data_1AM2_A # _pdbx_database_status.entry_id 1AM2_A _pdbx_database_status.status_code . _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.recvd_initial_deposition_date ? _pdbx_database_status.status_code_nmr_data ? _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.methods_development_category ? # _entity_poly.entity_id 1 _entity_poly.type "polypeptide(L)" _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;ASITGDALVALPEGESVRIADIVPGARPNSDNAIDLKVLDRHGNPVLADRLFHSGEHPVYAVRTVEGLRVTGTANHPLLC LVDVAGVPTLLWKLIDEIKPGDYAVIQRSAFSTVGVPGLVRFLEAHHRDPDAKAIADELTDGRFYYAKVASVTDAGVQPV YSLRVDTADHAFITNGFVSHN ; _entity_poly.pdbx_seq_one_letter_code_can ;ASITGDALVALPEGESVRIADIVPGARPNSDNAIDLKVLDRHGNPVLADRLFHSGEHPVYAVRTVEGLRVTGTANHPLLC LVDVAGVPTLLWKLIDEIKPGDYAVIQRSAFSTVGVPGLVRFLEAHHRDPDAKAIADELTDGRFYYAKVASVTDAGVQPV YSLRVDTADHAFITNGFVSHN ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 SER n 1 3 ILE n 1 4 THR n 1 5 GLY n 1 6 ASP n 1 7 ALA n 1 8 LEU n 1 9 VAL n 1 10 ALA n 1 11 LEU n 1 12 PRO n 1 13 GLU n 1 14 GLY n 1 15 GLU n 1 16 SER n 1 17 VAL n 1 18 ARG n 1 19 ILE n 1 20 ALA n 1 21 ASP n 1 22 ILE n 1 23 VAL n 1 24 PRO n 1 25 GLY n 1 26 ALA n 1 27 ARG n 1 28 PRO n 1 29 ASN n 1 30 SER n 1 31 ASP n 1 32 ASN n 1 33 ALA n 1 34 ILE n 1 35 ASP n 1 36 LEU n 1 37 LYS n 1 38 VAL n 1 39 LEU n 1 40 ASP n 1 41 ARG n 1 42 HIS n 1 43 GLY n 1 44 ASN n 1 45 PRO n 1 46 VAL n 1 47 LEU n 1 48 ALA n 1 49 ASP n 1 50 ARG n 1 51 LEU n 1 52 PHE n 1 53 HIS n 1 54 SER n 1 55 GLY n 1 56 GLU n 1 57 HIS n 1 58 PRO n 1 59 VAL n 1 60 TYR n 1 61 ALA n 1 62 VAL n 1 63 ARG n 1 64 THR n 1 65 VAL n 1 66 GLU n 1 67 GLY n 1 68 LEU n 1 69 ARG n 1 70 VAL n 1 71 THR n 1 72 GLY n 1 73 THR n 1 74 ALA n 1 75 ASN n 1 76 HIS n 1 77 PRO n 1 78 LEU n 1 79 LEU n 1 80 CYS n 1 81 LEU n 1 82 VAL n 1 83 ASP n 1 84 VAL n 1 85 ALA n 1 86 GLY n 1 87 VAL n 1 88 PRO n 1 89 THR n 1 90 LEU n 1 91 LEU n 1 92 TRP n 1 93 LYS n 1 94 LEU n 1 95 ILE n 1 96 ASP n 1 97 GLU n 1 98 ILE n 1 99 LYS n 1 100 PRO n 1 101 GLY n 1 102 ASP n 1 103 TYR n 1 104 ALA n 1 105 VAL n 1 106 ILE n 1 107 GLN n 1 108 ARG n 1 109 SER n 1 110 ALA n 1 111 PHE n 1 112 SER n 1 113 THR n 1 114 VAL n 1 115 GLY n 1 116 VAL n 1 117 PRO n 1 118 GLY n 1 119 LEU n 1 120 VAL n 1 121 ARG n 1 122 PHE n 1 123 LEU n 1 124 GLU n 1 125 ALA n 1 126 HIS n 1 127 HIS n 1 128 ARG n 1 129 ASP n 1 130 PRO n 1 131 ASP n 1 132 ALA n 1 133 LYS n 1 134 ALA n 1 135 ILE n 1 136 ALA n 1 137 ASP n 1 138 GLU n 1 139 LEU n 1 140 THR n 1 141 ASP n 1 142 GLY n 1 143 ARG n 1 144 PHE n 1 145 TYR n 1 146 TYR n 1 147 ALA n 1 148 LYS n 1 149 VAL n 1 150 ALA n 1 151 SER n 1 152 VAL n 1 153 THR n 1 154 ASP n 1 155 ALA n 1 156 GLY n 1 157 VAL n 1 158 GLN n 1 159 PRO n 1 160 VAL n 1 161 TYR n 1 162 SER n 1 163 LEU n 1 164 ARG n 1 165 VAL n 1 166 ASP n 1 167 THR n 1 168 ALA n 1 169 ASP n 1 170 HIS n 1 171 ALA n 1 172 PHE n 1 173 ILE n 1 174 THR n 1 175 ASN n 1 176 GLY n 1 177 PHE n 1 178 VAL n 1 179 SER n 1 180 HIS n 1 181 ASN n # _entity.id 1 _entity.type polymer _entity.src_method man _entity.pdbx_description ? _entity.formula_weight 19449.920 _entity.pdbx_number_of_molecules 1 _entity.pdbx_ec ? _entity.pdbx_mutation ? _entity.pdbx_fragment ? _entity.details ? # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 1 1 ALA ALA A . n A 1 2 SER 2 2 2 SER SER A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 THR 4 4 4 THR THR A . n A 1 5 GLY 5 5 5 GLY GLY A . n A 1 6 ASP 6 6 6 ASP ASP A . n A 1 7 ALA 7 7 7 ALA ALA A . n A 1 8 LEU 8 8 8 LEU LEU A . n A 1 9 VAL 9 9 9 VAL VAL A . n A 1 10 ALA 10 10 10 ALA ALA A . n A 1 11 LEU 11 11 11 LEU LEU A . n A 1 12 PRO 12 12 12 PRO PRO A . n A 1 13 GLU 13 13 13 GLU GLU A . n A 1 14 GLY 14 14 14 GLY GLY A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 SER 16 16 16 SER SER A . n A 1 17 VAL 17 17 17 VAL VAL A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 ALA 20 20 20 ALA ALA A . n A 1 21 ASP 21 21 21 ASP ASP A . n A 1 22 ILE 22 22 22 ILE ILE A . n A 1 23 VAL 23 23 23 VAL VAL A . n A 1 24 PRO 24 24 24 PRO PRO A . n A 1 25 GLY 25 25 25 GLY GLY A . n A 1 26 ALA 26 26 26 ALA ALA A . n A 1 27 ARG 27 27 27 ARG ARG A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 ASN 29 29 29 ASN ASN A . n A 1 30 SER 30 30 30 SER SER A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ASN 32 32 32 ASN ASN A . n A 1 33 ALA 33 33 33 ALA ALA A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 ASP 35 35 35 ASP ASP A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 LYS 37 37 37 LYS LYS A . n A 1 38 VAL 38 38 38 VAL VAL A . n A 1 39 LEU 39 39 39 LEU LEU A . n A 1 40 ASP 40 40 40 ASP ASP A . n A 1 41 ARG 41 41 41 ARG ARG A . n A 1 42 HIS 42 42 42 HIS HIS A . n A 1 43 GLY 43 43 43 GLY GLY A . n A 1 44 ASN 44 44 44 ASN ASN A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 LEU 47 47 47 LEU LEU A . n A 1 48 ALA 48 48 48 ALA ALA A . n A 1 49 ASP 49 49 49 ASP ASP A . n A 1 50 ARG 50 50 50 ARG ARG A . n A 1 51 LEU 51 51 51 LEU LEU A . n A 1 52 PHE 52 52 52 PHE PHE A . n A 1 53 HIS 53 53 53 HIS HIS A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 GLU 56 56 56 GLU GLU A . n A 1 57 HIS 57 57 57 HIS HIS A . n A 1 58 PRO 58 58 58 PRO PRO A . n A 1 59 VAL 59 59 59 VAL VAL A . n A 1 60 TYR 60 60 60 TYR TYR A . n A 1 61 ALA 61 61 61 ALA ALA A . n A 1 62 VAL 62 62 62 VAL VAL A . n A 1 63 ARG 63 63 63 ARG ARG A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 GLU 66 66 66 GLU GLU A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 LEU 68 68 68 LEU LEU A . n A 1 69 ARG 69 69 69 ARG ARG A . n A 1 70 VAL 70 70 70 VAL VAL A . n A 1 71 THR 71 71 71 THR THR A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 THR 73 73 73 THR THR A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 ASN 75 75 75 ASN ASN A . n A 1 76 HIS 76 76 76 HIS HIS A . n A 1 77 PRO 77 77 77 PRO PRO A . n A 1 78 LEU 78 78 78 LEU LEU A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 CYS 80 80 80 CYS CYS A . n A 1 81 LEU 81 81 81 LEU LEU A . n A 1 82 VAL 82 82 82 VAL VAL A . n A 1 83 ASP 83 83 83 ASP ASP A . n A 1 84 VAL 84 84 84 VAL VAL A . n A 1 85 ALA 85 85 85 ALA ALA A . n A 1 86 GLY 86 86 86 GLY GLY A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 PRO 88 88 88 PRO PRO A . n A 1 89 THR 89 89 89 THR THR A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 LEU 91 91 91 LEU LEU A . n A 1 92 TRP 92 92 92 TRP TRP A . n A 1 93 LYS 93 93 93 LYS LYS A . n A 1 94 LEU 94 94 94 LEU LEU A . n A 1 95 ILE 95 95 95 ILE ILE A . n A 1 96 ASP 96 96 96 ASP ASP A . n A 1 97 GLU 97 97 97 GLU GLU A . n A 1 98 ILE 98 98 98 ILE ILE A . n A 1 99 LYS 99 99 99 LYS LYS A . n A 1 100 PRO 100 100 100 PRO PRO A . n A 1 101 GLY 101 101 101 GLY GLY A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 TYR 103 103 103 TYR TYR A . n A 1 104 ALA 104 104 104 ALA ALA A . n A 1 105 VAL 105 105 105 VAL VAL A . n A 1 106 ILE 106 106 106 ILE ILE A . n A 1 107 GLN 107 107 107 GLN GLN A . n A 1 108 ARG 108 108 108 ARG ARG A . n A 1 109 SER 109 109 109 SER SER A . n A 1 110 ALA 110 110 110 ALA ALA A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 THR 113 113 113 THR THR A . n A 1 114 VAL 114 114 114 VAL VAL A . n A 1 115 GLY 115 115 115 GLY GLY A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 PRO 117 117 117 PRO PRO A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 LEU 119 119 119 LEU LEU A . n A 1 120 VAL 120 120 120 VAL VAL A . n A 1 121 ARG 121 121 121 ARG ARG A . n A 1 122 PHE 122 122 122 PHE PHE A . n A 1 123 LEU 123 123 123 LEU LEU A . n A 1 124 GLU 124 124 124 GLU GLU A . n A 1 125 ALA 125 125 125 ALA ALA A . n A 1 126 HIS 126 126 126 HIS HIS A . n A 1 127 HIS 127 127 127 HIS HIS A . n A 1 128 ARG 128 128 128 ARG ARG A . n A 1 129 ASP 129 129 129 ASP ASP A . n A 1 130 PRO 130 130 130 PRO PRO A . n A 1 131 ASP 131 131 131 ASP ASP A . n A 1 132 ALA 132 132 132 ALA ALA A . n A 1 133 LYS 133 133 133 LYS LYS A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 ILE 135 135 135 ILE ILE A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 GLU 138 138 138 GLU GLU A . n A 1 139 LEU 139 139 139 LEU LEU A . n A 1 140 THR 140 140 140 THR THR A . n A 1 141 ASP 141 141 141 ASP ASP A . n A 1 142 GLY 142 142 142 GLY GLY A . n A 1 143 ARG 143 143 143 ARG ARG A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 TYR 145 145 145 TYR TYR A . n A 1 146 TYR 146 146 146 TYR TYR A . n A 1 147 ALA 147 147 147 ALA ALA A . n A 1 148 LYS 148 148 148 LYS LYS A . n A 1 149 VAL 149 149 149 VAL VAL A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 SER 151 151 151 SER SER A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 ASP 154 154 154 ASP ASP A . n A 1 155 ALA 155 155 155 ALA ALA A . n A 1 156 GLY 156 156 156 GLY GLY A . n A 1 157 VAL 157 157 157 VAL VAL A . n A 1 158 GLN 158 158 158 GLN GLN A . n A 1 159 PRO 159 159 159 PRO PRO A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 SER 162 162 162 SER SER A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 ARG 164 164 164 ARG ARG A . n A 1 165 VAL 165 165 165 VAL VAL A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ALA 168 168 168 ALA ALA A . n A 1 169 ASP 169 169 169 ASP ASP A . n A 1 170 HIS 170 170 170 HIS HIS A . n A 1 171 ALA 171 171 171 ALA ALA A . n A 1 172 PHE 172 172 172 PHE PHE A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 THR 174 174 174 THR THR A . n A 1 175 ASN 175 175 175 ASN ASN A . n A 1 176 GLY 176 176 176 GLY GLY A . n A 1 177 PHE 177 177 177 PHE PHE A . n A 1 178 VAL 178 178 178 VAL VAL A . n A 1 179 SER 179 179 179 SER SER A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 ASN 181 181 181 ASN ASN A . n # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA "L-peptide linking" y ALANINE ? "C3 H7 N O2" 89.093 ARG "L-peptide linking" y ARGININE ? "C6 H15 N4 O2 1" 175.209 ASN "L-peptide linking" y ASPARAGINE ? "C4 H8 N2 O3" 132.118 ASP "L-peptide linking" y "ASPARTIC ACID" ? "C4 H7 N O4" 133.103 CYS "L-peptide linking" y CYSTEINE ? "C3 H7 N O2 S" 121.158 GLN "L-peptide linking" y GLUTAMINE ? "C5 H10 N2 O3" 146.144 GLU "L-peptide linking" y "GLUTAMIC ACID" ? "C5 H9 N O4" 147.129 GLY "peptide linking" y GLYCINE ? "C2 H5 N O2" 75.067 HIS "L-peptide linking" y HISTIDINE ? "C6 H10 N3 O2 1" 156.162 ILE "L-peptide linking" y ISOLEUCINE ? "C6 H13 N O2" 131.173 LEU "L-peptide linking" y LEUCINE ? "C6 H13 N O2" 131.173 LYS "L-peptide linking" y LYSINE ? "C6 H15 N2 O2 1" 147.195 PHE "L-peptide linking" y PHENYLALANINE ? "C9 H11 N O2" 165.189 PRO "L-peptide linking" y PROLINE ? "C5 H9 N O2" 115.130 SER "L-peptide linking" y SERINE ? "C3 H7 N O3" 105.093 THR "L-peptide linking" y THREONINE ? "C4 H9 N O3" 119.119 TRP "L-peptide linking" y TRYPTOPHAN ? "C11 H12 N2 O2" 204.225 TYR "L-peptide linking" y TYROSINE ? "C9 H11 N O3" 181.189 VAL "L-peptide linking" y VALINE ? "C5 H11 N O2" 117.146 # _struct_asym.id A _struct_asym.pdbx_blank_PDB_chainid_flag N _struct_asym.pdbx_modified N _struct_asym.entity_id 1 _struct_asym.details ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id ALA _struct_mon_prot_cis.label_seq_id 1 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id ALA _struct_mon_prot_cis.auth_seq_id 1 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 SER _struct_mon_prot_cis.pdbx_label_seq_id_2 2 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 SER _struct_mon_prot_cis.pdbx_auth_seq_id_2 2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 0.69 # _atom_sites.entry_id 1AM2_A _atom_sites.fract_transf_matrix[1][1] 1.000000 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 1.000000 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 1.000000 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 NE A ARG 50 ? ? CZ A ARG 50 ? ? NH1 A ARG 50 ? ? 125.15 120.30 4.85 0.50 N 2 1 N A ASP 129 ? ? CA A ASP 129 ? ? C A ASP 129 ? ? 90.08 111.00 -20.92 2.70 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 HIS A 126 ? ? -93.45 -80.61 2 1 HIS A 127 ? ? 51.55 -62.01 # _pdbx_validate_polymer_linkage.id 1 _pdbx_validate_polymer_linkage.PDB_model_num 1 _pdbx_validate_polymer_linkage.auth_atom_id_1 C _pdbx_validate_polymer_linkage.auth_asym_id_1 A _pdbx_validate_polymer_linkage.auth_comp_id_1 SER _pdbx_validate_polymer_linkage.auth_seq_id_1 112 _pdbx_validate_polymer_linkage.PDB_ins_code_1 ? _pdbx_validate_polymer_linkage.label_alt_id_1 ? _pdbx_validate_polymer_linkage.auth_atom_id_2 N _pdbx_validate_polymer_linkage.auth_asym_id_2 A _pdbx_validate_polymer_linkage.auth_comp_id_2 THR _pdbx_validate_polymer_linkage.auth_seq_id_2 113 _pdbx_validate_polymer_linkage.PDB_ins_code_2 ? _pdbx_validate_polymer_linkage.label_alt_id_2 ? _pdbx_validate_polymer_linkage.dist 19.18 # loop_ _atom_type.symbol C N O S # _entry.id 1AM2_A # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? -6.733 27.027 22.853 1.00 22.21 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -5.371 27.460 22.402 1.00 22.72 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? -5.625 28.406 21.245 1.00 23.83 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -6.451 28.063 20.407 1.00 25.97 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? -4.618 26.234 21.913 1.00 21.33 ? 1 ALA A CB 1 ATOM 6 N N . SER A 1 2 ? -4.945 29.548 21.117 1.00 20.03 ? 2 SER A N 1 ATOM 7 C CA . SER A 1 2 ? -3.910 30.030 21.999 1.00 18.64 ? 2 SER A CA 1 ATOM 8 C C . SER A 1 2 ? -4.118 31.504 22.248 1.00 18.57 ? 2 SER A C 1 ATOM 9 O O . SER A 1 2 ? -4.798 32.196 21.494 1.00 18.23 ? 2 SER A O 1 ATOM 10 C CB . SER A 1 2 ? -2.557 29.907 21.311 1.00 15.83 ? 2 SER A CB 1 ATOM 11 O OG . SER A 1 2 ? -2.235 28.562 21.036 1.00 21.34 ? 2 SER A OG 1 ATOM 12 N N . ILE A 1 3 ? -3.439 31.986 23.270 1.00 18.53 ? 3 ILE A N 1 ATOM 13 C CA . ILE A 1 3 ? -3.510 33.346 23.648 1.00 17.17 ? 3 ILE A CA 1 ATOM 14 C C . ILE A 1 3 ? -2.150 33.983 23.778 1.00 18.08 ? 3 ILE A C 1 ATOM 15 O O . ILE A 1 3 ? -1.117 33.356 24.027 1.00 21.02 ? 3 ILE A O 1 ATOM 16 C CB . ILE A 1 3 ? -4.253 33.543 24.948 1.00 18.46 ? 3 ILE A CB 1 ATOM 17 C CG1 . ILE A 1 3 ? -3.578 32.785 26.060 1.00 19.51 ? 3 ILE A CG1 1 ATOM 18 C CG2 . ILE A 1 3 ? -5.681 33.107 24.790 1.00 22.71 ? 3 ILE A CG2 1 ATOM 19 C CD1 . ILE A 1 3 ? -4.253 32.981 27.360 1.00 24.15 ? 3 ILE A CD1 1 ATOM 20 N N . THR A 1 4 ? -2.235 35.285 23.732 1.00 17.16 ? 4 THR A N 1 ATOM 21 C CA . THR A 1 4 ? -1.184 36.229 23.792 1.00 18.89 ? 4 THR A CA 1 ATOM 22 C C . THR A 1 4 ? -0.416 36.192 25.129 1.00 21.13 ? 4 THR A C 1 ATOM 23 O O . THR A 1 4 ? -0.998 35.982 26.212 1.00 19.21 ? 4 THR A O 1 ATOM 24 C CB . THR A 1 4 ? -1.886 37.510 23.391 1.00 23.66 ? 4 THR A CB 1 ATOM 25 O OG1 . THR A 1 4 ? -1.541 37.856 22.044 1.00 28.76 ? 4 THR A OG1 1 ATOM 26 C CG2 . THR A 1 4 ? -1.776 38.566 24.332 1.00 20.36 ? 4 THR A CG2 1 ATOM 27 N N . GLY A 1 5 ? 0.905 36.401 25.026 1.00 21.49 ? 5 GLY A N 1 ATOM 28 C CA . GLY A 1 5 ? 1.813 36.320 26.151 1.00 20.06 ? 5 GLY A CA 1 ATOM 29 C C . GLY A 1 5 ? 1.531 37.215 27.324 1.00 23.79 ? 5 GLY A C 1 ATOM 30 O O . GLY A 1 5 ? 2.054 36.990 28.394 1.00 28.58 ? 5 GLY A O 1 ATOM 31 N N . ASP A 1 6 ? 0.683 38.213 27.155 1.00 26.91 ? 6 ASP A N 1 ATOM 32 C CA . ASP A 1 6 ? 0.343 39.130 28.245 1.00 26.92 ? 6 ASP A CA 1 ATOM 33 C C . ASP A 1 6 ? -0.839 38.688 29.126 1.00 26.06 ? 6 ASP A C 1 ATOM 34 O O . ASP A 1 6 ? -1.065 39.267 30.192 1.00 25.84 ? 6 ASP A O 1 ATOM 35 C CB . ASP A 1 6 ? 0.048 40.517 27.678 1.00 32.75 ? 6 ASP A CB 1 ATOM 36 C CG . ASP A 1 6 ? -0.770 40.460 26.396 1.00 37.44 ? 6 ASP A CG 1 ATOM 37 O OD1 . ASP A 1 6 ? -2.028 40.394 26.484 1.00 41.06 ? 6 ASP A OD1 1 ATOM 38 O OD2 . ASP A 1 6 ? -0.136 40.484 25.299 1.00 44.54 ? 6 ASP A OD2 1 ATOM 39 N N . ALA A 1 7 ? -1.587 37.685 28.676 1.00 20.46 ? 7 ALA A N 1 ATOM 40 C CA . ALA A 1 7 ? -2.718 37.204 29.422 1.00 19.14 ? 7 ALA A CA 1 ATOM 41 C C . ALA A 1 7 ? -2.307 36.798 30.821 1.00 20.50 ? 7 ALA A C 1 ATOM 42 O O . ALA A 1 7 ? -1.321 36.098 31.004 1.00 24.01 ? 7 ALA A O 1 ATOM 43 C CB . ALA A 1 7 ? -3.315 36.032 28.699 1.00 19.21 ? 7 ALA A CB 1 ATOM 44 N N . LEU A 1 8 ? -3.054 37.209 31.824 1.00 17.24 ? 8 LEU A N 1 ATOM 45 C CA . LEU A 1 8 ? -2.701 36.811 33.160 1.00 17.36 ? 8 LEU A CA 1 ATOM 46 C C . LEU A 1 8 ? -3.399 35.521 33.493 1.00 16.97 ? 8 LEU A C 1 ATOM 47 O O . LEU A 1 8 ? -4.629 35.462 33.379 1.00 20.27 ? 8 LEU A O 1 ATOM 48 C CB . LEU A 1 8 ? -3.138 37.867 34.150 1.00 18.99 ? 8 LEU A CB 1 ATOM 49 C CG . LEU A 1 8 ? -2.371 39.172 34.086 1.00 22.37 ? 8 LEU A CG 1 ATOM 50 C CD1 . LEU A 1 8 ? -3.106 40.132 34.979 1.00 25.50 ? 8 LEU A CD1 1 ATOM 51 C CD2 . LEU A 1 8 ? -0.989 38.999 34.574 1.00 16.94 ? 8 LEU A CD2 1 ATOM 52 N N . VAL A 1 9 ? -2.638 34.496 33.888 1.00 14.73 ? 9 VAL A N 1 ATOM 53 C CA . VAL A 1 9 ? -3.214 33.203 34.248 1.00 17.95 ? 9 VAL A CA 1 ATOM 54 C C . VAL A 1 9 ? -3.505 33.249 35.744 1.00 20.39 ? 9 VAL A C 1 ATOM 55 O O . VAL A 1 9 ? -2.605 33.469 36.551 1.00 23.94 ? 9 VAL A O 1 ATOM 56 C CB . VAL A 1 9 ? -2.227 32.050 33.953 1.00 16.40 ? 9 VAL A CB 1 ATOM 57 C CG1 . VAL A 1 9 ? -2.704 30.752 34.533 1.00 10.60 ? 9 VAL A CG1 1 ATOM 58 C CG2 . VAL A 1 9 ? -2.108 31.868 32.471 1.00 20.66 ? 9 VAL A CG2 1 ATOM 59 N N . ALA A 1 10 ? -4.759 33.057 36.124 1.00 20.45 ? 10 ALA A N 1 ATOM 60 C CA . ALA A 1 10 ? -5.131 33.066 37.535 1.00 21.16 ? 10 ALA A CA 1 ATOM 61 C C . ALA A 1 10 ? -4.578 31.852 38.309 1.00 22.52 ? 10 ALA A C 1 ATOM 62 O O . ALA A 1 10 ? -4.779 30.692 37.930 1.00 22.54 ? 10 ALA A O 1 ATOM 63 C CB . ALA A 1 10 ? -6.650 33.158 37.685 1.00 18.59 ? 10 ALA A CB 1 ATOM 64 N N . LEU A 1 11 ? -3.913 32.134 39.420 1.00 22.67 ? 11 LEU A N 1 ATOM 65 C CA . LEU A 1 11 ? -3.330 31.101 40.258 1.00 22.54 ? 11 LEU A CA 1 ATOM 66 C C . LEU A 1 11 ? -4.019 31.232 41.580 1.00 23.30 ? 11 LEU A C 1 ATOM 67 O O . LEU A 1 11 ? -4.752 32.199 41.806 1.00 21.45 ? 11 LEU A O 1 ATOM 68 C CB . LEU A 1 11 ? -1.851 31.391 40.502 1.00 21.42 ? 11 LEU A CB 1 ATOM 69 C CG . LEU A 1 11 ? -0.951 31.582 39.301 1.00 22.61 ? 11 LEU A CG 1 ATOM 70 C CD1 . LEU A 1 11 ? 0.373 32.006 39.819 1.00 18.63 ? 11 LEU A CD1 1 ATOM 71 C CD2 . LEU A 1 11 ? -0.850 30.321 38.478 1.00 21.37 ? 11 LEU A CD2 1 ATOM 72 N N . PRO A 1 12 ? -3.842 30.241 42.466 1.00 28.05 ? 12 PRO A N 1 ATOM 73 C CA . PRO A 1 12 ? -4.467 30.286 43.800 1.00 30.86 ? 12 PRO A CA 1 ATOM 74 C C . PRO A 1 12 ? -3.906 31.408 44.709 1.00 33.35 ? 12 PRO A C 1 ATOM 75 O O . PRO A 1 12 ? -2.816 31.961 44.465 1.00 35.48 ? 12 PRO A O 1 ATOM 76 C CB . PRO A 1 12 ? -4.169 28.900 44.357 1.00 26.41 ? 12 PRO A CB 1 ATOM 77 C CG . PRO A 1 12 ? -4.198 28.036 43.126 1.00 25.35 ? 12 PRO A CG 1 ATOM 78 C CD . PRO A 1 12 ? -3.385 28.873 42.161 1.00 28.03 ? 12 PRO A CD 1 ATOM 79 N N . GLU A 1 13 ? -4.697 31.776 45.715 1.00 37.14 ? 13 GLU A N 1 ATOM 80 C CA . GLU A 1 13 ? -4.320 32.802 46.681 1.00 39.44 ? 13 GLU A CA 1 ATOM 81 C C . GLU A 1 13 ? -4.300 34.200 46.103 1.00 39.77 ? 13 GLU A C 1 ATOM 82 O O . GLU A 1 13 ? -3.511 35.029 46.542 1.00 42.15 ? 13 GLU A O 1 ATOM 83 C CB . GLU A 1 13 ? -2.953 32.494 47.311 1.00 45.43 ? 13 GLU A CB 1 ATOM 84 C CG . GLU A 1 13 ? -2.982 32.040 48.768 1.00 55.80 ? 13 GLU A CG 1 ATOM 85 C CD . GLU A 1 13 ? -3.162 30.531 48.959 1.00 61.63 ? 13 GLU A CD 1 ATOM 86 O OE1 . GLU A 1 13 ? -4.308 30.025 48.855 1.00 65.16 ? 13 GLU A OE1 1 ATOM 87 O OE2 . GLU A 1 13 ? -2.148 29.850 49.248 1.00 65.79 ? 13 GLU A OE2 1 ATOM 88 N N . GLY A 1 14 ? -5.135 34.464 45.104 1.00 40.97 ? 14 GLY A N 1 ATOM 89 C CA . GLY A 1 14 ? -5.199 35.801 44.526 1.00 40.88 ? 14 GLY A CA 1 ATOM 90 C C . GLY A 1 14 ? -4.030 36.151 43.640 1.00 41.26 ? 14 GLY A C 1 ATOM 91 O O . GLY A 1 14 ? -4.001 37.222 43.048 1.00 41.23 ? 14 GLY A O 1 ATOM 92 N N . GLU A 1 15 ? -3.102 35.212 43.510 1.00 42.71 ? 15 GLU A N 1 ATOM 93 C CA . GLU A 1 15 ? -1.888 35.345 42.697 1.00 44.42 ? 15 GLU A CA 1 ATOM 94 C C . GLU A 1 15 ? -2.176 35.123 41.197 1.00 42.30 ? 15 GLU A C 1 ATOM 95 O O . GLU A 1 15 ? -3.169 34.477 40.842 1.00 41.58 ? 15 GLU A O 1 ATOM 96 C CB . GLU A 1 15 ? -0.897 34.274 43.180 1.00 51.20 ? 15 GLU A CB 1 ATOM 97 C CG . GLU A 1 15 ? 0.565 34.625 43.058 1.00 62.76 ? 15 GLU A CG 1 ATOM 98 C CD . GLU A 1 15 ? 0.997 35.709 44.041 1.00 70.07 ? 15 GLU A CD 1 ATOM 99 O OE1 . GLU A 1 15 ? 0.714 36.906 43.790 1.00 73.34 ? 15 GLU A OE1 1 ATOM 100 O OE2 . GLU A 1 15 ? 1.635 35.365 45.063 1.00 75.48 ? 15 GLU A OE2 1 ATOM 101 N N . SER A 1 16 ? -1.311 35.629 40.315 1.00 38.11 ? 16 SER A N 1 ATOM 102 C CA . SER A 1 16 ? -1.499 35.415 38.874 1.00 34.78 ? 16 SER A CA 1 ATOM 103 C C . SER A 1 16 ? -0.182 35.637 38.151 1.00 32.03 ? 16 SER A C 1 ATOM 104 O O . SER A 1 16 ? 0.675 36.334 38.662 1.00 32.34 ? 16 SER A O 1 ATOM 105 C CB . SER A 1 16 ? -2.590 36.324 38.312 1.00 34.53 ? 16 SER A CB 1 ATOM 106 O OG . SER A 1 16 ? -2.185 37.665 38.353 1.00 42.30 ? 16 SER A OG 1 ATOM 107 N N . VAL A 1 17 ? -0.020 35.056 36.965 1.00 28.42 ? 17 VAL A N 1 ATOM 108 C CA . VAL A 1 17 ? 1.232 35.168 36.229 1.00 23.71 ? 17 VAL A CA 1 ATOM 109 C C . VAL A 1 17 ? 0.948 35.291 34.744 1.00 22.97 ? 17 VAL A C 1 ATOM 110 O O . VAL A 1 17 ? 0.040 34.640 34.254 1.00 24.23 ? 17 VAL A O 1 ATOM 111 C CB . VAL A 1 17 ? 2.131 33.890 36.510 1.00 24.14 ? 17 VAL A CB 1 ATOM 112 C CG1 . VAL A 1 17 ? 1.427 32.609 36.032 1.00 21.12 ? 17 VAL A CG1 1 ATOM 113 C CG2 . VAL A 1 17 ? 3.523 34.015 35.840 1.00 24.54 ? 17 VAL A CG2 1 ATOM 114 N N . ARG A 1 18 ? 1.682 36.151 34.035 1.00 22.19 ? 18 ARG A N 1 ATOM 115 C CA . ARG A 1 18 ? 1.498 36.288 32.591 1.00 20.78 ? 18 ARG A CA 1 ATOM 116 C C . ARG A 1 18 ? 1.888 34.959 31.980 1.00 21.52 ? 18 ARG A C 1 ATOM 117 O O . ARG A 1 18 ? 2.864 34.365 32.381 1.00 19.21 ? 18 ARG A O 1 ATOM 118 C CB . ARG A 1 18 ? 2.390 37.374 32.026 1.00 21.10 ? 18 ARG A CB 1 ATOM 119 C CG . ARG A 1 18 ? 2.105 38.764 32.584 1.00 29.79 ? 18 ARG A CG 1 ATOM 120 C CD . ARG A 1 18 ? 2.904 39.833 31.849 1.00 34.64 ? 18 ARG A CD 1 ATOM 121 N NE . ARG A 1 18 ? 4.265 39.367 31.569 1.00 47.30 ? 18 ARG A NE 1 ATOM 122 C CZ . ARG A 1 18 ? 4.841 39.301 30.351 1.00 51.78 ? 18 ARG A CZ 1 ATOM 123 N NH1 . ARG A 1 18 ? 4.188 39.688 29.248 1.00 53.97 ? 18 ARG A NH1 1 ATOM 124 N NH2 . ARG A 1 18 ? 6.066 38.775 30.210 1.00 53.91 ? 18 ARG A NH2 1 ATOM 125 N N . ILE A 1 19 ? 1.130 34.466 31.013 1.00 22.03 ? 19 ILE A N 1 ATOM 126 C CA . ILE A 1 19 ? 1.476 33.191 30.411 1.00 20.13 ? 19 ILE A CA 1 ATOM 127 C C . ILE A 1 19 ? 2.922 33.120 29.794 1.00 21.76 ? 19 ILE A C 1 ATOM 128 O O . ILE A 1 19 ? 3.550 32.062 29.757 1.00 21.02 ? 19 ILE A O 1 ATOM 129 C CB . ILE A 1 19 ? 0.378 32.771 29.413 1.00 19.18 ? 19 ILE A CB 1 ATOM 130 C CG1 . ILE A 1 19 ? 0.632 31.353 28.899 1.00 22.24 ? 19 ILE A CG1 1 ATOM 131 C CG2 . ILE A 1 19 ? 0.298 33.739 28.258 1.00 14.57 ? 19 ILE A CG2 1 ATOM 132 C CD1 . ILE A 1 19 ? -0.648 30.621 28.450 1.00 20.08 ? 19 ILE A CD1 1 ATOM 133 N N . ALA A 1 20 ? 3.482 34.238 29.359 1.00 22.99 ? 20 ALA A N 1 ATOM 134 C CA . ALA A 1 20 ? 4.836 34.226 28.770 1.00 24.77 ? 20 ALA A CA 1 ATOM 135 C C . ALA A 1 20 ? 5.938 34.015 29.821 1.00 26.83 ? 20 ALA A C 1 ATOM 136 O O . ALA A 1 20 ? 7.101 33.712 29.482 1.00 26.73 ? 20 ALA A O 1 ATOM 137 C CB . ALA A 1 20 ? 5.092 35.533 27.980 1.00 18.12 ? 20 ALA A CB 1 ATOM 138 N N . ASP A 1 21 ? 5.557 34.154 31.089 1.00 26.44 ? 21 ASP A N 1 ATOM 139 C CA . ASP A 1 21 ? 6.479 34.004 32.208 1.00 28.66 ? 21 ASP A CA 1 ATOM 140 C C . ASP A 1 21 ? 6.446 32.669 32.968 1.00 29.17 ? 21 ASP A C 1 ATOM 141 O O . ASP A 1 21 ? 7.168 32.468 33.962 1.00 31.84 ? 21 ASP A O 1 ATOM 142 C CB . ASP A 1 21 ? 6.239 35.131 33.202 1.00 30.23 ? 21 ASP A CB 1 ATOM 143 C CG . ASP A 1 21 ? 6.399 36.479 32.587 1.00 29.46 ? 21 ASP A CG 1 ATOM 144 O OD1 . ASP A 1 21 ? 6.950 36.595 31.472 1.00 30.47 ? 21 ASP A OD1 1 ATOM 145 O OD2 . ASP A 1 21 ? 5.963 37.424 33.247 1.00 31.65 ? 21 ASP A OD2 1 ATOM 146 N N . ILE A 1 22 ? 5.578 31.769 32.550 1.00 27.92 ? 22 ILE A N 1 ATOM 147 C CA . ILE A 1 22 ? 5.497 30.482 33.208 1.00 25.44 ? 22 ILE A CA 1 ATOM 148 C C . ILE A 1 22 ? 6.799 29.715 32.899 1.00 28.30 ? 22 ILE A C 1 ATOM 149 O O . ILE A 1 22 ? 7.317 29.022 33.763 1.00 31.52 ? 22 ILE A O 1 ATOM 150 C CB . ILE A 1 22 ? 4.185 29.761 32.795 1.00 21.93 ? 22 ILE A CB 1 ATOM 151 C CG1 . ILE A 1 22 ? 3.000 30.508 33.431 1.00 16.21 ? 22 ILE A CG1 1 ATOM 152 C CG2 . ILE A 1 22 ? 4.237 28.259 33.126 1.00 18.68 ? 22 ILE A CG2 1 ATOM 153 C CD1 . ILE A 1 22 ? 1.669 30.006 33.048 1.00 17.90 ? 22 ILE A CD1 1 ATOM 154 N N . VAL A 1 23 ? 7.281 29.789 31.655 1.00 28.33 ? 23 VAL A N 1 ATOM 155 C CA . VAL A 1 23 ? 8.574 29.189 31.254 1.00 28.20 ? 23 VAL A CA 1 ATOM 156 C C . VAL A 1 23 ? 9.260 30.425 30.652 1.00 27.91 ? 23 VAL A C 1 ATOM 157 O O . VAL A 1 23 ? 9.149 30.728 29.457 1.00 27.04 ? 23 VAL A O 1 ATOM 158 C CB . VAL A 1 23 ? 8.492 28.023 30.175 1.00 27.22 ? 23 VAL A CB 1 ATOM 159 C CG1 . VAL A 1 23 ? 9.880 27.632 29.731 1.00 22.19 ? 23 VAL A CG1 1 ATOM 160 C CG2 . VAL A 1 23 ? 7.795 26.787 30.730 1.00 24.33 ? 23 VAL A CG2 1 ATOM 161 N N . PRO A 1 24 ? 9.923 31.208 31.503 1.00 28.71 ? 24 PRO A N 1 ATOM 162 C CA . PRO A 1 24 ? 10.579 32.402 30.978 1.00 28.86 ? 24 PRO A CA 1 ATOM 163 C C . PRO A 1 24 ? 11.485 32.068 29.811 1.00 27.72 ? 24 PRO A C 1 ATOM 164 O O . PRO A 1 24 ? 12.193 31.070 29.816 1.00 30.46 ? 24 PRO A O 1 ATOM 165 C CB . PRO A 1 24 ? 11.360 32.892 32.190 1.00 29.08 ? 24 PRO A CB 1 ATOM 166 C CG . PRO A 1 24 ? 10.527 32.385 33.356 1.00 25.63 ? 24 PRO A CG 1 ATOM 167 C CD . PRO A 1 24 ? 10.273 30.998 32.920 1.00 25.50 ? 24 PRO A CD 1 ATOM 168 N N . GLY A 1 25 ? 11.416 32.850 28.765 1.00 28.12 ? 25 GLY A N 1 ATOM 169 C CA . GLY A 1 25 ? 12.283 32.540 27.641 1.00 31.27 ? 25 GLY A CA 1 ATOM 170 C C . GLY A 1 25 ? 12.013 31.274 26.831 1.00 33.17 ? 25 GLY A C 1 ATOM 171 O O . GLY A 1 25 ? 12.883 30.835 26.093 1.00 37.02 ? 25 GLY A O 1 ATOM 172 N N . ALA A 1 26 ? 10.825 30.686 26.976 1.00 34.83 ? 26 ALA A N 1 ATOM 173 C CA . ALA A 1 26 ? 10.394 29.503 26.225 1.00 31.09 ? 26 ALA A CA 1 ATOM 174 C C . ALA A 1 26 ? 10.626 29.731 24.749 1.00 29.25 ? 26 ALA A C 1 ATOM 175 O O . ALA A 1 26 ? 10.353 30.829 24.239 1.00 28.18 ? 26 ALA A O 1 ATOM 176 C CB . ALA A 1 26 ? 8.887 29.252 26.440 1.00 29.23 ? 26 ALA A CB 1 ATOM 177 N N . ARG A 1 27 ? 11.137 28.696 24.077 1.00 28.50 ? 27 ARG A N 1 ATOM 178 C CA . ARG A 1 27 ? 11.373 28.755 22.640 1.00 25.61 ? 27 ARG A CA 1 ATOM 179 C C . ARG A 1 27 ? 10.046 28.707 21.935 1.00 23.80 ? 27 ARG A C 1 ATOM 180 O O . ARG A 1 27 ? 9.072 28.113 22.395 1.00 24.19 ? 27 ARG A O 1 ATOM 181 C CB . ARG A 1 27 ? 12.185 27.554 22.121 1.00 26.55 ? 27 ARG A CB 1 ATOM 182 C CG . ARG A 1 27 ? 13.599 27.473 22.577 1.00 28.86 ? 27 ARG A CG 1 ATOM 183 C CD . ARG A 1 27 ? 14.319 26.223 22.020 1.00 30.62 ? 27 ARG A CD 1 ATOM 184 N NE . ARG A 1 27 ? 15.756 26.286 22.330 1.00 33.80 ? 27 ARG A NE 1 ATOM 185 C CZ . ARG A 1 27 ? 16.396 25.447 23.144 1.00 35.67 ? 27 ARG A CZ 1 ATOM 186 N NH1 . ARG A 1 27 ? 15.709 24.458 23.730 1.00 37.88 ? 27 ARG A NH1 1 ATOM 187 N NH2 . ARG A 1 27 ? 17.708 25.597 23.378 1.00 32.15 ? 27 ARG A NH2 1 ATOM 188 N N . PRO A 1 28 ? 9.994 29.350 20.791 1.00 24.49 ? 28 PRO A N 1 ATOM 189 C CA . PRO A 1 28 ? 8.829 29.434 19.914 1.00 24.04 ? 28 PRO A CA 1 ATOM 190 C C . PRO A 1 28 ? 8.632 28.028 19.360 1.00 21.57 ? 28 PRO A C 1 ATOM 191 O O . PRO A 1 28 ? 9.599 27.394 18.993 1.00 24.31 ? 28 PRO A O 1 ATOM 192 C CB . PRO A 1 28 ? 9.311 30.398 18.848 1.00 26.39 ? 28 PRO A CB 1 ATOM 193 C CG . PRO A 1 28 ? 10.348 31.245 19.594 1.00 24.89 ? 28 PRO A CG 1 ATOM 194 C CD . PRO A 1 28 ? 11.078 30.234 20.337 1.00 23.35 ? 28 PRO A CD 1 ATOM 195 N N . ASN A 1 29 ? 7.406 27.532 19.308 1.00 18.15 ? 29 ASN A N 1 ATOM 196 C CA . ASN A 1 29 ? 7.143 26.162 18.847 1.00 17.66 ? 29 ASN A CA 1 ATOM 197 C C . ASN A 1 29 ? 7.839 25.167 19.741 1.00 16.35 ? 29 ASN A C 1 ATOM 198 O O . ASN A 1 29 ? 8.488 24.245 19.259 1.00 16.65 ? 29 ASN A O 1 ATOM 199 C CB . ASN A 1 29 ? 7.582 25.902 17.418 1.00 19.84 ? 29 ASN A CB 1 ATOM 200 C CG . ASN A 1 29 ? 7.309 27.042 16.520 1.00 27.51 ? 29 ASN A CG 1 ATOM 201 O OD1 . ASN A 1 29 ? 6.168 27.527 16.391 1.00 29.64 ? 29 ASN A OD1 1 ATOM 202 N ND2 . ASN A 1 29 ? 8.373 27.555 15.934 1.00 32.26 ? 29 ASN A ND2 1 ATOM 203 N N . SER A 1 30 ? 7.619 25.282 21.042 1.00 15.18 ? 30 SER A N 1 ATOM 204 C CA . SER A 1 30 ? 8.252 24.374 21.981 1.00 14.46 ? 30 SER A CA 1 ATOM 205 C C . SER A 1 30 ? 7.192 23.779 22.828 1.00 16.94 ? 30 SER A C 1 ATOM 206 O O . SER A 1 30 ? 6.159 24.379 23.005 1.00 18.03 ? 30 SER A O 1 ATOM 207 C CB . SER A 1 30 ? 9.223 25.120 22.866 1.00 16.67 ? 30 SER A CB 1 ATOM 208 O OG . SER A 1 30 ? 8.559 26.089 23.634 1.00 19.25 ? 30 SER A OG 1 ATOM 209 N N . ASP A 1 31 ? 7.378 22.530 23.228 1.00 17.89 ? 31 ASP A N 1 ATOM 210 C CA . ASP A 1 31 ? 6.451 21.838 24.112 1.00 15.85 ? 31 ASP A CA 1 ATOM 211 C C . ASP A 1 31 ? 7.251 21.775 25.448 1.00 19.04 ? 31 ASP A C 1 ATOM 212 O O . ASP A 1 31 ? 8.306 21.158 25.507 1.00 18.84 ? 31 ASP A O 1 ATOM 213 C CB . ASP A 1 31 ? 6.186 20.448 23.556 1.00 16.10 ? 31 ASP A CB 1 ATOM 214 C CG . ASP A 1 31 ? 5.381 19.574 24.502 1.00 16.48 ? 31 ASP A CG 1 ATOM 215 O OD1 . ASP A 1 31 ? 5.298 19.792 25.727 1.00 18.91 ? 31 ASP A OD1 1 ATOM 216 O OD2 . ASP A 1 31 ? 4.830 18.608 24.000 1.00 22.30 ? 31 ASP A OD2 1 ATOM 217 N N . ASN A 1 32 ? 6.759 22.402 26.518 1.00 20.67 ? 32 ASN A N 1 ATOM 218 C CA . ASN A 1 32 ? 7.505 22.457 27.770 1.00 18.24 ? 32 ASN A CA 1 ATOM 219 C C . ASN A 1 32 ? 6.766 21.883 28.914 1.00 18.53 ? 32 ASN A C 1 ATOM 220 O O . ASN A 1 32 ? 5.678 22.324 29.177 1.00 19.34 ? 32 ASN A O 1 ATOM 221 C CB . ASN A 1 32 ? 7.807 23.923 28.122 1.00 18.95 ? 32 ASN A CB 1 ATOM 222 C CG . ASN A 1 32 ? 8.440 24.721 26.947 1.00 20.16 ? 32 ASN A CG 1 ATOM 223 O OD1 . ASN A 1 32 ? 9.664 24.747 26.765 1.00 20.13 ? 32 ASN A OD1 1 ATOM 224 N ND2 . ASN A 1 32 ? 7.599 25.419 26.199 1.00 19.81 ? 32 ASN A ND2 1 ATOM 225 N N . ALA A 1 33 ? 7.352 20.932 29.638 1.00 20.87 ? 33 ALA A N 1 ATOM 226 C CA . ALA A 1 33 ? 6.698 20.357 30.820 1.00 18.29 ? 33 ALA A CA 1 ATOM 227 C C . ALA A 1 33 ? 6.761 21.321 31.983 1.00 18.98 ? 33 ALA A C 1 ATOM 228 O O . ALA A 1 33 ? 7.753 21.983 32.169 1.00 21.63 ? 33 ALA A O 1 ATOM 229 C CB . ALA A 1 33 ? 7.329 19.067 31.204 1.00 17.43 ? 33 ALA A CB 1 ATOM 230 N N . ILE A 1 34 ? 5.661 21.461 32.716 1.00 22.69 ? 34 ILE A N 1 ATOM 231 C CA . ILE A 1 34 ? 5.572 22.346 33.888 1.00 23.04 ? 34 ILE A CA 1 ATOM 232 C C . ILE A 1 34 ? 4.769 21.615 34.959 1.00 23.24 ? 34 ILE A C 1 ATOM 233 O O . ILE A 1 34 ? 4.199 20.571 34.695 1.00 23.77 ? 34 ILE A O 1 ATOM 234 C CB . ILE A 1 34 ? 4.805 23.717 33.601 1.00 22.76 ? 34 ILE A CB 1 ATOM 235 C CG1 . ILE A 1 34 ? 3.344 23.493 33.197 1.00 18.11 ? 34 ILE A CG1 1 ATOM 236 C CG2 . ILE A 1 34 ? 5.536 24.539 32.573 1.00 25.93 ? 34 ILE A CG2 1 ATOM 237 C CD1 . ILE A 1 34 ? 2.527 24.760 33.116 1.00 16.84 ? 34 ILE A CD1 1 ATOM 238 N N . ASP A 1 35 ? 4.750 22.159 36.168 1.00 28.30 ? 35 ASP A N 1 ATOM 239 C CA . ASP A 1 35 ? 3.956 21.605 37.273 1.00 34.16 ? 35 ASP A CA 1 ATOM 240 C C . ASP A 1 35 ? 3.441 22.858 37.999 1.00 34.13 ? 35 ASP A C 1 ATOM 241 O O . ASP A 1 35 ? 4.075 23.373 38.916 1.00 39.18 ? 35 ASP A O 1 ATOM 242 C CB . ASP A 1 35 ? 4.809 20.720 38.185 1.00 40.35 ? 35 ASP A CB 1 ATOM 243 C CG . ASP A 1 35 ? 3.960 19.899 39.154 1.00 48.17 ? 35 ASP A CG 1 ATOM 244 O OD1 . ASP A 1 35 ? 3.431 18.831 38.767 1.00 53.02 ? 35 ASP A OD1 1 ATOM 245 O OD2 . ASP A 1 35 ? 3.792 20.335 40.310 1.00 57.69 ? 35 ASP A OD2 1 ATOM 246 N N . LEU A 1 36 ? 2.314 23.378 37.524 1.00 31.83 ? 36 LEU A N 1 ATOM 247 C CA . LEU A 1 36 ? 1.749 24.601 38.030 1.00 25.71 ? 36 LEU A CA 1 ATOM 248 C C . LEU A 1 36 ? 0.342 24.377 38.484 1.00 27.58 ? 36 LEU A C 1 ATOM 249 O O . LEU A 1 36 ? -0.418 23.655 37.851 1.00 29.65 ? 36 LEU A O 1 ATOM 250 C CB . LEU A 1 36 ? 1.685 25.583 36.893 1.00 24.58 ? 36 LEU A CB 1 ATOM 251 C CG . LEU A 1 36 ? 2.063 27.024 37.110 1.00 25.05 ? 36 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 36 ? 1.375 27.920 36.089 1.00 24.12 ? 36 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 36 ? 1.688 27.410 38.485 1.00 28.87 ? 36 LEU A CD2 1 ATOM 254 N N . LYS A 1 37 ? -0.012 24.998 39.593 1.00 27.81 ? 37 LYS A N 1 ATOM 255 C CA . LYS A 1 37 ? -1.368 24.911 40.102 1.00 26.35 ? 37 LYS A CA 1 ATOM 256 C C . LYS A 1 37 ? -2.045 26.174 39.510 1.00 22.85 ? 37 LYS A C 1 ATOM 257 O O . LYS A 1 37 ? -1.575 27.305 39.648 1.00 21.16 ? 37 LYS A O 1 ATOM 258 C CB . LYS A 1 37 ? -1.335 24.913 41.638 1.00 34.14 ? 37 LYS A CB 1 ATOM 259 C CG . LYS A 1 37 ? -2.338 24.000 42.346 1.00 40.91 ? 37 LYS A CG 1 ATOM 260 C CD . LYS A 1 37 ? -2.085 22.540 42.024 1.00 49.92 ? 37 LYS A CD 1 ATOM 261 C CE . LYS A 1 37 ? -0.639 22.157 42.300 1.00 57.00 ? 37 LYS A CE 1 ATOM 262 N NZ . LYS A 1 37 ? -0.264 20.896 41.572 1.00 63.25 ? 37 LYS A NZ 1 ATOM 263 N N . VAL A 1 38 ? -3.211 25.996 38.940 1.00 20.67 ? 38 VAL A N 1 ATOM 264 C CA . VAL A 1 38 ? -3.862 27.088 38.266 1.00 19.82 ? 38 VAL A CA 1 ATOM 265 C C . VAL A 1 38 ? -5.351 27.021 38.594 1.00 17.59 ? 38 VAL A C 1 ATOM 266 O O . VAL A 1 38 ? -5.833 25.990 39.014 1.00 20.27 ? 38 VAL A O 1 ATOM 267 C CB . VAL A 1 38 ? -3.523 26.840 36.733 1.00 21.07 ? 38 VAL A CB 1 ATOM 268 C CG1 . VAL A 1 38 ? -4.726 26.485 35.903 1.00 20.21 ? 38 VAL A CG1 1 ATOM 269 C CG2 . VAL A 1 38 ? -2.646 27.879 36.191 1.00 18.69 ? 38 VAL A CG2 1 ATOM 270 N N . LEU A 1 39 ? -6.067 28.124 38.511 1.00 17.12 ? 39 LEU A N 1 ATOM 271 C CA . LEU A 1 39 ? -7.489 28.060 38.785 1.00 16.22 ? 39 LEU A CA 1 ATOM 272 C C . LEU A 1 39 ? -8.237 27.498 37.600 1.00 16.61 ? 39 LEU A C 1 ATOM 273 O O . LEU A 1 39 ? -7.920 27.837 36.477 1.00 16.81 ? 39 LEU A O 1 ATOM 274 C CB . LEU A 1 39 ? -8.042 29.435 39.052 1.00 14.11 ? 39 LEU A CB 1 ATOM 275 C CG . LEU A 1 39 ? -7.471 30.012 40.302 1.00 17.14 ? 39 LEU A CG 1 ATOM 276 C CD1 . LEU A 1 39 ? -8.303 31.230 40.666 1.00 18.29 ? 39 LEU A CD1 1 ATOM 277 C CD2 . LEU A 1 39 ? -7.470 28.977 41.386 1.00 14.84 ? 39 LEU A CD2 1 ATOM 278 N N . ASP A 1 40 ? -9.298 26.746 37.870 1.00 15.96 ? 40 ASP A N 1 ATOM 279 C CA . ASP A 1 40 ? -10.121 26.156 36.853 1.00 16.28 ? 40 ASP A CA 1 ATOM 280 C C . ASP A 1 40 ? -11.370 27.010 36.618 1.00 19.50 ? 40 ASP A C 1 ATOM 281 O O . ASP A 1 40 ? -11.480 28.131 37.118 1.00 20.04 ? 40 ASP A O 1 ATOM 282 C CB . ASP A 1 40 ? -10.467 24.693 37.200 1.00 20.59 ? 40 ASP A CB 1 ATOM 283 C CG . ASP A 1 40 ? -11.586 24.530 38.264 1.00 19.80 ? 40 ASP A CG 1 ATOM 284 O OD1 . ASP A 1 40 ? -12.002 25.479 38.957 1.00 23.53 ? 40 ASP A OD1 1 ATOM 285 O OD2 . ASP A 1 40 ? -12.073 23.394 38.417 1.00 21.72 ? 40 ASP A OD2 1 ATOM 286 N N . ARG A 1 41 ? -12.327 26.457 35.896 1.00 20.69 ? 41 ARG A N 1 ATOM 287 C CA . ARG A 1 41 ? -13.554 27.149 35.551 1.00 21.78 ? 41 ARG A CA 1 ATOM 288 C C . ARG A 1 41 ? -14.285 27.751 36.749 1.00 20.99 ? 41 ARG A C 1 ATOM 289 O O . ARG A 1 41 ? -14.912 28.786 36.609 1.00 21.02 ? 41 ARG A O 1 ATOM 290 C CB . ARG A 1 41 ? -14.467 26.184 34.794 1.00 21.79 ? 41 ARG A CB 1 ATOM 291 C CG . ARG A 1 41 ? -15.835 26.672 34.622 1.00 24.57 ? 41 ARG A CG 1 ATOM 292 C CD . ARG A 1 41 ? -16.747 25.532 34.396 1.00 24.43 ? 41 ARG A CD 1 ATOM 293 N NE . ARG A 1 41 ? -16.568 25.018 33.055 1.00 24.32 ? 41 ARG A NE 1 ATOM 294 C CZ . ARG A 1 41 ? -17.566 24.823 32.201 1.00 26.99 ? 41 ARG A CZ 1 ATOM 295 N NH1 . ARG A 1 41 ? -18.816 25.103 32.545 1.00 25.19 ? 41 ARG A NH1 1 ATOM 296 N NH2 . ARG A 1 41 ? -17.310 24.332 30.994 1.00 29.89 ? 41 ARG A NH2 1 ATOM 297 N N . HIS A 1 42 ? -14.236 27.091 37.907 1.00 21.08 ? 42 HIS A N 1 ATOM 298 C CA . HIS A 1 42 ? -14.893 27.593 39.135 1.00 19.88 ? 42 HIS A CA 1 ATOM 299 C C . HIS A 1 42 ? -14.021 28.331 40.131 1.00 20.35 ? 42 HIS A C 1 ATOM 300 O O . HIS A 1 42 ? -14.515 28.636 41.201 1.00 22.71 ? 42 HIS A O 1 ATOM 301 C CB . HIS A 1 42 ? -15.506 26.468 39.911 1.00 16.16 ? 42 HIS A CB 1 ATOM 302 C CG . HIS A 1 42 ? -16.540 25.746 39.141 1.00 18.04 ? 42 HIS A CG 1 ATOM 303 N ND1 . HIS A 1 42 ? -17.711 26.350 38.744 1.00 20.02 ? 42 HIS A ND1 1 ATOM 304 C CD2 . HIS A 1 42 ? -16.564 24.500 38.632 1.00 16.12 ? 42 HIS A CD2 1 ATOM 305 C CE1 . HIS A 1 42 ? -18.409 25.506 38.018 1.00 17.09 ? 42 HIS A CE1 1 ATOM 306 N NE2 . HIS A 1 42 ? -17.734 24.376 37.942 1.00 19.21 ? 42 HIS A NE2 1 ATOM 307 N N . GLY A 1 43 ? -12.764 28.626 39.783 1.00 19.16 ? 43 GLY A N 1 ATOM 308 C CA . GLY A 1 43 ? -11.864 29.287 40.695 1.00 17.63 ? 43 GLY A CA 1 ATOM 309 C C . GLY A 1 43 ? -11.193 28.296 41.639 1.00 19.37 ? 43 GLY A C 1 ATOM 310 O O . GLY A 1 43 ? -10.610 28.677 42.635 1.00 21.38 ? 43 GLY A O 1 ATOM 311 N N . ASN A 1 44 ? -11.279 27.015 41.323 1.00 18.38 ? 44 ASN A N 1 ATOM 312 C CA . ASN A 1 44 ? -10.674 25.963 42.133 1.00 21.22 ? 44 ASN A CA 1 ATOM 313 C C . ASN A 1 44 ? -9.273 25.550 41.538 1.00 23.02 ? 44 ASN A C 1 ATOM 314 O O . ASN A 1 44 ? -9.129 25.486 40.324 1.00 24.85 ? 44 ASN A O 1 ATOM 315 C CB . ASN A 1 44 ? -11.672 24.791 42.174 1.00 19.86 ? 44 ASN A CB 1 ATOM 316 C CG . ASN A 1 44 ? -12.939 25.115 42.978 1.00 20.98 ? 44 ASN A CG 1 ATOM 317 O OD1 . ASN A 1 44 ? -12.859 25.819 43.971 1.00 18.58 ? 44 ASN A OD1 1 ATOM 318 N ND2 . ASN A 1 44 ? -14.110 24.609 42.541 1.00 18.39 ? 44 ASN A ND2 1 ATOM 319 N N . PRO A 1 45 ? -8.233 25.292 42.376 1.00 23.91 ? 45 PRO A N 1 ATOM 320 C CA . PRO A 1 45 ? -6.879 24.911 41.925 1.00 22.75 ? 45 PRO A CA 1 ATOM 321 C C . PRO A 1 45 ? -6.818 23.592 41.210 1.00 26.88 ? 45 PRO A C 1 ATOM 322 O O . PRO A 1 45 ? -7.229 22.554 41.718 1.00 28.17 ? 45 PRO A O 1 ATOM 323 C CB . PRO A 1 45 ? -6.070 24.902 43.200 1.00 24.81 ? 45 PRO A CB 1 ATOM 324 C CG . PRO A 1 45 ? -7.093 24.510 44.227 1.00 25.67 ? 45 PRO A CG 1 ATOM 325 C CD . PRO A 1 45 ? -8.284 25.335 43.845 1.00 24.54 ? 45 PRO A CD 1 ATOM 326 N N . VAL A 1 46 ? -6.206 23.628 40.042 1.00 26.20 ? 46 VAL A N 1 ATOM 327 C CA . VAL A 1 46 ? -6.169 22.478 39.186 1.00 23.73 ? 46 VAL A CA 1 ATOM 328 C C . VAL A 1 46 ? -4.720 22.434 38.655 1.00 23.39 ? 46 VAL A C 1 ATOM 329 O O . VAL A 1 46 ? -3.977 23.409 38.781 1.00 19.71 ? 46 VAL A O 1 ATOM 330 C CB . VAL A 1 46 ? -7.299 22.707 38.113 1.00 25.21 ? 46 VAL A CB 1 ATOM 331 C CG1 . VAL A 1 46 ? -6.817 23.517 36.916 1.00 21.88 ? 46 VAL A CG1 1 ATOM 332 C CG2 . VAL A 1 46 ? -7.975 21.462 37.756 1.00 24.79 ? 46 VAL A CG2 1 ATOM 333 N N . LEU A 1 47 ? -4.295 21.289 38.148 1.00 24.40 ? 47 LEU A N 1 ATOM 334 C CA . LEU A 1 47 ? -2.929 21.133 37.658 1.00 25.30 ? 47 LEU A CA 1 ATOM 335 C C . LEU A 1 47 ? -2.754 21.352 36.151 1.00 23.82 ? 47 LEU A C 1 ATOM 336 O O . LEU A 1 47 ? -3.450 20.750 35.342 1.00 22.39 ? 47 LEU A O 1 ATOM 337 C CB . LEU A 1 47 ? -2.399 19.738 38.021 1.00 27.19 ? 47 LEU A CB 1 ATOM 338 C CG . LEU A 1 47 ? -0.952 19.587 37.543 1.00 32.78 ? 47 LEU A CG 1 ATOM 339 C CD1 . LEU A 1 47 ? -0.007 20.471 38.387 1.00 32.55 ? 47 LEU A CD1 1 ATOM 340 C CD2 . LEU A 1 47 ? -0.527 18.140 37.510 1.00 31.73 ? 47 LEU A CD2 1 ATOM 341 N N . ALA A 1 48 ? -1.808 22.213 35.791 1.00 23.31 ? 48 ALA A N 1 ATOM 342 C CA . ALA A 1 48 ? -1.481 22.489 34.404 1.00 21.01 ? 48 ALA A CA 1 ATOM 343 C C . ALA A 1 48 ? -0.131 21.781 34.218 1.00 22.60 ? 48 ALA A C 1 ATOM 344 O O . ALA A 1 48 ? 0.811 22.030 34.967 1.00 21.32 ? 48 ALA A O 1 ATOM 345 C CB . ALA A 1 48 ? -1.344 23.978 34.188 1.00 20.27 ? 48 ALA A CB 1 ATOM 346 N N . ASP A 1 49 ? -0.035 20.890 33.237 1.00 24.38 ? 49 ASP A N 1 ATOM 347 C CA . ASP A 1 49 ? 1.213 20.166 33.028 1.00 25.99 ? 49 ASP A CA 1 ATOM 348 C C . ASP A 1 49 ? 2.041 20.448 31.756 1.00 23.67 ? 49 ASP A C 1 ATOM 349 O O . ASP A 1 49 ? 3.111 19.863 31.591 1.00 22.37 ? 49 ASP A O 1 ATOM 350 C CB . ASP A 1 49 ? 1.016 18.652 33.270 1.00 23.91 ? 49 ASP A CB 1 ATOM 351 C CG . ASP A 1 49 ? 0.158 18.002 32.240 1.00 22.63 ? 49 ASP A CG 1 ATOM 352 O OD1 . ASP A 1 49 ? -0.685 18.663 31.668 1.00 25.57 ? 49 ASP A OD1 1 ATOM 353 O OD2 . ASP A 1 49 ? 0.300 16.793 32.003 1.00 34.10 ? 49 ASP A OD2 1 ATOM 354 N N . ARG A 1 50 ? 1.560 21.299 30.842 1.00 23.89 ? 50 ARG A N 1 ATOM 355 C CA . ARG A 1 50 ? 2.346 21.646 29.649 1.00 20.39 ? 50 ARG A CA 1 ATOM 356 C C . ARG A 1 50 ? 2.129 23.127 29.308 1.00 19.23 ? 50 ARG A C 1 ATOM 357 O O . ARG A 1 50 ? 1.095 23.685 29.634 1.00 17.05 ? 50 ARG A O 1 ATOM 358 C CB . ARG A 1 50 ? 2.096 20.663 28.436 1.00 23.87 ? 50 ARG A CB 1 ATOM 359 C CG . ARG A 1 50 ? 3.014 19.284 28.357 1.00 25.22 ? 50 ARG A CG 1 ATOM 360 C CD . ARG A 1 50 ? 2.913 18.408 26.945 1.00 38.36 ? 50 ARG A CD 1 ATOM 361 N NE . ARG A 1 50 ? 3.199 16.930 27.021 1.00 37.56 ? 50 ARG A NE 1 ATOM 362 C CZ . ARG A 1 50 ? 3.115 15.981 26.040 1.00 29.73 ? 50 ARG A CZ 1 ATOM 363 N NH1 . ARG A 1 50 ? 2.787 16.211 24.799 1.00 18.74 ? 50 ARG A NH1 1 ATOM 364 N NH2 . ARG A 1 50 ? 3.133 14.705 26.380 1.00 31.05 ? 50 ARG A NH2 1 ATOM 365 N N . LEU A 1 51 ? 3.205 23.812 28.911 1.00 20.14 ? 51 LEU A N 1 ATOM 366 C CA . LEU A 1 51 ? 3.172 25.212 28.439 1.00 18.39 ? 51 LEU A CA 1 ATOM 367 C C . LEU A 1 51 ? 3.596 25.094 26.977 1.00 16.08 ? 51 LEU A C 1 ATOM 368 O O . LEU A 1 51 ? 4.680 24.573 26.717 1.00 15.24 ? 51 LEU A O 1 ATOM 369 C CB . LEU A 1 51 ? 4.168 26.156 29.196 1.00 17.96 ? 51 LEU A CB 1 ATOM 370 C CG . LEU A 1 51 ? 4.367 27.685 28.918 1.00 16.27 ? 51 LEU A CG 1 ATOM 371 C CD1 . LEU A 1 51 ? 5.223 27.916 27.704 1.00 17.44 ? 51 LEU A CD1 1 ATOM 372 C CD2 . LEU A 1 51 ? 3.079 28.444 28.730 1.00 12.34 ? 51 LEU A CD2 1 ATOM 373 N N . PHE A 1 52 ? 2.714 25.448 26.038 1.00 17.04 ? 52 PHE A N 1 ATOM 374 C CA . PHE A 1 52 ? 3.048 25.403 24.601 1.00 16.45 ? 52 PHE A CA 1 ATOM 375 C C . PHE A 1 52 ? 3.207 26.828 24.076 1.00 18.02 ? 52 PHE A C 1 ATOM 376 O O . PHE A 1 52 ? 2.401 27.698 24.362 1.00 17.69 ? 52 PHE A O 1 ATOM 377 C CB . PHE A 1 52 ? 1.963 24.730 23.759 1.00 13.56 ? 52 PHE A CB 1 ATOM 378 C CG . PHE A 1 52 ? 1.584 23.353 24.235 1.00 18.43 ? 52 PHE A CG 1 ATOM 379 C CD1 . PHE A 1 52 ? 2.400 22.281 24.025 1.00 17.53 ? 52 PHE A CD1 1 ATOM 380 C CD2 . PHE A 1 52 ? 0.381 23.122 24.859 1.00 17.11 ? 52 PHE A CD2 1 ATOM 381 C CE1 . PHE A 1 52 ? 2.011 20.998 24.441 1.00 15.94 ? 52 PHE A CE1 1 ATOM 382 C CE2 . PHE A 1 52 ? 0.014 21.836 25.262 1.00 14.21 ? 52 PHE A CE2 1 ATOM 383 C CZ . PHE A 1 52 ? 0.834 20.800 25.050 1.00 14.97 ? 52 PHE A CZ 1 ATOM 384 N N . HIS A 1 53 ? 4.311 27.079 23.381 1.00 19.51 ? 53 HIS A N 1 ATOM 385 C CA . HIS A 1 53 ? 4.574 28.369 22.758 1.00 18.14 ? 53 HIS A CA 1 ATOM 386 C C . HIS A 1 53 ? 4.340 27.975 21.303 1.00 18.08 ? 53 HIS A C 1 ATOM 387 O O . HIS A 1 53 ? 5.165 27.301 20.738 1.00 19.72 ? 53 HIS A O 1 ATOM 388 C CB . HIS A 1 53 ? 6.018 28.783 22.944 1.00 15.14 ? 53 HIS A CB 1 ATOM 389 C CG . HIS A 1 53 ? 6.347 30.026 22.210 1.00 17.50 ? 53 HIS A CG 1 ATOM 390 N ND1 . HIS A 1 53 ? 6.038 30.191 20.878 1.00 21.85 ? 53 HIS A ND1 1 ATOM 391 C CD2 . HIS A 1 53 ? 6.857 31.206 22.628 1.00 16.47 ? 53 HIS A CD2 1 ATOM 392 C CE1 . HIS A 1 53 ? 6.329 31.425 20.512 1.00 18.33 ? 53 HIS A CE1 1 ATOM 393 N NE2 . HIS A 1 53 ? 6.827 32.060 21.552 1.00 18.05 ? 53 HIS A NE2 1 ATOM 394 N N . SER A 1 54 ? 3.216 28.349 20.714 1.00 19.94 ? 54 SER A N 1 ATOM 395 C CA . SER A 1 54 ? 2.906 27.926 19.361 1.00 25.42 ? 54 SER A CA 1 ATOM 396 C C . SER A 1 54 ? 3.391 28.802 18.198 1.00 28.26 ? 54 SER A C 1 ATOM 397 O O . SER A 1 54 ? 2.867 28.708 17.085 1.00 32.69 ? 54 SER A O 1 ATOM 398 C CB . SER A 1 54 ? 1.386 27.704 19.244 1.00 29.93 ? 54 SER A CB 1 ATOM 399 O OG . SER A 1 54 ? 0.797 27.287 20.474 1.00 37.31 ? 54 SER A OG 1 ATOM 400 N N . GLY A 1 55 ? 4.400 29.628 18.413 1.00 28.96 ? 55 GLY A N 1 ATOM 401 C CA . GLY A 1 55 ? 4.861 30.462 17.325 1.00 26.84 ? 55 GLY A CA 1 ATOM 402 C C . GLY A 1 55 ? 3.982 31.690 17.229 1.00 27.87 ? 55 GLY A C 1 ATOM 403 O O . GLY A 1 55 ? 3.270 31.994 18.167 1.00 28.42 ? 55 GLY A O 1 ATOM 404 N N . GLU A 1 56 ? 4.069 32.425 16.127 1.00 30.48 ? 56 GLU A N 1 ATOM 405 C CA . GLU A 1 56 ? 3.287 33.638 15.938 1.00 33.38 ? 56 GLU A CA 1 ATOM 406 C C . GLU A 1 56 ? 2.135 33.387 14.998 1.00 32.15 ? 56 GLU A C 1 ATOM 407 O O . GLU A 1 56 ? 2.270 32.702 13.976 1.00 31.52 ? 56 GLU A O 1 ATOM 408 C CB . GLU A 1 56 ? 4.151 34.756 15.397 1.00 38.99 ? 56 GLU A CB 1 ATOM 409 C CG . GLU A 1 56 ? 5.191 35.269 16.381 1.00 52.20 ? 56 GLU A CG 1 ATOM 410 C CD . GLU A 1 56 ? 5.990 36.469 15.828 1.00 60.69 ? 56 GLU A CD 1 ATOM 411 O OE1 . GLU A 1 56 ? 6.707 36.288 14.798 1.00 64.64 ? 56 GLU A OE1 1 ATOM 412 O OE2 . GLU A 1 56 ? 5.898 37.584 16.424 1.00 63.85 ? 56 GLU A OE2 1 ATOM 413 N N . HIS A 1 57 ? 0.977 33.912 15.373 1.00 31.06 ? 57 HIS A N 1 ATOM 414 C CA . HIS A 1 57 ? -0.233 33.727 14.598 1.00 28.40 ? 57 HIS A CA 1 ATOM 415 C C . HIS A 1 57 ? -1.069 34.955 14.737 1.00 26.90 ? 57 HIS A C 1 ATOM 416 O O . HIS A 1 57 ? -0.861 35.752 15.643 1.00 28.31 ? 57 HIS A O 1 ATOM 417 C CB . HIS A 1 57 ? -1.042 32.552 15.149 1.00 29.01 ? 57 HIS A CB 1 ATOM 418 C CG . HIS A 1 57 ? -0.327 31.257 15.061 1.00 30.54 ? 57 HIS A CG 1 ATOM 419 N ND1 . HIS A 1 57 ? -0.146 30.597 13.867 1.00 38.27 ? 57 HIS A ND1 1 ATOM 420 C CD2 . HIS A 1 57 ? 0.369 30.558 15.985 1.00 34.88 ? 57 HIS A CD2 1 ATOM 421 C CE1 . HIS A 1 57 ? 0.643 29.555 14.056 1.00 36.91 ? 57 HIS A CE1 1 ATOM 422 N NE2 . HIS A 1 57 ? 0.970 29.509 15.333 1.00 33.13 ? 57 HIS A NE2 1 ATOM 423 N N . PRO A 1 58 ? -2.015 35.145 13.810 1.00 28.33 ? 58 PRO A N 1 ATOM 424 C CA . PRO A 1 58 ? -2.941 36.282 13.797 1.00 25.72 ? 58 PRO A CA 1 ATOM 425 C C . PRO A 1 58 ? -3.702 36.135 15.114 1.00 25.53 ? 58 PRO A C 1 ATOM 426 O O . PRO A 1 58 ? -4.146 35.026 15.466 1.00 23.59 ? 58 PRO A O 1 ATOM 427 C CB . PRO A 1 58 ? -3.868 35.954 12.637 1.00 23.92 ? 58 PRO A CB 1 ATOM 428 C CG . PRO A 1 58 ? -3.053 35.081 11.777 1.00 27.32 ? 58 PRO A CG 1 ATOM 429 C CD . PRO A 1 58 ? -2.316 34.211 12.714 1.00 27.55 ? 58 PRO A CD 1 ATOM 430 N N . VAL A 1 59 ? -4.012 37.270 15.715 1.00 24.90 ? 59 VAL A N 1 ATOM 431 C CA . VAL A 1 59 ? -4.624 37.303 17.008 1.00 25.81 ? 59 VAL A CA 1 ATOM 432 C C . VAL A 1 59 ? -5.701 38.423 16.939 1.00 28.31 ? 59 VAL A C 1 ATOM 433 O O . VAL A 1 59 ? -5.641 39.281 16.027 1.00 24.90 ? 59 VAL A O 1 ATOM 434 C CB . VAL A 1 59 ? -3.424 37.544 17.960 1.00 27.00 ? 59 VAL A CB 1 ATOM 435 C CG1 . VAL A 1 59 ? -3.387 38.928 18.492 1.00 31.33 ? 59 VAL A CG1 1 ATOM 436 C CG2 . VAL A 1 59 ? -3.296 36.457 18.980 1.00 26.93 ? 59 VAL A CG2 1 ATOM 437 N N . TYR A 1 60 ? -6.747 38.292 17.783 1.00 27.11 ? 60 TYR A N 1 ATOM 438 C CA . TYR A 1 60 ? -7.907 39.216 17.909 1.00 23.37 ? 60 TYR A CA 1 ATOM 439 C C . TYR A 1 60 ? -8.187 39.554 19.372 1.00 25.12 ? 60 TYR A C 1 ATOM 440 O O . TYR A 1 60 ? -8.161 38.698 20.259 1.00 26.92 ? 60 TYR A O 1 ATOM 441 C CB . TYR A 1 60 ? -9.167 38.607 17.310 1.00 22.53 ? 60 TYR A CB 1 ATOM 442 C CG . TYR A 1 60 ? -8.882 37.987 15.995 1.00 26.48 ? 60 TYR A CG 1 ATOM 443 C CD1 . TYR A 1 60 ? -8.282 36.743 15.923 1.00 31.45 ? 60 TYR A CD1 1 ATOM 444 C CD2 . TYR A 1 60 ? -9.098 38.685 14.819 1.00 34.55 ? 60 TYR A CD2 1 ATOM 445 C CE1 . TYR A 1 60 ? -7.887 36.198 14.719 1.00 38.18 ? 60 TYR A CE1 1 ATOM 446 C CE2 . TYR A 1 60 ? -8.709 38.155 13.582 1.00 39.52 ? 60 TYR A CE2 1 ATOM 447 C CZ . TYR A 1 60 ? -8.101 36.905 13.537 1.00 43.42 ? 60 TYR A CZ 1 ATOM 448 O OH . TYR A 1 60 ? -7.713 36.340 12.319 1.00 49.54 ? 60 TYR A OH 1 ATOM 449 N N . ALA A 1 61 ? -8.498 40.812 19.619 1.00 25.41 ? 61 ALA A N 1 ATOM 450 C CA . ALA A 1 61 ? -8.753 41.300 20.948 1.00 20.80 ? 61 ALA A CA 1 ATOM 451 C C . ALA A 1 61 ? -10.226 41.304 21.273 1.00 22.60 ? 61 ALA A C 1 ATOM 452 O O . ALA A 1 61 ? -11.001 41.969 20.582 1.00 23.89 ? 61 ALA A O 1 ATOM 453 C CB . ALA A 1 61 ? -8.202 42.696 21.041 1.00 20.13 ? 61 ALA A CB 1 ATOM 454 N N . VAL A 1 62 ? -10.631 40.561 22.302 1.00 20.34 ? 62 VAL A N 1 ATOM 455 C CA . VAL A 1 62 ? -12.018 40.552 22.702 1.00 17.10 ? 62 VAL A CA 1 ATOM 456 C C . VAL A 1 62 ? -12.100 41.491 23.852 1.00 21.10 ? 62 VAL A C 1 ATOM 457 O O . VAL A 1 62 ? -11.363 41.344 24.798 1.00 24.65 ? 62 VAL A O 1 ATOM 458 C CB . VAL A 1 62 ? -12.446 39.236 23.235 1.00 19.32 ? 62 VAL A CB 1 ATOM 459 C CG1 . VAL A 1 62 ? -13.887 39.331 23.715 1.00 19.24 ? 62 VAL A CG1 1 ATOM 460 C CG2 . VAL A 1 62 ? -12.263 38.173 22.188 1.00 19.01 ? 62 VAL A CG2 1 ATOM 461 N N . ARG A 1 63 ? -12.942 42.509 23.739 1.00 26.63 ? 63 ARG A N 1 ATOM 462 C CA . ARG A 1 63 ? -13.135 43.529 24.778 1.00 27.71 ? 63 ARG A CA 1 ATOM 463 C C . ARG A 1 63 ? -14.544 43.497 25.302 1.00 25.96 ? 63 ARG A C 1 ATOM 464 O O . ARG A 1 63 ? -15.512 43.402 24.555 1.00 27.37 ? 63 ARG A O 1 ATOM 465 C CB . ARG A 1 63 ? -12.854 44.916 24.229 1.00 30.61 ? 63 ARG A CB 1 ATOM 466 C CG . ARG A 1 63 ? -11.515 44.990 23.624 1.00 36.70 ? 63 ARG A CG 1 ATOM 467 C CD . ARG A 1 63 ? -11.544 45.477 22.187 1.00 41.05 ? 63 ARG A CD 1 ATOM 468 N NE . ARG A 1 63 ? -10.165 45.698 21.784 1.00 43.17 ? 63 ARG A NE 1 ATOM 469 C CZ . ARG A 1 63 ? -9.251 46.328 22.522 1.00 41.28 ? 63 ARG A CZ 1 ATOM 470 N NH1 . ARG A 1 63 ? -9.555 46.849 23.712 1.00 42.65 ? 63 ARG A NH1 1 ATOM 471 N NH2 . ARG A 1 63 ? -7.981 46.305 22.136 1.00 44.73 ? 63 ARG A NH2 1 ATOM 472 N N . THR A 1 64 ? -14.642 43.700 26.590 1.00 25.79 ? 64 THR A N 1 ATOM 473 C CA . THR A 1 64 ? -15.886 43.644 27.315 1.00 26.54 ? 64 THR A CA 1 ATOM 474 C C . THR A 1 64 ? -16.385 45.053 27.639 1.00 30.14 ? 64 THR A C 1 ATOM 475 O O . THR A 1 64 ? -15.614 46.017 27.731 1.00 31.64 ? 64 THR A O 1 ATOM 476 C CB . THR A 1 64 ? -15.614 42.795 28.531 1.00 24.19 ? 64 THR A CB 1 ATOM 477 O OG1 . THR A 1 64 ? -16.374 41.603 28.459 1.00 31.14 ? 64 THR A OG1 1 ATOM 478 C CG2 . THR A 1 64 ? -15.791 43.488 29.760 1.00 17.49 ? 64 THR A CG2 1 ATOM 479 N N . VAL A 1 65 ? -17.691 45.178 27.784 1.00 31.80 ? 65 VAL A N 1 ATOM 480 C CA . VAL A 1 65 ? -18.319 46.460 28.067 1.00 33.11 ? 65 VAL A CA 1 ATOM 481 C C . VAL A 1 65 ? -17.730 47.127 29.328 1.00 33.99 ? 65 VAL A C 1 ATOM 482 O O . VAL A 1 65 ? -17.764 48.346 29.466 1.00 34.74 ? 65 VAL A O 1 ATOM 483 C CB . VAL A 1 65 ? -19.827 46.223 28.171 1.00 34.37 ? 65 VAL A CB 1 ATOM 484 C CG1 . VAL A 1 65 ? -20.436 46.878 29.410 1.00 38.39 ? 65 VAL A CG1 1 ATOM 485 C CG2 . VAL A 1 65 ? -20.479 46.641 26.868 1.00 36.25 ? 65 VAL A CG2 1 ATOM 486 N N . GLU A 1 66 ? -17.188 46.295 30.227 1.00 33.94 ? 66 GLU A N 1 ATOM 487 C CA . GLU A 1 66 ? -16.586 46.705 31.489 1.00 27.88 ? 66 GLU A CA 1 ATOM 488 C C . GLU A 1 66 ? -15.131 47.067 31.285 1.00 28.15 ? 66 GLU A C 1 ATOM 489 O O . GLU A 1 66 ? -14.507 47.570 32.200 1.00 29.79 ? 66 GLU A O 1 ATOM 490 C CB . GLU A 1 66 ? -16.642 45.562 32.505 1.00 26.12 ? 66 GLU A CB 1 ATOM 491 C CG . GLU A 1 66 ? -18.022 45.117 32.884 1.00 27.33 ? 66 GLU A CG 1 ATOM 492 C CD . GLU A 1 66 ? -18.670 44.090 31.957 1.00 27.15 ? 66 GLU A CD 1 ATOM 493 O OE1 . GLU A 1 66 ? -18.144 43.734 30.906 1.00 29.61 ? 66 GLU A OE1 1 ATOM 494 O OE2 . GLU A 1 66 ? -19.769 43.631 32.283 1.00 31.12 ? 66 GLU A OE2 1 ATOM 495 N N . GLY A 1 67 ? -14.591 46.764 30.106 1.00 27.64 ? 67 GLY A N 1 ATOM 496 C CA . GLY A 1 67 ? -13.198 47.033 29.802 1.00 25.81 ? 67 GLY A CA 1 ATOM 497 C C . GLY A 1 67 ? -12.279 45.808 29.844 1.00 27.65 ? 67 GLY A C 1 ATOM 498 O O . GLY A 1 67 ? -11.090 45.938 29.569 1.00 28.71 ? 67 GLY A O 1 ATOM 499 N N . LEU A 1 68 ? -12.786 44.633 30.223 1.00 27.33 ? 68 LEU A N 1 ATOM 500 C CA . LEU A 1 68 ? -11.958 43.412 30.267 1.00 25.08 ? 68 LEU A CA 1 ATOM 501 C C . LEU A 1 68 ? -11.546 43.111 28.852 1.00 24.53 ? 68 LEU A C 1 ATOM 502 O O . LEU A 1 68 ? -12.293 43.411 27.931 1.00 27.66 ? 68 LEU A O 1 ATOM 503 C CB . LEU A 1 68 ? -12.784 42.242 30.798 1.00 22.10 ? 68 LEU A CB 1 ATOM 504 C CG . LEU A 1 68 ? -13.387 42.537 32.154 1.00 22.94 ? 68 LEU A CG 1 ATOM 505 C CD1 . LEU A 1 68 ? -14.353 41.502 32.604 1.00 24.97 ? 68 LEU A CD1 1 ATOM 506 C CD2 . LEU A 1 68 ? -12.249 42.586 33.103 1.00 29.42 ? 68 LEU A CD2 1 ATOM 507 N N . ARG A 1 69 ? -10.411 42.464 28.653 1.00 23.20 ? 69 ARG A N 1 ATOM 508 C CA . ARG A 1 69 ? -9.991 42.165 27.291 1.00 24.50 ? 69 ARG A CA 1 ATOM 509 C C . ARG A 1 69 ? -9.125 40.920 27.309 1.00 23.69 ? 69 ARG A C 1 ATOM 510 O O . ARG A 1 69 ? -8.478 40.656 28.312 1.00 24.19 ? 69 ARG A O 1 ATOM 511 C CB . ARG A 1 69 ? -9.155 43.345 26.755 1.00 25.12 ? 69 ARG A CB 1 ATOM 512 C CG . ARG A 1 69 ? -8.355 43.143 25.439 1.00 31.77 ? 69 ARG A CG 1 ATOM 513 C CD . ARG A 1 69 ? -7.015 43.960 25.459 1.00 45.06 ? 69 ARG A CD 1 ATOM 514 N NE . ARG A 1 69 ? -7.040 45.041 26.486 1.00 60.55 ? 69 ARG A NE 1 ATOM 515 C CZ . ARG A 1 69 ? -6.858 46.370 26.279 1.00 64.88 ? 69 ARG A CZ 1 ATOM 516 N NH1 . ARG A 1 69 ? -6.594 46.847 25.061 1.00 67.75 ? 69 ARG A NH1 1 ATOM 517 N NH2 . ARG A 1 69 ? -7.095 47.257 27.265 1.00 64.29 ? 69 ARG A NH2 1 ATOM 518 N N . VAL A 1 70 ? -9.174 40.105 26.266 1.00 18.55 ? 70 VAL A N 1 ATOM 519 C CA . VAL A 1 70 ? -8.261 38.983 26.163 1.00 18.94 ? 70 VAL A CA 1 ATOM 520 C C . VAL A 1 70 ? -7.981 38.895 24.685 1.00 21.87 ? 70 VAL A C 1 ATOM 521 O O . VAL A 1 70 ? -8.852 39.197 23.858 1.00 22.28 ? 70 VAL A O 1 ATOM 522 C CB . VAL A 1 70 ? -8.770 37.627 26.763 1.00 19.60 ? 70 VAL A CB 1 ATOM 523 C CG1 . VAL A 1 70 ? -9.929 37.057 25.957 1.00 16.57 ? 70 VAL A CG1 1 ATOM 524 C CG2 . VAL A 1 70 ? -7.573 36.633 26.869 1.00 17.98 ? 70 VAL A CG2 1 ATOM 525 N N . THR A 1 71 ? -6.737 38.570 24.347 1.00 21.89 ? 71 THR A N 1 ATOM 526 C CA . THR A 1 71 ? -6.339 38.493 22.947 1.00 20.01 ? 71 THR A CA 1 ATOM 527 C C . THR A 1 71 ? -5.864 37.098 22.605 1.00 20.89 ? 71 THR A C 1 ATOM 528 O O . THR A 1 71 ? -4.972 36.590 23.246 1.00 25.88 ? 71 THR A O 1 ATOM 529 C CB . THR A 1 71 ? -5.208 39.468 22.735 1.00 21.80 ? 71 THR A CB 1 ATOM 530 O OG1 . THR A 1 71 ? -5.542 40.724 23.367 1.00 23.58 ? 71 THR A OG1 1 ATOM 531 C CG2 . THR A 1 71 ? -4.946 39.656 21.262 1.00 19.41 ? 71 THR A CG2 1 ATOM 532 N N . GLY A 1 72 ? -6.452 36.463 21.609 1.00 20.94 ? 72 GLY A N 1 ATOM 533 C CA . GLY A 1 72 ? -6.041 35.116 21.282 1.00 17.70 ? 72 GLY A CA 1 ATOM 534 C C . GLY A 1 72 ? -6.339 34.845 19.840 1.00 17.97 ? 72 GLY A C 1 ATOM 535 O O . GLY A 1 72 ? -6.860 35.695 19.127 1.00 18.33 ? 72 GLY A O 1 ATOM 536 N N . THR A 1 73 ? -6.059 33.637 19.409 1.00 17.32 ? 73 THR A N 1 ATOM 537 C CA . THR A 1 73 ? -6.262 33.294 18.032 1.00 19.01 ? 73 THR A CA 1 ATOM 538 C C . THR A 1 73 ? -7.742 33.043 17.652 1.00 22.10 ? 73 THR A C 1 ATOM 539 O O . THR A 1 73 ? -8.610 32.860 18.534 1.00 26.26 ? 73 THR A O 1 ATOM 540 C CB . THR A 1 73 ? -5.392 32.115 17.741 1.00 20.96 ? 73 THR A CB 1 ATOM 541 O OG1 . THR A 1 73 ? -5.726 31.079 18.661 1.00 22.00 ? 73 THR A OG1 1 ATOM 542 C CG2 . THR A 1 73 ? -3.935 32.490 17.990 1.00 20.88 ? 73 THR A CG2 1 ATOM 543 N N . ALA A 1 74 ? -8.029 33.044 16.355 1.00 17.61 ? 74 ALA A N 1 ATOM 544 C CA . ALA A 1 74 ? -9.378 32.842 15.856 1.00 16.77 ? 74 ALA A CA 1 ATOM 545 C C . ALA A 1 74 ? -10.108 31.615 16.376 1.00 18.95 ? 74 ALA A C 1 ATOM 546 O O . ALA A 1 74 ? -11.323 31.632 16.557 1.00 18.89 ? 74 ALA A O 1 ATOM 547 C CB . ALA A 1 74 ? -9.333 32.770 14.378 1.00 16.17 ? 74 ALA A CB 1 ATOM 548 N N . ASN A 1 75 ? -9.402 30.499 16.465 1.00 19.20 ? 75 ASN A N 1 ATOM 549 C CA . ASN A 1 75 ? -9.995 29.273 16.961 1.00 17.49 ? 75 ASN A CA 1 ATOM 550 C C . ASN A 1 75 ? -9.807 29.075 18.493 1.00 19.52 ? 75 ASN A C 1 ATOM 551 O O . ASN A 1 75 ? -9.932 27.973 18.992 1.00 20.92 ? 75 ASN A O 1 ATOM 552 C CB . ASN A 1 75 ? -9.402 28.100 16.229 1.00 22.99 ? 75 ASN A CB 1 ATOM 553 C CG . ASN A 1 75 ? -7.885 27.984 16.431 1.00 31.75 ? 75 ASN A CG 1 ATOM 554 O OD1 . ASN A 1 75 ? -7.320 26.883 16.319 1.00 39.91 ? 75 ASN A OD1 1 ATOM 555 N ND2 . ASN A 1 75 ? -7.218 29.094 16.752 1.00 29.81 ? 75 ASN A ND2 1 ATOM 556 N N . HIS A 1 76 ? -9.505 30.124 19.250 1.00 19.33 ? 76 HIS A N 1 ATOM 557 C CA . HIS A 1 76 ? -9.355 29.934 20.676 1.00 16.25 ? 76 HIS A CA 1 ATOM 558 C C . HIS A 1 76 ? -10.731 30.001 21.289 1.00 16.68 ? 76 HIS A C 1 ATOM 559 O O . HIS A 1 76 ? -11.454 30.945 21.036 1.00 19.03 ? 76 HIS A O 1 ATOM 560 C CB . HIS A 1 76 ? -8.552 31.035 21.278 1.00 14.58 ? 76 HIS A CB 1 ATOM 561 C CG . HIS A 1 76 ? -8.370 30.851 22.752 1.00 17.66 ? 76 HIS A CG 1 ATOM 562 N ND1 . HIS A 1 76 ? -7.770 29.731 23.286 1.00 19.15 ? 76 HIS A ND1 1 ATOM 563 C CD2 . HIS A 1 76 ? -8.739 31.620 23.799 1.00 16.39 ? 76 HIS A CD2 1 ATOM 564 C CE1 . HIS A 1 76 ? -7.779 29.812 24.600 1.00 17.94 ? 76 HIS A CE1 1 ATOM 565 N NE2 . HIS A 1 76 ? -8.365 30.954 24.936 1.00 20.12 ? 76 HIS A NE2 1 ATOM 566 N N . PRO A 1 77 ? -11.122 28.999 22.085 1.00 17.82 ? 77 PRO A N 1 ATOM 567 C CA . PRO A 1 77 ? -12.434 28.932 22.763 1.00 16.82 ? 77 PRO A CA 1 ATOM 568 C C . PRO A 1 77 ? -12.525 29.652 24.128 1.00 17.23 ? 77 PRO A C 1 ATOM 569 O O . PRO A 1 77 ? -11.682 29.447 24.993 1.00 16.88 ? 77 PRO A O 1 ATOM 570 C CB . PRO A 1 77 ? -12.640 27.422 22.964 1.00 18.44 ? 77 PRO A CB 1 ATOM 571 C CG . PRO A 1 77 ? -11.592 26.770 22.085 1.00 19.50 ? 77 PRO A CG 1 ATOM 572 C CD . PRO A 1 77 ? -10.445 27.690 22.121 1.00 14.37 ? 77 PRO A CD 1 ATOM 573 N N . LEU A 1 78 ? -13.561 30.462 24.309 1.00 18.71 ? 78 LEU A N 1 ATOM 574 C CA . LEU A 1 78 ? -13.816 31.218 25.534 1.00 16.38 ? 78 LEU A CA 1 ATOM 575 C C . LEU A 1 78 ? -15.209 30.754 25.929 1.00 17.01 ? 78 LEU A C 1 ATOM 576 O O . LEU A 1 78 ? -16.023 30.564 25.033 1.00 16.07 ? 78 LEU A O 1 ATOM 577 C CB . LEU A 1 78 ? -13.862 32.734 25.256 1.00 15.45 ? 78 LEU A CB 1 ATOM 578 C CG . LEU A 1 78 ? -12.558 33.473 24.941 1.00 13.72 ? 78 LEU A CG 1 ATOM 579 C CD1 . LEU A 1 78 ? -12.861 34.953 24.792 1.00 12.29 ? 78 LEU A CD1 1 ATOM 580 C CD2 . LEU A 1 78 ? -11.611 33.299 26.110 1.00 12.54 ? 78 LEU A CD2 1 ATOM 581 N N . LEU A 1 79 ? -15.488 30.567 27.225 1.00 15.08 ? 79 LEU A N 1 ATOM 582 C CA . LEU A 1 79 ? -16.809 30.097 27.664 1.00 14.71 ? 79 LEU A CA 1 ATOM 583 C C . LEU A 1 79 ? -17.740 31.272 27.652 1.00 17.42 ? 79 LEU A C 1 ATOM 584 O O . LEU A 1 79 ? -17.419 32.340 28.190 1.00 17.32 ? 79 LEU A O 1 ATOM 585 C CB . LEU A 1 79 ? -16.746 29.489 29.065 1.00 11.45 ? 79 LEU A CB 1 ATOM 586 C CG . LEU A 1 79 ? -17.959 28.655 29.465 1.00 11.72 ? 79 LEU A CG 1 ATOM 587 C CD1 . LEU A 1 79 ? -17.992 27.410 28.656 1.00 10.38 ? 79 LEU A CD1 1 ATOM 588 C CD2 . LEU A 1 79 ? -17.828 28.307 30.912 1.00 12.30 ? 79 LEU A CD2 1 ATOM 589 N N . CYS A 1 80 ? -18.875 31.088 26.979 1.00 20.64 ? 80 CYS A N 1 ATOM 590 C CA . CYS A 1 80 ? -19.875 32.146 26.815 1.00 19.38 ? 80 CYS A CA 1 ATOM 591 C C . CYS A 1 80 ? -21.198 31.646 27.321 1.00 21.89 ? 80 CYS A C 1 ATOM 592 O O . CYS A 1 80 ? -21.354 30.431 27.525 1.00 18.94 ? 80 CYS A O 1 ATOM 593 C CB . CYS A 1 80 ? -20.005 32.500 25.327 1.00 18.62 ? 80 CYS A CB 1 ATOM 594 S SG . CYS A 1 80 ? -18.562 33.362 24.705 1.00 20.58 ? 80 CYS A SG 1 ATOM 595 N N . LEU A 1 81 ? -22.089 32.590 27.652 1.00 23.65 ? 81 LEU A N 1 ATOM 596 C CA . LEU A 1 81 ? -23.446 32.263 28.111 1.00 21.96 ? 81 LEU A CA 1 ATOM 597 C C . LEU A 1 81 ? -24.303 32.377 26.843 1.00 21.24 ? 81 LEU A C 1 ATOM 598 O O . LEU A 1 81 ? -24.522 33.471 26.351 1.00 19.15 ? 81 LEU A O 1 ATOM 599 C CB . LEU A 1 81 ? -23.947 33.247 29.176 1.00 20.08 ? 81 LEU A CB 1 ATOM 600 C CG . LEU A 1 81 ? -25.410 33.035 29.634 1.00 21.37 ? 81 LEU A CG 1 ATOM 601 C CD1 . LEU A 1 81 ? -25.533 31.744 30.423 1.00 24.64 ? 81 LEU A CD1 1 ATOM 602 C CD2 . LEU A 1 81 ? -25.881 34.190 30.448 1.00 18.81 ? 81 LEU A CD2 1 ATOM 603 N N . VAL A 1 82 ? -24.754 31.247 26.317 1.00 17.75 ? 82 VAL A N 1 ATOM 604 C CA . VAL A 1 82 ? -25.516 31.231 25.089 1.00 20.03 ? 82 VAL A CA 1 ATOM 605 C C . VAL A 1 82 ? -26.978 30.834 25.306 1.00 24.27 ? 82 VAL A C 1 ATOM 606 O O . VAL A 1 82 ? -27.279 29.987 26.153 1.00 25.51 ? 82 VAL A O 1 ATOM 607 C CB . VAL A 1 82 ? -24.798 30.262 24.083 1.00 22.37 ? 82 VAL A CB 1 ATOM 608 C CG1 . VAL A 1 82 ? -25.588 30.041 22.768 1.00 15.22 ? 82 VAL A CG1 1 ATOM 609 C CG2 . VAL A 1 82 ? -23.402 30.812 23.793 1.00 22.44 ? 82 VAL A CG2 1 ATOM 610 N N . ASP A 1 83 ? -27.898 31.466 24.578 1.00 25.76 ? 83 ASP A N 1 ATOM 611 C CA . ASP A 1 83 ? -29.314 31.122 24.690 1.00 26.89 ? 83 ASP A CA 1 ATOM 612 C C . ASP A 1 83 ? -29.566 29.961 23.715 1.00 28.09 ? 83 ASP A C 1 ATOM 613 O O . ASP A 1 83 ? -29.450 30.136 22.497 1.00 28.06 ? 83 ASP A O 1 ATOM 614 C CB . ASP A 1 83 ? -30.170 32.334 24.312 1.00 33.71 ? 83 ASP A CB 1 ATOM 615 C CG . ASP A 1 83 ? -31.652 32.156 24.649 1.00 39.07 ? 83 ASP A CG 1 ATOM 616 O OD1 . ASP A 1 83 ? -32.232 31.137 24.244 1.00 43.57 ? 83 ASP A OD1 1 ATOM 617 O OD2 . ASP A 1 83 ? -32.254 33.041 25.309 1.00 44.64 ? 83 ASP A OD2 1 ATOM 618 N N . VAL A 1 84 ? -29.769 28.757 24.249 1.00 27.42 ? 84 VAL A N 1 ATOM 619 C CA . VAL A 1 84 ? -30.068 27.586 23.416 1.00 29.49 ? 84 VAL A CA 1 ATOM 620 C C . VAL A 1 84 ? -31.554 27.224 23.593 1.00 30.22 ? 84 VAL A C 1 ATOM 621 O O . VAL A 1 84 ? -31.937 26.618 24.592 1.00 33.36 ? 84 VAL A O 1 ATOM 622 C CB . VAL A 1 84 ? -29.190 26.341 23.777 1.00 27.73 ? 84 VAL A CB 1 ATOM 623 C CG1 . VAL A 1 84 ? -29.674 25.105 23.022 1.00 23.08 ? 84 VAL A CG1 1 ATOM 624 C CG2 . VAL A 1 84 ? -27.719 26.604 23.469 1.00 22.80 ? 84 VAL A CG2 1 ATOM 625 N N . ALA A 1 85 ? -32.398 27.704 22.685 1.00 31.28 ? 85 ALA A N 1 ATOM 626 C CA . ALA A 1 85 ? -33.848 27.424 22.717 1.00 32.16 ? 85 ALA A CA 1 ATOM 627 C C . ALA A 1 85 ? -34.492 27.803 24.028 1.00 31.97 ? 85 ALA A C 1 ATOM 628 O O . ALA A 1 85 ? -35.323 27.052 24.571 1.00 35.02 ? 85 ALA A O 1 ATOM 629 C CB . ALA A 1 85 ? -34.133 25.933 22.420 1.00 31.78 ? 85 ALA A CB 1 ATOM 630 N N . GLY A 1 86 ? -34.077 28.940 24.565 1.00 29.97 ? 86 GLY A N 1 ATOM 631 C CA . GLY A 1 86 ? -34.656 29.387 25.810 1.00 26.70 ? 86 GLY A CA 1 ATOM 632 C C . GLY A 1 86 ? -33.899 29.006 27.058 1.00 28.03 ? 86 GLY A C 1 ATOM 633 O O . GLY A 1 86 ? -34.263 29.463 28.154 1.00 29.87 ? 86 GLY A O 1 ATOM 634 N N . VAL A 1 87 ? -32.927 28.108 26.948 1.00 26.42 ? 87 VAL A N 1 ATOM 635 C CA . VAL A 1 87 ? -32.174 27.792 28.128 1.00 25.77 ? 87 VAL A CA 1 ATOM 636 C C . VAL A 1 87 ? -30.766 28.413 28.087 1.00 27.77 ? 87 VAL A C 1 ATOM 637 O O . VAL A 1 87 ? -30.071 28.344 27.066 1.00 24.36 ? 87 VAL A O 1 ATOM 638 C CB . VAL A 1 87 ? -32.299 26.301 28.558 1.00 28.12 ? 87 VAL A CB 1 ATOM 639 C CG1 . VAL A 1 87 ? -32.922 25.453 27.507 1.00 30.47 ? 87 VAL A CG1 1 ATOM 640 C CG2 . VAL A 1 87 ? -31.020 25.756 29.010 1.00 26.79 ? 87 VAL A CG2 1 ATOM 641 N N . PRO A 1 88 ? -30.436 29.244 29.117 1.00 28.31 ? 88 PRO A N 1 ATOM 642 C CA . PRO A 1 88 ? -29.108 29.866 29.141 1.00 23.30 ? 88 PRO A CA 1 ATOM 643 C C . PRO A 1 88 ? -28.123 28.719 29.387 1.00 23.00 ? 88 PRO A C 1 ATOM 644 O O . PRO A 1 88 ? -28.203 28.001 30.372 1.00 24.27 ? 88 PRO A O 1 ATOM 645 C CB . PRO A 1 88 ? -29.196 30.822 30.336 1.00 24.32 ? 88 PRO A CB 1 ATOM 646 C CG . PRO A 1 88 ? -30.717 30.987 30.608 1.00 23.97 ? 88 PRO A CG 1 ATOM 647 C CD . PRO A 1 88 ? -31.210 29.603 30.335 1.00 25.30 ? 88 PRO A CD 1 ATOM 648 N N . THR A 1 89 ? -27.275 28.478 28.418 1.00 21.12 ? 89 THR A N 1 ATOM 649 C CA . THR A 1 89 ? -26.317 27.403 28.480 1.00 20.90 ? 89 THR A CA 1 ATOM 650 C C . THR A 1 89 ? -24.889 27.939 28.405 1.00 20.97 ? 89 THR A C 1 ATOM 651 O O . THR A 1 89 ? -24.618 28.864 27.639 1.00 22.60 ? 89 THR A O 1 ATOM 652 C CB . THR A 1 89 ? -26.558 26.501 27.268 1.00 20.00 ? 89 THR A CB 1 ATOM 653 O OG1 . THR A 1 89 ? -27.925 26.093 27.272 1.00 23.56 ? 89 THR A OG1 1 ATOM 654 C CG2 . THR A 1 89 ? -25.716 25.262 27.321 1.00 20.93 ? 89 THR A CG2 1 ATOM 655 N N . LEU A 1 90 ? -24.001 27.391 29.237 1.00 20.28 ? 90 LEU A N 1 ATOM 656 C CA . LEU A 1 90 ? -22.565 27.751 29.243 1.00 20.46 ? 90 LEU A CA 1 ATOM 657 C C . LEU A 1 90 ? -21.922 26.898 28.120 1.00 18.17 ? 90 LEU A C 1 ATOM 658 O O . LEU A 1 90 ? -21.904 25.673 28.205 1.00 19.13 ? 90 LEU A O 1 ATOM 659 C CB . LEU A 1 90 ? -21.906 27.433 30.610 1.00 16.58 ? 90 LEU A CB 1 ATOM 660 C CG . LEU A 1 90 ? -22.481 28.188 31.813 1.00 14.38 ? 90 LEU A CG 1 ATOM 661 C CD1 . LEU A 1 90 ? -21.806 27.800 33.073 1.00 16.76 ? 90 LEU A CD1 1 ATOM 662 C CD2 . LEU A 1 90 ? -22.370 29.644 31.621 1.00 10.26 ? 90 LEU A CD2 1 ATOM 663 N N . LEU A 1 91 ? -21.412 27.544 27.076 1.00 17.30 ? 91 LEU A N 1 ATOM 664 C CA . LEU A 1 91 ? -20.830 26.846 25.921 1.00 15.94 ? 91 LEU A CA 1 ATOM 665 C C . LEU A 1 91 ? -19.560 27.485 25.389 1.00 17.13 ? 91 LEU A C 1 ATOM 666 O O . LEU A 1 91 ? -19.398 28.692 25.437 1.00 21.14 ? 91 LEU A O 1 ATOM 667 C CB . LEU A 1 91 ? -21.828 26.823 24.756 1.00 17.94 ? 91 LEU A CB 1 ATOM 668 C CG . LEU A 1 91 ? -23.207 26.188 24.881 1.00 15.11 ? 91 LEU A CG 1 ATOM 669 C CD1 . LEU A 1 91 ? -23.997 26.492 23.653 1.00 19.21 ? 91 LEU A CD1 1 ATOM 670 C CD2 . LEU A 1 91 ? -23.125 24.712 25.044 1.00 14.17 ? 91 LEU A CD2 1 ATOM 671 N N . TRP A 1 92 ? -18.641 26.678 24.888 1.00 16.71 ? 92 TRP A N 1 ATOM 672 C CA . TRP A 1 92 ? -17.429 27.220 24.316 1.00 16.13 ? 92 TRP A CA 1 ATOM 673 C C . TRP A 1 92 ? -17.740 27.833 22.958 1.00 18.49 ? 92 TRP A C 1 ATOM 674 O O . TRP A 1 92 ? -18.393 27.178 22.134 1.00 22.57 ? 92 TRP A O 1 ATOM 675 C CB . TRP A 1 92 ? -16.421 26.096 24.083 1.00 14.37 ? 92 TRP A CB 1 ATOM 676 C CG . TRP A 1 92 ? -15.996 25.415 25.316 1.00 14.69 ? 92 TRP A CG 1 ATOM 677 C CD1 . TRP A 1 92 ? -16.252 24.135 25.662 1.00 15.93 ? 92 TRP A CD1 1 ATOM 678 C CD2 . TRP A 1 92 ? -15.167 25.960 26.358 1.00 15.57 ? 92 TRP A CD2 1 ATOM 679 N NE1 . TRP A 1 92 ? -15.631 23.833 26.850 1.00 16.96 ? 92 TRP A NE1 1 ATOM 680 C CE2 . TRP A 1 92 ? -14.956 24.943 27.296 1.00 16.16 ? 92 TRP A CE2 1 ATOM 681 C CE3 . TRP A 1 92 ? -14.576 27.219 26.584 1.00 14.14 ? 92 TRP A CE3 1 ATOM 682 C CZ2 . TRP A 1 92 ? -14.176 25.132 28.443 1.00 15.35 ? 92 TRP A CZ2 1 ATOM 683 C CZ3 . TRP A 1 92 ? -13.810 27.402 27.709 1.00 11.96 ? 92 TRP A CZ3 1 ATOM 684 C CH2 . TRP A 1 92 ? -13.613 26.364 28.630 1.00 9.96 ? 92 TRP A CH2 1 ATOM 685 N N . LYS A 1 93 ? -17.284 29.057 22.709 1.00 17.08 ? 93 LYS A N 1 ATOM 686 C CA . LYS A 1 93 ? -17.447 29.713 21.400 1.00 19.24 ? 93 LYS A CA 1 ATOM 687 C C . LYS A 1 93 ? -16.030 30.089 21.018 1.00 18.48 ? 93 LYS A C 1 ATOM 688 O O . LYS A 1 93 ? -15.274 30.525 21.874 1.00 18.52 ? 93 LYS A O 1 ATOM 689 C CB . LYS A 1 93 ? -18.261 31.024 21.467 1.00 18.62 ? 93 LYS A CB 1 ATOM 690 C CG . LYS A 1 93 ? -19.749 30.866 21.611 1.00 23.76 ? 93 LYS A CG 1 ATOM 691 C CD . LYS A 1 93 ? -20.513 32.185 21.410 1.00 25.19 ? 93 LYS A CD 1 ATOM 692 C CE . LYS A 1 93 ? -20.371 32.648 19.966 1.00 27.63 ? 93 LYS A CE 1 ATOM 693 N NZ . LYS A 1 93 ? -21.394 33.636 19.535 1.00 27.09 ? 93 LYS A NZ 1 ATOM 694 N N . LEU A 1 94 ? -15.676 29.983 19.744 1.00 20.55 ? 94 LEU A N 1 ATOM 695 C CA . LEU A 1 94 ? -14.321 30.367 19.322 1.00 19.37 ? 94 LEU A CA 1 ATOM 696 C C . LEU A 1 94 ? -14.266 31.861 19.183 1.00 19.69 ? 94 LEU A C 1 ATOM 697 O O . LEU A 1 94 ? -15.288 32.478 18.862 1.00 21.91 ? 94 LEU A O 1 ATOM 698 C CB . LEU A 1 94 ? -13.991 29.766 17.986 1.00 14.21 ? 94 LEU A CB 1 ATOM 699 C CG . LEU A 1 94 ? -14.254 28.277 18.000 1.00 16.54 ? 94 LEU A CG 1 ATOM 700 C CD1 . LEU A 1 94 ? -13.896 27.761 16.618 1.00 20.09 ? 94 LEU A CD1 1 ATOM 701 C CD2 . LEU A 1 94 ? -13.400 27.598 19.056 1.00 14.81 ? 94 LEU A CD2 1 ATOM 702 N N . ILE A 1 95 ? -13.081 32.451 19.353 1.00 20.12 ? 95 ILE A N 1 ATOM 703 C CA . ILE A 1 95 ? -12.935 33.902 19.226 1.00 21.21 ? 95 ILE A CA 1 ATOM 704 C C . ILE A 1 95 ? -13.492 34.357 17.883 1.00 24.27 ? 95 ILE A C 1 ATOM 705 O O . ILE A 1 95 ? -14.161 35.369 17.769 1.00 26.07 ? 95 ILE A O 1 ATOM 706 C CB . ILE A 1 95 ? -11.478 34.311 19.434 1.00 20.39 ? 95 ILE A CB 1 ATOM 707 C CG1 . ILE A 1 95 ? -11.201 34.257 20.929 1.00 19.28 ? 95 ILE A CG1 1 ATOM 708 C CG2 . ILE A 1 95 ? -11.231 35.706 18.914 1.00 22.84 ? 95 ILE A CG2 1 ATOM 709 C CD1 . ILE A 1 95 ? -9.917 34.809 21.337 1.00 24.98 ? 95 ILE A CD1 1 ATOM 710 N N . ASP A 1 96 ? -13.290 33.513 16.894 1.00 27.47 ? 96 ASP A N 1 ATOM 711 C CA . ASP A 1 96 ? -13.760 33.668 15.524 1.00 31.51 ? 96 ASP A CA 1 ATOM 712 C C . ASP A 1 96 ? -15.261 34.052 15.496 1.00 32.64 ? 96 ASP A C 1 ATOM 713 O O . ASP A 1 96 ? -15.704 34.850 14.660 1.00 32.11 ? 96 ASP A O 1 ATOM 714 C CB . ASP A 1 96 ? -13.665 32.261 14.909 1.00 36.92 ? 96 ASP A CB 1 ATOM 715 C CG . ASP A 1 96 ? -13.284 32.255 13.473 1.00 46.96 ? 96 ASP A CG 1 ATOM 716 O OD1 . ASP A 1 96 ? -13.087 33.347 12.879 1.00 53.57 ? 96 ASP A OD1 1 ATOM 717 O OD2 . ASP A 1 96 ? -13.170 31.116 12.933 1.00 57.76 ? 96 ASP A OD2 1 ATOM 718 N N . GLU A 1 97 ? -16.041 33.410 16.376 1.00 31.84 ? 97 GLU A N 1 ATOM 719 C CA . GLU A 1 97 ? -17.480 33.566 16.417 1.00 26.87 ? 97 GLU A CA 1 ATOM 720 C C . GLU A 1 97 ? -18.075 34.512 17.416 1.00 27.92 ? 97 GLU A C 1 ATOM 721 O O . GLU A 1 97 ? -19.292 34.701 17.446 1.00 29.57 ? 97 GLU A O 1 ATOM 722 C CB . GLU A 1 97 ? -18.118 32.207 16.598 1.00 28.95 ? 97 GLU A CB 1 ATOM 723 C CG . GLU A 1 97 ? -17.822 31.221 15.515 1.00 31.25 ? 97 GLU A CG 1 ATOM 724 C CD . GLU A 1 97 ? -18.222 31.704 14.134 1.00 38.16 ? 97 GLU A CD 1 ATOM 725 O OE1 . GLU A 1 97 ? -19.224 32.444 13.983 1.00 42.76 ? 97 GLU A OE1 1 ATOM 726 O OE2 . GLU A 1 97 ? -17.523 31.338 13.171 1.00 43.86 ? 97 GLU A OE2 1 ATOM 727 N N . ILE A 1 98 ? -17.250 35.128 18.238 1.00 25.73 ? 98 ILE A N 1 ATOM 728 C CA . ILE A 1 98 ? -17.794 36.036 19.229 1.00 22.38 ? 98 ILE A CA 1 ATOM 729 C C . ILE A 1 98 ? -18.165 37.383 18.636 1.00 21.96 ? 98 ILE A C 1 ATOM 730 O O . ILE A 1 98 ? -17.430 37.976 17.871 1.00 22.91 ? 98 ILE A O 1 ATOM 731 C CB . ILE A 1 98 ? -16.818 36.168 20.427 1.00 21.57 ? 98 ILE A CB 1 ATOM 732 C CG1 . ILE A 1 98 ? -16.769 34.814 21.172 1.00 19.53 ? 98 ILE A CG1 1 ATOM 733 C CG2 . ILE A 1 98 ? -17.231 37.349 21.333 1.00 16.91 ? 98 ILE A CG2 1 ATOM 734 C CD1 . ILE A 1 98 ? -15.619 34.630 22.176 1.00 17.84 ? 98 ILE A CD1 1 ATOM 735 N N . LYS A 1 99 ? -19.321 37.884 19.000 1.00 24.91 ? 99 LYS A N 1 ATOM 736 C CA . LYS A 1 99 ? -19.741 39.169 18.478 1.00 27.52 ? 99 LYS A CA 1 ATOM 737 C C . LYS A 1 99 ? -20.135 40.042 19.627 1.00 27.05 ? 99 LYS A C 1 ATOM 738 O O . LYS A 1 99 ? -20.442 39.553 20.703 1.00 28.19 ? 99 LYS A O 1 ATOM 739 C CB . LYS A 1 99 ? -20.978 39.010 17.615 1.00 31.89 ? 99 LYS A CB 1 ATOM 740 C CG . LYS A 1 99 ? -20.922 37.884 16.638 1.00 40.04 ? 99 LYS A CG 1 ATOM 741 C CD . LYS A 1 99 ? -22.362 37.411 16.355 1.00 49.40 ? 99 LYS A CD 1 ATOM 742 C CE . LYS A 1 99 ? -23.068 36.766 17.584 1.00 49.65 ? 99 LYS A CE 1 ATOM 743 N NZ . LYS A 1 99 ? -22.541 35.368 17.794 1.00 52.54 ? 99 LYS A NZ 1 ATOM 744 N N . PRO A 1 100 ? -20.168 41.356 19.408 1.00 28.65 ? 100 PRO A N 1 ATOM 745 C CA . PRO A 1 100 ? -20.558 42.277 20.478 1.00 27.72 ? 100 PRO A CA 1 ATOM 746 C C . PRO A 1 100 ? -21.953 41.841 20.937 1.00 25.10 ? 100 PRO A C 1 ATOM 747 O O . PRO A 1 100 ? -22.740 41.378 20.124 1.00 22.90 ? 100 PRO A O 1 ATOM 748 C CB . PRO A 1 100 ? -20.627 43.611 19.756 1.00 29.10 ? 100 PRO A CB 1 ATOM 749 C CG . PRO A 1 100 ? -19.607 43.448 18.669 1.00 30.56 ? 100 PRO A CG 1 ATOM 750 C CD . PRO A 1 100 ? -19.871 42.080 18.161 1.00 27.09 ? 100 PRO A CD 1 ATOM 751 N N . GLY A 1 101 ? -22.232 41.925 22.230 1.00 22.13 ? 101 GLY A N 1 ATOM 752 C CA . GLY A 1 101 ? -23.527 41.504 22.699 1.00 22.08 ? 101 GLY A CA 1 ATOM 753 C C . GLY A 1 101 ? -23.516 40.120 23.283 1.00 22.95 ? 101 GLY A C 1 ATOM 754 O O . GLY A 1 101 ? -24.419 39.800 24.065 1.00 24.88 ? 101 GLY A O 1 ATOM 755 N N . ASP A 1 102 ? -22.552 39.289 22.867 1.00 23.23 ? 102 ASP A N 1 ATOM 756 C CA . ASP A 1 102 ? -22.392 37.926 23.418 1.00 21.46 ? 102 ASP A CA 1 ATOM 757 C C . ASP A 1 102 ? -22.016 38.126 24.875 1.00 20.66 ? 102 ASP A C 1 ATOM 758 O O . ASP A 1 102 ? -21.529 39.182 25.237 1.00 21.14 ? 102 ASP A O 1 ATOM 759 C CB . ASP A 1 102 ? -21.218 37.188 22.775 1.00 17.74 ? 102 ASP A CB 1 ATOM 760 C CG . ASP A 1 102 ? -21.585 36.506 21.494 1.00 20.39 ? 102 ASP A CG 1 ATOM 761 O OD1 . ASP A 1 102 ? -22.745 36.602 21.084 1.00 23.25 ? 102 ASP A OD1 1 ATOM 762 O OD2 . ASP A 1 102 ? -20.729 35.836 20.901 1.00 22.67 ? 102 ASP A OD2 1 ATOM 763 N N . TYR A 1 103 ? -22.158 37.091 25.689 1.00 21.17 ? 103 TYR A N 1 ATOM 764 C CA . TYR A 1 103 ? -21.815 37.201 27.088 1.00 17.90 ? 103 TYR A CA 1 ATOM 765 C C . TYR A 1 103 ? -20.740 36.216 27.342 1.00 17.21 ? 103 TYR A C 1 ATOM 766 O O . TYR A 1 103 ? -20.975 35.029 27.201 1.00 19.71 ? 103 TYR A O 1 ATOM 767 C CB . TYR A 1 103 ? -22.994 36.812 27.980 1.00 21.15 ? 103 TYR A CB 1 ATOM 768 C CG . TYR A 1 103 ? -23.960 37.918 28.209 1.00 19.18 ? 103 TYR A CG 1 ATOM 769 C CD1 . TYR A 1 103 ? -23.646 38.919 29.089 1.00 21.62 ? 103 TYR A CD1 1 ATOM 770 C CD2 . TYR A 1 103 ? -25.135 38.016 27.474 1.00 22.13 ? 103 TYR A CD2 1 ATOM 771 C CE1 . TYR A 1 103 ? -24.469 40.037 29.245 1.00 30.69 ? 103 TYR A CE1 1 ATOM 772 C CE2 . TYR A 1 103 ? -25.995 39.138 27.606 1.00 27.51 ? 103 TYR A CE2 1 ATOM 773 C CZ . TYR A 1 103 ? -25.646 40.143 28.499 1.00 31.90 ? 103 TYR A CZ 1 ATOM 774 O OH . TYR A 1 103 ? -26.430 41.262 28.723 1.00 35.14 ? 103 TYR A OH 1 ATOM 775 N N . ALA A 1 104 ? -19.564 36.715 27.679 1.00 16.97 ? 104 ALA A N 1 ATOM 776 C CA . ALA A 1 104 ? -18.425 35.877 28.026 1.00 19.33 ? 104 ALA A CA 1 ATOM 777 C C . ALA A 1 104 ? -18.495 35.592 29.567 1.00 19.65 ? 104 ALA A C 1 ATOM 778 O O . ALA A 1 104 ? -18.883 36.479 30.341 1.00 18.11 ? 104 ALA A O 1 ATOM 779 C CB . ALA A 1 104 ? -17.144 36.606 27.699 1.00 19.04 ? 104 ALA A CB 1 ATOM 780 N N . VAL A 1 105 ? -18.137 34.378 30.003 1.00 17.20 ? 105 VAL A N 1 ATOM 781 C CA . VAL A 1 105 ? -18.173 34.044 31.439 1.00 17.47 ? 105 VAL A CA 1 ATOM 782 C C . VAL A 1 105 ? -16.874 34.507 32.099 1.00 19.04 ? 105 VAL A C 1 ATOM 783 O O . VAL A 1 105 ? -15.790 34.279 31.559 1.00 19.48 ? 105 VAL A O 1 ATOM 784 C CB . VAL A 1 105 ? -18.372 32.524 31.667 1.00 17.34 ? 105 VAL A CB 1 ATOM 785 C CG1 . VAL A 1 105 ? -18.409 32.163 33.160 1.00 12.29 ? 105 VAL A CG1 1 ATOM 786 C CG2 . VAL A 1 105 ? -19.635 32.102 30.978 1.00 13.17 ? 105 VAL A CG2 1 ATOM 787 N N . ILE A 1 106 ? -17.003 35.275 33.168 1.00 17.38 ? 106 ILE A N 1 ATOM 788 C CA . ILE A 1 106 ? -15.869 35.782 33.911 1.00 16.98 ? 106 ILE A CA 1 ATOM 789 C C . ILE A 1 106 ? -15.833 35.051 35.268 1.00 18.44 ? 106 ILE A C 1 ATOM 790 O O . ILE A 1 106 ? -16.877 34.811 35.882 1.00 18.58 ? 106 ILE A O 1 ATOM 791 C CB . ILE A 1 106 ? -16.017 37.312 34.122 1.00 16.16 ? 106 ILE A CB 1 ATOM 792 C CG1 . ILE A 1 106 ? -16.153 38.021 32.767 1.00 17.24 ? 106 ILE A CG1 1 ATOM 793 C CG2 . ILE A 1 106 ? -14.820 37.893 34.868 1.00 13.61 ? 106 ILE A CG2 1 ATOM 794 C CD1 . ILE A 1 106 ? -14.955 37.929 31.848 1.00 15.48 ? 106 ILE A CD1 1 ATOM 795 N N . GLN A 1 107 ? -14.641 34.620 35.676 1.00 18.81 ? 107 GLN A N 1 ATOM 796 C CA . GLN A 1 107 ? -14.409 33.933 36.934 1.00 17.92 ? 107 GLN A CA 1 ATOM 797 C C . GLN A 1 107 ? -13.880 35.037 37.854 1.00 19.09 ? 107 GLN A C 1 ATOM 798 O O . GLN A 1 107 ? -12.783 35.518 37.688 1.00 20.31 ? 107 GLN A O 1 ATOM 799 C CB . GLN A 1 107 ? -13.353 32.847 36.729 1.00 18.15 ? 107 GLN A CB 1 ATOM 800 C CG . GLN A 1 107 ? -12.816 32.274 37.987 1.00 17.93 ? 107 GLN A CG 1 ATOM 801 C CD . GLN A 1 107 ? -13.929 31.945 38.906 1.00 19.99 ? 107 GLN A CD 1 ATOM 802 O OE1 . GLN A 1 107 ? -14.798 31.170 38.570 1.00 27.40 ? 107 GLN A OE1 1 ATOM 803 N NE2 . GLN A 1 107 ? -13.958 32.585 40.049 1.00 19.56 ? 107 GLN A NE2 1 ATOM 804 N N . ARG A 1 108 ? -14.690 35.446 38.814 1.00 23.48 ? 108 ARG A N 1 ATOM 805 C CA . ARG A 1 108 ? -14.366 36.521 39.753 1.00 26.15 ? 108 ARG A CA 1 ATOM 806 C C . ARG A 1 108 ? -13.161 36.329 40.652 1.00 28.47 ? 108 ARG A C 1 ATOM 807 O O . ARG A 1 108 ? -12.625 37.313 41.197 1.00 28.15 ? 108 ARG A O 1 ATOM 808 C CB . ARG A 1 108 ? -15.564 36.795 40.632 1.00 24.35 ? 108 ARG A CB 1 ATOM 809 C CG . ARG A 1 108 ? -16.692 37.385 39.886 1.00 31.37 ? 108 ARG A CG 1 ATOM 810 C CD . ARG A 1 108 ? -17.624 38.063 40.834 1.00 37.90 ? 108 ARG A CD 1 ATOM 811 N NE . ARG A 1 108 ? -18.846 37.302 40.965 1.00 47.73 ? 108 ARG A NE 1 ATOM 812 C CZ . ARG A 1 108 ? -20.056 37.812 40.749 1.00 57.07 ? 108 ARG A CZ 1 ATOM 813 N NH1 . ARG A 1 108 ? -20.181 39.101 40.400 1.00 57.80 ? 108 ARG A NH1 1 ATOM 814 N NH2 . ARG A 1 108 ? -21.141 37.028 40.844 1.00 61.02 ? 108 ARG A NH2 1 ATOM 815 N N . SER A 1 109 ? -12.783 35.068 40.872 1.00 26.72 ? 109 SER A N 1 ATOM 816 C CA . SER A 1 109 ? -11.650 34.772 41.719 1.00 23.25 ? 109 SER A CA 1 ATOM 817 C C . SER A 1 109 ? -10.354 35.216 41.113 1.00 25.50 ? 109 SER A C 1 ATOM 818 O O . SER A 1 109 ? -9.331 35.242 41.795 1.00 28.30 ? 109 SER A O 1 ATOM 819 C CB . SER A 1 109 ? -11.629 33.299 42.066 1.00 23.04 ? 109 SER A CB 1 ATOM 820 O OG . SER A 1 109 ? -12.837 32.954 42.723 1.00 28.19 ? 109 SER A OG 1 ATOM 821 N N . ALA A 1 110 ? -10.387 35.506 39.815 1.00 26.64 ? 110 ALA A N 1 ATOM 822 C CA . ALA A 1 110 ? -9.227 35.995 39.085 1.00 30.71 ? 110 ALA A CA 1 ATOM 823 C C . ALA A 1 110 ? -8.867 37.414 39.500 1.00 37.63 ? 110 ALA A C 1 ATOM 824 O O . ALA A 1 110 ? -7.913 37.978 38.972 1.00 42.65 ? 110 ALA A O 1 ATOM 825 C CB . ALA A 1 110 ? -9.503 35.990 37.614 1.00 29.33 ? 110 ALA A CB 1 ATOM 826 N N . PHE A 1 111 ? -9.661 38.017 40.380 1.00 41.88 ? 111 PHE A N 1 ATOM 827 C CA . PHE A 1 111 ? -9.424 39.374 40.848 1.00 47.16 ? 111 PHE A CA 1 ATOM 828 C C . PHE A 1 111 ? -9.327 39.348 42.383 1.00 56.40 ? 111 PHE A C 1 ATOM 829 O O . PHE A 1 111 ? -10.027 38.549 43.034 1.00 59.23 ? 111 PHE A O 1 ATOM 830 C CB . PHE A 1 111 ? -10.578 40.266 40.373 1.00 42.97 ? 111 PHE A CB 1 ATOM 831 C CG . PHE A 1 111 ? -10.788 40.238 38.883 1.00 40.23 ? 111 PHE A CG 1 ATOM 832 C CD1 . PHE A 1 111 ? -9.869 40.819 38.024 1.00 43.29 ? 111 PHE A CD1 1 ATOM 833 C CD2 . PHE A 1 111 ? -11.844 39.550 38.334 1.00 41.14 ? 111 PHE A CD2 1 ATOM 834 C CE1 . PHE A 1 111 ? -9.992 40.705 36.626 1.00 42.12 ? 111 PHE A CE1 1 ATOM 835 C CE2 . PHE A 1 111 ? -11.980 39.427 36.936 1.00 43.44 ? 111 PHE A CE2 1 ATOM 836 C CZ . PHE A 1 111 ? -11.046 40.006 36.083 1.00 42.05 ? 111 PHE A CZ 1 ATOM 837 N N . SER A 1 112 ? -8.436 40.163 42.963 1.00 66.19 ? 112 SER A N 1 ATOM 838 C CA . SER A 1 112 ? -8.280 40.211 44.444 1.00 74.56 ? 112 SER A CA 1 ATOM 839 C C . SER A 1 112 ? -8.077 41.628 45.095 1.00 79.18 ? 112 SER A C 1 ATOM 840 O O . SER A 1 112 ? -6.956 41.922 45.603 1.00 81.19 ? 112 SER A O 1 ATOM 841 C CB . SER A 1 112 ? -7.179 39.229 44.907 1.00 72.77 ? 112 SER A CB 1 ATOM 842 O OG . SER A 1 112 ? -7.201 39.063 46.318 1.00 66.13 ? 112 SER A OG 1 ATOM 843 N N . THR A 1 113 ? -23.729 43.003 34.094 1.00 88.16 ? 113 THR A N 1 ATOM 844 C CA . THR A 1 113 ? -23.443 43.312 35.517 1.00 88.51 ? 113 THR A CA 1 ATOM 845 C C . THR A 1 113 ? -24.468 42.612 36.411 1.00 87.45 ? 113 THR A C 1 ATOM 846 O O . THR A 1 113 ? -24.164 41.613 37.065 1.00 87.28 ? 113 THR A O 1 ATOM 847 C CB . THR A 1 113 ? -23.451 44.871 35.794 1.00 89.87 ? 113 THR A CB 1 ATOM 848 O OG1 . THR A 1 113 ? -22.987 45.584 34.635 1.00 90.14 ? 113 THR A OG1 1 ATOM 849 C CG2 . THR A 1 113 ? -22.531 45.229 36.974 1.00 89.49 ? 113 THR A CG2 1 ATOM 850 N N . VAL A 1 114 ? -25.706 43.092 36.354 1.00 86.97 ? 114 VAL A N 1 ATOM 851 C CA . VAL A 1 114 ? -26.793 42.572 37.177 1.00 85.49 ? 114 VAL A CA 1 ATOM 852 C C . VAL A 1 114 ? -27.472 41.306 36.642 1.00 83.06 ? 114 VAL A C 1 ATOM 853 O O . VAL A 1 114 ? -28.121 41.325 35.581 1.00 84.61 ? 114 VAL A O 1 ATOM 854 C CB . VAL A 1 114 ? -27.886 43.658 37.394 1.00 88.07 ? 114 VAL A CB 1 ATOM 855 C CG1 . VAL A 1 114 ? -28.788 43.282 38.579 1.00 89.55 ? 114 VAL A CG1 1 ATOM 856 C CG2 . VAL A 1 114 ? -27.248 45.047 37.588 1.00 89.50 ? 114 VAL A CG2 1 ATOM 857 N N . GLY A 1 115 ? -27.277 40.206 37.369 1.00 77.98 ? 115 GLY A N 1 ATOM 858 C CA . GLY A 1 115 ? -27.894 38.932 37.024 1.00 70.83 ? 115 GLY A CA 1 ATOM 859 C C . GLY A 1 115 ? -27.462 38.076 35.834 1.00 64.98 ? 115 GLY A C 1 ATOM 860 O O . GLY A 1 115 ? -26.801 38.529 34.890 1.00 66.69 ? 115 GLY A O 1 ATOM 861 N N . VAL A 1 116 ? -27.857 36.802 35.918 1.00 57.42 ? 116 VAL A N 1 ATOM 862 C CA . VAL A 1 116 ? -27.604 35.805 34.894 1.00 48.00 ? 116 VAL A CA 1 ATOM 863 C C . VAL A 1 116 ? -28.525 36.233 33.777 1.00 45.51 ? 116 VAL A C 1 ATOM 864 O O . VAL A 1 116 ? -29.738 36.294 33.952 1.00 45.47 ? 116 VAL A O 1 ATOM 865 C CB . VAL A 1 116 ? -28.029 34.361 35.344 1.00 45.03 ? 116 VAL A CB 1 ATOM 866 C CG1 . VAL A 1 116 ? -27.625 33.319 34.298 1.00 43.35 ? 116 VAL A CG1 1 ATOM 867 C CG2 . VAL A 1 116 ? -27.427 34.007 36.689 1.00 45.77 ? 116 VAL A CG2 1 ATOM 868 N N . PRO A 1 117 ? -27.961 36.671 32.665 1.00 42.78 ? 117 PRO A N 1 ATOM 869 C CA . PRO A 1 117 ? -28.854 37.070 31.593 1.00 43.66 ? 117 PRO A CA 1 ATOM 870 C C . PRO A 1 117 ? -29.793 35.909 31.121 1.00 45.35 ? 117 PRO A C 1 ATOM 871 O O . PRO A 1 117 ? -29.337 34.778 30.824 1.00 44.69 ? 117 PRO A O 1 ATOM 872 C CB . PRO A 1 117 ? -27.863 37.520 30.521 1.00 41.59 ? 117 PRO A CB 1 ATOM 873 C CG . PRO A 1 117 ? -26.771 38.114 31.347 1.00 39.51 ? 117 PRO A CG 1 ATOM 874 C CD . PRO A 1 117 ? -26.581 37.101 32.394 1.00 40.71 ? 117 PRO A CD 1 ATOM 875 N N . GLY A 1 118 ? -31.108 36.188 31.135 1.00 46.25 ? 118 GLY A N 1 ATOM 876 C CA . GLY A 1 118 ? -32.137 35.240 30.694 1.00 43.24 ? 118 GLY A CA 1 ATOM 877 C C . GLY A 1 118 ? -32.574 34.109 31.615 1.00 42.71 ? 118 GLY A C 1 ATOM 878 O O . GLY A 1 118 ? -33.358 33.269 31.190 1.00 43.25 ? 118 GLY A O 1 ATOM 879 N N . LEU A 1 119 ? -32.130 34.113 32.873 1.00 42.39 ? 119 LEU A N 1 ATOM 880 C CA . LEU A 1 119 ? -32.432 33.050 33.830 1.00 42.21 ? 119 LEU A CA 1 ATOM 881 C C . LEU A 1 119 ? -33.837 33.150 34.360 1.00 47.16 ? 119 LEU A C 1 ATOM 882 O O . LEU A 1 119 ? -34.499 32.125 34.546 1.00 47.93 ? 119 LEU A O 1 ATOM 883 C CB . LEU A 1 119 ? -31.448 33.080 35.004 1.00 38.53 ? 119 LEU A CB 1 ATOM 884 C CG . LEU A 1 119 ? -31.571 31.975 36.052 1.00 36.51 ? 119 LEU A CG 1 ATOM 885 C CD1 . LEU A 1 119 ? -31.275 30.671 35.415 1.00 35.51 ? 119 LEU A CD1 1 ATOM 886 C CD2 . LEU A 1 119 ? -30.606 32.211 37.166 1.00 36.41 ? 119 LEU A CD2 1 ATOM 887 N N . VAL A 1 120 ? -34.287 34.382 34.614 1.00 49.35 ? 120 VAL A N 1 ATOM 888 C CA . VAL A 1 120 ? -35.635 34.630 35.142 1.00 50.27 ? 120 VAL A CA 1 ATOM 889 C C . VAL A 1 120 ? -36.720 34.109 34.221 1.00 48.72 ? 120 VAL A C 1 ATOM 890 O O . VAL A 1 120 ? -37.553 33.308 34.648 1.00 45.69 ? 120 VAL A O 1 ATOM 891 C CB . VAL A 1 120 ? -35.867 36.130 35.443 1.00 52.80 ? 120 VAL A CB 1 ATOM 892 C CG1 . VAL A 1 120 ? -37.365 36.469 35.384 1.00 53.50 ? 120 VAL A CG1 1 ATOM 893 C CG2 . VAL A 1 120 ? -35.310 36.474 36.843 1.00 52.49 ? 120 VAL A CG2 1 ATOM 894 N N . ARG A 1 121 ? -36.687 34.552 32.963 1.00 50.06 ? 121 ARG A N 1 ATOM 895 C CA . ARG A 1 121 ? -37.664 34.107 31.975 1.00 53.59 ? 121 ARG A CA 1 ATOM 896 C C . ARG A 1 121 ? -37.569 32.593 31.840 1.00 51.07 ? 121 ARG A C 1 ATOM 897 O O . ARG A 1 121 ? -38.578 31.915 31.637 1.00 52.27 ? 121 ARG A O 1 ATOM 898 C CB . ARG A 1 121 ? -37.421 34.738 30.597 1.00 60.63 ? 121 ARG A CB 1 ATOM 899 C CG . ARG A 1 121 ? -37.385 36.264 30.554 1.00 72.22 ? 121 ARG A CG 1 ATOM 900 C CD . ARG A 1 121 ? -37.323 36.797 29.086 1.00 81.59 ? 121 ARG A CD 1 ATOM 901 N NE . ARG A 1 121 ? -36.179 36.294 28.301 1.00 89.62 ? 121 ARG A NE 1 ATOM 902 C CZ . ARG A 1 121 ? -35.243 37.054 27.713 1.00 93.30 ? 121 ARG A CZ 1 ATOM 903 N NH1 . ARG A 1 121 ? -35.286 38.388 27.801 1.00 93.40 ? 121 ARG A NH1 1 ATOM 904 N NH2 . ARG A 1 121 ? -34.243 36.473 27.035 1.00 94.96 ? 121 ARG A NH2 1 ATOM 905 N N . PHE A 1 122 ? -36.351 32.068 31.941 1.00 47.51 ? 122 PHE A N 1 ATOM 906 C CA . PHE A 1 122 ? -36.139 30.640 31.828 1.00 44.24 ? 122 PHE A CA 1 ATOM 907 C C . PHE A 1 122 ? -36.817 29.931 32.963 1.00 44.95 ? 122 PHE A C 1 ATOM 908 O O . PHE A 1 122 ? -37.434 28.896 32.744 1.00 46.86 ? 122 PHE A O 1 ATOM 909 C CB . PHE A 1 122 ? -34.661 30.299 31.864 1.00 42.56 ? 122 PHE A CB 1 ATOM 910 C CG . PHE A 1 122 ? -34.388 28.858 32.136 1.00 39.46 ? 122 PHE A CG 1 ATOM 911 C CD1 . PHE A 1 122 ? -34.783 27.881 31.230 1.00 39.48 ? 122 PHE A CD1 1 ATOM 912 C CD2 . PHE A 1 122 ? -33.769 28.474 33.309 1.00 36.77 ? 122 PHE A CD2 1 ATOM 913 C CE1 . PHE A 1 122 ? -34.568 26.532 31.492 1.00 40.53 ? 122 PHE A CE1 1 ATOM 914 C CE2 . PHE A 1 122 ? -33.552 27.142 33.580 1.00 38.55 ? 122 PHE A CE2 1 ATOM 915 C CZ . PHE A 1 122 ? -33.953 26.159 32.670 1.00 38.49 ? 122 PHE A CZ 1 ATOM 916 N N . LEU A 1 123 ? -36.672 30.476 34.168 1.00 45.42 ? 123 LEU A N 1 ATOM 917 C CA . LEU A 1 123 ? -37.243 29.905 35.375 1.00 46.65 ? 123 LEU A CA 1 ATOM 918 C C . LEU A 1 123 ? -38.738 29.982 35.358 1.00 50.30 ? 123 LEU A C 1 ATOM 919 O O . LEU A 1 123 ? -39.385 28.971 35.529 1.00 51.17 ? 123 LEU A O 1 ATOM 920 C CB . LEU A 1 123 ? -36.677 30.581 36.629 1.00 44.77 ? 123 LEU A CB 1 ATOM 921 C CG . LEU A 1 123 ? -35.266 30.072 36.996 1.00 44.42 ? 123 LEU A CG 1 ATOM 922 C CD1 . LEU A 1 123 ? -34.581 30.964 38.004 1.00 39.42 ? 123 LEU A CD1 1 ATOM 923 C CD2 . LEU A 1 123 ? -35.329 28.620 37.479 1.00 40.11 ? 123 LEU A CD2 1 ATOM 924 N N . GLU A 1 124 ? -39.305 31.148 35.089 1.00 54.05 ? 124 GLU A N 1 ATOM 925 C CA . GLU A 1 124 ? -40.754 31.236 35.069 1.00 60.00 ? 124 GLU A CA 1 ATOM 926 C C . GLU A 1 124 ? -41.372 30.460 33.903 1.00 63.95 ? 124 GLU A C 1 ATOM 927 O O . GLU A 1 124 ? -42.443 29.869 34.038 1.00 65.53 ? 124 GLU A O 1 ATOM 928 C CB . GLU A 1 124 ? -41.197 32.678 35.070 1.00 60.34 ? 124 GLU A CB 1 ATOM 929 C CG . GLU A 1 124 ? -40.796 33.410 33.845 1.00 68.24 ? 124 GLU A CG 1 ATOM 930 C CD . GLU A 1 124 ? -41.123 34.875 33.933 1.00 73.04 ? 124 GLU A CD 1 ATOM 931 O OE1 . GLU A 1 124 ? -41.424 35.343 35.066 1.00 75.26 ? 124 GLU A OE1 1 ATOM 932 O OE2 . GLU A 1 124 ? -41.071 35.551 32.870 1.00 75.32 ? 124 GLU A OE2 1 ATOM 933 N N . ALA A 1 125 ? -40.688 30.433 32.768 1.00 69.72 ? 125 ALA A N 1 ATOM 934 C CA . ALA A 1 125 ? -41.176 29.685 31.613 1.00 75.36 ? 125 ALA A CA 1 ATOM 935 C C . ALA A 1 125 ? -41.027 28.174 31.858 1.00 80.08 ? 125 ALA A C 1 ATOM 936 O O . ALA A 1 125 ? -41.983 27.418 31.699 1.00 82.89 ? 125 ALA A O 1 ATOM 937 C CB . ALA A 1 125 ? -40.416 30.091 30.368 1.00 75.66 ? 125 ALA A CB 1 ATOM 938 N N . HIS A 1 126 ? -39.825 27.747 32.253 1.00 83.89 ? 126 HIS A N 1 ATOM 939 C CA . HIS A 1 126 ? -39.526 26.342 32.531 1.00 86.59 ? 126 HIS A CA 1 ATOM 940 C C . HIS A 1 126 ? -39.696 25.962 34.007 1.00 89.73 ? 126 HIS A C 1 ATOM 941 O O . HIS A 1 126 ? -40.740 25.445 34.387 1.00 90.88 ? 126 HIS A O 1 ATOM 942 C CB . HIS A 1 126 ? -38.110 25.989 32.081 1.00 86.41 ? 126 HIS A CB 1 ATOM 943 C CG . HIS A 1 126 ? -37.899 26.079 30.602 1.00 87.37 ? 126 HIS A CG 1 ATOM 944 N ND1 . HIS A 1 126 ? -37.830 27.281 29.930 1.00 88.52 ? 126 HIS A ND1 1 ATOM 945 C CD2 . HIS A 1 126 ? -37.711 25.116 29.666 1.00 88.49 ? 126 HIS A CD2 1 ATOM 946 C CE1 . HIS A 1 126 ? -37.610 27.056 28.644 1.00 88.48 ? 126 HIS A CE1 1 ATOM 947 N NE2 . HIS A 1 126 ? -37.534 25.750 28.459 1.00 88.14 ? 126 HIS A NE2 1 ATOM 948 N N . HIS A 1 127 ? -38.696 26.271 34.835 1.00 93.16 ? 127 HIS A N 1 ATOM 949 C CA . HIS A 1 127 ? -38.668 25.952 36.274 1.00 97.50 ? 127 HIS A CA 1 ATOM 950 C C . HIS A 1 127 ? -38.951 24.504 36.624 1.00 99.12 ? 127 HIS A C 1 ATOM 951 O O . HIS A 1 127 ? -38.123 23.858 37.266 1.00 100.48 ? 127 HIS A O 1 ATOM 952 C CB . HIS A 1 127 ? -39.547 26.870 37.136 1.00 99.75 ? 127 HIS A CB 1 ATOM 953 C CG . HIS A 1 127 ? -41.015 26.664 36.953 1.00 102.82 ? 127 HIS A CG 1 ATOM 954 N ND1 . HIS A 1 127 ? -41.698 25.616 37.533 1.00 104.36 ? 127 HIS A ND1 1 ATOM 955 C CD2 . HIS A 1 127 ? -41.928 27.356 36.232 1.00 104.70 ? 127 HIS A CD2 1 ATOM 956 C CE1 . HIS A 1 127 ? -42.967 25.668 37.170 1.00 105.61 ? 127 HIS A CE1 1 ATOM 957 N NE2 . HIS A 1 127 ? -43.133 26.714 36.380 1.00 105.78 ? 127 HIS A NE2 1 ATOM 958 N N . ARG A 1 128 ? -40.138 24.002 36.302 1.00 100.07 ? 128 ARG A N 1 ATOM 959 C CA . ARG A 1 128 ? -40.391 22.614 36.598 1.00 101.16 ? 128 ARG A CA 1 ATOM 960 C C . ARG A 1 128 ? -39.961 21.722 35.449 1.00 101.03 ? 128 ARG A C 1 ATOM 961 O O . ARG A 1 128 ? -40.739 20.970 34.849 1.00 102.45 ? 128 ARG A O 1 ATOM 962 C CB . ARG A 1 128 ? -41.806 22.320 37.086 1.00 102.78 ? 128 ARG A CB 1 ATOM 963 C CG . ARG A 1 128 ? -41.792 21.534 38.417 1.00 106.33 ? 128 ARG A CG 1 ATOM 964 C CD . ARG A 1 128 ? -40.922 20.221 38.397 1.00 109.36 ? 128 ARG A CD 1 ATOM 965 N NE . ARG A 1 128 ? -39.491 20.434 38.112 1.00 111.92 ? 128 ARG A NE 1 ATOM 966 C CZ . ARG A 1 128 ? -38.571 20.815 39.002 1.00 113.46 ? 128 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 128 ? -38.899 21.022 40.272 1.00 115.21 ? 128 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 128 ? -37.324 21.051 38.610 1.00 112.59 ? 128 ARG A NH2 1 ATOM 969 N N . ASP A 1 129 ? -38.690 21.895 35.128 1.00 99.32 ? 129 ASP A N 1 ATOM 970 C CA . ASP A 1 129 ? -37.985 21.128 34.131 1.00 97.35 ? 129 ASP A CA 1 ATOM 971 C C . ASP A 1 129 ? -37.112 20.511 35.220 1.00 94.84 ? 129 ASP A C 1 ATOM 972 O O . ASP A 1 129 ? -36.499 21.240 35.998 1.00 94.78 ? 129 ASP A O 1 ATOM 973 C CB . ASP A 1 129 ? -37.169 22.078 33.235 1.00 101.00 ? 129 ASP A CB 1 ATOM 974 C CG . ASP A 1 129 ? -36.796 21.461 31.873 1.00 103.50 ? 129 ASP A CG 1 ATOM 975 O OD1 . ASP A 1 129 ? -37.695 20.904 31.183 1.00 105.17 ? 129 ASP A OD1 1 ATOM 976 O OD2 . ASP A 1 129 ? -35.603 21.575 31.483 1.00 103.62 ? 129 ASP A OD2 1 ATOM 977 N N . PRO A 1 130 ? -37.129 19.178 35.368 1.00 92.57 ? 130 PRO A N 1 ATOM 978 C CA . PRO A 1 130 ? -36.322 18.510 36.406 1.00 90.35 ? 130 PRO A CA 1 ATOM 979 C C . PRO A 1 130 ? -34.880 19.014 36.609 1.00 86.16 ? 130 PRO A C 1 ATOM 980 O O . PRO A 1 130 ? -34.361 19.000 37.723 1.00 87.14 ? 130 PRO A O 1 ATOM 981 C CB . PRO A 1 130 ? -36.372 17.043 35.983 1.00 92.13 ? 130 PRO A CB 1 ATOM 982 C CG . PRO A 1 130 ? -37.769 16.935 35.390 1.00 93.70 ? 130 PRO A CG 1 ATOM 983 C CD . PRO A 1 130 ? -37.862 18.196 34.547 1.00 92.37 ? 130 PRO A CD 1 ATOM 984 N N . ASP A 1 131 ? -34.242 19.482 35.545 1.00 80.83 ? 131 ASP A N 1 ATOM 985 C CA . ASP A 1 131 ? -32.887 19.969 35.665 1.00 75.38 ? 131 ASP A CA 1 ATOM 986 C C . ASP A 1 131 ? -32.858 21.470 35.750 1.00 69.02 ? 131 ASP A C 1 ATOM 987 O O . ASP A 1 131 ? -31.800 22.057 35.793 1.00 65.80 ? 131 ASP A O 1 ATOM 988 C CB . ASP A 1 131 ? -32.029 19.482 34.489 1.00 82.64 ? 131 ASP A CB 1 ATOM 989 C CG . ASP A 1 131 ? -31.061 18.330 34.880 1.00 88.41 ? 131 ASP A CG 1 ATOM 990 O OD1 . ASP A 1 131 ? -31.358 17.586 35.859 1.00 90.68 ? 131 ASP A OD1 1 ATOM 991 O OD2 . ASP A 1 131 ? -30.000 18.173 34.200 1.00 90.28 ? 131 ASP A OD2 1 ATOM 992 N N . ALA A 1 132 ? -34.017 22.102 35.799 1.00 65.74 ? 132 ALA A N 1 ATOM 993 C CA . ALA A 1 132 ? -34.054 23.555 35.881 1.00 65.52 ? 132 ALA A CA 1 ATOM 994 C C . ALA A 1 132 ? -33.393 24.041 37.176 1.00 65.53 ? 132 ALA A C 1 ATOM 995 O O . ALA A 1 132 ? -32.769 25.101 37.209 1.00 66.10 ? 132 ALA A O 1 ATOM 996 C CB . ALA A 1 132 ? -35.474 24.080 35.766 1.00 62.73 ? 132 ALA A CB 1 ATOM 997 N N . LYS A 1 133 ? -33.465 23.237 38.229 1.00 64.93 ? 133 LYS A N 1 ATOM 998 C CA . LYS A 1 133 ? -32.851 23.636 39.480 1.00 62.85 ? 133 LYS A CA 1 ATOM 999 C C . LYS A 1 133 ? -31.324 23.431 39.450 1.00 61.09 ? 133 LYS A C 1 ATOM 1000 O O . LYS A 1 133 ? -30.577 24.255 39.988 1.00 61.21 ? 133 LYS A O 1 ATOM 1001 C CB . LYS A 1 133 ? -33.516 22.919 40.648 1.00 64.29 ? 133 LYS A CB 1 ATOM 1002 C CG . LYS A 1 133 ? -33.382 23.689 41.945 1.00 67.51 ? 133 LYS A CG 1 ATOM 1003 C CD . LYS A 1 133 ? -32.153 23.252 42.733 1.00 69.41 ? 133 LYS A CD 1 ATOM 1004 C CE . LYS A 1 133 ? -32.465 22.046 43.610 1.00 71.98 ? 133 LYS A CE 1 ATOM 1005 N NZ . LYS A 1 133 ? -32.922 20.832 42.860 1.00 73.98 ? 133 LYS A NZ 1 ATOM 1006 N N . ALA A 1 134 ? -30.868 22.359 38.790 1.00 57.13 ? 134 ALA A N 1 ATOM 1007 C CA . ALA A 1 134 ? -29.435 22.069 38.641 1.00 52.04 ? 134 ALA A CA 1 ATOM 1008 C C . ALA A 1 134 ? -28.782 23.142 37.745 1.00 50.15 ? 134 ALA A C 1 ATOM 1009 O O . ALA A 1 134 ? -27.649 23.558 37.951 1.00 49.47 ? 134 ALA A O 1 ATOM 1010 C CB . ALA A 1 134 ? -29.246 20.694 38.028 1.00 51.11 ? 134 ALA A CB 1 ATOM 1011 N N . ILE A 1 135 ? -29.524 23.560 36.733 1.00 46.76 ? 135 ILE A N 1 ATOM 1012 C CA . ILE A 1 135 ? -29.103 24.577 35.803 1.00 43.20 ? 135 ILE A CA 1 ATOM 1013 C C . ILE A 1 135 ? -28.951 25.875 36.555 1.00 41.13 ? 135 ILE A C 1 ATOM 1014 O O . ILE A 1 135 ? -27.906 26.494 36.506 1.00 39.92 ? 135 ILE A O 1 ATOM 1015 C CB . ILE A 1 135 ? -30.157 24.728 34.680 1.00 44.25 ? 135 ILE A CB 1 ATOM 1016 C CG1 . ILE A 1 135 ? -29.954 23.630 33.639 1.00 43.21 ? 135 ILE A CG1 1 ATOM 1017 C CG2 . ILE A 1 135 ? -30.114 26.107 34.054 1.00 44.53 ? 135 ILE A CG2 1 ATOM 1018 C CD1 . ILE A 1 135 ? -30.968 23.645 32.546 1.00 44.19 ? 135 ILE A CD1 1 ATOM 1019 N N . ALA A 1 136 ? -30.000 26.283 37.252 1.00 40.75 ? 136 ALA A N 1 ATOM 1020 C CA . ALA A 1 136 ? -29.973 27.525 38.019 1.00 42.01 ? 136 ALA A CA 1 ATOM 1021 C C . ALA A 1 136 ? -28.797 27.589 38.966 1.00 42.72 ? 136 ALA A C 1 ATOM 1022 O O . ALA A 1 136 ? -28.211 28.640 39.153 1.00 40.84 ? 136 ALA A O 1 ATOM 1023 C CB . ALA A 1 136 ? -31.251 27.683 38.813 1.00 44.42 ? 136 ALA A CB 1 ATOM 1024 N N . ASP A 1 137 ? -28.461 26.455 39.570 1.00 45.43 ? 137 ASP A N 1 ATOM 1025 C CA . ASP A 1 137 ? -27.347 26.388 40.512 1.00 45.73 ? 137 ASP A CA 1 ATOM 1026 C C . ASP A 1 137 ? -26.036 26.811 39.849 1.00 40.71 ? 137 ASP A C 1 ATOM 1027 O O . ASP A 1 137 ? -25.433 27.783 40.266 1.00 41.59 ? 137 ASP A O 1 ATOM 1028 C CB . ASP A 1 137 ? -27.238 24.969 41.129 1.00 51.76 ? 137 ASP A CB 1 ATOM 1029 C CG . ASP A 1 137 ? -26.619 24.972 42.549 1.00 57.14 ? 137 ASP A CG 1 ATOM 1030 O OD1 . ASP A 1 137 ? -27.276 25.459 43.510 1.00 61.15 ? 137 ASP A OD1 1 ATOM 1031 O OD2 . ASP A 1 137 ? -25.477 24.470 42.708 1.00 59.74 ? 137 ASP A OD2 1 ATOM 1032 N N . GLU A 1 138 ? -25.652 26.132 38.775 1.00 36.66 ? 138 GLU A N 1 ATOM 1033 C CA . GLU A 1 138 ? -24.411 26.427 38.066 1.00 35.52 ? 138 GLU A CA 1 ATOM 1034 C C . GLU A 1 138 ? -24.303 27.885 37.578 1.00 33.55 ? 138 GLU A C 1 ATOM 1035 O O . GLU A 1 138 ? -23.259 28.536 37.761 1.00 33.29 ? 138 GLU A O 1 ATOM 1036 C CB . GLU A 1 138 ? -24.241 25.438 36.902 1.00 37.17 ? 138 GLU A CB 1 ATOM 1037 C CG . GLU A 1 138 ? -23.200 25.774 35.783 1.00 48.06 ? 138 GLU A CG 1 ATOM 1038 C CD . GLU A 1 138 ? -21.717 25.725 36.235 1.00 53.18 ? 138 GLU A CD 1 ATOM 1039 O OE1 . GLU A 1 138 ? -21.491 25.954 37.456 1.00 56.96 ? 138 GLU A OE1 1 ATOM 1040 O OE2 . GLU A 1 138 ? -20.794 25.472 35.380 1.00 49.38 ? 138 GLU A OE2 1 ATOM 1041 N N . LEU A 1 139 ? -25.368 28.402 36.975 1.00 28.49 ? 139 LEU A N 1 ATOM 1042 C CA . LEU A 1 139 ? -25.359 29.766 36.442 1.00 27.65 ? 139 LEU A CA 1 ATOM 1043 C C . LEU A 1 139 ? -25.276 30.805 37.526 1.00 27.48 ? 139 LEU A C 1 ATOM 1044 O O . LEU A 1 139 ? -24.737 31.905 37.365 1.00 25.30 ? 139 LEU A O 1 ATOM 1045 C CB . LEU A 1 139 ? -26.637 30.021 35.649 1.00 25.68 ? 139 LEU A CB 1 ATOM 1046 C CG . LEU A 1 139 ? -26.834 29.096 34.463 1.00 29.30 ? 139 LEU A CG 1 ATOM 1047 C CD1 . LEU A 1 139 ? -28.087 29.492 33.734 1.00 33.23 ? 139 LEU A CD1 1 ATOM 1048 C CD2 . LEU A 1 139 ? -25.651 29.177 33.539 1.00 30.08 ? 139 LEU A CD2 1 ATOM 1049 N N . THR A 1 140 ? -25.852 30.411 38.633 1.00 27.22 ? 140 THR A N 1 ATOM 1050 C CA . THR A 1 140 ? -25.998 31.213 39.797 1.00 29.00 ? 140 THR A CA 1 ATOM 1051 C C . THR A 1 140 ? -24.773 31.270 40.766 1.00 30.08 ? 140 THR A C 1 ATOM 1052 O O . THR A 1 140 ? -24.723 32.120 41.665 1.00 31.96 ? 140 THR A O 1 ATOM 1053 C CB . THR A 1 140 ? -27.358 30.726 40.376 1.00 29.75 ? 140 THR A CB 1 ATOM 1054 O OG1 . THR A 1 140 ? -28.376 31.665 40.044 1.00 37.89 ? 140 THR A OG1 1 ATOM 1055 C CG2 . THR A 1 140 ? -27.354 30.334 41.780 1.00 29.28 ? 140 THR A CG2 1 ATOM 1056 N N . ASP A 1 141 ? -23.789 30.391 40.555 1.00 26.72 ? 141 ASP A N 1 ATOM 1057 C CA . ASP A 1 141 ? -22.552 30.327 41.329 1.00 23.05 ? 141 ASP A CA 1 ATOM 1058 C C . ASP A 1 141 ? -22.056 31.778 41.522 1.00 23.37 ? 141 ASP A C 1 ATOM 1059 O O . ASP A 1 141 ? -21.953 32.530 40.557 1.00 25.32 ? 141 ASP A O 1 ATOM 1060 C CB . ASP A 1 141 ? -21.559 29.481 40.523 1.00 19.89 ? 141 ASP A CB 1 ATOM 1061 C CG . ASP A 1 141 ? -20.215 29.361 41.161 1.00 20.07 ? 141 ASP A CG 1 ATOM 1062 O OD1 . ASP A 1 141 ? -19.850 30.166 42.034 1.00 20.45 ? 141 ASP A OD1 1 ATOM 1063 O OD2 . ASP A 1 141 ? -19.494 28.442 40.765 1.00 22.12 ? 141 ASP A OD2 1 ATOM 1064 N N . GLY A 1 142 ? -21.785 32.171 42.770 1.00 24.28 ? 142 GLY A N 1 ATOM 1065 C CA . GLY A 1 142 ? -21.352 33.529 43.091 1.00 19.14 ? 142 GLY A CA 1 ATOM 1066 C C . GLY A 1 142 ? -20.030 33.963 42.497 1.00 22.13 ? 142 GLY A C 1 ATOM 1067 O O . GLY A 1 142 ? -19.736 35.163 42.389 1.00 20.75 ? 142 GLY A O 1 ATOM 1068 N N . ARG A 1 143 ? -19.211 32.987 42.130 1.00 18.87 ? 143 ARG A N 1 ATOM 1069 C CA . ARG A 1 143 ? -17.938 33.276 41.506 1.00 17.96 ? 143 ARG A CA 1 ATOM 1070 C C . ARG A 1 143 ? -18.013 33.658 40.013 1.00 20.89 ? 143 ARG A C 1 ATOM 1071 O O . ARG A 1 143 ? -16.993 34.068 39.458 1.00 22.40 ? 143 ARG A O 1 ATOM 1072 C CB . ARG A 1 143 ? -17.046 32.075 41.650 1.00 16.99 ? 143 ARG A CB 1 ATOM 1073 C CG . ARG A 1 143 ? -16.805 31.669 43.077 1.00 16.04 ? 143 ARG A CG 1 ATOM 1074 C CD . ARG A 1 143 ? -15.747 30.593 43.136 1.00 12.66 ? 143 ARG A CD 1 ATOM 1075 N NE . ARG A 1 143 ? -15.386 30.283 44.515 1.00 17.60 ? 143 ARG A NE 1 ATOM 1076 C CZ . ARG A 1 143 ? -14.631 29.248 44.876 1.00 18.39 ? 143 ARG A CZ 1 ATOM 1077 N NH1 . ARG A 1 143 ? -14.160 28.416 43.953 1.00 17.97 ? 143 ARG A NH1 1 ATOM 1078 N NH2 . ARG A 1 143 ? -14.340 29.040 46.154 1.00 15.55 ? 143 ARG A NH2 1 ATOM 1079 N N . PHE A 1 144 ? -19.193 33.576 39.377 1.00 21.05 ? 144 PHE A N 1 ATOM 1080 C CA . PHE A 1 144 ? -19.348 33.889 37.939 1.00 20.04 ? 144 PHE A CA 1 ATOM 1081 C C . PHE A 1 144 ? -19.841 35.299 37.717 1.00 21.08 ? 144 PHE A C 1 ATOM 1082 O O . PHE A 1 144 ? -20.631 35.811 38.476 1.00 24.22 ? 144 PHE A O 1 ATOM 1083 C CB . PHE A 1 144 ? -20.375 32.970 37.248 1.00 14.21 ? 144 PHE A CB 1 ATOM 1084 C CG . PHE A 1 144 ? -19.843 31.638 36.841 1.00 15.21 ? 144 PHE A CG 1 ATOM 1085 C CD1 . PHE A 1 144 ? -18.515 31.481 36.468 1.00 19.00 ? 144 PHE A CD1 1 ATOM 1086 C CD2 . PHE A 1 144 ? -20.675 30.533 36.814 1.00 15.21 ? 144 PHE A CD2 1 ATOM 1087 C CE1 . PHE A 1 144 ? -18.018 30.229 36.069 1.00 18.90 ? 144 PHE A CE1 1 ATOM 1088 C CE2 . PHE A 1 144 ? -20.202 29.286 36.420 1.00 16.43 ? 144 PHE A CE2 1 ATOM 1089 C CZ . PHE A 1 144 ? -18.859 29.132 36.044 1.00 17.19 ? 144 PHE A CZ 1 ATOM 1090 N N . TYR A 1 145 ? -19.438 35.892 36.614 1.00 23.76 ? 145 TYR A N 1 ATOM 1091 C CA . TYR A 1 145 ? -19.901 37.212 36.248 1.00 22.36 ? 145 TYR A CA 1 ATOM 1092 C C . TYR A 1 145 ? -20.087 37.096 34.748 1.00 23.64 ? 145 TYR A C 1 ATOM 1093 O O . TYR A 1 145 ? -19.324 36.378 34.113 1.00 21.71 ? 145 TYR A O 1 ATOM 1094 C CB . TYR A 1 145 ? -18.851 38.280 36.545 1.00 23.94 ? 145 TYR A CB 1 ATOM 1095 C CG . TYR A 1 145 ? -19.297 39.618 36.036 1.00 24.75 ? 145 TYR A CG 1 ATOM 1096 C CD1 . TYR A 1 145 ? -20.350 40.284 36.645 1.00 28.12 ? 145 TYR A CD1 1 ATOM 1097 C CD2 . TYR A 1 145 ? -18.702 40.200 34.925 1.00 24.67 ? 145 TYR A CD2 1 ATOM 1098 C CE1 . TYR A 1 145 ? -20.794 41.482 36.171 1.00 27.69 ? 145 TYR A CE1 1 ATOM 1099 C CE2 . TYR A 1 145 ? -19.141 41.399 34.443 1.00 24.57 ? 145 TYR A CE2 1 ATOM 1100 C CZ . TYR A 1 145 ? -20.185 42.023 35.075 1.00 27.85 ? 145 TYR A CZ 1 ATOM 1101 O OH . TYR A 1 145 ? -20.646 43.194 34.629 1.00 28.02 ? 145 TYR A OH 1 ATOM 1102 N N . TYR A 1 146 ? -21.129 37.725 34.192 1.00 23.17 ? 146 TYR A N 1 ATOM 1103 C CA . TYR A 1 146 ? -21.381 37.678 32.737 1.00 21.40 ? 146 TYR A CA 1 ATOM 1104 C C . TYR A 1 146 ? -21.131 39.059 32.136 1.00 22.05 ? 146 TYR A C 1 ATOM 1105 O O . TYR A 1 146 ? -21.873 40.011 32.417 1.00 24.67 ? 146 TYR A O 1 ATOM 1106 C CB . TYR A 1 146 ? -22.792 37.154 32.454 1.00 19.54 ? 146 TYR A CB 1 ATOM 1107 C CG . TYR A 1 146 ? -23.004 35.805 33.104 1.00 18.85 ? 146 TYR A CG 1 ATOM 1108 C CD1 . TYR A 1 146 ? -22.592 34.648 32.476 1.00 21.60 ? 146 TYR A CD1 1 ATOM 1109 C CD2 . TYR A 1 146 ? -23.537 35.691 34.400 1.00 20.61 ? 146 TYR A CD2 1 ATOM 1110 C CE1 . TYR A 1 146 ? -22.689 33.407 33.124 1.00 21.37 ? 146 TYR A CE1 1 ATOM 1111 C CE2 . TYR A 1 146 ? -23.653 34.447 35.040 1.00 15.51 ? 146 TYR A CE2 1 ATOM 1112 C CZ . TYR A 1 146 ? -23.225 33.328 34.399 1.00 18.14 ? 146 TYR A CZ 1 ATOM 1113 O OH . TYR A 1 146 ? -23.300 32.099 34.981 1.00 17.40 ? 146 TYR A OH 1 ATOM 1114 N N . ALA A 1 147 ? -20.015 39.177 31.401 1.00 21.81 ? 147 ALA A N 1 ATOM 1115 C CA . ALA A 1 147 ? -19.570 40.418 30.786 1.00 19.73 ? 147 ALA A CA 1 ATOM 1116 C C . ALA A 1 147 ? -20.049 40.513 29.364 1.00 20.52 ? 147 ALA A C 1 ATOM 1117 O O . ALA A 1 147 ? -19.856 39.599 28.601 1.00 20.86 ? 147 ALA A O 1 ATOM 1118 C CB . ALA A 1 147 ? -18.065 40.503 30.832 1.00 19.51 ? 147 ALA A CB 1 ATOM 1119 N N . LYS A 1 148 ? -20.616 41.650 28.980 1.00 23.90 ? 148 LYS A N 1 ATOM 1120 C CA . LYS A 1 148 ? -21.132 41.798 27.629 1.00 24.24 ? 148 LYS A CA 1 ATOM 1121 C C . LYS A 1 148 ? -20.033 42.192 26.681 1.00 22.70 ? 148 LYS A C 1 ATOM 1122 O O . LYS A 1 148 ? -19.358 43.164 26.926 1.00 24.41 ? 148 LYS A O 1 ATOM 1123 C CB . LYS A 1 148 ? -22.248 42.830 27.592 1.00 25.61 ? 148 LYS A CB 1 ATOM 1124 C CG . LYS A 1 148 ? -23.050 42.780 26.318 1.00 34.18 ? 148 LYS A CG 1 ATOM 1125 C CD . LYS A 1 148 ? -24.232 43.740 26.379 1.00 44.18 ? 148 LYS A CD 1 ATOM 1126 C CE . LYS A 1 148 ? -25.191 43.607 25.156 1.00 52.66 ? 148 LYS A CE 1 ATOM 1127 N NZ . LYS A 1 148 ? -26.047 42.335 25.060 1.00 57.91 ? 148 LYS A NZ 1 ATOM 1128 N N . VAL A 1 149 ? -19.856 41.444 25.600 1.00 22.12 ? 149 VAL A N 1 ATOM 1129 C CA . VAL A 1 149 ? -18.823 41.759 24.629 1.00 23.82 ? 149 VAL A CA 1 ATOM 1130 C C . VAL A 1 149 ? -19.160 43.051 23.882 1.00 25.23 ? 149 VAL A C 1 ATOM 1131 O O . VAL A 1 149 ? -20.274 43.255 23.400 1.00 21.87 ? 149 VAL A O 1 ATOM 1132 C CB . VAL A 1 149 ? -18.592 40.590 23.641 1.00 23.79 ? 149 VAL A CB 1 ATOM 1133 C CG1 . VAL A 1 149 ? -17.494 40.904 22.646 1.00 19.05 ? 149 VAL A CG1 1 ATOM 1134 C CG2 . VAL A 1 149 ? -18.246 39.341 24.424 1.00 24.97 ? 149 VAL A CG2 1 ATOM 1135 N N . ALA A 1 150 ? -18.172 43.931 23.828 1.00 28.25 ? 150 ALA A N 1 ATOM 1136 C CA . ALA A 1 150 ? -18.285 45.224 23.165 1.00 31.38 ? 150 ALA A CA 1 ATOM 1137 C C . ALA A 1 150 ? -17.679 45.169 21.791 1.00 31.01 ? 150 ALA A C 1 ATOM 1138 O O . ALA A 1 150 ? -18.250 45.710 20.859 1.00 35.23 ? 150 ALA A O 1 ATOM 1139 C CB . ALA A 1 150 ? -17.606 46.323 23.986 1.00 28.03 ? 150 ALA A CB 1 ATOM 1140 N N . SER A 1 151 ? -16.565 44.459 21.645 1.00 33.17 ? 151 SER A N 1 ATOM 1141 C CA . SER A 1 151 ? -15.884 44.375 20.353 1.00 32.60 ? 151 SER A CA 1 ATOM 1142 C C . SER A 1 151 ? -14.877 43.253 20.269 1.00 29.39 ? 151 SER A C 1 ATOM 1143 O O . SER A 1 151 ? -14.336 42.863 21.270 1.00 27.88 ? 151 SER A O 1 ATOM 1144 C CB . SER A 1 151 ? -15.132 45.714 20.053 1.00 36.89 ? 151 SER A CB 1 ATOM 1145 O OG . SER A 1 151 ? -14.200 46.123 21.076 1.00 37.89 ? 151 SER A OG 1 ATOM 1146 N N . VAL A 1 152 ? -14.672 42.722 19.072 1.00 28.77 ? 152 VAL A N 1 ATOM 1147 C CA . VAL A 1 152 ? -13.643 41.711 18.811 1.00 27.82 ? 152 VAL A CA 1 ATOM 1148 C C . VAL A 1 152 ? -12.821 42.412 17.696 1.00 29.43 ? 152 VAL A C 1 ATOM 1149 O O . VAL A 1 152 ? -13.336 42.611 16.609 1.00 30.56 ? 152 VAL A O 1 ATOM 1150 C CB . VAL A 1 152 ? -14.246 40.396 18.291 1.00 21.08 ? 152 VAL A CB 1 ATOM 1151 C CG1 . VAL A 1 152 ? -13.168 39.390 17.997 1.00 20.08 ? 152 VAL A CG1 1 ATOM 1152 C CG2 . VAL A 1 152 ? -15.152 39.853 19.294 1.00 22.66 ? 152 VAL A CG2 1 ATOM 1153 N N . THR A 1 153 ? -11.604 42.872 17.970 1.00 28.17 ? 153 THR A N 1 ATOM 1154 C CA . THR A 1 153 ? -10.835 43.572 16.948 1.00 31.38 ? 153 THR A CA 1 ATOM 1155 C C . THR A 1 153 ? -9.517 42.908 16.570 1.00 32.55 ? 153 THR A C 1 ATOM 1156 O O . THR A 1 153 ? -8.897 42.268 17.405 1.00 33.26 ? 153 THR A O 1 ATOM 1157 C CB . THR A 1 153 ? -10.544 44.978 17.418 1.00 33.13 ? 153 THR A CB 1 ATOM 1158 O OG1 . THR A 1 153 ? -10.131 44.915 18.778 1.00 41.49 ? 153 THR A OG1 1 ATOM 1159 C CG2 . THR A 1 153 ? -11.797 45.816 17.377 1.00 38.52 ? 153 THR A CG2 1 ATOM 1160 N N . ASP A 1 154 ? -9.080 43.032 15.314 1.00 34.37 ? 154 ASP A N 1 ATOM 1161 C CA . ASP A 1 154 ? -7.800 42.418 14.947 1.00 36.12 ? 154 ASP A CA 1 ATOM 1162 C C . ASP A 1 154 ? -6.673 43.024 15.761 1.00 30.56 ? 154 ASP A C 1 ATOM 1163 O O . ASP A 1 154 ? -6.595 44.215 15.962 1.00 27.58 ? 154 ASP A O 1 ATOM 1164 C CB . ASP A 1 154 ? -7.485 42.459 13.432 1.00 45.34 ? 154 ASP A CB 1 ATOM 1165 C CG . ASP A 1 154 ? -6.060 41.885 13.095 1.00 53.00 ? 154 ASP A CG 1 ATOM 1166 O OD1 . ASP A 1 154 ? -5.797 40.631 13.186 1.00 58.22 ? 154 ASP A OD1 1 ATOM 1167 O OD2 . ASP A 1 154 ? -5.185 42.720 12.763 1.00 55.39 ? 154 ASP A OD2 1 ATOM 1168 N N . ALA A 1 155 ? -5.822 42.158 16.266 1.00 29.77 ? 155 ALA A N 1 ATOM 1169 C CA . ALA A 1 155 ? -4.733 42.589 17.094 1.00 28.12 ? 155 ALA A CA 1 ATOM 1170 C C . ALA A 1 155 ? -3.371 42.276 16.495 1.00 25.17 ? 155 ALA A C 1 ATOM 1171 O O . ALA A 1 155 ? -2.370 42.319 17.178 1.00 27.46 ? 155 ALA A O 1 ATOM 1172 C CB . ALA A 1 155 ? -4.893 41.975 18.521 1.00 28.34 ? 155 ALA A CB 1 ATOM 1173 N N . GLY A 1 156 ? -3.327 41.915 15.230 1.00 24.76 ? 156 GLY A N 1 ATOM 1174 C CA . GLY A 1 156 ? -2.041 41.655 14.634 1.00 22.96 ? 156 GLY A CA 1 ATOM 1175 C C . GLY A 1 156 ? -1.577 40.230 14.719 1.00 23.73 ? 156 GLY A C 1 ATOM 1176 O O . GLY A 1 156 ? -2.373 39.326 14.903 1.00 26.75 ? 156 GLY A O 1 ATOM 1177 N N . VAL A 1 157 ? -0.299 40.036 14.438 1.00 25.08 ? 157 VAL A N 1 ATOM 1178 C CA . VAL A 1 157 ? 0.323 38.730 14.490 1.00 26.98 ? 157 VAL A CA 1 ATOM 1179 C C . VAL A 1 157 ? 1.216 38.757 15.701 1.00 27.20 ? 157 VAL A C 1 ATOM 1180 O O . VAL A 1 157 ? 1.982 39.696 15.894 1.00 29.70 ? 157 VAL A O 1 ATOM 1181 C CB . VAL A 1 157 ? 1.096 38.408 13.230 1.00 23.32 ? 157 VAL A CB 1 ATOM 1182 C CG1 . VAL A 1 157 ? 1.737 37.072 13.353 1.00 26.53 ? 157 VAL A CG1 1 ATOM 1183 C CG2 . VAL A 1 157 ? 0.134 38.337 12.083 1.00 22.89 ? 157 VAL A CG2 1 ATOM 1184 N N . GLN A 1 158 ? 1.077 37.755 16.553 1.00 25.96 ? 158 GLN A N 1 ATOM 1185 C CA . GLN A 1 158 ? 1.850 37.733 17.765 1.00 24.86 ? 158 GLN A CA 1 ATOM 1186 C C . GLN A 1 158 ? 2.210 36.341 18.245 1.00 25.66 ? 158 GLN A C 1 ATOM 1187 O O . GLN A 1 158 ? 1.678 35.351 17.736 1.00 24.19 ? 158 GLN A O 1 ATOM 1188 C CB . GLN A 1 158 ? 1.036 38.408 18.838 1.00 26.82 ? 158 GLN A CB 1 ATOM 1189 C CG . GLN A 1 158 ? 0.783 39.848 18.589 1.00 31.53 ? 158 GLN A CG 1 ATOM 1190 C CD . GLN A 1 158 ? 0.284 40.536 19.817 1.00 35.24 ? 158 GLN A CD 1 ATOM 1191 O OE1 . GLN A 1 158 ? 0.829 40.362 20.922 1.00 40.35 ? 158 GLN A OE1 1 ATOM 1192 N NE2 . GLN A 1 158 ? -0.776 41.311 19.656 1.00 41.30 ? 158 GLN A NE2 1 ATOM 1193 N N . PRO A 1 159 ? 3.268 36.239 19.071 1.00 26.25 ? 159 PRO A N 1 ATOM 1194 C CA . PRO A 1 159 ? 3.672 34.942 19.619 1.00 25.97 ? 159 PRO A CA 1 ATOM 1195 C C . PRO A 1 159 ? 2.466 34.574 20.484 1.00 25.77 ? 159 PRO A C 1 ATOM 1196 O O . PRO A 1 159 ? 1.903 35.420 21.201 1.00 25.29 ? 159 PRO A O 1 ATOM 1197 C CB . PRO A 1 159 ? 4.902 35.270 20.460 1.00 25.42 ? 159 PRO A CB 1 ATOM 1198 C CG . PRO A 1 159 ? 4.831 36.763 20.667 1.00 30.62 ? 159 PRO A CG 1 ATOM 1199 C CD . PRO A 1 159 ? 4.276 37.264 19.369 1.00 27.11 ? 159 PRO A CD 1 ATOM 1200 N N . VAL A 1 160 ? 2.106 33.302 20.459 1.00 25.90 ? 160 VAL A N 1 ATOM 1201 C CA . VAL A 1 160 ? 0.900 32.878 21.112 1.00 22.06 ? 160 VAL A CA 1 ATOM 1202 C C . VAL A 1 160 ? 1.149 31.596 21.941 1.00 22.46 ? 160 VAL A C 1 ATOM 1203 O O . VAL A 1 160 ? 1.953 30.761 21.546 1.00 20.46 ? 160 VAL A O 1 ATOM 1204 C CB . VAL A 1 160 ? -0.094 32.810 19.934 1.00 19.43 ? 160 VAL A CB 1 ATOM 1205 C CG1 . VAL A 1 160 ? -0.439 31.465 19.558 1.00 20.76 ? 160 VAL A CG1 1 ATOM 1206 C CG2 . VAL A 1 160 ? -1.187 33.796 20.073 1.00 16.47 ? 160 VAL A CG2 1 ATOM 1207 N N . TYR A 1 161 ? 0.593 31.572 23.162 1.00 21.15 ? 161 TYR A N 1 ATOM 1208 C CA . TYR A 1 161 ? 0.731 30.482 24.146 1.00 21.15 ? 161 TYR A CA 1 ATOM 1209 C C . TYR A 1 161 ? -0.541 29.763 24.598 1.00 22.13 ? 161 TYR A C 1 ATOM 1210 O O . TYR A 1 161 ? -1.644 30.287 24.476 1.00 23.01 ? 161 TYR A O 1 ATOM 1211 C CB . TYR A 1 161 ? 1.305 31.042 25.448 1.00 18.09 ? 161 TYR A CB 1 ATOM 1212 C CG . TYR A 1 161 ? 2.549 31.822 25.280 1.00 18.07 ? 161 TYR A CG 1 ATOM 1213 C CD1 . TYR A 1 161 ? 2.515 33.086 24.727 1.00 19.19 ? 161 TYR A CD1 1 ATOM 1214 C CD2 . TYR A 1 161 ? 3.767 31.272 25.603 1.00 21.12 ? 161 TYR A CD2 1 ATOM 1215 C CE1 . TYR A 1 161 ? 3.643 33.782 24.486 1.00 22.00 ? 161 TYR A CE1 1 ATOM 1216 C CE2 . TYR A 1 161 ? 4.924 31.954 25.359 1.00 26.92 ? 161 TYR A CE2 1 ATOM 1217 C CZ . TYR A 1 161 ? 4.855 33.212 24.795 1.00 28.16 ? 161 TYR A CZ 1 ATOM 1218 O OH . TYR A 1 161 ? 6.011 33.877 24.496 1.00 35.22 ? 161 TYR A OH 1 ATOM 1219 N N . SER A 1 162 ? -0.368 28.563 25.142 1.00 20.00 ? 162 SER A N 1 ATOM 1220 C CA . SER A 1 162 ? -1.466 27.845 25.741 1.00 18.98 ? 162 SER A CA 1 ATOM 1221 C C . SER A 1 162 ? -0.935 26.909 26.791 1.00 19.42 ? 162 SER A C 1 ATOM 1222 O O . SER A 1 162 ? 0.270 26.688 26.889 1.00 16.63 ? 162 SER A O 1 ATOM 1223 C CB . SER A 1 162 ? -2.276 27.047 24.772 1.00 21.65 ? 162 SER A CB 1 ATOM 1224 O OG . SER A 1 162 ? -3.573 26.933 25.354 1.00 24.88 ? 162 SER A OG 1 ATOM 1225 N N . LEU A 1 163 ? -1.833 26.536 27.694 1.00 18.88 ? 163 LEU A N 1 ATOM 1226 C CA . LEU A 1 163 ? -1.541 25.598 28.764 1.00 22.70 ? 163 LEU A CA 1 ATOM 1227 C C . LEU A 1 163 ? -2.217 24.258 28.521 1.00 23.53 ? 163 LEU A C 1 ATOM 1228 O O . LEU A 1 163 ? -3.097 24.123 27.671 1.00 23.25 ? 163 LEU A O 1 ATOM 1229 C CB . LEU A 1 163 ? -2.105 26.100 30.112 1.00 18.00 ? 163 LEU A CB 1 ATOM 1230 C CG . LEU A 1 163 ? -1.424 27.260 30.811 1.00 20.05 ? 163 LEU A CG 1 ATOM 1231 C CD1 . LEU A 1 163 ? -2.012 27.361 32.185 1.00 17.94 ? 163 LEU A CD1 1 ATOM 1232 C CD2 . LEU A 1 163 ? 0.078 27.031 30.865 1.00 13.59 ? 163 LEU A CD2 1 ATOM 1233 N N . ARG A 1 164 ? -1.749 23.236 29.208 1.00 22.45 ? 164 ARG A N 1 ATOM 1234 C CA . ARG A 1 164 ? -2.472 22.026 29.115 1.00 20.68 ? 164 ARG A CA 1 ATOM 1235 C C . ARG A 1 164 ? -2.883 21.801 30.560 1.00 20.44 ? 164 ARG A C 1 ATOM 1236 O O . ARG A 1 164 ? -2.054 21.829 31.452 1.00 20.12 ? 164 ARG A O 1 ATOM 1237 C CB . ARG A 1 164 ? -1.632 20.903 28.599 1.00 22.59 ? 164 ARG A CB 1 ATOM 1238 C CG . ARG A 1 164 ? -2.521 19.728 28.271 1.00 27.76 ? 164 ARG A CG 1 ATOM 1239 C CD . ARG A 1 164 ? -1.935 18.474 28.839 1.00 34.61 ? 164 ARG A CD 1 ATOM 1240 N NE . ARG A 1 164 ? -1.290 17.676 27.801 1.00 39.52 ? 164 ARG A NE 1 ATOM 1241 C CZ . ARG A 1 164 ? -0.441 16.675 28.034 1.00 42.14 ? 164 ARG A CZ 1 ATOM 1242 N NH1 . ARG A 1 164 ? -0.091 16.334 29.287 1.00 38.47 ? 164 ARG A NH1 1 ATOM 1243 N NH2 . ARG A 1 164 ? -0.016 15.953 27.002 1.00 44.05 ? 164 ARG A NH2 1 ATOM 1244 N N . VAL A 1 165 ? -4.179 21.730 30.802 1.00 23.10 ? 165 VAL A N 1 ATOM 1245 C CA . VAL A 1 165 ? -4.668 21.489 32.127 1.00 23.18 ? 165 VAL A CA 1 ATOM 1246 C C . VAL A 1 165 ? -5.260 20.100 32.212 1.00 27.41 ? 165 VAL A C 1 ATOM 1247 O O . VAL A 1 165 ? -5.952 19.607 31.303 1.00 25.55 ? 165 VAL A O 1 ATOM 1248 C CB . VAL A 1 165 ? -5.661 22.558 32.613 1.00 25.03 ? 165 VAL A CB 1 ATOM 1249 C CG1 . VAL A 1 165 ? -5.589 23.790 31.735 1.00 25.26 ? 165 VAL A CG1 1 ATOM 1250 C CG2 . VAL A 1 165 ? -7.039 22.011 32.734 1.00 23.20 ? 165 VAL A CG2 1 ATOM 1251 N N . ASP A 1 166 ? -4.868 19.437 33.289 1.00 35.24 ? 166 ASP A N 1 ATOM 1252 C CA . ASP A 1 166 ? -5.278 18.088 33.632 1.00 40.35 ? 166 ASP A CA 1 ATOM 1253 C C . ASP A 1 166 ? -6.692 18.098 34.181 1.00 38.85 ? 166 ASP A C 1 ATOM 1254 O O . ASP A 1 166 ? -6.901 17.951 35.393 1.00 42.05 ? 166 ASP A O 1 ATOM 1255 C CB . ASP A 1 166 ? -4.335 17.584 34.696 1.00 50.61 ? 166 ASP A CB 1 ATOM 1256 C CG . ASP A 1 166 ? -3.327 16.657 34.149 1.00 59.62 ? 166 ASP A CG 1 ATOM 1257 O OD1 . ASP A 1 166 ? -2.754 16.960 33.056 1.00 65.37 ? 166 ASP A OD1 1 ATOM 1258 O OD2 . ASP A 1 166 ? -3.145 15.608 34.816 1.00 64.42 ? 166 ASP A OD2 1 ATOM 1259 N N . THR A 1 167 ? -7.657 18.106 33.273 1.00 33.99 ? 167 THR A N 1 ATOM 1260 C CA . THR A 1 167 ? -9.041 18.233 33.645 1.00 29.06 ? 167 THR A CA 1 ATOM 1261 C C . THR A 1 167 ? -9.895 17.840 32.445 1.00 28.80 ? 167 THR A C 1 ATOM 1262 O O . THR A 1 167 ? -9.537 18.073 31.297 1.00 29.96 ? 167 THR A O 1 ATOM 1263 C CB . THR A 1 167 ? -9.222 19.698 34.044 1.00 26.84 ? 167 THR A CB 1 ATOM 1264 O OG1 . THR A 1 167 ? -9.218 19.788 35.453 1.00 31.63 ? 167 THR A OG1 1 ATOM 1265 C CG2 . THR A 1 167 ? -10.403 20.286 33.527 1.00 22.56 ? 167 THR A CG2 1 ATOM 1266 N N . ALA A 1 168 ? -11.029 17.229 32.709 1.00 28.75 ? 168 ALA A N 1 ATOM 1267 C CA . ALA A 1 168 ? -11.905 16.796 31.641 1.00 30.99 ? 168 ALA A CA 1 ATOM 1268 C C . ALA A 1 168 ? -12.449 18.011 30.927 1.00 29.17 ? 168 ALA A C 1 ATOM 1269 O O . ALA A 1 168 ? -12.810 17.962 29.768 1.00 32.66 ? 168 ALA A O 1 ATOM 1270 C CB . ALA A 1 168 ? -13.052 15.985 32.227 1.00 32.43 ? 168 ALA A CB 1 ATOM 1271 N N . ASP A 1 169 ? -12.568 19.084 31.682 1.00 28.65 ? 169 ASP A N 1 ATOM 1272 C CA . ASP A 1 169 ? -13.081 20.358 31.209 1.00 24.79 ? 169 ASP A CA 1 ATOM 1273 C C . ASP A 1 169 ? -12.035 21.109 30.367 1.00 24.04 ? 169 ASP A C 1 ATOM 1274 O O . ASP A 1 169 ? -12.382 21.730 29.362 1.00 22.16 ? 169 ASP A O 1 ATOM 1275 C CB . ASP A 1 169 ? -13.470 21.169 32.442 1.00 24.72 ? 169 ASP A CB 1 ATOM 1276 C CG . ASP A 1 169 ? -14.213 22.426 32.108 1.00 28.39 ? 169 ASP A CG 1 ATOM 1277 O OD1 . ASP A 1 169 ? -14.816 22.486 31.011 1.00 35.64 ? 169 ASP A OD1 1 ATOM 1278 O OD2 . ASP A 1 169 ? -14.198 23.358 32.940 1.00 28.72 ? 169 ASP A OD2 1 ATOM 1279 N N . HIS A 1 170 ? -10.758 20.991 30.758 1.00 23.89 ? 170 HIS A N 1 ATOM 1280 C CA . HIS A 1 170 ? -9.628 21.651 30.078 1.00 23.16 ? 170 HIS A CA 1 ATOM 1281 C C . HIS A 1 170 ? -9.711 23.154 30.065 1.00 22.75 ? 170 HIS A C 1 ATOM 1282 O O . HIS A 1 170 ? -9.379 23.769 29.064 1.00 24.18 ? 170 HIS A O 1 ATOM 1283 C CB . HIS A 1 170 ? -9.550 21.176 28.626 1.00 25.60 ? 170 HIS A CB 1 ATOM 1284 C CG . HIS A 1 170 ? -9.144 19.747 28.496 1.00 27.67 ? 170 HIS A CG 1 ATOM 1285 N ND1 . HIS A 1 170 ? -7.946 19.277 28.986 1.00 30.92 ? 170 HIS A ND1 1 ATOM 1286 C CD2 . HIS A 1 170 ? -9.842 18.661 28.105 1.00 27.66 ? 170 HIS A CD2 1 ATOM 1287 C CE1 . HIS A 1 170 ? -7.933 17.962 28.924 1.00 31.70 ? 170 HIS A CE1 1 ATOM 1288 N NE2 . HIS A 1 170 ? -9.075 17.565 28.397 1.00 29.84 ? 170 HIS A NE2 1 ATOM 1289 N N . ALA A 1 171 ? -10.130 23.759 31.165 1.00 20.90 ? 171 ALA A N 1 ATOM 1290 C CA . ALA A 1 171 ? -10.272 25.205 31.192 1.00 19.06 ? 171 ALA A CA 1 ATOM 1291 C C . ALA A 1 171 ? -9.360 25.861 32.214 1.00 19.19 ? 171 ALA A C 1 ATOM 1292 O O . ALA A 1 171 ? -9.036 25.278 33.263 1.00 18.99 ? 171 ALA A O 1 ATOM 1293 C CB . ALA A 1 171 ? -11.718 25.568 31.505 1.00 15.13 ? 171 ALA A CB 1 ATOM 1294 N N . PHE A 1 172 ? -8.979 27.089 31.908 1.00 18.35 ? 172 PHE A N 1 ATOM 1295 C CA . PHE A 1 172 ? -8.151 27.874 32.791 1.00 16.60 ? 172 PHE A CA 1 ATOM 1296 C C . PHE A 1 172 ? -8.602 29.314 32.621 1.00 15.99 ? 172 PHE A C 1 ATOM 1297 O O . PHE A 1 172 ? -9.399 29.627 31.736 1.00 14.30 ? 172 PHE A O 1 ATOM 1298 C CB . PHE A 1 172 ? -6.633 27.626 32.612 1.00 16.01 ? 172 PHE A CB 1 ATOM 1299 C CG . PHE A 1 172 ? -6.088 27.954 31.250 1.00 17.72 ? 172 PHE A CG 1 ATOM 1300 C CD1 . PHE A 1 172 ? -6.462 27.204 30.131 1.00 14.18 ? 172 PHE A CD1 1 ATOM 1301 C CD2 . PHE A 1 172 ? -5.203 29.027 31.094 1.00 15.64 ? 172 PHE A CD2 1 ATOM 1302 C CE1 . PHE A 1 172 ? -5.994 27.517 28.893 1.00 16.27 ? 172 PHE A CE1 1 ATOM 1303 C CE2 . PHE A 1 172 ? -4.723 29.350 29.857 1.00 16.93 ? 172 PHE A CE2 1 ATOM 1304 C CZ . PHE A 1 172 ? -5.117 28.594 28.736 1.00 19.55 ? 172 PHE A CZ 1 ATOM 1305 N N . ILE A 1 173 ? -8.186 30.150 33.549 1.00 14.51 ? 173 ILE A N 1 ATOM 1306 C CA . ILE A 1 173 ? -8.598 31.530 33.621 1.00 13.90 ? 173 ILE A CA 1 ATOM 1307 C C . ILE A 1 173 ? -7.482 32.385 33.083 1.00 18.92 ? 173 ILE A C 1 ATOM 1308 O O . ILE A 1 173 ? -6.335 32.306 33.567 1.00 16.91 ? 173 ILE A O 1 ATOM 1309 C CB . ILE A 1 173 ? -8.934 31.890 35.117 1.00 14.19 ? 173 ILE A CB 1 ATOM 1310 C CG1 . ILE A 1 173 ? -9.971 30.909 35.688 1.00 14.62 ? 173 ILE A CG1 1 ATOM 1311 C CG2 . ILE A 1 173 ? -9.400 33.278 35.264 1.00 13.61 ? 173 ILE A CG2 1 ATOM 1312 C CD1 . ILE A 1 173 ? -11.207 30.677 34.825 1.00 11.61 ? 173 ILE A CD1 1 ATOM 1313 N N . THR A 1 174 ? -7.829 33.220 32.093 1.00 18.98 ? 174 THR A N 1 ATOM 1314 C CA . THR A 1 174 ? -6.885 34.094 31.417 1.00 17.46 ? 174 THR A CA 1 ATOM 1315 C C . THR A 1 174 ? -7.521 35.472 31.404 1.00 17.96 ? 174 THR A C 1 ATOM 1316 O O . THR A 1 174 ? -8.447 35.701 30.652 1.00 21.38 ? 174 THR A O 1 ATOM 1317 C CB . THR A 1 174 ? -6.657 33.615 29.966 1.00 17.63 ? 174 THR A CB 1 ATOM 1318 O OG1 . THR A 1 174 ? -7.918 33.455 29.315 1.00 19.03 ? 174 THR A OG1 1 ATOM 1319 C CG2 . THR A 1 174 ? -5.955 32.322 29.964 1.00 12.76 ? 174 THR A CG2 1 ATOM 1320 N N . ASN A 1 175 ? -7.005 36.392 32.201 1.00 16.37 ? 175 ASN A N 1 ATOM 1321 C CA . ASN A 1 175 ? -7.587 37.715 32.297 1.00 16.49 ? 175 ASN A CA 1 ATOM 1322 C C . ASN A 1 175 ? -9.060 37.702 32.795 1.00 18.30 ? 175 ASN A C 1 ATOM 1323 O O . ASN A 1 175 ? -9.877 38.552 32.407 1.00 19.68 ? 175 ASN A O 1 ATOM 1324 C CB . ASN A 1 175 ? -7.465 38.464 30.978 1.00 19.37 ? 175 ASN A CB 1 ATOM 1325 C CG . ASN A 1 175 ? -6.049 38.988 30.714 1.00 19.44 ? 175 ASN A CG 1 ATOM 1326 O OD1 . ASN A 1 175 ? -5.159 38.900 31.556 1.00 21.40 ? 175 ASN A OD1 1 ATOM 1327 N ND2 . ASN A 1 175 ? -5.848 39.534 29.534 1.00 21.89 ? 175 ASN A ND2 1 ATOM 1328 N N . GLY A 1 176 ? -9.386 36.790 33.708 1.00 17.77 ? 176 GLY A N 1 ATOM 1329 C CA . GLY A 1 176 ? -10.739 36.733 34.189 1.00 16.87 ? 176 GLY A CA 1 ATOM 1330 C C . GLY A 1 176 ? -11.619 35.858 33.336 1.00 18.44 ? 176 GLY A C 1 ATOM 1331 O O . GLY A 1 176 ? -12.590 35.299 33.862 1.00 17.93 ? 176 GLY A O 1 ATOM 1332 N N . PHE A 1 177 ? -11.266 35.696 32.053 1.00 16.71 ? 177 PHE A N 1 ATOM 1333 C CA . PHE A 1 177 ? -12.033 34.891 31.070 1.00 16.14 ? 177 PHE A CA 1 ATOM 1334 C C . PHE A 1 177 ? -11.765 33.404 31.263 1.00 15.61 ? 177 PHE A C 1 ATOM 1335 O O . PHE A 1 177 ? -10.652 33.038 31.541 1.00 19.82 ? 177 PHE A O 1 ATOM 1336 C CB . PHE A 1 177 ? -11.595 35.273 29.623 1.00 14.09 ? 177 PHE A CB 1 ATOM 1337 C CG . PHE A 1 177 ? -12.058 36.645 29.167 1.00 12.59 ? 177 PHE A CG 1 ATOM 1338 C CD1 . PHE A 1 177 ? -11.361 37.806 29.533 1.00 15.64 ? 177 PHE A CD1 1 ATOM 1339 C CD2 . PHE A 1 177 ? -13.170 36.788 28.363 1.00 16.19 ? 177 PHE A CD2 1 ATOM 1340 C CE1 . PHE A 1 177 ? -11.780 39.048 29.096 1.00 13.47 ? 177 PHE A CE1 1 ATOM 1341 C CE2 . PHE A 1 177 ? -13.580 38.052 27.932 1.00 15.53 ? 177 PHE A CE2 1 ATOM 1342 C CZ . PHE A 1 177 ? -12.886 39.167 28.286 1.00 11.48 ? 177 PHE A CZ 1 ATOM 1343 N N . VAL A 1 178 ? -12.739 32.564 30.985 1.00 16.03 ? 178 VAL A N 1 ATOM 1344 C CA . VAL A 1 178 ? -12.567 31.125 31.117 1.00 17.03 ? 178 VAL A CA 1 ATOM 1345 C C . VAL A 1 178 ? -12.144 30.596 29.748 1.00 18.70 ? 178 VAL A C 1 ATOM 1346 O O . VAL A 1 178 ? -12.954 30.592 28.813 1.00 18.77 ? 178 VAL A O 1 ATOM 1347 C CB . VAL A 1 178 ? -13.868 30.426 31.527 1.00 15.06 ? 178 VAL A CB 1 ATOM 1348 C CG1 . VAL A 1 178 ? -13.644 28.961 31.599 1.00 10.78 ? 178 VAL A CG1 1 ATOM 1349 C CG2 . VAL A 1 178 ? -14.359 30.944 32.912 1.00 13.66 ? 178 VAL A CG2 1 ATOM 1350 N N . SER A 1 179 ? -10.864 30.233 29.619 1.00 17.78 ? 179 SER A N 1 ATOM 1351 C CA . SER A 1 179 ? -10.300 29.722 28.371 1.00 16.04 ? 179 SER A CA 1 ATOM 1352 C C . SER A 1 179 ? -10.215 28.214 28.284 1.00 18.16 ? 179 SER A C 1 ATOM 1353 O O . SER A 1 179 ? -10.090 27.524 29.295 1.00 19.21 ? 179 SER A O 1 ATOM 1354 C CB . SER A 1 179 ? -8.875 30.226 28.182 1.00 13.65 ? 179 SER A CB 1 ATOM 1355 O OG . SER A 1 179 ? -8.785 31.581 27.775 1.00 17.08 ? 179 SER A OG 1 ATOM 1356 N N . HIS A 1 180 ? -10.325 27.701 27.068 1.00 15.96 ? 180 HIS A N 1 ATOM 1357 C CA . HIS A 1 180 ? -10.143 26.287 26.897 1.00 20.14 ? 180 HIS A CA 1 ATOM 1358 C C . HIS A 1 180 ? -8.687 26.031 26.448 1.00 22.12 ? 180 HIS A C 1 ATOM 1359 O O . HIS A 1 180 ? -8.119 26.872 25.768 1.00 25.99 ? 180 HIS A O 1 ATOM 1360 C CB . HIS A 1 180 ? -11.094 25.770 25.850 1.00 18.48 ? 180 HIS A CB 1 ATOM 1361 C CG . HIS A 1 180 ? -11.035 24.291 25.694 1.00 21.64 ? 180 HIS A CG 1 ATOM 1362 N ND1 . HIS A 1 180 ? -10.026 23.654 24.997 1.00 26.40 ? 180 HIS A ND1 1 ATOM 1363 C CD2 . HIS A 1 180 ? -11.842 23.314 26.170 1.00 23.53 ? 180 HIS A CD2 1 ATOM 1364 C CE1 . HIS A 1 180 ? -10.216 22.349 25.049 1.00 23.13 ? 180 HIS A CE1 1 ATOM 1365 N NE2 . HIS A 1 180 ? -11.311 22.116 25.754 1.00 25.79 ? 180 HIS A NE2 1 ATOM 1366 N N . ASN A 1 181 ? -8.087 24.895 26.848 1.00 26.61 ? 181 ASN A N 1 ATOM 1367 C CA . ASN A 1 181 ? -6.704 24.480 26.455 1.00 28.32 ? 181 ASN A CA 1 ATOM 1368 C C . ASN A 1 181 ? -6.459 24.766 24.959 1.00 28.62 ? 181 ASN A C 1 ATOM 1369 O O . ASN A 1 181 ? -7.390 24.502 24.140 1.00 27.92 ? 181 ASN A O 1 ATOM 1370 C CB . ASN A 1 181 ? -6.515 22.948 26.572 1.00 28.82 ? 181 ASN A CB 1 ATOM 1371 C CG . ASN A 1 181 ? -6.299 22.486 27.939 1.00 27.35 ? 181 ASN A CG 1 ATOM 1372 O OD1 . ASN A 1 181 ? -6.227 23.257 28.866 1.00 38.35 ? 181 ASN A OD1 1 ATOM 1373 N ND2 . ASN A 1 181 ? -6.213 21.196 28.092 1.00 26.49 ? 181 ASN A ND2 1 ATOM 1374 O OXT . ASN A 1 181 ? -5.307 25.129 24.620 1.00 27.84 ? 181 ASN A OXT 1 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 1998-06-24 2 'Structure model' 1 1 2008-03-24 3 'Structure model' 1 2 2011-07-13 #