data_8EN4
# 
_entry.id   8EN4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.367 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8EN4         pdb_00008en4 10.2210/pdb8en4/pdb 
WWPDB D_1000267282 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8EN4 
_pdbx_database_status.recvd_initial_deposition_date   2022-09-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Kher, G.'        1 ? 
'Sabin, C.'       2 ? 
'Koromyslova, A.' 3 ? 
'Pancera, M.'     4 ? 
'Hansman, G.'     5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of GII.4 norovirus in complex with Nanobody 53' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kher, G.'        1 ? 
primary 'Sabin, C.'       2 ? 
primary 'Koromyslova, A.' 3 ? 
primary 'Pancera, M.'     4 ? 
primary 'Hansman, G.'     5 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8EN4 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     108.411 
_cell.length_a_esd                 ? 
_cell.length_b                     137.292 
_cell.length_b_esd                 ? 
_cell.length_c                     140.176 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8EN4 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man VP1            34132.039 2   ? ? ? ? 
2 polymer     man 'Nanobody 53'  13391.939 2   ? ? ? ? 
3 non-polymer nat 1,2-ETHANEDIOL 62.068    3   ? ? ? ? 
4 water       nat water          18.015    113 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMG
;
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMG
;
B,A ? 
2 'polypeptide(L)' no no 
;QVQLQESGGGLVQPGGSLRLSCAASGDIFSIYLMGWYRQSPGKQRELVATITSSGETKHVYSVKGRFTISRENAKNAWYL
QMNSLKPEDTGVYYCHAVTGVIASSWGQGTQVTVSSHHHHHH
;
;QVQLQESGGGLVQPGGSLRLSCAASGDIFSIYLMGWYRQSPGKQRELVATITSSGETKHVYSVKGRFTISRENAKNAWYL
QMNSLKPEDTGVYYCHAVTGVIASSWGQGTQVTVSSHHHHHH
;
C,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   LYS n 
1 3   PRO n 
1 4   PHE n 
1 5   SER n 
1 6   VAL n 
1 7   PRO n 
1 8   VAL n 
1 9   LEU n 
1 10  THR n 
1 11  VAL n 
1 12  GLU n 
1 13  GLU n 
1 14  MET n 
1 15  THR n 
1 16  ASN n 
1 17  SER n 
1 18  ARG n 
1 19  PHE n 
1 20  PRO n 
1 21  ILE n 
1 22  PRO n 
1 23  LEU n 
1 24  GLU n 
1 25  LYS n 
1 26  LEU n 
1 27  PHE n 
1 28  THR n 
1 29  GLY n 
1 30  PRO n 
1 31  SER n 
1 32  SER n 
1 33  ALA n 
1 34  PHE n 
1 35  VAL n 
1 36  VAL n 
1 37  GLN n 
1 38  PRO n 
1 39  GLN n 
1 40  ASN n 
1 41  GLY n 
1 42  ARG n 
1 43  CYS n 
1 44  THR n 
1 45  THR n 
1 46  ASP n 
1 47  GLY n 
1 48  VAL n 
1 49  LEU n 
1 50  LEU n 
1 51  GLY n 
1 52  THR n 
1 53  THR n 
1 54  GLN n 
1 55  LEU n 
1 56  SER n 
1 57  PRO n 
1 58  VAL n 
1 59  ASN n 
1 60  ILE n 
1 61  CYS n 
1 62  THR n 
1 63  PHE n 
1 64  ARG n 
1 65  GLY n 
1 66  ASP n 
1 67  VAL n 
1 68  THR n 
1 69  HIS n 
1 70  ILE n 
1 71  THR n 
1 72  GLY n 
1 73  SER n 
1 74  ARG n 
1 75  ASN n 
1 76  TYR n 
1 77  THR n 
1 78  MET n 
1 79  ASN n 
1 80  LEU n 
1 81  ALA n 
1 82  SER n 
1 83  GLN n 
1 84  ASN n 
1 85  TRP n 
1 86  ASN n 
1 87  ASP n 
1 88  TYR n 
1 89  ASP n 
1 90  PRO n 
1 91  THR n 
1 92  GLU n 
1 93  GLU n 
1 94  ILE n 
1 95  PRO n 
1 96  ALA n 
1 97  PRO n 
1 98  LEU n 
1 99  GLY n 
1 100 THR n 
1 101 PRO n 
1 102 ASP n 
1 103 PHE n 
1 104 VAL n 
1 105 GLY n 
1 106 LYS n 
1 107 ILE n 
1 108 GLN n 
1 109 GLY n 
1 110 VAL n 
1 111 LEU n 
1 112 THR n 
1 113 GLN n 
1 114 THR n 
1 115 THR n 
1 116 ARG n 
1 117 THR n 
1 118 ASP n 
1 119 GLY n 
1 120 SER n 
1 121 THR n 
1 122 ARG n 
1 123 GLY n 
1 124 HIS n 
1 125 LYS n 
1 126 ALA n 
1 127 THR n 
1 128 VAL n 
1 129 TYR n 
1 130 THR n 
1 131 GLY n 
1 132 SER n 
1 133 ALA n 
1 134 ASP n 
1 135 PHE n 
1 136 ALA n 
1 137 PRO n 
1 138 LYS n 
1 139 LEU n 
1 140 GLY n 
1 141 ARG n 
1 142 VAL n 
1 143 GLN n 
1 144 PHE n 
1 145 GLU n 
1 146 THR n 
1 147 ASP n 
1 148 THR n 
1 149 ASP n 
1 150 ARG n 
1 151 ASP n 
1 152 PHE n 
1 153 GLU n 
1 154 ALA n 
1 155 ASN n 
1 156 GLN n 
1 157 ASN n 
1 158 THR n 
1 159 LYS n 
1 160 PHE n 
1 161 THR n 
1 162 PRO n 
1 163 VAL n 
1 164 GLY n 
1 165 VAL n 
1 166 ILE n 
1 167 GLN n 
1 168 ASP n 
1 169 GLY n 
1 170 GLY n 
1 171 THR n 
1 172 THR n 
1 173 HIS n 
1 174 ARG n 
1 175 ASN n 
1 176 GLU n 
1 177 PRO n 
1 178 GLN n 
1 179 GLN n 
1 180 TRP n 
1 181 VAL n 
1 182 LEU n 
1 183 PRO n 
1 184 SER n 
1 185 TYR n 
1 186 SER n 
1 187 GLY n 
1 188 ARG n 
1 189 ASN n 
1 190 THR n 
1 191 HIS n 
1 192 ASN n 
1 193 VAL n 
1 194 HIS n 
1 195 LEU n 
1 196 ALA n 
1 197 PRO n 
1 198 ALA n 
1 199 VAL n 
1 200 ALA n 
1 201 PRO n 
1 202 THR n 
1 203 PHE n 
1 204 PRO n 
1 205 GLY n 
1 206 GLU n 
1 207 GLN n 
1 208 LEU n 
1 209 LEU n 
1 210 PHE n 
1 211 PHE n 
1 212 ARG n 
1 213 SER n 
1 214 THR n 
1 215 MET n 
1 216 PRO n 
1 217 GLY n 
1 218 CYS n 
1 219 SER n 
1 220 GLY n 
1 221 TYR n 
1 222 PRO n 
1 223 ASN n 
1 224 MET n 
1 225 ASP n 
1 226 LEU n 
1 227 ASP n 
1 228 CYS n 
1 229 LEU n 
1 230 LEU n 
1 231 PRO n 
1 232 GLN n 
1 233 GLU n 
1 234 TRP n 
1 235 VAL n 
1 236 GLN n 
1 237 TYR n 
1 238 PHE n 
1 239 TYR n 
1 240 GLN n 
1 241 GLU n 
1 242 ALA n 
1 243 ALA n 
1 244 PRO n 
1 245 ALA n 
1 246 GLN n 
1 247 SER n 
1 248 ASP n 
1 249 VAL n 
1 250 ALA n 
1 251 LEU n 
1 252 LEU n 
1 253 ARG n 
1 254 PHE n 
1 255 VAL n 
1 256 ASN n 
1 257 PRO n 
1 258 ASP n 
1 259 THR n 
1 260 GLY n 
1 261 ARG n 
1 262 VAL n 
1 263 LEU n 
1 264 PHE n 
1 265 GLU n 
1 266 CYS n 
1 267 LYS n 
1 268 LEU n 
1 269 HIS n 
1 270 LYS n 
1 271 SER n 
1 272 GLY n 
1 273 TYR n 
1 274 VAL n 
1 275 THR n 
1 276 VAL n 
1 277 ALA n 
1 278 HIS n 
1 279 THR n 
1 280 GLY n 
1 281 GLN n 
1 282 HIS n 
1 283 ASP n 
1 284 LEU n 
1 285 VAL n 
1 286 ILE n 
1 287 PRO n 
1 288 PRO n 
1 289 ASN n 
1 290 GLY n 
1 291 TYR n 
1 292 PHE n 
1 293 ARG n 
1 294 PHE n 
1 295 ASP n 
1 296 SER n 
1 297 TRP n 
1 298 VAL n 
1 299 ASN n 
1 300 GLN n 
1 301 PHE n 
1 302 TYR n 
1 303 THR n 
1 304 LEU n 
1 305 ALA n 
1 306 PRO n 
1 307 MET n 
1 308 GLY n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  ASP n 
2 28  ILE n 
2 29  PHE n 
2 30  SER n 
2 31  ILE n 
2 32  TYR n 
2 33  LEU n 
2 34  MET n 
2 35  GLY n 
2 36  TRP n 
2 37  TYR n 
2 38  ARG n 
2 39  GLN n 
2 40  SER n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLN n 
2 45  ARG n 
2 46  GLU n 
2 47  LEU n 
2 48  VAL n 
2 49  ALA n 
2 50  THR n 
2 51  ILE n 
2 52  THR n 
2 53  SER n 
2 54  SER n 
2 55  GLY n 
2 56  GLU n 
2 57  THR n 
2 58  LYS n 
2 59  HIS n 
2 60  VAL n 
2 61  TYR n 
2 62  SER n 
2 63  VAL n 
2 64  LYS n 
2 65  GLY n 
2 66  ARG n 
2 67  PHE n 
2 68  THR n 
2 69  ILE n 
2 70  SER n 
2 71  ARG n 
2 72  GLU n 
2 73  ASN n 
2 74  ALA n 
2 75  LYS n 
2 76  ASN n 
2 77  ALA n 
2 78  TRP n 
2 79  TYR n 
2 80  LEU n 
2 81  GLN n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  LYS n 
2 87  PRO n 
2 88  GLU n 
2 89  ASP n 
2 90  THR n 
2 91  GLY n 
2 92  VAL n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  HIS n 
2 97  ALA n 
2 98  VAL n 
2 99  THR n 
2 100 GLY n 
2 101 VAL n 
2 102 ILE n 
2 103 ALA n 
2 104 SER n 
2 105 SER n 
2 106 TRP n 
2 107 GLY n 
2 108 GLN n 
2 109 GLY n 
2 110 THR n 
2 111 GLN n 
2 112 VAL n 
2 113 THR n 
2 114 VAL n 
2 115 SER n 
2 116 SER n 
2 117 HIS n 
2 118 HIS n 
2 119 HIS n 
2 120 HIS n 
2 121 HIS n 
2 122 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 308 ? ? ? ? ? ? ? ? ? Norovirus       142786 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 122 ? ? ? ? ? ? ? ? ? 'Vicugna pacos' 30538  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP K4LM89_9CALI K4LM89 ? 1 
;TKPFSVPVLTVEEMTNSRFPIPLEKLFTGPSSAFVVQPQNGRCTTDGVLLGTTQLSPVNICTFRGDVTHITGSRNYTMNL
ASQNWNDYDPTEEIPAPLGTPDFVGKIQGVLTQTTRTDGSTRGHKATVYTGSADFAPKLGRVQFETDTDRDFEANQNTKF
TPVGVIQDGGTTHRNEPQQWVLPSYSGRNTHNVHLAPAVAPTFPGEQLLFFRSTMPGCSGYPNMDLDCLLPQEWVQYFYQ
EAAPAQSDVALLRFVNPDTGRVLFECKLHKSGYVTVAHTGQHDLVIPPNGYFRFDSWVNQFYTLAPMG
;
224 
2 PDB 8EN4         8EN4   ? 2 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8EN4 B 1 ? 308 ? K4LM89 224 ? 531 ? 224 531 
2 2 8EN4 C 1 ? 122 ? 8EN4   1   ? 122 ? 1   122 
3 2 8EN4 D 1 ? 122 ? 8EN4   1   ? 122 ? 1   122 
4 1 8EN4 A 1 ? 308 ? K4LM89 224 ? 531 ? 224 531 
# 
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 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
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 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
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 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8EN4 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.6 M ammonium sulfate, 0.08 M sodium acetate, and 20% [v/v] glycerol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-22 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918400 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL14-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.918400 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL14-1 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          41.960 
_reflns.entry_id                                       8EN4 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.300 
_reflns.d_resolution_low                               54.100 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     46757 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.700 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.100 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.800 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           561 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.075 
_reflns.pdbx_Rpim_I_all                                0.033 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       236322 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
_reflns.pdbx_CC_split_method                           ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.300 2.380  ? ? 22404 ? ? ? 4469 98.300 ? ? ? ? 0.432 ? ? ? ? ? ? ? ? 5.000 ? ? ? 3.100  0.482 0.211 ? 1 1 0.931 ? ? ? ? ? ? ? ? 
? ? 
8.900 54.100 ? ? 4197  ? ? ? 890  99.200 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 4.700 ? ? ? 25.300 0.040 0.017 ? 2 1 0.998 ? ? ? ? ? ? ? ? 
? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                117.740 
_refine.B_iso_mean                               50.1943 
_refine.B_iso_min                                28.380 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8EN4 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.3000 
_refine.ls_d_res_low                             49.0400 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     46628 
_refine.ls_number_reflns_R_free                  3837 
_refine.ls_number_reflns_R_work                  85578 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.5800 
_refine.ls_percent_reflns_R_free                 4.2900 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2160 
_refine.ls_R_factor_R_free                       0.2483 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2146 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4oos 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 30.6300 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3200 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.3000 
_refine_hist.d_res_low                        49.0400 
_refine_hist.number_atoms_solvent             113 
_refine_hist.number_atoms_total               6661 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       841 
_refine_hist.pdbx_B_iso_mean_ligand           45.24 
_refine_hist.pdbx_B_iso_mean_solvent          41.01 
_refine_hist.pdbx_number_atoms_protein        6536 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.3000 2.3300 . . 150 3132 100.0000 . . . 0.3906 0.0000 0.3491 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3300 2.3600 . . 143 3210 100.0000 . . . 0.3949 0.0000 0.3366 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3600 2.3900 . . 136 3149 100.0000 . . . 0.3416 0.0000 0.3099 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.3900 2.4300 . . 163 3164 99.0000  . . . 0.3528 0.0000 0.3177 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4300 2.4600 . . 129 3201 100.0000 . . . 0.3310 0.0000 0.2940 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.4600 2.5000 . . 148 3152 100.0000 . . . 0.3532 0.0000 0.2854 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5000 2.5400 . . 140 3204 100.0000 . . . 0.3411 0.0000 0.2906 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5400 2.5900 . . 140 3112 100.0000 . . . 0.2998 0.0000 0.2806 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5900 2.6300 . . 142 3174 100.0000 . . . 0.3885 0.0000 0.2712 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6300 2.6800 . . 136 3210 99.0000  . . . 0.3027 0.0000 0.2809 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6800 2.7400 . . 136 3168 100.0000 . . . 0.3412 0.0000 0.2705 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7400 2.8000 . . 144 3207 99.0000  . . . 0.2903 0.0000 0.2793 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8000 2.8600 . . 149 3120 99.0000  . . . 0.3383 0.0000 0.2782 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8600 2.9300 . . 128 3145 99.0000  . . . 0.3253 0.0000 0.2790 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.9300 3.0100 . . 149 3187 99.0000  . . . 0.3066 0.0000 0.2610 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0100 3.1000 . . 145 3170 100.0000 . . . 0.2828 0.0000 0.2507 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.1000 3.2000 . . 137 3180 100.0000 . . . 0.2709 0.0000 0.2445 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.2000 3.3200 . . 149 3135 99.0000  . . . 0.2492 0.0000 0.2403 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.3200 3.4500 . . 140 3161 99.0000  . . . 0.2671 0.0000 0.2279 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.4500 3.6100 . . 144 3175 99.0000  . . . 0.2267 0.0000 0.2279 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.6100 3.8000 . . 143 3144 100.0000 . . . 0.2723 0.0000 0.2072 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.8000 4.0300 . . 141 3194 100.0000 . . . 0.2104 0.0000 0.1886 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.0300 4.3500 . . 144 3173 100.0000 . . . 0.2262 0.0000 0.1636 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.3500 4.7800 . . 140 3168 100.0000 . . . 0.1751 0.0000 0.1490 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.7800 5.4700 . . 143 3174 99.0000  . . . 0.1710 0.0000 0.1575 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.4800 6.8900 . . 143 3168 100.0000 . . . 0.1793 0.0000 0.1675 . . . . . . . . . . . 
# 
_struct.entry_id                     8EN4 
_struct.title                        'Structure of GII.4 norovirus in complex with Nanobody 53' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8EN4 
_struct_keywords.text            'norovirus, nanobody, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 1 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 231 ? ALA A 242 ? PRO B 454 ALA B 465 1 ? 12 
HELX_P HELX_P2  AA2 ILE B 28  ? ILE B 31  ? ILE C 28  ILE C 31  5 ? 4  
HELX_P HELX_P3  AA3 TYR B 61  ? LYS B 64  ? TYR C 61  LYS C 64  5 ? 4  
HELX_P HELX_P4  AA4 LYS B 86  ? THR B 90  ? LYS C 86  THR C 90  5 ? 5  
HELX_P HELX_P5  AA5 ASP C 27  ? ILE C 31  ? ASP D 27  ILE D 31  5 ? 5  
HELX_P HELX_P6  AA6 TYR C 61  ? LYS C 64  ? TYR D 61  LYS D 64  5 ? 4  
HELX_P HELX_P7  AA7 LYS C 86  ? THR C 90  ? LYS D 86  THR D 90  5 ? 5  
HELX_P HELX_P8  AA8 THR D 10  ? MET D 14  ? THR A 233 MET A 237 5 ? 5  
HELX_P HELX_P9  AA9 ALA D 136 ? LEU D 139 ? ALA A 359 LEU A 362 5 ? 4  
HELX_P HELX_P10 AB1 PRO D 231 ? ALA D 242 ? PRO A 454 ALA A 465 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 95 SG ? ? C CYS 22 C CYS 95 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
disulf2 disulf ? ? C CYS 22 SG ? ? ? 1_555 C CYS 95 SG ? ? D CYS 22 D CYS 95 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 176 A . ? GLU 399 B PRO 177 A ? PRO 400 B 1 -3.40 
2 GLU 176 D . ? GLU 399 A PRO 177 D ? PRO 400 A 1 -3.62 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8  ? 
AA2 ? 14 ? 
AA3 ? 4  ? 
AA4 ? 7  ? 
AA5 ? 4  ? 
AA6 ? 5  ? 
AA7 ? 8  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 1  7  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 2  6  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 4  8  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 1  6  ? anti-parallel 
AA2 2  5  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 3  6  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 4  14 ? anti-parallel 
AA2 6  7  ? parallel      
AA2 7  11 ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 8  13 ? anti-parallel 
AA2 9  12 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 10 13 ? anti-parallel 
AA2 11 12 ? anti-parallel 
AA2 13 14 ? parallel      
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? anti-parallel 
AA4 1  7  ? parallel      
AA4 2  3  ? anti-parallel 
AA4 2  5  ? anti-parallel 
AA4 3  4  ? anti-parallel 
AA4 5  6  ? anti-parallel 
AA4 5  7  ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA5 2  3  ? anti-parallel 
AA5 3  4  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA6 4  5  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA7 1  7  ? anti-parallel 
AA7 2  3  ? anti-parallel 
AA7 2  6  ? anti-parallel 
AA7 4  5  ? anti-parallel 
AA7 4  8  ? anti-parallel 
AA7 5  6  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LYS A 25  ? GLY A 29  ? LYS B 248 GLY B 252 
AA1 2  GLU A 206 ? THR A 214 ? GLU B 429 THR B 437 
AA1 3  ASP A 225 ? CYS A 228 ? ASP B 448 CYS B 451 
AA1 4  VAL A 249 ? VAL A 255 ? VAL B 472 VAL B 478 
AA1 5  VAL A 262 ? HIS A 269 ? VAL B 485 HIS B 492 
AA1 6  TYR A 273 ? ALA A 277 ? TYR B 496 ALA B 500 
AA1 7  HIS A 282 ? LEU A 284 ? HIS B 505 LEU B 507 
AA1 8  TYR A 291 ? VAL A 298 ? TYR B 514 VAL B 521 
AA2 1  PHE A 63  ? THR A 68  ? PHE B 286 THR B 291 
AA2 2  ASN A 75  ? LEU A 80  ? ASN B 298 LEU B 303 
AA2 3  LYS A 106 ? THR A 114 ? LYS B 329 THR B 337 
AA2 4  THR A 121 ? TYR A 129 ? THR B 344 TYR B 352 
AA2 5  ARG A 141 ? THR A 146 ? ARG B 364 THR B 369 
AA2 6  THR A 158 ? ILE A 166 ? THR B 381 ILE B 389 
AA2 7  GLY A 217 ? GLY A 220 ? GLY B 440 GLY B 443 
AA2 8  PHE D 63  ? HIS D 69  ? PHE A 286 HIS A 292 
AA2 9  ASN D 75  ? LEU D 80  ? ASN A 298 LEU A 303 
AA2 10 LYS D 106 ? THR D 114 ? LYS A 329 THR A 337 
AA2 11 THR D 121 ? TYR D 129 ? THR A 344 TYR A 352 
AA2 12 ARG D 141 ? THR D 146 ? ARG A 364 THR A 369 
AA2 13 THR D 158 ? ILE D 166 ? THR A 381 ILE A 389 
AA2 14 GLY D 217 ? GLY D 220 ? GLY A 440 GLY A 443 
AA3 1  VAL B 2   ? SER B 7   ? VAL C 2   SER C 7   
AA3 2  LEU B 18  ? GLY B 26  ? LEU C 18  GLY C 26  
AA3 3  ALA B 77  ? MET B 82  ? ALA C 77  MET C 82  
AA3 4  PHE B 67  ? ARG B 71  ? PHE C 67  ARG C 71  
AA4 1  GLY B 10  ? VAL B 12  ? GLY C 10  VAL C 12  
AA4 2  LEU B 33  ? GLN B 39  ? LEU C 33  GLN C 39  
AA4 3  ARG B 45  ? THR B 52  ? ARG C 45  THR C 52  
AA4 4  THR B 57  ? HIS B 59  ? THR C 57  HIS C 59  
AA4 5  GLY B 91  ? VAL B 98  ? GLY C 91  VAL C 98  
AA4 6  SER B 104 ? TRP B 106 ? SER C 104 TRP C 106 
AA4 7  THR B 110 ? VAL B 114 ? THR C 110 VAL C 114 
AA5 1  GLN C 3   ? SER C 7   ? GLN D 3   SER D 7   
AA5 2  SER C 17  ? SER C 25  ? SER D 17  SER D 25  
AA5 3  ALA C 77  ? ASN C 83  ? ALA D 77  ASN D 83  
AA5 4  PHE C 67  ? ARG C 71  ? PHE D 67  ARG D 71  
AA6 1  THR C 57  ? HIS C 59  ? THR D 57  HIS D 59  
AA6 2  GLU C 46  ? THR C 52  ? GLU D 46  THR D 52  
AA6 3  LEU C 33  ? GLN C 39  ? LEU D 33  GLN D 39  
AA6 4  VAL C 92  ? VAL C 98  ? VAL D 92  VAL D 98  
AA6 5  SER C 104 ? TRP C 106 ? SER D 104 TRP D 106 
AA7 1  LYS D 25  ? GLY D 29  ? LYS A 248 GLY A 252 
AA7 2  GLU D 206 ? THR D 214 ? GLU A 429 THR A 437 
AA7 3  ASP D 225 ? CYS D 228 ? ASP A 448 CYS A 451 
AA7 4  VAL D 249 ? VAL D 255 ? VAL A 472 VAL A 478 
AA7 5  VAL D 262 ? HIS D 269 ? VAL A 485 HIS A 492 
AA7 6  TYR D 273 ? ALA D 277 ? TYR A 496 ALA A 500 
AA7 7  HIS D 282 ? LEU D 284 ? HIS A 505 LEU A 507 
AA7 8  TYR D 291 ? VAL D 298 ? TYR A 514 VAL A 521 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N PHE A 27  ? N PHE B 250 O PHE A 210 ? O PHE B 433 
AA1 1  7  N LEU A 26  ? N LEU B 249 O LEU A 284 ? O LEU B 507 
AA1 2  3  N SER A 213 ? N SER B 436 O LEU A 226 ? O LEU B 449 
AA1 2  6  N GLN A 207 ? N GLN B 430 O VAL A 276 ? O VAL B 499 
AA1 4  5  N PHE A 254 ? N PHE B 477 O LEU A 263 ? O LEU B 486 
AA1 4  8  N LEU A 251 ? N LEU B 474 O SER A 296 ? O SER B 519 
AA1 5  6  N HIS A 269 ? N HIS B 492 O TYR A 273 ? O TYR B 496 
AA2 1  2  N THR A 68  ? N THR B 291 O THR A 77  ? O THR B 300 
AA2 1  6  N GLY A 65  ? N GLY B 288 O THR A 158 ? O THR B 381 
AA2 2  5  N MET A 78  ? N MET B 301 O VAL A 142 ? O VAL B 365 
AA2 3  4  N LEU A 111 ? N LEU B 334 O HIS A 124 ? O HIS B 347 
AA2 3  6  N GLN A 108 ? N GLN B 331 O GLY A 164 ? O GLY B 387 
AA2 4  5  N THR A 127 ? N THR B 350 O GLU A 145 ? O GLU B 368 
AA2 4  14 N THR A 121 ? N THR B 344 O GLY D 220 ? O GLY A 443 
AA2 6  7  N VAL A 165 ? N VAL B 388 O CYS A 218 ? O CYS B 441 
AA2 7  11 N GLY A 220 ? N GLY B 443 O THR D 121 ? O THR A 344 
AA2 8  9  N THR D 68  ? N THR A 291 O THR D 77  ? O THR A 300 
AA2 8  13 N GLY D 65  ? N GLY A 288 O THR D 158 ? O THR A 381 
AA2 9  12 N MET D 78  ? N MET A 301 O VAL D 142 ? O VAL A 365 
AA2 10 11 N GLY D 109 ? N GLY A 332 O ALA D 126 ? O ALA A 349 
AA2 10 13 N THR D 112 ? N THR A 335 O LYS D 159 ? O LYS A 382 
AA2 11 12 N THR D 127 ? N THR A 350 O GLU D 145 ? O GLU A 368 
AA2 13 14 N VAL D 165 ? N VAL A 388 O CYS D 218 ? O CYS A 441 
AA3 1  2  N GLN B 5   ? N GLN C 5   O ALA B 23  ? O ALA C 23  
AA3 2  3  N LEU B 18  ? N LEU C 18  O MET B 82  ? O MET C 82  
AA3 3  4  O TYR B 79  ? O TYR C 79  N SER B 70  ? N SER C 70  
AA4 1  7  N GLY B 10  ? N GLY C 10  O GLN B 111 ? O GLN C 111 
AA4 2  3  N MET B 34  ? N MET C 34  O ILE B 51  ? O ILE C 51  
AA4 2  5  N TYR B 37  ? N TYR C 37  O TYR B 94  ? O TYR C 94  
AA4 3  4  N THR B 50  ? N THR C 50  O LYS B 58  ? O LYS C 58  
AA4 5  6  N ALA B 97  ? N ALA C 97  O SER B 105 ? O SER C 105 
AA4 5  7  N TYR B 93  ? N TYR C 93  O THR B 110 ? O THR C 110 
AA5 1  2  N GLN C 5   ? N GLN D 5   O ALA C 23  ? O ALA D 23  
AA5 2  3  N LEU C 18  ? N LEU D 18  O MET C 82  ? O MET D 82  
AA5 3  4  O TYR C 79  ? O TYR D 79  N SER C 70  ? N SER D 70  
AA6 1  2  O LYS C 58  ? O LYS D 58  N THR C 50  ? N THR D 50  
AA6 2  3  O ILE C 51  ? O ILE D 51  N MET C 34  ? N MET D 34  
AA6 3  4  N TYR C 37  ? N TYR D 37  O TYR C 94  ? O TYR D 94  
AA6 4  5  N ALA C 97  ? N ALA D 97  O SER C 105 ? O SER D 105 
AA7 1  2  N PHE D 27  ? N PHE A 250 O PHE D 210 ? O PHE A 433 
AA7 1  7  N THR D 28  ? N THR A 251 O HIS D 282 ? O HIS A 505 
AA7 2  3  N PHE D 211 ? N PHE A 434 O CYS D 228 ? O CYS A 451 
AA7 2  6  N GLN D 207 ? N GLN A 430 O VAL D 276 ? O VAL A 499 
AA7 4  5  N ALA D 250 ? N ALA A 473 O LEU D 268 ? O LEU A 491 
AA7 4  8  N LEU D 251 ? N LEU A 474 O ASP D 295 ? O ASP A 518 
AA7 5  6  N HIS D 269 ? N HIS A 492 O TYR D 273 ? O TYR A 496 
# 
_atom_sites.entry_id                    8EN4 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.009224 
_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]   0.007284 
_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]   0.007134 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   . THR A 1 1   ? 14.129 40.264  43.565  1.00 67.35  ?  224 THR B N   1 
ATOM   2    C CA  . THR A 1 1   ? 13.751 39.562  42.344  1.00 73.19  ?  224 THR B CA  1 
ATOM   3    C C   . THR A 1 1   ? 14.925 39.489  41.371  1.00 69.35  ?  224 THR B C   1 
ATOM   4    O O   . THR A 1 1   ? 15.541 40.507  41.048  1.00 68.52  ?  224 THR B O   1 
ATOM   5    C CB  . THR A 1 1   ? 12.557 40.243  41.649  1.00 71.86  ?  224 THR B CB  1 
ATOM   6    O OG1 . THR A 1 1   ? 11.640 40.727  42.638  1.00 79.47  ?  224 THR B OG1 1 
ATOM   7    C CG2 . THR A 1 1   ? 11.838 39.257  40.738  1.00 68.40  ?  224 THR B CG2 1 
ATOM   8    N N   . LYS A 1 2   ? 15.226 38.280  40.909  1.00 67.70  ?  225 LYS B N   1 
ATOM   9    C CA  . LYS A 1 2   ? 16.359 38.076  40.016  1.00 62.10  ?  225 LYS B CA  1 
ATOM   10   C C   . LYS A 1 2   ? 16.125 38.804  38.695  1.00 60.74  ?  225 LYS B C   1 
ATOM   11   O O   . LYS A 1 2   ? 15.080 38.602  38.059  1.00 60.94  ?  225 LYS B O   1 
ATOM   12   C CB  . LYS A 1 2   ? 16.577 36.585  39.767  1.00 59.88  ?  225 LYS B CB  1 
ATOM   13   C CG  . LYS A 1 2   ? 17.945 36.241  39.203  1.00 63.75  ?  225 LYS B CG  1 
ATOM   14   C CD  . LYS A 1 2   ? 18.007 34.791  38.754  1.00 55.71  ?  225 LYS B CD  1 
ATOM   15   C CE  . LYS A 1 2   ? 18.648 33.913  39.818  1.00 58.26  ?  225 LYS B CE  1 
ATOM   16   N NZ  . LYS A 1 2   ? 18.007 32.569  39.907  1.00 60.51  ?  225 LYS B NZ  1 
ATOM   17   N N   . PRO A 1 3   ? 17.053 39.652  38.254  1.00 56.90  ?  226 PRO B N   1 
ATOM   18   C CA  . PRO A 1 3   ? 16.860 40.349  36.978  1.00 59.31  ?  226 PRO B CA  1 
ATOM   19   C C   . PRO A 1 3   ? 16.937 39.384  35.805  1.00 55.07  ?  226 PRO B C   1 
ATOM   20   O O   . PRO A 1 3   ? 17.770 38.476  35.775  1.00 52.43  ?  226 PRO B O   1 
ATOM   21   C CB  . PRO A 1 3   ? 18.010 41.365  36.943  1.00 53.35  ?  226 PRO B CB  1 
ATOM   22   C CG  . PRO A 1 3   ? 18.570 41.398  38.332  1.00 44.62  ?  226 PRO B CG  1 
ATOM   23   C CD  . PRO A 1 3   ? 18.297 40.056  38.927  1.00 53.41  ?  226 PRO B CD  1 
ATOM   24   N N   . PHE A 1 4   ? 16.052 39.591  34.836  1.00 55.89  ?  227 PHE B N   1 
ATOM   25   C CA  . PHE A 1 4   ? 16.022 38.758  33.644  1.00 52.96  ?  227 PHE B CA  1 
ATOM   26   C C   . PHE A 1 4   ? 17.075 39.220  32.644  1.00 50.92  ?  227 PHE B C   1 
ATOM   27   O O   . PHE A 1 4   ? 17.431 40.401  32.581  1.00 49.74  ?  227 PHE B O   1 
ATOM   28   C CB  . PHE A 1 4   ? 14.635 38.795  33.002  1.00 49.65  ?  227 PHE B CB  1 
ATOM   29   C CG  . PHE A 1 4   ? 14.504 37.919  31.789  1.00 47.09  ?  227 PHE B CG  1 
ATOM   30   C CD1 . PHE A 1 4   ? 14.368 36.547  31.919  1.00 49.19  ?  227 PHE B CD1 1 
ATOM   31   C CD2 . PHE A 1 4   ? 14.515 38.469  30.517  1.00 51.44  ?  227 PHE B CD2 1 
ATOM   32   C CE1 . PHE A 1 4   ? 14.247 35.740  30.805  1.00 46.07  ?  227 PHE B CE1 1 
ATOM   33   C CE2 . PHE A 1 4   ? 14.393 37.667  29.399  1.00 46.70  ?  227 PHE B CE2 1 
ATOM   34   C CZ  . PHE A 1 4   ? 14.258 36.301  29.544  1.00 43.97  ?  227 PHE B CZ  1 
ATOM   35   N N   . SER A 1 5   ? 17.576 38.270  31.858  1.00 49.76  ?  228 SER B N   1 
ATOM   36   C CA  . SER A 1 5   ? 18.569 38.565  30.836  1.00 49.69  ?  228 SER B CA  1 
ATOM   37   C C   . SER A 1 5   ? 18.615 37.406  29.850  1.00 49.57  ?  228 SER B C   1 
ATOM   38   O O   . SER A 1 5   ? 18.149 36.301  30.139  1.00 48.95  ?  228 SER B O   1 
ATOM   39   C CB  . SER A 1 5   ? 19.953 38.811  31.448  1.00 46.47  ?  228 SER B CB  1 
ATOM   40   O OG  . SER A 1 5   ? 20.480 37.621  32.010  1.00 50.03  ?  228 SER B OG  1 
ATOM   41   N N   . VAL A 1 6   ? 19.182 37.679  28.680  1.00 44.41  ?  229 VAL B N   1 
ATOM   42   C CA  . VAL A 1 6   ? 19.372 36.664  27.647  1.00 45.20  ?  229 VAL B CA  1 
ATOM   43   C C   . VAL A 1 6   ? 20.869 36.501  27.407  1.00 43.18  ?  229 VAL B C   1 
ATOM   44   O O   . VAL A 1 6   ? 21.634 37.449  27.634  1.00 41.92  ?  229 VAL B O   1 
ATOM   45   C CB  . VAL A 1 6   ? 18.632 37.032  26.350  1.00 40.95  ?  229 VAL B CB  1 
ATOM   46   C CG1 . VAL A 1 6   ? 17.125 36.991  26.564  1.00 41.07  ?  229 VAL B CG1 1 
ATOM   47   C CG2 . VAL A 1 6   ? 19.074 38.399  25.854  1.00 35.16  ?  229 VAL B CG2 1 
ATOM   48   N N   . PRO A 1 7   ? 21.331 35.333  26.958  1.00 47.00  ?  230 PRO B N   1 
ATOM   49   C CA  . PRO A 1 7   ? 22.766 35.154  26.713  1.00 40.95  ?  230 PRO B CA  1 
ATOM   50   C C   . PRO A 1 7   ? 23.281 36.129  25.663  1.00 42.18  ?  230 PRO B C   1 
ATOM   51   O O   . PRO A 1 7   ? 22.535 36.617  24.813  1.00 34.60  ?  230 PRO B O   1 
ATOM   52   C CB  . PRO A 1 7   ? 22.865 33.705  26.222  1.00 40.05  ?  230 PRO B CB  1 
ATOM   53   C CG  . PRO A 1 7   ? 21.642 33.039  26.749  1.00 40.41  ?  230 PRO B CG  1 
ATOM   54   C CD  . PRO A 1 7   ? 20.574 34.090  26.732  1.00 39.49  ?  230 PRO B CD  1 
ATOM   55   N N   . VAL A 1 8   ? 24.581 36.413  25.740  1.00 43.97  ?  231 VAL B N   1 
ATOM   56   C CA  . VAL A 1 8   ? 25.242 37.289  24.781  1.00 42.77  ?  231 VAL B CA  1 
ATOM   57   C C   . VAL A 1 8   ? 25.932 36.500  23.673  1.00 45.80  ?  231 VAL B C   1 
ATOM   58   O O   . VAL A 1 8   ? 26.736 37.064  22.924  1.00 47.68  ?  231 VAL B O   1 
ATOM   59   C CB  . VAL A 1 8   ? 26.236 38.230  25.480  1.00 43.83  ?  231 VAL B CB  1 
ATOM   60   C CG1 . VAL A 1 8   ? 25.522 39.061  26.537  1.00 41.09  ?  231 VAL B CG1 1 
ATOM   61   C CG2 . VAL A 1 8   ? 27.376 37.435  26.100  1.00 44.87  ?  231 VAL B CG2 1 
ATOM   62   N N   . LEU A 1 9   ? 25.638 35.209  23.553  1.00 42.13  ?  232 LEU B N   1 
ATOM   63   C CA  . LEU A 1 9   ? 26.239 34.399  22.503  1.00 44.34  ?  232 LEU B CA  1 
ATOM   64   C C   . LEU A 1 9   ? 25.664 34.776  21.144  1.00 44.59  ?  232 LEU B C   1 
ATOM   65   O O   . LEU A 1 9   ? 24.451 34.938  20.988  1.00 44.40  ?  232 LEU B O   1 
ATOM   66   C CB  . LEU A 1 9   ? 26.005 32.914  22.778  1.00 43.11  ?  232 LEU B CB  1 
ATOM   67   C CG  . LEU A 1 9   ? 26.633 32.329  24.046  1.00 45.56  ?  232 LEU B CG  1 
ATOM   68   C CD1 . LEU A 1 9   ? 26.001 30.988  24.387  1.00 39.87  ?  232 LEU B CD1 1 
ATOM   69   C CD2 . LEU A 1 9   ? 28.139 32.190  23.888  1.00 43.05  ?  232 LEU B CD2 1 
ATOM   70   N N   . THR A 1 10  ? 26.544 34.912  20.155  1.00 44.37  ?  233 THR B N   1 
ATOM   71   C CA  . THR A 1 10  ? 26.104 35.218  18.803  1.00 44.69  ?  233 THR B CA  1 
ATOM   72   C C   . THR A 1 10  ? 25.304 34.049  18.227  1.00 40.95  ?  233 THR B C   1 
ATOM   73   O O   . THR A 1 10  ? 25.289 32.938  18.766  1.00 42.10  ?  233 THR B O   1 
ATOM   74   C CB  . THR A 1 10  ? 27.299 35.536  17.905  1.00 43.94  ?  233 THR B CB  1 
ATOM   75   O OG1 . THR A 1 10  ? 27.958 34.319  17.535  1.00 44.17  ?  233 THR B OG1 1 
ATOM   76   C CG2 . THR A 1 10  ? 28.285 36.440  18.632  1.00 43.60  ?  233 THR B CG2 1 
ATOM   77   N N   . VAL A 1 11  ? 24.624 34.318  17.109  1.00 40.71  ?  234 VAL B N   1 
ATOM   78   C CA  . VAL A 1 11  ? 23.790 33.298  16.479  1.00 42.08  ?  234 VAL B CA  1 
ATOM   79   C C   . VAL A 1 11  ? 24.642 32.125  16.011  1.00 40.02  ?  234 VAL B C   1 
ATOM   80   O O   . VAL A 1 11  ? 24.257 30.958  16.163  1.00 39.34  ?  234 VAL B O   1 
ATOM   81   C CB  . VAL A 1 11  ? 22.982 33.915  15.322  1.00 44.70  ?  234 VAL B CB  1 
ATOM   82   C CG1 . VAL A 1 11  ? 22.419 32.829  14.413  1.00 41.54  ?  234 VAL B CG1 1 
ATOM   83   C CG2 . VAL A 1 11  ? 21.864 34.793  15.865  1.00 43.39  ?  234 VAL B CG2 1 
ATOM   84   N N   . GLU A 1 12  ? 25.819 32.412  15.447  1.00 47.64  ?  235 GLU B N   1 
ATOM   85   C CA  . GLU A 1 12  ? 26.685 31.346  14.954  1.00 46.96  ?  235 GLU B CA  1 
ATOM   86   C C   . GLU A 1 12  ? 27.220 30.479  16.088  1.00 43.40  ?  235 GLU B C   1 
ATOM   87   O O   . GLU A 1 12  ? 27.536 29.304  15.870  1.00 51.01  ?  235 GLU B O   1 
ATOM   88   C CB  . GLU A 1 12  ? 27.845 31.940  14.153  1.00 50.89  ?  235 GLU B CB  1 
ATOM   89   C CG  . GLU A 1 12  ? 27.666 31.864  12.645  1.00 55.07  ?  235 GLU B CG  1 
ATOM   90   C CD  . GLU A 1 12  ? 28.447 32.939  11.910  1.00 63.64  ?  235 GLU B CD  1 
ATOM   91   O OE1 . GLU A 1 12  ? 29.363 33.535  12.519  1.00 58.78  ?  235 GLU B OE1 1 
ATOM   92   O OE2 . GLU A 1 12  ? 28.146 33.188  10.722  1.00 60.70  ?  235 GLU B OE2 1 
ATOM   93   N N   . GLU A 1 13  ? 27.326 31.032  17.296  1.00 45.79  ?  236 GLU B N   1 
ATOM   94   C CA  . GLU A 1 13  ? 27.858 30.298  18.437  1.00 43.62  ?  236 GLU B CA  1 
ATOM   95   C C   . GLU A 1 13  ? 26.811 29.453  19.151  1.00 41.78  ?  236 GLU B C   1 
ATOM   96   O O   . GLU A 1 13  ? 27.146 28.795  20.141  1.00 47.91  ?  236 GLU B O   1 
ATOM   97   C CB  . GLU A 1 13  ? 28.487 31.266  19.444  1.00 42.11  ?  236 GLU B CB  1 
ATOM   98   C CG  . GLU A 1 13  ? 29.726 31.987  18.947  1.00 49.39  ?  236 GLU B CG  1 
ATOM   99   C CD  . GLU A 1 13  ? 30.015 33.253  19.735  1.00 49.32  ?  236 GLU B CD  1 
ATOM   100  O OE1 . GLU A 1 13  ? 29.227 33.577  20.650  1.00 47.40  ?  236 GLU B OE1 1 
ATOM   101  O OE2 . GLU A 1 13  ? 31.028 33.922  19.442  1.00 47.44  ?  236 GLU B OE2 1 
ATOM   102  N N   . MET A 1 14  ? 25.566 29.449  18.689  1.00 36.87  ?  237 MET B N   1 
ATOM   103  C CA  . MET A 1 14  ? 24.488 28.778  19.397  1.00 38.78  ?  237 MET B CA  1 
ATOM   104  C C   . MET A 1 14  ? 23.966 27.598  18.587  1.00 37.90  ?  237 MET B C   1 
ATOM   105  O O   . MET A 1 14  ? 24.168 27.507  17.373  1.00 43.05  ?  237 MET B O   1 
ATOM   106  C CB  . MET A 1 14  ? 23.355 29.761  19.715  1.00 38.06  ?  237 MET B CB  1 
ATOM   107  C CG  . MET A 1 14  ? 23.609 30.568  20.984  1.00 43.48  ?  237 MET B CG  1 
ATOM   108  S SD  . MET A 1 14  ? 22.210 31.555  21.545  1.00 41.90  ?  237 MET B SD  1 
ATOM   109  C CE  . MET A 1 14  ? 22.009 32.695  20.178  1.00 35.51  ?  237 MET B CE  1 
ATOM   110  N N   . THR A 1 15  ? 23.286 26.691  19.285  1.00 36.30  ?  238 THR B N   1 
ATOM   111  C CA  . THR A 1 15  ? 22.855 25.414  18.737  1.00 39.59  ?  238 THR B CA  1 
ATOM   112  C C   . THR A 1 15  ? 21.356 25.430  18.466  1.00 37.85  ?  238 THR B C   1 
ATOM   113  O O   . THR A 1 15  ? 20.583 26.014  19.232  1.00 36.81  ?  238 THR B O   1 
ATOM   114  C CB  . THR A 1 15  ? 23.190 24.271  19.706  1.00 40.26  ?  238 THR B CB  1 
ATOM   115  O OG1 . THR A 1 15  ? 24.571 24.347  20.080  1.00 43.18  ?  238 THR B OG1 1 
ATOM   116  C CG2 . THR A 1 15  ? 22.921 22.917  19.066  1.00 38.26  ?  238 THR B CG2 1 
ATOM   117  N N   . ASN A 1 16  ? 20.951 24.790  17.371  1.00 36.41  ?  239 ASN B N   1 
ATOM   118  C CA  . ASN A 1 16  ? 19.534 24.559  17.130  1.00 37.26  ?  239 ASN B CA  1 
ATOM   119  C C   . ASN A 1 16  ? 18.972 23.629  18.197  1.00 33.08  ?  239 ASN B C   1 
ATOM   120  O O   . ASN A 1 16  ? 19.600 22.636  18.574  1.00 34.97  ?  239 ASN B O   1 
ATOM   121  C CB  . ASN A 1 16  ? 19.322 23.960  15.738  1.00 34.44  ?  239 ASN B CB  1 
ATOM   122  C CG  . ASN A 1 16  ? 17.892 24.106  15.252  1.00 35.01  ?  239 ASN B CG  1 
ATOM   123  O OD1 . ASN A 1 16  ? 16.961 23.583  15.863  1.00 33.65  ?  239 ASN B OD1 1 
ATOM   124  N ND2 . ASN A 1 16  ? 17.714 24.818  14.144  1.00 36.09  ?  239 ASN B ND2 1 
ATOM   125  N N   . SER A 1 17  ? 17.782 23.957  18.690  1.00 36.34  ?  240 SER B N   1 
ATOM   126  C CA  . SER A 1 17  ? 17.174 23.219  19.789  1.00 39.16  ?  240 SER B CA  1 
ATOM   127  C C   . SER A 1 17  ? 16.307 22.058  19.321  1.00 42.83  ?  240 SER B C   1 
ATOM   128  O O   . SER A 1 17  ? 15.665 21.411  20.156  1.00 37.21  ?  240 SER B O   1 
ATOM   129  C CB  . SER A 1 17  ? 16.341 24.167  20.655  1.00 36.94  ?  240 SER B CB  1 
ATOM   130  O OG  . SER A 1 17  ? 15.378 24.853  19.876  1.00 42.66  ?  240 SER B OG  1 
ATOM   131  N N   . ARG A 1 18  ? 16.275 21.777  18.018  1.00 35.23  ?  241 ARG B N   1 
ATOM   132  C CA  . ARG A 1 18  ? 15.500 20.670  17.475  1.00 37.15  ?  241 ARG B CA  1 
ATOM   133  C C   . ARG A 1 18  ? 16.349 19.666  16.709  1.00 36.53  ?  241 ARG B C   1 
ATOM   134  O O   . ARG A 1 18  ? 15.810 18.663  16.226  1.00 36.39  ?  241 ARG B O   1 
ATOM   135  C CB  . ARG A 1 18  ? 14.380 21.200  16.568  1.00 37.38  ?  241 ARG B CB  1 
ATOM   136  C CG  . ARG A 1 18  ? 13.500 22.248  17.231  1.00 39.09  ?  241 ARG B CG  1 
ATOM   137  C CD  . ARG A 1 18  ? 12.442 22.777  16.279  1.00 34.17  ?  241 ARG B CD  1 
ATOM   138  N NE  . ARG A 1 18  ? 11.679 21.701  15.660  1.00 36.31  ?  241 ARG B NE  1 
ATOM   139  C CZ  . ARG A 1 18  ? 10.963 21.834  14.552  1.00 39.46  ?  241 ARG B CZ  1 
ATOM   140  N NH1 . ARG A 1 18  ? 10.887 22.988  13.912  1.00 38.99  ?  241 ARG B NH1 1 
ATOM   141  N NH2 . ARG A 1 18  ? 10.305 20.780  14.075  1.00 43.00  ?  241 ARG B NH2 1 
ATOM   142  N N   . PHE A 1 19  ? 17.659 19.902  16.584  1.00 35.87  ?  242 PHE B N   1 
ATOM   143  C CA  . PHE A 1 19  ? 18.582 18.992  15.919  1.00 33.78  ?  242 PHE B CA  1 
ATOM   144  C C   . PHE A 1 19  ? 19.985 19.364  16.355  1.00 31.82  ?  242 PHE B C   1 
ATOM   145  O O   . PHE A 1 19  ? 20.285 20.561  16.458  1.00 33.66  ?  242 PHE B O   1 
ATOM   146  C CB  . PHE A 1 19  ? 18.461 19.075  14.393  1.00 34.19  ?  242 PHE B CB  1 
ATOM   147  C CG  . PHE A 1 19  ? 18.834 17.806  13.675  1.00 35.46  ?  242 PHE B CG  1 
ATOM   148  C CD1 . PHE A 1 19  ? 17.975 16.718  13.668  1.00 36.16  ?  242 PHE B CD1 1 
ATOM   149  C CD2 . PHE A 1 19  ? 20.037 17.706  12.995  1.00 33.76  ?  242 PHE B CD2 1 
ATOM   150  C CE1 . PHE A 1 19  ? 18.314 15.552  13.004  1.00 38.00  ?  242 PHE B CE1 1 
ATOM   151  C CE2 . PHE A 1 19  ? 20.382 16.541  12.329  1.00 34.66  ?  242 PHE B CE2 1 
ATOM   152  C CZ  . PHE A 1 19  ? 19.518 15.465  12.332  1.00 33.45  ?  242 PHE B CZ  1 
ATOM   153  N N   . PRO A 1 20  ? 20.864 18.394  16.618  1.00 33.34  ?  243 PRO B N   1 
ATOM   154  C CA  . PRO A 1 20  ? 22.218 18.731  17.082  1.00 33.83  ?  243 PRO B CA  1 
ATOM   155  C C   . PRO A 1 20  ? 23.086 19.346  15.994  1.00 33.22  ?  243 PRO B C   1 
ATOM   156  O O   . PRO A 1 20  ? 24.116 18.777  15.613  1.00 35.62  ?  243 PRO B O   1 
ATOM   157  C CB  . PRO A 1 20  ? 22.775 17.379  17.550  1.00 36.73  ?  243 PRO B CB  1 
ATOM   158  C CG  . PRO A 1 20  ? 22.010 16.367  16.768  1.00 34.99  ?  243 PRO B CG  1 
ATOM   159  C CD  . PRO A 1 20  ? 20.635 16.939  16.567  1.00 35.42  ?  243 PRO B CD  1 
ATOM   160  N N   . ILE A 1 21  ? 22.679 20.507  15.488  1.00 32.51  ?  244 ILE B N   1 
ATOM   161  C CA  . ILE A 1 21  ? 23.465 21.247  14.498  1.00 36.71  ?  244 ILE B CA  1 
ATOM   162  C C   . ILE A 1 21  ? 23.484 22.714  14.876  1.00 37.21  ?  244 ILE B C   1 
ATOM   163  O O   . ILE A 1 21  ? 22.561 23.227  15.523  1.00 34.33  ?  244 ILE B O   1 
ATOM   164  C CB  . ILE A 1 21  ? 22.896 21.086  13.070  1.00 33.01  ?  244 ILE B CB  1 
ATOM   165  C CG1 . ILE A 1 21  ? 21.431 21.528  13.018  1.00 30.29  ?  244 ILE B CG1 1 
ATOM   166  C CG2 . ILE A 1 21  ? 23.060 19.651  12.583  1.00 32.57  ?  244 ILE B CG2 1 
ATOM   167  C CD1 . ILE A 1 21  ? 20.767 21.269  11.683  1.00 36.47  ?  244 ILE B CD1 1 
ATOM   168  N N   . PRO A 1 22  ? 24.542 23.423  14.489  1.00 37.38  ?  245 PRO B N   1 
ATOM   169  C CA  . PRO A 1 22  ? 24.654 24.836  14.868  1.00 35.82  ?  245 PRO B CA  1 
ATOM   170  C C   . PRO A 1 22  ? 23.631 25.699  14.144  1.00 38.25  ?  245 PRO B C   1 
ATOM   171  O O   . PRO A 1 22  ? 23.110 25.347  13.083  1.00 36.76  ?  245 PRO B O   1 
ATOM   172  C CB  . PRO A 1 22  ? 26.082 25.205  14.453  1.00 37.48  ?  245 PRO B CB  1 
ATOM   173  C CG  . PRO A 1 22  ? 26.414 24.243  13.365  1.00 41.75  ?  245 PRO B CG  1 
ATOM   174  C CD  . PRO A 1 22  ? 25.719 22.963  13.729  1.00 30.89  ?  245 PRO B CD  1 
ATOM   175  N N   . LEU A 1 23  ? 23.340 26.847  14.749  1.00 36.67  ?  246 LEU B N   1 
ATOM   176  C CA  . LEU A 1 23  ? 22.482 27.831  14.108  1.00 37.27  ?  246 LEU B CA  1 
ATOM   177  C C   . LEU A 1 23  ? 23.241 28.543  12.994  1.00 38.73  ?  246 LEU B C   1 
ATOM   178  O O   . LEU A 1 23  ? 24.452 28.765  13.080  1.00 38.63  ?  246 LEU B O   1 
ATOM   179  C CB  . LEU A 1 23  ? 21.973 28.850  15.128  1.00 35.56  ?  246 LEU B CB  1 
ATOM   180  C CG  . LEU A 1 23  ? 20.918 28.372  16.128  1.00 38.42  ?  246 LEU B CG  1 
ATOM   181  C CD1 . LEU A 1 23  ? 20.460 29.525  17.011  1.00 34.42  ?  246 LEU B CD1 1 
ATOM   182  C CD2 . LEU A 1 23  ? 19.736 27.741  15.407  1.00 36.31  ?  246 LEU B CD2 1 
ATOM   183  N N   . GLU A 1 24  ? 22.517 28.905  11.941  1.00 35.77  ?  247 GLU B N   1 
ATOM   184  C CA  . GLU A 1 24  ? 23.118 29.566  10.788  1.00 37.14  ?  247 GLU B CA  1 
ATOM   185  C C   . GLU A 1 24  ? 22.638 30.992  10.583  1.00 35.31  ?  247 GLU B C   1 
ATOM   186  O O   . GLU A 1 24  ? 23.448 31.867  10.271  1.00 37.04  ?  247 GLU B O   1 
ATOM   187  C CB  . GLU A 1 24  ? 22.843 28.763  9.514   1.00 38.13  ?  247 GLU B CB  1 
ATOM   188  C CG  . GLU A 1 24  ? 23.702 27.521  9.367   1.00 40.46  ?  247 GLU B CG  1 
ATOM   189  C CD  . GLU A 1 24  ? 22.927 26.362  8.781   1.00 49.11  ?  247 GLU B CD  1 
ATOM   190  O OE1 . GLU A 1 24  ? 22.076 26.610  7.902   1.00 51.94  ?  247 GLU B OE1 1 
ATOM   191  O OE2 . GLU A 1 24  ? 23.169 25.207  9.193   1.00 52.82  ?  247 GLU B OE2 1 
ATOM   192  N N   . LYS A 1 25  ? 21.346 31.256  10.754  1.00 31.89  ?  248 LYS B N   1 
ATOM   193  C CA  . LYS A 1 25  ? 20.794 32.557  10.409  1.00 36.93  ?  248 LYS B CA  1 
ATOM   194  C C   . LYS A 1 25  ? 19.476 32.755  11.144  1.00 34.91  ?  248 LYS B C   1 
ATOM   195  O O   . LYS A 1 25  ? 18.882 31.810  11.666  1.00 34.85  ?  248 LYS B O   1 
ATOM   196  C CB  . LYS A 1 25  ? 20.587 32.683  8.896   1.00 41.76  ?  248 LYS B CB  1 
ATOM   197  C CG  . LYS A 1 25  ? 19.358 31.935  8.394   1.00 35.40  ?  248 LYS B CG  1 
ATOM   198  C CD  . LYS A 1 25  ? 19.246 31.984  6.880   1.00 47.64  ?  248 LYS B CD  1 
ATOM   199  C CE  . LYS A 1 25  ? 20.414 31.279  6.212   1.00 49.41  ?  248 LYS B CE  1 
ATOM   200  N NZ  . LYS A 1 25  ? 20.139 31.024  4.769   1.00 59.85  ?  248 LYS B NZ  1 
ATOM   201  N N   . LEU A 1 26  ? 19.026 34.006  11.166  1.00 39.54  ?  249 LEU B N   1 
ATOM   202  C CA  . LEU A 1 26  ? 17.697 34.362  11.641  1.00 39.64  ?  249 LEU B CA  1 
ATOM   203  C C   . LEU A 1 26  ? 16.770 34.509  10.443  1.00 39.73  ?  249 LEU B C   1 
ATOM   204  O O   . LEU A 1 26  ? 17.174 35.016  9.394   1.00 43.42  ?  249 LEU B O   1 
ATOM   205  C CB  . LEU A 1 26  ? 17.728 35.664  12.444  1.00 35.80  ?  249 LEU B CB  1 
ATOM   206  C CG  . LEU A 1 26  ? 18.672 35.708  13.647  1.00 41.62  ?  249 LEU B CG  1 
ATOM   207  C CD1 . LEU A 1 26  ? 18.672 37.092  14.278  1.00 42.95  ?  249 LEU B CD1 1 
ATOM   208  C CD2 . LEU A 1 26  ? 18.286 34.653  14.670  1.00 38.84  ?  249 LEU B CD2 1 
ATOM   209  N N   . PHE A 1 27  ? 15.527 34.062  10.604  1.00 41.71  ?  250 PHE B N   1 
ATOM   210  C CA  . PHE A 1 27  ? 14.569 34.047  9.509   1.00 42.91  ?  250 PHE B CA  1 
ATOM   211  C C   . PHE A 1 27  ? 13.196 34.447  10.027  1.00 41.22  ?  250 PHE B C   1 
ATOM   212  O O   . PHE A 1 27  ? 12.828 34.109  11.156  1.00 39.41  ?  250 PHE B O   1 
ATOM   213  C CB  . PHE A 1 27  ? 14.507 32.659  8.850   1.00 39.85  ?  250 PHE B CB  1 
ATOM   214  C CG  . PHE A 1 27  ? 13.470 32.542  7.771   1.00 43.10  ?  250 PHE B CG  1 
ATOM   215  C CD1 . PHE A 1 27  ? 13.711 33.045  6.502   1.00 43.39  ?  250 PHE B CD1 1 
ATOM   216  C CD2 . PHE A 1 27  ? 12.258 31.916  8.018   1.00 42.61  ?  250 PHE B CD2 1 
ATOM   217  C CE1 . PHE A 1 27  ? 12.761 32.933  5.503   1.00 43.58  ?  250 PHE B CE1 1 
ATOM   218  C CE2 . PHE A 1 27  ? 11.303 31.801  7.022   1.00 44.52  ?  250 PHE B CE2 1 
ATOM   219  C CZ  . PHE A 1 27  ? 11.555 32.311  5.764   1.00 41.75  ?  250 PHE B CZ  1 
ATOM   220  N N   . THR A 1 28  ? 12.447 35.170  9.196   1.00 41.17  ?  251 THR B N   1 
ATOM   221  C CA  . THR A 1 28  ? 11.077 35.541  9.517   1.00 42.02  ?  251 THR B CA  1 
ATOM   222  C C   . THR A 1 28  ? 10.197 35.308  8.298   1.00 42.94  ?  251 THR B C   1 
ATOM   223  O O   . THR A 1 28  ? 10.655 35.386  7.155   1.00 45.01  ?  251 THR B O   1 
ATOM   224  C CB  . THR A 1 28  ? 10.966 37.004  9.983   1.00 40.05  ?  251 THR B CB  1 
ATOM   225  O OG1 . THR A 1 28  ? 9.623  37.273  10.405  1.00 39.46  ?  251 THR B OG1 1 
ATOM   226  C CG2 . THR A 1 28  ? 11.347 37.965  8.862   1.00 42.29  ?  251 THR B CG2 1 
ATOM   227  N N   . GLY A 1 29  ? 8.928  35.007  8.555   1.00 43.19  ?  252 GLY B N   1 
ATOM   228  C CA  . GLY A 1 29  ? 7.973  34.754  7.502   1.00 42.64  ?  252 GLY B CA  1 
ATOM   229  C C   . GLY A 1 29  ? 6.599  34.438  8.054   1.00 46.99  ?  252 GLY B C   1 
ATOM   230  O O   . GLY A 1 29  ? 6.431  34.169  9.248   1.00 45.67  ?  252 GLY B O   1 
ATOM   231  N N   . PRO A 1 30  ? 5.583  34.470  7.191   1.00 47.72  ?  253 PRO B N   1 
ATOM   232  C CA  . PRO A 1 30  ? 4.224  34.158  7.645   1.00 47.05  ?  253 PRO B CA  1 
ATOM   233  C C   . PRO A 1 30  ? 4.113  32.713  8.107   1.00 49.65  ?  253 PRO B C   1 
ATOM   234  O O   . PRO A 1 30  ? 4.743  31.812  7.548   1.00 55.51  ?  253 PRO B O   1 
ATOM   235  C CB  . PRO A 1 30  ? 3.361  34.425  6.404   1.00 47.90  ?  253 PRO B CB  1 
ATOM   236  C CG  . PRO A 1 30  ? 4.311  34.360  5.250   1.00 46.05  ?  253 PRO B CG  1 
ATOM   237  C CD  . PRO A 1 30  ? 5.628  34.846  5.767   1.00 46.39  ?  253 PRO B CD  1 
ATOM   238  N N   . SER A 1 31  ? 3.297  32.497  9.145   1.00 46.36  ?  254 SER B N   1 
ATOM   239  C CA  . SER A 1 31  ? 3.124  31.175  9.736   1.00 49.09  ?  254 SER B CA  1 
ATOM   240  C C   . SER A 1 31  ? 1.659  30.754  9.795   1.00 55.09  ?  254 SER B C   1 
ATOM   241  O O   . SER A 1 31  ? 1.319  29.820  10.527  1.00 55.51  ?  254 SER B O   1 
ATOM   242  C CB  . SER A 1 31  ? 3.740  31.125  11.136  1.00 53.91  ?  254 SER B CB  1 
ATOM   243  O OG  . SER A 1 31  ? 2.818  31.569  12.115  1.00 57.08  ?  254 SER B OG  1 
ATOM   244  N N   . SER A 1 32  ? 0.784  31.422  9.041   1.00 57.46  ?  255 SER B N   1 
ATOM   245  C CA  . SER A 1 32  ? -0.631 31.066  9.031   1.00 54.90  ?  255 SER B CA  1 
ATOM   246  C C   . SER A 1 32  ? -0.923 29.811  8.220   1.00 61.12  ?  255 SER B C   1 
ATOM   247  O O   . SER A 1 32  ? -1.920 29.134  8.489   1.00 62.06  ?  255 SER B O   1 
ATOM   248  C CB  . SER A 1 32  ? -1.461 32.230  8.488   1.00 55.30  ?  255 SER B CB  1 
ATOM   249  O OG  . SER A 1 32  ? -0.819 32.852  7.387   1.00 58.67  ?  255 SER B OG  1 
ATOM   250  N N   . ALA A 1 33  ? -0.074 29.477  7.248   1.00 55.49  ?  256 ALA B N   1 
ATOM   251  C CA  . ALA A 1 33  ? -0.327 28.331  6.382   1.00 58.23  ?  256 ALA B CA  1 
ATOM   252  C C   . ALA A 1 33  ? -0.069 26.996  7.065   1.00 60.61  ?  256 ALA B C   1 
ATOM   253  O O   . ALA A 1 33  ? -0.349 25.953  6.464   1.00 62.33  ?  256 ALA B O   1 
ATOM   254  C CB  . ALA A 1 33  ? 0.526  28.428  5.115   1.00 54.80  ?  256 ALA B CB  1 
ATOM   255  N N   . PHE A 1 34  ? 0.449  26.996  8.291   1.00 59.51  ?  257 PHE B N   1 
ATOM   256  C CA  . PHE A 1 34  ? 0.776  25.757  8.977   1.00 51.54  ?  257 PHE B CA  1 
ATOM   257  C C   . PHE A 1 34  ? 0.697  25.983  10.479  1.00 56.22  ?  257 PHE B C   1 
ATOM   258  O O   . PHE A 1 34  ? 0.519  27.108  10.953  1.00 51.70  ?  257 PHE B O   1 
ATOM   259  C CB  . PHE A 1 34  ? 2.163  25.239  8.573   1.00 49.59  ?  257 PHE B CB  1 
ATOM   260  C CG  . PHE A 1 34  ? 3.237  26.293  8.577   1.00 55.58  ?  257 PHE B CG  1 
ATOM   261  C CD1 . PHE A 1 34  ? 3.420  27.131  7.487   1.00 54.80  ?  257 PHE B CD1 1 
ATOM   262  C CD2 . PHE A 1 34  ? 4.067  26.446  9.676   1.00 56.37  ?  257 PHE B CD2 1 
ATOM   263  C CE1 . PHE A 1 34  ? 4.408  28.100  7.495   1.00 48.87  ?  257 PHE B CE1 1 
ATOM   264  C CE2 . PHE A 1 34  ? 5.056  27.412  9.689   1.00 56.78  ?  257 PHE B CE2 1 
ATOM   265  C CZ  . PHE A 1 34  ? 5.227  28.240  8.597   1.00 52.28  ?  257 PHE B CZ  1 
ATOM   266  N N   . VAL A 1 35  ? 0.831  24.892  11.228  1.00 55.30  ?  258 VAL B N   1 
ATOM   267  C CA  . VAL A 1 35  ? 0.747  24.913  12.683  1.00 48.50  ?  258 VAL B CA  1 
ATOM   268  C C   . VAL A 1 35  ? 2.160  24.868  13.245  1.00 49.26  ?  258 VAL B C   1 
ATOM   269  O O   . VAL A 1 35  ? 2.902  23.906  13.009  1.00 45.41  ?  258 VAL B O   1 
ATOM   270  C CB  . VAL A 1 35  ? -0.095 23.741  13.212  1.00 51.65  ?  258 VAL B CB  1 
ATOM   271  C CG1 . VAL A 1 35  ? 0.072  23.606  14.718  1.00 49.45  ?  258 VAL B CG1 1 
ATOM   272  C CG2 . VAL A 1 35  ? -1.557 23.934  12.848  1.00 55.06  ?  258 VAL B CG2 1 
ATOM   273  N N   . VAL A 1 36  ? 2.535  25.907  13.989  1.00 49.10  ?  259 VAL B N   1 
ATOM   274  C CA  . VAL A 1 36  ? 3.855  25.982  14.615  1.00 46.75  ?  259 VAL B CA  1 
ATOM   275  C C   . VAL A 1 36  ? 3.691  25.441  16.032  1.00 46.69  ?  259 VAL B C   1 
ATOM   276  O O   . VAL A 1 36  ? 3.364  26.170  16.969  1.00 46.36  ?  259 VAL B O   1 
ATOM   277  C CB  . VAL A 1 36  ? 4.420  27.399  14.595  1.00 42.47  ?  259 VAL B CB  1 
ATOM   278  C CG1 . VAL A 1 36  ? 5.799  27.430  15.238  1.00 41.43  ?  259 VAL B CG1 1 
ATOM   279  C CG2 . VAL A 1 36  ? 4.478  27.924  13.170  1.00 46.56  ?  259 VAL B CG2 1 
ATOM   280  N N   . GLN A 1 37  ? 3.921  24.138  16.192  1.00 45.07  ?  260 GLN B N   1 
ATOM   281  C CA  . GLN A 1 37  ? 3.825  23.484  17.499  1.00 45.03  ?  260 GLN B CA  1 
ATOM   282  C C   . GLN A 1 37  ? 4.975  22.500  17.685  1.00 40.93  ?  260 GLN B C   1 
ATOM   283  O O   . GLN A 1 37  ? 4.763  21.296  17.852  1.00 41.97  ?  260 GLN B O   1 
ATOM   284  C CB  . GLN A 1 37  ? 2.474  22.786  17.650  1.00 46.05  ?  260 GLN B CB  1 
ATOM   285  C CG  . GLN A 1 37  ? 2.091  22.480  19.087  1.00 47.10  ?  260 GLN B CG  1 
ATOM   286  C CD  . GLN A 1 37  ? 0.742  21.798  19.199  1.00 47.69  ?  260 GLN B CD  1 
ATOM   287  O OE1 . GLN A 1 37  ? 0.219  21.267  18.219  1.00 53.57  ?  260 GLN B OE1 1 
ATOM   288  N NE2 . GLN A 1 37  ? 0.171  21.810  20.397  1.00 51.29  ?  260 GLN B NE2 1 
ATOM   289  N N   . PRO A 1 38  ? 6.217  22.983  17.678  1.00 40.74  ?  261 PRO B N   1 
ATOM   290  C CA  . PRO A 1 38  ? 7.338  22.086  17.964  1.00 38.43  ?  261 PRO B CA  1 
ATOM   291  C C   . PRO A 1 38  ? 7.379  21.740  19.443  1.00 42.45  ?  261 PRO B C   1 
ATOM   292  O O   . PRO A 1 38  ? 6.961  22.524  20.298  1.00 39.16  ?  261 PRO B O   1 
ATOM   293  C CB  . PRO A 1 38  ? 8.563  22.904  17.545  1.00 39.86  ?  261 PRO B CB  1 
ATOM   294  C CG  . PRO A 1 38  ? 8.151  24.311  17.776  1.00 38.45  ?  261 PRO B CG  1 
ATOM   295  C CD  . PRO A 1 38  ? 6.666  24.379  17.513  1.00 37.37  ?  261 PRO B CD  1 
ATOM   296  N N   . GLN A 1 39  ? 7.881  20.541  19.738  1.00 41.14  ?  262 GLN B N   1 
ATOM   297  C CA  . GLN A 1 39  ? 7.957  20.062  21.113  1.00 39.49  ?  262 GLN B CA  1 
ATOM   298  C C   . GLN A 1 39  ? 9.347  20.189  21.715  1.00 41.84  ?  262 GLN B C   1 
ATOM   299  O O   . GLN A 1 39  ? 9.482  20.114  22.941  1.00 41.12  ?  262 GLN B O   1 
ATOM   300  C CB  . GLN A 1 39  ? 7.500  18.601  21.192  1.00 42.54  ?  262 GLN B CB  1 
ATOM   301  C CG  . GLN A 1 39  ? 6.012  18.414  20.939  1.00 45.51  ?  262 GLN B CG  1 
ATOM   302  C CD  . GLN A 1 39  ? 5.157  19.368  21.752  1.00 43.02  ?  262 GLN B CD  1 
ATOM   303  O OE1 . GLN A 1 39  ? 4.989  19.194  22.959  1.00 45.15  ?  262 GLN B OE1 1 
ATOM   304  N NE2 . GLN A 1 39  ? 4.612  20.385  21.094  1.00 46.33  ?  262 GLN B NE2 1 
ATOM   305  N N   . ASN A 1 40  ? 10.373 20.373  20.892  1.00 41.54  ?  263 ASN B N   1 
ATOM   306  C CA  . ASN A 1 40  ? 11.722 20.639  21.362  1.00 39.96  ?  263 ASN B CA  1 
ATOM   307  C C   . ASN A 1 40  ? 12.018 22.128  21.244  1.00 37.71  ?  263 ASN B C   1 
ATOM   308  O O   . ASN A 1 40  ? 11.440 22.830  20.410  1.00 37.20  ?  263 ASN B O   1 
ATOM   309  C CB  . ASN A 1 40  ? 12.749 19.826  20.570  1.00 38.31  ?  263 ASN B CB  1 
ATOM   310  C CG  . ASN A 1 40  ? 12.780 18.366  20.987  1.00 39.84  ?  263 ASN B CG  1 
ATOM   311  O OD1 . ASN A 1 40  ? 12.779 18.051  22.177  1.00 38.05  ?  263 ASN B OD1 1 
ATOM   312  N ND2 . ASN A 1 40  ? 12.806 17.468  20.007  1.00 36.35  ?  263 ASN B ND2 1 
ATOM   313  N N   . GLY A 1 41  ? 12.921 22.608  22.094  1.00 38.74  ?  264 GLY B N   1 
ATOM   314  C CA  . GLY A 1 41  ? 13.179 24.033  22.154  1.00 35.67  ?  264 GLY B CA  1 
ATOM   315  C C   . GLY A 1 41  ? 12.045 24.836  22.746  1.00 40.37  ?  264 GLY B C   1 
ATOM   316  O O   . GLY A 1 41  ? 11.862 26.002  22.382  1.00 40.67  ?  264 GLY B O   1 
ATOM   317  N N   . ARG A 1 42  ? 11.272 24.238  23.649  1.00 36.26  ?  265 ARG B N   1 
ATOM   318  C CA  . ARG A 1 42  ? 10.148 24.897  24.300  1.00 38.12  ?  265 ARG B CA  1 
ATOM   319  C C   . ARG A 1 42  ? 10.507 25.148  25.758  1.00 38.48  ?  265 ARG B C   1 
ATOM   320  O O   . ARG A 1 42  ? 10.767 24.201  26.507  1.00 38.48  ?  265 ARG B O   1 
ATOM   321  C CB  . ARG A 1 42  ? 8.882  24.049  24.195  1.00 39.86  ?  265 ARG B CB  1 
ATOM   322  C CG  . ARG A 1 42  ? 8.401  23.829  22.772  1.00 39.20  ?  265 ARG B CG  1 
ATOM   323  C CD  . ARG A 1 42  ? 8.198  25.149  22.044  1.00 37.40  ?  265 ARG B CD  1 
ATOM   324  N NE  . ARG A 1 42  ? 7.058  25.885  22.578  1.00 45.22  ?  265 ARG B NE  1 
ATOM   325  C CZ  . ARG A 1 42  ? 5.800  25.686  22.209  1.00 45.37  ?  265 ARG B CZ  1 
ATOM   326  N NH1 . ARG A 1 42  ? 5.483  24.798  21.280  1.00 41.33  ?  265 ARG B NH1 1 
ATOM   327  N NH2 . ARG A 1 42  ? 4.835  26.397  22.787  1.00 42.94  ?  265 ARG B NH2 1 
ATOM   328  N N   . CYS A 1 43  ? 10.518 26.419  26.153  1.00 43.84  ?  266 CYS B N   1 
ATOM   329  C CA  . CYS A 1 43  ? 10.870 26.798  27.514  1.00 41.90  ?  266 CYS B CA  1 
ATOM   330  C C   . CYS A 1 43  ? 10.418 28.230  27.757  1.00 42.68  ?  266 CYS B C   1 
ATOM   331  O O   . CYS A 1 43  ? 10.631 29.104  26.914  1.00 41.22  ?  266 CYS B O   1 
ATOM   332  C CB  . CYS A 1 43  ? 12.380 26.668  27.756  1.00 41.34  ?  266 CYS B CB  1 
ATOM   333  S SG  . CYS A 1 43  ? 12.912 27.045  29.442  1.00 48.64  ?  266 CYS B SG  1 
ATOM   334  N N   . THR A 1 44  ? 9.795  28.464  28.909  1.00 43.58  ?  267 THR B N   1 
ATOM   335  C CA  . THR A 1 44  ? 9.358  29.804  29.261  1.00 44.36  ?  267 THR B CA  1 
ATOM   336  C C   . THR A 1 44  ? 10.545 30.645  29.726  1.00 41.11  ?  267 THR B C   1 
ATOM   337  O O   . THR A 1 44  ? 11.640 30.140  29.985  1.00 40.98  ?  267 THR B O   1 
ATOM   338  C CB  . THR A 1 44  ? 8.282  29.752  30.345  1.00 39.53  ?  267 THR B CB  1 
ATOM   339  O OG1 . THR A 1 44  ? 8.846  29.232  31.555  1.00 41.44  ?  267 THR B OG1 1 
ATOM   340  C CG2 . THR A 1 44  ? 7.127  28.863  29.907  1.00 38.95  ?  267 THR B CG2 1 
ATOM   341  N N   . THR A 1 45  ? 10.316 31.956  29.831  1.00 38.99  ?  268 THR B N   1 
ATOM   342  C CA  . THR A 1 45  ? 11.385 32.864  30.235  1.00 42.65  ?  268 THR B CA  1 
ATOM   343  C C   . THR A 1 45  ? 11.815 32.654  31.682  1.00 44.49  ?  268 THR B C   1 
ATOM   344  O O   . THR A 1 45  ? 12.939 33.024  32.038  1.00 45.20  ?  268 THR B O   1 
ATOM   345  C CB  . THR A 1 45  ? 10.953 34.316  30.027  1.00 42.63  ?  268 THR B CB  1 
ATOM   346  O OG1 . THR A 1 45  ? 9.743  34.570  30.751  1.00 42.03  ?  268 THR B OG1 1 
ATOM   347  C CG2 . THR A 1 45  ? 10.724 34.597  28.548  1.00 44.73  ?  268 THR B CG2 1 
ATOM   348  N N   . ASP A 1 46  ? 10.956 32.077  32.520  1.00 41.30  ?  269 ASP B N   1 
ATOM   349  C CA  . ASP A 1 46  ? 11.306 31.786  33.904  1.00 48.36  ?  269 ASP B CA  1 
ATOM   350  C C   . ASP A 1 46  ? 11.759 30.345  34.110  1.00 46.74  ?  269 ASP B C   1 
ATOM   351  O O   . ASP A 1 46  ? 11.871 29.900  35.257  1.00 47.70  ?  269 ASP B O   1 
ATOM   352  C CB  . ASP A 1 46  ? 10.131 32.116  34.832  1.00 51.51  ?  269 ASP B CB  1 
ATOM   353  C CG  . ASP A 1 46  ? 8.843  31.434  34.417  1.00 54.95  ?  269 ASP B CG  1 
ATOM   354  O OD1 . ASP A 1 46  ? 8.799  30.863  33.308  1.00 59.14  ?  269 ASP B OD1 1 
ATOM   355  O OD2 . ASP A 1 46  ? 7.872  31.471  35.201  1.00 64.50  ?  269 ASP B OD2 1 
ATOM   356  N N   . GLY A 1 47  ? 12.010 29.606  33.034  1.00 45.33  ?  270 GLY B N   1 
ATOM   357  C CA  . GLY A 1 47  ? 12.679 28.325  33.119  1.00 41.56  ?  270 GLY B CA  1 
ATOM   358  C C   . GLY A 1 47  ? 11.809 27.089  33.224  1.00 43.48  ?  270 GLY B C   1 
ATOM   359  O O   . GLY A 1 47  ? 12.288 26.069  33.732  1.00 45.26  ?  270 GLY B O   1 
ATOM   360  N N   . VAL A 1 48  ? 10.564 27.135  32.760  1.00 39.65  ?  271 VAL B N   1 
ATOM   361  C CA  . VAL A 1 48  ? 9.692  25.966  32.777  1.00 40.29  ?  271 VAL B CA  1 
ATOM   362  C C   . VAL A 1 48  ? 9.862  25.232  31.452  1.00 44.62  ?  271 VAL B C   1 
ATOM   363  O O   . VAL A 1 48  ? 9.517  25.758  30.390  1.00 44.52  ?  271 VAL B O   1 
ATOM   364  C CB  . VAL A 1 48  ? 8.228  26.354  33.016  1.00 40.49  ?  271 VAL B CB  1 
ATOM   365  C CG1 . VAL A 1 48  ? 7.344  25.113  33.027  1.00 43.02  ?  271 VAL B CG1 1 
ATOM   366  C CG2 . VAL A 1 48  ? 8.090  27.124  34.321  1.00 41.68  ?  271 VAL B CG2 1 
ATOM   367  N N   . LEU A 1 49  ? 10.395 24.014  31.511  1.00 37.66  ?  272 LEU B N   1 
ATOM   368  C CA  . LEU A 1 49  ? 10.557 23.212  30.308  1.00 40.94  ?  272 LEU B CA  1 
ATOM   369  C C   . LEU A 1 49  ? 9.211  22.664  29.853  1.00 46.96  ?  272 LEU B C   1 
ATOM   370  O O   . LEU A 1 49  ? 8.398  22.215  30.667  1.00 46.73  ?  272 LEU B O   1 
ATOM   371  C CB  . LEU A 1 49  ? 11.535 22.066  30.559  1.00 44.27  ?  272 LEU B CB  1 
ATOM   372  C CG  . LEU A 1 49  ? 12.950 22.462  30.981  1.00 44.82  ?  272 LEU B CG  1 
ATOM   373  C CD1 . LEU A 1 49  ? 13.739 21.236  31.399  1.00 46.02  ?  272 LEU B CD1 1 
ATOM   374  C CD2 . LEU A 1 49  ? 13.657 23.204  29.860  1.00 39.87  ?  272 LEU B CD2 1 
ATOM   375  N N   . LEU A 1 50  ? 8.973  22.699  28.544  1.00 44.28  ?  273 LEU B N   1 
ATOM   376  C CA  . LEU A 1 50  ? 7.702  22.290  27.969  1.00 41.91  ?  273 LEU B CA  1 
ATOM   377  C C   . LEU A 1 50  ? 7.911  21.186  26.941  1.00 46.93  ?  273 LEU B C   1 
ATOM   378  O O   . LEU A 1 50  ? 9.000  21.022  26.382  1.00 46.38  ?  273 LEU B O   1 
ATOM   379  C CB  . LEU A 1 50  ? 6.981  23.477  27.316  1.00 37.91  ?  273 LEU B CB  1 
ATOM   380  C CG  . LEU A 1 50  ? 6.777  24.724  28.181  1.00 46.03  ?  273 LEU B CG  1 
ATOM   381  C CD1 . LEU A 1 50  ? 6.277  25.890  27.340  1.00 37.22  ?  273 LEU B CD1 1 
ATOM   382  C CD2 . LEU A 1 50  ? 5.818  24.435  29.327  1.00 45.47  ?  273 LEU B CD2 1 
ATOM   383  N N   . GLY A 1 51  ? 6.846  20.426  26.703  1.00 45.60  ?  274 GLY B N   1 
ATOM   384  C CA  . GLY A 1 51  ? 6.869  19.427  25.644  1.00 42.21  ?  274 GLY B CA  1 
ATOM   385  C C   . GLY A 1 51  ? 7.872  18.327  25.922  1.00 46.27  ?  274 GLY B C   1 
ATOM   386  O O   . GLY A 1 51  ? 7.870  17.703  26.990  1.00 44.19  ?  274 GLY B O   1 
ATOM   387  N N   . THR A 1 52  ? 8.740  18.074  24.942  1.00 42.61  ?  275 THR B N   1 
ATOM   388  C CA  . THR A 1 52  ? 9.785  17.066  25.054  1.00 39.09  ?  275 THR B CA  1 
ATOM   389  C C   . THR A 1 52  ? 11.160 17.690  25.253  1.00 41.00  ?  275 THR B C   1 
ATOM   390  O O   . THR A 1 52  ? 12.179 17.038  24.998  1.00 37.92  ?  275 THR B O   1 
ATOM   391  C CB  . THR A 1 52  ? 9.790  16.166  23.815  1.00 42.04  ?  275 THR B CB  1 
ATOM   392  O OG1 . THR A 1 52  ? 10.192 16.930  22.670  1.00 36.96  ?  275 THR B OG1 1 
ATOM   393  C CG2 . THR A 1 52  ? 8.407  15.587  23.571  1.00 40.00  ?  275 THR B CG2 1 
ATOM   394  N N   . THR A 1 53  ? 11.209 18.936  25.719  1.00 33.95  ?  276 THR B N   1 
ATOM   395  C CA  . THR A 1 53  ? 12.457 19.684  25.769  1.00 35.88  ?  276 THR B CA  1 
ATOM   396  C C   . THR A 1 53  ? 13.298 19.263  26.967  1.00 38.67  ?  276 THR B C   1 
ATOM   397  O O   . THR A 1 53  ? 12.819 19.251  28.105  1.00 40.49  ?  276 THR B O   1 
ATOM   398  C CB  . THR A 1 53  ? 12.176 21.186  25.830  1.00 36.48  ?  276 THR B CB  1 
ATOM   399  O OG1 . THR A 1 53  ? 11.467 21.588  24.652  1.00 36.95  ?  276 THR B OG1 1 
ATOM   400  C CG2 . THR A 1 53  ? 13.476 21.969  25.925  1.00 31.13  ?  276 THR B CG2 1 
ATOM   401  N N   . GLN A 1 54  ? 14.554 18.910  26.701  1.00 37.76  ?  277 GLN B N   1 
ATOM   402  C CA  . GLN A 1 54  ? 15.538 18.710  27.754  1.00 34.42  ?  277 GLN B CA  1 
ATOM   403  C C   . GLN A 1 54  ? 16.680 19.699  27.554  1.00 39.23  ?  277 GLN B C   1 
ATOM   404  O O   . GLN A 1 54  ? 16.535 20.670  26.802  1.00 41.73  ?  277 GLN B O   1 
ATOM   405  C CB  . GLN A 1 54  ? 16.042 17.265  27.766  1.00 40.95  ?  277 GLN B CB  1 
ATOM   406  C CG  . GLN A 1 54  ? 16.253 16.669  26.388  1.00 33.97  ?  277 GLN B CG  1 
ATOM   407  C CD  . GLN A 1 54  ? 17.652 16.914  25.868  1.00 41.23  ?  277 GLN B CD  1 
ATOM   408  O OE1 . GLN A 1 54  ? 18.632 16.482  26.472  1.00 41.67  ?  277 GLN B OE1 1 
ATOM   409  N NE2 . GLN A 1 54  ? 17.754 17.615  24.744  1.00 44.06  ?  277 GLN B NE2 1 
ATOM   410  N N   . LEU A 1 55  ? 17.820 19.468  28.206  1.00 42.33  ?  278 LEU B N   1 
ATOM   411  C CA  . LEU A 1 55  ? 18.887 20.459  28.239  1.00 39.81  ?  278 LEU B CA  1 
ATOM   412  C C   . LEU A 1 55  ? 20.116 20.096  27.419  1.00 35.54  ?  278 LEU B C   1 
ATOM   413  O O   . LEU A 1 55  ? 20.909 20.991  27.106  1.00 39.42  ?  278 LEU B O   1 
ATOM   414  C CB  . LEU A 1 55  ? 19.328 20.719  29.688  1.00 39.53  ?  278 LEU B CB  1 
ATOM   415  C CG  . LEU A 1 55  ? 18.371 21.524  30.572  1.00 43.05  ?  278 LEU B CG  1 
ATOM   416  C CD1 . LEU A 1 55  ? 17.703 22.641  29.782  1.00 53.31  ?  278 LEU B CD1 1 
ATOM   417  C CD2 . LEU A 1 55  ? 17.334 20.617  31.218  1.00 45.35  ?  278 LEU B CD2 1 
ATOM   418  N N   . SER A 1 56  ? 20.303 18.829  27.072  1.00 36.81  ?  279 SER B N   1 
ATOM   419  C CA  . SER A 1 56  ? 21.491 18.424  26.329  1.00 41.44  ?  279 SER B CA  1 
ATOM   420  C C   . SER A 1 56  ? 21.338 18.801  24.861  1.00 43.37  ?  279 SER B C   1 
ATOM   421  O O   . SER A 1 56  ? 20.381 18.357  24.216  1.00 40.00  ?  279 SER B O   1 
ATOM   422  C CB  . SER A 1 56  ? 21.726 16.924  26.463  1.00 41.73  ?  279 SER B CB  1 
ATOM   423  O OG  . SER A 1 56  ? 22.829 16.505  25.678  1.00 40.38  ?  279 SER B OG  1 
ATOM   424  N N   . PRO A 1 57  ? 22.241 19.607  24.298  1.00 40.46  ?  280 PRO B N   1 
ATOM   425  C CA  . PRO A 1 57  ? 22.123 19.952  22.874  1.00 42.01  ?  280 PRO B CA  1 
ATOM   426  C C   . PRO A 1 57  ? 22.499 18.814  21.944  1.00 43.01  ?  280 PRO B C   1 
ATOM   427  O O   . PRO A 1 57  ? 22.030 18.792  20.799  1.00 44.40  ?  280 PRO B O   1 
ATOM   428  C CB  . PRO A 1 57  ? 23.085 21.137  22.721  1.00 42.24  ?  280 PRO B CB  1 
ATOM   429  C CG  . PRO A 1 57  ? 24.111 20.914  23.782  1.00 45.35  ?  280 PRO B CG  1 
ATOM   430  C CD  . PRO A 1 57  ? 23.406 20.244  24.936  1.00 42.86  ?  280 PRO B CD  1 
ATOM   431  N N   . VAL A 1 58  ? 23.325 17.866  22.398  1.00 42.97  ?  281 VAL B N   1 
ATOM   432  C CA  . VAL A 1 58  ? 23.768 16.769  21.540  1.00 46.72  ?  281 VAL B CA  1 
ATOM   433  C C   . VAL A 1 58  ? 22.856 15.554  21.607  1.00 46.25  ?  281 VAL B C   1 
ATOM   434  O O   . VAL A 1 58  ? 22.997 14.641  20.781  1.00 48.56  ?  281 VAL B O   1 
ATOM   435  C CB  . VAL A 1 58  ? 25.203 16.330  21.898  1.00 46.65  ?  281 VAL B CB  1 
ATOM   436  C CG1 . VAL A 1 58  ? 26.192 17.443  21.588  1.00 38.87  ?  281 VAL B CG1 1 
ATOM   437  C CG2 . VAL A 1 58  ? 25.279 15.924  23.364  1.00 37.22  ?  281 VAL B CG2 1 
ATOM   438  N N   . ASN A 1 59  ? 21.924 15.511  22.559  1.00 41.78  ?  282 ASN B N   1 
ATOM   439  C CA  . ASN A 1 59  ? 21.047 14.362  22.727  1.00 41.95  ?  282 ASN B CA  1 
ATOM   440  C C   . ASN A 1 59  ? 19.656 14.594  22.149  1.00 41.76  ?  282 ASN B C   1 
ATOM   441  O O   . ASN A 1 59  ? 18.723 13.852  22.473  1.00 48.80  ?  282 ASN B O   1 
ATOM   442  C CB  . ASN A 1 59  ? 20.962 13.981  24.202  1.00 45.07  ?  282 ASN B CB  1 
ATOM   443  C CG  . ASN A 1 59  ? 21.921 12.869  24.562  1.00 50.44  ?  282 ASN B CG  1 
ATOM   444  O OD1 . ASN A 1 59  ? 22.524 12.243  23.688  1.00 55.04  ?  282 ASN B OD1 1 
ATOM   445  N ND2 . ASN A 1 59  ? 22.088 12.631  25.853  1.00 56.11  ?  282 ASN B ND2 1 
ATOM   446  N N   . ILE A 1 60  ? 19.497 15.604  21.301  1.00 41.79  ?  283 ILE B N   1 
ATOM   447  C CA  . ILE A 1 60  ? 18.267 15.759  20.536  1.00 39.49  ?  283 ILE B CA  1 
ATOM   448  C C   . ILE A 1 60  ? 18.296 14.771  19.378  1.00 40.71  ?  283 ILE B C   1 
ATOM   449  O O   . ILE A 1 60  ? 19.305 14.661  18.670  1.00 39.64  ?  283 ILE B O   1 
ATOM   450  C CB  . ILE A 1 60  ? 18.108 17.206  20.042  1.00 37.53  ?  283 ILE B CB  1 
ATOM   451  C CG1 . ILE A 1 60  ? 18.183 18.181  21.220  1.00 39.32  ?  283 ILE B CG1 1 
ATOM   452  C CG2 . ILE A 1 60  ? 16.794 17.375  19.294  1.00 35.29  ?  283 ILE B CG2 1 
ATOM   453  C CD1 . ILE A 1 60  ? 18.604 19.580  20.827  1.00 41.00  ?  283 ILE B CD1 1 
ATOM   454  N N   . CYS A 1 61  ? 17.199 14.029  19.206  1.00 38.13  ?  284 CYS B N   1 
ATOM   455  C CA  . CYS A 1 61  ? 17.040 13.038  18.140  1.00 42.42  ?  284 CYS B CA  1 
ATOM   456  C C   . CYS A 1 61  ? 18.002 11.860  18.287  1.00 42.46  ?  284 CYS B C   1 
ATOM   457  O O   . CYS A 1 61  ? 18.360 11.217  17.298  1.00 42.24  ?  284 CYS B O   1 
ATOM   458  C CB  . CYS A 1 61  ? 17.189 13.672  16.752  1.00 39.92  ?  284 CYS B CB  1 
ATOM   459  S SG  . CYS A 1 61  ? 15.930 14.911  16.361  1.00 43.15  ?  284 CYS B SG  1 
ATOM   460  N N   . THR A 1 62  ? 18.423 11.560  19.513  1.00 38.60  ?  285 THR B N   1 
ATOM   461  C CA  . THR A 1 62  ? 19.197 10.361  19.805  1.00 41.16  ?  285 THR B CA  1 
ATOM   462  C C   . THR A 1 62  ? 18.340 9.379   20.594  1.00 44.06  ?  285 THR B C   1 
ATOM   463  O O   . THR A 1 62  ? 17.471 9.775   21.376  1.00 45.09  ?  285 THR B O   1 
ATOM   464  C CB  . THR A 1 62  ? 20.469 10.682  20.598  1.00 40.59  ?  285 THR B CB  1 
ATOM   465  O OG1 . THR A 1 62  ? 20.125 10.975  21.958  1.00 45.63  ?  285 THR B OG1 1 
ATOM   466  C CG2 . THR A 1 62  ? 21.190 11.872  19.994  1.00 32.09  ?  285 THR B CG2 1 
ATOM   467  N N   . PHE A 1 63  ? 18.591 8.090   20.377  1.00 40.50  ?  286 PHE B N   1 
ATOM   468  C CA  . PHE A 1 63  ? 17.858 7.026   21.049  1.00 40.97  ?  286 PHE B CA  1 
ATOM   469  C C   . PHE A 1 63  ? 18.839 6.063   21.697  1.00 37.79  ?  286 PHE B C   1 
ATOM   470  O O   . PHE A 1 63  ? 19.905 5.781   21.140  1.00 38.78  ?  286 PHE B O   1 
ATOM   471  C CB  . PHE A 1 63  ? 16.955 6.261   20.077  1.00 37.36  ?  286 PHE B CB  1 
ATOM   472  C CG  . PHE A 1 63  ? 15.962 7.125   19.357  1.00 38.26  ?  286 PHE B CG  1 
ATOM   473  C CD1 . PHE A 1 63  ? 14.723 7.390   19.914  1.00 38.20  ?  286 PHE B CD1 1 
ATOM   474  C CD2 . PHE A 1 63  ? 16.262 7.659   18.116  1.00 40.63  ?  286 PHE B CD2 1 
ATOM   475  C CE1 . PHE A 1 63  ? 13.805 8.179   19.251  1.00 37.78  ?  286 PHE B CE1 1 
ATOM   476  C CE2 . PHE A 1 63  ? 15.349 8.449   17.449  1.00 37.44  ?  286 PHE B CE2 1 
ATOM   477  C CZ  . PHE A 1 63  ? 14.119 8.709   18.017  1.00 40.08  ?  286 PHE B CZ  1 
ATOM   478  N N   . ARG A 1 64  ? 18.468 5.559   22.873  1.00 39.71  ?  287 ARG B N   1 
ATOM   479  C CA  . ARG A 1 64  ? 19.269 4.594   23.608  1.00 37.93  ?  287 ARG B CA  1 
ATOM   480  C C   . ARG A 1 64  ? 18.386 3.432   24.039  1.00 36.57  ?  287 ARG B C   1 
ATOM   481  O O   . ARG A 1 64  ? 17.196 3.608   24.318  1.00 35.84  ?  287 ARG B O   1 
ATOM   482  C CB  . ARG A 1 64  ? 19.928 5.229   24.841  1.00 40.62  ?  287 ARG B CB  1 
ATOM   483  C CG  . ARG A 1 64  ? 21.211 5.984   24.544  1.00 42.44  ?  287 ARG B CG  1 
ATOM   484  C CD  . ARG A 1 64  ? 21.700 6.739   25.772  1.00 42.00  ?  287 ARG B CD  1 
ATOM   485  N NE  . ARG A 1 64  ? 22.831 7.603   25.458  1.00 38.08  ?  287 ARG B NE  1 
ATOM   486  C CZ  . ARG A 1 64  ? 22.730 8.780   24.854  1.00 41.97  ?  287 ARG B CZ  1 
ATOM   487  N NH1 . ARG A 1 64  ? 21.553 9.279   24.503  1.00 40.11  ?  287 ARG B NH1 1 
ATOM   488  N NH2 . ARG A 1 64  ? 23.833 9.473   24.595  1.00 38.98  ?  287 ARG B NH2 1 
ATOM   489  N N   . GLY A 1 65  ? 18.979 2.246   24.092  1.00 40.31  ?  288 GLY B N   1 
ATOM   490  C CA  . GLY A 1 65  ? 18.257 1.068   24.538  1.00 35.40  ?  288 GLY B CA  1 
ATOM   491  C C   . GLY A 1 65  ? 18.912 -0.197  24.009  1.00 40.59  ?  288 GLY B C   1 
ATOM   492  O O   . GLY A 1 65  ? 20.099 -0.210  23.687  1.00 40.40  ?  288 GLY B O   1 
ATOM   493  N N   . ASP A 1 66  ? 18.106 -1.256  23.940  1.00 41.22  ?  289 ASP B N   1 
ATOM   494  C CA  . ASP A 1 66  ? 18.516 -2.535  23.378  1.00 42.09  ?  289 ASP B CA  1 
ATOM   495  C C   . ASP A 1 66  ? 17.669 -2.837  22.149  1.00 41.69  ?  289 ASP B C   1 
ATOM   496  O O   . ASP A 1 66  ? 16.519 -2.401  22.047  1.00 42.55  ?  289 ASP B O   1 
ATOM   497  C CB  . ASP A 1 66  ? 18.379 -3.669  24.401  1.00 41.38  ?  289 ASP B CB  1 
ATOM   498  C CG  . ASP A 1 66  ? 16.934 -4.049  24.664  1.00 48.05  ?  289 ASP B CG  1 
ATOM   499  O OD1 . ASP A 1 66  ? 16.225 -3.262  25.326  1.00 58.20  ?  289 ASP B OD1 1 
ATOM   500  O OD2 . ASP A 1 66  ? 16.507 -5.131  24.209  1.00 54.08  ?  289 ASP B OD2 1 
ATOM   501  N N   . VAL A 1 67  ? 18.243 -3.593  21.215  1.00 39.88  ?  290 VAL B N   1 
ATOM   502  C CA  . VAL A 1 67  ? 17.612 -3.866  19.929  1.00 45.23  ?  290 VAL B CA  1 
ATOM   503  C C   . VAL A 1 67  ? 17.298 -5.353  19.819  1.00 42.41  ?  290 VAL B C   1 
ATOM   504  O O   . VAL A 1 67  ? 18.074 -6.203  20.272  1.00 39.55  ?  290 VAL B O   1 
ATOM   505  C CB  . VAL A 1 67  ? 18.496 -3.406  18.753  1.00 44.65  ?  290 VAL B CB  1 
ATOM   506  C CG1 . VAL A 1 67  ? 18.544 -1.886  18.688  1.00 46.07  ?  290 VAL B CG1 1 
ATOM   507  C CG2 . VAL A 1 67  ? 19.900 -3.983  18.874  1.00 41.66  ?  290 VAL B CG2 1 
ATOM   508  N N   . THR A 1 68  ? 16.144 -5.656  19.229  1.00 47.18  ?  291 THR B N   1 
ATOM   509  C CA  . THR A 1 68  ? 15.766 -6.997  18.805  1.00 48.93  ?  291 THR B CA  1 
ATOM   510  C C   . THR A 1 68  ? 15.209 -6.908  17.389  1.00 48.85  ?  291 THR B C   1 
ATOM   511  O O   . THR A 1 68  ? 14.985 -5.815  16.859  1.00 44.92  ?  291 THR B O   1 
ATOM   512  C CB  . THR A 1 68  ? 14.728 -7.630  19.746  1.00 47.88  ?  291 THR B CB  1 
ATOM   513  O OG1 . THR A 1 68  ? 13.553 -6.811  19.786  1.00 50.76  ?  291 THR B OG1 1 
ATOM   514  C CG2 . THR A 1 68  ? 15.291 -7.777  21.155  1.00 43.43  ?  291 THR B CG2 1 
ATOM   515  N N   . HIS A 1 69  ? 14.978 -8.066  16.772  1.00 46.34  ?  292 HIS B N   1 
ATOM   516  C CA  . HIS A 1 69  ? 14.470 -8.081  15.407  1.00 46.37  ?  292 HIS B CA  1 
ATOM   517  C C   . HIS A 1 69  ? 13.933 -9.464  15.069  1.00 45.35  ?  292 HIS B C   1 
ATOM   518  O O   . HIS A 1 69  ? 14.297 -10.465 15.691  1.00 43.88  ?  292 HIS B O   1 
ATOM   519  C CB  . HIS A 1 69  ? 15.552 -7.679  14.397  1.00 43.39  ?  292 HIS B CB  1 
ATOM   520  C CG  . HIS A 1 69  ? 16.620 -8.713  14.205  1.00 48.04  ?  292 HIS B CG  1 
ATOM   521  N ND1 . HIS A 1 69  ? 17.270 -8.894  13.004  1.00 47.20  ?  292 HIS B ND1 1 
ATOM   522  C CD2 . HIS A 1 69  ? 17.156 -9.613  15.063  1.00 45.91  ?  292 HIS B CD2 1 
ATOM   523  C CE1 . HIS A 1 69  ? 18.158 -9.865  13.128  1.00 44.86  ?  292 HIS B CE1 1 
ATOM   524  N NE2 . HIS A 1 69  ? 18.108 -10.319 14.368  1.00 46.01  ?  292 HIS B NE2 1 
ATOM   525  N N   . ILE A 1 70  ? 13.049 -9.497  14.069  1.00 44.86  ?  293 ILE B N   1 
ATOM   526  C CA  . ILE A 1 70  ? 12.687 -10.761 13.442  1.00 46.95  ?  293 ILE B CA  1 
ATOM   527  C C   . ILE A 1 70  ? 13.934 -11.357 12.806  1.00 44.33  ?  293 ILE B C   1 
ATOM   528  O O   . ILE A 1 70  ? 14.718 -10.653 12.157  1.00 44.39  ?  293 ILE B O   1 
ATOM   529  C CB  . ILE A 1 70  ? 11.571 -10.542 12.405  1.00 47.55  ?  293 ILE B CB  1 
ATOM   530  C CG1 . ILE A 1 70  ? 10.239 -10.260 13.104  1.00 47.52  ?  293 ILE B CG1 1 
ATOM   531  C CG2 . ILE A 1 70  ? 11.445 -11.747 11.476  1.00 46.39  ?  293 ILE B CG2 1 
ATOM   532  C CD1 . ILE A 1 70  ? 9.185  -9.663  12.192  1.00 48.01  ?  293 ILE B CD1 1 
ATOM   533  N N   . THR A 1 71  ? 14.135 -12.658 13.011  1.00 43.84  ?  294 THR B N   1 
ATOM   534  C CA  . THR A 1 71  ? 15.343 -13.317 12.528  1.00 45.79  ?  294 THR B CA  1 
ATOM   535  C C   . THR A 1 71  ? 15.499 -13.126 11.023  1.00 45.94  ?  294 THR B C   1 
ATOM   536  O O   . THR A 1 71  ? 14.577 -13.406 10.250  1.00 44.97  ?  294 THR B O   1 
ATOM   537  C CB  . THR A 1 71  ? 15.309 -14.807 12.868  1.00 43.56  ?  294 THR B CB  1 
ATOM   538  O OG1 . THR A 1 71  ? 15.029 -14.976 14.263  1.00 51.73  ?  294 THR B OG1 1 
ATOM   539  C CG2 . THR A 1 71  ? 16.646 -15.457 12.544  1.00 39.31  ?  294 THR B CG2 1 
ATOM   540  N N   . GLY A 1 72  ? 16.665 -12.633 10.614  1.00 44.21  ?  295 GLY B N   1 
ATOM   541  C CA  . GLY A 1 72  ? 16.957 -12.396 9.217   1.00 46.31  ?  295 GLY B CA  1 
ATOM   542  C C   . GLY A 1 72  ? 16.542 -11.041 8.684   1.00 52.37  ?  295 GLY B C   1 
ATOM   543  O O   . GLY A 1 72  ? 16.830 -10.741 7.519   1.00 53.88  ?  295 GLY B O   1 
ATOM   544  N N   . SER A 1 73  ? 15.883 -10.214 9.490   1.00 47.88  ?  296 SER B N   1 
ATOM   545  C CA  . SER A 1 73  ? 15.412 -8.916  9.032   1.00 46.63  ?  296 SER B CA  1 
ATOM   546  C C   . SER A 1 73  ? 16.458 -7.838  9.282   1.00 45.97  ?  296 SER B C   1 
ATOM   547  O O   . SER A 1 73  ? 17.257 -7.921  10.219  1.00 49.17  ?  296 SER B O   1 
ATOM   548  C CB  . SER A 1 73  ? 14.105 -8.536  9.730   1.00 45.03  ?  296 SER B CB  1 
ATOM   549  O OG  . SER A 1 73  ? 13.737 -7.201  9.424   1.00 41.61  ?  296 SER B OG  1 
ATOM   550  N N   . ARG A 1 74  ? 16.446 -6.819  8.425   1.00 45.64  ?  297 ARG B N   1 
ATOM   551  C CA  . ARG A 1 74  ? 17.304 -5.656  8.598   1.00 48.73  ?  297 ARG B CA  1 
ATOM   552  C C   . ARG A 1 74  ? 16.661 -4.575  9.455   1.00 47.24  ?  297 ARG B C   1 
ATOM   553  O O   . ARG A 1 74  ? 17.357 -3.647  9.880   1.00 41.49  ?  297 ARG B O   1 
ATOM   554  C CB  . ARG A 1 74  ? 17.687 -5.072  7.235   1.00 49.20  ?  297 ARG B CB  1 
ATOM   555  C CG  . ARG A 1 74  ? 18.635 -5.949  6.433   1.00 56.29  ?  297 ARG B CG  1 
ATOM   556  C CD  . ARG A 1 74  ? 18.482 -5.716  4.939   1.00 61.05  ?  297 ARG B CD  1 
ATOM   557  N NE  . ARG A 1 74  ? 19.771 -5.657  4.261   1.00 63.63  ?  297 ARG B NE  1 
ATOM   558  C CZ  . ARG A 1 74  ? 20.307 -6.663  3.584   1.00 68.93  ?  297 ARG B CZ  1 
ATOM   559  N NH1 . ARG A 1 74  ? 19.689 -7.827  3.473   1.00 62.93  ?  297 ARG B NH1 1 
ATOM   560  N NH2 . ARG A 1 74  ? 21.492 -6.497  3.003   1.00 70.40  ?  297 ARG B NH2 1 
ATOM   561  N N   . ASN A 1 75  ? 15.359 -4.672  9.711   1.00 46.05  ?  298 ASN B N   1 
ATOM   562  C CA  . ASN A 1 75  ? 14.683 -3.747  10.609  1.00 45.51  ?  298 ASN B CA  1 
ATOM   563  C C   . ASN A 1 75  ? 14.864 -4.205  12.050  1.00 46.42  ?  298 ASN B C   1 
ATOM   564  O O   . ASN A 1 75  ? 14.613 -5.369  12.378  1.00 43.88  ?  298 ASN B O   1 
ATOM   565  C CB  . ASN A 1 75  ? 13.197 -3.661  10.261  1.00 45.08  ?  298 ASN B CB  1 
ATOM   566  C CG  . ASN A 1 75  ? 12.641 -2.262  10.420  1.00 56.23  ?  298 ASN B CG  1 
ATOM   567  O OD1 . ASN A 1 75  ? 12.999 -1.349  9.674   1.00 59.90  ?  298 ASN B OD1 1 
ATOM   568  N ND2 . ASN A 1 75  ? 11.757 -2.085  11.394  1.00 59.59  ?  298 ASN B ND2 1 
ATOM   569  N N   . TYR A 1 76  ? 15.305 -3.289  12.909  1.00 38.80  ?  299 TYR B N   1 
ATOM   570  C CA  . TYR A 1 76  ? 15.531 -3.573  14.321  1.00 40.43  ?  299 TYR B CA  1 
ATOM   571  C C   . TYR A 1 76  ? 14.600 -2.715  15.162  1.00 44.54  ?  299 TYR B C   1 
ATOM   572  O O   . TYR A 1 76  ? 14.476 -1.510  14.923  1.00 47.67  ?  299 TYR B O   1 
ATOM   573  C CB  . TYR A 1 76  ? 16.985 -3.305  14.715  1.00 38.85  ?  299 TYR B CB  1 
ATOM   574  C CG  . TYR A 1 76  ? 17.960 -4.346  14.220  1.00 44.14  ?  299 TYR B CG  1 
ATOM   575  C CD1 . TYR A 1 76  ? 18.529 -4.246  12.959  1.00 46.97  ?  299 TYR B CD1 1 
ATOM   576  C CD2 . TYR A 1 76  ? 18.313 -5.429  15.015  1.00 47.94  ?  299 TYR B CD2 1 
ATOM   577  C CE1 . TYR A 1 76  ? 19.422 -5.193  12.501  1.00 47.57  ?  299 TYR B CE1 1 
ATOM   578  C CE2 . TYR A 1 76  ? 19.206 -6.383  14.567  1.00 46.13  ?  299 TYR B CE2 1 
ATOM   579  C CZ  . TYR A 1 76  ? 19.758 -6.259  13.308  1.00 50.34  ?  299 TYR B CZ  1 
ATOM   580  O OH  . TYR A 1 76  ? 20.648 -7.206  12.856  1.00 51.48  ?  299 TYR B OH  1 
ATOM   581  N N   . THR A 1 77  ? 13.951 -3.337  16.142  1.00 42.78  ?  300 THR B N   1 
ATOM   582  C CA  . THR A 1 77  ? 13.133 -2.630  17.116  1.00 44.78  ?  300 THR B CA  1 
ATOM   583  C C   . THR A 1 77  ? 13.972 -2.357  18.357  1.00 46.44  ?  300 THR B C   1 
ATOM   584  O O   . THR A 1 77  ? 14.553 -3.284  18.933  1.00 44.64  ?  300 THR B O   1 
ATOM   585  C CB  . THR A 1 77  ? 11.888 -3.440  17.486  1.00 46.06  ?  300 THR B CB  1 
ATOM   586  O OG1 . THR A 1 77  ? 10.920 -3.340  16.435  1.00 51.03  ?  300 THR B OG1 1 
ATOM   587  C CG2 . THR A 1 77  ? 11.273 -2.918  18.779  1.00 46.38  ?  300 THR B CG2 1 
ATOM   588  N N   . MET A 1 78  ? 14.044 -1.092  18.758  1.00 42.77  ?  301 MET B N   1 
ATOM   589  C CA  . MET A 1 78  ? 14.813 -0.688  19.926  1.00 42.80  ?  301 MET B CA  1 
ATOM   590  C C   . MET A 1 78  ? 13.863 -0.386  21.079  1.00 44.38  ?  301 MET B C   1 
ATOM   591  O O   . MET A 1 78  ? 12.969 0.458   20.948  1.00 46.46  ?  301 MET B O   1 
ATOM   592  C CB  . MET A 1 78  ? 15.687 0.528   19.619  1.00 46.81  ?  301 MET B CB  1 
ATOM   593  C CG  . MET A 1 78  ? 16.465 1.047   20.823  1.00 41.89  ?  301 MET B CG  1 
ATOM   594  S SD  . MET A 1 78  ? 17.016 2.755   20.633  1.00 41.53  ?  301 MET B SD  1 
ATOM   595  C CE  . MET A 1 78  ? 18.724 2.512   20.157  1.00 38.79  ?  301 MET B CE  1 
ATOM   596  N N   . ASN A 1 79  ? 14.049 -1.083  22.197  1.00 42.15  ?  302 ASN B N   1 
ATOM   597  C CA  . ASN A 1 79  ? 13.318 -0.787  23.424  1.00 47.04  ?  302 ASN B CA  1 
ATOM   598  C C   . ASN A 1 79  ? 14.049 0.335   24.149  1.00 39.06  ?  302 ASN B C   1 
ATOM   599  O O   . ASN A 1 79  ? 15.175 0.149   24.619  1.00 38.07  ?  302 ASN B O   1 
ATOM   600  C CB  . ASN A 1 79  ? 13.200 -2.034  24.295  1.00 37.93  ?  302 ASN B CB  1 
ATOM   601  C CG  . ASN A 1 79  ? 12.658 -3.228  23.531  1.00 48.97  ?  302 ASN B CG  1 
ATOM   602  O OD1 . ASN A 1 79  ? 13.274 -4.292  23.498  1.00 51.38  ?  302 ASN B OD1 1 
ATOM   603  N ND2 . ASN A 1 79  ? 11.497 -3.052  22.908  1.00 51.27  ?  302 ASN B ND2 1 
ATOM   604  N N   . LEU A 1 80  ? 13.412 1.500   24.236  1.00 41.90  ?  303 LEU B N   1 
ATOM   605  C CA  . LEU A 1 80  ? 14.099 2.695   24.707  1.00 42.48  ?  303 LEU B CA  1 
ATOM   606  C C   . LEU A 1 80  ? 14.418 2.609   26.195  1.00 39.95  ?  303 LEU B C   1 
ATOM   607  O O   . LEU A 1 80  ? 13.584 2.200   27.009  1.00 47.04  ?  303 LEU B O   1 
ATOM   608  C CB  . LEU A 1 80  ? 13.253 3.938   24.433  1.00 37.63  ?  303 LEU B CB  1 
ATOM   609  C CG  . LEU A 1 80  ? 12.947 4.260   22.968  1.00 43.28  ?  303 LEU B CG  1 
ATOM   610  C CD1 . LEU A 1 80  ? 12.009 5.454   22.862  1.00 42.84  ?  303 LEU B CD1 1 
ATOM   611  C CD2 . LEU A 1 80  ? 14.230 4.515   22.191  1.00 42.65  ?  303 LEU B CD2 1 
ATOM   612  N N   . ALA A 1 81  ? 15.644 2.986   26.539  1.00 40.02  ?  304 ALA B N   1 
ATOM   613  C CA  . ALA A 1 81  ? 16.038 3.270   27.910  1.00 37.75  ?  304 ALA B CA  1 
ATOM   614  C C   . ALA A 1 81  ? 16.185 4.775   28.085  1.00 42.03  ?  304 ALA B C   1 
ATOM   615  O O   . ALA A 1 81  ? 16.071 5.553   27.136  1.00 40.06  ?  304 ALA B O   1 
ATOM   616  C CB  . ALA A 1 81  ? 17.343 2.559   28.275  1.00 32.36  ?  304 ALA B CB  1 
ATOM   617  N N   . SER A 1 82  ? 16.434 5.184   29.324  1.00 45.09  ?  305 SER B N   1 
ATOM   618  C CA  . SER A 1 82  ? 16.687 6.588   29.588  1.00 44.55  ?  305 SER B CA  1 
ATOM   619  C C   . SER A 1 82  ? 18.031 7.003   28.995  1.00 45.81  ?  305 SER B C   1 
ATOM   620  O O   . SER A 1 82  ? 18.831 6.175   28.543  1.00 39.64  ?  305 SER B O   1 
ATOM   621  C CB  . SER A 1 82  ? 16.653 6.862   31.090  1.00 38.66  ?  305 SER B CB  1 
ATOM   622  O OG  . SER A 1 82  ? 16.401 8.231   31.349  1.00 56.38  ?  305 SER B OG  1 
ATOM   623  N N   . GLN A 1 83  ? 18.274 8.316   28.989  1.00 41.18  ?  306 GLN B N   1 
ATOM   624  C CA  . GLN A 1 83  ? 19.538 8.829   28.473  1.00 39.46  ?  306 GLN B CA  1 
ATOM   625  C C   . GLN A 1 83  ? 20.718 8.349   29.309  1.00 40.21  ?  306 GLN B C   1 
ATOM   626  O O   . GLN A 1 83  ? 21.811 8.133   28.774  1.00 43.50  ?  306 GLN B O   1 
ATOM   627  C CB  . GLN A 1 83  ? 19.496 10.356  28.424  1.00 47.66  ?  306 GLN B CB  1 
ATOM   628  C CG  . GLN A 1 83  ? 20.855 11.008  28.261  1.00 46.96  ?  306 GLN B CG  1 
ATOM   629  C CD  . GLN A 1 83  ? 21.054 12.201  29.172  1.00 63.42  ?  306 GLN B CD  1 
ATOM   630  O OE1 . GLN A 1 83  ? 21.195 12.054  30.388  1.00 46.33  ?  306 GLN B OE1 1 
ATOM   631  N NE2 . GLN A 1 83  ? 21.073 13.395  28.588  1.00 60.25  ?  306 GLN B NE2 1 
ATOM   632  N N   . ASN A 1 84  ? 20.518 8.163   30.614  1.00 39.78  ?  307 ASN B N   1 
ATOM   633  C CA  . ASN A 1 84  ? 21.542 7.605   31.487  1.00 41.22  ?  307 ASN B CA  1 
ATOM   634  C C   . ASN A 1 84  ? 21.449 6.086   31.599  1.00 43.83  ?  307 ASN B C   1 
ATOM   635  O O   . ASN A 1 84  ? 22.002 5.508   32.542  1.00 41.33  ?  307 ASN B O   1 
ATOM   636  C CB  . ASN A 1 84  ? 21.461 8.247   32.875  1.00 42.03  ?  307 ASN B CB  1 
ATOM   637  C CG  . ASN A 1 84  ? 20.084 8.126   33.501  1.00 45.76  ?  307 ASN B CG  1 
ATOM   638  O OD1 . ASN A 1 84  ? 19.219 7.404   33.004  1.00 43.80  ?  307 ASN B OD1 1 
ATOM   639  N ND2 . ASN A 1 84  ? 19.872 8.842   34.601  1.00 48.22  ?  307 ASN B ND2 1 
ATOM   640  N N   . TRP A 1 85  ? 20.753 5.439   30.661  1.00 45.47  ?  308 TRP B N   1 
ATOM   641  C CA  . TRP A 1 85  ? 20.581 3.992   30.559  1.00 43.28  ?  308 TRP B CA  1 
ATOM   642  C C   . TRP A 1 85  ? 19.682 3.414   31.644  1.00 42.88  ?  308 TRP B C   1 
ATOM   643  O O   . TRP A 1 85  ? 19.654 2.190   31.822  1.00 50.96  ?  308 TRP B O   1 
ATOM   644  C CB  . TRP A 1 85  ? 21.925 3.255   30.565  1.00 40.25  ?  308 TRP B CB  1 
ATOM   645  C CG  . TRP A 1 85  ? 22.791 3.616   29.408  1.00 43.82  ?  308 TRP B CG  1 
ATOM   646  C CD1 . TRP A 1 85  ? 23.886 4.430   29.424  1.00 42.71  ?  308 TRP B CD1 1 
ATOM   647  C CD2 . TRP A 1 85  ? 22.630 3.185   28.052  1.00 40.71  ?  308 TRP B CD2 1 
ATOM   648  N NE1 . TRP A 1 85  ? 24.421 4.528   28.162  1.00 44.97  ?  308 TRP B NE1 1 
ATOM   649  C CE2 . TRP A 1 85  ? 23.667 3.772   27.302  1.00 37.13  ?  308 TRP B CE2 1 
ATOM   650  C CE3 . TRP A 1 85  ? 21.712 2.355   27.402  1.00 45.22  ?  308 TRP B CE3 1 
ATOM   651  C CZ2 . TRP A 1 85  ? 23.812 3.559   25.932  1.00 41.48  ?  308 TRP B CZ2 1 
ATOM   652  C CZ3 . TRP A 1 85  ? 21.856 2.142   26.042  1.00 35.11  ?  308 TRP B CZ3 1 
ATOM   653  C CH2 . TRP A 1 85  ? 22.899 2.742   25.321  1.00 38.98  ?  308 TRP B CH2 1 
ATOM   654  N N   . ASN A 1 86  ? 18.932 4.271   32.311  1.00 43.69  ?  309 ASN B N   1 
ATOM   655  C CA  . ASN A 1 86  ? 17.989 3.772   33.335  1.00 43.96  ?  309 ASN B CA  1 
ATOM   656  C C   . ASN A 1 86  ? 16.686 3.362   32.653  1.00 46.23  ?  309 ASN B C   1 
ATOM   657  O O   . ASN A 1 86  ? 16.562 3.566   31.454  1.00 43.52  ?  309 ASN B O   1 
ATOM   658  C CB  . ASN A 1 86  ? 17.900 4.718   34.533  1.00 47.07  ?  309 ASN B CB  1 
ATOM   659  C CG  . ASN A 1 86  ? 19.180 4.725   35.341  1.00 45.05  ?  309 ASN B CG  1 
ATOM   660  O OD1 . ASN A 1 86  ? 20.137 4.037   35.007  1.00 44.84  ?  309 ASN B OD1 1 
ATOM   661  N ND2 . ASN A 1 86  ? 19.214 5.505   36.402  1.00 52.93  ?  309 ASN B ND2 1 
ATOM   662  N N   . ASP A 1 87  ? 15.767 2.784   33.409  1.00 41.68  ?  310 ASP B N   1 
ATOM   663  C CA  . ASP A 1 87  ? 14.508 2.310   32.851  1.00 46.38  ?  310 ASP B CA  1 
ATOM   664  C C   . ASP A 1 87  ? 13.656 3.477   32.369  1.00 45.05  ?  310 ASP B C   1 
ATOM   665  O O   . ASP A 1 87  ? 13.492 4.474   33.078  1.00 48.98  ?  310 ASP B O   1 
ATOM   666  C CB  . ASP A 1 87  ? 13.739 1.493   33.889  1.00 45.18  ?  310 ASP B CB  1 
ATOM   667  C CG  . ASP A 1 87  ? 14.490 0.250   34.332  1.00 48.36  ?  310 ASP B CG  1 
ATOM   668  O OD1 . ASP A 1 87  ? 15.435 -0.164  33.625  1.00 50.47  ?  310 ASP B OD1 1 
ATOM   669  O OD2 . ASP A 1 87  ? 14.134 -0.315  35.386  1.00 45.67  ?  310 ASP B OD2 1 
ATOM   670  N N   . TYR A 1 88  ? 13.110 3.350   31.161  1.00 48.26  ?  311 TYR B N   1 
ATOM   671  C CA  . TYR A 1 88  ? 12.212 4.369   30.636  1.00 51.34  ?  311 TYR B CA  1 
ATOM   672  C C   . TYR A 1 88  ? 10.893 4.342   31.399  1.00 51.42  ?  311 TYR B C   1 
ATOM   673  O O   . TYR A 1 88  ? 10.304 3.277   31.609  1.00 58.51  ?  311 TYR B O   1 
ATOM   674  C CB  . TYR A 1 88  ? 11.967 4.147   29.144  1.00 48.45  ?  311 TYR B CB  1 
ATOM   675  C CG  . TYR A 1 88  ? 10.828 4.973   28.587  1.00 51.66  ?  311 TYR B CG  1 
ATOM   676  C CD1 . TYR A 1 88  ? 10.857 6.362   28.646  1.00 46.17  ?  311 TYR B CD1 1 
ATOM   677  C CD2 . TYR A 1 88  ? 9.720  4.364   28.010  1.00 50.56  ?  311 TYR B CD2 1 
ATOM   678  C CE1 . TYR A 1 88  ? 9.815  7.120   28.144  1.00 45.67  ?  311 TYR B CE1 1 
ATOM   679  C CE2 . TYR A 1 88  ? 8.674  5.117   27.503  1.00 49.16  ?  311 TYR B CE2 1 
ATOM   680  C CZ  . TYR A 1 88  ? 8.727  6.493   27.572  1.00 48.30  ?  311 TYR B CZ  1 
ATOM   681  O OH  . TYR A 1 88  ? 7.690  7.245   27.072  1.00 53.45  ?  311 TYR B OH  1 
ATOM   682  N N   . ASP A 1 89  ? 10.430 5.521   31.819  1.00 51.17  ?  312 ASP B N   1 
ATOM   683  C CA  . ASP A 1 89  ? 9.186  5.647   32.565  1.00 54.61  ?  312 ASP B CA  1 
ATOM   684  C C   . ASP A 1 89  ? 8.098  6.174   31.639  1.00 55.98  ?  312 ASP B C   1 
ATOM   685  O O   . ASP A 1 89  ? 8.040  7.388   31.386  1.00 56.79  ?  312 ASP B O   1 
ATOM   686  C CB  . ASP A 1 89  ? 9.370  6.580   33.765  1.00 58.75  ?  312 ASP B CB  1 
ATOM   687  C CG  . ASP A 1 89  ? 8.095  6.758   34.567  1.00 64.26  ?  312 ASP B CG  1 
ATOM   688  O OD1 . ASP A 1 89  ? 7.251  5.837   34.557  1.00 57.75  ?  312 ASP B OD1 1 
ATOM   689  O OD2 . ASP A 1 89  ? 7.937  7.819   35.208  1.00 65.95  ?  312 ASP B OD2 1 
ATOM   690  N N   . PRO A 1 90  ? 7.215  5.321   31.112  1.00 54.26  ?  313 PRO B N   1 
ATOM   691  C CA  . PRO A 1 90  ? 6.186  5.794   30.178  1.00 53.90  ?  313 PRO B CA  1 
ATOM   692  C C   . PRO A 1 90  ? 5.037  6.540   30.836  1.00 60.59  ?  313 PRO B C   1 
ATOM   693  O O   . PRO A 1 90  ? 4.097  6.927   30.134  1.00 58.53  ?  313 PRO B O   1 
ATOM   694  C CB  . PRO A 1 90  ? 5.683  4.489   29.524  1.00 55.14  ?  313 PRO B CB  1 
ATOM   695  C CG  . PRO A 1 90  ? 6.591  3.387   30.026  1.00 56.91  ?  313 PRO B CG  1 
ATOM   696  C CD  . PRO A 1 90  ? 7.141  3.868   31.323  1.00 56.21  ?  313 PRO B CD  1 
ATOM   697  N N   . THR A 1 91  ? 5.082  6.755   32.151  1.00 61.14  ?  314 THR B N   1 
ATOM   698  C CA  . THR A 1 91  ? 3.986  7.378   32.880  1.00 61.35  ?  314 THR B CA  1 
ATOM   699  C C   . THR A 1 91  ? 4.211  8.857   33.164  1.00 61.54  ?  314 THR B C   1 
ATOM   700  O O   . THR A 1 91  ? 3.320  9.506   33.720  1.00 61.60  ?  314 THR B O   1 
ATOM   701  C CB  . THR A 1 91  ? 3.743  6.638   34.202  1.00 64.43  ?  314 THR B CB  1 
ATOM   702  O OG1 . THR A 1 91  ? 4.742  7.020   35.157  1.00 63.09  ?  314 THR B OG1 1 
ATOM   703  C CG2 . THR A 1 91  ? 3.801  5.133   33.990  1.00 54.30  ?  314 THR B CG2 1 
ATOM   704  N N   . GLU A 1 92  ? 5.367  9.407   32.803  1.00 62.11  ?  315 GLU B N   1 
ATOM   705  C CA  . GLU A 1 92  ? 5.613  10.822  33.034  1.00 60.96  ?  315 GLU B CA  1 
ATOM   706  C C   . GLU A 1 92  ? 4.719  11.673  32.137  1.00 62.03  ?  315 GLU B C   1 
ATOM   707  O O   . GLU A 1 92  ? 4.347  11.275  31.031  1.00 58.06  ?  315 GLU B O   1 
ATOM   708  C CB  . GLU A 1 92  ? 7.085  11.164  32.788  1.00 62.96  ?  315 GLU B CB  1 
ATOM   709  C CG  . GLU A 1 92  ? 7.879  11.501  34.052  1.00 72.08  ?  315 GLU B CG  1 
ATOM   710  C CD  . GLU A 1 92  ? 7.618  12.907  34.581  1.00 83.72  ?  315 GLU B CD  1 
ATOM   711  O OE1 . GLU A 1 92  ? 6.530  13.467  34.322  1.00 79.92  ?  315 GLU B OE1 1 
ATOM   712  O OE2 . GLU A 1 92  ? 8.508  13.458  35.262  1.00 84.37  ?  315 GLU B OE2 1 
ATOM   713  N N   . GLU A 1 93  ? 4.372  12.861  32.633  1.00 63.21  ?  316 GLU B N   1 
ATOM   714  C CA  . GLU A 1 93  ? 3.453  13.762  31.936  1.00 65.97  ?  316 GLU B CA  1 
ATOM   715  C C   . GLU A 1 93  ? 4.175  14.518  30.819  1.00 64.49  ?  316 GLU B C   1 
ATOM   716  O O   . GLU A 1 93  ? 4.305  15.743  30.825  1.00 57.58  ?  316 GLU B O   1 
ATOM   717  C CB  . GLU A 1 93  ? 2.805  14.718  32.931  1.00 68.58  ?  316 GLU B CB  1 
ATOM   718  C CG  . GLU A 1 93  ? 2.089  14.021  34.079  1.00 74.54  ?  316 GLU B CG  1 
ATOM   719  C CD  . GLU A 1 93  ? 0.673  14.525  34.279  1.00 78.48  ?  316 GLU B CD  1 
ATOM   720  O OE1 . GLU A 1 93  ? 0.506  15.700  34.669  1.00 80.88  ?  316 GLU B OE1 1 
ATOM   721  O OE2 . GLU A 1 93  ? -0.274 13.744  34.046  1.00 77.08  ?  316 GLU B OE2 1 
ATOM   722  N N   . ILE A 1 94  ? 4.654  13.748  29.843  1.00 56.20  ?  317 ILE B N   1 
ATOM   723  C CA  . ILE A 1 94  ? 5.336  14.304  28.673  1.00 52.08  ?  317 ILE B CA  1 
ATOM   724  C C   . ILE A 1 94  ? 4.825  13.612  27.423  1.00 53.68  ?  317 ILE B C   1 
ATOM   725  O O   . ILE A 1 94  ? 4.355  12.466  27.465  1.00 50.63  ?  317 ILE B O   1 
ATOM   726  C CB  . ILE A 1 94  ? 6.870  14.140  28.766  1.00 50.25  ?  317 ILE B CB  1 
ATOM   727  C CG1 . ILE A 1 94  ? 7.248  12.660  28.881  1.00 48.21  ?  317 ILE B CG1 1 
ATOM   728  C CG2 . ILE A 1 94  ? 7.432  14.964  29.923  1.00 51.01  ?  317 ILE B CG2 1 
ATOM   729  C CD1 . ILE A 1 94  ? 8.646  12.420  29.412  1.00 44.66  ?  317 ILE B CD1 1 
ATOM   730  N N   . PRO A 1 95  ? 4.893  14.301  26.280  1.00 50.22  ?  318 PRO B N   1 
ATOM   731  C CA  . PRO A 1 95  ? 4.423  13.679  25.030  1.00 49.75  ?  318 PRO B CA  1 
ATOM   732  C C   . PRO A 1 95  ? 5.227  12.460  24.622  1.00 50.07  ?  318 PRO B C   1 
ATOM   733  O O   . PRO A 1 95  ? 4.685  11.558  23.968  1.00 45.58  ?  318 PRO B O   1 
ATOM   734  C CB  . PRO A 1 95  ? 4.558  14.807  23.999  1.00 45.29  ?  318 PRO B CB  1 
ATOM   735  C CG  . PRO A 1 95  ? 4.617  16.068  24.796  1.00 49.87  ?  318 PRO B CG  1 
ATOM   736  C CD  . PRO A 1 95  ? 5.282  15.709  26.085  1.00 47.90  ?  318 PRO B CD  1 
ATOM   737  N N   . ALA A 1 96  ? 6.502  12.405  24.992  1.00 46.73  ?  319 ALA B N   1 
ATOM   738  C CA  . ALA A 1 96  ? 7.423  11.354  24.581  1.00 43.11  ?  319 ALA B CA  1 
ATOM   739  C C   . ALA A 1 96  ? 8.707  11.523  25.382  1.00 42.63  ?  319 ALA B C   1 
ATOM   740  O O   . ALA A 1 96  ? 8.860  12.536  26.076  1.00 44.77  ?  319 ALA B O   1 
ATOM   741  C CB  . ALA A 1 96  ? 7.691  11.431  23.074  1.00 40.94  ?  319 ALA B CB  1 
ATOM   742  N N   . PRO A 1 97  ? 9.636  10.564  25.341  1.00 43.47  ?  320 PRO B N   1 
ATOM   743  C CA  . PRO A 1 97  ? 10.934 10.771  25.994  1.00 43.24  ?  320 PRO B CA  1 
ATOM   744  C C   . PRO A 1 97  ? 11.567 12.088  25.565  1.00 43.99  ?  320 PRO B C   1 
ATOM   745  O O   . PRO A 1 97  ? 11.417 12.531  24.424  1.00 45.21  ?  320 PRO B O   1 
ATOM   746  C CB  . PRO A 1 97  ? 11.766 9.565   25.535  1.00 37.00  ?  320 PRO B CB  1 
ATOM   747  C CG  . PRO A 1 97  ? 10.892 8.793   24.565  1.00 43.86  ?  320 PRO B CG  1 
ATOM   748  C CD  . PRO A 1 97  ? 9.489  9.177   24.875  1.00 40.84  ?  320 PRO B CD  1 
ATOM   749  N N   . LEU A 1 98  ? 12.267 12.723  26.503  1.00 37.66  ?  321 LEU B N   1 
ATOM   750  C CA  . LEU A 1 98  ? 12.832 14.042  26.253  1.00 46.79  ?  321 LEU B CA  1 
ATOM   751  C C   . LEU A 1 98  ? 13.871 13.979  25.140  1.00 42.21  ?  321 LEU B C   1 
ATOM   752  O O   . LEU A 1 98  ? 14.763 13.127  25.151  1.00 49.10  ?  321 LEU B O   1 
ATOM   753  C CB  . LEU A 1 98  ? 13.451 14.597  27.536  1.00 38.61  ?  321 LEU B CB  1 
ATOM   754  C CG  . LEU A 1 98  ? 12.487 14.701  28.720  1.00 44.13  ?  321 LEU B CG  1 
ATOM   755  C CD1 . LEU A 1 98  ? 13.175 15.303  29.937  1.00 38.77  ?  321 LEU B CD1 1 
ATOM   756  C CD2 . LEU A 1 98  ? 11.258 15.514  28.334  1.00 44.29  ?  321 LEU B CD2 1 
ATOM   757  N N   . GLY A 1 99  ? 13.746 14.887  24.173  1.00 41.66  ?  322 GLY B N   1 
ATOM   758  C CA  . GLY A 1 99  ? 14.619 14.908  23.020  1.00 43.35  ?  322 GLY B CA  1 
ATOM   759  C C   . GLY A 1 99  ? 14.100 14.160  21.812  1.00 41.48  ?  322 GLY B C   1 
ATOM   760  O O   . GLY A 1 99  ? 14.789 14.127  20.784  1.00 38.12  ?  322 GLY B O   1 
ATOM   761  N N   . THR A 1 100 ? 12.918 13.557  21.903  1.00 40.50  ?  323 THR B N   1 
ATOM   762  C CA  . THR A 1 100 ? 12.344 12.847  20.770  1.00 40.93  ?  323 THR B CA  1 
ATOM   763  C C   . THR A 1 100 ? 12.111 13.817  19.613  1.00 41.20  ?  323 THR B C   1 
ATOM   764  O O   . THR A 1 100 ? 11.688 14.957  19.839  1.00 39.35  ?  323 THR B O   1 
ATOM   765  C CB  . THR A 1 100 ? 11.027 12.180  21.181  1.00 43.12  ?  323 THR B CB  1 
ATOM   766  O OG1 . THR A 1 100 ? 11.287 11.181  22.177  1.00 42.93  ?  323 THR B OG1 1 
ATOM   767  C CG2 . THR A 1 100 ? 10.330 11.532  19.991  1.00 44.46  ?  323 THR B CG2 1 
ATOM   768  N N   . PRO A 1 101 ? 12.408 13.416  18.374  1.00 43.01  ?  324 PRO B N   1 
ATOM   769  C CA  . PRO A 1 101 ? 12.154 14.299  17.229  1.00 38.65  ?  324 PRO B CA  1 
ATOM   770  C C   . PRO A 1 101 ? 10.713 14.792  17.211  1.00 36.84  ?  324 PRO B C   1 
ATOM   771  O O   . PRO A 1 101 ? 9.778  14.050  17.517  1.00 37.80  ?  324 PRO B O   1 
ATOM   772  C CB  . PRO A 1 101 ? 12.459 13.409  16.020  1.00 39.38  ?  324 PRO B CB  1 
ATOM   773  C CG  . PRO A 1 101 ? 13.405 12.382  16.527  1.00 39.45  ?  324 PRO B CG  1 
ATOM   774  C CD  . PRO A 1 101 ? 13.111 12.180  17.987  1.00 41.54  ?  324 PRO B CD  1 
ATOM   775  N N   . ASP A 1 102 ? 10.540 16.064  16.855  1.00 37.62  ?  325 ASP B N   1 
ATOM   776  C CA  . ASP A 1 102 ? 9.227  16.694  16.817  1.00 42.14  ?  325 ASP B CA  1 
ATOM   777  C C   . ASP A 1 102 ? 8.792  17.031  15.392  1.00 41.04  ?  325 ASP B C   1 
ATOM   778  O O   . ASP A 1 102 ? 8.066  18.002  15.173  1.00 37.80  ?  325 ASP B O   1 
ATOM   779  C CB  . ASP A 1 102 ? 9.210  17.947  17.693  1.00 38.59  ?  325 ASP B CB  1 
ATOM   780  C CG  . ASP A 1 102 ? 10.274 18.954  17.298  1.00 42.72  ?  325 ASP B CG  1 
ATOM   781  O OD1 . ASP A 1 102 ? 11.094 18.645  16.407  1.00 42.43  ?  325 ASP B OD1 1 
ATOM   782  O OD2 . ASP A 1 102 ? 10.292 20.057  17.883  1.00 44.24  ?  325 ASP B OD2 1 
ATOM   783  N N   . PHE A 1 103 ? 9.229  16.237  14.416  1.00 37.12  ?  326 PHE B N   1 
ATOM   784  C CA  . PHE A 1 103 ? 8.816  16.436  13.035  1.00 41.10  ?  326 PHE B CA  1 
ATOM   785  C C   . PHE A 1 103 ? 8.736  15.086  12.338  1.00 44.35  ?  326 PHE B C   1 
ATOM   786  O O   . PHE A 1 103 ? 9.418  14.131  12.720  1.00 41.29  ?  326 PHE B O   1 
ATOM   787  C CB  . PHE A 1 103 ? 9.768  17.375  12.280  1.00 39.86  ?  326 PHE B CB  1 
ATOM   788  C CG  . PHE A 1 103 ? 11.206 16.938  12.299  1.00 42.74  ?  326 PHE B CG  1 
ATOM   789  C CD1 . PHE A 1 103 ? 11.692 16.054  11.348  1.00 46.42  ?  326 PHE B CD1 1 
ATOM   790  C CD2 . PHE A 1 103 ? 12.077 17.423  13.261  1.00 44.82  ?  326 PHE B CD2 1 
ATOM   791  C CE1 . PHE A 1 103 ? 13.016 15.653  11.364  1.00 46.40  ?  326 PHE B CE1 1 
ATOM   792  C CE2 . PHE A 1 103 ? 13.403 17.026  13.283  1.00 45.97  ?  326 PHE B CE2 1 
ATOM   793  C CZ  . PHE A 1 103 ? 13.872 16.140  12.333  1.00 44.44  ?  326 PHE B CZ  1 
ATOM   794  N N   . VAL A 1 104 ? 7.896  15.019  11.311  1.00 41.32  ?  327 VAL B N   1 
ATOM   795  C CA  . VAL A 1 104 ? 7.703  13.798  10.540  1.00 41.19  ?  327 VAL B CA  1 
ATOM   796  C C   . VAL A 1 104 ? 8.709  13.785  9.397   1.00 42.87  ?  327 VAL B C   1 
ATOM   797  O O   . VAL A 1 104 ? 8.737  14.701  8.569   1.00 43.45  ?  327 VAL B O   1 
ATOM   798  C CB  . VAL A 1 104 ? 6.265  13.694  10.010  1.00 43.50  ?  327 VAL B CB  1 
ATOM   799  C CG1 . VAL A 1 104 ? 6.175  12.641  8.914   1.00 39.66  ?  327 VAL B CG1 1 
ATOM   800  C CG2 . VAL A 1 104 ? 5.309  13.369  11.147  1.00 44.26  ?  327 VAL B CG2 1 
ATOM   801  N N   . GLY A 1 105 ? 9.535  12.748  9.352   1.00 42.29  ?  328 GLY B N   1 
ATOM   802  C CA  . GLY A 1 105 ? 10.519 12.631  8.293   1.00 37.69  ?  328 GLY B CA  1 
ATOM   803  C C   . GLY A 1 105 ? 11.395 11.423  8.522   1.00 40.57  ?  328 GLY B C   1 
ATOM   804  O O   . GLY A 1 105 ? 11.245 10.690  9.505   1.00 42.07  ?  328 GLY B O   1 
ATOM   805  N N   . LYS A 1 106 ? 12.320 11.220  7.588   1.00 42.92  ?  329 LYS B N   1 
ATOM   806  C CA  . LYS A 1 106 ? 13.262 10.110  7.645   1.00 42.79  ?  329 LYS B CA  1 
ATOM   807  C C   . LYS A 1 106 ? 14.609 10.645  8.112   1.00 38.34  ?  329 LYS B C   1 
ATOM   808  O O   . LYS A 1 106 ? 15.285 11.374  7.377   1.00 36.87  ?  329 LYS B O   1 
ATOM   809  C CB  . LYS A 1 106 ? 13.389 9.422   6.287   1.00 37.48  ?  329 LYS B CB  1 
ATOM   810  C CG  . LYS A 1 106 ? 12.088 8.880   5.718   1.00 43.58  ?  329 LYS B CG  1 
ATOM   811  C CD  . LYS A 1 106 ? 11.970 9.165   4.226   1.00 51.14  ?  329 LYS B CD  1 
ATOM   812  C CE  . LYS A 1 106 ? 10.779 8.436   3.622   1.00 58.57  ?  329 LYS B CE  1 
ATOM   813  N NZ  . LYS A 1 106 ? 10.793 8.470   2.132   1.00 54.75  ?  329 LYS B NZ  1 
ATOM   814  N N   . ILE A 1 107 ? 14.997 10.283  9.332   1.00 34.80  ?  330 ILE B N   1 
ATOM   815  C CA  . ILE A 1 107 ? 16.264 10.701  9.916   1.00 36.65  ?  330 ILE B CA  1 
ATOM   816  C C   . ILE A 1 107 ? 17.272 9.579   9.716   1.00 37.39  ?  330 ILE B C   1 
ATOM   817  O O   . ILE A 1 107 ? 17.045 8.445   10.155  1.00 40.29  ?  330 ILE B O   1 
ATOM   818  C CB  . ILE A 1 107 ? 16.109 11.039  11.407  1.00 36.33  ?  330 ILE B CB  1 
ATOM   819  C CG1 . ILE A 1 107 ? 15.181 12.242  11.591  1.00 37.53  ?  330 ILE B CG1 1 
ATOM   820  C CG2 . ILE A 1 107 ? 17.471 11.300  12.038  1.00 30.83  ?  330 ILE B CG2 1 
ATOM   821  C CD1 . ILE A 1 107 ? 14.783 12.491  13.031  1.00 38.92  ?  330 ILE B CD1 1 
ATOM   822  N N   . GLN A 1 108 ? 18.380 9.888   9.054   1.00 37.04  ?  331 GLN B N   1 
ATOM   823  C CA  . GLN A 1 108 ? 19.452 8.924   8.853   1.00 38.37  ?  331 GLN B CA  1 
ATOM   824  C C   . GLN A 1 108 ? 20.590 9.205   9.824   1.00 35.81  ?  331 GLN B C   1 
ATOM   825  O O   . GLN A 1 108 ? 20.960 10.360  10.052  1.00 35.47  ?  331 GLN B O   1 
ATOM   826  C CB  . GLN A 1 108 ? 19.973 8.961   7.416   1.00 31.66  ?  331 GLN B CB  1 
ATOM   827  C CG  . GLN A 1 108 ? 20.860 7.772   7.071   1.00 36.97  ?  331 GLN B CG  1 
ATOM   828  C CD  . GLN A 1 108 ? 21.029 7.570   5.579   1.00 45.64  ?  331 GLN B CD  1 
ATOM   829  O OE1 . GLN A 1 108 ? 21.988 8.057   4.982   1.00 46.45  ?  331 GLN B OE1 1 
ATOM   830  N NE2 . GLN A 1 108 ? 20.100 6.841   4.969   1.00 50.24  ?  331 GLN B NE2 1 
ATOM   831  N N   . GLY A 1 109 ? 21.133 8.147   10.392  1.00 35.16  ?  332 GLY B N   1 
ATOM   832  C CA  . GLY A 1 109 ? 22.232 8.261   11.329  1.00 39.12  ?  332 GLY B CA  1 
ATOM   833  C C   . GLY A 1 109 ? 23.005 6.969   11.384  1.00 39.38  ?  332 GLY B C   1 
ATOM   834  O O   . GLY A 1 109 ? 23.028 6.198   10.422  1.00 37.14  ?  332 GLY B O   1 
ATOM   835  N N   . VAL A 1 110 ? 23.647 6.726   12.523  1.00 37.31  ?  333 VAL B N   1 
ATOM   836  C CA  . VAL A 1 110 ? 24.453 5.530   12.730  1.00 32.89  ?  333 VAL B CA  1 
ATOM   837  C C   . VAL A 1 110 ? 23.995 4.853   14.013  1.00 39.37  ?  333 VAL B C   1 
ATOM   838  O O   . VAL A 1 110 ? 23.881 5.503   15.059  1.00 35.24  ?  333 VAL B O   1 
ATOM   839  C CB  . VAL A 1 110 ? 25.959 5.851   12.791  1.00 31.88  ?  333 VAL B CB  1 
ATOM   840  C CG1 . VAL A 1 110 ? 26.767 4.570   12.906  1.00 34.26  ?  333 VAL B CG1 1 
ATOM   841  C CG2 . VAL A 1 110 ? 26.383 6.639   11.562  1.00 37.77  ?  333 VAL B CG2 1 
ATOM   842  N N   . LEU A 1 111 ? 23.725 3.555   13.927  1.00 35.23  ?  334 LEU B N   1 
ATOM   843  C CA  . LEU A 1 111 ? 23.349 2.738   15.074  1.00 34.88  ?  334 LEU B CA  1 
ATOM   844  C C   . LEU A 1 111 ? 24.604 2.031   15.574  1.00 37.91  ?  334 LEU B C   1 
ATOM   845  O O   . LEU A 1 111 ? 25.181 1.205   14.859  1.00 42.18  ?  334 LEU B O   1 
ATOM   846  C CB  . LEU A 1 111 ? 22.263 1.738   14.689  1.00 34.86  ?  334 LEU B CB  1 
ATOM   847  C CG  . LEU A 1 111 ? 21.296 1.253   15.767  1.00 40.64  ?  334 LEU B CG  1 
ATOM   848  C CD1 . LEU A 1 111 ? 20.656 2.421   16.498  1.00 36.97  ?  334 LEU B CD1 1 
ATOM   849  C CD2 . LEU A 1 111 ? 20.232 0.365   15.142  1.00 41.06  ?  334 LEU B CD2 1 
ATOM   850  N N   . THR A 1 112 ? 25.033 2.361   16.789  1.00 36.25  ?  335 THR B N   1 
ATOM   851  C CA  . THR A 1 112 ? 26.245 1.802   17.367  1.00 36.51  ?  335 THR B CA  1 
ATOM   852  C C   . THR A 1 112 ? 25.904 0.940   18.576  1.00 37.80  ?  335 THR B C   1 
ATOM   853  O O   . THR A 1 112 ? 24.874 1.133   19.230  1.00 38.44  ?  335 THR B O   1 
ATOM   854  C CB  . THR A 1 112 ? 27.231 2.902   17.780  1.00 34.36  ?  335 THR B CB  1 
ATOM   855  O OG1 . THR A 1 112 ? 26.607 3.786   18.721  1.00 36.51  ?  335 THR B OG1 1 
ATOM   856  C CG2 . THR A 1 112 ? 27.685 3.699   16.559  1.00 37.10  ?  335 THR B CG2 1 
ATOM   857  N N   . GLN A 1 113 ? 26.787 -0.010  18.871  1.00 38.51  ?  336 GLN B N   1 
ATOM   858  C CA  . GLN A 1 113 ? 26.543 -0.979  19.929  1.00 40.23  ?  336 GLN B CA  1 
ATOM   859  C C   . GLN A 1 113 ? 27.874 -1.441  20.503  1.00 37.33  ?  336 GLN B C   1 
ATOM   860  O O   . GLN A 1 113 ? 28.871 -1.551  19.787  1.00 38.79  ?  336 GLN B O   1 
ATOM   861  C CB  . GLN A 1 113 ? 25.740 -2.175  19.405  1.00 35.30  ?  336 GLN B CB  1 
ATOM   862  C CG  . GLN A 1 113 ? 25.235 -3.123  20.478  1.00 38.29  ?  336 GLN B CG  1 
ATOM   863  C CD  . GLN A 1 113 ? 24.563 -4.347  19.890  1.00 40.30  ?  336 GLN B CD  1 
ATOM   864  O OE1 . GLN A 1 113 ? 25.230 -5.296  19.479  1.00 39.58  ?  336 GLN B OE1 1 
ATOM   865  N NE2 . GLN A 1 113 ? 23.235 -4.329  19.840  1.00 35.62  ?  336 GLN B NE2 1 
ATOM   866  N N   . THR A 1 114 ? 27.875 -1.709  21.807  1.00 37.85  ?  337 THR B N   1 
ATOM   867  C CA  . THR A 1 114 ? 29.049 -2.209  22.509  1.00 36.86  ?  337 THR B CA  1 
ATOM   868  C C   . THR A 1 114 ? 28.660 -3.455  23.290  1.00 39.32  ?  337 THR B C   1 
ATOM   869  O O   . THR A 1 114 ? 27.648 -3.454  23.998  1.00 37.60  ?  337 THR B O   1 
ATOM   870  C CB  . THR A 1 114 ? 29.628 -1.145  23.454  1.00 38.63  ?  337 THR B CB  1 
ATOM   871  O OG1 . THR A 1 114 ? 30.224 -0.096  22.681  1.00 46.33  ?  337 THR B OG1 1 
ATOM   872  C CG2 . THR A 1 114 ? 30.682 -1.751  24.372  1.00 37.16  ?  337 THR B CG2 1 
ATOM   873  N N   . THR A 1 115 ? 29.451 -4.516  23.146  1.00 39.43  ?  338 THR B N   1 
ATOM   874  C CA  . THR A 1 115 ? 29.250 -5.742  23.909  1.00 43.25  ?  338 THR B CA  1 
ATOM   875  C C   . THR A 1 115 ? 29.963 -5.598  25.249  1.00 43.31  ?  338 THR B C   1 
ATOM   876  O O   . THR A 1 115 ? 31.180 -5.383  25.291  1.00 48.34  ?  338 THR B O   1 
ATOM   877  C CB  . THR A 1 115 ? 29.773 -6.955  23.140  1.00 44.00  ?  338 THR B CB  1 
ATOM   878  O OG1 . THR A 1 115 ? 28.869 -7.274  22.076  1.00 42.58  ?  338 THR B OG1 1 
ATOM   879  C CG2 . THR A 1 115 ? 29.891 -8.164  24.062  1.00 43.75  ?  338 THR B CG2 1 
ATOM   880  N N   . ARG A 1 116 ? 29.205 -5.715  26.341  1.00 39.26  ?  339 ARG B N   1 
ATOM   881  C CA  . ARG A 1 116 ? 29.732 -5.371  27.659  1.00 47.96  ?  339 ARG B CA  1 
ATOM   882  C C   . ARG A 1 116 ? 30.856 -6.304  28.098  1.00 51.17  ?  339 ARG B C   1 
ATOM   883  O O   . ARG A 1 116 ? 31.783 -5.866  28.791  1.00 54.35  ?  339 ARG B O   1 
ATOM   884  C CB  . ARG A 1 116 ? 28.599 -5.385  28.688  1.00 50.68  ?  339 ARG B CB  1 
ATOM   885  C CG  . ARG A 1 116 ? 29.029 -5.058  30.109  1.00 56.43  ?  339 ARG B CG  1 
ATOM   886  C CD  . ARG A 1 116 ? 27.834 -5.025  31.051  1.00 67.34  ?  339 ARG B CD  1 
ATOM   887  N NE  . ARG A 1 116 ? 27.351 -3.666  31.271  1.00 79.89  ?  339 ARG B NE  1 
ATOM   888  C CZ  . ARG A 1 116 ? 26.197 -3.198  30.815  1.00 85.67  ?  339 ARG B CZ  1 
ATOM   889  N NH1 . ARG A 1 116 ? 25.374 -3.955  30.107  1.00 84.90  ?  339 ARG B NH1 1 
ATOM   890  N NH2 . ARG A 1 116 ? 25.859 -1.938  31.076  1.00 87.28  ?  339 ARG B NH2 1 
ATOM   891  N N   . THR A 1 117 ? 30.806 -7.576  27.698  1.00 50.82  ?  340 THR B N   1 
ATOM   892  C CA  . THR A 1 117 ? 31.733 -8.565  28.242  1.00 51.67  ?  340 THR B CA  1 
ATOM   893  C C   . THR A 1 117 ? 33.164 -8.323  27.768  1.00 53.16  ?  340 THR B C   1 
ATOM   894  O O   . THR A 1 117 ? 34.103 -8.344  28.571  1.00 56.83  ?  340 THR B O   1 
ATOM   895  C CB  . THR A 1 117 ? 31.274 -9.976  27.875  1.00 57.14  ?  340 THR B CB  1 
ATOM   896  O OG1 . THR A 1 117 ? 31.800 -10.336 26.591  1.00 62.55  ?  340 THR B OG1 1 
ATOM   897  C CG2 . THR A 1 117 ? 29.752 -10.046 27.834  1.00 57.02  ?  340 THR B CG2 1 
ATOM   898  N N   . ASP A 1 118 ? 33.356 -8.095  26.467  1.00 55.90  ?  341 ASP B N   1 
ATOM   899  C CA  . ASP A 1 118 ? 34.696 -7.943  25.912  1.00 58.54  ?  341 ASP B CA  1 
ATOM   900  C C   . ASP A 1 118 ? 34.959 -6.578  25.288  1.00 53.21  ?  341 ASP B C   1 
ATOM   901  O O   . ASP A 1 118 ? 36.061 -6.353  24.773  1.00 54.38  ?  341 ASP B O   1 
ATOM   902  C CB  . ASP A 1 118 ? 34.975 -9.044  24.876  1.00 52.29  ?  341 ASP B CB  1 
ATOM   903  C CG  . ASP A 1 118 ? 33.910 -9.123  23.793  1.00 57.01  ?  341 ASP B CG  1 
ATOM   904  O OD1 . ASP A 1 118 ? 33.113 -8.174  23.653  1.00 58.23  ?  341 ASP B OD1 1 
ATOM   905  O OD2 . ASP A 1 118 ? 33.871 -10.150 23.080  1.00 54.14  ?  341 ASP B OD2 1 
ATOM   906  N N   . GLY A 1 119 ? 33.992 -5.665  25.315  1.00 51.47  ?  342 GLY B N   1 
ATOM   907  C CA  . GLY A 1 119 ? 34.214 -4.348  24.753  1.00 44.51  ?  342 GLY B CA  1 
ATOM   908  C C   . GLY A 1 119 ? 34.224 -4.293  23.244  1.00 50.91  ?  342 GLY B C   1 
ATOM   909  O O   . GLY A 1 119 ? 34.690 -3.301  22.675  1.00 50.36  ?  342 GLY B O   1 
ATOM   910  N N   . SER A 1 120 ? 33.731 -5.332  22.574  1.00 49.15  ?  343 SER B N   1 
ATOM   911  C CA  . SER A 1 120 ? 33.639 -5.306  21.122  1.00 48.52  ?  343 SER B CA  1 
ATOM   912  C C   . SER A 1 120 ? 32.536 -4.350  20.687  1.00 40.72  ?  343 SER B C   1 
ATOM   913  O O   . SER A 1 120 ? 31.471 -4.280  21.308  1.00 40.51  ?  343 SER B O   1 
ATOM   914  C CB  . SER A 1 120 ? 33.369 -6.706  20.576  1.00 46.02  ?  343 SER B CB  1 
ATOM   915  O OG  . SER A 1 120 ? 32.062 -7.138  20.907  1.00 44.81  ?  343 SER B OG  1 
ATOM   916  N N   . THR A 1 121 ? 32.794 -3.608  19.614  1.00 40.06  ?  344 THR B N   1 
ATOM   917  C CA  . THR A 1 121 ? 31.879 -2.574  19.157  1.00 43.09  ?  344 THR B CA  1 
ATOM   918  C C   . THR A 1 121 ? 31.540 -2.788  17.688  1.00 46.25  ?  344 THR B C   1 
ATOM   919  O O   . THR A 1 121 ? 32.266 -3.456  16.948  1.00 43.18  ?  344 THR B O   1 
ATOM   920  C CB  . THR A 1 121 ? 32.468 -1.171  19.356  1.00 38.84  ?  344 THR B CB  1 
ATOM   921  O OG1 . THR A 1 121 ? 33.667 -1.034  18.583  1.00 38.76  ?  344 THR B OG1 1 
ATOM   922  C CG2 . THR A 1 121 ? 32.790 -0.930  20.826  1.00 39.46  ?  344 THR B CG2 1 
ATOM   923  N N   . ARG A 1 122 ? 30.416 -2.206  17.280  1.00 44.32  ?  345 ARG B N   1 
ATOM   924  C CA  . ARG A 1 122 ? 29.978 -2.259  15.894  1.00 41.35  ?  345 ARG B CA  1 
ATOM   925  C C   . ARG A 1 122 ? 29.066 -1.070  15.630  1.00 43.89  ?  345 ARG B C   1 
ATOM   926  O O   . ARG A 1 122 ? 28.395 -0.571  16.537  1.00 41.56  ?  345 ARG B O   1 
ATOM   927  C CB  . ARG A 1 122 ? 29.258 -3.575  15.576  1.00 40.17  ?  345 ARG B CB  1 
ATOM   928  C CG  . ARG A 1 122 ? 27.910 -3.734  16.262  1.00 43.31  ?  345 ARG B CG  1 
ATOM   929  C CD  . ARG A 1 122 ? 27.661 -5.180  16.650  1.00 43.83  ?  345 ARG B CD  1 
ATOM   930  N NE  . ARG A 1 122 ? 28.847 -5.795  17.233  1.00 43.21  ?  345 ARG B NE  1 
ATOM   931  C CZ  . ARG A 1 122 ? 29.024 -5.996  18.531  1.00 44.85  ?  345 ARG B CZ  1 
ATOM   932  N NH1 . ARG A 1 122 ? 28.102 -5.653  19.415  1.00 42.14  ?  345 ARG B NH1 1 
ATOM   933  N NH2 . ARG A 1 122 ? 30.156 -6.553  18.953  1.00 46.39  ?  345 ARG B NH2 1 
ATOM   934  N N   . GLY A 1 123 ? 29.058 -0.621  14.378  1.00 35.76  ?  346 GLY B N   1 
ATOM   935  C CA  . GLY A 1 123 ? 28.217 0.488   13.972  1.00 41.88  ?  346 GLY B CA  1 
ATOM   936  C C   . GLY A 1 123 ? 27.736 0.344   12.544  1.00 43.43  ?  346 GLY B C   1 
ATOM   937  O O   . GLY A 1 123 ? 28.506 -0.048  11.662  1.00 42.81  ?  346 GLY B O   1 
ATOM   938  N N   . HIS A 1 124 ? 26.466 0.658   12.298  1.00 41.71  ?  347 HIS B N   1 
ATOM   939  C CA  . HIS A 1 124 ? 25.875 0.493   10.979  1.00 39.59  ?  347 HIS B CA  1 
ATOM   940  C C   . HIS A 1 124 ? 24.987 1.683   10.653  1.00 42.89  ?  347 HIS B C   1 
ATOM   941  O O   . HIS A 1 124 ? 24.445 2.339   11.546  1.00 41.63  ?  347 HIS B O   1 
ATOM   942  C CB  . HIS A 1 124 ? 25.055 -0.800  10.889  1.00 45.94  ?  347 HIS B CB  1 
ATOM   943  C CG  . HIS A 1 124 ? 25.872 -2.045  11.022  1.00 47.26  ?  347 HIS B CG  1 
ATOM   944  N ND1 . HIS A 1 124 ? 26.534 -2.619  9.959   1.00 52.82  ?  347 HIS B ND1 1 
ATOM   945  C CD2 . HIS A 1 124 ? 26.136 -2.827  12.096  1.00 43.30  ?  347 HIS B CD2 1 
ATOM   946  C CE1 . HIS A 1 124 ? 27.170 -3.700  10.370  1.00 53.92  ?  347 HIS B CE1 1 
ATOM   947  N NE2 . HIS A 1 124 ? 26.945 -3.849  11.663  1.00 46.98  ?  347 HIS B NE2 1 
ATOM   948  N N   . LYS A 1 125 ? 24.850 1.954   9.357   1.00 39.48  ?  348 LYS B N   1 
ATOM   949  C CA  . LYS A 1 125 ? 23.906 2.960   8.895   1.00 39.81  ?  348 LYS B CA  1 
ATOM   950  C C   . LYS A 1 125 ? 22.491 2.565   9.294   1.00 36.44  ?  348 LYS B C   1 
ATOM   951  O O   . LYS A 1 125 ? 22.106 1.397   9.206   1.00 39.73  ?  348 LYS B O   1 
ATOM   952  C CB  . LYS A 1 125 ? 24.005 3.119   7.377   1.00 36.15  ?  348 LYS B CB  1 
ATOM   953  C CG  . LYS A 1 125 ? 23.239 4.304   6.816   1.00 43.08  ?  348 LYS B CG  1 
ATOM   954  C CD  . LYS A 1 125 ? 22.702 3.998   5.423   1.00 46.89  ?  348 LYS B CD  1 
ATOM   955  C CE  . LYS A 1 125 ? 23.625 4.540   4.342   1.00 51.95  ?  348 LYS B CE  1 
ATOM   956  N NZ  . LYS A 1 125 ? 22.869 5.202   3.240   1.00 56.42  ?  348 LYS B NZ  1 
ATOM   957  N N   . ALA A 1 126 ? 21.714 3.546   9.742   1.00 33.90  ?  349 ALA B N   1 
ATOM   958  C CA  . ALA A 1 126 ? 20.366 3.278   10.215  1.00 34.71  ?  349 ALA B CA  1 
ATOM   959  C C   . ALA A 1 126 ? 19.492 4.489   9.942   1.00 34.55  ?  349 ALA B C   1 
ATOM   960  O O   . ALA A 1 126 ? 19.962 5.629   9.954   1.00 36.11  ?  349 ALA B O   1 
ATOM   961  C CB  . ALA A 1 126 ? 20.349 2.935   11.711  1.00 32.85  ?  349 ALA B CB  1 
ATOM   962  N N   . THR A 1 127 ? 18.211 4.231   9.697   1.00 32.62  ?  350 THR B N   1 
ATOM   963  C CA  . THR A 1 127 ? 17.247 5.282   9.408   1.00 35.94  ?  350 THR B CA  1 
ATOM   964  C C   . THR A 1 127 ? 15.978 5.023   10.203  1.00 39.04  ?  350 THR B C   1 
ATOM   965  O O   . THR A 1 127 ? 15.479 3.895   10.229  1.00 38.35  ?  350 THR B O   1 
ATOM   966  C CB  . THR A 1 127 ? 16.934 5.350   7.907   1.00 38.43  ?  350 THR B CB  1 
ATOM   967  O OG1 . THR A 1 127 ? 18.160 5.400   7.165   1.00 36.94  ?  350 THR B OG1 1 
ATOM   968  C CG2 . THR A 1 127 ? 16.104 6.585   7.585   1.00 32.40  ?  350 THR B CG2 1 
ATOM   969  N N   . VAL A 1 128 ? 15.468 6.062   10.861  1.00 39.52  ?  351 VAL B N   1 
ATOM   970  C CA  . VAL A 1 128 ? 14.218 5.990   11.608  1.00 39.90  ?  351 VAL B CA  1 
ATOM   971  C C   . VAL A 1 128 ? 13.184 6.840   10.885  1.00 40.59  ?  351 VAL B C   1 
ATOM   972  O O   . VAL A 1 128 ? 13.439 8.010   10.569  1.00 42.39  ?  351 VAL B O   1 
ATOM   973  C CB  . VAL A 1 128 ? 14.400 6.442   13.069  1.00 40.90  ?  351 VAL B CB  1 
ATOM   974  C CG1 . VAL A 1 128 ? 15.209 7.732   13.148  1.00 40.31  ?  351 VAL B CG1 1 
ATOM   975  C CG2 . VAL A 1 128 ? 13.051 6.599   13.756  1.00 40.11  ?  351 VAL B CG2 1 
ATOM   976  N N   . TYR A 1 129 ? 12.027 6.246   10.603  1.00 36.99  ?  352 TYR B N   1 
ATOM   977  C CA  . TYR A 1 129 ? 10.939 6.916   9.894   1.00 43.33  ?  352 TYR B CA  1 
ATOM   978  C C   . TYR A 1 129 ? 9.948  7.389   10.954  1.00 43.60  ?  352 TYR B C   1 
ATOM   979  O O   . TYR A 1 129 ? 9.066  6.643   11.381  1.00 43.00  ?  352 TYR B O   1 
ATOM   980  C CB  . TYR A 1 129 ? 10.283 5.985   8.874   1.00 39.23  ?  352 TYR B CB  1 
ATOM   981  C CG  . TYR A 1 129 ? 11.215 5.422   7.813   1.00 44.29  ?  352 TYR B CG  1 
ATOM   982  C CD1 . TYR A 1 129 ? 12.229 4.528   8.142   1.00 45.47  ?  352 TYR B CD1 1 
ATOM   983  C CD2 . TYR A 1 129 ? 11.060 5.766   6.475   1.00 54.21  ?  352 TYR B CD2 1 
ATOM   984  C CE1 . TYR A 1 129 ? 13.074 4.011   7.174   1.00 48.42  ?  352 TYR B CE1 1 
ATOM   985  C CE2 . TYR A 1 129 ? 11.903 5.255   5.499   1.00 47.12  ?  352 TYR B CE2 1 
ATOM   986  C CZ  . TYR A 1 129 ? 12.906 4.377   5.856   1.00 52.04  ?  352 TYR B CZ  1 
ATOM   987  O OH  . TYR A 1 129 ? 13.745 3.861   4.894   1.00 52.91  ?  352 TYR B OH  1 
ATOM   988  N N   . THR A 1 130 ? 10.099 8.645   11.384  1.00 40.79  ?  353 THR B N   1 
ATOM   989  C CA  . THR A 1 130 ? 9.282  9.152   12.483  1.00 43.78  ?  353 THR B CA  1 
ATOM   990  C C   . THR A 1 130 ? 7.814  9.288   12.101  1.00 44.65  ?  353 THR B C   1 
ATOM   991  O O   . THR A 1 130 ? 6.967  9.446   12.988  1.00 38.55  ?  353 THR B O   1 
ATOM   992  C CB  . THR A 1 130 ? 9.814  10.501  12.976  1.00 44.46  ?  353 THR B CB  1 
ATOM   993  O OG1 . THR A 1 130 ? 9.547  11.517  12.002  1.00 40.05  ?  353 THR B OG1 1 
ATOM   994  C CG2 . THR A 1 130 ? 11.313 10.424  13.236  1.00 39.53  ?  353 THR B CG2 1 
ATOM   995  N N   . GLY A 1 131 ? 7.494  9.236   10.811  1.00 37.62  ?  354 GLY B N   1 
ATOM   996  C CA  . GLY A 1 131 ? 6.122  9.251   10.357  1.00 34.48  ?  354 GLY B CA  1 
ATOM   997  C C   . GLY A 1 131 ? 5.500  7.886   10.178  1.00 44.37  ?  354 GLY B C   1 
ATOM   998  O O   . GLY A 1 131 ? 4.310  7.792   9.858   1.00 46.00  ?  354 GLY B O   1 
ATOM   999  N N   . SER A 1 132 ? 6.269  6.822   10.380  1.00 47.26  ?  355 SER B N   1 
ATOM   1000 C CA  . SER A 1 132 ? 5.755  5.474   10.193  1.00 50.56  ?  355 SER B CA  1 
ATOM   1001 C C   . SER A 1 132 ? 4.813  5.091   11.329  1.00 56.76  ?  355 SER B C   1 
ATOM   1002 O O   . SER A 1 132 ? 4.909  5.601   12.449  1.00 49.52  ?  355 SER B O   1 
ATOM   1003 C CB  . SER A 1 132 ? 6.905  4.470   10.113  1.00 50.88  ?  355 SER B CB  1 
ATOM   1004 O OG  . SER A 1 132 ? 7.344  4.101   11.409  1.00 59.06  ?  355 SER B OG  1 
ATOM   1005 N N   . ALA A 1 133 ? 3.890  4.174   11.023  1.00 55.77  ?  356 ALA B N   1 
ATOM   1006 C CA  . ALA A 1 133 ? 2.956  3.686   12.027  1.00 62.81  ?  356 ALA B CA  1 
ATOM   1007 C C   . ALA A 1 133 ? 3.666  2.965   13.163  1.00 61.84  ?  356 ALA B C   1 
ATOM   1008 O O   . ALA A 1 133 ? 3.087  2.806   14.244  1.00 58.13  ?  356 ALA B O   1 
ATOM   1009 C CB  . ALA A 1 133 ? 1.932  2.752   11.378  1.00 71.02  ?  356 ALA B CB  1 
ATOM   1010 N N   . ASP A 1 134 ? 4.907  2.534   12.940  1.00 63.03  ?  357 ASP B N   1 
ATOM   1011 C CA  . ASP A 1 134 ? 5.691  1.809   13.929  1.00 65.43  ?  357 ASP B CA  1 
ATOM   1012 C C   . ASP A 1 134 ? 6.450  2.726   14.879  1.00 60.14  ?  357 ASP B C   1 
ATOM   1013 O O   . ASP A 1 134 ? 6.992  2.242   15.879  1.00 57.76  ?  357 ASP B O   1 
ATOM   1014 C CB  . ASP A 1 134 ? 6.679  0.867   13.222  1.00 70.88  ?  357 ASP B CB  1 
ATOM   1015 C CG  . ASP A 1 134 ? 6.078  -0.497  12.928  1.00 80.31  ?  357 ASP B CG  1 
ATOM   1016 O OD1 . ASP A 1 134 ? 5.179  -0.922  13.681  1.00 82.36  ?  357 ASP B OD1 1 
ATOM   1017 O OD2 . ASP A 1 134 ? 6.487  -1.139  11.936  1.00 85.90  ?  357 ASP B OD2 1 
ATOM   1018 N N   . PHE A 1 135 ? 6.506  4.025   14.594  1.00 56.66  ?  358 PHE B N   1 
ATOM   1019 C CA  . PHE A 1 135 ? 7.204  4.983   15.448  1.00 52.70  ?  358 PHE B CA  1 
ATOM   1020 C C   . PHE A 1 135 ? 6.365  5.258   16.692  1.00 47.70  ?  358 PHE B C   1 
ATOM   1021 O O   . PHE A 1 135 ? 5.340  5.942   16.620  1.00 49.56  ?  358 PHE B O   1 
ATOM   1022 C CB  . PHE A 1 135 ? 7.468  6.265   14.663  1.00 45.32  ?  358 PHE B CB  1 
ATOM   1023 C CG  . PHE A 1 135 ? 8.302  7.282   15.395  1.00 43.80  ?  358 PHE B CG  1 
ATOM   1024 C CD1 . PHE A 1 135 ? 9.665  7.097   15.563  1.00 43.61  ?  358 PHE B CD1 1 
ATOM   1025 C CD2 . PHE A 1 135 ? 7.724  8.440   15.890  1.00 42.37  ?  358 PHE B CD2 1 
ATOM   1026 C CE1 . PHE A 1 135 ? 10.432 8.040   16.227  1.00 43.32  ?  358 PHE B CE1 1 
ATOM   1027 C CE2 . PHE A 1 135 ? 8.483  9.388   16.552  1.00 42.56  ?  358 PHE B CE2 1 
ATOM   1028 C CZ  . PHE A 1 135 ? 9.838  9.186   16.722  1.00 44.62  ?  358 PHE B CZ  1 
ATOM   1029 N N   . ALA A 1 136 ? 6.791  4.724   17.836  1.00 49.04  ?  359 ALA B N   1 
ATOM   1030 C CA  . ALA A 1 136 ? 6.057  4.876   19.094  1.00 50.44  ?  359 ALA B CA  1 
ATOM   1031 C C   . ALA A 1 136 ? 7.035  5.078   20.243  1.00 47.55  ?  359 ALA B C   1 
ATOM   1032 O O   . ALA A 1 136 ? 7.181  4.216   21.120  1.00 46.92  ?  359 ALA B O   1 
ATOM   1033 C CB  . ALA A 1 136 ? 5.157  3.664   19.345  1.00 49.79  ?  359 ALA B CB  1 
ATOM   1034 N N   . PRO A 1 137 ? 7.722  6.224   20.278  1.00 43.45  ?  360 PRO B N   1 
ATOM   1035 C CA  . PRO A 1 137 ? 8.671  6.461   21.376  1.00 43.48  ?  360 PRO B CA  1 
ATOM   1036 C C   . PRO A 1 137 ? 8.002  6.611   22.732  1.00 47.39  ?  360 PRO B C   1 
ATOM   1037 O O   . PRO A 1 137 ? 8.616  6.262   23.747  1.00 46.51  ?  360 PRO B O   1 
ATOM   1038 C CB  . PRO A 1 137 ? 9.383  7.753   20.954  1.00 42.44  ?  360 PRO B CB  1 
ATOM   1039 C CG  . PRO A 1 137 ? 8.413  8.433   20.050  1.00 47.93  ?  360 PRO B CG  1 
ATOM   1040 C CD  . PRO A 1 137 ? 7.722  7.331   19.306  1.00 45.30  ?  360 PRO B CD  1 
ATOM   1041 N N   . LYS A 1 138 ? 6.766  7.118   22.783  1.00 47.66  ?  361 LYS B N   1 
ATOM   1042 C CA  . LYS A 1 138 ? 6.083  7.263   24.065  1.00 46.55  ?  361 LYS B CA  1 
ATOM   1043 C C   . LYS A 1 138 ? 5.862  5.909   24.728  1.00 49.96  ?  361 LYS B C   1 
ATOM   1044 O O   . LYS A 1 138 ? 5.944  5.788   25.956  1.00 49.17  ?  361 LYS B O   1 
ATOM   1045 C CB  . LYS A 1 138 ? 4.753  7.996   23.874  1.00 44.84  ?  361 LYS B CB  1 
ATOM   1046 C CG  . LYS A 1 138 ? 3.844  7.982   25.095  1.00 50.10  ?  361 LYS B CG  1 
ATOM   1047 C CD  . LYS A 1 138 ? 4.047  9.216   25.961  1.00 49.73  ?  361 LYS B CD  1 
ATOM   1048 C CE  . LYS A 1 138 ? 4.126  8.854   27.434  1.00 52.47  ?  361 LYS B CE  1 
ATOM   1049 N NZ  . LYS A 1 138 ? 4.000  10.056  28.302  1.00 51.23  ?  361 LYS B NZ  1 
ATOM   1050 N N   . LEU A 1 139 ? 5.590  4.875   23.931  1.00 47.21  ?  362 LEU B N   1 
ATOM   1051 C CA  . LEU A 1 139 ? 5.480  3.519   24.449  1.00 47.81  ?  362 LEU B CA  1 
ATOM   1052 C C   . LEU A 1 139 ? 6.835  2.852   24.650  1.00 47.48  ?  362 LEU B C   1 
ATOM   1053 O O   . LEU A 1 139 ? 6.890  1.768   25.241  1.00 47.28  ?  362 LEU B O   1 
ATOM   1054 C CB  . LEU A 1 139 ? 4.624  2.661   23.514  1.00 49.44  ?  362 LEU B CB  1 
ATOM   1055 C CG  . LEU A 1 139 ? 3.251  3.227   23.146  1.00 52.68  ?  362 LEU B CG  1 
ATOM   1056 C CD1 . LEU A 1 139 ? 2.504  2.273   22.225  1.00 47.92  ?  362 LEU B CD1 1 
ATOM   1057 C CD2 . LEU A 1 139 ? 2.439  3.519   24.399  1.00 46.59  ?  362 LEU B CD2 1 
ATOM   1058 N N   . GLY A 1 140 ? 7.916  3.464   24.175  1.00 44.95  ?  363 GLY B N   1 
ATOM   1059 C CA  . GLY A 1 140 ? 9.244  2.921   24.372  1.00 42.37  ?  363 GLY B CA  1 
ATOM   1060 C C   . GLY A 1 140 ? 9.768  2.054   23.251  1.00 47.40  ?  363 GLY B C   1 
ATOM   1061 O O   . GLY A 1 140 ? 10.679 1.252   23.489  1.00 42.19  ?  363 GLY B O   1 
ATOM   1062 N N   . ARG A 1 141 ? 9.234  2.190   22.037  1.00 46.53  ?  364 ARG B N   1 
ATOM   1063 C CA  . ARG A 1 141 ? 9.619  1.350   20.910  1.00 49.30  ?  364 ARG B CA  1 
ATOM   1064 C C   . ARG A 1 141 ? 9.875  2.215   19.685  1.00 46.34  ?  364 ARG B C   1 
ATOM   1065 O O   . ARG A 1 141 ? 9.045  3.057   19.331  1.00 40.22  ?  364 ARG B O   1 
ATOM   1066 C CB  . ARG A 1 141 ? 8.537  0.313   20.596  1.00 48.16  ?  364 ARG B CB  1 
ATOM   1067 C CG  . ARG A 1 141 ? 8.583  -0.927  21.474  1.00 56.69  ?  364 ARG B CG  1 
ATOM   1068 C CD  . ARG A 1 141 ? 7.677  -2.019  20.919  1.00 61.08  ?  364 ARG B CD  1 
ATOM   1069 N NE  . ARG A 1 141 ? 6.488  -1.473  20.272  1.00 57.84  ?  364 ARG B NE  1 
ATOM   1070 C CZ  . ARG A 1 141 ? 5.397  -1.079  20.915  1.00 61.55  ?  364 ARG B CZ  1 
ATOM   1071 N NH1 . ARG A 1 141 ? 5.304  -1.158  22.233  1.00 60.72  ?  364 ARG B NH1 1 
ATOM   1072 N NH2 . ARG A 1 141 ? 4.372  -0.595  20.217  1.00 55.95  ?  364 ARG B NH2 1 
ATOM   1073 N N   . VAL A 1 142 ? 11.017 1.992   19.037  1.00 48.12  ?  365 VAL B N   1 
ATOM   1074 C CA  . VAL A 1 142 ? 11.413 2.710   17.831  1.00 45.78  ?  365 VAL B CA  1 
ATOM   1075 C C   . VAL A 1 142 ? 12.169 1.740   16.932  1.00 51.15  ?  365 VAL B C   1 
ATOM   1076 O O   . VAL A 1 142 ? 12.990 0.950   17.410  1.00 50.34  ?  365 VAL B O   1 
ATOM   1077 C CB  . VAL A 1 142 ? 12.272 3.952   18.165  1.00 44.58  ?  365 VAL B CB  1 
ATOM   1078 C CG1 . VAL A 1 142 ? 13.236 4.276   17.036  1.00 40.71  ?  365 VAL B CG1 1 
ATOM   1079 C CG2 . VAL A 1 142 ? 11.384 5.148   18.473  1.00 45.36  ?  365 VAL B CG2 1 
ATOM   1080 N N   . GLN A 1 143 ? 11.889 1.795   15.631  1.00 48.09  ?  366 GLN B N   1 
ATOM   1081 C CA  . GLN A 1 143 ? 12.448 0.861   14.665  1.00 47.63  ?  366 GLN B CA  1 
ATOM   1082 C C   . GLN A 1 143 ? 13.471 1.566   13.784  1.00 45.49  ?  366 GLN B C   1 
ATOM   1083 O O   . GLN A 1 143 ? 13.308 2.742   13.445  1.00 41.56  ?  366 GLN B O   1 
ATOM   1084 C CB  . GLN A 1 143 ? 11.344 0.254   13.796  1.00 52.97  ?  366 GLN B CB  1 
ATOM   1085 C CG  . GLN A 1 143 ? 10.462 -0.746  14.514  1.00 58.42  ?  366 GLN B CG  1 
ATOM   1086 C CD  . GLN A 1 143 ? 9.471  -0.063  15.429  1.00 67.99  ?  366 GLN B CD  1 
ATOM   1087 O OE1 . GLN A 1 143 ? 9.047  -0.633  16.436  1.00 71.90  ?  366 GLN B OE1 1 
ATOM   1088 N NE2 . GLN A 1 143 ? 9.149  1.189   15.123  1.00 68.24  ?  366 GLN B NE2 1 
ATOM   1089 N N   . PHE A 1 144 ? 14.516 0.834   13.406  1.00 42.40  ?  367 PHE B N   1 
ATOM   1090 C CA  . PHE A 1 144 ? 15.615 1.380   12.623  1.00 40.14  ?  367 PHE B CA  1 
ATOM   1091 C C   . PHE A 1 144 ? 15.851 0.494   11.410  1.00 45.79  ?  367 PHE B C   1 
ATOM   1092 O O   . PHE A 1 144 ? 16.140 -0.699  11.558  1.00 38.73  ?  367 PHE B O   1 
ATOM   1093 C CB  . PHE A 1 144 ? 16.892 1.482   13.463  1.00 37.14  ?  367 PHE B CB  1 
ATOM   1094 C CG  . PHE A 1 144 ? 16.869 2.598   14.463  1.00 43.08  ?  367 PHE B CG  1 
ATOM   1095 C CD1 . PHE A 1 144 ? 16.929 3.916   14.050  1.00 42.06  ?  367 PHE B CD1 1 
ATOM   1096 C CD2 . PHE A 1 144 ? 16.785 2.326   15.819  1.00 46.70  ?  367 PHE B CD2 1 
ATOM   1097 C CE1 . PHE A 1 144 ? 16.906 4.945   14.971  1.00 42.90  ?  367 PHE B CE1 1 
ATOM   1098 C CE2 . PHE A 1 144 ? 16.762 3.352   16.744  1.00 44.33  ?  367 PHE B CE2 1 
ATOM   1099 C CZ  . PHE A 1 144 ? 16.821 4.663   16.319  1.00 42.15  ?  367 PHE B CZ  1 
ATOM   1100 N N   . GLU A 1 145 ? 15.718 1.072   10.218  1.00 45.10  ?  368 GLU B N   1 
ATOM   1101 C CA  . GLU A 1 145 ? 16.068 0.382   8.981   1.00 42.32  ?  368 GLU B CA  1 
ATOM   1102 C C   . GLU A 1 145 ? 17.581 0.439   8.816   1.00 43.76  ?  368 GLU B C   1 
ATOM   1103 O O   . GLU A 1 145 ? 18.150 1.517   8.616   1.00 47.45  ?  368 GLU B O   1 
ATOM   1104 C CB  . GLU A 1 145 ? 15.359 1.020   7.791   1.00 47.91  ?  368 GLU B CB  1 
ATOM   1105 C CG  . GLU A 1 145 ? 15.164 0.089   6.606   1.00 55.33  ?  368 GLU B CG  1 
ATOM   1106 C CD  . GLU A 1 145 ? 14.106 -0.967  6.861   1.00 68.25  ?  368 GLU B CD  1 
ATOM   1107 O OE1 . GLU A 1 145 ? 12.905 -0.626  6.825   1.00 70.36  ?  368 GLU B OE1 1 
ATOM   1108 O OE2 . GLU A 1 145 ? 14.475 -2.138  7.098   1.00 60.04  ?  368 GLU B OE2 1 
ATOM   1109 N N   . THR A 1 146 ? 18.238 -0.712  8.904   1.00 43.46  ?  369 THR B N   1 
ATOM   1110 C CA  . THR A 1 146 ? 19.689 -0.788  8.846   1.00 44.12  ?  369 THR B CA  1 
ATOM   1111 C C   . THR A 1 146 ? 20.130 -1.504  7.573   1.00 46.04  ?  369 THR B C   1 
ATOM   1112 O O   . THR A 1 146 ? 19.315 -1.925  6.746   1.00 50.58  ?  369 THR B O   1 
ATOM   1113 C CB  . THR A 1 146 ? 20.242 -1.490  10.089  1.00 44.92  ?  369 THR B CB  1 
ATOM   1114 O OG1 . THR A 1 146 ? 20.008 -2.900  9.985   1.00 46.88  ?  369 THR B OG1 1 
ATOM   1115 C CG2 . THR A 1 146 ? 19.567 -0.957  11.346  1.00 40.52  ?  369 THR B CG2 1 
ATOM   1116 N N   . ASP A 1 147 ? 21.447 -1.636  7.420   1.00 44.89  ?  370 ASP B N   1 
ATOM   1117 C CA  . ASP A 1 147 ? 22.044 -2.342  6.294   1.00 52.26  ?  370 ASP B CA  1 
ATOM   1118 C C   . ASP A 1 147 ? 22.602 -3.706  6.689   1.00 51.50  ?  370 ASP B C   1 
ATOM   1119 O O   . ASP A 1 147 ? 23.357 -4.303  5.915   1.00 48.08  ?  370 ASP B O   1 
ATOM   1120 C CB  . ASP A 1 147 ? 23.144 -1.490  5.656   1.00 50.43  ?  370 ASP B CB  1 
ATOM   1121 C CG  . ASP A 1 147 ? 24.238 -1.111  6.637   1.00 55.35  ?  370 ASP B CG  1 
ATOM   1122 O OD1 . ASP A 1 147 ? 24.103 -1.424  7.838   1.00 51.72  ?  370 ASP B OD1 1 
ATOM   1123 O OD2 . ASP A 1 147 ? 25.236 -0.494  6.205   1.00 62.88  ?  370 ASP B OD2 1 
ATOM   1124 N N   . THR A 1 148 ? 22.259 -4.208  7.874   1.00 48.24  ?  371 THR B N   1 
ATOM   1125 C CA  . THR A 1 148 ? 22.708 -5.514  8.329   1.00 49.44  ?  371 THR B CA  1 
ATOM   1126 C C   . THR A 1 148 ? 21.515 -6.315  8.829   1.00 52.83  ?  371 THR B C   1 
ATOM   1127 O O   . THR A 1 148 ? 20.486 -5.762  9.222   1.00 50.65  ?  371 THR B O   1 
ATOM   1128 C CB  . THR A 1 148 ? 23.765 -5.409  9.437   1.00 53.00  ?  371 THR B CB  1 
ATOM   1129 O OG1 . THR A 1 148 ? 24.226 -6.721  9.780   1.00 51.61  ?  371 THR B OG1 1 
ATOM   1130 C CG2 . THR A 1 148 ? 23.180 -4.743  10.677  1.00 52.01  ?  371 THR B CG2 1 
ATOM   1131 N N   . ASP A 1 149 ? 21.669 -7.640  8.816   1.00 49.24  ?  372 ASP B N   1 
ATOM   1132 C CA  . ASP A 1 149 ? 20.582 -8.536  9.184   1.00 54.66  ?  372 ASP B CA  1 
ATOM   1133 C C   . ASP A 1 149 ? 20.960 -9.514  10.292  1.00 50.82  ?  372 ASP B C   1 
ATOM   1134 O O   . ASP A 1 149 ? 20.158 -10.400 10.613  1.00 52.20  ?  372 ASP B O   1 
ATOM   1135 C CB  . ASP A 1 149 ? 20.088 -9.309  7.954   1.00 56.78  ?  372 ASP B CB  1 
ATOM   1136 C CG  . ASP A 1 149 ? 21.208 -10.037 7.228   1.00 53.43  ?  372 ASP B CG  1 
ATOM   1137 O OD1 . ASP A 1 149 ? 22.391 -9.726  7.479   1.00 55.51  ?  372 ASP B OD1 1 
ATOM   1138 O OD2 . ASP A 1 149 ? 20.901 -10.926 6.405   1.00 61.83  ?  372 ASP B OD2 1 
ATOM   1139 N N   . ARG A 1 150 ? 22.142 -9.376  10.893  1.00 45.70  ?  373 ARG B N   1 
ATOM   1140 C CA  . ARG A 1 150 ? 22.582 -10.351 11.885  1.00 55.14  ?  373 ARG B CA  1 
ATOM   1141 C C   . ARG A 1 150 ? 23.737 -9.848  12.746  1.00 53.17  ?  373 ARG B C   1 
ATOM   1142 O O   . ARG A 1 150 ? 24.260 -10.596 13.576  1.00 54.02  ?  373 ARG B O   1 
ATOM   1143 C CB  . ARG A 1 150 ? 22.991 -11.652 11.192  1.00 54.46  ?  373 ARG B CB  1 
ATOM   1144 C CG  . ARG A 1 150 ? 24.223 -11.514 10.313  1.00 56.96  ?  373 ARG B CG  1 
ATOM   1145 C CD  . ARG A 1 150 ? 24.417 -12.731 9.426   1.00 58.46  ?  373 ARG B CD  1 
ATOM   1146 N NE  . ARG A 1 150 ? 25.741 -12.745 8.816   1.00 64.20  ?  373 ARG B NE  1 
ATOM   1147 C CZ  . ARG A 1 150 ? 26.050 -12.125 7.685   1.00 61.20  ?  373 ARG B CZ  1 
ATOM   1148 N NH1 . ARG A 1 150 ? 25.148 -11.442 7.001   1.00 61.98  ?  373 ARG B NH1 1 
ATOM   1149 N NH2 . ARG A 1 150 ? 27.297 -12.195 7.228   1.00 64.45  ?  373 ARG B NH2 1 
ATOM   1150 N N   . ASP A 1 151 ? 24.143 -8.590  12.568  1.00 51.71  ?  374 ASP B N   1 
ATOM   1151 C CA  . ASP A 1 151 ? 25.326 -8.110  13.276  1.00 51.44  ?  374 ASP B CA  1 
ATOM   1152 C C   . ASP A 1 151 ? 25.000 -7.628  14.686  1.00 54.53  ?  374 ASP B C   1 
ATOM   1153 O O   . ASP A 1 151 ? 25.794 -7.838  15.609  1.00 56.02  ?  374 ASP B O   1 
ATOM   1154 C CB  . ASP A 1 151 ? 26.005 -6.995  12.482  1.00 54.12  ?  374 ASP B CB  1 
ATOM   1155 C CG  . ASP A 1 151 ? 27.464 -6.823  12.859  1.00 55.08  ?  374 ASP B CG  1 
ATOM   1156 O OD1 . ASP A 1 151 ? 28.039 -7.763  13.447  1.00 50.31  ?  374 ASP B OD1 1 
ATOM   1157 O OD2 . ASP A 1 151 ? 28.037 -5.751  12.572  1.00 53.64  ?  374 ASP B OD2 1 
ATOM   1158 N N   . PHE A 1 152 ? 23.852 -6.981  14.876  1.00 49.67  ?  375 PHE B N   1 
ATOM   1159 C CA  . PHE A 1 152 ? 23.511 -6.421  16.177  1.00 46.85  ?  375 PHE B CA  1 
ATOM   1160 C C   . PHE A 1 152 ? 23.092 -7.526  17.140  1.00 51.84  ?  375 PHE B C   1 
ATOM   1161 O O   . PHE A 1 152 ? 22.276 -8.387  16.796  1.00 55.29  ?  375 PHE B O   1 
ATOM   1162 C CB  . PHE A 1 152 ? 22.400 -5.382  16.039  1.00 44.85  ?  375 PHE B CB  1 
ATOM   1163 C CG  . PHE A 1 152 ? 22.872 -4.068  15.490  1.00 46.85  ?  375 PHE B CG  1 
ATOM   1164 C CD1 . PHE A 1 152 ? 23.847 -3.338  16.150  1.00 41.00  ?  375 PHE B CD1 1 
ATOM   1165 C CD2 . PHE A 1 152 ? 22.351 -3.566  14.309  1.00 42.40  ?  375 PHE B CD2 1 
ATOM   1166 C CE1 . PHE A 1 152 ? 24.287 -2.128  15.647  1.00 42.16  ?  375 PHE B CE1 1 
ATOM   1167 C CE2 . PHE A 1 152 ? 22.786 -2.359  13.800  1.00 46.13  ?  375 PHE B CE2 1 
ATOM   1168 C CZ  . PHE A 1 152 ? 23.756 -1.639  14.470  1.00 46.08  ?  375 PHE B CZ  1 
ATOM   1169 N N   . GLU A 1 153 ? 23.653 -7.495  18.345  1.00 46.71  ?  376 GLU B N   1 
ATOM   1170 C CA  . GLU A 1 153 ? 23.371 -8.486  19.371  1.00 44.64  ?  376 GLU B CA  1 
ATOM   1171 C C   . GLU A 1 153 ? 22.280 -7.983  20.308  1.00 45.77  ?  376 GLU B C   1 
ATOM   1172 O O   . GLU A 1 153 ? 22.110 -6.778  20.505  1.00 44.45  ?  376 GLU B O   1 
ATOM   1173 C CB  . GLU A 1 153 ? 24.634 -8.816  20.168  1.00 45.30  ?  376 GLU B CB  1 
ATOM   1174 C CG  . GLU A 1 153 ? 25.862 -9.053  19.302  1.00 47.66  ?  376 GLU B CG  1 
ATOM   1175 C CD  . GLU A 1 153 ? 27.150 -9.076  20.101  1.00 54.56  ?  376 GLU B CD  1 
ATOM   1176 O OE1 . GLU A 1 153 ? 27.086 -8.934  21.340  1.00 53.69  ?  376 GLU B OE1 1 
ATOM   1177 O OE2 . GLU A 1 153 ? 28.228 -9.236  19.490  1.00 58.32  ?  376 GLU B OE2 1 
ATOM   1178 N N   . ALA A 1 154 ? 21.537 -8.925  20.882  1.00 42.46  ?  377 ALA B N   1 
ATOM   1179 C CA  . ALA A 1 154 ? 20.469 -8.581  21.803  1.00 43.61  ?  377 ALA B CA  1 
ATOM   1180 C C   . ALA A 1 154 ? 21.027 -8.332  23.202  1.00 39.05  ?  377 ALA B C   1 
ATOM   1181 O O   . ALA A 1 154 ? 22.126 -8.774  23.550  1.00 44.59  ?  377 ALA B O   1 
ATOM   1182 C CB  . ALA A 1 154 ? 19.415 -9.687  21.843  1.00 42.92  ?  377 ALA B CB  1 
ATOM   1183 N N   . ASN A 1 155 ? 20.248 -7.602  24.003  1.00 43.57  ?  378 ASN B N   1 
ATOM   1184 C CA  . ASN A 1 155 ? 20.575 -7.328  25.406  1.00 45.24  ?  378 ASN B CA  1 
ATOM   1185 C C   . ASN A 1 155 ? 21.924 -6.627  25.549  1.00 46.41  ?  378 ASN B C   1 
ATOM   1186 O O   . ASN A 1 155 ? 22.713 -6.936  26.444  1.00 44.01  ?  378 ASN B O   1 
ATOM   1187 C CB  . ASN A 1 155 ? 20.540 -8.611  26.241  1.00 45.44  ?  378 ASN B CB  1 
ATOM   1188 C CG  . ASN A 1 155 ? 19.143 -9.178  26.378  1.00 43.05  ?  378 ASN B CG  1 
ATOM   1189 O OD1 . ASN A 1 155 ? 18.160 -8.437  26.407  1.00 44.85  ?  378 ASN B OD1 1 
ATOM   1190 N ND2 . ASN A 1 155 ? 19.046 -10.498 26.465  1.00 47.13  ?  378 ASN B ND2 1 
ATOM   1191 N N   . GLN A 1 156 ? 22.194 -5.672  24.659  1.00 39.87  ?  379 GLN B N   1 
ATOM   1192 C CA  . GLN A 1 156 ? 23.412 -4.878  24.722  1.00 38.58  ?  379 GLN B CA  1 
ATOM   1193 C C   . GLN A 1 156 ? 23.071 -3.418  24.459  1.00 41.65  ?  379 GLN B C   1 
ATOM   1194 O O   . GLN A 1 156 ? 22.131 -3.107  23.721  1.00 36.12  ?  379 GLN B O   1 
ATOM   1195 C CB  . GLN A 1 156 ? 24.468 -5.359  23.716  1.00 40.71  ?  379 GLN B CB  1 
ATOM   1196 C CG  . GLN A 1 156 ? 24.920 -6.802  23.911  1.00 45.17  ?  379 GLN B CG  1 
ATOM   1197 C CD  . GLN A 1 156 ? 25.780 -6.995  25.149  1.00 46.92  ?  379 GLN B CD  1 
ATOM   1198 O OE1 . GLN A 1 156 ? 26.231 -6.031  25.767  1.00 39.88  ?  379 GLN B OE1 1 
ATOM   1199 N NE2 . GLN A 1 156 ? 26.008 -8.251  25.517  1.00 43.49  ?  379 GLN B NE2 1 
ATOM   1200 N N   . ASN A 1 157 ? 23.848 -2.527  25.073  1.00 39.61  ?  380 ASN B N   1 
ATOM   1201 C CA  . ASN A 1 157 ? 23.615 -1.094  24.941  1.00 38.41  ?  380 ASN B CA  1 
ATOM   1202 C C   . ASN A 1 157 ? 23.774 -0.653  23.491  1.00 32.17  ?  380 ASN B C   1 
ATOM   1203 O O   . ASN A 1 157 ? 24.829 -0.857  22.881  1.00 33.92  ?  380 ASN B O   1 
ATOM   1204 C CB  . ASN A 1 157 ? 24.581 -0.325  25.841  1.00 29.66  ?  380 ASN B CB  1 
ATOM   1205 C CG  . ASN A 1 157 ? 24.216 -0.423  27.313  1.00 40.09  ?  380 ASN B CG  1 
ATOM   1206 O OD1 . ASN A 1 157 ? 23.110 -0.836  27.666  1.00 35.89  ?  380 ASN B OD1 1 
ATOM   1207 N ND2 . ASN A 1 157 ? 25.148 -0.045  28.178  1.00 34.65  ?  380 ASN B ND2 1 
ATOM   1208 N N   . THR A 1 158 ? 22.721 -0.047  22.944  1.00 29.80  ?  381 THR B N   1 
ATOM   1209 C CA  . THR A 1 158 ? 22.691 0.413   21.564  1.00 35.32  ?  381 THR B CA  1 
ATOM   1210 C C   . THR A 1 158 ? 22.265 1.874   21.535  1.00 38.72  ?  381 THR B C   1 
ATOM   1211 O O   . THR A 1 158 ? 21.393 2.289   22.304  1.00 40.14  ?  381 THR B O   1 
ATOM   1212 C CB  . THR A 1 158 ? 21.728 -0.433  20.718  1.00 39.91  ?  381 THR B CB  1 
ATOM   1213 O OG1 . THR A 1 158 ? 21.970 -1.824  20.971  1.00 37.57  ?  381 THR B OG1 1 
ATOM   1214 C CG2 . THR A 1 158 ? 21.918 -0.152  19.231  1.00 39.15  ?  381 THR B CG2 1 
ATOM   1215 N N   . LYS A 1 159 ? 22.885 2.653   20.647  1.00 38.06  ?  382 LYS B N   1 
ATOM   1216 C CA  . LYS A 1 159 ? 22.646 4.087   20.575  1.00 41.31  ?  382 LYS B CA  1 
ATOM   1217 C C   . LYS A 1 159 ? 22.536 4.524   19.122  1.00 36.43  ?  382 LYS B C   1 
ATOM   1218 O O   . LYS A 1 159 ? 23.281 4.045   18.263  1.00 35.20  ?  382 LYS B O   1 
ATOM   1219 C CB  . LYS A 1 159 ? 23.766 4.874   21.272  1.00 38.70  ?  382 LYS B CB  1 
ATOM   1220 C CG  . LYS A 1 159 ? 23.612 6.388   21.196  1.00 33.85  ?  382 LYS B CG  1 
ATOM   1221 C CD  . LYS A 1 159 ? 24.962 7.092   21.186  1.00 38.87  ?  382 LYS B CD  1 
ATOM   1222 C CE  . LYS A 1 159 ? 24.803 8.605   21.294  1.00 46.39  ?  382 LYS B CE  1 
ATOM   1223 N NZ  . LYS A 1 159 ? 26.087 9.328   21.058  1.00 37.44  ?  382 LYS B NZ  1 
ATOM   1224 N N   . PHE A 1 160 ? 21.604 5.437   18.856  1.00 39.60  ?  383 PHE B N   1 
ATOM   1225 C CA  . PHE A 1 160 ? 21.418 6.029   17.538  1.00 37.25  ?  383 PHE B CA  1 
ATOM   1226 C C   . PHE A 1 160 ? 21.907 7.469   17.569  1.00 37.37  ?  383 PHE B C   1 
ATOM   1227 O O   . PHE A 1 160 ? 21.413 8.279   18.362  1.00 39.72  ?  383 PHE B O   1 
ATOM   1228 C CB  . PHE A 1 160 ? 19.952 5.976   17.108  1.00 38.25  ?  383 PHE B CB  1 
ATOM   1229 C CG  . PHE A 1 160 ? 19.684 6.638   15.784  1.00 42.69  ?  383 PHE B CG  1 
ATOM   1230 C CD1 . PHE A 1 160 ? 20.117 6.057   14.603  1.00 36.84  ?  383 PHE B CD1 1 
ATOM   1231 C CD2 . PHE A 1 160 ? 18.996 7.840   15.721  1.00 38.66  ?  383 PHE B CD2 1 
ATOM   1232 C CE1 . PHE A 1 160 ? 19.868 6.663   13.383  1.00 39.46  ?  383 PHE B CE1 1 
ATOM   1233 C CE2 . PHE A 1 160 ? 18.744 8.451   14.504  1.00 40.40  ?  383 PHE B CE2 1 
ATOM   1234 C CZ  . PHE A 1 160 ? 19.181 7.862   13.334  1.00 35.80  ?  383 PHE B CZ  1 
ATOM   1235 N N   . THR A 1 161 ? 22.873 7.785   16.710  1.00 38.56  ?  384 THR B N   1 
ATOM   1236 C CA  . THR A 1 161 ? 23.367 9.147   16.561  1.00 37.76  ?  384 THR B CA  1 
ATOM   1237 C C   . THR A 1 161 ? 22.817 9.736   15.273  1.00 36.83  ?  384 THR B C   1 
ATOM   1238 O O   . THR A 1 161 ? 23.123 9.221   14.188  1.00 37.38  ?  384 THR B O   1 
ATOM   1239 C CB  . THR A 1 161 ? 24.894 9.174   16.547  1.00 36.65  ?  384 THR B CB  1 
ATOM   1240 O OG1 . THR A 1 161 ? 25.395 8.712   17.807  1.00 40.53  ?  384 THR B OG1 1 
ATOM   1241 C CG2 . THR A 1 161 ? 25.400 10.588  16.294  1.00 32.41  ?  384 THR B CG2 1 
ATOM   1242 N N   . PRO A 1 162 ? 22.017 10.799  15.331  1.00 39.65  ?  385 PRO B N   1 
ATOM   1243 C CA  . PRO A 1 162 ? 21.456 11.366  14.102  1.00 35.00  ?  385 PRO B CA  1 
ATOM   1244 C C   . PRO A 1 162 ? 22.514 12.086  13.285  1.00 37.81  ?  385 PRO B C   1 
ATOM   1245 O O   . PRO A 1 162 ? 23.489 12.625  13.817  1.00 37.78  ?  385 PRO B O   1 
ATOM   1246 C CB  . PRO A 1 162 ? 20.394 12.343  14.616  1.00 37.02  ?  385 PRO B CB  1 
ATOM   1247 C CG  . PRO A 1 162 ? 20.911 12.769  15.953  1.00 35.38  ?  385 PRO B CG  1 
ATOM   1248 C CD  . PRO A 1 162 ? 21.644 11.581  16.524  1.00 36.84  ?  385 PRO B CD  1 
ATOM   1249 N N   . VAL A 1 163 ? 22.310 12.094  11.969  1.00 39.13  ?  386 VAL B N   1 
ATOM   1250 C CA  . VAL A 1 163 ? 23.237 12.753  11.056  1.00 37.44  ?  386 VAL B CA  1 
ATOM   1251 C C   . VAL A 1 163 ? 22.472 13.718  10.160  1.00 34.90  ?  386 VAL B C   1 
ATOM   1252 O O   . VAL A 1 163 ? 22.821 14.899  10.060  1.00 36.92  ?  386 VAL B O   1 
ATOM   1253 C CB  . VAL A 1 163 ? 24.024 11.727  10.221  1.00 35.79  ?  386 VAL B CB  1 
ATOM   1254 C CG1 . VAL A 1 163 ? 24.751 12.420  9.079   1.00 37.71  ?  386 VAL B CG1 1 
ATOM   1255 C CG2 . VAL A 1 163 ? 25.007 10.970  11.099  1.00 32.24  ?  386 VAL B CG2 1 
ATOM   1256 N N   . GLY A 1 164 ? 21.427 13.229  9.506   1.00 35.31  ?  387 GLY B N   1 
ATOM   1257 C CA  . GLY A 1 164 ? 20.673 14.074  8.611   1.00 34.85  ?  387 GLY B CA  1 
ATOM   1258 C C   . GLY A 1 164 ? 19.366 13.446  8.186   1.00 39.82  ?  387 GLY B C   1 
ATOM   1259 O O   . GLY A 1 164 ? 18.873 12.509  8.817   1.00 36.61  ?  387 GLY B O   1 
ATOM   1260 N N   . VAL A 1 165 ? 18.809 13.981  7.096   1.00 34.26  ?  388 VAL B N   1 
ATOM   1261 C CA  . VAL A 1 165 ? 17.514 13.562  6.584   1.00 36.73  ?  388 VAL B CA  1 
ATOM   1262 C C   . VAL A 1 165 ? 17.655 13.175  5.116   1.00 37.80  ?  388 VAL B C   1 
ATOM   1263 O O   . VAL A 1 165 ? 18.566 13.618  4.414   1.00 35.27  ?  388 VAL B O   1 
ATOM   1264 C CB  . VAL A 1 165 ? 16.440 14.660  6.749   1.00 31.22  ?  388 VAL B CB  1 
ATOM   1265 C CG1 . VAL A 1 165 ? 16.088 14.839  8.219   1.00 36.87  ?  388 VAL B CG1 1 
ATOM   1266 C CG2 . VAL A 1 165 ? 16.921 15.970  6.143   1.00 31.64  ?  388 VAL B CG2 1 
ATOM   1267 N N   . ILE A 1 166 ? 16.727 12.336  4.655   1.00 40.79  ?  389 ILE B N   1 
ATOM   1268 C CA  . ILE A 1 166 ? 16.719 11.830  3.292   1.00 39.30  ?  389 ILE B CA  1 
ATOM   1269 C C   . ILE A 1 166 ? 15.351 12.099  2.669   1.00 41.19  ?  389 ILE B C   1 
ATOM   1270 O O   . ILE A 1 166 ? 14.427 12.577  3.327   1.00 40.52  ?  389 ILE B O   1 
ATOM   1271 C CB  . ILE A 1 166 ? 17.067 10.327  3.221   1.00 39.41  ?  389 ILE B CB  1 
ATOM   1272 C CG1 . ILE A 1 166 ? 16.088 9.510   4.063   1.00 41.64  ?  389 ILE B CG1 1 
ATOM   1273 C CG2 . ILE A 1 166 ? 18.489 10.083  3.689   1.00 37.87  ?  389 ILE B CG2 1 
ATOM   1274 C CD1 . ILE A 1 166 ? 15.869 8.104   3.554   1.00 40.12  ?  389 ILE B CD1 1 
ATOM   1275 N N   . GLN A 1 167 ? 15.238 11.779  1.381   1.00 42.17  ?  390 GLN B N   1 
ATOM   1276 C CA  . GLN A 1 167 ? 14.017 11.988  0.618   1.00 40.29  ?  390 GLN B CA  1 
ATOM   1277 C C   . GLN A 1 167 ? 14.075 11.113  -0.629  1.00 42.57  ?  390 GLN B C   1 
ATOM   1278 O O   . GLN A 1 167 ? 15.155 10.842  -1.160  1.00 40.78  ?  390 GLN B O   1 
ATOM   1279 C CB  . GLN A 1 167 ? 13.846 13.465  0.239   1.00 39.03  ?  390 GLN B CB  1 
ATOM   1280 C CG  . GLN A 1 167 ? 12.556 13.791  -0.494  1.00 39.45  ?  390 GLN B CG  1 
ATOM   1281 C CD  . GLN A 1 167 ? 12.755 13.902  -1.993  1.00 44.03  ?  390 GLN B CD  1 
ATOM   1282 O OE1 . GLN A 1 167 ? 13.877 13.798  -2.492  1.00 41.89  ?  390 GLN B OE1 1 
ATOM   1283 N NE2 . GLN A 1 167 ? 11.665 14.111  -2.723  1.00 38.52  ?  390 GLN B NE2 1 
ATOM   1284 N N   . ASP A 1 168 ? 12.904 10.665  -1.078  1.00 44.14  ?  391 ASP B N   1 
ATOM   1285 C CA  . ASP A 1 168 ? 12.800 9.843   -2.282  1.00 46.49  ?  391 ASP B CA  1 
ATOM   1286 C C   . ASP A 1 168 ? 12.932 10.749  -3.501  1.00 49.63  ?  391 ASP B C   1 
ATOM   1287 O O   . ASP A 1 168 ? 12.028 11.535  -3.799  1.00 45.07  ?  391 ASP B O   1 
ATOM   1288 C CB  . ASP A 1 168 ? 11.476 9.083   -2.295  1.00 43.49  ?  391 ASP B CB  1 
ATOM   1289 C CG  . ASP A 1 168 ? 11.400 8.053   -3.410  1.00 52.60  ?  391 ASP B CG  1 
ATOM   1290 O OD1 . ASP A 1 168 ? 12.342 7.972   -4.227  1.00 47.89  ?  391 ASP B OD1 1 
ATOM   1291 O OD2 . ASP A 1 168 ? 10.390 7.321   -3.468  1.00 54.07  ?  391 ASP B OD2 1 
ATOM   1292 N N   . GLY A 1 169 ? 14.053 10.633  -4.216  1.00 45.36  ?  392 GLY B N   1 
ATOM   1293 C CA  . GLY A 1 169 ? 14.311 11.520  -5.338  1.00 46.07  ?  392 GLY B CA  1 
ATOM   1294 C C   . GLY A 1 169 ? 13.342 11.366  -6.489  1.00 55.04  ?  392 GLY B C   1 
ATOM   1295 O O   . GLY A 1 169 ? 13.275 12.243  -7.357  1.00 53.26  ?  392 GLY B O   1 
ATOM   1296 N N   . GLY A 1 170 ? 12.598 10.262  -6.524  1.00 51.76  ?  393 GLY B N   1 
ATOM   1297 C CA  . GLY A 1 170 ? 11.606 10.051  -7.557  1.00 44.46  ?  393 GLY B CA  1 
ATOM   1298 C C   . GLY A 1 170 ? 10.293 10.771  -7.344  1.00 50.69  ?  393 GLY B C   1 
ATOM   1299 O O   . GLY A 1 170 ? 9.463  10.805  -8.259  1.00 53.06  ?  393 GLY B O   1 
ATOM   1300 N N   . THR A 1 171 ? 10.083 11.348  -6.165  1.00 52.15  ?  394 THR B N   1 
ATOM   1301 C CA  . THR A 1 171 ? 8.879  12.103  -5.862  1.00 46.86  ?  394 THR B CA  1 
ATOM   1302 C C   . THR A 1 171 ? 9.191  13.598  -5.884  1.00 46.53  ?  394 THR B C   1 
ATOM   1303 O O   . THR A 1 171 ? 10.321 14.017  -6.145  1.00 45.21  ?  394 THR B O   1 
ATOM   1304 C CB  . THR A 1 171 ? 8.298  11.673  -4.512  1.00 52.16  ?  394 THR B CB  1 
ATOM   1305 O OG1 . THR A 1 171 ? 9.359  11.478  -3.569  1.00 50.61  ?  394 THR B OG1 1 
ATOM   1306 C CG2 . THR A 1 171 ? 7.516  10.376  -4.661  1.00 49.69  ?  394 THR B CG2 1 
ATOM   1307 N N   . THR A 1 172 ? 8.167  14.409  -5.615  1.00 48.68  ?  395 THR B N   1 
ATOM   1308 C CA  . THR A 1 172 ? 8.318  15.859  -5.651  1.00 44.90  ?  395 THR B CA  1 
ATOM   1309 C C   . THR A 1 172 ? 9.444  16.303  -4.725  1.00 50.28  ?  395 THR B C   1 
ATOM   1310 O O   . THR A 1 172 ? 9.515  15.882  -3.567  1.00 44.51  ?  395 THR B O   1 
ATOM   1311 C CB  . THR A 1 172 ? 7.008  16.543  -5.252  1.00 46.63  ?  395 THR B CB  1 
ATOM   1312 O OG1 . THR A 1 172 ? 5.925  15.988  -6.006  1.00 52.18  ?  395 THR B OG1 1 
ATOM   1313 C CG2 . THR A 1 172 ? 7.090  18.040  -5.516  1.00 44.21  ?  395 THR B CG2 1 
ATOM   1314 N N   . HIS A 1 173 ? 10.332 17.144  -5.243  1.00 43.98  ?  396 HIS B N   1 
ATOM   1315 C CA  . HIS A 1 173 ? 11.512 17.537  -4.488  1.00 45.40  ?  396 HIS B CA  1 
ATOM   1316 C C   . HIS A 1 173 ? 11.128 18.421  -3.307  1.00 45.20  ?  396 HIS B C   1 
ATOM   1317 O O   . HIS A 1 173 ? 10.182 19.210  -3.381  1.00 43.96  ?  396 HIS B O   1 
ATOM   1318 C CB  . HIS A 1 173 ? 12.506 18.259  -5.395  1.00 45.75  ?  396 HIS B CB  1 
ATOM   1319 C CG  . HIS A 1 173 ? 13.148 17.367  -6.413  1.00 48.06  ?  396 HIS B CG  1 
ATOM   1320 N ND1 . HIS A 1 173 ? 14.039 17.831  -7.357  1.00 50.62  ?  396 HIS B ND1 1 
ATOM   1321 C CD2 . HIS A 1 173 ? 13.028 16.036  -6.633  1.00 46.99  ?  396 HIS B CD2 1 
ATOM   1322 C CE1 . HIS A 1 173 ? 14.440 16.825  -8.114  1.00 49.24  ?  396 HIS B CE1 1 
ATOM   1323 N NE2 . HIS A 1 173 ? 13.842 15.724  -7.695  1.00 45.89  ?  396 HIS B NE2 1 
ATOM   1324 N N   . ARG A 1 174 ? 11.864 18.266  -2.206  1.00 48.06  ?  397 ARG B N   1 
ATOM   1325 C CA  . ARG A 1 174 ? 11.663 19.023  -0.971  1.00 44.46  ?  397 ARG B CA  1 
ATOM   1326 C C   . ARG A 1 174 ? 10.295 18.767  -0.345  1.00 42.35  ?  397 ARG B C   1 
ATOM   1327 O O   . ARG A 1 174 ? 9.780  19.611  0.393   1.00 48.55  ?  397 ARG B O   1 
ATOM   1328 C CB  . ARG A 1 174 ? 11.868 20.526  -1.201  1.00 42.97  ?  397 ARG B CB  1 
ATOM   1329 C CG  . ARG A 1 174 ? 13.321 20.964  -1.169  1.00 45.31  ?  397 ARG B CG  1 
ATOM   1330 C CD  . ARG A 1 174 ? 13.451 22.445  -1.473  1.00 49.83  ?  397 ARG B CD  1 
ATOM   1331 N NE  . ARG A 1 174 ? 13.832 23.201  -0.286  1.00 61.00  ?  397 ARG B NE  1 
ATOM   1332 C CZ  . ARG A 1 174 ? 12.983 23.879  0.474   1.00 62.88  ?  397 ARG B CZ  1 
ATOM   1333 N NH1 . ARG A 1 174 ? 11.693 23.936  0.187   1.00 62.26  ?  397 ARG B NH1 1 
ATOM   1334 N NH2 . ARG A 1 174 ? 13.440 24.514  1.550   1.00 45.27  ?  397 ARG B NH2 1 
ATOM   1335 N N   . ASN A 1 175 ? 9.693  17.611  -0.619  1.00 41.05  ?  398 ASN B N   1 
ATOM   1336 C CA  . ASN A 1 175 ? 8.435  17.236  0.015   1.00 43.39  ?  398 ASN B CA  1 
ATOM   1337 C C   . ASN A 1 175 ? 8.637  16.575  1.372   1.00 48.94  ?  398 ASN B C   1 
ATOM   1338 O O   . ASN A 1 175 ? 7.655  16.147  1.990   1.00 48.93  ?  398 ASN B O   1 
ATOM   1339 C CB  . ASN A 1 175 ? 7.636  16.299  -0.898  1.00 39.05  ?  398 ASN B CB  1 
ATOM   1340 C CG  . ASN A 1 175 ? 8.285  14.931  -1.054  1.00 44.14  ?  398 ASN B CG  1 
ATOM   1341 O OD1 . ASN A 1 175 ? 9.475  14.760  -0.787  1.00 45.24  ?  398 ASN B OD1 1 
ATOM   1342 N ND2 . ASN A 1 175 ? 7.502  13.953  -1.494  1.00 45.64  ?  398 ASN B ND2 1 
ATOM   1343 N N   . GLU A 1 176 ? 9.880  16.488  1.849   1.00 42.88  ?  399 GLU B N   1 
ATOM   1344 C CA  . GLU A 1 176 ? 10.184 15.745  3.058   1.00 41.34  ?  399 GLU B CA  1 
ATOM   1345 C C   . GLU A 1 176 ? 11.523 16.223  3.587   1.00 42.47  ?  399 GLU B C   1 
ATOM   1346 O O   . GLU A 1 176 ? 12.418 16.505  2.781   1.00 44.64  ?  399 GLU B O   1 
ATOM   1347 C CB  . GLU A 1 176 ? 10.237 14.241  2.772   1.00 43.77  ?  399 GLU B CB  1 
ATOM   1348 C CG  . GLU A 1 176 ? 9.522  13.399  3.794   1.00 46.53  ?  399 GLU B CG  1 
ATOM   1349 C CD  . GLU A 1 176 ? 9.768  11.923  3.597   1.00 50.97  ?  399 GLU B CD  1 
ATOM   1350 O OE1 . GLU A 1 176 ? 10.181 11.525  2.487   1.00 53.77  ?  399 GLU B OE1 1 
ATOM   1351 O OE2 . GLU A 1 176 ? 9.553  11.162  4.565   1.00 54.08  ?  399 GLU B OE2 1 
ATOM   1352 N N   . PRO A 1 177 ? 11.705 16.336  4.913   1.00 43.24  ?  400 PRO B N   1 
ATOM   1353 C CA  . PRO A 1 177 ? 10.678 16.099  5.934   1.00 46.36  ?  400 PRO B CA  1 
ATOM   1354 C C   . PRO A 1 177 ? 9.724  17.280  6.106   1.00 42.97  ?  400 PRO B C   1 
ATOM   1355 O O   . PRO A 1 177 ? 9.895  18.313  5.458   1.00 40.05  ?  400 PRO B O   1 
ATOM   1356 C CB  . PRO A 1 177 ? 11.498 15.883  7.207   1.00 41.84  ?  400 PRO B CB  1 
ATOM   1357 C CG  . PRO A 1 177 ? 12.728 16.687  6.991   1.00 40.54  ?  400 PRO B CG  1 
ATOM   1358 C CD  . PRO A 1 177 ? 13.026 16.591  5.516   1.00 42.12  ?  400 PRO B CD  1 
ATOM   1359 N N   . GLN A 1 178 ? 8.727  17.119  6.972   1.00 38.27  ?  401 GLN B N   1 
ATOM   1360 C CA  . GLN A 1 178 ? 7.768  18.175  7.289   1.00 44.12  ?  401 GLN B CA  1 
ATOM   1361 C C   . GLN A 1 178 ? 8.053  18.641  8.713   1.00 42.27  ?  401 GLN B C   1 
ATOM   1362 O O   . GLN A 1 178 ? 7.656  17.988  9.683   1.00 39.47  ?  401 GLN B O   1 
ATOM   1363 C CB  . GLN A 1 178 ? 6.336  17.677  7.126   1.00 43.81  ?  401 GLN B CB  1 
ATOM   1364 C CG  . GLN A 1 178 ? 6.040  17.117  5.742   1.00 42.15  ?  401 GLN B CG  1 
ATOM   1365 C CD  . GLN A 1 178 ? 4.832  16.205  5.730   1.00 48.97  ?  401 GLN B CD  1 
ATOM   1366 O OE1 . GLN A 1 178 ? 4.964  14.981  5.700   1.00 51.55  ?  401 GLN B OE1 1 
ATOM   1367 N NE2 . GLN A 1 178 ? 3.643  16.798  5.752   1.00 52.85  ?  401 GLN B NE2 1 
ATOM   1368 N N   . GLN A 1 179 ? 8.742  19.779  8.833   1.00 41.37  ?  402 GLN B N   1 
ATOM   1369 C CA  . GLN A 1 179 ? 9.223  20.228  10.133  1.00 43.84  ?  402 GLN B CA  1 
ATOM   1370 C C   . GLN A 1 179 ? 8.105  20.734  11.034  1.00 43.76  ?  402 GLN B C   1 
ATOM   1371 O O   . GLN A 1 179 ? 8.318  20.865  12.244  1.00 40.27  ?  402 GLN B O   1 
ATOM   1372 C CB  . GLN A 1 179 ? 10.279 21.318  9.955   1.00 42.02  ?  402 GLN B CB  1 
ATOM   1373 C CG  . GLN A 1 179 ? 9.724  22.651  9.492   1.00 42.30  ?  402 GLN B CG  1 
ATOM   1374 C CD  . GLN A 1 179 ? 10.639 23.807  9.835   1.00 43.77  ?  402 GLN B CD  1 
ATOM   1375 O OE1 . GLN A 1 179 ? 11.261 23.827  10.896  1.00 42.47  ?  402 GLN B OE1 1 
ATOM   1376 N NE2 . GLN A 1 179 ? 10.731 24.779  8.930   1.00 38.42  ?  402 GLN B NE2 1 
ATOM   1377 N N   . TRP A 1 180 ? 6.924  21.019  10.483  1.00 44.54  ?  403 TRP B N   1 
ATOM   1378 C CA  . TRP A 1 180 ? 5.803  21.528  11.264  1.00 44.69  ?  403 TRP B CA  1 
ATOM   1379 C C   . TRP A 1 180 ? 4.691  20.499  11.427  1.00 44.81  ?  403 TRP B C   1 
ATOM   1380 O O   . TRP A 1 180 ? 3.543  20.869  11.695  1.00 47.67  ?  403 TRP B O   1 
ATOM   1381 C CB  . TRP A 1 180 ? 5.261  22.810  10.631  1.00 45.14  ?  403 TRP B CB  1 
ATOM   1382 C CG  . TRP A 1 180 ? 6.300  23.881  10.492  1.00 47.19  ?  403 TRP B CG  1 
ATOM   1383 C CD1 . TRP A 1 180 ? 6.719  24.471  9.335   1.00 44.15  ?  403 TRP B CD1 1 
ATOM   1384 C CD2 . TRP A 1 180 ? 7.060  24.482  11.548  1.00 44.09  ?  403 TRP B CD2 1 
ATOM   1385 N NE1 . TRP A 1 180 ? 7.687  25.407  9.607   1.00 48.94  ?  403 TRP B NE1 1 
ATOM   1386 C CE2 . TRP A 1 180 ? 7.917  25.432  10.958  1.00 44.76  ?  403 TRP B CE2 1 
ATOM   1387 C CE3 . TRP A 1 180 ? 7.099  24.310  12.936  1.00 43.08  ?  403 TRP B CE3 1 
ATOM   1388 C CZ2 . TRP A 1 180 ? 8.801  26.207  11.704  1.00 41.07  ?  403 TRP B CZ2 1 
ATOM   1389 C CZ3 . TRP A 1 180 ? 7.978  25.080  13.675  1.00 43.16  ?  403 TRP B CZ3 1 
ATOM   1390 C CH2 . TRP A 1 180 ? 8.815  26.017  13.059  1.00 39.58  ?  403 TRP B CH2 1 
ATOM   1391 N N   . VAL A 1 181 ? 5.008  19.215  11.276  1.00 43.91  ?  404 VAL B N   1 
ATOM   1392 C CA  . VAL A 1 181 ? 4.050  18.127  11.443  1.00 45.37  ?  404 VAL B CA  1 
ATOM   1393 C C   . VAL A 1 181 ? 4.578  17.225  12.551  1.00 44.72  ?  404 VAL B C   1 
ATOM   1394 O O   . VAL A 1 181 ? 5.580  16.521  12.365  1.00 48.03  ?  404 VAL B O   1 
ATOM   1395 C CB  . VAL A 1 181 ? 3.837  17.339  10.142  1.00 44.29  ?  404 VAL B CB  1 
ATOM   1396 C CG1 . VAL A 1 181 ? 2.961  16.120  10.393  1.00 39.36  ?  404 VAL B CG1 1 
ATOM   1397 C CG2 . VAL A 1 181 ? 3.219  18.232  9.076   1.00 41.82  ?  404 VAL B CG2 1 
ATOM   1398 N N   . LEU A 1 182 ? 3.909  17.242  13.701  1.00 45.71  ?  405 LEU B N   1 
ATOM   1399 C CA  . LEU A 1 182 ? 4.365  16.454  14.836  1.00 44.78  ?  405 LEU B CA  1 
ATOM   1400 C C   . LEU A 1 182 ? 4.163  14.965  14.566  1.00 44.57  ?  405 LEU B C   1 
ATOM   1401 O O   . LEU A 1 182 ? 3.162  14.572  13.959  1.00 43.45  ?  405 LEU B O   1 
ATOM   1402 C CB  . LEU A 1 182 ? 3.612  16.853  16.106  1.00 44.56  ?  405 LEU B CB  1 
ATOM   1403 C CG  . LEU A 1 182 ? 4.006  18.172  16.770  1.00 49.06  ?  405 LEU B CG  1 
ATOM   1404 C CD1 . LEU A 1 182 ? 3.179  18.397  18.026  1.00 47.91  ?  405 LEU B CD1 1 
ATOM   1405 C CD2 . LEU A 1 182 ? 5.490  18.188  17.093  1.00 41.84  ?  405 LEU B CD2 1 
ATOM   1406 N N   . PRO A 1 183 ? 5.087  14.116  15.005  1.00 44.23  ?  406 PRO B N   1 
ATOM   1407 C CA  . PRO A 1 183 ? 4.896  12.671  14.852  1.00 44.16  ?  406 PRO B CA  1 
ATOM   1408 C C   . PRO A 1 183 ? 3.812  12.163  15.788  1.00 47.02  ?  406 PRO B C   1 
ATOM   1409 O O   . PRO A 1 183 ? 3.379  12.838  16.724  1.00 46.18  ?  406 PRO B O   1 
ATOM   1410 C CB  . PRO A 1 183 ? 6.264  12.076  15.216  1.00 42.59  ?  406 PRO B CB  1 
ATOM   1411 C CG  . PRO A 1 183 ? 7.212  13.244  15.295  1.00 39.53  ?  406 PRO B CG  1 
ATOM   1412 C CD  . PRO A 1 183 ? 6.375  14.435  15.638  1.00 42.15  ?  406 PRO B CD  1 
ATOM   1413 N N   . SER A 1 184 ? 3.367  10.940  15.513  1.00 41.60  ?  407 SER B N   1 
ATOM   1414 C CA  . SER A 1 184 ? 2.447  10.223  16.392  1.00 51.67  ?  407 SER B CA  1 
ATOM   1415 C C   . SER A 1 184 ? 3.294  9.479   17.418  1.00 52.25  ?  407 SER B C   1 
ATOM   1416 O O   . SER A 1 184 ? 3.890  8.443   17.116  1.00 51.93  ?  407 SER B O   1 
ATOM   1417 C CB  . SER A 1 184 ? 1.559  9.279   15.590  1.00 57.57  ?  407 SER B CB  1 
ATOM   1418 O OG  . SER A 1 184 ? 0.461  9.973   15.027  1.00 62.57  ?  407 SER B OG  1 
ATOM   1419 N N   . TYR A 1 185 ? 3.343  10.012  18.641  1.00 48.47  ?  408 TYR B N   1 
ATOM   1420 C CA  . TYR A 1 185 ? 4.329  9.564   19.619  1.00 51.38  ?  408 TYR B CA  1 
ATOM   1421 C C   . TYR A 1 185 ? 4.045  8.170   20.168  1.00 50.96  ?  408 TYR B C   1 
ATOM   1422 O O   . TYR A 1 185 ? 4.962  7.536   20.697  1.00 53.94  ?  408 TYR B O   1 
ATOM   1423 C CB  . TYR A 1 185 ? 4.412  10.566  20.770  1.00 44.18  ?  408 TYR B CB  1 
ATOM   1424 C CG  . TYR A 1 185 ? 5.050  11.885  20.391  1.00 45.80  ?  408 TYR B CG  1 
ATOM   1425 C CD1 . TYR A 1 185 ? 6.326  11.931  19.844  1.00 47.08  ?  408 TYR B CD1 1 
ATOM   1426 C CD2 . TYR A 1 185 ? 4.376  13.084  20.584  1.00 41.90  ?  408 TYR B CD2 1 
ATOM   1427 C CE1 . TYR A 1 185 ? 6.914  13.137  19.501  1.00 40.02  ?  408 TYR B CE1 1 
ATOM   1428 C CE2 . TYR A 1 185 ? 4.954  14.291  20.243  1.00 42.35  ?  408 TYR B CE2 1 
ATOM   1429 C CZ  . TYR A 1 185 ? 6.222  14.313  19.705  1.00 40.83  ?  408 TYR B CZ  1 
ATOM   1430 O OH  . TYR A 1 185 ? 6.795  15.517  19.368  1.00 45.60  ?  408 TYR B OH  1 
ATOM   1431 N N   . SER A 1 186 ? 2.810  7.677   20.069  1.00 48.09  ?  409 SER B N   1 
ATOM   1432 C CA  . SER A 1 186 ? 2.477  6.354   20.588  1.00 56.56  ?  409 SER B CA  1 
ATOM   1433 C C   . SER A 1 186 ? 1.916  5.427   19.516  1.00 57.93  ?  409 SER B C   1 
ATOM   1434 O O   . SER A 1 186 ? 1.373  4.368   19.850  1.00 58.78  ?  409 SER B O   1 
ATOM   1435 C CB  . SER A 1 186 ? 1.480  6.463   21.747  1.00 55.40  ?  409 SER B CB  1 
ATOM   1436 O OG  . SER A 1 186 ? 1.827  7.514   22.631  1.00 55.32  ?  409 SER B OG  1 
ATOM   1437 N N   . GLY A 1 187 ? 2.033  5.791   18.243  1.00 60.23  ?  410 GLY B N   1 
ATOM   1438 C CA  . GLY A 1 187 ? 1.458  4.993   17.179  1.00 63.46  ?  410 GLY B CA  1 
ATOM   1439 C C   . GLY A 1 187 ? 0.516  5.791   16.303  1.00 66.51  ?  410 GLY B C   1 
ATOM   1440 O O   . GLY A 1 187 ? 0.013  6.840   16.718  1.00 69.49  ?  410 GLY B O   1 
ATOM   1441 N N   . ARG A 1 188 ? 0.256  5.291   15.093  1.00 71.56  ?  411 ARG B N   1 
ATOM   1442 C CA  . ARG A 1 188 ? -0.508 6.051   14.108  1.00 77.44  ?  411 ARG B CA  1 
ATOM   1443 C C   . ARG A 1 188 ? -1.934 6.337   14.570  1.00 83.55  ?  411 ARG B C   1 
ATOM   1444 O O   . ARG A 1 188 ? -2.539 7.322   14.130  1.00 82.94  ?  411 ARG B O   1 
ATOM   1445 C CB  . ARG A 1 188 ? -0.527 5.306   12.768  1.00 76.71  ?  411 ARG B CB  1 
ATOM   1446 C CG  . ARG A 1 188 ? -1.469 4.102   12.714  1.00 82.69  ?  411 ARG B CG  1 
ATOM   1447 C CD  . ARG A 1 188 ? -0.907 2.919   13.487  1.00 88.27  ?  411 ARG B CD  1 
ATOM   1448 N NE  . ARG A 1 188 ? -1.804 1.770   13.504  1.00 92.22  ?  411 ARG B NE  1 
ATOM   1449 C CZ  . ARG A 1 188 ? -2.353 1.274   14.603  1.00 88.77  ?  411 ARG B CZ  1 
ATOM   1450 N NH1 . ARG A 1 188 ? -2.140 1.820   15.790  1.00 87.36  ?  411 ARG B NH1 1 
ATOM   1451 N NH2 . ARG A 1 188 ? -3.136 0.204   14.512  1.00 84.39  ?  411 ARG B NH2 1 
ATOM   1452 N N   . ASN A 1 189 ? -2.487 5.501   15.450  1.00 83.13  ?  412 ASN B N   1 
ATOM   1453 C CA  . ASN A 1 189 ? -3.873 5.656   15.872  1.00 85.70  ?  412 ASN B CA  1 
ATOM   1454 C C   . ASN A 1 189 ? -4.031 6.391   17.196  1.00 83.36  ?  412 ASN B C   1 
ATOM   1455 O O   . ASN A 1 189 ? -5.118 6.912   17.468  1.00 84.76  ?  412 ASN B O   1 
ATOM   1456 C CB  . ASN A 1 189 ? -4.553 4.286   15.979  1.00 92.23  ?  412 ASN B CB  1 
ATOM   1457 C CG  . ASN A 1 189 ? -5.848 4.216   15.193  1.00 91.15  ?  412 ASN B CG  1 
ATOM   1458 O OD1 . ASN A 1 189 ? -6.012 4.903   14.185  1.00 88.59  ?  412 ASN B OD1 1 
ATOM   1459 N ND2 . ASN A 1 189 ? -6.777 3.386   15.656  1.00 87.75  ?  412 ASN B ND2 1 
ATOM   1460 N N   . THR A 1 190 ? -2.987 6.448   18.018  1.00 80.09  ?  413 THR B N   1 
ATOM   1461 C CA  . THR A 1 190 ? -3.087 7.100   19.313  1.00 82.31  ?  413 THR B CA  1 
ATOM   1462 C C   . THR A 1 190 ? -3.115 8.619   19.151  1.00 78.57  ?  413 THR B C   1 
ATOM   1463 O O   . THR A 1 190 ? -2.945 9.166   18.056  1.00 79.33  ?  413 THR B O   1 
ATOM   1464 C CB  . THR A 1 190 ? -1.921 6.692   20.210  1.00 77.41  ?  413 THR B CB  1 
ATOM   1465 O OG1 . THR A 1 190 ? -0.694 7.145   19.625  1.00 74.19  ?  413 THR B OG1 1 
ATOM   1466 C CG2 . THR A 1 190 ? -1.875 5.178   20.375  1.00 73.43  ?  413 THR B CG2 1 
ATOM   1467 N N   . HIS A 1 191 ? -3.331 9.304   20.270  1.00 74.32  ?  414 HIS B N   1 
ATOM   1468 C CA  . HIS A 1 191 ? -3.385 10.758  20.314  1.00 70.19  ?  414 HIS B CA  1 
ATOM   1469 C C   . HIS A 1 191 ? -2.255 11.285  21.187  1.00 68.83  ?  414 HIS B C   1 
ATOM   1470 O O   . HIS A 1 191 ? -1.975 10.733  22.257  1.00 68.81  ?  414 HIS B O   1 
ATOM   1471 C CB  . HIS A 1 191 ? -4.737 11.243  20.851  1.00 75.13  ?  414 HIS B CB  1 
ATOM   1472 C CG  . HIS A 1 191 ? -4.954 12.718  20.704  1.00 82.58  ?  414 HIS B CG  1 
ATOM   1473 N ND1 . HIS A 1 191 ? -4.555 13.627  21.660  1.00 86.22  ?  414 HIS B ND1 1 
ATOM   1474 C CD2 . HIS A 1 191 ? -5.530 13.441  19.715  1.00 82.31  ?  414 HIS B CD2 1 
ATOM   1475 C CE1 . HIS A 1 191 ? -4.876 14.847  21.265  1.00 84.63  ?  414 HIS B CE1 1 
ATOM   1476 N NE2 . HIS A 1 191 ? -5.467 14.761  20.087  1.00 81.14  ?  414 HIS B NE2 1 
ATOM   1477 N N   . ASN A 1 192 ? -1.606 12.350  20.724  1.00 64.29  ?  415 ASN B N   1 
ATOM   1478 C CA  . ASN A 1 192 ? -0.521 12.956  21.483  1.00 59.83  ?  415 ASN B CA  1 
ATOM   1479 C C   . ASN A 1 192 ? -1.069 13.659  22.720  1.00 59.11  ?  415 ASN B C   1 
ATOM   1480 O O   . ASN A 1 192 ? -2.156 14.243  22.692  1.00 61.57  ?  415 ASN B O   1 
ATOM   1481 C CB  . ASN A 1 192 ? 0.250  13.946  20.611  1.00 54.69  ?  415 ASN B CB  1 
ATOM   1482 C CG  . ASN A 1 192 ? 1.031  13.262  19.501  1.00 51.31  ?  415 ASN B CG  1 
ATOM   1483 O OD1 . ASN A 1 192 ? 1.260  12.053  19.538  1.00 48.48  ?  415 ASN B OD1 1 
ATOM   1484 N ND2 . ASN A 1 192 ? 1.445  14.038  18.506  1.00 49.33  ?  415 ASN B ND2 1 
ATOM   1485 N N   . VAL A 1 193 ? -0.304 13.605  23.812  1.00 58.51  ?  416 VAL B N   1 
ATOM   1486 C CA  . VAL A 1 193 ? -0.734 14.144  25.095  1.00 58.62  ?  416 VAL B CA  1 
ATOM   1487 C C   . VAL A 1 193 ? 0.343  15.068  25.646  1.00 59.00  ?  416 VAL B C   1 
ATOM   1488 O O   . VAL A 1 193 ? 1.520  14.971  25.293  1.00 61.42  ?  416 VAL B O   1 
ATOM   1489 C CB  . VAL A 1 193 ? -1.052 13.028  26.114  1.00 54.00  ?  416 VAL B CB  1 
ATOM   1490 C CG1 . VAL A 1 193 ? -2.408 12.408  25.819  1.00 53.87  ?  416 VAL B CG1 1 
ATOM   1491 C CG2 . VAL A 1 193 ? 0.041  11.968  26.103  1.00 53.45  ?  416 VAL B CG2 1 
ATOM   1492 N N   . HIS A 1 194 ? -0.087 15.981  26.524  1.00 58.33  ?  417 HIS B N   1 
ATOM   1493 C CA  . HIS A 1 194 ? 0.804  16.895  27.241  1.00 53.76  ?  417 HIS B CA  1 
ATOM   1494 C C   . HIS A 1 194 ? 1.677  17.717  26.295  1.00 52.25  ?  417 HIS B C   1 
ATOM   1495 O O   . HIS A 1 194 ? 2.814  18.062  26.625  1.00 53.30  ?  417 HIS B O   1 
ATOM   1496 C CB  . HIS A 1 194 ? 1.682  16.142  28.248  1.00 59.30  ?  417 HIS B CB  1 
ATOM   1497 C CG  . HIS A 1 194 ? 0.920  15.194  29.123  1.00 61.25  ?  417 HIS B CG  1 
ATOM   1498 N ND1 . HIS A 1 194 ? 0.008  15.620  30.065  1.00 60.03  ?  417 HIS B ND1 1 
ATOM   1499 C CD2 . HIS A 1 194 ? 0.938  13.842  29.202  1.00 60.55  ?  417 HIS B CD2 1 
ATOM   1500 C CE1 . HIS A 1 194 ? -0.506 14.572  30.683  1.00 63.31  ?  417 HIS B CE1 1 
ATOM   1501 N NE2 . HIS A 1 194 ? 0.042  13.480  30.178  1.00 59.86  ?  417 HIS B NE2 1 
ATOM   1502 N N   . LEU A 1 195 ? 1.152  18.043  25.117  1.00 53.24  ?  418 LEU B N   1 
ATOM   1503 C CA  . LEU A 1 195 ? 1.925  18.797  24.141  1.00 54.88  ?  418 LEU B CA  1 
ATOM   1504 C C   . LEU A 1 195 ? 2.087  20.247  24.579  1.00 50.12  ?  418 LEU B C   1 
ATOM   1505 O O   . LEU A 1 195 ? 1.190  20.835  25.190  1.00 48.15  ?  418 LEU B O   1 
ATOM   1506 C CB  . LEU A 1 195 ? 1.246  18.748  22.771  1.00 47.59  ?  418 LEU B CB  1 
ATOM   1507 C CG  . LEU A 1 195 ? 1.103  17.391  22.081  1.00 55.72  ?  418 LEU B CG  1 
ATOM   1508 C CD1 . LEU A 1 195 ? 0.320  17.545  20.786  1.00 53.07  ?  418 LEU B CD1 1 
ATOM   1509 C CD2 . LEU A 1 195 ? 2.464  16.769  21.813  1.00 51.97  ?  418 LEU B CD2 1 
ATOM   1510 N N   . ALA A 1 196 ? 3.244  20.819  24.266  1.00 47.32  ?  419 ALA B N   1 
ATOM   1511 C CA  . ALA A 1 196 ? 3.409  22.255  24.398  1.00 43.69  ?  419 ALA B CA  1 
ATOM   1512 C C   . ALA A 1 196 ? 2.467  22.958  23.424  1.00 48.36  ?  419 ALA B C   1 
ATOM   1513 O O   . ALA A 1 196 ? 2.234  22.457  22.318  1.00 45.97  ?  419 ALA B O   1 
ATOM   1514 C CB  . ALA A 1 196 ? 4.858  22.662  24.126  1.00 45.17  ?  419 ALA B CB  1 
ATOM   1515 N N   . PRO A 1 197 ? 1.906  24.107  23.795  1.00 48.87  ?  420 PRO B N   1 
ATOM   1516 C CA  . PRO A 1 197 ? 0.900  24.746  22.941  1.00 46.71  ?  420 PRO B CA  1 
ATOM   1517 C C   . PRO A 1 197 ? 1.484  25.219  21.618  1.00 52.01  ?  420 PRO B C   1 
ATOM   1518 O O   . PRO A 1 197 ? 2.692  25.420  21.467  1.00 49.56  ?  420 PRO B O   1 
ATOM   1519 C CB  . PRO A 1 197 ? 0.419  25.931  23.785  1.00 48.09  ?  420 PRO B CB  1 
ATOM   1520 C CG  . PRO A 1 197 ? 1.553  26.214  24.717  1.00 50.05  ?  420 PRO B CG  1 
ATOM   1521 C CD  . PRO A 1 197 ? 2.166  24.879  25.022  1.00 43.85  ?  420 PRO B CD  1 
ATOM   1522 N N   . ALA A 1 198 ? 0.593  25.390  20.644  1.00 46.48  ?  421 ALA B N   1 
ATOM   1523 C CA  . ALA A 1 198 ? 0.978  25.978  19.372  1.00 47.27  ?  421 ALA B CA  1 
ATOM   1524 C C   . ALA A 1 198 ? 1.316  27.453  19.559  1.00 47.71  ?  421 ALA B C   1 
ATOM   1525 O O   . ALA A 1 198 ? 0.963  28.081  20.562  1.00 52.18  ?  421 ALA B O   1 
ATOM   1526 C CB  . ALA A 1 198 ? -0.138 25.814  18.341  1.00 38.99  ?  421 ALA B CB  1 
ATOM   1527 N N   . VAL A 1 199 ? 2.013  28.010  18.572  1.00 45.84  ?  422 VAL B N   1 
ATOM   1528 C CA  . VAL A 1 199 ? 2.523  29.373  18.645  1.00 40.85  ?  422 VAL B CA  1 
ATOM   1529 C C   . VAL A 1 199 ? 2.199  30.082  17.337  1.00 51.72  ?  422 VAL B C   1 
ATOM   1530 O O   . VAL A 1 199 ? 2.409  29.525  16.253  1.00 50.46  ?  422 VAL B O   1 
ATOM   1531 C CB  . VAL A 1 199 ? 4.039  29.393  18.921  1.00 42.42  ?  422 VAL B CB  1 
ATOM   1532 C CG1 . VAL A 1 199 ? 4.633  30.744  18.580  1.00 45.20  ?  422 VAL B CG1 1 
ATOM   1533 C CG2 . VAL A 1 199 ? 4.314  29.041  20.376  1.00 43.96  ?  422 VAL B CG2 1 
ATOM   1534 N N   . ALA A 1 200 ? 1.678  31.302  17.441  1.00 47.58  ?  423 ALA B N   1 
ATOM   1535 C CA  . ALA A 1 200 ? 1.337  32.110  16.280  1.00 50.28  ?  423 ALA B CA  1 
ATOM   1536 C C   . ALA A 1 200 ? 1.476  33.575  16.654  1.00 56.93  ?  423 ALA B C   1 
ATOM   1537 O O   . ALA A 1 200 ? 1.208  33.946  17.803  1.00 53.95  ?  423 ALA B O   1 
ATOM   1538 C CB  . ALA A 1 200 ? -0.089 31.821  15.787  1.00 50.57  ?  423 ALA B CB  1 
ATOM   1539 N N   . PRO A 1 201 ? 1.899  34.426  15.720  1.00 58.79  ?  424 PRO B N   1 
ATOM   1540 C CA  . PRO A 1 201 ? 1.970  35.865  16.013  1.00 54.17  ?  424 PRO B CA  1 
ATOM   1541 C C   . PRO A 1 201 ? 0.573  36.451  16.157  1.00 60.11  ?  424 PRO B C   1 
ATOM   1542 O O   . PRO A 1 201 ? -0.282 36.277  15.288  1.00 62.17  ?  424 PRO B O   1 
ATOM   1543 C CB  . PRO A 1 201 ? 2.707  36.442  14.800  1.00 56.62  ?  424 PRO B CB  1 
ATOM   1544 C CG  . PRO A 1 201 ? 2.449  35.461  13.700  1.00 51.80  ?  424 PRO B CG  1 
ATOM   1545 C CD  . PRO A 1 201 ? 2.362  34.111  14.356  1.00 52.58  ?  424 PRO B CD  1 
ATOM   1546 N N   . THR A 1 202 ? 0.347  37.147  17.270  1.00 66.34  ?  425 THR B N   1 
ATOM   1547 C CA  . THR A 1 202 ? -0.962 37.708  17.578  1.00 65.12  ?  425 THR B CA  1 
ATOM   1548 C C   . THR A 1 202 ? -1.072 39.195  17.268  1.00 67.38  ?  425 THR B C   1 
ATOM   1549 O O   . THR A 1 202 ? -2.148 39.651  16.869  1.00 69.00  ?  425 THR B O   1 
ATOM   1550 C CB  . THR A 1 202 ? -1.305 37.477  19.054  1.00 67.86  ?  425 THR B CB  1 
ATOM   1551 O OG1 . THR A 1 202 ? -0.191 37.863  19.871  1.00 64.84  ?  425 THR B OG1 1 
ATOM   1552 C CG2 . THR A 1 202 ? -1.619 36.010  19.300  1.00 60.71  ?  425 THR B CG2 1 
ATOM   1553 N N   . PHE A 1 203 ? 0.003  39.956  17.444  1.00 64.30  ?  426 PHE B N   1 
ATOM   1554 C CA  . PHE A 1 203 ? -0.046 41.381  17.154  1.00 64.01  ?  426 PHE B CA  1 
ATOM   1555 C C   . PHE A 1 203 ? -0.173 41.604  15.648  1.00 67.94  ?  426 PHE B C   1 
ATOM   1556 O O   . PHE A 1 203 ? 0.504  40.935  14.861  1.00 69.70  ?  426 PHE B O   1 
ATOM   1557 C CB  . PHE A 1 203 ? 1.208  42.075  17.690  1.00 64.57  ?  426 PHE B CB  1 
ATOM   1558 C CG  . PHE A 1 203 ? 1.083  43.572  17.796  1.00 64.76  ?  426 PHE B CG  1 
ATOM   1559 C CD1 . PHE A 1 203 ? 1.415  44.386  16.724  1.00 67.16  ?  426 PHE B CD1 1 
ATOM   1560 C CD2 . PHE A 1 203 ? 0.648  44.165  18.969  1.00 65.83  ?  426 PHE B CD2 1 
ATOM   1561 C CE1 . PHE A 1 203 ? 1.303  45.762  16.818  1.00 60.69  ?  426 PHE B CE1 1 
ATOM   1562 C CE2 . PHE A 1 203 ? 0.535  45.541  19.070  1.00 62.97  ?  426 PHE B CE2 1 
ATOM   1563 C CZ  . PHE A 1 203 ? 0.864  46.338  17.993  1.00 63.32  ?  426 PHE B CZ  1 
ATOM   1564 N N   . PRO A 1 204 ? -1.036 42.526  15.216  1.00 71.59  ?  427 PRO B N   1 
ATOM   1565 C CA  . PRO A 1 204 ? -1.199 42.766  13.773  1.00 70.02  ?  427 PRO B CA  1 
ATOM   1566 C C   . PRO A 1 204 ? 0.067  43.358  13.170  1.00 65.62  ?  427 PRO B C   1 
ATOM   1567 O O   . PRO A 1 204 ? 0.650  44.299  13.710  1.00 67.35  ?  427 PRO B O   1 
ATOM   1568 C CB  . PRO A 1 204 ? -2.374 43.748  13.695  1.00 71.67  ?  427 PRO B CB  1 
ATOM   1569 C CG  . PRO A 1 204 ? -2.550 44.298  15.062  1.00 75.22  ?  427 PRO B CG  1 
ATOM   1570 C CD  . PRO A 1 204 ? -1.897 43.385  16.046  1.00 73.14  ?  427 PRO B CD  1 
ATOM   1571 N N   . GLY A 1 205 ? 0.486  42.795  12.039  1.00 61.11  ?  428 GLY B N   1 
ATOM   1572 C CA  . GLY A 1 205 ? 1.708  43.220  11.394  1.00 59.53  ?  428 GLY B CA  1 
ATOM   1573 C C   . GLY A 1 205 ? 2.966  42.580  11.930  1.00 60.08  ?  428 GLY B C   1 
ATOM   1574 O O   . GLY A 1 205 ? 4.066  43.006  11.559  1.00 54.71  ?  428 GLY B O   1 
ATOM   1575 N N   . GLU A 1 206 ? 2.841  41.570  12.787  1.00 58.36  ?  429 GLU B N   1 
ATOM   1576 C CA  . GLU A 1 206 ? 3.982  40.901  13.389  1.00 53.64  ?  429 GLU B CA  1 
ATOM   1577 C C   . GLU A 1 206 ? 4.101  39.475  12.864  1.00 49.01  ?  429 GLU B C   1 
ATOM   1578 O O   . GLU A 1 206 ? 3.107  38.844  12.492  1.00 47.21  ?  429 GLU B O   1 
ATOM   1579 C CB  . GLU A 1 206 ? 3.873  40.884  14.917  1.00 52.01  ?  429 GLU B CB  1 
ATOM   1580 C CG  . GLU A 1 206 ? 4.352  42.166  15.582  1.00 54.72  ?  429 GLU B CG  1 
ATOM   1581 C CD  . GLU A 1 206 ? 4.516  42.026  17.084  1.00 57.30  ?  429 GLU B CD  1 
ATOM   1582 O OE1 . GLU A 1 206 ? 4.301  40.915  17.611  1.00 53.53  ?  429 GLU B OE1 1 
ATOM   1583 O OE2 . GLU A 1 206 ? 4.854  43.035  17.739  1.00 54.19  ?  429 GLU B OE2 1 
ATOM   1584 N N   . GLN A 1 207 ? 5.335  38.978  12.841  1.00 43.60  ?  430 GLN B N   1 
ATOM   1585 C CA  . GLN A 1 207 ? 5.627  37.629  12.381  1.00 46.14  ?  430 GLN B CA  1 
ATOM   1586 C C   . GLN A 1 207 ? 6.610  36.977  13.340  1.00 46.84  ?  430 GLN B C   1 
ATOM   1587 O O   . GLN A 1 207 ? 7.369  37.654  14.039  1.00 40.80  ?  430 GLN B O   1 
ATOM   1588 C CB  . GLN A 1 207 ? 6.200  37.628  10.957  1.00 46.23  ?  430 GLN B CB  1 
ATOM   1589 C CG  . GLN A 1 207 ? 5.174  37.359  9.870   1.00 46.16  ?  430 GLN B CG  1 
ATOM   1590 C CD  . GLN A 1 207 ? 5.658  37.784  8.499   1.00 50.15  ?  430 GLN B CD  1 
ATOM   1591 O OE1 . GLN A 1 207 ? 4.888  37.816  7.539   1.00 54.42  ?  430 GLN B OE1 1 
ATOM   1592 N NE2 . GLN A 1 207 ? 6.941  38.115  8.400   1.00 47.78  ?  430 GLN B NE2 1 
ATOM   1593 N N   . LEU A 1 208 ? 6.589  35.647  13.365  1.00 44.35  ?  431 LEU B N   1 
ATOM   1594 C CA  . LEU A 1 208 ? 7.523  34.901  14.194  1.00 36.45  ?  431 LEU B CA  1 
ATOM   1595 C C   . LEU A 1 208 ? 8.949  35.093  13.694  1.00 40.27  ?  431 LEU B C   1 
ATOM   1596 O O   . LEU A 1 208 ? 9.193  35.194  12.487  1.00 43.51  ?  431 LEU B O   1 
ATOM   1597 C CB  . LEU A 1 208 ? 7.169  33.415  14.192  1.00 39.67  ?  431 LEU B CB  1 
ATOM   1598 C CG  . LEU A 1 208 ? 5.872  32.998  14.886  1.00 44.67  ?  431 LEU B CG  1 
ATOM   1599 C CD1 . LEU A 1 208 ? 5.596  31.520  14.664  1.00 42.84  ?  431 LEU B CD1 1 
ATOM   1600 C CD2 . LEU A 1 208 ? 5.936  33.319  16.369  1.00 45.53  ?  431 LEU B CD2 1 
ATOM   1601 N N   . LEU A 1 209 ? 9.893  35.149  14.629  1.00 40.65  ?  432 LEU B N   1 
ATOM   1602 C CA  . LEU A 1 209 ? 11.314 35.165  14.304  1.00 43.33  ?  432 LEU B CA  1 
ATOM   1603 C C   . LEU A 1 209 ? 11.871 33.774  14.585  1.00 46.75  ?  432 LEU B C   1 
ATOM   1604 O O   . LEU A 1 209 ? 11.889 33.323  15.736  1.00 37.66  ?  432 LEU B O   1 
ATOM   1605 C CB  . LEU A 1 209 ? 12.063 36.226  15.104  1.00 37.26  ?  432 LEU B CB  1 
ATOM   1606 C CG  . LEU A 1 209 ? 13.522 36.412  14.677  1.00 36.12  ?  432 LEU B CG  1 
ATOM   1607 C CD1 . LEU A 1 209 ? 13.601 36.929  13.247  1.00 36.91  ?  432 LEU B CD1 1 
ATOM   1608 C CD2 . LEU A 1 209 ? 14.257 37.343  15.628  1.00 39.04  ?  432 LEU B CD2 1 
ATOM   1609 N N   . PHE A 1 210 ? 12.321 33.097  13.533  1.00 42.40  ?  433 PHE B N   1 
ATOM   1610 C CA  . PHE A 1 210 ? 12.813 31.733  13.629  1.00 42.24  ?  433 PHE B CA  1 
ATOM   1611 C C   . PHE A 1 210 ? 14.332 31.723  13.704  1.00 41.52  ?  433 PHE B C   1 
ATOM   1612 O O   . PHE A 1 210 ? 15.004 32.552  13.081  1.00 41.00  ?  433 PHE B O   1 
ATOM   1613 C CB  . PHE A 1 210 ? 12.349 30.902  12.431  1.00 44.03  ?  433 PHE B CB  1 
ATOM   1614 C CG  . PHE A 1 210 ? 10.856 30.773  12.323  1.00 45.79  ?  433 PHE B CG  1 
ATOM   1615 C CD1 . PHE A 1 210 ? 10.160 29.906  13.150  1.00 43.87  ?  433 PHE B CD1 1 
ATOM   1616 C CD2 . PHE A 1 210 ? 10.148 31.513  11.388  1.00 38.41  ?  433 PHE B CD2 1 
ATOM   1617 C CE1 . PHE A 1 210 ? 8.788  29.781  13.052  1.00 44.21  ?  433 PHE B CE1 1 
ATOM   1618 C CE2 . PHE A 1 210 ? 8.775  31.395  11.286  1.00 36.48  ?  433 PHE B CE2 1 
ATOM   1619 C CZ  . PHE A 1 210 ? 8.095  30.527  12.117  1.00 43.60  ?  433 PHE B CZ  1 
ATOM   1620 N N   . PHE A 1 211 ? 14.866 30.781  14.474  1.00 36.73  ?  434 PHE B N   1 
ATOM   1621 C CA  . PHE A 1 211 ? 16.299 30.519  14.527  1.00 35.07  ?  434 PHE B CA  1 
ATOM   1622 C C   . PHE A 1 211 ? 16.564 29.318  13.624  1.00 35.15  ?  434 PHE B C   1 
ATOM   1623 O O   . PHE A 1 211 ? 16.225 28.183  13.970  1.00 31.82  ?  434 PHE B O   1 
ATOM   1624 C CB  . PHE A 1 211 ? 16.750 30.273  15.966  1.00 36.07  ?  434 PHE B CB  1 
ATOM   1625 C CG  . PHE A 1 211 ? 16.460 31.427  16.895  1.00 40.23  ?  434 PHE B CG  1 
ATOM   1626 C CD1 . PHE A 1 211 ? 15.212 31.573  17.480  1.00 36.33  ?  434 PHE B CD1 1 
ATOM   1627 C CD2 . PHE A 1 211 ? 17.436 32.370  17.173  1.00 35.47  ?  434 PHE B CD2 1 
ATOM   1628 C CE1 . PHE A 1 211 ? 14.944 32.637  18.325  1.00 37.28  ?  434 PHE B CE1 1 
ATOM   1629 C CE2 . PHE A 1 211 ? 17.176 33.437  18.019  1.00 36.85  ?  434 PHE B CE2 1 
ATOM   1630 C CZ  . PHE A 1 211 ? 15.927 33.570  18.597  1.00 33.31  ?  434 PHE B CZ  1 
ATOM   1631 N N   . ARG A 1 212 ? 17.157 29.575  12.461  1.00 35.94  ?  435 ARG B N   1 
ATOM   1632 C CA  . ARG A 1 212 ? 17.140 28.634  11.349  1.00 35.29  ?  435 ARG B CA  1 
ATOM   1633 C C   . ARG A 1 212 ? 18.481 27.930  11.185  1.00 34.05  ?  435 ARG B C   1 
ATOM   1634 O O   . ARG A 1 212 ? 19.542 28.558  11.265  1.00 30.30  ?  435 ARG B O   1 
ATOM   1635 C CB  . ARG A 1 212 ? 16.774 29.362  10.052  1.00 32.60  ?  435 ARG B CB  1 
ATOM   1636 C CG  . ARG A 1 212 ? 17.118 28.613  8.776   1.00 41.28  ?  435 ARG B CG  1 
ATOM   1637 C CD  . ARG A 1 212 ? 16.258 29.096  7.620   1.00 42.16  ?  435 ARG B CD  1 
ATOM   1638 N NE  . ARG A 1 212 ? 14.851 28.780  7.828   1.00 44.57  ?  435 ARG B NE  1 
ATOM   1639 C CZ  . ARG A 1 212 ? 13.907 28.906  6.905   1.00 45.56  ?  435 ARG B CZ  1 
ATOM   1640 N NH1 . ARG A 1 212 ? 14.186 29.348  5.690   1.00 41.53  ?  435 ARG B NH1 1 
ATOM   1641 N NH2 . ARG A 1 212 ? 12.655 28.581  7.209   1.00 42.59  ?  435 ARG B NH2 1 
ATOM   1642 N N   . SER A 1 213 ? 18.419 26.619  10.958  1.00 30.34  ?  436 SER B N   1 
ATOM   1643 C CA  . SER A 1 213 ? 19.570 25.815  10.573  1.00 32.47  ?  436 SER B CA  1 
ATOM   1644 C C   . SER A 1 213 ? 19.230 25.038  9.306   1.00 38.62  ?  436 SER B C   1 
ATOM   1645 O O   . SER A 1 213 ? 18.074 24.982  8.873   1.00 33.13  ?  436 SER B O   1 
ATOM   1646 C CB  . SER A 1 213 ? 19.988 24.853  11.693  1.00 37.01  ?  436 SER B CB  1 
ATOM   1647 O OG  . SER A 1 213 ? 20.351 25.555  12.867  1.00 40.28  ?  436 SER B OG  1 
ATOM   1648 N N   . THR A 1 214 ? 20.254 24.438  8.704   1.00 35.73  ?  437 THR B N   1 
ATOM   1649 C CA  . THR A 1 214 ? 20.092 23.575  7.537   1.00 41.82  ?  437 THR B CA  1 
ATOM   1650 C C   . THR A 1 214 ? 20.550 22.174  7.924   1.00 37.54  ?  437 THR B C   1 
ATOM   1651 O O   . THR A 1 214 ? 21.746 21.942  8.132   1.00 37.68  ?  437 THR B O   1 
ATOM   1652 C CB  . THR A 1 214 ? 20.881 24.101  6.337   1.00 43.84  ?  437 THR B CB  1 
ATOM   1653 O OG1 . THR A 1 214 ? 20.301 25.331  5.881   1.00 45.85  ?  437 THR B OG1 1 
ATOM   1654 C CG2 . THR A 1 214 ? 20.860 23.094  5.196   1.00 45.28  ?  437 THR B CG2 1 
ATOM   1655 N N   . MET A 1 215 ? 19.600 21.251  8.034   1.00 38.74  ?  438 MET B N   1 
ATOM   1656 C CA  . MET A 1 215 ? 19.941 19.875  8.356   1.00 37.85  ?  438 MET B CA  1 
ATOM   1657 C C   . MET A 1 215 ? 20.778 19.272  7.230   1.00 41.58  ?  438 MET B C   1 
ATOM   1658 O O   . MET A 1 215 ? 20.517 19.542  6.051   1.00 40.58  ?  438 MET B O   1 
ATOM   1659 C CB  . MET A 1 215 ? 18.679 19.037  8.568   1.00 38.44  ?  438 MET B CB  1 
ATOM   1660 C CG  . MET A 1 215 ? 17.862 19.418  9.789   1.00 41.81  ?  438 MET B CG  1 
ATOM   1661 S SD  . MET A 1 215 ? 16.446 18.324  10.026  1.00 48.54  ?  438 MET B SD  1 
ATOM   1662 C CE  . MET A 1 215 ? 15.344 18.906  8.741   1.00 40.73  ?  438 MET B CE  1 
ATOM   1663 N N   . PRO A 1 216 ? 21.790 18.468  7.550   1.00 42.13  ?  439 PRO B N   1 
ATOM   1664 C CA  . PRO A 1 216 ? 22.536 17.779  6.492   1.00 36.80  ?  439 PRO B CA  1 
ATOM   1665 C C   . PRO A 1 216 ? 21.633 16.812  5.740   1.00 38.99  ?  439 PRO B C   1 
ATOM   1666 O O   . PRO A 1 216 ? 20.773 16.154  6.327   1.00 34.94  ?  439 PRO B O   1 
ATOM   1667 C CB  . PRO A 1 216 ? 23.643 17.040  7.254   1.00 37.59  ?  439 PRO B CB  1 
ATOM   1668 C CG  . PRO A 1 216 ? 23.715 17.709  8.596   1.00 36.60  ?  439 PRO B CG  1 
ATOM   1669 C CD  . PRO A 1 216 ? 22.329 18.185  8.891   1.00 38.23  ?  439 PRO B CD  1 
ATOM   1670 N N   . GLY A 1 217 ? 21.827 16.745  4.426   1.00 39.02  ?  440 GLY B N   1 
ATOM   1671 C CA  . GLY A 1 217 ? 21.105 15.808  3.583   1.00 33.26  ?  440 GLY B CA  1 
ATOM   1672 C C   . GLY A 1 217 ? 21.960 14.589  3.288   1.00 38.24  ?  440 GLY B C   1 
ATOM   1673 O O   . GLY A 1 217 ? 23.155 14.707  3.017   1.00 40.95  ?  440 GLY B O   1 
ATOM   1674 N N   . CYS A 1 218 ? 21.331 13.412  3.341   1.00 33.99  ?  441 CYS B N   1 
ATOM   1675 C CA  . CYS A 1 218 ? 22.035 12.155  3.133   1.00 40.08  ?  441 CYS B CA  1 
ATOM   1676 C C   . CYS A 1 218 ? 21.646 11.431  1.852   1.00 41.48  ?  441 CYS B C   1 
ATOM   1677 O O   . CYS A 1 218 ? 22.419 10.588  1.386   1.00 44.56  ?  441 CYS B O   1 
ATOM   1678 C CB  . CYS A 1 218 ? 21.804 11.207  4.319   1.00 36.06  ?  441 CYS B CB  1 
ATOM   1679 S SG  . CYS A 1 218 ? 22.373 11.836  5.914   1.00 44.87  ?  441 CYS B SG  1 
ATOM   1680 N N   . SER A 1 219 ? 20.481 11.731  1.279   1.00 40.89  ?  442 SER B N   1 
ATOM   1681 C CA  . SER A 1 219 ? 20.041 11.092  0.048   1.00 38.45  ?  442 SER B CA  1 
ATOM   1682 C C   . SER A 1 219 ? 18.811 11.819  -0.473  1.00 38.28  ?  442 SER B C   1 
ATOM   1683 O O   . SER A 1 219 ? 17.927 12.181  0.306   1.00 38.96  ?  442 SER B O   1 
ATOM   1684 C CB  . SER A 1 219 ? 19.722 9.605   0.268   1.00 43.11  ?  442 SER B CB  1 
ATOM   1685 O OG  . SER A 1 219 ? 19.137 9.028   -0.886  1.00 51.02  ?  442 SER B OG  1 
ATOM   1686 N N   . GLY A 1 220 ? 18.764 12.029  -1.788  1.00 40.45  ?  443 GLY B N   1 
ATOM   1687 C CA  . GLY A 1 220 ? 17.584 12.609  -2.402  1.00 41.14  ?  443 GLY B CA  1 
ATOM   1688 C C   . GLY A 1 220 ? 17.584 14.129  -2.359  1.00 41.18  ?  443 GLY B C   1 
ATOM   1689 O O   . GLY A 1 220 ? 18.629 14.783  -2.323  1.00 40.39  ?  443 GLY B O   1 
ATOM   1690 N N   . TYR A 1 221 ? 16.377 14.697  -2.364  1.00 34.96  ?  444 TYR B N   1 
ATOM   1691 C CA  . TYR A 1 221 ? 16.169 16.144  -2.381  1.00 40.87  ?  444 TYR B CA  1 
ATOM   1692 C C   . TYR A 1 221 ? 15.310 16.535  -1.183  1.00 40.90  ?  444 TYR B C   1 
ATOM   1693 O O   . TYR A 1 221 ? 14.134 16.892  -1.336  1.00 40.54  ?  444 TYR B O   1 
ATOM   1694 C CB  . TYR A 1 221 ? 15.511 16.593  -3.687  1.00 43.33  ?  444 TYR B CB  1 
ATOM   1695 C CG  . TYR A 1 221 ? 16.307 16.286  -4.940  1.00 41.63  ?  444 TYR B CG  1 
ATOM   1696 C CD1 . TYR A 1 221 ? 16.442 14.981  -5.403  1.00 41.03  ?  444 TYR B CD1 1 
ATOM   1697 C CD2 . TYR A 1 221 ? 16.911 17.303  -5.669  1.00 44.98  ?  444 TYR B CD2 1 
ATOM   1698 C CE1 . TYR A 1 221 ? 17.164 14.697  -6.548  1.00 44.77  ?  444 TYR B CE1 1 
ATOM   1699 C CE2 . TYR A 1 221 ? 17.635 17.029  -6.820  1.00 42.03  ?  444 TYR B CE2 1 
ATOM   1700 C CZ  . TYR A 1 221 ? 17.758 15.724  -7.254  1.00 48.76  ?  444 TYR B CZ  1 
ATOM   1701 O OH  . TYR A 1 221 ? 18.476 15.443  -8.395  1.00 49.31  ?  444 TYR B OH  1 
ATOM   1702 N N   . PRO A 1 222 ? 15.866 16.484  0.024   1.00 37.93  ?  445 PRO B N   1 
ATOM   1703 C CA  . PRO A 1 222 ? 15.065 16.777  1.213   1.00 40.80  ?  445 PRO B CA  1 
ATOM   1704 C C   . PRO A 1 222 ? 14.935 18.267  1.477   1.00 39.89  ?  445 PRO B C   1 
ATOM   1705 O O   . PRO A 1 222 ? 15.794 19.072  1.108   1.00 36.67  ?  445 PRO B O   1 
ATOM   1706 C CB  . PRO A 1 222 ? 15.847 16.090  2.338   1.00 34.88  ?  445 PRO B CB  1 
ATOM   1707 C CG  . PRO A 1 222 ? 17.267 16.172  1.886   1.00 36.76  ?  445 PRO B CG  1 
ATOM   1708 C CD  . PRO A 1 222 ? 17.259 16.143  0.370   1.00 38.91  ?  445 PRO B CD  1 
ATOM   1709 N N   . ASN A 1 223 ? 13.826 18.626  2.118   1.00 40.30  ?  446 ASN B N   1 
ATOM   1710 C CA  . ASN A 1 223 ? 13.632 19.973  2.649   1.00 45.44  ?  446 ASN B CA  1 
ATOM   1711 C C   . ASN A 1 223 ? 14.431 20.068  3.940   1.00 40.70  ?  446 ASN B C   1 
ATOM   1712 O O   . ASN A 1 223 ? 14.005 19.573  4.986   1.00 43.10  ?  446 ASN B O   1 
ATOM   1713 C CB  . ASN A 1 223 ? 12.152 20.255  2.879   1.00 44.79  ?  446 ASN B CB  1 
ATOM   1714 C CG  . ASN A 1 223 ? 11.882 21.698  3.272   1.00 45.10  ?  446 ASN B CG  1 
ATOM   1715 O OD1 . ASN A 1 223 ? 12.804 22.461  3.556   1.00 44.43  ?  446 ASN B OD1 1 
ATOM   1716 N ND2 . ASN A 1 223 ? 10.609 22.077  3.289   1.00 44.49  ?  446 ASN B ND2 1 
ATOM   1717 N N   . MET A 1 224 ? 15.596 20.705  3.874   1.00 40.39  ?  447 MET B N   1 
ATOM   1718 C CA  . MET A 1 224 ? 16.529 20.725  4.991   1.00 43.29  ?  447 MET B CA  1 
ATOM   1719 C C   . MET A 1 224 ? 16.349 21.934  5.904   1.00 44.19  ?  447 MET B C   1 
ATOM   1720 O O   . MET A 1 224 ? 17.153 22.125  6.821   1.00 42.22  ?  447 MET B O   1 
ATOM   1721 C CB  . MET A 1 224 ? 17.964 20.669  4.465   1.00 40.47  ?  447 MET B CB  1 
ATOM   1722 C CG  . MET A 1 224 ? 18.234 19.455  3.580   1.00 40.09  ?  447 MET B CG  1 
ATOM   1723 S SD  . MET A 1 224 ? 19.878 19.464  2.842   1.00 44.81  ?  447 MET B SD  1 
ATOM   1724 C CE  . MET A 1 224 ? 19.488 20.098  1.215   1.00 36.76  ?  447 MET B CE  1 
ATOM   1725 N N   . ASP A 1 225 ? 15.317 22.746  5.680   1.00 42.22  ?  448 ASP B N   1 
ATOM   1726 C CA  . ASP A 1 225 ? 15.049 23.873  6.564   1.00 42.30  ?  448 ASP B CA  1 
ATOM   1727 C C   . ASP A 1 225 ? 14.562 23.372  7.917   1.00 42.74  ?  448 ASP B C   1 
ATOM   1728 O O   . ASP A 1 225 ? 13.687 22.504  7.992   1.00 45.54  ?  448 ASP B O   1 
ATOM   1729 C CB  . ASP A 1 225 ? 14.008 24.805  5.944   1.00 45.73  ?  448 ASP B CB  1 
ATOM   1730 C CG  . ASP A 1 225 ? 14.554 25.599  4.773   1.00 49.49  ?  448 ASP B CG  1 
ATOM   1731 O OD1 . ASP A 1 225 ? 15.791 25.722  4.657   1.00 47.95  ?  448 ASP B OD1 1 
ATOM   1732 O OD2 . ASP A 1 225 ? 13.742 26.106  3.969   1.00 52.92  ?  448 ASP B OD2 1 
ATOM   1733 N N   . LEU A 1 226 ? 15.133 23.915  8.992   1.00 39.45  ?  449 LEU B N   1 
ATOM   1734 C CA  . LEU A 1 226 ? 14.700 23.581  10.347  1.00 42.57  ?  449 LEU B CA  1 
ATOM   1735 C C   . LEU A 1 226 ? 14.700 24.852  11.181  1.00 38.04  ?  449 LEU B C   1 
ATOM   1736 O O   . LEU A 1 226 ? 15.762 25.421  11.452  1.00 37.41  ?  449 LEU B O   1 
ATOM   1737 C CB  . LEU A 1 226 ? 15.596 22.522  10.982  1.00 32.92  ?  449 LEU B CB  1 
ATOM   1738 C CG  . LEU A 1 226 ? 15.062 22.073  12.343  1.00 40.42  ?  449 LEU B CG  1 
ATOM   1739 C CD1 . LEU A 1 226 ? 13.774 21.279  12.178  1.00 38.43  ?  449 LEU B CD1 1 
ATOM   1740 C CD2 . LEU A 1 226 ? 16.105 21.275  13.092  1.00 35.86  ?  449 LEU B CD2 1 
ATOM   1741 N N   . ASP A 1 227 ? 13.514 25.286  11.594  1.00 38.37  ?  450 ASP B N   1 
ATOM   1742 C CA  . ASP A 1 227 ? 13.342 26.486  12.398  1.00 38.35  ?  450 ASP B CA  1 
ATOM   1743 C C   . ASP A 1 227 ? 12.967 26.094  13.820  1.00 40.23  ?  450 ASP B C   1 
ATOM   1744 O O   . ASP A 1 227 ? 12.086 25.253  14.023  1.00 34.18  ?  450 ASP B O   1 
ATOM   1745 C CB  . ASP A 1 227 ? 12.263 27.392  11.799  1.00 38.96  ?  450 ASP B CB  1 
ATOM   1746 C CG  . ASP A 1 227 ? 12.570 27.803  10.372  1.00 42.04  ?  450 ASP B CG  1 
ATOM   1747 O OD1 . ASP A 1 227 ? 13.588 28.491  10.155  1.00 44.12  ?  450 ASP B OD1 1 
ATOM   1748 O OD2 . ASP A 1 227 ? 11.789 27.441  9.466   1.00 48.86  ?  450 ASP B OD2 1 
ATOM   1749 N N   . CYS A 1 228 ? 13.638 26.698  14.796  1.00 35.34  ?  451 CYS B N   1 
ATOM   1750 C CA  . CYS A 1 228 ? 13.314 26.503  16.200  1.00 40.65  ?  451 CYS B CA  1 
ATOM   1751 C C   . CYS A 1 228 ? 12.928 27.839  16.818  1.00 37.98  ?  451 CYS B C   1 
ATOM   1752 O O   . CYS A 1 228 ? 13.357 28.903  16.358  1.00 38.78  ?  451 CYS B O   1 
ATOM   1753 C CB  . CYS A 1 228 ? 14.484 25.867  16.967  1.00 39.45  ?  451 CYS B CB  1 
ATOM   1754 S SG  . CYS A 1 228 ? 15.922 26.932  17.229  1.00 41.18  ?  451 CYS B SG  1 
ATOM   1755 N N   . LEU A 1 229 ? 12.098 27.774  17.862  1.00 38.19  ?  452 LEU B N   1 
ATOM   1756 C CA  . LEU A 1 229 ? 11.575 28.989  18.477  1.00 36.45  ?  452 LEU B CA  1 
ATOM   1757 C C   . LEU A 1 229 ? 12.584 29.644  19.408  1.00 38.21  ?  452 LEU B C   1 
ATOM   1758 O O   . LEU A 1 229 ? 12.550 30.866  19.589  1.00 41.29  ?  452 LEU B O   1 
ATOM   1759 C CB  . LEU A 1 229 ? 10.282 28.678  19.233  1.00 32.65  ?  452 LEU B CB  1 
ATOM   1760 C CG  . LEU A 1 229 ? 9.167  28.042  18.398  1.00 41.73  ?  452 LEU B CG  1 
ATOM   1761 C CD1 . LEU A 1 229 ? 7.915  27.816  19.233  1.00 36.79  ?  452 LEU B CD1 1 
ATOM   1762 C CD2 . LEU A 1 229 ? 8.857  28.910  17.188  1.00 39.19  ?  452 LEU B CD2 1 
ATOM   1763 N N   . LEU A 1 230 ? 13.479 28.860  20.005  1.00 39.10  ?  453 LEU B N   1 
ATOM   1764 C CA  . LEU A 1 230 ? 14.495 29.364  20.912  1.00 40.86  ?  453 LEU B CA  1 
ATOM   1765 C C   . LEU A 1 230 ? 15.787 28.592  20.688  1.00 36.04  ?  453 LEU B C   1 
ATOM   1766 O O   . LEU A 1 230 ? 15.749 27.371  20.470  1.00 35.25  ?  453 LEU B O   1 
ATOM   1767 C CB  . LEU A 1 230 ? 14.070 29.229  22.382  1.00 33.85  ?  453 LEU B CB  1 
ATOM   1768 C CG  . LEU A 1 230 ? 12.821 29.974  22.859  1.00 38.46  ?  453 LEU B CG  1 
ATOM   1769 C CD1 . LEU A 1 230 ? 12.318 29.374  24.160  1.00 35.90  ?  453 LEU B CD1 1 
ATOM   1770 C CD2 . LEU A 1 230 ? 13.103 31.461  23.027  1.00 31.26  ?  453 LEU B CD2 1 
ATOM   1771 N N   . PRO A 1 231 ? 16.935 29.266  20.731  1.00 35.13  ?  454 PRO B N   1 
ATOM   1772 C CA  . PRO A 1 231 ? 18.209 28.540  20.718  1.00 32.96  ?  454 PRO B CA  1 
ATOM   1773 C C   . PRO A 1 231 ? 18.339 27.664  21.955  1.00 37.23  ?  454 PRO B C   1 
ATOM   1774 O O   . PRO A 1 231 ? 17.810 27.979  23.024  1.00 35.15  ?  454 PRO B O   1 
ATOM   1775 C CB  . PRO A 1 231 ? 19.260 29.658  20.712  1.00 36.42  ?  454 PRO B CB  1 
ATOM   1776 C CG  . PRO A 1 231 ? 18.527 30.887  20.266  1.00 34.91  ?  454 PRO B CG  1 
ATOM   1777 C CD  . PRO A 1 231 ? 17.123 30.725  20.756  1.00 33.20  ?  454 PRO B CD  1 
ATOM   1778 N N   . GLN A 1 232 ? 19.048 26.542  21.797  1.00 39.33  ?  455 GLN B N   1 
ATOM   1779 C CA  . GLN A 1 232 ? 19.202 25.604  22.905  1.00 34.11  ?  455 GLN B CA  1 
ATOM   1780 C C   . GLN A 1 232 ? 19.939 26.237  24.078  1.00 35.07  ?  455 GLN B C   1 
ATOM   1781 O O   . GLN A 1 232 ? 19.692 25.875  25.235  1.00 38.05  ?  455 GLN B O   1 
ATOM   1782 C CB  . GLN A 1 232 ? 19.931 24.346  22.434  1.00 31.67  ?  455 GLN B CB  1 
ATOM   1783 C CG  . GLN A 1 232 ? 20.072 23.268  23.496  1.00 31.91  ?  455 GLN B CG  1 
ATOM   1784 C CD  . GLN A 1 232 ? 18.734 22.691  23.928  1.00 40.40  ?  455 GLN B CD  1 
ATOM   1785 O OE1 . GLN A 1 232 ? 17.750 22.749  23.189  1.00 36.15  ?  455 GLN B OE1 1 
ATOM   1786 N NE2 . GLN A 1 232 ? 18.694 22.130  25.129  1.00 35.79  ?  455 GLN B NE2 1 
ATOM   1787 N N   . GLU A 1 233 ? 20.841 27.182  23.804  1.00 35.61  ?  456 GLU B N   1 
ATOM   1788 C CA  . GLU A 1 233 ? 21.535 27.875  24.883  1.00 39.04  ?  456 GLU B CA  1 
ATOM   1789 C C   . GLU A 1 233 ? 20.590 28.773  25.671  1.00 39.58  ?  456 GLU B C   1 
ATOM   1790 O O   . GLU A 1 233 ? 20.781 28.963  26.877  1.00 40.39  ?  456 GLU B O   1 
ATOM   1791 C CB  . GLU A 1 233 ? 22.703 28.684  24.316  1.00 33.75  ?  456 GLU B CB  1 
ATOM   1792 C CG  . GLU A 1 233 ? 23.940 27.847  24.011  1.00 44.91  ?  456 GLU B CG  1 
ATOM   1793 C CD  . GLU A 1 233 ? 23.808 27.031  22.733  1.00 47.61  ?  456 GLU B CD  1 
ATOM   1794 O OE1 . GLU A 1 233 ? 22.798 27.192  22.014  1.00 40.60  ?  456 GLU B OE1 1 
ATOM   1795 O OE2 . GLU A 1 233 ? 24.716 26.221  22.450  1.00 46.80  ?  456 GLU B OE2 1 
ATOM   1796 N N   . TRP A 1 234 ? 19.570 29.332  25.012  1.00 35.78  ?  457 TRP B N   1 
ATOM   1797 C CA  . TRP A 1 234 ? 18.569 30.112  25.732  1.00 38.54  ?  457 TRP B CA  1 
ATOM   1798 C C   . TRP A 1 234 ? 17.716 29.216  26.621  1.00 37.71  ?  457 TRP B C   1 
ATOM   1799 O O   . TRP A 1 234 ? 17.317 29.620  27.720  1.00 39.65  ?  457 TRP B O   1 
ATOM   1800 C CB  . TRP A 1 234 ? 17.687 30.882  24.749  1.00 34.78  ?  457 TRP B CB  1 
ATOM   1801 C CG  . TRP A 1 234 ? 18.376 32.031  24.069  1.00 39.73  ?  457 TRP B CG  1 
ATOM   1802 C CD1 . TRP A 1 234 ? 19.718 32.184  23.867  1.00 36.64  ?  457 TRP B CD1 1 
ATOM   1803 C CD2 . TRP A 1 234 ? 17.751 33.185  23.495  1.00 36.39  ?  457 TRP B CD2 1 
ATOM   1804 N NE1 . TRP A 1 234 ? 19.967 33.362  23.203  1.00 35.11  ?  457 TRP B NE1 1 
ATOM   1805 C CE2 . TRP A 1 234 ? 18.775 33.996  22.965  1.00 35.72  ?  457 TRP B CE2 1 
ATOM   1806 C CE3 . TRP A 1 234 ? 16.425 33.614  23.380  1.00 35.66  ?  457 TRP B CE3 1 
ATOM   1807 C CZ2 . TRP A 1 234 ? 18.514 35.210  22.330  1.00 34.62  ?  457 TRP B CZ2 1 
ATOM   1808 C CZ3 . TRP A 1 234 ? 16.167 34.820  22.747  1.00 36.98  ?  457 TRP B CZ3 1 
ATOM   1809 C CH2 . TRP A 1 234 ? 17.208 35.603  22.231  1.00 34.01  ?  457 TRP B CH2 1 
ATOM   1810 N N   . VAL A 1 235 ? 17.422 27.997  26.161  1.00 38.25  ?  458 VAL B N   1 
ATOM   1811 C CA  . VAL A 1 235 ? 16.691 27.046  26.992  1.00 35.11  ?  458 VAL B CA  1 
ATOM   1812 C C   . VAL A 1 235 ? 17.516 26.676  28.218  1.00 44.73  ?  458 VAL B C   1 
ATOM   1813 O O   . VAL A 1 235 ? 16.983 26.533  29.325  1.00 43.97  ?  458 VAL B O   1 
ATOM   1814 C CB  . VAL A 1 235 ? 16.305 25.802  26.170  1.00 39.29  ?  458 VAL B CB  1 
ATOM   1815 C CG1 . VAL A 1 235 ? 15.578 24.791  27.043  1.00 39.97  ?  458 VAL B CG1 1 
ATOM   1816 C CG2 . VAL A 1 235 ? 15.445 26.199  24.978  1.00 38.81  ?  458 VAL B CG2 1 
ATOM   1817 N N   . GLN A 1 236 ? 18.830 26.525  28.042  1.00 41.38  ?  459 GLN B N   1 
ATOM   1818 C CA  . GLN A 1 236 ? 19.699 26.246  29.179  1.00 43.84  ?  459 GLN B CA  1 
ATOM   1819 C C   . GLN A 1 236 ? 19.785 27.442  30.117  1.00 44.36  ?  459 GLN B C   1 
ATOM   1820 O O   . GLN A 1 236 ? 19.857 27.276  31.340  1.00 43.09  ?  459 GLN B O   1 
ATOM   1821 C CB  . GLN A 1 236 ? 21.092 25.854  28.691  1.00 39.86  ?  459 GLN B CB  1 
ATOM   1822 C CG  . GLN A 1 236 ? 21.218 24.410  28.253  1.00 40.53  ?  459 GLN B CG  1 
ATOM   1823 C CD  . GLN A 1 236 ? 22.545 24.130  27.583  1.00 41.25  ?  459 GLN B CD  1 
ATOM   1824 O OE1 . GLN A 1 236 ? 23.163 25.026  27.006  1.00 39.06  ?  459 GLN B OE1 1 
ATOM   1825 N NE2 . GLN A 1 236 ? 22.994 22.882  27.656  1.00 43.60  ?  459 GLN B NE2 1 
ATOM   1826 N N   . TYR A 1 237 ? 19.773 28.658  29.564  1.00 42.69  ?  460 TYR B N   1 
ATOM   1827 C CA  . TYR A 1 237 ? 19.943 29.854  30.385  1.00 44.22  ?  460 TYR B CA  1 
ATOM   1828 C C   . TYR A 1 237 ? 18.704 30.128  31.229  1.00 44.03  ?  460 TYR B C   1 
ATOM   1829 O O   . TYR A 1 237 ? 18.805 30.360  32.440  1.00 41.58  ?  460 TYR B O   1 
ATOM   1830 C CB  . TYR A 1 237 ? 20.268 31.055  29.497  1.00 45.04  ?  460 TYR B CB  1 
ATOM   1831 C CG  . TYR A 1 237 ? 20.847 32.237  30.244  1.00 49.91  ?  460 TYR B CG  1 
ATOM   1832 C CD1 . TYR A 1 237 ? 22.078 32.145  30.880  1.00 51.44  ?  460 TYR B CD1 1 
ATOM   1833 C CD2 . TYR A 1 237 ? 20.165 33.445  30.309  1.00 47.50  ?  460 TYR B CD2 1 
ATOM   1834 C CE1 . TYR A 1 237 ? 22.613 33.223  31.563  1.00 58.12  ?  460 TYR B CE1 1 
ATOM   1835 C CE2 . TYR A 1 237 ? 20.691 34.529  30.991  1.00 48.43  ?  460 TYR B CE2 1 
ATOM   1836 C CZ  . TYR A 1 237 ? 21.916 34.411  31.616  1.00 53.74  ?  460 TYR B CZ  1 
ATOM   1837 O OH  . TYR A 1 237 ? 22.444 35.485  32.295  1.00 62.14  ?  460 TYR B OH  1 
ATOM   1838 N N   . PHE A 1 238 ? 17.524 30.111  30.605  1.00 41.94  ?  461 PHE B N   1 
ATOM   1839 C CA  . PHE A 1 238 ? 16.294 30.384  31.342  1.00 42.74  ?  461 PHE B CA  1 
ATOM   1840 C C   . PHE A 1 238 ? 16.044 29.325  32.408  1.00 47.66  ?  461 PHE B C   1 
ATOM   1841 O O   . PHE A 1 238 ? 15.528 29.630  33.490  1.00 47.29  ?  461 PHE B O   1 
ATOM   1842 C CB  . PHE A 1 238 ? 15.108 30.466  30.378  1.00 41.47  ?  461 PHE B CB  1 
ATOM   1843 C CG  . PHE A 1 238 ? 15.260 31.517  29.311  1.00 42.20  ?  461 PHE B CG  1 
ATOM   1844 C CD1 . PHE A 1 238 ? 16.051 32.635  29.519  1.00 40.06  ?  461 PHE B CD1 1 
ATOM   1845 C CD2 . PHE A 1 238 ? 14.604 31.386  28.097  1.00 41.18  ?  461 PHE B CD2 1 
ATOM   1846 C CE1 . PHE A 1 238 ? 16.188 33.600  28.537  1.00 43.96  ?  461 PHE B CE1 1 
ATOM   1847 C CE2 . PHE A 1 238 ? 14.736 32.348  27.109  1.00 41.08  ?  461 PHE B CE2 1 
ATOM   1848 C CZ  . PHE A 1 238 ? 15.530 33.456  27.331  1.00 36.04  ?  461 PHE B CZ  1 
ATOM   1849 N N   . TYR A 1 239 ? 16.410 28.074  32.120  1.00 42.78  ?  462 TYR B N   1 
ATOM   1850 C CA  . TYR A 1 239 ? 16.212 26.994  33.083  1.00 43.42  ?  462 TYR B CA  1 
ATOM   1851 C C   . TYR A 1 239 ? 17.074 27.191  34.324  1.00 44.13  ?  462 TYR B C   1 
ATOM   1852 O O   . TYR A 1 239 ? 16.656 26.852  35.438  1.00 46.58  ?  462 TYR B O   1 
ATOM   1853 C CB  . TYR A 1 239 ? 16.519 25.652  32.418  1.00 46.84  ?  462 TYR B CB  1 
ATOM   1854 C CG  . TYR A 1 239 ? 16.504 24.459  33.348  1.00 51.17  ?  462 TYR B CG  1 
ATOM   1855 C CD1 . TYR A 1 239 ? 15.319 23.798  33.643  1.00 53.61  ?  462 TYR B CD1 1 
ATOM   1856 C CD2 . TYR A 1 239 ? 17.679 23.983  33.917  1.00 52.06  ?  462 TYR B CD2 1 
ATOM   1857 C CE1 . TYR A 1 239 ? 15.301 22.702  34.485  1.00 59.32  ?  462 TYR B CE1 1 
ATOM   1858 C CE2 . TYR A 1 239 ? 17.671 22.890  34.763  1.00 59.76  ?  462 TYR B CE2 1 
ATOM   1859 C CZ  . TYR A 1 239 ? 16.480 22.253  35.043  1.00 63.68  ?  462 TYR B CZ  1 
ATOM   1860 O OH  . TYR A 1 239 ? 16.470 21.163  35.883  1.00 71.62  ?  462 TYR B OH  1 
ATOM   1861 N N   . GLN A 1 240 ? 18.277 27.741  34.152  1.00 41.94  ?  463 GLN B N   1 
ATOM   1862 C CA  . GLN A 1 240 ? 19.180 27.937  35.279  1.00 45.49  ?  463 GLN B CA  1 
ATOM   1863 C C   . GLN A 1 240 ? 18.802 29.168  36.093  1.00 45.94  ?  463 GLN B C   1 
ATOM   1864 O O   . GLN A 1 240 ? 18.650 29.090  37.317  1.00 56.74  ?  463 GLN B O   1 
ATOM   1865 C CB  . GLN A 1 240 ? 20.619 28.057  34.781  1.00 42.47  ?  463 GLN B CB  1 
ATOM   1866 C CG  . GLN A 1 240 ? 21.194 26.768  34.235  1.00 45.74  ?  463 GLN B CG  1 
ATOM   1867 C CD  . GLN A 1 240 ? 22.608 26.947  33.732  1.00 49.22  ?  463 GLN B CD  1 
ATOM   1868 O OE1 . GLN A 1 240 ? 23.544 27.072  34.520  1.00 48.04  ?  463 GLN B OE1 1 
ATOM   1869 N NE2 . GLN A 1 240 ? 22.772 26.966  32.414  1.00 39.69  ?  463 GLN B NE2 1 
ATOM   1870 N N   . GLU A 1 241 ? 18.656 30.315  35.426  1.00 49.55  ?  464 GLU B N   1 
ATOM   1871 C CA  . GLU A 1 241 ? 18.343 31.551  36.133  1.00 51.09  ?  464 GLU B CA  1 
ATOM   1872 C C   . GLU A 1 241 ? 16.977 31.471  36.803  1.00 51.78  ?  464 GLU B C   1 
ATOM   1873 O O   . GLU A 1 241 ? 16.830 31.813  37.983  1.00 58.54  ?  464 GLU B O   1 
ATOM   1874 C CB  . GLU A 1 241 ? 18.404 32.734  35.167  1.00 46.71  ?  464 GLU B CB  1 
ATOM   1875 C CG  . GLU A 1 241 ? 19.773 32.947  34.546  1.00 50.98  ?  464 GLU B CG  1 
ATOM   1876 C CD  . GLU A 1 241 ? 20.704 33.736  35.447  1.00 57.66  ?  464 GLU B CD  1 
ATOM   1877 O OE1 . GLU A 1 241 ? 20.392 34.909  35.744  1.00 59.54  ?  464 GLU B OE1 1 
ATOM   1878 O OE2 . GLU A 1 241 ? 21.743 33.179  35.863  1.00 55.31  ?  464 GLU B OE2 1 
ATOM   1879 N N   . ALA A 1 242 ? 15.966 31.011  36.062  1.00 50.26  ?  465 ALA B N   1 
ATOM   1880 C CA  . ALA A 1 242 ? 14.587 30.946  36.553  1.00 50.54  ?  465 ALA B CA  1 
ATOM   1881 C C   . ALA A 1 242 ? 14.118 32.309  37.062  1.00 53.80  ?  465 ALA B C   1 
ATOM   1882 O O   . ALA A 1 242 ? 13.389 32.407  38.052  1.00 51.54  ?  465 ALA B O   1 
ATOM   1883 C CB  . ALA A 1 242 ? 14.427 29.870  37.632  1.00 48.08  ?  465 ALA B CB  1 
ATOM   1884 N N   . ALA A 1 243 ? 14.543 33.365  36.378  1.00 48.93  ?  466 ALA B N   1 
ATOM   1885 C CA  . ALA A 1 243 ? 14.163 34.713  36.777  1.00 51.38  ?  466 ALA B CA  1 
ATOM   1886 C C   . ALA A 1 243 ? 12.673 34.925  36.533  1.00 54.08  ?  466 ALA B C   1 
ATOM   1887 O O   . ALA A 1 243 ? 12.172 34.578  35.459  1.00 55.56  ?  466 ALA B O   1 
ATOM   1888 C CB  . ALA A 1 243 ? 14.978 35.749  36.006  1.00 48.44  ?  466 ALA B CB  1 
ATOM   1889 N N   . PRO A 1 244 ? 11.937 35.475  37.498  1.00 57.45  ?  467 PRO B N   1 
ATOM   1890 C CA  . PRO A 1 244 ? 10.503 35.704  37.285  1.00 55.88  ?  467 PRO B CA  1 
ATOM   1891 C C   . PRO A 1 244 ? 10.264 36.748  36.206  1.00 52.00  ?  467 PRO B C   1 
ATOM   1892 O O   . PRO A 1 244 ? 11.024 37.709  36.062  1.00 52.55  ?  467 PRO B O   1 
ATOM   1893 C CB  . PRO A 1 244 ? 10.008 36.191  38.654  1.00 50.46  ?  467 PRO B CB  1 
ATOM   1894 C CG  . PRO A 1 244 ? 11.085 35.801  39.628  1.00 54.64  ?  467 PRO B CG  1 
ATOM   1895 C CD  . PRO A 1 244 ? 12.364 35.850  38.855  1.00 55.17  ?  467 PRO B CD  1 
ATOM   1896 N N   . ALA A 1 245 ? 9.195  36.547  35.440  1.00 46.45  ?  468 ALA B N   1 
ATOM   1897 C CA  . ALA A 1 245 ? 8.813  37.468  34.379  1.00 56.90  ?  468 ALA B CA  1 
ATOM   1898 C C   . ALA A 1 245 ? 7.956  38.582  34.968  1.00 55.02  ?  468 ALA B C   1 
ATOM   1899 O O   . ALA A 1 245 ? 6.907  38.315  35.565  1.00 54.47  ?  468 ALA B O   1 
ATOM   1900 C CB  . ALA A 1 245 ? 8.060  36.739  33.267  1.00 49.39  ?  468 ALA B CB  1 
ATOM   1901 N N   . GLN A 1 246 ? 8.404  39.827  34.804  1.00 50.82  ?  469 GLN B N   1 
ATOM   1902 C CA  . GLN A 1 246 ? 7.664  40.972  35.318  1.00 54.86  ?  469 GLN B CA  1 
ATOM   1903 C C   . GLN A 1 246 ? 6.515  41.394  34.413  1.00 58.52  ?  469 GLN B C   1 
ATOM   1904 O O   . GLN A 1 246 ? 5.708  42.238  34.818  1.00 56.42  ?  469 GLN B O   1 
ATOM   1905 C CB  . GLN A 1 246 ? 8.609  42.158  35.534  1.00 56.74  ?  469 GLN B CB  1 
ATOM   1906 C CG  . GLN A 1 246 ? 9.926  41.793  36.206  1.00 61.75  ?  469 GLN B CG  1 
ATOM   1907 C CD  . GLN A 1 246 ? 9.805  41.647  37.713  1.00 66.74  ?  469 GLN B CD  1 
ATOM   1908 O OE1 . GLN A 1 246 ? 8.702  41.577  38.259  1.00 67.67  ?  469 GLN B OE1 1 
ATOM   1909 N NE2 . GLN A 1 246 ? 10.944 41.599  38.395  1.00 72.96  ?  469 GLN B NE2 1 
ATOM   1910 N N   . SER A 1 247 ? 6.424  40.835  33.210  1.00 58.78  ?  470 SER B N   1 
ATOM   1911 C CA  . SER A 1 247 ? 5.326  41.118  32.294  1.00 55.75  ?  470 SER B CA  1 
ATOM   1912 C C   . SER A 1 247 ? 5.232  39.966  31.302  1.00 57.99  ?  470 SER B C   1 
ATOM   1913 O O   . SER A 1 247 ? 5.948  38.967  31.411  1.00 60.08  ?  470 SER B O   1 
ATOM   1914 C CB  . SER A 1 247 ? 5.519  42.464  31.590  1.00 55.98  ?  470 SER B CB  1 
ATOM   1915 O OG  . SER A 1 247 ? 6.383  42.339  30.473  1.00 56.80  ?  470 SER B OG  1 
ATOM   1916 N N   . ASP A 1 248 ? 4.340  40.112  30.323  1.00 55.42  ?  471 ASP B N   1 
ATOM   1917 C CA  . ASP A 1 248 ? 4.102  39.051  29.354  1.00 58.90  ?  471 ASP B CA  1 
ATOM   1918 C C   . ASP A 1 248 ? 5.046  39.099  28.160  1.00 55.94  ?  471 ASP B C   1 
ATOM   1919 O O   . ASP A 1 248 ? 5.133  38.112  27.421  1.00 59.21  ?  471 ASP B O   1 
ATOM   1920 C CB  . ASP A 1 248 ? 2.656  39.107  28.854  1.00 67.66  ?  471 ASP B CB  1 
ATOM   1921 C CG  . ASP A 1 248 ? 1.758  38.106  29.552  1.00 74.07  ?  471 ASP B CG  1 
ATOM   1922 O OD1 . ASP A 1 248 ? 2.201  37.504  30.554  1.00 73.05  ?  471 ASP B OD1 1 
ATOM   1923 O OD2 . ASP A 1 248 ? 0.610  37.923  29.098  1.00 78.15  ?  471 ASP B OD2 1 
ATOM   1924 N N   . VAL A 1 249 ? 5.749  40.209  27.953  1.00 47.22  ?  472 VAL B N   1 
ATOM   1925 C CA  . VAL A 1 249 ? 6.642  40.368  26.811  1.00 48.46  ?  472 VAL B CA  1 
ATOM   1926 C C   . VAL A 1 249 ? 7.929  41.028  27.283  1.00 47.94  ?  472 VAL B C   1 
ATOM   1927 O O   . VAL A 1 249 ? 7.893  42.076  27.935  1.00 54.28  ?  472 VAL B O   1 
ATOM   1928 C CB  . VAL A 1 249 ? 5.995  41.201  25.688  1.00 51.87  ?  472 VAL B CB  1 
ATOM   1929 C CG1 . VAL A 1 249 ? 7.041  41.611  24.670  1.00 49.62  ?  472 VAL B CG1 1 
ATOM   1930 C CG2 . VAL A 1 249 ? 4.871  40.424  25.022  1.00 49.41  ?  472 VAL B CG2 1 
ATOM   1931 N N   . ALA A 1 250 ? 9.064  40.419  26.951  1.00 47.47  ?  473 ALA B N   1 
ATOM   1932 C CA  . ALA A 1 250 ? 10.376 40.995  27.217  1.00 46.94  ?  473 ALA B CA  1 
ATOM   1933 C C   . ALA A 1 250 ? 10.911 41.603  25.927  1.00 50.74  ?  473 ALA B C   1 
ATOM   1934 O O   . ALA A 1 250 ? 11.071 40.900  24.924  1.00 53.17  ?  473 ALA B O   1 
ATOM   1935 C CB  . ALA A 1 250 ? 11.339 39.940  27.758  1.00 45.09  ?  473 ALA B CB  1 
ATOM   1936 N N   . LEU A 1 251 ? 11.185 42.905  25.954  1.00 46.35  ?  474 LEU B N   1 
ATOM   1937 C CA  . LEU A 1 251 ? 11.672 43.610  24.773  1.00 48.05  ?  474 LEU B CA  1 
ATOM   1938 C C   . LEU A 1 251 ? 13.174 43.398  24.630  1.00 48.47  ?  474 LEU B C   1 
ATOM   1939 O O   . LEU A 1 251 ? 13.945 43.752  25.528  1.00 49.47  ?  474 LEU B O   1 
ATOM   1940 C CB  . LEU A 1 251 ? 11.342 45.099  24.868  1.00 43.74  ?  474 LEU B CB  1 
ATOM   1941 C CG  . LEU A 1 251 ? 11.950 46.000  23.793  1.00 45.04  ?  474 LEU B CG  1 
ATOM   1942 C CD1 . LEU A 1 251 ? 11.287 45.755  22.444  1.00 47.76  ?  474 LEU B CD1 1 
ATOM   1943 C CD2 . LEU A 1 251 ? 11.838 47.465  24.190  1.00 49.49  ?  474 LEU B CD2 1 
ATOM   1944 N N   . LEU A 1 252 ? 13.588 42.823  23.505  1.00 46.59  ?  475 LEU B N   1 
ATOM   1945 C CA  . LEU A 1 252 ? 14.991 42.586  23.207  1.00 43.70  ?  475 LEU B CA  1 
ATOM   1946 C C   . LEU A 1 252 ? 15.448 43.494  22.073  1.00 42.65  ?  475 LEU B C   1 
ATOM   1947 O O   . LEU A 1 252 ? 14.649 43.940  21.243  1.00 42.85  ?  475 LEU B O   1 
ATOM   1948 C CB  . LEU A 1 252 ? 15.239 41.121  22.829  1.00 45.09  ?  475 LEU B CB  1 
ATOM   1949 C CG  . LEU A 1 252 ? 14.650 40.030  23.724  1.00 46.94  ?  475 LEU B CG  1 
ATOM   1950 C CD1 . LEU A 1 252 ? 15.083 38.658  23.232  1.00 36.69  ?  475 LEU B CD1 1 
ATOM   1951 C CD2 . LEU A 1 252 ? 15.060 40.235  25.171  1.00 41.39  ?  475 LEU B CD2 1 
ATOM   1952 N N   . ARG A 1 253 ? 16.751 43.768  22.071  1.00 41.60  ?  476 ARG B N   1 
ATOM   1953 C CA  . ARG A 1 253 ? 17.359 44.614  21.027  1.00 43.13  ?  476 ARG B CA  1 
ATOM   1954 C C   . ARG A 1 253 ? 18.607 43.911  20.504  1.00 47.36  ?  476 ARG B C   1 
ATOM   1955 O O   . ARG A 1 253 ? 19.418 43.490  21.325  1.00 46.21  ?  476 ARG B O   1 
ATOM   1956 C CB  . ARG A 1 253 ? 17.710 45.989  21.593  1.00 44.16  ?  476 ARG B CB  1 
ATOM   1957 C CG  . ARG A 1 253 ? 16.680 47.068  21.300  1.00 50.59  ?  476 ARG B CG  1 
ATOM   1958 C CD  . ARG A 1 253 ? 15.638 47.158  22.394  1.00 58.95  ?  476 ARG B CD  1 
ATOM   1959 N NE  . ARG A 1 253 ? 14.638 48.176  22.124  1.00 64.73  ?  476 ARG B NE  1 
ATOM   1960 C CZ  . ARG A 1 253 ? 14.622 49.379  22.679  1.00 56.54  ?  476 ARG B CZ  1 
ATOM   1961 N NH1 . ARG A 1 253 ? 15.561 49.722  23.541  1.00 52.58  ?  476 ARG B NH1 1 
ATOM   1962 N NH2 . ARG A 1 253 ? 13.668 50.236  22.371  1.00 60.51  ?  476 ARG B NH2 1 
ATOM   1963 N N   . PHE A 1 254 ? 18.739 43.790  19.186  1.00 45.28  ?  477 PHE B N   1 
ATOM   1964 C CA  . PHE A 1 254 ? 19.903 43.186  18.550  1.00 42.61  ?  477 PHE B CA  1 
ATOM   1965 C C   . PHE A 1 254 ? 20.949 44.264  18.300  1.00 38.72  ?  477 PHE B C   1 
ATOM   1966 O O   . PHE A 1 254 ? 20.675 45.252  17.609  1.00 44.92  ?  477 PHE B O   1 
ATOM   1967 C CB  . PHE A 1 254 ? 19.509 42.503  17.243  1.00 44.93  ?  477 PHE B CB  1 
ATOM   1968 C CG  . PHE A 1 254 ? 20.518 41.506  16.748  1.00 42.29  ?  477 PHE B CG  1 
ATOM   1969 C CD1 . PHE A 1 254 ? 20.511 40.202  17.215  1.00 41.05  ?  477 PHE B CD1 1 
ATOM   1970 C CD2 . PHE A 1 254 ? 21.472 41.870  15.811  1.00 46.73  ?  477 PHE B CD2 1 
ATOM   1971 C CE1 . PHE A 1 254 ? 21.436 39.281  16.760  1.00 43.23  ?  477 PHE B CE1 1 
ATOM   1972 C CE2 . PHE A 1 254 ? 22.402 40.952  15.352  1.00 44.89  ?  477 PHE B CE2 1 
ATOM   1973 C CZ  . PHE A 1 254 ? 22.383 39.657  15.828  1.00 40.25  ?  477 PHE B CZ  1 
ATOM   1974 N N   . VAL A 1 255 ? 22.146 44.070  18.846  1.00 42.39  ?  478 VAL B N   1 
ATOM   1975 C CA  . VAL A 1 255 ? 23.182 45.095  18.863  1.00 48.54  ?  478 VAL B CA  1 
ATOM   1976 C C   . VAL A 1 255 ? 24.402 44.595  18.104  1.00 47.07  ?  478 VAL B C   1 
ATOM   1977 O O   . VAL A 1 255 ? 24.806 43.436  18.249  1.00 47.38  ?  478 VAL B O   1 
ATOM   1978 C CB  . VAL A 1 255 ? 23.560 45.484  20.309  1.00 46.39  ?  478 VAL B CB  1 
ATOM   1979 C CG1 . VAL A 1 255 ? 24.667 46.528  20.315  1.00 46.69  ?  478 VAL B CG1 1 
ATOM   1980 C CG2 . VAL A 1 255 ? 22.339 45.990  21.059  1.00 46.63  ?  478 VAL B CG2 1 
ATOM   1981 N N   . ASN A 1 256 ? 24.987 45.478  17.293  1.00 45.74  ?  479 ASN B N   1 
ATOM   1982 C CA  . ASN A 1 256 ? 26.267 45.211  16.654  1.00 51.34  ?  479 ASN B CA  1 
ATOM   1983 C C   . ASN A 1 256 ? 27.369 45.786  17.533  1.00 53.71  ?  479 ASN B C   1 
ATOM   1984 O O   . ASN A 1 256 ? 27.532 47.015  17.573  1.00 55.12  ?  479 ASN B O   1 
ATOM   1985 C CB  . ASN A 1 256 ? 26.315 45.830  15.263  1.00 50.55  ?  479 ASN B CB  1 
ATOM   1986 C CG  . ASN A 1 256 ? 27.612 45.529  14.536  1.00 57.36  ?  479 ASN B CG  1 
ATOM   1987 O OD1 . ASN A 1 256 ? 28.401 44.687  14.970  1.00 60.83  ?  479 ASN B OD1 1 
ATOM   1988 N ND2 . ASN A 1 256 ? 27.840 46.215  13.422  1.00 59.83  ?  479 ASN B ND2 1 
ATOM   1989 N N   . PRO A 1 257 ? 28.142 44.960  18.244  1.00 54.96  ?  480 PRO B N   1 
ATOM   1990 C CA  . PRO A 1 257 ? 29.163 45.510  19.152  1.00 56.80  ?  480 PRO B CA  1 
ATOM   1991 C C   . PRO A 1 257 ? 30.301 46.220  18.441  1.00 63.18  ?  480 PRO B C   1 
ATOM   1992 O O   . PRO A 1 257 ? 31.033 46.977  19.092  1.00 63.32  ?  480 PRO B O   1 
ATOM   1993 C CB  . PRO A 1 257 ? 29.665 44.273  19.907  1.00 53.30  ?  480 PRO B CB  1 
ATOM   1994 C CG  . PRO A 1 257 ? 29.386 43.136  18.985  1.00 55.40  ?  480 PRO B CG  1 
ATOM   1995 C CD  . PRO A 1 257 ? 28.117 43.488  18.260  1.00 55.36  ?  480 PRO B CD  1 
ATOM   1996 N N   . ASP A 1 258 ? 30.481 46.004  17.136  1.00 62.76  ?  481 ASP B N   1 
ATOM   1997 C CA  . ASP A 1 258 ? 31.501 46.737  16.393  1.00 66.02  ?  481 ASP B CA  1 
ATOM   1998 C C   . ASP A 1 258 ? 31.178 48.221  16.289  1.00 64.81  ?  481 ASP B C   1 
ATOM   1999 O O   . ASP A 1 258 ? 32.087 49.031  16.081  1.00 66.01  ?  481 ASP B O   1 
ATOM   2000 C CB  . ASP A 1 258 ? 31.664 46.148  14.989  1.00 65.85  ?  481 ASP B CB  1 
ATOM   2001 C CG  . ASP A 1 258 ? 32.141 44.707  15.008  1.00 71.43  ?  481 ASP B CG  1 
ATOM   2002 O OD1 . ASP A 1 258 ? 32.143 44.088  16.094  1.00 68.50  ?  481 ASP B OD1 1 
ATOM   2003 O OD2 . ASP A 1 258 ? 32.506 44.189  13.930  1.00 67.91  ?  481 ASP B OD2 1 
ATOM   2004 N N   . THR A 1 259 ? 29.904 48.589  16.419  1.00 65.11  ?  482 THR B N   1 
ATOM   2005 C CA  . THR A 1 259 ? 29.462 49.972  16.302  1.00 64.69  ?  482 THR B CA  1 
ATOM   2006 C C   . THR A 1 259 ? 28.571 50.441  17.441  1.00 62.47  ?  482 THR B C   1 
ATOM   2007 O O   . THR A 1 259 ? 28.474 51.656  17.653  1.00 73.00  ?  482 THR B O   1 
ATOM   2008 C CB  . THR A 1 259 ? 28.707 50.183  14.980  1.00 65.61  ?  482 THR B CB  1 
ATOM   2009 O OG1 . THR A 1 259 ? 27.438 49.521  15.047  1.00 65.10  ?  482 THR B OG1 1 
ATOM   2010 C CG2 . THR A 1 259 ? 29.507 49.645  13.799  1.00 65.87  ?  482 THR B CG2 1 
ATOM   2011 N N   . GLY A 1 260 ? 27.919 49.538  18.171  1.00 62.24  ?  483 GLY B N   1 
ATOM   2012 C CA  . GLY A 1 260 ? 27.017 49.908  19.240  1.00 59.65  ?  483 GLY B CA  1 
ATOM   2013 C C   . GLY A 1 260 ? 25.588 50.170  18.813  1.00 59.57  ?  483 GLY B C   1 
ATOM   2014 O O   . GLY A 1 260 ? 24.708 50.252  19.679  1.00 57.61  ?  483 GLY B O   1 
ATOM   2015 N N   . ARG A 1 261 ? 25.325 50.294  17.514  1.00 59.45  ?  484 ARG B N   1 
ATOM   2016 C CA  . ARG A 1 261 ? 23.987 50.624  17.048  1.00 57.80  ?  484 ARG B CA  1 
ATOM   2017 C C   . ARG A 1 261 ? 23.050 49.426  17.163  1.00 53.66  ?  484 ARG B C   1 
ATOM   2018 O O   . ARG A 1 261 ? 23.458 48.269  17.032  1.00 51.48  ?  484 ARG B O   1 
ATOM   2019 C CB  . ARG A 1 261 ? 24.028 51.108  15.598  1.00 57.43  ?  484 ARG B CB  1 
ATOM   2020 C CG  . ARG A 1 261 ? 25.327 51.789  15.203  1.00 64.85  ?  484 ARG B CG  1 
ATOM   2021 C CD  . ARG A 1 261 ? 25.137 53.282  14.997  1.00 71.85  ?  484 ARG B CD  1 
ATOM   2022 N NE  . ARG A 1 261 ? 24.414 53.567  13.764  1.00 74.71  ?  484 ARG B NE  1 
ATOM   2023 C CZ  . ARG A 1 261 ? 24.957 54.124  12.689  1.00 82.82  ?  484 ARG B CZ  1 
ATOM   2024 N NH1 . ARG A 1 261 ? 26.231 54.478  12.665  1.00 84.63  ?  484 ARG B NH1 1 
ATOM   2025 N NH2 . ARG A 1 261 ? 24.204 54.333  11.613  1.00 80.80  ?  484 ARG B NH2 1 
ATOM   2026 N N   . VAL A 1 262 ? 21.777 49.721  17.408  1.00 50.00  ?  485 VAL B N   1 
ATOM   2027 C CA  . VAL A 1 262 ? 20.736 48.703  17.476  1.00 47.05  ?  485 VAL B CA  1 
ATOM   2028 C C   . VAL A 1 262 ? 20.231 48.430  16.066  1.00 50.76  ?  485 VAL B C   1 
ATOM   2029 O O   . VAL A 1 262 ? 19.829 49.355  15.350  1.00 45.22  ?  485 VAL B O   1 
ATOM   2030 C CB  . VAL A 1 262 ? 19.590 49.151  18.396  1.00 46.80  ?  485 VAL B CB  1 
ATOM   2031 C CG1 . VAL A 1 262 ? 18.358 48.286  18.171  1.00 46.05  ?  485 VAL B CG1 1 
ATOM   2032 C CG2 . VAL A 1 262 ? 20.027 49.101  19.853  1.00 41.56  ?  485 VAL B CG2 1 
ATOM   2033 N N   . LEU A 1 263 ? 20.250 47.159  15.664  1.00 48.75  ?  486 LEU B N   1 
ATOM   2034 C CA  . LEU A 1 263 ? 19.852 46.790  14.312  1.00 46.66  ?  486 LEU B CA  1 
ATOM   2035 C C   . LEU A 1 263 ? 18.361 46.501  14.199  1.00 40.12  ?  486 LEU B C   1 
ATOM   2036 O O   . LEU A 1 263 ? 17.742 46.848  13.187  1.00 49.04  ?  486 LEU B O   1 
ATOM   2037 C CB  . LEU A 1 263 ? 20.657 45.580  13.842  1.00 45.12  ?  486 LEU B CB  1 
ATOM   2038 C CG  . LEU A 1 263 ? 22.148 45.860  13.671  1.00 49.42  ?  486 LEU B CG  1 
ATOM   2039 C CD1 . LEU A 1 263 ? 22.853 44.612  13.208  1.00 47.43  ?  486 LEU B CD1 1 
ATOM   2040 C CD2 . LEU A 1 263 ? 22.376 47.001  12.692  1.00 38.21  ?  486 LEU B CD2 1 
ATOM   2041 N N   . PHE A 1 264 ? 17.773 45.867  15.208  1.00 43.51  ?  487 PHE B N   1 
ATOM   2042 C CA  . PHE A 1 264 ? 16.331 45.668  15.253  1.00 44.44  ?  487 PHE B CA  1 
ATOM   2043 C C   . PHE A 1 264 ? 15.941 45.306  16.677  1.00 42.92  ?  487 PHE B C   1 
ATOM   2044 O O   . PHE A 1 264 ? 16.788 44.979  17.513  1.00 42.87  ?  487 PHE B O   1 
ATOM   2045 C CB  . PHE A 1 264 ? 15.868 44.595  14.254  1.00 45.60  ?  487 PHE B CB  1 
ATOM   2046 C CG  . PHE A 1 264 ? 16.280 43.191  14.618  1.00 44.87  ?  487 PHE B CG  1 
ATOM   2047 C CD1 . PHE A 1 264 ? 15.452 42.383  15.384  1.00 42.53  ?  487 PHE B CD1 1 
ATOM   2048 C CD2 . PHE A 1 264 ? 17.482 42.669  14.167  1.00 44.71  ?  487 PHE B CD2 1 
ATOM   2049 C CE1 . PHE A 1 264 ? 15.825 41.091  15.710  1.00 42.39  ?  487 PHE B CE1 1 
ATOM   2050 C CE2 . PHE A 1 264 ? 17.857 41.377  14.486  1.00 41.55  ?  487 PHE B CE2 1 
ATOM   2051 C CZ  . PHE A 1 264 ? 17.029 40.588  15.261  1.00 37.84  ?  487 PHE B CZ  1 
ATOM   2052 N N   . GLU A 1 265 ? 14.642 45.374  16.945  1.00 45.45  ?  488 GLU B N   1 
ATOM   2053 C CA  . GLU A 1 265 ? 14.089 44.987  18.231  1.00 48.28  ?  488 GLU B CA  1 
ATOM   2054 C C   . GLU A 1 265 ? 12.966 43.987  18.011  1.00 45.17  ?  488 GLU B C   1 
ATOM   2055 O O   . GLU A 1 265 ? 12.300 43.992  16.971  1.00 44.06  ?  488 GLU B O   1 
ATOM   2056 C CB  . GLU A 1 265 ? 13.581 46.206  19.022  1.00 47.90  ?  488 GLU B CB  1 
ATOM   2057 C CG  . GLU A 1 265 ? 12.367 46.893  18.420  1.00 53.21  ?  488 GLU B CG  1 
ATOM   2058 C CD  . GLU A 1 265 ? 11.987 48.159  19.169  1.00 58.85  ?  488 GLU B CD  1 
ATOM   2059 O OE1 . GLU A 1 265 ? 12.816 48.656  19.959  1.00 60.38  ?  488 GLU B OE1 1 
ATOM   2060 O OE2 . GLU A 1 265 ? 10.859 48.657  18.967  1.00 57.85  ?  488 GLU B OE2 1 
ATOM   2061 N N   . CYS A 1 266 ? 12.766 43.118  18.998  1.00 44.70  ?  489 CYS B N   1 
ATOM   2062 C CA  . CYS A 1 266 ? 11.800 42.038  18.890  1.00 46.83  ?  489 CYS B CA  1 
ATOM   2063 C C   . CYS A 1 266 ? 11.156 41.794  20.247  1.00 43.63  ?  489 CYS B C   1 
ATOM   2064 O O   . CYS A 1 266 ? 11.630 42.270  21.283  1.00 46.15  ?  489 CYS B O   1 
ATOM   2065 C CB  . CYS A 1 266 ? 12.457 40.756  18.372  1.00 44.63  ?  489 CYS B CB  1 
ATOM   2066 S SG  . CYS A 1 266 ? 13.880 40.218  19.343  1.00 45.81  ?  489 CYS B SG  1 
ATOM   2067 N N   . LYS A 1 267 ? 10.064 41.036  20.228  1.00 43.63  ?  490 LYS B N   1 
ATOM   2068 C CA  . LYS A 1 267 ? 9.331  40.668  21.431  1.00 45.46  ?  490 LYS B CA  1 
ATOM   2069 C C   . LYS A 1 267 ? 9.666  39.230  21.801  1.00 46.55  ?  490 LYS B C   1 
ATOM   2070 O O   . LYS A 1 267 ? 9.438  38.315  21.004  1.00 41.94  ?  490 LYS B O   1 
ATOM   2071 C CB  . LYS A 1 267 ? 7.826  40.811  21.218  1.00 45.22  ?  490 LYS B CB  1 
ATOM   2072 C CG  . LYS A 1 267 ? 7.329  42.232  21.088  1.00 51.95  ?  490 LYS B CG  1 
ATOM   2073 C CD  . LYS A 1 267 ? 5.831  42.275  21.318  1.00 55.56  ?  490 LYS B CD  1 
ATOM   2074 C CE  . LYS A 1 267 ? 5.240  43.586  20.857  1.00 50.53  ?  490 LYS B CE  1 
ATOM   2075 N NZ  . LYS A 1 267 ? 3.872  43.396  20.302  1.00 52.57  ?  490 LYS B NZ  1 
ATOM   2076 N N   . LEU A 1 268 ? 10.196 39.032  23.005  1.00 46.92  ?  491 LEU B N   1 
ATOM   2077 C CA  . LEU A 1 268 ? 10.405 37.695  23.559  1.00 43.21  ?  491 LEU B CA  1 
ATOM   2078 C C   . LEU A 1 268 ? 9.233  37.412  24.493  1.00 42.31  ?  491 LEU B C   1 
ATOM   2079 O O   . LEU A 1 268 ? 9.192  37.901  25.623  1.00 46.15  ?  491 LEU B O   1 
ATOM   2080 C CB  . LEU A 1 268 ? 11.742 37.597  24.285  1.00 40.26  ?  491 LEU B CB  1 
ATOM   2081 C CG  . LEU A 1 268 ? 11.995 36.302  25.067  1.00 39.60  ?  491 LEU B CG  1 
ATOM   2082 C CD1 . LEU A 1 268 ? 11.783 35.077  24.189  1.00 41.87  ?  491 LEU B CD1 1 
ATOM   2083 C CD2 . LEU A 1 268 ? 13.392 36.295  25.670  1.00 41.07  ?  491 LEU B CD2 1 
ATOM   2084 N N   . HIS A 1 269 ? 8.275  36.628  24.010  1.00 43.08  ?  492 HIS B N   1 
ATOM   2085 C CA  . HIS A 1 269 ? 7.076  36.354  24.784  1.00 43.78  ?  492 HIS B CA  1 
ATOM   2086 C C   . HIS A 1 269 ? 7.383  35.403  25.935  1.00 47.01  ?  492 HIS B C   1 
ATOM   2087 O O   . HIS A 1 269 ? 8.267  34.546  25.845  1.00 39.95  ?  492 HIS B O   1 
ATOM   2088 C CB  . HIS A 1 269 ? 5.986  35.772  23.887  1.00 39.69  ?  492 HIS B CB  1 
ATOM   2089 C CG  . HIS A 1 269 ? 5.584  36.682  22.769  1.00 48.76  ?  492 HIS B CG  1 
ATOM   2090 N ND1 . HIS A 1 269 ? 4.475  37.498  22.835  1.00 50.66  ?  492 HIS B ND1 1 
ATOM   2091 C CD2 . HIS A 1 269 ? 6.154  36.919  21.563  1.00 46.64  ?  492 HIS B CD2 1 
ATOM   2092 C CE1 . HIS A 1 269 ? 4.374  38.191  21.716  1.00 54.58  ?  492 HIS B CE1 1 
ATOM   2093 N NE2 . HIS A 1 269 ? 5.380  37.859  20.926  1.00 52.50  ?  492 HIS B NE2 1 
ATOM   2094 N N   . LYS A 1 270 ? 6.632  35.569  27.028  1.00 44.53  ?  493 LYS B N   1 
ATOM   2095 C CA  . LYS A 1 270 ? 6.903  34.817  28.250  1.00 47.51  ?  493 LYS B CA  1 
ATOM   2096 C C   . LYS A 1 270 ? 6.824  33.315  28.009  1.00 44.36  ?  493 LYS B C   1 
ATOM   2097 O O   . LYS A 1 270 ? 7.592  32.543  28.598  1.00 38.73  ?  493 LYS B O   1 
ATOM   2098 C CB  . LYS A 1 270 ? 5.926  35.242  29.347  1.00 47.47  ?  493 LYS B CB  1 
ATOM   2099 C CG  . LYS A 1 270 ? 5.908  34.337  30.570  1.00 55.96  ?  493 LYS B CG  1 
ATOM   2100 C CD  . LYS A 1 270 ? 4.786  34.711  31.526  1.00 60.54  ?  493 LYS B CD  1 
ATOM   2101 C CE  . LYS A 1 270 ? 4.535  33.602  32.537  1.00 64.71  ?  493 LYS B CE  1 
ATOM   2102 N NZ  . LYS A 1 270 ? 3.959  34.123  33.808  1.00 69.04  ?  493 LYS B NZ  1 
ATOM   2103 N N   . SER A 1 271 ? 5.916  32.879  27.131  1.00 43.57  ?  494 SER B N   1 
ATOM   2104 C CA  . SER A 1 271 ? 5.766  31.454  26.864  1.00 45.01  ?  494 SER B CA  1 
ATOM   2105 C C   . SER A 1 271 ? 6.952  30.873  26.103  1.00 44.58  ?  494 SER B C   1 
ATOM   2106 O O   . SER A 1 271 ? 7.093  29.647  26.047  1.00 44.16  ?  494 SER B O   1 
ATOM   2107 C CB  . SER A 1 271 ? 4.467  31.197  26.095  1.00 40.98  ?  494 SER B CB  1 
ATOM   2108 O OG  . SER A 1 271 ? 4.179  32.268  25.214  1.00 51.05  ?  494 SER B OG  1 
ATOM   2109 N N   . GLY A 1 272 ? 7.796  31.716  25.513  1.00 41.69  ?  495 GLY B N   1 
ATOM   2110 C CA  . GLY A 1 272 ? 9.034  31.245  24.921  1.00 43.39  ?  495 GLY B CA  1 
ATOM   2111 C C   . GLY A 1 272 ? 9.076  31.245  23.407  1.00 42.94  ?  495 GLY B C   1 
ATOM   2112 O O   . GLY A 1 272 ? 9.333  30.205  22.792  1.00 44.50  ?  495 GLY B O   1 
ATOM   2113 N N   . TYR A 1 273 ? 8.820  32.396  22.791  1.00 39.51  ?  496 TYR B N   1 
ATOM   2114 C CA  . TYR A 1 273 ? 9.005  32.557  21.353  1.00 40.46  ?  496 TYR B CA  1 
ATOM   2115 C C   . TYR A 1 273 ? 9.197  34.039  21.060  1.00 41.68  ?  496 TYR B C   1 
ATOM   2116 O O   . TYR A 1 273 ? 8.971  34.895  21.919  1.00 40.52  ?  496 TYR B O   1 
ATOM   2117 C CB  . TYR A 1 273 ? 7.837  31.965  20.556  1.00 37.98  ?  496 TYR B CB  1 
ATOM   2118 C CG  . TYR A 1 273 ? 6.506  32.655  20.751  1.00 41.47  ?  496 TYR B CG  1 
ATOM   2119 C CD1 . TYR A 1 273 ? 5.655  32.288  21.787  1.00 44.12  ?  496 TYR B CD1 1 
ATOM   2120 C CD2 . TYR A 1 273 ? 6.088  33.658  19.887  1.00 45.38  ?  496 TYR B CD2 1 
ATOM   2121 C CE1 . TYR A 1 273 ? 4.432  32.912  21.963  1.00 46.77  ?  496 TYR B CE1 1 
ATOM   2122 C CE2 . TYR A 1 273 ? 4.868  34.284  20.053  1.00 49.88  ?  496 TYR B CE2 1 
ATOM   2123 C CZ  . TYR A 1 273 ? 4.044  33.910  21.092  1.00 48.97  ?  496 TYR B CZ  1 
ATOM   2124 O OH  . TYR A 1 273 ? 2.829  34.535  21.258  1.00 50.27  ?  496 TYR B OH  1 
ATOM   2125 N N   . VAL A 1 274 ? 9.630  34.329  19.834  1.00 37.67  ?  497 VAL B N   1 
ATOM   2126 C CA  . VAL A 1 274 ? 10.040 35.670  19.434  1.00 34.71  ?  497 VAL B CA  1 
ATOM   2127 C C   . VAL A 1 274 ? 9.229  36.106  18.222  1.00 43.87  ?  497 VAL B C   1 
ATOM   2128 O O   . VAL A 1 274 ? 9.025  35.327  17.285  1.00 46.62  ?  497 VAL B O   1 
ATOM   2129 C CB  . VAL A 1 274 ? 11.551 35.728  19.127  1.00 35.06  ?  497 VAL B CB  1 
ATOM   2130 C CG1 . VAL A 1 274 ? 11.962 37.134  18.722  1.00 37.52  ?  497 VAL B CG1 1 
ATOM   2131 C CG2 . VAL A 1 274 ? 12.357 35.256  20.326  1.00 39.44  ?  497 VAL B CG2 1 
ATOM   2132 N N   . THR A 1 275 ? 8.771  37.358  18.242  1.00 39.64  ?  498 THR B N   1 
ATOM   2133 C CA  . THR A 1 275 ? 8.075  37.959  17.114  1.00 44.77  ?  498 THR B CA  1 
ATOM   2134 C C   . THR A 1 275 ? 8.763  39.259  16.720  1.00 47.05  ?  498 THR B C   1 
ATOM   2135 O O   . THR A 1 275 ? 9.410  39.912  17.542  1.00 41.39  ?  498 THR B O   1 
ATOM   2136 C CB  . THR A 1 275 ? 6.597  38.236  17.431  1.00 44.68  ?  498 THR B CB  1 
ATOM   2137 O OG1 . THR A 1 275 ? 6.503  39.098  18.572  1.00 50.72  ?  498 THR B OG1 1 
ATOM   2138 C CG2 . THR A 1 275 ? 5.857  36.937  17.713  1.00 42.57  ?  498 THR B CG2 1 
ATOM   2139 N N   . VAL A 1 276 ? 8.616  39.626  15.445  1.00 42.64  ?  499 VAL B N   1 
ATOM   2140 C CA  . VAL A 1 276 ? 9.184  40.849  14.895  1.00 43.28  ?  499 VAL B CA  1 
ATOM   2141 C C   . VAL A 1 276 ? 8.117  41.563  14.076  1.00 49.39  ?  499 VAL B C   1 
ATOM   2142 O O   . VAL A 1 276 ? 7.126  40.967  13.649  1.00 47.46  ?  499 VAL B O   1 
ATOM   2143 C CB  . VAL A 1 276 ? 10.431 40.583  14.023  1.00 46.66  ?  499 VAL B CB  1 
ATOM   2144 C CG1 . VAL A 1 276 ? 11.659 40.386  14.891  1.00 49.29  ?  499 VAL B CG1 1 
ATOM   2145 C CG2 . VAL A 1 276 ? 10.203 39.378  13.118  1.00 44.93  ?  499 VAL B CG2 1 
ATOM   2146 N N   . ALA A 1 277 ? 8.341  42.858  13.851  1.00 45.20  ?  500 ALA B N   1 
ATOM   2147 C CA  . ALA A 1 277 ? 7.419  43.688  13.075  1.00 56.15  ?  500 ALA B CA  1 
ATOM   2148 C C   . ALA A 1 277 ? 7.856  43.658  11.616  1.00 52.10  ?  500 ALA B C   1 
ATOM   2149 O O   . ALA A 1 277 ? 8.684  44.456  11.173  1.00 53.01  ?  500 ALA B O   1 
ATOM   2150 C CB  . ALA A 1 277 ? 7.383  45.110  13.621  1.00 48.47  ?  500 ALA B CB  1 
ATOM   2151 N N   . HIS A 1 278 ? 7.285  42.725  10.856  1.00 49.05  ?  501 HIS B N   1 
ATOM   2152 C CA  . HIS A 1 278 ? 7.617  42.573  9.447   1.00 50.61  ?  501 HIS B CA  1 
ATOM   2153 C C   . HIS A 1 278 ? 6.549  41.720  8.781   1.00 49.46  ?  501 HIS B C   1 
ATOM   2154 O O   . HIS A 1 278 ? 5.860  40.932  9.433   1.00 50.73  ?  501 HIS B O   1 
ATOM   2155 C CB  . HIS A 1 278 ? 9.003  41.946  9.260   1.00 52.74  ?  501 HIS B CB  1 
ATOM   2156 C CG  . HIS A 1 278 ? 9.553  42.094  7.876   1.00 52.88  ?  501 HIS B CG  1 
ATOM   2157 N ND1 . HIS A 1 278 ? 9.445  41.106  6.922   1.00 56.43  ?  501 HIS B ND1 1 
ATOM   2158 C CD2 . HIS A 1 278 ? 10.217 43.116  7.287   1.00 52.22  ?  501 HIS B CD2 1 
ATOM   2159 C CE1 . HIS A 1 278 ? 10.018 41.513  5.802   1.00 53.94  ?  501 HIS B CE1 1 
ATOM   2160 N NE2 . HIS A 1 278 ? 10.494 42.729  5.998   1.00 57.38  ?  501 HIS B NE2 1 
ATOM   2161 N N   . THR A 1 279 ? 6.420  41.894  7.468   1.00 53.64  ?  502 THR B N   1 
ATOM   2162 C CA  . THR A 1 279 ? 5.477  41.133  6.657   1.00 55.77  ?  502 THR B CA  1 
ATOM   2163 C C   . THR A 1 279 ? 6.221  40.560  5.461   1.00 54.53  ?  502 THR B C   1 
ATOM   2164 O O   . THR A 1 279 ? 6.844  41.308  4.700   1.00 53.92  ?  502 THR B O   1 
ATOM   2165 C CB  . THR A 1 279 ? 4.305  42.005  6.194   1.00 54.23  ?  502 THR B CB  1 
ATOM   2166 O OG1 . THR A 1 279 ? 4.807  43.136  5.471   1.00 66.45  ?  502 THR B OG1 1 
ATOM   2167 C CG2 . THR A 1 279 ? 3.491  42.491  7.387   1.00 52.57  ?  502 THR B CG2 1 
ATOM   2168 N N   . GLY A 1 280 ? 6.160  39.246  5.300   1.00 51.61  ?  503 GLY B N   1 
ATOM   2169 C CA  . GLY A 1 280 ? 6.811  38.562  4.201   1.00 48.55  ?  503 GLY B CA  1 
ATOM   2170 C C   . GLY A 1 280 ? 8.020  37.761  4.661   1.00 52.83  ?  503 GLY B C   1 
ATOM   2171 O O   . GLY A 1 280 ? 8.525  37.906  5.774   1.00 50.84  ?  503 GLY B O   1 
ATOM   2172 N N   . GLN A 1 281 ? 8.478  36.896  3.760   1.00 51.82  ?  504 GLN B N   1 
ATOM   2173 C CA  . GLN A 1 281 ? 9.645  36.068  4.025   1.00 47.55  ?  504 GLN B CA  1 
ATOM   2174 C C   . GLN A 1 281 ? 10.924 36.871  3.830   1.00 46.20  ?  504 GLN B C   1 
ATOM   2175 O O   . GLN A 1 281 ? 11.033 37.671  2.895   1.00 53.13  ?  504 GLN B O   1 
ATOM   2176 C CB  . GLN A 1 281 ? 9.654  34.848  3.106   1.00 51.27  ?  504 GLN B CB  1 
ATOM   2177 C CG  . GLN A 1 281 ? 8.561  33.838  3.402   1.00 49.85  ?  504 GLN B CG  1 
ATOM   2178 C CD  . GLN A 1 281 ? 8.638  32.625  2.501   1.00 61.71  ?  504 GLN B CD  1 
ATOM   2179 O OE1 . GLN A 1 281 ? 9.694  32.312  1.949   1.00 60.16  ?  504 GLN B OE1 1 
ATOM   2180 N NE2 . GLN A 1 281 ? 7.515  31.931  2.344   1.00 61.39  ?  504 GLN B NE2 1 
ATOM   2181 N N   . HIS A 1 282 ? 11.893 36.652  4.719   1.00 47.07  ?  505 HIS B N   1 
ATOM   2182 C CA  . HIS A 1 282 ? 13.173 37.343  4.627   1.00 45.45  ?  505 HIS B CA  1 
ATOM   2183 C C   . HIS A 1 282 ? 14.223 36.714  5.533   1.00 44.80  ?  505 HIS B C   1 
ATOM   2184 O O   . HIS A 1 282 ? 13.966 36.457  6.714   1.00 43.25  ?  505 HIS B O   1 
ATOM   2185 C CB  . HIS A 1 282 ? 13.013 38.825  4.977   1.00 50.82  ?  505 HIS B CB  1 
ATOM   2186 C CG  . HIS A 1 282 ? 13.802 39.741  4.093   1.00 57.87  ?  505 HIS B CG  1 
ATOM   2187 N ND1 . HIS A 1 282 ? 15.173 39.663  3.976   1.00 55.69  ?  505 HIS B ND1 1 
ATOM   2188 C CD2 . HIS A 1 282 ? 13.412 40.755  3.284   1.00 56.27  ?  505 HIS B CD2 1 
ATOM   2189 C CE1 . HIS A 1 282 ? 15.594 40.589  3.132   1.00 51.62  ?  505 HIS B CE1 1 
ATOM   2190 N NE2 . HIS A 1 282 ? 14.546 41.265  2.699   1.00 58.35  ?  505 HIS B NE2 1 
ATOM   2191 N N   . ASP A 1 283 ? 15.408 36.460  4.983   1.00 45.56  ?  506 ASP B N   1 
ATOM   2192 C CA  . ASP A 1 283 ? 16.555 36.072  5.788   1.00 42.23  ?  506 ASP B CA  1 
ATOM   2193 C C   . ASP A 1 283 ? 17.245 37.320  6.319   1.00 49.95  ?  506 ASP B C   1 
ATOM   2194 O O   . ASP A 1 283 ? 17.378 38.321  5.611   1.00 48.99  ?  506 ASP B O   1 
ATOM   2195 C CB  . ASP A 1 283 ? 17.540 35.241  4.965   1.00 49.28  ?  506 ASP B CB  1 
ATOM   2196 C CG  . ASP A 1 283 ? 16.921 33.970  4.417   1.00 50.27  ?  506 ASP B CG  1 
ATOM   2197 O OD1 . ASP A 1 283 ? 16.581 33.075  5.220   1.00 54.75  ?  506 ASP B OD1 1 
ATOM   2198 O OD2 . ASP A 1 283 ? 16.775 33.865  3.181   1.00 61.79  ?  506 ASP B OD2 1 
ATOM   2199 N N   . LEU A 1 284 ? 17.681 37.258  7.573   1.00 40.50  ?  507 LEU B N   1 
ATOM   2200 C CA  . LEU A 1 284 ? 18.331 38.393  8.211   1.00 43.22  ?  507 LEU B CA  1 
ATOM   2201 C C   . LEU A 1 284 ? 19.839 38.289  8.024   1.00 40.16  ?  507 LEU B C   1 
ATOM   2202 O O   . LEU A 1 284 ? 20.438 37.249  8.316   1.00 44.19  ?  507 LEU B O   1 
ATOM   2203 C CB  . LEU A 1 284 ? 17.980 38.455  9.698   1.00 36.21  ?  507 LEU B CB  1 
ATOM   2204 C CG  . LEU A 1 284 ? 16.677 39.163  10.086  1.00 40.07  ?  507 LEU B CG  1 
ATOM   2205 C CD1 . LEU A 1 284 ? 15.457 38.352  9.672   1.00 36.77  ?  507 LEU B CD1 1 
ATOM   2206 C CD2 . LEU A 1 284 ? 16.648 39.440  11.583  1.00 40.10  ?  507 LEU B CD2 1 
ATOM   2207 N N   . VAL A 1 285 ? 20.444 39.361  7.525   1.00 41.54  ?  508 VAL B N   1 
ATOM   2208 C CA  . VAL A 1 285 ? 21.891 39.450  7.372   1.00 40.85  ?  508 VAL B CA  1 
ATOM   2209 C C   . VAL A 1 285 ? 22.423 40.204  8.584   1.00 43.94  ?  508 VAL B C   1 
ATOM   2210 O O   . VAL A 1 285 ? 22.259 41.425  8.691   1.00 48.11  ?  508 VAL B O   1 
ATOM   2211 C CB  . VAL A 1 285 ? 22.284 40.138  6.059   1.00 42.45  ?  508 VAL B CB  1 
ATOM   2212 C CG1 . VAL A 1 285 ? 23.785 40.030  5.836   1.00 37.99  ?  508 VAL B CG1 1 
ATOM   2213 C CG2 . VAL A 1 285 ? 21.523 39.523  4.890   1.00 41.96  ?  508 VAL B CG2 1 
ATOM   2214 N N   . ILE A 1 286 ? 23.054 39.478  9.500   1.00 37.76  ?  509 ILE B N   1 
ATOM   2215 C CA  . ILE A 1 286 ? 23.502 40.043  10.769  1.00 43.03  ?  509 ILE B CA  1 
ATOM   2216 C C   . ILE A 1 286 ? 25.026 40.080  10.799  1.00 42.94  ?  509 ILE B C   1 
ATOM   2217 O O   . ILE A 1 286 ? 25.678 39.281  10.111  1.00 46.44  ?  509 ILE B O   1 
ATOM   2218 C CB  . ILE A 1 286 ? 22.946 39.238  11.956  1.00 43.42  ?  509 ILE B CB  1 
ATOM   2219 C CG1 . ILE A 1 286 ? 23.331 37.763  11.825  1.00 39.38  ?  509 ILE B CG1 1 
ATOM   2220 C CG2 . ILE A 1 286 ? 21.435 39.392  12.049  1.00 39.16  ?  509 ILE B CG2 1 
ATOM   2221 C CD1 . ILE A 1 286 ? 22.886 36.909  12.990  1.00 39.87  ?  509 ILE B CD1 1 
ATOM   2222 N N   . PRO A 1 287 ? 25.636 40.986  11.569  1.00 46.22  ?  510 PRO B N   1 
ATOM   2223 C CA  . PRO A 1 287 ? 27.083 40.932  11.744  1.00 45.28  ?  510 PRO B CA  1 
ATOM   2224 C C   . PRO A 1 287 ? 27.472 39.685  12.527  1.00 48.41  ?  510 PRO B C   1 
ATOM   2225 O O   . PRO A 1 287 ? 26.681 39.182  13.340  1.00 44.41  ?  510 PRO B O   1 
ATOM   2226 C CB  . PRO A 1 287 ? 27.396 42.213  12.539  1.00 45.65  ?  510 PRO B CB  1 
ATOM   2227 C CG  . PRO A 1 287 ? 26.148 43.035  12.502  1.00 45.61  ?  510 PRO B CG  1 
ATOM   2228 C CD  . PRO A 1 287 ? 25.024 42.076  12.341  1.00 41.74  ?  510 PRO B CD  1 
ATOM   2229 N N   . PRO A 1 288 ? 28.680 39.166  12.313  1.00 50.64  ?  511 PRO B N   1 
ATOM   2230 C CA  . PRO A 1 288 ? 29.055 37.904  12.977  1.00 52.11  ?  511 PRO B CA  1 
ATOM   2231 C C   . PRO A 1 288 ? 29.096 37.997  14.491  1.00 51.83  ?  511 PRO B C   1 
ATOM   2232 O O   . PRO A 1 288 ? 28.989 36.963  15.162  1.00 49.47  ?  511 PRO B O   1 
ATOM   2233 C CB  . PRO A 1 288 ? 30.444 37.600  12.397  1.00 48.38  ?  511 PRO B CB  1 
ATOM   2234 C CG  . PRO A 1 288 ? 30.964 38.924  11.942  1.00 55.03  ?  511 PRO B CG  1 
ATOM   2235 C CD  . PRO A 1 288 ? 29.770 39.706  11.485  1.00 47.84  ?  511 PRO B CD  1 
ATOM   2236 N N   . ASN A 1 289 ? 29.231 39.196  15.054  1.00 49.33  ?  512 ASN B N   1 
ATOM   2237 C CA  . ASN A 1 289 ? 29.348 39.371  16.495  1.00 51.52  ?  512 ASN B CA  1 
ATOM   2238 C C   . ASN A 1 289 ? 28.084 39.942  17.127  1.00 48.34  ?  512 ASN B C   1 
ATOM   2239 O O   . ASN A 1 289 ? 28.090 40.255  18.322  1.00 48.45  ?  512 ASN B O   1 
ATOM   2240 C CB  . ASN A 1 289 ? 30.549 40.261  16.817  1.00 46.95  ?  512 ASN B CB  1 
ATOM   2241 C CG  . ASN A 1 289 ? 31.863 39.510  16.747  1.00 61.40  ?  512 ASN B CG  1 
ATOM   2242 O OD1 . ASN A 1 289 ? 31.989 38.404  17.273  1.00 58.55  ?  512 ASN B OD1 1 
ATOM   2243 N ND2 . ASN A 1 289 ? 32.851 40.106  16.088  1.00 65.20  ?  512 ASN B ND2 1 
ATOM   2244 N N   . GLY A 1 290 ? 27.003 40.080  16.361  1.00 46.96  ?  513 GLY B N   1 
ATOM   2245 C CA  . GLY A 1 290 ? 25.762 40.572  16.924  1.00 45.19  ?  513 GLY B CA  1 
ATOM   2246 C C   . GLY A 1 290 ? 25.208 39.649  17.993  1.00 42.14  ?  513 GLY B C   1 
ATOM   2247 O O   . GLY A 1 290 ? 25.499 38.452  18.044  1.00 43.99  ?  513 GLY B O   1 
ATOM   2248 N N   . TYR A 1 291 ? 24.392 40.228  18.872  1.00 42.33  ?  514 TYR B N   1 
ATOM   2249 C CA  . TYR A 1 291 ? 23.809 39.480  19.977  1.00 45.70  ?  514 TYR B CA  1 
ATOM   2250 C C   . TYR A 1 291 ? 22.531 40.169  20.426  1.00 42.37  ?  514 TYR B C   1 
ATOM   2251 O O   . TYR A 1 291 ? 22.316 41.356  20.163  1.00 44.38  ?  514 TYR B O   1 
ATOM   2252 C CB  . TYR A 1 291 ? 24.792 39.350  21.149  1.00 41.60  ?  514 TYR B CB  1 
ATOM   2253 C CG  . TYR A 1 291 ? 25.113 40.659  21.834  1.00 47.36  ?  514 TYR B CG  1 
ATOM   2254 C CD1 . TYR A 1 291 ? 26.082 41.513  21.323  1.00 49.58  ?  514 TYR B CD1 1 
ATOM   2255 C CD2 . TYR A 1 291 ? 24.445 41.042  22.991  1.00 46.75  ?  514 TYR B CD2 1 
ATOM   2256 C CE1 . TYR A 1 291 ? 26.378 42.713  21.947  1.00 55.69  ?  514 TYR B CE1 1 
ATOM   2257 C CE2 . TYR A 1 291 ? 24.734 42.242  23.620  1.00 50.47  ?  514 TYR B CE2 1 
ATOM   2258 C CZ  . TYR A 1 291 ? 25.701 43.072  23.094  1.00 50.88  ?  514 TYR B CZ  1 
ATOM   2259 O OH  . TYR A 1 291 ? 25.992 44.265  23.715  1.00 58.11  ?  514 TYR B OH  1 
ATOM   2260 N N   . PHE A 1 292 ? 21.685 39.403  21.109  1.00 40.32  ?  515 PHE B N   1 
ATOM   2261 C CA  . PHE A 1 292 ? 20.447 39.923  21.671  1.00 41.90  ?  515 PHE B CA  1 
ATOM   2262 C C   . PHE A 1 292 ? 20.704 40.477  23.066  1.00 46.39  ?  515 PHE B C   1 
ATOM   2263 O O   . PHE A 1 292 ? 21.515 39.935  23.824  1.00 43.79  ?  515 PHE B O   1 
ATOM   2264 C CB  . PHE A 1 292 ? 19.376 38.833  21.734  1.00 39.50  ?  515 PHE B CB  1 
ATOM   2265 C CG  . PHE A 1 292 ? 18.849 38.417  20.389  1.00 44.54  ?  515 PHE B CG  1 
ATOM   2266 C CD1 . PHE A 1 292 ? 19.502 37.449  19.641  1.00 39.17  ?  515 PHE B CD1 1 
ATOM   2267 C CD2 . PHE A 1 292 ? 17.696 38.988  19.876  1.00 40.10  ?  515 PHE B CD2 1 
ATOM   2268 C CE1 . PHE A 1 292 ? 19.015 37.062  18.405  1.00 39.07  ?  515 PHE B CE1 1 
ATOM   2269 C CE2 . PHE A 1 292 ? 17.204 38.602  18.638  1.00 39.38  ?  515 PHE B CE2 1 
ATOM   2270 C CZ  . PHE A 1 292 ? 17.866 37.641  17.903  1.00 35.81  ?  515 PHE B CZ  1 
ATOM   2271 N N   . ARG A 1 293 ? 20.007 41.561  23.401  1.00 44.95  ?  516 ARG B N   1 
ATOM   2272 C CA  . ARG A 1 293 ? 20.179 42.229  24.687  1.00 47.87  ?  516 ARG B CA  1 
ATOM   2273 C C   . ARG A 1 293 ? 18.810 42.562  25.257  1.00 47.83  ?  516 ARG B C   1 
ATOM   2274 O O   . ARG A 1 293 ? 18.022 43.262  24.614  1.00 49.49  ?  516 ARG B O   1 
ATOM   2275 C CB  . ARG A 1 293 ? 21.022 43.502  24.539  1.00 50.91  ?  516 ARG B CB  1 
ATOM   2276 C CG  . ARG A 1 293 ? 21.163 44.312  25.817  1.00 49.59  ?  516 ARG B CG  1 
ATOM   2277 C CD  . ARG A 1 293 ? 21.891 45.624  25.561  1.00 46.98  ?  516 ARG B CD  1 
ATOM   2278 N NE  . ARG A 1 293 ? 21.054 46.586  24.850  1.00 53.31  ?  516 ARG B NE  1 
ATOM   2279 C CZ  . ARG A 1 293 ? 21.519 47.595  24.127  1.00 54.82  ?  516 ARG B CZ  1 
ATOM   2280 N NH1 . ARG A 1 293 ? 22.818 47.812  23.997  1.00 53.02  ?  516 ARG B NH1 1 
ATOM   2281 N NH2 . ARG A 1 293 ? 20.660 48.407  23.518  1.00 51.30  ?  516 ARG B NH2 1 
ATOM   2282 N N   . PHE A 1 294 ? 18.530 42.056  26.456  1.00 43.46  ?  517 PHE B N   1 
ATOM   2283 C CA  . PHE A 1 294 ? 17.309 42.424  27.159  1.00 49.72  ?  517 PHE B CA  1 
ATOM   2284 C C   . PHE A 1 294 ? 17.383 43.884  27.587  1.00 54.74  ?  517 PHE B C   1 
ATOM   2285 O O   . PHE A 1 294 ? 18.401 44.333  28.122  1.00 53.16  ?  517 PHE B O   1 
ATOM   2286 C CB  . PHE A 1 294 ? 17.106 41.520  28.375  1.00 49.29  ?  517 PHE B CB  1 
ATOM   2287 C CG  . PHE A 1 294 ? 15.953 41.925  29.247  1.00 53.87  ?  517 PHE B CG  1 
ATOM   2288 C CD1 . PHE A 1 294 ? 14.651 41.832  28.786  1.00 53.35  ?  517 PHE B CD1 1 
ATOM   2289 C CD2 . PHE A 1 294 ? 16.172 42.398  30.530  1.00 56.63  ?  517 PHE B CD2 1 
ATOM   2290 C CE1 . PHE A 1 294 ? 13.587 42.204  29.588  1.00 52.53  ?  517 PHE B CE1 1 
ATOM   2291 C CE2 . PHE A 1 294 ? 15.113 42.770  31.339  1.00 56.33  ?  517 PHE B CE2 1 
ATOM   2292 C CZ  . PHE A 1 294 ? 13.819 42.672  30.866  1.00 54.50  ?  517 PHE B CZ  1 
ATOM   2293 N N   . ASP A 1 295 ? 16.306 44.628  27.348  1.00 52.57  ?  518 ASP B N   1 
ATOM   2294 C CA  . ASP A 1 295 ? 16.298 46.059  27.628  1.00 57.34  ?  518 ASP B CA  1 
ATOM   2295 C C   . ASP A 1 295 ? 15.229 46.486  28.620  1.00 55.91  ?  518 ASP B C   1 
ATOM   2296 O O   . ASP A 1 295 ? 15.521 47.275  29.522  1.00 61.04  ?  518 ASP B O   1 
ATOM   2297 C CB  . ASP A 1 295 ? 16.135 46.853  26.323  1.00 49.99  ?  518 ASP B CB  1 
ATOM   2298 C CG  . ASP A 1 295 ? 17.465 47.275  25.734  1.00 53.98  ?  518 ASP B CG  1 
ATOM   2299 O OD1 . ASP A 1 295 ? 18.499 46.701  26.137  1.00 52.42  ?  518 ASP B OD1 1 
ATOM   2300 O OD2 . ASP A 1 295 ? 17.483 48.181  24.873  1.00 59.92  ?  518 ASP B OD2 1 
ATOM   2301 N N   . SER A 1 296 ? 14.000 45.992  28.488  1.00 52.57  ?  519 SER B N   1 
ATOM   2302 C CA  . SER A 1 296 ? 12.935 46.376  29.406  1.00 53.70  ?  519 SER B CA  1 
ATOM   2303 C C   . SER A 1 296 ? 11.764 45.421  29.238  1.00 56.12  ?  519 SER B C   1 
ATOM   2304 O O   . SER A 1 296 ? 11.630 44.748  28.213  1.00 57.84  ?  519 SER B O   1 
ATOM   2305 C CB  . SER A 1 296 ? 12.479 47.821  29.171  1.00 53.29  ?  519 SER B CB  1 
ATOM   2306 O OG  . SER A 1 296 ? 11.300 47.863  28.386  1.00 58.52  ?  519 SER B OG  1 
ATOM   2307 N N   . TRP A 1 297 ? 10.918 45.373  30.265  1.00 50.87  ?  520 TRP B N   1 
ATOM   2308 C CA  . TRP A 1 297 ? 9.653  44.654  30.202  1.00 51.62  ?  520 TRP B CA  1 
ATOM   2309 C C   . TRP A 1 297 ? 8.582  45.577  29.636  1.00 54.69  ?  520 TRP B C   1 
ATOM   2310 O O   . TRP A 1 297 ? 8.358  46.671  30.162  1.00 56.44  ?  520 TRP B O   1 
ATOM   2311 C CB  . TRP A 1 297 ? 9.233  44.159  31.586  1.00 53.73  ?  520 TRP B CB  1 
ATOM   2312 C CG  . TRP A 1 297 ? 10.081 43.056  32.134  1.00 52.17  ?  520 TRP B CG  1 
ATOM   2313 C CD1 . TRP A 1 297 ? 11.061 43.166  33.079  1.00 55.50  ?  520 TRP B CD1 1 
ATOM   2314 C CD2 . TRP A 1 297 ? 10.019 41.669  31.781  1.00 55.82  ?  520 TRP B CD2 1 
ATOM   2315 N NE1 . TRP A 1 297 ? 11.615 41.934  33.333  1.00 53.87  ?  520 TRP B NE1 1 
ATOM   2316 C CE2 . TRP A 1 297 ? 10.992 40.999  32.549  1.00 54.20  ?  520 TRP B CE2 1 
ATOM   2317 C CE3 . TRP A 1 297 ? 9.235  40.931  30.888  1.00 54.81  ?  520 TRP B CE3 1 
ATOM   2318 C CZ2 . TRP A 1 297 ? 11.204 39.625  32.449  1.00 51.64  ?  520 TRP B CZ2 1 
ATOM   2319 C CZ3 . TRP A 1 297 ? 9.445  39.570  30.792  1.00 47.79  ?  520 TRP B CZ3 1 
ATOM   2320 C CH2 . TRP A 1 297 ? 10.422 38.930  31.567  1.00 53.59  ?  520 TRP B CH2 1 
ATOM   2321 N N   . VAL A 1 298 ? 7.929  45.138  28.563  1.00 49.28  ?  521 VAL B N   1 
ATOM   2322 C CA  . VAL A 1 298 ? 6.816  45.886  27.993  1.00 47.41  ?  521 VAL B CA  1 
ATOM   2323 C C   . VAL A 1 298 ? 5.573  45.013  28.084  1.00 52.07  ?  521 VAL B C   1 
ATOM   2324 O O   . VAL A 1 298 ? 5.601  43.935  28.688  1.00 52.85  ?  521 VAL B O   1 
ATOM   2325 C CB  . VAL A 1 298 ? 7.103  46.311  26.540  1.00 52.48  ?  521 VAL B CB  1 
ATOM   2326 C CG1 . VAL A 1 298 ? 8.334  47.208  26.476  1.00 48.87  ?  521 VAL B CG1 1 
ATOM   2327 C CG2 . VAL A 1 298 ? 7.281  45.096  25.659  1.00 49.51  ?  521 VAL B CG2 1 
ATOM   2328 N N   . ASN A 1 299 ? 4.472  45.478  27.512  1.00 54.04  ?  522 ASN B N   1 
ATOM   2329 C CA  . ASN A 1 299 ? 3.269  44.675  27.424  1.00 59.43  ?  522 ASN B CA  1 
ATOM   2330 C C   . ASN A 1 299 ? 3.108  44.172  25.996  1.00 62.38  ?  522 ASN B C   1 
ATOM   2331 O O   . ASN A 1 299 ? 3.948  44.410  25.112  1.00 59.43  ?  522 ASN B O   1 
ATOM   2332 C CB  . ASN A 1 299 ? 2.034  45.459  27.898  1.00 61.73  ?  522 ASN B CB  1 
ATOM   2333 C CG  . ASN A 1 299 ? 1.832  46.768  27.145  1.00 64.37  ?  522 ASN B CG  1 
ATOM   2334 O OD1 . ASN A 1 299 ? 2.432  46.988  26.094  1.00 61.29  ?  522 ASN B OD1 1 
ATOM   2335 N ND2 . ASN A 1 299 ? 0.992  47.650  27.688  1.00 56.04  ?  522 ASN B ND2 1 
ATOM   2336 N N   . GLN A 1 300 ? 1.991  43.480  25.789  1.00 64.49  ?  523 GLN B N   1 
ATOM   2337 C CA  . GLN A 1 300 ? 1.727  42.798  24.534  1.00 63.98  ?  523 GLN B CA  1 
ATOM   2338 C C   . GLN A 1 300 ? 1.318  43.756  23.425  1.00 64.36  ?  523 GLN B C   1 
ATOM   2339 O O   . GLN A 1 300 ? 1.374  43.381  22.251  1.00 63.89  ?  523 GLN B O   1 
ATOM   2340 C CB  . GLN A 1 300 ? 0.647  41.765  24.783  1.00 66.20  ?  523 GLN B CB  1 
ATOM   2341 C CG  . GLN A 1 300 ? -0.265 42.209  25.872  1.00 72.41  ?  523 GLN B CG  1 
ATOM   2342 C CD  . GLN A 1 300 ? -1.105 41.066  26.342  1.00 82.57  ?  523 GLN B CD  1 
ATOM   2343 O OE1 . GLN A 1 300 ? -1.438 40.183  25.580  1.00 82.44  ?  523 GLN B OE1 1 
ATOM   2344 N NE2 . GLN A 1 300 ? -1.558 41.147  27.578  1.00 82.97  ?  523 GLN B NE2 1 
ATOM   2345 N N   . PHE A 1 301 ? 0.900  44.973  23.767  1.00 62.17  ?  524 PHE B N   1 
ATOM   2346 C CA  . PHE A 1 301 ? 0.448  45.954  22.792  1.00 61.58  ?  524 PHE B CA  1 
ATOM   2347 C C   . PHE A 1 301 ? 1.556  46.905  22.373  1.00 56.34  ?  524 PHE B C   1 
ATOM   2348 O O   . PHE A 1 301 ? 1.288  47.872  21.656  1.00 63.70  ?  524 PHE B O   1 
ATOM   2349 C CB  . PHE A 1 301 ? -0.738 46.734  23.358  1.00 60.55  ?  524 PHE B CB  1 
ATOM   2350 C CG  . PHE A 1 301 ? -1.865 45.859  23.841  1.00 63.22  ?  524 PHE B CG  1 
ATOM   2351 C CD1 . PHE A 1 301 ? -2.695 45.214  22.937  1.00 64.96  ?  524 PHE B CD1 1 
ATOM   2352 C CD2 . PHE A 1 301 ? -2.095 45.684  25.196  1.00 67.13  ?  524 PHE B CD2 1 
ATOM   2353 C CE1 . PHE A 1 301 ? -3.731 44.413  23.376  1.00 65.19  ?  524 PHE B CE1 1 
ATOM   2354 C CE2 . PHE A 1 301 ? -3.132 44.884  25.640  1.00 69.36  ?  524 PHE B CE2 1 
ATOM   2355 C CZ  . PHE A 1 301 ? -3.951 44.248  24.728  1.00 67.96  ?  524 PHE B CZ  1 
ATOM   2356 N N   . TYR A 1 302 ? 2.791  46.653  22.802  1.00 53.02  ?  525 TYR B N   1 
ATOM   2357 C CA  . TYR A 1 302 ? 3.914  47.467  22.358  1.00 54.08  ?  525 TYR B CA  1 
ATOM   2358 C C   . TYR A 1 302 ? 4.084  47.341  20.850  1.00 59.91  ?  525 TYR B C   1 
ATOM   2359 O O   . TYR A 1 302 ? 3.838  46.282  20.266  1.00 62.99  ?  525 TYR B O   1 
ATOM   2360 C CB  . TYR A 1 302 ? 5.194  47.038  23.080  1.00 50.62  ?  525 TYR B CB  1 
ATOM   2361 C CG  . TYR A 1 302 ? 6.399  47.908  22.795  1.00 54.02  ?  525 TYR B CG  1 
ATOM   2362 C CD1 . TYR A 1 302 ? 6.656  49.046  23.550  1.00 56.10  ?  525 TYR B CD1 1 
ATOM   2363 C CD2 . TYR A 1 302 ? 7.286  47.586  21.775  1.00 55.71  ?  525 TYR B CD2 1 
ATOM   2364 C CE1 . TYR A 1 302 ? 7.761  49.841  23.293  1.00 56.06  ?  525 TYR B CE1 1 
ATOM   2365 C CE2 . TYR A 1 302 ? 8.391  48.375  21.510  1.00 58.55  ?  525 TYR B CE2 1 
ATOM   2366 C CZ  . TYR A 1 302 ? 8.624  49.500  22.271  1.00 58.51  ?  525 TYR B CZ  1 
ATOM   2367 O OH  . TYR A 1 302 ? 9.723  50.281  22.005  1.00 62.64  ?  525 TYR B OH  1 
ATOM   2368 N N   . THR A 1 303 ? 4.491  48.433  20.215  1.00 56.47  ?  526 THR B N   1 
ATOM   2369 C CA  . THR A 1 303 ? 4.676  48.477  18.771  1.00 57.32  ?  526 THR B CA  1 
ATOM   2370 C C   . THR A 1 303 ? 6.167  48.551  18.470  1.00 58.67  ?  526 THR B C   1 
ATOM   2371 O O   . THR A 1 303 ? 6.827  49.537  18.816  1.00 55.64  ?  526 THR B O   1 
ATOM   2372 C CB  . THR A 1 303 ? 3.936  49.665  18.155  1.00 58.12  ?  526 THR B CB  1 
ATOM   2373 O OG1 . THR A 1 303 ? 2.528  49.399  18.151  1.00 61.18  ?  526 THR B OG1 1 
ATOM   2374 C CG2 . THR A 1 303 ? 4.399  49.896  16.723  1.00 53.68  ?  526 THR B CG2 1 
ATOM   2375 N N   . LEU A 1 304 ? 6.690  47.508  17.830  1.00 58.48  ?  527 LEU B N   1 
ATOM   2376 C CA  . LEU A 1 304 ? 8.106  47.447  17.510  1.00 54.50  ?  527 LEU B CA  1 
ATOM   2377 C C   . LEU A 1 304 ? 8.432  48.329  16.311  1.00 49.89  ?  527 LEU B C   1 
ATOM   2378 O O   . LEU A 1 304 ? 7.581  48.595  15.458  1.00 49.01  ?  527 LEU B O   1 
ATOM   2379 C CB  . LEU A 1 304 ? 8.533  46.007  17.211  1.00 49.77  ?  527 LEU B CB  1 
ATOM   2380 C CG  . LEU A 1 304 ? 8.177  44.925  18.232  1.00 50.65  ?  527 LEU B CG  1 
ATOM   2381 C CD1 . LEU A 1 304 ? 8.043  43.572  17.547  1.00 47.47  ?  527 LEU B CD1 1 
ATOM   2382 C CD2 . LEU A 1 304 ? 9.221  44.871  19.335  1.00 48.94  ?  527 LEU B CD2 1 
ATOM   2383 N N   . ALA A 1 305 ? 9.679  48.784  16.259  1.00 44.86  ?  528 ALA B N   1 
ATOM   2384 C CA  . ALA A 1 305 ? 10.169 49.437  15.057  1.00 49.05  ?  528 ALA B CA  1 
ATOM   2385 C C   . ALA A 1 305 ? 10.162 48.435  13.903  1.00 60.76  ?  528 ALA B C   1 
ATOM   2386 O O   . ALA A 1 305 ? 10.535 47.270  14.089  1.00 54.41  ?  528 ALA B O   1 
ATOM   2387 C CB  . ALA A 1 305 ? 11.579 49.987  15.276  1.00 47.12  ?  528 ALA B CB  1 
ATOM   2388 N N   . PRO A 1 306 ? 9.735  48.845  12.703  1.00 62.45  ?  529 PRO B N   1 
ATOM   2389 C CA  . PRO A 1 306 ? 9.554  47.890  11.584  1.00 61.59  ?  529 PRO B CA  1 
ATOM   2390 C C   . PRO A 1 306 ? 10.860 47.439  10.932  1.00 68.82  ?  529 PRO B C   1 
ATOM   2391 O O   . PRO A 1 306 ? 11.274 47.897  9.867   1.00 77.47  ?  529 PRO B O   1 
ATOM   2392 C CB  . PRO A 1 306 ? 8.673  48.675  10.607  1.00 61.16  ?  529 PRO B CB  1 
ATOM   2393 C CG  . PRO A 1 306 ? 8.348  49.997  11.276  1.00 55.11  ?  529 PRO B CG  1 
ATOM   2394 C CD  . PRO A 1 306 ? 9.385  50.218  12.314  1.00 57.60  ?  529 PRO B CD  1 
ATOM   2395 N N   . MET A 1 307 ? 11.537 46.507  11.595  1.00 64.92  ?  530 MET B N   1 
ATOM   2396 C CA  . MET A 1 307 ? 12.755 45.900  11.068  1.00 66.36  ?  530 MET B CA  1 
ATOM   2397 C C   . MET A 1 307 ? 12.657 44.395  11.302  1.00 64.66  ?  530 MET B C   1 
ATOM   2398 O O   . MET A 1 307 ? 11.570 43.848  11.518  1.00 62.19  ?  530 MET B O   1 
ATOM   2399 C CB  . MET A 1 307 ? 14.007 46.523  11.710  1.00 71.40  ?  530 MET B CB  1 
ATOM   2400 C CG  . MET A 1 307 ? 13.908 48.019  11.995  1.00 66.61  ?  530 MET B CG  1 
ATOM   2401 S SD  . MET A 1 307 ? 15.511 48.829  12.154  1.00 93.46  ?  530 MET B SD  1 
ATOM   2402 C CE  . MET A 1 307 ? 15.273 49.776  13.658  1.00 77.46  ?  530 MET B CE  1 
ATOM   2403 N N   . GLY A 1 308 ? 13.798 43.712  11.258  1.00 68.17  ?  531 GLY B N   1 
ATOM   2404 C CA  . GLY A 1 308 ? 13.865 42.293  11.563  1.00 57.33  ?  531 GLY B CA  1 
ATOM   2405 C C   . GLY A 1 308 ? 13.018 41.395  10.681  1.00 44.57  ?  531 GLY B C   1 
ATOM   2406 O O   . GLY A 1 308 ? 12.938 41.591  9.469   1.00 56.33  ?  531 GLY B O   1 
ATOM   2407 N N   . GLN B 2 1   ? 20.710 55.733  2.113   1.00 70.78  ?  1   GLN C N   1 
ATOM   2408 C CA  . GLN B 2 1   ? 21.575 55.694  3.287   1.00 81.76  ?  1   GLN C CA  1 
ATOM   2409 C C   . GLN B 2 1   ? 23.033 55.500  2.882   1.00 75.69  ?  1   GLN C C   1 
ATOM   2410 O O   . GLN B 2 1   ? 23.930 56.155  3.413   1.00 73.42  ?  1   GLN C O   1 
ATOM   2411 C CB  . GLN B 2 1   ? 21.139 54.581  4.241   1.00 84.41  ?  1   GLN C CB  1 
ATOM   2412 C CG  . GLN B 2 1   ? 21.462 54.854  5.699   1.00 86.03  ?  1   GLN C CG  1 
ATOM   2413 C CD  . GLN B 2 1   ? 20.410 55.708  6.376   1.00 93.86  ?  1   GLN C CD  1 
ATOM   2414 O OE1 . GLN B 2 1   ? 19.243 55.323  6.466   1.00 95.37  ?  1   GLN C OE1 1 
ATOM   2415 N NE2 . GLN B 2 1   ? 20.816 56.878  6.858   1.00 93.23  ?  1   GLN C NE2 1 
ATOM   2416 N N   . VAL B 2 2   ? 23.259 54.587  1.941   1.00 68.59  ?  2   VAL C N   1 
ATOM   2417 C CA  . VAL B 2 2   ? 24.587 54.315  1.399   1.00 65.44  ?  2   VAL C CA  1 
ATOM   2418 C C   . VAL B 2 2   ? 24.459 54.210  -0.114  1.00 61.31  ?  2   VAL C C   1 
ATOM   2419 O O   . VAL B 2 2   ? 23.546 53.548  -0.619  1.00 54.74  ?  2   VAL C O   1 
ATOM   2420 C CB  . VAL B 2 2   ? 25.201 53.028  1.987   1.00 60.69  ?  2   VAL C CB  1 
ATOM   2421 C CG1 . VAL B 2 2   ? 26.458 52.632  1.225   1.00 57.58  ?  2   VAL C CG1 1 
ATOM   2422 C CG2 . VAL B 2 2   ? 25.508 53.209  3.465   1.00 59.18  ?  2   VAL C CG2 1 
ATOM   2423 N N   . GLN B 2 3   ? 25.355 54.875  -0.837  1.00 60.97  ?  3   GLN C N   1 
ATOM   2424 C CA  . GLN B 2 3   ? 25.368 54.854  -2.293  1.00 60.24  ?  3   GLN C CA  1 
ATOM   2425 C C   . GLN B 2 3   ? 26.682 54.263  -2.782  1.00 55.33  ?  3   GLN C C   1 
ATOM   2426 O O   . GLN B 2 3   ? 27.751 54.576  -2.247  1.00 54.74  ?  3   GLN C O   1 
ATOM   2427 C CB  . GLN B 2 3   ? 25.172 56.261  -2.871  1.00 63.06  ?  3   GLN C CB  1 
ATOM   2428 C CG  . GLN B 2 3   ? 23.714 56.658  -3.057  1.00 68.48  ?  3   GLN C CG  1 
ATOM   2429 C CD  . GLN B 2 3   ? 23.418 58.057  -2.547  1.00 77.85  ?  3   GLN C CD  1 
ATOM   2430 O OE1 . GLN B 2 3   ? 24.325 58.866  -2.350  1.00 86.46  ?  3   GLN C OE1 1 
ATOM   2431 N NE2 . GLN B 2 3   ? 22.139 58.350  -2.330  1.00 75.17  ?  3   GLN C NE2 1 
ATOM   2432 N N   . LEU B 2 4   ? 26.596 53.408  -3.798  1.00 49.12  ?  4   LEU C N   1 
ATOM   2433 C CA  . LEU B 2 4   ? 27.751 52.706  -4.333  1.00 51.77  ?  4   LEU C CA  1 
ATOM   2434 C C   . LEU B 2 4   ? 27.913 53.015  -5.815  1.00 49.84  ?  4   LEU C C   1 
ATOM   2435 O O   . LEU B 2 4   ? 26.939 53.295  -6.520  1.00 50.89  ?  4   LEU C O   1 
ATOM   2436 C CB  . LEU B 2 4   ? 27.625 51.189  -4.124  1.00 45.34  ?  4   LEU C CB  1 
ATOM   2437 C CG  . LEU B 2 4   ? 27.270 50.725  -2.709  1.00 46.67  ?  4   LEU C CG  1 
ATOM   2438 C CD1 . LEU B 2 4   ? 27.079 49.213  -2.662  1.00 41.82  ?  4   LEU C CD1 1 
ATOM   2439 C CD2 . LEU B 2 4   ? 28.332 51.167  -1.715  1.00 43.29  ?  4   LEU C CD2 1 
ATOM   2440 N N   . GLN B 2 5   ? 29.159 52.959  -6.283  1.00 51.67  ?  5   GLN C N   1 
ATOM   2441 C CA  . GLN B 2 5   ? 29.478 53.259  -7.675  1.00 50.90  ?  5   GLN C CA  1 
ATOM   2442 C C   . GLN B 2 5   ? 30.672 52.416  -8.095  1.00 52.51  ?  5   GLN C C   1 
ATOM   2443 O O   . GLN B 2 5   ? 31.756 52.551  -7.519  1.00 50.38  ?  5   GLN C O   1 
ATOM   2444 C CB  . GLN B 2 5   ? 29.778 54.748  -7.862  1.00 57.20  ?  5   GLN C CB  1 
ATOM   2445 C CG  . GLN B 2 5   ? 30.130 55.138  -9.287  1.00 62.65  ?  5   GLN C CG  1 
ATOM   2446 C CD  . GLN B 2 5   ? 28.917 55.179  -10.193 1.00 65.38  ?  5   GLN C CD  1 
ATOM   2447 O OE1 . GLN B 2 5   ? 28.801 54.390  -11.132 1.00 72.44  ?  5   GLN C OE1 1 
ATOM   2448 N NE2 . GLN B 2 5   ? 28.002 56.102  -9.915  1.00 59.82  ?  5   GLN C NE2 1 
ATOM   2449 N N   . GLU B 2 6   ? 30.475 51.561  -9.093  1.00 54.15  ?  6   GLU C N   1 
ATOM   2450 C CA  . GLU B 2 6   ? 31.533 50.695  -9.590  1.00 54.54  ?  6   GLU C CA  1 
ATOM   2451 C C   . GLU B 2 6   ? 32.340 51.393  -10.679 1.00 51.58  ?  6   GLU C C   1 
ATOM   2452 O O   . GLU B 2 6   ? 31.899 52.367  -11.292 1.00 53.43  ?  6   GLU C O   1 
ATOM   2453 C CB  . GLU B 2 6   ? 30.959 49.390  -10.143 1.00 52.18  ?  6   GLU C CB  1 
ATOM   2454 C CG  . GLU B 2 6   ? 30.153 48.594  -9.147  1.00 53.72  ?  6   GLU C CG  1 
ATOM   2455 C CD  . GLU B 2 6   ? 28.666 48.735  -9.378  1.00 55.98  ?  6   GLU C CD  1 
ATOM   2456 O OE1 . GLU B 2 6   ? 28.248 49.769  -9.941  1.00 53.92  ?  6   GLU C OE1 1 
ATOM   2457 O OE2 . GLU B 2 6   ? 27.916 47.812  -9.004  1.00 51.04  ?  6   GLU C OE2 1 
ATOM   2458 N N   . SER B 2 7   ? 33.536 50.864  -10.921 1.00 47.00  ?  7   SER C N   1 
ATOM   2459 C CA  . SER B 2 7   ? 34.430 51.378  -11.946 1.00 52.51  ?  7   SER C CA  1 
ATOM   2460 C C   . SER B 2 7   ? 35.506 50.340  -12.214 1.00 45.72  ?  7   SER C C   1 
ATOM   2461 O O   . SER B 2 7   ? 35.823 49.525  -11.345 1.00 48.63  ?  7   SER C O   1 
ATOM   2462 C CB  . SER B 2 7   ? 35.067 52.705  -11.522 1.00 52.80  ?  7   SER C CB  1 
ATOM   2463 O OG  . SER B 2 7   ? 36.121 52.484  -10.601 1.00 56.89  ?  7   SER C OG  1 
ATOM   2464 N N   . GLY B 2 8   ? 36.060 50.379  -13.419 1.00 52.80  ?  8   GLY C N   1 
ATOM   2465 C CA  . GLY B 2 8   ? 37.188 49.546  -13.763 1.00 41.47  ?  8   GLY C CA  1 
ATOM   2466 C C   . GLY B 2 8   ? 36.878 48.261  -14.497 1.00 47.12  ?  8   GLY C C   1 
ATOM   2467 O O   . GLY B 2 8   ? 37.697 47.337  -14.447 1.00 48.96  ?  8   GLY C O   1 
ATOM   2468 N N   . GLY B 2 9   ? 35.733 48.163  -15.165 1.00 45.52  ?  9   GLY C N   1 
ATOM   2469 C CA  . GLY B 2 9   ? 35.410 47.018  -15.990 1.00 47.02  ?  9   GLY C CA  1 
ATOM   2470 C C   . GLY B 2 9   ? 35.877 47.209  -17.419 1.00 47.84  ?  9   GLY C C   1 
ATOM   2471 O O   . GLY B 2 9   ? 36.743 48.036  -17.714 1.00 47.46  ?  9   GLY C O   1 
ATOM   2472 N N   . GLY B 2 10  ? 35.294 46.418  -18.323 1.00 45.42  ?  10  GLY C N   1 
ATOM   2473 C CA  . GLY B 2 10  ? 35.539 46.599  -19.735 1.00 49.22  ?  10  GLY C CA  1 
ATOM   2474 C C   . GLY B 2 10  ? 36.011 45.319  -20.393 1.00 44.89  ?  10  GLY C C   1 
ATOM   2475 O O   . GLY B 2 10  ? 35.824 44.217  -19.865 1.00 44.05  ?  10  GLY C O   1 
ATOM   2476 N N   . LEU B 2 11  ? 36.625 45.481  -21.565 1.00 44.89  ?  11  LEU C N   1 
ATOM   2477 C CA  . LEU B 2 11  ? 37.097 44.365  -22.372 1.00 45.86  ?  11  LEU C CA  1 
ATOM   2478 C C   . LEU B 2 11  ? 38.483 43.922  -21.922 1.00 49.62  ?  11  LEU C C   1 
ATOM   2479 O O   . LEU B 2 11  ? 39.334 44.748  -21.581 1.00 52.27  ?  11  LEU C O   1 
ATOM   2480 C CB  . LEU B 2 11  ? 37.134 44.756  -23.850 1.00 51.08  ?  11  LEU C CB  1 
ATOM   2481 C CG  . LEU B 2 11  ? 36.177 44.025  -24.791 1.00 47.31  ?  11  LEU C CG  1 
ATOM   2482 C CD1 . LEU B 2 11  ? 36.251 44.619  -26.190 1.00 52.28  ?  11  LEU C CD1 1 
ATOM   2483 C CD2 . LEU B 2 11  ? 36.480 42.535  -24.820 1.00 49.11  ?  11  LEU C CD2 1 
ATOM   2484 N N   . VAL B 2 12  ? 38.707 42.608  -21.936 1.00 45.98  ?  12  VAL C N   1 
ATOM   2485 C CA  . VAL B 2 12  ? 39.974 42.033  -21.499 1.00 46.89  ?  12  VAL C CA  1 
ATOM   2486 C C   . VAL B 2 12  ? 40.179 40.712  -22.229 1.00 48.54  ?  12  VAL C C   1 
ATOM   2487 O O   . VAL B 2 12  ? 39.223 39.990  -22.525 1.00 50.58  ?  12  VAL C O   1 
ATOM   2488 C CB  . VAL B 2 12  ? 40.006 41.853  -19.960 1.00 49.79  ?  12  VAL C CB  1 
ATOM   2489 C CG1 . VAL B 2 12  ? 38.883 40.932  -19.501 1.00 45.09  ?  12  VAL C CG1 1 
ATOM   2490 C CG2 . VAL B 2 12  ? 41.365 41.345  -19.491 1.00 49.28  ?  12  VAL C CG2 1 
ATOM   2491 N N   . GLN B 2 13  ? 41.438 40.409  -22.538 1.00 49.88  ?  13  GLN C N   1 
ATOM   2492 C CA  . GLN B 2 13  ? 41.778 39.168  -23.213 1.00 48.67  ?  13  GLN C CA  1 
ATOM   2493 C C   . GLN B 2 13  ? 41.590 37.977  -22.273 1.00 53.26  ?  13  GLN C C   1 
ATOM   2494 O O   . GLN B 2 13  ? 41.645 38.124  -21.049 1.00 51.22  ?  13  GLN C O   1 
ATOM   2495 C CB  . GLN B 2 13  ? 43.222 39.212  -23.708 1.00 52.13  ?  13  GLN C CB  1 
ATOM   2496 C CG  . GLN B 2 13  ? 43.506 40.222  -24.814 1.00 51.03  ?  13  GLN C CG  1 
ATOM   2497 C CD  . GLN B 2 13  ? 42.770 39.908  -26.102 1.00 61.39  ?  13  GLN C CD  1 
ATOM   2498 O OE1 . GLN B 2 13  ? 41.979 40.714  -26.592 1.00 61.86  ?  13  GLN C OE1 1 
ATOM   2499 N NE2 . GLN B 2 13  ? 43.016 38.725  -26.651 1.00 62.33  ?  13  GLN C NE2 1 
ATOM   2500 N N   . PRO B 2 14  ? 41.359 36.783  -22.823 1.00 51.79  ?  14  PRO C N   1 
ATOM   2501 C CA  . PRO B 2 14  ? 41.358 35.580  -21.985 1.00 48.98  ?  14  PRO C CA  1 
ATOM   2502 C C   . PRO B 2 14  ? 42.706 35.391  -21.305 1.00 51.09  ?  14  PRO C C   1 
ATOM   2503 O O   . PRO B 2 14  ? 43.762 35.544  -21.922 1.00 53.49  ?  14  PRO C O   1 
ATOM   2504 C CB  . PRO B 2 14  ? 41.061 34.453  -22.981 1.00 47.47  ?  14  PRO C CB  1 
ATOM   2505 C CG  . PRO B 2 14  ? 40.340 35.122  -24.100 1.00 51.76  ?  14  PRO C CG  1 
ATOM   2506 C CD  . PRO B 2 14  ? 40.945 36.494  -24.207 1.00 47.80  ?  14  PRO C CD  1 
ATOM   2507 N N   . GLY B 2 15  ? 42.658 35.060  -20.017 1.00 50.28  ?  15  GLY C N   1 
ATOM   2508 C CA  . GLY B 2 15  ? 43.854 34.998  -19.208 1.00 46.74  ?  15  GLY C CA  1 
ATOM   2509 C C   . GLY B 2 15  ? 44.346 36.336  -18.702 1.00 50.33  ?  15  GLY C C   1 
ATOM   2510 O O   . GLY B 2 15  ? 45.360 36.376  -17.993 1.00 56.79  ?  15  GLY C O   1 
ATOM   2511 N N   . GLY B 2 16  ? 43.666 37.427  -19.041 1.00 50.52  ?  16  GLY C N   1 
ATOM   2512 C CA  . GLY B 2 16  ? 44.050 38.746  -18.586 1.00 48.32  ?  16  GLY C CA  1 
ATOM   2513 C C   . GLY B 2 16  ? 43.639 38.997  -17.148 1.00 49.19  ?  16  GLY C C   1 
ATOM   2514 O O   . GLY B 2 16  ? 43.254 38.094  -16.404 1.00 51.75  ?  16  GLY C O   1 
ATOM   2515 N N   . SER B 2 17  ? 43.720 40.269  -16.759 1.00 47.35  ?  17  SER C N   1 
ATOM   2516 C CA  . SER B 2 17  ? 43.449 40.666  -15.387 1.00 49.72  ?  17  SER C CA  1 
ATOM   2517 C C   . SER B 2 17  ? 42.708 41.993  -15.363 1.00 50.65  ?  17  SER C C   1 
ATOM   2518 O O   . SER B 2 17  ? 42.882 42.842  -16.241 1.00 49.99  ?  17  SER C O   1 
ATOM   2519 C CB  . SER B 2 17  ? 44.740 40.776  -14.569 1.00 46.59  ?  17  SER C CB  1 
ATOM   2520 O OG  . SER B 2 17  ? 45.350 39.505  -14.414 1.00 56.18  ?  17  SER C OG  1 
ATOM   2521 N N   . LEU B 2 18  ? 41.877 42.162  -14.337 1.00 43.07  ?  18  LEU C N   1 
ATOM   2522 C CA  . LEU B 2 18  ? 41.138 43.397  -14.124 1.00 48.15  ?  18  LEU C CA  1 
ATOM   2523 C C   . LEU B 2 18  ? 41.009 43.619  -12.625 1.00 47.74  ?  18  LEU C C   1 
ATOM   2524 O O   . LEU B 2 18  ? 41.056 42.672  -11.836 1.00 48.19  ?  18  LEU C O   1 
ATOM   2525 C CB  . LEU B 2 18  ? 39.751 43.352  -14.777 1.00 43.23  ?  18  LEU C CB  1 
ATOM   2526 C CG  . LEU B 2 18  ? 39.605 43.983  -16.163 1.00 53.89  ?  18  LEU C CG  1 
ATOM   2527 C CD1 . LEU B 2 18  ? 38.340 43.481  -16.853 1.00 50.56  ?  18  LEU C CD1 1 
ATOM   2528 C CD2 . LEU B 2 18  ? 39.632 45.499  -16.091 1.00 53.89  ?  18  LEU C CD2 1 
ATOM   2529 N N   . ARG B 2 19  ? 40.843 44.882  -12.238 1.00 48.40  ?  19  ARG C N   1 
ATOM   2530 C CA  . ARG B 2 19  ? 40.644 45.253  -10.840 1.00 48.64  ?  19  ARG C CA  1 
ATOM   2531 C C   . ARG B 2 19  ? 39.432 46.171  -10.756 1.00 46.55  ?  19  ARG C C   1 
ATOM   2532 O O   . ARG B 2 19  ? 39.480 47.310  -11.231 1.00 46.21  ?  19  ARG C O   1 
ATOM   2533 C CB  . ARG B 2 19  ? 41.884 45.931  -10.259 1.00 43.32  ?  19  ARG C CB  1 
ATOM   2534 C CG  . ARG B 2 19  ? 41.737 46.328  -8.795  1.00 49.77  ?  19  ARG C CG  1 
ATOM   2535 C CD  . ARG B 2 19  ? 43.076 46.697  -8.176  1.00 52.04  ?  19  ARG C CD  1 
ATOM   2536 N NE  . ARG B 2 19  ? 42.920 47.299  -6.857  1.00 61.76  ?  19  ARG C NE  1 
ATOM   2537 C CZ  . ARG B 2 19  ? 43.126 46.663  -5.712  1.00 62.59  ?  19  ARG C CZ  1 
ATOM   2538 N NH1 . ARG B 2 19  ? 43.497 45.394  -5.684  1.00 57.53  ?  19  ARG C NH1 1 
ATOM   2539 N NH2 . ARG B 2 19  ? 42.957 47.317  -4.567  1.00 61.30  ?  19  ARG C NH2 1 
ATOM   2540 N N   . LEU B 2 20  ? 38.351 45.674  -10.164 1.00 43.50  ?  20  LEU C N   1 
ATOM   2541 C CA  . LEU B 2 20  ? 37.143 46.461  -9.975  1.00 49.52  ?  20  LEU C CA  1 
ATOM   2542 C C   . LEU B 2 20  ? 37.197 47.204  -8.646  1.00 49.81  ?  20  LEU C C   1 
ATOM   2543 O O   . LEU B 2 20  ? 37.814 46.746  -7.681  1.00 46.59  ?  20  LEU C O   1 
ATOM   2544 C CB  . LEU B 2 20  ? 35.899 45.572  -10.021 1.00 45.08  ?  20  LEU C CB  1 
ATOM   2545 C CG  . LEU B 2 20  ? 35.756 44.622  -11.210 1.00 50.30  ?  20  LEU C CG  1 
ATOM   2546 C CD1 . LEU B 2 20  ? 34.516 43.757  -11.042 1.00 45.43  ?  20  LEU C CD1 1 
ATOM   2547 C CD2 . LEU B 2 20  ? 35.703 45.396  -12.519 1.00 46.39  ?  20  LEU C CD2 1 
ATOM   2548 N N   . SER B 2 21  ? 36.538 48.361  -8.607  1.00 48.80  ?  21  SER C N   1 
ATOM   2549 C CA  . SER B 2 21  ? 36.505 49.200  -7.418  1.00 49.67  ?  21  SER C CA  1 
ATOM   2550 C C   . SER B 2 21  ? 35.085 49.686  -7.178  1.00 46.81  ?  21  SER C C   1 
ATOM   2551 O O   . SER B 2 21  ? 34.377 50.046  -8.123  1.00 49.44  ?  21  SER C O   1 
ATOM   2552 C CB  . SER B 2 21  ? 37.451 50.399  -7.554  1.00 50.36  ?  21  SER C CB  1 
ATOM   2553 O OG  . SER B 2 21  ? 38.789 49.975  -7.742  1.00 53.70  ?  21  SER C OG  1 
ATOM   2554 N N   . CYS B 2 22  ? 34.674 49.691  -5.911  1.00 47.11  ?  22  CYS C N   1 
ATOM   2555 C CA  . CYS B 2 22  ? 33.360 50.172  -5.501  1.00 52.54  ?  22  CYS C CA  1 
ATOM   2556 C C   . CYS B 2 22  ? 33.549 51.388  -4.608  1.00 53.90  ?  22  CYS C C   1 
ATOM   2557 O O   . CYS B 2 22  ? 34.171 51.290  -3.546  1.00 56.42  ?  22  CYS C O   1 
ATOM   2558 C CB  . CYS B 2 22  ? 32.576 49.083  -4.767  1.00 49.10  ?  22  CYS C CB  1 
ATOM   2559 S SG  . CYS B 2 22  ? 30.886 49.545  -4.289  1.00 60.81  ?  22  CYS C SG  1 
ATOM   2560 N N   . ALA B 2 23  ? 33.018 52.529  -5.038  1.00 50.55  ?  23  ALA C N   1 
ATOM   2561 C CA  . ALA B 2 23  ? 33.101 53.763  -4.268  1.00 50.35  ?  23  ALA C CA  1 
ATOM   2562 C C   . ALA B 2 23  ? 31.846 53.909  -3.418  1.00 53.54  ?  23  ALA C C   1 
ATOM   2563 O O   . ALA B 2 23  ? 30.733 53.992  -3.953  1.00 54.21  ?  23  ALA C O   1 
ATOM   2564 C CB  . ALA B 2 23  ? 33.274 54.970  -5.189  1.00 40.01  ?  23  ALA C CB  1 
ATOM   2565 N N   . ALA B 2 24  ? 32.025 53.934  -2.100  1.00 47.29  ?  24  ALA C N   1 
ATOM   2566 C CA  . ALA B 2 24  ? 30.919 54.061  -1.161  1.00 52.73  ?  24  ALA C CA  1 
ATOM   2567 C C   . ALA B 2 24  ? 30.867 55.475  -0.599  1.00 57.32  ?  24  ALA C C   1 
ATOM   2568 O O   . ALA B 2 24  ? 31.906 56.093  -0.346  1.00 55.30  ?  24  ALA C O   1 
ATOM   2569 C CB  . ALA B 2 24  ? 31.049 53.050  -0.017  1.00 49.26  ?  24  ALA C CB  1 
ATOM   2570 N N   . SER B 2 25  ? 29.650 55.980  -0.404  1.00 55.01  ?  25  SER C N   1 
ATOM   2571 C CA  . SER B 2 25  ? 29.439 57.327  0.093   1.00 61.09  ?  25  SER C CA  1 
ATOM   2572 C C   . SER B 2 25  ? 28.267 57.330  1.062   1.00 64.10  ?  25  SER C C   1 
ATOM   2573 O O   . SER B 2 25  ? 27.323 56.551  0.926   1.00 62.48  ?  25  SER C O   1 
ATOM   2574 C CB  . SER B 2 25  ? 29.167 58.316  -1.045  1.00 58.87  ?  25  SER C CB  1 
ATOM   2575 O OG  . SER B 2 25  ? 28.084 57.883  -1.854  1.00 57.52  ?  25  SER C OG  1 
ATOM   2576 N N   . GLY B 2 26  ? 28.341 58.218  2.039   1.00 64.63  ?  26  GLY C N   1 
ATOM   2577 C CA  . GLY B 2 26  ? 27.263 58.409  2.997   1.00 60.86  ?  26  GLY C CA  1 
ATOM   2578 C C   . GLY B 2 26  ? 27.600 57.813  4.362   1.00 67.70  ?  26  GLY C C   1 
ATOM   2579 O O   . GLY B 2 26  ? 28.647 58.103  4.934   1.00 81.60  ?  26  GLY C O   1 
ATOM   2580 N N   . ASP B 2 27  ? 26.692 57.001  4.890   1.00 68.14  ?  27  ASP C N   1 
ATOM   2581 C CA  . ASP B 2 27  ? 26.869 56.386  6.204   1.00 69.33  ?  27  ASP C CA  1 
ATOM   2582 C C   . ASP B 2 27  ? 27.693 55.102  6.074   1.00 63.29  ?  27  ASP C C   1 
ATOM   2583 O O   . ASP B 2 27  ? 27.244 54.002  6.389   1.00 60.97  ?  27  ASP C O   1 
ATOM   2584 C CB  . ASP B 2 27  ? 25.511 56.116  6.842   1.00 71.16  ?  27  ASP C CB  1 
ATOM   2585 C CG  . ASP B 2 27  ? 25.615 55.721  8.304   1.00 76.63  ?  27  ASP C CG  1 
ATOM   2586 O OD1 . ASP B 2 27  ? 26.743 55.704  8.842   1.00 69.25  ?  27  ASP C OD1 1 
ATOM   2587 O OD2 . ASP B 2 27  ? 24.566 55.433  8.911   1.00 74.77  ?  27  ASP C OD2 1 
ATOM   2588 N N   . ILE B 2 28  ? 28.933 55.260  5.601   1.00 58.97  ?  28  ILE C N   1 
ATOM   2589 C CA  . ILE B 2 28  ? 29.786 54.099  5.392   1.00 59.05  ?  28  ILE C CA  1 
ATOM   2590 C C   . ILE B 2 28  ? 30.144 53.419  6.706   1.00 61.35  ?  28  ILE C C   1 
ATOM   2591 O O   . ILE B 2 28  ? 30.464 52.224  6.711   1.00 54.08  ?  28  ILE C O   1 
ATOM   2592 C CB  . ILE B 2 28  ? 31.046 54.491  4.596   1.00 57.55  ?  28  ILE C CB  1 
ATOM   2593 C CG1 . ILE B 2 28  ? 32.135 55.030  5.527   1.00 57.51  ?  28  ILE C CG1 1 
ATOM   2594 C CG2 . ILE B 2 28  ? 30.696 55.519  3.504   1.00 59.29  ?  28  ILE C CG2 1 
ATOM   2595 C CD1 . ILE B 2 28  ? 33.334 55.586  4.792   1.00 59.69  ?  28  ILE C CD1 1 
ATOM   2596 N N   . PHE B 2 29  ? 30.069 54.140  7.829   1.00 55.28  ?  29  PHE C N   1 
ATOM   2597 C CA  . PHE B 2 29  ? 30.382 53.547  9.126   1.00 55.65  ?  29  PHE C CA  1 
ATOM   2598 C C   . PHE B 2 29  ? 29.404 52.438  9.504   1.00 60.27  ?  29  PHE C C   1 
ATOM   2599 O O   . PHE B 2 29  ? 29.741 51.590  10.337  1.00 54.23  ?  29  PHE C O   1 
ATOM   2600 C CB  . PHE B 2 29  ? 30.411 54.646  10.198  1.00 65.28  ?  29  PHE C CB  1 
ATOM   2601 C CG  . PHE B 2 29  ? 30.456 54.131  11.617  1.00 69.69  ?  29  PHE C CG  1 
ATOM   2602 C CD1 . PHE B 2 29  ? 31.614 53.571  12.142  1.00 73.60  ?  29  PHE C CD1 1 
ATOM   2603 C CD2 . PHE B 2 29  ? 29.345 54.239  12.439  1.00 72.48  ?  29  PHE C CD2 1 
ATOM   2604 C CE1 . PHE B 2 29  ? 31.650 53.108  13.453  1.00 70.46  ?  29  PHE C CE1 1 
ATOM   2605 C CE2 . PHE B 2 29  ? 29.376 53.781  13.745  1.00 70.19  ?  29  PHE C CE2 1 
ATOM   2606 C CZ  . PHE B 2 29  ? 30.528 53.215  14.253  1.00 71.56  ?  29  PHE C CZ  1 
ATOM   2607 N N   . SER B 2 30  ? 28.221 52.406  8.888   1.00 59.02  ?  30  SER C N   1 
ATOM   2608 C CA  . SER B 2 30  ? 27.197 51.417  9.205   1.00 58.50  ?  30  SER C CA  1 
ATOM   2609 C C   . SER B 2 30  ? 27.327 50.124  8.406   1.00 55.32  ?  30  SER C C   1 
ATOM   2610 O O   . SER B 2 30  ? 26.564 49.183  8.657   1.00 52.83  ?  30  SER C O   1 
ATOM   2611 C CB  . SER B 2 30  ? 25.805 52.014  8.973   1.00 59.91  ?  30  SER C CB  1 
ATOM   2612 O OG  . SER B 2 30  ? 25.536 52.154  7.588   1.00 61.34  ?  30  SER C OG  1 
ATOM   2613 N N   . ILE B 2 31  ? 28.256 50.051  7.459   1.00 49.55  ?  31  ILE C N   1 
ATOM   2614 C CA  . ILE B 2 31  ? 28.428 48.853  6.645   1.00 50.87  ?  31  ILE C CA  1 
ATOM   2615 C C   . ILE B 2 31  ? 29.183 47.809  7.454   1.00 48.67  ?  31  ILE C C   1 
ATOM   2616 O O   . ILE B 2 31  ? 30.213 48.109  8.067   1.00 51.09  ?  31  ILE C O   1 
ATOM   2617 C CB  . ILE B 2 31  ? 29.169 49.188  5.340   1.00 45.80  ?  31  ILE C CB  1 
ATOM   2618 C CG1 . ILE B 2 31  ? 28.317 50.099  4.455   1.00 48.81  ?  31  ILE C CG1 1 
ATOM   2619 C CG2 . ILE B 2 31  ? 29.545 47.919  4.594   1.00 47.35  ?  31  ILE C CG2 1 
ATOM   2620 C CD1 . ILE B 2 31  ? 29.119 50.893  3.442   1.00 43.05  ?  31  ILE C CD1 1 
ATOM   2621 N N   . TYR B 2 32  ? 28.671 46.579  7.472   1.00 47.04  ?  32  TYR C N   1 
ATOM   2622 C CA  . TYR B 2 32  ? 29.395 45.491  8.107   1.00 44.30  ?  32  TYR C CA  1 
ATOM   2623 C C   . TYR B 2 32  ? 29.592 44.288  7.198   1.00 46.63  ?  32  TYR C C   1 
ATOM   2624 O O   . TYR B 2 32  ? 30.148 43.278  7.646   1.00 48.73  ?  32  TYR C O   1 
ATOM   2625 C CB  . TYR B 2 32  ? 28.702 45.055  9.406   1.00 40.94  ?  32  TYR C CB  1 
ATOM   2626 C CG  . TYR B 2 32  ? 27.229 44.747  9.282   1.00 46.13  ?  32  TYR C CG  1 
ATOM   2627 C CD1 . TYR B 2 32  ? 26.792 43.474  8.939   1.00 40.80  ?  32  TYR C CD1 1 
ATOM   2628 C CD2 . TYR B 2 32  ? 26.274 45.722  9.538   1.00 41.96  ?  32  TYR C CD2 1 
ATOM   2629 C CE1 . TYR B 2 32  ? 25.446 43.186  8.836   1.00 41.34  ?  32  TYR C CE1 1 
ATOM   2630 C CE2 . TYR B 2 32  ? 24.926 45.445  9.439   1.00 45.42  ?  32  TYR C CE2 1 
ATOM   2631 C CZ  . TYR B 2 32  ? 24.515 44.175  9.089   1.00 43.49  ?  32  TYR C CZ  1 
ATOM   2632 O OH  . TYR B 2 32  ? 23.172 43.893  8.992   1.00 40.75  ?  32  TYR C OH  1 
ATOM   2633 N N   . LEU B 2 33  ? 29.170 44.368  5.938   1.00 42.94  ?  33  LEU C N   1 
ATOM   2634 C CA  . LEU B 2 33  ? 29.429 43.312  4.968   1.00 43.80  ?  33  LEU C CA  1 
ATOM   2635 C C   . LEU B 2 33  ? 29.532 43.946  3.592   1.00 43.54  ?  33  LEU C C   1 
ATOM   2636 O O   . LEU B 2 33  ? 28.599 44.624  3.150   1.00 41.39  ?  33  LEU C O   1 
ATOM   2637 C CB  . LEU B 2 33  ? 28.331 42.249  4.994   1.00 42.81  ?  33  LEU C CB  1 
ATOM   2638 C CG  . LEU B 2 33  ? 28.659 40.969  4.220   1.00 42.21  ?  33  LEU C CG  1 
ATOM   2639 C CD1 . LEU B 2 33  ? 29.935 40.334  4.750   1.00 38.96  ?  33  LEU C CD1 1 
ATOM   2640 C CD2 . LEU B 2 33  ? 27.500 39.991  4.283   1.00 41.07  ?  33  LEU C CD2 1 
ATOM   2641 N N   . MET B 2 34  ? 30.665 43.736  2.928   1.00 41.08  ?  34  MET C N   1 
ATOM   2642 C CA  . MET B 2 34  ? 30.906 44.231  1.582   1.00 40.95  ?  34  MET C CA  1 
ATOM   2643 C C   . MET B 2 34  ? 31.122 43.048  0.653   1.00 42.37  ?  34  MET C C   1 
ATOM   2644 O O   . MET B 2 34  ? 31.764 42.063  1.032   1.00 37.64  ?  34  MET C O   1 
ATOM   2645 C CB  . MET B 2 34  ? 32.120 45.156  1.544   1.00 44.74  ?  34  MET C CB  1 
ATOM   2646 C CG  . MET B 2 34  ? 31.930 46.445  2.317   1.00 48.17  ?  34  MET C CG  1 
ATOM   2647 S SD  . MET B 2 34  ? 33.393 46.897  3.269   1.00 51.40  ?  34  MET C SD  1 
ATOM   2648 C CE  . MET B 2 34  ? 33.341 45.681  4.583   1.00 51.28  ?  34  MET C CE  1 
ATOM   2649 N N   . GLY B 2 35  ? 30.588 43.140  -0.562  1.00 39.01  ?  35  GLY C N   1 
ATOM   2650 C CA  . GLY B 2 35  ? 30.675 42.002  -1.457  1.00 40.20  ?  35  GLY C CA  1 
ATOM   2651 C C   . GLY B 2 35  ? 30.588 42.391  -2.914  1.00 39.47  ?  35  GLY C C   1 
ATOM   2652 O O   . GLY B 2 35  ? 30.337 43.544  -3.268  1.00 39.85  ?  35  GLY C O   1 
ATOM   2653 N N   . TRP B 2 36  ? 30.807 41.389  -3.760  1.00 38.91  ?  36  TRP C N   1 
ATOM   2654 C CA  . TRP B 2 36  ? 30.741 41.532  -5.207  1.00 40.72  ?  36  TRP C CA  1 
ATOM   2655 C C   . TRP B 2 36  ? 29.823 40.456  -5.763  1.00 40.87  ?  36  TRP C C   1 
ATOM   2656 O O   . TRP B 2 36  ? 29.937 39.284  -5.388  1.00 38.81  ?  36  TRP C O   1 
ATOM   2657 C CB  . TRP B 2 36  ? 32.134 41.426  -5.840  1.00 38.35  ?  36  TRP C CB  1 
ATOM   2658 C CG  . TRP B 2 36  ? 32.982 42.643  -5.638  1.00 46.47  ?  36  TRP C CG  1 
ATOM   2659 C CD1 . TRP B 2 36  ? 33.947 42.821  -4.690  1.00 44.12  ?  36  TRP C CD1 1 
ATOM   2660 C CD2 . TRP B 2 36  ? 32.949 43.853  -6.408  1.00 46.30  ?  36  TRP C CD2 1 
ATOM   2661 N NE1 . TRP B 2 36  ? 34.514 44.067  -4.818  1.00 43.08  ?  36  TRP C NE1 1 
ATOM   2662 C CE2 . TRP B 2 36  ? 33.919 44.719  -5.866  1.00 45.27  ?  36  TRP C CE2 1 
ATOM   2663 C CE3 . TRP B 2 36  ? 32.193 44.286  -7.503  1.00 43.78  ?  36  TRP C CE3 1 
ATOM   2664 C CZ2 . TRP B 2 36  ? 34.152 45.994  -6.380  1.00 47.91  ?  36  TRP C CZ2 1 
ATOM   2665 C CZ3 . TRP B 2 36  ? 32.424 45.551  -8.011  1.00 44.91  ?  36  TRP C CZ3 1 
ATOM   2666 C CH2 . TRP B 2 36  ? 33.395 46.390  -7.449  1.00 49.04  ?  36  TRP C CH2 1 
ATOM   2667 N N   . TYR B 2 37  ? 28.910 40.857  -6.641  1.00 38.58  ?  37  TYR C N   1 
ATOM   2668 C CA  . TYR B 2 37  ? 28.003 39.949  -7.325  1.00 38.76  ?  37  TYR C CA  1 
ATOM   2669 C C   . TYR B 2 37  ? 28.205 40.081  -8.828  1.00 42.14  ?  37  TYR C C   1 
ATOM   2670 O O   . TYR B 2 37  ? 28.782 41.060  -9.312  1.00 39.69  ?  37  TYR C O   1 
ATOM   2671 C CB  . TYR B 2 37  ? 26.538 40.242  -6.971  1.00 40.69  ?  37  TYR C CB  1 
ATOM   2672 C CG  . TYR B 2 37  ? 26.123 39.813  -5.580  1.00 45.39  ?  37  TYR C CG  1 
ATOM   2673 C CD1 . TYR B 2 37  ? 26.617 40.459  -4.453  1.00 41.11  ?  37  TYR C CD1 1 
ATOM   2674 C CD2 . TYR B 2 37  ? 25.228 38.766  -5.395  1.00 44.48  ?  37  TYR C CD2 1 
ATOM   2675 C CE1 . TYR B 2 37  ? 26.235 40.070  -3.182  1.00 38.02  ?  37  TYR C CE1 1 
ATOM   2676 C CE2 . TYR B 2 37  ? 24.841 38.370  -4.128  1.00 45.83  ?  37  TYR C CE2 1 
ATOM   2677 C CZ  . TYR B 2 37  ? 25.346 39.025  -3.026  1.00 45.01  ?  37  TYR C CZ  1 
ATOM   2678 O OH  . TYR B 2 37  ? 24.961 38.631  -1.763  1.00 43.49  ?  37  TYR C OH  1 
ATOM   2679 N N   . ARG B 2 38  ? 27.721 39.089  -9.571  1.00 35.16  ?  38  ARG C N   1 
ATOM   2680 C CA  . ARG B 2 38  ? 27.812 39.140  -11.021 1.00 40.16  ?  38  ARG C CA  1 
ATOM   2681 C C   . ARG B 2 38  ? 26.586 38.481  -11.633 1.00 43.76  ?  38  ARG C C   1 
ATOM   2682 O O   . ARG B 2 38  ? 26.002 37.557  -11.058 1.00 43.79  ?  38  ARG C O   1 
ATOM   2683 C CB  . ARG B 2 38  ? 29.096 38.477  -11.538 1.00 35.93  ?  38  ARG C CB  1 
ATOM   2684 C CG  . ARG B 2 38  ? 29.067 36.959  -11.590 1.00 41.43  ?  38  ARG C CG  1 
ATOM   2685 C CD  . ARG B 2 38  ? 30.343 36.435  -12.224 1.00 40.68  ?  38  ARG C CD  1 
ATOM   2686 N NE  . ARG B 2 38  ? 30.563 35.017  -11.971 1.00 37.31  ?  38  ARG C NE  1 
ATOM   2687 C CZ  . ARG B 2 38  ? 31.715 34.394  -12.185 1.00 39.23  ?  38  ARG C CZ  1 
ATOM   2688 N NH1 . ARG B 2 38  ? 32.775 35.042  -12.644 1.00 38.37  ?  38  ARG C NH1 1 
ATOM   2689 N NH2 . ARG B 2 38  ? 31.806 33.091  -11.935 1.00 35.33  ?  38  ARG C NH2 1 
ATOM   2690 N N   . GLN B 2 39  ? 26.194 38.979  -12.804 1.00 41.66  ?  39  GLN C N   1 
ATOM   2691 C CA  . GLN B 2 39  ? 25.045 38.471  -13.548 1.00 44.90  ?  39  GLN C CA  1 
ATOM   2692 C C   . GLN B 2 39  ? 25.531 38.132  -14.954 1.00 43.60  ?  39  GLN C C   1 
ATOM   2693 O O   . GLN B 2 39  ? 25.741 39.027  -15.778 1.00 44.18  ?  39  GLN C O   1 
ATOM   2694 C CB  . GLN B 2 39  ? 23.910 39.491  -13.573 1.00 42.79  ?  39  GLN C CB  1 
ATOM   2695 C CG  . GLN B 2 39  ? 22.642 39.011  -14.262 1.00 46.69  ?  39  GLN C CG  1 
ATOM   2696 C CD  . GLN B 2 39  ? 22.574 39.430  -15.718 1.00 55.23  ?  39  GLN C CD  1 
ATOM   2697 O OE1 . GLN B 2 39  ? 22.568 40.620  -16.035 1.00 57.10  ?  39  GLN C OE1 1 
ATOM   2698 N NE2 . GLN B 2 39  ? 22.520 38.451  -16.614 1.00 56.70  ?  39  GLN C NE2 1 
ATOM   2699 N N   . SER B 2 40  ? 25.714 36.846  -15.220 1.00 45.47  ?  40  SER C N   1 
ATOM   2700 C CA  . SER B 2 40  ? 26.209 36.374  -16.503 1.00 48.87  ?  40  SER C CA  1 
ATOM   2701 C C   . SER B 2 40  ? 25.063 36.204  -17.490 1.00 50.84  ?  40  SER C C   1 
ATOM   2702 O O   . SER B 2 40  ? 23.900 36.074  -17.093 1.00 50.05  ?  40  SER C O   1 
ATOM   2703 C CB  . SER B 2 40  ? 26.953 35.052  -16.319 1.00 47.34  ?  40  SER C CB  1 
ATOM   2704 O OG  . SER B 2 40  ? 28.224 35.267  -15.728 1.00 47.96  ?  40  SER C OG  1 
ATOM   2705 N N   . PRO B 2 41  ? 25.357 36.226  -18.791 1.00 46.64  ?  41  PRO C N   1 
ATOM   2706 C CA  . PRO B 2 41  ? 24.293 36.071  -19.794 1.00 50.13  ?  41  PRO C CA  1 
ATOM   2707 C C   . PRO B 2 41  ? 23.512 34.779  -19.595 1.00 52.37  ?  41  PRO C C   1 
ATOM   2708 O O   . PRO B 2 41  ? 24.087 33.700  -19.441 1.00 53.40  ?  41  PRO C O   1 
ATOM   2709 C CB  . PRO B 2 41  ? 25.062 36.068  -21.119 1.00 54.70  ?  41  PRO C CB  1 
ATOM   2710 C CG  . PRO B 2 41  ? 26.277 36.877  -20.838 1.00 56.02  ?  41  PRO C CG  1 
ATOM   2711 C CD  . PRO B 2 41  ? 26.649 36.571  -19.413 1.00 45.88  ?  41  PRO C CD  1 
ATOM   2712 N N   . GLY B 2 42  ? 22.186 34.903  -19.595 1.00 51.11  ?  42  GLY C N   1 
ATOM   2713 C CA  . GLY B 2 42  ? 21.327 33.753  -19.402 1.00 57.65  ?  42  GLY C CA  1 
ATOM   2714 C C   . GLY B 2 42  ? 21.365 33.156  -18.015 1.00 56.26  ?  42  GLY C C   1 
ATOM   2715 O O   . GLY B 2 42  ? 21.062 31.971  -17.854 1.00 62.02  ?  42  GLY C O   1 
ATOM   2716 N N   . LYS B 2 43  ? 21.728 33.941  -17.004 1.00 54.56  ?  43  LYS C N   1 
ATOM   2717 C CA  . LYS B 2 43  ? 21.826 33.449  -15.638 1.00 54.11  ?  43  LYS C CA  1 
ATOM   2718 C C   . LYS B 2 43  ? 21.328 34.517  -14.677 1.00 54.72  ?  43  LYS C C   1 
ATOM   2719 O O   . LYS B 2 43  ? 21.348 35.713  -14.976 1.00 49.77  ?  43  LYS C O   1 
ATOM   2720 C CB  . LYS B 2 43  ? 23.267 33.062  -15.279 1.00 51.41  ?  43  LYS C CB  1 
ATOM   2721 C CG  . LYS B 2 43  ? 23.709 31.714  -15.816 1.00 53.85  ?  43  LYS C CG  1 
ATOM   2722 C CD  . LYS B 2 43  ? 24.663 31.031  -14.850 1.00 67.23  ?  43  LYS C CD  1 
ATOM   2723 C CE  . LYS B 2 43  ? 26.049 30.885  -15.452 1.00 66.98  ?  43  LYS C CE  1 
ATOM   2724 N NZ  . LYS B 2 43  ? 27.106 30.861  -14.404 1.00 74.21  ?  43  LYS C NZ  1 
ATOM   2725 N N   . GLN B 2 44  ? 20.878 34.067  -13.509 1.00 51.86  ?  44  GLN C N   1 
ATOM   2726 C CA  . GLN B 2 44  ? 20.490 34.989  -12.455 1.00 58.71  ?  44  GLN C CA  1 
ATOM   2727 C C   . GLN B 2 44  ? 21.732 35.595  -11.805 1.00 53.15  ?  44  GLN C C   1 
ATOM   2728 O O   . GLN B 2 44  ? 22.861 35.130  -11.993 1.00 53.73  ?  44  GLN C O   1 
ATOM   2729 C CB  . GLN B 2 44  ? 19.636 34.275  -11.406 1.00 60.34  ?  44  GLN C CB  1 
ATOM   2730 C CG  . GLN B 2 44  ? 20.366 33.156  -10.675 1.00 65.64  ?  44  GLN C CG  1 
ATOM   2731 C CD  . GLN B 2 44  ? 19.503 32.469  -9.631  1.00 75.57  ?  44  GLN C CD  1 
ATOM   2732 O OE1 . GLN B 2 44  ? 19.806 31.359  -9.192  1.00 74.78  ?  44  GLN C OE1 1 
ATOM   2733 N NE2 . GLN B 2 44  ? 18.423 33.128  -9.228  1.00 73.94  ?  44  GLN C NE2 1 
ATOM   2734 N N   . ARG B 2 45  ? 21.516 36.660  -11.036 1.00 50.73  ?  45  ARG C N   1 
ATOM   2735 C CA  . ARG B 2 45  ? 22.604 37.254  -10.272 1.00 50.97  ?  45  ARG C CA  1 
ATOM   2736 C C   . ARG B 2 45  ? 23.119 36.256  -9.241  1.00 51.43  ?  45  ARG C C   1 
ATOM   2737 O O   . ARG B 2 45  ? 22.341 35.562  -8.582  1.00 50.96  ?  45  ARG C O   1 
ATOM   2738 C CB  . ARG B 2 45  ? 22.131 38.536  -9.584  1.00 46.33  ?  45  ARG C CB  1 
ATOM   2739 C CG  . ARG B 2 45  ? 23.240 39.529  -9.277  1.00 49.93  ?  45  ARG C CG  1 
ATOM   2740 C CD  . ARG B 2 45  ? 22.690 40.797  -8.637  1.00 51.30  ?  45  ARG C CD  1 
ATOM   2741 N NE  . ARG B 2 45  ? 22.084 41.688  -9.620  1.00 52.95  ?  45  ARG C NE  1 
ATOM   2742 C CZ  . ARG B 2 45  ? 21.585 42.884  -9.341  1.00 52.62  ?  45  ARG C CZ  1 
ATOM   2743 N NH1 . ARG B 2 45  ? 21.603 43.373  -8.112  1.00 53.44  ?  45  ARG C NH1 1 
ATOM   2744 N NH2 . ARG B 2 45  ? 21.054 43.610  -10.321 1.00 63.08  ?  45  ARG C NH2 1 
ATOM   2745 N N   . GLU B 2 46  ? 24.442 36.176  -9.111  1.00 49.04  ?  46  GLU C N   1 
ATOM   2746 C CA  . GLU B 2 46  ? 25.062 35.226  -8.201  1.00 48.17  ?  46  GLU C CA  1 
ATOM   2747 C C   . GLU B 2 46  ? 26.196 35.898  -7.442  1.00 43.95  ?  46  GLU C C   1 
ATOM   2748 O O   . GLU B 2 46  ? 26.820 36.845  -7.929  1.00 40.55  ?  46  GLU C O   1 
ATOM   2749 C CB  . GLU B 2 46  ? 25.588 33.989  -8.946  1.00 48.19  ?  46  GLU C CB  1 
ATOM   2750 C CG  . GLU B 2 46  ? 26.865 34.229  -9.734  1.00 51.19  ?  46  GLU C CG  1 
ATOM   2751 C CD  . GLU B 2 46  ? 27.120 33.152  -10.770 1.00 64.74  ?  46  GLU C CD  1 
ATOM   2752 O OE1 . GLU B 2 46  ? 26.150 32.707  -11.419 1.00 68.73  ?  46  GLU C OE1 1 
ATOM   2753 O OE2 . GLU B 2 46  ? 28.292 32.751  -10.936 1.00 66.37  ?  46  GLU C OE2 1 
ATOM   2754 N N   . LEU B 2 47  ? 26.455 35.389  -6.241  1.00 37.34  ?  47  LEU C N   1 
ATOM   2755 C CA  . LEU B 2 47  ? 27.508 35.933  -5.398  1.00 38.41  ?  47  LEU C CA  1 
ATOM   2756 C C   . LEU B 2 47  ? 28.881 35.554  -5.941  1.00 37.52  ?  47  LEU C C   1 
ATOM   2757 O O   . LEU B 2 47  ? 29.072 34.466  -6.489  1.00 46.19  ?  47  LEU C O   1 
ATOM   2758 C CB  . LEU B 2 47  ? 27.346 35.418  -3.967  1.00 37.67  ?  47  LEU C CB  1 
ATOM   2759 C CG  . LEU B 2 47  ? 28.433 35.794  -2.961  1.00 41.43  ?  47  LEU C CG  1 
ATOM   2760 C CD1 . LEU B 2 47  ? 28.499 37.299  -2.831  1.00 40.66  ?  47  LEU C CD1 1 
ATOM   2761 C CD2 . LEU B 2 47  ? 28.177 35.139  -1.610  1.00 38.52  ?  47  LEU C CD2 1 
ATOM   2762 N N   . VAL B 2 48  ? 29.839 36.463  -5.790  1.00 39.16  ?  48  VAL C N   1 
ATOM   2763 C CA  . VAL B 2 48  ? 31.225 36.228  -6.172  1.00 41.58  ?  48  VAL C CA  1 
ATOM   2764 C C   . VAL B 2 48  ? 32.139 36.190  -4.952  1.00 41.93  ?  48  VAL C C   1 
ATOM   2765 O O   . VAL B 2 48  ? 32.898 35.238  -4.766  1.00 47.10  ?  48  VAL C O   1 
ATOM   2766 C CB  . VAL B 2 48  ? 31.707 37.287  -7.192  1.00 41.75  ?  48  VAL C CB  1 
ATOM   2767 C CG1 . VAL B 2 48  ? 33.162 37.048  -7.562  1.00 38.19  ?  48  VAL C CG1 1 
ATOM   2768 C CG2 . VAL B 2 48  ? 30.827 37.267  -8.431  1.00 37.75  ?  48  VAL C CG2 1 
ATOM   2769 N N   . ALA B 2 49  ? 32.068 37.214  -4.104  1.00 39.09  ?  49  ALA C N   1 
ATOM   2770 C CA  . ALA B 2 49  ? 32.921 37.291  -2.926  1.00 40.08  ?  49  ALA C CA  1 
ATOM   2771 C C   . ALA B 2 49  ? 32.318 38.271  -1.929  1.00 40.05  ?  49  ALA C C   1 
ATOM   2772 O O   . ALA B 2 49  ? 31.618 39.211  -2.313  1.00 43.66  ?  49  ALA C O   1 
ATOM   2773 C CB  . ALA B 2 49  ? 34.349 37.716  -3.290  1.00 35.17  ?  49  ALA C CB  1 
ATOM   2774 N N   . THR B 2 50  ? 32.593 38.036  -0.645  1.00 41.03  ?  50  THR C N   1 
ATOM   2775 C CA  . THR B 2 50  ? 32.184 38.930  0.431   1.00 40.61  ?  50  THR C CA  1 
ATOM   2776 C C   . THR B 2 50  ? 33.341 39.133  1.399   1.00 40.07  ?  50  THR C C   1 
ATOM   2777 O O   . THR B 2 50  ? 34.272 38.327  1.468   1.00 39.34  ?  50  THR C O   1 
ATOM   2778 C CB  . THR B 2 50  ? 30.974 38.402  1.220   1.00 38.63  ?  50  THR C CB  1 
ATOM   2779 O OG1 . THR B 2 50  ? 31.295 37.133  1.803   1.00 39.05  ?  50  THR C OG1 1 
ATOM   2780 C CG2 . THR B 2 50  ? 29.761 38.259  0.326   1.00 40.47  ?  50  THR C CG2 1 
ATOM   2781 N N   . ILE B 2 51  ? 33.260 40.219  2.163   1.00 37.63  ?  51  ILE C N   1 
ATOM   2782 C CA  . ILE B 2 51  ? 34.251 40.516  3.192   1.00 37.48  ?  51  ILE C CA  1 
ATOM   2783 C C   . ILE B 2 51  ? 33.569 41.311  4.299   1.00 42.24  ?  51  ILE C C   1 
ATOM   2784 O O   . ILE B 2 51  ? 32.767 42.213  4.034   1.00 45.59  ?  51  ILE C O   1 
ATOM   2785 C CB  . ILE B 2 51  ? 35.469 41.267  2.609   1.00 44.21  ?  51  ILE C CB  1 
ATOM   2786 C CG1 . ILE B 2 51  ? 36.540 41.467  3.684   1.00 45.19  ?  51  ILE C CG1 1 
ATOM   2787 C CG2 . ILE B 2 51  ? 35.055 42.597  1.987   1.00 40.19  ?  51  ILE C CG2 1 
ATOM   2788 C CD1 . ILE B 2 51  ? 37.905 41.805  3.128   1.00 50.56  ?  51  ILE C CD1 1 
ATOM   2789 N N   . THR B 2 52  ? 33.874 40.954  5.541   1.00 41.65  ?  52  THR C N   1 
ATOM   2790 C CA  . THR B 2 52  ? 33.315 41.631  6.700   1.00 46.87  ?  52  THR C CA  1 
ATOM   2791 C C   . THR B 2 52  ? 34.209 42.795  7.118   1.00 49.37  ?  52  THR C C   1 
ATOM   2792 O O   . THR B 2 52  ? 35.307 42.994  6.592   1.00 47.84  ?  52  THR C O   1 
ATOM   2793 C CB  . THR B 2 52  ? 33.138 40.653  7.862   1.00 48.76  ?  52  THR C CB  1 
ATOM   2794 O OG1 . THR B 2 52  ? 34.422 40.319  8.407   1.00 48.29  ?  52  THR C OG1 1 
ATOM   2795 C CG2 . THR B 2 52  ? 32.446 39.380  7.394   1.00 44.70  ?  52  THR C CG2 1 
ATOM   2796 N N   . SER B 2 53  ? 33.718 43.578  8.082   1.00 52.95  ?  53  SER C N   1 
ATOM   2797 C CA  . SER B 2 53  ? 34.513 44.678  8.616   1.00 54.26  ?  53  SER C CA  1 
ATOM   2798 C C   . SER B 2 53  ? 35.803 44.166  9.245   1.00 56.13  ?  53  SER C C   1 
ATOM   2799 O O   . SER B 2 53  ? 36.863 44.787  9.100   1.00 57.42  ?  53  SER C O   1 
ATOM   2800 C CB  . SER B 2 53  ? 33.698 45.472  9.637   1.00 55.56  ?  53  SER C CB  1 
ATOM   2801 O OG  . SER B 2 53  ? 32.572 46.085  9.032   1.00 60.60  ?  53  SER C OG  1 
ATOM   2802 N N   . SER B 2 54  ? 35.735 43.027  9.939   1.00 55.48  ?  54  SER C N   1 
ATOM   2803 C CA  . SER B 2 54  ? 36.920 42.458  10.569  1.00 58.97  ?  54  SER C CA  1 
ATOM   2804 C C   . SER B 2 54  ? 37.875 41.837  9.557   1.00 60.82  ?  54  SER C C   1 
ATOM   2805 O O   . SER B 2 54  ? 39.044 41.611  9.887   1.00 62.99  ?  54  SER C O   1 
ATOM   2806 C CB  . SER B 2 54  ? 36.512 41.414  11.610  1.00 60.19  ?  54  SER C CB  1 
ATOM   2807 O OG  . SER B 2 54  ? 35.706 40.400  11.032  1.00 62.13  ?  54  SER C OG  1 
ATOM   2808 N N   . GLY B 2 55  ? 37.412 41.556  8.343   1.00 59.15  ?  55  GLY C N   1 
ATOM   2809 C CA  . GLY B 2 55  ? 38.255 40.998  7.307   1.00 54.82  ?  55  GLY C CA  1 
ATOM   2810 C C   . GLY B 2 55  ? 37.993 39.549  6.945   1.00 55.65  ?  55  GLY C C   1 
ATOM   2811 O O   . GLY B 2 55  ? 38.769 38.978  6.171   1.00 53.94  ?  55  GLY C O   1 
ATOM   2812 N N   . GLU B 2 56  ? 36.939 38.935  7.480   1.00 52.56  ?  56  GLU C N   1 
ATOM   2813 C CA  . GLU B 2 56  ? 36.600 37.565  7.114   1.00 50.48  ?  56  GLU C CA  1 
ATOM   2814 C C   . GLU B 2 56  ? 36.049 37.538  5.692   1.00 47.43  ?  56  GLU C C   1 
ATOM   2815 O O   . GLU B 2 56  ? 35.063 38.218  5.386   1.00 43.87  ?  56  GLU C O   1 
ATOM   2816 C CB  . GLU B 2 56  ? 35.585 36.990  8.099   1.00 51.20  ?  56  GLU C CB  1 
ATOM   2817 C CG  . GLU B 2 56  ? 36.108 35.814  8.909   1.00 57.28  ?  56  GLU C CG  1 
ATOM   2818 C CD  . GLU B 2 56  ? 34.997 34.938  9.454   1.00 69.88  ?  56  GLU C CD  1 
ATOM   2819 O OE1 . GLU B 2 56  ? 34.077 35.477  10.102  1.00 65.07  ?  56  GLU C OE1 1 
ATOM   2820 O OE2 . GLU B 2 56  ? 35.043 33.708  9.233   1.00 67.20  ?  56  GLU C OE2 1 
ATOM   2821 N N   . THR B 2 57  ? 36.681 36.754  4.824   1.00 41.99  ?  57  THR C N   1 
ATOM   2822 C CA  . THR B 2 57  ? 36.339 36.723  3.410   1.00 46.98  ?  57  THR C CA  1 
ATOM   2823 C C   . THR B 2 57  ? 35.690 35.397  3.031   1.00 47.14  ?  57  THR C C   1 
ATOM   2824 O O   . THR B 2 57  ? 35.833 34.381  3.717   1.00 46.41  ?  57  THR C O   1 
ATOM   2825 C CB  . THR B 2 57  ? 37.579 36.945  2.534   1.00 44.54  ?  57  THR C CB  1 
ATOM   2826 O OG1 . THR B 2 57  ? 38.417 35.784  2.585   1.00 45.37  ?  57  THR C OG1 1 
ATOM   2827 C CG2 . THR B 2 57  ? 38.363 38.156  3.013   1.00 43.69  ?  57  THR C CG2 1 
ATOM   2828 N N   . LYS B 2 58  ? 34.972 35.430  1.913   1.00 43.19  ?  58  LYS C N   1 
ATOM   2829 C CA  . LYS B 2 58  ? 34.374 34.240  1.323   1.00 45.85  ?  58  LYS C CA  1 
ATOM   2830 C C   . LYS B 2 58  ? 34.408 34.399  -0.188  1.00 48.48  ?  58  LYS C C   1 
ATOM   2831 O O   . LYS B 2 58  ? 33.936 35.412  -0.709  1.00 43.37  ?  58  LYS C O   1 
ATOM   2832 C CB  . LYS B 2 58  ? 32.934 34.037  1.809   1.00 45.50  ?  58  LYS C CB  1 
ATOM   2833 C CG  . LYS B 2 58  ? 32.223 32.862  1.157   1.00 46.70  ?  58  LYS C CG  1 
ATOM   2834 C CD  . LYS B 2 58  ? 30.850 32.637  1.770   1.00 52.58  ?  58  LYS C CD  1 
ATOM   2835 C CE  . LYS B 2 58  ? 29.983 31.765  0.877   1.00 62.52  ?  58  LYS C CE  1 
ATOM   2836 N NZ  . LYS B 2 58  ? 30.426 30.343  0.898   1.00 59.33  ?  58  LYS C NZ  1 
ATOM   2837 N N   . HIS B 2 59  ? 34.976 33.414  -0.880  1.00 44.22  ?  59  HIS C N   1 
ATOM   2838 C CA  . HIS B 2 59  ? 35.016 33.392  -2.337  1.00 45.10  ?  59  HIS C CA  1 
ATOM   2839 C C   . HIS B 2 59  ? 34.336 32.125  -2.832  1.00 40.61  ?  59  HIS C C   1 
ATOM   2840 O O   . HIS B 2 59  ? 34.629 31.029  -2.343  1.00 46.42  ?  59  HIS C O   1 
ATOM   2841 C CB  . HIS B 2 59  ? 36.453 33.459  -2.866  1.00 42.35  ?  59  HIS C CB  1 
ATOM   2842 C CG  . HIS B 2 59  ? 37.242 34.618  -2.342  1.00 45.67  ?  59  HIS C CG  1 
ATOM   2843 N ND1 . HIS B 2 59  ? 37.611 35.687  -3.131  1.00 43.09  ?  59  HIS C ND1 1 
ATOM   2844 C CD2 . HIS B 2 59  ? 37.750 34.869  -1.113  1.00 46.83  ?  59  HIS C CD2 1 
ATOM   2845 C CE1 . HIS B 2 59  ? 38.304 36.548  -2.408  1.00 46.47  ?  59  HIS C CE1 1 
ATOM   2846 N NE2 . HIS B 2 59  ? 38.403 36.076  -1.179  1.00 48.22  ?  59  HIS C NE2 1 
ATOM   2847 N N   . VAL B 2 60  ? 33.426 32.274  -3.799  1.00 39.50  ?  60  VAL C N   1 
ATOM   2848 C CA  . VAL B 2 60  ? 32.740 31.108  -4.342  1.00 40.68  ?  60  VAL C CA  1 
ATOM   2849 C C   . VAL B 2 60  ? 33.738 30.205  -5.061  1.00 41.63  ?  60  VAL C C   1 
ATOM   2850 O O   . VAL B 2 60  ? 34.831 30.623  -5.462  1.00 40.41  ?  60  VAL C O   1 
ATOM   2851 C CB  . VAL B 2 60  ? 31.587 31.522  -5.274  1.00 37.31  ?  60  VAL C CB  1 
ATOM   2852 C CG1 . VAL B 2 60  ? 30.567 32.352  -4.511  1.00 39.36  ?  60  VAL C CG1 1 
ATOM   2853 C CG2 . VAL B 2 60  ? 32.116 32.282  -6.484  1.00 33.19  ?  60  VAL C CG2 1 
ATOM   2854 N N   . TYR B 2 61  ? 33.343 28.938  -5.224  1.00 39.79  ?  61  TYR C N   1 
ATOM   2855 C CA  . TYR B 2 61  ? 34.263 27.926  -5.735  1.00 42.01  ?  61  TYR C CA  1 
ATOM   2856 C C   . TYR B 2 61  ? 34.757 28.265  -7.137  1.00 41.06  ?  61  TYR C C   1 
ATOM   2857 O O   . TYR B 2 61  ? 35.924 28.018  -7.467  1.00 43.97  ?  61  TYR C O   1 
ATOM   2858 C CB  . TYR B 2 61  ? 33.587 26.554  -5.730  1.00 42.70  ?  61  TYR C CB  1 
ATOM   2859 C CG  . TYR B 2 61  ? 33.294 26.007  -4.350  1.00 36.20  ?  61  TYR C CG  1 
ATOM   2860 C CD1 . TYR B 2 61  ? 34.318 25.757  -3.447  1.00 33.66  ?  61  TYR C CD1 1 
ATOM   2861 C CD2 . TYR B 2 61  ? 31.991 25.732  -3.955  1.00 37.06  ?  61  TYR C CD2 1 
ATOM   2862 C CE1 . TYR B 2 61  ? 34.054 25.253  -2.186  1.00 41.16  ?  61  TYR C CE1 1 
ATOM   2863 C CE2 . TYR B 2 61  ? 31.715 25.227  -2.697  1.00 37.90  ?  61  TYR C CE2 1 
ATOM   2864 C CZ  . TYR B 2 61  ? 32.750 24.989  -1.817  1.00 40.77  ?  61  TYR C CZ  1 
ATOM   2865 O OH  . TYR B 2 61  ? 32.479 24.488  -0.563  1.00 42.61  ?  61  TYR C OH  1 
ATOM   2866 N N   . SER B 2 62  ? 33.889 28.836  -7.976  1.00 40.00  ?  62  SER C N   1 
ATOM   2867 C CA  . SER B 2 62  ? 34.245 29.063  -9.374  1.00 43.03  ?  62  SER C CA  1 
ATOM   2868 C C   . SER B 2 62  ? 35.322 30.129  -9.546  1.00 47.21  ?  62  SER C C   1 
ATOM   2869 O O   . SER B 2 62  ? 35.943 30.196  -10.611 1.00 42.11  ?  62  SER C O   1 
ATOM   2870 C CB  . SER B 2 62  ? 33.002 29.448  -10.178 1.00 40.12  ?  62  SER C CB  1 
ATOM   2871 O OG  . SER B 2 62  ? 32.443 30.665  -9.711  1.00 44.63  ?  62  SER C OG  1 
ATOM   2872 N N   . VAL B 2 63  ? 35.557 30.962  -8.531  1.00 41.35  ?  63  VAL C N   1 
ATOM   2873 C CA  . VAL B 2 63  ? 36.560 32.016  -8.595  1.00 42.57  ?  63  VAL C CA  1 
ATOM   2874 C C   . VAL B 2 63  ? 37.665 31.843  -7.564  1.00 47.24  ?  63  VAL C C   1 
ATOM   2875 O O   . VAL B 2 63  ? 38.569 32.684  -7.498  1.00 45.84  ?  63  VAL C O   1 
ATOM   2876 C CB  . VAL B 2 63  ? 35.919 33.414  -8.459  1.00 41.79  ?  63  VAL C CB  1 
ATOM   2877 C CG1 . VAL B 2 63  ? 34.662 33.509  -9.313  1.00 40.71  ?  63  VAL C CG1 1 
ATOM   2878 C CG2 . VAL B 2 63  ? 35.596 33.714  -6.999  1.00 45.01  ?  63  VAL C CG2 1 
ATOM   2879 N N   . LYS B 2 64  ? 37.624 30.780  -6.762  1.00 46.45  ?  64  LYS C N   1 
ATOM   2880 C CA  . LYS B 2 64  ? 38.643 30.554  -5.744  1.00 46.44  ?  64  LYS C CA  1 
ATOM   2881 C C   . LYS B 2 64  ? 40.026 30.453  -6.378  1.00 46.72  ?  64  LYS C C   1 
ATOM   2882 O O   . LYS B 2 64  ? 40.223 29.729  -7.358  1.00 50.16  ?  64  LYS C O   1 
ATOM   2883 C CB  . LYS B 2 64  ? 38.329 29.277  -4.962  1.00 48.38  ?  64  LYS C CB  1 
ATOM   2884 C CG  . LYS B 2 64  ? 37.808 29.514  -3.553  1.00 49.23  ?  64  LYS C CG  1 
ATOM   2885 C CD  . LYS B 2 64  ? 37.803 28.220  -2.745  1.00 50.12  ?  64  LYS C CD  1 
ATOM   2886 C CE  . LYS B 2 64  ? 37.059 28.386  -1.430  1.00 55.12  ?  64  LYS C CE  1 
ATOM   2887 N NZ  . LYS B 2 64  ? 35.684 28.922  -1.630  1.00 49.48  ?  64  LYS C NZ  1 
ATOM   2888 N N   . GLY B 2 65  ? 40.985 31.186  -5.814  1.00 48.29  ?  65  GLY C N   1 
ATOM   2889 C CA  . GLY B 2 65  ? 42.335 31.211  -6.331  1.00 51.26  ?  65  GLY C CA  1 
ATOM   2890 C C   . GLY B 2 65  ? 42.564 32.151  -7.493  1.00 52.50  ?  65  GLY C C   1 
ATOM   2891 O O   . GLY B 2 65  ? 43.721 32.352  -7.887  1.00 54.43  ?  65  GLY C O   1 
ATOM   2892 N N   . ARG B 2 66  ? 41.509 32.729  -8.061  1.00 53.39  ?  66  ARG C N   1 
ATOM   2893 C CA  . ARG B 2 66  ? 41.621 33.688  -9.153  1.00 49.37  ?  66  ARG C CA  1 
ATOM   2894 C C   . ARG B 2 66  ? 41.158 35.086  -8.774  1.00 45.66  ?  66  ARG C C   1 
ATOM   2895 O O   . ARG B 2 66  ? 41.797 36.067  -9.161  1.00 45.93  ?  66  ARG C O   1 
ATOM   2896 C CB  . ARG B 2 66  ? 40.816 33.207  -10.367 1.00 42.22  ?  66  ARG C CB  1 
ATOM   2897 C CG  . ARG B 2 66  ? 41.184 31.815  -10.846 1.00 46.84  ?  66  ARG C CG  1 
ATOM   2898 C CD  . ARG B 2 66  ? 40.592 31.528  -12.215 1.00 46.79  ?  66  ARG C CD  1 
ATOM   2899 N NE  . ARG B 2 66  ? 39.142 31.383  -12.165 1.00 45.27  ?  66  ARG C NE  1 
ATOM   2900 C CZ  . ARG B 2 66  ? 38.286 32.202  -12.761 1.00 46.01  ?  66  ARG C CZ  1 
ATOM   2901 N NH1 . ARG B 2 66  ? 38.701 33.245  -13.462 1.00 47.59  ?  66  ARG C NH1 1 
ATOM   2902 N NH2 . ARG B 2 66  ? 36.980 31.969  -12.651 1.00 35.92  ?  66  ARG C NH2 1 
ATOM   2903 N N   . PHE B 2 67  ? 40.062 35.202  -8.031  1.00 44.79  ?  67  PHE C N   1 
ATOM   2904 C CA  . PHE B 2 67  ? 39.539 36.487  -7.596  1.00 44.73  ?  67  PHE C CA  1 
ATOM   2905 C C   . PHE B 2 67  ? 39.904 36.721  -6.135  1.00 48.01  ?  67  PHE C C   1 
ATOM   2906 O O   . PHE B 2 67  ? 39.960 35.786  -5.333  1.00 48.46  ?  67  PHE C O   1 
ATOM   2907 C CB  . PHE B 2 67  ? 38.016 36.561  -7.761  1.00 43.04  ?  67  PHE C CB  1 
ATOM   2908 C CG  . PHE B 2 67  ? 37.542 36.539  -9.195  1.00 44.92  ?  67  PHE C CG  1 
ATOM   2909 C CD1 . PHE B 2 67  ? 38.417 36.294  -10.242 1.00 46.63  ?  67  PHE C CD1 1 
ATOM   2910 C CD2 . PHE B 2 67  ? 36.207 36.766  -9.491  1.00 44.75  ?  67  PHE C CD2 1 
ATOM   2911 C CE1 . PHE B 2 67  ? 37.973 36.269  -11.549 1.00 43.92  ?  67  PHE C CE1 1 
ATOM   2912 C CE2 . PHE B 2 67  ? 35.756 36.743  -10.798 1.00 41.09  ?  67  PHE C CE2 1 
ATOM   2913 C CZ  . PHE B 2 67  ? 36.640 36.494  -11.827 1.00 45.53  ?  67  PHE C CZ  1 
ATOM   2914 N N   . THR B 2 68  ? 40.151 37.984  -5.793  1.00 43.94  ?  68  THR C N   1 
ATOM   2915 C CA  . THR B 2 68  ? 40.552 38.350  -4.439  1.00 48.11  ?  68  THR C CA  1 
ATOM   2916 C C   . THR B 2 68  ? 39.825 39.620  -4.032  1.00 46.37  ?  68  THR C C   1 
ATOM   2917 O O   . THR B 2 68  ? 39.989 40.663  -4.672  1.00 45.93  ?  68  THR C O   1 
ATOM   2918 C CB  . THR B 2 68  ? 42.068 38.550  -4.345  1.00 47.93  ?  68  THR C CB  1 
ATOM   2919 O OG1 . THR B 2 68  ? 42.733 37.311  -4.625  1.00 52.48  ?  68  THR C OG1 1 
ATOM   2920 C CG2 . THR B 2 68  ? 42.454 39.023  -2.951  1.00 53.27  ?  68  THR C CG2 1 
ATOM   2921 N N   . ILE B 2 69  ? 39.029 39.532  -2.973  1.00 45.07  ?  69  ILE C N   1 
ATOM   2922 C CA  . ILE B 2 69  ? 38.318 40.685  -2.438  1.00 47.54  ?  69  ILE C CA  1 
ATOM   2923 C C   . ILE B 2 69  ? 39.170 41.333  -1.357  1.00 50.19  ?  69  ILE C C   1 
ATOM   2924 O O   . ILE B 2 69  ? 39.892 40.655  -0.615  1.00 53.13  ?  69  ILE C O   1 
ATOM   2925 C CB  . ILE B 2 69  ? 36.929 40.279  -1.901  1.00 45.80  ?  69  ILE C CB  1 
ATOM   2926 C CG1 . ILE B 2 69  ? 36.088 41.520  -1.588  1.00 41.24  ?  69  ILE C CG1 1 
ATOM   2927 C CG2 . ILE B 2 69  ? 37.053 39.385  -0.673  1.00 44.39  ?  69  ILE C CG2 1 
ATOM   2928 C CD1 . ILE B 2 69  ? 34.595 41.274  -1.620  1.00 43.33  ?  69  ILE C CD1 1 
ATOM   2929 N N   . SER B 2 70  ? 39.106 42.660  -1.289  1.00 51.54  ?  70  SER C N   1 
ATOM   2930 C CA  . SER B 2 70  ? 39.808 43.430  -0.274  1.00 51.02  ?  70  SER C CA  1 
ATOM   2931 C C   . SER B 2 70  ? 39.036 44.719  -0.047  1.00 54.05  ?  70  SER C C   1 
ATOM   2932 O O   . SER B 2 70  ? 38.241 45.141  -0.891  1.00 53.27  ?  70  SER C O   1 
ATOM   2933 C CB  . SER B 2 70  ? 41.256 43.726  -0.682  1.00 52.70  ?  70  SER C CB  1 
ATOM   2934 O OG  . SER B 2 70  ? 41.304 44.615  -1.785  1.00 50.34  ?  70  SER C OG  1 
ATOM   2935 N N   . ARG B 2 71  ? 39.277 45.345  1.103   1.00 50.56  ?  71  ARG C N   1 
ATOM   2936 C CA  . ARG B 2 71  ? 38.534 46.534  1.488   1.00 48.42  ?  71  ARG C CA  1 
ATOM   2937 C C   . ARG B 2 71  ? 39.442 47.492  2.246   1.00 56.21  ?  71  ARG C C   1 
ATOM   2938 O O   . ARG B 2 71  ? 40.454 47.096  2.827   1.00 54.90  ?  71  ARG C O   1 
ATOM   2939 C CB  . ARG B 2 71  ? 37.312 46.177  2.350   1.00 53.58  ?  71  ARG C CB  1 
ATOM   2940 C CG  . ARG B 2 71  ? 37.648 45.393  3.614   1.00 56.47  ?  71  ARG C CG  1 
ATOM   2941 C CD  . ARG B 2 71  ? 37.571 46.272  4.854   1.00 60.47  ?  71  ARG C CD  1 
ATOM   2942 N NE  . ARG B 2 71  ? 37.870 45.536  6.077   1.00 61.05  ?  71  ARG C NE  1 
ATOM   2943 C CZ  . ARG B 2 71  ? 39.094 45.251  6.501   1.00 59.56  ?  71  ARG C CZ  1 
ATOM   2944 N NH1 . ARG B 2 71  ? 40.165 45.614  5.814   1.00 59.12  ?  71  ARG C NH1 1 
ATOM   2945 N NH2 . ARG B 2 71  ? 39.246 44.586  7.642   1.00 61.52  ?  71  ARG C NH2 1 
ATOM   2946 N N   . GLU B 2 72  ? 39.059 48.767  2.224   1.00 63.01  ?  72  GLU C N   1 
ATOM   2947 C CA  . GLU B 2 72  ? 39.707 49.777  3.045   1.00 62.26  ?  72  GLU C CA  1 
ATOM   2948 C C   . GLU B 2 72  ? 39.158 49.724  4.465   1.00 64.27  ?  72  GLU C C   1 
ATOM   2949 O O   . GLU B 2 72  ? 37.979 49.435  4.686   1.00 64.02  ?  72  GLU C O   1 
ATOM   2950 C CB  . GLU B 2 72  ? 39.493 51.172  2.457   1.00 59.80  ?  72  GLU C CB  1 
ATOM   2951 C CG  . GLU B 2 72  ? 40.136 51.388  1.097   1.00 63.59  ?  72  GLU C CG  1 
ATOM   2952 C CD  . GLU B 2 72  ? 41.650 51.426  1.171   1.00 70.14  ?  72  GLU C CD  1 
ATOM   2953 O OE1 . GLU B 2 72  ? 42.191 52.356  1.805   1.00 72.88  ?  72  GLU C OE1 1 
ATOM   2954 O OE2 . GLU B 2 72  ? 42.297 50.529  0.590   1.00 69.55  ?  72  GLU C OE2 1 
ATOM   2955 N N   . ASN B 2 73  ? 40.030 50.014  5.435   1.00 69.85  ?  73  ASN C N   1 
ATOM   2956 C CA  . ASN B 2 73  ? 39.628 49.934  6.837   1.00 65.15  ?  73  ASN C CA  1 
ATOM   2957 C C   . ASN B 2 73  ? 38.498 50.904  7.158   1.00 65.74  ?  73  ASN C C   1 
ATOM   2958 O O   . ASN B 2 73  ? 37.698 50.647  8.066   1.00 64.55  ?  73  ASN C O   1 
ATOM   2959 C CB  . ASN B 2 73  ? 40.832 50.199  7.742   1.00 66.22  ?  73  ASN C CB  1 
ATOM   2960 C CG  . ASN B 2 73  ? 41.667 48.954  7.979   1.00 68.98  ?  73  ASN C CG  1 
ATOM   2961 O OD1 . ASN B 2 73  ? 41.138 47.847  8.072   1.00 72.45  ?  73  ASN C OD1 1 
ATOM   2962 N ND2 . ASN B 2 73  ? 42.980 49.132  8.071   1.00 71.61  ?  73  ASN C ND2 1 
ATOM   2963 N N   . ALA B 2 74  ? 38.409 52.015  6.424   1.00 64.96  ?  74  ALA C N   1 
ATOM   2964 C CA  . ALA B 2 74  ? 37.343 52.987  6.624   1.00 59.22  ?  74  ALA C CA  1 
ATOM   2965 C C   . ALA B 2 74  ? 36.044 52.597  5.935   1.00 62.58  ?  74  ALA C C   1 
ATOM   2966 O O   . ALA B 2 74  ? 35.023 53.256  6.162   1.00 63.24  ?  74  ALA C O   1 
ATOM   2967 C CB  . ALA B 2 74  ? 37.786 54.365  6.126   1.00 55.98  ?  74  ALA C CB  1 
ATOM   2968 N N   . LYS B 2 75  ? 36.061 51.555  5.101   1.00 61.44  ?  75  LYS C N   1 
ATOM   2969 C CA  . LYS B 2 75  ? 34.877 51.055  4.407   1.00 58.19  ?  75  LYS C CA  1 
ATOM   2970 C C   . LYS B 2 75  ? 34.314 52.077  3.417   1.00 56.41  ?  75  LYS C C   1 
ATOM   2971 O O   . LYS B 2 75  ? 33.111 52.095  3.140   1.00 56.90  ?  75  LYS C O   1 
ATOM   2972 C CB  . LYS B 2 75  ? 33.811 50.596  5.406   1.00 59.58  ?  75  LYS C CB  1 
ATOM   2973 C CG  . LYS B 2 75  ? 34.161 49.285  6.123   1.00 58.89  ?  75  LYS C CG  1 
ATOM   2974 C CD  . LYS B 2 75  ? 33.636 49.262  7.558   1.00 58.79  ?  75  LYS C CD  1 
ATOM   2975 C CE  . LYS B 2 75  ? 32.418 50.148  7.701   1.00 57.45  ?  75  LYS C CE  1 
ATOM   2976 N NZ  . LYS B 2 75  ? 31.648 50.027  8.985   1.00 53.39  ?  75  LYS C NZ  1 
ATOM   2977 N N   . ASN B 2 76  ? 35.181 52.919  2.852   1.00 54.14  ?  76  ASN C N   1 
ATOM   2978 C CA  . ASN B 2 76  ? 34.778 53.818  1.780   1.00 59.53  ?  76  ASN C CA  1 
ATOM   2979 C C   . ASN B 2 76  ? 34.998 53.219  0.397   1.00 55.96  ?  76  ASN C C   1 
ATOM   2980 O O   . ASN B 2 76  ? 34.520 53.791  -0.590  1.00 53.28  ?  76  ASN C O   1 
ATOM   2981 C CB  . ASN B 2 76  ? 35.526 55.155  1.887   1.00 54.45  ?  76  ASN C CB  1 
ATOM   2982 C CG  . ASN B 2 76  ? 37.033 54.990  1.871   1.00 56.19  ?  76  ASN C CG  1 
ATOM   2983 O OD1 . ASN B 2 76  ? 37.591 54.190  2.620   1.00 55.16  ?  76  ASN C OD1 1 
ATOM   2984 N ND2 . ASN B 2 76  ? 37.700 55.751  1.011   1.00 60.33  ?  76  ASN C ND2 1 
ATOM   2985 N N   . ALA B 2 77  ? 35.689 52.084  0.305   1.00 56.33  ?  77  ALA C N   1 
ATOM   2986 C CA  . ALA B 2 77  ? 35.940 51.428  -0.969  1.00 54.43  ?  77  ALA C CA  1 
ATOM   2987 C C   . ALA B 2 77  ? 36.408 50.002  -0.718  1.00 55.23  ?  77  ALA C C   1 
ATOM   2988 O O   . ALA B 2 77  ? 37.186 49.756  0.207   1.00 52.22  ?  77  ALA C O   1 
ATOM   2989 C CB  . ALA B 2 77  ? 36.992 52.189  -1.789  1.00 54.16  ?  77  ALA C CB  1 
ATOM   2990 N N   . TRP B 2 78  ? 35.923 49.071  -1.538  1.00 48.89  ?  78  TRP C N   1 
ATOM   2991 C CA  . TRP B 2 78  ? 36.447 47.715  -1.574  1.00 48.14  ?  78  TRP C CA  1 
ATOM   2992 C C   . TRP B 2 78  ? 36.698 47.323  -3.023  1.00 48.19  ?  78  TRP C C   1 
ATOM   2993 O O   . TRP B 2 78  ? 36.192 47.954  -3.955  1.00 52.06  ?  78  TRP C O   1 
ATOM   2994 C CB  . TRP B 2 78  ? 35.513 46.701  -0.886  1.00 45.01  ?  78  TRP C CB  1 
ATOM   2995 C CG  . TRP B 2 78  ? 34.057 46.832  -1.207  1.00 47.71  ?  78  TRP C CG  1 
ATOM   2996 C CD1 . TRP B 2 78  ? 33.329 46.039  -2.046  1.00 41.30  ?  78  TRP C CD1 1 
ATOM   2997 C CD2 . TRP B 2 78  ? 33.141 47.791  -0.666  1.00 48.59  ?  78  TRP C CD2 1 
ATOM   2998 N NE1 . TRP B 2 78  ? 32.019 46.455  -2.073  1.00 41.50  ?  78  TRP C NE1 1 
ATOM   2999 C CE2 . TRP B 2 78  ? 31.878 47.529  -1.234  1.00 46.01  ?  78  TRP C CE2 1 
ATOM   3000 C CE3 . TRP B 2 78  ? 33.266 48.851  0.236   1.00 48.32  ?  78  TRP C CE3 1 
ATOM   3001 C CZ2 . TRP B 2 78  ? 30.749 48.287  -0.929  1.00 42.11  ?  78  TRP C CZ2 1 
ATOM   3002 C CZ3 . TRP B 2 78  ? 32.145 49.602  0.539   1.00 48.03  ?  78  TRP C CZ3 1 
ATOM   3003 C CH2 . TRP B 2 78  ? 30.903 49.317  -0.043  1.00 46.03  ?  78  TRP C CH2 1 
ATOM   3004 N N   . TYR B 2 79  ? 37.497 46.275  -3.207  1.00 48.96  ?  79  TYR C N   1 
ATOM   3005 C CA  . TYR B 2 79  ? 38.060 45.951  -4.509  1.00 47.93  ?  79  TYR C CA  1 
ATOM   3006 C C   . TYR B 2 79  ? 37.889 44.471  -4.820  1.00 50.99  ?  79  TYR C C   1 
ATOM   3007 O O   . TYR B 2 79  ? 37.555 43.656  -3.954  1.00 46.78  ?  79  TYR C O   1 
ATOM   3008 C CB  . TYR B 2 79  ? 39.544 46.335  -4.567  1.00 48.64  ?  79  TYR C CB  1 
ATOM   3009 C CG  . TYR B 2 79  ? 39.811 47.748  -4.104  1.00 54.08  ?  79  TYR C CG  1 
ATOM   3010 C CD1 . TYR B 2 79  ? 39.533 48.832  -4.926  1.00 55.16  ?  79  TYR C CD1 1 
ATOM   3011 C CD2 . TYR B 2 79  ? 40.322 48.001  -2.837  1.00 50.81  ?  79  TYR C CD2 1 
ATOM   3012 C CE1 . TYR B 2 79  ? 39.767 50.128  -4.506  1.00 58.16  ?  79  TYR C CE1 1 
ATOM   3013 C CE2 . TYR B 2 79  ? 40.559 49.293  -2.407  1.00 54.09  ?  79  TYR C CE2 1 
ATOM   3014 C CZ  . TYR B 2 79  ? 40.280 50.353  -3.246  1.00 51.01  ?  79  TYR C CZ  1 
ATOM   3015 O OH  . TYR B 2 79  ? 40.512 51.641  -2.826  1.00 58.85  ?  79  TYR C OH  1 
ATOM   3016 N N   . LEU B 2 80  ? 38.125 44.135  -6.088  1.00 46.00  ?  80  LEU C N   1 
ATOM   3017 C CA  . LEU B 2 80  ? 38.074 42.758  -6.573  1.00 44.70  ?  80  LEU C CA  1 
ATOM   3018 C C   . LEU B 2 80  ? 39.178 42.586  -7.606  1.00 44.79  ?  80  LEU C C   1 
ATOM   3019 O O   . LEU B 2 80  ? 39.055 43.071  -8.735  1.00 43.34  ?  80  LEU C O   1 
ATOM   3020 C CB  . LEU B 2 80  ? 36.710 42.427  -7.180  1.00 45.02  ?  80  LEU C CB  1 
ATOM   3021 C CG  . LEU B 2 80  ? 36.482 40.951  -7.516  1.00 44.73  ?  80  LEU C CG  1 
ATOM   3022 C CD1 . LEU B 2 80  ? 36.708 40.086  -6.287  1.00 41.62  ?  80  LEU C CD1 1 
ATOM   3023 C CD2 . LEU B 2 80  ? 35.092 40.726  -8.095  1.00 41.74  ?  80  LEU C CD2 1 
ATOM   3024 N N   . GLN B 2 81  ? 40.255 41.906  -7.221  1.00 40.80  ?  81  GLN C N   1 
ATOM   3025 C CA  . GLN B 2 81  ? 41.364 41.616  -8.126  1.00 43.90  ?  81  GLN C CA  1 
ATOM   3026 C C   . GLN B 2 81  ? 41.043 40.334  -8.883  1.00 47.65  ?  81  GLN C C   1 
ATOM   3027 O O   . GLN B 2 81  ? 41.007 39.249  -8.295  1.00 49.81  ?  81  GLN C O   1 
ATOM   3028 C CB  . GLN B 2 81  ? 42.672 41.492  -7.350  1.00 41.93  ?  81  GLN C CB  1 
ATOM   3029 C CG  . GLN B 2 81  ? 43.905 41.298  -8.219  1.00 48.95  ?  81  GLN C CG  1 
ATOM   3030 C CD  . GLN B 2 81  ? 44.064 42.390  -9.262  1.00 47.84  ?  81  GLN C CD  1 
ATOM   3031 O OE1 . GLN B 2 81  ? 43.895 43.574  -8.970  1.00 54.98  ?  81  GLN C OE1 1 
ATOM   3032 N NE2 . GLN B 2 81  ? 44.399 41.994  -10.483 1.00 48.75  ?  81  GLN C NE2 1 
ATOM   3033 N N   . MET B 2 82  ? 40.809 40.457  -10.188 1.00 46.22  ?  82  MET C N   1 
ATOM   3034 C CA  . MET B 2 82  ? 40.398 39.340  -11.032 1.00 47.67  ?  82  MET C CA  1 
ATOM   3035 C C   . MET B 2 82  ? 41.569 38.937  -11.922 1.00 45.81  ?  82  MET C C   1 
ATOM   3036 O O   . MET B 2 82  ? 41.952 39.685  -12.827 1.00 49.48  ?  82  MET C O   1 
ATOM   3037 C CB  . MET B 2 82  ? 39.178 39.716  -11.872 1.00 47.86  ?  82  MET C CB  1 
ATOM   3038 C CG  . MET B 2 82  ? 37.969 40.156  -11.061 1.00 45.22  ?  82  MET C CG  1 
ATOM   3039 S SD  . MET B 2 82  ? 36.795 41.105  -12.045 1.00 48.70  ?  82  MET C SD  1 
ATOM   3040 C CE  . MET B 2 82  ? 35.872 39.793  -12.831 1.00 45.38  ?  82  MET C CE  1 
ATOM   3041 N N   . ASN B 2 83  ? 42.129 37.756  -11.669 1.00 50.13  ?  83  ASN C N   1 
ATOM   3042 C CA  . ASN B 2 83  ? 43.224 37.216  -12.458 1.00 49.84  ?  83  ASN C CA  1 
ATOM   3043 C C   . ASN B 2 83  ? 42.775 35.943  -13.167 1.00 49.17  ?  83  ASN C C   1 
ATOM   3044 O O   . ASN B 2 83  ? 41.782 35.316  -12.791 1.00 52.14  ?  83  ASN C O   1 
ATOM   3045 C CB  . ASN B 2 83  ? 44.450 36.919  -11.584 1.00 44.77  ?  83  ASN C CB  1 
ATOM   3046 C CG  . ASN B 2 83  ? 44.920 38.130  -10.805 1.00 47.01  ?  83  ASN C CG  1 
ATOM   3047 O OD1 . ASN B 2 83  ? 44.884 39.257  -11.302 1.00 56.95  ?  83  ASN C OD1 1 
ATOM   3048 N ND2 . ASN B 2 83  ? 45.360 37.905  -9.572  1.00 51.59  ?  83  ASN C ND2 1 
ATOM   3049 N N   . SER B 2 84  ? 43.532 35.567  -14.200 1.00 45.55  ?  84  SER C N   1 
ATOM   3050 C CA  . SER B 2 84  ? 43.263 34.365  -14.991 1.00 47.24  ?  84  SER C CA  1 
ATOM   3051 C C   . SER B 2 84  ? 41.818 34.345  -15.481 1.00 46.25  ?  84  SER C C   1 
ATOM   3052 O O   . SER B 2 84  ? 41.073 33.384  -15.277 1.00 47.79  ?  84  SER C O   1 
ATOM   3053 C CB  . SER B 2 84  ? 43.590 33.100  -14.195 1.00 47.97  ?  84  SER C CB  1 
ATOM   3054 O OG  . SER B 2 84  ? 44.965 33.056  -13.857 1.00 57.84  ?  84  SER C OG  1 
ATOM   3055 N N   . LEU B 2 85  ? 41.424 35.433  -16.135 1.00 45.96  ?  85  LEU C N   1 
ATOM   3056 C CA  . LEU B 2 85  ? 40.043 35.583  -16.570 1.00 44.20  ?  85  LEU C CA  1 
ATOM   3057 C C   . LEU B 2 85  ? 39.726 34.619  -17.706 1.00 44.13  ?  85  LEU C C   1 
ATOM   3058 O O   . LEU B 2 85  ? 40.561 34.355  -18.575 1.00 44.48  ?  85  LEU C O   1 
ATOM   3059 C CB  . LEU B 2 85  ? 39.780 37.025  -17.004 1.00 44.58  ?  85  LEU C CB  1 
ATOM   3060 C CG  . LEU B 2 85  ? 39.522 38.005  -15.856 1.00 44.99  ?  85  LEU C CG  1 
ATOM   3061 C CD1 . LEU B 2 85  ? 39.763 39.439  -16.298 1.00 45.00  ?  85  LEU C CD1 1 
ATOM   3062 C CD2 . LEU B 2 85  ? 38.110 37.839  -15.317 1.00 45.23  ?  85  LEU C CD2 1 
ATOM   3063 N N   . LYS B 2 86  ? 38.511 34.086  -17.684 1.00 42.76  ?  86  LYS C N   1 
ATOM   3064 C CA  . LYS B 2 86  ? 37.997 33.168  -18.686 1.00 46.69  ?  86  LYS C CA  1 
ATOM   3065 C C   . LYS B 2 86  ? 36.709 33.730  -19.272 1.00 45.86  ?  86  LYS C C   1 
ATOM   3066 O O   . LYS B 2 86  ? 36.042 34.557  -18.639 1.00 44.53  ?  86  LYS C O   1 
ATOM   3067 C CB  . LYS B 2 86  ? 37.732 31.783  -18.075 1.00 42.37  ?  86  LYS C CB  1 
ATOM   3068 C CG  . LYS B 2 86  ? 38.612 31.455  -16.879 1.00 47.28  ?  86  LYS C CG  1 
ATOM   3069 C CD  . LYS B 2 86  ? 38.031 30.319  -16.050 1.00 52.40  ?  86  LYS C CD  1 
ATOM   3070 C CE  . LYS B 2 86  ? 39.125 29.382  -15.563 1.00 55.93  ?  86  LYS C CE  1 
ATOM   3071 N NZ  . LYS B 2 86  ? 38.576 28.119  -15.001 1.00 51.77  ?  86  LYS C NZ  1 
ATOM   3072 N N   . PRO B 2 87  ? 36.331 33.311  -20.484 1.00 46.57  ?  87  PRO C N   1 
ATOM   3073 C CA  . PRO B 2 87  ? 35.069 33.799  -21.067 1.00 48.72  ?  87  PRO C CA  1 
ATOM   3074 C C   . PRO B 2 87  ? 33.854 33.541  -20.192 1.00 48.42  ?  87  PRO C C   1 
ATOM   3075 O O   . PRO B 2 87  ? 32.849 34.249  -20.330 1.00 43.74  ?  87  PRO C O   1 
ATOM   3076 C CB  . PRO B 2 87  ? 34.972 33.029  -22.391 1.00 49.98  ?  87  PRO C CB  1 
ATOM   3077 C CG  . PRO B 2 87  ? 36.383 32.695  -22.735 1.00 48.42  ?  87  PRO C CG  1 
ATOM   3078 C CD  . PRO B 2 87  ? 37.089 32.469  -21.428 1.00 48.82  ?  87  PRO C CD  1 
ATOM   3079 N N   . GLU B 2 88  ? 33.916 32.559  -19.292 1.00 46.62  ?  88  GLU C N   1 
ATOM   3080 C CA  . GLU B 2 88  ? 32.798 32.287  -18.397 1.00 47.29  ?  88  GLU C CA  1 
ATOM   3081 C C   . GLU B 2 88  ? 32.596 33.398  -17.375 1.00 42.65  ?  88  GLU C C   1 
ATOM   3082 O O   . GLU B 2 88  ? 31.498 33.521  -16.821 1.00 42.38  ?  88  GLU C O   1 
ATOM   3083 C CB  . GLU B 2 88  ? 33.010 30.950  -17.679 1.00 48.90  ?  88  GLU C CB  1 
ATOM   3084 C CG  . GLU B 2 88  ? 34.027 30.013  -18.342 1.00 54.78  ?  88  GLU C CG  1 
ATOM   3085 C CD  . GLU B 2 88  ? 33.661 29.609  -19.767 1.00 68.10  ?  88  GLU C CD  1 
ATOM   3086 O OE1 . GLU B 2 88  ? 32.473 29.708  -20.144 1.00 58.18  ?  88  GLU C OE1 1 
ATOM   3087 O OE2 . GLU B 2 88  ? 34.575 29.200  -20.514 1.00 74.32  ?  88  GLU C OE2 1 
ATOM   3088 N N   . ASP B 2 89  ? 33.625 34.204  -17.112 1.00 41.80  ?  89  ASP C N   1 
ATOM   3089 C CA  . ASP B 2 89  ? 33.526 35.319  -16.179 1.00 42.11  ?  89  ASP C CA  1 
ATOM   3090 C C   . ASP B 2 89  ? 32.849 36.541  -16.784 1.00 42.26  ?  89  ASP C C   1 
ATOM   3091 O O   . ASP B 2 89  ? 32.724 37.560  -16.096 1.00 39.44  ?  89  ASP C O   1 
ATOM   3092 C CB  . ASP B 2 89  ? 34.919 35.703  -15.670 1.00 41.46  ?  89  ASP C CB  1 
ATOM   3093 C CG  . ASP B 2 89  ? 35.653 34.535  -15.034 1.00 45.29  ?  89  ASP C CG  1 
ATOM   3094 O OD1 . ASP B 2 89  ? 35.056 33.842  -14.182 1.00 46.78  ?  89  ASP C OD1 1 
ATOM   3095 O OD2 . ASP B 2 89  ? 36.830 34.311  -15.388 1.00 45.02  ?  89  ASP C OD2 1 
ATOM   3096 N N   . THR B 2 90  ? 32.415 36.468  -18.042 1.00 38.82  ?  90  THR C N   1 
ATOM   3097 C CA  . THR B 2 90  ? 31.760 37.600  -18.687 1.00 38.09  ?  90  THR C CA  1 
ATOM   3098 C C   . THR B 2 90  ? 30.403 37.864  -18.044 1.00 39.95  ?  90  THR C C   1 
ATOM   3099 O O   . THR B 2 90  ? 29.608 36.941  -17.843 1.00 43.47  ?  90  THR C O   1 
ATOM   3100 C CB  . THR B 2 90  ? 31.592 37.334  -20.186 1.00 41.38  ?  90  THR C CB  1 
ATOM   3101 O OG1 . THR B 2 90  ? 32.865 37.421  -20.838 1.00 39.01  ?  90  THR C OG1 1 
ATOM   3102 C CG2 . THR B 2 90  ? 30.640 38.343  -20.814 1.00 42.01  ?  90  THR C CG2 1 
ATOM   3103 N N   . GLY B 2 91  ? 30.146 39.120  -17.716 1.00 42.91  ?  91  GLY C N   1 
ATOM   3104 C CA  . GLY B 2 91  ? 28.871 39.500  -17.144 1.00 38.43  ?  91  GLY C CA  1 
ATOM   3105 C C   . GLY B 2 91  ? 28.956 40.872  -16.513 1.00 36.40  ?  91  GLY C C   1 
ATOM   3106 O O   . GLY B 2 91  ? 30.005 41.518  -16.500 1.00 39.27  ?  91  GLY C O   1 
ATOM   3107 N N   . VAL B 2 92  ? 27.816 41.306  -15.987 1.00 37.54  ?  92  VAL C N   1 
ATOM   3108 C CA  . VAL B 2 92  ? 27.717 42.574  -15.274 1.00 38.63  ?  92  VAL C CA  1 
ATOM   3109 C C   . VAL B 2 92  ? 28.025 42.317  -13.805 1.00 41.89  ?  92  VAL C C   1 
ATOM   3110 O O   . VAL B 2 92  ? 27.383 41.477  -13.165 1.00 38.32  ?  92  VAL C O   1 
ATOM   3111 C CB  . VAL B 2 92  ? 26.330 43.207  -15.448 1.00 41.89  ?  92  VAL C CB  1 
ATOM   3112 C CG1 . VAL B 2 92  ? 26.278 44.567  -14.770 1.00 39.69  ?  92  VAL C CG1 1 
ATOM   3113 C CG2 . VAL B 2 92  ? 25.983 43.326  -16.928 1.00 41.52  ?  92  VAL C CG2 1 
ATOM   3114 N N   . TYR B 2 93  ? 29.007 43.037  -13.271 1.00 41.78  ?  93  TYR C N   1 
ATOM   3115 C CA  . TYR B 2 93  ? 29.450 42.869  -11.894 1.00 39.06  ?  93  TYR C CA  1 
ATOM   3116 C C   . TYR B 2 93  ? 28.939 44.021  -11.040 1.00 41.05  ?  93  TYR C C   1 
ATOM   3117 O O   . TYR B 2 93  ? 29.170 45.191  -11.363 1.00 45.49  ?  93  TYR C O   1 
ATOM   3118 C CB  . TYR B 2 93  ? 30.976 42.791  -11.820 1.00 37.80  ?  93  TYR C CB  1 
ATOM   3119 C CG  . TYR B 2 93  ? 31.537 41.457  -12.263 1.00 37.73  ?  93  TYR C CG  1 
ATOM   3120 C CD1 . TYR B 2 93  ? 31.546 41.100  -13.605 1.00 34.27  ?  93  TYR C CD1 1 
ATOM   3121 C CD2 . TYR B 2 93  ? 32.048 40.555  -11.340 1.00 36.90  ?  93  TYR C CD2 1 
ATOM   3122 C CE1 . TYR B 2 93  ? 32.050 39.882  -14.015 1.00 37.25  ?  93  TYR C CE1 1 
ATOM   3123 C CE2 . TYR B 2 93  ? 32.555 39.335  -11.742 1.00 38.71  ?  93  TYR C CE2 1 
ATOM   3124 C CZ  . TYR B 2 93  ? 32.553 39.003  -13.081 1.00 39.87  ?  93  TYR C CZ  1 
ATOM   3125 O OH  . TYR B 2 93  ? 33.060 37.791  -13.488 1.00 35.69  ?  93  TYR C OH  1 
ATOM   3126 N N   . TYR B 2 94  ? 28.246 43.687  -9.954  1.00 41.92  ?  94  TYR C N   1 
ATOM   3127 C CA  . TYR B 2 94  ? 27.693 44.665  -9.027  1.00 36.17  ?  94  TYR C CA  1 
ATOM   3128 C C   . TYR B 2 94  ? 28.410 44.560  -7.689  1.00 44.30  ?  94  TYR C C   1 
ATOM   3129 O O   . TYR B 2 94  ? 28.586 43.456  -7.161  1.00 38.31  ?  94  TYR C O   1 
ATOM   3130 C CB  . TYR B 2 94  ? 26.191 44.452  -8.813  1.00 40.04  ?  94  TYR C CB  1 
ATOM   3131 C CG  . TYR B 2 94  ? 25.362 44.310  -10.072 1.00 43.29  ?  94  TYR C CG  1 
ATOM   3132 C CD1 . TYR B 2 94  ? 25.321 43.108  -10.769 1.00 45.24  ?  94  TYR C CD1 1 
ATOM   3133 C CD2 . TYR B 2 94  ? 24.599 45.368  -10.547 1.00 41.83  ?  94  TYR C CD2 1 
ATOM   3134 C CE1 . TYR B 2 94  ? 24.560 42.971  -11.914 1.00 46.67  ?  94  TYR C CE1 1 
ATOM   3135 C CE2 . TYR B 2 94  ? 23.833 45.240  -11.691 1.00 44.96  ?  94  TYR C CE2 1 
ATOM   3136 C CZ  . TYR B 2 94  ? 23.817 44.039  -12.370 1.00 52.54  ?  94  TYR C CZ  1 
ATOM   3137 O OH  . TYR B 2 94  ? 23.058 43.904  -13.511 1.00 61.52  ?  94  TYR C OH  1 
ATOM   3138 N N   . CYS B 2 95  ? 28.811 45.701  -7.138  1.00 41.80  ?  95  CYS C N   1 
ATOM   3139 C CA  . CYS B 2 95  ? 29.289 45.740  -5.765  1.00 38.58  ?  95  CYS C CA  1 
ATOM   3140 C C   . CYS B 2 95  ? 28.105 45.922  -4.824  1.00 41.13  ?  95  CYS C C   1 
ATOM   3141 O O   . CYS B 2 95  ? 27.085 46.513  -5.185  1.00 43.09  ?  95  CYS C O   1 
ATOM   3142 C CB  . CYS B 2 95  ? 30.321 46.853  -5.561  1.00 44.53  ?  95  CYS C CB  1 
ATOM   3143 S SG  . CYS B 2 95  ? 29.693 48.546  -5.602  1.00 59.29  ?  95  CYS C SG  1 
ATOM   3144 N N   . HIS B 2 96  ? 28.245 45.386  -3.615  1.00 41.16  ?  96  HIS C N   1 
ATOM   3145 C CA  . HIS B 2 96  ? 27.139 45.310  -2.673  1.00 42.18  ?  96  HIS C CA  1 
ATOM   3146 C C   . HIS B 2 96  ? 27.647 45.648  -1.279  1.00 39.48  ?  96  HIS C C   1 
ATOM   3147 O O   . HIS B 2 96  ? 28.833 45.500  -0.975  1.00 38.63  ?  96  HIS C O   1 
ATOM   3148 C CB  . HIS B 2 96  ? 26.494 43.916  -2.695  1.00 38.11  ?  96  HIS C CB  1 
ATOM   3149 C CG  . HIS B 2 96  ? 25.163 43.850  -2.014  1.00 40.74  ?  96  HIS C CG  1 
ATOM   3150 N ND1 . HIS B 2 96  ? 24.898 42.973  -0.984  1.00 47.91  ?  96  HIS C ND1 1 
ATOM   3151 C CD2 . HIS B 2 96  ? 24.020 44.546  -2.218  1.00 46.21  ?  96  HIS C CD2 1 
ATOM   3152 C CE1 . HIS B 2 96  ? 23.651 43.134  -0.581  1.00 44.38  ?  96  HIS C CE1 1 
ATOM   3153 N NE2 . HIS B 2 96  ? 23.096 44.080  -1.314  1.00 43.03  ?  96  HIS C NE2 1 
ATOM   3154 N N   . ALA B 2 97  ? 26.729 46.111  -0.432  1.00 40.06  ?  97  ALA C N   1 
ATOM   3155 C CA  . ALA B 2 97  ? 27.054 46.468  0.943   1.00 37.88  ?  97  ALA C CA  1 
ATOM   3156 C C   . ALA B 2 97  ? 25.807 46.314  1.799   1.00 41.92  ?  97  ALA C C   1 
ATOM   3157 O O   . ALA B 2 97  ? 24.740 46.812  1.431   1.00 43.49  ?  97  ALA C O   1 
ATOM   3158 C CB  . ALA B 2 97  ? 27.590 47.900  1.037   1.00 40.04  ?  97  ALA C CB  1 
ATOM   3159 N N   . VAL B 2 98  ? 25.948 45.627  2.930   1.00 41.30  ?  98  VAL C N   1 
ATOM   3160 C CA  . VAL B 2 98  ? 24.851 45.413  3.868   1.00 42.86  ?  98  VAL C CA  1 
ATOM   3161 C C   . VAL B 2 98  ? 24.978 46.423  5.001   1.00 44.42  ?  98  VAL C C   1 
ATOM   3162 O O   . VAL B 2 98  ? 26.040 46.541  5.625   1.00 44.85  ?  98  VAL C O   1 
ATOM   3163 C CB  . VAL B 2 98  ? 24.854 43.973  4.410   1.00 41.35  ?  98  VAL C CB  1 
ATOM   3164 C CG1 . VAL B 2 98  ? 23.780 43.803  5.469   1.00 37.71  ?  98  VAL C CG1 1 
ATOM   3165 C CG2 . VAL B 2 98  ? 24.640 42.980  3.277   1.00 42.83  ?  98  VAL C CG2 1 
ATOM   3166 N N   . THR B 2 99  ? 23.896 47.158  5.263   1.00 41.95  ?  99  THR C N   1 
ATOM   3167 C CA  . THR B 2 99  ? 23.861 48.127  6.349   1.00 50.75  ?  99  THR C CA  1 
ATOM   3168 C C   . THR B 2 99  ? 22.881 47.766  7.456   1.00 48.72  ?  99  THR C C   1 
ATOM   3169 O O   . THR B 2 99  ? 23.033 48.263  8.577   1.00 56.26  ?  99  THR C O   1 
ATOM   3170 C CB  . THR B 2 99  ? 23.512 49.524  5.810   1.00 49.05  ?  99  THR C CB  1 
ATOM   3171 O OG1 . THR B 2 99  ? 22.096 49.630  5.615   1.00 47.76  ?  99  THR C OG1 1 
ATOM   3172 C CG2 . THR B 2 99  ? 24.225 49.783  4.490   1.00 49.26  ?  99  THR C CG2 1 
ATOM   3173 N N   . GLY B 2 100 ? 21.891 46.920  7.172   1.00 49.17  ?  100 GLY C N   1 
ATOM   3174 C CA  . GLY B 2 100 ? 20.941 46.473  8.169   1.00 49.03  ?  100 GLY C CA  1 
ATOM   3175 C C   . GLY B 2 100 ? 20.562 45.026  7.928   1.00 46.97  ?  100 GLY C C   1 
ATOM   3176 O O   . GLY B 2 100 ? 21.031 44.395  6.979   1.00 53.30  ?  100 GLY C O   1 
ATOM   3177 N N   . VAL B 2 101 ? 19.701 44.508  8.805   1.00 43.95  ?  101 VAL C N   1 
ATOM   3178 C CA  . VAL B 2 101 ? 19.298 43.110  8.687   1.00 50.96  ?  101 VAL C CA  1 
ATOM   3179 C C   . VAL B 2 101 ? 18.517 42.872  7.399   1.00 51.53  ?  101 VAL C C   1 
ATOM   3180 O O   . VAL B 2 101 ? 18.518 41.756  6.863   1.00 52.51  ?  101 VAL C O   1 
ATOM   3181 C CB  . VAL B 2 101 ? 18.493 42.673  9.925   1.00 46.17  ?  101 VAL C CB  1 
ATOM   3182 C CG1 . VAL B 2 101 ? 19.354 42.773  11.173  1.00 48.92  ?  101 VAL C CG1 1 
ATOM   3183 C CG2 . VAL B 2 101 ? 17.231 43.513  10.068  1.00 47.42  ?  101 VAL C CG2 1 
ATOM   3184 N N   . ILE B 2 102 ? 17.845 43.898  6.880   1.00 49.62  ?  102 ILE C N   1 
ATOM   3185 C CA  . ILE B 2 102 ? 17.106 43.787  5.628   1.00 52.77  ?  102 ILE C CA  1 
ATOM   3186 C C   . ILE B 2 102 ? 17.352 45.031  4.786   1.00 52.05  ?  102 ILE C C   1 
ATOM   3187 O O   . ILE B 2 102 ? 16.581 45.335  3.870   1.00 59.46  ?  102 ILE C O   1 
ATOM   3188 C CB  . ILE B 2 102 ? 15.598 43.587  5.875   1.00 56.66  ?  102 ILE C CB  1 
ATOM   3189 C CG1 . ILE B 2 102 ? 15.069 44.645  6.847   1.00 59.69  ?  102 ILE C CG1 1 
ATOM   3190 C CG2 . ILE B 2 102 ? 15.312 42.176  6.380   1.00 53.34  ?  102 ILE C CG2 1 
ATOM   3191 C CD1 . ILE B 2 102 ? 13.558 44.705  6.927   1.00 59.70  ?  102 ILE C CD1 1 
ATOM   3192 N N   . ALA B 2 103 ? 18.426 45.755  5.088   1.00 51.73  ?  103 ALA C N   1 
ATOM   3193 C CA  . ALA B 2 103 ? 18.765 46.992  4.397   1.00 50.83  ?  103 ALA C CA  1 
ATOM   3194 C C   . ALA B 2 103 ? 20.138 46.860  3.757   1.00 51.09  ?  103 ALA C C   1 
ATOM   3195 O O   . ALA B 2 103 ? 21.116 46.531  4.437   1.00 55.62  ?  103 ALA C O   1 
ATOM   3196 C CB  . ALA B 2 103 ? 18.740 48.186  5.355   1.00 45.31  ?  103 ALA C CB  1 
ATOM   3197 N N   . SER B 2 104 ? 20.208 47.120  2.454   1.00 48.14  ?  104 SER C N   1 
ATOM   3198 C CA  . SER B 2 104 ? 21.462 47.040  1.720   1.00 47.80  ?  104 SER C CA  1 
ATOM   3199 C C   . SER B 2 104 ? 21.383 47.961  0.511   1.00 52.83  ?  104 SER C C   1 
ATOM   3200 O O   . SER B 2 104 ? 20.307 48.420  0.119   1.00 50.82  ?  104 SER C O   1 
ATOM   3201 C CB  . SER B 2 104 ? 21.768 45.600  1.292   1.00 46.23  ?  104 SER C CB  1 
ATOM   3202 O OG  . SER B 2 104 ? 20.776 45.109  0.409   1.00 48.33  ?  104 SER C OG  1 
ATOM   3203 N N   . SER B 2 105 ? 22.546 48.230  -0.079  1.00 45.68  ?  105 SER C N   1 
ATOM   3204 C CA  . SER B 2 105 ? 22.648 49.094  -1.246  1.00 49.73  ?  105 SER C CA  1 
ATOM   3205 C C   . SER B 2 105 ? 23.383 48.366  -2.363  1.00 52.49  ?  105 SER C C   1 
ATOM   3206 O O   . SER B 2 105 ? 24.317 47.599  -2.110  1.00 48.83  ?  105 SER C O   1 
ATOM   3207 C CB  . SER B 2 105 ? 23.370 50.407  -0.913  1.00 51.47  ?  105 SER C CB  1 
ATOM   3208 O OG  . SER B 2 105 ? 23.800 50.434  0.437   1.00 55.90  ?  105 SER C OG  1 
ATOM   3209 N N   . TRP B 2 106 ? 22.953 48.613  -3.596  1.00 49.21  ?  106 TRP C N   1 
ATOM   3210 C CA  . TRP B 2 106 ? 23.527 47.992  -4.780  1.00 49.94  ?  106 TRP C CA  1 
ATOM   3211 C C   . TRP B 2 106 ? 24.210 49.044  -5.640  1.00 51.46  ?  106 TRP C C   1 
ATOM   3212 O O   . TRP B 2 106 ? 23.732 50.177  -5.750  1.00 46.81  ?  106 TRP C O   1 
ATOM   3213 C CB  . TRP B 2 106 ? 22.453 47.286  -5.609  1.00 45.35  ?  106 TRP C CB  1 
ATOM   3214 C CG  . TRP B 2 106 ? 22.021 45.968  -5.067  1.00 52.31  ?  106 TRP C CG  1 
ATOM   3215 C CD1 . TRP B 2 106 ? 20.901 45.712  -4.331  1.00 51.21  ?  106 TRP C CD1 1 
ATOM   3216 C CD2 . TRP B 2 106 ? 22.696 44.713  -5.223  1.00 47.70  ?  106 TRP C CD2 1 
ATOM   3217 N NE1 . TRP B 2 106 ? 20.838 44.376  -4.016  1.00 48.13  ?  106 TRP C NE1 1 
ATOM   3218 C CE2 . TRP B 2 106 ? 21.926 43.742  -4.552  1.00 52.43  ?  106 TRP C CE2 1 
ATOM   3219 C CE3 . TRP B 2 106 ? 23.876 44.320  -5.860  1.00 45.57  ?  106 TRP C CE3 1 
ATOM   3220 C CZ2 . TRP B 2 106 ? 22.300 42.399  -4.501  1.00 46.61  ?  106 TRP C CZ2 1 
ATOM   3221 C CZ3 . TRP B 2 106 ? 24.244 42.987  -5.809  1.00 47.46  ?  106 TRP C CZ3 1 
ATOM   3222 C CH2 . TRP B 2 106 ? 23.458 42.043  -5.134  1.00 48.49  ?  106 TRP C CH2 1 
ATOM   3223 N N   . GLY B 2 107 ? 25.323 48.663  -6.252  1.00 48.85  ?  107 GLY C N   1 
ATOM   3224 C CA  . GLY B 2 107 ? 25.947 49.497  -7.252  1.00 53.45  ?  107 GLY C CA  1 
ATOM   3225 C C   . GLY B 2 107 ? 25.181 49.458  -8.561  1.00 52.31  ?  107 GLY C C   1 
ATOM   3226 O O   . GLY B 2 107 ? 24.193 48.742  -8.730  1.00 48.00  ?  107 GLY C O   1 
ATOM   3227 N N   . GLN B 2 108 ? 25.661 50.256  -9.517  1.00 52.58  ?  108 GLN C N   1 
ATOM   3228 C CA  . GLN B 2 108 ? 24.990 50.347  -10.808 1.00 52.52  ?  108 GLN C CA  1 
ATOM   3229 C C   . GLN B 2 108 ? 25.278 49.129  -11.677 1.00 52.05  ?  108 GLN C C   1 
ATOM   3230 O O   . GLN B 2 108 ? 24.397 48.658  -12.406 1.00 47.93  ?  108 GLN C O   1 
ATOM   3231 C CB  . GLN B 2 108 ? 25.411 51.629  -11.531 1.00 57.73  ?  108 GLN C CB  1 
ATOM   3232 C CG  . GLN B 2 108 ? 26.021 52.695  -10.627 1.00 63.62  ?  108 GLN C CG  1 
ATOM   3233 C CD  . GLN B 2 108 ? 25.035 53.248  -9.611  1.00 75.79  ?  108 GLN C CD  1 
ATOM   3234 O OE1 . GLN B 2 108 ? 24.006 53.820  -9.974  1.00 66.60  ?  108 GLN C OE1 1 
ATOM   3235 N NE2 . GLN B 2 108 ? 25.349 53.084  -8.331  1.00 73.86  ?  108 GLN C NE2 1 
ATOM   3236 N N   . GLY B 2 109 ? 26.499 48.606  -11.614 1.00 43.57  ?  109 GLY C N   1 
ATOM   3237 C CA  . GLY B 2 109 ? 26.864 47.447  -12.401 1.00 48.54  ?  109 GLY C CA  1 
ATOM   3238 C C   . GLY B 2 109 ? 27.778 47.784  -13.561 1.00 51.87  ?  109 GLY C C   1 
ATOM   3239 O O   . GLY B 2 109 ? 27.406 48.555  -14.451 1.00 57.15  ?  109 GLY C O   1 
ATOM   3240 N N   . THR B 2 110 ? 28.979 47.214  -13.557 1.00 50.45  ?  110 THR C N   1 
ATOM   3241 C CA  . THR B 2 110 ? 29.947 47.408  -14.625 1.00 46.23  ?  110 THR C CA  1 
ATOM   3242 C C   . THR B 2 110 ? 30.068 46.131  -15.447 1.00 49.41  ?  110 THR C C   1 
ATOM   3243 O O   . THR B 2 110 ? 30.020 45.020  -14.906 1.00 47.60  ?  110 THR C O   1 
ATOM   3244 C CB  . THR B 2 110 ? 31.316 47.819  -14.063 1.00 47.35  ?  110 THR C CB  1 
ATOM   3245 O OG1 . THR B 2 110 ? 32.239 48.029  -15.138 1.00 50.74  ?  110 THR C OG1 1 
ATOM   3246 C CG2 . THR B 2 110 ? 31.866 46.754  -13.119 1.00 55.14  ?  110 THR C CG2 1 
ATOM   3247 N N   . GLN B 2 111 ? 30.205 46.296  -16.760 1.00 39.71  ?  111 GLN C N   1 
ATOM   3248 C CA  . GLN B 2 111 ? 30.291 45.167  -17.672 1.00 38.06  ?  111 GLN C CA  1 
ATOM   3249 C C   . GLN B 2 111 ? 31.732 44.683  -17.770 1.00 41.18  ?  111 GLN C C   1 
ATOM   3250 O O   . GLN B 2 111 ? 32.645 45.474  -18.021 1.00 39.37  ?  111 GLN C O   1 
ATOM   3251 C CB  . GLN B 2 111 ? 29.763 45.550  -19.057 1.00 40.30  ?  111 GLN C CB  1 
ATOM   3252 C CG  . GLN B 2 111 ? 30.049 44.523  -20.141 1.00 36.03  ?  111 GLN C CG  1 
ATOM   3253 C CD  . GLN B 2 111 ? 29.142 43.307  -20.052 1.00 40.92  ?  111 GLN C CD  1 
ATOM   3254 O OE1 . GLN B 2 111 ? 27.939 43.431  -19.823 1.00 42.34  ?  111 GLN C OE1 1 
ATOM   3255 N NE2 . GLN B 2 111 ? 29.719 42.124  -20.231 1.00 43.09  ?  111 GLN C NE2 1 
ATOM   3256 N N   . VAL B 2 112 ? 31.925 43.386  -17.562 1.00 43.98  ?  112 VAL C N   1 
ATOM   3257 C CA  . VAL B 2 112 ? 33.215 42.731  -17.735 1.00 41.07  ?  112 VAL C CA  1 
ATOM   3258 C C   . VAL B 2 112 ? 33.054 41.704  -18.845 1.00 41.90  ?  112 VAL C C   1 
ATOM   3259 O O   . VAL B 2 112 ? 32.184 40.830  -18.764 1.00 43.24  ?  112 VAL C O   1 
ATOM   3260 C CB  . VAL B 2 112 ? 33.707 42.071  -16.437 1.00 44.36  ?  112 VAL C CB  1 
ATOM   3261 C CG1 . VAL B 2 112 ? 34.964 41.254  -16.698 1.00 42.61  ?  112 VAL C CG1 1 
ATOM   3262 C CG2 . VAL B 2 112 ? 33.961 43.124  -15.368 1.00 42.15  ?  112 VAL C CG2 1 
ATOM   3263 N N   . THR B 2 113 ? 33.876 41.818  -19.883 1.00 43.30  ?  113 THR C N   1 
ATOM   3264 C CA  . THR B 2 113 ? 33.785 40.946  -21.047 1.00 38.76  ?  113 THR C CA  1 
ATOM   3265 C C   . THR B 2 113 ? 35.156 40.356  -21.326 1.00 44.02  ?  113 THR C C   1 
ATOM   3266 O O   . THR B 2 113 ? 36.113 41.094  -21.583 1.00 43.58  ?  113 THR C O   1 
ATOM   3267 C CB  . THR B 2 113 ? 33.265 41.706  -22.269 1.00 45.04  ?  113 THR C CB  1 
ATOM   3268 O OG1 . THR B 2 113 ? 31.936 42.177  -22.010 1.00 44.14  ?  113 THR C OG1 1 
ATOM   3269 C CG2 . THR B 2 113 ? 33.246 40.800  -23.488 1.00 41.84  ?  113 THR C CG2 1 
ATOM   3270 N N   . VAL B 2 114 ? 35.250 39.032  -21.273 1.00 45.06  ?  114 VAL C N   1 
ATOM   3271 C CA  . VAL B 2 114 ? 36.489 38.309  -21.533 1.00 46.84  ?  114 VAL C CA  1 
ATOM   3272 C C   . VAL B 2 114 ? 36.359 37.667  -22.906 1.00 47.39  ?  114 VAL C C   1 
ATOM   3273 O O   . VAL B 2 114 ? 35.620 36.691  -23.078 1.00 47.28  ?  114 VAL C O   1 
ATOM   3274 C CB  . VAL B 2 114 ? 36.779 37.261  -20.451 1.00 46.04  ?  114 VAL C CB  1 
ATOM   3275 C CG1 . VAL B 2 114 ? 38.173 36.690  -20.632 1.00 42.76  ?  114 VAL C CG1 1 
ATOM   3276 C CG2 . VAL B 2 114 ? 36.625 37.874  -19.067 1.00 45.01  ?  114 VAL C CG2 1 
ATOM   3277 N N   . SER B 2 115 ? 37.071 38.217  -23.884 1.00 50.40  ?  115 SER C N   1 
ATOM   3278 C CA  . SER B 2 115 ? 37.015 37.718  -25.251 1.00 53.78  ?  115 SER C CA  1 
ATOM   3279 C C   . SER B 2 115 ? 38.182 38.298  -26.031 1.00 52.56  ?  115 SER C C   1 
ATOM   3280 O O   . SER B 2 115 ? 38.633 39.414  -25.756 1.00 53.65  ?  115 SER C O   1 
ATOM   3281 C CB  . SER B 2 115 ? 35.688 38.086  -25.930 1.00 55.28  ?  115 SER C CB  1 
ATOM   3282 O OG  . SER B 2 115 ? 35.540 37.407  -27.165 1.00 63.37  ?  115 SER C OG  1 
ATOM   3283 N N   . SER B 2 116 ? 38.667 37.526  -26.998 1.00 56.80  ?  116 SER C N   1 
ATOM   3284 C CA  . SER B 2 116 ? 39.679 38.032  -27.913 1.00 59.41  ?  116 SER C CA  1 
ATOM   3285 C C   . SER B 2 116 ? 39.081 39.126  -28.787 1.00 50.70  ?  116 SER C C   1 
ATOM   3286 O O   . SER B 2 116 ? 37.960 38.998  -29.289 1.00 55.56  ?  116 SER C O   1 
ATOM   3287 C CB  . SER B 2 116 ? 40.225 36.899  -28.780 1.00 54.96  ?  116 SER C CB  1 
ATOM   3288 O OG  . SER B 2 116 ? 39.178 36.054  -29.226 1.00 53.32  ?  116 SER C OG  1 
ATOM   3289 N N   . HIS B 2 117 ? 39.826 40.214  -28.959 1.00 55.20  ?  117 HIS C N   1 
ATOM   3290 C CA  . HIS B 2 117 ? 39.350 41.341  -29.751 1.00 62.68  ?  117 HIS C CA  1 
ATOM   3291 C C   . HIS B 2 117 ? 40.545 42.061  -30.364 1.00 62.79  ?  117 HIS C C   1 
ATOM   3292 O O   . HIS B 2 117 ? 41.699 41.661  -30.188 1.00 63.24  ?  117 HIS C O   1 
ATOM   3293 C CB  . HIS B 2 117 ? 38.493 42.296  -28.911 1.00 57.62  ?  117 HIS C CB  1 
ATOM   3294 C CG  . HIS B 2 117 ? 39.175 42.812  -27.680 1.00 62.43  ?  117 HIS C CG  1 
ATOM   3295 N ND1 . HIS B 2 117 ? 39.492 42.005  -26.607 1.00 62.25  ?  117 HIS C ND1 1 
ATOM   3296 C CD2 . HIS B 2 117 ? 39.603 44.054  -27.354 1.00 68.18  ?  117 HIS C CD2 1 
ATOM   3297 C CE1 . HIS B 2 117 ? 40.080 42.731  -25.671 1.00 62.31  ?  117 HIS C CE1 1 
ATOM   3298 N NE2 . HIS B 2 117 ? 40.162 43.977  -26.102 1.00 68.77  ?  117 HIS C NE2 1 
ATOM   3299 N N   . HIS B 2 118 ? 40.252 43.130  -31.097 1.00 67.87  ?  118 HIS C N   1 
ATOM   3300 C CA  . HIS B 2 118 ? 41.276 43.931  -31.757 1.00 70.98  ?  118 HIS C CA  1 
ATOM   3301 C C   . HIS B 2 118 ? 42.204 44.600  -30.747 1.00 67.68  ?  118 HIS C C   1 
ATOM   3302 O O   . HIS B 2 118 ? 42.621 45.741  -30.935 1.00 71.77  ?  118 HIS C O   1 
ATOM   3303 C CB  . HIS B 2 118 ? 40.624 44.988  -32.649 1.00 70.34  ?  118 HIS C CB  1 
ATOM   3304 C CG  . HIS B 2 118 ? 39.588 45.809  -31.946 1.00 75.68  ?  118 HIS C CG  1 
ATOM   3305 N ND1 . HIS B 2 118 ? 39.897 46.946  -31.229 1.00 76.91  ?  118 HIS C ND1 1 
ATOM   3306 C CD2 . HIS B 2 118 ? 38.247 45.653  -31.843 1.00 70.58  ?  118 HIS C CD2 1 
ATOM   3307 C CE1 . HIS B 2 118 ? 38.790 47.456  -30.719 1.00 77.87  ?  118 HIS C CE1 1 
ATOM   3308 N NE2 . HIS B 2 118 ? 37.775 46.691  -31.077 1.00 75.83  ?  118 HIS C NE2 1 
ATOM   3309 N N   . GLN C 2 1   ? 28.972 4.169   58.334  1.00 93.82  ?  1   GLN D N   1 
ATOM   3310 C CA  . GLN C 2 1   ? 27.821 4.947   58.779  1.00 91.67  ?  1   GLN D CA  1 
ATOM   3311 C C   . GLN C 2 1   ? 26.527 4.165   58.575  1.00 92.54  ?  1   GLN D C   1 
ATOM   3312 O O   . GLN C 2 1   ? 25.587 4.287   59.362  1.00 94.60  ?  1   GLN D O   1 
ATOM   3313 C CB  . GLN C 2 1   ? 27.759 6.285   58.035  1.00 87.99  ?  1   GLN D CB  1 
ATOM   3314 C CG  . GLN C 2 1   ? 26.555 7.150   58.386  1.00 91.76  ?  1   GLN D CG  1 
ATOM   3315 C CD  . GLN C 2 1   ? 26.433 7.415   59.876  1.00 98.34  ?  1   GLN D CD  1 
ATOM   3316 O OE1 . GLN C 2 1   ? 27.097 8.298   60.419  1.00 103.95 ?  1   GLN D OE1 1 
ATOM   3317 N NE2 . GLN C 2 1   ? 25.572 6.652   60.545  1.00 90.42  ?  1   GLN D NE2 1 
ATOM   3318 N N   . VAL C 2 2   ? 26.486 3.355   57.520  1.00 90.53  ?  2   VAL D N   1 
ATOM   3319 C CA  . VAL C 2 2   ? 25.309 2.571   57.167  1.00 86.89  ?  2   VAL D CA  1 
ATOM   3320 C C   . VAL C 2 2   ? 25.713 1.105   57.102  1.00 83.11  ?  2   VAL D C   1 
ATOM   3321 O O   . VAL C 2 2   ? 26.708 0.757   56.453  1.00 75.56  ?  2   VAL D O   1 
ATOM   3322 C CB  . VAL C 2 2   ? 24.703 3.032   55.829  1.00 82.05  ?  2   VAL D CB  1 
ATOM   3323 C CG1 . VAL C 2 2   ? 23.688 2.026   55.328  1.00 79.27  ?  2   VAL D CG1 1 
ATOM   3324 C CG2 . VAL C 2 2   ? 24.063 4.401   55.978  1.00 80.41  ?  2   VAL D CG2 1 
ATOM   3325 N N   . GLN C 2 3   ? 24.949 0.249   57.781  1.00 85.29  ?  3   GLN D N   1 
ATOM   3326 C CA  . GLN C 2 3   ? 25.156 -1.192  57.754  1.00 90.57  ?  3   GLN D CA  1 
ATOM   3327 C C   . GLN C 2 3   ? 23.854 -1.873  57.364  1.00 85.08  ?  3   GLN D C   1 
ATOM   3328 O O   . GLN C 2 3   ? 22.775 -1.470  57.813  1.00 83.88  ?  3   GLN D O   1 
ATOM   3329 C CB  . GLN C 2 3   ? 25.643 -1.719  59.110  1.00 91.04  ?  3   GLN D CB  1 
ATOM   3330 C CG  . GLN C 2 3   ? 26.227 -3.121  59.050  1.00 86.83  ?  3   GLN D CG  1 
ATOM   3331 C CD  . GLN C 2 3   ? 27.712 -3.148  59.353  1.00 91.76  ?  3   GLN D CD  1 
ATOM   3332 O OE1 . GLN C 2 3   ? 28.256 -2.207  59.931  1.00 95.90  ?  3   GLN D OE1 1 
ATOM   3333 N NE2 . GLN C 2 3   ? 28.377 -4.227  58.959  1.00 89.65  ?  3   GLN D NE2 1 
ATOM   3334 N N   . LEU C 2 4   ? 23.955 -2.905  56.530  1.00 79.41  ?  4   LEU D N   1 
ATOM   3335 C CA  . LEU C 2 4   ? 22.783 -3.572  55.987  1.00 81.96  ?  4   LEU D CA  1 
ATOM   3336 C C   . LEU C 2 4   ? 22.886 -5.079  56.173  1.00 81.61  ?  4   LEU D C   1 
ATOM   3337 O O   . LEU C 2 4   ? 23.973 -5.636  56.350  1.00 82.19  ?  4   LEU D O   1 
ATOM   3338 C CB  . LEU C 2 4   ? 22.588 -3.249  54.498  1.00 85.58  ?  4   LEU D CB  1 
ATOM   3339 C CG  . LEU C 2 4   ? 23.459 -2.152  53.889  1.00 76.16  ?  4   LEU D CG  1 
ATOM   3340 C CD1 . LEU C 2 4   ? 24.084 -2.618  52.585  1.00 72.29  ?  4   LEU D CD1 1 
ATOM   3341 C CD2 . LEU C 2 4   ? 22.630 -0.907  53.671  1.00 76.43  ?  4   LEU D CD2 1 
ATOM   3342 N N   . GLN C 2 5   ? 21.726 -5.730  56.124  1.00 81.94  ?  5   GLN D N   1 
ATOM   3343 C CA  . GLN C 2 5   ? 21.623 -7.180  56.211  1.00 86.98  ?  5   GLN D CA  1 
ATOM   3344 C C   . GLN C 2 5   ? 20.506 -7.645  55.291  1.00 81.05  ?  5   GLN D C   1 
ATOM   3345 O O   . GLN C 2 5   ? 19.416 -7.065  55.297  1.00 76.26  ?  5   GLN D O   1 
ATOM   3346 C CB  . GLN C 2 5   ? 21.350 -7.638  57.649  1.00 86.13  ?  5   GLN D CB  1 
ATOM   3347 C CG  . GLN C 2 5   ? 22.600 -7.939  58.455  1.00 91.13  ?  5   GLN D CG  1 
ATOM   3348 C CD  . GLN C 2 5   ? 22.284 -8.557  59.804  1.00 89.60  ?  5   GLN D CD  1 
ATOM   3349 O OE1 . GLN C 2 5   ? 21.219 -8.322  60.374  1.00 83.36  ?  5   GLN D OE1 1 
ATOM   3350 N NE2 . GLN C 2 5   ? 23.211 -9.357  60.319  1.00 87.46  ?  5   GLN D NE2 1 
ATOM   3351 N N   . GLU C 2 6   ? 20.774 -8.685  54.509  1.00 78.03  ?  6   GLU D N   1 
ATOM   3352 C CA  . GLU C 2 6   ? 19.799 -9.230  53.577  1.00 81.04  ?  6   GLU D CA  1 
ATOM   3353 C C   . GLU C 2 6   ? 19.105 -10.451 54.171  1.00 81.29  ?  6   GLU D C   1 
ATOM   3354 O O   . GLU C 2 6   ? 19.610 -11.098 55.091  1.00 81.28  ?  6   GLU D O   1 
ATOM   3355 C CB  . GLU C 2 6   ? 20.465 -9.597  52.246  1.00 77.04  ?  6   GLU D CB  1 
ATOM   3356 C CG  . GLU C 2 6   ? 21.710 -10.452 52.390  1.00 80.91  ?  6   GLU D CG  1 
ATOM   3357 C CD  . GLU C 2 6   ? 22.970 -9.623  52.529  1.00 85.66  ?  6   GLU D CD  1 
ATOM   3358 O OE1 . GLU C 2 6   ? 23.127 -8.952  53.571  1.00 83.91  ?  6   GLU D OE1 1 
ATOM   3359 O OE2 . GLU C 2 6   ? 23.800 -9.642  51.596  1.00 83.34  -1 6   GLU D OE2 1 
ATOM   3360 N N   . SER C 2 7   ? 17.929 -10.762 53.622  1.00 79.56  ?  7   SER D N   1 
ATOM   3361 C CA  . SER C 2 7   ? 17.117 -11.876 54.112  1.00 79.19  ?  7   SER D CA  1 
ATOM   3362 C C   . SER C 2 7   ? 16.068 -12.232 53.070  1.00 78.57  ?  7   SER D C   1 
ATOM   3363 O O   . SER C 2 7   ? 15.284 -11.367 52.668  1.00 81.24  ?  7   SER D O   1 
ATOM   3364 C CB  . SER C 2 7   ? 16.449 -11.507 55.438  1.00 76.13  ?  7   SER D CB  1 
ATOM   3365 O OG  . SER C 2 7   ? 15.636 -10.356 55.293  1.00 74.58  ?  7   SER D OG  1 
ATOM   3366 N N   . GLY C 2 8   ? 16.044 -13.494 52.641  1.00 66.56  ?  8   GLY D N   1 
ATOM   3367 C CA  . GLY C 2 8   ? 15.016 -13.943 51.720  1.00 67.01  ?  8   GLY D CA  1 
ATOM   3368 C C   . GLY C 2 8   ? 15.461 -14.975 50.704  1.00 71.23  ?  8   GLY D C   1 
ATOM   3369 O O   . GLY C 2 8   ? 14.681 -15.363 49.829  1.00 69.27  ?  8   GLY D O   1 
ATOM   3370 N N   . GLY C 2 9   ? 16.708 -15.430 50.808  1.00 69.19  ?  9   GLY D N   1 
ATOM   3371 C CA  . GLY C 2 9   ? 17.261 -16.386 49.871  1.00 74.81  ?  9   GLY D CA  1 
ATOM   3372 C C   . GLY C 2 9   ? 16.772 -17.798 50.125  1.00 77.45  ?  9   GLY D C   1 
ATOM   3373 O O   . GLY C 2 9   ? 15.742 -18.026 50.762  1.00 75.40  ?  9   GLY D O   1 
ATOM   3374 N N   . GLY C 2 10  ? 17.522 -18.759 49.610  1.00 79.38  ?  10  GLY D N   1 
ATOM   3375 C CA  . GLY C 2 10  ? 17.231 -20.166 49.812  1.00 85.32  ?  10  GLY D CA  1 
ATOM   3376 C C   . GLY C 2 10  ? 17.013 -20.902 48.508  1.00 86.85  ?  10  GLY D C   1 
ATOM   3377 O O   . GLY C 2 10  ? 17.320 -20.409 47.420  1.00 84.04  ?  10  GLY D O   1 
ATOM   3378 N N   . LEU C 2 11  ? 16.471 -22.112 48.630  1.00 91.33  ?  11  LEU D N   1 
ATOM   3379 C CA  . LEU C 2 11  ? 16.208 -22.964 47.477  1.00 90.82  ?  11  LEU D CA  1 
ATOM   3380 C C   . LEU C 2 11  ? 14.783 -22.752 46.981  1.00 91.62  ?  11  LEU D C   1 
ATOM   3381 O O   . LEU C 2 11  ? 13.857 -22.551 47.772  1.00 82.88  ?  11  LEU D O   1 
ATOM   3382 C CB  . LEU C 2 11  ? 16.423 -24.438 47.837  1.00 90.58  ?  11  LEU D CB  1 
ATOM   3383 C CG  . LEU C 2 11  ? 16.934 -25.403 46.762  1.00 90.68  ?  11  LEU D CG  1 
ATOM   3384 C CD1 . LEU C 2 11  ? 17.542 -26.635 47.409  1.00 95.89  ?  11  LEU D CD1 1 
ATOM   3385 C CD2 . LEU C 2 11  ? 15.826 -25.811 45.799  1.00 91.88  ?  11  LEU D CD2 1 
ATOM   3386 N N   . VAL C 2 12  ? 14.618 -22.781 45.657  1.00 92.86  ?  12  VAL D N   1 
ATOM   3387 C CA  . VAL C 2 12  ? 13.304 -22.706 45.028  1.00 93.15  ?  12  VAL D CA  1 
ATOM   3388 C C   . VAL C 2 12  ? 13.387 -23.406 43.679  1.00 94.94  ?  12  VAL D C   1 
ATOM   3389 O O   . VAL C 2 12  ? 14.469 -23.583 43.112  1.00 91.41  ?  12  VAL D O   1 
ATOM   3390 C CB  . VAL C 2 12  ? 12.812 -21.244 44.872  1.00 92.80  ?  12  VAL D CB  1 
ATOM   3391 C CG1 . VAL C 2 12  ? 13.288 -20.649 43.558  1.00 91.41  ?  12  VAL D CG1 1 
ATOM   3392 C CG2 . VAL C 2 12  ? 11.292 -21.181 44.983  1.00 87.83  ?  12  VAL D CG2 1 
ATOM   3393 N N   . GLN C 2 13  ? 12.230 -23.822 43.170  1.00 96.29  ?  13  GLN D N   1 
ATOM   3394 C CA  . GLN C 2 13  ? 12.184 -24.526 41.902  1.00 97.13  ?  13  GLN D CA  1 
ATOM   3395 C C   . GLN C 2 13  ? 12.221 -23.540 40.735  1.00 91.55  ?  13  GLN D C   1 
ATOM   3396 O O   . GLN C 2 13  ? 11.805 -22.386 40.877  1.00 86.76  ?  13  GLN D O   1 
ATOM   3397 C CB  . GLN C 2 13  ? 10.923 -25.382 41.812  1.00 101.17 ?  13  GLN D CB  1 
ATOM   3398 C CG  . GLN C 2 13  ? 10.838 -26.466 42.877  1.00 105.21 ?  13  GLN D CG  1 
ATOM   3399 C CD  . GLN C 2 13  ? 11.591 -27.724 42.490  1.00 111.73 ?  13  GLN D CD  1 
ATOM   3400 O OE1 . GLN C 2 13  ? 12.204 -27.791 41.424  1.00 114.18 ?  13  GLN D OE1 1 
ATOM   3401 N NE2 . GLN C 2 13  ? 11.553 -28.728 43.358  1.00 111.57 ?  13  GLN D NE2 1 
ATOM   3402 N N   . PRO C 2 14  ? 12.733 -23.965 39.578  1.00 88.11  ?  14  PRO D N   1 
ATOM   3403 C CA  . PRO C 2 14  ? 12.725 -23.086 38.402  1.00 84.43  ?  14  PRO D CA  1 
ATOM   3404 C C   . PRO C 2 14  ? 11.312 -22.640 38.058  1.00 82.09  ?  14  PRO D C   1 
ATOM   3405 O O   . PRO C 2 14  ? 10.357 -23.416 38.134  1.00 80.79  ?  14  PRO D O   1 
ATOM   3406 C CB  . PRO C 2 14  ? 13.328 -23.962 37.300  1.00 82.79  ?  14  PRO D CB  1 
ATOM   3407 C CG  . PRO C 2 14  ? 14.174 -24.948 38.030  1.00 85.10  ?  14  PRO D CG  1 
ATOM   3408 C CD  . PRO C 2 14  ? 13.459 -25.221 39.324  1.00 85.76  ?  14  PRO D CD  1 
ATOM   3409 N N   . GLY C 2 15  ? 11.186 -21.373 37.675  1.00 80.66  ?  15  GLY D N   1 
ATOM   3410 C CA  . GLY C 2 15  ? 9.890  -20.765 37.478  1.00 73.94  ?  15  GLY D CA  1 
ATOM   3411 C C   . GLY C 2 15  ? 9.224  -20.273 38.743  1.00 73.82  ?  15  GLY D C   1 
ATOM   3412 O O   . GLY C 2 15  ? 8.136  -19.688 38.662  1.00 72.55  ?  15  GLY D O   1 
ATOM   3413 N N   . GLY C 2 16  ? 9.837  -20.488 39.906  1.00 79.20  ?  16  GLY D N   1 
ATOM   3414 C CA  . GLY C 2 16  ? 9.287  -20.042 41.168  1.00 75.33  ?  16  GLY D CA  1 
ATOM   3415 C C   . GLY C 2 16  ? 9.510  -18.560 41.396  1.00 72.47  ?  16  GLY D C   1 
ATOM   3416 O O   . GLY C 2 16  ? 9.720  -17.780 40.464  1.00 76.29  ?  16  GLY D O   1 
ATOM   3417 N N   . SER C 2 17  ? 9.467  -18.171 42.669  1.00 72.91  ?  17  SER D N   1 
ATOM   3418 C CA  . SER C 2 17  ? 9.591  -16.767 43.035  1.00 70.53  ?  17  SER D CA  1 
ATOM   3419 C C   . SER C 2 17  ? 10.191 -16.640 44.427  1.00 74.17  ?  17  SER D C   1 
ATOM   3420 O O   . SER C 2 17  ? 9.896  -17.442 45.317  1.00 80.44  ?  17  SER D O   1 
ATOM   3421 C CB  . SER C 2 17  ? 8.233  -16.056 42.983  1.00 67.36  ?  17  SER D CB  1 
ATOM   3422 O OG  . SER C 2 17  ? 7.699  -16.064 41.671  1.00 72.41  ?  17  SER D OG  1 
ATOM   3423 N N   . LEU C 2 18  ? 11.034 -15.622 44.600  1.00 69.69  ?  18  LEU D N   1 
ATOM   3424 C CA  . LEU C 2 18  ? 11.591 -15.262 45.894  1.00 69.24  ?  18  LEU D CA  1 
ATOM   3425 C C   . LEU C 2 18  ? 11.572 -13.747 46.027  1.00 70.42  ?  18  LEU D C   1 
ATOM   3426 O O   . LEU C 2 18  ? 11.690 -13.021 45.037  1.00 67.88  ?  18  LEU D O   1 
ATOM   3427 C CB  . LEU C 2 18  ? 13.027 -15.778 46.072  1.00 70.86  ?  18  LEU D CB  1 
ATOM   3428 C CG  . LEU C 2 18  ? 13.256 -17.287 46.160  1.00 81.18  ?  18  LEU D CG  1 
ATOM   3429 C CD1 . LEU C 2 18  ? 14.743 -17.604 46.062  1.00 78.53  ?  18  LEU D CD1 1 
ATOM   3430 C CD2 . LEU C 2 18  ? 12.673 -17.846 47.449  1.00 78.30  ?  18  LEU D CD2 1 
ATOM   3431 N N   . ARG C 2 19  ? 11.418 -13.274 47.261  1.00 70.39  ?  19  ARG D N   1 
ATOM   3432 C CA  . ARG C 2 19  ? 11.455 -11.848 47.568  1.00 67.41  ?  19  ARG D CA  1 
ATOM   3433 C C   . ARG C 2 19  ? 12.599 -11.600 48.541  1.00 69.68  ?  19  ARG D C   1 
ATOM   3434 O O   . ARG C 2 19  ? 12.565 -12.074 49.682  1.00 67.98  ?  19  ARG D O   1 
ATOM   3435 C CB  . ARG C 2 19  ? 10.129 -11.361 48.148  1.00 67.50  ?  19  ARG D CB  1 
ATOM   3436 C CG  . ARG C 2 19  ? 10.141 -9.882  48.504  1.00 65.12  ?  19  ARG D CG  1 
ATOM   3437 C CD  . ARG C 2 19  ? 8.751  -9.272  48.456  1.00 64.39  ?  19  ARG D CD  1 
ATOM   3438 N NE  . ARG C 2 19  ? 8.515  -8.383  49.587  1.00 77.99  ?  19  ARG D NE  1 
ATOM   3439 C CZ  . ARG C 2 19  ? 7.876  -7.225  49.511  1.00 80.16  ?  19  ARG D CZ  1 
ATOM   3440 N NH1 . ARG C 2 19  ? 7.385  -6.782  48.365  1.00 78.01  ?  19  ARG D NH1 1 
ATOM   3441 N NH2 . ARG C 2 19  ? 7.724  -6.493  50.611  1.00 78.31  ?  19  ARG D NH2 1 
ATOM   3442 N N   . LEU C 2 20  ? 13.607 -10.859 48.093  1.00 66.93  ?  20  LEU D N   1 
ATOM   3443 C CA  . LEU C 2 20  ? 14.764 -10.551 48.922  1.00 64.94  ?  20  LEU D CA  1 
ATOM   3444 C C   . LEU C 2 20  ? 14.561 -9.209  49.612  1.00 70.27  ?  20  LEU D C   1 
ATOM   3445 O O   . LEU C 2 20  ? 14.034 -8.265  49.019  1.00 65.74  ?  20  LEU D O   1 
ATOM   3446 C CB  . LEU C 2 20  ? 16.042 -10.523 48.081  1.00 55.69  ?  20  LEU D CB  1 
ATOM   3447 C CG  . LEU C 2 20  ? 16.354 -11.671 47.112  1.00 63.06  ?  20  LEU D CG  1 
ATOM   3448 C CD1 . LEU C 2 20  ? 17.852 -11.745 46.869  1.00 63.02  ?  20  LEU D CD1 1 
ATOM   3449 C CD2 . LEU C 2 20  ? 15.846 -13.015 47.622  1.00 66.55  ?  20  LEU D CD2 1 
ATOM   3450 N N   . SER C 2 21  ? 14.979 -9.134  50.872  1.00 71.67  ?  21  SER D N   1 
ATOM   3451 C CA  . SER C 2 21  ? 14.879 -7.917  51.661  1.00 72.02  ?  21  SER D CA  1 
ATOM   3452 C C   . SER C 2 21  ? 16.266 -7.483  52.114  1.00 75.61  ?  21  SER D C   1 
ATOM   3453 O O   . SER C 2 21  ? 17.208 -8.279  52.142  1.00 74.73  ?  21  SER D O   1 
ATOM   3454 C CB  . SER C 2 21  ? 13.964 -8.114  52.878  1.00 73.68  ?  21  SER D CB  1 
ATOM   3455 O OG  . SER C 2 21  ? 12.606 -7.913  52.532  1.00 73.46  ?  21  SER D OG  1 
ATOM   3456 N N   . CYS C 2 22  ? 16.385 -6.205  52.461  1.00 74.43  ?  22  CYS D N   1 
ATOM   3457 C CA  . CYS C 2 22  ? 17.641 -5.646  52.945  1.00 75.31  ?  22  CYS D CA  1 
ATOM   3458 C C   . CYS C 2 22  ? 17.317 -4.504  53.894  1.00 76.34  ?  22  CYS D C   1 
ATOM   3459 O O   . CYS C 2 22  ? 16.682 -3.527  53.488  1.00 74.13  ?  22  CYS D O   1 
ATOM   3460 C CB  . CYS C 2 22  ? 18.515 -5.161  51.783  1.00 76.72  ?  22  CYS D CB  1 
ATOM   3461 S SG  . CYS C 2 22  ? 20.103 -4.436  52.273  1.00 79.41  ?  22  CYS D SG  1 
ATOM   3462 N N   . ALA C 2 23  ? 17.746 -4.624  55.147  1.00 79.11  ?  23  ALA D N   1 
ATOM   3463 C CA  . ALA C 2 23  ? 17.421 -3.657  56.189  1.00 78.25  ?  23  ALA D CA  1 
ATOM   3464 C C   . ALA C 2 23  ? 18.597 -2.720  56.422  1.00 77.41  ?  23  ALA D C   1 
ATOM   3465 O O   . ALA C 2 23  ? 19.733 -3.175  56.595  1.00 77.34  ?  23  ALA D O   1 
ATOM   3466 C CB  . ALA C 2 23  ? 17.045 -4.367  57.490  1.00 72.81  ?  23  ALA D CB  1 
ATOM   3467 N N   . ALA C 2 24  ? 18.323 -1.419  56.438  1.00 78.12  ?  24  ALA D N   1 
ATOM   3468 C CA  . ALA C 2 24  ? 19.333 -0.395  56.651  1.00 84.28  ?  24  ALA D CA  1 
ATOM   3469 C C   . ALA C 2 24  ? 19.117 0.294   57.994  1.00 85.64  ?  24  ALA D C   1 
ATOM   3470 O O   . ALA C 2 24  ? 18.020 0.269   58.559  1.00 86.97  ?  24  ALA D O   1 
ATOM   3471 C CB  . ALA C 2 24  ? 19.311 0.643   55.522  1.00 81.73  ?  24  ALA D CB  1 
ATOM   3472 N N   . SER C 2 25  ? 20.182 0.915   58.498  1.00 89.65  ?  25  SER D N   1 
ATOM   3473 C CA  . SER C 2 25  ? 20.131 1.583   59.792  1.00 92.44  ?  25  SER D CA  1 
ATOM   3474 C C   . SER C 2 25  ? 21.296 2.556   59.909  1.00 89.19  ?  25  SER D C   1 
ATOM   3475 O O   . SER C 2 25  ? 22.403 2.265   59.447  1.00 94.12  ?  25  SER D O   1 
ATOM   3476 C CB  . SER C 2 25  ? 20.174 0.569   60.941  1.00 86.66  ?  25  SER D CB  1 
ATOM   3477 O OG  . SER C 2 25  ? 21.396 -0.150  60.939  1.00 88.83  ?  25  SER D OG  1 
ATOM   3478 N N   . GLY C 2 26  ? 21.037 3.705   60.531  1.00 84.24  ?  26  GLY D N   1 
ATOM   3479 C CA  . GLY C 2 26  ? 22.079 4.675   60.808  1.00 81.97  ?  26  GLY D CA  1 
ATOM   3480 C C   . GLY C 2 26  ? 22.306 5.687   59.705  1.00 88.17  ?  26  GLY D C   1 
ATOM   3481 O O   . GLY C 2 26  ? 23.039 5.417   58.751  1.00 89.00  ?  26  GLY D O   1 
ATOM   3482 N N   . ASP C 2 27  ? 21.685 6.862   59.834  1.00 85.82  ?  27  ASP D N   1 
ATOM   3483 C CA  . ASP C 2 27  ? 21.816 7.949   58.861  1.00 89.06  ?  27  ASP D CA  1 
ATOM   3484 C C   . ASP C 2 27  ? 21.431 7.484   57.455  1.00 85.77  ?  27  ASP D C   1 
ATOM   3485 O O   . ASP C 2 27  ? 22.134 7.739   56.474  1.00 80.53  ?  27  ASP D O   1 
ATOM   3486 C CB  . ASP C 2 27  ? 23.228 8.544   58.880  1.00 86.32  ?  27  ASP D CB  1 
ATOM   3487 C CG  . ASP C 2 27  ? 23.294 9.920   58.236  1.00 85.98  ?  27  ASP D CG  1 
ATOM   3488 O OD1 . ASP C 2 27  ? 22.276 10.646  58.265  1.00 86.12  -1 27  ASP D OD1 1 
ATOM   3489 O OD2 . ASP C 2 27  ? 24.365 10.277  57.699  1.00 80.07  ?  27  ASP D OD2 1 
ATOM   3490 N N   . ILE C 2 28  ? 20.297 6.785   57.366  1.00 85.57  ?  28  ILE D N   1 
ATOM   3491 C CA  . ILE C 2 28  ? 19.748 6.407   56.069  1.00 81.10  ?  28  ILE D CA  1 
ATOM   3492 C C   . ILE C 2 28  ? 19.274 7.613   55.274  1.00 83.42  ?  28  ILE D C   1 
ATOM   3493 O O   . ILE C 2 28  ? 18.996 7.488   54.076  1.00 84.33  ?  28  ILE D O   1 
ATOM   3494 C CB  . ILE C 2 28  ? 18.597 5.396   56.245  1.00 84.42  ?  28  ILE D CB  1 
ATOM   3495 C CG1 . ILE C 2 28  ? 17.455 6.023   57.049  1.00 79.97  ?  28  ILE D CG1 1 
ATOM   3496 C CG2 . ILE C 2 28  ? 19.106 4.124   56.912  1.00 80.69  ?  28  ILE D CG2 1 
ATOM   3497 C CD1 . ILE C 2 28  ? 16.510 5.014   57.670  1.00 81.99  ?  28  ILE D CD1 1 
ATOM   3498 N N   . PHE C 2 29  ? 19.174 8.778   55.921  1.00 83.23  ?  29  PHE D N   1 
ATOM   3499 C CA  . PHE C 2 29  ? 18.914 10.029  55.219  1.00 82.80  ?  29  PHE D CA  1 
ATOM   3500 C C   . PHE C 2 29  ? 19.992 10.340  54.186  1.00 77.55  ?  29  PHE D C   1 
ATOM   3501 O O   . PHE C 2 29  ? 19.736 11.100  53.245  1.00 78.68  ?  29  PHE D O   1 
ATOM   3502 C CB  . PHE C 2 29  ? 18.805 11.167  56.238  1.00 81.53  ?  29  PHE D CB  1 
ATOM   3503 C CG  . PHE C 2 29  ? 18.347 12.474  55.656  1.00 79.45  ?  29  PHE D CG  1 
ATOM   3504 C CD1 . PHE C 2 29  ? 17.002 12.713  55.423  1.00 79.27  ?  29  PHE D CD1 1 
ATOM   3505 C CD2 . PHE C 2 29  ? 19.259 13.474  55.360  1.00 75.88  ?  29  PHE D CD2 1 
ATOM   3506 C CE1 . PHE C 2 29  ? 16.577 13.920  54.895  1.00 72.80  ?  29  PHE D CE1 1 
ATOM   3507 C CE2 . PHE C 2 29  ? 18.842 14.681  54.834  1.00 71.77  ?  29  PHE D CE2 1 
ATOM   3508 C CZ  . PHE C 2 29  ? 17.500 14.903  54.600  1.00 71.82  ?  29  PHE D CZ  1 
ATOM   3509 N N   . SER C 2 30  ? 21.189 9.765   54.339  1.00 76.52  ?  30  SER D N   1 
ATOM   3510 C CA  . SER C 2 30  ? 22.277 9.973   53.393  1.00 75.46  ?  30  SER D CA  1 
ATOM   3511 C C   . SER C 2 30  ? 22.204 9.043   52.189  1.00 72.53  ?  30  SER D C   1 
ATOM   3512 O O   . SER C 2 30  ? 22.808 9.349   51.154  1.00 63.58  ?  30  SER D O   1 
ATOM   3513 C CB  . SER C 2 30  ? 23.624 9.786   54.095  1.00 71.63  ?  30  SER D CB  1 
ATOM   3514 O OG  . SER C 2 30  ? 23.888 8.413   54.330  1.00 67.54  ?  30  SER D OG  1 
ATOM   3515 N N   . ILE C 2 31  ? 21.492 7.922   52.300  1.00 71.84  ?  31  ILE D N   1 
ATOM   3516 C CA  . ILE C 2 31  ? 21.412 6.960   51.206  1.00 62.77  ?  31  ILE D CA  1 
ATOM   3517 C C   . ILE C 2 31  ? 20.661 7.581   50.037  1.00 61.55  ?  31  ILE D C   1 
ATOM   3518 O O   . ILE C 2 31  ? 19.563 8.130   50.206  1.00 62.61  ?  31  ILE D O   1 
ATOM   3519 C CB  . ILE C 2 31  ? 20.730 5.668   51.678  1.00 66.73  ?  31  ILE D CB  1 
ATOM   3520 C CG1 . ILE C 2 31  ? 21.675 4.854   52.565  1.00 68.73  ?  31  ILE D CG1 1 
ATOM   3521 C CG2 . ILE C 2 31  ? 20.267 4.840   50.490  1.00 64.34  ?  31  ILE D CG2 1 
ATOM   3522 C CD1 . ILE C 2 31  ? 21.043 3.601   53.136  1.00 69.22  ?  31  ILE D CD1 1 
ATOM   3523 N N   . TYR C 2 32  ? 21.248 7.501   48.839  1.00 58.18  ?  32  TYR D N   1 
ATOM   3524 C CA  . TYR C 2 32  ? 20.584 7.993   47.641  1.00 58.81  ?  32  TYR D CA  1 
ATOM   3525 C C   . TYR C 2 32  ? 20.603 7.015   46.471  1.00 55.48  ?  32  TYR D C   1 
ATOM   3526 O O   . TYR C 2 32  ? 20.052 7.337   45.414  1.00 56.54  ?  32  TYR D O   1 
ATOM   3527 C CB  . TYR C 2 32  ? 21.188 9.335   47.195  1.00 53.49  ?  32  TYR D CB  1 
ATOM   3528 C CG  . TYR C 2 32  ? 22.691 9.346   47.028  1.00 55.39  ?  32  TYR D CG  1 
ATOM   3529 C CD1 . TYR C 2 32  ? 23.273 9.026   45.807  1.00 49.76  ?  32  TYR D CD1 1 
ATOM   3530 C CD2 . TYR C 2 32  ? 23.527 9.711   48.077  1.00 52.35  ?  32  TYR D CD2 1 
ATOM   3531 C CE1 . TYR C 2 32  ? 24.643 9.043   45.642  1.00 49.97  ?  32  TYR D CE1 1 
ATOM   3532 C CE2 . TYR C 2 32  ? 24.903 9.735   47.920  1.00 53.16  ?  32  TYR D CE2 1 
ATOM   3533 C CZ  . TYR C 2 32  ? 25.453 9.400   46.698  1.00 53.28  ?  32  TYR D CZ  1 
ATOM   3534 O OH  . TYR C 2 32  ? 26.818 9.421   46.527  1.00 47.96  ?  32  TYR D OH  1 
ATOM   3535 N N   . LEU C 2 33  ? 21.211 5.840   46.624  1.00 54.70  ?  33  LEU D N   1 
ATOM   3536 C CA  . LEU C 2 33  ? 21.135 4.796   45.603  1.00 58.47  ?  33  LEU D CA  1 
ATOM   3537 C C   . LEU C 2 33  ? 21.118 3.443   46.293  1.00 56.68  ?  33  LEU D C   1 
ATOM   3538 O O   . LEU C 2 33  ? 22.034 3.124   47.057  1.00 54.30  ?  33  LEU D O   1 
ATOM   3539 C CB  . LEU C 2 33  ? 22.302 4.881   44.617  1.00 54.07  ?  33  LEU D CB  1 
ATOM   3540 C CG  . LEU C 2 33  ? 22.168 3.986   43.378  1.00 54.45  ?  33  LEU D CG  1 
ATOM   3541 C CD1 . LEU C 2 33  ? 21.191 4.594   42.384  1.00 47.20  ?  33  LEU D CD1 1 
ATOM   3542 C CD2 . LEU C 2 33  ? 23.516 3.732   42.716  1.00 42.62  ?  33  LEU D CD2 1 
ATOM   3543 N N   . MET C 2 34  ? 20.083 2.656   46.021  1.00 54.41  ?  34  MET D N   1 
ATOM   3544 C CA  . MET C 2 34  ? 19.912 1.333   46.604  1.00 55.41  ?  34  MET D CA  1 
ATOM   3545 C C   . MET C 2 34  ? 19.899 0.301   45.486  1.00 55.24  ?  34  MET D C   1 
ATOM   3546 O O   . MET C 2 34  ? 19.157 0.452   44.511  1.00 47.46  ?  34  MET D O   1 
ATOM   3547 C CB  . MET C 2 34  ? 18.619 1.258   47.416  1.00 54.99  ?  34  MET D CB  1 
ATOM   3548 C CG  . MET C 2 34  ? 18.597 2.196   48.607  1.00 53.91  ?  34  MET D CG  1 
ATOM   3549 S SD  . MET C 2 34  ? 16.947 2.826   48.967  1.00 58.67  ?  34  MET D SD  1 
ATOM   3550 C CE  . MET C 2 34  ? 16.853 4.231   47.857  1.00 55.99  ?  34  MET D CE  1 
ATOM   3551 N N   . GLY C 2 35  ? 20.715 -0.746  45.629  1.00 53.60  ?  35  GLY D N   1 
ATOM   3552 C CA  . GLY C 2 35  ? 20.897 -1.697  44.556  1.00 52.94  ?  35  GLY D CA  1 
ATOM   3553 C C   . GLY C 2 35  ? 21.006 -3.123  45.057  1.00 56.49  ?  35  GLY D C   1 
ATOM   3554 O O   . GLY C 2 35  ? 21.157 -3.383  46.253  1.00 52.07  ?  35  GLY D O   1 
ATOM   3555 N N   . TRP C 2 36  ? 20.923 -4.049  44.103  1.00 52.50  ?  36  TRP D N   1 
ATOM   3556 C CA  . TRP C 2 36  ? 21.106 -5.472  44.342  1.00 48.15  ?  36  TRP D CA  1 
ATOM   3557 C C   . TRP C 2 36  ? 22.182 -5.996  43.402  1.00 53.56  ?  36  TRP D C   1 
ATOM   3558 O O   . TRP C 2 36  ? 22.227 -5.621  42.228  1.00 57.50  ?  36  TRP D O   1 
ATOM   3559 C CB  . TRP C 2 36  ? 19.804 -6.259  44.126  1.00 48.28  ?  36  TRP D CB  1 
ATOM   3560 C CG  . TRP C 2 36  ? 18.753 -6.012  45.164  1.00 54.92  ?  36  TRP D CG  1 
ATOM   3561 C CD1 . TRP C 2 36  ? 17.716 -5.129  45.086  1.00 57.82  ?  36  TRP D CD1 1 
ATOM   3562 C CD2 . TRP C 2 36  ? 18.630 -6.666  46.435  1.00 55.14  ?  36  TRP D CD2 1 
ATOM   3563 N NE1 . TRP C 2 36  ? 16.958 -5.187  46.229  1.00 55.46  ?  36  TRP D NE1 1 
ATOM   3564 C CE2 . TRP C 2 36  ? 17.496 -6.123  47.074  1.00 59.42  ?  36  TRP D CE2 1 
ATOM   3565 C CE3 . TRP C 2 36  ? 19.367 -7.653  47.094  1.00 61.21  ?  36  TRP D CE3 1 
ATOM   3566 C CZ2 . TRP C 2 36  ? 17.083 -6.536  48.339  1.00 61.55  ?  36  TRP D CZ2 1 
ATOM   3567 C CZ3 . TRP C 2 36  ? 18.955 -8.063  48.351  1.00 60.16  ?  36  TRP D CZ3 1 
ATOM   3568 C CH2 . TRP C 2 36  ? 17.825 -7.503  48.959  1.00 61.39  ?  36  TRP D CH2 1 
ATOM   3569 N N   . TYR C 2 37  ? 23.057 -6.845  43.929  1.00 53.68  ?  37  TYR D N   1 
ATOM   3570 C CA  . TYR C 2 37  ? 24.091 -7.495  43.141  1.00 56.16  ?  37  TYR D CA  1 
ATOM   3571 C C   . TYR C 2 37  ? 24.001 -8.997  43.369  1.00 64.34  ?  37  TYR D C   1 
ATOM   3572 O O   . TYR C 2 37  ? 23.414 -9.461  44.348  1.00 65.22  ?  37  TYR D O   1 
ATOM   3573 C CB  . TYR C 2 37  ? 25.499 -6.992  43.505  1.00 60.12  ?  37  TYR D CB  1 
ATOM   3574 C CG  . TYR C 2 37  ? 25.802 -5.559  43.106  1.00 58.16  ?  37  TYR D CG  1 
ATOM   3575 C CD1 . TYR C 2 37  ? 25.072 -4.497  43.627  1.00 60.11  ?  37  TYR D CD1 1 
ATOM   3576 C CD2 . TYR C 2 37  ? 26.828 -5.270  42.214  1.00 60.38  ?  37  TYR D CD2 1 
ATOM   3577 C CE1 . TYR C 2 37  ? 25.350 -3.191  43.267  1.00 61.44  ?  37  TYR D CE1 1 
ATOM   3578 C CE2 . TYR C 2 37  ? 27.112 -3.965  41.848  1.00 58.57  ?  37  TYR D CE2 1 
ATOM   3579 C CZ  . TYR C 2 37  ? 26.370 -2.931  42.378  1.00 60.09  ?  37  TYR D CZ  1 
ATOM   3580 O OH  . TYR C 2 37  ? 26.648 -1.631  42.019  1.00 60.39  ?  37  TYR D OH  1 
ATOM   3581 N N   . ARG C 2 38  ? 24.589 -9.762  42.450  1.00 64.97  ?  38  ARG D N   1 
ATOM   3582 C CA  . ARG C 2 38  ? 24.639 -11.210 42.596  1.00 66.11  ?  38  ARG D CA  1 
ATOM   3583 C C   . ARG C 2 38  ? 25.999 -11.722 42.150  1.00 73.40  ?  38  ARG D C   1 
ATOM   3584 O O   . ARG C 2 38  ? 26.642 -11.140 41.273  1.00 69.43  ?  38  ARG D O   1 
ATOM   3585 C CB  . ARG C 2 38  ? 23.519 -11.911 41.810  1.00 65.46  ?  38  ARG D CB  1 
ATOM   3586 C CG  . ARG C 2 38  ? 23.706 -11.959 40.304  1.00 62.62  ?  38  ARG D CG  1 
ATOM   3587 C CD  . ARG C 2 38  ? 22.357 -12.109 39.624  1.00 61.91  ?  38  ARG D CD  1 
ATOM   3588 N NE  . ARG C 2 38  ? 22.459 -12.199 38.173  1.00 64.31  ?  38  ARG D NE  1 
ATOM   3589 C CZ  . ARG C 2 38  ? 21.482 -12.619 37.381  1.00 64.77  ?  38  ARG D CZ  1 
ATOM   3590 N NH1 . ARG C 2 38  ? 20.313 -13.002 37.869  1.00 62.08  ?  38  ARG D NH1 1 
ATOM   3591 N NH2 . ARG C 2 38  ? 21.681 -12.654 36.067  1.00 68.14  ?  38  ARG D NH2 1 
ATOM   3592 N N   . GLN C 2 39  ? 26.433 -12.817 42.772  1.00 79.41  ?  39  GLN D N   1 
ATOM   3593 C CA  . GLN C 2 39  ? 27.731 -13.433 42.496  1.00 85.15  ?  39  GLN D CA  1 
ATOM   3594 C C   . GLN C 2 39  ? 27.501 -14.861 42.010  1.00 88.95  ?  39  GLN D C   1 
ATOM   3595 O O   . GLN C 2 39  ? 27.380 -15.793 42.811  1.00 84.11  ?  39  GLN D O   1 
ATOM   3596 C CB  . GLN C 2 39  ? 28.633 -13.407 43.732  1.00 86.95  ?  39  GLN D CB  1 
ATOM   3597 C CG  . GLN C 2 39  ? 29.920 -12.589 43.578  1.00 96.82  ?  39  GLN D CG  1 
ATOM   3598 C CD  . GLN C 2 39  ? 30.960 -13.229 42.659  1.00 95.41  ?  39  GLN D CD  1 
ATOM   3599 O OE1 . GLN C 2 39  ? 30.638 -14.042 41.793  1.00 97.76  ?  39  GLN D OE1 1 
ATOM   3600 N NE2 . GLN C 2 39  ? 32.217 -12.853 42.851  1.00 87.22  ?  39  GLN D NE2 1 
ATOM   3601 N N   . SER C 2 40  ? 27.443 -15.023 40.693  1.00 98.39  ?  40  SER D N   1 
ATOM   3602 C CA  . SER C 2 40  ? 27.335 -16.346 40.107  1.00 103.16 ?  40  SER D CA  1 
ATOM   3603 C C   . SER C 2 40  ? 28.666 -17.088 40.241  1.00 111.06 ?  40  SER D C   1 
ATOM   3604 O O   . SER C 2 40  ? 29.727 -16.463 40.318  1.00 111.62 ?  40  SER D O   1 
ATOM   3605 C CB  . SER C 2 40  ? 26.936 -16.239 38.636  1.00 99.39  ?  40  SER D CB  1 
ATOM   3606 O OG  . SER C 2 40  ? 25.540 -16.034 38.501  1.00 88.16  ?  40  SER D OG  1 
ATOM   3607 N N   . PRO C 2 41  ? 28.639 -18.421 40.279  1.00 115.09 ?  41  PRO D N   1 
ATOM   3608 C CA  . PRO C 2 41  ? 29.895 -19.172 40.422  1.00 115.96 ?  41  PRO D CA  1 
ATOM   3609 C C   . PRO C 2 41  ? 30.728 -19.088 39.150  1.00 117.74 ?  41  PRO D C   1 
ATOM   3610 O O   . PRO C 2 41  ? 30.228 -19.308 38.045  1.00 117.23 ?  41  PRO D O   1 
ATOM   3611 C CB  . PRO C 2 41  ? 29.437 -20.609 40.706  1.00 114.90 ?  41  PRO D CB  1 
ATOM   3612 C CG  . PRO C 2 41  ? 27.943 -20.610 40.653  1.00 113.06 ?  41  PRO D CG  1 
ATOM   3613 C CD  . PRO C 2 41  ? 27.465 -19.299 40.138  1.00 112.08 ?  41  PRO D CD  1 
ATOM   3614 N N   . GLY C 2 42  ? 32.011 -18.762 39.318  1.00 115.02 ?  42  GLY D N   1 
ATOM   3615 C CA  . GLY C 2 42  ? 32.928 -18.635 38.207  1.00 114.68 ?  42  GLY D CA  1 
ATOM   3616 C C   . GLY C 2 42  ? 32.960 -17.272 37.551  1.00 116.13 ?  42  GLY D C   1 
ATOM   3617 O O   . GLY C 2 42  ? 33.880 -17.003 36.768  1.00 116.88 ?  42  GLY D O   1 
ATOM   3618 N N   . LYS C 2 43  ? 31.993 -16.407 37.838  1.00 116.26 ?  43  LYS D N   1 
ATOM   3619 C CA  . LYS C 2 43  ? 31.922 -15.073 37.261  1.00 109.98 ?  43  LYS D CA  1 
ATOM   3620 C C   . LYS C 2 43  ? 32.159 -14.022 38.337  1.00 107.99 ?  43  LYS D C   1 
ATOM   3621 O O   . LYS C 2 43  ? 32.206 -14.317 39.534  1.00 105.87 ?  43  LYS D O   1 
ATOM   3622 C CB  . LYS C 2 43  ? 30.566 -14.850 36.578  1.00 104.45 ?  43  LYS D CB  1 
ATOM   3623 C CG  . LYS C 2 43  ? 30.394 -15.594 35.259  1.00 104.34 ?  43  LYS D CG  1 
ATOM   3624 C CD  . LYS C 2 43  ? 31.722 -15.780 34.539  1.00 105.01 ?  43  LYS D CD  1 
ATOM   3625 C CE  . LYS C 2 43  ? 31.559 -16.627 33.288  1.00 99.31  ?  43  LYS D CE  1 
ATOM   3626 N NZ  . LYS C 2 43  ? 30.996 -15.839 32.157  1.00 91.19  ?  43  LYS D NZ  1 
ATOM   3627 N N   . GLN C 2 44  ? 32.314 -12.777 37.893  1.00 106.02 ?  44  GLN D N   1 
ATOM   3628 C CA  . GLN C 2 44  ? 32.528 -11.671 38.810  1.00 98.95  ?  44  GLN D CA  1 
ATOM   3629 C C   . GLN C 2 44  ? 31.195 -11.154 39.346  1.00 91.70  ?  44  GLN D C   1 
ATOM   3630 O O   . GLN C 2 44  ? 30.116 -11.506 38.862  1.00 91.00  ?  44  GLN D O   1 
ATOM   3631 C CB  . GLN C 2 44  ? 33.294 -10.542 38.121  1.00 100.53 ?  44  GLN D CB  1 
ATOM   3632 C CG  . GLN C 2 44  ? 34.618 -10.967 37.511  1.00 106.03 ?  44  GLN D CG  1 
ATOM   3633 C CD  . GLN C 2 44  ? 35.165 -9.939  36.538  1.00 112.61 ?  44  GLN D CD  1 
ATOM   3634 O OE1 . GLN C 2 44  ? 35.990 -9.101  36.900  1.00 116.27 ?  44  GLN D OE1 1 
ATOM   3635 N NE2 . GLN C 2 44  ? 34.702 -9.998  35.294  1.00 110.73 ?  44  GLN D NE2 1 
ATOM   3636 N N   . ARG C 2 45  ? 31.281 -10.304 40.367  1.00 85.50  ?  45  ARG D N   1 
ATOM   3637 C CA  . ARG C 2 45  ? 30.093 -9.681  40.936  1.00 84.05  ?  45  ARG D CA  1 
ATOM   3638 C C   . ARG C 2 45  ? 29.477 -8.726  39.921  1.00 79.95  ?  45  ARG D C   1 
ATOM   3639 O O   . ARG C 2 45  ? 30.118 -7.757  39.500  1.00 83.16  ?  45  ARG D O   1 
ATOM   3640 C CB  . ARG C 2 45  ? 30.451 -8.939  42.223  1.00 83.71  ?  45  ARG D CB  1 
ATOM   3641 C CG  . ARG C 2 45  ? 29.379 -8.999  43.301  1.00 75.09  ?  45  ARG D CG  1 
ATOM   3642 C CD  . ARG C 2 45  ? 29.833 -8.286  44.565  1.00 80.66  ?  45  ARG D CD  1 
ATOM   3643 N NE  . ARG C 2 45  ? 30.583 -9.167  45.452  1.00 86.79  ?  45  ARG D NE  1 
ATOM   3644 C CZ  . ARG C 2 45  ? 31.118 -8.790  46.606  1.00 83.74  ?  45  ARG D CZ  1 
ATOM   3645 N NH1 . ARG C 2 45  ? 31.008 -7.545  47.044  1.00 81.56  ?  45  ARG D NH1 1 
ATOM   3646 N NH2 . ARG C 2 45  ? 31.781 -9.681  47.336  1.00 83.94  ?  45  ARG D NH2 1 
ATOM   3647 N N   . GLU C 2 46  ? 28.238 -8.998  39.524  1.00 71.46  ?  46  GLU D N   1 
ATOM   3648 C CA  . GLU C 2 46  ? 27.533 -8.180  38.550  1.00 70.21  ?  46  GLU D CA  1 
ATOM   3649 C C   . GLU C 2 46  ? 26.311 -7.535  39.190  1.00 69.42  ?  46  GLU D C   1 
ATOM   3650 O O   . GLU C 2 46  ? 25.785 -8.009  40.202  1.00 62.68  ?  46  GLU D O   1 
ATOM   3651 C CB  . GLU C 2 46  ? 27.112 -9.001  37.324  1.00 67.87  ?  46  GLU D CB  1 
ATOM   3652 C CG  . GLU C 2 46  ? 26.520 -10.361 37.651  1.00 79.15  ?  46  GLU D CG  1 
ATOM   3653 C CD  . GLU C 2 46  ? 25.535 -10.833 36.599  1.00 76.00  ?  46  GLU D CD  1 
ATOM   3654 O OE1 . GLU C 2 46  ? 25.578 -10.313 35.465  1.00 80.91  ?  46  GLU D OE1 1 
ATOM   3655 O OE2 . GLU C 2 46  ? 24.717 -11.727 36.907  1.00 76.67  -1 46  GLU D OE2 1 
ATOM   3656 N N   . LEU C 2 47  ? 25.865 -6.442  38.580  1.00 65.75  ?  47  LEU D N   1 
ATOM   3657 C CA  . LEU C 2 47  ? 24.726 -5.692  39.081  1.00 56.39  ?  47  LEU D CA  1 
ATOM   3658 C C   . LEU C 2 47  ? 23.418 -6.357  38.667  1.00 53.85  ?  47  LEU D C   1 
ATOM   3659 O O   . LEU C 2 47  ? 23.328 -6.992  37.611  1.00 59.90  ?  47  LEU D O   1 
ATOM   3660 C CB  . LEU C 2 47  ? 24.780 -4.251  38.565  1.00 53.48  ?  47  LEU D CB  1 
ATOM   3661 C CG  . LEU C 2 47  ? 23.513 -3.397  38.633  1.00 51.34  ?  47  LEU D CG  1 
ATOM   3662 C CD1 . LEU C 2 47  ? 23.433 -2.724  39.984  1.00 54.81  ?  47  LEU D CD1 1 
ATOM   3663 C CD2 . LEU C 2 47  ? 23.483 -2.369  37.513  1.00 56.08  ?  47  LEU D CD2 1 
ATOM   3664 N N   . VAL C 2 48  ? 22.404 -6.222  39.520  1.00 47.98  ?  48  VAL D N   1 
ATOM   3665 C CA  . VAL C 2 48  ? 21.060 -6.726  39.244  1.00 50.67  ?  48  VAL D CA  1 
ATOM   3666 C C   . VAL C 2 48  ? 20.088 -5.582  38.978  1.00 47.27  ?  48  VAL D C   1 
ATOM   3667 O O   . VAL C 2 48  ? 19.449 -5.529  37.925  1.00 47.65  ?  48  VAL D O   1 
ATOM   3668 C CB  . VAL C 2 48  ? 20.556 -7.630  40.392  1.00 47.67  ?  48  VAL D CB  1 
ATOM   3669 C CG1 . VAL C 2 48  ? 19.111 -8.047  40.148  1.00 48.73  ?  48  VAL D CG1 1 
ATOM   3670 C CG2 . VAL C 2 48  ? 21.453 -8.841  40.546  1.00 51.37  ?  48  VAL D CG2 1 
ATOM   3671 N N   . ALA C 2 49  ? 19.960 -4.654  39.924  1.00 44.20  ?  49  ALA D N   1 
ATOM   3672 C CA  . ALA C 2 49  ? 19.035 -3.539  39.786  1.00 43.60  ?  49  ALA D CA  1 
ATOM   3673 C C   . ALA C 2 49  ? 19.411 -2.455  40.784  1.00 46.45  ?  49  ALA D C   1 
ATOM   3674 O O   . ALA C 2 49  ? 19.996 -2.738  41.831  1.00 49.21  ?  49  ALA D O   1 
ATOM   3675 C CB  . ALA C 2 49  ? 17.584 -3.983  40.003  1.00 41.94  ?  49  ALA D CB  1 
ATOM   3676 N N   . THR C 2 50  ? 19.073 -1.210  40.442  1.00 44.33  ?  50  THR D N   1 
ATOM   3677 C CA  . THR C 2 50  ? 19.272 -0.068  41.322  1.00 42.58  ?  50  THR D CA  1 
ATOM   3678 C C   . THR C 2 50  ? 17.992 0.751   41.398  1.00 43.32  ?  50  THR D C   1 
ATOM   3679 O O   . THR C 2 50  ? 17.088 0.614   40.571  1.00 46.49  ?  50  THR D O   1 
ATOM   3680 C CB  . THR C 2 50  ? 20.416 0.848   40.854  1.00 43.50  ?  50  THR D CB  1 
ATOM   3681 O OG1 . THR C 2 50  ? 20.228 1.198   39.477  1.00 44.70  ?  50  THR D OG1 1 
ATOM   3682 C CG2 . THR C 2 50  ? 21.760 0.174   41.033  1.00 43.53  ?  50  THR D CG2 1 
ATOM   3683 N N   . ILE C 2 51  ? 17.936 1.617   42.407  1.00 42.62  ?  51  ILE D N   1 
ATOM   3684 C CA  . ILE C 2 51  ? 16.835 2.561   42.570  1.00 46.95  ?  51  ILE D CA  1 
ATOM   3685 C C   . ILE C 2 51  ? 17.345 3.751   43.371  1.00 50.33  ?  51  ILE D C   1 
ATOM   3686 O O   . ILE C 2 51  ? 18.107 3.591   44.329  1.00 49.94  ?  51  ILE D O   1 
ATOM   3687 C CB  . ILE C 2 51  ? 15.610 1.895   43.240  1.00 45.70  ?  51  ILE D CB  1 
ATOM   3688 C CG1 . ILE C 2 51  ? 14.434 2.873   43.305  1.00 49.48  ?  51  ILE D CG1 1 
ATOM   3689 C CG2 . ILE C 2 51  ? 15.961 1.367   44.627  1.00 49.88  ?  51  ILE D CG2 1 
ATOM   3690 C CD1 . ILE C 2 51  ? 13.104 2.204   43.579  1.00 51.10  ?  51  ILE D CD1 1 
ATOM   3691 N N   . THR C 2 52  ? 16.943 4.951   42.957  1.00 51.45  ?  52  THR D N   1 
ATOM   3692 C CA  . THR C 2 52  ? 17.355 6.173   43.627  1.00 54.73  ?  52  THR D CA  1 
ATOM   3693 C C   . THR C 2 52  ? 16.322 6.572   44.682  1.00 58.28  ?  52  THR D C   1 
ATOM   3694 O O   . THR C 2 52  ? 15.270 5.945   44.830  1.00 54.03  ?  52  THR D O   1 
ATOM   3695 C CB  . THR C 2 52  ? 17.557 7.300   42.614  1.00 48.07  ?  52  THR D CB  1 
ATOM   3696 O OG1 . THR C 2 52  ? 16.289 7.691   42.072  1.00 51.37  ?  52  THR D OG1 1 
ATOM   3697 C CG2 . THR C 2 52  ? 18.462 6.845   41.481  1.00 52.32  ?  52  THR D CG2 1 
ATOM   3698 N N   . SER C 2 53  ? 16.629 7.635   45.429  1.00 59.41  ?  53  SER D N   1 
ATOM   3699 C CA  . SER C 2 53  ? 15.672 8.158   46.398  1.00 57.16  ?  53  SER D CA  1 
ATOM   3700 C C   . SER C 2 53  ? 14.413 8.663   45.706  1.00 60.66  ?  53  SER D C   1 
ATOM   3701 O O   . SER C 2 53  ? 13.303 8.519   46.234  1.00 68.88  ?  53  SER D O   1 
ATOM   3702 C CB  . SER C 2 53  ? 16.312 9.273   47.224  1.00 58.65  ?  53  SER D CB  1 
ATOM   3703 O OG  . SER C 2 53  ? 17.554 8.861   47.764  1.00 55.97  ?  53  SER D OG  1 
ATOM   3704 N N   . SER C 2 54  ? 14.566 9.254   44.519  1.00 61.13  ?  54  SER D N   1 
ATOM   3705 C CA  . SER C 2 54  ? 13.425 9.730   43.747  1.00 60.47  ?  54  SER D CA  1 
ATOM   3706 C C   . SER C 2 54  ? 12.630 8.598   43.107  1.00 65.00  ?  54  SER D C   1 
ATOM   3707 O O   . SER C 2 54  ? 11.556 8.857   42.556  1.00 67.51  ?  54  SER D O   1 
ATOM   3708 C CB  . SER C 2 54  ? 13.897 10.702  42.664  1.00 63.84  ?  54  SER D CB  1 
ATOM   3709 O OG  . SER C 2 54  ? 15.181 10.344  42.182  1.00 68.86  ?  54  SER D OG  1 
ATOM   3710 N N   . GLY C 2 55  ? 13.125 7.365   43.162  1.00 62.12  ?  55  GLY D N   1 
ATOM   3711 C CA  . GLY C 2 55  ? 12.438 6.234   42.577  1.00 61.80  ?  55  GLY D CA  1 
ATOM   3712 C C   . GLY C 2 55  ? 12.897 5.832   41.193  1.00 60.57  ?  55  GLY D C   1 
ATOM   3713 O O   . GLY C 2 55  ? 12.247 4.983   40.570  1.00 59.68  ?  55  GLY D O   1 
ATOM   3714 N N   . GLU C 2 56  ? 13.990 6.405   40.694  1.00 58.72  ?  56  GLU D N   1 
ATOM   3715 C CA  . GLU C 2 56  ? 14.485 6.079   39.364  1.00 53.19  ?  56  GLU D CA  1 
ATOM   3716 C C   . GLU C 2 56  ? 15.141 4.701   39.382  1.00 48.88  ?  56  GLU D C   1 
ATOM   3717 O O   . GLU C 2 56  ? 16.133 4.489   40.088  1.00 47.62  ?  56  GLU D O   1 
ATOM   3718 C CB  . GLU C 2 56  ? 15.472 7.146   38.900  1.00 54.71  ?  56  GLU D CB  1 
ATOM   3719 C CG  . GLU C 2 56  ? 15.787 7.115   37.415  1.00 61.01  ?  56  GLU D CG  1 
ATOM   3720 C CD  . GLU C 2 56  ? 16.914 8.058   37.040  1.00 66.14  ?  56  GLU D CD  1 
ATOM   3721 O OE1 . GLU C 2 56  ? 16.893 9.224   37.490  1.00 65.14  ?  56  GLU D OE1 1 
ATOM   3722 O OE2 . GLU C 2 56  ? 17.817 7.636   36.286  1.00 61.47  -1 56  GLU D OE2 1 
ATOM   3723 N N   . THR C 2 57  ? 14.594 3.769   38.606  1.00 42.99  ?  57  THR D N   1 
ATOM   3724 C CA  . THR C 2 57  ? 15.021 2.377   38.638  1.00 49.12  ?  57  THR D CA  1 
ATOM   3725 C C   . THR C 2 57  ? 15.826 2.020   37.393  1.00 47.78  ?  57  THR D C   1 
ATOM   3726 O O   . THR C 2 57  ? 15.667 2.624   36.329  1.00 46.30  ?  57  THR D O   1 
ATOM   3727 C CB  . THR C 2 57  ? 13.822 1.426   38.737  1.00 47.98  ?  57  THR D CB  1 
ATOM   3728 O OG1 . THR C 2 57  ? 12.992 1.574   37.579  1.00 44.09  ?  57  THR D OG1 1 
ATOM   3729 C CG2 . THR C 2 57  ? 13.005 1.727   39.980  1.00 47.22  ?  57  THR D CG2 1 
ATOM   3730 N N   . LYS C 2 58  ? 16.691 1.021   37.552  1.00 45.48  ?  58  LYS D N   1 
ATOM   3731 C CA  . LYS C 2 58  ? 17.397 0.398   36.442  1.00 45.57  ?  58  LYS D CA  1 
ATOM   3732 C C   . LYS C 2 58  ? 17.523 -1.088  36.732  1.00 48.10  ?  58  LYS D C   1 
ATOM   3733 O O   . LYS C 2 58  ? 17.954 -1.471  37.822  1.00 44.97  ?  58  LYS D O   1 
ATOM   3734 C CB  . LYS C 2 58  ? 18.787 1.008   36.233  1.00 44.43  ?  58  LYS D CB  1 
ATOM   3735 C CG  . LYS C 2 58  ? 19.771 0.056   35.567  1.00 46.22  ?  58  LYS D CG  1 
ATOM   3736 C CD  . LYS C 2 58  ? 20.963 0.783   34.972  1.00 47.27  ?  58  LYS D CD  1 
ATOM   3737 C CE  . LYS C 2 58  ? 21.863 -0.183  34.213  1.00 48.42  ?  58  LYS D CE  1 
ATOM   3738 N NZ  . LYS C 2 58  ? 22.218 0.320   32.857  1.00 48.25  ?  58  LYS D NZ  1 
ATOM   3739 N N   . HIS C 2 59  ? 17.130 -1.918  35.770  1.00 50.03  ?  59  HIS D N   1 
ATOM   3740 C CA  . HIS C 2 59  ? 17.320 -3.357  35.845  1.00 47.83  ?  59  HIS D CA  1 
ATOM   3741 C C   . HIS C 2 59  ? 18.260 -3.788  34.727  1.00 44.98  ?  59  HIS D C   1 
ATOM   3742 O O   . HIS C 2 59  ? 18.383 -3.115  33.701  1.00 45.18  ?  59  HIS D O   1 
ATOM   3743 C CB  . HIS C 2 59  ? 15.985 -4.107  35.730  1.00 42.18  ?  59  HIS D CB  1 
ATOM   3744 C CG  . HIS C 2 59  ? 15.001 -3.755  36.803  1.00 48.08  ?  59  HIS D CG  1 
ATOM   3745 N ND1 . HIS C 2 59  ? 14.136 -2.687  36.697  1.00 48.61  ?  59  HIS D ND1 1 
ATOM   3746 C CD2 . HIS C 2 59  ? 14.738 -4.334  38.000  1.00 45.84  ?  59  HIS D CD2 1 
ATOM   3747 C CE1 . HIS C 2 59  ? 13.386 -2.619  37.783  1.00 48.61  ?  59  HIS D CE1 1 
ATOM   3748 N NE2 . HIS C 2 59  ? 13.732 -3.607  38.590  1.00 50.21  ?  59  HIS D NE2 1 
ATOM   3749 N N   . VAL C 2 60  ? 18.940 -4.911  34.934  1.00 44.76  ?  60  VAL D N   1 
ATOM   3750 C CA  . VAL C 2 60  ? 19.816 -5.431  33.893  1.00 44.56  ?  60  VAL D CA  1 
ATOM   3751 C C   . VAL C 2 60  ? 18.999 -6.242  32.892  1.00 48.35  ?  60  VAL D C   1 
ATOM   3752 O O   . VAL C 2 60  ? 17.916 -6.752  33.198  1.00 44.90  ?  60  VAL D O   1 
ATOM   3753 C CB  . VAL C 2 60  ? 20.969 -6.261  34.483  1.00 48.96  ?  60  VAL D CB  1 
ATOM   3754 C CG1 . VAL C 2 60  ? 21.849 -5.380  35.353  1.00 48.98  ?  60  VAL D CG1 1 
ATOM   3755 C CG2 . VAL C 2 60  ? 20.430 -7.443  35.272  1.00 42.80  ?  60  VAL D CG2 1 
ATOM   3756 N N   . TYR C 2 61  ? 19.536 -6.357  31.674  1.00 47.56  ?  61  TYR D N   1 
ATOM   3757 C CA  . TYR C 2 61  ? 18.788 -6.966  30.576  1.00 48.32  ?  61  TYR D CA  1 
ATOM   3758 C C   . TYR C 2 61  ? 18.367 -8.393  30.903  1.00 47.70  ?  61  TYR D C   1 
ATOM   3759 O O   . TYR C 2 61  ? 17.265 -8.822  30.542  1.00 48.13  ?  61  TYR D O   1 
ATOM   3760 C CB  . TYR C 2 61  ? 19.621 -6.931  29.294  1.00 45.13  ?  61  TYR D CB  1 
ATOM   3761 C CG  . TYR C 2 61  ? 19.818 -5.542  28.729  1.00 49.12  ?  61  TYR D CG  1 
ATOM   3762 C CD1 . TYR C 2 61  ? 18.735 -4.697  28.511  1.00 46.78  ?  61  TYR D CD1 1 
ATOM   3763 C CD2 . TYR C 2 61  ? 21.087 -5.070  28.415  1.00 43.60  ?  61  TYR D CD2 1 
ATOM   3764 C CE1 . TYR C 2 61  ? 18.910 -3.426  27.996  1.00 45.38  ?  61  TYR D CE1 1 
ATOM   3765 C CE2 . TYR C 2 61  ? 21.273 -3.800  27.899  1.00 47.36  ?  61  TYR D CE2 1 
ATOM   3766 C CZ  . TYR C 2 61  ? 20.182 -2.982  27.692  1.00 45.52  ?  61  TYR D CZ  1 
ATOM   3767 O OH  . TYR C 2 61  ? 20.362 -1.716  27.179  1.00 47.39  ?  61  TYR D OH  1 
ATOM   3768 N N   . SER C 2 62  ? 19.225 -9.143  31.599  1.00 49.55  ?  62  SER D N   1 
ATOM   3769 C CA  . SER C 2 62  ? 18.941 -10.547 31.870  1.00 56.53  ?  62  SER D CA  1 
ATOM   3770 C C   . SER C 2 62  ? 17.753 -10.745 32.804  1.00 56.29  ?  62  SER D C   1 
ATOM   3771 O O   . SER C 2 62  ? 17.197 -11.849 32.846  1.00 56.74  ?  62  SER D O   1 
ATOM   3772 C CB  . SER C 2 62  ? 20.179 -11.229 32.458  1.00 55.07  ?  62  SER D CB  1 
ATOM   3773 O OG  . SER C 2 62  ? 20.393 -10.827 33.800  1.00 55.68  ?  62  SER D OG  1 
ATOM   3774 N N   . VAL C 2 63  ? 17.346 -9.715  33.548  1.00 49.90  ?  63  VAL D N   1 
ATOM   3775 C CA  . VAL C 2 63  ? 16.264 -9.830  34.517  1.00 50.36  ?  63  VAL D CA  1 
ATOM   3776 C C   . VAL C 2 63  ? 15.087 -8.920  34.185  1.00 49.08  ?  63  VAL D C   1 
ATOM   3777 O O   . VAL C 2 63  ? 14.157 -8.802  34.985  1.00 50.21  ?  63  VAL D O   1 
ATOM   3778 C CB  . VAL C 2 63  ? 16.768 -9.572  35.952  1.00 56.83  ?  63  VAL D CB  1 
ATOM   3779 C CG1 . VAL C 2 63  ? 18.071 -10.317 36.204  1.00 59.55  ?  63  VAL D CG1 1 
ATOM   3780 C CG2 . VAL C 2 63  ? 16.954 -8.078  36.196  1.00 51.84  ?  63  VAL D CG2 1 
ATOM   3781 N N   . LYS C 2 64  ? 15.102 -8.282  33.016  1.00 49.19  ?  64  LYS D N   1 
ATOM   3782 C CA  . LYS C 2 64  ? 14.022 -7.377  32.635  1.00 50.33  ?  64  LYS D CA  1 
ATOM   3783 C C   . LYS C 2 64  ? 12.688 -8.112  32.582  1.00 51.79  ?  64  LYS D C   1 
ATOM   3784 O O   . LYS C 2 64  ? 12.570 -9.170  31.956  1.00 54.12  ?  64  LYS D O   1 
ATOM   3785 C CB  . LYS C 2 64  ? 14.323 -6.745  31.276  1.00 54.64  ?  64  LYS D CB  1 
ATOM   3786 C CG  . LYS C 2 64  ? 15.523 -5.817  31.262  1.00 53.76  ?  64  LYS D CG  1 
ATOM   3787 C CD  . LYS C 2 64  ? 15.119 -4.389  30.938  1.00 53.33  ?  64  LYS D CD  1 
ATOM   3788 C CE  . LYS C 2 64  ? 16.285 -3.433  31.115  1.00 52.19  ?  64  LYS D CE  1 
ATOM   3789 N NZ  . LYS C 2 64  ? 16.370 -2.938  32.515  1.00 58.33  ?  64  LYS D NZ  1 
ATOM   3790 N N   . GLY C 2 65  ? 11.678 -7.539  33.235  1.00 56.10  ?  65  GLY D N   1 
ATOM   3791 C CA  . GLY C 2 65  ? 10.359 -8.128  33.288  1.00 59.06  ?  65  GLY D CA  1 
ATOM   3792 C C   . GLY C 2 65  ? 10.176 -9.209  34.328  1.00 60.90  ?  65  GLY D C   1 
ATOM   3793 O O   . GLY C 2 65  ? 9.035  -9.487  34.718  1.00 63.20  ?  65  GLY D O   1 
ATOM   3794 N N   . ARG C 2 66  ? 11.257 -9.835  34.791  1.00 59.39  ?  66  ARG D N   1 
ATOM   3795 C CA  . ARG C 2 66  ? 11.192 -10.867 35.818  1.00 56.60  ?  66  ARG D CA  1 
ATOM   3796 C C   . ARG C 2 66  ? 11.469 -10.329 37.215  1.00 60.81  ?  66  ARG D C   1 
ATOM   3797 O O   . ARG C 2 66  ? 10.771 -10.699 38.164  1.00 58.16  ?  66  ARG D O   1 
ATOM   3798 C CB  . ARG C 2 66  ? 12.183 -11.992 35.502  1.00 57.26  ?  66  ARG D CB  1 
ATOM   3799 C CG  . ARG C 2 66  ? 12.241 -12.385 34.033  1.00 56.49  ?  66  ARG D CG  1 
ATOM   3800 C CD  . ARG C 2 66  ? 12.902 -13.743 33.850  1.00 55.59  ?  66  ARG D CD  1 
ATOM   3801 N NE  . ARG C 2 66  ? 14.358 -13.656 33.899  1.00 59.41  ?  66  ARG D NE  1 
ATOM   3802 C CZ  . ARG C 2 66  ? 15.111 -14.208 34.842  1.00 59.75  ?  66  ARG D CZ  1 
ATOM   3803 N NH1 . ARG C 2 66  ? 14.578 -14.899 35.835  1.00 64.47  ?  66  ARG D NH1 1 
ATOM   3804 N NH2 . ARG C 2 66  ? 16.432 -14.062 34.785  1.00 55.68  ?  66  ARG D NH2 1 
ATOM   3805 N N   . PHE C 2 67  ? 12.469 -9.467  37.362  1.00 60.22  ?  67  PHE D N   1 
ATOM   3806 C CA  . PHE C 2 67  ? 12.845 -8.905  38.648  1.00 55.75  ?  67  PHE D CA  1 
ATOM   3807 C C   . PHE C 2 67  ? 12.299 -7.487  38.777  1.00 54.60  ?  67  PHE D C   1 
ATOM   3808 O O   . PHE C 2 67  ? 12.050 -6.797  37.786  1.00 57.15  ?  67  PHE D O   1 
ATOM   3809 C CB  . PHE C 2 67  ? 14.369 -8.895  38.823  1.00 57.49  ?  67  PHE D CB  1 
ATOM   3810 C CG  . PHE C 2 67  ? 14.991 -10.266 38.968  1.00 59.08  ?  67  PHE D CG  1 
ATOM   3811 C CD1 . PHE C 2 67  ? 14.283 -11.418 38.661  1.00 62.71  ?  67  PHE D CD1 1 
ATOM   3812 C CD2 . PHE C 2 67  ? 16.300 -10.394 39.406  1.00 60.23  ?  67  PHE D CD2 1 
ATOM   3813 C CE1 . PHE C 2 67  ? 14.864 -12.667 38.791  1.00 61.94  ?  67  PHE D CE1 1 
ATOM   3814 C CE2 . PHE C 2 67  ? 16.887 -11.639 39.537  1.00 63.16  ?  67  PHE D CE2 1 
ATOM   3815 C CZ  . PHE C 2 67  ? 16.167 -12.776 39.228  1.00 64.27  ?  67  PHE D CZ  1 
ATOM   3816 N N   . THR C 2 68  ? 12.115 -7.053  40.023  1.00 57.65  ?  68  THR D N   1 
ATOM   3817 C CA  . THR C 2 68  ? 11.609 -5.714  40.298  1.00 53.75  ?  68  THR D CA  1 
ATOM   3818 C C   . THR C 2 68  ? 12.208 -5.218  41.604  1.00 58.28  ?  68  THR D C   1 
ATOM   3819 O O   . THR C 2 68  ? 12.164 -5.926  42.616  1.00 55.98  ?  68  THR D O   1 
ATOM   3820 C CB  . THR C 2 68  ? 10.078 -5.700  40.380  1.00 56.02  ?  68  THR D CB  1 
ATOM   3821 O OG1 . THR C 2 68  ? 9.525  -6.176  39.147  1.00 59.57  ?  68  THR D OG1 1 
ATOM   3822 C CG2 . THR C 2 68  ? 9.569  -4.291  40.646  1.00 54.84  ?  68  THR D CG2 1 
ATOM   3823 N N   . ILE C 2 69  ? 12.764 -4.010  41.578  1.00 55.63  ?  69  ILE D N   1 
ATOM   3824 C CA  . ILE C 2 69  ? 13.328 -3.380  42.765  1.00 50.83  ?  69  ILE D CA  1 
ATOM   3825 C C   . ILE C 2 69  ? 12.311 -2.402  43.332  1.00 54.13  ?  69  ILE D C   1 
ATOM   3826 O O   . ILE C 2 69  ? 11.550 -1.768  42.588  1.00 57.34  ?  69  ILE D O   1 
ATOM   3827 C CB  . ILE C 2 69  ? 14.669 -2.684  42.452  1.00 51.60  ?  69  ILE D CB  1 
ATOM   3828 C CG1 . ILE C 2 69  ? 15.384 -2.282  43.747  1.00 42.79  ?  69  ILE D CG1 1 
ATOM   3829 C CG2 . ILE C 2 69  ? 14.462 -1.474  41.550  1.00 45.76  ?  69  ILE D CG2 1 
ATOM   3830 C CD1 . ILE C 2 69  ? 16.881 -2.123  43.598  1.00 44.80  ?  69  ILE D CD1 1 
ATOM   3831 N N   . SER C 2 70  ? 12.276 -2.299  44.659  1.00 57.00  ?  70  SER D N   1 
ATOM   3832 C CA  . SER C 2 70  ? 11.389 -1.376  45.349  1.00 58.30  ?  70  SER D CA  1 
ATOM   3833 C C   . SER C 2 70  ? 12.042 -0.984  46.664  1.00 59.62  ?  70  SER D C   1 
ATOM   3834 O O   . SER C 2 70  ? 12.861 -1.724  47.211  1.00 62.16  ?  70  SER D O   1 
ATOM   3835 C CB  . SER C 2 70  ? 10.006 -1.990  45.593  1.00 58.54  ?  70  SER D CB  1 
ATOM   3836 O OG  . SER C 2 70  ? 9.147  -1.766  44.487  1.00 63.02  ?  70  SER D OG  1 
ATOM   3837 N N   . ARG C 2 71  ? 11.673 0.191   47.168  1.00 62.99  ?  71  ARG D N   1 
ATOM   3838 C CA  . ARG C 2 71  ? 12.245 0.708   48.403  1.00 68.06  ?  71  ARG D CA  1 
ATOM   3839 C C   . ARG C 2 71  ? 11.182 1.449   49.197  1.00 72.84  ?  71  ARG D C   1 
ATOM   3840 O O   . ARG C 2 71  ? 10.225 1.989   48.635  1.00 70.38  ?  71  ARG D O   1 
ATOM   3841 C CB  . ARG C 2 71  ? 13.439 1.635   48.123  1.00 64.95  ?  71  ARG D CB  1 
ATOM   3842 C CG  . ARG C 2 71  ? 13.127 2.814   47.208  1.00 66.08  ?  71  ARG D CG  1 
ATOM   3843 C CD  . ARG C 2 71  ? 12.844 4.094   47.995  1.00 70.10  ?  71  ARG D CD  1 
ATOM   3844 N NE  . ARG C 2 71  ? 12.117 5.104   47.233  1.00 71.85  ?  71  ARG D NE  1 
ATOM   3845 C CZ  . ARG C 2 71  ? 10.895 4.955   46.734  1.00 69.33  ?  71  ARG D CZ  1 
ATOM   3846 N NH1 . ARG C 2 71  ? 10.204 3.839   46.905  1.00 66.26  ?  71  ARG D NH1 1 
ATOM   3847 N NH2 . ARG C 2 71  ? 10.347 5.958   46.053  1.00 68.39  ?  71  ARG D NH2 1 
ATOM   3848 N N   . GLU C 2 72  ? 11.360 1.467   50.515  1.00 76.00  ?  72  GLU D N   1 
ATOM   3849 C CA  . GLU C 2 72  ? 10.513 2.269   51.382  1.00 77.39  ?  72  GLU D CA  1 
ATOM   3850 C C   . GLU C 2 72  ? 10.939 3.731   51.319  1.00 75.35  ?  72  GLU D C   1 
ATOM   3851 O O   . GLU C 2 72  ? 12.115 4.049   51.122  1.00 73.90  ?  72  GLU D O   1 
ATOM   3852 C CB  . GLU C 2 72  ? 10.585 1.765   52.825  1.00 78.45  ?  72  GLU D CB  1 
ATOM   3853 C CG  . GLU C 2 72  ? 10.208 0.301   52.995  1.00 78.65  ?  72  GLU D CG  1 
ATOM   3854 C CD  . GLU C 2 72  ? 8.708  0.078   52.991  1.00 80.62  ?  72  GLU D CD  1 
ATOM   3855 O OE1 . GLU C 2 72  ? 7.957  1.072   53.101  1.00 81.76  ?  72  GLU D OE1 1 
ATOM   3856 O OE2 . GLU C 2 72  ? 8.279  -1.089  52.878  1.00 74.69  -1 72  GLU D OE2 1 
ATOM   3857 N N   . ASN C 2 73  ? 9.962  4.625   51.490  1.00 77.62  ?  73  ASN D N   1 
ATOM   3858 C CA  . ASN C 2 73  ? 10.235 6.055   51.390  1.00 78.44  ?  73  ASN D CA  1 
ATOM   3859 C C   . ASN C 2 73  ? 11.234 6.532   52.438  1.00 76.94  ?  73  ASN D C   1 
ATOM   3860 O O   . ASN C 2 73  ? 11.895 7.555   52.226  1.00 80.80  ?  73  ASN D O   1 
ATOM   3861 C CB  . ASN C 2 73  ? 8.932  6.846   51.508  1.00 77.80  ?  73  ASN D CB  1 
ATOM   3862 C CG  . ASN C 2 73  ? 8.248  7.043   50.168  1.00 82.92  ?  73  ASN D CG  1 
ATOM   3863 O OD1 . ASN C 2 73  ? 8.889  7.389   49.175  1.00 84.15  ?  73  ASN D OD1 1 
ATOM   3864 N ND2 . ASN C 2 73  ? 6.939  6.822   50.133  1.00 82.52  ?  73  ASN D ND2 1 
ATOM   3865 N N   . ALA C 2 74  ? 11.362 5.820   53.556  1.00 81.71  ?  74  ALA D N   1 
ATOM   3866 C CA  . ALA C 2 74  ? 12.318 6.164   54.598  1.00 80.69  ?  74  ALA D CA  1 
ATOM   3867 C C   . ALA C 2 74  ? 13.700 5.572   54.357  1.00 81.14  ?  74  ALA D C   1 
ATOM   3868 O O   . ALA C 2 74  ? 14.609 5.815   55.158  1.00 81.01  ?  74  ALA D O   1 
ATOM   3869 C CB  . ALA C 2 74  ? 11.796 5.712   55.964  1.00 80.07  ?  74  ALA D CB  1 
ATOM   3870 N N   . LYS C 2 75  ? 13.875 4.799   53.283  1.00 80.61  ?  75  LYS D N   1 
ATOM   3871 C CA  . LYS C 2 75  ? 15.148 4.179   52.909  1.00 79.29  ?  75  LYS D CA  1 
ATOM   3872 C C   . LYS C 2 75  ? 15.696 3.258   53.994  1.00 79.49  ?  75  LYS D C   1 
ATOM   3873 O O   . LYS C 2 75  ? 16.898 2.968   54.017  1.00 78.60  ?  75  LYS D O   1 
ATOM   3874 C CB  . LYS C 2 75  ? 16.195 5.236   52.536  1.00 76.89  ?  75  LYS D CB  1 
ATOM   3875 C CG  . LYS C 2 75  ? 15.866 6.009   51.272  1.00 74.32  ?  75  LYS D CG  1 
ATOM   3876 C CD  . LYS C 2 75  ? 16.462 7.404   51.310  1.00 73.92  ?  75  LYS D CD  1 
ATOM   3877 C CE  . LYS C 2 75  ? 15.537 8.413   50.655  1.00 68.55  ?  75  LYS D CE  1 
ATOM   3878 N NZ  . LYS C 2 75  ? 16.127 9.780   50.641  1.00 73.86  ?  75  LYS D NZ  1 
ATOM   3879 N N   . ASN C 2 76  ? 14.841 2.786   54.900  1.00 82.85  ?  76  ASN D N   1 
ATOM   3880 C CA  . ASN C 2 76  ? 15.260 1.801   55.887  1.00 80.72  ?  76  ASN D CA  1 
ATOM   3881 C C   . ASN C 2 76  ? 15.293 0.387   55.324  1.00 80.56  ?  76  ASN D C   1 
ATOM   3882 O O   . ASN C 2 76  ? 15.869 -0.501  55.962  1.00 79.97  ?  76  ASN D O   1 
ATOM   3883 C CB  . ASN C 2 76  ? 14.336 1.845   57.109  1.00 82.82  ?  76  ASN D CB  1 
ATOM   3884 C CG  . ASN C 2 76  ? 12.889 1.543   56.762  1.00 82.61  ?  76  ASN D CG  1 
ATOM   3885 O OD1 . ASN C 2 76  ? 12.343 2.085   55.801  1.00 82.84  ?  76  ASN D OD1 1 
ATOM   3886 N ND2 . ASN C 2 76  ? 12.263 0.673   57.545  1.00 81.67  ?  76  ASN D ND2 1 
ATOM   3887 N N   . ALA C 2 77  ? 14.701 0.164   54.152  1.00 78.28  ?  77  ALA D N   1 
ATOM   3888 C CA  . ALA C 2 77  ? 14.681 -1.155  53.537  1.00 73.48  ?  77  ALA D CA  1 
ATOM   3889 C C   . ALA C 2 77  ? 14.326 -1.025  52.065  1.00 69.49  ?  77  ALA D C   1 
ATOM   3890 O O   . ALA C 2 77  ? 13.546 -0.153  51.673  1.00 65.64  ?  77  ALA D O   1 
ATOM   3891 C CB  . ALA C 2 77  ? 13.688 -2.090  54.237  1.00 71.80  ?  77  ALA D CB  1 
ATOM   3892 N N   . TRP C 2 78  ? 14.910 -1.905  51.255  1.00 65.59  ?  78  TRP D N   1 
ATOM   3893 C CA  . TRP C 2 78  ? 14.531 -2.052  49.859  1.00 67.90  ?  78  TRP D CA  1 
ATOM   3894 C C   . TRP C 2 78  ? 14.507 -3.533  49.513  1.00 66.17  ?  78  TRP D C   1 
ATOM   3895 O O   . TRP C 2 78  ? 15.207 -4.341  50.129  1.00 67.22  ?  78  TRP D O   1 
ATOM   3896 C CB  . TRP C 2 78  ? 15.472 -1.287  48.916  1.00 54.81  ?  78  TRP D CB  1 
ATOM   3897 C CG  . TRP C 2 78  ? 16.913 -1.652  49.036  1.00 53.90  ?  78  TRP D CG  1 
ATOM   3898 C CD1 . TRP C 2 78  ? 17.587 -2.580  48.298  1.00 55.18  ?  78  TRP D CD1 1 
ATOM   3899 C CD2 . TRP C 2 78  ? 17.868 -1.084  49.937  1.00 60.94  ?  78  TRP D CD2 1 
ATOM   3900 N NE1 . TRP C 2 78  ? 18.904 -2.628  48.688  1.00 55.23  ?  78  TRP D NE1 1 
ATOM   3901 C CE2 . TRP C 2 78  ? 19.101 -1.719  49.694  1.00 60.74  ?  78  TRP D CE2 1 
ATOM   3902 C CE3 . TRP C 2 78  ? 17.796 -0.105  50.933  1.00 59.39  ?  78  TRP D CE3 1 
ATOM   3903 C CZ2 . TRP C 2 78  ? 20.253 -1.405  50.409  1.00 58.66  ?  78  TRP D CZ2 1 
ATOM   3904 C CZ3 . TRP C 2 78  ? 18.943 0.209   51.636  1.00 61.29  ?  78  TRP D CZ3 1 
ATOM   3905 C CH2 . TRP C 2 78  ? 20.154 -0.440  51.371  1.00 57.62  ?  78  TRP D CH2 1 
ATOM   3906 N N   . TYR C 2 79  ? 13.689 -3.883  48.525  1.00 63.13  ?  79  TYR D N   1 
ATOM   3907 C CA  . TYR C 2 79  ? 13.387 -5.273  48.220  1.00 66.71  ?  79  TYR D CA  1 
ATOM   3908 C C   . TYR C 2 79  ? 13.725 -5.596  46.770  1.00 61.15  ?  79  TYR D C   1 
ATOM   3909 O O   . TYR C 2 79  ? 14.053 -4.720  45.966  1.00 59.67  ?  79  TYR D O   1 
ATOM   3910 C CB  . TYR C 2 79  ? 11.911 -5.581  48.501  1.00 66.74  ?  79  TYR D CB  1 
ATOM   3911 C CG  . TYR C 2 79  ? 11.369 -4.878  49.726  1.00 72.29  ?  79  TYR D CG  1 
ATOM   3912 C CD1 . TYR C 2 79  ? 11.615 -5.373  51.000  1.00 75.28  ?  79  TYR D CD1 1 
ATOM   3913 C CD2 . TYR C 2 79  ? 10.616 -3.717  49.609  1.00 74.38  ?  79  TYR D CD2 1 
ATOM   3914 C CE1 . TYR C 2 79  ? 11.125 -4.734  52.124  1.00 68.50  ?  79  TYR D CE1 1 
ATOM   3915 C CE2 . TYR C 2 79  ? 10.121 -3.071  50.727  1.00 72.54  ?  79  TYR D CE2 1 
ATOM   3916 C CZ  . TYR C 2 79  ? 10.378 -3.584  51.982  1.00 72.88  ?  79  TYR D CZ  1 
ATOM   3917 O OH  . TYR C 2 79  ? 9.890  -2.946  53.099  1.00 72.14  ?  79  TYR D OH  1 
ATOM   3918 N N   . LEU C 2 80  ? 13.643 -6.888  46.447  1.00 62.45  ?  80  LEU D N   1 
ATOM   3919 C CA  . LEU C 2 80  ? 13.877 -7.386  45.092  1.00 59.40  ?  80  LEU D CA  1 
ATOM   3920 C C   . LEU C 2 80  ? 12.903 -8.534  44.849  1.00 62.47  ?  80  LEU D C   1 
ATOM   3921 O O   . LEU C 2 80  ? 13.128 -9.658  45.311  1.00 63.58  ?  80  LEU D O   1 
ATOM   3922 C CB  . LEU C 2 80  ? 15.321 -7.837  44.902  1.00 54.43  ?  80  LEU D CB  1 
ATOM   3923 C CG  . LEU C 2 80  ? 15.640 -8.458  43.539  1.00 56.98  ?  80  LEU D CG  1 
ATOM   3924 C CD1 . LEU C 2 80  ? 15.521 -7.419  42.431  1.00 51.40  ?  80  LEU D CD1 1 
ATOM   3925 C CD2 . LEU C 2 80  ? 17.023 -9.089  43.543  1.00 59.61  ?  80  LEU D CD2 1 
ATOM   3926 N N   . GLN C 2 81  ? 11.821 -8.249  44.128  1.00 59.74  ?  81  GLN D N   1 
ATOM   3927 C CA  . GLN C 2 81  ? 10.833 -9.265  43.786  1.00 60.30  ?  81  GLN D CA  1 
ATOM   3928 C C   . GLN C 2 81  ? 11.328 -10.041 42.571  1.00 61.03  ?  81  GLN D C   1 
ATOM   3929 O O   . GLN C 2 81  ? 11.310 -9.528  41.448  1.00 58.27  ?  81  GLN D O   1 
ATOM   3930 C CB  . GLN C 2 81  ? 9.477  -8.623  43.509  1.00 61.38  ?  81  GLN D CB  1 
ATOM   3931 C CG  . GLN C 2 81  ? 8.327  -9.611  43.363  1.00 68.18  ?  81  GLN D CG  1 
ATOM   3932 C CD  . GLN C 2 81  ? 8.346  -10.699 44.421  1.00 66.98  ?  81  GLN D CD  1 
ATOM   3933 O OE1 . GLN C 2 81  ? 7.901  -10.492 45.549  1.00 65.52  ?  81  GLN D OE1 1 
ATOM   3934 N NE2 . GLN C 2 81  ? 8.846  -11.875 44.053  1.00 61.44  ?  81  GLN D NE2 1 
ATOM   3935 N N   . MET C 2 82  ? 11.771 -11.275 42.792  1.00 62.37  ?  82  MET D N   1 
ATOM   3936 C CA  . MET C 2 82  ? 12.258 -12.141 41.727  1.00 62.79  ?  82  MET D CA  1 
ATOM   3937 C C   . MET C 2 82  ? 11.145 -13.095 41.311  1.00 64.91  ?  82  MET D C   1 
ATOM   3938 O O   . MET C 2 82  ? 10.684 -13.905 42.123  1.00 63.11  ?  82  MET D O   1 
ATOM   3939 C CB  . MET C 2 82  ? 13.494 -12.918 42.179  1.00 62.77  ?  82  MET D CB  1 
ATOM   3940 C CG  . MET C 2 82  ? 14.562 -12.070 42.845  1.00 61.39  ?  82  MET D CG  1 
ATOM   3941 S SD  . MET C 2 82  ? 15.713 -13.056 43.824  1.00 75.56  ?  82  MET D SD  1 
ATOM   3942 C CE  . MET C 2 82  ? 16.693 -13.826 42.538  1.00 56.29  ?  82  MET D CE  1 
ATOM   3943 N N   . ASN C 2 83  ? 10.715 -12.995 40.056  1.00 66.07  ?  83  ASN D N   1 
ATOM   3944 C CA  . ASN C 2 83  ? 9.680  -13.856 39.504  1.00 66.69  ?  83  ASN D CA  1 
ATOM   3945 C C   . ASN C 2 83  ? 10.238 -14.644 38.328  1.00 65.66  ?  83  ASN D C   1 
ATOM   3946 O O   . ASN C 2 83  ? 11.142 -14.179 37.626  1.00 64.69  ?  83  ASN D O   1 
ATOM   3947 C CB  . ASN C 2 83  ? 8.458  -13.043 39.051  1.00 61.22  ?  83  ASN D CB  1 
ATOM   3948 C CG  . ASN C 2 83  ? 7.747  -12.365 40.207  1.00 64.48  ?  83  ASN D CG  1 
ATOM   3949 O OD1 . ASN C 2 83  ? 8.006  -12.665 41.372  1.00 65.22  ?  83  ASN D OD1 1 
ATOM   3950 N ND2 . ASN C 2 83  ? 6.844  -11.444 39.888  1.00 64.22  ?  83  ASN D ND2 1 
ATOM   3951 N N   . SER C 2 84  ? 9.685  -15.841 38.119  1.00 67.19  ?  84  SER D N   1 
ATOM   3952 C CA  . SER C 2 84  ? 10.136 -16.750 37.068  1.00 66.75  ?  84  SER D CA  1 
ATOM   3953 C C   . SER C 2 84  ? 11.643 -16.957 37.146  1.00 71.04  ?  84  SER D C   1 
ATOM   3954 O O   . SER C 2 84  ? 12.395 -16.372 36.361  1.00 68.78  ?  84  SER D O   1 
ATOM   3955 C CB  . SER C 2 84  ? 9.741  -16.220 35.686  1.00 60.75  ?  84  SER D CB  1 
ATOM   3956 O OG  . SER C 2 84  ? 8.530  -15.487 35.743  1.00 62.63  ?  84  SER D OG  1 
ATOM   3957 N N   . LEU C 2 85  ? 12.095 -17.779 38.090  1.00 72.68  ?  85  LEU D N   1 
ATOM   3958 C CA  . LEU C 2 85  ? 13.518 -17.942 38.360  1.00 74.30  ?  85  LEU D CA  1 
ATOM   3959 C C   . LEU C 2 85  ? 14.098 -19.030 37.468  1.00 78.86  ?  85  LEU D C   1 
ATOM   3960 O O   . LEU C 2 85  ? 13.533 -20.122 37.360  1.00 84.99  ?  85  LEU D O   1 
ATOM   3961 C CB  . LEU C 2 85  ? 13.749 -18.281 39.833  1.00 76.12  ?  85  LEU D CB  1 
ATOM   3962 C CG  . LEU C 2 85  ? 14.050 -17.082 40.733  1.00 78.44  ?  85  LEU D CG  1 
ATOM   3963 C CD1 . LEU C 2 85  ? 12.873 -16.124 40.748  1.00 71.66  ?  85  LEU D CD1 1 
ATOM   3964 C CD2 . LEU C 2 85  ? 14.401 -17.527 42.144  1.00 78.17  ?  85  LEU D CD2 1 
ATOM   3965 N N   . LYS C 2 86  ? 15.220 -18.726 36.828  1.00 77.32  ?  86  LYS D N   1 
ATOM   3966 C CA  . LYS C 2 86  ? 15.860 -19.636 35.892  1.00 83.01  ?  86  LYS D CA  1 
ATOM   3967 C C   . LYS C 2 86  ? 17.169 -20.158 36.480  1.00 87.64  ?  86  LYS D C   1 
ATOM   3968 O O   . LYS C 2 86  ? 17.687 -19.599 37.454  1.00 80.46  ?  86  LYS D O   1 
ATOM   3969 C CB  . LYS C 2 86  ? 16.133 -18.943 34.541  1.00 78.59  ?  86  LYS D CB  1 
ATOM   3970 C CG  . LYS C 2 86  ? 15.025 -18.040 33.918  1.00 74.66  ?  86  LYS D CG  1 
ATOM   3971 C CD  . LYS C 2 86  ? 13.556 -18.344 34.269  1.00 76.77  ?  86  LYS D CD  1 
ATOM   3972 C CE  . LYS C 2 86  ? 13.103 -19.765 33.961  1.00 74.85  ?  86  LYS D CE  1 
ATOM   3973 N NZ  . LYS C 2 86  ? 11.865 -20.082 34.732  1.00 68.55  ?  86  LYS D NZ  1 
ATOM   3974 N N   . PRO C 2 87  ? 17.726 -21.243 35.929  1.00 91.84  ?  87  PRO D N   1 
ATOM   3975 C CA  . PRO C 2 87  ? 18.996 -21.766 36.471  1.00 91.01  ?  87  PRO D CA  1 
ATOM   3976 C C   . PRO C 2 87  ? 20.138 -20.762 36.453  1.00 89.68  ?  87  PRO D C   1 
ATOM   3977 O O   . PRO C 2 87  ? 21.082 -20.909 37.242  1.00 88.43  ?  87  PRO D O   1 
ATOM   3978 C CB  . PRO C 2 87  ? 19.308 -22.974 35.575  1.00 86.41  ?  87  PRO D CB  1 
ATOM   3979 C CG  . PRO C 2 87  ? 18.064 -23.284 34.843  1.00 89.05  ?  87  PRO D CG  1 
ATOM   3980 C CD  . PRO C 2 87  ? 17.135 -22.127 34.908  1.00 89.14  ?  87  PRO D CD  1 
ATOM   3981 N N   . GLU C 2 88  ? 20.085 -19.746 35.590  1.00 89.23  ?  88  GLU D N   1 
ATOM   3982 C CA  . GLU C 2 88  ? 21.138 -18.737 35.539  1.00 89.66  ?  88  GLU D CA  1 
ATOM   3983 C C   . GLU C 2 88  ? 21.088 -17.768 36.714  1.00 84.20  ?  88  GLU D C   1 
ATOM   3984 O O   . GLU C 2 88  ? 22.027 -16.983 36.884  1.00 83.31  ?  88  GLU D O   1 
ATOM   3985 C CB  . GLU C 2 88  ? 21.050 -17.959 34.225  1.00 94.87  ?  88  GLU D CB  1 
ATOM   3986 C CG  . GLU C 2 88  ? 21.269 -18.807 32.980  1.00 99.49  ?  88  GLU D CG  1 
ATOM   3987 C CD  . GLU C 2 88  ? 19.982 -19.413 32.449  1.00 99.49  ?  88  GLU D CD  1 
ATOM   3988 O OE1 . GLU C 2 88  ? 18.901 -18.851 32.725  1.00 98.55  ?  88  GLU D OE1 1 
ATOM   3989 O OE2 . GLU C 2 88  ? 20.053 -20.449 31.754  1.00 94.41  ?  88  GLU D OE2 1 
ATOM   3990 N N   . ASP C 2 89  ? 20.030 -17.800 37.521  1.00 80.73  ?  89  ASP D N   1 
ATOM   3991 C CA  . ASP C 2 89  ? 19.879 -16.901 38.657  1.00 76.63  ?  89  ASP D CA  1 
ATOM   3992 C C   . ASP C 2 89  ? 20.546 -17.424 39.923  1.00 78.03  ?  89  ASP D C   1 
ATOM   3993 O O   . ASP C 2 89  ? 20.380 -16.822 40.988  1.00 79.52  ?  89  ASP D O   1 
ATOM   3994 C CB  . ASP C 2 89  ? 18.394 -16.643 38.928  1.00 71.69  ?  89  ASP D CB  1 
ATOM   3995 C CG  . ASP C 2 89  ? 17.672 -16.060 37.728  1.00 74.01  ?  89  ASP D CG  1 
ATOM   3996 O OD1 . ASP C 2 89  ? 18.350 -15.597 36.787  1.00 76.14  -1 89  ASP D OD1 1 
ATOM   3997 O OD2 . ASP C 2 89  ? 16.423 -16.068 37.728  1.00 68.79  ?  89  ASP D OD2 1 
ATOM   3998 N N   . THR C 2 90  ? 21.315 -18.499 39.791  1.00 81.52  ?  90  THR D N   1 
ATOM   3999 C CA  . THR C 2 90  ? 21.913 -19.116 40.999  1.00 85.32  ?  90  THR D CA  1 
ATOM   4000 C C   . THR C 2 90  ? 23.155 -18.329 41.410  1.00 80.87  ?  90  THR D C   1 
ATOM   4001 O O   . THR C 2 90  ? 23.999 -18.068 40.541  1.00 84.01  ?  90  THR D O   1 
ATOM   4002 C CB  . THR C 2 90  ? 22.109 -20.630 40.836  1.00 87.24  ?  90  THR D CB  1 
ATOM   4003 O OG1 . THR C 2 90  ? 21.022 -21.149 40.070  1.00 83.91  ?  90  THR D OG1 1 
ATOM   4004 C CG2 . THR C 2 90  ? 22.182 -21.349 42.164  1.00 80.94  ?  90  THR D CG2 1 
ATOM   4005 N N   . GLY C 2 91  ? 23.237 -17.964 42.685  1.00 74.68  ?  91  GLY D N   1 
ATOM   4006 C CA  . GLY C 2 91  ? 24.391 -17.247 43.191  1.00 74.36  ?  91  GLY D CA  1 
ATOM   4007 C C   . GLY C 2 91  ? 24.074 -16.539 44.485  1.00 74.19  ?  91  GLY D C   1 
ATOM   4008 O O   . GLY C 2 91  ? 22.933 -16.496 44.945  1.00 75.27  ?  91  GLY D O   1 
ATOM   4009 N N   . VAL C 2 92  ? 25.125 -15.976 45.077  1.00 72.23  ?  92  VAL D N   1 
ATOM   4010 C CA  . VAL C 2 92  ? 24.992 -15.198 46.303  1.00 75.11  ?  92  VAL D CA  1 
ATOM   4011 C C   . VAL C 2 92  ? 24.549 -13.787 45.941  1.00 76.15  ?  92  VAL D C   1 
ATOM   4012 O O   . VAL C 2 92  ? 25.128 -13.150 45.052  1.00 77.21  ?  92  VAL D O   1 
ATOM   4013 C CB  . VAL C 2 92  ? 26.317 -15.181 47.083  1.00 76.52  ?  92  VAL D CB  1 
ATOM   4014 C CG1 . VAL C 2 92  ? 26.179 -14.354 48.353  1.00 76.88  ?  92  VAL D CG1 1 
ATOM   4015 C CG2 . VAL C 2 92  ? 26.765 -16.598 47.407  1.00 77.07  ?  92  VAL D CG2 1 
ATOM   4016 N N   . TYR C 2 93  ? 23.523 -13.292 46.630  1.00 73.07  ?  93  TYR D N   1 
ATOM   4017 C CA  . TYR C 2 93  ? 22.934 -11.988 46.347  1.00 69.54  ?  93  TYR D CA  1 
ATOM   4018 C C   . TYR C 2 93  ? 23.289 -11.017 47.466  1.00 77.32  ?  93  TYR D C   1 
ATOM   4019 O O   . TYR C 2 93  ? 22.955 -11.256 48.631  1.00 77.11  ?  93  TYR D O   1 
ATOM   4020 C CB  . TYR C 2 93  ? 21.417 -12.097 46.189  1.00 62.49  ?  93  TYR D CB  1 
ATOM   4021 C CG  . TYR C 2 93  ? 20.976 -12.504 44.801  1.00 72.75  ?  93  TYR D CG  1 
ATOM   4022 C CD1 . TYR C 2 93  ? 21.337 -13.735 44.269  1.00 68.34  ?  93  TYR D CD1 1 
ATOM   4023 C CD2 . TYR C 2 93  ? 20.200 -11.655 44.020  1.00 66.79  ?  93  TYR D CD2 1 
ATOM   4024 C CE1 . TYR C 2 93  ? 20.938 -14.110 43.000  1.00 69.08  ?  93  TYR D CE1 1 
ATOM   4025 C CE2 . TYR C 2 93  ? 19.798 -12.024 42.750  1.00 62.86  ?  93  TYR D CE2 1 
ATOM   4026 C CZ  . TYR C 2 93  ? 20.169 -13.253 42.245  1.00 67.63  ?  93  TYR D CZ  1 
ATOM   4027 O OH  . TYR C 2 93  ? 19.771 -13.627 40.981  1.00 67.88  ?  93  TYR D OH  1 
ATOM   4028 N N   . TYR C 2 94  ? 23.962 -9.925  47.109  1.00 70.55  ?  94  TYR D N   1 
ATOM   4029 C CA  . TYR C 2 94  ? 24.319 -8.867  48.046  1.00 69.64  ?  94  TYR D CA  1 
ATOM   4030 C C   . TYR C 2 94  ? 23.468 -7.637  47.763  1.00 68.65  ?  94  TYR D C   1 
ATOM   4031 O O   . TYR C 2 94  ? 23.327 -7.231  46.606  1.00 67.15  ?  94  TYR D O   1 
ATOM   4032 C CB  . TYR C 2 94  ? 25.802 -8.497  47.937  1.00 69.81  ?  94  TYR D CB  1 
ATOM   4033 C CG  . TYR C 2 94  ? 26.765 -9.665  47.898  1.00 78.80  ?  94  TYR D CG  1 
ATOM   4034 C CD1 . TYR C 2 94  ? 27.078 -10.296 46.700  1.00 76.79  ?  94  TYR D CD1 1 
ATOM   4035 C CD2 . TYR C 2 94  ? 27.382 -10.120 49.057  1.00 81.49  ?  94  TYR D CD2 1 
ATOM   4036 C CE1 . TYR C 2 94  ? 27.964 -11.357 46.661  1.00 81.91  ?  94  TYR D CE1 1 
ATOM   4037 C CE2 . TYR C 2 94  ? 28.270 -11.182 49.028  1.00 77.15  ?  94  TYR D CE2 1 
ATOM   4038 C CZ  . TYR C 2 94  ? 28.558 -11.795 47.826  1.00 83.16  ?  94  TYR D CZ  1 
ATOM   4039 O OH  . TYR C 2 94  ? 29.441 -12.851 47.789  1.00 85.61  ?  94  TYR D OH  1 
ATOM   4040 N N   . CYS C 2 95  ? 22.904 -7.050  48.813  1.00 69.23  ?  95  CYS D N   1 
ATOM   4041 C CA  . CYS C 2 95  ? 22.256 -5.755  48.684  1.00 64.91  ?  95  CYS D CA  1 
ATOM   4042 C C   . CYS C 2 95  ? 23.285 -4.653  48.905  1.00 67.38  ?  95  CYS D C   1 
ATOM   4043 O O   . CYS C 2 95  ? 24.238 -4.808  49.673  1.00 64.18  ?  95  CYS D O   1 
ATOM   4044 C CB  . CYS C 2 95  ? 21.088 -5.614  49.664  1.00 67.31  ?  95  CYS D CB  1 
ATOM   4045 S SG  . CYS C 2 95  ? 21.509 -5.632  51.417  1.00 79.10  ?  95  CYS D SG  1 
ATOM   4046 N N   . HIS C 2 96  ? 23.093 -3.538  48.205  1.00 66.67  ?  96  HIS D N   1 
ATOM   4047 C CA  . HIS C 2 96  ? 24.101 -2.491  48.123  1.00 62.10  ?  96  HIS D CA  1 
ATOM   4048 C C   . HIS C 2 96  ? 23.479 -1.132  48.400  1.00 62.26  ?  96  HIS D C   1 
ATOM   4049 O O   . HIS C 2 96  ? 22.296 -0.904  48.136  1.00 61.05  ?  96  HIS D O   1 
ATOM   4050 C CB  . HIS C 2 96  ? 24.774 -2.486  46.743  1.00 58.89  ?  96  HIS D CB  1 
ATOM   4051 C CG  . HIS C 2 96  ? 25.998 -1.629  46.667  1.00 63.18  ?  96  HIS D CG  1 
ATOM   4052 N ND1 . HIS C 2 96  ? 26.151 -0.634  45.725  1.00 64.02  ?  96  HIS D ND1 1 
ATOM   4053 C CD2 . HIS C 2 96  ? 27.126 -1.619  47.413  1.00 62.24  ?  96  HIS D CD2 1 
ATOM   4054 C CE1 . HIS C 2 96  ? 27.322 -0.047  45.895  1.00 61.43  ?  96  HIS D CE1 1 
ATOM   4055 N NE2 . HIS C 2 96  ? 27.935 -0.626  46.913  1.00 64.36  ?  96  HIS D NE2 1 
ATOM   4056 N N   . ALA C 2 97  ? 24.297 -0.227  48.934  1.00 61.85  ?  97  ALA D N   1 
ATOM   4057 C CA  . ALA C 2 97  ? 23.865 1.131   49.227  1.00 63.02  ?  97  ALA D CA  1 
ATOM   4058 C C   . ALA C 2 97  ? 25.030 2.081   48.989  1.00 61.35  ?  97  ALA D C   1 
ATOM   4059 O O   . ALA C 2 97  ? 26.185 1.733   49.249  1.00 62.49  ?  97  ALA D O   1 
ATOM   4060 C CB  . ALA C 2 97  ? 23.353 1.263   50.667  1.00 67.31  ?  97  ALA D CB  1 
ATOM   4061 N N   . VAL C 2 98  ? 24.718 3.275   48.491  1.00 58.96  ?  98  VAL D N   1 
ATOM   4062 C CA  . VAL C 2 98  ? 25.711 4.310   48.221  1.00 59.56  ?  98  VAL D CA  1 
ATOM   4063 C C   . VAL C 2 98  ? 25.443 5.480   49.158  1.00 54.82  ?  98  VAL D C   1 
ATOM   4064 O O   . VAL C 2 98  ? 24.357 6.073   49.130  1.00 50.62  ?  98  VAL D O   1 
ATOM   4065 C CB  . VAL C 2 98  ? 25.681 4.759   46.751  1.00 52.97  ?  98  VAL D CB  1 
ATOM   4066 C CG1 . VAL C 2 98  ? 26.988 5.440   46.382  1.00 49.13  ?  98  VAL D CG1 1 
ATOM   4067 C CG2 . VAL C 2 98  ? 25.429 3.567   45.839  1.00 49.49  ?  98  VAL D CG2 1 
ATOM   4068 N N   . THR C 2 99  ? 26.435 5.812   49.983  1.00 58.29  ?  99  THR D N   1 
ATOM   4069 C CA  . THR C 2 99  ? 26.318 6.902   50.945  1.00 60.85  ?  99  THR D CA  1 
ATOM   4070 C C   . THR C 2 99  ? 27.071 8.156   50.528  1.00 64.75  ?  99  THR D C   1 
ATOM   4071 O O   . THR C 2 99  ? 26.711 9.254   50.964  1.00 64.49  ?  99  THR D O   1 
ATOM   4072 C CB  . THR C 2 99  ? 26.825 6.453   52.321  1.00 62.32  ?  99  THR D CB  1 
ATOM   4073 O OG1 . THR C 2 99  ? 27.963 5.595   52.158  1.00 63.63  ?  99  THR D OG1 1 
ATOM   4074 C CG2 . THR C 2 99  ? 25.738 5.701   53.063  1.00 64.37  ?  99  THR D CG2 1 
ATOM   4075 N N   . GLY C 2 100 ? 28.106 8.018   49.702  1.00 61.10  ?  100 GLY D N   1 
ATOM   4076 C CA  . GLY C 2 100 ? 28.874 9.150   49.234  1.00 53.76  ?  100 GLY D CA  1 
ATOM   4077 C C   . GLY C 2 100 ? 29.440 8.865   47.859  1.00 54.09  ?  100 GLY D C   1 
ATOM   4078 O O   . GLY C 2 100 ? 29.251 7.781   47.303  1.00 53.55  ?  100 GLY D O   1 
ATOM   4079 N N   . VAL C 2 101 ? 30.139 9.861   47.310  1.00 51.75  ?  101 VAL D N   1 
ATOM   4080 C CA  . VAL C 2 101 ? 30.730 9.719   45.981  1.00 54.74  ?  101 VAL D CA  1 
ATOM   4081 C C   . VAL C 2 101 ? 31.697 8.544   45.943  1.00 54.61  ?  101 VAL D C   1 
ATOM   4082 O O   . VAL C 2 101 ? 31.833 7.872   44.914  1.00 50.27  ?  101 VAL D O   1 
ATOM   4083 C CB  . VAL C 2 101 ? 31.417 11.032  45.562  1.00 44.77  ?  101 VAL D CB  1 
ATOM   4084 C CG1 . VAL C 2 101 ? 30.385 12.035  45.077  1.00 44.39  ?  101 VAL D CG1 1 
ATOM   4085 C CG2 . VAL C 2 101 ? 32.213 11.607  46.722  1.00 47.71  ?  101 VAL D CG2 1 
ATOM   4086 N N   . ILE C 2 102 ? 32.378 8.277   47.057  1.00 54.70  ?  102 ILE D N   1 
ATOM   4087 C CA  . ILE C 2 102 ? 33.235 7.111   47.179  1.00 52.09  ?  102 ILE D CA  1 
ATOM   4088 C C   . ILE C 2 102 ? 32.675 6.087   48.163  1.00 54.83  ?  102 ILE D C   1 
ATOM   4089 O O   . ILE C 2 102 ? 32.816 4.880   47.932  1.00 56.31  ?  102 ILE D O   1 
ATOM   4090 C CB  . ILE C 2 102 ? 34.665 7.537   47.586  1.00 58.87  ?  102 ILE D CB  1 
ATOM   4091 C CG1 . ILE C 2 102 ? 35.394 8.207   46.419  1.00 58.89  ?  102 ILE D CG1 1 
ATOM   4092 C CG2 . ILE C 2 102 ? 35.475 6.350   48.082  1.00 61.25  ?  102 ILE D CG2 1 
ATOM   4093 C CD1 . ILE C 2 102 ? 35.008 7.685   45.052  1.00 54.74  ?  102 ILE D CD1 1 
ATOM   4094 N N   . ALA C 2 103 ? 32.013 6.531   49.229  1.00 59.64  ?  103 ALA D N   1 
ATOM   4095 C CA  . ALA C 2 103 ? 31.575 5.630   50.284  1.00 62.07  ?  103 ALA D CA  1 
ATOM   4096 C C   . ALA C 2 103 ? 30.422 4.748   49.823  1.00 63.69  ?  103 ALA D C   1 
ATOM   4097 O O   . ALA C 2 103 ? 29.535 5.185   49.084  1.00 61.70  ?  103 ALA D O   1 
ATOM   4098 C CB  . ALA C 2 103 ? 31.157 6.430   51.517  1.00 54.22  ?  103 ALA D CB  1 
ATOM   4099 N N   . SER C 2 104 ? 30.442 3.495   50.272  1.00 67.29  ?  104 SER D N   1 
ATOM   4100 C CA  . SER C 2 104 ? 29.377 2.541   49.998  1.00 66.78  ?  104 SER D CA  1 
ATOM   4101 C C   . SER C 2 104 ? 29.490 1.402   50.999  1.00 70.50  ?  104 SER D C   1 
ATOM   4102 O O   . SER C 2 104 ? 30.562 1.145   51.553  1.00 70.32  ?  104 SER D O   1 
ATOM   4103 C CB  . SER C 2 104 ? 29.444 2.010   48.561  1.00 66.44  ?  104 SER D CB  1 
ATOM   4104 O OG  . SER C 2 104 ? 30.646 1.293   48.337  1.00 68.30  ?  104 SER D OG  1 
ATOM   4105 N N   . SER C 2 105 ? 28.367 0.723   51.228  1.00 71.74  ?  105 SER D N   1 
ATOM   4106 C CA  . SER C 2 105 ? 28.310 -0.391  52.163  1.00 75.52  ?  105 SER D CA  1 
ATOM   4107 C C   . SER C 2 105 ? 27.594 -1.568  51.519  1.00 74.73  ?  105 SER D C   1 
ATOM   4108 O O   . SER C 2 105 ? 26.627 -1.387  50.770  1.00 70.58  ?  105 SER D O   1 
ATOM   4109 C CB  . SER C 2 105 ? 27.601 0.007   53.465  1.00 76.70  ?  105 SER D CB  1 
ATOM   4110 O OG  . SER C 2 105 ? 26.324 0.558   53.209  1.00 80.29  ?  105 SER D OG  1 
ATOM   4111 N N   . TRP C 2 106 ? 28.071 -2.771  51.817  1.00 76.48  ?  106 TRP D N   1 
ATOM   4112 C CA  . TRP C 2 106 ? 27.528 -4.005  51.271  1.00 78.61  ?  106 TRP D CA  1 
ATOM   4113 C C   . TRP C 2 106 ? 26.764 -4.770  52.341  1.00 85.25  ?  106 TRP D C   1 
ATOM   4114 O O   . TRP C 2 106 ? 26.762 -4.415  53.524  1.00 86.58  ?  106 TRP D O   1 
ATOM   4115 C CB  . TRP C 2 106 ? 28.645 -4.885  50.700  1.00 74.81  ?  106 TRP D CB  1 
ATOM   4116 C CG  . TRP C 2 106 ? 29.313 -4.317  49.493  1.00 74.65  ?  106 TRP D CG  1 
ATOM   4117 C CD1 . TRP C 2 106 ? 30.401 -3.494  49.470  1.00 74.63  ?  106 TRP D CD1 1 
ATOM   4118 C CD2 . TRP C 2 106 ? 28.943 -4.534  48.128  1.00 72.97  ?  106 TRP D CD2 1 
ATOM   4119 N NE1 . TRP C 2 106 ? 30.729 -3.183  48.173  1.00 75.43  ?  106 TRP D NE1 1 
ATOM   4120 C CE2 . TRP C 2 106 ? 29.850 -3.809  47.329  1.00 73.53  ?  106 TRP D CE2 1 
ATOM   4121 C CE3 . TRP C 2 106 ? 27.932 -5.271  47.501  1.00 70.75  ?  106 TRP D CE3 1 
ATOM   4122 C CZ2 . TRP C 2 106 ? 29.777 -3.797  45.938  1.00 66.76  ?  106 TRP D CZ2 1 
ATOM   4123 C CZ3 . TRP C 2 106 ? 27.861 -5.258  46.121  1.00 67.18  ?  106 TRP D CZ3 1 
ATOM   4124 C CH2 . TRP C 2 106 ? 28.778 -4.526  45.355  1.00 69.15  ?  106 TRP D CH2 1 
ATOM   4125 N N   . GLY C 2 107 ? 26.102 -5.843  51.902  1.00 84.71  ?  107 GLY D N   1 
ATOM   4126 C CA  . GLY C 2 107 ? 25.461 -6.762  52.819  1.00 86.33  ?  107 GLY D CA  1 
ATOM   4127 C C   . GLY C 2 107 ? 26.353 -7.942  53.154  1.00 89.24  ?  107 GLY D C   1 
ATOM   4128 O O   . GLY C 2 107 ? 27.440 -8.107  52.601  1.00 86.50  ?  107 GLY D O   1 
ATOM   4129 N N   . GLN C 2 108 ? 25.905 -8.776  54.090  1.00 91.40  ?  108 GLN D N   1 
ATOM   4130 C CA  . GLN C 2 108 ? 26.758 -9.909  54.536  1.00 90.06  ?  108 GLN D CA  1 
ATOM   4131 C C   . GLN C 2 108 ? 26.779 -10.982 53.446  1.00 82.83  ?  108 GLN D C   1 
ATOM   4132 O O   . GLN C 2 108 ? 27.804 -11.674 53.331  1.00 81.47  ?  108 GLN D O   1 
ATOM   4133 C CB  . GLN C 2 108 ? 26.247 -10.398 55.895  1.00 88.30  ?  108 GLN D CB  1 
ATOM   4134 C CG  . GLN C 2 108 ? 25.218 -11.519 55.820  1.00 87.98  ?  108 GLN D CG  1 
ATOM   4135 C CD  . GLN C 2 108 ? 23.944 -11.216 56.568  1.00 86.36  ?  108 GLN D CD  1 
ATOM   4136 O OE1 . GLN C 2 108 ? 23.895 -11.265 57.793  1.00 88.44  ?  108 GLN D OE1 1 
ATOM   4137 N NE2 . GLN C 2 108 ? 22.891 -10.913 55.830  1.00 82.86  ?  108 GLN D NE2 1 
ATOM   4138 N N   . LYS D 1 2   ? 31.562 41.832  38.626  1.00 63.17  ?  225 LYS A N   1 
ATOM   4139 C CA  . LYS D 1 2   ? 30.639 40.703  38.599  1.00 68.49  ?  225 LYS A CA  1 
ATOM   4140 C C   . LYS D 1 2   ? 31.141 39.557  39.473  1.00 68.73  ?  225 LYS A C   1 
ATOM   4141 O O   . LYS D 1 2   ? 32.312 39.185  39.402  1.00 65.10  ?  225 LYS A O   1 
ATOM   4142 C CB  . LYS D 1 2   ? 30.430 40.217  37.161  1.00 61.53  ?  225 LYS A CB  1 
ATOM   4143 C CG  . LYS D 1 2   ? 29.570 38.967  37.048  1.00 63.78  ?  225 LYS A CG  1 
ATOM   4144 C CD  . LYS D 1 2   ? 29.308 38.596  35.599  1.00 60.61  ?  225 LYS A CD  1 
ATOM   4145 C CE  . LYS D 1 2   ? 28.178 39.423  35.011  1.00 60.70  ?  225 LYS A CE  1 
ATOM   4146 N NZ  . LYS D 1 2   ? 27.937 39.089  33.580  1.00 60.79  ?  225 LYS A NZ  1 
ATOM   4147 N N   . PRO D 1 3   ? 30.257 39.003  40.303  1.00 67.73  ?  226 PRO A N   1 
ATOM   4148 C CA  . PRO D 1 3   ? 30.650 37.858  41.134  1.00 63.59  ?  226 PRO A CA  1 
ATOM   4149 C C   . PRO D 1 3   ? 30.751 36.583  40.311  1.00 61.10  ?  226 PRO A C   1 
ATOM   4150 O O   . PRO D 1 3   ? 29.981 36.362  39.372  1.00 60.73  ?  226 PRO A O   1 
ATOM   4151 C CB  . PRO D 1 3   ? 29.525 37.769  42.171  1.00 59.75  ?  226 PRO A CB  1 
ATOM   4152 C CG  . PRO D 1 3   ? 28.343 38.369  41.490  1.00 65.15  ?  226 PRO A CG  1 
ATOM   4153 C CD  . PRO D 1 3   ? 28.872 39.434  40.567  1.00 64.57  ?  226 PRO A CD  1 
ATOM   4154 N N   . PHE D 1 4   ? 31.711 35.740  40.678  1.00 59.67  ?  227 PHE A N   1 
ATOM   4155 C CA  . PHE D 1 4   ? 31.957 34.499  39.960  1.00 50.82  ?  227 PHE A CA  1 
ATOM   4156 C C   . PHE D 1 4   ? 30.963 33.423  40.382  1.00 53.46  ?  227 PHE A C   1 
ATOM   4157 O O   . PHE D 1 4   ? 30.478 33.402  41.517  1.00 50.27  ?  227 PHE A O   1 
ATOM   4158 C CB  . PHE D 1 4   ? 33.388 34.017  40.210  1.00 50.65  ?  227 PHE A CB  1 
ATOM   4159 C CG  . PHE D 1 4   ? 33.724 32.720  39.529  1.00 49.74  ?  227 PHE A CG  1 
ATOM   4160 C CD1 . PHE D 1 4   ? 33.956 32.675  38.164  1.00 48.11  ?  227 PHE A CD1 1 
ATOM   4161 C CD2 . PHE D 1 4   ? 33.808 31.545  40.257  1.00 41.55  ?  227 PHE A CD2 1 
ATOM   4162 C CE1 . PHE D 1 4   ? 34.266 31.483  37.538  1.00 44.97  ?  227 PHE A CE1 1 
ATOM   4163 C CE2 . PHE D 1 4   ? 34.117 30.349  39.638  1.00 42.36  ?  227 PHE A CE2 1 
ATOM   4164 C CZ  . PHE D 1 4   ? 34.348 30.318  38.277  1.00 45.28  ?  227 PHE A CZ  1 
ATOM   4165 N N   . SER D 1 5   ? 30.659 32.525  39.445  1.00 46.88  ?  228 SER A N   1 
ATOM   4166 C CA  . SER D 1 5   ? 29.737 31.428  39.706  1.00 42.11  ?  228 SER A CA  1 
ATOM   4167 C C   . SER D 1 5   ? 29.908 30.370  38.627  1.00 46.34  ?  228 SER A C   1 
ATOM   4168 O O   . SER D 1 5   ? 30.462 30.631  37.556  1.00 39.55  ?  228 SER A O   1 
ATOM   4169 C CB  . SER D 1 5   ? 28.284 31.913  39.762  1.00 38.08  ?  228 SER A CB  1 
ATOM   4170 O OG  . SER D 1 5   ? 27.792 32.219  38.469  1.00 42.76  ?  228 SER A OG  1 
ATOM   4171 N N   . VAL D 1 6   ? 29.425 29.172  38.926  1.00 43.70  ?  229 VAL A N   1 
ATOM   4172 C CA  . VAL D 1 6   ? 29.437 28.062  37.976  1.00 39.45  ?  229 VAL A CA  1 
ATOM   4173 C C   . VAL D 1 6   ? 27.990 27.712  37.663  1.00 36.97  ?  229 VAL A C   1 
ATOM   4174 O O   . VAL D 1 6   ? 27.078 28.013  38.454  1.00 38.70  ?  229 VAL A O   1 
ATOM   4175 C CB  . VAL D 1 6   ? 30.218 26.845  38.523  1.00 36.83  ?  229 VAL A CB  1 
ATOM   4176 C CG1 . VAL D 1 6   ? 31.670 27.216  38.768  1.00 39.91  ?  229 VAL A CG1 1 
ATOM   4177 C CG2 . VAL D 1 6   ? 29.568 26.326  39.796  1.00 42.35  ?  229 VAL A CG2 1 
ATOM   4178 N N   . PRO D 1 7   ? 27.738 27.090  36.509  1.00 43.75  ?  230 PRO A N   1 
ATOM   4179 C CA  . PRO D 1 7   ? 26.370 26.675  36.177  1.00 44.47  ?  230 PRO A CA  1 
ATOM   4180 C C   . PRO D 1 7   ? 25.798 25.717  37.208  1.00 40.70  ?  230 PRO A C   1 
ATOM   4181 O O   . PRO D 1 7   ? 26.516 24.971  37.884  1.00 35.19  ?  230 PRO A O   1 
ATOM   4182 C CB  . PRO D 1 7   ? 26.520 25.990  34.814  1.00 39.37  ?  230 PRO A CB  1 
ATOM   4183 C CG  . PRO D 1 7   ? 27.746 26.571  34.241  1.00 41.45  ?  230 PRO A CG  1 
ATOM   4184 C CD  . PRO D 1 7   ? 28.666 26.847  35.394  1.00 37.36  ?  230 PRO A CD  1 
ATOM   4185 N N   . VAL D 1 8   ? 24.469 25.738  37.312  1.00 39.25  ?  231 VAL A N   1 
ATOM   4186 C CA  . VAL D 1 8   ? 23.751 24.847  38.215  1.00 42.33  ?  231 VAL A CA  1 
ATOM   4187 C C   . VAL D 1 8   ? 23.294 23.566  37.512  1.00 43.03  ?  231 VAL A C   1 
ATOM   4188 O O   . VAL D 1 8   ? 22.507 22.803  38.076  1.00 49.16  ?  231 VAL A O   1 
ATOM   4189 C CB  . VAL D 1 8   ? 22.554 25.569  38.861  1.00 41.95  ?  231 VAL A CB  1 
ATOM   4190 C CG1 . VAL D 1 8   ? 23.025 26.831  39.607  1.00 41.62  ?  231 VAL A CG1 1 
ATOM   4191 C CG2 . VAL D 1 8   ? 21.499 25.919  37.838  1.00 42.26  ?  231 VAL A CG2 1 
ATOM   4192 N N   . LEU D 1 9   ? 23.768 23.309  36.296  1.00 43.87  ?  232 LEU A N   1 
ATOM   4193 C CA  . LEU D 1 9   ? 23.381 22.097  35.588  1.00 42.24  ?  232 LEU A CA  1 
ATOM   4194 C C   . LEU D 1 9   ? 24.010 20.871  36.232  1.00 40.48  ?  232 LEU A C   1 
ATOM   4195 O O   . LEU D 1 9   ? 25.185 20.883  36.608  1.00 41.55  ?  232 LEU A O   1 
ATOM   4196 C CB  . LEU D 1 9   ? 23.811 22.196  34.132  1.00 37.54  ?  232 LEU A CB  1 
ATOM   4197 C CG  . LEU D 1 9   ? 23.281 23.405  33.348  1.00 49.45  ?  232 LEU A CG  1 
ATOM   4198 C CD1 . LEU D 1 9   ? 24.113 23.655  32.099  1.00 40.17  ?  232 LEU A CD1 1 
ATOM   4199 C CD2 . LEU D 1 9   ? 21.812 23.234  32.984  1.00 43.25  ?  232 LEU A CD2 1 
ATOM   4200 N N   . THR D 1 10  ? 23.229 19.801  36.334  1.00 41.26  ?  233 THR A N   1 
ATOM   4201 C CA  . THR D 1 10  ? 23.755 18.530  36.803  1.00 42.22  ?  233 THR A CA  1 
ATOM   4202 C C   . THR D 1 10  ? 24.740 17.953  35.782  1.00 42.67  ?  233 THR A C   1 
ATOM   4203 O O   . THR D 1 10  ? 24.799 18.377  34.624  1.00 38.33  ?  233 THR A O   1 
ATOM   4204 C CB  . THR D 1 10  ? 22.621 17.541  37.059  1.00 41.82  ?  233 THR A CB  1 
ATOM   4205 O OG1 . THR D 1 10  ? 22.062 17.107  35.812  1.00 40.53  ?  233 THR A OG1 1 
ATOM   4206 C CG2 . THR D 1 10  ? 21.537 18.174  37.900  1.00 41.84  ?  233 THR A CG2 1 
ATOM   4207 N N   . VAL D 1 11  ? 25.518 16.963  36.229  1.00 41.95  ?  234 VAL A N   1 
ATOM   4208 C CA  . VAL D 1 11  ? 26.549 16.379  35.369  1.00 40.82  ?  234 VAL A CA  1 
ATOM   4209 C C   . VAL D 1 11  ? 25.933 15.793  34.102  1.00 41.91  ?  234 VAL A C   1 
ATOM   4210 O O   . VAL D 1 11  ? 26.438 16.003  32.992  1.00 42.93  ?  234 VAL A O   1 
ATOM   4211 C CB  . VAL D 1 11  ? 27.360 15.324  36.147  1.00 38.56  ?  234 VAL A CB  1 
ATOM   4212 C CG1 . VAL D 1 11  ? 28.165 14.452  35.196  1.00 44.52  ?  234 VAL A CG1 1 
ATOM   4213 C CG2 . VAL D 1 11  ? 28.273 15.998  37.159  1.00 43.41  ?  234 VAL A CG2 1 
ATOM   4214 N N   . GLU D 1 12  ? 24.819 15.071  34.241  1.00 39.00  ?  235 GLU A N   1 
ATOM   4215 C CA  . GLU D 1 12  ? 24.196 14.424  33.093  1.00 41.34  ?  235 GLU A CA  1 
ATOM   4216 C C   . GLU D 1 12  ? 23.503 15.405  32.156  1.00 42.99  ?  235 GLU A C   1 
ATOM   4217 O O   . GLU D 1 12  ? 23.159 15.018  31.034  1.00 45.85  ?  235 GLU A O   1 
ATOM   4218 C CB  . GLU D 1 12  ? 23.198 13.365  33.566  1.00 41.99  ?  235 GLU A CB  1 
ATOM   4219 C CG  . GLU D 1 12  ? 23.835 12.017  33.873  1.00 41.19  ?  235 GLU A CG  1 
ATOM   4220 C CD  . GLU D 1 12  ? 22.882 11.064  34.568  1.00 55.95  ?  235 GLU A CD  1 
ATOM   4221 O OE1 . GLU D 1 12  ? 21.680 11.388  34.666  1.00 59.29  ?  235 GLU A OE1 1 
ATOM   4222 O OE2 . GLU D 1 12  ? 23.337 9.991   35.018  1.00 56.56  ?  235 GLU A OE2 1 
ATOM   4223 N N   . GLU D 1 13  ? 23.290 16.649  32.579  1.00 37.99  ?  236 GLU A N   1 
ATOM   4224 C CA  . GLU D 1 13  ? 22.703 17.673  31.724  1.00 38.90  ?  236 GLU A CA  1 
ATOM   4225 C C   . GLU D 1 13  ? 23.744 18.422  30.904  1.00 43.81  ?  236 GLU A C   1 
ATOM   4226 O O   . GLU D 1 13  ? 23.376 19.302  30.118  1.00 44.10  ?  236 GLU A O   1 
ATOM   4227 C CB  . GLU D 1 13  ? 21.907 18.677  32.565  1.00 38.07  ?  236 GLU A CB  1 
ATOM   4228 C CG  . GLU D 1 13  ? 20.582 18.157  33.097  1.00 40.29  ?  236 GLU A CG  1 
ATOM   4229 C CD  . GLU D 1 13  ? 20.032 19.019  34.223  1.00 48.08  ?  236 GLU A CD  1 
ATOM   4230 O OE1 . GLU D 1 13  ? 20.780 19.884  34.729  1.00 46.90  ?  236 GLU A OE1 1 
ATOM   4231 O OE2 . GLU D 1 13  ? 18.857 18.833  34.602  1.00 49.62  ?  236 GLU A OE2 1 
ATOM   4232 N N   . MET D 1 14  ? 25.023 18.103  31.063  1.00 40.08  ?  237 MET A N   1 
ATOM   4233 C CA  . MET D 1 14  ? 26.101 18.823  30.406  1.00 39.98  ?  237 MET A CA  1 
ATOM   4234 C C   . MET D 1 14  ? 26.737 17.966  29.320  1.00 34.92  ?  237 MET A C   1 
ATOM   4235 O O   . MET D 1 14  ? 26.543 16.750  29.248  1.00 43.56  ?  237 MET A O   1 
ATOM   4236 C CB  . MET D 1 14  ? 27.151 19.275  31.427  1.00 35.67  ?  237 MET A CB  1 
ATOM   4237 C CG  . MET D 1 14  ? 26.566 19.992  32.627  1.00 44.86  ?  237 MET A CG  1 
ATOM   4238 S SD  . MET D 1 14  ? 27.720 21.137  33.399  1.00 40.95  ?  237 MET A SD  1 
ATOM   4239 C CE  . MET D 1 14  ? 28.226 20.166  34.820  1.00 33.20  ?  237 MET A CE  1 
ATOM   4240 N N   . THR D 1 15  ? 27.515 18.631  28.473  1.00 36.50  ?  238 THR A N   1 
ATOM   4241 C CA  . THR D 1 15  ? 28.106 18.034  27.287  1.00 35.73  ?  238 THR A CA  1 
ATOM   4242 C C   . THR D 1 15  ? 29.615 17.931  27.456  1.00 40.34  ?  238 THR A C   1 
ATOM   4243 O O   . THR D 1 15  ? 30.248 18.831  28.016  1.00 34.46  ?  238 THR A O   1 
ATOM   4244 C CB  . THR D 1 15  ? 27.777 18.871  26.044  1.00 39.12  ?  238 THR A CB  1 
ATOM   4245 O OG1 . THR D 1 15  ? 26.364 19.106  25.985  1.00 43.13  ?  238 THR A OG1 1 
ATOM   4246 C CG2 . THR D 1 15  ? 28.223 18.162  24.769  1.00 36.13  ?  238 THR A CG2 1 
ATOM   4247 N N   . ASN D 1 16  ? 30.183 16.821  26.988  1.00 32.18  ?  239 ASN A N   1 
ATOM   4248 C CA  . ASN D 1 16  ? 31.632 16.708  26.908  1.00 33.55  ?  239 ASN A CA  1 
ATOM   4249 C C   . ASN D 1 16  ? 32.173 17.761  25.951  1.00 37.30  ?  239 ASN A C   1 
ATOM   4250 O O   . ASN D 1 16  ? 31.596 18.016  24.890  1.00 36.92  ?  239 ASN A O   1 
ATOM   4251 C CB  . ASN D 1 16  ? 32.030 15.305  26.446  1.00 33.76  ?  239 ASN A CB  1 
ATOM   4252 C CG  . ASN D 1 16  ? 33.458 14.948  26.813  1.00 28.38  ?  239 ASN A CG  1 
ATOM   4253 O OD1 . ASN D 1 16  ? 34.410 15.485  26.249  1.00 32.45  ?  239 ASN A OD1 1 
ATOM   4254 N ND2 . ASN D 1 16  ? 33.613 14.028  27.756  1.00 29.93  ?  239 ASN A ND2 1 
ATOM   4255 N N   . SER D 1 17  ? 33.282 18.386  26.331  1.00 35.51  ?  240 SER A N   1 
ATOM   4256 C CA  . SER D 1 17  ? 33.843 19.481  25.553  1.00 36.48  ?  240 SER A CA  1 
ATOM   4257 C C   . SER D 1 17  ? 34.860 19.021  24.517  1.00 38.12  ?  240 SER A C   1 
ATOM   4258 O O   . SER D 1 17  ? 35.454 19.864  23.839  1.00 38.28  ?  240 SER A O   1 
ATOM   4259 C CB  . SER D 1 17  ? 34.486 20.508  26.487  1.00 36.83  ?  240 SER A CB  1 
ATOM   4260 O OG  . SER D 1 17  ? 35.475 19.903  27.298  1.00 38.10  ?  240 SER A OG  1 
ATOM   4261 N N   . ARG D 1 18  ? 35.070 17.713  24.375  1.00 39.31  ?  241 ARG A N   1 
ATOM   4262 C CA  . ARG D 1 18  ? 35.997 17.178  23.388  1.00 37.63  ?  241 ARG A CA  1 
ATOM   4263 C C   . ARG D 1 18  ? 35.326 16.270  22.368  1.00 36.66  ?  241 ARG A C   1 
ATOM   4264 O O   . ARG D 1 18  ? 36.000 15.790  21.450  1.00 32.55  ?  241 ARG A O   1 
ATOM   4265 C CB  . ARG D 1 18  ? 37.136 16.419  24.087  1.00 37.50  ?  241 ARG A CB  1 
ATOM   4266 C CG  . ARG D 1 18  ? 37.874 17.248  25.125  1.00 37.43  ?  241 ARG A CG  1 
ATOM   4267 C CD  . ARG D 1 18  ? 38.935 16.430  25.836  1.00 38.07  ?  241 ARG A CD  1 
ATOM   4268 N NE  . ARG D 1 18  ? 39.959 15.947  24.917  1.00 39.63  ?  241 ARG A NE  1 
ATOM   4269 C CZ  . ARG D 1 18  ? 40.759 14.919  25.165  1.00 39.97  ?  241 ARG A CZ  1 
ATOM   4270 N NH1 . ARG D 1 18  ? 40.677 14.236  26.296  1.00 35.32  ?  241 ARG A NH1 1 
ATOM   4271 N NH2 . ARG D 1 18  ? 41.665 14.568  24.257  1.00 36.55  ?  241 ARG A NH2 1 
ATOM   4272 N N   . PHE D 1 19  ? 34.018 16.026  22.499  1.00 32.55  ?  242 PHE A N   1 
ATOM   4273 C CA  . PHE D 1 19  ? 33.257 15.200  21.572  1.00 33.37  ?  242 PHE A CA  1 
ATOM   4274 C C   . PHE D 1 19  ? 31.789 15.511  21.786  1.00 34.17  ?  242 PHE A C   1 
ATOM   4275 O O   . PHE D 1 19  ? 31.368 15.666  22.941  1.00 35.10  ?  242 PHE A O   1 
ATOM   4276 C CB  . PHE D 1 19  ? 33.521 13.706  21.795  1.00 35.72  ?  242 PHE A CB  1 
ATOM   4277 C CG  . PHE D 1 19  ? 33.339 12.861  20.566  1.00 31.86  ?  242 PHE A CG  1 
ATOM   4278 C CD1 . PHE D 1 19  ? 34.292 12.860  19.562  1.00 32.04  ?  242 PHE A CD1 1 
ATOM   4279 C CD2 . PHE D 1 19  ? 32.219 12.059  20.421  1.00 30.11  ?  242 PHE A CD2 1 
ATOM   4280 C CE1 . PHE D 1 19  ? 34.128 12.079  18.430  1.00 36.98  ?  242 PHE A CE1 1 
ATOM   4281 C CE2 . PHE D 1 19  ? 32.049 11.276  19.294  1.00 35.42  ?  242 PHE A CE2 1 
ATOM   4282 C CZ  . PHE D 1 19  ? 33.004 11.288  18.297  1.00 35.03  ?  242 PHE A CZ  1 
ATOM   4283 N N   . PRO D 1 20  ? 30.984 15.614  20.726  1.00 34.44  ?  243 PRO A N   1 
ATOM   4284 C CA  . PRO D 1 20  ? 29.562 15.940  20.910  1.00 37.00  ?  243 PRO A CA  1 
ATOM   4285 C C   . PRO D 1 20  ? 28.771 14.815  21.563  1.00 36.57  ?  243 PRO A C   1 
ATOM   4286 O O   . PRO D 1 20  ? 27.864 14.248  20.947  1.00 39.59  ?  243 PRO A O   1 
ATOM   4287 C CB  . PRO D 1 20  ? 29.077 16.211  19.481  1.00 38.33  ?  243 PRO A CB  1 
ATOM   4288 C CG  . PRO D 1 20  ? 30.021 15.450  18.610  1.00 34.31  ?  243 PRO A CG  1 
ATOM   4289 C CD  . PRO D 1 20  ? 31.352 15.498  19.305  1.00 31.88  ?  243 PRO A CD  1 
ATOM   4290 N N   . ILE D 1 21  ? 29.108 14.489  22.810  1.00 35.59  ?  244 ILE A N   1 
ATOM   4291 C CA  . ILE D 1 21  ? 28.373 13.481  23.577  1.00 35.65  ?  244 ILE A CA  1 
ATOM   4292 C C   . ILE D 1 21  ? 28.171 13.983  24.994  1.00 37.49  ?  244 ILE A C   1 
ATOM   4293 O O   . ILE D 1 21  ? 28.958 14.786  25.513  1.00 32.28  ?  244 ILE A O   1 
ATOM   4294 C CB  . ILE D 1 21  ? 29.113 12.123  23.607  1.00 34.91  ?  244 ILE A CB  1 
ATOM   4295 C CG1 . ILE D 1 21  ? 30.539 12.293  24.139  1.00 30.71  ?  244 ILE A CG1 1 
ATOM   4296 C CG2 . ILE D 1 21  ? 29.108 11.479  22.225  1.00 32.90  ?  244 ILE A CG2 1 
ATOM   4297 C CD1 . ILE D 1 21  ? 31.406 11.059  23.979  1.00 35.40  ?  244 ILE A CD1 1 
ATOM   4298 N N   . PRO D 1 22  ? 27.100 13.533  25.645  1.00 34.99  ?  245 PRO A N   1 
ATOM   4299 C CA  . PRO D 1 22  ? 26.827 13.991  27.012  1.00 36.95  ?  245 PRO A CA  1 
ATOM   4300 C C   . PRO D 1 22  ? 27.829 13.432  28.010  1.00 35.93  ?  245 PRO A C   1 
ATOM   4301 O O   . PRO D 1 22  ? 28.467 12.399  27.792  1.00 33.55  ?  245 PRO A O   1 
ATOM   4302 C CB  . PRO D 1 22  ? 25.418 13.458  27.293  1.00 31.22  ?  245 PRO A CB  1 
ATOM   4303 C CG  . PRO D 1 22  ? 25.271 12.292  26.383  1.00 43.19  ?  245 PRO A CG  1 
ATOM   4304 C CD  . PRO D 1 22  ? 26.042 12.638  25.143  1.00 35.38  ?  245 PRO A CD  1 
ATOM   4305 N N   . LEU D 1 23  ? 27.965 14.144  29.125  1.00 39.76  ?  246 LEU A N   1 
ATOM   4306 C CA  . LEU D 1 23  ? 28.751 13.640  30.240  1.00 37.91  ?  246 LEU A CA  1 
ATOM   4307 C C   . LEU D 1 23  ? 28.019 12.490  30.921  1.00 37.76  ?  246 LEU A C   1 
ATOM   4308 O O   . LEU D 1 23  ? 26.786 12.442  30.956  1.00 38.46  ?  246 LEU A O   1 
ATOM   4309 C CB  . LEU D 1 23  ? 29.032 14.753  31.251  1.00 34.74  ?  246 LEU A CB  1 
ATOM   4310 C CG  . LEU D 1 23  ? 29.891 15.923  30.771  1.00 39.39  ?  246 LEU A CG  1 
ATOM   4311 C CD1 . LEU D 1 23  ? 30.011 16.981  31.860  1.00 35.11  ?  246 LEU A CD1 1 
ATOM   4312 C CD2 . LEU D 1 23  ? 31.265 15.441  30.333  1.00 36.17  ?  246 LEU A CD2 1 
ATOM   4313 N N   . GLU D 1 24  ? 28.791 11.555  31.461  1.00 33.23  ?  247 GLU A N   1 
ATOM   4314 C CA  . GLU D 1 24  ? 28.228 10.388  32.130  1.00 39.59  ?  247 GLU A CA  1 
ATOM   4315 C C   . GLU D 1 24  ? 28.585 10.307  33.604  1.00 38.71  ?  247 GLU A C   1 
ATOM   4316 O O   . GLU D 1 24  ? 27.740 9.918   34.415  1.00 37.91  ?  247 GLU A O   1 
ATOM   4317 C CB  . GLU D 1 24  ? 28.687 9.102   31.424  1.00 35.88  ?  247 GLU A CB  1 
ATOM   4318 C CG  . GLU D 1 24  ? 28.103 8.923   30.032  1.00 39.90  ?  247 GLU A CG  1 
ATOM   4319 C CD  . GLU D 1 24  ? 28.839 7.880   29.213  1.00 49.82  ?  247 GLU A CD  1 
ATOM   4320 O OE1 . GLU D 1 24  ? 29.396 6.934   29.813  1.00 50.01  ?  247 GLU A OE1 1 
ATOM   4321 O OE2 . GLU D 1 24  ? 28.862 8.008   27.970  1.00 53.58  ?  247 GLU A OE2 1 
ATOM   4322 N N   . LYS D 1 25  ? 29.808 10.666  33.980  1.00 35.77  ?  248 LYS A N   1 
ATOM   4323 C CA  . LYS D 1 25  ? 30.239 10.521  35.363  1.00 39.63  ?  248 LYS A CA  1 
ATOM   4324 C C   . LYS D 1 25  ? 31.461 11.394  35.597  1.00 37.27  ?  248 LYS A C   1 
ATOM   4325 O O   . LYS D 1 25  ? 32.082 11.898  34.659  1.00 37.60  ?  248 LYS A O   1 
ATOM   4326 C CB  . LYS D 1 25  ? 30.549 9.057   35.694  1.00 40.50  ?  248 LYS A CB  1 
ATOM   4327 C CG  . LYS D 1 25  ? 31.688 8.473   34.871  1.00 41.26  ?  248 LYS A CG  1 
ATOM   4328 C CD  . LYS D 1 25  ? 32.174 7.153   35.450  1.00 48.49  ?  248 LYS A CD  1 
ATOM   4329 C CE  . LYS D 1 25  ? 31.618 5.974   34.672  1.00 47.39  ?  248 LYS A CE  1 
ATOM   4330 N NZ  . LYS D 1 25  ? 31.665 6.219   33.204  1.00 49.44  ?  248 LYS A NZ  1 
ATOM   4331 N N   . LEU D 1 26  ? 31.794 11.569  36.871  1.00 39.35  ?  249 LEU A N   1 
ATOM   4332 C CA  . LEU D 1 26  ? 33.045 12.190  37.275  1.00 37.07  ?  249 LEU A CA  1 
ATOM   4333 C C   . LEU D 1 26  ? 34.063 11.096  37.564  1.00 38.47  ?  249 LEU A C   1 
ATOM   4334 O O   . LEU D 1 26  ? 33.710 10.024  38.067  1.00 36.27  ?  249 LEU A O   1 
ATOM   4335 C CB  . LEU D 1 26  ? 32.851 13.075  38.508  1.00 35.47  ?  249 LEU A CB  1 
ATOM   4336 C CG  . LEU D 1 26  ? 31.709 14.095  38.462  1.00 39.31  ?  249 LEU A CG  1 
ATOM   4337 C CD1 . LEU D 1 26  ? 31.404 14.625  39.854  1.00 40.23  ?  249 LEU A CD1 1 
ATOM   4338 C CD2 . LEU D 1 26  ? 32.054 15.235  37.523  1.00 35.94  ?  249 LEU A CD2 1 
ATOM   4339 N N   . PHE D 1 27  ? 35.325 11.363  37.236  1.00 38.55  ?  250 PHE A N   1 
ATOM   4340 C CA  . PHE D 1 27  ? 36.382 10.377  37.398  1.00 39.76  ?  250 PHE A CA  1 
ATOM   4341 C C   . PHE D 1 27  ? 37.657 11.068  37.854  1.00 40.51  ?  250 PHE A C   1 
ATOM   4342 O O   . PHE D 1 27  ? 38.004 12.140  37.353  1.00 40.18  ?  250 PHE A O   1 
ATOM   4343 C CB  . PHE D 1 27  ? 36.636 9.615   36.089  1.00 39.32  ?  250 PHE A CB  1 
ATOM   4344 C CG  . PHE D 1 27  ? 37.776 8.636   36.162  1.00 41.46  ?  250 PHE A CG  1 
ATOM   4345 C CD1 . PHE D 1 27  ? 37.602 7.394   36.751  1.00 45.33  ?  250 PHE A CD1 1 
ATOM   4346 C CD2 . PHE D 1 27  ? 39.017 8.954   35.634  1.00 40.87  ?  250 PHE A CD2 1 
ATOM   4347 C CE1 . PHE D 1 27  ? 38.647 6.487   36.815  1.00 47.48  ?  250 PHE A CE1 1 
ATOM   4348 C CE2 . PHE D 1 27  ? 40.066 8.054   35.697  1.00 42.18  ?  250 PHE A CE2 1 
ATOM   4349 C CZ  . PHE D 1 27  ? 39.880 6.819   36.287  1.00 46.74  ?  250 PHE A CZ  1 
ATOM   4350 N N   . THR D 1 28  ? 38.350 10.448  38.807  1.00 43.52  ?  251 THR A N   1 
ATOM   4351 C CA  . THR D 1 28  ? 39.635 10.940  39.275  1.00 42.86  ?  251 THR A CA  1 
ATOM   4352 C C   . THR D 1 28  ? 40.641 9.798   39.291  1.00 38.56  ?  251 THR A C   1 
ATOM   4353 O O   . THR D 1 28  ? 40.287 8.636   39.509  1.00 44.02  ?  251 THR A O   1 
ATOM   4354 C CB  . THR D 1 28  ? 39.533 11.579  40.673  1.00 42.00  ?  251 THR A CB  1 
ATOM   4355 O OG1 . THR D 1 28  ? 40.818 12.079  41.065  1.00 44.33  ?  251 THR A OG1 1 
ATOM   4356 C CG2 . THR D 1 28  ? 39.046 10.569  41.704  1.00 41.02  ?  251 THR A CG2 1 
ATOM   4357 N N   . GLY D 1 29  ? 41.900 10.144  39.043  1.00 41.93  ?  252 GLY A N   1 
ATOM   4358 C CA  . GLY D 1 29  ? 42.969 9.177   39.016  1.00 42.14  ?  252 GLY A CA  1 
ATOM   4359 C C   . GLY D 1 29  ? 44.316 9.847   38.848  1.00 42.96  ?  252 GLY A C   1 
ATOM   4360 O O   . GLY D 1 29  ? 44.406 11.048  38.575  1.00 43.08  ?  252 GLY A O   1 
ATOM   4361 N N   . PRO D 1 30  ? 45.394 9.084   39.022  1.00 46.01  ?  253 PRO A N   1 
ATOM   4362 C CA  . PRO D 1 30  ? 46.731 9.650   38.810  1.00 50.03  ?  253 PRO A CA  1 
ATOM   4363 C C   . PRO D 1 30  ? 46.949 10.003  37.347  1.00 47.92  ?  253 PRO A C   1 
ATOM   4364 O O   . PRO D 1 30  ? 46.492 9.300   36.444  1.00 51.84  ?  253 PRO A O   1 
ATOM   4365 C CB  . PRO D 1 30  ? 47.671 8.527   39.264  1.00 50.77  ?  253 PRO A CB  1 
ATOM   4366 C CG  . PRO D 1 30  ? 46.858 7.280   39.146  1.00 49.66  ?  253 PRO A CG  1 
ATOM   4367 C CD  . PRO D 1 30  ? 45.446 7.679   39.459  1.00 48.12  ?  253 PRO A CD  1 
ATOM   4368 N N   . SER D 1 31  ? 47.655 11.111  37.119  1.00 51.04  ?  254 SER A N   1 
ATOM   4369 C CA  . SER D 1 31  ? 47.888 11.619  35.772  1.00 54.28  ?  254 SER A CA  1 
ATOM   4370 C C   . SER D 1 31  ? 49.363 11.933  35.545  1.00 56.51  ?  254 SER A C   1 
ATOM   4371 O O   . SER D 1 31  ? 49.699 12.829  34.766  1.00 59.01  ?  254 SER A O   1 
ATOM   4372 C CB  . SER D 1 31  ? 47.028 12.853  35.502  1.00 50.21  ?  254 SER A CB  1 
ATOM   4373 O OG  . SER D 1 31  ? 46.959 13.687  36.646  1.00 54.90  ?  254 SER A OG  1 
ATOM   4374 N N   . SER D 1 32  ? 50.253 11.203  36.216  1.00 56.20  ?  255 SER A N   1 
ATOM   4375 C CA  . SER D 1 32  ? 51.687 11.396  36.042  1.00 58.91  ?  255 SER A CA  1 
ATOM   4376 C C   . SER D 1 32  ? 52.278 10.519  34.947  1.00 59.34  ?  255 SER A C   1 
ATOM   4377 O O   . SER D 1 32  ? 53.376 10.814  34.461  1.00 57.91  ?  255 SER A O   1 
ATOM   4378 C CB  . SER D 1 32  ? 52.419 11.122  37.360  1.00 64.07  ?  255 SER A CB  1 
ATOM   4379 O OG  . SER D 1 32  ? 51.950 9.928   37.966  1.00 65.28  ?  255 SER A OG  1 
ATOM   4380 N N   . ALA D 1 33  ? 51.579 9.459   34.547  1.00 55.46  ?  256 ALA A N   1 
ATOM   4381 C CA  . ALA D 1 33  ? 52.067 8.555   33.514  1.00 58.10  ?  256 ALA A CA  1 
ATOM   4382 C C   . ALA D 1 33  ? 51.813 9.063   32.101  1.00 57.56  ?  256 ALA A C   1 
ATOM   4383 O O   . ALA D 1 33  ? 52.234 8.407   31.143  1.00 59.84  ?  256 ALA A O   1 
ATOM   4384 C CB  . ALA D 1 33  ? 51.431 7.172   33.685  1.00 52.21  ?  256 ALA A CB  1 
ATOM   4385 N N   . PHE D 1 34  ? 51.142 10.203  31.942  1.00 57.17  ?  257 PHE A N   1 
ATOM   4386 C CA  . PHE D 1 34  ? 50.847 10.737  30.621  1.00 53.84  ?  257 PHE A CA  1 
ATOM   4387 C C   . PHE D 1 34  ? 50.768 12.254  30.702  1.00 51.90  ?  257 PHE A C   1 
ATOM   4388 O O   . PHE D 1 34  ? 50.711 12.840  31.786  1.00 55.28  ?  257 PHE A O   1 
ATOM   4389 C CB  . PHE D 1 34  ? 49.545 10.155  30.055  1.00 51.61  ?  257 PHE A CB  1 
ATOM   4390 C CG  . PHE D 1 34  ? 48.428 10.070  31.057  1.00 56.06  ?  257 PHE A CG  1 
ATOM   4391 C CD1 . PHE D 1 34  ? 47.568 11.139  31.252  1.00 51.29  ?  257 PHE A CD1 1 
ATOM   4392 C CD2 . PHE D 1 34  ? 48.232 8.917   31.800  1.00 56.21  ?  257 PHE A CD2 1 
ATOM   4393 C CE1 . PHE D 1 34  ? 46.536 11.059  32.172  1.00 52.08  ?  257 PHE A CE1 1 
ATOM   4394 C CE2 . PHE D 1 34  ? 47.205 8.833   32.722  1.00 53.85  ?  257 PHE A CE2 1 
ATOM   4395 C CZ  . PHE D 1 34  ? 46.356 9.905   32.906  1.00 54.74  ?  257 PHE A CZ  1 
ATOM   4396 N N   . VAL D 1 35  ? 50.763 12.888  29.533  1.00 53.46  ?  258 VAL A N   1 
ATOM   4397 C CA  . VAL D 1 35  ? 50.664 14.338  29.436  1.00 52.13  ?  258 VAL A CA  1 
ATOM   4398 C C   . VAL D 1 35  ? 49.199 14.699  29.229  1.00 48.57  ?  258 VAL A C   1 
ATOM   4399 O O   . VAL D 1 35  ? 48.564 14.244  28.271  1.00 51.71  ?  258 VAL A O   1 
ATOM   4400 C CB  . VAL D 1 35  ? 51.540 14.881  28.297  1.00 54.56  ?  258 VAL A CB  1 
ATOM   4401 C CG1 . VAL D 1 35  ? 50.974 16.193  27.764  1.00 52.07  ?  258 VAL A CG1 1 
ATOM   4402 C CG2 . VAL D 1 35  ? 52.970 15.069  28.773  1.00 59.57  ?  258 VAL A CG2 1 
ATOM   4403 N N   . VAL D 1 36  ? 48.658 15.504  30.137  1.00 45.55  ?  259 VAL A N   1 
ATOM   4404 C CA  . VAL D 1 36  ? 47.268 15.951  30.064  1.00 43.68  ?  259 VAL A CA  1 
ATOM   4405 C C   . VAL D 1 36  ? 47.303 17.335  29.426  1.00 42.38  ?  259 VAL A C   1 
ATOM   4406 O O   . VAL D 1 36  ? 47.412 18.357  30.106  1.00 39.71  ?  259 VAL A O   1 
ATOM   4407 C CB  . VAL D 1 36  ? 46.597 15.962  31.438  1.00 40.19  ?  259 VAL A CB  1 
ATOM   4408 C CG1 . VAL D 1 36  ? 45.142 16.391  31.321  1.00 35.74  ?  259 VAL A CG1 1 
ATOM   4409 C CG2 . VAL D 1 36  ? 46.701 14.593  32.089  1.00 44.71  ?  259 VAL A CG2 1 
ATOM   4410 N N   . GLN D 1 37  ? 47.212 17.370  28.098  1.00 39.17  ?  260 GLN A N   1 
ATOM   4411 C CA  . GLN D 1 37  ? 47.255 18.624  27.342  1.00 41.12  ?  260 GLN A CA  1 
ATOM   4412 C C   . GLN D 1 37  ? 46.204 18.607  26.238  1.00 42.50  ?  260 GLN A C   1 
ATOM   4413 O O   . GLN D 1 37  ? 46.529 18.637  25.046  1.00 41.91  ?  260 GLN A O   1 
ATOM   4414 C CB  . GLN D 1 37  ? 48.653 18.857  26.765  1.00 37.54  ?  260 GLN A CB  1 
ATOM   4415 C CG  . GLN D 1 37  ? 48.932 20.299  26.358  1.00 42.47  ?  260 GLN A CG  1 
ATOM   4416 C CD  . GLN D 1 37  ? 50.384 20.532  25.990  1.00 42.88  ?  260 GLN A CD  1 
ATOM   4417 O OE1 . GLN D 1 37  ? 51.153 19.585  25.809  1.00 46.47  ?  260 GLN A OE1 1 
ATOM   4418 N NE2 . GLN D 1 37  ? 50.768 21.798  25.869  1.00 38.04  ?  260 GLN A NE2 1 
ATOM   4419 N N   . PRO D 1 38  ? 44.923 18.570  26.601  1.00 40.95  ?  261 PRO A N   1 
ATOM   4420 C CA  . PRO D 1 38  ? 43.878 18.674  25.581  1.00 37.97  ?  261 PRO A CA  1 
ATOM   4421 C C   . PRO D 1 38  ? 43.735 20.109  25.100  1.00 39.66  ?  261 PRO A C   1 
ATOM   4422 O O   . PRO D 1 38  ? 44.019 21.065  25.824  1.00 38.41  ?  261 PRO A O   1 
ATOM   4423 C CB  . PRO D 1 38  ? 42.619 18.206  26.319  1.00 41.09  ?  261 PRO A CB  1 
ATOM   4424 C CG  . PRO D 1 38  ? 42.864 18.609  27.728  1.00 35.25  ?  261 PRO A CG  1 
ATOM   4425 C CD  . PRO D 1 38  ? 44.353 18.486  27.959  1.00 38.72  ?  261 PRO A CD  1 
ATOM   4426 N N   . GLN D 1 39  ? 43.301 20.249  23.848  1.00 33.95  ?  262 GLN A N   1 
ATOM   4427 C CA  . GLN D 1 39  ? 43.128 21.566  23.251  1.00 35.17  ?  262 GLN A CA  1 
ATOM   4428 C C   . GLN D 1 39  ? 41.676 22.016  23.205  1.00 36.76  ?  262 GLN A C   1 
ATOM   4429 O O   . GLN D 1 39  ? 41.418 23.223  23.113  1.00 40.30  ?  262 GLN A O   1 
ATOM   4430 C CB  . GLN D 1 39  ? 43.717 21.592  21.836  1.00 36.46  ?  262 GLN A CB  1 
ATOM   4431 C CG  . GLN D 1 39  ? 45.232 21.460  21.808  1.00 41.54  ?  262 GLN A CG  1 
ATOM   4432 C CD  . GLN D 1 39  ? 45.911 22.285  22.887  1.00 42.23  ?  262 GLN A CD  1 
ATOM   4433 O OE1 . GLN D 1 39  ? 45.906 23.516  22.840  1.00 39.65  ?  262 GLN A OE1 1 
ATOM   4434 N NE2 . GLN D 1 39  ? 46.498 21.609  23.867  1.00 40.12  ?  262 GLN A NE2 1 
ATOM   4435 N N   . ASN D 1 40  ? 40.729 21.085  23.264  1.00 34.99  ?  263 ASN A N   1 
ATOM   4436 C CA  . ASN D 1 40  ? 39.323 21.425  23.394  1.00 34.55  ?  263 ASN A CA  1 
ATOM   4437 C C   . ASN D 1 40  ? 38.927 21.418  24.865  1.00 35.72  ?  263 ASN A C   1 
ATOM   4438 O O   . ASN D 1 40  ? 39.546 20.745  25.693  1.00 35.90  ?  263 ASN A O   1 
ATOM   4439 C CB  . ASN D 1 40  ? 38.453 20.449  22.601  1.00 33.85  ?  263 ASN A CB  1 
ATOM   4440 C CG  . ASN D 1 40  ? 38.567 20.656  21.101  1.00 38.36  ?  263 ASN A CG  1 
ATOM   4441 O OD1 . ASN D 1 40  ? 38.549 21.790  20.616  1.00 34.99  ?  263 ASN A OD1 1 
ATOM   4442 N ND2 . ASN D 1 40  ? 38.687 19.560  20.357  1.00 33.05  ?  263 ASN A ND2 1 
ATOM   4443 N N   . GLY D 1 41  ? 37.889 22.185  25.187  1.00 37.42  ?  264 GLY A N   1 
ATOM   4444 C CA  . GLY D 1 41  ? 37.478 22.317  26.571  1.00 34.11  ?  264 GLY A CA  1 
ATOM   4445 C C   . GLY D 1 41  ? 38.464 23.060  27.441  1.00 39.96  ?  264 GLY A C   1 
ATOM   4446 O O   . GLY D 1 41  ? 38.607 22.736  28.624  1.00 31.59  ?  264 GLY A O   1 
ATOM   4447 N N   . ARG D 1 42  ? 39.157 24.050  26.884  1.00 34.72  ?  265 ARG A N   1 
ATOM   4448 C CA  . ARG D 1 42  ? 40.133 24.848  27.613  1.00 38.47  ?  265 ARG A CA  1 
ATOM   4449 C C   . ARG D 1 42  ? 39.623 26.279  27.700  1.00 38.29  ?  265 ARG A C   1 
ATOM   4450 O O   . ARG D 1 42  ? 39.417 26.932  26.670  1.00 38.37  ?  265 ARG A O   1 
ATOM   4451 C CB  . ARG D 1 42  ? 41.499 24.801  26.926  1.00 37.21  ?  265 ARG A CB  1 
ATOM   4452 C CG  . ARG D 1 42  ? 42.061 23.398  26.779  1.00 34.52  ?  265 ARG A CG  1 
ATOM   4453 C CD  . ARG D 1 42  ? 42.203 22.719  28.132  1.00 38.59  ?  265 ARG A CD  1 
ATOM   4454 N NE  . ARG D 1 42  ? 43.188 23.391  28.969  1.00 39.89  ?  265 ARG A NE  1 
ATOM   4455 C CZ  . ARG D 1 42  ? 44.490 23.142  28.938  1.00 40.87  ?  265 ARG A CZ  1 
ATOM   4456 N NH1 . ARG D 1 42  ? 45.000 22.225  28.132  1.00 39.35  ?  265 ARG A NH1 1 
ATOM   4457 N NH2 . ARG D 1 42  ? 45.302 23.833  29.733  1.00 39.84  ?  265 ARG A NH2 1 
ATOM   4458 N N   . CYS D 1 43  ? 39.419 26.762  28.925  1.00 38.47  ?  266 CYS A N   1 
ATOM   4459 C CA  . CYS D 1 43  ? 38.889 28.102  29.140  1.00 39.94  ?  266 CYS A CA  1 
ATOM   4460 C C   . CYS D 1 43  ? 39.200 28.531  30.564  1.00 44.08  ?  266 CYS A C   1 
ATOM   4461 O O   . CYS D 1 43  ? 38.947 27.777  31.508  1.00 37.63  ?  266 CYS A O   1 
ATOM   4462 C CB  . CYS D 1 43  ? 37.377 28.141  28.889  1.00 41.86  ?  266 CYS A CB  1 
ATOM   4463 S SG  . CYS D 1 43  ? 36.598 29.745  29.193  1.00 45.86  ?  266 CYS A SG  1 
ATOM   4464 N N   . THR D 1 44  ? 39.748 29.734  30.717  1.00 41.73  ?  267 THR A N   1 
ATOM   4465 C CA  . THR D 1 44  ? 40.017 30.256  32.049  1.00 40.33  ?  267 THR A CA  1 
ATOM   4466 C C   . THR D 1 44  ? 38.712 30.642  32.740  1.00 37.04  ?  267 THR A C   1 
ATOM   4467 O O   . THR D 1 44  ? 37.664 30.802  32.106  1.00 38.21  ?  267 THR A O   1 
ATOM   4468 C CB  . THR D 1 44  ? 40.955 31.462  31.980  1.00 39.77  ?  267 THR A CB  1 
ATOM   4469 O OG1 . THR D 1 44  ? 40.290 32.554  31.332  1.00 42.33  ?  267 THR A OG1 1 
ATOM   4470 C CG2 . THR D 1 44  ? 42.219 31.111  31.206  1.00 37.87  ?  267 THR A CG2 1 
ATOM   4471 N N   . THR D 1 45  ? 38.785 30.790  34.065  1.00 37.60  ?  268 THR A N   1 
ATOM   4472 C CA  . THR D 1 45  ? 37.593 31.119  34.838  1.00 41.76  ?  268 THR A CA  1 
ATOM   4473 C C   . THR D 1 45  ? 37.023 32.486  34.478  1.00 41.91  ?  268 THR A C   1 
ATOM   4474 O O   . THR D 1 45  ? 35.828 32.718  34.690  1.00 41.88  ?  268 THR A O   1 
ATOM   4475 C CB  . THR D 1 45  ? 37.896 31.056  36.337  1.00 43.65  ?  268 THR A CB  1 
ATOM   4476 O OG1 . THR D 1 45  ? 38.995 31.924  36.645  1.00 45.76  ?  268 THR A OG1 1 
ATOM   4477 C CG2 . THR D 1 45  ? 38.247 29.632  36.751  1.00 40.81  ?  268 THR A CG2 1 
ATOM   4478 N N   . ASP D 1 46  ? 37.837 33.389  33.936  1.00 38.78  ?  269 ASP A N   1 
ATOM   4479 C CA  . ASP D 1 46  ? 37.355 34.699  33.519  1.00 46.92  ?  269 ASP A CA  1 
ATOM   4480 C C   . ASP D 1 46  ? 36.937 34.737  32.052  1.00 52.19  ?  269 ASP A C   1 
ATOM   4481 O O   . ASP D 1 46  ? 36.627 35.817  31.538  1.00 55.61  ?  269 ASP A O   1 
ATOM   4482 C CB  . ASP D 1 46  ? 38.411 35.775  33.800  1.00 50.88  ?  269 ASP A CB  1 
ATOM   4483 C CG  . ASP D 1 46  ? 39.812 35.336  33.426  1.00 57.53  ?  269 ASP A CG  1 
ATOM   4484 O OD1 . ASP D 1 46  ? 39.993 34.765  32.332  1.00 54.77  ?  269 ASP A OD1 1 
ATOM   4485 O OD2 . ASP D 1 46  ? 40.735 35.568  34.235  1.00 70.34  ?  269 ASP A OD2 1 
ATOM   4486 N N   . GLY D 1 47  ? 36.929 33.596  31.372  1.00 44.84  ?  270 GLY A N   1 
ATOM   4487 C CA  . GLY D 1 47  ? 36.334 33.493  30.057  1.00 43.76  ?  270 GLY A CA  1 
ATOM   4488 C C   . GLY D 1 47  ? 37.266 33.584  28.869  1.00 44.52  ?  270 GLY A C   1 
ATOM   4489 O O   . GLY D 1 47  ? 36.796 33.885  27.767  1.00 44.75  ?  270 GLY A O   1 
ATOM   4490 N N   . VAL D 1 48  ? 38.558 33.331  29.048  1.00 44.40  ?  271 VAL A N   1 
ATOM   4491 C CA  . VAL D 1 48  ? 39.505 33.341  27.937  1.00 45.44  ?  271 VAL A CA  1 
ATOM   4492 C C   . VAL D 1 48  ? 39.612 31.918  27.399  1.00 47.12  ?  271 VAL A C   1 
ATOM   4493 O O   . VAL D 1 48  ? 40.101 31.018  28.088  1.00 43.59  ?  271 VAL A O   1 
ATOM   4494 C CB  . VAL D 1 48  ? 40.876 33.877  28.365  1.00 44.87  ?  271 VAL A CB  1 
ATOM   4495 C CG1 . VAL D 1 48  ? 41.816 33.931  27.168  1.00 43.72  ?  271 VAL A CG1 1 
ATOM   4496 C CG2 . VAL D 1 48  ? 40.733 35.253  28.998  1.00 45.02  ?  271 VAL A CG2 1 
ATOM   4497 N N   . LEU D 1 49  ? 39.149 31.712  26.168  1.00 45.86  ?  272 LEU A N   1 
ATOM   4498 C CA  . LEU D 1 49  ? 39.277 30.406  25.537  1.00 41.98  ?  272 LEU A CA  1 
ATOM   4499 C C   . LEU D 1 49  ? 40.723 30.159  25.124  1.00 41.57  ?  272 LEU A C   1 
ATOM   4500 O O   . LEU D 1 49  ? 41.412 31.060  24.636  1.00 44.08  ?  272 LEU A O   1 
ATOM   4501 C CB  . LEU D 1 49  ? 38.360 30.300  24.320  1.00 42.76  ?  272 LEU A CB  1 
ATOM   4502 C CG  . LEU D 1 49  ? 36.900 30.732  24.481  1.00 47.44  ?  272 LEU A CG  1 
ATOM   4503 C CD1 . LEU D 1 49  ? 36.141 30.536  23.177  1.00 49.39  ?  272 LEU A CD1 1 
ATOM   4504 C CD2 . LEU D 1 49  ? 36.228 29.977  25.615  1.00 42.32  ?  272 LEU A CD2 1 
ATOM   4505 N N   . LEU D 1 50  ? 41.184 28.928  25.328  1.00 36.15  ?  273 LEU A N   1 
ATOM   4506 C CA  . LEU D 1 50  ? 42.545 28.533  25.008  1.00 38.96  ?  273 LEU A CA  1 
ATOM   4507 C C   . LEU D 1 50  ? 42.533 27.393  23.999  1.00 37.65  ?  273 LEU A C   1 
ATOM   4508 O O   . LEU D 1 50  ? 41.511 26.732  23.787  1.00 33.37  ?  273 LEU A O   1 
ATOM   4509 C CB  . LEU D 1 50  ? 43.311 28.109  26.268  1.00 38.50  ?  273 LEU A CB  1 
ATOM   4510 C CG  . LEU D 1 50  ? 43.067 28.939  27.529  1.00 42.54  ?  273 LEU A CG  1 
ATOM   4511 C CD1 . LEU D 1 50  ? 43.598 28.219  28.757  1.00 38.59  ?  273 LEU A CD1 1 
ATOM   4512 C CD2 . LEU D 1 50  ? 43.696 30.319  27.397  1.00 43.24  ?  273 LEU A CD2 1 
ATOM   4513 N N   . GLY D 1 51  ? 43.689 27.171  23.378  1.00 39.77  ?  274 GLY A N   1 
ATOM   4514 C CA  . GLY D 1 51  ? 43.830 26.064  22.445  1.00 38.28  ?  274 GLY A CA  1 
ATOM   4515 C C   . GLY D 1 51  ? 42.902 26.206  21.256  1.00 41.09  ?  274 GLY A C   1 
ATOM   4516 O O   . GLY D 1 51  ? 42.787 27.276  20.648  1.00 42.58  ?  274 GLY A O   1 
ATOM   4517 N N   . THR D 1 52  ? 42.231 25.107  20.911  1.00 33.88  ?  275 THR A N   1 
ATOM   4518 C CA  . THR D 1 52  ? 41.265 25.081  19.821  1.00 37.20  ?  275 THR A CA  1 
ATOM   4519 C C   . THR D 1 52  ? 39.826 25.134  20.323  1.00 34.25  ?  275 THR A C   1 
ATOM   4520 O O   . THR D 1 52  ? 38.908 24.729  19.603  1.00 40.07  ?  275 THR A O   1 
ATOM   4521 C CB  . THR D 1 52  ? 41.472 23.834  18.958  1.00 37.82  ?  275 THR A CB  1 
ATOM   4522 O OG1 . THR D 1 52  ? 41.285 22.660  19.759  1.00 36.90  ?  275 THR A OG1 1 
ATOM   4523 C CG2 . THR D 1 52  ? 42.875 23.818  18.370  1.00 37.50  ?  275 THR A CG2 1 
ATOM   4524 N N   . THR D 1 53  ? 39.614 25.627  21.539  1.00 34.08  ?  276 THR A N   1 
ATOM   4525 C CA  . THR D 1 53  ? 38.289 25.619  22.143  1.00 38.25  ?  276 THR A CA  1 
ATOM   4526 C C   . THR D 1 53  ? 37.412 26.703  21.528  1.00 40.13  ?  276 THR A C   1 
ATOM   4527 O O   . THR D 1 53  ? 37.828 27.860  21.410  1.00 39.50  ?  276 THR A O   1 
ATOM   4528 C CB  . THR D 1 53  ? 38.393 25.819  23.657  1.00 34.98  ?  276 THR A CB  1 
ATOM   4529 O OG1 . THR D 1 53  ? 39.160 24.753  24.231  1.00 37.05  ?  276 THR A OG1 1 
ATOM   4530 C CG2 . THR D 1 53  ? 37.010 25.837  24.292  1.00 35.74  ?  276 THR A CG2 1 
ATOM   4531 N N   . GLN D 1 54  ? 36.205 26.321  21.124  1.00 37.60  ?  277 GLN A N   1 
ATOM   4532 C CA  . GLN D 1 54  ? 35.167 27.254  20.713  1.00 37.93  ?  277 GLN A CA  1 
ATOM   4533 C C   . GLN D 1 54  ? 33.913 26.978  21.546  1.00 38.89  ?  277 GLN A C   1 
ATOM   4534 O O   . GLN D 1 54  ? 33.933 26.177  22.484  1.00 33.98  ?  277 GLN A O   1 
ATOM   4535 C CB  . GLN D 1 54  ? 34.904 27.150  19.208  1.00 40.36  ?  277 GLN A CB  1 
ATOM   4536 C CG  . GLN D 1 54  ? 34.859 25.734  18.672  1.00 38.93  ?  277 GLN A CG  1 
ATOM   4537 C CD  . GLN D 1 54  ? 33.468 25.147  18.736  1.00 39.39  ?  277 GLN A CD  1 
ATOM   4538 O OE1 . GLN D 1 54  ? 32.534 25.670  18.129  1.00 43.67  ?  277 GLN A OE1 1 
ATOM   4539 N NE2 . GLN D 1 54  ? 33.320 24.057  19.480  1.00 39.03  ?  277 GLN A NE2 1 
ATOM   4540 N N   . LEU D 1 55  ? 32.814 27.649  21.201  1.00 37.37  ?  278 LEU A N   1 
ATOM   4541 C CA  . LEU D 1 55  ? 31.642 27.666  22.068  1.00 36.72  ?  278 LEU A CA  1 
ATOM   4542 C C   . LEU D 1 55  ? 30.550 26.681  21.668  1.00 42.03  ?  278 LEU A C   1 
ATOM   4543 O O   . LEU D 1 55  ? 29.711 26.344  22.510  1.00 47.26  ?  278 LEU A O   1 
ATOM   4544 C CB  . LEU D 1 55  ? 31.046 29.079  22.118  1.00 40.10  ?  278 LEU A CB  1 
ATOM   4545 C CG  . LEU D 1 55  ? 31.877 30.106  22.890  1.00 42.96  ?  278 LEU A CG  1 
ATOM   4546 C CD1 . LEU D 1 55  ? 31.570 31.516  22.415  1.00 46.80  ?  278 LEU A CD1 1 
ATOM   4547 C CD2 . LEU D 1 55  ? 31.634 29.975  24.385  1.00 35.57  ?  278 LEU A CD2 1 
ATOM   4548 N N   . SER D 1 56  ? 30.533 26.216  20.424  1.00 41.41  ?  279 SER A N   1 
ATOM   4549 C CA  . SER D 1 56  ? 29.473 25.319  19.976  1.00 43.34  ?  279 SER A CA  1 
ATOM   4550 C C   . SER D 1 56  ? 29.751 23.895  20.448  1.00 44.49  ?  279 SER A C   1 
ATOM   4551 O O   . SER D 1 56  ? 30.798 23.334  20.107  1.00 44.97  ?  279 SER A O   1 
ATOM   4552 C CB  . SER D 1 56  ? 29.349 25.347  18.459  1.00 41.02  ?  279 SER A CB  1 
ATOM   4553 O OG  . SER D 1 56  ? 28.239 24.577  18.029  1.00 45.77  ?  279 SER A OG  1 
ATOM   4554 N N   . PRO D 1 57  ? 28.850 23.278  21.217  1.00 41.23  ?  280 PRO A N   1 
ATOM   4555 C CA  . PRO D 1 57  ? 29.083 21.889  21.646  1.00 39.33  ?  280 PRO A CA  1 
ATOM   4556 C C   . PRO D 1 57  ? 28.938 20.878  20.525  1.00 43.47  ?  280 PRO A C   1 
ATOM   4557 O O   . PRO D 1 57  ? 29.502 19.782  20.630  1.00 44.80  ?  280 PRO A O   1 
ATOM   4558 C CB  . PRO D 1 57  ? 28.015 21.674  22.726  1.00 40.82  ?  280 PRO A CB  1 
ATOM   4559 C CG  . PRO D 1 57  ? 26.912 22.603  22.332  1.00 42.78  ?  280 PRO A CG  1 
ATOM   4560 C CD  . PRO D 1 57  ? 27.574 23.811  21.726  1.00 42.41  ?  280 PRO A CD  1 
ATOM   4561 N N   . VAL D 1 58  ? 28.202 21.204  19.462  1.00 41.65  ?  281 VAL A N   1 
ATOM   4562 C CA  . VAL D 1 58  ? 28.004 20.263  18.366  1.00 41.47  ?  281 VAL A CA  1 
ATOM   4563 C C   . VAL D 1 58  ? 29.047 20.410  17.264  1.00 43.23  ?  281 VAL A C   1 
ATOM   4564 O O   . VAL D 1 58  ? 29.227 19.479  16.467  1.00 43.31  ?  281 VAL A O   1 
ATOM   4565 C CB  . VAL D 1 58  ? 26.597 20.411  17.758  1.00 40.68  ?  281 VAL A CB  1 
ATOM   4566 C CG1 . VAL D 1 58  ? 25.535 20.083  18.795  1.00 38.66  ?  281 VAL A CG1 1 
ATOM   4567 C CG2 . VAL D 1 58  ? 26.402 21.815  17.207  1.00 36.80  ?  281 VAL A CG2 1 
ATOM   4568 N N   . ASN D 1 59  ? 29.738 21.548  17.195  1.00 36.84  ?  282 ASN A N   1 
ATOM   4569 C CA  . ASN D 1 59  ? 30.767 21.778  16.194  1.00 35.54  ?  282 ASN A CA  1 
ATOM   4570 C C   . ASN D 1 59  ? 32.130 21.251  16.621  1.00 40.19  ?  282 ASN A C   1 
ATOM   4571 O O   . ASN D 1 59  ? 33.154 21.710  16.103  1.00 43.41  ?  282 ASN A O   1 
ATOM   4572 C CB  . ASN D 1 59  ? 30.857 23.269  15.868  1.00 42.53  ?  282 ASN A CB  1 
ATOM   4573 C CG  . ASN D 1 59  ? 29.935 23.670  14.741  1.00 45.94  ?  282 ASN A CG  1 
ATOM   4574 O OD1 . ASN D 1 59  ? 29.354 22.821  14.064  1.00 51.99  ?  282 ASN A OD1 1 
ATOM   4575 N ND2 . ASN D 1 59  ? 29.778 24.971  14.543  1.00 50.63  ?  282 ASN A ND2 1 
ATOM   4576 N N   . ILE D 1 60  ? 32.164 20.308  17.556  1.00 38.68  ?  283 ILE A N   1 
ATOM   4577 C CA  . ILE D 1 60  ? 33.406 19.674  17.980  1.00 34.96  ?  283 ILE A CA  1 
ATOM   4578 C C   . ILE D 1 60  ? 33.605 18.413  17.151  1.00 35.55  ?  283 ILE A C   1 
ATOM   4579 O O   . ILE D 1 60  ? 32.685 17.596  17.018  1.00 34.33  ?  283 ILE A O   1 
ATOM   4580 C CB  . ILE D 1 60  ? 33.376 19.358  19.485  1.00 35.64  ?  283 ILE A CB  1 
ATOM   4581 C CG1 . ILE D 1 60  ? 33.240 20.649  20.293  1.00 34.33  ?  283 ILE A CG1 1 
ATOM   4582 C CG2 . ILE D 1 60  ? 34.629 18.602  19.898  1.00 31.64  ?  283 ILE A CG2 1 
ATOM   4583 C CD1 . ILE D 1 60  ? 32.594 20.462  21.651  1.00 34.69  ?  283 ILE A CD1 1 
ATOM   4584 N N   . CYS D 1 61  ? 34.800 18.267  16.576  1.00 33.70  ?  284 CYS A N   1 
ATOM   4585 C CA  . CYS D 1 61  ? 35.168 17.144  15.715  1.00 39.46  ?  284 CYS A CA  1 
ATOM   4586 C C   . CYS D 1 61  ? 34.367 17.112  14.416  1.00 40.69  ?  284 CYS A C   1 
ATOM   4587 O O   . CYS D 1 61  ? 34.236 16.053  13.791  1.00 39.38  ?  284 CYS A O   1 
ATOM   4588 C CB  . CYS D 1 61  ? 35.041 15.804  16.451  1.00 37.34  ?  284 CYS A CB  1 
ATOM   4589 S SG  . CYS D 1 61  ? 36.282 15.545  17.740  1.00 40.90  ?  284 CYS A SG  1 
ATOM   4590 N N   . THR D 1 62  ? 33.824 18.250  13.995  1.00 39.33  ?  285 THR A N   1 
ATOM   4591 C CA  . THR D 1 62  ? 33.181 18.381  12.696  1.00 39.51  ?  285 THR A CA  1 
ATOM   4592 C C   . THR D 1 62  ? 34.119 19.089  11.728  1.00 38.35  ?  285 THR A C   1 
ATOM   4593 O O   . THR D 1 62  ? 34.991 19.861  12.134  1.00 35.62  ?  285 THR A O   1 
ATOM   4594 C CB  . THR D 1 62  ? 31.865 19.157  12.792  1.00 38.05  ?  285 THR A CB  1 
ATOM   4595 O OG1 . THR D 1 62  ? 32.133 20.509  13.184  1.00 44.82  ?  285 THR A OG1 1 
ATOM   4596 C CG2 . THR D 1 62  ? 30.935 18.515  13.807  1.00 35.11  ?  285 THR A CG2 1 
ATOM   4597 N N   . PHE D 1 63  ? 33.933 18.815  10.438  1.00 33.34  ?  286 PHE A N   1 
ATOM   4598 C CA  . PHE D 1 63  ? 34.723 19.433  9.384   1.00 31.58  ?  286 PHE A CA  1 
ATOM   4599 C C   . PHE D 1 63  ? 33.802 19.912  8.274   1.00 34.25  ?  286 PHE A C   1 
ATOM   4600 O O   . PHE D 1 63  ? 32.785 19.282  7.975   1.00 31.60  ?  286 PHE A O   1 
ATOM   4601 C CB  . PHE D 1 63  ? 35.759 18.465  8.803   1.00 34.60  ?  286 PHE A CB  1 
ATOM   4602 C CG  . PHE D 1 63  ? 36.750 17.952  9.810   1.00 35.84  ?  286 PHE A CG  1 
ATOM   4603 C CD1 . PHE D 1 63  ? 37.919 18.649  10.071  1.00 33.86  ?  286 PHE A CD1 1 
ATOM   4604 C CD2 . PHE D 1 63  ? 36.520 16.764  10.484  1.00 33.20  ?  286 PHE A CD2 1 
ATOM   4605 C CE1 . PHE D 1 63  ? 38.836 18.173  10.989  1.00 31.80  ?  286 PHE A CE1 1 
ATOM   4606 C CE2 . PHE D 1 63  ? 37.431 16.285  11.404  1.00 35.74  ?  286 PHE A CE2 1 
ATOM   4607 C CZ  . PHE D 1 63  ? 38.590 16.991  11.657  1.00 35.69  ?  286 PHE A CZ  1 
ATOM   4608 N N   . ARG D 1 64  ? 34.175 21.037  7.662   1.00 36.22  ?  287 ARG A N   1 
ATOM   4609 C CA  . ARG D 1 64  ? 33.414 21.624  6.569   1.00 36.88  ?  287 ARG A CA  1 
ATOM   4610 C C   . ARG D 1 64  ? 34.368 22.087  5.478   1.00 37.81  ?  287 ARG A C   1 
ATOM   4611 O O   . ARG D 1 64  ? 35.468 22.568  5.767   1.00 37.97  ?  287 ARG A O   1 
ATOM   4612 C CB  . ARG D 1 64  ? 32.565 22.807  7.049   1.00 37.21  ?  287 ARG A CB  1 
ATOM   4613 C CG  . ARG D 1 64  ? 31.354 22.401  7.866   1.00 40.87  ?  287 ARG A CG  1 
ATOM   4614 C CD  . ARG D 1 64  ? 30.578 23.614  8.345   1.00 39.45  ?  287 ARG A CD  1 
ATOM   4615 N NE  . ARG D 1 64  ? 29.417 23.232  9.139   1.00 41.85  ?  287 ARG A NE  1 
ATOM   4616 C CZ  . ARG D 1 64  ? 29.470 22.843  10.406  1.00 44.39  ?  287 ARG A CZ  1 
ATOM   4617 N NH1 . ARG D 1 64  ? 30.616 22.784  11.065  1.00 40.15  ?  287 ARG A NH1 1 
ATOM   4618 N NH2 . ARG D 1 64  ? 28.344 22.505  11.027  1.00 39.34  ?  287 ARG A NH2 1 
ATOM   4619 N N   . GLY D 1 65  ? 33.939 21.942  4.231   1.00 35.12  ?  288 GLY A N   1 
ATOM   4620 C CA  . GLY D 1 65  ? 34.740 22.380  3.096   1.00 34.75  ?  288 GLY A CA  1 
ATOM   4621 C C   . GLY D 1 65  ? 34.268 21.710  1.814   1.00 36.84  ?  288 GLY A C   1 
ATOM   4622 O O   . GLY D 1 65  ? 33.100 21.342  1.685   1.00 34.88  ?  288 GLY A O   1 
ATOM   4623 N N   . ASP D 1 66  ? 35.203 21.580  0.875   1.00 37.87  ?  289 ASP A N   1 
ATOM   4624 C CA  . ASP D 1 66  ? 34.978 20.875  -0.379  1.00 42.09  ?  289 ASP A CA  1 
ATOM   4625 C C   . ASP D 1 66  ? 35.983 19.737  -0.500  1.00 39.01  ?  289 ASP A C   1 
ATOM   4626 O O   . ASP D 1 66  ? 37.073 19.788  0.077   1.00 41.92  ?  289 ASP A O   1 
ATOM   4627 C CB  . ASP D 1 66  ? 35.092 21.821  -1.584  1.00 38.99  ?  289 ASP A CB  1 
ATOM   4628 C CG  . ASP D 1 66  ? 36.478 22.421  -1.728  1.00 45.91  ?  289 ASP A CG  1 
ATOM   4629 O OD1 . ASP D 1 66  ? 37.328 21.809  -2.410  1.00 48.09  ?  289 ASP A OD1 1 
ATOM   4630 O OD2 . ASP D 1 66  ? 36.718 23.506  -1.156  1.00 51.28  ?  289 ASP A OD2 1 
ATOM   4631 N N   . VAL D 1 67  ? 35.610 18.705  -1.255  1.00 40.42  ?  290 VAL A N   1 
ATOM   4632 C CA  . VAL D 1 67  ? 36.377 17.466  -1.318  1.00 46.20  ?  290 VAL A CA  1 
ATOM   4633 C C   . VAL D 1 67  ? 36.853 17.226  -2.745  1.00 42.97  ?  290 VAL A C   1 
ATOM   4634 O O   . VAL D 1 67  ? 36.119 17.466  -3.708  1.00 40.17  ?  290 VAL A O   1 
ATOM   4635 C CB  . VAL D 1 67  ? 35.551 16.263  -0.814  1.00 43.43  ?  290 VAL A CB  1 
ATOM   4636 C CG1 . VAL D 1 67  ? 35.436 16.297  0.706   1.00 38.25  ?  290 VAL A CG1 1 
ATOM   4637 C CG2 . VAL D 1 67  ? 34.173 16.248  -1.460  1.00 41.76  ?  290 VAL A CG2 1 
ATOM   4638 N N   . THR D 1 68  ? 38.094 16.758  -2.866  1.00 44.13  ?  291 THR A N   1 
ATOM   4639 C CA  . THR D 1 68  ? 38.646 16.239  -4.107  1.00 46.62  ?  291 THR A CA  1 
ATOM   4640 C C   . THR D 1 68  ? 39.301 14.896  -3.812  1.00 47.76  ?  291 THR A C   1 
ATOM   4641 O O   . THR D 1 68  ? 39.577 14.561  -2.657  1.00 45.06  ?  291 THR A O   1 
ATOM   4642 C CB  . THR D 1 68  ? 39.673 17.195  -4.737  1.00 50.36  ?  291 THR A CB  1 
ATOM   4643 O OG1 . THR D 1 68  ? 40.805 17.326  -3.867  1.00 52.75  ?  291 THR A OG1 1 
ATOM   4644 C CG2 . THR D 1 68  ? 39.061 18.570  -4.980  1.00 44.05  ?  291 THR A CG2 1 
ATOM   4645 N N   . HIS D 1 69  ? 39.551 14.121  -4.865  1.00 50.37  ?  292 HIS A N   1 
ATOM   4646 C CA  . HIS D 1 69  ? 40.173 12.818  -4.682  1.00 52.47  ?  292 HIS A CA  1 
ATOM   4647 C C   . HIS D 1 69  ? 40.824 12.377  -5.984  1.00 59.59  ?  292 HIS A C   1 
ATOM   4648 O O   . HIS D 1 69  ? 40.531 12.906  -7.060  1.00 58.96  ?  292 HIS A O   1 
ATOM   4649 C CB  . HIS D 1 69  ? 39.159 11.768  -4.213  1.00 55.52  ?  292 HIS A CB  1 
ATOM   4650 C CG  . HIS D 1 69  ? 38.360 11.160  -5.324  1.00 59.40  ?  292 HIS A CG  1 
ATOM   4651 N ND1 . HIS D 1 69  ? 37.760 11.915  -6.310  1.00 56.85  ?  292 HIS A ND1 1 
ATOM   4652 C CD2 . HIS D 1 69  ? 38.058 9.870   -5.602  1.00 58.46  ?  292 HIS A CD2 1 
ATOM   4653 C CE1 . HIS D 1 69  ? 37.127 11.116  -7.150  1.00 62.45  ?  292 HIS A CE1 1 
ATOM   4654 N NE2 . HIS D 1 69  ? 37.291 9.870   -6.743  1.00 60.51  ?  292 HIS A NE2 1 
ATOM   4655 N N   . ILE D 1 70  ? 41.712 11.396  -5.864  1.00 65.01  ?  293 ILE A N   1 
ATOM   4656 C CA  . ILE D 1 70  ? 42.335 10.772  -7.024  1.00 66.28  ?  293 ILE A CA  1 
ATOM   4657 C C   . ILE D 1 70  ? 41.345 9.797   -7.644  1.00 67.02  ?  293 ILE A C   1 
ATOM   4658 O O   . ILE D 1 70  ? 40.654 9.056   -6.934  1.00 67.26  ?  293 ILE A O   1 
ATOM   4659 C CB  . ILE D 1 70  ? 43.645 10.066  -6.625  1.00 67.17  ?  293 ILE A CB  1 
ATOM   4660 C CG1 . ILE D 1 70  ? 44.559 11.010  -5.835  1.00 67.64  ?  293 ILE A CG1 1 
ATOM   4661 C CG2 . ILE D 1 70  ? 44.365 9.525   -7.854  1.00 66.54  ?  293 ILE A CG2 1 
ATOM   4662 C CD1 . ILE D 1 70  ? 44.470 10.841  -4.327  1.00 69.85  ?  293 ILE A CD1 1 
ATOM   4663 N N   . THR D 1 71  ? 41.262 9.804   -8.976  1.00 69.44  ?  294 THR A N   1 
ATOM   4664 C CA  . THR D 1 71  ? 40.318 8.940   -9.677  1.00 68.82  ?  294 THR A CA  1 
ATOM   4665 C C   . THR D 1 71  ? 40.593 7.477   -9.348  1.00 68.93  ?  294 THR A C   1 
ATOM   4666 O O   . THR D 1 71  ? 41.737 7.017   -9.404  1.00 69.17  ?  294 THR A O   1 
ATOM   4667 C CB  . THR D 1 71  ? 40.409 9.169   -11.187 1.00 71.80  ?  294 THR A CB  1 
ATOM   4668 O OG1 . THR D 1 71  ? 39.907 10.473  -11.503 1.00 71.40  ?  294 THR A OG1 1 
ATOM   4669 C CG2 . THR D 1 71  ? 39.594 8.125   -11.939 1.00 58.64  ?  294 THR A CG2 1 
ATOM   4670 N N   . GLY D 1 72  ? 39.535 6.749   -8.989  1.00 64.85  ?  295 GLY A N   1 
ATOM   4671 C CA  . GLY D 1 72  ? 39.649 5.372   -8.574  1.00 67.75  ?  295 GLY A CA  1 
ATOM   4672 C C   . GLY D 1 72  ? 39.939 5.174   -7.101  1.00 66.06  ?  295 GLY A C   1 
ATOM   4673 O O   . GLY D 1 72  ? 39.616 4.113   -6.557  1.00 69.51  ?  295 GLY A O   1 
ATOM   4674 N N   . SER D 1 73  ? 40.541 6.162   -6.444  1.00 70.95  ?  296 SER A N   1 
ATOM   4675 C CA  . SER D 1 73  ? 40.808 6.079   -5.018  1.00 62.83  ?  296 SER A CA  1 
ATOM   4676 C C   . SER D 1 73  ? 39.540 6.363   -4.221  1.00 58.60  ?  296 SER A C   1 
ATOM   4677 O O   . SER D 1 73  ? 38.507 6.773   -4.757  1.00 62.09  ?  296 SER A O   1 
ATOM   4678 C CB  . SER D 1 73  ? 41.911 7.057   -4.617  1.00 61.68  ?  296 SER A CB  1 
ATOM   4679 O OG  . SER D 1 73  ? 41.968 7.204   -3.207  1.00 58.74  ?  296 SER A OG  1 
ATOM   4680 N N   . ARG D 1 74  ? 39.632 6.150   -2.910  1.00 60.20  ?  297 ARG A N   1 
ATOM   4681 C CA  . ARG D 1 74  ? 38.504 6.375   -2.027  1.00 55.28  ?  297 ARG A CA  1 
ATOM   4682 C C   . ARG D 1 74  ? 38.806 7.297   -0.864  1.00 50.74  ?  297 ARG A C   1 
ATOM   4683 O O   . ARG D 1 74  ? 37.875 7.679   -0.147  1.00 46.00  ?  297 ARG A O   1 
ATOM   4684 C CB  . ARG D 1 74  ? 37.985 5.046   -1.484  1.00 48.22  ?  297 ARG A CB  1 
ATOM   4685 C CG  . ARG D 1 74  ? 36.767 4.632   -2.216  1.00 57.70  ?  297 ARG A CG  1 
ATOM   4686 C CD  . ARG D 1 74  ? 36.496 3.177   -2.049  1.00 58.69  ?  297 ARG A CD  1 
ATOM   4687 N NE  . ARG D 1 74  ? 36.843 2.722   -0.713  1.00 64.46  ?  297 ARG A NE  1 
ATOM   4688 C CZ  . ARG D 1 74  ? 36.174 1.783   -0.067  1.00 68.88  ?  297 ARG A CZ  1 
ATOM   4689 N NH1 . ARG D 1 74  ? 35.063 1.270   -0.564  1.00 74.28  ?  297 ARG A NH1 1 
ATOM   4690 N NH2 . ARG D 1 74  ? 36.611 1.370   1.118   1.00 64.71  ?  297 ARG A NH2 1 
ATOM   4691 N N   . ASN D 1 75  ? 40.064 7.658   -0.649  1.00 52.31  ?  298 ASN A N   1 
ATOM   4692 C CA  . ASN D 1 75  ? 40.407 8.682   0.323   1.00 48.77  ?  298 ASN A CA  1 
ATOM   4693 C C   . ASN D 1 75  ? 40.213 10.049  -0.319  1.00 48.83  ?  298 ASN A C   1 
ATOM   4694 O O   . ASN D 1 75  ? 40.850 10.360  -1.332  1.00 50.69  ?  298 ASN A O   1 
ATOM   4695 C CB  . ASN D 1 75  ? 41.843 8.495   0.801   1.00 51.65  ?  298 ASN A CB  1 
ATOM   4696 C CG  . ASN D 1 75  ? 42.129 7.073   1.249   1.00 60.58  ?  298 ASN A CG  1 
ATOM   4697 O OD1 . ASN D 1 75  ? 41.233 6.365   1.716   1.00 59.59  ?  298 ASN A OD1 1 
ATOM   4698 N ND2 . ASN D 1 75  ? 43.378 6.645   1.103   1.00 62.03  ?  298 ASN A ND2 1 
ATOM   4699 N N   . TYR D 1 76  ? 39.318 10.849  0.250   1.00 47.32  ?  299 TYR A N   1 
ATOM   4700 C CA  . TYR D 1 76  ? 39.041 12.190  -0.242  1.00 44.45  ?  299 TYR A CA  1 
ATOM   4701 C C   . TYR D 1 76  ? 39.779 13.215  0.606   1.00 43.67  ?  299 TYR A C   1 
ATOM   4702 O O   . TYR D 1 76  ? 39.842 13.093  1.833   1.00 43.27  ?  299 TYR A O   1 
ATOM   4703 C CB  . TYR D 1 76  ? 37.541 12.489  -0.217  1.00 43.19  ?  299 TYR A CB  1 
ATOM   4704 C CG  . TYR D 1 76  ? 36.748 11.765  -1.277  1.00 46.78  ?  299 TYR A CG  1 
ATOM   4705 C CD1 . TYR D 1 76  ? 36.472 10.410  -1.158  1.00 46.44  ?  299 TYR A CD1 1 
ATOM   4706 C CD2 . TYR D 1 76  ? 36.273 12.437  -2.396  1.00 47.60  ?  299 TYR A CD2 1 
ATOM   4707 C CE1 . TYR D 1 76  ? 35.748 9.742   -2.123  1.00 49.56  ?  299 TYR A CE1 1 
ATOM   4708 C CE2 . TYR D 1 76  ? 35.547 11.778  -3.368  1.00 44.07  ?  299 TYR A CE2 1 
ATOM   4709 C CZ  . TYR D 1 76  ? 35.288 10.430  -3.226  1.00 50.09  ?  299 TYR A CZ  1 
ATOM   4710 O OH  . TYR D 1 76  ? 34.565 9.763   -4.187  1.00 52.75  ?  299 TYR A OH  1 
ATOM   4711 N N   . THR D 1 77  ? 40.334 14.225  -0.056  1.00 42.63  ?  300 THR A N   1 
ATOM   4712 C CA  . THR D 1 77  ? 40.991 15.339  0.615   1.00 45.39  ?  300 THR A CA  1 
ATOM   4713 C C   . THR D 1 77  ? 40.001 16.489  0.717   1.00 45.66  ?  300 THR A C   1 
ATOM   4714 O O   . THR D 1 77  ? 39.456 16.936  -0.298  1.00 42.95  ?  300 THR A O   1 
ATOM   4715 C CB  . THR D 1 77  ? 42.248 15.775  -0.139  1.00 48.38  ?  300 THR A CB  1 
ATOM   4716 O OG1 . THR D 1 77  ? 43.285 14.806  0.055   1.00 54.54  ?  300 THR A OG1 1 
ATOM   4717 C CG2 . THR D 1 77  ? 42.728 17.132  0.365   1.00 41.23  ?  300 THR A CG2 1 
ATOM   4718 N N   . MET D 1 78  ? 39.763 16.961  1.937   1.00 45.12  ?  301 MET A N   1 
ATOM   4719 C CA  . MET D 1 78  ? 38.847 18.068  2.172   1.00 41.34  ?  301 MET A CA  1 
ATOM   4720 C C   . MET D 1 78  ? 39.650 19.341  2.406   1.00 42.57  ?  301 MET A C   1 
ATOM   4721 O O   . MET D 1 78  ? 40.471 19.403  3.328   1.00 42.59  ?  301 MET A O   1 
ATOM   4722 C CB  . MET D 1 78  ? 37.931 17.790  3.363   1.00 41.34  ?  301 MET A CB  1 
ATOM   4723 C CG  . MET D 1 78  ? 36.824 18.823  3.524   1.00 37.92  ?  301 MET A CG  1 
ATOM   4724 S SD  . MET D 1 78  ? 36.115 18.878  5.179   1.00 38.20  ?  301 MET A SD  1 
ATOM   4725 C CE  . MET D 1 78  ? 34.630 17.907  4.938   1.00 37.99  ?  301 MET A CE  1 
ATOM   4726 N N   . ASN D 1 79  ? 39.426 20.340  1.558   1.00 38.49  ?  302 ASN A N   1 
ATOM   4727 C CA  . ASN D 1 79  ? 39.968 21.673  1.782   1.00 41.32  ?  302 ASN A CA  1 
ATOM   4728 C C   . ASN D 1 79  ? 39.050 22.383  2.767   1.00 38.21  ?  302 ASN A C   1 
ATOM   4729 O O   . ASN D 1 79  ? 37.887 22.659  2.456   1.00 36.42  ?  302 ASN A O   1 
ATOM   4730 C CB  . ASN D 1 79  ? 40.087 22.431  0.466   1.00 43.86  ?  302 ASN A CB  1 
ATOM   4731 C CG  . ASN D 1 79  ? 40.732 21.598  -0.622  1.00 48.55  ?  302 ASN A CG  1 
ATOM   4732 O OD1 . ASN D 1 79  ? 41.889 21.194  -0.506  1.00 49.40  ?  302 ASN A OD1 1 
ATOM   4733 N ND2 . ASN D 1 79  ? 39.983 21.330  -1.687  1.00 54.01  ?  302 ASN A ND2 1 
ATOM   4734 N N   . LEU D 1 80  ? 39.567 22.664  3.959   1.00 37.34  ?  303 LEU A N   1 
ATOM   4735 C CA  . LEU D 1 80  ? 38.717 23.107  5.054   1.00 38.15  ?  303 LEU A CA  1 
ATOM   4736 C C   . LEU D 1 80  ? 38.230 24.532  4.836   1.00 35.05  ?  303 LEU A C   1 
ATOM   4737 O O   . LEU D 1 80  ? 38.964 25.397  4.350   1.00 35.56  ?  303 LEU A O   1 
ATOM   4738 C CB  . LEU D 1 80  ? 39.469 23.019  6.380   1.00 40.69  ?  303 LEU A CB  1 
ATOM   4739 C CG  . LEU D 1 80  ? 39.883 21.626  6.857   1.00 39.26  ?  303 LEU A CG  1 
ATOM   4740 C CD1 . LEU D 1 80  ? 40.504 21.712  8.244   1.00 38.55  ?  303 LEU A CD1 1 
ATOM   4741 C CD2 . LEU D 1 80  ? 38.692 20.687  6.856   1.00 33.14  ?  303 LEU A CD2 1 
ATOM   4742 N N   . ALA D 1 81  ? 36.976 24.768  5.201   1.00 38.24  ?  304 ALA A N   1 
ATOM   4743 C CA  . ALA D 1 81  ? 36.418 26.100  5.352   1.00 35.01  ?  304 ALA A CA  1 
ATOM   4744 C C   . ALA D 1 81  ? 36.097 26.339  6.821   1.00 41.14  ?  304 ALA A C   1 
ATOM   4745 O O   . ALA D 1 81  ? 36.160 25.428  7.653   1.00 40.74  ?  304 ALA A O   1 
ATOM   4746 C CB  . ALA D 1 81  ? 35.164 26.272  4.488   1.00 31.93  ?  304 ALA A CB  1 
ATOM   4747 N N   . SER D 1 82  ? 35.756 27.584  7.141   1.00 41.89  ?  305 SER A N   1 
ATOM   4748 C CA  . SER D 1 82  ? 35.349 27.911  8.497   1.00 41.63  ?  305 SER A CA  1 
ATOM   4749 C C   . SER D 1 82  ? 34.022 27.228  8.829   1.00 46.41  ?  305 SER A C   1 
ATOM   4750 O O   . SER D 1 82  ? 33.333 26.686  7.960   1.00 45.74  ?  305 SER A O   1 
ATOM   4751 C CB  . SER D 1 82  ? 35.229 29.425  8.673   1.00 42.95  ?  305 SER A CB  1 
ATOM   4752 O OG  . SER D 1 82  ? 36.503 30.019  8.847   1.00 51.90  ?  305 SER A OG  1 
ATOM   4753 N N   . GLN D 1 83  ? 33.666 27.261  10.116  1.00 44.64  ?  306 GLN A N   1 
ATOM   4754 C CA  . GLN D 1 83  ? 32.416 26.648  10.553  1.00 45.71  ?  306 GLN A CA  1 
ATOM   4755 C C   . GLN D 1 83  ? 31.197 27.304  9.914   1.00 44.98  ?  306 GLN A C   1 
ATOM   4756 O O   . GLN D 1 83  ? 30.134 26.677  9.850   1.00 50.13  ?  306 GLN A O   1 
ATOM   4757 C CB  . GLN D 1 83  ? 32.309 26.707  12.078  1.00 48.87  ?  306 GLN A CB  1 
ATOM   4758 C CG  . GLN D 1 83  ? 31.664 27.976  12.615  1.00 61.81  ?  306 GLN A CG  1 
ATOM   4759 C CD  . GLN D 1 83  ? 30.838 27.730  13.863  1.00 69.80  ?  306 GLN A CD  1 
ATOM   4760 O OE1 . GLN D 1 83  ? 31.349 27.248  14.877  1.00 63.22  ?  306 GLN A OE1 1 
ATOM   4761 N NE2 . GLN D 1 83  ? 29.551 28.050  13.792  1.00 66.91  ?  306 GLN A NE2 1 
ATOM   4762 N N   . ASN D 1 84  ? 31.328 28.541  9.428   1.00 43.47  ?  307 ASN A N   1 
ATOM   4763 C CA  . ASN D 1 84  ? 30.239 29.251  8.766   1.00 49.18  ?  307 ASN A CA  1 
ATOM   4764 C C   . ASN D 1 84  ? 30.451 29.361  7.258   1.00 45.52  ?  307 ASN A C   1 
ATOM   4765 O O   . ASN D 1 84  ? 29.876 30.249  6.620   1.00 50.12  ?  307 ASN A O   1 
ATOM   4766 C CB  . ASN D 1 84  ? 30.059 30.640  9.385   1.00 47.09  ?  307 ASN A CB  1 
ATOM   4767 C CG  . ASN D 1 84  ? 31.298 31.509  9.250   1.00 56.80  ?  307 ASN A CG  1 
ATOM   4768 O OD1 . ASN D 1 84  ? 32.326 31.078  8.727   1.00 56.26  ?  307 ASN A OD1 1 
ATOM   4769 N ND2 . ASN D 1 84  ? 31.204 32.746  9.728   1.00 59.22  ?  307 ASN A ND2 1 
ATOM   4770 N N   . TRP D 1 85  ? 31.277 28.484  6.685   1.00 42.97  ?  308 TRP A N   1 
ATOM   4771 C CA  . TRP D 1 85  ? 31.558 28.374  5.255   1.00 46.22  ?  308 TRP A CA  1 
ATOM   4772 C C   . TRP D 1 85  ? 32.355 29.549  4.702   1.00 46.11  ?  308 TRP A C   1 
ATOM   4773 O O   . TRP D 1 85  ? 32.481 29.679  3.477   1.00 48.38  ?  308 TRP A O   1 
ATOM   4774 C CB  . TRP D 1 85  ? 30.274 28.189  4.437   1.00 42.97  ?  308 TRP A CB  1 
ATOM   4775 C CG  . TRP D 1 85  ? 29.540 26.951  4.824   1.00 45.25  ?  308 TRP A CG  1 
ATOM   4776 C CD1 . TRP D 1 85  ? 28.410 26.869  5.583   1.00 42.51  ?  308 TRP A CD1 1 
ATOM   4777 C CD2 . TRP D 1 85  ? 29.901 25.605  4.494   1.00 45.36  ?  308 TRP A CD2 1 
ATOM   4778 N NE1 . TRP D 1 85  ? 28.038 25.555  5.738   1.00 47.04  ?  308 TRP A NE1 1 
ATOM   4779 C CE2 . TRP D 1 85  ? 28.938 24.758  5.079   1.00 41.79  ?  308 TRP A CE2 1 
ATOM   4780 C CE3 . TRP D 1 85  ? 30.941 25.033  3.754   1.00 36.38  ?  308 TRP A CE3 1 
ATOM   4781 C CZ2 . TRP D 1 85  ? 28.983 23.372  4.947   1.00 37.04  ?  308 TRP A CZ2 1 
ATOM   4782 C CZ3 . TRP D 1 85  ? 30.985 23.658  3.627   1.00 36.24  ?  308 TRP A CZ3 1 
ATOM   4783 C CH2 . TRP D 1 85  ? 30.013 22.843  4.220   1.00 37.02  ?  308 TRP A CH2 1 
ATOM   4784 N N   . ASN D 1 86  ? 32.905 30.402  5.561   1.00 45.64  ?  309 ASN A N   1 
ATOM   4785 C CA  . ASN D 1 86  ? 33.865 31.399  5.117   1.00 45.28  ?  309 ASN A CA  1 
ATOM   4786 C C   . ASN D 1 86  ? 35.222 30.739  4.880   1.00 46.43  ?  309 ASN A C   1 
ATOM   4787 O O   . ASN D 1 86  ? 35.464 29.592  5.266   1.00 46.51  ?  309 ASN A O   1 
ATOM   4788 C CB  . ASN D 1 86  ? 33.987 32.525  6.143   1.00 50.66  ?  309 ASN A CB  1 
ATOM   4789 C CG  . ASN D 1 86  ? 32.801 33.472  6.114   1.00 51.07  ?  309 ASN A CG  1 
ATOM   4790 O OD1 . ASN D 1 86  ? 32.175 33.671  5.070   1.00 52.70  ?  309 ASN A OD1 1 
ATOM   4791 N ND2 . ASN D 1 86  ? 32.489 34.066  7.259   1.00 54.92  ?  309 ASN A ND2 1 
ATOM   4792 N N   . ASP D 1 87  ? 36.119 31.478  4.234   1.00 42.93  ?  310 ASP A N   1 
ATOM   4793 C CA  . ASP D 1 87  ? 37.434 30.937  3.922   1.00 44.53  ?  310 ASP A CA  1 
ATOM   4794 C C   . ASP D 1 87  ? 38.250 30.719  5.193   1.00 48.37  ?  310 ASP A C   1 
ATOM   4795 O O   . ASP D 1 87  ? 38.141 31.469  6.167   1.00 47.02  ?  310 ASP A O   1 
ATOM   4796 C CB  . ASP D 1 87  ? 38.188 31.870  2.977   1.00 46.00  ?  310 ASP A CB  1 
ATOM   4797 C CG  . ASP D 1 87  ? 37.448 32.105  1.677   1.00 48.68  ?  310 ASP A CG  1 
ATOM   4798 O OD1 . ASP D 1 87  ? 36.879 31.142  1.120   1.00 44.93  ?  310 ASP A OD1 1 
ATOM   4799 O OD2 . ASP D 1 87  ? 37.432 33.261  1.216   1.00 41.87  ?  310 ASP A OD2 1 
ATOM   4800 N N   . TYR D 1 88  ? 39.073 29.675  5.172   1.00 50.53  ?  311 TYR A N   1 
ATOM   4801 C CA  . TYR D 1 88  ? 39.931 29.359  6.302   1.00 48.83  ?  311 TYR A CA  1 
ATOM   4802 C C   . TYR D 1 88  ? 41.150 30.272  6.315   1.00 55.32  ?  311 TYR A C   1 
ATOM   4803 O O   . TYR D 1 88  ? 41.774 30.516  5.278   1.00 57.19  ?  311 TYR A O   1 
ATOM   4804 C CB  . TYR D 1 88  ? 40.369 27.893  6.246   1.00 49.98  ?  311 TYR A CB  1 
ATOM   4805 C CG  . TYR D 1 88  ? 41.423 27.525  7.265   1.00 52.08  ?  311 TYR A CG  1 
ATOM   4806 C CD1 . TYR D 1 88  ? 41.213 27.740  8.621   1.00 46.62  ?  311 TYR A CD1 1 
ATOM   4807 C CD2 . TYR D 1 88  ? 42.631 26.965  6.871   1.00 48.24  ?  311 TYR A CD2 1 
ATOM   4808 C CE1 . TYR D 1 88  ? 42.174 27.409  9.556   1.00 46.44  ?  311 TYR A CE1 1 
ATOM   4809 C CE2 . TYR D 1 88  ? 43.599 26.627  7.799   1.00 51.10  ?  311 TYR A CE2 1 
ATOM   4810 C CZ  . TYR D 1 88  ? 43.365 26.853  9.139   1.00 45.28  ?  311 TYR A CZ  1 
ATOM   4811 O OH  . TYR D 1 88  ? 44.327 26.520  10.065  1.00 47.19  ?  311 TYR A OH  1 
ATOM   4812 N N   . ASP D 1 89  ? 41.480 30.782  7.498   1.00 57.72  ?  312 ASP A N   1 
ATOM   4813 C CA  . ASP D 1 89  ? 42.610 31.693  7.680   1.00 54.06  ?  312 ASP A CA  1 
ATOM   4814 C C   . ASP D 1 89  ? 43.656 31.023  8.559   1.00 58.76  ?  312 ASP A C   1 
ATOM   4815 O O   . ASP D 1 89  ? 43.504 30.991  9.794   1.00 58.57  ?  312 ASP A O   1 
ATOM   4816 C CB  . ASP D 1 89  ? 42.148 33.012  8.304   1.00 57.80  ?  312 ASP A CB  1 
ATOM   4817 C CG  . ASP D 1 89  ? 43.294 33.974  8.550   1.00 63.78  ?  312 ASP A CG  1 
ATOM   4818 O OD1 . ASP D 1 89  ? 44.292 33.920  7.799   1.00 66.12  ?  312 ASP A OD1 1 
ATOM   4819 O OD2 . ASP D 1 89  ? 43.195 34.788  9.493   1.00 67.63  ?  312 ASP A OD2 1 
ATOM   4820 N N   . PRO D 1 90  ? 44.734 30.480  7.984   1.00 54.73  ?  313 PRO A N   1 
ATOM   4821 C CA  . PRO D 1 90  ? 45.725 29.767  8.802   1.00 54.69  ?  313 PRO A CA  1 
ATOM   4822 C C   . PRO D 1 90  ? 46.623 30.685  9.616   1.00 61.19  ?  313 PRO A C   1 
ATOM   4823 O O   . PRO D 1 90  ? 47.419 30.180  10.420  1.00 60.28  ?  313 PRO A O   1 
ATOM   4824 C CB  . PRO D 1 90  ? 46.540 28.972  7.766   1.00 57.08  ?  313 PRO A CB  1 
ATOM   4825 C CG  . PRO D 1 90  ? 45.864 29.203  6.430   1.00 52.58  ?  313 PRO A CG  1 
ATOM   4826 C CD  . PRO D 1 90  ? 45.084 30.467  6.555   1.00 54.71  ?  313 PRO A CD  1 
ATOM   4827 N N   . THR D 1 91  ? 46.525 32.004  9.443   1.00 60.65  ?  314 THR A N   1 
ATOM   4828 C CA  . THR D 1 91  ? 47.375 32.931  10.177  1.00 61.54  ?  314 THR A CA  1 
ATOM   4829 C C   . THR D 1 91  ? 46.879 33.206  11.592  1.00 61.44  ?  314 THR A C   1 
ATOM   4830 O O   . THR D 1 91  ? 47.570 33.901  12.346  1.00 66.67  ?  314 THR A O   1 
ATOM   4831 C CB  . THR D 1 91  ? 47.504 34.252  9.413   1.00 60.67  ?  314 THR A CB  1 
ATOM   4832 O OG1 . THR D 1 91  ? 46.340 35.060  9.639   1.00 57.80  ?  314 THR A OG1 1 
ATOM   4833 C CG2 . THR D 1 91  ? 47.654 33.993  7.921   1.00 60.10  ?  314 THR A CG2 1 
ATOM   4834 N N   . GLU D 1 92  ? 45.712 32.687  11.968  1.00 61.45  ?  315 GLU A N   1 
ATOM   4835 C CA  . GLU D 1 92  ? 45.220 32.873  13.326  1.00 60.02  ?  315 GLU A CA  1 
ATOM   4836 C C   . GLU D 1 92  ? 46.103 32.121  14.316  1.00 55.05  ?  315 GLU A C   1 
ATOM   4837 O O   . GLU D 1 92  ? 46.569 31.012  14.039  1.00 51.89  ?  315 GLU A O   1 
ATOM   4838 C CB  . GLU D 1 92  ? 43.772 32.391  13.439  1.00 63.50  ?  315 GLU A CB  1 
ATOM   4839 C CG  . GLU D 1 92  ? 42.781 33.480  13.831  1.00 68.35  ?  315 GLU A CG  1 
ATOM   4840 C CD  . GLU D 1 92  ? 41.410 32.924  14.173  1.00 75.17  ?  315 GLU A CD  1 
ATOM   4841 O OE1 . GLU D 1 92  ? 40.581 32.777  13.250  1.00 81.01  ?  315 GLU A OE1 1 
ATOM   4842 O OE2 . GLU D 1 92  ? 41.162 32.637  15.363  1.00 70.60  ?  315 GLU A OE2 1 
ATOM   4843 N N   . GLU D 1 93  ? 46.337 32.736  15.478  1.00 55.20  ?  316 GLU A N   1 
ATOM   4844 C CA  . GLU D 1 93  ? 47.225 32.170  16.494  1.00 57.82  ?  316 GLU A CA  1 
ATOM   4845 C C   . GLU D 1 93  ? 46.493 31.064  17.258  1.00 56.01  ?  316 GLU A C   1 
ATOM   4846 O O   . GLU D 1 93  ? 46.182 31.162  18.446  1.00 53.89  ?  316 GLU A O   1 
ATOM   4847 C CB  . GLU D 1 93  ? 47.729 33.254  17.431  1.00 56.28  ?  316 GLU A CB  1 
ATOM   4848 C CG  . GLU D 1 93  ? 48.507 34.359  16.740  1.00 63.60  ?  316 GLU A CG  1 
ATOM   4849 C CD  . GLU D 1 93  ? 48.748 35.544  17.653  1.00 75.89  ?  316 GLU A CD  1 
ATOM   4850 O OE1 . GLU D 1 93  ? 49.706 35.491  18.454  1.00 74.69  ?  316 GLU A OE1 1 
ATOM   4851 O OE2 . GLU D 1 93  ? 47.978 36.525  17.570  1.00 77.75  ?  316 GLU A OE2 1 
ATOM   4852 N N   . ILE D 1 94  ? 46.224 29.980  16.539  1.00 52.11  ?  317 ILE A N   1 
ATOM   4853 C CA  . ILE D 1 94  ? 45.586 28.795  17.108  1.00 50.15  ?  317 ILE A CA  1 
ATOM   4854 C C   . ILE D 1 94  ? 46.292 27.561  16.593  1.00 49.50  ?  317 ILE A C   1 
ATOM   4855 O O   . ILE D 1 94  ? 46.824 27.541  15.467  1.00 49.17  ?  317 ILE A O   1 
ATOM   4856 C CB  . ILE D 1 94  ? 44.088 28.723  16.772  1.00 51.60  ?  317 ILE A CB  1 
ATOM   4857 C CG1 . ILE D 1 94  ? 43.862 29.048  15.301  1.00 48.91  ?  317 ILE A CG1 1 
ATOM   4858 C CG2 . ILE D 1 94  ? 43.299 29.639  17.684  1.00 46.71  ?  317 ILE A CG2 1 
ATOM   4859 C CD1 . ILE D 1 94  ? 42.398 29.102  14.927  1.00 46.50  ?  317 ILE A CD1 1 
ATOM   4860 N N   . PRO D 1 95  ? 46.300 26.484  17.378  1.00 44.96  ?  318 PRO A N   1 
ATOM   4861 C CA  . PRO D 1 95  ? 46.976 25.258  16.926  1.00 43.31  ?  318 PRO A CA  1 
ATOM   4862 C C   . PRO D 1 95  ? 46.346 24.647  15.684  1.00 42.71  ?  318 PRO A C   1 
ATOM   4863 O O   . PRO D 1 95  ? 47.044 23.994  14.900  1.00 43.91  ?  318 PRO A O   1 
ATOM   4864 C CB  . PRO D 1 95  ? 46.852 24.316  18.138  1.00 44.64  ?  318 PRO A CB  1 
ATOM   4865 C CG  . PRO D 1 95  ? 46.432 25.193  19.293  1.00 47.29  ?  318 PRO A CG  1 
ATOM   4866 C CD  . PRO D 1 95  ? 45.688 26.329  18.702  1.00 45.19  ?  318 PRO A CD  1 
ATOM   4867 N N   . ALA D 1 96  ? 45.055 24.860  15.480  1.00 40.23  ?  319 ALA A N   1 
ATOM   4868 C CA  . ALA D 1 96  ? 44.291 24.256  14.399  1.00 42.84  ?  319 ALA A CA  1 
ATOM   4869 C C   . ALA D 1 96  ? 42.942 24.964  14.329  1.00 42.62  ?  319 ALA A C   1 
ATOM   4870 O O   . ALA D 1 96  ? 42.647 25.793  15.199  1.00 42.65  ?  319 ALA A O   1 
ATOM   4871 C CB  . ALA D 1 96  ? 44.124 22.753  14.641  1.00 39.44  ?  319 ALA A CB  1 
ATOM   4872 N N   . PRO D 1 97  ? 42.118 24.701  13.313  1.00 40.74  ?  320 PRO A N   1 
ATOM   4873 C CA  . PRO D 1 97  ? 40.747 25.221  13.332  1.00 39.53  ?  320 PRO A CA  1 
ATOM   4874 C C   . PRO D 1 97  ? 40.046 24.875  14.639  1.00 41.67  ?  320 PRO A C   1 
ATOM   4875 O O   . PRO D 1 97  ? 40.229 23.790  15.195  1.00 42.96  ?  320 PRO A O   1 
ATOM   4876 C CB  . PRO D 1 97  ? 40.092 24.527  12.136  1.00 36.37  ?  320 PRO A CB  1 
ATOM   4877 C CG  . PRO D 1 97  ? 41.214 24.318  11.182  1.00 38.61  ?  320 PRO A CG  1 
ATOM   4878 C CD  . PRO D 1 97  ? 42.458 24.103  12.007  1.00 34.65  ?  320 PRO A CD  1 
ATOM   4879 N N   . LEU D 1 98  ? 39.247 25.818  15.134  1.00 35.99  ?  321 LEU A N   1 
ATOM   4880 C CA  . LEU D 1 98  ? 38.564 25.629  16.407  1.00 37.08  ?  321 LEU A CA  1 
ATOM   4881 C C   . LEU D 1 98  ? 37.617 24.437  16.332  1.00 38.01  ?  321 LEU A C   1 
ATOM   4882 O O   . LEU D 1 98  ? 36.784 24.345  15.426  1.00 36.86  ?  321 LEU A O   1 
ATOM   4883 C CB  . LEU D 1 98  ? 37.801 26.897  16.788  1.00 39.43  ?  321 LEU A CB  1 
ATOM   4884 C CG  . LEU D 1 98  ? 38.639 28.174  16.899  1.00 43.40  ?  321 LEU A CG  1 
ATOM   4885 C CD1 . LEU D 1 98  ? 37.750 29.385  17.150  1.00 42.27  ?  321 LEU A CD1 1 
ATOM   4886 C CD2 . LEU D 1 98  ? 39.685 28.040  17.996  1.00 45.80  ?  321 LEU A CD2 1 
ATOM   4887 N N   . GLY D 1 99  ? 37.752 23.521  17.288  1.00 37.82  ?  322 GLY A N   1 
ATOM   4888 C CA  . GLY D 1 99  ? 36.988 22.293  17.292  1.00 38.16  ?  322 GLY A CA  1 
ATOM   4889 C C   . GLY D 1 99  ? 37.693 21.101  16.681  1.00 35.22  ?  322 GLY A C   1 
ATOM   4890 O O   . GLY D 1 99  ? 37.118 20.006  16.670  1.00 37.30  ?  322 GLY A O   1 
ATOM   4891 N N   . THR D 1 100 ? 38.907 21.284  16.171  1.00 34.75  ?  323 THR A N   1 
ATOM   4892 C CA  . THR D 1 100 ? 39.673 20.174  15.628  1.00 32.44  ?  323 THR A CA  1 
ATOM   4893 C C   . THR D 1 100 ? 39.899 19.121  16.711  1.00 38.66  ?  323 THR A C   1 
ATOM   4894 O O   . THR D 1 100 ? 40.134 19.473  17.874  1.00 35.78  ?  323 THR A O   1 
ATOM   4895 C CB  . THR D 1 100 ? 41.017 20.677  15.087  1.00 34.53  ?  323 THR A CB  1 
ATOM   4896 O OG1 . THR D 1 100 ? 40.786 21.641  14.055  1.00 39.74  ?  323 THR A OG1 1 
ATOM   4897 C CG2 . THR D 1 100 ? 41.852 19.537  14.527  1.00 37.25  ?  323 THR A CG2 1 
ATOM   4898 N N   . PRO D 1 101 ? 39.803 17.832  16.380  1.00 36.51  ?  324 PRO A N   1 
ATOM   4899 C CA  . PRO D 1 101 ? 40.082 16.788  17.374  1.00 36.08  ?  324 PRO A CA  1 
ATOM   4900 C C   . PRO D 1 101 ? 41.454 16.971  18.009  1.00 36.64  ?  324 PRO A C   1 
ATOM   4901 O O   . PRO D 1 101 ? 42.427 17.330  17.341  1.00 39.07  ?  324 PRO A O   1 
ATOM   4902 C CB  . PRO D 1 101 ? 40.009 15.493  16.559  1.00 34.18  ?  324 PRO A CB  1 
ATOM   4903 C CG  . PRO D 1 101 ? 39.115 15.812  15.415  1.00 31.30  ?  324 PRO A CG  1 
ATOM   4904 C CD  . PRO D 1 101 ? 39.277 17.278  15.119  1.00 36.82  ?  324 PRO A CD  1 
ATOM   4905 N N   . ASP D 1 102 ? 41.525 16.724  19.318  1.00 36.17  ?  325 ASP A N   1 
ATOM   4906 C CA  . ASP D 1 102 ? 42.752 16.890  20.085  1.00 36.65  ?  325 ASP A CA  1 
ATOM   4907 C C   . ASP D 1 102 ? 43.285 15.559  20.609  1.00 39.42  ?  325 ASP A C   1 
ATOM   4908 O O   . ASP D 1 102 ? 43.899 15.507  21.678  1.00 39.22  ?  325 ASP A O   1 
ATOM   4909 C CB  . ASP D 1 102 ? 42.535 17.870  21.238  1.00 37.77  ?  325 ASP A CB  1 
ATOM   4910 C CG  . ASP D 1 102 ? 41.461 17.407  22.206  1.00 41.36  ?  325 ASP A CG  1 
ATOM   4911 O OD1 . ASP D 1 102 ? 40.731 16.447  21.881  1.00 45.05  ?  325 ASP A OD1 1 
ATOM   4912 O OD2 . ASP D 1 102 ? 41.347 18.009  23.294  1.00 39.71  ?  325 ASP A OD2 1 
ATOM   4913 N N   . PHE D 1 103 ? 43.053 14.475  19.873  1.00 39.06  ?  326 PHE A N   1 
ATOM   4914 C CA  . PHE D 1 103 ? 43.578 13.175  20.258  1.00 42.22  ?  326 PHE A CA  1 
ATOM   4915 C C   . PHE D 1 103 ? 43.886 12.372  19.004  1.00 42.79  ?  326 PHE A C   1 
ATOM   4916 O O   . PHE D 1 103 ? 43.265 12.564  17.955  1.00 43.16  ?  326 PHE A O   1 
ATOM   4917 C CB  . PHE D 1 103 ? 42.602 12.409  21.164  1.00 36.66  ?  326 PHE A CB  1 
ATOM   4918 C CG  . PHE D 1 103 ? 41.253 12.164  20.549  1.00 39.75  ?  326 PHE A CG  1 
ATOM   4919 C CD1 . PHE D 1 103 ? 40.234 13.092  20.687  1.00 44.03  ?  326 PHE A CD1 1 
ATOM   4920 C CD2 . PHE D 1 103 ? 40.998 10.998  19.843  1.00 41.94  ?  326 PHE A CD2 1 
ATOM   4921 C CE1 . PHE D 1 103 ? 38.990 12.867  20.124  1.00 43.17  ?  326 PHE A CE1 1 
ATOM   4922 C CE2 . PHE D 1 103 ? 39.757 10.767  19.280  1.00 39.07  ?  326 PHE A CE2 1 
ATOM   4923 C CZ  . PHE D 1 103 ? 38.752 11.702  19.421  1.00 38.55  ?  326 PHE A CZ  1 
ATOM   4924 N N   . VAL D 1 104 ? 44.862 11.477  19.124  1.00 44.04  ?  327 VAL A N   1 
ATOM   4925 C CA  . VAL D 1 104 ? 45.239 10.602  18.020  1.00 39.08  ?  327 VAL A CA  1 
ATOM   4926 C C   . VAL D 1 104 ? 44.306 9.399   18.019  1.00 41.12  ?  327 VAL A C   1 
ATOM   4927 O O   . VAL D 1 104 ? 44.179 8.695   19.027  1.00 39.00  ?  327 VAL A O   1 
ATOM   4928 C CB  . VAL D 1 104 ? 46.706 10.167  18.135  1.00 39.16  ?  327 VAL A CB  1 
ATOM   4929 C CG1 . VAL D 1 104 ? 46.974 8.961   17.247  1.00 44.77  ?  327 VAL A CG1 1 
ATOM   4930 C CG2 . VAL D 1 104 ? 47.626 11.322  17.770  1.00 39.74  ?  327 VAL A CG2 1 
ATOM   4931 N N   . GLY D 1 105 ? 43.646 9.164   16.893  1.00 39.26  ?  328 GLY A N   1 
ATOM   4932 C CA  . GLY D 1 105 ? 42.724 8.053   16.795  1.00 38.18  ?  328 GLY A CA  1 
ATOM   4933 C C   . GLY D 1 105 ? 41.961 8.110   15.493  1.00 39.47  ?  328 GLY A C   1 
ATOM   4934 O O   . GLY D 1 105 ? 42.122 9.029   14.685  1.00 37.67  ?  328 GLY A O   1 
ATOM   4935 N N   . LYS D 1 106 ? 41.117 7.103   15.307  1.00 39.55  ?  329 LYS A N   1 
ATOM   4936 C CA  . LYS D 1 106 ? 40.317 6.956   14.097  1.00 41.44  ?  329 LYS A CA  1 
ATOM   4937 C C   . LYS D 1 106 ? 38.872 7.301   14.432  1.00 40.19  ?  329 LYS A C   1 
ATOM   4938 O O   . LYS D 1 106 ? 38.174 6.514   15.078  1.00 37.64  ?  329 LYS A O   1 
ATOM   4939 C CB  . LYS D 1 106 ? 40.433 5.540   13.538  1.00 42.04  ?  329 LYS A CB  1 
ATOM   4940 C CG  . LYS D 1 106 ? 41.860 5.121   13.234  1.00 46.14  ?  329 LYS A CG  1 
ATOM   4941 C CD  . LYS D 1 106 ? 42.054 3.620   13.370  1.00 52.72  ?  329 LYS A CD  1 
ATOM   4942 C CE  . LYS D 1 106 ? 43.336 3.171   12.682  1.00 55.40  ?  329 LYS A CE  1 
ATOM   4943 N NZ  . LYS D 1 106 ? 44.032 2.083   13.421  1.00 54.78  ?  329 LYS A NZ  1 
ATOM   4944 N N   . ILE D 1 107 ? 38.433 8.477   13.996  1.00 39.73  ?  330 ILE A N   1 
ATOM   4945 C CA  . ILE D 1 107 ? 37.067 8.936   14.219  1.00 40.23  ?  330 ILE A CA  1 
ATOM   4946 C C   . ILE D 1 107 ? 36.228 8.549   13.009  1.00 40.10  ?  330 ILE A C   1 
ATOM   4947 O O   . ILE D 1 107 ? 36.558 8.913   11.874  1.00 41.84  ?  330 ILE A O   1 
ATOM   4948 C CB  . ILE D 1 107 ? 37.021 10.454  14.453  1.00 35.01  ?  330 ILE A CB  1 
ATOM   4949 C CG1 . ILE D 1 107 ? 37.981 10.858  15.575  1.00 37.46  ?  330 ILE A CG1 1 
ATOM   4950 C CG2 . ILE D 1 107 ? 35.596 10.899  14.749  1.00 28.99  ?  330 ILE A CG2 1 
ATOM   4951 C CD1 . ILE D 1 107 ? 37.847 12.308  16.005  1.00 37.66  ?  330 ILE A CD1 1 
ATOM   4952 N N   . GLN D 1 108 ? 35.144 7.820   13.246  1.00 35.74  ?  331 GLN A N   1 
ATOM   4953 C CA  . GLN D 1 108 ? 34.226 7.429   12.186  1.00 41.30  ?  331 GLN A CA  1 
ATOM   4954 C C   . GLN D 1 108 ? 32.967 8.285   12.241  1.00 37.21  ?  331 GLN A C   1 
ATOM   4955 O O   . GLN D 1 108 ? 32.456 8.591   13.323  1.00 34.97  ?  331 GLN A O   1 
ATOM   4956 C CB  . GLN D 1 108 ? 33.853 5.949   12.292  1.00 37.08  ?  331 GLN A CB  1 
ATOM   4957 C CG  . GLN D 1 108 ? 33.227 5.385   11.024  1.00 40.08  ?  331 GLN A CG  1 
ATOM   4958 C CD  . GLN D 1 108 ? 33.062 3.880   11.070  1.00 49.03  ?  331 GLN A CD  1 
ATOM   4959 O OE1 . GLN D 1 108 ? 32.014 3.373   11.471  1.00 42.60  ?  331 GLN A OE1 1 
ATOM   4960 N NE2 . GLN D 1 108 ? 34.096 3.157   10.655  1.00 45.27  ?  331 GLN A NE2 1 
ATOM   4961 N N   . GLY D 1 109 ? 32.475 8.660   11.076  1.00 34.27  ?  332 GLY A N   1 
ATOM   4962 C CA  . GLY D 1 109 ? 31.261 9.443   10.973  1.00 34.31  ?  332 GLY A CA  1 
ATOM   4963 C C   . GLY D 1 109 ? 30.662 9.313   9.593   1.00 39.24  ?  332 GLY A C   1 
ATOM   4964 O O   . GLY D 1 109 ? 30.833 8.296   8.917   1.00 40.03  ?  332 GLY A O   1 
ATOM   4965 N N   . VAL D 1 110 ? 29.951 10.356  9.171   1.00 34.60  ?  333 VAL A N   1 
ATOM   4966 C CA  . VAL D 1 110 ? 29.279 10.381  7.878   1.00 34.89  ?  333 VAL A CA  1 
ATOM   4967 C C   . VAL D 1 110 ? 29.657 11.669  7.161   1.00 39.04  ?  333 VAL A C   1 
ATOM   4968 O O   . VAL D 1 110 ? 29.594 12.755  7.749   1.00 38.33  ?  333 VAL A O   1 
ATOM   4969 C CB  . VAL D 1 110 ? 27.748 10.273  8.025   1.00 36.24  ?  333 VAL A CB  1 
ATOM   4970 C CG1 . VAL D 1 110 ? 27.085 10.279  6.656   1.00 29.15  ?  333 VAL A CG1 1 
ATOM   4971 C CG2 . VAL D 1 110 ? 27.374 9.014   8.794   1.00 36.77  ?  333 VAL A CG2 1 
ATOM   4972 N N   . LEU D 1 111 ? 30.055 11.544  5.900   1.00 35.98  ?  334 LEU A N   1 
ATOM   4973 C CA  . LEU D 1 111 ? 30.331 12.689  5.038   1.00 34.08  ?  334 LEU A CA  1 
ATOM   4974 C C   . LEU D 1 111 ? 29.078 12.970  4.218   1.00 37.84  ?  334 LEU A C   1 
ATOM   4975 O O   . LEU D 1 111 ? 28.661 12.134  3.409   1.00 36.05  ?  334 LEU A O   1 
ATOM   4976 C CB  . LEU D 1 111 ? 31.528 12.411  4.130   1.00 33.23  ?  334 LEU A CB  1 
ATOM   4977 C CG  . LEU D 1 111 ? 32.883 13.029  4.491   1.00 39.03  ?  334 LEU A CG  1 
ATOM   4978 C CD1 . LEU D 1 111 ? 33.860 12.861  3.339   1.00 37.33  ?  334 LEU A CD1 1 
ATOM   4979 C CD2 . LEU D 1 111 ? 32.733 14.495  4.858   1.00 36.77  ?  334 LEU A CD2 1 
ATOM   4980 N N   . THR D 1 112 ? 28.476 14.135  4.431   1.00 37.50  ?  335 THR A N   1 
ATOM   4981 C CA  . THR D 1 112 ? 27.286 14.548  3.705   1.00 35.50  ?  335 THR A CA  1 
ATOM   4982 C C   . THR D 1 112 ? 27.623 15.697  2.765   1.00 37.71  ?  335 THR A C   1 
ATOM   4983 O O   . THR D 1 112 ? 28.533 16.489  3.025   1.00 42.91  ?  335 THR A O   1 
ATOM   4984 C CB  . THR D 1 112 ? 26.163 14.971  4.658   1.00 35.19  ?  335 THR A CB  1 
ATOM   4985 O OG1 . THR D 1 112 ? 26.552 16.152  5.369   1.00 36.67  ?  335 THR A OG1 1 
ATOM   4986 C CG2 . THR D 1 112 ? 25.852 13.855  5.649   1.00 40.20  ?  335 THR A CG2 1 
ATOM   4987 N N   . GLN D 1 113 ? 26.874 15.783  1.667   1.00 35.67  ?  336 GLN A N   1 
ATOM   4988 C CA  . GLN D 1 113 ? 27.133 16.786  0.647   1.00 38.24  ?  336 GLN A CA  1 
ATOM   4989 C C   . GLN D 1 113 ? 25.822 17.181  -0.014  1.00 36.54  ?  336 GLN A C   1 
ATOM   4990 O O   . GLN D 1 113 ? 24.947 16.338  -0.224  1.00 37.83  ?  336 GLN A O   1 
ATOM   4991 C CB  . GLN D 1 113 ? 28.120 16.261  -0.401  1.00 37.91  ?  336 GLN A CB  1 
ATOM   4992 C CG  . GLN D 1 113 ? 28.518 17.281  -1.451  1.00 36.50  ?  336 GLN A CG  1 
ATOM   4993 C CD  . GLN D 1 113 ? 29.497 16.717  -2.456  1.00 39.59  ?  336 GLN A CD  1 
ATOM   4994 O OE1 . GLN D 1 113 ? 29.103 16.085  -3.437  1.00 43.31  ?  336 GLN A OE1 1 
ATOM   4995 N NE2 . GLN D 1 113 ? 30.784 16.938  -2.216  1.00 35.90  ?  336 GLN A NE2 1 
ATOM   4996 N N   . THR D 1 114 ? 25.697 18.466  -0.334  1.00 36.53  ?  337 THR A N   1 
ATOM   4997 C CA  . THR D 1 114 ? 24.532 19.009  -1.019  1.00 36.09  ?  337 THR A CA  1 
ATOM   4998 C C   . THR D 1 114 ? 24.994 19.731  -2.276  1.00 40.94  ?  337 THR A C   1 
ATOM   4999 O O   . THR D 1 114 ? 25.860 20.608  -2.206  1.00 39.17  ?  337 THR A O   1 
ATOM   5000 C CB  . THR D 1 114 ? 23.752 19.973  -0.116  1.00 42.52  ?  337 THR A CB  1 
ATOM   5001 O OG1 . THR D 1 114 ? 23.021 19.231  0.870   1.00 39.98  ?  337 THR A OG1 1 
ATOM   5002 C CG2 . THR D 1 114 ? 22.779 20.810  -0.937  1.00 40.14  ?  337 THR A CG2 1 
ATOM   5003 N N   . THR D 1 115 ? 24.427 19.355  -3.420  1.00 39.16  ?  338 THR A N   1 
ATOM   5004 C CA  . THR D 1 115 ? 24.684 20.074  -4.661  1.00 39.90  ?  338 THR A CA  1 
ATOM   5005 C C   . THR D 1 115 ? 23.848 21.347  -4.666  1.00 38.86  ?  338 THR A C   1 
ATOM   5006 O O   . THR D 1 115 ? 22.616 21.289  -4.577  1.00 39.83  ?  338 THR A O   1 
ATOM   5007 C CB  . THR D 1 115 ? 24.365 19.204  -5.875  1.00 43.37  ?  338 THR A CB  1 
ATOM   5008 O OG1 . THR D 1 115 ? 25.233 18.065  -5.886  1.00 37.41  ?  338 THR A OG1 1 
ATOM   5009 C CG2 . THR D 1 115 ? 24.567 19.993  -7.164  1.00 37.99  ?  338 THR A CG2 1 
ATOM   5010 N N   . ARG D 1 116 ? 24.520 22.496  -4.764  1.00 40.18  ?  339 ARG A N   1 
ATOM   5011 C CA  . ARG D 1 116 ? 23.842 23.775  -4.574  1.00 42.51  ?  339 ARG A CA  1 
ATOM   5012 C C   . ARG D 1 116 ? 22.841 24.071  -5.684  1.00 48.10  ?  339 ARG A C   1 
ATOM   5013 O O   . ARG D 1 116 ? 21.798 24.682  -5.425  1.00 49.29  ?  339 ARG A O   1 
ATOM   5014 C CB  . ARG D 1 116 ? 24.878 24.895  -4.476  1.00 49.70  ?  339 ARG A CB  1 
ATOM   5015 C CG  . ARG D 1 116 ? 24.292 26.294  -4.465  1.00 57.71  ?  339 ARG A CG  1 
ATOM   5016 C CD  . ARG D 1 116 ? 25.382 27.354  -4.527  1.00 60.29  ?  339 ARG A CD  1 
ATOM   5017 N NE  . ARG D 1 116 ? 24.856 28.715  -4.509  1.00 76.71  ?  339 ARG A NE  1 
ATOM   5018 C CZ  . ARG D 1 116 ? 24.174 29.259  -3.510  1.00 78.68  ?  339 ARG A CZ  1 
ATOM   5019 N NH1 . ARG D 1 116 ? 23.936 28.599  -2.387  1.00 72.74  ?  339 ARG A NH1 1 
ATOM   5020 N NH2 . ARG D 1 116 ? 23.723 30.504  -3.636  1.00 71.63  ?  339 ARG A NH2 1 
ATOM   5021 N N   . THR D 1 117 ? 23.120 23.634  -6.915  1.00 44.91  ?  340 THR A N   1 
ATOM   5022 C CA  . THR D 1 117 ? 22.303 24.058  -8.047  1.00 47.46  ?  340 THR A CA  1 
ATOM   5023 C C   . THR D 1 117 ? 20.917 23.413  -8.040  1.00 48.18  ?  340 THR A C   1 
ATOM   5024 O O   . THR D 1 117 ? 19.965 24.004  -8.564  1.00 53.02  ?  340 THR A O   1 
ATOM   5025 C CB  . THR D 1 117 ? 23.035 23.765  -9.362  1.00 51.36  ?  340 THR A CB  1 
ATOM   5026 O OG1 . THR D 1 117 ? 22.517 24.608  -10.398 1.00 55.83  ?  340 THR A OG1 1 
ATOM   5027 C CG2 . THR D 1 117 ? 22.883 22.303  -9.773  1.00 48.50  ?  340 THR A CG2 1 
ATOM   5028 N N   . ASP D 1 118 ? 20.768 22.225  -7.446  1.00 50.62  ?  341 ASP A N   1 
ATOM   5029 C CA  . ASP D 1 118 ? 19.479 21.547  -7.453  1.00 50.65  ?  341 ASP A CA  1 
ATOM   5030 C C   . ASP D 1 118 ? 19.085 20.947  -6.110  1.00 46.05  ?  341 ASP A C   1 
ATOM   5031 O O   . ASP D 1 118 ? 18.021 20.327  -6.023  1.00 42.45  ?  341 ASP A O   1 
ATOM   5032 C CB  . ASP D 1 118 ? 19.458 20.442  -8.529  1.00 38.68  ?  341 ASP A CB  1 
ATOM   5033 C CG  . ASP D 1 118 ? 20.456 19.333  -8.250  1.00 49.97  ?  341 ASP A CG  1 
ATOM   5034 O OD1 . ASP D 1 118 ? 21.398 19.561  -7.462  1.00 53.18  ?  341 ASP A OD1 1 
ATOM   5035 O OD2 . ASP D 1 118 ? 20.296 18.230  -8.816  1.00 51.45  ?  341 ASP A OD2 1 
ATOM   5036 N N   . GLY D 1 119 ? 19.893 21.109  -5.066  1.00 44.58  ?  342 GLY A N   1 
ATOM   5037 C CA  . GLY D 1 119 ? 19.534 20.593  -3.762  1.00 38.93  ?  342 GLY A CA  1 
ATOM   5038 C C   . GLY D 1 119 ? 19.603 19.091  -3.612  1.00 46.87  ?  342 GLY A C   1 
ATOM   5039 O O   . GLY D 1 119 ? 19.041 18.557  -2.651  1.00 40.72  ?  342 GLY A O   1 
ATOM   5040 N N   . SER D 1 120 ? 20.263 18.389  -4.530  1.00 41.50  ?  343 SER A N   1 
ATOM   5041 C CA  . SER D 1 120 ? 20.455 16.954  -4.372  1.00 43.11  ?  343 SER A CA  1 
ATOM   5042 C C   . SER D 1 120 ? 21.509 16.686  -3.304  1.00 40.13  ?  343 SER A C   1 
ATOM   5043 O O   . SER D 1 120 ? 22.508 17.404  -3.200  1.00 38.22  ?  343 SER A O   1 
ATOM   5044 C CB  . SER D 1 120 ? 20.869 16.315  -5.699  1.00 43.46  ?  343 SER A CB  1 
ATOM   5045 O OG  . SER D 1 120 ? 22.207 16.636  -6.041  1.00 38.60  ?  343 SER A OG  1 
ATOM   5046 N N   . THR D 1 121 ? 21.281 15.647  -2.505  1.00 38.42  ?  344 THR A N   1 
ATOM   5047 C CA  . THR D 1 121 ? 22.133 15.341  -1.367  1.00 40.63  ?  344 THR A CA  1 
ATOM   5048 C C   . THR D 1 121 ? 22.647 13.908  -1.451  1.00 43.26  ?  344 THR A C   1 
ATOM   5049 O O   . THR D 1 121 ? 22.129 13.078  -2.203  1.00 40.50  ?  344 THR A O   1 
ATOM   5050 C CB  . THR D 1 121 ? 21.388 15.549  -0.041  1.00 41.47  ?  344 THR A CB  1 
ATOM   5051 O OG1 . THR D 1 121 ? 20.315 14.605  0.066   1.00 35.11  ?  344 THR A OG1 1 
ATOM   5052 C CG2 . THR D 1 121 ? 20.824 16.959  0.038   1.00 35.85  ?  344 THR A CG2 1 
ATOM   5053 N N   . ARG D 1 122 ? 23.681 13.631  -0.660  1.00 41.16  ?  345 ARG A N   1 
ATOM   5054 C CA  . ARG D 1 122 ? 24.287 12.308  -0.608  1.00 41.32  ?  345 ARG A CA  1 
ATOM   5055 C C   . ARG D 1 122 ? 25.114 12.199  0.664   1.00 40.76  ?  345 ARG A C   1 
ATOM   5056 O O   . ARG D 1 122 ? 25.690 13.185  1.132   1.00 40.27  ?  345 ARG A O   1 
ATOM   5057 C CB  . ARG D 1 122 ? 25.157 12.036  -1.841  1.00 40.84  ?  345 ARG A CB  1 
ATOM   5058 C CG  . ARG D 1 122 ? 26.368 12.944  -1.963  1.00 39.94  ?  345 ARG A CG  1 
ATOM   5059 C CD  . ARG D 1 122 ? 26.730 13.181  -3.417  1.00 49.52  ?  345 ARG A CD  1 
ATOM   5060 N NE  . ARG D 1 122 ? 25.582 13.615  -4.205  1.00 47.15  ?  345 ARG A NE  1 
ATOM   5061 C CZ  . ARG D 1 122 ? 25.338 14.875  -4.537  1.00 42.48  ?  345 ARG A CZ  1 
ATOM   5062 N NH1 . ARG D 1 122 ? 26.139 15.858  -4.160  1.00 39.80  ?  345 ARG A NH1 1 
ATOM   5063 N NH2 . ARG D 1 122 ? 24.260 15.156  -5.266  1.00 45.96  ?  345 ARG A NH2 1 
ATOM   5064 N N   . GLY D 1 123 ? 25.159 10.990  1.219   1.00 38.76  ?  346 GLY A N   1 
ATOM   5065 C CA  . GLY D 1 123 ? 25.915 10.739  2.432   1.00 38.28  ?  346 GLY A CA  1 
ATOM   5066 C C   . GLY D 1 123 ? 26.590 9.384   2.432   1.00 46.48  ?  346 GLY A C   1 
ATOM   5067 O O   . GLY D 1 123 ? 26.002 8.394   1.985   1.00 45.04  ?  346 GLY A O   1 
ATOM   5068 N N   . HIS D 1 124 ? 27.823 9.321   2.931   1.00 42.98  ?  347 HIS A N   1 
ATOM   5069 C CA  . HIS D 1 124 ? 28.593 8.085   2.926   1.00 39.44  ?  347 HIS A CA  1 
ATOM   5070 C C   . HIS D 1 124 ? 29.372 7.951   4.226   1.00 43.41  ?  347 HIS A C   1 
ATOM   5071 O O   . HIS D 1 124 ? 29.712 8.946   4.872   1.00 40.25  ?  347 HIS A O   1 
ATOM   5072 C CB  . HIS D 1 124 ? 29.555 8.029   1.735   1.00 40.67  ?  347 HIS A CB  1 
ATOM   5073 C CG  . HIS D 1 124 ? 28.865 7.997   0.407   1.00 48.31  ?  347 HIS A CG  1 
ATOM   5074 N ND1 . HIS D 1 124 ? 28.246 6.867   -0.082  1.00 49.49  ?  347 HIS A ND1 1 
ATOM   5075 C CD2 . HIS D 1 124 ? 28.689 8.959   -0.529  1.00 42.12  ?  347 HIS A CD2 1 
ATOM   5076 C CE1 . HIS D 1 124 ? 27.721 7.133   -1.264  1.00 48.67  ?  347 HIS A CE1 1 
ATOM   5077 N NE2 . HIS D 1 124 ? 27.974 8.395   -1.558  1.00 49.94  ?  347 HIS A NE2 1 
ATOM   5078 N N   . LYS D 1 125 ? 29.651 6.704   4.598   1.00 43.46  ?  348 LYS A N   1 
ATOM   5079 C CA  . LYS D 1 125 ? 30.480 6.432   5.763   1.00 40.22  ?  348 LYS A CA  1 
ATOM   5080 C C   . LYS D 1 125 ? 31.897 6.933   5.518   1.00 38.16  ?  348 LYS A C   1 
ATOM   5081 O O   . LYS D 1 125 ? 32.478 6.691   4.457   1.00 40.84  ?  348 LYS A O   1 
ATOM   5082 C CB  . LYS D 1 125 ? 30.498 4.932   6.065   1.00 43.28  ?  348 LYS A CB  1 
ATOM   5083 C CG  . LYS D 1 125 ? 31.418 4.543   7.215   1.00 40.31  ?  348 LYS A CG  1 
ATOM   5084 C CD  . LYS D 1 125 ? 31.743 3.057   7.188   1.00 51.53  ?  348 LYS A CD  1 
ATOM   5085 C CE  . LYS D 1 125 ? 30.534 2.223   7.570   1.00 54.01  ?  348 LYS A CE  1 
ATOM   5086 N NZ  . LYS D 1 125 ? 30.923 0.880   8.082   1.00 61.31  ?  348 LYS A NZ  1 
ATOM   5087 N N   . ALA D 1 126 ? 32.455 7.632   6.502   1.00 34.90  ?  349 ALA A N   1 
ATOM   5088 C CA  . ALA D 1 126 ? 33.792 8.189   6.380   1.00 34.89  ?  349 ALA A CA  1 
ATOM   5089 C C   . ALA D 1 126 ? 34.521 8.064   7.709   1.00 40.86  ?  349 ALA A C   1 
ATOM   5090 O O   . ALA D 1 126 ? 33.912 8.132   8.780   1.00 41.12  ?  349 ALA A O   1 
ATOM   5091 C CB  . ALA D 1 126 ? 33.752 9.657   5.936   1.00 37.79  ?  349 ALA A CB  1 
ATOM   5092 N N   . THR D 1 127 ? 35.836 7.881   7.624   1.00 39.95  ?  350 THR A N   1 
ATOM   5093 C CA  . THR D 1 127 ? 36.698 7.783   8.793   1.00 46.59  ?  350 THR A CA  1 
ATOM   5094 C C   . THR D 1 127 ? 37.898 8.694   8.589   1.00 41.58  ?  350 THR A C   1 
ATOM   5095 O O   . THR D 1 127 ? 38.513 8.681   7.518   1.00 40.16  ?  350 THR A O   1 
ATOM   5096 C CB  . THR D 1 127 ? 37.158 6.337   9.031   1.00 38.94  ?  350 THR A CB  1 
ATOM   5097 O OG1 . THR D 1 127 ? 36.014 5.482   9.146   1.00 39.47  ?  350 THR A OG1 1 
ATOM   5098 C CG2 . THR D 1 127 ? 37.984 6.242   10.307  1.00 36.09  ?  350 THR A CG2 1 
ATOM   5099 N N   . VAL D 1 128 ? 38.222 9.485   9.608   1.00 36.38  ?  351 VAL A N   1 
ATOM   5100 C CA  . VAL D 1 128 ? 39.378 10.374  9.585   1.00 37.15  ?  351 VAL A CA  1 
ATOM   5101 C C   . VAL D 1 128 ? 40.418 9.830   10.555  1.00 40.44  ?  351 VAL A C   1 
ATOM   5102 O O   . VAL D 1 128 ? 40.101 9.517   11.709  1.00 38.78  ?  351 VAL A O   1 
ATOM   5103 C CB  . VAL D 1 128 ? 38.990 11.825  9.926   1.00 39.83  ?  351 VAL A CB  1 
ATOM   5104 C CG1 . VAL D 1 128 ? 38.125 11.884  11.180  1.00 36.03  ?  351 VAL A CG1 1 
ATOM   5105 C CG2 . VAL D 1 128 ? 40.234 12.690  10.080  1.00 38.14  ?  351 VAL A CG2 1 
ATOM   5106 N N   . TYR D 1 129 ? 41.656 9.706   10.081  1.00 40.21  ?  352 TYR A N   1 
ATOM   5107 C CA  . TYR D 1 129 ? 42.763 9.165   10.868  1.00 42.29  ?  352 TYR A CA  1 
ATOM   5108 C C   . TYR D 1 129 ? 43.596 10.349  11.346  1.00 44.01  ?  352 TYR A C   1 
ATOM   5109 O O   . TYR D 1 129 ? 44.481 10.836  10.640  1.00 42.42  ?  352 TYR A O   1 
ATOM   5110 C CB  . TYR D 1 129 ? 43.588 8.183   10.038  1.00 43.59  ?  352 TYR A CB  1 
ATOM   5111 C CG  . TYR D 1 129 ? 42.820 6.963   9.564   1.00 44.55  ?  352 TYR A CG  1 
ATOM   5112 C CD1 . TYR D 1 129 ? 41.842 7.066   8.581   1.00 50.88  ?  352 TYR A CD1 1 
ATOM   5113 C CD2 . TYR D 1 129 ? 43.081 5.707   10.093  1.00 46.19  ?  352 TYR A CD2 1 
ATOM   5114 C CE1 . TYR D 1 129 ? 41.140 5.956   8.148   1.00 55.30  ?  352 TYR A CE1 1 
ATOM   5115 C CE2 . TYR D 1 129 ? 42.387 4.590   9.665   1.00 50.11  ?  352 TYR A CE2 1 
ATOM   5116 C CZ  . TYR D 1 129 ? 41.417 4.720   8.694   1.00 52.19  ?  352 TYR A CZ  1 
ATOM   5117 O OH  . TYR D 1 129 ? 40.727 3.609   8.271   1.00 60.01  ?  352 TYR A OH  1 
ATOM   5118 N N   . THR D 1 130 ? 43.307 10.819  12.564  1.00 39.40  ?  353 THR A N   1 
ATOM   5119 C CA  . THR D 1 130 ? 43.971 12.009  13.090  1.00 43.43  ?  353 THR A CA  1 
ATOM   5120 C C   . THR D 1 130 ? 45.454 11.795  13.355  1.00 46.86  ?  353 THR A C   1 
ATOM   5121 O O   . THR D 1 130 ? 46.176 12.780  13.550  1.00 44.13  ?  353 THR A O   1 
ATOM   5122 C CB  . THR D 1 130 ? 43.291 12.482  14.378  1.00 43.75  ?  353 THR A CB  1 
ATOM   5123 O OG1 . THR D 1 130 ? 43.432 11.480  15.394  1.00 42.64  ?  353 THR A OG1 1 
ATOM   5124 C CG2 . THR D 1 130 ? 41.815 12.760  14.137  1.00 39.49  ?  353 THR A CG2 1 
ATOM   5125 N N   . GLY D 1 131 ? 45.916 10.547  13.366  1.00 44.38  ?  354 GLY A N   1 
ATOM   5126 C CA  . GLY D 1 131 ? 47.321 10.228  13.471  1.00 48.15  ?  354 GLY A CA  1 
ATOM   5127 C C   . GLY D 1 131 ? 48.034 10.036  12.155  1.00 50.46  ?  354 GLY A C   1 
ATOM   5128 O O   . GLY D 1 131 ? 49.259 9.877   12.149  1.00 52.38  ?  354 GLY A O   1 
ATOM   5129 N N   . SER D 1 132 ? 47.310 10.053  11.037  1.00 47.92  ?  355 SER A N   1 
ATOM   5130 C CA  . SER D 1 132 ? 47.924 9.847   9.734   1.00 50.47  ?  355 SER A CA  1 
ATOM   5131 C C   . SER D 1 132 ? 48.784 11.047  9.340   1.00 52.75  ?  355 SER A C   1 
ATOM   5132 O O   . SER D 1 132 ? 48.650 12.149  9.879   1.00 57.54  ?  355 SER A O   1 
ATOM   5133 C CB  . SER D 1 132 ? 46.854 9.599   8.671   1.00 44.90  ?  355 SER A CB  1 
ATOM   5134 O OG  . SER D 1 132 ? 46.151 10.792  8.372   1.00 49.63  ?  355 SER A OG  1 
ATOM   5135 N N   . ALA D 1 133 ? 49.674 10.819  8.372   1.00 52.18  ?  356 ALA A N   1 
ATOM   5136 C CA  . ALA D 1 133 ? 50.605 11.857  7.949   1.00 56.82  ?  356 ALA A CA  1 
ATOM   5137 C C   . ALA D 1 133 ? 49.919 12.991  7.199   1.00 55.04  ?  356 ALA A C   1 
ATOM   5138 O O   . ALA D 1 133 ? 50.461 14.099  7.156   1.00 57.54  ?  356 ALA A O   1 
ATOM   5139 C CB  . ALA D 1 133 ? 51.707 11.251  7.079   1.00 59.82  ?  356 ALA A CB  1 
ATOM   5140 N N   . ASP D 1 134 ? 48.748 12.745  6.614   1.00 57.40  ?  357 ASP A N   1 
ATOM   5141 C CA  . ASP D 1 134 ? 48.041 13.752  5.834   1.00 54.49  ?  357 ASP A CA  1 
ATOM   5142 C C   . ASP D 1 134 ? 46.996 14.508  6.645   1.00 53.87  ?  357 ASP A C   1 
ATOM   5143 O O   . ASP D 1 134 ? 46.236 15.298  6.075   1.00 53.57  ?  357 ASP A O   1 
ATOM   5144 C CB  . ASP D 1 134 ? 47.390 13.107  4.611   1.00 61.26  ?  357 ASP A CB  1 
ATOM   5145 C CG  . ASP D 1 134 ? 48.360 12.936  3.459   1.00 72.33  ?  357 ASP A CG  1 
ATOM   5146 O OD1 . ASP D 1 134 ? 48.947 13.947  3.018   1.00 70.87  ?  357 ASP A OD1 1 
ATOM   5147 O OD2 . ASP D 1 134 ? 48.538 11.789  2.995   1.00 75.16  ?  357 ASP A OD2 1 
ATOM   5148 N N   . PHE D 1 135 ? 46.933 14.282  7.955   1.00 51.33  ?  358 PHE A N   1 
ATOM   5149 C CA  . PHE D 1 135 ? 46.039 15.042  8.826   1.00 45.54  ?  358 PHE A CA  1 
ATOM   5150 C C   . PHE D 1 135 ? 46.712 16.369  9.148   1.00 44.61  ?  358 PHE A C   1 
ATOM   5151 O O   . PHE D 1 135 ? 47.530 16.459  10.067  1.00 47.57  ?  358 PHE A O   1 
ATOM   5152 C CB  . PHE D 1 135 ? 45.720 14.255  10.093  1.00 45.63  ?  358 PHE A CB  1 
ATOM   5153 C CG  . PHE D 1 135 ? 44.734 14.935  10.999  1.00 42.36  ?  358 PHE A CG  1 
ATOM   5154 C CD1 . PHE D 1 135 ? 43.388 14.986  10.672  1.00 40.45  ?  358 PHE A CD1 1 
ATOM   5155 C CD2 . PHE D 1 135 ? 45.151 15.523  12.183  1.00 41.71  ?  358 PHE A CD2 1 
ATOM   5156 C CE1 . PHE D 1 135 ? 42.478 15.609  11.508  1.00 37.43  ?  358 PHE A CE1 1 
ATOM   5157 C CE2 . PHE D 1 135 ? 44.247 16.148  13.024  1.00 39.26  ?  358 PHE A CE2 1 
ATOM   5158 C CZ  . PHE D 1 135 ? 42.908 16.190  12.685  1.00 39.35  ?  358 PHE A CZ  1 
ATOM   5159 N N   . ALA D 1 136 ? 46.379 17.406  8.384   1.00 42.59  ?  359 ALA A N   1 
ATOM   5160 C CA  . ALA D 1 136 ? 46.959 18.737  8.559   1.00 45.31  ?  359 ALA A CA  1 
ATOM   5161 C C   . ALA D 1 136 ? 45.855 19.787  8.540   1.00 42.76  ?  359 ALA A C   1 
ATOM   5162 O O   . ALA D 1 136 ? 45.772 20.605  7.614   1.00 43.98  ?  359 ALA A O   1 
ATOM   5163 C CB  . ALA D 1 136 ? 48.003 19.023  7.477   1.00 42.68  ?  359 ALA A CB  1 
ATOM   5164 N N   . PRO D 1 137 ? 44.986 19.797  9.555   1.00 41.66  ?  360 PRO A N   1 
ATOM   5165 C CA  . PRO D 1 137 ? 43.929 20.821  9.588   1.00 43.49  ?  360 PRO A CA  1 
ATOM   5166 C C   . PRO D 1 137 ? 44.465 22.234  9.721   1.00 40.81  ?  360 PRO A C   1 
ATOM   5167 O O   . PRO D 1 137 ? 43.832 23.173  9.223   1.00 42.53  ?  360 PRO A O   1 
ATOM   5168 C CB  . PRO D 1 137 ? 43.090 20.417  10.809  1.00 35.68  ?  360 PRO A CB  1 
ATOM   5169 C CG  . PRO D 1 137 ? 44.030 19.645  11.668  1.00 39.90  ?  360 PRO A CG  1 
ATOM   5170 C CD  . PRO D 1 137 ? 44.915 18.898  10.721  1.00 37.69  ?  360 PRO A CD  1 
ATOM   5171 N N   . LYS D 1 138 ? 45.614 22.415  10.380  1.00 41.39  ?  361 LYS A N   1 
ATOM   5172 C CA  . LYS D 1 138 ? 46.198 23.747  10.493  1.00 43.67  ?  361 LYS A CA  1 
ATOM   5173 C C   . LYS D 1 138 ? 46.529 24.327  9.124   1.00 43.24  ?  361 LYS A C   1 
ATOM   5174 O O   . LYS D 1 138 ? 46.409 25.541  8.919   1.00 47.96  ?  361 LYS A O   1 
ATOM   5175 C CB  . LYS D 1 138 ? 47.447 23.701  11.374  1.00 46.22  ?  361 LYS A CB  1 
ATOM   5176 C CG  . LYS D 1 138 ? 48.122 25.051  11.590  1.00 39.07  ?  361 LYS A CG  1 
ATOM   5177 C CD  . LYS D 1 138 ? 47.165 26.075  12.176  1.00 41.21  ?  361 LYS A CD  1 
ATOM   5178 C CE  . LYS D 1 138 ? 47.870 27.400  12.427  1.00 45.41  ?  361 LYS A CE  1 
ATOM   5179 N NZ  . LYS D 1 138 ? 46.906 28.520  12.607  1.00 46.21  ?  361 LYS A NZ  1 
ATOM   5180 N N   . LEU D 1 139 ? 46.939 23.481  8.178   1.00 46.27  ?  362 LEU A N   1 
ATOM   5181 C CA  . LEU D 1 139 ? 47.135 23.919  6.802   1.00 45.84  ?  362 LEU A CA  1 
ATOM   5182 C C   . LEU D 1 139 ? 45.839 23.944  6.003   1.00 44.42  ?  362 LEU A C   1 
ATOM   5183 O O   . LEU D 1 139 ? 45.846 24.406  4.858   1.00 45.79  ?  362 LEU A O   1 
ATOM   5184 C CB  . LEU D 1 139 ? 48.148 23.011  6.098   1.00 46.78  ?  362 LEU A CB  1 
ATOM   5185 C CG  . LEU D 1 139 ? 49.545 22.929  6.712   1.00 49.89  ?  362 LEU A CG  1 
ATOM   5186 C CD1 . LEU D 1 139 ? 50.368 21.855  6.017   1.00 45.03  ?  362 LEU A CD1 1 
ATOM   5187 C CD2 . LEU D 1 139 ? 50.244 24.276  6.636   1.00 45.24  ?  362 LEU A CD2 1 
ATOM   5188 N N   . GLY D 1 140 ? 44.739 23.457  6.574   1.00 45.44  ?  363 GLY A N   1 
ATOM   5189 C CA  . GLY D 1 140 ? 43.464 23.464  5.889   1.00 43.53  ?  363 GLY A CA  1 
ATOM   5190 C C   . GLY D 1 140 ? 43.165 22.233  5.066   1.00 44.56  ?  363 GLY A C   1 
ATOM   5191 O O   . GLY D 1 140 ? 42.383 22.319  4.111   1.00 40.01  ?  363 GLY A O   1 
ATOM   5192 N N   . ARG D 1 141 ? 43.749 21.084  5.408   1.00 41.80  ?  364 ARG A N   1 
ATOM   5193 C CA  . ARG D 1 141 ? 43.598 19.868  4.619   1.00 44.80  ?  364 ARG A CA  1 
ATOM   5194 C C   . ARG D 1 141 ? 43.406 18.674  5.541   1.00 42.47  ?  364 ARG A C   1 
ATOM   5195 O O   . ARG D 1 141 ? 44.222 18.443  6.437   1.00 39.01  ?  364 ARG A O   1 
ATOM   5196 C CB  . ARG D 1 141 ? 44.820 19.632  3.725   1.00 41.86  ?  364 ARG A CB  1 
ATOM   5197 C CG  . ARG D 1 141 ? 44.901 20.526  2.503   1.00 49.72  ?  364 ARG A CG  1 
ATOM   5198 C CD  . ARG D 1 141 ? 46.020 20.069  1.576   1.00 59.55  ?  364 ARG A CD  1 
ATOM   5199 N NE  . ARG D 1 141 ? 46.821 19.004  2.171   1.00 65.42  ?  364 ARG A NE  1 
ATOM   5200 C CZ  . ARG D 1 141 ? 48.021 19.178  2.709   1.00 65.12  ?  364 ARG A CZ  1 
ATOM   5201 N NH1 . ARG D 1 141 ? 48.604 20.366  2.732   1.00 62.86  ?  364 ARG A NH1 1 
ATOM   5202 N NH2 . ARG D 1 141 ? 48.652 18.134  3.240   1.00 57.96  ?  364 ARG A NH2 1 
ATOM   5203 N N   . VAL D 1 142 ? 42.344 17.908  5.305   1.00 40.84  ?  365 VAL A N   1 
ATOM   5204 C CA  . VAL D 1 142 ? 42.043 16.709  6.078   1.00 40.00  ?  365 VAL A CA  1 
ATOM   5205 C C   . VAL D 1 142 ? 41.634 15.605  5.110   1.00 45.11  ?  365 VAL A C   1 
ATOM   5206 O O   . VAL D 1 142 ? 40.886 15.848  4.157   1.00 45.87  ?  365 VAL A O   1 
ATOM   5207 C CB  . VAL D 1 142 ? 40.938 16.974  7.124   1.00 40.13  ?  365 VAL A CB  1 
ATOM   5208 C CG1 . VAL D 1 142 ? 40.366 15.671  7.658   1.00 42.82  ?  365 VAL A CG1 1 
ATOM   5209 C CG2 . VAL D 1 142 ? 41.480 17.825  8.264   1.00 41.41  ?  365 VAL A CG2 1 
ATOM   5210 N N   . GLN D 1 143 ? 42.135 14.395  5.347   1.00 45.17  ?  366 GLN A N   1 
ATOM   5211 C CA  . GLN D 1 143 ? 41.852 13.243  4.501   1.00 45.44  ?  366 GLN A CA  1 
ATOM   5212 C C   . GLN D 1 143 ? 40.775 12.370  5.133   1.00 43.66  ?  366 GLN A C   1 
ATOM   5213 O O   . GLN D 1 143 ? 40.815 12.088  6.335   1.00 46.07  ?  366 GLN A O   1 
ATOM   5214 C CB  . GLN D 1 143 ? 43.122 12.422  4.263   1.00 45.60  ?  366 GLN A CB  1 
ATOM   5215 C CG  . GLN D 1 143 ? 43.719 12.585  2.875   1.00 57.47  ?  366 GLN A CG  1 
ATOM   5216 C CD  . GLN D 1 143 ? 44.518 11.372  2.442   1.00 66.26  ?  366 GLN A CD  1 
ATOM   5217 O OE1 . GLN D 1 143 ? 43.988 10.266  2.353   1.00 61.30  ?  366 GLN A OE1 1 
ATOM   5218 N NE2 . GLN D 1 143 ? 45.801 11.574  2.164   1.00 66.83  ?  366 GLN A NE2 1 
ATOM   5219 N N   . PHE D 1 144 ? 39.817 11.939  4.314   1.00 38.90  ?  367 PHE A N   1 
ATOM   5220 C CA  . PHE D 1 144 ? 38.714 11.094  4.754   1.00 38.41  ?  367 PHE A CA  1 
ATOM   5221 C C   . PHE D 1 144 ? 38.701 9.813   3.937   1.00 46.25  ?  367 PHE A C   1 
ATOM   5222 O O   . PHE D 1 144 ? 38.696 9.861   2.702   1.00 43.65  ?  367 PHE A O   1 
ATOM   5223 C CB  . PHE D 1 144 ? 37.368 11.810  4.603   1.00 41.99  ?  367 PHE A CB  1 
ATOM   5224 C CG  . PHE D 1 144 ? 37.157 12.930  5.581   1.00 41.54  ?  367 PHE A CG  1 
ATOM   5225 C CD1 . PHE D 1 144 ? 36.797 12.662  6.891   1.00 39.37  ?  367 PHE A CD1 1 
ATOM   5226 C CD2 . PHE D 1 144 ? 37.310 14.248  5.188   1.00 41.07  ?  367 PHE A CD2 1 
ATOM   5227 C CE1 . PHE D 1 144 ? 36.599 13.689  7.793   1.00 41.82  ?  367 PHE A CE1 1 
ATOM   5228 C CE2 . PHE D 1 144 ? 37.114 15.280  6.084   1.00 40.93  ?  367 PHE A CE2 1 
ATOM   5229 C CZ  . PHE D 1 144 ? 36.759 15.001  7.388   1.00 40.48  ?  367 PHE A CZ  1 
ATOM   5230 N N   . GLU D 1 145 ? 38.683 8.672   4.621   1.00 42.10  ?  368 GLU A N   1 
ATOM   5231 C CA  . GLU D 1 145 ? 38.530 7.378   3.967   1.00 47.61  ?  368 GLU A CA  1 
ATOM   5232 C C   . GLU D 1 145 ? 37.047 7.027   3.955   1.00 45.69  ?  368 GLU A C   1 
ATOM   5233 O O   . GLU D 1 145 ? 36.438 6.843   5.014   1.00 46.03  ?  368 GLU A O   1 
ATOM   5234 C CB  . GLU D 1 145 ? 39.349 6.307   4.684   1.00 49.15  ?  368 GLU A CB  1 
ATOM   5235 C CG  . GLU D 1 145 ? 39.101 4.897   4.178   1.00 60.27  ?  368 GLU A CG  1 
ATOM   5236 C CD  . GLU D 1 145 ? 39.036 3.877   5.300   1.00 74.30  ?  368 GLU A CD  1 
ATOM   5237 O OE1 . GLU D 1 145 ? 40.102 3.502   5.831   1.00 76.25  ?  368 GLU A OE1 1 
ATOM   5238 O OE2 . GLU D 1 145 ? 37.914 3.453   5.650   1.00 78.03  ?  368 GLU A OE2 1 
ATOM   5239 N N   . THR D 1 146 ? 36.466 6.938   2.764   1.00 42.77  ?  369 THR A N   1 
ATOM   5240 C CA  . THR D 1 146 ? 35.043 6.689   2.596   1.00 41.59  ?  369 THR A CA  1 
ATOM   5241 C C   . THR D 1 146 ? 34.820 5.310   1.980   1.00 48.20  ?  369 THR A C   1 
ATOM   5242 O O   . THR D 1 146 ? 35.758 4.539   1.763   1.00 48.85  ?  369 THR A O   1 
ATOM   5243 C CB  . THR D 1 146 ? 34.403 7.778   1.732   1.00 44.72  ?  369 THR A CB  1 
ATOM   5244 O OG1 . THR D 1 146 ? 34.690 7.524   0.354   1.00 46.61  ?  369 THR A OG1 1 
ATOM   5245 C CG2 . THR D 1 146 ? 34.946 9.148   2.112   1.00 42.20  ?  369 THR A CG2 1 
ATOM   5246 N N   . ASP D 1 147 ? 33.552 5.004   1.700   1.00 46.22  ?  370 ASP A N   1 
ATOM   5247 C CA  . ASP D 1 147 ? 33.170 3.743   1.075   1.00 53.44  ?  370 ASP A CA  1 
ATOM   5248 C C   . ASP D 1 147 ? 32.663 3.930   -0.354  1.00 52.66  ?  370 ASP A C   1 
ATOM   5249 O O   . ASP D 1 147 ? 32.047 3.018   -0.914  1.00 55.11  ?  370 ASP A O   1 
ATOM   5250 C CB  . ASP D 1 147 ? 32.128 3.020   1.932   1.00 56.33  ?  370 ASP A CB  1 
ATOM   5251 C CG  . ASP D 1 147 ? 30.725 3.585   1.770   1.00 59.02  ?  370 ASP A CG  1 
ATOM   5252 O OD1 . ASP D 1 147 ? 30.587 4.792   1.482   1.00 53.29  ?  370 ASP A OD1 1 
ATOM   5253 O OD2 . ASP D 1 147 ? 29.758 2.812   1.929   1.00 68.65  ?  370 ASP A OD2 1 
ATOM   5254 N N   . THR D 1 148 ? 32.911 5.094   -0.952  1.00 53.29  ?  371 THR A N   1 
ATOM   5255 C CA  . THR D 1 148 ? 32.569 5.359   -2.342  1.00 50.49  ?  371 THR A CA  1 
ATOM   5256 C C   . THR D 1 148 ? 33.756 6.008   -3.039  1.00 52.50  ?  371 THR A C   1 
ATOM   5257 O O   . THR D 1 148 ? 34.534 6.744   -2.425  1.00 47.28  ?  371 THR A O   1 
ATOM   5258 C CB  . THR D 1 148 ? 31.319 6.257   -2.465  1.00 52.26  ?  371 THR A CB  1 
ATOM   5259 O OG1 . THR D 1 148 ? 30.676 6.019   -3.723  1.00 58.05  ?  371 THR A OG1 1 
ATOM   5260 C CG2 . THR D 1 148 ? 31.680 7.735   -2.351  1.00 52.55  ?  371 THR A CG2 1 
ATOM   5261 N N   . ASP D 1 149 ? 33.901 5.714   -4.332  1.00 52.06  ?  372 ASP A N   1 
ATOM   5262 C CA  . ASP D 1 149 ? 35.037 6.193   -5.106  1.00 49.65  ?  372 ASP A CA  1 
ATOM   5263 C C   . ASP D 1 149 ? 34.657 7.167   -6.213  1.00 52.28  ?  372 ASP A C   1 
ATOM   5264 O O   . ASP D 1 149 ? 35.553 7.666   -6.904  1.00 57.48  ?  372 ASP A O   1 
ATOM   5265 C CB  . ASP D 1 149 ? 35.812 5.011   -5.707  1.00 61.85  ?  372 ASP A CB  1 
ATOM   5266 C CG  . ASP D 1 149 ? 34.939 4.107   -6.557  1.00 64.12  ?  372 ASP A CG  1 
ATOM   5267 O OD1 . ASP D 1 149 ? 33.737 3.969   -6.248  1.00 62.26  ?  372 ASP A OD1 1 
ATOM   5268 O OD2 . ASP D 1 149 ? 35.460 3.531   -7.536  1.00 68.33  ?  372 ASP A OD2 1 
ATOM   5269 N N   . ARG D 1 150 ? 33.366 7.443   -6.415  1.00 52.50  ?  373 ARG A N   1 
ATOM   5270 C CA  . ARG D 1 150 ? 32.947 8.418   -7.420  1.00 51.91  ?  373 ARG A CA  1 
ATOM   5271 C C   . ARG D 1 150 ? 31.783 9.301   -6.996  1.00 51.83  ?  373 ARG A C   1 
ATOM   5272 O O   . ARG D 1 150 ? 31.475 10.251  -7.722  1.00 51.04  ?  373 ARG A O   1 
ATOM   5273 C CB  . ARG D 1 150 ? 32.557 7.721   -8.736  1.00 54.78  ?  373 ARG A CB  1 
ATOM   5274 C CG  . ARG D 1 150 ? 33.099 6.312   -8.932  1.00 61.19  ?  373 ARG A CG  1 
ATOM   5275 C CD  . ARG D 1 150 ? 32.806 5.807   -10.339 1.00 66.38  ?  373 ARG A CD  1 
ATOM   5276 N NE  . ARG D 1 150 ? 32.658 4.356   -10.388 1.00 73.93  ?  373 ARG A NE  1 
ATOM   5277 C CZ  . ARG D 1 150 ? 33.669 3.498   -10.394 1.00 72.68  ?  373 ARG A CZ  1 
ATOM   5278 N NH1 . ARG D 1 150 ? 34.926 3.909   -10.355 1.00 67.82  ?  373 ARG A NH1 1 
ATOM   5279 N NH2 . ARG D 1 150 ? 33.414 2.193   -10.440 1.00 72.28  ?  373 ARG A NH2 1 
ATOM   5280 N N   . ASP D 1 151 ? 31.129 9.042   -5.862  1.00 50.35  ?  374 ASP A N   1 
ATOM   5281 C CA  . ASP D 1 151 ? 29.841 9.668   -5.587  1.00 54.10  ?  374 ASP A CA  1 
ATOM   5282 C C   . ASP D 1 151 ? 29.948 11.106  -5.092  1.00 51.84  ?  374 ASP A C   1 
ATOM   5283 O O   . ASP D 1 151 ? 28.957 11.840  -5.166  1.00 53.01  ?  374 ASP A O   1 
ATOM   5284 C CB  . ASP D 1 151 ? 29.062 8.837   -4.565  1.00 54.59  ?  374 ASP A CB  1 
ATOM   5285 C CG  . ASP D 1 151 ? 27.568 8.851   -4.823  1.00 57.67  ?  374 ASP A CG  1 
ATOM   5286 O OD1 . ASP D 1 151 ? 26.933 9.910   -4.629  1.00 57.55  ?  374 ASP A OD1 1 
ATOM   5287 O OD2 . ASP D 1 151 ? 27.026 7.799   -5.219  1.00 71.59  ?  374 ASP A OD2 1 
ATOM   5288 N N   . PHE D 1 152 ? 31.104 11.530  -4.592  1.00 49.09  ?  375 PHE A N   1 
ATOM   5289 C CA  . PHE D 1 152 ? 31.249 12.877  -4.057  1.00 44.16  ?  375 PHE A CA  1 
ATOM   5290 C C   . PHE D 1 152 ? 31.687 13.836  -5.157  1.00 44.75  ?  375 PHE A C   1 
ATOM   5291 O O   . PHE D 1 152 ? 32.695 13.603  -5.831  1.00 48.26  ?  375 PHE A O   1 
ATOM   5292 C CB  . PHE D 1 152 ? 32.246 12.896  -2.900  1.00 43.89  ?  375 PHE A CB  1 
ATOM   5293 C CG  . PHE D 1 152 ? 31.655 12.463  -1.589  1.00 42.75  ?  375 PHE A CG  1 
ATOM   5294 C CD1 . PHE D 1 152 ? 30.549 13.112  -1.065  1.00 40.21  ?  375 PHE A CD1 1 
ATOM   5295 C CD2 . PHE D 1 152 ? 32.200 11.403  -0.883  1.00 40.26  ?  375 PHE A CD2 1 
ATOM   5296 C CE1 . PHE D 1 152 ? 29.998 12.716  0.140   1.00 35.87  ?  375 PHE A CE1 1 
ATOM   5297 C CE2 . PHE D 1 152 ? 31.653 11.000  0.322   1.00 41.59  ?  375 PHE A CE2 1 
ATOM   5298 C CZ  . PHE D 1 152 ? 30.550 11.658  0.833   1.00 41.73  ?  375 PHE A CZ  1 
ATOM   5299 N N   . GLU D 1 153 ? 30.926 14.912  -5.332  1.00 44.38  ?  376 GLU A N   1 
ATOM   5300 C CA  . GLU D 1 153 ? 31.207 15.909  -6.353  1.00 43.09  ?  376 GLU A CA  1 
ATOM   5301 C C   . GLU D 1 153 ? 32.147 16.979  -5.813  1.00 42.23  ?  376 GLU A C   1 
ATOM   5302 O O   . GLU D 1 153 ? 32.196 17.243  -4.610  1.00 37.61  ?  376 GLU A O   1 
ATOM   5303 C CB  . GLU D 1 153 ? 29.911 16.553  -6.850  1.00 38.63  ?  376 GLU A CB  1 
ATOM   5304 C CG  . GLU D 1 153 ? 28.744 15.583  -6.943  1.00 51.99  ?  376 GLU A CG  1 
ATOM   5305 C CD  . GLU D 1 153 ? 27.493 16.218  -7.521  1.00 60.19  ?  376 GLU A CD  1 
ATOM   5306 O OE1 . GLU D 1 153 ? 27.388 17.462  -7.498  1.00 68.54  ?  376 GLU A OE1 1 
ATOM   5307 O OE2 . GLU D 1 153 ? 26.613 15.469  -7.999  1.00 55.67  ?  376 GLU A OE2 1 
ATOM   5308 N N   . ALA D 1 154 ? 32.897 17.590  -6.721  1.00 42.12  ?  377 ALA A N   1 
ATOM   5309 C CA  . ALA D 1 154 ? 33.840 18.637  -6.365  1.00 40.27  ?  377 ALA A CA  1 
ATOM   5310 C C   . ALA D 1 154 ? 33.149 19.998  -6.352  1.00 38.02  ?  377 ALA A C   1 
ATOM   5311 O O   . ALA D 1 154 ? 32.098 20.196  -6.967  1.00 42.69  ?  377 ALA A O   1 
ATOM   5312 C CB  . ALA D 1 154 ? 35.020 18.653  -7.336  1.00 38.51  ?  377 ALA A CB  1 
ATOM   5313 N N   . ASN D 1 155 ? 33.758 20.939  -5.626  1.00 36.49  ?  378 ASN A N   1 
ATOM   5314 C CA  . ASN D 1 155 ? 33.249 22.308  -5.510  1.00 38.00  ?  378 ASN A CA  1 
ATOM   5315 C C   . ASN D 1 155 ? 31.816 22.331  -4.979  1.00 38.30  ?  378 ASN A C   1 
ATOM   5316 O O   . ASN D 1 155 ? 30.955 23.047  -5.494  1.00 36.60  ?  378 ASN A O   1 
ATOM   5317 C CB  . ASN D 1 155 ? 33.347 23.050  -6.844  1.00 38.26  ?  378 ASN A CB  1 
ATOM   5318 C CG  . ASN D 1 155 ? 34.764 23.091  -7.384  1.00 43.35  ?  378 ASN A CG  1 
ATOM   5319 O OD1 . ASN D 1 155 ? 35.717 23.332  -6.641  1.00 45.88  ?  378 ASN A OD1 1 
ATOM   5320 N ND2 . ASN D 1 155 ? 34.910 22.854  -8.681  1.00 45.41  ?  378 ASN A ND2 1 
ATOM   5321 N N   . GLN D 1 156 ? 31.556 21.533  -3.947  1.00 33.05  ?  379 GLN A N   1 
ATOM   5322 C CA  . GLN D 1 156 ? 30.256 21.498  -3.293  1.00 35.62  ?  379 GLN A CA  1 
ATOM   5323 C C   . GLN D 1 156 ? 30.460 21.393  -1.789  1.00 38.28  ?  379 GLN A C   1 
ATOM   5324 O O   . GLN D 1 156 ? 31.410 20.759  -1.321  1.00 33.46  ?  379 GLN A O   1 
ATOM   5325 C CB  . GLN D 1 156 ? 29.391 20.328  -3.790  1.00 37.09  ?  379 GLN A CB  1 
ATOM   5326 C CG  . GLN D 1 156 ? 29.084 20.350  -5.284  1.00 39.90  ?  379 GLN A CG  1 
ATOM   5327 C CD  . GLN D 1 156 ? 28.180 21.501  -5.689  1.00 41.83  ?  379 GLN A CD  1 
ATOM   5328 O OE1 . GLN D 1 156 ? 27.500 22.098  -4.854  1.00 42.70  ?  379 GLN A OE1 1 
ATOM   5329 N NE2 . GLN D 1 156 ? 28.170 21.818  -6.979  1.00 41.47  ?  379 GLN A NE2 1 
ATOM   5330 N N   . ASN D 1 157 ? 29.556 22.020  -1.038  1.00 36.21  ?  380 ASN A N   1 
ATOM   5331 C CA  . ASN D 1 157 ? 29.660 22.049  0.416   1.00 37.97  ?  380 ASN A CA  1 
ATOM   5332 C C   . ASN D 1 157 ? 29.546 20.642  0.993   1.00 39.22  ?  380 ASN A C   1 
ATOM   5333 O O   . ASN D 1 157 ? 28.546 19.950  0.777   1.00 36.58  ?  380 ASN A O   1 
ATOM   5334 C CB  . ASN D 1 157 ? 28.575 22.957  0.995   1.00 32.61  ?  380 ASN A CB  1 
ATOM   5335 C CG  . ASN D 1 157 ? 28.836 24.430  0.720   1.00 37.67  ?  380 ASN A CG  1 
ATOM   5336 O OD1 . ASN D 1 157 ? 29.938 24.820  0.334   1.00 35.06  ?  380 ASN A OD1 1 
ATOM   5337 N ND2 . ASN D 1 157 ? 27.815 25.255  0.916   1.00 36.90  ?  380 ASN A ND2 1 
ATOM   5338 N N   . THR D 1 158 ? 30.575 20.223  1.729   1.00 35.52  ?  381 THR A N   1 
ATOM   5339 C CA  . THR D 1 158 ? 30.649 18.892  2.316   1.00 36.82  ?  381 THR A CA  1 
ATOM   5340 C C   . THR D 1 158 ? 30.934 19.011  3.806   1.00 37.55  ?  381 THR A C   1 
ATOM   5341 O O   . THR D 1 158 ? 31.794 19.795  4.220   1.00 37.69  ?  381 THR A O   1 
ATOM   5342 C CB  . THR D 1 158 ? 31.739 18.046  1.639   1.00 38.49  ?  381 THR A CB  1 
ATOM   5343 O OG1 . THR D 1 158 ? 31.636 18.181  0.216   1.00 42.07  ?  381 THR A OG1 1 
ATOM   5344 C CG2 . THR D 1 158 ? 31.598 16.577  2.014   1.00 35.63  ?  381 THR A CG2 1 
ATOM   5345 N N   . LYS D 1 159 ? 30.211 18.231  4.609   1.00 37.21  ?  382 LYS A N   1 
ATOM   5346 C CA  . LYS D 1 159 ? 30.334 18.269  6.060   1.00 32.53  ?  382 LYS A CA  1 
ATOM   5347 C C   . LYS D 1 159 ? 30.571 16.867  6.603   1.00 38.01  ?  382 LYS A C   1 
ATOM   5348 O O   . LYS D 1 159 ? 29.968 15.899  6.130   1.00 35.08  ?  382 LYS A O   1 
ATOM   5349 C CB  . LYS D 1 159 ? 29.077 18.871  6.712   1.00 33.17  ?  382 LYS A CB  1 
ATOM   5350 C CG  . LYS D 1 159 ? 29.081 18.804  8.234   1.00 37.12  ?  382 LYS A CG  1 
ATOM   5351 C CD  . LYS D 1 159 ? 27.694 19.016  8.825   1.00 44.42  ?  382 LYS A CD  1 
ATOM   5352 C CE  . LYS D 1 159 ? 27.718 18.851  10.342  1.00 38.90  ?  382 LYS A CE  1 
ATOM   5353 N NZ  . LYS D 1 159 ? 26.379 19.072  10.955  1.00 37.19  ?  382 LYS A NZ  1 
ATOM   5354 N N   . PHE D 1 160 ? 31.448 16.767  7.601   1.00 34.98  ?  383 PHE A N   1 
ATOM   5355 C CA  . PHE D 1 160 ? 31.704 15.525  8.320   1.00 33.01  ?  383 PHE A CA  1 
ATOM   5356 C C   . PHE D 1 160 ? 31.064 15.611  9.698   1.00 32.79  ?  383 PHE A C   1 
ATOM   5357 O O   . PHE D 1 160 ? 31.359 16.534  10.466  1.00 34.33  ?  383 PHE A O   1 
ATOM   5358 C CB  . PHE D 1 160 ? 33.204 15.260  8.449   1.00 33.15  ?  383 PHE A CB  1 
ATOM   5359 C CG  . PHE D 1 160 ? 33.536 14.066  9.300   1.00 38.04  ?  383 PHE A CG  1 
ATOM   5360 C CD1 . PHE D 1 160 ? 33.416 12.783  8.792   1.00 35.37  ?  383 PHE A CD1 1 
ATOM   5361 C CD2 . PHE D 1 160 ? 33.963 14.225  10.610  1.00 33.54  ?  383 PHE A CD2 1 
ATOM   5362 C CE1 . PHE D 1 160 ? 33.718 11.681  9.571   1.00 38.01  ?  383 PHE A CE1 1 
ATOM   5363 C CE2 . PHE D 1 160 ? 34.265 13.126  11.395  1.00 33.14  ?  383 PHE A CE2 1 
ATOM   5364 C CZ  . PHE D 1 160 ? 34.143 11.854  10.874  1.00 35.86  ?  383 PHE A CZ  1 
ATOM   5365 N N   . THR D 1 161 ? 30.196 14.650  10.011  1.00 32.66  ?  384 THR A N   1 
ATOM   5366 C CA  . THR D 1 161 ? 29.561 14.568  11.321  1.00 35.41  ?  384 THR A CA  1 
ATOM   5367 C C   . THR D 1 161 ? 30.166 13.410  12.098  1.00 40.51  ?  384 THR A C   1 
ATOM   5368 O O   . THR D 1 161 ? 30.050 12.256  11.657  1.00 32.33  ?  384 THR A O   1 
ATOM   5369 C CB  . THR D 1 161 ? 28.049 14.384  11.183  1.00 38.04  ?  384 THR A CB  1 
ATOM   5370 O OG1 . THR D 1 161 ? 27.491 15.490  10.463  1.00 39.10  ?  384 THR A OG1 1 
ATOM   5371 C CG2 . THR D 1 161 ? 27.395 14.295  12.559  1.00 30.17  ?  384 THR A CG2 1 
ATOM   5372 N N   . PRO D 1 162 ? 30.807 13.654  13.240  1.00 33.89  ?  385 PRO A N   1 
ATOM   5373 C CA  . PRO D 1 162 ? 31.442 12.554  13.974  1.00 35.87  ?  385 PRO A CA  1 
ATOM   5374 C C   . PRO D 1 162 ? 30.412 11.699  14.696  1.00 36.74  ?  385 PRO A C   1 
ATOM   5375 O O   . PRO D 1 162 ? 29.397 12.196  15.188  1.00 37.37  ?  385 PRO A O   1 
ATOM   5376 C CB  . PRO D 1 162 ? 32.363 13.277  14.961  1.00 32.83  ?  385 PRO A CB  1 
ATOM   5377 C CG  . PRO D 1 162 ? 31.664 14.569  15.221  1.00 30.76  ?  385 PRO A CG  1 
ATOM   5378 C CD  . PRO D 1 162 ? 30.971 14.946  13.930  1.00 36.77  ?  385 PRO A CD  1 
ATOM   5379 N N   . VAL D 1 163 ? 30.684 10.396  14.753  1.00 35.80  ?  386 VAL A N   1 
ATOM   5380 C CA  . VAL D 1 163 ? 29.813 9.434   15.419  1.00 38.22  ?  386 VAL A CA  1 
ATOM   5381 C C   . VAL D 1 163 ? 30.545 8.699   16.536  1.00 33.95  ?  386 VAL A C   1 
ATOM   5382 O O   . VAL D 1 163 ? 30.087 8.676   17.683  1.00 33.09  ?  386 VAL A O   1 
ATOM   5383 C CB  . VAL D 1 163 ? 29.202 8.436   14.412  1.00 35.16  ?  386 VAL A CB  1 
ATOM   5384 C CG1 . VAL D 1 163 ? 28.498 7.304   15.144  1.00 34.64  ?  386 VAL A CG1 1 
ATOM   5385 C CG2 . VAL D 1 163 ? 28.235 9.154   13.483  1.00 35.07  ?  386 VAL A CG2 1 
ATOM   5386 N N   . GLY D 1 164 ? 31.686 8.105   16.225  1.00 34.68  ?  387 GLY A N   1 
ATOM   5387 C CA  . GLY D 1 164 ? 32.435 7.370   17.216  1.00 36.19  ?  387 GLY A CA  1 
ATOM   5388 C C   . GLY D 1 164 ? 33.857 7.091   16.784  1.00 39.01  ?  387 GLY A C   1 
ATOM   5389 O O   . GLY D 1 164 ? 34.394 7.741   15.886  1.00 35.60  ?  387 GLY A O   1 
ATOM   5390 N N   . VAL D 1 165 ? 34.467 6.104   17.446  1.00 32.80  ?  388 VAL A N   1 
ATOM   5391 C CA  . VAL D 1 165 ? 35.851 5.724   17.201  1.00 38.25  ?  388 VAL A CA  1 
ATOM   5392 C C   . VAL D 1 165 ? 35.916 4.237   16.881  1.00 37.34  ?  388 VAL A C   1 
ATOM   5393 O O   . VAL D 1 165 ? 35.002 3.468   17.188  1.00 33.76  ?  388 VAL A O   1 
ATOM   5394 C CB  . VAL D 1 165 ? 36.767 6.052   18.402  1.00 37.59  ?  388 VAL A CB  1 
ATOM   5395 C CG1 . VAL D 1 165 ? 36.774 7.546   18.676  1.00 35.26  ?  388 VAL A CG1 1 
ATOM   5396 C CG2 . VAL D 1 165 ? 36.324 5.276   19.637  1.00 34.79  ?  388 VAL A CG2 1 
ATOM   5397 N N   . ILE D 1 166 ? 37.022 3.835   16.251  1.00 39.62  ?  389 ILE A N   1 
ATOM   5398 C CA  . ILE D 1 166 ? 37.277 2.445   15.887  1.00 40.58  ?  389 ILE A CA  1 
ATOM   5399 C C   . ILE D 1 166 ? 38.717 2.097   16.246  1.00 45.49  ?  389 ILE A C   1 
ATOM   5400 O O   . ILE D 1 166 ? 39.519 2.958   16.614  1.00 42.09  ?  389 ILE A O   1 
ATOM   5401 C CB  . ILE D 1 166 ? 37.027 2.171   14.387  1.00 39.02  ?  389 ILE A CB  1 
ATOM   5402 C CG1 . ILE D 1 166 ? 37.983 2.994   13.523  1.00 37.48  ?  389 ILE A CG1 1 
ATOM   5403 C CG2 . ILE D 1 166 ? 35.588 2.460   14.010  1.00 41.29  ?  389 ILE A CG2 1 
ATOM   5404 C CD1 . ILE D 1 166 ? 38.381 2.315   12.228  1.00 41.28  ?  389 ILE A CD1 1 
ATOM   5405 N N   . GLN D 1 167 ? 39.037 0.810   16.130  1.00 42.79  ?  390 GLN A N   1 
ATOM   5406 C CA  . GLN D 1 167 ? 40.408 0.342   16.278  1.00 49.02  ?  390 GLN A CA  1 
ATOM   5407 C C   . GLN D 1 167 ? 40.543 -0.981  15.540  1.00 48.55  ?  390 GLN A C   1 
ATOM   5408 O O   . GLN D 1 167 ? 39.560 -1.698  15.327  1.00 42.82  ?  390 GLN A O   1 
ATOM   5409 C CB  . GLN D 1 167 ? 40.801 0.180   17.749  1.00 49.74  ?  390 GLN A CB  1 
ATOM   5410 C CG  . GLN D 1 167 ? 40.126 -0.986  18.437  1.00 47.13  ?  390 GLN A CG  1 
ATOM   5411 C CD  . GLN D 1 167 ? 40.978 -2.247  18.434  1.00 53.02  ?  390 GLN A CD  1 
ATOM   5412 O OE1 . GLN D 1 167 ? 42.188 -2.192  18.635  1.00 59.07  ?  390 GLN A OE1 1 
ATOM   5413 N NE2 . GLN D 1 167 ? 40.349 -3.381  18.182  1.00 47.21  ?  390 GLN A NE2 1 
ATOM   5414 N N   . ASP D 1 168 ? 41.778 -1.295  15.155  1.00 55.76  ?  391 ASP A N   1 
ATOM   5415 C CA  . ASP D 1 168 ? 42.073 -2.538  14.448  1.00 62.05  ?  391 ASP A CA  1 
ATOM   5416 C C   . ASP D 1 168 ? 41.867 -3.719  15.389  1.00 66.48  ?  391 ASP A C   1 
ATOM   5417 O O   . ASP D 1 168 ? 42.612 -3.884  16.362  1.00 64.84  ?  391 ASP A O   1 
ATOM   5418 C CB  . ASP D 1 168 ? 43.502 -2.505  13.911  1.00 63.46  ?  391 ASP A CB  1 
ATOM   5419 C CG  . ASP D 1 168 ? 43.807 -3.672  12.990  1.00 72.66  ?  391 ASP A CG  1 
ATOM   5420 O OD1 . ASP D 1 168 ? 42.861 -4.380  12.585  1.00 75.32  ?  391 ASP A OD1 1 
ATOM   5421 O OD2 . ASP D 1 168 ? 44.997 -3.880  12.671  1.00 74.64  ?  391 ASP A OD2 1 
ATOM   5422 N N   . GLY D 1 169 ? 40.860 -4.547  15.098  1.00 63.59  ?  392 GLY A N   1 
ATOM   5423 C CA  . GLY D 1 169 ? 40.542 -5.682  15.949  1.00 61.57  ?  392 GLY A CA  1 
ATOM   5424 C C   . GLY D 1 169 ? 41.657 -6.698  16.077  1.00 68.01  ?  392 GLY A C   1 
ATOM   5425 O O   . GLY D 1 169 ? 41.652 -7.497  17.021  1.00 62.83  ?  392 GLY A O   1 
ATOM   5426 N N   . GLY D 1 170 ? 42.616 -6.694  15.147  1.00 71.72  ?  393 GLY A N   1 
ATOM   5427 C CA  . GLY D 1 170 ? 43.731 -7.620  15.224  1.00 75.04  ?  393 GLY A CA  1 
ATOM   5428 C C   . GLY D 1 170 ? 44.791 -7.249  16.236  1.00 77.40  ?  393 GLY A C   1 
ATOM   5429 O O   . GLY D 1 170 ? 45.530 -8.129  16.693  1.00 79.16  ?  393 GLY A O   1 
ATOM   5430 N N   . THR D 1 171 ? 44.887 -5.971  16.598  1.00 74.40  ?  394 THR A N   1 
ATOM   5431 C CA  . THR D 1 171 ? 45.876 -5.521  17.564  1.00 73.21  ?  394 THR A CA  1 
ATOM   5432 C C   . THR D 1 171 ? 45.355 -5.725  18.987  1.00 70.20  ?  394 THR A C   1 
ATOM   5433 O O   . THR D 1 171 ? 44.258 -6.245  19.211  1.00 65.40  ?  394 THR A O   1 
ATOM   5434 C CB  . THR D 1 171 ? 46.235 -4.056  17.321  1.00 68.47  ?  394 THR A CB  1 
ATOM   5435 O OG1 . THR D 1 171 ? 45.071 -3.336  16.893  1.00 65.67  ?  394 THR A OG1 1 
ATOM   5436 C CG2 . THR D 1 171 ? 47.318 -3.938  16.256  1.00 69.18  ?  394 THR A CG2 1 
ATOM   5437 N N   . THR D 1 172 ? 46.162 -5.312  19.964  1.00 70.00  ?  395 THR A N   1 
ATOM   5438 C CA  . THR D 1 172 ? 45.756 -5.406  21.360  1.00 61.48  ?  395 THR A CA  1 
ATOM   5439 C C   . THR D 1 172 ? 44.520 -4.550  21.610  1.00 61.58  ?  395 THR A C   1 
ATOM   5440 O O   . THR D 1 172 ? 44.334 -3.493  21.003  1.00 64.33  ?  395 THR A O   1 
ATOM   5441 C CB  . THR D 1 172 ? 46.895 -4.967  22.283  1.00 63.57  ?  395 THR A CB  1 
ATOM   5442 O OG1 . THR D 1 172 ? 48.152 -5.354  21.713  1.00 68.89  ?  395 THR A OG1 1 
ATOM   5443 C CG2 . THR D 1 172 ? 46.748 -5.611  23.655  1.00 62.05  ?  395 THR A CG2 1 
ATOM   5444 N N   . HIS D 1 173 ? 43.668 -5.018  22.516  1.00 58.10  ?  396 HIS A N   1 
ATOM   5445 C CA  . HIS D 1 173 ? 42.398 -4.352  22.758  1.00 58.12  ?  396 HIS A CA  1 
ATOM   5446 C C   . HIS D 1 173 ? 42.600 -3.036  23.499  1.00 55.44  ?  396 HIS A C   1 
ATOM   5447 O O   . HIS D 1 173 ? 43.426 -2.937  24.412  1.00 52.46  ?  396 HIS A O   1 
ATOM   5448 C CB  . HIS D 1 173 ? 41.466 -5.268  23.547  1.00 57.54  ?  396 HIS A CB  1 
ATOM   5449 C CG  . HIS D 1 173 ? 41.002 -6.463  22.772  1.00 55.33  ?  396 HIS A CG  1 
ATOM   5450 N ND1 . HIS D 1 173 ? 40.165 -7.420  23.306  1.00 55.38  ?  396 HIS A ND1 1 
ATOM   5451 C CD2 . HIS D 1 173 ? 41.262 -6.856  21.503  1.00 51.33  ?  396 HIS A CD2 1 
ATOM   5452 C CE1 . HIS D 1 173 ? 39.927 -8.348  22.396  1.00 50.51  ?  396 HIS A CE1 1 
ATOM   5453 N NE2 . HIS D 1 173 ? 40.581 -8.030  21.293  1.00 51.39  ?  396 HIS A NE2 1 
ATOM   5454 N N   . ARG D 1 174 ? 41.835 -2.022  23.089  1.00 53.18  ?  397 ARG A N   1 
ATOM   5455 C CA  . ARG D 1 174 ? 41.835 -0.692  23.700  1.00 50.97  ?  397 ARG A CA  1 
ATOM   5456 C C   . ARG D 1 174 ? 43.193 -0.001  23.606  1.00 43.96  ?  397 ARG A C   1 
ATOM   5457 O O   . ARG D 1 174 ? 43.502 0.877   24.416  1.00 42.13  ?  397 ARG A O   1 
ATOM   5458 C CB  . ARG D 1 174 ? 41.367 -0.755  25.157  1.00 46.85  ?  397 ARG A CB  1 
ATOM   5459 C CG  . ARG D 1 174 ? 39.990 -1.389  25.314  1.00 47.25  ?  397 ARG A CG  1 
ATOM   5460 C CD  . ARG D 1 174 ? 39.600 -1.542  26.774  1.00 50.28  ?  397 ARG A CD  1 
ATOM   5461 N NE  . ARG D 1 174 ? 39.912 -2.868  27.295  1.00 66.67  ?  397 ARG A NE  1 
ATOM   5462 C CZ  . ARG D 1 174 ? 39.304 -3.991  26.930  1.00 66.20  ?  397 ARG A CZ  1 
ATOM   5463 N NH1 . ARG D 1 174 ? 38.335 -3.995  26.026  1.00 55.55  ?  397 ARG A NH1 1 
ATOM   5464 N NH2 . ARG D 1 174 ? 39.676 -5.141  27.487  1.00 61.23  ?  397 ARG A NH2 1 
ATOM   5465 N N   . ASN D 1 175 ? 44.012 -0.373  22.620  1.00 46.01  ?  398 ASN A N   1 
ATOM   5466 C CA  . ASN D 1 175 ? 45.243 0.352   22.349  1.00 48.71  ?  398 ASN A CA  1 
ATOM   5467 C C   . ASN D 1 175 ? 45.000 1.625   21.553  1.00 47.61  ?  398 ASN A C   1 
ATOM   5468 O O   . ASN D 1 175 ? 45.907 2.455   21.446  1.00 44.52  ?  398 ASN A O   1 
ATOM   5469 C CB  . ASN D 1 175 ? 46.235 -0.543  21.598  1.00 50.16  ?  398 ASN A CB  1 
ATOM   5470 C CG  . ASN D 1 175 ? 45.749 -0.924  20.209  1.00 55.63  ?  398 ASN A CG  1 
ATOM   5471 O OD1 . ASN D 1 175 ? 44.548 -0.925  19.934  1.00 51.89  ?  398 ASN A OD1 1 
ATOM   5472 N ND2 . ASN D 1 175 ? 46.686 -1.257  19.328  1.00 59.59  ?  398 ASN A ND2 1 
ATOM   5473 N N   . GLU D 1 176 ? 43.802 1.791   21.001  1.00 45.20  ?  399 GLU A N   1 
ATOM   5474 C CA  . GLU D 1 176 ? 43.395 2.956   20.237  1.00 46.45  ?  399 GLU A CA  1 
ATOM   5475 C C   . GLU D 1 176 ? 41.975 3.321   20.638  1.00 47.31  ?  399 GLU A C   1 
ATOM   5476 O O   . GLU D 1 176 ? 41.168 2.432   20.932  1.00 46.03  ?  399 GLU A O   1 
ATOM   5477 C CB  . GLU D 1 176 ? 43.450 2.694   18.724  1.00 45.21  ?  399 GLU A CB  1 
ATOM   5478 C CG  . GLU D 1 176 ? 44.104 3.799   17.916  1.00 55.66  ?  399 GLU A CG  1 
ATOM   5479 C CD  . GLU D 1 176 ? 43.871 3.640   16.427  1.00 59.43  ?  399 GLU A CD  1 
ATOM   5480 O OE1 . GLU D 1 176 ? 43.494 2.526   15.999  1.00 54.53  ?  399 GLU A OE1 1 
ATOM   5481 O OE2 . GLU D 1 176 ? 44.046 4.633   15.688  1.00 51.20  ?  399 GLU A OE2 1 
ATOM   5482 N N   . PRO D 1 177 ? 41.639 4.620   20.670  1.00 46.60  ?  400 PRO A N   1 
ATOM   5483 C CA  . PRO D 1 177 ? 42.516 5.771   20.428  1.00 45.69  ?  400 PRO A CA  1 
ATOM   5484 C C   . PRO D 1 177 ? 43.346 6.148   21.649  1.00 44.79  ?  400 PRO A C   1 
ATOM   5485 O O   . PRO D 1 177 ? 43.222 5.521   22.703  1.00 42.20  ?  400 PRO A O   1 
ATOM   5486 C CB  . PRO D 1 177 ? 41.534 6.900   20.080  1.00 43.14  ?  400 PRO A CB  1 
ATOM   5487 C CG  . PRO D 1 177 ? 40.180 6.247   19.944  1.00 40.52  ?  400 PRO A CG  1 
ATOM   5488 C CD  . PRO D 1 177 ? 40.234 5.033   20.794  1.00 46.43  ?  400 PRO A CD  1 
ATOM   5489 N N   . GLN D 1 178 ? 44.183 7.169   21.500  1.00 40.16  ?  401 GLN A N   1 
ATOM   5490 C CA  . GLN D 1 178 ? 45.006 7.696   22.586  1.00 44.83  ?  401 GLN A CA  1 
ATOM   5491 C C   . GLN D 1 178 ? 44.502 9.100   22.906  1.00 41.19  ?  401 GLN A C   1 
ATOM   5492 O O   . GLN D 1 178 ? 44.912 10.076  22.271  1.00 43.67  ?  401 GLN A O   1 
ATOM   5493 C CB  . GLN D 1 178 ? 46.481 7.700   22.201  1.00 44.96  ?  401 GLN A CB  1 
ATOM   5494 C CG  . GLN D 1 178 ? 47.013 6.343   21.776  1.00 51.85  ?  401 GLN A CG  1 
ATOM   5495 C CD  . GLN D 1 178 ? 48.348 6.440   21.066  1.00 57.37  ?  401 GLN A CD  1 
ATOM   5496 O OE1 . GLN D 1 178 ? 49.403 6.422   21.701  1.00 59.66  ?  401 GLN A OE1 1 
ATOM   5497 N NE2 . GLN D 1 178 ? 48.309 6.547   19.743  1.00 51.96  ?  401 GLN A NE2 1 
ATOM   5498 N N   . GLN D 1 179 ? 43.617 9.195   23.901  1.00 38.32  ?  402 GLN A N   1 
ATOM   5499 C CA  . GLN D 1 179 ? 42.965 10.465  24.200  1.00 42.99  ?  402 GLN A CA  1 
ATOM   5500 C C   . GLN D 1 179 ? 43.928 11.509  24.756  1.00 43.21  ?  402 GLN A C   1 
ATOM   5501 O O   . GLN D 1 179 ? 43.588 12.697  24.765  1.00 40.79  ?  402 GLN A O   1 
ATOM   5502 C CB  . GLN D 1 179 ? 41.810 10.242  25.178  1.00 34.57  ?  402 GLN A CB  1 
ATOM   5503 C CG  . GLN D 1 179 ? 42.240 9.938   26.602  1.00 41.29  ?  402 GLN A CG  1 
ATOM   5504 C CD  . GLN D 1 179 ? 41.152 10.256  27.611  1.00 44.22  ?  402 GLN A CD  1 
ATOM   5505 O OE1 . GLN D 1 179 ? 40.392 11.210  27.442  1.00 38.30  ?  402 GLN A OE1 1 
ATOM   5506 N NE2 . GLN D 1 179 ? 41.072 9.455   28.669  1.00 36.18  ?  402 GLN A NE2 1 
ATOM   5507 N N   . TRP D 1 180 ? 45.117 11.104  25.208  1.00 46.07  ?  403 TRP A N   1 
ATOM   5508 C CA  . TRP D 1 180 ? 46.090 12.028  25.777  1.00 38.92  ?  403 TRP A CA  1 
ATOM   5509 C C   . TRP D 1 180 ? 47.283 12.265  24.857  1.00 44.85  ?  403 TRP A C   1 
ATOM   5510 O O   . TRP D 1 180 ? 48.322 12.756  25.311  1.00 49.38  ?  403 TRP A O   1 
ATOM   5511 C CB  . TRP D 1 180 ? 46.569 11.526  27.140  1.00 43.64  ?  403 TRP A CB  1 
ATOM   5512 C CG  . TRP D 1 180 ? 45.479 11.390  28.163  1.00 41.59  ?  403 TRP A CG  1 
ATOM   5513 C CD1 . TRP D 1 180 ? 45.216 10.295  28.934  1.00 43.88  ?  403 TRP A CD1 1 
ATOM   5514 C CD2 . TRP D 1 180 ? 44.509 12.381  28.532  1.00 43.51  ?  403 TRP A CD2 1 
ATOM   5515 N NE1 . TRP D 1 180 ? 44.145 10.541  29.758  1.00 47.68  ?  403 TRP A NE1 1 
ATOM   5516 C CE2 . TRP D 1 180 ? 43.692 11.814  29.531  1.00 40.50  ?  403 TRP A CE2 1 
ATOM   5517 C CE3 . TRP D 1 180 ? 44.250 13.692  28.114  1.00 41.26  ?  403 TRP A CE3 1 
ATOM   5518 C CZ2 . TRP D 1 180 ? 42.636 12.509  30.117  1.00 38.89  ?  403 TRP A CZ2 1 
ATOM   5519 C CZ3 . TRP D 1 180 ? 43.201 14.381  28.698  1.00 40.02  ?  403 TRP A CZ3 1 
ATOM   5520 C CH2 . TRP D 1 180 ? 42.407 13.788  29.689  1.00 41.13  ?  403 TRP A CH2 1 
ATOM   5521 N N   . VAL D 1 181 ? 47.160 11.927  23.577  1.00 45.80  ?  404 VAL A N   1 
ATOM   5522 C CA  . VAL D 1 181 ? 48.216 12.142  22.595  1.00 41.36  ?  404 VAL A CA  1 
ATOM   5523 C C   . VAL D 1 181 ? 47.688 13.129  21.564  1.00 46.04  ?  404 VAL A C   1 
ATOM   5524 O O   . VAL D 1 181 ? 46.751 12.817  20.818  1.00 43.32  ?  404 VAL A O   1 
ATOM   5525 C CB  . VAL D 1 181 ? 48.665 10.834  21.930  1.00 46.16  ?  404 VAL A CB  1 
ATOM   5526 C CG1 . VAL D 1 181 ? 49.666 11.124  20.821  1.00 44.82  ?  404 VAL A CG1 1 
ATOM   5527 C CG2 . VAL D 1 181 ? 49.270 9.896   22.965  1.00 45.79  ?  404 VAL A CG2 1 
ATOM   5528 N N   . LEU D 1 182 ? 48.287 14.316  21.520  1.00 44.04  ?  405 LEU A N   1 
ATOM   5529 C CA  . LEU D 1 182 ? 47.844 15.342  20.589  1.00 42.16  ?  405 LEU A CA  1 
ATOM   5530 C C   . LEU D 1 182 ? 48.257 14.978  19.165  1.00 43.81  ?  405 LEU A C   1 
ATOM   5531 O O   . LEU D 1 182 ? 49.369 14.487  18.944  1.00 46.26  ?  405 LEU A O   1 
ATOM   5532 C CB  . LEU D 1 182 ? 48.435 16.700  20.963  1.00 40.28  ?  405 LEU A CB  1 
ATOM   5533 C CG  . LEU D 1 182 ? 47.766 17.482  22.093  1.00 42.67  ?  405 LEU A CG  1 
ATOM   5534 C CD1 . LEU D 1 182 ? 48.431 18.838  22.259  1.00 40.25  ?  405 LEU A CD1 1 
ATOM   5535 C CD2 . LEU D 1 182 ? 46.281 17.644  21.828  1.00 38.42  ?  405 LEU A CD2 1 
ATOM   5536 N N   . PRO D 1 183 ? 47.392 15.206  18.180  1.00 43.07  ?  406 PRO A N   1 
ATOM   5537 C CA  . PRO D 1 183 ? 47.792 15.001  16.787  1.00 45.70  ?  406 PRO A CA  1 
ATOM   5538 C C   . PRO D 1 183 ? 48.764 16.078  16.331  1.00 46.24  ?  406 PRO A C   1 
ATOM   5539 O O   . PRO D 1 183 ? 48.916 17.129  16.957  1.00 50.32  ?  406 PRO A O   1 
ATOM   5540 C CB  . PRO D 1 183 ? 46.471 15.086  16.009  1.00 42.00  ?  406 PRO A CB  1 
ATOM   5541 C CG  . PRO D 1 183 ? 45.381 15.059  17.047  1.00 40.78  ?  406 PRO A CG  1 
ATOM   5542 C CD  . PRO D 1 183 ? 45.983 15.611  18.296  1.00 45.04  ?  406 PRO A CD  1 
ATOM   5543 N N   . SER D 1 184 ? 49.433 15.794  15.218  1.00 46.25  ?  407 SER A N   1 
ATOM   5544 C CA  . SER D 1 184 ? 50.308 16.766  14.568  1.00 48.38  ?  407 SER A CA  1 
ATOM   5545 C C   . SER D 1 184 ? 49.439 17.606  13.640  1.00 48.76  ?  407 SER A C   1 
ATOM   5546 O O   . SER D 1 184 ? 49.033 17.152  12.567  1.00 46.86  ?  407 SER A O   1 
ATOM   5547 C CB  . SER D 1 184 ? 51.434 16.062  13.821  1.00 52.94  ?  407 SER A CB  1 
ATOM   5548 O OG  . SER D 1 184 ? 52.470 15.680  14.708  1.00 60.77  ?  407 SER A OG  1 
ATOM   5549 N N   . TYR D 1 185 ? 49.153 18.841  14.058  1.00 46.42  ?  408 TYR A N   1 
ATOM   5550 C CA  . TYR D 1 185 ? 48.110 19.632  13.416  1.00 45.05  ?  408 TYR A CA  1 
ATOM   5551 C C   . TYR D 1 185 ? 48.493 20.115  12.022  1.00 46.61  ?  408 TYR A C   1 
ATOM   5552 O O   . TYR D 1 185 ? 47.600 20.461  11.241  1.00 46.02  ?  408 TYR A O   1 
ATOM   5553 C CB  . TYR D 1 185 ? 47.751 20.833  14.293  1.00 45.77  ?  408 TYR A CB  1 
ATOM   5554 C CG  . TYR D 1 185 ? 47.014 20.473  15.565  1.00 44.80  ?  408 TYR A CG  1 
ATOM   5555 C CD1 . TYR D 1 185 ? 45.815 19.771  15.525  1.00 41.58  ?  408 TYR A CD1 1 
ATOM   5556 C CD2 . TYR D 1 185 ? 47.516 20.841  16.806  1.00 41.16  ?  408 TYR A CD2 1 
ATOM   5557 C CE1 . TYR D 1 185 ? 45.138 19.446  16.687  1.00 37.02  ?  408 TYR A CE1 1 
ATOM   5558 C CE2 . TYR D 1 185 ? 46.847 20.518  17.971  1.00 43.51  ?  408 TYR A CE2 1 
ATOM   5559 C CZ  . TYR D 1 185 ? 45.661 19.822  17.908  1.00 42.46  ?  408 TYR A CZ  1 
ATOM   5560 O OH  . TYR D 1 185 ? 44.997 19.504  19.073  1.00 38.60  ?  408 TYR A OH  1 
ATOM   5561 N N   . SER D 1 186 ? 49.781 20.155  11.684  1.00 51.29  ?  409 SER A N   1 
ATOM   5562 C CA  . SER D 1 186 ? 50.217 20.679  10.393  1.00 50.76  ?  409 SER A CA  1 
ATOM   5563 C C   . SER D 1 186 ? 50.854 19.624  9.496   1.00 54.25  ?  409 SER A C   1 
ATOM   5564 O O   . SER D 1 186 ? 51.390 19.972  8.436   1.00 54.56  ?  409 SER A O   1 
ATOM   5565 C CB  . SER D 1 186 ? 51.189 21.847  10.587  1.00 51.42  ?  409 SER A CB  1 
ATOM   5566 O OG  . SER D 1 186 ? 50.507 23.046  10.900  1.00 51.54  ?  409 SER A OG  1 
ATOM   5567 N N   . GLY D 1 187 ? 50.819 18.355  9.883   1.00 53.32  ?  410 GLY A N   1 
ATOM   5568 C CA  . GLY D 1 187 ? 51.401 17.291  9.093   1.00 56.87  ?  410 GLY A CA  1 
ATOM   5569 C C   . GLY D 1 187 ? 52.360 16.451  9.906   1.00 58.11  ?  410 GLY A C   1 
ATOM   5570 O O   . GLY D 1 187 ? 52.605 16.697  11.084  1.00 63.44  ?  410 GLY A O   1 
ATOM   5571 N N   . ARG D 1 188 ? 52.929 15.447  9.234   1.00 65.25  ?  411 ARG A N   1 
ATOM   5572 C CA  . ARG D 1 188 ? 53.737 14.443  9.921   1.00 71.55  ?  411 ARG A CA  1 
ATOM   5573 C C   . ARG D 1 188 ? 54.959 15.064  10.591  1.00 78.49  ?  411 ARG A C   1 
ATOM   5574 O O   . ARG D 1 188 ? 55.229 14.810  11.771  1.00 83.51  ?  411 ARG A O   1 
ATOM   5575 C CB  . ARG D 1 188 ? 54.161 13.356  8.930   1.00 70.62  ?  411 ARG A CB  1 
ATOM   5576 C CG  . ARG D 1 188 ? 55.139 12.334  9.494   1.00 76.55  ?  411 ARG A CG  1 
ATOM   5577 C CD  . ARG D 1 188 ? 54.452 11.374  10.454  1.00 79.35  ?  411 ARG A CD  1 
ATOM   5578 N NE  . ARG D 1 188 ? 54.483 11.861  11.828  1.00 89.49  ?  411 ARG A NE  1 
ATOM   5579 C CZ  . ARG D 1 188 ? 53.407 12.058  12.576  1.00 84.62  ?  411 ARG A CZ  1 
ATOM   5580 N NH1 . ARG D 1 188 ? 52.191 11.807  12.117  1.00 78.44  ?  411 ARG A NH1 1 
ATOM   5581 N NH2 . ARG D 1 188 ? 53.554 12.519  13.816  1.00 80.53  ?  411 ARG A NH2 1 
ATOM   5582 N N   . ASN D 1 189 ? 55.709 15.882  9.855   1.00 76.15  ?  412 ASN A N   1 
ATOM   5583 C CA  . ASN D 1 189 ? 56.987 16.396  10.331  1.00 83.85  ?  412 ASN A CA  1 
ATOM   5584 C C   . ASN D 1 189 ? 56.865 17.662  11.170  1.00 78.90  ?  412 ASN A C   1 
ATOM   5585 O O   . ASN D 1 189 ? 57.828 18.026  11.854  1.00 85.57  ?  412 ASN A O   1 
ATOM   5586 C CB  . ASN D 1 189 ? 57.914 16.675  9.141   1.00 94.07  ?  412 ASN A CB  1 
ATOM   5587 C CG  . ASN D 1 189 ? 58.839 15.513  8.838   1.00 99.72  ?  412 ASN A CG  1 
ATOM   5588 O OD1 . ASN D 1 189 ? 58.831 14.499  9.534   1.00 97.11  ?  412 ASN A OD1 1 
ATOM   5589 N ND2 . ASN D 1 189 ? 59.646 15.658  7.791   1.00 95.87  ?  412 ASN A ND2 1 
ATOM   5590 N N   . THR D 1 190 ? 55.717 18.331  11.147  1.00 76.51  ?  413 THR A N   1 
ATOM   5591 C CA  . THR D 1 190 ? 55.602 19.665  11.711  1.00 76.48  ?  413 THR A CA  1 
ATOM   5592 C C   . THR D 1 190 ? 55.521 19.627  13.237  1.00 70.12  ?  413 THR A C   1 
ATOM   5593 O O   . THR D 1 190 ? 55.413 18.568  13.862  1.00 72.65  ?  413 THR A O   1 
ATOM   5594 C CB  . THR D 1 190 ? 54.374 20.372  11.146  1.00 69.86  ?  413 THR A CB  1 
ATOM   5595 O OG1 . THR D 1 190 ? 53.207 19.594  11.436  1.00 68.65  ?  413 THR A OG1 1 
ATOM   5596 C CG2 . THR D 1 190 ? 54.506 20.535  9.639   1.00 65.27  ?  413 THR A CG2 1 
ATOM   5597 N N   . HIS D 1 191 ? 55.574 20.815  13.833  1.00 68.93  ?  414 HIS A N   1 
ATOM   5598 C CA  . HIS D 1 191 ? 55.453 21.002  15.271  1.00 65.21  ?  414 HIS A CA  1 
ATOM   5599 C C   . HIS D 1 191 ? 54.236 21.867  15.566  1.00 60.04  ?  414 HIS A C   1 
ATOM   5600 O O   . HIS D 1 191 ? 53.953 22.825  14.839  1.00 59.09  ?  414 HIS A O   1 
ATOM   5601 C CB  . HIS D 1 191 ? 56.713 21.651  15.858  1.00 69.32  ?  414 HIS A CB  1 
ATOM   5602 C CG  . HIS D 1 191 ? 57.815 20.680  16.148  1.00 84.76  ?  414 HIS A CG  1 
ATOM   5603 N ND1 . HIS D 1 191 ? 57.592 19.451  16.731  1.00 85.59  ?  414 HIS A ND1 1 
ATOM   5604 C CD2 . HIS D 1 191 ? 59.150 20.758  15.935  1.00 83.66  ?  414 HIS A CD2 1 
ATOM   5605 C CE1 . HIS D 1 191 ? 58.741 18.813  16.864  1.00 86.33  ?  414 HIS A CE1 1 
ATOM   5606 N NE2 . HIS D 1 191 ? 59.703 19.585  16.389  1.00 89.34  ?  414 HIS A NE2 1 
ATOM   5607 N N   . ASN D 1 192 ? 53.520 21.529  16.636  1.00 52.41  ?  415 ASN A N   1 
ATOM   5608 C CA  . ASN D 1 192 ? 52.327 22.273  17.009  1.00 48.37  ?  415 ASN A CA  1 
ATOM   5609 C C   . ASN D 1 192 ? 52.701 23.656  17.540  1.00 49.68  ?  415 ASN A C   1 
ATOM   5610 O O   . ASN D 1 192 ? 53.821 23.896  18.000  1.00 50.75  ?  415 ASN A O   1 
ATOM   5611 C CB  . ASN D 1 192 ? 51.521 21.501  18.055  1.00 47.02  ?  415 ASN A CB  1 
ATOM   5612 C CG  . ASN D 1 192 ? 50.873 20.253  17.482  1.00 47.15  ?  415 ASN A CG  1 
ATOM   5613 O OD1 . ASN D 1 192 ? 50.600 20.176  16.285  1.00 46.86  ?  415 ASN A OD1 1 
ATOM   5614 N ND2 . ASN D 1 192 ? 50.628 19.266  18.338  1.00 43.43  ?  415 ASN A ND2 1 
ATOM   5615 N N   . VAL D 1 193 ? 51.740 24.578  17.468  1.00 51.18  ?  416 VAL A N   1 
ATOM   5616 C CA  . VAL D 1 193 ? 51.953 25.964  17.865  1.00 46.88  ?  416 VAL A CA  1 
ATOM   5617 C C   . VAL D 1 193 ? 50.764 26.443  18.687  1.00 49.07  ?  416 VAL A C   1 
ATOM   5618 O O   . VAL D 1 193 ? 49.639 25.964  18.525  1.00 49.56  ?  416 VAL A O   1 
ATOM   5619 C CB  . VAL D 1 193 ? 52.168 26.888  16.643  1.00 49.51  ?  416 VAL A CB  1 
ATOM   5620 C CG1 . VAL D 1 193 ? 53.512 26.607  15.986  1.00 50.14  ?  416 VAL A CG1 1 
ATOM   5621 C CG2 . VAL D 1 193 ? 51.033 26.723  15.642  1.00 49.20  ?  416 VAL A CG2 1 
ATOM   5622 N N   . HIS D 1 194 ? 51.031 27.400  19.581  1.00 51.46  ?  417 HIS A N   1 
ATOM   5623 C CA  . HIS D 1 194 ? 49.994 28.083  20.361  1.00 46.63  ?  417 HIS A CA  1 
ATOM   5624 C C   . HIS D 1 194 ? 49.124 27.099  21.138  1.00 42.63  ?  417 HIS A C   1 
ATOM   5625 O O   . HIS D 1 194 ? 47.904 27.254  21.227  1.00 42.58  ?  417 HIS A O   1 
ATOM   5626 C CB  . HIS D 1 194 ? 49.135 28.976  19.465  1.00 47.86  ?  417 HIS A CB  1 
ATOM   5627 C CG  . HIS D 1 194 ? 49.928 29.907  18.602  1.00 52.22  ?  417 HIS A CG  1 
ATOM   5628 N ND1 . HIS D 1 194 ? 50.149 29.674  17.261  1.00 54.91  ?  417 HIS A ND1 1 
ATOM   5629 C CD2 . HIS D 1 194 ? 50.555 31.072  18.889  1.00 56.17  ?  417 HIS A CD2 1 
ATOM   5630 C CE1 . HIS D 1 194 ? 50.878 30.655  16.760  1.00 57.14  ?  417 HIS A CE1 1 
ATOM   5631 N NE2 . HIS D 1 194 ? 51.137 31.518  17.726  1.00 58.62  ?  417 HIS A NE2 1 
ATOM   5632 N N   . LEU D 1 195 ? 49.754 26.079  21.711  1.00 43.93  ?  418 LEU A N   1 
ATOM   5633 C CA  . LEU D 1 195 ? 49.023 25.073  22.465  1.00 42.51  ?  418 LEU A CA  1 
ATOM   5634 C C   . LEU D 1 195 ? 48.625 25.606  23.836  1.00 43.49  ?  418 LEU A C   1 
ATOM   5635 O O   . LEU D 1 195 ? 49.335 26.410  24.448  1.00 46.31  ?  418 LEU A O   1 
ATOM   5636 C CB  . LEU D 1 195 ? 49.867 23.809  22.638  1.00 42.14  ?  418 LEU A CB  1 
ATOM   5637 C CG  . LEU D 1 195 ? 50.120 22.944  21.403  1.00 41.44  ?  418 LEU A CG  1 
ATOM   5638 C CD1 . LEU D 1 195 ? 51.097 21.826  21.732  1.00 43.47  ?  418 LEU A CD1 1 
ATOM   5639 C CD2 . LEU D 1 195 ? 48.817 22.378  20.865  1.00 41.92  ?  418 LEU A CD2 1 
ATOM   5640 N N   . ALA D 1 196 ? 47.469 25.155  24.310  1.00 43.69  ?  419 ALA A N   1 
ATOM   5641 C CA  . ALA D 1 196 ? 47.134 25.352  25.709  1.00 35.40  ?  419 ALA A CA  1 
ATOM   5642 C C   . ALA D 1 196 ? 48.118 24.572  26.576  1.00 35.74  ?  419 ALA A C   1 
ATOM   5643 O O   . ALA D 1 196 ? 48.539 23.473  26.200  1.00 40.25  ?  419 ALA A O   1 
ATOM   5644 C CB  . ALA D 1 196 ? 45.703 24.898  25.993  1.00 34.77  ?  419 ALA A CB  1 
ATOM   5645 N N   . PRO D 1 197 ? 48.513 25.109  27.728  1.00 41.53  ?  420 PRO A N   1 
ATOM   5646 C CA  . PRO D 1 197 ? 49.534 24.435  28.538  1.00 34.64  ?  420 PRO A CA  1 
ATOM   5647 C C   . PRO D 1 197 ? 49.047 23.099  29.077  1.00 40.34  ?  420 PRO A C   1 
ATOM   5648 O O   . PRO D 1 197 ? 47.849 22.872  29.262  1.00 41.73  ?  420 PRO A O   1 
ATOM   5649 C CB  . PRO D 1 197 ? 49.797 25.428  29.676  1.00 41.35  ?  420 PRO A CB  1 
ATOM   5650 C CG  . PRO D 1 197 ? 48.548 26.244  29.759  1.00 42.80  ?  420 PRO A CG  1 
ATOM   5651 C CD  . PRO D 1 197 ? 48.047 26.361  28.348  1.00 38.28  ?  420 PRO A CD  1 
ATOM   5652 N N   . ALA D 1 198 ? 50.003 22.205  29.320  1.00 39.81  ?  421 ALA A N   1 
ATOM   5653 C CA  . ALA D 1 198 ? 49.691 20.939  29.961  1.00 41.15  ?  421 ALA A CA  1 
ATOM   5654 C C   . ALA D 1 198 ? 49.253 21.177  31.405  1.00 43.81  ?  421 ALA A C   1 
ATOM   5655 O O   . ALA D 1 198 ? 49.589 22.187  32.026  1.00 44.79  ?  421 ALA A O   1 
ATOM   5656 C CB  . ALA D 1 198 ? 50.898 20.002  29.917  1.00 37.50  ?  421 ALA A CB  1 
ATOM   5657 N N   . VAL D 1 199 ? 48.492 20.224  31.937  1.00 42.21  ?  422 VAL A N   1 
ATOM   5658 C CA  . VAL D 1 199 ? 47.851 20.358  33.239  1.00 38.18  ?  422 VAL A CA  1 
ATOM   5659 C C   . VAL D 1 199 ? 48.272 19.186  34.115  1.00 45.14  ?  422 VAL A C   1 
ATOM   5660 O O   . VAL D 1 199 ? 48.230 18.030  33.677  1.00 48.02  ?  422 VAL A O   1 
ATOM   5661 C CB  . VAL D 1 199 ? 46.318 20.424  33.104  1.00 36.93  ?  422 VAL A CB  1 
ATOM   5662 C CG1 . VAL D 1 199 ? 45.642 19.987  34.391  1.00 43.18  ?  422 VAL A CG1 1 
ATOM   5663 C CG2 . VAL D 1 199 ? 45.882 21.829  32.720  1.00 43.78  ?  422 VAL A CG2 1 
ATOM   5664 N N   . ALA D 1 200 ? 48.678 19.487  35.351  1.00 42.62  ?  423 ALA A N   1 
ATOM   5665 C CA  . ALA D 1 200 ? 49.064 18.466  36.308  1.00 49.19  ?  423 ALA A CA  1 
ATOM   5666 C C   . ALA D 1 200 ? 48.704 18.938  37.707  1.00 52.90  ?  423 ALA A C   1 
ATOM   5667 O O   . ALA D 1 200 ? 48.880 20.126  38.014  1.00 48.27  ?  423 ALA A O   1 
ATOM   5668 C CB  . ALA D 1 200 ? 50.561 18.149  36.234  1.00 47.09  ?  423 ALA A CB  1 
ATOM   5669 N N   . PRO D 1 201 ? 48.195 18.052  38.565  1.00 55.25  ?  424 PRO A N   1 
ATOM   5670 C CA  . PRO D 1 201 ? 47.903 18.444  39.954  1.00 54.59  ?  424 PRO A CA  1 
ATOM   5671 C C   . PRO D 1 201 ? 49.194 18.621  40.740  1.00 60.94  ?  424 PRO A C   1 
ATOM   5672 O O   . PRO D 1 201 ? 49.975 17.681  40.895  1.00 61.73  ?  424 PRO A O   1 
ATOM   5673 C CB  . PRO D 1 201 ? 47.068 17.273  40.484  1.00 55.59  ?  424 PRO A CB  1 
ATOM   5674 C CG  . PRO D 1 201 ? 47.474 16.107  39.643  1.00 50.49  ?  424 PRO A CG  1 
ATOM   5675 C CD  . PRO D 1 201 ? 47.821 16.654  38.285  1.00 53.68  ?  424 PRO A CD  1 
ATOM   5676 N N   . THR D 1 202 ? 49.414 19.837  41.239  1.00 58.60  ?  425 THR A N   1 
ATOM   5677 C CA  . THR D 1 202 ? 50.643 20.169  41.947  1.00 61.14  ?  425 THR A CA  1 
ATOM   5678 C C   . THR D 1 202 ? 50.524 20.053  43.460  1.00 62.23  ?  425 THR A C   1 
ATOM   5679 O O   . THR D 1 202 ? 51.538 19.841  44.134  1.00 60.66  ?  425 THR A O   1 
ATOM   5680 C CB  . THR D 1 202 ? 51.094 21.590  41.594  1.00 57.11  ?  425 THR A CB  1 
ATOM   5681 O OG1 . THR D 1 202 ? 49.977 22.483  41.688  1.00 63.38  ?  425 THR A OG1 1 
ATOM   5682 C CG2 . THR D 1 202 ? 51.654 21.633  40.181  1.00 58.67  ?  425 THR A CG2 1 
ATOM   5683 N N   . PHE D 1 203 ? 49.322 20.190  44.013  1.00 60.69  ?  426 PHE A N   1 
ATOM   5684 C CA  . PHE D 1 203 ? 49.156 20.086  45.454  1.00 59.96  ?  426 PHE A CA  1 
ATOM   5685 C C   . PHE D 1 203 ? 49.375 18.643  45.904  1.00 60.61  ?  426 PHE A C   1 
ATOM   5686 O O   . PHE D 1 203 ? 48.870 17.710  45.270  1.00 55.77  ?  426 PHE A O   1 
ATOM   5687 C CB  . PHE D 1 203 ? 47.764 20.561  45.868  1.00 60.41  ?  426 PHE A CB  1 
ATOM   5688 C CG  . PHE D 1 203 ? 47.654 20.942  47.319  1.00 64.67  ?  426 PHE A CG  1 
ATOM   5689 C CD1 . PHE D 1 203 ? 47.358 19.989  48.281  1.00 61.13  ?  426 PHE A CD1 1 
ATOM   5690 C CD2 . PHE D 1 203 ? 47.839 22.255  47.720  1.00 60.67  ?  426 PHE A CD2 1 
ATOM   5691 C CE1 . PHE D 1 203 ? 47.254 20.339  49.615  1.00 59.79  ?  426 PHE A CE1 1 
ATOM   5692 C CE2 . PHE D 1 203 ? 47.736 22.610  49.052  1.00 60.80  ?  426 PHE A CE2 1 
ATOM   5693 C CZ  . PHE D 1 203 ? 47.444 21.652  50.001  1.00 60.98  ?  426 PHE A CZ  1 
ATOM   5694 N N   . PRO D 1 204 ? 50.123 18.425  46.987  1.00 60.12  ?  427 PRO A N   1 
ATOM   5695 C CA  . PRO D 1 204 ? 50.376 17.051  47.449  1.00 63.05  ?  427 PRO A CA  1 
ATOM   5696 C C   . PRO D 1 204 ? 49.093 16.384  47.923  1.00 58.14  ?  427 PRO A C   1 
ATOM   5697 O O   . PRO D 1 204 ? 48.372 16.919  48.767  1.00 56.24  ?  427 PRO A O   1 
ATOM   5698 C CB  . PRO D 1 204 ? 51.373 17.240  48.599  1.00 61.70  ?  427 PRO A CB  1 
ATOM   5699 C CG  . PRO D 1 204 ? 51.180 18.655  49.046  1.00 59.62  ?  427 PRO A CG  1 
ATOM   5700 C CD  . PRO D 1 204 ? 50.818 19.426  47.812  1.00 57.10  ?  427 PRO A CD  1 
ATOM   5701 N N   . GLY D 1 205 ? 48.816 15.204  47.371  1.00 53.88  ?  428 GLY A N   1 
ATOM   5702 C CA  . GLY D 1 205 ? 47.621 14.461  47.702  1.00 52.32  ?  428 GLY A CA  1 
ATOM   5703 C C   . GLY D 1 205 ? 46.415 14.761  46.838  1.00 49.80  ?  428 GLY A C   1 
ATOM   5704 O O   . GLY D 1 205 ? 45.337 14.209  47.097  1.00 48.18  ?  428 GLY A O   1 
ATOM   5705 N N   . GLU D 1 206 ? 46.558 15.608  45.824  1.00 47.32  ?  429 GLU A N   1 
ATOM   5706 C CA  . GLU D 1 206 ? 45.455 15.985  44.954  1.00 50.28  ?  429 GLU A CA  1 
ATOM   5707 C C   . GLU D 1 206 ? 45.600 15.323  43.589  1.00 46.58  ?  429 GLU A C   1 
ATOM   5708 O O   . GLU D 1 206 ? 46.712 15.105  43.097  1.00 49.88  ?  429 GLU A O   1 
ATOM   5709 C CB  . GLU D 1 206 ? 45.378 17.507  44.787  1.00 50.95  ?  429 GLU A CB  1 
ATOM   5710 C CG  . GLU D 1 206 ? 44.558 18.210  45.860  1.00 51.53  ?  429 GLU A CG  1 
ATOM   5711 C CD  . GLU D 1 206 ? 44.447 19.706  45.625  1.00 54.39  ?  429 GLU A CD  1 
ATOM   5712 O OE1 . GLU D 1 206 ? 44.748 20.158  44.501  1.00 56.83  ?  429 GLU A OE1 1 
ATOM   5713 O OE2 . GLU D 1 206 ? 44.065 20.431  46.568  1.00 57.58  ?  429 GLU A OE2 1 
ATOM   5714 N N   . GLN D 1 207 ? 44.459 15.000  42.986  1.00 49.45  ?  430 GLN A N   1 
ATOM   5715 C CA  . GLN D 1 207 ? 44.403 14.448  41.641  1.00 43.47  ?  430 GLN A CA  1 
ATOM   5716 C C   . GLN D 1 207 ? 43.418 15.257  40.812  1.00 44.07  ?  430 GLN A C   1 
ATOM   5717 O O   . GLN D 1 207 ? 42.541 15.941  41.345  1.00 46.62  ?  430 GLN A O   1 
ATOM   5718 C CB  . GLN D 1 207 ? 43.980 12.973  41.646  1.00 40.07  ?  430 GLN A CB  1 
ATOM   5719 C CG  . GLN D 1 207 ? 45.132 11.988  41.714  1.00 42.02  ?  430 GLN A CG  1 
ATOM   5720 C CD  . GLN D 1 207 ? 44.684 10.614  42.169  1.00 49.02  ?  430 GLN A CD  1 
ATOM   5721 O OE1 . GLN D 1 207 ? 45.495 9.801   42.613  1.00 52.31  ?  430 GLN A OE1 1 
ATOM   5722 N NE2 . GLN D 1 207 ? 43.387 10.348  42.060  1.00 46.82  ?  430 GLN A NE2 1 
ATOM   5723 N N   . LEU D 1 208 ? 43.570 15.167  39.495  1.00 45.30  ?  431 LEU A N   1 
ATOM   5724 C CA  . LEU D 1 208 ? 42.637 15.825  38.593  1.00 41.83  ?  431 LEU A CA  1 
ATOM   5725 C C   . LEU D 1 208 ? 41.252 15.201  38.712  1.00 39.54  ?  431 LEU A C   1 
ATOM   5726 O O   . LEU D 1 208 ? 41.113 13.991  38.908  1.00 41.92  ?  431 LEU A O   1 
ATOM   5727 C CB  . LEU D 1 208 ? 43.129 15.720  37.148  1.00 40.30  ?  431 LEU A CB  1 
ATOM   5728 C CG  . LEU D 1 208 ? 44.364 16.543  36.782  1.00 41.81  ?  431 LEU A CG  1 
ATOM   5729 C CD1 . LEU D 1 208 ? 44.809 16.245  35.359  1.00 46.53  ?  431 LEU A CD1 1 
ATOM   5730 C CD2 . LEU D 1 208 ? 44.077 18.021  36.962  1.00 39.66  ?  431 LEU A CD2 1 
ATOM   5731 N N   . LEU D 1 209 ? 40.224 16.038  38.597  1.00 38.09  ?  432 LEU A N   1 
ATOM   5732 C CA  . LEU D 1 209 ? 38.843 15.577  38.500  1.00 39.80  ?  432 LEU A CA  1 
ATOM   5733 C C   . LEU D 1 209 ? 38.411 15.693  37.043  1.00 40.38  ?  432 LEU A C   1 
ATOM   5734 O O   . LEU D 1 209 ? 38.308 16.801  36.506  1.00 39.20  ?  432 LEU A O   1 
ATOM   5735 C CB  . LEU D 1 209 ? 37.920 16.379  39.414  1.00 41.26  ?  432 LEU A CB  1 
ATOM   5736 C CG  . LEU D 1 209 ? 36.491 15.841  39.531  1.00 40.68  ?  432 LEU A CG  1 
ATOM   5737 C CD1 . LEU D 1 209 ? 36.493 14.425  40.087  1.00 34.49  ?  432 LEU A CD1 1 
ATOM   5738 C CD2 . LEU D 1 209 ? 35.631 16.753  40.389  1.00 45.23  ?  432 LEU A CD2 1 
ATOM   5739 N N   . PHE D 1 210 ? 38.166 14.553  36.406  1.00 35.80  ?  433 PHE A N   1 
ATOM   5740 C CA  . PHE D 1 210 ? 37.800 14.503  35.000  1.00 37.11  ?  433 PHE A CA  1 
ATOM   5741 C C   . PHE D 1 210 ? 36.287 14.398  34.846  1.00 38.93  ?  433 PHE A C   1 
ATOM   5742 O O   . PHE D 1 210 ? 35.613 13.740  35.644  1.00 34.52  ?  433 PHE A O   1 
ATOM   5743 C CB  . PHE D 1 210 ? 38.462 13.311  34.304  1.00 38.57  ?  433 PHE A CB  1 
ATOM   5744 C CG  . PHE D 1 210 ? 39.962 13.380  34.269  1.00 38.64  ?  433 PHE A CG  1 
ATOM   5745 C CD1 . PHE D 1 210 ? 40.610 14.249  33.408  1.00 37.15  ?  433 PHE A CD1 1 
ATOM   5746 C CD2 . PHE D 1 210 ? 40.725 12.563  35.086  1.00 38.16  ?  433 PHE A CD2 1 
ATOM   5747 C CE1 . PHE D 1 210 ? 41.991 14.310  33.370  1.00 39.31  ?  433 PHE A CE1 1 
ATOM   5748 C CE2 . PHE D 1 210 ? 42.106 12.619  35.053  1.00 38.31  ?  433 PHE A CE2 1 
ATOM   5749 C CZ  . PHE D 1 210 ? 42.739 13.493  34.194  1.00 37.03  ?  433 PHE A CZ  1 
ATOM   5750 N N   . PHE D 1 211 ? 35.763 15.057  33.814  1.00 31.45  ?  434 PHE A N   1 
ATOM   5751 C CA  . PHE D 1 211 ? 34.376 14.895  33.390  1.00 35.66  ?  434 PHE A CA  1 
ATOM   5752 C C   . PHE D 1 211 ? 34.370 13.892  32.240  1.00 34.71  ?  434 PHE A C   1 
ATOM   5753 O O   . PHE D 1 211 ? 34.782 14.218  31.121  1.00 35.84  ?  434 PHE A O   1 
ATOM   5754 C CB  . PHE D 1 211 ? 33.769 16.236  32.980  1.00 38.55  ?  434 PHE A CB  1 
ATOM   5755 C CG  . PHE D 1 211 ? 33.769 17.262  34.083  1.00 37.08  ?  434 PHE A CG  1 
ATOM   5756 C CD1 . PHE D 1 211 ? 34.897 18.024  34.342  1.00 39.33  ?  434 PHE A CD1 1 
ATOM   5757 C CD2 . PHE D 1 211 ? 32.641 17.460  34.860  1.00 33.42  ?  434 PHE A CD2 1 
ATOM   5758 C CE1 . PHE D 1 211 ? 34.900 18.964  35.358  1.00 39.18  ?  434 PHE A CE1 1 
ATOM   5759 C CE2 . PHE D 1 211 ? 32.636 18.400  35.876  1.00 37.38  ?  434 PHE A CE2 1 
ATOM   5760 C CZ  . PHE D 1 211 ? 33.768 19.153  36.124  1.00 34.64  ?  434 PHE A CZ  1 
ATOM   5761 N N   . ARG D 1 212 ? 33.911 12.674  32.518  1.00 37.43  ?  435 ARG A N   1 
ATOM   5762 C CA  . ARG D 1 212 ? 34.141 11.524  31.653  1.00 35.70  ?  435 ARG A CA  1 
ATOM   5763 C C   . ARG D 1 212 ? 32.887 11.151  30.871  1.00 34.93  ?  435 ARG A C   1 
ATOM   5764 O O   . ARG D 1 212 ? 31.779 11.144  31.416  1.00 35.12  ?  435 ARG A O   1 
ATOM   5765 C CB  . ARG D 1 212 ? 34.611 10.323  32.479  1.00 35.01  ?  435 ARG A CB  1 
ATOM   5766 C CG  . ARG D 1 212 ? 34.578 8.993   31.749  1.00 41.74  ?  435 ARG A CG  1 
ATOM   5767 C CD  . ARG D 1 212 ? 35.368 7.941   32.506  1.00 41.42  ?  435 ARG A CD  1 
ATOM   5768 N NE  . ARG D 1 212 ? 36.805 8.165   32.402  1.00 42.35  ?  435 ARG A NE  1 
ATOM   5769 C CZ  . ARG D 1 212 ? 37.727 7.269   32.723  1.00 41.63  ?  435 ARG A CZ  1 
ATOM   5770 N NH1 . ARG D 1 212 ? 37.398 6.072   33.183  1.00 45.28  ?  435 ARG A NH1 1 
ATOM   5771 N NH2 . ARG D 1 212 ? 39.012 7.579   32.574  1.00 41.57  ?  435 ARG A NH2 1 
ATOM   5772 N N   . SER D 1 213 ? 33.079 10.839  29.588  1.00 35.07  ?  436 SER A N   1 
ATOM   5773 C CA  . SER D 1 213 ? 32.044 10.299  28.720  1.00 37.01  ?  436 SER A CA  1 
ATOM   5774 C C   . SER D 1 213 ? 32.565 9.028   28.061  1.00 35.21  ?  436 SER A C   1 
ATOM   5775 O O   . SER D 1 213 ? 33.763 8.733   28.083  1.00 36.30  ?  436 SER A O   1 
ATOM   5776 C CB  . SER D 1 213 ? 31.616 11.309  27.643  1.00 32.46  ?  436 SER A CB  1 
ATOM   5777 O OG  . SER D 1 213 ? 31.032 12.468  28.213  1.00 39.08  ?  436 SER A OG  1 
ATOM   5778 N N   . THR D 1 214 ? 31.651 8.272   27.460  1.00 37.08  ?  437 THR A N   1 
ATOM   5779 C CA  . THR D 1 214 ? 31.993 7.081   26.690  1.00 40.38  ?  437 THR A CA  1 
ATOM   5780 C C   . THR D 1 214 ? 31.695 7.363   25.223  1.00 35.91  ?  437 THR A C   1 
ATOM   5781 O O   . THR D 1 214 ? 30.528 7.506   24.837  1.00 35.77  ?  437 THR A O   1 
ATOM   5782 C CB  . THR D 1 214 ? 31.220 5.858   27.183  1.00 36.54  ?  437 THR A CB  1 
ATOM   5783 O OG1 . THR D 1 214 ? 31.306 5.779   28.610  1.00 36.47  ?  437 THR A OG1 1 
ATOM   5784 C CG2 . THR D 1 214 ? 31.792 4.585   26.574  1.00 38.48  ?  437 THR A CG2 1 
ATOM   5785 N N   . MET D 1 215 ? 32.744 7.457   24.412  1.00 32.93  ?  438 MET A N   1 
ATOM   5786 C CA  . MET D 1 215 ? 32.554 7.627   22.980  1.00 35.39  ?  438 MET A CA  1 
ATOM   5787 C C   . MET D 1 215 ? 31.939 6.362   22.386  1.00 36.77  ?  438 MET A C   1 
ATOM   5788 O O   . MET D 1 215 ? 32.326 5.251   22.757  1.00 39.38  ?  438 MET A O   1 
ATOM   5789 C CB  . MET D 1 215 ? 33.880 7.929   22.285  1.00 34.57  ?  438 MET A CB  1 
ATOM   5790 C CG  . MET D 1 215 ? 34.399 9.337   22.501  1.00 38.70  ?  438 MET A CG  1 
ATOM   5791 S SD  . MET D 1 215 ? 35.982 9.606   21.687  1.00 47.51  ?  438 MET A SD  1 
ATOM   5792 C CE  . MET D 1 215 ? 37.042 8.531   22.652  1.00 35.21  ?  438 MET A CE  1 
ATOM   5793 N N   . PRO D 1 216 ? 30.972 6.495   21.480  1.00 38.65  ?  439 PRO A N   1 
ATOM   5794 C CA  . PRO D 1 216 ? 30.448 5.309   20.791  1.00 38.71  ?  439 PRO A CA  1 
ATOM   5795 C C   . PRO D 1 216 ? 31.552 4.593   20.030  1.00 39.70  ?  439 PRO A C   1 
ATOM   5796 O O   . PRO D 1 216 ? 32.461 5.221   19.480  1.00 36.49  ?  439 PRO A O   1 
ATOM   5797 C CB  . PRO D 1 216 ? 29.391 5.886   19.840  1.00 33.66  ?  439 PRO A CB  1 
ATOM   5798 C CG  . PRO D 1 216 ? 29.017 7.201   20.433  1.00 41.74  ?  439 PRO A CG  1 
ATOM   5799 C CD  . PRO D 1 216 ? 30.252 7.723   21.106  1.00 38.63  ?  439 PRO A CD  1 
ATOM   5800 N N   . GLY D 1 217 ? 31.476 3.267   20.016  1.00 38.66  ?  440 GLY A N   1 
ATOM   5801 C CA  . GLY D 1 217 ? 32.401 2.445   19.254  1.00 39.12  ?  440 GLY A CA  1 
ATOM   5802 C C   . GLY D 1 217 ? 31.730 1.913   17.999  1.00 40.72  ?  440 GLY A C   1 
ATOM   5803 O O   . GLY D 1 217 ? 30.572 1.497   18.032  1.00 42.77  ?  440 GLY A O   1 
ATOM   5804 N N   . CYS D 1 218 ? 32.474 1.930   16.892  1.00 39.96  ?  441 CYS A N   1 
ATOM   5805 C CA  . CYS D 1 218 ? 31.930 1.536   15.601  1.00 40.11  ?  441 CYS A CA  1 
ATOM   5806 C C   . CYS D 1 218 ? 32.550 0.271   15.023  1.00 42.78  ?  441 CYS A C   1 
ATOM   5807 O O   . CYS D 1 218 ? 31.940 -0.338  14.139  1.00 42.73  ?  441 CYS A O   1 
ATOM   5808 C CB  . CYS D 1 218 ? 32.092 2.679   14.587  1.00 36.49  ?  441 CYS A CB  1 
ATOM   5809 S SG  . CYS D 1 218 ? 31.272 4.226   15.054  1.00 41.79  ?  441 CYS A SG  1 
ATOM   5810 N N   . SER D 1 219 ? 33.731 -0.132  15.490  1.00 44.47  ?  442 SER A N   1 
ATOM   5811 C CA  . SER D 1 219 ? 34.375 -1.351  15.021  1.00 48.03  ?  442 SER A CA  1 
ATOM   5812 C C   . SER D 1 219 ? 35.571 -1.656  15.911  1.00 47.19  ?  442 SER A C   1 
ATOM   5813 O O   . SER D 1 219 ? 36.303 -0.745  16.304  1.00 42.49  ?  442 SER A O   1 
ATOM   5814 C CB  . SER D 1 219 ? 34.825 -1.227  13.558  1.00 47.35  ?  442 SER A CB  1 
ATOM   5815 O OG  . SER D 1 219 ? 35.560 -2.370  13.152  1.00 53.01  ?  442 SER A OG  1 
ATOM   5816 N N   . GLY D 1 220 ? 35.759 -2.937  16.218  1.00 46.88  ?  443 GLY A N   1 
ATOM   5817 C CA  . GLY D 1 220 ? 36.879 -3.367  17.035  1.00 46.49  ?  443 GLY A CA  1 
ATOM   5818 C C   . GLY D 1 220 ? 36.644 -3.303  18.530  1.00 44.37  ?  443 GLY A C   1 
ATOM   5819 O O   . GLY D 1 220 ? 35.515 -3.458  19.008  1.00 42.95  ?  443 GLY A O   1 
ATOM   5820 N N   . TYR D 1 221 ? 37.727 -3.077  19.273  1.00 40.94  ?  444 TYR A N   1 
ATOM   5821 C CA  . TYR D 1 221 ? 37.713 -3.001  20.735  1.00 45.49  ?  444 TYR A CA  1 
ATOM   5822 C C   . TYR D 1 221 ? 38.383 -1.698  21.156  1.00 48.34  ?  444 TYR A C   1 
ATOM   5823 O O   . TYR D 1 221 ? 39.473 -1.708  21.742  1.00 46.97  ?  444 TYR A O   1 
ATOM   5824 C CB  . TYR D 1 221 ? 38.436 -4.199  21.355  1.00 47.27  ?  444 TYR A CB  1 
ATOM   5825 C CG  . TYR D 1 221 ? 37.980 -5.556  20.862  1.00 49.50  ?  444 TYR A CG  1 
ATOM   5826 C CD1 . TYR D 1 221 ? 38.434 -6.074  19.651  1.00 49.94  ?  444 TYR A CD1 1 
ATOM   5827 C CD2 . TYR D 1 221 ? 37.111 -6.330  21.618  1.00 53.87  ?  444 TYR A CD2 1 
ATOM   5828 C CE1 . TYR D 1 221 ? 38.021 -7.319  19.206  1.00 51.09  ?  444 TYR A CE1 1 
ATOM   5829 C CE2 . TYR D 1 221 ? 36.695 -7.575  21.182  1.00 53.87  ?  444 TYR A CE2 1 
ATOM   5830 C CZ  . TYR D 1 221 ? 37.152 -8.064  19.978  1.00 54.26  ?  444 TYR A CZ  1 
ATOM   5831 O OH  . TYR D 1 221 ? 36.732 -9.303  19.549  1.00 63.70  ?  444 TYR A OH  1 
ATOM   5832 N N   . PRO D 1 222 ? 37.769 -0.556  20.861  1.00 42.75  ?  445 PRO A N   1 
ATOM   5833 C CA  . PRO D 1 222 ? 38.449 0.720   21.091  1.00 43.35  ?  445 PRO A CA  1 
ATOM   5834 C C   . PRO D 1 222 ? 38.341 1.189   22.532  1.00 41.56  ?  445 PRO A C   1 
ATOM   5835 O O   . PRO D 1 222 ? 37.384 0.883   23.247  1.00 37.20  ?  445 PRO A O   1 
ATOM   5836 C CB  . PRO D 1 222 ? 37.711 1.676   20.145  1.00 40.42  ?  445 PRO A CB  1 
ATOM   5837 C CG  . PRO D 1 222 ? 36.322 1.130   20.091  1.00 39.58  ?  445 PRO A CG  1 
ATOM   5838 C CD  . PRO D 1 222 ? 36.413 -0.368  20.313  1.00 40.74  ?  445 PRO A CD  1 
ATOM   5839 N N   . ASN D 1 223 ? 39.358 1.936   22.954  1.00 43.42  ?  446 ASN A N   1 
ATOM   5840 C CA  . ASN D 1 223 ? 39.342 2.624   24.244  1.00 43.11  ?  446 ASN A CA  1 
ATOM   5841 C C   . ASN D 1 223 ? 38.395 3.810   24.130  1.00 42.29  ?  446 ASN A C   1 
ATOM   5842 O O   . ASN D 1 223 ? 38.738 4.843   23.552  1.00 40.64  ?  446 ASN A O   1 
ATOM   5843 C CB  . ASN D 1 223 ? 40.748 3.067   24.633  1.00 40.97  ?  446 ASN A CB  1 
ATOM   5844 C CG  . ASN D 1 223 ? 40.819 3.627   26.045  1.00 44.85  ?  446 ASN A CG  1 
ATOM   5845 O OD1 . ASN D 1 223 ? 39.797 3.827   26.704  1.00 41.82  ?  446 ASN A OD1 1 
ATOM   5846 N ND2 . ASN D 1 223 ? 42.034 3.883   26.514  1.00 45.48  ?  446 ASN A ND2 1 
ATOM   5847 N N   . MET D 1 224 ? 37.195 3.669   24.685  1.00 39.26  ?  447 MET A N   1 
ATOM   5848 C CA  . MET D 1 224 ? 36.132 4.644   24.491  1.00 41.40  ?  447 MET A CA  1 
ATOM   5849 C C   . MET D 1 224 ? 36.053 5.679   25.607  1.00 42.14  ?  447 MET A C   1 
ATOM   5850 O O   . MET D 1 224 ? 35.129 6.500   25.609  1.00 42.19  ?  447 MET A O   1 
ATOM   5851 C CB  . MET D 1 224 ? 34.792 3.925   24.338  1.00 39.58  ?  447 MET A CB  1 
ATOM   5852 C CG  . MET D 1 224 ? 34.700 3.107   23.060  1.00 40.04  ?  447 MET A CG  1 
ATOM   5853 S SD  . MET D 1 224 ? 33.277 2.009   23.026  1.00 41.48  ?  447 MET A SD  1 
ATOM   5854 C CE  . MET D 1 224 ? 33.862 0.663   24.055  1.00 33.66  ?  447 MET A CE  1 
ATOM   5855 N N   . ASP D 1 225 ? 36.998 5.672   26.544  1.00 44.23  ?  448 ASP A N   1 
ATOM   5856 C CA  . ASP D 1 225 ? 37.014 6.685   27.593  1.00 41.21  ?  448 ASP A CA  1 
ATOM   5857 C C   . ASP D 1 225 ? 37.458 8.026   27.025  1.00 38.31  ?  448 ASP A C   1 
ATOM   5858 O O   . ASP D 1 225 ? 38.460 8.108   26.307  1.00 41.64  ?  448 ASP A O   1 
ATOM   5859 C CB  . ASP D 1 225 ? 37.948 6.266   28.728  1.00 40.38  ?  448 ASP A CB  1 
ATOM   5860 C CG  . ASP D 1 225 ? 37.504 4.990   29.410  1.00 46.30  ?  448 ASP A CG  1 
ATOM   5861 O OD1 . ASP D 1 225 ? 36.296 4.677   29.364  1.00 48.78  ?  448 ASP A OD1 1 
ATOM   5862 O OD2 . ASP D 1 225 ? 38.366 4.300   29.995  1.00 48.38  ?  448 ASP A OD2 1 
ATOM   5863 N N   . LEU D 1 226 ? 36.714 9.082   27.348  1.00 38.14  ?  449 LEU A N   1 
ATOM   5864 C CA  . LEU D 1 226 ? 37.090 10.440  26.975  1.00 36.89  ?  449 LEU A CA  1 
ATOM   5865 C C   . LEU D 1 226 ? 36.904 11.347  28.181  1.00 36.16  ?  449 LEU A C   1 
ATOM   5866 O O   . LEU D 1 226 ? 35.780 11.521  28.663  1.00 34.90  ?  449 LEU A O   1 
ATOM   5867 C CB  . LEU D 1 226 ? 36.267 10.949  25.790  1.00 32.48  ?  449 LEU A CB  1 
ATOM   5868 C CG  . LEU D 1 226 ? 36.816 12.255  25.209  1.00 37.36  ?  449 LEU A CG  1 
ATOM   5869 C CD1 . LEU D 1 226 ? 38.142 12.022  24.496  1.00 29.75  ?  449 LEU A CD1 1 
ATOM   5870 C CD2 . LEU D 1 226 ? 35.812 12.892  24.278  1.00 34.15  ?  449 LEU A CD2 1 
ATOM   5871 N N   . ASP D 1 227 ? 38.001 11.920  28.660  1.00 36.47  ?  450 ASP A N   1 
ATOM   5872 C CA  . ASP D 1 227 ? 37.994 12.813  29.810  1.00 35.91  ?  450 ASP A CA  1 
ATOM   5873 C C   . ASP D 1 227 ? 38.253 14.237  29.342  1.00 35.45  ?  450 ASP A C   1 
ATOM   5874 O O   . ASP D 1 227 ? 39.178 14.479  28.561  1.00 40.05  ?  450 ASP A O   1 
ATOM   5875 C CB  . ASP D 1 227 ? 39.055 12.395  30.831  1.00 36.45  ?  450 ASP A CB  1 
ATOM   5876 C CG  . ASP D 1 227 ? 38.857 10.979  31.335  1.00 44.11  ?  450 ASP A CG  1 
ATOM   5877 O OD1 . ASP D 1 227 ? 37.778 10.689  31.894  1.00 42.02  ?  450 ASP A OD1 1 
ATOM   5878 O OD2 . ASP D 1 227 ? 39.781 10.154  31.169  1.00 48.39  ?  450 ASP A OD2 1 
ATOM   5879 N N   . CYS D 1 228 ? 37.435 15.175  29.815  1.00 34.79  ?  451 CYS A N   1 
ATOM   5880 C CA  . CYS D 1 228 ? 37.649 16.591  29.566  1.00 33.63  ?  451 CYS A CA  1 
ATOM   5881 C C   . CYS D 1 228 ? 37.779 17.329  30.893  1.00 40.66  ?  451 CYS A C   1 
ATOM   5882 O O   . CYS D 1 228 ? 37.263 16.885  31.924  1.00 35.20  ?  451 CYS A O   1 
ATOM   5883 C CB  . CYS D 1 228 ? 36.520 17.195  28.716  1.00 33.82  ?  451 CYS A CB  1 
ATOM   5884 S SG  . CYS D 1 228 ? 34.916 17.367  29.531  1.00 37.74  ?  451 CYS A SG  1 
ATOM   5885 N N   . LEU D 1 229 ? 38.488 18.461  30.857  1.00 39.68  ?  452 LEU A N   1 
ATOM   5886 C CA  . LEU D 1 229 ? 38.789 19.201  32.077  1.00 33.86  ?  452 LEU A CA  1 
ATOM   5887 C C   . LEU D 1 229 ? 37.638 20.100  32.508  1.00 36.18  ?  452 LEU A C   1 
ATOM   5888 O O   . LEU D 1 229 ? 37.482 20.369  33.705  1.00 37.93  ?  452 LEU A O   1 
ATOM   5889 C CB  . LEU D 1 229 ? 40.055 20.036  31.884  1.00 35.43  ?  452 LEU A CB  1 
ATOM   5890 C CG  . LEU D 1 229 ? 41.313 19.267  31.472  1.00 38.28  ?  452 LEU A CG  1 
ATOM   5891 C CD1 . LEU D 1 229 ? 42.451 20.227  31.161  1.00 41.68  ?  452 LEU A CD1 1 
ATOM   5892 C CD2 . LEU D 1 229 ? 41.720 18.284  32.555  1.00 36.48  ?  452 LEU A CD2 1 
ATOM   5893 N N   . LEU D 1 230 ? 36.831 20.575  31.560  1.00 35.24  ?  453 LEU A N   1 
ATOM   5894 C CA  . LEU D 1 230 ? 35.689 21.419  31.857  1.00 36.79  ?  453 LEU A CA  1 
ATOM   5895 C C   . LEU D 1 230 ? 34.527 21.004  30.968  1.00 36.86  ?  453 LEU A C   1 
ATOM   5896 O O   . LEU D 1 230 ? 34.719 20.774  29.764  1.00 38.01  ?  453 LEU A O   1 
ATOM   5897 C CB  . LEU D 1 230 ? 35.998 22.906  31.632  1.00 35.58  ?  453 LEU A CB  1 
ATOM   5898 C CG  . LEU D 1 230 ? 37.085 23.558  32.491  1.00 42.45  ?  453 LEU A CG  1 
ATOM   5899 C CD1 . LEU D 1 230 ? 37.437 24.930  31.938  1.00 35.69  ?  453 LEU A CD1 1 
ATOM   5900 C CD2 . LEU D 1 230 ? 36.648 23.658  33.948  1.00 30.27  ?  453 LEU A CD2 1 
ATOM   5901 N N   . PRO D 1 231 ? 33.321 20.888  31.522  1.00 34.90  ?  454 PRO A N   1 
ATOM   5902 C CA  . PRO D 1 231 ? 32.145 20.685  30.672  1.00 33.88  ?  454 PRO A CA  1 
ATOM   5903 C C   . PRO D 1 231 ? 31.963 21.864  29.730  1.00 35.03  ?  454 PRO A C   1 
ATOM   5904 O O   . PRO D 1 231 ? 32.300 23.004  30.059  1.00 40.00  ?  454 PRO A O   1 
ATOM   5905 C CB  . PRO D 1 231 ? 30.986 20.581  31.672  1.00 31.83  ?  454 PRO A CB  1 
ATOM   5906 C CG  . PRO D 1 231 ? 31.625 20.289  32.990  1.00 35.65  ?  454 PRO A CG  1 
ATOM   5907 C CD  . PRO D 1 231 ? 32.983 20.913  32.954  1.00 32.54  ?  454 PRO A CD  1 
ATOM   5908 N N   . GLN D 1 232 ? 31.426 21.575  28.543  1.00 35.01  ?  455 GLN A N   1 
ATOM   5909 C CA  . GLN D 1 232 ? 31.257 22.616  27.536  1.00 39.84  ?  455 GLN A CA  1 
ATOM   5910 C C   . GLN D 1 232 ? 30.357 23.740  28.036  1.00 37.90  ?  455 GLN A C   1 
ATOM   5911 O O   . GLN D 1 232 ? 30.561 24.905  27.675  1.00 36.30  ?  455 GLN A O   1 
ATOM   5912 C CB  . GLN D 1 232 ? 30.696 22.010  26.247  1.00 32.88  ?  455 GLN A CB  1 
ATOM   5913 C CG  . GLN D 1 232 ? 30.572 22.991  25.089  1.00 36.23  ?  455 GLN A CG  1 
ATOM   5914 C CD  . GLN D 1 232 ? 31.914 23.521  24.617  1.00 38.52  ?  455 GLN A CD  1 
ATOM   5915 O OE1 . GLN D 1 232 ? 32.954 22.895  24.823  1.00 37.75  ?  455 GLN A OE1 1 
ATOM   5916 N NE2 . GLN D 1 232 ? 31.896 24.685  23.980  1.00 36.71  ?  455 GLN A NE2 1 
ATOM   5917 N N   . GLU D 1 233 ? 29.373 23.416  28.876  1.00 38.24  ?  456 GLU A N   1 
ATOM   5918 C CA  . GLU D 1 233 ? 28.499 24.449  29.419  1.00 39.70  ?  456 GLU A CA  1 
ATOM   5919 C C   . GLU D 1 233 ? 29.241 25.362  30.388  1.00 42.08  ?  456 GLU A C   1 
ATOM   5920 O O   . GLU D 1 233 ? 28.886 26.538  30.522  1.00 43.84  ?  456 GLU A O   1 
ATOM   5921 C CB  . GLU D 1 233 ? 27.288 23.808  30.099  1.00 34.78  ?  456 GLU A CB  1 
ATOM   5922 C CG  . GLU D 1 233 ? 26.229 23.292  29.128  1.00 35.26  ?  456 GLU A CG  1 
ATOM   5923 C CD  . GLU D 1 233 ? 26.639 22.004  28.425  1.00 42.42  ?  456 GLU A CD  1 
ATOM   5924 O OE1 . GLU D 1 233 ? 27.612 21.356  28.870  1.00 36.50  ?  456 GLU A OE1 1 
ATOM   5925 O OE2 . GLU D 1 233 ? 25.987 21.642  27.422  1.00 40.09  ?  456 GLU A OE2 1 
ATOM   5926 N N   . TRP D 1 234 ? 30.270 24.846  31.068  1.00 38.73  ?  457 TRP A N   1 
ATOM   5927 C CA  . TRP D 1 234 ? 31.103 25.711  31.898  1.00 38.05  ?  457 TRP A CA  1 
ATOM   5928 C C   . TRP D 1 234 ? 31.937 26.652  31.038  1.00 40.18  ?  457 TRP A C   1 
ATOM   5929 O O   . TRP D 1 234 ? 32.186 27.800  31.424  1.00 41.50  ?  457 TRP A O   1 
ATOM   5930 C CB  . TRP D 1 234 ? 32.008 24.873  32.800  1.00 33.17  ?  457 TRP A CB  1 
ATOM   5931 C CG  . TRP D 1 234 ? 31.306 24.239  33.961  1.00 32.45  ?  457 TRP A CG  1 
ATOM   5932 C CD1 . TRP D 1 234 ? 29.980 23.931  34.053  1.00 30.71  ?  457 TRP A CD1 1 
ATOM   5933 C CD2 . TRP D 1 234 ? 31.901 23.822  35.196  1.00 32.97  ?  457 TRP A CD2 1 
ATOM   5934 N NE1 . TRP D 1 234 ? 29.712 23.354  35.271  1.00 33.31  ?  457 TRP A NE1 1 
ATOM   5935 C CE2 . TRP D 1 234 ? 30.875 23.275  35.990  1.00 30.04  ?  457 TRP A CE2 1 
ATOM   5936 C CE3 . TRP D 1 234 ? 33.203 23.859  35.707  1.00 34.30  ?  457 TRP A CE3 1 
ATOM   5937 C CZ2 . TRP D 1 234 ? 31.109 22.770  37.268  1.00 33.06  ?  457 TRP A CZ2 1 
ATOM   5938 C CZ3 . TRP D 1 234 ? 33.434 23.355  36.973  1.00 34.81  ?  457 TRP A CZ3 1 
ATOM   5939 C CH2 . TRP D 1 234 ? 32.391 22.818  37.739  1.00 33.79  ?  457 TRP A CH2 1 
ATOM   5940 N N   . VAL D 1 235 ? 32.382 26.178  29.872  1.00 40.90  ?  458 VAL A N   1 
ATOM   5941 C CA  . VAL D 1 235 ? 33.125 27.033  28.951  1.00 38.79  ?  458 VAL A CA  1 
ATOM   5942 C C   . VAL D 1 235 ? 32.236 28.162  28.442  1.00 43.12  ?  458 VAL A C   1 
ATOM   5943 O O   . VAL D 1 235 ? 32.643 29.330  28.410  1.00 41.57  ?  458 VAL A O   1 
ATOM   5944 C CB  . VAL D 1 235 ? 33.698 26.198  27.790  1.00 38.50  ?  458 VAL A CB  1 
ATOM   5945 C CG1 . VAL D 1 235 ? 34.242 27.102  26.695  1.00 38.29  ?  458 VAL A CG1 1 
ATOM   5946 C CG2 . VAL D 1 235 ? 34.780 25.254  28.295  1.00 37.91  ?  458 VAL A CG2 1 
ATOM   5947 N N   . GLN D 1 236 ? 31.007 27.829  28.038  1.00 44.40  ?  459 GLN A N   1 
ATOM   5948 C CA  . GLN D 1 236 ? 30.069 28.852  27.588  1.00 44.32  ?  459 GLN A CA  1 
ATOM   5949 C C   . GLN D 1 236 ? 29.741 29.830  28.708  1.00 48.24  ?  459 GLN A C   1 
ATOM   5950 O O   . GLN D 1 236 ? 29.594 31.034  28.470  1.00 43.53  ?  459 GLN A O   1 
ATOM   5951 C CB  . GLN D 1 236 ? 28.789 28.196  27.070  1.00 36.09  ?  459 GLN A CB  1 
ATOM   5952 C CG  . GLN D 1 236 ? 28.937 27.477  25.743  1.00 45.15  ?  459 GLN A CG  1 
ATOM   5953 C CD  . GLN D 1 236 ? 27.744 26.595  25.432  1.00 46.07  ?  459 GLN A CD  1 
ATOM   5954 O OE1 . GLN D 1 236 ? 27.149 25.998  26.331  1.00 48.90  ?  459 GLN A OE1 1 
ATOM   5955 N NE2 . GLN D 1 236 ? 27.382 26.515  24.157  1.00 46.72  ?  459 GLN A NE2 1 
ATOM   5956 N N   . TYR D 1 237 ? 29.624 29.327  29.937  1.00 47.07  ?  460 TYR A N   1 
ATOM   5957 C CA  . TYR D 1 237 ? 29.259 30.176  31.066  1.00 44.28  ?  460 TYR A CA  1 
ATOM   5958 C C   . TYR D 1 237 ? 30.386 31.139  31.417  1.00 49.10  ?  460 TYR A C   1 
ATOM   5959 O O   . TYR D 1 237 ? 30.151 32.335  31.628  1.00 46.25  ?  460 TYR A O   1 
ATOM   5960 C CB  . TYR D 1 237 ? 28.899 29.303  32.267  1.00 44.35  ?  460 TYR A CB  1 
ATOM   5961 C CG  . TYR D 1 237 ? 28.156 30.021  33.369  1.00 48.24  ?  460 TYR A CG  1 
ATOM   5962 C CD1 . TYR D 1 237 ? 26.801 30.301  33.251  1.00 47.00  ?  460 TYR A CD1 1 
ATOM   5963 C CD2 . TYR D 1 237 ? 28.808 30.407  34.530  1.00 50.30  ?  460 TYR A CD2 1 
ATOM   5964 C CE1 . TYR D 1 237 ? 26.118 30.954  34.261  1.00 51.88  ?  460 TYR A CE1 1 
ATOM   5965 C CE2 . TYR D 1 237 ? 28.135 31.061  35.544  1.00 55.38  ?  460 TYR A CE2 1 
ATOM   5966 C CZ  . TYR D 1 237 ? 26.791 31.332  35.405  1.00 55.96  ?  460 TYR A CZ  1 
ATOM   5967 O OH  . TYR D 1 237 ? 26.118 31.982  36.415  1.00 59.72  ?  460 TYR A OH  1 
ATOM   5968 N N   . PHE D 1 238 ? 31.620 30.635  31.485  1.00 44.69  ?  461 PHE A N   1 
ATOM   5969 C CA  . PHE D 1 238 ? 32.746 31.492  31.844  1.00 41.93  ?  461 PHE A CA  1 
ATOM   5970 C C   . PHE D 1 238 ? 32.976 32.569  30.791  1.00 46.55  ?  461 PHE A C   1 
ATOM   5971 O O   . PHE D 1 238 ? 33.338 33.705  31.122  1.00 43.54  ?  461 PHE A O   1 
ATOM   5972 C CB  . PHE D 1 238 ? 34.008 30.649  32.037  1.00 37.20  ?  461 PHE A CB  1 
ATOM   5973 C CG  . PHE D 1 238 ? 33.927 29.682  33.190  1.00 44.21  ?  461 PHE A CG  1 
ATOM   5974 C CD1 . PHE D 1 238 ? 33.043 29.896  34.234  1.00 42.75  ?  461 PHE A CD1 1 
ATOM   5975 C CD2 . PHE D 1 238 ? 34.741 28.559  33.227  1.00 37.85  ?  461 PHE A CD2 1 
ATOM   5976 C CE1 . PHE D 1 238 ? 32.966 29.004  35.294  1.00 40.08  ?  461 PHE A CE1 1 
ATOM   5977 C CE2 . PHE D 1 238 ? 34.671 27.667  34.284  1.00 36.07  ?  461 PHE A CE2 1 
ATOM   5978 C CZ  . PHE D 1 238 ? 33.783 27.890  35.318  1.00 35.26  ?  461 PHE A CZ  1 
ATOM   5979 N N   . TYR D 1 239 ? 32.757 32.236  29.517  1.00 45.20  ?  462 TYR A N   1 
ATOM   5980 C CA  . TYR D 1 239 ? 32.973 33.207  28.450  1.00 46.89  ?  462 TYR A CA  1 
ATOM   5981 C C   . TYR D 1 239 ? 31.978 34.359  28.536  1.00 47.36  ?  462 TYR A C   1 
ATOM   5982 O O   . TYR D 1 239 ? 32.324 35.508  28.238  1.00 53.42  ?  462 TYR A O   1 
ATOM   5983 C CB  . TYR D 1 239 ? 32.879 32.513  27.091  1.00 46.31  ?  462 TYR A CB  1 
ATOM   5984 C CG  . TYR D 1 239 ? 32.910 33.451  25.907  1.00 45.22  ?  462 TYR A CG  1 
ATOM   5985 C CD1 . TYR D 1 239 ? 34.114 33.922  25.399  1.00 48.44  ?  462 TYR A CD1 1 
ATOM   5986 C CD2 . TYR D 1 239 ? 31.734 33.857  25.285  1.00 47.30  ?  462 TYR A CD2 1 
ATOM   5987 C CE1 . TYR D 1 239 ? 34.147 34.777  24.314  1.00 55.05  ?  462 TYR A CE1 1 
ATOM   5988 C CE2 . TYR D 1 239 ? 31.758 34.713  24.199  1.00 48.65  ?  462 TYR A CE2 1 
ATOM   5989 C CZ  . TYR D 1 239 ? 32.968 35.168  23.717  1.00 49.31  ?  462 TYR A CZ  1 
ATOM   5990 O OH  . TYR D 1 239 ? 32.998 36.017  22.636  1.00 55.05  ?  462 TYR A OH  1 
ATOM   5991 N N   . GLN D 1 240 ? 30.740 34.072  28.943  1.00 46.62  ?  463 GLN A N   1 
ATOM   5992 C CA  . GLN D 1 240 ? 29.721 35.114  29.004  1.00 49.15  ?  463 GLN A CA  1 
ATOM   5993 C C   . GLN D 1 240 ? 29.836 35.945  30.274  1.00 56.36  ?  463 GLN A C   1 
ATOM   5994 O O   . GLN D 1 240 ? 29.739 37.176  30.222  1.00 53.81  ?  463 GLN A O   1 
ATOM   5995 C CB  . GLN D 1 240 ? 28.329 34.494  28.910  1.00 47.70  ?  463 GLN A CB  1 
ATOM   5996 C CG  . GLN D 1 240 ? 28.084 33.717  27.636  1.00 46.31  ?  463 GLN A CG  1 
ATOM   5997 C CD  . GLN D 1 240 ? 26.727 33.055  27.627  1.00 49.73  ?  463 GLN A CD  1 
ATOM   5998 O OE1 . GLN D 1 240 ? 25.697 33.729  27.635  1.00 46.13  ?  463 GLN A OE1 1 
ATOM   5999 N NE2 . GLN D 1 240 ? 26.714 31.726  27.621  1.00 49.80  ?  463 GLN A NE2 1 
ATOM   6000 N N   . GLU D 1 241 ? 30.032 35.293  31.422  1.00 49.31  ?  464 GLU A N   1 
ATOM   6001 C CA  . GLU D 1 241 ? 30.120 36.022  32.682  1.00 52.58  ?  464 GLU A CA  1 
ATOM   6002 C C   . GLU D 1 241 ? 31.334 36.942  32.698  1.00 53.12  ?  464 GLU A C   1 
ATOM   6003 O O   . GLU D 1 241 ? 31.240 38.106  33.105  1.00 59.46  ?  464 GLU A O   1 
ATOM   6004 C CB  . GLU D 1 241 ? 30.175 35.038  33.854  1.00 48.49  ?  464 GLU A CB  1 
ATOM   6005 C CG  . GLU D 1 241 ? 28.931 34.180  34.005  1.00 55.13  ?  464 GLU A CG  1 
ATOM   6006 C CD  . GLU D 1 241 ? 27.698 34.995  34.338  1.00 61.48  ?  464 GLU A CD  1 
ATOM   6007 O OE1 . GLU D 1 241 ? 27.502 35.317  35.529  1.00 64.24  ?  464 GLU A OE1 1 
ATOM   6008 O OE2 . GLU D 1 241 ? 26.922 35.310  33.410  1.00 58.19  ?  464 GLU A OE2 1 
ATOM   6009 N N   . ALA D 1 242 ? 32.486 36.434  32.251  1.00 47.73  ?  465 ALA A N   1 
ATOM   6010 C CA  . ALA D 1 242 ? 33.741 37.189  32.254  1.00 52.98  ?  465 ALA A CA  1 
ATOM   6011 C C   . ALA D 1 242 ? 34.062 37.729  33.644  1.00 55.73  ?  465 ALA A C   1 
ATOM   6012 O O   . ALA D 1 242 ? 34.664 38.795  33.790  1.00 52.31  ?  465 ALA A O   1 
ATOM   6013 C CB  . ALA D 1 242 ? 33.712 38.320  31.223  1.00 58.48  ?  465 ALA A CB  1 
ATOM   6014 N N   . ALA D 1 243 ? 33.656 36.992  34.672  1.00 53.22  ?  466 ALA A N   1 
ATOM   6015 C CA  . ALA D 1 243 ? 33.896 37.422  36.041  1.00 49.42  ?  466 ALA A CA  1 
ATOM   6016 C C   . ALA D 1 243 ? 35.379 37.294  36.370  1.00 54.27  ?  466 ALA A C   1 
ATOM   6017 O O   . ALA D 1 243 ? 35.963 36.222  36.165  1.00 51.47  ?  466 ALA A O   1 
ATOM   6018 C CB  . ALA D 1 243 ? 33.063 36.595  37.016  1.00 48.80  ?  466 ALA A CB  1 
ATOM   6019 N N   . PRO D 1 244 ? 36.017 38.345  36.877  1.00 58.05  ?  467 PRO A N   1 
ATOM   6020 C CA  . PRO D 1 244 ? 37.450 38.262  37.172  1.00 53.83  ?  467 PRO A CA  1 
ATOM   6021 C C   . PRO D 1 244 ? 37.733 37.317  38.329  1.00 48.34  ?  467 PRO A C   1 
ATOM   6022 O O   . PRO D 1 244 ? 36.914 37.137  39.233  1.00 49.48  ?  467 PRO A O   1 
ATOM   6023 C CB  . PRO D 1 244 ? 37.822 39.705  37.532  1.00 58.14  ?  467 PRO A CB  1 
ATOM   6024 C CG  . PRO D 1 244 ? 36.546 40.304  38.024  1.00 57.60  ?  467 PRO A CG  1 
ATOM   6025 C CD  . PRO D 1 244 ? 35.455 39.665  37.210  1.00 54.58  ?  467 PRO A CD  1 
ATOM   6026 N N   . ALA D 1 245 ? 38.915 36.709  38.285  1.00 49.94  ?  468 ALA A N   1 
ATOM   6027 C CA  . ALA D 1 245 ? 39.363 35.812  39.339  1.00 53.05  ?  468 ALA A CA  1 
ATOM   6028 C C   . ALA D 1 245 ? 40.089 36.608  40.414  1.00 52.51  ?  468 ALA A C   1 
ATOM   6029 O O   . ALA D 1 245 ? 41.032 37.348  40.117  1.00 53.95  ?  468 ALA A O   1 
ATOM   6030 C CB  . ALA D 1 245 ? 40.278 34.724  38.775  1.00 48.52  ?  468 ALA A CB  1 
ATOM   6031 N N   . GLN D 1 246 ? 39.643 36.460  41.658  1.00 56.03  ?  469 GLN A N   1 
ATOM   6032 C CA  . GLN D 1 246 ? 40.255 37.132  42.794  1.00 58.82  ?  469 GLN A CA  1 
ATOM   6033 C C   . GLN D 1 246 ? 41.281 36.258  43.505  1.00 55.54  ?  469 GLN A C   1 
ATOM   6034 O O   . GLN D 1 246 ? 41.799 36.653  44.553  1.00 56.97  ?  469 GLN A O   1 
ATOM   6035 C CB  . GLN D 1 246 ? 39.174 37.589  43.775  1.00 48.59  ?  469 GLN A CB  1 
ATOM   6036 C CG  . GLN D 1 246 ? 38.060 38.385  43.117  1.00 59.73  ?  469 GLN A CG  1 
ATOM   6037 C CD  . GLN D 1 246 ? 36.832 38.515  43.996  1.00 66.83  ?  469 GLN A CD  1 
ATOM   6038 O OE1 . GLN D 1 246 ? 36.896 38.306  45.208  1.00 66.54  ?  469 GLN A OE1 1 
ATOM   6039 N NE2 . GLN D 1 246 ? 35.704 38.860  43.385  1.00 67.96  ?  469 GLN A NE2 1 
ATOM   6040 N N   . SER D 1 247 ? 41.586 35.088  42.954  1.00 53.40  ?  470 SER A N   1 
ATOM   6041 C CA  . SER D 1 247 ? 42.590 34.190  43.510  1.00 55.77  ?  470 SER A CA  1 
ATOM   6042 C C   . SER D 1 247 ? 43.047 33.254  42.394  1.00 57.42  ?  470 SER A C   1 
ATOM   6043 O O   . SER D 1 247 ? 42.703 33.446  41.223  1.00 57.70  ?  470 SER A O   1 
ATOM   6044 C CB  . SER D 1 247 ? 42.036 33.427  44.718  1.00 54.95  ?  470 SER A CB  1 
ATOM   6045 O OG  . SER D 1 247 ? 42.651 32.158  44.847  1.00 56.69  ?  470 SER A OG  1 
ATOM   6046 N N   . ASP D 1 248 ? 43.826 32.236  42.757  1.00 53.49  ?  471 ASP A N   1 
ATOM   6047 C CA  . ASP D 1 248 ? 44.301 31.259  41.788  1.00 57.56  ?  471 ASP A CA  1 
ATOM   6048 C C   . ASP D 1 248 ? 43.502 29.963  41.802  1.00 55.80  ?  471 ASP A C   1 
ATOM   6049 O O   . ASP D 1 248 ? 43.554 29.213  40.822  1.00 56.83  ?  471 ASP A O   1 
ATOM   6050 C CB  . ASP D 1 248 ? 45.782 30.943  42.032  1.00 63.00  ?  471 ASP A CB  1 
ATOM   6051 C CG  . ASP D 1 248 ? 46.708 31.868  41.263  1.00 68.68  ?  471 ASP A CG  1 
ATOM   6052 O OD1 . ASP D 1 248 ? 46.265 32.973  40.882  1.00 74.99  ?  471 ASP A OD1 1 
ATOM   6053 O OD2 . ASP D 1 248 ? 47.877 31.489  41.038  1.00 69.71  ?  471 ASP A OD2 1 
ATOM   6054 N N   . VAL D 1 249 ? 42.776 29.680  42.881  1.00 50.27  ?  472 VAL A N   1 
ATOM   6055 C CA  . VAL D 1 249 ? 41.902 28.517  42.969  1.00 52.34  ?  472 VAL A CA  1 
ATOM   6056 C C   . VAL D 1 249 ? 40.566 28.956  43.549  1.00 53.05  ?  472 VAL A C   1 
ATOM   6057 O O   . VAL D 1 249 ? 40.512 29.808  44.443  1.00 49.00  ?  472 VAL A O   1 
ATOM   6058 C CB  . VAL D 1 249 ? 42.523 27.383  43.818  1.00 49.24  ?  472 VAL A CB  1 
ATOM   6059 C CG1 . VAL D 1 249 ? 43.810 26.877  43.183  1.00 52.88  ?  472 VAL A CG1 1 
ATOM   6060 C CG2 . VAL D 1 249 ? 42.787 27.852  45.239  1.00 58.22  ?  472 VAL A CG2 1 
ATOM   6061 N N   . ALA D 1 250 ? 39.484 28.386  43.027  1.00 50.61  ?  473 ALA A N   1 
ATOM   6062 C CA  . ALA D 1 250 ? 38.139 28.646  43.518  1.00 45.14  ?  473 ALA A CA  1 
ATOM   6063 C C   . ALA D 1 250 ? 37.602 27.386  44.179  1.00 46.56  ?  473 ALA A C   1 
ATOM   6064 O O   . ALA D 1 250 ? 37.666 26.299  43.596  1.00 49.98  ?  473 ALA A O   1 
ATOM   6065 C CB  . ALA D 1 250 ? 37.212 29.087  42.383  1.00 47.16  ?  473 ALA A CB  1 
ATOM   6066 N N   . LEU D 1 251 ? 37.085 27.531  45.396  1.00 47.73  ?  474 LEU A N   1 
ATOM   6067 C CA  . LEU D 1 251 ? 36.546 26.395  46.129  1.00 40.63  ?  474 LEU A CA  1 
ATOM   6068 C C   . LEU D 1 251 ? 35.110 26.139  45.687  1.00 43.78  ?  474 LEU A C   1 
ATOM   6069 O O   . LEU D 1 251 ? 34.252 27.021  45.795  1.00 40.49  ?  474 LEU A O   1 
ATOM   6070 C CB  . LEU D 1 251 ? 36.610 26.646  47.634  1.00 46.51  ?  474 LEU A CB  1 
ATOM   6071 C CG  . LEU D 1 251 ? 36.062 25.522  48.517  1.00 48.50  ?  474 LEU A CG  1 
ATOM   6072 C CD1 . LEU D 1 251 ? 36.976 24.312  48.468  1.00 38.83  ?  474 LEU A CD1 1 
ATOM   6073 C CD2 . LEU D 1 251 ? 35.881 25.994  49.949  1.00 44.33  ?  474 LEU A CD2 1 
ATOM   6074 N N   . LEU D 1 252 ? 34.854 24.938  45.179  1.00 40.32  ?  475 LEU A N   1 
ATOM   6075 C CA  . LEU D 1 252 ? 33.513 24.521  44.805  1.00 36.15  ?  475 LEU A CA  1 
ATOM   6076 C C   . LEU D 1 252 ? 33.043 23.408  45.729  1.00 36.81  ?  475 LEU A C   1 
ATOM   6077 O O   . LEU D 1 252 ? 33.844 22.622  46.246  1.00 37.21  ?  475 LEU A O   1 
ATOM   6078 C CB  . LEU D 1 252 ? 33.459 24.037  43.351  1.00 35.90  ?  475 LEU A CB  1 
ATOM   6079 C CG  . LEU D 1 252 ? 34.139 24.878  42.269  1.00 35.56  ?  475 LEU A CG  1 
ATOM   6080 C CD1 . LEU D 1 252 ? 34.012 24.185  40.921  1.00 36.50  ?  475 LEU A CD1 1 
ATOM   6081 C CD2 . LEU D 1 252 ? 33.552 26.279  42.210  1.00 36.72  ?  475 LEU A CD2 1 
ATOM   6082 N N   . ARG D 1 253 ? 31.732 23.351  45.937  1.00 37.16  ?  476 ARG A N   1 
ATOM   6083 C CA  . ARG D 1 253 ? 31.104 22.292  46.711  1.00 44.50  ?  476 ARG A CA  1 
ATOM   6084 C C   . ARG D 1 253 ? 30.054 21.611  45.850  1.00 37.89  ?  476 ARG A C   1 
ATOM   6085 O O   . ARG D 1 253 ? 29.185 22.279  45.276  1.00 36.77  ?  476 ARG A O   1 
ATOM   6086 C CB  . ARG D 1 253 ? 30.469 22.840  47.992  1.00 39.43  ?  476 ARG A CB  1 
ATOM   6087 C CG  . ARG D 1 253 ? 31.442 23.542  48.916  1.00 46.53  ?  476 ARG A CG  1 
ATOM   6088 C CD  . ARG D 1 253 ? 31.111 23.258  50.371  1.00 47.45  ?  476 ARG A CD  1 
ATOM   6089 N NE  . ARG D 1 253 ? 32.101 23.827  51.276  1.00 49.02  ?  476 ARG A NE  1 
ATOM   6090 C CZ  . ARG D 1 253 ? 32.146 25.105  51.629  1.00 55.71  ?  476 ARG A CZ  1 
ATOM   6091 N NH1 . ARG D 1 253 ? 31.263 25.978  51.172  1.00 49.74  ?  476 ARG A NH1 1 
ATOM   6092 N NH2 . ARG D 1 253 ? 33.099 25.515  52.459  1.00 57.89  ?  476 ARG A NH2 1 
ATOM   6093 N N   . PHE D 1 254 ? 30.145 20.288  45.749  1.00 40.32  ?  477 PHE A N   1 
ATOM   6094 C CA  . PHE D 1 254 ? 29.138 19.487  45.069  1.00 37.78  ?  477 PHE A CA  1 
ATOM   6095 C C   . PHE D 1 254 ? 28.065 19.111  46.081  1.00 34.45  ?  477 PHE A C   1 
ATOM   6096 O O   . PHE D 1 254 ? 28.352 18.435  47.075  1.00 34.73  ?  477 PHE A O   1 
ATOM   6097 C CB  . PHE D 1 254 ? 29.763 18.241  44.449  1.00 37.59  ?  477 PHE A CB  1 
ATOM   6098 C CG  . PHE D 1 254 ? 28.850 17.501  43.514  1.00 39.17  ?  477 PHE A CG  1 
ATOM   6099 C CD1 . PHE D 1 254 ? 27.996 16.517  43.990  1.00 37.08  ?  477 PHE A CD1 1 
ATOM   6100 C CD2 . PHE D 1 254 ? 28.849 17.786  42.158  1.00 38.12  ?  477 PHE A CD2 1 
ATOM   6101 C CE1 . PHE D 1 254 ? 27.156 15.835  43.130  1.00 36.52  ?  477 PHE A CE1 1 
ATOM   6102 C CE2 . PHE D 1 254 ? 28.012 17.107  41.294  1.00 39.13  ?  477 PHE A CE2 1 
ATOM   6103 C CZ  . PHE D 1 254 ? 27.165 16.129  41.781  1.00 40.50  ?  477 PHE A CZ  1 
ATOM   6104 N N   . VAL D 1 255 ? 26.834 19.542  45.827  1.00 34.32  ?  478 VAL A N   1 
ATOM   6105 C CA  . VAL D 1 255 ? 25.765 19.460  46.810  1.00 35.77  ?  478 VAL A CA  1 
ATOM   6106 C C   . VAL D 1 255 ? 24.570 18.730  46.220  1.00 36.16  ?  478 VAL A C   1 
ATOM   6107 O O   . VAL D 1 255 ? 24.305 18.797  45.015  1.00 42.09  ?  478 VAL A O   1 
ATOM   6108 C CB  . VAL D 1 255 ? 25.352 20.863  47.302  1.00 41.26  ?  478 VAL A CB  1 
ATOM   6109 C CG1 . VAL D 1 255 ? 26.448 21.461  48.166  1.00 32.91  ?  478 VAL A CG1 1 
ATOM   6110 C CG2 . VAL D 1 255 ? 25.068 21.764  46.117  1.00 40.20  ?  478 VAL A CG2 1 
ATOM   6111 N N   . ASN D 1 256 ? 23.846 18.023  47.086  1.00 38.04  ?  479 ASN A N   1 
ATOM   6112 C CA  . ASN D 1 256 ? 22.584 17.403  46.715  1.00 40.49  ?  479 ASN A CA  1 
ATOM   6113 C C   . ASN D 1 256 ? 21.458 18.354  47.095  1.00 41.22  ?  479 ASN A C   1 
ATOM   6114 O O   . ASN D 1 256 ? 21.203 18.543  48.294  1.00 44.40  ?  479 ASN A O   1 
ATOM   6115 C CB  . ASN D 1 256 ? 22.416 16.064  47.422  1.00 39.38  ?  479 ASN A CB  1 
ATOM   6116 C CG  . ASN D 1 256 ? 21.223 15.277  46.913  1.00 42.69  ?  479 ASN A CG  1 
ATOM   6117 O OD1 . ASN D 1 256 ? 20.427 15.775  46.118  1.00 41.40  ?  479 ASN A OD1 1 
ATOM   6118 N ND2 . ASN D 1 256 ? 21.097 14.035  47.371  1.00 45.03  ?  479 ASN A ND2 1 
ATOM   6119 N N   . PRO D 1 257 ? 20.764 18.970  46.134  1.00 41.38  ?  480 PRO A N   1 
ATOM   6120 C CA  . PRO D 1 257 ? 19.709 19.933  46.488  1.00 42.43  ?  480 PRO A CA  1 
ATOM   6121 C C   . PRO D 1 257 ? 18.512 19.306  47.182  1.00 47.31  ?  480 PRO A C   1 
ATOM   6122 O O   . PRO D 1 257 ? 17.668 20.046  47.707  1.00 46.97  ?  480 PRO A O   1 
ATOM   6123 C CB  . PRO D 1 257 ? 19.310 20.532  45.132  1.00 45.27  ?  480 PRO A CB  1 
ATOM   6124 C CG  . PRO D 1 257 ? 19.677 19.485  44.135  1.00 42.74  ?  480 PRO A CG  1 
ATOM   6125 C CD  . PRO D 1 257 ? 20.908 18.815  44.676  1.00 42.51  ?  480 PRO A CD  1 
ATOM   6126 N N   . ASP D 1 258 ? 18.412 17.976  47.208  1.00 43.77  ?  481 ASP A N   1 
ATOM   6127 C CA  . ASP D 1 258 ? 17.283 17.324  47.860  1.00 47.67  ?  481 ASP A CA  1 
ATOM   6128 C C   . ASP D 1 258 ? 17.463 17.237  49.371  1.00 46.75  ?  481 ASP A C   1 
ATOM   6129 O O   . ASP D 1 258 ? 16.471 17.225  50.108  1.00 48.91  ?  481 ASP A O   1 
ATOM   6130 C CB  . ASP D 1 258 ? 17.078 15.925  47.273  1.00 49.10  ?  481 ASP A CB  1 
ATOM   6131 C CG  . ASP D 1 258 ? 16.962 15.937  45.758  1.00 56.98  ?  481 ASP A CG  1 
ATOM   6132 O OD1 . ASP D 1 258 ? 16.393 16.904  45.211  1.00 60.44  ?  481 ASP A OD1 1 
ATOM   6133 O OD2 . ASP D 1 258 ? 17.441 14.978  45.116  1.00 65.69  ?  481 ASP A OD2 1 
ATOM   6134 N N   . THR D 1 259 ? 18.708 17.178  49.847  1.00 46.60  ?  482 THR A N   1 
ATOM   6135 C CA  . THR D 1 259 ? 18.989 17.013  51.267  1.00 47.44  ?  482 THR A CA  1 
ATOM   6136 C C   . THR D 1 259 ? 19.909 18.076  51.849  1.00 48.61  ?  482 THR A C   1 
ATOM   6137 O O   . THR D 1 259 ? 20.010 18.164  53.078  1.00 49.69  ?  482 THR A O   1 
ATOM   6138 C CB  . THR D 1 259 ? 19.615 15.635  51.535  1.00 51.94  ?  482 THR A CB  1 
ATOM   6139 O OG1 . THR D 1 259 ? 20.868 15.541  50.846  1.00 49.89  ?  482 THR A OG1 1 
ATOM   6140 C CG2 . THR D 1 259 ? 18.692 14.520  51.061  1.00 48.11  ?  482 THR A CG2 1 
ATOM   6141 N N   . GLY D 1 260 ? 20.579 18.877  51.023  1.00 43.35  ?  483 GLY A N   1 
ATOM   6142 C CA  . GLY D 1 260 ? 21.558 19.825  51.508  1.00 40.13  ?  483 GLY A CA  1 
ATOM   6143 C C   . GLY D 1 260 ? 22.909 19.229  51.833  1.00 44.51  ?  483 GLY A C   1 
ATOM   6144 O O   . GLY D 1 260 ? 23.798 19.964  52.283  1.00 41.41  ?  483 GLY A O   1 
ATOM   6145 N N   . ARG D 1 261 ? 23.096 17.930  51.616  1.00 40.42  ?  484 ARG A N   1 
ATOM   6146 C CA  . ARG D 1 261 ? 24.363 17.282  51.927  1.00 38.96  ?  484 ARG A CA  1 
ATOM   6147 C C   . ARG D 1 261 ? 25.458 17.776  50.990  1.00 39.40  ?  484 ARG A C   1 
ATOM   6148 O O   . ARG D 1 261 ? 25.282 17.800  49.768  1.00 35.86  ?  484 ARG A O   1 
ATOM   6149 C CB  . ARG D 1 261 ? 24.222 15.763  51.814  1.00 48.64  ?  484 ARG A CB  1 
ATOM   6150 C CG  . ARG D 1 261 ? 23.514 15.099  52.985  1.00 54.57  ?  484 ARG A CG  1 
ATOM   6151 C CD  . ARG D 1 261 ? 24.110 15.525  54.317  1.00 58.65  ?  484 ARG A CD  1 
ATOM   6152 N NE  . ARG D 1 261 ? 23.159 15.371  55.410  1.00 66.76  ?  484 ARG A NE  1 
ATOM   6153 C CZ  . ARG D 1 261 ? 22.917 14.228  56.036  1.00 66.91  ?  484 ARG A CZ  1 
ATOM   6154 N NH1 . ARG D 1 261 ? 23.543 13.111  55.703  1.00 66.10  ?  484 ARG A NH1 1 
ATOM   6155 N NH2 . ARG D 1 261 ? 22.026 14.206  57.024  1.00 71.86  ?  484 ARG A NH2 1 
ATOM   6156 N N   . VAL D 1 262 ? 26.590 18.173  51.566  1.00 41.00  ?  485 VAL A N   1 
ATOM   6157 C CA  . VAL D 1 262 ? 27.778 18.506  50.786  1.00 38.88  ?  485 VAL A CA  1 
ATOM   6158 C C   . VAL D 1 262 ? 28.502 17.198  50.484  1.00 40.52  ?  485 VAL A C   1 
ATOM   6159 O O   . VAL D 1 262 ? 29.027 16.547  51.390  1.00 42.54  ?  485 VAL A O   1 
ATOM   6160 C CB  . VAL D 1 262 ? 28.689 19.486  51.531  1.00 38.77  ?  485 VAL A CB  1 
ATOM   6161 C CG1 . VAL D 1 262 ? 29.988 19.685  50.762  1.00 37.93  ?  485 VAL A CG1 1 
ATOM   6162 C CG2 . VAL D 1 262 ? 27.978 20.810  51.745  1.00 35.41  ?  485 VAL A CG2 1 
ATOM   6163 N N   . LEU D 1 263 ? 28.533 16.812  49.210  1.00 40.98  ?  486 LEU A N   1 
ATOM   6164 C CA  . LEU D 1 263 ? 29.005 15.482  48.852  1.00 39.38  ?  486 LEU A CA  1 
ATOM   6165 C C   . LEU D 1 263 ? 30.510 15.414  48.631  1.00 40.23  ?  486 LEU A C   1 
ATOM   6166 O O   . LEU D 1 263 ? 31.093 14.343  48.828  1.00 37.20  ?  486 LEU A O   1 
ATOM   6167 C CB  . LEU D 1 263 ? 28.267 14.978  47.610  1.00 35.78  ?  486 LEU A CB  1 
ATOM   6168 C CG  . LEU D 1 263 ? 26.840 14.514  47.919  1.00 39.94  ?  486 LEU A CG  1 
ATOM   6169 C CD1 . LEU D 1 263 ? 25.951 14.654  46.699  1.00 39.47  ?  486 LEU A CD1 1 
ATOM   6170 C CD2 . LEU D 1 263 ? 26.828 13.081  48.437  1.00 43.02  ?  486 LEU A CD2 1 
ATOM   6171 N N   . PHE D 1 264 ? 31.147 16.510  48.215  1.00 38.55  ?  487 PHE A N   1 
ATOM   6172 C CA  . PHE D 1 264 ? 32.605 16.609  48.209  1.00 36.91  ?  487 PHE A CA  1 
ATOM   6173 C C   . PHE D 1 264 ? 33.002 18.050  47.914  1.00 34.86  ?  487 PHE A C   1 
ATOM   6174 O O   . PHE D 1 264 ? 32.168 18.888  47.559  1.00 36.49  ?  487 PHE A O   1 
ATOM   6175 C CB  . PHE D 1 264 ? 33.264 15.633  47.215  1.00 39.77  ?  487 PHE A CB  1 
ATOM   6176 C CG  . PHE D 1 264 ? 33.062 15.974  45.759  1.00 36.87  ?  487 PHE A CG  1 
ATOM   6177 C CD1 . PHE D 1 264 ? 33.948 16.813  45.096  1.00 39.30  ?  487 PHE A CD1 1 
ATOM   6178 C CD2 . PHE D 1 264 ? 32.020 15.410  45.039  1.00 38.11  ?  487 PHE A CD2 1 
ATOM   6179 C CE1 . PHE D 1 264 ? 33.774 17.110  43.754  1.00 41.61  ?  487 PHE A CE1 1 
ATOM   6180 C CE2 . PHE D 1 264 ? 31.846 15.699  43.694  1.00 37.61  ?  487 PHE A CE2 1 
ATOM   6181 C CZ  . PHE D 1 264 ? 32.723 16.552  43.054  1.00 34.71  ?  487 PHE A CZ  1 
ATOM   6182 N N   . GLU D 1 265 ? 34.295 18.326  48.080  1.00 34.82  ?  488 GLU A N   1 
ATOM   6183 C CA  . GLU D 1 265 ? 34.885 19.635  47.849  1.00 41.82  ?  488 GLU A CA  1 
ATOM   6184 C C   . GLU D 1 265 ? 35.984 19.521  46.800  1.00 41.65  ?  488 GLU A C   1 
ATOM   6185 O O   . GLU D 1 265 ? 36.684 18.507  46.727  1.00 37.16  ?  488 GLU A O   1 
ATOM   6186 C CB  . GLU D 1 265 ? 35.472 20.210  49.143  1.00 41.82  ?  488 GLU A CB  1 
ATOM   6187 C CG  . GLU D 1 265 ? 34.766 21.437  49.679  1.00 48.00  ?  488 GLU A CG  1 
ATOM   6188 C CD  . GLU D 1 265 ? 35.263 21.821  51.060  1.00 52.01  ?  488 GLU A CD  1 
ATOM   6189 O OE1 . GLU D 1 265 ? 36.464 21.606  51.341  1.00 41.28  ?  488 GLU A OE1 1 
ATOM   6190 O OE2 . GLU D 1 265 ? 34.453 22.321  51.867  1.00 60.40  ?  488 GLU A OE2 1 
ATOM   6191 N N   . CYS D 1 266 ? 36.142 20.569  45.994  1.00 37.24  ?  489 CYS A N   1 
ATOM   6192 C CA  . CYS D 1 266 ? 37.152 20.548  44.945  1.00 42.14  ?  489 CYS A CA  1 
ATOM   6193 C C   . CYS D 1 266 ? 37.647 21.961  44.670  1.00 39.16  ?  489 CYS A C   1 
ATOM   6194 O O   . CYS D 1 266 ? 37.022 22.951  45.056  1.00 42.60  ?  489 CYS A O   1 
ATOM   6195 C CB  . CYS D 1 266 ? 36.613 19.910  43.656  1.00 37.62  ?  489 CYS A CB  1 
ATOM   6196 S SG  . CYS D 1 266 ? 35.200 20.758  42.913  1.00 40.21  ?  489 CYS A SG  1 
ATOM   6197 N N   . LYS D 1 267 ? 38.792 22.034  43.993  1.00 41.98  ?  490 LYS A N   1 
ATOM   6198 C CA  . LYS D 1 267 ? 39.395 23.290  43.569  1.00 39.82  ?  490 LYS A CA  1 
ATOM   6199 C C   . LYS D 1 267 ? 39.145 23.497  42.082  1.00 45.03  ?  490 LYS A C   1 
ATOM   6200 O O   . LYS D 1 267 ? 39.405 22.598  41.277  1.00 42.19  ?  490 LYS A O   1 
ATOM   6201 C CB  . LYS D 1 267 ? 40.901 23.292  43.830  1.00 40.78  ?  490 LYS A CB  1 
ATOM   6202 C CG  . LYS D 1 267 ? 41.319 23.412  45.275  1.00 46.33  ?  490 LYS A CG  1 
ATOM   6203 C CD  . LYS D 1 267 ? 42.832 23.320  45.373  1.00 51.94  ?  490 LYS A CD  1 
ATOM   6204 C CE  . LYS D 1 267 ? 43.334 23.734  46.738  1.00 51.01  ?  490 LYS A CE  1 
ATOM   6205 N NZ  . LYS D 1 267 ? 44.519 22.933  47.147  1.00 55.64  ?  490 LYS A NZ  1 
ATOM   6206 N N   . LEU D 1 268 ? 38.654 24.679  41.721  1.00 42.56  ?  491 LEU A N   1 
ATOM   6207 C CA  . LEU D 1 268 ? 38.555 25.094  40.322  1.00 41.47  ?  491 LEU A CA  1 
ATOM   6208 C C   . LEU D 1 268 ? 39.665 26.111  40.082  1.00 42.97  ?  491 LEU A C   1 
ATOM   6209 O O   . LEU D 1 268 ? 39.572 27.263  40.516  1.00 47.84  ?  491 LEU A O   1 
ATOM   6210 C CB  . LEU D 1 268 ? 37.180 25.673  40.006  1.00 40.00  ?  491 LEU A CB  1 
ATOM   6211 C CG  . LEU D 1 268 ? 37.033 26.322  38.625  1.00 39.06  ?  491 LEU A CG  1 
ATOM   6212 C CD1 . LEU D 1 268 ? 37.318 25.322  37.514  1.00 40.34  ?  491 LEU A CD1 1 
ATOM   6213 C CD2 . LEU D 1 268 ? 35.652 26.946  38.448  1.00 33.87  ?  491 LEU A CD2 1 
ATOM   6214 N N   . HIS D 1 269 ? 40.720 25.679  39.402  1.00 39.18  ?  492 HIS A N   1 
ATOM   6215 C CA  . HIS D 1 269 ? 41.862 26.547  39.165  1.00 42.18  ?  492 HIS A CA  1 
ATOM   6216 C C   . HIS D 1 269 ? 41.538 27.584  38.096  1.00 43.82  ?  492 HIS A C   1 
ATOM   6217 O O   . HIS D 1 269 ? 40.709 27.359  37.210  1.00 46.16  ?  492 HIS A O   1 
ATOM   6218 C CB  . HIS D 1 269 ? 43.082 25.723  38.756  1.00 46.76  ?  492 HIS A CB  1 
ATOM   6219 C CG  . HIS D 1 269 ? 43.525 24.746  39.802  1.00 45.83  ?  492 HIS A CG  1 
ATOM   6220 N ND1 . HIS D 1 269 ? 44.677 24.916  40.538  1.00 47.82  ?  492 HIS A ND1 1 
ATOM   6221 C CD2 . HIS D 1 269 ? 42.967 23.591  40.237  1.00 41.73  ?  492 HIS A CD2 1 
ATOM   6222 C CE1 . HIS D 1 269 ? 44.812 23.906  41.379  1.00 43.16  ?  492 HIS A CE1 1 
ATOM   6223 N NE2 . HIS D 1 269 ? 43.787 23.089  41.216  1.00 45.39  ?  492 HIS A NE2 1 
ATOM   6224 N N   . LYS D 1 270 ? 42.211 28.734  38.189  1.00 41.59  ?  493 LYS A N   1 
ATOM   6225 C CA  . LYS D 1 270 ? 41.902 29.854  37.306  1.00 45.44  ?  493 LYS A CA  1 
ATOM   6226 C C   . LYS D 1 270 ? 42.183 29.521  35.845  1.00 44.27  ?  493 LYS A C   1 
ATOM   6227 O O   . LYS D 1 270 ? 41.488 30.020  34.952  1.00 39.57  ?  493 LYS A O   1 
ATOM   6228 C CB  . LYS D 1 270 ? 42.694 31.089  37.739  1.00 46.81  ?  493 LYS A CB  1 
ATOM   6229 C CG  . LYS D 1 270 ? 42.374 32.350  36.951  1.00 52.02  ?  493 LYS A CG  1 
ATOM   6230 C CD  . LYS D 1 270 ? 43.607 33.225  36.793  1.00 57.36  ?  493 LYS A CD  1 
ATOM   6231 C CE  . LYS D 1 270 ? 44.005 33.859  38.116  1.00 59.94  ?  493 LYS A CE  1 
ATOM   6232 N NZ  . LYS D 1 270 ? 45.462 33.716  38.385  1.00 67.23  ?  493 LYS A NZ  1 
ATOM   6233 N N   . SER D 1 271 ? 43.186 28.681  35.581  1.00 41.31  ?  494 SER A N   1 
ATOM   6234 C CA  . SER D 1 271 ? 43.500 28.302  34.207  1.00 48.09  ?  494 SER A CA  1 
ATOM   6235 C C   . SER D 1 271 ? 42.472 27.352  33.604  1.00 43.98  ?  494 SER A C   1 
ATOM   6236 O O   . SER D 1 271 ? 42.475 27.162  32.383  1.00 48.21  ?  494 SER A O   1 
ATOM   6237 C CB  . SER D 1 271 ? 44.893 27.674  34.141  1.00 42.68  ?  494 SER A CB  1 
ATOM   6238 O OG  . SER D 1 271 ? 45.087 26.753  35.200  1.00 54.59  ?  494 SER A OG  1 
ATOM   6239 N N   . GLY D 1 272 ? 41.608 26.746  34.417  1.00 40.45  ?  495 GLY A N   1 
ATOM   6240 C CA  . GLY D 1 272 ? 40.487 25.993  33.887  1.00 42.78  ?  495 GLY A CA  1 
ATOM   6241 C C   . GLY D 1 272 ? 40.559 24.487  34.037  1.00 41.70  ?  495 GLY A C   1 
ATOM   6242 O O   . GLY D 1 272 ? 40.434 23.758  33.049  1.00 41.48  ?  495 GLY A O   1 
ATOM   6243 N N   . TYR D 1 273 ? 40.752 24.005  35.263  1.00 39.89  ?  496 TYR A N   1 
ATOM   6244 C CA  . TYR D 1 273 ? 40.679 22.574  35.538  1.00 41.69  ?  496 TYR A CA  1 
ATOM   6245 C C   . TYR D 1 273 ? 40.381 22.381  37.019  1.00 42.53  ?  496 TYR A C   1 
ATOM   6246 O O   . TYR D 1 273 ? 40.488 23.311  37.822  1.00 38.32  ?  496 TYR A O   1 
ATOM   6247 C CB  . TYR D 1 273 ? 41.963 21.848  35.118  1.00 36.36  ?  496 TYR A CB  1 
ATOM   6248 C CG  . TYR D 1 273 ? 43.210 22.253  35.872  1.00 39.26  ?  496 TYR A CG  1 
ATOM   6249 C CD1 . TYR D 1 273 ? 43.974 23.337  35.460  1.00 37.99  ?  496 TYR A CD1 1 
ATOM   6250 C CD2 . TYR D 1 273 ? 43.634 21.536  36.982  1.00 43.09  ?  496 TYR A CD2 1 
ATOM   6251 C CE1 . TYR D 1 273 ? 45.119 23.702  36.142  1.00 39.31  ?  496 TYR A CE1 1 
ATOM   6252 C CE2 . TYR D 1 273 ? 44.778 21.894  37.669  1.00 44.79  ?  496 TYR A CE2 1 
ATOM   6253 C CZ  . TYR D 1 273 ? 45.516 22.977  37.245  1.00 43.30  ?  496 TYR A CZ  1 
ATOM   6254 O OH  . TYR D 1 273 ? 46.654 23.333  37.930  1.00 44.73  ?  496 TYR A OH  1 
ATOM   6255 N N   . VAL D 1 274 ? 39.999 21.153  37.370  1.00 41.24  ?  497 VAL A N   1 
ATOM   6256 C CA  . VAL D 1 274 ? 39.494 20.825  38.697  1.00 39.79  ?  497 VAL A CA  1 
ATOM   6257 C C   . VAL D 1 274 ? 40.371 19.748  39.320  1.00 45.27  ?  497 VAL A C   1 
ATOM   6258 O O   . VAL D 1 274 ? 40.798 18.808  38.640  1.00 41.29  ?  497 VAL A O   1 
ATOM   6259 C CB  . VAL D 1 274 ? 38.022 20.361  38.637  1.00 36.39  ?  497 VAL A CB  1 
ATOM   6260 C CG1 . VAL D 1 274 ? 37.491 20.060  40.031  1.00 40.53  ?  497 VAL A CG1 1 
ATOM   6261 C CG2 . VAL D 1 274 ? 37.161 21.412  37.952  1.00 41.51  ?  497 VAL A CG2 1 
ATOM   6262 N N   . THR D 1 275 ? 40.638 19.887  40.620  1.00 38.63  ?  498 THR A N   1 
ATOM   6263 C CA  . THR D 1 275 ? 41.388 18.900  41.382  1.00 41.67  ?  498 THR A CA  1 
ATOM   6264 C C   . THR D 1 275 ? 40.618 18.530  42.643  1.00 43.66  ?  498 THR A C   1 
ATOM   6265 O O   . THR D 1 275 ? 39.857 19.335  43.186  1.00 39.58  ?  498 THR A O   1 
ATOM   6266 C CB  . THR D 1 275 ? 42.786 19.413  41.765  1.00 44.70  ?  498 THR A CB  1 
ATOM   6267 O OG1 . THR D 1 275 ? 42.669 20.661  42.460  1.00 46.71  ?  498 THR A OG1 1 
ATOM   6268 C CG2 . THR D 1 275 ? 43.646 19.605  40.525  1.00 43.57  ?  498 THR A CG2 1 
ATOM   6269 N N   . VAL D 1 276 ? 40.824 17.292  43.102  1.00 44.84  ?  499 VAL A N   1 
ATOM   6270 C CA  . VAL D 1 276 ? 40.187 16.773  44.304  1.00 40.75  ?  499 VAL A CA  1 
ATOM   6271 C C   . VAL D 1 276 ? 41.244 16.091  45.163  1.00 45.77  ?  499 VAL A C   1 
ATOM   6272 O O   . VAL D 1 276 ? 42.279 15.633  44.674  1.00 44.52  ?  499 VAL A O   1 
ATOM   6273 C CB  . VAL D 1 276 ? 39.043 15.786  43.988  1.00 40.27  ?  499 VAL A CB  1 
ATOM   6274 C CG1 . VAL D 1 276 ? 37.818 16.528  43.487  1.00 40.71  ?  499 VAL A CG1 1 
ATOM   6275 C CG2 . VAL D 1 276 ? 39.501 14.747  42.973  1.00 45.87  ?  499 VAL A CG2 1 
ATOM   6276 N N   . ALA D 1 277 ? 40.964 16.017  46.465  1.00 44.23  ?  500 ALA A N   1 
ATOM   6277 C CA  . ALA D 1 277 ? 41.870 15.390  47.427  1.00 48.50  ?  500 ALA A CA  1 
ATOM   6278 C C   . ALA D 1 277 ? 41.568 13.897  47.473  1.00 45.94  ?  500 ALA A C   1 
ATOM   6279 O O   . ALA D 1 277 ? 40.683 13.440  48.200  1.00 47.07  ?  500 ALA A O   1 
ATOM   6280 C CB  . ALA D 1 277 ? 41.732 16.035  48.800  1.00 41.58  ?  500 ALA A CB  1 
ATOM   6281 N N   . HIS D 1 278 ? 42.318 13.125  46.690  1.00 48.86  ?  501 HIS A N   1 
ATOM   6282 C CA  . HIS D 1 278 ? 42.143 11.681  46.640  1.00 49.95  ?  501 HIS A CA  1 
ATOM   6283 C C   . HIS D 1 278 ? 43.372 11.055  45.998  1.00 51.42  ?  501 HIS A C   1 
ATOM   6284 O O   . HIS D 1 278 ? 44.075 11.701  45.215  1.00 53.27  ?  501 HIS A O   1 
ATOM   6285 C CB  . HIS D 1 278 ? 40.880 11.291  45.863  1.00 54.12  ?  501 HIS A CB  1 
ATOM   6286 C CG  . HIS D 1 278 ? 40.585 9.823   45.888  1.00 52.41  ?  501 HIS A CG  1 
ATOM   6287 N ND1 . HIS D 1 278 ? 40.093 9.183   47.004  1.00 54.41  ?  501 HIS A ND1 1 
ATOM   6288 C CD2 . HIS D 1 278 ? 40.721 8.872   44.936  1.00 49.71  ?  501 HIS A CD2 1 
ATOM   6289 C CE1 . HIS D 1 278 ? 39.935 7.898   46.738  1.00 53.55  ?  501 HIS A CE1 1 
ATOM   6290 N NE2 . HIS D 1 278 ? 40.309 7.682   45.490  1.00 55.34  ?  501 HIS A NE2 1 
ATOM   6291 N N   . THR D 1 279 ? 43.617 9.791   46.339  1.00 53.90  ?  502 THR A N   1 
ATOM   6292 C CA  . THR D 1 279 ? 44.721 9.019   45.781  1.00 53.10  ?  502 THR A CA  1 
ATOM   6293 C C   . THR D 1 279 ? 44.168 7.710   45.242  1.00 53.30  ?  502 THR A C   1 
ATOM   6294 O O   . THR D 1 279 ? 43.576 6.926   45.993  1.00 54.09  ?  502 THR A O   1 
ATOM   6295 C CB  . THR D 1 279 ? 45.804 8.754   46.832  1.00 54.53  ?  502 THR A CB  1 
ATOM   6296 O OG1 . THR D 1 279 ? 46.368 9.998   47.266  1.00 52.75  ?  502 THR A OG1 1 
ATOM   6297 C CG2 . THR D 1 279 ? 46.908 7.880   46.255  1.00 50.97  ?  502 THR A CG2 1 
ATOM   6298 N N   . GLY D 1 280 ? 44.353 7.477   43.949  1.00 54.02  ?  503 GLY A N   1 
ATOM   6299 C CA  . GLY D 1 280 ? 43.894 6.270   43.297  1.00 51.15  ?  503 GLY A CA  1 
ATOM   6300 C C   . GLY D 1 280 ? 42.789 6.548   42.286  1.00 51.97  ?  503 GLY A C   1 
ATOM   6301 O O   . GLY D 1 280 ? 42.159 7.609   42.275  1.00 50.23  ?  503 GLY A O   1 
ATOM   6302 N N   . GLN D 1 281 ? 42.560 5.562   41.421  1.00 42.03  ?  504 GLN A N   1 
ATOM   6303 C CA  . GLN D 1 281 ? 41.527 5.663   40.398  1.00 46.51  ?  504 GLN A CA  1 
ATOM   6304 C C   . GLN D 1 281 ? 40.180 5.270   40.986  1.00 45.06  ?  504 GLN A C   1 
ATOM   6305 O O   . GLN D 1 281 ? 40.067 4.276   41.710  1.00 49.66  ?  504 GLN A O   1 
ATOM   6306 C CB  . GLN D 1 281 ? 41.857 4.762   39.208  1.00 48.04  ?  504 GLN A CB  1 
ATOM   6307 C CG  . GLN D 1 281 ? 43.009 5.257   38.343  1.00 52.48  ?  504 GLN A CG  1 
ATOM   6308 C CD  . GLN D 1 281 ? 43.214 4.407   37.103  1.00 61.23  ?  504 GLN A CD  1 
ATOM   6309 O OE1 . GLN D 1 281 ? 44.173 4.601   36.354  1.00 66.35  ?  504 GLN A OE1 1 
ATOM   6310 N NE2 . GLN D 1 281 ? 42.314 3.456   36.880  1.00 61.30  ?  504 GLN A NE2 1 
ATOM   6311 N N   . HIS D 1 282 ? 39.156 6.055   40.666  1.00 48.59  ?  505 HIS A N   1 
ATOM   6312 C CA  . HIS D 1 282 ? 37.838 5.835   41.240  1.00 48.59  ?  505 HIS A CA  1 
ATOM   6313 C C   . HIS D 1 282 ? 36.803 6.623   40.453  1.00 45.73  ?  505 HIS A C   1 
ATOM   6314 O O   . HIS D 1 282 ? 37.008 7.803   40.149  1.00 46.99  ?  505 HIS A O   1 
ATOM   6315 C CB  . HIS D 1 282 ? 37.813 6.250   42.715  1.00 49.46  ?  505 HIS A CB  1 
ATOM   6316 C CG  . HIS D 1 282 ? 37.009 5.337   43.587  1.00 60.54  ?  505 HIS A CG  1 
ATOM   6317 N ND1 . HIS D 1 282 ? 35.767 4.868   43.221  1.00 57.41  ?  505 HIS A ND1 1 
ATOM   6318 C CD2 . HIS D 1 282 ? 37.262 4.815   44.812  1.00 59.77  ?  505 HIS A CD2 1 
ATOM   6319 C CE1 . HIS D 1 282 ? 35.289 4.095   44.179  1.00 61.97  ?  505 HIS A CE1 1 
ATOM   6320 N NE2 . HIS D 1 282 ? 36.175 4.046   45.156  1.00 59.02  ?  505 HIS A NE2 1 
ATOM   6321 N N   . ASP D 1 283 ? 35.703 5.959   40.123  1.00 42.75  ?  506 ASP A N   1 
ATOM   6322 C CA  . ASP D 1 283 ? 34.511 6.636   39.647  1.00 46.12  ?  506 ASP A CA  1 
ATOM   6323 C C   . ASP D 1 283 ? 33.764 7.248   40.825  1.00 49.29  ?  506 ASP A C   1 
ATOM   6324 O O   . ASP D 1 283 ? 33.855 6.775   41.961  1.00 53.47  ?  506 ASP A O   1 
ATOM   6325 C CB  . ASP D 1 283 ? 33.590 5.664   38.906  1.00 48.66  ?  506 ASP A CB  1 
ATOM   6326 C CG  . ASP D 1 283 ? 34.250 5.027   37.697  1.00 53.32  ?  506 ASP A CG  1 
ATOM   6327 O OD1 . ASP D 1 283 ? 35.005 5.724   36.991  1.00 53.79  ?  506 ASP A OD1 1 
ATOM   6328 O OD2 . ASP D 1 283 ? 34.002 3.828   37.448  1.00 50.75  ?  506 ASP A OD2 1 
ATOM   6329 N N   . LEU D 1 284 ? 33.015 8.308   40.541  1.00 48.18  ?  507 LEU A N   1 
ATOM   6330 C CA  . LEU D 1 284 ? 32.229 9.010   41.548  1.00 44.02  ?  507 LEU A CA  1 
ATOM   6331 C C   . LEU D 1 284 ? 30.752 8.725   41.307  1.00 45.43  ?  507 LEU A C   1 
ATOM   6332 O O   . LEU D 1 284 ? 30.231 9.018   40.225  1.00 46.67  ?  507 LEU A O   1 
ATOM   6333 C CB  . LEU D 1 284 ? 32.503 10.514  41.513  1.00 39.35  ?  507 LEU A CB  1 
ATOM   6334 C CG  . LEU D 1 284 ? 33.728 11.005  42.292  1.00 44.34  ?  507 LEU A CG  1 
ATOM   6335 C CD1 . LEU D 1 284 ? 35.021 10.697  41.546  1.00 42.49  ?  507 LEU A CD1 1 
ATOM   6336 C CD2 . LEU D 1 284 ? 33.618 12.493  42.590  1.00 37.47  ?  507 LEU A CD2 1 
ATOM   6337 N N   . VAL D 1 285 ? 30.088 8.149   42.304  1.00 40.14  ?  508 VAL A N   1 
ATOM   6338 C CA  . VAL D 1 285 ? 28.658 7.869   42.233  1.00 41.14  ?  508 VAL A CA  1 
ATOM   6339 C C   . VAL D 1 285 ? 27.926 9.050   42.862  1.00 42.73  ?  508 VAL A C   1 
ATOM   6340 O O   . VAL D 1 285 ? 28.017 9.275   44.072  1.00 46.16  ?  508 VAL A O   1 
ATOM   6341 C CB  . VAL D 1 285 ? 28.305 6.553   42.934  1.00 46.11  ?  508 VAL A CB  1 
ATOM   6342 C CG1 . VAL D 1 285 ? 26.819 6.268   42.805  1.00 40.11  ?  508 VAL A CG1 1 
ATOM   6343 C CG2 . VAL D 1 285 ? 29.125 5.404   42.353  1.00 40.28  ?  508 VAL A CG2 1 
ATOM   6344 N N   . ILE D 1 286 ? 27.199 9.803   42.043  1.00 41.26  ?  509 ILE A N   1 
ATOM   6345 C CA  . ILE D 1 286 ? 26.547 11.033  42.490  1.00 46.98  ?  509 ILE A CA  1 
ATOM   6346 C C   . ILE D 1 286 ? 25.036 10.893  42.345  1.00 47.84  ?  509 ILE A C   1 
ATOM   6347 O O   . ILE D 1 286 ? 24.566 10.131  41.489  1.00 46.92  ?  509 ILE A O   1 
ATOM   6348 C CB  . ILE D 1 286 ? 27.062 12.251  41.704  1.00 45.25  ?  509 ILE A CB  1 
ATOM   6349 C CG1 . ILE D 1 286 ? 26.831 12.056  40.204  1.00 44.15  ?  509 ILE A CG1 1 
ATOM   6350 C CG2 . ILE D 1 286 ? 28.537 12.484  41.989  1.00 39.08  ?  509 ILE A CG2 1 
ATOM   6351 C CD1 . ILE D 1 286 ? 27.369 13.187  39.355  1.00 45.37  ?  509 ILE A CD1 1 
ATOM   6352 N N   . PRO D 1 287 ? 24.236 11.589  43.158  1.00 51.66  ?  510 PRO A N   1 
ATOM   6353 C CA  . PRO D 1 287 ? 22.796 11.586  42.932  1.00 50.03  ?  510 PRO A CA  1 
ATOM   6354 C C   . PRO D 1 287 ? 22.453 12.343  41.662  1.00 52.46  ?  510 PRO A C   1 
ATOM   6355 O O   . PRO D 1 287 ? 23.218 13.218  41.216  1.00 47.22  ?  510 PRO A O   1 
ATOM   6356 C CB  . PRO D 1 287 ? 22.240 12.295  44.180  1.00 44.35  ?  510 PRO A CB  1 
ATOM   6357 C CG  . PRO D 1 287 ? 23.359 13.119  44.679  1.00 48.50  ?  510 PRO A CG  1 
ATOM   6358 C CD  . PRO D 1 287 ? 24.605 12.352  44.364  1.00 48.42  ?  510 PRO A CD  1 
ATOM   6359 N N   . PRO D 1 288 ? 21.316 12.035  41.035  1.00 53.52  ?  511 PRO A N   1 
ATOM   6360 C CA  . PRO D 1 288 ? 21.011 12.645  39.732  1.00 53.50  ?  511 PRO A CA  1 
ATOM   6361 C C   . PRO D 1 288 ? 20.819 14.152  39.784  1.00 52.61  ?  511 PRO A C   1 
ATOM   6362 O O   . PRO D 1 288 ? 20.928 14.808  38.739  1.00 51.22  ?  511 PRO A O   1 
ATOM   6363 C CB  . PRO D 1 288 ? 19.719 11.935  39.300  1.00 55.16  ?  511 PRO A CB  1 
ATOM   6364 C CG  . PRO D 1 288 ? 19.127 11.408  40.570  1.00 57.06  ?  511 PRO A CG  1 
ATOM   6365 C CD  . PRO D 1 288 ? 20.280 11.079  41.462  1.00 53.22  ?  511 PRO A CD  1 
ATOM   6366 N N   . ASN D 1 289 ? 20.551 14.727  40.954  1.00 49.74  ?  512 ASN A N   1 
ATOM   6367 C CA  . ASN D 1 289 ? 20.287 16.153  41.070  1.00 47.61  ?  512 ASN A CA  1 
ATOM   6368 C C   . ASN D 1 289 ? 21.490 16.960  41.543  1.00 42.48  ?  512 ASN A C   1 
ATOM   6369 O O   . ASN D 1 289 ? 21.408 18.193  41.573  1.00 47.26  ?  512 ASN A O   1 
ATOM   6370 C CB  . ASN D 1 289 ? 19.115 16.401  42.026  1.00 57.27  ?  512 ASN A CB  1 
ATOM   6371 C CG  . ASN D 1 289 ? 17.774 16.120  41.386  1.00 61.66  ?  512 ASN A CG  1 
ATOM   6372 O OD1 . ASN D 1 289 ? 17.665 16.016  40.164  1.00 61.29  ?  512 ASN A OD1 1 
ATOM   6373 N ND2 . ASN D 1 289 ? 16.741 15.992  42.211  1.00 61.68  ?  512 ASN A ND2 1 
ATOM   6374 N N   . GLY D 1 290 ? 22.594 16.307  41.903  1.00 39.23  ?  513 GLY A N   1 
ATOM   6375 C CA  . GLY D 1 290 ? 23.732 17.033  42.433  1.00 40.08  ?  513 GLY A CA  1 
ATOM   6376 C C   . GLY D 1 290 ? 24.354 17.959  41.405  1.00 39.07  ?  513 GLY A C   1 
ATOM   6377 O O   . GLY D 1 290 ? 24.287 17.723  40.197  1.00 43.37  ?  513 GLY A O   1 
ATOM   6378 N N   . TYR D 1 291 ? 24.971 19.030  41.898  1.00 42.11  ?  514 TYR A N   1 
ATOM   6379 C CA  . TYR D 1 291 ? 25.629 19.993  41.026  1.00 42.52  ?  514 TYR A CA  1 
ATOM   6380 C C   . TYR D 1 291 ? 26.646 20.786  41.835  1.00 42.45  ?  514 TYR A C   1 
ATOM   6381 O O   . TYR D 1 291 ? 26.613 20.801  43.068  1.00 40.79  ?  514 TYR A O   1 
ATOM   6382 C CB  . TYR D 1 291 ? 24.614 20.925  40.351  1.00 44.15  ?  514 TYR A CB  1 
ATOM   6383 C CG  . TYR D 1 291 ? 23.958 21.926  41.275  1.00 44.65  ?  514 TYR A CG  1 
ATOM   6384 C CD1 . TYR D 1 291 ? 22.867 21.572  42.058  1.00 45.83  ?  514 TYR A CD1 1 
ATOM   6385 C CD2 . TYR D 1 291 ? 24.420 23.232  41.354  1.00 44.29  ?  514 TYR A CD2 1 
ATOM   6386 C CE1 . TYR D 1 291 ? 22.264 22.487  42.900  1.00 43.88  ?  514 TYR A CE1 1 
ATOM   6387 C CE2 . TYR D 1 291 ? 23.825 24.154  42.189  1.00 47.22  ?  514 TYR A CE2 1 
ATOM   6388 C CZ  . TYR D 1 291 ? 22.748 23.778  42.962  1.00 49.52  ?  514 TYR A CZ  1 
ATOM   6389 O OH  . TYR D 1 291 ? 22.157 24.702  43.794  1.00 43.06  ?  514 TYR A OH  1 
ATOM   6390 N N   . PHE D 1 292 ? 27.556 21.441  41.115  1.00 37.77  ?  515 PHE A N   1 
ATOM   6391 C CA  . PHE D 1 292 ? 28.620 22.215  41.744  1.00 38.92  ?  515 PHE A CA  1 
ATOM   6392 C C   . PHE D 1 292 ? 28.123 23.600  42.133  1.00 42.66  ?  515 PHE A C   1 
ATOM   6393 O O   . PHE D 1 292 ? 27.315 24.209  41.426  1.00 38.17  ?  515 PHE A O   1 
ATOM   6394 C CB  . PHE D 1 292 ? 29.816 22.349  40.800  1.00 37.35  ?  515 PHE A CB  1 
ATOM   6395 C CG  . PHE D 1 292 ? 30.478 21.045  40.459  1.00 38.85  ?  515 PHE A CG  1 
ATOM   6396 C CD1 . PHE D 1 292 ? 30.022 20.276  39.400  1.00 37.79  ?  515 PHE A CD1 1 
ATOM   6397 C CD2 . PHE D 1 292 ? 31.566 20.594  41.186  1.00 35.55  ?  515 PHE A CD2 1 
ATOM   6398 C CE1 . PHE D 1 292 ? 30.632 19.077  39.080  1.00 37.59  ?  515 PHE A CE1 1 
ATOM   6399 C CE2 . PHE D 1 292 ? 32.182 19.396  40.870  1.00 39.50  ?  515 PHE A CE2 1 
ATOM   6400 C CZ  . PHE D 1 292 ? 31.714 18.637  39.815  1.00 37.14  ?  515 PHE A CZ  1 
ATOM   6401 N N   . ARG D 1 293 ? 28.626 24.105  43.258  1.00 39.31  ?  516 ARG A N   1 
ATOM   6402 C CA  . ARG D 1 293 ? 28.284 25.437  43.740  1.00 41.11  ?  516 ARG A CA  1 
ATOM   6403 C C   . ARG D 1 293 ? 29.554 26.160  44.156  1.00 41.46  ?  516 ARG A C   1 
ATOM   6404 O O   . ARG D 1 293 ? 30.358 25.619  44.922  1.00 40.21  ?  516 ARG A O   1 
ATOM   6405 C CB  . ARG D 1 293 ? 27.304 25.369  44.915  1.00 43.41  ?  516 ARG A CB  1 
ATOM   6406 C CG  . ARG D 1 293 ? 25.890 25.780  44.555  1.00 49.35  ?  516 ARG A CG  1 
ATOM   6407 C CD  . ARG D 1 293 ? 25.087 26.159  45.791  1.00 54.68  ?  516 ARG A CD  1 
ATOM   6408 N NE  . ARG D 1 293 ? 24.893 27.600  45.898  1.00 50.60  ?  516 ARG A NE  1 
ATOM   6409 C CZ  . ARG D 1 293 ? 24.089 28.312  45.120  1.00 52.11  ?  516 ARG A CZ  1 
ATOM   6410 N NH1 . ARG D 1 293 ? 23.372 27.746  44.162  1.00 58.26  ?  516 ARG A NH1 1 
ATOM   6411 N NH2 . ARG D 1 293 ? 24.000 29.626  45.308  1.00 48.08  ?  516 ARG A NH2 1 
ATOM   6412 N N   . PHE D 1 294 ? 29.733 27.376  43.651  1.00 45.24  ?  517 PHE A N   1 
ATOM   6413 C CA  . PHE D 1 294 ? 30.896 28.171  44.016  1.00 42.87  ?  517 PHE A CA  1 
ATOM   6414 C C   . PHE D 1 294 ? 30.741 28.699  45.436  1.00 44.41  ?  517 PHE A C   1 
ATOM   6415 O O   . PHE D 1 294 ? 29.698 29.256  45.792  1.00 46.31  ?  517 PHE A O   1 
ATOM   6416 C CB  . PHE D 1 294 ? 31.080 29.328  43.035  1.00 39.99  ?  517 PHE A CB  1 
ATOM   6417 C CG  . PHE D 1 294 ? 32.082 30.354  43.485  1.00 48.39  ?  517 PHE A CG  1 
ATOM   6418 C CD1 . PHE D 1 294 ? 33.429 30.041  43.566  1.00 45.27  ?  517 PHE A CD1 1 
ATOM   6419 C CD2 . PHE D 1 294 ? 31.676 31.635  43.819  1.00 51.52  ?  517 PHE A CD2 1 
ATOM   6420 C CE1 . PHE D 1 294 ? 34.352 30.986  43.976  1.00 48.29  ?  517 PHE A CE1 1 
ATOM   6421 C CE2 . PHE D 1 294 ? 32.592 32.584  44.231  1.00 48.22  ?  517 PHE A CE2 1 
ATOM   6422 C CZ  . PHE D 1 294 ? 33.932 32.259  44.310  1.00 50.05  ?  517 PHE A CZ  1 
ATOM   6423 N N   . ASP D 1 295 ? 31.776 28.512  46.251  1.00 41.26  ?  518 ASP A N   1 
ATOM   6424 C CA  . ASP D 1 295 ? 31.745 29.010  47.619  1.00 52.07  ?  518 ASP A CA  1 
ATOM   6425 C C   . ASP D 1 295 ? 32.507 30.325  47.722  1.00 52.94  ?  518 ASP A C   1 
ATOM   6426 O O   . ASP D 1 295 ? 31.905 31.381  47.937  1.00 54.94  ?  518 ASP A O   1 
ATOM   6427 C CB  . ASP D 1 295 ? 32.321 27.978  48.591  1.00 46.86  ?  518 ASP A CB  1 
ATOM   6428 C CG  . ASP D 1 295 ? 32.755 28.597  49.907  1.00 61.70  ?  518 ASP A CG  1 
ATOM   6429 O OD1 . ASP D 1 295 ? 31.887 29.140  50.623  1.00 60.24  ?  518 ASP A OD1 1 
ATOM   6430 O OD2 . ASP D 1 295 ? 33.962 28.545  50.225  1.00 65.61  ?  518 ASP A OD2 1 
ATOM   6431 N N   . SER D 1 296 ? 33.826 30.278  47.557  1.00 50.25  ?  519 SER A N   1 
ATOM   6432 C CA  . SER D 1 296 ? 34.642 31.473  47.713  1.00 54.85  ?  519 SER A CA  1 
ATOM   6433 C C   . SER D 1 296 ? 35.990 31.253  47.044  1.00 54.76  ?  519 SER A C   1 
ATOM   6434 O O   . SER D 1 296 ? 36.385 30.122  46.755  1.00 51.93  ?  519 SER A O   1 
ATOM   6435 C CB  . SER D 1 296 ? 34.827 31.830  49.193  1.00 58.34  ?  519 SER A CB  1 
ATOM   6436 O OG  . SER D 1 296 ? 35.672 30.896  49.841  1.00 56.27  ?  519 SER A OG  1 
ATOM   6437 N N   . TRP D 1 297 ? 36.684 32.361  46.796  1.00 48.03  ?  520 TRP A N   1 
ATOM   6438 C CA  . TRP D 1 297 ? 38.064 32.312  46.332  1.00 49.75  ?  520 TRP A CA  1 
ATOM   6439 C C   . TRP D 1 297 ? 38.977 32.051  47.524  1.00 49.68  ?  520 TRP A C   1 
ATOM   6440 O O   . TRP D 1 297 ? 39.019 32.850  48.465  1.00 58.77  ?  520 TRP A O   1 
ATOM   6441 C CB  . TRP D 1 297 ? 38.445 33.620  45.642  1.00 45.05  ?  520 TRP A CB  1 
ATOM   6442 C CG  . TRP D 1 297 ? 37.734 33.849  44.346  1.00 51.23  ?  520 TRP A CG  1 
ATOM   6443 C CD1 . TRP D 1 297 ? 36.670 34.677  44.129  1.00 48.82  ?  520 TRP A CD1 1 
ATOM   6444 C CD2 . TRP D 1 297 ? 38.035 33.244  43.084  1.00 47.59  ?  520 TRP A CD2 1 
ATOM   6445 N NE1 . TRP D 1 297 ? 36.290 34.622  42.810  1.00 52.32  ?  520 TRP A NE1 1 
ATOM   6446 C CE2 . TRP D 1 297 ? 37.112 33.750  42.148  1.00 47.87  ?  520 TRP A CE2 1 
ATOM   6447 C CE3 . TRP D 1 297 ? 38.995 32.321  42.655  1.00 46.54  ?  520 TRP A CE3 1 
ATOM   6448 C CZ2 . TRP D 1 297 ? 37.121 33.364  40.808  1.00 50.83  ?  520 TRP A CZ2 1 
ATOM   6449 C CZ3 . TRP D 1 297 ? 39.004 31.942  41.326  1.00 47.12  ?  520 TRP A CZ3 1 
ATOM   6450 C CH2 . TRP D 1 297 ? 38.072 32.461  40.419  1.00 49.97  ?  520 TRP A CH2 1 
ATOM   6451 N N   . VAL D 1 298 ? 39.698 30.932  47.492  1.00 47.65  ?  521 VAL A N   1 
ATOM   6452 C CA  . VAL D 1 298 ? 40.612 30.591  48.575  1.00 45.50  ?  521 VAL A CA  1 
ATOM   6453 C C   . VAL D 1 298 ? 42.038 30.646  48.055  1.00 57.12  ?  521 VAL A C   1 
ATOM   6454 O O   . VAL D 1 298 ? 42.271 30.840  46.856  1.00 56.54  ?  521 VAL A O   1 
ATOM   6455 C CB  . VAL D 1 298 ? 40.292 29.208  49.167  1.00 53.11  ?  521 VAL A CB  1 
ATOM   6456 C CG1 . VAL D 1 298 ? 38.856 29.164  49.667  1.00 50.79  ?  521 VAL A CG1 1 
ATOM   6457 C CG2 . VAL D 1 298 ? 40.535 28.125  48.132  1.00 52.88  ?  521 VAL A CG2 1 
ATOM   6458 N N   . ASN D 1 299 ? 42.997 30.485  48.955  1.00 59.73  ?  522 ASN A N   1 
ATOM   6459 C CA  . ASN D 1 299 ? 44.388 30.475  48.554  1.00 65.03  ?  522 ASN A CA  1 
ATOM   6460 C C   . ASN D 1 299 ? 44.781 29.075  48.109  1.00 64.77  ?  522 ASN A C   1 
ATOM   6461 O O   . ASN D 1 299 ? 44.089 28.084  48.357  1.00 71.75  ?  522 ASN A O   1 
ATOM   6462 C CB  . ASN D 1 299 ? 45.291 30.972  49.687  1.00 64.86  ?  522 ASN A CB  1 
ATOM   6463 C CG  . ASN D 1 299 ? 45.938 29.849  50.468  1.00 72.03  ?  522 ASN A CG  1 
ATOM   6464 O OD1 . ASN D 1 299 ? 46.969 29.312  50.062  1.00 75.28  ?  522 ASN A OD1 1 
ATOM   6465 N ND2 . ASN D 1 299 ? 45.333 29.481  51.591  1.00 70.98  ?  522 ASN A ND2 1 
ATOM   6466 N N   . GLN D 1 300 ? 45.908 29.019  47.426  1.00 70.16  ?  523 GLN A N   1 
ATOM   6467 C CA  . GLN D 1 300 ? 46.406 27.804  46.816  1.00 68.81  ?  523 GLN A CA  1 
ATOM   6468 C C   . GLN D 1 300 ? 46.855 26.740  47.823  1.00 70.22  ?  523 GLN A C   1 
ATOM   6469 O O   . GLN D 1 300 ? 46.912 25.558  47.462  1.00 70.09  ?  523 GLN A O   1 
ATOM   6470 C CB  . GLN D 1 300 ? 47.558 28.210  45.944  1.00 69.78  ?  523 GLN A CB  1 
ATOM   6471 C CG  . GLN D 1 300 ? 48.648 28.742  46.832  1.00 75.89  ?  523 GLN A CG  1 
ATOM   6472 C CD  . GLN D 1 300 ? 49.776 29.263  46.043  1.00 83.49  ?  523 GLN A CD  1 
ATOM   6473 O OE1 . GLN D 1 300 ? 50.511 28.486  45.485  1.00 84.22  ?  523 GLN A OE1 1 
ATOM   6474 N NE2 . GLN D 1 300 ? 49.968 30.577  46.030  1.00 81.51  ?  523 GLN A NE2 1 
ATOM   6475 N N   . PHE D 1 301 ? 47.208 27.123  49.055  1.00 68.56  ?  524 PHE A N   1 
ATOM   6476 C CA  . PHE D 1 301 ? 47.592 26.161  50.080  1.00 69.96  ?  524 PHE A CA  1 
ATOM   6477 C C   . PHE D 1 301 ? 46.387 25.629  50.848  1.00 66.52  ?  524 PHE A C   1 
ATOM   6478 O O   . PHE D 1 301 ? 46.560 24.915  51.841  1.00 61.01  ?  524 PHE A O   1 
ATOM   6479 C CB  . PHE D 1 301 ? 48.595 26.783  51.054  1.00 71.57  ?  524 PHE A CB  1 
ATOM   6480 C CG  . PHE D 1 301 ? 49.964 27.014  50.469  1.00 72.90  ?  524 PHE A CG  1 
ATOM   6481 C CD1 . PHE D 1 301 ? 50.222 28.096  49.642  1.00 69.11  ?  524 PHE A CD1 1 
ATOM   6482 C CD2 . PHE D 1 301 ? 50.988 26.124  50.732  1.00 73.19  ?  524 PHE A CD2 1 
ATOM   6483 C CE1 . PHE D 1 301 ? 51.489 28.291  49.099  1.00 73.57  ?  524 PHE A CE1 1 
ATOM   6484 C CE2 . PHE D 1 301 ? 52.245 26.310  50.197  1.00 75.10  ?  524 PHE A CE2 1 
ATOM   6485 C CZ  . PHE D 1 301 ? 52.500 27.393  49.381  1.00 69.87  ?  524 PHE A CZ  1 
ATOM   6486 N N   . TYR D 1 302 ? 45.177 25.978  50.418  1.00 66.28  ?  525 TYR A N   1 
ATOM   6487 C CA  . TYR D 1 302 ? 43.975 25.431  51.027  1.00 62.65  ?  525 TYR A CA  1 
ATOM   6488 C C   . TYR D 1 302 ? 43.957 23.918  50.853  1.00 60.83  ?  525 TYR A C   1 
ATOM   6489 O O   . TYR D 1 302 ? 44.153 23.402  49.749  1.00 61.76  ?  525 TYR A O   1 
ATOM   6490 C CB  . TYR D 1 302 ? 42.735 26.067  50.396  1.00 59.69  ?  525 TYR A CB  1 
ATOM   6491 C CG  . TYR D 1 302 ? 41.414 25.667  51.028  1.00 64.20  ?  525 TYR A CG  1 
ATOM   6492 C CD1 . TYR D 1 302 ? 40.828 24.436  50.754  1.00 61.04  ?  525 TYR A CD1 1 
ATOM   6493 C CD2 . TYR D 1 302 ? 40.750 26.528  51.893  1.00 64.68  ?  525 TYR A CD2 1 
ATOM   6494 C CE1 . TYR D 1 302 ? 39.627 24.072  51.327  1.00 57.61  ?  525 TYR A CE1 1 
ATOM   6495 C CE2 . TYR D 1 302 ? 39.547 26.172  52.470  1.00 62.08  ?  525 TYR A CE2 1 
ATOM   6496 C CZ  . TYR D 1 302 ? 38.990 24.943  52.183  1.00 60.38  ?  525 TYR A CZ  1 
ATOM   6497 O OH  . TYR D 1 302 ? 37.791 24.579  52.753  1.00 57.11  ?  525 TYR A OH  1 
ATOM   6498 N N   . THR D 1 303 ? 43.730 23.208  51.951  1.00 59.36  ?  526 THR A N   1 
ATOM   6499 C CA  . THR D 1 303 ? 43.653 21.755  51.937  1.00 61.33  ?  526 THR A CA  1 
ATOM   6500 C C   . THR D 1 303 ? 42.186 21.346  51.885  1.00 57.83  ?  526 THR A C   1 
ATOM   6501 O O   . THR D 1 303 ? 41.407 21.695  52.781  1.00 51.33  ?  526 THR A O   1 
ATOM   6502 C CB  . THR D 1 303 ? 44.344 21.152  53.160  1.00 59.12  ?  526 THR A CB  1 
ATOM   6503 O OG1 . THR D 1 303 ? 45.764 21.264  53.008  1.00 59.14  ?  526 THR A OG1 1 
ATOM   6504 C CG2 . THR D 1 303 ? 43.974 19.685  53.317  1.00 58.71  ?  526 THR A CG2 1 
ATOM   6505 N N   . LEU D 1 304 ? 41.810 20.630  50.829  1.00 56.25  ?  527 LEU A N   1 
ATOM   6506 C CA  . LEU D 1 304 ? 40.444 20.156  50.688  1.00 49.24  ?  527 LEU A CA  1 
ATOM   6507 C C   . LEU D 1 304 ? 40.187 18.979  51.622  1.00 50.77  ?  527 LEU A C   1 
ATOM   6508 O O   . LEU D 1 304 ? 41.105 18.262  52.032  1.00 46.68  ?  527 LEU A O   1 
ATOM   6509 C CB  . LEU D 1 304 ? 40.160 19.734  49.245  1.00 48.38  ?  527 LEU A CB  1 
ATOM   6510 C CG  . LEU D 1 304 ? 40.542 20.700  48.125  1.00 46.38  ?  527 LEU A CG  1 
ATOM   6511 C CD1 . LEU D 1 304 ? 40.847 19.934  46.846  1.00 48.05  ?  527 LEU A CD1 1 
ATOM   6512 C CD2 . LEU D 1 304 ? 39.430 21.703  47.894  1.00 44.38  ?  527 LEU A CD2 1 
ATOM   6513 N N   . ALA D 1 305 ? 38.918 18.788  51.959  1.00 48.47  ?  528 ALA A N   1 
ATOM   6514 C CA  . ALA D 1 305 ? 38.525 17.594  52.683  1.00 44.98  ?  528 ALA A CA  1 
ATOM   6515 C C   . ALA D 1 305 ? 38.823 16.364  51.827  1.00 56.17  ?  528 ALA A C   1 
ATOM   6516 O O   . ALA D 1 305 ? 38.533 16.362  50.625  1.00 53.24  ?  528 ALA A O   1 
ATOM   6517 C CB  . ALA D 1 305 ? 37.040 17.647  53.044  1.00 45.86  ?  528 ALA A CB  1 
ATOM   6518 N N   . PRO D 1 306 ? 39.403 15.307  52.403  1.00 53.73  ?  529 PRO A N   1 
ATOM   6519 C CA  . PRO D 1 306 ? 39.801 14.154  51.585  1.00 56.28  ?  529 PRO A CA  1 
ATOM   6520 C C   . PRO D 1 306 ? 38.604 13.325  51.154  1.00 62.23  ?  529 PRO A C   1 
ATOM   6521 O O   . PRO D 1 306 ? 38.075 12.526  51.936  1.00 72.82  ?  529 PRO A O   1 
ATOM   6522 C CB  . PRO D 1 306 ? 40.733 13.372  52.518  1.00 58.12  ?  529 PRO A CB  1 
ATOM   6523 C CG  . PRO D 1 306 ? 40.344 13.791  53.919  1.00 55.42  ?  529 PRO A CG  1 
ATOM   6524 C CD  . PRO D 1 306 ? 39.446 15.003  53.843  1.00 54.14  ?  529 PRO A CD  1 
ATOM   6525 N N   . MET D 1 307 ? 38.182 13.493  49.902  1.00 60.90  ?  530 MET A N   1 
ATOM   6526 C CA  . MET D 1 307 ? 36.898 12.953  49.484  1.00 67.95  ?  530 MET A CA  1 
ATOM   6527 C C   . MET D 1 307 ? 36.776 13.061  47.970  1.00 68.26  ?  530 MET A C   1 
ATOM   6528 O O   . MET D 1 307 ? 37.367 13.954  47.353  1.00 65.10  ?  530 MET A O   1 
ATOM   6529 C CB  . MET D 1 307 ? 35.762 13.705  50.187  1.00 70.77  ?  530 MET A CB  1 
ATOM   6530 C CG  . MET D 1 307 ? 34.381 13.122  50.032  1.00 74.35  ?  530 MET A CG  1 
ATOM   6531 S SD  . MET D 1 307 ? 33.189 14.208  50.836  1.00 99.57  ?  530 MET A SD  1 
ATOM   6532 C CE  . MET D 1 307 ? 33.314 13.673  52.536  1.00 72.26  ?  530 MET A CE  1 
ATOM   6533 N N   . GLY D 1 308 ? 36.019 12.139  47.384  1.00 70.16  ?  531 GLY A N   1 
ATOM   6534 C CA  . GLY D 1 308 ? 35.763 12.152  45.955  1.00 60.39  ?  531 GLY A CA  1 
ATOM   6535 C C   . GLY D 1 308 ? 36.975 11.834  45.103  1.00 54.70  ?  531 GLY A C   1 
ATOM   6536 O O   . GLY D 1 308 ? 37.389 12.645  44.275  1.00 55.41  ?  531 GLY A O   1 
HETATM 6537 C C1  . EDO E 3 .   ? 26.748 40.191  0.325   1.00 41.83  ?  201 EDO C C1  1 
HETATM 6538 O O1  . EDO E 3 .   ? 25.619 39.556  0.936   1.00 54.13  ?  201 EDO C O1  1 
HETATM 6539 C C2  . EDO E 3 .   ? 27.000 41.532  0.998   1.00 37.14  ?  201 EDO C C2  1 
HETATM 6540 O O2  . EDO E 3 .   ? 28.199 42.113  0.482   1.00 38.22  ?  201 EDO C O2  1 
HETATM 6541 C C1  . EDO F 3 .   ? 33.036 45.708  -22.191 1.00 38.43  ?  202 EDO C C1  1 
HETATM 6542 O O1  . EDO F 3 .   ? 32.311 46.729  -21.497 1.00 45.15  ?  202 EDO C O1  1 
HETATM 6543 C C2  . EDO F 3 .   ? 32.143 45.121  -23.273 1.00 44.57  ?  202 EDO C C2  1 
HETATM 6544 O O2  . EDO F 3 .   ? 32.951 44.474  -24.262 1.00 53.19  ?  202 EDO C O2  1 
HETATM 6545 C C1  . EDO G 3 .   ? 27.960 4.880   8.546   1.00 43.41  ?  601 EDO A C1  1 
HETATM 6546 O O1  . EDO G 3 .   ? 27.650 3.756   9.378   1.00 55.50  ?  601 EDO A O1  1 
HETATM 6547 C C2  . EDO G 3 .   ? 26.686 5.405   7.895   1.00 40.45  ?  601 EDO A C2  1 
HETATM 6548 O O2  . EDO G 3 .   ? 26.990 5.955   6.607   1.00 50.84  ?  601 EDO A O2  1 
HETATM 6549 O O   . HOH H 4 .   ? 0.495  9.169   20.073  1.00 57.24  ?  601 HOH B O   1 
HETATM 6550 O O   . HOH H 4 .   ? 10.078 20.632  6.358   1.00 30.00  ?  602 HOH B O   1 
HETATM 6551 O O   . HOH H 4 .   ? 0.468  9.544   23.188  1.00 52.25  ?  603 HOH B O   1 
HETATM 6552 O O   . HOH H 4 .   ? 12.660 39.354  37.022  1.00 53.72  ?  604 HOH B O   1 
HETATM 6553 O O   . HOH H 4 .   ? 20.861 35.796  10.327  1.00 40.72  ?  605 HOH B O   1 
HETATM 6554 O O   . HOH H 4 .   ? 10.915 32.274  18.209  1.00 30.00  ?  606 HOH B O   1 
HETATM 6555 O O   . HOH H 4 .   ? 15.179 10.787  20.637  1.00 42.78  ?  607 HOH B O   1 
HETATM 6556 O O   . HOH H 4 .   ? 9.484  24.586  6.614   1.00 30.00  ?  608 HOH B O   1 
HETATM 6557 O O   . HOH H 4 .   ? 36.570 -1.865  23.842  1.00 30.00  ?  609 HOH B O   1 
HETATM 6558 O O   . HOH H 4 .   ? 11.644 25.239  19.347  1.00 39.63  ?  610 HOH B O   1 
HETATM 6559 O O   . HOH H 4 .   ? 20.503 5.379   38.715  1.00 44.91  ?  611 HOH B O   1 
HETATM 6560 O O   . HOH H 4 .   ? 3.783  6.763   14.634  1.00 50.51  ?  612 HOH B O   1 
HETATM 6561 O O   . HOH H 4 .   ? 20.729 -5.117  22.095  1.00 34.55  ?  613 HOH B O   1 
HETATM 6562 O O   . HOH H 4 .   ? 29.835 39.704  20.291  1.00 30.00  ?  614 HOH B O   1 
HETATM 6563 O O   . HOH H 4 .   ? 25.463 5.920   17.536  1.00 36.66  ?  615 HOH B O   1 
HETATM 6564 O O   . HOH H 4 .   ? 15.521 21.252  22.881  1.00 37.73  ?  616 HOH B O   1 
HETATM 6565 O O   . HOH H 4 .   ? 8.408  27.595  24.223  1.00 40.35  ?  617 HOH B O   1 
HETATM 6566 O O   . HOH H 4 .   ? 13.640 0.841   29.399  1.00 30.00  ?  618 HOH B O   1 
HETATM 6567 O O   . HOH H 4 .   ? 24.788 16.526  14.159  1.00 33.86  ?  619 HOH B O   1 
HETATM 6568 O O   . HOH H 4 .   ? 1.752  22.076  9.951   1.00 30.00  ?  620 HOH B O   1 
HETATM 6569 O O   . HOH H 4 .   ? 8.690  20.069  3.224   1.00 45.32  ?  621 HOH B O   1 
HETATM 6570 O O   . HOH H 4 .   ? 24.385 14.046  18.433  1.00 30.00  ?  622 HOH B O   1 
HETATM 6571 O O   . HOH H 4 .   ? 2.000  11.748  23.226  1.00 49.15  ?  623 HOH B O   1 
HETATM 6572 O O   . HOH H 4 .   ? 26.396 34.930  14.367  1.00 47.70  ?  624 HOH B O   1 
HETATM 6573 O O   . HOH H 4 .   ? 27.139 36.908  9.795   1.00 30.00  ?  625 HOH B O   1 
HETATM 6574 O O   . HOH H 4 .   ? 27.636 10.130  18.784  1.00 34.97  ?  626 HOH B O   1 
HETATM 6575 O O   . HOH H 4 .   ? 12.356 12.881  5.296   1.00 30.00  ?  627 HOH B O   1 
HETATM 6576 O O   . HOH H 4 .   ? 4.887  34.178  11.628  1.00 45.62  ?  628 HOH B O   1 
HETATM 6577 O O   . HOH H 4 .   ? 12.286 -14.448 14.787  1.00 45.24  ?  629 HOH B O   1 
HETATM 6578 O O   . HOH H 4 .   ? 0.635  27.913  14.702  1.00 48.00  ?  630 HOH B O   1 
HETATM 6579 O O   . HOH H 4 .   ? 15.265 18.808  23.583  1.00 38.19  ?  631 HOH B O   1 
HETATM 6580 O O   . HOH H 4 .   ? 13.767 41.387  35.406  1.00 50.02  ?  632 HOH B O   1 
HETATM 6581 O O   . HOH H 4 .   ? 12.120 -7.022  12.586  1.00 42.81  ?  633 HOH B O   1 
HETATM 6582 O O   . HOH H 4 .   ? 6.017  20.993  7.521   1.00 45.51  ?  634 HOH B O   1 
HETATM 6583 O O   . HOH H 4 .   ? 17.933 17.335  30.480  1.00 38.52  ?  635 HOH B O   1 
HETATM 6584 O O   . HOH H 4 .   ? 10.273 3.935   14.022  1.00 50.91  ?  636 HOH B O   1 
HETATM 6585 O O   . HOH H 4 .   ? 17.134 34.591  32.588  1.00 40.88  ?  637 HOH B O   1 
HETATM 6586 O O   . HOH H 4 .   ? 16.582 -10.689 18.309  1.00 30.00  ?  638 HOH B O   1 
HETATM 6587 O O   . HOH H 4 .   ? 3.228  27.183  27.408  1.00 30.00  ?  639 HOH B O   1 
HETATM 6588 O O   . HOH I 4 .   ? 33.949 31.872  -13.224 1.00 46.16  ?  301 HOH C O   1 
HETATM 6589 O O   . HOH I 4 .   ? 26.156 37.219  1.754   1.00 30.00  ?  302 HOH C O   1 
HETATM 6590 O O   . HOH I 4 .   ? 39.516 49.850  -10.292 1.00 47.81  ?  303 HOH C O   1 
HETATM 6591 O O   . HOH I 4 .   ? 21.703 48.281  -12.880 1.00 42.79  ?  304 HOH C O   1 
HETATM 6592 O O   . HOH I 4 .   ? 25.439 35.017  -13.053 1.00 49.24  ?  305 HOH C O   1 
HETATM 6593 O O   . HOH I 4 .   ? 32.661 37.186  4.406   1.00 41.16  ?  306 HOH C O   1 
HETATM 6594 O O   . HOH I 4 .   ? 40.586 47.616  -13.784 1.00 47.97  ?  307 HOH C O   1 
HETATM 6595 O O   . HOH I 4 .   ? 38.796 29.313  -9.807  1.00 30.00  ?  308 HOH C O   1 
HETATM 6596 O O   . HOH I 4 .   ? 25.209 39.725  -18.599 1.00 47.63  ?  309 HOH C O   1 
HETATM 6597 O O   . HOH I 4 .   ? 43.263 41.008  -32.693 1.00 30.00  ?  310 HOH C O   1 
HETATM 6598 O O   . HOH I 4 .   ? 21.224 28.215  -8.454  1.00 61.72  ?  311 HOH C O   1 
HETATM 6599 O O   . HOH J 4 .   ? 22.546 8.236   62.703  1.00 68.06  ?  201 HOH D O   1 
HETATM 6600 O O   . HOH K 4 .   ? 29.671 10.609  38.630  1.00 38.16  ?  701 HOH A O   1 
HETATM 6601 O O   . HOH K 4 .   ? 24.979 15.787  38.936  1.00 42.56  ?  702 HOH A O   1 
HETATM 6602 O O   . HOH K 4 .   ? 46.259 24.430  45.387  1.00 56.11  ?  703 HOH A O   1 
HETATM 6603 O O   . HOH K 4 .   ? 17.027 19.543  -1.602  1.00 37.89  ?  704 HOH A O   1 
HETATM 6604 O O   . HOH K 4 .   ? 25.891 18.284  4.257   1.00 39.45  ?  705 HOH A O   1 
HETATM 6605 O O   . HOH K 4 .   ? 51.703 17.631  24.324  1.00 30.00  ?  706 HOH A O   1 
HETATM 6606 O O   . HOH K 4 .   ? 23.820 17.526  2.589   1.00 35.00  ?  707 HOH A O   1 
HETATM 6607 O O   . HOH K 4 .   ? 49.751 8.684   36.222  1.00 53.74  ?  708 HOH A O   1 
HETATM 6608 O O   . HOH K 4 .   ? 49.972 11.570  26.910  1.00 30.00  ?  709 HOH A O   1 
HETATM 6609 O O   . HOH K 4 .   ? 49.330 14.281  11.179  1.00 48.95  ?  710 HOH A O   1 
HETATM 6610 O O   . HOH K 4 .   ? 38.248 16.660  47.652  1.00 41.44  ?  711 HOH A O   1 
HETATM 6611 O O   . HOH K 4 .   ? 27.054 20.226  2.887   1.00 38.36  ?  712 HOH A O   1 
HETATM 6612 O O   . HOH K 4 .   ? 38.404 16.932  20.809  1.00 33.50  ?  713 HOH A O   1 
HETATM 6613 O O   . HOH K 4 .   ? 42.375 7.229   29.081  1.00 46.48  ?  714 HOH A O   1 
HETATM 6614 O O   . HOH K 4 .   ? 27.794 15.080  7.899   1.00 33.63  ?  715 HOH A O   1 
HETATM 6615 O O   . HOH K 4 .   ? 39.236 19.448  35.541  1.00 30.00  ?  716 HOH A O   1 
HETATM 6616 O O   . HOH K 4 .   ? 42.421 20.345  18.828  1.00 34.77  ?  717 HOH A O   1 
HETATM 6617 O O   . HOH K 4 .   ? 48.764 13.693  13.788  1.00 42.33  ?  718 HOH A O   1 
HETATM 6618 O O   . HOH K 4 .   ? 49.610 23.765  15.451  1.00 46.09  ?  719 HOH A O   1 
HETATM 6619 O O   . HOH K 4 .   ? 36.397 24.865  1.098   1.00 42.85  ?  720 HOH A O   1 
HETATM 6620 O O   . HOH K 4 .   ? 44.066 3.470   24.310  1.00 30.00  ?  721 HOH A O   1 
HETATM 6621 O O   . HOH K 4 .   ? 22.117 13.144  49.659  1.00 49.39  ?  722 HOH A O   1 
HETATM 6622 O O   . HOH K 4 .   ? 42.682 6.968   25.123  1.00 30.00  ?  723 HOH A O   1 
HETATM 6623 O O   . HOH K 4 .   ? 51.841 20.261  13.867  1.00 54.43  ?  724 HOH A O   1 
HETATM 6624 O O   . HOH K 4 .   ? 48.550 15.571  34.811  1.00 49.38  ?  725 HOH A O   1 
HETATM 6625 O O   . HOH K 4 .   ? 36.259 20.400  -4.491  1.00 38.92  ?  726 HOH A O   1 
HETATM 6626 O O   . HOH K 4 .   ? 51.532 23.559  13.390  1.00 47.41  ?  727 HOH A O   1 
HETATM 6627 O O   . HOH K 4 .   ? 44.965 28.183  37.626  1.00 50.16  ?  728 HOH A O   1 
HETATM 6628 O O   . HOH K 4 .   ? 41.766 25.075  30.715  1.00 38.27  ?  729 HOH A O   1 
HETATM 6629 O O   . HOH K 4 .   ? 27.566 12.621  18.696  1.00 33.81  ?  730 HOH A O   1 
HETATM 6630 O O   . HOH K 4 .   ? 33.315 33.908  34.397  1.00 30.00  ?  731 HOH A O   1 
HETATM 6631 O O   . HOH K 4 .   ? 38.985 19.881  28.499  1.00 38.38  ?  732 HOH A O   1 
HETATM 6632 O O   . HOH K 4 .   ? 26.915 22.229  38.385  1.00 30.00  ?  733 HOH A O   1 
HETATM 6633 O O   . HOH K 4 .   ? 28.205 28.662  41.665  1.00 39.44  ?  734 HOH A O   1 
HETATM 6634 O O   . HOH K 4 .   ? 22.949 7.935   42.229  1.00 30.00  ?  735 HOH A O   1 
HETATM 6635 O O   . HOH K 4 .   ? 35.533 22.723  23.645  1.00 31.61  ?  736 HOH A O   1 
HETATM 6636 O O   . HOH K 4 .   ? 35.803 22.875  9.105   1.00 33.58  ?  737 HOH A O   1 
HETATM 6637 O O   . HOH K 4 .   ? 22.546 21.499  2.534   1.00 43.94  ?  738 HOH A O   1 
HETATM 6638 O O   . HOH K 4 .   ? 27.171 10.474  37.166  1.00 43.04  ?  739 HOH A O   1 
HETATM 6639 O O   . HOH K 4 .   ? 38.529 27.743  2.712   1.00 47.71  ?  740 HOH A O   1 
HETATM 6640 O O   . HOH K 4 .   ? 24.749 30.303  38.352  1.00 49.71  ?  741 HOH A O   1 
HETATM 6641 O O   . HOH K 4 .   ? 31.338 32.964  36.057  1.00 43.83  ?  742 HOH A O   1 
HETATM 6642 O O   . HOH K 4 .   ? 24.886 11.303  37.101  1.00 43.01  ?  743 HOH A O   1 
HETATM 6643 O O   . HOH K 4 .   ? 36.039 23.414  20.943  1.00 34.15  ?  744 HOH A O   1 
HETATM 6644 O O   . HOH K 4 .   ? 28.183 16.782  15.886  1.00 36.65  ?  745 HOH A O   1 
HETATM 6645 O O   . HOH K 4 .   ? 47.306 15.530  25.746  1.00 50.37  ?  746 HOH A O   1 
HETATM 6646 O O   . HOH K 4 .   ? 43.570 12.947  7.579   1.00 50.22  ?  747 HOH A O   1 
HETATM 6647 O O   . HOH K 4 .   ? 33.202 42.312  41.165  1.00 30.00  ?  748 HOH A O   1 
HETATM 6648 O O   . HOH K 4 .   ? 19.691 21.449  37.191  1.00 49.59  ?  749 HOH A O   1 
HETATM 6649 O O   . HOH K 4 .   ? 43.920 -7.934  23.635  1.00 54.39  ?  750 HOH A O   1 
HETATM 6650 O O   . HOH K 4 .   ? 24.514 33.196  -5.045  1.00 30.00  ?  751 HOH A O   1 
HETATM 6651 O O   . HOH K 4 .   ? 23.760 13.871  36.960  1.00 41.24  ?  752 HOH A O   1 
HETATM 6652 O O   . HOH K 4 .   ? 46.494 8.261   25.596  1.00 44.08  ?  753 HOH A O   1 
HETATM 6653 O O   . HOH K 4 .   ? 26.641 31.219  46.209  1.00 48.81  ?  754 HOH A O   1 
HETATM 6654 O O   . HOH K 4 .   ? 40.408 29.747  20.991  1.00 44.12  ?  755 HOH A O   1 
HETATM 6655 O O   . HOH K 4 .   ? 17.742 18.727  38.368  1.00 60.33  ?  756 HOH A O   1 
HETATM 6656 O O   . HOH K 4 .   ? 19.803 20.708  40.266  1.00 52.07  ?  757 HOH A O   1 
HETATM 6657 O O   . HOH K 4 .   ? 38.551 33.241  17.490  1.00 30.00  ?  758 HOH A O   1 
HETATM 6658 O O   . HOH K 4 .   ? 37.366 1.269   27.142  1.00 46.99  ?  759 HOH A O   1 
HETATM 6659 O O   . HOH K 4 .   ? 35.790 -1.259  26.206  1.00 43.41  ?  760 HOH A O   1 
HETATM 6660 O O   . HOH K 4 .   ? 38.163 41.059  41.282  1.00 30.00  ?  761 HOH A O   1 
HETATM 6661 O O   . HOH K 4 .   ? 37.632 23.012  10.603  1.00 40.50  ?  762 HOH A O   1 
# 
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   THR 1   224 224 THR THR B . n 
A 1 2   LYS 2   225 225 LYS LYS B . n 
A 1 3   PRO 3   226 226 PRO PRO B . n 
A 1 4   PHE 4   227 227 PHE PHE B . n 
A 1 5   SER 5   228 228 SER SER B . n 
A 1 6   VAL 6   229 229 VAL VAL B . n 
A 1 7   PRO 7   230 230 PRO PRO B . n 
A 1 8   VAL 8   231 231 VAL VAL B . n 
A 1 9   LEU 9   232 232 LEU LEU B . n 
A 1 10  THR 10  233 233 THR THR B . n 
A 1 11  VAL 11  234 234 VAL VAL B . n 
A 1 12  GLU 12  235 235 GLU GLU B . n 
A 1 13  GLU 13  236 236 GLU GLU B . n 
A 1 14  MET 14  237 237 MET MET B . n 
A 1 15  THR 15  238 238 THR THR B . n 
A 1 16  ASN 16  239 239 ASN ASN B . n 
A 1 17  SER 17  240 240 SER SER B . n 
A 1 18  ARG 18  241 241 ARG ARG B . n 
A 1 19  PHE 19  242 242 PHE PHE B . n 
A 1 20  PRO 20  243 243 PRO PRO B . n 
A 1 21  ILE 21  244 244 ILE ILE B . n 
A 1 22  PRO 22  245 245 PRO PRO B . n 
A 1 23  LEU 23  246 246 LEU LEU B . n 
A 1 24  GLU 24  247 247 GLU GLU B . n 
A 1 25  LYS 25  248 248 LYS LYS B . n 
A 1 26  LEU 26  249 249 LEU LEU B . n 
A 1 27  PHE 27  250 250 PHE PHE B . n 
A 1 28  THR 28  251 251 THR THR B . n 
A 1 29  GLY 29  252 252 GLY GLY B . n 
A 1 30  PRO 30  253 253 PRO PRO B . n 
A 1 31  SER 31  254 254 SER SER B . n 
A 1 32  SER 32  255 255 SER SER B . n 
A 1 33  ALA 33  256 256 ALA ALA B . n 
A 1 34  PHE 34  257 257 PHE PHE B . n 
A 1 35  VAL 35  258 258 VAL VAL B . n 
A 1 36  VAL 36  259 259 VAL VAL B . n 
A 1 37  GLN 37  260 260 GLN GLN B . n 
A 1 38  PRO 38  261 261 PRO PRO B . n 
A 1 39  GLN 39  262 262 GLN GLN B . n 
A 1 40  ASN 40  263 263 ASN ASN B . n 
A 1 41  GLY 41  264 264 GLY GLY B . n 
A 1 42  ARG 42  265 265 ARG ARG B . n 
A 1 43  CYS 43  266 266 CYS CYS B . n 
A 1 44  THR 44  267 267 THR THR B . n 
A 1 45  THR 45  268 268 THR THR B . n 
A 1 46  ASP 46  269 269 ASP ASP B . n 
A 1 47  GLY 47  270 270 GLY GLY B . n 
A 1 48  VAL 48  271 271 VAL VAL B . n 
A 1 49  LEU 49  272 272 LEU LEU B . n 
A 1 50  LEU 50  273 273 LEU LEU B . n 
A 1 51  GLY 51  274 274 GLY GLY B . n 
A 1 52  THR 52  275 275 THR THR B . n 
A 1 53  THR 53  276 276 THR THR B . n 
A 1 54  GLN 54  277 277 GLN GLN B . n 
A 1 55  LEU 55  278 278 LEU LEU B . n 
A 1 56  SER 56  279 279 SER SER B . n 
A 1 57  PRO 57  280 280 PRO PRO B . n 
A 1 58  VAL 58  281 281 VAL VAL B . n 
A 1 59  ASN 59  282 282 ASN ASN B . n 
A 1 60  ILE 60  283 283 ILE ILE B . n 
A 1 61  CYS 61  284 284 CYS CYS B . n 
A 1 62  THR 62  285 285 THR THR B . n 
A 1 63  PHE 63  286 286 PHE PHE B . n 
A 1 64  ARG 64  287 287 ARG ARG B . n 
A 1 65  GLY 65  288 288 GLY GLY B . n 
A 1 66  ASP 66  289 289 ASP ASP B . n 
A 1 67  VAL 67  290 290 VAL VAL B . n 
A 1 68  THR 68  291 291 THR THR B . n 
A 1 69  HIS 69  292 292 HIS HIS B . n 
A 1 70  ILE 70  293 293 ILE ILE B . n 
A 1 71  THR 71  294 294 THR THR B . n 
A 1 72  GLY 72  295 295 GLY GLY B . n 
A 1 73  SER 73  296 296 SER SER B . n 
A 1 74  ARG 74  297 297 ARG ARG B . n 
A 1 75  ASN 75  298 298 ASN ASN B . n 
A 1 76  TYR 76  299 299 TYR TYR B . n 
A 1 77  THR 77  300 300 THR THR B . n 
A 1 78  MET 78  301 301 MET MET B . n 
A 1 79  ASN 79  302 302 ASN ASN B . n 
A 1 80  LEU 80  303 303 LEU LEU B . n 
A 1 81  ALA 81  304 304 ALA ALA B . n 
A 1 82  SER 82  305 305 SER SER B . n 
A 1 83  GLN 83  306 306 GLN GLN B . n 
A 1 84  ASN 84  307 307 ASN ASN B . n 
A 1 85  TRP 85  308 308 TRP TRP B . n 
A 1 86  ASN 86  309 309 ASN ASN B . n 
A 1 87  ASP 87  310 310 ASP ASP B . n 
A 1 88  TYR 88  311 311 TYR TYR B . n 
A 1 89  ASP 89  312 312 ASP ASP B . n 
A 1 90  PRO 90  313 313 PRO PRO B . n 
A 1 91  THR 91  314 314 THR THR B . n 
A 1 92  GLU 92  315 315 GLU GLU B . n 
A 1 93  GLU 93  316 316 GLU GLU B . n 
A 1 94  ILE 94  317 317 ILE ILE B . n 
A 1 95  PRO 95  318 318 PRO PRO B . n 
A 1 96  ALA 96  319 319 ALA ALA B . n 
A 1 97  PRO 97  320 320 PRO PRO B . n 
A 1 98  LEU 98  321 321 LEU LEU B . n 
A 1 99  GLY 99  322 322 GLY GLY B . n 
A 1 100 THR 100 323 323 THR THR B . n 
A 1 101 PRO 101 324 324 PRO PRO B . n 
A 1 102 ASP 102 325 325 ASP ASP B . n 
A 1 103 PHE 103 326 326 PHE PHE B . n 
A 1 104 VAL 104 327 327 VAL VAL B . n 
A 1 105 GLY 105 328 328 GLY GLY B . n 
A 1 106 LYS 106 329 329 LYS LYS B . n 
A 1 107 ILE 107 330 330 ILE ILE B . n 
A 1 108 GLN 108 331 331 GLN GLN B . n 
A 1 109 GLY 109 332 332 GLY GLY B . n 
A 1 110 VAL 110 333 333 VAL VAL B . n 
A 1 111 LEU 111 334 334 LEU LEU B . n 
A 1 112 THR 112 335 335 THR THR B . n 
A 1 113 GLN 113 336 336 GLN GLN B . n 
A 1 114 THR 114 337 337 THR THR B . n 
A 1 115 THR 115 338 338 THR THR B . n 
A 1 116 ARG 116 339 339 ARG ARG B . n 
A 1 117 THR 117 340 340 THR THR B . n 
A 1 118 ASP 118 341 341 ASP ASP B . n 
A 1 119 GLY 119 342 342 GLY GLY B . n 
A 1 120 SER 120 343 343 SER SER B . n 
A 1 121 THR 121 344 344 THR THR B . n 
A 1 122 ARG 122 345 345 ARG ARG B . n 
A 1 123 GLY 123 346 346 GLY GLY B . n 
A 1 124 HIS 124 347 347 HIS HIS B . n 
A 1 125 LYS 125 348 348 LYS LYS B . n 
A 1 126 ALA 126 349 349 ALA ALA B . n 
A 1 127 THR 127 350 350 THR THR B . n 
A 1 128 VAL 128 351 351 VAL VAL B . n 
A 1 129 TYR 129 352 352 TYR TYR B . n 
A 1 130 THR 130 353 353 THR THR B . n 
A 1 131 GLY 131 354 354 GLY GLY B . n 
A 1 132 SER 132 355 355 SER SER B . n 
A 1 133 ALA 133 356 356 ALA ALA B . n 
A 1 134 ASP 134 357 357 ASP ASP B . n 
A 1 135 PHE 135 358 358 PHE PHE B . n 
A 1 136 ALA 136 359 359 ALA ALA B . n 
A 1 137 PRO 137 360 360 PRO PRO B . n 
A 1 138 LYS 138 361 361 LYS LYS B . n 
A 1 139 LEU 139 362 362 LEU LEU B . n 
A 1 140 GLY 140 363 363 GLY GLY B . n 
A 1 141 ARG 141 364 364 ARG ARG B . n 
A 1 142 VAL 142 365 365 VAL VAL B . n 
A 1 143 GLN 143 366 366 GLN GLN B . n 
A 1 144 PHE 144 367 367 PHE PHE B . n 
A 1 145 GLU 145 368 368 GLU GLU B . n 
A 1 146 THR 146 369 369 THR THR B . n 
A 1 147 ASP 147 370 370 ASP ASP B . n 
A 1 148 THR 148 371 371 THR THR B . n 
A 1 149 ASP 149 372 372 ASP ASP B . n 
A 1 150 ARG 150 373 373 ARG ARG B . n 
A 1 151 ASP 151 374 374 ASP ASP B . n 
A 1 152 PHE 152 375 375 PHE PHE B . n 
A 1 153 GLU 153 376 376 GLU GLU B . n 
A 1 154 ALA 154 377 377 ALA ALA B . n 
A 1 155 ASN 155 378 378 ASN ASN B . n 
A 1 156 GLN 156 379 379 GLN GLN B . n 
A 1 157 ASN 157 380 380 ASN ASN B . n 
A 1 158 THR 158 381 381 THR THR B . n 
A 1 159 LYS 159 382 382 LYS LYS B . n 
A 1 160 PHE 160 383 383 PHE PHE B . n 
A 1 161 THR 161 384 384 THR THR B . n 
A 1 162 PRO 162 385 385 PRO PRO B . n 
A 1 163 VAL 163 386 386 VAL VAL B . n 
A 1 164 GLY 164 387 387 GLY GLY B . n 
A 1 165 VAL 165 388 388 VAL VAL B . n 
A 1 166 ILE 166 389 389 ILE ILE B . n 
A 1 167 GLN 167 390 390 GLN GLN B . n 
A 1 168 ASP 168 391 391 ASP ASP B . n 
A 1 169 GLY 169 392 392 GLY GLY B . n 
A 1 170 GLY 170 393 393 GLY GLY B . n 
A 1 171 THR 171 394 394 THR THR B . n 
A 1 172 THR 172 395 395 THR THR B . n 
A 1 173 HIS 173 396 396 HIS HIS B . n 
A 1 174 ARG 174 397 397 ARG ARG B . n 
A 1 175 ASN 175 398 398 ASN ASN B . n 
A 1 176 GLU 176 399 399 GLU GLU B . n 
A 1 177 PRO 177 400 400 PRO PRO B . n 
A 1 178 GLN 178 401 401 GLN GLN B . n 
A 1 179 GLN 179 402 402 GLN GLN B . n 
A 1 180 TRP 180 403 403 TRP TRP B . n 
A 1 181 VAL 181 404 404 VAL VAL B . n 
A 1 182 LEU 182 405 405 LEU LEU B . n 
A 1 183 PRO 183 406 406 PRO PRO B . n 
A 1 184 SER 184 407 407 SER SER B . n 
A 1 185 TYR 185 408 408 TYR TYR B . n 
A 1 186 SER 186 409 409 SER SER B . n 
A 1 187 GLY 187 410 410 GLY GLY B . n 
A 1 188 ARG 188 411 411 ARG ARG B . n 
A 1 189 ASN 189 412 412 ASN ASN B . n 
A 1 190 THR 190 413 413 THR THR B . n 
A 1 191 HIS 191 414 414 HIS HIS B . n 
A 1 192 ASN 192 415 415 ASN ASN B . n 
A 1 193 VAL 193 416 416 VAL VAL B . n 
A 1 194 HIS 194 417 417 HIS HIS B . n 
A 1 195 LEU 195 418 418 LEU LEU B . n 
A 1 196 ALA 196 419 419 ALA ALA B . n 
A 1 197 PRO 197 420 420 PRO PRO B . n 
A 1 198 ALA 198 421 421 ALA ALA B . n 
A 1 199 VAL 199 422 422 VAL VAL B . n 
A 1 200 ALA 200 423 423 ALA ALA B . n 
A 1 201 PRO 201 424 424 PRO PRO B . n 
A 1 202 THR 202 425 425 THR THR B . n 
A 1 203 PHE 203 426 426 PHE PHE B . n 
A 1 204 PRO 204 427 427 PRO PRO B . n 
A 1 205 GLY 205 428 428 GLY GLY B . n 
A 1 206 GLU 206 429 429 GLU GLU B . n 
A 1 207 GLN 207 430 430 GLN GLN B . n 
A 1 208 LEU 208 431 431 LEU LEU B . n 
A 1 209 LEU 209 432 432 LEU LEU B . n 
A 1 210 PHE 210 433 433 PHE PHE B . n 
A 1 211 PHE 211 434 434 PHE PHE B . n 
A 1 212 ARG 212 435 435 ARG ARG B . n 
A 1 213 SER 213 436 436 SER SER B . n 
A 1 214 THR 214 437 437 THR THR B . n 
A 1 215 MET 215 438 438 MET MET B . n 
A 1 216 PRO 216 439 439 PRO PRO B . n 
A 1 217 GLY 217 440 440 GLY GLY B . n 
A 1 218 CYS 218 441 441 CYS CYS B . n 
A 1 219 SER 219 442 442 SER SER B . n 
A 1 220 GLY 220 443 443 GLY GLY B . n 
A 1 221 TYR 221 444 444 TYR TYR B . n 
A 1 222 PRO 222 445 445 PRO PRO B . n 
A 1 223 ASN 223 446 446 ASN ASN B . n 
A 1 224 MET 224 447 447 MET MET B . n 
A 1 225 ASP 225 448 448 ASP ASP B . n 
A 1 226 LEU 226 449 449 LEU LEU B . n 
A 1 227 ASP 227 450 450 ASP ASP B . n 
A 1 228 CYS 228 451 451 CYS CYS B . n 
A 1 229 LEU 229 452 452 LEU LEU B . n 
A 1 230 LEU 230 453 453 LEU LEU B . n 
A 1 231 PRO 231 454 454 PRO PRO B . n 
A 1 232 GLN 232 455 455 GLN GLN B . n 
A 1 233 GLU 233 456 456 GLU GLU B . n 
A 1 234 TRP 234 457 457 TRP TRP B . n 
A 1 235 VAL 235 458 458 VAL VAL B . n 
A 1 236 GLN 236 459 459 GLN GLN B . n 
A 1 237 TYR 237 460 460 TYR TYR B . n 
A 1 238 PHE 238 461 461 PHE PHE B . n 
A 1 239 TYR 239 462 462 TYR TYR B . n 
A 1 240 GLN 240 463 463 GLN GLN B . n 
A 1 241 GLU 241 464 464 GLU GLU B . n 
A 1 242 ALA 242 465 465 ALA ALA B . n 
A 1 243 ALA 243 466 466 ALA ALA B . n 
A 1 244 PRO 244 467 467 PRO PRO B . n 
A 1 245 ALA 245 468 468 ALA ALA B . n 
A 1 246 GLN 246 469 469 GLN GLN B . n 
A 1 247 SER 247 470 470 SER SER B . n 
A 1 248 ASP 248 471 471 ASP ASP B . n 
A 1 249 VAL 249 472 472 VAL VAL B . n 
A 1 250 ALA 250 473 473 ALA ALA B . n 
A 1 251 LEU 251 474 474 LEU LEU B . n 
A 1 252 LEU 252 475 475 LEU LEU B . n 
A 1 253 ARG 253 476 476 ARG ARG B . n 
A 1 254 PHE 254 477 477 PHE PHE B . n 
A 1 255 VAL 255 478 478 VAL VAL B . n 
A 1 256 ASN 256 479 479 ASN ASN B . n 
A 1 257 PRO 257 480 480 PRO PRO B . n 
A 1 258 ASP 258 481 481 ASP ASP B . n 
A 1 259 THR 259 482 482 THR THR B . n 
A 1 260 GLY 260 483 483 GLY GLY B . n 
A 1 261 ARG 261 484 484 ARG ARG B . n 
A 1 262 VAL 262 485 485 VAL VAL B . n 
A 1 263 LEU 263 486 486 LEU LEU B . n 
A 1 264 PHE 264 487 487 PHE PHE B . n 
A 1 265 GLU 265 488 488 GLU GLU B . n 
A 1 266 CYS 266 489 489 CYS CYS B . n 
A 1 267 LYS 267 490 490 LYS LYS B . n 
A 1 268 LEU 268 491 491 LEU LEU B . n 
A 1 269 HIS 269 492 492 HIS HIS B . n 
A 1 270 LYS 270 493 493 LYS LYS B . n 
A 1 271 SER 271 494 494 SER SER B . n 
A 1 272 GLY 272 495 495 GLY GLY B . n 
A 1 273 TYR 273 496 496 TYR TYR B . n 
A 1 274 VAL 274 497 497 VAL VAL B . n 
A 1 275 THR 275 498 498 THR THR B . n 
A 1 276 VAL 276 499 499 VAL VAL B . n 
A 1 277 ALA 277 500 500 ALA ALA B . n 
A 1 278 HIS 278 501 501 HIS HIS B . n 
A 1 279 THR 279 502 502 THR THR B . n 
A 1 280 GLY 280 503 503 GLY GLY B . n 
A 1 281 GLN 281 504 504 GLN GLN B . n 
A 1 282 HIS 282 505 505 HIS HIS B . n 
A 1 283 ASP 283 506 506 ASP ASP B . n 
A 1 284 LEU 284 507 507 LEU LEU B . n 
A 1 285 VAL 285 508 508 VAL VAL B . n 
A 1 286 ILE 286 509 509 ILE ILE B . n 
A 1 287 PRO 287 510 510 PRO PRO B . n 
A 1 288 PRO 288 511 511 PRO PRO B . n 
A 1 289 ASN 289 512 512 ASN ASN B . n 
A 1 290 GLY 290 513 513 GLY GLY B . n 
A 1 291 TYR 291 514 514 TYR TYR B . n 
A 1 292 PHE 292 515 515 PHE PHE B . n 
A 1 293 ARG 293 516 516 ARG ARG B . n 
A 1 294 PHE 294 517 517 PHE PHE B . n 
A 1 295 ASP 295 518 518 ASP ASP B . n 
A 1 296 SER 296 519 519 SER SER B . n 
A 1 297 TRP 297 520 520 TRP TRP B . n 
A 1 298 VAL 298 521 521 VAL VAL B . n 
A 1 299 ASN 299 522 522 ASN ASN B . n 
A 1 300 GLN 300 523 523 GLN GLN B . n 
A 1 301 PHE 301 524 524 PHE PHE B . n 
A 1 302 TYR 302 525 525 TYR TYR B . n 
A 1 303 THR 303 526 526 THR THR B . n 
A 1 304 LEU 304 527 527 LEU LEU B . n 
A 1 305 ALA 305 528 528 ALA ALA B . n 
A 1 306 PRO 306 529 529 PRO PRO B . n 
A 1 307 MET 307 530 530 MET MET B . n 
A 1 308 GLY 308 531 531 GLY GLY B . n 
B 2 1   GLN 1   1   1   GLN GLN C . n 
B 2 2   VAL 2   2   2   VAL VAL C . n 
B 2 3   GLN 3   3   3   GLN GLN C . n 
B 2 4   LEU 4   4   4   LEU LEU C . n 
B 2 5   GLN 5   5   5   GLN GLN C . n 
B 2 6   GLU 6   6   6   GLU GLU C . n 
B 2 7   SER 7   7   7   SER SER C . n 
B 2 8   GLY 8   8   8   GLY GLY C . n 
B 2 9   GLY 9   9   9   GLY GLY C . n 
B 2 10  GLY 10  10  10  GLY GLY C . n 
B 2 11  LEU 11  11  11  LEU LEU C . n 
B 2 12  VAL 12  12  12  VAL VAL C . n 
B 2 13  GLN 13  13  13  GLN GLN C . n 
B 2 14  PRO 14  14  14  PRO PRO C . n 
B 2 15  GLY 15  15  15  GLY GLY C . n 
B 2 16  GLY 16  16  16  GLY GLY C . n 
B 2 17  SER 17  17  17  SER SER C . n 
B 2 18  LEU 18  18  18  LEU LEU C . n 
B 2 19  ARG 19  19  19  ARG ARG C . n 
B 2 20  LEU 20  20  20  LEU LEU C . n 
B 2 21  SER 21  21  21  SER SER C . n 
B 2 22  CYS 22  22  22  CYS CYS C . n 
B 2 23  ALA 23  23  23  ALA ALA C . n 
B 2 24  ALA 24  24  24  ALA ALA C . n 
B 2 25  SER 25  25  25  SER SER C . n 
B 2 26  GLY 26  26  26  GLY GLY C . n 
B 2 27  ASP 27  27  27  ASP ASP C . n 
B 2 28  ILE 28  28  28  ILE ILE C . n 
B 2 29  PHE 29  29  29  PHE PHE C . n 
B 2 30  SER 30  30  30  SER SER C . n 
B 2 31  ILE 31  31  31  ILE ILE C . n 
B 2 32  TYR 32  32  32  TYR TYR C . n 
B 2 33  LEU 33  33  33  LEU LEU C . n 
B 2 34  MET 34  34  34  MET MET C . n 
B 2 35  GLY 35  35  35  GLY GLY C . n 
B 2 36  TRP 36  36  36  TRP TRP C . n 
B 2 37  TYR 37  37  37  TYR TYR C . n 
B 2 38  ARG 38  38  38  ARG ARG C . n 
B 2 39  GLN 39  39  39  GLN GLN C . n 
B 2 40  SER 40  40  40  SER SER C . n 
B 2 41  PRO 41  41  41  PRO PRO C . n 
B 2 42  GLY 42  42  42  GLY GLY C . n 
B 2 43  LYS 43  43  43  LYS LYS C . n 
B 2 44  GLN 44  44  44  GLN GLN C . n 
B 2 45  ARG 45  45  45  ARG ARG C . n 
B 2 46  GLU 46  46  46  GLU GLU C . n 
B 2 47  LEU 47  47  47  LEU LEU C . n 
B 2 48  VAL 48  48  48  VAL VAL C . n 
B 2 49  ALA 49  49  49  ALA ALA C . n 
B 2 50  THR 50  50  50  THR THR C . n 
B 2 51  ILE 51  51  51  ILE ILE C . n 
B 2 52  THR 52  52  52  THR THR C . n 
B 2 53  SER 53  53  53  SER SER C . n 
B 2 54  SER 54  54  54  SER SER C . n 
B 2 55  GLY 55  55  55  GLY GLY C . n 
B 2 56  GLU 56  56  56  GLU GLU C . n 
B 2 57  THR 57  57  57  THR THR C . n 
B 2 58  LYS 58  58  58  LYS LYS C . n 
B 2 59  HIS 59  59  59  HIS HIS C . n 
B 2 60  VAL 60  60  60  VAL VAL C . n 
B 2 61  TYR 61  61  61  TYR TYR C . n 
B 2 62  SER 62  62  62  SER SER C . n 
B 2 63  VAL 63  63  63  VAL VAL C . n 
B 2 64  LYS 64  64  64  LYS LYS C . n 
B 2 65  GLY 65  65  65  GLY GLY C . n 
B 2 66  ARG 66  66  66  ARG ARG C . n 
B 2 67  PHE 67  67  67  PHE PHE C . n 
B 2 68  THR 68  68  68  THR THR C . n 
B 2 69  ILE 69  69  69  ILE ILE C . n 
B 2 70  SER 70  70  70  SER SER C . n 
B 2 71  ARG 71  71  71  ARG ARG C . n 
B 2 72  GLU 72  72  72  GLU GLU C . n 
B 2 73  ASN 73  73  73  ASN ASN C . n 
B 2 74  ALA 74  74  74  ALA ALA C . n 
B 2 75  LYS 75  75  75  LYS LYS C . n 
B 2 76  ASN 76  76  76  ASN ASN C . n 
B 2 77  ALA 77  77  77  ALA ALA C . n 
B 2 78  TRP 78  78  78  TRP TRP C . n 
B 2 79  TYR 79  79  79  TYR TYR C . n 
B 2 80  LEU 80  80  80  LEU LEU C . n 
B 2 81  GLN 81  81  81  GLN GLN C . n 
B 2 82  MET 82  82  82  MET MET C . n 
B 2 83  ASN 83  83  83  ASN ASN C . n 
B 2 84  SER 84  84  84  SER SER C . n 
B 2 85  LEU 85  85  85  LEU LEU C . n 
B 2 86  LYS 86  86  86  LYS LYS C . n 
B 2 87  PRO 87  87  87  PRO PRO C . n 
B 2 88  GLU 88  88  88  GLU GLU C . n 
B 2 89  ASP 89  89  89  ASP ASP C . n 
B 2 90  THR 90  90  90  THR THR C . n 
B 2 91  GLY 91  91  91  GLY GLY C . n 
B 2 92  VAL 92  92  92  VAL VAL C . n 
B 2 93  TYR 93  93  93  TYR TYR C . n 
B 2 94  TYR 94  94  94  TYR TYR C . n 
B 2 95  CYS 95  95  95  CYS CYS C . n 
B 2 96  HIS 96  96  96  HIS HIS C . n 
B 2 97  ALA 97  97  97  ALA ALA C . n 
B 2 98  VAL 98  98  98  VAL VAL C . n 
B 2 99  THR 99  99  99  THR THR C . n 
B 2 100 GLY 100 100 100 GLY GLY C . n 
B 2 101 VAL 101 101 101 VAL VAL C . n 
B 2 102 ILE 102 102 102 ILE ILE C . n 
B 2 103 ALA 103 103 103 ALA ALA C . n 
B 2 104 SER 104 104 104 SER SER C . n 
B 2 105 SER 105 105 105 SER SER C . n 
B 2 106 TRP 106 106 106 TRP TRP C . n 
B 2 107 GLY 107 107 107 GLY GLY C . n 
B 2 108 GLN 108 108 108 GLN GLN C . n 
B 2 109 GLY 109 109 109 GLY GLY C . n 
B 2 110 THR 110 110 110 THR THR C . n 
B 2 111 GLN 111 111 111 GLN GLN C . n 
B 2 112 VAL 112 112 112 VAL VAL C . n 
B 2 113 THR 113 113 113 THR THR C . n 
B 2 114 VAL 114 114 114 VAL VAL C . n 
B 2 115 SER 115 115 115 SER SER C . n 
B 2 116 SER 116 116 116 SER SER C . n 
B 2 117 HIS 117 117 117 HIS HIS C . n 
B 2 118 HIS 118 118 118 HIS HIS C . n 
B 2 119 HIS 119 119 ?   ?   ?   C . n 
B 2 120 HIS 120 120 ?   ?   ?   C . n 
B 2 121 HIS 121 121 ?   ?   ?   C . n 
B 2 122 HIS 122 122 ?   ?   ?   C . n 
C 2 1   GLN 1   1   1   GLN GLN D . n 
C 2 2   VAL 2   2   2   VAL VAL D . n 
C 2 3   GLN 3   3   3   GLN GLN D . n 
C 2 4   LEU 4   4   4   LEU LEU D . n 
C 2 5   GLN 5   5   5   GLN GLN D . n 
C 2 6   GLU 6   6   6   GLU GLU D . n 
C 2 7   SER 7   7   7   SER SER D . n 
C 2 8   GLY 8   8   8   GLY GLY D . n 
C 2 9   GLY 9   9   9   GLY GLY D . n 
C 2 10  GLY 10  10  10  GLY GLY D . n 
C 2 11  LEU 11  11  11  LEU LEU D . n 
C 2 12  VAL 12  12  12  VAL VAL D . n 
C 2 13  GLN 13  13  13  GLN GLN D . n 
C 2 14  PRO 14  14  14  PRO PRO D . n 
C 2 15  GLY 15  15  15  GLY GLY D . n 
C 2 16  GLY 16  16  16  GLY GLY D . n 
C 2 17  SER 17  17  17  SER SER D . n 
C 2 18  LEU 18  18  18  LEU LEU D . n 
C 2 19  ARG 19  19  19  ARG ARG D . n 
C 2 20  LEU 20  20  20  LEU LEU D . n 
C 2 21  SER 21  21  21  SER SER D . n 
C 2 22  CYS 22  22  22  CYS CYS D . n 
C 2 23  ALA 23  23  23  ALA ALA D . n 
C 2 24  ALA 24  24  24  ALA ALA D . n 
C 2 25  SER 25  25  25  SER SER D . n 
C 2 26  GLY 26  26  26  GLY GLY D . n 
C 2 27  ASP 27  27  27  ASP ASP D . n 
C 2 28  ILE 28  28  28  ILE ILE D . n 
C 2 29  PHE 29  29  29  PHE PHE D . n 
C 2 30  SER 30  30  30  SER SER D . n 
C 2 31  ILE 31  31  31  ILE ILE D . n 
C 2 32  TYR 32  32  32  TYR TYR D . n 
C 2 33  LEU 33  33  33  LEU LEU D . n 
C 2 34  MET 34  34  34  MET MET D . n 
C 2 35  GLY 35  35  35  GLY GLY D . n 
C 2 36  TRP 36  36  36  TRP TRP D . n 
C 2 37  TYR 37  37  37  TYR TYR D . n 
C 2 38  ARG 38  38  38  ARG ARG D . n 
C 2 39  GLN 39  39  39  GLN GLN D . n 
C 2 40  SER 40  40  40  SER SER D . n 
C 2 41  PRO 41  41  41  PRO PRO D . n 
C 2 42  GLY 42  42  42  GLY GLY D . n 
C 2 43  LYS 43  43  43  LYS LYS D . n 
C 2 44  GLN 44  44  44  GLN GLN D . n 
C 2 45  ARG 45  45  45  ARG ARG D . n 
C 2 46  GLU 46  46  46  GLU GLU D . n 
C 2 47  LEU 47  47  47  LEU LEU D . n 
C 2 48  VAL 48  48  48  VAL VAL D . n 
C 2 49  ALA 49  49  49  ALA ALA D . n 
C 2 50  THR 50  50  50  THR THR D . n 
C 2 51  ILE 51  51  51  ILE ILE D . n 
C 2 52  THR 52  52  52  THR THR D . n 
C 2 53  SER 53  53  53  SER SER D . n 
C 2 54  SER 54  54  54  SER SER D . n 
C 2 55  GLY 55  55  55  GLY GLY D . n 
C 2 56  GLU 56  56  56  GLU GLU D . n 
C 2 57  THR 57  57  57  THR THR D . n 
C 2 58  LYS 58  58  58  LYS LYS D . n 
C 2 59  HIS 59  59  59  HIS HIS D . n 
C 2 60  VAL 60  60  60  VAL VAL D . n 
C 2 61  TYR 61  61  61  TYR TYR D . n 
C 2 62  SER 62  62  62  SER SER D . n 
C 2 63  VAL 63  63  63  VAL VAL D . n 
C 2 64  LYS 64  64  64  LYS LYS D . n 
C 2 65  GLY 65  65  65  GLY GLY D . n 
C 2 66  ARG 66  66  66  ARG ARG D . n 
C 2 67  PHE 67  67  67  PHE PHE D . n 
C 2 68  THR 68  68  68  THR THR D . n 
C 2 69  ILE 69  69  69  ILE ILE D . n 
C 2 70  SER 70  70  70  SER SER D . n 
C 2 71  ARG 71  71  71  ARG ARG D . n 
C 2 72  GLU 72  72  72  GLU GLU D . n 
C 2 73  ASN 73  73  73  ASN ASN D . n 
C 2 74  ALA 74  74  74  ALA ALA D . n 
C 2 75  LYS 75  75  75  LYS LYS D . n 
C 2 76  ASN 76  76  76  ASN ASN D . n 
C 2 77  ALA 77  77  77  ALA ALA D . n 
C 2 78  TRP 78  78  78  TRP TRP D . n 
C 2 79  TYR 79  79  79  TYR TYR D . n 
C 2 80  LEU 80  80  80  LEU LEU D . n 
C 2 81  GLN 81  81  81  GLN GLN D . n 
C 2 82  MET 82  82  82  MET MET D . n 
C 2 83  ASN 83  83  83  ASN ASN D . n 
C 2 84  SER 84  84  84  SER SER D . n 
C 2 85  LEU 85  85  85  LEU LEU D . n 
C 2 86  LYS 86  86  86  LYS LYS D . n 
C 2 87  PRO 87  87  87  PRO PRO D . n 
C 2 88  GLU 88  88  88  GLU GLU D . n 
C 2 89  ASP 89  89  89  ASP ASP D . n 
C 2 90  THR 90  90  90  THR THR D . n 
C 2 91  GLY 91  91  91  GLY GLY D . n 
C 2 92  VAL 92  92  92  VAL VAL D . n 
C 2 93  TYR 93  93  93  TYR TYR D . n 
C 2 94  TYR 94  94  94  TYR TYR D . n 
C 2 95  CYS 95  95  95  CYS CYS D . n 
C 2 96  HIS 96  96  96  HIS HIS D . n 
C 2 97  ALA 97  97  97  ALA ALA D . n 
C 2 98  VAL 98  98  98  VAL VAL D . n 
C 2 99  THR 99  99  99  THR THR D . n 
C 2 100 GLY 100 100 100 GLY GLY D . n 
C 2 101 VAL 101 101 101 VAL VAL D . n 
C 2 102 ILE 102 102 102 ILE ILE D . n 
C 2 103 ALA 103 103 103 ALA ALA D . n 
C 2 104 SER 104 104 104 SER SER D . n 
C 2 105 SER 105 105 105 SER SER D . n 
C 2 106 TRP 106 106 106 TRP TRP D . n 
C 2 107 GLY 107 107 107 GLY GLY D . n 
C 2 108 GLN 108 108 108 GLN GLN D . n 
C 2 109 GLY 109 109 ?   ?   ?   D . n 
C 2 110 THR 110 110 ?   ?   ?   D . n 
C 2 111 GLN 111 111 ?   ?   ?   D . n 
C 2 112 VAL 112 112 ?   ?   ?   D . n 
C 2 113 THR 113 113 ?   ?   ?   D . n 
C 2 114 VAL 114 114 ?   ?   ?   D . n 
C 2 115 SER 115 115 ?   ?   ?   D . n 
C 2 116 SER 116 116 ?   ?   ?   D . n 
C 2 117 HIS 117 117 ?   ?   ?   D . n 
C 2 118 HIS 118 118 ?   ?   ?   D . n 
C 2 119 HIS 119 119 ?   ?   ?   D . n 
C 2 120 HIS 120 120 ?   ?   ?   D . n 
C 2 121 HIS 121 121 ?   ?   ?   D . n 
C 2 122 HIS 122 122 ?   ?   ?   D . n 
D 1 1   THR 1   224 ?   ?   ?   A . n 
D 1 2   LYS 2   225 225 LYS LYS A . n 
D 1 3   PRO 3   226 226 PRO PRO A . n 
D 1 4   PHE 4   227 227 PHE PHE A . n 
D 1 5   SER 5   228 228 SER SER A . n 
D 1 6   VAL 6   229 229 VAL VAL A . n 
D 1 7   PRO 7   230 230 PRO PRO A . n 
D 1 8   VAL 8   231 231 VAL VAL A . n 
D 1 9   LEU 9   232 232 LEU LEU A . n 
D 1 10  THR 10  233 233 THR THR A . n 
D 1 11  VAL 11  234 234 VAL VAL A . n 
D 1 12  GLU 12  235 235 GLU GLU A . n 
D 1 13  GLU 13  236 236 GLU GLU A . n 
D 1 14  MET 14  237 237 MET MET A . n 
D 1 15  THR 15  238 238 THR THR A . n 
D 1 16  ASN 16  239 239 ASN ASN A . n 
D 1 17  SER 17  240 240 SER SER A . n 
D 1 18  ARG 18  241 241 ARG ARG A . n 
D 1 19  PHE 19  242 242 PHE PHE A . n 
D 1 20  PRO 20  243 243 PRO PRO A . n 
D 1 21  ILE 21  244 244 ILE ILE A . n 
D 1 22  PRO 22  245 245 PRO PRO A . n 
D 1 23  LEU 23  246 246 LEU LEU A . n 
D 1 24  GLU 24  247 247 GLU GLU A . n 
D 1 25  LYS 25  248 248 LYS LYS A . n 
D 1 26  LEU 26  249 249 LEU LEU A . n 
D 1 27  PHE 27  250 250 PHE PHE A . n 
D 1 28  THR 28  251 251 THR THR A . n 
D 1 29  GLY 29  252 252 GLY GLY A . n 
D 1 30  PRO 30  253 253 PRO PRO A . n 
D 1 31  SER 31  254 254 SER SER A . n 
D 1 32  SER 32  255 255 SER SER A . n 
D 1 33  ALA 33  256 256 ALA ALA A . n 
D 1 34  PHE 34  257 257 PHE PHE A . n 
D 1 35  VAL 35  258 258 VAL VAL A . n 
D 1 36  VAL 36  259 259 VAL VAL A . n 
D 1 37  GLN 37  260 260 GLN GLN A . n 
D 1 38  PRO 38  261 261 PRO PRO A . n 
D 1 39  GLN 39  262 262 GLN GLN A . n 
D 1 40  ASN 40  263 263 ASN ASN A . n 
D 1 41  GLY 41  264 264 GLY GLY A . n 
D 1 42  ARG 42  265 265 ARG ARG A . n 
D 1 43  CYS 43  266 266 CYS CYS A . n 
D 1 44  THR 44  267 267 THR THR A . n 
D 1 45  THR 45  268 268 THR THR A . n 
D 1 46  ASP 46  269 269 ASP ASP A . n 
D 1 47  GLY 47  270 270 GLY GLY A . n 
D 1 48  VAL 48  271 271 VAL VAL A . n 
D 1 49  LEU 49  272 272 LEU LEU A . n 
D 1 50  LEU 50  273 273 LEU LEU A . n 
D 1 51  GLY 51  274 274 GLY GLY A . n 
D 1 52  THR 52  275 275 THR THR A . n 
D 1 53  THR 53  276 276 THR THR A . n 
D 1 54  GLN 54  277 277 GLN GLN A . n 
D 1 55  LEU 55  278 278 LEU LEU A . n 
D 1 56  SER 56  279 279 SER SER A . n 
D 1 57  PRO 57  280 280 PRO PRO A . n 
D 1 58  VAL 58  281 281 VAL VAL A . n 
D 1 59  ASN 59  282 282 ASN ASN A . n 
D 1 60  ILE 60  283 283 ILE ILE A . n 
D 1 61  CYS 61  284 284 CYS CYS A . n 
D 1 62  THR 62  285 285 THR THR A . n 
D 1 63  PHE 63  286 286 PHE PHE A . n 
D 1 64  ARG 64  287 287 ARG ARG A . n 
D 1 65  GLY 65  288 288 GLY GLY A . n 
D 1 66  ASP 66  289 289 ASP ASP A . n 
D 1 67  VAL 67  290 290 VAL VAL A . n 
D 1 68  THR 68  291 291 THR THR A . n 
D 1 69  HIS 69  292 292 HIS HIS A . n 
D 1 70  ILE 70  293 293 ILE ILE A . n 
D 1 71  THR 71  294 294 THR THR A . n 
D 1 72  GLY 72  295 295 GLY GLY A . n 
D 1 73  SER 73  296 296 SER SER A . n 
D 1 74  ARG 74  297 297 ARG ARG A . n 
D 1 75  ASN 75  298 298 ASN ASN A . n 
D 1 76  TYR 76  299 299 TYR TYR A . n 
D 1 77  THR 77  300 300 THR THR A . n 
D 1 78  MET 78  301 301 MET MET A . n 
D 1 79  ASN 79  302 302 ASN ASN A . n 
D 1 80  LEU 80  303 303 LEU LEU A . n 
D 1 81  ALA 81  304 304 ALA ALA A . n 
D 1 82  SER 82  305 305 SER SER A . n 
D 1 83  GLN 83  306 306 GLN GLN A . n 
D 1 84  ASN 84  307 307 ASN ASN A . n 
D 1 85  TRP 85  308 308 TRP TRP A . n 
D 1 86  ASN 86  309 309 ASN ASN A . n 
D 1 87  ASP 87  310 310 ASP ASP A . n 
D 1 88  TYR 88  311 311 TYR TYR A . n 
D 1 89  ASP 89  312 312 ASP ASP A . n 
D 1 90  PRO 90  313 313 PRO PRO A . n 
D 1 91  THR 91  314 314 THR THR A . n 
D 1 92  GLU 92  315 315 GLU GLU A . n 
D 1 93  GLU 93  316 316 GLU GLU A . n 
D 1 94  ILE 94  317 317 ILE ILE A . n 
D 1 95  PRO 95  318 318 PRO PRO A . n 
D 1 96  ALA 96  319 319 ALA ALA A . n 
D 1 97  PRO 97  320 320 PRO PRO A . n 
D 1 98  LEU 98  321 321 LEU LEU A . n 
D 1 99  GLY 99  322 322 GLY GLY A . n 
D 1 100 THR 100 323 323 THR THR A . n 
D 1 101 PRO 101 324 324 PRO PRO A . n 
D 1 102 ASP 102 325 325 ASP ASP A . n 
D 1 103 PHE 103 326 326 PHE PHE A . n 
D 1 104 VAL 104 327 327 VAL VAL A . n 
D 1 105 GLY 105 328 328 GLY GLY A . n 
D 1 106 LYS 106 329 329 LYS LYS A . n 
D 1 107 ILE 107 330 330 ILE ILE A . n 
D 1 108 GLN 108 331 331 GLN GLN A . n 
D 1 109 GLY 109 332 332 GLY GLY A . n 
D 1 110 VAL 110 333 333 VAL VAL A . n 
D 1 111 LEU 111 334 334 LEU LEU A . n 
D 1 112 THR 112 335 335 THR THR A . n 
D 1 113 GLN 113 336 336 GLN GLN A . n 
D 1 114 THR 114 337 337 THR THR A . n 
D 1 115 THR 115 338 338 THR THR A . n 
D 1 116 ARG 116 339 339 ARG ARG A . n 
D 1 117 THR 117 340 340 THR THR A . n 
D 1 118 ASP 118 341 341 ASP ASP A . n 
D 1 119 GLY 119 342 342 GLY GLY A . n 
D 1 120 SER 120 343 343 SER SER A . n 
D 1 121 THR 121 344 344 THR THR A . n 
D 1 122 ARG 122 345 345 ARG ARG A . n 
D 1 123 GLY 123 346 346 GLY GLY A . n 
D 1 124 HIS 124 347 347 HIS HIS A . n 
D 1 125 LYS 125 348 348 LYS LYS A . n 
D 1 126 ALA 126 349 349 ALA ALA A . n 
D 1 127 THR 127 350 350 THR THR A . n 
D 1 128 VAL 128 351 351 VAL VAL A . n 
D 1 129 TYR 129 352 352 TYR TYR A . n 
D 1 130 THR 130 353 353 THR THR A . n 
D 1 131 GLY 131 354 354 GLY GLY A . n 
D 1 132 SER 132 355 355 SER SER A . n 
D 1 133 ALA 133 356 356 ALA ALA A . n 
D 1 134 ASP 134 357 357 ASP ASP A . n 
D 1 135 PHE 135 358 358 PHE PHE A . n 
D 1 136 ALA 136 359 359 ALA ALA A . n 
D 1 137 PRO 137 360 360 PRO PRO A . n 
D 1 138 LYS 138 361 361 LYS LYS A . n 
D 1 139 LEU 139 362 362 LEU LEU A . n 
D 1 140 GLY 140 363 363 GLY GLY A . n 
D 1 141 ARG 141 364 364 ARG ARG A . n 
D 1 142 VAL 142 365 365 VAL VAL A . n 
D 1 143 GLN 143 366 366 GLN GLN A . n 
D 1 144 PHE 144 367 367 PHE PHE A . n 
D 1 145 GLU 145 368 368 GLU GLU A . n 
D 1 146 THR 146 369 369 THR THR A . n 
D 1 147 ASP 147 370 370 ASP ASP A . n 
D 1 148 THR 148 371 371 THR THR A . n 
D 1 149 ASP 149 372 372 ASP ASP A . n 
D 1 150 ARG 150 373 373 ARG ARG A . n 
D 1 151 ASP 151 374 374 ASP ASP A . n 
D 1 152 PHE 152 375 375 PHE PHE A . n 
D 1 153 GLU 153 376 376 GLU GLU A . n 
D 1 154 ALA 154 377 377 ALA ALA A . n 
D 1 155 ASN 155 378 378 ASN ASN A . n 
D 1 156 GLN 156 379 379 GLN GLN A . n 
D 1 157 ASN 157 380 380 ASN ASN A . n 
D 1 158 THR 158 381 381 THR THR A . n 
D 1 159 LYS 159 382 382 LYS LYS A . n 
D 1 160 PHE 160 383 383 PHE PHE A . n 
D 1 161 THR 161 384 384 THR THR A . n 
D 1 162 PRO 162 385 385 PRO PRO A . n 
D 1 163 VAL 163 386 386 VAL VAL A . n 
D 1 164 GLY 164 387 387 GLY GLY A . n 
D 1 165 VAL 165 388 388 VAL VAL A . n 
D 1 166 ILE 166 389 389 ILE ILE A . n 
D 1 167 GLN 167 390 390 GLN GLN A . n 
D 1 168 ASP 168 391 391 ASP ASP A . n 
D 1 169 GLY 169 392 392 GLY GLY A . n 
D 1 170 GLY 170 393 393 GLY GLY A . n 
D 1 171 THR 171 394 394 THR THR A . n 
D 1 172 THR 172 395 395 THR THR A . n 
D 1 173 HIS 173 396 396 HIS HIS A . n 
D 1 174 ARG 174 397 397 ARG ARG A . n 
D 1 175 ASN 175 398 398 ASN ASN A . n 
D 1 176 GLU 176 399 399 GLU GLU A . n 
D 1 177 PRO 177 400 400 PRO PRO A . n 
D 1 178 GLN 178 401 401 GLN GLN A . n 
D 1 179 GLN 179 402 402 GLN GLN A . n 
D 1 180 TRP 180 403 403 TRP TRP A . n 
D 1 181 VAL 181 404 404 VAL VAL A . n 
D 1 182 LEU 182 405 405 LEU LEU A . n 
D 1 183 PRO 183 406 406 PRO PRO A . n 
D 1 184 SER 184 407 407 SER SER A . n 
D 1 185 TYR 185 408 408 TYR TYR A . n 
D 1 186 SER 186 409 409 SER SER A . n 
D 1 187 GLY 187 410 410 GLY GLY A . n 
D 1 188 ARG 188 411 411 ARG ARG A . n 
D 1 189 ASN 189 412 412 ASN ASN A . n 
D 1 190 THR 190 413 413 THR THR A . n 
D 1 191 HIS 191 414 414 HIS HIS A . n 
D 1 192 ASN 192 415 415 ASN ASN A . n 
D 1 193 VAL 193 416 416 VAL VAL A . n 
D 1 194 HIS 194 417 417 HIS HIS A . n 
D 1 195 LEU 195 418 418 LEU LEU A . n 
D 1 196 ALA 196 419 419 ALA ALA A . n 
D 1 197 PRO 197 420 420 PRO PRO A . n 
D 1 198 ALA 198 421 421 ALA ALA A . n 
D 1 199 VAL 199 422 422 VAL VAL A . n 
D 1 200 ALA 200 423 423 ALA ALA A . n 
D 1 201 PRO 201 424 424 PRO PRO A . n 
D 1 202 THR 202 425 425 THR THR A . n 
D 1 203 PHE 203 426 426 PHE PHE A . n 
D 1 204 PRO 204 427 427 PRO PRO A . n 
D 1 205 GLY 205 428 428 GLY GLY A . n 
D 1 206 GLU 206 429 429 GLU GLU A . n 
D 1 207 GLN 207 430 430 GLN GLN A . n 
D 1 208 LEU 208 431 431 LEU LEU A . n 
D 1 209 LEU 209 432 432 LEU LEU A . n 
D 1 210 PHE 210 433 433 PHE PHE A . n 
D 1 211 PHE 211 434 434 PHE PHE A . n 
D 1 212 ARG 212 435 435 ARG ARG A . n 
D 1 213 SER 213 436 436 SER SER A . n 
D 1 214 THR 214 437 437 THR THR A . n 
D 1 215 MET 215 438 438 MET MET A . n 
D 1 216 PRO 216 439 439 PRO PRO A . n 
D 1 217 GLY 217 440 440 GLY GLY A . n 
D 1 218 CYS 218 441 441 CYS CYS A . n 
D 1 219 SER 219 442 442 SER SER A . n 
D 1 220 GLY 220 443 443 GLY GLY A . n 
D 1 221 TYR 221 444 444 TYR TYR A . n 
D 1 222 PRO 222 445 445 PRO PRO A . n 
D 1 223 ASN 223 446 446 ASN ASN A . n 
D 1 224 MET 224 447 447 MET MET A . n 
D 1 225 ASP 225 448 448 ASP ASP A . n 
D 1 226 LEU 226 449 449 LEU LEU A . n 
D 1 227 ASP 227 450 450 ASP ASP A . n 
D 1 228 CYS 228 451 451 CYS CYS A . n 
D 1 229 LEU 229 452 452 LEU LEU A . n 
D 1 230 LEU 230 453 453 LEU LEU A . n 
D 1 231 PRO 231 454 454 PRO PRO A . n 
D 1 232 GLN 232 455 455 GLN GLN A . n 
D 1 233 GLU 233 456 456 GLU GLU A . n 
D 1 234 TRP 234 457 457 TRP TRP A . n 
D 1 235 VAL 235 458 458 VAL VAL A . n 
D 1 236 GLN 236 459 459 GLN GLN A . n 
D 1 237 TYR 237 460 460 TYR TYR A . n 
D 1 238 PHE 238 461 461 PHE PHE A . n 
D 1 239 TYR 239 462 462 TYR TYR A . n 
D 1 240 GLN 240 463 463 GLN GLN A . n 
D 1 241 GLU 241 464 464 GLU GLU A . n 
D 1 242 ALA 242 465 465 ALA ALA A . n 
D 1 243 ALA 243 466 466 ALA ALA A . n 
D 1 244 PRO 244 467 467 PRO PRO A . n 
D 1 245 ALA 245 468 468 ALA ALA A . n 
D 1 246 GLN 246 469 469 GLN GLN A . n 
D 1 247 SER 247 470 470 SER SER A . n 
D 1 248 ASP 248 471 471 ASP ASP A . n 
D 1 249 VAL 249 472 472 VAL VAL A . n 
D 1 250 ALA 250 473 473 ALA ALA A . n 
D 1 251 LEU 251 474 474 LEU LEU A . n 
D 1 252 LEU 252 475 475 LEU LEU A . n 
D 1 253 ARG 253 476 476 ARG ARG A . n 
D 1 254 PHE 254 477 477 PHE PHE A . n 
D 1 255 VAL 255 478 478 VAL VAL A . n 
D 1 256 ASN 256 479 479 ASN ASN A . n 
D 1 257 PRO 257 480 480 PRO PRO A . n 
D 1 258 ASP 258 481 481 ASP ASP A . n 
D 1 259 THR 259 482 482 THR THR A . n 
D 1 260 GLY 260 483 483 GLY GLY A . n 
D 1 261 ARG 261 484 484 ARG ARG A . n 
D 1 262 VAL 262 485 485 VAL VAL A . n 
D 1 263 LEU 263 486 486 LEU LEU A . n 
D 1 264 PHE 264 487 487 PHE PHE A . n 
D 1 265 GLU 265 488 488 GLU GLU A . n 
D 1 266 CYS 266 489 489 CYS CYS A . n 
D 1 267 LYS 267 490 490 LYS LYS A . n 
D 1 268 LEU 268 491 491 LEU LEU A . n 
D 1 269 HIS 269 492 492 HIS HIS A . n 
D 1 270 LYS 270 493 493 LYS LYS A . n 
D 1 271 SER 271 494 494 SER SER A . n 
D 1 272 GLY 272 495 495 GLY GLY A . n 
D 1 273 TYR 273 496 496 TYR TYR A . n 
D 1 274 VAL 274 497 497 VAL VAL A . n 
D 1 275 THR 275 498 498 THR THR A . n 
D 1 276 VAL 276 499 499 VAL VAL A . n 
D 1 277 ALA 277 500 500 ALA ALA A . n 
D 1 278 HIS 278 501 501 HIS HIS A . n 
D 1 279 THR 279 502 502 THR THR A . n 
D 1 280 GLY 280 503 503 GLY GLY A . n 
D 1 281 GLN 281 504 504 GLN GLN A . n 
D 1 282 HIS 282 505 505 HIS HIS A . n 
D 1 283 ASP 283 506 506 ASP ASP A . n 
D 1 284 LEU 284 507 507 LEU LEU A . n 
D 1 285 VAL 285 508 508 VAL VAL A . n 
D 1 286 ILE 286 509 509 ILE ILE A . n 
D 1 287 PRO 287 510 510 PRO PRO A . n 
D 1 288 PRO 288 511 511 PRO PRO A . n 
D 1 289 ASN 289 512 512 ASN ASN A . n 
D 1 290 GLY 290 513 513 GLY GLY A . n 
D 1 291 TYR 291 514 514 TYR TYR A . n 
D 1 292 PHE 292 515 515 PHE PHE A . n 
D 1 293 ARG 293 516 516 ARG ARG A . n 
D 1 294 PHE 294 517 517 PHE PHE A . n 
D 1 295 ASP 295 518 518 ASP ASP A . n 
D 1 296 SER 296 519 519 SER SER A . n 
D 1 297 TRP 297 520 520 TRP TRP A . n 
D 1 298 VAL 298 521 521 VAL VAL A . n 
D 1 299 ASN 299 522 522 ASN ASN A . n 
D 1 300 GLN 300 523 523 GLN GLN A . n 
D 1 301 PHE 301 524 524 PHE PHE A . n 
D 1 302 TYR 302 525 525 TYR TYR A . n 
D 1 303 THR 303 526 526 THR THR A . n 
D 1 304 LEU 304 527 527 LEU LEU A . n 
D 1 305 ALA 305 528 528 ALA ALA A . n 
D 1 306 PRO 306 529 529 PRO PRO A . n 
D 1 307 MET 307 530 530 MET MET A . n 
D 1 308 GLY 308 531 531 GLY GLY A . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              g.hansman@griffith.edu.au 
_pdbx_contact_author.name_first         Grant 
_pdbx_contact_author.name_last          Hansman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8735-4618 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 EDO 1  201 201 EDO EDO C . 
F 3 EDO 1  202 301 EDO EDO C . 
G 3 EDO 1  601 624 EDO EDO A . 
H 4 HOH 1  601 49  HOH HOH B . 
H 4 HOH 2  602 102 HOH HOH B . 
H 4 HOH 3  603 25  HOH HOH B . 
H 4 HOH 4  604 18  HOH HOH B . 
H 4 HOH 5  605 77  HOH HOH B . 
H 4 HOH 6  606 89  HOH HOH B . 
H 4 HOH 7  607 57  HOH HOH B . 
H 4 HOH 8  608 100 HOH HOH B . 
H 4 HOH 9  609 87  HOH HOH B . 
H 4 HOH 10 610 31  HOH HOH B . 
H 4 HOH 11 611 60  HOH HOH B . 
H 4 HOH 12 612 1   HOH HOH B . 
H 4 HOH 13 613 34  HOH HOH B . 
H 4 HOH 14 614 99  HOH HOH B . 
H 4 HOH 15 615 70  HOH HOH B . 
H 4 HOH 16 616 22  HOH HOH B . 
H 4 HOH 17 617 82  HOH HOH B . 
H 4 HOH 18 618 108 HOH HOH B . 
H 4 HOH 19 619 53  HOH HOH B . 
H 4 HOH 20 620 106 HOH HOH B . 
H 4 HOH 21 621 56  HOH HOH B . 
H 4 HOH 22 622 105 HOH HOH B . 
H 4 HOH 23 623 42  HOH HOH B . 
H 4 HOH 24 624 47  HOH HOH B . 
H 4 HOH 25 625 112 HOH HOH B . 
H 4 HOH 26 626 16  HOH HOH B . 
H 4 HOH 27 627 90  HOH HOH B . 
H 4 HOH 28 628 9   HOH HOH B . 
H 4 HOH 29 629 14  HOH HOH B . 
H 4 HOH 30 630 43  HOH HOH B . 
H 4 HOH 31 631 44  HOH HOH B . 
H 4 HOH 32 632 15  HOH HOH B . 
H 4 HOH 33 633 45  HOH HOH B . 
H 4 HOH 34 634 13  HOH HOH B . 
H 4 HOH 35 635 76  HOH HOH B . 
H 4 HOH 36 636 68  HOH HOH B . 
H 4 HOH 37 637 3   HOH HOH B . 
H 4 HOH 38 638 101 HOH HOH B . 
H 4 HOH 39 639 111 HOH HOH B . 
I 4 HOH 1  301 6   HOH HOH C . 
I 4 HOH 2  302 107 HOH HOH C . 
I 4 HOH 3  303 21  HOH HOH C . 
I 4 HOH 4  304 80  HOH HOH C . 
I 4 HOH 5  305 23  HOH HOH C . 
I 4 HOH 6  306 67  HOH HOH C . 
I 4 HOH 7  307 73  HOH HOH C . 
I 4 HOH 8  308 97  HOH HOH C . 
I 4 HOH 9  309 7   HOH HOH C . 
I 4 HOH 10 310 103 HOH HOH C . 
I 4 HOH 11 311 51  HOH HOH C . 
J 4 HOH 1  201 72  HOH HOH D . 
K 4 HOH 1  701 17  HOH HOH A . 
K 4 HOH 2  702 86  HOH HOH A . 
K 4 HOH 3  703 33  HOH HOH A . 
K 4 HOH 4  704 2   HOH HOH A . 
K 4 HOH 5  705 55  HOH HOH A . 
K 4 HOH 6  706 104 HOH HOH A . 
K 4 HOH 7  707 36  HOH HOH A . 
K 4 HOH 8  708 61  HOH HOH A . 
K 4 HOH 9  709 94  HOH HOH A . 
K 4 HOH 10 710 83  HOH HOH A . 
K 4 HOH 11 711 4   HOH HOH A . 
K 4 HOH 12 712 40  HOH HOH A . 
K 4 HOH 13 713 39  HOH HOH A . 
K 4 HOH 14 714 65  HOH HOH A . 
K 4 HOH 15 715 35  HOH HOH A . 
K 4 HOH 16 716 88  HOH HOH A . 
K 4 HOH 17 717 62  HOH HOH A . 
K 4 HOH 18 718 5   HOH HOH A . 
K 4 HOH 19 719 38  HOH HOH A . 
K 4 HOH 20 720 46  HOH HOH A . 
K 4 HOH 21 721 96  HOH HOH A . 
K 4 HOH 22 722 11  HOH HOH A . 
K 4 HOH 23 723 113 HOH HOH A . 
K 4 HOH 24 724 12  HOH HOH A . 
K 4 HOH 25 725 58  HOH HOH A . 
K 4 HOH 26 726 63  HOH HOH A . 
K 4 HOH 27 727 69  HOH HOH A . 
K 4 HOH 28 728 59  HOH HOH A . 
K 4 HOH 29 729 26  HOH HOH A . 
K 4 HOH 30 730 85  HOH HOH A . 
K 4 HOH 31 731 91  HOH HOH A . 
K 4 HOH 32 732 27  HOH HOH A . 
K 4 HOH 33 733 93  HOH HOH A . 
K 4 HOH 34 734 54  HOH HOH A . 
K 4 HOH 35 735 110 HOH HOH A . 
K 4 HOH 36 736 41  HOH HOH A . 
K 4 HOH 37 737 75  HOH HOH A . 
K 4 HOH 38 738 19  HOH HOH A . 
K 4 HOH 39 739 79  HOH HOH A . 
K 4 HOH 40 740 28  HOH HOH A . 
K 4 HOH 41 741 64  HOH HOH A . 
K 4 HOH 42 742 74  HOH HOH A . 
K 4 HOH 43 743 81  HOH HOH A . 
K 4 HOH 44 744 48  HOH HOH A . 
K 4 HOH 45 745 30  HOH HOH A . 
K 4 HOH 46 746 66  HOH HOH A . 
K 4 HOH 47 747 71  HOH HOH A . 
K 4 HOH 48 748 98  HOH HOH A . 
K 4 HOH 49 749 32  HOH HOH A . 
K 4 HOH 50 750 52  HOH HOH A . 
K 4 HOH 51 751 109 HOH HOH A . 
K 4 HOH 52 752 29  HOH HOH A . 
K 4 HOH 53 753 24  HOH HOH A . 
K 4 HOH 54 754 78  HOH HOH A . 
K 4 HOH 55 755 20  HOH HOH A . 
K 4 HOH 56 756 37  HOH HOH A . 
K 4 HOH 57 757 10  HOH HOH A . 
K 4 HOH 58 758 92  HOH HOH A . 
K 4 HOH 59 759 8   HOH HOH A . 
K 4 HOH 60 760 50  HOH HOH A . 
K 4 HOH 61 761 95  HOH HOH A . 
K 4 HOH 62 762 84  HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2023-03-15 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.19.2_4158 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27        2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .           5 
# 
_pdbx_entry_details.entry_id                 8EN4 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   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 GLN B 277 ? ? -119.08 -164.04 
2 1 ARG B 373 ? ? -163.58 4.31    
3 1 VAL B 386 ? ? -127.32 -52.59  
4 1 SER D 84  ? ? 51.65   77.35   
5 1 PRO A 243 ? ? -69.35  64.10   
6 1 ARG A 373 ? ? -140.73 -8.17   
7 1 VAL A 386 ? ? -120.98 -53.36  
8 1 SER A 442 ? ? -170.15 140.00  
9 1 ASP A 518 ? ? -99.38  -68.26  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 C HIS 119 ? B HIS 119 
2  1 Y 1 C HIS 120 ? B HIS 120 
3  1 Y 1 C HIS 121 ? B HIS 121 
4  1 Y 1 C HIS 122 ? B HIS 122 
5  1 Y 1 D GLY 109 ? C GLY 109 
6  1 Y 1 D THR 110 ? C THR 110 
7  1 Y 1 D GLN 111 ? C GLN 111 
8  1 Y 1 D VAL 112 ? C VAL 112 
9  1 Y 1 D THR 113 ? C THR 113 
10 1 Y 1 D VAL 114 ? C VAL 114 
11 1 Y 1 D SER 115 ? C SER 115 
12 1 Y 1 D SER 116 ? C SER 116 
13 1 Y 1 D HIS 117 ? C HIS 117 
14 1 Y 1 D HIS 118 ? C HIS 118 
15 1 Y 1 D HIS 119 ? C HIS 119 
16 1 Y 1 D HIS 120 ? C HIS 120 
17 1 Y 1 D HIS 121 ? C HIS 121 
18 1 Y 1 D HIS 122 ? C HIS 122 
19 1 Y 1 A THR 224 ? D THR 1   
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-ETHANEDIOL EDO 
4 water          HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
