38 ASN 14 A . 38 ASN m 1 7260 14 1 1 1 39 PHE 14 A . 39 PHE m 1 7260 14 1 1 1 40 LEU 14 A . 40 LEU m 1 7260 14 1 1 1 41 LYS 14 A . 41 LYS m 1 7260 14 1 1 1 42 ARG 14 A . 42 ARG n 1 7260 14 1 1 1 43 GLU 14 A . 43 GLU o 1 7260 14 1 1 1 44 GLY 14 A . 44 GLY p 1 7260 14 1 1 1 45 TYR 14 A . 45 TYR a 1 7260 14 1 1 1 46 ILE 14 A . 46 ILE g 1 7260 14 1 1 1 47 ILE 14 A . 47 ILE h 1 7260 14 1 1 1 48 GLY 14 A . 48 GLY i 1 7260 14 1 1 1 49 VAL 14 A . 49 VAL a 1 7260 14 1 1 1 50 HIS 14 A . 50 HIS c 1 7260 14 1 1 1 51 TYR 14 A . 51 TYR f 1 7260 14 1 1 1 52 SER 14 A . 52 SER b 1 7260 14 1 1 1 53 ASP 14 A . 53 ASP d 1 7260 14 1 1 1 54 ASP 14 A . 54 ASP c 1 7260 14 1 1 1 55 ARG 14 A . 55 ARG d 1 7260 14 1 1 1 56 PRO 14 A . 56 PRO c 1 7260 14 1 1 1 57 HIS 14 A . 57 HIS d 1 7260 14 1 1 1 58 LEU 14 A . 58 LEU d 1 7260 14 1 1 1 59 TYR 14 A . 59 TYR f 1 7260 14 1 1 1 60 LYS 14 A . 60 LYS b 1 7260 14 1 1 1 61 LEU 14 A . 61 LEU h 1 7260 14 1 1 1 62 GLY 14 A . 62 GLY p 1 7260 14 1 1 1 63 PRO 14 A . 63 PRO a 1 7260 14 1 1 1 64 GLU 14 A . 64 GLU c 1 7260 14 1 1 1 65 LEU 14 A . 65 LEU d 1 7260 14 1 1 1 66 THR 14 A . 66 THR f 1 7260 14 1 1 1 67 GLU 14 A . 67 GLU k 1 7260 14 1 1 1 68 LYS 14 A . 68 LYS l 1 7260 14 1 1 1 69 GLY 14 A . 69 GLY m 1 7260 14 1 1 1 70 GLU 14 A . 70 GLU m 1 7260 14 1 1 1 71 ASN 14 A . 71 ASN m 1 7260 14 1 1 1 72 TYR 14 A . 72 TYR m 1 7260 14 1 1 1 73 LEU 14 A . 73 LEU m 1 7260 14 1 1 1 74 LYS 14 A . 74 LYS m 1 7260 14 1 1 1 75 GLU 14 A . 75 GLU m 1 7260 14 1 1 1 76 ASN 14 A . 76 ASN m 1 7260 14 1 1 1 77 GLY 14 A . 77 GLY m 1 7260 14 1 1 1 78 THR 14 A . 78 THR g 1 7260 14 1 1 1 79 TRP 14 A . 79 TRP o 1 7260 14 1 1 1 80 SER 14 A . 80 SER p 1 7260 14 1 1 1 81 LYS 14 A . 81 LYS . 1 7260 14 1 1 1 82 ALA 14 A . 82 ALA . 1 7260 14 1 1 1 83 TYR 14 A . 83 TYR . 1 7260 14 1 1 1 84 LYS 14 A . 84 LYS . 1 7260 14 1 1 1 85 THR 14 A . 85 THR . 1 7260 14 1 1 1 86 ILE 14 A . 86 ILE . 1 7260 14 1 1 1 87 LYS 14 A . 87 LYS . 1 7260 14 1 1 1 88 GLU 14 A . 88 GLU . 1 7260 14 1 1 1 89 ILE 14 A . 89 ILE . 1 7260 14 1 1 1 90 LYS 14 A . 90 LYS . 1 7260 14 1 1 1 91 ASP 14 A . 91 ASP . 1 7260 14 1 1 1 92 TRP 14 A . 92 TRP . 1 7260 14 1 1 1 93 ILE 14 A . 93 ILE . 1 7260 14 1 1 1 94 LYS 14 A . 94 LYS . 1 7260 14 1 1 1 95 LEU 14 A . 95 LEU . 1 7260 14 1 1 1 96 GLU 14 A . 96 GLU . 1 7260 14 1 1 1 97 HIS 14 A . 97 HIS . 1 7260 14 1 1 1 98 HIS 14 A . 98 HIS . 1 7260 14 1 1 1 99 HIS 14 A . 99 HIS . 1 7260 14 1 1 1 100 HIS 14 A . 100 HIS . 1 7260 14 1 1 1 101 HIS 14 A . 101 HIS . 1 7260 14 1 1 1 102 HIS 14 A . 102 HIS . 1 7260 14 stop_ save_ save_PB_annotation_15 _PB_list.Sf_category PB_list _PB_list.ID 15 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacehjaccddfbopacdfklmmmmmmmmnghizz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 15 A . 1 MET . 1 7260 15 1 1 1 2 ASN 15 A . 2 ASN . 1 7260 15 1 1 1 3 LYS 15 A . 3 LYS . 1 7260 15 1 1 1 4 ASP 15 A . 4 ASP . 1 7260 15 1 1 1 5 LYS 15 A . 5 LYS . 1 7260 15 1 1 1 6 LEU 15 A . 6 LEU . 1 7260 15 1 1 1 7 ARG 15 A . 7 ARG m 1 7260 15 1 1 1 8 TYR 15 A . 8 TYR m 1 7260 15 1 1 1 9 ALA 15 A . 9 ALA m 1 7260 15 1 1 1 10 ILE 15 A . 10 ILE m 1 7260 15 1 1 1 11 LEU 15 A . 11 LEU m 1 7260 15 1 1 1 12 LYS 15 A . 12 LYS m 1 7260 15 1 1 1 13 GLU 15 A . 13 GLU m 1 7260 15 1 1 1 14 ILE 15 A . 14 ILE m 1 7260 15 1 1 1 15 PHE 15 A . 15 PHE m 1 7260 15 1 1 1 16 GLU 15 A . 16 GLU n 1 7260 15 1 1 1 17 GLY 15 A . 17 GLY o 1 7260 15 1 1 1 18 ASN 15 A . 18 ASN p 1 7260 15 1 1 1 19 THR 15 A . 19 THR a 1 7260 15 1 1 1 20 PRO 15 A . 20 PRO a 1 7260 15 1 1 1 21 LEU 15 A . 21 LEU d 1 7260 15 1 1 1 22 SER 15 A . 22 SER f 1 7260 15 1 1 1 23 GLU 15 A . 23 GLU k 1 7260 15 1 1 1 24 ASN 15 A . 24 ASN l 1 7260 15 1 1 1 25 ASP 15 A . 25 ASP n 1 7260 15 1 1 1 26 ILE 15 A . 26 ILE o 1 7260 15 1 1 1 27 GLY 15 A . 27 GLY p 1 7260 15 1 1 1 28 VAL 15 A . 28 VAL a 1 7260 15 1 1 1 29 THR 15 A . 29 THR f 1 7260 15 1 1 1 30 GLU 15 A . 30 GLU k 1 7260 15 1 1 1 31 ASP 15 A . 31 ASP l 1 7260 15 1 1 1 32 GLN 15 A . 32 GLN m 1 7260 15 1 1 1 33 PHE 15 A . 33 PHE m 1 7260 15 1 1 1 34 ASP 15 A . 34 ASP m 1 7260 15 1 1 1 35 ASP 15 A . 35 ASP m 1 7260 15 1 1 1 36 ALA 15 A . 36 ALA m 1 7260 15 1 1 1 37 VAL 15 A . 37 VAL m 1 7260 15 1 1 1 38 ASN 15 A . 38 ASN m 1 7260 15 1 1 1 39 PHE 15 A . 39 PHE m 1 7260 15 1 1 1 40 LEU 15 A . 40 LEU m 1 7260 15 1 1 1 41 LYS 15 A . 41 LYS m 1 7260 15 1 1 1 42 ARG 15 A . 42 ARG n 1 7260 15 1 1 1 43 GLU 15 A . 43 GLU o 1 7260 15 1 1 1 44 GLY 15 A . 44 GLY p 1 7260 15 1 1 1 45 TYR 15 A . 45 TYR a 1 7260 15 1 1 1 46 ILE 15 A . 46 ILE g 1 7260 15 1 1 1 47 ILE 15 A . 47 ILE h 1 7260 15 1 1 1 48 GLY 15 A . 48 GLY i 1 7260 15 1 1 1 49 VAL 15 A . 49 VAL a 1 7260 15 1 1 1 50 HIS 15 A . 50 HIS c 1 7260 15 1 1 1 51 TYR 15 A . 51 TYR e 1 7260 15 1 1 1 52 SER 15 A . 52 SER h 1 7260 15 1 1 1 53 ASP 15 A . 53 ASP j 1 7260 15 1 1 1 54 ASP 15 A . 54 ASP a 1 7260 15 1 1 1 55 ARG 15 A . 55 ARG c 1 7260 15 1 1 1 56 PRO 15 A . 56 PRO c 1 7260 15 1 1 1 57 HIS 15 A . 57 HIS d 1 7260 15 1 1 1 58 LEU 15 A . 58 LEU d 1 7260 15 1 1 1 59 TYR 15 A . 59 TYR f 1 7260 15 1 1 1 60 LYS 15 A . 60 LYS b 1 7260 15 1 1 1 61 LEU 15 A . 61 LEU o 1 7260 15 1 1 1 62 GLY 15 A . 62 GLY p 1 7260 15 1 1 1 63 PRO 15 A . 63 PRO a 1 7260 15 1 1 1 64 GLU 15 A . 64 GLU c 1 7260 15 1 1 1 65 LEU 15 A . 65 LEU d 1 7260 15 1 1 1 66 THR 15 A . 66 THR f 1 7260 15 1 1 1 67 GLU 15 A . 67 GLU k 1 7260 15 1 1 1 68 LYS 15 A . 68 LYS l 1 7260 15 1 1 1 69 GLY 15 A . 69 GLY m 1 7260 15 1 1 1 70 GLU 15 A . 70 GLU m 1 7260 15 1 1 1 71 ASN 15 A . 71 ASN m 1 7260 15 1 1 1 72 TYR 15 A . 72 TYR m 1 7260 15 1 1 1 73 LEU 15 A . 73 LEU m 1 7260 15 1 1 1 74 LYS 15 A . 74 LYS m 1 7260 15 1 1 1 75 GLU 15 A . 75 GLU m 1 7260 15 1 1 1 76 ASN 15 A . 76 ASN m 1 7260 15 1 1 1 77 GLY 15 A . 77 GLY n 1 7260 15 1 1 1 78 THR 15 A . 78 THR g 1 7260 15 1 1 1 79 TRP 15 A . 79 TRP h 1 7260 15 1 1 1 80 SER 15 A . 80 SER i 1 7260 15 1 1 1 81 LYS 15 A . 81 LYS . 1 7260 15 1 1 1 82 ALA 15 A . 82 ALA . 1 7260 15 1 1 1 83 TYR 15 A . 83 TYR . 1 7260 15 1 1 1 84 LYS 15 A . 84 LYS . 1 7260 15 1 1 1 85 THR 15 A . 85 THR . 1 7260 15 1 1 1 86 ILE 15 A . 86 ILE . 1 7260 15 1 1 1 87 LYS 15 A . 87 LYS . 1 7260 15 1 1 1 88 GLU 15 A . 88 GLU . 1 7260 15 1 1 1 89 ILE 15 A . 89 ILE . 1 7260 15 1 1 1 90 LYS 15 A . 90 LYS . 1 7260 15 1 1 1 91 ASP 15 A . 91 ASP . 1 7260 15 1 1 1 92 TRP 15 A . 92 TRP . 1 7260 15 1 1 1 93 ILE 15 A . 93 ILE . 1 7260 15 1 1 1 94 LYS 15 A . 94 LYS . 1 7260 15 1 1 1 95 LEU 15 A . 95 LEU . 1 7260 15 1 1 1 96 GLU 15 A . 96 GLU . 1 7260 15 1 1 1 97 HIS 15 A . 97 HIS . 1 7260 15 1 1 1 98 HIS 15 A . 98 HIS . 1 7260 15 1 1 1 99 HIS 15 A . 99 HIS . 1 7260 15 1 1 1 100 HIS 15 A . 100 HIS . 1 7260 15 1 1 1 101 HIS 15 A . 101 HIS . 1 7260 15 1 1 1 102 HIS 15 A . 102 HIS . 1 7260 15 stop_ save_ save_PB_annotation_16 _PB_list.Sf_category PB_list _PB_list.ID 16 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpccddfbhjacdfklmmmmmmmmnopazz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 16 A . 1 MET . 1 7260 16 1 1 1 2 ASN 16 A . 2 ASN . 1 7260 16 1 1 1 3 LYS 16 A . 3 LYS . 1 7260 16 1 1 1 4 ASP 16 A . 4 ASP . 1 7260 16 1 1 1 5 LYS 16 A . 5 LYS . 1 7260 16 1 1 1 6 LEU 16 A . 6 LEU . 1 7260 16 1 1 1 7 ARG 16 A . 7 ARG m 1 7260 16 1 1 1 8 TYR 16 A . 8 TYR m 1 7260 16 1 1 1 9 ALA 16 A . 9 ALA m 1 7260 16 1 1 1 10 ILE 16 A . 10 ILE m 1 7260 16 1 1 1 11 LEU 16 A . 11 LEU m 1 7260 16 1 1 1 12 LYS 16 A . 12 LYS m 1 7260 16 1 1 1 13 GLU 16 A . 13 GLU m 1 7260 16 1 1 1 14 ILE 16 A . 14 ILE m 1 7260 16 1 1 1 15 PHE 16 A . 15 PHE m 1 7260 16 1 1 1 16 GLU 16 A . 16 GLU n 1 7260 16 1 1 1 17 GLY 16 A . 17 GLY o 1 7260 16 1 1 1 18 ASN 16 A . 18 ASN p 1 7260 16 1 1 1 19 THR 16 A . 19 THR a 1 7260 16 1 1 1 20 PRO 16 A . 20 PRO a 1 7260 16 1 1 1 21 LEU 16 A . 21 LEU d 1 7260 16 1 1 1 22 SER 16 A . 22 SER f 1 7260 16 1 1 1 23 GLU 16 A . 23 GLU k 1 7260 16 1 1 1 24 ASN 16 A . 24 ASN l 1 7260 16 1 1 1 25 ASP 16 A . 25 ASP n 1 7260 16 1 1 1 26 ILE 16 A . 26 ILE o 1 7260 16 1 1 1 27 GLY 16 A . 27 GLY p 1 7260 16 1 1 1 28 VAL 16 A . 28 VAL a 1 7260 16 1 1 1 29 THR 16 A . 29 THR f 1 7260 16 1 1 1 30 GLU 16 A . 30 GLU k 1 7260 16 1 1 1 31 ASP 16 A . 31 ASP l 1 7260 16 1 1 1 32 GLN 16 A . 32 GLN m 1 7260 16 1 1 1 33 PHE 16 A . 33 PHE m 1 7260 16 1 1 1 34 ASP 16 A . 34 ASP m 1 7260 16 1 1 1 35 ASP 16 A . 35 ASP m 1 7260 16 1 1 1 36 ALA 16 A . 36 ALA m 1 7260 16 1 1 1 37 VAL 16 A . 37 VAL m 1 7260 16 1 1 1 38 ASN 16 A . 38 ASN m 1 7260 16 1 1 1 39 PHE 16 A . 39 PHE m 1 7260 16 1 1 1 40 LEU 16 A . 40 LEU m 1 7260 16 1 1 1 41 LYS 16 A . 41 LYS m 1 7260 16 1 1 1 42 ARG 16 A . 42 ARG n 1 7260 16 1 1 1 43 GLU 16 A . 43 GLU o 1 7260 16 1 1 1 44 GLY 16 A . 44 GLY p 1 7260 16 1 1 1 45 TYR 16 A . 45 TYR a 1 7260 16 1 1 1 46 ILE 16 A . 46 ILE g 1 7260 16 1 1 1 47 ILE 16 A . 47 ILE h 1 7260 16 1 1 1 48 GLY 16 A . 48 GLY i 1 7260 16 1 1 1 49 VAL 16 A . 49 VAL a 1 7260 16 1 1 1 50 HIS 16 A . 50 HIS c 1 7260 16 1 1 1 51 TYR 16 A . 51 TYR f 1 7260 16 1 1 1 52 SER 16 A . 52 SER k 1 7260 16 1 1 1 53 ASP 16 A . 53 ASP l 1 7260 16 1 1 1 54 ASP 16 A . 54 ASP p 1 7260 16 1 1 1 55 ARG 16 A . 55 ARG c 1 7260 16 1 1 1 56 PRO 16 A . 56 PRO c 1 7260 16 1 1 1 57 HIS 16 A . 57 HIS d 1 7260 16 1 1 1 58 LEU 16 A . 58 LEU d 1 7260 16 1 1 1 59 TYR 16 A . 59 TYR f 1 7260 16 1 1 1 60 LYS 16 A . 60 LYS b 1 7260 16 1 1 1 61 LEU 16 A . 61 LEU h 1 7260 16 1 1 1 62 GLY 16 A . 62 GLY j 1 7260 16 1 1 1 63 PRO 16 A . 63 PRO a 1 7260 16 1 1 1 64 GLU 16 A . 64 GLU c 1 7260 16 1 1 1 65 LEU 16 A . 65 LEU d 1 7260 16 1 1 1 66 THR 16 A . 66 THR f 1 7260 16 1 1 1 67 GLU 16 A . 67 GLU k 1 7260 16 1 1 1 68 LYS 16 A . 68 LYS l 1 7260 16 1 1 1 69 GLY 16 A . 69 GLY m 1 7260 16 1 1 1 70 GLU 16 A . 70 GLU m 1 7260 16 1 1 1 71 ASN 16 A . 71 ASN m 1 7260 16 1 1 1 72 TYR 16 A . 72 TYR m 1 7260 16 1 1 1 73 LEU 16 A . 73 LEU m 1 7260 16 1 1 1 74 LYS 16 A . 74 LYS m 1 7260 16 1 1 1 75 GLU 16 A . 75 GLU m 1 7260 16 1 1 1 76 ASN 16 A . 76 ASN m 1 7260 16 1 1 1 77 GLY 16 A . 77 GLY n 1 7260 16 1 1 1 78 THR 16 A . 78 THR o 1 7260 16 1 1 1 79 TRP 16 A . 79 TRP p 1 7260 16 1 1 1 80 SER 16 A . 80 SER a 1 7260 16 1 1 1 81 LYS 16 A . 81 LYS . 1 7260 16 1 1 1 82 ALA 16 A . 82 ALA . 1 7260 16 1 1 1 83 TYR 16 A . 83 TYR . 1 7260 16 1 1 1 84 LYS 16 A . 84 LYS . 1 7260 16 1 1 1 85 THR 16 A . 85 THR . 1 7260 16 1 1 1 86 ILE 16 A . 86 ILE . 1 7260 16 1 1 1 87 LYS 16 A . 87 LYS . 1 7260 16 1 1 1 88 GLU 16 A . 88 GLU . 1 7260 16 1 1 1 89 ILE 16 A . 89 ILE . 1 7260 16 1 1 1 90 LYS 16 A . 90 LYS . 1 7260 16 1 1 1 91 ASP 16 A . 91 ASP . 1 7260 16 1 1 1 92 TRP 16 A . 92 TRP . 1 7260 16 1 1 1 93 ILE 16 A . 93 ILE . 1 7260 16 1 1 1 94 LYS 16 A . 94 LYS . 1 7260 16 1 1 1 95 LEU 16 A . 95 LEU . 1 7260 16 1 1 1 96 GLU 16 A . 96 GLU . 1 7260 16 1 1 1 97 HIS 16 A . 97 HIS . 1 7260 16 1 1 1 98 HIS 16 A . 98 HIS . 1 7260 16 1 1 1 99 HIS 16 A . 99 HIS . 1 7260 16 1 1 1 100 HIS 16 A . 100 HIS . 1 7260 16 1 1 1 101 HIS 16 A . 101 HIS . 1 7260 16 1 1 1 102 HIS 16 A . 102 HIS . 1 7260 16 stop_ save_ save_PB_annotation_17 _PB_list.Sf_category PB_list _PB_list.ID 17 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnomaghiacehjacdddfbhpacdfklmmmmmmmmmgcezz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 17 A . 1 MET . 1 7260 17 1 1 1 2 ASN 17 A . 2 ASN . 1 7260 17 1 1 1 3 LYS 17 A . 3 LYS . 1 7260 17 1 1 1 4 ASP 17 A . 4 ASP . 1 7260 17 1 1 1 5 LYS 17 A . 5 LYS . 1 7260 17 1 1 1 6 LEU 17 A . 6 LEU . 1 7260 17 1 1 1 7 ARG 17 A . 7 ARG m 1 7260 17 1 1 1 8 TYR 17 A . 8 TYR m 1 7260 17 1 1 1 9 ALA 17 A . 9 ALA m 1 7260 17 1 1 1 10 ILE 17 A . 10 ILE m 1 7260 17 1 1 1 11 LEU 17 A . 11 LEU m 1 7260 17 1 1 1 12 LYS 17 A . 12 LYS m 1 7260 17 1 1 1 13 GLU 17 A . 13 GLU m 1 7260 17 1 1 1 14 ILE 17 A . 14 ILE m 1 7260 17 1 1 1 15 PHE 17 A . 15 PHE m 1 7260 17 1 1 1 16 GLU 17 A . 16 GLU n 1 7260 17 1 1 1 17 GLY 17 A . 17 GLY o 1 7260 17 1 1 1 18 ASN 17 A . 18 ASN p 1 7260 17 1 1 1 19 THR 17 A . 19 THR a 1 7260 17 1 1 1 20 PRO 17 A . 20 PRO a 1 7260 17 1 1 1 21 LEU 17 A . 21 LEU d 1 7260 17 1 1 1 22 SER 17 A . 22 SER f 1 7260 17 1 1 1 23 GLU 17 A . 23 GLU k 1 7260 17 1 1 1 24 ASN 17 A . 24 ASN l 1 7260 17 1 1 1 25 ASP 17 A . 25 ASP n 1 7260 17 1 1 1 26 ILE 17 A . 26 ILE o 1 7260 17 1 1 1 27 GLY 17 A . 27 GLY p 1 7260 17 1 1 1 28 VAL 17 A . 28 VAL a 1 7260 17 1 1 1 29 THR 17 A . 29 THR f 1 7260 17 1 1 1 30 GLU 17 A . 30 GLU k 1 7260 17 1 1 1 31 ASP 17 A . 31 ASP l 1 7260 17 1 1 1 32 GLN 17 A . 32 GLN m 1 7260 17 1 1 1 33 PHE 17 A . 33 PHE m 1 7260 17 1 1 1 34 ASP 17 A . 34 ASP m 1 7260 17 1 1 1 35 ASP 17 A . 35 ASP m 1 7260 17 1 1 1 36 ALA 17 A . 36 ALA m 1 7260 17 1 1 1 37 VAL 17 A . 37 VAL m 1 7260 17 1 1 1 38 ASN 17 A . 38 ASN m 1 7260 17 1 1 1 39 PHE 17 A . 39 PHE m 1 7260 17 1 1 1 40 LEU 17 A . 40 LEU m 1 7260 17 1 1 1 41 LYS 17 A . 41 LYS m 1 7260 17 1 1 1 42 ARG 17 A . 42 ARG n 1 7260 17 1 1 1 43 GLU 17 A . 43 GLU o 1 7260 17 1 1 1 44 GLY 17 A . 44 GLY m 1 7260 17 1 1 1 45 TYR 17 A . 45 TYR a 1 7260 17 1 1 1 46 ILE 17 A . 46 ILE g 1 7260 17 1 1 1 47 ILE 17 A . 47 ILE h 1 7260 17 1 1 1 48 GLY 17 A . 48 GLY i 1 7260 17 1 1 1 49 VAL 17 A . 49 VAL a 1 7260 17 1 1 1 50 HIS 17 A . 50 HIS c 1 7260 17 1 1 1 51 TYR 17 A . 51 TYR e 1 7260 17 1 1 1 52 SER 17 A . 52 SER h 1 7260 17 1 1 1 53 ASP 17 A . 53 ASP j 1 7260 17 1 1 1 54 ASP 17 A . 54 ASP a 1 7260 17 1 1 1 55 ARG 17 A . 55 ARG c 1 7260 17 1 1 1 56 PRO 17 A . 56 PRO d 1 7260 17 1 1 1 57 HIS 17 A . 57 HIS d 1 7260 17 1 1 1 58 LEU 17 A . 58 LEU d 1 7260 17 1 1 1 59 TYR 17 A . 59 TYR f 1 7260 17 1 1 1 60 LYS 17 A . 60 LYS b 1 7260 17 1 1 1 61 LEU 17 A . 61 LEU h 1 7260 17 1 1 1 62 GLY 17 A . 62 GLY p 1 7260 17 1 1 1 63 PRO 17 A . 63 PRO a 1 7260 17 1 1 1 64 GLU 17 A . 64 GLU c 1 7260 17 1 1 1 65 LEU 17 A . 65 LEU d 1 7260 17 1 1 1 66 THR 17 A . 66 THR f 1 7260 17 1 1 1 67 GLU 17 A . 67 GLU k 1 7260 17 1 1 1 68 LYS 17 A . 68 LYS l 1 7260 17 1 1 1 69 GLY 17 A . 69 GLY m 1 7260 17 1 1 1 70 GLU 17 A . 70 GLU m 1 7260 17 1 1 1 71 ASN 17 A . 71 ASN m 1 7260 17 1 1 1 72 TYR 17 A . 72 TYR m 1 7260 17 1 1 1 73 LEU 17 A . 73 LEU m 1 7260 17 1 1 1 74 LYS 17 A . 74 LYS m 1 7260 17 1 1 1 75 GLU 17 A . 75 GLU m 1 7260 17 1 1 1 76 ASN 17 A . 76 ASN m 1 7260 17 1 1 1 77 GLY 17 A . 77 GLY m 1 7260 17 1 1 1 78 THR 17 A . 78 THR g 1 7260 17 1 1 1 79 TRP 17 A . 79 TRP c 1 7260 17 1 1 1 80 SER 17 A . 80 SER e 1 7260 17 1 1 1 81 LYS 17 A . 81 LYS . 1 7260 17 1 1 1 82 ALA 17 A . 82 ALA . 1 7260 17 1 1 1 83 TYR 17 A . 83 TYR . 1 7260 17 1 1 1 84 LYS 17 A . 84 LYS . 1 7260 17 1 1 1 85 THR 17 A . 85 THR . 1 7260 17 1 1 1 86 ILE 17 A . 86 ILE . 1 7260 17 1 1 1 87 LYS 17 A . 87 LYS . 1 7260 17 1 1 1 88 GLU 17 A . 88 GLU . 1 7260 17 1 1 1 89 ILE 17 A . 89 ILE . 1 7260 17 1 1 1 90 LYS 17 A . 90 LYS . 1 7260 17 1 1 1 91 ASP 17 A . 91 ASP . 1 7260 17 1 1 1 92 TRP 17 A . 92 TRP . 1 7260 17 1 1 1 93 ILE 17 A . 93 ILE . 1 7260 17 1 1 1 94 LYS 17 A . 94 LYS . 1 7260 17 1 1 1 95 LEU 17 A . 95 LEU . 1 7260 17 1 1 1 96 GLU 17 A . 96 GLU . 1 7260 17 1 1 1 97 HIS 17 A . 97 HIS . 1 7260 17 1 1 1 98 HIS 17 A . 98 HIS . 1 7260 17 1 1 1 99 HIS 17 A . 99 HIS . 1 7260 17 1 1 1 100 HIS 17 A . 100 HIS . 1 7260 17 1 1 1 101 HIS 17 A . 101 HIS . 1 7260 17 1 1 1 102 HIS 17 A . 102 HIS . 1 7260 17 stop_ save_ save_PB_annotation_18 _PB_list.Sf_category PB_list _PB_list.ID 18 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopacdfklnopafklmmmmmmmmmmnopaghiacfklpgcddfbhpacdfklmmmmmmmmmpcfzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 18 A . 1 MET . 1 7260 18 1 1 1 2 ASN 18 A . 2 ASN . 1 7260 18 1 1 1 3 LYS 18 A . 3 LYS . 1 7260 18 1 1 1 4 ASP 18 A . 4 ASP . 1 7260 18 1 1 1 5 LYS 18 A . 5 LYS . 1 7260 18 1 1 1 6 LEU 18 A . 6 LEU . 1 7260 18 1 1 1 7 ARG 18 A . 7 ARG m 1 7260 18 1 1 1 8 TYR 18 A . 8 TYR m 1 7260 18 1 1 1 9 ALA 18 A . 9 ALA m 1 7260 18 1 1 1 10 ILE 18 A . 10 ILE m 1 7260 18 1 1 1 11 LEU 18 A . 11 LEU m 1 7260 18 1 1 1 12 LYS 18 A . 12 LYS m 1 7260 18 1 1 1 13 GLU 18 A . 13 GLU m 1 7260 18 1 1 1 14 ILE 18 A . 14 ILE m 1 7260 18 1 1 1 15 PHE 18 A . 15 PHE m 1 7260 18 1 1 1 16 GLU 18 A . 16 GLU n 1 7260 18 1 1 1 17 GLY 18 A . 17 GLY o 1 7260 18 1 1 1 18 ASN 18 A . 18 ASN p 1 7260 18 1 1 1 19 THR 18 A . 19 THR a 1 7260 18 1 1 1 20 PRO 18 A . 20 PRO c 1 7260 18 1 1 1 21 LEU 18 A . 21 LEU d 1 7260 18 1 1 1 22 SER 18 A . 22 SER f 1 7260 18 1 1 1 23 GLU 18 A . 23 GLU k 1 7260 18 1 1 1 24 ASN 18 A . 24 ASN l 1 7260 18 1 1 1 25 ASP 18 A . 25 ASP n 1 7260 18 1 1 1 26 ILE 18 A . 26 ILE o 1 7260 18 1 1 1 27 GLY 18 A . 27 GLY p 1 7260 18 1 1 1 28 VAL 18 A . 28 VAL a 1 7260 18 1 1 1 29 THR 18 A . 29 THR f 1 7260 18 1 1 1 30 GLU 18 A . 30 GLU k 1 7260 18 1 1 1 31 ASP 18 A . 31 ASP l 1 7260 18 1 1 1 32 GLN 18 A . 32 GLN m 1 7260 18 1 1 1 33 PHE 18 A . 33 PHE m 1 7260 18 1 1 1 34 ASP 18 A . 34 ASP m 1 7260 18 1 1 1 35 ASP 18 A . 35 ASP m 1 7260 18 1 1 1 36 ALA 18 A . 36 ALA m 1 7260 18 1 1 1 37 VAL 18 A . 37 VAL m 1 7260 18 1 1 1 38 ASN 18 A . 38 ASN m 1 7260 18 1 1 1 39 PHE 18 A . 39 PHE m 1 7260 18 1 1 1 40 LEU 18 A . 40 LEU m 1 7260 18 1 1 1 41 LYS 18 A . 41 LYS m 1 7260 18 1 1 1 42 ARG 18 A . 42 ARG n 1 7260 18 1 1 1 43 GLU 18 A . 43 GLU o 1 7260 18 1 1 1 44 GLY 18 A . 44 GLY p 1 7260 18 1 1 1 45 TYR 18 A . 45 TYR a 1 7260 18 1 1 1 46 ILE 18 A . 46 ILE g 1 7260 18 1 1 1 47 ILE 18 A . 47 ILE h 1 7260 18 1 1 1 48 GLY 18 A . 48 GLY i 1 7260 18 1 1 1 49 VAL 18 A . 49 VAL a 1 7260 18 1 1 1 50 HIS 18 A . 50 HIS c 1 7260 18 1 1 1 51 TYR 18 A . 51 TYR f 1 7260 18 1 1 1 52 SER 18 A . 52 SER k 1 7260 18 1 1 1 53 ASP 18 A . 53 ASP l 1 7260 18 1 1 1 54 ASP 18 A . 54 ASP p 1 7260 18 1 1 1 55 ARG 18 A . 55 ARG g 1 7260 18 1 1 1 56 PRO 18 A . 56 PRO c 1 7260 18 1 1 1 57 HIS 18 A . 57 HIS d 1 7260 18 1 1 1 58 LEU 18 A . 58 LEU d 1 7260 18 1 1 1 59 TYR 18 A . 59 TYR f 1 7260 18 1 1 1 60 LYS 18 A . 60 LYS b 1 7260 18 1 1 1 61 LEU 18 A . 61 LEU h 1 7260 18 1 1 1 62 GLY 18 A . 62 GLY p 1 7260 18 1 1 1 63 PRO 18 A . 63 PRO a 1 7260 18 1 1 1 64 GLU 18 A . 64 GLU c 1 7260 18 1 1 1 65 LEU 18 A . 65 LEU d 1 7260 18 1 1 1 66 THR 18 A . 66 THR f 1 7260 18 1 1 1 67 GLU 18 A . 67 GLU k 1 7260 18 1 1 1 68 LYS 18 A . 68 LYS l 1 7260 18 1 1 1 69 GLY 18 A . 69 GLY m 1 7260 18 1 1 1 70 GLU 18 A . 70 GLU m 1 7260 18 1 1 1 71 ASN 18 A . 71 ASN m 1 7260 18 1 1 1 72 TYR 18 A . 72 TYR m 1 7260 18 1 1 1 73 LEU 18 A . 73 LEU m 1 7260 18 1 1 1 74 LYS 18 A . 74 LYS m 1 7260 18 1 1 1 75 GLU 18 A . 75 GLU m 1 7260 18 1 1 1 76 ASN 18 A . 76 ASN m 1 7260 18 1 1 1 77 GLY 18 A . 77 GLY m 1 7260 18 1 1 1 78 THR 18 A . 78 THR p 1 7260 18 1 1 1 79 TRP 18 A . 79 TRP c 1 7260 18 1 1 1 80 SER 18 A . 80 SER f 1 7260 18 1 1 1 81 LYS 18 A . 81 LYS . 1 7260 18 1 1 1 82 ALA 18 A . 82 ALA . 1 7260 18 1 1 1 83 TYR 18 A . 83 TYR . 1 7260 18 1 1 1 84 LYS 18 A . 84 LYS . 1 7260 18 1 1 1 85 THR 18 A . 85 THR . 1 7260 18 1 1 1 86 ILE 18 A . 86 ILE . 1 7260 18 1 1 1 87 LYS 18 A . 87 LYS . 1 7260 18 1 1 1 88 GLU 18 A . 88 GLU . 1 7260 18 1 1 1 89 ILE 18 A . 89 ILE . 1 7260 18 1 1 1 90 LYS 18 A . 90 LYS . 1 7260 18 1 1 1 91 ASP 18 A . 91 ASP . 1 7260 18 1 1 1 92 TRP 18 A . 92 TRP . 1 7260 18 1 1 1 93 ILE 18 A . 93 ILE . 1 7260 18 1 1 1 94 LYS 18 A . 94 LYS . 1 7260 18 1 1 1 95 LEU 18 A . 95 LEU . 1 7260 18 1 1 1 96 GLU 18 A . 96 GLU . 1 7260 18 1 1 1 97 HIS 18 A . 97 HIS . 1 7260 18 1 1 1 98 HIS 18 A . 98 HIS . 1 7260 18 1 1 1 99 HIS 18 A . 99 HIS . 1 7260 18 1 1 1 100 HIS 18 A . 100 HIS . 1 7260 18 1 1 1 101 HIS 18 A . 101 HIS . 1 7260 18 1 1 1 102 HIS 18 A . 102 HIS . 1 7260 18 stop_ save_ save_PB_annotation_19 _PB_list.Sf_category PB_list _PB_list.ID 19 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpacddfblcdcdfklmmmmmmmmmgghzz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 19 A . 1 MET . 1 7260 19 1 1 1 2 ASN 19 A . 2 ASN . 1 7260 19 1 1 1 3 LYS 19 A . 3 LYS . 1 7260 19 1 1 1 4 ASP 19 A . 4 ASP . 1 7260 19 1 1 1 5 LYS 19 A . 5 LYS . 1 7260 19 1 1 1 6 LEU 19 A . 6 LEU . 1 7260 19 1 1 1 7 ARG 19 A . 7 ARG m 1 7260 19 1 1 1 8 TYR 19 A . 8 TYR m 1 7260 19 1 1 1 9 ALA 19 A . 9 ALA m 1 7260 19 1 1 1 10 ILE 19 A . 10 ILE m 1 7260 19 1 1 1 11 LEU 19 A . 11 LEU m 1 7260 19 1 1 1 12 LYS 19 A . 12 LYS m 1 7260 19 1 1 1 13 GLU 19 A . 13 GLU m 1 7260 19 1 1 1 14 ILE 19 A . 14 ILE m 1 7260 19 1 1 1 15 PHE 19 A . 15 PHE m 1 7260 19 1 1 1 16 GLU 19 A . 16 GLU n 1 7260 19 1 1 1 17 GLY 19 A . 17 GLY o 1 7260 19 1 1 1 18 ASN 19 A . 18 ASN p 1 7260 19 1 1 1 19 THR 19 A . 19 THR a 1 7260 19 1 1 1 20 PRO 19 A . 20 PRO a 1 7260 19 1 1 1 21 LEU 19 A . 21 LEU d 1 7260 19 1 1 1 22 SER 19 A . 22 SER f 1 7260 19 1 1 1 23 GLU 19 A . 23 GLU k 1 7260 19 1 1 1 24 ASN 19 A . 24 ASN l 1 7260 19 1 1 1 25 ASP 19 A . 25 ASP n 1 7260 19 1 1 1 26 ILE 19 A . 26 ILE o 1 7260 19 1 1 1 27 GLY 19 A . 27 GLY p 1 7260 19 1 1 1 28 VAL 19 A . 28 VAL a 1 7260 19 1 1 1 29 THR 19 A . 29 THR f 1 7260 19 1 1 1 30 GLU 19 A . 30 GLU k 1 7260 19 1 1 1 31 ASP 19 A . 31 ASP l 1 7260 19 1 1 1 32 GLN 19 A . 32 GLN m 1 7260 19 1 1 1 33 PHE 19 A . 33 PHE m 1 7260 19 1 1 1 34 ASP 19 A . 34 ASP m 1 7260 19 1 1 1 35 ASP 19 A . 35 ASP m 1 7260 19 1 1 1 36 ALA 19 A . 36 ALA m 1 7260 19 1 1 1 37 VAL 19 A . 37 VAL m 1 7260 19 1 1 1 38 ASN 19 A . 38 ASN m 1 7260 19 1 1 1 39 PHE 19 A . 39 PHE m 1 7260 19 1 1 1 40 LEU 19 A . 40 LEU m 1 7260 19 1 1 1 41 LYS 19 A . 41 LYS m 1 7260 19 1 1 1 42 ARG 19 A . 42 ARG n 1 7260 19 1 1 1 43 GLU 19 A . 43 GLU o 1 7260 19 1 1 1 44 GLY 19 A . 44 GLY p 1 7260 19 1 1 1 45 TYR 19 A . 45 TYR a 1 7260 19 1 1 1 46 ILE 19 A . 46 ILE g 1 7260 19 1 1 1 47 ILE 19 A . 47 ILE h 1 7260 19 1 1 1 48 GLY 19 A . 48 GLY i 1 7260 19 1 1 1 49 VAL 19 A . 49 VAL a 1 7260 19 1 1 1 50 HIS 19 A . 50 HIS c 1 7260 19 1 1 1 51 TYR 19 A . 51 TYR f 1 7260 19 1 1 1 52 SER 19 A . 52 SER k 1 7260 19 1 1 1 53 ASP 19 A . 53 ASP l 1 7260 19 1 1 1 54 ASP 19 A . 54 ASP p 1 7260 19 1 1 1 55 ARG 19 A . 55 ARG a 1 7260 19 1 1 1 56 PRO 19 A . 56 PRO c 1 7260 19 1 1 1 57 HIS 19 A . 57 HIS d 1 7260 19 1 1 1 58 LEU 19 A . 58 LEU d 1 7260 19 1 1 1 59 TYR 19 A . 59 TYR f 1 7260 19 1 1 1 60 LYS 19 A . 60 LYS b 1 7260 19 1 1 1 61 LEU 19 A . 61 LEU l 1 7260 19 1 1 1 62 GLY 19 A . 62 GLY c 1 7260 19 1 1 1 63 PRO 19 A . 63 PRO d 1 7260 19 1 1 1 64 GLU 19 A . 64 GLU c 1 7260 19 1 1 1 65 LEU 19 A . 65 LEU d 1 7260 19 1 1 1 66 THR 19 A . 66 THR f 1 7260 19 1 1 1 67 GLU 19 A . 67 GLU k 1 7260 19 1 1 1 68 LYS 19 A . 68 LYS l 1 7260 19 1 1 1 69 GLY 19 A . 69 GLY m 1 7260 19 1 1 1 70 GLU 19 A . 70 GLU m 1 7260 19 1 1 1 71 ASN 19 A . 71 ASN m 1 7260 19 1 1 1 72 TYR 19 A . 72 TYR m 1 7260 19 1 1 1 73 LEU 19 A . 73 LEU m 1 7260 19 1 1 1 74 LYS 19 A . 74 LYS m 1 7260 19 1 1 1 75 GLU 19 A . 75 GLU m 1 7260 19 1 1 1 76 ASN 19 A . 76 ASN m 1 7260 19 1 1 1 77 GLY 19 A . 77 GLY m 1 7260 19 1 1 1 78 THR 19 A . 78 THR g 1 7260 19 1 1 1 79 TRP 19 A . 79 TRP g 1 7260 19 1 1 1 80 SER 19 A . 80 SER h 1 7260 19 1 1 1 81 LYS 19 A . 81 LYS . 1 7260 19 1 1 1 82 ALA 19 A . 82 ALA . 1 7260 19 1 1 1 83 TYR 19 A . 83 TYR . 1 7260 19 1 1 1 84 LYS 19 A . 84 LYS . 1 7260 19 1 1 1 85 THR 19 A . 85 THR . 1 7260 19 1 1 1 86 ILE 19 A . 86 ILE . 1 7260 19 1 1 1 87 LYS 19 A . 87 LYS . 1 7260 19 1 1 1 88 GLU 19 A . 88 GLU . 1 7260 19 1 1 1 89 ILE 19 A . 89 ILE . 1 7260 19 1 1 1 90 LYS 19 A . 90 LYS . 1 7260 19 1 1 1 91 ASP 19 A . 91 ASP . 1 7260 19 1 1 1 92 TRP 19 A . 92 TRP . 1 7260 19 1 1 1 93 ILE 19 A . 93 ILE . 1 7260 19 1 1 1 94 LYS 19 A . 94 LYS . 1 7260 19 1 1 1 95 LEU 19 A . 95 LEU . 1 7260 19 1 1 1 96 GLU 19 A . 96 GLU . 1 7260 19 1 1 1 97 HIS 19 A . 97 HIS . 1 7260 19 1 1 1 98 HIS 19 A . 98 HIS . 1 7260 19 1 1 1 99 HIS 19 A . 99 HIS . 1 7260 19 1 1 1 100 HIS 19 A . 100 HIS . 1 7260 19 1 1 1 101 HIS 19 A . 101 HIS . 1 7260 19 1 1 1 102 HIS 19 A . 102 HIS . 1 7260 19 stop_ save_ save_PB_annotation_20 _PB_list.Sf_category PB_list _PB_list.ID 20 _PB_list.Query_ID db2hgc_1791#A _PB_list.Queried_date 2014-12-15 _PB_list.Input_file_name pdb2hgc.ent _PB_list.Output_file_name bmr7260_PB.str _PB_list.Electronic_address http://bmrbpub.protein.osaka-u.ac.jp/archive/pb/bmr7260_PB.str _PB_list.AA_seq_one_letter_code KLRYAILKEIFEGNTPLSENDIGVTEDQFDDAVNFLKREGYIIGVHYSDDRPHLYKLGPELTEKGENYLKENGTWSKA _PB_list.PB_seq_code zzmmmmmmmmmnopaadfklnopafklmmmmmmmmmmnopaghiacfklpagbpabfbacdfklmmmmmmmmnopazz _PB_list.PDB_ID 2HGC _PB_list.PDBX_exptl_method "SOLUTION NMR" _PB_list.PDBX_NMR_refine_method "Noesy assignments made with iterative method using CS, 3J, Hyper (dihedral), and Dyana for simulated annealing MD. Converged structures are further refined using NIH-xplor followed by CNS in explicit water shell (Nielges) . Full lenght sequence was carried through the refinement protocol, the disordered regions and hexHIS tag are not reported. Structure based on 595 constraints, 249 long range, 163 dihedral constraints and 36 H-bond constraints." _PB_list.Entry_ID 7260 loop_ _PB_char.Entity_assembly_ID _PB_char.Assembly_ID _PB_char.Entity_ID _PB_char.Comp_index_ID _PB_char.Comp_ID _PB_char.PDB_model_num _PB_char.PDB_strand_ID _PB_char.PDB_ins_code _PB_char.PDB_residue_no _PB_char.PDB_residue_name _PB_char.PB_code _PB_char.Align _PB_char.Entry_ID _PB_char.PB_list_ID 1 1 1 1 MET 20 A . 1 MET . 1 7260 20 1 1 1 2 ASN 20 A . 2 ASN . 1 7260 20 1 1 1 3 LYS 20 A . 3 LYS . 1 7260 20 1 1 1 4 ASP 20 A . 4 ASP . 1 7260 20 1 1 1 5 LYS 20 A . 5 LYS . 1 7260 20 1 1 1 6 LEU 20 A . 6 LEU . 1 7260 20 1 1 1 7 ARG 20 A . 7 ARG m 1 7260 20 1 1 1 8 TYR 20 A . 8 TYR m 1 7260 20 1 1 1 9 ALA 20 A . 9 ALA m 1 7260 20 1 1 1 10 ILE 20 A . 10 ILE m 1 7260 20 1 1 1 11 LEU 20 A . 11 LEU m 1 7260 20 1 1 1 12 LYS 20 A . 12 LYS m 1 7260 20 1 1 1 13 GLU 20 A . 13 GLU m 1 7260 20 1 1 1 14 ILE 20 A . 14 ILE m 1 7260 20 1 1 1 15 PHE 20 A . 15 PHE m 1 7260 20 1 1 1 16 GLU 20 A . 16 GLU n 1 7260 20 1 1 1 17 GLY 20 A . 17 GLY o 1 7260 20 1 1 1 18 ASN 20 A . 18 ASN p 1 7260 20 1 1 1 19 THR 20 A . 19 THR a 1 7260 20 1 1 1 20 PRO 20 A . 20 PRO a 1 7260 20 1 1 1 21 LEU 20 A . 21 LEU d 1 7260 20 1 1 1 22 SER 20 A . 22 SER f 1 7260 20 1 1 1 23 GLU 20 A . 23 GLU k 1 7260 20 1 1 1 24 ASN 20 A . 24 ASN l 1 7260 20 1 1 1 25 ASP 20 A . 25 ASP n 1 7260 20 1 1 1 26 ILE 20 A . 26 ILE o 1 7260 20 1 1 1 27 GLY 20 A . 27 GLY p 1 7260 20 1 1 1 28 VAL 20 A . 28 VAL a 1 7260 20 1 1 1 29 THR 20 A . 29 THR f 1 7260 20 1 1 1 30 GLU 20 A . 30 GLU k 1 7260 20 1 1 1 31 ASP 20 A . 31 ASP l 1 7260 20 1 1 1 32 GLN 20 A . 32 GLN m 1 7260 20 1 1 1 33 PHE 20 A . 33 PHE m 1 7260 20 1 1 1 34 ASP 20 A . 34 ASP m 1 7260 20 1 1 1 35 ASP 20 A . 35 ASP m 1 7260 20 1 1 1 36 ALA 20 A . 36 ALA m 1 7260 20 1 1 1 37 VAL 20 A . 37 VAL m 1 7260 20 1 1 1 38 ASN 20 A . 38 ASN m 1 7260 20 1 1 1 39 PHE 20 A . 39 PHE m 1 7260 20 1 1 1 40 LEU 20 A . 40 LEU m 1 7260 20 1 1 1 41 LYS 20 A . 41 LYS m 1 7260 20 1 1 1 42 ARG 20 A . 42 ARG n 1 7260 20 1 1 1 43 GLU 20 A . 43 GLU o 1 7260 20 1 1 1 44 GLY 20 A . 44 GLY p 1 7260 20 1 1 1 45 TYR 20 A . 45 TYR a 1 7260 20 1 1 1 46 ILE 20 A . 46 ILE g 1 7260 20 1 1 1 47 ILE 20 A . 47 ILE h 1 7260 20 1 1 1 48 GLY 20 A . 48 GLY i 1 7260 20 1 1 1 49 VAL 20 A . 49 VAL a 1 7260 20 1 1 1 50 HIS 20 A . 50 HIS c 1 7260 20 1 1 1 51 TYR 20 A . 51 TYR f 1 7260 20 1 1 1 52 SER 20 A . 52 SER k 1 7260 20 1 1 1 53 ASP 20 A . 53 ASP l 1 7260 20 1 1 1 54 ASP 20 A . 54 ASP p 1 7260 20 1 1 1 55 ARG 20 A . 55 ARG a 1 7260 20 1 1 1 56 PRO 20 A . 56 PRO g 1 7260 20 1 1 1 57 HIS 20 A . 57 HIS b 1 7260 20 1 1 1 58 LEU 20 A . 58 LEU p 1 7260 20 1 1 1 59 TYR 20 A . 59 TYR a 1 7260 20 1 1 1 60 LYS 20 A . 60 LYS b 1 7260 20 1 1 1 61 LEU 20 A . 61 LEU f 1 7260 20 1 1 1 62 GLY 20 A . 62 GLY b 1 7260 20 1 1 1 63 PRO 20 A . 63 PRO a 1 7260 20 1 1 1 64 GLU 20 A . 64 GLU c 1 7260 20 1 1 1 65 LEU 20 A . 65 LEU d 1 7260 20 1 1 1 66 THR 20 A . 66 THR f 1 7260 20 1 1 1 67 GLU 20 A . 67 GLU k 1 7260 20 1 1 1 68 LYS 20 A . 68 LYS l 1 7260 20 1 1 1 69 GLY 20 A . 69 GLY m 1 7260 20 1 1 1 70 GLU 20 A . 70 GLU m 1 7260 20 1 1 1 71 ASN 20 A . 71 ASN m 1 7260 20 1 1 1 72 TYR 20 A . 72 TYR m 1 7260 20 1 1 1 73 LEU 20 A . 73 LEU m 1 7260 20 1 1 1 74 LYS 20 A . 74 LYS m 1 7260 20 1 1 1 75 GLU 20 A . 75 GLU m 1 7260 20 1 1 1 76 ASN 20 A . 76 ASN m 1 7260 20 1 1 1 77 GLY 20 A . 77 GLY n 1 7260 20 1 1 1 78 THR 20 A . 78 THR o 1 7260 20 1 1 1 79 TRP 20 A . 79 TRP p 1 7260 20 1 1 1 80 SER 20 A . 80 SER a 1 7260 20 1 1 1 81 LYS 20 A . 81 LYS . 1 7260 20 1 1 1 82 ALA 20 A . 82 ALA . 1 7260 20 1 1 1 83 TYR 20 A . 83 TYR . 1 7260 20 1 1 1 84 LYS 20 A . 84 LYS . 1 7260 20 1 1 1 85 THR 20 A . 85 THR . 1 7260 20 1 1 1 86 ILE 20 A . 86 ILE . 1 7260 20 1 1 1 87 LYS 20 A . 87 LYS . 1 7260 20 1 1 1 88 GLU 20 A . 88 GLU . 1 7260 20 1 1 1 89 ILE 20 A . 89 ILE . 1 7260 20 1 1 1 90 LYS 20 A . 90 LYS . 1 7260 20 1 1 1 91 ASP 20 A . 91 ASP . 1 7260 20 1 1 1 92 TRP 20 A . 92 TRP . 1 7260 20 1 1 1 93 ILE 20 A . 93 ILE . 1 7260 20 1 1 1 94 LYS 20 A . 94 LYS . 1 7260 20 1 1 1 95 LEU 20 A . 95 LEU . 1 7260 20 1 1 1 96 GLU 20 A . 96 GLU . 1 7260 20 1 1 1 97 HIS 20 A . 97 HIS . 1 7260 20 1 1 1 98 HIS 20 A . 98 HIS . 1 7260 20 1 1 1 99 HIS 20 A . 99 HIS . 1 7260 20 1 1 1 100 HIS 20 A . 100 HIS . 1 7260 20 1 1 1 101 HIS 20 A . 101 HIS . 1 7260 20 1 1 1 102 HIS 20 A . 102 HIS . 1 7260 20 stop_ save_