data_3M5H
# 
_entry.id   3M5H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3M5H         
RCSB  RCSB058132   
WWPDB D_1000058132 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M5G 'Crystal structure of a H7 influenza virus hemagglutinin'                     unspecified 
PDB 3M5I 'Crystal structure of a H7 influenza virus hemagglutinin complexed with 6SLN' unspecified 
PDB 3M5J 'Crystal structure of a H7 influenza virus hemagglutinin complexed with LSTb' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3M5H 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-12 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Yang, H.'     1 
'Chen, L.M.'   2 
'Carney, P.J.' 3 
'Donis, R.O.'  4 
'Stevens, J.'  5 
# 
_citation.id                        primary 
_citation.title                     
;Structures of receptor complexes of a North American H7N2 influenza hemagglutinin with a loop deletion in the receptor binding site.
;
_citation.journal_abbrev            'Plos Pathog.' 
_citation.journal_volume            6 
_citation.page_first                e1001081 
_citation.page_last                 e1001081 
_citation.year                      2010 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1553-7366 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20824086 
_citation.pdbx_database_id_DOI      10.1371/journal.ppat.1001081 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Yang, H.'     1 
primary 'Chen, L.M.'   2 
primary 'Carney, P.J.' 3 
primary 'Donis, R.O.'  4 
primary 'Stevens, J.'  5 
# 
_cell.entry_id           3M5H 
_cell.length_a           67.798 
_cell.length_b           116.698 
_cell.length_c           249.836 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3M5H 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
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 Hemagglutinin          34880.359 3   ? ? 'Hemagglutinin HA1' ? 
2 polymer     man Hemagglutinin          20895.980 3   ? ? 'Hemagglutinin HA2' ? 
3 non-polymer man 'O-SIALIC ACID'        309.270   3   ? ? ?                   ? 
4 non-polymer man BETA-D-GALACTOSE       180.156   3   ? ? ?                   ? 
5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   10  ? ? ?                   ? 
6 non-polymer syn GLYCEROL               92.094    4   ? ? ?                   ? 
7 water       nat water                  18.015    257 ? ? ?                   ? 
# 
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 
;ADPGDKICLGHHAVANGTKVNTLTERGIEVVNATETVETTNIKKICTQGKRPTDLGQCGLLGTLIGPPQCDQFLEFSSDL
IIERREGTDICYPGRFTNEESLRQILRRSGGIGKESMGFTYSGIRTNGATSACTRSGSSFYAEMKWLLSNSDNAAFPQMT
KAYRNPRNKPALIIWGVHHSESVSEQTKLYGSGNKLITVRSSKYQQSFTPNPGARRIDFHWLLLDPNDTVTFTFNGAFIA
PDRTSFFRGESLGVQSDAPLDSSCRGDCFHSGGTIVSSLPFQNINSRTVGKCPRYVKQKSLLLATGMRNVPEKPKPR
;
;ADPGDKICLGHHAVANGTKVNTLTERGIEVVNATETVETTNIKKICTQGKRPTDLGQCGLLGTLIGPPQCDQFLEFSSDL
IIERREGTDICYPGRFTNEESLRQILRRSGGIGKESMGFTYSGIRTNGATSACTRSGSSFYAEMKWLLSNSDNAAFPQMT
KAYRNPRNKPALIIWGVHHSESVSEQTKLYGSGNKLITVRSSKYQQSFTPNPGARRIDFHWLLLDPNDTVTFTFNGAFIA
PDRTSFFRGESLGVQSDAPLDSSCRGDCFHSGGTIVSSLPFQNINSRTVGKCPRYVKQKSLLLATGMRNVPEKPKPR
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIENGWEGLINGWYGFRHQNAQGEGTAADYKSTQSAIDQITGKLNRLIGKTNQQFELIDNEFNEIEQQIGNV
INWTRDAMTEIWSYNAELLVAMENQHTIDLADSEMSKLYERVKKQLRENAEEDGTGCFEIFHKCDDQCMESIRNNTYDHT
QYRTESLQNRIQIDSGRLVPRG
;
;GLFGAIAGFIENGWEGLINGWYGFRHQNAQGEGTAADYKSTQSAIDQITGKLNRLIGKTNQQFELIDNEFNEIEQQIGNV
INWTRDAMTEIWSYNAELLVAMENQHTIDLADSEMSKLYERVKKQLRENAEEDGTGCFEIFHKCDDQCMESIRNNTYDHT
QYRTESLQNRIQIDSGRLVPRG
;
B,D,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   PRO n 
1 4   GLY n 
1 5   ASP n 
1 6   LYS n 
1 7   ILE n 
1 8   CYS n 
1 9   LEU n 
1 10  GLY n 
1 11  HIS n 
1 12  HIS n 
1 13  ALA n 
1 14  VAL n 
1 15  ALA n 
1 16  ASN n 
1 17  GLY n 
1 18  THR n 
1 19  LYS n 
1 20  VAL n 
1 21  ASN n 
1 22  THR n 
1 23  LEU n 
1 24  THR n 
1 25  GLU n 
1 26  ARG n 
1 27  GLY n 
1 28  ILE n 
1 29  GLU n 
1 30  VAL n 
1 31  VAL n 
1 32  ASN n 
1 33  ALA n 
1 34  THR n 
1 35  GLU n 
1 36  THR n 
1 37  VAL n 
1 38  GLU n 
1 39  THR n 
1 40  THR n 
1 41  ASN n 
1 42  ILE n 
1 43  LYS n 
1 44  LYS n 
1 45  ILE n 
1 46  CYS n 
1 47  THR n 
1 48  GLN n 
1 49  GLY n 
1 50  LYS n 
1 51  ARG n 
1 52  PRO n 
1 53  THR n 
1 54  ASP n 
1 55  LEU n 
1 56  GLY n 
1 57  GLN n 
1 58  CYS n 
1 59  GLY n 
1 60  LEU n 
1 61  LEU n 
1 62  GLY n 
1 63  THR n 
1 64  LEU n 
1 65  ILE n 
1 66  GLY n 
1 67  PRO n 
1 68  PRO n 
1 69  GLN n 
1 70  CYS n 
1 71  ASP n 
1 72  GLN n 
1 73  PHE n 
1 74  LEU n 
1 75  GLU n 
1 76  PHE n 
1 77  SER n 
1 78  SER n 
1 79  ASP n 
1 80  LEU n 
1 81  ILE n 
1 82  ILE n 
1 83  GLU n 
1 84  ARG n 
1 85  ARG n 
1 86  GLU n 
1 87  GLY n 
1 88  THR n 
1 89  ASP n 
1 90  ILE n 
1 91  CYS n 
1 92  TYR n 
1 93  PRO n 
1 94  GLY n 
1 95  ARG n 
1 96  PHE n 
1 97  THR n 
1 98  ASN n 
1 99  GLU n 
1 100 GLU n 
1 101 SER n 
1 102 LEU n 
1 103 ARG n 
1 104 GLN n 
1 105 ILE n 
1 106 LEU n 
1 107 ARG n 
1 108 ARG n 
1 109 SER n 
1 110 GLY n 
1 111 GLY n 
1 112 ILE n 
1 113 GLY n 
1 114 LYS n 
1 115 GLU n 
1 116 SER n 
1 117 MET n 
1 118 GLY n 
1 119 PHE n 
1 120 THR n 
1 121 TYR n 
1 122 SER n 
1 123 GLY n 
1 124 ILE n 
1 125 ARG n 
1 126 THR n 
1 127 ASN n 
1 128 GLY n 
1 129 ALA n 
1 130 THR n 
1 131 SER n 
1 132 ALA n 
1 133 CYS n 
1 134 THR n 
1 135 ARG n 
1 136 SER n 
1 137 GLY n 
1 138 SER n 
1 139 SER n 
1 140 PHE n 
1 141 TYR n 
1 142 ALA n 
1 143 GLU n 
1 144 MET n 
1 145 LYS n 
1 146 TRP n 
1 147 LEU n 
1 148 LEU n 
1 149 SER n 
1 150 ASN n 
1 151 SER n 
1 152 ASP n 
1 153 ASN n 
1 154 ALA n 
1 155 ALA n 
1 156 PHE n 
1 157 PRO n 
1 158 GLN n 
1 159 MET n 
1 160 THR n 
1 161 LYS n 
1 162 ALA n 
1 163 TYR n 
1 164 ARG n 
1 165 ASN n 
1 166 PRO n 
1 167 ARG n 
1 168 ASN n 
1 169 LYS n 
1 170 PRO n 
1 171 ALA n 
1 172 LEU n 
1 173 ILE n 
1 174 ILE n 
1 175 TRP n 
1 176 GLY n 
1 177 VAL n 
1 178 HIS n 
1 179 HIS n 
1 180 SER n 
1 181 GLU n 
1 182 SER n 
1 183 VAL n 
1 184 SER n 
1 185 GLU n 
1 186 GLN n 
1 187 THR n 
1 188 LYS n 
1 189 LEU n 
1 190 TYR n 
1 191 GLY n 
1 192 SER n 
1 193 GLY n 
1 194 ASN n 
1 195 LYS n 
1 196 LEU n 
1 197 ILE n 
1 198 THR n 
1 199 VAL n 
1 200 ARG n 
1 201 SER n 
1 202 SER n 
1 203 LYS n 
1 204 TYR n 
1 205 GLN n 
1 206 GLN n 
1 207 SER n 
1 208 PHE n 
1 209 THR n 
1 210 PRO n 
1 211 ASN n 
1 212 PRO n 
1 213 GLY n 
1 214 ALA n 
1 215 ARG n 
1 216 ARG n 
1 217 ILE n 
1 218 ASP n 
1 219 PHE n 
1 220 HIS n 
1 221 TRP n 
1 222 LEU n 
1 223 LEU n 
1 224 LEU n 
1 225 ASP n 
1 226 PRO n 
1 227 ASN n 
1 228 ASP n 
1 229 THR n 
1 230 VAL n 
1 231 THR n 
1 232 PHE n 
1 233 THR n 
1 234 PHE n 
1 235 ASN n 
1 236 GLY n 
1 237 ALA n 
1 238 PHE n 
1 239 ILE n 
1 240 ALA n 
1 241 PRO n 
1 242 ASP n 
1 243 ARG n 
1 244 THR n 
1 245 SER n 
1 246 PHE n 
1 247 PHE n 
1 248 ARG n 
1 249 GLY n 
1 250 GLU n 
1 251 SER n 
1 252 LEU n 
1 253 GLY n 
1 254 VAL n 
1 255 GLN n 
1 256 SER n 
1 257 ASP n 
1 258 ALA n 
1 259 PRO n 
1 260 LEU n 
1 261 ASP n 
1 262 SER n 
1 263 SER n 
1 264 CYS n 
1 265 ARG n 
1 266 GLY n 
1 267 ASP n 
1 268 CYS n 
1 269 PHE n 
1 270 HIS n 
1 271 SER n 
1 272 GLY n 
1 273 GLY n 
1 274 THR n 
1 275 ILE n 
1 276 VAL n 
1 277 SER n 
1 278 SER n 
1 279 LEU n 
1 280 PRO n 
1 281 PHE n 
1 282 GLN n 
1 283 ASN n 
1 284 ILE n 
1 285 ASN n 
1 286 SER n 
1 287 ARG n 
1 288 THR n 
1 289 VAL n 
1 290 GLY n 
1 291 LYS n 
1 292 CYS n 
1 293 PRO n 
1 294 ARG n 
1 295 TYR n 
1 296 VAL n 
1 297 LYS n 
1 298 GLN n 
1 299 LYS n 
1 300 SER n 
1 301 LEU n 
1 302 LEU n 
1 303 LEU n 
1 304 ALA n 
1 305 THR n 
1 306 GLY n 
1 307 MET n 
1 308 ARG n 
1 309 ASN n 
1 310 VAL n 
1 311 PRO n 
1 312 GLU n 
1 313 LYS n 
1 314 PRO n 
1 315 LYS n 
1 316 PRO n 
1 317 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  ASN n 
2 13  GLY n 
2 14  TRP n 
2 15  GLU n 
2 16  GLY n 
2 17  LEU n 
2 18  ILE n 
2 19  ASN n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  PHE n 
2 25  ARG n 
2 26  HIS n 
2 27  GLN n 
2 28  ASN n 
2 29  ALA n 
2 30  GLN n 
2 31  GLY n 
2 32  GLU n 
2 33  GLY n 
2 34  THR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  TYR n 
2 39  LYS n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  SER n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLN n 
2 48  ILE n 
2 49  THR n 
2 50  GLY n 
2 51  LYS n 
2 52  LEU n 
2 53  ASN n 
2 54  ARG n 
2 55  LEU n 
2 56  ILE n 
2 57  GLY n 
2 58  LYS n 
2 59  THR n 
2 60  ASN n 
2 61  GLN n 
2 62  GLN n 
2 63  PHE n 
2 64  GLU n 
2 65  LEU n 
2 66  ILE n 
2 67  ASP n 
2 68  ASN n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  GLU n 
2 73  ILE n 
2 74  GLU n 
2 75  GLN n 
2 76  GLN n 
2 77  ILE n 
2 78  GLY n 
2 79  ASN n 
2 80  VAL n 
2 81  ILE n 
2 82  ASN n 
2 83  TRP n 
2 84  THR n 
2 85  ARG n 
2 86  ASP n 
2 87  ALA n 
2 88  MET n 
2 89  THR n 
2 90  GLU n 
2 91  ILE n 
2 92  TRP n 
2 93  SER n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 ALA n 
2 102 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLN n 
2 106 HIS n 
2 107 THR n 
2 108 ILE n 
2 109 ASP n 
2 110 LEU n 
2 111 ALA n 
2 112 ASP n 
2 113 SER n 
2 114 GLU n 
2 115 MET n 
2 116 SER n 
2 117 LYS n 
2 118 LEU n 
2 119 TYR n 
2 120 GLU n 
2 121 ARG n 
2 122 VAL n 
2 123 LYS n 
2 124 LYS n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 GLU n 
2 129 ASN n 
2 130 ALA n 
2 131 GLU n 
2 132 GLU n 
2 133 ASP n 
2 134 GLY n 
2 135 THR n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 ILE n 
2 141 PHE n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASP n 
2 146 ASP n 
2 147 GLN n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 ILE n 
2 153 ARG n 
2 154 ASN n 
2 155 ASN n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 HIS n 
2 160 THR n 
2 161 GLN n 
2 162 TYR n 
2 163 ARG n 
2 164 THR n 
2 165 GLU n 
2 166 SER n 
2 167 LEU n 
2 168 GLN n 
2 169 ASN n 
2 170 ARG n 
2 171 ILE n 
2 172 GLN n 
2 173 ILE n 
2 174 ASP n 
2 175 SER n 
2 176 GLY n 
2 177 ARG n 
2 178 LEU n 
2 179 VAL n 
2 180 PRO n 
2 181 ARG n 
2 182 GLY 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 ? ? ? ? ? ?  ? 'A/New York/107/2003'                       ? ? ? ? 'Influenza A virus' 490450 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? ? ? HA ? 'A/environment/New York/30732-1/2005(H7N2)' ? ? ? ? 'Influenza A virus' 490450 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP B7NY59_9INFA B7NY59 1 
;GDKICLGHHAVANGTKVNTLTERGIEVVNATETVETTNIKKICTQGKRPTDLGQCGLLGTLIGPPQCDQFLEFSSDLIIE
RREGTDICYPGRFTNEESLRQILRRSGGIGKESMGFTYSGIRTNGATSACTRSGSSFYAEMKWLLSNSDNAAFPQMTKAY
RNPRNKPALIIWGVHHSESVSEQTKLYGSGNKLITVRSSKYQQSFTPSPGARRIDFHWLLLDPNDTVTFTFNGAFIAPDR
ASFFRGESLGVQSDAPLDSSCRGDCFHSGGTIVSSLPFQNINSRTVGKCPRYIKQKSLLLATGMRNVPEKPKPR
;
14  ? 
2 UNP B7NYS1_9INFA B7NYS1 2 
;GLFGAIAGFIENGWEGLINGWYGFRHQNAQGEGTAADYKSTQSAIDQITGKLNRLIGKTNQQFELIDNEFNEIEQQIGNV
INWTRDAMTEIWSYNAELLVAMENQHTIDLADSEMSKLYERVKKQLRENAEEDGTGCFEIFHKCDDQCMESIRNNTYDHT
QYRTESLQNRIQIDSVKL
;
332 ? 
# 
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 3M5H A 4 ? 317 ? B7NY59 14  ? 327 ? 10 330 
2 2 3M5H B 1 ? 178 ? B7NYS1 332 ? 509 ? 1  178 
3 1 3M5H C 4 ? 317 ? B7NY59 14  ? 327 ? 10 330 
4 2 3M5H D 1 ? 178 ? B7NYS1 332 ? 509 ? 1  178 
5 1 3M5H E 4 ? 317 ? B7NY59 14  ? 327 ? 10 330 
6 2 3M5H F 1 ? 178 ? B7NYS1 332 ? 509 ? 1  178 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3M5H ALA A 1   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 7   1  
1 3M5H ASP A 2   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 8   2  
1 3M5H PRO A 3   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 9   3  
1 3M5H ASN A 211 ? UNP B7NY59 SER 221 'SEE REMARK 999' 216 4  
1 3M5H THR A 244 ? UNP B7NY59 ALA 254 'SEE REMARK 999' 257 5  
1 3M5H VAL A 296 ? UNP B7NY59 ILE 306 'SEE REMARK 999' 309 6  
2 3M5H GLY B 176 ? UNP B7NYS1 VAL 507 'SEE REMARK 999' 176 7  
2 3M5H ARG B 177 ? UNP B7NYS1 LYS 508 'SEE REMARK 999' 177 8  
2 3M5H VAL B 179 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 179 9  
2 3M5H PRO B 180 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 180 10 
2 3M5H ARG B 181 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 181 11 
2 3M5H GLY B 182 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 182 12 
3 3M5H ALA C 1   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 7   13 
3 3M5H ASP C 2   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 8   14 
3 3M5H PRO C 3   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 9   15 
3 3M5H ASN C 211 ? UNP B7NY59 SER 221 'SEE REMARK 999' 216 16 
3 3M5H THR C 244 ? UNP B7NY59 ALA 254 'SEE REMARK 999' 257 17 
3 3M5H VAL C 296 ? UNP B7NY59 ILE 306 'SEE REMARK 999' 309 18 
4 3M5H GLY D 176 ? UNP B7NYS1 VAL 507 'SEE REMARK 999' 176 19 
4 3M5H ARG D 177 ? UNP B7NYS1 LYS 508 'SEE REMARK 999' 177 20 
4 3M5H VAL D 179 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 179 21 
4 3M5H PRO D 180 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 180 22 
4 3M5H ARG D 181 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 181 23 
4 3M5H GLY D 182 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 182 24 
5 3M5H ALA E 1   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 7   25 
5 3M5H ASP E 2   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 8   26 
5 3M5H PRO E 3   ? UNP B7NY59 ?   ?   'EXPRESSION TAG' 9   27 
5 3M5H ASN E 211 ? UNP B7NY59 SER 221 'SEE REMARK 999' 216 28 
5 3M5H THR E 244 ? UNP B7NY59 ALA 254 'SEE REMARK 999' 257 29 
5 3M5H VAL E 296 ? UNP B7NY59 ILE 306 'SEE REMARK 999' 309 30 
6 3M5H GLY F 176 ? UNP B7NYS1 VAL 507 'SEE REMARK 999' 176 31 
6 3M5H ARG F 177 ? UNP B7NYS1 LYS 508 'SEE REMARK 999' 177 32 
6 3M5H VAL F 179 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 179 33 
6 3M5H PRO F 180 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 180 34 
6 3M5H ARG F 181 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 181 35 
6 3M5H GLY F 182 ? UNP B7NYS1 ?   ?   'EXPRESSION TAG' 182 36 
# 
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 
GAL D-saccharide        . BETA-D-GALACTOSE       ?                               'C6 H12 O6'      180.156 
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  
GOL non-polymer         . GLYCEROL               'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                               'C8 H15 N O6'    221.208 
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 
SIA non-polymer         . 'O-SIALIC ACID'        ?                               'C11 H19 N O9'   309.270 
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.entry_id          3M5H 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.95 
_exptl_crystal.density_percent_sol   58.35 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'microbatch under oil' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.2 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;20% PEG 3350, 0.2 M magnesium chloride at pH 7.2 
, microbatch under oil, temperature 298K
;
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR 225' 
_diffrn_detector.pdbx_collection_date   2008-11-25 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 22-BM' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   22-BM 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     3M5H 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            2.70 
_reflns.number_obs                   54617 
_reflns.number_all                   55091 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.146 
_reflns.pdbx_netI_over_sigmaI        24.3 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.8 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.70 
_reflns_shell.d_res_low              2.8 
_reflns_shell.percent_possible_all   94.6 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.486 
_reflns_shell.meanI_over_sigI_obs    1.7 
_reflns_shell.pdbx_redundancy        5.5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3M5H 
_refine.ls_number_reflns_obs                     51770 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             30.00 
_refine.ls_d_res_high                            2.70 
_refine.ls_percent_reflns_obs                    98.49 
_refine.ls_R_factor_obs                          0.21692 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21439 
_refine.ls_R_factor_R_free                       0.26365 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2769 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.920 
_refine.correlation_coeff_Fo_to_Fc_free          0.878 
_refine.B_iso_mean                               18.061 
_refine.aniso_B[1][1]                            4.36 
_refine.aniso_B[2][2]                            0.18 
_refine.aniso_B[3][3]                            -4.55 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.987 
_refine.pdbx_overall_ESU_R_Free                  0.349 
_refine.overall_SU_ML                            0.258 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             28.060 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11359 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         259 
_refine_hist.number_atoms_solvent             257 
_refine_hist.number_atoms_total               11875 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        30.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.006  0.021  ? 11861 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          0.974  1.962  ? 16037 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.114  5.000  ? 1441  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.749 24.359 ? 585   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.623 15.000 ? 1999  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.715 15.000 ? 87    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.062  0.200  ? 1761  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.003  0.021  ? 9018  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.593  3.000  ? 7142  'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.258  5.000  ? 11484 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.528  8.000  ? 4719  'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.295  11.000 ? 4553  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.700 
_refine_ls_shell.d_res_low                        2.770 
_refine_ls_shell.number_reflns_R_work             3157 
_refine_ls_shell.R_factor_R_work                  0.298 
_refine_ls_shell.percent_reflns_obs               83.49 
_refine_ls_shell.R_factor_R_free                  0.403 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             160 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  3M5H 
_struct.title                     'Crystal structure of a H7 influenza virus hemagglutinin complexed with 3SLN' 
_struct.pdbx_descriptor           Hemagglutinin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M5H 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Influenza virus, Hemagglutinin, 3SLN, Envelope protein, Fusion protein, Host cell membrane, Host membrane, Membrane, Transmembrane, Virion, 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 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 5 ? 
J  N N 5 ? 
K  N N 5 ? 
L  N N 5 ? 
M  N N 6 ? 
N  N N 6 ? 
O  N N 3 ? 
P  N N 4 ? 
Q  N N 5 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 6 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 5 ? 
X  N N 5 ? 
Y  N N 5 ? 
Z  N N 6 ? 
AA N N 7 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
FA N N 7 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  LEU A 61  ? GLY A 66  ? LEU A 67  GLY A 72  1 ? 6  
HELX_P HELX_P2  2  PRO A 67  ? LEU A 74  ? PRO A 73  LEU A 80  5 ? 8  
HELX_P HELX_P3  3  ASN A 98  ? ARG A 108 ? ASN A 104 ARG A 114 1 ? 11 
HELX_P HELX_P4  4  SER A 182 ? GLY A 191 ? SER A 187 GLY A 196 1 ? 10 
HELX_P HELX_P5  5  ASP B 37  ? ILE B 56  ? ASP B 37  ILE B 56  1 ? 20 
HELX_P HELX_P6  6  GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P7  7  ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 
HELX_P HELX_P8  8  ASP B 158 ? GLN B 161 ? ASP B 158 GLN B 161 5 ? 4  
HELX_P HELX_P9  9  TYR B 162 ? ILE B 171 ? TYR B 162 ILE B 171 1 ? 10 
HELX_P HELX_P10 10 LEU C 61  ? GLY C 66  ? LEU C 67  GLY C 72  1 ? 6  
HELX_P HELX_P11 11 PRO C 67  ? LEU C 74  ? PRO C 73  LEU C 80  5 ? 8  
HELX_P HELX_P12 12 ASN C 98  ? ARG C 108 ? ASN C 104 ARG C 114 1 ? 11 
HELX_P HELX_P13 13 SER C 182 ? TYR C 190 ? SER C 187 TYR C 195 1 ? 9  
HELX_P HELX_P14 14 ASP D 37  ? ILE D 56  ? ASP D 37  ILE D 56  1 ? 20 
HELX_P HELX_P15 15 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P16 16 ASP D 145 ? ASN D 154 ? ASP D 145 ASN D 154 1 ? 10 
HELX_P HELX_P17 17 ASP D 158 ? GLN D 161 ? ASP D 158 GLN D 161 5 ? 4  
HELX_P HELX_P18 18 TYR D 162 ? GLN D 172 ? TYR D 162 GLN D 172 1 ? 11 
HELX_P HELX_P19 19 LEU E 61  ? GLY E 66  ? LEU E 67  GLY E 72  1 ? 6  
HELX_P HELX_P20 20 PRO E 67  ? LEU E 74  ? PRO E 73  LEU E 80  5 ? 8  
HELX_P HELX_P21 21 ASN E 98  ? ARG E 108 ? ASN E 104 ARG E 114 1 ? 11 
HELX_P HELX_P22 22 SER E 182 ? TYR E 190 ? SER E 187 TYR E 195 1 ? 9  
HELX_P HELX_P23 23 ASP F 37  ? ILE F 56  ? ASP F 37  ILE F 56  1 ? 20 
HELX_P HELX_P24 24 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P25 25 ASP F 145 ? ASN F 154 ? ASP F 145 ASN F 154 1 ? 10 
HELX_P HELX_P26 26 ASP F 158 ? ARG F 170 ? ASP F 158 ARG F 170 1 ? 13 
# 
_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 
disulf1  disulf ? ? A CYS 8   SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf2  disulf ? ? A CYS 46  SG  ? ? ? 1_555 A CYS 264 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf3  disulf ? ? A CYS 58  SG  ? ? ? 1_555 A CYS 70  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf4  disulf ? ? A CYS 91  SG  ? ? ? 1_555 A CYS 133 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf5  disulf ? ? A CYS 268 SG  ? ? ? 1_555 A CYS 292 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf6  disulf ? ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf7  disulf ? ? C CYS 8   SG  ? ? ? 1_555 D CYS 137 SG ? ? C CYS 14  D CYS 137 1_555 ? ? ? ? ? ? ? 2.021 ? 
disulf8  disulf ? ? C CYS 46  SG  ? ? ? 1_555 C CYS 264 SG ? ? C CYS 52  C CYS 277 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf9  disulf ? ? C CYS 58  SG  ? ? ? 1_555 C CYS 70  SG ? ? C CYS 64  C CYS 76  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf10 disulf ? ? C CYS 91  SG  ? ? ? 1_555 C CYS 133 SG ? ? C CYS 97  C CYS 139 1_555 ? ? ? ? ? ? ? 2.029 ? 
disulf11 disulf ? ? C CYS 268 SG  ? ? ? 1_555 C CYS 292 SG ? ? C CYS 281 C CYS 305 1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf12 disulf ? ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf13 disulf ? ? E CYS 8   SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14  F CYS 137 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf14 disulf ? ? E CYS 46  SG  ? ? ? 1_555 E CYS 264 SG ? ? E CYS 52  E CYS 277 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf15 disulf ? ? E CYS 58  SG  ? ? ? 1_555 E CYS 70  SG ? ? E CYS 64  E CYS 76  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf16 disulf ? ? E CYS 91  SG  ? ? ? 1_555 E CYS 133 SG ? ? E CYS 97  E CYS 139 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf17 disulf ? ? E CYS 268 SG  ? ? ? 1_555 E CYS 292 SG ? ? E CYS 281 E CYS 305 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf18 disulf ? ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.043 ? 
covale1  covale ? ? A ASN 32  ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 38  A NAG 331 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale2  covale ? ? C ASN 32  ND2 ? ? ? 1_555 Q NAG .   C1 ? ? C ASN 38  C NAG 331 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale3  covale ? ? E ASN 32  ND2 ? ? ? 1_555 X NAG .   C1 ? ? E ASN 38  E NAG 331 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale4  covale ? ? D ASN 82  ND2 ? ? ? 1_555 S NAG .   C1 ? ? D ASN 82  D NAG 183 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale5  covale ? ? B ASN 82  ND2 ? ? ? 1_555 K NAG .   C1 ? ? B ASN 82  B NAG 183 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale6  covale ? ? Q NAG .   O4  ? ? ? 1_555 R NAG .   C1 ? ? C NAG 331 C NAG 332 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale7  covale ? ? I NAG .   O4  ? ? ? 1_555 H GAL .   C1 ? ? A NAG 3   A GAL 2   1_555 ? ? ? ? ? ? ? 1.447 ? 
covale8  covale ? ? W NAG .   O4  ? ? ? 1_555 V GAL .   C1 ? ? E NAG 3   E GAL 2   1_555 ? ? ? ? ? ? ? 1.451 ? 
covale9  covale ? ? F ASN 82  ND2 ? ? ? 1_555 Y NAG .   C1 ? ? F ASN 82  F NAG 183 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale10 covale ? ? O SIA .   C2  ? ? ? 1_555 P GAL .   O3 ? ? C SIA 1   C GAL 2   1_555 ? ? ? ? ? ? ? 1.452 ? 
covale11 covale ? ? G SIA .   C2  ? ? ? 1_555 H GAL .   O3 ? ? A SIA 1   A GAL 2   1_555 ? ? ? ? ? ? ? 1.452 ? 
covale12 covale ? ? U SIA .   C2  ? ? ? 1_555 V GAL .   O3 ? ? E SIA 1   E GAL 2   1_555 ? ? ? ? ? ? ? 1.453 ? 
covale13 covale ? ? K NAG .   O4  ? ? ? 1_555 L NAG .   C1 ? ? B NAG 183 B NAG 184 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale14 covale ? ? O SIA .   O6  ? ? ? 1_555 P GAL .   O3 ? ? C SIA 1   C GAL 2   1_555 ? ? ? ? ? ? ? 1.822 ? 
covale15 covale ? ? U SIA .   O6  ? ? ? 1_555 V GAL .   O3 ? ? E SIA 1   E GAL 2   1_555 ? ? ? ? ? ? ? 1.915 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 5 ? 
B  ? 2 ? 
C  ? 2 ? 
D  ? 3 ? 
E  ? 2 ? 
F  ? 3 ? 
G  ? 3 ? 
H  ? 5 ? 
I  ? 2 ? 
J  ? 4 ? 
K  ? 4 ? 
L  ? 5 ? 
M  ? 2 ? 
N  ? 2 ? 
O  ? 3 ? 
P  ? 2 ? 
Q  ? 3 ? 
R  ? 6 ? 
S  ? 5 ? 
T  ? 2 ? 
U  ? 4 ? 
V  ? 4 ? 
W  ? 5 ? 
X  ? 2 ? 
Y  ? 2 ? 
Z  ? 3 ? 
AA ? 2 ? 
AB ? 3 ? 
AC ? 3 ? 
AD ? 2 ? 
AE ? 4 ? 
AF ? 4 ? 
AG ? 4 ? 
# 
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 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
B  1 2 ? anti-parallel 
C  1 2 ? anti-parallel 
D  1 2 ? parallel      
D  2 3 ? parallel      
E  1 2 ? parallel      
F  1 2 ? parallel      
F  2 3 ? parallel      
G  1 2 ? anti-parallel 
G  2 3 ? anti-parallel 
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
H  3 4 ? anti-parallel 
H  4 5 ? anti-parallel 
I  1 2 ? anti-parallel 
J  1 2 ? anti-parallel 
J  2 3 ? anti-parallel 
J  3 4 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
K  3 4 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
L  3 4 ? anti-parallel 
L  4 5 ? anti-parallel 
M  1 2 ? anti-parallel 
N  1 2 ? anti-parallel 
O  1 2 ? parallel      
O  2 3 ? parallel      
P  1 2 ? parallel      
Q  1 2 ? parallel      
Q  2 3 ? parallel      
R  1 2 ? anti-parallel 
R  2 3 ? anti-parallel 
R  3 4 ? anti-parallel 
R  4 5 ? anti-parallel 
R  5 6 ? anti-parallel 
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
S  4 5 ? anti-parallel 
T  1 2 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
U  3 4 ? anti-parallel 
V  1 2 ? anti-parallel 
V  2 3 ? anti-parallel 
V  3 4 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
W  4 5 ? anti-parallel 
X  1 2 ? anti-parallel 
Y  1 2 ? anti-parallel 
Z  1 2 ? parallel      
Z  2 3 ? parallel      
AA 1 2 ? parallel      
AB 1 2 ? parallel      
AB 2 3 ? parallel      
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AD 1 2 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AE 3 4 ? anti-parallel 
AF 1 2 ? anti-parallel 
AF 2 3 ? anti-parallel 
AF 3 4 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
AG 3 4 ? 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 
A  1 GLY B 31  ? ALA B 36  ? GLY B 31  ALA B 36  
A  2 TYR B 22  ? ASN B 28  ? TYR B 22  ASN B 28  
A  3 LYS A 6   ? HIS A 11  ? LYS A 12  HIS A 17  
A  4 CYS B 137 ? ILE B 140 ? CYS B 137 ILE B 140 
A  5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 
B  1 THR A 18  ? VAL A 20  ? THR A 24  VAL A 26  
B  2 ILE A 28  ? VAL A 30  ? ILE A 34  VAL A 36  
C  1 ALA A 33  ? GLU A 35  ? ALA A 39  GLU A 41  
C  2 LEU A 302 ? ALA A 304 ? LEU A 315 ALA A 317 
D  1 VAL A 37  ? GLU A 38  ? VAL A 43  GLU A 44  
D  2 PHE A 281 ? GLN A 282 ? PHE A 294 GLN A 295 
D  3 ARG A 294 ? TYR A 295 ? ARG A 307 TYR A 308 
E  1 ILE A 45  ? CYS A 46  ? ILE A 51  CYS A 52  
E  2 LEU A 260 ? ASP A 261 ? LEU A 274 ASP A 275 
F  1 PRO A 52  ? ASP A 54  ? PRO A 58  ASP A 60  
F  2 LEU A 80  ? GLU A 83  ? LEU A 86  GLU A 89  
F  3 LEU A 252 ? GLN A 255 ? LEU A 266 GLN A 269 
G  1 PHE A 76  ? SER A 77  ? PHE A 82  SER A 83  
G  2 GLY A 111 ? SER A 116 ? GLY A 117 SER A 122 
G  3 ARG A 243 ? PHE A 247 ? ARG A 256 PHE A 260 
H  1 ARG A 125 ? GLY A 128 ? ARG A 131 GLY A 134 
H  2 MET A 144 ? LEU A 148 ? MET A 151 LEU A 155 
H  3 PHE A 238 ? PRO A 241 ? PHE A 251 PRO A 254 
H  4 ALA A 171 ? HIS A 179 ? ALA A 176 HIS A 184 
H  5 ARG A 216 ? LEU A 224 ? ARG A 229 LEU A 237 
I  1 THR A 130 ? THR A 134 ? THR A 136 THR A 140 
I  2 SER A 138 ? SER A 139 ? SER A 145 SER A 146 
J  1 MET A 159 ? ARG A 164 ? MET A 164 ARG A 169 
J  2 THR A 229 ? PHE A 234 ? THR A 242 PHE A 247 
J  3 ILE A 197 ? ARG A 200 ? ILE A 202 ARG A 205 
J  4 GLN A 205 ? PHE A 208 ? GLN A 210 PHE A 213 
K  1 GLY A 273 ? THR A 274 ? GLY A 286 THR A 287 
K  2 CYS A 268 ? HIS A 270 ? CYS A 281 HIS A 283 
K  3 VAL A 289 ? CYS A 292 ? VAL A 302 CYS A 305 
K  4 GLN B 61  ? PHE B 63  ? GLN B 61  PHE B 63  
L  1 GLY D 31  ? ALA D 36  ? GLY D 31  ALA D 36  
L  2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
L  3 LYS C 6   ? HIS C 11  ? LYS C 12  HIS C 17  
L  4 CYS D 137 ? ILE D 140 ? CYS D 137 ILE D 140 
L  5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
M  1 THR C 18  ? VAL C 20  ? THR C 24  VAL C 26  
M  2 ILE C 28  ? VAL C 30  ? ILE C 34  VAL C 36  
N  1 ALA C 33  ? GLU C 35  ? ALA C 39  GLU C 41  
N  2 LEU C 302 ? ALA C 304 ? LEU C 315 ALA C 317 
O  1 VAL C 37  ? GLU C 38  ? VAL C 43  GLU C 44  
O  2 PHE C 281 ? GLN C 282 ? PHE C 294 GLN C 295 
O  3 ARG C 294 ? TYR C 295 ? ARG C 307 TYR C 308 
P  1 ILE C 45  ? CYS C 46  ? ILE C 51  CYS C 52  
P  2 LEU C 260 ? ASP C 261 ? LEU C 274 ASP C 275 
Q  1 PRO C 52  ? ASP C 54  ? PRO C 58  ASP C 60  
Q  2 LEU C 80  ? GLU C 83  ? LEU C 86  GLU C 89  
Q  3 LEU C 252 ? GLN C 255 ? LEU C 266 GLN C 269 
R  1 PHE C 76  ? SER C 77  ? PHE C 82  SER C 83  
R  2 GLY C 111 ? SER C 116 ? GLY C 117 SER C 122 
R  3 ARG C 243 ? PHE C 247 ? ARG C 256 PHE C 260 
R  4 ALA C 171 ? HIS C 179 ? ALA C 176 HIS C 184 
R  5 PHE C 238 ? PRO C 241 ? PHE C 251 PRO C 254 
R  6 MET C 144 ? TRP C 146 ? MET C 151 TRP C 153 
S  1 PHE C 76  ? SER C 77  ? PHE C 82  SER C 83  
S  2 GLY C 111 ? SER C 116 ? GLY C 117 SER C 122 
S  3 ARG C 243 ? PHE C 247 ? ARG C 256 PHE C 260 
S  4 ALA C 171 ? HIS C 179 ? ALA C 176 HIS C 184 
S  5 ARG C 216 ? LEU C 224 ? ARG C 229 LEU C 237 
T  1 THR C 130 ? THR C 134 ? THR C 136 THR C 140 
T  2 SER C 138 ? SER C 139 ? SER C 145 SER C 146 
U  1 MET C 159 ? ARG C 164 ? MET C 164 ARG C 169 
U  2 THR C 229 ? PHE C 234 ? THR C 242 PHE C 247 
U  3 ILE C 197 ? ARG C 200 ? ILE C 202 ARG C 205 
U  4 GLN C 205 ? PHE C 208 ? GLN C 210 PHE C 213 
V  1 GLY C 273 ? ILE C 275 ? GLY C 286 ILE C 288 
V  2 CYS C 268 ? HIS C 270 ? CYS C 281 HIS C 283 
V  3 VAL C 289 ? LYS C 291 ? VAL C 302 LYS C 304 
V  4 GLN D 62  ? PHE D 63  ? GLN D 62  PHE D 63  
W  1 GLY F 31  ? ALA F 36  ? GLY F 31  ALA F 36  
W  2 TYR F 22  ? ASN F 28  ? TYR F 22  ASN F 28  
W  3 LYS E 6   ? HIS E 11  ? LYS E 12  HIS E 17  
W  4 CYS F 137 ? ILE F 140 ? CYS F 137 ILE F 140 
W  5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
X  1 THR E 18  ? VAL E 20  ? THR E 24  VAL E 26  
X  2 ILE E 28  ? VAL E 30  ? ILE E 34  VAL E 36  
Y  1 ALA E 33  ? GLU E 35  ? ALA E 39  GLU E 41  
Y  2 LEU E 302 ? ALA E 304 ? LEU E 315 ALA E 317 
Z  1 VAL E 37  ? GLU E 38  ? VAL E 43  GLU E 44  
Z  2 PHE E 281 ? GLN E 282 ? PHE E 294 GLN E 295 
Z  3 ARG E 294 ? TYR E 295 ? ARG E 307 TYR E 308 
AA 1 ILE E 45  ? CYS E 46  ? ILE E 51  CYS E 52  
AA 2 LEU E 260 ? ASP E 261 ? LEU E 274 ASP E 275 
AB 1 PRO E 52  ? ASP E 54  ? PRO E 58  ASP E 60  
AB 2 LEU E 80  ? GLU E 83  ? LEU E 86  GLU E 89  
AB 3 LEU E 252 ? GLN E 255 ? LEU E 266 GLN E 269 
AC 1 PHE E 76  ? SER E 77  ? PHE E 82  SER E 83  
AC 2 GLY E 111 ? SER E 116 ? GLY E 117 SER E 122 
AC 3 ARG E 243 ? PHE E 247 ? ARG E 256 PHE E 260 
AD 1 THR E 130 ? THR E 134 ? THR E 136 THR E 140 
AD 2 SER E 138 ? SER E 139 ? SER E 145 SER E 146 
AE 1 MET E 144 ? TRP E 146 ? MET E 151 TRP E 153 
AE 2 PHE E 238 ? PRO E 241 ? PHE E 251 PRO E 254 
AE 3 ALA E 171 ? HIS E 179 ? ALA E 176 HIS E 184 
AE 4 ARG E 216 ? LEU E 224 ? ARG E 229 LEU E 237 
AF 1 MET E 159 ? ARG E 164 ? MET E 164 ARG E 169 
AF 2 THR E 229 ? PHE E 234 ? THR E 242 PHE E 247 
AF 3 ILE E 197 ? ARG E 200 ? ILE E 202 ARG E 205 
AF 4 GLN E 205 ? PHE E 208 ? GLN E 210 PHE E 213 
AG 1 GLY E 273 ? THR E 274 ? GLY E 286 THR E 287 
AG 2 CYS E 268 ? HIS E 270 ? CYS E 281 HIS E 283 
AG 3 THR E 288 ? LYS E 291 ? THR E 301 LYS E 304 
AG 4 GLN F 62  ? PHE F 63  ? GLN F 62  PHE F 63  
# 
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 
A  1 2 O ALA B 35  ? O ALA B 35  N PHE B 24  ? N PHE B 24  
A  2 3 O GLY B 23  ? O GLY B 23  N GLY A 10  ? N GLY A 16  
A  3 4 N ILE A 7   ? N ILE A 13  O PHE B 138 ? O PHE B 138 
A  4 5 O GLU B 139 ? O GLU B 139 N GLU B 131 ? N GLU B 131 
B  1 2 N VAL A 20  ? N VAL A 26  O ILE A 28  ? O ILE A 34  
C  1 2 N THR A 34  ? N THR A 40  O LEU A 303 ? O LEU A 316 
D  1 2 N GLU A 38  ? N GLU A 44  O PHE A 281 ? O PHE A 294 
D  2 3 N GLN A 282 ? N GLN A 295 O ARG A 294 ? O ARG A 307 
E  1 2 N ILE A 45  ? N ILE A 51  O ASP A 261 ? O ASP A 275 
F  1 2 N THR A 53  ? N THR A 59  O ILE A 82  ? O ILE A 88  
F  2 3 N ILE A 81  ? N ILE A 87  O LEU A 252 ? O LEU A 266 
G  1 2 N PHE A 76  ? N PHE A 82  O ILE A 112 ? O ILE A 118 
G  2 3 N GLY A 113 ? N GLY A 119 O PHE A 246 ? O PHE A 259 
H  1 2 N ARG A 125 ? N ARG A 131 O LEU A 148 ? O LEU A 155 
H  2 3 N LYS A 145 ? N LYS A 152 O ALA A 240 ? O ALA A 253 
H  3 4 O ILE A 239 ? O ILE A 252 N GLY A 176 ? N GLY A 181 
H  4 5 N ALA A 171 ? N ALA A 176 O LEU A 224 ? O LEU A 237 
I  1 2 N THR A 130 ? N THR A 136 O SER A 139 ? O SER A 146 
J  1 2 N LYS A 161 ? N LYS A 166 O PHE A 232 ? O PHE A 245 
J  2 3 O THR A 233 ? O THR A 246 N THR A 198 ? N THR A 203 
J  3 4 N ILE A 197 ? N ILE A 202 O PHE A 208 ? O PHE A 213 
K  1 2 O GLY A 273 ? O GLY A 286 N HIS A 270 ? N HIS A 283 
K  2 3 N PHE A 269 ? N PHE A 282 O VAL A 289 ? O VAL A 302 
K  3 4 N GLY A 290 ? N GLY A 303 O PHE B 63  ? O PHE B 63  
L  1 2 O ALA D 35  ? O ALA D 35  N PHE D 24  ? N PHE D 24  
L  2 3 O ARG D 25  ? O ARG D 25  N CYS C 8   ? N CYS C 14  
L  3 4 N ILE C 7   ? N ILE C 13  O PHE D 138 ? O PHE D 138 
L  4 5 O GLU D 139 ? O GLU D 139 N GLU D 131 ? N GLU D 131 
M  1 2 N VAL C 20  ? N VAL C 26  O ILE C 28  ? O ILE C 34  
N  1 2 N THR C 34  ? N THR C 40  O LEU C 303 ? O LEU C 316 
O  1 2 N GLU C 38  ? N GLU C 44  O PHE C 281 ? O PHE C 294 
O  2 3 N GLN C 282 ? N GLN C 295 O ARG C 294 ? O ARG C 307 
P  1 2 N ILE C 45  ? N ILE C 51  O ASP C 261 ? O ASP C 275 
Q  1 2 N THR C 53  ? N THR C 59  O ILE C 82  ? O ILE C 88  
Q  2 3 N GLU C 83  ? N GLU C 89  O VAL C 254 ? O VAL C 268 
R  1 2 N PHE C 76  ? N PHE C 82  O ILE C 112 ? O ILE C 118 
R  2 3 N GLY C 113 ? N GLY C 119 O PHE C 246 ? O PHE C 259 
R  3 4 O SER C 245 ? O SER C 258 N LEU C 172 ? N LEU C 177 
R  4 5 N GLY C 176 ? N GLY C 181 O ILE C 239 ? O ILE C 252 
R  5 6 O ALA C 240 ? O ALA C 253 N LYS C 145 ? N LYS C 152 
S  1 2 N PHE C 76  ? N PHE C 82  O ILE C 112 ? O ILE C 118 
S  2 3 N GLY C 113 ? N GLY C 119 O PHE C 246 ? O PHE C 259 
S  3 4 O SER C 245 ? O SER C 258 N LEU C 172 ? N LEU C 177 
S  4 5 N ALA C 171 ? N ALA C 176 O LEU C 224 ? O LEU C 237 
T  1 2 N THR C 130 ? N THR C 136 O SER C 139 ? O SER C 146 
U  1 2 N LYS C 161 ? N LYS C 166 O PHE C 232 ? O PHE C 245 
U  2 3 O THR C 233 ? O THR C 246 N THR C 198 ? N THR C 203 
U  3 4 N ILE C 197 ? N ILE C 202 O PHE C 208 ? O PHE C 213 
V  1 2 O GLY C 273 ? O GLY C 286 N HIS C 270 ? N HIS C 283 
V  2 3 N PHE C 269 ? N PHE C 282 O VAL C 289 ? O VAL C 302 
V  3 4 N GLY C 290 ? N GLY C 303 O PHE D 63  ? O PHE D 63  
W  1 2 O ALA F 35  ? O ALA F 35  N PHE F 24  ? N PHE F 24  
W  2 3 O ARG F 25  ? O ARG F 25  N CYS E 8   ? N CYS E 14  
W  3 4 N ILE E 7   ? N ILE E 13  O PHE F 138 ? O PHE F 138 
W  4 5 O GLU F 139 ? O GLU F 139 N GLU F 131 ? N GLU F 131 
X  1 2 N THR E 18  ? N THR E 24  O VAL E 30  ? O VAL E 36  
Y  1 2 N THR E 34  ? N THR E 40  O LEU E 303 ? O LEU E 316 
Z  1 2 N GLU E 38  ? N GLU E 44  O PHE E 281 ? O PHE E 294 
Z  2 3 N GLN E 282 ? N GLN E 295 O ARG E 294 ? O ARG E 307 
AA 1 2 N ILE E 45  ? N ILE E 51  O ASP E 261 ? O ASP E 275 
AB 1 2 N THR E 53  ? N THR E 59  O ILE E 82  ? O ILE E 88  
AB 2 3 N GLU E 83  ? N GLU E 89  O VAL E 254 ? O VAL E 268 
AC 1 2 N PHE E 76  ? N PHE E 82  O ILE E 112 ? O ILE E 118 
AC 2 3 N GLY E 113 ? N GLY E 119 O PHE E 246 ? O PHE E 259 
AD 1 2 N THR E 130 ? N THR E 136 O SER E 139 ? O SER E 146 
AE 1 2 N LYS E 145 ? N LYS E 152 O ALA E 240 ? O ALA E 253 
AE 2 3 O ILE E 239 ? O ILE E 252 N GLY E 176 ? N GLY E 181 
AE 3 4 N ALA E 171 ? N ALA E 176 O LEU E 224 ? O LEU E 237 
AF 1 2 N LYS E 161 ? N LYS E 166 O PHE E 232 ? O PHE E 245 
AF 2 3 O THR E 233 ? O THR E 246 N THR E 198 ? N THR E 203 
AF 3 4 N ILE E 197 ? N ILE E 202 O PHE E 208 ? O PHE E 213 
AG 1 2 O GLY E 273 ? O GLY E 286 N HIS E 270 ? N HIS E 283 
AG 2 3 N PHE E 269 ? N PHE E 282 O VAL E 289 ? O VAL E 302 
AG 3 4 N GLY E 290 ? N GLY E 303 O PHE F 63  ? O PHE F 63  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SIA A 1'   
AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 3'   
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GAL A 2'   
AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SIA C 1'   
AC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE GAL C 2'   
AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SIA E 1'   
AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 3'   
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GAL E 2'   
AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 331' 
BC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG B 183' 
BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 184' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG C 331' 
BC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 332' 
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG D 183' 
BC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG E 331' 
BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG F 183' 
BC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL F 184' 
BC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL D 184' 
CC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL B 186' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 9 GAL H .   ? GAL A 2   . ? 1_555 ? 
2  AC1 9 TYR A 92  ? TYR A 98  . ? 1_555 ? 
3  AC1 9 ALA A 129 ? ALA A 135 . ? 1_555 ? 
4  AC1 9 THR A 130 ? THR A 136 . ? 1_555 ? 
5  AC1 9 SER A 131 ? SER A 137 . ? 1_555 ? 
6  AC1 9 HIS A 178 ? HIS A 183 . ? 1_555 ? 
7  AC1 9 GLU A 185 ? GLU A 190 . ? 1_555 ? 
8  AC1 9 LEU A 189 ? LEU A 194 . ? 1_555 ? 
9  AC1 9 ARG A 215 ? ARG A 220 . ? 1_555 ? 
10 AC2 1 GAL H .   ? GAL A 2   . ? 1_555 ? 
11 AC3 4 SIA G .   ? SIA A 1   . ? 1_555 ? 
12 AC3 4 NAG I .   ? NAG A 3   . ? 1_555 ? 
13 AC3 4 GLU A 185 ? GLU A 190 . ? 1_555 ? 
14 AC3 4 ARG A 215 ? ARG A 220 . ? 1_555 ? 
15 AC4 9 GAL P .   ? GAL C 2   . ? 1_555 ? 
16 AC4 9 TYR C 92  ? TYR C 98  . ? 1_555 ? 
17 AC4 9 ALA C 129 ? ALA C 135 . ? 1_555 ? 
18 AC4 9 THR C 130 ? THR C 136 . ? 1_555 ? 
19 AC4 9 SER C 131 ? SER C 137 . ? 1_555 ? 
20 AC4 9 HIS C 178 ? HIS C 183 . ? 1_555 ? 
21 AC4 9 GLU C 181 ? GLU C 186 . ? 1_555 ? 
22 AC4 9 GLU C 185 ? GLU C 190 . ? 1_555 ? 
23 AC4 9 ARG C 215 ? ARG C 220 . ? 1_555 ? 
24 AC5 2 SIA O .   ? SIA C 1   . ? 1_555 ? 
25 AC5 2 ARG C 215 ? ARG C 220 . ? 1_555 ? 
26 AC6 9 GAL V .   ? GAL E 2   . ? 1_555 ? 
27 AC6 9 TYR E 92  ? TYR E 98  . ? 1_555 ? 
28 AC6 9 ALA E 129 ? ALA E 135 . ? 1_555 ? 
29 AC6 9 THR E 130 ? THR E 136 . ? 1_555 ? 
30 AC6 9 SER E 131 ? SER E 137 . ? 1_555 ? 
31 AC6 9 LEU E 148 ? LEU E 155 . ? 1_555 ? 
32 AC6 9 HIS E 178 ? HIS E 183 . ? 1_555 ? 
33 AC6 9 GLU E 185 ? GLU E 190 . ? 1_555 ? 
34 AC6 9 LEU E 189 ? LEU E 194 . ? 1_555 ? 
35 AC7 1 GAL V .   ? GAL E 2   . ? 1_555 ? 
36 AC8 4 SIA U .   ? SIA E 1   . ? 1_555 ? 
37 AC8 4 NAG W .   ? NAG E 3   . ? 1_555 ? 
38 AC8 4 LYS E 188 ? LYS E 193 . ? 1_555 ? 
39 AC8 4 ARG E 215 ? ARG E 220 . ? 1_555 ? 
40 AC9 3 ASN A 32  ? ASN A 38  . ? 1_555 ? 
41 AC9 3 ALA A 33  ? ALA A 39  . ? 1_555 ? 
42 AC9 3 THR A 34  ? THR A 40  . ? 1_555 ? 
43 BC1 8 ARG A 287 ? ARG A 300 . ? 1_555 ? 
44 BC1 8 GLU B 72  ? GLU B 72  . ? 1_555 ? 
45 BC1 8 GLN B 75  ? GLN B 75  . ? 1_555 ? 
46 BC1 8 GLY B 78  ? GLY B 78  . ? 1_555 ? 
47 BC1 8 ASN B 79  ? ASN B 79  . ? 1_555 ? 
48 BC1 8 ASN B 82  ? ASN B 82  . ? 1_555 ? 
49 BC1 8 NAG L .   ? NAG B 184 . ? 1_555 ? 
50 BC1 8 ARG E 108 ? ARG E 114 . ? 1_555 ? 
51 BC2 3 GLU B 69  ? GLU B 69  . ? 1_555 ? 
52 BC2 3 GLU B 72  ? GLU B 72  . ? 1_555 ? 
53 BC2 3 NAG K .   ? NAG B 183 . ? 1_555 ? 
54 BC3 4 ASN C 32  ? ASN C 38  . ? 1_555 ? 
55 BC3 4 ALA C 33  ? ALA C 39  . ? 1_555 ? 
56 BC3 4 THR C 34  ? THR C 40  . ? 1_555 ? 
57 BC3 4 NAG R .   ? NAG C 332 . ? 1_555 ? 
58 BC4 1 NAG Q .   ? NAG C 331 . ? 1_555 ? 
59 BC5 4 GLU D 72  ? GLU D 72  . ? 1_555 ? 
60 BC5 4 GLN D 75  ? GLN D 75  . ? 1_555 ? 
61 BC5 4 ASN D 79  ? ASN D 79  . ? 1_555 ? 
62 BC5 4 ASN D 82  ? ASN D 82  . ? 1_555 ? 
63 BC6 2 ASN E 32  ? ASN E 38  . ? 1_555 ? 
64 BC6 2 THR E 34  ? THR E 40  . ? 1_555 ? 
65 BC7 5 ARG C 108 ? ARG C 114 . ? 1_555 ? 
66 BC7 5 GLU F 72  ? GLU F 72  . ? 1_555 ? 
67 BC7 5 GLN F 75  ? GLN F 75  . ? 1_555 ? 
68 BC7 5 ASN F 79  ? ASN F 79  . ? 1_555 ? 
69 BC7 5 ASN F 82  ? ASN F 82  . ? 1_555 ? 
70 BC8 6 TYR B 94  ? TYR B 94  . ? 1_555 ? 
71 BC8 6 GLU B 97  ? GLU B 97  . ? 1_555 ? 
72 BC8 6 LEU B 98  ? LEU B 98  . ? 1_555 ? 
73 BC8 6 ARG F 54  ? ARG F 54  . ? 1_555 ? 
74 BC8 6 LEU F 55  ? LEU F 55  . ? 1_555 ? 
75 BC8 6 LYS F 58  ? LYS F 58  . ? 1_555 ? 
76 BC9 6 ARG D 54  ? ARG D 54  . ? 1_555 ? 
77 BC9 6 LEU D 55  ? LEU D 55  . ? 1_555 ? 
78 BC9 6 LYS D 58  ? LYS D 58  . ? 1_555 ? 
79 BC9 6 TYR F 94  ? TYR F 94  . ? 1_555 ? 
80 BC9 6 GLU F 97  ? GLU F 97  . ? 1_555 ? 
81 BC9 6 LEU F 98  ? LEU F 98  . ? 1_555 ? 
82 CC1 5 ARG B 54  ? ARG B 54  . ? 1_555 ? 
83 CC1 5 LEU B 55  ? LEU B 55  . ? 1_555 ? 
84 CC1 5 LYS B 58  ? LYS B 58  . ? 1_555 ? 
85 CC1 5 GLU D 97  ? GLU D 97  . ? 1_555 ? 
86 CC1 5 LEU D 98  ? LEU D 98  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3M5H 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3M5H 
_atom_sites.fract_transf_matrix[1][1]   0.014750 
_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]   0.008569 
_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]   0.004003 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_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   . GLY A  1 4   ? -12.260 3.493   -20.252 1.00 12.66  ? 10  GLY A N   1 
ATOM   2     C CA  . GLY A  1 4   ? -12.845 2.143   -20.508 1.00 12.45  ? 10  GLY A CA  1 
ATOM   3     C C   . GLY A  1 4   ? -13.546 1.558   -19.293 1.00 12.13  ? 10  GLY A C   1 
ATOM   4     O O   . GLY A  1 4   ? -14.357 2.226   -18.642 1.00 11.84  ? 10  GLY A O   1 
ATOM   5     N N   . ASP A  1 5   ? -13.229 0.303   -18.988 1.00 11.69  ? 11  ASP A N   1 
ATOM   6     C CA  . ASP A  1 5   ? -13.849 -0.398  -17.869 1.00 10.98  ? 11  ASP A CA  1 
ATOM   7     C C   . ASP A  1 5   ? -13.088 -0.151  -16.575 1.00 10.32  ? 11  ASP A C   1 
ATOM   8     O O   . ASP A  1 5   ? -11.874 0.068   -16.593 1.00 10.65  ? 11  ASP A O   1 
ATOM   9     C CB  . ASP A  1 5   ? -13.938 -1.897  -18.162 1.00 10.93  ? 11  ASP A CB  1 
ATOM   10    C CG  . ASP A  1 5   ? -14.609 -2.195  -19.494 1.00 12.54  ? 11  ASP A CG  1 
ATOM   11    O OD1 . ASP A  1 5   ? -14.452 -3.326  -19.997 1.00 16.08  ? 11  ASP A OD1 1 
ATOM   12    O OD2 . ASP A  1 5   ? -15.290 -1.303  -20.044 1.00 14.60  ? 11  ASP A OD2 1 
ATOM   13    N N   . LYS A  1 6   ? -13.809 -0.173  -15.456 1.00 9.16   ? 12  LYS A N   1 
ATOM   14    C CA  . LYS A  1 6   ? -13.199 0.010   -14.140 1.00 8.14   ? 12  LYS A CA  1 
ATOM   15    C C   . LYS A  1 6   ? -13.994 -0.663  -13.032 1.00 7.20   ? 12  LYS A C   1 
ATOM   16    O O   . LYS A  1 6   ? -15.218 -0.772  -13.110 1.00 6.88   ? 12  LYS A O   1 
ATOM   17    C CB  . LYS A  1 6   ? -12.973 1.502   -13.823 1.00 8.94   ? 12  LYS A CB  1 
ATOM   18    C CG  . LYS A  1 6   ? -14.223 2.360   -13.594 1.00 9.59   ? 12  LYS A CG  1 
ATOM   19    C CD  . LYS A  1 6   ? -13.824 3.811   -13.301 1.00 15.48  ? 12  LYS A CD  1 
ATOM   20    C CE  . LYS A  1 6   ? -15.030 4.740   -13.146 1.00 17.09  ? 12  LYS A CE  1 
ATOM   21    N NZ  . LYS A  1 6   ? -15.698 4.616   -11.815 1.00 15.89  ? 12  LYS A NZ  1 
ATOM   22    N N   . ILE A  1 7   ? -13.278 -1.127  -12.011 1.00 6.36   ? 13  ILE A N   1 
ATOM   23    C CA  . ILE A  1 7   ? -13.891 -1.692  -10.811 1.00 5.54   ? 13  ILE A CA  1 
ATOM   24    C C   . ILE A  1 7   ? -13.516 -0.852  -9.587  1.00 6.32   ? 13  ILE A C   1 
ATOM   25    O O   . ILE A  1 7   ? -12.376 -0.406  -9.449  1.00 6.46   ? 13  ILE A O   1 
ATOM   26    C CB  . ILE A  1 7   ? -13.511 -3.188  -10.616 1.00 5.05   ? 13  ILE A CB  1 
ATOM   27    C CG1 . ILE A  1 7   ? -14.437 -3.858  -9.596  1.00 3.57   ? 13  ILE A CG1 1 
ATOM   28    C CG2 . ILE A  1 7   ? -12.027 -3.352  -10.251 1.00 3.97   ? 13  ILE A CG2 1 
ATOM   29    C CD1 . ILE A  1 7   ? -14.383 -5.373  -9.618  1.00 2.00   ? 13  ILE A CD1 1 
ATOM   30    N N   . CYS A  1 8   ? -14.488 -0.627  -8.711  1.00 7.22   ? 14  CYS A N   1 
ATOM   31    C CA  . CYS A  1 8   ? -14.280 0.195   -7.528  1.00 7.92   ? 14  CYS A CA  1 
ATOM   32    C C   . CYS A  1 8   ? -14.545 -0.607  -6.272  1.00 7.57   ? 14  CYS A C   1 
ATOM   33    O O   . CYS A  1 8   ? -15.477 -1.408  -6.224  1.00 7.58   ? 14  CYS A O   1 
ATOM   34    C CB  . CYS A  1 8   ? -15.194 1.420   -7.559  1.00 7.77   ? 14  CYS A CB  1 
ATOM   35    S SG  . CYS A  1 8   ? -15.014 2.404   -9.049  1.00 14.22  ? 14  CYS A SG  1 
ATOM   36    N N   . LEU A  1 9   ? -13.723 -0.385  -5.255  1.00 7.44   ? 15  LEU A N   1 
ATOM   37    C CA  . LEU A  1 9   ? -13.940 -1.019  -3.968  1.00 7.72   ? 15  LEU A CA  1 
ATOM   38    C C   . LEU A  1 9   ? -14.529 -0.035  -2.986  1.00 7.98   ? 15  LEU A C   1 
ATOM   39    O O   . LEU A  1 9   ? -14.132 1.130   -2.952  1.00 8.35   ? 15  LEU A O   1 
ATOM   40    C CB  . LEU A  1 9   ? -12.651 -1.638  -3.436  1.00 7.75   ? 15  LEU A CB  1 
ATOM   41    C CG  . LEU A  1 9   ? -12.380 -3.023  -4.031  1.00 8.64   ? 15  LEU A CG  1 
ATOM   42    C CD1 . LEU A  1 9   ? -11.679 -2.940  -5.388  1.00 7.14   ? 15  LEU A CD1 1 
ATOM   43    C CD2 . LEU A  1 9   ? -11.566 -3.844  -3.071  1.00 12.55  ? 15  LEU A CD2 1 
ATOM   44    N N   . GLY A  1 10  ? -15.493 -0.510  -2.203  1.00 8.20   ? 16  GLY A N   1 
ATOM   45    C CA  . GLY A  1 10  ? -16.217 0.336   -1.263  1.00 7.61   ? 16  GLY A CA  1 
ATOM   46    C C   . GLY A  1 10  ? -16.890 -0.437  -0.149  1.00 7.39   ? 16  GLY A C   1 
ATOM   47    O O   . GLY A  1 10  ? -16.774 -1.660  -0.063  1.00 7.92   ? 16  GLY A O   1 
ATOM   48    N N   . HIS A  1 11  ? -17.601 0.295   0.700   1.00 7.12   ? 17  HIS A N   1 
ATOM   49    C CA  . HIS A  1 11  ? -18.200 -0.251  1.909   1.00 6.76   ? 17  HIS A CA  1 
ATOM   50    C C   . HIS A  1 11  ? -19.604 0.298   2.093   1.00 6.67   ? 17  HIS A C   1 
ATOM   51    O O   . HIS A  1 11  ? -19.988 1.263   1.434   1.00 6.66   ? 17  HIS A O   1 
ATOM   52    C CB  . HIS A  1 11  ? -17.335 0.094   3.124   1.00 6.86   ? 17  HIS A CB  1 
ATOM   53    C CG  . HIS A  1 11  ? -17.051 1.558   3.267   1.00 5.11   ? 17  HIS A CG  1 
ATOM   54    N ND1 . HIS A  1 11  ? -17.749 2.371   4.134   1.00 3.18   ? 17  HIS A ND1 1 
ATOM   55    C CD2 . HIS A  1 11  ? -16.146 2.355   2.650   1.00 2.47   ? 17  HIS A CD2 1 
ATOM   56    C CE1 . HIS A  1 11  ? -17.290 3.606   4.040   1.00 3.46   ? 17  HIS A CE1 1 
ATOM   57    N NE2 . HIS A  1 11  ? -16.316 3.623   3.148   1.00 2.43   ? 17  HIS A NE2 1 
ATOM   58    N N   . HIS A  1 12  ? -20.367 -0.314  2.990   1.00 7.58   ? 18  HIS A N   1 
ATOM   59    C CA  . HIS A  1 12  ? -21.746 0.107   3.214   1.00 9.06   ? 18  HIS A CA  1 
ATOM   60    C C   . HIS A  1 12  ? -21.860 1.370   4.071   1.00 9.33   ? 18  HIS A C   1 
ATOM   61    O O   . HIS A  1 12  ? -20.898 1.790   4.722   1.00 8.68   ? 18  HIS A O   1 
ATOM   62    C CB  . HIS A  1 12  ? -22.597 -1.037  3.801   1.00 9.20   ? 18  HIS A CB  1 
ATOM   63    C CG  . HIS A  1 12  ? -22.262 -1.398  5.218   1.00 10.28  ? 18  HIS A CG  1 
ATOM   64    N ND1 . HIS A  1 12  ? -22.710 -2.560  5.807   1.00 13.05  ? 18  HIS A ND1 1 
ATOM   65    C CD2 . HIS A  1 12  ? -21.523 -0.762  6.159   1.00 12.56  ? 18  HIS A CD2 1 
ATOM   66    C CE1 . HIS A  1 12  ? -22.273 -2.619  7.052   1.00 13.96  ? 18  HIS A CE1 1 
ATOM   67    N NE2 . HIS A  1 12  ? -21.548 -1.541  7.290   1.00 15.50  ? 18  HIS A NE2 1 
ATOM   68    N N   . ALA A  1 13  ? -23.046 1.968   4.042   1.00 10.06  ? 19  ALA A N   1 
ATOM   69    C CA  . ALA A  1 13  ? -23.399 3.083   4.909   1.00 11.24  ? 19  ALA A CA  1 
ATOM   70    C C   . ALA A  1 13  ? -24.910 3.109   5.121   1.00 12.33  ? 19  ALA A C   1 
ATOM   71    O O   . ALA A  1 13  ? -25.662 2.396   4.442   1.00 12.80  ? 19  ALA A O   1 
ATOM   72    C CB  . ALA A  1 13  ? -22.916 4.407   4.308   1.00 10.88  ? 19  ALA A CB  1 
ATOM   73    N N   . VAL A  1 14  ? -25.345 3.926   6.074   1.00 13.13  ? 20  VAL A N   1 
ATOM   74    C CA  . VAL A  1 14  ? -26.766 4.188   6.295   1.00 13.88  ? 20  VAL A CA  1 
ATOM   75    C C   . VAL A  1 14  ? -26.997 5.696   6.339   1.00 14.76  ? 20  VAL A C   1 
ATOM   76    O O   . VAL A  1 14  ? -26.053 6.463   6.544   1.00 15.31  ? 20  VAL A O   1 
ATOM   77    C CB  . VAL A  1 14  ? -27.293 3.512   7.583   1.00 13.90  ? 20  VAL A CB  1 
ATOM   78    C CG1 . VAL A  1 14  ? -27.319 1.993   7.419   1.00 11.97  ? 20  VAL A CG1 1 
ATOM   79    C CG2 . VAL A  1 14  ? -26.463 3.922   8.802   1.00 13.22  ? 20  VAL A CG2 1 
ATOM   80    N N   . ALA A  1 15  ? -28.241 6.118   6.129   1.00 15.58  ? 21  ALA A N   1 
ATOM   81    C CA  . ALA A  1 15  ? -28.578 7.543   6.121   1.00 16.17  ? 21  ALA A CA  1 
ATOM   82    C C   . ALA A  1 15  ? -28.320 8.189   7.489   1.00 16.83  ? 21  ALA A C   1 
ATOM   83    O O   . ALA A  1 15  ? -27.668 9.234   7.577   1.00 16.18  ? 21  ALA A O   1 
ATOM   84    C CB  . ALA A  1 15  ? -30.022 7.755   5.675   1.00 15.64  ? 21  ALA A CB  1 
ATOM   85    N N   . ASN A  1 16  ? -28.830 7.560   8.547   1.00 17.26  ? 22  ASN A N   1 
ATOM   86    C CA  . ASN A  1 16  ? -28.558 8.023   9.903   1.00 17.92  ? 22  ASN A CA  1 
ATOM   87    C C   . ASN A  1 16  ? -27.961 6.937   10.784  1.00 16.85  ? 22  ASN A C   1 
ATOM   88    O O   . ASN A  1 16  ? -28.618 5.940   11.102  1.00 16.84  ? 22  ASN A O   1 
ATOM   89    C CB  . ASN A  1 16  ? -29.796 8.676   10.548  1.00 19.86  ? 22  ASN A CB  1 
ATOM   90    C CG  . ASN A  1 16  ? -31.048 7.803   10.471  1.00 24.37  ? 22  ASN A CG  1 
ATOM   91    O OD1 . ASN A  1 16  ? -31.914 8.017   9.619   1.00 30.12  ? 22  ASN A OD1 1 
ATOM   92    N ND2 . ASN A  1 16  ? -31.155 6.828   11.373  1.00 24.61  ? 22  ASN A ND2 1 
ATOM   93    N N   . GLY A  1 17  ? -26.697 7.126   11.152  1.00 15.51  ? 23  GLY A N   1 
ATOM   94    C CA  . GLY A  1 17  ? -25.981 6.159   11.978  1.00 13.85  ? 23  GLY A CA  1 
ATOM   95    C C   . GLY A  1 17  ? -26.121 6.470   13.452  1.00 12.56  ? 23  GLY A C   1 
ATOM   96    O O   . GLY A  1 17  ? -27.003 7.226   13.850  1.00 12.47  ? 23  GLY A O   1 
ATOM   97    N N   . THR A  1 18  ? -25.238 5.891   14.259  1.00 11.83  ? 24  THR A N   1 
ATOM   98    C CA  . THR A  1 18  ? -25.287 6.063   15.705  1.00 11.78  ? 24  THR A CA  1 
ATOM   99    C C   . THR A  1 18  ? -23.981 6.655   16.225  1.00 12.58  ? 24  THR A C   1 
ATOM   100   O O   . THR A  1 18  ? -22.897 6.121   15.962  1.00 12.95  ? 24  THR A O   1 
ATOM   101   C CB  . THR A  1 18  ? -25.559 4.724   16.421  1.00 11.47  ? 24  THR A CB  1 
ATOM   102   O OG1 . THR A  1 18  ? -26.521 3.971   15.680  1.00 9.04   ? 24  THR A OG1 1 
ATOM   103   C CG2 . THR A  1 18  ? -26.077 4.956   17.831  1.00 11.44  ? 24  THR A CG2 1 
ATOM   104   N N   . LYS A  1 19  ? -24.096 7.752   16.968  1.00 12.42  ? 25  LYS A N   1 
ATOM   105   C CA  . LYS A  1 19  ? -22.936 8.432   17.536  1.00 12.86  ? 25  LYS A CA  1 
ATOM   106   C C   . LYS A  1 19  ? -22.319 7.640   18.694  1.00 12.37  ? 25  LYS A C   1 
ATOM   107   O O   . LYS A  1 19  ? -23.029 7.171   19.585  1.00 12.65  ? 25  LYS A O   1 
ATOM   108   C CB  . LYS A  1 19  ? -23.311 9.849   17.982  1.00 13.26  ? 25  LYS A CB  1 
ATOM   109   C CG  . LYS A  1 19  ? -23.877 10.723  16.863  1.00 16.46  ? 25  LYS A CG  1 
ATOM   110   C CD  . LYS A  1 19  ? -24.164 12.144  17.338  1.00 22.80  ? 25  LYS A CD  1 
ATOM   111   C CE  . LYS A  1 19  ? -25.088 12.891  16.373  1.00 25.20  ? 25  LYS A CE  1 
ATOM   112   N NZ  . LYS A  1 19  ? -24.570 12.929  14.971  1.00 24.00  ? 25  LYS A NZ  1 
ATOM   113   N N   . VAL A  1 20  ? -20.997 7.474   18.652  1.00 11.43  ? 26  VAL A N   1 
ATOM   114   C CA  . VAL A  1 20  ? -20.239 6.818   19.723  1.00 10.80  ? 26  VAL A CA  1 
ATOM   115   C C   . VAL A  1 20  ? -18.986 7.623   20.083  1.00 11.36  ? 26  VAL A C   1 
ATOM   116   O O   . VAL A  1 20  ? -18.603 8.546   19.362  1.00 12.04  ? 26  VAL A O   1 
ATOM   117   C CB  . VAL A  1 20  ? -19.817 5.361   19.361  1.00 10.96  ? 26  VAL A CB  1 
ATOM   118   C CG1 . VAL A  1 20  ? -21.032 4.467   19.172  1.00 8.39   ? 26  VAL A CG1 1 
ATOM   119   C CG2 . VAL A  1 20  ? -18.903 5.331   18.130  1.00 10.88  ? 26  VAL A CG2 1 
ATOM   120   N N   . ASN A  1 21  ? -18.350 7.261   21.193  1.00 11.51  ? 27  ASN A N   1 
ATOM   121   C CA  . ASN A  1 21  ? -17.122 7.915   21.628  1.00 11.15  ? 27  ASN A CA  1 
ATOM   122   C C   . ASN A  1 21  ? -15.914 7.006   21.496  1.00 10.94  ? 27  ASN A C   1 
ATOM   123   O O   . ASN A  1 21  ? -15.999 5.803   21.745  1.00 11.98  ? 27  ASN A O   1 
ATOM   124   C CB  . ASN A  1 21  ? -17.261 8.408   23.065  1.00 10.89  ? 27  ASN A CB  1 
ATOM   125   C CG  . ASN A  1 21  ? -18.347 9.456   23.214  1.00 13.04  ? 27  ASN A CG  1 
ATOM   126   O OD1 . ASN A  1 21  ? -18.675 10.172  22.263  1.00 13.53  ? 27  ASN A OD1 1 
ATOM   127   N ND2 . ASN A  1 21  ? -18.913 9.554   24.411  1.00 13.75  ? 27  ASN A ND2 1 
ATOM   128   N N   . THR A  1 22  ? -14.793 7.588   21.087  1.00 9.76   ? 28  THR A N   1 
ATOM   129   C CA  . THR A  1 22  ? -13.542 6.854   20.952  1.00 8.66   ? 28  THR A CA  1 
ATOM   130   C C   . THR A  1 22  ? -12.484 7.491   21.845  1.00 7.74   ? 28  THR A C   1 
ATOM   131   O O   . THR A  1 22  ? -12.785 8.402   22.614  1.00 7.62   ? 28  THR A O   1 
ATOM   132   C CB  . THR A  1 22  ? -13.044 6.864   19.495  1.00 8.85   ? 28  THR A CB  1 
ATOM   133   O OG1 . THR A  1 22  ? -12.754 8.212   19.100  1.00 9.25   ? 28  THR A OG1 1 
ATOM   134   C CG2 . THR A  1 22  ? -14.085 6.276   18.563  1.00 6.73   ? 28  THR A CG2 1 
ATOM   135   N N   . LEU A  1 23  ? -11.247 7.019   21.734  1.00 7.34   ? 29  LEU A N   1 
ATOM   136   C CA  . LEU A  1 23  ? -10.133 7.608   22.468  1.00 7.86   ? 29  LEU A CA  1 
ATOM   137   C C   . LEU A  1 23  ? -9.844  9.036   22.002  1.00 8.75   ? 29  LEU A C   1 
ATOM   138   O O   . LEU A  1 23  ? -9.481  9.900   22.802  1.00 9.20   ? 29  LEU A O   1 
ATOM   139   C CB  . LEU A  1 23  ? -8.871  6.748   22.322  1.00 7.65   ? 29  LEU A CB  1 
ATOM   140   C CG  . LEU A  1 23  ? -8.836  5.340   22.934  1.00 7.72   ? 29  LEU A CG  1 
ATOM   141   C CD1 . LEU A  1 23  ? -7.600  4.584   22.462  1.00 5.58   ? 29  LEU A CD1 1 
ATOM   142   C CD2 . LEU A  1 23  ? -8.886  5.382   24.456  1.00 6.53   ? 29  LEU A CD2 1 
ATOM   143   N N   . THR A  1 24  ? -10.026 9.278   20.707  1.00 9.09   ? 30  THR A N   1 
ATOM   144   C CA  . THR A  1 24  ? -9.635  10.543  20.095  1.00 9.12   ? 30  THR A CA  1 
ATOM   145   C C   . THR A  1 24  ? -10.805 11.440  19.688  1.00 9.67   ? 30  THR A C   1 
ATOM   146   O O   . THR A  1 24  ? -10.611 12.614  19.386  1.00 9.29   ? 30  THR A O   1 
ATOM   147   C CB  . THR A  1 24  ? -8.769  10.297  18.853  1.00 8.75   ? 30  THR A CB  1 
ATOM   148   O OG1 . THR A  1 24  ? -9.470  9.434   17.952  1.00 9.27   ? 30  THR A OG1 1 
ATOM   149   C CG2 . THR A  1 24  ? -7.451  9.648   19.244  1.00 9.71   ? 30  THR A CG2 1 
ATOM   150   N N   . GLU A  1 25  ? -12.015 10.894  19.674  1.00 10.90  ? 31  GLU A N   1 
ATOM   151   C CA  . GLU A  1 25  ? -13.149 11.632  19.139  1.00 12.23  ? 31  GLU A CA  1 
ATOM   152   C C   . GLU A  1 25  ? -14.419 11.449  19.958  1.00 13.37  ? 31  GLU A C   1 
ATOM   153   O O   . GLU A  1 25  ? -14.633 10.400  20.570  1.00 14.11  ? 31  GLU A O   1 
ATOM   154   C CB  . GLU A  1 25  ? -13.393 11.224  17.690  1.00 12.03  ? 31  GLU A CB  1 
ATOM   155   C CG  . GLU A  1 25  ? -13.814 12.366  16.802  1.00 15.76  ? 31  GLU A CG  1 
ATOM   156   C CD  . GLU A  1 25  ? -13.746 12.016  15.329  1.00 21.76  ? 31  GLU A CD  1 
ATOM   157   O OE1 . GLU A  1 25  ? -12.972 11.102  14.953  1.00 20.28  ? 31  GLU A OE1 1 
ATOM   158   O OE2 . GLU A  1 25  ? -14.465 12.670  14.544  1.00 24.65  ? 31  GLU A OE2 1 
ATOM   159   N N   . ARG A  1 26  ? -15.255 12.482  19.958  1.00 14.40  ? 32  ARG A N   1 
ATOM   160   C CA  . ARG A  1 26  ? -16.514 12.465  20.689  1.00 15.42  ? 32  ARG A CA  1 
ATOM   161   C C   . ARG A  1 26  ? -17.683 12.605  19.717  1.00 15.15  ? 32  ARG A C   1 
ATOM   162   O O   . ARG A  1 26  ? -17.708 13.516  18.889  1.00 14.86  ? 32  ARG A O   1 
ATOM   163   C CB  . ARG A  1 26  ? -16.534 13.586  21.728  1.00 15.74  ? 32  ARG A CB  1 
ATOM   164   C CG  . ARG A  1 26  ? -17.420 13.303  22.922  1.00 20.26  ? 32  ARG A CG  1 
ATOM   165   C CD  . ARG A  1 26  ? -17.744 14.583  23.663  1.00 29.20  ? 32  ARG A CD  1 
ATOM   166   N NE  . ARG A  1 26  ? -18.872 14.410  24.577  1.00 35.75  ? 32  ARG A NE  1 
ATOM   167   C CZ  . ARG A  1 26  ? -19.731 15.375  24.904  1.00 39.24  ? 32  ARG A CZ  1 
ATOM   168   N NH1 . ARG A  1 26  ? -19.607 16.594  24.384  1.00 39.05  ? 32  ARG A NH1 1 
ATOM   169   N NH2 . ARG A  1 26  ? -20.726 15.119  25.745  1.00 40.22  ? 32  ARG A NH2 1 
ATOM   170   N N   . GLY A  1 27  ? -18.641 11.687  19.814  1.00 15.35  ? 33  GLY A N   1 
ATOM   171   C CA  . GLY A  1 27  ? -19.807 11.686  18.933  1.00 15.16  ? 33  GLY A CA  1 
ATOM   172   C C   . GLY A  1 27  ? -19.486 11.467  17.463  1.00 15.22  ? 33  GLY A C   1 
ATOM   173   O O   . GLY A  1 27  ? -20.013 12.165  16.596  1.00 15.56  ? 33  GLY A O   1 
ATOM   174   N N   . ILE A  1 28  ? -18.607 10.508  17.185  1.00 14.92  ? 34  ILE A N   1 
ATOM   175   C CA  . ILE A  1 28  ? -18.353 10.065  15.816  1.00 14.32  ? 34  ILE A CA  1 
ATOM   176   C C   . ILE A  1 28  ? -19.404 9.013   15.440  1.00 13.88  ? 34  ILE A C   1 
ATOM   177   O O   . ILE A  1 28  ? -19.778 8.175   16.262  1.00 13.78  ? 34  ILE A O   1 
ATOM   178   C CB  . ILE A  1 28  ? -16.886 9.553   15.628  1.00 14.80  ? 34  ILE A CB  1 
ATOM   179   C CG1 . ILE A  1 28  ? -16.653 9.053   14.195  1.00 16.50  ? 34  ILE A CG1 1 
ATOM   180   C CG2 . ILE A  1 28  ? -16.525 8.480   16.662  1.00 12.52  ? 34  ILE A CG2 1 
ATOM   181   C CD1 . ILE A  1 28  ? -15.191 9.003   13.770  1.00 18.98  ? 34  ILE A CD1 1 
ATOM   182   N N   . GLU A  1 29  ? -19.890 9.077   14.205  1.00 13.58  ? 35  GLU A N   1 
ATOM   183   C CA  . GLU A  1 29  ? -21.003 8.236   13.758  1.00 12.66  ? 35  GLU A CA  1 
ATOM   184   C C   . GLU A  1 29  ? -20.537 6.897   13.167  1.00 10.36  ? 35  GLU A C   1 
ATOM   185   O O   . GLU A  1 29  ? -19.792 6.870   12.193  1.00 9.81   ? 35  GLU A O   1 
ATOM   186   C CB  . GLU A  1 29  ? -21.861 9.019   12.752  1.00 12.97  ? 35  GLU A CB  1 
ATOM   187   C CG  . GLU A  1 29  ? -23.240 8.423   12.478  1.00 17.52  ? 35  GLU A CG  1 
ATOM   188   C CD  . GLU A  1 29  ? -24.190 9.403   11.794  1.00 21.85  ? 35  GLU A CD  1 
ATOM   189   O OE1 . GLU A  1 29  ? -24.511 10.448  12.403  1.00 24.60  ? 35  GLU A OE1 1 
ATOM   190   O OE2 . GLU A  1 29  ? -24.628 9.120   10.656  1.00 19.80  ? 35  GLU A OE2 1 
ATOM   191   N N   . VAL A  1 30  ? -20.970 5.796   13.776  1.00 9.42   ? 36  VAL A N   1 
ATOM   192   C CA  . VAL A  1 30  ? -20.726 4.445   13.245  1.00 8.90   ? 36  VAL A CA  1 
ATOM   193   C C   . VAL A  1 30  ? -22.003 3.841   12.650  1.00 9.43   ? 36  VAL A C   1 
ATOM   194   O O   . VAL A  1 30  ? -23.104 4.329   12.914  1.00 9.26   ? 36  VAL A O   1 
ATOM   195   C CB  . VAL A  1 30  ? -20.146 3.479   14.314  1.00 8.33   ? 36  VAL A CB  1 
ATOM   196   C CG1 . VAL A  1 30  ? -18.710 3.855   14.665  1.00 12.02  ? 36  VAL A CG1 1 
ATOM   197   C CG2 . VAL A  1 30  ? -21.021 3.434   15.563  1.00 7.29   ? 36  VAL A CG2 1 
ATOM   198   N N   . VAL A  1 31  ? -21.859 2.781   11.856  1.00 10.32  ? 37  VAL A N   1 
ATOM   199   C CA  . VAL A  1 31  ? -23.013 2.141   11.205  1.00 11.57  ? 37  VAL A CA  1 
ATOM   200   C C   . VAL A  1 31  ? -23.995 1.560   12.228  1.00 13.01  ? 37  VAL A C   1 
ATOM   201   O O   . VAL A  1 31  ? -25.214 1.709   12.090  1.00 13.67  ? 37  VAL A O   1 
ATOM   202   C CB  . VAL A  1 31  ? -22.577 1.057   10.188  1.00 11.28  ? 37  VAL A CB  1 
ATOM   203   C CG1 . VAL A  1 31  ? -23.782 0.380   9.558   1.00 7.88   ? 37  VAL A CG1 1 
ATOM   204   C CG2 . VAL A  1 31  ? -21.707 1.676   9.107   1.00 12.12  ? 37  VAL A CG2 1 
ATOM   205   N N   . ASN A  1 32  ? -23.457 0.917   13.259  1.00 13.81  ? 38  ASN A N   1 
ATOM   206   C CA  . ASN A  1 32  ? -24.273 0.335   14.310  1.00 15.61  ? 38  ASN A CA  1 
ATOM   207   C C   . ASN A  1 32  ? -23.530 0.300   15.639  1.00 15.38  ? 38  ASN A C   1 
ATOM   208   O O   . ASN A  1 32  ? -22.297 0.276   15.672  1.00 15.80  ? 38  ASN A O   1 
ATOM   209   C CB  . ASN A  1 32  ? -24.724 -1.074  13.912  1.00 17.00  ? 38  ASN A CB  1 
ATOM   210   C CG  . ASN A  1 32  ? -26.014 -1.493  14.594  1.00 24.84  ? 38  ASN A CG  1 
ATOM   211   O OD1 . ASN A  1 32  ? -26.648 -0.707  15.311  1.00 24.74  ? 38  ASN A OD1 1 
ATOM   212   N ND2 . ASN A  1 32  ? -26.413 -2.744  14.368  1.00 37.63  ? 38  ASN A ND2 1 
ATOM   213   N N   . ALA A  1 33  ? -24.287 0.298   16.732  1.00 15.03  ? 39  ALA A N   1 
ATOM   214   C CA  . ALA A  1 33  ? -23.720 0.290   18.075  1.00 14.96  ? 39  ALA A CA  1 
ATOM   215   C C   . ALA A  1 33  ? -24.654 -0.419  19.050  1.00 15.52  ? 39  ALA A C   1 
ATOM   216   O O   . ALA A  1 33  ? -25.831 -0.615  18.753  1.00 16.09  ? 39  ALA A O   1 
ATOM   217   C CB  . ALA A  1 33  ? -23.452 1.711   18.537  1.00 14.36  ? 39  ALA A CB  1 
ATOM   218   N N   . THR A  1 34  ? -24.135 -0.811  20.210  1.00 15.94  ? 40  THR A N   1 
ATOM   219   C CA  . THR A  1 34  ? -24.994 -1.387  21.242  1.00 16.11  ? 40  THR A CA  1 
ATOM   220   C C   . THR A  1 34  ? -24.716 -0.890  22.656  1.00 15.62  ? 40  THR A C   1 
ATOM   221   O O   . THR A  1 34  ? -23.572 -0.646  23.043  1.00 15.03  ? 40  THR A O   1 
ATOM   222   C CB  . THR A  1 34  ? -25.033 -2.944  21.204  1.00 16.59  ? 40  THR A CB  1 
ATOM   223   O OG1 . THR A  1 34  ? -26.208 -3.398  21.888  1.00 20.22  ? 40  THR A OG1 1 
ATOM   224   C CG2 . THR A  1 34  ? -23.807 -3.562  21.858  1.00 13.72  ? 40  THR A CG2 1 
ATOM   225   N N   . GLU A  1 35  ? -25.802 -0.740  23.408  1.00 15.76  ? 41  GLU A N   1 
ATOM   226   C CA  . GLU A  1 35  ? -25.766 -0.308  24.791  1.00 15.29  ? 41  GLU A CA  1 
ATOM   227   C C   . GLU A  1 35  ? -25.066 -1.350  25.666  1.00 15.38  ? 41  GLU A C   1 
ATOM   228   O O   . GLU A  1 35  ? -25.301 -2.557  25.527  1.00 15.22  ? 41  GLU A O   1 
ATOM   229   C CB  . GLU A  1 35  ? -27.196 -0.046  25.278  1.00 14.65  ? 41  GLU A CB  1 
ATOM   230   C CG  . GLU A  1 35  ? -27.305 0.673   26.614  1.00 15.91  ? 41  GLU A CG  1 
ATOM   231   C CD  . GLU A  1 35  ? -26.509 1.957   26.656  1.00 17.42  ? 41  GLU A CD  1 
ATOM   232   O OE1 . GLU A  1 35  ? -26.907 2.930   25.983  1.00 17.94  ? 41  GLU A OE1 1 
ATOM   233   O OE2 . GLU A  1 35  ? -25.480 1.990   27.364  1.00 22.33  ? 41  GLU A OE2 1 
ATOM   234   N N   . THR A  1 36  ? -24.193 -0.869  26.550  1.00 15.04  ? 42  THR A N   1 
ATOM   235   C CA  . THR A  1 36  ? -23.483 -1.732  27.494  1.00 14.58  ? 42  THR A CA  1 
ATOM   236   C C   . THR A  1 36  ? -23.891 -1.422  28.934  1.00 14.70  ? 42  THR A C   1 
ATOM   237   O O   . THR A  1 36  ? -23.445 -2.098  29.867  1.00 15.15  ? 42  THR A O   1 
ATOM   238   C CB  . THR A  1 36  ? -21.952 -1.590  27.365  1.00 14.25  ? 42  THR A CB  1 
ATOM   239   O OG1 . THR A  1 36  ? -21.555 -0.274  27.768  1.00 14.44  ? 42  THR A OG1 1 
ATOM   240   C CG2 . THR A  1 36  ? -21.501 -1.837  25.937  1.00 12.81  ? 42  THR A CG2 1 
ATOM   241   N N   . VAL A  1 37  ? -24.735 -0.401  29.101  1.00 14.30  ? 43  VAL A N   1 
ATOM   242   C CA  . VAL A  1 37  ? -25.192 0.051   30.422  1.00 13.93  ? 43  VAL A CA  1 
ATOM   243   C C   . VAL A  1 37  ? -26.705 -0.097  30.565  1.00 14.12  ? 43  VAL A C   1 
ATOM   244   O O   . VAL A  1 37  ? -27.468 0.575   29.874  1.00 14.75  ? 43  VAL A O   1 
ATOM   245   C CB  . VAL A  1 37  ? -24.789 1.520   30.698  1.00 13.78  ? 43  VAL A CB  1 
ATOM   246   C CG1 . VAL A  1 37  ? -25.366 2.005   32.030  1.00 13.45  ? 43  VAL A CG1 1 
ATOM   247   C CG2 . VAL A  1 37  ? -23.273 1.672   30.683  1.00 12.89  ? 43  VAL A CG2 1 
ATOM   248   N N   . GLU A  1 38  ? -27.127 -0.972  31.475  1.00 14.69  ? 44  GLU A N   1 
ATOM   249   C CA  . GLU A  1 38  ? -28.545 -1.270  31.674  1.00 14.75  ? 44  GLU A CA  1 
ATOM   250   C C   . GLU A  1 38  ? -29.261 -0.177  32.458  1.00 14.15  ? 44  GLU A C   1 
ATOM   251   O O   . GLU A  1 38  ? -28.800 0.232   33.524  1.00 14.19  ? 44  GLU A O   1 
ATOM   252   C CB  . GLU A  1 38  ? -28.717 -2.614  32.388  1.00 15.29  ? 44  GLU A CB  1 
ATOM   253   C CG  . GLU A  1 38  ? -30.165 -3.085  32.479  1.00 18.08  ? 44  GLU A CG  1 
ATOM   254   C CD  . GLU A  1 38  ? -30.808 -3.237  31.113  1.00 19.90  ? 44  GLU A CD  1 
ATOM   255   O OE1 . GLU A  1 38  ? -30.342 -4.092  30.329  1.00 20.43  ? 44  GLU A OE1 1 
ATOM   256   O OE2 . GLU A  1 38  ? -31.772 -2.497  30.823  1.00 18.74  ? 44  GLU A OE2 1 
ATOM   257   N N   . THR A  1 39  ? -30.391 0.282   31.925  1.00 13.62  ? 45  THR A N   1 
ATOM   258   C CA  . THR A  1 39  ? -31.203 1.308   32.584  1.00 13.67  ? 45  THR A CA  1 
ATOM   259   C C   . THR A  1 39  ? -32.665 0.888   32.728  1.00 13.46  ? 45  THR A C   1 
ATOM   260   O O   . THR A  1 39  ? -33.475 1.630   33.288  1.00 13.76  ? 45  THR A O   1 
ATOM   261   C CB  . THR A  1 39  ? -31.144 2.667   31.834  1.00 13.97  ? 45  THR A CB  1 
ATOM   262   O OG1 . THR A  1 39  ? -31.455 2.469   30.449  1.00 12.09  ? 45  THR A OG1 1 
ATOM   263   C CG2 . THR A  1 39  ? -29.764 3.302   31.960  1.00 14.79  ? 45  THR A CG2 1 
ATOM   264   N N   . THR A  1 40  ? -33.000 -0.295  32.220  1.00 12.91  ? 46  THR A N   1 
ATOM   265   C CA  . THR A  1 40  ? -34.374 -0.785  32.264  1.00 12.61  ? 46  THR A CA  1 
ATOM   266   C C   . THR A  1 40  ? -34.611 -1.635  33.513  1.00 13.14  ? 46  THR A C   1 
ATOM   267   O O   . THR A  1 40  ? -34.129 -2.766  33.620  1.00 12.69  ? 46  THR A O   1 
ATOM   268   C CB  . THR A  1 40  ? -34.745 -1.563  30.978  1.00 12.82  ? 46  THR A CB  1 
ATOM   269   O OG1 . THR A  1 40  ? -34.410 -0.774  29.828  1.00 11.79  ? 46  THR A OG1 1 
ATOM   270   C CG2 . THR A  1 40  ? -36.226 -1.897  30.945  1.00 9.46   ? 46  THR A CG2 1 
ATOM   271   N N   . ASN A  1 41  ? -35.357 -1.062  34.455  1.00 13.97  ? 47  ASN A N   1 
ATOM   272   C CA  . ASN A  1 41  ? -35.691 -1.725  35.709  1.00 14.47  ? 47  ASN A CA  1 
ATOM   273   C C   . ASN A  1 41  ? -37.071 -2.358  35.646  1.00 15.01  ? 47  ASN A C   1 
ATOM   274   O O   . ASN A  1 41  ? -37.972 -1.819  35.010  1.00 16.11  ? 47  ASN A O   1 
ATOM   275   C CB  . ASN A  1 41  ? -35.636 -0.723  36.869  1.00 14.22  ? 47  ASN A CB  1 
ATOM   276   C CG  . ASN A  1 41  ? -35.896 -1.372  38.219  1.00 14.58  ? 47  ASN A CG  1 
ATOM   277   O OD1 . ASN A  1 41  ? -35.495 -2.509  38.463  1.00 15.54  ? 47  ASN A OD1 1 
ATOM   278   N ND2 . ASN A  1 41  ? -36.571 -0.648  39.104  1.00 14.10  ? 47  ASN A ND2 1 
ATOM   279   N N   . ILE A  1 42  ? -37.226 -3.505  36.299  1.00 15.35  ? 48  ILE A N   1 
ATOM   280   C CA  . ILE A  1 42  ? -38.536 -4.120  36.490  1.00 15.91  ? 48  ILE A CA  1 
ATOM   281   C C   . ILE A  1 42  ? -39.015 -3.833  37.920  1.00 16.65  ? 48  ILE A C   1 
ATOM   282   O O   . ILE A  1 42  ? -38.381 -4.251  38.892  1.00 15.58  ? 48  ILE A O   1 
ATOM   283   C CB  . ILE A  1 42  ? -38.503 -5.644  36.206  1.00 16.09  ? 48  ILE A CB  1 
ATOM   284   C CG1 . ILE A  1 42  ? -38.038 -5.908  34.768  1.00 16.00  ? 48  ILE A CG1 1 
ATOM   285   C CG2 . ILE A  1 42  ? -39.877 -6.274  36.462  1.00 15.37  ? 48  ILE A CG2 1 
ATOM   286   C CD1 . ILE A  1 42  ? -37.705 -7.366  34.466  1.00 15.74  ? 48  ILE A CD1 1 
ATOM   287   N N   . LYS A  1 43  ? -40.136 -3.122  38.038  1.00 17.94  ? 49  LYS A N   1 
ATOM   288   C CA  . LYS A  1 43  ? -40.626 -2.644  39.336  1.00 19.13  ? 49  LYS A CA  1 
ATOM   289   C C   . LYS A  1 43  ? -41.314 -3.738  40.156  1.00 19.62  ? 49  LYS A C   1 
ATOM   290   O O   . LYS A  1 43  ? -42.348 -3.502  40.789  1.00 20.45  ? 49  LYS A O   1 
ATOM   291   C CB  . LYS A  1 43  ? -41.554 -1.433  39.154  1.00 19.58  ? 49  LYS A CB  1 
ATOM   292   C CG  . LYS A  1 43  ? -40.914 -0.246  38.441  1.00 22.61  ? 49  LYS A CG  1 
ATOM   293   C CD  . LYS A  1 43  ? -41.798 1.001   38.472  1.00 28.35  ? 49  LYS A CD  1 
ATOM   294   C CE  . LYS A  1 43  ? -41.628 1.787   39.771  1.00 30.97  ? 49  LYS A CE  1 
ATOM   295   N NZ  . LYS A  1 43  ? -42.308 3.113   39.705  1.00 34.06  ? 49  LYS A NZ  1 
ATOM   296   N N   . LYS A  1 44  ? -40.719 -4.930  40.142  1.00 19.94  ? 50  LYS A N   1 
ATOM   297   C CA  . LYS A  1 44  ? -41.252 -6.114  40.813  1.00 19.93  ? 50  LYS A CA  1 
ATOM   298   C C   . LYS A  1 44  ? -40.098 -7.010  41.247  1.00 19.71  ? 50  LYS A C   1 
ATOM   299   O O   . LYS A  1 44  ? -39.013 -6.944  40.670  1.00 19.97  ? 50  LYS A O   1 
ATOM   300   C CB  . LYS A  1 44  ? -42.170 -6.895  39.864  1.00 20.12  ? 50  LYS A CB  1 
ATOM   301   C CG  . LYS A  1 44  ? -43.555 -6.286  39.666  1.00 23.61  ? 50  LYS A CG  1 
ATOM   302   C CD  . LYS A  1 44  ? -44.137 -6.654  38.308  1.00 29.68  ? 50  LYS A CD  1 
ATOM   303   C CE  . LYS A  1 44  ? -45.470 -5.961  38.058  1.00 33.61  ? 50  LYS A CE  1 
ATOM   304   N NZ  . LYS A  1 44  ? -46.536 -6.405  39.007  1.00 35.39  ? 50  LYS A NZ  1 
ATOM   305   N N   . ILE A  1 45  ? -40.322 -7.837  42.267  1.00 19.77  ? 51  ILE A N   1 
ATOM   306   C CA  . ILE A  1 45  ? -39.348 -8.871  42.624  1.00 19.41  ? 51  ILE A CA  1 
ATOM   307   C C   . ILE A  1 45  ? -39.684 -10.149 41.858  1.00 20.07  ? 51  ILE A C   1 
ATOM   308   O O   . ILE A  1 45  ? -40.655 -10.847 42.170  1.00 20.00  ? 51  ILE A O   1 
ATOM   309   C CB  . ILE A  1 45  ? -39.264 -9.135  44.153  1.00 19.43  ? 51  ILE A CB  1 
ATOM   310   C CG1 . ILE A  1 45  ? -38.937 -7.844  44.924  1.00 17.85  ? 51  ILE A CG1 1 
ATOM   311   C CG2 . ILE A  1 45  ? -38.253 -10.255 44.456  1.00 15.24  ? 51  ILE A CG2 1 
ATOM   312   C CD1 . ILE A  1 45  ? -37.499 -7.322  44.754  1.00 17.29  ? 51  ILE A CD1 1 
ATOM   313   N N   . CYS A  1 46  ? -38.879 -10.424 40.837  1.00 20.82  ? 52  CYS A N   1 
ATOM   314   C CA  . CYS A  1 46  ? -39.090 -11.565 39.957  1.00 21.59  ? 52  CYS A CA  1 
ATOM   315   C C   . CYS A  1 46  ? -38.712 -12.862 40.667  1.00 21.07  ? 52  CYS A C   1 
ATOM   316   O O   . CYS A  1 46  ? -37.540 -13.110 40.962  1.00 21.03  ? 52  CYS A O   1 
ATOM   317   C CB  . CYS A  1 46  ? -38.313 -11.377 38.651  1.00 22.14  ? 52  CYS A CB  1 
ATOM   318   S SG  . CYS A  1 46  ? -38.957 -10.031 37.607  1.00 24.23  ? 52  CYS A SG  1 
ATOM   319   N N   . THR A  1 47  ? -39.727 -13.676 40.946  1.00 20.48  ? 53  THR A N   1 
ATOM   320   C CA  . THR A  1 47  ? -39.580 -14.847 41.804  1.00 20.13  ? 53  THR A CA  1 
ATOM   321   C C   . THR A  1 47  ? -39.787 -16.168 41.068  1.00 20.43  ? 53  THR A C   1 
ATOM   322   O O   . THR A  1 47  ? -39.935 -17.219 41.702  1.00 20.73  ? 53  THR A O   1 
ATOM   323   C CB  . THR A  1 47  ? -40.575 -14.798 42.985  1.00 19.90  ? 53  THR A CB  1 
ATOM   324   O OG1 . THR A  1 47  ? -41.913 -14.708 42.480  1.00 20.37  ? 53  THR A OG1 1 
ATOM   325   C CG2 . THR A  1 47  ? -40.293 -13.611 43.889  1.00 18.17  ? 53  THR A CG2 1 
ATOM   326   N N   . GLN A  1 48  ? -39.803 -16.124 39.739  1.00 20.41  ? 54  GLN A N   1 
ATOM   327   C CA  . GLN A  1 48  ? -40.052 -17.332 38.962  1.00 20.49  ? 54  GLN A CA  1 
ATOM   328   C C   . GLN A  1 48  ? -38.855 -18.274 39.019  1.00 20.36  ? 54  GLN A C   1 
ATOM   329   O O   . GLN A  1 48  ? -37.709 -17.855 38.831  1.00 19.74  ? 54  GLN A O   1 
ATOM   330   C CB  . GLN A  1 48  ? -40.413 -17.006 37.514  1.00 20.63  ? 54  GLN A CB  1 
ATOM   331   C CG  . GLN A  1 48  ? -41.152 -18.132 36.804  1.00 21.25  ? 54  GLN A CG  1 
ATOM   332   C CD  . GLN A  1 48  ? -41.153 -17.974 35.300  1.00 24.46  ? 54  GLN A CD  1 
ATOM   333   O OE1 . GLN A  1 48  ? -40.098 -17.881 34.670  1.00 26.40  ? 54  GLN A OE1 1 
ATOM   334   N NE2 . GLN A  1 48  ? -42.343 -17.953 34.711  1.00 24.84  ? 54  GLN A NE2 1 
ATOM   335   N N   . GLY A  1 49  ? -39.143 -19.546 39.289  1.00 20.27  ? 55  GLY A N   1 
ATOM   336   C CA  . GLY A  1 49  ? -38.114 -20.570 39.433  1.00 20.08  ? 55  GLY A CA  1 
ATOM   337   C C   . GLY A  1 49  ? -37.403 -20.453 40.763  1.00 20.06  ? 55  GLY A C   1 
ATOM   338   O O   . GLY A  1 49  ? -36.273 -20.920 40.913  1.00 20.62  ? 55  GLY A O   1 
ATOM   339   N N   . LYS A  1 50  ? -38.073 -19.822 41.724  1.00 19.62  ? 56  LYS A N   1 
ATOM   340   C CA  . LYS A  1 50  ? -37.519 -19.601 43.056  1.00 19.79  ? 56  LYS A CA  1 
ATOM   341   C C   . LYS A  1 50  ? -38.531 -19.912 44.150  1.00 19.64  ? 56  LYS A C   1 
ATOM   342   O O   . LYS A  1 50  ? -39.724 -20.071 43.880  1.00 19.77  ? 56  LYS A O   1 
ATOM   343   C CB  . LYS A  1 50  ? -37.014 -18.162 43.195  1.00 19.91  ? 56  LYS A CB  1 
ATOM   344   C CG  . LYS A  1 50  ? -35.613 -17.967 42.672  1.00 19.62  ? 56  LYS A CG  1 
ATOM   345   C CD  . LYS A  1 50  ? -35.325 -16.512 42.402  1.00 19.07  ? 56  LYS A CD  1 
ATOM   346   C CE  . LYS A  1 50  ? -33.939 -16.345 41.804  1.00 19.50  ? 56  LYS A CE  1 
ATOM   347   N NZ  . LYS A  1 50  ? -33.821 -16.954 40.447  1.00 15.43  ? 56  LYS A NZ  1 
ATOM   348   N N   . ARG A  1 51  ? -38.039 -20.005 45.381  1.00 19.31  ? 57  ARG A N   1 
ATOM   349   C CA  . ARG A  1 51  ? -38.880 -20.257 46.543  1.00 19.59  ? 57  ARG A CA  1 
ATOM   350   C C   . ARG A  1 51  ? -38.784 -19.035 47.452  1.00 19.01  ? 57  ARG A C   1 
ATOM   351   O O   . ARG A  1 51  ? -37.987 -19.019 48.394  1.00 18.90  ? 57  ARG A O   1 
ATOM   352   C CB  . ARG A  1 51  ? -38.431 -21.529 47.275  1.00 19.75  ? 57  ARG A CB  1 
ATOM   353   C CG  . ARG A  1 51  ? -38.372 -22.778 46.397  1.00 21.66  ? 57  ARG A CG  1 
ATOM   354   C CD  . ARG A  1 51  ? -37.649 -23.939 47.081  1.00 26.13  ? 57  ARG A CD  1 
ATOM   355   N NE  . ARG A  1 51  ? -36.243 -23.638 47.364  1.00 29.12  ? 57  ARG A NE  1 
ATOM   356   C CZ  . ARG A  1 51  ? -35.722 -23.517 48.585  1.00 29.25  ? 57  ARG A CZ  1 
ATOM   357   N NH1 . ARG A  1 51  ? -36.479 -23.680 49.665  1.00 28.55  ? 57  ARG A NH1 1 
ATOM   358   N NH2 . ARG A  1 51  ? -34.433 -23.239 48.728  1.00 28.15  ? 57  ARG A NH2 1 
ATOM   359   N N   . PRO A  1 52  ? -39.593 -17.998 47.163  1.00 18.48  ? 58  PRO A N   1 
ATOM   360   C CA  . PRO A  1 52  ? -39.466 -16.731 47.873  1.00 17.75  ? 58  PRO A CA  1 
ATOM   361   C C   . PRO A  1 52  ? -40.130 -16.745 49.242  1.00 17.19  ? 58  PRO A C   1 
ATOM   362   O O   . PRO A  1 52  ? -40.995 -17.585 49.505  1.00 17.65  ? 58  PRO A O   1 
ATOM   363   C CB  . PRO A  1 52  ? -40.191 -15.751 46.953  1.00 17.78  ? 58  PRO A CB  1 
ATOM   364   C CG  . PRO A  1 52  ? -41.249 -16.574 46.299  1.00 18.61  ? 58  PRO A CG  1 
ATOM   365   C CD  . PRO A  1 52  ? -40.688 -17.968 46.173  1.00 18.38  ? 58  PRO A CD  1 
ATOM   366   N N   . THR A  1 53  ? -39.717 -15.819 50.102  1.00 16.45  ? 59  THR A N   1 
ATOM   367   C CA  . THR A  1 53  ? -40.367 -15.607 51.388  1.00 15.60  ? 59  THR A CA  1 
ATOM   368   C C   . THR A  1 53  ? -40.588 -14.117 51.611  1.00 15.49  ? 59  THR A C   1 
ATOM   369   O O   . THR A  1 53  ? -39.645 -13.365 51.860  1.00 16.21  ? 59  THR A O   1 
ATOM   370   C CB  . THR A  1 53  ? -39.568 -16.241 52.547  1.00 15.24  ? 59  THR A CB  1 
ATOM   371   O OG1 . THR A  1 53  ? -39.614 -17.668 52.422  1.00 15.47  ? 59  THR A OG1 1 
ATOM   372   C CG2 . THR A  1 53  ? -40.158 -15.851 53.897  1.00 15.43  ? 59  THR A CG2 1 
ATOM   373   N N   . ASP A  1 54  ? -41.842 -13.697 51.493  1.00 15.37  ? 60  ASP A N   1 
ATOM   374   C CA  . ASP A  1 54  ? -42.217 -12.311 51.730  1.00 15.44  ? 60  ASP A CA  1 
ATOM   375   C C   . ASP A  1 54  ? -42.505 -12.130 53.219  1.00 15.23  ? 60  ASP A C   1 
ATOM   376   O O   . ASP A  1 54  ? -43.593 -12.464 53.697  1.00 15.30  ? 60  ASP A O   1 
ATOM   377   C CB  . ASP A  1 54  ? -43.434 -11.943 50.874  1.00 15.69  ? 60  ASP A CB  1 
ATOM   378   C CG  . ASP A  1 54  ? -43.802 -10.468 50.962  1.00 16.35  ? 60  ASP A CG  1 
ATOM   379   O OD1 . ASP A  1 54  ? -43.071 -9.686  51.606  1.00 15.53  ? 60  ASP A OD1 1 
ATOM   380   O OD2 . ASP A  1 54  ? -44.840 -10.093 50.380  1.00 16.81  ? 60  ASP A OD2 1 
ATOM   381   N N   . LEU A  1 55  ? -41.518 -11.600 53.942  1.00 14.49  ? 61  LEU A N   1 
ATOM   382   C CA  . LEU A  1 55  ? -41.584 -11.492 55.401  1.00 14.13  ? 61  LEU A CA  1 
ATOM   383   C C   . LEU A  1 55  ? -42.649 -10.530 55.936  1.00 14.62  ? 61  LEU A C   1 
ATOM   384   O O   . LEU A  1 55  ? -43.015 -10.612 57.111  1.00 15.03  ? 61  LEU A O   1 
ATOM   385   C CB  . LEU A  1 55  ? -40.214 -11.136 55.985  1.00 13.26  ? 61  LEU A CB  1 
ATOM   386   C CG  . LEU A  1 55  ? -39.089 -12.176 55.937  1.00 13.02  ? 61  LEU A CG  1 
ATOM   387   C CD1 . LEU A  1 55  ? -37.779 -11.532 56.361  1.00 11.96  ? 61  LEU A CD1 1 
ATOM   388   C CD2 . LEU A  1 55  ? -39.385 -13.403 56.796  1.00 8.48   ? 61  LEU A CD2 1 
ATOM   389   N N   . GLY A  1 56  ? -43.132 -9.626  55.082  1.00 14.39  ? 62  GLY A N   1 
ATOM   390   C CA  . GLY A  1 56  ? -44.171 -8.658  55.449  1.00 14.93  ? 62  GLY A CA  1 
ATOM   391   C C   . GLY A  1 56  ? -43.959 -7.950  56.780  1.00 15.95  ? 62  GLY A C   1 
ATOM   392   O O   . GLY A  1 56  ? -42.963 -7.243  56.969  1.00 15.99  ? 62  GLY A O   1 
ATOM   393   N N   . GLN A  1 57  ? -44.901 -8.158  57.700  1.00 16.38  ? 63  GLN A N   1 
ATOM   394   C CA  . GLN A  1 57  ? -44.874 -7.565  59.042  1.00 16.96  ? 63  GLN A CA  1 
ATOM   395   C C   . GLN A  1 57  ? -43.698 -8.064  59.888  1.00 16.63  ? 63  GLN A C   1 
ATOM   396   O O   . GLN A  1 57  ? -43.279 -7.393  60.834  1.00 16.65  ? 63  GLN A O   1 
ATOM   397   C CB  . GLN A  1 57  ? -46.179 -7.882  59.784  1.00 17.93  ? 63  GLN A CB  1 
ATOM   398   C CG  . GLN A  1 57  ? -47.456 -7.275  59.193  1.00 22.01  ? 63  GLN A CG  1 
ATOM   399   C CD  . GLN A  1 57  ? -47.930 -6.042  59.951  1.00 25.90  ? 63  GLN A CD  1 
ATOM   400   O OE1 . GLN A  1 57  ? -47.388 -4.947  59.786  1.00 29.60  ? 63  GLN A OE1 1 
ATOM   401   N NE2 . GLN A  1 57  ? -48.952 -6.217  60.783  1.00 23.07  ? 63  GLN A NE2 1 
ATOM   402   N N   . CYS A  1 58  ? -43.177 -9.241  59.543  1.00 16.35  ? 64  CYS A N   1 
ATOM   403   C CA  . CYS A  1 58  ? -42.165 -9.929  60.348  1.00 16.61  ? 64  CYS A CA  1 
ATOM   404   C C   . CYS A  1 58  ? -40.740 -9.515  59.989  1.00 15.96  ? 64  CYS A C   1 
ATOM   405   O O   . CYS A  1 58  ? -40.324 -9.618  58.836  1.00 16.37  ? 64  CYS A O   1 
ATOM   406   C CB  . CYS A  1 58  ? -42.333 -11.445 60.202  1.00 16.59  ? 64  CYS A CB  1 
ATOM   407   S SG  . CYS A  1 58  ? -40.981 -12.440 60.858  1.00 21.88  ? 64  CYS A SG  1 
ATOM   408   N N   . GLY A  1 59  ? -39.997 -9.040  60.983  1.00 15.66  ? 65  GLY A N   1 
ATOM   409   C CA  . GLY A  1 59  ? -38.591 -8.696  60.790  1.00 15.66  ? 65  GLY A CA  1 
ATOM   410   C C   . GLY A  1 59  ? -37.762 -9.962  60.696  1.00 15.99  ? 65  GLY A C   1 
ATOM   411   O O   . GLY A  1 59  ? -38.056 -10.944 61.382  1.00 16.37  ? 65  GLY A O   1 
ATOM   412   N N   . LEU A  1 60  ? -36.732 -9.948  59.850  1.00 15.74  ? 66  LEU A N   1 
ATOM   413   C CA  . LEU A  1 60  ? -35.895 -11.135 59.633  1.00 15.34  ? 66  LEU A CA  1 
ATOM   414   C C   . LEU A  1 60  ? -35.341 -11.721 60.935  1.00 15.13  ? 66  LEU A C   1 
ATOM   415   O O   . LEU A  1 60  ? -35.321 -12.936 61.113  1.00 15.41  ? 66  LEU A O   1 
ATOM   416   C CB  . LEU A  1 60  ? -34.757 -10.834 58.652  1.00 15.53  ? 66  LEU A CB  1 
ATOM   417   C CG  . LEU A  1 60  ? -33.799 -11.969 58.262  1.00 16.26  ? 66  LEU A CG  1 
ATOM   418   C CD1 . LEU A  1 60  ? -34.532 -13.204 57.730  1.00 14.70  ? 66  LEU A CD1 1 
ATOM   419   C CD2 . LEU A  1 60  ? -32.797 -11.465 57.241  1.00 18.67  ? 66  LEU A CD2 1 
ATOM   420   N N   . LEU A  1 61  ? -34.906 -10.854 61.841  1.00 15.03  ? 67  LEU A N   1 
ATOM   421   C CA  . LEU A  1 61  ? -34.387 -11.293 63.129  1.00 15.21  ? 67  LEU A CA  1 
ATOM   422   C C   . LEU A  1 61  ? -35.482 -11.886 64.014  1.00 16.39  ? 67  LEU A C   1 
ATOM   423   O O   . LEU A  1 61  ? -35.226 -12.801 64.798  1.00 17.24  ? 67  LEU A O   1 
ATOM   424   C CB  . LEU A  1 61  ? -33.669 -10.148 63.838  1.00 14.48  ? 67  LEU A CB  1 
ATOM   425   C CG  . LEU A  1 61  ? -32.468 -9.554  63.093  1.00 13.24  ? 67  LEU A CG  1 
ATOM   426   C CD1 . LEU A  1 61  ? -31.764 -8.510  63.951  1.00 13.30  ? 67  LEU A CD1 1 
ATOM   427   C CD2 . LEU A  1 61  ? -31.494 -10.643 62.670  1.00 8.68   ? 67  LEU A CD2 1 
ATOM   428   N N   . GLY A  1 62  ? -36.704 -11.378 63.864  1.00 16.71  ? 68  GLY A N   1 
ATOM   429   C CA  . GLY A  1 62  ? -37.857 -11.900 64.591  1.00 16.51  ? 68  GLY A CA  1 
ATOM   430   C C   . GLY A  1 62  ? -38.059 -13.396 64.415  1.00 16.35  ? 68  GLY A C   1 
ATOM   431   O O   . GLY A  1 62  ? -38.549 -14.070 65.320  1.00 16.43  ? 68  GLY A O   1 
ATOM   432   N N   . THR A  1 63  ? -37.662 -13.917 63.255  1.00 15.85  ? 69  THR A N   1 
ATOM   433   C CA  . THR A  1 63  ? -37.800 -15.346 62.944  1.00 15.16  ? 69  THR A CA  1 
ATOM   434   C C   . THR A  1 63  ? -37.045 -16.243 63.924  1.00 14.76  ? 69  THR A C   1 
ATOM   435   O O   . THR A  1 63  ? -37.320 -17.437 64.013  1.00 14.48  ? 69  THR A O   1 
ATOM   436   C CB  . THR A  1 63  ? -37.303 -15.677 61.519  1.00 15.38  ? 69  THR A CB  1 
ATOM   437   O OG1 . THR A  1 63  ? -35.911 -15.351 61.408  1.00 13.78  ? 69  THR A OG1 1 
ATOM   438   C CG2 . THR A  1 63  ? -38.107 -14.913 60.461  1.00 13.61  ? 69  THR A CG2 1 
ATOM   439   N N   . LEU A  1 64  ? -36.094 -15.661 64.651  1.00 14.58  ? 70  LEU A N   1 
ATOM   440   C CA  . LEU A  1 64  ? -35.267 -16.412 65.592  1.00 13.72  ? 70  LEU A CA  1 
ATOM   441   C C   . LEU A  1 64  ? -35.887 -16.475 66.976  1.00 13.11  ? 70  LEU A C   1 
ATOM   442   O O   . LEU A  1 64  ? -35.890 -17.532 67.608  1.00 13.75  ? 70  LEU A O   1 
ATOM   443   C CB  . LEU A  1 64  ? -33.868 -15.802 65.691  1.00 13.71  ? 70  LEU A CB  1 
ATOM   444   C CG  . LEU A  1 64  ? -33.100 -15.561 64.391  1.00 13.51  ? 70  LEU A CG  1 
ATOM   445   C CD1 . LEU A  1 64  ? -31.801 -14.850 64.700  1.00 14.08  ? 70  LEU A CD1 1 
ATOM   446   C CD2 . LEU A  1 64  ? -32.844 -16.862 63.648  1.00 10.96  ? 70  LEU A CD2 1 
ATOM   447   N N   . ILE A  1 65  ? -36.400 -15.340 67.442  1.00 12.48  ? 71  ILE A N   1 
ATOM   448   C CA  . ILE A  1 65  ? -36.952 -15.227 68.794  1.00 11.86  ? 71  ILE A CA  1 
ATOM   449   C C   . ILE A  1 65  ? -38.456 -15.421 68.812  1.00 11.34  ? 71  ILE A C   1 
ATOM   450   O O   . ILE A  1 65  ? -39.002 -15.963 69.771  1.00 11.31  ? 71  ILE A O   1 
ATOM   451   C CB  . ILE A  1 65  ? -36.574 -13.891 69.471  1.00 11.71  ? 71  ILE A CB  1 
ATOM   452   C CG1 . ILE A  1 65  ? -36.970 -12.692 68.592  1.00 12.92  ? 71  ILE A CG1 1 
ATOM   453   C CG2 . ILE A  1 65  ? -35.088 -13.884 69.785  1.00 10.85  ? 71  ILE A CG2 1 
ATOM   454   C CD1 . ILE A  1 65  ? -36.755 -11.329 69.238  1.00 11.90  ? 71  ILE A CD1 1 
ATOM   455   N N   . GLY A  1 66  ? -39.110 -14.971 67.746  1.00 11.53  ? 72  GLY A N   1 
ATOM   456   C CA  . GLY A  1 66  ? -40.525 -15.240 67.514  1.00 11.98  ? 72  GLY A CA  1 
ATOM   457   C C   . GLY A  1 66  ? -41.538 -14.367 68.228  1.00 11.97  ? 72  GLY A C   1 
ATOM   458   O O   . GLY A  1 66  ? -42.223 -14.843 69.132  1.00 11.50  ? 72  GLY A O   1 
ATOM   459   N N   . PRO A  1 67  ? -41.643 -13.084 67.830  1.00 12.78  ? 73  PRO A N   1 
ATOM   460   C CA  . PRO A  1 67  ? -42.778 -12.266 68.259  1.00 13.46  ? 73  PRO A CA  1 
ATOM   461   C C   . PRO A  1 67  ? -44.025 -12.658 67.458  1.00 14.49  ? 73  PRO A C   1 
ATOM   462   O O   . PRO A  1 67  ? -43.890 -13.280 66.404  1.00 15.22  ? 73  PRO A O   1 
ATOM   463   C CB  . PRO A  1 67  ? -42.333 -10.844 67.911  1.00 13.44  ? 73  PRO A CB  1 
ATOM   464   C CG  . PRO A  1 67  ? -41.372 -11.006 66.800  1.00 12.59  ? 73  PRO A CG  1 
ATOM   465   C CD  . PRO A  1 67  ? -40.671 -12.305 67.040  1.00 12.73  ? 73  PRO A CD  1 
ATOM   466   N N   . PRO A  1 68  ? -45.233 -12.299 67.943  1.00 14.89  ? 74  PRO A N   1 
ATOM   467   C CA  . PRO A  1 68  ? -46.481 -12.702 67.281  1.00 14.21  ? 74  PRO A CA  1 
ATOM   468   C C   . PRO A  1 68  ? -46.499 -12.509 65.761  1.00 13.87  ? 74  PRO A C   1 
ATOM   469   O O   . PRO A  1 68  ? -47.106 -13.312 65.048  1.00 14.43  ? 74  PRO A O   1 
ATOM   470   C CB  . PRO A  1 68  ? -47.544 -11.810 67.941  1.00 14.02  ? 74  PRO A CB  1 
ATOM   471   C CG  . PRO A  1 68  ? -46.791 -10.853 68.830  1.00 16.14  ? 74  PRO A CG  1 
ATOM   472   C CD  . PRO A  1 68  ? -45.509 -11.525 69.164  1.00 15.34  ? 74  PRO A CD  1 
ATOM   473   N N   . GLN A  1 69  ? -45.833 -11.463 65.276  1.00 13.04  ? 75  GLN A N   1 
ATOM   474   C CA  . GLN A  1 69  ? -45.828 -11.147 63.848  1.00 12.97  ? 75  GLN A CA  1 
ATOM   475   C C   . GLN A  1 69  ? -44.994 -12.131 63.017  1.00 13.49  ? 75  GLN A C   1 
ATOM   476   O O   . GLN A  1 69  ? -45.153 -12.215 61.797  1.00 13.45  ? 75  GLN A O   1 
ATOM   477   C CB  . GLN A  1 69  ? -45.376 -9.700  63.603  1.00 12.60  ? 75  GLN A CB  1 
ATOM   478   C CG  . GLN A  1 69  ? -43.948 -9.377  64.047  1.00 12.11  ? 75  GLN A CG  1 
ATOM   479   C CD  . GLN A  1 69  ? -43.871 -8.790  65.444  1.00 12.53  ? 75  GLN A CD  1 
ATOM   480   O OE1 . GLN A  1 69  ? -44.749 -9.010  66.284  1.00 15.06  ? 75  GLN A OE1 1 
ATOM   481   N NE2 . GLN A  1 69  ? -42.808 -8.039  65.703  1.00 10.91  ? 75  GLN A NE2 1 
ATOM   482   N N   . CYS A  1 70  ? -44.120 -12.875 63.686  1.00 13.75  ? 76  CYS A N   1 
ATOM   483   C CA  . CYS A  1 70  ? -43.257 -13.844 63.018  1.00 14.99  ? 76  CYS A CA  1 
ATOM   484   C C   . CYS A  1 70  ? -43.696 -15.303 63.202  1.00 15.46  ? 76  CYS A C   1 
ATOM   485   O O   . CYS A  1 70  ? -42.938 -16.225 62.882  1.00 15.11  ? 76  CYS A O   1 
ATOM   486   C CB  . CYS A  1 70  ? -41.812 -13.655 63.479  1.00 15.16  ? 76  CYS A CB  1 
ATOM   487   S SG  . CYS A  1 70  ? -41.066 -12.136 62.873  1.00 19.83  ? 76  CYS A SG  1 
ATOM   488   N N   . ASP A  1 71  ? -44.919 -15.508 63.696  1.00 15.90  ? 77  ASP A N   1 
ATOM   489   C CA  . ASP A  1 71  ? -45.450 -16.855 63.950  1.00 16.73  ? 77  ASP A CA  1 
ATOM   490   C C   . ASP A  1 71  ? -45.378 -17.762 62.723  1.00 16.33  ? 77  ASP A C   1 
ATOM   491   O O   . ASP A  1 71  ? -45.045 -18.944 62.832  1.00 16.49  ? 77  ASP A O   1 
ATOM   492   C CB  . ASP A  1 71  ? -46.895 -16.789 64.462  1.00 17.45  ? 77  ASP A CB  1 
ATOM   493   C CG  . ASP A  1 71  ? -46.980 -16.580 65.967  1.00 20.46  ? 77  ASP A CG  1 
ATOM   494   O OD1 . ASP A  1 71  ? -48.075 -16.232 66.461  1.00 22.06  ? 77  ASP A OD1 1 
ATOM   495   O OD2 . ASP A  1 71  ? -45.956 -16.766 66.659  1.00 24.89  ? 77  ASP A OD2 1 
ATOM   496   N N   . GLN A  1 72  ? -45.674 -17.192 61.559  1.00 15.60  ? 78  GLN A N   1 
ATOM   497   C CA  . GLN A  1 72  ? -45.712 -17.945 60.308  1.00 14.82  ? 78  GLN A CA  1 
ATOM   498   C C   . GLN A  1 72  ? -44.327 -18.157 59.695  1.00 14.19  ? 78  GLN A C   1 
ATOM   499   O O   . GLN A  1 72  ? -44.205 -18.738 58.616  1.00 13.42  ? 78  GLN A O   1 
ATOM   500   C CB  . GLN A  1 72  ? -46.640 -17.252 59.302  1.00 14.96  ? 78  GLN A CB  1 
ATOM   501   C CG  . GLN A  1 72  ? -48.103 -17.197 59.737  1.00 13.99  ? 78  GLN A CG  1 
ATOM   502   C CD  . GLN A  1 72  ? -49.034 -16.664 58.657  1.00 15.09  ? 78  GLN A CD  1 
ATOM   503   O OE1 . GLN A  1 72  ? -48.650 -16.522 57.493  1.00 17.80  ? 78  GLN A OE1 1 
ATOM   504   N NE2 . GLN A  1 72  ? -50.272 -16.369 59.042  1.00 11.54  ? 78  GLN A NE2 1 
ATOM   505   N N   . PHE A  1 73  ? -43.288 -17.692 60.386  1.00 14.41  ? 79  PHE A N   1 
ATOM   506   C CA  . PHE A  1 73  ? -41.923 -17.741 59.853  1.00 14.11  ? 79  PHE A CA  1 
ATOM   507   C C   . PHE A  1 73  ? -40.899 -18.341 60.821  1.00 13.61  ? 79  PHE A C   1 
ATOM   508   O O   . PHE A  1 73  ? -39.696 -18.290 60.556  1.00 13.77  ? 79  PHE A O   1 
ATOM   509   C CB  . PHE A  1 73  ? -41.467 -16.344 59.409  1.00 14.20  ? 79  PHE A CB  1 
ATOM   510   C CG  . PHE A  1 73  ? -42.377 -15.690 58.406  1.00 15.64  ? 79  PHE A CG  1 
ATOM   511   C CD1 . PHE A  1 73  ? -43.330 -14.761 58.816  1.00 18.13  ? 79  PHE A CD1 1 
ATOM   512   C CD2 . PHE A  1 73  ? -42.282 -15.998 57.051  1.00 14.98  ? 79  PHE A CD2 1 
ATOM   513   C CE1 . PHE A  1 73  ? -44.180 -14.150 57.891  1.00 17.36  ? 79  PHE A CE1 1 
ATOM   514   C CE2 . PHE A  1 73  ? -43.122 -15.394 56.121  1.00 13.49  ? 79  PHE A CE2 1 
ATOM   515   C CZ  . PHE A  1 73  ? -44.073 -14.467 56.542  1.00 15.64  ? 79  PHE A CZ  1 
ATOM   516   N N   . LEU A  1 74  ? -41.374 -18.916 61.926  1.00 13.06  ? 80  LEU A N   1 
ATOM   517   C CA  . LEU A  1 74  ? -40.496 -19.483 62.960  1.00 12.21  ? 80  LEU A CA  1 
ATOM   518   C C   . LEU A  1 74  ? -39.552 -20.532 62.398  1.00 12.34  ? 80  LEU A C   1 
ATOM   519   O O   . LEU A  1 74  ? -38.406 -20.646 62.827  1.00 13.10  ? 80  LEU A O   1 
ATOM   520   C CB  . LEU A  1 74  ? -41.316 -20.085 64.096  1.00 12.16  ? 80  LEU A CB  1 
ATOM   521   C CG  . LEU A  1 74  ? -42.272 -19.160 64.845  1.00 11.49  ? 80  LEU A CG  1 
ATOM   522   C CD1 . LEU A  1 74  ? -42.973 -19.939 65.946  1.00 10.58  ? 80  LEU A CD1 1 
ATOM   523   C CD2 . LEU A  1 74  ? -41.532 -17.947 65.404  1.00 9.32   ? 80  LEU A CD2 1 
ATOM   524   N N   . GLU A  1 75  ? -40.064 -21.308 61.453  1.00 12.76  ? 81  GLU A N   1 
ATOM   525   C CA  . GLU A  1 75  ? -39.261 -22.166 60.602  1.00 13.15  ? 81  GLU A CA  1 
ATOM   526   C C   . GLU A  1 75  ? -39.710 -21.871 59.183  1.00 14.45  ? 81  GLU A C   1 
ATOM   527   O O   . GLU A  1 75  ? -40.912 -21.796 58.912  1.00 15.28  ? 81  GLU A O   1 
ATOM   528   C CB  . GLU A  1 75  ? -39.503 -23.638 60.927  1.00 12.41  ? 81  GLU A CB  1 
ATOM   529   C CG  . GLU A  1 75  ? -39.030 -24.063 62.299  1.00 12.67  ? 81  GLU A CG  1 
ATOM   530   C CD  . GLU A  1 75  ? -39.328 -25.514 62.595  1.00 15.14  ? 81  GLU A CD  1 
ATOM   531   O OE1 . GLU A  1 75  ? -38.367 -26.291 62.770  1.00 17.83  ? 81  GLU A OE1 1 
ATOM   532   O OE2 . GLU A  1 75  ? -40.521 -25.885 62.646  1.00 17.80  ? 81  GLU A OE2 1 
ATOM   533   N N   . PHE A  1 76  ? -38.751 -21.675 58.284  1.00 14.86  ? 82  PHE A N   1 
ATOM   534   C CA  . PHE A  1 76  ? -39.064 -21.400 56.888  1.00 14.87  ? 82  PHE A CA  1 
ATOM   535   C C   . PHE A  1 76  ? -37.925 -21.833 55.985  1.00 15.66  ? 82  PHE A C   1 
ATOM   536   O O   . PHE A  1 76  ? -36.781 -21.951 56.430  1.00 15.70  ? 82  PHE A O   1 
ATOM   537   C CB  . PHE A  1 76  ? -39.426 -19.920 56.665  1.00 14.77  ? 82  PHE A CB  1 
ATOM   538   C CG  . PHE A  1 76  ? -38.255 -18.974 56.727  1.00 13.81  ? 82  PHE A CG  1 
ATOM   539   C CD1 . PHE A  1 76  ? -37.626 -18.547 55.557  1.00 12.60  ? 82  PHE A CD1 1 
ATOM   540   C CD2 . PHE A  1 76  ? -37.794 -18.487 57.950  1.00 14.31  ? 82  PHE A CD2 1 
ATOM   541   C CE1 . PHE A  1 76  ? -36.542 -17.657 55.603  1.00 11.28  ? 82  PHE A CE1 1 
ATOM   542   C CE2 . PHE A  1 76  ? -36.711 -17.596 58.010  1.00 13.04  ? 82  PHE A CE2 1 
ATOM   543   C CZ  . PHE A  1 76  ? -36.085 -17.183 56.833  1.00 12.27  ? 82  PHE A CZ  1 
ATOM   544   N N   . SER A  1 77  ? -38.256 -22.069 54.719  1.00 16.20  ? 83  SER A N   1 
ATOM   545   C CA  . SER A  1 77  ? -37.295 -22.538 53.735  1.00 16.53  ? 83  SER A CA  1 
ATOM   546   C C   . SER A  1 77  ? -37.360 -21.662 52.485  1.00 16.78  ? 83  SER A C   1 
ATOM   547   O O   . SER A  1 77  ? -38.395 -21.602 51.810  1.00 17.03  ? 83  SER A O   1 
ATOM   548   C CB  . SER A  1 77  ? -37.576 -24.001 53.392  1.00 15.97  ? 83  SER A CB  1 
ATOM   549   O OG  . SER A  1 77  ? -36.698 -24.468 52.384  1.00 17.92  ? 83  SER A OG  1 
ATOM   550   N N   . SER A  1 78  ? -36.257 -20.979 52.184  1.00 16.16  ? 84  SER A N   1 
ATOM   551   C CA  . SER A  1 78  ? -36.231 -20.036 51.066  1.00 16.18  ? 84  SER A CA  1 
ATOM   552   C C   . SER A  1 78  ? -34.887 -19.978 50.346  1.00 16.30  ? 84  SER A C   1 
ATOM   553   O O   . SER A  1 78  ? -33.858 -20.366 50.895  1.00 16.49  ? 84  SER A O   1 
ATOM   554   C CB  . SER A  1 78  ? -36.616 -18.634 51.551  1.00 16.08  ? 84  SER A CB  1 
ATOM   555   O OG  . SER A  1 78  ? -36.847 -17.761 50.460  1.00 16.09  ? 84  SER A OG  1 
ATOM   556   N N   . ASP A  1 79  ? -34.918 -19.495 49.108  1.00 16.80  ? 85  ASP A N   1 
ATOM   557   C CA  . ASP A  1 79  ? -33.706 -19.156 48.362  1.00 17.35  ? 85  ASP A CA  1 
ATOM   558   C C   . ASP A  1 79  ? -33.690 -17.660 48.019  1.00 17.46  ? 85  ASP A C   1 
ATOM   559   O O   . ASP A  1 79  ? -32.700 -17.134 47.495  1.00 17.59  ? 85  ASP A O   1 
ATOM   560   C CB  . ASP A  1 79  ? -33.568 -20.020 47.100  1.00 17.41  ? 85  ASP A CB  1 
ATOM   561   C CG  . ASP A  1 79  ? -34.756 -19.894 46.155  1.00 19.98  ? 85  ASP A CG  1 
ATOM   562   O OD1 . ASP A  1 79  ? -35.683 -19.099 46.432  1.00 20.78  ? 85  ASP A OD1 1 
ATOM   563   O OD2 . ASP A  1 79  ? -34.761 -20.604 45.124  1.00 23.51  ? 85  ASP A OD2 1 
ATOM   564   N N   . LEU A  1 80  ? -34.800 -16.991 48.329  1.00 16.81  ? 86  LEU A N   1 
ATOM   565   C CA  . LEU A  1 80  ? -34.956 -15.559 48.101  1.00 16.28  ? 86  LEU A CA  1 
ATOM   566   C C   . LEU A  1 80  ? -35.806 -14.932 49.212  1.00 16.50  ? 86  LEU A C   1 
ATOM   567   O O   . LEU A  1 80  ? -37.040 -15.029 49.199  1.00 16.08  ? 86  LEU A O   1 
ATOM   568   C CB  . LEU A  1 80  ? -35.581 -15.305 46.721  1.00 15.96  ? 86  LEU A CB  1 
ATOM   569   C CG  . LEU A  1 80  ? -35.753 -13.861 46.242  1.00 14.43  ? 86  LEU A CG  1 
ATOM   570   C CD1 . LEU A  1 80  ? -34.407 -13.188 46.042  1.00 14.75  ? 86  LEU A CD1 1 
ATOM   571   C CD2 . LEU A  1 80  ? -36.555 -13.825 44.960  1.00 13.08  ? 86  LEU A CD2 1 
ATOM   572   N N   . ILE A  1 81  ? -35.135 -14.294 50.168  1.00 15.80  ? 87  ILE A N   1 
ATOM   573   C CA  . ILE A  1 81  ? -35.800 -13.684 51.318  1.00 16.05  ? 87  ILE A CA  1 
ATOM   574   C C   . ILE A  1 81  ? -36.068 -12.195 51.073  1.00 16.18  ? 87  ILE A C   1 
ATOM   575   O O   . ILE A  1 81  ? -35.136 -11.417 50.857  1.00 16.86  ? 87  ILE A O   1 
ATOM   576   C CB  . ILE A  1 81  ? -34.979 -13.894 52.620  1.00 15.88  ? 87  ILE A CB  1 
ATOM   577   C CG1 . ILE A  1 81  ? -34.839 -15.389 52.926  1.00 16.51  ? 87  ILE A CG1 1 
ATOM   578   C CG2 . ILE A  1 81  ? -35.629 -13.178 53.799  1.00 15.53  ? 87  ILE A CG2 1 
ATOM   579   C CD1 . ILE A  1 81  ? -33.645 -15.745 53.799  1.00 16.59  ? 87  ILE A CD1 1 
ATOM   580   N N   . ILE A  1 82  ? -37.342 -11.807 51.112  1.00 15.49  ? 88  ILE A N   1 
ATOM   581   C CA  . ILE A  1 82  ? -37.738 -10.416 50.878  1.00 15.02  ? 88  ILE A CA  1 
ATOM   582   C C   . ILE A  1 82  ? -38.133 -9.710  52.178  1.00 14.74  ? 88  ILE A C   1 
ATOM   583   O O   . ILE A  1 82  ? -39.126 -10.068 52.821  1.00 14.72  ? 88  ILE A O   1 
ATOM   584   C CB  . ILE A  1 82  ? -38.894 -10.294 49.847  1.00 14.89  ? 88  ILE A CB  1 
ATOM   585   C CG1 . ILE A  1 82  ? -38.562 -11.034 48.547  1.00 15.76  ? 88  ILE A CG1 1 
ATOM   586   C CG2 . ILE A  1 82  ? -39.206 -8.832  49.555  1.00 13.38  ? 88  ILE A CG2 1 
ATOM   587   C CD1 . ILE A  1 82  ? -39.101 -12.451 48.488  1.00 18.26  ? 88  ILE A CD1 1 
ATOM   588   N N   . GLU A  1 83  ? -37.347 -8.701  52.544  1.00 13.82  ? 89  GLU A N   1 
ATOM   589   C CA  . GLU A  1 83  ? -37.600 -7.886  53.725  1.00 13.65  ? 89  GLU A CA  1 
ATOM   590   C C   . GLU A  1 83  ? -38.409 -6.658  53.350  1.00 13.10  ? 89  GLU A C   1 
ATOM   591   O O   . GLU A  1 83  ? -38.178 -6.054  52.303  1.00 12.51  ? 89  GLU A O   1 
ATOM   592   C CB  . GLU A  1 83  ? -36.285 -7.455  54.363  1.00 13.82  ? 89  GLU A CB  1 
ATOM   593   C CG  . GLU A  1 83  ? -35.725 -8.435  55.368  1.00 17.57  ? 89  GLU A CG  1 
ATOM   594   C CD  . GLU A  1 83  ? -34.295 -8.111  55.738  1.00 23.89  ? 89  GLU A CD  1 
ATOM   595   O OE1 . GLU A  1 83  ? -34.082 -7.389  56.738  1.00 24.06  ? 89  GLU A OE1 1 
ATOM   596   O OE2 . GLU A  1 83  ? -33.385 -8.564  55.011  1.00 27.23  ? 89  GLU A OE2 1 
ATOM   597   N N   . ARG A  1 84  ? -39.353 -6.293  54.213  1.00 13.60  ? 90  ARG A N   1 
ATOM   598   C CA  . ARG A  1 84  ? -40.240 -5.162  53.955  1.00 14.66  ? 90  ARG A CA  1 
ATOM   599   C C   . ARG A  1 84  ? -39.988 -4.039  54.944  1.00 15.69  ? 90  ARG A C   1 
ATOM   600   O O   . ARG A  1 84  ? -39.470 -4.276  56.039  1.00 16.35  ? 90  ARG A O   1 
ATOM   601   C CB  . ARG A  1 84  ? -41.701 -5.604  54.018  1.00 14.31  ? 90  ARG A CB  1 
ATOM   602   C CG  . ARG A  1 84  ? -42.067 -6.689  53.020  1.00 15.03  ? 90  ARG A CG  1 
ATOM   603   C CD  . ARG A  1 84  ? -42.020 -6.180  51.591  1.00 16.65  ? 90  ARG A CD  1 
ATOM   604   N NE  . ARG A  1 84  ? -42.579 -7.154  50.657  1.00 21.01  ? 90  ARG A NE  1 
ATOM   605   C CZ  . ARG A  1 84  ? -42.399 -7.131  49.340  1.00 20.75  ? 90  ARG A CZ  1 
ATOM   606   N NH1 . ARG A  1 84  ? -41.660 -6.183  48.780  1.00 22.09  ? 90  ARG A NH1 1 
ATOM   607   N NH2 . ARG A  1 84  ? -42.952 -8.067  48.583  1.00 20.38  ? 90  ARG A NH2 1 
ATOM   608   N N   . ARG A  1 85  ? -40.345 -2.817  54.558  1.00 16.70  ? 91  ARG A N   1 
ATOM   609   C CA  . ARG A  1 85  ? -40.115 -1.657  55.417  1.00 18.11  ? 91  ARG A CA  1 
ATOM   610   C C   . ARG A  1 85  ? -40.838 -1.789  56.759  1.00 18.45  ? 91  ARG A C   1 
ATOM   611   O O   . ARG A  1 85  ? -40.276 -1.437  57.797  1.00 19.06  ? 91  ARG A O   1 
ATOM   612   C CB  . ARG A  1 85  ? -40.476 -0.341  54.709  1.00 18.20  ? 91  ARG A CB  1 
ATOM   613   C CG  . ARG A  1 85  ? -40.399 0.899   55.610  1.00 22.37  ? 91  ARG A CG  1 
ATOM   614   C CD  . ARG A  1 85  ? -40.394 2.206   54.828  1.00 26.53  ? 91  ARG A CD  1 
ATOM   615   N NE  . ARG A  1 85  ? -39.052 2.552   54.362  1.00 29.94  ? 91  ARG A NE  1 
ATOM   616   C CZ  . ARG A  1 85  ? -38.617 2.391   53.115  1.00 29.62  ? 91  ARG A CZ  1 
ATOM   617   N NH1 . ARG A  1 85  ? -39.417 1.894   52.179  1.00 32.05  ? 91  ARG A NH1 1 
ATOM   618   N NH2 . ARG A  1 85  ? -37.376 2.733   52.800  1.00 27.94  ? 91  ARG A NH2 1 
ATOM   619   N N   . GLU A  1 86  ? -42.059 -2.325  56.738  1.00 18.41  ? 92  GLU A N   1 
ATOM   620   C CA  . GLU A  1 86  ? -42.869 -2.437  57.958  1.00 18.71  ? 92  GLU A CA  1 
ATOM   621   C C   . GLU A  1 86  ? -42.448 -3.565  58.912  1.00 17.87  ? 92  GLU A C   1 
ATOM   622   O O   . GLU A  1 86  ? -42.964 -3.658  60.033  1.00 17.89  ? 92  GLU A O   1 
ATOM   623   C CB  . GLU A  1 86  ? -44.373 -2.507  57.633  1.00 19.39  ? 92  GLU A CB  1 
ATOM   624   C CG  . GLU A  1 86  ? -44.889 -3.864  57.144  1.00 23.48  ? 92  GLU A CG  1 
ATOM   625   C CD  . GLU A  1 86  ? -44.771 -4.057  55.640  1.00 28.48  ? 92  GLU A CD  1 
ATOM   626   O OE1 . GLU A  1 86  ? -43.982 -3.336  54.984  1.00 30.96  ? 92  GLU A OE1 1 
ATOM   627   O OE2 . GLU A  1 86  ? -45.475 -4.945  55.114  1.00 30.21  ? 92  GLU A OE2 1 
ATOM   628   N N   . GLY A  1 87  ? -41.516 -4.409  58.465  1.00 16.83  ? 93  GLY A N   1 
ATOM   629   C CA  . GLY A  1 87  ? -40.971 -5.498  59.286  1.00 15.21  ? 93  GLY A CA  1 
ATOM   630   C C   . GLY A  1 87  ? -40.417 -5.043  60.627  1.00 13.86  ? 93  GLY A C   1 
ATOM   631   O O   . GLY A  1 87  ? -39.779 -3.995  60.720  1.00 13.31  ? 93  GLY A O   1 
ATOM   632   N N   . THR A  1 88  ? -40.669 -5.845  61.659  1.00 13.76  ? 94  THR A N   1 
ATOM   633   C CA  . THR A  1 88  ? -40.307 -5.535  63.047  1.00 13.19  ? 94  THR A CA  1 
ATOM   634   C C   . THR A  1 88  ? -39.806 -6.817  63.714  1.00 13.35  ? 94  THR A C   1 
ATOM   635   O O   . THR A  1 88  ? -40.433 -7.869  63.595  1.00 12.91  ? 94  THR A O   1 
ATOM   636   C CB  . THR A  1 88  ? -41.528 -4.950  63.815  1.00 12.65  ? 94  THR A CB  1 
ATOM   637   O OG1 . THR A  1 88  ? -41.713 -3.581  63.444  1.00 12.73  ? 94  THR A OG1 1 
ATOM   638   C CG2 . THR A  1 88  ? -41.345 -5.003  65.312  1.00 13.61  ? 94  THR A CG2 1 
ATOM   639   N N   . ASP A  1 89  ? -38.674 -6.719  64.406  1.00 14.49  ? 95  ASP A N   1 
ATOM   640   C CA  . ASP A  1 89  ? -38.034 -7.878  65.038  1.00 14.82  ? 95  ASP A CA  1 
ATOM   641   C C   . ASP A  1 89  ? -38.591 -8.178  66.417  1.00 14.90  ? 95  ASP A C   1 
ATOM   642   O O   . ASP A  1 89  ? -38.406 -9.277  66.937  1.00 15.92  ? 95  ASP A O   1 
ATOM   643   C CB  . ASP A  1 89  ? -36.531 -7.644  65.193  1.00 14.55  ? 95  ASP A CB  1 
ATOM   644   C CG  . ASP A  1 89  ? -35.832 -7.392  63.879  1.00 17.16  ? 95  ASP A CG  1 
ATOM   645   O OD1 . ASP A  1 89  ? -36.255 -7.955  62.844  1.00 20.27  ? 95  ASP A OD1 1 
ATOM   646   O OD2 . ASP A  1 89  ? -34.834 -6.640  63.894  1.00 19.84  ? 95  ASP A OD2 1 
ATOM   647   N N   . ILE A  1 90  ? -39.255 -7.197  67.014  1.00 14.81  ? 96  ILE A N   1 
ATOM   648   C CA  . ILE A  1 90  ? -39.598 -7.265  68.428  1.00 15.37  ? 96  ILE A CA  1 
ATOM   649   C C   . ILE A  1 90  ? -41.082 -7.024  68.711  1.00 16.43  ? 96  ILE A C   1 
ATOM   650   O O   . ILE A  1 90  ? -41.825 -6.549  67.851  1.00 16.65  ? 96  ILE A O   1 
ATOM   651   C CB  . ILE A  1 90  ? -38.706 -6.294  69.272  1.00 15.43  ? 96  ILE A CB  1 
ATOM   652   C CG1 . ILE A  1 90  ? -38.730 -4.861  68.721  1.00 14.15  ? 96  ILE A CG1 1 
ATOM   653   C CG2 . ILE A  1 90  ? -37.267 -6.781  69.313  1.00 14.23  ? 96  ILE A CG2 1 
ATOM   654   C CD1 . ILE A  1 90  ? -39.784 -3.962  69.330  1.00 15.06  ? 96  ILE A CD1 1 
ATOM   655   N N   . CYS A  1 91  ? -41.510 -7.386  69.916  1.00 16.92  ? 97  CYS A N   1 
ATOM   656   C CA  . CYS A  1 91  ? -42.791 -6.936  70.435  1.00 17.46  ? 97  CYS A CA  1 
ATOM   657   C C   . CYS A  1 91  ? -42.508 -6.108  71.679  1.00 18.07  ? 97  CYS A C   1 
ATOM   658   O O   . CYS A  1 91  ? -42.774 -4.904  71.708  1.00 19.08  ? 97  CYS A O   1 
ATOM   659   C CB  . CYS A  1 91  ? -43.741 -8.107  70.714  1.00 17.79  ? 97  CYS A CB  1 
ATOM   660   S SG  . CYS A  1 91  ? -42.998 -9.609  71.405  1.00 20.47  ? 97  CYS A SG  1 
ATOM   661   N N   . TYR A  1 92  ? -41.937 -6.750  72.692  1.00 18.02  ? 98  TYR A N   1 
ATOM   662   C CA  . TYR A  1 92  ? -41.398 -6.053  73.852  1.00 18.46  ? 98  TYR A CA  1 
ATOM   663   C C   . TYR A  1 92  ? -40.250 -5.150  73.381  1.00 18.46  ? 98  TYR A C   1 
ATOM   664   O O   . TYR A  1 92  ? -39.528 -5.520  72.456  1.00 18.14  ? 98  TYR A O   1 
ATOM   665   C CB  . TYR A  1 92  ? -40.883 -7.082  74.850  1.00 18.84  ? 98  TYR A CB  1 
ATOM   666   C CG  . TYR A  1 92  ? -40.776 -6.602  76.276  1.00 18.64  ? 98  TYR A CG  1 
ATOM   667   C CD1 . TYR A  1 92  ? -41.890 -6.587  77.109  1.00 18.83  ? 98  TYR A CD1 1 
ATOM   668   C CD2 . TYR A  1 92  ? -39.553 -6.189  76.801  1.00 19.12  ? 98  TYR A CD2 1 
ATOM   669   C CE1 . TYR A  1 92  ? -41.792 -6.158  78.429  1.00 21.19  ? 98  TYR A CE1 1 
ATOM   670   C CE2 . TYR A  1 92  ? -39.442 -5.763  78.117  1.00 19.61  ? 98  TYR A CE2 1 
ATOM   671   C CZ  . TYR A  1 92  ? -40.564 -5.750  78.924  1.00 20.00  ? 98  TYR A CZ  1 
ATOM   672   O OH  . TYR A  1 92  ? -40.459 -5.330  80.224  1.00 22.15  ? 98  TYR A OH  1 
ATOM   673   N N   . PRO A  1 93  ? -40.080 -3.962  73.999  1.00 18.70  ? 99  PRO A N   1 
ATOM   674   C CA  . PRO A  1 93  ? -38.993 -3.072  73.562  1.00 18.60  ? 99  PRO A CA  1 
ATOM   675   C C   . PRO A  1 93  ? -37.618 -3.733  73.653  1.00 18.92  ? 99  PRO A C   1 
ATOM   676   O O   . PRO A  1 93  ? -37.367 -4.527  74.562  1.00 19.03  ? 99  PRO A O   1 
ATOM   677   C CB  . PRO A  1 93  ? -39.080 -1.897  74.545  1.00 18.18  ? 99  PRO A CB  1 
ATOM   678   C CG  . PRO A  1 93  ? -40.499 -1.897  75.005  1.00 17.93  ? 99  PRO A CG  1 
ATOM   679   C CD  . PRO A  1 93  ? -40.902 -3.345  75.057  1.00 18.73  ? 99  PRO A CD  1 
ATOM   680   N N   . GLY A  1 94  ? -36.743 -3.413  72.708  1.00 19.20  ? 100 GLY A N   1 
ATOM   681   C CA  . GLY A  1 94  ? -35.393 -3.954  72.707  1.00 19.83  ? 100 GLY A CA  1 
ATOM   682   C C   . GLY A  1 94  ? -34.763 -3.985  71.334  1.00 20.76  ? 100 GLY A C   1 
ATOM   683   O O   . GLY A  1 94  ? -35.365 -3.563  70.350  1.00 20.59  ? 100 GLY A O   1 
ATOM   684   N N   . ARG A  1 95  ? -33.534 -4.482  71.277  1.00 22.52  ? 101 ARG A N   1 
ATOM   685   C CA  . ARG A  1 95  ? -32.811 -4.628  70.020  1.00 24.01  ? 101 ARG A CA  1 
ATOM   686   C C   . ARG A  1 95  ? -31.812 -5.775  70.121  1.00 23.50  ? 101 ARG A C   1 
ATOM   687   O O   . ARG A  1 95  ? -31.402 -6.162  71.218  1.00 23.23  ? 101 ARG A O   1 
ATOM   688   C CB  . ARG A  1 95  ? -32.100 -3.319  69.628  1.00 24.48  ? 101 ARG A CB  1 
ATOM   689   C CG  . ARG A  1 95  ? -31.016 -2.863  70.598  1.00 29.65  ? 101 ARG A CG  1 
ATOM   690   C CD  . ARG A  1 95  ? -30.313 -1.596  70.113  1.00 40.43  ? 101 ARG A CD  1 
ATOM   691   N NE  . ARG A  1 95  ? -29.177 -1.235  70.968  1.00 46.76  ? 101 ARG A NE  1 
ATOM   692   C CZ  . ARG A  1 95  ? -29.199 -0.296  71.916  1.00 49.99  ? 101 ARG A CZ  1 
ATOM   693   N NH1 . ARG A  1 95  ? -30.300 0.410   72.153  1.00 50.62  ? 101 ARG A NH1 1 
ATOM   694   N NH2 . ARG A  1 95  ? -28.108 -0.056  72.630  1.00 51.02  ? 101 ARG A NH2 1 
ATOM   695   N N   . PHE A  1 96  ? -31.448 -6.327  68.968  1.00 23.09  ? 102 PHE A N   1 
ATOM   696   C CA  . PHE A  1 96  ? -30.351 -7.274  68.884  1.00 22.52  ? 102 PHE A CA  1 
ATOM   697   C C   . PHE A  1 96  ? -29.046 -6.491  68.855  1.00 22.52  ? 102 PHE A C   1 
ATOM   698   O O   . PHE A  1 96  ? -28.957 -5.458  68.190  1.00 22.78  ? 102 PHE A O   1 
ATOM   699   C CB  . PHE A  1 96  ? -30.463 -8.103  67.605  1.00 22.53  ? 102 PHE A CB  1 
ATOM   700   C CG  . PHE A  1 96  ? -31.471 -9.216  67.675  1.00 20.00  ? 102 PHE A CG  1 
ATOM   701   C CD1 . PHE A  1 96  ? -32.835 -8.954  67.549  1.00 17.73  ? 102 PHE A CD1 1 
ATOM   702   C CD2 . PHE A  1 96  ? -31.052 -10.534 67.835  1.00 15.01  ? 102 PHE A CD2 1 
ATOM   703   C CE1 . PHE A  1 96  ? -33.767 -9.989  67.602  1.00 19.05  ? 102 PHE A CE1 1 
ATOM   704   C CE2 . PHE A  1 96  ? -31.972 -11.577 67.886  1.00 15.69  ? 102 PHE A CE2 1 
ATOM   705   C CZ  . PHE A  1 96  ? -33.333 -11.306 67.769  1.00 17.39  ? 102 PHE A CZ  1 
ATOM   706   N N   . THR A  1 97  ? -28.043 -6.964  69.589  1.00 22.33  ? 103 THR A N   1 
ATOM   707   C CA  . THR A  1 97  ? -26.688 -6.440  69.433  1.00 22.20  ? 103 THR A CA  1 
ATOM   708   C C   . THR A  1 97  ? -26.063 -7.104  68.208  1.00 21.58  ? 103 THR A C   1 
ATOM   709   O O   . THR A  1 97  ? -26.308 -8.286  67.950  1.00 20.71  ? 103 THR A O   1 
ATOM   710   C CB  . THR A  1 97  ? -25.815 -6.654  70.691  1.00 22.26  ? 103 THR A CB  1 
ATOM   711   O OG1 . THR A  1 97  ? -25.795 -8.042  71.043  1.00 22.64  ? 103 THR A OG1 1 
ATOM   712   C CG2 . THR A  1 97  ? -26.355 -5.841  71.859  1.00 23.84  ? 103 THR A CG2 1 
ATOM   713   N N   . ASN A  1 98  ? -25.281 -6.336  67.449  1.00 21.58  ? 104 ASN A N   1 
ATOM   714   C CA  . ASN A  1 98  ? -24.753 -6.789  66.162  1.00 22.64  ? 104 ASN A CA  1 
ATOM   715   C C   . ASN A  1 98  ? -25.861 -7.160  65.181  1.00 22.88  ? 104 ASN A C   1 
ATOM   716   O O   . ASN A  1 98  ? -25.685 -8.051  64.344  1.00 23.64  ? 104 ASN A O   1 
ATOM   717   C CB  . ASN A  1 98  ? -23.807 -7.982  66.346  1.00 23.46  ? 104 ASN A CB  1 
ATOM   718   C CG  . ASN A  1 98  ? -22.359 -7.570  66.442  1.00 26.22  ? 104 ASN A CG  1 
ATOM   719   O OD1 . ASN A  1 98  ? -21.783 -7.544  67.529  1.00 27.08  ? 104 ASN A OD1 1 
ATOM   720   N ND2 . ASN A  1 98  ? -21.755 -7.247  65.299  1.00 28.63  ? 104 ASN A ND2 1 
ATOM   721   N N   . GLU A  1 99  ? -26.997 -6.472  65.284  1.00 22.38  ? 105 GLU A N   1 
ATOM   722   C CA  . GLU A  1 99  ? -28.180 -6.789  64.477  1.00 22.49  ? 105 GLU A CA  1 
ATOM   723   C C   . GLU A  1 99  ? -27.887 -6.887  62.979  1.00 22.03  ? 105 GLU A C   1 
ATOM   724   O O   . GLU A  1 99  ? -28.385 -7.788  62.305  1.00 21.62  ? 105 GLU A O   1 
ATOM   725   C CB  . GLU A  1 99  ? -29.338 -5.808  64.753  1.00 22.68  ? 105 GLU A CB  1 
ATOM   726   C CG  . GLU A  1 99  ? -28.973 -4.326  64.694  1.00 23.38  ? 105 GLU A CG  1 
ATOM   727   C CD  . GLU A  1 99  ? -30.172 -3.415  64.862  1.00 23.77  ? 105 GLU A CD  1 
ATOM   728   O OE1 . GLU A  1 99  ? -30.960 -3.279  63.903  1.00 25.02  ? 105 GLU A OE1 1 
ATOM   729   O OE2 . GLU A  1 99  ? -30.318 -2.818  65.949  1.00 26.78  ? 105 GLU A OE2 1 
ATOM   730   N N   . GLU A  1 100 ? -27.064 -5.973  62.473  1.00 22.49  ? 106 GLU A N   1 
ATOM   731   C CA  . GLU A  1 100 ? -26.818 -5.884  61.037  1.00 23.20  ? 106 GLU A CA  1 
ATOM   732   C C   . GLU A  1 100 ? -25.993 -7.043  60.486  1.00 23.37  ? 106 GLU A C   1 
ATOM   733   O O   . GLU A  1 100 ? -26.240 -7.502  59.373  1.00 23.98  ? 106 GLU A O   1 
ATOM   734   C CB  . GLU A  1 100 ? -26.179 -4.546  60.664  1.00 22.52  ? 106 GLU A CB  1 
ATOM   735   C CG  . GLU A  1 100 ? -26.451 -4.138  59.226  1.00 24.48  ? 106 GLU A CG  1 
ATOM   736   C CD  . GLU A  1 100 ? -27.938 -3.989  58.925  1.00 27.07  ? 106 GLU A CD  1 
ATOM   737   O OE1 . GLU A  1 100 ? -28.679 -3.481  59.796  1.00 26.46  ? 106 GLU A OE1 1 
ATOM   738   O OE2 . GLU A  1 100 ? -28.367 -4.375  57.814  1.00 28.17  ? 106 GLU A OE2 1 
ATOM   739   N N   . SER A  1 101 ? -25.019 -7.511  61.259  1.00 23.34  ? 107 SER A N   1 
ATOM   740   C CA  . SER A  1 101 ? -24.204 -8.645  60.832  1.00 23.67  ? 107 SER A CA  1 
ATOM   741   C C   . SER A  1 101 ? -24.975 -9.955  60.946  1.00 23.87  ? 107 SER A C   1 
ATOM   742   O O   . SER A  1 101 ? -24.718 -10.893 60.188  1.00 24.76  ? 107 SER A O   1 
ATOM   743   C CB  . SER A  1 101 ? -22.876 -8.706  61.594  1.00 23.49  ? 107 SER A CB  1 
ATOM   744   O OG  . SER A  1 101 ? -23.061 -8.534  62.989  1.00 25.85  ? 107 SER A OG  1 
ATOM   745   N N   . LEU A  1 102 ? -25.920 -10.014 61.883  1.00 23.46  ? 108 LEU A N   1 
ATOM   746   C CA  . LEU A  1 102 ? -26.808 -11.169 62.007  1.00 22.97  ? 108 LEU A CA  1 
ATOM   747   C C   . LEU A  1 102 ? -27.810 -11.217 60.851  1.00 23.28  ? 108 LEU A C   1 
ATOM   748   O O   . LEU A  1 102 ? -28.082 -12.293 60.304  1.00 23.64  ? 108 LEU A O   1 
ATOM   749   C CB  . LEU A  1 102 ? -27.531 -11.173 63.358  1.00 22.78  ? 108 LEU A CB  1 
ATOM   750   C CG  . LEU A  1 102 ? -28.333 -12.427 63.739  1.00 21.68  ? 108 LEU A CG  1 
ATOM   751   C CD1 . LEU A  1 102 ? -27.473 -13.689 63.708  1.00 21.72  ? 108 LEU A CD1 1 
ATOM   752   C CD2 . LEU A  1 102 ? -28.975 -12.255 65.108  1.00 18.92  ? 108 LEU A CD2 1 
ATOM   753   N N   . ARG A  1 103 ? -28.345 -10.053 60.481  1.00 22.71  ? 109 ARG A N   1 
ATOM   754   C CA  . ARG A  1 103 ? -29.221 -9.940  59.317  1.00 22.26  ? 109 ARG A CA  1 
ATOM   755   C C   . ARG A  1 103 ? -28.516 -10.445 58.062  1.00 22.64  ? 109 ARG A C   1 
ATOM   756   O O   . ARG A  1 103 ? -29.112 -11.156 57.249  1.00 22.72  ? 109 ARG A O   1 
ATOM   757   C CB  . ARG A  1 103 ? -29.694 -8.499  59.118  1.00 21.60  ? 109 ARG A CB  1 
ATOM   758   C CG  . ARG A  1 103 ? -30.789 -8.082  60.078  1.00 22.08  ? 109 ARG A CG  1 
ATOM   759   C CD  . ARG A  1 103 ? -31.504 -6.819  59.628  1.00 18.72  ? 109 ARG A CD  1 
ATOM   760   N NE  . ARG A  1 103 ? -32.370 -6.300  60.684  1.00 18.58  ? 109 ARG A NE  1 
ATOM   761   C CZ  . ARG A  1 103 ? -32.029 -5.335  61.536  1.00 18.94  ? 109 ARG A CZ  1 
ATOM   762   N NH1 . ARG A  1 103 ? -30.834 -4.762  61.463  1.00 18.27  ? 109 ARG A NH1 1 
ATOM   763   N NH2 . ARG A  1 103 ? -32.889 -4.934  62.462  1.00 15.84  ? 109 ARG A NH2 1 
ATOM   764   N N   . GLN A  1 104 ? -27.241 -10.089 57.923  1.00 22.67  ? 110 GLN A N   1 
ATOM   765   C CA  . GLN A  1 104 ? -26.443 -10.499 56.772  1.00 23.03  ? 110 GLN A CA  1 
ATOM   766   C C   . GLN A  1 104 ? -26.272 -12.018 56.719  1.00 22.78  ? 110 GLN A C   1 
ATOM   767   O O   . GLN A  1 104 ? -26.383 -12.616 55.647  1.00 23.56  ? 110 GLN A O   1 
ATOM   768   C CB  . GLN A  1 104 ? -25.092 -9.771  56.759  1.00 23.33  ? 110 GLN A CB  1 
ATOM   769   C CG  . GLN A  1 104 ? -25.208 -8.274  56.411  1.00 24.90  ? 110 GLN A CG  1 
ATOM   770   C CD  . GLN A  1 104 ? -24.002 -7.436  56.844  1.00 25.99  ? 110 GLN A CD  1 
ATOM   771   O OE1 . GLN A  1 104 ? -22.994 -7.958  57.319  1.00 28.41  ? 110 GLN A OE1 1 
ATOM   772   N NE2 . GLN A  1 104 ? -24.112 -6.124  56.678  1.00 27.18  ? 110 GLN A NE2 1 
ATOM   773   N N   . ILE A  1 105 ? -26.036 -12.638 57.874  1.00 21.94  ? 111 ILE A N   1 
ATOM   774   C CA  . ILE A  1 105 ? -25.900 -14.097 57.955  1.00 21.17  ? 111 ILE A CA  1 
ATOM   775   C C   . ILE A  1 105 ? -27.211 -14.796 57.587  1.00 21.23  ? 111 ILE A C   1 
ATOM   776   O O   . ILE A  1 105 ? -27.211 -15.776 56.829  1.00 21.36  ? 111 ILE A O   1 
ATOM   777   C CB  . ILE A  1 105 ? -25.426 -14.559 59.355  1.00 20.73  ? 111 ILE A CB  1 
ATOM   778   C CG1 . ILE A  1 105 ? -24.060 -13.952 59.685  1.00 21.42  ? 111 ILE A CG1 1 
ATOM   779   C CG2 . ILE A  1 105 ? -25.350 -16.082 59.428  1.00 20.11  ? 111 ILE A CG2 1 
ATOM   780   C CD1 . ILE A  1 105 ? -23.672 -14.032 61.154  1.00 23.53  ? 111 ILE A CD1 1 
ATOM   781   N N   . LEU A  1 106 ? -28.319 -14.277 58.117  1.00 20.59  ? 112 LEU A N   1 
ATOM   782   C CA  . LEU A  1 106 ? -29.643 -14.860 57.900  1.00 19.66  ? 112 LEU A CA  1 
ATOM   783   C C   . LEU A  1 106 ? -30.143 -14.731 56.466  1.00 19.59  ? 112 LEU A C   1 
ATOM   784   O O   . LEU A  1 106 ? -30.891 -15.587 55.991  1.00 20.95  ? 112 LEU A O   1 
ATOM   785   C CB  . LEU A  1 106 ? -30.671 -14.248 58.853  1.00 19.55  ? 112 LEU A CB  1 
ATOM   786   C CG  . LEU A  1 106 ? -30.767 -14.768 60.290  1.00 19.59  ? 112 LEU A CG  1 
ATOM   787   C CD1 . LEU A  1 106 ? -31.929 -14.087 60.993  1.00 22.90  ? 112 LEU A CD1 1 
ATOM   788   C CD2 . LEU A  1 106 ? -30.937 -16.280 60.344  1.00 14.86  ? 112 LEU A CD2 1 
ATOM   789   N N   . ARG A  1 107 ? -29.737 -13.662 55.785  1.00 18.52  ? 113 ARG A N   1 
ATOM   790   C CA  . ARG A  1 107 ? -30.171 -13.412 54.411  1.00 17.36  ? 113 ARG A CA  1 
ATOM   791   C C   . ARG A  1 107 ? -29.708 -14.497 53.453  1.00 17.98  ? 113 ARG A C   1 
ATOM   792   O O   . ARG A  1 107 ? -30.381 -14.777 52.467  1.00 19.40  ? 113 ARG A O   1 
ATOM   793   C CB  . ARG A  1 107 ? -29.668 -12.053 53.925  1.00 17.33  ? 113 ARG A CB  1 
ATOM   794   C CG  . ARG A  1 107 ? -30.531 -10.891 54.346  1.00 12.61  ? 113 ARG A CG  1 
ATOM   795   C CD  . ARG A  1 107 ? -29.779 -9.585  54.249  1.00 12.17  ? 113 ARG A CD  1 
ATOM   796   N NE  . ARG A  1 107 ? -30.603 -8.490  54.744  1.00 14.57  ? 113 ARG A NE  1 
ATOM   797   C CZ  . ARG A  1 107 ? -30.134 -7.355  55.249  1.00 13.13  ? 113 ARG A CZ  1 
ATOM   798   N NH1 . ARG A  1 107 ? -28.828 -7.145  55.332  1.00 10.64  ? 113 ARG A NH1 1 
ATOM   799   N NH2 . ARG A  1 107 ? -30.982 -6.428  55.679  1.00 14.49  ? 113 ARG A NH2 1 
ATOM   800   N N   . ARG A  1 108 ? -28.560 -15.100 53.749  1.00 18.39  ? 114 ARG A N   1 
ATOM   801   C CA  . ARG A  1 108 ? -27.977 -16.134 52.894  1.00 19.16  ? 114 ARG A CA  1 
ATOM   802   C C   . ARG A  1 108 ? -28.095 -17.541 53.495  1.00 19.39  ? 114 ARG A C   1 
ATOM   803   O O   . ARG A  1 108 ? -27.495 -18.495 52.992  1.00 20.28  ? 114 ARG A O   1 
ATOM   804   C CB  . ARG A  1 108 ? -26.514 -15.792 52.567  1.00 19.29  ? 114 ARG A CB  1 
ATOM   805   C CG  . ARG A  1 108 ? -25.663 -15.474 53.784  1.00 20.14  ? 114 ARG A CG  1 
ATOM   806   C CD  . ARG A  1 108 ? -24.198 -15.239 53.438  1.00 20.61  ? 114 ARG A CD  1 
ATOM   807   N NE  . ARG A  1 108 ? -23.426 -14.979 54.653  1.00 22.01  ? 114 ARG A NE  1 
ATOM   808   C CZ  . ARG A  1 108 ? -22.948 -13.791 55.015  1.00 20.06  ? 114 ARG A CZ  1 
ATOM   809   N NH1 . ARG A  1 108 ? -23.126 -12.725 54.243  1.00 16.30  ? 114 ARG A NH1 1 
ATOM   810   N NH2 . ARG A  1 108 ? -22.272 -13.675 56.152  1.00 21.02  ? 114 ARG A NH2 1 
ATOM   811   N N   . SER A  1 109 ? -28.891 -17.663 54.554  1.00 19.13  ? 115 SER A N   1 
ATOM   812   C CA  . SER A  1 109 ? -29.023 -18.907 55.312  1.00 18.97  ? 115 SER A CA  1 
ATOM   813   C C   . SER A  1 109 ? -29.762 -20.023 54.574  1.00 18.16  ? 115 SER A C   1 
ATOM   814   O O   . SER A  1 109 ? -29.593 -21.200 54.893  1.00 18.40  ? 115 SER A O   1 
ATOM   815   C CB  . SER A  1 109 ? -29.761 -18.629 56.620  1.00 19.82  ? 115 SER A CB  1 
ATOM   816   O OG  . SER A  1 109 ? -31.149 -18.447 56.384  1.00 20.66  ? 115 SER A OG  1 
ATOM   817   N N   . GLY A  1 110 ? -30.600 -19.654 53.610  1.00 17.17  ? 116 GLY A N   1 
ATOM   818   C CA  . GLY A  1 110 ? -31.482 -20.617 52.962  1.00 16.20  ? 116 GLY A CA  1 
ATOM   819   C C   . GLY A  1 110 ? -32.683 -20.961 53.828  1.00 16.15  ? 116 GLY A C   1 
ATOM   820   O O   . GLY A  1 110 ? -33.408 -21.914 53.545  1.00 16.26  ? 116 GLY A O   1 
ATOM   821   N N   . GLY A  1 111 ? -32.900 -20.177 54.881  1.00 15.88  ? 117 GLY A N   1 
ATOM   822   C CA  . GLY A  1 111 ? -33.997 -20.415 55.811  1.00 16.16  ? 117 GLY A CA  1 
ATOM   823   C C   . GLY A  1 111 ? -33.492 -21.023 57.102  1.00 16.74  ? 117 GLY A C   1 
ATOM   824   O O   . GLY A  1 111 ? -32.283 -21.186 57.281  1.00 17.30  ? 117 GLY A O   1 
ATOM   825   N N   . ILE A  1 112 ? -34.413 -21.358 58.004  1.00 16.44  ? 118 ILE A N   1 
ATOM   826   C CA  . ILE A  1 112 ? -34.043 -21.893 59.317  1.00 16.26  ? 118 ILE A CA  1 
ATOM   827   C C   . ILE A  1 112 ? -34.911 -23.070 59.767  1.00 17.05  ? 118 ILE A C   1 
ATOM   828   O O   . ILE A  1 112 ? -36.095 -23.159 59.431  1.00 17.45  ? 118 ILE A O   1 
ATOM   829   C CB  . ILE A  1 112 ? -34.047 -20.796 60.428  1.00 16.25  ? 118 ILE A CB  1 
ATOM   830   C CG1 . ILE A  1 112 ? -35.436 -20.158 60.573  1.00 16.30  ? 118 ILE A CG1 1 
ATOM   831   C CG2 . ILE A  1 112 ? -32.957 -19.749 60.177  1.00 14.00  ? 118 ILE A CG2 1 
ATOM   832   C CD1 . ILE A  1 112 ? -35.565 -19.201 61.741  1.00 13.52  ? 118 ILE A CD1 1 
ATOM   833   N N   . GLY A  1 113 ? -34.290 -23.973 60.521  1.00 17.41  ? 119 GLY A N   1 
ATOM   834   C CA  . GLY A  1 113 ? -34.984 -25.054 61.211  1.00 17.46  ? 119 GLY A CA  1 
ATOM   835   C C   . GLY A  1 113 ? -34.738 -24.915 62.704  1.00 18.00  ? 119 GLY A C   1 
ATOM   836   O O   . GLY A  1 113 ? -33.635 -24.550 63.126  1.00 17.85  ? 119 GLY A O   1 
ATOM   837   N N   . LYS A  1 114 ? -35.768 -25.191 63.503  1.00 17.13  ? 120 LYS A N   1 
ATOM   838   C CA  . LYS A  1 114 ? -35.676 -25.062 64.953  1.00 16.15  ? 120 LYS A CA  1 
ATOM   839   C C   . LYS A  1 114 ? -35.562 -26.414 65.659  1.00 16.69  ? 120 LYS A C   1 
ATOM   840   O O   . LYS A  1 114 ? -36.182 -27.398 65.249  1.00 16.89  ? 120 LYS A O   1 
ATOM   841   C CB  . LYS A  1 114 ? -36.880 -24.291 65.502  1.00 16.17  ? 120 LYS A CB  1 
ATOM   842   C CG  . LYS A  1 114 ? -36.981 -22.818 65.086  1.00 14.25  ? 120 LYS A CG  1 
ATOM   843   C CD  . LYS A  1 114 ? -35.805 -21.993 65.592  1.00 13.62  ? 120 LYS A CD  1 
ATOM   844   C CE  . LYS A  1 114 ? -36.194 -20.570 65.984  1.00 10.85  ? 120 LYS A CE  1 
ATOM   845   N NZ  . LYS A  1 114 ? -37.202 -19.933 65.095  1.00 9.34   ? 120 LYS A NZ  1 
ATOM   846   N N   . GLU A  1 115 ? -34.762 -26.451 66.720  1.00 17.04  ? 121 GLU A N   1 
ATOM   847   C CA  . GLU A  1 115 ? -34.650 -27.634 67.565  1.00 17.92  ? 121 GLU A CA  1 
ATOM   848   C C   . GLU A  1 115 ? -34.676 -27.245 69.037  1.00 18.15  ? 121 GLU A C   1 
ATOM   849   O O   . GLU A  1 115 ? -34.046 -26.266 69.437  1.00 18.46  ? 121 GLU A O   1 
ATOM   850   C CB  . GLU A  1 115 ? -33.375 -28.417 67.246  1.00 18.47  ? 121 GLU A CB  1 
ATOM   851   C CG  . GLU A  1 115 ? -33.227 -29.708 68.051  1.00 22.05  ? 121 GLU A CG  1 
ATOM   852   C CD  . GLU A  1 115 ? -32.268 -30.703 67.425  1.00 26.90  ? 121 GLU A CD  1 
ATOM   853   O OE1 . GLU A  1 115 ? -32.134 -30.717 66.181  1.00 27.13  ? 121 GLU A OE1 1 
ATOM   854   O OE2 . GLU A  1 115 ? -31.654 -31.485 68.184  1.00 30.69  ? 121 GLU A OE2 1 
ATOM   855   N N   . SER A  1 116 ? -35.412 -28.018 69.831  1.00 18.37  ? 122 SER A N   1 
ATOM   856   C CA  . SER A  1 116 ? -35.514 -27.796 71.271  1.00 18.44  ? 122 SER A CA  1 
ATOM   857   C C   . SER A  1 116 ? -34.145 -27.948 71.930  1.00 18.53  ? 122 SER A C   1 
ATOM   858   O O   . SER A  1 116 ? -33.458 -28.953 71.727  1.00 18.46  ? 122 SER A O   1 
ATOM   859   C CB  . SER A  1 116 ? -36.526 -28.773 71.892  1.00 18.27  ? 122 SER A CB  1 
ATOM   860   O OG  . SER A  1 116 ? -36.564 -28.668 73.307  1.00 17.15  ? 122 SER A OG  1 
ATOM   861   N N   . MET A  1 117 ? -33.747 -26.940 72.704  1.00 18.05  ? 123 MET A N   1 
ATOM   862   C CA  . MET A  1 117 ? -32.484 -26.992 73.435  1.00 18.16  ? 123 MET A CA  1 
ATOM   863   C C   . MET A  1 117 ? -32.572 -27.878 74.679  1.00 18.41  ? 123 MET A C   1 
ATOM   864   O O   . MET A  1 117 ? -31.549 -28.229 75.269  1.00 18.37  ? 123 MET A O   1 
ATOM   865   C CB  . MET A  1 117 ? -32.000 -25.589 73.790  1.00 17.72  ? 123 MET A CB  1 
ATOM   866   C CG  . MET A  1 117 ? -31.341 -24.882 72.628  1.00 18.57  ? 123 MET A CG  1 
ATOM   867   S SD  . MET A  1 117 ? -30.960 -23.156 72.955  1.00 23.49  ? 123 MET A SD  1 
ATOM   868   C CE  . MET A  1 117 ? -29.467 -23.293 73.934  1.00 22.62  ? 123 MET A CE  1 
ATOM   869   N N   . GLY A  1 118 ? -33.796 -28.235 75.062  1.00 18.35  ? 124 GLY A N   1 
ATOM   870   C CA  . GLY A  1 118 ? -34.033 -29.185 76.146  1.00 18.67  ? 124 GLY A CA  1 
ATOM   871   C C   . GLY A  1 118 ? -33.723 -28.691 77.546  1.00 19.11  ? 124 GLY A C   1 
ATOM   872   O O   . GLY A  1 118 ? -33.389 -29.488 78.422  1.00 19.62  ? 124 GLY A O   1 
ATOM   873   N N   . PHE A  1 119 ? -33.823 -27.382 77.763  1.00 19.53  ? 125 PHE A N   1 
ATOM   874   C CA  . PHE A  1 119 ? -33.674 -26.820 79.100  1.00 19.60  ? 125 PHE A CA  1 
ATOM   875   C C   . PHE A  1 119 ? -34.958 -27.025 79.887  1.00 20.57  ? 125 PHE A C   1 
ATOM   876   O O   . PHE A  1 119 ? -36.029 -26.580 79.468  1.00 20.82  ? 125 PHE A O   1 
ATOM   877   C CB  . PHE A  1 119 ? -33.348 -25.321 79.057  1.00 19.44  ? 125 PHE A CB  1 
ATOM   878   C CG  . PHE A  1 119 ? -31.957 -24.997 78.573  1.00 18.08  ? 125 PHE A CG  1 
ATOM   879   C CD1 . PHE A  1 119 ? -31.708 -23.788 77.930  1.00 14.30  ? 125 PHE A CD1 1 
ATOM   880   C CD2 . PHE A  1 119 ? -30.899 -25.884 78.761  1.00 17.61  ? 125 PHE A CD2 1 
ATOM   881   C CE1 . PHE A  1 119 ? -30.433 -23.468 77.482  1.00 14.77  ? 125 PHE A CE1 1 
ATOM   882   C CE2 . PHE A  1 119 ? -29.617 -25.572 78.310  1.00 16.89  ? 125 PHE A CE2 1 
ATOM   883   C CZ  . PHE A  1 119 ? -29.386 -24.362 77.670  1.00 16.15  ? 125 PHE A CZ  1 
ATOM   884   N N   . THR A  1 120 ? -34.840 -27.711 81.020  1.00 21.55  ? 126 THR A N   1 
ATOM   885   C CA  . THR A  1 120 ? -35.925 -27.826 81.991  1.00 22.11  ? 126 THR A CA  1 
ATOM   886   C C   . THR A  1 120 ? -35.524 -27.054 83.241  1.00 22.32  ? 126 THR A C   1 
ATOM   887   O O   . THR A  1 120 ? -34.332 -26.843 83.487  1.00 21.94  ? 126 THR A O   1 
ATOM   888   C CB  . THR A  1 120 ? -36.229 -29.297 82.349  1.00 22.68  ? 126 THR A CB  1 
ATOM   889   O OG1 . THR A  1 120 ? -35.000 -30.001 82.579  1.00 22.96  ? 126 THR A OG1 1 
ATOM   890   C CG2 . THR A  1 120 ? -37.006 -29.980 81.222  1.00 22.14  ? 126 THR A CG2 1 
ATOM   891   N N   . TYR A  1 121 ? -36.509 -26.627 84.027  1.00 22.89  ? 127 TYR A N   1 
ATOM   892   C CA  . TYR A  1 121 ? -36.234 -25.745 85.161  1.00 23.69  ? 127 TYR A CA  1 
ATOM   893   C C   . TYR A  1 121 ? -36.934 -26.157 86.449  1.00 24.85  ? 127 TYR A C   1 
ATOM   894   O O   . TYR A  1 121 ? -38.055 -26.671 86.432  1.00 25.03  ? 127 TYR A O   1 
ATOM   895   C CB  . TYR A  1 121 ? -36.596 -24.297 84.814  1.00 23.02  ? 127 TYR A CB  1 
ATOM   896   C CG  . TYR A  1 121 ? -35.849 -23.738 83.622  1.00 22.12  ? 127 TYR A CG  1 
ATOM   897   C CD1 . TYR A  1 121 ? -36.396 -23.807 82.337  1.00 19.22  ? 127 TYR A CD1 1 
ATOM   898   C CD2 . TYR A  1 121 ? -34.597 -23.137 83.776  1.00 20.84  ? 127 TYR A CD2 1 
ATOM   899   C CE1 . TYR A  1 121 ? -35.717 -23.294 81.236  1.00 19.26  ? 127 TYR A CE1 1 
ATOM   900   C CE2 . TYR A  1 121 ? -33.905 -22.619 82.678  1.00 20.14  ? 127 TYR A CE2 1 
ATOM   901   C CZ  . TYR A  1 121 ? -34.474 -22.701 81.414  1.00 19.66  ? 127 TYR A CZ  1 
ATOM   902   O OH  . TYR A  1 121 ? -33.801 -22.200 80.328  1.00 16.48  ? 127 TYR A OH  1 
ATOM   903   N N   . SER A  1 122 ? -36.258 -25.906 87.565  1.00 26.21  ? 128 SER A N   1 
ATOM   904   C CA  . SER A  1 122 ? -36.769 -26.240 88.885  1.00 27.28  ? 128 SER A CA  1 
ATOM   905   C C   . SER A  1 122 ? -36.604 -25.061 89.849  1.00 27.37  ? 128 SER A C   1 
ATOM   906   O O   . SER A  1 122 ? -35.562 -24.396 89.858  1.00 27.40  ? 128 SER A O   1 
ATOM   907   C CB  . SER A  1 122 ? -36.046 -27.477 89.422  1.00 27.39  ? 128 SER A CB  1 
ATOM   908   O OG  . SER A  1 122 ? -36.664 -27.963 90.598  1.00 29.57  ? 128 SER A OG  1 
ATOM   909   N N   . GLY A  1 123 ? -37.640 -24.800 90.645  1.00 27.14  ? 129 GLY A N   1 
ATOM   910   C CA  . GLY A  1 123 ? -37.568 -23.798 91.715  1.00 26.79  ? 129 GLY A CA  1 
ATOM   911   C C   . GLY A  1 123 ? -37.727 -22.348 91.288  1.00 26.29  ? 129 GLY A C   1 
ATOM   912   O O   . GLY A  1 123 ? -37.604 -21.434 92.111  1.00 25.92  ? 129 GLY A O   1 
ATOM   913   N N   . ILE A  1 124 ? -37.989 -22.139 90.000  1.00 25.77  ? 130 ILE A N   1 
ATOM   914   C CA  . ILE A  1 124 ? -38.273 -20.812 89.454  1.00 25.07  ? 130 ILE A CA  1 
ATOM   915   C C   . ILE A  1 124 ? -39.512 -20.871 88.567  1.00 24.84  ? 130 ILE A C   1 
ATOM   916   O O   . ILE A  1 124 ? -39.939 -21.956 88.172  1.00 24.87  ? 130 ILE A O   1 
ATOM   917   C CB  . ILE A  1 124 ? -37.062 -20.219 88.668  1.00 24.89  ? 130 ILE A CB  1 
ATOM   918   C CG1 . ILE A  1 124 ? -36.506 -21.210 87.636  1.00 23.79  ? 130 ILE A CG1 1 
ATOM   919   C CG2 . ILE A  1 124 ? -35.962 -19.801 89.617  1.00 25.57  ? 130 ILE A CG2 1 
ATOM   920   C CD1 . ILE A  1 124 ? -36.943 -20.933 86.215  1.00 23.67  ? 130 ILE A CD1 1 
ATOM   921   N N   . ARG A  1 125 ? -40.092 -19.710 88.272  1.00 24.75  ? 131 ARG A N   1 
ATOM   922   C CA  . ARG A  1 125 ? -41.194 -19.622 87.315  1.00 24.65  ? 131 ARG A CA  1 
ATOM   923   C C   . ARG A  1 125 ? -40.679 -19.482 85.883  1.00 24.54  ? 131 ARG A C   1 
ATOM   924   O O   . ARG A  1 125 ? -39.612 -18.911 85.641  1.00 24.52  ? 131 ARG A O   1 
ATOM   925   C CB  . ARG A  1 125 ? -42.141 -18.476 87.669  1.00 24.70  ? 131 ARG A CB  1 
ATOM   926   C CG  . ARG A  1 125 ? -43.309 -18.891 88.540  1.00 26.88  ? 131 ARG A CG  1 
ATOM   927   C CD  . ARG A  1 125 ? -43.718 -17.774 89.478  1.00 29.48  ? 131 ARG A CD  1 
ATOM   928   N NE  . ARG A  1 125 ? -44.392 -16.669 88.801  1.00 36.18  ? 131 ARG A NE  1 
ATOM   929   C CZ  . ARG A  1 125 ? -44.360 -15.402 89.213  1.00 40.01  ? 131 ARG A CZ  1 
ATOM   930   N NH1 . ARG A  1 125 ? -43.669 -15.054 90.297  1.00 39.45  ? 131 ARG A NH1 1 
ATOM   931   N NH2 . ARG A  1 125 ? -45.013 -14.472 88.528  1.00 42.05  ? 131 ARG A NH2 1 
ATOM   932   N N   . THR A  1 126 ? -41.460 -20.000 84.942  1.00 24.29  ? 132 THR A N   1 
ATOM   933   C CA  . THR A  1 126 ? -41.051 -20.121 83.549  1.00 24.20  ? 132 THR A CA  1 
ATOM   934   C C   . THR A  1 126 ? -42.001 -19.365 82.612  1.00 24.54  ? 132 THR A C   1 
ATOM   935   O O   . THR A  1 126 ? -41.662 -19.082 81.459  1.00 24.03  ? 132 THR A O   1 
ATOM   936   C CB  . THR A  1 126 ? -40.914 -21.631 83.176  1.00 24.16  ? 132 THR A CB  1 
ATOM   937   O OG1 . THR A  1 126 ? -39.528 -21.990 83.134  1.00 24.62  ? 132 THR A OG1 1 
ATOM   938   C CG2 . THR A  1 126 ? -41.568 -21.976 81.838  1.00 25.33  ? 132 THR A CG2 1 
ATOM   939   N N   . ASN A  1 127 ? -43.176 -19.013 83.132  1.00 24.96  ? 133 ASN A N   1 
ATOM   940   C CA  . ASN A  1 127 ? -44.254 -18.443 82.323  1.00 25.15  ? 133 ASN A CA  1 
ATOM   941   C C   . ASN A  1 127 ? -44.309 -16.910 82.302  1.00 24.67  ? 133 ASN A C   1 
ATOM   942   O O   . ASN A  1 127 ? -45.392 -16.318 82.353  1.00 24.91  ? 133 ASN A O   1 
ATOM   943   C CB  . ASN A  1 127 ? -45.605 -19.033 82.758  1.00 25.60  ? 133 ASN A CB  1 
ATOM   944   C CG  . ASN A  1 127 ? -45.912 -18.792 84.235  1.00 26.95  ? 133 ASN A CG  1 
ATOM   945   O OD1 . ASN A  1 127 ? -45.133 -18.169 84.958  1.00 29.09  ? 133 ASN A OD1 1 
ATOM   946   N ND2 . ASN A  1 127 ? -47.059 -19.289 84.685  1.00 27.52  ? 133 ASN A ND2 1 
ATOM   947   N N   . GLY A  1 128 ? -43.145 -16.272 82.219  1.00 23.76  ? 134 GLY A N   1 
ATOM   948   C CA  . GLY A  1 128 ? -43.076 -14.815 82.124  1.00 23.45  ? 134 GLY A CA  1 
ATOM   949   C C   . GLY A  1 128 ? -43.677 -14.314 80.824  1.00 23.15  ? 134 GLY A C   1 
ATOM   950   O O   . GLY A  1 128 ? -43.249 -14.710 79.738  1.00 23.14  ? 134 GLY A O   1 
ATOM   951   N N   . ALA A  1 129 ? -44.683 -13.451 80.938  1.00 22.70  ? 135 ALA A N   1 
ATOM   952   C CA  . ALA A  1 129 ? -45.399 -12.941 79.772  1.00 22.22  ? 135 ALA A CA  1 
ATOM   953   C C   . ALA A  1 129 ? -45.488 -11.420 79.777  1.00 22.58  ? 135 ALA A C   1 
ATOM   954   O O   . ALA A  1 129 ? -45.168 -10.768 80.771  1.00 22.58  ? 135 ALA A O   1 
ATOM   955   C CB  . ALA A  1 129 ? -46.787 -13.554 79.700  1.00 21.97  ? 135 ALA A CB  1 
ATOM   956   N N   . THR A  1 130 ? -45.923 -10.864 78.651  1.00 23.20  ? 136 THR A N   1 
ATOM   957   C CA  . THR A  1 130 ? -46.114 -9.425  78.507  1.00 23.83  ? 136 THR A CA  1 
ATOM   958   C C   . THR A  1 130 ? -47.209 -9.134  77.487  1.00 24.54  ? 136 THR A C   1 
ATOM   959   O O   . THR A  1 130 ? -47.316 -9.818  76.469  1.00 24.85  ? 136 THR A O   1 
ATOM   960   C CB  . THR A  1 130 ? -44.801 -8.691  78.111  1.00 23.67  ? 136 THR A CB  1 
ATOM   961   O OG1 . THR A  1 130 ? -45.106 -7.366  77.661  1.00 22.95  ? 136 THR A OG1 1 
ATOM   962   C CG2 . THR A  1 130 ? -44.058 -9.435  77.001  1.00 23.33  ? 136 THR A CG2 1 
ATOM   963   N N   . SER A  1 131 ? -48.015 -8.114  77.769  1.00 25.31  ? 137 SER A N   1 
ATOM   964   C CA  . SER A  1 131 ? -49.095 -7.695  76.875  1.00 25.78  ? 137 SER A CA  1 
ATOM   965   C C   . SER A  1 131 ? -48.576 -6.973  75.626  1.00 26.15  ? 137 SER A C   1 
ATOM   966   O O   . SER A  1 131 ? -49.354 -6.628  74.731  1.00 26.35  ? 137 SER A O   1 
ATOM   967   C CB  . SER A  1 131 ? -50.086 -6.808  77.625  1.00 25.47  ? 137 SER A CB  1 
ATOM   968   O OG  . SER A  1 131 ? -49.441 -5.641  78.101  1.00 26.30  ? 137 SER A OG  1 
ATOM   969   N N   . ALA A  1 132 ? -47.266 -6.740  75.573  1.00 26.10  ? 138 ALA A N   1 
ATOM   970   C CA  . ALA A  1 132 ? -46.635 -6.156  74.396  1.00 26.86  ? 138 ALA A CA  1 
ATOM   971   C C   . ALA A  1 132 ? -46.502 -7.209  73.295  1.00 27.59  ? 138 ALA A C   1 
ATOM   972   O O   . ALA A  1 132 ? -46.379 -6.874  72.112  1.00 27.60  ? 138 ALA A O   1 
ATOM   973   C CB  . ALA A  1 132 ? -45.277 -5.573  74.755  1.00 26.63  ? 138 ALA A CB  1 
ATOM   974   N N   . CYS A  1 133 ? -46.531 -8.477  73.704  1.00 28.05  ? 139 CYS A N   1 
ATOM   975   C CA  . CYS A  1 133 ? -46.481 -9.610  72.791  1.00 29.05  ? 139 CYS A CA  1 
ATOM   976   C C   . CYS A  1 133 ? -47.784 -10.397 72.868  1.00 30.12  ? 139 CYS A C   1 
ATOM   977   O O   . CYS A  1 133 ? -47.788 -11.573 73.233  1.00 30.15  ? 139 CYS A O   1 
ATOM   978   C CB  . CYS A  1 133 ? -45.301 -10.522 73.129  1.00 28.52  ? 139 CYS A CB  1 
ATOM   979   S SG  . CYS A  1 133 ? -43.721 -9.678  73.296  1.00 30.06  ? 139 CYS A SG  1 
ATOM   980   N N   . THR A  1 134 ? -48.890 -9.741  72.527  1.00 31.68  ? 140 THR A N   1 
ATOM   981   C CA  . THR A  1 134 ? -50.202 -10.382 72.567  1.00 32.96  ? 140 THR A CA  1 
ATOM   982   C C   . THR A  1 134 ? -50.356 -11.394 71.445  1.00 34.21  ? 140 THR A C   1 
ATOM   983   O O   . THR A  1 134 ? -50.041 -11.115 70.285  1.00 34.49  ? 140 THR A O   1 
ATOM   984   C CB  . THR A  1 134 ? -51.355 -9.370  72.493  1.00 33.02  ? 140 THR A CB  1 
ATOM   985   O OG1 . THR A  1 134 ? -51.057 -8.381  71.498  1.00 33.91  ? 140 THR A OG1 1 
ATOM   986   C CG2 . THR A  1 134 ? -51.564 -8.691  73.841  1.00 32.37  ? 140 THR A CG2 1 
ATOM   987   N N   . ARG A  1 135 ? -50.846 -12.564 71.821  1.00 35.84  ? 141 ARG A N   1 
ATOM   988   C CA  . ARG A  1 135 ? -51.027 -13.678 70.916  1.00 37.39  ? 141 ARG A CA  1 
ATOM   989   C C   . ARG A  1 135 ? -51.908 -14.665 71.669  1.00 38.67  ? 141 ARG A C   1 
ATOM   990   O O   . ARG A  1 135 ? -51.419 -15.618 72.273  1.00 39.11  ? 141 ARG A O   1 
ATOM   991   C CB  . ARG A  1 135 ? -49.667 -14.284 70.550  1.00 37.23  ? 141 ARG A CB  1 
ATOM   992   C CG  . ARG A  1 135 ? -49.738 -15.616 69.794  1.00 37.07  ? 141 ARG A CG  1 
ATOM   993   C CD  . ARG A  1 135 ? -48.594 -16.541 70.193  1.00 33.69  ? 141 ARG A CD  1 
ATOM   994   N NE  . ARG A  1 135 ? -47.368 -16.270 69.439  1.00 32.34  ? 141 ARG A NE  1 
ATOM   995   C CZ  . ARG A  1 135 ? -46.292 -15.651 69.929  1.00 30.04  ? 141 ARG A CZ  1 
ATOM   996   N NH1 . ARG A  1 135 ? -46.270 -15.209 71.178  1.00 28.79  ? 141 ARG A NH1 1 
ATOM   997   N NH2 . ARG A  1 135 ? -45.237 -15.468 69.157  1.00 27.72  ? 141 ARG A NH2 1 
ATOM   998   N N   . SER A  1 136 ? -53.216 -14.407 71.646  1.00 39.70  ? 142 SER A N   1 
ATOM   999   C CA  . SER A  1 136 ? -54.162 -15.131 72.489  1.00 40.54  ? 142 SER A CA  1 
ATOM   1000  C C   . SER A  1 136 ? -53.854 -14.799 73.948  1.00 40.53  ? 142 SER A C   1 
ATOM   1001  O O   . SER A  1 136 ? -53.415 -15.657 74.726  1.00 40.51  ? 142 SER A O   1 
ATOM   1002  C CB  . SER A  1 136 ? -54.103 -16.648 72.234  1.00 40.93  ? 142 SER A CB  1 
ATOM   1003  O OG  . SER A  1 136 ? -55.332 -17.277 72.640  1.00 42.27  ? 142 SER A OG  1 
ATOM   1004  N N   . GLY A  1 137 ? -54.088 -13.535 74.302  1.00 39.94  ? 144 GLY A N   1 
ATOM   1005  C CA  . GLY A  1 137 ? -53.756 -13.017 75.626  1.00 38.42  ? 144 GLY A CA  1 
ATOM   1006  C C   . GLY A  1 137 ? -52.333 -12.500 75.680  1.00 37.26  ? 144 GLY A C   1 
ATOM   1007  O O   . GLY A  1 137 ? -51.700 -12.276 74.653  1.00 37.43  ? 144 GLY A O   1 
ATOM   1008  N N   . SER A  1 138 ? -51.837 -12.305 76.894  1.00 36.00  ? 145 SER A N   1 
ATOM   1009  C CA  . SER A  1 138 ? -50.456 -11.903 77.118  1.00 34.28  ? 145 SER A CA  1 
ATOM   1010  C C   . SER A  1 138 ? -49.548 -13.088 76.889  1.00 32.31  ? 145 SER A C   1 
ATOM   1011  O O   . SER A  1 138 ? -49.602 -14.084 77.603  1.00 32.10  ? 145 SER A O   1 
ATOM   1012  C CB  . SER A  1 138 ? -50.270 -11.370 78.537  1.00 34.68  ? 145 SER A CB  1 
ATOM   1013  O OG  . SER A  1 138 ? -50.922 -10.128 78.695  1.00 36.81  ? 145 SER A OG  1 
ATOM   1014  N N   . SER A  1 139 ? -48.721 -12.973 75.866  1.00 29.87  ? 146 SER A N   1 
ATOM   1015  C CA  . SER A  1 139 ? -47.762 -14.019 75.543  1.00 27.59  ? 146 SER A CA  1 
ATOM   1016  C C   . SER A  1 139 ? -46.337 -13.467 75.596  1.00 25.25  ? 146 SER A C   1 
ATOM   1017  O O   . SER A  1 139 ? -46.071 -12.486 76.295  1.00 25.06  ? 146 SER A O   1 
ATOM   1018  C CB  . SER A  1 139 ? -48.083 -14.644 74.179  1.00 27.74  ? 146 SER A CB  1 
ATOM   1019  O OG  . SER A  1 139 ? -47.474 -15.917 74.046  1.00 27.95  ? 146 SER A OG  1 
ATOM   1020  N N   . PHE A  1 140 ? -45.433 -14.104 74.857  1.00 22.65  ? 147 PHE A N   1 
ATOM   1021  C CA  . PHE A  1 140 ? -44.018 -13.765 74.865  1.00 19.74  ? 147 PHE A CA  1 
ATOM   1022  C C   . PHE A  1 140 ? -43.381 -14.284 73.580  1.00 19.05  ? 147 PHE A C   1 
ATOM   1023  O O   . PHE A  1 140 ? -44.064 -14.873 72.744  1.00 19.20  ? 147 PHE A O   1 
ATOM   1024  C CB  . PHE A  1 140 ? -43.354 -14.397 76.092  1.00 18.45  ? 147 PHE A CB  1 
ATOM   1025  C CG  . PHE A  1 140 ? -41.968 -13.903 76.360  1.00 17.25  ? 147 PHE A CG  1 
ATOM   1026  C CD1 . PHE A  1 140 ? -41.714 -12.543 76.509  1.00 16.71  ? 147 PHE A CD1 1 
ATOM   1027  C CD2 . PHE A  1 140 ? -40.914 -14.800 76.484  1.00 16.70  ? 147 PHE A CD2 1 
ATOM   1028  C CE1 . PHE A  1 140 ? -40.429 -12.081 76.764  1.00 17.05  ? 147 PHE A CE1 1 
ATOM   1029  C CE2 . PHE A  1 140 ? -39.624 -14.350 76.742  1.00 18.17  ? 147 PHE A CE2 1 
ATOM   1030  C CZ  . PHE A  1 140 ? -39.381 -12.985 76.885  1.00 17.85  ? 147 PHE A CZ  1 
ATOM   1031  N N   . TYR A  1 141 ? -42.080 -14.061 73.422  1.00 18.59  ? 148 TYR A N   1 
ATOM   1032  C CA  . TYR A  1 141 ? -41.319 -14.616 72.306  1.00 17.55  ? 148 TYR A CA  1 
ATOM   1033  C C   . TYR A  1 141 ? -41.411 -16.140 72.287  1.00 17.47  ? 148 TYR A C   1 
ATOM   1034  O O   . TYR A  1 141 ? -41.090 -16.802 73.278  1.00 17.83  ? 148 TYR A O   1 
ATOM   1035  C CB  . TYR A  1 141 ? -39.864 -14.156 72.381  1.00 17.44  ? 148 TYR A CB  1 
ATOM   1036  C CG  . TYR A  1 141 ? -39.706 -12.661 72.226  1.00 17.22  ? 148 TYR A CG  1 
ATOM   1037  C CD1 . TYR A  1 141 ? -39.393 -11.855 73.317  1.00 15.23  ? 148 TYR A CD1 1 
ATOM   1038  C CD2 . TYR A  1 141 ? -39.889 -12.050 70.985  1.00 18.99  ? 148 TYR A CD2 1 
ATOM   1039  C CE1 . TYR A  1 141 ? -39.257 -10.473 73.173  1.00 16.44  ? 148 TYR A CE1 1 
ATOM   1040  C CE2 . TYR A  1 141 ? -39.754 -10.673 70.832  1.00 18.46  ? 148 TYR A CE2 1 
ATOM   1041  C CZ  . TYR A  1 141 ? -39.437 -9.894  71.926  1.00 16.73  ? 148 TYR A CZ  1 
ATOM   1042  O OH  . TYR A  1 141 ? -39.305 -8.538  71.763  1.00 18.82  ? 148 TYR A OH  1 
ATOM   1043  N N   . ALA A  1 142 ? -41.856 -16.681 71.153  1.00 16.77  ? 149 ALA A N   1 
ATOM   1044  C CA  . ALA A  1 142 ? -42.222 -18.096 71.031  1.00 16.14  ? 149 ALA A CA  1 
ATOM   1045  C C   . ALA A  1 142 ? -41.065 -19.072 71.228  1.00 16.22  ? 149 ALA A C   1 
ATOM   1046  O O   . ALA A  1 142 ? -41.278 -20.227 71.602  1.00 16.44  ? 149 ALA A O   1 
ATOM   1047  C CB  . ALA A  1 142 ? -42.900 -18.350 69.695  1.00 16.37  ? 149 ALA A CB  1 
ATOM   1048  N N   . GLU A  1 143 ? -39.846 -18.604 70.982  1.00 16.01  ? 150 GLU A N   1 
ATOM   1049  C CA  . GLU A  1 143 ? -38.662 -19.452 71.070  1.00 15.57  ? 150 GLU A CA  1 
ATOM   1050  C C   . GLU A  1 143 ? -37.906 -19.209 72.366  1.00 14.89  ? 150 GLU A C   1 
ATOM   1051  O O   . GLU A  1 143 ? -36.865 -19.819 72.619  1.00 14.65  ? 150 GLU A O   1 
ATOM   1052  C CB  . GLU A  1 143 ? -37.750 -19.199 69.869  1.00 16.03  ? 150 GLU A CB  1 
ATOM   1053  C CG  . GLU A  1 143 ? -38.484 -19.141 68.531  1.00 16.35  ? 150 GLU A CG  1 
ATOM   1054  C CD  . GLU A  1 143 ? -39.028 -20.483 68.094  1.00 17.11  ? 150 GLU A CD  1 
ATOM   1055  O OE1 . GLU A  1 143 ? -39.310 -21.330 68.967  1.00 13.76  ? 150 GLU A OE1 1 
ATOM   1056  O OE2 . GLU A  1 143 ? -39.182 -20.691 66.871  1.00 20.76  ? 150 GLU A OE2 1 
ATOM   1057  N N   . MET A  1 144 ? -38.446 -18.314 73.185  1.00 14.12  ? 151 MET A N   1 
ATOM   1058  C CA  . MET A  1 144 ? -37.772 -17.877 74.393  1.00 14.25  ? 151 MET A CA  1 
ATOM   1059  C C   . MET A  1 144 ? -38.601 -18.188 75.634  1.00 14.48  ? 151 MET A C   1 
ATOM   1060  O O   . MET A  1 144 ? -39.774 -18.551 75.537  1.00 15.25  ? 151 MET A O   1 
ATOM   1061  C CB  . MET A  1 144 ? -37.450 -16.378 74.309  1.00 14.48  ? 151 MET A CB  1 
ATOM   1062  C CG  . MET A  1 144 ? -36.652 -15.976 73.073  1.00 12.93  ? 151 MET A CG  1 
ATOM   1063  S SD  . MET A  1 144 ? -35.004 -16.708 73.019  1.00 20.41  ? 151 MET A SD  1 
ATOM   1064  C CE  . MET A  1 144 ? -34.941 -17.243 71.320  1.00 23.16  ? 151 MET A CE  1 
ATOM   1065  N N   . LYS A  1 145 ? -37.969 -18.067 76.796  1.00 14.46  ? 152 LYS A N   1 
ATOM   1066  C CA  . LYS A  1 145 ? -38.630 -18.267 78.075  1.00 15.39  ? 152 LYS A CA  1 
ATOM   1067  C C   . LYS A  1 145 ? -38.198 -17.172 79.047  1.00 14.99  ? 152 LYS A C   1 
ATOM   1068  O O   . LYS A  1 145 ? -37.003 -16.996 79.303  1.00 15.07  ? 152 LYS A O   1 
ATOM   1069  C CB  . LYS A  1 145 ? -38.312 -19.659 78.644  1.00 16.37  ? 152 LYS A CB  1 
ATOM   1070  C CG  . LYS A  1 145 ? -39.082 -20.815 77.998  1.00 18.37  ? 152 LYS A CG  1 
ATOM   1071  C CD  . LYS A  1 145 ? -40.507 -20.913 78.539  1.00 25.33  ? 152 LYS A CD  1 
ATOM   1072  C CE  . LYS A  1 145 ? -41.436 -21.695 77.606  1.00 29.86  ? 152 LYS A CE  1 
ATOM   1073  N NZ  . LYS A  1 145 ? -41.106 -23.150 77.512  1.00 28.75  ? 152 LYS A NZ  1 
ATOM   1074  N N   . TRP A  1 146 ? -39.176 -16.429 79.562  1.00 14.39  ? 153 TRP A N   1 
ATOM   1075  C CA  . TRP A  1 146 ? -38.936 -15.391 80.559  1.00 13.96  ? 153 TRP A CA  1 
ATOM   1076  C C   . TRP A  1 146 ? -38.898 -16.049 81.934  1.00 14.93  ? 153 TRP A C   1 
ATOM   1077  O O   . TRP A  1 146 ? -39.928 -16.492 82.450  1.00 15.14  ? 153 TRP A O   1 
ATOM   1078  C CB  . TRP A  1 146 ? -40.045 -14.343 80.503  1.00 12.80  ? 153 TRP A CB  1 
ATOM   1079  C CG  . TRP A  1 146 ? -39.763 -13.054 81.227  1.00 12.81  ? 153 TRP A CG  1 
ATOM   1080  C CD1 . TRP A  1 146 ? -38.919 -12.863 82.289  1.00 14.06  ? 153 TRP A CD1 1 
ATOM   1081  C CD2 . TRP A  1 146 ? -40.365 -11.777 80.964  1.00 11.67  ? 153 TRP A CD2 1 
ATOM   1082  N NE1 . TRP A  1 146 ? -38.943 -11.545 82.684  1.00 12.94  ? 153 TRP A NE1 1 
ATOM   1083  C CE2 . TRP A  1 146 ? -39.825 -10.859 81.891  1.00 12.29  ? 153 TRP A CE2 1 
ATOM   1084  C CE3 . TRP A  1 146 ? -41.302 -11.320 80.028  1.00 9.75   ? 153 TRP A CE3 1 
ATOM   1085  C CZ2 . TRP A  1 146 ? -40.190 -9.509  81.909  1.00 13.32  ? 153 TRP A CZ2 1 
ATOM   1086  C CZ3 . TRP A  1 146 ? -41.664 -9.976  80.046  1.00 11.12  ? 153 TRP A CZ3 1 
ATOM   1087  C CH2 . TRP A  1 146 ? -41.109 -9.088  80.982  1.00 10.56  ? 153 TRP A CH2 1 
ATOM   1088  N N   . LEU A  1 147 ? -37.702 -16.117 82.516  1.00 15.49  ? 154 LEU A N   1 
ATOM   1089  C CA  . LEU A  1 147 ? -37.506 -16.736 83.826  1.00 15.80  ? 154 LEU A CA  1 
ATOM   1090  C C   . LEU A  1 147 ? -37.560 -15.693 84.935  1.00 16.19  ? 154 LEU A C   1 
ATOM   1091  O O   . LEU A  1 147 ? -36.980 -14.611 84.807  1.00 16.40  ? 154 LEU A O   1 
ATOM   1092  C CB  . LEU A  1 147 ? -36.165 -17.476 83.884  1.00 15.21  ? 154 LEU A CB  1 
ATOM   1093  C CG  . LEU A  1 147 ? -35.779 -18.419 82.741  1.00 15.35  ? 154 LEU A CG  1 
ATOM   1094  C CD1 . LEU A  1 147 ? -34.351 -18.899 82.933  1.00 14.76  ? 154 LEU A CD1 1 
ATOM   1095  C CD2 . LEU A  1 147 ? -36.736 -19.601 82.620  1.00 15.06  ? 154 LEU A CD2 1 
ATOM   1096  N N   . LEU A  1 148 ? -38.262 -16.027 86.014  1.00 16.13  ? 155 LEU A N   1 
ATOM   1097  C CA  . LEU A  1 148 ? -38.326 -15.179 87.209  1.00 16.42  ? 155 LEU A CA  1 
ATOM   1098  C C   . LEU A  1 148 ? -38.598 -15.975 88.484  1.00 17.37  ? 155 LEU A C   1 
ATOM   1099  O O   . LEU A  1 148 ? -38.956 -17.156 88.429  1.00 17.31  ? 155 LEU A O   1 
ATOM   1100  C CB  . LEU A  1 148 ? -39.351 -14.038 87.063  1.00 15.39  ? 155 LEU A CB  1 
ATOM   1101  C CG  . LEU A  1 148 ? -40.738 -14.104 86.399  1.00 15.26  ? 155 LEU A CG  1 
ATOM   1102  C CD1 . LEU A  1 148 ? -41.325 -15.499 86.216  1.00 14.26  ? 155 LEU A CD1 1 
ATOM   1103  C CD2 . LEU A  1 148 ? -41.710 -13.215 87.173  1.00 13.67  ? 155 LEU A CD2 1 
ATOM   1104  N N   . SER A  1 149 ? -38.426 -15.312 89.625  1.00 18.52  ? 156 SER A N   1 
ATOM   1105  C CA  . SER A  1 149 ? -38.653 -15.908 90.942  1.00 19.64  ? 156 SER A CA  1 
ATOM   1106  C C   . SER A  1 149 ? -40.053 -16.500 91.110  1.00 20.55  ? 156 SER A C   1 
ATOM   1107  O O   . SER A  1 149 ? -40.977 -16.170 90.357  1.00 20.22  ? 156 SER A O   1 
ATOM   1108  C CB  . SER A  1 149 ? -38.401 -14.870 92.035  1.00 19.45  ? 156 SER A CB  1 
ATOM   1109  O OG  . SER A  1 149 ? -37.068 -14.400 91.986  1.00 19.59  ? 156 SER A OG  1 
ATOM   1110  N N   . ASN A  1 150 ? -40.194 -17.368 92.111  1.00 21.61  ? 157 ASN A N   1 
ATOM   1111  C CA  . ASN A  1 150 ? -41.458 -18.046 92.397  1.00 22.67  ? 157 ASN A CA  1 
ATOM   1112  C C   . ASN A  1 150 ? -42.587 -17.116 92.836  1.00 23.05  ? 157 ASN A C   1 
ATOM   1113  O O   . ASN A  1 150 ? -43.763 -17.431 92.638  1.00 23.42  ? 157 ASN A O   1 
ATOM   1114  C CB  . ASN A  1 150 ? -41.253 -19.164 93.422  1.00 22.91  ? 157 ASN A CB  1 
ATOM   1115  C CG  . ASN A  1 150 ? -41.005 -20.517 92.771  1.00 24.69  ? 157 ASN A CG  1 
ATOM   1116  O OD1 . ASN A  1 150 ? -40.701 -20.609 91.581  1.00 25.72  ? 157 ASN A OD1 1 
ATOM   1117  N ND2 . ASN A  1 150 ? -41.145 -21.579 93.555  1.00 27.08  ? 157 ASN A ND2 1 
ATOM   1118  N N   . SER A  1 151 ? -42.221 -15.981 93.430  1.00 23.29  ? 158 SER A N   1 
ATOM   1119  C CA  . SER A  1 151 ? -43.177 -14.943 93.829  1.00 23.86  ? 158 SER A CA  1 
ATOM   1120  C C   . SER A  1 151 ? -42.479 -13.586 93.905  1.00 23.57  ? 158 SER A C   1 
ATOM   1121  O O   . SER A  1 151 ? -41.260 -13.504 93.745  1.00 24.08  ? 158 SER A O   1 
ATOM   1122  C CB  . SER A  1 151 ? -43.836 -15.289 95.174  1.00 23.93  ? 158 SER A CB  1 
ATOM   1123  O OG  . SER A  1 151 ? -42.879 -15.356 96.219  1.00 25.80  ? 158 SER A OG  1 
ATOM   1124  N N   . ASP A  1 152 A -43.253 -12.529 94.147  1.00 23.33  ? 158 ASP A N   1 
ATOM   1125  C CA  . ASP A  1 152 A -42.709 -11.178 94.284  1.00 23.43  ? 158 ASP A CA  1 
ATOM   1126  C C   . ASP A  1 152 A -41.582 -11.112 95.322  1.00 23.49  ? 158 ASP A C   1 
ATOM   1127  O O   . ASP A  1 152 A -41.768 -11.523 96.473  1.00 23.93  ? 158 ASP A O   1 
ATOM   1128  C CB  . ASP A  1 152 A -43.819 -10.187 94.661  1.00 23.66  ? 158 ASP A CB  1 
ATOM   1129  C CG  . ASP A  1 152 A -44.751 -9.863  93.498  1.00 25.87  ? 158 ASP A CG  1 
ATOM   1130  O OD1 . ASP A  1 152 A -44.485 -10.289 92.352  1.00 25.10  ? 158 ASP A OD1 1 
ATOM   1131  O OD2 . ASP A  1 152 A -45.760 -9.165  93.736  1.00 29.64  ? 158 ASP A OD2 1 
ATOM   1132  N N   . ASN A  1 153 B -40.420 -10.612 94.891  1.00 22.64  ? 158 ASN A N   1 
ATOM   1133  C CA  . ASN A  1 153 B -39.259 -10.321 95.760  1.00 21.67  ? 158 ASN A CA  1 
ATOM   1134  C C   . ASN A  1 153 B -38.370 -11.507 96.159  1.00 21.63  ? 158 ASN A C   1 
ATOM   1135  O O   . ASN A  1 153 B -37.285 -11.308 96.718  1.00 21.88  ? 158 ASN A O   1 
ATOM   1136  C CB  . ASN A  1 153 B -39.675 -9.538  97.014  1.00 20.99  ? 158 ASN A CB  1 
ATOM   1137  C CG  . ASN A  1 153 B -40.419 -8.264  96.689  1.00 20.20  ? 158 ASN A CG  1 
ATOM   1138  O OD1 . ASN A  1 153 B -39.847 -7.317  96.153  1.00 20.98  ? 158 ASN A OD1 1 
ATOM   1139  N ND2 . ASN A  1 153 B -41.705 -8.228  97.023  1.00 15.94  ? 158 ASN A ND2 1 
ATOM   1140  N N   . ALA A  1 154 ? -38.817 -12.728 95.872  1.00 21.26  ? 159 ALA A N   1 
ATOM   1141  C CA  . ALA A  1 154 ? -38.077 -13.933 96.262  1.00 21.41  ? 159 ALA A CA  1 
ATOM   1142  C C   . ALA A  1 154 ? -36.725 -14.022 95.559  1.00 21.34  ? 159 ALA A C   1 
ATOM   1143  O O   . ALA A  1 154 ? -36.579 -13.571 94.422  1.00 21.29  ? 159 ALA A O   1 
ATOM   1144  C CB  . ALA A  1 154 ? -38.906 -15.187 95.998  1.00 21.26  ? 159 ALA A CB  1 
ATOM   1145  N N   . ALA A  1 155 ? -35.740 -14.592 96.252  1.00 21.12  ? 160 ALA A N   1 
ATOM   1146  C CA  . ALA A  1 155 ? -34.389 -14.727 95.709  1.00 20.65  ? 160 ALA A CA  1 
ATOM   1147  C C   . ALA A  1 155 ? -34.318 -15.764 94.589  1.00 20.47  ? 160 ALA A C   1 
ATOM   1148  O O   . ALA A  1 155 ? -34.580 -16.956 94.802  1.00 20.44  ? 160 ALA A O   1 
ATOM   1149  C CB  . ALA A  1 155 ? -33.397 -15.061 96.813  1.00 20.81  ? 160 ALA A CB  1 
ATOM   1150  N N   . PHE A  1 156 ? -33.977 -15.286 93.395  1.00 19.80  ? 161 PHE A N   1 
ATOM   1151  C CA  . PHE A  1 156 ? -33.760 -16.138 92.237  1.00 19.96  ? 161 PHE A CA  1 
ATOM   1152  C C   . PHE A  1 156 ? -32.423 -16.849 92.434  1.00 20.32  ? 161 PHE A C   1 
ATOM   1153  O O   . PHE A  1 156 ? -31.390 -16.191 92.581  1.00 20.93  ? 161 PHE A O   1 
ATOM   1154  C CB  . PHE A  1 156 ? -33.742 -15.287 90.963  1.00 19.90  ? 161 PHE A CB  1 
ATOM   1155  C CG  . PHE A  1 156 ? -33.824 -16.078 89.683  1.00 18.69  ? 161 PHE A CG  1 
ATOM   1156  C CD1 . PHE A  1 156 ? -35.037 -16.220 89.018  1.00 18.86  ? 161 PHE A CD1 1 
ATOM   1157  C CD2 . PHE A  1 156 ? -32.686 -16.653 89.125  1.00 17.50  ? 161 PHE A CD2 1 
ATOM   1158  C CE1 . PHE A  1 156 ? -35.116 -16.937 87.821  1.00 17.61  ? 161 PHE A CE1 1 
ATOM   1159  C CE2 . PHE A  1 156 ? -32.756 -17.375 87.932  1.00 16.15  ? 161 PHE A CE2 1 
ATOM   1160  C CZ  . PHE A  1 156 ? -33.974 -17.518 87.281  1.00 14.48  ? 161 PHE A CZ  1 
ATOM   1161  N N   . PRO A  1 157 ? -32.440 -18.193 92.457  1.00 20.35  ? 162 PRO A N   1 
ATOM   1162  C CA  . PRO A  1 157 ? -31.235 -18.982 92.721  1.00 20.70  ? 162 PRO A CA  1 
ATOM   1163  C C   . PRO A  1 157 ? -30.191 -18.894 91.609  1.00 21.30  ? 162 PRO A C   1 
ATOM   1164  O O   . PRO A  1 157 ? -30.550 -18.845 90.429  1.00 20.58  ? 162 PRO A O   1 
ATOM   1165  C CB  . PRO A  1 157 ? -31.770 -20.414 92.824  1.00 20.09  ? 162 PRO A CB  1 
ATOM   1166  C CG  . PRO A  1 157 ? -33.037 -20.402 92.052  1.00 19.84  ? 162 PRO A CG  1 
ATOM   1167  C CD  . PRO A  1 157 ? -33.626 -19.049 92.282  1.00 20.18  ? 162 PRO A CD  1 
ATOM   1168  N N   . GLN A  1 158 ? -28.915 -18.869 92.000  1.00 22.41  ? 163 GLN A N   1 
ATOM   1169  C CA  . GLN A  1 158 ? -27.797 -18.971 91.059  1.00 23.57  ? 163 GLN A CA  1 
ATOM   1170  C C   . GLN A  1 158 ? -27.922 -20.286 90.290  1.00 23.97  ? 163 GLN A C   1 
ATOM   1171  O O   . GLN A  1 158 ? -28.121 -21.347 90.889  1.00 24.10  ? 163 GLN A O   1 
ATOM   1172  C CB  . GLN A  1 158 ? -26.456 -18.893 91.799  1.00 23.95  ? 163 GLN A CB  1 
ATOM   1173  C CG  . GLN A  1 158 ? -25.211 -18.920 90.900  1.00 25.40  ? 163 GLN A CG  1 
ATOM   1174  C CD  . GLN A  1 158 ? -25.087 -17.694 90.004  1.00 27.25  ? 163 GLN A CD  1 
ATOM   1175  O OE1 . GLN A  1 158 ? -25.257 -16.557 90.451  1.00 26.96  ? 163 GLN A OE1 1 
ATOM   1176  N NE2 . GLN A  1 158 ? -24.780 -17.923 88.731  1.00 28.26  ? 163 GLN A NE2 1 
ATOM   1177  N N   . MET A  1 159 ? -27.806 -20.205 88.968  1.00 24.14  ? 164 MET A N   1 
ATOM   1178  C CA  . MET A  1 159 ? -28.219 -21.296 88.089  1.00 24.31  ? 164 MET A CA  1 
ATOM   1179  C C   . MET A  1 159 ? -27.231 -21.517 86.943  1.00 24.10  ? 164 MET A C   1 
ATOM   1180  O O   . MET A  1 159 ? -26.520 -20.594 86.543  1.00 23.95  ? 164 MET A O   1 
ATOM   1181  C CB  . MET A  1 159 ? -29.607 -20.971 87.536  1.00 24.25  ? 164 MET A CB  1 
ATOM   1182  C CG  . MET A  1 159 ? -30.428 -22.159 87.091  1.00 26.00  ? 164 MET A CG  1 
ATOM   1183  S SD  . MET A  1 159 ? -32.136 -21.682 86.755  1.00 30.42  ? 164 MET A SD  1 
ATOM   1184  C CE  . MET A  1 159 ? -32.800 -21.587 88.416  1.00 27.68  ? 164 MET A CE  1 
ATOM   1185  N N   . THR A  1 160 ? -27.193 -22.743 86.422  1.00 24.18  ? 165 THR A N   1 
ATOM   1186  C CA  . THR A  1 160 ? -26.328 -23.085 85.285  1.00 24.33  ? 165 THR A CA  1 
ATOM   1187  C C   . THR A  1 160 ? -27.049 -23.967 84.261  1.00 23.79  ? 165 THR A C   1 
ATOM   1188  O O   . THR A  1 160 ? -27.612 -25.008 84.609  1.00 23.60  ? 165 THR A O   1 
ATOM   1189  C CB  . THR A  1 160 ? -25.009 -23.774 85.740  1.00 24.30  ? 165 THR A CB  1 
ATOM   1190  O OG1 . THR A  1 160 ? -24.326 -22.939 86.683  1.00 24.62  ? 165 THR A OG1 1 
ATOM   1191  C CG2 . THR A  1 160 ? -24.088 -24.026 84.554  1.00 24.39  ? 165 THR A CG2 1 
ATOM   1192  N N   . LYS A  1 161 ? -27.031 -23.538 83.002  1.00 23.24  ? 166 LYS A N   1 
ATOM   1193  C CA  . LYS A  1 161 ? -27.604 -24.321 81.911  1.00 22.98  ? 166 LYS A CA  1 
ATOM   1194  C C   . LYS A  1 161 ? -26.599 -24.478 80.780  1.00 23.21  ? 166 LYS A C   1 
ATOM   1195  O O   . LYS A  1 161 ? -25.963 -23.507 80.357  1.00 23.20  ? 166 LYS A O   1 
ATOM   1196  C CB  . LYS A  1 161 ? -28.907 -23.694 81.398  1.00 22.73  ? 166 LYS A CB  1 
ATOM   1197  C CG  . LYS A  1 161 ? -30.051 -23.696 82.408  1.00 21.82  ? 166 LYS A CG  1 
ATOM   1198  C CD  . LYS A  1 161 ? -30.491 -25.111 82.752  1.00 21.07  ? 166 LYS A CD  1 
ATOM   1199  C CE  . LYS A  1 161 ? -31.215 -25.158 84.086  1.00 20.61  ? 166 LYS A CE  1 
ATOM   1200  N NZ  . LYS A  1 161 ? -31.569 -26.554 84.450  1.00 19.93  ? 166 LYS A NZ  1 
ATOM   1201  N N   . ALA A  1 162 ? -26.450 -25.710 80.305  1.00 23.06  ? 167 ALA A N   1 
ATOM   1202  C CA  . ALA A  1 162 ? -25.489 -26.009 79.254  1.00 23.23  ? 167 ALA A CA  1 
ATOM   1203  C C   . ALA A  1 162 ? -26.152 -26.737 78.099  1.00 23.27  ? 167 ALA A C   1 
ATOM   1204  O O   . ALA A  1 162 ? -27.010 -27.600 78.304  1.00 23.85  ? 167 ALA A O   1 
ATOM   1205  C CB  . ALA A  1 162 ? -24.325 -26.820 79.805  1.00 23.30  ? 167 ALA A CB  1 
ATOM   1206  N N   . TYR A  1 163 ? -25.752 -26.376 76.886  1.00 22.67  ? 168 TYR A N   1 
ATOM   1207  C CA  . TYR A  1 163 ? -26.271 -27.010 75.685  1.00 22.00  ? 168 TYR A CA  1 
ATOM   1208  C C   . TYR A  1 163 ? -25.137 -27.297 74.719  1.00 22.35  ? 168 TYR A C   1 
ATOM   1209  O O   . TYR A  1 163 ? -24.348 -26.410 74.393  1.00 23.14  ? 168 TYR A O   1 
ATOM   1210  C CB  . TYR A  1 163 ? -27.330 -26.123 75.019  1.00 21.74  ? 168 TYR A CB  1 
ATOM   1211  C CG  . TYR A  1 163 ? -27.749 -26.594 73.643  1.00 19.33  ? 168 TYR A CG  1 
ATOM   1212  C CD1 . TYR A  1 163 ? -28.723 -27.583 73.487  1.00 17.34  ? 168 TYR A CD1 1 
ATOM   1213  C CD2 . TYR A  1 163 ? -27.167 -26.055 72.497  1.00 18.16  ? 168 TYR A CD2 1 
ATOM   1214  C CE1 . TYR A  1 163 ? -29.104 -28.022 72.224  1.00 16.38  ? 168 TYR A CE1 1 
ATOM   1215  C CE2 . TYR A  1 163 ? -27.539 -26.487 71.230  1.00 17.98  ? 168 TYR A CE2 1 
ATOM   1216  C CZ  . TYR A  1 163 ? -28.506 -27.468 71.101  1.00 17.41  ? 168 TYR A CZ  1 
ATOM   1217  O OH  . TYR A  1 163 ? -28.872 -27.890 69.846  1.00 17.90  ? 168 TYR A OH  1 
ATOM   1218  N N   . ARG A  1 164 ? -25.067 -28.542 74.262  1.00 22.24  ? 169 ARG A N   1 
ATOM   1219  C CA  . ARG A  1 164 ? -24.067 -28.951 73.287  1.00 22.07  ? 169 ARG A CA  1 
ATOM   1220  C C   . ARG A  1 164 ? -24.726 -29.082 71.916  1.00 21.54  ? 169 ARG A C   1 
ATOM   1221  O O   . ARG A  1 164 ? -25.795 -29.679 71.793  1.00 21.13  ? 169 ARG A O   1 
ATOM   1222  C CB  . ARG A  1 164 ? -23.436 -30.282 73.715  1.00 22.54  ? 169 ARG A CB  1 
ATOM   1223  C CG  . ARG A  1 164 ? -22.237 -30.732 72.882  1.00 23.48  ? 169 ARG A CG  1 
ATOM   1224  C CD  . ARG A  1 164 ? -21.788 -32.146 73.258  1.00 24.80  ? 169 ARG A CD  1 
ATOM   1225  N NE  . ARG A  1 164 ? -22.807 -33.152 72.953  1.00 26.67  ? 169 ARG A NE  1 
ATOM   1226  C CZ  . ARG A  1 164 ? -22.915 -33.797 71.792  1.00 27.64  ? 169 ARG A CZ  1 
ATOM   1227  N NH1 . ARG A  1 164 ? -22.066 -33.555 70.799  1.00 25.90  ? 169 ARG A NH1 1 
ATOM   1228  N NH2 . ARG A  1 164 ? -23.881 -34.690 71.621  1.00 27.19  ? 169 ARG A NH2 1 
ATOM   1229  N N   . ASN A  1 165 ? -24.092 -28.508 70.896  1.00 21.40  ? 170 ASN A N   1 
ATOM   1230  C CA  . ASN A  1 165 ? -24.549 -28.657 69.516  1.00 21.32  ? 170 ASN A CA  1 
ATOM   1231  C C   . ASN A  1 165 ? -24.417 -30.117 69.085  1.00 21.49  ? 170 ASN A C   1 
ATOM   1232  O O   . ASN A  1 165 ? -23.300 -30.628 68.972  1.00 21.82  ? 170 ASN A O   1 
ATOM   1233  C CB  . ASN A  1 165 ? -23.751 -27.735 68.581  1.00 21.32  ? 170 ASN A CB  1 
ATOM   1234  C CG  . ASN A  1 165 ? -24.349 -27.642 67.175  1.00 20.63  ? 170 ASN A CG  1 
ATOM   1235  O OD1 . ASN A  1 165 ? -25.235 -28.411 66.799  1.00 20.28  ? 170 ASN A OD1 1 
ATOM   1236  N ND2 . ASN A  1 165 ? -23.854 -26.692 66.393  1.00 16.05  ? 170 ASN A ND2 1 
ATOM   1237  N N   . PRO A  1 166 ? -25.558 -30.801 68.865  1.00 21.66  ? 171 PRO A N   1 
ATOM   1238  C CA  . PRO A  1 166 ? -25.533 -32.218 68.509  1.00 21.08  ? 171 PRO A CA  1 
ATOM   1239  C C   . PRO A  1 166 ? -25.560 -32.449 67.000  1.00 21.04  ? 171 PRO A C   1 
ATOM   1240  O O   . PRO A  1 166 ? -25.636 -33.598 66.555  1.00 21.81  ? 171 PRO A O   1 
ATOM   1241  C CB  . PRO A  1 166 ? -26.825 -32.739 69.133  1.00 20.86  ? 171 PRO A CB  1 
ATOM   1242  C CG  . PRO A  1 166 ? -27.773 -31.571 69.046  1.00 22.10  ? 171 PRO A CG  1 
ATOM   1243  C CD  . PRO A  1 166 ? -26.941 -30.303 68.994  1.00 21.63  ? 171 PRO A CD  1 
ATOM   1244  N N   . ARG A  1 167 ? -25.491 -31.367 66.227  1.00 20.23  ? 172 ARG A N   1 
ATOM   1245  C CA  . ARG A  1 167 ? -25.612 -31.452 64.777  1.00 19.73  ? 172 ARG A CA  1 
ATOM   1246  C C   . ARG A  1 167 ? -24.291 -31.325 64.017  1.00 19.58  ? 172 ARG A C   1 
ATOM   1247  O O   . ARG A  1 167 ? -23.213 -31.226 64.606  1.00 19.87  ? 172 ARG A O   1 
ATOM   1248  C CB  . ARG A  1 167 ? -26.642 -30.444 64.252  1.00 19.78  ? 172 ARG A CB  1 
ATOM   1249  C CG  . ARG A  1 167 ? -28.087 -30.866 64.469  1.00 19.28  ? 172 ARG A CG  1 
ATOM   1250  C CD  . ARG A  1 167 ? -29.007 -30.245 63.435  1.00 20.50  ? 172 ARG A CD  1 
ATOM   1251  N NE  . ARG A  1 167 ? -30.383 -30.146 63.926  1.00 25.40  ? 172 ARG A NE  1 
ATOM   1252  C CZ  . ARG A  1 167 ? -31.403 -29.635 63.236  1.00 25.79  ? 172 ARG A CZ  1 
ATOM   1253  N NH1 . ARG A  1 167 ? -31.217 -29.167 62.004  1.00 25.05  ? 172 ARG A NH1 1 
ATOM   1254  N NH2 . ARG A  1 167 ? -32.616 -29.589 63.781  1.00 22.30  ? 172 ARG A NH2 1 
ATOM   1255  N N   . ASN A  1 168 ? -24.415 -31.323 62.695  1.00 19.06  ? 173 ASN A N   1 
ATOM   1256  C CA  . ASN A  1 168 ? -23.301 -31.297 61.758  1.00 18.42  ? 173 ASN A CA  1 
ATOM   1257  C C   . ASN A  1 168 ? -22.949 -29.872 61.323  1.00 18.72  ? 173 ASN A C   1 
ATOM   1258  O O   . ASN A  1 168 ? -21.978 -29.651 60.592  1.00 18.01  ? 173 ASN A O   1 
ATOM   1259  C CB  . ASN A  1 168 ? -23.671 -32.146 60.535  1.00 17.90  ? 173 ASN A CB  1 
ATOM   1260  C CG  . ASN A  1 168 ? -25.100 -31.871 60.031  1.00 16.27  ? 173 ASN A CG  1 
ATOM   1261  O OD1 . ASN A  1 168 ? -26.095 -32.039 60.755  1.00 4.24   ? 173 ASN A OD1 1 
ATOM   1262  N ND2 . ASN A  1 168 ? -25.197 -31.454 58.778  1.00 15.87  ? 173 ASN A ND2 1 
ATOM   1263  N N   . LYS A  1 169 ? -23.749 -28.910 61.779  1.00 18.91  ? 174 LYS A N   1 
ATOM   1264  C CA  . LYS A  1 169 ? -23.591 -27.504 61.398  1.00 19.19  ? 174 LYS A CA  1 
ATOM   1265  C C   . LYS A  1 169 ? -23.729 -26.558 62.609  1.00 18.83  ? 174 LYS A C   1 
ATOM   1266  O O   . LYS A  1 169 ? -24.221 -26.976 63.661  1.00 18.99  ? 174 LYS A O   1 
ATOM   1267  C CB  . LYS A  1 169 ? -24.572 -27.141 60.271  1.00 19.62  ? 174 LYS A CB  1 
ATOM   1268  C CG  . LYS A  1 169 ? -26.025 -27.578 60.496  1.00 22.36  ? 174 LYS A CG  1 
ATOM   1269  C CD  . LYS A  1 169 ? -26.919 -27.271 59.287  1.00 25.95  ? 174 LYS A CD  1 
ATOM   1270  C CE  . LYS A  1 169 ? -26.723 -28.274 58.150  1.00 27.36  ? 174 LYS A CE  1 
ATOM   1271  N NZ  . LYS A  1 169 ? -27.613 -27.989 56.988  1.00 28.86  ? 174 LYS A NZ  1 
ATOM   1272  N N   . PRO A  1 170 ? -23.276 -25.288 62.473  1.00 18.57  ? 175 PRO A N   1 
ATOM   1273  C CA  . PRO A  1 170 ? -23.334 -24.332 63.587  1.00 18.16  ? 175 PRO A CA  1 
ATOM   1274  C C   . PRO A  1 170 ? -24.742 -24.080 64.128  1.00 17.86  ? 175 PRO A C   1 
ATOM   1275  O O   . PRO A  1 170 ? -25.706 -24.032 63.359  1.00 18.04  ? 175 PRO A O   1 
ATOM   1276  C CB  . PRO A  1 170 ? -22.780 -23.043 62.974  1.00 17.99  ? 175 PRO A CB  1 
ATOM   1277  C CG  . PRO A  1 170 ? -21.909 -23.496 61.870  1.00 19.06  ? 175 PRO A CG  1 
ATOM   1278  C CD  . PRO A  1 170 ? -22.580 -24.712 61.306  1.00 18.85  ? 175 PRO A CD  1 
ATOM   1279  N N   . ALA A  1 171 ? -24.841 -23.927 65.447  1.00 16.99  ? 176 ALA A N   1 
ATOM   1280  C CA  . ALA A  1 171 ? -26.095 -23.590 66.111  1.00 16.10  ? 176 ALA A CA  1 
ATOM   1281  C C   . ALA A  1 171 ? -26.137 -22.099 66.417  1.00 16.17  ? 176 ALA A C   1 
ATOM   1282  O O   . ALA A  1 171 ? -25.202 -21.554 67.012  1.00 16.90  ? 176 ALA A O   1 
ATOM   1283  C CB  . ALA A  1 171 ? -26.249 -24.393 67.388  1.00 15.78  ? 176 ALA A CB  1 
ATOM   1284  N N   . LEU A  1 172 ? -27.217 -21.440 66.002  1.00 15.24  ? 177 LEU A N   1 
ATOM   1285  C CA  . LEU A  1 172 ? -27.399 -20.020 66.284  1.00 14.31  ? 177 LEU A CA  1 
ATOM   1286  C C   . LEU A  1 172 ? -28.064 -19.829 67.645  1.00 14.08  ? 177 LEU A C   1 
ATOM   1287  O O   . LEU A  1 172 ? -29.293 -19.881 67.765  1.00 14.92  ? 177 LEU A O   1 
ATOM   1288  C CB  . LEU A  1 172 ? -28.198 -19.339 65.168  1.00 13.84  ? 177 LEU A CB  1 
ATOM   1289  C CG  . LEU A  1 172 ? -28.445 -17.827 65.256  1.00 14.73  ? 177 LEU A CG  1 
ATOM   1290  C CD1 . LEU A  1 172 ? -27.172 -17.030 65.546  1.00 16.47  ? 177 LEU A CD1 1 
ATOM   1291  C CD2 . LEU A  1 172 ? -29.097 -17.337 63.982  1.00 15.77  ? 177 LEU A CD2 1 
ATOM   1292  N N   . ILE A  1 173 ? -27.241 -19.623 68.669  1.00 13.30  ? 178 ILE A N   1 
ATOM   1293  C CA  . ILE A  1 173 ? -27.729 -19.480 70.037  1.00 12.76  ? 178 ILE A CA  1 
ATOM   1294  C C   . ILE A  1 173 ? -28.151 -18.035 70.302  1.00 13.32  ? 178 ILE A C   1 
ATOM   1295  O O   . ILE A  1 173 ? -27.424 -17.096 69.971  1.00 13.81  ? 178 ILE A O   1 
ATOM   1296  C CB  . ILE A  1 173 ? -26.669 -19.939 71.069  1.00 12.49  ? 178 ILE A CB  1 
ATOM   1297  C CG1 . ILE A  1 173 ? -26.215 -21.386 70.789  1.00 12.13  ? 178 ILE A CG1 1 
ATOM   1298  C CG2 . ILE A  1 173 ? -27.176 -19.750 72.501  1.00 10.54  ? 178 ILE A CG2 1 
ATOM   1299  C CD1 . ILE A  1 173 ? -27.293 -22.469 70.942  1.00 9.05   ? 178 ILE A CD1 1 
ATOM   1300  N N   . ILE A  1 174 ? -29.339 -17.874 70.878  1.00 12.90  ? 179 ILE A N   1 
ATOM   1301  C CA  . ILE A  1 174 ? -29.910 -16.562 71.172  1.00 12.63  ? 179 ILE A CA  1 
ATOM   1302  C C   . ILE A  1 174 ? -30.256 -16.486 72.654  1.00 11.61  ? 179 ILE A C   1 
ATOM   1303  O O   . ILE A  1 174 ? -30.724 -17.462 73.230  1.00 11.75  ? 179 ILE A O   1 
ATOM   1304  C CB  . ILE A  1 174 ? -31.207 -16.304 70.347  1.00 12.92  ? 179 ILE A CB  1 
ATOM   1305  C CG1 . ILE A  1 174 ? -31.065 -16.794 68.897  1.00 14.42  ? 179 ILE A CG1 1 
ATOM   1306  C CG2 . ILE A  1 174 ? -31.620 -14.825 70.408  1.00 13.76  ? 179 ILE A CG2 1 
ATOM   1307  C CD1 . ILE A  1 174 ? -30.131 -15.966 68.021  1.00 14.57  ? 179 ILE A CD1 1 
ATOM   1308  N N   . TRP A  1 175 ? -30.018 -15.334 73.273  1.00 11.07  ? 180 TRP A N   1 
ATOM   1309  C CA  . TRP A  1 175 ? -30.453 -15.103 74.654  1.00 11.20  ? 180 TRP A CA  1 
ATOM   1310  C C   . TRP A  1 175 ? -30.799 -13.636 74.873  1.00 11.07  ? 180 TRP A C   1 
ATOM   1311  O O   . TRP A  1 175 ? -30.393 -12.773 74.089  1.00 11.19  ? 180 TRP A O   1 
ATOM   1312  C CB  . TRP A  1 175 ? -29.404 -15.587 75.667  1.00 10.29  ? 180 TRP A CB  1 
ATOM   1313  C CG  . TRP A  1 175 ? -28.104 -14.828 75.650  1.00 13.11  ? 180 TRP A CG  1 
ATOM   1314  C CD1 . TRP A  1 175 ? -27.737 -13.807 76.483  1.00 14.99  ? 180 TRP A CD1 1 
ATOM   1315  C CD2 . TRP A  1 175 ? -26.994 -15.041 74.767  1.00 14.25  ? 180 TRP A CD2 1 
ATOM   1316  N NE1 . TRP A  1 175 ? -26.474 -13.367 76.169  1.00 14.33  ? 180 TRP A NE1 1 
ATOM   1317  C CE2 . TRP A  1 175 ? -25.994 -14.108 75.122  1.00 14.28  ? 180 TRP A CE2 1 
ATOM   1318  C CE3 . TRP A  1 175 ? -26.748 -15.928 73.709  1.00 12.97  ? 180 TRP A CE3 1 
ATOM   1319  C CZ2 . TRP A  1 175 ? -24.767 -14.037 74.457  1.00 14.15  ? 180 TRP A CZ2 1 
ATOM   1320  C CZ3 . TRP A  1 175 ? -25.528 -15.855 73.049  1.00 15.24  ? 180 TRP A CZ3 1 
ATOM   1321  C CH2 . TRP A  1 175 ? -24.553 -14.915 73.426  1.00 13.82  ? 180 TRP A CH2 1 
ATOM   1322  N N   . GLY A  1 176 ? -31.550 -13.355 75.934  1.00 10.38  ? 181 GLY A N   1 
ATOM   1323  C CA  . GLY A  1 176 ? -31.955 -11.986 76.227  1.00 10.59  ? 181 GLY A CA  1 
ATOM   1324  C C   . GLY A  1 176 ? -31.606 -11.508 77.623  1.00 10.50  ? 181 GLY A C   1 
ATOM   1325  O O   . GLY A  1 176 ? -31.548 -12.298 78.569  1.00 10.99  ? 181 GLY A O   1 
ATOM   1326  N N   . VAL A  1 177 ? -31.370 -10.207 77.745  1.00 9.76   ? 182 VAL A N   1 
ATOM   1327  C CA  . VAL A  1 177 ? -31.179 -9.585  79.045  1.00 9.91   ? 182 VAL A CA  1 
ATOM   1328  C C   . VAL A  1 177 ? -32.335 -8.624  79.294  1.00 10.56  ? 182 VAL A C   1 
ATOM   1329  O O   . VAL A  1 177 ? -32.562 -7.695  78.518  1.00 10.48  ? 182 VAL A O   1 
ATOM   1330  C CB  . VAL A  1 177 ? -29.809 -8.861  79.148  1.00 9.80   ? 182 VAL A CB  1 
ATOM   1331  C CG1 . VAL A  1 177 ? -29.669 -8.136  80.486  1.00 9.11   ? 182 VAL A CG1 1 
ATOM   1332  C CG2 . VAL A  1 177 ? -28.674 -9.848  78.974  1.00 6.89   ? 182 VAL A CG2 1 
ATOM   1333  N N   . HIS A  1 178 ? -33.086 -8.869  80.362  1.00 11.78  ? 183 HIS A N   1 
ATOM   1334  C CA  . HIS A  1 178 ? -34.196 -7.993  80.711  1.00 12.62  ? 183 HIS A CA  1 
ATOM   1335  C C   . HIS A  1 178 ? -33.728 -6.836  81.585  1.00 13.58  ? 183 HIS A C   1 
ATOM   1336  O O   . HIS A  1 178 ? -33.189 -7.038  82.675  1.00 14.56  ? 183 HIS A O   1 
ATOM   1337  C CB  . HIS A  1 178 ? -35.335 -8.755  81.394  1.00 11.40  ? 183 HIS A CB  1 
ATOM   1338  C CG  . HIS A  1 178 ? -36.439 -7.867  81.878  1.00 13.42  ? 183 HIS A CG  1 
ATOM   1339  N ND1 . HIS A  1 178 ? -36.798 -7.780  83.206  1.00 13.81  ? 183 HIS A ND1 1 
ATOM   1340  C CD2 . HIS A  1 178 ? -37.244 -7.001  81.214  1.00 14.00  ? 183 HIS A CD2 1 
ATOM   1341  C CE1 . HIS A  1 178 ? -37.783 -6.909  83.338  1.00 13.09  ? 183 HIS A CE1 1 
ATOM   1342  N NE2 . HIS A  1 178 ? -38.072 -6.422  82.144  1.00 11.52  ? 183 HIS A NE2 1 
ATOM   1343  N N   . HIS A  1 179 ? -33.931 -5.625  81.084  1.00 13.84  ? 184 HIS A N   1 
ATOM   1344  C CA  . HIS A  1 179 ? -33.665 -4.422  81.842  1.00 14.49  ? 184 HIS A CA  1 
ATOM   1345  C C   . HIS A  1 179 ? -35.009 -3.910  82.339  1.00 15.16  ? 184 HIS A C   1 
ATOM   1346  O O   . HIS A  1 179 ? -35.867 -3.513  81.544  1.00 16.37  ? 184 HIS A O   1 
ATOM   1347  C CB  . HIS A  1 179 ? -32.946 -3.387  80.972  1.00 14.49  ? 184 HIS A CB  1 
ATOM   1348  C CG  . HIS A  1 179 ? -31.767 -3.939  80.229  1.00 16.32  ? 184 HIS A CG  1 
ATOM   1349  N ND1 . HIS A  1 179 ? -30.476 -3.850  80.707  1.00 17.99  ? 184 HIS A ND1 1 
ATOM   1350  C CD2 . HIS A  1 179 ? -31.686 -4.602  79.051  1.00 14.83  ? 184 HIS A CD2 1 
ATOM   1351  C CE1 . HIS A  1 179 ? -29.651 -4.432  79.854  1.00 16.62  ? 184 HIS A CE1 1 
ATOM   1352  N NE2 . HIS A  1 179 ? -30.360 -4.898  78.841  1.00 15.44  ? 184 HIS A NE2 1 
ATOM   1353  N N   . SER A  1 180 ? -35.192 -3.955  83.656  1.00 15.09  ? 185 SER A N   1 
ATOM   1354  C CA  . SER A  1 180 ? -36.451 -3.589  84.300  1.00 14.80  ? 185 SER A CA  1 
ATOM   1355  C C   . SER A  1 180 ? -36.701 -2.085  84.243  1.00 15.01  ? 185 SER A C   1 
ATOM   1356  O O   . SER A  1 180 ? -35.786 -1.305  83.970  1.00 15.44  ? 185 SER A O   1 
ATOM   1357  C CB  . SER A  1 180 ? -36.448 -4.058  85.758  1.00 14.67  ? 185 SER A CB  1 
ATOM   1358  O OG  . SER A  1 180 ? -35.882 -5.353  85.874  1.00 15.31  ? 185 SER A OG  1 
ATOM   1359  N N   . GLU A  1 181 ? -37.946 -1.687  84.502  1.00 15.22  ? 186 GLU A N   1 
ATOM   1360  C CA  . GLU A  1 181 ? -38.325 -0.272  84.578  1.00 15.44  ? 186 GLU A CA  1 
ATOM   1361  C C   . GLU A  1 181 ? -37.564 0.470   85.685  1.00 15.03  ? 186 GLU A C   1 
ATOM   1362  O O   . GLU A  1 181 ? -37.253 1.656   85.548  1.00 15.03  ? 186 GLU A O   1 
ATOM   1363  C CB  . GLU A  1 181 ? -39.844 -0.147  84.789  1.00 15.73  ? 186 GLU A CB  1 
ATOM   1364  C CG  . GLU A  1 181 ? -40.401 1.284   84.802  1.00 17.70  ? 186 GLU A CG  1 
ATOM   1365  C CD  . GLU A  1 181 ? -40.445 1.945   83.427  1.00 22.84  ? 186 GLU A CD  1 
ATOM   1366  O OE1 . GLU A  1 181 ? -40.240 1.257   82.397  1.00 25.40  ? 186 GLU A OE1 1 
ATOM   1367  O OE2 . GLU A  1 181 ? -40.691 3.169   83.379  1.00 22.37  ? 186 GLU A OE2 1 
ATOM   1368  N N   . SER A  1 182 ? -37.263 -0.238  86.772  1.00 14.48  ? 187 SER A N   1 
ATOM   1369  C CA  . SER A  1 182 ? -36.616 0.361   87.934  1.00 14.47  ? 187 SER A CA  1 
ATOM   1370  C C   . SER A  1 182 ? -35.901 -0.678  88.798  1.00 14.13  ? 187 SER A C   1 
ATOM   1371  O O   . SER A  1 182 ? -36.036 -1.884  88.581  1.00 14.81  ? 187 SER A O   1 
ATOM   1372  C CB  . SER A  1 182 ? -37.654 1.111   88.778  1.00 14.77  ? 187 SER A CB  1 
ATOM   1373  O OG  . SER A  1 182 ? -38.573 0.209   89.372  1.00 16.36  ? 187 SER A OG  1 
ATOM   1374  N N   . VAL A  1 183 ? -35.145 -0.191  89.779  1.00 13.36  ? 188 VAL A N   1 
ATOM   1375  C CA  . VAL A  1 183 ? -34.507 -1.037  90.784  1.00 12.76  ? 188 VAL A CA  1 
ATOM   1376  C C   . VAL A  1 183 ? -35.545 -1.886  91.526  1.00 12.52  ? 188 VAL A C   1 
ATOM   1377  O O   . VAL A  1 183 ? -35.345 -3.088  91.728  1.00 12.52  ? 188 VAL A O   1 
ATOM   1378  C CB  . VAL A  1 183 ? -33.684 -0.180  91.782  1.00 13.20  ? 188 VAL A CB  1 
ATOM   1379  C CG1 . VAL A  1 183 ? -33.359 -0.961  93.060  1.00 12.07  ? 188 VAL A CG1 1 
ATOM   1380  C CG2 . VAL A  1 183 ? -32.408 0.330   91.117  1.00 12.17  ? 188 VAL A CG2 1 
ATOM   1381  N N   . SER A  1 184 ? -36.655 -1.255  91.909  1.00 12.30  ? 189 SER A N   1 
ATOM   1382  C CA  . SER A  1 184 ? -37.752 -1.934  92.598  1.00 11.92  ? 189 SER A CA  1 
ATOM   1383  C C   . SER A  1 184 ? -38.303 -3.107  91.797  1.00 12.23  ? 189 SER A C   1 
ATOM   1384  O O   . SER A  1 184 ? -38.523 -4.191  92.349  1.00 11.58  ? 189 SER A O   1 
ATOM   1385  C CB  . SER A  1 184 ? -38.886 -0.956  92.896  1.00 11.32  ? 189 SER A CB  1 
ATOM   1386  O OG  . SER A  1 184 ? -38.451 0.066   93.762  1.00 10.55  ? 189 SER A OG  1 
ATOM   1387  N N   . GLU A  1 185 ? -38.518 -2.883  90.498  1.00 12.12  ? 190 GLU A N   1 
ATOM   1388  C CA  . GLU A  1 185 ? -39.120 -3.889  89.632  1.00 11.79  ? 190 GLU A CA  1 
ATOM   1389  C C   . GLU A  1 185 ? -38.192 -5.072  89.383  1.00 11.81  ? 190 GLU A C   1 
ATOM   1390  O O   . GLU A  1 185 ? -38.651 -6.212  89.296  1.00 12.64  ? 190 GLU A O   1 
ATOM   1391  C CB  . GLU A  1 185 ? -39.584 -3.283  88.312  1.00 11.78  ? 190 GLU A CB  1 
ATOM   1392  C CG  . GLU A  1 185 ? -40.552 -4.185  87.554  1.00 14.49  ? 190 GLU A CG  1 
ATOM   1393  C CD  . GLU A  1 185 ? -40.947 -3.625  86.207  1.00 18.82  ? 190 GLU A CD  1 
ATOM   1394  O OE1 . GLU A  1 185 ? -40.056 -3.471  85.340  1.00 16.50  ? 190 GLU A OE1 1 
ATOM   1395  O OE2 . GLU A  1 185 ? -42.152 -3.347  86.017  1.00 19.67  ? 190 GLU A OE2 1 
ATOM   1396  N N   . GLN A  1 186 ? -36.895 -4.802  89.265  1.00 11.78  ? 191 GLN A N   1 
ATOM   1397  C CA  . GLN A  1 186 ? -35.900 -5.869  89.174  1.00 12.16  ? 191 GLN A CA  1 
ATOM   1398  C C   . GLN A  1 186 ? -35.972 -6.720  90.442  1.00 12.40  ? 191 GLN A C   1 
ATOM   1399  O O   . GLN A  1 186 ? -35.981 -7.953  90.377  1.00 12.26  ? 191 GLN A O   1 
ATOM   1400  C CB  . GLN A  1 186 ? -34.495 -5.287  88.968  1.00 12.37  ? 191 GLN A CB  1 
ATOM   1401  C CG  . GLN A  1 186 ? -33.392 -6.322  88.762  1.00 12.59  ? 191 GLN A CG  1 
ATOM   1402  C CD  . GLN A  1 186 ? -32.105 -5.706  88.240  1.00 15.42  ? 191 GLN A CD  1 
ATOM   1403  O OE1 . GLN A  1 186 ? -32.027 -5.292  87.084  1.00 18.39  ? 191 GLN A OE1 1 
ATOM   1404  N NE2 . GLN A  1 186 ? -31.084 -5.654  89.088  1.00 15.27  ? 191 GLN A NE2 1 
ATOM   1405  N N   . THR A  1 187 ? -36.055 -6.045  91.587  1.00 12.81  ? 192 THR A N   1 
ATOM   1406  C CA  . THR A  1 187 ? -36.173 -6.705  92.882  1.00 13.08  ? 192 THR A CA  1 
ATOM   1407  C C   . THR A  1 187 ? -37.449 -7.546  92.961  1.00 13.54  ? 192 THR A C   1 
ATOM   1408  O O   . THR A  1 187 ? -37.412 -8.676  93.452  1.00 13.99  ? 192 THR A O   1 
ATOM   1409  C CB  . THR A  1 187 ? -36.103 -5.677  94.042  1.00 13.14  ? 192 THR A CB  1 
ATOM   1410  O OG1 . THR A  1 187 ? -34.839 -5.005  94.001  1.00 14.39  ? 192 THR A OG1 1 
ATOM   1411  C CG2 . THR A  1 187 ? -36.264 -6.347  95.402  1.00 11.14  ? 192 THR A CG2 1 
ATOM   1412  N N   . LYS A  1 188 ? -38.564 -7.012  92.465  1.00 13.79  ? 193 LYS A N   1 
ATOM   1413  C CA  . LYS A  1 188 ? -39.826 -7.748  92.493  1.00 14.80  ? 193 LYS A CA  1 
ATOM   1414  C C   . LYS A  1 188 ? -39.738 -9.053  91.698  1.00 15.33  ? 193 LYS A C   1 
ATOM   1415  O O   . LYS A  1 188 ? -40.103 -10.118 92.205  1.00 15.60  ? 193 LYS A O   1 
ATOM   1416  C CB  . LYS A  1 188 ? -40.990 -6.895  91.984  1.00 15.02  ? 193 LYS A CB  1 
ATOM   1417  C CG  . LYS A  1 188 ? -42.346 -7.610  92.066  1.00 18.04  ? 193 LYS A CG  1 
ATOM   1418  C CD  . LYS A  1 188 ? -43.509 -6.743  91.602  1.00 23.37  ? 193 LYS A CD  1 
ATOM   1419  C CE  . LYS A  1 188 ? -43.558 -6.619  90.081  1.00 25.93  ? 193 LYS A CE  1 
ATOM   1420  N NZ  . LYS A  1 188 ? -44.810 -5.951  89.631  1.00 27.89  ? 193 LYS A NZ  1 
ATOM   1421  N N   . LEU A  1 189 ? -39.242 -8.966  90.466  1.00 15.27  ? 194 LEU A N   1 
ATOM   1422  C CA  . LEU A  1 189 ? -39.196 -10.126 89.578  1.00 15.51  ? 194 LEU A CA  1 
ATOM   1423  C C   . LEU A  1 189 ? -38.135 -11.156 89.970  1.00 15.83  ? 194 LEU A C   1 
ATOM   1424  O O   . LEU A  1 189 ? -38.388 -12.358 89.897  1.00 16.33  ? 194 LEU A O   1 
ATOM   1425  C CB  . LEU A  1 189 ? -38.987 -9.705  88.115  1.00 15.19  ? 194 LEU A CB  1 
ATOM   1426  C CG  . LEU A  1 189 ? -39.859 -8.646  87.429  1.00 15.02  ? 194 LEU A CG  1 
ATOM   1427  C CD1 . LEU A  1 189 ? -39.470 -8.540  85.963  1.00 14.74  ? 194 LEU A CD1 1 
ATOM   1428  C CD2 . LEU A  1 189 ? -41.346 -8.931  87.553  1.00 13.88  ? 194 LEU A CD2 1 
ATOM   1429  N N   . TYR A  1 190 ? -36.960 -10.689 90.390  1.00 15.79  ? 195 TYR A N   1 
ATOM   1430  C CA  . TYR A  1 190 ? -35.794 -11.573 90.512  1.00 16.13  ? 195 TYR A CA  1 
ATOM   1431  C C   . TYR A  1 190 ? -35.110 -11.575 91.887  1.00 15.74  ? 195 TYR A C   1 
ATOM   1432  O O   . TYR A  1 190 ? -34.109 -12.262 92.082  1.00 14.63  ? 195 TYR A O   1 
ATOM   1433  C CB  . TYR A  1 190 ? -34.763 -11.244 89.416  1.00 16.55  ? 195 TYR A CB  1 
ATOM   1434  C CG  . TYR A  1 190 ? -35.348 -11.008 88.036  1.00 16.28  ? 195 TYR A CG  1 
ATOM   1435  C CD1 . TYR A  1 190 ? -35.367 -9.731  87.475  1.00 17.96  ? 195 TYR A CD1 1 
ATOM   1436  C CD2 . TYR A  1 190 ? -35.883 -12.057 87.293  1.00 17.16  ? 195 TYR A CD2 1 
ATOM   1437  C CE1 . TYR A  1 190 ? -35.904 -9.507  86.208  1.00 18.94  ? 195 TYR A CE1 1 
ATOM   1438  C CE2 . TYR A  1 190 ? -36.423 -11.843 86.029  1.00 16.58  ? 195 TYR A CE2 1 
ATOM   1439  C CZ  . TYR A  1 190 ? -36.431 -10.570 85.492  1.00 19.30  ? 195 TYR A CZ  1 
ATOM   1440  O OH  . TYR A  1 190 ? -36.963 -10.365 84.238  1.00 20.87  ? 195 TYR A OH  1 
ATOM   1441  N N   . GLY A  1 191 ? -35.655 -10.818 92.834  1.00 16.39  ? 196 GLY A N   1 
ATOM   1442  C CA  . GLY A  1 191 ? -35.031 -10.651 94.148  1.00 16.70  ? 196 GLY A CA  1 
ATOM   1443  C C   . GLY A  1 191 ? -34.051 -9.492  94.147  1.00 16.93  ? 196 GLY A C   1 
ATOM   1444  O O   . GLY A  1 191 ? -33.586 -9.061  93.085  1.00 16.27  ? 196 GLY A O   1 
ATOM   1445  N N   . SER A  1 192 ? -33.733 -8.988  95.339  1.00 17.00  ? 197 SER A N   1 
ATOM   1446  C CA  . SER A  1 192 ? -32.823 -7.851  95.479  1.00 16.79  ? 197 SER A CA  1 
ATOM   1447  C C   . SER A  1 192 ? -31.380 -8.261  95.215  1.00 16.79  ? 197 SER A C   1 
ATOM   1448  O O   . SER A  1 192 ? -31.084 -9.445  95.058  1.00 16.40  ? 197 SER A O   1 
ATOM   1449  C CB  . SER A  1 192 ? -32.955 -7.225  96.867  1.00 16.63  ? 197 SER A CB  1 
ATOM   1450  O OG  . SER A  1 192 ? -32.629 -8.158  97.882  1.00 18.37  ? 197 SER A OG  1 
ATOM   1451  N N   . GLY A  1 193 ? -30.488 -7.277  95.160  1.00 17.41  ? 198 GLY A N   1 
ATOM   1452  C CA  . GLY A  1 193 ? -29.071 -7.536  94.935  1.00 18.21  ? 198 GLY A CA  1 
ATOM   1453  C C   . GLY A  1 193 ? -28.711 -7.423  93.471  1.00 19.22  ? 198 GLY A C   1 
ATOM   1454  O O   . GLY A  1 193 ? -29.587 -7.321  92.611  1.00 18.97  ? 198 GLY A O   1 
ATOM   1455  N N   . ASN A  1 194 ? -27.416 -7.446  93.185  1.00 20.62  ? 199 ASN A N   1 
ATOM   1456  C CA  . ASN A  1 194 ? -26.942 -7.295  91.817  1.00 22.25  ? 199 ASN A CA  1 
ATOM   1457  C C   . ASN A  1 194 ? -27.151 -8.571  91.001  1.00 21.53  ? 199 ASN A C   1 
ATOM   1458  O O   . ASN A  1 194 ? -27.281 -9.663  91.561  1.00 21.65  ? 199 ASN A O   1 
ATOM   1459  C CB  . ASN A  1 194 ? -25.471 -6.862  91.802  1.00 23.77  ? 199 ASN A CB  1 
ATOM   1460  C CG  . ASN A  1 194 ? -25.209 -5.706  90.841  1.00 28.25  ? 199 ASN A CG  1 
ATOM   1461  O OD1 . ASN A  1 194 ? -25.479 -5.800  89.638  1.00 30.98  ? 199 ASN A OD1 1 
ATOM   1462  N ND2 . ASN A  1 194 ? -24.676 -4.606  91.374  1.00 29.50  ? 199 ASN A ND2 1 
ATOM   1463  N N   . LYS A  1 195 ? -27.202 -8.420  89.681  1.00 20.73  ? 200 LYS A N   1 
ATOM   1464  C CA  . LYS A  1 195 ? -27.448 -9.541  88.778  1.00 19.74  ? 200 LYS A CA  1 
ATOM   1465  C C   . LYS A  1 195 ? -26.351 -9.657  87.727  1.00 19.93  ? 200 LYS A C   1 
ATOM   1466  O O   . LYS A  1 195 ? -25.903 -8.649  87.171  1.00 20.33  ? 200 LYS A O   1 
ATOM   1467  C CB  . LYS A  1 195 ? -28.812 -9.392  88.094  1.00 19.34  ? 200 LYS A CB  1 
ATOM   1468  C CG  . LYS A  1 195 ? -30.001 -9.290  89.042  1.00 18.04  ? 200 LYS A CG  1 
ATOM   1469  C CD  . LYS A  1 195 ? -30.224 -10.578 89.816  1.00 16.63  ? 200 LYS A CD  1 
ATOM   1470  C CE  . LYS A  1 195 ? -31.251 -10.386 90.909  1.00 15.65  ? 200 LYS A CE  1 
ATOM   1471  N NZ  . LYS A  1 195 ? -31.639 -11.692 91.492  1.00 13.17  ? 200 LYS A NZ  1 
ATOM   1472  N N   . LEU A  1 196 ? -25.917 -10.887 87.465  1.00 19.41  ? 201 LEU A N   1 
ATOM   1473  C CA  . LEU A  1 196 ? -24.929 -11.144 86.420  1.00 19.18  ? 201 LEU A CA  1 
ATOM   1474  C C   . LEU A  1 196 ? -25.301 -12.355 85.576  1.00 19.04  ? 201 LEU A C   1 
ATOM   1475  O O   . LEU A  1 196 ? -25.734 -13.385 86.096  1.00 19.54  ? 201 LEU A O   1 
ATOM   1476  C CB  . LEU A  1 196 ? -23.521 -11.315 87.007  1.00 19.40  ? 201 LEU A CB  1 
ATOM   1477  C CG  . LEU A  1 196 ? -22.374 -11.372 85.981  1.00 19.80  ? 201 LEU A CG  1 
ATOM   1478  C CD1 . LEU A  1 196 ? -21.796 -9.997  85.683  1.00 15.12  ? 201 LEU A CD1 1 
ATOM   1479  C CD2 . LEU A  1 196 ? -21.278 -12.314 86.435  1.00 18.61  ? 201 LEU A CD2 1 
ATOM   1480  N N   . ILE A  1 197 ? -25.123 -12.210 84.267  1.00 18.66  ? 202 ILE A N   1 
ATOM   1481  C CA  . ILE A  1 197 ? -25.366 -13.274 83.304  1.00 18.32  ? 202 ILE A CA  1 
ATOM   1482  C C   . ILE A  1 197 ? -24.069 -13.529 82.549  1.00 18.63  ? 202 ILE A C   1 
ATOM   1483  O O   . ILE A  1 197 ? -23.479 -12.601 81.990  1.00 18.47  ? 202 ILE A O   1 
ATOM   1484  C CB  . ILE A  1 197 ? -26.491 -12.884 82.308  1.00 18.44  ? 202 ILE A CB  1 
ATOM   1485  C CG1 . ILE A  1 197 ? -27.830 -12.746 83.043  1.00 17.67  ? 202 ILE A CG1 1 
ATOM   1486  C CG2 . ILE A  1 197 ? -26.584 -13.895 81.158  1.00 15.85  ? 202 ILE A CG2 1 
ATOM   1487  C CD1 . ILE A  1 197 ? -28.860 -11.921 82.303  1.00 20.26  ? 202 ILE A CD1 1 
ATOM   1488  N N   . THR A  1 198 ? -23.625 -14.782 82.540  1.00 19.21  ? 203 THR A N   1 
ATOM   1489  C CA  . THR A  1 198 ? -22.386 -15.146 81.855  1.00 19.71  ? 203 THR A CA  1 
ATOM   1490  C C   . THR A  1 198 ? -22.637 -16.233 80.815  1.00 19.71  ? 203 THR A C   1 
ATOM   1491  O O   . THR A  1 198 ? -23.261 -17.255 81.100  1.00 19.84  ? 203 THR A O   1 
ATOM   1492  C CB  . THR A  1 198 ? -21.287 -15.569 82.855  1.00 19.96  ? 203 THR A CB  1 
ATOM   1493  O OG1 . THR A  1 198 ? -21.170 -14.578 83.886  1.00 19.96  ? 203 THR A OG1 1 
ATOM   1494  C CG2 . THR A  1 198 ? -19.941 -15.721 82.155  1.00 21.99  ? 203 THR A CG2 1 
ATOM   1495  N N   . VAL A  1 199 ? -22.151 -15.987 79.604  1.00 20.13  ? 204 VAL A N   1 
ATOM   1496  C CA  . VAL A  1 199 ? -22.350 -16.887 78.475  1.00 21.22  ? 204 VAL A CA  1 
ATOM   1497  C C   . VAL A  1 199 ? -20.984 -17.282 77.914  1.00 22.33  ? 204 VAL A C   1 
ATOM   1498  O O   . VAL A  1 199 ? -20.210 -16.430 77.465  1.00 21.74  ? 204 VAL A O   1 
ATOM   1499  C CB  . VAL A  1 199 ? -23.232 -16.230 77.371  1.00 21.11  ? 204 VAL A CB  1 
ATOM   1500  C CG1 . VAL A  1 199 ? -23.450 -17.184 76.196  1.00 19.77  ? 204 VAL A CG1 1 
ATOM   1501  C CG2 . VAL A  1 199 ? -24.571 -15.773 77.946  1.00 20.26  ? 204 VAL A CG2 1 
ATOM   1502  N N   . ARG A  1 200 ? -20.691 -18.580 77.951  1.00 23.78  ? 205 ARG A N   1 
ATOM   1503  C CA  . ARG A  1 200 ? -19.379 -19.077 77.557  1.00 24.98  ? 205 ARG A CA  1 
ATOM   1504  C C   . ARG A  1 200 ? -19.417 -20.299 76.640  1.00 25.09  ? 205 ARG A C   1 
ATOM   1505  O O   . ARG A  1 200 ? -20.069 -21.302 76.940  1.00 25.12  ? 205 ARG A O   1 
ATOM   1506  C CB  . ARG A  1 200 ? -18.524 -19.370 78.798  1.00 25.51  ? 205 ARG A CB  1 
ATOM   1507  C CG  . ARG A  1 200 ? -17.803 -18.146 79.352  1.00 29.02  ? 205 ARG A CG  1 
ATOM   1508  C CD  . ARG A  1 200 ? -16.922 -18.488 80.549  1.00 35.25  ? 205 ARG A CD  1 
ATOM   1509  N NE  . ARG A  1 200 ? -17.652 -18.415 81.816  1.00 40.48  ? 205 ARG A NE  1 
ATOM   1510  C CZ  . ARG A  1 200 ? -18.145 -19.463 82.474  1.00 42.49  ? 205 ARG A CZ  1 
ATOM   1511  N NH1 . ARG A  1 200 ? -17.994 -20.695 82.000  1.00 43.20  ? 205 ARG A NH1 1 
ATOM   1512  N NH2 . ARG A  1 200 ? -18.792 -19.277 83.616  1.00 43.30  ? 205 ARG A NH2 1 
ATOM   1513  N N   . SER A  1 201 ? -18.723 -20.182 75.512  1.00 25.41  ? 206 SER A N   1 
ATOM   1514  C CA  . SER A  1 201 ? -18.374 -21.326 74.675  1.00 26.15  ? 206 SER A CA  1 
ATOM   1515  C C   . SER A  1 201 ? -16.856 -21.324 74.484  1.00 26.70  ? 206 SER A C   1 
ATOM   1516  O O   . SER A  1 201 ? -16.170 -20.419 74.971  1.00 27.05  ? 206 SER A O   1 
ATOM   1517  C CB  . SER A  1 201 ? -19.099 -21.270 73.329  1.00 25.78  ? 206 SER A CB  1 
ATOM   1518  O OG  . SER A  1 201 ? -18.556 -20.267 72.490  1.00 25.42  ? 206 SER A OG  1 
ATOM   1519  N N   . SER A  1 202 ? -16.329 -22.325 73.780  1.00 26.64  ? 207 SER A N   1 
ATOM   1520  C CA  . SER A  1 202 ? -14.883 -22.418 73.551  1.00 26.57  ? 207 SER A CA  1 
ATOM   1521  C C   . SER A  1 202 ? -14.347 -21.328 72.605  1.00 26.52  ? 207 SER A C   1 
ATOM   1522  O O   . SER A  1 202 ? -13.147 -21.275 72.329  1.00 26.64  ? 207 SER A O   1 
ATOM   1523  C CB  . SER A  1 202 ? -14.491 -23.822 73.066  1.00 26.36  ? 207 SER A CB  1 
ATOM   1524  O OG  . SER A  1 202 ? -15.076 -24.120 71.811  1.00 25.63  ? 207 SER A OG  1 
ATOM   1525  N N   . LYS A  1 203 ? -15.238 -20.458 72.131  1.00 26.53  ? 208 LYS A N   1 
ATOM   1526  C CA  . LYS A  1 203 ? -14.860 -19.320 71.285  1.00 26.90  ? 208 LYS A CA  1 
ATOM   1527  C C   . LYS A  1 203 ? -15.398 -17.976 71.797  1.00 27.19  ? 208 LYS A C   1 
ATOM   1528  O O   . LYS A  1 203 ? -14.851 -16.921 71.469  1.00 27.10  ? 208 LYS A O   1 
ATOM   1529  C CB  . LYS A  1 203 ? -15.327 -19.544 69.844  1.00 26.68  ? 208 LYS A CB  1 
ATOM   1530  C CG  . LYS A  1 203 ? -14.437 -20.465 69.030  1.00 27.84  ? 208 LYS A CG  1 
ATOM   1531  C CD  . LYS A  1 203 ? -14.923 -20.576 67.585  1.00 30.00  ? 208 LYS A CD  1 
ATOM   1532  C CE  . LYS A  1 203 ? -13.814 -21.060 66.651  1.00 29.83  ? 208 LYS A CE  1 
ATOM   1533  N NZ  . LYS A  1 203 ? -13.235 -22.374 67.065  1.00 29.06  ? 208 LYS A NZ  1 
ATOM   1534  N N   . TYR A  1 204 ? -16.460 -18.024 72.600  1.00 27.50  ? 209 TYR A N   1 
ATOM   1535  C CA  . TYR A  1 204 ? -17.179 -16.823 73.036  1.00 27.58  ? 209 TYR A CA  1 
ATOM   1536  C C   . TYR A  1 204 ? -17.210 -16.718 74.557  1.00 28.66  ? 209 TYR A C   1 
ATOM   1537  O O   . TYR A  1 204 ? -17.396 -17.720 75.251  1.00 29.64  ? 209 TYR A O   1 
ATOM   1538  C CB  . TYR A  1 204 ? -18.601 -16.848 72.468  1.00 26.81  ? 209 TYR A CB  1 
ATOM   1539  C CG  . TYR A  1 204 ? -19.496 -15.683 72.847  1.00 24.51  ? 209 TYR A CG  1 
ATOM   1540  C CD1 . TYR A  1 204 ? -19.725 -14.634 71.953  1.00 20.22  ? 209 TYR A CD1 1 
ATOM   1541  C CD2 . TYR A  1 204 ? -20.152 -15.652 74.084  1.00 22.14  ? 209 TYR A CD2 1 
ATOM   1542  C CE1 . TYR A  1 204 ? -20.567 -13.571 72.291  1.00 19.35  ? 209 TYR A CE1 1 
ATOM   1543  C CE2 . TYR A  1 204 ? -20.990 -14.594 74.432  1.00 18.55  ? 209 TYR A CE2 1 
ATOM   1544  C CZ  . TYR A  1 204 ? -21.194 -13.560 73.532  1.00 19.04  ? 209 TYR A CZ  1 
ATOM   1545  O OH  . TYR A  1 204 ? -22.021 -12.516 73.880  1.00 16.57  ? 209 TYR A OH  1 
ATOM   1546  N N   . GLN A  1 205 ? -17.040 -15.495 75.061  1.00 29.14  ? 210 GLN A N   1 
ATOM   1547  C CA  . GLN A  1 205 ? -17.000 -15.225 76.498  1.00 29.35  ? 210 GLN A CA  1 
ATOM   1548  C C   . GLN A  1 205 ? -17.429 -13.780 76.801  1.00 29.19  ? 210 GLN A C   1 
ATOM   1549  O O   . GLN A  1 205 ? -16.681 -12.836 76.532  1.00 29.51  ? 210 GLN A O   1 
ATOM   1550  C CB  . GLN A  1 205 ? -15.590 -15.497 77.029  1.00 29.38  ? 210 GLN A CB  1 
ATOM   1551  C CG  . GLN A  1 205 ? -15.413 -15.325 78.526  1.00 31.94  ? 210 GLN A CG  1 
ATOM   1552  C CD  . GLN A  1 205 ? -14.029 -15.739 78.995  1.00 34.98  ? 210 GLN A CD  1 
ATOM   1553  O OE1 . GLN A  1 205 ? -13.882 -16.704 79.747  1.00 36.37  ? 210 GLN A OE1 1 
ATOM   1554  N NE2 . GLN A  1 205 ? -13.003 -15.016 78.545  1.00 35.06  ? 210 GLN A NE2 1 
ATOM   1555  N N   . GLN A  1 206 ? -18.635 -13.618 77.349  1.00 28.90  ? 211 GLN A N   1 
ATOM   1556  C CA  . GLN A  1 206 ? -19.183 -12.292 77.686  1.00 28.63  ? 211 GLN A CA  1 
ATOM   1557  C C   . GLN A  1 206 ? -20.014 -12.298 78.966  1.00 27.34  ? 211 GLN A C   1 
ATOM   1558  O O   . GLN A  1 206 ? -20.686 -13.282 79.278  1.00 26.81  ? 211 GLN A O   1 
ATOM   1559  C CB  . GLN A  1 206 ? -20.043 -11.742 76.543  1.00 29.27  ? 211 GLN A CB  1 
ATOM   1560  C CG  . GLN A  1 206 ? -19.273 -11.272 75.315  1.00 34.02  ? 211 GLN A CG  1 
ATOM   1561  C CD  . GLN A  1 206 ? -18.684 -9.879  75.462  1.00 39.95  ? 211 GLN A CD  1 
ATOM   1562  O OE1 . GLN A  1 206 ? -18.483 -9.378  76.573  1.00 40.47  ? 211 GLN A OE1 1 
ATOM   1563  N NE2 . GLN A  1 206 ? -18.395 -9.245  74.328  1.00 41.19  ? 211 GLN A NE2 1 
ATOM   1564  N N   . SER A  1 207 ? -19.964 -11.186 79.694  1.00 26.74  ? 212 SER A N   1 
ATOM   1565  C CA  . SER A  1 207 ? -20.784 -10.988 80.888  1.00 25.89  ? 212 SER A CA  1 
ATOM   1566  C C   . SER A  1 207 ? -21.782 -9.861  80.662  1.00 25.22  ? 212 SER A C   1 
ATOM   1567  O O   . SER A  1 207 ? -21.502 -8.908  79.932  1.00 25.55  ? 212 SER A O   1 
ATOM   1568  C CB  . SER A  1 207 ? -19.912 -10.685 82.103  1.00 25.84  ? 212 SER A CB  1 
ATOM   1569  O OG  . SER A  1 207 ? -19.106 -11.801 82.429  1.00 27.53  ? 212 SER A OG  1 
ATOM   1570  N N   . PHE A  1 208 ? -22.952 -9.980  81.282  1.00 24.13  ? 213 PHE A N   1 
ATOM   1571  C CA  . PHE A  1 208 ? -24.013 -8.993  81.118  1.00 23.08  ? 213 PHE A CA  1 
ATOM   1572  C C   . PHE A  1 208 ? -24.631 -8.641  82.466  1.00 22.93  ? 213 PHE A C   1 
ATOM   1573  O O   . PHE A  1 208 ? -24.996 -9.531  83.239  1.00 22.74  ? 213 PHE A O   1 
ATOM   1574  C CB  . PHE A  1 208 ? -25.099 -9.508  80.158  1.00 22.66  ? 213 PHE A CB  1 
ATOM   1575  C CG  . PHE A  1 208 ? -24.576 -9.948  78.813  1.00 21.41  ? 213 PHE A CG  1 
ATOM   1576  C CD1 . PHE A  1 208 ? -24.260 -11.288 78.576  1.00 20.79  ? 213 PHE A CD1 1 
ATOM   1577  C CD2 . PHE A  1 208 ? -24.404 -9.029  77.781  1.00 20.28  ? 213 PHE A CD2 1 
ATOM   1578  C CE1 . PHE A  1 208 ? -23.773 -11.705 77.332  1.00 18.74  ? 213 PHE A CE1 1 
ATOM   1579  C CE2 . PHE A  1 208 ? -23.918 -9.435  76.530  1.00 19.67  ? 213 PHE A CE2 1 
ATOM   1580  C CZ  . PHE A  1 208 ? -23.602 -10.777 76.308  1.00 19.21  ? 213 PHE A CZ  1 
ATOM   1581  N N   . THR A  1 209 ? -24.719 -7.345  82.754  1.00 22.66  ? 214 THR A N   1 
ATOM   1582  C CA  . THR A  1 209 ? -25.484 -6.864  83.905  1.00 22.31  ? 214 THR A CA  1 
ATOM   1583  C C   . THR A  1 209 ? -26.643 -6.016  83.408  1.00 21.40  ? 214 THR A C   1 
ATOM   1584  O O   . THR A  1 209 ? -26.471 -5.214  82.490  1.00 21.40  ? 214 THR A O   1 
ATOM   1585  C CB  . THR A  1 209 ? -24.635 -6.034  84.905  1.00 22.46  ? 214 THR A CB  1 
ATOM   1586  O OG1 . THR A  1 209 ? -24.216 -4.808  84.294  1.00 21.43  ? 214 THR A OG1 1 
ATOM   1587  C CG2 . THR A  1 209 ? -23.419 -6.815  85.371  1.00 22.08  ? 214 THR A CG2 1 
ATOM   1588  N N   . PRO A  1 210 ? -27.834 -6.204  83.997  1.00 20.91  ? 215 PRO A N   1 
ATOM   1589  C CA  . PRO A  1 210 ? -28.974 -5.380  83.606  1.00 20.86  ? 215 PRO A CA  1 
ATOM   1590  C C   . PRO A  1 210 ? -28.829 -3.932  84.066  1.00 20.47  ? 215 PRO A C   1 
ATOM   1591  O O   . PRO A  1 210 ? -28.305 -3.669  85.147  1.00 20.27  ? 215 PRO A O   1 
ATOM   1592  C CB  . PRO A  1 210 ? -30.163 -6.058  84.298  1.00 20.47  ? 215 PRO A CB  1 
ATOM   1593  C CG  . PRO A  1 210 ? -29.569 -6.846  85.401  1.00 21.45  ? 215 PRO A CG  1 
ATOM   1594  C CD  . PRO A  1 210 ? -28.222 -7.282  84.923  1.00 20.90  ? 215 PRO A CD  1 
ATOM   1595  N N   . ASN A  1 211 ? -29.289 -3.014  83.224  1.00 20.30  ? 216 ASN A N   1 
ATOM   1596  C CA  . ASN A  1 211 ? -29.267 -1.587  83.500  1.00 20.38  ? 216 ASN A CA  1 
ATOM   1597  C C   . ASN A  1 211 ? -30.707 -1.063  83.570  1.00 19.85  ? 216 ASN A C   1 
ATOM   1598  O O   . ASN A  1 211 ? -31.252 -0.597  82.563  1.00 19.87  ? 216 ASN A O   1 
ATOM   1599  C CB  . ASN A  1 211 ? -28.453 -0.869  82.409  1.00 20.69  ? 216 ASN A CB  1 
ATOM   1600  C CG  . ASN A  1 211 ? -28.401 0.644   82.595  1.00 22.58  ? 216 ASN A CG  1 
ATOM   1601  O OD1 . ASN A  1 211 ? -28.249 1.155   83.709  1.00 23.79  ? 216 ASN A OD1 1 
ATOM   1602  N ND2 . ASN A  1 211 ? -28.515 1.367   81.488  1.00 22.61  ? 216 ASN A ND2 1 
ATOM   1603  N N   . PRO A  1 212 ? -31.339 -1.160  84.756  1.00 19.39  ? 217 PRO A N   1 
ATOM   1604  C CA  . PRO A  1 212 ? -32.743 -0.761  84.905  1.00 19.49  ? 217 PRO A CA  1 
ATOM   1605  C C   . PRO A  1 212 ? -32.982 0.732   84.688  1.00 19.23  ? 217 PRO A C   1 
ATOM   1606  O O   . PRO A  1 212 ? -32.091 1.541   84.934  1.00 19.65  ? 217 PRO A O   1 
ATOM   1607  C CB  . PRO A  1 212 ? -33.069 -1.147  86.353  1.00 19.12  ? 217 PRO A CB  1 
ATOM   1608  C CG  . PRO A  1 212 ? -31.752 -1.209  87.041  1.00 18.57  ? 217 PRO A CG  1 
ATOM   1609  C CD  . PRO A  1 212 ? -30.793 -1.703  86.013  1.00 19.32  ? 217 PRO A CD  1 
ATOM   1610  N N   . GLY A  1 213 ? -34.182 1.079   84.232  1.00 19.35  ? 218 GLY A N   1 
ATOM   1611  C CA  . GLY A  1 213 ? -34.548 2.472   83.988  1.00 20.08  ? 218 GLY A CA  1 
ATOM   1612  C C   . GLY A  1 213 ? -35.697 2.615   83.006  1.00 20.70  ? 218 GLY A C   1 
ATOM   1613  O O   . GLY A  1 213 ? -36.603 3.432   83.203  1.00 20.55  ? 218 GLY A O   1 
ATOM   1614  N N   . ALA A  1 214 ? -35.655 1.815   81.944  1.00 21.15  ? 219 ALA A N   1 
ATOM   1615  C CA  . ALA A  1 214 ? -36.709 1.802   80.937  1.00 21.49  ? 219 ALA A CA  1 
ATOM   1616  C C   . ALA A  1 214 ? -36.906 0.393   80.384  1.00 21.49  ? 219 ALA A C   1 
ATOM   1617  O O   . ALA A  1 214 ? -36.003 -0.157  79.746  1.00 21.16  ? 219 ALA A O   1 
ATOM   1618  C CB  . ALA A  1 214 ? -36.383 2.782   79.814  1.00 21.41  ? 219 ALA A CB  1 
ATOM   1619  N N   . ARG A  1 215 ? -38.085 -0.177  80.647  1.00 21.41  ? 220 ARG A N   1 
ATOM   1620  C CA  . ARG A  1 215 ? -38.489 -1.503  80.154  1.00 21.81  ? 220 ARG A CA  1 
ATOM   1621  C C   . ARG A  1 215 ? -37.910 -1.884  78.793  1.00 21.66  ? 220 ARG A C   1 
ATOM   1622  O O   . ARG A  1 215 ? -38.165 -1.206  77.795  1.00 21.98  ? 220 ARG A O   1 
ATOM   1623  C CB  . ARG A  1 215 ? -40.015 -1.589  80.073  1.00 22.12  ? 220 ARG A CB  1 
ATOM   1624  C CG  . ARG A  1 215 ? -40.654 -2.343  81.209  1.00 24.33  ? 220 ARG A CG  1 
ATOM   1625  C CD  . ARG A  1 215 ? -42.157 -2.480  81.014  1.00 26.29  ? 220 ARG A CD  1 
ATOM   1626  N NE  . ARG A  1 215 ? -42.874 -1.290  81.471  1.00 28.07  ? 220 ARG A NE  1 
ATOM   1627  C CZ  . ARG A  1 215 ? -43.188 -1.041  82.740  1.00 28.33  ? 220 ARG A CZ  1 
ATOM   1628  N NH1 . ARG A  1 215 ? -42.850 -1.892  83.700  1.00 29.02  ? 220 ARG A NH1 1 
ATOM   1629  N NH2 . ARG A  1 215 ? -43.841 0.069   83.054  1.00 30.64  ? 220 ARG A NH2 1 
ATOM   1630  N N   . ARG A  1 216 ? -37.137 -2.969  78.765  1.00 21.26  ? 229 ARG A N   1 
ATOM   1631  C CA  . ARG A  1 216 ? -36.573 -3.504  77.521  1.00 21.00  ? 229 ARG A CA  1 
ATOM   1632  C C   . ARG A  1 216 ? -35.974 -4.903  77.703  1.00 20.18  ? 229 ARG A C   1 
ATOM   1633  O O   . ARG A  1 216 ? -35.532 -5.265  78.795  1.00 20.50  ? 229 ARG A O   1 
ATOM   1634  C CB  . ARG A  1 216 ? -35.527 -2.546  76.924  1.00 20.83  ? 229 ARG A CB  1 
ATOM   1635  C CG  . ARG A  1 216 ? -34.298 -2.320  77.796  1.00 25.17  ? 229 ARG A CG  1 
ATOM   1636  C CD  . ARG A  1 216 ? -33.478 -1.108  77.362  1.00 30.79  ? 229 ARG A CD  1 
ATOM   1637  N NE  . ARG A  1 216 ? -32.725 -1.361  76.136  1.00 35.68  ? 229 ARG A NE  1 
ATOM   1638  C CZ  . ARG A  1 216 ? -33.056 -0.895  74.934  1.00 38.95  ? 229 ARG A CZ  1 
ATOM   1639  N NH1 . ARG A  1 216 ? -34.132 -0.132  74.779  1.00 40.57  ? 229 ARG A NH1 1 
ATOM   1640  N NH2 . ARG A  1 216 ? -32.302 -1.188  73.881  1.00 40.93  ? 229 ARG A NH2 1 
ATOM   1641  N N   . ILE A  1 217 ? -35.988 -5.686  76.627  1.00 19.14  ? 230 ILE A N   1 
ATOM   1642  C CA  . ILE A  1 217 ? -35.254 -6.949  76.563  1.00 18.02  ? 230 ILE A CA  1 
ATOM   1643  C C   . ILE A  1 217 ? -34.319 -6.883  75.360  1.00 18.41  ? 230 ILE A C   1 
ATOM   1644  O O   . ILE A  1 217 ? -34.768 -6.806  74.214  1.00 17.78  ? 230 ILE A O   1 
ATOM   1645  C CB  . ILE A  1 217 ? -36.190 -8.190  76.461  1.00 17.56  ? 230 ILE A CB  1 
ATOM   1646  C CG1 . ILE A  1 217 ? -37.014 -8.357  77.742  1.00 16.17  ? 230 ILE A CG1 1 
ATOM   1647  C CG2 . ILE A  1 217 ? -35.379 -9.452  76.216  1.00 13.59  ? 230 ILE A CG2 1 
ATOM   1648  C CD1 . ILE A  1 217 ? -38.124 -9.387  77.652  1.00 15.17  ? 230 ILE A CD1 1 
ATOM   1649  N N   . ASP A  1 218 ? -33.018 -6.889  75.636  1.00 19.01  ? 231 ASP A N   1 
ATOM   1650  C CA  . ASP A  1 218 ? -32.004 -6.826  74.590  1.00 19.25  ? 231 ASP A CA  1 
ATOM   1651  C C   . ASP A  1 218 ? -31.474 -8.214  74.278  1.00 18.81  ? 231 ASP A C   1 
ATOM   1652  O O   . ASP A  1 218 ? -31.174 -8.988  75.185  1.00 19.98  ? 231 ASP A O   1 
ATOM   1653  C CB  . ASP A  1 218 ? -30.861 -5.885  74.990  1.00 19.05  ? 231 ASP A CB  1 
ATOM   1654  C CG  . ASP A  1 218 ? -31.194 -4.415  74.738  1.00 21.66  ? 231 ASP A CG  1 
ATOM   1655  O OD1 . ASP A  1 218 ? -32.065 -4.131  73.885  1.00 21.71  ? 231 ASP A OD1 1 
ATOM   1656  O OD2 . ASP A  1 218 ? -30.574 -3.541  75.387  1.00 22.54  ? 231 ASP A OD2 1 
ATOM   1657  N N   . PHE A  1 219 ? -31.363 -8.525  72.993  1.00 17.72  ? 232 PHE A N   1 
ATOM   1658  C CA  . PHE A  1 219 ? -30.944 -9.857  72.577  1.00 17.43  ? 232 PHE A CA  1 
ATOM   1659  C C   . PHE A  1 219 ? -29.492 -9.941  72.118  1.00 17.19  ? 232 PHE A C   1 
ATOM   1660  O O   . PHE A  1 219 ? -28.978 -9.031  71.460  1.00 17.50  ? 232 PHE A O   1 
ATOM   1661  C CB  . PHE A  1 219 ? -31.897 -10.409 71.516  1.00 17.10  ? 232 PHE A CB  1 
ATOM   1662  C CG  . PHE A  1 219 ? -33.267 -10.698 72.046  1.00 16.15  ? 232 PHE A CG  1 
ATOM   1663  C CD1 . PHE A  1 219 ? -34.310 -9.804  71.835  1.00 14.62  ? 232 PHE A CD1 1 
ATOM   1664  C CD2 . PHE A  1 219 ? -33.509 -11.854 72.786  1.00 13.54  ? 232 PHE A CD2 1 
ATOM   1665  C CE1 . PHE A  1 219 ? -35.576 -10.064 72.337  1.00 13.05  ? 232 PHE A CE1 1 
ATOM   1666  C CE2 . PHE A  1 219 ? -34.767 -12.122 73.293  1.00 11.82  ? 232 PHE A CE2 1 
ATOM   1667  C CZ  . PHE A  1 219 ? -35.805 -11.228 73.065  1.00 14.96  ? 232 PHE A CZ  1 
ATOM   1668  N N   . HIS A  1 220 ? -28.843 -11.041 72.490  1.00 16.25  ? 233 HIS A N   1 
ATOM   1669  C CA  . HIS A  1 220 ? -27.462 -11.314 72.099  1.00 16.47  ? 233 HIS A CA  1 
ATOM   1670  C C   . HIS A  1 220 ? -27.350 -12.708 71.468  1.00 16.97  ? 233 HIS A C   1 
ATOM   1671  O O   . HIS A  1 220 ? -28.232 -13.553 71.652  1.00 17.72  ? 233 HIS A O   1 
ATOM   1672  C CB  . HIS A  1 220 ? -26.527 -11.193 73.301  1.00 15.72  ? 233 HIS A CB  1 
ATOM   1673  C CG  . HIS A  1 220 ? -26.755 -9.965  74.126  1.00 15.39  ? 233 HIS A CG  1 
ATOM   1674  N ND1 . HIS A  1 220 ? -26.226 -8.737  73.796  1.00 16.37  ? 233 HIS A ND1 1 
ATOM   1675  C CD2 . HIS A  1 220 ? -27.453 -9.779  75.271  1.00 16.41  ? 233 HIS A CD2 1 
ATOM   1676  C CE1 . HIS A  1 220 ? -26.588 -7.846  74.702  1.00 15.80  ? 233 HIS A CE1 1 
ATOM   1677  N NE2 . HIS A  1 220 ? -27.333 -8.453  75.608  1.00 16.39  ? 233 HIS A NE2 1 
ATOM   1678  N N   . TRP A  1 221 ? -26.267 -12.945 70.730  1.00 16.72  ? 234 TRP A N   1 
ATOM   1679  C CA  . TRP A  1 221 ? -26.134 -14.172 69.948  1.00 16.89  ? 234 TRP A CA  1 
ATOM   1680  C C   . TRP A  1 221 ? -24.693 -14.602 69.688  1.00 17.01  ? 234 TRP A C   1 
ATOM   1681  O O   . TRP A  1 221 ? -23.769 -13.783 69.719  1.00 18.13  ? 234 TRP A O   1 
ATOM   1682  C CB  . TRP A  1 221 ? -26.867 -14.026 68.614  1.00 16.57  ? 234 TRP A CB  1 
ATOM   1683  C CG  . TRP A  1 221 ? -26.324 -12.931 67.754  1.00 17.63  ? 234 TRP A CG  1 
ATOM   1684  C CD1 . TRP A  1 221 ? -26.656 -11.608 67.805  1.00 19.78  ? 234 TRP A CD1 1 
ATOM   1685  C CD2 . TRP A  1 221 ? -25.350 -13.061 66.712  1.00 19.01  ? 234 TRP A CD2 1 
ATOM   1686  N NE1 . TRP A  1 221 ? -25.952 -10.904 66.855  1.00 21.06  ? 234 TRP A NE1 1 
ATOM   1687  C CE2 . TRP A  1 221 ? -25.142 -11.772 66.171  1.00 20.32  ? 234 TRP A CE2 1 
ATOM   1688  C CE3 . TRP A  1 221 ? -24.632 -14.141 66.181  1.00 19.48  ? 234 TRP A CE3 1 
ATOM   1689  C CZ2 . TRP A  1 221 ? -24.246 -11.534 65.126  1.00 19.99  ? 234 TRP A CZ2 1 
ATOM   1690  C CZ3 . TRP A  1 221 ? -23.743 -13.904 65.142  1.00 17.90  ? 234 TRP A CZ3 1 
ATOM   1691  C CH2 . TRP A  1 221 ? -23.558 -12.611 64.626  1.00 19.18  ? 234 TRP A CH2 1 
ATOM   1692  N N   . LEU A  1 222 ? -24.525 -15.897 69.430  1.00 16.24  ? 235 LEU A N   1 
ATOM   1693  C CA  . LEU A  1 222 ? -23.253 -16.481 69.010  1.00 15.64  ? 235 LEU A CA  1 
ATOM   1694  C C   . LEU A  1 222 ? -23.521 -17.655 68.067  1.00 15.66  ? 235 LEU A C   1 
ATOM   1695  O O   . LEU A  1 222 ? -24.635 -18.186 68.026  1.00 16.04  ? 235 LEU A O   1 
ATOM   1696  C CB  . LEU A  1 222 ? -22.426 -16.947 70.224  1.00 15.30  ? 235 LEU A CB  1 
ATOM   1697  C CG  . LEU A  1 222 ? -22.982 -17.983 71.218  1.00 14.27  ? 235 LEU A CG  1 
ATOM   1698  C CD1 . LEU A  1 222 ? -22.970 -19.392 70.641  1.00 16.25  ? 235 LEU A CD1 1 
ATOM   1699  C CD2 . LEU A  1 222 ? -22.186 -17.969 72.509  1.00 8.49   ? 235 LEU A CD2 1 
ATOM   1700  N N   . LEU A  1 223 ? -22.502 -18.056 67.312  1.00 15.03  ? 236 LEU A N   1 
ATOM   1701  C CA  . LEU A  1 223 ? -22.575 -19.292 66.542  1.00 13.76  ? 236 LEU A CA  1 
ATOM   1702  C C   . LEU A  1 223 ? -21.826 -20.391 67.288  1.00 13.78  ? 236 LEU A C   1 
ATOM   1703  O O   . LEU A  1 223 ? -20.623 -20.277 67.545  1.00 13.76  ? 236 LEU A O   1 
ATOM   1704  C CB  . LEU A  1 223 ? -22.025 -19.100 65.128  1.00 12.67  ? 236 LEU A CB  1 
ATOM   1705  C CG  . LEU A  1 223 ? -22.835 -18.196 64.192  1.00 12.15  ? 236 LEU A CG  1 
ATOM   1706  C CD1 . LEU A  1 223 ? -21.955 -17.650 63.068  1.00 9.58   ? 236 LEU A CD1 1 
ATOM   1707  C CD2 . LEU A  1 223 ? -24.076 -18.905 63.629  1.00 8.47   ? 236 LEU A CD2 1 
ATOM   1708  N N   . LEU A  1 224 ? -22.554 -21.438 67.661  1.00 13.48  ? 237 LEU A N   1 
ATOM   1709  C CA  . LEU A  1 224 ? -21.971 -22.548 68.398  1.00 13.68  ? 237 LEU A CA  1 
ATOM   1710  C C   . LEU A  1 224 ? -21.522 -23.636 67.435  1.00 14.93  ? 237 LEU A C   1 
ATOM   1711  O O   . LEU A  1 224 ? -22.339 -24.206 66.716  1.00 15.61  ? 237 LEU A O   1 
ATOM   1712  C CB  . LEU A  1 224 ? -22.970 -23.106 69.417  1.00 12.66  ? 237 LEU A CB  1 
ATOM   1713  C CG  . LEU A  1 224 ? -22.480 -24.178 70.392  1.00 9.42   ? 237 LEU A CG  1 
ATOM   1714  C CD1 . LEU A  1 224 ? -21.284 -23.684 71.198  1.00 7.02   ? 237 LEU A CD1 1 
ATOM   1715  C CD2 . LEU A  1 224 ? -23.606 -24.606 71.318  1.00 6.17   ? 237 LEU A CD2 1 
ATOM   1716  N N   . ASP A  1 225 ? -20.220 -23.909 67.420  1.00 15.86  ? 238 ASP A N   1 
ATOM   1717  C CA  . ASP A  1 225 ? -19.659 -24.965 66.580  1.00 16.96  ? 238 ASP A CA  1 
ATOM   1718  C C   . ASP A  1 225 ? -20.225 -26.343 66.936  1.00 17.17  ? 238 ASP A C   1 
ATOM   1719  O O   . ASP A  1 225 ? -20.583 -26.583 68.093  1.00 17.71  ? 238 ASP A O   1 
ATOM   1720  C CB  . ASP A  1 225 ? -18.129 -24.979 66.687  1.00 17.64  ? 238 ASP A CB  1 
ATOM   1721  C CG  . ASP A  1 225 ? -17.468 -23.890 65.855  1.00 19.80  ? 238 ASP A CG  1 
ATOM   1722  O OD1 . ASP A  1 225 ? -18.091 -23.392 64.886  1.00 20.62  ? 238 ASP A OD1 1 
ATOM   1723  O OD2 . ASP A  1 225 ? -16.312 -23.537 66.171  1.00 21.53  ? 238 ASP A OD2 1 
ATOM   1724  N N   . PRO A  1 226 ? -20.324 -27.247 65.939  1.00 17.22  ? 239 PRO A N   1 
ATOM   1725  C CA  . PRO A  1 226 ? -20.724 -28.627 66.201  1.00 17.28  ? 239 PRO A CA  1 
ATOM   1726  C C   . PRO A  1 226 ? -19.891 -29.256 67.314  1.00 17.63  ? 239 PRO A C   1 
ATOM   1727  O O   . PRO A  1 226 ? -18.661 -29.127 67.322  1.00 17.35  ? 239 PRO A O   1 
ATOM   1728  C CB  . PRO A  1 226 ? -20.434 -29.330 64.872  1.00 17.21  ? 239 PRO A CB  1 
ATOM   1729  C CG  . PRO A  1 226 ? -20.610 -28.281 63.854  1.00 16.56  ? 239 PRO A CG  1 
ATOM   1730  C CD  . PRO A  1 226 ? -20.166 -26.992 64.493  1.00 17.38  ? 239 PRO A CD  1 
ATOM   1731  N N   . ASN A  1 227 ? -20.574 -29.904 68.254  1.00 17.98  ? 240 ASN A N   1 
ATOM   1732  C CA  . ASN A  1 227 ? -19.940 -30.618 69.370  1.00 18.58  ? 240 ASN A CA  1 
ATOM   1733  C C   . ASN A  1 227 ? -19.442 -29.717 70.511  1.00 18.87  ? 240 ASN A C   1 
ATOM   1734  O O   . ASN A  1 227 ? -19.097 -30.203 71.591  1.00 19.19  ? 240 ASN A O   1 
ATOM   1735  C CB  . ASN A  1 227 ? -18.831 -31.557 68.863  1.00 18.49  ? 240 ASN A CB  1 
ATOM   1736  C CG  . ASN A  1 227 ? -18.548 -32.704 69.814  1.00 18.48  ? 240 ASN A CG  1 
ATOM   1737  O OD1 . ASN A  1 227 ? -19.353 -33.021 70.691  1.00 17.04  ? 240 ASN A OD1 1 
ATOM   1738  N ND2 . ASN A  1 227 ? -17.395 -33.340 69.638  1.00 21.17  ? 240 ASN A ND2 1 
ATOM   1739  N N   . ASP A  1 228 ? -19.422 -28.407 70.272  1.00 19.10  ? 241 ASP A N   1 
ATOM   1740  C CA  . ASP A  1 228 ? -19.071 -27.430 71.302  1.00 19.25  ? 241 ASP A CA  1 
ATOM   1741  C C   . ASP A  1 228 ? -20.280 -27.143 72.195  1.00 18.96  ? 241 ASP A C   1 
ATOM   1742  O O   . ASP A  1 228 ? -21.427 -27.309 71.773  1.00 19.20  ? 241 ASP A O   1 
ATOM   1743  C CB  . ASP A  1 228 ? -18.550 -26.140 70.652  1.00 19.77  ? 241 ASP A CB  1 
ATOM   1744  C CG  . ASP A  1 228 ? -17.976 -25.147 71.661  1.00 20.02  ? 241 ASP A CG  1 
ATOM   1745  O OD1 . ASP A  1 228 ? -17.711 -25.521 72.825  1.00 18.45  ? 241 ASP A OD1 1 
ATOM   1746  O OD2 . ASP A  1 228 ? -17.785 -23.975 71.277  1.00 21.19  ? 241 ASP A OD2 1 
ATOM   1747  N N   . THR A  1 229 ? -20.011 -26.713 73.426  1.00 18.50  ? 242 THR A N   1 
ATOM   1748  C CA  . THR A  1 229 ? -21.053 -26.452 74.418  1.00 17.82  ? 242 THR A CA  1 
ATOM   1749  C C   . THR A  1 229 ? -21.156 -24.966 74.768  1.00 17.39  ? 242 THR A C   1 
ATOM   1750  O O   . THR A  1 229 ? -20.142 -24.278 74.906  1.00 18.26  ? 242 THR A O   1 
ATOM   1751  C CB  . THR A  1 229 ? -20.805 -27.276 75.703  1.00 17.57  ? 242 THR A CB  1 
ATOM   1752  O OG1 . THR A  1 229 ? -20.679 -28.662 75.360  1.00 18.61  ? 242 THR A OG1 1 
ATOM   1753  C CG2 . THR A  1 229 ? -21.950 -27.114 76.699  1.00 16.79  ? 242 THR A CG2 1 
ATOM   1754  N N   . VAL A  1 230 ? -22.388 -24.479 74.894  1.00 16.06  ? 243 VAL A N   1 
ATOM   1755  C CA  . VAL A  1 230 ? -22.647 -23.133 75.399  1.00 15.41  ? 243 VAL A CA  1 
ATOM   1756  C C   . VAL A  1 230 ? -23.130 -23.227 76.849  1.00 15.44  ? 243 VAL A C   1 
ATOM   1757  O O   . VAL A  1 230 ? -23.973 -24.067 77.173  1.00 15.58  ? 243 VAL A O   1 
ATOM   1758  C CB  . VAL A  1 230 ? -23.647 -22.343 74.486  1.00 15.52  ? 243 VAL A CB  1 
ATOM   1759  C CG1 . VAL A  1 230 ? -25.052 -22.967 74.492  1.00 14.16  ? 243 VAL A CG1 1 
ATOM   1760  C CG2 . VAL A  1 230 ? -23.696 -20.870 74.870  1.00 14.08  ? 243 VAL A CG2 1 
ATOM   1761  N N   . THR A  1 231 ? -22.579 -22.380 77.718  1.00 15.36  ? 244 THR A N   1 
ATOM   1762  C CA  . THR A  1 231 ? -22.910 -22.411 79.143  1.00 15.61  ? 244 THR A CA  1 
ATOM   1763  C C   . THR A  1 231 ? -23.465 -21.074 79.638  1.00 16.21  ? 244 THR A C   1 
ATOM   1764  O O   . THR A  1 231 ? -22.809 -20.033 79.530  1.00 16.20  ? 244 THR A O   1 
ATOM   1765  C CB  . THR A  1 231 ? -21.693 -22.849 80.002  1.00 15.93  ? 244 THR A CB  1 
ATOM   1766  O OG1 . THR A  1 231 ? -21.206 -24.112 79.535  1.00 13.83  ? 244 THR A OG1 1 
ATOM   1767  C CG2 . THR A  1 231 ? -22.073 -22.980 81.475  1.00 14.46  ? 244 THR A CG2 1 
ATOM   1768  N N   . PHE A  1 232 ? -24.684 -21.126 80.173  1.00 16.80  ? 245 PHE A N   1 
ATOM   1769  C CA  . PHE A  1 232 ? -25.360 -19.962 80.742  1.00 16.48  ? 245 PHE A CA  1 
ATOM   1770  C C   . PHE A  1 232 ? -25.358 -20.032 82.262  1.00 16.73  ? 245 PHE A C   1 
ATOM   1771  O O   . PHE A  1 232 ? -25.869 -20.993 82.843  1.00 17.12  ? 245 PHE A O   1 
ATOM   1772  C CB  . PHE A  1 232 ? -26.813 -19.897 80.266  1.00 16.09  ? 245 PHE A CB  1 
ATOM   1773  C CG  . PHE A  1 232 ? -26.974 -19.795 78.776  1.00 17.67  ? 245 PHE A CG  1 
ATOM   1774  C CD1 . PHE A  1 232 ? -27.367 -20.906 78.031  1.00 16.73  ? 245 PHE A CD1 1 
ATOM   1775  C CD2 . PHE A  1 232 ? -26.756 -18.584 78.117  1.00 16.95  ? 245 PHE A CD2 1 
ATOM   1776  C CE1 . PHE A  1 232 ? -27.531 -20.816 76.654  1.00 14.82  ? 245 PHE A CE1 1 
ATOM   1777  C CE2 . PHE A  1 232 ? -26.914 -18.484 76.740  1.00 14.87  ? 245 PHE A CE2 1 
ATOM   1778  C CZ  . PHE A  1 232 ? -27.302 -19.603 76.009  1.00 15.95  ? 245 PHE A CZ  1 
ATOM   1779  N N   . THR A  1 233 ? -24.781 -19.018 82.901  1.00 16.95  ? 246 THR A N   1 
ATOM   1780  C CA  . THR A  1 233 ? -24.869 -18.863 84.357  1.00 17.46  ? 246 THR A CA  1 
ATOM   1781  C C   . THR A  1 233 ? -25.560 -17.540 84.664  1.00 17.28  ? 246 THR A C   1 
ATOM   1782  O O   . THR A  1 233 ? -25.213 -16.506 84.087  1.00 17.67  ? 246 THR A O   1 
ATOM   1783  C CB  . THR A  1 233 ? -23.484 -18.900 85.042  1.00 17.64  ? 246 THR A CB  1 
ATOM   1784  O OG1 . THR A  1 233 ? -22.650 -17.871 84.495  1.00 19.81  ? 246 THR A OG1 1 
ATOM   1785  C CG2 . THR A  1 233 ? -22.809 -20.259 84.844  1.00 16.57  ? 246 THR A CG2 1 
ATOM   1786  N N   . PHE A  1 234 ? -26.539 -17.572 85.565  1.00 17.03  ? 247 PHE A N   1 
ATOM   1787  C CA  . PHE A  1 234 ? -27.389 -16.406 85.810  1.00 17.39  ? 247 PHE A CA  1 
ATOM   1788  C C   . PHE A  1 234 ? -28.150 -16.490 87.129  1.00 18.09  ? 247 PHE A C   1 
ATOM   1789  O O   . PHE A  1 234 ? -28.571 -17.572 87.550  1.00 18.53  ? 247 PHE A O   1 
ATOM   1790  C CB  . PHE A  1 234 ? -28.385 -16.216 84.654  1.00 16.93  ? 247 PHE A CB  1 
ATOM   1791  C CG  . PHE A  1 234 ? -29.267 -17.409 84.415  1.00 16.14  ? 247 PHE A CG  1 
ATOM   1792  C CD1 . PHE A  1 234 ? -30.504 -17.512 85.045  1.00 14.40  ? 247 PHE A CD1 1 
ATOM   1793  C CD2 . PHE A  1 234 ? -28.856 -18.437 83.570  1.00 14.26  ? 247 PHE A CD2 1 
ATOM   1794  C CE1 . PHE A  1 234 ? -31.317 -18.618 84.835  1.00 16.02  ? 247 PHE A CE1 1 
ATOM   1795  C CE2 . PHE A  1 234 ? -29.660 -19.547 83.354  1.00 12.63  ? 247 PHE A CE2 1 
ATOM   1796  C CZ  . PHE A  1 234 ? -30.896 -19.638 83.985  1.00 13.96  ? 247 PHE A CZ  1 
ATOM   1797  N N   . ASN A  1 235 ? -28.335 -15.334 87.762  1.00 18.28  ? 248 ASN A N   1 
ATOM   1798  C CA  . ASN A  1 235 ? -29.106 -15.236 88.994  1.00 18.41  ? 248 ASN A CA  1 
ATOM   1799  C C   . ASN A  1 235 ? -30.352 -14.365 88.827  1.00 18.38  ? 248 ASN A C   1 
ATOM   1800  O O   . ASN A  1 235 ? -30.939 -13.913 89.812  1.00 19.05  ? 248 ASN A O   1 
ATOM   1801  C CB  . ASN A  1 235 ? -28.225 -14.708 90.133  1.00 18.69  ? 248 ASN A CB  1 
ATOM   1802  C CG  . ASN A  1 235 ? -27.763 -13.274 89.908  1.00 19.78  ? 248 ASN A CG  1 
ATOM   1803  O OD1 . ASN A  1 235 ? -27.535 -12.847 88.772  1.00 18.95  ? 248 ASN A OD1 1 
ATOM   1804  N ND2 . ASN A  1 235 ? -27.620 -12.524 90.997  1.00 17.14  ? 248 ASN A ND2 1 
ATOM   1805  N N   . GLY A  1 236 ? -30.751 -14.136 87.578  1.00 18.06  ? 249 GLY A N   1 
ATOM   1806  C CA  . GLY A  1 236 ? -31.945 -13.344 87.273  1.00 17.70  ? 249 GLY A CA  1 
ATOM   1807  C C   . GLY A  1 236 ? -31.798 -12.465 86.044  1.00 17.17  ? 249 GLY A C   1 
ATOM   1808  O O   . GLY A  1 236 ? -30.728 -12.417 85.429  1.00 17.06  ? 249 GLY A O   1 
ATOM   1809  N N   . ALA A  1 237 ? -32.883 -11.771 85.693  1.00 16.43  ? 250 ALA A N   1 
ATOM   1810  C CA  . ALA A  1 237 ? -32.939 -10.883 84.517  1.00 16.35  ? 250 ALA A CA  1 
ATOM   1811  C C   . ALA A  1 237 ? -32.574 -11.583 83.207  1.00 16.24  ? 250 ALA A C   1 
ATOM   1812  O O   . ALA A  1 237 ? -32.192 -10.934 82.229  1.00 15.96  ? 250 ALA A O   1 
ATOM   1813  C CB  . ALA A  1 237 ? -32.071 -9.635  84.725  1.00 15.88  ? 250 ALA A CB  1 
ATOM   1814  N N   . PHE A  1 238 ? -32.713 -12.906 83.196  1.00 16.48  ? 251 PHE A N   1 
ATOM   1815  C CA  . PHE A  1 238 ? -32.298 -13.720 82.063  1.00 16.84  ? 251 PHE A CA  1 
ATOM   1816  C C   . PHE A  1 238 ? -33.483 -14.192 81.229  1.00 16.55  ? 251 PHE A C   1 
ATOM   1817  O O   . PHE A  1 238 ? -34.434 -14.783 81.751  1.00 16.89  ? 251 PHE A O   1 
ATOM   1818  C CB  . PHE A  1 238 ? -31.473 -14.919 82.548  1.00 16.96  ? 251 PHE A CB  1 
ATOM   1819  C CG  . PHE A  1 238 ? -30.851 -15.720 81.438  1.00 18.82  ? 251 PHE A CG  1 
ATOM   1820  C CD1 . PHE A  1 238 ? -29.942 -15.135 80.560  1.00 20.41  ? 251 PHE A CD1 1 
ATOM   1821  C CD2 . PHE A  1 238 ? -31.167 -17.062 81.273  1.00 21.22  ? 251 PHE A CD2 1 
ATOM   1822  C CE1 . PHE A  1 238 ? -29.364 -15.873 79.533  1.00 16.37  ? 251 PHE A CE1 1 
ATOM   1823  C CE2 . PHE A  1 238 ? -30.589 -17.809 80.248  1.00 21.30  ? 251 PHE A CE2 1 
ATOM   1824  C CZ  . PHE A  1 238 ? -29.689 -17.211 79.378  1.00 19.03  ? 251 PHE A CZ  1 
ATOM   1825  N N   . ILE A  1 239 ? -33.417 -13.920 79.929  1.00 15.89  ? 252 ILE A N   1 
ATOM   1826  C CA  . ILE A  1 239 ? -34.382 -14.452 78.978  1.00 15.27  ? 252 ILE A CA  1 
ATOM   1827  C C   . ILE A  1 239 ? -33.735 -15.640 78.281  1.00 15.85  ? 252 ILE A C   1 
ATOM   1828  O O   . ILE A  1 239 ? -32.796 -15.480 77.499  1.00 16.42  ? 252 ILE A O   1 
ATOM   1829  C CB  . ILE A  1 239 ? -34.837 -13.385 77.954  1.00 14.36  ? 252 ILE A CB  1 
ATOM   1830  C CG1 . ILE A  1 239 ? -35.371 -12.134 78.667  1.00 12.27  ? 252 ILE A CG1 1 
ATOM   1831  C CG2 . ILE A  1 239 ? -35.863 -13.962 76.979  1.00 14.45  ? 252 ILE A CG2 1 
ATOM   1832  C CD1 . ILE A  1 239 ? -36.497 -12.387 79.664  1.00 9.78   ? 252 ILE A CD1 1 
ATOM   1833  N N   . ALA A  1 240 ? -34.244 -16.830 78.582  1.00 16.27  ? 253 ALA A N   1 
ATOM   1834  C CA  . ALA A  1 240 ? -33.617 -18.078 78.152  1.00 16.62  ? 253 ALA A CA  1 
ATOM   1835  C C   . ALA A  1 240 ? -34.111 -18.546 76.789  1.00 16.82  ? 253 ALA A C   1 
ATOM   1836  O O   . ALA A  1 240 ? -35.277 -18.341 76.446  1.00 16.83  ? 253 ALA A O   1 
ATOM   1837  C CB  . ALA A  1 240 ? -33.841 -19.165 79.192  1.00 15.93  ? 253 ALA A CB  1 
ATOM   1838  N N   . PRO A  1 241 ? -33.221 -19.178 76.005  1.00 16.60  ? 254 PRO A N   1 
ATOM   1839  C CA  . PRO A  1 241 ? -33.678 -19.817 74.783  1.00 16.94  ? 254 PRO A CA  1 
ATOM   1840  C C   . PRO A  1 241 ? -34.381 -21.140 75.081  1.00 17.53  ? 254 PRO A C   1 
ATOM   1841  O O   . PRO A  1 241 ? -33.991 -21.860 76.004  1.00 17.86  ? 254 PRO A O   1 
ATOM   1842  C CB  . PRO A  1 241 ? -32.379 -20.069 74.016  1.00 16.61  ? 254 PRO A CB  1 
ATOM   1843  C CG  . PRO A  1 241 ? -31.341 -20.175 75.057  1.00 15.64  ? 254 PRO A CG  1 
ATOM   1844  C CD  . PRO A  1 241 ? -31.758 -19.255 76.158  1.00 16.39  ? 254 PRO A CD  1 
ATOM   1845  N N   . ASP A  1 242 ? -35.424 -21.438 74.314  1.00 17.47  ? 255 ASP A N   1 
ATOM   1846  C CA  . ASP A  1 242 ? -36.046 -22.749 74.352  1.00 17.70  ? 255 ASP A CA  1 
ATOM   1847  C C   . ASP A  1 242 ? -35.597 -23.541 73.127  1.00 18.47  ? 255 ASP A C   1 
ATOM   1848  O O   . ASP A  1 242 ? -35.186 -24.699 73.236  1.00 19.64  ? 255 ASP A O   1 
ATOM   1849  C CB  . ASP A  1 242 ? -37.567 -22.627 74.384  1.00 17.52  ? 255 ASP A CB  1 
ATOM   1850  C CG  . ASP A  1 242 ? -38.249 -23.967 74.537  1.00 18.91  ? 255 ASP A CG  1 
ATOM   1851  O OD1 . ASP A  1 242 ? -39.098 -24.301 73.683  1.00 18.85  ? 255 ASP A OD1 1 
ATOM   1852  O OD2 . ASP A  1 242 ? -37.923 -24.690 75.504  1.00 19.36  ? 255 ASP A OD2 1 
ATOM   1853  N N   . ARG A  1 243 ? -35.680 -22.899 71.965  1.00 18.22  ? 256 ARG A N   1 
ATOM   1854  C CA  . ARG A  1 243 ? -35.221 -23.476 70.713  1.00 17.27  ? 256 ARG A CA  1 
ATOM   1855  C C   . ARG A  1 243 ? -34.015 -22.696 70.201  1.00 17.10  ? 256 ARG A C   1 
ATOM   1856  O O   . ARG A  1 243 ? -33.826 -21.521 70.541  1.00 17.24  ? 256 ARG A O   1 
ATOM   1857  C CB  . ARG A  1 243 ? -36.337 -23.434 69.665  1.00 17.22  ? 256 ARG A CB  1 
ATOM   1858  C CG  . ARG A  1 243 ? -37.312 -24.611 69.671  1.00 16.19  ? 256 ARG A CG  1 
ATOM   1859  C CD  . ARG A  1 243 ? -38.655 -24.137 69.136  1.00 17.36  ? 256 ARG A CD  1 
ATOM   1860  N NE  . ARG A  1 243 ? -39.244 -24.998 68.113  1.00 18.27  ? 256 ARG A NE  1 
ATOM   1861  C CZ  . ARG A  1 243 ? -39.991 -24.555 67.100  1.00 19.65  ? 256 ARG A CZ  1 
ATOM   1862  N NH1 . ARG A  1 243 ? -40.220 -23.255 66.947  1.00 18.09  ? 256 ARG A NH1 1 
ATOM   1863  N NH2 . ARG A  1 243 ? -40.497 -25.410 66.219  1.00 21.14  ? 256 ARG A NH2 1 
ATOM   1864  N N   . THR A  1 244 ? -33.197 -23.371 69.398  1.00 16.30  ? 257 THR A N   1 
ATOM   1865  C CA  . THR A  1 244 ? -32.134 -22.732 68.629  1.00 15.01  ? 257 THR A CA  1 
ATOM   1866  C C   . THR A  1 244 ? -32.379 -22.991 67.139  1.00 15.05  ? 257 THR A C   1 
ATOM   1867  O O   . THR A  1 244 ? -33.258 -23.779 66.782  1.00 14.38  ? 257 THR A O   1 
ATOM   1868  C CB  . THR A  1 244 ? -30.733 -23.225 69.051  1.00 14.74  ? 257 THR A CB  1 
ATOM   1869  O OG1 . THR A  1 244 ? -29.735 -22.554 68.270  1.00 12.90  ? 257 THR A OG1 1 
ATOM   1870  C CG2 . THR A  1 244 ? -30.599 -24.740 68.860  1.00 13.11  ? 257 THR A CG2 1 
ATOM   1871  N N   . SER A  1 245 ? -31.602 -22.336 66.279  1.00 15.00  ? 258 SER A N   1 
ATOM   1872  C CA  . SER A  1 245 ? -31.825 -22.409 64.839  1.00 15.17  ? 258 SER A CA  1 
ATOM   1873  C C   . SER A  1 245 ? -30.679 -23.072 64.090  1.00 16.25  ? 258 SER A C   1 
ATOM   1874  O O   . SER A  1 245 ? -29.519 -22.966 64.486  1.00 17.55  ? 258 SER A O   1 
ATOM   1875  C CB  . SER A  1 245 ? -32.080 -21.014 64.269  1.00 15.09  ? 258 SER A CB  1 
ATOM   1876  O OG  . SER A  1 245 ? -33.167 -20.383 64.925  1.00 13.62  ? 258 SER A OG  1 
ATOM   1877  N N   . PHE A  1 246 ? -31.020 -23.758 63.006  1.00 16.73  ? 259 PHE A N   1 
ATOM   1878  C CA  . PHE A  1 246 ? -30.037 -24.337 62.105  1.00 17.38  ? 259 PHE A CA  1 
ATOM   1879  C C   . PHE A  1 246 ? -30.376 -23.947 60.672  1.00 18.85  ? 259 PHE A C   1 
ATOM   1880  O O   . PHE A  1 246 ? -31.532 -24.044 60.255  1.00 19.11  ? 259 PHE A O   1 
ATOM   1881  C CB  . PHE A  1 246 ? -30.000 -25.859 62.246  1.00 16.71  ? 259 PHE A CB  1 
ATOM   1882  C CG  . PHE A  1 246 ? -29.429 -26.335 63.550  1.00 16.27  ? 259 PHE A CG  1 
ATOM   1883  C CD1 . PHE A  1 246 ? -30.266 -26.759 64.577  1.00 15.44  ? 259 PHE A CD1 1 
ATOM   1884  C CD2 . PHE A  1 246 ? -28.050 -26.367 63.753  1.00 14.78  ? 259 PHE A CD2 1 
ATOM   1885  C CE1 . PHE A  1 246 ? -29.740 -27.208 65.789  1.00 14.84  ? 259 PHE A CE1 1 
ATOM   1886  C CE2 . PHE A  1 246 ? -27.515 -26.813 64.958  1.00 12.21  ? 259 PHE A CE2 1 
ATOM   1887  C CZ  . PHE A  1 246 ? -28.360 -27.231 65.980  1.00 13.00  ? 259 PHE A CZ  1 
ATOM   1888  N N   . PHE A  1 247 ? -29.367 -23.504 59.926  1.00 19.84  ? 260 PHE A N   1 
ATOM   1889  C CA  . PHE A  1 247 ? -29.567 -23.029 58.560  1.00 20.45  ? 260 PHE A CA  1 
ATOM   1890  C C   . PHE A  1 247 ? -29.773 -24.185 57.593  1.00 21.35  ? 260 PHE A C   1 
ATOM   1891  O O   . PHE A  1 247 ? -29.344 -25.312 57.858  1.00 21.93  ? 260 PHE A O   1 
ATOM   1892  C CB  . PHE A  1 247 ? -28.403 -22.142 58.116  1.00 20.10  ? 260 PHE A CB  1 
ATOM   1893  C CG  . PHE A  1 247 ? -28.076 -21.041 59.086  1.00 21.90  ? 260 PHE A CG  1 
ATOM   1894  C CD1 . PHE A  1 247 ? -29.080 -20.216 59.594  1.00 20.15  ? 260 PHE A CD1 1 
ATOM   1895  C CD2 . PHE A  1 247 ? -26.763 -20.823 59.492  1.00 23.52  ? 260 PHE A CD2 1 
ATOM   1896  C CE1 . PHE A  1 247 ? -28.782 -19.200 60.490  1.00 20.29  ? 260 PHE A CE1 1 
ATOM   1897  C CE2 . PHE A  1 247 ? -26.455 -19.804 60.391  1.00 23.52  ? 260 PHE A CE2 1 
ATOM   1898  C CZ  . PHE A  1 247 ? -27.468 -18.990 60.890  1.00 21.59  ? 260 PHE A CZ  1 
ATOM   1899  N N   . ARG A  1 248 ? -30.436 -23.899 56.476  1.00 21.68  ? 261 ARG A N   1 
ATOM   1900  C CA  . ARG A  1 248 ? -30.811 -24.937 55.518  1.00 21.95  ? 261 ARG A CA  1 
ATOM   1901  C C   . ARG A  1 248 ? -29.866 -25.040 54.317  1.00 22.66  ? 261 ARG A C   1 
ATOM   1902  O O   . ARG A  1 248 ? -29.547 -26.143 53.872  1.00 23.20  ? 261 ARG A O   1 
ATOM   1903  C CB  . ARG A  1 248 ? -32.261 -24.752 55.061  1.00 21.37  ? 261 ARG A CB  1 
ATOM   1904  C CG  . ARG A  1 248 ? -33.279 -24.889 56.187  1.00 19.83  ? 261 ARG A CG  1 
ATOM   1905  C CD  . ARG A  1 248 ? -34.696 -24.660 55.691  1.00 16.18  ? 261 ARG A CD  1 
ATOM   1906  N NE  . ARG A  1 248 ? -35.663 -24.610 56.788  1.00 16.45  ? 261 ARG A NE  1 
ATOM   1907  C CZ  . ARG A  1 248 ? -36.295 -25.667 57.298  1.00 14.74  ? 261 ARG A CZ  1 
ATOM   1908  N NH1 . ARG A  1 248 ? -36.073 -26.888 56.826  1.00 11.01  ? 261 ARG A NH1 1 
ATOM   1909  N NH2 . ARG A  1 248 ? -37.157 -25.501 58.292  1.00 12.63  ? 261 ARG A NH2 1 
ATOM   1910  N N   . GLY A  1 249 ? -29.422 -23.898 53.799  1.00 22.86  ? 263 GLY A N   1 
ATOM   1911  C CA  . GLY A  1 249 ? -28.540 -23.890 52.637  1.00 23.58  ? 263 GLY A CA  1 
ATOM   1912  C C   . GLY A  1 249 ? -28.158 -22.518 52.120  1.00 24.16  ? 263 GLY A C   1 
ATOM   1913  O O   . GLY A  1 249 ? -27.391 -21.797 52.758  1.00 24.70  ? 263 GLY A O   1 
ATOM   1914  N N   . GLU A  1 250 ? -28.695 -22.160 50.958  1.00 24.47  ? 264 GLU A N   1 
ATOM   1915  C CA  . GLU A  1 250 ? -28.299 -20.935 50.267  1.00 25.44  ? 264 GLU A CA  1 
ATOM   1916  C C   . GLU A  1 250 ? -29.506 -20.068 49.901  1.00 24.36  ? 264 GLU A C   1 
ATOM   1917  O O   . GLU A  1 250 ? -30.551 -20.583 49.494  1.00 24.49  ? 264 GLU A O   1 
ATOM   1918  C CB  . GLU A  1 250 ? -27.487 -21.286 49.010  1.00 26.25  ? 264 GLU A CB  1 
ATOM   1919  C CG  . GLU A  1 250 ? -26.601 -20.153 48.481  1.00 31.38  ? 264 GLU A CG  1 
ATOM   1920  C CD  . GLU A  1 250 ? -25.722 -20.564 47.299  1.00 35.99  ? 264 GLU A CD  1 
ATOM   1921  O OE1 . GLU A  1 250 ? -25.824 -21.719 46.828  1.00 35.67  ? 264 GLU A OE1 1 
ATOM   1922  O OE2 . GLU A  1 250 ? -24.924 -19.719 46.839  1.00 39.13  ? 264 GLU A OE2 1 
ATOM   1923  N N   . SER A  1 251 ? -29.352 -18.754 50.049  1.00 23.25  ? 265 SER A N   1 
ATOM   1924  C CA  . SER A  1 251 ? -30.404 -17.801 49.692  1.00 22.15  ? 265 SER A CA  1 
ATOM   1925  C C   . SER A  1 251 ? -29.866 -16.398 49.439  1.00 21.45  ? 265 SER A C   1 
ATOM   1926  O O   . SER A  1 251 ? -28.702 -16.103 49.720  1.00 20.41  ? 265 SER A O   1 
ATOM   1927  C CB  . SER A  1 251 ? -31.484 -17.744 50.777  1.00 21.95  ? 265 SER A CB  1 
ATOM   1928  O OG  . SER A  1 251 ? -30.939 -17.368 52.028  1.00 21.70  ? 265 SER A OG  1 
ATOM   1929  N N   . LEU A  1 252 ? -30.729 -15.548 48.891  1.00 20.96  ? 266 LEU A N   1 
ATOM   1930  C CA  . LEU A  1 252 ? -30.470 -14.118 48.796  1.00 20.49  ? 266 LEU A CA  1 
ATOM   1931  C C   . LEU A  1 252 ? -31.452 -13.388 49.697  1.00 20.03  ? 266 LEU A C   1 
ATOM   1932  O O   . LEU A  1 252 ? -32.548 -13.883 49.965  1.00 20.97  ? 266 LEU A O   1 
ATOM   1933  C CB  . LEU A  1 252 ? -30.630 -13.622 47.357  1.00 20.59  ? 266 LEU A CB  1 
ATOM   1934  C CG  . LEU A  1 252 ? -29.913 -14.355 46.219  1.00 21.79  ? 266 LEU A CG  1 
ATOM   1935  C CD1 . LEU A  1 252 ? -30.259 -13.704 44.890  1.00 20.89  ? 266 LEU A CD1 1 
ATOM   1936  C CD2 . LEU A  1 252 ? -28.400 -14.386 46.430  1.00 24.48  ? 266 LEU A CD2 1 
ATOM   1937  N N   . GLY A  1 253 ? -31.051 -12.216 50.171  1.00 19.13  ? 267 GLY A N   1 
ATOM   1938  C CA  . GLY A  1 253 ? -31.936 -11.366 50.948  1.00 17.84  ? 267 GLY A CA  1 
ATOM   1939  C C   . GLY A  1 253 ? -32.024 -10.002 50.303  1.00 17.42  ? 267 GLY A C   1 
ATOM   1940  O O   . GLY A  1 253 ? -30.998 -9.361  50.071  1.00 16.92  ? 267 GLY A O   1 
ATOM   1941  N N   . VAL A  1 254 ? -33.248 -9.573  50.001  1.00 17.27  ? 268 VAL A N   1 
ATOM   1942  C CA  . VAL A  1 254 ? -33.499 -8.251  49.436  1.00 17.65  ? 268 VAL A CA  1 
ATOM   1943  C C   . VAL A  1 254 ? -34.268 -7.397  50.430  1.00 18.59  ? 268 VAL A C   1 
ATOM   1944  O O   . VAL A  1 254 ? -35.153 -7.893  51.130  1.00 19.43  ? 268 VAL A O   1 
ATOM   1945  C CB  . VAL A  1 254 ? -34.371 -8.299  48.155  1.00 17.87  ? 268 VAL A CB  1 
ATOM   1946  C CG1 . VAL A  1 254 ? -33.990 -7.155  47.210  1.00 16.85  ? 268 VAL A CG1 1 
ATOM   1947  C CG2 . VAL A  1 254 ? -34.273 -9.650  47.453  1.00 17.59  ? 268 VAL A CG2 1 
ATOM   1948  N N   . GLN A  1 255 ? -33.925 -6.116  50.488  1.00 18.88  ? 269 GLN A N   1 
ATOM   1949  C CA  . GLN A  1 255 ? -34.772 -5.123  51.123  1.00 19.00  ? 269 GLN A CA  1 
ATOM   1950  C C   . GLN A  1 255 ? -35.488 -4.387  50.002  1.00 19.37  ? 269 GLN A C   1 
ATOM   1951  O O   . GLN A  1 255 ? -34.837 -3.762  49.161  1.00 18.51  ? 269 GLN A O   1 
ATOM   1952  C CB  . GLN A  1 255 ? -33.944 -4.128  51.921  1.00 19.64  ? 269 GLN A CB  1 
ATOM   1953  C CG  . GLN A  1 255 ? -33.223 -4.687  53.122  1.00 19.53  ? 269 GLN A CG  1 
ATOM   1954  C CD  . GLN A  1 255 ? -32.641 -3.580  53.966  1.00 23.10  ? 269 GLN A CD  1 
ATOM   1955  O OE1 . GLN A  1 255 ? -31.897 -2.730  53.471  1.00 20.61  ? 269 GLN A OE1 1 
ATOM   1956  N NE2 . GLN A  1 255 ? -32.993 -3.568  55.246  1.00 25.14  ? 269 GLN A NE2 1 
ATOM   1957  N N   . SER A  1 256 ? -36.818 -4.476  49.986  1.00 19.47  ? 270 SER A N   1 
ATOM   1958  C CA  . SER A  1 256 ? -37.628 -3.883  48.925  1.00 19.49  ? 270 SER A CA  1 
ATOM   1959  C C   . SER A  1 256 ? -39.107 -3.837  49.271  1.00 20.50  ? 270 SER A C   1 
ATOM   1960  O O   . SER A  1 256 ? -39.608 -4.662  50.040  1.00 20.65  ? 270 SER A O   1 
ATOM   1961  C CB  . SER A  1 256 ? -37.459 -4.660  47.621  1.00 19.35  ? 270 SER A CB  1 
ATOM   1962  O OG  . SER A  1 256 ? -38.313 -4.139  46.619  1.00 18.18  ? 270 SER A OG  1 
ATOM   1963  N N   . ASP A  1 257 ? -39.801 -2.873  48.676  1.00 21.12  ? 271 ASP A N   1 
ATOM   1964  C CA  . ASP A  1 257 ? -41.249 -2.770  48.789  1.00 22.01  ? 271 ASP A CA  1 
ATOM   1965  C C   . ASP A  1 257 ? -41.942 -3.199  47.488  1.00 21.30  ? 271 ASP A C   1 
ATOM   1966  O O   . ASP A  1 257 ? -43.176 -3.189  47.392  1.00 20.65  ? 271 ASP A O   1 
ATOM   1967  C CB  . ASP A  1 257 ? -41.647 -1.348  49.195  1.00 22.99  ? 271 ASP A CB  1 
ATOM   1968  C CG  . ASP A  1 257 ? -41.287 -1.028  50.645  1.00 28.49  ? 271 ASP A CG  1 
ATOM   1969  O OD1 . ASP A  1 257 ? -41.103 -1.971  51.454  1.00 31.49  ? 271 ASP A OD1 1 
ATOM   1970  O OD2 . ASP A  1 257 ? -41.193 0.175   50.980  1.00 34.25  ? 271 ASP A OD2 1 
ATOM   1971  N N   . ALA A  1 258 ? -41.133 -3.595  46.504  1.00 20.36  ? 272 ALA A N   1 
ATOM   1972  C CA  . ALA A  1 258 ? -41.624 -4.068  45.207  1.00 19.39  ? 272 ALA A CA  1 
ATOM   1973  C C   . ALA A  1 258 ? -42.434 -5.361  45.333  1.00 18.50  ? 272 ALA A C   1 
ATOM   1974  O O   . ALA A  1 258 ? -42.026 -6.285  46.041  1.00 17.89  ? 272 ALA A O   1 
ATOM   1975  C CB  . ALA A  1 258 ? -40.466 -4.260  44.239  1.00 19.16  ? 272 ALA A CB  1 
ATOM   1976  N N   . PRO A  1 259 ? -43.591 -5.422  44.652  1.00 18.12  ? 273 PRO A N   1 
ATOM   1977  C CA  . PRO A  1 259 ? -44.443 -6.615  44.657  1.00 18.02  ? 273 PRO A CA  1 
ATOM   1978  C C   . PRO A  1 259 ? -43.732 -7.833  44.082  1.00 17.71  ? 273 PRO A C   1 
ATOM   1979  O O   . PRO A  1 259 ? -42.843 -7.690  43.245  1.00 17.92  ? 273 PRO A O   1 
ATOM   1980  C CB  . PRO A  1 259 ? -45.608 -6.216  43.742  1.00 17.87  ? 273 PRO A CB  1 
ATOM   1981  C CG  . PRO A  1 259 ? -45.646 -4.729  43.808  1.00 18.50  ? 273 PRO A CG  1 
ATOM   1982  C CD  . PRO A  1 259 ? -44.211 -4.310  43.907  1.00 18.19  ? 273 PRO A CD  1 
ATOM   1983  N N   . LEU A  1 260 ? -44.115 -9.021  44.539  1.00 17.48  ? 274 LEU A N   1 
ATOM   1984  C CA  . LEU A  1 260 ? -43.582 -10.254 43.972  1.00 17.63  ? 274 LEU A CA  1 
ATOM   1985  C C   . LEU A  1 260 ? -44.243 -10.512 42.628  1.00 17.93  ? 274 LEU A C   1 
ATOM   1986  O O   . LEU A  1 260 ? -45.432 -10.240 42.456  1.00 17.62  ? 274 LEU A O   1 
ATOM   1987  C CB  . LEU A  1 260 ? -43.826 -11.446 44.902  1.00 17.45  ? 274 LEU A CB  1 
ATOM   1988  C CG  . LEU A  1 260 ? -43.365 -11.424 46.363  1.00 16.32  ? 274 LEU A CG  1 
ATOM   1989  C CD1 . LEU A  1 260 ? -43.574 -12.800 46.978  1.00 12.44  ? 274 LEU A CD1 1 
ATOM   1990  C CD2 . LEU A  1 260 ? -41.915 -10.973 46.516  1.00 11.55  ? 274 LEU A CD2 1 
ATOM   1991  N N   . ASP A  1 261 ? -43.470 -11.020 41.675  1.00 18.63  ? 275 ASP A N   1 
ATOM   1992  C CA  . ASP A  1 261 ? -44.018 -11.401 40.377  1.00 19.92  ? 275 ASP A CA  1 
ATOM   1993  C C   . ASP A  1 261 ? -43.452 -12.747 39.958  1.00 20.29  ? 275 ASP A C   1 
ATOM   1994  O O   . ASP A  1 261 ? -42.250 -12.878 39.717  1.00 20.67  ? 275 ASP A O   1 
ATOM   1995  C CB  . ASP A  1 261 ? -43.741 -10.329 39.314  1.00 20.10  ? 275 ASP A CB  1 
ATOM   1996  C CG  . ASP A  1 261 ? -44.713 -10.397 38.137  1.00 21.17  ? 275 ASP A CG  1 
ATOM   1997  O OD1 . ASP A  1 261 ? -45.608 -11.269 38.140  1.00 24.38  ? 275 ASP A OD1 1 
ATOM   1998  O OD2 . ASP A  1 261 ? -44.587 -9.573  37.204  1.00 22.69  ? 275 ASP A OD2 1 
ATOM   1999  N N   . SER A  1 262 ? -44.330 -13.744 39.889  1.00 20.76  ? 276 SER A N   1 
ATOM   2000  C CA  . SER A  1 262 ? -43.938 -15.116 39.575  1.00 21.55  ? 276 SER A CA  1 
ATOM   2001  C C   . SER A  1 262 ? -44.009 -15.409 38.075  1.00 21.97  ? 276 SER A C   1 
ATOM   2002  O O   . SER A  1 262 ? -44.032 -16.573 37.661  1.00 22.39  ? 276 SER A O   1 
ATOM   2003  C CB  . SER A  1 262 ? -44.804 -16.108 40.361  1.00 21.35  ? 276 SER A CB  1 
ATOM   2004  O OG  . SER A  1 262 ? -46.161 -16.023 39.969  1.00 21.08  ? 276 SER A OG  1 
ATOM   2005  N N   . SER A  1 263 A -44.038 -14.349 37.269  1.00 22.14  ? 276 SER A N   1 
ATOM   2006  C CA  . SER A  1 263 A -44.100 -14.474 35.814  1.00 22.12  ? 276 SER A CA  1 
ATOM   2007  C C   . SER A  1 263 A -42.808 -14.015 35.129  1.00 22.02  ? 276 SER A C   1 
ATOM   2008  O O   . SER A  1 263 A -42.668 -14.140 33.909  1.00 21.65  ? 276 SER A O   1 
ATOM   2009  C CB  . SER A  1 263 A -45.313 -13.722 35.259  1.00 21.88  ? 276 SER A CB  1 
ATOM   2010  O OG  . SER A  1 263 A -45.243 -12.342 35.566  1.00 23.34  ? 276 SER A OG  1 
ATOM   2011  N N   . CYS A  1 264 ? -41.873 -13.486 35.919  1.00 22.24  ? 277 CYS A N   1 
ATOM   2012  C CA  . CYS A  1 264 ? -40.543 -13.119 35.425  1.00 22.90  ? 277 CYS A CA  1 
ATOM   2013  C C   . CYS A  1 264 ? -39.430 -13.768 36.247  1.00 22.78  ? 277 CYS A C   1 
ATOM   2014  O O   . CYS A  1 264 ? -39.529 -13.877 37.469  1.00 22.26  ? 277 CYS A O   1 
ATOM   2015  C CB  . CYS A  1 264 ? -40.361 -11.594 35.386  1.00 22.79  ? 277 CYS A CB  1 
ATOM   2016  S SG  . CYS A  1 264 ? -40.752 -10.727 36.931  1.00 26.96  ? 277 CYS A SG  1 
ATOM   2017  N N   . ARG A  1 265 ? -38.381 -14.202 35.551  1.00 23.42  ? 278 ARG A N   1 
ATOM   2018  C CA  . ARG A  1 265 ? -37.185 -14.778 36.161  1.00 23.92  ? 278 ARG A CA  1 
ATOM   2019  C C   . ARG A  1 265 ? -36.140 -13.675 36.324  1.00 23.65  ? 278 ARG A C   1 
ATOM   2020  O O   . ARG A  1 265 ? -36.060 -12.769 35.493  1.00 24.26  ? 278 ARG A O   1 
ATOM   2021  C CB  . ARG A  1 265 ? -36.651 -15.919 35.279  1.00 24.41  ? 278 ARG A CB  1 
ATOM   2022  C CG  . ARG A  1 265 ? -35.439 -16.678 35.831  1.00 29.35  ? 278 ARG A CG  1 
ATOM   2023  C CD  . ARG A  1 265 ? -35.175 -17.978 35.067  1.00 33.73  ? 278 ARG A CD  1 
ATOM   2024  N NE  . ARG A  1 265 ? -35.998 -19.089 35.556  1.00 37.92  ? 278 ARG A NE  1 
ATOM   2025  C CZ  . ARG A  1 265 ? -36.975 -19.681 34.867  1.00 37.63  ? 278 ARG A CZ  1 
ATOM   2026  N NH1 . ARG A  1 265 ? -37.270 -19.285 33.634  1.00 36.82  ? 278 ARG A NH1 1 
ATOM   2027  N NH2 . ARG A  1 265 ? -37.660 -20.681 35.414  1.00 34.06  ? 278 ARG A NH2 1 
ATOM   2028  N N   . GLY A  1 266 ? -35.347 -13.751 37.392  1.00 23.22  ? 279 GLY A N   1 
ATOM   2029  C CA  . GLY A  1 266 ? -34.284 -12.770 37.652  1.00 22.27  ? 279 GLY A CA  1 
ATOM   2030  C C   . GLY A  1 266 ? -33.306 -13.240 38.714  1.00 22.01  ? 279 GLY A C   1 
ATOM   2031  O O   . GLY A  1 266 ? -33.650 -14.072 39.551  1.00 22.03  ? 279 GLY A O   1 
ATOM   2032  N N   . ASP A  1 267 ? -32.085 -12.711 38.675  1.00 22.15  ? 280 ASP A N   1 
ATOM   2033  C CA  . ASP A  1 267 ? -31.023 -13.117 39.602  1.00 22.36  ? 280 ASP A CA  1 
ATOM   2034  C C   . ASP A  1 267 ? -30.305 -11.926 40.227  1.00 21.41  ? 280 ASP A C   1 
ATOM   2035  O O   . ASP A  1 267 ? -29.359 -12.100 40.997  1.00 22.26  ? 280 ASP A O   1 
ATOM   2036  C CB  . ASP A  1 267 ? -30.001 -14.009 38.889  1.00 23.64  ? 280 ASP A CB  1 
ATOM   2037  C CG  . ASP A  1 267 ? -30.627 -15.255 38.290  1.00 28.94  ? 280 ASP A CG  1 
ATOM   2038  O OD1 . ASP A  1 267 ? -31.387 -15.949 39.005  1.00 32.93  ? 280 ASP A OD1 1 
ATOM   2039  O OD2 . ASP A  1 267 ? -30.355 -15.539 37.101  1.00 33.27  ? 280 ASP A OD2 1 
ATOM   2040  N N   . CYS A  1 268 ? -30.751 -10.721 39.883  1.00 20.00  ? 281 CYS A N   1 
ATOM   2041  C CA  . CYS A  1 268 ? -30.181 -9.494  40.421  1.00 18.38  ? 281 CYS A CA  1 
ATOM   2042  C C   . CYS A  1 268 ? -31.297 -8.657  41.007  1.00 17.26  ? 281 CYS A C   1 
ATOM   2043  O O   . CYS A  1 268 ? -32.217 -8.258  40.290  1.00 18.07  ? 281 CYS A O   1 
ATOM   2044  C CB  . CYS A  1 268 ? -29.472 -8.701  39.325  1.00 18.48  ? 281 CYS A CB  1 
ATOM   2045  S SG  . CYS A  1 268 ? -28.771 -7.144  39.911  1.00 20.18  ? 281 CYS A SG  1 
ATOM   2046  N N   . PHE A  1 269 ? -31.219 -8.384  42.305  1.00 15.66  ? 282 PHE A N   1 
ATOM   2047  C CA  . PHE A  1 269 ? -32.301 -7.683  42.990  1.00 15.00  ? 282 PHE A CA  1 
ATOM   2048  C C   . PHE A  1 269 ? -31.811 -6.469  43.762  1.00 14.88  ? 282 PHE A C   1 
ATOM   2049  O O   . PHE A  1 269 ? -30.639 -6.387  44.138  1.00 15.23  ? 282 PHE A O   1 
ATOM   2050  C CB  . PHE A  1 269 ? -33.062 -8.640  43.914  1.00 14.85  ? 282 PHE A CB  1 
ATOM   2051  C CG  . PHE A  1 269 ? -33.547 -9.887  43.228  1.00 13.95  ? 282 PHE A CG  1 
ATOM   2052  C CD1 . PHE A  1 269 ? -34.701 -9.867  42.454  1.00 12.66  ? 282 PHE A CD1 1 
ATOM   2053  C CD2 . PHE A  1 269 ? -32.840 -11.079 43.346  1.00 11.51  ? 282 PHE A CD2 1 
ATOM   2054  C CE1 . PHE A  1 269 ? -35.146 -11.016 41.810  1.00 13.06  ? 282 PHE A CE1 1 
ATOM   2055  C CE2 . PHE A  1 269 ? -33.277 -12.234 42.709  1.00 12.85  ? 282 PHE A CE2 1 
ATOM   2056  C CZ  . PHE A  1 269 ? -34.436 -12.203 41.941  1.00 13.64  ? 282 PHE A CZ  1 
ATOM   2057  N N   . HIS A  1 270 ? -32.728 -5.529  43.983  1.00 14.17  ? 283 HIS A N   1 
ATOM   2058  C CA  . HIS A  1 270 ? -32.463 -4.297  44.719  1.00 14.18  ? 283 HIS A CA  1 
ATOM   2059  C C   . HIS A  1 270 ? -33.789 -3.702  45.204  1.00 14.06  ? 283 HIS A C   1 
ATOM   2060  O O   . HIS A  1 270 ? -34.862 -4.188  44.832  1.00 14.52  ? 283 HIS A O   1 
ATOM   2061  C CB  . HIS A  1 270 ? -31.723 -3.300  43.826  1.00 14.34  ? 283 HIS A CB  1 
ATOM   2062  C CG  . HIS A  1 270 ? -32.532 -2.816  42.664  1.00 14.95  ? 283 HIS A CG  1 
ATOM   2063  N ND1 . HIS A  1 270 ? -33.069 -1.547  42.608  1.00 12.68  ? 283 HIS A ND1 1 
ATOM   2064  C CD2 . HIS A  1 270 ? -32.905 -3.433  41.518  1.00 11.58  ? 283 HIS A CD2 1 
ATOM   2065  C CE1 . HIS A  1 270 ? -33.728 -1.401  41.473  1.00 12.89  ? 283 HIS A CE1 1 
ATOM   2066  N NE2 . HIS A  1 270 ? -33.645 -2.532  40.794  1.00 11.63  ? 283 HIS A NE2 1 
ATOM   2067  N N   . SER A  1 271 ? -33.720 -2.644  46.009  1.00 13.17  ? 284 SER A N   1 
ATOM   2068  C CA  . SER A  1 271 ? -34.924 -2.043  46.593  1.00 13.26  ? 284 SER A CA  1 
ATOM   2069  C C   . SER A  1 271 ? -36.024 -1.671  45.586  1.00 13.54  ? 284 SER A C   1 
ATOM   2070  O O   . SER A  1 271 ? -37.209 -1.684  45.924  1.00 13.57  ? 284 SER A O   1 
ATOM   2071  C CB  . SER A  1 271 ? -34.564 -0.834  47.465  1.00 13.04  ? 284 SER A CB  1 
ATOM   2072  O OG  . SER A  1 271 ? -33.929 0.180   46.711  1.00 14.11  ? 284 SER A OG  1 
ATOM   2073  N N   . GLY A  1 272 ? -35.632 -1.354  44.354  1.00 13.74  ? 285 GLY A N   1 
ATOM   2074  C CA  . GLY A  1 272 ? -36.583 -0.923  43.332  1.00 13.62  ? 285 GLY A CA  1 
ATOM   2075  C C   . GLY A  1 272 ? -37.091 -2.038  42.435  1.00 13.78  ? 285 GLY A C   1 
ATOM   2076  O O   . GLY A  1 272 ? -37.815 -1.777  41.477  1.00 13.81  ? 285 GLY A O   1 
ATOM   2077  N N   . GLY A  1 273 ? -36.705 -3.277  42.738  1.00 14.09  ? 286 GLY A N   1 
ATOM   2078  C CA  . GLY A  1 273 ? -37.176 -4.440  41.988  1.00 14.66  ? 286 GLY A CA  1 
ATOM   2079  C C   . GLY A  1 273 ? -36.071 -5.343  41.471  1.00 15.36  ? 286 GLY A C   1 
ATOM   2080  O O   . GLY A  1 273 ? -35.117 -5.642  42.189  1.00 16.21  ? 286 GLY A O   1 
ATOM   2081  N N   . THR A  1 274 ? -36.204 -5.766  40.215  1.00 15.23  ? 287 THR A N   1 
ATOM   2082  C CA  . THR A  1 274 ? -35.299 -6.735  39.600  1.00 15.50  ? 287 THR A CA  1 
ATOM   2083  C C   . THR A  1 274 ? -34.590 -6.136  38.389  1.00 15.95  ? 287 THR A C   1 
ATOM   2084  O O   . THR A  1 274 ? -35.205 -5.436  37.582  1.00 16.12  ? 287 THR A O   1 
ATOM   2085  C CB  . THR A  1 274 ? -36.067 -8.014  39.149  1.00 15.49  ? 287 THR A CB  1 
ATOM   2086  O OG1 . THR A  1 274 ? -36.862 -8.511  40.230  1.00 16.46  ? 287 THR A OG1 1 
ATOM   2087  C CG2 . THR A  1 274 ? -35.114 -9.112  38.703  1.00 14.73  ? 287 THR A CG2 1 
ATOM   2088  N N   . ILE A  1 275 ? -33.295 -6.419  38.272  1.00 16.46  ? 288 ILE A N   1 
ATOM   2089  C CA  . ILE A  1 275 ? -32.523 -6.060  37.086  1.00 17.31  ? 288 ILE A CA  1 
ATOM   2090  C C   . ILE A  1 275 ? -32.279 -7.315  36.246  1.00 18.37  ? 288 ILE A C   1 
ATOM   2091  O O   . ILE A  1 275 ? -31.574 -8.236  36.669  1.00 19.16  ? 288 ILE A O   1 
ATOM   2092  C CB  . ILE A  1 275 ? -31.172 -5.394  37.441  1.00 16.97  ? 288 ILE A CB  1 
ATOM   2093  C CG1 . ILE A  1 275 ? -31.387 -4.159  38.321  1.00 17.43  ? 288 ILE A CG1 1 
ATOM   2094  C CG2 . ILE A  1 275 ? -30.420 -5.015  36.178  1.00 16.94  ? 288 ILE A CG2 1 
ATOM   2095  C CD1 . ILE A  1 275 ? -30.112 -3.614  38.954  1.00 17.16  ? 288 ILE A CD1 1 
ATOM   2096  N N   . VAL A  1 276 ? -32.880 -7.346  35.061  1.00 18.81  ? 289 VAL A N   1 
ATOM   2097  C CA  . VAL A  1 276 ? -32.705 -8.454  34.129  1.00 18.60  ? 289 VAL A CA  1 
ATOM   2098  C C   . VAL A  1 276 ? -31.916 -7.938  32.936  1.00 18.20  ? 289 VAL A C   1 
ATOM   2099  O O   . VAL A  1 276 ? -32.405 -7.112  32.157  1.00 17.58  ? 289 VAL A O   1 
ATOM   2100  C CB  . VAL A  1 276 ? -34.064 -9.067  33.693  1.00 18.81  ? 289 VAL A CB  1 
ATOM   2101  C CG1 . VAL A  1 276 ? -33.878 -10.075 32.567  1.00 17.51  ? 289 VAL A CG1 1 
ATOM   2102  C CG2 . VAL A  1 276 ? -34.750 -9.728  34.881  1.00 19.85  ? 289 VAL A CG2 1 
ATOM   2103  N N   . SER A  1 277 ? -30.684 -8.421  32.815  1.00 18.03  ? 290 SER A N   1 
ATOM   2104  C CA  . SER A  1 277 ? -29.755 -7.906  31.825  1.00 17.51  ? 290 SER A CA  1 
ATOM   2105  C C   . SER A  1 277 ? -28.672 -8.918  31.527  1.00 17.62  ? 290 SER A C   1 
ATOM   2106  O O   . SER A  1 277 ? -28.323 -9.736  32.375  1.00 17.00  ? 290 SER A O   1 
ATOM   2107  C CB  . SER A  1 277 ? -29.107 -6.613  32.335  1.00 17.57  ? 290 SER A CB  1 
ATOM   2108  O OG  . SER A  1 277 ? -28.553 -5.854  31.273  1.00 14.71  ? 290 SER A OG  1 
ATOM   2109  N N   . SER A  1 278 ? -28.149 -8.854  30.308  1.00 18.47  ? 291 SER A N   1 
ATOM   2110  C CA  . SER A  1 278 ? -26.934 -9.571  29.946  1.00 18.79  ? 291 SER A CA  1 
ATOM   2111  C C   . SER A  1 278 ? -25.803 -8.569  29.678  1.00 18.47  ? 291 SER A C   1 
ATOM   2112  O O   . SER A  1 278 ? -24.746 -8.933  29.151  1.00 19.36  ? 291 SER A O   1 
ATOM   2113  C CB  . SER A  1 278 ? -27.186 -10.470 28.735  1.00 18.68  ? 291 SER A CB  1 
ATOM   2114  O OG  . SER A  1 278 ? -27.823 -9.746  27.698  1.00 21.65  ? 291 SER A OG  1 
ATOM   2115  N N   . LEU A  1 279 ? -26.030 -7.311  30.059  1.00 17.64  ? 292 LEU A N   1 
ATOM   2116  C CA  . LEU A  1 279 ? -25.057 -6.237  29.851  1.00 16.59  ? 292 LEU A CA  1 
ATOM   2117  C C   . LEU A  1 279 ? -24.059 -6.173  31.002  1.00 16.19  ? 292 LEU A C   1 
ATOM   2118  O O   . LEU A  1 279 ? -24.400 -6.532  32.128  1.00 16.66  ? 292 LEU A O   1 
ATOM   2119  C CB  . LEU A  1 279 ? -25.759 -4.882  29.675  1.00 16.27  ? 292 LEU A CB  1 
ATOM   2120  C CG  . LEU A  1 279 ? -26.841 -4.722  28.594  1.00 15.08  ? 292 LEU A CG  1 
ATOM   2121  C CD1 . LEU A  1 279 ? -27.217 -3.248  28.443  1.00 11.40  ? 292 LEU A CD1 1 
ATOM   2122  C CD2 . LEU A  1 279 ? -26.421 -5.317  27.245  1.00 7.36   ? 292 LEU A CD2 1 
ATOM   2123  N N   . PRO A  1 280 ? -22.823 -5.710  30.723  1.00 15.69  ? 293 PRO A N   1 
ATOM   2124  C CA  . PRO A  1 280 ? -21.771 -5.685  31.740  1.00 14.89  ? 293 PRO A CA  1 
ATOM   2125  C C   . PRO A  1 280 ? -21.963 -4.629  32.832  1.00 14.16  ? 293 PRO A C   1 
ATOM   2126  O O   . PRO A  1 280 ? -21.429 -4.794  33.934  1.00 15.23  ? 293 PRO A O   1 
ATOM   2127  C CB  . PRO A  1 280 ? -20.503 -5.392  30.928  1.00 14.63  ? 293 PRO A CB  1 
ATOM   2128  C CG  . PRO A  1 280 ? -20.980 -4.665  29.731  1.00 14.68  ? 293 PRO A CG  1 
ATOM   2129  C CD  . PRO A  1 280 ? -22.329 -5.237  29.413  1.00 16.15  ? 293 PRO A CD  1 
ATOM   2130  N N   . PHE A  1 281 ? -22.711 -3.566  32.533  1.00 12.58  ? 294 PHE A N   1 
ATOM   2131  C CA  . PHE A  1 281 ? -22.885 -2.447  33.468  1.00 11.49  ? 294 PHE A CA  1 
ATOM   2132  C C   . PHE A  1 281 ? -24.349 -2.038  33.667  1.00 11.38  ? 294 PHE A C   1 
ATOM   2133  O O   . PHE A  1 281 ? -25.213 -2.346  32.834  1.00 11.10  ? 294 PHE A O   1 
ATOM   2134  C CB  . PHE A  1 281 ? -22.059 -1.236  33.011  1.00 11.05  ? 294 PHE A CB  1 
ATOM   2135  C CG  . PHE A  1 281 ? -20.640 -1.574  32.648  1.00 10.41  ? 294 PHE A CG  1 
ATOM   2136  C CD1 . PHE A  1 281 ? -20.213 -1.497  31.328  1.00 8.73   ? 294 PHE A CD1 1 
ATOM   2137  C CD2 . PHE A  1 281 ? -19.733 -1.990  33.625  1.00 8.09   ? 294 PHE A CD2 1 
ATOM   2138  C CE1 . PHE A  1 281 ? -18.899 -1.821  30.985  1.00 9.21   ? 294 PHE A CE1 1 
ATOM   2139  C CE2 . PHE A  1 281 ? -18.423 -2.319  33.294  1.00 5.38   ? 294 PHE A CE2 1 
ATOM   2140  C CZ  . PHE A  1 281 ? -18.004 -2.235  31.974  1.00 7.86   ? 294 PHE A CZ  1 
ATOM   2141  N N   . GLN A  1 282 ? -24.617 -1.348  34.778  1.00 10.19  ? 295 GLN A N   1 
ATOM   2142  C CA  . GLN A  1 282 ? -25.951 -0.825  35.068  1.00 9.62   ? 295 GLN A CA  1 
ATOM   2143  C C   . GLN A  1 282 ? -25.908 0.492   35.832  1.00 9.81   ? 295 GLN A C   1 
ATOM   2144  O O   . GLN A  1 282 ? -24.993 0.731   36.624  1.00 9.55   ? 295 GLN A O   1 
ATOM   2145  C CB  . GLN A  1 282 ? -26.813 -1.864  35.806  1.00 10.24  ? 295 GLN A CB  1 
ATOM   2146  C CG  . GLN A  1 282 ? -26.244 -2.403  37.121  1.00 7.44   ? 295 GLN A CG  1 
ATOM   2147  C CD  . GLN A  1 282 ? -26.712 -1.630  38.346  1.00 7.54   ? 295 GLN A CD  1 
ATOM   2148  O OE1 . GLN A  1 282 ? -27.486 -0.672  38.245  1.00 3.88   ? 295 GLN A OE1 1 
ATOM   2149  N NE2 . GLN A  1 282 ? -26.235 -2.044  39.517  1.00 5.52   ? 295 GLN A NE2 1 
ATOM   2150  N N   . ASN A  1 283 ? -26.912 1.332   35.586  1.00 9.79   ? 296 ASN A N   1 
ATOM   2151  C CA  . ASN A  1 283 ? -27.020 2.661   36.181  1.00 9.81   ? 296 ASN A CA  1 
ATOM   2152  C C   . ASN A  1 283 ? -28.295 2.772   37.027  1.00 10.81  ? 296 ASN A C   1 
ATOM   2153  O O   . ASN A  1 283 ? -28.738 3.865   37.389  1.00 11.06  ? 296 ASN A O   1 
ATOM   2154  C CB  . ASN A  1 283 ? -27.005 3.714   35.071  1.00 9.72   ? 296 ASN A CB  1 
ATOM   2155  C CG  . ASN A  1 283 ? -26.810 5.133   35.592  1.00 11.88  ? 296 ASN A CG  1 
ATOM   2156  O OD1 . ASN A  1 283 ? -27.516 6.053   35.179  1.00 12.71  ? 296 ASN A OD1 1 
ATOM   2157  N ND2 . ASN A  1 283 ? -25.847 5.318   36.489  1.00 16.00  ? 296 ASN A ND2 1 
ATOM   2158  N N   . ILE A  1 284 ? -28.866 1.622   37.360  1.00 11.41  ? 297 ILE A N   1 
ATOM   2159  C CA  . ILE A  1 284 ? -30.142 1.565   38.053  1.00 11.58  ? 297 ILE A CA  1 
ATOM   2160  C C   . ILE A  1 284 ? -30.001 1.800   39.562  1.00 12.54  ? 297 ILE A C   1 
ATOM   2161  O O   . ILE A  1 284 ? -30.635 2.696   40.111  1.00 13.34  ? 297 ILE A O   1 
ATOM   2162  C CB  . ILE A  1 284 ? -30.863 0.233   37.752  1.00 10.84  ? 297 ILE A CB  1 
ATOM   2163  C CG1 . ILE A  1 284 ? -31.220 0.166   36.263  1.00 8.90   ? 297 ILE A CG1 1 
ATOM   2164  C CG2 . ILE A  1 284 ? -32.108 0.084   38.618  1.00 12.00  ? 297 ILE A CG2 1 
ATOM   2165  C CD1 . ILE A  1 284 ? -31.484 -1.226  35.740  1.00 8.18   ? 297 ILE A CD1 1 
ATOM   2166  N N   . ASN A  1 285 ? -29.167 1.000   40.221  1.00 13.09  ? 298 ASN A N   1 
ATOM   2167  C CA  . ASN A  1 285 ? -29.016 1.060   41.674  1.00 12.94  ? 298 ASN A CA  1 
ATOM   2168  C C   . ASN A  1 285 ? -27.640 0.560   42.113  1.00 12.53  ? 298 ASN A C   1 
ATOM   2169  O O   . ASN A  1 285 ? -27.154 -0.453  41.612  1.00 12.27  ? 298 ASN A O   1 
ATOM   2170  C CB  . ASN A  1 285 ? -30.116 0.229   42.340  1.00 13.14  ? 298 ASN A CB  1 
ATOM   2171  C CG  . ASN A  1 285 ? -30.292 0.549   43.815  1.00 13.89  ? 298 ASN A CG  1 
ATOM   2172  O OD1 . ASN A  1 285 ? -29.321 0.760   44.548  1.00 13.59  ? 298 ASN A OD1 1 
ATOM   2173  N ND2 . ASN A  1 285 ? -31.544 0.570   44.263  1.00 12.67  ? 298 ASN A ND2 1 
ATOM   2174  N N   . SER A  1 286 ? -27.017 1.270   43.049  1.00 12.40  ? 299 SER A N   1 
ATOM   2175  C CA  . SER A  1 286 ? -25.676 0.910   43.511  1.00 12.73  ? 299 SER A CA  1 
ATOM   2176  C C   . SER A  1 286 ? -25.698 -0.154  44.601  1.00 13.27  ? 299 SER A C   1 
ATOM   2177  O O   . SER A  1 286 ? -24.678 -0.797  44.866  1.00 12.95  ? 299 SER A O   1 
ATOM   2178  C CB  . SER A  1 286 ? -24.903 2.148   43.976  1.00 12.90  ? 299 SER A CB  1 
ATOM   2179  O OG  . SER A  1 286 ? -25.441 2.681   45.171  1.00 14.36  ? 299 SER A OG  1 
ATOM   2180  N N   . ARG A  1 287 ? -26.861 -0.333  45.228  1.00 14.49  ? 300 ARG A N   1 
ATOM   2181  C CA  . ARG A  1 287 ? -27.058 -1.371  46.243  1.00 14.64  ? 300 ARG A CA  1 
ATOM   2182  C C   . ARG A  1 287 ? -27.844 -2.518  45.641  1.00 15.58  ? 300 ARG A C   1 
ATOM   2183  O O   . ARG A  1 287 ? -29.062 -2.423  45.459  1.00 16.57  ? 300 ARG A O   1 
ATOM   2184  C CB  . ARG A  1 287 ? -27.801 -0.819  47.459  1.00 14.47  ? 300 ARG A CB  1 
ATOM   2185  C CG  . ARG A  1 287 ? -27.010 0.187   48.263  1.00 15.05  ? 300 ARG A CG  1 
ATOM   2186  C CD  . ARG A  1 287 ? -27.868 0.865   49.317  1.00 15.57  ? 300 ARG A CD  1 
ATOM   2187  N NE  . ARG A  1 287 ? -27.045 1.739   50.145  1.00 20.74  ? 300 ARG A NE  1 
ATOM   2188  C CZ  . ARG A  1 287 ? -26.684 2.981   49.822  1.00 23.30  ? 300 ARG A CZ  1 
ATOM   2189  N NH1 . ARG A  1 287 ? -27.070 3.536   48.677  1.00 24.97  ? 300 ARG A NH1 1 
ATOM   2190  N NH2 . ARG A  1 287 ? -25.924 3.671   50.656  1.00 27.20  ? 300 ARG A NH2 1 
ATOM   2191  N N   . THR A  1 288 ? -27.140 -3.599  45.323  1.00 16.04  ? 301 THR A N   1 
ATOM   2192  C CA  . THR A  1 288 ? -27.752 -4.759  44.683  1.00 16.17  ? 301 THR A CA  1 
ATOM   2193  C C   . THR A  1 288 ? -27.363 -6.065  45.374  1.00 16.23  ? 301 THR A C   1 
ATOM   2194  O O   . THR A  1 288 ? -26.309 -6.158  46.007  1.00 15.39  ? 301 THR A O   1 
ATOM   2195  C CB  . THR A  1 288 ? -27.381 -4.845  43.183  1.00 16.18  ? 301 THR A CB  1 
ATOM   2196  O OG1 . THR A  1 288 ? -25.956 -4.877  43.039  1.00 15.87  ? 301 THR A OG1 1 
ATOM   2197  C CG2 . THR A  1 288 ? -27.939 -3.658  42.416  1.00 15.07  ? 301 THR A CG2 1 
ATOM   2198  N N   . VAL A  1 289 ? -28.236 -7.061  45.250  1.00 16.55  ? 302 VAL A N   1 
ATOM   2199  C CA  . VAL A  1 289 ? -27.977 -8.407  45.746  1.00 17.51  ? 302 VAL A CA  1 
ATOM   2200  C C   . VAL A  1 289 ? -28.118 -9.398  44.587  1.00 17.65  ? 302 VAL A C   1 
ATOM   2201  O O   . VAL A  1 289 ? -29.011 -9.260  43.753  1.00 18.36  ? 302 VAL A O   1 
ATOM   2202  C CB  . VAL A  1 289 ? -28.911 -8.780  46.955  1.00 17.49  ? 302 VAL A CB  1 
ATOM   2203  C CG1 . VAL A  1 289 ? -30.375 -8.485  46.654  1.00 18.82  ? 302 VAL A CG1 1 
ATOM   2204  C CG2 . VAL A  1 289 ? -28.740 -10.244 47.372  1.00 18.79  ? 302 VAL A CG2 1 
ATOM   2205  N N   . GLY A  1 290 ? -27.223 -10.379 44.528  1.00 18.25  ? 303 GLY A N   1 
ATOM   2206  C CA  . GLY A  1 290 ? -27.311 -11.441 43.525  1.00 19.06  ? 303 GLY A CA  1 
ATOM   2207  C C   . GLY A  1 290 ? -26.239 -11.356 42.457  1.00 19.36  ? 303 GLY A C   1 
ATOM   2208  O O   . GLY A  1 290 ? -25.152 -10.825 42.699  1.00 19.13  ? 303 GLY A O   1 
ATOM   2209  N N   . LYS A  1 291 ? -26.548 -11.894 41.278  1.00 19.62  ? 304 LYS A N   1 
ATOM   2210  C CA  . LYS A  1 291 ? -25.647 -11.840 40.129  1.00 20.41  ? 304 LYS A CA  1 
ATOM   2211  C C   . LYS A  1 291 ? -25.999 -10.640 39.249  1.00 20.27  ? 304 LYS A C   1 
ATOM   2212  O O   . LYS A  1 291 ? -27.002 -10.656 38.525  1.00 20.07  ? 304 LYS A O   1 
ATOM   2213  C CB  . LYS A  1 291 ? -25.701 -13.151 39.344  1.00 20.77  ? 304 LYS A CB  1 
ATOM   2214  C CG  . LYS A  1 291 ? -25.038 -14.322 40.064  1.00 24.94  ? 304 LYS A CG  1 
ATOM   2215  C CD  . LYS A  1 291 ? -25.671 -15.654 39.675  1.00 30.40  ? 304 LYS A CD  1 
ATOM   2216  C CE  . LYS A  1 291 ? -25.395 -16.719 40.731  1.00 32.37  ? 304 LYS A CE  1 
ATOM   2217  N NZ  . LYS A  1 291 ? -26.263 -17.914 40.552  1.00 33.41  ? 304 LYS A NZ  1 
ATOM   2218  N N   . CYS A  1 292 ? -25.160 -9.606  39.326  1.00 19.75  ? 305 CYS A N   1 
ATOM   2219  C CA  . CYS A  1 292 ? -25.479 -8.280  38.795  1.00 19.16  ? 305 CYS A CA  1 
ATOM   2220  C C   . CYS A  1 292 ? -24.369 -7.659  37.947  1.00 18.22  ? 305 CYS A C   1 
ATOM   2221  O O   . CYS A  1 292 ? -23.184 -7.927  38.173  1.00 17.47  ? 305 CYS A O   1 
ATOM   2222  C CB  . CYS A  1 292 ? -25.771 -7.319  39.951  1.00 19.56  ? 305 CYS A CB  1 
ATOM   2223  S SG  . CYS A  1 292 ? -27.160 -7.758  40.996  1.00 22.04  ? 305 CYS A SG  1 
ATOM   2224  N N   . PRO A  1 293 ? -24.752 -6.806  36.976  1.00 17.35  ? 306 PRO A N   1 
ATOM   2225  C CA  . PRO A  1 293 ? -23.773 -5.948  36.311  1.00 16.40  ? 306 PRO A CA  1 
ATOM   2226  C C   . PRO A  1 293 ? -23.197 -4.942  37.311  1.00 16.26  ? 306 PRO A C   1 
ATOM   2227  O O   . PRO A  1 293 ? -23.863 -4.617  38.297  1.00 16.27  ? 306 PRO A O   1 
ATOM   2228  C CB  . PRO A  1 293 ? -24.603 -5.218  35.250  1.00 16.23  ? 306 PRO A CB  1 
ATOM   2229  C CG  . PRO A  1 293 ? -25.860 -6.003  35.103  1.00 16.98  ? 306 PRO A CG  1 
ATOM   2230  C CD  . PRO A  1 293 ? -26.110 -6.629  36.427  1.00 16.95  ? 306 PRO A CD  1 
ATOM   2231  N N   . ARG A  1 294 ? -21.973 -4.468  37.070  1.00 15.85  ? 307 ARG A N   1 
ATOM   2232  C CA  . ARG A  1 294 ? -21.324 -3.511  37.969  1.00 15.26  ? 307 ARG A CA  1 
ATOM   2233  C C   . ARG A  1 294 ? -21.958 -2.134  37.827  1.00 15.23  ? 307 ARG A C   1 
ATOM   2234  O O   . ARG A  1 294 ? -22.238 -1.686  36.714  1.00 16.11  ? 307 ARG A O   1 
ATOM   2235  C CB  . ARG A  1 294 ? -19.818 -3.416  37.700  1.00 15.27  ? 307 ARG A CB  1 
ATOM   2236  C CG  . ARG A  1 294 ? -19.017 -4.693  37.948  1.00 19.03  ? 307 ARG A CG  1 
ATOM   2237  C CD  . ARG A  1 294 ? -18.924 -5.537  36.688  1.00 24.90  ? 307 ARG A CD  1 
ATOM   2238  N NE  . ARG A  1 294 ? -17.812 -6.486  36.724  1.00 30.48  ? 307 ARG A NE  1 
ATOM   2239  C CZ  . ARG A  1 294 ? -17.386 -7.183  35.671  1.00 32.47  ? 307 ARG A CZ  1 
ATOM   2240  N NH1 . ARG A  1 294 ? -17.974 -7.045  34.488  1.00 33.93  ? 307 ARG A NH1 1 
ATOM   2241  N NH2 . ARG A  1 294 ? -16.366 -8.019  35.800  1.00 33.49  ? 307 ARG A NH2 1 
ATOM   2242  N N   . TYR A  1 295 ? -22.184 -1.465  38.954  1.00 14.75  ? 308 TYR A N   1 
ATOM   2243  C CA  . TYR A  1 295 ? -22.783 -0.137  38.931  1.00 13.95  ? 308 TYR A CA  1 
ATOM   2244  C C   . TYR A  1 295 ? -21.814 0.886   38.360  1.00 13.13  ? 308 TYR A C   1 
ATOM   2245  O O   . TYR A  1 295 ? -20.639 0.902   38.723  1.00 13.52  ? 308 TYR A O   1 
ATOM   2246  C CB  . TYR A  1 295 ? -23.252 0.299   40.324  1.00 13.80  ? 308 TYR A CB  1 
ATOM   2247  C CG  . TYR A  1 295 ? -23.938 1.645   40.318  1.00 12.20  ? 308 TYR A CG  1 
ATOM   2248  C CD1 . TYR A  1 295 ? -25.279 1.763   39.944  1.00 13.20  ? 308 TYR A CD1 1 
ATOM   2249  C CD2 . TYR A  1 295 ? -23.246 2.805   40.659  1.00 11.76  ? 308 TYR A CD2 1 
ATOM   2250  C CE1 . TYR A  1 295 ? -25.919 3.001   39.924  1.00 9.91   ? 308 TYR A CE1 1 
ATOM   2251  C CE2 . TYR A  1 295 ? -23.874 4.048   40.639  1.00 13.25  ? 308 TYR A CE2 1 
ATOM   2252  C CZ  . TYR A  1 295 ? -25.211 4.137   40.272  1.00 11.78  ? 308 TYR A CZ  1 
ATOM   2253  O OH  . TYR A  1 295 ? -25.839 5.360   40.257  1.00 12.13  ? 308 TYR A OH  1 
ATOM   2254  N N   . VAL A  1 296 ? -22.324 1.722   37.458  1.00 11.53  ? 309 VAL A N   1 
ATOM   2255  C CA  . VAL A  1 296 ? -21.568 2.824   36.866  1.00 11.15  ? 309 VAL A CA  1 
ATOM   2256  C C   . VAL A  1 296 ? -22.411 4.102   36.936  1.00 12.46  ? 309 VAL A C   1 
ATOM   2257  O O   . VAL A  1 296 ? -23.637 4.027   37.037  1.00 13.57  ? 309 VAL A O   1 
ATOM   2258  C CB  . VAL A  1 296 ? -21.158 2.530   35.396  1.00 10.30  ? 309 VAL A CB  1 
ATOM   2259  C CG1 . VAL A  1 296 ? -20.227 1.322   35.318  1.00 7.78   ? 309 VAL A CG1 1 
ATOM   2260  C CG2 . VAL A  1 296 ? -22.381 2.337   34.509  1.00 9.24   ? 309 VAL A CG2 1 
ATOM   2261  N N   . LYS A  1 297 ? -21.773 5.269   36.893  1.00 12.23  ? 310 LYS A N   1 
ATOM   2262  C CA  . LYS A  1 297 ? -22.521 6.519   37.046  1.00 13.02  ? 310 LYS A CA  1 
ATOM   2263  C C   . LYS A  1 297 ? -23.025 7.092   35.719  1.00 13.51  ? 310 LYS A C   1 
ATOM   2264  O O   . LYS A  1 297 ? -23.860 7.995   35.706  1.00 13.45  ? 310 LYS A O   1 
ATOM   2265  C CB  . LYS A  1 297 ? -21.737 7.561   37.864  1.00 12.81  ? 310 LYS A CB  1 
ATOM   2266  C CG  . LYS A  1 297 ? -20.426 8.002   37.257  1.00 13.96  ? 310 LYS A CG  1 
ATOM   2267  C CD  . LYS A  1 297 ? -19.602 8.816   38.237  1.00 16.13  ? 310 LYS A CD  1 
ATOM   2268  C CE  . LYS A  1 297 ? -18.305 9.267   37.574  1.00 23.37  ? 310 LYS A CE  1 
ATOM   2269  N NZ  . LYS A  1 297 ? -17.349 9.882   38.536  1.00 27.12  ? 310 LYS A NZ  1 
ATOM   2270  N N   . GLN A  1 298 ? -22.524 6.547   34.613  1.00 14.18  ? 311 GLN A N   1 
ATOM   2271  C CA  . GLN A  1 298 ? -22.908 6.999   33.279  1.00 13.94  ? 311 GLN A CA  1 
ATOM   2272  C C   . GLN A  1 298 ? -24.222 6.360   32.858  1.00 14.76  ? 311 GLN A C   1 
ATOM   2273  O O   . GLN A  1 298 ? -24.448 5.173   33.102  1.00 14.90  ? 311 GLN A O   1 
ATOM   2274  C CB  . GLN A  1 298 ? -21.820 6.668   32.253  1.00 13.22  ? 311 GLN A CB  1 
ATOM   2275  C CG  . GLN A  1 298 ? -20.421 7.159   32.620  1.00 11.17  ? 311 GLN A CG  1 
ATOM   2276  C CD  . GLN A  1 298 ? -19.571 6.083   33.274  1.00 12.23  ? 311 GLN A CD  1 
ATOM   2277  O OE1 . GLN A  1 298 ? -20.045 5.323   34.119  1.00 11.89  ? 311 GLN A OE1 1 
ATOM   2278  N NE2 . GLN A  1 298 ? -18.304 6.012   32.878  1.00 8.73   ? 311 GLN A NE2 1 
ATOM   2279  N N   . LYS A  1 299 ? -25.080 7.152   32.220  1.00 15.58  ? 312 LYS A N   1 
ATOM   2280  C CA  . LYS A  1 299 ? -26.378 6.666   31.753  1.00 16.80  ? 312 LYS A CA  1 
ATOM   2281  C C   . LYS A  1 299 ? -26.259 5.771   30.520  1.00 16.19  ? 312 LYS A C   1 
ATOM   2282  O O   . LYS A  1 299 ? -27.023 4.821   30.358  1.00 17.39  ? 312 LYS A O   1 
ATOM   2283  C CB  . LYS A  1 299 ? -27.325 7.835   31.464  1.00 17.45  ? 312 LYS A CB  1 
ATOM   2284  C CG  . LYS A  1 299 ? -27.957 8.438   32.715  1.00 22.68  ? 312 LYS A CG  1 
ATOM   2285  C CD  . LYS A  1 299 ? -29.052 9.434   32.361  1.00 27.94  ? 312 LYS A CD  1 
ATOM   2286  C CE  . LYS A  1 299 ? -29.701 10.007  33.613  1.00 30.02  ? 312 LYS A CE  1 
ATOM   2287  N NZ  . LYS A  1 299 ? -30.756 11.000  33.268  1.00 31.10  ? 312 LYS A NZ  1 
ATOM   2288  N N   . SER A  1 300 ? -25.295 6.078   29.660  1.00 15.15  ? 313 SER A N   1 
ATOM   2289  C CA  . SER A  1 300 ? -25.145 5.380   28.389  1.00 14.24  ? 313 SER A CA  1 
ATOM   2290  C C   . SER A  1 300 ? -23.673 5.195   28.027  1.00 13.59  ? 313 SER A C   1 
ATOM   2291  O O   . SER A  1 300 ? -22.855 6.097   28.226  1.00 13.71  ? 313 SER A O   1 
ATOM   2292  C CB  . SER A  1 300 ? -25.868 6.157   27.282  1.00 13.85  ? 313 SER A CB  1 
ATOM   2293  O OG  . SER A  1 300 ? -25.922 5.423   26.073  1.00 14.12  ? 313 SER A OG  1 
ATOM   2294  N N   . LEU A  1 301 ? -23.341 4.012   27.515  1.00 12.53  ? 314 LEU A N   1 
ATOM   2295  C CA  . LEU A  1 301 ? -22.016 3.758   26.946  1.00 12.36  ? 314 LEU A CA  1 
ATOM   2296  C C   . LEU A  1 301 ? -22.148 2.898   25.696  1.00 11.49  ? 314 LEU A C   1 
ATOM   2297  O O   . LEU A  1 301 ? -22.058 1.672   25.756  1.00 11.59  ? 314 LEU A O   1 
ATOM   2298  C CB  . LEU A  1 301 ? -21.064 3.122   27.974  1.00 12.03  ? 314 LEU A CB  1 
ATOM   2299  C CG  . LEU A  1 301 ? -20.531 4.024   29.098  1.00 12.42  ? 314 LEU A CG  1 
ATOM   2300  C CD1 . LEU A  1 301 ? -19.768 3.211   30.125  1.00 11.79  ? 314 LEU A CD1 1 
ATOM   2301  C CD2 . LEU A  1 301 ? -19.667 5.168   28.565  1.00 11.67  ? 314 LEU A CD2 1 
ATOM   2302  N N   . LEU A  1 302 ? -22.380 3.557   24.564  1.00 10.95  ? 315 LEU A N   1 
ATOM   2303  C CA  . LEU A  1 302 ? -22.615 2.862   23.304  1.00 10.05  ? 315 LEU A CA  1 
ATOM   2304  C C   . LEU A  1 302 ? -21.324 2.267   22.751  1.00 9.20   ? 315 LEU A C   1 
ATOM   2305  O O   . LEU A  1 302 ? -20.323 2.966   22.596  1.00 9.05   ? 315 LEU A O   1 
ATOM   2306  C CB  . LEU A  1 302 ? -23.289 3.785   22.275  1.00 9.64   ? 315 LEU A CB  1 
ATOM   2307  C CG  . LEU A  1 302 ? -24.655 4.406   22.620  1.00 9.16   ? 315 LEU A CG  1 
ATOM   2308  C CD1 . LEU A  1 302 ? -25.125 5.318   21.506  1.00 6.84   ? 315 LEU A CD1 1 
ATOM   2309  C CD2 . LEU A  1 302 ? -25.722 3.354   22.910  1.00 9.90   ? 315 LEU A CD2 1 
ATOM   2310  N N   . LEU A  1 303 ? -21.367 0.966   22.477  1.00 8.83   ? 316 LEU A N   1 
ATOM   2311  C CA  . LEU A  1 303 ? -20.244 0.226   21.916  1.00 9.40   ? 316 LEU A CA  1 
ATOM   2312  C C   . LEU A  1 303 ? -20.452 0.014   20.416  1.00 9.68   ? 316 LEU A C   1 
ATOM   2313  O O   . LEU A  1 303 ? -21.466 -0.547  20.000  1.00 9.87   ? 316 LEU A O   1 
ATOM   2314  C CB  . LEU A  1 303 ? -20.111 -1.129  22.621  1.00 8.57   ? 316 LEU A CB  1 
ATOM   2315  C CG  . LEU A  1 303 ? -18.948 -2.025  22.195  1.00 9.42   ? 316 LEU A CG  1 
ATOM   2316  C CD1 . LEU A  1 303 ? -17.682 -1.657  22.953  1.00 10.29  ? 316 LEU A CD1 1 
ATOM   2317  C CD2 . LEU A  1 303 ? -19.297 -3.487  22.413  1.00 9.12   ? 316 LEU A CD2 1 
ATOM   2318  N N   . ALA A  1 304 ? -19.490 0.459   19.611  1.00 9.61   ? 317 ALA A N   1 
ATOM   2319  C CA  . ALA A  1 304 ? -19.574 0.329   18.156  1.00 9.56   ? 317 ALA A CA  1 
ATOM   2320  C C   . ALA A  1 304 ? -19.575 -1.133  17.724  1.00 10.25  ? 317 ALA A C   1 
ATOM   2321  O O   . ALA A  1 304 ? -18.681 -1.900  18.091  1.00 10.90  ? 317 ALA A O   1 
ATOM   2322  C CB  . ALA A  1 304 ? -18.433 1.085   17.482  1.00 8.43   ? 317 ALA A CB  1 
ATOM   2323  N N   . THR A  1 305 ? -20.597 -1.511  16.961  1.00 10.59  ? 318 THR A N   1 
ATOM   2324  C CA  . THR A  1 305 ? -20.678 -2.839  16.351  1.00 10.59  ? 318 THR A CA  1 
ATOM   2325  C C   . THR A  1 305 ? -20.690 -2.720  14.829  1.00 10.95  ? 318 THR A C   1 
ATOM   2326  O O   . THR A  1 305 ? -21.290 -3.542  14.128  1.00 11.68  ? 318 THR A O   1 
ATOM   2327  C CB  . THR A  1 305 ? -21.924 -3.611  16.816  1.00 10.09  ? 318 THR A CB  1 
ATOM   2328  O OG1 . THR A  1 305 ? -23.082 -2.778  16.684  1.00 9.91   ? 318 THR A OG1 1 
ATOM   2329  C CG2 . THR A  1 305 ? -21.768 -4.038  18.261  1.00 11.10  ? 318 THR A CG2 1 
ATOM   2330  N N   . GLY A  1 306 ? -20.026 -1.681  14.332  1.00 10.75  ? 319 GLY A N   1 
ATOM   2331  C CA  . GLY A  1 306 ? -19.920 -1.423  12.904  1.00 10.54  ? 319 GLY A CA  1 
ATOM   2332  C C   . GLY A  1 306 ? -18.828 -0.416  12.602  1.00 11.04  ? 319 GLY A C   1 
ATOM   2333  O O   . GLY A  1 306 ? -18.244 0.178   13.516  1.00 10.77  ? 319 GLY A O   1 
ATOM   2334  N N   . MET A  1 307 ? -18.561 -0.220  11.313  1.00 11.21  ? 320 MET A N   1 
ATOM   2335  C CA  . MET A  1 307 ? -17.542 0.727   10.855  1.00 10.23  ? 320 MET A CA  1 
ATOM   2336  C C   . MET A  1 307 ? -18.010 2.170   10.971  1.00 10.94  ? 320 MET A C   1 
ATOM   2337  O O   . MET A  1 307 ? -19.172 2.432   11.290  1.00 11.48  ? 320 MET A O   1 
ATOM   2338  C CB  . MET A  1 307 ? -17.158 0.433   9.402   1.00 9.88   ? 320 MET A CB  1 
ATOM   2339  C CG  . MET A  1 307 ? -18.220 0.795   8.375   1.00 6.58   ? 320 MET A CG  1 
ATOM   2340  S SD  . MET A  1 307 ? -17.808 0.248   6.711   1.00 7.90   ? 320 MET A SD  1 
ATOM   2341  C CE  . MET A  1 307 ? -18.041 -1.523  6.873   1.00 2.54   ? 320 MET A CE  1 
ATOM   2342  N N   . ARG A  1 308 ? -17.090 3.095   10.700  1.00 11.64  ? 321 ARG A N   1 
ATOM   2343  C CA  . ARG A  1 308 ? -17.395 4.514   10.562  1.00 11.54  ? 321 ARG A CA  1 
ATOM   2344  C C   . ARG A  1 308 ? -18.501 4.698   9.528   1.00 11.46  ? 321 ARG A C   1 
ATOM   2345  O O   . ARG A  1 308 ? -18.475 4.075   8.465   1.00 10.67  ? 321 ARG A O   1 
ATOM   2346  C CB  . ARG A  1 308 ? -16.140 5.268   10.113  1.00 11.76  ? 321 ARG A CB  1 
ATOM   2347  C CG  . ARG A  1 308 ? -15.938 6.614   10.782  1.00 13.36  ? 321 ARG A CG  1 
ATOM   2348  C CD  . ARG A  1 308 ? -16.585 7.739   10.022  1.00 18.81  ? 321 ARG A CD  1 
ATOM   2349  N NE  . ARG A  1 308 ? -16.890 8.862   10.906  1.00 25.23  ? 321 ARG A NE  1 
ATOM   2350  C CZ  . ARG A  1 308 ? -17.055 10.123  10.508  1.00 28.65  ? 321 ARG A CZ  1 
ATOM   2351  N NH1 . ARG A  1 308 ? -16.936 10.451  9.222   1.00 26.89  ? 321 ARG A NH1 1 
ATOM   2352  N NH2 . ARG A  1 308 ? -17.332 11.064  11.404  1.00 27.85  ? 321 ARG A NH2 1 
ATOM   2353  N N   . ASN A  1 309 ? -19.482 5.536   9.850   1.00 12.08  ? 322 ASN A N   1 
ATOM   2354  C CA  . ASN A  1 309 ? -20.560 5.817   8.913   1.00 12.28  ? 322 ASN A CA  1 
ATOM   2355  C C   . ASN A  1 309 ? -20.256 7.054   8.090   1.00 12.69  ? 322 ASN A C   1 
ATOM   2356  O O   . ASN A  1 309 ? -20.071 8.147   8.630   1.00 12.71  ? 322 ASN A O   1 
ATOM   2357  C CB  . ASN A  1 309 ? -21.910 5.950   9.620   1.00 11.82  ? 322 ASN A CB  1 
ATOM   2358  C CG  . ASN A  1 309 ? -23.084 5.788   8.665   1.00 13.67  ? 322 ASN A CG  1 
ATOM   2359  O OD1 . ASN A  1 309 ? -23.147 4.828   7.893   1.00 15.24  ? 322 ASN A OD1 1 
ATOM   2360  N ND2 . ASN A  1 309 ? -24.024 6.727   8.716   1.00 14.79  ? 322 ASN A ND2 1 
ATOM   2361  N N   . VAL A  1 310 ? -20.170 6.856   6.778   1.00 13.35  ? 323 VAL A N   1 
ATOM   2362  C CA  . VAL A  1 310 ? -19.970 7.944   5.832   1.00 13.68  ? 323 VAL A CA  1 
ATOM   2363  C C   . VAL A  1 310 ? -21.113 7.907   4.815   1.00 15.38  ? 323 VAL A C   1 
ATOM   2364  O O   . VAL A  1 310 ? -21.010 7.241   3.781   1.00 14.78  ? 323 VAL A O   1 
ATOM   2365  C CB  . VAL A  1 310 ? -18.599 7.851   5.116   1.00 13.43  ? 323 VAL A CB  1 
ATOM   2366  C CG1 . VAL A  1 310 ? -18.285 9.160   4.396   1.00 11.03  ? 323 VAL A CG1 1 
ATOM   2367  C CG2 . VAL A  1 310 ? -17.486 7.513   6.108   1.00 12.76  ? 323 VAL A CG2 1 
ATOM   2368  N N   . PRO A  1 311 ? -22.218 8.614   5.116   1.00 17.46  ? 324 PRO A N   1 
ATOM   2369  C CA  . PRO A  1 311 ? -23.377 8.629   4.224   1.00 19.40  ? 324 PRO A CA  1 
ATOM   2370  C C   . PRO A  1 311 ? -23.057 9.239   2.863   1.00 21.73  ? 324 PRO A C   1 
ATOM   2371  O O   . PRO A  1 311 ? -22.128 10.040  2.745   1.00 21.71  ? 324 PRO A O   1 
ATOM   2372  C CB  . PRO A  1 311 ? -24.393 9.497   4.976   1.00 18.83  ? 324 PRO A CB  1 
ATOM   2373  C CG  . PRO A  1 311 ? -23.591 10.292  5.943   1.00 18.30  ? 324 PRO A CG  1 
ATOM   2374  C CD  . PRO A  1 311 ? -22.452 9.413   6.333   1.00 17.59  ? 324 PRO A CD  1 
ATOM   2375  N N   . GLU A  1 312 ? -23.829 8.848   1.853   1.00 24.81  ? 325 GLU A N   1 
ATOM   2376  C CA  . GLU A  1 312 ? -23.656 9.333   0.485   1.00 27.88  ? 325 GLU A CA  1 
ATOM   2377  C C   . GLU A  1 312 ? -23.960 10.823  0.353   1.00 29.93  ? 325 GLU A C   1 
ATOM   2378  O O   . GLU A  1 312 ? -24.721 11.383  1.149   1.00 30.16  ? 325 GLU A O   1 
ATOM   2379  C CB  . GLU A  1 312 ? -24.550 8.544   -0.474  1.00 27.95  ? 325 GLU A CB  1 
ATOM   2380  C CG  . GLU A  1 312 ? -24.212 7.064   -0.583  1.00 29.53  ? 325 GLU A CG  1 
ATOM   2381  C CD  . GLU A  1 312 ? -24.906 6.387   -1.753  1.00 32.16  ? 325 GLU A CD  1 
ATOM   2382  O OE1 . GLU A  1 312 ? -25.461 5.287   -1.556  1.00 34.67  ? 325 GLU A OE1 1 
ATOM   2383  O OE2 . GLU A  1 312 ? -24.899 6.951   -2.868  1.00 31.47  ? 325 GLU A OE2 1 
ATOM   2384  N N   . LYS A  1 313 ? -23.354 11.455  -0.652  1.00 32.55  ? 326 LYS A N   1 
ATOM   2385  C CA  . LYS A  1 313 ? -23.651 12.847  -0.998  1.00 35.13  ? 326 LYS A CA  1 
ATOM   2386  C C   . LYS A  1 313 ? -24.290 12.951  -2.381  1.00 35.55  ? 326 LYS A C   1 
ATOM   2387  O O   . LYS A  1 313 ? -25.513 12.871  -2.516  1.00 36.01  ? 326 LYS A O   1 
ATOM   2388  C CB  . LYS A  1 313 ? -22.391 13.717  -0.933  1.00 36.06  ? 326 LYS A CB  1 
ATOM   2389  C CG  . LYS A  1 313 ? -22.016 14.156  0.476   1.00 40.45  ? 326 LYS A CG  1 
ATOM   2390  C CD  . LYS A  1 313 ? -21.055 15.337  0.455   1.00 45.15  ? 326 LYS A CD  1 
ATOM   2391  C CE  . LYS A  1 313 ? -20.817 15.869  1.862   1.00 46.82  ? 326 LYS A CE  1 
ATOM   2392  N NZ  . LYS A  1 313 ? -19.940 17.073  1.860   1.00 48.22  ? 326 LYS A NZ  1 
ATOM   2393  N N   . GLY B  2 1   ? -9.748  6.942   10.140  1.00 13.95  ? 1   GLY B N   1 
ATOM   2394  C CA  . GLY B  2 1   ? -9.209  5.594   10.489  1.00 14.67  ? 1   GLY B CA  1 
ATOM   2395  C C   . GLY B  2 1   ? -7.718  5.456   10.231  1.00 14.78  ? 1   GLY B C   1 
ATOM   2396  O O   . GLY B  2 1   ? -7.152  6.156   9.388   1.00 14.89  ? 1   GLY B O   1 
ATOM   2397  N N   . LEU B  2 2   ? -7.088  4.535   10.957  1.00 14.90  ? 2   LEU B N   1 
ATOM   2398  C CA  . LEU B  2 2   ? -5.643  4.312   10.877  1.00 14.69  ? 2   LEU B CA  1 
ATOM   2399  C C   . LEU B  2 2   ? -5.141  3.874   9.502   1.00 14.13  ? 2   LEU B C   1 
ATOM   2400  O O   . LEU B  2 2   ? -3.957  4.014   9.203   1.00 13.63  ? 2   LEU B O   1 
ATOM   2401  C CB  . LEU B  2 2   ? -5.210  3.275   11.914  1.00 14.54  ? 2   LEU B CB  1 
ATOM   2402  C CG  . LEU B  2 2   ? -5.035  3.709   13.364  1.00 15.41  ? 2   LEU B CG  1 
ATOM   2403  C CD1 . LEU B  2 2   ? -4.698  2.499   14.226  1.00 13.31  ? 2   LEU B CD1 1 
ATOM   2404  C CD2 . LEU B  2 2   ? -3.968  4.792   13.489  1.00 13.09  ? 2   LEU B CD2 1 
ATOM   2405  N N   . PHE B  2 3   ? -6.040  3.350   8.674   1.00 14.05  ? 3   PHE B N   1 
ATOM   2406  C CA  . PHE B  2 3   ? -5.649  2.713   7.417   1.00 14.38  ? 3   PHE B CA  1 
ATOM   2407  C C   . PHE B  2 3   ? -6.014  3.515   6.172   1.00 15.13  ? 3   PHE B C   1 
ATOM   2408  O O   . PHE B  2 3   ? -5.705  3.108   5.048   1.00 15.53  ? 3   PHE B O   1 
ATOM   2409  C CB  . PHE B  2 3   ? -6.181  1.279   7.369   1.00 13.80  ? 3   PHE B CB  1 
ATOM   2410  C CG  . PHE B  2 3   ? -5.561  0.393   8.405   1.00 13.16  ? 3   PHE B CG  1 
ATOM   2411  C CD1 . PHE B  2 3   ? -6.095  0.321   9.690   1.00 14.69  ? 3   PHE B CD1 1 
ATOM   2412  C CD2 . PHE B  2 3   ? -4.412  -0.329  8.117   1.00 12.40  ? 3   PHE B CD2 1 
ATOM   2413  C CE1 . PHE B  2 3   ? -5.507  -0.479  10.664  1.00 12.57  ? 3   PHE B CE1 1 
ATOM   2414  C CE2 . PHE B  2 3   ? -3.816  -1.129  9.082   1.00 12.29  ? 3   PHE B CE2 1 
ATOM   2415  C CZ  . PHE B  2 3   ? -4.366  -1.205  10.357  1.00 13.14  ? 3   PHE B CZ  1 
ATOM   2416  N N   . GLY B  2 4   ? -6.664  4.656   6.385   1.00 15.83  ? 4   GLY B N   1 
ATOM   2417  C CA  . GLY B  2 4   ? -6.890  5.641   5.333   1.00 15.57  ? 4   GLY B CA  1 
ATOM   2418  C C   . GLY B  2 4   ? -7.846  5.272   4.217   1.00 15.26  ? 4   GLY B C   1 
ATOM   2419  O O   . GLY B  2 4   ? -7.935  5.993   3.223   1.00 15.88  ? 4   GLY B O   1 
ATOM   2420  N N   . ALA B  2 5   ? -8.564  4.162   4.365   1.00 13.79  ? 5   ALA B N   1 
ATOM   2421  C CA  . ALA B  2 5   ? -9.553  3.784   3.366   1.00 13.47  ? 5   ALA B CA  1 
ATOM   2422  C C   . ALA B  2 5   ? -10.935 4.355   3.712   1.00 13.23  ? 5   ALA B C   1 
ATOM   2423  O O   . ALA B  2 5   ? -11.392 5.305   3.074   1.00 13.43  ? 5   ALA B O   1 
ATOM   2424  C CB  . ALA B  2 5   ? -9.592  2.274   3.185   1.00 13.71  ? 5   ALA B CB  1 
ATOM   2425  N N   . ILE B  2 6   ? -11.586 3.782   4.723   1.00 12.61  ? 6   ILE B N   1 
ATOM   2426  C CA  . ILE B  2 6   ? -12.874 4.281   5.203   1.00 11.74  ? 6   ILE B CA  1 
ATOM   2427  C C   . ILE B  2 6   ? -12.685 5.681   5.782   1.00 11.74  ? 6   ILE B C   1 
ATOM   2428  O O   . ILE B  2 6   ? -11.820 5.886   6.641   1.00 12.49  ? 6   ILE B O   1 
ATOM   2429  C CB  . ILE B  2 6   ? -13.512 3.342   6.264   1.00 11.21  ? 6   ILE B CB  1 
ATOM   2430  C CG1 . ILE B  2 6   ? -13.612 1.908   5.728   1.00 9.98   ? 6   ILE B CG1 1 
ATOM   2431  C CG2 . ILE B  2 6   ? -14.889 3.854   6.673   1.00 10.73  ? 6   ILE B CG2 1 
ATOM   2432  C CD1 . ILE B  2 6   ? -14.277 0.922   6.670   1.00 3.69   ? 6   ILE B CD1 1 
ATOM   2433  N N   . ALA B  2 7   ? -13.493 6.629   5.300   1.00 10.91  ? 7   ALA B N   1 
ATOM   2434  C CA  . ALA B  2 7   ? -13.345 8.054   5.606   1.00 10.68  ? 7   ALA B CA  1 
ATOM   2435  C C   . ALA B  2 7   ? -11.978 8.583   5.157   1.00 10.83  ? 7   ALA B C   1 
ATOM   2436  O O   . ALA B  2 7   ? -11.434 9.523   5.739   1.00 10.77  ? 7   ALA B O   1 
ATOM   2437  C CB  . ALA B  2 7   ? -13.585 8.329   7.096   1.00 10.45  ? 7   ALA B CB  1 
ATOM   2438  N N   . GLY B  2 8   ? -11.434 7.966   4.114   1.00 10.89  ? 8   GLY B N   1 
ATOM   2439  C CA  . GLY B  2 8   ? -10.127 8.328   3.590   1.00 11.13  ? 8   GLY B CA  1 
ATOM   2440  C C   . GLY B  2 8   ? -10.204 8.479   2.091   1.00 12.03  ? 8   GLY B C   1 
ATOM   2441  O O   . GLY B  2 8   ? -10.988 9.291   1.595   1.00 13.07  ? 8   GLY B O   1 
ATOM   2442  N N   . PHE B  2 9   ? -9.411  7.692   1.363   1.00 11.76  ? 9   PHE B N   1 
ATOM   2443  C CA  . PHE B  2 9   ? -9.364  7.822   -0.093  1.00 11.33  ? 9   PHE B CA  1 
ATOM   2444  C C   . PHE B  2 9   ? -10.648 7.357   -0.768  1.00 11.63  ? 9   PHE B C   1 
ATOM   2445  O O   . PHE B  2 9   ? -10.958 7.784   -1.881  1.00 11.84  ? 9   PHE B O   1 
ATOM   2446  C CB  . PHE B  2 9   ? -8.100  7.202   -0.712  1.00 10.82  ? 9   PHE B CB  1 
ATOM   2447  C CG  . PHE B  2 9   ? -8.006  5.708   -0.582  1.00 12.03  ? 9   PHE B CG  1 
ATOM   2448  C CD1 . PHE B  2 9   ? -8.622  4.872   -1.512  1.00 12.24  ? 9   PHE B CD1 1 
ATOM   2449  C CD2 . PHE B  2 9   ? -7.265  5.135   0.446   1.00 7.87   ? 9   PHE B CD2 1 
ATOM   2450  C CE1 . PHE B  2 9   ? -8.523  3.484   -1.398  1.00 13.83  ? 9   PHE B CE1 1 
ATOM   2451  C CE2 . PHE B  2 9   ? -7.157  3.752   0.568   1.00 8.98   ? 9   PHE B CE2 1 
ATOM   2452  C CZ  . PHE B  2 9   ? -7.788  2.923   -0.356  1.00 10.47  ? 9   PHE B CZ  1 
ATOM   2453  N N   . ILE B  2 10  ? -11.390 6.486   -0.088  1.00 12.14  ? 10  ILE B N   1 
ATOM   2454  C CA  . ILE B  2 10  ? -12.748 6.155   -0.512  1.00 13.53  ? 10  ILE B CA  1 
ATOM   2455  C C   . ILE B  2 10  ? -13.687 7.240   0.015   1.00 14.96  ? 10  ILE B C   1 
ATOM   2456  O O   . ILE B  2 10  ? -13.904 7.354   1.223   1.00 15.98  ? 10  ILE B O   1 
ATOM   2457  C CB  . ILE B  2 10  ? -13.182 4.745   -0.055  1.00 13.12  ? 10  ILE B CB  1 
ATOM   2458  C CG1 . ILE B  2 10  ? -12.218 3.695   -0.628  1.00 14.34  ? 10  ILE B CG1 1 
ATOM   2459  C CG2 . ILE B  2 10  ? -14.619 4.459   -0.489  1.00 13.19  ? 10  ILE B CG2 1 
ATOM   2460  C CD1 . ILE B  2 10  ? -12.504 2.264   -0.225  1.00 13.21  ? 10  ILE B CD1 1 
ATOM   2461  N N   . GLU B  2 11  ? -14.217 8.040   -0.910  1.00 15.77  ? 11  GLU B N   1 
ATOM   2462  C CA  . GLU B  2 11  ? -15.006 9.232   -0.596  1.00 17.12  ? 11  GLU B CA  1 
ATOM   2463  C C   . GLU B  2 11  ? -16.106 8.982   0.436   1.00 16.56  ? 11  GLU B C   1 
ATOM   2464  O O   . GLU B  2 11  ? -16.160 9.658   1.465   1.00 16.93  ? 11  GLU B O   1 
ATOM   2465  C CB  . GLU B  2 11  ? -15.615 9.809   -1.880  1.00 18.63  ? 11  GLU B CB  1 
ATOM   2466  C CG  . GLU B  2 11  ? -16.184 11.223  -1.747  1.00 25.17  ? 11  GLU B CG  1 
ATOM   2467  C CD  . GLU B  2 11  ? -15.221 12.306  -2.222  1.00 34.16  ? 11  GLU B CD  1 
ATOM   2468  O OE1 . GLU B  2 11  ? -13.987 12.134  -2.073  1.00 38.43  ? 11  GLU B OE1 1 
ATOM   2469  O OE2 . GLU B  2 11  ? -15.704 13.337  -2.743  1.00 33.94  ? 11  GLU B OE2 1 
ATOM   2470  N N   . ASN B  2 12  ? -16.977 8.014   0.155   1.00 15.64  ? 12  ASN B N   1 
ATOM   2471  C CA  . ASN B  2 12  ? -18.134 7.735   1.007   1.00 14.88  ? 12  ASN B CA  1 
ATOM   2472  C C   . ASN B  2 12  ? -18.629 6.302   0.888   1.00 14.44  ? 12  ASN B C   1 
ATOM   2473  O O   . ASN B  2 12  ? -18.215 5.568   -0.009  1.00 15.04  ? 12  ASN B O   1 
ATOM   2474  C CB  . ASN B  2 12  ? -19.277 8.721   0.711   1.00 14.97  ? 12  ASN B CB  1 
ATOM   2475  C CG  . ASN B  2 12  ? -19.591 8.833   -0.771  1.00 13.58  ? 12  ASN B CG  1 
ATOM   2476  O OD1 . ASN B  2 12  ? -19.268 9.836   -1.405  1.00 13.46  ? 12  ASN B OD1 1 
ATOM   2477  N ND2 . ASN B  2 12  ? -20.214 7.801   -1.330  1.00 12.78  ? 12  ASN B ND2 1 
ATOM   2478  N N   . GLY B  2 13  ? -19.512 5.911   1.800   1.00 13.80  ? 13  GLY B N   1 
ATOM   2479  C CA  . GLY B  2 13  ? -20.091 4.574   1.784   1.00 14.57  ? 13  GLY B CA  1 
ATOM   2480  C C   . GLY B  2 13  ? -21.170 4.431   0.728   1.00 15.54  ? 13  GLY B C   1 
ATOM   2481  O O   . GLY B  2 13  ? -21.601 5.422   0.133   1.00 16.34  ? 13  GLY B O   1 
ATOM   2482  N N   . TRP B  2 14  ? -21.598 3.194   0.486   1.00 15.36  ? 14  TRP B N   1 
ATOM   2483  C CA  . TRP B  2 14  ? -22.686 2.920   -0.443  1.00 14.42  ? 14  TRP B CA  1 
ATOM   2484  C C   . TRP B  2 14  ? -23.917 2.481   0.338   1.00 15.09  ? 14  TRP B C   1 
ATOM   2485  O O   . TRP B  2 14  ? -23.949 1.378   0.888   1.00 15.59  ? 14  TRP B O   1 
ATOM   2486  C CB  . TRP B  2 14  ? -22.288 1.838   -1.449  1.00 14.06  ? 14  TRP B CB  1 
ATOM   2487  C CG  . TRP B  2 14  ? -21.123 2.183   -2.337  1.00 12.94  ? 14  TRP B CG  1 
ATOM   2488  C CD1 . TRP B  2 14  ? -20.779 3.422   -2.808  1.00 13.10  ? 14  TRP B CD1 1 
ATOM   2489  C CD2 . TRP B  2 14  ? -20.169 1.267   -2.893  1.00 12.11  ? 14  TRP B CD2 1 
ATOM   2490  N NE1 . TRP B  2 14  ? -19.660 3.335   -3.606  1.00 12.12  ? 14  TRP B NE1 1 
ATOM   2491  C CE2 . TRP B  2 14  ? -19.267 2.024   -3.678  1.00 12.40  ? 14  TRP B CE2 1 
ATOM   2492  C CE3 . TRP B  2 14  ? -19.980 -0.120  -2.794  1.00 11.14  ? 14  TRP B CE3 1 
ATOM   2493  C CZ2 . TRP B  2 14  ? -18.196 1.440   -4.363  1.00 11.74  ? 14  TRP B CZ2 1 
ATOM   2494  C CZ3 . TRP B  2 14  ? -18.915 -0.702  -3.479  1.00 8.68   ? 14  TRP B CZ3 1 
ATOM   2495  C CH2 . TRP B  2 14  ? -18.039 0.079   -4.253  1.00 11.78  ? 14  TRP B CH2 1 
ATOM   2496  N N   . GLU B  2 15  ? -24.924 3.350   0.392   1.00 15.44  ? 15  GLU B N   1 
ATOM   2497  C CA  . GLU B  2 15  ? -26.159 3.075   1.134   1.00 15.55  ? 15  GLU B CA  1 
ATOM   2498  C C   . GLU B  2 15  ? -26.965 1.923   0.516   1.00 15.70  ? 15  GLU B C   1 
ATOM   2499  O O   . GLU B  2 15  ? -27.786 1.293   1.191   1.00 15.26  ? 15  GLU B O   1 
ATOM   2500  C CB  . GLU B  2 15  ? -27.012 4.345   1.268   1.00 15.18  ? 15  GLU B CB  1 
ATOM   2501  C CG  . GLU B  2 15  ? -26.383 5.424   2.157   1.00 16.36  ? 15  GLU B CG  1 
ATOM   2502  C CD  . GLU B  2 15  ? -27.232 6.690   2.298   1.00 17.79  ? 15  GLU B CD  1 
ATOM   2503  O OE1 . GLU B  2 15  ? -28.480 6.603   2.311   1.00 16.59  ? 15  GLU B OE1 1 
ATOM   2504  O OE2 . GLU B  2 15  ? -26.641 7.783   2.416   1.00 16.69  ? 15  GLU B OE2 1 
ATOM   2505  N N   . GLY B  2 16  ? -26.707 1.645   -0.759  1.00 15.77  ? 16  GLY B N   1 
ATOM   2506  C CA  . GLY B  2 16  ? -27.392 0.579   -1.482  1.00 16.79  ? 16  GLY B CA  1 
ATOM   2507  C C   . GLY B  2 16  ? -26.762 -0.796  -1.339  1.00 18.05  ? 16  GLY B C   1 
ATOM   2508  O O   . GLY B  2 16  ? -27.304 -1.779  -1.847  1.00 18.12  ? 16  GLY B O   1 
ATOM   2509  N N   . LEU B  2 17  ? -25.616 -0.870  -0.659  1.00 18.67  ? 17  LEU B N   1 
ATOM   2510  C CA  . LEU B  2 17  ? -24.961 -2.151  -0.385  1.00 18.93  ? 17  LEU B CA  1 
ATOM   2511  C C   . LEU B  2 17  ? -25.544 -2.778  0.885   1.00 19.81  ? 17  LEU B C   1 
ATOM   2512  O O   . LEU B  2 17  ? -24.966 -2.686  1.973   1.00 19.53  ? 17  LEU B O   1 
ATOM   2513  C CB  . LEU B  2 17  ? -23.438 -1.983  -0.286  1.00 18.56  ? 17  LEU B CB  1 
ATOM   2514  C CG  . LEU B  2 17  ? -22.554 -3.237  -0.186  1.00 18.59  ? 17  LEU B CG  1 
ATOM   2515  C CD1 . LEU B  2 17  ? -22.608 -4.074  -1.456  1.00 19.81  ? 17  LEU B CD1 1 
ATOM   2516  C CD2 . LEU B  2 17  ? -21.115 -2.865  0.133   1.00 17.98  ? 17  LEU B CD2 1 
ATOM   2517  N N   . ILE B  2 18  ? -26.707 -3.407  0.735   1.00 20.91  ? 18  ILE B N   1 
ATOM   2518  C CA  . ILE B  2 18  ? -27.414 -4.003  1.874   1.00 21.73  ? 18  ILE B CA  1 
ATOM   2519  C C   . ILE B  2 18  ? -27.048 -5.476  2.076   1.00 21.63  ? 18  ILE B C   1 
ATOM   2520  O O   . ILE B  2 18  ? -27.408 -6.081  3.090   1.00 21.36  ? 18  ILE B O   1 
ATOM   2521  C CB  . ILE B  2 18  ? -28.962 -3.829  1.771   1.00 21.96  ? 18  ILE B CB  1 
ATOM   2522  C CG1 . ILE B  2 18  ? -29.512 -4.477  0.490   1.00 22.35  ? 18  ILE B CG1 1 
ATOM   2523  C CG2 . ILE B  2 18  ? -29.343 -2.345  1.869   1.00 21.19  ? 18  ILE B CG2 1 
ATOM   2524  C CD1 . ILE B  2 18  ? -30.989 -4.865  0.565   1.00 21.83  ? 18  ILE B CD1 1 
ATOM   2525  N N   . ASN B  2 19  ? -26.320 -6.032  1.110   1.00 21.33  ? 19  ASN B N   1 
ATOM   2526  C CA  . ASN B  2 19  ? -25.963 -7.450  1.114   1.00 21.13  ? 19  ASN B CA  1 
ATOM   2527  C C   . ASN B  2 19  ? -24.625 -7.767  1.804   1.00 19.87  ? 19  ASN B C   1 
ATOM   2528  O O   . ASN B  2 19  ? -24.204 -8.925  1.846   1.00 19.77  ? 19  ASN B O   1 
ATOM   2529  C CB  . ASN B  2 19  ? -26.047 -8.060  -0.310  1.00 21.90  ? 19  ASN B CB  1 
ATOM   2530  C CG  . ASN B  2 19  ? -25.519 -7.120  -1.420  1.00 25.77  ? 19  ASN B CG  1 
ATOM   2531  O OD1 . ASN B  2 19  ? -25.690 -5.899  -1.374  1.00 27.26  ? 19  ASN B OD1 1 
ATOM   2532  N ND2 . ASN B  2 19  ? -24.900 -7.711  -2.438  1.00 30.56  ? 19  ASN B ND2 1 
ATOM   2533  N N   . GLY B  2 20  ? -23.977 -6.742  2.358   1.00 18.56  ? 20  GLY B N   1 
ATOM   2534  C CA  . GLY B  2 20  ? -22.699 -6.910  3.052   1.00 16.96  ? 20  GLY B CA  1 
ATOM   2535  C C   . GLY B  2 20  ? -22.025 -5.620  3.498   1.00 16.71  ? 20  GLY B C   1 
ATOM   2536  O O   . GLY B  2 20  ? -22.553 -4.526  3.293   1.00 16.77  ? 20  GLY B O   1 
ATOM   2537  N N   . TRP B  2 21  ? -20.848 -5.759  4.107   1.00 16.14  ? 21  TRP B N   1 
ATOM   2538  C CA  . TRP B  2 21  ? -20.083 -4.627  4.645   1.00 14.79  ? 21  TRP B CA  1 
ATOM   2539  C C   . TRP B  2 21  ? -19.162 -4.008  3.603   1.00 13.85  ? 21  TRP B C   1 
ATOM   2540  O O   . TRP B  2 21  ? -18.991 -2.794  3.562   1.00 13.71  ? 21  TRP B O   1 
ATOM   2541  C CB  . TRP B  2 21  ? -19.244 -5.073  5.846   1.00 14.52  ? 21  TRP B CB  1 
ATOM   2542  C CG  . TRP B  2 21  ? -20.022 -5.299  7.121   1.00 15.59  ? 21  TRP B CG  1 
ATOM   2543  C CD1 . TRP B  2 21  ? -21.291 -5.805  7.241   1.00 14.85  ? 21  TRP B CD1 1 
ATOM   2544  C CD2 . TRP B  2 21  ? -19.561 -5.058  8.455   1.00 15.51  ? 21  TRP B CD2 1 
ATOM   2545  N NE1 . TRP B  2 21  ? -21.650 -5.874  8.564   1.00 15.43  ? 21  TRP B NE1 1 
ATOM   2546  C CE2 . TRP B  2 21  ? -20.607 -5.425  9.331   1.00 16.99  ? 21  TRP B CE2 1 
ATOM   2547  C CE3 . TRP B  2 21  ? -18.368 -4.561  8.996   1.00 16.97  ? 21  TRP B CE3 1 
ATOM   2548  C CZ2 . TRP B  2 21  ? -20.495 -5.310  10.722  1.00 19.33  ? 21  TRP B CZ2 1 
ATOM   2549  C CZ3 . TRP B  2 21  ? -18.256 -4.447  10.378  1.00 17.04  ? 21  TRP B CZ3 1 
ATOM   2550  C CH2 . TRP B  2 21  ? -19.314 -4.823  11.225  1.00 18.49  ? 21  TRP B CH2 1 
ATOM   2551  N N   . TYR B  2 22  ? -18.562 -4.855  2.773   1.00 13.16  ? 22  TYR B N   1 
ATOM   2552  C CA  . TYR B  2 22  ? -17.622 -4.411  1.752   1.00 12.37  ? 22  TYR B CA  1 
ATOM   2553  C C   . TYR B  2 22  ? -18.070 -4.916  0.394   1.00 12.95  ? 22  TYR B C   1 
ATOM   2554  O O   . TYR B  2 22  ? -18.733 -5.955  0.305   1.00 13.58  ? 22  TYR B O   1 
ATOM   2555  C CB  . TYR B  2 22  ? -16.218 -4.912  2.075   1.00 11.88  ? 22  TYR B CB  1 
ATOM   2556  C CG  . TYR B  2 22  ? -15.770 -4.573  3.477   1.00 9.72   ? 22  TYR B CG  1 
ATOM   2557  C CD1 . TYR B  2 22  ? -15.825 -5.525  4.491   1.00 8.44   ? 22  TYR B CD1 1 
ATOM   2558  C CD2 . TYR B  2 22  ? -15.304 -3.295  3.794   1.00 5.89   ? 22  TYR B CD2 1 
ATOM   2559  C CE1 . TYR B  2 22  ? -15.417 -5.220  5.779   1.00 9.50   ? 22  TYR B CE1 1 
ATOM   2560  C CE2 . TYR B  2 22  ? -14.896 -2.979  5.080   1.00 4.64   ? 22  TYR B CE2 1 
ATOM   2561  C CZ  . TYR B  2 22  ? -14.956 -3.946  6.067   1.00 6.53   ? 22  TYR B CZ  1 
ATOM   2562  O OH  . TYR B  2 22  ? -14.556 -3.650  7.347   1.00 7.13   ? 22  TYR B OH  1 
ATOM   2563  N N   . GLY B  2 23  ? -17.718 -4.185  -0.662  1.00 12.57  ? 23  GLY B N   1 
ATOM   2564  C CA  . GLY B  2 23  ? -18.247 -4.492  -1.983  1.00 12.82  ? 23  GLY B CA  1 
ATOM   2565  C C   . GLY B  2 23  ? -17.450 -4.036  -3.187  1.00 13.15  ? 23  GLY B C   1 
ATOM   2566  O O   . GLY B  2 23  ? -16.434 -3.345  -3.060  1.00 13.33  ? 23  GLY B O   1 
ATOM   2567  N N   . PHE B  2 24  ? -17.934 -4.443  -4.359  1.00 13.10  ? 24  PHE B N   1 
ATOM   2568  C CA  . PHE B  2 24  ? -17.344 -4.085  -5.640  1.00 13.78  ? 24  PHE B CA  1 
ATOM   2569  C C   . PHE B  2 24  ? -18.392 -3.375  -6.473  1.00 14.47  ? 24  PHE B C   1 
ATOM   2570  O O   . PHE B  2 24  ? -19.502 -3.881  -6.638  1.00 14.95  ? 24  PHE B O   1 
ATOM   2571  C CB  . PHE B  2 24  ? -16.915 -5.334  -6.421  1.00 13.44  ? 24  PHE B CB  1 
ATOM   2572  C CG  . PHE B  2 24  ? -15.913 -6.201  -5.717  1.00 13.04  ? 24  PHE B CG  1 
ATOM   2573  C CD1 . PHE B  2 24  ? -16.327 -7.184  -4.823  1.00 12.27  ? 24  PHE B CD1 1 
ATOM   2574  C CD2 . PHE B  2 24  ? -14.557 -6.069  -5.982  1.00 12.55  ? 24  PHE B CD2 1 
ATOM   2575  C CE1 . PHE B  2 24  ? -15.404 -8.001  -4.188  1.00 11.48  ? 24  PHE B CE1 1 
ATOM   2576  C CE2 . PHE B  2 24  ? -13.626 -6.883  -5.349  1.00 12.62  ? 24  PHE B CE2 1 
ATOM   2577  C CZ  . PHE B  2 24  ? -14.050 -7.850  -4.451  1.00 12.05  ? 24  PHE B CZ  1 
ATOM   2578  N N   . ARG B  2 25  ? -18.043 -2.212  -7.009  1.00 15.24  ? 25  ARG B N   1 
ATOM   2579  C CA  . ARG B  2 25  ? -18.899 -1.552  -7.986  1.00 16.11  ? 25  ARG B CA  1 
ATOM   2580  C C   . ARG B  2 25  ? -18.131 -1.381  -9.292  1.00 16.84  ? 25  ARG B C   1 
ATOM   2581  O O   . ARG B  2 25  ? -17.136 -0.658  -9.349  1.00 16.68  ? 25  ARG B O   1 
ATOM   2582  C CB  . ARG B  2 25  ? -19.422 -0.218  -7.450  1.00 15.76  ? 25  ARG B CB  1 
ATOM   2583  C CG  . ARG B  2 25  ? -20.491 0.419   -8.315  1.00 15.79  ? 25  ARG B CG  1 
ATOM   2584  C CD  . ARG B  2 25  ? -21.182 1.556   -7.591  1.00 13.77  ? 25  ARG B CD  1 
ATOM   2585  N NE  . ARG B  2 25  ? -22.172 1.084   -6.626  1.00 10.41  ? 25  ARG B NE  1 
ATOM   2586  C CZ  . ARG B  2 25  ? -22.769 1.857   -5.723  1.00 9.90   ? 25  ARG B CZ  1 
ATOM   2587  N NH1 . ARG B  2 25  ? -22.479 3.153   -5.644  1.00 6.61   ? 25  ARG B NH1 1 
ATOM   2588  N NH2 . ARG B  2 25  ? -23.656 1.331   -4.889  1.00 10.08  ? 25  ARG B NH2 1 
ATOM   2589  N N   . HIS B  2 26  ? -18.595 -2.067  -10.333 1.00 18.05  ? 26  HIS B N   1 
ATOM   2590  C CA  . HIS B  2 26  ? -17.921 -2.067  -11.629 1.00 18.98  ? 26  HIS B CA  1 
ATOM   2591  C C   . HIS B  2 26  ? -18.674 -1.254  -12.679 1.00 19.30  ? 26  HIS B C   1 
ATOM   2592  O O   . HIS B  2 26  ? -19.889 -1.073  -12.587 1.00 19.15  ? 26  HIS B O   1 
ATOM   2593  C CB  . HIS B  2 26  ? -17.713 -3.502  -12.128 1.00 19.01  ? 26  HIS B CB  1 
ATOM   2594  C CG  . HIS B  2 26  ? -18.944 -4.128  -12.712 1.00 20.77  ? 26  HIS B CG  1 
ATOM   2595  N ND1 . HIS B  2 26  ? -19.794 -4.928  -11.978 1.00 21.47  ? 26  HIS B ND1 1 
ATOM   2596  C CD2 . HIS B  2 26  ? -19.465 -4.074  -13.961 1.00 21.55  ? 26  HIS B CD2 1 
ATOM   2597  C CE1 . HIS B  2 26  ? -20.786 -5.338  -12.748 1.00 19.73  ? 26  HIS B CE1 1 
ATOM   2598  N NE2 . HIS B  2 26  ? -20.611 -4.832  -13.956 1.00 20.89  ? 26  HIS B NE2 1 
ATOM   2599  N N   . GLN B  2 27  ? -17.938 -0.778  -13.677 1.00 20.12  ? 27  GLN B N   1 
ATOM   2600  C CA  . GLN B  2 27  ? -18.526 -0.124  -14.837 1.00 21.29  ? 27  GLN B CA  1 
ATOM   2601  C C   . GLN B  2 27  ? -17.901 -0.721  -16.091 1.00 20.58  ? 27  GLN B C   1 
ATOM   2602  O O   . GLN B  2 27  ? -16.680 -0.709  -16.240 1.00 21.22  ? 27  GLN B O   1 
ATOM   2603  C CB  . GLN B  2 27  ? -18.284 1.390   -14.789 1.00 21.84  ? 27  GLN B CB  1 
ATOM   2604  C CG  . GLN B  2 27  ? -19.185 2.202   -15.728 1.00 28.31  ? 27  GLN B CG  1 
ATOM   2605  C CD  . GLN B  2 27  ? -18.503 3.447   -16.307 1.00 36.12  ? 27  GLN B CD  1 
ATOM   2606  O OE1 . GLN B  2 27  ? -18.657 3.754   -17.493 1.00 36.71  ? 27  GLN B OE1 1 
ATOM   2607  N NE2 . GLN B  2 27  ? -17.750 4.164   -15.472 1.00 37.84  ? 27  GLN B NE2 1 
ATOM   2608  N N   . ASN B  2 28  ? -18.738 -1.262  -16.974 1.00 19.93  ? 28  ASN B N   1 
ATOM   2609  C CA  . ASN B  2 28  ? -18.286 -1.800  -18.262 1.00 19.64  ? 28  ASN B CA  1 
ATOM   2610  C C   . ASN B  2 28  ? -19.314 -1.561  -19.374 1.00 19.29  ? 28  ASN B C   1 
ATOM   2611  O O   . ASN B  2 28  ? -20.326 -0.898  -19.146 1.00 19.08  ? 28  ASN B O   1 
ATOM   2612  C CB  . ASN B  2 28  ? -17.915 -3.289  -18.142 1.00 19.57  ? 28  ASN B CB  1 
ATOM   2613  C CG  . ASN B  2 28  ? -19.112 -4.182  -17.827 1.00 20.38  ? 28  ASN B CG  1 
ATOM   2614  O OD1 . ASN B  2 28  ? -20.223 -3.708  -17.589 1.00 23.50  ? 28  ASN B OD1 1 
ATOM   2615  N ND2 . ASN B  2 28  ? -18.882 -5.487  -17.827 1.00 20.73  ? 28  ASN B ND2 1 
ATOM   2616  N N   . ALA B  2 29  ? -19.064 -2.102  -20.565 1.00 19.30  ? 29  ALA B N   1 
ATOM   2617  C CA  . ALA B  2 29  ? -19.943 -1.863  -21.719 1.00 19.76  ? 29  ALA B CA  1 
ATOM   2618  C C   . ALA B  2 29  ? -21.371 -2.383  -21.511 1.00 20.33  ? 29  ALA B C   1 
ATOM   2619  O O   . ALA B  2 29  ? -22.313 -1.912  -22.156 1.00 20.24  ? 29  ALA B O   1 
ATOM   2620  C CB  . ALA B  2 29  ? -19.337 -2.443  -22.994 1.00 19.07  ? 29  ALA B CB  1 
ATOM   2621  N N   . GLN B  2 30  ? -21.518 -3.343  -20.601 1.00 20.62  ? 30  GLN B N   1 
ATOM   2622  C CA  . GLN B  2 30  ? -22.813 -3.937  -20.284 1.00 20.71  ? 30  GLN B CA  1 
ATOM   2623  C C   . GLN B  2 30  ? -23.573 -3.138  -19.215 1.00 21.07  ? 30  GLN B C   1 
ATOM   2624  O O   . GLN B  2 30  ? -24.783 -3.312  -19.043 1.00 20.92  ? 30  GLN B O   1 
ATOM   2625  C CB  . GLN B  2 30  ? -22.632 -5.402  -19.865 1.00 20.91  ? 30  GLN B CB  1 
ATOM   2626  C CG  . GLN B  2 30  ? -22.198 -6.326  -21.016 1.00 21.58  ? 30  GLN B CG  1 
ATOM   2627  C CD  . GLN B  2 30  ? -21.426 -7.558  -20.552 1.00 21.44  ? 30  GLN B CD  1 
ATOM   2628  O OE1 . GLN B  2 30  ? -20.438 -7.455  -19.826 1.00 24.46  ? 30  GLN B OE1 1 
ATOM   2629  N NE2 . GLN B  2 30  ? -21.865 -8.727  -20.993 1.00 20.61  ? 30  GLN B NE2 1 
ATOM   2630  N N   . GLY B  2 31  ? -22.859 -2.263  -18.505 1.00 21.19  ? 31  GLY B N   1 
ATOM   2631  C CA  . GLY B  2 31  ? -23.475 -1.374  -17.519 1.00 21.07  ? 31  GLY B CA  1 
ATOM   2632  C C   . GLY B  2 31  ? -22.769 -1.316  -16.178 1.00 21.29  ? 31  GLY B C   1 
ATOM   2633  O O   . GLY B  2 31  ? -21.578 -1.611  -16.078 1.00 21.14  ? 31  GLY B O   1 
ATOM   2634  N N   . GLU B  2 32  ? -23.515 -0.916  -15.149 1.00 21.97  ? 32  GLU B N   1 
ATOM   2635  C CA  . GLU B  2 32  ? -23.017 -0.895  -13.777 1.00 22.78  ? 32  GLU B CA  1 
ATOM   2636  C C   . GLU B  2 32  ? -23.540 -2.109  -13.009 1.00 22.30  ? 32  GLU B C   1 
ATOM   2637  O O   . GLU B  2 32  ? -24.559 -2.693  -13.375 1.00 22.38  ? 32  GLU B O   1 
ATOM   2638  C CB  . GLU B  2 32  ? -23.428 0.401   -13.062 1.00 23.45  ? 32  GLU B CB  1 
ATOM   2639  C CG  . GLU B  2 32  ? -22.568 0.734   -11.835 1.00 27.69  ? 32  GLU B CG  1 
ATOM   2640  C CD  . GLU B  2 32  ? -23.344 1.432   -10.730 1.00 30.82  ? 32  GLU B CD  1 
ATOM   2641  O OE1 . GLU B  2 32  ? -23.495 2.670   -10.794 1.00 33.01  ? 32  GLU B OE1 1 
ATOM   2642  O OE2 . GLU B  2 32  ? -23.788 0.741   -9.786  1.00 30.14  ? 32  GLU B OE2 1 
ATOM   2643  N N   . GLY B  2 33  ? -22.831 -2.486  -11.949 1.00 22.12  ? 33  GLY B N   1 
ATOM   2644  C CA  . GLY B  2 33  ? -23.237 -3.593  -11.091 1.00 21.32  ? 33  GLY B CA  1 
ATOM   2645  C C   . GLY B  2 33  ? -22.519 -3.565  -9.755  1.00 20.82  ? 33  GLY B C   1 
ATOM   2646  O O   . GLY B  2 33  ? -21.328 -3.237  -9.684  1.00 20.78  ? 33  GLY B O   1 
ATOM   2647  N N   . THR B  2 34  ? -23.256 -3.905  -8.699  1.00 19.98  ? 34  THR B N   1 
ATOM   2648  C CA  . THR B  2 34  ? -22.725 -3.929  -7.337  1.00 19.07  ? 34  THR B CA  1 
ATOM   2649  C C   . THR B  2 34  ? -22.930 -5.303  -6.702  1.00 18.34  ? 34  THR B C   1 
ATOM   2650  O O   . THR B  2 34  ? -24.015 -5.890  -6.790  1.00 18.18  ? 34  THR B O   1 
ATOM   2651  C CB  . THR B  2 34  ? -23.379 -2.842  -6.447  1.00 19.35  ? 34  THR B CB  1 
ATOM   2652  O OG1 . THR B  2 34  ? -23.346 -1.578  -7.122  1.00 19.86  ? 34  THR B OG1 1 
ATOM   2653  C CG2 . THR B  2 34  ? -22.651 -2.717  -5.109  1.00 17.69  ? 34  THR B CG2 1 
ATOM   2654  N N   . ALA B  2 35  ? -21.874 -5.808  -6.071  1.00 17.37  ? 35  ALA B N   1 
ATOM   2655  C CA  . ALA B  2 35  ? -21.923 -7.084  -5.368  1.00 16.90  ? 35  ALA B CA  1 
ATOM   2656  C C   . ALA B  2 35  ? -21.141 -7.005  -4.064  1.00 16.97  ? 35  ALA B C   1 
ATOM   2657  O O   . ALA B  2 35  ? -20.139 -6.295  -3.972  1.00 16.02  ? 35  ALA B O   1 
ATOM   2658  C CB  . ALA B  2 35  ? -21.391 -8.203  -6.248  1.00 15.78  ? 35  ALA B CB  1 
ATOM   2659  N N   . ALA B  2 36  ? -21.613 -7.737  -3.058  1.00 17.84  ? 36  ALA B N   1 
ATOM   2660  C CA  . ALA B  2 36  ? -20.953 -7.782  -1.755  1.00 18.79  ? 36  ALA B CA  1 
ATOM   2661  C C   . ALA B  2 36  ? -19.754 -8.723  -1.777  1.00 18.94  ? 36  ALA B C   1 
ATOM   2662  O O   . ALA B  2 36  ? -19.700 -9.647  -2.590  1.00 19.36  ? 36  ALA B O   1 
ATOM   2663  C CB  . ALA B  2 36  ? -21.945 -8.212  -0.675  1.00 18.45  ? 36  ALA B CB  1 
ATOM   2664  N N   . ASP B  2 37  ? -18.789 -8.474  -0.894  1.00 19.27  ? 37  ASP B N   1 
ATOM   2665  C CA  . ASP B  2 37  ? -17.702 -9.425  -0.674  1.00 19.92  ? 37  ASP B CA  1 
ATOM   2666  C C   . ASP B  2 37  ? -17.859 -10.144 0.660   1.00 20.83  ? 37  ASP B C   1 
ATOM   2667  O O   . ASP B  2 37  ? -17.849 -9.513  1.719   1.00 21.19  ? 37  ASP B O   1 
ATOM   2668  C CB  . ASP B  2 37  ? -16.333 -8.758  -0.740  1.00 19.38  ? 37  ASP B CB  1 
ATOM   2669  C CG  . ASP B  2 37  ? -15.211 -9.762  -0.658  1.00 18.63  ? 37  ASP B CG  1 
ATOM   2670  O OD1 . ASP B  2 37  ? -15.077 -10.583 -1.589  1.00 22.35  ? 37  ASP B OD1 1 
ATOM   2671  O OD2 . ASP B  2 37  ? -14.478 -9.753  0.346   1.00 18.58  ? 37  ASP B OD2 1 
ATOM   2672  N N   . TYR B  2 38  ? -17.977 -11.466 0.592   1.00 21.36  ? 38  TYR B N   1 
ATOM   2673  C CA  . TYR B  2 38  ? -18.294 -12.290 1.754   1.00 22.28  ? 38  TYR B CA  1 
ATOM   2674  C C   . TYR B  2 38  ? -17.122 -12.462 2.727   1.00 22.24  ? 38  TYR B C   1 
ATOM   2675  O O   . TYR B  2 38  ? -17.286 -12.279 3.934   1.00 22.78  ? 38  TYR B O   1 
ATOM   2676  C CB  . TYR B  2 38  ? -18.822 -13.655 1.292   1.00 22.95  ? 38  TYR B CB  1 
ATOM   2677  C CG  . TYR B  2 38  ? -19.225 -14.588 2.413   1.00 26.33  ? 38  TYR B CG  1 
ATOM   2678  C CD1 . TYR B  2 38  ? -20.468 -14.466 3.035   1.00 28.41  ? 38  TYR B CD1 1 
ATOM   2679  C CD2 . TYR B  2 38  ? -18.365 -15.602 2.845   1.00 28.41  ? 38  TYR B CD2 1 
ATOM   2680  C CE1 . TYR B  2 38  ? -20.844 -15.328 4.062   1.00 31.69  ? 38  TYR B CE1 1 
ATOM   2681  C CE2 . TYR B  2 38  ? -18.728 -16.465 3.874   1.00 29.95  ? 38  TYR B CE2 1 
ATOM   2682  C CZ  . TYR B  2 38  ? -19.968 -16.324 4.476   1.00 31.92  ? 38  TYR B CZ  1 
ATOM   2683  O OH  . TYR B  2 38  ? -20.333 -17.175 5.493   1.00 33.90  ? 38  TYR B OH  1 
ATOM   2684  N N   . LYS B  2 39  ? -15.953 -12.816 2.197   1.00 22.00  ? 39  LYS B N   1 
ATOM   2685  C CA  . LYS B  2 39  ? -14.767 -13.096 3.010   1.00 22.40  ? 39  LYS B CA  1 
ATOM   2686  C C   . LYS B  2 39  ? -14.408 -11.931 3.937   1.00 21.78  ? 39  LYS B C   1 
ATOM   2687  O O   . LYS B  2 39  ? -14.152 -12.130 5.127   1.00 22.28  ? 39  LYS B O   1 
ATOM   2688  C CB  . LYS B  2 39  ? -13.578 -13.455 2.104   1.00 23.41  ? 39  LYS B CB  1 
ATOM   2689  C CG  . LYS B  2 39  ? -12.322 -13.948 2.822   1.00 26.76  ? 39  LYS B CG  1 
ATOM   2690  C CD  . LYS B  2 39  ? -12.382 -15.446 3.104   1.00 36.78  ? 39  LYS B CD  1 
ATOM   2691  C CE  . LYS B  2 39  ? -11.111 -15.946 3.788   1.00 40.94  ? 39  LYS B CE  1 
ATOM   2692  N NZ  . LYS B  2 39  ? -9.932  -15.945 2.873   1.00 42.53  ? 39  LYS B NZ  1 
ATOM   2693  N N   . SER B  2 40  ? -14.403 -10.721 3.386   1.00 20.93  ? 40  SER B N   1 
ATOM   2694  C CA  . SER B  2 40  ? -14.035 -9.523  4.132   1.00 20.52  ? 40  SER B CA  1 
ATOM   2695  C C   . SER B  2 40  ? -15.117 -9.104  5.120   1.00 20.01  ? 40  SER B C   1 
ATOM   2696  O O   . SER B  2 40  ? -14.811 -8.699  6.245   1.00 20.23  ? 40  SER B O   1 
ATOM   2697  C CB  . SER B  2 40  ? -13.747 -8.372  3.174   1.00 20.88  ? 40  SER B CB  1 
ATOM   2698  O OG  . SER B  2 40  ? -14.900 -8.057  2.412   1.00 22.96  ? 40  SER B OG  1 
ATOM   2699  N N   . THR B  2 41  ? -16.375 -9.191  4.689   1.00 18.42  ? 41  THR B N   1 
ATOM   2700  C CA  . THR B  2 41  ? -17.518 -8.850  5.531   1.00 17.03  ? 41  THR B CA  1 
ATOM   2701  C C   . THR B  2 41  ? -17.563 -9.743  6.773   1.00 16.41  ? 41  THR B C   1 
ATOM   2702  O O   . THR B  2 41  ? -17.704 -9.249  7.896   1.00 15.80  ? 41  THR B O   1 
ATOM   2703  C CB  . THR B  2 41  ? -18.841 -8.923  4.728   1.00 17.18  ? 41  THR B CB  1 
ATOM   2704  O OG1 . THR B  2 41  ? -18.863 -7.869  3.760   1.00 18.05  ? 41  THR B OG1 1 
ATOM   2705  C CG2 . THR B  2 41  ? -20.059 -8.775  5.625   1.00 17.08  ? 41  THR B CG2 1 
ATOM   2706  N N   . GLN B  2 42  ? -17.414 -11.050 6.565   1.00 15.87  ? 42  GLN B N   1 
ATOM   2707  C CA  . GLN B  2 42  ? -17.471 -12.023 7.659   1.00 15.23  ? 42  GLN B CA  1 
ATOM   2708  C C   . GLN B  2 42  ? -16.283 -11.953 8.604   1.00 14.49  ? 42  GLN B C   1 
ATOM   2709  O O   . GLN B  2 42  ? -16.417 -12.256 9.781   1.00 14.70  ? 42  GLN B O   1 
ATOM   2710  C CB  . GLN B  2 42  ? -17.622 -13.446 7.124   1.00 15.32  ? 42  GLN B CB  1 
ATOM   2711  C CG  . GLN B  2 42  ? -19.040 -13.793 6.690   1.00 16.45  ? 42  GLN B CG  1 
ATOM   2712  C CD  . GLN B  2 42  ? -20.005 -13.987 7.851   1.00 16.23  ? 42  GLN B CD  1 
ATOM   2713  O OE1 . GLN B  2 42  ? -19.604 -14.285 8.981   1.00 15.52  ? 42  GLN B OE1 1 
ATOM   2714  N NE2 . GLN B  2 42  ? -21.292 -13.827 7.569   1.00 15.71  ? 42  GLN B NE2 1 
ATOM   2715  N N   . SER B  2 43  ? -15.125 -11.557 8.088   1.00 14.48  ? 43  SER B N   1 
ATOM   2716  C CA  . SER B  2 43  ? -13.949 -11.357 8.927   1.00 14.52  ? 43  SER B CA  1 
ATOM   2717  C C   . SER B  2 43  ? -14.148 -10.182 9.889   1.00 14.05  ? 43  SER B C   1 
ATOM   2718  O O   . SER B  2 43  ? -13.728 -10.241 11.045  1.00 14.39  ? 43  SER B O   1 
ATOM   2719  C CB  . SER B  2 43  ? -12.707 -11.143 8.064   1.00 14.48  ? 43  SER B CB  1 
ATOM   2720  O OG  . SER B  2 43  ? -11.560 -10.961 8.872   1.00 18.12  ? 43  SER B OG  1 
ATOM   2721  N N   . ALA B  2 44  ? -14.795 -9.124  9.408   1.00 13.62  ? 44  ALA B N   1 
ATOM   2722  C CA  . ALA B  2 44  ? -15.089 -7.963  10.241  1.00 13.79  ? 44  ALA B CA  1 
ATOM   2723  C C   . ALA B  2 44  ? -16.185 -8.271  11.261  1.00 14.88  ? 44  ALA B C   1 
ATOM   2724  O O   . ALA B  2 44  ? -16.121 -7.816  12.403  1.00 15.82  ? 44  ALA B O   1 
ATOM   2725  C CB  . ALA B  2 44  ? -15.468 -6.773  9.386   1.00 13.24  ? 44  ALA B CB  1 
ATOM   2726  N N   . ILE B  2 45  ? -17.182 -9.052  10.848  1.00 14.82  ? 45  ILE B N   1 
ATOM   2727  C CA  . ILE B  2 45  ? -18.265 -9.457  11.739  1.00 14.52  ? 45  ILE B CA  1 
ATOM   2728  C C   . ILE B  2 45  ? -17.765 -10.410 12.833  1.00 15.35  ? 45  ILE B C   1 
ATOM   2729  O O   . ILE B  2 45  ? -18.066 -10.211 14.015  1.00 15.76  ? 45  ILE B O   1 
ATOM   2730  C CB  . ILE B  2 45  ? -19.459 -10.061 10.955  1.00 14.20  ? 45  ILE B CB  1 
ATOM   2731  C CG1 . ILE B  2 45  ? -20.152 -8.968  10.132  1.00 13.34  ? 45  ILE B CG1 1 
ATOM   2732  C CG2 . ILE B  2 45  ? -20.457 -10.729 11.906  1.00 13.13  ? 45  ILE B CG2 1 
ATOM   2733  C CD1 . ILE B  2 45  ? -21.100 -9.488  9.052   1.00 12.42  ? 45  ILE B CD1 1 
ATOM   2734  N N   . ASP B  2 46  ? -16.998 -11.429 12.440  1.00 15.63  ? 46  ASP B N   1 
ATOM   2735  C CA  . ASP B  2 46  ? -16.413 -12.375 13.396  1.00 16.03  ? 46  ASP B CA  1 
ATOM   2736  C C   . ASP B  2 46  ? -15.621 -11.662 14.502  1.00 16.70  ? 46  ASP B C   1 
ATOM   2737  O O   . ASP B  2 46  ? -15.680 -12.062 15.664  1.00 17.03  ? 46  ASP B O   1 
ATOM   2738  C CB  . ASP B  2 46  ? -15.524 -13.414 12.690  1.00 15.63  ? 46  ASP B CB  1 
ATOM   2739  C CG  . ASP B  2 46  ? -16.325 -14.471 11.923  1.00 15.40  ? 46  ASP B CG  1 
ATOM   2740  O OD1 . ASP B  2 46  ? -15.699 -15.388 11.350  1.00 15.78  ? 46  ASP B OD1 1 
ATOM   2741  O OD2 . ASP B  2 46  ? -17.570 -14.397 11.881  1.00 14.15  ? 46  ASP B OD2 1 
ATOM   2742  N N   . GLN B  2 47  ? -14.902 -10.601 14.136  1.00 16.75  ? 47  GLN B N   1 
ATOM   2743  C CA  . GLN B  2 47  ? -14.096 -9.842  15.092  1.00 17.20  ? 47  GLN B CA  1 
ATOM   2744  C C   . GLN B  2 47  ? -14.951 -8.996  16.029  1.00 16.90  ? 47  GLN B C   1 
ATOM   2745  O O   . GLN B  2 47  ? -14.669 -8.909  17.225  1.00 17.18  ? 47  GLN B O   1 
ATOM   2746  C CB  . GLN B  2 47  ? -13.062 -8.975  14.368  1.00 17.72  ? 47  GLN B CB  1 
ATOM   2747  C CG  . GLN B  2 47  ? -11.855 -9.754  13.869  1.00 19.14  ? 47  GLN B CG  1 
ATOM   2748  C CD  . GLN B  2 47  ? -11.005 -8.953  12.910  1.00 22.42  ? 47  GLN B CD  1 
ATOM   2749  O OE1 . GLN B  2 47  ? -10.265 -8.052  13.313  1.00 22.40  ? 47  GLN B OE1 1 
ATOM   2750  N NE2 . GLN B  2 47  ? -11.097 -9.286  11.626  1.00 20.75  ? 47  GLN B NE2 1 
ATOM   2751  N N   . ILE B  2 48  ? -15.986 -8.369  15.477  1.00 16.91  ? 48  ILE B N   1 
ATOM   2752  C CA  . ILE B  2 48  ? -16.987 -7.649  16.269  1.00 16.57  ? 48  ILE B CA  1 
ATOM   2753  C C   . ILE B  2 48  ? -17.730 -8.605  17.218  1.00 16.30  ? 48  ILE B C   1 
ATOM   2754  O O   . ILE B  2 48  ? -17.904 -8.306  18.406  1.00 17.30  ? 48  ILE B O   1 
ATOM   2755  C CB  . ILE B  2 48  ? -17.989 -6.898  15.346  1.00 16.50  ? 48  ILE B CB  1 
ATOM   2756  C CG1 . ILE B  2 48  ? -17.315 -5.689  14.688  1.00 16.98  ? 48  ILE B CG1 1 
ATOM   2757  C CG2 . ILE B  2 48  ? -19.276 -6.508  16.090  1.00 14.90  ? 48  ILE B CG2 1 
ATOM   2758  C CD1 . ILE B  2 48  ? -16.847 -4.626  15.653  1.00 22.50  ? 48  ILE B CD1 1 
ATOM   2759  N N   . THR B  2 49  ? -18.151 -9.752  16.690  1.00 14.31  ? 49  THR B N   1 
ATOM   2760  C CA  . THR B  2 49  ? -18.854 -10.753 17.482  1.00 13.81  ? 49  THR B CA  1 
ATOM   2761  C C   . THR B  2 49  ? -17.974 -11.200 18.648  1.00 13.72  ? 49  THR B C   1 
ATOM   2762  O O   . THR B  2 49  ? -18.457 -11.353 19.775  1.00 13.96  ? 49  THR B O   1 
ATOM   2763  C CB  . THR B  2 49  ? -19.278 -11.957 16.614  1.00 13.82  ? 49  THR B CB  1 
ATOM   2764  O OG1 . THR B  2 49  ? -20.007 -11.481 15.477  1.00 13.35  ? 49  THR B OG1 1 
ATOM   2765  C CG2 . THR B  2 49  ? -20.154 -12.933 17.403  1.00 11.96  ? 49  THR B CG2 1 
ATOM   2766  N N   . GLY B  2 50  ? -16.685 -11.379 18.365  1.00 13.14  ? 50  GLY B N   1 
ATOM   2767  C CA  . GLY B  2 50  ? -15.686 -11.690 19.382  1.00 13.17  ? 50  GLY B CA  1 
ATOM   2768  C C   . GLY B  2 50  ? -15.719 -10.723 20.548  1.00 13.90  ? 50  GLY B C   1 
ATOM   2769  O O   . GLY B  2 50  ? -15.686 -11.148 21.706  1.00 14.20  ? 50  GLY B O   1 
ATOM   2770  N N   . LYS B  2 51  ? -15.794 -9.426  20.242  1.00 14.22  ? 51  LYS B N   1 
ATOM   2771  C CA  . LYS B  2 51  ? -15.906 -8.383  21.265  1.00 15.03  ? 51  LYS B CA  1 
ATOM   2772  C C   . LYS B  2 51  ? -17.190 -8.525  22.069  1.00 15.74  ? 51  LYS B C   1 
ATOM   2773  O O   . LYS B  2 51  ? -17.170 -8.440  23.297  1.00 16.23  ? 51  LYS B O   1 
ATOM   2774  C CB  . LYS B  2 51  ? -15.827 -6.983  20.648  1.00 14.80  ? 51  LYS B CB  1 
ATOM   2775  C CG  . LYS B  2 51  ? -14.514 -6.698  19.959  1.00 16.49  ? 51  LYS B CG  1 
ATOM   2776  C CD  . LYS B  2 51  ? -14.356 -5.235  19.597  1.00 15.11  ? 51  LYS B CD  1 
ATOM   2777  C CE  . LYS B  2 51  ? -12.971 -5.003  19.017  1.00 15.80  ? 51  LYS B CE  1 
ATOM   2778  N NZ  . LYS B  2 51  ? -12.504 -3.612  19.232  1.00 14.12  ? 51  LYS B NZ  1 
ATOM   2779  N N   . LEU B  2 52  ? -18.301 -8.757  21.374  1.00 16.28  ? 52  LEU B N   1 
ATOM   2780  C CA  . LEU B  2 52  ? -19.595 -8.942  22.030  1.00 17.26  ? 52  LEU B CA  1 
ATOM   2781  C C   . LEU B  2 52  ? -19.629 -10.156 22.960  1.00 18.15  ? 52  LEU B C   1 
ATOM   2782  O O   . LEU B  2 52  ? -20.260 -10.101 24.016  1.00 18.02  ? 52  LEU B O   1 
ATOM   2783  C CB  . LEU B  2 52  ? -20.727 -9.021  21.003  1.00 17.11  ? 52  LEU B CB  1 
ATOM   2784  C CG  . LEU B  2 52  ? -20.992 -7.745  20.197  1.00 17.14  ? 52  LEU B CG  1 
ATOM   2785  C CD1 . LEU B  2 52  ? -22.030 -8.018  19.123  1.00 15.70  ? 52  LEU B CD1 1 
ATOM   2786  C CD2 . LEU B  2 52  ? -21.422 -6.577  21.097  1.00 11.01  ? 52  LEU B CD2 1 
ATOM   2787  N N   . ASN B  2 53  ? -18.947 -11.237 22.571  1.00 18.66  ? 53  ASN B N   1 
ATOM   2788  C CA  . ASN B  2 53  ? -18.830 -12.433 23.414  1.00 19.38  ? 53  ASN B CA  1 
ATOM   2789  C C   . ASN B  2 53  ? -18.100 -12.159 24.727  1.00 20.03  ? 53  ASN B C   1 
ATOM   2790  O O   . ASN B  2 53  ? -18.402 -12.765 25.754  1.00 19.89  ? 53  ASN B O   1 
ATOM   2791  C CB  . ASN B  2 53  ? -18.127 -13.571 22.667  1.00 19.15  ? 53  ASN B CB  1 
ATOM   2792  C CG  . ASN B  2 53  ? -18.958 -14.134 21.527  1.00 21.04  ? 53  ASN B CG  1 
ATOM   2793  O OD1 . ASN B  2 53  ? -20.114 -13.756 21.331  1.00 26.36  ? 53  ASN B OD1 1 
ATOM   2794  N ND2 . ASN B  2 53  ? -18.366 -15.044 20.764  1.00 21.10  ? 53  ASN B ND2 1 
ATOM   2795  N N   . ARG B  2 54  ? -17.141 -11.239 24.678  1.00 21.19  ? 54  ARG B N   1 
ATOM   2796  C CA  . ARG B  2 54  ? -16.333 -10.882 25.836  1.00 22.30  ? 54  ARG B CA  1 
ATOM   2797  C C   . ARG B  2 54  ? -17.085 -10.014 26.830  1.00 23.81  ? 54  ARG B C   1 
ATOM   2798  O O   . ARG B  2 54  ? -16.779 -10.039 28.020  1.00 24.69  ? 54  ARG B O   1 
ATOM   2799  C CB  . ARG B  2 54  ? -15.080 -10.140 25.390  1.00 22.40  ? 54  ARG B CB  1 
ATOM   2800  C CG  . ARG B  2 54  ? -13.838 -10.994 25.293  1.00 21.85  ? 54  ARG B CG  1 
ATOM   2801  C CD  . ARG B  2 54  ? -12.625 -10.164 24.882  1.00 24.12  ? 54  ARG B CD  1 
ATOM   2802  N NE  . ARG B  2 54  ? -12.511 -8.916  25.641  1.00 22.95  ? 54  ARG B NE  1 
ATOM   2803  C CZ  . ARG B  2 54  ? -12.707 -7.700  25.134  1.00 22.30  ? 54  ARG B CZ  1 
ATOM   2804  N NH1 . ARG B  2 54  ? -13.019 -7.543  23.852  1.00 17.11  ? 54  ARG B NH1 1 
ATOM   2805  N NH2 . ARG B  2 54  ? -12.583 -6.632  25.911  1.00 22.78  ? 54  ARG B NH2 1 
ATOM   2806  N N   . LEU B  2 55  ? -18.061 -9.250  26.340  1.00 24.94  ? 55  LEU B N   1 
ATOM   2807  C CA  . LEU B  2 55  ? -18.731 -8.230  27.151  1.00 25.52  ? 55  LEU B CA  1 
ATOM   2808  C C   . LEU B  2 55  ? -20.201 -8.522  27.458  1.00 26.26  ? 55  LEU B C   1 
ATOM   2809  O O   . LEU B  2 55  ? -20.684 -8.194  28.542  1.00 26.97  ? 55  LEU B O   1 
ATOM   2810  C CB  . LEU B  2 55  ? -18.585 -6.850  26.496  1.00 25.41  ? 55  LEU B CB  1 
ATOM   2811  C CG  . LEU B  2 55  ? -17.156 -6.366  26.229  1.00 26.07  ? 55  LEU B CG  1 
ATOM   2812  C CD1 . LEU B  2 55  ? -17.137 -5.134  25.338  1.00 27.67  ? 55  LEU B CD1 1 
ATOM   2813  C CD2 . LEU B  2 55  ? -16.424 -6.097  27.532  1.00 30.06  ? 55  LEU B CD2 1 
ATOM   2814  N N   . ILE B  2 56  ? -20.906 -9.127  26.505  1.00 26.97  ? 56  ILE B N   1 
ATOM   2815  C CA  . ILE B  2 56  ? -22.325 -9.450  26.677  1.00 28.21  ? 56  ILE B CA  1 
ATOM   2816  C C   . ILE B  2 56  ? -22.479 -10.909 27.098  1.00 29.18  ? 56  ILE B C   1 
ATOM   2817  O O   . ILE B  2 56  ? -21.809 -11.792 26.560  1.00 29.12  ? 56  ILE B O   1 
ATOM   2818  C CB  . ILE B  2 56  ? -23.161 -9.171  25.375  1.00 28.32  ? 56  ILE B CB  1 
ATOM   2819  C CG1 . ILE B  2 56  ? -22.878 -7.771  24.802  1.00 27.97  ? 56  ILE B CG1 1 
ATOM   2820  C CG2 . ILE B  2 56  ? -24.663 -9.385  25.604  1.00 26.77  ? 56  ILE B CG2 1 
ATOM   2821  C CD1 . ILE B  2 56  ? -23.180 -6.600  25.733  1.00 27.75  ? 56  ILE B CD1 1 
ATOM   2822  N N   . GLY B  2 57  ? -23.355 -11.151 28.070  1.00 30.63  ? 57  GLY B N   1 
ATOM   2823  C CA  . GLY B  2 57  ? -23.677 -12.509 28.505  1.00 31.94  ? 57  GLY B CA  1 
ATOM   2824  C C   . GLY B  2 57  ? -22.679 -13.137 29.460  1.00 33.24  ? 57  GLY B C   1 
ATOM   2825  O O   . GLY B  2 57  ? -22.844 -14.291 29.850  1.00 33.75  ? 57  GLY B O   1 
ATOM   2826  N N   . LYS B  2 58  ? -21.636 -12.384 29.818  1.00 34.59  ? 58  LYS B N   1 
ATOM   2827  C CA  . LYS B  2 58  ? -20.683 -12.760 30.869  1.00 35.41  ? 58  LYS B CA  1 
ATOM   2828  C C   . LYS B  2 58  ? -21.377 -13.248 32.140  1.00 35.28  ? 58  LYS B C   1 
ATOM   2829  O O   . LYS B  2 58  ? -22.507 -12.844 32.440  1.00 35.23  ? 58  LYS B O   1 
ATOM   2830  C CB  . LYS B  2 58  ? -19.836 -11.546 31.254  1.00 36.03  ? 58  LYS B CB  1 
ATOM   2831  C CG  . LYS B  2 58  ? -18.345 -11.608 30.952  1.00 39.32  ? 58  LYS B CG  1 
ATOM   2832  C CD  . LYS B  2 58  ? -17.652 -10.473 31.725  1.00 43.68  ? 58  LYS B CD  1 
ATOM   2833  C CE  . LYS B  2 58  ? -16.311 -10.072 31.130  1.00 44.87  ? 58  LYS B CE  1 
ATOM   2834  N NZ  . LYS B  2 58  ? -16.037 -8.616  31.360  1.00 44.35  ? 58  LYS B NZ  1 
ATOM   2835  N N   . THR B  2 59  ? -20.689 -14.111 32.885  1.00 34.99  ? 59  THR B N   1 
ATOM   2836  C CA  . THR B  2 59  ? -21.082 -14.432 34.252  1.00 34.23  ? 59  THR B CA  1 
ATOM   2837  C C   . THR B  2 59  ? -20.824 -13.187 35.107  1.00 33.73  ? 59  THR B C   1 
ATOM   2838  O O   . THR B  2 59  ? -19.681 -12.736 35.233  1.00 33.93  ? 59  THR B O   1 
ATOM   2839  C CB  . THR B  2 59  ? -20.286 -15.635 34.806  1.00 34.28  ? 59  THR B CB  1 
ATOM   2840  O OG1 . THR B  2 59  ? -20.407 -16.748 33.911  1.00 33.55  ? 59  THR B OG1 1 
ATOM   2841  C CG2 . THR B  2 59  ? -20.798 -16.041 36.187  1.00 34.07  ? 59  THR B CG2 1 
ATOM   2842  N N   . ASN B  2 60  ? -21.892 -12.625 35.666  1.00 32.51  ? 60  ASN B N   1 
ATOM   2843  C CA  . ASN B  2 60  ? -21.792 -11.443 36.519  1.00 31.40  ? 60  ASN B CA  1 
ATOM   2844  C C   . ASN B  2 60  ? -21.133 -11.785 37.856  1.00 30.85  ? 60  ASN B C   1 
ATOM   2845  O O   . ASN B  2 60  ? -21.136 -12.947 38.272  1.00 30.96  ? 60  ASN B O   1 
ATOM   2846  C CB  . ASN B  2 60  ? -23.183 -10.843 36.759  1.00 31.39  ? 60  ASN B CB  1 
ATOM   2847  C CG  . ASN B  2 60  ? -23.828 -10.291 35.487  1.00 30.88  ? 60  ASN B CG  1 
ATOM   2848  O OD1 . ASN B  2 60  ? -23.149 -9.808  34.577  1.00 29.89  ? 60  ASN B OD1 1 
ATOM   2849  N ND2 . ASN B  2 60  ? -25.153 -10.349 35.435  1.00 28.85  ? 60  ASN B ND2 1 
ATOM   2850  N N   . GLN B  2 61  ? -20.565 -10.783 38.525  1.00 30.23  ? 61  GLN B N   1 
ATOM   2851  C CA  . GLN B  2 61  ? -20.024 -10.992 39.872  1.00 29.98  ? 61  GLN B CA  1 
ATOM   2852  C C   . GLN B  2 61  ? -21.130 -10.973 40.940  1.00 29.27  ? 61  GLN B C   1 
ATOM   2853  O O   . GLN B  2 61  ? -22.183 -10.360 40.744  1.00 29.22  ? 61  GLN B O   1 
ATOM   2854  C CB  . GLN B  2 61  ? -18.874 -10.019 40.196  1.00 30.00  ? 61  GLN B CB  1 
ATOM   2855  C CG  . GLN B  2 61  ? -19.197 -8.533  40.128  1.00 30.26  ? 61  GLN B CG  1 
ATOM   2856  C CD  . GLN B  2 61  ? -17.950 -7.649  40.225  1.00 33.37  ? 61  GLN B CD  1 
ATOM   2857  O OE1 . GLN B  2 61  ? -17.159 -7.556  39.278  1.00 32.62  ? 61  GLN B OE1 1 
ATOM   2858  N NE2 . GLN B  2 61  ? -17.780 -6.985  41.368  1.00 28.06  ? 61  GLN B NE2 1 
ATOM   2859  N N   . GLN B  2 62  ? -20.884 -11.665 42.050  1.00 27.91  ? 62  GLN B N   1 
ATOM   2860  C CA  . GLN B  2 62  ? -21.879 -11.840 43.110  1.00 27.02  ? 62  GLN B CA  1 
ATOM   2861  C C   . GLN B  2 62  ? -21.968 -10.597 44.000  1.00 25.51  ? 62  GLN B C   1 
ATOM   2862  O O   . GLN B  2 62  ? -20.958 -9.942  44.261  1.00 25.41  ? 62  GLN B O   1 
ATOM   2863  C CB  . GLN B  2 62  ? -21.528 -13.074 43.949  1.00 27.43  ? 62  GLN B CB  1 
ATOM   2864  C CG  . GLN B  2 62  ? -22.690 -13.684 44.729  1.00 30.06  ? 62  GLN B CG  1 
ATOM   2865  C CD  . GLN B  2 62  ? -23.612 -14.537 43.866  1.00 32.70  ? 62  GLN B CD  1 
ATOM   2866  O OE1 . GLN B  2 62  ? -23.198 -15.101 42.847  1.00 30.46  ? 62  GLN B OE1 1 
ATOM   2867  N NE2 . GLN B  2 62  ? -24.872 -14.640 44.281  1.00 30.89  ? 62  GLN B NE2 1 
ATOM   2868  N N   . PHE B  2 63  ? -23.175 -10.279 44.467  1.00 23.70  ? 63  PHE B N   1 
ATOM   2869  C CA  . PHE B  2 63  ? -23.384 -9.100  45.309  1.00 22.50  ? 63  PHE B CA  1 
ATOM   2870  C C   . PHE B  2 63  ? -24.228 -9.377  46.550  1.00 22.28  ? 63  PHE B C   1 
ATOM   2871  O O   . PHE B  2 63  ? -25.124 -10.222 46.525  1.00 22.41  ? 63  PHE B O   1 
ATOM   2872  C CB  . PHE B  2 63  ? -24.003 -7.960  44.495  1.00 22.08  ? 63  PHE B CB  1 
ATOM   2873  C CG  . PHE B  2 63  ? -23.044 -7.307  43.538  1.00 19.83  ? 63  PHE B CG  1 
ATOM   2874  C CD1 . PHE B  2 63  ? -22.167 -6.317  43.972  1.00 16.19  ? 63  PHE B CD1 1 
ATOM   2875  C CD2 . PHE B  2 63  ? -23.017 -7.682  42.201  1.00 16.76  ? 63  PHE B CD2 1 
ATOM   2876  C CE1 . PHE B  2 63  ? -21.274 -5.714  43.091  1.00 13.52  ? 63  PHE B CE1 1 
ATOM   2877  C CE2 . PHE B  2 63  ? -22.129 -7.084  41.312  1.00 14.84  ? 63  PHE B CE2 1 
ATOM   2878  C CZ  . PHE B  2 63  ? -21.257 -6.097  41.758  1.00 12.08  ? 63  PHE B CZ  1 
ATOM   2879  N N   . GLU B  2 64  ? -23.918 -8.660  47.630  1.00 21.88  ? 64  GLU B N   1 
ATOM   2880  C CA  . GLU B  2 64  ? -24.665 -8.738  48.891  1.00 21.86  ? 64  GLU B CA  1 
ATOM   2881  C C   . GLU B  2 64  ? -24.802 -7.369  49.552  1.00 21.76  ? 64  GLU B C   1 
ATOM   2882  O O   . GLU B  2 64  ? -23.895 -6.532  49.472  1.00 21.92  ? 64  GLU B O   1 
ATOM   2883  C CB  . GLU B  2 64  ? -23.980 -9.685  49.877  1.00 21.85  ? 64  GLU B CB  1 
ATOM   2884  C CG  . GLU B  2 64  ? -24.184 -11.162 49.600  1.00 24.27  ? 64  GLU B CG  1 
ATOM   2885  C CD  . GLU B  2 64  ? -23.808 -12.027 50.785  1.00 27.71  ? 64  GLU B CD  1 
ATOM   2886  O OE1 . GLU B  2 64  ? -23.356 -11.472 51.811  1.00 25.94  ? 64  GLU B OE1 1 
ATOM   2887  O OE2 . GLU B  2 64  ? -23.970 -13.264 50.690  1.00 29.64  ? 64  GLU B OE2 1 
ATOM   2888  N N   . LEU B  2 65  ? -25.934 -7.159  50.220  1.00 21.70  ? 65  LEU B N   1 
ATOM   2889  C CA  . LEU B  2 65  ? -26.198 -5.917  50.938  1.00 21.26  ? 65  LEU B CA  1 
ATOM   2890  C C   . LEU B  2 65  ? -25.373 -5.837  52.222  1.00 21.52  ? 65  LEU B C   1 
ATOM   2891  O O   . LEU B  2 65  ? -25.351 -6.782  53.015  1.00 21.67  ? 65  LEU B O   1 
ATOM   2892  C CB  . LEU B  2 65  ? -27.691 -5.786  51.260  1.00 21.15  ? 65  LEU B CB  1 
ATOM   2893  C CG  . LEU B  2 65  ? -28.728 -5.927  50.136  1.00 21.19  ? 65  LEU B CG  1 
ATOM   2894  C CD1 . LEU B  2 65  ? -30.128 -6.099  50.723  1.00 19.42  ? 65  LEU B CD1 1 
ATOM   2895  C CD2 . LEU B  2 65  ? -28.692 -4.746  49.169  1.00 20.76  ? 65  LEU B CD2 1 
ATOM   2896  N N   . ILE B  2 66  ? -24.680 -4.713  52.395  1.00 21.56  ? 66  ILE B N   1 
ATOM   2897  C CA  . ILE B  2 66  ? -23.942 -4.394  53.622  1.00 22.16  ? 66  ILE B CA  1 
ATOM   2898  C C   . ILE B  2 66  ? -24.573 -3.195  54.303  1.00 21.75  ? 66  ILE B C   1 
ATOM   2899  O O   . ILE B  2 66  ? -24.265 -2.889  55.454  1.00 21.76  ? 66  ILE B O   1 
ATOM   2900  C CB  . ILE B  2 66  ? -22.474 -4.036  53.344  1.00 22.62  ? 66  ILE B CB  1 
ATOM   2901  C CG1 . ILE B  2 66  ? -22.329 -3.533  51.911  1.00 23.43  ? 66  ILE B CG1 1 
ATOM   2902  C CG2 . ILE B  2 66  ? -21.555 -5.234  53.608  1.00 23.93  ? 66  ILE B CG2 1 
ATOM   2903  C CD1 . ILE B  2 66  ? -21.520 -2.309  51.814  1.00 27.08  ? 66  ILE B CD1 1 
ATOM   2904  N N   . ASP B  2 67  ? -25.441 -2.509  53.567  1.00 22.16  ? 67  ASP B N   1 
ATOM   2905  C CA  . ASP B  2 67  ? -26.209 -1.389  54.088  1.00 22.83  ? 67  ASP B CA  1 
ATOM   2906  C C   . ASP B  2 67  ? -27.573 -1.846  54.584  1.00 22.76  ? 67  ASP B C   1 
ATOM   2907  O O   . ASP B  2 67  ? -27.975 -2.995  54.385  1.00 22.30  ? 67  ASP B O   1 
ATOM   2908  C CB  . ASP B  2 67  ? -26.400 -0.326  53.002  1.00 22.98  ? 67  ASP B CB  1 
ATOM   2909  C CG  . ASP B  2 67  ? -25.314 0.726   53.014  1.00 25.45  ? 67  ASP B CG  1 
ATOM   2910  O OD1 . ASP B  2 67  ? -24.657 0.916   54.062  1.00 30.63  ? 67  ASP B OD1 1 
ATOM   2911  O OD2 . ASP B  2 67  ? -25.122 1.377   51.970  1.00 28.80  ? 67  ASP B OD2 1 
ATOM   2912  N N   . ASN B  2 68  ? -28.275 -0.927  55.235  1.00 22.96  ? 68  ASN B N   1 
ATOM   2913  C CA  . ASN B  2 68  ? -29.668 -1.116  55.582  1.00 23.01  ? 68  ASN B CA  1 
ATOM   2914  C C   . ASN B  2 68  ? -30.440 0.083   55.060  1.00 23.15  ? 68  ASN B C   1 
ATOM   2915  O O   . ASN B  2 68  ? -30.221 1.208   55.509  1.00 23.24  ? 68  ASN B O   1 
ATOM   2916  C CB  . ASN B  2 68  ? -29.825 -1.255  57.097  1.00 22.90  ? 68  ASN B CB  1 
ATOM   2917  C CG  . ASN B  2 68  ? -31.223 -1.677  57.512  1.00 23.33  ? 68  ASN B CG  1 
ATOM   2918  O OD1 . ASN B  2 68  ? -32.190 -1.523  56.764  1.00 22.45  ? 68  ASN B OD1 1 
ATOM   2919  N ND2 . ASN B  2 68  ? -31.337 -2.206  58.723  1.00 26.25  ? 68  ASN B ND2 1 
ATOM   2920  N N   . GLU B  2 69  ? -31.328 -0.166  54.099  1.00 23.43  ? 69  GLU B N   1 
ATOM   2921  C CA  . GLU B  2 69  ? -32.124 0.890   53.463  1.00 23.55  ? 69  GLU B CA  1 
ATOM   2922  C C   . GLU B  2 69  ? -33.363 1.291   54.265  1.00 22.79  ? 69  GLU B C   1 
ATOM   2923  O O   . GLU B  2 69  ? -34.006 2.289   53.940  1.00 23.13  ? 69  GLU B O   1 
ATOM   2924  C CB  . GLU B  2 69  ? -32.519 0.490   52.033  1.00 23.78  ? 69  GLU B CB  1 
ATOM   2925  C CG  . GLU B  2 69  ? -31.494 0.877   50.967  1.00 27.68  ? 69  GLU B CG  1 
ATOM   2926  C CD  . GLU B  2 69  ? -31.633 0.075   49.677  1.00 33.28  ? 69  GLU B CD  1 
ATOM   2927  O OE1 . GLU B  2 69  ? -31.515 -1.171  49.725  1.00 36.76  ? 69  GLU B OE1 1 
ATOM   2928  O OE2 . GLU B  2 69  ? -31.837 0.691   48.608  1.00 34.24  ? 69  GLU B OE2 1 
ATOM   2929  N N   . PHE B  2 70  ? -33.696 0.522   55.302  1.00 22.38  ? 70  PHE B N   1 
ATOM   2930  C CA  . PHE B  2 70  ? -34.870 0.815   56.134  1.00 22.13  ? 70  PHE B CA  1 
ATOM   2931  C C   . PHE B  2 70  ? -34.493 1.529   57.429  1.00 23.61  ? 70  PHE B C   1 
ATOM   2932  O O   . PHE B  2 70  ? -35.157 2.487   57.832  1.00 23.38  ? 70  PHE B O   1 
ATOM   2933  C CB  . PHE B  2 70  ? -35.678 -0.453  56.459  1.00 21.00  ? 70  PHE B CB  1 
ATOM   2934  C CG  . PHE B  2 70  ? -36.199 -1.190  55.249  1.00 17.91  ? 70  PHE B CG  1 
ATOM   2935  C CD1 . PHE B  2 70  ? -36.476 -2.552  55.328  1.00 16.70  ? 70  PHE B CD1 1 
ATOM   2936  C CD2 . PHE B  2 70  ? -36.410 -0.535  54.034  1.00 16.89  ? 70  PHE B CD2 1 
ATOM   2937  C CE1 . PHE B  2 70  ? -36.955 -3.252  54.220  1.00 15.43  ? 70  PHE B CE1 1 
ATOM   2938  C CE2 . PHE B  2 70  ? -36.886 -1.227  52.920  1.00 16.52  ? 70  PHE B CE2 1 
ATOM   2939  C CZ  . PHE B  2 70  ? -37.160 -2.587  53.014  1.00 15.46  ? 70  PHE B CZ  1 
ATOM   2940  N N   . ASN B  2 71  ? -33.435 1.050   58.082  1.00 25.22  ? 71  ASN B N   1 
ATOM   2941  C CA  . ASN B  2 71  ? -32.961 1.636   59.335  1.00 26.32  ? 71  ASN B CA  1 
ATOM   2942  C C   . ASN B  2 71  ? -31.455 1.851   59.322  1.00 26.46  ? 71  ASN B C   1 
ATOM   2943  O O   . ASN B  2 71  ? -30.686 0.905   59.512  1.00 27.01  ? 71  ASN B O   1 
ATOM   2944  C CB  . ASN B  2 71  ? -33.358 0.760   60.527  1.00 26.77  ? 71  ASN B CB  1 
ATOM   2945  C CG  . ASN B  2 71  ? -34.847 0.475   60.571  1.00 29.51  ? 71  ASN B CG  1 
ATOM   2946  O OD1 . ASN B  2 71  ? -35.662 1.380   60.766  1.00 29.04  ? 71  ASN B OD1 1 
ATOM   2947  N ND2 . ASN B  2 71  ? -35.209 -0.792  60.388  1.00 31.16  ? 71  ASN B ND2 1 
ATOM   2948  N N   . GLU B  2 72  ? -31.054 3.102   59.094  1.00 26.58  ? 72  GLU B N   1 
ATOM   2949  C CA  . GLU B  2 72  ? -29.645 3.515   59.056  1.00 26.62  ? 72  GLU B CA  1 
ATOM   2950  C C   . GLU B  2 72  ? -28.766 2.875   60.127  1.00 26.39  ? 72  GLU B C   1 
ATOM   2951  O O   . GLU B  2 72  ? -29.063 2.959   61.324  1.00 26.97  ? 72  GLU B O   1 
ATOM   2952  C CB  . GLU B  2 72  ? -29.536 5.035   59.178  1.00 26.82  ? 72  GLU B CB  1 
ATOM   2953  C CG  . GLU B  2 72  ? -29.094 5.742   57.911  1.00 29.57  ? 72  GLU B CG  1 
ATOM   2954  C CD  . GLU B  2 72  ? -28.320 7.021   58.201  1.00 34.36  ? 72  GLU B CD  1 
ATOM   2955  O OE1 . GLU B  2 72  ? -28.703 7.769   59.131  1.00 36.86  ? 72  GLU B OE1 1 
ATOM   2956  O OE2 . GLU B  2 72  ? -27.323 7.278   57.498  1.00 33.54  ? 72  GLU B OE2 1 
ATOM   2957  N N   . ILE B  2 73  ? -27.683 2.241   59.683  1.00 25.44  ? 73  ILE B N   1 
ATOM   2958  C CA  . ILE B  2 73  ? -26.672 1.686   60.583  1.00 24.49  ? 73  ILE B CA  1 
ATOM   2959  C C   . ILE B  2 73  ? -25.877 2.821   61.234  1.00 25.06  ? 73  ILE B C   1 
ATOM   2960  O O   . ILE B  2 73  ? -26.085 3.989   60.903  1.00 24.97  ? 73  ILE B O   1 
ATOM   2961  C CB  . ILE B  2 73  ? -25.718 0.712   59.844  1.00 23.93  ? 73  ILE B CB  1 
ATOM   2962  C CG1 . ILE B  2 73  ? -25.057 1.400   58.640  1.00 20.07  ? 73  ILE B CG1 1 
ATOM   2963  C CG2 . ILE B  2 73  ? -26.471 -0.541  59.420  1.00 23.55  ? 73  ILE B CG2 1 
ATOM   2964  C CD1 . ILE B  2 73  ? -23.927 0.617   58.005  1.00 10.43  ? 73  ILE B CD1 1 
ATOM   2965  N N   . GLU B  2 74  ? -24.977 2.479   62.156  1.00 25.95  ? 74  GLU B N   1 
ATOM   2966  C CA  . GLU B  2 74  ? -24.153 3.484   62.831  1.00 26.51  ? 74  GLU B CA  1 
ATOM   2967  C C   . GLU B  2 74  ? -23.417 4.360   61.828  1.00 26.09  ? 74  GLU B C   1 
ATOM   2968  O O   . GLU B  2 74  ? -22.950 3.880   60.794  1.00 25.63  ? 74  GLU B O   1 
ATOM   2969  C CB  . GLU B  2 74  ? -23.164 2.840   63.809  1.00 26.86  ? 74  GLU B CB  1 
ATOM   2970  C CG  . GLU B  2 74  ? -23.782 2.428   65.143  1.00 31.52  ? 74  GLU B CG  1 
ATOM   2971  C CD  . GLU B  2 74  ? -24.416 3.590   65.911  1.00 38.26  ? 74  GLU B CD  1 
ATOM   2972  O OE1 . GLU B  2 74  ? -23.953 4.746   65.763  1.00 42.03  ? 74  GLU B OE1 1 
ATOM   2973  O OE2 . GLU B  2 74  ? -25.379 3.342   66.672  1.00 39.20  ? 74  GLU B OE2 1 
ATOM   2974  N N   . GLN B  2 75  ? -23.326 5.647   62.151  1.00 26.22  ? 75  GLN B N   1 
ATOM   2975  C CA  . GLN B  2 75  ? -22.791 6.651   61.238  1.00 26.47  ? 75  GLN B CA  1 
ATOM   2976  C C   . GLN B  2 75  ? -21.369 6.367   60.760  1.00 25.60  ? 75  GLN B C   1 
ATOM   2977  O O   . GLN B  2 75  ? -21.097 6.479   59.566  1.00 25.84  ? 75  GLN B O   1 
ATOM   2978  C CB  . GLN B  2 75  ? -22.859 8.047   61.863  1.00 27.04  ? 75  GLN B CB  1 
ATOM   2979  C CG  . GLN B  2 75  ? -23.044 9.169   60.843  1.00 30.17  ? 75  GLN B CG  1 
ATOM   2980  C CD  . GLN B  2 75  ? -24.467 9.246   60.297  1.00 35.35  ? 75  GLN B CD  1 
ATOM   2981  O OE1 . GLN B  2 75  ? -24.677 9.567   59.127  1.00 36.99  ? 75  GLN B OE1 1 
ATOM   2982  N NE2 . GLN B  2 75  ? -25.451 8.956   61.149  1.00 38.85  ? 75  GLN B NE2 1 
ATOM   2983  N N   . GLN B  2 76  ? -20.475 6.001   61.680  1.00 24.58  ? 76  GLN B N   1 
ATOM   2984  C CA  . GLN B  2 76  ? -19.053 5.843   61.345  1.00 23.97  ? 76  GLN B CA  1 
ATOM   2985  C C   . GLN B  2 76  ? -18.804 4.732   60.326  1.00 23.02  ? 76  GLN B C   1 
ATOM   2986  O O   . GLN B  2 76  ? -18.281 4.995   59.240  1.00 23.29  ? 76  GLN B O   1 
ATOM   2987  C CB  . GLN B  2 76  ? -18.189 5.646   62.597  1.00 24.13  ? 76  GLN B CB  1 
ATOM   2988  C CG  . GLN B  2 76  ? -16.694 5.860   62.341  1.00 25.60  ? 76  GLN B CG  1 
ATOM   2989  C CD  . GLN B  2 76  ? -15.843 5.764   63.598  1.00 27.03  ? 76  GLN B CD  1 
ATOM   2990  O OE1 . GLN B  2 76  ? -16.193 5.068   64.554  1.00 28.21  ? 76  GLN B OE1 1 
ATOM   2991  N NE2 . GLN B  2 76  ? -14.711 6.461   63.596  1.00 25.59  ? 76  GLN B NE2 1 
ATOM   2992  N N   . ILE B  2 77  ? -19.189 3.504   60.672  1.00 21.88  ? 77  ILE B N   1 
ATOM   2993  C CA  . ILE B  2 77  ? -19.049 2.367   59.760  1.00 20.58  ? 77  ILE B CA  1 
ATOM   2994  C C   . ILE B  2 77  ? -19.885 2.584   58.488  1.00 19.54  ? 77  ILE B C   1 
ATOM   2995  O O   . ILE B  2 77  ? -19.498 2.158   57.391  1.00 18.91  ? 77  ILE B O   1 
ATOM   2996  C CB  . ILE B  2 77  ? -19.377 1.010   60.461  1.00 20.60  ? 77  ILE B CB  1 
ATOM   2997  C CG1 . ILE B  2 77  ? -19.076 -0.181  59.544  1.00 19.86  ? 77  ILE B CG1 1 
ATOM   2998  C CG2 . ILE B  2 77  ? -20.821 0.970   60.959  1.00 22.76  ? 77  ILE B CG2 1 
ATOM   2999  C CD1 . ILE B  2 77  ? -17.600 -0.370  59.235  1.00 21.59  ? 77  ILE B CD1 1 
ATOM   3000  N N   . GLY B  2 78  ? -21.014 3.273   58.648  1.00 17.89  ? 78  GLY B N   1 
ATOM   3001  C CA  . GLY B  2 78  ? -21.877 3.626   57.532  1.00 16.30  ? 78  GLY B CA  1 
ATOM   3002  C C   . GLY B  2 78  ? -21.178 4.549   56.560  1.00 15.59  ? 78  GLY B C   1 
ATOM   3003  O O   . GLY B  2 78  ? -21.346 4.419   55.347  1.00 16.25  ? 78  GLY B O   1 
ATOM   3004  N N   . ASN B  2 79  ? -20.392 5.484   57.095  1.00 14.77  ? 79  ASN B N   1 
ATOM   3005  C CA  . ASN B  2 79  ? -19.634 6.432   56.276  1.00 14.08  ? 79  ASN B CA  1 
ATOM   3006  C C   . ASN B  2 79  ? -18.453 5.768   55.579  1.00 13.54  ? 79  ASN B C   1 
ATOM   3007  O O   . ASN B  2 79  ? -18.101 6.139   54.459  1.00 13.55  ? 79  ASN B O   1 
ATOM   3008  C CB  . ASN B  2 79  ? -19.168 7.635   57.105  1.00 13.53  ? 79  ASN B CB  1 
ATOM   3009  C CG  . ASN B  2 79  ? -20.233 8.721   57.215  1.00 16.23  ? 79  ASN B CG  1 
ATOM   3010  O OD1 . ASN B  2 79  ? -20.821 9.135   56.213  1.00 20.73  ? 79  ASN B OD1 1 
ATOM   3011  N ND2 . ASN B  2 79  ? -20.476 9.196   58.435  1.00 15.50  ? 79  ASN B ND2 1 
ATOM   3012  N N   . VAL B  2 80  ? -17.853 4.785   56.249  1.00 12.63  ? 80  VAL B N   1 
ATOM   3013  C CA  . VAL B  2 80  ? -16.776 3.986   55.672  1.00 10.82  ? 80  VAL B CA  1 
ATOM   3014  C C   . VAL B  2 80  ? -17.300 3.182   54.485  1.00 10.70  ? 80  VAL B C   1 
ATOM   3015  O O   . VAL B  2 80  ? -16.660 3.128   53.440  1.00 11.41  ? 80  VAL B O   1 
ATOM   3016  C CB  . VAL B  2 80  ? -16.148 3.037   56.721  1.00 10.72  ? 80  VAL B CB  1 
ATOM   3017  C CG1 . VAL B  2 80  ? -15.138 2.096   56.072  1.00 8.87   ? 80  VAL B CG1 1 
ATOM   3018  C CG2 . VAL B  2 80  ? -15.492 3.833   57.840  1.00 9.03   ? 80  VAL B CG2 1 
ATOM   3019  N N   . ILE B  2 81  ? -18.469 2.570   54.657  1.00 10.95  ? 81  ILE B N   1 
ATOM   3020  C CA  . ILE B  2 81  ? -19.118 1.788   53.607  1.00 11.67  ? 81  ILE B CA  1 
ATOM   3021  C C   . ILE B  2 81  ? -19.411 2.649   52.374  1.00 12.67  ? 81  ILE B C   1 
ATOM   3022  O O   . ILE B  2 81  ? -19.014 2.302   51.258  1.00 12.33  ? 81  ILE B O   1 
ATOM   3023  C CB  . ILE B  2 81  ? -20.395 1.092   54.146  1.00 11.85  ? 81  ILE B CB  1 
ATOM   3024  C CG1 . ILE B  2 81  ? -20.019 -0.213  54.853  1.00 12.02  ? 81  ILE B CG1 1 
ATOM   3025  C CG2 . ILE B  2 81  ? -21.398 0.822   53.031  1.00 10.88  ? 81  ILE B CG2 1 
ATOM   3026  C CD1 . ILE B  2 81  ? -21.102 -0.771  55.761  1.00 12.25  ? 81  ILE B CD1 1 
ATOM   3027  N N   . ASN B  2 82  ? -20.085 3.778   52.585  1.00 14.06  ? 82  ASN B N   1 
ATOM   3028  C CA  . ASN B  2 82  ? -20.344 4.726   51.508  1.00 15.14  ? 82  ASN B CA  1 
ATOM   3029  C C   . ASN B  2 82  ? -19.052 5.148   50.807  1.00 15.01  ? 82  ASN B C   1 
ATOM   3030  O O   . ASN B  2 82  ? -18.970 5.089   49.577  1.00 16.06  ? 82  ASN B O   1 
ATOM   3031  C CB  . ASN B  2 82  ? -21.125 5.937   52.022  1.00 15.70  ? 82  ASN B CB  1 
ATOM   3032  C CG  . ASN B  2 82  ? -22.607 5.639   52.228  1.00 21.20  ? 82  ASN B CG  1 
ATOM   3033  O OD1 . ASN B  2 82  ? -23.054 4.496   52.097  1.00 21.00  ? 82  ASN B OD1 1 
ATOM   3034  N ND2 . ASN B  2 82  ? -23.374 6.678   52.554  1.00 31.89  ? 82  ASN B ND2 1 
ATOM   3035  N N   . TRP B  2 83  ? -18.043 5.535   51.589  1.00 14.38  ? 83  TRP B N   1 
ATOM   3036  C CA  . TRP B  2 83  ? -16.738 5.920   51.049  1.00 14.67  ? 83  TRP B CA  1 
ATOM   3037  C C   . TRP B  2 83  ? -16.185 4.847   50.115  1.00 14.66  ? 83  TRP B C   1 
ATOM   3038  O O   . TRP B  2 83  ? -15.805 5.145   48.981  1.00 14.99  ? 83  TRP B O   1 
ATOM   3039  C CB  . TRP B  2 83  ? -15.736 6.189   52.174  1.00 15.62  ? 83  TRP B CB  1 
ATOM   3040  C CG  . TRP B  2 83  ? -14.469 6.857   51.705  1.00 20.15  ? 83  TRP B CG  1 
ATOM   3041  C CD1 . TRP B  2 83  ? -14.183 8.189   51.759  1.00 23.05  ? 83  TRP B CD1 1 
ATOM   3042  C CD2 . TRP B  2 83  ? -13.324 6.225   51.112  1.00 25.58  ? 83  TRP B CD2 1 
ATOM   3043  N NE1 . TRP B  2 83  ? -12.935 8.431   51.235  1.00 25.89  ? 83  TRP B NE1 1 
ATOM   3044  C CE2 . TRP B  2 83  ? -12.385 7.244   50.831  1.00 27.01  ? 83  TRP B CE2 1 
ATOM   3045  C CE3 . TRP B  2 83  ? -13.000 4.898   50.790  1.00 27.98  ? 83  TRP B CE3 1 
ATOM   3046  C CZ2 . TRP B  2 83  ? -11.141 6.980   50.241  1.00 29.72  ? 83  TRP B CZ2 1 
ATOM   3047  C CZ3 . TRP B  2 83  ? -11.765 4.634   50.199  1.00 28.56  ? 83  TRP B CZ3 1 
ATOM   3048  C CH2 . TRP B  2 83  ? -10.851 5.673   49.932  1.00 30.80  ? 83  TRP B CH2 1 
ATOM   3049  N N   . THR B  2 84  ? -16.144 3.605   50.601  1.00 13.40  ? 84  THR B N   1 
ATOM   3050  C CA  . THR B  2 84  ? -15.632 2.472   49.833  1.00 12.11  ? 84  THR B CA  1 
ATOM   3051  C C   . THR B  2 84  ? -16.473 2.213   48.577  1.00 12.21  ? 84  THR B C   1 
ATOM   3052  O O   . THR B  2 84  ? -15.924 1.992   47.496  1.00 12.16  ? 84  THR B O   1 
ATOM   3053  C CB  . THR B  2 84  ? -15.527 1.200   50.716  1.00 12.36  ? 84  THR B CB  1 
ATOM   3054  O OG1 . THR B  2 84  ? -14.688 1.471   51.845  1.00 10.25  ? 84  THR B OG1 1 
ATOM   3055  C CG2 . THR B  2 84  ? -14.936 0.033   49.949  1.00 11.02  ? 84  THR B CG2 1 
ATOM   3056  N N   . ARG B  2 85  ? -17.799 2.257   48.714  1.00 12.00  ? 85  ARG B N   1 
ATOM   3057  C CA  . ARG B  2 85  ? -18.685 2.015   47.574  1.00 10.90  ? 85  ARG B CA  1 
ATOM   3058  C C   . ARG B  2 85  ? -18.482 3.049   46.480  1.00 10.72  ? 85  ARG B C   1 
ATOM   3059  O O   . ARG B  2 85  ? -18.341 2.696   45.309  1.00 10.65  ? 85  ARG B O   1 
ATOM   3060  C CB  . ARG B  2 85  ? -20.156 1.989   47.985  1.00 10.76  ? 85  ARG B CB  1 
ATOM   3061  C CG  . ARG B  2 85  ? -21.082 1.578   46.840  1.00 9.33   ? 85  ARG B CG  1 
ATOM   3062  C CD  . ARG B  2 85  ? -22.548 1.672   47.210  1.00 10.92  ? 85  ARG B CD  1 
ATOM   3063  N NE  . ARG B  2 85  ? -22.901 0.718   48.258  1.00 13.86  ? 85  ARG B NE  1 
ATOM   3064  C CZ  . ARG B  2 85  ? -23.122 1.037   49.529  1.00 11.60  ? 85  ARG B CZ  1 
ATOM   3065  N NH1 . ARG B  2 85  ? -23.048 2.302   49.933  1.00 13.92  ? 85  ARG B NH1 1 
ATOM   3066  N NH2 . ARG B  2 85  ? -23.426 0.086   50.397  1.00 9.95   ? 85  ARG B NH2 1 
ATOM   3067  N N   . ASP B  2 86  ? -18.471 4.324   46.866  1.00 10.48  ? 86  ASP B N   1 
ATOM   3068  C CA  . ASP B  2 86  ? -18.292 5.409   45.902  1.00 10.21  ? 86  ASP B CA  1 
ATOM   3069  C C   . ASP B  2 86  ? -16.965 5.270   45.164  1.00 9.29   ? 86  ASP B C   1 
ATOM   3070  O O   . ASP B  2 86  ? -16.898 5.523   43.964  1.00 9.49   ? 86  ASP B O   1 
ATOM   3071  C CB  . ASP B  2 86  ? -18.419 6.781   46.574  1.00 10.24  ? 86  ASP B CB  1 
ATOM   3072  C CG  . ASP B  2 86  ? -19.855 7.112   46.976  1.00 12.13  ? 86  ASP B CG  1 
ATOM   3073  O OD1 . ASP B  2 86  ? -20.771 6.324   46.665  1.00 14.47  ? 86  ASP B OD1 1 
ATOM   3074  O OD2 . ASP B  2 86  ? -20.071 8.169   47.607  1.00 17.97  ? 86  ASP B OD2 1 
ATOM   3075  N N   . ALA B  2 87  ? -15.927 4.846   45.885  1.00 8.77   ? 87  ALA B N   1 
ATOM   3076  C CA  . ALA B  2 87  ? -14.622 4.561   45.294  1.00 8.51   ? 87  ALA B CA  1 
ATOM   3077  C C   . ALA B  2 87  ? -14.706 3.440   44.260  1.00 9.24   ? 87  ALA B C   1 
ATOM   3078  O O   . ALA B  2 87  ? -14.096 3.536   43.193  1.00 9.65   ? 87  ALA B O   1 
ATOM   3079  C CB  . ALA B  2 87  ? -13.614 4.216   46.372  1.00 8.57   ? 87  ALA B CB  1 
ATOM   3080  N N   . MET B  2 88  ? -15.461 2.385   44.574  1.00 9.44   ? 88  MET B N   1 
ATOM   3081  C CA  . MET B  2 88  ? -15.730 1.316   43.607  1.00 10.85  ? 88  MET B CA  1 
ATOM   3082  C C   . MET B  2 88  ? -16.460 1.854   42.376  1.00 10.84  ? 88  MET B C   1 
ATOM   3083  O O   . MET B  2 88  ? -16.104 1.514   41.248  1.00 11.56  ? 88  MET B O   1 
ATOM   3084  C CB  . MET B  2 88  ? -16.547 0.179   44.232  1.00 11.55  ? 88  MET B CB  1 
ATOM   3085  C CG  . MET B  2 88  ? -15.914 -0.485  45.433  1.00 14.49  ? 88  MET B CG  1 
ATOM   3086  S SD  . MET B  2 88  ? -14.268 -1.136  45.115  1.00 23.55  ? 88  MET B SD  1 
ATOM   3087  C CE  . MET B  2 88  ? -13.853 -1.688  46.766  1.00 23.75  ? 88  MET B CE  1 
ATOM   3088  N N   . THR B  2 89  ? -17.473 2.689   42.604  1.00 10.74  ? 89  THR B N   1 
ATOM   3089  C CA  . THR B  2 89  ? -18.236 3.325   41.528  1.00 10.76  ? 89  THR B CA  1 
ATOM   3090  C C   . THR B  2 89  ? -17.301 4.152   40.648  1.00 11.18  ? 89  THR B C   1 
ATOM   3091  O O   . THR B  2 89  ? -17.425 4.147   39.424  1.00 11.32  ? 89  THR B O   1 
ATOM   3092  C CB  . THR B  2 89  ? -19.387 4.213   42.086  1.00 10.01  ? 89  THR B CB  1 
ATOM   3093  O OG1 . THR B  2 89  ? -20.277 3.411   42.868  1.00 11.70  ? 89  THR B OG1 1 
ATOM   3094  C CG2 . THR B  2 89  ? -20.185 4.863   40.968  1.00 9.89   ? 89  THR B CG2 1 
ATOM   3095  N N   . GLU B  2 90  ? -16.357 4.842   41.280  1.00 12.13  ? 90  GLU B N   1 
ATOM   3096  C CA  . GLU B  2 90  ? -15.382 5.652   40.567  1.00 13.56  ? 90  GLU B CA  1 
ATOM   3097  C C   . GLU B  2 90  ? -14.537 4.778   39.649  1.00 13.37  ? 90  GLU B C   1 
ATOM   3098  O O   . GLU B  2 90  ? -14.375 5.088   38.465  1.00 13.76  ? 90  GLU B O   1 
ATOM   3099  C CB  . GLU B  2 90  ? -14.496 6.425   41.550  1.00 14.20  ? 90  GLU B CB  1 
ATOM   3100  C CG  . GLU B  2 90  ? -13.608 7.478   40.889  1.00 19.83  ? 90  GLU B CG  1 
ATOM   3101  C CD  . GLU B  2 90  ? -13.064 8.505   41.870  1.00 28.81  ? 90  GLU B CD  1 
ATOM   3102  O OE1 . GLU B  2 90  ? -12.677 8.120   42.999  1.00 31.28  ? 90  GLU B OE1 1 
ATOM   3103  O OE2 . GLU B  2 90  ? -13.020 9.702   41.505  1.00 30.94  ? 90  GLU B OE2 1 
ATOM   3104  N N   . ILE B  2 91  ? -14.027 3.678   40.200  1.00 12.96  ? 91  ILE B N   1 
ATOM   3105  C CA  . ILE B  2 91  ? -13.178 2.747   39.462  1.00 12.47  ? 91  ILE B CA  1 
ATOM   3106  C C   . ILE B  2 91  ? -13.922 2.108   38.281  1.00 12.45  ? 91  ILE B C   1 
ATOM   3107  O O   . ILE B  2 91  ? -13.426 2.125   37.148  1.00 13.25  ? 91  ILE B O   1 
ATOM   3108  C CB  . ILE B  2 91  ? -12.559 1.688   40.409  1.00 12.63  ? 91  ILE B CB  1 
ATOM   3109  C CG1 . ILE B  2 91  ? -11.514 2.351   41.310  1.00 10.85  ? 91  ILE B CG1 1 
ATOM   3110  C CG2 . ILE B  2 91  ? -11.912 0.548   39.628  1.00 12.25  ? 91  ILE B CG2 1 
ATOM   3111  C CD1 . ILE B  2 91  ? -11.164 1.564   42.541  1.00 8.89   ? 91  ILE B CD1 1 
ATOM   3112  N N   . TRP B  2 92  ? -15.114 1.574   38.538  1.00 11.12  ? 92  TRP B N   1 
ATOM   3113  C CA  . TRP B  2 92  ? -15.892 0.911   37.492  1.00 10.32  ? 92  TRP B CA  1 
ATOM   3114  C C   . TRP B  2 92  ? -16.433 1.837   36.400  1.00 10.33  ? 92  TRP B C   1 
ATOM   3115  O O   . TRP B  2 92  ? -16.561 1.425   35.243  1.00 10.10  ? 92  TRP B O   1 
ATOM   3116  C CB  . TRP B  2 92  ? -17.007 0.057   38.092  1.00 10.28  ? 92  TRP B CB  1 
ATOM   3117  C CG  . TRP B  2 92  ? -16.504 -1.265  38.572  1.00 9.16   ? 92  TRP B CG  1 
ATOM   3118  C CD1 . TRP B  2 92  ? -16.448 -1.701  39.860  1.00 9.51   ? 92  TRP B CD1 1 
ATOM   3119  C CD2 . TRP B  2 92  ? -15.962 -2.318  37.767  1.00 7.61   ? 92  TRP B CD2 1 
ATOM   3120  N NE1 . TRP B  2 92  ? -15.915 -2.966  39.909  1.00 10.32  ? 92  TRP B NE1 1 
ATOM   3121  C CE2 . TRP B  2 92  ? -15.606 -3.367  38.637  1.00 7.85   ? 92  TRP B CE2 1 
ATOM   3122  C CE3 . TRP B  2 92  ? -15.745 -2.478  36.392  1.00 8.26   ? 92  TRP B CE3 1 
ATOM   3123  C CZ2 . TRP B  2 92  ? -15.046 -4.560  38.181  1.00 8.48   ? 92  TRP B CZ2 1 
ATOM   3124  C CZ3 . TRP B  2 92  ? -15.184 -3.663  35.941  1.00 9.28   ? 92  TRP B CZ3 1 
ATOM   3125  C CH2 . TRP B  2 92  ? -14.846 -4.688  36.833  1.00 6.77   ? 92  TRP B CH2 1 
ATOM   3126  N N   . SER B  2 93  ? -16.744 3.078   36.763  1.00 9.57   ? 93  SER B N   1 
ATOM   3127  C CA  . SER B  2 93  ? -17.153 4.071   35.779  1.00 9.21   ? 93  SER B CA  1 
ATOM   3128  C C   . SER B  2 93  ? -15.980 4.398   34.859  1.00 9.92   ? 93  SER B C   1 
ATOM   3129  O O   . SER B  2 93  ? -16.140 4.488   33.635  1.00 10.81  ? 93  SER B O   1 
ATOM   3130  C CB  . SER B  2 93  ? -17.676 5.329   36.465  1.00 9.02   ? 93  SER B CB  1 
ATOM   3131  O OG  . SER B  2 93  ? -18.798 5.020   37.278  1.00 10.17  ? 93  SER B OG  1 
ATOM   3132  N N   . TYR B  2 94  ? -14.799 4.550   35.450  1.00 9.54   ? 94  TYR B N   1 
ATOM   3133  C CA  . TYR B  2 94  ? -13.583 4.770   34.684  1.00 9.93   ? 94  TYR B CA  1 
ATOM   3134  C C   . TYR B  2 94  ? -13.292 3.571   33.772  1.00 10.73  ? 94  TYR B C   1 
ATOM   3135  O O   . TYR B  2 94  ? -13.066 3.740   32.574  1.00 11.38  ? 94  TYR B O   1 
ATOM   3136  C CB  . TYR B  2 94  ? -12.403 5.063   35.617  1.00 9.16   ? 94  TYR B CB  1 
ATOM   3137  C CG  . TYR B  2 94  ? -11.051 4.990   34.947  1.00 9.64   ? 94  TYR B CG  1 
ATOM   3138  C CD1 . TYR B  2 94  ? -10.502 6.106   34.321  1.00 9.74   ? 94  TYR B CD1 1 
ATOM   3139  C CD2 . TYR B  2 94  ? -10.317 3.801   34.941  1.00 7.18   ? 94  TYR B CD2 1 
ATOM   3140  C CE1 . TYR B  2 94  ? -9.257  6.041   33.700  1.00 10.01  ? 94  TYR B CE1 1 
ATOM   3141  C CE2 . TYR B  2 94  ? -9.076  3.726   34.325  1.00 8.17   ? 94  TYR B CE2 1 
ATOM   3142  C CZ  . TYR B  2 94  ? -8.551  4.849   33.706  1.00 9.35   ? 94  TYR B CZ  1 
ATOM   3143  O OH  . TYR B  2 94  ? -7.319  4.780   33.094  1.00 12.53  ? 94  TYR B OH  1 
ATOM   3144  N N   . ASN B  2 95  ? -13.303 2.367   34.342  1.00 11.33  ? 95  ASN B N   1 
ATOM   3145  C CA  . ASN B  2 95  ? -13.083 1.145   33.572  1.00 11.68  ? 95  ASN B CA  1 
ATOM   3146  C C   . ASN B  2 95  ? -14.007 1.082   32.365  1.00 12.08  ? 95  ASN B C   1 
ATOM   3147  O O   . ASN B  2 95  ? -13.549 0.931   31.234  1.00 12.49  ? 95  ASN B O   1 
ATOM   3148  C CB  . ASN B  2 95  ? -13.304 -0.096  34.444  1.00 11.69  ? 95  ASN B CB  1 
ATOM   3149  C CG  . ASN B  2 95  ? -12.110 -0.431  35.325  1.00 12.14  ? 95  ASN B CG  1 
ATOM   3150  O OD1 . ASN B  2 95  ? -11.013 0.111   35.160  1.00 15.40  ? 95  ASN B OD1 1 
ATOM   3151  N ND2 . ASN B  2 95  ? -12.320 -1.346  36.265  1.00 8.33   ? 95  ASN B ND2 1 
ATOM   3152  N N   . ALA B  2 96  ? -15.307 1.220   32.630  1.00 12.07  ? 96  ALA B N   1 
ATOM   3153  C CA  . ALA B  2 96  ? -16.357 1.134   31.621  1.00 11.38  ? 96  ALA B CA  1 
ATOM   3154  C C   . ALA B  2 96  ? -16.200 2.184   30.532  1.00 11.59  ? 96  ALA B C   1 
ATOM   3155  O O   . ALA B  2 96  ? -16.244 1.864   29.344  1.00 12.18  ? 96  ALA B O   1 
ATOM   3156  C CB  . ALA B  2 96  ? -17.717 1.256   32.277  1.00 11.33  ? 96  ALA B CB  1 
ATOM   3157  N N   . GLU B  2 97  ? -16.011 3.435   30.939  1.00 11.56  ? 97  GLU B N   1 
ATOM   3158  C CA  . GLU B  2 97  ? -15.803 4.515   29.986  1.00 12.46  ? 97  GLU B CA  1 
ATOM   3159  C C   . GLU B  2 97  ? -14.615 4.192   29.080  1.00 12.17  ? 97  GLU B C   1 
ATOM   3160  O O   . GLU B  2 97  ? -14.738 4.238   27.857  1.00 13.05  ? 97  GLU B O   1 
ATOM   3161  C CB  . GLU B  2 97  ? -15.576 5.840   30.717  1.00 13.17  ? 97  GLU B CB  1 
ATOM   3162  C CG  . GLU B  2 97  ? -15.590 7.080   29.820  1.00 16.99  ? 97  GLU B CG  1 
ATOM   3163  C CD  . GLU B  2 97  ? -16.865 7.900   29.933  1.00 19.85  ? 97  GLU B CD  1 
ATOM   3164  O OE1 . GLU B  2 97  ? -17.150 8.675   28.998  1.00 22.38  ? 97  GLU B OE1 1 
ATOM   3165  O OE2 . GLU B  2 97  ? -17.578 7.783   30.952  1.00 22.23  ? 97  GLU B OE2 1 
ATOM   3166  N N   . LEU B  2 98  ? -13.484 3.836   29.689  1.00 11.63  ? 98  LEU B N   1 
ATOM   3167  C CA  . LEU B  2 98  ? -12.246 3.565   28.957  1.00 11.11  ? 98  LEU B CA  1 
ATOM   3168  C C   . LEU B  2 98  ? -12.347 2.330   28.064  1.00 10.79  ? 98  LEU B C   1 
ATOM   3169  O O   . LEU B  2 98  ? -11.993 2.389   26.885  1.00 10.65  ? 98  LEU B O   1 
ATOM   3170  C CB  . LEU B  2 98  ? -11.058 3.434   29.919  1.00 11.14  ? 98  LEU B CB  1 
ATOM   3171  C CG  . LEU B  2 98  ? -9.687  3.088   29.328  1.00 9.62   ? 98  LEU B CG  1 
ATOM   3172  C CD1 . LEU B  2 98  ? -9.190  4.192   28.405  1.00 11.41  ? 98  LEU B CD1 1 
ATOM   3173  C CD2 . LEU B  2 98  ? -8.695  2.842   30.438  1.00 8.00   ? 98  LEU B CD2 1 
ATOM   3174  N N   . LEU B  2 99  ? -12.822 1.219   28.626  1.00 9.56   ? 99  LEU B N   1 
ATOM   3175  C CA  . LEU B  2 99  ? -12.999 -0.001  27.854  1.00 9.21   ? 99  LEU B CA  1 
ATOM   3176  C C   . LEU B  2 99  ? -13.741 0.309   26.558  1.00 10.26  ? 99  LEU B C   1 
ATOM   3177  O O   . LEU B  2 99  ? -13.236 0.018   25.472  1.00 11.25  ? 99  LEU B O   1 
ATOM   3178  C CB  . LEU B  2 99  ? -13.759 -1.059  28.656  1.00 8.87   ? 99  LEU B CB  1 
ATOM   3179  C CG  . LEU B  2 99  ? -14.267 -2.265  27.859  1.00 8.15   ? 99  LEU B CG  1 
ATOM   3180  C CD1 . LEU B  2 99  ? -13.148 -3.267  27.622  1.00 7.34   ? 99  LEU B CD1 1 
ATOM   3181  C CD2 . LEU B  2 99  ? -15.450 -2.923  28.557  1.00 3.59   ? 99  LEU B CD2 1 
ATOM   3182  N N   . VAL B  2 100 ? -14.921 0.921   26.685  1.00 9.17   ? 100 VAL B N   1 
ATOM   3183  C CA  . VAL B  2 100 ? -15.780 1.200   25.539  1.00 8.07   ? 100 VAL B CA  1 
ATOM   3184  C C   . VAL B  2 100 ? -15.081 2.125   24.546  1.00 8.85   ? 100 VAL B C   1 
ATOM   3185  O O   . VAL B  2 100 ? -15.135 1.894   23.342  1.00 9.01   ? 100 VAL B O   1 
ATOM   3186  C CB  . VAL B  2 100 ? -17.165 1.771   25.970  1.00 8.29   ? 100 VAL B CB  1 
ATOM   3187  C CG1 . VAL B  2 100 ? -17.916 2.351   24.787  1.00 3.72   ? 100 VAL B CG1 1 
ATOM   3188  C CG2 . VAL B  2 100 ? -18.003 0.694   26.638  1.00 5.59   ? 100 VAL B CG2 1 
ATOM   3189  N N   . ALA B  2 101 ? -14.412 3.156   25.053  1.00 9.73   ? 101 ALA B N   1 
ATOM   3190  C CA  . ALA B  2 101 ? -13.719 4.109   24.191  1.00 10.54  ? 101 ALA B CA  1 
ATOM   3191  C C   . ALA B  2 101 ? -12.607 3.414   23.414  1.00 11.96  ? 101 ALA B C   1 
ATOM   3192  O O   . ALA B  2 101 ? -12.478 3.595   22.201  1.00 12.25  ? 101 ALA B O   1 
ATOM   3193  C CB  . ALA B  2 101 ? -13.168 5.271   25.000  1.00 9.28   ? 101 ALA B CB  1 
ATOM   3194  N N   . MET B  2 102 ? -11.828 2.600   24.125  1.00 14.02  ? 102 MET B N   1 
ATOM   3195  C CA  . MET B  2 102 ? -10.686 1.885   23.562  1.00 15.43  ? 102 MET B CA  1 
ATOM   3196  C C   . MET B  2 102 ? -11.134 0.880   22.508  1.00 15.25  ? 102 MET B C   1 
ATOM   3197  O O   . MET B  2 102 ? -10.523 0.776   21.438  1.00 15.16  ? 102 MET B O   1 
ATOM   3198  C CB  . MET B  2 102 ? -9.928  1.170   24.676  1.00 16.25  ? 102 MET B CB  1 
ATOM   3199  C CG  . MET B  2 102 ? -8.661  0.477   24.223  1.00 23.80  ? 102 MET B CG  1 
ATOM   3200  S SD  . MET B  2 102 ? -8.473  -1.106  25.053  1.00 37.41  ? 102 MET B SD  1 
ATOM   3201  C CE  . MET B  2 102 ? -9.798  -2.048  24.293  1.00 33.37  ? 102 MET B CE  1 
ATOM   3202  N N   . GLU B  2 103 ? -12.206 0.152   22.821  1.00 15.13  ? 103 GLU B N   1 
ATOM   3203  C CA  . GLU B  2 103 ? -12.789 -0.814  21.900  1.00 15.01  ? 103 GLU B CA  1 
ATOM   3204  C C   . GLU B  2 103 ? -13.284 -0.135  20.630  1.00 14.96  ? 103 GLU B C   1 
ATOM   3205  O O   . GLU B  2 103 ? -12.975 -0.585  19.526  1.00 15.75  ? 103 GLU B O   1 
ATOM   3206  C CB  . GLU B  2 103 ? -13.929 -1.591  22.565  1.00 15.67  ? 103 GLU B CB  1 
ATOM   3207  C CG  . GLU B  2 103 ? -13.493 -2.548  23.684  1.00 16.81  ? 103 GLU B CG  1 
ATOM   3208  C CD  . GLU B  2 103 ? -12.817 -3.824  23.187  1.00 17.82  ? 103 GLU B CD  1 
ATOM   3209  O OE1 . GLU B  2 103 ? -12.444 -3.910  22.000  1.00 19.75  ? 103 GLU B OE1 1 
ATOM   3210  O OE2 . GLU B  2 103 ? -12.655 -4.753  23.999  1.00 20.12  ? 103 GLU B OE2 1 
ATOM   3211  N N   . ASN B  2 104 ? -14.031 0.956   20.790  1.00 13.97  ? 104 ASN B N   1 
ATOM   3212  C CA  . ASN B  2 104 ? -14.569 1.697   19.644  1.00 13.22  ? 104 ASN B CA  1 
ATOM   3213  C C   . ASN B  2 104 ? -13.490 2.226   18.702  1.00 12.52  ? 104 ASN B C   1 
ATOM   3214  O O   . ASN B  2 104 ? -13.682 2.251   17.488  1.00 12.60  ? 104 ASN B O   1 
ATOM   3215  C CB  . ASN B  2 104 ? -15.490 2.831   20.101  1.00 12.99  ? 104 ASN B CB  1 
ATOM   3216  C CG  . ASN B  2 104 ? -16.757 2.324   20.759  1.00 12.47  ? 104 ASN B CG  1 
ATOM   3217  O OD1 . ASN B  2 104 ? -17.069 1.135   20.705  1.00 12.78  ? 104 ASN B OD1 1 
ATOM   3218  N ND2 . ASN B  2 104 ? -17.495 3.228   21.389  1.00 13.61  ? 104 ASN B ND2 1 
ATOM   3219  N N   . GLN B  2 105 ? -12.363 2.650   19.265  1.00 11.69  ? 105 GLN B N   1 
ATOM   3220  C CA  . GLN B  2 105 ? -11.218 3.045   18.461  1.00 11.48  ? 105 GLN B CA  1 
ATOM   3221  C C   . GLN B  2 105 ? -10.774 1.847   17.631  1.00 11.82  ? 105 GLN B C   1 
ATOM   3222  O O   . GLN B  2 105 ? -10.719 1.929   16.406  1.00 12.78  ? 105 GLN B O   1 
ATOM   3223  C CB  . GLN B  2 105 ? -10.071 3.536   19.347  1.00 11.32  ? 105 GLN B CB  1 
ATOM   3224  C CG  . GLN B  2 105 ? -8.980  4.297   18.602  1.00 11.14  ? 105 GLN B CG  1 
ATOM   3225  C CD  . GLN B  2 105 ? -9.363  5.738   18.289  1.00 12.67  ? 105 GLN B CD  1 
ATOM   3226  O OE1 . GLN B  2 105 ? -10.039 6.403   19.077  1.00 10.26  ? 105 GLN B OE1 1 
ATOM   3227  N NE2 . GLN B  2 105 ? -8.921  6.229   17.138  1.00 11.71  ? 105 GLN B NE2 1 
ATOM   3228  N N   . HIS B  2 106 ? -10.491 0.732   18.306  1.00 11.51  ? 106 HIS B N   1 
ATOM   3229  C CA  . HIS B  2 106 ? -10.022 -0.486  17.645  1.00 10.96  ? 106 HIS B CA  1 
ATOM   3230  C C   . HIS B  2 106 ? -11.027 -0.994  16.615  1.00 10.97  ? 106 HIS B C   1 
ATOM   3231  O O   . HIS B  2 106 ? -10.640 -1.375  15.513  1.00 9.88   ? 106 HIS B O   1 
ATOM   3232  C CB  . HIS B  2 106 ? -9.696  -1.577  18.675  1.00 10.86  ? 106 HIS B CB  1 
ATOM   3233  C CG  . HIS B  2 106 ? -9.160  -2.841  18.071  1.00 11.71  ? 106 HIS B CG  1 
ATOM   3234  N ND1 . HIS B  2 106 ? -9.869  -4.024  18.068  1.00 12.78  ? 106 HIS B ND1 1 
ATOM   3235  C CD2 . HIS B  2 106 ? -7.988  -3.106  17.445  1.00 11.75  ? 106 HIS B CD2 1 
ATOM   3236  C CE1 . HIS B  2 106 ? -9.155  -4.963  17.472  1.00 12.11  ? 106 HIS B CE1 1 
ATOM   3237  N NE2 . HIS B  2 106 ? -8.010  -4.432  17.083  1.00 11.70  ? 106 HIS B NE2 1 
ATOM   3238  N N   . THR B  2 107 ? -12.310 -0.978  16.979  1.00 11.36  ? 107 THR B N   1 
ATOM   3239  C CA  . THR B  2 107 ? -13.393 -1.403  16.090  1.00 12.02  ? 107 THR B CA  1 
ATOM   3240  C C   . THR B  2 107 ? -13.416 -0.631  14.757  1.00 13.05  ? 107 THR B C   1 
ATOM   3241  O O   . THR B  2 107 ? -13.434 -1.243  13.688  1.00 12.83  ? 107 THR B O   1 
ATOM   3242  C CB  . THR B  2 107 ? -14.763 -1.343  16.815  1.00 11.84  ? 107 THR B CB  1 
ATOM   3243  O OG1 . THR B  2 107 ? -14.901 -2.501  17.649  1.00 10.93  ? 107 THR B OG1 1 
ATOM   3244  C CG2 . THR B  2 107 ? -15.927 -1.294  15.828  1.00 9.15   ? 107 THR B CG2 1 
ATOM   3245  N N   . ILE B  2 108 ? -13.401 0.700   14.833  1.00 13.77  ? 108 ILE B N   1 
ATOM   3246  C CA  . ILE B  2 108 ? -13.385 1.561   13.646  1.00 14.46  ? 108 ILE B CA  1 
ATOM   3247  C C   . ILE B  2 108 ? -12.149 1.291   12.772  1.00 15.57  ? 108 ILE B C   1 
ATOM   3248  O O   . ILE B  2 108 ? -12.259 1.160   11.548  1.00 15.39  ? 108 ILE B O   1 
ATOM   3249  C CB  . ILE B  2 108 ? -13.483 3.063   14.043  1.00 14.54  ? 108 ILE B CB  1 
ATOM   3250  C CG1 . ILE B  2 108 ? -14.866 3.365   14.630  1.00 14.85  ? 108 ILE B CG1 1 
ATOM   3251  C CG2 . ILE B  2 108 ? -13.215 3.980   12.855  1.00 12.32  ? 108 ILE B CG2 1 
ATOM   3252  C CD1 . ILE B  2 108 ? -14.938 4.665   15.403  1.00 16.01  ? 108 ILE B CD1 1 
ATOM   3253  N N   . ASP B  2 109 ? -10.986 1.192   13.414  1.00 16.32  ? 109 ASP B N   1 
ATOM   3254  C CA  . ASP B  2 109 ? -9.721  0.933   12.726  1.00 17.29  ? 109 ASP B CA  1 
ATOM   3255  C C   . ASP B  2 109 ? -9.654  -0.466  12.127  1.00 17.63  ? 109 ASP B C   1 
ATOM   3256  O O   . ASP B  2 109 ? -9.091  -0.667  11.045  1.00 17.89  ? 109 ASP B O   1 
ATOM   3257  C CB  . ASP B  2 109 ? -8.550  1.146   13.683  1.00 17.44  ? 109 ASP B CB  1 
ATOM   3258  C CG  . ASP B  2 109 ? -8.373  2.596   14.061  1.00 19.30  ? 109 ASP B CG  1 
ATOM   3259  O OD1 . ASP B  2 109 ? -8.184  2.873   15.261  1.00 24.96  ? 109 ASP B OD1 1 
ATOM   3260  O OD2 . ASP B  2 109 ? -8.428  3.458   13.156  1.00 20.89  ? 109 ASP B OD2 1 
ATOM   3261  N N   . LEU B  2 110 ? -10.222 -1.424  12.852  1.00 17.43  ? 110 LEU B N   1 
ATOM   3262  C CA  . LEU B  2 110 ? -10.349 -2.805  12.408  1.00 17.12  ? 110 LEU B CA  1 
ATOM   3263  C C   . LEU B  2 110 ? -11.149 -2.869  11.108  1.00 17.05  ? 110 LEU B C   1 
ATOM   3264  O O   . LEU B  2 110 ? -10.733 -3.511  10.143  1.00 17.25  ? 110 LEU B O   1 
ATOM   3265  C CB  . LEU B  2 110 ? -11.023 -3.606  13.524  1.00 16.94  ? 110 LEU B CB  1 
ATOM   3266  C CG  . LEU B  2 110 ? -11.662 -4.985  13.425  1.00 20.28  ? 110 LEU B CG  1 
ATOM   3267  C CD1 . LEU B  2 110 ? -11.860 -5.482  14.848  1.00 22.04  ? 110 LEU B CD1 1 
ATOM   3268  C CD2 . LEU B  2 110 ? -12.997 -4.966  12.678  1.00 20.72  ? 110 LEU B CD2 1 
ATOM   3269  N N   . ALA B  2 111 ? -12.289 -2.181  11.082  1.00 16.61  ? 111 ALA B N   1 
ATOM   3270  C CA  . ALA B  2 111 ? -13.163 -2.191  9.915   1.00 15.78  ? 111 ALA B CA  1 
ATOM   3271  C C   . ALA B  2 111 ? -12.462 -1.533  8.734   1.00 15.30  ? 111 ALA B C   1 
ATOM   3272  O O   . ALA B  2 111 ? -12.543 -2.021  7.606   1.00 14.87  ? 111 ALA B O   1 
ATOM   3273  C CB  . ALA B  2 111 ? -14.471 -1.498  10.225  1.00 15.05  ? 111 ALA B CB  1 
ATOM   3274  N N   . ASP B  2 112 ? -11.762 -0.435  9.022   1.00 14.87  ? 112 ASP B N   1 
ATOM   3275  C CA  . ASP B  2 112 ? -10.928 0.266   8.055   1.00 15.11  ? 112 ASP B CA  1 
ATOM   3276  C C   . ASP B  2 112 ? -9.830  -0.660  7.523   1.00 15.69  ? 112 ASP B C   1 
ATOM   3277  O O   . ASP B  2 112 ? -9.558  -0.693  6.318   1.00 15.67  ? 112 ASP B O   1 
ATOM   3278  C CB  . ASP B  2 112 ? -10.310 1.509   8.709   1.00 15.17  ? 112 ASP B CB  1 
ATOM   3279  C CG  . ASP B  2 112 ? -9.728  2.487   7.700   1.00 16.53  ? 112 ASP B CG  1 
ATOM   3280  O OD1 . ASP B  2 112 ? -10.029 2.373   6.493   1.00 17.79  ? 112 ASP B OD1 1 
ATOM   3281  O OD2 . ASP B  2 112 ? -8.971  3.387   8.122   1.00 19.49  ? 112 ASP B OD2 1 
ATOM   3282  N N   . SER B  2 113 ? -9.217  -1.419  8.429   1.00 15.58  ? 113 SER B N   1 
ATOM   3283  C CA  . SER B  2 113 ? -8.187  -2.380  8.063   1.00 15.67  ? 113 SER B CA  1 
ATOM   3284  C C   . SER B  2 113 ? -8.695  -3.342  6.990   1.00 16.13  ? 113 SER B C   1 
ATOM   3285  O O   . SER B  2 113 ? -8.064  -3.482  5.944   1.00 17.10  ? 113 SER B O   1 
ATOM   3286  C CB  . SER B  2 113 ? -7.695  -3.140  9.297   1.00 15.47  ? 113 SER B CB  1 
ATOM   3287  O OG  . SER B  2 113 ? -6.880  -4.240  8.944   1.00 14.88  ? 113 SER B OG  1 
ATOM   3288  N N   . GLU B  2 114 ? -9.845  -3.971  7.236   1.00 15.90  ? 114 GLU B N   1 
ATOM   3289  C CA  . GLU B  2 114 ? -10.419 -4.942  6.295   1.00 15.83  ? 114 GLU B CA  1 
ATOM   3290  C C   . GLU B  2 114 ? -10.692 -4.349  4.913   1.00 16.18  ? 114 GLU B C   1 
ATOM   3291  O O   . GLU B  2 114 ? -10.502 -5.026  3.898   1.00 16.81  ? 114 GLU B O   1 
ATOM   3292  C CB  . GLU B  2 114 ? -11.695 -5.590  6.851   1.00 15.65  ? 114 GLU B CB  1 
ATOM   3293  C CG  . GLU B  2 114 ? -11.505 -6.481  8.090   1.00 16.17  ? 114 GLU B CG  1 
ATOM   3294  C CD  . GLU B  2 114 ? -10.519 -7.632  7.891   1.00 19.32  ? 114 GLU B CD  1 
ATOM   3295  O OE1 . GLU B  2 114 ? -10.500 -8.252  6.805   1.00 21.80  ? 114 GLU B OE1 1 
ATOM   3296  O OE2 . GLU B  2 114 ? -9.764  -7.925  8.838   1.00 20.06  ? 114 GLU B OE2 1 
ATOM   3297  N N   . MET B  2 115 ? -11.137 -3.093  4.875   1.00 16.03  ? 115 MET B N   1 
ATOM   3298  C CA  . MET B  2 115 ? -11.354 -2.392  3.612   1.00 15.76  ? 115 MET B CA  1 
ATOM   3299  C C   . MET B  2 115 ? -10.034 -2.273  2.856   1.00 16.11  ? 115 MET B C   1 
ATOM   3300  O O   . MET B  2 115 ? -9.969  -2.568  1.664   1.00 16.32  ? 115 MET B O   1 
ATOM   3301  C CB  . MET B  2 115 ? -11.982 -1.015  3.853   1.00 16.23  ? 115 MET B CB  1 
ATOM   3302  C CG  . MET B  2 115 ? -12.255 -0.188  2.592   1.00 16.75  ? 115 MET B CG  1 
ATOM   3303  S SD  . MET B  2 115 ? -13.741 -0.637  1.666   1.00 17.02  ? 115 MET B SD  1 
ATOM   3304  C CE  . MET B  2 115 ? -13.133 -1.939  0.593   1.00 17.35  ? 115 MET B CE  1 
ATOM   3305  N N   . SER B  2 116 ? -8.980  -1.867  3.562   1.00 16.97  ? 116 SER B N   1 
ATOM   3306  C CA  . SER B  2 116 ? -7.638  -1.794  2.982   1.00 17.48  ? 116 SER B CA  1 
ATOM   3307  C C   . SER B  2 116 ? -7.147  -3.155  2.476   1.00 17.66  ? 116 SER B C   1 
ATOM   3308  O O   . SER B  2 116 ? -6.610  -3.252  1.368   1.00 18.08  ? 116 SER B O   1 
ATOM   3309  C CB  . SER B  2 116 ? -6.645  -1.217  3.988   1.00 16.93  ? 116 SER B CB  1 
ATOM   3310  O OG  . SER B  2 116 ? -5.331  -1.228  3.458   1.00 20.89  ? 116 SER B OG  1 
ATOM   3311  N N   . LYS B  2 117 ? -7.339  -4.194  3.288   1.00 17.05  ? 117 LYS B N   1 
ATOM   3312  C CA  . LYS B  2 117 ? -6.938  -5.551  2.925   1.00 17.10  ? 117 LYS B CA  1 
ATOM   3313  C C   . LYS B  2 117 ? -7.580  -6.010  1.617   1.00 17.75  ? 117 LYS B C   1 
ATOM   3314  O O   . LYS B  2 117 ? -6.898  -6.541  0.740   1.00 18.68  ? 117 LYS B O   1 
ATOM   3315  C CB  . LYS B  2 117 ? -7.302  -6.537  4.026   1.00 16.75  ? 117 LYS B CB  1 
ATOM   3316  C CG  . LYS B  2 117 ? -6.536  -6.382  5.309   1.00 16.52  ? 117 LYS B CG  1 
ATOM   3317  C CD  . LYS B  2 117 ? -6.765  -7.603  6.170   1.00 15.14  ? 117 LYS B CD  1 
ATOM   3318  C CE  . LYS B  2 117 ? -6.778  -7.246  7.631   1.00 14.63  ? 117 LYS B CE  1 
ATOM   3319  N NZ  . LYS B  2 117 ? -6.956  -8.466  8.456   1.00 17.08  ? 117 LYS B NZ  1 
ATOM   3320  N N   . LEU B  2 118 ? -8.890  -5.803  1.497   1.00 17.15  ? 118 LEU B N   1 
ATOM   3321  C CA  . LEU B  2 118 ? -9.626  -6.208  0.310   1.00 17.25  ? 118 LEU B CA  1 
ATOM   3322  C C   . LEU B  2 118 ? -9.146  -5.415  -0.898  1.00 17.61  ? 118 LEU B C   1 
ATOM   3323  O O   . LEU B  2 118 ? -9.039  -5.956  -1.998  1.00 18.39  ? 118 LEU B O   1 
ATOM   3324  C CB  . LEU B  2 118 ? -11.130 -6.014  0.519   1.00 17.31  ? 118 LEU B CB  1 
ATOM   3325  C CG  . LEU B  2 118 ? -12.078 -6.340  -0.641  1.00 16.89  ? 118 LEU B CG  1 
ATOM   3326  C CD1 . LEU B  2 118 ? -12.150 -7.837  -0.908  1.00 16.39  ? 118 LEU B CD1 1 
ATOM   3327  C CD2 . LEU B  2 118 ? -13.464 -5.774  -0.376  1.00 15.20  ? 118 LEU B CD2 1 
ATOM   3328  N N   . TYR B  2 119 ? -8.849  -4.137  -0.672  1.00 17.18  ? 119 TYR B N   1 
ATOM   3329  C CA  . TYR B  2 119 ? -8.330  -3.246  -1.705  1.00 16.62  ? 119 TYR B CA  1 
ATOM   3330  C C   . TYR B  2 119 ? -6.962  -3.709  -2.204  1.00 16.56  ? 119 TYR B C   1 
ATOM   3331  O O   . TYR B  2 119 ? -6.770  -3.891  -3.407  1.00 16.57  ? 119 TYR B O   1 
ATOM   3332  C CB  . TYR B  2 119 ? -8.274  -1.809  -1.179  1.00 16.36  ? 119 TYR B CB  1 
ATOM   3333  C CG  . TYR B  2 119 ? -7.801  -0.780  -2.180  1.00 16.98  ? 119 TYR B CG  1 
ATOM   3334  C CD1 . TYR B  2 119 ? -8.671  -0.252  -3.136  1.00 16.56  ? 119 TYR B CD1 1 
ATOM   3335  C CD2 . TYR B  2 119 ? -6.484  -0.316  -2.158  1.00 18.14  ? 119 TYR B CD2 1 
ATOM   3336  C CE1 . TYR B  2 119 ? -8.235  0.704   -4.054  1.00 16.49  ? 119 TYR B CE1 1 
ATOM   3337  C CE2 . TYR B  2 119 ? -6.041  0.637   -3.070  1.00 16.73  ? 119 TYR B CE2 1 
ATOM   3338  C CZ  . TYR B  2 119 ? -6.918  1.143   -4.013  1.00 14.51  ? 119 TYR B CZ  1 
ATOM   3339  O OH  . TYR B  2 119 ? -6.474  2.087   -4.911  1.00 12.26  ? 119 TYR B OH  1 
ATOM   3340  N N   . GLU B  2 120 ? -6.025  -3.914  -1.279  1.00 16.39  ? 120 GLU B N   1 
ATOM   3341  C CA  . GLU B  2 120 ? -4.692  -4.407  -1.625  1.00 16.46  ? 120 GLU B CA  1 
ATOM   3342  C C   . GLU B  2 120 ? -4.731  -5.768  -2.304  1.00 16.38  ? 120 GLU B C   1 
ATOM   3343  O O   . GLU B  2 120 ? -3.926  -6.042  -3.197  1.00 16.17  ? 120 GLU B O   1 
ATOM   3344  C CB  . GLU B  2 120 ? -3.790  -4.481  -0.393  1.00 16.62  ? 120 GLU B CB  1 
ATOM   3345  C CG  . GLU B  2 120 ? -3.384  -3.135  0.184   1.00 19.33  ? 120 GLU B CG  1 
ATOM   3346  C CD  . GLU B  2 120 ? -2.707  -2.230  -0.827  1.00 21.27  ? 120 GLU B CD  1 
ATOM   3347  O OE1 . GLU B  2 120 ? -1.884  -2.731  -1.631  1.00 23.10  ? 120 GLU B OE1 1 
ATOM   3348  O OE2 . GLU B  2 120 ? -3.003  -1.014  -0.809  1.00 20.84  ? 120 GLU B OE2 1 
ATOM   3349  N N   . ARG B  2 121 ? -5.664  -6.617  -1.877  1.00 16.71  ? 121 ARG B N   1 
ATOM   3350  C CA  . ARG B  2 121 ? -5.815  -7.950  -2.454  1.00 16.84  ? 121 ARG B CA  1 
ATOM   3351  C C   . ARG B  2 121 ? -6.174  -7.857  -3.936  1.00 16.75  ? 121 ARG B C   1 
ATOM   3352  O O   . ARG B  2 121 ? -5.562  -8.531  -4.770  1.00 16.38  ? 121 ARG B O   1 
ATOM   3353  C CB  . ARG B  2 121 ? -6.855  -8.755  -1.677  1.00 17.07  ? 121 ARG B CB  1 
ATOM   3354  C CG  . ARG B  2 121 ? -6.895  -10.236 -2.016  1.00 21.05  ? 121 ARG B CG  1 
ATOM   3355  C CD  . ARG B  2 121 ? -8.108  -10.584 -2.865  1.00 27.77  ? 121 ARG B CD  1 
ATOM   3356  N NE  . ARG B  2 121 ? -9.329  -10.729 -2.073  1.00 31.94  ? 121 ARG B NE  1 
ATOM   3357  C CZ  . ARG B  2 121 ? -10.553 -10.841 -2.588  1.00 36.98  ? 121 ARG B CZ  1 
ATOM   3358  N NH1 . ARG B  2 121 ? -10.737 -10.816 -3.905  1.00 35.39  ? 121 ARG B NH1 1 
ATOM   3359  N NH2 . ARG B  2 121 ? -11.600 -10.975 -1.782  1.00 38.35  ? 121 ARG B NH2 1 
ATOM   3360  N N   . VAL B  2 122 ? -7.150  -7.004  -4.250  1.00 16.32  ? 122 VAL B N   1 
ATOM   3361  C CA  . VAL B  2 122 ? -7.568  -6.762  -5.632  1.00 16.06  ? 122 VAL B CA  1 
ATOM   3362  C C   . VAL B  2 122 ? -6.424  -6.153  -6.448  1.00 16.33  ? 122 VAL B C   1 
ATOM   3363  O O   . VAL B  2 122 ? -6.195  -6.541  -7.594  1.00 16.22  ? 122 VAL B O   1 
ATOM   3364  C CB  . VAL B  2 122 ? -8.845  -5.881  -5.697  1.00 16.00  ? 122 VAL B CB  1 
ATOM   3365  C CG1 . VAL B  2 122 ? -9.154  -5.448  -7.128  1.00 13.27  ? 122 VAL B CG1 1 
ATOM   3366  C CG2 . VAL B  2 122 ? -10.027 -6.638  -5.117  1.00 14.76  ? 122 VAL B CG2 1 
ATOM   3367  N N   . LYS B  2 123 ? -5.706  -5.213  -5.840  1.00 17.21  ? 123 LYS B N   1 
ATOM   3368  C CA  . LYS B  2 123 ? -4.563  -4.565  -6.477  1.00 17.78  ? 123 LYS B CA  1 
ATOM   3369  C C   . LYS B  2 123 ? -3.550  -5.597  -6.945  1.00 17.71  ? 123 LYS B C   1 
ATOM   3370  O O   . LYS B  2 123 ? -3.053  -5.522  -8.069  1.00 18.22  ? 123 LYS B O   1 
ATOM   3371  C CB  . LYS B  2 123 ? -3.894  -3.586  -5.514  1.00 18.13  ? 123 LYS B CB  1 
ATOM   3372  C CG  . LYS B  2 123 ? -2.872  -2.686  -6.179  1.00 22.17  ? 123 LYS B CG  1 
ATOM   3373  C CD  . LYS B  2 123 ? -1.973  -2.019  -5.161  1.00 27.55  ? 123 LYS B CD  1 
ATOM   3374  C CE  . LYS B  2 123 ? -0.742  -1.454  -5.839  1.00 29.58  ? 123 LYS B CE  1 
ATOM   3375  N NZ  . LYS B  2 123 ? 0.301   -1.096  -4.846  1.00 33.98  ? 123 LYS B NZ  1 
ATOM   3376  N N   . LYS B  2 124 ? -3.262  -6.562  -6.075  1.00 17.57  ? 124 LYS B N   1 
ATOM   3377  C CA  . LYS B  2 124 ? -2.309  -7.625  -6.371  1.00 16.65  ? 124 LYS B CA  1 
ATOM   3378  C C   . LYS B  2 124 ? -2.826  -8.569  -7.451  1.00 16.24  ? 124 LYS B C   1 
ATOM   3379  O O   . LYS B  2 124 ? -2.040  -9.089  -8.236  1.00 16.71  ? 124 LYS B O   1 
ATOM   3380  C CB  . LYS B  2 124 ? -1.954  -8.403  -5.099  1.00 16.84  ? 124 LYS B CB  1 
ATOM   3381  C CG  . LYS B  2 124 ? -1.054  -7.643  -4.118  1.00 16.63  ? 124 LYS B CG  1 
ATOM   3382  C CD  . LYS B  2 124 ? -0.825  -8.452  -2.841  1.00 16.44  ? 124 LYS B CD  1 
ATOM   3383  C CE  . LYS B  2 124 ? -0.108  -7.652  -1.764  1.00 16.19  ? 124 LYS B CE  1 
ATOM   3384  N NZ  . LYS B  2 124 ? -0.933  -6.514  -1.273  1.00 17.07  ? 124 LYS B NZ  1 
ATOM   3385  N N   . GLN B  2 125 ? -4.142  -8.780  -7.486  1.00 16.33  ? 125 GLN B N   1 
ATOM   3386  C CA  . GLN B  2 125 ? -4.781  -9.629  -8.496  1.00 16.74  ? 125 GLN B CA  1 
ATOM   3387  C C   . GLN B  2 125 ? -4.595  -9.077  -9.905  1.00 16.19  ? 125 GLN B C   1 
ATOM   3388  O O   . GLN B  2 125 ? -4.259  -9.820  -10.829 1.00 15.96  ? 125 GLN B O   1 
ATOM   3389  C CB  . GLN B  2 125 ? -6.283  -9.747  -8.236  1.00 18.08  ? 125 GLN B CB  1 
ATOM   3390  C CG  . GLN B  2 125 ? -6.705  -10.661 -7.104  1.00 22.08  ? 125 GLN B CG  1 
ATOM   3391  C CD  . GLN B  2 125 ? -8.216  -10.651 -6.912  1.00 28.24  ? 125 GLN B CD  1 
ATOM   3392  O OE1 . GLN B  2 125 ? -8.728  -10.047 -5.968  1.00 31.58  ? 125 GLN B OE1 1 
ATOM   3393  N NE2 . GLN B  2 125 ? -8.936  -11.299 -7.824  1.00 26.32  ? 125 GLN B NE2 1 
ATOM   3394  N N   . LEU B  2 126 ? -4.822  -7.773  -10.055 1.00 15.56  ? 126 LEU B N   1 
ATOM   3395  C CA  . LEU B  2 126 ? -4.822  -7.113  -11.362 1.00 14.97  ? 126 LEU B CA  1 
ATOM   3396  C C   . LEU B  2 126 ? -3.422  -6.913  -11.950 1.00 15.04  ? 126 LEU B C   1 
ATOM   3397  O O   . LEU B  2 126 ? -3.283  -6.699  -13.158 1.00 14.44  ? 126 LEU B O   1 
ATOM   3398  C CB  . LEU B  2 126 ? -5.588  -5.785  -11.291 1.00 14.48  ? 126 LEU B CB  1 
ATOM   3399  C CG  . LEU B  2 126 ? -7.059  -5.883  -10.861 1.00 13.95  ? 126 LEU B CG  1 
ATOM   3400  C CD1 . LEU B  2 126 ? -7.637  -4.513  -10.541 1.00 7.66   ? 126 LEU B CD1 1 
ATOM   3401  C CD2 . LEU B  2 126 ? -7.907  -6.597  -11.910 1.00 7.20   ? 126 LEU B CD2 1 
ATOM   3402  N N   . ARG B  2 127 ? -2.398  -6.981  -11.096 1.00 14.89  ? 127 ARG B N   1 
ATOM   3403  C CA  . ARG B  2 127 ? -0.987  -6.893  -11.517 1.00 15.49  ? 127 ARG B CA  1 
ATOM   3404  C C   . ARG B  2 127 ? -0.635  -5.629  -12.315 1.00 15.09  ? 127 ARG B C   1 
ATOM   3405  O O   . ARG B  2 127 ? -0.590  -4.529  -11.764 1.00 15.56  ? 127 ARG B O   1 
ATOM   3406  C CB  . ARG B  2 127 ? -0.560  -8.153  -12.296 1.00 15.63  ? 127 ARG B CB  1 
ATOM   3407  C CG  . ARG B  2 127 ? -0.391  -9.397  -11.447 1.00 14.69  ? 127 ARG B CG  1 
ATOM   3408  C CD  . ARG B  2 127 ? 0.902   -9.360  -10.655 1.00 16.39  ? 127 ARG B CD  1 
ATOM   3409  N NE  . ARG B  2 127 ? 2.072   -9.658  -11.480 1.00 17.92  ? 127 ARG B NE  1 
ATOM   3410  C CZ  . ARG B  2 127 ? 2.569   -10.878 -11.672 1.00 17.29  ? 127 ARG B CZ  1 
ATOM   3411  N NH1 . ARG B  2 127 ? 2.001   -11.935 -11.105 1.00 19.05  ? 127 ARG B NH1 1 
ATOM   3412  N NH2 . ARG B  2 127 ? 3.639   -11.042 -12.435 1.00 13.87  ? 127 ARG B NH2 1 
ATOM   3413  N N   . GLU B  2 128 ? -0.379  -5.806  -13.607 1.00 14.56  ? 128 GLU B N   1 
ATOM   3414  C CA  . GLU B  2 128 ? 0.021   -4.708  -14.481 1.00 14.32  ? 128 GLU B CA  1 
ATOM   3415  C C   . GLU B  2 128 ? -1.084  -4.362  -15.475 1.00 14.59  ? 128 GLU B C   1 
ATOM   3416  O O   . GLU B  2 128 ? -0.854  -3.628  -16.436 1.00 15.43  ? 128 GLU B O   1 
ATOM   3417  C CB  . GLU B  2 128 ? 1.316   -5.056  -15.226 1.00 13.92  ? 128 GLU B CB  1 
ATOM   3418  C CG  . GLU B  2 128 ? 2.498   -5.417  -14.326 1.00 12.96  ? 128 GLU B CG  1 
ATOM   3419  C CD  . GLU B  2 128 ? 2.972   -4.267  -13.444 1.00 11.53  ? 128 GLU B CD  1 
ATOM   3420  O OE1 . GLU B  2 128 ? 3.063   -3.124  -13.939 1.00 11.85  ? 128 GLU B OE1 1 
ATOM   3421  O OE2 . GLU B  2 128 ? 3.263   -4.510  -12.251 1.00 10.14  ? 128 GLU B OE2 1 
ATOM   3422  N N   . ASN B  2 129 ? -2.283  -4.885  -15.221 1.00 14.44  ? 129 ASN B N   1 
ATOM   3423  C CA  . ASN B  2 129 ? -3.437  -4.693  -16.097 1.00 14.18  ? 129 ASN B CA  1 
ATOM   3424  C C   . ASN B  2 129 ? -4.348  -3.523  -15.704 1.00 14.59  ? 129 ASN B C   1 
ATOM   3425  O O   . ASN B  2 129 ? -5.307  -3.210  -16.421 1.00 15.25  ? 129 ASN B O   1 
ATOM   3426  C CB  . ASN B  2 129 ? -4.252  -5.993  -16.186 1.00 13.91  ? 129 ASN B CB  1 
ATOM   3427  C CG  . ASN B  2 129 ? -3.453  -7.150  -16.777 1.00 15.63  ? 129 ASN B CG  1 
ATOM   3428  O OD1 . ASN B  2 129 ? -2.286  -6.993  -17.147 1.00 17.40  ? 129 ASN B OD1 1 
ATOM   3429  N ND2 . ASN B  2 129 ? -4.081  -8.322  -16.865 1.00 13.18  ? 129 ASN B ND2 1 
ATOM   3430  N N   . ALA B  2 130 ? -4.046  -2.877  -14.577 1.00 14.24  ? 130 ALA B N   1 
ATOM   3431  C CA  . ALA B  2 130 ? -4.893  -1.810  -14.043 1.00 14.31  ? 130 ALA B CA  1 
ATOM   3432  C C   . ALA B  2 130 ? -4.118  -0.782  -13.219 1.00 15.33  ? 130 ALA B C   1 
ATOM   3433  O O   . ALA B  2 130 ? -3.050  -1.080  -12.674 1.00 16.45  ? 130 ALA B O   1 
ATOM   3434  C CB  . ALA B  2 130 ? -6.017  -2.402  -13.214 1.00 14.33  ? 130 ALA B CB  1 
ATOM   3435  N N   . GLU B  2 131 ? -4.667  0.426   -13.125 1.00 14.93  ? 131 GLU B N   1 
ATOM   3436  C CA  . GLU B  2 131 ? -4.074  1.472   -12.300 1.00 15.40  ? 131 GLU B CA  1 
ATOM   3437  C C   . GLU B  2 131 ? -5.076  1.986   -11.270 1.00 15.79  ? 131 GLU B C   1 
ATOM   3438  O O   . GLU B  2 131 ? -6.285  1.903   -11.479 1.00 15.64  ? 131 GLU B O   1 
ATOM   3439  C CB  . GLU B  2 131 ? -3.568  2.622   -13.171 1.00 15.60  ? 131 GLU B CB  1 
ATOM   3440  C CG  . GLU B  2 131 ? -2.372  2.271   -14.050 1.00 15.14  ? 131 GLU B CG  1 
ATOM   3441  C CD  . GLU B  2 131 ? -1.966  3.405   -14.981 1.00 14.77  ? 131 GLU B CD  1 
ATOM   3442  O OE1 . GLU B  2 131 ? -2.360  4.565   -14.731 1.00 14.90  ? 131 GLU B OE1 1 
ATOM   3443  O OE2 . GLU B  2 131 ? -1.246  3.135   -15.965 1.00 10.23  ? 131 GLU B OE2 1 
ATOM   3444  N N   . GLU B  2 132 ? -4.562  2.515   -10.162 1.00 16.06  ? 132 GLU B N   1 
ATOM   3445  C CA  . GLU B  2 132 ? -5.392  3.072   -9.097  1.00 16.53  ? 132 GLU B CA  1 
ATOM   3446  C C   . GLU B  2 132 ? -5.694  4.534   -9.392  1.00 17.11  ? 132 GLU B C   1 
ATOM   3447  O O   . GLU B  2 132 ? -4.767  5.331   -9.558  1.00 17.89  ? 132 GLU B O   1 
ATOM   3448  C CB  . GLU B  2 132 ? -4.664  2.982   -7.755  1.00 16.19  ? 132 GLU B CB  1 
ATOM   3449  C CG  . GLU B  2 132 ? -4.001  1.649   -7.474  1.00 17.62  ? 132 GLU B CG  1 
ATOM   3450  C CD  . GLU B  2 132 ? -3.172  1.672   -6.207  1.00 19.60  ? 132 GLU B CD  1 
ATOM   3451  O OE1 . GLU B  2 132 ? -1.938  1.509   -6.300  1.00 21.14  ? 132 GLU B OE1 1 
ATOM   3452  O OE2 . GLU B  2 132 ? -3.752  1.862   -5.117  1.00 20.40  ? 132 GLU B OE2 1 
ATOM   3453  N N   . ASP B  2 133 ? -6.975  4.898   -9.447  1.00 17.32  ? 133 ASP B N   1 
ATOM   3454  C CA  . ASP B  2 133 ? -7.332  6.299   -9.719  1.00 18.19  ? 133 ASP B CA  1 
ATOM   3455  C C   . ASP B  2 133 ? -7.236  7.186   -8.479  1.00 17.83  ? 133 ASP B C   1 
ATOM   3456  O O   . ASP B  2 133 ? -7.305  8.411   -8.578  1.00 18.21  ? 133 ASP B O   1 
ATOM   3457  C CB  . ASP B  2 133 ? -8.702  6.434   -10.412 1.00 18.66  ? 133 ASP B CB  1 
ATOM   3458  C CG  . ASP B  2 133 ? -9.875  6.028   -9.526  1.00 20.12  ? 133 ASP B CG  1 
ATOM   3459  O OD1 . ASP B  2 133 ? -9.677  5.669   -8.342  1.00 18.86  ? 133 ASP B OD1 1 
ATOM   3460  O OD2 . ASP B  2 133 ? -11.015 6.074   -10.037 1.00 22.84  ? 133 ASP B OD2 1 
ATOM   3461  N N   . GLY B  2 134 ? -7.071  6.558   -7.319  1.00 17.24  ? 134 GLY B N   1 
ATOM   3462  C CA  . GLY B  2 134 ? -6.893  7.282   -6.068  1.00 16.21  ? 134 GLY B CA  1 
ATOM   3463  C C   . GLY B  2 134 ? -8.167  7.451   -5.270  1.00 15.63  ? 134 GLY B C   1 
ATOM   3464  O O   . GLY B  2 134 ? -8.124  7.942   -4.142  1.00 15.70  ? 134 GLY B O   1 
ATOM   3465  N N   . THR B  2 135 ? -9.297  7.048   -5.855  1.00 15.18  ? 135 THR B N   1 
ATOM   3466  C CA  . THR B  2 135 ? -10.605 7.126   -5.187  1.00 14.89  ? 135 THR B CA  1 
ATOM   3467  C C   . THR B  2 135 ? -11.108 5.761   -4.711  1.00 14.59  ? 135 THR B C   1 
ATOM   3468  O O   . THR B  2 135 ? -12.228 5.647   -4.208  1.00 14.02  ? 135 THR B O   1 
ATOM   3469  C CB  . THR B  2 135 ? -11.696 7.759   -6.095  1.00 14.93  ? 135 THR B CB  1 
ATOM   3470  O OG1 . THR B  2 135 ? -12.001 6.874   -7.183  1.00 14.45  ? 135 THR B OG1 1 
ATOM   3471  C CG2 . THR B  2 135 ? -11.250 9.111   -6.634  1.00 15.23  ? 135 THR B CG2 1 
ATOM   3472  N N   . GLY B  2 136 ? -10.282 4.732   -4.875  1.00 14.68  ? 136 GLY B N   1 
ATOM   3473  C CA  . GLY B  2 136 ? -10.679 3.368   -4.535  1.00 15.45  ? 136 GLY B CA  1 
ATOM   3474  C C   . GLY B  2 136 ? -11.044 2.515   -5.741  1.00 15.64  ? 136 GLY B C   1 
ATOM   3475  O O   . GLY B  2 136 ? -11.370 1.336   -5.595  1.00 15.75  ? 136 GLY B O   1 
ATOM   3476  N N   . CYS B  2 137 ? -10.997 3.106   -6.933  1.00 15.68  ? 137 CYS B N   1 
ATOM   3477  C CA  . CYS B  2 137 ? -11.238 2.357   -8.163  1.00 15.66  ? 137 CYS B CA  1 
ATOM   3478  C C   . CYS B  2 137 ? -9.938  1.931   -8.823  1.00 15.30  ? 137 CYS B C   1 
ATOM   3479  O O   . CYS B  2 137 ? -8.883  2.536   -8.605  1.00 16.28  ? 137 CYS B O   1 
ATOM   3480  C CB  . CYS B  2 137 ? -12.067 3.164   -9.171  1.00 15.58  ? 137 CYS B CB  1 
ATOM   3481  S SG  . CYS B  2 137 ? -13.625 3.804   -8.546  1.00 16.78  ? 137 CYS B SG  1 
ATOM   3482  N N   . PHE B  2 138 ? -10.033 0.879   -9.628  1.00 14.15  ? 138 PHE B N   1 
ATOM   3483  C CA  . PHE B  2 138 ? -8.964  0.478   -10.515 1.00 13.17  ? 138 PHE B CA  1 
ATOM   3484  C C   . PHE B  2 138 ? -9.431  0.670   -11.947 1.00 13.46  ? 138 PHE B C   1 
ATOM   3485  O O   . PHE B  2 138 ? -10.460 0.119   -12.341 1.00 13.80  ? 138 PHE B O   1 
ATOM   3486  C CB  . PHE B  2 138 ? -8.618  -0.989  -10.298 1.00 13.37  ? 138 PHE B CB  1 
ATOM   3487  C CG  . PHE B  2 138 ? -8.061  -1.290  -8.946  1.00 10.95  ? 138 PHE B CG  1 
ATOM   3488  C CD1 . PHE B  2 138 ? -8.903  -1.629  -7.893  1.00 11.36  ? 138 PHE B CD1 1 
ATOM   3489  C CD2 . PHE B  2 138 ? -6.690  -1.259  -8.728  1.00 9.81   ? 138 PHE B CD2 1 
ATOM   3490  C CE1 . PHE B  2 138 ? -8.384  -1.917  -6.635  1.00 13.12  ? 138 PHE B CE1 1 
ATOM   3491  C CE2 . PHE B  2 138 ? -6.161  -1.547  -7.480  1.00 9.15   ? 138 PHE B CE2 1 
ATOM   3492  C CZ  . PHE B  2 138 ? -7.010  -1.878  -6.428  1.00 11.65  ? 138 PHE B CZ  1 
ATOM   3493  N N   . GLU B  2 139 ? -8.686  1.465   -12.711 1.00 13.55  ? 139 GLU B N   1 
ATOM   3494  C CA  . GLU B  2 139 ? -8.921  1.616   -14.142 1.00 14.02  ? 139 GLU B CA  1 
ATOM   3495  C C   . GLU B  2 139 ? -8.341  0.401   -14.854 1.00 13.88  ? 139 GLU B C   1 
ATOM   3496  O O   . GLU B  2 139 ? -7.125  0.219   -14.895 1.00 14.43  ? 139 GLU B O   1 
ATOM   3497  C CB  . GLU B  2 139 ? -8.262  2.892   -14.679 1.00 14.40  ? 139 GLU B CB  1 
ATOM   3498  C CG  . GLU B  2 139 ? -8.854  4.205   -14.165 1.00 18.02  ? 139 GLU B CG  1 
ATOM   3499  C CD  . GLU B  2 139 ? -8.124  5.436   -14.704 1.00 22.26  ? 139 GLU B CD  1 
ATOM   3500  O OE1 . GLU B  2 139 ? -8.262  6.527   -14.103 1.00 23.34  ? 139 GLU B OE1 1 
ATOM   3501  O OE2 . GLU B  2 139 ? -7.413  5.316   -15.727 1.00 23.17  ? 139 GLU B OE2 1 
ATOM   3502  N N   . ILE B  2 140 ? -9.214  -0.432  -15.405 1.00 13.59  ? 140 ILE B N   1 
ATOM   3503  C CA  . ILE B  2 140 ? -8.795  -1.653  -16.086 1.00 13.04  ? 140 ILE B CA  1 
ATOM   3504  C C   . ILE B  2 140 ? -8.470  -1.334  -17.544 1.00 13.44  ? 140 ILE B C   1 
ATOM   3505  O O   . ILE B  2 140 ? -9.279  -0.717  -18.244 1.00 13.85  ? 140 ILE B O   1 
ATOM   3506  C CB  . ILE B  2 140 ? -9.878  -2.748  -15.973 1.00 12.69  ? 140 ILE B CB  1 
ATOM   3507  C CG1 . ILE B  2 140 ? -10.134 -3.080  -14.497 1.00 11.70  ? 140 ILE B CG1 1 
ATOM   3508  C CG2 . ILE B  2 140 ? -9.468  -4.000  -16.741 1.00 13.05  ? 140 ILE B CG2 1 
ATOM   3509  C CD1 . ILE B  2 140 ? -11.490 -3.713  -14.210 1.00 12.05  ? 140 ILE B CD1 1 
ATOM   3510  N N   . PHE B  2 141 ? -7.285  -1.748  -17.994 1.00 13.41  ? 141 PHE B N   1 
ATOM   3511  C CA  . PHE B  2 141 ? -6.795  -1.375  -19.328 1.00 13.77  ? 141 PHE B CA  1 
ATOM   3512  C C   . PHE B  2 141 ? -7.067  -2.401  -20.429 1.00 14.31  ? 141 PHE B C   1 
ATOM   3513  O O   . PHE B  2 141 ? -6.375  -2.437  -21.453 1.00 14.80  ? 141 PHE B O   1 
ATOM   3514  C CB  . PHE B  2 141 ? -5.314  -0.993  -19.273 1.00 12.79  ? 141 PHE B CB  1 
ATOM   3515  C CG  . PHE B  2 141 ? -5.079  0.383   -18.737 1.00 13.65  ? 141 PHE B CG  1 
ATOM   3516  C CD1 . PHE B  2 141 ? -5.006  0.608   -17.365 1.00 11.96  ? 141 PHE B CD1 1 
ATOM   3517  C CD2 . PHE B  2 141 ? -4.949  1.463   -19.602 1.00 12.33  ? 141 PHE B CD2 1 
ATOM   3518  C CE1 . PHE B  2 141 ? -4.794  1.884   -16.863 1.00 10.29  ? 141 PHE B CE1 1 
ATOM   3519  C CE2 . PHE B  2 141 ? -4.740  2.746   -19.109 1.00 11.21  ? 141 PHE B CE2 1 
ATOM   3520  C CZ  . PHE B  2 141 ? -4.663  2.957   -17.737 1.00 11.30  ? 141 PHE B CZ  1 
ATOM   3521  N N   . HIS B  2 142 ? -8.087  -3.222  -20.208 1.00 14.10  ? 142 HIS B N   1 
ATOM   3522  C CA  . HIS B  2 142 ? -8.531  -4.203  -21.185 1.00 14.53  ? 142 HIS B CA  1 
ATOM   3523  C C   . HIS B  2 142 ? -10.039 -4.368  -21.055 1.00 15.12  ? 142 HIS B C   1 
ATOM   3524  O O   . HIS B  2 142 ? -10.610 -4.049  -20.009 1.00 14.87  ? 142 HIS B O   1 
ATOM   3525  C CB  . HIS B  2 142 ? -7.816  -5.545  -20.976 1.00 13.91  ? 142 HIS B CB  1 
ATOM   3526  C CG  . HIS B  2 142 ? -8.138  -6.214  -19.674 1.00 13.26  ? 142 HIS B CG  1 
ATOM   3527  N ND1 . HIS B  2 142 ? -9.280  -6.962  -19.482 1.00 12.50  ? 142 HIS B ND1 1 
ATOM   3528  C CD2 . HIS B  2 142 ? -7.457  -6.265  -18.505 1.00 14.25  ? 142 HIS B CD2 1 
ATOM   3529  C CE1 . HIS B  2 142 ? -9.295  -7.436  -18.249 1.00 11.03  ? 142 HIS B CE1 1 
ATOM   3530  N NE2 . HIS B  2 142 ? -8.197  -7.033  -17.637 1.00 11.71  ? 142 HIS B NE2 1 
ATOM   3531  N N   . LYS B  2 143 ? -10.686 -4.854  -22.113 1.00 15.31  ? 143 LYS B N   1 
ATOM   3532  C CA  . LYS B  2 143 ? -12.113 -5.125  -22.044 1.00 15.29  ? 143 LYS B CA  1 
ATOM   3533  C C   . LYS B  2 143 ? -12.369 -6.176  -20.967 1.00 15.89  ? 143 LYS B C   1 
ATOM   3534  O O   . LYS B  2 143 ? -11.851 -7.297  -21.031 1.00 16.28  ? 143 LYS B O   1 
ATOM   3535  C CB  . LYS B  2 143 ? -12.682 -5.564  -23.399 1.00 15.08  ? 143 LYS B CB  1 
ATOM   3536  C CG  . LYS B  2 143 ? -14.202 -5.690  -23.399 1.00 12.98  ? 143 LYS B CG  1 
ATOM   3537  C CD  . LYS B  2 143 ? -14.758 -5.976  -24.774 1.00 12.32  ? 143 LYS B CD  1 
ATOM   3538  C CE  . LYS B  2 143 ? -16.275 -6.085  -24.726 1.00 12.14  ? 143 LYS B CE  1 
ATOM   3539  N NZ  . LYS B  2 143 ? -16.850 -6.392  -26.062 1.00 14.21  ? 143 LYS B NZ  1 
ATOM   3540  N N   . CYS B  2 144 ? -13.144 -5.784  -19.962 1.00 15.98  ? 144 CYS B N   1 
ATOM   3541  C CA  . CYS B  2 144 ? -13.496 -6.670  -18.867 1.00 16.23  ? 144 CYS B CA  1 
ATOM   3542  C C   . CYS B  2 144 ? -15.018 -6.759  -18.777 1.00 15.67  ? 144 CYS B C   1 
ATOM   3543  O O   . CYS B  2 144 ? -15.667 -5.892  -18.189 1.00 15.55  ? 144 CYS B O   1 
ATOM   3544  C CB  . CYS B  2 144 ? -12.873 -6.168  -17.557 1.00 16.07  ? 144 CYS B CB  1 
ATOM   3545  S SG  . CYS B  2 144 ? -12.966 -7.310  -16.151 1.00 18.61  ? 144 CYS B SG  1 
ATOM   3546  N N   . ASP B  2 145 ? -15.581 -7.799  -19.387 1.00 15.58  ? 145 ASP B N   1 
ATOM   3547  C CA  . ASP B  2 145 ? -17.033 -7.990  -19.399 1.00 15.70  ? 145 ASP B CA  1 
ATOM   3548  C C   . ASP B  2 145 ? -17.550 -8.497  -18.052 1.00 15.98  ? 145 ASP B C   1 
ATOM   3549  O O   . ASP B  2 145 ? -16.779 -8.643  -17.101 1.00 16.39  ? 145 ASP B O   1 
ATOM   3550  C CB  . ASP B  2 145 ? -17.475 -8.896  -20.566 1.00 15.55  ? 145 ASP B CB  1 
ATOM   3551  C CG  . ASP B  2 145 ? -16.792 -10.265 -20.565 1.00 14.60  ? 145 ASP B CG  1 
ATOM   3552  O OD1 . ASP B  2 145 ? -16.033 -10.572 -19.621 1.00 9.27   ? 145 ASP B OD1 1 
ATOM   3553  O OD2 . ASP B  2 145 ? -17.023 -11.038 -21.527 1.00 11.82  ? 145 ASP B OD2 1 
ATOM   3554  N N   . ASP B  2 146 ? -18.853 -8.758  -17.973 1.00 16.25  ? 146 ASP B N   1 
ATOM   3555  C CA  . ASP B  2 146 ? -19.482 -9.192  -16.723 1.00 16.99  ? 146 ASP B CA  1 
ATOM   3556  C C   . ASP B  2 146 ? -18.826 -10.421 -16.101 1.00 17.28  ? 146 ASP B C   1 
ATOM   3557  O O   . ASP B  2 146 ? -18.733 -10.520 -14.877 1.00 17.50  ? 146 ASP B O   1 
ATOM   3558  C CB  . ASP B  2 146 ? -20.985 -9.421  -16.917 1.00 16.99  ? 146 ASP B CB  1 
ATOM   3559  C CG  . ASP B  2 146 ? -21.777 -8.121  -16.961 1.00 17.18  ? 146 ASP B CG  1 
ATOM   3560  O OD1 . ASP B  2 146 ? -21.175 -7.036  -16.795 1.00 14.18  ? 146 ASP B OD1 1 
ATOM   3561  O OD2 . ASP B  2 146 ? -23.008 -8.185  -17.162 1.00 17.97  ? 146 ASP B OD2 1 
ATOM   3562  N N   . GLN B  2 147 ? -18.370 -11.344 -16.944 1.00 18.09  ? 147 GLN B N   1 
ATOM   3563  C CA  . GLN B  2 147 ? -17.693 -12.558 -16.482 1.00 19.35  ? 147 GLN B CA  1 
ATOM   3564  C C   . GLN B  2 147 ? -16.289 -12.255 -15.986 1.00 18.97  ? 147 GLN B C   1 
ATOM   3565  O O   . GLN B  2 147 ? -15.861 -12.782 -14.959 1.00 19.55  ? 147 GLN B O   1 
ATOM   3566  C CB  . GLN B  2 147 ? -17.656 -13.619 -17.584 1.00 19.78  ? 147 GLN B CB  1 
ATOM   3567  C CG  . GLN B  2 147 ? -18.984 -14.338 -17.784 1.00 25.28  ? 147 GLN B CG  1 
ATOM   3568  C CD  . GLN B  2 147 ? -19.178 -14.842 -19.207 1.00 32.39  ? 147 GLN B CD  1 
ATOM   3569  O OE1 . GLN B  2 147 ? -18.832 -14.160 -20.178 1.00 36.18  ? 147 GLN B OE1 1 
ATOM   3570  N NE2 . GLN B  2 147 ? -19.749 -16.036 -19.338 1.00 31.79  ? 147 GLN B NE2 1 
ATOM   3571  N N   . CYS B  2 148 ? -15.578 -11.402 -16.717 1.00 18.34  ? 148 CYS B N   1 
ATOM   3572  C CA  . CYS B  2 148 ? -14.267 -10.933 -16.294 1.00 18.98  ? 148 CYS B CA  1 
ATOM   3573  C C   . CYS B  2 148 ? -14.359 -10.239 -14.930 1.00 19.45  ? 148 CYS B C   1 
ATOM   3574  O O   . CYS B  2 148 ? -13.561 -10.523 -14.031 1.00 19.38  ? 148 CYS B O   1 
ATOM   3575  C CB  . CYS B  2 148 ? -13.678 -9.998  -17.350 1.00 18.70  ? 148 CYS B CB  1 
ATOM   3576  S SG  . CYS B  2 148 ? -12.213 -9.074  -16.850 1.00 21.75  ? 148 CYS B SG  1 
ATOM   3577  N N   . MET B  2 149 ? -15.341 -9.345  -14.785 1.00 19.49  ? 149 MET B N   1 
ATOM   3578  C CA  . MET B  2 149 ? -15.601 -8.657  -13.519 1.00 19.65  ? 149 MET B CA  1 
ATOM   3579  C C   . MET B  2 149 ? -15.842 -9.661  -12.401 1.00 20.10  ? 149 MET B C   1 
ATOM   3580  O O   . MET B  2 149 ? -15.322 -9.507  -11.295 1.00 20.22  ? 149 MET B O   1 
ATOM   3581  C CB  . MET B  2 149 ? -16.812 -7.728  -13.639 1.00 19.81  ? 149 MET B CB  1 
ATOM   3582  C CG  . MET B  2 149 ? -16.604 -6.511  -14.521 1.00 19.68  ? 149 MET B CG  1 
ATOM   3583  S SD  . MET B  2 149 ? -15.270 -5.447  -13.945 1.00 20.76  ? 149 MET B SD  1 
ATOM   3584  C CE  . MET B  2 149 ? -15.464 -4.059  -15.060 1.00 19.40  ? 149 MET B CE  1 
ATOM   3585  N N   . GLU B  2 150 ? -16.631 -10.688 -12.713 1.00 20.67  ? 150 GLU B N   1 
ATOM   3586  C CA  . GLU B  2 150 ? -16.924 -11.782 -11.792 1.00 21.51  ? 150 GLU B CA  1 
ATOM   3587  C C   . GLU B  2 150 ? -15.644 -12.474 -11.309 1.00 21.52  ? 150 GLU B C   1 
ATOM   3588  O O   . GLU B  2 150 ? -15.490 -12.722 -10.108 1.00 22.24  ? 150 GLU B O   1 
ATOM   3589  C CB  . GLU B  2 150 ? -17.893 -12.782 -12.449 1.00 21.43  ? 150 GLU B CB  1 
ATOM   3590  C CG  . GLU B  2 150 ? -18.183 -14.061 -11.654 1.00 25.07  ? 150 GLU B CG  1 
ATOM   3591  C CD  . GLU B  2 150 ? -18.876 -13.811 -10.317 1.00 31.67  ? 150 GLU B CD  1 
ATOM   3592  O OE1 . GLU B  2 150 ? -19.542 -12.761 -10.158 1.00 32.16  ? 150 GLU B OE1 1 
ATOM   3593  O OE2 . GLU B  2 150 ? -18.755 -14.677 -9.420  1.00 33.98  ? 150 GLU B OE2 1 
ATOM   3594  N N   . SER B  2 151 ? -14.728 -12.754 -12.238 1.00 20.78  ? 151 SER B N   1 
ATOM   3595  C CA  . SER B  2 151 ? -13.474 -13.442 -11.918 1.00 20.29  ? 151 SER B CA  1 
ATOM   3596  C C   . SER B  2 151 ? -12.587 -12.641 -10.963 1.00 20.34  ? 151 SER B C   1 
ATOM   3597  O O   . SER B  2 151 ? -11.842 -13.224 -10.173 1.00 20.37  ? 151 SER B O   1 
ATOM   3598  C CB  . SER B  2 151 ? -12.706 -13.822 -13.191 1.00 19.99  ? 151 SER B CB  1 
ATOM   3599  O OG  . SER B  2 151 ? -12.194 -12.682 -13.860 1.00 19.54  ? 151 SER B OG  1 
ATOM   3600  N N   . ILE B  2 152 ? -12.673 -11.314 -11.039 1.00 20.24  ? 152 ILE B N   1 
ATOM   3601  C CA  . ILE B  2 152 ? -11.954 -10.440 -10.111 1.00 20.62  ? 152 ILE B CA  1 
ATOM   3602  C C   . ILE B  2 152 ? -12.555 -10.564 -8.712  1.00 21.62  ? 152 ILE B C   1 
ATOM   3603  O O   . ILE B  2 152 ? -11.824 -10.660 -7.721  1.00 22.54  ? 152 ILE B O   1 
ATOM   3604  C CB  . ILE B  2 152 ? -11.975 -8.952  -10.553 1.00 20.21  ? 152 ILE B CB  1 
ATOM   3605  C CG1 . ILE B  2 152 ? -11.419 -8.793  -11.968 1.00 18.54  ? 152 ILE B CG1 1 
ATOM   3606  C CG2 . ILE B  2 152 ? -11.179 -8.091  -9.575  1.00 19.17  ? 152 ILE B CG2 1 
ATOM   3607  C CD1 . ILE B  2 152 ? -11.517 -7.385  -12.526 1.00 15.49  ? 152 ILE B CD1 1 
ATOM   3608  N N   . ARG B  2 153 ? -13.886 -10.572 -8.647  1.00 21.87  ? 153 ARG B N   1 
ATOM   3609  C CA  . ARG B  2 153 ? -14.608 -10.679 -7.381  1.00 22.36  ? 153 ARG B CA  1 
ATOM   3610  C C   . ARG B  2 153 ? -14.366 -12.009 -6.663  1.00 22.92  ? 153 ARG B C   1 
ATOM   3611  O O   . ARG B  2 153 ? -14.054 -12.024 -5.472  1.00 22.80  ? 153 ARG B O   1 
ATOM   3612  C CB  . ARG B  2 153 ? -16.109 -10.452 -7.585  1.00 22.38  ? 153 ARG B CB  1 
ATOM   3613  C CG  . ARG B  2 153 ? -16.496 -9.015  -7.915  1.00 22.11  ? 153 ARG B CG  1 
ATOM   3614  C CD  . ARG B  2 153 ? -17.983 -8.770  -7.691  1.00 20.43  ? 153 ARG B CD  1 
ATOM   3615  N NE  . ARG B  2 153 ? -18.818 -9.608  -8.549  1.00 20.83  ? 153 ARG B NE  1 
ATOM   3616  C CZ  . ARG B  2 153 ? -19.219 -9.273  -9.772  1.00 21.56  ? 153 ARG B CZ  1 
ATOM   3617  N NH1 . ARG B  2 153 ? -18.872 -8.106  -10.298 1.00 24.04  ? 153 ARG B NH1 1 
ATOM   3618  N NH2 . ARG B  2 153 ? -19.970 -10.109 -10.474 1.00 20.46  ? 153 ARG B NH2 1 
ATOM   3619  N N   . ASN B  2 154 ? -14.500 -13.122 -7.382  1.00 23.51  ? 154 ASN B N   1 
ATOM   3620  C CA  . ASN B  2 154 ? -14.352 -14.436 -6.754  1.00 24.31  ? 154 ASN B CA  1 
ATOM   3621  C C   . ASN B  2 154 ? -12.912 -14.977 -6.782  1.00 24.00  ? 154 ASN B C   1 
ATOM   3622  O O   . ASN B  2 154 ? -12.672 -16.154 -6.500  1.00 24.02  ? 154 ASN B O   1 
ATOM   3623  C CB  . ASN B  2 154 ? -15.394 -15.438 -7.293  1.00 24.62  ? 154 ASN B CB  1 
ATOM   3624  C CG  . ASN B  2 154 ? -14.875 -16.286 -8.442  1.00 27.99  ? 154 ASN B CG  1 
ATOM   3625  O OD1 . ASN B  2 154 ? -14.398 -15.774 -9.458  1.00 31.75  ? 154 ASN B OD1 1 
ATOM   3626  N ND2 . ASN B  2 154 ? -14.981 -17.602 -8.287  1.00 33.93  ? 154 ASN B ND2 1 
ATOM   3627  N N   . ASN B  2 155 ? -11.969 -14.092 -7.109  1.00 23.55  ? 155 ASN B N   1 
ATOM   3628  C CA  . ASN B  2 155 ? -10.527 -14.366 -7.028  1.00 23.44  ? 155 ASN B CA  1 
ATOM   3629  C C   . ASN B  2 155 ? -10.011 -15.432 -8.003  1.00 23.14  ? 155 ASN B C   1 
ATOM   3630  O O   . ASN B  2 155 ? -9.057  -16.148 -7.698  1.00 23.88  ? 155 ASN B O   1 
ATOM   3631  C CB  . ASN B  2 155 ? -10.114 -14.708 -5.583  1.00 23.71  ? 155 ASN B CB  1 
ATOM   3632  C CG  . ASN B  2 155 ? -8.697  -14.256 -5.247  1.00 24.79  ? 155 ASN B CG  1 
ATOM   3633  O OD1 . ASN B  2 155 ? -7.899  -13.944 -6.131  1.00 27.55  ? 155 ASN B OD1 1 
ATOM   3634  N ND2 . ASN B  2 155 ? -8.385  -14.216 -3.959  1.00 24.58  ? 155 ASN B ND2 1 
ATOM   3635  N N   . THR B  2 156 ? -10.634 -15.530 -9.175  1.00 22.16  ? 156 THR B N   1 
ATOM   3636  C CA  . THR B  2 156 ? -10.183 -16.478 -10.196 1.00 21.36  ? 156 THR B CA  1 
ATOM   3637  C C   . THR B  2 156 ? -9.586  -15.778 -11.424 1.00 20.81  ? 156 THR B C   1 
ATOM   3638  O O   . THR B  2 156 ? -9.155  -16.440 -12.375 1.00 21.20  ? 156 THR B O   1 
ATOM   3639  C CB  . THR B  2 156 ? -11.304 -17.456 -10.620 1.00 21.44  ? 156 THR B CB  1 
ATOM   3640  O OG1 . THR B  2 156 ? -12.425 -16.720 -11.129 1.00 22.26  ? 156 THR B OG1 1 
ATOM   3641  C CG2 . THR B  2 156 ? -11.750 -18.300 -9.435  1.00 22.39  ? 156 THR B CG2 1 
ATOM   3642  N N   . TYR B  2 157 ? -9.556  -14.444 -11.381 1.00 19.09  ? 157 TYR B N   1 
ATOM   3643  C CA  . TYR B  2 157 ? -8.972  -13.608 -12.437 1.00 17.48  ? 157 TYR B CA  1 
ATOM   3644  C C   . TYR B  2 157 ? -7.515  -13.966 -12.721 1.00 17.24  ? 157 TYR B C   1 
ATOM   3645  O O   . TYR B  2 157 ? -6.666  -13.928 -11.824 1.00 17.03  ? 157 TYR B O   1 
ATOM   3646  C CB  . TYR B  2 157 ? -9.082  -12.132 -12.039 1.00 17.24  ? 157 TYR B CB  1 
ATOM   3647  C CG  . TYR B  2 157 ? -8.480  -11.133 -13.007 1.00 13.66  ? 157 TYR B CG  1 
ATOM   3648  C CD1 . TYR B  2 157 ? -9.241  -10.591 -14.042 1.00 13.47  ? 157 TYR B CD1 1 
ATOM   3649  C CD2 . TYR B  2 157 ? -7.161  -10.703 -12.867 1.00 11.79  ? 157 TYR B CD2 1 
ATOM   3650  C CE1 . TYR B  2 157 ? -8.698  -9.653  -14.924 1.00 12.92  ? 157 TYR B CE1 1 
ATOM   3651  C CE2 . TYR B  2 157 ? -6.604  -9.770  -13.746 1.00 11.31  ? 157 TYR B CE2 1 
ATOM   3652  C CZ  . TYR B  2 157 ? -7.378  -9.251  -14.771 1.00 11.86  ? 157 TYR B CZ  1 
ATOM   3653  O OH  . TYR B  2 157 ? -6.839  -8.332  -15.641 1.00 9.72   ? 157 TYR B OH  1 
ATOM   3654  N N   . ASP B  2 158 ? -7.241  -14.314 -13.974 1.00 16.53  ? 158 ASP B N   1 
ATOM   3655  C CA  . ASP B  2 158 ? -5.899  -14.659 -14.414 1.00 16.26  ? 158 ASP B CA  1 
ATOM   3656  C C   . ASP B  2 158 ? -5.343  -13.507 -15.244 1.00 16.33  ? 158 ASP B C   1 
ATOM   3657  O O   . ASP B  2 158 ? -5.754  -13.305 -16.387 1.00 16.82  ? 158 ASP B O   1 
ATOM   3658  C CB  . ASP B  2 158 ? -5.933  -15.962 -15.227 1.00 16.27  ? 158 ASP B CB  1 
ATOM   3659  C CG  . ASP B  2 158 ? -4.586  -16.312 -15.856 1.00 17.25  ? 158 ASP B CG  1 
ATOM   3660  O OD1 . ASP B  2 158 ? -3.529  -15.940 -15.300 1.00 15.28  ? 158 ASP B OD1 1 
ATOM   3661  O OD2 . ASP B  2 158 ? -4.587  -16.976 -16.913 1.00 17.63  ? 158 ASP B OD2 1 
ATOM   3662  N N   . HIS B  2 159 ? -4.404  -12.759 -14.667 1.00 16.05  ? 159 HIS B N   1 
ATOM   3663  C CA  . HIS B  2 159 ? -3.873  -11.547 -15.305 1.00 15.90  ? 159 HIS B CA  1 
ATOM   3664  C C   . HIS B  2 159 ? -3.120  -11.827 -16.606 1.00 15.75  ? 159 HIS B C   1 
ATOM   3665  O O   . HIS B  2 159 ? -2.987  -10.945 -17.452 1.00 16.31  ? 159 HIS B O   1 
ATOM   3666  C CB  . HIS B  2 159 ? -2.971  -10.780 -14.336 1.00 15.74  ? 159 HIS B CB  1 
ATOM   3667  C CG  . HIS B  2 159 ? -1.610  -11.381 -14.179 1.00 14.71  ? 159 HIS B CG  1 
ATOM   3668  N ND1 . HIS B  2 159 ? -0.513  -10.931 -14.882 1.00 13.38  ? 159 HIS B ND1 1 
ATOM   3669  C CD2 . HIS B  2 159 ? -1.172  -12.409 -13.414 1.00 11.49  ? 159 HIS B CD2 1 
ATOM   3670  C CE1 . HIS B  2 159 ? 0.545   -11.649 -14.549 1.00 12.73  ? 159 HIS B CE1 1 
ATOM   3671  N NE2 . HIS B  2 159 ? 0.172   -12.551 -13.659 1.00 14.93  ? 159 HIS B NE2 1 
ATOM   3672  N N   . THR B  2 160 ? -2.624  -13.054 -16.741 1.00 15.45  ? 160 THR B N   1 
ATOM   3673  C CA  . THR B  2 160 ? -1.913  -13.512 -17.936 1.00 15.78  ? 160 THR B CA  1 
ATOM   3674  C C   . THR B  2 160 ? -2.810  -13.432 -19.175 1.00 15.48  ? 160 THR B C   1 
ATOM   3675  O O   . THR B  2 160 ? -2.348  -13.130 -20.276 1.00 14.88  ? 160 THR B O   1 
ATOM   3676  C CB  . THR B  2 160 ? -1.414  -14.964 -17.730 1.00 15.45  ? 160 THR B CB  1 
ATOM   3677  O OG1 . THR B  2 160 ? -0.569  -15.008 -16.576 1.00 15.97  ? 160 THR B OG1 1 
ATOM   3678  C CG2 . THR B  2 160 ? -0.633  -15.475 -18.934 1.00 18.15  ? 160 THR B CG2 1 
ATOM   3679  N N   . GLN B  2 161 ? -4.098  -13.684 -18.968 1.00 15.67  ? 161 GLN B N   1 
ATOM   3680  C CA  . GLN B  2 161 ? -5.092  -13.679 -20.031 1.00 15.32  ? 161 GLN B CA  1 
ATOM   3681  C C   . GLN B  2 161 ? -5.186  -12.320 -20.718 1.00 15.02  ? 161 GLN B C   1 
ATOM   3682  O O   . GLN B  2 161 ? -5.469  -12.248 -21.913 1.00 16.12  ? 161 GLN B O   1 
ATOM   3683  C CB  . GLN B  2 161 ? -6.453  -14.074 -19.453 1.00 15.54  ? 161 GLN B CB  1 
ATOM   3684  C CG  . GLN B  2 161 ? -7.541  -14.356 -20.471 1.00 15.67  ? 161 GLN B CG  1 
ATOM   3685  C CD  . GLN B  2 161 ? -8.805  -14.895 -19.826 1.00 17.70  ? 161 GLN B CD  1 
ATOM   3686  O OE1 . GLN B  2 161 ? -8.750  -15.750 -18.940 1.00 20.90  ? 161 GLN B OE1 1 
ATOM   3687  N NE2 . GLN B  2 161 ? -9.954  -14.403 -20.275 1.00 16.43  ? 161 GLN B NE2 1 
ATOM   3688  N N   . TYR B  2 162 ? -4.919  -11.252 -19.967 1.00 13.59  ? 162 TYR B N   1 
ATOM   3689  C CA  . TYR B  2 162 ? -5.185  -9.895  -20.440 1.00 12.10  ? 162 TYR B CA  1 
ATOM   3690  C C   . TYR B  2 162 ? -3.964  -8.982  -20.529 1.00 11.25  ? 162 TYR B C   1 
ATOM   3691  O O   . TYR B  2 162 ? -4.093  -7.814  -20.900 1.00 11.03  ? 162 TYR B O   1 
ATOM   3692  C CB  . TYR B  2 162 ? -6.222  -9.228  -19.541 1.00 11.89  ? 162 TYR B CB  1 
ATOM   3693  C CG  . TYR B  2 162 ? -7.480  -10.028 -19.297 1.00 11.31  ? 162 TYR B CG  1 
ATOM   3694  C CD1 . TYR B  2 162 ? -8.521  -10.029 -20.224 1.00 8.45   ? 162 TYR B CD1 1 
ATOM   3695  C CD2 . TYR B  2 162 ? -7.639  -10.764 -18.126 1.00 10.00  ? 162 TYR B CD2 1 
ATOM   3696  C CE1 . TYR B  2 162 ? -9.688  -10.749 -19.991 1.00 10.82  ? 162 TYR B CE1 1 
ATOM   3697  C CE2 . TYR B  2 162 ? -8.794  -11.493 -17.885 1.00 11.19  ? 162 TYR B CE2 1 
ATOM   3698  C CZ  . TYR B  2 162 ? -9.816  -11.479 -18.818 1.00 12.76  ? 162 TYR B CZ  1 
ATOM   3699  O OH  . TYR B  2 162 ? -10.965 -12.197 -18.574 1.00 13.11  ? 162 TYR B OH  1 
ATOM   3700  N N   . ARG B  2 163 ? -2.788  -9.503  -20.197 1.00 10.67  ? 163 ARG B N   1 
ATOM   3701  C CA  . ARG B  2 163 ? -1.588  -8.677  -20.091 1.00 10.50  ? 163 ARG B CA  1 
ATOM   3702  C C   . ARG B  2 163 ? -1.246  -7.917  -21.381 1.00 10.81  ? 163 ARG B C   1 
ATOM   3703  O O   . ARG B  2 163 ? -1.053  -6.702  -21.346 1.00 11.39  ? 163 ARG B O   1 
ATOM   3704  C CB  . ARG B  2 163 ? -0.405  -9.519  -19.614 1.00 10.70  ? 163 ARG B CB  1 
ATOM   3705  C CG  . ARG B  2 163 ? 0.774   -8.714  -19.087 1.00 11.62  ? 163 ARG B CG  1 
ATOM   3706  C CD  . ARG B  2 163 ? 1.824   -9.645  -18.506 1.00 10.24  ? 163 ARG B CD  1 
ATOM   3707  N NE  . ARG B  2 163 ? 3.104   -8.974  -18.288 1.00 12.11  ? 163 ARG B NE  1 
ATOM   3708  C CZ  . ARG B  2 163 ? 3.496   -8.443  -17.134 1.00 10.41  ? 163 ARG B CZ  1 
ATOM   3709  N NH1 . ARG B  2 163 ? 2.711   -8.489  -16.067 1.00 13.32  ? 163 ARG B NH1 1 
ATOM   3710  N NH2 . ARG B  2 163 ? 4.683   -7.863  -17.046 1.00 10.88  ? 163 ARG B NH2 1 
ATOM   3711  N N   . THR B  2 164 ? -1.193  -8.625  -22.508 1.00 10.63  ? 164 THR B N   1 
ATOM   3712  C CA  . THR B  2 164 ? -0.817  -8.024  -23.792 1.00 10.92  ? 164 THR B CA  1 
ATOM   3713  C C   . THR B  2 164 ? -1.726  -6.855  -24.213 1.00 12.48  ? 164 THR B C   1 
ATOM   3714  O O   . THR B  2 164 ? -1.234  -5.809  -24.647 1.00 13.09  ? 164 THR B O   1 
ATOM   3715  C CB  . THR B  2 164 ? -0.741  -9.087  -24.905 1.00 10.82  ? 164 THR B CB  1 
ATOM   3716  O OG1 . THR B  2 164 ? 0.097   -10.159 -24.467 1.00 11.64  ? 164 THR B OG1 1 
ATOM   3717  C CG2 . THR B  2 164 ? -0.175  -8.504  -26.201 1.00 7.16   ? 164 THR B CG2 1 
ATOM   3718  N N   . GLU B  2 165 ? -3.041  -7.029  -24.078 1.00 13.01  ? 165 GLU B N   1 
ATOM   3719  C CA  . GLU B  2 165 ? -3.980  -5.944  -24.362 1.00 12.87  ? 165 GLU B CA  1 
ATOM   3720  C C   . GLU B  2 165 ? -3.757  -4.787  -23.396 1.00 13.05  ? 165 GLU B C   1 
ATOM   3721  O O   . GLU B  2 165 ? -3.819  -3.617  -23.788 1.00 13.45  ? 165 GLU B O   1 
ATOM   3722  C CB  . GLU B  2 165 ? -5.430  -6.429  -24.278 1.00 12.74  ? 165 GLU B CB  1 
ATOM   3723  C CG  . GLU B  2 165 ? -6.463  -5.361  -24.661 1.00 14.13  ? 165 GLU B CG  1 
ATOM   3724  C CD  . GLU B  2 165 ? -7.902  -5.825  -24.509 1.00 15.94  ? 165 GLU B CD  1 
ATOM   3725  O OE1 . GLU B  2 165 ? -8.800  -4.958  -24.469 1.00 17.92  ? 165 GLU B OE1 1 
ATOM   3726  O OE2 . GLU B  2 165 ? -8.142  -7.048  -24.430 1.00 16.07  ? 165 GLU B OE2 1 
ATOM   3727  N N   . SER B  2 166 ? -3.487  -5.124  -22.139 1.00 13.28  ? 166 SER B N   1 
ATOM   3728  C CA  . SER B  2 166 ? -3.327  -4.125  -21.087 1.00 14.12  ? 166 SER B CA  1 
ATOM   3729  C C   . SER B  2 166 ? -2.108  -3.237  -21.316 1.00 14.54  ? 166 SER B C   1 
ATOM   3730  O O   . SER B  2 166 ? -2.224  -2.011  -21.301 1.00 14.39  ? 166 SER B O   1 
ATOM   3731  C CB  . SER B  2 166 ? -3.265  -4.793  -19.712 1.00 13.77  ? 166 SER B CB  1 
ATOM   3732  O OG  . SER B  2 166 ? -4.509  -5.393  -19.397 1.00 11.97  ? 166 SER B OG  1 
ATOM   3733  N N   . LEU B  2 167 ? -0.954  -3.861  -21.550 1.00 15.21  ? 167 LEU B N   1 
ATOM   3734  C CA  . LEU B  2 167 ? 0.300   -3.133  -21.760 1.00 15.27  ? 167 LEU B CA  1 
ATOM   3735  C C   . LEU B  2 167 ? 0.259   -2.260  -23.010 1.00 15.46  ? 167 LEU B C   1 
ATOM   3736  O O   . LEU B  2 167 ? 0.906   -1.213  -23.054 1.00 15.69  ? 167 LEU B O   1 
ATOM   3737  C CB  . LEU B  2 167 ? 1.494   -4.090  -21.820 1.00 15.19  ? 167 LEU B CB  1 
ATOM   3738  C CG  . LEU B  2 167 ? 1.764   -5.011  -20.623 1.00 15.67  ? 167 LEU B CG  1 
ATOM   3739  C CD1 . LEU B  2 167 ? 2.807   -6.059  -20.993 1.00 18.19  ? 167 LEU B CD1 1 
ATOM   3740  C CD2 . LEU B  2 167 ? 2.191   -4.237  -19.387 1.00 13.03  ? 167 LEU B CD2 1 
ATOM   3741  N N   . GLN B  2 168 ? -0.501  -2.693  -24.017 1.00 15.51  ? 168 GLN B N   1 
ATOM   3742  C CA  . GLN B  2 168 ? -0.716  -1.894  -25.224 1.00 15.39  ? 168 GLN B CA  1 
ATOM   3743  C C   . GLN B  2 168 ? -1.491  -0.615  -24.916 1.00 15.54  ? 168 GLN B C   1 
ATOM   3744  O O   . GLN B  2 168 ? -1.220  0.434   -25.501 1.00 15.74  ? 168 GLN B O   1 
ATOM   3745  C CB  . GLN B  2 168 ? -1.440  -2.705  -26.300 1.00 14.90  ? 168 GLN B CB  1 
ATOM   3746  C CG  . GLN B  2 168 ? -0.528  -3.613  -27.116 1.00 15.82  ? 168 GLN B CG  1 
ATOM   3747  C CD  . GLN B  2 168 ? -1.289  -4.674  -27.902 1.00 17.61  ? 168 GLN B CD  1 
ATOM   3748  O OE1 . GLN B  2 168 ? -2.525  -4.687  -27.937 1.00 18.48  ? 168 GLN B OE1 1 
ATOM   3749  N NE2 . GLN B  2 168 ? -0.549  -5.574  -28.534 1.00 16.82  ? 168 GLN B NE2 1 
ATOM   3750  N N   . ASN B  2 169 ? -2.450  -0.704  -23.997 1.00 15.62  ? 169 ASN B N   1 
ATOM   3751  C CA  . ASN B  2 169 ? -3.247  0.461   -23.614 1.00 15.81  ? 169 ASN B CA  1 
ATOM   3752  C C   . ASN B  2 169 ? -2.571  1.314   -22.544 1.00 15.79  ? 169 ASN B C   1 
ATOM   3753  O O   . ASN B  2 169 ? -2.772  2.530   -22.498 1.00 15.85  ? 169 ASN B O   1 
ATOM   3754  C CB  . ASN B  2 169 ? -4.653  0.046   -23.173 1.00 16.00  ? 169 ASN B CB  1 
ATOM   3755  C CG  . ASN B  2 169 ? -5.476  -0.534  -24.311 1.00 17.34  ? 169 ASN B CG  1 
ATOM   3756  O OD1 . ASN B  2 169 ? -5.526  0.025   -25.408 1.00 16.29  ? 169 ASN B OD1 1 
ATOM   3757  N ND2 . ASN B  2 169 ? -6.132  -1.661  -24.051 1.00 18.47  ? 169 ASN B ND2 1 
ATOM   3758  N N   . ARG B  2 170 ? -1.766  0.677   -21.697 1.00 15.90  ? 170 ARG B N   1 
ATOM   3759  C CA  . ARG B  2 170 ? -1.022  1.386   -20.653 1.00 16.63  ? 170 ARG B CA  1 
ATOM   3760  C C   . ARG B  2 170 ? 0.201   2.139   -21.194 1.00 17.32  ? 170 ARG B C   1 
ATOM   3761  O O   . ARG B  2 170 ? 0.308   3.359   -21.034 1.00 17.26  ? 170 ARG B O   1 
ATOM   3762  C CB  . ARG B  2 170 ? -0.603  0.432   -19.533 1.00 16.40  ? 170 ARG B CB  1 
ATOM   3763  C CG  . ARG B  2 170 ? -1.738  0.001   -18.630 1.00 14.37  ? 170 ARG B CG  1 
ATOM   3764  C CD  . ARG B  2 170 ? -1.367  0.207   -17.177 1.00 14.25  ? 170 ARG B CD  1 
ATOM   3765  N NE  . ARG B  2 170 ? -0.420  -0.787  -16.680 1.00 13.79  ? 170 ARG B NE  1 
ATOM   3766  C CZ  . ARG B  2 170 ? 0.455   -0.572  -15.700 1.00 15.20  ? 170 ARG B CZ  1 
ATOM   3767  N NH1 . ARG B  2 170 ? 0.534   0.616   -15.108 1.00 11.89  ? 170 ARG B NH1 1 
ATOM   3768  N NH2 . ARG B  2 170 ? 1.265   -1.547  -15.317 1.00 17.30  ? 170 ARG B NH2 1 
ATOM   3769  N N   . ILE B  2 171 ? 1.118   1.405   -21.821 1.00 17.90  ? 171 ILE B N   1 
ATOM   3770  C CA  . ILE B  2 171 ? 2.308   1.998   -22.417 1.00 18.98  ? 171 ILE B CA  1 
ATOM   3771  C C   . ILE B  2 171 ? 1.941   2.512   -23.810 1.00 20.14  ? 171 ILE B C   1 
ATOM   3772  O O   . ILE B  2 171 ? 2.091   1.804   -24.813 1.00 19.77  ? 171 ILE B O   1 
ATOM   3773  C CB  . ILE B  2 171 ? 3.513   0.999   -22.475 1.00 18.70  ? 171 ILE B CB  1 
ATOM   3774  C CG1 . ILE B  2 171 ? 3.913   0.519   -21.080 1.00 20.58  ? 171 ILE B CG1 1 
ATOM   3775  C CG2 . ILE B  2 171 ? 4.735   1.650   -23.088 1.00 18.59  ? 171 ILE B CG2 1 
ATOM   3776  C CD1 . ILE B  2 171 ? 3.258   -0.773  -20.643 1.00 26.68  ? 171 ILE B CD1 1 
ATOM   3777  N N   . GLN B  2 172 ? 1.438   3.742   -23.866 1.00 21.51  ? 172 GLN B N   1 
ATOM   3778  C CA  . GLN B  2 172 ? 1.081   4.340   -25.149 1.00 22.95  ? 172 GLN B CA  1 
ATOM   3779  C C   . GLN B  2 172 ? 2.182   5.241   -25.704 1.00 23.10  ? 172 GLN B C   1 
ATOM   3780  O O   . GLN B  2 172 ? 1.962   6.417   -26.002 1.00 22.90  ? 172 GLN B O   1 
ATOM   3781  C CB  . GLN B  2 172 ? -0.299  5.008   -25.102 1.00 23.77  ? 172 GLN B CB  1 
ATOM   3782  C CG  . GLN B  2 172 ? -1.439  4.016   -25.386 1.00 24.66  ? 172 GLN B CG  1 
ATOM   3783  C CD  . GLN B  2 172 ? -2.806  4.673   -25.459 1.00 26.42  ? 172 GLN B CD  1 
ATOM   3784  O OE1 . GLN B  2 172 ? -3.311  5.195   -24.464 1.00 28.05  ? 172 GLN B OE1 1 
ATOM   3785  N NE2 . GLN B  2 172 ? -3.419  4.637   -26.638 1.00 25.63  ? 172 GLN B NE2 1 
ATOM   3786  N N   . ILE B  2 173 ? 3.375   4.655   -25.815 1.00 23.71  ? 173 ILE B N   1 
ATOM   3787  C CA  . ILE B  2 173 ? 4.533   5.244   -26.496 1.00 23.79  ? 173 ILE B CA  1 
ATOM   3788  C C   . ILE B  2 173 ? 5.265   4.140   -27.281 1.00 24.81  ? 173 ILE B C   1 
ATOM   3789  O O   . ILE B  2 173 ? 4.943   2.957   -27.140 1.00 24.61  ? 173 ILE B O   1 
ATOM   3790  C CB  . ILE B  2 173 ? 5.526   5.927   -25.511 1.00 23.46  ? 173 ILE B CB  1 
ATOM   3791  C CG1 . ILE B  2 173 ? 6.030   4.927   -24.463 1.00 22.99  ? 173 ILE B CG1 1 
ATOM   3792  C CG2 . ILE B  2 173 ? 4.903   7.167   -24.857 1.00 21.13  ? 173 ILE B CG2 1 
ATOM   3793  C CD1 . ILE B  2 173 ? 7.408   5.240   -23.917 1.00 23.89  ? 173 ILE B CD1 1 
ATOM   3794  N N   . ASP B  2 174 ? 6.242   4.527   -28.100 1.00 25.75  ? 174 ASP B N   1 
ATOM   3795  C CA  . ASP B  2 174 ? 7.057   3.569   -28.850 1.00 26.50  ? 174 ASP B CA  1 
ATOM   3796  C C   . ASP B  2 174 ? 8.160   2.972   -27.975 1.00 27.53  ? 174 ASP B C   1 
ATOM   3797  O O   . ASP B  2 174 ? 8.889   3.701   -27.305 1.00 27.38  ? 174 ASP B O   1 
ATOM   3798  C CB  . ASP B  2 174 ? 7.673   4.246   -30.078 1.00 26.19  ? 174 ASP B CB  1 
ATOM   3799  C CG  . ASP B  2 174 ? 8.375   3.263   -31.007 1.00 26.34  ? 174 ASP B CG  1 
ATOM   3800  O OD1 . ASP B  2 174 ? 8.075   2.049   -30.960 1.00 24.02  ? 174 ASP B OD1 1 
ATOM   3801  O OD2 . ASP B  2 174 ? 9.229   3.715   -31.799 1.00 26.25  ? 174 ASP B OD2 1 
ATOM   3802  N N   . SER B  2 175 ? 8.283   1.645   -27.994 1.00 29.13  ? 175 SER B N   1 
ATOM   3803  C CA  . SER B  2 175 ? 9.314   0.946   -27.216 1.00 30.48  ? 175 SER B CA  1 
ATOM   3804  C C   . SER B  2 175 ? 10.522  0.522   -28.071 1.00 32.17  ? 175 SER B C   1 
ATOM   3805  O O   . SER B  2 175 ? 10.403  -0.323  -28.970 1.00 32.69  ? 175 SER B O   1 
ATOM   3806  C CB  . SER B  2 175 ? 8.712   -0.257  -26.485 1.00 30.15  ? 175 SER B CB  1 
ATOM   3807  O OG  . SER B  2 175 ? 7.722   0.160   -25.558 1.00 27.98  ? 175 SER B OG  1 
ATOM   3808  N N   . GLY B  2 176 ? 11.678  1.121   -27.785 1.00 32.91  ? 176 GLY B N   1 
ATOM   3809  C CA  . GLY B  2 176 ? 12.910  0.844   -28.526 1.00 32.89  ? 176 GLY B CA  1 
ATOM   3810  C C   . GLY B  2 176 ? 14.022  0.320   -27.637 1.00 32.92  ? 176 GLY B C   1 
ATOM   3811  O O   . GLY B  2 176 ? 14.447  0.990   -26.696 1.00 32.62  ? 176 GLY B O   1 
ATOM   3812  N N   . ASP C  1 5   ? 13.022  -16.744 -11.815 1.00 2.00   ? 11  ASP C N   1 
ATOM   3813  C CA  . ASP C  1 5   ? 13.644  -16.461 -10.488 1.00 2.29   ? 11  ASP C CA  1 
ATOM   3814  C C   . ASP C  1 5   ? 12.729  -15.598 -9.628  1.00 2.46   ? 11  ASP C C   1 
ATOM   3815  O O   . ASP C  1 5   ? 12.098  -14.667 -10.132 1.00 2.46   ? 11  ASP C O   1 
ATOM   3816  C CB  . ASP C  1 5   ? 15.004  -15.771 -10.654 1.00 2.46   ? 11  ASP C CB  1 
ATOM   3817  C CG  . ASP C  1 5   ? 15.997  -16.596 -11.469 1.00 4.34   ? 11  ASP C CG  1 
ATOM   3818  O OD1 . ASP C  1 5   ? 15.836  -17.834 -11.564 1.00 8.01   ? 11  ASP C OD1 1 
ATOM   3819  O OD2 . ASP C  1 5   ? 16.952  -16.001 -12.013 1.00 4.17   ? 11  ASP C OD2 1 
ATOM   3820  N N   . LYS C  1 6   ? 12.662  -15.907 -8.332  1.00 2.73   ? 12  LYS C N   1 
ATOM   3821  C CA  . LYS C  1 6   ? 11.784  -15.182 -7.408  1.00 3.28   ? 12  LYS C CA  1 
ATOM   3822  C C   . LYS C  1 6   ? 12.301  -15.130 -5.962  1.00 3.56   ? 12  LYS C C   1 
ATOM   3823  O O   . LYS C  1 6   ? 13.000  -16.041 -5.510  1.00 4.60   ? 12  LYS C O   1 
ATOM   3824  C CB  . LYS C  1 6   ? 10.355  -15.751 -7.451  1.00 3.67   ? 12  LYS C CB  1 
ATOM   3825  C CG  . LYS C  1 6   ? 10.192  -17.160 -6.884  1.00 5.52   ? 12  LYS C CG  1 
ATOM   3826  C CD  . LYS C  1 6   ? 8.745   -17.625 -6.972  1.00 9.41   ? 12  LYS C CD  1 
ATOM   3827  C CE  . LYS C  1 6   ? 8.572   -19.001 -6.348  1.00 13.20  ? 12  LYS C CE  1 
ATOM   3828  N NZ  . LYS C  1 6   ? 7.164   -19.479 -6.436  1.00 16.38  ? 12  LYS C NZ  1 
ATOM   3829  N N   . ILE C  1 7   ? 11.958  -14.056 -5.248  1.00 2.51   ? 13  ILE C N   1 
ATOM   3830  C CA  . ILE C  1 7   ? 12.256  -13.945 -3.820  1.00 2.00   ? 13  ILE C CA  1 
ATOM   3831  C C   . ILE C  1 7   ? 10.959  -13.810 -3.025  1.00 2.00   ? 13  ILE C C   1 
ATOM   3832  O O   . ILE C  1 7   ? 10.128  -12.953 -3.318  1.00 2.13   ? 13  ILE C O   1 
ATOM   3833  C CB  . ILE C  1 7   ? 13.272  -12.801 -3.493  1.00 2.01   ? 13  ILE C CB  1 
ATOM   3834  C CG1 . ILE C  1 7   ? 13.744  -12.898 -2.033  1.00 2.00   ? 13  ILE C CG1 1 
ATOM   3835  C CG2 . ILE C  1 7   ? 12.698  -11.415 -3.820  1.00 2.00   ? 13  ILE C CG2 1 
ATOM   3836  C CD1 . ILE C  1 7   ? 15.114  -12.284 -1.770  1.00 2.00   ? 13  ILE C CD1 1 
ATOM   3837  N N   . CYS C  1 8   ? 10.797  -14.674 -2.030  1.00 2.00   ? 14  CYS C N   1 
ATOM   3838  C CA  . CYS C  1 8   ? 9.558   -14.765 -1.276  1.00 2.00   ? 14  CYS C CA  1 
ATOM   3839  C C   . CYS C  1 8   ? 9.764   -14.377 0.179   1.00 2.00   ? 14  CYS C C   1 
ATOM   3840  O O   . CYS C  1 8   ? 10.729  -14.803 0.819   1.00 2.00   ? 14  CYS C O   1 
ATOM   3841  C CB  . CYS C  1 8   ? 9.001   -16.185 -1.352  1.00 2.00   ? 14  CYS C CB  1 
ATOM   3842  S SG  . CYS C  1 8   ? 8.550   -16.723 -2.998  0.60 2.00   ? 14  CYS C SG  1 
ATOM   3843  N N   . LEU C  1 9   ? 8.846   -13.574 0.703   1.00 2.00   ? 15  LEU C N   1 
ATOM   3844  C CA  . LEU C  1 9   ? 8.918   -13.166 2.094   1.00 2.00   ? 15  LEU C CA  1 
ATOM   3845  C C   . LEU C  1 9   ? 7.957   -13.966 2.950   1.00 2.00   ? 15  LEU C C   1 
ATOM   3846  O O   . LEU C  1 9   ? 6.875   -14.352 2.499   1.00 2.00   ? 15  LEU C O   1 
ATOM   3847  C CB  . LEU C  1 9   ? 8.690   -11.664 2.241   1.00 2.00   ? 15  LEU C CB  1 
ATOM   3848  C CG  . LEU C  1 9   ? 9.952   -10.850 1.959   1.00 2.00   ? 15  LEU C CG  1 
ATOM   3849  C CD1 . LEU C  1 9   ? 10.047  -10.425 0.503   1.00 2.00   ? 15  LEU C CD1 1 
ATOM   3850  C CD2 . LEU C  1 9   ? 9.988   -9.647  2.848   1.00 4.32   ? 15  LEU C CD2 1 
ATOM   3851  N N   . GLY C  1 10  ? 8.375   -14.230 4.181   1.00 2.00   ? 16  GLY C N   1 
ATOM   3852  C CA  . GLY C  1 10  ? 7.625   -15.082 5.082   1.00 2.02   ? 16  GLY C CA  1 
ATOM   3853  C C   . GLY C  1 10  ? 8.120   -14.956 6.503   1.00 2.40   ? 16  GLY C C   1 
ATOM   3854  O O   . GLY C  1 10  ? 8.950   -14.101 6.813   1.00 2.60   ? 16  GLY C O   1 
ATOM   3855  N N   . HIS C  1 11  ? 7.610   -15.826 7.363   1.00 2.63   ? 17  HIS C N   1 
ATOM   3856  C CA  . HIS C  1 11  ? 7.824   -15.715 8.792   1.00 3.16   ? 17  HIS C CA  1 
ATOM   3857  C C   . HIS C  1 11  ? 7.832   -17.106 9.418   1.00 4.28   ? 17  HIS C C   1 
ATOM   3858  O O   . HIS C  1 11  ? 7.402   -18.073 8.791   1.00 4.68   ? 17  HIS C O   1 
ATOM   3859  C CB  . HIS C  1 11  ? 6.719   -14.860 9.408   1.00 2.91   ? 17  HIS C CB  1 
ATOM   3860  C CG  . HIS C  1 11  ? 5.343   -15.393 9.165   1.00 2.80   ? 17  HIS C CG  1 
ATOM   3861  N ND1 . HIS C  1 11  ? 4.788   -16.397 9.930   1.00 2.60   ? 17  HIS C ND1 1 
ATOM   3862  C CD2 . HIS C  1 11  ? 4.414   -15.071 8.234   1.00 2.34   ? 17  HIS C CD2 1 
ATOM   3863  C CE1 . HIS C  1 11  ? 3.574   -16.665 9.484   1.00 3.09   ? 17  HIS C CE1 1 
ATOM   3864  N NE2 . HIS C  1 11  ? 3.322   -15.873 8.457   1.00 2.02   ? 17  HIS C NE2 1 
ATOM   3865  N N   . HIS C  1 12  ? 8.311   -17.205 10.653  1.00 5.02   ? 18  HIS C N   1 
ATOM   3866  C CA  . HIS C  1 12  ? 8.442   -18.505 11.300  1.00 6.44   ? 18  HIS C CA  1 
ATOM   3867  C C   . HIS C  1 12  ? 7.115   -19.036 11.845  1.00 7.06   ? 18  HIS C C   1 
ATOM   3868  O O   . HIS C  1 12  ? 6.140   -18.289 11.975  1.00 7.84   ? 18  HIS C O   1 
ATOM   3869  C CB  . HIS C  1 12  ? 9.542   -18.476 12.378  1.00 6.79   ? 18  HIS C CB  1 
ATOM   3870  C CG  . HIS C  1 12  ? 9.170   -17.734 13.627  1.00 7.30   ? 18  HIS C CG  1 
ATOM   3871  N ND1 . HIS C  1 12  ? 9.799   -17.960 14.834  1.00 9.45   ? 18  HIS C ND1 1 
ATOM   3872  C CD2 . HIS C  1 12  ? 8.236   -16.782 13.863  1.00 9.83   ? 18  HIS C CD2 1 
ATOM   3873  C CE1 . HIS C  1 12  ? 9.274   -17.175 15.757  1.00 6.51   ? 18  HIS C CE1 1 
ATOM   3874  N NE2 . HIS C  1 12  ? 8.322   -16.452 15.194  1.00 11.52  ? 18  HIS C NE2 1 
ATOM   3875  N N   . ALA C  1 13  ? 7.088   -20.335 12.125  1.00 7.22   ? 19  ALA C N   1 
ATOM   3876  C CA  . ALA C  1 13  ? 5.957   -20.989 12.770  1.00 8.24   ? 19  ALA C CA  1 
ATOM   3877  C C   . ALA C  1 13  ? 6.434   -22.275 13.440  1.00 9.39   ? 19  ALA C C   1 
ATOM   3878  O O   . ALA C  1 13  ? 7.481   -22.819 13.083  1.00 9.90   ? 19  ALA C O   1 
ATOM   3879  C CB  . ALA C  1 13  ? 4.859   -21.291 11.756  1.00 7.94   ? 19  ALA C CB  1 
ATOM   3880  N N   . VAL C  1 14  ? 5.674   -22.754 14.417  1.00 10.27  ? 20  VAL C N   1 
ATOM   3881  C CA  . VAL C  1 14  ? 5.964   -24.045 15.039  1.00 11.44  ? 20  VAL C CA  1 
ATOM   3882  C C   . VAL C  1 14  ? 4.823   -25.025 14.777  1.00 12.98  ? 20  VAL C C   1 
ATOM   3883  O O   . VAL C  1 14  ? 3.743   -24.623 14.338  1.00 13.94  ? 20  VAL C O   1 
ATOM   3884  C CB  . VAL C  1 14  ? 6.237   -23.924 16.565  1.00 11.45  ? 20  VAL C CB  1 
ATOM   3885  C CG1 . VAL C  1 14  ? 7.587   -23.260 16.820  1.00 8.59   ? 20  VAL C CG1 1 
ATOM   3886  C CG2 . VAL C  1 14  ? 5.099   -23.182 17.279  1.00 10.29  ? 20  VAL C CG2 1 
ATOM   3887  N N   . ALA C  1 15  ? 5.068   -26.306 15.034  1.00 14.35  ? 21  ALA C N   1 
ATOM   3888  C CA  . ALA C  1 15  ? 4.028   -27.323 14.894  1.00 15.96  ? 21  ALA C CA  1 
ATOM   3889  C C   . ALA C  1 15  ? 2.936   -27.147 15.959  1.00 17.03  ? 21  ALA C C   1 
ATOM   3890  O O   . ALA C  1 15  ? 1.749   -27.083 15.634  1.00 17.18  ? 21  ALA C O   1 
ATOM   3891  C CB  . ALA C  1 15  ? 4.636   -28.721 14.956  1.00 15.44  ? 21  ALA C CB  1 
ATOM   3892  N N   . ASN C  1 16  ? 3.353   -27.057 17.222  1.00 18.24  ? 22  ASN C N   1 
ATOM   3893  C CA  . ASN C  1 16  ? 2.437   -26.889 18.350  1.00 19.18  ? 22  ASN C CA  1 
ATOM   3894  C C   . ASN C  1 16  ? 2.600   -25.517 19.001  1.00 18.64  ? 22  ASN C C   1 
ATOM   3895  O O   . ASN C  1 16  ? 3.551   -25.280 19.753  1.00 18.35  ? 22  ASN C O   1 
ATOM   3896  C CB  . ASN C  1 16  ? 2.643   -27.997 19.394  1.00 19.76  ? 22  ASN C CB  1 
ATOM   3897  C CG  . ASN C  1 16  ? 2.548   -29.396 18.798  1.00 24.79  ? 22  ASN C CG  1 
ATOM   3898  O OD1 . ASN C  1 16  ? 1.552   -29.750 18.162  1.00 29.42  ? 22  ASN C OD1 1 
ATOM   3899  N ND2 . ASN C  1 16  ? 3.587   -30.202 19.010  1.00 27.60  ? 22  ASN C ND2 1 
ATOM   3900  N N   . GLY C  1 17  ? 1.669   -24.616 18.699  1.00 17.77  ? 23  GLY C N   1 
ATOM   3901  C CA  . GLY C  1 17  ? 1.665   -23.286 19.297  1.00 16.89  ? 23  GLY C CA  1 
ATOM   3902  C C   . GLY C  1 17  ? 0.985   -23.248 20.655  1.00 16.19  ? 23  GLY C C   1 
ATOM   3903  O O   . GLY C  1 17  ? 0.646   -24.290 21.221  1.00 15.80  ? 23  GLY C O   1 
ATOM   3904  N N   . THR C  1 18  ? 0.793   -22.039 21.178  1.00 15.01  ? 24  THR C N   1 
ATOM   3905  C CA  . THR C  1 18  ? 0.143   -21.841 22.467  1.00 14.10  ? 24  THR C CA  1 
ATOM   3906  C C   . THR C  1 18  ? -1.124  -21.011 22.271  1.00 12.82  ? 24  THR C C   1 
ATOM   3907  O O   . THR C  1 18  ? -1.090  -19.955 21.639  1.00 12.29  ? 24  THR C O   1 
ATOM   3908  C CB  . THR C  1 18  ? 1.092   -21.143 23.468  1.00 14.33  ? 24  THR C CB  1 
ATOM   3909  O OG1 . THR C  1 18  ? 2.383   -21.762 23.415  1.00 16.95  ? 24  THR C OG1 1 
ATOM   3910  C CG2 . THR C  1 18  ? 0.555   -21.236 24.888  1.00 15.42  ? 24  THR C CG2 1 
ATOM   3911  N N   . LYS C  1 19  ? -2.242  -21.505 22.798  1.00 11.62  ? 25  LYS C N   1 
ATOM   3912  C CA  . LYS C  1 19  ? -3.520  -20.810 22.679  1.00 10.66  ? 25  LYS C CA  1 
ATOM   3913  C C   . LYS C  1 19  ? -3.630  -19.660 23.682  1.00 10.34  ? 25  LYS C C   1 
ATOM   3914  O O   . LYS C  1 19  ? -3.428  -19.844 24.888  1.00 10.61  ? 25  LYS C O   1 
ATOM   3915  C CB  . LYS C  1 19  ? -4.693  -21.779 22.854  1.00 10.32  ? 25  LYS C CB  1 
ATOM   3916  C CG  . LYS C  1 19  ? -4.887  -22.748 21.699  1.00 11.56  ? 25  LYS C CG  1 
ATOM   3917  C CD  . LYS C  1 19  ? -6.218  -23.488 21.808  1.00 11.22  ? 25  LYS C CD  1 
ATOM   3918  C CE  . LYS C  1 19  ? -6.282  -24.664 20.847  1.00 11.38  ? 25  LYS C CE  1 
ATOM   3919  N NZ  . LYS C  1 19  ? -6.090  -24.234 19.433  1.00 14.07  ? 25  LYS C NZ  1 
ATOM   3920  N N   . VAL C  1 20  ? -3.939  -18.472 23.171  1.00 9.10   ? 26  VAL C N   1 
ATOM   3921  C CA  . VAL C  1 20  ? -4.161  -17.296 24.012  1.00 8.23   ? 26  VAL C CA  1 
ATOM   3922  C C   . VAL C  1 20  ? -5.457  -16.594 23.626  1.00 8.31   ? 26  VAL C C   1 
ATOM   3923  O O   . VAL C  1 20  ? -6.026  -16.856 22.562  1.00 8.55   ? 26  VAL C O   1 
ATOM   3924  C CB  . VAL C  1 20  ? -2.980  -16.281 23.955  1.00 7.71   ? 26  VAL C CB  1 
ATOM   3925  C CG1 . VAL C  1 20  ? -1.698  -16.905 24.487  1.00 9.08   ? 26  VAL C CG1 1 
ATOM   3926  C CG2 . VAL C  1 20  ? -2.777  -15.733 22.543  1.00 5.52   ? 26  VAL C CG2 1 
ATOM   3927  N N   . ASN C  1 21  ? -5.914  -15.701 24.496  1.00 8.17   ? 27  ASN C N   1 
ATOM   3928  C CA  . ASN C  1 21  ? -7.098  -14.896 24.223  1.00 7.85   ? 27  ASN C CA  1 
ATOM   3929  C C   . ASN C  1 21  ? -6.746  -13.453 23.877  1.00 7.15   ? 27  ASN C C   1 
ATOM   3930  O O   . ASN C  1 21  ? -5.786  -12.887 24.410  1.00 7.32   ? 27  ASN C O   1 
ATOM   3931  C CB  . ASN C  1 21  ? -8.060  -14.961 25.408  1.00 7.78   ? 27  ASN C CB  1 
ATOM   3932  C CG  . ASN C  1 21  ? -8.412  -16.390 25.788  1.00 10.11  ? 27  ASN C CG  1 
ATOM   3933  O OD1 . ASN C  1 21  ? -8.646  -17.239 24.917  1.00 11.66  ? 27  ASN C OD1 1 
ATOM   3934  N ND2 . ASN C  1 21  ? -8.445  -16.668 27.091  1.00 3.56   ? 27  ASN C ND2 1 
ATOM   3935  N N   . THR C  1 22  ? -7.509  -12.879 22.953  1.00 6.27   ? 28  THR C N   1 
ATOM   3936  C CA  . THR C  1 22  ? -7.353  -11.479 22.565  1.00 5.73   ? 28  THR C CA  1 
ATOM   3937  C C   . THR C  1 22  ? -8.694  -10.758 22.734  1.00 5.75   ? 28  THR C C   1 
ATOM   3938  O O   . THR C  1 22  ? -9.651  -11.329 23.270  1.00 5.95   ? 28  THR C O   1 
ATOM   3939  C CB  . THR C  1 22  ? -6.820  -11.328 21.102  1.00 5.42   ? 28  THR C CB  1 
ATOM   3940  O OG1 . THR C  1 22  ? -7.833  -11.702 20.162  1.00 5.45   ? 28  THR C OG1 1 
ATOM   3941  C CG2 . THR C  1 22  ? -5.581  -12.176 20.867  1.00 3.61   ? 28  THR C CG2 1 
ATOM   3942  N N   . LEU C  1 23  ? -8.764  -9.511  22.278  1.00 5.35   ? 29  LEU C N   1 
ATOM   3943  C CA  . LEU C  1 23  ? -10.009 -8.750  22.322  1.00 5.12   ? 29  LEU C CA  1 
ATOM   3944  C C   . LEU C  1 23  ? -11.067 -9.295  21.364  1.00 5.51   ? 29  LEU C C   1 
ATOM   3945  O O   . LEU C  1 23  ? -12.265 -9.179  21.629  1.00 6.21   ? 29  LEU C O   1 
ATOM   3946  C CB  . LEU C  1 23  ? -9.754  -7.272  22.019  1.00 4.94   ? 29  LEU C CB  1 
ATOM   3947  C CG  . LEU C  1 23  ? -8.861  -6.461  22.963  1.00 3.92   ? 29  LEU C CG  1 
ATOM   3948  C CD1 . LEU C  1 23  ? -8.610  -5.085  22.364  1.00 2.58   ? 29  LEU C CD1 1 
ATOM   3949  C CD2 . LEU C  1 23  ? -9.451  -6.348  24.364  1.00 2.00   ? 29  LEU C CD2 1 
ATOM   3950  N N   . THR C  1 24  ? -10.629 -9.890  20.257  1.00 5.35   ? 30  THR C N   1 
ATOM   3951  C CA  . THR C  1 24  ? -11.559 -10.369 19.230  1.00 5.49   ? 30  THR C CA  1 
ATOM   3952  C C   . THR C  1 24  ? -11.692 -11.899 19.151  1.00 6.31   ? 30  THR C C   1 
ATOM   3953  O O   . THR C  1 24  ? -12.656 -12.407 18.576  1.00 5.59   ? 30  THR C O   1 
ATOM   3954  C CB  . THR C  1 24  ? -11.205 -9.809  17.835  1.00 4.53   ? 30  THR C CB  1 
ATOM   3955  O OG1 . THR C  1 24  ? -9.854  -10.144 17.512  1.00 5.76   ? 30  THR C OG1 1 
ATOM   3956  C CG2 . THR C  1 24  ? -11.358 -8.296  17.804  1.00 5.87   ? 30  THR C CG2 1 
ATOM   3957  N N   . GLU C  1 25  ? -10.739 -12.628 19.731  1.00 7.73   ? 31  GLU C N   1 
ATOM   3958  C CA  . GLU C  1 25  ? -10.707 -14.089 19.594  1.00 9.09   ? 31  GLU C CA  1 
ATOM   3959  C C   . GLU C  1 25  ? -10.456 -14.839 20.899  1.00 9.44   ? 31  GLU C C   1 
ATOM   3960  O O   . GLU C  1 25  ? -9.832  -14.313 21.820  1.00 9.48   ? 31  GLU C O   1 
ATOM   3961  C CB  . GLU C  1 25  ? -9.674  -14.509 18.540  1.00 9.38   ? 31  GLU C CB  1 
ATOM   3962  C CG  . GLU C  1 25  ? -9.960  -13.972 17.136  1.00 13.20  ? 31  GLU C CG  1 
ATOM   3963  C CD  . GLU C  1 25  ? -9.151  -14.659 16.056  1.00 15.02  ? 31  GLU C CD  1 
ATOM   3964  O OE1 . GLU C  1 25  ? -9.266  -15.896 15.913  1.00 17.11  ? 31  GLU C OE1 1 
ATOM   3965  O OE2 . GLU C  1 25  ? -8.411  -13.956 15.338  1.00 16.45  ? 31  GLU C OE2 1 
ATOM   3966  N N   . ARG C  1 26  ? -10.962 -16.070 20.961  1.00 10.51  ? 32  ARG C N   1 
ATOM   3967  C CA  . ARG C  1 26  ? -10.678 -16.991 22.064  1.00 11.51  ? 32  ARG C CA  1 
ATOM   3968  C C   . ARG C  1 26  ? -9.863  -18.190 21.587  1.00 11.07  ? 32  ARG C C   1 
ATOM   3969  O O   . ARG C  1 26  ? -10.234 -18.863 20.624  1.00 10.67  ? 32  ARG C O   1 
ATOM   3970  C CB  . ARG C  1 26  ? -11.969 -17.468 22.744  1.00 11.53  ? 32  ARG C CB  1 
ATOM   3971  C CG  . ARG C  1 26  ? -12.538 -16.481 23.753  1.00 15.08  ? 32  ARG C CG  1 
ATOM   3972  C CD  . ARG C  1 26  ? -13.404 -17.168 24.806  1.00 23.21  ? 32  ARG C CD  1 
ATOM   3973  N NE  . ARG C  1 26  ? -12.614 -17.906 25.798  1.00 28.38  ? 32  ARG C NE  1 
ATOM   3974  C CZ  . ARG C  1 26  ? -12.087 -17.374 26.903  1.00 30.60  ? 32  ARG C CZ  1 
ATOM   3975  N NH1 . ARG C  1 26  ? -12.247 -16.084 27.179  1.00 29.16  ? 32  ARG C NH1 1 
ATOM   3976  N NH2 . ARG C  1 26  ? -11.388 -18.137 27.735  1.00 32.17  ? 32  ARG C NH2 1 
ATOM   3977  N N   . GLY C  1 27  ? -8.748  -18.442 22.269  1.00 11.26  ? 33  GLY C N   1 
ATOM   3978  C CA  . GLY C  1 27  ? -7.900  -19.595 21.978  1.00 11.17  ? 33  GLY C CA  1 
ATOM   3979  C C   . GLY C  1 27  ? -7.183  -19.533 20.642  1.00 11.40  ? 33  GLY C C   1 
ATOM   3980  O O   . GLY C  1 27  ? -6.967  -20.565 20.002  1.00 11.26  ? 33  GLY C O   1 
ATOM   3981  N N   . ILE C  1 28  ? -6.823  -18.323 20.219  1.00 11.72  ? 34  ILE C N   1 
ATOM   3982  C CA  . ILE C  1 28  ? -6.018  -18.129 19.015  1.00 11.91  ? 34  ILE C CA  1 
ATOM   3983  C C   . ILE C  1 28  ? -4.579  -18.575 19.299  1.00 11.76  ? 34  ILE C C   1 
ATOM   3984  O O   . ILE C  1 28  ? -4.049  -18.333 20.384  1.00 11.66  ? 34  ILE C O   1 
ATOM   3985  C CB  . ILE C  1 28  ? -6.100  -16.662 18.487  1.00 12.04  ? 34  ILE C CB  1 
ATOM   3986  C CG1 . ILE C  1 28  ? -5.554  -16.567 17.059  1.00 15.26  ? 34  ILE C CG1 1 
ATOM   3987  C CG2 . ILE C  1 28  ? -5.404  -15.676 19.432  1.00 12.26  ? 34  ILE C CG2 1 
ATOM   3988  C CD1 . ILE C  1 28  ? -5.639  -15.181 16.434  1.00 21.20  ? 34  ILE C CD1 1 
ATOM   3989  N N   . GLU C  1 29  ? -3.964  -19.242 18.328  1.00 12.15  ? 35  GLU C N   1 
ATOM   3990  C CA  . GLU C  1 29  ? -2.667  -19.885 18.524  1.00 12.62  ? 35  GLU C CA  1 
ATOM   3991  C C   . GLU C  1 29  ? -1.504  -18.948 18.182  1.00 12.11  ? 35  GLU C C   1 
ATOM   3992  O O   . GLU C  1 29  ? -1.427  -18.419 17.069  1.00 11.63  ? 35  GLU C O   1 
ATOM   3993  C CB  . GLU C  1 29  ? -2.597  -21.163 17.675  1.00 13.74  ? 35  GLU C CB  1 
ATOM   3994  C CG  . GLU C  1 29  ? -1.698  -22.274 18.223  1.00 16.21  ? 35  GLU C CG  1 
ATOM   3995  C CD  . GLU C  1 29  ? -1.488  -23.415 17.224  1.00 20.49  ? 35  GLU C CD  1 
ATOM   3996  O OE1 . GLU C  1 29  ? -1.514  -24.594 17.643  1.00 20.69  ? 35  GLU C OE1 1 
ATOM   3997  O OE2 . GLU C  1 29  ? -1.297  -23.135 16.017  1.00 21.89  ? 35  GLU C OE2 1 
ATOM   3998  N N   . VAL C  1 30  ? -0.614  -18.742 19.152  1.00 11.88  ? 36  VAL C N   1 
ATOM   3999  C CA  . VAL C  1 30  ? 0.607   -17.949 18.950  1.00 11.88  ? 36  VAL C CA  1 
ATOM   4000  C C   . VAL C  1 30  ? 1.862   -18.823 19.049  1.00 12.54  ? 36  VAL C C   1 
ATOM   4001  O O   . VAL C  1 30  ? 1.797   -19.956 19.525  1.00 13.18  ? 36  VAL C O   1 
ATOM   4002  C CB  . VAL C  1 30  ? 0.713   -16.747 19.937  1.00 11.70  ? 36  VAL C CB  1 
ATOM   4003  C CG1 . VAL C  1 30  ? -0.297  -15.659 19.585  1.00 10.46  ? 36  VAL C CG1 1 
ATOM   4004  C CG2 . VAL C  1 30  ? 0.551   -17.197 21.382  1.00 10.47  ? 36  VAL C CG2 1 
ATOM   4005  N N   . VAL C  1 31  ? 2.996   -18.287 18.599  1.00 12.96  ? 37  VAL C N   1 
ATOM   4006  C CA  . VAL C  1 31  ? 4.277   -19.011 18.586  1.00 13.29  ? 37  VAL C CA  1 
ATOM   4007  C C   . VAL C  1 31  ? 4.771   -19.362 20.000  1.00 14.64  ? 37  VAL C C   1 
ATOM   4008  O O   . VAL C  1 31  ? 5.239   -20.479 20.245  1.00 14.97  ? 37  VAL C O   1 
ATOM   4009  C CB  . VAL C  1 31  ? 5.357   -18.211 17.793  1.00 12.64  ? 37  VAL C CB  1 
ATOM   4010  C CG1 . VAL C  1 31  ? 6.765   -18.707 18.088  1.00 13.84  ? 37  VAL C CG1 1 
ATOM   4011  C CG2 . VAL C  1 31  ? 5.077   -18.282 16.303  1.00 11.34  ? 37  VAL C CG2 1 
ATOM   4012  N N   . ASN C  1 32  ? 4.650   -18.405 20.919  1.00 15.87  ? 38  ASN C N   1 
ATOM   4013  C CA  . ASN C  1 32  ? 5.074   -18.577 22.306  1.00 17.02  ? 38  ASN C CA  1 
ATOM   4014  C C   . ASN C  1 32  ? 4.323   -17.618 23.235  1.00 16.15  ? 38  ASN C C   1 
ATOM   4015  O O   . ASN C  1 32  ? 3.865   -16.554 22.807  1.00 15.28  ? 38  ASN C O   1 
ATOM   4016  C CB  . ASN C  1 32  ? 6.591   -18.371 22.430  1.00 18.01  ? 38  ASN C CB  1 
ATOM   4017  C CG  . ASN C  1 32  ? 7.174   -18.982 23.699  1.00 24.93  ? 38  ASN C CG  1 
ATOM   4018  O OD1 . ASN C  1 32  ? 6.507   -19.734 24.417  1.00 24.86  ? 38  ASN C OD1 1 
ATOM   4019  N ND2 . ASN C  1 32  ? 8.435   -18.658 23.976  1.00 38.82  ? 38  ASN C ND2 1 
ATOM   4020  N N   . ALA C  1 33  ? 4.205   -18.006 24.504  1.00 15.83  ? 39  ALA C N   1 
ATOM   4021  C CA  . ALA C  1 33  ? 3.491   -17.222 25.509  1.00 15.83  ? 39  ALA C CA  1 
ATOM   4022  C C   . ALA C  1 33  ? 4.081   -17.424 26.901  1.00 16.20  ? 39  ALA C C   1 
ATOM   4023  O O   . ALA C  1 33  ? 4.725   -18.435 27.166  1.00 16.24  ? 39  ALA C O   1 
ATOM   4024  C CB  . ALA C  1 33  ? 2.010   -17.583 25.505  1.00 15.03  ? 39  ALA C CB  1 
ATOM   4025  N N   . THR C  1 34  ? 3.855   -16.456 27.786  1.00 17.38  ? 40  THR C N   1 
ATOM   4026  C CA  . THR C  1 34  ? 4.312   -16.543 29.173  1.00 17.97  ? 40  THR C CA  1 
ATOM   4027  C C   . THR C  1 34  ? 3.147   -16.366 30.144  1.00 17.45  ? 40  THR C C   1 
ATOM   4028  O O   . THR C  1 34  ? 2.282   -15.514 29.945  1.00 17.81  ? 40  THR C O   1 
ATOM   4029  C CB  . THR C  1 34  ? 5.405   -15.493 29.488  1.00 17.84  ? 40  THR C CB  1 
ATOM   4030  O OG1 . THR C  1 34  ? 6.478   -15.622 28.551  1.00 19.54  ? 40  THR C OG1 1 
ATOM   4031  C CG2 . THR C  1 34  ? 5.963   -15.693 30.889  1.00 21.47  ? 40  THR C CG2 1 
ATOM   4032  N N   . GLU C  1 35  ? 3.143   -17.190 31.188  1.00 16.78  ? 41  GLU C N   1 
ATOM   4033  C CA  . GLU C  1 35  ? 2.183   -17.098 32.280  1.00 15.54  ? 41  GLU C CA  1 
ATOM   4034  C C   . GLU C  1 35  ? 2.373   -15.806 33.073  1.00 15.07  ? 41  GLU C C   1 
ATOM   4035  O O   . GLU C  1 35  ? 3.504   -15.413 33.370  1.00 15.89  ? 41  GLU C O   1 
ATOM   4036  C CB  . GLU C  1 35  ? 2.350   -18.311 33.204  1.00 15.22  ? 41  GLU C CB  1 
ATOM   4037  C CG  . GLU C  1 35  ? 1.317   -18.427 34.307  1.00 14.21  ? 41  GLU C CG  1 
ATOM   4038  C CD  . GLU C  1 35  ? -0.094  -18.326 33.785  1.00 14.44  ? 41  GLU C CD  1 
ATOM   4039  O OE1 . GLU C  1 35  ? -0.528  -19.254 33.073  1.00 15.77  ? 41  GLU C OE1 1 
ATOM   4040  O OE2 . GLU C  1 35  ? -0.763  -17.314 34.081  1.00 14.80  ? 41  GLU C OE2 1 
ATOM   4041  N N   . THR C  1 36  ? 1.263   -15.154 33.411  1.00 14.03  ? 42  THR C N   1 
ATOM   4042  C CA  . THR C  1 36  ? 1.292   -13.938 34.224  1.00 12.96  ? 42  THR C CA  1 
ATOM   4043  C C   . THR C  1 36  ? 0.694   -14.160 35.615  1.00 13.04  ? 42  THR C C   1 
ATOM   4044  O O   . THR C  1 36  ? 0.804   -13.292 36.484  1.00 13.67  ? 42  THR C O   1 
ATOM   4045  C CB  . THR C  1 36  ? 0.559   -12.754 33.542  1.00 13.26  ? 42  THR C CB  1 
ATOM   4046  O OG1 . THR C  1 36  ? -0.811  -13.102 33.299  1.00 13.80  ? 42  THR C OG1 1 
ATOM   4047  C CG2 . THR C  1 36  ? 1.232   -12.368 32.226  1.00 12.14  ? 42  THR C CG2 1 
ATOM   4048  N N   . VAL C  1 37  ? 0.061   -15.314 35.822  1.00 12.19  ? 43  VAL C N   1 
ATOM   4049  C CA  . VAL C  1 37  ? -0.535  -15.649 37.116  1.00 11.76  ? 43  VAL C CA  1 
ATOM   4050  C C   . VAL C  1 37  ? 0.325   -16.690 37.837  1.00 12.84  ? 43  VAL C C   1 
ATOM   4051  O O   . VAL C  1 37  ? 0.455   -17.824 37.375  1.00 13.58  ? 43  VAL C O   1 
ATOM   4052  C CB  . VAL C  1 37  ? -1.989  -16.176 36.963  1.00 11.31  ? 43  VAL C CB  1 
ATOM   4053  C CG1 . VAL C  1 37  ? -2.614  -16.452 38.324  1.00 8.37   ? 43  VAL C CG1 1 
ATOM   4054  C CG2 . VAL C  1 37  ? -2.844  -15.191 36.180  1.00 10.18  ? 43  VAL C CG2 1 
ATOM   4055  N N   . GLU C  1 38  ? 0.912   -16.304 38.966  1.00 13.49  ? 44  GLU C N   1 
ATOM   4056  C CA  . GLU C  1 38  ? 1.729   -17.230 39.749  1.00 14.14  ? 44  GLU C CA  1 
ATOM   4057  C C   . GLU C  1 38  ? 0.854   -18.246 40.468  1.00 14.39  ? 44  GLU C C   1 
ATOM   4058  O O   . GLU C  1 38  ? -0.142  -17.877 41.094  1.00 14.96  ? 44  GLU C O   1 
ATOM   4059  C CB  . GLU C  1 38  ? 2.603   -16.486 40.762  1.00 14.13  ? 44  GLU C CB  1 
ATOM   4060  C CG  . GLU C  1 38  ? 3.585   -17.395 41.514  1.00 16.84  ? 44  GLU C CG  1 
ATOM   4061  C CD  . GLU C  1 38  ? 4.528   -18.144 40.580  1.00 16.68  ? 44  GLU C CD  1 
ATOM   4062  O OE1 . GLU C  1 38  ? 5.169   -17.491 39.729  1.00 14.98  ? 44  GLU C OE1 1 
ATOM   4063  O OE2 . GLU C  1 38  ? 4.624   -19.385 40.694  1.00 17.32  ? 44  GLU C OE2 1 
ATOM   4064  N N   . THR C  1 39  ? 1.223   -19.521 40.366  1.00 14.27  ? 45  THR C N   1 
ATOM   4065  C CA  . THR C  1 39  ? 0.467   -20.593 41.019  1.00 14.33  ? 45  THR C CA  1 
ATOM   4066  C C   . THR C  1 39  ? 1.355   -21.558 41.803  1.00 14.49  ? 45  THR C C   1 
ATOM   4067  O O   . THR C  1 39  ? 0.857   -22.506 42.415  1.00 13.91  ? 45  THR C O   1 
ATOM   4068  C CB  . THR C  1 39  ? -0.425  -21.389 40.021  1.00 14.52  ? 45  THR C CB  1 
ATOM   4069  O OG1 . THR C  1 39  ? 0.356   -21.816 38.898  1.00 14.22  ? 45  THR C OG1 1 
ATOM   4070  C CG2 . THR C  1 39  ? -1.609  -20.542 39.540  1.00 12.60  ? 45  THR C CG2 1 
ATOM   4071  N N   . THR C  1 40  ? 2.664   -21.312 41.790  1.00 15.02  ? 46  THR C N   1 
ATOM   4072  C CA  . THR C  1 40  ? 3.596   -22.130 42.560  1.00 16.38  ? 46  THR C CA  1 
ATOM   4073  C C   . THR C  1 40  ? 3.841   -21.531 43.945  1.00 16.91  ? 46  THR C C   1 
ATOM   4074  O O   . THR C  1 40  ? 4.496   -20.495 44.091  1.00 16.77  ? 46  THR C O   1 
ATOM   4075  C CB  . THR C  1 40  ? 4.933   -22.372 41.808  1.00 17.12  ? 46  THR C CB  1 
ATOM   4076  O OG1 . THR C  1 40  ? 4.661   -22.891 40.499  1.00 18.33  ? 46  THR C OG1 1 
ATOM   4077  C CG2 . THR C  1 40  ? 5.816   -23.364 42.570  1.00 13.58  ? 46  THR C CG2 1 
ATOM   4078  N N   . ASN C  1 41  ? 3.296   -22.198 44.956  1.00 17.76  ? 47  ASN C N   1 
ATOM   4079  C CA  . ASN C  1 41  ? 3.477   -21.795 46.342  1.00 18.21  ? 47  ASN C CA  1 
ATOM   4080  C C   . ASN C  1 41  ? 4.626   -22.549 47.009  1.00 18.92  ? 47  ASN C C   1 
ATOM   4081  O O   . ASN C  1 41  ? 4.841   -23.733 46.745  1.00 19.27  ? 47  ASN C O   1 
ATOM   4082  C CB  . ASN C  1 41  ? 2.184   -22.025 47.125  1.00 17.79  ? 47  ASN C CB  1 
ATOM   4083  C CG  . ASN C  1 41  ? 2.323   -21.681 48.592  1.00 17.50  ? 47  ASN C CG  1 
ATOM   4084  O OD1 . ASN C  1 41  ? 2.626   -20.541 48.948  1.00 16.57  ? 47  ASN C OD1 1 
ATOM   4085  N ND2 . ASN C  1 41  ? 2.111   -22.672 49.455  1.00 12.75  ? 47  ASN C ND2 1 
ATOM   4086  N N   . ILE C  1 42  ? 5.370   -21.851 47.861  1.00 19.11  ? 48  ILE C N   1 
ATOM   4087  C CA  . ILE C  1 42  ? 6.345   -22.500 48.725  1.00 19.43  ? 48  ILE C CA  1 
ATOM   4088  C C   . ILE C  1 42  ? 5.676   -22.701 50.080  1.00 19.71  ? 48  ILE C C   1 
ATOM   4089  O O   . ILE C  1 42  ? 5.282   -21.730 50.736  1.00 20.20  ? 48  ILE C O   1 
ATOM   4090  C CB  . ILE C  1 42  ? 7.654   -21.679 48.839  1.00 19.74  ? 48  ILE C CB  1 
ATOM   4091  C CG1 . ILE C  1 42  ? 8.410   -21.713 47.506  1.00 20.65  ? 48  ILE C CG1 1 
ATOM   4092  C CG2 . ILE C  1 42  ? 8.539   -22.206 49.971  1.00 19.30  ? 48  ILE C CG2 1 
ATOM   4093  C CD1 . ILE C  1 42  ? 9.390   -20.569 47.315  1.00 23.40  ? 48  ILE C CD1 1 
ATOM   4094  N N   . LYS C  1 43  ? 5.536   -23.964 50.481  1.00 19.49  ? 49  LYS C N   1 
ATOM   4095  C CA  . LYS C  1 43  ? 4.801   -24.331 51.697  1.00 19.02  ? 49  LYS C CA  1 
ATOM   4096  C C   . LYS C  1 43  ? 5.621   -24.117 52.972  1.00 18.09  ? 49  LYS C C   1 
ATOM   4097  O O   . LYS C  1 43  ? 5.560   -24.920 53.910  1.00 18.09  ? 49  LYS C O   1 
ATOM   4098  C CB  . LYS C  1 43  ? 4.309   -25.780 51.610  1.00 19.63  ? 49  LYS C CB  1 
ATOM   4099  C CG  . LYS C  1 43  ? 3.266   -26.028 50.533  1.00 23.16  ? 49  LYS C CG  1 
ATOM   4100  C CD  . LYS C  1 43  ? 2.418   -27.244 50.868  1.00 29.15  ? 49  LYS C CD  1 
ATOM   4101  C CE  . LYS C  1 43  ? 1.105   -27.221 50.099  1.00 32.16  ? 49  LYS C CE  1 
ATOM   4102  N NZ  . LYS C  1 43  ? 0.089   -28.131 50.700  1.00 31.80  ? 49  LYS C NZ  1 
ATOM   4103  N N   . LYS C  1 44  ? 6.381   -23.025 52.995  1.00 16.86  ? 50  LYS C N   1 
ATOM   4104  C CA  . LYS C  1 44  ? 7.267   -22.691 54.102  1.00 16.20  ? 50  LYS C CA  1 
ATOM   4105  C C   . LYS C  1 44  ? 7.256   -21.183 54.318  1.00 15.83  ? 50  LYS C C   1 
ATOM   4106  O O   . LYS C  1 44  ? 6.907   -20.428 53.411  1.00 16.15  ? 50  LYS C O   1 
ATOM   4107  C CB  . LYS C  1 44  ? 8.698   -23.144 53.792  1.00 16.58  ? 50  LYS C CB  1 
ATOM   4108  C CG  . LYS C  1 44  ? 8.852   -24.644 53.551  1.00 18.28  ? 50  LYS C CG  1 
ATOM   4109  C CD  . LYS C  1 44  ? 10.288  -25.058 53.271  1.00 19.85  ? 50  LYS C CD  1 
ATOM   4110  C CE  . LYS C  1 44  ? 10.707  -24.782 51.830  1.00 20.09  ? 50  LYS C CE  1 
ATOM   4111  N NZ  . LYS C  1 44  ? 11.977  -25.502 51.501  1.00 17.42  ? 50  LYS C NZ  1 
ATOM   4112  N N   . ILE C  1 45  ? 7.619   -20.748 55.521  1.00 14.98  ? 51  ILE C N   1 
ATOM   4113  C CA  . ILE C  1 45  ? 7.894   -19.337 55.766  1.00 13.72  ? 51  ILE C CA  1 
ATOM   4114  C C   . ILE C  1 45  ? 9.376   -19.121 55.491  1.00 14.00  ? 51  ILE C C   1 
ATOM   4115  O O   . ILE C  1 45  ? 10.230  -19.579 56.251  1.00 14.80  ? 51  ILE C O   1 
ATOM   4116  C CB  . ILE C  1 45  ? 7.542   -18.908 57.210  1.00 13.20  ? 51  ILE C CB  1 
ATOM   4117  C CG1 . ILE C  1 45  ? 6.055   -19.147 57.516  1.00 13.77  ? 51  ILE C CG1 1 
ATOM   4118  C CG2 . ILE C  1 45  ? 7.929   -17.455 57.454  1.00 10.86  ? 51  ILE C CG2 1 
ATOM   4119  C CD1 . ILE C  1 45  ? 5.077   -18.204 56.813  1.00 16.37  ? 51  ILE C CD1 1 
ATOM   4120  N N   . CYS C  1 46  ? 9.677   -18.449 54.386  1.00 14.40  ? 52  CYS C N   1 
ATOM   4121  C CA  . CYS C  1 46  ? 11.061  -18.226 53.977  1.00 14.35  ? 52  CYS C CA  1 
ATOM   4122  C C   . CYS C  1 46  ? 11.698  -17.099 54.792  1.00 14.43  ? 52  CYS C C   1 
ATOM   4123  O O   . CYS C  1 46  ? 11.410  -15.915 54.578  1.00 13.67  ? 52  CYS C O   1 
ATOM   4124  C CB  . CYS C  1 46  ? 11.142  -17.957 52.474  1.00 14.28  ? 52  CYS C CB  1 
ATOM   4125  S SG  . CYS C  1 46  ? 10.789  -19.406 51.450  1.00 13.66  ? 52  CYS C SG  1 
ATOM   4126  N N   . THR C  1 47  ? 12.563  -17.488 55.727  1.00 14.43  ? 53  THR C N   1 
ATOM   4127  C CA  . THR C  1 47  ? 13.102  -16.560 56.722  1.00 15.19  ? 53  THR C CA  1 
ATOM   4128  C C   . THR C  1 47  ? 14.560  -16.146 56.493  1.00 16.01  ? 53  THR C C   1 
ATOM   4129  O O   . THR C  1 47  ? 15.158  -15.499 57.356  1.00 16.16  ? 53  THR C O   1 
ATOM   4130  C CB  . THR C  1 47  ? 12.952  -17.108 58.171  1.00 15.23  ? 53  THR C CB  1 
ATOM   4131  O OG1 . THR C  1 47  ? 13.737  -18.299 58.336  1.00 14.50  ? 53  THR C OG1 1 
ATOM   4132  C CG2 . THR C  1 47  ? 11.497  -17.390 58.499  1.00 13.36  ? 53  THR C CG2 1 
ATOM   4133  N N   . GLN C  1 48  ? 15.128  -16.507 55.343  1.00 16.45  ? 54  GLN C N   1 
ATOM   4134  C CA  . GLN C  1 48  ? 16.495  -16.098 55.020  1.00 16.92  ? 54  GLN C CA  1 
ATOM   4135  C C   . GLN C  1 48  ? 16.598  -14.579 54.894  1.00 17.32  ? 54  GLN C C   1 
ATOM   4136  O O   . GLN C  1 48  ? 15.758  -13.940 54.259  1.00 17.52  ? 54  GLN C O   1 
ATOM   4137  C CB  . GLN C  1 48  ? 16.987  -16.767 53.741  1.00 16.74  ? 54  GLN C CB  1 
ATOM   4138  C CG  . GLN C  1 48  ? 18.490  -16.663 53.536  1.00 16.90  ? 54  GLN C CG  1 
ATOM   4139  C CD  . GLN C  1 48  ? 18.934  -17.161 52.178  1.00 18.24  ? 54  GLN C CD  1 
ATOM   4140  O OE1 . GLN C  1 48  ? 18.280  -16.911 51.165  1.00 20.38  ? 54  GLN C OE1 1 
ATOM   4141  N NE2 . GLN C  1 48  ? 20.058  -17.865 52.148  1.00 16.83  ? 54  GLN C NE2 1 
ATOM   4142  N N   . GLY C  1 49  ? 17.629  -14.012 55.516  1.00 17.91  ? 55  GLY C N   1 
ATOM   4143  C CA  . GLY C  1 49  ? 17.842  -12.568 55.518  1.00 18.75  ? 55  GLY C CA  1 
ATOM   4144  C C   . GLY C  1 49  ? 17.108  -11.865 56.645  1.00 19.53  ? 55  GLY C C   1 
ATOM   4145  O O   . GLY C  1 49  ? 17.392  -10.707 56.954  1.00 20.34  ? 55  GLY C O   1 
ATOM   4146  N N   . LYS C  1 50  ? 16.172  -12.578 57.267  1.00 19.71  ? 56  LYS C N   1 
ATOM   4147  C CA  . LYS C  1 50  ? 15.313  -12.020 58.307  1.00 19.41  ? 56  LYS C CA  1 
ATOM   4148  C C   . LYS C  1 50  ? 15.777  -12.419 59.709  1.00 19.16  ? 56  LYS C C   1 
ATOM   4149  O O   . LYS C  1 50  ? 16.668  -13.260 59.870  1.00 18.35  ? 56  LYS C O   1 
ATOM   4150  C CB  . LYS C  1 50  ? 13.865  -12.491 58.101  1.00 19.43  ? 56  LYS C CB  1 
ATOM   4151  C CG  . LYS C  1 50  ? 13.315  -12.336 56.685  1.00 20.01  ? 56  LYS C CG  1 
ATOM   4152  C CD  . LYS C  1 50  ? 12.785  -10.934 56.429  1.00 21.48  ? 56  LYS C CD  1 
ATOM   4153  C CE  . LYS C  1 50  ? 11.916  -10.883 55.182  1.00 23.25  ? 56  LYS C CE  1 
ATOM   4154  N NZ  . LYS C  1 50  ? 12.686  -11.179 53.942  1.00 23.28  ? 56  LYS C NZ  1 
ATOM   4155  N N   . ARG C  1 51  ? 15.168  -11.793 60.715  1.00 19.29  ? 57  ARG C N   1 
ATOM   4156  C CA  . ARG C  1 51  ? 15.285  -12.229 62.104  1.00 19.33  ? 57  ARG C CA  1 
ATOM   4157  C C   . ARG C  1 51  ? 13.888  -12.611 62.596  1.00 18.11  ? 57  ARG C C   1 
ATOM   4158  O O   . ARG C  1 51  ? 13.207  -11.787 63.198  1.00 17.94  ? 57  ARG C O   1 
ATOM   4159  C CB  . ARG C  1 51  ? 15.875  -11.120 62.984  1.00 19.83  ? 57  ARG C CB  1 
ATOM   4160  C CG  . ARG C  1 51  ? 17.382  -10.910 62.837  1.00 23.11  ? 57  ARG C CG  1 
ATOM   4161  C CD  . ARG C  1 51  ? 17.850  -9.648  63.570  1.00 28.75  ? 57  ARG C CD  1 
ATOM   4162  N NE  . ARG C  1 51  ? 17.269  -8.430  62.997  1.00 32.40  ? 57  ARG C NE  1 
ATOM   4163  C CZ  . ARG C  1 51  ? 16.337  -7.677  63.583  1.00 33.01  ? 57  ARG C CZ  1 
ATOM   4164  N NH1 . ARG C  1 51  ? 15.864  -7.991  64.786  1.00 31.63  ? 57  ARG C NH1 1 
ATOM   4165  N NH2 . ARG C  1 51  ? 15.880  -6.596  62.963  1.00 32.56  ? 57  ARG C NH2 1 
ATOM   4166  N N   . PRO C  1 52  ? 13.452  -13.859 62.331  1.00 16.93  ? 58  PRO C N   1 
ATOM   4167  C CA  . PRO C  1 52  ? 12.072  -14.242 62.631  1.00 16.34  ? 58  PRO C CA  1 
ATOM   4168  C C   . PRO C  1 52  ? 11.820  -14.577 64.099  1.00 16.71  ? 58  PRO C C   1 
ATOM   4169  O O   . PRO C  1 52  ? 12.735  -14.994 64.811  1.00 16.13  ? 58  PRO C O   1 
ATOM   4170  C CB  . PRO C  1 52  ? 11.874  -15.495 61.783  1.00 16.20  ? 58  PRO C CB  1 
ATOM   4171  C CG  . PRO C  1 52  ? 13.227  -16.113 61.722  1.00 16.15  ? 58  PRO C CG  1 
ATOM   4172  C CD  . PRO C  1 52  ? 14.219  -14.977 61.748  1.00 16.43  ? 58  PRO C CD  1 
ATOM   4173  N N   . THR C  1 53  ? 10.578  -14.384 64.536  1.00 17.72  ? 59  THR C N   1 
ATOM   4174  C CA  . THR C  1 53  ? 10.125  -14.875 65.836  1.00 18.21  ? 59  THR C CA  1 
ATOM   4175  C C   . THR C  1 53  ? 8.901   -15.768 65.664  1.00 18.16  ? 59  THR C C   1 
ATOM   4176  O O   . THR C  1 53  ? 7.834   -15.314 65.243  1.00 18.36  ? 59  THR C O   1 
ATOM   4177  C CB  . THR C  1 53  ? 9.835   -13.729 66.834  1.00 18.52  ? 59  THR C CB  1 
ATOM   4178  O OG1 . THR C  1 53  ? 11.074  -13.142 67.247  1.00 19.41  ? 59  THR C OG1 1 
ATOM   4179  C CG2 . THR C  1 53  ? 9.096   -14.246 68.076  1.00 17.93  ? 59  THR C CG2 1 
ATOM   4180  N N   . ASP C  1 54  ? 9.084   -17.048 65.971  1.00 18.27  ? 60  ASP C N   1 
ATOM   4181  C CA  . ASP C  1 54  ? 7.993   -18.006 66.000  1.00 18.10  ? 60  ASP C CA  1 
ATOM   4182  C C   . ASP C  1 54  ? 7.468   -18.062 67.427  1.00 18.12  ? 60  ASP C C   1 
ATOM   4183  O O   . ASP C  1 54  ? 8.118   -18.620 68.318  1.00 18.27  ? 60  ASP C O   1 
ATOM   4184  C CB  . ASP C  1 54  ? 8.480   -19.385 65.548  1.00 18.16  ? 60  ASP C CB  1 
ATOM   4185  C CG  . ASP C  1 54  ? 7.348   -20.380 65.370  1.00 17.90  ? 60  ASP C CG  1 
ATOM   4186  O OD1 . ASP C  1 54  ? 6.192   -20.049 65.697  1.00 18.18  ? 60  ASP C OD1 1 
ATOM   4187  O OD2 . ASP C  1 54  ? 7.617   -21.503 64.899  1.00 17.66  ? 60  ASP C OD2 1 
ATOM   4188  N N   . LEU C  1 55  ? 6.293   -17.476 67.637  1.00 17.69  ? 61  LEU C N   1 
ATOM   4189  C CA  . LEU C  1 55  ? 5.709   -17.357 68.973  1.00 17.20  ? 61  LEU C CA  1 
ATOM   4190  C C   . LEU C  1 55  ? 5.270   -18.689 69.574  1.00 16.63  ? 61  LEU C C   1 
ATOM   4191  O O   . LEU C  1 55  ? 5.235   -18.838 70.794  1.00 16.97  ? 61  LEU C O   1 
ATOM   4192  C CB  . LEU C  1 55  ? 4.538   -16.371 68.960  1.00 17.41  ? 61  LEU C CB  1 
ATOM   4193  C CG  . LEU C  1 55  ? 4.866   -14.897 68.702  1.00 17.67  ? 61  LEU C CG  1 
ATOM   4194  C CD1 . LEU C  1 55  ? 3.589   -14.107 68.446  1.00 16.74  ? 61  LEU C CD1 1 
ATOM   4195  C CD2 . LEU C  1 55  ? 5.660   -14.294 69.858  1.00 17.81  ? 61  LEU C CD2 1 
ATOM   4196  N N   . GLY C  1 56  ? 4.943   -19.649 68.712  1.00 15.99  ? 62  GLY C N   1 
ATOM   4197  C CA  . GLY C  1 56  ? 4.528   -20.982 69.141  1.00 16.02  ? 62  GLY C CA  1 
ATOM   4198  C C   . GLY C  1 56  ? 3.317   -20.995 70.058  1.00 16.05  ? 62  GLY C C   1 
ATOM   4199  O O   . GLY C  1 56  ? 2.219   -20.588 69.666  1.00 15.34  ? 62  GLY C O   1 
ATOM   4200  N N   . GLN C  1 57  ? 3.532   -21.464 71.286  1.00 16.05  ? 63  GLN C N   1 
ATOM   4201  C CA  . GLN C  1 57  ? 2.469   -21.592 72.288  1.00 15.71  ? 63  GLN C CA  1 
ATOM   4202  C C   . GLN C  1 57  ? 2.050   -20.237 72.856  1.00 14.99  ? 63  GLN C C   1 
ATOM   4203  O O   . GLN C  1 57  ? 1.011   -20.119 73.507  1.00 15.28  ? 63  GLN C O   1 
ATOM   4204  C CB  . GLN C  1 57  ? 2.903   -22.548 73.416  1.00 15.58  ? 63  GLN C CB  1 
ATOM   4205  C CG  . GLN C  1 57  ? 3.923   -21.979 74.429  1.00 15.93  ? 63  GLN C CG  1 
ATOM   4206  C CD  . GLN C  1 57  ? 5.357   -21.886 73.900  1.00 17.71  ? 63  GLN C CD  1 
ATOM   4207  O OE1 . GLN C  1 57  ? 5.699   -22.460 72.861  1.00 17.69  ? 63  GLN C OE1 1 
ATOM   4208  N NE2 . GLN C  1 57  ? 6.204   -21.164 74.629  1.00 17.46  ? 63  GLN C NE2 1 
ATOM   4209  N N   . CYS C  1 58  ? 2.869   -19.224 72.596  1.00 14.58  ? 64  CYS C N   1 
ATOM   4210  C CA  . CYS C  1 58  ? 2.672   -17.888 73.140  1.00 14.72  ? 64  CYS C CA  1 
ATOM   4211  C C   . CYS C  1 58  ? 1.803   -17.013 72.235  1.00 14.77  ? 64  CYS C C   1 
ATOM   4212  O O   . CYS C  1 58  ? 2.041   -16.910 71.027  1.00 14.83  ? 64  CYS C O   1 
ATOM   4213  C CB  . CYS C  1 58  ? 4.028   -17.226 73.378  1.00 14.14  ? 64  CYS C CB  1 
ATOM   4214  S SG  . CYS C  1 58  ? 3.954   -15.488 73.805  1.00 16.71  ? 64  CYS C SG  1 
ATOM   4215  N N   . GLY C  1 59  ? 0.791   -16.391 72.829  1.00 14.17  ? 65  GLY C N   1 
ATOM   4216  C CA  . GLY C  1 59  ? -0.041  -15.434 72.111  1.00 13.70  ? 65  GLY C CA  1 
ATOM   4217  C C   . GLY C  1 59  ? 0.652   -14.086 72.061  1.00 13.43  ? 65  GLY C C   1 
ATOM   4218  O O   . GLY C  1 59  ? 1.272   -13.663 73.043  1.00 13.03  ? 65  GLY C O   1 
ATOM   4219  N N   . LEU C  1 60  ? 0.543   -13.410 70.919  1.00 12.64  ? 66  LEU C N   1 
ATOM   4220  C CA  . LEU C  1 60  ? 1.213   -12.127 70.701  1.00 11.71  ? 66  LEU C CA  1 
ATOM   4221  C C   . LEU C  1 60  ? 0.995   -11.106 71.829  1.00 11.42  ? 66  LEU C C   1 
ATOM   4222  O O   . LEU C  1 60  ? 1.933   -10.411 72.217  1.00 10.88  ? 66  LEU C O   1 
ATOM   4223  C CB  . LEU C  1 60  ? 0.816   -11.540 69.342  1.00 11.38  ? 66  LEU C CB  1 
ATOM   4224  C CG  . LEU C  1 60  ? 1.478   -10.237 68.884  1.00 11.03  ? 66  LEU C CG  1 
ATOM   4225  C CD1 . LEU C  1 60  ? 3.002   -10.304 68.946  1.00 14.20  ? 66  LEU C CD1 1 
ATOM   4226  C CD2 . LEU C  1 60  ? 1.023   -9.899  67.486  1.00 13.02  ? 66  LEU C CD2 1 
ATOM   4227  N N   . LEU C  1 61  ? -0.231  -11.027 72.348  1.00 11.47  ? 67  LEU C N   1 
ATOM   4228  C CA  . LEU C  1 61  ? -0.563  -10.102 73.440  1.00 11.67  ? 67  LEU C CA  1 
ATOM   4229  C C   . LEU C  1 61  ? -0.044  -10.580 74.798  1.00 12.34  ? 67  LEU C C   1 
ATOM   4230  O O   . LEU C  1 61  ? 0.192   -9.772  75.702  1.00 12.52  ? 67  LEU C O   1 
ATOM   4231  C CB  . LEU C  1 61  ? -2.074  -9.851  73.512  1.00 11.60  ? 67  LEU C CB  1 
ATOM   4232  C CG  . LEU C  1 61  ? -2.800  -9.409  72.235  1.00 10.11  ? 67  LEU C CG  1 
ATOM   4233  C CD1 . LEU C  1 61  ? -4.281  -9.206  72.514  1.00 4.41   ? 67  LEU C CD1 1 
ATOM   4234  C CD2 . LEU C  1 61  ? -2.186  -8.142  71.660  1.00 8.37   ? 67  LEU C CD2 1 
ATOM   4235  N N   . GLY C  1 62  ? 0.129   -11.894 74.933  1.00 12.70  ? 68  GLY C N   1 
ATOM   4236  C CA  . GLY C  1 62  ? 0.728   -12.484 76.126  1.00 12.46  ? 68  GLY C CA  1 
ATOM   4237  C C   . GLY C  1 62  ? 2.132   -11.970 76.393  1.00 12.89  ? 68  GLY C C   1 
ATOM   4238  O O   . GLY C  1 62  ? 2.533   -11.841 77.547  1.00 13.80  ? 68  GLY C O   1 
ATOM   4239  N N   . THR C  1 63  ? 2.872   -11.660 75.328  1.00 12.74  ? 69  THR C N   1 
ATOM   4240  C CA  . THR C  1 63  ? 4.233   -11.124 75.449  1.00 13.48  ? 69  THR C CA  1 
ATOM   4241  C C   . THR C  1 63  ? 4.291   -9.857  76.302  1.00 14.04  ? 69  THR C C   1 
ATOM   4242  O O   . THR C  1 63  ? 5.334   -9.541  76.875  1.00 14.32  ? 69  THR C O   1 
ATOM   4243  C CB  . THR C  1 63  ? 4.855   -10.781 74.075  1.00 13.34  ? 69  THR C CB  1 
ATOM   4244  O OG1 . THR C  1 63  ? 4.119   -9.713  73.474  1.00 13.46  ? 69  THR C OG1 1 
ATOM   4245  C CG2 . THR C  1 63  ? 4.854   -11.983 73.145  1.00 13.29  ? 69  THR C CG2 1 
ATOM   4246  N N   . LEU C  1 64  ? 3.172   -9.139  76.372  1.00 14.36  ? 70  LEU C N   1 
ATOM   4247  C CA  . LEU C  1 64  ? 3.098   -7.865  77.088  1.00 14.23  ? 70  LEU C CA  1 
ATOM   4248  C C   . LEU C  1 64  ? 2.886   -8.028  78.590  1.00 14.51  ? 70  LEU C C   1 
ATOM   4249  O O   . LEU C  1 64  ? 3.367   -7.208  79.377  1.00 14.98  ? 70  LEU C O   1 
ATOM   4250  C CB  . LEU C  1 64  ? 1.978   -6.993  76.517  1.00 13.64  ? 70  LEU C CB  1 
ATOM   4251  C CG  . LEU C  1 64  ? 1.946   -6.689  75.017  1.00 15.11  ? 70  LEU C CG  1 
ATOM   4252  C CD1 . LEU C  1 64  ? 0.596   -6.095  74.639  1.00 12.70  ? 70  LEU C CD1 1 
ATOM   4253  C CD2 . LEU C  1 64  ? 3.089   -5.772  74.588  1.00 14.19  ? 70  LEU C CD2 1 
ATOM   4254  N N   . ILE C  1 65  ? 2.161   -9.076  78.979  1.00 14.39  ? 71  ILE C N   1 
ATOM   4255  C CA  . ILE C  1 65  ? 1.774   -9.282  80.378  1.00 14.19  ? 71  ILE C CA  1 
ATOM   4256  C C   . ILE C  1 65  ? 2.495   -10.471 81.016  1.00 15.00  ? 71  ILE C C   1 
ATOM   4257  O O   . ILE C  1 65  ? 2.726   -10.495 82.230  1.00 15.17  ? 71  ILE C O   1 
ATOM   4258  C CB  . ILE C  1 65  ? 0.237   -9.399  80.544  1.00 14.07  ? 71  ILE C CB  1 
ATOM   4259  C CG1 . ILE C  1 65  ? -0.331  -10.492 79.630  1.00 13.72  ? 71  ILE C CG1 1 
ATOM   4260  C CG2 . ILE C  1 65  ? -0.435  -8.048  80.268  1.00 12.68  ? 71  ILE C CG2 1 
ATOM   4261  C CD1 . ILE C  1 65  ? -1.822  -10.710 79.778  1.00 15.03  ? 71  ILE C CD1 1 
ATOM   4262  N N   . GLY C  1 66  ? 2.842   -11.452 80.185  1.00 15.05  ? 72  GLY C N   1 
ATOM   4263  C CA  . GLY C  1 66  ? 3.701   -12.561 80.585  1.00 14.72  ? 72  GLY C CA  1 
ATOM   4264  C C   . GLY C  1 66  ? 3.086   -13.707 81.371  1.00 14.67  ? 72  GLY C C   1 
ATOM   4265  O O   . GLY C  1 66  ? 3.478   -13.940 82.516  1.00 15.03  ? 72  GLY C O   1 
ATOM   4266  N N   . PRO C  1 67  ? 2.127   -14.440 80.765  1.00 14.25  ? 73  PRO C N   1 
ATOM   4267  C CA  . PRO C  1 67  ? 1.736   -15.735 81.326  1.00 13.95  ? 73  PRO C CA  1 
ATOM   4268  C C   . PRO C  1 67  ? 2.850   -16.761 81.068  1.00 14.22  ? 73  PRO C C   1 
ATOM   4269  O O   . PRO C  1 67  ? 3.660   -16.548 80.161  1.00 14.46  ? 73  PRO C O   1 
ATOM   4270  C CB  . PRO C  1 67  ? 0.482   -16.094 80.523  1.00 13.61  ? 73  PRO C CB  1 
ATOM   4271  C CG  . PRO C  1 67  ? 0.642   -15.385 79.239  1.00 13.11  ? 73  PRO C CG  1 
ATOM   4272  C CD  . PRO C  1 67  ? 1.315   -14.093 79.584  1.00 13.89  ? 73  PRO C CD  1 
ATOM   4273  N N   . PRO C  1 68  ? 2.894   -17.866 81.843  1.00 14.07  ? 74  PRO C N   1 
ATOM   4274  C CA  . PRO C  1 68  ? 3.990   -18.845 81.746  1.00 14.02  ? 74  PRO C CA  1 
ATOM   4275  C C   . PRO C  1 68  ? 4.423   -19.203 80.316  1.00 14.28  ? 74  PRO C C   1 
ATOM   4276  O O   . PRO C  1 68  ? 5.619   -19.344 80.062  1.00 14.03  ? 74  PRO C O   1 
ATOM   4277  C CB  . PRO C  1 68  ? 3.413   -20.076 82.446  1.00 14.18  ? 74  PRO C CB  1 
ATOM   4278  C CG  . PRO C  1 68  ? 2.482   -19.517 83.453  1.00 13.63  ? 74  PRO C CG  1 
ATOM   4279  C CD  . PRO C  1 68  ? 1.885   -18.280 82.838  1.00 14.04  ? 74  PRO C CD  1 
ATOM   4280  N N   . GLN C  1 69  ? 3.458   -19.330 79.403  1.00 14.94  ? 75  GLN C N   1 
ATOM   4281  C CA  . GLN C  1 69  ? 3.718   -19.686 77.999  1.00 15.79  ? 75  GLN C CA  1 
ATOM   4282  C C   . GLN C  1 69  ? 4.596   -18.662 77.276  1.00 16.47  ? 75  GLN C C   1 
ATOM   4283  O O   . GLN C  1 69  ? 5.352   -19.012 76.365  1.00 16.83  ? 75  GLN C O   1 
ATOM   4284  C CB  . GLN C  1 69  ? 2.410   -19.849 77.211  1.00 15.79  ? 75  GLN C CB  1 
ATOM   4285  C CG  . GLN C  1 69  ? 1.233   -20.441 77.984  1.00 16.94  ? 75  GLN C CG  1 
ATOM   4286  C CD  . GLN C  1 69  ? 0.382   -19.380 78.669  1.00 16.20  ? 75  GLN C CD  1 
ATOM   4287  O OE1 . GLN C  1 69  ? 0.288   -19.349 79.897  1.00 18.82  ? 75  GLN C OE1 1 
ATOM   4288  N NE2 . GLN C  1 69  ? -0.237  -18.504 77.878  1.00 6.80   ? 75  GLN C NE2 1 
ATOM   4289  N N   . CYS C  1 70  ? 4.482   -17.401 77.684  1.00 16.71  ? 76  CYS C N   1 
ATOM   4290  C CA  . CYS C  1 70  ? 5.205   -16.305 77.043  1.00 16.99  ? 76  CYS C CA  1 
ATOM   4291  C C   . CYS C  1 70  ? 6.443   -15.836 77.821  1.00 17.22  ? 76  CYS C C   1 
ATOM   4292  O O   . CYS C  1 70  ? 7.021   -14.795 77.492  1.00 17.48  ? 76  CYS C O   1 
ATOM   4293  C CB  . CYS C  1 70  ? 4.258   -15.128 76.781  1.00 16.71  ? 76  CYS C CB  1 
ATOM   4294  S SG  . CYS C  1 70  ? 2.959   -15.470 75.577  1.00 16.52  ? 76  CYS C SG  1 
ATOM   4295  N N   . ASP C  1 71  ? 6.851   -16.602 78.835  1.00 17.26  ? 77  ASP C N   1 
ATOM   4296  C CA  . ASP C  1 71  ? 8.068   -16.300 79.600  1.00 17.74  ? 77  ASP C CA  1 
ATOM   4297  C C   . ASP C  1 71  ? 9.276   -16.158 78.679  1.00 18.50  ? 77  ASP C C   1 
ATOM   4298  O O   . ASP C  1 71  ? 10.178  -15.358 78.935  1.00 18.35  ? 77  ASP C O   1 
ATOM   4299  C CB  . ASP C  1 71  ? 8.340   -17.384 80.650  1.00 17.52  ? 77  ASP C CB  1 
ATOM   4300  C CG  . ASP C  1 71  ? 7.571   -17.162 81.945  1.00 17.54  ? 77  ASP C CG  1 
ATOM   4301  O OD1 . ASP C  1 71  ? 7.585   -18.068 82.805  1.00 17.77  ? 77  ASP C OD1 1 
ATOM   4302  O OD2 . ASP C  1 71  ? 6.961   -16.086 82.113  1.00 16.79  ? 77  ASP C OD2 1 
ATOM   4303  N N   . GLN C  1 72  ? 9.261   -16.934 77.598  1.00 19.39  ? 78  GLN C N   1 
ATOM   4304  C CA  . GLN C  1 72  ? 10.328  -16.959 76.607  1.00 20.63  ? 78  GLN C CA  1 
ATOM   4305  C C   . GLN C  1 72  ? 10.282  -15.767 75.641  1.00 20.63  ? 78  GLN C C   1 
ATOM   4306  O O   . GLN C  1 72  ? 11.195  -15.596 74.831  1.00 20.68  ? 78  GLN C O   1 
ATOM   4307  C CB  . GLN C  1 72  ? 10.255  -18.263 75.796  1.00 21.38  ? 78  GLN C CB  1 
ATOM   4308  C CG  . GLN C  1 72  ? 10.099  -19.542 76.623  1.00 24.59  ? 78  GLN C CG  1 
ATOM   4309  C CD  . GLN C  1 72  ? 11.415  -20.053 77.194  1.00 28.82  ? 78  GLN C CD  1 
ATOM   4310  O OE1 . GLN C  1 72  ? 12.427  -20.127 76.492  1.00 28.09  ? 78  GLN C OE1 1 
ATOM   4311  N NE2 . GLN C  1 72  ? 11.399  -20.424 78.472  1.00 29.78  ? 78  GLN C NE2 1 
ATOM   4312  N N   . PHE C  1 73  ? 9.232   -14.949 75.719  1.00 20.06  ? 79  PHE C N   1 
ATOM   4313  C CA  . PHE C  1 73  ? 9.013   -13.894 74.724  1.00 19.57  ? 79  PHE C CA  1 
ATOM   4314  C C   . PHE C  1 73  ? 8.781   -12.489 75.295  1.00 19.23  ? 79  PHE C C   1 
ATOM   4315  O O   . PHE C  1 73  ? 8.345   -11.586 74.570  1.00 19.50  ? 79  PHE C O   1 
ATOM   4316  C CB  . PHE C  1 73  ? 7.857   -14.282 73.788  1.00 19.89  ? 79  PHE C CB  1 
ATOM   4317  C CG  . PHE C  1 73  ? 8.102   -15.544 73.002  1.00 18.59  ? 79  PHE C CG  1 
ATOM   4318  C CD1 . PHE C  1 73  ? 7.609   -16.764 73.452  1.00 17.80  ? 79  PHE C CD1 1 
ATOM   4319  C CD2 . PHE C  1 73  ? 8.824   -15.509 71.813  1.00 17.85  ? 79  PHE C CD2 1 
ATOM   4320  C CE1 . PHE C  1 73  ? 7.830   -17.935 72.728  1.00 19.94  ? 79  PHE C CE1 1 
ATOM   4321  C CE2 . PHE C  1 73  ? 9.056   -16.676 71.081  1.00 18.01  ? 79  PHE C CE2 1 
ATOM   4322  C CZ  . PHE C  1 73  ? 8.556   -17.890 71.539  1.00 19.04  ? 79  PHE C CZ  1 
ATOM   4323  N N   . LEU C  1 74  ? 9.086   -12.300 76.579  1.00 18.24  ? 80  LEU C N   1 
ATOM   4324  C CA  . LEU C  1 74  ? 8.868   -11.017 77.265  1.00 17.51  ? 80  LEU C CA  1 
ATOM   4325  C C   . LEU C  1 74  ? 9.545   -9.830  76.572  1.00 17.11  ? 80  LEU C C   1 
ATOM   4326  O O   . LEU C  1 74  ? 8.986   -8.734  76.512  1.00 16.99  ? 80  LEU C O   1 
ATOM   4327  C CB  . LEU C  1 74  ? 9.319   -11.101 78.727  1.00 17.55  ? 80  LEU C CB  1 
ATOM   4328  C CG  . LEU C  1 74  ? 8.635   -12.136 79.621  1.00 16.56  ? 80  LEU C CG  1 
ATOM   4329  C CD1 . LEU C  1 74  ? 9.293   -12.153 80.987  1.00 16.15  ? 80  LEU C CD1 1 
ATOM   4330  C CD2 . LEU C  1 74  ? 7.145   -11.857 79.743  1.00 16.68  ? 80  LEU C CD2 1 
ATOM   4331  N N   . GLU C  1 75  ? 10.755  -10.058 76.071  1.00 16.72  ? 81  GLU C N   1 
ATOM   4332  C CA  . GLU C  1 75  ? 11.446  -9.106  75.214  1.00 16.35  ? 81  GLU C CA  1 
ATOM   4333  C C   . GLU C  1 75  ? 11.889  -9.855  73.961  1.00 16.60  ? 81  GLU C C   1 
ATOM   4334  O O   . GLU C  1 75  ? 12.794  -10.695 74.016  1.00 17.92  ? 81  GLU C O   1 
ATOM   4335  C CB  . GLU C  1 75  ? 12.667  -8.506  75.925  1.00 16.35  ? 81  GLU C CB  1 
ATOM   4336  C CG  . GLU C  1 75  ? 12.359  -7.599  77.111  1.00 15.66  ? 81  GLU C CG  1 
ATOM   4337  C CD  . GLU C  1 75  ? 13.617  -7.089  77.794  1.00 15.25  ? 81  GLU C CD  1 
ATOM   4338  O OE1 . GLU C  1 75  ? 14.014  -5.937  77.519  1.00 12.95  ? 81  GLU C OE1 1 
ATOM   4339  O OE2 . GLU C  1 75  ? 14.213  -7.842  78.598  1.00 15.67  ? 81  GLU C OE2 1 
ATOM   4340  N N   . PHE C  1 76  ? 11.240  -9.584  72.835  1.00 15.46  ? 82  PHE C N   1 
ATOM   4341  C CA  . PHE C  1 76  ? 11.672  -10.179 71.574  1.00 14.31  ? 82  PHE C CA  1 
ATOM   4342  C C   . PHE C  1 76  ? 12.100  -9.102  70.585  1.00 14.23  ? 82  PHE C C   1 
ATOM   4343  O O   . PHE C  1 76  ? 11.687  -7.950  70.695  1.00 14.56  ? 82  PHE C O   1 
ATOM   4344  C CB  . PHE C  1 76  ? 10.612  -11.132 70.989  1.00 13.41  ? 82  PHE C CB  1 
ATOM   4345  C CG  . PHE C  1 76  ? 9.377   -10.448 70.465  1.00 11.83  ? 82  PHE C CG  1 
ATOM   4346  C CD1 . PHE C  1 76  ? 9.239   -10.182 69.109  1.00 12.00  ? 82  PHE C CD1 1 
ATOM   4347  C CD2 . PHE C  1 76  ? 8.340   -10.092 71.324  1.00 10.79  ? 82  PHE C CD2 1 
ATOM   4348  C CE1 . PHE C  1 76  ? 8.094   -9.558  68.615  1.00 12.41  ? 82  PHE C CE1 1 
ATOM   4349  C CE2 . PHE C  1 76  ? 7.194   -9.466  70.843  1.00 9.03   ? 82  PHE C CE2 1 
ATOM   4350  C CZ  . PHE C  1 76  ? 7.072   -9.196  69.484  1.00 10.73  ? 82  PHE C CZ  1 
ATOM   4351  N N   . SER C  1 77  ? 12.964  -9.480  69.649  1.00 14.22  ? 83  SER C N   1 
ATOM   4352  C CA  . SER C  1 77  ? 13.399  -8.581  68.591  1.00 14.68  ? 83  SER C CA  1 
ATOM   4353  C C   . SER C  1 77  ? 13.358  -9.323  67.265  1.00 15.06  ? 83  SER C C   1 
ATOM   4354  O O   . SER C  1 77  ? 14.146  -10.246 67.033  1.00 15.43  ? 83  SER C O   1 
ATOM   4355  C CB  . SER C  1 77  ? 14.809  -8.057  68.867  1.00 14.80  ? 83  SER C CB  1 
ATOM   4356  O OG  . SER C  1 77  ? 15.220  -7.151  67.859  1.00 14.85  ? 83  SER C OG  1 
ATOM   4357  N N   . SER C  1 78  ? 12.424  -8.933  66.404  1.00 14.85  ? 84  SER C N   1 
ATOM   4358  C CA  . SER C  1 78  ? 12.298  -9.568  65.104  1.00 15.36  ? 84  SER C CA  1 
ATOM   4359  C C   . SER C  1 78  ? 11.806  -8.597  64.040  1.00 15.43  ? 84  SER C C   1 
ATOM   4360  O O   . SER C  1 78  ? 11.302  -7.518  64.357  1.00 15.72  ? 84  SER C O   1 
ATOM   4361  C CB  . SER C  1 78  ? 11.386  -10.805 65.187  1.00 15.23  ? 84  SER C CB  1 
ATOM   4362  O OG  . SER C  1 78  ? 10.055  -10.518 64.807  1.00 15.85  ? 84  SER C OG  1 
ATOM   4363  N N   . ASP C  1 79  ? 11.975  -8.987  62.778  1.00 15.41  ? 85  ASP C N   1 
ATOM   4364  C CA  . ASP C  1 79  ? 11.391  -8.262  61.655  1.00 15.55  ? 85  ASP C CA  1 
ATOM   4365  C C   . ASP C  1 79  ? 10.274  -9.070  60.975  1.00 15.41  ? 85  ASP C C   1 
ATOM   4366  O O   . ASP C  1 79  ? 9.623   -8.585  60.042  1.00 15.42  ? 85  ASP C O   1 
ATOM   4367  C CB  . ASP C  1 79  ? 12.466  -7.808  60.654  1.00 15.00  ? 85  ASP C CB  1 
ATOM   4368  C CG  . ASP C  1 79  ? 13.253  -8.959  60.057  1.00 17.56  ? 85  ASP C CG  1 
ATOM   4369  O OD1 . ASP C  1 79  ? 14.197  -8.672  59.295  1.00 22.31  ? 85  ASP C OD1 1 
ATOM   4370  O OD2 . ASP C  1 79  ? 12.948  -10.141 60.335  1.00 20.39  ? 85  ASP C OD2 1 
ATOM   4371  N N   . LEU C  1 80  ? 10.054  -10.291 61.467  1.00 14.60  ? 86  LEU C N   1 
ATOM   4372  C CA  . LEU C  1 80  ? 9.014   -11.178 60.946  1.00 13.98  ? 86  LEU C CA  1 
ATOM   4373  C C   . LEU C  1 80  ? 8.378   -11.977 62.086  1.00 14.07  ? 86  LEU C C   1 
ATOM   4374  O O   . LEU C  1 80  ? 8.920   -12.988 62.534  1.00 14.28  ? 86  LEU C O   1 
ATOM   4375  C CB  . LEU C  1 80  ? 9.599   -12.111 59.880  1.00 13.79  ? 86  LEU C CB  1 
ATOM   4376  C CG  . LEU C  1 80  ? 8.680   -13.006 59.050  1.00 12.53  ? 86  LEU C CG  1 
ATOM   4377  C CD1 . LEU C  1 80  ? 7.953   -12.209 57.986  1.00 15.25  ? 86  LEU C CD1 1 
ATOM   4378  C CD2 . LEU C  1 80  ? 9.498   -14.100 58.404  1.00 12.35  ? 86  LEU C CD2 1 
ATOM   4379  N N   . ILE C  1 81  ? 7.230   -11.504 62.562  1.00 14.16  ? 87  ILE C N   1 
ATOM   4380  C CA  . ILE C  1 81  ? 6.544   -12.132 63.685  1.00 14.45  ? 87  ILE C CA  1 
ATOM   4381  C C   . ILE C  1 81  ? 5.544   -13.173 63.184  1.00 14.89  ? 87  ILE C C   1 
ATOM   4382  O O   . ILE C  1 81  ? 4.558   -12.833 62.518  1.00 15.64  ? 87  ILE C O   1 
ATOM   4383  C CB  . ILE C  1 81  ? 5.836   -11.084 64.577  1.00 14.46  ? 87  ILE C CB  1 
ATOM   4384  C CG1 . ILE C  1 81  ? 6.849   -10.058 65.095  1.00 14.35  ? 87  ILE C CG1 1 
ATOM   4385  C CG2 . ILE C  1 81  ? 5.114   -11.764 65.742  1.00 14.24  ? 87  ILE C CG2 1 
ATOM   4386  C CD1 . ILE C  1 81  ? 6.236   -8.765  65.589  1.00 16.44  ? 87  ILE C CD1 1 
ATOM   4387  N N   . ILE C  1 82  ? 5.807   -14.440 63.503  1.00 13.61  ? 88  ILE C N   1 
ATOM   4388  C CA  . ILE C  1 82  ? 4.923   -15.527 63.092  1.00 12.86  ? 88  ILE C CA  1 
ATOM   4389  C C   . ILE C  1 82  ? 4.015   -15.966 64.242  1.00 12.90  ? 88  ILE C C   1 
ATOM   4390  O O   . ILE C  1 82  ? 4.483   -16.477 65.266  1.00 13.13  ? 88  ILE C O   1 
ATOM   4391  C CB  . ILE C  1 82  ? 5.700   -16.739 62.506  1.00 12.54  ? 88  ILE C CB  1 
ATOM   4392  C CG1 . ILE C  1 82  ? 6.506   -16.331 61.270  1.00 11.22  ? 88  ILE C CG1 1 
ATOM   4393  C CG2 . ILE C  1 82  ? 4.749   -17.866 62.139  1.00 11.25  ? 88  ILE C CG2 1 
ATOM   4394  C CD1 . ILE C  1 82  ? 7.966   -16.031 61.550  1.00 11.86  ? 88  ILE C CD1 1 
ATOM   4395  N N   . GLU C  1 83  ? 2.716   -15.746 64.058  1.00 12.96  ? 89  GLU C N   1 
ATOM   4396  C CA  . GLU C  1 83  ? 1.690   -16.186 65.004  1.00 13.25  ? 89  GLU C CA  1 
ATOM   4397  C C   . GLU C  1 83  ? 1.262   -17.620 64.700  1.00 13.71  ? 89  GLU C C   1 
ATOM   4398  O O   . GLU C  1 83  ? 1.119   -17.999 63.535  1.00 13.55  ? 89  GLU C O   1 
ATOM   4399  C CB  . GLU C  1 83  ? 0.469   -15.263 64.946  1.00 12.69  ? 89  GLU C CB  1 
ATOM   4400  C CG  . GLU C  1 83  ? 0.624   -13.935 65.678  1.00 12.08  ? 89  GLU C CG  1 
ATOM   4401  C CD  . GLU C  1 83  ? -0.665  -13.127 65.694  1.00 13.47  ? 89  GLU C CD  1 
ATOM   4402  O OE1 . GLU C  1 83  ? -1.188  -12.864 66.796  1.00 13.16  ? 89  GLU C OE1 1 
ATOM   4403  O OE2 . GLU C  1 83  ? -1.165  -12.762 64.608  1.00 14.71  ? 89  GLU C OE2 1 
ATOM   4404  N N   . ARG C  1 84  ? 1.060   -18.413 65.748  1.00 14.69  ? 90  ARG C N   1 
ATOM   4405  C CA  . ARG C  1 84  ? 0.625   -19.801 65.589  1.00 15.92  ? 90  ARG C CA  1 
ATOM   4406  C C   . ARG C  1 84  ? -0.764  -20.037 66.179  1.00 17.02  ? 90  ARG C C   1 
ATOM   4407  O O   . ARG C  1 84  ? -1.199  -19.310 67.073  1.00 17.98  ? 90  ARG C O   1 
ATOM   4408  C CB  . ARG C  1 84  ? 1.638   -20.766 66.215  1.00 15.86  ? 90  ARG C CB  1 
ATOM   4409  C CG  . ARG C  1 84  ? 3.054   -20.647 65.683  1.00 14.11  ? 90  ARG C CG  1 
ATOM   4410  C CD  . ARG C  1 84  ? 3.172   -21.138 64.253  1.00 15.22  ? 90  ARG C CD  1 
ATOM   4411  N NE  . ARG C  1 84  ? 4.564   -21.184 63.811  1.00 15.49  ? 90  ARG C NE  1 
ATOM   4412  C CZ  . ARG C  1 84  ? 4.956   -21.454 62.570  1.00 15.47  ? 90  ARG C CZ  1 
ATOM   4413  N NH1 . ARG C  1 84  ? 4.064   -21.700 61.619  1.00 13.88  ? 90  ARG C NH1 1 
ATOM   4414  N NH2 . ARG C  1 84  ? 6.248   -21.471 62.276  1.00 17.12  ? 90  ARG C NH2 1 
ATOM   4415  N N   . ARG C  1 85  ? -1.437  -21.068 65.670  1.00 17.85  ? 91  ARG C N   1 
ATOM   4416  C CA  . ARG C  1 85  ? -2.792  -21.454 66.081  1.00 19.08  ? 91  ARG C CA  1 
ATOM   4417  C C   . ARG C  1 85  ? -2.941  -21.708 67.590  1.00 19.10  ? 91  ARG C C   1 
ATOM   4418  O O   . ARG C  1 85  ? -3.969  -21.365 68.183  1.00 18.96  ? 91  ARG C O   1 
ATOM   4419  C CB  . ARG C  1 85  ? -3.204  -22.709 65.305  1.00 19.63  ? 91  ARG C CB  1 
ATOM   4420  C CG  . ARG C  1 85  ? -4.695  -22.881 65.056  1.00 25.14  ? 91  ARG C CG  1 
ATOM   4421  C CD  . ARG C  1 85  ? -4.903  -23.760 63.824  1.00 33.72  ? 91  ARG C CD  1 
ATOM   4422  N NE  . ARG C  1 85  ? -6.310  -24.022 63.523  1.00 41.05  ? 91  ARG C NE  1 
ATOM   4423  C CZ  . ARG C  1 85  ? -6.863  -25.234 63.483  1.00 43.78  ? 91  ARG C CZ  1 
ATOM   4424  N NH1 . ARG C  1 85  ? -6.133  -26.318 63.723  1.00 44.69  ? 91  ARG C NH1 1 
ATOM   4425  N NH2 . ARG C  1 85  ? -8.152  -25.365 63.194  1.00 44.47  ? 91  ARG C NH2 1 
ATOM   4426  N N   . GLU C  1 86  ? -1.913  -22.297 68.201  1.00 18.92  ? 92  GLU C N   1 
ATOM   4427  C CA  . GLU C  1 86  ? -1.977  -22.726 69.602  1.00 19.19  ? 92  GLU C CA  1 
ATOM   4428  C C   . GLU C  1 86  ? -1.593  -21.648 70.618  1.00 19.03  ? 92  GLU C C   1 
ATOM   4429  O O   . GLU C  1 86  ? -1.539  -21.907 71.822  1.00 19.24  ? 92  GLU C O   1 
ATOM   4430  C CB  . GLU C  1 86  ? -1.145  -24.003 69.822  1.00 19.46  ? 92  GLU C CB  1 
ATOM   4431  C CG  . GLU C  1 86  ? 0.369   -23.841 69.661  1.00 21.23  ? 92  GLU C CG  1 
ATOM   4432  C CD  . GLU C  1 86  ? 0.860   -24.067 68.235  1.00 24.88  ? 92  GLU C CD  1 
ATOM   4433  O OE1 . GLU C  1 86  ? 0.051   -24.463 67.360  1.00 24.13  ? 92  GLU C OE1 1 
ATOM   4434  O OE2 . GLU C  1 86  ? 2.069   -23.848 67.996  1.00 23.08  ? 92  GLU C OE2 1 
ATOM   4435  N N   . GLY C  1 87  ? -1.341  -20.439 70.128  1.00 19.00  ? 93  GLY C N   1 
ATOM   4436  C CA  . GLY C  1 87  ? -0.976  -19.318 70.986  1.00 19.00  ? 93  GLY C CA  1 
ATOM   4437  C C   . GLY C  1 87  ? -2.141  -18.799 71.810  1.00 19.15  ? 93  GLY C C   1 
ATOM   4438  O O   . GLY C  1 87  ? -3.259  -18.649 71.306  1.00 19.06  ? 93  GLY C O   1 
ATOM   4439  N N   . THR C  1 88  ? -1.879  -18.546 73.089  1.00 18.30  ? 94  THR C N   1 
ATOM   4440  C CA  . THR C  1 88  ? -2.861  -17.944 73.977  1.00 17.52  ? 94  THR C CA  1 
ATOM   4441  C C   . THR C  1 88  ? -2.225  -16.771 74.705  1.00 18.03  ? 94  THR C C   1 
ATOM   4442  O O   . THR C  1 88  ? -1.039  -16.803 75.045  1.00 17.54  ? 94  THR C O   1 
ATOM   4443  C CB  . THR C  1 88  ? -3.438  -18.950 74.997  1.00 17.53  ? 94  THR C CB  1 
ATOM   4444  O OG1 . THR C  1 88  ? -2.371  -19.593 75.709  1.00 17.83  ? 94  THR C OG1 1 
ATOM   4445  C CG2 . THR C  1 88  ? -4.296  -19.998 74.294  1.00 16.71  ? 94  THR C CG2 1 
ATOM   4446  N N   . ASP C  1 89  ? -3.026  -15.735 74.931  1.00 18.61  ? 95  ASP C N   1 
ATOM   4447  C CA  . ASP C  1 89  ? -2.543  -14.497 75.520  1.00 19.02  ? 95  ASP C CA  1 
ATOM   4448  C C   . ASP C  1 89  ? -2.644  -14.535 77.042  1.00 19.59  ? 95  ASP C C   1 
ATOM   4449  O O   . ASP C  1 89  ? -1.891  -13.848 77.738  1.00 19.08  ? 95  ASP C O   1 
ATOM   4450  C CB  . ASP C  1 89  ? -3.335  -13.311 74.956  1.00 19.12  ? 95  ASP C CB  1 
ATOM   4451  C CG  . ASP C  1 89  ? -3.291  -13.245 73.433  1.00 19.06  ? 95  ASP C CG  1 
ATOM   4452  O OD1 . ASP C  1 89  ? -2.180  -13.175 72.866  1.00 15.09  ? 95  ASP C OD1 1 
ATOM   4453  O OD2 . ASP C  1 89  ? -4.370  -13.253 72.802  1.00 19.34  ? 95  ASP C OD2 1 
ATOM   4454  N N   . ILE C  1 90  ? -3.562  -15.360 77.544  1.00 20.36  ? 96  ILE C N   1 
ATOM   4455  C CA  . ILE C  1 90  ? -3.913  -15.387 78.966  1.00 21.25  ? 96  ILE C CA  1 
ATOM   4456  C C   . ILE C  1 90  ? -3.657  -16.740 79.634  1.00 22.33  ? 96  ILE C C   1 
ATOM   4457  O O   . ILE C  1 90  ? -3.465  -17.753 78.958  1.00 22.75  ? 96  ILE C O   1 
ATOM   4458  C CB  . ILE C  1 90  ? -5.405  -15.029 79.177  1.00 20.78  ? 96  ILE C CB  1 
ATOM   4459  C CG1 . ILE C  1 90  ? -6.302  -15.986 78.381  1.00 20.41  ? 96  ILE C CG1 1 
ATOM   4460  C CG2 . ILE C  1 90  ? -5.664  -13.583 78.783  1.00 19.93  ? 96  ILE C CG2 1 
ATOM   4461  C CD1 . ILE C  1 90  ? -7.574  -16.392 79.096  1.00 21.86  ? 96  ILE C CD1 1 
ATOM   4462  N N   . CYS C  1 91  ? -3.649  -16.736 80.966  1.00 23.26  ? 97  CYS C N   1 
ATOM   4463  C CA  . CYS C  1 91  ? -3.714  -17.963 81.760  1.00 24.35  ? 97  CYS C CA  1 
ATOM   4464  C C   . CYS C  1 91  ? -4.982  -17.934 82.618  1.00 25.22  ? 97  CYS C C   1 
ATOM   4465  O O   . CYS C  1 91  ? -5.841  -18.814 82.503  1.00 25.53  ? 97  CYS C O   1 
ATOM   4466  C CB  . CYS C  1 91  ? -2.451  -18.160 82.615  1.00 24.27  ? 97  CYS C CB  1 
ATOM   4467  S SG  . CYS C  1 91  ? -1.815  -16.685 83.476  1.00 24.93  ? 97  CYS C SG  1 
ATOM   4468  N N   . TYR C  1 92  ? -5.091  -16.911 83.465  1.00 25.93  ? 98  TYR C N   1 
ATOM   4469  C CA  . TYR C  1 92  ? -6.305  -16.631 84.220  1.00 26.16  ? 98  TYR C CA  1 
ATOM   4470  C C   . TYR C  1 92  ? -7.336  -16.088 83.232  1.00 26.75  ? 98  TYR C C   1 
ATOM   4471  O O   . TYR C  1 92  ? -6.981  -15.281 82.368  1.00 26.98  ? 98  TYR C O   1 
ATOM   4472  C CB  . TYR C  1 92  ? -6.003  -15.600 85.313  1.00 26.04  ? 98  TYR C CB  1 
ATOM   4473  C CG  . TYR C  1 92  ? -7.075  -15.433 86.375  1.00 25.86  ? 98  TYR C CG  1 
ATOM   4474  C CD1 . TYR C  1 92  ? -7.066  -16.210 87.534  1.00 26.10  ? 98  TYR C CD1 1 
ATOM   4475  C CD2 . TYR C  1 92  ? -8.084  -14.483 86.231  1.00 25.20  ? 98  TYR C CD2 1 
ATOM   4476  C CE1 . TYR C  1 92  ? -8.045  -16.051 88.517  1.00 25.07  ? 98  TYR C CE1 1 
ATOM   4477  C CE2 . TYR C  1 92  ? -9.063  -14.317 87.205  1.00 24.97  ? 98  TYR C CE2 1 
ATOM   4478  C CZ  . TYR C  1 92  ? -9.040  -15.103 88.344  1.00 25.70  ? 98  TYR C CZ  1 
ATOM   4479  O OH  . TYR C  1 92  ? -10.012 -14.931 89.305  1.00 23.53  ? 98  TYR C OH  1 
ATOM   4480  N N   . PRO C  1 93  ? -8.609  -16.532 83.341  1.00 27.22  ? 99  PRO C N   1 
ATOM   4481  C CA  . PRO C  1 93  ? -9.647  -16.104 82.395  1.00 27.19  ? 99  PRO C CA  1 
ATOM   4482  C C   . PRO C  1 93  ? -9.714  -14.588 82.233  1.00 27.69  ? 99  PRO C C   1 
ATOM   4483  O O   . PRO C  1 93  ? -9.494  -13.846 83.192  1.00 27.33  ? 99  PRO C O   1 
ATOM   4484  C CB  . PRO C  1 93  ? -10.937 -16.626 83.031  1.00 26.89  ? 99  PRO C CB  1 
ATOM   4485  C CG  . PRO C  1 93  ? -10.507 -17.818 83.797  1.00 27.29  ? 99  PRO C CG  1 
ATOM   4486  C CD  . PRO C  1 93  ? -9.148  -17.472 84.344  1.00 27.16  ? 99  PRO C CD  1 
ATOM   4487  N N   . GLY C  1 94  ? -10.004 -14.145 81.014  1.00 28.50  ? 100 GLY C N   1 
ATOM   4488  C CA  . GLY C  1 94  ? -10.089 -12.722 80.700  1.00 29.04  ? 100 GLY C CA  1 
ATOM   4489  C C   . GLY C  1 94  ? -9.747  -12.449 79.251  1.00 29.47  ? 100 GLY C C   1 
ATOM   4490  O O   . GLY C  1 94  ? -9.475  -13.377 78.487  1.00 30.07  ? 100 GLY C O   1 
ATOM   4491  N N   . ARG C  1 95  ? -9.768  -11.175 78.870  1.00 29.70  ? 101 ARG C N   1 
ATOM   4492  C CA  . ARG C  1 95  ? -9.425  -10.772 77.508  1.00 30.16  ? 101 ARG C CA  1 
ATOM   4493  C C   . ARG C  1 95  ? -9.089  -9.286  77.421  1.00 29.54  ? 101 ARG C C   1 
ATOM   4494  O O   . ARG C  1 95  ? -9.538  -8.488  78.247  1.00 30.09  ? 101 ARG C O   1 
ATOM   4495  C CB  . ARG C  1 95  ? -10.550 -11.138 76.525  1.00 30.53  ? 101 ARG C CB  1 
ATOM   4496  C CG  . ARG C  1 95  ? -11.815 -10.306 76.669  1.00 33.06  ? 101 ARG C CG  1 
ATOM   4497  C CD  . ARG C  1 95  ? -13.038 -11.029 76.125  1.00 36.78  ? 101 ARG C CD  1 
ATOM   4498  N NE  . ARG C  1 95  ? -14.052 -10.087 75.650  1.00 41.47  ? 101 ARG C NE  1 
ATOM   4499  C CZ  . ARG C  1 95  ? -14.877 -9.389  76.433  1.00 42.95  ? 101 ARG C CZ  1 
ATOM   4500  N NH1 . ARG C  1 95  ? -14.829 -9.505  77.757  1.00 42.47  ? 101 ARG C NH1 1 
ATOM   4501  N NH2 . ARG C  1 95  ? -15.755 -8.559  75.884  1.00 43.70  ? 101 ARG C NH2 1 
ATOM   4502  N N   . PHE C  1 96  ? -8.291  -8.937  76.415  1.00 28.71  ? 102 PHE C N   1 
ATOM   4503  C CA  . PHE C  1 96  ? -7.923  -7.555  76.132  1.00 27.81  ? 102 PHE C CA  1 
ATOM   4504  C C   . PHE C  1 96  ? -9.072  -6.832  75.443  1.00 27.65  ? 102 PHE C C   1 
ATOM   4505  O O   . PHE C  1 96  ? -9.696  -7.374  74.524  1.00 27.64  ? 102 PHE C O   1 
ATOM   4506  C CB  . PHE C  1 96  ? -6.702  -7.509  75.207  1.00 27.80  ? 102 PHE C CB  1 
ATOM   4507  C CG  . PHE C  1 96  ? -5.407  -7.887  75.869  1.00 26.96  ? 102 PHE C CG  1 
ATOM   4508  C CD1 . PHE C  1 96  ? -5.092  -9.222  76.113  1.00 25.73  ? 102 PHE C CD1 1 
ATOM   4509  C CD2 . PHE C  1 96  ? -4.485  -6.906  76.220  1.00 25.09  ? 102 PHE C CD2 1 
ATOM   4510  C CE1 . PHE C  1 96  ? -3.887  -9.571  76.716  1.00 26.60  ? 102 PHE C CE1 1 
ATOM   4511  C CE2 . PHE C  1 96  ? -3.278  -7.245  76.821  1.00 26.58  ? 102 PHE C CE2 1 
ATOM   4512  C CZ  . PHE C  1 96  ? -2.977  -8.580  77.068  1.00 26.55  ? 102 PHE C CZ  1 
ATOM   4513  N N   . THR C  1 97  ? -9.351  -5.607  75.880  1.00 27.11  ? 103 THR C N   1 
ATOM   4514  C CA  . THR C  1 97  ? -10.266 -4.746  75.139  1.00 26.54  ? 103 THR C CA  1 
ATOM   4515  C C   . THR C  1 97  ? -9.523  -4.199  73.927  1.00 26.28  ? 103 THR C C   1 
ATOM   4516  O O   . THR C  1 97  ? -8.346  -3.829  74.027  1.00 25.76  ? 103 THR C O   1 
ATOM   4517  C CB  . THR C  1 97  ? -10.826 -3.592  75.996  1.00 26.55  ? 103 THR C CB  1 
ATOM   4518  O OG1 . THR C  1 97  ? -9.752  -2.910  76.652  1.00 26.67  ? 103 THR C OG1 1 
ATOM   4519  C CG2 . THR C  1 97  ? -11.805 -4.124  77.036  1.00 27.02  ? 103 THR C CG2 1 
ATOM   4520  N N   . ASN C  1 98  ? -10.214 -4.172  72.786  1.00 26.03  ? 104 ASN C N   1 
ATOM   4521  C CA  . ASN C  1 98  ? -9.626  -3.782  71.497  1.00 25.78  ? 104 ASN C CA  1 
ATOM   4522  C C   . ASN C  1 98  ? -8.453  -4.683  71.105  1.00 24.81  ? 104 ASN C C   1 
ATOM   4523  O O   . ASN C  1 98  ? -7.465  -4.222  70.525  1.00 24.44  ? 104 ASN C O   1 
ATOM   4524  C CB  . ASN C  1 98  ? -9.207  -2.302  71.502  1.00 26.33  ? 104 ASN C CB  1 
ATOM   4525  C CG  . ASN C  1 98  ? -10.379 -1.353  71.285  1.00 28.79  ? 104 ASN C CG  1 
ATOM   4526  O OD1 . ASN C  1 98  ? -10.363 -0.541  70.358  1.00 31.82  ? 104 ASN C OD1 1 
ATOM   4527  N ND2 . ASN C  1 98  ? -11.398 -1.450  72.137  1.00 29.45  ? 104 ASN C ND2 1 
ATOM   4528  N N   . GLU C  1 99  ? -8.587  -5.974  71.413  1.00 23.75  ? 105 GLU C N   1 
ATOM   4529  C CA  . GLU C  1 99  ? -7.487  -6.935  71.296  1.00 22.21  ? 105 GLU C CA  1 
ATOM   4530  C C   . GLU C  1 99  ? -6.816  -6.953  69.922  1.00 21.12  ? 105 GLU C C   1 
ATOM   4531  O O   . GLU C  1 99  ? -5.591  -7.052  69.831  1.00 20.54  ? 105 GLU C O   1 
ATOM   4532  C CB  . GLU C  1 99  ? -7.919  -8.347  71.738  1.00 22.52  ? 105 GLU C CB  1 
ATOM   4533  C CG  . GLU C  1 99  ? -9.085  -8.978  70.972  1.00 22.41  ? 105 GLU C CG  1 
ATOM   4534  C CD  . GLU C  1 99  ? -9.500  -10.331 71.550  1.00 23.09  ? 105 GLU C CD  1 
ATOM   4535  O OE1 . GLU C  1 99  ? -9.038  -11.373 71.034  1.00 21.19  ? 105 GLU C OE1 1 
ATOM   4536  O OE2 . GLU C  1 99  ? -10.283 -10.352 72.525  1.00 21.31  ? 105 GLU C OE2 1 
ATOM   4537  N N   . GLU C  1 100 ? -7.612  -6.828  68.863  1.00 20.09  ? 106 GLU C N   1 
ATOM   4538  C CA  . GLU C  1 100 ? -7.070  -6.888  67.510  1.00 19.07  ? 106 GLU C CA  1 
ATOM   4539  C C   . GLU C  1 100 ? -6.291  -5.632  67.125  1.00 18.86  ? 106 GLU C C   1 
ATOM   4540  O O   . GLU C  1 100 ? -5.268  -5.720  66.433  1.00 19.32  ? 106 GLU C O   1 
ATOM   4541  C CB  . GLU C  1 100 ? -8.158  -7.199  66.485  1.00 18.39  ? 106 GLU C CB  1 
ATOM   4542  C CG  . GLU C  1 100 ? -7.621  -7.886  65.240  1.00 17.62  ? 106 GLU C CG  1 
ATOM   4543  C CD  . GLU C  1 100 ? -6.892  -9.188  65.545  1.00 18.14  ? 106 GLU C CD  1 
ATOM   4544  O OE1 . GLU C  1 100 ? -7.398  -9.996  66.356  1.00 19.00  ? 106 GLU C OE1 1 
ATOM   4545  O OE2 . GLU C  1 100 ? -5.810  -9.405  64.965  1.00 18.25  ? 106 GLU C OE2 1 
ATOM   4546  N N   . SER C  1 101 ? -6.773  -4.474  67.576  1.00 17.57  ? 107 SER C N   1 
ATOM   4547  C CA  . SER C  1 101 ? -6.045  -3.215  67.413  1.00 16.72  ? 107 SER C CA  1 
ATOM   4548  C C   . SER C  1 101 ? -4.628  -3.352  67.980  1.00 15.86  ? 107 SER C C   1 
ATOM   4549  O O   . SER C  1 101 ? -3.651  -2.970  67.331  1.00 15.38  ? 107 SER C O   1 
ATOM   4550  C CB  . SER C  1 101 ? -6.780  -2.067  68.108  1.00 16.44  ? 107 SER C CB  1 
ATOM   4551  O OG  . SER C  1 101 ? -8.133  -1.988  67.695  1.00 19.47  ? 107 SER C OG  1 
ATOM   4552  N N   . LEU C  1 102 ? -4.530  -3.921  69.181  1.00 15.20  ? 108 LEU C N   1 
ATOM   4553  C CA  . LEU C  1 102 ? -3.244  -4.123  69.843  1.00 14.98  ? 108 LEU C CA  1 
ATOM   4554  C C   . LEU C  1 102 ? -2.351  -5.123  69.099  1.00 14.95  ? 108 LEU C C   1 
ATOM   4555  O O   . LEU C  1 102 ? -1.142  -4.896  68.967  1.00 15.23  ? 108 LEU C O   1 
ATOM   4556  C CB  . LEU C  1 102 ? -3.438  -4.538  71.306  1.00 14.40  ? 108 LEU C CB  1 
ATOM   4557  C CG  . LEU C  1 102 ? -2.230  -4.378  72.232  1.00 13.58  ? 108 LEU C CG  1 
ATOM   4558  C CD1 . LEU C  1 102 ? -1.607  -2.995  72.092  1.00 11.11  ? 108 LEU C CD1 1 
ATOM   4559  C CD2 . LEU C  1 102 ? -2.622  -4.643  73.677  1.00 12.96  ? 108 LEU C CD2 1 
ATOM   4560  N N   . ARG C  1 103 ? -2.944  -6.211  68.604  1.00 14.09  ? 109 ARG C N   1 
ATOM   4561  C CA  . ARG C  1 103 ? -2.207  -7.177  67.785  1.00 14.54  ? 109 ARG C CA  1 
ATOM   4562  C C   . ARG C  1 103 ? -1.631  -6.510  66.543  1.00 15.25  ? 109 ARG C C   1 
ATOM   4563  O O   . ARG C  1 103 ? -0.473  -6.739  66.187  1.00 15.69  ? 109 ARG C O   1 
ATOM   4564  C CB  . ARG C  1 103 ? -3.093  -8.355  67.371  1.00 14.29  ? 109 ARG C CB  1 
ATOM   4565  C CG  . ARG C  1 103 ? -3.375  -9.336  68.480  1.00 13.02  ? 109 ARG C CG  1 
ATOM   4566  C CD  . ARG C  1 103 ? -4.167  -10.531 68.000  1.00 12.73  ? 109 ARG C CD  1 
ATOM   4567  N NE  . ARG C  1 103 ? -4.525  -11.387 69.128  1.00 16.23  ? 109 ARG C NE  1 
ATOM   4568  C CZ  . ARG C  1 103 ? -5.737  -11.453 69.674  1.00 15.99  ? 109 ARG C CZ  1 
ATOM   4569  N NH1 . ARG C  1 103 ? -6.734  -10.726 69.185  1.00 16.63  ? 109 ARG C NH1 1 
ATOM   4570  N NH2 . ARG C  1 103 ? -5.953  -12.257 70.707  1.00 15.33  ? 109 ARG C NH2 1 
ATOM   4571  N N   . GLN C  1 104 ? -2.446  -5.675  65.902  1.00 15.81  ? 110 GLN C N   1 
ATOM   4572  C CA  . GLN C  1 104 ? -2.061  -4.999  64.666  1.00 16.59  ? 110 GLN C CA  1 
ATOM   4573  C C   . GLN C  1 104 ? -0.907  -4.025  64.870  1.00 16.37  ? 110 GLN C C   1 
ATOM   4574  O O   . GLN C  1 104 ? -0.055  -3.888  63.992  1.00 16.75  ? 110 GLN C O   1 
ATOM   4575  C CB  . GLN C  1 104 ? -3.266  -4.298  64.044  1.00 17.15  ? 110 GLN C CB  1 
ATOM   4576  C CG  . GLN C  1 104 ? -4.234  -5.257  63.367  1.00 19.22  ? 110 GLN C CG  1 
ATOM   4577  C CD  . GLN C  1 104 ? -5.531  -4.599  62.941  1.00 20.25  ? 110 GLN C CD  1 
ATOM   4578  O OE1 . GLN C  1 104 ? -5.914  -3.548  63.454  1.00 20.80  ? 110 GLN C OE1 1 
ATOM   4579  N NE2 . GLN C  1 104 ? -6.220  -5.225  61.999  1.00 22.69  ? 110 GLN C NE2 1 
ATOM   4580  N N   . ILE C  1 105 ? -0.887  -3.362  66.027  1.00 15.78  ? 111 ILE C N   1 
ATOM   4581  C CA  . ILE C  1 105 ? 0.228   -2.494  66.421  1.00 15.61  ? 111 ILE C CA  1 
ATOM   4582  C C   . ILE C  1 105 ? 1.482   -3.319  66.738  1.00 15.69  ? 111 ILE C C   1 
ATOM   4583  O O   . ILE C  1 105 ? 2.599   -2.912  66.409  1.00 15.77  ? 111 ILE C O   1 
ATOM   4584  C CB  . ILE C  1 105 ? -0.142  -1.597  67.635  1.00 15.72  ? 111 ILE C CB  1 
ATOM   4585  C CG1 . ILE C  1 105 ? -1.319  -0.681  67.291  1.00 14.31  ? 111 ILE C CG1 1 
ATOM   4586  C CG2 . ILE C  1 105 ? 1.050   -0.747  68.083  1.00 16.65  ? 111 ILE C CG2 1 
ATOM   4587  C CD1 . ILE C  1 105 ? -2.076  -0.184  68.510  1.00 15.86  ? 111 ILE C CD1 1 
ATOM   4588  N N   . LEU C  1 106 ? 1.289   -4.479  67.365  1.00 15.64  ? 112 LEU C N   1 
ATOM   4589  C CA  . LEU C  1 106 ? 2.402   -5.347  67.749  1.00 15.81  ? 112 LEU C CA  1 
ATOM   4590  C C   . LEU C  1 106 ? 3.086   -6.022  66.566  1.00 15.91  ? 112 LEU C C   1 
ATOM   4591  O O   . LEU C  1 106 ? 4.311   -6.135  66.545  1.00 16.02  ? 112 LEU C O   1 
ATOM   4592  C CB  . LEU C  1 106 ? 1.960   -6.402  68.774  1.00 16.09  ? 112 LEU C CB  1 
ATOM   4593  C CG  . LEU C  1 106 ? 1.799   -5.963  70.235  1.00 16.10  ? 112 LEU C CG  1 
ATOM   4594  C CD1 . LEU C  1 106 ? 1.341   -7.127  71.096  1.00 15.81  ? 112 LEU C CD1 1 
ATOM   4595  C CD2 . LEU C  1 106 ? 3.089   -5.384  70.783  1.00 14.82  ? 112 LEU C CD2 1 
ATOM   4596  N N   . ARG C  1 107 ? 2.299   -6.461  65.586  1.00 15.78  ? 113 ARG C N   1 
ATOM   4597  C CA  . ARG C  1 107 ? 2.833   -7.205  64.443  1.00 15.41  ? 113 ARG C CA  1 
ATOM   4598  C C   . ARG C  1 107 ? 3.859   -6.423  63.635  1.00 15.74  ? 113 ARG C C   1 
ATOM   4599  O O   . ARG C  1 107 ? 4.767   -7.009  63.047  1.00 16.34  ? 113 ARG C O   1 
ATOM   4600  C CB  . ARG C  1 107 ? 1.710   -7.664  63.522  1.00 15.31  ? 113 ARG C CB  1 
ATOM   4601  C CG  . ARG C  1 107 ? 0.862   -8.775  64.089  1.00 14.55  ? 113 ARG C CG  1 
ATOM   4602  C CD  . ARG C  1 107 ? -0.082  -9.310  63.039  1.00 11.67  ? 113 ARG C CD  1 
ATOM   4603  N NE  . ARG C  1 107 ? -1.151  -10.100 63.634  1.00 9.98   ? 113 ARG C NE  1 
ATOM   4604  C CZ  . ARG C  1 107 ? -2.383  -9.651  63.851  1.00 11.18  ? 113 ARG C CZ  1 
ATOM   4605  N NH1 . ARG C  1 107 ? -2.716  -8.408  63.518  1.00 9.08   ? 113 ARG C NH1 1 
ATOM   4606  N NH2 . ARG C  1 107 ? -3.286  -10.454 64.399  1.00 10.87  ? 113 ARG C NH2 1 
ATOM   4607  N N   . ARG C  1 108 ? 3.708   -5.103  63.608  1.00 16.06  ? 114 ARG C N   1 
ATOM   4608  C CA  . ARG C  1 108 ? 4.621   -4.231  62.869  1.00 16.21  ? 114 ARG C CA  1 
ATOM   4609  C C   . ARG C  1 108 ? 5.590   -3.467  63.778  1.00 16.42  ? 114 ARG C C   1 
ATOM   4610  O O   . ARG C  1 108 ? 6.336   -2.603  63.306  1.00 16.82  ? 114 ARG C O   1 
ATOM   4611  C CB  . ARG C  1 108 ? 3.829   -3.245  62.008  1.00 16.54  ? 114 ARG C CB  1 
ATOM   4612  C CG  . ARG C  1 108 ? 2.940   -2.313  62.810  1.00 14.15  ? 114 ARG C CG  1 
ATOM   4613  C CD  . ARG C  1 108 ? 2.548   -1.097  62.009  1.00 15.81  ? 114 ARG C CD  1 
ATOM   4614  N NE  . ARG C  1 108 ? 1.523   -0.335  62.712  1.00 17.29  ? 114 ARG C NE  1 
ATOM   4615  C CZ  . ARG C  1 108 ? 0.221   -0.423  62.464  1.00 12.70  ? 114 ARG C CZ  1 
ATOM   4616  N NH1 . ARG C  1 108 ? -0.231  -1.231  61.511  1.00 8.18   ? 114 ARG C NH1 1 
ATOM   4617  N NH2 . ARG C  1 108 ? -0.627  0.309   63.168  1.00 11.07  ? 114 ARG C NH2 1 
ATOM   4618  N N   . SER C  1 109 ? 5.577   -3.794  65.070  1.00 15.79  ? 115 SER C N   1 
ATOM   4619  C CA  . SER C  1 109 ? 6.343   -3.063  66.082  1.00 15.77  ? 115 SER C CA  1 
ATOM   4620  C C   . SER C  1 109 ? 7.864   -3.251  66.008  1.00 15.17  ? 115 SER C C   1 
ATOM   4621  O O   . SER C  1 109 ? 8.618   -2.423  66.520  1.00 15.24  ? 115 SER C O   1 
ATOM   4622  C CB  . SER C  1 109 ? 5.856   -3.447  67.479  1.00 16.28  ? 115 SER C CB  1 
ATOM   4623  O OG  . SER C  1 109 ? 6.174   -4.798  67.779  1.00 17.36  ? 115 SER C OG  1 
ATOM   4624  N N   . GLY C  1 110 ? 8.307   -4.341  65.390  1.00 14.76  ? 116 GLY C N   1 
ATOM   4625  C CA  . GLY C  1 110 ? 9.731   -4.680  65.345  1.00 15.01  ? 116 GLY C CA  1 
ATOM   4626  C C   . GLY C  1 110 ? 10.208  -5.397  66.597  1.00 14.93  ? 116 GLY C C   1 
ATOM   4627  O O   . GLY C  1 110 ? 11.409  -5.573  66.806  1.00 14.83  ? 116 GLY C O   1 
ATOM   4628  N N   . GLY C  1 111 ? 9.257   -5.819  67.425  1.00 14.96  ? 117 GLY C N   1 
ATOM   4629  C CA  . GLY C  1 111 ? 9.562   -6.416  68.715  1.00 14.80  ? 117 GLY C CA  1 
ATOM   4630  C C   . GLY C  1 111 ? 9.323   -5.428  69.836  1.00 15.35  ? 117 GLY C C   1 
ATOM   4631  O O   . GLY C  1 111 ? 9.113   -4.235  69.594  1.00 14.92  ? 117 GLY C O   1 
ATOM   4632  N N   . ILE C  1 112 ? 9.357   -5.924  71.068  1.00 16.25  ? 118 ILE C N   1 
ATOM   4633  C CA  . ILE C  1 112 ? 9.123   -5.083  72.238  1.00 16.89  ? 118 ILE C CA  1 
ATOM   4634  C C   . ILE C  1 112 ? 10.281  -5.135  73.224  1.00 17.67  ? 118 ILE C C   1 
ATOM   4635  O O   . ILE C  1 112 ? 10.829  -6.204  73.508  1.00 17.92  ? 118 ILE C O   1 
ATOM   4636  C CB  . ILE C  1 112 ? 7.793   -5.432  72.956  1.00 16.99  ? 118 ILE C CB  1 
ATOM   4637  C CG1 . ILE C  1 112 ? 7.786   -6.890  73.444  1.00 16.53  ? 118 ILE C CG1 1 
ATOM   4638  C CG2 . ILE C  1 112 ? 6.601   -5.138  72.039  1.00 16.46  ? 118 ILE C CG2 1 
ATOM   4639  C CD1 . ILE C  1 112 ? 6.651   -7.234  74.401  1.00 15.51  ? 118 ILE C CD1 1 
ATOM   4640  N N   . GLY C  1 113 ? 10.657  -3.963  73.720  1.00 18.40  ? 119 GLY C N   1 
ATOM   4641  C CA  . GLY C  1 113 ? 11.620  -3.848  74.803  1.00 19.09  ? 119 GLY C CA  1 
ATOM   4642  C C   . GLY C  1 113 ? 10.881  -3.448  76.063  1.00 19.91  ? 119 GLY C C   1 
ATOM   4643  O O   . GLY C  1 113 ? 10.077  -2.515  76.049  1.00 19.91  ? 119 GLY C O   1 
ATOM   4644  N N   . LYS C  1 114 ? 11.141  -4.164  77.152  1.00 20.69  ? 120 LYS C N   1 
ATOM   4645  C CA  . LYS C  1 114 ? 10.503  -3.873  78.431  1.00 21.19  ? 120 LYS C CA  1 
ATOM   4646  C C   . LYS C  1 114 ? 11.384  -2.979  79.297  1.00 21.64  ? 120 LYS C C   1 
ATOM   4647  O O   . LYS C  1 114 ? 12.613  -3.071  79.255  1.00 21.61  ? 120 LYS C O   1 
ATOM   4648  C CB  . LYS C  1 114 ? 10.165  -5.167  79.172  1.00 21.27  ? 120 LYS C CB  1 
ATOM   4649  C CG  . LYS C  1 114 ? 9.144   -6.048  78.471  1.00 20.63  ? 120 LYS C CG  1 
ATOM   4650  C CD  . LYS C  1 114 ? 7.715   -5.679  78.845  1.00 22.23  ? 120 LYS C CD  1 
ATOM   4651  C CE  . LYS C  1 114 ? 6.705   -6.576  78.135  1.00 22.83  ? 120 LYS C CE  1 
ATOM   4652  N NZ  . LYS C  1 114 ? 6.963   -8.026  78.362  1.00 22.90  ? 120 LYS C NZ  1 
ATOM   4653  N N   . GLU C  1 115 ? 10.741  -2.112  80.074  1.00 22.44  ? 121 GLU C N   1 
ATOM   4654  C CA  . GLU C  1 115 ? 11.428  -1.176  80.961  1.00 23.08  ? 121 GLU C CA  1 
ATOM   4655  C C   . GLU C  1 115 ? 10.612  -1.027  82.233  1.00 23.33  ? 121 GLU C C   1 
ATOM   4656  O O   . GLU C  1 115 ? 9.392   -0.884  82.172  1.00 23.19  ? 121 GLU C O   1 
ATOM   4657  C CB  . GLU C  1 115 ? 11.595  0.181   80.274  1.00 23.02  ? 121 GLU C CB  1 
ATOM   4658  C CG  . GLU C  1 115 ? 12.542  1.147   80.974  1.00 24.82  ? 121 GLU C CG  1 
ATOM   4659  C CD  . GLU C  1 115 ? 12.736  2.442   80.197  1.00 28.11  ? 121 GLU C CD  1 
ATOM   4660  O OE1 . GLU C  1 115 ? 12.968  2.378   78.967  1.00 27.42  ? 121 GLU C OE1 1 
ATOM   4661  O OE2 . GLU C  1 115 ? 12.660  3.524   80.819  1.00 28.09  ? 121 GLU C OE2 1 
ATOM   4662  N N   . SER C  1 116 ? 11.284  -1.060  83.381  1.00 24.32  ? 122 SER C N   1 
ATOM   4663  C CA  . SER C  1 116 ? 10.599  -0.964  84.670  1.00 25.37  ? 122 SER C CA  1 
ATOM   4664  C C   . SER C  1 116 ? 10.020  0.431   84.903  1.00 26.00  ? 122 SER C C   1 
ATOM   4665  O O   . SER C  1 116 ? 10.721  1.437   84.768  1.00 25.92  ? 122 SER C O   1 
ATOM   4666  C CB  . SER C  1 116 ? 11.533  -1.362  85.816  1.00 25.50  ? 122 SER C CB  1 
ATOM   4667  O OG  . SER C  1 116 ? 10.803  -1.552  87.019  1.00 25.56  ? 122 SER C OG  1 
ATOM   4668  N N   . MET C  1 117 ? 8.733   0.479   85.236  1.00 26.95  ? 123 MET C N   1 
ATOM   4669  C CA  . MET C  1 117 ? 8.052   1.738   85.538  1.00 28.23  ? 123 MET C CA  1 
ATOM   4670  C C   . MET C  1 117 ? 8.453   2.269   86.914  1.00 29.15  ? 123 MET C C   1 
ATOM   4671  O O   . MET C  1 117 ? 8.455   3.480   87.142  1.00 29.54  ? 123 MET C O   1 
ATOM   4672  C CB  . MET C  1 117 ? 6.530   1.574   85.442  1.00 28.49  ? 123 MET C CB  1 
ATOM   4673  C CG  . MET C  1 117 ? 6.025   1.312   84.024  1.00 28.37  ? 123 MET C CG  1 
ATOM   4674  S SD  . MET C  1 117 ? 4.280   0.865   83.928  1.00 28.35  ? 123 MET C SD  1 
ATOM   4675  C CE  . MET C  1 117 ? 3.494   2.468   84.004  1.00 28.43  ? 123 MET C CE  1 
ATOM   4676  N N   . GLY C  1 118 ? 8.793   1.355   87.821  1.00 29.76  ? 124 GLY C N   1 
ATOM   4677  C CA  . GLY C  1 118 ? 9.309   1.719   89.136  1.00 30.48  ? 124 GLY C CA  1 
ATOM   4678  C C   . GLY C  1 118 ? 8.242   2.116   90.138  1.00 31.06  ? 124 GLY C C   1 
ATOM   4679  O O   . GLY C  1 118 ? 8.317   3.189   90.743  1.00 31.02  ? 124 GLY C O   1 
ATOM   4680  N N   . PHE C  1 119 ? 7.246   1.252   90.311  1.00 31.64  ? 125 PHE C N   1 
ATOM   4681  C CA  . PHE C  1 119 ? 6.234   1.449   91.340  1.00 32.10  ? 125 PHE C CA  1 
ATOM   4682  C C   . PHE C  1 119 ? 6.575   0.624   92.572  1.00 32.63  ? 125 PHE C C   1 
ATOM   4683  O O   . PHE C  1 119 ? 6.845   -0.575  92.472  1.00 32.63  ? 125 PHE C O   1 
ATOM   4684  C CB  . PHE C  1 119 ? 4.839   1.079   90.828  1.00 31.99  ? 125 PHE C CB  1 
ATOM   4685  C CG  . PHE C  1 119 ? 4.329   1.970   89.724  1.00 32.51  ? 125 PHE C CG  1 
ATOM   4686  C CD1 . PHE C  1 119 ? 3.531   1.443   88.709  1.00 32.57  ? 125 PHE C CD1 1 
ATOM   4687  C CD2 . PHE C  1 119 ? 4.640   3.331   89.695  1.00 32.18  ? 125 PHE C CD2 1 
ATOM   4688  C CE1 . PHE C  1 119 ? 3.048   2.258   87.684  1.00 31.66  ? 125 PHE C CE1 1 
ATOM   4689  C CE2 . PHE C  1 119 ? 4.164   4.152   88.670  1.00 31.10  ? 125 PHE C CE2 1 
ATOM   4690  C CZ  . PHE C  1 119 ? 3.366   3.613   87.665  1.00 29.82  ? 125 PHE C CZ  1 
ATOM   4691  N N   . THR C  1 120 ? 6.575   1.280   93.729  1.00 33.27  ? 126 THR C N   1 
ATOM   4692  C CA  . THR C  1 120 ? 6.789   0.607   95.007  1.00 33.99  ? 126 THR C CA  1 
ATOM   4693  C C   . THR C  1 120 ? 5.553   0.756   95.883  1.00 34.72  ? 126 THR C C   1 
ATOM   4694  O O   . THR C  1 120 ? 4.792   1.718   95.737  1.00 34.73  ? 126 THR C O   1 
ATOM   4695  C CB  . THR C  1 120 ? 8.015   1.158   95.750  1.00 34.07  ? 126 THR C CB  1 
ATOM   4696  O OG1 . THR C  1 120 ? 7.915   2.584   95.844  1.00 33.64  ? 126 THR C OG1 1 
ATOM   4697  C CG2 . THR C  1 120 ? 9.303   0.779   95.021  1.00 34.22  ? 126 THR C CG2 1 
ATOM   4698  N N   . TYR C  1 121 ? 5.358   -0.199  96.789  1.00 35.54  ? 127 TYR C N   1 
ATOM   4699  C CA  . TYR C  1 121 ? 4.148   -0.244  97.608  1.00 36.32  ? 127 TYR C CA  1 
ATOM   4700  C C   . TYR C  1 121 ? 4.436   -0.499  99.086  1.00 36.28  ? 127 TYR C C   1 
ATOM   4701  O O   . TYR C  1 121 ? 5.434   -1.133  99.438  1.00 36.17  ? 127 TYR C O   1 
ATOM   4702  C CB  . TYR C  1 121 ? 3.180   -1.306  97.072  1.00 36.53  ? 127 TYR C CB  1 
ATOM   4703  C CG  . TYR C  1 121 ? 2.858   -1.164  95.599  1.00 37.63  ? 127 TYR C CG  1 
ATOM   4704  C CD1 . TYR C  1 121 ? 3.640   -1.798  94.631  1.00 37.94  ? 127 TYR C CD1 1 
ATOM   4705  C CD2 . TYR C  1 121 ? 1.777   -0.392  95.171  1.00 37.92  ? 127 TYR C CD2 1 
ATOM   4706  C CE1 . TYR C  1 121 ? 3.353   -1.669  93.275  1.00 37.93  ? 127 TYR C CE1 1 
ATOM   4707  C CE2 . TYR C  1 121 ? 1.480   -0.259  93.813  1.00 37.91  ? 127 TYR C CE2 1 
ATOM   4708  C CZ  . TYR C  1 121 ? 2.273   -0.901  92.874  1.00 36.79  ? 127 TYR C CZ  1 
ATOM   4709  O OH  . TYR C  1 121 ? 1.993   -0.777  91.533  1.00 36.45  ? 127 TYR C OH  1 
ATOM   4710  N N   . SER C  1 122 ? 3.554   0.018   99.939  1.00 36.36  ? 128 SER C N   1 
ATOM   4711  C CA  . SER C  1 122 ? 3.581   -0.252  101.376 1.00 36.39  ? 128 SER C CA  1 
ATOM   4712  C C   . SER C  1 122 ? 2.164   -0.196  101.946 1.00 36.57  ? 128 SER C C   1 
ATOM   4713  O O   . SER C  1 122 ? 1.336   0.606   101.498 1.00 36.62  ? 128 SER C O   1 
ATOM   4714  C CB  . SER C  1 122 ? 4.503   0.728   102.111 1.00 36.26  ? 128 SER C CB  1 
ATOM   4715  O OG  . SER C  1 122 ? 4.080   2.070   101.936 1.00 35.11  ? 128 SER C OG  1 
ATOM   4716  N N   . GLY C  1 123 ? 1.892   -1.060  102.923 1.00 36.52  ? 129 GLY C N   1 
ATOM   4717  C CA  . GLY C  1 123 ? 0.566   -1.151  103.541 1.00 36.22  ? 129 GLY C CA  1 
ATOM   4718  C C   . GLY C  1 123 ? -0.385  -2.094  102.822 1.00 35.90  ? 129 GLY C C   1 
ATOM   4719  O O   . GLY C  1 123 ? -1.527  -2.279  103.251 1.00 35.88  ? 129 GLY C O   1 
ATOM   4720  N N   . ILE C  1 124 ? 0.088   -2.684  101.724 1.00 35.59  ? 130 ILE C N   1 
ATOM   4721  C CA  . ILE C  1 124 ? -0.690  -3.640  100.930 1.00 34.97  ? 130 ILE C CA  1 
ATOM   4722  C C   . ILE C  1 124 ? 0.173   -4.820  100.475 1.00 34.46  ? 130 ILE C C   1 
ATOM   4723  O O   . ILE C  1 124 ? 1.394   -4.811  100.659 1.00 34.28  ? 130 ILE C O   1 
ATOM   4724  C CB  . ILE C  1 124 ? -1.354  -2.975  99.690  1.00 35.03  ? 130 ILE C CB  1 
ATOM   4725  C CG1 . ILE C  1 124 ? -0.344  -2.124  98.909  1.00 36.14  ? 130 ILE C CG1 1 
ATOM   4726  C CG2 . ILE C  1 124 ? -2.579  -2.159  100.097 1.00 34.38  ? 130 ILE C CG2 1 
ATOM   4727  C CD1 . ILE C  1 124 ? -0.739  -1.872  97.462  1.00 37.64  ? 130 ILE C CD1 1 
ATOM   4728  N N   . ARG C  1 125 ? -0.475  -5.831  99.894  1.00 33.89  ? 131 ARG C N   1 
ATOM   4729  C CA  . ARG C  1 125 ? 0.212   -6.984  99.303  1.00 33.21  ? 131 ARG C CA  1 
ATOM   4730  C C   . ARG C  1 125 ? 0.520   -6.748  97.826  1.00 32.72  ? 131 ARG C C   1 
ATOM   4731  O O   . ARG C  1 125 ? -0.162  -5.970  97.154  1.00 32.61  ? 131 ARG C O   1 
ATOM   4732  C CB  . ARG C  1 125 ? -0.647  -8.245  99.418  1.00 33.36  ? 131 ARG C CB  1 
ATOM   4733  C CG  . ARG C  1 125 ? -0.672  -8.928  100.774 1.00 31.58  ? 131 ARG C CG  1 
ATOM   4734  C CD  . ARG C  1 125 ? -1.834  -9.911  100.785 1.00 32.22  ? 131 ARG C CD  1 
ATOM   4735  N NE  . ARG C  1 125 ? -1.892  -10.747 101.986 1.00 32.59  ? 131 ARG C NE  1 
ATOM   4736  C CZ  . ARG C  1 125 ? -3.001  -11.341 102.425 1.00 33.15  ? 131 ARG C CZ  1 
ATOM   4737  N NH1 . ARG C  1 125 ? -4.160  -11.181 101.777 1.00 30.53  ? 131 ARG C NH1 1 
ATOM   4738  N NH2 . ARG C  1 125 ? -2.958  -12.087 103.528 1.00 34.94  ? 131 ARG C NH2 1 
ATOM   4739  N N   . THR C  1 126 ? 1.545   -7.437  97.329  1.00 32.21  ? 132 THR C N   1 
ATOM   4740  C CA  . THR C  1 126 ? 1.909   -7.409  95.910  1.00 31.81  ? 132 THR C CA  1 
ATOM   4741  C C   . THR C  1 126 ? 2.139   -8.830  95.371  1.00 31.54  ? 132 THR C C   1 
ATOM   4742  O O   . THR C  1 126 ? 2.499   -9.016  94.205  1.00 31.33  ? 132 THR C O   1 
ATOM   4743  C CB  . THR C  1 126 ? 3.168   -6.532  95.652  1.00 31.81  ? 132 THR C CB  1 
ATOM   4744  O OG1 . THR C  1 126 ? 4.219   -6.914  96.548  1.00 31.96  ? 132 THR C OG1 1 
ATOM   4745  C CG2 . THR C  1 126 ? 2.856   -5.054  95.851  1.00 30.95  ? 132 THR C CG2 1 
ATOM   4746  N N   . ASN C  1 127 ? 1.897   -9.822  96.228  1.00 31.19  ? 133 ASN C N   1 
ATOM   4747  C CA  . ASN C  1 127 ? 2.224   -11.222 95.947  1.00 30.89  ? 133 ASN C CA  1 
ATOM   4748  C C   . ASN C  1 127 ? 1.052   -12.085 95.456  1.00 30.39  ? 133 ASN C C   1 
ATOM   4749  O O   . ASN C  1 127 ? 1.037   -13.301 95.667  1.00 30.18  ? 133 ASN C O   1 
ATOM   4750  C CB  . ASN C  1 127 ? 2.870   -11.863 97.189  1.00 31.36  ? 133 ASN C CB  1 
ATOM   4751  C CG  . ASN C  1 127 ? 1.944   -11.867 98.404  1.00 31.87  ? 133 ASN C CG  1 
ATOM   4752  O OD1 . ASN C  1 127 ? 1.363   -10.842 98.763  1.00 33.25  ? 133 ASN C OD1 1 
ATOM   4753  N ND2 . ASN C  1 127 ? 1.811   -13.025 99.042  1.00 30.85  ? 133 ASN C ND2 1 
ATOM   4754  N N   . GLY C  1 128 ? 0.083   -11.458 94.791  1.00 29.80  ? 134 GLY C N   1 
ATOM   4755  C CA  . GLY C  1 128 ? -1.102  -12.165 94.301  1.00 29.27  ? 134 GLY C CA  1 
ATOM   4756  C C   . GLY C  1 128 ? -0.802  -13.219 93.248  1.00 28.65  ? 134 GLY C C   1 
ATOM   4757  O O   . GLY C  1 128 ? -0.149  -12.933 92.243  1.00 28.45  ? 134 GLY C O   1 
ATOM   4758  N N   . ALA C  1 129 ? -1.287  -14.437 93.487  1.00 27.79  ? 135 ALA C N   1 
ATOM   4759  C CA  . ALA C  1 129 ? -1.019  -15.580 92.616  1.00 26.98  ? 135 ALA C CA  1 
ATOM   4760  C C   . ALA C  1 129 ? -2.255  -16.462 92.411  1.00 26.66  ? 135 ALA C C   1 
ATOM   4761  O O   . ALA C  1 129 ? -3.207  -16.403 93.192  1.00 26.23  ? 135 ALA C O   1 
ATOM   4762  C CB  . ALA C  1 129 ? 0.138   -16.400 93.170  1.00 26.72  ? 135 ALA C CB  1 
ATOM   4763  N N   . THR C  1 130 ? -2.226  -17.278 91.357  1.00 26.52  ? 136 THR C N   1 
ATOM   4764  C CA  . THR C  1 130 ? -3.345  -18.160 91.005  1.00 26.49  ? 136 THR C CA  1 
ATOM   4765  C C   . THR C  1 130 ? -2.873  -19.507 90.456  1.00 26.71  ? 136 THR C C   1 
ATOM   4766  O O   . THR C  1 130 ? -1.804  -19.600 89.846  1.00 26.72  ? 136 THR C O   1 
ATOM   4767  C CB  . THR C  1 130 ? -4.317  -17.494 89.989  1.00 26.49  ? 136 THR C CB  1 
ATOM   4768  O OG1 . THR C  1 130 ? -5.248  -18.467 89.495  1.00 25.26  ? 136 THR C OG1 1 
ATOM   4769  C CG2 . THR C  1 130 ? -3.559  -16.893 88.811  1.00 26.02  ? 136 THR C CG2 1 
ATOM   4770  N N   . SER C  1 131 ? -3.689  -20.539 90.669  1.00 26.95  ? 137 SER C N   1 
ATOM   4771  C CA  . SER C  1 131 ? -3.373  -21.898 90.225  1.00 27.30  ? 137 SER C CA  1 
ATOM   4772  C C   . SER C  1 131 ? -3.545  -22.091 88.717  1.00 27.19  ? 137 SER C C   1 
ATOM   4773  O O   . SER C  1 131 ? -3.034  -23.058 88.152  1.00 27.55  ? 137 SER C O   1 
ATOM   4774  C CB  . SER C  1 131 ? -4.206  -22.929 90.995  1.00 27.29  ? 137 SER C CB  1 
ATOM   4775  O OG  . SER C  1 131 ? -5.593  -22.729 90.785  1.00 29.05  ? 137 SER C OG  1 
ATOM   4776  N N   . ALA C  1 132 ? -4.265  -21.174 88.074  1.00 27.18  ? 138 ALA C N   1 
ATOM   4777  C CA  . ALA C  1 132 ? -4.431  -21.198 86.620  1.00 27.40  ? 138 ALA C CA  1 
ATOM   4778  C C   . ALA C  1 132 ? -3.142  -20.791 85.899  1.00 27.32  ? 138 ALA C C   1 
ATOM   4779  O O   . ALA C  1 132 ? -2.831  -21.315 84.826  1.00 27.43  ? 138 ALA C O   1 
ATOM   4780  C CB  . ALA C  1 132 ? -5.592  -20.307 86.197  1.00 27.54  ? 138 ALA C CB  1 
ATOM   4781  N N   . CYS C  1 133 ? -2.402  -19.858 86.497  1.00 27.06  ? 139 CYS C N   1 
ATOM   4782  C CA  . CYS C  1 133 ? -1.101  -19.437 85.983  1.00 26.74  ? 139 CYS C CA  1 
ATOM   4783  C C   . CYS C  1 133 ? 0.011   -20.145 86.754  1.00 27.28  ? 139 CYS C C   1 
ATOM   4784  O O   . CYS C  1 133 ? 0.646   -19.557 87.634  1.00 26.95  ? 139 CYS C O   1 
ATOM   4785  C CB  . CYS C  1 133 ? -0.944  -17.917 86.088  1.00 26.24  ? 139 CYS C CB  1 
ATOM   4786  S SG  . CYS C  1 133 ? -2.325  -16.981 85.417  0.60 23.39  ? 139 CYS C SG  1 
ATOM   4787  N N   . THR C  1 134 ? 0.238   -21.413 86.422  1.00 28.20  ? 140 THR C N   1 
ATOM   4788  C CA  . THR C  1 134 ? 1.215   -22.224 87.145  1.00 29.65  ? 140 THR C CA  1 
ATOM   4789  C C   . THR C  1 134 ? 2.630   -22.116 86.561  1.00 30.45  ? 140 THR C C   1 
ATOM   4790  O O   . THR C  1 134 ? 2.848   -22.308 85.360  1.00 30.57  ? 140 THR C O   1 
ATOM   4791  C CB  . THR C  1 134 ? 0.747   -23.706 87.317  1.00 29.80  ? 140 THR C CB  1 
ATOM   4792  O OG1 . THR C  1 134 ? 1.556   -24.358 88.307  1.00 29.45  ? 140 THR C OG1 1 
ATOM   4793  C CG2 . THR C  1 134 ? 0.804   -24.491 85.996  1.00 30.36  ? 140 THR C CG2 1 
ATOM   4794  N N   . ARG C  1 135 ? 3.576   -21.785 87.436  1.00 31.29  ? 141 ARG C N   1 
ATOM   4795  C CA  . ARG C  1 135 ? 4.973   -21.562 87.073  1.00 32.43  ? 141 ARG C CA  1 
ATOM   4796  C C   . ARG C  1 135 ? 5.826   -21.845 88.313  1.00 32.81  ? 141 ARG C C   1 
ATOM   4797  O O   . ARG C  1 135 ? 6.121   -20.937 89.100  1.00 33.29  ? 141 ARG C O   1 
ATOM   4798  C CB  . ARG C  1 135 ? 5.154   -20.120 86.573  1.00 32.58  ? 141 ARG C CB  1 
ATOM   4799  C CG  . ARG C  1 135 ? 6.589   -19.677 86.283  1.00 34.13  ? 141 ARG C CG  1 
ATOM   4800  C CD  . ARG C  1 135 ? 6.746   -18.161 86.442  1.00 34.75  ? 141 ARG C CD  1 
ATOM   4801  N NE  . ARG C  1 135 ? 6.345   -17.409 85.250  1.00 35.39  ? 141 ARG C NE  1 
ATOM   4802  C CZ  . ARG C  1 135 ? 5.133   -16.888 85.046  1.00 35.32  ? 141 ARG C CZ  1 
ATOM   4803  N NH1 . ARG C  1 135 ? 4.167   -17.032 85.948  1.00 34.90  ? 141 ARG C NH1 1 
ATOM   4804  N NH2 . ARG C  1 135 ? 4.883   -16.220 83.927  1.00 35.51  ? 141 ARG C NH2 1 
ATOM   4805  N N   . SER C  1 136 ? 6.204   -23.114 88.482  1.00 32.86  ? 142 SER C N   1 
ATOM   4806  C CA  . SER C  1 136 ? 6.868   -23.604 89.700  1.00 33.13  ? 142 SER C CA  1 
ATOM   4807  C C   . SER C  1 136 ? 6.029   -23.275 90.941  1.00 32.81  ? 142 SER C C   1 
ATOM   4808  O O   . SER C  1 136 ? 6.429   -22.468 91.788  1.00 33.21  ? 142 SER C O   1 
ATOM   4809  C CB  . SER C  1 136 ? 8.300   -23.056 89.828  1.00 33.44  ? 142 SER C CB  1 
ATOM   4810  O OG  . SER C  1 136 ? 9.054   -23.288 88.647  1.00 34.07  ? 142 SER C OG  1 
ATOM   4811  N N   . GLY C  1 137 ? 4.861   -23.908 91.029  1.00 32.07  ? 144 GLY C N   1 
ATOM   4812  C CA  . GLY C  1 137 ? 3.866   -23.582 92.050  1.00 31.03  ? 144 GLY C CA  1 
ATOM   4813  C C   . GLY C  1 137 ? 2.798   -22.661 91.483  1.00 30.30  ? 144 GLY C C   1 
ATOM   4814  O O   . GLY C  1 137 ? 2.456   -22.748 90.300  1.00 30.38  ? 144 GLY C O   1 
ATOM   4815  N N   . SER C  1 138 ? 2.268   -21.779 92.326  1.00 29.31  ? 145 SER C N   1 
ATOM   4816  C CA  . SER C  1 138 ? 1.288   -20.787 91.884  1.00 28.13  ? 145 SER C CA  1 
ATOM   4817  C C   . SER C  1 138 ? 1.943   -19.420 91.725  1.00 27.55  ? 145 SER C C   1 
ATOM   4818  O O   . SER C  1 138 ? 2.663   -18.962 92.617  1.00 27.61  ? 145 SER C O   1 
ATOM   4819  C CB  . SER C  1 138 ? 0.111   -20.703 92.861  1.00 28.03  ? 145 SER C CB  1 
ATOM   4820  O OG  . SER C  1 138 ? -0.804  -21.767 92.660  1.00 26.37  ? 145 SER C OG  1 
ATOM   4821  N N   . SER C  1 139 ? 1.701   -18.782 90.580  1.00 26.29  ? 146 SER C N   1 
ATOM   4822  C CA  . SER C  1 139 ? 2.216   -17.437 90.326  1.00 25.03  ? 146 SER C CA  1 
ATOM   4823  C C   . SER C  1 139 ? 1.248   -16.589 89.493  1.00 24.01  ? 146 SER C C   1 
ATOM   4824  O O   . SER C  1 139 ? 0.029   -16.779 89.564  1.00 24.16  ? 146 SER C O   1 
ATOM   4825  C CB  . SER C  1 139 ? 3.617   -17.485 89.701  1.00 25.07  ? 146 SER C CB  1 
ATOM   4826  O OG  . SER C  1 139 ? 3.576   -18.030 88.400  1.00 24.78  ? 146 SER C OG  1 
ATOM   4827  N N   . PHE C  1 140 ? 1.797   -15.662 88.708  1.00 22.30  ? 147 PHE C N   1 
ATOM   4828  C CA  . PHE C  1 140 ? 1.001   -14.634 88.039  1.00 20.15  ? 147 PHE C CA  1 
ATOM   4829  C C   . PHE C  1 140 ? 1.609   -14.218 86.693  1.00 19.43  ? 147 PHE C C   1 
ATOM   4830  O O   . PHE C  1 140 ? 2.524   -14.867 86.189  1.00 19.64  ? 147 PHE C O   1 
ATOM   4831  C CB  . PHE C  1 140 ? 0.864   -13.426 88.977  1.00 19.27  ? 147 PHE C CB  1 
ATOM   4832  C CG  . PHE C  1 140 ? -0.257  -12.493 88.619  1.00 16.26  ? 147 PHE C CG  1 
ATOM   4833  C CD1 . PHE C  1 140 ? -1.546  -12.974 88.408  1.00 13.84  ? 147 PHE C CD1 1 
ATOM   4834  C CD2 . PHE C  1 140 ? -0.026  -11.126 88.513  1.00 12.94  ? 147 PHE C CD2 1 
ATOM   4835  C CE1 . PHE C  1 140 ? -2.584  -12.109 88.080  1.00 13.46  ? 147 PHE C CE1 1 
ATOM   4836  C CE2 . PHE C  1 140 ? -1.054  -10.257 88.189  1.00 12.89  ? 147 PHE C CE2 1 
ATOM   4837  C CZ  . PHE C  1 140 ? -2.340  -10.748 87.973  1.00 12.34  ? 147 PHE C CZ  1 
ATOM   4838  N N   . TYR C  1 141 ? 1.079   -13.147 86.111  1.00 18.60  ? 148 TYR C N   1 
ATOM   4839  C CA  . TYR C  1 141 ? 1.638   -12.544 84.910  1.00 17.89  ? 148 TYR C CA  1 
ATOM   4840  C C   . TYR C  1 141 ? 2.941   -11.836 85.269  1.00 17.59  ? 148 TYR C C   1 
ATOM   4841  O O   . TYR C  1 141 ? 2.961   -10.971 86.148  1.00 17.39  ? 148 TYR C O   1 
ATOM   4842  C CB  . TYR C  1 141 ? 0.641   -11.554 84.296  1.00 17.77  ? 148 TYR C CB  1 
ATOM   4843  C CG  . TYR C  1 141 ? -0.633  -12.191 83.783  1.00 17.07  ? 148 TYR C CG  1 
ATOM   4844  C CD1 . TYR C  1 141 ? -1.801  -12.174 84.543  1.00 15.11  ? 148 TYR C CD1 1 
ATOM   4845  C CD2 . TYR C  1 141 ? -0.669  -12.813 82.536  1.00 17.38  ? 148 TYR C CD2 1 
ATOM   4846  C CE1 . TYR C  1 141 ? -2.977  -12.762 84.070  1.00 17.61  ? 148 TYR C CE1 1 
ATOM   4847  C CE2 . TYR C  1 141 ? -1.836  -13.401 82.056  1.00 16.69  ? 148 TYR C CE2 1 
ATOM   4848  C CZ  . TYR C  1 141 ? -2.984  -13.372 82.822  1.00 17.44  ? 148 TYR C CZ  1 
ATOM   4849  O OH  . TYR C  1 141 ? -4.135  -13.956 82.336  1.00 17.84  ? 148 TYR C OH  1 
ATOM   4850  N N   . ALA C  1 142 ? 4.019   -12.212 84.583  1.00 17.23  ? 149 ALA C N   1 
ATOM   4851  C CA  . ALA C  1 142 ? 5.377   -11.776 84.930  1.00 16.91  ? 149 ALA C CA  1 
ATOM   4852  C C   . ALA C  1 142 ? 5.588   -10.257 84.946  1.00 16.92  ? 149 ALA C C   1 
ATOM   4853  O O   . ALA C  1 142 ? 6.441   -9.757  85.676  1.00 16.78  ? 149 ALA C O   1 
ATOM   4854  C CB  . ALA C  1 142 ? 6.398   -12.449 84.020  1.00 16.55  ? 149 ALA C CB  1 
ATOM   4855  N N   . GLU C  1 143 ? 4.809   -9.532  84.151  1.00 17.26  ? 150 GLU C N   1 
ATOM   4856  C CA  . GLU C  1 143 ? 4.943   -8.079  84.065  1.00 18.04  ? 150 GLU C CA  1 
ATOM   4857  C C   . GLU C  1 143 ? 3.896   -7.352  84.913  1.00 19.12  ? 150 GLU C C   1 
ATOM   4858  O O   . GLU C  1 143 ? 3.870   -6.119  84.966  1.00 18.64  ? 150 GLU C O   1 
ATOM   4859  C CB  . GLU C  1 143 ? 4.865   -7.620  82.603  1.00 17.66  ? 150 GLU C CB  1 
ATOM   4860  C CG  . GLU C  1 143 ? 5.684   -8.460  81.618  1.00 16.80  ? 150 GLU C CG  1 
ATOM   4861  C CD  . GLU C  1 143 ? 7.188   -8.311  81.789  1.00 17.71  ? 150 GLU C CD  1 
ATOM   4862  O OE1 . GLU C  1 143 ? 7.653   -8.039  82.917  1.00 16.55  ? 150 GLU C OE1 1 
ATOM   4863  O OE2 . GLU C  1 143 ? 7.914   -8.481  80.785  1.00 17.67  ? 150 GLU C OE2 1 
ATOM   4864  N N   . MET C  1 144 ? 3.048   -8.128  85.584  1.00 20.33  ? 151 MET C N   1 
ATOM   4865  C CA  . MET C  1 144 ? 1.926   -7.585  86.341  1.00 21.45  ? 151 MET C CA  1 
ATOM   4866  C C   . MET C  1 144 ? 2.012   -7.908  87.829  1.00 22.14  ? 151 MET C C   1 
ATOM   4867  O O   . MET C  1 144 ? 2.542   -8.949  88.225  1.00 22.43  ? 151 MET C O   1 
ATOM   4868  C CB  . MET C  1 144 ? 0.601   -8.097  85.766  1.00 21.79  ? 151 MET C CB  1 
ATOM   4869  C CG  . MET C  1 144 ? 0.384   -7.748  84.301  1.00 24.02  ? 151 MET C CG  1 
ATOM   4870  S SD  . MET C  1 144 ? 0.248   -5.971  84.046  1.00 28.65  ? 151 MET C SD  1 
ATOM   4871  C CE  . MET C  1 144 ? 1.263   -5.762  82.586  1.00 28.79  ? 151 MET C CE  1 
ATOM   4872  N N   . LYS C  1 145 ? 1.483   -7.002  88.646  1.00 22.55  ? 152 LYS C N   1 
ATOM   4873  C CA  . LYS C  1 145 ? 1.453   -7.173  90.090  1.00 23.01  ? 152 LYS C CA  1 
ATOM   4874  C C   . LYS C  1 145 ? 0.005   -7.232  90.564  1.00 23.28  ? 152 LYS C C   1 
ATOM   4875  O O   . LYS C  1 145 ? -0.793  -6.350  90.241  1.00 23.67  ? 152 LYS C O   1 
ATOM   4876  C CB  . LYS C  1 145 ? 2.201   -6.025  90.779  1.00 23.08  ? 152 LYS C CB  1 
ATOM   4877  C CG  . LYS C  1 145 ? 3.715   -6.009  90.531  1.00 23.31  ? 152 LYS C CG  1 
ATOM   4878  C CD  . LYS C  1 145 ? 4.519   -6.490  91.741  1.00 26.03  ? 152 LYS C CD  1 
ATOM   4879  C CE  . LYS C  1 145 ? 4.526   -8.012  91.893  1.00 27.93  ? 152 LYS C CE  1 
ATOM   4880  N NZ  . LYS C  1 145 ? 5.403   -8.692  90.900  1.00 29.55  ? 152 LYS C NZ  1 
ATOM   4881  N N   . TRP C  1 146 ? -0.337  -8.284  91.307  1.00 23.47  ? 153 TRP C N   1 
ATOM   4882  C CA  . TRP C  1 146 ? -1.676  -8.419  91.876  1.00 23.97  ? 153 TRP C CA  1 
ATOM   4883  C C   . TRP C  1 146 ? -1.713  -7.764  93.260  1.00 25.16  ? 153 TRP C C   1 
ATOM   4884  O O   . TRP C  1 146 ? -1.044  -8.214  94.196  1.00 25.36  ? 153 TRP C O   1 
ATOM   4885  C CB  . TRP C  1 146 ? -2.097  -9.893  91.950  1.00 23.40  ? 153 TRP C CB  1 
ATOM   4886  C CG  . TRP C  1 146 ? -3.589  -10.124 92.148  1.00 23.34  ? 153 TRP C CG  1 
ATOM   4887  C CD1 . TRP C  1 146 ? -4.497  -9.253  92.693  1.00 22.77  ? 153 TRP C CD1 1 
ATOM   4888  C CD2 . TRP C  1 146 ? -4.328  -11.314 91.827  1.00 22.96  ? 153 TRP C CD2 1 
ATOM   4889  N NE1 . TRP C  1 146 ? -5.749  -9.820  92.716  1.00 21.02  ? 153 TRP C NE1 1 
ATOM   4890  C CE2 . TRP C  1 146 ? -5.675  -11.083 92.192  1.00 22.46  ? 153 TRP C CE2 1 
ATOM   4891  C CE3 . TRP C  1 146 ? -3.984  -12.549 91.262  1.00 22.56  ? 153 TRP C CE3 1 
ATOM   4892  C CZ2 . TRP C  1 146 ? -6.679  -12.043 92.010  1.00 22.02  ? 153 TRP C CZ2 1 
ATOM   4893  C CZ3 . TRP C  1 146 ? -4.986  -13.504 91.077  1.00 22.09  ? 153 TRP C CZ3 1 
ATOM   4894  C CH2 . TRP C  1 146 ? -6.315  -13.243 91.451  1.00 21.28  ? 153 TRP C CH2 1 
ATOM   4895  N N   . LEU C  1 147 ? -2.499  -6.695  93.376  1.00 26.07  ? 154 LEU C N   1 
ATOM   4896  C CA  . LEU C  1 147 ? -2.577  -5.918  94.610  1.00 26.64  ? 154 LEU C CA  1 
ATOM   4897  C C   . LEU C  1 147 ? -3.771  -6.331  95.467  1.00 27.35  ? 154 LEU C C   1 
ATOM   4898  O O   . LEU C  1 147 ? -4.907  -6.344  94.995  1.00 27.34  ? 154 LEU C O   1 
ATOM   4899  C CB  . LEU C  1 147 ? -2.638  -4.417  94.298  1.00 26.51  ? 154 LEU C CB  1 
ATOM   4900  C CG  . LEU C  1 147 ? -1.639  -3.821  93.295  1.00 26.83  ? 154 LEU C CG  1 
ATOM   4901  C CD1 . LEU C  1 147 ? -1.861  -2.323  93.170  1.00 25.58  ? 154 LEU C CD1 1 
ATOM   4902  C CD2 . LEU C  1 147 ? -0.185  -4.115  93.677  1.00 27.00  ? 154 LEU C CD2 1 
ATOM   4903  N N   . LEU C  1 148 ? -3.495  -6.670  96.725  1.00 28.63  ? 155 LEU C N   1 
ATOM   4904  C CA  . LEU C  1 148 ? -4.525  -7.051  97.698  1.00 29.38  ? 155 LEU C CA  1 
ATOM   4905  C C   . LEU C  1 148 ? -4.460  -6.155  98.931  1.00 30.25  ? 155 LEU C C   1 
ATOM   4906  O O   . LEU C  1 148 ? -3.607  -5.272  99.023  1.00 30.56  ? 155 LEU C O   1 
ATOM   4907  C CB  . LEU C  1 148 ? -4.337  -8.505  98.150  1.00 29.10  ? 155 LEU C CB  1 
ATOM   4908  C CG  . LEU C  1 148 ? -4.600  -9.686  97.220  1.00 28.22  ? 155 LEU C CG  1 
ATOM   4909  C CD1 . LEU C  1 148 ? -3.388  -9.963  96.348  1.00 28.14  ? 155 LEU C CD1 1 
ATOM   4910  C CD2 . LEU C  1 148 ? -4.930  -10.913 98.054  1.00 27.93  ? 155 LEU C CD2 1 
ATOM   4911  N N   . SER C  1 149 ? -5.366  -6.397  99.876  1.00 31.21  ? 156 SER C N   1 
ATOM   4912  C CA  . SER C  1 149 ? -5.264  -5.830  101.218 1.00 31.62  ? 156 SER C CA  1 
ATOM   4913  C C   . SER C  1 149 ? -4.375  -6.736  102.072 1.00 31.90  ? 156 SER C C   1 
ATOM   4914  O O   . SER C  1 149 ? -4.161  -7.901  101.725 1.00 31.85  ? 156 SER C O   1 
ATOM   4915  C CB  . SER C  1 149 ? -6.649  -5.684  101.850 1.00 31.61  ? 156 SER C CB  1 
ATOM   4916  O OG  . SER C  1 149 ? -7.482  -4.846  101.065 1.00 31.96  ? 156 SER C OG  1 
ATOM   4917  N N   . ASN C  1 150 ? -3.870  -6.199  103.184 1.00 32.20  ? 157 ASN C N   1 
ATOM   4918  C CA  . ASN C  1 150 ? -2.924  -6.912  104.054 1.00 32.30  ? 157 ASN C CA  1 
ATOM   4919  C C   . ASN C  1 150 ? -3.403  -8.272  104.574 1.00 32.19  ? 157 ASN C C   1 
ATOM   4920  O O   . ASN C  1 150 ? -2.593  -9.179  104.784 1.00 32.23  ? 157 ASN C O   1 
ATOM   4921  C CB  . ASN C  1 150 ? -2.482  -6.018  105.218 1.00 32.57  ? 157 ASN C CB  1 
ATOM   4922  C CG  . ASN C  1 150 ? -1.349  -5.073  104.840 1.00 33.30  ? 157 ASN C CG  1 
ATOM   4923  O OD1 . ASN C  1 150 ? -0.581  -5.335  103.909 1.00 32.09  ? 157 ASN C OD1 1 
ATOM   4924  N ND2 . ASN C  1 150 ? -1.233  -3.971  105.574 1.00 33.26  ? 157 ASN C ND2 1 
ATOM   4925  N N   . SER C  1 151 ? -4.711  -8.398  104.787 1.00 32.09  ? 158 SER C N   1 
ATOM   4926  C CA  . SER C  1 151 ? -5.335  -9.671  105.159 1.00 32.10  ? 158 SER C CA  1 
ATOM   4927  C C   . SER C  1 151 ? -6.786  -9.727  104.669 1.00 32.04  ? 158 SER C C   1 
ATOM   4928  O O   . SER C  1 151 ? -7.248  -8.815  103.973 1.00 31.98  ? 158 SER C O   1 
ATOM   4929  C CB  . SER C  1 151 ? -5.246  -9.916  106.676 1.00 32.20  ? 158 SER C CB  1 
ATOM   4930  O OG  . SER C  1 151 ? -5.934  -8.916  107.410 1.00 30.98  ? 158 SER C OG  1 
ATOM   4931  N N   . ASP C  1 152 A -7.493  -10.800 105.028 1.00 31.92  ? 158 ASP C N   1 
ATOM   4932  C CA  . ASP C  1 152 A -8.877  -11.011 104.600 1.00 31.65  ? 158 ASP C CA  1 
ATOM   4933  C C   . ASP C  1 152 A -9.804  -9.898  105.087 1.00 31.22  ? 158 ASP C C   1 
ATOM   4934  O O   . ASP C  1 152 A -9.840  -9.579  106.279 1.00 31.11  ? 158 ASP C O   1 
ATOM   4935  C CB  . ASP C  1 152 A -9.394  -12.379 105.071 1.00 31.87  ? 158 ASP C CB  1 
ATOM   4936  C CG  . ASP C  1 152 A -8.661  -13.552 104.421 1.00 33.11  ? 158 ASP C CG  1 
ATOM   4937  O OD1 . ASP C  1 152 A -7.576  -13.351 103.831 1.00 34.51  ? 158 ASP C OD1 1 
ATOM   4938  O OD2 . ASP C  1 152 A -9.176  -14.688 104.508 1.00 34.10  ? 158 ASP C OD2 1 
ATOM   4939  N N   . ASN C  1 153 B -10.525 -9.301  104.141 1.00 30.84  ? 158 ASN C N   1 
ATOM   4940  C CA  . ASN C  1 153 B -11.548 -8.281  104.412 1.00 30.47  ? 158 ASN C CA  1 
ATOM   4941  C C   . ASN C  1 153 B -11.042 -6.929  104.945 1.00 30.18  ? 158 ASN C C   1 
ATOM   4942  O O   . ASN C  1 153 B -11.834 -6.107  105.410 1.00 29.98  ? 158 ASN C O   1 
ATOM   4943  C CB  . ASN C  1 153 B -12.672 -8.850  105.295 1.00 30.47  ? 158 ASN C CB  1 
ATOM   4944  C CG  . ASN C  1 153 B -13.319 -10.084 104.690 1.00 30.02  ? 158 ASN C CG  1 
ATOM   4945  O OD1 . ASN C  1 153 B -14.050 -9.998  103.702 1.00 28.69  ? 158 ASN C OD1 1 
ATOM   4946  N ND2 . ASN C  1 153 B -13.051 -11.241 105.284 1.00 29.60  ? 158 ASN C ND2 1 
ATOM   4947  N N   . ALA C  1 154 ? -9.732  -6.701  104.856 1.00 30.08  ? 159 ALA C N   1 
ATOM   4948  C CA  . ALA C  1 154 ? -9.136  -5.421  105.247 1.00 30.17  ? 159 ALA C CA  1 
ATOM   4949  C C   . ALA C  1 154 ? -9.360  -4.347  104.179 1.00 30.38  ? 159 ALA C C   1 
ATOM   4950  O O   . ALA C  1 154 ? -9.553  -4.660  103.002 1.00 30.41  ? 159 ALA C O   1 
ATOM   4951  C CB  . ALA C  1 154 ? -7.649  -5.590  105.543 1.00 30.11  ? 159 ALA C CB  1 
ATOM   4952  N N   . ALA C  1 155 ? -9.335  -3.083  104.597 1.00 30.63  ? 160 ALA C N   1 
ATOM   4953  C CA  . ALA C  1 155 ? -9.599  -1.961  103.696 1.00 30.76  ? 160 ALA C CA  1 
ATOM   4954  C C   . ALA C  1 155 ? -8.397  -1.621  102.816 1.00 30.96  ? 160 ALA C C   1 
ATOM   4955  O O   . ALA C  1 155 ? -7.287  -1.415  103.313 1.00 30.86  ? 160 ALA C O   1 
ATOM   4956  C CB  . ALA C  1 155 ? -10.043 -0.741  104.487 1.00 30.56  ? 160 ALA C CB  1 
ATOM   4957  N N   . PHE C  1 156 ? -8.633  -1.567  101.508 1.00 31.30  ? 161 PHE C N   1 
ATOM   4958  C CA  . PHE C  1 156 ? -7.616  -1.153  100.547 1.00 31.94  ? 161 PHE C CA  1 
ATOM   4959  C C   . PHE C  1 156 ? -7.600  0.374   100.450 1.00 31.93  ? 161 PHE C C   1 
ATOM   4960  O O   . PHE C  1 156 ? -8.617  0.983   100.106 1.00 31.88  ? 161 PHE C O   1 
ATOM   4961  C CB  . PHE C  1 156 ? -7.892  -1.776  99.174  1.00 32.29  ? 161 PHE C CB  1 
ATOM   4962  C CG  . PHE C  1 156 ? -6.707  -1.762  98.242  1.00 34.07  ? 161 PHE C CG  1 
ATOM   4963  C CD1 . PHE C  1 156 ? -5.974  -2.925  98.017  1.00 35.18  ? 161 PHE C CD1 1 
ATOM   4964  C CD2 . PHE C  1 156 ? -6.330  -0.594  97.580  1.00 35.68  ? 161 PHE C CD2 1 
ATOM   4965  C CE1 . PHE C  1 156 ? -4.879  -2.925  97.151  1.00 35.65  ? 161 PHE C CE1 1 
ATOM   4966  C CE2 . PHE C  1 156 ? -5.235  -0.583  96.714  1.00 36.32  ? 161 PHE C CE2 1 
ATOM   4967  C CZ  . PHE C  1 156 ? -4.510  -1.751  96.499  1.00 36.20  ? 161 PHE C CZ  1 
ATOM   4968  N N   . PRO C  1 157 ? -6.445  0.998   100.751 1.00 32.11  ? 162 PRO C N   1 
ATOM   4969  C CA  . PRO C  1 157 ? -6.367  2.457   100.791 1.00 32.25  ? 162 PRO C CA  1 
ATOM   4970  C C   . PRO C  1 157 ? -6.333  3.088   99.402  1.00 32.11  ? 162 PRO C C   1 
ATOM   4971  O O   . PRO C  1 157 ? -5.707  2.543   98.487  1.00 32.05  ? 162 PRO C O   1 
ATOM   4972  C CB  . PRO C  1 157 ? -5.053  2.719   101.535 1.00 32.38  ? 162 PRO C CB  1 
ATOM   4973  C CG  . PRO C  1 157 ? -4.211  1.531   101.247 1.00 32.55  ? 162 PRO C CG  1 
ATOM   4974  C CD  . PRO C  1 157 ? -5.144  0.365   101.041 1.00 32.35  ? 162 PRO C CD  1 
ATOM   4975  N N   . GLN C  1 158 ? -7.015  4.226   99.261  1.00 32.11  ? 163 GLN C N   1 
ATOM   4976  C CA  . GLN C  1 158 ? -7.001  5.006   98.026  1.00 32.15  ? 163 GLN C CA  1 
ATOM   4977  C C   . GLN C  1 158 ? -5.561  5.370   97.667  1.00 31.98  ? 163 GLN C C   1 
ATOM   4978  O O   . GLN C  1 158 ? -4.826  5.923   98.487  1.00 32.09  ? 163 GLN C O   1 
ATOM   4979  C CB  . GLN C  1 158 ? -7.868  6.262   98.169  1.00 32.28  ? 163 GLN C CB  1 
ATOM   4980  C CG  . GLN C  1 158 ? -8.055  7.070   96.882  1.00 33.02  ? 163 GLN C CG  1 
ATOM   4981  C CD  . GLN C  1 158 ? -8.859  6.332   95.823  1.00 33.44  ? 163 GLN C CD  1 
ATOM   4982  O OE1 . GLN C  1 158 ? -9.933  5.795   96.099  1.00 33.88  ? 163 GLN C OE1 1 
ATOM   4983  N NE2 . GLN C  1 158 ? -8.342  6.310   94.600  1.00 33.99  ? 163 GLN C NE2 1 
ATOM   4984  N N   . MET C  1 159 ? -5.170  5.045   96.440  1.00 31.81  ? 164 MET C N   1 
ATOM   4985  C CA  . MET C  1 159 ? -3.773  5.085   96.038  1.00 31.74  ? 164 MET C CA  1 
ATOM   4986  C C   . MET C  1 159 ? -3.592  5.825   94.722  1.00 31.49  ? 164 MET C C   1 
ATOM   4987  O O   . MET C  1 159 ? -4.494  5.839   93.882  1.00 32.00  ? 164 MET C O   1 
ATOM   4988  C CB  . MET C  1 159 ? -3.260  3.656   95.897  1.00 31.83  ? 164 MET C CB  1 
ATOM   4989  C CG  . MET C  1 159 ? -1.841  3.455   96.357  1.00 33.19  ? 164 MET C CG  1 
ATOM   4990  S SD  . MET C  1 159 ? -1.540  1.719   96.718  1.00 35.61  ? 164 MET C SD  1 
ATOM   4991  C CE  . MET C  1 159 ? 0.029   1.836   97.581  1.00 37.89  ? 164 MET C CE  1 
ATOM   4992  N N   . THR C  1 160 ? -2.426  6.441   94.546  1.00 30.92  ? 165 THR C N   1 
ATOM   4993  C CA  . THR C  1 160 ? -2.100  7.123   93.296  1.00 30.70  ? 165 THR C CA  1 
ATOM   4994  C C   . THR C  1 160 ? -0.670  6.799   92.846  1.00 30.34  ? 165 THR C C   1 
ATOM   4995  O O   . THR C  1 160 ? 0.298   7.148   93.526  1.00 30.70  ? 165 THR C O   1 
ATOM   4996  C CB  . THR C  1 160 ? -2.315  8.657   93.399  1.00 30.79  ? 165 THR C CB  1 
ATOM   4997  O OG1 . THR C  1 160 ? -3.616  8.930   93.935  1.00 31.30  ? 165 THR C OG1 1 
ATOM   4998  C CG2 . THR C  1 160 ? -2.201  9.314   92.030  1.00 31.15  ? 165 THR C CG2 1 
ATOM   4999  N N   . LYS C  1 161 ? -0.555  6.117   91.706  1.00 29.67  ? 166 LYS C N   1 
ATOM   5000  C CA  . LYS C  1 161 ? 0.747   5.802   91.107  1.00 29.00  ? 166 LYS C CA  1 
ATOM   5001  C C   . LYS C  1 161 ? 0.852   6.422   89.716  1.00 28.44  ? 166 LYS C C   1 
ATOM   5002  O O   . LYS C  1 161 ? -0.021  6.217   88.870  1.00 28.46  ? 166 LYS C O   1 
ATOM   5003  C CB  . LYS C  1 161 ? 0.981   4.284   91.040  1.00 28.60  ? 166 LYS C CB  1 
ATOM   5004  C CG  . LYS C  1 161 ? 0.958   3.558   92.388  1.00 29.11  ? 166 LYS C CG  1 
ATOM   5005  C CD  . LYS C  1 161 ? 2.101   3.996   93.303  1.00 31.41  ? 166 LYS C CD  1 
ATOM   5006  C CE  . LYS C  1 161 ? 1.981   3.365   94.682  1.00 31.41  ? 166 LYS C CE  1 
ATOM   5007  N NZ  . LYS C  1 161 ? 2.992   3.898   95.635  1.00 29.75  ? 166 LYS C NZ  1 
ATOM   5008  N N   . ALA C  1 162 ? 1.920   7.185   89.490  1.00 27.95  ? 167 ALA C N   1 
ATOM   5009  C CA  . ALA C  1 162 ? 2.106   7.904   88.231  1.00 27.40  ? 167 ALA C CA  1 
ATOM   5010  C C   . ALA C  1 162 ? 3.438   7.586   87.557  1.00 26.99  ? 167 ALA C C   1 
ATOM   5011  O O   . ALA C  1 162 ? 4.454   7.387   88.229  1.00 26.69  ? 167 ALA C O   1 
ATOM   5012  C CB  . ALA C  1 162 ? 1.958   9.406   88.447  1.00 27.54  ? 167 ALA C CB  1 
ATOM   5013  N N   . TYR C  1 163 ? 3.419   7.548   86.227  1.00 26.84  ? 168 TYR C N   1 
ATOM   5014  C CA  . TYR C  1 163 ? 4.609   7.244   85.434  1.00 26.85  ? 168 TYR C CA  1 
ATOM   5015  C C   . TYR C  1 163 ? 4.788   8.207   84.261  1.00 27.26  ? 168 TYR C C   1 
ATOM   5016  O O   . TYR C  1 163 ? 3.914   8.318   83.398  1.00 26.94  ? 168 TYR C O   1 
ATOM   5017  C CB  . TYR C  1 163 ? 4.567   5.795   84.933  1.00 26.34  ? 168 TYR C CB  1 
ATOM   5018  C CG  . TYR C  1 163 ? 5.675   5.433   83.962  1.00 26.12  ? 168 TYR C CG  1 
ATOM   5019  C CD1 . TYR C  1 163 ? 6.972   5.174   84.414  1.00 26.37  ? 168 TYR C CD1 1 
ATOM   5020  C CD2 . TYR C  1 163 ? 5.425   5.341   82.593  1.00 24.06  ? 168 TYR C CD2 1 
ATOM   5021  C CE1 . TYR C  1 163 ? 7.992   4.841   83.524  1.00 25.38  ? 168 TYR C CE1 1 
ATOM   5022  C CE2 . TYR C  1 163 ? 6.435   5.010   81.698  1.00 24.07  ? 168 TYR C CE2 1 
ATOM   5023  C CZ  . TYR C  1 163 ? 7.714   4.760   82.168  1.00 25.69  ? 168 TYR C CZ  1 
ATOM   5024  O OH  . TYR C  1 163 ? 8.712   4.426   81.280  1.00 25.74  ? 168 TYR C OH  1 
ATOM   5025  N N   . ARG C  1 164 ? 5.929   8.892   84.240  1.00 27.85  ? 169 ARG C N   1 
ATOM   5026  C CA  . ARG C  1 164 ? 6.287   9.777   83.132  1.00 28.55  ? 169 ARG C CA  1 
ATOM   5027  C C   . ARG C  1 164 ? 7.196   9.040   82.148  1.00 28.50  ? 169 ARG C C   1 
ATOM   5028  O O   . ARG C  1 164 ? 8.144   8.368   82.560  1.00 28.57  ? 169 ARG C O   1 
ATOM   5029  C CB  . ARG C  1 164 ? 6.976   11.043  83.654  1.00 28.75  ? 169 ARG C CB  1 
ATOM   5030  C CG  . ARG C  1 164 ? 7.158   12.144  82.611  1.00 30.29  ? 169 ARG C CG  1 
ATOM   5031  C CD  . ARG C  1 164 ? 8.003   13.298  83.145  1.00 34.03  ? 169 ARG C CD  1 
ATOM   5032  N NE  . ARG C  1 164 ? 9.410   12.930  83.316  1.00 35.67  ? 169 ARG C NE  1 
ATOM   5033  C CZ  . ARG C  1 164 ? 10.351  13.071  82.383  1.00 36.33  ? 169 ARG C CZ  1 
ATOM   5034  N NH1 . ARG C  1 164 ? 10.053  13.578  81.192  1.00 36.30  ? 169 ARG C NH1 1 
ATOM   5035  N NH2 . ARG C  1 164 ? 11.598  12.703  82.644  1.00 35.75  ? 169 ARG C NH2 1 
ATOM   5036  N N   . ASN C  1 165 ? 6.897   9.170   80.857  1.00 28.50  ? 170 ASN C N   1 
ATOM   5037  C CA  . ASN C  1 165 ? 7.675   8.519   79.798  1.00 28.79  ? 170 ASN C CA  1 
ATOM   5038  C C   . ASN C  1 165 ? 9.010   9.223   79.536  1.00 28.92  ? 170 ASN C C   1 
ATOM   5039  O O   . ASN C  1 165 ? 9.035   10.306  78.942  1.00 29.05  ? 170 ASN C O   1 
ATOM   5040  C CB  . ASN C  1 165 ? 6.852   8.427   78.505  1.00 28.71  ? 170 ASN C CB  1 
ATOM   5041  C CG  . ASN C  1 165 ? 7.588   7.705   77.376  1.00 29.27  ? 170 ASN C CG  1 
ATOM   5042  O OD1 . ASN C  1 165 ? 8.691   7.181   77.556  1.00 29.27  ? 170 ASN C OD1 1 
ATOM   5043  N ND2 . ASN C  1 165 ? 6.968   7.674   76.202  1.00 29.05  ? 170 ASN C ND2 1 
ATOM   5044  N N   . PRO C  1 166 ? 10.126  8.597   79.962  1.00 29.07  ? 171 PRO C N   1 
ATOM   5045  C CA  . PRO C  1 166 ? 11.444  9.215   79.830  1.00 29.47  ? 171 PRO C CA  1 
ATOM   5046  C C   . PRO C  1 166 ? 12.006  9.138   78.409  1.00 29.71  ? 171 PRO C C   1 
ATOM   5047  O O   . PRO C  1 166 ? 12.696  10.059  77.969  1.00 29.74  ? 171 PRO C O   1 
ATOM   5048  C CB  . PRO C  1 166 ? 12.321  8.397   80.795  1.00 29.61  ? 171 PRO C CB  1 
ATOM   5049  C CG  . PRO C  1 166 ? 11.420  7.345   81.408  1.00 29.16  ? 171 PRO C CG  1 
ATOM   5050  C CD  . PRO C  1 166 ? 10.222  7.244   80.534  1.00 28.93  ? 171 PRO C CD  1 
ATOM   5051  N N   . ARG C  1 167 ? 11.700  8.052   77.703  1.00 30.10  ? 172 ARG C N   1 
ATOM   5052  C CA  . ARG C  1 167 ? 12.233  7.803   76.362  1.00 30.61  ? 172 ARG C CA  1 
ATOM   5053  C C   . ARG C  1 167 ? 11.656  8.768   75.324  1.00 30.72  ? 172 ARG C C   1 
ATOM   5054  O O   . ARG C  1 167 ? 10.752  9.555   75.623  1.00 30.64  ? 172 ARG C O   1 
ATOM   5055  C CB  . ARG C  1 167 ? 11.977  6.348   75.949  1.00 30.54  ? 172 ARG C CB  1 
ATOM   5056  C CG  . ARG C  1 167 ? 12.619  5.304   76.867  1.00 32.36  ? 172 ARG C CG  1 
ATOM   5057  C CD  . ARG C  1 167 ? 13.979  4.833   76.355  1.00 37.13  ? 172 ARG C CD  1 
ATOM   5058  N NE  . ARG C  1 167 ? 13.851  3.997   75.160  1.00 39.94  ? 172 ARG C NE  1 
ATOM   5059  C CZ  . ARG C  1 167 ? 13.649  2.680   75.171  1.00 40.41  ? 172 ARG C CZ  1 
ATOM   5060  N NH1 . ARG C  1 167 ? 13.553  2.019   76.320  1.00 39.52  ? 172 ARG C NH1 1 
ATOM   5061  N NH2 . ARG C  1 167 ? 13.541  2.022   74.025  1.00 41.57  ? 172 ARG C NH2 1 
ATOM   5062  N N   . ASN C  1 168 ? 12.193  8.705   74.107  1.00 31.07  ? 173 ASN C N   1 
ATOM   5063  C CA  . ASN C  1 168 ? 11.778  9.601   73.029  1.00 31.25  ? 173 ASN C CA  1 
ATOM   5064  C C   . ASN C  1 168 ? 10.831  8.929   72.031  1.00 30.57  ? 173 ASN C C   1 
ATOM   5065  O O   . ASN C  1 168 ? 10.646  9.405   70.907  1.00 30.26  ? 173 ASN C O   1 
ATOM   5066  C CB  . ASN C  1 168 ? 13.006  10.201  72.328  1.00 31.76  ? 173 ASN C CB  1 
ATOM   5067  C CG  . ASN C  1 168 ? 13.863  11.045  73.268  1.00 33.43  ? 173 ASN C CG  1 
ATOM   5068  O OD1 . ASN C  1 168 ? 14.410  10.543  74.253  1.00 34.90  ? 173 ASN C OD1 1 
ATOM   5069  N ND2 . ASN C  1 168 ? 13.982  12.334  72.962  1.00 34.84  ? 173 ASN C ND2 1 
ATOM   5070  N N   . LYS C  1 169 ? 10.233  7.822   72.464  1.00 30.00  ? 174 LYS C N   1 
ATOM   5071  C CA  . LYS C  1 169 ? 9.233   7.090   71.682  1.00 29.34  ? 174 LYS C CA  1 
ATOM   5072  C C   . LYS C  1 169 ? 8.123   6.562   72.606  1.00 28.10  ? 174 LYS C C   1 
ATOM   5073  O O   . LYS C  1 169 ? 8.381   6.291   73.782  1.00 28.15  ? 174 LYS C O   1 
ATOM   5074  C CB  . LYS C  1 169 ? 9.892   5.968   70.861  1.00 29.50  ? 174 LYS C CB  1 
ATOM   5075  C CG  . LYS C  1 169 ? 10.749  4.979   71.660  1.00 32.19  ? 174 LYS C CG  1 
ATOM   5076  C CD  . LYS C  1 169 ? 11.910  4.416   70.833  1.00 35.04  ? 174 LYS C CD  1 
ATOM   5077  C CE  . LYS C  1 169 ? 11.432  3.606   69.631  1.00 37.03  ? 174 LYS C CE  1 
ATOM   5078  N NZ  . LYS C  1 169 ? 12.562  2.982   68.883  1.00 37.49  ? 174 LYS C NZ  1 
ATOM   5079  N N   . PRO C  1 170 ? 6.887   6.421   72.081  1.00 27.09  ? 175 PRO C N   1 
ATOM   5080  C CA  . PRO C  1 170 ? 5.717   6.105   72.918  1.00 26.27  ? 175 PRO C CA  1 
ATOM   5081  C C   . PRO C  1 170 ? 5.830   4.806   73.724  1.00 25.57  ? 175 PRO C C   1 
ATOM   5082  O O   . PRO C  1 170 ? 6.444   3.838   73.268  1.00 25.67  ? 175 PRO C O   1 
ATOM   5083  C CB  . PRO C  1 170 ? 4.569   6.006   71.903  1.00 26.30  ? 175 PRO C CB  1 
ATOM   5084  C CG  . PRO C  1 170 ? 5.232   5.767   70.588  1.00 26.65  ? 175 PRO C CG  1 
ATOM   5085  C CD  . PRO C  1 170 ? 6.518   6.524   70.657  1.00 26.95  ? 175 PRO C CD  1 
ATOM   5086  N N   . ALA C  1 171 ? 5.232   4.803   74.913  1.00 24.46  ? 176 ALA C N   1 
ATOM   5087  C CA  . ALA C  1 171 ? 5.242   3.644   75.801  1.00 23.21  ? 176 ALA C CA  1 
ATOM   5088  C C   . ALA C  1 171 ? 3.873   2.985   75.847  1.00 22.45  ? 176 ALA C C   1 
ATOM   5089  O O   . ALA C  1 171 ? 2.855   3.669   75.983  1.00 22.68  ? 176 ALA C O   1 
ATOM   5090  C CB  . ALA C  1 171 ? 5.667   4.058   77.200  1.00 23.20  ? 176 ALA C CB  1 
ATOM   5091  N N   . LEU C  1 172 ? 3.849   1.659   75.737  1.00 21.20  ? 177 LEU C N   1 
ATOM   5092  C CA  . LEU C  1 172 ? 2.600   0.913   75.848  1.00 20.17  ? 177 LEU C CA  1 
ATOM   5093  C C   . LEU C  1 172 ? 2.313   0.558   77.303  1.00 19.86  ? 177 LEU C C   1 
ATOM   5094  O O   . LEU C  1 172 ? 3.033   -0.236  77.913  1.00 20.40  ? 177 LEU C O   1 
ATOM   5095  C CB  . LEU C  1 172 ? 2.619   -0.344  74.970  1.00 19.84  ? 177 LEU C CB  1 
ATOM   5096  C CG  . LEU C  1 172 ? 1.331   -1.178  74.906  1.00 18.78  ? 177 LEU C CG  1 
ATOM   5097  C CD1 . LEU C  1 172 ? 0.183   -0.404  74.268  1.00 20.56  ? 177 LEU C CD1 1 
ATOM   5098  C CD2 . LEU C  1 172 ? 1.576   -2.460  74.148  1.00 18.55  ? 177 LEU C CD2 1 
ATOM   5099  N N   . ILE C  1 173 ? 1.259   1.158   77.850  1.00 19.26  ? 178 ILE C N   1 
ATOM   5100  C CA  . ILE C  1 173 ? 0.861   0.918   79.235  1.00 18.38  ? 178 ILE C CA  1 
ATOM   5101  C C   . ILE C  1 173 ? -0.295  -0.080  79.297  1.00 18.26  ? 178 ILE C C   1 
ATOM   5102  O O   . ILE C  1 173 ? -1.315  0.107   78.629  1.00 18.15  ? 178 ILE C O   1 
ATOM   5103  C CB  . ILE C  1 173 ? 0.451   2.232   79.949  1.00 18.01  ? 178 ILE C CB  1 
ATOM   5104  C CG1 . ILE C  1 173 ? 1.383   3.394   79.563  1.00 18.40  ? 178 ILE C CG1 1 
ATOM   5105  C CG2 . ILE C  1 173 ? 0.378   2.023   81.463  1.00 16.86  ? 178 ILE C CG2 1 
ATOM   5106  C CD1 . ILE C  1 173 ? 2.794   3.340   80.160  1.00 18.51  ? 178 ILE C CD1 1 
ATOM   5107  N N   . ILE C  1 174 ? -0.120  -1.136  80.094  1.00 17.56  ? 179 ILE C N   1 
ATOM   5108  C CA  . ILE C  1 174 ? -1.166  -2.139  80.319  1.00 17.36  ? 179 ILE C CA  1 
ATOM   5109  C C   . ILE C  1 174 ? -1.573  -2.150  81.790  1.00 17.18  ? 179 ILE C C   1 
ATOM   5110  O O   . ILE C  1 174 ? -0.739  -1.935  82.667  1.00 17.24  ? 179 ILE C O   1 
ATOM   5111  C CB  . ILE C  1 174 ? -0.698  -3.575  79.940  1.00 17.54  ? 179 ILE C CB  1 
ATOM   5112  C CG1 . ILE C  1 174 ? 0.158   -3.583  78.661  1.00 19.11  ? 179 ILE C CG1 1 
ATOM   5113  C CG2 . ILE C  1 174 ? -1.890  -4.540  79.847  1.00 15.94  ? 179 ILE C CG2 1 
ATOM   5114  C CD1 . ILE C  1 174 ? -0.608  -3.399  77.357  1.00 21.04  ? 179 ILE C CD1 1 
ATOM   5115  N N   . TRP C  1 175 ? -2.856  -2.396  82.053  1.00 16.73  ? 180 TRP C N   1 
ATOM   5116  C CA  . TRP C  1 175 ? -3.353  -2.606  83.413  1.00 16.67  ? 180 TRP C CA  1 
ATOM   5117  C C   . TRP C  1 175 ? -4.528  -3.572  83.402  1.00 17.08  ? 180 TRP C C   1 
ATOM   5118  O O   . TRP C  1 175 ? -5.193  -3.737  82.380  1.00 17.57  ? 180 TRP C O   1 
ATOM   5119  C CB  . TRP C  1 175 ? -3.754  -1.282  84.076  1.00 16.81  ? 180 TRP C CB  1 
ATOM   5120  C CG  . TRP C  1 175 ? -4.931  -0.606  83.440  1.00 15.20  ? 180 TRP C CG  1 
ATOM   5121  C CD1 . TRP C  1 175 ? -6.238  -0.696  83.829  1.00 16.15  ? 180 TRP C CD1 1 
ATOM   5122  C CD2 . TRP C  1 175 ? -4.907  0.266   82.307  1.00 13.78  ? 180 TRP C CD2 1 
ATOM   5123  N NE1 . TRP C  1 175 ? -7.032  0.064   83.003  1.00 15.18  ? 180 TRP C NE1 1 
ATOM   5124  C CE2 . TRP C  1 175 ? -6.240  0.665   82.059  1.00 14.70  ? 180 TRP C CE2 1 
ATOM   5125  C CE3 . TRP C  1 175 ? -3.889  0.749   81.474  1.00 14.58  ? 180 TRP C CE3 1 
ATOM   5126  C CZ2 . TRP C  1 175 ? -6.584  1.528   81.012  1.00 14.50  ? 180 TRP C CZ2 1 
ATOM   5127  C CZ3 . TRP C  1 175 ? -4.231  1.605   80.430  1.00 16.83  ? 180 TRP C CZ3 1 
ATOM   5128  C CH2 . TRP C  1 175 ? -5.569  1.984   80.209  1.00 15.46  ? 180 TRP C CH2 1 
ATOM   5129  N N   . GLY C  1 176 ? -4.786  -4.200  84.542  1.00 17.37  ? 181 GLY C N   1 
ATOM   5130  C CA  . GLY C  1 176 ? -5.836  -5.204  84.632  1.00 18.00  ? 181 GLY C CA  1 
ATOM   5131  C C   . GLY C  1 176 ? -6.903  -4.883  85.655  1.00 18.70  ? 181 GLY C C   1 
ATOM   5132  O O   . GLY C  1 176 ? -6.623  -4.290  86.700  1.00 19.02  ? 181 GLY C O   1 
ATOM   5133  N N   . VAL C  1 177 ? -8.134  -5.278  85.341  1.00 19.14  ? 182 VAL C N   1 
ATOM   5134  C CA  . VAL C  1 177 ? -9.263  -5.142  86.255  1.00 19.14  ? 182 VAL C CA  1 
ATOM   5135  C C   . VAL C  1 177 ? -9.713  -6.543  86.662  1.00 19.70  ? 182 VAL C C   1 
ATOM   5136  O O   . VAL C  1 177 ? -10.214 -7.304  85.834  1.00 19.34  ? 182 VAL C O   1 
ATOM   5137  C CB  . VAL C  1 177 ? -10.443 -4.372  85.604  1.00 18.85  ? 182 VAL C CB  1 
ATOM   5138  C CG1 . VAL C  1 177 ? -11.615 -4.248  86.574  1.00 18.04  ? 182 VAL C CG1 1 
ATOM   5139  C CG2 . VAL C  1 177 ? -9.995  -2.996  85.127  1.00 17.69  ? 182 VAL C CG2 1 
ATOM   5140  N N   . HIS C  1 178 ? -9.519  -6.885  87.932  1.00 21.06  ? 183 HIS C N   1 
ATOM   5141  C CA  . HIS C  1 178 ? -9.935  -8.193  88.424  1.00 22.55  ? 183 HIS C CA  1 
ATOM   5142  C C   . HIS C  1 178 ? -11.399 -8.211  88.844  1.00 23.52  ? 183 HIS C C   1 
ATOM   5143  O O   . HIS C  1 178 ? -11.784 -7.595  89.841  1.00 23.30  ? 183 HIS C O   1 
ATOM   5144  C CB  . HIS C  1 178 ? -9.046  -8.682  89.571  1.00 22.82  ? 183 HIS C CB  1 
ATOM   5145  C CG  . HIS C  1 178 ? -9.546  -9.937  90.219  1.00 24.03  ? 183 HIS C CG  1 
ATOM   5146  N ND1 . HIS C  1 178 ? -10.116 -9.950  91.475  1.00 25.36  ? 183 HIS C ND1 1 
ATOM   5147  C CD2 . HIS C  1 178 ? -9.590  -11.215 89.772  1.00 25.34  ? 183 HIS C CD2 1 
ATOM   5148  C CE1 . HIS C  1 178 ? -10.476 -11.185 91.778  1.00 26.43  ? 183 HIS C CE1 1 
ATOM   5149  N NE2 . HIS C  1 178 ? -10.167 -11.971 90.762  1.00 27.57  ? 183 HIS C NE2 1 
ATOM   5150  N N   . HIS C  1 179 ? -12.205 -8.920  88.062  1.00 25.23  ? 184 HIS C N   1 
ATOM   5151  C CA  . HIS C  1 179 ? -13.597 -9.178  88.399  1.00 26.70  ? 184 HIS C CA  1 
ATOM   5152  C C   . HIS C  1 179 ? -13.637 -10.441 89.257  1.00 27.71  ? 184 HIS C C   1 
ATOM   5153  O O   . HIS C  1 179 ? -13.251 -11.521 88.803  1.00 27.92  ? 184 HIS C O   1 
ATOM   5154  C CB  . HIS C  1 179 ? -14.442 -9.351  87.129  1.00 26.55  ? 184 HIS C CB  1 
ATOM   5155  C CG  . HIS C  1 179 ? -14.305 -8.225  86.147  1.00 26.75  ? 184 HIS C CG  1 
ATOM   5156  N ND1 . HIS C  1 179 ? -15.166 -7.149  86.121  1.00 27.63  ? 184 HIS C ND1 1 
ATOM   5157  C CD2 . HIS C  1 179 ? -13.408 -8.011  85.154  1.00 26.91  ? 184 HIS C CD2 1 
ATOM   5158  C CE1 . HIS C  1 179 ? -14.805 -6.319  85.158  1.00 26.63  ? 184 HIS C CE1 1 
ATOM   5159  N NE2 . HIS C  1 179 ? -13.741 -6.819  84.556  1.00 26.07  ? 184 HIS C NE2 1 
ATOM   5160  N N   . SER C  1 180 ? -14.086 -10.295 90.501  1.00 29.07  ? 185 SER C N   1 
ATOM   5161  C CA  . SER C  1 180 ? -14.075 -11.395 91.471  1.00 30.65  ? 185 SER C CA  1 
ATOM   5162  C C   . SER C  1 180 ? -15.126 -12.469 91.174  1.00 31.45  ? 185 SER C C   1 
ATOM   5163  O O   . SER C  1 180 ? -16.000 -12.276 90.324  1.00 31.51  ? 185 SER C O   1 
ATOM   5164  C CB  . SER C  1 180 ? -14.243 -10.850 92.890  1.00 30.68  ? 185 SER C CB  1 
ATOM   5165  O OG  . SER C  1 180 ? -13.210 -9.930  93.195  1.00 32.00  ? 185 SER C OG  1 
ATOM   5166  N N   . GLU C  1 181 ? -15.028 -13.599 91.875  1.00 32.33  ? 186 GLU C N   1 
ATOM   5167  C CA  . GLU C  1 181 ? -15.941 -14.724 91.668  1.00 33.26  ? 186 GLU C CA  1 
ATOM   5168  C C   . GLU C  1 181 ? -17.345 -14.440 92.206  1.00 34.02  ? 186 GLU C C   1 
ATOM   5169  O O   . GLU C  1 181 ? -18.338 -14.770 91.558  1.00 34.13  ? 186 GLU C O   1 
ATOM   5170  C CB  . GLU C  1 181 ? -15.367 -16.015 92.272  1.00 33.22  ? 186 GLU C CB  1 
ATOM   5171  C CG  . GLU C  1 181 ? -16.266 -17.258 92.142  1.00 34.42  ? 186 GLU C CG  1 
ATOM   5172  C CD  . GLU C  1 181 ? -16.702 -17.555 90.707  1.00 36.56  ? 186 GLU C CD  1 
ATOM   5173  O OE1 . GLU C  1 181 ? -15.839 -17.593 89.804  1.00 37.07  ? 186 GLU C OE1 1 
ATOM   5174  O OE2 . GLU C  1 181 ? -17.914 -17.764 90.483  1.00 36.40  ? 186 GLU C OE2 1 
ATOM   5175  N N   . SER C  1 182 ? -17.420 -13.837 93.390  1.00 34.91  ? 187 SER C N   1 
ATOM   5176  C CA  . SER C  1 182 ? -18.700 -13.463 93.991  1.00 35.27  ? 187 SER C CA  1 
ATOM   5177  C C   . SER C  1 182 ? -18.594 -12.134 94.736  1.00 35.82  ? 187 SER C C   1 
ATOM   5178  O O   . SER C  1 182 ? -17.501 -11.577 94.876  1.00 35.81  ? 187 SER C O   1 
ATOM   5179  C CB  . SER C  1 182 ? -19.216 -14.573 94.915  1.00 35.15  ? 187 SER C CB  1 
ATOM   5180  O OG  . SER C  1 182 ? -18.261 -14.909 95.903  1.00 34.61  ? 187 SER C OG  1 
ATOM   5181  N N   . VAL C  1 183 ? -19.739 -11.635 95.204  1.00 36.31  ? 188 VAL C N   1 
ATOM   5182  C CA  . VAL C  1 183 ? -19.828 -10.345 95.896  1.00 36.88  ? 188 VAL C CA  1 
ATOM   5183  C C   . VAL C  1 183 ? -18.908 -10.274 97.128  1.00 37.24  ? 188 VAL C C   1 
ATOM   5184  O O   . VAL C  1 183 ? -18.232 -9.264  97.345  1.00 37.48  ? 188 VAL C O   1 
ATOM   5185  C CB  . VAL C  1 183 ? -21.307 -10.005 96.273  1.00 37.23  ? 188 VAL C CB  1 
ATOM   5186  C CG1 . VAL C  1 183 ? -21.405 -8.670  97.018  1.00 36.81  ? 188 VAL C CG1 1 
ATOM   5187  C CG2 . VAL C  1 183 ? -22.190 -9.981  95.022  1.00 37.17  ? 188 VAL C CG2 1 
ATOM   5188  N N   . SER C  1 184 ? -18.869 -11.352 97.912  1.00 37.24  ? 189 SER C N   1 
ATOM   5189  C CA  . SER C  1 184 ? -18.048 -11.400 99.128  1.00 37.26  ? 189 SER C CA  1 
ATOM   5190  C C   . SER C  1 184 ? -16.588 -11.797 98.866  1.00 37.20  ? 189 SER C C   1 
ATOM   5191  O O   . SER C  1 184 ? -15.742 -11.683 99.757  1.00 37.04  ? 189 SER C O   1 
ATOM   5192  C CB  . SER C  1 184 ? -18.679 -12.323 100.176 1.00 37.12  ? 189 SER C CB  1 
ATOM   5193  O OG  . SER C  1 184 ? -18.708 -13.664 99.720  1.00 37.76  ? 189 SER C OG  1 
ATOM   5194  N N   . GLU C  1 185 ? -16.302 -12.265 97.652  1.00 37.39  ? 190 GLU C N   1 
ATOM   5195  C CA  . GLU C  1 185 ? -14.926 -12.546 97.231  1.00 37.71  ? 190 GLU C CA  1 
ATOM   5196  C C   . GLU C  1 185 ? -14.150 -11.245 97.051  1.00 37.18  ? 190 GLU C C   1 
ATOM   5197  O O   . GLU C  1 185 ? -12.965 -11.164 97.389  1.00 37.09  ? 190 GLU C O   1 
ATOM   5198  C CB  . GLU C  1 185 ? -14.911 -13.353 95.931  1.00 38.09  ? 190 GLU C CB  1 
ATOM   5199  C CG  . GLU C  1 185 ? -15.108 -14.853 96.116  1.00 41.04  ? 190 GLU C CG  1 
ATOM   5200  C CD  . GLU C  1 185 ? -13.802 -15.635 96.112  1.00 44.20  ? 190 GLU C CD  1 
ATOM   5201  O OE1 . GLU C  1 185 ? -13.621 -16.490 97.008  1.00 45.06  ? 190 GLU C OE1 1 
ATOM   5202  O OE2 . GLU C  1 185 ? -12.963 -15.403 95.210  1.00 44.18  ? 190 GLU C OE2 1 
ATOM   5203  N N   . GLN C  1 186 ? -14.837 -10.233 96.523  1.00 36.69  ? 191 GLN C N   1 
ATOM   5204  C CA  . GLN C  1 186 ? -14.274 -8.899  96.326  1.00 36.07  ? 191 GLN C CA  1 
ATOM   5205  C C   . GLN C  1 186 ? -13.896 -8.238  97.654  1.00 35.92  ? 191 GLN C C   1 
ATOM   5206  O O   . GLN C  1 186 ? -12.841 -7.607  97.752  1.00 36.13  ? 191 GLN C O   1 
ATOM   5207  C CB  . GLN C  1 186 ? -15.256 -8.021  95.540  1.00 35.97  ? 191 GLN C CB  1 
ATOM   5208  C CG  . GLN C  1 186 ? -14.714 -6.654  95.135  1.00 35.24  ? 191 GLN C CG  1 
ATOM   5209  C CD  . GLN C  1 186 ? -15.520 -6.010  94.019  1.00 35.30  ? 191 GLN C CD  1 
ATOM   5210  O OE1 . GLN C  1 186 ? -15.678 -6.583  92.938  1.00 35.91  ? 191 GLN C OE1 1 
ATOM   5211  N NE2 . GLN C  1 186 ? -16.022 -4.806  94.271  1.00 33.56  ? 191 GLN C NE2 1 
ATOM   5212  N N   . THR C  1 187 ? -14.750 -8.391  98.669  1.00 35.28  ? 192 THR C N   1 
ATOM   5213  C CA  . THR C  1 187 ? -14.476 -7.834  100.000 1.00 34.40  ? 192 THR C CA  1 
ATOM   5214  C C   . THR C  1 187 ? -13.382 -8.597  100.753 1.00 33.95  ? 192 THR C C   1 
ATOM   5215  O O   . THR C  1 187 ? -12.723 -8.030  101.620 1.00 33.84  ? 192 THR C O   1 
ATOM   5216  C CB  . THR C  1 187 ? -15.752 -7.713  100.885 1.00 34.31  ? 192 THR C CB  1 
ATOM   5217  O OG1 . THR C  1 187 ? -16.357 -9.002  101.061 1.00 34.23  ? 192 THR C OG1 1 
ATOM   5218  C CG2 . THR C  1 187 ? -16.763 -6.751  100.266 1.00 34.69  ? 192 THR C CG2 1 
ATOM   5219  N N   . LYS C  1 188 ? -13.190 -9.874  100.418 1.00 33.60  ? 193 LYS C N   1 
ATOM   5220  C CA  . LYS C  1 188 ? -12.132 -10.688 101.030 1.00 33.36  ? 193 LYS C CA  1 
ATOM   5221  C C   . LYS C  1 188 ? -10.740 -10.278 100.543 1.00 33.18  ? 193 LYS C C   1 
ATOM   5222  O O   . LYS C  1 188 ? -9.778  -10.286 101.315 1.00 33.09  ? 193 LYS C O   1 
ATOM   5223  C CB  . LYS C  1 188 ? -12.366 -12.185 100.778 1.00 33.40  ? 193 LYS C CB  1 
ATOM   5224  C CG  . LYS C  1 188 ? -11.461 -13.108 101.607 1.00 32.18  ? 193 LYS C CG  1 
ATOM   5225  C CD  . LYS C  1 188 ? -11.768 -14.587 101.385 1.00 32.33  ? 193 LYS C CD  1 
ATOM   5226  C CE  . LYS C  1 188 ? -10.982 -15.173 100.212 1.00 33.16  ? 193 LYS C CE  1 
ATOM   5227  N NZ  . LYS C  1 188 ? -11.085 -16.665 100.159 1.00 31.35  ? 193 LYS C NZ  1 
ATOM   5228  N N   . LEU C  1 189 ? -10.643 -9.921  99.265  1.00 32.98  ? 194 LEU C N   1 
ATOM   5229  C CA  . LEU C  1 189 ? -9.372  -9.518  98.669  1.00 33.02  ? 194 LEU C CA  1 
ATOM   5230  C C   . LEU C  1 189 ? -9.058  -8.048  98.938  1.00 32.93  ? 194 LEU C C   1 
ATOM   5231  O O   . LEU C  1 189 ? -7.939  -7.704  99.330  1.00 32.86  ? 194 LEU C O   1 
ATOM   5232  C CB  . LEU C  1 189 ? -9.378  -9.782  97.160  1.00 33.15  ? 194 LEU C CB  1 
ATOM   5233  C CG  . LEU C  1 189 ? -9.566  -11.219 96.666  1.00 33.39  ? 194 LEU C CG  1 
ATOM   5234  C CD1 . LEU C  1 189 ? -9.916  -11.220 95.190  1.00 33.89  ? 194 LEU C CD1 1 
ATOM   5235  C CD2 . LEU C  1 189 ? -8.331  -12.063 96.920  1.00 34.53  ? 194 LEU C CD2 1 
ATOM   5236  N N   . TYR C  1 190 ? -10.057 -7.193  98.728  1.00 32.85  ? 195 TYR C N   1 
ATOM   5237  C CA  . TYR C  1 190 ? -9.896  -5.744  98.837  1.00 32.79  ? 195 TYR C CA  1 
ATOM   5238  C C   . TYR C  1 190 ? -10.820 -5.182  99.929  1.00 33.14  ? 195 TYR C C   1 
ATOM   5239  O O   . TYR C  1 190 ? -11.199 -5.903  100.853 1.00 33.54  ? 195 TYR C O   1 
ATOM   5240  C CB  . TYR C  1 190 ? -10.162 -5.080  97.476  1.00 32.70  ? 195 TYR C CB  1 
ATOM   5241  C CG  . TYR C  1 190 ? -9.702  -5.901  96.283  1.00 31.02  ? 195 TYR C CG  1 
ATOM   5242  C CD1 . TYR C  1 190 ? -10.611 -6.651  95.537  1.00 30.25  ? 195 TYR C CD1 1 
ATOM   5243  C CD2 . TYR C  1 190 ? -8.359  -5.934  95.905  1.00 30.98  ? 195 TYR C CD2 1 
ATOM   5244  C CE1 . TYR C  1 190 ? -10.197 -7.411  94.443  1.00 29.92  ? 195 TYR C CE1 1 
ATOM   5245  C CE2 . TYR C  1 190 ? -7.935  -6.692  94.813  1.00 30.28  ? 195 TYR C CE2 1 
ATOM   5246  C CZ  . TYR C  1 190 ? -8.858  -7.426  94.090  1.00 30.18  ? 195 TYR C CZ  1 
ATOM   5247  O OH  . TYR C  1 190 ? -8.443  -8.172  93.010  1.00 28.70  ? 195 TYR C OH  1 
ATOM   5248  N N   . GLY C  1 191 ? -11.176 -3.903  99.830  1.00 32.72  ? 196 GLY C N   1 
ATOM   5249  C CA  . GLY C  1 191 ? -12.045 -3.277  100.827 1.00 32.60  ? 196 GLY C CA  1 
ATOM   5250  C C   . GLY C  1 191 ? -13.514 -3.619  100.644 1.00 32.21  ? 196 GLY C C   1 
ATOM   5251  O O   . GLY C  1 191 ? -13.868 -4.449  99.801  1.00 32.42  ? 196 GLY C O   1 
ATOM   5252  N N   . SER C  1 192 ? -14.368 -2.981  101.441 1.00 31.34  ? 197 SER C N   1 
ATOM   5253  C CA  . SER C  1 192 ? -15.813 -3.149  101.313 1.00 30.56  ? 197 SER C CA  1 
ATOM   5254  C C   . SER C  1 192 ? -16.388 -2.103  100.359 1.00 30.14  ? 197 SER C C   1 
ATOM   5255  O O   . SER C  1 192 ? -15.784 -1.048  100.146 1.00 30.18  ? 197 SER C O   1 
ATOM   5256  C CB  . SER C  1 192 ? -16.498 -3.068  102.685 1.00 30.76  ? 197 SER C CB  1 
ATOM   5257  O OG  . SER C  1 192 ? -16.537 -1.736  103.180 1.00 29.33  ? 197 SER C OG  1 
ATOM   5258  N N   . GLY C  1 193 ? -17.546 -2.412  99.776  1.00 29.44  ? 198 GLY C N   1 
ATOM   5259  C CA  . GLY C  1 193 ? -18.285 -1.463  98.943  1.00 28.50  ? 198 GLY C CA  1 
ATOM   5260  C C   . GLY C  1 193 ? -17.700 -1.174  97.571  1.00 28.01  ? 198 GLY C C   1 
ATOM   5261  O O   . GLY C  1 193 ? -16.864 -1.928  97.063  1.00 26.91  ? 198 GLY C O   1 
ATOM   5262  N N   . ASN C  1 194 ? -18.151 -0.061  96.988  1.00 28.07  ? 199 ASN C N   1 
ATOM   5263  C CA  . ASN C  1 194 ? -17.824 0.338   95.615  1.00 27.93  ? 199 ASN C CA  1 
ATOM   5264  C C   . ASN C  1 194 ? -16.333 0.466   95.325  1.00 27.12  ? 199 ASN C C   1 
ATOM   5265  O O   . ASN C  1 194 ? -15.596 1.088   96.090  1.00 27.16  ? 199 ASN C O   1 
ATOM   5266  C CB  . ASN C  1 194 ? -18.523 1.660   95.264  1.00 28.32  ? 199 ASN C CB  1 
ATOM   5267  C CG  . ASN C  1 194 ? -20.039 1.535   95.215  1.00 30.15  ? 199 ASN C CG  1 
ATOM   5268  O OD1 . ASN C  1 194 ? -20.587 0.434   95.128  1.00 31.45  ? 199 ASN C OD1 1 
ATOM   5269  N ND2 . ASN C  1 194 ? -20.725 2.675   95.262  1.00 30.58  ? 199 ASN C ND2 1 
ATOM   5270  N N   . LYS C  1 195 ? -15.903 -0.118  94.210  1.00 26.28  ? 200 LYS C N   1 
ATOM   5271  C CA  . LYS C  1 195 ? -14.516 -0.019  93.763  1.00 25.56  ? 200 LYS C CA  1 
ATOM   5272  C C   . LYS C  1 195 ? -14.429 0.759   92.456  1.00 25.88  ? 200 LYS C C   1 
ATOM   5273  O O   . LYS C  1 195 ? -15.331 0.678   91.616  1.00 26.37  ? 200 LYS C O   1 
ATOM   5274  C CB  . LYS C  1 195 ? -13.901 -1.411  93.593  1.00 24.84  ? 200 LYS C CB  1 
ATOM   5275  C CG  . LYS C  1 195 ? -13.772 -2.200  94.887  1.00 23.74  ? 200 LYS C CG  1 
ATOM   5276  C CD  . LYS C  1 195 ? -12.740 -1.576  95.810  1.00 21.40  ? 200 LYS C CD  1 
ATOM   5277  C CE  . LYS C  1 195 ? -12.926 -2.024  97.242  1.00 19.12  ? 200 LYS C CE  1 
ATOM   5278  N NZ  . LYS C  1 195 ? -12.181 -1.129  98.161  1.00 19.09  ? 200 LYS C NZ  1 
ATOM   5279  N N   . LEU C  1 196 ? -13.343 1.514   92.291  1.00 25.64  ? 201 LEU C N   1 
ATOM   5280  C CA  . LEU C  1 196 ? -13.152 2.339   91.096  1.00 25.29  ? 201 LEU C CA  1 
ATOM   5281  C C   . LEU C  1 196 ? -11.678 2.514   90.714  1.00 24.63  ? 201 LEU C C   1 
ATOM   5282  O O   . LEU C  1 196 ? -10.832 2.809   91.564  1.00 24.60  ? 201 LEU C O   1 
ATOM   5283  C CB  . LEU C  1 196 ? -13.851 3.697   91.266  1.00 25.18  ? 201 LEU C CB  1 
ATOM   5284  C CG  . LEU C  1 196 ? -13.824 4.674   90.086  1.00 26.87  ? 201 LEU C CG  1 
ATOM   5285  C CD1 . LEU C  1 196 ? -15.207 5.230   89.791  1.00 28.06  ? 201 LEU C CD1 1 
ATOM   5286  C CD2 . LEU C  1 196 ? -12.827 5.790   90.354  1.00 28.42  ? 201 LEU C CD2 1 
ATOM   5287  N N   . ILE C  1 197 ? -11.394 2.329   89.425  1.00 23.83  ? 202 ILE C N   1 
ATOM   5288  C CA  . ILE C  1 197 ? -10.063 2.551   88.862  1.00 23.70  ? 202 ILE C CA  1 
ATOM   5289  C C   . ILE C  1 197 ? -10.130 3.658   87.808  1.00 24.13  ? 202 ILE C C   1 
ATOM   5290  O O   . ILE C  1 197 ? -10.887 3.553   86.841  1.00 24.11  ? 202 ILE C O   1 
ATOM   5291  C CB  . ILE C  1 197 ? -9.470  1.254   88.218  1.00 23.39  ? 202 ILE C CB  1 
ATOM   5292  C CG1 . ILE C  1 197 ? -9.361  0.115   89.235  1.00 21.64  ? 202 ILE C CG1 1 
ATOM   5293  C CG2 . ILE C  1 197 ? -8.103  1.524   87.597  1.00 22.89  ? 202 ILE C CG2 1 
ATOM   5294  C CD1 . ILE C  1 197 ? -10.503 -0.878  89.180  1.00 20.14  ? 202 ILE C CD1 1 
ATOM   5295  N N   . THR C  1 198 ? -9.345  4.716   88.003  1.00 24.81  ? 203 THR C N   1 
ATOM   5296  C CA  . THR C  1 198 ? -9.254  5.807   87.025  1.00 25.77  ? 203 THR C CA  1 
ATOM   5297  C C   . THR C  1 198 ? -7.860  5.856   86.402  1.00 26.10  ? 203 THR C C   1 
ATOM   5298  O O   . THR C  1 198 ? -6.851  5.873   87.110  1.00 26.88  ? 203 THR C O   1 
ATOM   5299  C CB  . THR C  1 198 ? -9.602  7.188   87.648  1.00 25.56  ? 203 THR C CB  1 
ATOM   5300  O OG1 . THR C  1 198 ? -10.881 7.124   88.285  1.00 26.46  ? 203 THR C OG1 1 
ATOM   5301  C CG2 . THR C  1 198 ? -9.633  8.287   86.588  1.00 25.49  ? 203 THR C CG2 1 
ATOM   5302  N N   . VAL C  1 199 ? -7.819  5.871   85.074  1.00 26.02  ? 204 VAL C N   1 
ATOM   5303  C CA  . VAL C  1 199 ? -6.565  5.962   84.338  1.00 26.51  ? 204 VAL C CA  1 
ATOM   5304  C C   . VAL C  1 199 ? -6.558  7.255   83.517  1.00 27.05  ? 204 VAL C C   1 
ATOM   5305  O O   . VAL C  1 199 ? -7.396  7.443   82.631  1.00 27.00  ? 204 VAL C O   1 
ATOM   5306  C CB  . VAL C  1 199 ? -6.346  4.719   83.430  1.00 26.61  ? 204 VAL C CB  1 
ATOM   5307  C CG1 . VAL C  1 199 ? -4.960  4.740   82.801  1.00 25.67  ? 204 VAL C CG1 1 
ATOM   5308  C CG2 . VAL C  1 199 ? -6.539  3.429   84.224  1.00 26.52  ? 204 VAL C CG2 1 
ATOM   5309  N N   . ARG C  1 200 ? -5.619  8.144   83.830  1.00 27.79  ? 205 ARG C N   1 
ATOM   5310  C CA  . ARG C  1 200 ? -5.522  9.444   83.159  1.00 28.95  ? 205 ARG C CA  1 
ATOM   5311  C C   . ARG C  1 200 ? -4.185  9.691   82.463  1.00 29.40  ? 205 ARG C C   1 
ATOM   5312  O O   . ARG C  1 200 ? -3.144  9.199   82.896  1.00 29.78  ? 205 ARG C O   1 
ATOM   5313  C CB  . ARG C  1 200 ? -5.810  10.587  84.141  1.00 29.12  ? 205 ARG C CB  1 
ATOM   5314  C CG  . ARG C  1 200 ? -7.057  11.390  83.807  1.00 30.73  ? 205 ARG C CG  1 
ATOM   5315  C CD  . ARG C  1 200 ? -7.316  12.519  84.802  1.00 34.30  ? 205 ARG C CD  1 
ATOM   5316  N NE  . ARG C  1 200 ? -7.981  12.058  86.022  1.00 36.43  ? 205 ARG C NE  1 
ATOM   5317  C CZ  . ARG C  1 200 ? -7.429  12.052  87.236  1.00 37.58  ? 205 ARG C CZ  1 
ATOM   5318  N NH1 . ARG C  1 200 ? -6.186  12.486  87.419  1.00 38.09  ? 205 ARG C NH1 1 
ATOM   5319  N NH2 . ARG C  1 200 ? -8.127  11.613  88.276  1.00 36.28  ? 205 ARG C NH2 1 
ATOM   5320  N N   . SER C  1 201 ? -4.241  10.444  81.367  1.00 29.80  ? 206 SER C N   1 
ATOM   5321  C CA  . SER C  1 201 ? -3.060  11.032  80.736  1.00 30.23  ? 206 SER C CA  1 
ATOM   5322  C C   . SER C  1 201 ? -3.450  12.389  80.140  1.00 30.90  ? 206 SER C C   1 
ATOM   5323  O O   . SER C  1 201 ? -4.478  12.955  80.518  1.00 31.04  ? 206 SER C O   1 
ATOM   5324  C CB  . SER C  1 201 ? -2.460  10.092  79.681  1.00 29.93  ? 206 SER C CB  1 
ATOM   5325  O OG  . SER C  1 201 ? -3.326  9.919   78.578  1.00 28.64  ? 206 SER C OG  1 
ATOM   5326  N N   . SER C  1 202 ? -2.637  12.915  79.225  1.00 31.49  ? 207 SER C N   1 
ATOM   5327  C CA  . SER C  1 202 ? -2.949  14.192  78.574  1.00 31.68  ? 207 SER C CA  1 
ATOM   5328  C C   . SER C  1 202 ? -4.024  14.045  77.492  1.00 31.68  ? 207 SER C C   1 
ATOM   5329  O O   . SER C  1 202 ? -4.644  15.033  77.092  1.00 31.48  ? 207 SER C O   1 
ATOM   5330  C CB  . SER C  1 202 ? -1.686  14.848  78.001  1.00 31.61  ? 207 SER C CB  1 
ATOM   5331  O OG  . SER C  1 202 ? -1.166  14.110  76.906  1.00 32.85  ? 207 SER C OG  1 
ATOM   5332  N N   . LYS C  1 203 ? -4.244  12.812  77.032  1.00 31.76  ? 208 LYS C N   1 
ATOM   5333  C CA  . LYS C  1 203 ? -5.230  12.537  75.979  1.00 31.98  ? 208 LYS C CA  1 
ATOM   5334  C C   . LYS C  1 203 ? -6.007  11.225  76.157  1.00 31.64  ? 208 LYS C C   1 
ATOM   5335  O O   . LYS C  1 203 ? -6.519  10.663  75.184  1.00 31.67  ? 208 LYS C O   1 
ATOM   5336  C CB  . LYS C  1 203 ? -4.582  12.607  74.587  1.00 32.36  ? 208 LYS C CB  1 
ATOM   5337  C CG  . LYS C  1 203 ? -3.373  11.693  74.378  1.00 33.03  ? 208 LYS C CG  1 
ATOM   5338  C CD  . LYS C  1 203 ? -2.621  12.052  73.100  1.00 35.02  ? 208 LYS C CD  1 
ATOM   5339  C CE  . LYS C  1 203 ? -1.987  13.441  73.192  1.00 36.55  ? 208 LYS C CE  1 
ATOM   5340  N NZ  . LYS C  1 203 ? -1.236  13.804  71.960  1.00 37.71  ? 208 LYS C NZ  1 
ATOM   5341  N N   . TYR C  1 204 ? -6.104  10.751  77.397  1.00 31.41  ? 209 TYR C N   1 
ATOM   5342  C CA  . TYR C  1 204 ? -6.882  9.551   77.712  1.00 30.80  ? 209 TYR C CA  1 
ATOM   5343  C C   . TYR C  1 204 ? -7.460  9.619   79.121  1.00 30.76  ? 209 TYR C C   1 
ATOM   5344  O O   . TYR C  1 204 ? -6.725  9.839   80.084  1.00 30.70  ? 209 TYR C O   1 
ATOM   5345  C CB  . TYR C  1 204 ? -6.021  8.285   77.553  1.00 30.73  ? 209 TYR C CB  1 
ATOM   5346  C CG  . TYR C  1 204 ? -6.712  6.982   77.929  1.00 29.89  ? 209 TYR C CG  1 
ATOM   5347  C CD1 . TYR C  1 204 ? -7.182  6.110   76.945  1.00 28.89  ? 209 TYR C CD1 1 
ATOM   5348  C CD2 . TYR C  1 204 ? -6.885  6.617   79.270  1.00 28.54  ? 209 TYR C CD2 1 
ATOM   5349  C CE1 . TYR C  1 204 ? -7.816  4.914   77.287  1.00 28.17  ? 209 TYR C CE1 1 
ATOM   5350  C CE2 . TYR C  1 204 ? -7.518  5.427   79.621  1.00 25.28  ? 209 TYR C CE2 1 
ATOM   5351  C CZ  . TYR C  1 204 ? -7.979  4.582   78.627  1.00 25.56  ? 209 TYR C CZ  1 
ATOM   5352  O OH  . TYR C  1 204 ? -8.600  3.404   78.972  1.00 24.34  ? 209 TYR C OH  1 
ATOM   5353  N N   . GLN C  1 205 ? -8.778  9.447   79.229  1.00 30.90  ? 210 GLN C N   1 
ATOM   5354  C CA  . GLN C  1 205 ? -9.402  9.081   80.504  1.00 30.41  ? 210 GLN C CA  1 
ATOM   5355  C C   . GLN C  1 205 ? -10.500 8.039   80.334  1.00 30.16  ? 210 GLN C C   1 
ATOM   5356  O O   . GLN C  1 205 ? -11.249 8.046   79.346  1.00 30.31  ? 210 GLN C O   1 
ATOM   5357  C CB  . GLN C  1 205 ? -9.931  10.283  81.300  1.00 29.91  ? 210 GLN C CB  1 
ATOM   5358  C CG  . GLN C  1 205 ? -9.907  10.004  82.815  1.00 29.02  ? 210 GLN C CG  1 
ATOM   5359  C CD  . GLN C  1 205 ? -11.140 10.476  83.569  1.00 25.77  ? 210 GLN C CD  1 
ATOM   5360  O OE1 . GLN C  1 205 ? -11.388 11.680  83.698  1.00 25.76  ? 210 GLN C OE1 1 
ATOM   5361  N NE2 . GLN C  1 205 ? -11.904 9.523   84.104  1.00 18.37  ? 210 GLN C NE2 1 
ATOM   5362  N N   . GLN C  1 206 ? -10.565 7.140   81.312  1.00 29.18  ? 211 GLN C N   1 
ATOM   5363  C CA  . GLN C  1 206 ? -11.582 6.108   81.392  1.00 28.50  ? 211 GLN C CA  1 
ATOM   5364  C C   . GLN C  1 206 ? -11.566 5.560   82.811  1.00 27.61  ? 211 GLN C C   1 
ATOM   5365  O O   . GLN C  1 206 ? -10.499 5.377   83.402  1.00 27.60  ? 211 GLN C O   1 
ATOM   5366  C CB  . GLN C  1 206 ? -11.305 4.994   80.375  1.00 28.85  ? 211 GLN C CB  1 
ATOM   5367  C CG  . GLN C  1 206 ? -12.270 3.808   80.425  1.00 31.30  ? 211 GLN C CG  1 
ATOM   5368  C CD  . GLN C  1 206 ? -13.598 4.053   79.716  1.00 35.00  ? 211 GLN C CD  1 
ATOM   5369  O OE1 . GLN C  1 206 ? -14.100 5.180   79.648  1.00 32.36  ? 211 GLN C OE1 1 
ATOM   5370  N NE2 . GLN C  1 206 ? -14.180 2.979   79.193  1.00 36.54  ? 211 GLN C NE2 1 
ATOM   5371  N N   . SER C  1 207 ? -12.752 5.321   83.358  1.00 26.85  ? 212 SER C N   1 
ATOM   5372  C CA  . SER C  1 207 ? -12.881 4.714   84.676  1.00 26.12  ? 212 SER C CA  1 
ATOM   5373  C C   . SER C  1 207 ? -13.351 3.269   84.553  1.00 25.43  ? 212 SER C C   1 
ATOM   5374  O O   . SER C  1 207 ? -13.909 2.874   83.525  1.00 24.95  ? 212 SER C O   1 
ATOM   5375  C CB  . SER C  1 207 ? -13.832 5.527   85.554  1.00 26.51  ? 212 SER C CB  1 
ATOM   5376  O OG  . SER C  1 207 ? -13.293 6.812   85.815  1.00 27.26  ? 212 SER C OG  1 
ATOM   5377  N N   . PHE C  1 208 ? -13.106 2.482   85.597  1.00 24.87  ? 213 PHE C N   1 
ATOM   5378  C CA  . PHE C  1 208 ? -13.421 1.057   85.574  1.00 24.67  ? 213 PHE C CA  1 
ATOM   5379  C C   . PHE C  1 208 ? -14.024 0.578   86.884  1.00 24.86  ? 213 PHE C C   1 
ATOM   5380  O O   . PHE C  1 208 ? -13.516 0.887   87.964  1.00 25.01  ? 213 PHE C O   1 
ATOM   5381  C CB  . PHE C  1 208 ? -12.168 0.233   85.258  1.00 24.42  ? 213 PHE C CB  1 
ATOM   5382  C CG  . PHE C  1 208 ? -11.581 0.513   83.907  1.00 22.63  ? 213 PHE C CG  1 
ATOM   5383  C CD1 . PHE C  1 208 ? -10.534 1.418   83.764  1.00 21.82  ? 213 PHE C CD1 1 
ATOM   5384  C CD2 . PHE C  1 208 ? -12.076 -0.124  82.775  1.00 21.31  ? 213 PHE C CD2 1 
ATOM   5385  C CE1 . PHE C  1 208 ? -9.987  1.686   82.513  1.00 21.73  ? 213 PHE C CE1 1 
ATOM   5386  C CE2 . PHE C  1 208 ? -11.534 0.133   81.519  1.00 22.46  ? 213 PHE C CE2 1 
ATOM   5387  C CZ  . PHE C  1 208 ? -10.485 1.038   81.389  1.00 22.07  ? 213 PHE C CZ  1 
ATOM   5388  N N   . THR C  1 209 ? -15.111 -0.179  86.774  1.00 25.10  ? 214 THR C N   1 
ATOM   5389  C CA  . THR C  1 209 ? -15.713 -0.848  87.922  1.00 25.73  ? 214 THR C CA  1 
ATOM   5390  C C   . THR C  1 209 ? -15.613 -2.362  87.739  1.00 26.14  ? 214 THR C C   1 
ATOM   5391  O O   . THR C  1 209 ? -15.723 -2.855  86.613  1.00 26.04  ? 214 THR C O   1 
ATOM   5392  C CB  . THR C  1 209 ? -17.197 -0.444  88.125  1.00 25.80  ? 214 THR C CB  1 
ATOM   5393  O OG1 . THR C  1 209 ? -17.865 -0.394  86.858  1.00 25.16  ? 214 THR C OG1 1 
ATOM   5394  C CG2 . THR C  1 209 ? -17.302 0.920   88.804  1.00 25.59  ? 214 THR C CG2 1 
ATOM   5395  N N   . PRO C  1 210 ? -15.379 -3.102  88.839  1.00 26.78  ? 215 PRO C N   1 
ATOM   5396  C CA  . PRO C  1 210 ? -15.414 -4.563  88.778  1.00 27.58  ? 215 PRO C CA  1 
ATOM   5397  C C   . PRO C  1 210 ? -16.842 -5.110  88.824  1.00 28.86  ? 215 PRO C C   1 
ATOM   5398  O O   . PRO C  1 210 ? -17.690 -4.581  89.548  1.00 29.05  ? 215 PRO C O   1 
ATOM   5399  C CB  . PRO C  1 210 ? -14.647 -4.982  90.032  1.00 27.22  ? 215 PRO C CB  1 
ATOM   5400  C CG  . PRO C  1 210 ? -14.843 -3.867  90.981  1.00 26.71  ? 215 PRO C CG  1 
ATOM   5401  C CD  . PRO C  1 210 ? -14.925 -2.616  90.155  1.00 26.56  ? 215 PRO C CD  1 
ATOM   5402  N N   . ASN C  1 211 ? -17.093 -6.157  88.045  1.00 30.14  ? 216 ASN C N   1 
ATOM   5403  C CA  . ASN C  1 211 ? -18.385 -6.838  88.037  1.00 31.19  ? 216 ASN C CA  1 
ATOM   5404  C C   . ASN C  1 211 ? -18.222 -8.283  88.504  1.00 31.58  ? 216 ASN C C   1 
ATOM   5405  O O   . ASN C  1 211 ? -17.813 -9.146  87.723  1.00 31.69  ? 216 ASN C O   1 
ATOM   5406  C CB  . ASN C  1 211 ? -19.031 -6.781  86.646  1.00 31.47  ? 216 ASN C CB  1 
ATOM   5407  C CG  . ASN C  1 211 ? -19.554 -5.394  86.292  1.00 32.13  ? 216 ASN C CG  1 
ATOM   5408  O OD1 . ASN C  1 211 ? -20.763 -5.171  86.239  1.00 30.80  ? 216 ASN C OD1 1 
ATOM   5409  N ND2 . ASN C  1 211 ? -18.643 -4.456  86.045  1.00 34.06  ? 216 ASN C ND2 1 
ATOM   5410  N N   . PRO C  1 212 ? -18.526 -8.548  89.788  1.00 32.18  ? 217 PRO C N   1 
ATOM   5411  C CA  . PRO C  1 212 ? -18.344 -9.884  90.362  1.00 32.41  ? 217 PRO C CA  1 
ATOM   5412  C C   . PRO C  1 212 ? -19.408 -10.874 89.887  1.00 32.62  ? 217 PRO C C   1 
ATOM   5413  O O   . PRO C  1 212 ? -20.493 -10.460 89.464  1.00 32.94  ? 217 PRO C O   1 
ATOM   5414  C CB  . PRO C  1 212 ? -18.471 -9.638  91.867  1.00 32.19  ? 217 PRO C CB  1 
ATOM   5415  C CG  . PRO C  1 212 ? -19.355 -8.444  91.977  1.00 32.95  ? 217 PRO C CG  1 
ATOM   5416  C CD  . PRO C  1 212 ? -19.079 -7.593  90.769  1.00 32.32  ? 217 PRO C CD  1 
ATOM   5417  N N   . GLY C  1 213 ? -19.087 -12.165 89.956  1.00 32.30  ? 218 GLY C N   1 
ATOM   5418  C CA  . GLY C  1 213 ? -20.002 -13.226 89.530  1.00 31.63  ? 218 GLY C CA  1 
ATOM   5419  C C   . GLY C  1 213 ? -19.330 -14.296 88.684  1.00 31.02  ? 218 GLY C C   1 
ATOM   5420  O O   . GLY C  1 213 ? -19.653 -15.485 88.799  1.00 30.78  ? 218 GLY C O   1 
ATOM   5421  N N   . ALA C  1 214 ? -18.408 -13.878 87.826  1.00 30.48  ? 219 ALA C N   1 
ATOM   5422  C CA  . ALA C  1 214 ? -17.607 -14.808 87.041  1.00 30.16  ? 219 ALA C CA  1 
ATOM   5423  C C   . ALA C  1 214 ? -16.172 -14.324 87.017  1.00 30.10  ? 219 ALA C C   1 
ATOM   5424  O O   . ALA C  1 214 ? -15.865 -13.294 86.415  1.00 29.92  ? 219 ALA C O   1 
ATOM   5425  C CB  . ALA C  1 214 ? -18.144 -14.937 85.640  1.00 30.20  ? 219 ALA C CB  1 
ATOM   5426  N N   . ARG C  1 215 ? -15.303 -15.080 87.684  1.00 29.66  ? 220 ARG C N   1 
ATOM   5427  C CA  . ARG C  1 215 ? -13.915 -14.688 87.873  1.00 28.85  ? 220 ARG C CA  1 
ATOM   5428  C C   . ARG C  1 215 ? -13.175 -14.507 86.563  1.00 27.43  ? 220 ARG C C   1 
ATOM   5429  O O   . ARG C  1 215 ? -13.267 -15.332 85.665  1.00 26.70  ? 220 ARG C O   1 
ATOM   5430  C CB  . ARG C  1 215 ? -13.177 -15.657 88.807  1.00 29.48  ? 220 ARG C CB  1 
ATOM   5431  C CG  . ARG C  1 215 ? -13.082 -17.108 88.355  1.00 32.21  ? 220 ARG C CG  1 
ATOM   5432  C CD  . ARG C  1 215 ? -12.107 -17.903 89.236  1.00 36.89  ? 220 ARG C CD  1 
ATOM   5433  N NE  . ARG C  1 215 ? -12.351 -17.712 90.672  1.00 40.59  ? 220 ARG C NE  1 
ATOM   5434  C CZ  . ARG C  1 215 ? -12.896 -18.619 91.482  1.00 41.43  ? 220 ARG C CZ  1 
ATOM   5435  N NH1 . ARG C  1 215 ? -13.263 -19.810 91.018  1.00 42.41  ? 220 ARG C NH1 1 
ATOM   5436  N NH2 . ARG C  1 215 ? -13.075 -18.333 92.765  1.00 40.97  ? 220 ARG C NH2 1 
ATOM   5437  N N   . ARG C  1 216 ? -12.457 -13.394 86.477  1.00 26.41  ? 229 ARG C N   1 
ATOM   5438  C CA  . ARG C  1 216 ? -11.699 -13.030 85.297  1.00 25.72  ? 229 ARG C CA  1 
ATOM   5439  C C   . ARG C  1 216 ? -10.857 -11.788 85.556  1.00 24.45  ? 229 ARG C C   1 
ATOM   5440  O O   . ARG C  1 216 ? -11.197 -10.962 86.382  1.00 23.88  ? 229 ARG C O   1 
ATOM   5441  C CB  . ARG C  1 216 ? -12.636 -12.783 84.121  1.00 26.09  ? 229 ARG C CB  1 
ATOM   5442  C CG  . ARG C  1 216 ? -13.532 -11.559 84.295  1.00 28.73  ? 229 ARG C CG  1 
ATOM   5443  C CD  . ARG C  1 216 ? -14.688 -11.598 83.328  1.00 32.76  ? 229 ARG C CD  1 
ATOM   5444  N NE  . ARG C  1 216 ? -14.302 -11.096 82.015  1.00 37.54  ? 229 ARG C NE  1 
ATOM   5445  C CZ  . ARG C  1 216 ? -13.984 -11.861 80.977  1.00 38.32  ? 229 ARG C CZ  1 
ATOM   5446  N NH1 . ARG C  1 216 ? -13.995 -13.181 81.084  1.00 39.68  ? 229 ARG C NH1 1 
ATOM   5447  N NH2 . ARG C  1 216 ? -13.654 -11.299 79.827  1.00 38.99  ? 229 ARG C NH2 1 
ATOM   5448  N N   . ILE C  1 217 ? -9.744  -11.681 84.847  1.00 23.47  ? 230 ILE C N   1 
ATOM   5449  C CA  . ILE C  1 217 ? -8.952  -10.455 84.817  1.00 22.70  ? 230 ILE C CA  1 
ATOM   5450  C C   . ILE C  1 217 ? -8.887  -9.938  83.384  1.00 22.06  ? 230 ILE C C   1 
ATOM   5451  O O   . ILE C  1 217 ? -8.293  -10.572 82.510  1.00 22.33  ? 230 ILE C O   1 
ATOM   5452  C CB  . ILE C  1 217 ? -7.520  -10.660 85.372  1.00 22.82  ? 230 ILE C CB  1 
ATOM   5453  C CG1 . ILE C  1 217 ? -7.564  -10.992 86.866  1.00 23.23  ? 230 ILE C CG1 1 
ATOM   5454  C CG2 . ILE C  1 217 ? -6.667  -9.413  85.136  1.00 22.11  ? 230 ILE C CG2 1 
ATOM   5455  C CD1 . ILE C  1 217 ? -6.252  -11.511 87.430  1.00 24.04  ? 230 ILE C CD1 1 
ATOM   5456  N N   . ASP C  1 218 ? -9.515  -8.790  83.151  1.00 21.38  ? 231 ASP C N   1 
ATOM   5457  C CA  . ASP C  1 218 ? -9.512  -8.164  81.836  1.00 20.71  ? 231 ASP C CA  1 
ATOM   5458  C C   . ASP C  1 218 ? -8.417  -7.115  81.757  1.00 19.79  ? 231 ASP C C   1 
ATOM   5459  O O   . ASP C  1 218 ? -8.207  -6.358  82.703  1.00 19.78  ? 231 ASP C O   1 
ATOM   5460  C CB  . ASP C  1 218 ? -10.880 -7.549  81.528  1.00 20.90  ? 231 ASP C CB  1 
ATOM   5461  C CG  . ASP C  1 218 ? -11.947 -8.600  81.260  1.00 22.24  ? 231 ASP C CG  1 
ATOM   5462  O OD1 . ASP C  1 218 ? -11.589 -9.761  80.967  1.00 24.85  ? 231 ASP C OD1 1 
ATOM   5463  O OD2 . ASP C  1 218 ? -13.147 -8.266  81.336  1.00 22.17  ? 231 ASP C OD2 1 
ATOM   5464  N N   . PHE C  1 219 ? -7.718  -7.083  80.628  1.00 19.02  ? 232 PHE C N   1 
ATOM   5465  C CA  . PHE C  1 219 ? -6.607  -6.158  80.439  1.00 18.72  ? 232 PHE C CA  1 
ATOM   5466  C C   . PHE C  1 219 ? -6.961  -5.002  79.511  1.00 18.75  ? 232 PHE C C   1 
ATOM   5467  O O   . PHE C  1 219 ? -7.614  -5.191  78.481  1.00 18.58  ? 232 PHE C O   1 
ATOM   5468  C CB  . PHE C  1 219 ? -5.368  -6.904  79.936  1.00 18.56  ? 232 PHE C CB  1 
ATOM   5469  C CG  . PHE C  1 219 ? -4.786  -7.846  80.948  1.00 19.22  ? 232 PHE C CG  1 
ATOM   5470  C CD1 . PHE C  1 219 ? -5.186  -9.178  80.989  1.00 17.88  ? 232 PHE C CD1 1 
ATOM   5471  C CD2 . PHE C  1 219 ? -3.852  -7.395  81.877  1.00 20.42  ? 232 PHE C CD2 1 
ATOM   5472  C CE1 . PHE C  1 219 ? -4.658  -10.052 81.934  1.00 20.49  ? 232 PHE C CE1 1 
ATOM   5473  C CE2 . PHE C  1 219 ? -3.315  -8.261  82.826  1.00 21.35  ? 232 PHE C CE2 1 
ATOM   5474  C CZ  . PHE C  1 219 ? -3.719  -9.592  82.855  1.00 21.79  ? 232 PHE C CZ  1 
ATOM   5475  N N   . HIS C  1 220 ? -6.534  -3.804  79.901  1.00 18.71  ? 233 HIS C N   1 
ATOM   5476  C CA  . HIS C  1 220 ? -6.755  -2.597  79.113  1.00 19.26  ? 233 HIS C CA  1 
ATOM   5477  C C   . HIS C  1 220 ? -5.434  -1.871  78.893  1.00 19.38  ? 233 HIS C C   1 
ATOM   5478  O O   . HIS C  1 220 ? -4.455  -2.130  79.594  1.00 19.70  ? 233 HIS C O   1 
ATOM   5479  C CB  . HIS C  1 220 ? -7.770  -1.685  79.798  1.00 19.46  ? 233 HIS C CB  1 
ATOM   5480  C CG  . HIS C  1 220 ? -8.958  -2.413  80.344  1.00 20.36  ? 233 HIS C CG  1 
ATOM   5481  N ND1 . HIS C  1 220 ? -10.078 -2.683  79.590  1.00 19.30  ? 233 HIS C ND1 1 
ATOM   5482  C CD2 . HIS C  1 220 ? -9.193  -2.939  81.569  1.00 21.01  ? 233 HIS C CD2 1 
ATOM   5483  C CE1 . HIS C  1 220 ? -10.956 -3.336  80.329  1.00 20.84  ? 233 HIS C CE1 1 
ATOM   5484  N NE2 . HIS C  1 220 ? -10.443 -3.505  81.533  1.00 20.80  ? 233 HIS C NE2 1 
ATOM   5485  N N   . TRP C  1 221 ? -5.405  -0.963  77.923  1.00 19.67  ? 234 TRP C N   1 
ATOM   5486  C CA  . TRP C  1 221 ? -4.144  -0.381  77.485  1.00 19.68  ? 234 TRP C CA  1 
ATOM   5487  C C   . TRP C  1 221 ? -4.260  1.014   76.873  1.00 20.78  ? 234 TRP C C   1 
ATOM   5488  O O   . TRP C  1 221 ? -5.349  1.455   76.493  1.00 21.53  ? 234 TRP C O   1 
ATOM   5489  C CB  . TRP C  1 221 ? -3.445  -1.330  76.507  1.00 19.02  ? 234 TRP C CB  1 
ATOM   5490  C CG  . TRP C  1 221 ? -4.264  -1.677  75.306  1.00 16.15  ? 234 TRP C CG  1 
ATOM   5491  C CD1 . TRP C  1 221 ? -5.235  -2.634  75.221  1.00 14.57  ? 234 TRP C CD1 1 
ATOM   5492  C CD2 . TRP C  1 221 ? -4.176  -1.077  74.009  1.00 13.98  ? 234 TRP C CD2 1 
ATOM   5493  N NE1 . TRP C  1 221 ? -5.761  -2.664  73.952  1.00 13.84  ? 234 TRP C NE1 1 
ATOM   5494  C CE2 . TRP C  1 221 ? -5.129  -1.719  73.187  1.00 12.58  ? 234 TRP C CE2 1 
ATOM   5495  C CE3 . TRP C  1 221 ? -3.388  -0.054  73.462  1.00 12.21  ? 234 TRP C CE3 1 
ATOM   5496  C CZ2 . TRP C  1 221 ? -5.318  -1.371  71.846  1.00 11.79  ? 234 TRP C CZ2 1 
ATOM   5497  C CZ3 . TRP C  1 221 ? -3.574  0.290   72.126  1.00 11.11  ? 234 TRP C CZ3 1 
ATOM   5498  C CH2 . TRP C  1 221 ? -4.532  -0.368  71.334  1.00 11.09  ? 234 TRP C CH2 1 
ATOM   5499  N N   . LEU C  1 222 ? -3.117  1.696   76.796  1.00 21.36  ? 235 LEU C N   1 
ATOM   5500  C CA  . LEU C  1 222 ? -2.995  2.999   76.140  1.00 21.65  ? 235 LEU C CA  1 
ATOM   5501  C C   . LEU C  1 222 ? -1.563  3.220   75.658  1.00 21.71  ? 235 LEU C C   1 
ATOM   5502  O O   . LEU C  1 222 ? -0.638  2.541   76.111  1.00 22.30  ? 235 LEU C O   1 
ATOM   5503  C CB  . LEU C  1 222 ? -3.428  4.136   77.079  1.00 21.28  ? 235 LEU C CB  1 
ATOM   5504  C CG  . LEU C  1 222 ? -2.597  4.483   78.323  1.00 22.28  ? 235 LEU C CG  1 
ATOM   5505  C CD1 . LEU C  1 222 ? -1.449  5.441   78.003  1.00 21.02  ? 235 LEU C CD1 1 
ATOM   5506  C CD2 . LEU C  1 222 ? -3.491  5.088   79.390  1.00 21.85  ? 235 LEU C CD2 1 
ATOM   5507  N N   . LEU C  1 223 ? -1.390  4.173   74.746  1.00 21.72  ? 236 LEU C N   1 
ATOM   5508  C CA  . LEU C  1 223 ? -0.069  4.575   74.273  1.00 21.79  ? 236 LEU C CA  1 
ATOM   5509  C C   . LEU C  1 223 ? 0.301   5.941   74.846  1.00 22.56  ? 236 LEU C C   1 
ATOM   5510  O O   . LEU C  1 223 ? -0.292  6.958   74.480  1.00 22.62  ? 236 LEU C O   1 
ATOM   5511  C CB  . LEU C  1 223 ? -0.032  4.607   72.741  1.00 21.35  ? 236 LEU C CB  1 
ATOM   5512  C CG  . LEU C  1 223 ? 0.042   3.272   71.993  1.00 20.22  ? 236 LEU C CG  1 
ATOM   5513  C CD1 . LEU C  1 223 ? -0.551  3.409   70.596  1.00 15.63  ? 236 LEU C CD1 1 
ATOM   5514  C CD2 . LEU C  1 223 ? 1.482   2.736   71.939  1.00 16.64  ? 236 LEU C CD2 1 
ATOM   5515  N N   . LEU C  1 224 ? 1.273   5.958   75.753  1.00 23.77  ? 237 LEU C N   1 
ATOM   5516  C CA  . LEU C  1 224 ? 1.695   7.194   76.412  1.00 24.55  ? 237 LEU C CA  1 
ATOM   5517  C C   . LEU C  1 224 ? 2.795   7.913   75.640  1.00 25.47  ? 237 LEU C C   1 
ATOM   5518  O O   . LEU C  1 224 ? 3.842   7.333   75.347  1.00 25.48  ? 237 LEU C O   1 
ATOM   5519  C CB  . LEU C  1 224 ? 2.154   6.924   77.848  1.00 24.12  ? 237 LEU C CB  1 
ATOM   5520  C CG  . LEU C  1 224 ? 2.618   8.162   78.621  1.00 24.57  ? 237 LEU C CG  1 
ATOM   5521  C CD1 . LEU C  1 224 ? 1.424   9.020   79.022  1.00 25.29  ? 237 LEU C CD1 1 
ATOM   5522  C CD2 . LEU C  1 224 ? 3.444   7.777   79.839  1.00 24.49  ? 237 LEU C CD2 1 
ATOM   5523  N N   . ASP C  1 225 ? 2.547   9.186   75.335  1.00 26.69  ? 238 ASP C N   1 
ATOM   5524  C CA  . ASP C  1 225 ? 3.487   10.035  74.601  1.00 27.60  ? 238 ASP C CA  1 
ATOM   5525  C C   . ASP C  1 225 ? 4.773   10.329  75.389  1.00 28.04  ? 238 ASP C C   1 
ATOM   5526  O O   . ASP C  1 225 ? 4.769   10.258  76.623  1.00 28.31  ? 238 ASP C O   1 
ATOM   5527  C CB  . ASP C  1 225 ? 2.802   11.351  74.219  1.00 27.78  ? 238 ASP C CB  1 
ATOM   5528  C CG  . ASP C  1 225 ? 1.689   11.163  73.202  1.00 28.07  ? 238 ASP C CG  1 
ATOM   5529  O OD1 . ASP C  1 225 ? 1.490   10.029  72.711  1.00 26.94  ? 238 ASP C OD1 1 
ATOM   5530  O OD2 . ASP C  1 225 ? 1.010   12.165  72.893  1.00 28.40  ? 238 ASP C OD2 1 
ATOM   5531  N N   . PRO C  1 226 ? 5.882   10.646  74.677  1.00 28.25  ? 239 PRO C N   1 
ATOM   5532  C CA  . PRO C  1 226 ? 7.115   11.094  75.338  1.00 28.27  ? 239 PRO C CA  1 
ATOM   5533  C C   . PRO C  1 226 ? 6.880   12.309  76.233  1.00 28.33  ? 239 PRO C C   1 
ATOM   5534  O O   . PRO C  1 226 ? 6.109   13.202  75.869  1.00 28.38  ? 239 PRO C O   1 
ATOM   5535  C CB  . PRO C  1 226 ? 8.022   11.474  74.164  1.00 28.20  ? 239 PRO C CB  1 
ATOM   5536  C CG  . PRO C  1 226 ? 7.573   10.594  73.056  1.00 28.03  ? 239 PRO C CG  1 
ATOM   5537  C CD  . PRO C  1 226 ? 6.084   10.445  73.227  1.00 27.93  ? 239 PRO C CD  1 
ATOM   5538  N N   . ASN C  1 227 ? 7.529   12.316  77.398  1.00 28.49  ? 240 ASN C N   1 
ATOM   5539  C CA  . ASN C  1 227 ? 7.429   13.403  78.386  1.00 28.51  ? 240 ASN C CA  1 
ATOM   5540  C C   . ASN C  1 227 ? 6.024   13.576  79.007  1.00 28.06  ? 240 ASN C C   1 
ATOM   5541  O O   . ASN C  1 227 ? 5.789   14.507  79.782  1.00 27.87  ? 240 ASN C O   1 
ATOM   5542  C CB  . ASN C  1 227 ? 7.955   14.726  77.796  1.00 28.66  ? 240 ASN C CB  1 
ATOM   5543  C CG  . ASN C  1 227 ? 8.792   15.529  78.789  1.00 30.95  ? 240 ASN C CG  1 
ATOM   5544  O OD1 . ASN C  1 227 ? 8.325   15.899  79.868  1.00 32.06  ? 240 ASN C OD1 1 
ATOM   5545  N ND2 . ASN C  1 227 ? 10.035  15.815  78.412  1.00 32.11  ? 240 ASN C ND2 1 
ATOM   5546  N N   . ASP C  1 228 ? 5.110   12.662  78.676  1.00 27.50  ? 241 ASP C N   1 
ATOM   5547  C CA  . ASP C  1 228 ? 3.739   12.666  79.208  1.00 26.82  ? 241 ASP C CA  1 
ATOM   5548  C C   . ASP C  1 228 ? 3.613   11.691  80.391  1.00 26.20  ? 241 ASP C C   1 
ATOM   5549  O O   . ASP C  1 228 ? 4.520   10.896  80.640  1.00 26.16  ? 241 ASP C O   1 
ATOM   5550  C CB  . ASP C  1 228 ? 2.739   12.330  78.087  1.00 26.92  ? 241 ASP C CB  1 
ATOM   5551  C CG  . ASP C  1 228 ? 1.289   12.637  78.459  1.00 26.20  ? 241 ASP C CG  1 
ATOM   5552  O OD1 . ASP C  1 228 ? 1.040   13.363  79.445  1.00 24.93  ? 241 ASP C OD1 1 
ATOM   5553  O OD2 . ASP C  1 228 ? 0.387   12.143  77.749  1.00 26.80  ? 241 ASP C OD2 1 
ATOM   5554  N N   . THR C  1 229 ? 2.492   11.756  81.111  1.00 25.69  ? 242 THR C N   1 
ATOM   5555  C CA  . THR C  1 229 ? 2.315   11.017  82.365  1.00 25.47  ? 242 THR C CA  1 
ATOM   5556  C C   . THR C  1 229 ? 1.005   10.223  82.415  1.00 25.49  ? 242 THR C C   1 
ATOM   5557  O O   . THR C  1 229 ? -0.049  10.729  82.021  1.00 25.52  ? 242 THR C O   1 
ATOM   5558  C CB  . THR C  1 229 ? 2.370   11.982  83.579  1.00 25.48  ? 242 THR C CB  1 
ATOM   5559  O OG1 . THR C  1 229 ? 3.554   12.786  83.500  1.00 25.72  ? 242 THR C OG1 1 
ATOM   5560  C CG2 . THR C  1 229 ? 2.364   11.219  84.904  1.00 25.27  ? 242 THR C CG2 1 
ATOM   5561  N N   . VAL C  1 230 ? 1.088   8.980   82.893  1.00 25.35  ? 243 VAL C N   1 
ATOM   5562  C CA  . VAL C  1 230 ? -0.096  8.168   83.191  1.00 25.12  ? 243 VAL C CA  1 
ATOM   5563  C C   . VAL C  1 230 ? -0.364  8.217   84.687  1.00 25.09  ? 243 VAL C C   1 
ATOM   5564  O O   . VAL C  1 230 ? 0.529   7.947   85.490  1.00 25.21  ? 243 VAL C O   1 
ATOM   5565  C CB  . VAL C  1 230 ? 0.067   6.678   82.787  1.00 25.10  ? 243 VAL C CB  1 
ATOM   5566  C CG1 . VAL C  1 230 ? -1.256  5.935   82.946  1.00 24.83  ? 243 VAL C CG1 1 
ATOM   5567  C CG2 . VAL C  1 230 ? 0.550   6.545   81.369  1.00 25.72  ? 243 VAL C CG2 1 
ATOM   5568  N N   . THR C  1 231 ? -1.596  8.555   85.056  1.00 25.26  ? 244 THR C N   1 
ATOM   5569  C CA  . THR C  1 231 ? -1.998  8.584   86.457  1.00 25.30  ? 244 THR C CA  1 
ATOM   5570  C C   . THR C  1 231 ? -3.013  7.479   86.742  1.00 25.08  ? 244 THR C C   1 
ATOM   5571  O O   . THR C  1 231 ? -4.094  7.443   86.143  1.00 24.86  ? 244 THR C O   1 
ATOM   5572  C CB  . THR C  1 231 ? -2.564  9.969   86.867  1.00 25.28  ? 244 THR C CB  1 
ATOM   5573  O OG1 . THR C  1 231 ? -1.629  10.995  86.513  1.00 24.74  ? 244 THR C OG1 1 
ATOM   5574  C CG2 . THR C  1 231 ? -2.821  10.033  88.366  1.00 25.53  ? 244 THR C CG2 1 
ATOM   5575  N N   . PHE C  1 232 ? -2.640  6.574   87.644  1.00 24.78  ? 245 PHE C N   1 
ATOM   5576  C CA  . PHE C  1 232 ? -3.531  5.519   88.115  1.00 24.73  ? 245 PHE C CA  1 
ATOM   5577  C C   . PHE C  1 232 ? -4.082  5.888   89.487  1.00 24.83  ? 245 PHE C C   1 
ATOM   5578  O O   . PHE C  1 232 ? -3.323  6.229   90.396  1.00 24.79  ? 245 PHE C O   1 
ATOM   5579  C CB  . PHE C  1 232 ? -2.794  4.177   88.223  1.00 24.77  ? 245 PHE C CB  1 
ATOM   5580  C CG  . PHE C  1 232 ? -2.248  3.659   86.918  1.00 24.03  ? 245 PHE C CG  1 
ATOM   5581  C CD1 . PHE C  1 232 ? -0.902  3.823   86.600  1.00 23.85  ? 245 PHE C CD1 1 
ATOM   5582  C CD2 . PHE C  1 232 ? -3.069  2.983   86.020  1.00 22.17  ? 245 PHE C CD2 1 
ATOM   5583  C CE1 . PHE C  1 232 ? -0.385  3.334   85.401  1.00 21.53  ? 245 PHE C CE1 1 
ATOM   5584  C CE2 . PHE C  1 232 ? -2.562  2.493   84.820  1.00 21.10  ? 245 PHE C CE2 1 
ATOM   5585  C CZ  . PHE C  1 232 ? -1.218  2.668   84.512  1.00 20.03  ? 245 PHE C CZ  1 
ATOM   5586  N N   . THR C  1 233 ? -5.403  5.830   89.626  1.00 24.96  ? 246 THR C N   1 
ATOM   5587  C CA  . THR C  1 233 ? -6.058  5.968   90.930  1.00 25.00  ? 246 THR C CA  1 
ATOM   5588  C C   . THR C  1 233 ? -7.006  4.787   91.129  1.00 24.75  ? 246 THR C C   1 
ATOM   5589  O O   . THR C  1 233 ? -7.816  4.478   90.251  1.00 24.73  ? 246 THR C O   1 
ATOM   5590  C CB  . THR C  1 233 ? -6.815  7.313   91.084  1.00 25.12  ? 246 THR C CB  1 
ATOM   5591  O OG1 . THR C  1 233 ? -7.741  7.479   90.005  1.00 24.32  ? 246 THR C OG1 1 
ATOM   5592  C CG2 . THR C  1 233 ? -5.842  8.490   91.100  1.00 25.57  ? 246 THR C CG2 1 
ATOM   5593  N N   . PHE C  1 234 ? -6.893  4.126   92.279  1.00 23.96  ? 247 PHE C N   1 
ATOM   5594  C CA  . PHE C  1 234 ? -7.574  2.852   92.502  1.00 23.72  ? 247 PHE C CA  1 
ATOM   5595  C C   . PHE C  1 234 ? -7.703  2.516   93.985  1.00 23.68  ? 247 PHE C C   1 
ATOM   5596  O O   . PHE C  1 234 ? -6.835  2.867   94.788  1.00 23.52  ? 247 PHE C O   1 
ATOM   5597  C CB  . PHE C  1 234 ? -6.834  1.718   91.773  1.00 23.85  ? 247 PHE C CB  1 
ATOM   5598  C CG  . PHE C  1 234 ? -5.349  1.680   92.050  1.00 23.46  ? 247 PHE C CG  1 
ATOM   5599  C CD1 . PHE C  1 234 ? -4.842  0.916   93.100  1.00 22.06  ? 247 PHE C CD1 1 
ATOM   5600  C CD2 . PHE C  1 234 ? -4.459  2.407   91.261  1.00 21.92  ? 247 PHE C CD2 1 
ATOM   5601  C CE1 . PHE C  1 234 ? -3.475  0.884   93.366  1.00 21.81  ? 247 PHE C CE1 1 
ATOM   5602  C CE2 . PHE C  1 234 ? -3.092  2.380   91.519  1.00 22.99  ? 247 PHE C CE2 1 
ATOM   5603  C CZ  . PHE C  1 234 ? -2.598  1.615   92.572  1.00 22.51  ? 247 PHE C CZ  1 
ATOM   5604  N N   . ASN C  1 235 ? -8.786  1.825   94.334  1.00 23.71  ? 248 ASN C N   1 
ATOM   5605  C CA  . ASN C  1 235 ? -9.038  1.393   95.710  1.00 23.88  ? 248 ASN C CA  1 
ATOM   5606  C C   . ASN C  1 235 ? -9.218  -0.123  95.825  1.00 23.50  ? 248 ASN C C   1 
ATOM   5607  O O   . ASN C  1 235 ? -9.820  -0.618  96.780  1.00 23.30  ? 248 ASN C O   1 
ATOM   5608  C CB  . ASN C  1 235 ? -10.256 2.129   96.288  1.00 24.27  ? 248 ASN C CB  1 
ATOM   5609  C CG  . ASN C  1 235 ? -11.522 1.928   95.459  1.00 25.45  ? 248 ASN C CG  1 
ATOM   5610  O OD1 . ASN C  1 235 ? -11.500 1.298   94.397  1.00 25.75  ? 248 ASN C OD1 1 
ATOM   5611  N ND2 . ASN C  1 235 ? -12.632 2.470   95.945  1.00 24.23  ? 248 ASN C ND2 1 
ATOM   5612  N N   . GLY C  1 236 ? -8.681  -0.848  94.847  1.00 23.58  ? 249 GLY C N   1 
ATOM   5613  C CA  . GLY C  1 236 ? -8.825  -2.301  94.771  1.00 23.33  ? 249 GLY C CA  1 
ATOM   5614  C C   . GLY C  1 236 ? -9.145  -2.783  93.366  1.00 23.19  ? 249 GLY C C   1 
ATOM   5615  O O   . GLY C  1 236 ? -9.293  -1.974  92.441  1.00 23.23  ? 249 GLY C O   1 
ATOM   5616  N N   . ALA C  1 237 ? -9.245  -4.107  93.216  1.00 22.74  ? 250 ALA C N   1 
ATOM   5617  C CA  . ALA C  1 237 ? -9.544  -4.777  91.937  1.00 22.21  ? 250 ALA C CA  1 
ATOM   5618  C C   . ALA C  1 237 ? -8.606  -4.378  90.793  1.00 21.65  ? 250 ALA C C   1 
ATOM   5619  O O   . ALA C  1 237 ? -8.971  -4.464  89.616  1.00 21.91  ? 250 ALA C O   1 
ATOM   5620  C CB  . ALA C  1 237 ? -11.014 -4.569  91.540  1.00 22.16  ? 250 ALA C CB  1 
ATOM   5621  N N   . PHE C  1 238 ? -7.393  -3.961  91.153  1.00 20.64  ? 251 PHE C N   1 
ATOM   5622  C CA  . PHE C  1 238 ? -6.458  -3.380  90.198  1.00 19.59  ? 251 PHE C CA  1 
ATOM   5623  C C   . PHE C  1 238 ? -5.185  -4.208  90.054  1.00 19.35  ? 251 PHE C C   1 
ATOM   5624  O O   . PHE C  1 238 ? -4.449  -4.423  91.022  1.00 19.57  ? 251 PHE C O   1 
ATOM   5625  C CB  . PHE C  1 238 ? -6.131  -1.935  90.596  1.00 19.17  ? 251 PHE C CB  1 
ATOM   5626  C CG  . PHE C  1 238 ? -5.184  -1.236  89.657  1.00 16.92  ? 251 PHE C CG  1 
ATOM   5627  C CD1 . PHE C  1 238 ? -5.597  -0.850  88.387  1.00 15.40  ? 251 PHE C CD1 1 
ATOM   5628  C CD2 . PHE C  1 238 ? -3.882  -0.947  90.053  1.00 14.45  ? 251 PHE C CD2 1 
ATOM   5629  C CE1 . PHE C  1 238 ? -4.723  -0.193  87.519  1.00 14.43  ? 251 PHE C CE1 1 
ATOM   5630  C CE2 . PHE C  1 238 ? -3.005  -0.290  89.194  1.00 12.87  ? 251 PHE C CE2 1 
ATOM   5631  C CZ  . PHE C  1 238 ? -3.426  0.085   87.925  1.00 12.84  ? 251 PHE C CZ  1 
ATOM   5632  N N   . ILE C  1 239 ? -4.948  -4.670  88.830  1.00 18.51  ? 252 ILE C N   1 
ATOM   5633  C CA  . ILE C  1 239 ? -3.720  -5.362  88.468  1.00 17.60  ? 252 ILE C CA  1 
ATOM   5634  C C   . ILE C  1 239 ? -2.749  -4.333  87.891  1.00 17.31  ? 252 ILE C C   1 
ATOM   5635  O O   . ILE C  1 239 ? -3.003  -3.745  86.835  1.00 16.97  ? 252 ILE C O   1 
ATOM   5636  C CB  . ILE C  1 239 ? -3.991  -6.494  87.448  1.00 17.15  ? 252 ILE C CB  1 
ATOM   5637  C CG1 . ILE C  1 239 ? -5.086  -7.445  87.955  1.00 16.90  ? 252 ILE C CG1 1 
ATOM   5638  C CG2 . ILE C  1 239 ? -2.709  -7.239  87.104  1.00 18.55  ? 252 ILE C CG2 1 
ATOM   5639  C CD1 . ILE C  1 239 ? -4.792  -8.129  89.285  1.00 17.16  ? 252 ILE C CD1 1 
ATOM   5640  N N   . ALA C  1 240 ? -1.643  -4.120  88.599  1.00 17.12  ? 253 ALA C N   1 
ATOM   5641  C CA  . ALA C  1 240 ? -0.711  -3.039  88.292  1.00 17.19  ? 253 ALA C CA  1 
ATOM   5642  C C   . ALA C  1 240 ? 0.421   -3.474  87.370  1.00 17.59  ? 253 ALA C C   1 
ATOM   5643  O O   . ALA C  1 240 ? 0.923   -4.590  87.492  1.00 17.56  ? 253 ALA C O   1 
ATOM   5644  C CB  . ALA C  1 240 ? -0.146  -2.457  89.575  1.00 17.17  ? 253 ALA C CB  1 
ATOM   5645  N N   . PRO C  1 241 ? 0.825   -2.590  86.440  1.00 18.28  ? 254 PRO C N   1 
ATOM   5646  C CA  . PRO C  1 241 ? 1.990   -2.854  85.599  1.00 19.27  ? 254 PRO C CA  1 
ATOM   5647  C C   . PRO C  1 241 ? 3.303   -2.704  86.364  1.00 20.16  ? 254 PRO C C   1 
ATOM   5648  O O   . PRO C  1 241 ? 3.482   -1.743  87.119  1.00 20.96  ? 254 PRO C O   1 
ATOM   5649  C CB  . PRO C  1 241 ? 1.889   -1.780  84.513  1.00 19.11  ? 254 PRO C CB  1 
ATOM   5650  C CG  . PRO C  1 241 ? 1.113   -0.682  85.137  1.00 17.97  ? 254 PRO C CG  1 
ATOM   5651  C CD  . PRO C  1 241 ? 0.120   -1.362  86.026  1.00 18.29  ? 254 PRO C CD  1 
ATOM   5652  N N   . ASP C  1 242 ? 4.204   -3.660  86.165  1.00 20.54  ? 255 ASP C N   1 
ATOM   5653  C CA  . ASP C  1 242 ? 5.539   -3.612  86.752  1.00 21.31  ? 255 ASP C CA  1 
ATOM   5654  C C   . ASP C  1 242 ? 6.553   -3.132  85.708  1.00 21.67  ? 255 ASP C C   1 
ATOM   5655  O O   . ASP C  1 242 ? 7.550   -2.489  86.046  1.00 21.74  ? 255 ASP C O   1 
ATOM   5656  C CB  . ASP C  1 242 ? 5.932   -4.990  87.294  1.00 21.46  ? 255 ASP C CB  1 
ATOM   5657  C CG  . ASP C  1 242 ? 7.224   -4.962  88.084  1.00 20.58  ? 255 ASP C CG  1 
ATOM   5658  O OD1 . ASP C  1 242 ? 8.169   -5.674  87.695  1.00 20.77  ? 255 ASP C OD1 1 
ATOM   5659  O OD2 . ASP C  1 242 ? 7.300   -4.228  89.090  1.00 20.99  ? 255 ASP C OD2 1 
ATOM   5660  N N   . ARG C  1 243 ? 6.285   -3.460  84.445  1.00 21.62  ? 256 ARG C N   1 
ATOM   5661  C CA  . ARG C  1 243 ? 7.104   -3.017  83.316  1.00 21.15  ? 256 ARG C CA  1 
ATOM   5662  C C   . ARG C  1 243 ? 6.227   -2.550  82.150  1.00 20.34  ? 256 ARG C C   1 
ATOM   5663  O O   . ARG C  1 243 ? 5.097   -3.019  81.982  1.00 20.23  ? 256 ARG C O   1 
ATOM   5664  C CB  . ARG C  1 243 ? 8.053   -4.135  82.862  1.00 21.68  ? 256 ARG C CB  1 
ATOM   5665  C CG  . ARG C  1 243 ? 9.259   -4.344  83.777  1.00 23.35  ? 256 ARG C CG  1 
ATOM   5666  C CD  . ARG C  1 243 ? 9.810   -5.754  83.664  1.00 25.77  ? 256 ARG C CD  1 
ATOM   5667  N NE  . ARG C  1 243 ? 10.912  -5.866  82.709  1.00 26.65  ? 256 ARG C NE  1 
ATOM   5668  C CZ  . ARG C  1 243 ? 11.204  -6.969  82.021  1.00 24.68  ? 256 ARG C CZ  1 
ATOM   5669  N NH1 . ARG C  1 243 ? 10.462  -8.065  82.147  1.00 22.94  ? 256 ARG C NH1 1 
ATOM   5670  N NH2 . ARG C  1 243 ? 12.233  -6.971  81.186  1.00 26.11  ? 256 ARG C NH2 1 
ATOM   5671  N N   . THR C  1 244 ? 6.752   -1.614  81.363  1.00 19.38  ? 257 THR C N   1 
ATOM   5672  C CA  . THR C  1 244 ? 6.079   -1.125  80.158  1.00 18.70  ? 257 THR C CA  1 
ATOM   5673  C C   . THR C  1 244 ? 6.857   -1.554  78.907  1.00 19.39  ? 257 THR C C   1 
ATOM   5674  O O   . THR C  1 244 ? 7.987   -2.034  79.014  1.00 19.69  ? 257 THR C O   1 
ATOM   5675  C CB  . THR C  1 244 ? 5.874   0.412   80.199  1.00 18.07  ? 257 THR C CB  1 
ATOM   5676  O OG1 . THR C  1 244 ? 5.263   0.852   78.981  1.00 19.03  ? 257 THR C OG1 1 
ATOM   5677  C CG2 . THR C  1 244 ? 7.196   1.146   80.394  1.00 15.73  ? 257 THR C CG2 1 
ATOM   5678  N N   . SER C  1 245 ? 6.259   -1.384  77.729  1.00 19.56  ? 258 SER C N   1 
ATOM   5679  C CA  . SER C  1 245 ? 6.895   -1.815  76.482  1.00 20.12  ? 258 SER C CA  1 
ATOM   5680  C C   . SER C  1 245 ? 7.230   -0.661  75.535  1.00 20.61  ? 258 SER C C   1 
ATOM   5681  O O   . SER C  1 245 ? 6.434   0.260   75.354  1.00 21.50  ? 258 SER C O   1 
ATOM   5682  C CB  . SER C  1 245 ? 6.023   -2.847  75.767  1.00 20.10  ? 258 SER C CB  1 
ATOM   5683  O OG  . SER C  1 245 ? 5.615   -3.866  76.664  1.00 20.65  ? 258 SER C OG  1 
ATOM   5684  N N   . PHE C  1 246 ? 8.421   -0.723  74.944  1.00 20.72  ? 259 PHE C N   1 
ATOM   5685  C CA  . PHE C  1 246 ? 8.849   0.232   73.929  1.00 21.20  ? 259 PHE C CA  1 
ATOM   5686  C C   . PHE C  1 246 ? 9.155   -0.508  72.636  1.00 21.70  ? 259 PHE C C   1 
ATOM   5687  O O   . PHE C  1 246 ? 9.881   -1.504  72.642  1.00 21.92  ? 259 PHE C O   1 
ATOM   5688  C CB  . PHE C  1 246 ? 10.090  0.995   74.392  1.00 21.47  ? 259 PHE C CB  1 
ATOM   5689  C CG  . PHE C  1 246 ? 9.827   1.963   75.505  1.00 23.36  ? 259 PHE C CG  1 
ATOM   5690  C CD1 . PHE C  1 246 ? 10.023  1.588   76.830  1.00 24.24  ? 259 PHE C CD1 1 
ATOM   5691  C CD2 . PHE C  1 246 ? 9.384   3.254   75.231  1.00 25.18  ? 259 PHE C CD2 1 
ATOM   5692  C CE1 . PHE C  1 246 ? 9.780   2.484   77.867  1.00 25.29  ? 259 PHE C CE1 1 
ATOM   5693  C CE2 . PHE C  1 246 ? 9.138   4.156   76.261  1.00 24.45  ? 259 PHE C CE2 1 
ATOM   5694  C CZ  . PHE C  1 246 ? 9.337   3.770   77.582  1.00 24.45  ? 259 PHE C CZ  1 
ATOM   5695  N N   . PHE C  1 247 ? 8.602   -0.019  71.529  1.00 21.86  ? 260 PHE C N   1 
ATOM   5696  C CA  . PHE C  1 247 ? 8.773   -0.680  70.236  1.00 22.23  ? 260 PHE C CA  1 
ATOM   5697  C C   . PHE C  1 247 ? 10.168  -0.451  69.657  1.00 22.18  ? 260 PHE C C   1 
ATOM   5698  O O   . PHE C  1 247 ? 10.764  0.608   69.857  1.00 22.17  ? 260 PHE C O   1 
ATOM   5699  C CB  . PHE C  1 247 ? 7.677   -0.252  69.255  1.00 22.34  ? 260 PHE C CB  1 
ATOM   5700  C CG  . PHE C  1 247 ? 6.278   -0.453  69.782  1.00 23.15  ? 260 PHE C CG  1 
ATOM   5701  C CD1 . PHE C  1 247 ? 5.918   -1.640  70.421  1.00 23.17  ? 260 PHE C CD1 1 
ATOM   5702  C CD2 . PHE C  1 247 ? 5.317   0.541   69.633  1.00 24.23  ? 260 PHE C CD2 1 
ATOM   5703  C CE1 . PHE C  1 247 ? 4.628   -1.831  70.906  1.00 22.87  ? 260 PHE C CE1 1 
ATOM   5704  C CE2 . PHE C  1 247 ? 4.021   0.358   70.116  1.00 24.03  ? 260 PHE C CE2 1 
ATOM   5705  C CZ  . PHE C  1 247 ? 3.678   -0.831  70.753  1.00 22.83  ? 260 PHE C CZ  1 
ATOM   5706  N N   . ARG C  1 248 ? 10.682  -1.450  68.948  1.00 22.25  ? 261 ARG C N   1 
ATOM   5707  C CA  . ARG C  1 248 ? 12.080  -1.444  68.511  1.00 22.71  ? 261 ARG C CA  1 
ATOM   5708  C C   . ARG C  1 248 ? 12.291  -0.809  67.135  1.00 23.16  ? 261 ARG C C   1 
ATOM   5709  O O   . ARG C  1 248 ? 13.215  -0.011  66.961  1.00 23.22  ? 261 ARG C O   1 
ATOM   5710  C CB  . ARG C  1 248 ? 12.675  -2.857  68.548  1.00 22.31  ? 261 ARG C CB  1 
ATOM   5711  C CG  . ARG C  1 248 ? 12.363  -3.631  69.820  1.00 22.13  ? 261 ARG C CG  1 
ATOM   5712  C CD  . ARG C  1 248 ? 13.125  -4.940  69.882  1.00 21.14  ? 261 ARG C CD  1 
ATOM   5713  N NE  . ARG C  1 248 ? 14.300  -4.833  70.743  1.00 22.35  ? 261 ARG C NE  1 
ATOM   5714  C CZ  . ARG C  1 248 ? 14.393  -5.366  71.959  1.00 23.32  ? 261 ARG C CZ  1 
ATOM   5715  N NH1 . ARG C  1 248 ? 13.385  -6.065  72.469  1.00 26.31  ? 261 ARG C NH1 1 
ATOM   5716  N NH2 . ARG C  1 248 ? 15.501  -5.207  72.667  1.00 23.24  ? 261 ARG C NH2 1 
ATOM   5717  N N   . GLY C  1 249 ? 11.442  -1.164  66.169  1.00 23.31  ? 263 GLY C N   1 
ATOM   5718  C CA  . GLY C  1 249 ? 11.566  -0.653  64.803  1.00 23.11  ? 263 GLY C CA  1 
ATOM   5719  C C   . GLY C  1 249 ? 10.454  -1.083  63.866  1.00 23.33  ? 263 GLY C C   1 
ATOM   5720  O O   . GLY C  1 249 ? 9.302   -0.674  64.032  1.00 23.14  ? 263 GLY C O   1 
ATOM   5721  N N   . GLU C  1 250 ? 10.811  -1.901  62.875  1.00 23.74  ? 264 GLU C N   1 
ATOM   5722  C CA  . GLU C  1 250 ? 9.876   -2.389  61.851  1.00 23.83  ? 264 GLU C CA  1 
ATOM   5723  C C   . GLU C  1 250 ? 9.795   -3.912  61.848  1.00 22.72  ? 264 GLU C C   1 
ATOM   5724  O O   . GLU C  1 250 ? 10.807  -4.594  62.035  1.00 22.92  ? 264 GLU C O   1 
ATOM   5725  C CB  . GLU C  1 250 ? 10.301  -1.917  60.452  1.00 24.41  ? 264 GLU C CB  1 
ATOM   5726  C CG  . GLU C  1 250 ? 9.624   -0.640  59.948  1.00 29.10  ? 264 GLU C CG  1 
ATOM   5727  C CD  . GLU C  1 250 ? 10.380  0.643   60.290  1.00 35.88  ? 264 GLU C CD  1 
ATOM   5728  O OE1 . GLU C  1 250 ? 9.861   1.734   59.965  1.00 37.93  ? 264 GLU C OE1 1 
ATOM   5729  O OE2 . GLU C  1 250 ? 11.487  0.572   60.874  1.00 38.48  ? 264 GLU C OE2 1 
ATOM   5730  N N   . SER C  1 251 ? 8.590   -4.437  61.632  1.00 21.41  ? 265 SER C N   1 
ATOM   5731  C CA  . SER C  1 251 ? 8.382   -5.876  61.436  1.00 20.16  ? 265 SER C CA  1 
ATOM   5732  C C   . SER C  1 251 ? 7.127   -6.169  60.614  1.00 19.58  ? 265 SER C C   1 
ATOM   5733  O O   . SER C  1 251 ? 6.292   -5.291  60.397  1.00 19.52  ? 265 SER C O   1 
ATOM   5734  C CB  . SER C  1 251 ? 8.321   -6.620  62.774  1.00 19.66  ? 265 SER C CB  1 
ATOM   5735  O OG  . SER C  1 251 ? 7.248   -6.158  63.573  1.00 19.24  ? 265 SER C OG  1 
ATOM   5736  N N   . LEU C  1 252 ? 7.013   -7.410  60.152  1.00 18.82  ? 266 LEU C N   1 
ATOM   5737  C CA  . LEU C  1 252 ? 5.833   -7.866  59.431  1.00 17.83  ? 266 LEU C CA  1 
ATOM   5738  C C   . LEU C  1 252 ? 5.225   -9.059  60.157  1.00 17.23  ? 266 LEU C C   1 
ATOM   5739  O O   . LEU C  1 252 ? 5.911   -10.047 60.419  1.00 17.92  ? 266 LEU C O   1 
ATOM   5740  C CB  . LEU C  1 252 ? 6.192   -8.247  57.990  1.00 17.68  ? 266 LEU C CB  1 
ATOM   5741  C CG  . LEU C  1 252 ? 5.029   -8.685  57.098  1.00 17.51  ? 266 LEU C CG  1 
ATOM   5742  C CD1 . LEU C  1 252 ? 4.231   -7.480  56.615  1.00 18.75  ? 266 LEU C CD1 1 
ATOM   5743  C CD2 . LEU C  1 252 ? 5.527   -9.507  55.925  1.00 19.33  ? 266 LEU C CD2 1 
ATOM   5744  N N   . GLY C  1 253 ? 3.939   -8.960  60.480  1.00 16.38  ? 267 GLY C N   1 
ATOM   5745  C CA  . GLY C  1 253 ? 3.229   -10.034 61.172  1.00 15.14  ? 267 GLY C CA  1 
ATOM   5746  C C   . GLY C  1 253 ? 2.594   -11.031 60.223  1.00 14.15  ? 267 GLY C C   1 
ATOM   5747  O O   . GLY C  1 253 ? 1.912   -10.649 59.274  1.00 14.38  ? 267 GLY C O   1 
ATOM   5748  N N   . VAL C  1 254 ? 2.826   -12.312 60.485  1.00 13.47  ? 268 VAL C N   1 
ATOM   5749  C CA  . VAL C  1 254 ? 2.255   -13.395 59.692  1.00 13.70  ? 268 VAL C CA  1 
ATOM   5750  C C   . VAL C  1 254 ? 1.474   -14.343 60.600  1.00 13.49  ? 268 VAL C C   1 
ATOM   5751  O O   . VAL C  1 254 ? 1.883   -14.598 61.731  1.00 14.02  ? 268 VAL C O   1 
ATOM   5752  C CB  . VAL C  1 254 ? 3.362   -14.205 58.950  1.00 14.07  ? 268 VAL C CB  1 
ATOM   5753  C CG1 . VAL C  1 254 ? 2.773   -15.393 58.187  1.00 13.29  ? 268 VAL C CG1 1 
ATOM   5754  C CG2 . VAL C  1 254 ? 4.154   -13.312 58.004  1.00 14.33  ? 268 VAL C CG2 1 
ATOM   5755  N N   . GLN C  1 255 ? 0.348   -14.845 60.105  1.00 12.96  ? 269 GLN C N   1 
ATOM   5756  C CA  . GLN C  1 255 ? -0.344  -15.964 60.732  1.00 12.64  ? 269 GLN C CA  1 
ATOM   5757  C C   . GLN C  1 255 ? -0.191  -17.173 59.824  1.00 13.26  ? 269 GLN C C   1 
ATOM   5758  O O   . GLN C  1 255 ? -0.610  -17.126 58.668  1.00 14.04  ? 269 GLN C O   1 
ATOM   5759  C CB  . GLN C  1 255 ? -1.825  -15.649 60.925  1.00 12.25  ? 269 GLN C CB  1 
ATOM   5760  C CG  . GLN C  1 255 ? -2.113  -14.651 62.028  1.00 10.32  ? 269 GLN C CG  1 
ATOM   5761  C CD  . GLN C  1 255 ? -3.590  -14.486 62.287  1.00 7.87   ? 269 GLN C CD  1 
ATOM   5762  O OE1 . GLN C  1 255 ? -4.387  -14.323 61.359  1.00 13.85  ? 269 GLN C OE1 1 
ATOM   5763  N NE2 . GLN C  1 255 ? -3.969  -14.524 63.553  1.00 5.82   ? 269 GLN C NE2 1 
ATOM   5764  N N   . SER C  1 256 ? 0.419   -18.245 60.330  1.00 13.38  ? 270 SER C N   1 
ATOM   5765  C CA  . SER C  1 256 ? 0.681   -19.422 59.498  1.00 13.63  ? 270 SER C CA  1 
ATOM   5766  C C   . SER C  1 256 ? 0.894   -20.728 60.264  1.00 13.87  ? 270 SER C C   1 
ATOM   5767  O O   . SER C  1 256 ? 1.325   -20.730 61.421  1.00 13.51  ? 270 SER C O   1 
ATOM   5768  C CB  . SER C  1 256 ? 1.877   -19.163 58.575  1.00 13.58  ? 270 SER C CB  1 
ATOM   5769  O OG  . SER C  1 256 ? 2.000   -20.192 57.612  1.00 14.31  ? 270 SER C OG  1 
ATOM   5770  N N   . ASP C  1 257 ? 0.580   -21.834 59.590  1.00 14.31  ? 271 ASP C N   1 
ATOM   5771  C CA  . ASP C  1 257 ? 0.844   -23.192 60.081  1.00 15.04  ? 271 ASP C CA  1 
ATOM   5772  C C   . ASP C  1 257 ? 2.110   -23.755 59.427  1.00 14.19  ? 271 ASP C C   1 
ATOM   5773  O O   . ASP C  1 257 ? 2.497   -24.897 59.683  1.00 13.77  ? 271 ASP C O   1 
ATOM   5774  C CB  . ASP C  1 257 ? -0.344  -24.107 59.761  1.00 15.70  ? 271 ASP C CB  1 
ATOM   5775  C CG  . ASP C  1 257 ? -0.645  -24.175 58.261  1.00 20.55  ? 271 ASP C CG  1 
ATOM   5776  O OD1 . ASP C  1 257 ? -1.518  -23.408 57.788  1.00 24.32  ? 271 ASP C OD1 1 
ATOM   5777  O OD2 . ASP C  1 257 ? 0.008   -24.973 57.551  1.00 20.67  ? 271 ASP C OD2 1 
ATOM   5778  N N   . ALA C  1 258 ? 2.736   -22.948 58.570  1.00 13.41  ? 272 ALA C N   1 
ATOM   5779  C CA  . ALA C  1 258 ? 3.906   -23.372 57.808  1.00 12.40  ? 272 ALA C CA  1 
ATOM   5780  C C   . ALA C  1 258 ? 5.183   -23.320 58.645  1.00 11.85  ? 272 ALA C C   1 
ATOM   5781  O O   . ALA C  1 258 ? 5.349   -22.415 59.470  1.00 12.26  ? 272 ALA C O   1 
ATOM   5782  C CB  . ALA C  1 258 ? 4.056   -22.518 56.552  1.00 12.28  ? 272 ALA C CB  1 
ATOM   5783  N N   . PRO C  1 259 ? 6.091   -24.294 58.438  1.00 10.59  ? 273 PRO C N   1 
ATOM   5784  C CA  . PRO C  1 259 ? 7.399   -24.277 59.093  1.00 10.04  ? 273 PRO C CA  1 
ATOM   5785  C C   . PRO C  1 259 ? 8.293   -23.166 58.552  1.00 10.33  ? 273 PRO C C   1 
ATOM   5786  O O   . PRO C  1 259 ? 8.156   -22.771 57.394  1.00 11.04  ? 273 PRO C O   1 
ATOM   5787  C CB  . PRO C  1 259 ? 7.993   -25.636 58.720  1.00 9.98   ? 273 PRO C CB  1 
ATOM   5788  C CG  . PRO C  1 259 ? 7.313   -26.009 57.447  1.00 11.18  ? 273 PRO C CG  1 
ATOM   5789  C CD  . PRO C  1 259 ? 5.918   -25.484 57.585  1.00 10.50  ? 273 PRO C CD  1 
ATOM   5790  N N   . LEU C  1 260 ? 9.196   -22.664 59.390  1.00 10.59  ? 274 LEU C N   1 
ATOM   5791  C CA  . LEU C  1 260 ? 10.184  -21.681 58.954  1.00 9.78   ? 274 LEU C CA  1 
ATOM   5792  C C   . LEU C  1 260 ? 11.302  -22.368 58.185  1.00 9.92   ? 274 LEU C C   1 
ATOM   5793  O O   . LEU C  1 260 ? 11.697  -23.496 58.506  1.00 9.06   ? 274 LEU C O   1 
ATOM   5794  C CB  . LEU C  1 260 ? 10.783  -20.930 60.144  1.00 9.77   ? 274 LEU C CB  1 
ATOM   5795  C CG  . LEU C  1 260 ? 9.882   -20.400 61.262  1.00 10.24  ? 274 LEU C CG  1 
ATOM   5796  C CD1 . LEU C  1 260 ? 10.725  -19.684 62.299  1.00 8.34   ? 274 LEU C CD1 1 
ATOM   5797  C CD2 . LEU C  1 260 ? 8.800   -19.477 60.722  1.00 10.56  ? 274 LEU C CD2 1 
ATOM   5798  N N   . ASP C  1 261 ? 11.807  -21.684 57.165  1.00 10.31  ? 275 ASP C N   1 
ATOM   5799  C CA  . ASP C  1 261 ? 12.968  -22.166 56.432  1.00 10.37  ? 275 ASP C CA  1 
ATOM   5800  C C   . ASP C  1 261 ? 13.927  -21.017 56.137  1.00 10.07  ? 275 ASP C C   1 
ATOM   5801  O O   . ASP C  1 261 ? 13.608  -20.097 55.379  1.00 9.58   ? 275 ASP C O   1 
ATOM   5802  C CB  . ASP C  1 261 ? 12.550  -22.883 55.148  1.00 10.14  ? 275 ASP C CB  1 
ATOM   5803  C CG  . ASP C  1 261 ? 13.663  -23.732 54.567  1.00 12.27  ? 275 ASP C CG  1 
ATOM   5804  O OD1 . ASP C  1 261 ? 14.839  -23.311 54.619  1.00 13.62  ? 275 ASP C OD1 1 
ATOM   5805  O OD2 . ASP C  1 261 ? 13.362  -24.830 54.056  1.00 17.99  ? 275 ASP C OD2 1 
ATOM   5806  N N   . SER C  1 262 ? 15.105  -21.088 56.748  1.00 10.01  ? 276 SER C N   1 
ATOM   5807  C CA  . SER C  1 262 ? 16.105  -20.031 56.627  1.00 10.56  ? 276 SER C CA  1 
ATOM   5808  C C   . SER C  1 262 ? 17.008  -20.195 55.399  1.00 10.90  ? 276 SER C C   1 
ATOM   5809  O O   . SER C  1 262 ? 18.026  -19.507 55.278  1.00 10.76  ? 276 SER C O   1 
ATOM   5810  C CB  . SER C  1 262 ? 16.945  -19.952 57.904  1.00 10.04  ? 276 SER C CB  1 
ATOM   5811  O OG  . SER C  1 262 ? 17.540  -21.202 58.187  1.00 7.10   ? 276 SER C OG  1 
ATOM   5812  N N   . SER C  1 263 A 16.630  -21.093 54.492  1.00 11.25  ? 276 SER C N   1 
ATOM   5813  C CA  . SER C  1 263 A 17.416  -21.345 53.284  1.00 12.09  ? 276 SER C CA  1 
ATOM   5814  C C   . SER C  1 263 A 16.757  -20.815 52.003  1.00 12.63  ? 276 SER C C   1 
ATOM   5815  O O   . SER C  1 263 A 17.354  -20.884 50.924  1.00 12.25  ? 276 SER C O   1 
ATOM   5816  C CB  . SER C  1 263 A 17.751  -22.832 53.150  1.00 12.12  ? 276 SER C CB  1 
ATOM   5817  O OG  . SER C  1 263 A 16.622  -23.575 52.730  1.00 13.24  ? 276 SER C OG  1 
ATOM   5818  N N   . CYS C  1 264 ? 15.531  -20.308 52.127  1.00 13.36  ? 277 CYS C N   1 
ATOM   5819  C CA  . CYS C  1 264 ? 14.858  -19.620 51.028  1.00 14.96  ? 277 CYS C CA  1 
ATOM   5820  C C   . CYS C  1 264 ? 14.528  -18.185 51.425  1.00 15.84  ? 277 CYS C C   1 
ATOM   5821  O O   . CYS C  1 264 ? 14.144  -17.921 52.566  1.00 15.53  ? 277 CYS C O   1 
ATOM   5822  C CB  . CYS C  1 264 ? 13.592  -20.369 50.567  1.00 15.28  ? 277 CYS C CB  1 
ATOM   5823  S SG  . CYS C  1 264 ? 12.312  -20.708 51.837  1.00 18.80  ? 277 CYS C SG  1 
ATOM   5824  N N   . ARG C  1 265 ? 14.695  -17.262 50.480  1.00 17.09  ? 278 ARG C N   1 
ATOM   5825  C CA  . ARG C  1 265 ? 14.373  -15.855 50.703  1.00 17.87  ? 278 ARG C CA  1 
ATOM   5826  C C   . ARG C  1 265 ? 12.974  -15.539 50.162  1.00 18.27  ? 278 ARG C C   1 
ATOM   5827  O O   . ARG C  1 265 ? 12.571  -16.066 49.124  1.00 18.01  ? 278 ARG C O   1 
ATOM   5828  C CB  . ARG C  1 265 ? 15.437  -14.952 50.061  1.00 17.71  ? 278 ARG C CB  1 
ATOM   5829  C CG  . ARG C  1 265 ? 15.393  -13.492 50.519  1.00 20.44  ? 278 ARG C CG  1 
ATOM   5830  C CD  . ARG C  1 265 ? 16.569  -12.677 49.982  1.00 24.69  ? 278 ARG C CD  1 
ATOM   5831  N NE  . ARG C  1 265 ? 17.752  -12.753 50.844  1.00 28.60  ? 278 ARG C NE  1 
ATOM   5832  C CZ  . ARG C  1 265 ? 18.829  -13.501 50.601  1.00 28.22  ? 278 ARG C CZ  1 
ATOM   5833  N NH1 . ARG C  1 265 ? 18.901  -14.256 49.508  1.00 28.49  ? 278 ARG C NH1 1 
ATOM   5834  N NH2 . ARG C  1 265 ? 19.842  -13.493 51.457  1.00 22.93  ? 278 ARG C NH2 1 
ATOM   5835  N N   . GLY C  1 266 ? 12.240  -14.689 50.880  1.00 19.01  ? 279 GLY C N   1 
ATOM   5836  C CA  . GLY C  1 266 ? 10.893  -14.276 50.475  1.00 19.47  ? 279 GLY C CA  1 
ATOM   5837  C C   . GLY C  1 266 ? 10.470  -12.944 51.073  1.00 20.26  ? 279 GLY C C   1 
ATOM   5838  O O   . GLY C  1 266 ? 11.094  -12.453 52.015  1.00 20.55  ? 279 GLY C O   1 
ATOM   5839  N N   . ASP C  1 267 ? 9.401   -12.366 50.525  1.00 20.60  ? 280 ASP C N   1 
ATOM   5840  C CA  . ASP C  1 267 ? 8.890   -11.064 50.966  1.00 20.84  ? 280 ASP C CA  1 
ATOM   5841  C C   . ASP C  1 267 ? 7.371   -11.024 51.049  1.00 20.05  ? 280 ASP C C   1 
ATOM   5842  O O   . ASP C  1 267 ? 6.795   -10.072 51.579  1.00 20.86  ? 280 ASP C O   1 
ATOM   5843  C CB  . ASP C  1 267 ? 9.365   -9.957  50.025  1.00 21.65  ? 280 ASP C CB  1 
ATOM   5844  C CG  . ASP C  1 267 ? 10.666  -9.336  50.468  1.00 26.63  ? 280 ASP C CG  1 
ATOM   5845  O OD1 . ASP C  1 267 ? 10.631  -8.180  50.947  1.00 34.18  ? 280 ASP C OD1 1 
ATOM   5846  O OD2 . ASP C  1 267 ? 11.719  -10.000 50.347  1.00 31.48  ? 280 ASP C OD2 1 
ATOM   5847  N N   . CYS C  1 268 ? 6.731   -12.051 50.501  1.00 18.77  ? 281 CYS C N   1 
ATOM   5848  C CA  . CYS C  1 268 ? 5.282   -12.162 50.499  1.00 17.10  ? 281 CYS C CA  1 
ATOM   5849  C C   . CYS C  1 268 ? 4.880   -13.443 51.216  1.00 16.62  ? 281 CYS C C   1 
ATOM   5850  O O   . CYS C  1 268 ? 5.361   -14.531 50.885  1.00 16.19  ? 281 CYS C O   1 
ATOM   5851  C CB  . CYS C  1 268 ? 4.756   -12.168 49.064  1.00 16.84  ? 281 CYS C CB  1 
ATOM   5852  S SG  . CYS C  1 268 ? 2.986   -12.454 48.940  1.00 16.34  ? 281 CYS C SG  1 
ATOM   5853  N N   . PHE C  1 269 ? 3.996   -13.311 52.199  1.00 16.48  ? 282 PHE C N   1 
ATOM   5854  C CA  . PHE C  1 269 ? 3.603   -14.446 53.032  1.00 16.08  ? 282 PHE C CA  1 
ATOM   5855  C C   . PHE C  1 269 ? 2.095   -14.555 53.195  1.00 16.35  ? 282 PHE C C   1 
ATOM   5856  O O   . PHE C  1 269 ? 1.370   -13.568 53.078  1.00 17.16  ? 282 PHE C O   1 
ATOM   5857  C CB  . PHE C  1 269 ? 4.262   -14.357 54.414  1.00 15.55  ? 282 PHE C CB  1 
ATOM   5858  C CG  . PHE C  1 269 ? 5.744   -14.139 54.369  1.00 9.97   ? 282 PHE C CG  1 
ATOM   5859  C CD1 . PHE C  1 269 ? 6.616   -15.218 54.259  1.00 6.80   ? 282 PHE C CD1 1 
ATOM   5860  C CD2 . PHE C  1 269 ? 6.270   -12.852 54.440  1.00 7.37   ? 282 PHE C CD2 1 
ATOM   5861  C CE1 . PHE C  1 269 ? 7.995   -15.022 54.216  1.00 4.69   ? 282 PHE C CE1 1 
ATOM   5862  C CE2 . PHE C  1 269 ? 7.648   -12.642 54.401  1.00 9.88   ? 282 PHE C CE2 1 
ATOM   5863  C CZ  . PHE C  1 269 ? 8.512   -13.731 54.287  1.00 7.93   ? 282 PHE C CZ  1 
ATOM   5864  N N   . HIS C  1 270 ? 1.638   -15.770 53.473  1.00 16.06  ? 283 HIS C N   1 
ATOM   5865  C CA  . HIS C  1 270 ? 0.236   -16.045 53.753  1.00 15.54  ? 283 HIS C CA  1 
ATOM   5866  C C   . HIS C  1 270 ? 0.185   -17.272 54.653  1.00 15.51  ? 283 HIS C C   1 
ATOM   5867  O O   . HIS C  1 270 ? 1.229   -17.840 54.975  1.00 16.04  ? 283 HIS C O   1 
ATOM   5868  C CB  . HIS C  1 270 ? -0.532  -16.280 52.453  1.00 15.16  ? 283 HIS C CB  1 
ATOM   5869  C CG  . HIS C  1 270 ? -0.022  -17.437 51.652  1.00 14.26  ? 283 HIS C CG  1 
ATOM   5870  N ND1 . HIS C  1 270 ? -0.772  -18.570 51.422  1.00 12.89  ? 283 HIS C ND1 1 
ATOM   5871  C CD2 . HIS C  1 270 ? 1.167   -17.640 51.037  1.00 11.67  ? 283 HIS C CD2 1 
ATOM   5872  C CE1 . HIS C  1 270 ? -0.071  -19.418 50.692  1.00 12.03  ? 283 HIS C CE1 1 
ATOM   5873  N NE2 . HIS C  1 270 ? 1.110   -18.879 50.447  1.00 12.30  ? 283 HIS C NE2 1 
ATOM   5874  N N   . SER C  1 271 ? -1.015  -17.684 55.055  1.00 15.75  ? 284 SER C N   1 
ATOM   5875  C CA  . SER C  1 271 ? -1.173  -18.820 55.969  1.00 17.01  ? 284 SER C CA  1 
ATOM   5876  C C   . SER C  1 271 ? -0.568  -20.118 55.441  1.00 17.40  ? 284 SER C C   1 
ATOM   5877  O O   . SER C  1 271 ? -0.115  -20.953 56.222  1.00 18.25  ? 284 SER C O   1 
ATOM   5878  C CB  . SER C  1 271 ? -2.645  -19.042 56.313  1.00 17.09  ? 284 SER C CB  1 
ATOM   5879  O OG  . SER C  1 271 ? -3.414  -19.237 55.143  1.00 19.99  ? 284 SER C OG  1 
ATOM   5880  N N   . GLY C  1 272 ? -0.563  -20.276 54.119  1.00 17.42  ? 285 GLY C N   1 
ATOM   5881  C CA  . GLY C  1 272 ? -0.043  -21.480 53.480  1.00 16.89  ? 285 GLY C CA  1 
ATOM   5882  C C   . GLY C  1 272 ? 1.417   -21.422 53.062  1.00 17.15  ? 285 GLY C C   1 
ATOM   5883  O O   . GLY C  1 272 ? 1.888   -22.310 52.346  1.00 17.67  ? 285 GLY C O   1 
ATOM   5884  N N   . GLY C  1 273 ? 2.133   -20.382 53.493  1.00 16.92  ? 286 GLY C N   1 
ATOM   5885  C CA  . GLY C  1 273 ? 3.577   -20.291 53.251  1.00 16.81  ? 286 GLY C CA  1 
ATOM   5886  C C   . GLY C  1 273 ? 4.081   -19.003 52.623  1.00 16.95  ? 286 GLY C C   1 
ATOM   5887  O O   . GLY C  1 273 ? 3.660   -17.901 53.007  1.00 17.82  ? 286 GLY C O   1 
ATOM   5888  N N   . THR C  1 274 ? 4.993   -19.148 51.660  1.00 15.60  ? 287 THR C N   1 
ATOM   5889  C CA  . THR C  1 274 ? 5.639   -18.011 51.003  1.00 14.98  ? 287 THR C CA  1 
ATOM   5890  C C   . THR C  1 274 ? 5.407   -18.035 49.497  1.00 15.60  ? 287 THR C C   1 
ATOM   5891  O O   . THR C  1 274 ? 5.468   -19.094 48.866  1.00 16.47  ? 287 THR C O   1 
ATOM   5892  C CB  . THR C  1 274 ? 7.163   -17.989 51.286  1.00 14.71  ? 287 THR C CB  1 
ATOM   5893  O OG1 . THR C  1 274 ? 7.386   -17.985 52.701  1.00 14.23  ? 287 THR C OG1 1 
ATOM   5894  C CG2 . THR C  1 274 ? 7.835   -16.760 50.670  1.00 13.02  ? 287 THR C CG2 1 
ATOM   5895  N N   . ILE C  1 275 ? 5.133   -16.861 48.932  1.00 15.81  ? 288 ILE C N   1 
ATOM   5896  C CA  . ILE C  1 275 ? 5.029   -16.696 47.485  1.00 15.40  ? 288 ILE C CA  1 
ATOM   5897  C C   . ILE C  1 275 ? 6.259   -15.959 46.965  1.00 15.14  ? 288 ILE C C   1 
ATOM   5898  O O   . ILE C  1 275 ? 6.508   -14.801 47.321  1.00 14.75  ? 288 ILE C O   1 
ATOM   5899  C CB  . ILE C  1 275 ? 3.739   -15.944 47.064  1.00 15.45  ? 288 ILE C CB  1 
ATOM   5900  C CG1 . ILE C  1 275 ? 2.492   -16.741 47.458  1.00 14.29  ? 288 ILE C CG1 1 
ATOM   5901  C CG2 . ILE C  1 275 ? 3.741   -15.676 45.555  1.00 16.69  ? 288 ILE C CG2 1 
ATOM   5902  C CD1 . ILE C  1 275 ? 1.196   -15.947 47.420  1.00 12.47  ? 288 ILE C CD1 1 
ATOM   5903  N N   . VAL C  1 276 ? 7.029   -16.651 46.134  1.00 15.47  ? 289 VAL C N   1 
ATOM   5904  C CA  . VAL C  1 276 ? 8.205   -16.078 45.497  1.00 16.16  ? 289 VAL C CA  1 
ATOM   5905  C C   . VAL C  1 276 ? 7.945   -16.060 43.999  1.00 16.24  ? 289 VAL C C   1 
ATOM   5906  O O   . VAL C  1 276 ? 7.808   -17.116 43.369  1.00 16.71  ? 289 VAL C O   1 
ATOM   5907  C CB  . VAL C  1 276 ? 9.492   -16.878 45.832  1.00 16.49  ? 289 VAL C CB  1 
ATOM   5908  C CG1 . VAL C  1 276 ? 10.677  -16.392 44.995  1.00 17.50  ? 289 VAL C CG1 1 
ATOM   5909  C CG2 . VAL C  1 276 ? 9.813   -16.774 47.318  1.00 15.96  ? 289 VAL C CG2 1 
ATOM   5910  N N   . SER C  1 277 ? 7.863   -14.852 43.445  1.00 15.51  ? 290 SER C N   1 
ATOM   5911  C CA  . SER C  1 277 ? 7.482   -14.660 42.052  1.00 15.03  ? 290 SER C CA  1 
ATOM   5912  C C   . SER C  1 277 ? 7.780   -13.253 41.573  1.00 15.37  ? 290 SER C C   1 
ATOM   5913  O O   . SER C  1 277 ? 7.654   -12.290 42.327  1.00 15.40  ? 290 SER C O   1 
ATOM   5914  C CB  . SER C  1 277 ? 5.990   -14.932 41.874  1.00 14.71  ? 290 SER C CB  1 
ATOM   5915  O OG  . SER C  1 277 ? 5.604   -14.776 40.523  1.00 15.19  ? 290 SER C OG  1 
ATOM   5916  N N   . SER C  1 278 ? 8.165   -13.145 40.307  1.00 16.13  ? 291 SER C N   1 
ATOM   5917  C CA  . SER C  1 278 ? 8.300   -11.852 39.647  1.00 16.65  ? 291 SER C CA  1 
ATOM   5918  C C   . SER C  1 278 ? 7.024   -11.479 38.884  1.00 15.44  ? 291 SER C C   1 
ATOM   5919  O O   . SER C  1 278 ? 6.900   -10.361 38.372  1.00 15.71  ? 291 SER C O   1 
ATOM   5920  C CB  . SER C  1 278 ? 9.506   -11.856 38.707  1.00 17.03  ? 291 SER C CB  1 
ATOM   5921  O OG  . SER C  1 278 ? 10.680  -11.456 39.394  1.00 21.36  ? 291 SER C OG  1 
ATOM   5922  N N   . LEU C  1 279 ? 6.079   -12.418 38.827  1.00 13.72  ? 292 LEU C N   1 
ATOM   5923  C CA  . LEU C  1 279 ? 4.840   -12.247 38.065  1.00 12.83  ? 292 LEU C CA  1 
ATOM   5924  C C   . LEU C  1 279 ? 3.879   -11.249 38.724  1.00 13.05  ? 292 LEU C C   1 
ATOM   5925  O O   . LEU C  1 279 ? 3.850   -11.132 39.952  1.00 13.33  ? 292 LEU C O   1 
ATOM   5926  C CB  . LEU C  1 279 ? 4.151   -13.601 37.830  1.00 11.88  ? 292 LEU C CB  1 
ATOM   5927  C CG  . LEU C  1 279 ? 4.968   -14.748 37.207  1.00 9.41   ? 292 LEU C CG  1 
ATOM   5928  C CD1 . LEU C  1 279 ? 4.061   -15.922 36.851  1.00 4.63   ? 292 LEU C CD1 1 
ATOM   5929  C CD2 . LEU C  1 279 ? 5.764   -14.302 35.982  1.00 4.61   ? 292 LEU C CD2 1 
ATOM   5930  N N   . PRO C  1 280 ? 3.097   -10.519 37.905  1.00 12.87  ? 293 PRO C N   1 
ATOM   5931  C CA  . PRO C  1 280 ? 2.195   -9.475  38.405  1.00 12.29  ? 293 PRO C CA  1 
ATOM   5932  C C   . PRO C  1 280 ? 1.011   -9.988  39.240  1.00 12.23  ? 293 PRO C C   1 
ATOM   5933  O O   . PRO C  1 280 ? 0.565   -9.291  40.158  1.00 12.46  ? 293 PRO C O   1 
ATOM   5934  C CB  . PRO C  1 280 ? 1.692   -8.805  37.122  1.00 12.01  ? 293 PRO C CB  1 
ATOM   5935  C CG  . PRO C  1 280 ? 1.839   -9.838  36.070  1.00 11.56  ? 293 PRO C CG  1 
ATOM   5936  C CD  . PRO C  1 280 ? 3.062   -10.610 36.433  1.00 12.93  ? 293 PRO C CD  1 
ATOM   5937  N N   . PHE C  1 281 ? 0.517   -11.187 38.929  1.00 11.35  ? 294 PHE C N   1 
ATOM   5938  C CA  . PHE C  1 281 ? -0.657  -11.744 39.610  1.00 11.19  ? 294 PHE C CA  1 
ATOM   5939  C C   . PHE C  1 281 ? -0.410  -13.124 40.225  1.00 11.44  ? 294 PHE C C   1 
ATOM   5940  O O   . PHE C  1 281 ? 0.581   -13.791 39.907  1.00 11.25  ? 294 PHE C O   1 
ATOM   5941  C CB  . PHE C  1 281 ? -1.854  -11.792 38.654  1.00 10.68  ? 294 PHE C CB  1 
ATOM   5942  C CG  . PHE C  1 281 ? -2.022  -10.545 37.835  1.00 12.20  ? 294 PHE C CG  1 
ATOM   5943  C CD1 . PHE C  1 281 ? -1.659  -10.529 36.493  1.00 13.65  ? 294 PHE C CD1 1 
ATOM   5944  C CD2 . PHE C  1 281 ? -2.523  -9.381  38.407  1.00 11.20  ? 294 PHE C CD2 1 
ATOM   5945  C CE1 . PHE C  1 281 ? -1.801  -9.377  35.733  1.00 12.50  ? 294 PHE C CE1 1 
ATOM   5946  C CE2 . PHE C  1 281 ? -2.671  -8.224  37.654  1.00 10.08  ? 294 PHE C CE2 1 
ATOM   5947  C CZ  . PHE C  1 281 ? -2.306  -8.220  36.316  1.00 11.10  ? 294 PHE C CZ  1 
ATOM   5948  N N   . GLN C  1 282 ? -1.319  -13.539 41.109  1.00 11.04  ? 295 GLN C N   1 
ATOM   5949  C CA  . GLN C  1 282 ? -1.254  -14.856 41.749  1.00 10.08  ? 295 GLN C CA  1 
ATOM   5950  C C   . GLN C  1 282 ? -2.642  -15.423 42.061  1.00 10.33  ? 295 GLN C C   1 
ATOM   5951  O O   . GLN C  1 282 ? -3.565  -14.673 42.380  1.00 11.16  ? 295 GLN C O   1 
ATOM   5952  C CB  . GLN C  1 282 ? -0.384  -14.808 43.011  1.00 9.82   ? 295 GLN C CB  1 
ATOM   5953  C CG  . GLN C  1 282 ? -0.742  -13.714 44.021  1.00 9.55   ? 295 GLN C CG  1 
ATOM   5954  C CD  . GLN C  1 282 ? -1.684  -14.183 45.125  1.00 10.74  ? 295 GLN C CD  1 
ATOM   5955  O OE1 . GLN C  1 282 ? -2.108  -15.343 45.163  1.00 10.35  ? 295 GLN C OE1 1 
ATOM   5956  N NE2 . GLN C  1 282 ? -2.013  -13.272 46.037  1.00 10.43  ? 295 GLN C NE2 1 
ATOM   5957  N N   . ASN C  1 283 ? -2.784  -16.744 41.949  1.00 9.44   ? 296 ASN C N   1 
ATOM   5958  C CA  . ASN C  1 283 ? -4.029  -17.433 42.288  1.00 8.15   ? 296 ASN C CA  1 
ATOM   5959  C C   . ASN C  1 283 ? -3.831  -18.347 43.503  1.00 8.34   ? 296 ASN C C   1 
ATOM   5960  O O   . ASN C  1 283 ? -4.509  -19.367 43.656  1.00 7.90   ? 296 ASN C O   1 
ATOM   5961  C CB  . ASN C  1 283 ? -4.545  -18.230 41.084  1.00 7.62   ? 296 ASN C CB  1 
ATOM   5962  C CG  . ASN C  1 283 ? -5.990  -18.701 41.255  1.00 8.64   ? 296 ASN C CG  1 
ATOM   5963  O OD1 . ASN C  1 283 ? -6.809  -18.027 41.882  1.00 8.05   ? 296 ASN C OD1 1 
ATOM   5964  N ND2 . ASN C  1 283 ? -6.305  -19.861 40.685  1.00 8.24   ? 296 ASN C ND2 1 
ATOM   5965  N N   . ILE C  1 284 ? -2.903  -17.963 44.373  1.00 8.60   ? 297 ILE C N   1 
ATOM   5966  C CA  . ILE C  1 284 ? -2.503  -18.817 45.492  1.00 9.44   ? 297 ILE C CA  1 
ATOM   5967  C C   . ILE C  1 284 ? -3.330  -18.576 46.759  1.00 10.38  ? 297 ILE C C   1 
ATOM   5968  O O   . ILE C  1 284 ? -3.848  -19.524 47.349  1.00 10.67  ? 297 ILE C O   1 
ATOM   5969  C CB  . ILE C  1 284 ? -0.979  -18.708 45.774  1.00 8.98   ? 297 ILE C CB  1 
ATOM   5970  C CG1 . ILE C  1 284 ? -0.189  -19.327 44.611  1.00 5.95   ? 297 ILE C CG1 1 
ATOM   5971  C CG2 . ILE C  1 284 ? -0.624  -19.386 47.095  1.00 8.04   ? 297 ILE C CG2 1 
ATOM   5972  C CD1 . ILE C  1 284 ? 1.276   -18.935 44.557  1.00 5.06   ? 297 ILE C CD1 1 
ATOM   5973  N N   . ASN C  1 285 ? -3.448  -17.312 47.164  1.00 11.24  ? 298 ASN C N   1 
ATOM   5974  C CA  . ASN C  1 285 ? -4.207  -16.937 48.354  1.00 12.62  ? 298 ASN C CA  1 
ATOM   5975  C C   . ASN C  1 285 ? -4.688  -15.490 48.286  1.00 13.48  ? 298 ASN C C   1 
ATOM   5976  O O   . ASN C  1 285 ? -3.897  -14.579 48.037  1.00 13.77  ? 298 ASN C O   1 
ATOM   5977  C CB  . ASN C  1 285 ? -3.366  -17.153 49.618  1.00 13.35  ? 298 ASN C CB  1 
ATOM   5978  C CG  . ASN C  1 285 ? -4.209  -17.231 50.883  1.00 15.79  ? 298 ASN C CG  1 
ATOM   5979  O OD1 . ASN C  1 285 ? -5.375  -16.826 50.905  1.00 18.35  ? 298 ASN C OD1 1 
ATOM   5980  N ND2 . ASN C  1 285 ? -3.617  -17.756 51.947  1.00 18.60  ? 298 ASN C ND2 1 
ATOM   5981  N N   . SER C  1 286 ? -5.986  -15.285 48.507  1.00 14.29  ? 299 SER C N   1 
ATOM   5982  C CA  . SER C  1 286 ? -6.579  -13.941 48.475  1.00 14.08  ? 299 SER C CA  1 
ATOM   5983  C C   . SER C  1 286 ? -6.218  -13.101 49.700  1.00 13.81  ? 299 SER C C   1 
ATOM   5984  O O   . SER C  1 286 ? -6.368  -11.880 49.680  1.00 14.26  ? 299 SER C O   1 
ATOM   5985  C CB  . SER C  1 286 ? -8.100  -14.015 48.310  1.00 13.93  ? 299 SER C CB  1 
ATOM   5986  O OG  . SER C  1 286 ? -8.700  -14.710 49.386  1.00 14.32  ? 299 SER C OG  1 
ATOM   5987  N N   . ARG C  1 287 ? -5.755  -13.761 50.760  1.00 13.35  ? 300 ARG C N   1 
ATOM   5988  C CA  . ARG C  1 287 ? -5.289  -13.075 51.960  1.00 13.19  ? 300 ARG C CA  1 
ATOM   5989  C C   . ARG C  1 287 ? -3.786  -13.269 52.069  1.00 12.43  ? 300 ARG C C   1 
ATOM   5990  O O   . ARG C  1 287 ? -3.317  -14.383 52.305  1.00 12.45  ? 300 ARG C O   1 
ATOM   5991  C CB  . ARG C  1 287 ? -5.998  -13.606 53.213  1.00 13.19  ? 300 ARG C CB  1 
ATOM   5992  C CG  . ARG C  1 287 ? -7.515  -13.398 53.225  1.00 17.50  ? 300 ARG C CG  1 
ATOM   5993  C CD  . ARG C  1 287 ? -8.214  -14.164 54.349  1.00 18.85  ? 300 ARG C CD  1 
ATOM   5994  N NE  . ARG C  1 287 ? -7.985  -13.566 55.665  1.00 22.59  ? 300 ARG C NE  1 
ATOM   5995  C CZ  . ARG C  1 287 ? -7.046  -13.959 56.525  1.00 25.46  ? 300 ARG C CZ  1 
ATOM   5996  N NH1 . ARG C  1 287 ? -6.225  -14.958 56.224  1.00 26.91  ? 300 ARG C NH1 1 
ATOM   5997  N NH2 . ARG C  1 287 ? -6.922  -13.349 57.695  1.00 26.02  ? 300 ARG C NH2 1 
ATOM   5998  N N   . THR C  1 288 ? -3.041  -12.184 51.866  1.00 11.82  ? 301 THR C N   1 
ATOM   5999  C CA  . THR C  1 288 ? -1.577  -12.205 51.916  1.00 11.52  ? 301 THR C CA  1 
ATOM   6000  C C   . THR C  1 288 ? -1.072  -11.060 52.782  1.00 11.84  ? 301 THR C C   1 
ATOM   6001  O O   . THR C  1 288 ? -1.842  -10.178 53.166  1.00 12.52  ? 301 THR C O   1 
ATOM   6002  C CB  . THR C  1 288 ? -0.930  -12.062 50.505  1.00 11.57  ? 301 THR C CB  1 
ATOM   6003  O OG1 . THR C  1 288 ? -1.277  -10.794 49.933  1.00 13.69  ? 301 THR C OG1 1 
ATOM   6004  C CG2 . THR C  1 288 ? -1.366  -13.175 49.562  1.00 8.94   ? 301 THR C CG2 1 
ATOM   6005  N N   . VAL C  1 289 ? 0.223   -11.081 53.089  1.00 11.62  ? 302 VAL C N   1 
ATOM   6006  C CA  . VAL C  1 289 ? 0.873   -10.004 53.835  1.00 12.22  ? 302 VAL C CA  1 
ATOM   6007  C C   . VAL C  1 289 ? 2.252   -9.742  53.237  1.00 13.21  ? 302 VAL C C   1 
ATOM   6008  O O   . VAL C  1 289 ? 2.862   -10.643 52.656  1.00 13.78  ? 302 VAL C O   1 
ATOM   6009  C CB  . VAL C  1 289 ? 0.990   -10.303 55.369  1.00 12.21  ? 302 VAL C CB  1 
ATOM   6010  C CG1 . VAL C  1 289 ? -0.386  -10.494 56.007  1.00 11.50  ? 302 VAL C CG1 1 
ATOM   6011  C CG2 . VAL C  1 289 ? 1.875   -11.513 55.640  1.00 13.15  ? 302 VAL C CG2 1 
ATOM   6012  N N   . GLY C  1 290 ? 2.741   -8.513  53.376  1.00 13.50  ? 303 GLY C N   1 
ATOM   6013  C CA  . GLY C  1 290 ? 4.034   -8.140  52.809  1.00 13.67  ? 303 GLY C CA  1 
ATOM   6014  C C   . GLY C  1 290 ? 3.897   -7.598  51.401  1.00 14.24  ? 303 GLY C C   1 
ATOM   6015  O O   . GLY C  1 290 ? 2.849   -7.054  51.041  1.00 15.56  ? 303 GLY C O   1 
ATOM   6016  N N   . LYS C  1 291 ? 4.955   -7.750  50.607  1.00 13.83  ? 304 LYS C N   1 
ATOM   6017  C CA  . LYS C  1 291 ? 5.001   -7.208  49.248  1.00 13.79  ? 304 LYS C CA  1 
ATOM   6018  C C   . LYS C  1 291 ? 4.700   -8.298  48.220  1.00 13.76  ? 304 LYS C C   1 
ATOM   6019  O O   . LYS C  1 291 ? 5.557   -9.131  47.904  1.00 13.96  ? 304 LYS C O   1 
ATOM   6020  C CB  . LYS C  1 291 ? 6.350   -6.528  48.982  1.00 14.01  ? 304 LYS C CB  1 
ATOM   6021  C CG  . LYS C  1 291 ? 6.528   -5.203  49.725  1.00 15.69  ? 304 LYS C CG  1 
ATOM   6022  C CD  . LYS C  1 291 ? 7.777   -4.446  49.271  1.00 21.81  ? 304 LYS C CD  1 
ATOM   6023  C CE  . LYS C  1 291 ? 8.990   -4.730  50.157  1.00 26.51  ? 304 LYS C CE  1 
ATOM   6024  N NZ  . LYS C  1 291 ? 8.950   -3.968  51.442  1.00 24.03  ? 304 LYS C NZ  1 
ATOM   6025  N N   . CYS C  1 292 ? 3.474   -8.272  47.700  1.00 13.84  ? 305 CYS C N   1 
ATOM   6026  C CA  . CYS C  1 292 ? 2.899   -9.403  46.966  1.00 14.16  ? 305 CYS C CA  1 
ATOM   6027  C C   . CYS C  1 292 ? 2.355   -9.069  45.574  1.00 13.66  ? 305 CYS C C   1 
ATOM   6028  O O   . CYS C  1 292 ? 1.901   -7.947  45.332  1.00 14.00  ? 305 CYS C O   1 
ATOM   6029  C CB  . CYS C  1 292 ? 1.746   -9.998  47.781  1.00 14.56  ? 305 CYS C CB  1 
ATOM   6030  S SG  . CYS C  1 292 ? 2.202   -10.642 49.389  1.00 18.41  ? 305 CYS C SG  1 
ATOM   6031  N N   . PRO C  1 293 ? 2.369   -10.060 44.658  1.00 13.03  ? 306 PRO C N   1 
ATOM   6032  C CA  . PRO C  1 293 ? 1.551   -9.923  43.453  1.00 12.79  ? 306 PRO C CA  1 
ATOM   6033  C C   . PRO C  1 293 ? 0.078   -9.857  43.835  1.00 12.48  ? 306 PRO C C   1 
ATOM   6034  O O   . PRO C  1 293 ? -0.337  -10.439 44.841  1.00 12.80  ? 306 PRO C O   1 
ATOM   6035  C CB  . PRO C  1 293 ? 1.821   -11.222 42.687  1.00 12.91  ? 306 PRO C CB  1 
ATOM   6036  C CG  . PRO C  1 293 ? 3.092   -11.757 43.249  1.00 11.92  ? 306 PRO C CG  1 
ATOM   6037  C CD  . PRO C  1 293 ? 3.119   -11.329 44.675  1.00 12.70  ? 306 PRO C CD  1 
ATOM   6038  N N   . ARG C  1 294 ? -0.702  -9.149  43.034  1.00 12.47  ? 307 ARG C N   1 
ATOM   6039  C CA  . ARG C  1 294 ? -2.125  -8.987  43.294  1.00 12.25  ? 307 ARG C CA  1 
ATOM   6040  C C   . ARG C  1 294 ? -2.889  -10.282 43.024  1.00 10.82  ? 307 ARG C C   1 
ATOM   6041  O O   . ARG C  1 294 ? -2.655  -10.953 42.018  1.00 10.51  ? 307 ARG C O   1 
ATOM   6042  C CB  . ARG C  1 294 ? -2.664  -7.826  42.461  1.00 12.72  ? 307 ARG C CB  1 
ATOM   6043  C CG  . ARG C  1 294 ? -2.159  -6.474  42.959  1.00 19.26  ? 307 ARG C CG  1 
ATOM   6044  C CD  . ARG C  1 294 ? -1.599  -5.597  41.838  1.00 28.45  ? 307 ARG C CD  1 
ATOM   6045  N NE  . ARG C  1 294 ? -0.345  -6.101  41.276  1.00 32.49  ? 307 ARG C NE  1 
ATOM   6046  C CZ  . ARG C  1 294 ? 0.443   -5.421  40.442  1.00 37.37  ? 307 ARG C CZ  1 
ATOM   6047  N NH1 . ARG C  1 294 ? 0.135   -4.180  40.058  1.00 34.80  ? 307 ARG C NH1 1 
ATOM   6048  N NH2 . ARG C  1 294 ? 1.557   -5.985  39.996  1.00 40.58  ? 307 ARG C NH2 1 
ATOM   6049  N N   . TYR C  1 295 ? -3.781  -10.643 43.941  1.00 9.67   ? 308 TYR C N   1 
ATOM   6050  C CA  . TYR C  1 295 ? -4.584  -11.849 43.777  1.00 9.20   ? 308 TYR C CA  1 
ATOM   6051  C C   . TYR C  1 295 ? -5.613  -11.677 42.666  1.00 9.88   ? 308 TYR C C   1 
ATOM   6052  O O   . TYR C  1 295 ? -6.229  -10.614 42.536  1.00 9.80   ? 308 TYR C O   1 
ATOM   6053  C CB  . TYR C  1 295 ? -5.279  -12.243 45.085  1.00 8.75   ? 308 TYR C CB  1 
ATOM   6054  C CG  . TYR C  1 295 ? -6.152  -13.477 44.964  1.00 8.46   ? 308 TYR C CG  1 
ATOM   6055  C CD1 . TYR C  1 295 ? -5.604  -14.762 45.070  1.00 8.14   ? 308 TYR C CD1 1 
ATOM   6056  C CD2 . TYR C  1 295 ? -7.526  -13.363 44.733  1.00 4.68   ? 308 TYR C CD2 1 
ATOM   6057  C CE1 . TYR C  1 295 ? -6.404  -15.905 44.957  1.00 6.28   ? 308 TYR C CE1 1 
ATOM   6058  C CE2 . TYR C  1 295 ? -8.333  -14.497 44.616  1.00 8.60   ? 308 TYR C CE2 1 
ATOM   6059  C CZ  . TYR C  1 295 ? -7.767  -15.763 44.731  1.00 10.28  ? 308 TYR C CZ  1 
ATOM   6060  O OH  . TYR C  1 295 ? -8.566  -16.877 44.617  1.00 8.07   ? 308 TYR C OH  1 
ATOM   6061  N N   . VAL C  1 296 ? -5.775  -12.732 41.868  1.00 10.35  ? 309 VAL C N   1 
ATOM   6062  C CA  . VAL C  1 296 ? -6.800  -12.804 40.825  1.00 10.78  ? 309 VAL C CA  1 
ATOM   6063  C C   . VAL C  1 296 ? -7.574  -14.125 40.934  1.00 11.92  ? 309 VAL C C   1 
ATOM   6064  O O   . VAL C  1 296 ? -7.086  -15.087 41.535  1.00 12.36  ? 309 VAL C O   1 
ATOM   6065  C CB  . VAL C  1 296 ? -6.198  -12.649 39.395  1.00 10.53  ? 309 VAL C CB  1 
ATOM   6066  C CG1 . VAL C  1 296 ? -5.638  -11.247 39.188  1.00 6.55   ? 309 VAL C CG1 1 
ATOM   6067  C CG2 . VAL C  1 296 ? -5.125  -13.700 39.132  1.00 9.52   ? 309 VAL C CG2 1 
ATOM   6068  N N   . LYS C  1 297 ? -8.774  -14.164 40.356  1.00 12.75  ? 310 LYS C N   1 
ATOM   6069  C CA  . LYS C  1 297 ? -9.602  -15.373 40.348  1.00 13.44  ? 310 LYS C CA  1 
ATOM   6070  C C   . LYS C  1 297 ? -9.133  -16.410 39.323  1.00 14.10  ? 310 LYS C C   1 
ATOM   6071  O O   . LYS C  1 297 ? -9.343  -17.612 39.517  1.00 14.55  ? 310 LYS C O   1 
ATOM   6072  C CB  . LYS C  1 297 ? -11.068 -15.030 40.079  1.00 13.47  ? 310 LYS C CB  1 
ATOM   6073  C CG  . LYS C  1 297 ? -11.775 -14.289 41.208  1.00 17.66  ? 310 LYS C CG  1 
ATOM   6074  C CD  . LYS C  1 297 ? -13.301 -14.466 41.143  1.00 22.60  ? 310 LYS C CD  1 
ATOM   6075  C CE  . LYS C  1 297 ? -13.911 -13.807 39.907  1.00 24.95  ? 310 LYS C CE  1 
ATOM   6076  N NZ  . LYS C  1 297 ? -15.303 -14.274 39.652  1.00 27.24  ? 310 LYS C NZ  1 
ATOM   6077  N N   . GLN C  1 298 ? -8.512  -15.943 38.237  1.00 13.93  ? 311 GLN C N   1 
ATOM   6078  C CA  . GLN C  1 298 ? -8.093  -16.818 37.134  1.00 13.69  ? 311 GLN C CA  1 
ATOM   6079  C C   . GLN C  1 298 ? -6.880  -17.682 37.476  1.00 14.48  ? 311 GLN C C   1 
ATOM   6080  O O   . GLN C  1 298 ? -5.953  -17.233 38.154  1.00 14.18  ? 311 GLN C O   1 
ATOM   6081  C CB  . GLN C  1 298 ? -7.797  -16.014 35.867  1.00 12.79  ? 311 GLN C CB  1 
ATOM   6082  C CG  . GLN C  1 298 ? -8.963  -15.204 35.339  1.00 12.54  ? 311 GLN C CG  1 
ATOM   6083  C CD  . GLN C  1 298 ? -8.941  -13.757 35.806  1.00 12.61  ? 311 GLN C CD  1 
ATOM   6084  O OE1 . GLN C  1 298 ? -8.313  -13.414 36.815  1.00 12.97  ? 311 GLN C OE1 1 
ATOM   6085  N NE2 . GLN C  1 298 ? -9.632  -12.896 35.067  1.00 6.86   ? 311 GLN C NE2 1 
ATOM   6086  N N   . LYS C  1 299 ? -6.897  -18.917 36.980  1.00 15.19  ? 312 LYS C N   1 
ATOM   6087  C CA  . LYS C  1 299 ? -5.838  -19.885 37.246  1.00 15.96  ? 312 LYS C CA  1 
ATOM   6088  C C   . LYS C  1 299 ? -4.607  -19.576 36.408  1.00 15.17  ? 312 LYS C C   1 
ATOM   6089  O O   . LYS C  1 299 ? -3.477  -19.818 36.832  1.00 15.76  ? 312 LYS C O   1 
ATOM   6090  C CB  . LYS C  1 299 ? -6.338  -21.300 36.939  1.00 16.77  ? 312 LYS C CB  1 
ATOM   6091  C CG  . LYS C  1 299 ? -5.668  -22.401 37.764  1.00 22.62  ? 312 LYS C CG  1 
ATOM   6092  C CD  . LYS C  1 299 ? -6.414  -23.746 37.673  1.00 29.85  ? 312 LYS C CD  1 
ATOM   6093  C CE  . LYS C  1 299 ? -7.834  -23.689 38.259  1.00 32.57  ? 312 LYS C CE  1 
ATOM   6094  N NZ  . LYS C  1 299 ? -7.882  -23.188 39.669  1.00 34.56  ? 312 LYS C NZ  1 
ATOM   6095  N N   . SER C  1 300 ? -4.845  -19.029 35.219  1.00 14.43  ? 313 SER C N   1 
ATOM   6096  C CA  . SER C  1 300 ? -3.806  -18.784 34.225  1.00 12.81  ? 313 SER C CA  1 
ATOM   6097  C C   . SER C  1 300 ? -4.237  -17.651 33.295  1.00 11.74  ? 313 SER C C   1 
ATOM   6098  O O   . SER C  1 300 ? -5.396  -17.590 32.878  1.00 11.17  ? 313 SER C O   1 
ATOM   6099  C CB  . SER C  1 300 ? -3.538  -20.070 33.428  1.00 12.74  ? 313 SER C CB  1 
ATOM   6100  O OG  . SER C  1 300 ? -2.907  -19.814 32.181  1.00 12.83  ? 313 SER C OG  1 
ATOM   6101  N N   . LEU C  1 301 ? -3.307  -16.747 32.997  1.00 11.20  ? 314 LEU C N   1 
ATOM   6102  C CA  . LEU C  1 301 ? -3.527  -15.683 32.011  1.00 10.90  ? 314 LEU C CA  1 
ATOM   6103  C C   . LEU C  1 301 ? -2.294  -15.531 31.137  1.00 11.05  ? 314 LEU C C   1 
ATOM   6104  O O   . LEU C  1 301 ? -1.304  -14.911 31.536  1.00 11.19  ? 314 LEU C O   1 
ATOM   6105  C CB  . LEU C  1 301 ? -3.880  -14.347 32.680  1.00 10.18  ? 314 LEU C CB  1 
ATOM   6106  C CG  . LEU C  1 301 ? -5.264  -14.205 33.325  1.00 8.94   ? 314 LEU C CG  1 
ATOM   6107  C CD1 . LEU C  1 301 ? -5.345  -12.923 34.145  1.00 3.69   ? 314 LEU C CD1 1 
ATOM   6108  C CD2 . LEU C  1 301 ? -6.389  -14.271 32.292  1.00 2.88   ? 314 LEU C CD2 1 
ATOM   6109  N N   . LEU C  1 302 ? -2.359  -16.104 29.940  1.00 10.68  ? 315 LEU C N   1 
ATOM   6110  C CA  . LEU C  1 302 ? -1.191  -16.175 29.070  1.00 10.59  ? 315 LEU C CA  1 
ATOM   6111  C C   . LEU C  1 302 ? -0.984  -14.916 28.218  1.00 10.79  ? 315 LEU C C   1 
ATOM   6112  O O   . LEU C  1 302 ? -1.838  -14.535 27.406  1.00 10.40  ? 315 LEU C O   1 
ATOM   6113  C CB  . LEU C  1 302 ? -1.237  -17.441 28.204  1.00 9.90   ? 315 LEU C CB  1 
ATOM   6114  C CG  . LEU C  1 302 ? -1.089  -18.780 28.941  1.00 10.46  ? 315 LEU C CG  1 
ATOM   6115  C CD1 . LEU C  1 302 ? -1.567  -19.946 28.076  1.00 6.56   ? 315 LEU C CD1 1 
ATOM   6116  C CD2 . LEU C  1 302 ? 0.344   -19.007 29.425  1.00 9.84   ? 315 LEU C CD2 1 
ATOM   6117  N N   . LEU C  1 303 ? 0.162   -14.275 28.430  1.00 10.86  ? 316 LEU C N   1 
ATOM   6118  C CA  . LEU C  1 303 ? 0.589   -13.144 27.620  1.00 10.83  ? 316 LEU C CA  1 
ATOM   6119  C C   . LEU C  1 303 ? 1.393   -13.647 26.417  1.00 11.11  ? 316 LEU C C   1 
ATOM   6120  O O   . LEU C  1 303 ? 2.407   -14.343 26.579  1.00 10.73  ? 316 LEU C O   1 
ATOM   6121  C CB  . LEU C  1 303 ? 1.429   -12.183 28.461  1.00 10.07  ? 316 LEU C CB  1 
ATOM   6122  C CG  . LEU C  1 303 ? 1.970   -10.923 27.785  1.00 10.27  ? 316 LEU C CG  1 
ATOM   6123  C CD1 . LEU C  1 303 ? 0.947   -9.810  27.859  1.00 8.58   ? 316 LEU C CD1 1 
ATOM   6124  C CD2 . LEU C  1 303 ? 3.281   -10.493 28.437  1.00 6.11   ? 316 LEU C CD2 1 
ATOM   6125  N N   . ALA C  1 304 ? 0.929   -13.297 25.220  1.00 10.61  ? 317 ALA C N   1 
ATOM   6126  C CA  . ALA C  1 304 ? 1.602   -13.688 23.986  1.00 10.74  ? 317 ALA C CA  1 
ATOM   6127  C C   . ALA C  1 304 ? 2.971   -13.034 23.912  1.00 10.80  ? 317 ALA C C   1 
ATOM   6128  O O   . ALA C  1 304 ? 3.114   -11.842 24.191  1.00 11.61  ? 317 ALA C O   1 
ATOM   6129  C CB  . ALA C  1 304 ? 0.764   -13.307 22.771  1.00 9.97   ? 317 ALA C CB  1 
ATOM   6130  N N   . THR C  1 305 ? 3.978   -13.826 23.558  1.00 10.06  ? 318 THR C N   1 
ATOM   6131  C CA  . THR C  1 305 ? 5.330   -13.309 23.370  1.00 9.14   ? 318 THR C CA  1 
ATOM   6132  C C   . THR C  1 305 ? 5.854   -13.635 21.973  1.00 9.17   ? 318 THR C C   1 
ATOM   6133  O O   . THR C  1 305 ? 7.060   -13.590 21.725  1.00 10.18  ? 318 THR C O   1 
ATOM   6134  C CB  . THR C  1 305 ? 6.299   -13.843 24.437  1.00 8.25   ? 318 THR C CB  1 
ATOM   6135  O OG1 . THR C  1 305 ? 6.234   -15.273 24.464  1.00 10.12  ? 318 THR C OG1 1 
ATOM   6136  C CG2 . THR C  1 305 ? 5.934   -13.291 25.812  1.00 6.19   ? 318 THR C CG2 1 
ATOM   6137  N N   . GLY C  1 306 ? 4.933   -13.955 21.068  1.00 8.33   ? 319 GLY C N   1 
ATOM   6138  C CA  . GLY C  1 306 ? 5.258   -14.267 19.682  1.00 8.46   ? 319 GLY C CA  1 
ATOM   6139  C C   . GLY C  1 306 ? 4.098   -14.001 18.741  1.00 8.92   ? 319 GLY C C   1 
ATOM   6140  O O   . GLY C  1 306 ? 2.974   -13.742 19.184  1.00 9.39   ? 319 GLY C O   1 
ATOM   6141  N N   . MET C  1 307 ? 4.366   -14.073 17.439  1.00 8.76   ? 320 MET C N   1 
ATOM   6142  C CA  . MET C  1 307 ? 3.351   -13.790 16.418  1.00 8.68   ? 320 MET C CA  1 
ATOM   6143  C C   . MET C  1 307 ? 2.230   -14.828 16.385  1.00 9.47   ? 320 MET C C   1 
ATOM   6144  O O   . MET C  1 307 ? 2.280   -15.838 17.092  1.00 10.63  ? 320 MET C O   1 
ATOM   6145  C CB  . MET C  1 307 ? 3.995   -13.697 15.035  1.00 8.45   ? 320 MET C CB  1 
ATOM   6146  C CG  . MET C  1 307 ? 4.547   -15.008 14.504  1.00 5.94   ? 320 MET C CG  1 
ATOM   6147  S SD  . MET C  1 307 ? 5.429   -14.785 12.954  1.00 7.49   ? 320 MET C SD  1 
ATOM   6148  C CE  . MET C  1 307 ? 6.755   -13.686 13.449  1.00 6.64   ? 320 MET C CE  1 
ATOM   6149  N N   . ARG C  1 308 ? 1.224   -14.570 15.554  1.00 9.23   ? 321 ARG C N   1 
ATOM   6150  C CA  . ARG C  1 308 ? 0.167   -15.537 15.306  1.00 9.89   ? 321 ARG C CA  1 
ATOM   6151  C C   . ARG C  1 308 ? 0.774   -16.751 14.610  1.00 9.40   ? 321 ARG C C   1 
ATOM   6152  O O   . ARG C  1 308 ? 1.420   -16.613 13.573  1.00 9.53   ? 321 ARG C O   1 
ATOM   6153  C CB  . ARG C  1 308 ? -0.931  -14.910 14.445  1.00 10.04  ? 321 ARG C CB  1 
ATOM   6154  C CG  . ARG C  1 308 ? -2.331  -15.368 14.807  1.00 12.92  ? 321 ARG C CG  1 
ATOM   6155  C CD  . ARG C  1 308 ? -2.806  -16.498 13.918  1.00 17.72  ? 321 ARG C CD  1 
ATOM   6156  N NE  . ARG C  1 308 ? -3.652  -17.435 14.655  1.00 23.02  ? 321 ARG C NE  1 
ATOM   6157  C CZ  . ARG C  1 308 ? -4.392  -18.390 14.098  1.00 26.69  ? 321 ARG C CZ  1 
ATOM   6158  N NH1 . ARG C  1 308 ? -4.413  -18.547 12.777  1.00 26.52  ? 321 ARG C NH1 1 
ATOM   6159  N NH2 . ARG C  1 308 ? -5.118  -19.193 14.866  1.00 28.62  ? 321 ARG C NH2 1 
ATOM   6160  N N   . ASN C  1 309 ? 0.597   -17.928 15.204  1.00 9.61   ? 322 ASN C N   1 
ATOM   6161  C CA  . ASN C  1 309 ? 1.158   -19.162 14.656  1.00 10.03  ? 322 ASN C CA  1 
ATOM   6162  C C   . ASN C  1 309 ? 0.313   -19.699 13.506  1.00 11.14  ? 322 ASN C C   1 
ATOM   6163  O O   . ASN C  1 309 ? -0.854  -20.057 13.693  1.00 11.85  ? 322 ASN C O   1 
ATOM   6164  C CB  . ASN C  1 309 ? 1.314   -20.228 15.748  1.00 9.35   ? 322 ASN C CB  1 
ATOM   6165  C CG  . ASN C  1 309 ? 2.163   -21.414 15.302  1.00 8.09   ? 322 ASN C CG  1 
ATOM   6166  O OD1 . ASN C  1 309 ? 3.247   -21.245 14.742  1.00 6.52   ? 322 ASN C OD1 1 
ATOM   6167  N ND2 . ASN C  1 309 ? 1.677   -22.620 15.563  1.00 6.56   ? 322 ASN C ND2 1 
ATOM   6168  N N   . VAL C  1 310 ? 0.900   -19.731 12.313  1.00 11.58  ? 323 VAL C N   1 
ATOM   6169  C CA  . VAL C  1 310 ? 0.236   -20.305 11.148  1.00 12.21  ? 323 VAL C CA  1 
ATOM   6170  C C   . VAL C  1 310 ? 1.126   -21.412 10.587  1.00 13.14  ? 323 VAL C C   1 
ATOM   6171  O O   . VAL C  1 310 ? 2.024   -21.146 9.787   1.00 12.33  ? 323 VAL C O   1 
ATOM   6172  C CB  . VAL C  1 310 ? -0.088  -19.251 10.058  1.00 12.21  ? 323 VAL C CB  1 
ATOM   6173  C CG1 . VAL C  1 310 ? -1.112  -19.803 9.075   1.00 11.36  ? 323 VAL C CG1 1 
ATOM   6174  C CG2 . VAL C  1 310 ? -0.604  -17.959 10.680  1.00 10.72  ? 323 VAL C CG2 1 
ATOM   6175  N N   . PRO C  1 311 ? 0.881   -22.662 11.021  1.00 14.78  ? 324 PRO C N   1 
ATOM   6176  C CA  . PRO C  1 311 ? 1.732   -23.793 10.665  1.00 16.18  ? 324 PRO C CA  1 
ATOM   6177  C C   . PRO C  1 311 ? 1.582   -24.230 9.213   1.00 17.91  ? 324 PRO C C   1 
ATOM   6178  O O   . PRO C  1 311 ? 0.645   -23.816 8.524   1.00 17.81  ? 324 PRO C O   1 
ATOM   6179  C CB  . PRO C  1 311 ? 1.257   -24.899 11.613  1.00 15.90  ? 324 PRO C CB  1 
ATOM   6180  C CG  . PRO C  1 311 ? -0.157  -24.565 11.899  1.00 15.52  ? 324 PRO C CG  1 
ATOM   6181  C CD  . PRO C  1 311 ? -0.228  -23.066 11.908  1.00 15.18  ? 324 PRO C CD  1 
ATOM   6182  N N   . GLU C  1 312 ? 2.520   -25.059 8.764   1.00 20.45  ? 325 GLU C N   1 
ATOM   6183  C CA  . GLU C  1 312 ? 2.516   -25.601 7.411   1.00 23.21  ? 325 GLU C CA  1 
ATOM   6184  C C   . GLU C  1 312 ? 1.567   -26.796 7.331   1.00 24.29  ? 325 GLU C C   1 
ATOM   6185  O O   . GLU C  1 312 ? 1.429   -27.551 8.297   1.00 24.79  ? 325 GLU C O   1 
ATOM   6186  C CB  . GLU C  1 312 ? 3.936   -26.028 7.032   1.00 23.84  ? 325 GLU C CB  1 
ATOM   6187  C CG  . GLU C  1 312 ? 4.359   -25.645 5.618   1.00 27.09  ? 325 GLU C CG  1 
ATOM   6188  C CD  . GLU C  1 312 ? 5.855   -25.359 5.505   1.00 31.08  ? 325 GLU C CD  1 
ATOM   6189  O OE1 . GLU C  1 312 ? 6.521   -25.175 6.553   1.00 30.47  ? 325 GLU C OE1 1 
ATOM   6190  O OE2 . GLU C  1 312 ? 6.361   -25.306 4.362   1.00 30.08  ? 325 GLU C OE2 1 
ATOM   6191  N N   . LYS C  1 313 ? 0.914   -26.956 6.182   1.00 25.63  ? 326 LYS C N   1 
ATOM   6192  C CA  . LYS C  1 313 ? -0.032  -28.058 5.965   1.00 26.67  ? 326 LYS C CA  1 
ATOM   6193  C C   . LYS C  1 313 ? 0.525   -29.115 5.014   1.00 27.00  ? 326 LYS C C   1 
ATOM   6194  O O   . LYS C  1 313 ? 0.759   -30.256 5.412   1.00 27.47  ? 326 LYS C O   1 
ATOM   6195  C CB  . LYS C  1 313 ? -1.391  -27.538 5.464   1.00 27.03  ? 326 LYS C CB  1 
ATOM   6196  C CG  . LYS C  1 313 ? -1.331  -26.314 4.538   1.00 28.06  ? 326 LYS C CG  1 
ATOM   6197  C CD  . LYS C  1 313 ? -1.002  -26.679 3.093   1.00 28.51  ? 326 LYS C CD  1 
ATOM   6198  C CE  . LYS C  1 313 ? -0.759  -25.428 2.258   1.00 28.43  ? 326 LYS C CE  1 
ATOM   6199  N NZ  . LYS C  1 313 ? -0.700  -25.729 0.800   1.00 22.66  ? 326 LYS C NZ  1 
ATOM   6200  N N   . GLY D  2 1   ? -3.947  -10.290 11.064  1.00 11.91  ? 1   GLY D N   1 
ATOM   6201  C CA  . GLY D  2 1   ? -4.048  -9.106  11.965  1.00 11.94  ? 1   GLY D CA  1 
ATOM   6202  C C   . GLY D  2 1   ? -4.468  -7.871  11.201  1.00 11.96  ? 1   GLY D C   1 
ATOM   6203  O O   . GLY D  2 1   ? -5.007  -7.973  10.100  1.00 12.70  ? 1   GLY D O   1 
ATOM   6204  N N   . LEU D  2 2   ? -4.212  -6.700  11.778  1.00 11.43  ? 2   LEU D N   1 
ATOM   6205  C CA  . LEU D  2 2   ? -4.588  -5.427  11.157  1.00 10.77  ? 2   LEU D CA  1 
ATOM   6206  C C   . LEU D  2 2   ? -3.871  -5.130  9.835   1.00 10.97  ? 2   LEU D C   1 
ATOM   6207  O O   . LEU D  2 2   ? -4.360  -4.337  9.034   1.00 10.37  ? 2   LEU D O   1 
ATOM   6208  C CB  . LEU D  2 2   ? -4.343  -4.269  12.123  1.00 10.13  ? 2   LEU D CB  1 
ATOM   6209  C CG  . LEU D  2 2   ? -5.271  -4.091  13.320  1.00 9.95   ? 2   LEU D CG  1 
ATOM   6210  C CD1 . LEU D  2 2   ? -4.733  -2.992  14.218  1.00 11.14  ? 2   LEU D CD1 1 
ATOM   6211  C CD2 . LEU D  2 2   ? -6.694  -3.779  12.881  1.00 13.02  ? 2   LEU D CD2 1 
ATOM   6212  N N   . PHE D  2 3   ? -2.725  -5.766  9.603   1.00 11.38  ? 3   PHE D N   1 
ATOM   6213  C CA  . PHE D  2 3   ? -1.875  -5.386  8.471   1.00 12.39  ? 3   PHE D CA  1 
ATOM   6214  C C   . PHE D  2 3   ? -1.910  -6.328  7.269   1.00 12.92  ? 3   PHE D C   1 
ATOM   6215  O O   . PHE D  2 3   ? -1.333  -6.029  6.223   1.00 13.54  ? 3   PHE D O   1 
ATOM   6216  C CB  . PHE D  2 3   ? -0.451  -5.083  8.946   1.00 12.50  ? 3   PHE D CB  1 
ATOM   6217  C CG  . PHE D  2 3   ? -0.381  -3.931  9.907   1.00 13.08  ? 3   PHE D CG  1 
ATOM   6218  C CD1 . PHE D  2 3   ? -0.485  -4.145  11.279  1.00 15.98  ? 3   PHE D CD1 1 
ATOM   6219  C CD2 . PHE D  2 3   ? -0.250  -2.629  9.440   1.00 13.95  ? 3   PHE D CD2 1 
ATOM   6220  C CE1 . PHE D  2 3   ? -0.441  -3.077  12.175  1.00 18.15  ? 3   PHE D CE1 1 
ATOM   6221  C CE2 . PHE D  2 3   ? -0.205  -1.555  10.327  1.00 16.77  ? 3   PHE D CE2 1 
ATOM   6222  C CZ  . PHE D  2 3   ? -0.300  -1.780  11.697  1.00 17.00  ? 3   PHE D CZ  1 
ATOM   6223  N N   . GLY D  2 4   ? -2.600  -7.456  7.425   1.00 13.13  ? 4   GLY D N   1 
ATOM   6224  C CA  . GLY D  2 4   ? -2.931  -8.327  6.302   1.00 12.11  ? 4   GLY D CA  1 
ATOM   6225  C C   . GLY D  2 4   ? -1.872  -9.305  5.829   1.00 11.54  ? 4   GLY D C   1 
ATOM   6226  O O   . GLY D  2 4   ? -2.128  -10.088 4.917   1.00 11.29  ? 4   GLY D O   1 
ATOM   6227  N N   . ALA D  2 5   ? -0.688  -9.273  6.434   1.00 11.11  ? 5   ALA D N   1 
ATOM   6228  C CA  . ALA D  2 5   ? 0.392   -10.172 6.013   1.00 10.71  ? 5   ALA D CA  1 
ATOM   6229  C C   . ALA D  2 5   ? 0.314   -11.548 6.683   1.00 10.39  ? 5   ALA D C   1 
ATOM   6230  O O   . ALA D  2 5   ? -0.110  -12.520 6.051   1.00 10.33  ? 5   ALA D O   1 
ATOM   6231  C CB  . ALA D  2 5   ? 1.752   -9.527  6.227   1.00 10.34  ? 5   ALA D CB  1 
ATOM   6232  N N   . ILE D  2 6   ? 0.718   -11.624 7.952   1.00 9.92   ? 6   ILE D N   1 
ATOM   6233  C CA  . ILE D  2 6   ? 0.692   -12.878 8.707   1.00 9.55   ? 6   ILE D CA  1 
ATOM   6234  C C   . ILE D  2 6   ? -0.753  -13.330 8.891   1.00 9.47   ? 6   ILE D C   1 
ATOM   6235  O O   . ILE D  2 6   ? -1.565  -12.617 9.489   1.00 10.36  ? 6   ILE D O   1 
ATOM   6236  C CB  . ILE D  2 6   ? 1.403   -12.757 10.085  1.00 9.75   ? 6   ILE D CB  1 
ATOM   6237  C CG1 . ILE D  2 6   ? 2.844   -12.260 9.910   1.00 10.75  ? 6   ILE D CG1 1 
ATOM   6238  C CG2 . ILE D  2 6   ? 1.381   -14.093 10.828  1.00 7.11   ? 6   ILE D CG2 1 
ATOM   6239  C CD1 . ILE D  2 6   ? 3.569   -11.955 11.212  1.00 9.08   ? 6   ILE D CD1 1 
ATOM   6240  N N   . ALA D  2 7   ? -1.052  -14.519 8.367   1.00 8.85   ? 7   ALA D N   1 
ATOM   6241  C CA  . ALA D  2 7   ? -2.409  -15.077 8.315   1.00 8.56   ? 7   ALA D CA  1 
ATOM   6242  C C   . ALA D  2 7   ? -3.302  -14.318 7.328   1.00 8.14   ? 7   ALA D C   1 
ATOM   6243  O O   . ALA D  2 7   ? -4.527  -14.327 7.451   1.00 8.16   ? 7   ALA D O   1 
ATOM   6244  C CB  . ALA D  2 7   ? -3.044  -15.143 9.710   1.00 8.16   ? 7   ALA D CB  1 
ATOM   6245  N N   . GLY D  2 8   ? -2.669  -13.681 6.343   1.00 7.81   ? 8   GLY D N   1 
ATOM   6246  C CA  . GLY D  2 8   ? -3.360  -12.927 5.304   1.00 7.64   ? 8   GLY D CA  1 
ATOM   6247  C C   . GLY D  2 8   ? -2.889  -13.341 3.924   1.00 8.11   ? 8   GLY D C   1 
ATOM   6248  O O   . GLY D  2 8   ? -3.047  -14.500 3.540   1.00 8.31   ? 8   GLY D O   1 
ATOM   6249  N N   . PHE D  2 9   ? -2.301  -12.403 3.179   1.00 9.07   ? 9   PHE D N   1 
ATOM   6250  C CA  . PHE D  2 9   ? -1.828  -12.697 1.820   1.00 9.64   ? 9   PHE D CA  1 
ATOM   6251  C C   . PHE D  2 9   ? -0.667  -13.700 1.800   1.00 10.39  ? 9   PHE D C   1 
ATOM   6252  O O   . PHE D  2 9   ? -0.473  -14.408 0.811   1.00 11.23  ? 9   PHE D O   1 
ATOM   6253  C CB  . PHE D  2 9   ? -1.533  -11.425 0.995   1.00 9.31   ? 9   PHE D CB  1 
ATOM   6254  C CG  . PHE D  2 9   ? -0.382  -10.586 1.509   1.00 10.98  ? 9   PHE D CG  1 
ATOM   6255  C CD1 . PHE D  2 9   ? 0.941   -10.926 1.218   1.00 12.22  ? 9   PHE D CD1 1 
ATOM   6256  C CD2 . PHE D  2 9   ? -0.626  -9.421  2.233   1.00 9.24   ? 9   PHE D CD2 1 
ATOM   6257  C CE1 . PHE D  2 9   ? 2.002   -10.144 1.677   1.00 8.81   ? 9   PHE D CE1 1 
ATOM   6258  C CE2 . PHE D  2 9   ? 0.424   -8.633  2.691   1.00 9.87   ? 9   PHE D CE2 1 
ATOM   6259  C CZ  . PHE D  2 9   ? 1.742   -8.999  2.413   1.00 11.58  ? 9   PHE D CZ  1 
ATOM   6260  N N   . ILE D  2 10  ? 0.091   -13.752 2.895   1.00 10.64  ? 10  ILE D N   1 
ATOM   6261  C CA  . ILE D  2 10  ? 1.057   -14.822 3.121   1.00 10.84  ? 10  ILE D CA  1 
ATOM   6262  C C   . ILE D  2 10  ? 0.311   -15.996 3.758   1.00 11.05  ? 10  ILE D C   1 
ATOM   6263  O O   . ILE D  2 10  ? -0.131  -15.914 4.907   1.00 10.43  ? 10  ILE D O   1 
ATOM   6264  C CB  . ILE D  2 10  ? 2.246   -14.363 4.006   1.00 10.77  ? 10  ILE D CB  1 
ATOM   6265  C CG1 . ILE D  2 10  ? 3.020   -13.237 3.315   1.00 11.48  ? 10  ILE D CG1 1 
ATOM   6266  C CG2 . ILE D  2 10  ? 3.182   -15.531 4.307   1.00 10.27  ? 10  ILE D CG2 1 
ATOM   6267  C CD1 . ILE D  2 10  ? 4.126   -12.615 4.164   1.00 12.58  ? 10  ILE D CD1 1 
ATOM   6268  N N   . GLU D  2 11  ? 0.171   -17.074 2.986   1.00 12.34  ? 11  GLU D N   1 
ATOM   6269  C CA  . GLU D  2 11  ? -0.621  -18.258 3.351   1.00 13.58  ? 11  GLU D CA  1 
ATOM   6270  C C   . GLU D  2 11  ? -0.305  -18.793 4.750   1.00 13.04  ? 11  GLU D C   1 
ATOM   6271  O O   . GLU D  2 11  ? -1.185  -18.850 5.610   1.00 13.66  ? 11  GLU D O   1 
ATOM   6272  C CB  . GLU D  2 11  ? -0.423  -19.359 2.296   1.00 14.92  ? 11  GLU D CB  1 
ATOM   6273  C CG  . GLU D  2 11  ? -1.231  -20.646 2.521   1.00 21.11  ? 11  GLU D CG  1 
ATOM   6274  C CD  . GLU D  2 11  ? -2.540  -20.693 1.741   1.00 27.18  ? 11  GLU D CD  1 
ATOM   6275  O OE1 . GLU D  2 11  ? -3.192  -19.635 1.584   1.00 30.33  ? 11  GLU D OE1 1 
ATOM   6276  O OE2 . GLU D  2 11  ? -2.919  -21.799 1.292   1.00 24.56  ? 11  GLU D OE2 1 
ATOM   6277  N N   . ASN D  2 12  ? 0.951   -19.178 4.970   1.00 12.55  ? 12  ASN D N   1 
ATOM   6278  C CA  . ASN D  2 12  ? 1.378   -19.745 6.246   1.00 11.74  ? 12  ASN D CA  1 
ATOM   6279  C C   . ASN D  2 12  ? 2.832   -19.440 6.602   1.00 10.67  ? 12  ASN D C   1 
ATOM   6280  O O   . ASN D  2 12  ? 3.566   -18.840 5.815   1.00 10.31  ? 12  ASN D O   1 
ATOM   6281  C CB  . ASN D  2 12  ? 1.111   -21.258 6.284   1.00 12.20  ? 12  ASN D CB  1 
ATOM   6282  C CG  . ASN D  2 12  ? 1.631   -21.982 5.053   1.00 13.77  ? 12  ASN D CG  1 
ATOM   6283  O OD1 . ASN D  2 12  ? 0.853   -22.426 4.208   1.00 17.81  ? 12  ASN D OD1 1 
ATOM   6284  N ND2 . ASN D  2 12  ? 2.950   -22.114 4.951   1.00 15.18  ? 12  ASN D ND2 1 
ATOM   6285  N N   . GLY D  2 13  ? 3.232   -19.845 7.803   1.00 9.96   ? 13  GLY D N   1 
ATOM   6286  C CA  . GLY D  2 13  ? 4.602   -19.662 8.260   1.00 9.90   ? 13  GLY D CA  1 
ATOM   6287  C C   . GLY D  2 13  ? 5.524   -20.786 7.834   1.00 9.86   ? 13  GLY D C   1 
ATOM   6288  O O   . GLY D  2 13  ? 5.076   -21.838 7.376   1.00 10.13  ? 13  GLY D O   1 
ATOM   6289  N N   . TRP D  2 14  ? 6.822   -20.556 7.985   1.00 9.70   ? 14  TRP D N   1 
ATOM   6290  C CA  . TRP D  2 14  ? 7.821   -21.559 7.669   1.00 10.00  ? 14  TRP D CA  1 
ATOM   6291  C C   . TRP D  2 14  ? 8.388   -22.151 8.951   1.00 11.10  ? 14  TRP D C   1 
ATOM   6292  O O   . TRP D  2 14  ? 9.046   -21.454 9.727   1.00 11.38  ? 14  TRP D O   1 
ATOM   6293  C CB  . TRP D  2 14  ? 8.950   -20.952 6.839   1.00 9.74   ? 14  TRP D CB  1 
ATOM   6294  C CG  . TRP D  2 14  ? 8.521   -20.321 5.552   1.00 8.43   ? 14  TRP D CG  1 
ATOM   6295  C CD1 . TRP D  2 14  ? 7.494   -20.716 4.737   1.00 9.43   ? 14  TRP D CD1 1 
ATOM   6296  C CD2 . TRP D  2 14  ? 9.134   -19.200 4.909   1.00 7.98   ? 14  TRP D CD2 1 
ATOM   6297  N NE1 . TRP D  2 14  ? 7.424   -19.900 3.633   1.00 10.75  ? 14  TRP D NE1 1 
ATOM   6298  C CE2 . TRP D  2 14  ? 8.419   -18.961 3.713   1.00 10.41  ? 14  TRP D CE2 1 
ATOM   6299  C CE3 . TRP D  2 14  ? 10.218  -18.371 5.228   1.00 9.26   ? 14  TRP D CE3 1 
ATOM   6300  C CZ2 . TRP D  2 14  ? 8.750   -17.923 2.837   1.00 9.95   ? 14  TRP D CZ2 1 
ATOM   6301  C CZ3 . TRP D  2 14  ? 10.550  -17.338 4.355   1.00 9.68   ? 14  TRP D CZ3 1 
ATOM   6302  C CH2 . TRP D  2 14  ? 9.816   -17.125 3.174   1.00 11.57  ? 14  TRP D CH2 1 
ATOM   6303  N N   . GLU D  2 15  ? 8.127   -23.438 9.169   1.00 11.92  ? 15  GLU D N   1 
ATOM   6304  C CA  . GLU D  2 15  ? 8.639   -24.146 10.341  1.00 12.67  ? 15  GLU D CA  1 
ATOM   6305  C C   . GLU D  2 15  ? 10.159  -24.347 10.280  1.00 13.46  ? 15  GLU D C   1 
ATOM   6306  O O   . GLU D  2 15  ? 10.810  -24.514 11.315  1.00 13.79  ? 15  GLU D O   1 
ATOM   6307  C CB  . GLU D  2 15  ? 7.920   -25.487 10.518  1.00 12.42  ? 15  GLU D CB  1 
ATOM   6308  C CG  . GLU D  2 15  ? 6.431   -25.353 10.835  1.00 11.64  ? 15  GLU D CG  1 
ATOM   6309  C CD  . GLU D  2 15  ? 5.698   -26.689 10.857  1.00 13.15  ? 15  GLU D CD  1 
ATOM   6310  O OE1 . GLU D  2 15  ? 4.471   -26.688 10.624  1.00 11.05  ? 15  GLU D OE1 1 
ATOM   6311  O OE2 . GLU D  2 15  ? 6.338   -27.738 11.105  1.00 13.35  ? 15  GLU D OE2 1 
ATOM   6312  N N   . GLY D  2 16  ? 10.714  -24.312 9.068   1.00 13.98  ? 16  GLY D N   1 
ATOM   6313  C CA  . GLY D  2 16  ? 12.155  -24.463 8.853   1.00 14.50  ? 16  GLY D CA  1 
ATOM   6314  C C   . GLY D  2 16  ? 12.972  -23.194 9.049   1.00 15.02  ? 16  GLY D C   1 
ATOM   6315  O O   . GLY D  2 16  ? 14.195  -23.214 8.904   1.00 15.04  ? 16  GLY D O   1 
ATOM   6316  N N   . LEU D  2 17  ? 12.300  -22.088 9.363   1.00 15.32  ? 17  LEU D N   1 
ATOM   6317  C CA  . LEU D  2 17  ? 12.976  -20.836 9.700   1.00 15.95  ? 17  LEU D CA  1 
ATOM   6318  C C   . LEU D  2 17  ? 13.197  -20.778 11.214  1.00 16.95  ? 17  LEU D C   1 
ATOM   6319  O O   . LEU D  2 17  ? 12.500  -20.067 11.941  1.00 16.93  ? 17  LEU D O   1 
ATOM   6320  C CB  . LEU D  2 17  ? 12.180  -19.622 9.192   1.00 15.56  ? 17  LEU D CB  1 
ATOM   6321  C CG  . LEU D  2 17  ? 12.766  -18.211 9.347   1.00 14.79  ? 17  LEU D CG  1 
ATOM   6322  C CD1 . LEU D  2 17  ? 13.831  -17.923 8.302   1.00 15.53  ? 17  LEU D CD1 1 
ATOM   6323  C CD2 . LEU D  2 17  ? 11.667  -17.162 9.278   1.00 13.09  ? 17  LEU D CD2 1 
ATOM   6324  N N   . ILE D  2 18  ? 14.167  -21.563 11.675  1.00 18.33  ? 18  ILE D N   1 
ATOM   6325  C CA  . ILE D  2 18  ? 14.533  -21.632 13.092  1.00 19.22  ? 18  ILE D CA  1 
ATOM   6326  C C   . ILE D  2 18  ? 15.480  -20.492 13.479  1.00 19.31  ? 18  ILE D C   1 
ATOM   6327  O O   . ILE D  2 18  ? 15.723  -20.248 14.664  1.00 19.34  ? 18  ILE D O   1 
ATOM   6328  C CB  . ILE D  2 18  ? 15.172  -23.011 13.453  1.00 19.64  ? 18  ILE D CB  1 
ATOM   6329  C CG1 . ILE D  2 18  ? 16.186  -23.464 12.388  1.00 21.26  ? 18  ILE D CG1 1 
ATOM   6330  C CG2 . ILE D  2 18  ? 14.098  -24.084 13.618  1.00 19.26  ? 18  ILE D CG2 1 
ATOM   6331  C CD1 . ILE D  2 18  ? 17.612  -22.971 12.603  1.00 23.34  ? 18  ILE D CD1 1 
ATOM   6332  N N   . ASN D  2 19  ? 16.002  -19.804 12.463  1.00 19.45  ? 19  ASN D N   1 
ATOM   6333  C CA  . ASN D  2 19  ? 17.032  -18.771 12.627  1.00 19.27  ? 19  ASN D CA  1 
ATOM   6334  C C   . ASN D  2 19  ? 16.512  -17.360 12.984  1.00 18.54  ? 19  ASN D C   1 
ATOM   6335  O O   . ASN D  2 19  ? 17.295  -16.482 13.354  1.00 18.72  ? 19  ASN D O   1 
ATOM   6336  C CB  . ASN D  2 19  ? 18.001  -18.742 11.412  1.00 19.35  ? 19  ASN D CB  1 
ATOM   6337  C CG  . ASN D  2 19  ? 17.365  -19.263 10.096  1.00 21.49  ? 19  ASN D CG  1 
ATOM   6338  O OD1 . ASN D  2 19  ? 16.663  -20.276 10.078  1.00 24.35  ? 19  ASN D OD1 1 
ATOM   6339  N ND2 . ASN D  2 19  ? 17.652  -18.581 8.992   1.00 18.84  ? 19  ASN D ND2 1 
ATOM   6340  N N   . GLY D  2 20  ? 15.198  -17.156 12.889  1.00 17.33  ? 20  GLY D N   1 
ATOM   6341  C CA  . GLY D  2 20  ? 14.592  -15.849 13.163  1.00 16.07  ? 20  GLY D CA  1 
ATOM   6342  C C   . GLY D  2 20  ? 13.070  -15.832 13.130  1.00 15.38  ? 20  GLY D C   1 
ATOM   6343  O O   . GLY D  2 20  ? 12.426  -16.883 13.084  1.00 15.53  ? 20  GLY D O   1 
ATOM   6344  N N   . TRP D  2 21  ? 12.497  -14.629 13.157  1.00 14.21  ? 21  TRP D N   1 
ATOM   6345  C CA  . TRP D  2 21  ? 11.043  -14.440 13.133  1.00 13.02  ? 21  TRP D CA  1 
ATOM   6346  C C   . TRP D  2 21  ? 10.526  -14.242 11.710  1.00 12.38  ? 21  TRP D C   1 
ATOM   6347  O O   . TRP D  2 21  ? 9.427   -14.688 11.374  1.00 12.72  ? 21  TRP D O   1 
ATOM   6348  C CB  . TRP D  2 21  ? 10.646  -13.235 13.990  1.00 12.90  ? 21  TRP D CB  1 
ATOM   6349  C CG  . TRP D  2 21  ? 10.616  -13.492 15.473  1.00 12.89  ? 21  TRP D CG  1 
ATOM   6350  C CD1 . TRP D  2 21  ? 11.478  -14.274 16.199  1.00 13.85  ? 21  TRP D CD1 1 
ATOM   6351  C CD2 . TRP D  2 21  ? 9.690   -12.940 16.416  1.00 12.31  ? 21  TRP D CD2 1 
ATOM   6352  N NE1 . TRP D  2 21  ? 11.135  -14.252 17.530  1.00 12.26  ? 21  TRP D NE1 1 
ATOM   6353  C CE2 . TRP D  2 21  ? 10.042  -13.442 17.692  1.00 11.86  ? 21  TRP D CE2 1 
ATOM   6354  C CE3 . TRP D  2 21  ? 8.591   -12.076 16.306  1.00 12.84  ? 21  TRP D CE3 1 
ATOM   6355  C CZ2 . TRP D  2 21  ? 9.336   -13.106 18.850  1.00 10.82  ? 21  TRP D CZ2 1 
ATOM   6356  C CZ3 . TRP D  2 21  ? 7.887   -11.740 17.462  1.00 13.81  ? 21  TRP D CZ3 1 
ATOM   6357  C CH2 . TRP D  2 21  ? 8.263   -12.257 18.717  1.00 14.33  ? 21  TRP D CH2 1 
ATOM   6358  N N   . TYR D  2 22  ? 11.326  -13.567 10.888  1.00 10.70  ? 22  TYR D N   1 
ATOM   6359  C CA  . TYR D  2 22  ? 10.972  -13.254 9.508   1.00 9.51   ? 22  TYR D CA  1 
ATOM   6360  C C   . TYR D  2 22  ? 12.141  -13.600 8.595   1.00 9.53   ? 22  TYR D C   1 
ATOM   6361  O O   . TYR D  2 22  ? 13.278  -13.718 9.058   1.00 9.45   ? 22  TYR D O   1 
ATOM   6362  C CB  . TYR D  2 22  ? 10.644  -11.766 9.372   1.00 9.10   ? 22  TYR D CB  1 
ATOM   6363  C CG  . TYR D  2 22  ? 9.678   -11.240 10.406  1.00 7.44   ? 22  TYR D CG  1 
ATOM   6364  C CD1 . TYR D  2 22  ? 10.136  -10.555 11.533  1.00 8.51   ? 22  TYR D CD1 1 
ATOM   6365  C CD2 . TYR D  2 22  ? 8.307   -11.427 10.261  1.00 7.30   ? 22  TYR D CD2 1 
ATOM   6366  C CE1 . TYR D  2 22  ? 9.248   -10.064 12.492  1.00 7.65   ? 22  TYR D CE1 1 
ATOM   6367  C CE2 . TYR D  2 22  ? 7.412   -10.943 11.209  1.00 9.67   ? 22  TYR D CE2 1 
ATOM   6368  C CZ  . TYR D  2 22  ? 7.888   -10.265 12.320  1.00 9.35   ? 22  TYR D CZ  1 
ATOM   6369  O OH  . TYR D  2 22  ? 6.999   -9.794  13.251  1.00 8.86   ? 22  TYR D OH  1 
ATOM   6370  N N   . GLY D  2 23  ? 11.873  -13.763 7.303   1.00 9.53   ? 23  GLY D N   1 
ATOM   6371  C CA  . GLY D  2 23  ? 12.935  -14.132 6.376   1.00 10.41  ? 23  GLY D CA  1 
ATOM   6372  C C   . GLY D  2 23  ? 12.632  -14.067 4.895   1.00 11.01  ? 23  GLY D C   1 
ATOM   6373  O O   . GLY D  2 23  ? 11.566  -13.606 4.479   1.00 11.25  ? 23  GLY D O   1 
ATOM   6374  N N   . PHE D  2 24  ? 13.599  -14.531 4.106   1.00 11.60  ? 24  PHE D N   1 
ATOM   6375  C CA  . PHE D  2 24  ? 13.504  -14.577 2.652   1.00 11.68  ? 24  PHE D CA  1 
ATOM   6376  C C   . PHE D  2 24  ? 13.645  -16.023 2.184   1.00 12.48  ? 24  PHE D C   1 
ATOM   6377  O O   . PHE D  2 24  ? 14.426  -16.790 2.747   1.00 13.03  ? 24  PHE D O   1 
ATOM   6378  C CB  . PHE D  2 24  ? 14.629  -13.759 2.008   1.00 11.25  ? 24  PHE D CB  1 
ATOM   6379  C CG  . PHE D  2 24  ? 14.708  -12.330 2.469   1.00 10.65  ? 24  PHE D CG  1 
ATOM   6380  C CD1 . PHE D  2 24  ? 15.400  -11.992 3.630   1.00 10.79  ? 24  PHE D CD1 1 
ATOM   6381  C CD2 . PHE D  2 24  ? 14.123  -11.315 1.723   1.00 9.77   ? 24  PHE D CD2 1 
ATOM   6382  C CE1 . PHE D  2 24  ? 15.489  -10.666 4.051   1.00 7.48   ? 24  PHE D CE1 1 
ATOM   6383  C CE2 . PHE D  2 24  ? 14.207  -9.990  2.136   1.00 10.06  ? 24  PHE D CE2 1 
ATOM   6384  C CZ  . PHE D  2 24  ? 14.894  -9.664  3.300   1.00 6.57   ? 24  PHE D CZ  1 
ATOM   6385  N N   . ARG D  2 25  ? 12.899  -16.389 1.149   1.00 13.35  ? 25  ARG D N   1 
ATOM   6386  C CA  . ARG D  2 25  ? 13.076  -17.683 0.503   1.00 14.35  ? 25  ARG D CA  1 
ATOM   6387  C C   . ARG D  2 25  ? 13.248  -17.476 -0.997  1.00 15.30  ? 25  ARG D C   1 
ATOM   6388  O O   . ARG D  2 25  ? 12.274  -17.248 -1.719  1.00 16.02  ? 25  ARG D O   1 
ATOM   6389  C CB  . ARG D  2 25  ? 11.896  -18.611 0.807   1.00 14.40  ? 25  ARG D CB  1 
ATOM   6390  C CG  . ARG D  2 25  ? 12.040  -20.031 0.267   1.00 12.60  ? 25  ARG D CG  1 
ATOM   6391  C CD  . ARG D  2 25  ? 11.038  -20.974 0.924   1.00 11.66  ? 25  ARG D CD  1 
ATOM   6392  N NE  . ARG D  2 25  ? 11.452  -21.355 2.275   1.00 7.64   ? 25  ARG D NE  1 
ATOM   6393  C CZ  . ARG D  2 25  ? 10.737  -22.113 3.101   1.00 6.63   ? 25  ARG D CZ  1 
ATOM   6394  N NH1 . ARG D  2 25  ? 9.551   -22.582 2.732   1.00 3.89   ? 25  ARG D NH1 1 
ATOM   6395  N NH2 . ARG D  2 25  ? 11.212  -22.401 4.307   1.00 6.69   ? 25  ARG D NH2 1 
ATOM   6396  N N   . HIS D  2 26  ? 14.494  -17.536 -1.457  1.00 15.60  ? 26  HIS D N   1 
ATOM   6397  C CA  . HIS D  2 26  ? 14.788  -17.317 -2.867  1.00 16.21  ? 26  HIS D CA  1 
ATOM   6398  C C   . HIS D  2 26  ? 14.682  -18.602 -3.685  1.00 16.47  ? 26  HIS D C   1 
ATOM   6399  O O   . HIS D  2 26  ? 14.617  -19.701 -3.133  1.00 16.45  ? 26  HIS D O   1 
ATOM   6400  C CB  . HIS D  2 26  ? 16.154  -16.641 -3.051  1.00 16.38  ? 26  HIS D CB  1 
ATOM   6401  C CG  . HIS D  2 26  ? 17.311  -17.452 -2.555  1.00 18.54  ? 26  HIS D CG  1 
ATOM   6402  N ND1 . HIS D  2 26  ? 17.938  -18.406 -3.328  1.00 20.12  ? 26  HIS D ND1 1 
ATOM   6403  C CD2 . HIS D  2 26  ? 17.963  -17.440 -1.369  1.00 20.42  ? 26  HIS D CD2 1 
ATOM   6404  C CE1 . HIS D  2 26  ? 18.921  -18.953 -2.636  1.00 21.86  ? 26  HIS D CE1 1 
ATOM   6405  N NE2 . HIS D  2 26  ? 18.958  -18.385 -1.444  1.00 21.51  ? 26  HIS D NE2 1 
ATOM   6406  N N   . GLN D  2 27  ? 14.652  -18.441 -5.004  1.00 17.08  ? 27  GLN D N   1 
ATOM   6407  C CA  . GLN D  2 27  ? 14.524  -19.543 -5.947  1.00 17.56  ? 27  GLN D CA  1 
ATOM   6408  C C   . GLN D  2 27  ? 15.156  -19.070 -7.246  1.00 17.77  ? 27  GLN D C   1 
ATOM   6409  O O   . GLN D  2 27  ? 14.657  -18.135 -7.875  1.00 17.99  ? 27  GLN D O   1 
ATOM   6410  C CB  . GLN D  2 27  ? 13.045  -19.883 -6.168  1.00 17.52  ? 27  GLN D CB  1 
ATOM   6411  C CG  . GLN D  2 27  ? 12.778  -21.150 -6.974  1.00 21.29  ? 27  GLN D CG  1 
ATOM   6412  C CD  . GLN D  2 27  ? 12.706  -22.400 -6.109  1.00 27.07  ? 27  GLN D CD  1 
ATOM   6413  O OE1 . GLN D  2 27  ? 12.160  -22.376 -5.000  1.00 28.35  ? 27  GLN D OE1 1 
ATOM   6414  N NE2 . GLN D  2 27  ? 13.249  -23.505 -6.617  1.00 25.92  ? 27  GLN D NE2 1 
ATOM   6415  N N   . ASN D  2 28  ? 16.269  -19.690 -7.628  1.00 18.00  ? 28  ASN D N   1 
ATOM   6416  C CA  . ASN D  2 28  ? 16.921  -19.371 -8.899  1.00 18.44  ? 28  ASN D CA  1 
ATOM   6417  C C   . ASN D  2 28  ? 17.404  -20.616 -9.657  1.00 18.92  ? 28  ASN D C   1 
ATOM   6418  O O   . ASN D  2 28  ? 16.841  -21.700 -9.486  1.00 18.76  ? 28  ASN D O   1 
ATOM   6419  C CB  . ASN D  2 28  ? 18.029  -18.317 -8.714  1.00 18.06  ? 28  ASN D CB  1 
ATOM   6420  C CG  . ASN D  2 28  ? 19.033  -18.685 -7.630  1.00 18.88  ? 28  ASN D CG  1 
ATOM   6421  O OD1 . ASN D  2 28  ? 19.207  -19.854 -7.282  1.00 19.75  ? 28  ASN D OD1 1 
ATOM   6422  N ND2 . ASN D  2 28  ? 19.714  -17.673 -7.099  1.00 18.86  ? 28  ASN D ND2 1 
ATOM   6423  N N   . ALA D  2 29  ? 18.424  -20.458 -10.500 1.00 19.53  ? 29  ALA D N   1 
ATOM   6424  C CA  . ALA D  2 29  ? 18.979  -21.581 -11.263 1.00 20.07  ? 29  ALA D CA  1 
ATOM   6425  C C   . ALA D  2 29  ? 19.870  -22.481 -10.400 1.00 20.40  ? 29  ALA D C   1 
ATOM   6426  O O   . ALA D  2 29  ? 20.117  -23.641 -10.743 1.00 19.93  ? 29  ALA D O   1 
ATOM   6427  C CB  . ALA D  2 29  ? 19.744  -21.074 -12.481 1.00 19.83  ? 29  ALA D CB  1 
ATOM   6428  N N   . GLN D  2 30  ? 20.338  -21.936 -9.278  1.00 20.83  ? 30  GLN D N   1 
ATOM   6429  C CA  . GLN D  2 30  ? 21.225  -22.652 -8.361  1.00 21.00  ? 30  GLN D CA  1 
ATOM   6430  C C   . GLN D  2 30  ? 20.457  -23.433 -7.288  1.00 20.97  ? 30  GLN D C   1 
ATOM   6431  O O   . GLN D  2 30  ? 21.054  -24.185 -6.513  1.00 20.95  ? 30  GLN D O   1 
ATOM   6432  C CB  . GLN D  2 30  ? 22.207  -21.674 -7.705  1.00 21.11  ? 30  GLN D CB  1 
ATOM   6433  C CG  . GLN D  2 30  ? 23.126  -20.948 -8.688  1.00 22.70  ? 30  GLN D CG  1 
ATOM   6434  C CD  . GLN D  2 30  ? 23.922  -19.828 -8.037  1.00 23.42  ? 30  GLN D CD  1 
ATOM   6435  O OE1 . GLN D  2 30  ? 23.743  -18.657 -8.364  1.00 25.45  ? 30  GLN D OE1 1 
ATOM   6436  N NE2 . GLN D  2 30  ? 24.803  -20.184 -7.109  1.00 23.58  ? 30  GLN D NE2 1 
ATOM   6437  N N   . GLY D  2 31  ? 19.138  -23.254 -7.252  1.00 20.92  ? 31  GLY D N   1 
ATOM   6438  C CA  . GLY D  2 31  ? 18.281  -23.921 -6.269  1.00 20.89  ? 31  GLY D CA  1 
ATOM   6439  C C   . GLY D  2 31  ? 17.635  -22.937 -5.311  1.00 20.99  ? 31  GLY D C   1 
ATOM   6440  O O   . GLY D  2 31  ? 17.757  -21.722 -5.487  1.00 21.11  ? 31  GLY D O   1 
ATOM   6441  N N   . GLU D  2 32  ? 16.944  -23.459 -4.298  1.00 20.71  ? 32  GLU D N   1 
ATOM   6442  C CA  . GLU D  2 32  ? 16.304  -22.605 -3.295  1.00 20.33  ? 32  GLU D CA  1 
ATOM   6443  C C   . GLU D  2 32  ? 17.131  -22.496 -2.012  1.00 19.64  ? 32  GLU D C   1 
ATOM   6444  O O   . GLU D  2 32  ? 17.973  -23.350 -1.729  1.00 19.05  ? 32  GLU D O   1 
ATOM   6445  C CB  . GLU D  2 32  ? 14.856  -23.050 -3.008  1.00 20.64  ? 32  GLU D CB  1 
ATOM   6446  C CG  . GLU D  2 32  ? 14.662  -24.055 -1.862  1.00 21.83  ? 32  GLU D CG  1 
ATOM   6447  C CD  . GLU D  2 32  ? 13.301  -23.919 -1.174  1.00 22.47  ? 32  GLU D CD  1 
ATOM   6448  O OE1 . GLU D  2 32  ? 13.150  -24.420 -0.040  1.00 20.90  ? 32  GLU D OE1 1 
ATOM   6449  O OE2 . GLU D  2 32  ? 12.381  -23.304 -1.758  1.00 22.61  ? 32  GLU D OE2 1 
ATOM   6450  N N   . GLY D  2 33  ? 16.886  -21.432 -1.253  1.00 19.10  ? 33  GLY D N   1 
ATOM   6451  C CA  . GLY D  2 33  ? 17.574  -21.189 0.011   1.00 18.77  ? 33  GLY D CA  1 
ATOM   6452  C C   . GLY D  2 33  ? 16.781  -20.245 0.890   1.00 18.56  ? 33  GLY D C   1 
ATOM   6453  O O   . GLY D  2 33  ? 15.975  -19.456 0.395   1.00 18.54  ? 33  GLY D O   1 
ATOM   6454  N N   . THR D  2 34  ? 17.009  -20.323 2.198   1.00 18.45  ? 34  THR D N   1 
ATOM   6455  C CA  . THR D  2 34  ? 16.272  -19.506 3.161   1.00 18.01  ? 34  THR D CA  1 
ATOM   6456  C C   . THR D  2 34  ? 17.221  -18.801 4.133   1.00 17.86  ? 34  THR D C   1 
ATOM   6457  O O   . THR D  2 34  ? 18.153  -19.414 4.656   1.00 17.19  ? 34  THR D O   1 
ATOM   6458  C CB  . THR D  2 34  ? 15.227  -20.355 3.929   1.00 18.06  ? 34  THR D CB  1 
ATOM   6459  O OG1 . THR D  2 34  ? 14.353  -21.001 2.993   1.00 17.46  ? 34  THR D OG1 1 
ATOM   6460  C CG2 . THR D  2 34  ? 14.394  -19.493 4.866   1.00 17.27  ? 34  THR D CG2 1 
ATOM   6461  N N   . ALA D  2 35  ? 16.979  -17.510 4.354   1.00 17.77  ? 35  ALA D N   1 
ATOM   6462  C CA  . ALA D  2 35  ? 17.774  -16.705 5.280   1.00 18.00  ? 35  ALA D CA  1 
ATOM   6463  C C   . ALA D  2 35  ? 16.883  -15.799 6.128   1.00 18.60  ? 35  ALA D C   1 
ATOM   6464  O O   . ALA D  2 35  ? 15.890  -15.260 5.638   1.00 19.16  ? 35  ALA D O   1 
ATOM   6465  C CB  . ALA D  2 35  ? 18.799  -15.881 4.520   1.00 17.39  ? 35  ALA D CB  1 
ATOM   6466  N N   . ALA D  2 36  ? 17.249  -15.633 7.397   1.00 18.56  ? 36  ALA D N   1 
ATOM   6467  C CA  . ALA D  2 36  ? 16.471  -14.817 8.329   1.00 18.79  ? 36  ALA D CA  1 
ATOM   6468  C C   . ALA D  2 36  ? 16.900  -13.354 8.316   1.00 19.08  ? 36  ALA D C   1 
ATOM   6469  O O   . ALA D  2 36  ? 18.086  -13.047 8.199   1.00 19.01  ? 36  ALA D O   1 
ATOM   6470  C CB  . ALA D  2 36  ? 16.570  -15.384 9.737   1.00 18.82  ? 36  ALA D CB  1 
ATOM   6471  N N   . ASP D  2 37  ? 15.924  -12.458 8.442   1.00 19.75  ? 37  ASP D N   1 
ATOM   6472  C CA  . ASP D  2 37  ? 16.188  -11.024 8.525   1.00 20.01  ? 37  ASP D CA  1 
ATOM   6473  C C   . ASP D  2 37  ? 16.352  -10.601 9.984   1.00 20.30  ? 37  ASP D C   1 
ATOM   6474  O O   . ASP D  2 37  ? 15.402  -10.662 10.765  1.00 20.14  ? 37  ASP D O   1 
ATOM   6475  C CB  . ASP D  2 37  ? 15.060  -10.231 7.854   1.00 20.14  ? 37  ASP D CB  1 
ATOM   6476  C CG  . ASP D  2 37  ? 15.396  -8.760  7.690   1.00 20.50  ? 37  ASP D CG  1 
ATOM   6477  O OD1 . ASP D  2 37  ? 16.479  -8.445  7.152   1.00 20.19  ? 37  ASP D OD1 1 
ATOM   6478  O OD2 . ASP D  2 37  ? 14.573  -7.913  8.094   1.00 24.90  ? 37  ASP D OD2 1 
ATOM   6479  N N   . TYR D  2 38  ? 17.565  -10.180 10.339  1.00 20.77  ? 38  TYR D N   1 
ATOM   6480  C CA  . TYR D  2 38  ? 17.908  -9.794  11.710  1.00 21.11  ? 38  TYR D CA  1 
ATOM   6481  C C   . TYR D  2 38  ? 17.130  -8.559  12.161  1.00 20.83  ? 38  TYR D C   1 
ATOM   6482  O O   . TYR D  2 38  ? 16.504  -8.567  13.223  1.00 20.62  ? 38  TYR D O   1 
ATOM   6483  C CB  . TYR D  2 38  ? 19.421  -9.543  11.823  1.00 21.55  ? 38  TYR D CB  1 
ATOM   6484  C CG  . TYR D  2 38  ? 19.909  -9.113  13.195  1.00 23.77  ? 38  TYR D CG  1 
ATOM   6485  C CD1 . TYR D  2 38  ? 20.404  -10.051 14.104  1.00 26.56  ? 38  TYR D CD1 1 
ATOM   6486  C CD2 . TYR D  2 38  ? 19.896  -7.765  13.577  1.00 25.39  ? 38  TYR D CD2 1 
ATOM   6487  C CE1 . TYR D  2 38  ? 20.863  -9.665  15.363  1.00 28.65  ? 38  TYR D CE1 1 
ATOM   6488  C CE2 . TYR D  2 38  ? 20.346  -7.367  14.836  1.00 27.54  ? 38  TYR D CE2 1 
ATOM   6489  C CZ  . TYR D  2 38  ? 20.831  -8.322  15.723  1.00 29.52  ? 38  TYR D CZ  1 
ATOM   6490  O OH  . TYR D  2 38  ? 21.282  -7.939  16.969  1.00 29.56  ? 38  TYR D OH  1 
ATOM   6491  N N   . LYS D  2 39  ? 17.178  -7.514  11.337  1.00 20.66  ? 39  LYS D N   1 
ATOM   6492  C CA  . LYS D  2 39  ? 16.620  -6.197  11.656  1.00 20.54  ? 39  LYS D CA  1 
ATOM   6493  C C   . LYS D  2 39  ? 15.134  -6.246  12.027  1.00 19.76  ? 39  LYS D C   1 
ATOM   6494  O O   . LYS D  2 39  ? 14.737  -5.707  13.061  1.00 19.64  ? 39  LYS D O   1 
ATOM   6495  C CB  . LYS D  2 39  ? 16.864  -5.239  10.484  1.00 21.25  ? 39  LYS D CB  1 
ATOM   6496  C CG  . LYS D  2 39  ? 16.603  -3.765  10.765  1.00 24.69  ? 39  LYS D CG  1 
ATOM   6497  C CD  . LYS D  2 39  ? 16.881  -2.934  9.515   1.00 30.35  ? 39  LYS D CD  1 
ATOM   6498  C CE  . LYS D  2 39  ? 16.111  -1.615  9.519   1.00 32.46  ? 39  LYS D CE  1 
ATOM   6499  N NZ  . LYS D  2 39  ? 16.743  -0.585  10.395  1.00 34.16  ? 39  LYS D NZ  1 
ATOM   6500  N N   . SER D  2 40  ? 14.326  -6.897  11.191  1.00 18.94  ? 40  SER D N   1 
ATOM   6501  C CA  . SER D  2 40  ? 12.886  -7.025  11.440  1.00 18.18  ? 40  SER D CA  1 
ATOM   6502  C C   . SER D  2 40  ? 12.590  -7.891  12.660  1.00 18.10  ? 40  SER D C   1 
ATOM   6503  O O   . SER D  2 40  ? 11.703  -7.572  13.456  1.00 18.02  ? 40  SER D O   1 
ATOM   6504  C CB  . SER D  2 40  ? 12.176  -7.601  10.216  1.00 18.07  ? 40  SER D CB  1 
ATOM   6505  O OG  . SER D  2 40  ? 12.676  -8.887  9.898   1.00 16.55  ? 40  SER D OG  1 
ATOM   6506  N N   . THR D  2 41  ? 13.343  -8.983  12.791  1.00 17.58  ? 41  THR D N   1 
ATOM   6507  C CA  . THR D  2 41  ? 13.200  -9.933  13.891  1.00 17.25  ? 41  THR D CA  1 
ATOM   6508  C C   . THR D  2 41  ? 13.571  -9.311  15.238  1.00 17.23  ? 41  THR D C   1 
ATOM   6509  O O   . THR D  2 41  ? 12.838  -9.456  16.219  1.00 17.36  ? 41  THR D O   1 
ATOM   6510  C CB  . THR D  2 41  ? 14.048  -11.192 13.631  1.00 17.31  ? 41  THR D CB  1 
ATOM   6511  O OG1 . THR D  2 41  ? 13.495  -11.908 12.522  1.00 18.56  ? 41  THR D OG1 1 
ATOM   6512  C CG2 . THR D  2 41  ? 14.091  -12.105 14.848  1.00 17.66  ? 41  THR D CG2 1 
ATOM   6513  N N   . GLN D  2 42  ? 14.703  -8.614  15.277  1.00 17.03  ? 42  GLN D N   1 
ATOM   6514  C CA  . GLN D  2 42  ? 15.146  -7.939  16.492  1.00 16.39  ? 42  GLN D CA  1 
ATOM   6515  C C   . GLN D  2 42  ? 14.172  -6.835  16.897  1.00 15.61  ? 42  GLN D C   1 
ATOM   6516  O O   . GLN D  2 42  ? 13.918  -6.634  18.084  1.00 15.85  ? 42  GLN D O   1 
ATOM   6517  C CB  . GLN D  2 42  ? 16.556  -7.371  16.318  1.00 16.63  ? 42  GLN D CB  1 
ATOM   6518  C CG  . GLN D  2 42  ? 17.286  -7.118  17.630  1.00 18.67  ? 42  GLN D CG  1 
ATOM   6519  C CD  . GLN D  2 42  ? 17.497  -8.387  18.447  1.00 21.09  ? 42  GLN D CD  1 
ATOM   6520  O OE1 . GLN D  2 42  ? 17.742  -9.479  17.868  1.00 20.42  ? 42  GLN D OE1 1 
ATOM   6521  N NE2 . GLN D  2 42  ? 17.414  -8.285  19.746  1.00 18.92  ? 42  GLN D NE2 1 
ATOM   6522  N N   . SER D  2 43  ? 13.623  -6.133  15.910  1.00 14.48  ? 43  SER D N   1 
ATOM   6523  C CA  . SER D  2 43  ? 12.657  -5.071  16.174  1.00 13.62  ? 43  SER D CA  1 
ATOM   6524  C C   . SER D  2 43  ? 11.445  -5.619  16.910  1.00 12.59  ? 43  SER D C   1 
ATOM   6525  O O   . SER D  2 43  ? 10.971  -5.007  17.871  1.00 12.14  ? 43  SER D O   1 
ATOM   6526  C CB  . SER D  2 43  ? 12.217  -4.393  14.875  1.00 13.97  ? 43  SER D CB  1 
ATOM   6527  O OG  . SER D  2 43  ? 11.139  -3.505  15.113  1.00 12.63  ? 43  SER D OG  1 
ATOM   6528  N N   . ALA D  2 44  ? 10.961  -6.774  16.453  1.00 11.68  ? 44  ALA D N   1 
ATOM   6529  C CA  . ALA D  2 44  ? 9.793   -7.428  17.039  1.00 10.71  ? 44  ALA D CA  1 
ATOM   6530  C C   . ALA D  2 44  ? 10.085  -7.924  18.454  1.00 10.61  ? 44  ALA D C   1 
ATOM   6531  O O   . ALA D  2 44  ? 9.309   -7.665  19.372  1.00 10.85  ? 44  ALA D O   1 
ATOM   6532  C CB  . ALA D  2 44  ? 9.323   -8.567  16.153  1.00 10.01  ? 44  ALA D CB  1 
ATOM   6533  N N   . ILE D  2 45  ? 11.216  -8.612  18.620  1.00 10.15  ? 45  ILE D N   1 
ATOM   6534  C CA  . ILE D  2 45  ? 11.631  -9.156  19.915  1.00 10.26  ? 45  ILE D CA  1 
ATOM   6535  C C   . ILE D  2 45  ? 11.806  -8.056  20.964  1.00 10.61  ? 45  ILE D C   1 
ATOM   6536  O O   . ILE D  2 45  ? 11.355  -8.205  22.104  1.00 11.14  ? 45  ILE D O   1 
ATOM   6537  C CB  . ILE D  2 45  ? 12.925  -10.018 19.800  1.00 10.14  ? 45  ILE D CB  1 
ATOM   6538  C CG1 . ILE D  2 45  ? 12.645  -11.309 19.019  1.00 10.45  ? 45  ILE D CG1 1 
ATOM   6539  C CG2 . ILE D  2 45  ? 13.495  -10.341 21.183  1.00 8.74   ? 45  ILE D CG2 1 
ATOM   6540  C CD1 . ILE D  2 45  ? 13.892  -12.113 18.636  1.00 8.17   ? 45  ILE D CD1 1 
ATOM   6541  N N   . ASP D  2 46  ? 12.444  -6.955  20.569  1.00 10.31  ? 46  ASP D N   1 
ATOM   6542  C CA  . ASP D  2 46  ? 12.658  -5.822  21.466  1.00 10.77  ? 46  ASP D CA  1 
ATOM   6543  C C   . ASP D  2 46  ? 11.337  -5.269  21.999  1.00 10.90  ? 46  ASP D C   1 
ATOM   6544  O O   . ASP D  2 46  ? 11.248  -4.891  23.171  1.00 11.02  ? 46  ASP D O   1 
ATOM   6545  C CB  . ASP D  2 46  ? 13.460  -4.709  20.774  1.00 11.06  ? 46  ASP D CB  1 
ATOM   6546  C CG  . ASP D  2 46  ? 14.930  -5.060  20.590  1.00 11.04  ? 46  ASP D CG  1 
ATOM   6547  O OD1 . ASP D  2 46  ? 15.606  -4.365  19.801  1.00 12.25  ? 46  ASP D OD1 1 
ATOM   6548  O OD2 . ASP D  2 46  ? 15.412  -6.022  21.226  1.00 9.79   ? 46  ASP D OD2 1 
ATOM   6549  N N   . GLN D  2 47  ? 10.317  -5.237  21.140  1.00 11.15  ? 47  GLN D N   1 
ATOM   6550  C CA  . GLN D  2 47  ? 8.989   -4.752  21.526  1.00 12.15  ? 47  GLN D CA  1 
ATOM   6551  C C   . GLN D  2 47  ? 8.291   -5.701  22.501  1.00 12.78  ? 47  GLN D C   1 
ATOM   6552  O O   . GLN D  2 47  ? 7.684   -5.255  23.474  1.00 13.51  ? 47  GLN D O   1 
ATOM   6553  C CB  . GLN D  2 47  ? 8.118   -4.474  20.296  1.00 11.65  ? 47  GLN D CB  1 
ATOM   6554  C CG  . GLN D  2 47  ? 8.613   -3.305  19.446  1.00 12.71  ? 47  GLN D CG  1 
ATOM   6555  C CD  . GLN D  2 47  ? 7.788   -3.080  18.195  1.00 16.48  ? 47  GLN D CD  1 
ATOM   6556  O OE1 . GLN D  2 47  ? 6.658   -2.598  18.258  1.00 16.96  ? 47  GLN D OE1 1 
ATOM   6557  N NE2 . GLN D  2 47  ? 8.361   -3.409  17.043  1.00 16.18  ? 47  GLN D NE2 1 
ATOM   6558  N N   . ILE D  2 48  ? 8.392   -7.005  22.254  1.00 12.96  ? 48  ILE D N   1 
ATOM   6559  C CA  . ILE D  2 48  ? 7.849   -7.999  23.181  1.00 13.04  ? 48  ILE D CA  1 
ATOM   6560  C C   . ILE D  2 48  ? 8.613   -7.984  24.510  1.00 13.46  ? 48  ILE D C   1 
ATOM   6561  O O   . ILE D  2 48  ? 8.006   -8.109  25.577  1.00 14.00  ? 48  ILE D O   1 
ATOM   6562  C CB  . ILE D  2 48  ? 7.787   -9.418  22.548  1.00 12.87  ? 48  ILE D CB  1 
ATOM   6563  C CG1 . ILE D  2 48  ? 6.478   -9.608  21.774  1.00 12.17  ? 48  ILE D CG1 1 
ATOM   6564  C CG2 . ILE D  2 48  ? 7.860   -10.503 23.606  1.00 13.55  ? 48  ILE D CG2 1 
ATOM   6565  C CD1 . ILE D  2 48  ? 6.445   -8.968  20.402  1.00 9.40   ? 48  ILE D CD1 1 
ATOM   6566  N N   . THR D  2 49  ? 9.933   -7.810  24.442  1.00 13.59  ? 49  THR D N   1 
ATOM   6567  C CA  . THR D  2 49  ? 10.758  -7.616  25.639  1.00 13.66  ? 49  THR D CA  1 
ATOM   6568  C C   . THR D  2 49  ? 10.251  -6.405  26.426  1.00 13.27  ? 49  THR D C   1 
ATOM   6569  O O   . THR D  2 49  ? 10.109  -6.467  27.650  1.00 13.40  ? 49  THR D O   1 
ATOM   6570  C CB  . THR D  2 49  ? 12.248  -7.415  25.280  1.00 13.66  ? 49  THR D CB  1 
ATOM   6571  O OG1 . THR D  2 49  ? 12.696  -8.506  24.467  1.00 17.26  ? 49  THR D OG1 1 
ATOM   6572  C CG2 . THR D  2 49  ? 13.114  -7.338  26.533  1.00 12.92  ? 49  THR D CG2 1 
ATOM   6573  N N   . GLY D  2 50  ? 9.970   -5.316  25.710  1.00 12.10  ? 50  GLY D N   1 
ATOM   6574  C CA  . GLY D  2 50  ? 9.391   -4.114  26.302  1.00 10.74  ? 50  GLY D CA  1 
ATOM   6575  C C   . GLY D  2 50  ? 8.183   -4.408  27.169  1.00 10.04  ? 50  GLY D C   1 
ATOM   6576  O O   . GLY D  2 50  ? 8.117   -3.965  28.317  1.00 10.11  ? 50  GLY D O   1 
ATOM   6577  N N   . LYS D  2 51  ? 7.237   -5.166  26.618  1.00 9.57   ? 51  LYS D N   1 
ATOM   6578  C CA  . LYS D  2 51  ? 6.054   -5.601  27.350  1.00 9.86   ? 51  LYS D CA  1 
ATOM   6579  C C   . LYS D  2 51  ? 6.411   -6.385  28.611  1.00 11.14  ? 51  LYS D C   1 
ATOM   6580  O O   . LYS D  2 51  ? 5.800   -6.186  29.662  1.00 12.16  ? 51  LYS D O   1 
ATOM   6581  C CB  . LYS D  2 51  ? 5.154   -6.453  26.458  1.00 9.79   ? 51  LYS D CB  1 
ATOM   6582  C CG  . LYS D  2 51  ? 4.266   -5.659  25.523  1.00 9.30   ? 51  LYS D CG  1 
ATOM   6583  C CD  . LYS D  2 51  ? 3.536   -6.583  24.579  1.00 5.39   ? 51  LYS D CD  1 
ATOM   6584  C CE  . LYS D  2 51  ? 3.148   -5.865  23.301  1.00 5.06   ? 51  LYS D CE  1 
ATOM   6585  N NZ  . LYS D  2 51  ? 1.820   -5.230  23.409  1.00 2.00   ? 51  LYS D NZ  1 
ATOM   6586  N N   . LEU D  2 52  ? 7.400   -7.271  28.504  1.00 11.16  ? 52  LEU D N   1 
ATOM   6587  C CA  . LEU D  2 52  ? 7.816   -8.089  29.638  1.00 11.21  ? 52  LEU D CA  1 
ATOM   6588  C C   . LEU D  2 52  ? 8.471   -7.255  30.734  1.00 11.83  ? 52  LEU D C   1 
ATOM   6589  O O   . LEU D  2 52  ? 8.234   -7.493  31.918  1.00 12.16  ? 52  LEU D O   1 
ATOM   6590  C CB  . LEU D  2 52  ? 8.740   -9.227  29.192  1.00 11.09  ? 52  LEU D CB  1 
ATOM   6591  C CG  . LEU D  2 52  ? 8.114   -10.347 28.352  1.00 10.71  ? 52  LEU D CG  1 
ATOM   6592  C CD1 . LEU D  2 52  ? 9.192   -11.161 27.652  1.00 11.60  ? 52  LEU D CD1 1 
ATOM   6593  C CD2 . LEU D  2 52  ? 7.221   -11.246 29.192  1.00 9.82   ? 52  LEU D CD2 1 
ATOM   6594  N N   . ASN D  2 53  ? 9.274   -6.270  30.337  1.00 12.31  ? 53  ASN D N   1 
ATOM   6595  C CA  . ASN D  2 53  ? 9.928   -5.367  31.288  1.00 12.71  ? 53  ASN D CA  1 
ATOM   6596  C C   . ASN D  2 53  ? 8.927   -4.566  32.112  1.00 12.57  ? 53  ASN D C   1 
ATOM   6597  O O   . ASN D  2 53  ? 9.207   -4.186  33.251  1.00 11.77  ? 53  ASN D O   1 
ATOM   6598  C CB  . ASN D  2 53  ? 10.886  -4.418  30.566  1.00 12.78  ? 53  ASN D CB  1 
ATOM   6599  C CG  . ASN D  2 53  ? 12.057  -5.140  29.920  1.00 15.84  ? 53  ASN D CG  1 
ATOM   6600  O OD1 . ASN D  2 53  ? 12.384  -6.276  30.278  1.00 18.71  ? 53  ASN D OD1 1 
ATOM   6601  N ND2 . ASN D  2 53  ? 12.699  -4.479  28.961  1.00 15.29  ? 53  ASN D ND2 1 
ATOM   6602  N N   . ARG D  2 54  ? 7.758   -4.322  31.526  1.00 12.91  ? 54  ARG D N   1 
ATOM   6603  C CA  . ARG D  2 54  ? 6.694   -3.575  32.189  1.00 13.38  ? 54  ARG D CA  1 
ATOM   6604  C C   . ARG D  2 54  ? 5.953   -4.410  33.222  1.00 13.33  ? 54  ARG D C   1 
ATOM   6605  O O   . ARG D  2 54  ? 5.668   -3.927  34.317  1.00 13.92  ? 54  ARG D O   1 
ATOM   6606  C CB  . ARG D  2 54  ? 5.693   -3.049  31.165  1.00 13.17  ? 54  ARG D CB  1 
ATOM   6607  C CG  . ARG D  2 54  ? 6.039   -1.700  30.570  1.00 13.86  ? 54  ARG D CG  1 
ATOM   6608  C CD  . ARG D  2 54  ? 4.984   -1.261  29.561  1.00 16.75  ? 54  ARG D CD  1 
ATOM   6609  N NE  . ARG D  2 54  ? 3.629   -1.614  29.992  1.00 17.95  ? 54  ARG D NE  1 
ATOM   6610  C CZ  . ARG D  2 54  ? 2.830   -2.477  29.366  1.00 14.43  ? 54  ARG D CZ  1 
ATOM   6611  N NH1 . ARG D  2 54  ? 3.221   -3.081  28.252  1.00 13.31  ? 54  ARG D NH1 1 
ATOM   6612  N NH2 . ARG D  2 54  ? 1.625   -2.729  29.853  1.00 13.17  ? 54  ARG D NH2 1 
ATOM   6613  N N   . LEU D  2 55  ? 5.653   -5.658  32.866  1.00 13.19  ? 55  LEU D N   1 
ATOM   6614  C CA  . LEU D  2 55  ? 4.770   -6.517  33.655  1.00 13.13  ? 55  LEU D CA  1 
ATOM   6615  C C   . LEU D  2 55  ? 5.485   -7.411  34.660  1.00 13.04  ? 55  LEU D C   1 
ATOM   6616  O O   . LEU D  2 55  ? 4.921   -7.732  35.710  1.00 13.80  ? 55  LEU D O   1 
ATOM   6617  C CB  . LEU D  2 55  ? 3.924   -7.397  32.733  1.00 13.56  ? 55  LEU D CB  1 
ATOM   6618  C CG  . LEU D  2 55  ? 3.044   -6.732  31.676  1.00 16.55  ? 55  LEU D CG  1 
ATOM   6619  C CD1 . LEU D  2 55  ? 2.382   -7.793  30.813  1.00 19.37  ? 55  LEU D CD1 1 
ATOM   6620  C CD2 . LEU D  2 55  ? 1.997   -5.838  32.315  1.00 20.21  ? 55  LEU D CD2 1 
ATOM   6621  N N   . ILE D  2 56  ? 6.708   -7.825  34.331  1.00 12.07  ? 56  ILE D N   1 
ATOM   6622  C CA  . ILE D  2 56  ? 7.465   -8.757  35.165  1.00 12.20  ? 56  ILE D CA  1 
ATOM   6623  C C   . ILE D  2 56  ? 8.473   -8.015  36.050  1.00 13.18  ? 56  ILE D C   1 
ATOM   6624  O O   . ILE D  2 56  ? 9.153   -7.093  35.595  1.00 13.31  ? 56  ILE D O   1 
ATOM   6625  C CB  . ILE D  2 56  ? 8.198   -9.833  34.302  1.00 12.60  ? 56  ILE D CB  1 
ATOM   6626  C CG1 . ILE D  2 56  ? 7.286   -10.391 33.189  1.00 12.76  ? 56  ILE D CG1 1 
ATOM   6627  C CG2 . ILE D  2 56  ? 8.807   -10.943 35.175  1.00 9.61   ? 56  ILE D CG2 1 
ATOM   6628  C CD1 . ILE D  2 56  ? 6.093   -11.227 33.652  1.00 13.40  ? 56  ILE D CD1 1 
ATOM   6629  N N   . GLY D  2 57  ? 8.555   -8.418  37.316  1.00 14.11  ? 57  GLY D N   1 
ATOM   6630  C CA  . GLY D  2 57  ? 9.544   -7.877  38.247  1.00 15.15  ? 57  GLY D CA  1 
ATOM   6631  C C   . GLY D  2 57  ? 9.221   -6.494  38.780  1.00 16.29  ? 57  GLY D C   1 
ATOM   6632  O O   . GLY D  2 57  ? 10.125  -5.699  39.037  1.00 15.94  ? 57  GLY D O   1 
ATOM   6633  N N   . LYS D  2 58  ? 7.932   -6.209  38.945  1.00 17.41  ? 58  LYS D N   1 
ATOM   6634  C CA  . LYS D  2 58  ? 7.479   -4.943  39.510  1.00 18.93  ? 58  LYS D CA  1 
ATOM   6635  C C   . LYS D  2 58  ? 7.715   -4.909  41.015  1.00 19.41  ? 58  LYS D C   1 
ATOM   6636  O O   . LYS D  2 58  ? 7.803   -5.956  41.663  1.00 19.59  ? 58  LYS D O   1 
ATOM   6637  C CB  . LYS D  2 58  ? 5.989   -4.736  39.235  1.00 19.77  ? 58  LYS D CB  1 
ATOM   6638  C CG  . LYS D  2 58  ? 5.646   -4.192  37.855  1.00 23.47  ? 58  LYS D CG  1 
ATOM   6639  C CD  . LYS D  2 58  ? 4.141   -4.302  37.619  1.00 29.71  ? 58  LYS D CD  1 
ATOM   6640  C CE  . LYS D  2 58  ? 3.621   -3.201  36.704  1.00 33.32  ? 58  LYS D CE  1 
ATOM   6641  N NZ  . LYS D  2 58  ? 2.172   -3.388  36.414  1.00 34.42  ? 58  LYS D NZ  1 
ATOM   6642  N N   . THR D  2 59  ? 7.815   -3.698  41.561  1.00 19.41  ? 59  THR D N   1 
ATOM   6643  C CA  . THR D  2 59  ? 7.941   -3.500  42.999  1.00 19.11  ? 59  THR D CA  1 
ATOM   6644  C C   . THR D  2 59  ? 6.548   -3.290  43.583  1.00 19.13  ? 59  THR D C   1 
ATOM   6645  O O   . THR D  2 59  ? 5.966   -2.214  43.449  1.00 19.74  ? 59  THR D O   1 
ATOM   6646  C CB  . THR D  2 59  ? 8.857   -2.290  43.333  1.00 19.26  ? 59  THR D CB  1 
ATOM   6647  O OG1 . THR D  2 59  ? 10.103  -2.425  42.639  1.00 18.62  ? 59  THR D OG1 1 
ATOM   6648  C CG2 . THR D  2 59  ? 9.123   -2.198  44.837  1.00 17.40  ? 59  THR D CG2 1 
ATOM   6649  N N   . ASN D  2 60  ? 6.015   -4.328  44.218  1.00 18.67  ? 60  ASN D N   1 
ATOM   6650  C CA  . ASN D  2 60  ? 4.692   -4.269  44.828  1.00 18.45  ? 60  ASN D CA  1 
ATOM   6651  C C   . ASN D  2 60  ? 4.713   -3.554  46.168  1.00 18.17  ? 60  ASN D C   1 
ATOM   6652  O O   . ASN D  2 60  ? 5.733   -3.565  46.858  1.00 17.48  ? 60  ASN D O   1 
ATOM   6653  C CB  . ASN D  2 60  ? 4.144   -5.677  45.008  1.00 18.60  ? 60  ASN D CB  1 
ATOM   6654  C CG  . ASN D  2 60  ? 3.953   -6.391  43.694  1.00 20.48  ? 60  ASN D CG  1 
ATOM   6655  O OD1 . ASN D  2 60  ? 3.088   -6.023  42.895  1.00 26.64  ? 60  ASN D OD1 1 
ATOM   6656  N ND2 . ASN D  2 60  ? 4.757   -7.424  43.460  1.00 17.84  ? 60  ASN D ND2 1 
ATOM   6657  N N   . GLN D  2 61  ? 3.589   -2.937  46.534  1.00 18.15  ? 61  GLN D N   1 
ATOM   6658  C CA  . GLN D  2 61  ? 3.496   -2.231  47.813  1.00 18.33  ? 61  GLN D CA  1 
ATOM   6659  C C   . GLN D  2 61  ? 3.017   -3.131  48.949  1.00 18.22  ? 61  GLN D C   1 
ATOM   6660  O O   . GLN D  2 61  ? 2.276   -4.094  48.725  1.00 18.24  ? 61  GLN D O   1 
ATOM   6661  C CB  . GLN D  2 61  ? 2.660   -0.946  47.702  1.00 18.11  ? 61  GLN D CB  1 
ATOM   6662  C CG  . GLN D  2 61  ? 1.166   -1.135  47.504  1.00 19.76  ? 61  GLN D CG  1 
ATOM   6663  C CD  . GLN D  2 61  ? 0.467   0.154   47.087  1.00 19.99  ? 61  GLN D CD  1 
ATOM   6664  O OE1 . GLN D  2 61  ? 0.521   0.555   45.922  1.00 14.77  ? 61  GLN D OE1 1 
ATOM   6665  N NE2 . GLN D  2 61  ? -0.201  0.801   48.038  1.00 19.54  ? 61  GLN D NE2 1 
ATOM   6666  N N   . GLN D  2 62  ? 3.462   -2.813  50.163  1.00 17.65  ? 62  GLN D N   1 
ATOM   6667  C CA  . GLN D  2 62  ? 3.210   -3.648  51.329  1.00 17.46  ? 62  GLN D CA  1 
ATOM   6668  C C   . GLN D  2 62  ? 1.765   -3.582  51.807  1.00 17.33  ? 62  GLN D C   1 
ATOM   6669  O O   . GLN D  2 62  ? 1.133   -2.521  51.779  1.00 17.60  ? 62  GLN D O   1 
ATOM   6670  C CB  . GLN D  2 62  ? 4.143   -3.261  52.478  1.00 17.57  ? 62  GLN D CB  1 
ATOM   6671  C CG  . GLN D  2 62  ? 4.316   -4.357  53.522  1.00 19.03  ? 62  GLN D CG  1 
ATOM   6672  C CD  . GLN D  2 62  ? 4.956   -3.859  54.799  1.00 23.85  ? 62  GLN D CD  1 
ATOM   6673  O OE1 . GLN D  2 62  ? 4.387   -3.028  55.513  1.00 26.76  ? 62  GLN D OE1 1 
ATOM   6674  N NE2 . GLN D  2 62  ? 6.142   -4.375  55.105  1.00 24.27  ? 62  GLN D NE2 1 
ATOM   6675  N N   . PHE D  2 63  ? 1.255   -4.731  52.241  1.00 16.37  ? 63  PHE D N   1 
ATOM   6676  C CA  . PHE D  2 63  ? -0.022  -4.806  52.940  1.00 14.74  ? 63  PHE D CA  1 
ATOM   6677  C C   . PHE D  2 63  ? 0.116   -5.646  54.198  1.00 13.75  ? 63  PHE D C   1 
ATOM   6678  O O   . PHE D  2 63  ? 0.857   -6.631  54.222  1.00 13.89  ? 63  PHE D O   1 
ATOM   6679  C CB  . PHE D  2 63  ? -1.110  -5.377  52.031  1.00 14.92  ? 63  PHE D CB  1 
ATOM   6680  C CG  . PHE D  2 63  ? -1.594  -4.411  50.990  1.00 15.20  ? 63  PHE D CG  1 
ATOM   6681  C CD1 . PHE D  2 63  ? -2.682  -3.580  51.248  1.00 15.33  ? 63  PHE D CD1 1 
ATOM   6682  C CD2 . PHE D  2 63  ? -0.961  -4.325  49.753  1.00 16.43  ? 63  PHE D CD2 1 
ATOM   6683  C CE1 . PHE D  2 63  ? -3.135  -2.678  50.289  1.00 15.60  ? 63  PHE D CE1 1 
ATOM   6684  C CE2 . PHE D  2 63  ? -1.407  -3.426  48.784  1.00 18.50  ? 63  PHE D CE2 1 
ATOM   6685  C CZ  . PHE D  2 63  ? -2.497  -2.601  49.054  1.00 17.41  ? 63  PHE D CZ  1 
ATOM   6686  N N   . GLU D  2 64  ? -0.599  -5.242  55.243  1.00 12.88  ? 64  GLU D N   1 
ATOM   6687  C CA  . GLU D  2 64  ? -0.579  -5.942  56.522  1.00 11.89  ? 64  GLU D CA  1 
ATOM   6688  C C   . GLU D  2 64  ? -1.854  -6.764  56.696  1.00 11.89  ? 64  GLU D C   1 
ATOM   6689  O O   . GLU D  2 64  ? -2.796  -6.630  55.908  1.00 11.61  ? 64  GLU D O   1 
ATOM   6690  C CB  . GLU D  2 64  ? -0.458  -4.941  57.677  1.00 11.22  ? 64  GLU D CB  1 
ATOM   6691  C CG  . GLU D  2 64  ? 0.619   -3.877  57.506  1.00 11.73  ? 64  GLU D CG  1 
ATOM   6692  C CD  . GLU D  2 64  ? 0.602   -2.845  58.620  1.00 14.50  ? 64  GLU D CD  1 
ATOM   6693  O OE1 . GLU D  2 64  ? -0.463  -2.634  59.236  1.00 13.96  ? 64  GLU D OE1 1 
ATOM   6694  O OE2 . GLU D  2 64  ? 1.661   -2.238  58.883  1.00 19.85  ? 64  GLU D OE2 1 
ATOM   6695  N N   . LEU D  2 65  ? -1.872  -7.611  57.726  1.00 11.98  ? 65  LEU D N   1 
ATOM   6696  C CA  . LEU D  2 65  ? -3.099  -8.257  58.190  1.00 11.93  ? 65  LEU D CA  1 
ATOM   6697  C C   . LEU D  2 65  ? -4.097  -7.224  58.692  1.00 11.62  ? 65  LEU D C   1 
ATOM   6698  O O   . LEU D  2 65  ? -3.729  -6.276  59.390  1.00 10.93  ? 65  LEU D O   1 
ATOM   6699  C CB  . LEU D  2 65  ? -2.808  -9.216  59.344  1.00 12.45  ? 65  LEU D CB  1 
ATOM   6700  C CG  . LEU D  2 65  ? -2.430  -10.681 59.145  1.00 13.49  ? 65  LEU D CG  1 
ATOM   6701  C CD1 . LEU D  2 65  ? -2.100  -11.255 60.507  1.00 15.51  ? 65  LEU D CD1 1 
ATOM   6702  C CD2 . LEU D  2 65  ? -3.548  -11.480 58.488  1.00 13.51  ? 65  LEU D CD2 1 
ATOM   6703  N N   . ILE D  2 66  ? -5.363  -7.422  58.344  1.00 12.11  ? 66  ILE D N   1 
ATOM   6704  C CA  . ILE D  2 66  ? -6.444  -6.589  58.869  1.00 12.16  ? 66  ILE D CA  1 
ATOM   6705  C C   . ILE D  2 66  ? -7.544  -7.429  59.515  1.00 12.90  ? 66  ILE D C   1 
ATOM   6706  O O   . ILE D  2 66  ? -8.464  -6.890  60.134  1.00 13.67  ? 66  ILE D O   1 
ATOM   6707  C CB  . ILE D  2 66  ? -7.042  -5.656  57.800  1.00 11.69  ? 66  ILE D CB  1 
ATOM   6708  C CG1 . ILE D  2 66  ? -7.312  -6.426  56.505  1.00 9.91   ? 66  ILE D CG1 1 
ATOM   6709  C CG2 . ILE D  2 66  ? -6.120  -4.465  57.569  1.00 11.81  ? 66  ILE D CG2 1 
ATOM   6710  C CD1 . ILE D  2 66  ? -8.278  -5.737  55.570  1.00 12.90  ? 66  ILE D CD1 1 
ATOM   6711  N N   . ASP D  2 67  ? -7.443  -8.746  59.360  1.00 13.33  ? 67  ASP D N   1 
ATOM   6712  C CA  . ASP D  2 67  ? -8.297  -9.683  60.085  1.00 14.25  ? 67  ASP D CA  1 
ATOM   6713  C C   . ASP D  2 67  ? -7.472  -10.793 60.732  1.00 14.74  ? 67  ASP D C   1 
ATOM   6714  O O   . ASP D  2 67  ? -6.241  -10.751 60.716  1.00 15.76  ? 67  ASP D O   1 
ATOM   6715  C CB  . ASP D  2 67  ? -9.425  -10.243 59.201  1.00 14.70  ? 67  ASP D CB  1 
ATOM   6716  C CG  . ASP D  2 67  ? -8.941  -10.722 57.837  1.00 17.78  ? 67  ASP D CG  1 
ATOM   6717  O OD1 . ASP D  2 67  ? -7.714  -10.769 57.595  1.00 21.74  ? 67  ASP D OD1 1 
ATOM   6718  O OD2 . ASP D  2 67  ? -9.808  -11.054 56.999  1.00 18.41  ? 67  ASP D OD2 1 
ATOM   6719  N N   . ASN D  2 68  ? -8.156  -11.781 61.301  1.00 15.19  ? 68  ASN D N   1 
ATOM   6720  C CA  . ASN D  2 68  ? -7.519  -12.785 62.136  1.00 15.15  ? 68  ASN D CA  1 
ATOM   6721  C C   . ASN D  2 68  ? -8.101  -14.172 61.869  1.00 15.93  ? 68  ASN D C   1 
ATOM   6722  O O   . ASN D  2 68  ? -9.308  -14.379 61.990  1.00 16.33  ? 68  ASN D O   1 
ATOM   6723  C CB  . ASN D  2 68  ? -7.687  -12.390 63.609  1.00 14.63  ? 68  ASN D CB  1 
ATOM   6724  C CG  . ASN D  2 68  ? -6.769  -13.158 64.545  1.00 13.28  ? 68  ASN D CG  1 
ATOM   6725  O OD1 . ASN D  2 68  ? -6.519  -14.350 64.364  1.00 12.78  ? 68  ASN D OD1 1 
ATOM   6726  N ND2 . ASN D  2 68  ? -6.274  -12.474 65.569  1.00 12.28  ? 68  ASN D ND2 1 
ATOM   6727  N N   . GLU D  2 69  ? -7.231  -15.110 61.503  1.00 16.70  ? 69  GLU D N   1 
ATOM   6728  C CA  . GLU D  2 69  ? -7.625  -16.494 61.228  1.00 18.11  ? 69  GLU D CA  1 
ATOM   6729  C C   . GLU D  2 69  ? -7.880  -17.312 62.492  1.00 18.51  ? 69  GLU D C   1 
ATOM   6730  O O   . GLU D  2 69  ? -8.633  -18.289 62.463  1.00 18.23  ? 69  GLU D O   1 
ATOM   6731  C CB  . GLU D  2 69  ? -6.546  -17.199 60.409  1.00 18.17  ? 69  GLU D CB  1 
ATOM   6732  C CG  . GLU D  2 69  ? -6.622  -16.954 58.919  1.00 21.49  ? 69  GLU D CG  1 
ATOM   6733  C CD  . GLU D  2 69  ? -5.564  -17.724 58.141  1.00 24.87  ? 69  GLU D CD  1 
ATOM   6734  O OE1 . GLU D  2 69  ? -5.013  -18.710 58.681  1.00 22.60  ? 69  GLU D OE1 1 
ATOM   6735  O OE2 . GLU D  2 69  ? -5.288  -17.340 56.983  1.00 26.84  ? 69  GLU D OE2 1 
ATOM   6736  N N   . PHE D  2 70  ? -7.239  -16.918 63.590  1.00 19.17  ? 70  PHE D N   1 
ATOM   6737  C CA  . PHE D  2 70  ? -7.257  -17.708 64.821  1.00 19.91  ? 70  PHE D CA  1 
ATOM   6738  C C   . PHE D  2 70  ? -8.257  -17.181 65.839  1.00 20.79  ? 70  PHE D C   1 
ATOM   6739  O O   . PHE D  2 70  ? -8.611  -17.877 66.789  1.00 21.19  ? 70  PHE D O   1 
ATOM   6740  C CB  . PHE D  2 70  ? -5.860  -17.759 65.455  1.00 19.61  ? 70  PHE D CB  1 
ATOM   6741  C CG  . PHE D  2 70  ? -4.774  -18.243 64.527  1.00 19.39  ? 70  PHE D CG  1 
ATOM   6742  C CD1 . PHE D  2 70  ? -5.002  -19.292 63.636  1.00 19.32  ? 70  PHE D CD1 1 
ATOM   6743  C CD2 . PHE D  2 70  ? -3.507  -17.665 64.570  1.00 18.40  ? 70  PHE D CD2 1 
ATOM   6744  C CE1 . PHE D  2 70  ? -3.992  -19.739 62.783  1.00 20.36  ? 70  PHE D CE1 1 
ATOM   6745  C CE2 . PHE D  2 70  ? -2.489  -18.106 63.725  1.00 19.50  ? 70  PHE D CE2 1 
ATOM   6746  C CZ  . PHE D  2 70  ? -2.732  -19.146 62.830  1.00 19.41  ? 70  PHE D CZ  1 
ATOM   6747  N N   . ASN D  2 71  ? -8.703  -15.947 65.638  1.00 22.38  ? 71  ASN D N   1 
ATOM   6748  C CA  . ASN D  2 71  ? -9.582  -15.278 66.580  1.00 23.40  ? 71  ASN D CA  1 
ATOM   6749  C C   . ASN D  2 71  ? -10.472 -14.304 65.824  1.00 23.87  ? 71  ASN D C   1 
ATOM   6750  O O   . ASN D  2 71  ? -10.088 -13.155 65.603  1.00 24.08  ? 71  ASN D O   1 
ATOM   6751  C CB  . ASN D  2 71  ? -8.747  -14.538 67.628  1.00 23.69  ? 71  ASN D CB  1 
ATOM   6752  C CG  . ASN D  2 71  ? -9.459  -14.403 68.957  1.00 26.41  ? 71  ASN D CG  1 
ATOM   6753  O OD1 . ASN D  2 71  ? -9.506  -15.349 69.749  1.00 29.98  ? 71  ASN D OD1 1 
ATOM   6754  N ND2 . ASN D  2 71  ? -10.003 -13.218 69.221  1.00 26.29  ? 71  ASN D ND2 1 
ATOM   6755  N N   . GLU D  2 72  ? -11.654 -14.771 65.423  1.00 24.75  ? 72  GLU D N   1 
ATOM   6756  C CA  . GLU D  2 72  ? -12.565 -13.982 64.585  1.00 25.54  ? 72  GLU D CA  1 
ATOM   6757  C C   . GLU D  2 72  ? -12.810 -12.582 65.151  1.00 25.09  ? 72  GLU D C   1 
ATOM   6758  O O   . GLU D  2 72  ? -13.127 -12.425 66.332  1.00 25.36  ? 72  GLU D O   1 
ATOM   6759  C CB  . GLU D  2 72  ? -13.897 -14.714 64.372  1.00 25.91  ? 72  GLU D CB  1 
ATOM   6760  C CG  . GLU D  2 72  ? -14.692 -14.211 63.161  1.00 28.96  ? 72  GLU D CG  1 
ATOM   6761  C CD  . GLU D  2 72  ? -16.112 -14.763 63.090  1.00 32.28  ? 72  GLU D CD  1 
ATOM   6762  O OE1 . GLU D  2 72  ? -16.629 -14.916 61.961  1.00 32.04  ? 72  GLU D OE1 1 
ATOM   6763  O OE2 . GLU D  2 72  ? -16.715 -15.036 64.153  1.00 32.63  ? 72  GLU D OE2 1 
ATOM   6764  N N   . ILE D  2 73  ? -12.647 -11.577 64.294  1.00 24.71  ? 73  ILE D N   1 
ATOM   6765  C CA  . ILE D  2 73  ? -12.847 -10.171 64.663  1.00 23.88  ? 73  ILE D CA  1 
ATOM   6766  C C   . ILE D  2 73  ? -14.337 -9.845  64.781  1.00 24.50  ? 73  ILE D C   1 
ATOM   6767  O O   . ILE D  2 73  ? -15.179 -10.676 64.430  1.00 24.78  ? 73  ILE D O   1 
ATOM   6768  C CB  . ILE D  2 73  ? -12.160 -9.217  63.653  1.00 23.14  ? 73  ILE D CB  1 
ATOM   6769  C CG1 . ILE D  2 73  ? -12.616 -9.524  62.222  1.00 20.98  ? 73  ILE D CG1 1 
ATOM   6770  C CG2 . ILE D  2 73  ? -10.641 -9.321  63.773  1.00 21.59  ? 73  ILE D CG2 1 
ATOM   6771  C CD1 . ILE D  2 73  ? -12.194 -8.492  61.205  1.00 19.04  ? 73  ILE D CD1 1 
ATOM   6772  N N   . GLU D  2 74  ? -14.665 -8.649  65.272  1.00 24.95  ? 74  GLU D N   1 
ATOM   6773  C CA  . GLU D  2 74  ? -16.071 -8.258  65.407  1.00 25.87  ? 74  GLU D CA  1 
ATOM   6774  C C   . GLU D  2 74  ? -16.788 -8.334  64.055  1.00 25.30  ? 74  GLU D C   1 
ATOM   6775  O O   . GLU D  2 74  ? -16.247 -7.931  63.023  1.00 24.98  ? 74  GLU D O   1 
ATOM   6776  C CB  . GLU D  2 74  ? -16.243 -6.891  66.098  1.00 26.22  ? 74  GLU D CB  1 
ATOM   6777  C CG  . GLU D  2 74  ? -15.827 -5.660  65.286  1.00 32.65  ? 74  GLU D CG  1 
ATOM   6778  C CD  . GLU D  2 74  ? -16.424 -4.355  65.822  1.00 38.36  ? 74  GLU D CD  1 
ATOM   6779  O OE1 . GLU D  2 74  ? -16.779 -4.287  67.022  1.00 40.43  ? 74  GLU D OE1 1 
ATOM   6780  O OE2 . GLU D  2 74  ? -16.536 -3.388  65.036  1.00 39.25  ? 74  GLU D OE2 1 
ATOM   6781  N N   . GLN D  2 75  ? -17.999 -8.877  64.082  1.00 25.33  ? 75  GLN D N   1 
ATOM   6782  C CA  . GLN D  2 75  ? -18.726 -9.275  62.876  1.00 25.18  ? 75  GLN D CA  1 
ATOM   6783  C C   . GLN D  2 75  ? -18.941 -8.159  61.847  1.00 24.17  ? 75  GLN D C   1 
ATOM   6784  O O   . GLN D  2 75  ? -18.925 -8.416  60.641  1.00 23.80  ? 75  GLN D O   1 
ATOM   6785  C CB  . GLN D  2 75  ? -20.073 -9.900  63.260  1.00 25.97  ? 75  GLN D CB  1 
ATOM   6786  C CG  . GLN D  2 75  ? -19.988 -11.097 64.215  1.00 29.44  ? 75  GLN D CG  1 
ATOM   6787  C CD  . GLN D  2 75  ? -19.875 -12.436 63.495  1.00 34.36  ? 75  GLN D CD  1 
ATOM   6788  O OE1 . GLN D  2 75  ? -19.486 -12.504 62.326  1.00 35.53  ? 75  GLN D OE1 1 
ATOM   6789  N NE2 . GLN D  2 75  ? -20.218 -13.511 64.199  1.00 34.35  ? 75  GLN D NE2 1 
ATOM   6790  N N   . GLN D  2 76  ? -19.133 -6.930  62.324  1.00 23.30  ? 76  GLN D N   1 
ATOM   6791  C CA  . GLN D  2 76  ? -19.457 -5.807  61.444  1.00 22.76  ? 76  GLN D CA  1 
ATOM   6792  C C   . GLN D  2 76  ? -18.264 -5.392  60.577  1.00 21.93  ? 76  GLN D C   1 
ATOM   6793  O O   . GLN D  2 76  ? -18.387 -5.305  59.354  1.00 22.01  ? 76  GLN D O   1 
ATOM   6794  C CB  . GLN D  2 76  ? -20.011 -4.623  62.245  1.00 23.09  ? 76  GLN D CB  1 
ATOM   6795  C CG  . GLN D  2 76  ? -20.902 -3.685  61.424  1.00 25.39  ? 76  GLN D CG  1 
ATOM   6796  C CD  . GLN D  2 76  ? -21.655 -2.664  62.272  1.00 28.65  ? 76  GLN D CD  1 
ATOM   6797  O OE1 . GLN D  2 76  ? -21.290 -2.388  63.421  1.00 27.21  ? 76  GLN D OE1 1 
ATOM   6798  N NE2 . GLN D  2 76  ? -22.715 -2.095  61.700  1.00 26.13  ? 76  GLN D NE2 1 
ATOM   6799  N N   . ILE D  2 77  ? -17.122 -5.147  61.216  1.00 20.99  ? 77  ILE D N   1 
ATOM   6800  C CA  . ILE D  2 77  ? -15.867 -4.845  60.524  1.00 19.88  ? 77  ILE D CA  1 
ATOM   6801  C C   . ILE D  2 77  ? -15.466 -5.995  59.593  1.00 18.47  ? 77  ILE D C   1 
ATOM   6802  O O   . ILE D  2 77  ? -15.071 -5.767  58.445  1.00 18.36  ? 77  ILE D O   1 
ATOM   6803  C CB  . ILE D  2 77  ? -14.717 -4.546  61.541  1.00 20.44  ? 77  ILE D CB  1 
ATOM   6804  C CG1 . ILE D  2 77  ? -15.000 -3.269  62.342  1.00 23.63  ? 77  ILE D CG1 1 
ATOM   6805  C CG2 . ILE D  2 77  ? -13.362 -4.435  60.851  1.00 20.59  ? 77  ILE D CG2 1 
ATOM   6806  C CD1 . ILE D  2 77  ? -14.981 -1.967  61.533  1.00 25.75  ? 77  ILE D CD1 1 
ATOM   6807  N N   . GLY D  2 78  ? -15.580 -7.222  60.097  1.00 17.10  ? 78  GLY D N   1 
ATOM   6808  C CA  . GLY D  2 78  ? -15.247 -8.424  59.336  1.00 15.84  ? 78  GLY D CA  1 
ATOM   6809  C C   . GLY D  2 78  ? -15.965 -8.506  58.007  1.00 15.25  ? 78  GLY D C   1 
ATOM   6810  O O   . GLY D  2 78  ? -15.337 -8.754  56.975  1.00 15.03  ? 78  GLY D O   1 
ATOM   6811  N N   . ASN D  2 79  ? -17.280 -8.286  58.039  1.00 15.24  ? 79  ASN D N   1 
ATOM   6812  C CA  . ASN D  2 79  ? -18.110 -8.275  56.832  1.00 15.46  ? 79  ASN D CA  1 
ATOM   6813  C C   . ASN D  2 79  ? -17.734 -7.179  55.841  1.00 14.33  ? 79  ASN D C   1 
ATOM   6814  O O   . ASN D  2 79  ? -17.750 -7.407  54.635  1.00 14.55  ? 79  ASN D O   1 
ATOM   6815  C CB  . ASN D  2 79  ? -19.600 -8.195  57.184  1.00 16.27  ? 79  ASN D CB  1 
ATOM   6816  C CG  . ASN D  2 79  ? -20.238 -9.571  57.356  1.00 19.65  ? 79  ASN D CG  1 
ATOM   6817  O OD1 . ASN D  2 79  ? -20.196 -10.408 56.451  1.00 23.10  ? 79  ASN D OD1 1 
ATOM   6818  N ND2 . ASN D  2 79  ? -20.843 -9.804  58.519  1.00 21.49  ? 79  ASN D ND2 1 
ATOM   6819  N N   . VAL D  2 80  ? -17.389 -6.000  56.354  1.00 13.22  ? 80  VAL D N   1 
ATOM   6820  C CA  . VAL D  2 80  ? -16.926 -4.899  55.508  1.00 12.30  ? 80  VAL D CA  1 
ATOM   6821  C C   . VAL D  2 80  ? -15.593 -5.251  54.851  1.00 12.02  ? 80  VAL D C   1 
ATOM   6822  O O   . VAL D  2 80  ? -15.398 -4.982  53.666  1.00 12.44  ? 80  VAL D O   1 
ATOM   6823  C CB  . VAL D  2 80  ? -16.826 -3.552  56.277  1.00 12.31  ? 80  VAL D CB  1 
ATOM   6824  C CG1 . VAL D  2 80  ? -16.196 -2.466  55.401  1.00 10.71  ? 80  VAL D CG1 1 
ATOM   6825  C CG2 . VAL D  2 80  ? -18.202 -3.104  56.752  1.00 10.36  ? 80  VAL D CG2 1 
ATOM   6826  N N   . ILE D  2 81  ? -14.688 -5.859  55.616  1.00 11.50  ? 81  ILE D N   1 
ATOM   6827  C CA  . ILE D  2 81  ? -13.406 -6.314  55.072  1.00 10.84  ? 81  ILE D CA  1 
ATOM   6828  C C   . ILE D  2 81  ? -13.630 -7.333  53.958  1.00 11.29  ? 81  ILE D C   1 
ATOM   6829  O O   . ILE D  2 81  ? -13.072 -7.195  52.867  1.00 10.87  ? 81  ILE D O   1 
ATOM   6830  C CB  . ILE D  2 81  ? -12.475 -6.892  56.165  1.00 10.46  ? 81  ILE D CB  1 
ATOM   6831  C CG1 . ILE D  2 81  ? -11.949 -5.767  57.061  1.00 9.05   ? 81  ILE D CG1 1 
ATOM   6832  C CG2 . ILE D  2 81  ? -11.306 -7.642  55.535  1.00 8.50   ? 81  ILE D CG2 1 
ATOM   6833  C CD1 . ILE D  2 81  ? -11.381 -6.237  58.387  1.00 6.60   ? 81  ILE D CD1 1 
ATOM   6834  N N   . ASN D  2 82  ? -14.466 -8.336  54.229  1.00 12.20  ? 82  ASN D N   1 
ATOM   6835  C CA  . ASN D  2 82  ? -14.787 -9.369  53.241  1.00 13.20  ? 82  ASN D CA  1 
ATOM   6836  C C   . ASN D  2 82  ? -15.395 -8.788  51.964  1.00 13.10  ? 82  ASN D C   1 
ATOM   6837  O O   . ASN D  2 82  ? -15.008 -9.161  50.856  1.00 13.60  ? 82  ASN D O   1 
ATOM   6838  C CB  . ASN D  2 82  ? -15.688 -10.450 53.855  1.00 13.86  ? 82  ASN D CB  1 
ATOM   6839  C CG  . ASN D  2 82  ? -14.921 -11.408 54.770  1.00 18.79  ? 82  ASN D CG  1 
ATOM   6840  O OD1 . ASN D  2 82  ? -13.730 -11.223 55.022  1.00 20.18  ? 82  ASN D OD1 1 
ATOM   6841  N ND2 . ASN D  2 82  ? -15.607 -12.436 55.268  1.00 29.10  ? 82  ASN D ND2 1 
ATOM   6842  N N   . TRP D  2 83  ? -16.322 -7.850  52.136  1.00 12.78  ? 83  TRP D N   1 
ATOM   6843  C CA  . TRP D  2 83  ? -16.945 -7.133  51.031  1.00 12.00  ? 83  TRP D CA  1 
ATOM   6844  C C   . TRP D  2 83  ? -15.940 -6.306  50.215  1.00 11.47  ? 83  TRP D C   1 
ATOM   6845  O O   . TRP D  2 83  ? -16.005 -6.284  48.981  1.00 11.05  ? 83  TRP D O   1 
ATOM   6846  C CB  . TRP D  2 83  ? -18.073 -6.253  51.570  1.00 11.70  ? 83  TRP D CB  1 
ATOM   6847  C CG  . TRP D  2 83  ? -18.612 -5.250  50.599  1.00 15.19  ? 83  TRP D CG  1 
ATOM   6848  C CD1 . TRP D  2 83  ? -19.343 -5.507  49.474  1.00 18.13  ? 83  TRP D CD1 1 
ATOM   6849  C CD2 . TRP D  2 83  ? -18.481 -3.825  50.677  1.00 16.83  ? 83  TRP D CD2 1 
ATOM   6850  N NE1 . TRP D  2 83  ? -19.671 -4.331  48.844  1.00 19.21  ? 83  TRP D NE1 1 
ATOM   6851  C CE2 . TRP D  2 83  ? -19.152 -3.283  49.559  1.00 18.57  ? 83  TRP D CE2 1 
ATOM   6852  C CE3 . TRP D  2 83  ? -17.858 -2.954  51.581  1.00 14.31  ? 83  TRP D CE3 1 
ATOM   6853  C CZ2 . TRP D  2 83  ? -19.219 -1.902  49.318  1.00 17.46  ? 83  TRP D CZ2 1 
ATOM   6854  C CZ3 . TRP D  2 83  ? -17.928 -1.583  51.343  1.00 16.50  ? 83  TRP D CZ3 1 
ATOM   6855  C CH2 . TRP D  2 83  ? -18.603 -1.072  50.219  1.00 15.22  ? 83  TRP D CH2 1 
ATOM   6856  N N   . THR D  2 84  ? -15.023 -5.631  50.905  1.00 10.99  ? 84  THR D N   1 
ATOM   6857  C CA  . THR D  2 84  ? -14.021 -4.783  50.254  1.00 10.91  ? 84  THR D CA  1 
ATOM   6858  C C   . THR D  2 84  ? -13.037 -5.638  49.468  1.00 11.63  ? 84  THR D C   1 
ATOM   6859  O O   . THR D  2 84  ? -12.826 -5.410  48.274  1.00 11.57  ? 84  THR D O   1 
ATOM   6860  C CB  . THR D  2 84  ? -13.257 -3.904  51.280  1.00 10.69  ? 84  THR D CB  1 
ATOM   6861  O OG1 . THR D  2 84  ? -14.181 -3.043  51.948  1.00 10.17  ? 84  THR D OG1 1 
ATOM   6862  C CG2 . THR D  2 84  ? -12.192 -3.045  50.600  1.00 8.66   ? 84  THR D CG2 1 
ATOM   6863  N N   . ARG D  2 85  ? -12.458 -6.629  50.145  1.00 12.07  ? 85  ARG D N   1 
ATOM   6864  C CA  . ARG D  2 85  ? -11.473 -7.521  49.547  1.00 13.26  ? 85  ARG D CA  1 
ATOM   6865  C C   . ARG D  2 85  ? -11.997 -8.178  48.269  1.00 13.51  ? 85  ARG D C   1 
ATOM   6866  O O   . ARG D  2 85  ? -11.328 -8.141  47.232  1.00 14.01  ? 85  ARG D O   1 
ATOM   6867  C CB  . ARG D  2 85  ? -11.014 -8.576  50.564  1.00 13.77  ? 85  ARG D CB  1 
ATOM   6868  C CG  . ARG D  2 85  ? -10.042 -9.610  50.005  1.00 16.44  ? 85  ARG D CG  1 
ATOM   6869  C CD  . ARG D  2 85  ? -9.566  -10.586 51.067  1.00 19.39  ? 85  ARG D CD  1 
ATOM   6870  N NE  . ARG D  2 85  ? -8.529  -10.004 51.915  1.00 21.54  ? 85  ARG D NE  1 
ATOM   6871  C CZ  . ARG D  2 85  ? -8.615  -9.876  53.235  1.00 22.02  ? 85  ARG D CZ  1 
ATOM   6872  N NH1 . ARG D  2 85  ? -9.693  -10.304 53.886  1.00 21.32  ? 85  ARG D NH1 1 
ATOM   6873  N NH2 . ARG D  2 85  ? -7.609  -9.330  53.906  1.00 20.34  ? 85  ARG D NH2 1 
ATOM   6874  N N   . ASP D  2 86  ? -13.191 -8.762  48.344  1.00 13.53  ? 86  ASP D N   1 
ATOM   6875  C CA  . ASP D  2 86  ? -13.788 -9.450  47.199  1.00 14.23  ? 86  ASP D CA  1 
ATOM   6876  C C   . ASP D  2 86  ? -14.013 -8.505  46.021  1.00 13.35  ? 86  ASP D C   1 
ATOM   6877  O O   . ASP D  2 86  ? -13.800 -8.883  44.870  1.00 13.49  ? 86  ASP D O   1 
ATOM   6878  C CB  . ASP D  2 86  ? -15.093 -10.154 47.595  1.00 14.88  ? 86  ASP D CB  1 
ATOM   6879  C CG  . ASP D  2 86  ? -14.859 -11.368 48.497  1.00 20.74  ? 86  ASP D CG  1 
ATOM   6880  O OD1 . ASP D  2 86  ? -13.860 -12.095 48.293  1.00 25.42  ? 86  ASP D OD1 1 
ATOM   6881  O OD2 . ASP D  2 86  ? -15.681 -11.602 49.411  1.00 27.03  ? 86  ASP D OD2 1 
ATOM   6882  N N   . ALA D  2 87  ? -14.431 -7.277  46.320  1.00 12.31  ? 87  ALA D N   1 
ATOM   6883  C CA  . ALA D  2 87  ? -14.616 -6.252  45.301  1.00 11.45  ? 87  ALA D CA  1 
ATOM   6884  C C   . ALA D  2 87  ? -13.283 -5.869  44.653  1.00 11.11  ? 87  ALA D C   1 
ATOM   6885  O O   . ALA D  2 87  ? -13.224 -5.620  43.445  1.00 10.74  ? 87  ALA D O   1 
ATOM   6886  C CB  . ALA D  2 87  ? -15.308 -5.034  45.891  1.00 11.30  ? 87  ALA D CB  1 
ATOM   6887  N N   . MET D  2 88  ? -12.219 -5.841  45.457  1.00 10.55  ? 88  MET D N   1 
ATOM   6888  C CA  . MET D  2 88  ? -10.860 -5.617  44.952  1.00 10.08  ? 88  MET D CA  1 
ATOM   6889  C C   . MET D  2 88  ? -10.448 -6.740  44.013  1.00 9.33   ? 88  MET D C   1 
ATOM   6890  O O   . MET D  2 88  ? -9.915  -6.500  42.928  1.00 10.13  ? 88  MET D O   1 
ATOM   6891  C CB  . MET D  2 88  ? -9.853  -5.512  46.101  1.00 10.32  ? 88  MET D CB  1 
ATOM   6892  C CG  . MET D  2 88  ? -10.093 -4.368  47.070  1.00 14.34  ? 88  MET D CG  1 
ATOM   6893  S SD  . MET D  2 88  ? -9.624  -2.759  46.419  1.00 25.26  ? 88  MET D SD  1 
ATOM   6894  C CE  . MET D  2 88  ? -10.887 -2.461  45.193  1.00 21.42  ? 88  MET D CE  1 
ATOM   6895  N N   . THR D  2 89  ? -10.705 -7.968  44.449  1.00 8.58   ? 89  THR D N   1 
ATOM   6896  C CA  . THR D  2 89  ? -10.414 -9.159  43.670  1.00 7.51   ? 89  THR D CA  1 
ATOM   6897  C C   . THR D  2 89  ? -11.115 -9.095  42.315  1.00 7.70   ? 89  THR D C   1 
ATOM   6898  O O   . THR D  2 89  ? -10.506 -9.393  41.292  1.00 8.53   ? 89  THR D O   1 
ATOM   6899  C CB  . THR D  2 89  ? -10.811 -10.431 44.456  1.00 7.21   ? 89  THR D CB  1 
ATOM   6900  O OG1 . THR D  2 89  ? -10.052 -10.486 45.668  1.00 5.02   ? 89  THR D OG1 1 
ATOM   6901  C CG2 . THR D  2 89  ? -10.551 -11.687 43.653  1.00 4.21   ? 89  THR D CG2 1 
ATOM   6902  N N   . GLU D  2 90  ? -12.377 -8.675  42.312  1.00 8.22   ? 90  GLU D N   1 
ATOM   6903  C CA  . GLU D  2 90  ? -13.158 -8.566  41.078  1.00 8.98   ? 90  GLU D CA  1 
ATOM   6904  C C   . GLU D  2 90  ? -12.593 -7.533  40.116  1.00 9.19   ? 90  GLU D C   1 
ATOM   6905  O O   . GLU D  2 90  ? -12.543 -7.770  38.905  1.00 9.69   ? 90  GLU D O   1 
ATOM   6906  C CB  . GLU D  2 90  ? -14.621 -8.255  41.379  1.00 8.74   ? 90  GLU D CB  1 
ATOM   6907  C CG  . GLU D  2 90  ? -15.348 -9.362  42.125  1.00 10.82  ? 90  GLU D CG  1 
ATOM   6908  C CD  . GLU D  2 90  ? -15.587 -10.603 41.283  1.00 13.95  ? 90  GLU D CD  1 
ATOM   6909  O OE1 . GLU D  2 90  ? -15.283 -10.582 40.069  1.00 15.78  ? 90  GLU D OE1 1 
ATOM   6910  O OE2 . GLU D  2 90  ? -16.095 -11.600 41.841  1.00 13.27  ? 90  GLU D OE2 1 
ATOM   6911  N N   . ILE D  2 91  ? -12.168 -6.394  40.659  1.00 9.06   ? 91  ILE D N   1 
ATOM   6912  C CA  . ILE D  2 91  ? -11.530 -5.348  39.860  1.00 9.56   ? 91  ILE D CA  1 
ATOM   6913  C C   . ILE D  2 91  ? -10.195 -5.833  39.296  1.00 9.78   ? 91  ILE D C   1 
ATOM   6914  O O   . ILE D  2 91  ? -9.925  -5.678  38.104  1.00 10.05  ? 91  ILE D O   1 
ATOM   6915  C CB  . ILE D  2 91  ? -11.358 -4.027  40.658  1.00 9.34   ? 91  ILE D CB  1 
ATOM   6916  C CG1 . ILE D  2 91  ? -12.726 -3.379  40.894  1.00 8.71   ? 91  ILE D CG1 1 
ATOM   6917  C CG2 . ILE D  2 91  ? -10.456 -3.045  39.907  1.00 9.41   ? 91  ILE D CG2 1 
ATOM   6918  C CD1 . ILE D  2 91  ? -12.749 -2.356  42.011  1.00 11.04  ? 91  ILE D CD1 1 
ATOM   6919  N N   . TRP D  2 92  ? -9.375  -6.438  40.150  1.00 10.44  ? 92  TRP D N   1 
ATOM   6920  C CA  . TRP D  2 92  ? -8.066  -6.917  39.716  1.00 10.81  ? 92  TRP D CA  1 
ATOM   6921  C C   . TRP D  2 92  ? -8.147  -8.057  38.718  1.00 10.92  ? 92  TRP D C   1 
ATOM   6922  O O   . TRP D  2 92  ? -7.343  -8.115  37.790  1.00 10.91  ? 92  TRP D O   1 
ATOM   6923  C CB  . TRP D  2 92  ? -7.171  -7.272  40.901  1.00 10.60  ? 92  TRP D CB  1 
ATOM   6924  C CG  . TRP D  2 92  ? -6.456  -6.073  41.425  1.00 10.01  ? 92  TRP D CG  1 
ATOM   6925  C CD1 . TRP D  2 92  ? -6.615  -5.493  42.646  1.00 8.88   ? 92  TRP D CD1 1 
ATOM   6926  C CD2 . TRP D  2 92  ? -5.490  -5.280  40.725  1.00 8.23   ? 92  TRP D CD2 1 
ATOM   6927  N NE1 . TRP D  2 92  ? -5.795  -4.398  42.760  1.00 10.34  ? 92  TRP D NE1 1 
ATOM   6928  C CE2 . TRP D  2 92  ? -5.095  -4.242  41.594  1.00 7.81   ? 92  TRP D CE2 1 
ATOM   6929  C CE3 . TRP D  2 92  ? -4.910  -5.354  39.451  1.00 7.38   ? 92  TRP D CE3 1 
ATOM   6930  C CZ2 . TRP D  2 92  ? -4.149  -3.279  41.231  1.00 9.00   ? 92  TRP D CZ2 1 
ATOM   6931  C CZ3 . TRP D  2 92  ? -3.968  -4.394  39.089  1.00 8.48   ? 92  TRP D CZ3 1 
ATOM   6932  C CH2 . TRP D  2 92  ? -3.600  -3.371  39.976  1.00 8.52   ? 92  TRP D CH2 1 
ATOM   6933  N N   . SER D  2 93  ? -9.124  -8.943  38.900  1.00 11.06  ? 93  SER D N   1 
ATOM   6934  C CA  . SER D  2 93  ? -9.372  -10.022 37.947  1.00 11.36  ? 93  SER D CA  1 
ATOM   6935  C C   . SER D  2 93  ? -9.771  -9.445  36.589  1.00 11.61  ? 93  SER D C   1 
ATOM   6936  O O   . SER D  2 93  ? -9.257  -9.873  35.551  1.00 11.64  ? 93  SER D O   1 
ATOM   6937  C CB  . SER D  2 93  ? -10.450 -10.976 38.466  1.00 11.34  ? 93  SER D CB  1 
ATOM   6938  O OG  . SER D  2 93  ? -10.062 -11.564 39.699  1.00 12.34  ? 93  SER D OG  1 
ATOM   6939  N N   . TYR D  2 94  ? -10.673 -8.462  36.613  1.00 11.69  ? 94  TYR D N   1 
ATOM   6940  C CA  . TYR D  2 94  ? -11.079 -7.737  35.416  1.00 11.48  ? 94  TYR D CA  1 
ATOM   6941  C C   . TYR D  2 94  ? -9.870  -7.083  34.743  1.00 12.79  ? 94  TYR D C   1 
ATOM   6942  O O   . TYR D  2 94  ? -9.647  -7.268  33.544  1.00 13.08  ? 94  TYR D O   1 
ATOM   6943  C CB  . TYR D  2 94  ? -12.142 -6.684  35.754  1.00 11.18  ? 94  TYR D CB  1 
ATOM   6944  C CG  . TYR D  2 94  ? -12.447 -5.724  34.620  1.00 8.77   ? 94  TYR D CG  1 
ATOM   6945  C CD1 . TYR D  2 94  ? -13.483 -5.983  33.722  1.00 7.15   ? 94  TYR D CD1 1 
ATOM   6946  C CD2 . TYR D  2 94  ? -11.698 -4.559  34.446  1.00 8.98   ? 94  TYR D CD2 1 
ATOM   6947  C CE1 . TYR D  2 94  ? -13.763 -5.115  32.674  1.00 7.06   ? 94  TYR D CE1 1 
ATOM   6948  C CE2 . TYR D  2 94  ? -11.967 -3.680  33.403  1.00 12.16  ? 94  TYR D CE2 1 
ATOM   6949  C CZ  . TYR D  2 94  ? -13.004 -3.964  32.522  1.00 12.83  ? 94  TYR D CZ  1 
ATOM   6950  O OH  . TYR D  2 94  ? -13.276 -3.097  31.488  1.00 15.68  ? 94  TYR D OH  1 
ATOM   6951  N N   . ASN D  2 95  ? -9.091  -6.328  35.518  1.00 13.24  ? 95  ASN D N   1 
ATOM   6952  C CA  . ASN D  2 95  ? -7.914  -5.643  34.990  1.00 13.81  ? 95  ASN D CA  1 
ATOM   6953  C C   . ASN D  2 95  ? -6.910  -6.590  34.358  1.00 14.26  ? 95  ASN D C   1 
ATOM   6954  O O   . ASN D  2 95  ? -6.365  -6.304  33.292  1.00 15.25  ? 95  ASN D O   1 
ATOM   6955  C CB  . ASN D  2 95  ? -7.230  -4.806  36.073  1.00 14.06  ? 95  ASN D CB  1 
ATOM   6956  C CG  . ASN D  2 95  ? -7.917  -3.470  36.305  1.00 16.11  ? 95  ASN D CG  1 
ATOM   6957  O OD1 . ASN D  2 95  ? -8.786  -3.053  35.534  1.00 17.28  ? 95  ASN D OD1 1 
ATOM   6958  N ND2 . ASN D  2 95  ? -7.524  -2.790  37.374  1.00 20.48  ? 95  ASN D ND2 1 
ATOM   6959  N N   . ALA D  2 96  ? -6.677  -7.721  35.018  1.00 14.13  ? 96  ALA D N   1 
ATOM   6960  C CA  . ALA D  2 96  ? -5.693  -8.686  34.560  1.00 13.78  ? 96  ALA D CA  1 
ATOM   6961  C C   . ALA D  2 96  ? -6.104  -9.305  33.230  1.00 14.27  ? 96  ALA D C   1 
ATOM   6962  O O   . ALA D  2 96  ? -5.299  -9.378  32.302  1.00 14.22  ? 96  ALA D O   1 
ATOM   6963  C CB  . ALA D  2 96  ? -5.475  -9.757  35.612  1.00 13.89  ? 96  ALA D CB  1 
ATOM   6964  N N   . GLU D  2 97  ? -7.360  -9.733  33.136  1.00 14.80  ? 97  GLU D N   1 
ATOM   6965  C CA  . GLU D  2 97  ? -7.849  -10.380 31.923  1.00 15.41  ? 97  GLU D CA  1 
ATOM   6966  C C   . GLU D  2 97  ? -7.874  -9.422  30.734  1.00 15.37  ? 97  GLU D C   1 
ATOM   6967  O O   . GLU D  2 97  ? -7.495  -9.808  29.620  1.00 15.96  ? 97  GLU D O   1 
ATOM   6968  C CB  . GLU D  2 97  ? -9.226  -11.016 32.138  1.00 15.26  ? 97  GLU D CB  1 
ATOM   6969  C CG  . GLU D  2 97  ? -9.633  -11.948 31.004  1.00 18.13  ? 97  GLU D CG  1 
ATOM   6970  C CD  . GLU D  2 97  ? -10.653 -12.988 31.417  1.00 23.65  ? 97  GLU D CD  1 
ATOM   6971  O OE1 . GLU D  2 97  ? -10.883 -13.164 32.631  1.00 25.94  ? 97  GLU D OE1 1 
ATOM   6972  O OE2 . GLU D  2 97  ? -11.222 -13.643 30.520  1.00 25.97  ? 97  GLU D OE2 1 
ATOM   6973  N N   . LEU D  2 98  ? -8.309  -8.184  30.978  1.00 14.45  ? 98  LEU D N   1 
ATOM   6974  C CA  . LEU D  2 98  ? -8.334  -7.152  29.946  1.00 14.22  ? 98  LEU D CA  1 
ATOM   6975  C C   . LEU D  2 98  ? -6.922  -6.834  29.474  1.00 14.49  ? 98  LEU D C   1 
ATOM   6976  O O   . LEU D  2 98  ? -6.667  -6.778  28.268  1.00 15.55  ? 98  LEU D O   1 
ATOM   6977  C CB  . LEU D  2 98  ? -9.025  -5.873  30.441  1.00 14.68  ? 98  LEU D CB  1 
ATOM   6978  C CG  . LEU D  2 98  ? -8.998  -4.670  29.484  1.00 14.17  ? 98  LEU D CG  1 
ATOM   6979  C CD1 . LEU D  2 98  ? -9.808  -4.943  28.224  1.00 13.78  ? 98  LEU D CD1 1 
ATOM   6980  C CD2 . LEU D  2 98  ? -9.484  -3.412  30.164  1.00 12.14  ? 98  LEU D CD2 1 
ATOM   6981  N N   . LEU D  2 99  ? -6.015  -6.632  30.429  1.00 13.63  ? 99  LEU D N   1 
ATOM   6982  C CA  . LEU D  2 99  ? -4.615  -6.353  30.128  1.00 12.78  ? 99  LEU D CA  1 
ATOM   6983  C C   . LEU D  2 99  ? -4.044  -7.374  29.152  1.00 12.89  ? 99  LEU D C   1 
ATOM   6984  O O   . LEU D  2 99  ? -3.481  -7.008  28.124  1.00 13.76  ? 99  LEU D O   1 
ATOM   6985  C CB  . LEU D  2 99  ? -3.779  -6.327  31.413  1.00 12.44  ? 99  LEU D CB  1 
ATOM   6986  C CG  . LEU D  2 99  ? -2.258  -6.174  31.292  1.00 9.89   ? 99  LEU D CG  1 
ATOM   6987  C CD1 . LEU D  2 99  ? -1.867  -4.839  30.667  1.00 9.21   ? 99  LEU D CD1 1 
ATOM   6988  C CD2 . LEU D  2 99  ? -1.631  -6.321  32.657  1.00 9.84   ? 99  LEU D CD2 1 
ATOM   6989  N N   . VAL D  2 100 ? -4.200  -8.651  29.478  1.00 12.02  ? 100 VAL D N   1 
ATOM   6990  C CA  . VAL D  2 100 ? -3.671  -9.723  28.650  1.00 12.45  ? 100 VAL D CA  1 
ATOM   6991  C C   . VAL D  2 100 ? -4.332  -9.719  27.271  1.00 13.41  ? 100 VAL D C   1 
ATOM   6992  O O   . VAL D  2 100 ? -3.640  -9.802  26.254  1.00 13.63  ? 100 VAL D O   1 
ATOM   6993  C CB  . VAL D  2 100 ? -3.800  -11.095 29.360  1.00 12.24  ? 100 VAL D CB  1 
ATOM   6994  C CG1 . VAL D  2 100 ? -3.780  -12.240 28.371  1.00 11.72  ? 100 VAL D CG1 1 
ATOM   6995  C CG2 . VAL D  2 100 ? -2.686  -11.257 30.392  1.00 11.80  ? 100 VAL D CG2 1 
ATOM   6996  N N   . ALA D  2 101 ? -5.659  -9.590  27.247  1.00 13.54  ? 101 ALA D N   1 
ATOM   6997  C CA  . ALA D  2 101 ? -6.426  -9.603  26.001  1.00 13.36  ? 101 ALA D CA  1 
ATOM   6998  C C   . ALA D  2 101 ? -6.003  -8.465  25.079  1.00 13.77  ? 101 ALA D C   1 
ATOM   6999  O O   . ALA D  2 101 ? -5.746  -8.676  23.892  1.00 14.12  ? 101 ALA D O   1 
ATOM   7000  C CB  . ALA D  2 101 ? -7.924  -9.532  26.292  1.00 12.56  ? 101 ALA D CB  1 
ATOM   7001  N N   . MET D  2 102 ? -5.925  -7.264  25.643  1.00 13.82  ? 102 MET D N   1 
ATOM   7002  C CA  . MET D  2 102 ? -5.533  -6.075  24.905  1.00 14.86  ? 102 MET D CA  1 
ATOM   7003  C C   . MET D  2 102 ? -4.094  -6.175  24.398  1.00 14.57  ? 102 MET D C   1 
ATOM   7004  O O   . MET D  2 102 ? -3.824  -5.900  23.226  1.00 14.56  ? 102 MET D O   1 
ATOM   7005  C CB  . MET D  2 102 ? -5.696  -4.842  25.793  1.00 15.92  ? 102 MET D CB  1 
ATOM   7006  C CG  . MET D  2 102 ? -5.430  -3.519  25.100  1.00 19.93  ? 102 MET D CG  1 
ATOM   7007  S SD  . MET D  2 102 ? -4.928  -2.266  26.289  1.00 28.05  ? 102 MET D SD  1 
ATOM   7008  C CE  . MET D  2 102 ? -3.196  -2.686  26.506  1.00 28.77  ? 102 MET D CE  1 
ATOM   7009  N N   . GLU D  2 103 ? -3.183  -6.573  25.283  1.00 14.06  ? 103 GLU D N   1 
ATOM   7010  C CA  . GLU D  2 103 ? -1.767  -6.685  24.943  1.00 14.36  ? 103 GLU D CA  1 
ATOM   7011  C C   . GLU D  2 103 ? -1.537  -7.693  23.823  1.00 13.99  ? 103 GLU D C   1 
ATOM   7012  O O   . GLU D  2 103 ? -0.780  -7.423  22.889  1.00 14.02  ? 103 GLU D O   1 
ATOM   7013  C CB  . GLU D  2 103 ? -0.935  -7.063  26.175  1.00 14.96  ? 103 GLU D CB  1 
ATOM   7014  C CG  . GLU D  2 103 ? -0.801  -5.961  27.228  1.00 16.15  ? 103 GLU D CG  1 
ATOM   7015  C CD  . GLU D  2 103 ? 0.302   -4.954  26.932  1.00 19.01  ? 103 GLU D CD  1 
ATOM   7016  O OE1 . GLU D  2 103 ? 0.828   -4.927  25.799  1.00 21.62  ? 103 GLU D OE1 1 
ATOM   7017  O OE2 . GLU D  2 103 ? 0.649   -4.180  27.847  1.00 19.12  ? 103 GLU D OE2 1 
ATOM   7018  N N   . ASN D  2 104 ? -2.199  -8.846  23.928  1.00 13.46  ? 104 ASN D N   1 
ATOM   7019  C CA  . ASN D  2 104 ? -2.121  -9.902  22.920  1.00 12.47  ? 104 ASN D CA  1 
ATOM   7020  C C   . ASN D  2 104 ? -2.610  -9.466  21.545  1.00 12.51  ? 104 ASN D C   1 
ATOM   7021  O O   . ASN D  2 104 ? -1.983  -9.784  20.534  1.00 13.32  ? 104 ASN D O   1 
ATOM   7022  C CB  . ASN D  2 104 ? -2.896  -11.136 23.383  1.00 12.65  ? 104 ASN D CB  1 
ATOM   7023  C CG  . ASN D  2 104 ? -2.227  -11.839 24.546  1.00 10.10  ? 104 ASN D CG  1 
ATOM   7024  O OD1 . ASN D  2 104 ? -1.131  -11.468 24.958  1.00 10.58  ? 104 ASN D OD1 1 
ATOM   7025  N ND2 . ASN D  2 104 ? -2.884  -12.857 25.081  1.00 6.24   ? 104 ASN D ND2 1 
ATOM   7026  N N   . GLN D  2 105 ? -3.728  -8.744  21.516  1.00 11.71  ? 105 GLN D N   1 
ATOM   7027  C CA  . GLN D  2 105 ? -4.254  -8.168  20.283  1.00 11.15  ? 105 GLN D CA  1 
ATOM   7028  C C   . GLN D  2 105 ? -3.200  -7.274  19.639  1.00 10.99  ? 105 GLN D C   1 
ATOM   7029  O O   . GLN D  2 105 ? -2.988  -7.322  18.425  1.00 10.90  ? 105 GLN D O   1 
ATOM   7030  C CB  . GLN D  2 105 ? -5.514  -7.349  20.575  1.00 11.08  ? 105 GLN D CB  1 
ATOM   7031  C CG  . GLN D  2 105 ? -6.309  -6.937  19.338  1.00 10.65  ? 105 GLN D CG  1 
ATOM   7032  C CD  . GLN D  2 105 ? -7.301  -7.999  18.878  1.00 9.98   ? 105 GLN D CD  1 
ATOM   7033  O OE1 . GLN D  2 105 ? -7.805  -8.785  19.676  1.00 10.41  ? 105 GLN D OE1 1 
ATOM   7034  N NE2 . GLN D  2 105 ? -7.598  -8.009  17.584  1.00 11.32  ? 105 GLN D NE2 1 
ATOM   7035  N N   . HIS D  2 106 ? -2.540  -6.469  20.468  1.00 10.93  ? 106 HIS D N   1 
ATOM   7036  C CA  . HIS D  2 106 ? -1.516  -5.543  20.000  1.00 10.65  ? 106 HIS D CA  1 
ATOM   7037  C C   . HIS D  2 106 ? -0.273  -6.278  19.526  1.00 10.53  ? 106 HIS D C   1 
ATOM   7038  O O   . HIS D  2 106 ? 0.293   -5.917  18.504  1.00 11.57  ? 106 HIS D O   1 
ATOM   7039  C CB  . HIS D  2 106 ? -1.158  -4.529  21.087  1.00 10.53  ? 106 HIS D CB  1 
ATOM   7040  C CG  . HIS D  2 106 ? -0.067  -3.584  20.693  1.00 10.57  ? 106 HIS D CG  1 
ATOM   7041  N ND1 . HIS D  2 106 ? 1.232   -3.726  21.128  1.00 6.40   ? 106 HIS D ND1 1 
ATOM   7042  C CD2 . HIS D  2 106 ? -0.079  -2.490  19.895  1.00 9.25   ? 106 HIS D CD2 1 
ATOM   7043  C CE1 . HIS D  2 106 ? 1.973   -2.757  20.620  1.00 7.79   ? 106 HIS D CE1 1 
ATOM   7044  N NE2 . HIS D  2 106 ? 1.201   -1.992  19.869  1.00 8.57   ? 106 HIS D NE2 1 
ATOM   7045  N N   . THR D  2 107 ? 0.128   -7.312  20.265  1.00 10.63  ? 107 THR D N   1 
ATOM   7046  C CA  . THR D  2 107 ? 1.310   -8.121  19.943  1.00 10.07  ? 107 THR D CA  1 
ATOM   7047  C C   . THR D  2 107 ? 1.205   -8.776  18.562  1.00 10.59  ? 107 THR D C   1 
ATOM   7048  O O   . THR D  2 107 ? 2.122   -8.670  17.738  1.00 10.38  ? 107 THR D O   1 
ATOM   7049  C CB  . THR D  2 107 ? 1.557   -9.197  21.023  1.00 9.29   ? 107 THR D CB  1 
ATOM   7050  O OG1 . THR D  2 107 ? 1.747   -8.561  22.290  1.00 7.88   ? 107 THR D OG1 1 
ATOM   7051  C CG2 . THR D  2 107 ? 2.796   -10.033 20.704  1.00 10.62  ? 107 THR D CG2 1 
ATOM   7052  N N   . ILE D  2 108 ? 0.085   -9.447  18.321  1.00 10.75  ? 108 ILE D N   1 
ATOM   7053  C CA  . ILE D  2 108 ? -0.175  -10.083 17.039  1.00 11.37  ? 108 ILE D CA  1 
ATOM   7054  C C   . ILE D  2 108 ? -0.136  -9.048  15.906  1.00 12.52  ? 108 ILE D C   1 
ATOM   7055  O O   . ILE D  2 108 ? 0.526   -9.266  14.888  1.00 13.49  ? 108 ILE D O   1 
ATOM   7056  C CB  . ILE D  2 108 ? -1.513  -10.851 17.073  1.00 11.42  ? 108 ILE D CB  1 
ATOM   7057  C CG1 . ILE D  2 108 ? -1.410  -12.026 18.049  1.00 9.78   ? 108 ILE D CG1 1 
ATOM   7058  C CG2 . ILE D  2 108 ? -1.905  -11.340 15.684  1.00 11.57  ? 108 ILE D CG2 1 
ATOM   7059  C CD1 . ILE D  2 108 ? -2.745  -12.612 18.449  1.00 11.53  ? 108 ILE D CD1 1 
ATOM   7060  N N   . ASP D  2 109 ? -0.815  -7.917  16.100  1.00 12.56  ? 109 ASP D N   1 
ATOM   7061  C CA  . ASP D  2 109 ? -0.817  -6.827  15.116  1.00 12.85  ? 109 ASP D CA  1 
ATOM   7062  C C   . ASP D  2 109 ? 0.567   -6.219  14.909  1.00 13.24  ? 109 ASP D C   1 
ATOM   7063  O O   . ASP D  2 109 ? 0.917   -5.811  13.796  1.00 12.88  ? 109 ASP D O   1 
ATOM   7064  C CB  . ASP D  2 109 ? -1.817  -5.739  15.515  1.00 12.89  ? 109 ASP D CB  1 
ATOM   7065  C CG  . ASP D  2 109 ? -3.260  -6.190  15.369  1.00 12.79  ? 109 ASP D CG  1 
ATOM   7066  O OD1 . ASP D  2 109 ? -4.128  -5.653  16.085  1.00 17.00  ? 109 ASP D OD1 1 
ATOM   7067  O OD2 . ASP D  2 109 ? -3.533  -7.084  14.541  1.00 13.93  ? 109 ASP D OD2 1 
ATOM   7068  N N   . LEU D  2 110 ? 1.338   -6.167  15.993  1.00 13.49  ? 110 LEU D N   1 
ATOM   7069  C CA  . LEU D  2 110 ? 2.714   -5.683  15.985  1.00 13.90  ? 110 LEU D CA  1 
ATOM   7070  C C   . LEU D  2 110 ? 3.602   -6.589  15.132  1.00 13.75  ? 110 LEU D C   1 
ATOM   7071  O O   . LEU D  2 110 ? 4.428   -6.108  14.357  1.00 14.02  ? 110 LEU D O   1 
ATOM   7072  C CB  . LEU D  2 110 ? 3.226   -5.609  17.428  1.00 14.37  ? 110 LEU D CB  1 
ATOM   7073  C CG  . LEU D  2 110 ? 4.665   -5.303  17.855  1.00 18.24  ? 110 LEU D CG  1 
ATOM   7074  C CD1 . LEU D  2 110 ? 4.638   -4.934  19.326  1.00 21.49  ? 110 LEU D CD1 1 
ATOM   7075  C CD2 . LEU D  2 110 ? 5.624   -6.470  17.628  1.00 18.12  ? 110 LEU D CD2 1 
ATOM   7076  N N   . ALA D  2 111 ? 3.426   -7.901  15.280  1.00 13.25  ? 111 ALA D N   1 
ATOM   7077  C CA  . ALA D  2 111 ? 4.212   -8.876  14.527  1.00 12.47  ? 111 ALA D CA  1 
ATOM   7078  C C   . ALA D  2 111 ? 3.860   -8.832  13.044  1.00 11.97  ? 111 ALA D C   1 
ATOM   7079  O O   . ALA D  2 111 ? 4.737   -8.949  12.185  1.00 11.17  ? 111 ALA D O   1 
ATOM   7080  C CB  . ALA D  2 111 ? 3.995   -10.267 15.083  1.00 12.49  ? 111 ALA D CB  1 
ATOM   7081  N N   . ASP D  2 112 ? 2.565   -8.664  12.773  1.00 11.85  ? 112 ASP D N   1 
ATOM   7082  C CA  . ASP D  2 112 ? 2.017   -8.535  11.429  1.00 11.83  ? 112 ASP D CA  1 
ATOM   7083  C C   . ASP D  2 112 ? 2.543   -7.265  10.763  1.00 12.13  ? 112 ASP D C   1 
ATOM   7084  O O   . ASP D  2 112 ? 2.883   -7.266  9.577   1.00 12.56  ? 112 ASP D O   1 
ATOM   7085  C CB  . ASP D  2 112 ? 0.489   -8.492  11.510  1.00 11.79  ? 112 ASP D CB  1 
ATOM   7086  C CG  . ASP D  2 112 ? -0.187  -8.735  10.173  1.00 11.42  ? 112 ASP D CG  1 
ATOM   7087  O OD1 . ASP D  2 112 ? 0.499   -9.087  9.192   1.00 7.35   ? 112 ASP D OD1 1 
ATOM   7088  O OD2 . ASP D  2 112 ? -1.425  -8.581  10.109  1.00 14.62  ? 112 ASP D OD2 1 
ATOM   7089  N N   . SER D  2 113 ? 2.610   -6.190  11.547  1.00 11.85  ? 113 SER D N   1 
ATOM   7090  C CA  . SER D  2 113 ? 3.157   -4.912  11.106  1.00 11.10  ? 113 SER D CA  1 
ATOM   7091  C C   . SER D  2 113 ? 4.599   -5.042  10.623  1.00 10.53  ? 113 SER D C   1 
ATOM   7092  O O   . SER D  2 113 ? 4.942   -4.551  9.545   1.00 10.18  ? 113 SER D O   1 
ATOM   7093  C CB  . SER D  2 113 ? 3.072   -3.899  12.245  1.00 11.04  ? 113 SER D CB  1 
ATOM   7094  O OG  . SER D  2 113 ? 3.886   -2.770  12.001  1.00 13.02  ? 113 SER D OG  1 
ATOM   7095  N N   . GLU D  2 114 ? 5.429   -5.716  11.419  1.00 9.98   ? 114 GLU D N   1 
ATOM   7096  C CA  . GLU D  2 114 ? 6.842   -5.900  11.088  1.00 10.20  ? 114 GLU D CA  1 
ATOM   7097  C C   . GLU D  2 114 ? 7.027   -6.735  9.826   1.00 10.11  ? 114 GLU D C   1 
ATOM   7098  O O   . GLU D  2 114 ? 7.998   -6.542  9.091   1.00 10.24  ? 114 GLU D O   1 
ATOM   7099  C CB  . GLU D  2 114 ? 7.621   -6.521  12.253  1.00 9.83   ? 114 GLU D CB  1 
ATOM   7100  C CG  . GLU D  2 114 ? 7.743   -5.643  13.501  1.00 12.30  ? 114 GLU D CG  1 
ATOM   7101  C CD  . GLU D  2 114 ? 8.433   -4.298  13.259  1.00 17.16  ? 114 GLU D CD  1 
ATOM   7102  O OE1 . GLU D  2 114 ? 9.343   -4.214  12.400  1.00 16.13  ? 114 GLU D OE1 1 
ATOM   7103  O OE2 . GLU D  2 114 ? 8.060   -3.319  13.945  1.00 16.55  ? 114 GLU D OE2 1 
ATOM   7104  N N   . MET D  2 115 ? 6.100   -7.660  9.586   1.00 9.72   ? 115 MET D N   1 
ATOM   7105  C CA  . MET D  2 115 ? 6.101   -8.453  8.361   1.00 9.75   ? 115 MET D CA  1 
ATOM   7106  C C   . MET D  2 115 ? 5.757   -7.559  7.174   1.00 10.07  ? 115 MET D C   1 
ATOM   7107  O O   . MET D  2 115 ? 6.441   -7.591  6.147   1.00 8.95   ? 115 MET D O   1 
ATOM   7108  C CB  . MET D  2 115 ? 5.110   -9.616  8.468   1.00 9.68   ? 115 MET D CB  1 
ATOM   7109  C CG  . MET D  2 115 ? 5.056   -10.530 7.250   1.00 7.65   ? 115 MET D CG  1 
ATOM   7110  S SD  . MET D  2 115 ? 6.447   -11.662 7.135   1.00 8.63   ? 115 MET D SD  1 
ATOM   7111  C CE  . MET D  2 115 ? 7.516   -10.808 5.984   1.00 7.71   ? 115 MET D CE  1 
ATOM   7112  N N   . SER D  2 116 ? 4.708   -6.753  7.335   1.00 10.61  ? 116 SER D N   1 
ATOM   7113  C CA  . SER D  2 116 ? 4.273   -5.826  6.296   1.00 11.78  ? 116 SER D CA  1 
ATOM   7114  C C   . SER D  2 116 ? 5.362   -4.811  5.946   1.00 12.24  ? 116 SER D C   1 
ATOM   7115  O O   . SER D  2 116 ? 5.597   -4.536  4.770   1.00 12.78  ? 116 SER D O   1 
ATOM   7116  C CB  . SER D  2 116 ? 2.988   -5.107  6.711   1.00 12.06  ? 116 SER D CB  1 
ATOM   7117  O OG  . SER D  2 116 ? 2.497   -4.301  5.654   1.00 13.11  ? 116 SER D OG  1 
ATOM   7118  N N   . LYS D  2 117 ? 6.026   -4.267  6.964   1.00 12.09  ? 117 LYS D N   1 
ATOM   7119  C CA  . LYS D  2 117 ? 7.109   -3.310  6.755   1.00 12.04  ? 117 LYS D CA  1 
ATOM   7120  C C   . LYS D  2 117 ? 8.236   -3.907  5.921   1.00 12.24  ? 117 LYS D C   1 
ATOM   7121  O O   . LYS D  2 117 ? 8.724   -3.271  4.984   1.00 12.94  ? 117 LYS D O   1 
ATOM   7122  C CB  . LYS D  2 117 ? 7.687   -2.839  8.086   1.00 12.33  ? 117 LYS D CB  1 
ATOM   7123  C CG  . LYS D  2 117 ? 6.771   -1.994  8.945   1.00 11.59  ? 117 LYS D CG  1 
ATOM   7124  C CD  . LYS D  2 117 ? 7.573   -1.434  10.103  1.00 9.18   ? 117 LYS D CD  1 
ATOM   7125  C CE  . LYS D  2 117 ? 6.797   -1.444  11.389  1.00 3.41   ? 117 LYS D CE  1 
ATOM   7126  N NZ  . LYS D  2 117 ? 7.603   -0.813  12.461  1.00 4.96   ? 117 LYS D NZ  1 
ATOM   7127  N N   . LEU D  2 118 ? 8.648   -5.123  6.276   1.00 12.04  ? 118 LEU D N   1 
ATOM   7128  C CA  . LEU D  2 118 ? 9.744   -5.815  5.596   1.00 12.10  ? 118 LEU D CA  1 
ATOM   7129  C C   . LEU D  2 118 ? 9.403   -6.106  4.137   1.00 12.67  ? 118 LEU D C   1 
ATOM   7130  O O   . LEU D  2 118 ? 10.207  -5.844  3.242   1.00 13.57  ? 118 LEU D O   1 
ATOM   7131  C CB  . LEU D  2 118 ? 10.106  -7.110  6.334   1.00 11.51  ? 118 LEU D CB  1 
ATOM   7132  C CG  . LEU D  2 118 ? 11.148  -8.045  5.712   1.00 10.79  ? 118 LEU D CG  1 
ATOM   7133  C CD1 . LEU D  2 118 ? 12.520  -7.388  5.625   1.00 11.34  ? 118 LEU D CD1 1 
ATOM   7134  C CD2 . LEU D  2 118 ? 11.219  -9.361  6.479   1.00 5.71   ? 118 LEU D CD2 1 
ATOM   7135  N N   . TYR D  2 119 ? 8.207   -6.644  3.913   1.00 12.49  ? 119 TYR D N   1 
ATOM   7136  C CA  . TYR D  2 119 ? 7.692   -6.875  2.571   1.00 11.96  ? 119 TYR D CA  1 
ATOM   7137  C C   . TYR D  2 119 ? 7.744   -5.589  1.747   1.00 11.75  ? 119 TYR D C   1 
ATOM   7138  O O   . TYR D  2 119 ? 8.286   -5.577  0.635   1.00 11.92  ? 119 TYR D O   1 
ATOM   7139  C CB  . TYR D  2 119 ? 6.265   -7.427  2.649   1.00 11.92  ? 119 TYR D CB  1 
ATOM   7140  C CG  . TYR D  2 119 ? 5.602   -7.652  1.311   1.00 11.47  ? 119 TYR D CG  1 
ATOM   7141  C CD1 . TYR D  2 119 ? 5.797   -8.835  0.606   1.00 9.48   ? 119 TYR D CD1 1 
ATOM   7142  C CD2 . TYR D  2 119 ? 4.770   -6.682  0.755   1.00 11.48  ? 119 TYR D CD2 1 
ATOM   7143  C CE1 . TYR D  2 119 ? 5.188   -9.043  -0.623  1.00 11.08  ? 119 TYR D CE1 1 
ATOM   7144  C CE2 . TYR D  2 119 ? 4.157   -6.880  -0.475  1.00 11.14  ? 119 TYR D CE2 1 
ATOM   7145  C CZ  . TYR D  2 119 ? 4.369   -8.062  -1.157  1.00 11.42  ? 119 TYR D CZ  1 
ATOM   7146  O OH  . TYR D  2 119 ? 3.758   -8.265  -2.370  1.00 12.44  ? 119 TYR D OH  1 
ATOM   7147  N N   . GLU D  2 120 ? 7.202   -4.510  2.310   1.00 11.42  ? 120 GLU D N   1 
ATOM   7148  C CA  . GLU D  2 120 ? 7.173   -3.210  1.639   1.00 11.98  ? 120 GLU D CA  1 
ATOM   7149  C C   . GLU D  2 120 ? 8.574   -2.659  1.370   1.00 12.01  ? 120 GLU D C   1 
ATOM   7150  O O   . GLU D  2 120 ? 8.786   -1.986  0.364   1.00 11.99  ? 120 GLU D O   1 
ATOM   7151  C CB  . GLU D  2 120 ? 6.337   -2.188  2.427   1.00 11.94  ? 120 GLU D CB  1 
ATOM   7152  C CG  . GLU D  2 120 ? 4.821   -2.462  2.470   1.00 14.27  ? 120 GLU D CG  1 
ATOM   7153  C CD  . GLU D  2 120 ? 4.137   -2.429  1.102   1.00 19.73  ? 120 GLU D CD  1 
ATOM   7154  O OE1 . GLU D  2 120 ? 4.509   -1.589  0.251   1.00 23.23  ? 120 GLU D OE1 1 
ATOM   7155  O OE2 . GLU D  2 120 ? 3.210   -3.243  0.886   1.00 18.67  ? 120 GLU D OE2 1 
ATOM   7156  N N   . ARG D  2 121 ? 9.522   -2.944  2.263   1.00 12.57  ? 121 ARG D N   1 
ATOM   7157  C CA  . ARG D  2 121 ? 10.907  -2.508  2.073   1.00 12.74  ? 121 ARG D CA  1 
ATOM   7158  C C   . ARG D  2 121 ? 11.487  -3.121  0.806   1.00 12.30  ? 121 ARG D C   1 
ATOM   7159  O O   . ARG D  2 121 ? 12.054  -2.414  -0.031  1.00 12.22  ? 121 ARG D O   1 
ATOM   7160  C CB  . ARG D  2 121 ? 11.782  -2.864  3.279   1.00 13.60  ? 121 ARG D CB  1 
ATOM   7161  C CG  . ARG D  2 121 ? 13.254  -2.495  3.086   1.00 16.58  ? 121 ARG D CG  1 
ATOM   7162  C CD  . ARG D  2 121 ? 14.089  -2.722  4.335   1.00 26.00  ? 121 ARG D CD  1 
ATOM   7163  N NE  . ARG D  2 121 ? 14.369  -4.137  4.602   1.00 32.30  ? 121 ARG D NE  1 
ATOM   7164  C CZ  . ARG D  2 121 ? 15.242  -4.886  3.926   1.00 33.80  ? 121 ARG D CZ  1 
ATOM   7165  N NH1 . ARG D  2 121 ? 15.929  -4.382  2.902   1.00 34.32  ? 121 ARG D NH1 1 
ATOM   7166  N NH2 . ARG D  2 121 ? 15.420  -6.156  4.268   1.00 34.26  ? 121 ARG D NH2 1 
ATOM   7167  N N   . VAL D  2 122 ? 11.327  -4.436  0.677   1.00 11.71  ? 122 VAL D N   1 
ATOM   7168  C CA  . VAL D  2 122 ? 11.782  -5.174  -0.497  1.00 11.43  ? 122 VAL D CA  1 
ATOM   7169  C C   . VAL D  2 122 ? 11.149  -4.628  -1.778  1.00 11.54  ? 122 VAL D C   1 
ATOM   7170  O O   . VAL D  2 122 ? 11.846  -4.426  -2.771  1.00 11.93  ? 122 VAL D O   1 
ATOM   7171  C CB  . VAL D  2 122 ? 11.497  -6.689  -0.357  1.00 11.63  ? 122 VAL D CB  1 
ATOM   7172  C CG1 . VAL D  2 122 ? 11.906  -7.443  -1.615  1.00 9.66   ? 122 VAL D CG1 1 
ATOM   7173  C CG2 . VAL D  2 122 ? 12.224  -7.253  0.855   1.00 11.11  ? 122 VAL D CG2 1 
ATOM   7174  N N   . LYS D  2 123 ? 9.839   -4.383  -1.749  1.00 11.36  ? 123 LYS D N   1 
ATOM   7175  C CA  . LYS D  2 123 ? 9.128   -3.856  -2.919  1.00 11.96  ? 123 LYS D CA  1 
ATOM   7176  C C   . LYS D  2 123 ? 9.743   -2.545  -3.420  1.00 12.38  ? 123 LYS D C   1 
ATOM   7177  O O   . LYS D  2 123 ? 10.040  -2.407  -4.610  1.00 13.16  ? 123 LYS D O   1 
ATOM   7178  C CB  . LYS D  2 123 ? 7.634   -3.674  -2.619  1.00 12.08  ? 123 LYS D CB  1 
ATOM   7179  C CG  . LYS D  2 123 ? 6.834   -3.143  -3.796  1.00 13.34  ? 123 LYS D CG  1 
ATOM   7180  C CD  . LYS D  2 123 ? 5.381   -2.897  -3.443  1.00 16.99  ? 123 LYS D CD  1 
ATOM   7181  C CE  . LYS D  2 123 ? 4.724   -1.994  -4.483  1.00 20.36  ? 123 LYS D CE  1 
ATOM   7182  N NZ  . LYS D  2 123 ? 3.273   -1.789  -4.221  1.00 19.73  ? 123 LYS D NZ  1 
ATOM   7183  N N   . LYS D  2 124 ? 9.938   -1.599  -2.502  1.00 11.99  ? 124 LYS D N   1 
ATOM   7184  C CA  . LYS D  2 124 ? 10.535  -0.301  -2.815  1.00 11.41  ? 124 LYS D CA  1 
ATOM   7185  C C   . LYS D  2 124 ? 11.989  -0.422  -3.251  1.00 11.07  ? 124 LYS D C   1 
ATOM   7186  O O   . LYS D  2 124 ? 12.506  0.431   -3.977  1.00 10.63  ? 124 LYS D O   1 
ATOM   7187  C CB  . LYS D  2 124 ? 10.431  0.634   -1.607  1.00 11.59  ? 124 LYS D CB  1 
ATOM   7188  C CG  . LYS D  2 124 ? 9.213   1.554   -1.639  1.00 10.96  ? 124 LYS D CG  1 
ATOM   7189  C CD  . LYS D  2 124 ? 8.926   2.169   -0.280  1.00 9.87   ? 124 LYS D CD  1 
ATOM   7190  C CE  . LYS D  2 124 ? 7.931   1.319   0.501   1.00 12.71  ? 124 LYS D CE  1 
ATOM   7191  N NZ  . LYS D  2 124 ? 7.696   1.869   1.859   1.00 13.66  ? 124 LYS D NZ  1 
ATOM   7192  N N   . GLN D  2 125 ? 12.638  -1.485  -2.791  1.00 11.05  ? 125 GLN D N   1 
ATOM   7193  C CA  . GLN D  2 125 ? 14.027  -1.756  -3.115  1.00 11.09  ? 125 GLN D CA  1 
ATOM   7194  C C   . GLN D  2 125 ? 14.134  -2.259  -4.550  1.00 10.96  ? 125 GLN D C   1 
ATOM   7195  O O   . GLN D  2 125 ? 14.981  -1.795  -5.314  1.00 11.52  ? 125 GLN D O   1 
ATOM   7196  C CB  . GLN D  2 125 ? 14.581  -2.796  -2.146  1.00 11.11  ? 125 GLN D CB  1 
ATOM   7197  C CG  . GLN D  2 125 ? 16.086  -2.879  -2.091  1.00 15.50  ? 125 GLN D CG  1 
ATOM   7198  C CD  . GLN D  2 125 ? 16.579  -4.015  -1.213  1.00 20.26  ? 125 GLN D CD  1 
ATOM   7199  O OE1 . GLN D  2 125 ? 17.686  -4.521  -1.406  1.00 25.64  ? 125 GLN D OE1 1 
ATOM   7200  N NE2 . GLN D  2 125 ? 15.761  -4.423  -0.242  1.00 17.63  ? 125 GLN D NE2 1 
ATOM   7201  N N   . LEU D  2 126 ? 13.248  -3.188  -4.909  1.00 10.20  ? 126 LEU D N   1 
ATOM   7202  C CA  . LEU D  2 126 ? 13.277  -3.846  -6.212  1.00 9.25   ? 126 LEU D CA  1 
ATOM   7203  C C   . LEU D  2 126 ? 12.781  -2.979  -7.371  1.00 9.51   ? 126 LEU D C   1 
ATOM   7204  O O   . LEU D  2 126 ? 12.990  -3.332  -8.535  1.00 9.89   ? 126 LEU D O   1 
ATOM   7205  C CB  . LEU D  2 126 ? 12.507  -5.170  -6.163  1.00 9.30   ? 126 LEU D CB  1 
ATOM   7206  C CG  . LEU D  2 126 ? 13.117  -6.317  -5.343  1.00 7.25   ? 126 LEU D CG  1 
ATOM   7207  C CD1 . LEU D  2 126 ? 12.209  -7.533  -5.372  1.00 3.03   ? 126 LEU D CD1 1 
ATOM   7208  C CD2 . LEU D  2 126 ? 14.517  -6.686  -5.828  1.00 4.61   ? 126 LEU D CD2 1 
ATOM   7209  N N   . ARG D  2 127 ? 12.129  -1.858  -7.054  1.00 9.01   ? 127 ARG D N   1 
ATOM   7210  C CA  . ARG D  2 127 ? 11.684  -0.877  -8.058  1.00 8.65   ? 127 ARG D CA  1 
ATOM   7211  C C   . ARG D  2 127 ? 10.869  -1.512  -9.192  1.00 8.71   ? 127 ARG D C   1 
ATOM   7212  O O   . ARG D  2 127 ? 9.850   -2.150  -8.935  1.00 9.25   ? 127 ARG D O   1 
ATOM   7213  C CB  . ARG D  2 127 ? 12.877  -0.084  -8.620  1.00 8.78   ? 127 ARG D CB  1 
ATOM   7214  C CG  . ARG D  2 127 ? 13.571  0.831   -7.625  1.00 7.07   ? 127 ARG D CG  1 
ATOM   7215  C CD  . ARG D  2 127 ? 12.782  2.101   -7.400  1.00 5.60   ? 127 ARG D CD  1 
ATOM   7216  N NE  . ARG D  2 127 ? 12.879  3.025   -8.528  1.00 5.76   ? 127 ARG D NE  1 
ATOM   7217  C CZ  . ARG D  2 127 ? 13.624  4.129   -8.539  1.00 4.39   ? 127 ARG D CZ  1 
ATOM   7218  N NH1 . ARG D  2 127 ? 14.350  4.463   -7.478  1.00 3.96   ? 127 ARG D NH1 1 
ATOM   7219  N NH2 . ARG D  2 127 ? 13.641  4.904   -9.615  1.00 2.00   ? 127 ARG D NH2 1 
ATOM   7220  N N   . GLU D  2 128 ? 11.335  -1.346  -10.432 1.00 8.71   ? 128 GLU D N   1 
ATOM   7221  C CA  . GLU D  2 128 ? 10.645  -1.857  -11.622 1.00 9.23   ? 128 GLU D CA  1 
ATOM   7222  C C   . GLU D  2 128 ? 11.248  -3.165  -12.138 1.00 9.69   ? 128 GLU D C   1 
ATOM   7223  O O   . GLU D  2 128 ? 10.978  -3.579  -13.267 1.00 10.02  ? 128 GLU D O   1 
ATOM   7224  C CB  . GLU D  2 128 ? 10.649  -0.811  -12.750 1.00 9.15   ? 128 GLU D CB  1 
ATOM   7225  C CG  . GLU D  2 128 ? 10.015  0.539   -12.409 1.00 9.76   ? 128 GLU D CG  1 
ATOM   7226  C CD  . GLU D  2 128 ? 8.525   0.458   -12.099 1.00 10.15  ? 128 GLU D CD  1 
ATOM   7227  O OE1 . GLU D  2 128 ? 7.805   -0.328  -12.748 1.00 9.90   ? 128 GLU D OE1 1 
ATOM   7228  O OE2 . GLU D  2 128 ? 8.069   1.197   -11.204 1.00 13.24  ? 128 GLU D OE2 1 
ATOM   7229  N N   . ASN D  2 129 ? 12.062  -3.814  -11.311 1.00 10.04  ? 129 ASN D N   1 
ATOM   7230  C CA  . ASN D  2 129 ? 12.725  -5.055  -11.700 1.00 10.12  ? 129 ASN D CA  1 
ATOM   7231  C C   . ASN D  2 129 ? 11.936  -6.301  -11.300 1.00 10.75  ? 129 ASN D C   1 
ATOM   7232  O O   . ASN D  2 129 ? 12.326  -7.427  -11.623 1.00 11.26  ? 129 ASN D O   1 
ATOM   7233  C CB  . ASN D  2 129 ? 14.137  -5.112  -11.101 1.00 10.06  ? 129 ASN D CB  1 
ATOM   7234  C CG  . ASN D  2 129 ? 15.041  -3.987  -11.595 1.00 9.93   ? 129 ASN D CG  1 
ATOM   7235  O OD1 . ASN D  2 129 ? 14.704  -3.254  -12.525 1.00 10.18  ? 129 ASN D OD1 1 
ATOM   7236  N ND2 . ASN D  2 129 ? 16.203  -3.854  -10.969 1.00 10.53  ? 129 ASN D ND2 1 
ATOM   7237  N N   . ALA D  2 130 ? 10.827  -6.098  -10.595 1.00 11.54  ? 130 ALA D N   1 
ATOM   7238  C CA  . ALA D  2 130 ? 10.060  -7.209  -10.039 1.00 12.10  ? 130 ALA D CA  1 
ATOM   7239  C C   . ALA D  2 130 ? 8.570   -6.911  -9.938  1.00 12.47  ? 130 ALA D C   1 
ATOM   7240  O O   . ALA D  2 130 ? 8.162   -5.759  -9.781  1.00 11.90  ? 130 ALA D O   1 
ATOM   7241  C CB  . ALA D  2 130 ? 10.609  -7.597  -8.671  1.00 12.06  ? 130 ALA D CB  1 
ATOM   7242  N N   . GLU D  2 131 ? 7.768   -7.965  -10.033 1.00 13.34  ? 131 GLU D N   1 
ATOM   7243  C CA  . GLU D  2 131 ? 6.333   -7.872  -9.808  1.00 14.09  ? 131 GLU D CA  1 
ATOM   7244  C C   . GLU D  2 131 ? 5.953   -8.764  -8.643  1.00 13.98  ? 131 GLU D C   1 
ATOM   7245  O O   . GLU D  2 131 ? 6.457   -9.882  -8.518  1.00 14.26  ? 131 GLU D O   1 
ATOM   7246  C CB  . GLU D  2 131 ? 5.556   -8.279  -11.060 1.00 14.34  ? 131 GLU D CB  1 
ATOM   7247  C CG  . GLU D  2 131 ? 5.579   -7.240  -12.174 1.00 15.67  ? 131 GLU D CG  1 
ATOM   7248  C CD  . GLU D  2 131 ? 4.902   -7.718  -13.448 1.00 16.96  ? 131 GLU D CD  1 
ATOM   7249  O OE1 . GLU D  2 131 ? 4.081   -8.654  -13.383 1.00 19.43  ? 131 GLU D OE1 1 
ATOM   7250  O OE2 . GLU D  2 131 ? 5.183   -7.149  -14.522 1.00 15.50  ? 131 GLU D OE2 1 
ATOM   7251  N N   . GLU D  2 132 ? 5.075   -8.261  -7.783  1.00 14.37  ? 132 GLU D N   1 
ATOM   7252  C CA  . GLU D  2 132 ? 4.570   -9.045  -6.661  1.00 15.22  ? 132 GLU D CA  1 
ATOM   7253  C C   . GLU D  2 132 ? 3.456   -9.977  -7.130  1.00 14.90  ? 132 GLU D C   1 
ATOM   7254  O O   . GLU D  2 132 ? 2.575   -9.572  -7.890  1.00 15.56  ? 132 GLU D O   1 
ATOM   7255  C CB  . GLU D  2 132 ? 4.119   -8.141  -5.505  1.00 15.22  ? 132 GLU D CB  1 
ATOM   7256  C CG  . GLU D  2 132 ? 3.144   -7.035  -5.882  1.00 19.45  ? 132 GLU D CG  1 
ATOM   7257  C CD  . GLU D  2 132 ? 3.012   -5.964  -4.812  1.00 22.72  ? 132 GLU D CD  1 
ATOM   7258  O OE1 . GLU D  2 132 ? 3.299   -4.795  -5.131  1.00 27.11  ? 132 GLU D OE1 1 
ATOM   7259  O OE2 . GLU D  2 132 ? 2.622   -6.278  -3.663  1.00 21.30  ? 132 GLU D OE2 1 
ATOM   7260  N N   . ASP D  2 133 ? 3.519   -11.231 -6.692  1.00 14.64  ? 133 ASP D N   1 
ATOM   7261  C CA  . ASP D  2 133 ? 2.592   -12.264 -7.157  1.00 14.69  ? 133 ASP D CA  1 
ATOM   7262  C C   . ASP D  2 133 ? 1.342   -12.411 -6.285  1.00 14.47  ? 133 ASP D C   1 
ATOM   7263  O O   . ASP D  2 133 ? 0.423   -13.153 -6.632  1.00 15.40  ? 133 ASP D O   1 
ATOM   7264  C CB  . ASP D  2 133 ? 3.318   -13.612 -7.309  1.00 14.94  ? 133 ASP D CB  1 
ATOM   7265  C CG  . ASP D  2 133 ? 3.550   -14.324 -5.980  1.00 15.71  ? 133 ASP D CG  1 
ATOM   7266  O OD1 . ASP D  2 133 ? 3.565   -13.666 -4.915  1.00 16.14  ? 133 ASP D OD1 1 
ATOM   7267  O OD2 . ASP D  2 133 ? 3.725   -15.562 -6.006  1.00 16.79  ? 133 ASP D OD2 1 
ATOM   7268  N N   . GLY D  2 134 ? 1.322   -11.722 -5.147  1.00 13.66  ? 134 GLY D N   1 
ATOM   7269  C CA  . GLY D  2 134 ? 0.161   -11.730 -4.268  1.00 12.90  ? 134 GLY D CA  1 
ATOM   7270  C C   . GLY D  2 134 ? 0.180   -12.787 -3.184  1.00 12.95  ? 134 GLY D C   1 
ATOM   7271  O O   . GLY D  2 134 ? -0.744  -12.855 -2.372  1.00 13.70  ? 134 GLY D O   1 
ATOM   7272  N N   . THR D  2 135 ? 1.220   -13.618 -3.170  1.00 12.44  ? 135 THR D N   1 
ATOM   7273  C CA  . THR D  2 135 ? 1.396   -14.625 -2.117  1.00 11.78  ? 135 THR D CA  1 
ATOM   7274  C C   . THR D  2 135 ? 2.559   -14.255 -1.196  1.00 11.72  ? 135 THR D C   1 
ATOM   7275  O O   . THR D  2 135 ? 2.967   -15.050 -0.347  1.00 11.78  ? 135 THR D O   1 
ATOM   7276  C CB  . THR D  2 135 ? 1.649   -16.038 -2.692  1.00 11.82  ? 135 THR D CB  1 
ATOM   7277  O OG1 . THR D  2 135 ? 2.934   -16.078 -3.330  1.00 13.18  ? 135 THR D OG1 1 
ATOM   7278  C CG2 . THR D  2 135 ? 0.558   -16.439 -3.688  1.00 10.42  ? 135 THR D CG2 1 
ATOM   7279  N N   . GLY D  2 136 ? 3.086   -13.045 -1.377  1.00 11.57  ? 136 GLY D N   1 
ATOM   7280  C CA  . GLY D  2 136 ? 4.221   -12.556 -0.604  1.00 10.36  ? 136 GLY D CA  1 
ATOM   7281  C C   . GLY D  2 136 ? 5.537   -12.673 -1.348  1.00 10.54  ? 136 GLY D C   1 
ATOM   7282  O O   . GLY D  2 136 ? 6.580   -12.278 -0.830  1.00 11.67  ? 136 GLY D O   1 
ATOM   7283  N N   . CYS D  2 137 ? 5.493   -13.221 -2.561  1.00 9.69   ? 137 CYS D N   1 
ATOM   7284  C CA  . CYS D  2 137 ? 6.693   -13.407 -3.382  1.00 8.72   ? 137 CYS D CA  1 
ATOM   7285  C C   . CYS D  2 137 ? 6.905   -12.265 -4.374  1.00 9.04   ? 137 CYS D C   1 
ATOM   7286  O O   . CYS D  2 137 ? 5.961   -11.571 -4.746  1.00 9.29   ? 137 CYS D O   1 
ATOM   7287  C CB  . CYS D  2 137 ? 6.625   -14.731 -4.150  1.00 8.44   ? 137 CYS D CB  1 
ATOM   7288  S SG  . CYS D  2 137 ? 6.600   -16.209 -3.131  0.60 3.28   ? 137 CYS D SG  1 
ATOM   7289  N N   . PHE D  2 138 ? 8.153   -12.087 -4.799  1.00 9.25   ? 138 PHE D N   1 
ATOM   7290  C CA  . PHE D  2 138 ? 8.497   -11.133 -5.847  1.00 9.53   ? 138 PHE D CA  1 
ATOM   7291  C C   . PHE D  2 138 ? 9.094   -11.855 -7.047  1.00 10.54  ? 138 PHE D C   1 
ATOM   7292  O O   . PHE D  2 138 ? 10.188  -12.422 -6.962  1.00 10.39  ? 138 PHE D O   1 
ATOM   7293  C CB  . PHE D  2 138 ? 9.487   -10.090 -5.327  1.00 8.67   ? 138 PHE D CB  1 
ATOM   7294  C CG  . PHE D  2 138 ? 8.891   -9.125  -4.355  1.00 9.17   ? 138 PHE D CG  1 
ATOM   7295  C CD1 . PHE D  2 138 ? 8.991   -9.347  -2.986  1.00 9.12   ? 138 PHE D CD1 1 
ATOM   7296  C CD2 . PHE D  2 138 ? 8.223   -7.993  -4.806  1.00 7.91   ? 138 PHE D CD2 1 
ATOM   7297  C CE1 . PHE D  2 138 ? 8.435   -8.456  -2.080  1.00 7.95   ? 138 PHE D CE1 1 
ATOM   7298  C CE2 . PHE D  2 138 ? 7.667   -7.098  -3.910  1.00 7.39   ? 138 PHE D CE2 1 
ATOM   7299  C CZ  . PHE D  2 138 ? 7.774   -7.330  -2.541  1.00 9.17   ? 138 PHE D CZ  1 
ATOM   7300  N N   . GLU D  2 139 ? 8.370   -11.840 -8.161  1.00 11.54  ? 139 GLU D N   1 
ATOM   7301  C CA  . GLU D  2 139 ? 8.895   -12.378 -9.407  1.00 12.93  ? 139 GLU D CA  1 
ATOM   7302  C C   . GLU D  2 139 ? 9.942   -11.430 -9.977  1.00 12.71  ? 139 GLU D C   1 
ATOM   7303  O O   . GLU D  2 139 ? 9.615   -10.341 -10.452 1.00 13.33  ? 139 GLU D O   1 
ATOM   7304  C CB  . GLU D  2 139 ? 7.770   -12.636 -10.410 1.00 13.11  ? 139 GLU D CB  1 
ATOM   7305  C CG  . GLU D  2 139 ? 7.100   -13.992 -10.220 1.00 19.45  ? 139 GLU D CG  1 
ATOM   7306  C CD  . GLU D  2 139 ? 5.727   -14.078 -10.870 1.00 26.92  ? 139 GLU D CD  1 
ATOM   7307  O OE1 . GLU D  2 139 ? 4.804   -14.614 -10.220 1.00 29.31  ? 139 GLU D OE1 1 
ATOM   7308  O OE2 . GLU D  2 139 ? 5.567   -13.614 -12.023 1.00 29.13  ? 139 GLU D OE2 1 
ATOM   7309  N N   . ILE D  2 140 ? 11.205  -11.838 -9.888  1.00 12.51  ? 140 ILE D N   1 
ATOM   7310  C CA  . ILE D  2 140 ? 12.302  -11.057 -10.445 1.00 12.65  ? 140 ILE D CA  1 
ATOM   7311  C C   . ILE D  2 140 ? 12.315  -11.272 -11.953 1.00 12.82  ? 140 ILE D C   1 
ATOM   7312  O O   . ILE D  2 140 ? 12.300  -12.412 -12.427 1.00 12.43  ? 140 ILE D O   1 
ATOM   7313  C CB  . ILE D  2 140 ? 13.672  -11.429 -9.807  1.00 12.62  ? 140 ILE D CB  1 
ATOM   7314  C CG1 . ILE D  2 140 ? 13.736  -10.976 -8.350  1.00 12.42  ? 140 ILE D CG1 1 
ATOM   7315  C CG2 . ILE D  2 140 ? 14.822  -10.784 -10.544 1.00 12.93  ? 140 ILE D CG2 1 
ATOM   7316  C CD1 . ILE D  2 140 ? 13.725  -12.112 -7.373  1.00 12.97  ? 140 ILE D CD1 1 
ATOM   7317  N N   . PHE D  2 141 ? 12.325  -10.172 -12.699 1.00 13.62  ? 141 PHE D N   1 
ATOM   7318  C CA  . PHE D  2 141 ? 12.262  -10.239 -14.158 1.00 14.55  ? 141 PHE D CA  1 
ATOM   7319  C C   . PHE D  2 141 ? 13.632  -10.204 -14.837 1.00 15.34  ? 141 PHE D C   1 
ATOM   7320  O O   . PHE D  2 141 ? 13.741  -9.934  -16.033 1.00 16.40  ? 141 PHE D O   1 
ATOM   7321  C CB  . PHE D  2 141 ? 11.309  -9.176  -14.717 1.00 14.60  ? 141 PHE D CB  1 
ATOM   7322  C CG  . PHE D  2 141 ? 9.869   -9.617  -14.751 1.00 14.25  ? 141 PHE D CG  1 
ATOM   7323  C CD1 . PHE D  2 141 ? 9.022   -9.362  -13.676 1.00 12.77  ? 141 PHE D CD1 1 
ATOM   7324  C CD2 . PHE D  2 141 ? 9.363   -10.298 -15.859 1.00 12.59  ? 141 PHE D CD2 1 
ATOM   7325  C CE1 . PHE D  2 141 ? 7.686   -9.772  -13.707 1.00 11.96  ? 141 PHE D CE1 1 
ATOM   7326  C CE2 . PHE D  2 141 ? 8.032   -10.714 -15.898 1.00 11.92  ? 141 PHE D CE2 1 
ATOM   7327  C CZ  . PHE D  2 141 ? 7.192   -10.449 -14.819 1.00 11.90  ? 141 PHE D CZ  1 
ATOM   7328  N N   . HIS D  2 142 ? 14.674  -10.468 -14.057 1.00 15.76  ? 142 HIS D N   1 
ATOM   7329  C CA  . HIS D  2 142 ? 16.013  -10.680 -14.583 1.00 15.80  ? 142 HIS D CA  1 
ATOM   7330  C C   . HIS D  2 142 ? 16.584  -11.932 -13.932 1.00 16.70  ? 142 HIS D C   1 
ATOM   7331  O O   . HIS D  2 142 ? 15.888  -12.610 -13.172 1.00 16.57  ? 142 HIS D O   1 
ATOM   7332  C CB  . HIS D  2 142 ? 16.909  -9.455  -14.341 1.00 15.93  ? 142 HIS D CB  1 
ATOM   7333  C CG  . HIS D  2 142 ? 17.120  -9.119  -12.896 1.00 14.52  ? 142 HIS D CG  1 
ATOM   7334  N ND1 . HIS D  2 142 ? 18.036  -9.778  -12.104 1.00 13.20  ? 142 HIS D ND1 1 
ATOM   7335  C CD2 . HIS D  2 142 ? 16.549  -8.178  -12.108 1.00 14.86  ? 142 HIS D CD2 1 
ATOM   7336  C CE1 . HIS D  2 142 ? 18.013  -9.264  -10.887 1.00 11.85  ? 142 HIS D CE1 1 
ATOM   7337  N NE2 . HIS D  2 142 ? 17.120  -8.290  -10.863 1.00 13.49  ? 142 HIS D NE2 1 
ATOM   7338  N N   . LYS D  2 143 ? 17.837  -12.252 -14.238 1.00 17.55  ? 143 LYS D N   1 
ATOM   7339  C CA  . LYS D  2 143 ? 18.496  -13.364 -13.570 1.00 18.19  ? 143 LYS D CA  1 
ATOM   7340  C C   . LYS D  2 143 ? 19.257  -12.869 -12.346 1.00 17.41  ? 143 LYS D C   1 
ATOM   7341  O O   . LYS D  2 143 ? 20.049  -11.930 -12.429 1.00 17.30  ? 143 LYS D O   1 
ATOM   7342  C CB  . LYS D  2 143 ? 19.381  -14.154 -14.536 1.00 18.94  ? 143 LYS D CB  1 
ATOM   7343  C CG  . LYS D  2 143 ? 18.565  -14.923 -15.572 1.00 22.77  ? 143 LYS D CG  1 
ATOM   7344  C CD  . LYS D  2 143 ? 19.399  -15.929 -16.345 1.00 28.17  ? 143 LYS D CD  1 
ATOM   7345  C CE  . LYS D  2 143 ? 18.541  -16.638 -17.386 1.00 29.83  ? 143 LYS D CE  1 
ATOM   7346  N NZ  . LYS D  2 143 ? 19.330  -17.621 -18.178 1.00 32.99  ? 143 LYS D NZ  1 
ATOM   7347  N N   . CYS D  2 144 ? 18.982  -13.499 -11.209 1.00 16.90  ? 144 CYS D N   1 
ATOM   7348  C CA  . CYS D  2 144 ? 19.506  -13.063 -9.924  1.00 16.64  ? 144 CYS D CA  1 
ATOM   7349  C C   . CYS D  2 144 ? 20.152  -14.249 -9.205  1.00 16.39  ? 144 CYS D C   1 
ATOM   7350  O O   . CYS D  2 144 ? 19.461  -15.084 -8.609  1.00 16.62  ? 144 CYS D O   1 
ATOM   7351  C CB  . CYS D  2 144 ? 18.369  -12.452 -9.091  1.00 16.73  ? 144 CYS D CB  1 
ATOM   7352  S SG  . CYS D  2 144 ? 18.821  -11.535 -7.592  1.00 16.94  ? 144 CYS D SG  1 
ATOM   7353  N N   . ASP D  2 145 ? 21.480  -14.323 -9.280  1.00 15.47  ? 145 ASP D N   1 
ATOM   7354  C CA  . ASP D  2 145 ? 22.233  -15.414 -8.658  1.00 14.34  ? 145 ASP D CA  1 
ATOM   7355  C C   . ASP D  2 145 ? 22.304  -15.274 -7.131  1.00 14.17  ? 145 ASP D C   1 
ATOM   7356  O O   . ASP D  2 145 ? 21.709  -14.354 -6.564  1.00 13.48  ? 145 ASP D O   1 
ATOM   7357  C CB  . ASP D  2 145 ? 23.629  -15.564 -9.298  1.00 13.96  ? 145 ASP D CB  1 
ATOM   7358  C CG  . ASP D  2 145 ? 24.499  -14.311 -9.167  1.00 12.79  ? 145 ASP D CG  1 
ATOM   7359  O OD1 . ASP D  2 145 ? 24.065  -13.307 -8.568  1.00 11.71  ? 145 ASP D OD1 1 
ATOM   7360  O OD2 . ASP D  2 145 ? 25.640  -14.338 -9.675  1.00 12.68  ? 145 ASP D OD2 1 
ATOM   7361  N N   . ASP D  2 146 ? 23.023  -16.187 -6.478  1.00 14.31  ? 146 ASP D N   1 
ATOM   7362  C CA  . ASP D  2 146 ? 23.128  -16.209 -5.012  1.00 14.40  ? 146 ASP D CA  1 
ATOM   7363  C C   . ASP D  2 146 ? 23.697  -14.922 -4.418  1.00 14.71  ? 146 ASP D C   1 
ATOM   7364  O O   . ASP D  2 146 ? 23.277  -14.501 -3.342  1.00 14.72  ? 146 ASP D O   1 
ATOM   7365  C CB  . ASP D  2 146 ? 23.949  -17.414 -4.537  1.00 14.29  ? 146 ASP D CB  1 
ATOM   7366  C CG  . ASP D  2 146 ? 23.169  -18.725 -4.582  1.00 13.57  ? 146 ASP D CG  1 
ATOM   7367  O OD1 . ASP D  2 146 ? 21.954  -18.719 -4.882  1.00 12.96  ? 146 ASP D OD1 1 
ATOM   7368  O OD2 . ASP D  2 146 ? 23.785  -19.774 -4.307  1.00 12.84  ? 146 ASP D OD2 1 
ATOM   7369  N N   . GLN D  2 147 ? 24.646  -14.304 -5.118  1.00 15.29  ? 147 GLN D N   1 
ATOM   7370  C CA  . GLN D  2 147 ? 25.201  -13.011 -4.705  1.00 15.96  ? 147 GLN D CA  1 
ATOM   7371  C C   . GLN D  2 147 ? 24.187  -11.882 -4.903  1.00 15.82  ? 147 GLN D C   1 
ATOM   7372  O O   . GLN D  2 147 ? 24.099  -10.966 -4.081  1.00 16.06  ? 147 GLN D O   1 
ATOM   7373  C CB  . GLN D  2 147 ? 26.495  -12.698 -5.466  1.00 16.07  ? 147 GLN D CB  1 
ATOM   7374  C CG  . GLN D  2 147 ? 27.728  -13.447 -4.962  1.00 18.38  ? 147 GLN D CG  1 
ATOM   7375  C CD  . GLN D  2 147 ? 28.996  -13.098 -5.736  1.00 22.99  ? 147 GLN D CD  1 
ATOM   7376  O OE1 . GLN D  2 147 ? 28.962  -12.872 -6.949  1.00 24.43  ? 147 GLN D OE1 1 
ATOM   7377  N NE2 . GLN D  2 147 ? 30.125  -13.060 -5.034  1.00 22.50  ? 147 GLN D NE2 1 
ATOM   7378  N N   . CYS D  2 148 ? 23.432  -11.956 -5.999  1.00 15.39  ? 148 CYS D N   1 
ATOM   7379  C CA  . CYS D  2 148 ? 22.381  -10.987 -6.302  1.00 15.06  ? 148 CYS D CA  1 
ATOM   7380  C C   . CYS D  2 148 ? 21.262  -11.085 -5.271  1.00 14.63  ? 148 CYS D C   1 
ATOM   7381  O O   . CYS D  2 148 ? 20.813  -10.072 -4.738  1.00 14.63  ? 148 CYS D O   1 
ATOM   7382  C CB  . CYS D  2 148 ? 21.843  -11.213 -7.717  1.00 15.02  ? 148 CYS D CB  1 
ATOM   7383  S SG  . CYS D  2 148 ? 20.349  -10.295 -8.151  1.00 16.88  ? 148 CYS D SG  1 
ATOM   7384  N N   . MET D  2 149 ? 20.824  -12.311 -4.996  1.00 14.70  ? 149 MET D N   1 
ATOM   7385  C CA  . MET D  2 149 ? 19.831  -12.574 -3.958  1.00 14.58  ? 149 MET D CA  1 
ATOM   7386  C C   . MET D  2 149 ? 20.312  -12.040 -2.614  1.00 14.98  ? 149 MET D C   1 
ATOM   7387  O O   . MET D  2 149 ? 19.555  -11.388 -1.893  1.00 14.95  ? 149 MET D O   1 
ATOM   7388  C CB  . MET D  2 149 ? 19.539  -14.072 -3.857  1.00 14.31  ? 149 MET D CB  1 
ATOM   7389  C CG  . MET D  2 149 ? 18.755  -14.637 -5.026  1.00 14.82  ? 149 MET D CG  1 
ATOM   7390  S SD  . MET D  2 149 ? 17.077  -13.991 -5.114  1.00 17.34  ? 149 MET D SD  1 
ATOM   7391  C CE  . MET D  2 149 ? 16.426  -14.927 -6.497  1.00 12.44  ? 149 MET D CE  1 
ATOM   7392  N N   . GLU D  2 150 ? 21.576  -12.320 -2.293  1.00 15.67  ? 150 GLU D N   1 
ATOM   7393  C CA  . GLU D  2 150 ? 22.238  -11.753 -1.122  1.00 16.32  ? 150 GLU D CA  1 
ATOM   7394  C C   . GLU D  2 150 ? 22.024  -10.238 -1.064  1.00 15.97  ? 150 GLU D C   1 
ATOM   7395  O O   . GLU D  2 150 ? 21.526  -9.722  -0.063  1.00 15.62  ? 150 GLU D O   1 
ATOM   7396  C CB  . GLU D  2 150 ? 23.734  -12.081 -1.147  1.00 17.22  ? 150 GLU D CB  1 
ATOM   7397  C CG  . GLU D  2 150 ? 24.578  -11.364 -0.092  1.00 20.84  ? 150 GLU D CG  1 
ATOM   7398  C CD  . GLU D  2 150 ? 24.784  -12.193 1.160   1.00 23.85  ? 150 GLU D CD  1 
ATOM   7399  O OE1 . GLU D  2 150 ? 25.405  -13.275 1.055   1.00 24.47  ? 150 GLU D OE1 1 
ATOM   7400  O OE2 . GLU D  2 150 ? 24.342  -11.754 2.248   1.00 24.33  ? 150 GLU D OE2 1 
ATOM   7401  N N   . SER D  2 151 ? 22.366  -9.543  -2.152  1.00 15.33  ? 151 SER D N   1 
ATOM   7402  C CA  . SER D  2 151 ? 22.301  -8.077  -2.200  1.00 14.93  ? 151 SER D CA  1 
ATOM   7403  C C   . SER D  2 151 ? 20.898  -7.506  -1.952  1.00 14.59  ? 151 SER D C   1 
ATOM   7404  O O   . SER D  2 151 ? 20.761  -6.346  -1.562  1.00 14.32  ? 151 SER D O   1 
ATOM   7405  C CB  . SER D  2 151 ? 22.896  -7.537  -3.510  1.00 14.79  ? 151 SER D CB  1 
ATOM   7406  O OG  . SER D  2 151 ? 22.008  -7.692  -4.602  1.00 15.03  ? 151 SER D OG  1 
ATOM   7407  N N   . ILE D  2 152 ? 19.868  -8.321  -2.176  1.00 14.74  ? 152 ILE D N   1 
ATOM   7408  C CA  . ILE D  2 152 ? 18.493  -7.941  -1.847  1.00 14.82  ? 152 ILE D CA  1 
ATOM   7409  C C   . ILE D  2 152 ? 18.265  -8.017  -0.334  1.00 15.62  ? 152 ILE D C   1 
ATOM   7410  O O   . ILE D  2 152 ? 17.786  -7.054  0.270   1.00 16.05  ? 152 ILE D O   1 
ATOM   7411  C CB  . ILE D  2 152 ? 17.447  -8.795  -2.605  1.00 14.31  ? 152 ILE D CB  1 
ATOM   7412  C CG1 . ILE D  2 152 ? 17.602  -8.611  -4.117  1.00 14.48  ? 152 ILE D CG1 1 
ATOM   7413  C CG2 . ILE D  2 152 ? 16.035  -8.418  -2.175  1.00 13.78  ? 152 ILE D CG2 1 
ATOM   7414  C CD1 . ILE D  2 152 ? 16.848  -9.627  -4.963  1.00 14.75  ? 152 ILE D CD1 1 
ATOM   7415  N N   . ARG D  2 153 ? 18.619  -9.154  0.268   1.00 16.22  ? 153 ARG D N   1 
ATOM   7416  C CA  . ARG D  2 153 ? 18.510  -9.342  1.720   1.00 16.64  ? 153 ARG D CA  1 
ATOM   7417  C C   . ARG D  2 153 ? 19.406  -8.356  2.457   1.00 17.80  ? 153 ARG D C   1 
ATOM   7418  O O   . ARG D  2 153 ? 18.997  -7.754  3.448   1.00 17.89  ? 153 ARG D O   1 
ATOM   7419  C CB  . ARG D  2 153 ? 18.889  -10.768 2.126   1.00 15.96  ? 153 ARG D CB  1 
ATOM   7420  C CG  . ARG D  2 153 ? 18.134  -11.869 1.399   1.00 16.55  ? 153 ARG D CG  1 
ATOM   7421  C CD  . ARG D  2 153 ? 18.384  -13.233 2.031   1.00 15.94  ? 153 ARG D CD  1 
ATOM   7422  N NE  . ARG D  2 153 ? 19.800  -13.604 2.033   1.00 17.70  ? 153 ARG D NE  1 
ATOM   7423  C CZ  . ARG D  2 153 ? 20.403  -14.296 1.071   1.00 17.42  ? 153 ARG D CZ  1 
ATOM   7424  N NH1 . ARG D  2 153 ? 19.720  -14.708 0.009   1.00 20.18  ? 153 ARG D NH1 1 
ATOM   7425  N NH2 . ARG D  2 153 ? 21.694  -14.575 1.170   1.00 14.89  ? 153 ARG D NH2 1 
ATOM   7426  N N   . ASN D  2 154 ? 20.626  -8.201  1.945   1.00 19.63  ? 154 ASN D N   1 
ATOM   7427  C CA  . ASN D  2 154 ? 21.644  -7.312  2.499   1.00 21.00  ? 154 ASN D CA  1 
ATOM   7428  C C   . ASN D  2 154 ? 21.259  -5.841  2.364   1.00 21.37  ? 154 ASN D C   1 
ATOM   7429  O O   . ASN D  2 154 ? 21.821  -4.985  3.049   1.00 21.59  ? 154 ASN D O   1 
ATOM   7430  C CB  . ASN D  2 154 ? 22.974  -7.552  1.770   1.00 21.85  ? 154 ASN D CB  1 
ATOM   7431  C CG  . ASN D  2 154 ? 24.186  -7.452  2.684   1.00 24.30  ? 154 ASN D CG  1 
ATOM   7432  O OD1 . ASN D  2 154 ? 25.214  -8.083  2.423   1.00 26.02  ? 154 ASN D OD1 1 
ATOM   7433  N ND2 . ASN D  2 154 ? 24.080  -6.663  3.751   1.00 26.70  ? 154 ASN D ND2 1 
ATOM   7434  N N   . ASN D  2 155 ? 20.303  -5.566  1.474   1.00 21.78  ? 155 ASN D N   1 
ATOM   7435  C CA  . ASN D  2 155 ? 19.848  -4.207  1.151   1.00 22.08  ? 155 ASN D CA  1 
ATOM   7436  C C   . ASN D  2 155 ? 20.899  -3.388  0.380   1.00 21.85  ? 155 ASN D C   1 
ATOM   7437  O O   . ASN D  2 155 ? 21.006  -2.168  0.541   1.00 21.91  ? 155 ASN D O   1 
ATOM   7438  C CB  . ASN D  2 155 ? 19.357  -3.474  2.410   1.00 22.30  ? 155 ASN D CB  1 
ATOM   7439  C CG  . ASN D  2 155 ? 18.536  -2.238  2.091   1.00 24.58  ? 155 ASN D CG  1 
ATOM   7440  O OD1 . ASN D  2 155 ? 17.869  -2.164  1.058   1.00 28.63  ? 155 ASN D OD1 1 
ATOM   7441  N ND2 . ASN D  2 155 ? 18.578  -1.259  2.985   1.00 28.18  ? 155 ASN D ND2 1 
ATOM   7442  N N   . THR D  2 156 ? 21.660  -4.077  -0.467  1.00 21.04  ? 156 THR D N   1 
ATOM   7443  C CA  . THR D  2 156 ? 22.695  -3.452  -1.289  1.00 20.68  ? 156 THR D CA  1 
ATOM   7444  C C   . THR D  2 156 ? 22.420  -3.631  -2.787  1.00 20.24  ? 156 THR D C   1 
ATOM   7445  O O   . THR D  2 156 ? 23.296  -3.403  -3.629  1.00 19.99  ? 156 THR D O   1 
ATOM   7446  C CB  . THR D  2 156 ? 24.100  -3.989  -0.934  1.00 21.06  ? 156 THR D CB  1 
ATOM   7447  O OG1 . THR D  2 156 ? 24.033  -5.404  -0.710  1.00 21.42  ? 156 THR D OG1 1 
ATOM   7448  C CG2 . THR D  2 156 ? 24.632  -3.302  0.322   1.00 21.02  ? 156 THR D CG2 1 
ATOM   7449  N N   . TYR D  2 157 ? 21.187  -4.027  -3.100  1.00 19.52  ? 157 TYR D N   1 
ATOM   7450  C CA  . TYR D  2 157 ? 20.723  -4.240  -4.468  1.00 17.86  ? 157 TYR D CA  1 
ATOM   7451  C C   . TYR D  2 157 ? 20.646  -2.926  -5.246  1.00 17.51  ? 157 TYR D C   1 
ATOM   7452  O O   . TYR D  2 157 ? 19.896  -2.016  -4.884  1.00 17.56  ? 157 TYR D O   1 
ATOM   7453  C CB  . TYR D  2 157 ? 19.356  -4.925  -4.424  1.00 17.34  ? 157 TYR D CB  1 
ATOM   7454  C CG  . TYR D  2 157 ? 18.695  -5.201  -5.758  1.00 15.13  ? 157 TYR D CG  1 
ATOM   7455  C CD1 . TYR D  2 157 ? 19.043  -6.317  -6.514  1.00 13.49  ? 157 TYR D CD1 1 
ATOM   7456  C CD2 . TYR D  2 157 ? 17.680  -4.372  -6.239  1.00 13.24  ? 157 TYR D CD2 1 
ATOM   7457  C CE1 . TYR D  2 157 ? 18.416  -6.586  -7.730  1.00 11.52  ? 157 TYR D CE1 1 
ATOM   7458  C CE2 . TYR D  2 157 ? 17.049  -4.631  -7.453  1.00 10.05  ? 157 TYR D CE2 1 
ATOM   7459  C CZ  . TYR D  2 157 ? 17.422  -5.739  -8.191  1.00 10.10  ? 157 TYR D CZ  1 
ATOM   7460  O OH  . TYR D  2 157 ? 16.801  -6.004  -9.390  1.00 9.91   ? 157 TYR D OH  1 
ATOM   7461  N N   . ASP D  2 158 ? 21.445  -2.832  -6.303  1.00 16.89  ? 158 ASP D N   1 
ATOM   7462  C CA  . ASP D  2 158 ? 21.400  -1.693  -7.204  1.00 16.57  ? 158 ASP D CA  1 
ATOM   7463  C C   . ASP D  2 158 ? 20.460  -2.036  -8.357  1.00 16.66  ? 158 ASP D C   1 
ATOM   7464  O O   . ASP D  2 158 ? 20.777  -2.874  -9.205  1.00 16.70  ? 158 ASP D O   1 
ATOM   7465  C CB  . ASP D  2 158 ? 22.808  -1.350  -7.711  1.00 16.24  ? 158 ASP D CB  1 
ATOM   7466  C CG  . ASP D  2 158 ? 22.820  -0.179  -8.689  1.00 16.23  ? 158 ASP D CG  1 
ATOM   7467  O OD1 . ASP D  2 158 ? 21.951  0.716   -8.587  1.00 15.12  ? 158 ASP D OD1 1 
ATOM   7468  O OD2 . ASP D  2 158 ? 23.713  -0.153  -9.562  1.00 15.36  ? 158 ASP D OD2 1 
ATOM   7469  N N   . HIS D  2 159 ? 19.300  -1.387  -8.376  1.00 16.57  ? 159 HIS D N   1 
ATOM   7470  C CA  . HIS D  2 159 ? 18.262  -1.689  -9.357  1.00 15.77  ? 159 HIS D CA  1 
ATOM   7471  C C   . HIS D  2 159 ? 18.625  -1.238  -10.773 1.00 15.87  ? 159 HIS D C   1 
ATOM   7472  O O   . HIS D  2 159 ? 18.095  -1.772  -11.748 1.00 16.17  ? 159 HIS D O   1 
ATOM   7473  C CB  . HIS D  2 159 ? 16.924  -1.086  -8.925  1.00 15.27  ? 159 HIS D CB  1 
ATOM   7474  C CG  . HIS D  2 159 ? 16.830  0.392   -9.142  1.00 14.53  ? 159 HIS D CG  1 
ATOM   7475  N ND1 . HIS D  2 159 ? 16.283  0.943   -10.281 1.00 13.07  ? 159 HIS D ND1 1 
ATOM   7476  C CD2 . HIS D  2 159 ? 17.218  1.434   -8.370  1.00 13.61  ? 159 HIS D CD2 1 
ATOM   7477  C CE1 . HIS D  2 159 ? 16.334  2.260   -10.199 1.00 11.83  ? 159 HIS D CE1 1 
ATOM   7478  N NE2 . HIS D  2 159 ? 16.898  2.584   -9.049  1.00 12.09  ? 159 HIS D NE2 1 
ATOM   7479  N N   . THR D  2 160 ? 19.523  -0.258  -10.872 1.00 15.61  ? 160 THR D N   1 
ATOM   7480  C CA  . THR D  2 160 ? 19.963  0.293   -12.160 1.00 15.60  ? 160 THR D CA  1 
ATOM   7481  C C   . THR D  2 160 ? 20.722  -0.749  -12.979 1.00 15.66  ? 160 THR D C   1 
ATOM   7482  O O   . THR D  2 160 ? 20.620  -0.786  -14.208 1.00 15.52  ? 160 THR D O   1 
ATOM   7483  C CB  . THR D  2 160 ? 20.859  1.537   -11.956 1.00 15.39  ? 160 THR D CB  1 
ATOM   7484  O OG1 . THR D  2 160 ? 20.214  2.443   -11.056 1.00 13.72  ? 160 THR D OG1 1 
ATOM   7485  C CG2 . THR D  2 160 ? 21.123  2.255   -13.282 1.00 17.36  ? 160 THR D CG2 1 
ATOM   7486  N N   . GLN D  2 161 ? 21.474  -1.590  -12.272 1.00 15.66  ? 161 GLN D N   1 
ATOM   7487  C CA  . GLN D  2 161 ? 22.272  -2.665  -12.851 1.00 15.33  ? 161 GLN D CA  1 
ATOM   7488  C C   . GLN D  2 161 ? 21.425  -3.670  -13.638 1.00 14.73  ? 161 GLN D C   1 
ATOM   7489  O O   . GLN D  2 161 ? 21.885  -4.231  -14.634 1.00 14.35  ? 161 GLN D O   1 
ATOM   7490  C CB  . GLN D  2 161 ? 23.023  -3.381  -11.725 1.00 15.67  ? 161 GLN D CB  1 
ATOM   7491  C CG  . GLN D  2 161 ? 24.122  -4.344  -12.161 1.00 18.27  ? 161 GLN D CG  1 
ATOM   7492  C CD  . GLN D  2 161 ? 24.647  -5.201  -11.012 1.00 20.76  ? 161 GLN D CD  1 
ATOM   7493  O OE1 . GLN D  2 161 ? 24.964  -6.375  -11.199 1.00 23.25  ? 161 GLN D OE1 1 
ATOM   7494  N NE2 . GLN D  2 161 ? 24.736  -4.616  -9.819  1.00 20.54  ? 161 GLN D NE2 1 
ATOM   7495  N N   . TYR D  2 162 ? 20.188  -3.880  -13.192 1.00 14.07  ? 162 TYR D N   1 
ATOM   7496  C CA  . TYR D  2 162 ? 19.324  -4.916  -13.759 1.00 13.39  ? 162 TYR D CA  1 
ATOM   7497  C C   . TYR D  2 162 ? 18.070  -4.377  -14.460 1.00 13.18  ? 162 TYR D C   1 
ATOM   7498  O O   . TYR D  2 162 ? 17.251  -5.163  -14.950 1.00 12.68  ? 162 TYR D O   1 
ATOM   7499  C CB  . TYR D  2 162 ? 18.900  -5.898  -12.663 1.00 13.16  ? 162 TYR D CB  1 
ATOM   7500  C CG  . TYR D  2 162 ? 20.037  -6.517  -11.885 1.00 12.34  ? 162 TYR D CG  1 
ATOM   7501  C CD1 . TYR D  2 162 ? 20.756  -7.593  -12.400 1.00 10.81  ? 162 TYR D CD1 1 
ATOM   7502  C CD2 . TYR D  2 162 ? 20.382  -6.037  -10.624 1.00 11.75  ? 162 TYR D CD2 1 
ATOM   7503  C CE1 . TYR D  2 162 ? 21.797  -8.169  -11.683 1.00 10.78  ? 162 TYR D CE1 1 
ATOM   7504  C CE2 . TYR D  2 162 ? 21.421  -6.606  -9.897  1.00 11.25  ? 162 TYR D CE2 1 
ATOM   7505  C CZ  . TYR D  2 162 ? 22.125  -7.670  -10.434 1.00 12.09  ? 162 TYR D CZ  1 
ATOM   7506  O OH  . TYR D  2 162 ? 23.159  -8.236  -9.720  1.00 12.64  ? 162 TYR D OH  1 
ATOM   7507  N N   . ARG D  2 163 ? 17.931  -3.052  -14.518 1.00 12.90  ? 163 ARG D N   1 
ATOM   7508  C CA  . ARG D  2 163 ? 16.684  -2.412  -14.962 1.00 12.76  ? 163 ARG D CA  1 
ATOM   7509  C C   . ARG D  2 163 ? 16.331  -2.670  -16.426 1.00 13.10  ? 163 ARG D C   1 
ATOM   7510  O O   . ARG D  2 163 ? 15.203  -3.060  -16.730 1.00 13.48  ? 163 ARG D O   1 
ATOM   7511  C CB  . ARG D  2 163 ? 16.708  -0.906  -14.677 1.00 12.66  ? 163 ARG D CB  1 
ATOM   7512  C CG  . ARG D  2 163 ? 15.383  -0.191  -14.919 1.00 11.34  ? 163 ARG D CG  1 
ATOM   7513  C CD  . ARG D  2 163 ? 15.503  1.284   -14.582 1.00 11.94  ? 163 ARG D CD  1 
ATOM   7514  N NE  . ARG D  2 163 ? 14.362  2.077   -15.039 1.00 8.61   ? 163 ARG D NE  1 
ATOM   7515  C CZ  . ARG D  2 163 ? 13.372  2.507   -14.260 1.00 8.79   ? 163 ARG D CZ  1 
ATOM   7516  N NH1 . ARG D  2 163 ? 13.353  2.223   -12.962 1.00 7.12   ? 163 ARG D NH1 1 
ATOM   7517  N NH2 . ARG D  2 163 ? 12.392  3.230   -14.786 1.00 7.57   ? 163 ARG D NH2 1 
ATOM   7518  N N   . THR D  2 164 ? 17.290  -2.452  -17.322 1.00 13.24  ? 164 THR D N   1 
ATOM   7519  C CA  . THR D  2 164 ? 17.047  -2.587  -18.757 1.00 13.56  ? 164 THR D CA  1 
ATOM   7520  C C   . THR D  2 164 ? 16.609  -4.005  -19.135 1.00 13.79  ? 164 THR D C   1 
ATOM   7521  O O   . THR D  2 164 ? 15.625  -4.180  -19.858 1.00 14.13  ? 164 THR D O   1 
ATOM   7522  C CB  . THR D  2 164 ? 18.275  -2.147  -19.589 1.00 13.67  ? 164 THR D CB  1 
ATOM   7523  O OG1 . THR D  2 164 ? 18.776  -0.905  -19.078 1.00 13.95  ? 164 THR D OG1 1 
ATOM   7524  C CG2 . THR D  2 164 ? 17.899  -1.966  -21.057 1.00 13.04  ? 164 THR D CG2 1 
ATOM   7525  N N   . GLU D  2 165 ? 17.331  -5.004  -18.628 1.00 13.88  ? 165 GLU D N   1 
ATOM   7526  C CA  . GLU D  2 165 ? 17.009  -6.412  -18.860 1.00 13.90  ? 165 GLU D CA  1 
ATOM   7527  C C   . GLU D  2 165 ? 15.601  -6.765  -18.378 1.00 14.09  ? 165 GLU D C   1 
ATOM   7528  O O   . GLU D  2 165 ? 14.848  -7.438  -19.086 1.00 14.51  ? 165 GLU D O   1 
ATOM   7529  C CB  . GLU D  2 165 ? 18.039  -7.316  -18.172 1.00 13.88  ? 165 GLU D CB  1 
ATOM   7530  C CG  . GLU D  2 165 ? 17.768  -8.816  -18.311 1.00 14.33  ? 165 GLU D CG  1 
ATOM   7531  C CD  . GLU D  2 165 ? 18.557  -9.663  -17.323 1.00 15.70  ? 165 GLU D CD  1 
ATOM   7532  O OE1 . GLU D  2 165 ? 18.288  -10.883 -17.241 1.00 15.38  ? 165 GLU D OE1 1 
ATOM   7533  O OE2 . GLU D  2 165 ? 19.439  -9.115  -16.625 1.00 15.52  ? 165 GLU D OE2 1 
ATOM   7534  N N   . SER D  2 166 ? 15.253  -6.307  -17.178 1.00 13.94  ? 166 SER D N   1 
ATOM   7535  C CA  . SER D  2 166 ? 13.967  -6.651  -16.576 1.00 14.22  ? 166 SER D CA  1 
ATOM   7536  C C   . SER D  2 166 ? 12.778  -5.970  -17.252 1.00 14.10  ? 166 SER D C   1 
ATOM   7537  O O   . SER D  2 166 ? 11.698  -6.556  -17.339 1.00 14.59  ? 166 SER D O   1 
ATOM   7538  C CB  . SER D  2 166 ? 13.972  -6.415  -15.058 1.00 14.22  ? 166 SER D CB  1 
ATOM   7539  O OG  . SER D  2 166 ? 14.670  -5.234  -14.708 1.00 16.04  ? 166 SER D OG  1 
ATOM   7540  N N   . LEU D  2 167 ? 12.981  -4.751  -17.746 1.00 14.07  ? 167 LEU D N   1 
ATOM   7541  C CA  . LEU D  2 167 ? 11.937  -4.040  -18.487 1.00 14.31  ? 167 LEU D CA  1 
ATOM   7542  C C   . LEU D  2 167 ? 11.613  -4.711  -19.820 1.00 15.28  ? 167 LEU D C   1 
ATOM   7543  O O   . LEU D  2 167 ? 10.464  -4.694  -20.265 1.00 16.03  ? 167 LEU D O   1 
ATOM   7544  C CB  . LEU D  2 167 ? 12.322  -2.580  -18.718 1.00 14.11  ? 167 LEU D CB  1 
ATOM   7545  C CG  . LEU D  2 167 ? 12.256  -1.608  -17.537 1.00 13.68  ? 167 LEU D CG  1 
ATOM   7546  C CD1 . LEU D  2 167 ? 12.822  -0.258  -17.943 1.00 14.78  ? 167 LEU D CD1 1 
ATOM   7547  C CD2 . LEU D  2 167 ? 10.838  -1.452  -17.012 1.00 13.73  ? 167 LEU D CD2 1 
ATOM   7548  N N   . GLN D  2 168 ? 12.629  -5.297  -20.451 1.00 16.02  ? 168 GLN D N   1 
ATOM   7549  C CA  . GLN D  2 168 ? 12.447  -6.040  -21.699 1.00 16.82  ? 168 GLN D CA  1 
ATOM   7550  C C   . GLN D  2 168 ? 11.624  -7.311  -21.478 1.00 16.78  ? 168 GLN D C   1 
ATOM   7551  O O   . GLN D  2 168 ? 10.807  -7.684  -22.321 1.00 17.11  ? 168 GLN D O   1 
ATOM   7552  C CB  . GLN D  2 168 ? 13.798  -6.403  -22.324 1.00 17.04  ? 168 GLN D CB  1 
ATOM   7553  C CG  . GLN D  2 168 ? 14.602  -5.223  -22.851 1.00 18.83  ? 168 GLN D CG  1 
ATOM   7554  C CD  . GLN D  2 168 ? 15.980  -5.623  -23.366 1.00 21.24  ? 168 GLN D CD  1 
ATOM   7555  O OE1 . GLN D  2 168 ? 16.541  -6.646  -22.965 1.00 21.72  ? 168 GLN D OE1 1 
ATOM   7556  N NE2 . GLN D  2 168 ? 16.532  -4.808  -24.256 1.00 22.03  ? 168 GLN D NE2 1 
ATOM   7557  N N   . ASN D  2 169 ? 11.854  -7.972  -20.347 1.00 16.36  ? 169 ASN D N   1 
ATOM   7558  C CA  . ASN D  2 169 ? 11.147  -9.203  -20.019 1.00 16.17  ? 169 ASN D CA  1 
ATOM   7559  C C   . ASN D  2 169 ? 9.712   -8.945  -19.581 1.00 16.60  ? 169 ASN D C   1 
ATOM   7560  O O   . ASN D  2 169 ? 8.827   -9.757  -19.845 1.00 16.64  ? 169 ASN D O   1 
ATOM   7561  C CB  . ASN D  2 169 ? 11.896  -9.984  -18.935 1.00 16.27  ? 169 ASN D CB  1 
ATOM   7562  C CG  . ASN D  2 169 ? 13.253  -10.475 -19.399 1.00 14.13  ? 169 ASN D CG  1 
ATOM   7563  O OD1 . ASN D  2 169 ? 13.384  -11.062 -20.470 1.00 17.11  ? 169 ASN D OD1 1 
ATOM   7564  N ND2 . ASN D  2 169 ? 14.270  -10.242 -18.587 1.00 14.17  ? 169 ASN D ND2 1 
ATOM   7565  N N   . ARG D  2 170 ? 9.488   -7.811  -18.919 1.00 17.09  ? 170 ARG D N   1 
ATOM   7566  C CA  . ARG D  2 170 ? 8.154   -7.443  -18.438 1.00 18.01  ? 170 ARG D CA  1 
ATOM   7567  C C   . ARG D  2 170 ? 7.207   -7.043  -19.560 1.00 18.99  ? 170 ARG D C   1 
ATOM   7568  O O   . ARG D  2 170 ? 5.997   -7.247  -19.461 1.00 18.48  ? 170 ARG D O   1 
ATOM   7569  C CB  . ARG D  2 170 ? 8.232   -6.306  -17.417 1.00 17.91  ? 170 ARG D CB  1 
ATOM   7570  C CG  . ARG D  2 170 ? 8.727   -6.734  -16.052 1.00 16.32  ? 170 ARG D CG  1 
ATOM   7571  C CD  . ARG D  2 170 ? 7.943   -6.067  -14.950 1.00 13.10  ? 170 ARG D CD  1 
ATOM   7572  N NE  . ARG D  2 170 ? 8.343   -4.681  -14.740 1.00 11.30  ? 170 ARG D NE  1 
ATOM   7573  C CZ  . ARG D  2 170 ? 7.561   -3.746  -14.207 1.00 11.15  ? 170 ARG D CZ  1 
ATOM   7574  N NH1 . ARG D  2 170 ? 6.316   -4.029  -13.837 1.00 5.98   ? 170 ARG D NH1 1 
ATOM   7575  N NH2 . ARG D  2 170 ? 8.028   -2.517  -14.053 1.00 12.37  ? 170 ARG D NH2 1 
ATOM   7576  N N   . ILE D  2 171 ? 7.772   -6.477  -20.623 1.00 20.77  ? 171 ILE D N   1 
ATOM   7577  C CA  . ILE D  2 171 ? 6.993   -5.933  -21.730 1.00 22.71  ? 171 ILE D CA  1 
ATOM   7578  C C   . ILE D  2 171 ? 6.727   -6.948  -22.850 1.00 24.14  ? 171 ILE D C   1 
ATOM   7579  O O   . ILE D  2 171 ? 5.646   -6.942  -23.443 1.00 24.26  ? 171 ILE D O   1 
ATOM   7580  C CB  . ILE D  2 171 ? 7.636   -4.612  -22.256 1.00 22.66  ? 171 ILE D CB  1 
ATOM   7581  C CG1 . ILE D  2 171 ? 6.996   -3.399  -21.575 1.00 23.79  ? 171 ILE D CG1 1 
ATOM   7582  C CG2 . ILE D  2 171 ? 7.507   -4.467  -23.769 1.00 23.88  ? 171 ILE D CG2 1 
ATOM   7583  C CD1 . ILE D  2 171 ? 7.418   -3.182  -20.123 1.00 25.74  ? 171 ILE D CD1 1 
ATOM   7584  N N   . GLN D  2 172 ? 7.695   -7.826  -23.114 1.00 25.99  ? 172 GLN D N   1 
ATOM   7585  C CA  . GLN D  2 172 ? 7.623   -8.750  -24.254 1.00 28.37  ? 172 GLN D CA  1 
ATOM   7586  C C   . GLN D  2 172 ? 6.368   -9.629  -24.235 1.00 28.83  ? 172 GLN D C   1 
ATOM   7587  O O   . GLN D  2 172 ? 6.184   -10.453 -23.337 1.00 29.69  ? 172 GLN D O   1 
ATOM   7588  C CB  . GLN D  2 172 ? 8.879   -9.624  -24.330 1.00 28.88  ? 172 GLN D CB  1 
ATOM   7589  C CG  . GLN D  2 172 ? 9.143   -10.191 -25.725 1.00 32.13  ? 172 GLN D CG  1 
ATOM   7590  C CD  . GLN D  2 172 ? 10.015  -11.437 -25.710 1.00 34.68  ? 172 GLN D CD  1 
ATOM   7591  O OE1 . GLN D  2 172 ? 10.668  -11.749 -24.710 1.00 36.15  ? 172 GLN D OE1 1 
ATOM   7592  N NE2 . GLN D  2 172 ? 10.029  -12.158 -26.828 1.00 32.58  ? 172 GLN D NE2 1 
ATOM   7593  N N   . GLY E  1 4   ? 17.566  14.983  -11.913 1.00 12.17  ? 10  GLY E N   1 
ATOM   7594  C CA  . GLY E  1 4   ? 16.094  14.865  -12.131 1.00 11.85  ? 10  GLY E CA  1 
ATOM   7595  C C   . GLY E  1 4   ? 15.273  15.393  -10.969 1.00 11.89  ? 10  GLY E C   1 
ATOM   7596  O O   . GLY E  1 4   ? 15.661  15.243  -9.807  1.00 12.00  ? 10  GLY E O   1 
ATOM   7597  N N   . ASP E  1 5   ? 14.131  16.004  -11.289 1.00 11.90  ? 11  ASP E N   1 
ATOM   7598  C CA  . ASP E  1 5   ? 13.202  16.546  -10.288 1.00 11.89  ? 11  ASP E CA  1 
ATOM   7599  C C   . ASP E  1 5   ? 12.650  15.465  -9.355  1.00 11.46  ? 11  ASP E C   1 
ATOM   7600  O O   . ASP E  1 5   ? 12.467  14.315  -9.766  1.00 11.55  ? 11  ASP E O   1 
ATOM   7601  C CB  . ASP E  1 5   ? 12.028  17.271  -10.964 1.00 12.09  ? 11  ASP E CB  1 
ATOM   7602  C CG  . ASP E  1 5   ? 12.465  18.449  -11.821 1.00 13.49  ? 11  ASP E CG  1 
ATOM   7603  O OD1 . ASP E  1 5   ? 11.574  19.157  -12.334 1.00 13.68  ? 11  ASP E OD1 1 
ATOM   7604  O OD2 . ASP E  1 5   ? 13.685  18.671  -11.991 1.00 17.37  ? 11  ASP E OD2 1 
ATOM   7605  N N   . LYS E  1 6   ? 12.384  15.847  -8.106  1.00 10.55  ? 12  LYS E N   1 
ATOM   7606  C CA  . LYS E  1 6   ? 11.801  14.942  -7.118  1.00 9.88   ? 12  LYS E CA  1 
ATOM   7607  C C   . LYS E  1 6   ? 11.009  15.676  -6.045  1.00 9.55   ? 12  LYS E C   1 
ATOM   7608  O O   . LYS E  1 6   ? 11.294  16.835  -5.739  1.00 10.30  ? 12  LYS E O   1 
ATOM   7609  C CB  . LYS E  1 6   ? 12.873  14.044  -6.480  1.00 10.21  ? 12  LYS E CB  1 
ATOM   7610  C CG  . LYS E  1 6   ? 13.978  14.757  -5.707  1.00 11.13  ? 12  LYS E CG  1 
ATOM   7611  C CD  . LYS E  1 6   ? 15.299  14.003  -5.883  1.00 18.05  ? 12  LYS E CD  1 
ATOM   7612  C CE  . LYS E  1 6   ? 16.364  14.427  -4.878  1.00 20.07  ? 12  LYS E CE  1 
ATOM   7613  N NZ  . LYS E  1 6   ? 16.268  13.662  -3.595  1.00 18.91  ? 12  LYS E NZ  1 
ATOM   7614  N N   . ILE E  1 7   ? 10.003  14.997  -5.495  1.00 8.35   ? 13  ILE E N   1 
ATOM   7615  C CA  . ILE E  1 7   ? 9.251   15.501  -4.343  1.00 7.04   ? 13  ILE E CA  1 
ATOM   7616  C C   . ILE E  1 7   ? 9.402   14.533  -3.168  1.00 6.86   ? 13  ILE E C   1 
ATOM   7617  O O   . ILE E  1 7   ? 9.197   13.324  -3.309  1.00 7.43   ? 13  ILE E O   1 
ATOM   7618  C CB  . ILE E  1 7   ? 7.755   15.794  -4.687  1.00 6.69   ? 13  ILE E CB  1 
ATOM   7619  C CG1 . ILE E  1 7   ? 7.078   16.576  -3.557  1.00 5.49   ? 13  ILE E CG1 1 
ATOM   7620  C CG2 . ILE E  1 7   ? 6.982   14.511  -5.033  1.00 5.49   ? 13  ILE E CG2 1 
ATOM   7621  C CD1 . ILE E  1 7   ? 5.794   17.275  -3.971  1.00 3.42   ? 13  ILE E CD1 1 
ATOM   7622  N N   . CYS E  1 8   ? 9.791   15.061  -2.017  1.00 6.30   ? 14  CYS E N   1 
ATOM   7623  C CA  . CYS E  1 8   ? 10.033  14.223  -0.848  1.00 6.40   ? 14  CYS E CA  1 
ATOM   7624  C C   . CYS E  1 8   ? 9.015   14.490  0.251   1.00 6.75   ? 14  CYS E C   1 
ATOM   7625  O O   . CYS E  1 8   ? 8.663   15.640  0.529   1.00 6.40   ? 14  CYS E O   1 
ATOM   7626  C CB  . CYS E  1 8   ? 11.459  14.424  -0.326  1.00 5.90   ? 14  CYS E CB  1 
ATOM   7627  S SG  . CYS E  1 8   ? 12.733  13.925  -1.494  0.60 3.09   ? 14  CYS E SG  1 
ATOM   7628  N N   . LEU E  1 9   ? 8.533   13.422  0.871   1.00 7.21   ? 15  LEU E N   1 
ATOM   7629  C CA  . LEU E  1 9   ? 7.608   13.568  1.984   1.00 7.40   ? 15  LEU E CA  1 
ATOM   7630  C C   . LEU E  1 9   ? 8.302   13.337  3.309   1.00 7.88   ? 15  LEU E C   1 
ATOM   7631  O O   . LEU E  1 9   ? 9.221   12.524  3.408   1.00 8.12   ? 15  LEU E O   1 
ATOM   7632  C CB  . LEU E  1 9   ? 6.399   12.653  1.824   1.00 6.54   ? 15  LEU E CB  1 
ATOM   7633  C CG  . LEU E  1 9   ? 5.314   13.316  0.981   1.00 5.99   ? 15  LEU E CG  1 
ATOM   7634  C CD1 . LEU E  1 9   ? 5.375   12.849  -0.469  1.00 6.25   ? 15  LEU E CD1 1 
ATOM   7635  C CD2 . LEU E  1 9   ? 3.973   13.010  1.578   1.00 7.48   ? 15  LEU E CD2 1 
ATOM   7636  N N   . GLY E  1 10  ? 7.862   14.074  4.320   1.00 8.45   ? 16  GLY E N   1 
ATOM   7637  C CA  . GLY E  1 10  ? 8.459   13.988  5.638   1.00 9.66   ? 16  GLY E CA  1 
ATOM   7638  C C   . GLY E  1 10  ? 7.622   14.647  6.710   1.00 10.82  ? 16  GLY E C   1 
ATOM   7639  O O   . GLY E  1 10  ? 6.488   15.077  6.468   1.00 11.05  ? 16  GLY E O   1 
ATOM   7640  N N   . HIS E  1 11  ? 8.197   14.720  7.904   1.00 11.22  ? 17  HIS E N   1 
ATOM   7641  C CA  . HIS E  1 11  ? 7.509   15.237  9.072   1.00 11.49  ? 17  HIS E CA  1 
ATOM   7642  C C   . HIS E  1 11  ? 8.443   16.173  9.815   1.00 12.13  ? 17  HIS E C   1 
ATOM   7643  O O   . HIS E  1 11  ? 9.646   16.193  9.550   1.00 12.44  ? 17  HIS E O   1 
ATOM   7644  C CB  . HIS E  1 11  ? 7.079   14.086  9.981   1.00 10.92  ? 17  HIS E CB  1 
ATOM   7645  C CG  . HIS E  1 11  ? 8.210   13.205  10.409  1.00 10.64  ? 17  HIS E CG  1 
ATOM   7646  N ND1 . HIS E  1 11  ? 8.725   12.212  9.603   1.00 11.85  ? 17  HIS E ND1 1 
ATOM   7647  C CD2 . HIS E  1 11  ? 8.935   13.175  11.551  1.00 10.86  ? 17  HIS E CD2 1 
ATOM   7648  C CE1 . HIS E  1 11  ? 9.713   11.604  10.233  1.00 12.07  ? 17  HIS E CE1 1 
ATOM   7649  N NE2 . HIS E  1 11  ? 9.859   12.168  11.418  1.00 13.49  ? 17  HIS E NE2 1 
ATOM   7650  N N   . HIS E  1 12  ? 7.886   16.946  10.740  1.00 12.82  ? 18  HIS E N   1 
ATOM   7651  C CA  . HIS E  1 12  ? 8.673   17.866  11.548  1.00 13.50  ? 18  HIS E CA  1 
ATOM   7652  C C   . HIS E  1 12  ? 9.380   17.137  12.690  1.00 13.87  ? 18  HIS E C   1 
ATOM   7653  O O   . HIS E  1 12  ? 9.048   15.991  13.012  1.00 13.85  ? 18  HIS E O   1 
ATOM   7654  C CB  . HIS E  1 12  ? 7.788   19.008  12.075  1.00 13.67  ? 18  HIS E CB  1 
ATOM   7655  C CG  . HIS E  1 12  ? 6.892   18.625  13.216  1.00 13.51  ? 18  HIS E CG  1 
ATOM   7656  N ND1 . HIS E  1 12  ? 6.403   17.347  13.395  1.00 13.44  ? 18  HIS E ND1 1 
ATOM   7657  C CD2 . HIS E  1 12  ? 6.375   19.369  14.224  1.00 13.87  ? 18  HIS E CD2 1 
ATOM   7658  C CE1 . HIS E  1 12  ? 5.645   17.315  14.477  1.00 13.94  ? 18  HIS E CE1 1 
ATOM   7659  N NE2 . HIS E  1 12  ? 5.608   18.530  14.995  1.00 13.19  ? 18  HIS E NE2 1 
ATOM   7660  N N   . ALA E  1 13  ? 10.363  17.806  13.284  1.00 14.25  ? 19  ALA E N   1 
ATOM   7661  C CA  . ALA E  1 13  ? 11.065  17.292  14.455  1.00 14.69  ? 19  ALA E CA  1 
ATOM   7662  C C   . ALA E  1 13  ? 11.743  18.432  15.203  1.00 14.99  ? 19  ALA E C   1 
ATOM   7663  O O   . ALA E  1 13  ? 11.992  19.500  14.640  1.00 15.84  ? 19  ALA E O   1 
ATOM   7664  C CB  . ALA E  1 13  ? 12.092  16.229  14.052  1.00 14.47  ? 19  ALA E CB  1 
ATOM   7665  N N   . VAL E  1 14  ? 12.028  18.199  16.478  1.00 14.78  ? 20  VAL E N   1 
ATOM   7666  C CA  . VAL E  1 14  ? 12.830  19.118  17.272  1.00 14.81  ? 20  VAL E CA  1 
ATOM   7667  C C   . VAL E  1 14  ? 14.134  18.423  17.660  1.00 16.30  ? 20  VAL E C   1 
ATOM   7668  O O   . VAL E  1 14  ? 14.189  17.191  17.730  1.00 16.66  ? 20  VAL E O   1 
ATOM   7669  C CB  . VAL E  1 14  ? 12.069  19.628  18.528  1.00 14.38  ? 20  VAL E CB  1 
ATOM   7670  C CG1 . VAL E  1 14  ? 10.828  20.422  18.119  1.00 11.94  ? 20  VAL E CG1 1 
ATOM   7671  C CG2 . VAL E  1 14  ? 11.693  18.476  19.461  1.00 11.51  ? 20  VAL E CG2 1 
ATOM   7672  N N   . ALA E  1 15  ? 15.184  19.205  17.895  1.00 17.37  ? 21  ALA E N   1 
ATOM   7673  C CA  . ALA E  1 15  ? 16.468  18.649  18.323  1.00 18.11  ? 21  ALA E CA  1 
ATOM   7674  C C   . ALA E  1 15  ? 16.369  18.136  19.755  1.00 18.51  ? 21  ALA E C   1 
ATOM   7675  O O   . ALA E  1 15  ? 17.106  17.233  20.160  1.00 18.26  ? 21  ALA E O   1 
ATOM   7676  C CB  . ALA E  1 15  ? 17.565  19.696  18.210  1.00 17.85  ? 21  ALA E CB  1 
ATOM   7677  N N   . ASN E  1 16  ? 15.425  18.708  20.497  1.00 19.29  ? 22  ASN E N   1 
ATOM   7678  C CA  . ASN E  1 16  ? 15.321  18.510  21.931  1.00 20.39  ? 22  ASN E CA  1 
ATOM   7679  C C   . ASN E  1 16  ? 13.902  18.085  22.330  1.00 20.02  ? 22  ASN E C   1 
ATOM   7680  O O   . ASN E  1 16  ? 13.080  18.915  22.735  1.00 20.37  ? 22  ASN E O   1 
ATOM   7681  C CB  . ASN E  1 16  ? 15.713  19.812  22.632  1.00 21.32  ? 22  ASN E CB  1 
ATOM   7682  C CG  . ASN E  1 16  ? 16.782  19.614  23.685  1.00 25.19  ? 22  ASN E CG  1 
ATOM   7683  O OD1 . ASN E  1 16  ? 16.651  18.771  24.577  1.00 30.54  ? 22  ASN E OD1 1 
ATOM   7684  N ND2 . ASN E  1 16  ? 17.848  20.406  23.596  1.00 26.02  ? 22  ASN E ND2 1 
ATOM   7685  N N   . GLY E  1 17  ? 13.618  16.791  22.201  1.00 18.92  ? 23  GLY E N   1 
ATOM   7686  C CA  . GLY E  1 17  ? 12.288  16.260  22.493  1.00 17.95  ? 23  GLY E CA  1 
ATOM   7687  C C   . GLY E  1 17  ? 12.083  15.841  23.937  1.00 17.40  ? 23  GLY E C   1 
ATOM   7688  O O   . GLY E  1 17  ? 12.985  15.976  24.766  1.00 17.26  ? 23  GLY E O   1 
ATOM   7689  N N   . THR E  1 18  ? 10.887  15.331  24.228  1.00 16.73  ? 24  THR E N   1 
ATOM   7690  C CA  . THR E  1 18  ? 10.532  14.853  25.565  1.00 16.56  ? 24  THR E CA  1 
ATOM   7691  C C   . THR E  1 18  ? 10.445  13.324  25.587  1.00 15.82  ? 24  THR E C   1 
ATOM   7692  O O   . THR E  1 18  ? 9.802   12.722  24.724  1.00 16.10  ? 24  THR E O   1 
ATOM   7693  C CB  . THR E  1 18  ? 9.183   15.447  26.027  1.00 16.76  ? 24  THR E CB  1 
ATOM   7694  O OG1 . THR E  1 18  ? 9.172   16.859  25.785  1.00 19.11  ? 24  THR E OG1 1 
ATOM   7695  C CG2 . THR E  1 18  ? 8.949   15.189  27.509  1.00 17.56  ? 24  THR E CG2 1 
ATOM   7696  N N   . LYS E  1 19  ? 11.094  12.705  26.571  1.00 15.20  ? 25  LYS E N   1 
ATOM   7697  C CA  . LYS E  1 19  ? 11.073  11.247  26.707  1.00 14.84  ? 25  LYS E CA  1 
ATOM   7698  C C   . LYS E  1 19  ? 9.814   10.782  27.443  1.00 13.86  ? 25  LYS E C   1 
ATOM   7699  O O   . LYS E  1 19  ? 9.524   11.246  28.546  1.00 13.79  ? 25  LYS E O   1 
ATOM   7700  C CB  . LYS E  1 19  ? 12.340  10.719  27.405  1.00 14.79  ? 25  LYS E CB  1 
ATOM   7701  C CG  . LYS E  1 19  ? 13.663  11.202  26.797  1.00 17.85  ? 25  LYS E CG  1 
ATOM   7702  C CD  . LYS E  1 19  ? 14.710  10.084  26.655  1.00 21.81  ? 25  LYS E CD  1 
ATOM   7703  C CE  . LYS E  1 19  ? 15.190  9.520   27.998  1.00 24.97  ? 25  LYS E CE  1 
ATOM   7704  N NZ  . LYS E  1 19  ? 16.047  10.470  28.768  1.00 26.73  ? 25  LYS E NZ  1 
ATOM   7705  N N   . VAL E  1 20  ? 9.066   9.880   26.809  1.00 12.82  ? 26  VAL E N   1 
ATOM   7706  C CA  . VAL E  1 20  ? 7.859   9.290   27.400  1.00 11.69  ? 26  VAL E CA  1 
ATOM   7707  C C   . VAL E  1 20  ? 7.924   7.762   27.368  1.00 11.41  ? 26  VAL E C   1 
ATOM   7708  O O   . VAL E  1 20  ? 8.781   7.182   26.693  1.00 12.02  ? 26  VAL E O   1 
ATOM   7709  C CB  . VAL E  1 20  ? 6.561   9.747   26.681  1.00 11.86  ? 26  VAL E CB  1 
ATOM   7710  C CG1 . VAL E  1 20  ? 6.348   11.247  26.835  1.00 9.93   ? 26  VAL E CG1 1 
ATOM   7711  C CG2 . VAL E  1 20  ? 6.571   9.333   25.204  1.00 11.17  ? 26  VAL E CG2 1 
ATOM   7712  N N   . ASN E  1 21  ? 7.014   7.119   28.094  1.00 9.94   ? 27  ASN E N   1 
ATOM   7713  C CA  . ASN E  1 21  ? 6.933   5.665   28.105  1.00 9.10   ? 27  ASN E CA  1 
ATOM   7714  C C   . ASN E  1 21  ? 5.738   5.181   27.307  1.00 8.81   ? 27  ASN E C   1 
ATOM   7715  O O   . ASN E  1 21  ? 4.675   5.806   27.323  1.00 8.63   ? 27  ASN E O   1 
ATOM   7716  C CB  . ASN E  1 21  ? 6.856   5.133   29.538  1.00 9.18   ? 27  ASN E CB  1 
ATOM   7717  C CG  . ASN E  1 21  ? 8.021   5.595   30.403  1.00 11.02  ? 27  ASN E CG  1 
ATOM   7718  O OD1 . ASN E  1 21  ? 9.165   5.677   29.945  1.00 11.89  ? 27  ASN E OD1 1 
ATOM   7719  N ND2 . ASN E  1 21  ? 7.734   5.895   31.666  1.00 7.57   ? 27  ASN E ND2 1 
ATOM   7720  N N   . THR E  1 22  ? 5.930   4.074   26.596  1.00 8.15   ? 28  THR E N   1 
ATOM   7721  C CA  . THR E  1 22  ? 4.847   3.392   25.896  1.00 7.34   ? 28  THR E CA  1 
ATOM   7722  C C   . THR E  1 22  ? 4.691   1.995   26.491  1.00 6.64   ? 28  THR E C   1 
ATOM   7723  O O   . THR E  1 22  ? 5.328   1.677   27.498  1.00 6.02   ? 28  THR E O   1 
ATOM   7724  C CB  . THR E  1 22  ? 5.121   3.280   24.381  1.00 7.42   ? 28  THR E CB  1 
ATOM   7725  O OG1 . THR E  1 22  ? 6.193   2.358   24.149  1.00 7.08   ? 28  THR E OG1 1 
ATOM   7726  C CG2 . THR E  1 22  ? 5.485   4.629   23.795  1.00 8.03   ? 28  THR E CG2 1 
ATOM   7727  N N   . LEU E  1 23  ? 3.852   1.168   25.867  1.00 6.34   ? 29  LEU E N   1 
ATOM   7728  C CA  . LEU E  1 23  ? 3.670   -0.226  26.281  1.00 6.21   ? 29  LEU E CA  1 
ATOM   7729  C C   . LEU E  1 23  ? 4.872   -1.070  25.897  1.00 6.98   ? 29  LEU E C   1 
ATOM   7730  O O   . LEU E  1 23  ? 5.063   -2.172  26.404  1.00 7.80   ? 29  LEU E O   1 
ATOM   7731  C CB  . LEU E  1 23  ? 2.435   -0.830  25.615  1.00 5.58   ? 29  LEU E CB  1 
ATOM   7732  C CG  . LEU E  1 23  ? 1.053   -0.243  25.873  1.00 3.14   ? 29  LEU E CG  1 
ATOM   7733  C CD1 . LEU E  1 23  ? 0.085   -0.840  24.874  1.00 2.00   ? 29  LEU E CD1 1 
ATOM   7734  C CD2 . LEU E  1 23  ? 0.594   -0.497  27.302  1.00 2.00   ? 29  LEU E CD2 1 
ATOM   7735  N N   . THR E  1 24  ? 5.677   -0.526  24.996  1.00 7.93   ? 30  THR E N   1 
ATOM   7736  C CA  . THR E  1 24  ? 6.714   -1.264  24.299  1.00 8.53   ? 30  THR E CA  1 
ATOM   7737  C C   . THR E  1 24  ? 8.102   -0.746  24.660  1.00 9.20   ? 30  THR E C   1 
ATOM   7738  O O   . THR E  1 24  ? 9.100   -1.463  24.540  1.00 9.21   ? 30  THR E O   1 
ATOM   7739  C CB  . THR E  1 24  ? 6.461   -1.155  22.773  1.00 7.88   ? 30  THR E CB  1 
ATOM   7740  O OG1 . THR E  1 24  ? 5.756   -2.317  22.329  1.00 9.11   ? 30  THR E OG1 1 
ATOM   7741  C CG2 . THR E  1 24  ? 7.745   -1.004  21.979  1.00 9.14   ? 30  THR E CG2 1 
ATOM   7742  N N   . GLU E  1 25  ? 8.155   0.500   25.119  1.00 9.66   ? 31  GLU E N   1 
ATOM   7743  C CA  . GLU E  1 25  ? 9.420   1.196   25.243  1.00 10.53  ? 31  GLU E CA  1 
ATOM   7744  C C   . GLU E  1 25  ? 9.428   2.150   26.424  1.00 10.34  ? 31  GLU E C   1 
ATOM   7745  O O   . GLU E  1 25  ? 8.422   2.785   26.733  1.00 10.54  ? 31  GLU E O   1 
ATOM   7746  C CB  . GLU E  1 25  ? 9.705   1.957   23.950  1.00 10.53  ? 31  GLU E CB  1 
ATOM   7747  C CG  . GLU E  1 25  ? 11.167  2.036   23.579  1.00 14.75  ? 31  GLU E CG  1 
ATOM   7748  C CD  . GLU E  1 25  ? 11.371  2.330   22.107  1.00 20.05  ? 31  GLU E CD  1 
ATOM   7749  O OE1 . GLU E  1 25  ? 10.483  1.988   21.292  1.00 20.83  ? 31  GLU E OE1 1 
ATOM   7750  O OE2 . GLU E  1 25  ? 12.424  2.903   21.762  1.00 24.83  ? 31  GLU E OE2 1 
ATOM   7751  N N   . ARG E  1 26  ? 10.576  2.230   27.084  1.00 10.87  ? 32  ARG E N   1 
ATOM   7752  C CA  . ARG E  1 26  ? 10.783  3.166   28.171  1.00 11.77  ? 32  ARG E CA  1 
ATOM   7753  C C   . ARG E  1 26  ? 11.670  4.311   27.675  1.00 11.65  ? 32  ARG E C   1 
ATOM   7754  O O   . ARG E  1 26  ? 12.687  4.076   27.023  1.00 11.99  ? 32  ARG E O   1 
ATOM   7755  C CB  . ARG E  1 26  ? 11.412  2.450   29.371  1.00 11.95  ? 32  ARG E CB  1 
ATOM   7756  C CG  . ARG E  1 26  ? 11.305  3.219   30.678  1.00 16.06  ? 32  ARG E CG  1 
ATOM   7757  C CD  . ARG E  1 26  ? 11.187  2.288   31.875  1.00 20.80  ? 32  ARG E CD  1 
ATOM   7758  N NE  . ARG E  1 26  ? 10.720  2.998   33.068  1.00 25.83  ? 32  ARG E NE  1 
ATOM   7759  C CZ  . ARG E  1 26  ? 9.440   3.225   33.370  1.00 27.13  ? 32  ARG E CZ  1 
ATOM   7760  N NH1 . ARG E  1 26  ? 8.465   2.802   32.571  1.00 28.34  ? 32  ARG E NH1 1 
ATOM   7761  N NH2 . ARG E  1 26  ? 9.130   3.882   34.479  1.00 26.72  ? 32  ARG E NH2 1 
ATOM   7762  N N   . GLY E  1 27  ? 11.265  5.544   27.961  1.00 11.53  ? 33  GLY E N   1 
ATOM   7763  C CA  . GLY E  1 27  ? 12.042  6.724   27.581  1.00 11.73  ? 33  GLY E CA  1 
ATOM   7764  C C   . GLY E  1 27  ? 12.284  6.887   26.089  1.00 11.99  ? 33  GLY E C   1 
ATOM   7765  O O   . GLY E  1 27  ? 13.413  7.135   25.663  1.00 12.18  ? 33  GLY E O   1 
ATOM   7766  N N   . ILE E  1 28  ? 11.225  6.735   25.296  1.00 12.05  ? 34  ILE E N   1 
ATOM   7767  C CA  . ILE E  1 28  ? 11.275  7.023   23.862  1.00 11.31  ? 34  ILE E CA  1 
ATOM   7768  C C   . ILE E  1 28  ? 10.964  8.507   23.651  1.00 11.02  ? 34  ILE E C   1 
ATOM   7769  O O   . ILE E  1 28  ? 10.101  9.067   24.326  1.00 11.48  ? 34  ILE E O   1 
ATOM   7770  C CB  . ILE E  1 28  ? 10.311  6.103   23.054  1.00 11.40  ? 34  ILE E CB  1 
ATOM   7771  C CG1 . ILE E  1 28  ? 10.621  6.164   21.554  1.00 13.47  ? 34  ILE E CG1 1 
ATOM   7772  C CG2 . ILE E  1 28  ? 8.839   6.422   23.356  1.00 9.74   ? 34  ILE E CG2 1 
ATOM   7773  C CD1 . ILE E  1 28  ? 9.863   5.139   20.712  1.00 17.14  ? 34  ILE E CD1 1 
ATOM   7774  N N   . GLU E  1 29  ? 11.676  9.141   22.727  1.00 10.61  ? 35  GLU E N   1 
ATOM   7775  C CA  . GLU E  1 29  ? 11.578  10.586  22.541  1.00 10.71  ? 35  GLU E CA  1 
ATOM   7776  C C   . GLU E  1 29  ? 10.424  10.983  21.620  1.00 10.14  ? 35  GLU E C   1 
ATOM   7777  O O   . GLU E  1 29  ? 10.361  10.545  20.471  1.00 11.09  ? 35  GLU E O   1 
ATOM   7778  C CB  . GLU E  1 29  ? 12.908  11.123  22.003  1.00 11.50  ? 35  GLU E CB  1 
ATOM   7779  C CG  . GLU E  1 29  ? 13.095  12.631  22.120  1.00 14.96  ? 35  GLU E CG  1 
ATOM   7780  C CD  . GLU E  1 29  ? 14.555  13.051  21.986  1.00 20.28  ? 35  GLU E CD  1 
ATOM   7781  O OE1 . GLU E  1 29  ? 15.374  12.637  22.838  1.00 23.87  ? 35  GLU E OE1 1 
ATOM   7782  O OE2 . GLU E  1 29  ? 14.882  13.801  21.037  1.00 18.30  ? 35  GLU E OE2 1 
ATOM   7783  N N   . VAL E  1 30  ? 9.508   11.802  22.130  1.00 9.04   ? 36  VAL E N   1 
ATOM   7784  C CA  . VAL E  1 30  ? 8.467   12.402  21.292  1.00 8.54   ? 36  VAL E CA  1 
ATOM   7785  C C   . VAL E  1 30  ? 8.650   13.917  21.185  1.00 9.10   ? 36  VAL E C   1 
ATOM   7786  O O   . VAL E  1 30  ? 9.398   14.519  21.967  1.00 8.48   ? 36  VAL E O   1 
ATOM   7787  C CB  . VAL E  1 30  ? 7.033   12.070  21.774  1.00 8.20   ? 36  VAL E CB  1 
ATOM   7788  C CG1 . VAL E  1 30  ? 6.760   10.577  21.646  1.00 9.22   ? 36  VAL E CG1 1 
ATOM   7789  C CG2 . VAL E  1 30  ? 6.801   12.555  23.200  1.00 7.12   ? 36  VAL E CG2 1 
ATOM   7790  N N   . VAL E  1 31  ? 7.966   14.521  20.214  1.00 9.31   ? 37  VAL E N   1 
ATOM   7791  C CA  . VAL E  1 31  ? 8.092   15.957  19.942  1.00 9.61   ? 37  VAL E CA  1 
ATOM   7792  C C   . VAL E  1 31  ? 7.627   16.798  21.135  1.00 10.26  ? 37  VAL E C   1 
ATOM   7793  O O   . VAL E  1 31  ? 8.321   17.729  21.554  1.00 10.30  ? 37  VAL E O   1 
ATOM   7794  C CB  . VAL E  1 31  ? 7.348   16.361  18.636  1.00 9.21   ? 37  VAL E CB  1 
ATOM   7795  C CG1 . VAL E  1 31  ? 7.393   17.865  18.414  1.00 6.25   ? 37  VAL E CG1 1 
ATOM   7796  C CG2 . VAL E  1 31  ? 7.959   15.651  17.443  1.00 9.10   ? 37  VAL E CG2 1 
ATOM   7797  N N   . ASN E  1 32  ? 6.469   16.442  21.687  1.00 10.58  ? 38  ASN E N   1 
ATOM   7798  C CA  . ASN E  1 32  ? 5.874   17.171  22.800  1.00 11.47  ? 38  ASN E CA  1 
ATOM   7799  C C   . ASN E  1 32  ? 5.085   16.231  23.714  1.00 11.07  ? 38  ASN E C   1 
ATOM   7800  O O   . ASN E  1 32  ? 4.594   15.185  23.273  1.00 11.30  ? 38  ASN E O   1 
ATOM   7801  C CB  . ASN E  1 32  ? 4.971   18.291  22.266  1.00 12.28  ? 38  ASN E CB  1 
ATOM   7802  C CG  . ASN E  1 32  ? 4.785   19.431  23.259  1.00 19.53  ? 38  ASN E CG  1 
ATOM   7803  O OD1 . ASN E  1 32  ? 5.617   19.651  24.144  1.00 19.11  ? 38  ASN E OD1 1 
ATOM   7804  N ND2 . ASN E  1 32  ? 3.682   20.167  23.108  1.00 33.34  ? 38  ASN E ND2 1 
ATOM   7805  N N   . ALA E  1 33  ? 4.971   16.611  24.986  1.00 10.24  ? 39  ALA E N   1 
ATOM   7806  C CA  . ALA E  1 33  ? 4.245   15.824  25.977  1.00 9.52   ? 39  ALA E CA  1 
ATOM   7807  C C   . ALA E  1 33  ? 3.739   16.701  27.114  1.00 10.36  ? 39  ALA E C   1 
ATOM   7808  O O   . ALA E  1 33  ? 4.402   17.662  27.510  1.00 10.93  ? 39  ALA E O   1 
ATOM   7809  C CB  . ALA E  1 33  ? 5.126   14.727  26.522  1.00 9.17   ? 39  ALA E CB  1 
ATOM   7810  N N   . THR E  1 34  ? 2.566   16.367  27.643  1.00 10.43  ? 40  THR E N   1 
ATOM   7811  C CA  . THR E  1 34  ? 2.001   17.120  28.757  1.00 10.85  ? 40  THR E CA  1 
ATOM   7812  C C   . THR E  1 34  ? 1.749   16.244  29.992  1.00 10.60  ? 40  THR E C   1 
ATOM   7813  O O   . THR E  1 34  ? 1.295   15.102  29.876  1.00 10.98  ? 40  THR E O   1 
ATOM   7814  C CB  . THR E  1 34  ? 0.732   17.924  28.338  1.00 11.15  ? 40  THR E CB  1 
ATOM   7815  O OG1 . THR E  1 34  ? 0.170   18.575  29.483  1.00 12.08  ? 40  THR E OG1 1 
ATOM   7816  C CG2 . THR E  1 34  ? -0.319  17.025  27.723  1.00 11.60  ? 40  THR E CG2 1 
ATOM   7817  N N   . GLU E  1 35  ? 2.064   16.797  31.162  1.00 9.82   ? 41  GLU E N   1 
ATOM   7818  C CA  . GLU E  1 35  ? 1.957   16.101  32.444  1.00 9.08   ? 41  GLU E CA  1 
ATOM   7819  C C   . GLU E  1 35  ? 0.506   15.783  32.801  1.00 8.82   ? 41  GLU E C   1 
ATOM   7820  O O   . GLU E  1 35  ? -0.397  16.541  32.462  1.00 9.01   ? 41  GLU E O   1 
ATOM   7821  C CB  . GLU E  1 35  ? 2.613   16.947  33.546  1.00 8.67   ? 41  GLU E CB  1 
ATOM   7822  C CG  . GLU E  1 35  ? 2.597   16.339  34.946  1.00 7.79   ? 41  GLU E CG  1 
ATOM   7823  C CD  . GLU E  1 35  ? 3.304   15.000  35.020  1.00 9.91   ? 41  GLU E CD  1 
ATOM   7824  O OE1 . GLU E  1 35  ? 4.552   14.984  35.018  1.00 7.50   ? 41  GLU E OE1 1 
ATOM   7825  O OE2 . GLU E  1 35  ? 2.611   13.962  35.084  1.00 10.61  ? 41  GLU E OE2 1 
ATOM   7826  N N   . THR E  1 36  ? 0.298   14.652  33.476  1.00 8.75   ? 42  THR E N   1 
ATOM   7827  C CA  . THR E  1 36  ? -1.033  14.213  33.910  1.00 8.19   ? 42  THR E CA  1 
ATOM   7828  C C   . THR E  1 36  ? -1.093  14.019  35.428  1.00 8.84   ? 42  THR E C   1 
ATOM   7829  O O   . THR E  1 36  ? -2.166  13.773  35.991  1.00 9.49   ? 42  THR E O   1 
ATOM   7830  C CB  . THR E  1 36  ? -1.470  12.889  33.224  1.00 7.90   ? 42  THR E CB  1 
ATOM   7831  O OG1 . THR E  1 36  ? -0.585  11.830  33.604  1.00 6.21   ? 42  THR E OG1 1 
ATOM   7832  C CG2 . THR E  1 36  ? -1.475  13.025  31.706  1.00 6.80   ? 42  THR E CG2 1 
ATOM   7833  N N   . VAL E  1 37  ? 0.064   14.121  36.079  1.00 8.79   ? 43  VAL E N   1 
ATOM   7834  C CA  . VAL E  1 37  ? 0.151   14.025  37.534  1.00 9.06   ? 43  VAL E CA  1 
ATOM   7835  C C   . VAL E  1 37  ? 0.448   15.407  38.137  1.00 9.20   ? 43  VAL E C   1 
ATOM   7836  O O   . VAL E  1 37  ? 1.521   15.979  37.914  1.00 9.35   ? 43  VAL E O   1 
ATOM   7837  C CB  . VAL E  1 37  ? 1.216   12.983  37.979  1.00 8.78   ? 43  VAL E CB  1 
ATOM   7838  C CG1 . VAL E  1 37  ? 1.228   12.828  39.486  1.00 9.17   ? 43  VAL E CG1 1 
ATOM   7839  C CG2 . VAL E  1 37  ? 0.953   11.640  37.336  1.00 10.28  ? 43  VAL E CG2 1 
ATOM   7840  N N   . GLU E  1 38  ? -0.512  15.942  38.889  1.00 9.25   ? 44  GLU E N   1 
ATOM   7841  C CA  . GLU E  1 38  ? -0.323  17.219  39.572  1.00 10.37  ? 44  GLU E CA  1 
ATOM   7842  C C   . GLU E  1 38  ? 0.559   17.061  40.807  1.00 10.76  ? 44  GLU E C   1 
ATOM   7843  O O   . GLU E  1 38  ? 0.287   16.228  41.671  1.00 11.28  ? 44  GLU E O   1 
ATOM   7844  C CB  . GLU E  1 38  ? -1.667  17.846  39.955  1.00 10.40  ? 44  GLU E CB  1 
ATOM   7845  C CG  . GLU E  1 38  ? -1.549  19.244  40.573  1.00 13.11  ? 44  GLU E CG  1 
ATOM   7846  C CD  . GLU E  1 38  ? -1.035  20.293  39.594  1.00 15.57  ? 44  GLU E CD  1 
ATOM   7847  O OE1 . GLU E  1 38  ? -1.556  20.368  38.460  1.00 15.72  ? 44  GLU E OE1 1 
ATOM   7848  O OE2 . GLU E  1 38  ? -0.116  21.052  39.963  1.00 17.11  ? 44  GLU E OE2 1 
ATOM   7849  N N   . THR E  1 39  ? 1.620   17.859  40.878  1.00 11.34  ? 45  THR E N   1 
ATOM   7850  C CA  . THR E  1 39  ? 2.524   17.838  42.027  1.00 11.86  ? 45  THR E CA  1 
ATOM   7851  C C   . THR E  1 39  ? 2.634   19.210  42.676  1.00 12.20  ? 45  THR E C   1 
ATOM   7852  O O   . THR E  1 39  ? 3.241   19.349  43.738  1.00 13.13  ? 45  THR E O   1 
ATOM   7853  C CB  . THR E  1 39  ? 3.944   17.350  41.650  1.00 11.70  ? 45  THR E CB  1 
ATOM   7854  O OG1 . THR E  1 39  ? 4.501   18.206  40.646  1.00 11.63  ? 45  THR E OG1 1 
ATOM   7855  C CG2 . THR E  1 39  ? 3.910   15.917  41.135  1.00 12.88  ? 45  THR E CG2 1 
ATOM   7856  N N   . THR E  1 40  ? 2.045   20.217  42.037  1.00 12.59  ? 46  THR E N   1 
ATOM   7857  C CA  . THR E  1 40  ? 2.124   21.591  42.525  1.00 12.62  ? 46  THR E CA  1 
ATOM   7858  C C   . THR E  1 40  ? 0.992   21.904  43.505  1.00 12.90  ? 46  THR E C   1 
ATOM   7859  O O   . THR E  1 40  ? -0.183  22.007  43.130  1.00 13.43  ? 46  THR E O   1 
ATOM   7860  C CB  . THR E  1 40  ? 2.202   22.608  41.359  1.00 12.79  ? 46  THR E CB  1 
ATOM   7861  O OG1 . THR E  1 40  ? 3.456   22.444  40.685  1.00 10.82  ? 46  THR E OG1 1 
ATOM   7862  C CG2 . THR E  1 40  ? 2.083   24.053  41.860  1.00 12.27  ? 46  THR E CG2 1 
ATOM   7863  N N   . ASN E  1 41  ? 1.382   22.038  44.768  1.00 12.53  ? 47  ASN E N   1 
ATOM   7864  C CA  . ASN E  1 41  ? 0.472   22.297  45.875  1.00 12.27  ? 47  ASN E CA  1 
ATOM   7865  C C   . ASN E  1 41  ? 0.346   23.795  46.166  1.00 11.78  ? 47  ASN E C   1 
ATOM   7866  O O   . ASN E  1 41  ? 1.247   24.576  45.850  1.00 11.40  ? 47  ASN E O   1 
ATOM   7867  C CB  . ASN E  1 41  ? 0.985   21.560  47.122  1.00 12.15  ? 47  ASN E CB  1 
ATOM   7868  C CG  . ASN E  1 41  ? 0.049   21.680  48.307  1.00 12.86  ? 47  ASN E CG  1 
ATOM   7869  O OD1 . ASN E  1 41  ? -1.137  21.363  48.211  1.00 16.53  ? 47  ASN E OD1 1 
ATOM   7870  N ND2 . ASN E  1 41  ? 0.581   22.134  49.436  1.00 9.33   ? 47  ASN E ND2 1 
ATOM   7871  N N   . ILE E  1 42  ? -0.779  24.190  46.754  1.00 11.59  ? 48  ILE E N   1 
ATOM   7872  C CA  . ILE E  1 42  ? -0.906  25.524  47.333  1.00 12.53  ? 48  ILE E CA  1 
ATOM   7873  C C   . ILE E  1 42  ? -1.060  25.387  48.847  1.00 12.91  ? 48  ILE E C   1 
ATOM   7874  O O   . ILE E  1 42  ? -2.055  24.835  49.327  1.00 12.96  ? 48  ILE E O   1 
ATOM   7875  C CB  . ILE E  1 42  ? -2.084  26.323  46.726  1.00 12.73  ? 48  ILE E CB  1 
ATOM   7876  C CG1 . ILE E  1 42  ? -1.844  26.564  45.231  1.00 12.80  ? 48  ILE E CG1 1 
ATOM   7877  C CG2 . ILE E  1 42  ? -2.265  27.652  47.465  1.00 13.22  ? 48  ILE E CG2 1 
ATOM   7878  C CD1 . ILE E  1 42  ? -3.063  27.011  44.464  1.00 11.78  ? 48  ILE E CD1 1 
ATOM   7879  N N   . LYS E  1 43  ? -0.065  25.879  49.588  1.00 13.48  ? 49  LYS E N   1 
ATOM   7880  C CA  . LYS E  1 43  ? -0.027  25.741  51.051  1.00 14.06  ? 49  LYS E CA  1 
ATOM   7881  C C   . LYS E  1 43  ? -1.024  26.669  51.750  1.00 14.21  ? 49  LYS E C   1 
ATOM   7882  O O   . LYS E  1 43  ? -0.686  27.351  52.721  1.00 14.09  ? 49  LYS E O   1 
ATOM   7883  C CB  . LYS E  1 43  ? 1.391   25.963  51.594  1.00 14.14  ? 49  LYS E CB  1 
ATOM   7884  C CG  . LYS E  1 43  ? 2.429   24.945  51.116  1.00 18.59  ? 49  LYS E CG  1 
ATOM   7885  C CD  . LYS E  1 43  ? 3.735   25.043  51.910  1.00 22.31  ? 49  LYS E CD  1 
ATOM   7886  C CE  . LYS E  1 43  ? 3.594   24.424  53.304  1.00 25.44  ? 49  LYS E CE  1 
ATOM   7887  N NZ  . LYS E  1 43  ? 4.840   24.535  54.115  1.00 26.30  ? 49  LYS E NZ  1 
ATOM   7888  N N   . LYS E  1 44  ? -2.253  26.678  51.236  1.00 14.42  ? 50  LYS E N   1 
ATOM   7889  C CA  . LYS E  1 44  ? -3.359  27.447  51.793  1.00 14.02  ? 50  LYS E CA  1 
ATOM   7890  C C   . LYS E  1 44  ? -4.677  26.707  51.592  1.00 13.52  ? 50  LYS E C   1 
ATOM   7891  O O   . LYS E  1 44  ? -4.787  25.858  50.708  1.00 13.32  ? 50  LYS E O   1 
ATOM   7892  C CB  . LYS E  1 44  ? -3.441  28.826  51.133  1.00 14.02  ? 50  LYS E CB  1 
ATOM   7893  C CG  . LYS E  1 44  ? -2.760  29.939  51.915  1.00 16.62  ? 50  LYS E CG  1 
ATOM   7894  C CD  . LYS E  1 44  ? -1.355  30.235  51.412  1.00 18.48  ? 50  LYS E CD  1 
ATOM   7895  C CE  . LYS E  1 44  ? -0.719  31.369  52.209  1.00 16.46  ? 50  LYS E CE  1 
ATOM   7896  N NZ  . LYS E  1 44  ? -1.409  32.669  51.975  1.00 15.65  ? 50  LYS E NZ  1 
ATOM   7897  N N   . ILE E  1 45  ? -5.666  27.021  52.425  1.00 13.23  ? 51  ILE E N   1 
ATOM   7898  C CA  . ILE E  1 45  ? -7.039  26.593  52.183  1.00 12.66  ? 51  ILE E CA  1 
ATOM   7899  C C   . ILE E  1 45  ? -7.702  27.674  51.334  1.00 13.13  ? 51  ILE E C   1 
ATOM   7900  O O   . ILE E  1 45  ? -7.999  28.765  51.822  1.00 13.94  ? 51  ILE E O   1 
ATOM   7901  C CB  . ILE E  1 45  ? -7.824  26.334  53.506  1.00 12.41  ? 51  ILE E CB  1 
ATOM   7902  C CG1 . ILE E  1 45  ? -7.149  25.239  54.347  1.00 12.71  ? 51  ILE E CG1 1 
ATOM   7903  C CG2 . ILE E  1 45  ? -9.291  25.981  53.231  1.00 10.16  ? 51  ILE E CG2 1 
ATOM   7904  C CD1 . ILE E  1 45  ? -6.943  23.895  53.633  1.00 12.38  ? 51  ILE E CD1 1 
ATOM   7905  N N   . CYS E  1 46  ? -7.893  27.373  50.053  1.00 13.59  ? 52  CYS E N   1 
ATOM   7906  C CA  . CYS E  1 46  ? -8.486  28.312  49.099  1.00 14.24  ? 52  CYS E CA  1 
ATOM   7907  C C   . CYS E  1 46  ? -9.987  28.469  49.328  1.00 14.42  ? 52  CYS E C   1 
ATOM   7908  O O   . CYS E  1 46  ? -10.756 27.523  49.132  1.00 14.66  ? 52  CYS E O   1 
ATOM   7909  C CB  . CYS E  1 46  ? -8.208  27.855  47.667  1.00 14.15  ? 52  CYS E CB  1 
ATOM   7910  S SG  . CYS E  1 46  ? -6.469  27.929  47.205  1.00 16.32  ? 52  CYS E SG  1 
ATOM   7911  N N   . THR E  1 47  ? -10.395 29.669  49.734  1.00 14.65  ? 53  THR E N   1 
ATOM   7912  C CA  . THR E  1 47  ? -11.774 29.906  50.168  1.00 15.44  ? 53  THR E CA  1 
ATOM   7913  C C   . THR E  1 47  ? -12.586 30.847  49.268  1.00 16.44  ? 53  THR E C   1 
ATOM   7914  O O   . THR E  1 47  ? -13.721 31.197  49.606  1.00 16.58  ? 53  THR E O   1 
ATOM   7915  C CB  . THR E  1 47  ? -11.835 30.417  51.632  1.00 15.01  ? 53  THR E CB  1 
ATOM   7916  O OG1 . THR E  1 47  ? -11.138 31.663  51.742  1.00 14.14  ? 53  THR E OG1 1 
ATOM   7917  C CG2 . THR E  1 47  ? -11.220 29.406  52.589  1.00 15.51  ? 53  THR E CG2 1 
ATOM   7918  N N   . GLN E  1 48  ? -12.020 31.247  48.129  1.00 17.09  ? 54  GLN E N   1 
ATOM   7919  C CA  . GLN E  1 48  ? -12.739 32.109  47.186  1.00 17.91  ? 54  GLN E CA  1 
ATOM   7920  C C   . GLN E  1 48  ? -14.028 31.442  46.707  1.00 17.62  ? 54  GLN E C   1 
ATOM   7921  O O   . GLN E  1 48  ? -14.038 30.248  46.408  1.00 17.42  ? 54  GLN E O   1 
ATOM   7922  C CB  . GLN E  1 48  ? -11.867 32.477  45.983  1.00 18.23  ? 54  GLN E CB  1 
ATOM   7923  C CG  . GLN E  1 48  ? -12.320 33.741  45.254  1.00 19.08  ? 54  GLN E CG  1 
ATOM   7924  C CD  . GLN E  1 48  ? -11.866 33.778  43.813  1.00 23.40  ? 54  GLN E CD  1 
ATOM   7925  O OE1 . GLN E  1 48  ? -12.379 33.040  42.971  1.00 27.32  ? 54  GLN E OE1 1 
ATOM   7926  N NE2 . GLN E  1 48  ? -10.904 34.644  43.517  1.00 24.87  ? 54  GLN E NE2 1 
ATOM   7927  N N   . GLY E  1 49  ? -15.107 32.222  46.653  1.00 18.00  ? 55  GLY E N   1 
ATOM   7928  C CA  . GLY E  1 49  ? -16.417 31.731  46.215  1.00 18.29  ? 55  GLY E CA  1 
ATOM   7929  C C   . GLY E  1 49  ? -17.117 30.872  47.252  1.00 18.48  ? 55  GLY E C   1 
ATOM   7930  O O   . GLY E  1 49  ? -18.213 30.362  47.013  1.00 18.89  ? 55  GLY E O   1 
ATOM   7931  N N   . LYS E  1 50  ? -16.483 30.720  48.411  1.00 18.08  ? 56  LYS E N   1 
ATOM   7932  C CA  . LYS E  1 50  ? -16.995 29.860  49.471  1.00 17.67  ? 56  LYS E CA  1 
ATOM   7933  C C   . LYS E  1 50  ? -17.275 30.631  50.761  1.00 17.26  ? 56  LYS E C   1 
ATOM   7934  O O   . LYS E  1 50  ? -16.846 31.774  50.914  1.00 17.44  ? 56  LYS E O   1 
ATOM   7935  C CB  . LYS E  1 50  ? -16.019 28.708  49.725  1.00 17.35  ? 56  LYS E CB  1 
ATOM   7936  C CG  . LYS E  1 50  ? -16.109 27.604  48.686  1.00 16.05  ? 56  LYS E CG  1 
ATOM   7937  C CD  . LYS E  1 50  ? -14.972 26.609  48.827  1.00 14.43  ? 56  LYS E CD  1 
ATOM   7938  C CE  . LYS E  1 50  ? -15.127 25.460  47.845  1.00 15.02  ? 56  LYS E CE  1 
ATOM   7939  N NZ  . LYS E  1 50  ? -15.327 25.940  46.447  1.00 15.56  ? 56  LYS E NZ  1 
ATOM   7940  N N   . ARG E  1 51  ? -18.015 30.003  51.671  1.00 16.77  ? 57  ARG E N   1 
ATOM   7941  C CA  . ARG E  1 51  ? -18.322 30.592  52.972  1.00 16.53  ? 57  ARG E CA  1 
ATOM   7942  C C   . ARG E  1 51  ? -17.683 29.728  54.062  1.00 15.61  ? 57  ARG E C   1 
ATOM   7943  O O   . ARG E  1 51  ? -18.301 28.782  54.554  1.00 15.00  ? 57  ARG E O   1 
ATOM   7944  C CB  . ARG E  1 51  ? -19.837 30.716  53.168  1.00 17.11  ? 57  ARG E CB  1 
ATOM   7945  C CG  . ARG E  1 51  ? -20.543 31.534  52.083  1.00 19.31  ? 57  ARG E CG  1 
ATOM   7946  C CD  . ARG E  1 51  ? -22.060 31.338  52.087  1.00 23.18  ? 57  ARG E CD  1 
ATOM   7947  N NE  . ARG E  1 51  ? -22.449 29.951  51.827  1.00 24.11  ? 57  ARG E NE  1 
ATOM   7948  C CZ  . ARG E  1 51  ? -23.008 29.141  52.724  1.00 22.93  ? 57  ARG E CZ  1 
ATOM   7949  N NH1 . ARG E  1 51  ? -23.261 29.569  53.954  1.00 23.87  ? 57  ARG E NH1 1 
ATOM   7950  N NH2 . ARG E  1 51  ? -23.317 27.898  52.387  1.00 24.20  ? 57  ARG E NH2 1 
ATOM   7951  N N   . PRO E  1 52  ? -16.428 30.048  54.429  1.00 14.99  ? 58  PRO E N   1 
ATOM   7952  C CA  . PRO E  1 52  ? -15.644 29.213  55.333  1.00 14.74  ? 58  PRO E CA  1 
ATOM   7953  C C   . PRO E  1 52  ? -15.855 29.529  56.811  1.00 14.75  ? 58  PRO E C   1 
ATOM   7954  O O   . PRO E  1 52  ? -16.207 30.656  57.166  1.00 14.73  ? 58  PRO E O   1 
ATOM   7955  C CB  . PRO E  1 52  ? -14.205 29.542  54.940  1.00 15.03  ? 58  PRO E CB  1 
ATOM   7956  C CG  . PRO E  1 52  ? -14.263 30.968  54.464  1.00 14.75  ? 58  PRO E CG  1 
ATOM   7957  C CD  . PRO E  1 52  ? -15.667 31.229  53.973  1.00 14.85  ? 58  PRO E CD  1 
ATOM   7958  N N   . THR E  1 53  ? -15.643 28.522  57.653  1.00 13.98  ? 59  THR E N   1 
ATOM   7959  C CA  . THR E  1 53  ? -15.627 28.705  59.093  1.00 13.11  ? 59  THR E CA  1 
ATOM   7960  C C   . THR E  1 53  ? -14.352 28.068  59.640  1.00 12.87  ? 59  THR E C   1 
ATOM   7961  O O   . THR E  1 53  ? -14.182 26.847  59.587  1.00 12.92  ? 59  THR E O   1 
ATOM   7962  C CB  . THR E  1 53  ? -16.883 28.106  59.759  1.00 13.49  ? 59  THR E CB  1 
ATOM   7963  O OG1 . THR E  1 53  ? -18.054 28.621  59.118  1.00 12.47  ? 59  THR E OG1 1 
ATOM   7964  C CG2 . THR E  1 53  ? -16.935 28.463  61.238  1.00 12.58  ? 59  THR E CG2 1 
ATOM   7965  N N   . ASP E  1 54  ? -13.449 28.911  60.135  1.00 12.42  ? 60  ASP E N   1 
ATOM   7966  C CA  . ASP E  1 54  ? -12.200 28.451  60.728  1.00 11.52  ? 60  ASP E CA  1 
ATOM   7967  C C   . ASP E  1 54  ? -12.387 28.307  62.232  1.00 11.23  ? 60  ASP E C   1 
ATOM   7968  O O   . ASP E  1 54  ? -12.246 29.272  62.986  1.00 11.42  ? 60  ASP E O   1 
ATOM   7969  C CB  . ASP E  1 54  ? -11.053 29.415  60.405  1.00 11.11  ? 60  ASP E CB  1 
ATOM   7970  C CG  . ASP E  1 54  ? -9.684  28.828  60.714  1.00 10.59  ? 60  ASP E CG  1 
ATOM   7971  O OD1 . ASP E  1 54  ? -9.605  27.736  61.320  1.00 8.74   ? 60  ASP E OD1 1 
ATOM   7972  O OD2 . ASP E  1 54  ? -8.677  29.466  60.346  1.00 14.13  ? 60  ASP E OD2 1 
ATOM   7973  N N   . LEU E  1 55  ? -12.701 27.086  62.656  1.00 11.19  ? 61  LEU E N   1 
ATOM   7974  C CA  . LEU E  1 55  ? -13.060 26.804  64.046  1.00 11.00  ? 61  LEU E CA  1 
ATOM   7975  C C   . LEU E  1 55  ? -11.955 27.108  65.063  1.00 10.87  ? 61  LEU E C   1 
ATOM   7976  O O   . LEU E  1 55  ? -12.251 27.420  66.216  1.00 11.21  ? 61  LEU E O   1 
ATOM   7977  C CB  . LEU E  1 55  ? -13.563 25.364  64.193  1.00 10.02  ? 61  LEU E CB  1 
ATOM   7978  C CG  . LEU E  1 55  ? -14.949 25.067  63.608  1.00 11.28  ? 61  LEU E CG  1 
ATOM   7979  C CD1 . LEU E  1 55  ? -15.236 23.579  63.666  1.00 13.29  ? 61  LEU E CD1 1 
ATOM   7980  C CD2 . LEU E  1 55  ? -16.057 25.849  64.319  1.00 6.77   ? 61  LEU E CD2 1 
ATOM   7981  N N   . GLY E  1 56  ? -10.698 27.024  64.631  1.00 10.72  ? 62  GLY E N   1 
ATOM   7982  C CA  . GLY E  1 56  ? -9.551  27.408  65.461  1.00 10.63  ? 62  GLY E CA  1 
ATOM   7983  C C   . GLY E  1 56  ? -9.471  26.691  66.796  1.00 10.60  ? 62  GLY E C   1 
ATOM   7984  O O   . GLY E  1 56  ? -9.356  25.468  66.844  1.00 10.58  ? 62  GLY E O   1 
ATOM   7985  N N   . GLN E  1 57  ? -9.540  27.462  67.881  1.00 10.68  ? 63  GLN E N   1 
ATOM   7986  C CA  . GLN E  1 57  ? -9.480  26.925  69.243  1.00 10.19  ? 63  GLN E CA  1 
ATOM   7987  C C   . GLN E  1 57  ? -10.757 26.187  69.635  1.00 10.85  ? 63  GLN E C   1 
ATOM   7988  O O   . GLN E  1 57  ? -10.771 25.423  70.609  1.00 11.77  ? 63  GLN E O   1 
ATOM   7989  C CB  . GLN E  1 57  ? -9.196  28.043  70.243  1.00 9.49   ? 63  GLN E CB  1 
ATOM   7990  C CG  . GLN E  1 57  ? -7.770  28.564  70.182  1.00 9.38   ? 63  GLN E CG  1 
ATOM   7991  C CD  . GLN E  1 57  ? -7.589  29.870  70.922  1.00 10.57  ? 63  GLN E CD  1 
ATOM   7992  O OE1 . GLN E  1 57  ? -8.342  30.189  71.846  1.00 13.39  ? 63  GLN E OE1 1 
ATOM   7993  N NE2 . GLN E  1 57  ? -6.583  30.638  70.519  1.00 7.47   ? 63  GLN E NE2 1 
ATOM   7994  N N   . CYS E  1 58  ? -11.823 26.423  68.873  1.00 10.23  ? 64  CYS E N   1 
ATOM   7995  C CA  . CYS E  1 58  ? -13.092 25.750  69.092  1.00 10.52  ? 64  CYS E CA  1 
ATOM   7996  C C   . CYS E  1 58  ? -13.134 24.396  68.395  1.00 10.70  ? 64  CYS E C   1 
ATOM   7997  O O   . CYS E  1 58  ? -12.927 24.311  67.183  1.00 11.27  ? 64  CYS E O   1 
ATOM   7998  C CB  . CYS E  1 58  ? -14.245 26.615  68.593  1.00 10.46  ? 64  CYS E CB  1 
ATOM   7999  S SG  . CYS E  1 58  ? -15.813 25.743  68.563  1.00 11.12  ? 64  CYS E SG  1 
ATOM   8000  N N   . GLY E  1 59  ? -13.404 23.344  69.167  1.00 10.47  ? 65  GLY E N   1 
ATOM   8001  C CA  . GLY E  1 59  ? -13.625 22.004  68.615  1.00 8.75   ? 65  GLY E CA  1 
ATOM   8002  C C   . GLY E  1 59  ? -15.037 21.886  68.068  1.00 8.67   ? 65  GLY E C   1 
ATOM   8003  O O   . GLY E  1 59  ? -15.972 22.441  68.642  1.00 8.54   ? 65  GLY E O   1 
ATOM   8004  N N   . LEU E  1 60  ? -15.191 21.156  66.963  1.00 8.46   ? 66  LEU E N   1 
ATOM   8005  C CA  . LEU E  1 60  ? -16.464 21.076  66.241  1.00 7.49   ? 66  LEU E CA  1 
ATOM   8006  C C   . LEU E  1 60  ? -17.656 20.691  67.118  1.00 7.31   ? 66  LEU E C   1 
ATOM   8007  O O   . LEU E  1 60  ? -18.739 21.271  66.992  1.00 8.06   ? 66  LEU E O   1 
ATOM   8008  C CB  . LEU E  1 60  ? -16.349 20.135  65.032  1.00 7.31   ? 66  LEU E CB  1 
ATOM   8009  C CG  . LEU E  1 60  ? -17.572 19.939  64.119  1.00 6.03   ? 66  LEU E CG  1 
ATOM   8010  C CD1 . LEU E  1 60  ? -18.132 21.253  63.569  1.00 6.28   ? 66  LEU E CD1 1 
ATOM   8011  C CD2 . LEU E  1 60  ? -17.223 19.003  62.988  1.00 6.25   ? 66  LEU E CD2 1 
ATOM   8012  N N   . LEU E  1 61  ? -17.455 19.719  68.003  1.00 6.30   ? 67  LEU E N   1 
ATOM   8013  C CA  . LEU E  1 61  ? -18.511 19.280  68.912  1.00 5.57   ? 67  LEU E CA  1 
ATOM   8014  C C   . LEU E  1 61  ? -18.835 20.355  69.944  1.00 6.03   ? 67  LEU E C   1 
ATOM   8015  O O   . LEU E  1 61  ? -19.985 20.486  70.379  1.00 6.68   ? 67  LEU E O   1 
ATOM   8016  C CB  . LEU E  1 61  ? -18.132 17.966  69.599  1.00 4.80   ? 67  LEU E CB  1 
ATOM   8017  C CG  . LEU E  1 61  ? -17.800 16.773  68.694  1.00 3.56   ? 67  LEU E CG  1 
ATOM   8018  C CD1 . LEU E  1 61  ? -17.468 15.538  69.524  1.00 2.14   ? 67  LEU E CD1 1 
ATOM   8019  C CD2 . LEU E  1 61  ? -18.932 16.484  67.717  1.00 2.62   ? 67  LEU E CD2 1 
ATOM   8020  N N   . GLY E  1 62  ? -17.817 21.131  70.316  1.00 5.48   ? 68  GLY E N   1 
ATOM   8021  C CA  . GLY E  1 62  ? -17.990 22.271  71.207  1.00 4.64   ? 68  GLY E CA  1 
ATOM   8022  C C   . GLY E  1 62  ? -19.085 23.235  70.777  1.00 4.51   ? 68  GLY E C   1 
ATOM   8023  O O   . GLY E  1 62  ? -19.702 23.877  71.620  1.00 4.20   ? 68  GLY E O   1 
ATOM   8024  N N   . THR E  1 63  ? -19.340 23.320  69.470  1.00 4.60   ? 69  THR E N   1 
ATOM   8025  C CA  . THR E  1 63  ? -20.373 24.214  68.931  1.00 5.76   ? 69  THR E CA  1 
ATOM   8026  C C   . THR E  1 63  ? -21.773 23.886  69.441  1.00 5.82   ? 69  THR E C   1 
ATOM   8027  O O   . THR E  1 63  ? -22.652 24.744  69.431  1.00 6.41   ? 69  THR E O   1 
ATOM   8028  C CB  . THR E  1 63  ? -20.413 24.219  67.379  1.00 6.34   ? 69  THR E CB  1 
ATOM   8029  O OG1 . THR E  1 63  ? -20.850 22.943  66.898  1.00 7.07   ? 69  THR E OG1 1 
ATOM   8030  C CG2 . THR E  1 63  ? -19.042 24.552  66.790  1.00 7.10   ? 69  THR E CG2 1 
ATOM   8031  N N   . LEU E  1 64  ? -21.971 22.648  69.887  1.00 6.27   ? 70  LEU E N   1 
ATOM   8032  C CA  . LEU E  1 64  ? -23.277 22.185  70.353  1.00 6.68   ? 70  LEU E CA  1 
ATOM   8033  C C   . LEU E  1 64  ? -23.523 22.494  71.823  1.00 7.19   ? 70  LEU E C   1 
ATOM   8034  O O   . LEU E  1 64  ? -24.641 22.830  72.209  1.00 7.76   ? 70  LEU E O   1 
ATOM   8035  C CB  . LEU E  1 64  ? -23.425 20.677  70.134  1.00 6.43   ? 70  LEU E CB  1 
ATOM   8036  C CG  . LEU E  1 64  ? -23.161 20.106  68.743  1.00 5.59   ? 70  LEU E CG  1 
ATOM   8037  C CD1 . LEU E  1 64  ? -23.091 18.598  68.823  1.00 6.60   ? 70  LEU E CD1 1 
ATOM   8038  C CD2 . LEU E  1 64  ? -24.218 20.556  67.749  1.00 4.38   ? 70  LEU E CD2 1 
ATOM   8039  N N   . ILE E  1 65  ? -22.481 22.355  72.637  1.00 6.80   ? 71  ILE E N   1 
ATOM   8040  C CA  . ILE E  1 65  ? -22.603 22.512  74.082  1.00 6.46   ? 71  ILE E CA  1 
ATOM   8041  C C   . ILE E  1 65  ? -22.159 23.903  74.532  1.00 6.56   ? 71  ILE E C   1 
ATOM   8042  O O   . ILE E  1 65  ? -22.764 24.502  75.426  1.00 7.51   ? 71  ILE E O   1 
ATOM   8043  C CB  . ILE E  1 65  ? -21.856 21.384  74.852  1.00 6.34   ? 71  ILE E CB  1 
ATOM   8044  C CG1 . ILE E  1 65  ? -20.388 21.290  74.420  1.00 7.41   ? 71  ILE E CG1 1 
ATOM   8045  C CG2 . ILE E  1 65  ? -22.550 20.046  74.628  1.00 4.87   ? 71  ILE E CG2 1 
ATOM   8046  C CD1 . ILE E  1 65  ? -19.578 20.265  75.184  1.00 7.08   ? 71  ILE E CD1 1 
ATOM   8047  N N   . GLY E  1 66  ? -21.110 24.415  73.897  1.00 5.42   ? 72  GLY E N   1 
ATOM   8048  C CA  . GLY E  1 66  ? -20.676 25.787  74.098  1.00 4.83   ? 72  GLY E CA  1 
ATOM   8049  C C   . GLY E  1 66  ? -19.721 26.052  75.243  1.00 4.89   ? 72  GLY E C   1 
ATOM   8050  O O   . GLY E  1 66  ? -20.088 26.729  76.198  1.00 6.18   ? 72  GLY E O   1 
ATOM   8051  N N   . PRO E  1 67  ? -18.480 25.534  75.157  1.00 4.95   ? 73  PRO E N   1 
ATOM   8052  C CA  . PRO E  1 67  ? -17.434 26.016  76.056  1.00 5.09   ? 73  PRO E CA  1 
ATOM   8053  C C   . PRO E  1 67  ? -17.003 27.418  75.609  1.00 6.06   ? 73  PRO E C   1 
ATOM   8054  O O   . PRO E  1 67  ? -17.367 27.837  74.505  1.00 6.52   ? 73  PRO E O   1 
ATOM   8055  C CB  . PRO E  1 67  ? -16.305 25.013  75.832  1.00 4.94   ? 73  PRO E CB  1 
ATOM   8056  C CG  . PRO E  1 67  ? -16.495 24.558  74.431  1.00 3.90   ? 73  PRO E CG  1 
ATOM   8057  C CD  . PRO E  1 67  ? -17.979 24.474  74.264  1.00 4.96   ? 73  PRO E CD  1 
ATOM   8058  N N   . PRO E  1 68  ? -16.239 28.148  76.445  1.00 6.53   ? 74  PRO E N   1 
ATOM   8059  C CA  . PRO E  1 68  ? -15.865 29.509  76.034  1.00 7.11   ? 74  PRO E CA  1 
ATOM   8060  C C   . PRO E  1 68  ? -15.199 29.603  74.652  1.00 8.04   ? 74  PRO E C   1 
ATOM   8061  O O   . PRO E  1 68  ? -15.428 30.579  73.939  1.00 8.30   ? 74  PRO E O   1 
ATOM   8062  C CB  . PRO E  1 68  ? -14.914 29.954  77.144  1.00 6.98   ? 74  PRO E CB  1 
ATOM   8063  C CG  . PRO E  1 68  ? -15.407 29.213  78.347  1.00 5.37   ? 74  PRO E CG  1 
ATOM   8064  C CD  . PRO E  1 68  ? -15.809 27.861  77.827  1.00 6.06   ? 74  PRO E CD  1 
ATOM   8065  N N   . GLN E  1 69  ? -14.415 28.589  74.274  1.00 9.01   ? 75  GLN E N   1 
ATOM   8066  C CA  . GLN E  1 69  ? -13.725 28.559  72.974  1.00 9.69   ? 75  GLN E CA  1 
ATOM   8067  C C   . GLN E  1 69  ? -14.687 28.632  71.793  1.00 9.78   ? 75  GLN E C   1 
ATOM   8068  O O   . GLN E  1 69  ? -14.300 29.047  70.703  1.00 10.27  ? 75  GLN E O   1 
ATOM   8069  C CB  . GLN E  1 69  ? -12.885 27.285  72.804  1.00 10.00  ? 75  GLN E CB  1 
ATOM   8070  C CG  . GLN E  1 69  ? -12.116 26.820  74.021  1.00 12.45  ? 75  GLN E CG  1 
ATOM   8071  C CD  . GLN E  1 69  ? -12.937 25.912  74.908  1.00 11.09  ? 75  GLN E CD  1 
ATOM   8072  O OE1 . GLN E  1 69  ? -13.449 26.345  75.939  1.00 12.07  ? 75  GLN E OE1 1 
ATOM   8073  N NE2 . GLN E  1 69  ? -13.077 24.649  74.509  1.00 4.94   ? 75  GLN E NE2 1 
ATOM   8074  N N   . CYS E  1 70  ? -15.931 28.219  72.017  1.00 9.60   ? 76  CYS E N   1 
ATOM   8075  C CA  . CYS E  1 70  ? -16.910 28.069  70.944  1.00 9.90   ? 76  CYS E CA  1 
ATOM   8076  C C   . CYS E  1 70  ? -18.066 29.073  71.007  1.00 9.87   ? 76  CYS E C   1 
ATOM   8077  O O   . CYS E  1 70  ? -19.053 28.936  70.273  1.00 10.39  ? 76  CYS E O   1 
ATOM   8078  C CB  . CYS E  1 70  ? -17.451 26.639  70.938  1.00 9.73   ? 76  CYS E CB  1 
ATOM   8079  S SG  . CYS E  1 70  ? -16.207 25.410  70.537  1.00 13.46  ? 76  CYS E SG  1 
ATOM   8080  N N   . ASP E  1 71  ? -17.937 30.079  71.871  1.00 8.96   ? 77  ASP E N   1 
ATOM   8081  C CA  . ASP E  1 71  ? -18.955 31.118  72.018  1.00 8.43   ? 77  ASP E CA  1 
ATOM   8082  C C   . ASP E  1 71  ? -19.314 31.797  70.698  1.00 8.77   ? 77  ASP E C   1 
ATOM   8083  O O   . ASP E  1 71  ? -20.484 32.110  70.455  1.00 8.60   ? 77  ASP E O   1 
ATOM   8084  C CB  . ASP E  1 71  ? -18.500 32.173  73.024  1.00 8.67   ? 77  ASP E CB  1 
ATOM   8085  C CG  . ASP E  1 71  ? -18.791 31.783  74.458  1.00 8.52   ? 77  ASP E CG  1 
ATOM   8086  O OD1 . ASP E  1 71  ? -18.255 32.447  75.368  1.00 8.27   ? 77  ASP E OD1 1 
ATOM   8087  O OD2 . ASP E  1 71  ? -19.559 30.824  74.679  1.00 7.98   ? 77  ASP E OD2 1 
ATOM   8088  N N   . GLN E  1 72  ? -18.306 32.011  69.852  1.00 8.61   ? 78  GLN E N   1 
ATOM   8089  C CA  . GLN E  1 72  ? -18.491 32.713  68.582  1.00 8.96   ? 78  GLN E CA  1 
ATOM   8090  C C   . GLN E  1 72  ? -18.922 31.776  67.454  1.00 8.95   ? 78  GLN E C   1 
ATOM   8091  O O   . GLN E  1 72  ? -19.082 32.205  66.311  1.00 8.89   ? 78  GLN E O   1 
ATOM   8092  C CB  . GLN E  1 72  ? -17.222 33.487  68.194  1.00 9.42   ? 78  GLN E CB  1 
ATOM   8093  C CG  . GLN E  1 72  ? -16.061 32.617  67.701  1.00 12.86  ? 78  GLN E CG  1 
ATOM   8094  C CD  . GLN E  1 72  ? -14.903 33.417  67.123  1.00 12.80  ? 78  GLN E CD  1 
ATOM   8095  O OE1 . GLN E  1 72  ? -15.098 34.393  66.397  1.00 13.30  ? 78  GLN E OE1 1 
ATOM   8096  N NE2 . GLN E  1 72  ? -13.686 32.995  67.437  1.00 15.79  ? 78  GLN E NE2 1 
ATOM   8097  N N   . PHE E  1 73  ? -19.103 30.498  67.778  1.00 8.97   ? 79  PHE E N   1 
ATOM   8098  C CA  . PHE E  1 73  ? -19.567 29.521  66.795  1.00 8.30   ? 79  PHE E CA  1 
ATOM   8099  C C   . PHE E  1 73  ? -20.783 28.746  67.284  1.00 7.37   ? 79  PHE E C   1 
ATOM   8100  O O   . PHE E  1 73  ? -21.064 27.663  66.784  1.00 7.48   ? 79  PHE E O   1 
ATOM   8101  C CB  . PHE E  1 73  ? -18.444 28.549  66.401  1.00 8.45   ? 79  PHE E CB  1 
ATOM   8102  C CG  . PHE E  1 73  ? -17.223 29.218  65.826  1.00 9.95   ? 79  PHE E CG  1 
ATOM   8103  C CD1 . PHE E  1 73  ? -15.997 29.126  66.477  1.00 11.37  ? 79  PHE E CD1 1 
ATOM   8104  C CD2 . PHE E  1 73  ? -17.294 29.933  64.633  1.00 11.39  ? 79  PHE E CD2 1 
ATOM   8105  C CE1 . PHE E  1 73  ? -14.860 29.733  65.952  1.00 10.14  ? 79  PHE E CE1 1 
ATOM   8106  C CE2 . PHE E  1 73  ? -16.161 30.548  64.102  1.00 10.90  ? 79  PHE E CE2 1 
ATOM   8107  C CZ  . PHE E  1 73  ? -14.943 30.445  64.763  1.00 9.44   ? 79  PHE E CZ  1 
ATOM   8108  N N   . LEU E  1 74  ? -21.505 29.299  68.257  1.00 7.16   ? 80  LEU E N   1 
ATOM   8109  C CA  . LEU E  1 74  ? -22.738 28.675  68.750  1.00 7.05   ? 80  LEU E CA  1 
ATOM   8110  C C   . LEU E  1 74  ? -23.748 28.486  67.626  1.00 7.27   ? 80  LEU E C   1 
ATOM   8111  O O   . LEU E  1 74  ? -24.442 27.478  67.561  1.00 7.77   ? 80  LEU E O   1 
ATOM   8112  C CB  . LEU E  1 74  ? -23.354 29.496  69.885  1.00 6.37   ? 80  LEU E CB  1 
ATOM   8113  C CG  . LEU E  1 74  ? -22.607 29.531  71.220  1.00 6.11   ? 80  LEU E CG  1 
ATOM   8114  C CD1 . LEU E  1 74  ? -23.411 30.307  72.245  1.00 3.23   ? 80  LEU E CD1 1 
ATOM   8115  C CD2 . LEU E  1 74  ? -22.291 28.123  71.731  1.00 5.76   ? 80  LEU E CD2 1 
ATOM   8116  N N   . GLU E  1 75  ? -23.819 29.478  66.750  1.00 8.15   ? 81  GLU E N   1 
ATOM   8117  C CA  . GLU E  1 75  ? -24.562 29.386  65.509  1.00 9.13   ? 81  GLU E CA  1 
ATOM   8118  C C   . GLU E  1 75  ? -23.629 29.908  64.440  1.00 9.63   ? 81  GLU E C   1 
ATOM   8119  O O   . GLU E  1 75  ? -22.892 30.868  64.671  1.00 10.69  ? 81  GLU E O   1 
ATOM   8120  C CB  . GLU E  1 75  ? -25.811 30.260  65.553  1.00 9.15   ? 81  GLU E CB  1 
ATOM   8121  C CG  . GLU E  1 75  ? -26.878 29.791  66.516  1.00 10.42  ? 81  GLU E CG  1 
ATOM   8122  C CD  . GLU E  1 75  ? -28.044 30.750  66.587  1.00 10.49  ? 81  GLU E CD  1 
ATOM   8123  O OE1 . GLU E  1 75  ? -29.151 30.374  66.158  1.00 12.04  ? 81  GLU E OE1 1 
ATOM   8124  O OE2 . GLU E  1 75  ? -27.851 31.885  67.063  1.00 13.65  ? 81  GLU E OE2 1 
ATOM   8125  N N   . PHE E  1 76  ? -23.648 29.261  63.282  1.00 9.75   ? 82  PHE E N   1 
ATOM   8126  C CA  . PHE E  1 76  ? -22.800 29.648  62.164  1.00 10.31  ? 82  PHE E CA  1 
ATOM   8127  C C   . PHE E  1 76  ? -23.319 29.014  60.886  1.00 11.21  ? 82  PHE E C   1 
ATOM   8128  O O   . PHE E  1 76  ? -23.969 27.963  60.924  1.00 11.32  ? 82  PHE E O   1 
ATOM   8129  C CB  . PHE E  1 76  ? -21.327 29.269  62.413  1.00 10.03  ? 82  PHE E CB  1 
ATOM   8130  C CG  . PHE E  1 76  ? -21.058 27.785  62.402  1.00 10.99  ? 82  PHE E CG  1 
ATOM   8131  C CD1 . PHE E  1 76  ? -20.594 27.157  61.247  1.00 13.11  ? 82  PHE E CD1 1 
ATOM   8132  C CD2 . PHE E  1 76  ? -21.254 27.016  63.545  1.00 11.57  ? 82  PHE E CD2 1 
ATOM   8133  C CE1 . PHE E  1 76  ? -20.342 25.783  61.225  1.00 10.52  ? 82  PHE E CE1 1 
ATOM   8134  C CE2 . PHE E  1 76  ? -21.000 25.645  63.536  1.00 11.96  ? 82  PHE E CE2 1 
ATOM   8135  C CZ  . PHE E  1 76  ? -20.544 25.028  62.369  1.00 11.44  ? 82  PHE E CZ  1 
ATOM   8136  N N   . SER E  1 77  ? -23.036 29.668  59.764  1.00 11.84  ? 83  SER E N   1 
ATOM   8137  C CA  . SER E  1 77  ? -23.437 29.180  58.453  1.00 12.04  ? 83  SER E CA  1 
ATOM   8138  C C   . SER E  1 77  ? -22.201 29.022  57.576  1.00 12.73  ? 83  SER E C   1 
ATOM   8139  O O   . SER E  1 77  ? -21.404 29.956  57.440  1.00 13.22  ? 83  SER E O   1 
ATOM   8140  C CB  . SER E  1 77  ? -24.434 30.144  57.815  1.00 11.45  ? 83  SER E CB  1 
ATOM   8141  O OG  . SER E  1 77  ? -25.081 29.543  56.713  1.00 11.79  ? 83  SER E OG  1 
ATOM   8142  N N   . SER E  1 78  ? -22.036 27.837  56.994  1.00 12.98  ? 84  SER E N   1 
ATOM   8143  C CA  . SER E  1 78  ? -20.835 27.531  56.227  1.00 13.77  ? 84  SER E CA  1 
ATOM   8144  C C   . SER E  1 78  ? -21.050 26.483  55.141  1.00 13.78  ? 84  SER E C   1 
ATOM   8145  O O   . SER E  1 78  ? -21.959 25.657  55.230  1.00 13.58  ? 84  SER E O   1 
ATOM   8146  C CB  . SER E  1 78  ? -19.724 27.060  57.167  1.00 14.08  ? 84  SER E CB  1 
ATOM   8147  O OG  . SER E  1 78  ? -18.496 26.912  56.473  1.00 17.67  ? 84  SER E OG  1 
ATOM   8148  N N   . ASP E  1 79  ? -20.203 26.534  54.116  1.00 13.99  ? 85  ASP E N   1 
ATOM   8149  C CA  . ASP E  1 79  ? -20.096 25.446  53.143  1.00 14.45  ? 85  ASP E CA  1 
ATOM   8150  C C   . ASP E  1 79  ? -18.719 24.779  53.222  1.00 13.73  ? 85  ASP E C   1 
ATOM   8151  O O   . ASP E  1 79  ? -18.445 23.810  52.514  1.00 14.05  ? 85  ASP E O   1 
ATOM   8152  C CB  . ASP E  1 79  ? -20.433 25.908  51.713  1.00 14.72  ? 85  ASP E CB  1 
ATOM   8153  C CG  . ASP E  1 79  ? -19.518 27.018  51.203  1.00 17.91  ? 85  ASP E CG  1 
ATOM   8154  O OD1 . ASP E  1 79  ? -18.402 27.204  51.739  1.00 18.71  ? 85  ASP E OD1 1 
ATOM   8155  O OD2 . ASP E  1 79  ? -19.924 27.705  50.242  1.00 22.14  ? 85  ASP E OD2 1 
ATOM   8156  N N   . LEU E  1 80  ? -17.867 25.301  54.101  1.00 12.79  ? 86  LEU E N   1 
ATOM   8157  C CA  . LEU E  1 80  ? -16.525 24.762  54.293  1.00 12.42  ? 86  LEU E CA  1 
ATOM   8158  C C   . LEU E  1 80  ? -16.075 24.900  55.752  1.00 11.90  ? 86  LEU E C   1 
ATOM   8159  O O   . LEU E  1 80  ? -15.598 25.954  56.170  1.00 12.47  ? 86  LEU E O   1 
ATOM   8160  C CB  . LEU E  1 80  ? -15.539 25.460  53.350  1.00 12.41  ? 86  LEU E CB  1 
ATOM   8161  C CG  . LEU E  1 80  ? -14.192 24.781  53.105  1.00 13.48  ? 86  LEU E CG  1 
ATOM   8162  C CD1 . LEU E  1 80  ? -14.352 23.555  52.211  1.00 12.90  ? 86  LEU E CD1 1 
ATOM   8163  C CD2 . LEU E  1 80  ? -13.221 25.771  52.492  1.00 12.96  ? 86  LEU E CD2 1 
ATOM   8164  N N   . ILE E  1 81  ? -16.234 23.827  56.519  1.00 10.88  ? 87  ILE E N   1 
ATOM   8165  C CA  . ILE E  1 81  ? -15.872 23.825  57.931  1.00 10.16  ? 87  ILE E CA  1 
ATOM   8166  C C   . ILE E  1 81  ? -14.432 23.335  58.110  1.00 10.72  ? 87  ILE E C   1 
ATOM   8167  O O   . ILE E  1 81  ? -14.103 22.201  57.737  1.00 11.08  ? 87  ILE E O   1 
ATOM   8168  C CB  . ILE E  1 81  ? -16.860 22.962  58.755  1.00 10.14  ? 87  ILE E CB  1 
ATOM   8169  C CG1 . ILE E  1 81  ? -18.272 23.559  58.681  1.00 8.19   ? 87  ILE E CG1 1 
ATOM   8170  C CG2 . ILE E  1 81  ? -16.393 22.827  60.202  1.00 8.91   ? 87  ILE E CG2 1 
ATOM   8171  C CD1 . ILE E  1 81  ? -19.359 22.682  59.281  1.00 8.01   ? 87  ILE E CD1 1 
ATOM   8172  N N   . ILE E  1 82  ? -13.579 24.193  58.673  1.00 10.51  ? 88  ILE E N   1 
ATOM   8173  C CA  . ILE E  1 82  ? -12.165 23.852  58.872  1.00 10.93  ? 88  ILE E CA  1 
ATOM   8174  C C   . ILE E  1 82  ? -11.823 23.563  60.336  1.00 11.05  ? 88  ILE E C   1 
ATOM   8175  O O   . ILE E  1 82  ? -11.987 24.421  61.205  1.00 12.30  ? 88  ILE E O   1 
ATOM   8176  C CB  . ILE E  1 82  ? -11.198 24.935  58.311  1.00 10.95  ? 88  ILE E CB  1 
ATOM   8177  C CG1 . ILE E  1 82  ? -11.607 25.374  56.902  1.00 11.25  ? 88  ILE E CG1 1 
ATOM   8178  C CG2 . ILE E  1 82  ? -9.764  24.416  58.289  1.00 10.77  ? 88  ILE E CG2 1 
ATOM   8179  C CD1 . ILE E  1 82  ? -12.260 26.734  56.839  1.00 10.29  ? 88  ILE E CD1 1 
ATOM   8180  N N   . GLU E  1 83  ? -11.344 22.348  60.588  1.00 10.47  ? 89  GLU E N   1 
ATOM   8181  C CA  . GLU E  1 83  ? -10.919 21.924  61.920  1.00 10.40  ? 89  GLU E CA  1 
ATOM   8182  C C   . GLU E  1 83  ? -9.430  22.166  62.107  1.00 10.56  ? 89  GLU E C   1 
ATOM   8183  O O   . GLU E  1 83  ? -8.649  22.006  61.170  1.00 10.80  ? 89  GLU E O   1 
ATOM   8184  C CB  . GLU E  1 83  ? -11.215 20.442  62.133  1.00 10.20  ? 89  GLU E CB  1 
ATOM   8185  C CG  . GLU E  1 83  ? -12.672 20.114  62.410  1.00 12.07  ? 89  GLU E CG  1 
ATOM   8186  C CD  . GLU E  1 83  ? -12.877 18.641  62.719  1.00 17.01  ? 89  GLU E CD  1 
ATOM   8187  O OE1 . GLU E  1 83  ? -13.438 18.331  63.791  1.00 17.63  ? 89  GLU E OE1 1 
ATOM   8188  O OE2 . GLU E  1 83  ? -12.467 17.790  61.897  1.00 18.52  ? 89  GLU E OE2 1 
ATOM   8189  N N   . ARG E  1 84  ? -9.041  22.540  63.323  1.00 10.48  ? 90  ARG E N   1 
ATOM   8190  C CA  . ARG E  1 84  ? -7.638  22.796  63.636  1.00 10.56  ? 90  ARG E CA  1 
ATOM   8191  C C   . ARG E  1 84  ? -7.153  21.928  64.790  1.00 11.38  ? 90  ARG E C   1 
ATOM   8192  O O   . ARG E  1 84  ? -7.921  21.608  65.703  1.00 11.40  ? 90  ARG E O   1 
ATOM   8193  C CB  . ARG E  1 84  ? -7.421  24.274  63.969  1.00 10.64  ? 90  ARG E CB  1 
ATOM   8194  C CG  . ARG E  1 84  ? -7.885  25.253  62.898  1.00 9.01   ? 90  ARG E CG  1 
ATOM   8195  C CD  . ARG E  1 84  ? -7.089  25.112  61.623  1.00 7.93   ? 90  ARG E CD  1 
ATOM   8196  N NE  . ARG E  1 84  ? -7.305  26.248  60.735  1.00 10.88  ? 90  ARG E NE  1 
ATOM   8197  C CZ  . ARG E  1 84  ? -6.707  26.411  59.559  1.00 11.58  ? 90  ARG E CZ  1 
ATOM   8198  N NH1 . ARG E  1 84  ? -5.847  25.506  59.107  1.00 13.17  ? 90  ARG E NH1 1 
ATOM   8199  N NH2 . ARG E  1 84  ? -6.974  27.487  58.832  1.00 12.89  ? 90  ARG E NH2 1 
ATOM   8200  N N   . ARG E  1 85  ? -5.868  21.574  64.750  1.00 11.69  ? 91  ARG E N   1 
ATOM   8201  C CA  . ARG E  1 85  ? -5.252  20.699  65.749  1.00 12.63  ? 91  ARG E CA  1 
ATOM   8202  C C   . ARG E  1 85  ? -5.478  21.162  67.189  1.00 12.62  ? 91  ARG E C   1 
ATOM   8203  O O   . ARG E  1 85  ? -5.636  20.336  68.092  1.00 13.15  ? 91  ARG E O   1 
ATOM   8204  C CB  . ARG E  1 85  ? -3.753  20.522  65.460  1.00 13.35  ? 91  ARG E CB  1 
ATOM   8205  C CG  . ARG E  1 85  ? -2.961  19.802  66.554  1.00 17.26  ? 91  ARG E CG  1 
ATOM   8206  C CD  . ARG E  1 85  ? -1.660  19.193  66.034  1.00 24.84  ? 91  ARG E CD  1 
ATOM   8207  N NE  . ARG E  1 85  ? -1.821  17.781  65.683  1.00 28.93  ? 91  ARG E NE  1 
ATOM   8208  C CZ  . ARG E  1 85  ? -1.854  17.302  64.440  1.00 31.81  ? 91  ARG E CZ  1 
ATOM   8209  N NH1 . ARG E  1 85  ? -1.726  18.113  63.394  1.00 32.88  ? 91  ARG E NH1 1 
ATOM   8210  N NH2 . ARG E  1 85  ? -2.011  16.000  64.244  1.00 32.11  ? 91  ARG E NH2 1 
ATOM   8211  N N   . GLU E  1 86  ? -5.512  22.477  67.393  1.00 11.96  ? 92  GLU E N   1 
ATOM   8212  C CA  . GLU E  1 86  ? -5.647  23.039  68.734  1.00 11.64  ? 92  GLU E CA  1 
ATOM   8213  C C   . GLU E  1 86  ? -7.096  23.159  69.215  1.00 11.93  ? 92  GLU E C   1 
ATOM   8214  O O   . GLU E  1 86  ? -7.341  23.630  70.324  1.00 12.81  ? 92  GLU E O   1 
ATOM   8215  C CB  . GLU E  1 86  ? -4.908  24.384  68.846  1.00 11.07  ? 92  GLU E CB  1 
ATOM   8216  C CG  . GLU E  1 86  ? -5.538  25.562  68.098  1.00 12.35  ? 92  GLU E CG  1 
ATOM   8217  C CD  . GLU E  1 86  ? -5.220  25.602  66.601  1.00 14.80  ? 92  GLU E CD  1 
ATOM   8218  O OE1 . GLU E  1 86  ? -4.431  24.766  66.105  1.00 13.60  ? 92  GLU E OE1 1 
ATOM   8219  O OE2 . GLU E  1 86  ? -5.768  26.492  65.916  1.00 15.38  ? 92  GLU E OE2 1 
ATOM   8220  N N   . GLY E  1 87  ? -8.047  22.722  68.394  1.00 12.28  ? 93  GLY E N   1 
ATOM   8221  C CA  . GLY E  1 87  ? -9.464  22.771  68.764  1.00 12.94  ? 93  GLY E CA  1 
ATOM   8222  C C   . GLY E  1 87  ? -9.831  21.776  69.850  1.00 13.25  ? 93  GLY E C   1 
ATOM   8223  O O   . GLY E  1 87  ? -9.417  20.618  69.797  1.00 13.84  ? 93  GLY E O   1 
ATOM   8224  N N   . THR E  1 88  ? -10.592 22.233  70.844  1.00 13.28  ? 94  THR E N   1 
ATOM   8225  C CA  . THR E  1 88  ? -11.096 21.357  71.911  1.00 14.18  ? 94  THR E CA  1 
ATOM   8226  C C   . THR E  1 88  ? -12.604 21.509  72.073  1.00 14.77  ? 94  THR E C   1 
ATOM   8227  O O   . THR E  1 88  ? -13.151 22.591  71.852  1.00 14.44  ? 94  THR E O   1 
ATOM   8228  C CB  . THR E  1 88  ? -10.420 21.622  73.277  1.00 14.51  ? 94  THR E CB  1 
ATOM   8229  O OG1 . THR E  1 88  ? -10.564 23.005  73.637  1.00 18.06  ? 94  THR E OG1 1 
ATOM   8230  C CG2 . THR E  1 88  ? -8.941  21.242  73.244  1.00 13.01  ? 94  THR E CG2 1 
ATOM   8231  N N   . ASP E  1 89  ? -13.265 20.421  72.470  1.00 15.66  ? 95  ASP E N   1 
ATOM   8232  C CA  . ASP E  1 89  ? -14.726 20.382  72.572  1.00 15.99  ? 95  ASP E CA  1 
ATOM   8233  C C   . ASP E  1 89  ? -15.249 20.765  73.950  1.00 16.35  ? 95  ASP E C   1 
ATOM   8234  O O   . ASP E  1 89  ? -16.370 21.258  74.076  1.00 16.37  ? 95  ASP E O   1 
ATOM   8235  C CB  . ASP E  1 89  ? -15.251 18.987  72.227  1.00 16.19  ? 95  ASP E CB  1 
ATOM   8236  C CG  . ASP E  1 89  ? -14.776 18.495  70.876  1.00 17.70  ? 95  ASP E CG  1 
ATOM   8237  O OD1 . ASP E  1 89  ? -14.599 19.315  69.953  1.00 19.16  ? 95  ASP E OD1 1 
ATOM   8238  O OD2 . ASP E  1 89  ? -14.585 17.271  70.739  1.00 21.76  ? 95  ASP E OD2 1 
ATOM   8239  N N   . ILE E  1 90  ? -14.433 20.534  74.975  1.00 16.78  ? 96  ILE E N   1 
ATOM   8240  C CA  . ILE E  1 90  ? -14.881 20.617  76.364  1.00 16.95  ? 96  ILE E CA  1 
ATOM   8241  C C   . ILE E  1 90  ? -14.079 21.624  77.186  1.00 17.37  ? 96  ILE E C   1 
ATOM   8242  O O   . ILE E  1 90  ? -12.978 22.012  76.795  1.00 18.28  ? 96  ILE E O   1 
ATOM   8243  C CB  . ILE E  1 90  ? -14.831 19.213  77.052  1.00 17.21  ? 96  ILE E CB  1 
ATOM   8244  C CG1 . ILE E  1 90  ? -13.500 18.496  76.783  1.00 16.52  ? 96  ILE E CG1 1 
ATOM   8245  C CG2 . ILE E  1 90  ? -15.970 18.327  76.567  1.00 15.23  ? 96  ILE E CG2 1 
ATOM   8246  C CD1 . ILE E  1 90  ? -12.400 18.799  77.781  1.00 15.54  ? 96  ILE E CD1 1 
ATOM   8247  N N   . CYS E  1 91  ? -14.644 22.051  78.313  1.00 17.09  ? 97  CYS E N   1 
ATOM   8248  C CA  . CYS E  1 91  ? -13.885 22.785  79.328  1.00 16.67  ? 97  CYS E CA  1 
ATOM   8249  C C   . CYS E  1 91  ? -13.790 21.964  80.614  1.00 16.42  ? 97  CYS E C   1 
ATOM   8250  O O   . CYS E  1 91  ? -12.708 21.814  81.187  1.00 16.36  ? 97  CYS E O   1 
ATOM   8251  C CB  . CYS E  1 91  ? -14.473 24.176  79.589  1.00 16.51  ? 97  CYS E CB  1 
ATOM   8252  S SG  . CYS E  1 91  ? -16.268 24.264  79.699  1.00 18.83  ? 97  CYS E SG  1 
ATOM   8253  N N   . TYR E  1 92  ? -14.924 21.425  81.052  1.00 16.31  ? 98  TYR E N   1 
ATOM   8254  C CA  . TYR E  1 92  ? -14.957 20.464  82.149  1.00 16.41  ? 98  TYR E CA  1 
ATOM   8255  C C   . TYR E  1 92  ? -14.670 19.067  81.591  1.00 16.09  ? 98  TYR E C   1 
ATOM   8256  O O   . TYR E  1 92  ? -15.277 18.670  80.595  1.00 16.92  ? 98  TYR E O   1 
ATOM   8257  C CB  . TYR E  1 92  ? -16.328 20.491  82.825  1.00 16.41  ? 98  TYR E CB  1 
ATOM   8258  C CG  . TYR E  1 92  ? -16.364 19.907  84.222  1.00 18.83  ? 98  TYR E CG  1 
ATOM   8259  C CD1 . TYR E  1 92  ? -16.086 20.699  85.335  1.00 21.07  ? 98  TYR E CD1 1 
ATOM   8260  C CD2 . TYR E  1 92  ? -16.696 18.570  84.431  1.00 20.87  ? 98  TYR E CD2 1 
ATOM   8261  C CE1 . TYR E  1 92  ? -16.127 20.173  86.622  1.00 23.20  ? 98  TYR E CE1 1 
ATOM   8262  C CE2 . TYR E  1 92  ? -16.740 18.032  85.714  1.00 22.85  ? 98  TYR E CE2 1 
ATOM   8263  C CZ  . TYR E  1 92  ? -16.456 18.840  86.804  1.00 25.11  ? 98  TYR E CZ  1 
ATOM   8264  O OH  . TYR E  1 92  ? -16.495 18.311  88.076  1.00 27.87  ? 98  TYR E OH  1 
ATOM   8265  N N   . PRO E  1 93  ? -13.745 18.317  82.223  1.00 15.91  ? 99  PRO E N   1 
ATOM   8266  C CA  . PRO E  1 93  ? -13.379 16.974  81.750  1.00 15.77  ? 99  PRO E CA  1 
ATOM   8267  C C   . PRO E  1 93  ? -14.591 16.102  81.414  1.00 15.80  ? 99  PRO E C   1 
ATOM   8268  O O   . PRO E  1 93  ? -15.619 16.171  82.093  1.00 15.43  ? 99  PRO E O   1 
ATOM   8269  C CB  . PRO E  1 93  ? -12.591 16.376  82.929  1.00 15.74  ? 99  PRO E CB  1 
ATOM   8270  C CG  . PRO E  1 93  ? -12.720 17.364  84.061  1.00 15.30  ? 99  PRO E CG  1 
ATOM   8271  C CD  . PRO E  1 93  ? -12.991 18.686  83.432  1.00 16.15  ? 99  PRO E CD  1 
ATOM   8272  N N   . GLY E  1 94  ? -14.463 15.305  80.358  1.00 16.07  ? 100 GLY E N   1 
ATOM   8273  C CA  . GLY E  1 94  ? -15.564 14.486  79.863  1.00 16.35  ? 100 GLY E CA  1 
ATOM   8274  C C   . GLY E  1 94  ? -15.525 14.365  78.353  1.00 16.99  ? 100 GLY E C   1 
ATOM   8275  O O   . GLY E  1 94  ? -14.825 15.127  77.682  1.00 16.87  ? 100 GLY E O   1 
ATOM   8276  N N   . ARG E  1 95  ? -16.286 13.409  77.821  1.00 17.15  ? 101 ARG E N   1 
ATOM   8277  C CA  . ARG E  1 95  ? -16.269 13.110  76.395  1.00 17.22  ? 101 ARG E CA  1 
ATOM   8278  C C   . ARG E  1 95  ? -17.683 12.954  75.835  1.00 16.96  ? 101 ARG E C   1 
ATOM   8279  O O   . ARG E  1 95  ? -18.639 12.766  76.589  1.00 17.44  ? 101 ARG E O   1 
ATOM   8280  C CB  . ARG E  1 95  ? -15.421 11.851  76.130  1.00 17.80  ? 101 ARG E CB  1 
ATOM   8281  C CG  . ARG E  1 95  ? -16.195 10.532  76.043  1.00 20.01  ? 101 ARG E CG  1 
ATOM   8282  C CD  . ARG E  1 95  ? -15.374 9.349   76.541  1.00 25.50  ? 101 ARG E CD  1 
ATOM   8283  N NE  . ARG E  1 95  ? -15.740 8.996   77.913  1.00 30.77  ? 101 ARG E NE  1 
ATOM   8284  C CZ  . ARG E  1 95  ? -15.070 8.151   78.693  1.00 33.78  ? 101 ARG E CZ  1 
ATOM   8285  N NH1 . ARG E  1 95  ? -13.965 7.551   78.258  1.00 34.94  ? 101 ARG E NH1 1 
ATOM   8286  N NH2 . ARG E  1 95  ? -15.506 7.915   79.926  1.00 34.51  ? 101 ARG E NH2 1 
ATOM   8287  N N   . PHE E  1 96  ? -17.804 13.050  74.513  1.00 16.54  ? 102 PHE E N   1 
ATOM   8288  C CA  . PHE E  1 96  ? -19.057 12.765  73.820  1.00 15.82  ? 102 PHE E CA  1 
ATOM   8289  C C   . PHE E  1 96  ? -19.145 11.288  73.510  1.00 15.79  ? 102 PHE E C   1 
ATOM   8290  O O   . PHE E  1 96  ? -18.132 10.648  73.231  1.00 16.67  ? 102 PHE E O   1 
ATOM   8291  C CB  . PHE E  1 96  ? -19.126 13.523  72.497  1.00 16.02  ? 102 PHE E CB  1 
ATOM   8292  C CG  . PHE E  1 96  ? -19.576 14.948  72.624  1.00 13.95  ? 102 PHE E CG  1 
ATOM   8293  C CD1 . PHE E  1 96  ? -18.696 15.936  73.066  1.00 10.60  ? 102 PHE E CD1 1 
ATOM   8294  C CD2 . PHE E  1 96  ? -20.870 15.309  72.267  1.00 7.93   ? 102 PHE E CD2 1 
ATOM   8295  C CE1 . PHE E  1 96  ? -19.110 17.260  73.173  1.00 10.38  ? 102 PHE E CE1 1 
ATOM   8296  C CE2 . PHE E  1 96  ? -21.293 16.629  72.366  1.00 8.79   ? 102 PHE E CE2 1 
ATOM   8297  C CZ  . PHE E  1 96  ? -20.411 17.608  72.818  1.00 8.90   ? 102 PHE E CZ  1 
ATOM   8298  N N   . THR E  1 97  ? -20.360 10.750  73.545  1.00 15.62  ? 103 THR E N   1 
ATOM   8299  C CA  . THR E  1 97  ? -20.609 9.388   73.094  1.00 15.39  ? 103 THR E CA  1 
ATOM   8300  C C   . THR E  1 97  ? -20.647 9.372   71.564  1.00 15.12  ? 103 THR E C   1 
ATOM   8301  O O   . THR E  1 97  ? -21.309 10.208  70.941  1.00 14.47  ? 103 THR E O   1 
ATOM   8302  C CB  . THR E  1 97  ? -21.915 8.835   73.688  1.00 15.18  ? 103 THR E CB  1 
ATOM   8303  O OG1 . THR E  1 97  ? -21.849 8.918   75.114  1.00 15.94  ? 103 THR E OG1 1 
ATOM   8304  C CG2 . THR E  1 97  ? -22.122 7.379   73.298  1.00 17.62  ? 103 THR E CG2 1 
ATOM   8305  N N   . ASN E  1 98  ? -19.922 8.420   70.976  1.00 15.22  ? 104 ASN E N   1 
ATOM   8306  C CA  . ASN E  1 98  ? -19.779 8.302   69.522  1.00 15.91  ? 104 ASN E CA  1 
ATOM   8307  C C   . ASN E  1 98  ? -19.370 9.632   68.893  1.00 15.28  ? 104 ASN E C   1 
ATOM   8308  O O   . ASN E  1 98  ? -20.020 10.131  67.969  1.00 14.95  ? 104 ASN E O   1 
ATOM   8309  C CB  . ASN E  1 98  ? -21.056 7.734   68.879  1.00 16.39  ? 104 ASN E CB  1 
ATOM   8310  C CG  . ASN E  1 98  ? -21.454 6.387   69.462  1.00 18.76  ? 104 ASN E CG  1 
ATOM   8311  O OD1 . ASN E  1 98  ? -22.502 6.261   70.091  1.00 23.07  ? 104 ASN E OD1 1 
ATOM   8312  N ND2 . ASN E  1 98  ? -20.609 5.378   69.270  1.00 21.37  ? 104 ASN E ND2 1 
ATOM   8313  N N   . GLU E  1 99  ? -18.280 10.189  69.417  1.00 14.86  ? 105 GLU E N   1 
ATOM   8314  C CA  . GLU E  1 99  ? -17.804 11.523  69.048  1.00 14.57  ? 105 GLU E CA  1 
ATOM   8315  C C   . GLU E  1 99  ? -17.546 11.704  67.554  1.00 13.96  ? 105 GLU E C   1 
ATOM   8316  O O   . GLU E  1 99  ? -17.889 12.741  66.981  1.00 14.24  ? 105 GLU E O   1 
ATOM   8317  C CB  . GLU E  1 99  ? -16.558 11.902  69.862  1.00 15.00  ? 105 GLU E CB  1 
ATOM   8318  C CG  . GLU E  1 99  ? -15.477 10.832  69.933  1.00 15.99  ? 105 GLU E CG  1 
ATOM   8319  C CD  . GLU E  1 99  ? -14.267 11.282  70.727  1.00 17.75  ? 105 GLU E CD  1 
ATOM   8320  O OE1 . GLU E  1 99  ? -13.437 12.034  70.173  1.00 18.65  ? 105 GLU E OE1 1 
ATOM   8321  O OE2 . GLU E  1 99  ? -14.142 10.877  71.902  1.00 18.18  ? 105 GLU E OE2 1 
ATOM   8322  N N   . GLU E  1 100 ? -16.955 10.692  66.927  1.00 13.12  ? 106 GLU E N   1 
ATOM   8323  C CA  . GLU E  1 100 ? -16.597 10.799  65.522  1.00 12.23  ? 106 GLU E CA  1 
ATOM   8324  C C   . GLU E  1 100 ? -17.815 10.778  64.606  1.00 11.78  ? 106 GLU E C   1 
ATOM   8325  O O   . GLU E  1 100 ? -17.852 11.504  63.618  1.00 11.89  ? 106 GLU E O   1 
ATOM   8326  C CB  . GLU E  1 100 ? -15.572 9.738   65.121  1.00 11.81  ? 106 GLU E CB  1 
ATOM   8327  C CG  . GLU E  1 100 ? -14.693 10.151  63.936  1.00 12.74  ? 106 GLU E CG  1 
ATOM   8328  C CD  . GLU E  1 100 ? -14.020 11.507  64.125  1.00 14.09  ? 106 GLU E CD  1 
ATOM   8329  O OE1 . GLU E  1 100 ? -13.375 11.728  65.174  1.00 15.24  ? 106 GLU E OE1 1 
ATOM   8330  O OE2 . GLU E  1 100 ? -14.131 12.354  63.216  1.00 15.24  ? 106 GLU E OE2 1 
ATOM   8331  N N   . SER E  1 101 ? -18.804 9.952   64.943  1.00 11.87  ? 107 SER E N   1 
ATOM   8332  C CA  . SER E  1 101 ? -20.054 9.886   64.185  1.00 12.29  ? 107 SER E CA  1 
ATOM   8333  C C   . SER E  1 101 ? -20.681 11.269  64.108  1.00 12.82  ? 107 SER E C   1 
ATOM   8334  O O   . SER E  1 101 ? -21.068 11.730  63.027  1.00 13.41  ? 107 SER E O   1 
ATOM   8335  C CB  . SER E  1 101 ? -21.042 8.912   64.835  1.00 12.54  ? 107 SER E CB  1 
ATOM   8336  O OG  . SER E  1 101 ? -20.554 7.584   64.825  1.00 13.93  ? 107 SER E OG  1 
ATOM   8337  N N   . LEU E  1 102 ? -20.760 11.925  65.266  1.00 12.18  ? 108 LEU E N   1 
ATOM   8338  C CA  . LEU E  1 102 ? -21.310 13.267  65.384  1.00 11.88  ? 108 LEU E CA  1 
ATOM   8339  C C   . LEU E  1 102 ? -20.496 14.274  64.573  1.00 11.50  ? 108 LEU E C   1 
ATOM   8340  O O   . LEU E  1 102 ? -21.061 15.153  63.913  1.00 10.78  ? 108 LEU E O   1 
ATOM   8341  C CB  . LEU E  1 102 ? -21.364 13.678  66.858  1.00 12.42  ? 108 LEU E CB  1 
ATOM   8342  C CG  . LEU E  1 102 ? -22.249 14.857  67.285  1.00 13.89  ? 108 LEU E CG  1 
ATOM   8343  C CD1 . LEU E  1 102 ? -23.678 14.710  66.774  1.00 15.57  ? 108 LEU E CD1 1 
ATOM   8344  C CD2 . LEU E  1 102 ? -22.239 14.990  68.802  1.00 13.95  ? 108 LEU E CD2 1 
ATOM   8345  N N   . ARG E  1 103 ? -19.172 14.138  64.616  1.00 10.94  ? 109 ARG E N   1 
ATOM   8346  C CA  . ARG E  1 103 ? -18.294 15.030  63.864  1.00 11.26  ? 109 ARG E CA  1 
ATOM   8347  C C   . ARG E  1 103 ? -18.555 14.932  62.368  1.00 11.49  ? 109 ARG E C   1 
ATOM   8348  O O   . ARG E  1 103 ? -18.455 15.926  61.652  1.00 11.96  ? 109 ARG E O   1 
ATOM   8349  C CB  . ARG E  1 103 ? -16.822 14.750  64.167  1.00 11.63  ? 109 ARG E CB  1 
ATOM   8350  C CG  . ARG E  1 103 ? -16.356 15.295  65.502  1.00 11.01  ? 109 ARG E CG  1 
ATOM   8351  C CD  . ARG E  1 103 ? -14.857 15.431  65.551  1.00 8.82   ? 109 ARG E CD  1 
ATOM   8352  N NE  . ARG E  1 103 ? -14.383 15.615  66.919  1.00 9.61   ? 109 ARG E NE  1 
ATOM   8353  C CZ  . ARG E  1 103 ? -13.938 14.636  67.700  1.00 8.66   ? 109 ARG E CZ  1 
ATOM   8354  N NH1 . ARG E  1 103 ? -13.899 13.389  67.257  1.00 15.84  ? 109 ARG E NH1 1 
ATOM   8355  N NH2 . ARG E  1 103 ? -13.530 14.902  68.929  1.00 7.99   ? 109 ARG E NH2 1 
ATOM   8356  N N   . GLN E  1 104 ? -18.914 13.735  61.913  1.00 11.39  ? 110 GLN E N   1 
ATOM   8357  C CA  . GLN E  1 104 ? -19.170 13.479  60.503  1.00 11.40  ? 110 GLN E CA  1 
ATOM   8358  C C   . GLN E  1 104 ? -20.465 14.110  59.995  1.00 12.40  ? 110 GLN E C   1 
ATOM   8359  O O   . GLN E  1 104 ? -20.500 14.616  58.874  1.00 12.80  ? 110 GLN E O   1 
ATOM   8360  C CB  . GLN E  1 104 ? -19.127 11.981  60.214  1.00 10.79  ? 110 GLN E CB  1 
ATOM   8361  C CG  . GLN E  1 104 ? -17.707 11.440  60.196  1.00 11.86  ? 110 GLN E CG  1 
ATOM   8362  C CD  . GLN E  1 104 ? -17.625 9.926   60.241  1.00 16.03  ? 110 GLN E CD  1 
ATOM   8363  O OE1 . GLN E  1 104 ? -18.636 9.231   60.388  1.00 15.19  ? 110 GLN E OE1 1 
ATOM   8364  N NE2 . GLN E  1 104 ? -16.405 9.405   60.123  1.00 15.77  ? 110 GLN E NE2 1 
ATOM   8365  N N   . ILE E  1 105 ? -21.520 14.086  60.808  1.00 13.23  ? 111 ILE E N   1 
ATOM   8366  C CA  . ILE E  1 105 ? -22.793 14.696  60.405  1.00 13.82  ? 111 ILE E CA  1 
ATOM   8367  C C   . ILE E  1 105 ? -22.720 16.218  60.461  1.00 14.53  ? 111 ILE E C   1 
ATOM   8368  O O   . ILE E  1 105 ? -23.381 16.906  59.674  1.00 15.00  ? 111 ILE E O   1 
ATOM   8369  C CB  . ILE E  1 105 ? -24.024 14.163  61.202  1.00 13.34  ? 111 ILE E CB  1 
ATOM   8370  C CG1 . ILE E  1 105 ? -23.879 14.386  62.705  1.00 17.19  ? 111 ILE E CG1 1 
ATOM   8371  C CG2 . ILE E  1 105 ? -24.236 12.689  60.949  1.00 15.79  ? 111 ILE E CG2 1 
ATOM   8372  C CD1 . ILE E  1 105 ? -24.595 15.604  63.214  1.00 22.88  ? 111 ILE E CD1 1 
ATOM   8373  N N   . LEU E  1 106 ? -21.905 16.731  61.382  1.00 14.73  ? 112 LEU E N   1 
ATOM   8374  C CA  . LEU E  1 106 ? -21.751 18.174  61.564  1.00 14.82  ? 112 LEU E CA  1 
ATOM   8375  C C   . LEU E  1 106 ? -20.901 18.813  60.466  1.00 15.28  ? 112 LEU E C   1 
ATOM   8376  O O   . LEU E  1 106 ? -21.168 19.943  60.054  1.00 16.00  ? 112 LEU E O   1 
ATOM   8377  C CB  . LEU E  1 106 ? -21.175 18.498  62.950  1.00 14.78  ? 112 LEU E CB  1 
ATOM   8378  C CG  . LEU E  1 106 ? -22.123 18.462  64.155  1.00 12.08  ? 112 LEU E CG  1 
ATOM   8379  C CD1 . LEU E  1 106 ? -21.349 18.688  65.433  1.00 13.17  ? 112 LEU E CD1 1 
ATOM   8380  C CD2 . LEU E  1 106 ? -23.208 19.504  64.029  1.00 7.74   ? 112 LEU E CD2 1 
ATOM   8381  N N   . ARG E  1 107 ? -19.889 18.087  59.992  1.00 14.71  ? 113 ARG E N   1 
ATOM   8382  C CA  . ARG E  1 107 ? -19.016 18.579  58.923  1.00 14.11  ? 113 ARG E CA  1 
ATOM   8383  C C   . ARG E  1 107 ? -19.754 18.871  57.619  1.00 14.44  ? 113 ARG E C   1 
ATOM   8384  O O   . ARG E  1 107 ? -19.309 19.711  56.834  1.00 15.06  ? 113 ARG E O   1 
ATOM   8385  C CB  . ARG E  1 107 ? -17.870 17.606  58.655  1.00 13.55  ? 113 ARG E CB  1 
ATOM   8386  C CG  . ARG E  1 107 ? -16.819 17.593  59.735  1.00 12.94  ? 113 ARG E CG  1 
ATOM   8387  C CD  . ARG E  1 107 ? -15.586 16.851  59.296  1.00 12.53  ? 113 ARG E CD  1 
ATOM   8388  N NE  . ARG E  1 107 ? -14.822 16.382  60.444  1.00 12.32  ? 113 ARG E NE  1 
ATOM   8389  C CZ  . ARG E  1 107 ? -14.809 15.122  60.864  1.00 15.55  ? 113 ARG E CZ  1 
ATOM   8390  N NH1 . ARG E  1 107 ? -15.515 14.194  60.223  1.00 17.05  ? 113 ARG E NH1 1 
ATOM   8391  N NH2 . ARG E  1 107 ? -14.084 14.787  61.921  1.00 14.06  ? 113 ARG E NH2 1 
ATOM   8392  N N   . ARG E  1 108 ? -20.869 18.174  57.396  1.00 14.42  ? 114 ARG E N   1 
ATOM   8393  C CA  . ARG E  1 108 ? -21.660 18.323  56.171  1.00 15.18  ? 114 ARG E CA  1 
ATOM   8394  C C   . ARG E  1 108 ? -23.016 18.996  56.412  1.00 15.65  ? 114 ARG E C   1 
ATOM   8395  O O   . ARG E  1 108 ? -23.869 19.038  55.520  1.00 15.78  ? 114 ARG E O   1 
ATOM   8396  C CB  . ARG E  1 108 ? -21.844 16.965  55.483  1.00 15.52  ? 114 ARG E CB  1 
ATOM   8397  C CG  . ARG E  1 108 ? -22.813 16.010  56.176  1.00 14.99  ? 114 ARG E CG  1 
ATOM   8398  C CD  . ARG E  1 108 ? -22.659 14.603  55.629  1.00 16.31  ? 114 ARG E CD  1 
ATOM   8399  N NE  . ARG E  1 108 ? -23.356 13.627  56.460  1.00 18.20  ? 114 ARG E NE  1 
ATOM   8400  C CZ  . ARG E  1 108 ? -22.925 12.391  56.697  1.00 16.27  ? 114 ARG E CZ  1 
ATOM   8401  N NH1 . ARG E  1 108 ? -21.783 11.957  56.177  1.00 12.40  ? 114 ARG E NH1 1 
ATOM   8402  N NH2 . ARG E  1 108 ? -23.640 11.587  57.468  1.00 17.41  ? 114 ARG E NH2 1 
ATOM   8403  N N   . SER E  1 109 ? -23.190 19.527  57.619  1.00 15.81  ? 115 SER E N   1 
ATOM   8404  C CA  . SER E  1 109 ? -24.452 20.122  58.067  1.00 16.01  ? 115 SER E CA  1 
ATOM   8405  C C   . SER E  1 109 ? -24.774 21.462  57.412  1.00 15.91  ? 115 SER E C   1 
ATOM   8406  O O   . SER E  1 109 ? -25.924 21.912  57.431  1.00 15.83  ? 115 SER E O   1 
ATOM   8407  C CB  . SER E  1 109 ? -24.408 20.319  59.582  1.00 16.51  ? 115 SER E CB  1 
ATOM   8408  O OG  . SER E  1 109 ? -23.379 21.227  59.944  1.00 15.51  ? 115 SER E OG  1 
ATOM   8409  N N   . GLY E  1 110 ? -23.753 22.102  56.851  1.00 15.65  ? 116 GLY E N   1 
ATOM   8410  C CA  . GLY E  1 110 ? -23.891 23.457  56.340  1.00 15.60  ? 116 GLY E CA  1 
ATOM   8411  C C   . GLY E  1 110 ? -23.938 24.486  57.454  1.00 15.34  ? 116 GLY E C   1 
ATOM   8412  O O   . GLY E  1 110 ? -24.343 25.625  57.232  1.00 15.76  ? 116 GLY E O   1 
ATOM   8413  N N   . GLY E  1 111 ? -23.514 24.083  58.651  1.00 15.06  ? 117 GLY E N   1 
ATOM   8414  C CA  . GLY E  1 111 ? -23.587 24.932  59.837  1.00 14.45  ? 117 GLY E CA  1 
ATOM   8415  C C   . GLY E  1 111 ? -24.786 24.602  60.707  1.00 14.38  ? 117 GLY E C   1 
ATOM   8416  O O   . GLY E  1 111 ? -25.652 23.818  60.314  1.00 14.62  ? 117 GLY E O   1 
ATOM   8417  N N   . ILE E  1 112 ? -24.837 25.205  61.893  1.00 14.09  ? 118 ILE E N   1 
ATOM   8418  C CA  . ILE E  1 112 ? -25.929 24.961  62.838  1.00 13.19  ? 118 ILE E CA  1 
ATOM   8419  C C   . ILE E  1 112 ? -26.695 26.229  63.206  1.00 13.13  ? 118 ILE E C   1 
ATOM   8420  O O   . ILE E  1 112 ? -26.117 27.313  63.301  1.00 14.35  ? 118 ILE E O   1 
ATOM   8421  C CB  . ILE E  1 112 ? -25.438 24.258  64.126  1.00 12.96  ? 118 ILE E CB  1 
ATOM   8422  C CG1 . ILE E  1 112 ? -24.370 25.103  64.841  1.00 13.54  ? 118 ILE E CG1 1 
ATOM   8423  C CG2 . ILE E  1 112 ? -24.923 22.867  63.800  1.00 11.91  ? 118 ILE E CG2 1 
ATOM   8424  C CD1 . ILE E  1 112 ? -24.029 24.636  66.243  1.00 9.67   ? 118 ILE E CD1 1 
ATOM   8425  N N   . GLY E  1 113 ? -28.003 26.079  63.386  1.00 12.25  ? 119 GLY E N   1 
ATOM   8426  C CA  . GLY E  1 113 ? -28.852 27.134  63.919  1.00 11.37  ? 119 GLY E CA  1 
ATOM   8427  C C   . GLY E  1 113 ? -29.437 26.621  65.217  1.00 11.80  ? 119 GLY E C   1 
ATOM   8428  O O   . GLY E  1 113 ? -29.866 25.465  65.294  1.00 11.92  ? 119 GLY E O   1 
ATOM   8429  N N   . LYS E  1 114 ? -29.445 27.464  66.244  1.00 11.55  ? 120 LYS E N   1 
ATOM   8430  C CA  . LYS E  1 114 ? -29.903 27.040  67.564  1.00 11.31  ? 120 LYS E CA  1 
ATOM   8431  C C   . LYS E  1 114 ? -31.318 27.507  67.871  1.00 12.27  ? 120 LYS E C   1 
ATOM   8432  O O   . LYS E  1 114 ? -31.786 28.517  67.339  1.00 11.67  ? 120 LYS E O   1 
ATOM   8433  C CB  . LYS E  1 114 ? -28.935 27.515  68.647  1.00 11.15  ? 120 LYS E CB  1 
ATOM   8434  C CG  . LYS E  1 114 ? -27.599 26.786  68.654  1.00 8.30   ? 120 LYS E CG  1 
ATOM   8435  C CD  . LYS E  1 114 ? -27.580 25.654  69.674  1.00 5.00   ? 120 LYS E CD  1 
ATOM   8436  C CE  . LYS E  1 114 ? -26.271 24.883  69.620  1.00 4.79   ? 120 LYS E CE  1 
ATOM   8437  N NZ  . LYS E  1 114 ? -25.067 25.751  69.748  1.00 2.73   ? 120 LYS E NZ  1 
ATOM   8438  N N   . GLU E  1 115 ? -31.994 26.753  68.732  1.00 13.83  ? 121 GLU E N   1 
ATOM   8439  C CA  . GLU E  1 115 ? -33.355 27.064  69.155  1.00 14.44  ? 121 GLU E CA  1 
ATOM   8440  C C   . GLU E  1 115 ? -33.563 26.614  70.597  1.00 14.27  ? 121 GLU E C   1 
ATOM   8441  O O   . GLU E  1 115 ? -33.078 25.550  71.001  1.00 13.90  ? 121 GLU E O   1 
ATOM   8442  C CB  . GLU E  1 115 ? -34.366 26.370  68.242  1.00 14.66  ? 121 GLU E CB  1 
ATOM   8443  C CG  . GLU E  1 115 ? -35.626 27.181  67.991  1.00 19.74  ? 121 GLU E CG  1 
ATOM   8444  C CD  . GLU E  1 115 ? -36.821 26.311  67.654  1.00 24.43  ? 121 GLU E CD  1 
ATOM   8445  O OE1 . GLU E  1 115 ? -37.369 26.467  66.540  1.00 24.22  ? 121 GLU E OE1 1 
ATOM   8446  O OE2 . GLU E  1 115 ? -37.209 25.471  68.501  1.00 25.74  ? 121 GLU E OE2 1 
ATOM   8447  N N   . SER E  1 116 ? -34.281 27.431  71.366  1.00 14.36  ? 122 SER E N   1 
ATOM   8448  C CA  . SER E  1 116 ? -34.600 27.121  72.759  1.00 14.20  ? 122 SER E CA  1 
ATOM   8449  C C   . SER E  1 116 ? -35.581 25.956  72.854  1.00 14.59  ? 122 SER E C   1 
ATOM   8450  O O   . SER E  1 116 ? -36.481 25.824  72.019  1.00 14.67  ? 122 SER E O   1 
ATOM   8451  C CB  . SER E  1 116 ? -35.179 28.349  73.460  1.00 13.77  ? 122 SER E CB  1 
ATOM   8452  O OG  . SER E  1 116 ? -35.452 28.073  74.821  1.00 13.81  ? 122 SER E OG  1 
ATOM   8453  N N   . MET E  1 117 ? -35.398 25.116  73.869  1.00 14.74  ? 123 MET E N   1 
ATOM   8454  C CA  . MET E  1 117 ? -36.273 23.962  74.088  1.00 15.12  ? 123 MET E CA  1 
ATOM   8455  C C   . MET E  1 117 ? -37.429 24.239  75.053  1.00 15.24  ? 123 MET E C   1 
ATOM   8456  O O   . MET E  1 117 ? -38.308 23.397  75.237  1.00 15.38  ? 123 MET E O   1 
ATOM   8457  C CB  . MET E  1 117 ? -35.458 22.753  74.542  1.00 15.35  ? 123 MET E CB  1 
ATOM   8458  C CG  . MET E  1 117 ? -34.718 22.076  73.402  1.00 16.67  ? 123 MET E CG  1 
ATOM   8459  S SD  . MET E  1 117 ? -33.533 20.837  73.933  1.00 16.33  ? 123 MET E SD  1 
ATOM   8460  C CE  . MET E  1 117 ? -34.599 19.474  74.393  1.00 14.18  ? 123 MET E CE  1 
ATOM   8461  N N   . GLY E  1 118 ? -37.423 25.425  75.657  1.00 15.68  ? 124 GLY E N   1 
ATOM   8462  C CA  . GLY E  1 118 ? -38.509 25.865  76.526  1.00 15.36  ? 124 GLY E CA  1 
ATOM   8463  C C   . GLY E  1 118 ? -38.537 25.212  77.896  1.00 15.34  ? 124 GLY E C   1 
ATOM   8464  O O   . GLY E  1 118 ? -39.585 25.167  78.537  1.00 15.20  ? 124 GLY E O   1 
ATOM   8465  N N   . PHE E  1 119 ? -37.394 24.707  78.354  1.00 15.28  ? 125 PHE E N   1 
ATOM   8466  C CA  . PHE E  1 119 ? -37.318 24.114  79.687  1.00 14.98  ? 125 PHE E CA  1 
ATOM   8467  C C   . PHE E  1 119 ? -37.162 25.178  80.767  1.00 15.37  ? 125 PHE E C   1 
ATOM   8468  O O   . PHE E  1 119 ? -36.169 25.912  80.791  1.00 15.80  ? 125 PHE E O   1 
ATOM   8469  C CB  . PHE E  1 119 ? -36.175 23.096  79.801  1.00 14.70  ? 125 PHE E CB  1 
ATOM   8470  C CG  . PHE E  1 119 ? -36.385 21.833  79.009  1.00 12.82  ? 125 PHE E CG  1 
ATOM   8471  C CD1 . PHE E  1 119 ? -35.300 21.030  78.678  1.00 12.81  ? 125 PHE E CD1 1 
ATOM   8472  C CD2 . PHE E  1 119 ? -37.653 21.446  78.585  1.00 9.61   ? 125 PHE E CD2 1 
ATOM   8473  C CE1 . PHE E  1 119 ? -35.472 19.859  77.946  1.00 11.39  ? 125 PHE E CE1 1 
ATOM   8474  C CE2 . PHE E  1 119 ? -37.832 20.281  77.846  1.00 9.33   ? 125 PHE E CE2 1 
ATOM   8475  C CZ  . PHE E  1 119 ? -36.738 19.486  77.526  1.00 7.03   ? 125 PHE E CZ  1 
ATOM   8476  N N   . THR E  1 120 ? -38.156 25.261  81.647  1.00 15.54  ? 126 THR E N   1 
ATOM   8477  C CA  . THR E  1 120 ? -38.060 26.065  82.864  1.00 15.71  ? 126 THR E CA  1 
ATOM   8478  C C   . THR E  1 120 ? -38.148 25.144  84.078  1.00 15.50  ? 126 THR E C   1 
ATOM   8479  O O   . THR E  1 120 ? -38.727 24.057  84.002  1.00 14.40  ? 126 THR E O   1 
ATOM   8480  C CB  . THR E  1 120 ? -39.150 27.153  82.949  1.00 15.94  ? 126 THR E CB  1 
ATOM   8481  O OG1 . THR E  1 120 ? -40.446 26.542  82.906  1.00 15.92  ? 126 THR E OG1 1 
ATOM   8482  C CG2 . THR E  1 120 ? -39.013 28.153  81.803  1.00 16.17  ? 126 THR E CG2 1 
ATOM   8483  N N   . TYR E  1 121 ? -37.575 25.588  85.193  1.00 15.94  ? 127 TYR E N   1 
ATOM   8484  C CA  . TYR E  1 121 ? -37.432 24.748  86.375  1.00 16.59  ? 127 TYR E CA  1 
ATOM   8485  C C   . TYR E  1 121 ? -37.926 25.429  87.645  1.00 17.90  ? 127 TYR E C   1 
ATOM   8486  O O   . TYR E  1 121 ? -37.830 26.653  87.785  1.00 18.52  ? 127 TYR E O   1 
ATOM   8487  C CB  . TYR E  1 121 ? -35.968 24.324  86.533  1.00 16.66  ? 127 TYR E CB  1 
ATOM   8488  C CG  . TYR E  1 121 ? -35.416 23.638  85.307  1.00 16.47  ? 127 TYR E CG  1 
ATOM   8489  C CD1 . TYR E  1 121 ? -34.764 24.369  84.313  1.00 14.05  ? 127 TYR E CD1 1 
ATOM   8490  C CD2 . TYR E  1 121 ? -35.568 22.261  85.126  1.00 15.18  ? 127 TYR E CD2 1 
ATOM   8491  C CE1 . TYR E  1 121 ? -34.266 23.746  83.176  1.00 17.01  ? 127 TYR E CE1 1 
ATOM   8492  C CE2 . TYR E  1 121 ? -35.074 21.628  83.990  1.00 15.68  ? 127 TYR E CE2 1 
ATOM   8493  C CZ  . TYR E  1 121 ? -34.425 22.378  83.022  1.00 17.35  ? 127 TYR E CZ  1 
ATOM   8494  O OH  . TYR E  1 121 ? -33.932 21.767  81.897  1.00 20.29  ? 127 TYR E OH  1 
ATOM   8495  N N   . SER E  1 122 ? -38.455 24.628  88.568  1.00 18.75  ? 128 SER E N   1 
ATOM   8496  C CA  . SER E  1 122 ? -38.896 25.135  89.866  1.00 19.81  ? 128 SER E CA  1 
ATOM   8497  C C   . SER E  1 122 ? -38.477 24.215  91.010  1.00 19.57  ? 128 SER E C   1 
ATOM   8498  O O   . SER E  1 122 ? -38.568 22.985  90.903  1.00 19.04  ? 128 SER E O   1 
ATOM   8499  C CB  . SER E  1 122 ? -40.413 25.345  89.882  1.00 20.47  ? 128 SER E CB  1 
ATOM   8500  O OG  . SER E  1 122 ? -41.103 24.123  89.671  1.00 23.32  ? 128 SER E OG  1 
ATOM   8501  N N   . GLY E  1 123 ? -38.020 24.828  92.100  1.00 19.44  ? 129 GLY E N   1 
ATOM   8502  C CA  . GLY E  1 123 ? -37.631 24.101  93.306  1.00 19.17  ? 129 GLY E CA  1 
ATOM   8503  C C   . GLY E  1 123 ? -36.221 23.541  93.270  1.00 18.99  ? 129 GLY E C   1 
ATOM   8504  O O   . GLY E  1 123 ? -35.877 22.661  94.065  1.00 19.44  ? 129 GLY E O   1 
ATOM   8505  N N   . ILE E  1 124 ? -35.412 24.046  92.338  1.00 18.05  ? 130 ILE E N   1 
ATOM   8506  C CA  . ILE E  1 124 ? -34.007 23.651  92.205  1.00 16.60  ? 130 ILE E CA  1 
ATOM   8507  C C   . ILE E  1 124 ? -33.138 24.830  91.782  1.00 15.84  ? 130 ILE E C   1 
ATOM   8508  O O   . ILE E  1 124 ? -33.642 25.873  91.363  1.00 15.24  ? 130 ILE E O   1 
ATOM   8509  C CB  . ILE E  1 124 ? -33.802 22.503  91.179  1.00 16.32  ? 130 ILE E CB  1 
ATOM   8510  C CG1 . ILE E  1 124 ? -34.345 22.895  89.798  1.00 16.96  ? 130 ILE E CG1 1 
ATOM   8511  C CG2 . ILE E  1 124 ? -34.430 21.211  91.672  1.00 15.74  ? 130 ILE E CG2 1 
ATOM   8512  C CD1 . ILE E  1 124 ? -33.789 22.059  88.658  1.00 17.54  ? 130 ILE E CD1 1 
ATOM   8513  N N   . ARG E  1 125 ? -31.828 24.651  91.901  1.00 15.48  ? 131 ARG E N   1 
ATOM   8514  C CA  . ARG E  1 125 ? -30.876 25.597  91.352  1.00 15.04  ? 131 ARG E CA  1 
ATOM   8515  C C   . ARG E  1 125 ? -30.507 25.213  89.921  1.00 15.65  ? 131 ARG E C   1 
ATOM   8516  O O   . ARG E  1 125 ? -30.466 24.030  89.560  1.00 15.90  ? 131 ARG E O   1 
ATOM   8517  C CB  . ARG E  1 125 ? -29.642 25.707  92.238  1.00 14.67  ? 131 ARG E CB  1 
ATOM   8518  C CG  . ARG E  1 125 ? -29.793 26.700  93.369  1.00 14.39  ? 131 ARG E CG  1 
ATOM   8519  C CD  . ARG E  1 125 ? -28.964 26.294  94.568  1.00 18.77  ? 131 ARG E CD  1 
ATOM   8520  N NE  . ARG E  1 125 ? -27.525 26.446  94.364  1.00 25.16  ? 131 ARG E NE  1 
ATOM   8521  C CZ  . ARG E  1 125 ? -26.594 25.829  95.090  1.00 28.68  ? 131 ARG E CZ  1 
ATOM   8522  N NH1 . ARG E  1 125 ? -26.937 24.995  96.068  1.00 27.07  ? 131 ARG E NH1 1 
ATOM   8523  N NH2 . ARG E  1 125 ? -25.311 26.038  94.829  1.00 33.04  ? 131 ARG E NH2 1 
ATOM   8524  N N   . THR E  1 126 ? -30.241 26.239  89.121  1.00 15.80  ? 132 THR E N   1 
ATOM   8525  C CA  . THR E  1 126 ? -30.075 26.123  87.679  1.00 15.24  ? 132 THR E CA  1 
ATOM   8526  C C   . THR E  1 126 ? -28.684 26.626  87.277  1.00 14.83  ? 132 THR E C   1 
ATOM   8527  O O   . THR E  1 126 ? -28.205 26.368  86.172  1.00 14.17  ? 132 THR E O   1 
ATOM   8528  C CB  . THR E  1 126 ? -31.229 26.909  86.978  1.00 15.51  ? 132 THR E CB  1 
ATOM   8529  O OG1 . THR E  1 126 ? -32.300 26.006  86.666  1.00 14.25  ? 132 THR E OG1 1 
ATOM   8530  C CG2 . THR E  1 126 ? -30.775 27.642  85.708  1.00 16.01  ? 132 THR E CG2 1 
ATOM   8531  N N   . ASN E  1 127 ? -28.030 27.294  88.222  1.00 15.52  ? 133 ASN E N   1 
ATOM   8532  C CA  . ASN E  1 127 ? -26.817 28.067  87.972  1.00 15.46  ? 133 ASN E CA  1 
ATOM   8533  C C   . ASN E  1 127 ? -25.498 27.337  88.248  1.00 14.92  ? 133 ASN E C   1 
ATOM   8534  O O   . ASN E  1 127 ? -24.496 27.972  88.585  1.00 16.41  ? 133 ASN E O   1 
ATOM   8535  C CB  . ASN E  1 127 ? -26.872 29.376  88.780  1.00 15.82  ? 133 ASN E CB  1 
ATOM   8536  C CG  . ASN E  1 127 ? -26.991 29.142  90.289  1.00 16.99  ? 133 ASN E CG  1 
ATOM   8537  O OD1 . ASN E  1 127 ? -27.259 28.027  90.751  1.00 16.95  ? 133 ASN E OD1 1 
ATOM   8538  N ND2 . ASN E  1 127 ? -26.793 30.203  91.060  1.00 18.48  ? 133 ASN E ND2 1 
ATOM   8539  N N   . GLY E  1 128 ? -25.490 26.016  88.100  1.00 13.95  ? 134 GLY E N   1 
ATOM   8540  C CA  . GLY E  1 128 ? -24.265 25.238  88.283  1.00 12.66  ? 134 GLY E CA  1 
ATOM   8541  C C   . GLY E  1 128 ? -23.153 25.797  87.417  1.00 12.26  ? 134 GLY E C   1 
ATOM   8542  O O   . GLY E  1 128 ? -23.365 26.070  86.238  1.00 13.28  ? 134 GLY E O   1 
ATOM   8543  N N   . ALA E  1 129 ? -21.977 25.995  88.009  1.00 11.59  ? 135 ALA E N   1 
ATOM   8544  C CA  . ALA E  1 129 ? -20.834 26.573  87.297  1.00 11.12  ? 135 ALA E CA  1 
ATOM   8545  C C   . ALA E  1 129 ? -19.512 25.965  87.760  1.00 11.17  ? 135 ALA E C   1 
ATOM   8546  O O   . ALA E  1 129 ? -19.458 25.291  88.787  1.00 11.58  ? 135 ALA E O   1 
ATOM   8547  C CB  . ALA E  1 129 ? -20.816 28.080  87.461  1.00 10.67  ? 135 ALA E CB  1 
ATOM   8548  N N   . THR E  1 130 ? -18.449 26.199  86.999  1.00 11.17  ? 136 THR E N   1 
ATOM   8549  C CA  . THR E  1 130 ? -17.139 25.641  87.329  1.00 11.95  ? 136 THR E CA  1 
ATOM   8550  C C   . THR E  1 130 ? -15.988 26.555  86.909  1.00 12.69  ? 136 THR E C   1 
ATOM   8551  O O   . THR E  1 130 ? -16.103 27.313  85.942  1.00 13.41  ? 136 THR E O   1 
ATOM   8552  C CB  . THR E  1 130 ? -16.950 24.221  86.724  1.00 11.93  ? 136 THR E CB  1 
ATOM   8553  O OG1 . THR E  1 130 ? -15.616 23.764  86.972  1.00 10.85  ? 136 THR E OG1 1 
ATOM   8554  C CG2 . THR E  1 130 ? -17.207 24.217  85.221  1.00 11.99  ? 136 THR E CG2 1 
ATOM   8555  N N   . SER E  1 131 ? -14.881 26.477  87.642  1.00 12.89  ? 137 SER E N   1 
ATOM   8556  C CA  . SER E  1 131 ? -13.676 27.237  87.303  1.00 13.29  ? 137 SER E CA  1 
ATOM   8557  C C   . SER E  1 131 ? -12.955 26.667  86.074  1.00 13.54  ? 137 SER E C   1 
ATOM   8558  O O   . SER E  1 131 ? -12.050 27.301  85.527  1.00 13.61  ? 137 SER E O   1 
ATOM   8559  C CB  . SER E  1 131 ? -12.729 27.333  88.505  1.00 13.27  ? 137 SER E CB  1 
ATOM   8560  O OG  . SER E  1 131 ? -12.499 26.065  89.092  1.00 12.48  ? 137 SER E OG  1 
ATOM   8561  N N   . ALA E  1 132 ? -13.369 25.477  85.642  1.00 13.59  ? 138 ALA E N   1 
ATOM   8562  C CA  . ALA E  1 132 ? -12.832 24.857  84.430  1.00 13.97  ? 138 ALA E CA  1 
ATOM   8563  C C   . ALA E  1 132 ? -13.364 25.542  83.169  1.00 14.27  ? 138 ALA E C   1 
ATOM   8564  O O   . ALA E  1 132 ? -12.718 25.508  82.117  1.00 14.41  ? 138 ALA E O   1 
ATOM   8565  C CB  . ALA E  1 132 ? -13.149 23.364  84.407  1.00 13.64  ? 138 ALA E CB  1 
ATOM   8566  N N   . CYS E  1 133 ? -14.544 26.153  83.287  1.00 14.26  ? 139 CYS E N   1 
ATOM   8567  C CA  . CYS E  1 133 ? -15.158 26.908  82.199  1.00 14.23  ? 139 CYS E CA  1 
ATOM   8568  C C   . CYS E  1 133 ? -15.246 28.384  82.589  1.00 14.70  ? 139 CYS E C   1 
ATOM   8569  O O   . CYS E  1 133 ? -16.263 28.829  83.117  1.00 14.30  ? 139 CYS E O   1 
ATOM   8570  C CB  . CYS E  1 133 ? -16.554 26.355  81.873  1.00 14.23  ? 139 CYS E CB  1 
ATOM   8571  S SG  . CYS E  1 133 ? -16.641 24.557  81.670  0.60 12.00  ? 139 CYS E SG  1 
ATOM   8572  N N   . THR E  1 134 ? -14.175 29.135  82.337  1.00 15.53  ? 140 THR E N   1 
ATOM   8573  C CA  . THR E  1 134 ? -14.114 30.543  82.743  1.00 16.48  ? 140 THR E CA  1 
ATOM   8574  C C   . THR E  1 134 ? -14.550 31.514  81.651  1.00 16.67  ? 140 THR E C   1 
ATOM   8575  O O   . THR E  1 134 ? -14.189 31.373  80.481  1.00 16.99  ? 140 THR E O   1 
ATOM   8576  C CB  . THR E  1 134 ? -12.724 30.964  83.292  1.00 16.56  ? 140 THR E CB  1 
ATOM   8577  O OG1 . THR E  1 134 ? -11.687 30.422  82.466  1.00 18.97  ? 140 THR E OG1 1 
ATOM   8578  C CG2 . THR E  1 134 ? -12.539 30.483  84.726  1.00 16.51  ? 140 THR E CG2 1 
ATOM   8579  N N   . ARG E  1 135 ? -15.321 32.510  82.076  1.00 16.75  ? 141 ARG E N   1 
ATOM   8580  C CA  . ARG E  1 135 ? -15.935 33.497  81.207  1.00 16.74  ? 141 ARG E CA  1 
ATOM   8581  C C   . ARG E  1 135 ? -16.185 34.705  82.105  1.00 16.94  ? 141 ARG E C   1 
ATOM   8582  O O   . ARG E  1 135 ? -17.307 34.928  82.576  1.00 17.17  ? 141 ARG E O   1 
ATOM   8583  C CB  . ARG E  1 135 ? -17.242 32.931  80.651  1.00 16.47  ? 141 ARG E CB  1 
ATOM   8584  C CG  . ARG E  1 135 ? -17.872 33.680  79.485  1.00 16.96  ? 141 ARG E CG  1 
ATOM   8585  C CD  . ARG E  1 135 ? -18.520 32.696  78.506  1.00 17.23  ? 141 ARG E CD  1 
ATOM   8586  N NE  . ARG E  1 135 ? -18.813 31.414  79.150  1.00 20.05  ? 141 ARG E NE  1 
ATOM   8587  C CZ  . ARG E  1 135 ? -19.056 30.270  78.519  1.00 17.61  ? 141 ARG E CZ  1 
ATOM   8588  N NH1 . ARG E  1 135 ? -19.060 30.197  77.198  1.00 20.17  ? 141 ARG E NH1 1 
ATOM   8589  N NH2 . ARG E  1 135 ? -19.297 29.184  79.225  1.00 21.01  ? 141 ARG E NH2 1 
ATOM   8590  N N   . SER E  1 136 ? -15.117 35.460  82.362  1.00 16.85  ? 142 SER E N   1 
ATOM   8591  C CA  . SER E  1 136 ? -15.118 36.513  83.385  1.00 17.08  ? 142 SER E CA  1 
ATOM   8592  C C   . SER E  1 136 ? -15.577 35.934  84.728  1.00 16.63  ? 142 SER E C   1 
ATOM   8593  O O   . SER E  1 136 ? -16.498 36.456  85.358  1.00 17.18  ? 142 SER E O   1 
ATOM   8594  C CB  . SER E  1 136 ? -15.998 37.705  82.969  1.00 17.17  ? 142 SER E CB  1 
ATOM   8595  O OG  . SER E  1 136 ? -15.766 38.080  81.619  1.00 17.82  ? 142 SER E OG  1 
ATOM   8596  N N   . GLY E  1 137 ? -14.935 34.844  85.146  1.00 15.82  ? 144 GLY E N   1 
ATOM   8597  C CA  . GLY E  1 137 ? -15.324 34.115  86.357  1.00 14.07  ? 144 GLY E CA  1 
ATOM   8598  C C   . GLY E  1 137 ? -15.834 32.712  86.066  1.00 13.38  ? 144 GLY E C   1 
ATOM   8599  O O   . GLY E  1 137 ? -15.850 32.273  84.912  1.00 12.54  ? 144 GLY E O   1 
ATOM   8600  N N   . SER E  1 138 ? -16.250 32.009  87.117  1.00 12.97  ? 145 SER E N   1 
ATOM   8601  C CA  . SER E  1 138 ? -16.818 30.666  86.984  1.00 12.16  ? 145 SER E CA  1 
ATOM   8602  C C   . SER E  1 138 ? -18.098 30.668  86.153  1.00 11.81  ? 145 SER E C   1 
ATOM   8603  O O   . SER E  1 138 ? -19.036 31.420  86.431  1.00 11.31  ? 145 SER E O   1 
ATOM   8604  C CB  . SER E  1 138 ? -17.080 30.045  88.355  1.00 11.89  ? 145 SER E CB  1 
ATOM   8605  O OG  . SER E  1 138 ? -15.897 29.482  88.885  1.00 12.69  ? 145 SER E OG  1 
ATOM   8606  N N   . SER E  1 139 ? -18.112 29.813  85.134  1.00 11.30  ? 146 SER E N   1 
ATOM   8607  C CA  . SER E  1 139 ? -19.214 29.711  84.187  1.00 11.11  ? 146 SER E CA  1 
ATOM   8608  C C   . SER E  1 139 ? -19.405 28.240  83.783  1.00 11.36  ? 146 SER E C   1 
ATOM   8609  O O   . SER E  1 139 ? -18.769 27.345  84.350  1.00 11.78  ? 146 SER E O   1 
ATOM   8610  C CB  . SER E  1 139 ? -18.925 30.598  82.970  1.00 10.83  ? 146 SER E CB  1 
ATOM   8611  O OG  . SER E  1 139 ? -19.934 30.499  81.984  1.00 11.45  ? 146 SER E OG  1 
ATOM   8612  N N   . PHE E  1 140 ? -20.280 27.990  82.814  1.00 10.78  ? 147 PHE E N   1 
ATOM   8613  C CA  . PHE E  1 140 ? -20.590 26.626  82.398  1.00 10.32  ? 147 PHE E CA  1 
ATOM   8614  C C   . PHE E  1 140 ? -20.685 26.539  80.877  1.00 9.97   ? 147 PHE E C   1 
ATOM   8615  O O   . PHE E  1 140 ? -20.228 27.436  80.180  1.00 9.49   ? 147 PHE E O   1 
ATOM   8616  C CB  . PHE E  1 140 ? -21.889 26.163  83.070  1.00 10.37  ? 147 PHE E CB  1 
ATOM   8617  C CG  . PHE E  1 140 ? -22.120 24.684  82.993  1.00 10.65  ? 147 PHE E CG  1 
ATOM   8618  C CD1 . PHE E  1 140 ? -21.112 23.787  83.353  1.00 11.81  ? 147 PHE E CD1 1 
ATOM   8619  C CD2 . PHE E  1 140 ? -23.348 24.185  82.568  1.00 10.35  ? 147 PHE E CD2 1 
ATOM   8620  C CE1 . PHE E  1 140 ? -21.318 22.414  83.282  1.00 9.89   ? 147 PHE E CE1 1 
ATOM   8621  C CE2 . PHE E  1 140 ? -23.568 22.812  82.493  1.00 10.35  ? 147 PHE E CE2 1 
ATOM   8622  C CZ  . PHE E  1 140 ? -22.549 21.923  82.852  1.00 12.25  ? 147 PHE E CZ  1 
ATOM   8623  N N   . TYR E  1 141 ? -21.254 25.450  80.364  1.00 9.76   ? 148 TYR E N   1 
ATOM   8624  C CA  . TYR E  1 141 ? -21.529 25.323  78.937  1.00 9.00   ? 148 TYR E CA  1 
ATOM   8625  C C   . TYR E  1 141 ? -22.701 26.219  78.565  1.00 9.15   ? 148 TYR E C   1 
ATOM   8626  O O   . TYR E  1 141 ? -23.762 26.160  79.190  1.00 9.75   ? 148 TYR E O   1 
ATOM   8627  C CB  . TYR E  1 141 ? -21.811 23.867  78.563  1.00 8.28   ? 148 TYR E CB  1 
ATOM   8628  C CG  . TYR E  1 141 ? -20.608 22.958  78.714  1.00 8.61   ? 148 TYR E CG  1 
ATOM   8629  C CD1 . TYR E  1 141 ? -20.505 22.081  79.791  1.00 5.05   ? 148 TYR E CD1 1 
ATOM   8630  C CD2 . TYR E  1 141 ? -19.569 22.980  77.779  1.00 8.01   ? 148 TYR E CD2 1 
ATOM   8631  C CE1 . TYR E  1 141 ? -19.399 21.247  79.935  1.00 10.36  ? 148 TYR E CE1 1 
ATOM   8632  C CE2 . TYR E  1 141 ? -18.459 22.155  77.916  1.00 9.83   ? 148 TYR E CE2 1 
ATOM   8633  C CZ  . TYR E  1 141 ? -18.380 21.287  78.994  1.00 13.83  ? 148 TYR E CZ  1 
ATOM   8634  O OH  . TYR E  1 141 ? -17.284 20.460  79.131  1.00 16.01  ? 148 TYR E OH  1 
ATOM   8635  N N   . ALA E  1 142 ? -22.494 27.054  77.550  1.00 9.15   ? 149 ALA E N   1 
ATOM   8636  C CA  . ALA E  1 142 ? -23.465 28.079  77.152  1.00 9.49   ? 149 ALA E CA  1 
ATOM   8637  C C   . ALA E  1 142 ? -24.851 27.540  76.780  1.00 9.28   ? 149 ALA E C   1 
ATOM   8638  O O   . ALA E  1 142 ? -25.863 28.177  77.076  1.00 9.46   ? 149 ALA E O   1 
ATOM   8639  C CB  . ALA E  1 142 ? -22.901 28.927  76.016  1.00 9.67   ? 149 ALA E CB  1 
ATOM   8640  N N   . GLU E  1 143 ? -24.891 26.374  76.138  1.00 8.50   ? 150 GLU E N   1 
ATOM   8641  C CA  . GLU E  1 143 ? -26.152 25.804  75.671  1.00 8.17   ? 150 GLU E CA  1 
ATOM   8642  C C   . GLU E  1 143 ? -26.827 24.895  76.704  1.00 8.62   ? 150 GLU E C   1 
ATOM   8643  O O   . GLU E  1 143 ? -27.963 24.448  76.499  1.00 8.36   ? 150 GLU E O   1 
ATOM   8644  C CB  . GLU E  1 143 ? -25.947 25.052  74.350  1.00 7.34   ? 150 GLU E CB  1 
ATOM   8645  C CG  . GLU E  1 143 ? -25.222 25.837  73.255  1.00 8.38   ? 150 GLU E CG  1 
ATOM   8646  C CD  . GLU E  1 143 ? -26.011 27.027  72.713  1.00 11.58  ? 150 GLU E CD  1 
ATOM   8647  O OE1 . GLU E  1 143 ? -26.987 27.457  73.358  1.00 13.73  ? 150 GLU E OE1 1 
ATOM   8648  O OE2 . GLU E  1 143 ? -25.643 27.546  71.638  1.00 11.77  ? 150 GLU E OE2 1 
ATOM   8649  N N   . MET E  1 144 ? -26.134 24.638  77.812  1.00 8.33   ? 151 MET E N   1 
ATOM   8650  C CA  . MET E  1 144 ? -26.596 23.676  78.815  1.00 8.42   ? 151 MET E CA  1 
ATOM   8651  C C   . MET E  1 144 ? -26.872 24.334  80.170  1.00 8.36   ? 151 MET E C   1 
ATOM   8652  O O   . MET E  1 144 ? -26.421 25.450  80.432  1.00 8.52   ? 151 MET E O   1 
ATOM   8653  C CB  . MET E  1 144 ? -25.566 22.555  78.993  1.00 8.52   ? 151 MET E CB  1 
ATOM   8654  C CG  . MET E  1 144 ? -25.043 21.925  77.702  1.00 10.73  ? 151 MET E CG  1 
ATOM   8655  S SD  . MET E  1 144 ? -26.162 20.708  76.984  1.00 17.82  ? 151 MET E SD  1 
ATOM   8656  C CE  . MET E  1 144 ? -26.796 21.590  75.566  1.00 16.93  ? 151 MET E CE  1 
ATOM   8657  N N   . LYS E  1 145 ? -27.620 23.633  81.021  1.00 8.34   ? 152 LYS E N   1 
ATOM   8658  C CA  . LYS E  1 145 ? -27.855 24.056  82.399  1.00 7.75   ? 152 LYS E CA  1 
ATOM   8659  C C   . LYS E  1 145 ? -27.469 22.941  83.368  1.00 7.68   ? 152 LYS E C   1 
ATOM   8660  O O   . LYS E  1 145 ? -27.949 21.813  83.246  1.00 7.57   ? 152 LYS E O   1 
ATOM   8661  C CB  . LYS E  1 145 ? -29.324 24.445  82.616  1.00 7.72   ? 152 LYS E CB  1 
ATOM   8662  C CG  . LYS E  1 145 ? -29.805 25.678  81.856  1.00 8.29   ? 152 LYS E CG  1 
ATOM   8663  C CD  . LYS E  1 145 ? -29.105 26.947  82.322  1.00 15.30  ? 152 LYS E CD  1 
ATOM   8664  C CE  . LYS E  1 145 ? -29.688 28.185  81.661  1.00 18.18  ? 152 LYS E CE  1 
ATOM   8665  N NZ  . LYS E  1 145 ? -30.929 28.631  82.350  1.00 23.59  ? 152 LYS E NZ  1 
ATOM   8666  N N   . TRP E  1 146 ? -26.593 23.266  84.318  1.00 8.07   ? 153 TRP E N   1 
ATOM   8667  C CA  . TRP E  1 146 ? -26.221 22.352  85.403  1.00 7.96   ? 153 TRP E CA  1 
ATOM   8668  C C   . TRP E  1 146 ? -27.271 22.422  86.513  1.00 7.98   ? 153 TRP E C   1 
ATOM   8669  O O   . TRP E  1 146 ? -27.277 23.361  87.313  1.00 8.43   ? 153 TRP E O   1 
ATOM   8670  C CB  . TRP E  1 146 ? -24.843 22.724  85.974  1.00 7.42   ? 153 TRP E CB  1 
ATOM   8671  C CG  . TRP E  1 146 ? -24.183 21.652  86.821  1.00 7.04   ? 153 TRP E CG  1 
ATOM   8672  C CD1 . TRP E  1 146 ? -24.800 20.623  87.481  1.00 7.76   ? 153 TRP E CD1 1 
ATOM   8673  C CD2 . TRP E  1 146 ? -22.782 21.528  87.114  1.00 6.14   ? 153 TRP E CD2 1 
ATOM   8674  N NE1 . TRP E  1 146 ? -23.872 19.859  88.145  1.00 7.15   ? 153 TRP E NE1 1 
ATOM   8675  C CE2 . TRP E  1 146 ? -22.626 20.391  87.941  1.00 6.08   ? 153 TRP E CE2 1 
ATOM   8676  C CE3 . TRP E  1 146 ? -21.643 22.264  86.757  1.00 5.75   ? 153 TRP E CE3 1 
ATOM   8677  C CZ2 . TRP E  1 146 ? -21.379 19.971  88.416  1.00 4.34   ? 153 TRP E CZ2 1 
ATOM   8678  C CZ3 . TRP E  1 146 ? -20.402 21.847  87.228  1.00 6.02   ? 153 TRP E CZ3 1 
ATOM   8679  C CH2 . TRP E  1 146 ? -20.282 20.710  88.050  1.00 6.75   ? 153 TRP E CH2 1 
ATOM   8680  N N   . LEU E  1 147 ? -28.152 21.427  86.561  1.00 7.71   ? 154 LEU E N   1 
ATOM   8681  C CA  . LEU E  1 147 ? -29.193 21.373  87.590  1.00 7.98   ? 154 LEU E CA  1 
ATOM   8682  C C   . LEU E  1 147 ? -28.665 20.756  88.880  1.00 8.60   ? 154 LEU E C   1 
ATOM   8683  O O   . LEU E  1 147 ? -27.884 19.802  88.842  1.00 8.69   ? 154 LEU E O   1 
ATOM   8684  C CB  . LEU E  1 147 ? -30.409 20.580  87.100  1.00 7.07   ? 154 LEU E CB  1 
ATOM   8685  C CG  . LEU E  1 147 ? -30.947 20.860  85.693  1.00 6.39   ? 154 LEU E CG  1 
ATOM   8686  C CD1 . LEU E  1 147 ? -31.995 19.826  85.337  1.00 5.32   ? 154 LEU E CD1 1 
ATOM   8687  C CD2 . LEU E  1 147 ? -31.510 22.272  85.556  1.00 2.70   ? 154 LEU E CD2 1 
ATOM   8688  N N   . LEU E  1 148 ? -29.101 21.315  90.009  1.00 8.93   ? 155 LEU E N   1 
ATOM   8689  C CA  . LEU E  1 148 ? -28.787 20.798  91.349  1.00 9.98   ? 155 LEU E CA  1 
ATOM   8690  C C   . LEU E  1 148 ? -29.767 21.298  92.413  1.00 11.16  ? 155 LEU E C   1 
ATOM   8691  O O   . LEU E  1 148 ? -30.485 22.276  92.195  1.00 12.37  ? 155 LEU E O   1 
ATOM   8692  C CB  . LEU E  1 148 ? -27.343 21.122  91.775  1.00 10.15  ? 155 LEU E CB  1 
ATOM   8693  C CG  . LEU E  1 148 ? -26.519 22.362  91.382  1.00 10.49  ? 155 LEU E CG  1 
ATOM   8694  C CD1 . LEU E  1 148 ? -27.331 23.596  91.036  1.00 12.02  ? 155 LEU E CD1 1 
ATOM   8695  C CD2 . LEU E  1 148 ? -25.527 22.678  92.489  1.00 10.30  ? 155 LEU E CD2 1 
ATOM   8696  N N   . SER E  1 149 ? -29.779 20.628  93.566  1.00 11.26  ? 156 SER E N   1 
ATOM   8697  C CA  . SER E  1 149 ? -30.644 20.987  94.696  1.00 11.34  ? 156 SER E CA  1 
ATOM   8698  C C   . SER E  1 149 ? -30.493 22.446  95.148  1.00 12.29  ? 156 SER E C   1 
ATOM   8699  O O   . SER E  1 149 ? -29.498 23.105  94.830  1.00 12.52  ? 156 SER E O   1 
ATOM   8700  C CB  . SER E  1 149 ? -30.368 20.060  95.882  1.00 10.98  ? 156 SER E CB  1 
ATOM   8701  O OG  . SER E  1 149 ? -30.550 18.702  95.532  1.00 8.00   ? 156 SER E OG  1 
ATOM   8702  N N   . ASN E  1 150 ? -31.481 22.931  95.903  1.00 12.72  ? 157 ASN E N   1 
ATOM   8703  C CA  . ASN E  1 150 ? -31.481 24.301  96.429  1.00 13.38  ? 157 ASN E CA  1 
ATOM   8704  C C   . ASN E  1 150 ? -30.349 24.609  97.411  1.00 13.47  ? 157 ASN E C   1 
ATOM   8705  O O   . ASN E  1 150 ? -29.923 25.759  97.531  1.00 14.05  ? 157 ASN E O   1 
ATOM   8706  C CB  . ASN E  1 150 ? -32.832 24.637  97.072  1.00 13.59  ? 157 ASN E CB  1 
ATOM   8707  C CG  . ASN E  1 150 ? -33.903 24.981  96.047  1.00 14.92  ? 157 ASN E CG  1 
ATOM   8708  O OD1 . ASN E  1 150 ? -33.621 25.566  94.997  1.00 13.45  ? 157 ASN E OD1 1 
ATOM   8709  N ND2 . ASN E  1 150 ? -35.147 24.629  96.356  1.00 15.95  ? 157 ASN E ND2 1 
ATOM   8710  N N   . SER E  1 151 ? -29.877 23.581  98.112  1.00 13.17  ? 158 SER E N   1 
ATOM   8711  C CA  . SER E  1 151 ? -28.787 23.721  99.078  1.00 12.63  ? 158 SER E CA  1 
ATOM   8712  C C   . SER E  1 151 ? -28.100 22.378  99.291  1.00 12.64  ? 158 SER E C   1 
ATOM   8713  O O   . SER E  1 151 ? -28.646 21.335  98.923  1.00 12.60  ? 158 SER E O   1 
ATOM   8714  C CB  . SER E  1 151 ? -29.310 24.268  100.413 1.00 12.53  ? 158 SER E CB  1 
ATOM   8715  O OG  . SER E  1 151 ? -30.322 23.434  100.951 1.00 10.96  ? 158 SER E OG  1 
ATOM   8716  N N   . ASP E  1 152 A -26.907 22.412  99.884  1.00 12.71  ? 158 ASP E N   1 
ATOM   8717  C CA  . ASP E  1 152 A -26.150 21.201  100.208 1.00 12.80  ? 158 ASP E CA  1 
ATOM   8718  C C   . ASP E  1 152 A -27.039 20.093  100.776 1.00 12.62  ? 158 ASP E C   1 
ATOM   8719  O O   . ASP E  1 152 A -27.817 20.327  101.705 1.00 13.01  ? 158 ASP E O   1 
ATOM   8720  C CB  . ASP E  1 152 A -25.034 21.517  101.209 1.00 12.98  ? 158 ASP E CB  1 
ATOM   8721  C CG  . ASP E  1 152 A -23.883 22.303  100.592 1.00 14.27  ? 158 ASP E CG  1 
ATOM   8722  O OD1 . ASP E  1 152 A -23.845 22.473  99.352  1.00 12.69  ? 158 ASP E OD1 1 
ATOM   8723  O OD2 . ASP E  1 152 A -23.005 22.746  101.364 1.00 13.12  ? 158 ASP E OD2 1 
ATOM   8724  N N   . ASN E  1 153 B -26.934 18.904  100.183 1.00 11.92  ? 158 ASN E N   1 
ATOM   8725  C CA  . ASN E  1 153 B -27.583 17.681  100.682 1.00 10.96  ? 158 ASN E CA  1 
ATOM   8726  C C   . ASN E  1 153 B -29.121 17.611  100.585 1.00 10.61  ? 158 ASN E C   1 
ATOM   8727  O O   . ASN E  1 153 B -29.737 16.647  101.050 1.00 10.01  ? 158 ASN E O   1 
ATOM   8728  C CB  . ASN E  1 153 B -27.099 17.355  102.105 1.00 10.94  ? 158 ASN E CB  1 
ATOM   8729  C CG  . ASN E  1 153 B -25.585 17.248  102.196 1.00 9.93   ? 158 ASN E CG  1 
ATOM   8730  O OD1 . ASN E  1 153 B -24.955 16.499  101.449 1.00 11.90  ? 158 ASN E OD1 1 
ATOM   8731  N ND2 . ASN E  1 153 B -24.996 17.995  103.117 1.00 8.16   ? 158 ASN E ND2 1 
ATOM   8732  N N   . ALA E  1 154 ? -29.736 18.616  99.968  1.00 10.28  ? 159 ALA E N   1 
ATOM   8733  C CA  . ALA E  1 154 ? -31.185 18.616  99.786  1.00 10.39  ? 159 ALA E CA  1 
ATOM   8734  C C   . ALA E  1 154 ? -31.609 17.656  98.671  1.00 10.54  ? 159 ALA E C   1 
ATOM   8735  O O   . ALA E  1 154 ? -30.880 17.462  97.694  1.00 10.29  ? 159 ALA E O   1 
ATOM   8736  C CB  . ALA E  1 154 ? -31.693 20.026  99.512  1.00 9.68   ? 159 ALA E CB  1 
ATOM   8737  N N   . ALA E  1 155 ? -32.788 17.057  98.833  1.00 10.56  ? 160 ALA E N   1 
ATOM   8738  C CA  . ALA E  1 155 ? -33.340 16.135  97.843  1.00 10.28  ? 160 ALA E CA  1 
ATOM   8739  C C   . ALA E  1 155 ? -33.676 16.855  96.544  1.00 10.21  ? 160 ALA E C   1 
ATOM   8740  O O   . ALA E  1 155 ? -34.427 17.835  96.541  1.00 9.83   ? 160 ALA E O   1 
ATOM   8741  C CB  . ALA E  1 155 ? -34.573 15.437  98.392  1.00 9.89   ? 160 ALA E CB  1 
ATOM   8742  N N   . PHE E  1 156 ? -33.102 16.366  95.448  1.00 9.98   ? 161 PHE E N   1 
ATOM   8743  C CA  . PHE E  1 156 ? -33.440 16.840  94.114  1.00 9.32   ? 161 PHE E CA  1 
ATOM   8744  C C   . PHE E  1 156 ? -34.750 16.171  93.695  1.00 9.71   ? 161 PHE E C   1 
ATOM   8745  O O   . PHE E  1 156 ? -34.833 14.944  93.670  1.00 9.95   ? 161 PHE E O   1 
ATOM   8746  C CB  . PHE E  1 156 ? -32.316 16.496  93.134  1.00 8.45   ? 161 PHE E CB  1 
ATOM   8747  C CG  . PHE E  1 156 ? -32.461 17.145  91.788  1.00 7.68   ? 161 PHE E CG  1 
ATOM   8748  C CD1 . PHE E  1 156 ? -31.694 18.254  91.456  1.00 4.67   ? 161 PHE E CD1 1 
ATOM   8749  C CD2 . PHE E  1 156 ? -33.361 16.647  90.849  1.00 5.99   ? 161 PHE E CD2 1 
ATOM   8750  C CE1 . PHE E  1 156 ? -31.823 18.857  90.216  1.00 2.58   ? 161 PHE E CE1 1 
ATOM   8751  C CE2 . PHE E  1 156 ? -33.496 17.244  89.603  1.00 4.33   ? 161 PHE E CE2 1 
ATOM   8752  C CZ  . PHE E  1 156 ? -32.727 18.352  89.286  1.00 2.99   ? 161 PHE E CZ  1 
ATOM   8753  N N   . PRO E  1 157 ? -35.784 16.974  93.378  1.00 10.58  ? 162 PRO E N   1 
ATOM   8754  C CA  . PRO E  1 157 ? -37.108 16.433  93.041  1.00 11.33  ? 162 PRO E CA  1 
ATOM   8755  C C   . PRO E  1 157 ? -37.111 15.648  91.737  1.00 12.12  ? 162 PRO E C   1 
ATOM   8756  O O   . PRO E  1 157 ? -36.464 16.051  90.765  1.00 12.95  ? 162 PRO E O   1 
ATOM   8757  C CB  . PRO E  1 157 ? -37.984 17.688  92.893  1.00 10.88  ? 162 PRO E CB  1 
ATOM   8758  C CG  . PRO E  1 157 ? -37.235 18.773  93.587  1.00 11.95  ? 162 PRO E CG  1 
ATOM   8759  C CD  . PRO E  1 157 ? -35.785 18.446  93.390  1.00 10.38  ? 162 PRO E CD  1 
ATOM   8760  N N   . GLN E  1 158 ? -37.832 14.531  91.729  1.00 12.74  ? 163 GLN E N   1 
ATOM   8761  C CA  . GLN E  1 158 ? -38.030 13.740  90.519  1.00 13.16  ? 163 GLN E CA  1 
ATOM   8762  C C   . GLN E  1 158 ? -38.686 14.624  89.463  1.00 13.09  ? 163 GLN E C   1 
ATOM   8763  O O   . GLN E  1 158 ? -39.747 15.198  89.703  1.00 13.06  ? 163 GLN E O   1 
ATOM   8764  C CB  . GLN E  1 158 ? -38.903 12.517  90.825  1.00 12.91  ? 163 GLN E CB  1 
ATOM   8765  C CG  . GLN E  1 158 ? -39.201 11.617  89.622  1.00 14.93  ? 163 GLN E CG  1 
ATOM   8766  C CD  . GLN E  1 158 ? -37.987 10.837  89.142  1.00 14.49  ? 163 GLN E CD  1 
ATOM   8767  O OE1 . GLN E  1 158 ? -37.350 10.115  89.908  1.00 13.00  ? 163 GLN E OE1 1 
ATOM   8768  N NE2 . GLN E  1 158 ? -37.669 10.977  87.863  1.00 15.80  ? 163 GLN E NE2 1 
ATOM   8769  N N   . MET E  1 159 ? -38.040 14.751  88.309  1.00 13.43  ? 164 MET E N   1 
ATOM   8770  C CA  . MET E  1 159 ? -38.543 15.627  87.253  1.00 13.98  ? 164 MET E CA  1 
ATOM   8771  C C   . MET E  1 159 ? -38.737 14.934  85.919  1.00 13.88  ? 164 MET E C   1 
ATOM   8772  O O   . MET E  1 159 ? -38.095 13.928  85.619  1.00 14.39  ? 164 MET E O   1 
ATOM   8773  C CB  . MET E  1 159 ? -37.616 16.823  87.055  1.00 14.21  ? 164 MET E CB  1 
ATOM   8774  C CG  . MET E  1 159 ? -37.890 17.981  87.977  1.00 17.24  ? 164 MET E CG  1 
ATOM   8775  S SD  . MET E  1 159 ? -36.668 19.282  87.759  1.00 19.92  ? 164 MET E SD  1 
ATOM   8776  C CE  . MET E  1 159 ? -37.344 20.525  88.858  1.00 21.67  ? 164 MET E CE  1 
ATOM   8777  N N   . THR E  1 160 ? -39.630 15.507  85.122  1.00 13.95  ? 165 THR E N   1 
ATOM   8778  C CA  . THR E  1 160 ? -39.852 15.092  83.751  1.00 13.32  ? 165 THR E CA  1 
ATOM   8779  C C   . THR E  1 160 ? -39.844 16.344  82.877  1.00 12.81  ? 165 THR E C   1 
ATOM   8780  O O   . THR E  1 160 ? -40.502 17.334  83.196  1.00 12.51  ? 165 THR E O   1 
ATOM   8781  C CB  . THR E  1 160 ? -41.184 14.335  83.615  1.00 13.27  ? 165 THR E CB  1 
ATOM   8782  O OG1 . THR E  1 160 ? -41.208 13.253  84.555  1.00 14.69  ? 165 THR E OG1 1 
ATOM   8783  C CG2 . THR E  1 160 ? -41.355 13.777  82.214  1.00 14.17  ? 165 THR E CG2 1 
ATOM   8784  N N   . LYS E  1 161 ? -39.070 16.304  81.796  1.00 12.77  ? 166 LYS E N   1 
ATOM   8785  C CA  . LYS E  1 161 ? -38.996 17.415  80.848  1.00 12.44  ? 166 LYS E CA  1 
ATOM   8786  C C   . LYS E  1 161 ? -39.085 16.891  79.424  1.00 12.80  ? 166 LYS E C   1 
ATOM   8787  O O   . LYS E  1 161 ? -38.296 16.035  79.017  1.00 13.43  ? 166 LYS E O   1 
ATOM   8788  C CB  . LYS E  1 161 ? -37.712 18.228  81.046  1.00 11.72  ? 166 LYS E CB  1 
ATOM   8789  C CG  . LYS E  1 161 ? -37.638 18.994  82.367  1.00 13.78  ? 166 LYS E CG  1 
ATOM   8790  C CD  . LYS E  1 161 ? -38.740 20.047  82.485  1.00 15.13  ? 166 LYS E CD  1 
ATOM   8791  C CE  . LYS E  1 161 ? -38.755 20.688  83.859  1.00 14.34  ? 166 LYS E CE  1 
ATOM   8792  N NZ  . LYS E  1 161 ? -39.952 21.557  84.033  1.00 18.48  ? 166 LYS E NZ  1 
ATOM   8793  N N   . ALA E  1 162 ? -40.057 17.406  78.674  1.00 12.76  ? 167 ALA E N   1 
ATOM   8794  C CA  . ALA E  1 162 ? -40.333 16.920  77.326  1.00 12.52  ? 167 ALA E CA  1 
ATOM   8795  C C   . ALA E  1 162 ? -40.260 18.037  76.290  1.00 12.80  ? 167 ALA E C   1 
ATOM   8796  O O   . ALA E  1 162 ? -40.616 19.182  76.569  1.00 12.72  ? 167 ALA E O   1 
ATOM   8797  C CB  . ALA E  1 162 ? -41.690 16.233  77.278  1.00 11.65  ? 167 ALA E CB  1 
ATOM   8798  N N   . TYR E  1 163 ? -39.791 17.687  75.097  1.00 12.87  ? 168 TYR E N   1 
ATOM   8799  C CA  . TYR E  1 163 ? -39.651 18.633  74.005  1.00 12.72  ? 168 TYR E CA  1 
ATOM   8800  C C   . TYR E  1 163 ? -40.059 17.976  72.698  1.00 13.46  ? 168 TYR E C   1 
ATOM   8801  O O   . TYR E  1 163 ? -39.527 16.928  72.332  1.00 13.43  ? 168 TYR E O   1 
ATOM   8802  C CB  . TYR E  1 163 ? -38.205 19.135  73.917  1.00 12.27  ? 168 TYR E CB  1 
ATOM   8803  C CG  . TYR E  1 163 ? -37.877 19.878  72.636  1.00 11.68  ? 168 TYR E CG  1 
ATOM   8804  C CD1 . TYR E  1 163 ? -38.186 21.232  72.493  1.00 9.36   ? 168 TYR E CD1 1 
ATOM   8805  C CD2 . TYR E  1 163 ? -37.257 19.226  71.568  1.00 8.79   ? 168 TYR E CD2 1 
ATOM   8806  C CE1 . TYR E  1 163 ? -37.890 21.917  71.322  1.00 6.49   ? 168 TYR E CE1 1 
ATOM   8807  C CE2 . TYR E  1 163 ? -36.957 19.903  70.390  1.00 7.42   ? 168 TYR E CE2 1 
ATOM   8808  C CZ  . TYR E  1 163 ? -37.276 21.247  70.275  1.00 8.36   ? 168 TYR E CZ  1 
ATOM   8809  O OH  . TYR E  1 163 ? -36.982 21.921  69.111  1.00 9.04   ? 168 TYR E OH  1 
ATOM   8810  N N   . ARG E  1 164 ? -41.010 18.596  72.005  1.00 14.46  ? 169 ARG E N   1 
ATOM   8811  C CA  . ARG E  1 164 ? -41.393 18.166  70.665  1.00 15.29  ? 169 ARG E CA  1 
ATOM   8812  C C   . ARG E  1 164 ? -40.621 18.985  69.632  1.00 15.54  ? 169 ARG E C   1 
ATOM   8813  O O   . ARG E  1 164 ? -40.449 20.197  69.789  1.00 15.70  ? 169 ARG E O   1 
ATOM   8814  C CB  . ARG E  1 164 ? -42.901 18.325  70.456  1.00 15.11  ? 169 ARG E CB  1 
ATOM   8815  C CG  . ARG E  1 164 ? -43.427 17.726  69.151  1.00 17.20  ? 169 ARG E CG  1 
ATOM   8816  C CD  . ARG E  1 164 ? -44.922 17.980  68.962  1.00 22.65  ? 169 ARG E CD  1 
ATOM   8817  N NE  . ARG E  1 164 ? -45.241 19.409  68.900  1.00 28.12  ? 169 ARG E NE  1 
ATOM   8818  C CZ  . ARG E  1 164 ? -45.233 20.144  67.788  1.00 30.07  ? 169 ARG E CZ  1 
ATOM   8819  N NH1 . ARG E  1 164 ? -44.923 19.599  66.615  1.00 29.11  ? 169 ARG E NH1 1 
ATOM   8820  N NH2 . ARG E  1 164 ? -45.536 21.436  67.850  1.00 29.15  ? 169 ARG E NH2 1 
ATOM   8821  N N   . ASN E  1 165 ? -40.145 18.308  68.590  1.00 15.74  ? 170 ASN E N   1 
ATOM   8822  C CA  . ASN E  1 165 ? -39.486 18.964  67.467  1.00 16.15  ? 170 ASN E CA  1 
ATOM   8823  C C   . ASN E  1 165 ? -40.521 19.578  66.529  1.00 16.17  ? 170 ASN E C   1 
ATOM   8824  O O   . ASN E  1 165 ? -41.175 18.858  65.773  1.00 16.93  ? 170 ASN E O   1 
ATOM   8825  C CB  . ASN E  1 165 ? -38.597 17.966  66.711  1.00 16.36  ? 170 ASN E CB  1 
ATOM   8826  C CG  . ASN E  1 165 ? -37.960 18.566  65.461  1.00 17.29  ? 170 ASN E CG  1 
ATOM   8827  O OD1 . ASN E  1 165 ? -38.125 19.749  65.166  1.00 17.97  ? 170 ASN E OD1 1 
ATOM   8828  N ND2 . ASN E  1 165 ? -37.222 17.744  64.725  1.00 20.26  ? 170 ASN E ND2 1 
ATOM   8829  N N   . PRO E  1 166 ? -40.660 20.918  66.561  1.00 16.30  ? 171 PRO E N   1 
ATOM   8830  C CA  . PRO E  1 166 ? -41.691 21.602  65.779  1.00 16.03  ? 171 PRO E CA  1 
ATOM   8831  C C   . PRO E  1 166 ? -41.209 21.994  64.378  1.00 16.22  ? 171 PRO E C   1 
ATOM   8832  O O   . PRO E  1 166 ? -41.770 22.904  63.765  1.00 16.79  ? 171 PRO E O   1 
ATOM   8833  C CB  . PRO E  1 166 ? -41.962 22.858  66.610  1.00 15.55  ? 171 PRO E CB  1 
ATOM   8834  C CG  . PRO E  1 166 ? -40.650 23.140  67.327  1.00 16.23  ? 171 PRO E CG  1 
ATOM   8835  C CD  . PRO E  1 166 ? -39.802 21.881  67.276  1.00 16.48  ? 171 PRO E CD  1 
ATOM   8836  N N   . ARG E  1 167 ? -40.192 21.299  63.877  1.00 16.03  ? 172 ARG E N   1 
ATOM   8837  C CA  . ARG E  1 167 ? -39.500 21.718  62.667  1.00 16.45  ? 172 ARG E CA  1 
ATOM   8838  C C   . ARG E  1 167 ? -39.555 20.703  61.536  1.00 17.01  ? 172 ARG E C   1 
ATOM   8839  O O   . ARG E  1 167 ? -39.744 19.504  61.750  1.00 17.71  ? 172 ARG E O   1 
ATOM   8840  C CB  . ARG E  1 167 ? -38.034 22.074  62.967  1.00 16.54  ? 172 ARG E CB  1 
ATOM   8841  C CG  . ARG E  1 167 ? -37.840 23.223  63.953  1.00 16.16  ? 172 ARG E CG  1 
ATOM   8842  C CD  . ARG E  1 167 ? -37.775 24.563  63.259  1.00 15.11  ? 172 ARG E CD  1 
ATOM   8843  N NE  . ARG E  1 167 ? -36.459 24.814  62.681  1.00 18.05  ? 172 ARG E NE  1 
ATOM   8844  C CZ  . ARG E  1 167 ? -35.503 25.539  63.258  1.00 17.91  ? 172 ARG E CZ  1 
ATOM   8845  N NH1 . ARG E  1 167 ? -35.700 26.100  64.448  1.00 17.78  ? 172 ARG E NH1 1 
ATOM   8846  N NH2 . ARG E  1 167 ? -34.343 25.705  62.640  1.00 16.48  ? 172 ARG E NH2 1 
ATOM   8847  N N   . ASN E  1 168 ? -39.372 21.232  60.332  1.00 16.76  ? 173 ASN E N   1 
ATOM   8848  C CA  . ASN E  1 168 ? -39.283 20.489  59.083  1.00 16.30  ? 173 ASN E CA  1 
ATOM   8849  C C   . ASN E  1 168 ? -38.146 19.454  59.013  1.00 15.62  ? 173 ASN E C   1 
ATOM   8850  O O   . ASN E  1 168 ? -38.186 18.551  58.178  1.00 15.72  ? 173 ASN E O   1 
ATOM   8851  C CB  . ASN E  1 168 ? -39.137 21.502  57.934  1.00 16.87  ? 173 ASN E CB  1 
ATOM   8852  C CG  . ASN E  1 168 ? -38.334 22.750  58.346  1.00 16.72  ? 173 ASN E CG  1 
ATOM   8853  O OD1 . ASN E  1 168 ? -38.799 23.585  59.132  1.00 10.40  ? 173 ASN E OD1 1 
ATOM   8854  N ND2 . ASN E  1 168 ? -37.125 22.868  57.818  1.00 16.55  ? 173 ASN E ND2 1 
ATOM   8855  N N   . LYS E  1 169 ? -37.142 19.588  59.878  1.00 14.84  ? 174 LYS E N   1 
ATOM   8856  C CA  . LYS E  1 169 ? -35.961 18.711  59.850  1.00 14.30  ? 174 LYS E CA  1 
ATOM   8857  C C   . LYS E  1 169 ? -35.540 18.237  61.257  1.00 13.14  ? 174 LYS E C   1 
ATOM   8858  O O   . LYS E  1 169 ? -35.995 18.802  62.251  1.00 13.73  ? 174 LYS E O   1 
ATOM   8859  C CB  . LYS E  1 169 ? -34.804 19.402  59.113  1.00 15.00  ? 174 LYS E CB  1 
ATOM   8860  C CG  . LYS E  1 169 ? -34.164 20.573  59.856  1.00 16.24  ? 174 LYS E CG  1 
ATOM   8861  C CD  . LYS E  1 169 ? -33.251 21.370  58.937  1.00 18.70  ? 174 LYS E CD  1 
ATOM   8862  C CE  . LYS E  1 169 ? -33.994 22.525  58.280  1.00 19.22  ? 174 LYS E CE  1 
ATOM   8863  N NZ  . LYS E  1 169 ? -33.367 22.947  56.998  1.00 21.59  ? 174 LYS E NZ  1 
ATOM   8864  N N   . PRO E  1 170 ? -34.675 17.198  61.346  1.00 11.83  ? 175 PRO E N   1 
ATOM   8865  C CA  . PRO E  1 170 ? -34.341 16.603  62.649  1.00 11.28  ? 175 PRO E CA  1 
ATOM   8866  C C   . PRO E  1 170 ? -33.575 17.524  63.605  1.00 11.01  ? 175 PRO E C   1 
ATOM   8867  O O   . PRO E  1 170 ? -32.702 18.283  63.173  1.00 11.22  ? 175 PRO E O   1 
ATOM   8868  C CB  . PRO E  1 170 ? -33.474 15.395  62.272  1.00 10.23  ? 175 PRO E CB  1 
ATOM   8869  C CG  . PRO E  1 170 ? -32.923 15.722  60.945  1.00 9.85   ? 175 PRO E CG  1 
ATOM   8870  C CD  . PRO E  1 170 ? -33.995 16.489  60.245  1.00 11.85  ? 175 PRO E CD  1 
ATOM   8871  N N   . ALA E  1 171 ? -33.915 17.448  64.891  1.00 9.58   ? 176 ALA E N   1 
ATOM   8872  C CA  . ALA E  1 171 ? -33.247 18.234  65.926  1.00 9.23   ? 176 ALA E CA  1 
ATOM   8873  C C   . ALA E  1 171 ? -32.151 17.421  66.598  1.00 9.11   ? 176 ALA E C   1 
ATOM   8874  O O   . ALA E  1 171 ? -32.361 16.261  66.966  1.00 9.36   ? 176 ALA E O   1 
ATOM   8875  C CB  . ALA E  1 171 ? -34.253 18.713  66.968  1.00 9.08   ? 176 ALA E CB  1 
ATOM   8876  N N   . LEU E  1 172 ? -30.985 18.035  66.766  1.00 8.57   ? 177 LEU E N   1 
ATOM   8877  C CA  . LEU E  1 172 ? -29.885 17.380  67.458  1.00 8.56   ? 177 LEU E CA  1 
ATOM   8878  C C   . LEU E  1 172 ? -29.975 17.640  68.963  1.00 8.59   ? 177 LEU E C   1 
ATOM   8879  O O   . LEU E  1 172 ? -29.647 18.731  69.446  1.00 8.52   ? 177 LEU E O   1 
ATOM   8880  C CB  . LEU E  1 172 ? -28.538 17.810  66.872  1.00 8.18   ? 177 LEU E CB  1 
ATOM   8881  C CG  . LEU E  1 172 ? -27.248 17.239  67.467  1.00 8.45   ? 177 LEU E CG  1 
ATOM   8882  C CD1 . LEU E  1 172 ? -27.232 15.715  67.505  1.00 7.79   ? 177 LEU E CD1 1 
ATOM   8883  C CD2 . LEU E  1 172 ? -26.070 17.760  66.668  1.00 12.41  ? 177 LEU E CD2 1 
ATOM   8884  N N   . ILE E  1 173 ? -30.448 16.627  69.688  1.00 8.48   ? 178 ILE E N   1 
ATOM   8885  C CA  . ILE E  1 173 ? -30.700 16.734  71.124  1.00 7.53   ? 178 ILE E CA  1 
ATOM   8886  C C   . ILE E  1 173 ? -29.474 16.266  71.896  1.00 7.47   ? 178 ILE E C   1 
ATOM   8887  O O   . ILE E  1 173 ? -28.909 15.222  71.581  1.00 6.45   ? 178 ILE E O   1 
ATOM   8888  C CB  . ILE E  1 173 ? -31.943 15.908  71.535  1.00 6.49   ? 178 ILE E CB  1 
ATOM   8889  C CG1 . ILE E  1 173 ? -33.200 16.400  70.801  1.00 6.68   ? 178 ILE E CG1 1 
ATOM   8890  C CG2 . ILE E  1 173 ? -32.138 15.914  73.050  1.00 6.73   ? 178 ILE E CG2 1 
ATOM   8891  C CD1 . ILE E  1 173 ? -33.606 17.848  71.081  1.00 5.87   ? 178 ILE E CD1 1 
ATOM   8892  N N   . ILE E  1 174 ? -29.061 17.059  72.886  1.00 7.82   ? 179 ILE E N   1 
ATOM   8893  C CA  . ILE E  1 174 ? -27.894 16.742  73.719  1.00 8.56   ? 179 ILE E CA  1 
ATOM   8894  C C   . ILE E  1 174 ? -28.256 16.822  75.190  1.00 8.10   ? 179 ILE E C   1 
ATOM   8895  O O   . ILE E  1 174 ? -29.114 17.609  75.586  1.00 8.33   ? 179 ILE E O   1 
ATOM   8896  C CB  . ILE E  1 174 ? -26.698 17.721  73.495  1.00 8.84   ? 179 ILE E CB  1 
ATOM   8897  C CG1 . ILE E  1 174 ? -26.630 18.236  72.052  1.00 10.95  ? 179 ILE E CG1 1 
ATOM   8898  C CG2 . ILE E  1 174 ? -25.376 17.078  73.939  1.00 8.70   ? 179 ILE E CG2 1 
ATOM   8899  C CD1 . ILE E  1 174 ? -26.183 17.207  71.023  1.00 16.29  ? 179 ILE E CD1 1 
ATOM   8900  N N   . TRP E  1 175 ? -27.588 16.005  75.996  1.00 7.69   ? 180 TRP E N   1 
ATOM   8901  C CA  . TRP E  1 175 ? -27.712 16.057  77.446  1.00 7.33   ? 180 TRP E CA  1 
ATOM   8902  C C   . TRP E  1 175 ? -26.419 15.534  78.049  1.00 7.04   ? 180 TRP E C   1 
ATOM   8903  O O   . TRP E  1 175 ? -25.628 14.875  77.365  1.00 6.75   ? 180 TRP E O   1 
ATOM   8904  C CB  . TRP E  1 175 ? -28.901 15.222  77.925  1.00 6.85   ? 180 TRP E CB  1 
ATOM   8905  C CG  . TRP E  1 175 ? -28.777 13.778  77.574  1.00 8.39   ? 180 TRP E CG  1 
ATOM   8906  C CD1 . TRP E  1 175 ? -28.267 12.783  78.358  1.00 6.08   ? 180 TRP E CD1 1 
ATOM   8907  C CD2 . TRP E  1 175 ? -29.154 13.161  76.337  1.00 8.45   ? 180 TRP E CD2 1 
ATOM   8908  N NE1 . TRP E  1 175 ? -28.309 11.586  77.689  1.00 6.02   ? 180 TRP E NE1 1 
ATOM   8909  C CE2 . TRP E  1 175 ? -28.849 11.789  76.446  1.00 8.01   ? 180 TRP E CE2 1 
ATOM   8910  C CE3 . TRP E  1 175 ? -29.724 13.635  75.149  1.00 9.21   ? 180 TRP E CE3 1 
ATOM   8911  C CZ2 . TRP E  1 175 ? -29.094 10.883  75.411  1.00 11.22  ? 180 TRP E CZ2 1 
ATOM   8912  C CZ3 . TRP E  1 175 ? -29.966 12.735  74.119  1.00 10.49  ? 180 TRP E CZ3 1 
ATOM   8913  C CH2 . TRP E  1 175 ? -29.649 11.374  74.257  1.00 10.99  ? 180 TRP E CH2 1 
ATOM   8914  N N   . GLY E  1 176 ? -26.207 15.828  79.327  1.00 6.51   ? 181 GLY E N   1 
ATOM   8915  C CA  . GLY E  1 176 ? -25.017 15.372  80.022  1.00 6.16   ? 181 GLY E CA  1 
ATOM   8916  C C   . GLY E  1 176 ? -25.335 14.628  81.302  1.00 6.12   ? 181 GLY E C   1 
ATOM   8917  O O   . GLY E  1 176 ? -26.332 14.919  81.970  1.00 6.51   ? 181 GLY E O   1 
ATOM   8918  N N   . VAL E  1 177 ? -24.488 13.654  81.624  1.00 5.47   ? 182 VAL E N   1 
ATOM   8919  C CA  . VAL E  1 177 ? -24.493 13.007  82.930  1.00 5.87   ? 182 VAL E CA  1 
ATOM   8920  C C   . VAL E  1 177 ? -23.292 13.536  83.716  1.00 6.39   ? 182 VAL E C   1 
ATOM   8921  O O   . VAL E  1 177 ? -22.163 13.526  83.217  1.00 5.73   ? 182 VAL E O   1 
ATOM   8922  C CB  . VAL E  1 177 ? -24.392 11.467  82.817  1.00 5.63   ? 182 VAL E CB  1 
ATOM   8923  C CG1 . VAL E  1 177 ? -24.518 10.818  84.189  1.00 5.66   ? 182 VAL E CG1 1 
ATOM   8924  C CG2 . VAL E  1 177 ? -25.455 10.923  81.880  1.00 6.17   ? 182 VAL E CG2 1 
ATOM   8925  N N   . HIS E  1 178 ? -23.533 14.001  84.937  1.00 6.92   ? 183 HIS E N   1 
ATOM   8926  C CA  . HIS E  1 178 ? -22.444 14.454  85.787  1.00 7.30   ? 183 HIS E CA  1 
ATOM   8927  C C   . HIS E  1 178 ? -22.017 13.383  86.771  1.00 7.75   ? 183 HIS E C   1 
ATOM   8928  O O   . HIS E  1 178 ? -22.758 13.041  87.690  1.00 8.73   ? 183 HIS E O   1 
ATOM   8929  C CB  . HIS E  1 178 ? -22.808 15.732  86.543  1.00 6.99   ? 183 HIS E CB  1 
ATOM   8930  C CG  . HIS E  1 178 ? -21.767 16.148  87.535  1.00 7.69   ? 183 HIS E CG  1 
ATOM   8931  N ND1 . HIS E  1 178 ? -21.989 16.145  88.894  1.00 7.50   ? 183 HIS E ND1 1 
ATOM   8932  C CD2 . HIS E  1 178 ? -20.484 16.546  87.364  1.00 8.61   ? 183 HIS E CD2 1 
ATOM   8933  C CE1 . HIS E  1 178 ? -20.894 16.540  89.517  1.00 8.07   ? 183 HIS E CE1 1 
ATOM   8934  N NE2 . HIS E  1 178 ? -19.965 16.791  88.611  1.00 6.52   ? 183 HIS E NE2 1 
ATOM   8935  N N   . HIS E  1 179 ? -20.810 12.869  86.577  1.00 8.21   ? 184 HIS E N   1 
ATOM   8936  C CA  . HIS E  1 179 ? -20.230 11.901  87.493  1.00 8.91   ? 184 HIS E CA  1 
ATOM   8937  C C   . HIS E  1 179 ? -19.373 12.650  88.508  1.00 9.66   ? 184 HIS E C   1 
ATOM   8938  O O   . HIS E  1 179 ? -18.337 13.214  88.154  1.00 9.72   ? 184 HIS E O   1 
ATOM   8939  C CB  . HIS E  1 179 ? -19.399 10.872  86.721  1.00 8.80   ? 184 HIS E CB  1 
ATOM   8940  C CG  . HIS E  1 179 ? -20.100 10.317  85.520  1.00 7.07   ? 184 HIS E CG  1 
ATOM   8941  N ND1 . HIS E  1 179 ? -20.852 9.164   85.563  1.00 5.74   ? 184 HIS E ND1 1 
ATOM   8942  C CD2 . HIS E  1 179 ? -20.175 10.766  84.245  1.00 5.33   ? 184 HIS E CD2 1 
ATOM   8943  C CE1 . HIS E  1 179 ? -21.357 8.925   84.366  1.00 6.87   ? 184 HIS E CE1 1 
ATOM   8944  N NE2 . HIS E  1 179 ? -20.962 9.882   83.548  1.00 3.57   ? 184 HIS E NE2 1 
ATOM   8945  N N   . SER E  1 180 ? -19.823 12.668  89.762  1.00 10.05  ? 185 SER E N   1 
ATOM   8946  C CA  . SER E  1 180 ? -19.133 13.401  90.832  1.00 9.82   ? 185 SER E CA  1 
ATOM   8947  C C   . SER E  1 180 ? -17.786 12.775  91.210  1.00 10.39  ? 185 SER E C   1 
ATOM   8948  O O   . SER E  1 180 ? -17.493 11.636  90.836  1.00 10.38  ? 185 SER E O   1 
ATOM   8949  C CB  . SER E  1 180 ? -20.027 13.511  92.068  1.00 9.57   ? 185 SER E CB  1 
ATOM   8950  O OG  . SER E  1 180 ? -21.281 14.071  91.738  1.00 7.89   ? 185 SER E OG  1 
ATOM   8951  N N   . GLU E  1 181 ? -16.975 13.537  91.943  1.00 10.75  ? 186 GLU E N   1 
ATOM   8952  C CA  . GLU E  1 181 ? -15.653 13.098  92.392  1.00 11.33  ? 186 GLU E CA  1 
ATOM   8953  C C   . GLU E  1 181 ? -15.747 12.008  93.460  1.00 10.81  ? 186 GLU E C   1 
ATOM   8954  O O   . GLU E  1 181 ? -14.878 11.140  93.553  1.00 11.15  ? 186 GLU E O   1 
ATOM   8955  C CB  . GLU E  1 181 ? -14.854 14.299  92.922  1.00 12.22  ? 186 GLU E CB  1 
ATOM   8956  C CG  . GLU E  1 181 ? -13.558 13.964  93.689  1.00 15.73  ? 186 GLU E CG  1 
ATOM   8957  C CD  . GLU E  1 181 ? -12.421 13.445  92.803  1.00 20.55  ? 186 GLU E CD  1 
ATOM   8958  O OE1 . GLU E  1 181 ? -11.331 13.173  93.349  1.00 23.73  ? 186 GLU E OE1 1 
ATOM   8959  O OE2 . GLU E  1 181 ? -12.603 13.310  91.574  1.00 21.57  ? 186 GLU E OE2 1 
ATOM   8960  N N   . SER E  1 182 ? -16.802 12.075  94.267  1.00 9.88   ? 187 SER E N   1 
ATOM   8961  C CA  . SER E  1 182 ? -17.043 11.113  95.336  1.00 8.66   ? 187 SER E CA  1 
ATOM   8962  C C   . SER E  1 182 ? -18.542 10.935  95.535  1.00 8.31   ? 187 SER E C   1 
ATOM   8963  O O   . SER E  1 182 ? -19.345 11.696  94.980  1.00 7.91   ? 187 SER E O   1 
ATOM   8964  C CB  . SER E  1 182 ? -16.394 11.592  96.637  1.00 8.48   ? 187 SER E CB  1 
ATOM   8965  O OG  . SER E  1 182 ? -16.932 12.838  97.045  1.00 5.97   ? 187 SER E OG  1 
ATOM   8966  N N   . VAL E  1 183 ? -18.920 9.931   96.320  1.00 7.90   ? 188 VAL E N   1 
ATOM   8967  C CA  . VAL E  1 183 ? -20.322 9.735   96.664  1.00 7.94   ? 188 VAL E CA  1 
ATOM   8968  C C   . VAL E  1 183 ? -20.829 10.942  97.451  1.00 8.40   ? 188 VAL E C   1 
ATOM   8969  O O   . VAL E  1 183 ? -21.890 11.483  97.136  1.00 8.83   ? 188 VAL E O   1 
ATOM   8970  C CB  . VAL E  1 183 ? -20.566 8.421   97.453  1.00 8.05   ? 188 VAL E CB  1 
ATOM   8971  C CG1 . VAL E  1 183 ? -22.014 8.340   97.943  1.00 6.82   ? 188 VAL E CG1 1 
ATOM   8972  C CG2 . VAL E  1 183 ? -20.230 7.208   96.593  1.00 7.48   ? 188 VAL E CG2 1 
ATOM   8973  N N   . SER E  1 184 ? -20.058 11.380  98.447  1.00 8.72   ? 189 SER E N   1 
ATOM   8974  C CA  . SER E  1 184 ? -20.484 12.487  99.309  1.00 9.10   ? 189 SER E CA  1 
ATOM   8975  C C   . SER E  1 184 ? -20.741 13.760  98.501  1.00 9.02   ? 189 SER E C   1 
ATOM   8976  O O   . SER E  1 184 ? -21.655 14.527  98.816  1.00 8.62   ? 189 SER E O   1 
ATOM   8977  C CB  . SER E  1 184 ? -19.478 12.744  100.437 1.00 8.88   ? 189 SER E CB  1 
ATOM   8978  O OG  . SER E  1 184 ? -18.494 13.686  100.050 1.00 10.16  ? 189 SER E OG  1 
ATOM   8979  N N   . GLU E  1 185 ? -19.941 13.970  97.455  1.00 8.54   ? 190 GLU E N   1 
ATOM   8980  C CA  . GLU E  1 185 ? -20.145 15.098  96.555  1.00 8.25   ? 190 GLU E CA  1 
ATOM   8981  C C   . GLU E  1 185 ? -21.480 14.991  95.814  1.00 7.84   ? 190 GLU E C   1 
ATOM   8982  O O   . GLU E  1 185 ? -22.195 15.983  95.688  1.00 8.25   ? 190 GLU E O   1 
ATOM   8983  C CB  . GLU E  1 185 ? -18.982 15.254  95.571  1.00 8.09   ? 190 GLU E CB  1 
ATOM   8984  C CG  . GLU E  1 185 ? -19.036 16.552  94.768  1.00 8.93   ? 190 GLU E CG  1 
ATOM   8985  C CD  . GLU E  1 185 ? -17.903 16.684  93.771  1.00 13.64  ? 190 GLU E CD  1 
ATOM   8986  O OE1 . GLU E  1 185 ? -17.016 17.539  93.992  1.00 16.56  ? 190 GLU E OE1 1 
ATOM   8987  O OE2 . GLU E  1 185 ? -17.897 15.940  92.766  1.00 13.52  ? 190 GLU E OE2 1 
ATOM   8988  N N   . GLN E  1 186 ? -21.813 13.794  95.335  1.00 7.47   ? 191 GLN E N   1 
ATOM   8989  C CA  . GLN E  1 186 ? -23.108 13.560  94.684  1.00 7.74   ? 191 GLN E CA  1 
ATOM   8990  C C   . GLN E  1 186 ? -24.263 13.813  95.662  1.00 7.89   ? 191 GLN E C   1 
ATOM   8991  O O   . GLN E  1 186 ? -25.282 14.402  95.291  1.00 7.67   ? 191 GLN E O   1 
ATOM   8992  C CB  . GLN E  1 186 ? -23.184 12.143  94.094  1.00 7.71   ? 191 GLN E CB  1 
ATOM   8993  C CG  . GLN E  1 186 ? -24.467 11.853  93.323  1.00 5.41   ? 191 GLN E CG  1 
ATOM   8994  C CD  . GLN E  1 186 ? -24.554 10.416  92.845  1.00 6.01   ? 191 GLN E CD  1 
ATOM   8995  O OE1 . GLN E  1 186 ? -23.948 10.042  91.842  1.00 2.84   ? 191 GLN E OE1 1 
ATOM   8996  N NE2 . GLN E  1 186 ? -25.328 9.606   93.556  1.00 8.58   ? 191 GLN E NE2 1 
ATOM   8997  N N   . THR E  1 187 ? -24.083 13.371  96.908  1.00 7.85   ? 192 THR E N   1 
ATOM   8998  C CA  . THR E  1 187 ? -25.025 13.645  97.993  1.00 7.98   ? 192 THR E CA  1 
ATOM   8999  C C   . THR E  1 187 ? -25.128 15.151  98.269  1.00 8.21   ? 192 THR E C   1 
ATOM   9000  O O   . THR E  1 187 ? -26.199 15.648  98.592  1.00 8.51   ? 192 THR E O   1 
ATOM   9001  C CB  . THR E  1 187 ? -24.629 12.888  99.295  1.00 8.42   ? 192 THR E CB  1 
ATOM   9002  O OG1 . THR E  1 187 ? -24.537 11.480  99.032  1.00 8.35   ? 192 THR E OG1 1 
ATOM   9003  C CG2 . THR E  1 187 ? -25.647 13.126  100.414 1.00 6.12   ? 192 THR E CG2 1 
ATOM   9004  N N   . LYS E  1 188 ? -24.013 15.867  98.135  1.00 8.80   ? 193 LYS E N   1 
ATOM   9005  C CA  . LYS E  1 188 ? -23.982 17.309  98.381  1.00 9.32   ? 193 LYS E CA  1 
ATOM   9006  C C   . LYS E  1 188 ? -24.794 18.080  97.341  1.00 9.40   ? 193 LYS E C   1 
ATOM   9007  O O   . LYS E  1 188 ? -25.669 18.875  97.692  1.00 9.55   ? 193 LYS E O   1 
ATOM   9008  C CB  . LYS E  1 188 ? -22.533 17.816  98.440  1.00 9.73   ? 193 LYS E CB  1 
ATOM   9009  C CG  . LYS E  1 188 ? -22.377 19.335  98.627  1.00 10.99  ? 193 LYS E CG  1 
ATOM   9010  C CD  . LYS E  1 188 ? -20.974 19.712  99.110  1.00 13.59  ? 193 LYS E CD  1 
ATOM   9011  C CE  . LYS E  1 188 ? -19.919 19.609  98.009  1.00 14.60  ? 193 LYS E CE  1 
ATOM   9012  N NZ  . LYS E  1 188 ? -19.796 20.864  97.216  1.00 16.33  ? 193 LYS E NZ  1 
ATOM   9013  N N   . LEU E  1 189 ? -24.510 17.827  96.068  1.00 9.77   ? 194 LEU E N   1 
ATOM   9014  C CA  . LEU E  1 189 ? -25.129 18.563  94.969  1.00 10.09  ? 194 LEU E CA  1 
ATOM   9015  C C   . LEU E  1 189 ? -26.585 18.170  94.758  1.00 10.75  ? 194 LEU E C   1 
ATOM   9016  O O   . LEU E  1 189 ? -27.426 19.015  94.442  1.00 11.66  ? 194 LEU E O   1 
ATOM   9017  C CB  . LEU E  1 189 ? -24.343 18.352  93.671  1.00 9.92   ? 194 LEU E CB  1 
ATOM   9018  C CG  . LEU E  1 189 ? -22.828 18.585  93.687  1.00 9.30   ? 194 LEU E CG  1 
ATOM   9019  C CD1 . LEU E  1 189 ? -22.241 18.268  92.323  1.00 8.11   ? 194 LEU E CD1 1 
ATOM   9020  C CD2 . LEU E  1 189 ? -22.479 20.005  94.112  1.00 5.95   ? 194 LEU E CD2 1 
ATOM   9021  N N   . TYR E  1 190 ? -26.868 16.882  94.930  1.00 10.66  ? 195 TYR E N   1 
ATOM   9022  C CA  . TYR E  1 190 ? -28.198 16.329  94.693  1.00 10.66  ? 195 TYR E CA  1 
ATOM   9023  C C   . TYR E  1 190 ? -28.681 15.698  95.997  1.00 11.72  ? 195 TYR E C   1 
ATOM   9024  O O   . TYR E  1 190 ? -28.133 15.991  97.059  1.00 12.82  ? 195 TYR E O   1 
ATOM   9025  C CB  . TYR E  1 190 ? -28.134 15.324  93.535  1.00 10.06  ? 195 TYR E CB  1 
ATOM   9026  C CG  . TYR E  1 190 ? -27.198 15.769  92.419  1.00 7.87   ? 195 TYR E CG  1 
ATOM   9027  C CD1 . TYR E  1 190 ? -25.988 15.111  92.188  1.00 8.68   ? 195 TYR E CD1 1 
ATOM   9028  C CD2 . TYR E  1 190 ? -27.505 16.872  91.623  1.00 5.82   ? 195 TYR E CD2 1 
ATOM   9029  C CE1 . TYR E  1 190 ? -25.117 15.527  91.176  1.00 3.87   ? 195 TYR E CE1 1 
ATOM   9030  C CE2 . TYR E  1 190 ? -26.643 17.297  90.614  1.00 4.95   ? 195 TYR E CE2 1 
ATOM   9031  C CZ  . TYR E  1 190 ? -25.454 16.621  90.395  1.00 5.75   ? 195 TYR E CZ  1 
ATOM   9032  O OH  . TYR E  1 190 ? -24.610 17.043  89.391  1.00 4.84   ? 195 TYR E OH  1 
ATOM   9033  N N   . GLY E  1 191 ? -29.704 14.855  95.956  1.00 11.65  ? 196 GLY E N   1 
ATOM   9034  C CA  . GLY E  1 191 ? -30.104 14.162  97.184  1.00 12.77  ? 196 GLY E CA  1 
ATOM   9035  C C   . GLY E  1 191 ? -29.158 13.015  97.512  1.00 12.89  ? 196 GLY E C   1 
ATOM   9036  O O   . GLY E  1 191 ? -28.157 12.806  96.817  1.00 13.39  ? 196 GLY E O   1 
ATOM   9037  N N   . SER E  1 192 ? -29.458 12.276  98.577  1.00 12.21  ? 197 SER E N   1 
ATOM   9038  C CA  . SER E  1 192 ? -28.841 10.968  98.765  1.00 11.53  ? 197 SER E CA  1 
ATOM   9039  C C   . SER E  1 192 ? -29.707 9.951   98.027  1.00 11.20  ? 197 SER E C   1 
ATOM   9040  O O   . SER E  1 192 ? -30.883 10.214  97.759  1.00 10.19  ? 197 SER E O   1 
ATOM   9041  C CB  . SER E  1 192 ? -28.712 10.603  100.248 1.00 11.60  ? 197 SER E CB  1 
ATOM   9042  O OG  . SER E  1 192 ? -29.947 10.171  100.800 1.00 10.78  ? 197 SER E OG  1 
ATOM   9043  N N   . GLY E  1 193 ? -29.117 8.810   97.681  1.00 10.82  ? 198 GLY E N   1 
ATOM   9044  C CA  . GLY E  1 193 ? -29.852 7.719   97.053  1.00 10.92  ? 198 GLY E CA  1 
ATOM   9045  C C   . GLY E  1 193 ? -29.551 7.519   95.581  1.00 11.48  ? 198 GLY E C   1 
ATOM   9046  O O   . GLY E  1 193 ? -28.847 8.325   94.962  1.00 11.30  ? 198 GLY E O   1 
ATOM   9047  N N   . ASN E  1 194 ? -30.101 6.437   95.028  1.00 11.95  ? 199 ASN E N   1 
ATOM   9048  C CA  . ASN E  1 194 ? -29.909 6.067   93.623  1.00 12.18  ? 199 ASN E CA  1 
ATOM   9049  C C   . ASN E  1 194 ? -30.368 7.156   92.649  1.00 11.04  ? 199 ASN E C   1 
ATOM   9050  O O   . ASN E  1 194 ? -31.511 7.615   92.702  1.00 10.86  ? 199 ASN E O   1 
ATOM   9051  C CB  . ASN E  1 194 ? -30.616 4.739   93.308  1.00 12.74  ? 199 ASN E CB  1 
ATOM   9052  C CG  . ASN E  1 194 ? -29.993 3.544   94.032  1.00 15.45  ? 199 ASN E CG  1 
ATOM   9053  O OD1 . ASN E  1 194 ? -28.833 3.195   93.806  1.00 15.40  ? 199 ASN E OD1 1 
ATOM   9054  N ND2 . ASN E  1 194 ? -30.777 2.901   94.892  1.00 18.30  ? 199 ASN E ND2 1 
ATOM   9055  N N   . LYS E  1 195 ? -29.456 7.567   91.774  1.00 10.00  ? 200 LYS E N   1 
ATOM   9056  C CA  . LYS E  1 195 ? -29.741 8.578   90.762  1.00 8.99   ? 200 LYS E CA  1 
ATOM   9057  C C   . LYS E  1 195 ? -29.936 7.914   89.402  1.00 8.95   ? 200 LYS E C   1 
ATOM   9058  O O   . LYS E  1 195 ? -29.137 7.062   88.987  1.00 8.34   ? 200 LYS E O   1 
ATOM   9059  C CB  . LYS E  1 195 ? -28.611 9.608   90.694  1.00 8.48   ? 200 LYS E CB  1 
ATOM   9060  C CG  . LYS E  1 195 ? -28.243 10.256  92.028  1.00 8.51   ? 200 LYS E CG  1 
ATOM   9061  C CD  . LYS E  1 195 ? -29.088 11.487  92.353  1.00 7.24   ? 200 LYS E CD  1 
ATOM   9062  C CE  . LYS E  1 195 ? -30.212 11.171  93.309  1.00 3.25   ? 200 LYS E CE  1 
ATOM   9063  N NZ  . LYS E  1 195 ? -30.671 12.390  94.027  1.00 4.20   ? 200 LYS E NZ  1 
ATOM   9064  N N   . LEU E  1 196 ? -30.999 8.314   88.710  1.00 8.37   ? 201 LEU E N   1 
ATOM   9065  C CA  . LEU E  1 196 ? -31.397 7.658   87.472  1.00 7.87   ? 201 LEU E CA  1 
ATOM   9066  C C   . LEU E  1 196 ? -31.900 8.674   86.451  1.00 7.62   ? 201 LEU E C   1 
ATOM   9067  O O   . LEU E  1 196 ? -32.760 9.502   86.756  1.00 7.89   ? 201 LEU E O   1 
ATOM   9068  C CB  . LEU E  1 196 ? -32.457 6.588   87.777  1.00 7.44   ? 201 LEU E CB  1 
ATOM   9069  C CG  . LEU E  1 196 ? -33.012 5.591   86.750  1.00 7.04   ? 201 LEU E CG  1 
ATOM   9070  C CD1 . LEU E  1 196 ? -34.309 6.090   86.130  1.00 8.23   ? 201 LEU E CD1 1 
ATOM   9071  C CD2 . LEU E  1 196 ? -31.997 5.169   85.680  1.00 11.14  ? 201 LEU E CD2 1 
ATOM   9072  N N   . ILE E  1 197 ? -31.340 8.606   85.246  1.00 7.10   ? 202 ILE E N   1 
ATOM   9073  C CA  . ILE E  1 197 ? -31.715 9.486   84.145  1.00 6.27   ? 202 ILE E CA  1 
ATOM   9074  C C   . ILE E  1 197 ? -32.129 8.630   82.954  1.00 6.77   ? 202 ILE E C   1 
ATOM   9075  O O   . ILE E  1 197 ? -31.362 7.778   82.513  1.00 7.21   ? 202 ILE E O   1 
ATOM   9076  C CB  . ILE E  1 197 ? -30.539 10.402  83.709  1.00 6.24   ? 202 ILE E CB  1 
ATOM   9077  C CG1 . ILE E  1 197 ? -29.977 11.196  84.893  1.00 5.86   ? 202 ILE E CG1 1 
ATOM   9078  C CG2 . ILE E  1 197 ? -30.969 11.337  82.569  1.00 4.74   ? 202 ILE E CG2 1 
ATOM   9079  C CD1 . ILE E  1 197 ? -28.646 11.878  84.602  1.00 6.18   ? 202 ILE E CD1 1 
ATOM   9080  N N   . THR E  1 198 ? -33.337 8.853   82.439  1.00 7.30   ? 203 THR E N   1 
ATOM   9081  C CA  . THR E  1 198 ? -33.809 8.148   81.243  1.00 8.44   ? 203 THR E CA  1 
ATOM   9082  C C   . THR E  1 198 ? -34.142 9.126   80.119  1.00 9.85   ? 203 THR E C   1 
ATOM   9083  O O   . THR E  1 198 ? -34.847 10.118  80.327  1.00 9.08   ? 203 THR E O   1 
ATOM   9084  C CB  . THR E  1 198 ? -35.058 7.272   81.512  1.00 7.98   ? 203 THR E CB  1 
ATOM   9085  O OG1 . THR E  1 198 ? -36.174 8.113   81.828  1.00 10.96  ? 203 THR E OG1 1 
ATOM   9086  C CG2 . THR E  1 198 ? -34.818 6.296   82.648  1.00 4.56   ? 203 THR E CG2 1 
ATOM   9087  N N   . VAL E  1 199 ? -33.628 8.824   78.929  1.00 11.47  ? 204 VAL E N   1 
ATOM   9088  C CA  . VAL E  1 199 ? -33.890 9.614   77.732  1.00 12.32  ? 204 VAL E CA  1 
ATOM   9089  C C   . VAL E  1 199 ? -34.669 8.750   76.738  1.00 14.10  ? 204 VAL E C   1 
ATOM   9090  O O   . VAL E  1 199 ? -34.289 7.608   76.462  1.00 14.11  ? 204 VAL E O   1 
ATOM   9091  C CB  . VAL E  1 199 ? -32.578 10.129  77.107  1.00 11.94  ? 204 VAL E CB  1 
ATOM   9092  C CG1 . VAL E  1 199 ? -32.865 11.048  75.930  1.00 10.25  ? 204 VAL E CG1 1 
ATOM   9093  C CG2 . VAL E  1 199 ? -31.737 10.853  78.159  1.00 11.55  ? 204 VAL E CG2 1 
ATOM   9094  N N   . ARG E  1 200 ? -35.763 9.293   76.210  1.00 15.73  ? 205 ARG E N   1 
ATOM   9095  C CA  . ARG E  1 200 ? -36.679 8.506   75.392  1.00 17.48  ? 205 ARG E CA  1 
ATOM   9096  C C   . ARG E  1 200 ? -37.336 9.308   74.265  1.00 17.77  ? 205 ARG E C   1 
ATOM   9097  O O   . ARG E  1 200 ? -37.991 10.326  74.510  1.00 18.20  ? 205 ARG E O   1 
ATOM   9098  C CB  . ARG E  1 200 ? -37.752 7.871   76.284  1.00 17.83  ? 205 ARG E CB  1 
ATOM   9099  C CG  . ARG E  1 200 ? -38.425 6.637   75.699  1.00 23.85  ? 205 ARG E CG  1 
ATOM   9100  C CD  . ARG E  1 200 ? -39.437 6.035   76.672  1.00 30.96  ? 205 ARG E CD  1 
ATOM   9101  N NE  . ARG E  1 200 ? -38.860 5.796   77.998  1.00 37.05  ? 205 ARG E NE  1 
ATOM   9102  C CZ  . ARG E  1 200 ? -39.521 5.280   79.034  1.00 38.47  ? 205 ARG E CZ  1 
ATOM   9103  N NH1 . ARG E  1 200 ? -40.798 4.932   78.918  1.00 39.50  ? 205 ARG E NH1 1 
ATOM   9104  N NH2 . ARG E  1 200 ? -38.899 5.107   80.192  1.00 38.45  ? 205 ARG E NH2 1 
ATOM   9105  N N   . SER E  1 201 ? -37.134 8.847   73.034  1.00 17.66  ? 206 SER E N   1 
ATOM   9106  C CA  . SER E  1 201 ? -37.915 9.296   71.887  1.00 17.77  ? 206 SER E CA  1 
ATOM   9107  C C   . SER E  1 201 ? -38.657 8.079   71.330  1.00 18.03  ? 206 SER E C   1 
ATOM   9108  O O   . SER E  1 201 ? -38.723 7.038   71.990  1.00 18.18  ? 206 SER E O   1 
ATOM   9109  C CB  . SER E  1 201 ? -37.018 9.931   70.824  1.00 17.64  ? 206 SER E CB  1 
ATOM   9110  O OG  . SER E  1 201 ? -36.359 8.947   70.045  1.00 19.03  ? 206 SER E OG  1 
ATOM   9111  N N   . SER E  1 202 ? -39.215 8.197   70.129  1.00 17.72  ? 207 SER E N   1 
ATOM   9112  C CA  . SER E  1 202 ? -39.899 7.058   69.520  1.00 17.78  ? 207 SER E CA  1 
ATOM   9113  C C   . SER E  1 202 ? -38.909 6.084   68.864  1.00 17.80  ? 207 SER E C   1 
ATOM   9114  O O   . SER E  1 202 ? -39.287 4.984   68.458  1.00 17.62  ? 207 SER E O   1 
ATOM   9115  C CB  . SER E  1 202 ? -40.985 7.516   68.531  1.00 17.69  ? 207 SER E CB  1 
ATOM   9116  O OG  . SER E  1 202 ? -40.428 7.958   67.306  1.00 17.83  ? 207 SER E OG  1 
ATOM   9117  N N   . LYS E  1 203 ? -37.643 6.493   68.784  1.00 17.91  ? 208 LYS E N   1 
ATOM   9118  C CA  . LYS E  1 203 ? -36.588 5.672   68.187  1.00 18.31  ? 208 LYS E CA  1 
ATOM   9119  C C   . LYS E  1 203 ? -35.422 5.417   69.148  1.00 18.51  ? 208 LYS E C   1 
ATOM   9120  O O   . LYS E  1 203 ? -34.549 4.590   68.870  1.00 18.39  ? 208 LYS E O   1 
ATOM   9121  C CB  . LYS E  1 203 ? -36.059 6.325   66.904  1.00 18.46  ? 208 LYS E CB  1 
ATOM   9122  C CG  . LYS E  1 203 ? -36.976 6.211   65.692  1.00 19.90  ? 208 LYS E CG  1 
ATOM   9123  C CD  . LYS E  1 203 ? -36.287 6.767   64.450  1.00 23.54  ? 208 LYS E CD  1 
ATOM   9124  C CE  . LYS E  1 203 ? -37.100 6.528   63.181  1.00 25.07  ? 208 LYS E CE  1 
ATOM   9125  N NZ  . LYS E  1 203 ? -36.414 7.106   61.982  1.00 22.32  ? 208 LYS E NZ  1 
ATOM   9126  N N   . TYR E  1 204 ? -35.413 6.124   70.276  1.00 18.56  ? 209 TYR E N   1 
ATOM   9127  C CA  . TYR E  1 204 ? -34.303 6.059   71.223  1.00 18.23  ? 209 TYR E CA  1 
ATOM   9128  C C   . TYR E  1 204 ? -34.797 5.755   72.629  1.00 19.12  ? 209 TYR E C   1 
ATOM   9129  O O   . TYR E  1 204 ? -35.749 6.370   73.109  1.00 19.65  ? 209 TYR E O   1 
ATOM   9130  C CB  . TYR E  1 204 ? -33.537 7.382   71.211  1.00 17.09  ? 209 TYR E CB  1 
ATOM   9131  C CG  . TYR E  1 204 ? -32.252 7.413   72.018  1.00 15.34  ? 209 TYR E CG  1 
ATOM   9132  C CD1 . TYR E  1 204 ? -31.018 7.203   71.404  1.00 13.11  ? 209 TYR E CD1 1 
ATOM   9133  C CD2 . TYR E  1 204 ? -32.265 7.692   73.388  1.00 13.23  ? 209 TYR E CD2 1 
ATOM   9134  C CE1 . TYR E  1 204 ? -29.829 7.252   72.133  1.00 12.51  ? 209 TYR E CE1 1 
ATOM   9135  C CE2 . TYR E  1 204 ? -31.082 7.744   74.125  1.00 11.53  ? 209 TYR E CE2 1 
ATOM   9136  C CZ  . TYR E  1 204 ? -29.868 7.522   73.491  1.00 12.43  ? 209 TYR E CZ  1 
ATOM   9137  O OH  . TYR E  1 204 ? -28.692 7.572   74.209  1.00 11.08  ? 209 TYR E OH  1 
ATOM   9138  N N   . GLN E  1 205 ? -34.144 4.799   73.281  1.00 19.90  ? 210 GLN E N   1 
ATOM   9139  C CA  . GLN E  1 205 ? -34.419 4.483   74.675  1.00 21.31  ? 210 GLN E CA  1 
ATOM   9140  C C   . GLN E  1 205 ? -33.118 4.031   75.333  1.00 21.24  ? 210 GLN E C   1 
ATOM   9141  O O   . GLN E  1 205 ? -32.481 3.074   74.883  1.00 22.11  ? 210 GLN E O   1 
ATOM   9142  C CB  . GLN E  1 205 ? -35.509 3.412   74.786  1.00 21.86  ? 210 GLN E CB  1 
ATOM   9143  C CG  . GLN E  1 205 ? -36.367 3.510   76.050  1.00 26.34  ? 210 GLN E CG  1 
ATOM   9144  C CD  . GLN E  1 205 ? -37.645 2.659   75.993  1.00 31.76  ? 210 GLN E CD  1 
ATOM   9145  O OE1 . GLN E  1 205 ? -38.330 2.485   77.003  1.00 33.11  ? 210 GLN E OE1 1 
ATOM   9146  N NE2 . GLN E  1 205 ? -37.969 2.135   74.813  1.00 32.23  ? 210 GLN E NE2 1 
ATOM   9147  N N   . GLN E  1 206 ? -32.720 4.744   76.383  1.00 20.42  ? 211 GLN E N   1 
ATOM   9148  C CA  . GLN E  1 206 ? -31.462 4.492   77.082  1.00 19.44  ? 211 GLN E CA  1 
ATOM   9149  C C   . GLN E  1 206 ? -31.492 5.190   78.442  1.00 17.80  ? 211 GLN E C   1 
ATOM   9150  O O   . GLN E  1 206 ? -31.912 6.345   78.549  1.00 17.28  ? 211 GLN E O   1 
ATOM   9151  C CB  . GLN E  1 206 ? -30.274 4.962   76.222  1.00 20.25  ? 211 GLN E CB  1 
ATOM   9152  C CG  . GLN E  1 206 ? -28.940 5.176   76.945  1.00 23.56  ? 211 GLN E CG  1 
ATOM   9153  C CD  . GLN E  1 206 ? -28.230 3.889   77.328  1.00 29.45  ? 211 GLN E CD  1 
ATOM   9154  O OE1 . GLN E  1 206 ? -28.321 2.879   76.630  1.00 30.80  ? 211 GLN E OE1 1 
ATOM   9155  N NE2 . GLN E  1 206 ? -27.503 3.928   78.442  1.00 31.55  ? 211 GLN E NE2 1 
ATOM   9156  N N   . SER E  1 207 ? -31.069 4.472   79.479  1.00 16.36  ? 212 SER E N   1 
ATOM   9157  C CA  . SER E  1 207 ? -31.031 5.021   80.830  1.00 15.43  ? 212 SER E CA  1 
ATOM   9158  C C   . SER E  1 207 ? -29.604 5.136   81.359  1.00 14.55  ? 212 SER E C   1 
ATOM   9159  O O   . SER E  1 207 ? -28.759 4.283   81.087  1.00 14.88  ? 212 SER E O   1 
ATOM   9160  C CB  . SER E  1 207 ? -31.903 4.196   81.781  1.00 15.65  ? 212 SER E CB  1 
ATOM   9161  O OG  . SER E  1 207 ? -31.635 2.813   81.657  1.00 18.00  ? 212 SER E OG  1 
ATOM   9162  N N   . PHE E  1 208 ? -29.350 6.198   82.117  1.00 13.45  ? 213 PHE E N   1 
ATOM   9163  C CA  . PHE E  1 208 ? -28.011 6.508   82.604  1.00 12.43  ? 213 PHE E CA  1 
ATOM   9164  C C   . PHE E  1 208 ? -27.976 6.613   84.118  1.00 12.04  ? 213 PHE E C   1 
ATOM   9165  O O   . PHE E  1 208 ? -28.833 7.261   84.722  1.00 11.72  ? 213 PHE E O   1 
ATOM   9166  C CB  . PHE E  1 208 ? -27.525 7.837   82.021  1.00 12.02  ? 213 PHE E CB  1 
ATOM   9167  C CG  . PHE E  1 208 ? -27.605 7.916   80.529  1.00 10.80  ? 213 PHE E CG  1 
ATOM   9168  C CD1 . PHE E  1 208 ? -26.498 7.605   79.747  1.00 9.95   ? 213 PHE E CD1 1 
ATOM   9169  C CD2 . PHE E  1 208 ? -28.782 8.315   79.904  1.00 9.24   ? 213 PHE E CD2 1 
ATOM   9170  C CE1 . PHE E  1 208 ? -26.559 7.683   78.370  1.00 8.20   ? 213 PHE E CE1 1 
ATOM   9171  C CE2 . PHE E  1 208 ? -28.858 8.391   78.526  1.00 10.42  ? 213 PHE E CE2 1 
ATOM   9172  C CZ  . PHE E  1 208 ? -27.743 8.082   77.755  1.00 12.28  ? 213 PHE E CZ  1 
ATOM   9173  N N   . THR E  1 209 ? -26.978 5.975   84.720  1.00 12.17  ? 214 THR E N   1 
ATOM   9174  C CA  . THR E  1 209 ? -26.692 6.146   86.143  1.00 12.64  ? 214 THR E CA  1 
ATOM   9175  C C   . THR E  1 209 ? -25.296 6.741   86.280  1.00 13.54  ? 214 THR E C   1 
ATOM   9176  O O   . THR E  1 209 ? -24.369 6.301   85.593  1.00 13.24  ? 214 THR E O   1 
ATOM   9177  C CB  . THR E  1 209 ? -26.796 4.819   86.958  1.00 12.41  ? 214 THR E CB  1 
ATOM   9178  O OG1 . THR E  1 209 ? -25.769 3.907   86.553  1.00 11.02  ? 214 THR E OG1 1 
ATOM   9179  C CG2 . THR E  1 209 ? -28.165 4.160   86.782  1.00 10.41  ? 214 THR E CG2 1 
ATOM   9180  N N   . PRO E  1 210 ? -25.144 7.762   87.147  1.00 14.64  ? 215 PRO E N   1 
ATOM   9181  C CA  . PRO E  1 210 ? -23.827 8.355   87.364  1.00 15.15  ? 215 PRO E CA  1 
ATOM   9182  C C   . PRO E  1 210 ? -22.881 7.385   88.055  1.00 16.15  ? 215 PRO E C   1 
ATOM   9183  O O   . PRO E  1 210 ? -23.322 6.503   88.796  1.00 16.22  ? 215 PRO E O   1 
ATOM   9184  C CB  . PRO E  1 210 ? -24.120 9.556   88.268  1.00 14.70  ? 215 PRO E CB  1 
ATOM   9185  C CG  . PRO E  1 210 ? -25.417 9.255   88.900  1.00 14.73  ? 215 PRO E CG  1 
ATOM   9186  C CD  . PRO E  1 210 ? -26.195 8.477   87.893  1.00 14.30  ? 215 PRO E CD  1 
ATOM   9187  N N   . ASN E  1 211 ? -21.591 7.566   87.798  1.00 17.64  ? 216 ASN E N   1 
ATOM   9188  C CA  . ASN E  1 211 ? -20.539 6.698   88.303  1.00 18.95  ? 216 ASN E CA  1 
ATOM   9189  C C   . ASN E  1 211 ? -19.556 7.537   89.124  1.00 19.02  ? 216 ASN E C   1 
ATOM   9190  O O   . ASN E  1 211 ? -18.510 7.947   88.612  1.00 19.44  ? 216 ASN E O   1 
ATOM   9191  C CB  . ASN E  1 211 ? -19.842 6.009   87.118  1.00 20.13  ? 216 ASN E CB  1 
ATOM   9192  C CG  . ASN E  1 211 ? -18.784 4.997   87.545  1.00 23.60  ? 216 ASN E CG  1 
ATOM   9193  O OD1 . ASN E  1 211 ? -18.924 4.307   88.558  1.00 27.77  ? 216 ASN E OD1 1 
ATOM   9194  N ND2 . ASN E  1 211 ? -17.720 4.897   86.753  1.00 28.58  ? 216 ASN E ND2 1 
ATOM   9195  N N   . PRO E  1 212 ? -19.898 7.806   90.402  1.00 19.38  ? 217 PRO E N   1 
ATOM   9196  C CA  . PRO E  1 212 ? -19.106 8.691   91.264  1.00 19.47  ? 217 PRO E CA  1 
ATOM   9197  C C   . PRO E  1 212 ? -17.687 8.189   91.481  1.00 20.03  ? 217 PRO E C   1 
ATOM   9198  O O   . PRO E  1 212 ? -17.459 6.980   91.550  1.00 20.28  ? 217 PRO E O   1 
ATOM   9199  C CB  . PRO E  1 212 ? -19.874 8.677   92.590  1.00 19.20  ? 217 PRO E CB  1 
ATOM   9200  C CG  . PRO E  1 212 ? -21.244 8.228   92.240  1.00 19.46  ? 217 PRO E CG  1 
ATOM   9201  C CD  . PRO E  1 212 ? -21.065 7.262   91.118  1.00 19.78  ? 217 PRO E CD  1 
ATOM   9202  N N   . GLY E  1 213 ? -16.753 9.127   91.598  1.00 20.74  ? 218 GLY E N   1 
ATOM   9203  C CA  . GLY E  1 213 ? -15.333 8.816   91.702  1.00 21.54  ? 218 GLY E CA  1 
ATOM   9204  C C   . GLY E  1 213 ? -14.555 9.404   90.541  1.00 22.14  ? 218 GLY E C   1 
ATOM   9205  O O   . GLY E  1 213 ? -13.360 9.689   90.660  1.00 22.61  ? 218 GLY E O   1 
ATOM   9206  N N   . ALA E  1 214 ? -15.254 9.607   89.426  1.00 22.28  ? 219 ALA E N   1 
ATOM   9207  C CA  . ALA E  1 214 ? -14.637 9.977   88.151  1.00 22.43  ? 219 ALA E CA  1 
ATOM   9208  C C   . ALA E  1 214 ? -14.379 11.477  87.961  1.00 21.78  ? 219 ALA E C   1 
ATOM   9209  O O   . ALA E  1 214 ? -13.342 11.856  87.423  1.00 22.49  ? 219 ALA E O   1 
ATOM   9210  C CB  . ALA E  1 214 ? -15.470 9.423   86.989  1.00 22.64  ? 219 ALA E CB  1 
ATOM   9211  N N   . ARG E  1 215 ? -15.321 12.309  88.404  1.00 20.91  ? 220 ARG E N   1 
ATOM   9212  C CA  . ARG E  1 215 ? -15.303 13.769  88.196  1.00 20.72  ? 220 ARG E CA  1 
ATOM   9213  C C   . ARG E  1 215 ? -15.273 14.176  86.718  1.00 19.67  ? 220 ARG E C   1 
ATOM   9214  O O   . ARG E  1 215 ? -14.227 14.569  86.187  1.00 19.09  ? 220 ARG E O   1 
ATOM   9215  C CB  . ARG E  1 215 ? -14.176 14.456  88.978  1.00 21.33  ? 220 ARG E CB  1 
ATOM   9216  C CG  . ARG E  1 215 ? -14.411 15.952  89.186  1.00 25.28  ? 220 ARG E CG  1 
ATOM   9217  C CD  . ARG E  1 215 ? -13.137 16.685  89.577  1.00 31.24  ? 220 ARG E CD  1 
ATOM   9218  N NE  . ARG E  1 215 ? -13.440 17.947  90.252  1.00 34.77  ? 220 ARG E NE  1 
ATOM   9219  C CZ  . ARG E  1 215 ? -13.459 18.115  91.575  1.00 35.89  ? 220 ARG E CZ  1 
ATOM   9220  N NH1 . ARG E  1 215 ? -13.179 17.106  92.391  1.00 33.57  ? 220 ARG E NH1 1 
ATOM   9221  N NH2 . ARG E  1 215 ? -13.752 19.303  92.085  1.00 36.94  ? 220 ARG E NH2 1 
ATOM   9222  N N   . ARG E  1 216 ? -16.434 14.088  86.072  1.00 18.35  ? 229 ARG E N   1 
ATOM   9223  C CA  . ARG E  1 216 ? -16.564 14.387  84.648  1.00 17.63  ? 229 ARG E CA  1 
ATOM   9224  C C   . ARG E  1 216 ? -18.014 14.607  84.218  1.00 16.61  ? 229 ARG E C   1 
ATOM   9225  O O   . ARG E  1 216 ? -18.946 14.132  84.869  1.00 17.09  ? 229 ARG E O   1 
ATOM   9226  C CB  . ARG E  1 216 ? -15.922 13.279  83.802  1.00 18.01  ? 229 ARG E CB  1 
ATOM   9227  C CG  . ARG E  1 216 ? -16.491 11.884  84.039  1.00 21.87  ? 229 ARG E CG  1 
ATOM   9228  C CD  . ARG E  1 216 ? -15.535 10.792  83.575  1.00 28.63  ? 229 ARG E CD  1 
ATOM   9229  N NE  . ARG E  1 216 ? -15.523 10.634  82.120  1.00 34.71  ? 229 ARG E NE  1 
ATOM   9230  C CZ  . ARG E  1 216 ? -14.578 11.111  81.310  1.00 37.68  ? 229 ARG E CZ  1 
ATOM   9231  N NH1 . ARG E  1 216 ? -13.542 11.787  81.796  1.00 39.91  ? 229 ARG E NH1 1 
ATOM   9232  N NH2 . ARG E  1 216 ? -14.671 10.913  80.003  1.00 38.94  ? 229 ARG E NH2 1 
ATOM   9233  N N   . ILE E  1 217 ? -18.190 15.338  83.120  1.00 14.90  ? 230 ILE E N   1 
ATOM   9234  C CA  . ILE E  1 217 ? -19.493 15.496  82.492  1.00 13.49  ? 230 ILE E CA  1 
ATOM   9235  C C   . ILE E  1 217 ? -19.441 14.908  81.083  1.00 13.04  ? 230 ILE E C   1 
ATOM   9236  O O   . ILE E  1 217 ? -18.803 15.469  80.188  1.00 13.62  ? 230 ILE E O   1 
ATOM   9237  C CB  . ILE E  1 217 ? -19.947 16.972  82.467  1.00 13.31  ? 230 ILE E CB  1 
ATOM   9238  C CG1 . ILE E  1 217 ? -20.216 17.463  83.893  1.00 13.11  ? 230 ILE E CG1 1 
ATOM   9239  C CG2 . ILE E  1 217 ? -21.194 17.133  81.601  1.00 13.31  ? 230 ILE E CG2 1 
ATOM   9240  C CD1 . ILE E  1 217 ? -20.377 18.970  84.028  1.00 12.95  ? 230 ILE E CD1 1 
ATOM   9241  N N   . ASP E  1 218 ? -20.098 13.764  80.905  1.00 12.25  ? 231 ASP E N   1 
ATOM   9242  C CA  . ASP E  1 218 ? -20.129 13.066  79.622  1.00 11.12  ? 231 ASP E CA  1 
ATOM   9243  C C   . ASP E  1 218 ? -21.399 13.399  78.856  1.00 10.24  ? 231 ASP E C   1 
ATOM   9244  O O   . ASP E  1 218 ? -22.495 13.367  79.417  1.00 10.54  ? 231 ASP E O   1 
ATOM   9245  C CB  . ASP E  1 218 ? -20.033 11.553  79.828  1.00 11.27  ? 231 ASP E CB  1 
ATOM   9246  C CG  . ASP E  1 218 ? -18.630 11.095  80.189  1.00 13.07  ? 231 ASP E CG  1 
ATOM   9247  O OD1 . ASP E  1 218 ? -17.655 11.783  79.815  1.00 17.35  ? 231 ASP E OD1 1 
ATOM   9248  O OD2 . ASP E  1 218 ? -18.504 10.034  80.840  1.00 12.98  ? 231 ASP E OD2 1 
ATOM   9249  N N   . PHE E  1 219 ? -21.249 13.711  77.573  1.00 8.63   ? 232 PHE E N   1 
ATOM   9250  C CA  . PHE E  1 219 ? -22.390 14.101  76.752  1.00 7.86   ? 232 PHE E CA  1 
ATOM   9251  C C   . PHE E  1 219 ? -22.874 12.973  75.849  1.00 7.36   ? 232 PHE E C   1 
ATOM   9252  O O   . PHE E  1 219 ? -22.080 12.176  75.349  1.00 7.34   ? 232 PHE E O   1 
ATOM   9253  C CB  . PHE E  1 219 ? -22.073 15.364  75.944  1.00 7.82   ? 232 PHE E CB  1 
ATOM   9254  C CG  . PHE E  1 219 ? -21.866 16.584  76.797  1.00 7.98   ? 232 PHE E CG  1 
ATOM   9255  C CD1 . PHE E  1 219 ? -20.586 16.992  77.154  1.00 6.27   ? 232 PHE E CD1 1 
ATOM   9256  C CD2 . PHE E  1 219 ? -22.956 17.314  77.264  1.00 10.38  ? 232 PHE E CD2 1 
ATOM   9257  C CE1 . PHE E  1 219 ? -20.392 18.112  77.955  1.00 8.38   ? 232 PHE E CE1 1 
ATOM   9258  C CE2 . PHE E  1 219 ? -22.773 18.438  78.063  1.00 11.64  ? 232 PHE E CE2 1 
ATOM   9259  C CZ  . PHE E  1 219 ? -21.487 18.838  78.408  1.00 10.50  ? 232 PHE E CZ  1 
ATOM   9260  N N   . HIS E  1 220 ? -24.191 12.912  75.670  1.00 6.89   ? 233 HIS E N   1 
ATOM   9261  C CA  . HIS E  1 220 ? -24.833 11.922  74.814  1.00 6.54   ? 233 HIS E CA  1 
ATOM   9262  C C   . HIS E  1 220 ? -25.829 12.645  73.919  1.00 7.00   ? 233 HIS E C   1 
ATOM   9263  O O   . HIS E  1 220 ? -26.260 13.757  74.239  1.00 6.73   ? 233 HIS E O   1 
ATOM   9264  C CB  . HIS E  1 220 ? -25.545 10.862  75.650  1.00 5.67   ? 233 HIS E CB  1 
ATOM   9265  C CG  . HIS E  1 220 ? -24.728 10.342  76.789  1.00 5.90   ? 233 HIS E CG  1 
ATOM   9266  N ND1 . HIS E  1 220 ? -23.895 9.251   76.671  1.00 6.46   ? 233 HIS E ND1 1 
ATOM   9267  C CD2 . HIS E  1 220 ? -24.611 10.767  78.069  1.00 5.84   ? 233 HIS E CD2 1 
ATOM   9268  C CE1 . HIS E  1 220 ? -23.300 9.025   77.829  1.00 6.84   ? 233 HIS E CE1 1 
ATOM   9269  N NE2 . HIS E  1 220 ? -23.718 9.931   78.695  1.00 8.64   ? 233 HIS E NE2 1 
ATOM   9270  N N   . TRP E  1 221 ? -26.196 12.017  72.804  1.00 7.25   ? 234 TRP E N   1 
ATOM   9271  C CA  . TRP E  1 221 ? -27.002 12.692  71.789  1.00 7.31   ? 234 TRP E CA  1 
ATOM   9272  C C   . TRP E  1 221 ? -27.946 11.775  71.028  1.00 7.37   ? 234 TRP E C   1 
ATOM   9273  O O   . TRP E  1 221 ? -27.748 10.564  70.971  1.00 8.62   ? 234 TRP E O   1 
ATOM   9274  C CB  . TRP E  1 221 ? -26.103 13.448  70.800  1.00 6.35   ? 234 TRP E CB  1 
ATOM   9275  C CG  . TRP E  1 221 ? -25.115 12.581  70.079  1.00 9.67   ? 234 TRP E CG  1 
ATOM   9276  C CD1 . TRP E  1 221 ? -23.918 12.125  70.558  1.00 12.36  ? 234 TRP E CD1 1 
ATOM   9277  C CD2 . TRP E  1 221 ? -25.231 12.070  68.742  1.00 12.29  ? 234 TRP E CD2 1 
ATOM   9278  N NE1 . TRP E  1 221 ? -23.285 11.359  69.606  1.00 12.61  ? 234 TRP E NE1 1 
ATOM   9279  C CE2 . TRP E  1 221 ? -24.067 11.311  68.482  1.00 11.96  ? 234 TRP E CE2 1 
ATOM   9280  C CE3 . TRP E  1 221 ? -26.209 12.175  67.740  1.00 12.29  ? 234 TRP E CE3 1 
ATOM   9281  C CZ2 . TRP E  1 221 ? -23.850 10.661  67.262  1.00 13.40  ? 234 TRP E CZ2 1 
ATOM   9282  C CZ3 . TRP E  1 221 ? -25.992 11.531  66.525  1.00 11.38  ? 234 TRP E CZ3 1 
ATOM   9283  C CH2 . TRP E  1 221 ? -24.820 10.783  66.299  1.00 12.47  ? 234 TRP E CH2 1 
ATOM   9284  N N   . LEU E  1 222 ? -28.979 12.377  70.448  1.00 7.15   ? 235 LEU E N   1 
ATOM   9285  C CA  . LEU E  1 222 ? -29.876 11.694  69.528  1.00 6.86   ? 235 LEU E CA  1 
ATOM   9286  C C   . LEU E  1 222 ? -30.424 12.698  68.515  1.00 7.69   ? 235 LEU E C   1 
ATOM   9287  O O   . LEU E  1 222 ? -30.468 13.907  68.784  1.00 8.10   ? 235 LEU E O   1 
ATOM   9288  C CB  . LEU E  1 222 ? -31.019 10.999  70.285  1.00 6.23   ? 235 LEU E CB  1 
ATOM   9289  C CG  . LEU E  1 222 ? -32.061 11.836  71.038  1.00 3.87   ? 235 LEU E CG  1 
ATOM   9290  C CD1 . LEU E  1 222 ? -33.131 12.377  70.101  1.00 2.18   ? 235 LEU E CD1 1 
ATOM   9291  C CD2 . LEU E  1 222 ? -32.701 11.020  72.146  1.00 2.00   ? 235 LEU E CD2 1 
ATOM   9292  N N   . LEU E  1 223 ? -30.831 12.192  67.352  1.00 7.28   ? 236 LEU E N   1 
ATOM   9293  C CA  . LEU E  1 223 ? -31.552 12.992  66.371  1.00 6.96   ? 236 LEU E CA  1 
ATOM   9294  C C   . LEU E  1 223 ? -33.050 12.774  66.556  1.00 7.43   ? 236 LEU E C   1 
ATOM   9295  O O   . LEU E  1 223 ? -33.519 11.636  66.552  1.00 8.01   ? 236 LEU E O   1 
ATOM   9296  C CB  . LEU E  1 223 ? -31.122 12.619  64.956  1.00 6.53   ? 236 LEU E CB  1 
ATOM   9297  C CG  . LEU E  1 223 ? -29.688 12.997  64.576  1.00 7.22   ? 236 LEU E CG  1 
ATOM   9298  C CD1 . LEU E  1 223 ? -29.190 12.129  63.438  1.00 2.93   ? 236 LEU E CD1 1 
ATOM   9299  C CD2 . LEU E  1 223 ? -29.572 14.488  64.228  1.00 7.98   ? 236 LEU E CD2 1 
ATOM   9300  N N   . LEU E  1 224 ? -33.787 13.864  66.747  1.00 7.56   ? 237 LEU E N   1 
ATOM   9301  C CA  . LEU E  1 224 ? -35.226 13.799  66.974  1.00 8.56   ? 237 LEU E CA  1 
ATOM   9302  C C   . LEU E  1 224 ? -35.988 14.164  65.701  1.00 9.80   ? 237 LEU E C   1 
ATOM   9303  O O   . LEU E  1 224 ? -35.870 15.282  65.194  1.00 10.15  ? 237 LEU E O   1 
ATOM   9304  C CB  . LEU E  1 224 ? -35.620 14.722  68.131  1.00 8.76   ? 237 LEU E CB  1 
ATOM   9305  C CG  . LEU E  1 224 ? -37.066 14.729  68.637  1.00 9.48   ? 237 LEU E CG  1 
ATOM   9306  C CD1 . LEU E  1 224 ? -37.439 13.406  69.299  1.00 10.53  ? 237 LEU E CD1 1 
ATOM   9307  C CD2 . LEU E  1 224 ? -37.270 15.880  69.606  1.00 5.83   ? 237 LEU E CD2 1 
ATOM   9308  N N   . ASP E  1 225 ? -36.758 13.207  65.186  1.00 10.94  ? 238 ASP E N   1 
ATOM   9309  C CA  . ASP E  1 225 ? -37.546 13.401  63.970  1.00 11.83  ? 238 ASP E CA  1 
ATOM   9310  C C   . ASP E  1 225 ? -38.590 14.496  64.159  1.00 12.64  ? 238 ASP E C   1 
ATOM   9311  O O   . ASP E  1 225 ? -38.998 14.768  65.292  1.00 12.50  ? 238 ASP E O   1 
ATOM   9312  C CB  . ASP E  1 225 ? -38.245 12.098  63.569  1.00 11.71  ? 238 ASP E CB  1 
ATOM   9313  C CG  . ASP E  1 225 ? -37.301 11.085  62.952  1.00 13.15  ? 238 ASP E CG  1 
ATOM   9314  O OD1 . ASP E  1 225 ? -36.386 11.481  62.194  1.00 18.36  ? 238 ASP E OD1 1 
ATOM   9315  O OD2 . ASP E  1 225 ? -37.487 9.880   63.215  1.00 12.89  ? 238 ASP E OD2 1 
ATOM   9316  N N   . PRO E  1 226 ? -39.019 15.139  63.053  1.00 13.55  ? 239 PRO E N   1 
ATOM   9317  C CA  . PRO E  1 226 ? -40.127 16.092  63.099  1.00 14.04  ? 239 PRO E CA  1 
ATOM   9318  C C   . PRO E  1 226 ? -41.349 15.532  63.823  1.00 14.82  ? 239 PRO E C   1 
ATOM   9319  O O   . PRO E  1 226 ? -41.682 14.352  63.663  1.00 15.30  ? 239 PRO E O   1 
ATOM   9320  C CB  . PRO E  1 226 ? -40.444 16.312  61.623  1.00 14.32  ? 239 PRO E CB  1 
ATOM   9321  C CG  . PRO E  1 226 ? -39.120 16.177  60.954  1.00 14.18  ? 239 PRO E CG  1 
ATOM   9322  C CD  . PRO E  1 226 ? -38.368 15.126  61.727  1.00 13.53  ? 239 PRO E CD  1 
ATOM   9323  N N   . ASN E  1 227 ? -41.987 16.382  64.628  1.00 15.23  ? 240 ASN E N   1 
ATOM   9324  C CA  . ASN E  1 227 ? -43.185 16.040  65.415  1.00 15.32  ? 240 ASN E CA  1 
ATOM   9325  C C   . ASN E  1 227 ? -42.974 14.967  66.499  1.00 14.88  ? 240 ASN E C   1 
ATOM   9326  O O   . ASN E  1 227 ? -43.882 14.685  67.288  1.00 15.15  ? 240 ASN E O   1 
ATOM   9327  C CB  . ASN E  1 227 ? -44.378 15.699  64.502  1.00 15.49  ? 240 ASN E CB  1 
ATOM   9328  C CG  . ASN E  1 227 ? -45.728 15.924  65.183  1.00 19.73  ? 240 ASN E CG  1 
ATOM   9329  O OD1 . ASN E  1 227 ? -45.935 16.927  65.873  1.00 23.52  ? 240 ASN E OD1 1 
ATOM   9330  N ND2 . ASN E  1 227 ? -46.654 14.989  64.984  1.00 21.40  ? 240 ASN E ND2 1 
ATOM   9331  N N   . ASP E  1 228 ? -41.776 14.384  66.543  1.00 14.28  ? 241 ASP E N   1 
ATOM   9332  C CA  . ASP E  1 228 ? -41.427 13.399  67.568  1.00 13.48  ? 241 ASP E CA  1 
ATOM   9333  C C   . ASP E  1 228 ? -41.042 14.106  68.876  1.00 12.65  ? 241 ASP E C   1 
ATOM   9334  O O   . ASP E  1 228 ? -40.682 15.285  68.873  1.00 12.30  ? 241 ASP E O   1 
ATOM   9335  C CB  . ASP E  1 228 ? -40.300 12.480  67.070  1.00 13.66  ? 241 ASP E CB  1 
ATOM   9336  C CG  . ASP E  1 228 ? -40.168 11.197  67.889  1.00 14.04  ? 241 ASP E CG  1 
ATOM   9337  O OD1 . ASP E  1 228 ? -41.093 10.864  68.659  1.00 14.98  ? 241 ASP E OD1 1 
ATOM   9338  O OD2 . ASP E  1 228 ? -39.131 10.513  67.757  1.00 16.62  ? 241 ASP E OD2 1 
ATOM   9339  N N   . THR E  1 229 ? -41.133 13.387  69.991  1.00 11.68  ? 242 THR E N   1 
ATOM   9340  C CA  . THR E  1 229 ? -40.891 13.981  71.303  1.00 10.56  ? 242 THR E CA  1 
ATOM   9341  C C   . THR E  1 229 ? -39.776 13.267  72.072  1.00 9.65   ? 242 THR E C   1 
ATOM   9342  O O   . THR E  1 229 ? -39.771 12.036  72.175  1.00 10.05  ? 242 THR E O   1 
ATOM   9343  C CB  . THR E  1 229 ? -42.193 14.007  72.148  1.00 10.57  ? 242 THR E CB  1 
ATOM   9344  O OG1 . THR E  1 229 ? -43.188 14.783  71.469  1.00 10.28  ? 242 THR E OG1 1 
ATOM   9345  C CG2 . THR E  1 229 ? -41.951 14.610  73.535  1.00 9.77   ? 242 THR E CG2 1 
ATOM   9346  N N   . VAL E  1 230 ? -38.833 14.046  72.600  1.00 7.66   ? 243 VAL E N   1 
ATOM   9347  C CA  . VAL E  1 230 ? -37.846 13.520  73.538  1.00 5.89   ? 243 VAL E CA  1 
ATOM   9348  C C   . VAL E  1 230 ? -38.259 13.818  74.988  1.00 6.50   ? 243 VAL E C   1 
ATOM   9349  O O   . VAL E  1 230 ? -38.541 14.966  75.349  1.00 6.75   ? 243 VAL E O   1 
ATOM   9350  C CB  . VAL E  1 230 ? -36.405 14.005  73.226  1.00 4.82   ? 243 VAL E CB  1 
ATOM   9351  C CG1 . VAL E  1 230 ? -36.295 15.529  73.294  1.00 3.55   ? 243 VAL E CG1 1 
ATOM   9352  C CG2 . VAL E  1 230 ? -35.403 13.335  74.154  1.00 3.01   ? 243 VAL E CG2 1 
ATOM   9353  N N   . THR E  1 231 ? -38.310 12.771  75.804  1.00 6.26   ? 244 THR E N   1 
ATOM   9354  C CA  . THR E  1 231 ? -38.707 12.904  77.200  1.00 6.31   ? 244 THR E CA  1 
ATOM   9355  C C   . THR E  1 231 ? -37.530 12.593  78.119  1.00 5.77   ? 244 THR E C   1 
ATOM   9356  O O   . THR E  1 231 ? -36.931 11.519  78.035  1.00 5.71   ? 244 THR E O   1 
ATOM   9357  C CB  . THR E  1 231 ? -39.914 11.990  77.531  1.00 6.59   ? 244 THR E CB  1 
ATOM   9358  O OG1 . THR E  1 231 ? -41.000 12.291  76.645  1.00 7.27   ? 244 THR E OG1 1 
ATOM   9359  C CG2 . THR E  1 231 ? -40.379 12.191  78.967  1.00 6.52   ? 244 THR E CG2 1 
ATOM   9360  N N   . PHE E  1 232 ? -37.202 13.553  78.981  1.00 5.59   ? 245 PHE E N   1 
ATOM   9361  C CA  . PHE E  1 232 ? -36.151 13.388  79.978  1.00 5.54   ? 245 PHE E CA  1 
ATOM   9362  C C   . PHE E  1 232 ? -36.747 13.113  81.345  1.00 5.99   ? 245 PHE E C   1 
ATOM   9363  O O   . PHE E  1 232 ? -37.618 13.844  81.812  1.00 6.87   ? 245 PHE E O   1 
ATOM   9364  C CB  . PHE E  1 232 ? -35.271 14.638  80.050  1.00 5.23   ? 245 PHE E CB  1 
ATOM   9365  C CG  . PHE E  1 232 ? -34.497 14.900  78.802  1.00 5.04   ? 245 PHE E CG  1 
ATOM   9366  C CD1 . PHE E  1 232 ? -34.922 15.868  77.899  1.00 3.76   ? 245 PHE E CD1 1 
ATOM   9367  C CD2 . PHE E  1 232 ? -33.349 14.167  78.514  1.00 2.86   ? 245 PHE E CD2 1 
ATOM   9368  C CE1 . PHE E  1 232 ? -34.209 16.106  76.730  1.00 4.75   ? 245 PHE E CE1 1 
ATOM   9369  C CE2 . PHE E  1 232 ? -32.625 14.401  77.351  1.00 2.03   ? 245 PHE E CE2 1 
ATOM   9370  C CZ  . PHE E  1 232 ? -33.054 15.369  76.458  1.00 2.31   ? 245 PHE E CZ  1 
ATOM   9371  N N   . THR E  1 233 ? -36.273 12.050  81.979  1.00 6.63   ? 246 THR E N   1 
ATOM   9372  C CA  . THR E  1 233 ? -36.676 11.717  83.338  1.00 7.42   ? 246 THR E CA  1 
ATOM   9373  C C   . THR E  1 233 ? -35.425 11.626  84.187  1.00 7.13   ? 246 THR E C   1 
ATOM   9374  O O   . THR E  1 233 ? -34.510 10.878  83.861  1.00 8.54   ? 246 THR E O   1 
ATOM   9375  C CB  . THR E  1 233 ? -37.479 10.405  83.371  1.00 7.02   ? 246 THR E CB  1 
ATOM   9376  O OG1 . THR E  1 233 ? -38.803 10.661  82.889  1.00 8.91   ? 246 THR E OG1 1 
ATOM   9377  C CG2 . THR E  1 233 ? -37.568 9.840   84.777  1.00 8.84   ? 246 THR E CG2 1 
ATOM   9378  N N   . PHE E  1 234 ? -35.382 12.399  85.266  1.00 6.57   ? 247 PHE E N   1 
ATOM   9379  C CA  . PHE E  1 234 ? -34.185 12.495  86.093  1.00 6.18   ? 247 PHE E CA  1 
ATOM   9380  C C   . PHE E  1 234 ? -34.503 12.920  87.521  1.00 5.72   ? 247 PHE E C   1 
ATOM   9381  O O   . PHE E  1 234 ? -35.561 13.502  87.788  1.00 5.71   ? 247 PHE E O   1 
ATOM   9382  C CB  . PHE E  1 234 ? -33.181 13.472  85.465  1.00 6.47   ? 247 PHE E CB  1 
ATOM   9383  C CG  . PHE E  1 234 ? -33.774 14.810  85.104  1.00 8.55   ? 247 PHE E CG  1 
ATOM   9384  C CD1 . PHE E  1 234 ? -33.758 15.863  86.015  1.00 8.62   ? 247 PHE E CD1 1 
ATOM   9385  C CD2 . PHE E  1 234 ? -34.349 15.018  83.851  1.00 9.26   ? 247 PHE E CD2 1 
ATOM   9386  C CE1 . PHE E  1 234 ? -34.308 17.099  85.687  1.00 8.86   ? 247 PHE E CE1 1 
ATOM   9387  C CE2 . PHE E  1 234 ? -34.902 16.254  83.515  1.00 8.21   ? 247 PHE E CE2 1 
ATOM   9388  C CZ  . PHE E  1 234 ? -34.881 17.294  84.435  1.00 7.11   ? 247 PHE E CZ  1 
ATOM   9389  N N   . ASN E  1 235 ? -33.577 12.621  88.429  1.00 4.97   ? 248 ASN E N   1 
ATOM   9390  C CA  . ASN E  1 235 ? -33.656 13.082  89.810  1.00 4.86   ? 248 ASN E CA  1 
ATOM   9391  C C   . ASN E  1 235 ? -32.302 13.573  90.336  1.00 4.69   ? 248 ASN E C   1 
ATOM   9392  O O   . ASN E  1 235 ? -32.037 13.531  91.542  1.00 4.50   ? 248 ASN E O   1 
ATOM   9393  C CB  . ASN E  1 235 ? -34.249 11.992  90.713  1.00 5.01   ? 248 ASN E CB  1 
ATOM   9394  C CG  . ASN E  1 235 ? -33.327 10.796  90.884  1.00 6.32   ? 248 ASN E CG  1 
ATOM   9395  O OD1 . ASN E  1 235 ? -32.555 10.445  89.988  1.00 11.49  ? 248 ASN E OD1 1 
ATOM   9396  N ND2 . ASN E  1 235 ? -33.405 10.162  92.047  1.00 3.40   ? 248 ASN E ND2 1 
ATOM   9397  N N   . GLY E  1 236 ? -31.460 14.047  89.417  1.00 4.65   ? 249 GLY E N   1 
ATOM   9398  C CA  . GLY E  1 236 ? -30.118 14.539  89.743  1.00 4.51   ? 249 GLY E CA  1 
ATOM   9399  C C   . GLY E  1 236 ? -29.067 14.152  88.713  1.00 4.33   ? 249 GLY E C   1 
ATOM   9400  O O   . GLY E  1 236 ? -29.361 13.419  87.763  1.00 4.87   ? 249 GLY E O   1 
ATOM   9401  N N   . ALA E  1 237 ? -27.844 14.652  88.909  1.00 3.42   ? 250 ALA E N   1 
ATOM   9402  C CA  . ALA E  1 237 ? -26.684 14.380  88.038  1.00 3.11   ? 250 ALA E CA  1 
ATOM   9403  C C   . ALA E  1 237 ? -26.924 14.684  86.559  1.00 3.20   ? 250 ALA E C   1 
ATOM   9404  O O   . ALA E  1 237 ? -26.189 14.206  85.692  1.00 3.02   ? 250 ALA E O   1 
ATOM   9405  C CB  . ALA E  1 237 ? -26.178 12.940  88.226  1.00 2.78   ? 250 ALA E CB  1 
ATOM   9406  N N   . PHE E  1 238 ? -27.939 15.499  86.285  1.00 3.62   ? 251 PHE E N   1 
ATOM   9407  C CA  . PHE E  1 238 ? -28.387 15.754  84.924  1.00 4.22   ? 251 PHE E CA  1 
ATOM   9408  C C   . PHE E  1 238 ? -27.980 17.133  84.423  1.00 4.71   ? 251 PHE E C   1 
ATOM   9409  O O   . PHE E  1 238 ? -28.377 18.150  84.989  1.00 5.52   ? 251 PHE E O   1 
ATOM   9410  C CB  . PHE E  1 238 ? -29.907 15.587  84.835  1.00 4.55   ? 251 PHE E CB  1 
ATOM   9411  C CG  . PHE E  1 238 ? -30.450 15.673  83.440  1.00 2.89   ? 251 PHE E CG  1 
ATOM   9412  C CD1 . PHE E  1 238 ? -30.089 14.736  82.477  1.00 2.57   ? 251 PHE E CD1 1 
ATOM   9413  C CD2 . PHE E  1 238 ? -31.331 16.683  83.089  1.00 2.39   ? 251 PHE E CD2 1 
ATOM   9414  C CE1 . PHE E  1 238 ? -30.594 14.806  81.184  1.00 2.00   ? 251 PHE E CE1 1 
ATOM   9415  C CE2 . PHE E  1 238 ? -31.844 16.760  81.798  1.00 3.67   ? 251 PHE E CE2 1 
ATOM   9416  C CZ  . PHE E  1 238 ? -31.471 15.820  80.844  1.00 2.00   ? 251 PHE E CZ  1 
ATOM   9417  N N   . ILE E  1 239 ? -27.184 17.152  83.356  1.00 4.49   ? 252 ILE E N   1 
ATOM   9418  C CA  . ILE E  1 239 ? -26.809 18.388  82.676  1.00 3.56   ? 252 ILE E CA  1 
ATOM   9419  C C   . ILE E  1 239 ? -27.777 18.567  81.517  1.00 3.84   ? 252 ILE E C   1 
ATOM   9420  O O   . ILE E  1 239 ? -27.673 17.885  80.499  1.00 4.73   ? 252 ILE E O   1 
ATOM   9421  C CB  . ILE E  1 239 ? -25.333 18.346  82.179  1.00 3.46   ? 252 ILE E CB  1 
ATOM   9422  C CG1 . ILE E  1 239 ? -24.355 18.088  83.343  1.00 2.39   ? 252 ILE E CG1 1 
ATOM   9423  C CG2 . ILE E  1 239 ? -24.968 19.601  81.384  1.00 2.15   ? 252 ILE E CG2 1 
ATOM   9424  C CD1 . ILE E  1 239 ? -24.581 18.920  84.590  1.00 2.00   ? 252 ILE E CD1 1 
ATOM   9425  N N   . ALA E  1 240 ? -28.725 19.481  81.689  1.00 4.45   ? 253 ALA E N   1 
ATOM   9426  C CA  . ALA E  1 240 ? -29.864 19.613  80.782  1.00 4.77   ? 253 ALA E CA  1 
ATOM   9427  C C   . ALA E  1 240 ? -29.589 20.548  79.607  1.00 5.19   ? 253 ALA E C   1 
ATOM   9428  O O   . ALA E  1 240 ? -28.810 21.492  79.742  1.00 5.54   ? 253 ALA E O   1 
ATOM   9429  C CB  . ALA E  1 240 ? -31.082 20.085  81.555  1.00 4.18   ? 253 ALA E CB  1 
ATOM   9430  N N   . PRO E  1 241 ? -30.222 20.285  78.446  1.00 5.60   ? 254 PRO E N   1 
ATOM   9431  C CA  . PRO E  1 241 ? -30.119 21.226  77.336  1.00 5.88   ? 254 PRO E CA  1 
ATOM   9432  C C   . PRO E  1 241 ? -31.027 22.429  77.537  1.00 7.76   ? 254 PRO E C   1 
ATOM   9433  O O   . PRO E  1 241 ? -32.146 22.294  78.050  1.00 9.44   ? 254 PRO E O   1 
ATOM   9434  C CB  . PRO E  1 241 ? -30.607 20.412  76.136  1.00 5.07   ? 254 PRO E CB  1 
ATOM   9435  C CG  . PRO E  1 241 ? -31.535 19.414  76.712  1.00 5.83   ? 254 PRO E CG  1 
ATOM   9436  C CD  . PRO E  1 241 ? -30.972 19.071  78.069  1.00 6.38   ? 254 PRO E CD  1 
ATOM   9437  N N   . ASP E  1 242 ? -30.537 23.600  77.153  1.00 8.27   ? 255 ASP E N   1 
ATOM   9438  C CA  . ASP E  1 242 ? -31.371 24.780  77.083  1.00 8.71   ? 255 ASP E CA  1 
ATOM   9439  C C   . ASP E  1 242 ? -31.775 24.971  75.628  1.00 9.72   ? 255 ASP E C   1 
ATOM   9440  O O   . ASP E  1 242 ? -32.869 25.464  75.334  1.00 10.39  ? 255 ASP E O   1 
ATOM   9441  C CB  . ASP E  1 242 ? -30.613 26.002  77.596  1.00 8.74   ? 255 ASP E CB  1 
ATOM   9442  C CG  . ASP E  1 242 ? -31.485 27.240  77.665  1.00 10.37  ? 255 ASP E CG  1 
ATOM   9443  O OD1 . ASP E  1 242 ? -32.540 27.187  78.330  1.00 11.24  ? 255 ASP E OD1 1 
ATOM   9444  O OD2 . ASP E  1 242 ? -31.113 28.264  77.053  1.00 9.99   ? 255 ASP E OD2 1 
ATOM   9445  N N   . ARG E  1 243 ? -30.882 24.559  74.727  1.00 9.97   ? 256 ARG E N   1 
ATOM   9446  C CA  . ARG E  1 243 ? -31.066 24.714  73.287  1.00 10.32  ? 256 ARG E CA  1 
ATOM   9447  C C   . ARG E  1 243 ? -30.731 23.438  72.527  1.00 11.10  ? 256 ARG E C   1 
ATOM   9448  O O   . ARG E  1 243 ? -29.957 22.600  73.001  1.00 12.21  ? 256 ARG E O   1 
ATOM   9449  C CB  . ARG E  1 243 ? -30.175 25.831  72.756  1.00 10.57  ? 256 ARG E CB  1 
ATOM   9450  C CG  . ARG E  1 243 ? -30.697 27.255  72.912  1.00 10.56  ? 256 ARG E CG  1 
ATOM   9451  C CD  . ARG E  1 243 ? -29.511 28.188  72.759  1.00 7.32   ? 256 ARG E CD  1 
ATOM   9452  N NE  . ARG E  1 243 ? -29.775 29.393  71.981  1.00 9.28   ? 256 ARG E NE  1 
ATOM   9453  C CZ  . ARG E  1 243 ? -28.859 30.026  71.251  1.00 7.28   ? 256 ARG E CZ  1 
ATOM   9454  N NH1 . ARG E  1 243 ? -27.617 29.558  71.167  1.00 3.37   ? 256 ARG E NH1 1 
ATOM   9455  N NH2 . ARG E  1 243 ? -29.189 31.125  70.584  1.00 11.19  ? 256 ARG E NH2 1 
ATOM   9456  N N   . THR E  1 244 ? -31.310 23.315  71.336  1.00 11.15  ? 257 THR E N   1 
ATOM   9457  C CA  . THR E  1 244 ? -31.024 22.215  70.417  1.00 10.49  ? 257 THR E CA  1 
ATOM   9458  C C   . THR E  1 244 ? -30.546 22.782  69.071  1.00 10.98  ? 257 THR E C   1 
ATOM   9459  O O   . THR E  1 244 ? -30.724 23.972  68.796  1.00 10.76  ? 257 THR E O   1 
ATOM   9460  C CB  . THR E  1 244 ? -32.261 21.289  70.231  1.00 10.39  ? 257 THR E CB  1 
ATOM   9461  O OG1 . THR E  1 244 ? -31.922 20.191  69.376  1.00 10.54  ? 257 THR E OG1 1 
ATOM   9462  C CG2 . THR E  1 244 ? -33.454 22.051  69.636  1.00 7.10   ? 257 THR E CG2 1 
ATOM   9463  N N   . SER E  1 245 ? -29.945 21.932  68.240  1.00 11.45  ? 258 SER E N   1 
ATOM   9464  C CA  . SER E  1 245 ? -29.370 22.379  66.971  1.00 11.98  ? 258 SER E CA  1 
ATOM   9465  C C   . SER E  1 245 ? -30.169 21.934  65.757  1.00 12.33  ? 258 SER E C   1 
ATOM   9466  O O   . SER E  1 245 ? -30.785 20.870  65.757  1.00 12.91  ? 258 SER E O   1 
ATOM   9467  C CB  . SER E  1 245 ? -27.925 21.893  66.826  1.00 12.08  ? 258 SER E CB  1 
ATOM   9468  O OG  . SER E  1 245 ? -27.107 22.390  67.868  1.00 11.33  ? 258 SER E OG  1 
ATOM   9469  N N   . PHE E  1 246 ? -30.137 22.762  64.719  1.00 12.69  ? 259 PHE E N   1 
ATOM   9470  C CA  . PHE E  1 246 ? -30.697 22.409  63.423  1.00 12.80  ? 259 PHE E CA  1 
ATOM   9471  C C   . PHE E  1 246 ? -29.689 22.691  62.316  1.00 13.78  ? 259 PHE E C   1 
ATOM   9472  O O   . PHE E  1 246 ? -29.059 23.754  62.293  1.00 13.83  ? 259 PHE E O   1 
ATOM   9473  C CB  . PHE E  1 246 ? -31.996 23.171  63.172  1.00 11.96  ? 259 PHE E CB  1 
ATOM   9474  C CG  . PHE E  1 246 ? -33.109 22.766  64.082  1.00 9.26   ? 259 PHE E CG  1 
ATOM   9475  C CD1 . PHE E  1 246 ? -33.414 23.527  65.203  1.00 6.05   ? 259 PHE E CD1 1 
ATOM   9476  C CD2 . PHE E  1 246 ? -33.844 21.614  63.828  1.00 6.09   ? 259 PHE E CD2 1 
ATOM   9477  C CE1 . PHE E  1 246 ? -34.444 23.151  66.056  1.00 7.78   ? 259 PHE E CE1 1 
ATOM   9478  C CE2 . PHE E  1 246 ? -34.874 21.230  64.672  1.00 7.14   ? 259 PHE E CE2 1 
ATOM   9479  C CZ  . PHE E  1 246 ? -35.175 21.999  65.792  1.00 7.50   ? 259 PHE E CZ  1 
ATOM   9480  N N   . PHE E  1 247 ? -29.539 21.733  61.405  1.00 14.42  ? 260 PHE E N   1 
ATOM   9481  C CA  . PHE E  1 247 ? -28.586 21.868  60.308  1.00 15.40  ? 260 PHE E CA  1 
ATOM   9482  C C   . PHE E  1 247 ? -29.131 22.802  59.238  1.00 15.82  ? 260 PHE E C   1 
ATOM   9483  O O   . PHE E  1 247 ? -30.349 22.902  59.050  1.00 15.97  ? 260 PHE E O   1 
ATOM   9484  C CB  . PHE E  1 247 ? -28.212 20.500  59.737  1.00 15.26  ? 260 PHE E CB  1 
ATOM   9485  C CG  . PHE E  1 247 ? -27.795 19.508  60.787  1.00 15.81  ? 260 PHE E CG  1 
ATOM   9486  C CD1 . PHE E  1 247 ? -26.902 19.873  61.794  1.00 14.70  ? 260 PHE E CD1 1 
ATOM   9487  C CD2 . PHE E  1 247 ? -28.298 18.216  60.779  1.00 17.61  ? 260 PHE E CD2 1 
ATOM   9488  C CE1 . PHE E  1 247 ? -26.522 18.970  62.769  1.00 10.78  ? 260 PHE E CE1 1 
ATOM   9489  C CE2 . PHE E  1 247 ? -27.915 17.302  61.754  1.00 15.91  ? 260 PHE E CE2 1 
ATOM   9490  C CZ  . PHE E  1 247 ? -27.030 17.684  62.749  1.00 12.41  ? 260 PHE E CZ  1 
ATOM   9491  N N   . ARG E  1 248 ? -28.228 23.504  58.561  1.00 15.92  ? 261 ARG E N   1 
ATOM   9492  C CA  . ARG E  1 248 ? -28.633 24.535  57.608  1.00 16.33  ? 261 ARG E CA  1 
ATOM   9493  C C   . ARG E  1 248 ? -28.726 23.997  56.185  1.00 16.10  ? 261 ARG E C   1 
ATOM   9494  O O   . ARG E  1 248 ? -29.676 24.309  55.472  1.00 16.10  ? 261 ARG E O   1 
ATOM   9495  C CB  . ARG E  1 248 ? -27.716 25.760  57.694  1.00 16.09  ? 261 ARG E CB  1 
ATOM   9496  C CG  . ARG E  1 248 ? -27.786 26.477  59.035  1.00 15.64  ? 261 ARG E CG  1 
ATOM   9497  C CD  . ARG E  1 248 ? -26.906 27.714  59.057  1.00 13.84  ? 261 ARG E CD  1 
ATOM   9498  N NE  . ARG E  1 248 ? -26.869 28.350  60.373  1.00 10.38  ? 261 ARG E NE  1 
ATOM   9499  C CZ  . ARG E  1 248 ? -27.772 29.223  60.821  1.00 12.67  ? 261 ARG E CZ  1 
ATOM   9500  N NH1 . ARG E  1 248 ? -28.814 29.580  60.071  1.00 6.76   ? 261 ARG E NH1 1 
ATOM   9501  N NH2 . ARG E  1 248 ? -27.633 29.740  62.033  1.00 8.75   ? 261 ARG E NH2 1 
ATOM   9502  N N   . GLY E  1 249 ? -27.753 23.182  55.785  1.00 15.98  ? 263 GLY E N   1 
ATOM   9503  C CA  . GLY E  1 249 ? -27.763 22.570  54.460  1.00 16.56  ? 263 GLY E CA  1 
ATOM   9504  C C   . GLY E  1 249 ? -26.604 21.628  54.199  1.00 17.09  ? 263 GLY E C   1 
ATOM   9505  O O   . GLY E  1 249 ? -26.511 20.556  54.805  1.00 16.75  ? 263 GLY E O   1 
ATOM   9506  N N   . GLU E  1 250 ? -25.724 22.036  53.286  1.00 17.54  ? 264 GLU E N   1 
ATOM   9507  C CA  . GLU E  1 250 ? -24.603 21.216  52.836  1.00 18.21  ? 264 GLU E CA  1 
ATOM   9508  C C   . GLU E  1 250 ? -23.278 21.927  53.082  1.00 17.49  ? 264 GLU E C   1 
ATOM   9509  O O   . GLU E  1 250 ? -23.175 23.138  52.895  1.00 17.79  ? 264 GLU E O   1 
ATOM   9510  C CB  . GLU E  1 250 ? -24.747 20.894  51.341  1.00 18.34  ? 264 GLU E CB  1 
ATOM   9511  C CG  . GLU E  1 250 ? -25.653 19.702  51.008  1.00 24.36  ? 264 GLU E CG  1 
ATOM   9512  C CD  . GLU E  1 250 ? -27.135 19.935  51.328  1.00 32.95  ? 264 GLU E CD  1 
ATOM   9513  O OE1 . GLU E  1 250 ? -27.637 21.068  51.135  1.00 34.18  ? 264 GLU E OE1 1 
ATOM   9514  O OE2 . GLU E  1 250 ? -27.801 18.970  51.770  1.00 34.91  ? 264 GLU E OE2 1 
ATOM   9515  N N   . SER E  1 251 ? -22.268 21.169  53.502  1.00 16.93  ? 265 SER E N   1 
ATOM   9516  C CA  . SER E  1 251 ? -20.909 21.694  53.658  1.00 15.94  ? 265 SER E CA  1 
ATOM   9517  C C   . SER E  1 251 ? -19.877 20.583  53.530  1.00 15.76  ? 265 SER E C   1 
ATOM   9518  O O   . SER E  1 251 ? -20.217 19.399  53.546  1.00 16.02  ? 265 SER E O   1 
ATOM   9519  C CB  . SER E  1 251 ? -20.735 22.437  54.997  1.00 16.09  ? 265 SER E CB  1 
ATOM   9520  O OG  . SER E  1 251 ? -21.066 21.631  56.118  1.00 12.06  ? 265 SER E OG  1 
ATOM   9521  N N   . LEU E  1 252 ? -18.617 20.977  53.394  1.00 15.39  ? 266 LEU E N   1 
ATOM   9522  C CA  . LEU E  1 252 ? -17.506 20.039  53.396  1.00 15.09  ? 266 LEU E CA  1 
ATOM   9523  C C   . LEU E  1 252 ? -16.640 20.291  54.623  1.00 14.90  ? 266 LEU E C   1 
ATOM   9524  O O   . LEU E  1 252 ? -16.372 21.441  54.974  1.00 15.55  ? 266 LEU E O   1 
ATOM   9525  C CB  . LEU E  1 252 ? -16.677 20.195  52.118  1.00 15.11  ? 266 LEU E CB  1 
ATOM   9526  C CG  . LEU E  1 252 ? -15.579 19.162  51.833  1.00 16.68  ? 266 LEU E CG  1 
ATOM   9527  C CD1 . LEU E  1 252 ? -16.162 17.807  51.430  1.00 14.32  ? 266 LEU E CD1 1 
ATOM   9528  C CD2 . LEU E  1 252 ? -14.635 19.678  50.760  1.00 15.89  ? 266 LEU E CD2 1 
ATOM   9529  N N   . GLY E  1 253 ? -16.219 19.217  55.281  1.00 14.60  ? 267 GLY E N   1 
ATOM   9530  C CA  . GLY E  1 253 ? -15.310 19.322  56.417  1.00 15.12  ? 267 GLY E CA  1 
ATOM   9531  C C   . GLY E  1 253 ? -13.872 19.208  55.958  1.00 15.55  ? 267 GLY E C   1 
ATOM   9532  O O   . GLY E  1 253 ? -13.560 18.383  55.104  1.00 16.33  ? 267 GLY E O   1 
ATOM   9533  N N   . VAL E  1 254 ? -12.993 20.038  56.514  1.00 15.62  ? 268 VAL E N   1 
ATOM   9534  C CA  . VAL E  1 254 ? -11.572 20.013  56.159  1.00 16.01  ? 268 VAL E CA  1 
ATOM   9535  C C   . VAL E  1 254 ? -10.706 20.003  57.419  1.00 16.26  ? 268 VAL E C   1 
ATOM   9536  O O   . VAL E  1 254 ? -10.976 20.736  58.366  1.00 16.95  ? 268 VAL E O   1 
ATOM   9537  C CB  . VAL E  1 254 ? -11.187 21.221  55.247  1.00 16.51  ? 268 VAL E CB  1 
ATOM   9538  C CG1 . VAL E  1 254 ? -9.689  21.255  54.965  1.00 16.41  ? 268 VAL E CG1 1 
ATOM   9539  C CG2 . VAL E  1 254 ? -11.960 21.175  53.936  1.00 17.28  ? 268 VAL E CG2 1 
ATOM   9540  N N   . GLN E  1 255 ? -9.678  19.159  57.429  1.00 16.65  ? 269 GLN E N   1 
ATOM   9541  C CA  . GLN E  1 255 ? -8.693  19.151  58.510  1.00 16.48  ? 269 GLN E CA  1 
ATOM   9542  C C   . GLN E  1 255 ? -7.359  19.621  57.969  1.00 15.98  ? 269 GLN E C   1 
ATOM   9543  O O   . GLN E  1 255 ? -6.800  18.993  57.073  1.00 16.49  ? 269 GLN E O   1 
ATOM   9544  C CB  . GLN E  1 255 ? -8.548  17.757  59.114  1.00 16.52  ? 269 GLN E CB  1 
ATOM   9545  C CG  . GLN E  1 255 ? -9.690  17.363  60.025  1.00 18.14  ? 269 GLN E CG  1 
ATOM   9546  C CD  . GLN E  1 255 ? -9.461  16.033  60.704  1.00 18.39  ? 269 GLN E CD  1 
ATOM   9547  O OE1 . GLN E  1 255 ? -8.911  15.106  60.109  1.00 22.22  ? 269 GLN E OE1 1 
ATOM   9548  N NE2 . GLN E  1 255 ? -9.892  15.925  61.957  1.00 19.01  ? 269 GLN E NE2 1 
ATOM   9549  N N   . SER E  1 256 ? -6.857  20.725  58.517  1.00 15.26  ? 270 SER E N   1 
ATOM   9550  C CA  . SER E  1 256 ? -5.658  21.372  57.993  1.00 14.69  ? 270 SER E CA  1 
ATOM   9551  C C   . SER E  1 256 ? -4.953  22.251  59.020  1.00 14.66  ? 270 SER E C   1 
ATOM   9552  O O   . SER E  1 256 ? -5.544  22.665  60.022  1.00 15.30  ? 270 SER E O   1 
ATOM   9553  C CB  . SER E  1 256 ? -6.015  22.220  56.771  1.00 14.54  ? 270 SER E CB  1 
ATOM   9554  O OG  . SER E  1 256 ? -4.856  22.798  56.201  1.00 13.17  ? 270 SER E OG  1 
ATOM   9555  N N   . ASP E  1 257 ? -3.681  22.529  58.755  1.00 13.73  ? 271 ASP E N   1 
ATOM   9556  C CA  . ASP E  1 257 ? -2.931  23.520  59.518  1.00 13.17  ? 271 ASP E CA  1 
ATOM   9557  C C   . ASP E  1 257 ? -2.549  24.698  58.615  1.00 12.47  ? 271 ASP E C   1 
ATOM   9558  O O   . ASP E  1 257 ? -1.738  25.550  58.986  1.00 12.47  ? 271 ASP E O   1 
ATOM   9559  C CB  . ASP E  1 257 ? -1.703  22.883  60.192  1.00 13.15  ? 271 ASP E CB  1 
ATOM   9560  C CG  . ASP E  1 257 ? -0.631  22.440  59.198  1.00 13.61  ? 271 ASP E CG  1 
ATOM   9561  O OD1 . ASP E  1 257 ? -0.960  21.979  58.081  1.00 12.20  ? 271 ASP E OD1 1 
ATOM   9562  O OD2 . ASP E  1 257 ? 0.559   22.544  59.551  1.00 16.34  ? 271 ASP E OD2 1 
ATOM   9563  N N   . ALA E  1 258 ? -3.165  24.739  57.436  1.00 11.93  ? 272 ALA E N   1 
ATOM   9564  C CA  . ALA E  1 258 ? -2.886  25.763  56.437  1.00 11.63  ? 272 ALA E CA  1 
ATOM   9565  C C   . ALA E  1 258 ? -3.801  26.975  56.593  1.00 11.19  ? 272 ALA E C   1 
ATOM   9566  O O   . ALA E  1 258 ? -5.012  26.822  56.742  1.00 10.67  ? 272 ALA E O   1 
ATOM   9567  C CB  . ALA E  1 258 ? -3.005  25.181  55.030  1.00 11.47  ? 272 ALA E CB  1 
ATOM   9568  N N   . PRO E  1 259 ? -3.219  28.189  56.549  1.00 11.56  ? 273 PRO E N   1 
ATOM   9569  C CA  . PRO E  1 259 ? -3.979  29.437  56.658  1.00 11.69  ? 273 PRO E CA  1 
ATOM   9570  C C   . PRO E  1 259 ? -5.018  29.585  55.548  1.00 11.83  ? 273 PRO E C   1 
ATOM   9571  O O   . PRO E  1 259 ? -4.841  29.038  54.458  1.00 12.50  ? 273 PRO E O   1 
ATOM   9572  C CB  . PRO E  1 259 ? -2.899  30.518  56.510  1.00 11.66  ? 273 PRO E CB  1 
ATOM   9573  C CG  . PRO E  1 259 ? -1.756  29.836  55.835  1.00 10.52  ? 273 PRO E CG  1 
ATOM   9574  C CD  . PRO E  1 259 ? -1.778  28.445  56.362  1.00 10.96  ? 273 PRO E CD  1 
ATOM   9575  N N   . LEU E  1 260 ? -6.094  30.313  55.828  1.00 11.71  ? 274 LEU E N   1 
ATOM   9576  C CA  . LEU E  1 260 ? -7.128  30.561  54.827  1.00 11.60  ? 274 LEU E CA  1 
ATOM   9577  C C   . LEU E  1 260 ? -6.634  31.565  53.798  1.00 11.93  ? 274 LEU E C   1 
ATOM   9578  O O   . LEU E  1 260 ? -5.826  32.434  54.114  1.00 11.61  ? 274 LEU E O   1 
ATOM   9579  C CB  . LEU E  1 260 ? -8.417  31.078  55.477  1.00 11.35  ? 274 LEU E CB  1 
ATOM   9580  C CG  . LEU E  1 260 ? -9.173  30.269  56.541  1.00 10.19  ? 274 LEU E CG  1 
ATOM   9581  C CD1 . LEU E  1 260 ? -10.631 30.705  56.555  1.00 7.43   ? 274 LEU E CD1 1 
ATOM   9582  C CD2 . LEU E  1 260 ? -9.084  28.759  56.334  1.00 7.94   ? 274 LEU E CD2 1 
ATOM   9583  N N   . ASP E  1 261 ? -7.113  31.435  52.565  1.00 13.33  ? 275 ASP E N   1 
ATOM   9584  C CA  . ASP E  1 261 ? -6.775  32.384  51.507  1.00 14.49  ? 275 ASP E CA  1 
ATOM   9585  C C   . ASP E  1 261 ? -7.981  32.653  50.616  1.00 14.86  ? 275 ASP E C   1 
ATOM   9586  O O   . ASP E  1 261 ? -8.367  31.820  49.797  1.00 15.14  ? 275 ASP E O   1 
ATOM   9587  C CB  . ASP E  1 261 ? -5.583  31.888  50.680  1.00 14.68  ? 275 ASP E CB  1 
ATOM   9588  C CG  . ASP E  1 261 ? -4.954  32.984  49.822  1.00 17.16  ? 275 ASP E CG  1 
ATOM   9589  O OD1 . ASP E  1 261 ? -5.689  33.846  49.287  1.00 17.54  ? 275 ASP E OD1 1 
ATOM   9590  O OD2 . ASP E  1 261 ? -3.711  32.975  49.673  1.00 18.91  ? 275 ASP E OD2 1 
ATOM   9591  N N   . SER E  1 262 ? -8.558  33.837  50.784  1.00 16.13  ? 276 SER E N   1 
ATOM   9592  C CA  . SER E  1 262 ? -9.732  34.263  50.028  1.00 16.86  ? 276 SER E CA  1 
ATOM   9593  C C   . SER E  1 262 ? -9.448  34.541  48.546  1.00 17.30  ? 276 SER E C   1 
ATOM   9594  O O   . SER E  1 262 ? -10.381 34.758  47.772  1.00 17.83  ? 276 SER E O   1 
ATOM   9595  C CB  . SER E  1 262 ? -10.355 35.501  50.690  1.00 17.19  ? 276 SER E CB  1 
ATOM   9596  O OG  . SER E  1 262 ? -9.382  36.509  50.922  1.00 16.57  ? 276 SER E OG  1 
ATOM   9597  N N   . SER E  1 263 A -8.174  34.522  48.150  1.00 17.11  ? 276 SER E N   1 
ATOM   9598  C CA  . SER E  1 263 A -7.789  34.911  46.789  1.00 17.38  ? 276 SER E CA  1 
ATOM   9599  C C   . SER E  1 263 A -7.528  33.753  45.809  1.00 17.99  ? 276 SER E C   1 
ATOM   9600  O O   . SER E  1 263 A -7.254  33.992  44.627  1.00 18.16  ? 276 SER E O   1 
ATOM   9601  C CB  . SER E  1 263 A -6.593  35.869  46.820  1.00 17.20  ? 276 SER E CB  1 
ATOM   9602  O OG  . SER E  1 263 A -5.378  35.166  46.999  1.00 16.66  ? 276 SER E OG  1 
ATOM   9603  N N   . CYS E  1 264 ? -7.600  32.512  46.288  1.00 17.88  ? 277 CYS E N   1 
ATOM   9604  C CA  . CYS E  1 264 ? -7.531  31.355  45.390  1.00 18.23  ? 277 CYS E CA  1 
ATOM   9605  C C   . CYS E  1 264 ? -8.795  30.502  45.466  1.00 18.06  ? 277 CYS E C   1 
ATOM   9606  O O   . CYS E  1 264 ? -9.464  30.468  46.496  1.00 18.49  ? 277 CYS E O   1 
ATOM   9607  C CB  . CYS E  1 264 ? -6.264  30.518  45.627  1.00 18.29  ? 277 CYS E CB  1 
ATOM   9608  S SG  . CYS E  1 264 ? -6.008  29.909  47.310  1.00 22.29  ? 277 CYS E SG  1 
ATOM   9609  N N   . ARG E  1 265 ? -9.115  29.827  44.364  1.00 18.48  ? 278 ARG E N   1 
ATOM   9610  C CA  . ARG E  1 265 ? -10.320 29.006  44.259  1.00 18.71  ? 278 ARG E CA  1 
ATOM   9611  C C   . ARG E  1 265 ? -9.955  27.534  44.093  1.00 18.41  ? 278 ARG E C   1 
ATOM   9612  O O   . ARG E  1 265 ? -9.064  27.191  43.313  1.00 18.66  ? 278 ARG E O   1 
ATOM   9613  C CB  . ARG E  1 265 ? -11.173 29.468  43.075  1.00 18.95  ? 278 ARG E CB  1 
ATOM   9614  C CG  . ARG E  1 265 ? -12.611 28.981  43.105  1.00 22.11  ? 278 ARG E CG  1 
ATOM   9615  C CD  . ARG E  1 265 ? -13.350 29.385  41.841  1.00 28.96  ? 278 ARG E CD  1 
ATOM   9616  N NE  . ARG E  1 265 ? -14.801 29.414  42.038  1.00 34.22  ? 278 ARG E NE  1 
ATOM   9617  C CZ  . ARG E  1 265 ? -15.513 30.515  42.281  1.00 35.71  ? 278 ARG E CZ  1 
ATOM   9618  N NH1 . ARG E  1 265 ? -14.923 31.705  42.361  1.00 32.54  ? 278 ARG E NH1 1 
ATOM   9619  N NH2 . ARG E  1 265 ? -16.827 30.426  42.443  1.00 36.75  ? 278 ARG E NH2 1 
ATOM   9620  N N   . GLY E  1 266 ? -10.651 26.669  44.827  1.00 17.95  ? 279 GLY E N   1 
ATOM   9621  C CA  . GLY E  1 266 ? -10.395 25.232  44.780  1.00 16.87  ? 279 GLY E CA  1 
ATOM   9622  C C   . GLY E  1 266 ? -11.541 24.414  45.338  1.00 16.92  ? 279 GLY E C   1 
ATOM   9623  O O   . GLY E  1 266 ? -12.377 24.926  46.084  1.00 17.45  ? 279 GLY E O   1 
ATOM   9624  N N   . ASP E  1 267 ? -11.574 23.136  44.974  1.00 16.69  ? 280 ASP E N   1 
ATOM   9625  C CA  . ASP E  1 267 ? -12.612 22.222  45.442  1.00 16.17  ? 280 ASP E CA  1 
ATOM   9626  C C   . ASP E  1 267 ? -12.016 20.935  46.002  1.00 15.75  ? 280 ASP E C   1 
ATOM   9627  O O   . ASP E  1 267 ? -12.743 20.004  46.350  1.00 16.46  ? 280 ASP E O   1 
ATOM   9628  C CB  . ASP E  1 267 ? -13.598 21.920  44.311  1.00 16.32  ? 280 ASP E CB  1 
ATOM   9629  C CG  . ASP E  1 267 ? -14.494 23.103  43.989  1.00 17.80  ? 280 ASP E CG  1 
ATOM   9630  O OD1 . ASP E  1 267 ? -15.307 23.495  44.855  1.00 18.45  ? 280 ASP E OD1 1 
ATOM   9631  O OD2 . ASP E  1 267 ? -14.389 23.640  42.869  1.00 20.10  ? 280 ASP E OD2 1 
ATOM   9632  N N   . CYS E  1 268 ? -10.689 20.896  46.091  1.00 15.07  ? 281 CYS E N   1 
ATOM   9633  C CA  . CYS E  1 268 ? -9.968  19.737  46.606  1.00 14.29  ? 281 CYS E CA  1 
ATOM   9634  C C   . CYS E  1 268 ? -9.024  20.164  47.721  1.00 13.53  ? 281 CYS E C   1 
ATOM   9635  O O   . CYS E  1 268 ? -8.064  20.900  47.485  1.00 13.60  ? 281 CYS E O   1 
ATOM   9636  C CB  . CYS E  1 268 ? -9.184  19.053  45.488  1.00 14.40  ? 281 CYS E CB  1 
ATOM   9637  S SG  . CYS E  1 268 ? -8.207  17.646  46.037  1.00 15.14  ? 281 CYS E SG  1 
ATOM   9638  N N   . PHE E  1 269 ? -9.297  19.685  48.931  1.00 12.54  ? 282 PHE E N   1 
ATOM   9639  C CA  . PHE E  1 269 ? -8.580  20.137  50.118  1.00 12.23  ? 282 PHE E CA  1 
ATOM   9640  C C   . PHE E  1 269 ? -7.934  18.978  50.858  1.00 12.03  ? 282 PHE E C   1 
ATOM   9641  O O   . PHE E  1 269 ? -8.381  17.832  50.753  1.00 11.87  ? 282 PHE E O   1 
ATOM   9642  C CB  . PHE E  1 269 ? -9.526  20.906  51.052  1.00 11.78  ? 282 PHE E CB  1 
ATOM   9643  C CG  . PHE E  1 269 ? -10.358 21.943  50.350  1.00 13.24  ? 282 PHE E CG  1 
ATOM   9644  C CD1 . PHE E  1 269 ? -9.852  23.225  50.120  1.00 14.83  ? 282 PHE E CD1 1 
ATOM   9645  C CD2 . PHE E  1 269 ? -11.642 21.636  49.902  1.00 12.04  ? 282 PHE E CD2 1 
ATOM   9646  C CE1 . PHE E  1 269 ? -10.617 24.186  49.458  1.00 15.54  ? 282 PHE E CE1 1 
ATOM   9647  C CE2 . PHE E  1 269 ? -12.416 22.587  49.241  1.00 15.52  ? 282 PHE E CE2 1 
ATOM   9648  C CZ  . PHE E  1 269 ? -11.905 23.865  49.019  1.00 16.03  ? 282 PHE E CZ  1 
ATOM   9649  N N   . HIS E  1 270 ? -6.882  19.286  51.609  1.00 12.23  ? 283 HIS E N   1 
ATOM   9650  C CA  . HIS E  1 270 ? -6.175  18.280  52.395  1.00 12.70  ? 283 HIS E CA  1 
ATOM   9651  C C   . HIS E  1 270 ? -5.368  18.899  53.536  1.00 12.99  ? 283 HIS E C   1 
ATOM   9652  O O   . HIS E  1 270 ? -5.309  20.119  53.683  1.00 13.16  ? 283 HIS E O   1 
ATOM   9653  C CB  . HIS E  1 270 ? -5.262  17.440  51.493  1.00 12.42  ? 283 HIS E CB  1 
ATOM   9654  C CG  . HIS E  1 270 ? -4.105  18.202  50.930  1.00 9.54   ? 283 HIS E CG  1 
ATOM   9655  N ND1 . HIS E  1 270 ? -2.840  18.138  51.472  1.00 8.36   ? 283 HIS E ND1 1 
ATOM   9656  C CD2 . HIS E  1 270 ? -4.021  19.048  49.878  1.00 7.36   ? 283 HIS E CD2 1 
ATOM   9657  C CE1 . HIS E  1 270 ? -2.024  18.906  50.772  1.00 7.99   ? 283 HIS E CE1 1 
ATOM   9658  N NE2 . HIS E  1 270 ? -2.716  19.471  49.800  1.00 7.01   ? 283 HIS E NE2 1 
ATOM   9659  N N   . SER E  1 271 ? -4.745  18.033  54.328  1.00 13.94  ? 284 SER E N   1 
ATOM   9660  C CA  . SER E  1 271 ? -3.929  18.419  55.477  1.00 14.74  ? 284 SER E CA  1 
ATOM   9661  C C   . SER E  1 271 ? -3.037  19.637  55.228  1.00 15.14  ? 284 SER E C   1 
ATOM   9662  O O   . SER E  1 271 ? -3.037  20.586  56.018  1.00 15.58  ? 284 SER E O   1 
ATOM   9663  C CB  . SER E  1 271 ? -3.071  17.228  55.912  1.00 14.53  ? 284 SER E CB  1 
ATOM   9664  O OG  . SER E  1 271 ? -2.434  17.486  57.145  1.00 16.34  ? 284 SER E OG  1 
ATOM   9665  N N   . GLY E  1 272 ? -2.294  19.610  54.124  1.00 14.93  ? 285 GLY E N   1 
ATOM   9666  C CA  . GLY E  1 272 ? -1.308  20.643  53.828  1.00 14.75  ? 285 GLY E CA  1 
ATOM   9667  C C   . GLY E  1 272 ? -1.713  21.697  52.814  1.00 15.04  ? 285 GLY E C   1 
ATOM   9668  O O   . GLY E  1 272 ? -0.848  22.346  52.225  1.00 15.78  ? 285 GLY E O   1 
ATOM   9669  N N   . GLY E  1 273 ? -3.018  21.877  52.606  1.00 14.93  ? 286 GLY E N   1 
ATOM   9670  C CA  . GLY E  1 273 ? -3.512  22.938  51.728  1.00 14.64  ? 286 GLY E CA  1 
ATOM   9671  C C   . GLY E  1 273 ? -4.561  22.521  50.716  1.00 15.12  ? 286 GLY E C   1 
ATOM   9672  O O   . GLY E  1 273 ? -5.427  21.693  51.014  1.00 15.87  ? 286 GLY E O   1 
ATOM   9673  N N   . THR E  1 274 ? -4.470  23.100  49.516  1.00 14.69  ? 287 THR E N   1 
ATOM   9674  C CA  . THR E  1 274 ? -5.455  22.915  48.444  1.00 14.38  ? 287 THR E CA  1 
ATOM   9675  C C   . THR E  1 274 ? -4.778  22.482  47.146  1.00 14.27  ? 287 THR E C   1 
ATOM   9676  O O   . THR E  1 274 ? -3.709  22.995  46.793  1.00 14.48  ? 287 THR E O   1 
ATOM   9677  C CB  . THR E  1 274 ? -6.219  24.236  48.148  1.00 14.22  ? 287 THR E CB  1 
ATOM   9678  O OG1 . THR E  1 274 ? -6.692  24.810  49.368  1.00 13.61  ? 287 THR E OG1 1 
ATOM   9679  C CG2 . THR E  1 274 ? -7.405  24.003  47.214  1.00 14.38  ? 287 THR E CG2 1 
ATOM   9680  N N   . ILE E  1 275 ? -5.412  21.546  46.440  1.00 13.62  ? 288 ILE E N   1 
ATOM   9681  C CA  . ILE E  1 275 ? -4.945  21.110  45.123  1.00 13.05  ? 288 ILE E CA  1 
ATOM   9682  C C   . ILE E  1 275 ? -5.829  21.715  44.036  1.00 13.66  ? 288 ILE E C   1 
ATOM   9683  O O   . ILE E  1 275 ? -7.010  21.376  43.917  1.00 14.29  ? 288 ILE E O   1 
ATOM   9684  C CB  . ILE E  1 275 ? -4.903  19.563  44.987  1.00 12.66  ? 288 ILE E CB  1 
ATOM   9685  C CG1 . ILE E  1 275 ? -4.108  18.941  46.140  1.00 10.38  ? 288 ILE E CG1 1 
ATOM   9686  C CG2 . ILE E  1 275 ? -4.319  19.158  43.631  1.00 10.25  ? 288 ILE E CG2 1 
ATOM   9687  C CD1 . ILE E  1 275 ? -4.094  17.427  46.147  1.00 8.74   ? 288 ILE E CD1 1 
ATOM   9688  N N   . VAL E  1 276 ? -5.239  22.620  43.260  1.00 13.71  ? 289 VAL E N   1 
ATOM   9689  C CA  . VAL E  1 276 ? -5.920  23.306  42.167  1.00 14.02  ? 289 VAL E CA  1 
ATOM   9690  C C   . VAL E  1 276 ? -5.372  22.759  40.858  1.00 14.10  ? 289 VAL E C   1 
ATOM   9691  O O   . VAL E  1 276 ? -4.218  23.016  40.501  1.00 14.84  ? 289 VAL E O   1 
ATOM   9692  C CB  . VAL E  1 276 ? -5.701  24.843  42.239  1.00 14.61  ? 289 VAL E CB  1 
ATOM   9693  C CG1 . VAL E  1 276 ? -6.337  25.550  41.040  1.00 13.91  ? 289 VAL E CG1 1 
ATOM   9694  C CG2 . VAL E  1 276 ? -6.252  25.406  43.546  1.00 14.99  ? 289 VAL E CG2 1 
ATOM   9695  N N   . SER E  1 277 ? -6.198  21.993  40.150  1.00 13.86  ? 290 SER E N   1 
ATOM   9696  C CA  . SER E  1 277 ? -5.735  21.256  38.980  1.00 13.82  ? 290 SER E CA  1 
ATOM   9697  C C   . SER E  1 277 ? -6.874  20.798  38.072  1.00 13.76  ? 290 SER E C   1 
ATOM   9698  O O   . SER E  1 277 ? -8.014  20.637  38.513  1.00 13.89  ? 290 SER E O   1 
ATOM   9699  C CB  . SER E  1 277 ? -4.908  20.041  39.426  1.00 13.90  ? 290 SER E CB  1 
ATOM   9700  O OG  . SER E  1 277 ? -4.125  19.519  38.365  1.00 13.33  ? 290 SER E OG  1 
ATOM   9701  N N   . SER E  1 278 ? -6.541  20.599  36.800  1.00 14.01  ? 291 SER E N   1 
ATOM   9702  C CA  . SER E  1 278 ? -7.427  19.962  35.828  1.00 13.96  ? 291 SER E CA  1 
ATOM   9703  C C   . SER E  1 278 ? -6.897  18.577  35.458  1.00 12.95  ? 291 SER E C   1 
ATOM   9704  O O   . SER E  1 278 ? -7.536  17.835  34.699  1.00 12.26  ? 291 SER E O   1 
ATOM   9705  C CB  . SER E  1 278 ? -7.543  20.821  34.571  1.00 14.05  ? 291 SER E CB  1 
ATOM   9706  O OG  . SER E  1 278 ? -8.252  22.014  34.836  1.00 18.03  ? 291 SER E OG  1 
ATOM   9707  N N   . LEU E  1 279 ? -5.726  18.241  35.999  1.00 11.96  ? 292 LEU E N   1 
ATOM   9708  C CA  . LEU E  1 279 ? -5.077  16.965  35.716  1.00 11.45  ? 292 LEU E CA  1 
ATOM   9709  C C   . LEU E  1 279 ? -5.818  15.813  36.398  1.00 11.75  ? 292 LEU E C   1 
ATOM   9710  O O   . LEU E  1 279 ? -6.344  15.976  37.508  1.00 10.74  ? 292 LEU E O   1 
ATOM   9711  C CB  . LEU E  1 279 ? -3.592  16.988  36.117  1.00 10.43  ? 292 LEU E CB  1 
ATOM   9712  C CG  . LEU E  1 279 ? -2.719  18.134  35.578  1.00 10.46  ? 292 LEU E CG  1 
ATOM   9713  C CD1 . LEU E  1 279 ? -1.272  18.001  36.041  1.00 3.70   ? 292 LEU E CD1 1 
ATOM   9714  C CD2 . LEU E  1 279 ? -2.788  18.249  34.056  1.00 7.04   ? 292 LEU E CD2 1 
ATOM   9715  N N   . PRO E  1 280 ? -5.875  14.648  35.725  1.00 12.17  ? 293 PRO E N   1 
ATOM   9716  C CA  . PRO E  1 280 ? -6.608  13.488  36.238  1.00 12.51  ? 293 PRO E CA  1 
ATOM   9717  C C   . PRO E  1 280 ? -6.003  12.869  37.505  1.00 12.46  ? 293 PRO E C   1 
ATOM   9718  O O   . PRO E  1 280 ? -6.721  12.201  38.253  1.00 13.54  ? 293 PRO E O   1 
ATOM   9719  C CB  . PRO E  1 280 ? -6.538  12.490  35.075  1.00 12.60  ? 293 PRO E CB  1 
ATOM   9720  C CG  . PRO E  1 280 ? -5.307  12.887  34.315  1.00 12.55  ? 293 PRO E CG  1 
ATOM   9721  C CD  . PRO E  1 280 ? -5.282  14.379  34.400  1.00 11.58  ? 293 PRO E CD  1 
ATOM   9722  N N   . PHE E  1 281 ? -4.707  13.078  37.738  1.00 11.69  ? 294 PHE E N   1 
ATOM   9723  C CA  . PHE E  1 281 ? -4.027  12.475  38.892  1.00 11.34  ? 294 PHE E CA  1 
ATOM   9724  C C   . PHE E  1 281 ? -3.252  13.485  39.732  1.00 11.45  ? 294 PHE E C   1 
ATOM   9725  O O   . PHE E  1 281 ? -2.908  14.570  39.258  1.00 12.53  ? 294 PHE E O   1 
ATOM   9726  C CB  . PHE E  1 281 ? -3.079  11.349  38.452  1.00 11.17  ? 294 PHE E CB  1 
ATOM   9727  C CG  . PHE E  1 281 ? -3.644  10.450  37.385  1.00 9.86   ? 294 PHE E CG  1 
ATOM   9728  C CD1 . PHE E  1 281 ? -3.097  10.448  36.107  1.00 8.28   ? 294 PHE E CD1 1 
ATOM   9729  C CD2 . PHE E  1 281 ? -4.721  9.609   37.657  1.00 7.25   ? 294 PHE E CD2 1 
ATOM   9730  C CE1 . PHE E  1 281 ? -3.615  9.625   35.113  1.00 10.35  ? 294 PHE E CE1 1 
ATOM   9731  C CE2 . PHE E  1 281 ? -5.246  8.784   36.674  1.00 5.82   ? 294 PHE E CE2 1 
ATOM   9732  C CZ  . PHE E  1 281 ? -4.696  8.791   35.398  1.00 9.97   ? 294 PHE E CZ  1 
ATOM   9733  N N   . GLN E  1 282 ? -2.976  13.114  40.980  1.00 10.82  ? 295 GLN E N   1 
ATOM   9734  C CA  . GLN E  1 282 ? -2.174  13.938  41.885  1.00 9.73   ? 295 GLN E CA  1 
ATOM   9735  C C   . GLN E  1 282 ? -1.252  13.094  42.774  1.00 9.40   ? 295 GLN E C   1 
ATOM   9736  O O   . GLN E  1 282 ? -1.650  12.036  43.262  1.00 8.62   ? 295 GLN E O   1 
ATOM   9737  C CB  . GLN E  1 282 ? -3.075  14.857  42.726  1.00 9.90   ? 295 GLN E CB  1 
ATOM   9738  C CG  . GLN E  1 282 ? -4.143  14.153  43.584  1.00 8.97   ? 295 GLN E CG  1 
ATOM   9739  C CD  . GLN E  1 282 ? -3.684  13.830  45.007  1.00 10.87  ? 295 GLN E CD  1 
ATOM   9740  O OE1 . GLN E  1 282 ? -2.545  14.107  45.395  1.00 10.99  ? 295 GLN E OE1 1 
ATOM   9741  N NE2 . GLN E  1 282 ? -4.583  13.243  45.793  1.00 9.56   ? 295 GLN E NE2 1 
ATOM   9742  N N   . ASN E  1 283 ? -0.021  13.562  42.966  1.00 9.53   ? 296 ASN E N   1 
ATOM   9743  C CA  . ASN E  1 283 ? 0.942   12.896  43.847  1.00 9.63   ? 296 ASN E CA  1 
ATOM   9744  C C   . ASN E  1 283 ? 1.237   13.719  45.106  1.00 9.83   ? 296 ASN E C   1 
ATOM   9745  O O   . ASN E  1 283 ? 2.315   13.610  45.695  1.00 9.48   ? 296 ASN E O   1 
ATOM   9746  C CB  . ASN E  1 283 ? 2.237   12.594  43.084  1.00 9.84   ? 296 ASN E CB  1 
ATOM   9747  C CG  . ASN E  1 283 ? 3.192   11.688  43.861  1.00 12.15  ? 296 ASN E CG  1 
ATOM   9748  O OD1 . ASN E  1 283 ? 4.389   11.962  43.940  1.00 12.97  ? 296 ASN E OD1 1 
ATOM   9749  N ND2 . ASN E  1 283 ? 2.664   10.612  44.440  1.00 13.82  ? 296 ASN E ND2 1 
ATOM   9750  N N   . ILE E  1 284 ? 0.263   14.524  45.526  1.00 9.92   ? 297 ILE E N   1 
ATOM   9751  C CA  . ILE E  1 284 ? 0.455   15.458  46.637  1.00 10.28  ? 297 ILE E CA  1 
ATOM   9752  C C   . ILE E  1 284 ? 0.078   14.855  47.992  1.00 12.03  ? 297 ILE E C   1 
ATOM   9753  O O   . ILE E  1 284 ? 0.894   14.837  48.914  1.00 12.83  ? 297 ILE E O   1 
ATOM   9754  C CB  . ILE E  1 284 ? -0.294  16.796  46.391  1.00 9.86   ? 297 ILE E CB  1 
ATOM   9755  C CG1 . ILE E  1 284 ? 0.337   17.543  45.210  1.00 7.19   ? 297 ILE E CG1 1 
ATOM   9756  C CG2 . ILE E  1 284 ? -0.291  17.665  47.645  1.00 7.12   ? 297 ILE E CG2 1 
ATOM   9757  C CD1 . ILE E  1 284 ? -0.539  18.617  44.606  1.00 4.53   ? 297 ILE E CD1 1 
ATOM   9758  N N   . ASN E  1 285 ? -1.154  14.369  48.112  1.00 13.51  ? 298 ASN E N   1 
ATOM   9759  C CA  . ASN E  1 285 ? -1.611  13.730  49.343  1.00 14.43  ? 298 ASN E CA  1 
ATOM   9760  C C   . ASN E  1 285 ? -2.577  12.596  49.043  1.00 15.27  ? 298 ASN E C   1 
ATOM   9761  O O   . ASN E  1 285 ? -3.506  12.754  48.242  1.00 15.48  ? 298 ASN E O   1 
ATOM   9762  C CB  . ASN E  1 285 ? -2.270  14.749  50.275  1.00 14.54  ? 298 ASN E CB  1 
ATOM   9763  C CG  . ASN E  1 285 ? -2.291  14.296  51.731  1.00 16.12  ? 298 ASN E CG  1 
ATOM   9764  O OD1 . ASN E  1 285 ? -2.388  13.105  52.036  1.00 19.86  ? 298 ASN E OD1 1 
ATOM   9765  N ND2 . ASN E  1 285 ? -2.210  15.257  52.640  1.00 17.86  ? 298 ASN E ND2 1 
ATOM   9766  N N   . SER E  1 286 ? -2.343  11.451  49.684  1.00 14.98  ? 299 SER E N   1 
ATOM   9767  C CA  . SER E  1 286 ? -3.226  10.300  49.553  1.00 14.70  ? 299 SER E CA  1 
ATOM   9768  C C   . SER E  1 286 ? -4.555  10.556  50.249  1.00 14.19  ? 299 SER E C   1 
ATOM   9769  O O   . SER E  1 286 ? -5.590  10.046  49.825  1.00 14.22  ? 299 SER E O   1 
ATOM   9770  C CB  . SER E  1 286 ? -2.562  9.033   50.102  1.00 15.21  ? 299 SER E CB  1 
ATOM   9771  O OG  . SER E  1 286 ? -2.060  9.230   51.412  1.00 15.82  ? 299 SER E OG  1 
ATOM   9772  N N   . ARG E  1 287 ? -4.514  11.358  51.308  1.00 14.15  ? 300 ARG E N   1 
ATOM   9773  C CA  . ARG E  1 287 ? -5.711  11.701  52.067  1.00 14.33  ? 300 ARG E CA  1 
ATOM   9774  C C   . ARG E  1 287 ? -6.228  13.074  51.651  1.00 13.01  ? 300 ARG E C   1 
ATOM   9775  O O   . ARG E  1 287 ? -5.615  14.093  51.966  1.00 12.31  ? 300 ARG E O   1 
ATOM   9776  C CB  . ARG E  1 287 ? -5.436  11.681  53.579  1.00 14.59  ? 300 ARG E CB  1 
ATOM   9777  C CG  . ARG E  1 287 ? -4.691  10.450  54.097  1.00 17.34  ? 300 ARG E CG  1 
ATOM   9778  C CD  . ARG E  1 287 ? -4.972  10.171  55.586  1.00 23.55  ? 300 ARG E CD  1 
ATOM   9779  N NE  . ARG E  1 287 ? -4.874  11.364  56.431  1.00 30.75  ? 300 ARG E NE  1 
ATOM   9780  C CZ  . ARG E  1 287 ? -5.905  11.959  57.031  1.00 33.99  ? 300 ARG E CZ  1 
ATOM   9781  N NH1 . ARG E  1 287 ? -7.137  11.478  56.900  1.00 35.67  ? 300 ARG E NH1 1 
ATOM   9782  N NH2 . ARG E  1 287 ? -5.704  13.041  57.773  1.00 35.96  ? 300 ARG E NH2 1 
ATOM   9783  N N   . THR E  1 288 ? -7.346  13.093  50.930  1.00 12.78  ? 301 THR E N   1 
ATOM   9784  C CA  . THR E  1 288 ? -7.969  14.349  50.499  1.00 13.04  ? 301 THR E CA  1 
ATOM   9785  C C   . THR E  1 288 ? -9.473  14.353  50.777  1.00 13.36  ? 301 THR E C   1 
ATOM   9786  O O   . THR E  1 288 ? -10.064 13.304  51.053  1.00 13.71  ? 301 THR E O   1 
ATOM   9787  C CB  . THR E  1 288 ? -7.760  14.628  48.986  1.00 12.68  ? 301 THR E CB  1 
ATOM   9788  O OG1 . THR E  1 288 ? -8.479  13.661  48.214  1.00 13.67  ? 301 THR E OG1 1 
ATOM   9789  C CG2 . THR E  1 288 ? -6.286  14.594  48.598  1.00 12.18  ? 301 THR E CG2 1 
ATOM   9790  N N   . VAL E  1 289 ? -10.076 15.540  50.706  1.00 13.12  ? 302 VAL E N   1 
ATOM   9791  C CA  . VAL E  1 289 ? -11.531 15.702  50.791  1.00 12.52  ? 302 VAL E CA  1 
ATOM   9792  C C   . VAL E  1 289 ? -12.015 16.608  49.658  1.00 12.57  ? 302 VAL E C   1 
ATOM   9793  O O   . VAL E  1 289 ? -11.266 17.468  49.184  1.00 12.67  ? 302 VAL E O   1 
ATOM   9794  C CB  . VAL E  1 289 ? -11.997 16.271  52.168  1.00 12.92  ? 302 VAL E CB  1 
ATOM   9795  C CG1 . VAL E  1 289 ? -11.571 15.355  53.321  1.00 12.54  ? 302 VAL E CG1 1 
ATOM   9796  C CG2 . VAL E  1 289 ? -11.497 17.703  52.385  1.00 11.82  ? 302 VAL E CG2 1 
ATOM   9797  N N   . GLY E  1 290 ? -13.260 16.413  49.226  1.00 12.15  ? 303 GLY E N   1 
ATOM   9798  C CA  . GLY E  1 290 ? -13.826 17.195  48.125  1.00 11.69  ? 303 GLY E CA  1 
ATOM   9799  C C   . GLY E  1 290 ? -13.655 16.541  46.764  1.00 12.21  ? 303 GLY E C   1 
ATOM   9800  O O   . GLY E  1 290 ? -13.505 15.315  46.668  1.00 13.01  ? 303 GLY E O   1 
ATOM   9801  N N   . LYS E  1 291 ? -13.688 17.363  45.714  1.00 11.44  ? 304 LYS E N   1 
ATOM   9802  C CA  . LYS E  1 291 ? -13.558 16.884  44.338  1.00 11.56  ? 304 LYS E CA  1 
ATOM   9803  C C   . LYS E  1 291 ? -12.102 16.959  43.898  1.00 12.11  ? 304 LYS E C   1 
ATOM   9804  O O   . LYS E  1 291 ? -11.563 18.045  43.648  1.00 12.21  ? 304 LYS E O   1 
ATOM   9805  C CB  . LYS E  1 291 ? -14.443 17.684  43.380  1.00 11.92  ? 304 LYS E CB  1 
ATOM   9806  C CG  . LYS E  1 291 ? -15.927 17.370  43.453  1.00 11.96  ? 304 LYS E CG  1 
ATOM   9807  C CD  . LYS E  1 291 ? -16.716 18.522  44.044  1.00 16.87  ? 304 LYS E CD  1 
ATOM   9808  C CE  . LYS E  1 291 ? -18.187 18.415  43.676  1.00 18.97  ? 304 LYS E CE  1 
ATOM   9809  N NZ  . LYS E  1 291 ? -18.951 19.629  44.075  1.00 21.44  ? 304 LYS E NZ  1 
ATOM   9810  N N   . CYS E  1 292 ? -11.474 15.792  43.799  1.00 12.23  ? 305 CYS E N   1 
ATOM   9811  C CA  . CYS E  1 292 ? -10.030 15.709  43.631  1.00 12.08  ? 305 CYS E CA  1 
ATOM   9812  C C   . CYS E  1 292 ? -9.594  14.856  42.454  1.00 11.28  ? 305 CYS E C   1 
ATOM   9813  O O   . CYS E  1 292 ? -10.317 13.947  42.039  1.00 10.92  ? 305 CYS E O   1 
ATOM   9814  C CB  . CYS E  1 292 ? -9.401  15.139  44.901  1.00 12.29  ? 305 CYS E CB  1 
ATOM   9815  S SG  . CYS E  1 292 ? -9.599  16.189  46.327  1.00 16.46  ? 305 CYS E SG  1 
ATOM   9816  N N   . PRO E  1 293 ? -8.396  15.148  41.913  1.00 11.23  ? 306 PRO E N   1 
ATOM   9817  C CA  . PRO E  1 293 ? -7.721  14.171  41.072  1.00 10.96  ? 306 PRO E CA  1 
ATOM   9818  C C   . PRO E  1 293 ? -7.428  12.923  41.907  1.00 11.00  ? 306 PRO E C   1 
ATOM   9819  O O   . PRO E  1 293 ? -7.272  13.011  43.131  1.00 10.58  ? 306 PRO E O   1 
ATOM   9820  C CB  . PRO E  1 293 ? -6.409  14.873  40.697  1.00 11.27  ? 306 PRO E CB  1 
ATOM   9821  C CG  . PRO E  1 293 ? -6.677  16.323  40.874  1.00 10.39  ? 306 PRO E CG  1 
ATOM   9822  C CD  . PRO E  1 293 ? -7.638  16.411  42.012  1.00 11.19  ? 306 PRO E CD  1 
ATOM   9823  N N   . ARG E  1 294 ? -7.371  11.771  41.254  1.00 11.21  ? 307 ARG E N   1 
ATOM   9824  C CA  . ARG E  1 294 ? -7.118  10.521  41.950  1.00 11.58  ? 307 ARG E CA  1 
ATOM   9825  C C   . ARG E  1 294 ? -5.648  10.427  42.354  1.00 11.20  ? 307 ARG E C   1 
ATOM   9826  O O   . ARG E  1 294 ? -4.759  10.754  41.563  1.00 11.63  ? 307 ARG E O   1 
ATOM   9827  C CB  . ARG E  1 294 ? -7.558  9.341   41.080  1.00 11.66  ? 307 ARG E CB  1 
ATOM   9828  C CG  . ARG E  1 294 ? -9.071  9.147   41.098  1.00 17.27  ? 307 ARG E CG  1 
ATOM   9829  C CD  . ARG E  1 294 ? -9.665  8.849   39.724  1.00 26.66  ? 307 ARG E CD  1 
ATOM   9830  N NE  . ARG E  1 294 ? -9.505  9.944   38.765  1.00 34.30  ? 307 ARG E NE  1 
ATOM   9831  C CZ  . ARG E  1 294 ? -10.172 10.053  37.614  1.00 37.59  ? 307 ARG E CZ  1 
ATOM   9832  N NH1 . ARG E  1 294 ? -11.079 9.143   37.254  1.00 33.53  ? 307 ARG E NH1 1 
ATOM   9833  N NH2 . ARG E  1 294 ? -9.936  11.090  36.820  1.00 39.94  ? 307 ARG E NH2 1 
ATOM   9834  N N   . TYR E  1 295 ? -5.398  10.013  43.595  1.00 10.16  ? 308 TYR E N   1 
ATOM   9835  C CA  . TYR E  1 295 ? -4.033  9.867   44.072  1.00 9.23   ? 308 TYR E CA  1 
ATOM   9836  C C   . TYR E  1 295 ? -3.323  8.713   43.377  1.00 9.49   ? 308 TYR E C   1 
ATOM   9837  O O   . TYR E  1 295 ? -3.874  7.618   43.236  1.00 9.59   ? 308 TYR E O   1 
ATOM   9838  C CB  . TYR E  1 295 ? -3.963  9.691   45.594  1.00 8.71   ? 308 TYR E CB  1 
ATOM   9839  C CG  . TYR E  1 295 ? -2.537  9.611   46.106  1.00 8.41   ? 308 TYR E CG  1 
ATOM   9840  C CD1 . TYR E  1 295 ? -1.771  10.768  46.271  1.00 8.99   ? 308 TYR E CD1 1 
ATOM   9841  C CD2 . TYR E  1 295 ? -1.944  8.379   46.403  1.00 8.50   ? 308 TYR E CD2 1 
ATOM   9842  C CE1 . TYR E  1 295 ? -0.454  10.707  46.727  1.00 8.70   ? 308 TYR E CE1 1 
ATOM   9843  C CE2 . TYR E  1 295 ? -0.624  8.305   46.863  1.00 10.59  ? 308 TYR E CE2 1 
ATOM   9844  C CZ  . TYR E  1 295 ? 0.113   9.475   47.021  1.00 11.02  ? 308 TYR E CZ  1 
ATOM   9845  O OH  . TYR E  1 295 ? 1.412   9.420   47.471  1.00 7.55   ? 308 TYR E OH  1 
ATOM   9846  N N   . VAL E  1 296 ? -2.099  8.986   42.939  1.00 9.34   ? 309 VAL E N   1 
ATOM   9847  C CA  . VAL E  1 296 ? -1.210  7.976   42.386  1.00 9.44   ? 309 VAL E CA  1 
ATOM   9848  C C   . VAL E  1 296 ? 0.134   8.110   43.084  1.00 10.38  ? 309 VAL E C   1 
ATOM   9849  O O   . VAL E  1 296 ? 0.440   9.167   43.639  1.00 11.98  ? 309 VAL E O   1 
ATOM   9850  C CB  . VAL E  1 296 ? -1.044  8.127   40.855  1.00 9.60   ? 309 VAL E CB  1 
ATOM   9851  C CG1 . VAL E  1 296 ? -2.349  7.780   40.140  1.00 9.00   ? 309 VAL E CG1 1 
ATOM   9852  C CG2 . VAL E  1 296 ? -0.577  9.534   40.485  1.00 8.39   ? 309 VAL E CG2 1 
ATOM   9853  N N   . LYS E  1 297 ? 0.931   7.047   43.072  1.00 10.76  ? 310 LYS E N   1 
ATOM   9854  C CA  . LYS E  1 297 ? 2.234   7.079   43.737  1.00 11.19  ? 310 LYS E CA  1 
ATOM   9855  C C   . LYS E  1 297 ? 3.384   7.527   42.823  1.00 10.59  ? 310 LYS E C   1 
ATOM   9856  O O   . LYS E  1 297 ? 4.515   7.678   43.279  1.00 10.83  ? 310 LYS E O   1 
ATOM   9857  C CB  . LYS E  1 297 ? 2.539   5.736   44.417  1.00 11.34  ? 310 LYS E CB  1 
ATOM   9858  C CG  . LYS E  1 297 ? 2.631   4.560   43.475  1.00 14.48  ? 310 LYS E CG  1 
ATOM   9859  C CD  . LYS E  1 297 ? 2.589   3.246   44.230  1.00 21.29  ? 310 LYS E CD  1 
ATOM   9860  C CE  . LYS E  1 297 ? 2.496   2.078   43.258  1.00 23.81  ? 310 LYS E CE  1 
ATOM   9861  N NZ  . LYS E  1 297 ? 2.068   0.818   43.935  1.00 25.91  ? 310 LYS E NZ  1 
ATOM   9862  N N   . GLN E  1 298 ? 3.086   7.754   41.545  1.00 10.21  ? 311 GLN E N   1 
ATOM   9863  C CA  . GLN E  1 298 ? 4.074   8.270   40.599  1.00 9.65   ? 311 GLN E CA  1 
ATOM   9864  C C   . GLN E  1 298 ? 4.161   9.790   40.677  1.00 10.47  ? 311 GLN E C   1 
ATOM   9865  O O   . GLN E  1 298 ? 3.143   10.463  40.834  1.00 10.94  ? 311 GLN E O   1 
ATOM   9866  C CB  . GLN E  1 298 ? 3.730   7.861   39.166  1.00 8.77   ? 311 GLN E CB  1 
ATOM   9867  C CG  . GLN E  1 298 ? 3.757   6.366   38.903  1.00 6.40   ? 311 GLN E CG  1 
ATOM   9868  C CD  . GLN E  1 298 ? 2.379   5.734   38.950  1.00 2.86   ? 311 GLN E CD  1 
ATOM   9869  O OE1 . GLN E  1 298 ? 1.483   6.211   39.648  1.00 2.68   ? 311 GLN E OE1 1 
ATOM   9870  N NE2 . GLN E  1 298 ? 2.201   4.652   38.198  1.00 2.00   ? 311 GLN E NE2 1 
ATOM   9871  N N   . LYS E  1 299 ? 5.377   10.321  40.557  1.00 10.64  ? 312 LYS E N   1 
ATOM   9872  C CA  . LYS E  1 299 ? 5.605   11.769  40.541  1.00 11.25  ? 312 LYS E CA  1 
ATOM   9873  C C   . LYS E  1 299 ? 5.210   12.356  39.194  1.00 10.74  ? 312 LYS E C   1 
ATOM   9874  O O   . LYS E  1 299 ? 4.716   13.484  39.119  1.00 11.33  ? 312 LYS E O   1 
ATOM   9875  C CB  . LYS E  1 299 ? 7.078   12.092  40.805  1.00 11.49  ? 312 LYS E CB  1 
ATOM   9876  C CG  . LYS E  1 299 ? 7.624   11.536  42.101  1.00 17.11  ? 312 LYS E CG  1 
ATOM   9877  C CD  . LYS E  1 299 ? 9.132   11.295  42.004  1.00 24.36  ? 312 LYS E CD  1 
ATOM   9878  C CE  . LYS E  1 299 ? 9.641   10.502  43.207  1.00 27.44  ? 312 LYS E CE  1 
ATOM   9879  N NZ  . LYS E  1 299 ? 9.344   11.175  44.510  1.00 28.32  ? 312 LYS E NZ  1 
ATOM   9880  N N   . SER E  1 300 ? 5.438   11.583  38.135  1.00 9.62   ? 313 SER E N   1 
ATOM   9881  C CA  . SER E  1 300 ? 5.238   12.049  36.770  1.00 9.54   ? 313 SER E CA  1 
ATOM   9882  C C   . SER E  1 300 ? 4.788   10.929  35.840  1.00 8.96   ? 313 SER E C   1 
ATOM   9883  O O   . SER E  1 300 ? 5.355   9.834   35.843  1.00 9.41   ? 313 SER E O   1 
ATOM   9884  C CB  . SER E  1 300 ? 6.529   12.674  36.231  1.00 9.87   ? 313 SER E CB  1 
ATOM   9885  O OG  . SER E  1 300 ? 6.405   12.989  34.854  1.00 10.04  ? 313 SER E OG  1 
ATOM   9886  N N   . LEU E  1 301 ? 3.763   11.217  35.048  1.00 7.86   ? 314 LEU E N   1 
ATOM   9887  C CA  . LEU E  1 301 ? 3.323   10.326  33.983  1.00 7.68   ? 314 LEU E CA  1 
ATOM   9888  C C   . LEU E  1 301 ? 3.030   11.191  32.767  1.00 7.68   ? 314 LEU E C   1 
ATOM   9889  O O   . LEU E  1 301 ? 1.963   11.803  32.672  1.00 8.23   ? 314 LEU E O   1 
ATOM   9890  C CB  . LEU E  1 301 ? 2.087   9.519   34.405  1.00 7.02   ? 314 LEU E CB  1 
ATOM   9891  C CG  . LEU E  1 301 ? 2.288   8.367   35.401  1.00 6.08   ? 314 LEU E CG  1 
ATOM   9892  C CD1 . LEU E  1 301 ? 0.984   8.020   36.095  1.00 2.85   ? 314 LEU E CD1 1 
ATOM   9893  C CD2 . LEU E  1 301 ? 2.892   7.127   34.738  1.00 2.00   ? 314 LEU E CD2 1 
ATOM   9894  N N   . LEU E  1 302 ? 3.993   11.261  31.853  1.00 6.63   ? 315 LEU E N   1 
ATOM   9895  C CA  . LEU E  1 302 ? 3.904   12.179  30.725  1.00 6.06   ? 315 LEU E CA  1 
ATOM   9896  C C   . LEU E  1 302 ? 3.106   11.599  29.565  1.00 6.09   ? 315 LEU E C   1 
ATOM   9897  O O   . LEU E  1 302 ? 3.424   10.518  29.055  1.00 5.04   ? 315 LEU E O   1 
ATOM   9898  C CB  . LEU E  1 302 ? 5.298   12.595  30.251  1.00 6.02   ? 315 LEU E CB  1 
ATOM   9899  C CG  . LEU E  1 302 ? 6.131   13.501  31.160  1.00 7.04   ? 315 LEU E CG  1 
ATOM   9900  C CD1 . LEU E  1 302 ? 7.580   13.512  30.695  1.00 9.61   ? 315 LEU E CD1 1 
ATOM   9901  C CD2 . LEU E  1 302 ? 5.567   14.913  31.199  1.00 7.79   ? 315 LEU E CD2 1 
ATOM   9902  N N   . LEU E  1 303 ? 2.072   12.330  29.156  1.00 6.11   ? 316 LEU E N   1 
ATOM   9903  C CA  . LEU E  1 303 ? 1.248   11.945  28.016  1.00 6.03   ? 316 LEU E CA  1 
ATOM   9904  C C   . LEU E  1 303 ? 1.768   12.609  26.760  1.00 5.69   ? 316 LEU E C   1 
ATOM   9905  O O   . LEU E  1 303 ? 1.874   13.832  26.703  1.00 7.09   ? 316 LEU E O   1 
ATOM   9906  C CB  . LEU E  1 303 ? -0.208  12.354  28.239  1.00 6.15   ? 316 LEU E CB  1 
ATOM   9907  C CG  . LEU E  1 303 ? -1.218  11.985  27.152  1.00 5.38   ? 316 LEU E CG  1 
ATOM   9908  C CD1 . LEU E  1 303 ? -1.584  10.529  27.260  1.00 3.93   ? 316 LEU E CD1 1 
ATOM   9909  C CD2 . LEU E  1 303 ? -2.462  12.842  27.266  1.00 9.56   ? 316 LEU E CD2 1 
ATOM   9910  N N   . ALA E  1 304 ? 2.082   11.798  25.755  1.00 4.69   ? 317 ALA E N   1 
ATOM   9911  C CA  . ALA E  1 304 ? 2.556   12.302  24.473  1.00 3.87   ? 317 ALA E CA  1 
ATOM   9912  C C   . ALA E  1 304 ? 1.485   13.141  23.790  1.00 3.64   ? 317 ALA E C   1 
ATOM   9913  O O   . ALA E  1 304 ? 0.307   12.779  23.783  1.00 3.48   ? 317 ALA E O   1 
ATOM   9914  C CB  . ALA E  1 304 ? 2.973   11.149  23.574  1.00 3.66   ? 317 ALA E CB  1 
ATOM   9915  N N   . THR E  1 305 ? 1.901   14.272  23.232  1.00 3.36   ? 318 THR E N   1 
ATOM   9916  C CA  . THR E  1 305 ? 1.013   15.109  22.432  1.00 2.64   ? 318 THR E CA  1 
ATOM   9917  C C   . THR E  1 305 ? 1.674   15.446  21.104  1.00 3.07   ? 318 THR E C   1 
ATOM   9918  O O   . THR E  1 305 ? 1.399   16.492  20.504  1.00 3.99   ? 318 THR E O   1 
ATOM   9919  C CB  . THR E  1 305 ? 0.652   16.414  23.146  1.00 2.55   ? 318 THR E CB  1 
ATOM   9920  O OG1 . THR E  1 305 ? 1.854   17.115  23.489  1.00 2.10   ? 318 THR E OG1 1 
ATOM   9921  C CG2 . THR E  1 305 ? -0.177  16.139  24.397  1.00 2.00   ? 318 THR E CG2 1 
ATOM   9922  N N   . GLY E  1 306 ? 2.550   14.553  20.655  1.00 2.33   ? 319 GLY E N   1 
ATOM   9923  C CA  . GLY E  1 306 ? 3.238   14.718  19.387  1.00 2.30   ? 319 GLY E CA  1 
ATOM   9924  C C   . GLY E  1 306 ? 3.769   13.403  18.870  1.00 2.23   ? 319 GLY E C   1 
ATOM   9925  O O   . GLY E  1 306 ? 3.751   12.399  19.570  1.00 2.38   ? 319 GLY E O   1 
ATOM   9926  N N   . MET E  1 307 ? 4.255   13.415  17.638  1.00 2.82   ? 320 MET E N   1 
ATOM   9927  C CA  . MET E  1 307 ? 4.796   12.213  17.016  1.00 3.87   ? 320 MET E CA  1 
ATOM   9928  C C   . MET E  1 307 ? 6.138   11.819  17.617  1.00 5.19   ? 320 MET E C   1 
ATOM   9929  O O   . MET E  1 307 ? 6.741   12.575  18.383  1.00 6.23   ? 320 MET E O   1 
ATOM   9930  C CB  . MET E  1 307 ? 4.966   12.424  15.509  1.00 3.35   ? 320 MET E CB  1 
ATOM   9931  C CG  . MET E  1 307 ? 5.988   13.490  15.144  1.00 2.56   ? 320 MET E CG  1 
ATOM   9932  S SD  . MET E  1 307 ? 6.112   13.794  13.379  1.00 2.27   ? 320 MET E SD  1 
ATOM   9933  C CE  . MET E  1 307 ? 4.492   14.468  13.003  1.00 2.28   ? 320 MET E CE  1 
ATOM   9934  N N   . ARG E  1 308 ? 6.588   10.625  17.252  1.00 5.94   ? 321 ARG E N   1 
ATOM   9935  C CA  . ARG E  1 308 ? 7.948   10.186  17.495  1.00 6.97   ? 321 ARG E CA  1 
ATOM   9936  C C   . ARG E  1 308 ? 8.916   11.247  16.966  1.00 7.40   ? 321 ARG E C   1 
ATOM   9937  O O   . ARG E  1 308 ? 8.811   11.669  15.812  1.00 7.23   ? 321 ARG E O   1 
ATOM   9938  C CB  . ARG E  1 308 ? 8.172   8.847   16.789  1.00 7.08   ? 321 ARG E CB  1 
ATOM   9939  C CG  . ARG E  1 308 ? 9.572   8.292   16.868  1.00 9.47   ? 321 ARG E CG  1 
ATOM   9940  C CD  . ARG E  1 308 ? 9.849   7.672   18.215  1.00 15.10  ? 321 ARG E CD  1 
ATOM   9941  N NE  . ARG E  1 308 ? 11.007  6.785   18.152  1.00 23.43  ? 321 ARG E NE  1 
ATOM   9942  C CZ  . ARG E  1 308 ? 12.261  7.162   18.385  1.00 27.74  ? 321 ARG E CZ  1 
ATOM   9943  N NH1 . ARG E  1 308 ? 12.539  8.421   18.707  1.00 29.42  ? 321 ARG E NH1 1 
ATOM   9944  N NH2 . ARG E  1 308 ? 13.241  6.275   18.296  1.00 31.05  ? 321 ARG E NH2 1 
ATOM   9945  N N   . ASN E  1 309 ? 9.838   11.683  17.822  1.00 8.01   ? 322 ASN E N   1 
ATOM   9946  C CA  . ASN E  1 309 ? 10.808  12.714  17.461  1.00 8.37   ? 322 ASN E CA  1 
ATOM   9947  C C   . ASN E  1 309 ? 12.126  12.124  16.976  1.00 9.28   ? 322 ASN E C   1 
ATOM   9948  O O   . ASN E  1 309 ? 12.809  11.412  17.714  1.00 9.34   ? 322 ASN E O   1 
ATOM   9949  C CB  . ASN E  1 309 ? 11.058  13.666  18.636  1.00 7.71   ? 322 ASN E CB  1 
ATOM   9950  C CG  . ASN E  1 309 ? 11.959  14.828  18.262  1.00 7.03   ? 322 ASN E CG  1 
ATOM   9951  O OD1 . ASN E  1 309 ? 11.596  15.658  17.429  1.00 8.56   ? 322 ASN E OD1 1 
ATOM   9952  N ND2 . ASN E  1 309 ? 13.140  14.891  18.872  1.00 2.28   ? 322 ASN E ND2 1 
ATOM   9953  N N   . VAL E  1 310 ? 12.472  12.425  15.728  1.00 10.53  ? 323 VAL E N   1 
ATOM   9954  C CA  . VAL E  1 310 ? 13.701  11.919  15.125  1.00 11.92  ? 323 VAL E CA  1 
ATOM   9955  C C   . VAL E  1 310 ? 14.511  13.090  14.557  1.00 12.74  ? 323 VAL E C   1 
ATOM   9956  O O   . VAL E  1 310 ? 14.270  13.527  13.427  1.00 12.53  ? 323 VAL E O   1 
ATOM   9957  C CB  . VAL E  1 310 ? 13.414  10.859  14.021  1.00 12.15  ? 323 VAL E CB  1 
ATOM   9958  C CG1 . VAL E  1 310 ? 14.706  10.182  13.572  1.00 12.44  ? 323 VAL E CG1 1 
ATOM   9959  C CG2 . VAL E  1 310 ? 12.415  9.809   14.510  1.00 11.88  ? 323 VAL E CG2 1 
ATOM   9960  N N   . PRO E  1 311 ? 15.479  13.601  15.343  1.00 13.83  ? 324 PRO E N   1 
ATOM   9961  C CA  . PRO E  1 311 ? 16.231  14.813  14.997  1.00 14.68  ? 324 PRO E CA  1 
ATOM   9962  C C   . PRO E  1 311 ? 17.077  14.664  13.737  1.00 15.90  ? 324 PRO E C   1 
ATOM   9963  O O   . PRO E  1 311 ? 17.314  13.544  13.273  1.00 16.07  ? 324 PRO E O   1 
ATOM   9964  C CB  . PRO E  1 311 ? 17.139  15.031  16.217  1.00 14.42  ? 324 PRO E CB  1 
ATOM   9965  C CG  . PRO E  1 311 ? 16.552  14.204  17.306  1.00 13.74  ? 324 PRO E CG  1 
ATOM   9966  C CD  . PRO E  1 311 ? 15.932  13.031  16.625  1.00 14.01  ? 324 PRO E CD  1 
ATOM   9967  N N   . GLU E  1 312 ? 17.520  15.796  13.193  1.00 17.13  ? 325 GLU E N   1 
ATOM   9968  C CA  . GLU E  1 312 ? 18.368  15.813  12.005  1.00 17.95  ? 325 GLU E CA  1 
ATOM   9969  C C   . GLU E  1 312 ? 19.804  15.443  12.362  1.00 17.80  ? 325 GLU E C   1 
ATOM   9970  O O   . GLU E  1 312 ? 20.523  14.862  11.549  1.00 17.94  ? 325 GLU E O   1 
ATOM   9971  C CB  . GLU E  1 312 ? 18.326  17.188  11.328  1.00 18.28  ? 325 GLU E CB  1 
ATOM   9972  C CG  . GLU E  1 312 ? 17.012  17.505  10.608  1.00 19.90  ? 325 GLU E CG  1 
ATOM   9973  C CD  . GLU E  1 312 ? 17.044  18.837  9.861   1.00 23.41  ? 325 GLU E CD  1 
ATOM   9974  O OE1 . GLU E  1 312 ? 17.572  19.829  10.411  1.00 25.27  ? 325 GLU E OE1 1 
ATOM   9975  O OE2 . GLU E  1 312 ? 16.534  18.895  8.720   1.00 24.22  ? 325 GLU E OE2 1 
ATOM   9976  N N   . GLY F  2 1   ? 6.854   2.545   15.465  1.00 13.00  ? 1   GLY F N   1 
ATOM   9977  C CA  . GLY F  2 1   ? 5.738   2.937   14.561  1.00 12.67  ? 1   GLY F CA  1 
ATOM   9978  C C   . GLY F  2 1   ? 5.171   1.771   13.775  1.00 12.26  ? 1   GLY F C   1 
ATOM   9979  O O   . GLY F  2 1   ? 5.844   1.220   12.907  1.00 11.68  ? 1   GLY F O   1 
ATOM   9980  N N   . LEU F  2 2   ? 3.922   1.411   14.076  1.00 12.05  ? 2   LEU F N   1 
ATOM   9981  C CA  . LEU F  2 2   ? 3.200   0.330   13.383  1.00 11.07  ? 2   LEU F CA  1 
ATOM   9982  C C   . LEU F  2 2   ? 3.140   0.466   11.859  1.00 11.41  ? 2   LEU F C   1 
ATOM   9983  O O   . LEU F  2 2   ? 3.007   -0.534  11.157  1.00 11.50  ? 2   LEU F O   1 
ATOM   9984  C CB  . LEU F  2 2   ? 1.767   0.212   13.913  1.00 9.81   ? 2   LEU F CB  1 
ATOM   9985  C CG  . LEU F  2 2   ? 1.465   -0.552  15.204  1.00 8.80   ? 2   LEU F CG  1 
ATOM   9986  C CD1 . LEU F  2 2   ? -0.012  -0.408  15.579  1.00 6.05   ? 2   LEU F CD1 1 
ATOM   9987  C CD2 . LEU F  2 2   ? 1.839   -2.017  15.091  1.00 4.24   ? 2   LEU F CD2 1 
ATOM   9988  N N   . PHE F  2 3   ? 3.226   1.695   11.353  1.00 11.85  ? 3   PHE F N   1 
ATOM   9989  C CA  . PHE F  2 3   ? 3.046   1.951   9.921   1.00 12.43  ? 3   PHE F CA  1 
ATOM   9990  C C   . PHE F  2 3   ? 4.356   2.170   9.162   1.00 12.89  ? 3   PHE F C   1 
ATOM   9991  O O   . PHE F  2 3   ? 4.351   2.350   7.942   1.00 12.93  ? 3   PHE F O   1 
ATOM   9992  C CB  . PHE F  2 3   ? 2.035   3.083   9.698   1.00 12.50  ? 3   PHE F CB  1 
ATOM   9993  C CG  . PHE F  2 3   ? 0.642   2.726   10.137  1.00 12.66  ? 3   PHE F CG  1 
ATOM   9994  C CD1 . PHE F  2 3   ? 0.222   2.982   11.437  1.00 13.17  ? 3   PHE F CD1 1 
ATOM   9995  C CD2 . PHE F  2 3   ? -0.235  2.092   9.262   1.00 12.07  ? 3   PHE F CD2 1 
ATOM   9996  C CE1 . PHE F  2 3   ? -1.059  2.629   11.851  1.00 13.96  ? 3   PHE F CE1 1 
ATOM   9997  C CE2 . PHE F  2 3   ? -1.512  1.735   9.667   1.00 8.41   ? 3   PHE F CE2 1 
ATOM   9998  C CZ  . PHE F  2 3   ? -1.926  2.006   10.961  1.00 11.71  ? 3   PHE F CZ  1 
ATOM   9999  N N   . GLY F  2 4   ? 5.466   2.160   9.901   1.00 13.11  ? 4   GLY F N   1 
ATOM   10000 C CA  . GLY F  2 4   ? 6.810   2.110   9.322   1.00 12.62  ? 4   GLY F CA  1 
ATOM   10001 C C   . GLY F  2 4   ? 7.289   3.295   8.503   1.00 12.26  ? 4   GLY F C   1 
ATOM   10002 O O   . GLY F  2 4   ? 8.276   3.179   7.771   1.00 12.20  ? 4   GLY F O   1 
ATOM   10003 N N   . ALA F  2 5   ? 6.600   4.430   8.625   1.00 11.41  ? 5   ALA F N   1 
ATOM   10004 C CA  . ALA F  2 5   ? 6.989   5.648   7.917   1.00 9.95   ? 5   ALA F CA  1 
ATOM   10005 C C   . ALA F  2 5   ? 7.874   6.536   8.790   1.00 9.46   ? 5   ALA F C   1 
ATOM   10006 O O   . ALA F  2 5   ? 9.056   6.718   8.484   1.00 9.60   ? 5   ALA F O   1 
ATOM   10007 C CB  . ALA F  2 5   ? 5.764   6.405   7.429   1.00 10.23  ? 5   ALA F CB  1 
ATOM   10008 N N   . ILE F  2 6   ? 7.304   7.080   9.868   1.00 8.05   ? 6   ILE F N   1 
ATOM   10009 C CA  . ILE F  2 6   ? 8.059   7.876   10.839  1.00 7.66   ? 6   ILE F CA  1 
ATOM   10010 C C   . ILE F  2 6   ? 8.964   6.937   11.630  1.00 7.95   ? 6   ILE F C   1 
ATOM   10011 O O   . ILE F  2 6   ? 8.492   5.938   12.184  1.00 9.10   ? 6   ILE F O   1 
ATOM   10012 C CB  . ILE F  2 6   ? 7.130   8.674   11.798  1.00 7.85   ? 6   ILE F CB  1 
ATOM   10013 C CG1 . ILE F  2 6   ? 6.244   9.651   11.018  1.00 7.55   ? 6   ILE F CG1 1 
ATOM   10014 C CG2 . ILE F  2 6   ? 7.945   9.443   12.838  1.00 8.13   ? 6   ILE F CG2 1 
ATOM   10015 C CD1 . ILE F  2 6   ? 5.193   10.354  11.869  1.00 5.62   ? 6   ILE F CD1 1 
ATOM   10016 N N   . ALA F  2 7   ? 10.260  7.259   11.672  1.00 7.76   ? 7   ALA F N   1 
ATOM   10017 C CA  . ALA F  2 7   ? 11.289  6.374   12.240  1.00 7.55   ? 7   ALA F CA  1 
ATOM   10018 C C   . ALA F  2 7   ? 11.284  5.014   11.534  1.00 7.71   ? 7   ALA F C   1 
ATOM   10019 O O   . ALA F  2 7   ? 11.497  3.970   12.154  1.00 8.00   ? 7   ALA F O   1 
ATOM   10020 C CB  . ALA F  2 7   ? 11.116  6.217   13.759  1.00 6.52   ? 7   ALA F CB  1 
ATOM   10021 N N   . GLY F  2 8   ? 11.021  5.052   10.230  1.00 7.66   ? 8   GLY F N   1 
ATOM   10022 C CA  . GLY F  2 8   ? 10.983  3.866   9.386   1.00 8.09   ? 8   GLY F CA  1 
ATOM   10023 C C   . GLY F  2 8   ? 11.729  4.132   8.095   1.00 8.86   ? 8   GLY F C   1 
ATOM   10024 O O   . GLY F  2 8   ? 12.946  4.344   8.113   1.00 8.83   ? 8   GLY F O   1 
ATOM   10025 N N   . PHE F  2 9   ? 11.010  4.136   6.972   1.00 9.15   ? 9   PHE F N   1 
ATOM   10026 C CA  . PHE F  2 9   ? 11.648  4.417   5.686   1.00 9.36   ? 9   PHE F CA  1 
ATOM   10027 C C   . PHE F  2 9   ? 11.962  5.906   5.504   1.00 9.95   ? 9   PHE F C   1 
ATOM   10028 O O   . PHE F  2 9   ? 12.779  6.268   4.664   1.00 10.37  ? 9   PHE F O   1 
ATOM   10029 C CB  . PHE F  2 9   ? 10.889  3.802   4.491   1.00 8.79   ? 9   PHE F CB  1 
ATOM   10030 C CG  . PHE F  2 9   ? 9.519   4.379   4.251   1.00 8.68   ? 9   PHE F CG  1 
ATOM   10031 C CD1 . PHE F  2 9   ? 9.346   5.488   3.422   1.00 7.12   ? 9   PHE F CD1 1 
ATOM   10032 C CD2 . PHE F  2 9   ? 8.393   3.786   4.809   1.00 6.89   ? 9   PHE F CD2 1 
ATOM   10033 C CE1 . PHE F  2 9   ? 8.078   6.017   3.183   1.00 3.16   ? 9   PHE F CE1 1 
ATOM   10034 C CE2 . PHE F  2 9   ? 7.118   4.310   4.574   1.00 5.52   ? 9   PHE F CE2 1 
ATOM   10035 C CZ  . PHE F  2 9   ? 6.966   5.430   3.761   1.00 3.23   ? 9   PHE F CZ  1 
ATOM   10036 N N   . ILE F  2 10  ? 11.325  6.757   6.306   1.00 11.14  ? 10  ILE F N   1 
ATOM   10037 C CA  . ILE F  2 10  ? 11.743  8.153   6.436   1.00 12.36  ? 10  ILE F CA  1 
ATOM   10038 C C   . ILE F  2 10  ? 12.793  8.238   7.548   1.00 13.83  ? 10  ILE F C   1 
ATOM   10039 O O   . ILE F  2 10  ? 12.477  8.087   8.731   1.00 13.81  ? 10  ILE F O   1 
ATOM   10040 C CB  . ILE F  2 10  ? 10.550  9.117   6.688   1.00 12.14  ? 10  ILE F CB  1 
ATOM   10041 C CG1 . ILE F  2 10  ? 9.573   9.072   5.508   1.00 10.89  ? 10  ILE F CG1 1 
ATOM   10042 C CG2 . ILE F  2 10  ? 11.043  10.546  6.901   1.00 11.87  ? 10  ILE F CG2 1 
ATOM   10043 C CD1 . ILE F  2 10  ? 8.258   9.758   5.761   1.00 9.54   ? 10  ILE F CD1 1 
ATOM   10044 N N   . GLU F  2 11  ? 14.041  8.470   7.139   1.00 15.91  ? 11  GLU F N   1 
ATOM   10045 C CA  . GLU F  2 11  ? 15.215  8.414   8.019   1.00 17.90  ? 11  GLU F CA  1 
ATOM   10046 C C   . GLU F  2 11  ? 15.093  9.302   9.257   1.00 17.68  ? 11  GLU F C   1 
ATOM   10047 O O   . GLU F  2 11  ? 15.426  8.877   10.368  1.00 17.89  ? 11  GLU F O   1 
ATOM   10048 C CB  . GLU F  2 11  ? 16.480  8.800   7.244   1.00 18.75  ? 11  GLU F CB  1 
ATOM   10049 C CG  . GLU F  2 11  ? 16.623  8.148   5.866   1.00 25.83  ? 11  GLU F CG  1 
ATOM   10050 C CD  . GLU F  2 11  ? 17.510  6.904   5.866   1.00 32.77  ? 11  GLU F CD  1 
ATOM   10051 O OE1 . GLU F  2 11  ? 17.578  6.203   6.905   1.00 34.07  ? 11  GLU F OE1 1 
ATOM   10052 O OE2 . GLU F  2 11  ? 18.135  6.628   4.814   1.00 31.97  ? 11  GLU F OE2 1 
ATOM   10053 N N   . ASN F  2 12  ? 14.620  10.532  9.051   1.00 17.28  ? 12  ASN F N   1 
ATOM   10054 C CA  . ASN F  2 12  ? 14.497  11.525  10.118  1.00 16.63  ? 12  ASN F CA  1 
ATOM   10055 C C   . ASN F  2 12  ? 13.480  12.624  9.808   1.00 16.41  ? 12  ASN F C   1 
ATOM   10056 O O   . ASN F  2 12  ? 13.032  12.767  8.666   1.00 16.23  ? 12  ASN F O   1 
ATOM   10057 C CB  . ASN F  2 12  ? 15.865  12.147  10.432  1.00 16.60  ? 12  ASN F CB  1 
ATOM   10058 C CG  . ASN F  2 12  ? 16.541  12.728  9.205   1.00 15.19  ? 12  ASN F CG  1 
ATOM   10059 O OD1 . ASN F  2 12  ? 17.480  12.141  8.666   1.00 14.27  ? 12  ASN F OD1 1 
ATOM   10060 N ND2 . ASN F  2 12  ? 16.065  13.886  8.754   1.00 12.53  ? 12  ASN F ND2 1 
ATOM   10061 N N   . GLY F  2 13  ? 13.126  13.397  10.834  1.00 16.01  ? 13  GLY F N   1 
ATOM   10062 C CA  . GLY F  2 13  ? 12.222  14.533  10.680  1.00 15.16  ? 13  GLY F CA  1 
ATOM   10063 C C   . GLY F  2 13  ? 12.942  15.763  10.163  1.00 14.94  ? 13  GLY F C   1 
ATOM   10064 O O   . GLY F  2 13  ? 14.156  15.743  9.959   1.00 14.79  ? 13  GLY F O   1 
ATOM   10065 N N   . TRP F  2 14  ? 12.188  16.836  9.944   1.00 14.92  ? 14  TRP F N   1 
ATOM   10066 C CA  . TRP F  2 14  ? 12.756  18.096  9.476   1.00 15.00  ? 14  TRP F CA  1 
ATOM   10067 C C   . TRP F  2 14  ? 12.608  19.177  10.541  1.00 16.27  ? 14  TRP F C   1 
ATOM   10068 O O   . TRP F  2 14  ? 11.494  19.631  10.824  1.00 16.56  ? 14  TRP F O   1 
ATOM   10069 C CB  . TRP F  2 14  ? 12.077  18.557  8.185   1.00 14.42  ? 14  TRP F CB  1 
ATOM   10070 C CG  . TRP F  2 14  ? 12.252  17.652  6.995   1.00 12.80  ? 14  TRP F CG  1 
ATOM   10071 C CD1 . TRP F  2 14  ? 13.371  16.944  6.648   1.00 12.03  ? 14  TRP F CD1 1 
ATOM   10072 C CD2 . TRP F  2 14  ? 11.285  17.399  5.971   1.00 11.05  ? 14  TRP F CD2 1 
ATOM   10073 N NE1 . TRP F  2 14  ? 13.151  16.252  5.481   1.00 10.63  ? 14  TRP F NE1 1 
ATOM   10074 C CE2 . TRP F  2 14  ? 11.879  16.513  5.044   1.00 10.54  ? 14  TRP F CE2 1 
ATOM   10075 C CE3 . TRP F  2 14  ? 9.968   17.827  5.751   1.00 10.45  ? 14  TRP F CE3 1 
ATOM   10076 C CZ2 . TRP F  2 14  ? 11.201  16.044  3.918   1.00 11.78  ? 14  TRP F CZ2 1 
ATOM   10077 C CZ3 . TRP F  2 14  ? 9.295   17.363  4.628   1.00 7.27   ? 14  TRP F CZ3 1 
ATOM   10078 C CH2 . TRP F  2 14  ? 9.914   16.481  3.727   1.00 10.34  ? 14  TRP F CH2 1 
ATOM   10079 N N   . GLU F  2 15  ? 13.732  19.585  11.128  1.00 16.87  ? 15  GLU F N   1 
ATOM   10080 C CA  . GLU F  2 15  ? 13.729  20.627  12.154  1.00 17.61  ? 15  GLU F CA  1 
ATOM   10081 C C   . GLU F  2 15  ? 13.393  22.000  11.564  1.00 18.54  ? 15  GLU F C   1 
ATOM   10082 O O   . GLU F  2 15  ? 12.928  22.893  12.273  1.00 19.05  ? 15  GLU F O   1 
ATOM   10083 C CB  . GLU F  2 15  ? 15.065  20.658  12.905  1.00 17.41  ? 15  GLU F CB  1 
ATOM   10084 C CG  . GLU F  2 15  ? 15.310  19.439  13.799  1.00 17.20  ? 15  GLU F CG  1 
ATOM   10085 C CD  . GLU F  2 15  ? 16.651  19.479  14.529  1.00 18.89  ? 15  GLU F CD  1 
ATOM   10086 O OE1 . GLU F  2 15  ? 17.131  20.583  14.869  1.00 19.58  ? 15  GLU F OE1 1 
ATOM   10087 O OE2 . GLU F  2 15  ? 17.224  18.396  14.773  1.00 19.26  ? 15  GLU F OE2 1 
ATOM   10088 N N   . GLY F  2 16  ? 13.623  22.152  10.261  1.00 19.43  ? 16  GLY F N   1 
ATOM   10089 C CA  . GLY F  2 16  ? 13.278  23.374  9.540   1.00 20.16  ? 16  GLY F CA  1 
ATOM   10090 C C   . GLY F  2 16  ? 11.791  23.508  9.247   1.00 20.77  ? 16  GLY F C   1 
ATOM   10091 O O   . GLY F  2 16  ? 11.313  24.605  8.951   1.00 20.79  ? 16  GLY F O   1 
ATOM   10092 N N   . LEU F  2 17  ? 11.060  22.395  9.322   1.00 21.29  ? 17  LEU F N   1 
ATOM   10093 C CA  . LEU F  2 17  ? 9.611   22.399  9.111   1.00 21.45  ? 17  LEU F CA  1 
ATOM   10094 C C   . LEU F  2 17  ? 8.888   22.925  10.351  1.00 22.25  ? 17  LEU F C   1 
ATOM   10095 O O   . LEU F  2 17  ? 8.282   22.165  11.110  1.00 22.68  ? 17  LEU F O   1 
ATOM   10096 C CB  . LEU F  2 17  ? 9.104   21.001  8.727   1.00 21.21  ? 17  LEU F CB  1 
ATOM   10097 C CG  . LEU F  2 17  ? 7.627   20.843  8.334   1.00 21.39  ? 17  LEU F CG  1 
ATOM   10098 C CD1 . LEU F  2 17  ? 7.335   21.452  6.969   1.00 20.39  ? 17  LEU F CD1 1 
ATOM   10099 C CD2 . LEU F  2 17  ? 7.209   19.378  8.358   1.00 20.90  ? 17  LEU F CD2 1 
ATOM   10100 N N   . ILE F  2 18  ? 8.972   24.237  10.554  1.00 23.06  ? 18  ILE F N   1 
ATOM   10101 C CA  . ILE F  2 18  ? 8.265   24.906  11.648  1.00 22.95  ? 18  ILE F CA  1 
ATOM   10102 C C   . ILE F  2 18  ? 6.811   25.204  11.253  1.00 23.07  ? 18  ILE F C   1 
ATOM   10103 O O   . ILE F  2 18  ? 5.992   25.593  12.091  1.00 22.75  ? 18  ILE F O   1 
ATOM   10104 C CB  . ILE F  2 18  ? 9.001   26.200  12.108  1.00 22.88  ? 18  ILE F CB  1 
ATOM   10105 C CG1 . ILE F  2 18  ? 9.244   27.153  10.925  1.00 22.81  ? 18  ILE F CG1 1 
ATOM   10106 C CG2 . ILE F  2 18  ? 10.314  25.842  12.818  1.00 22.64  ? 18  ILE F CG2 1 
ATOM   10107 C CD1 . ILE F  2 18  ? 9.640   28.580  11.323  1.00 21.03  ? 18  ILE F CD1 1 
ATOM   10108 N N   . ASN F  2 19  ? 6.511   24.991  9.970   1.00 22.95  ? 19  ASN F N   1 
ATOM   10109 C CA  . ASN F  2 19  ? 5.206   25.286  9.375   1.00 22.12  ? 19  ASN F CA  1 
ATOM   10110 C C   . ASN F  2 19  ? 4.072   24.420  9.954   1.00 21.80  ? 19  ASN F C   1 
ATOM   10111 O O   . ASN F  2 19  ? 3.040   24.946  10.371  1.00 22.15  ? 19  ASN F O   1 
ATOM   10112 C CB  . ASN F  2 19  ? 5.264   25.144  7.837   1.00 21.81  ? 19  ASN F CB  1 
ATOM   10113 C CG  . ASN F  2 19  ? 6.546   25.728  7.216   1.00 21.13  ? 19  ASN F CG  1 
ATOM   10114 O OD1 . ASN F  2 19  ? 7.167   25.110  6.341   1.00 12.15  ? 19  ASN F OD1 1 
ATOM   10115 N ND2 . ASN F  2 19  ? 6.934   26.922  7.658   1.00 22.36  ? 19  ASN F ND2 1 
ATOM   10116 N N   . GLY F  2 20  ? 4.278   23.101  9.982   1.00 20.82  ? 20  GLY F N   1 
ATOM   10117 C CA  . GLY F  2 20  ? 3.269   22.144  10.455  1.00 19.01  ? 20  GLY F CA  1 
ATOM   10118 C C   . GLY F  2 20  ? 3.867   20.822  10.916  1.00 17.83  ? 20  GLY F C   1 
ATOM   10119 O O   . GLY F  2 20  ? 5.032   20.772  11.316  1.00 18.74  ? 20  GLY F O   1 
ATOM   10120 N N   . TRP F  2 21  ? 3.070   19.753  10.862  1.00 15.74  ? 21  TRP F N   1 
ATOM   10121 C CA  . TRP F  2 21  ? 3.513   18.420  11.292  1.00 14.08  ? 21  TRP F CA  1 
ATOM   10122 C C   . TRP F  2 21  ? 4.082   17.595  10.143  1.00 13.32  ? 21  TRP F C   1 
ATOM   10123 O O   . TRP F  2 21  ? 5.105   16.925  10.297  1.00 13.28  ? 21  TRP F O   1 
ATOM   10124 C CB  . TRP F  2 21  ? 2.365   17.652  11.958  1.00 14.03  ? 21  TRP F CB  1 
ATOM   10125 C CG  . TRP F  2 21  ? 2.086   18.057  13.381  1.00 14.54  ? 21  TRP F CG  1 
ATOM   10126 C CD1 . TRP F  2 21  ? 2.177   19.313  13.912  1.00 15.49  ? 21  TRP F CD1 1 
ATOM   10127 C CD2 . TRP F  2 21  ? 1.640   17.206  14.444  1.00 15.74  ? 21  TRP F CD2 1 
ATOM   10128 N NE1 . TRP F  2 21  ? 1.832   19.294  15.239  1.00 16.38  ? 21  TRP F NE1 1 
ATOM   10129 C CE2 . TRP F  2 21  ? 1.496   18.015  15.593  1.00 17.44  ? 21  TRP F CE2 1 
ATOM   10130 C CE3 . TRP F  2 21  ? 1.355   15.839  14.541  1.00 19.08  ? 21  TRP F CE3 1 
ATOM   10131 C CZ2 . TRP F  2 21  ? 1.079   17.502  16.826  1.00 17.70  ? 21  TRP F CZ2 1 
ATOM   10132 C CZ3 . TRP F  2 21  ? 0.939   15.328  15.771  1.00 18.47  ? 21  TRP F CZ3 1 
ATOM   10133 C CH2 . TRP F  2 21  ? 0.808   16.160  16.894  1.00 17.17  ? 21  TRP F CH2 1 
ATOM   10134 N N   . TYR F  2 22  ? 3.404   17.641  9.000   1.00 12.32  ? 22  TYR F N   1 
ATOM   10135 C CA  . TYR F  2 22  ? 3.818   16.908  7.811   1.00 11.15  ? 22  TYR F CA  1 
ATOM   10136 C C   . TYR F  2 22  ? 3.977   17.869  6.642   1.00 11.05  ? 22  TYR F C   1 
ATOM   10137 O O   . TYR F  2 22  ? 3.312   18.906  6.583   1.00 10.39  ? 22  TYR F O   1 
ATOM   10138 C CB  . TYR F  2 22  ? 2.792   15.829  7.468   1.00 10.55  ? 22  TYR F CB  1 
ATOM   10139 C CG  . TYR F  2 22  ? 2.387   14.976  8.648   1.00 11.47  ? 22  TYR F CG  1 
ATOM   10140 C CD1 . TYR F  2 22  ? 1.272   15.307  9.419   1.00 12.93  ? 22  TYR F CD1 1 
ATOM   10141 C CD2 . TYR F  2 22  ? 3.120   13.845  8.999   1.00 9.93   ? 22  TYR F CD2 1 
ATOM   10142 C CE1 . TYR F  2 22  ? 0.898   14.533  10.510  1.00 10.76  ? 22  TYR F CE1 1 
ATOM   10143 C CE2 . TYR F  2 22  ? 2.754   13.064  10.088  1.00 9.95   ? 22  TYR F CE2 1 
ATOM   10144 C CZ  . TYR F  2 22  ? 1.642   13.415  10.837  1.00 10.67  ? 22  TYR F CZ  1 
ATOM   10145 O OH  . TYR F  2 22  ? 1.273   12.647  11.913  1.00 8.63   ? 22  TYR F OH  1 
ATOM   10146 N N   . GLY F  2 23  ? 4.855   17.523  5.709   1.00 11.15  ? 23  GLY F N   1 
ATOM   10147 C CA  . GLY F  2 23  ? 5.090   18.382  4.564   1.00 10.93  ? 23  GLY F CA  1 
ATOM   10148 C C   . GLY F  2 23  ? 5.757   17.734  3.374   1.00 10.80  ? 23  GLY F C   1 
ATOM   10149 O O   . GLY F  2 23  ? 5.986   16.519  3.352   1.00 10.57  ? 23  GLY F O   1 
ATOM   10150 N N   . PHE F  2 24  ? 6.053   18.576  2.383   1.00 10.97  ? 24  PHE F N   1 
ATOM   10151 C CA  . PHE F  2 24  ? 6.733   18.199  1.153   1.00 11.04  ? 24  PHE F CA  1 
ATOM   10152 C C   . PHE F  2 24  ? 8.006   19.028  1.004   1.00 11.35  ? 24  PHE F C   1 
ATOM   10153 O O   . PHE F  2 24  ? 8.024   20.226  1.308   1.00 11.03  ? 24  PHE F O   1 
ATOM   10154 C CB  . PHE F  2 24  ? 5.861   18.484  -0.075  1.00 11.27  ? 24  PHE F CB  1 
ATOM   10155 C CG  . PHE F  2 24  ? 4.444   17.991  0.027   1.00 13.76  ? 24  PHE F CG  1 
ATOM   10156 C CD1 . PHE F  2 24  ? 3.481   18.723  0.721   1.00 13.15  ? 24  PHE F CD1 1 
ATOM   10157 C CD2 . PHE F  2 24  ? 4.058   16.819  -0.620  1.00 16.49  ? 24  PHE F CD2 1 
ATOM   10158 C CE1 . PHE F  2 24  ? 2.165   18.281  0.794   1.00 15.45  ? 24  PHE F CE1 1 
ATOM   10159 C CE2 . PHE F  2 24  ? 2.744   16.369  -0.553  1.00 15.49  ? 24  PHE F CE2 1 
ATOM   10160 C CZ  . PHE F  2 24  ? 1.796   17.100  0.156   1.00 17.00  ? 24  PHE F CZ  1 
ATOM   10161 N N   . ARG F  2 25  ? 9.059   18.380  0.515   1.00 11.75  ? 25  ARG F N   1 
ATOM   10162 C CA  . ARG F  2 25  ? 10.303  19.045  0.154   1.00 12.09  ? 25  ARG F CA  1 
ATOM   10163 C C   . ARG F  2 25  ? 10.653  18.612  -1.263  1.00 12.90  ? 25  ARG F C   1 
ATOM   10164 O O   . ARG F  2 25  ? 10.724  17.415  -1.547  1.00 12.54  ? 25  ARG F O   1 
ATOM   10165 C CB  . ARG F  2 25  ? 11.419  18.682  1.138   1.00 11.28  ? 25  ARG F CB  1 
ATOM   10166 C CG  . ARG F  2 25  ? 12.712  19.466  0.950   1.00 11.46  ? 25  ARG F CG  1 
ATOM   10167 C CD  . ARG F  2 25  ? 13.629  19.346  2.165   1.00 11.35  ? 25  ARG F CD  1 
ATOM   10168 N NE  . ARG F  2 25  ? 13.145  20.147  3.289   1.00 13.28  ? 25  ARG F NE  1 
ATOM   10169 C CZ  . ARG F  2 25  ? 13.636  20.097  4.525   1.00 12.28  ? 25  ARG F CZ  1 
ATOM   10170 N NH1 . ARG F  2 25  ? 14.639  19.280  4.822   1.00 12.49  ? 25  ARG F NH1 1 
ATOM   10171 N NH2 . ARG F  2 25  ? 13.120  20.868  5.472   1.00 10.83  ? 25  ARG F NH2 1 
ATOM   10172 N N   . HIS F  2 26  ? 10.861  19.583  -2.149  1.00 14.27  ? 26  HIS F N   1 
ATOM   10173 C CA  . HIS F  2 26  ? 11.073  19.294  -3.571  1.00 15.07  ? 26  HIS F CA  1 
ATOM   10174 C C   . HIS F  2 26  ? 12.367  19.878  -4.139  1.00 15.95  ? 26  HIS F C   1 
ATOM   10175 O O   . HIS F  2 26  ? 12.816  20.944  -3.717  1.00 16.17  ? 26  HIS F O   1 
ATOM   10176 C CB  . HIS F  2 26  ? 9.873   19.768  -4.398  1.00 14.87  ? 26  HIS F CB  1 
ATOM   10177 C CG  . HIS F  2 26  ? 9.673   21.253  -4.383  1.00 14.36  ? 26  HIS F CG  1 
ATOM   10178 N ND1 . HIS F  2 26  ? 10.390  22.109  -5.192  1.00 13.51  ? 26  HIS F ND1 1 
ATOM   10179 C CD2 . HIS F  2 26  ? 8.834   22.033  -3.661  1.00 13.06  ? 26  HIS F CD2 1 
ATOM   10180 C CE1 . HIS F  2 26  ? 10.007  23.352  -4.963  1.00 12.68  ? 26  HIS F CE1 1 
ATOM   10181 N NE2 . HIS F  2 26  ? 9.063   23.334  -4.040  1.00 10.95  ? 26  HIS F NE2 1 
ATOM   10182 N N   . GLN F  2 27  ? 12.952  19.165  -5.100  1.00 16.88  ? 27  GLN F N   1 
ATOM   10183 C CA  . GLN F  2 27  ? 14.110  19.642  -5.861  1.00 17.67  ? 27  GLN F CA  1 
ATOM   10184 C C   . GLN F  2 27  ? 13.735  19.788  -7.330  1.00 17.37  ? 27  GLN F C   1 
ATOM   10185 O O   . GLN F  2 27  ? 13.122  18.889  -7.907  1.00 16.92  ? 27  GLN F O   1 
ATOM   10186 C CB  . GLN F  2 27  ? 15.288  18.666  -5.742  1.00 17.93  ? 27  GLN F CB  1 
ATOM   10187 C CG  . GLN F  2 27  ? 16.266  18.957  -4.611  1.00 22.11  ? 27  GLN F CG  1 
ATOM   10188 C CD  . GLN F  2 27  ? 15.816  18.409  -3.266  1.00 27.60  ? 27  GLN F CD  1 
ATOM   10189 O OE1 . GLN F  2 27  ? 15.314  17.285  -3.170  1.00 32.16  ? 27  GLN F OE1 1 
ATOM   10190 N NE2 . GLN F  2 27  ? 16.011  19.198  -2.215  1.00 27.69  ? 27  GLN F NE2 1 
ATOM   10191 N N   . ASN F  2 28  ? 14.097  20.921  -7.928  1.00 17.55  ? 28  ASN F N   1 
ATOM   10192 C CA  . ASN F  2 28  ? 13.930  21.121  -9.371  1.00 17.53  ? 28  ASN F CA  1 
ATOM   10193 C C   . ASN F  2 28  ? 14.980  22.053  -9.978  1.00 17.90  ? 28  ASN F C   1 
ATOM   10194 O O   . ASN F  2 28  ? 16.063  22.228  -9.413  1.00 18.04  ? 28  ASN F O   1 
ATOM   10195 C CB  . ASN F  2 28  ? 12.496  21.563  -9.721  1.00 17.13  ? 28  ASN F CB  1 
ATOM   10196 C CG  . ASN F  2 28  ? 12.078  22.847  -9.023  1.00 16.80  ? 28  ASN F CG  1 
ATOM   10197 O OD1 . ASN F  2 28  ? 12.904  23.591  -8.486  1.00 17.34  ? 28  ASN F OD1 1 
ATOM   10198 N ND2 . ASN F  2 28  ? 10.778  23.115  -9.036  1.00 15.92  ? 28  ASN F ND2 1 
ATOM   10199 N N   . ALA F  2 29  ? 14.651  22.650  -11.123 1.00 18.11  ? 29  ALA F N   1 
ATOM   10200 C CA  . ALA F  2 29  ? 15.544  23.587  -11.806 1.00 18.33  ? 29  ALA F CA  1 
ATOM   10201 C C   . ALA F  2 29  ? 15.606  24.950  -11.108 1.00 18.78  ? 29  ALA F C   1 
ATOM   10202 O O   . ALA F  2 29  ? 16.322  25.851  -11.549 1.00 18.77  ? 29  ALA F O   1 
ATOM   10203 C CB  . ALA F  2 29  ? 15.117  23.750  -13.262 1.00 17.74  ? 29  ALA F CB  1 
ATOM   10204 N N   . GLN F  2 30  ? 14.862  25.091  -10.014 1.00 19.31  ? 30  GLN F N   1 
ATOM   10205 C CA  . GLN F  2 30  ? 14.737  26.370  -9.317  1.00 19.89  ? 30  GLN F CA  1 
ATOM   10206 C C   . GLN F  2 30  ? 15.183  26.310  -7.851  1.00 20.00  ? 30  GLN F C   1 
ATOM   10207 O O   . GLN F  2 30  ? 15.199  27.331  -7.158  1.00 20.20  ? 30  GLN F O   1 
ATOM   10208 C CB  . GLN F  2 30  ? 13.299  26.889  -9.435  1.00 20.11  ? 30  GLN F CB  1 
ATOM   10209 C CG  . GLN F  2 30  ? 12.919  27.325  -10.853 1.00 21.32  ? 30  GLN F CG  1 
ATOM   10210 C CD  . GLN F  2 30  ? 11.475  27.007  -11.211 1.00 23.18  ? 30  GLN F CD  1 
ATOM   10211 O OE1 . GLN F  2 30  ? 11.018  25.870  -11.068 1.00 22.17  ? 30  GLN F OE1 1 
ATOM   10212 N NE2 . GLN F  2 30  ? 10.755  28.011  -11.698 1.00 24.34  ? 30  GLN F NE2 1 
ATOM   10213 N N   . GLY F  2 31  ? 15.549  25.112  -7.392  1.00 19.94  ? 31  GLY F N   1 
ATOM   10214 C CA  . GLY F  2 31  ? 16.098  24.920  -6.050  1.00 19.49  ? 31  GLY F CA  1 
ATOM   10215 C C   . GLY F  2 31  ? 15.196  24.117  -5.134  1.00 19.54  ? 31  GLY F C   1 
ATOM   10216 O O   . GLY F  2 31  ? 14.177  23.577  -5.574  1.00 19.88  ? 31  GLY F O   1 
ATOM   10217 N N   . GLU F  2 32  ? 15.578  24.037  -3.859  1.00 18.90  ? 32  GLU F N   1 
ATOM   10218 C CA  . GLU F  2 32  ? 14.787  23.338  -2.848  1.00 18.64  ? 32  GLU F CA  1 
ATOM   10219 C C   . GLU F  2 32  ? 13.545  24.157  -2.476  1.00 18.11  ? 32  GLU F C   1 
ATOM   10220 O O   . GLU F  2 32  ? 13.474  25.354  -2.764  1.00 18.21  ? 32  GLU F O   1 
ATOM   10221 C CB  . GLU F  2 32  ? 15.637  23.032  -1.603  1.00 18.96  ? 32  GLU F CB  1 
ATOM   10222 C CG  . GLU F  2 32  ? 15.082  21.899  -0.732  1.00 20.20  ? 32  GLU F CG  1 
ATOM   10223 C CD  . GLU F  2 32  ? 15.856  21.679  0.560   1.00 23.03  ? 32  GLU F CD  1 
ATOM   10224 O OE1 . GLU F  2 32  ? 15.742  22.516  1.483   1.00 24.46  ? 32  GLU F OE1 1 
ATOM   10225 O OE2 . GLU F  2 32  ? 16.557  20.649  0.665   1.00 22.73  ? 32  GLU F OE2 1 
ATOM   10226 N N   . GLY F  2 33  ? 12.566  23.501  -1.854  1.00 17.73  ? 33  GLY F N   1 
ATOM   10227 C CA  . GLY F  2 33  ? 11.354  24.163  -1.369  1.00 17.14  ? 33  GLY F CA  1 
ATOM   10228 C C   . GLY F  2 33  ? 10.606  23.308  -0.361  1.00 16.72  ? 33  GLY F C   1 
ATOM   10229 O O   . GLY F  2 33  ? 10.356  22.127  -0.609  1.00 16.94  ? 33  GLY F O   1 
ATOM   10230 N N   . THR F  2 34  ? 10.249  23.903  0.777   1.00 15.91  ? 34  THR F N   1 
ATOM   10231 C CA  . THR F  2 34  ? 9.518   23.191  1.830   1.00 14.99  ? 34  THR F CA  1 
ATOM   10232 C C   . THR F  2 34  ? 8.158   23.835  2.120   1.00 14.17  ? 34  THR F C   1 
ATOM   10233 O O   . THR F  2 34  ? 8.047   25.056  2.223   1.00 13.28  ? 34  THR F O   1 
ATOM   10234 C CB  . THR F  2 34  ? 10.356  23.073  3.129   1.00 14.81  ? 34  THR F CB  1 
ATOM   10235 O OG1 . THR F  2 34  ? 11.635  22.506  2.821   1.00 16.11  ? 34  THR F OG1 1 
ATOM   10236 C CG2 . THR F  2 34  ? 9.670   22.176  4.142   1.00 14.84  ? 34  THR F CG2 1 
ATOM   10237 N N   . ALA F  2 35  ? 7.129   22.997  2.239   1.00 14.21  ? 35  ALA F N   1 
ATOM   10238 C CA  . ALA F  2 35  ? 5.777   23.452  2.558   1.00 14.38  ? 35  ALA F CA  1 
ATOM   10239 C C   . ALA F  2 35  ? 5.044   22.435  3.431   1.00 14.76  ? 35  ALA F C   1 
ATOM   10240 O O   . ALA F  2 35  ? 5.298   21.235  3.341   1.00 14.24  ? 35  ALA F O   1 
ATOM   10241 C CB  . ALA F  2 35  ? 4.994   23.718  1.283   1.00 14.17  ? 35  ALA F CB  1 
ATOM   10242 N N   . ALA F  2 36  ? 4.140   22.920  4.278   1.00 15.35  ? 36  ALA F N   1 
ATOM   10243 C CA  . ALA F  2 36  ? 3.351   22.042  5.142   1.00 15.95  ? 36  ALA F CA  1 
ATOM   10244 C C   . ALA F  2 36  ? 2.060   21.576  4.465   1.00 16.92  ? 36  ALA F C   1 
ATOM   10245 O O   . ALA F  2 36  ? 1.521   22.267  3.595   1.00 17.05  ? 36  ALA F O   1 
ATOM   10246 C CB  . ALA F  2 36  ? 3.036   22.734  6.450   1.00 15.09  ? 36  ALA F CB  1 
ATOM   10247 N N   . ASP F  2 37  ? 1.579   20.398  4.860   1.00 17.19  ? 37  ASP F N   1 
ATOM   10248 C CA  . ASP F  2 37  ? 0.263   19.924  4.445   1.00 17.70  ? 37  ASP F CA  1 
ATOM   10249 C C   . ASP F  2 37  ? -0.734  20.130  5.582   1.00 18.56  ? 37  ASP F C   1 
ATOM   10250 O O   . ASP F  2 37  ? -0.583  19.555  6.661   1.00 19.04  ? 37  ASP F O   1 
ATOM   10251 C CB  . ASP F  2 37  ? 0.311   18.448  4.031   1.00 17.62  ? 37  ASP F CB  1 
ATOM   10252 C CG  . ASP F  2 37  ? -1.066  17.883  3.705   1.00 17.59  ? 37  ASP F CG  1 
ATOM   10253 O OD1 . ASP F  2 37  ? -1.774  18.462  2.857   1.00 19.33  ? 37  ASP F OD1 1 
ATOM   10254 O OD2 . ASP F  2 37  ? -1.444  16.856  4.299   1.00 19.05  ? 37  ASP F OD2 1 
ATOM   10255 N N   . TYR F  2 38  ? -1.749  20.950  5.329   1.00 19.15  ? 38  TYR F N   1 
ATOM   10256 C CA  . TYR F  2 38  ? -2.755  21.285  6.334   1.00 20.14  ? 38  TYR F CA  1 
ATOM   10257 C C   . TYR F  2 38  ? -3.598  20.073  6.756   1.00 19.92  ? 38  TYR F C   1 
ATOM   10258 O O   . TYR F  2 38  ? -3.717  19.778  7.945   1.00 20.14  ? 38  TYR F O   1 
ATOM   10259 C CB  . TYR F  2 38  ? -3.646  22.433  5.829   1.00 20.57  ? 38  TYR F CB  1 
ATOM   10260 C CG  . TYR F  2 38  ? -4.669  22.920  6.835   1.00 24.65  ? 38  TYR F CG  1 
ATOM   10261 C CD1 . TYR F  2 38  ? -4.341  23.900  7.774   1.00 27.04  ? 38  TYR F CD1 1 
ATOM   10262 C CD2 . TYR F  2 38  ? -5.969  22.402  6.845   1.00 28.39  ? 38  TYR F CD2 1 
ATOM   10263 C CE1 . TYR F  2 38  ? -5.278  24.350  8.703   1.00 30.21  ? 38  TYR F CE1 1 
ATOM   10264 C CE2 . TYR F  2 38  ? -6.913  22.841  7.772   1.00 30.84  ? 38  TYR F CE2 1 
ATOM   10265 C CZ  . TYR F  2 38  ? -6.561  23.816  8.696   1.00 32.41  ? 38  TYR F CZ  1 
ATOM   10266 O OH  . TYR F  2 38  ? -7.491  24.256  9.612   1.00 34.77  ? 38  TYR F OH  1 
ATOM   10267 N N   . LYS F  2 39  ? -4.163  19.378  5.770   1.00 20.15  ? 39  LYS F N   1 
ATOM   10268 C CA  . LYS F  2 39  ? -5.093  18.262  5.981   1.00 20.43  ? 39  LYS F CA  1 
ATOM   10269 C C   . LYS F  2 39  ? -4.596  17.218  6.991   1.00 19.85  ? 39  LYS F C   1 
ATOM   10270 O O   . LYS F  2 39  ? -5.279  16.928  7.975   1.00 20.99  ? 39  LYS F O   1 
ATOM   10271 C CB  . LYS F  2 39  ? -5.437  17.608  4.629   1.00 20.85  ? 39  LYS F CB  1 
ATOM   10272 C CG  . LYS F  2 39  ? -6.497  16.493  4.663   1.00 25.43  ? 39  LYS F CG  1 
ATOM   10273 C CD  . LYS F  2 39  ? -7.881  16.977  5.138   1.00 35.21  ? 39  LYS F CD  1 
ATOM   10274 C CE  . LYS F  2 39  ? -8.510  18.022  4.204   1.00 38.70  ? 39  LYS F CE  1 
ATOM   10275 N NZ  . LYS F  2 39  ? -8.915  17.463  2.879   1.00 40.26  ? 39  LYS F NZ  1 
ATOM   10276 N N   . SER F  2 40  ? -3.411  16.667  6.744   1.00 18.19  ? 40  SER F N   1 
ATOM   10277 C CA  . SER F  2 40  ? -2.834  15.648  7.611   1.00 17.16  ? 40  SER F CA  1 
ATOM   10278 C C   . SER F  2 40  ? -2.431  16.197  8.982   1.00 16.74  ? 40  SER F C   1 
ATOM   10279 O O   . SER F  2 40  ? -2.656  15.543  10.003  1.00 17.03  ? 40  SER F O   1 
ATOM   10280 C CB  . SER F  2 40  ? -1.627  15.002  6.934   1.00 17.39  ? 40  SER F CB  1 
ATOM   10281 O OG  . SER F  2 40  ? -0.618  15.967  6.690   1.00 18.28  ? 40  SER F OG  1 
ATOM   10282 N N   . THR F  2 41  ? -1.832  17.388  8.996   1.00 15.65  ? 41  THR F N   1 
ATOM   10283 C CA  . THR F  2 41  ? -1.403  18.035  10.234  1.00 14.75  ? 41  THR F CA  1 
ATOM   10284 C C   . THR F  2 41  ? -2.598  18.245  11.147  1.00 15.05  ? 41  THR F C   1 
ATOM   10285 O O   . THR F  2 41  ? -2.568  17.872  12.321  1.00 15.06  ? 41  THR F O   1 
ATOM   10286 C CB  . THR F  2 41  ? -0.711  19.390  9.963   1.00 14.75  ? 41  THR F CB  1 
ATOM   10287 O OG1 . THR F  2 41  ? 0.464   19.177  9.173   1.00 15.53  ? 41  THR F OG1 1 
ATOM   10288 C CG2 . THR F  2 41  ? -0.311  20.077  11.265  1.00 13.12  ? 41  THR F CG2 1 
ATOM   10289 N N   . GLN F  2 42  ? -3.656  18.828  10.594  1.00 15.43  ? 42  GLN F N   1 
ATOM   10290 C CA  . GLN F  2 42  ? -4.865  19.078  11.355  1.00 15.90  ? 42  GLN F CA  1 
ATOM   10291 C C   . GLN F  2 42  ? -5.512  17.783  11.818  1.00 16.11  ? 42  GLN F C   1 
ATOM   10292 O O   . GLN F  2 42  ? -6.060  17.724  12.911  1.00 16.92  ? 42  GLN F O   1 
ATOM   10293 C CB  . GLN F  2 42  ? -5.858  19.906  10.547  1.00 16.19  ? 42  GLN F CB  1 
ATOM   10294 C CG  . GLN F  2 42  ? -6.758  20.774  11.414  1.00 18.67  ? 42  GLN F CG  1 
ATOM   10295 C CD  . GLN F  2 42  ? -5.968  21.717  12.313  1.00 20.08  ? 42  GLN F CD  1 
ATOM   10296 O OE1 . GLN F  2 42  ? -5.057  22.418  11.857  1.00 18.68  ? 42  GLN F OE1 1 
ATOM   10297 N NE2 . GLN F  2 42  ? -6.313  21.732  13.600  1.00 15.96  ? 42  GLN F NE2 1 
ATOM   10298 N N   . SER F  2 43  ? -5.435  16.745  10.991  1.00 15.89  ? 43  SER F N   1 
ATOM   10299 C CA  . SER F  2 43  ? -5.984  15.444  11.354  1.00 15.72  ? 43  SER F CA  1 
ATOM   10300 C C   . SER F  2 43  ? -5.311  14.858  12.595  1.00 16.17  ? 43  SER F C   1 
ATOM   10301 O O   . SER F  2 43  ? -5.976  14.243  13.428  1.00 16.84  ? 43  SER F O   1 
ATOM   10302 C CB  . SER F  2 43  ? -5.881  14.466  10.187  1.00 15.46  ? 43  SER F CB  1 
ATOM   10303 O OG  . SER F  2 43  ? -6.308  13.172  10.580  1.00 15.31  ? 43  SER F OG  1 
ATOM   10304 N N   . ALA F  2 44  ? -3.998  15.052  12.713  1.00 16.18  ? 44  ALA F N   1 
ATOM   10305 C CA  . ALA F  2 44  ? -3.235  14.510  13.836  1.00 15.60  ? 44  ALA F CA  1 
ATOM   10306 C C   . ALA F  2 44  ? -3.422  15.345  15.099  1.00 16.06  ? 44  ALA F C   1 
ATOM   10307 O O   . ALA F  2 44  ? -3.626  14.793  16.184  1.00 15.63  ? 44  ALA F O   1 
ATOM   10308 C CB  . ALA F  2 44  ? -1.771  14.393  13.478  1.00 15.49  ? 44  ALA F CB  1 
ATOM   10309 N N   . ILE F  2 45  ? -3.358  16.670  14.950  1.00 16.52  ? 45  ILE F N   1 
ATOM   10310 C CA  . ILE F  2 45  ? -3.608  17.593  16.060  1.00 17.00  ? 45  ILE F CA  1 
ATOM   10311 C C   . ILE F  2 45  ? -5.013  17.389  16.636  1.00 17.93  ? 45  ILE F C   1 
ATOM   10312 O O   . ILE F  2 45  ? -5.172  17.267  17.857  1.00 18.45  ? 45  ILE F O   1 
ATOM   10313 C CB  . ILE F  2 45  ? -3.377  19.074  15.653  1.00 16.75  ? 45  ILE F CB  1 
ATOM   10314 C CG1 . ILE F  2 45  ? -1.878  19.347  15.484  1.00 15.61  ? 45  ILE F CG1 1 
ATOM   10315 C CG2 . ILE F  2 45  ? -3.974  20.036  16.690  1.00 17.36  ? 45  ILE F CG2 1 
ATOM   10316 C CD1 . ILE F  2 45  ? -1.549  20.694  14.861  1.00 6.55   ? 45  ILE F CD1 1 
ATOM   10317 N N   . ASP F  2 46  ? -6.012  17.326  15.753  1.00 18.22  ? 46  ASP F N   1 
ATOM   10318 C CA  . ASP F  2 46  ? -7.406  17.105  16.149  1.00 18.84  ? 46  ASP F CA  1 
ATOM   10319 C C   . ASP F  2 46  ? -7.579  15.862  17.013  1.00 19.02  ? 46  ASP F C   1 
ATOM   10320 O O   . ASP F  2 46  ? -8.335  15.880  17.985  1.00 19.80  ? 46  ASP F O   1 
ATOM   10321 C CB  . ASP F  2 46  ? -8.319  17.004  14.923  1.00 19.22  ? 46  ASP F CB  1 
ATOM   10322 C CG  . ASP F  2 46  ? -8.763  18.362  14.402  1.00 21.57  ? 46  ASP F CG  1 
ATOM   10323 O OD1 . ASP F  2 46  ? -9.744  18.403  13.628  1.00 25.32  ? 46  ASP F OD1 1 
ATOM   10324 O OD2 . ASP F  2 46  ? -8.138  19.386  14.759  1.00 23.65  ? 46  ASP F OD2 1 
ATOM   10325 N N   . GLN F  2 47  ? -6.872  14.793  16.657  1.00 18.38  ? 47  GLN F N   1 
ATOM   10326 C CA  . GLN F  2 47  ? -6.952  13.542  17.400  1.00 18.25  ? 47  GLN F CA  1 
ATOM   10327 C C   . GLN F  2 47  ? -6.280  13.632  18.770  1.00 17.72  ? 47  GLN F C   1 
ATOM   10328 O O   . GLN F  2 47  ? -6.816  13.121  19.752  1.00 16.63  ? 47  GLN F O   1 
ATOM   10329 C CB  . GLN F  2 47  ? -6.371  12.390  16.582  1.00 18.44  ? 47  GLN F CB  1 
ATOM   10330 C CG  . GLN F  2 47  ? -7.326  11.834  15.539  1.00 22.25  ? 47  GLN F CG  1 
ATOM   10331 C CD  . GLN F  2 47  ? -6.680  10.779  14.665  1.00 27.06  ? 47  GLN F CD  1 
ATOM   10332 O OE1 . GLN F  2 47  ? -6.838  9.577   14.899  1.00 27.98  ? 47  GLN F OE1 1 
ATOM   10333 N NE2 . GLN F  2 47  ? -5.936  11.221  13.656  1.00 28.22  ? 47  GLN F NE2 1 
ATOM   10334 N N   . ILE F  2 48  ? -5.115  14.281  18.832  1.00 17.52  ? 48  ILE F N   1 
ATOM   10335 C CA  . ILE F  2 48  ? -4.414  14.487  20.103  1.00 17.37  ? 48  ILE F CA  1 
ATOM   10336 C C   . ILE F  2 48  ? -5.233  15.383  21.035  1.00 17.49  ? 48  ILE F C   1 
ATOM   10337 O O   . ILE F  2 48  ? -5.329  15.110  22.235  1.00 17.85  ? 48  ILE F O   1 
ATOM   10338 C CB  . ILE F  2 48  ? -2.960  15.017  19.901  1.00 17.81  ? 48  ILE F CB  1 
ATOM   10339 C CG1 . ILE F  2 48  ? -1.980  13.852  19.746  1.00 17.29  ? 48  ILE F CG1 1 
ATOM   10340 C CG2 . ILE F  2 48  ? -2.496  15.860  21.081  1.00 17.52  ? 48  ILE F CG2 1 
ATOM   10341 C CD1 . ILE F  2 48  ? -1.815  13.346  18.338  1.00 16.19  ? 48  ILE F CD1 1 
ATOM   10342 N N   . THR F  2 49  ? -5.837  16.432  20.475  1.00 17.31  ? 49  THR F N   1 
ATOM   10343 C CA  . THR F  2 49  ? -6.771  17.286  21.216  1.00 17.07  ? 49  THR F CA  1 
ATOM   10344 C C   . THR F  2 49  ? -7.911  16.445  21.793  1.00 16.82  ? 49  THR F C   1 
ATOM   10345 O O   . THR F  2 49  ? -8.351  16.674  22.925  1.00 16.97  ? 49  THR F O   1 
ATOM   10346 C CB  . THR F  2 49  ? -7.325  18.432  20.327  1.00 17.07  ? 49  THR F CB  1 
ATOM   10347 O OG1 . THR F  2 49  ? -6.239  19.253  19.886  1.00 17.83  ? 49  THR F OG1 1 
ATOM   10348 C CG2 . THR F  2 49  ? -8.319  19.306  21.088  1.00 15.11  ? 49  THR F CG2 1 
ATOM   10349 N N   . GLY F  2 50  ? -8.364  15.464  21.012  1.00 16.18  ? 50  GLY F N   1 
ATOM   10350 C CA  . GLY F  2 50  ? -9.405  14.534  21.437  1.00 15.94  ? 50  GLY F CA  1 
ATOM   10351 C C   . GLY F  2 50  ? -9.048  13.743  22.682  1.00 16.14  ? 50  GLY F C   1 
ATOM   10352 O O   . GLY F  2 50  ? -9.901  13.510  23.539  1.00 17.13  ? 50  GLY F O   1 
ATOM   10353 N N   . LYS F  2 51  ? -7.786  13.331  22.785  1.00 15.45  ? 51  LYS F N   1 
ATOM   10354 C CA  . LYS F  2 51  ? -7.315  12.607  23.958  1.00 14.97  ? 51  LYS F CA  1 
ATOM   10355 C C   . LYS F  2 51  ? -7.287  13.526  25.170  1.00 15.31  ? 51  LYS F C   1 
ATOM   10356 O O   . LYS F  2 51  ? -7.675  13.123  26.267  1.00 15.47  ? 51  LYS F O   1 
ATOM   10357 C CB  . LYS F  2 51  ? -5.929  12.015  23.719  1.00 14.67  ? 51  LYS F CB  1 
ATOM   10358 C CG  . LYS F  2 51  ? -5.897  10.930  22.663  1.00 15.38  ? 51  LYS F CG  1 
ATOM   10359 C CD  . LYS F  2 51  ? -4.566  10.211  22.653  1.00 14.34  ? 51  LYS F CD  1 
ATOM   10360 C CE  . LYS F  2 51  ? -4.593  9.081   21.652  1.00 16.46  ? 51  LYS F CE  1 
ATOM   10361 N NZ  . LYS F  2 51  ? -3.431  8.174   21.803  1.00 17.81  ? 51  LYS F NZ  1 
ATOM   10362 N N   . LEU F  2 52  ? -6.837  14.762  24.958  1.00 14.85  ? 52  LEU F N   1 
ATOM   10363 C CA  . LEU F  2 52  ? -6.736  15.743  26.030  1.00 14.54  ? 52  LEU F CA  1 
ATOM   10364 C C   . LEU F  2 52  ? -8.101  16.101  26.603  1.00 15.18  ? 52  LEU F C   1 
ATOM   10365 O O   . LEU F  2 52  ? -8.238  16.254  27.818  1.00 15.76  ? 52  LEU F O   1 
ATOM   10366 C CB  . LEU F  2 52  ? -6.009  17.006  25.560  1.00 14.73  ? 52  LEU F CB  1 
ATOM   10367 C CG  . LEU F  2 52  ? -4.516  16.917  25.233  1.00 13.91  ? 52  LEU F CG  1 
ATOM   10368 C CD1 . LEU F  2 52  ? -3.998  18.286  24.824  1.00 12.52  ? 52  LEU F CD1 1 
ATOM   10369 C CD2 . LEU F  2 52  ? -3.708  16.367  26.405  1.00 11.68  ? 52  LEU F CD2 1 
ATOM   10370 N N   . ASN F  2 53  ? -9.107  16.223  25.735  1.00 15.02  ? 53  ASN F N   1 
ATOM   10371 C CA  . ASN F  2 53  ? -10.475 16.491  26.183  1.00 15.54  ? 53  ASN F CA  1 
ATOM   10372 C C   . ASN F  2 53  ? -10.996 15.391  27.103  1.00 15.58  ? 53  ASN F C   1 
ATOM   10373 O O   . ASN F  2 53  ? -11.764 15.655  28.023  1.00 15.87  ? 53  ASN F O   1 
ATOM   10374 C CB  . ASN F  2 53  ? -11.425 16.668  24.993  1.00 16.36  ? 53  ASN F CB  1 
ATOM   10375 C CG  . ASN F  2 53  ? -11.130 17.918  24.174  1.00 16.71  ? 53  ASN F CG  1 
ATOM   10376 O OD1 . ASN F  2 53  ? -10.573 18.897  24.674  1.00 18.76  ? 53  ASN F OD1 1 
ATOM   10377 N ND2 . ASN F  2 53  ? -11.514 17.888  22.904  1.00 18.02  ? 53  ASN F ND2 1 
ATOM   10378 N N   . ARG F  2 54  ? -10.560 14.161  26.851  1.00 15.88  ? 54  ARG F N   1 
ATOM   10379 C CA  . ARG F  2 54  ? -10.954 13.014  27.658  1.00 15.63  ? 54  ARG F CA  1 
ATOM   10380 C C   . ARG F  2 54  ? -10.308 12.986  29.034  1.00 15.89  ? 54  ARG F C   1 
ATOM   10381 O O   . ARG F  2 54  ? -10.926 12.512  29.986  1.00 17.42  ? 54  ARG F O   1 
ATOM   10382 C CB  . ARG F  2 54  ? -10.639 11.711  26.927  1.00 15.43  ? 54  ARG F CB  1 
ATOM   10383 C CG  . ARG F  2 54  ? -11.806 11.126  26.161  1.00 15.66  ? 54  ARG F CG  1 
ATOM   10384 C CD  . ARG F  2 54  ? -11.412 9.852   25.427  1.00 18.67  ? 54  ARG F CD  1 
ATOM   10385 N NE  . ARG F  2 54  ? -10.689 8.917   26.286  1.00 18.01  ? 54  ARG F NE  1 
ATOM   10386 C CZ  . ARG F  2 54  ? -9.406  8.587   26.150  1.00 19.07  ? 54  ARG F CZ  1 
ATOM   10387 N NH1 . ARG F  2 54  ? -8.670  9.097   25.170  1.00 10.54  ? 54  ARG F NH1 1 
ATOM   10388 N NH2 . ARG F  2 54  ? -8.858  7.729   27.002  1.00 21.23  ? 54  ARG F NH2 1 
ATOM   10389 N N   . LEU F  2 55  ? -9.079  13.488  29.139  1.00 15.97  ? 55  LEU F N   1 
ATOM   10390 C CA  . LEU F  2 55  ? -8.297  13.379  30.380  1.00 16.79  ? 55  LEU F CA  1 
ATOM   10391 C C   . LEU F  2 55  ? -8.229  14.640  31.236  1.00 17.58  ? 55  LEU F C   1 
ATOM   10392 O O   . LEU F  2 55  ? -8.070  14.550  32.453  1.00 18.39  ? 55  LEU F O   1 
ATOM   10393 C CB  . LEU F  2 55  ? -6.872  12.898  30.082  1.00 16.95  ? 55  LEU F CB  1 
ATOM   10394 C CG  . LEU F  2 55  ? -6.680  11.552  29.377  1.00 19.03  ? 55  LEU F CG  1 
ATOM   10395 C CD1 . LEU F  2 55  ? -5.214  11.171  29.385  1.00 21.80  ? 55  LEU F CD1 1 
ATOM   10396 C CD2 . LEU F  2 55  ? -7.505  10.465  30.036  1.00 22.37  ? 55  LEU F CD2 1 
ATOM   10397 N N   . ILE F  2 56  ? -8.338  15.804  30.600  1.00 17.95  ? 56  ILE F N   1 
ATOM   10398 C CA  . ILE F  2 56  ? -8.164  17.089  31.275  1.00 18.80  ? 56  ILE F CA  1 
ATOM   10399 C C   . ILE F  2 56  ? -9.512  17.760  31.540  1.00 20.12  ? 56  ILE F C   1 
ATOM   10400 O O   . ILE F  2 56  ? -10.427 17.673  30.715  1.00 20.43  ? 56  ILE F O   1 
ATOM   10401 C CB  . ILE F  2 56  ? -7.240  18.036  30.442  1.00 18.75  ? 56  ILE F CB  1 
ATOM   10402 C CG1 . ILE F  2 56  ? -5.914  17.345  30.086  1.00 19.83  ? 56  ILE F CG1 1 
ATOM   10403 C CG2 . ILE F  2 56  ? -6.991  19.368  31.147  1.00 17.52  ? 56  ILE F CG2 1 
ATOM   10404 C CD1 . ILE F  2 56  ? -5.022  16.987  31.273  1.00 20.70  ? 56  ILE F CD1 1 
ATOM   10405 N N   . GLY F  2 57  ? -9.626  18.420  32.693  1.00 20.93  ? 57  GLY F N   1 
ATOM   10406 C CA  . GLY F  2 57  ? -10.826 19.179  33.052  1.00 22.47  ? 57  GLY F CA  1 
ATOM   10407 C C   . GLY F  2 57  ? -12.037 18.330  33.397  1.00 24.05  ? 57  GLY F C   1 
ATOM   10408 O O   . GLY F  2 57  ? -13.175 18.778  33.254  1.00 24.45  ? 57  GLY F O   1 
ATOM   10409 N N   . LYS F  2 58  ? -11.787 17.104  33.852  1.00 25.39  ? 58  LYS F N   1 
ATOM   10410 C CA  . LYS F  2 58  ? -12.834 16.168  34.252  1.00 26.53  ? 58  LYS F CA  1 
ATOM   10411 C C   . LYS F  2 58  ? -13.555 16.632  35.513  1.00 26.19  ? 58  LYS F C   1 
ATOM   10412 O O   . LYS F  2 58  ? -12.931 17.198  36.412  1.00 26.06  ? 58  LYS F O   1 
ATOM   10413 C CB  . LYS F  2 58  ? -12.213 14.804  34.550  1.00 27.60  ? 58  LYS F CB  1 
ATOM   10414 C CG  . LYS F  2 58  ? -11.941 13.907  33.359  1.00 30.81  ? 58  LYS F CG  1 
ATOM   10415 C CD  . LYS F  2 58  ? -11.059 12.746  33.816  1.00 34.05  ? 58  LYS F CD  1 
ATOM   10416 C CE  . LYS F  2 58  ? -11.358 11.456  33.079  1.00 35.20  ? 58  LYS F CE  1 
ATOM   10417 N NZ  . LYS F  2 58  ? -10.586 10.330  33.674  1.00 36.91  ? 58  LYS F NZ  1 
ATOM   10418 N N   . THR F  2 59  ? -14.861 16.380  35.581  1.00 26.11  ? 59  THR F N   1 
ATOM   10419 C CA  . THR F  2 59  ? -15.610 16.532  36.826  1.00 26.50  ? 59  THR F CA  1 
ATOM   10420 C C   . THR F  2 59  ? -15.323 15.297  37.691  1.00 26.42  ? 59  THR F C   1 
ATOM   10421 O O   . THR F  2 59  ? -15.296 14.177  37.186  1.00 26.78  ? 59  THR F O   1 
ATOM   10422 C CB  . THR F  2 59  ? -17.144 16.660  36.584  1.00 26.96  ? 59  THR F CB  1 
ATOM   10423 O OG1 . THR F  2 59  ? -17.404 17.526  35.469  1.00 27.18  ? 59  THR F OG1 1 
ATOM   10424 C CG2 . THR F  2 59  ? -17.849 17.214  37.824  1.00 26.82  ? 59  THR F CG2 1 
ATOM   10425 N N   . ASN F  2 60  ? -15.102 15.508  38.985  1.00 25.86  ? 60  ASN F N   1 
ATOM   10426 C CA  . ASN F  2 60  ? -14.770 14.418  39.897  1.00 25.29  ? 60  ASN F CA  1 
ATOM   10427 C C   . ASN F  2 60  ? -15.854 14.164  40.947  1.00 24.42  ? 60  ASN F C   1 
ATOM   10428 O O   . ASN F  2 60  ? -16.727 15.007  41.167  1.00 24.44  ? 60  ASN F O   1 
ATOM   10429 C CB  . ASN F  2 60  ? -13.429 14.700  40.579  1.00 25.89  ? 60  ASN F CB  1 
ATOM   10430 C CG  . ASN F  2 60  ? -12.264 14.712  39.602  1.00 28.72  ? 60  ASN F CG  1 
ATOM   10431 O OD1 . ASN F  2 60  ? -11.981 13.710  38.940  1.00 34.49  ? 60  ASN F OD1 1 
ATOM   10432 N ND2 . ASN F  2 60  ? -11.572 15.847  39.519  1.00 27.31  ? 60  ASN F ND2 1 
ATOM   10433 N N   . GLN F  2 61  ? -15.798 12.993  41.580  1.00 23.06  ? 61  GLN F N   1 
ATOM   10434 C CA  . GLN F  2 61  ? -16.693 12.661  42.688  1.00 21.92  ? 61  GLN F CA  1 
ATOM   10435 C C   . GLN F  2 61  ? -16.229 13.331  43.968  1.00 19.51  ? 61  GLN F C   1 
ATOM   10436 O O   . GLN F  2 61  ? -15.029 13.465  44.207  1.00 19.13  ? 61  GLN F O   1 
ATOM   10437 C CB  . GLN F  2 61  ? -16.738 11.152  42.914  1.00 22.65  ? 61  GLN F CB  1 
ATOM   10438 C CG  . GLN F  2 61  ? -17.843 10.428  42.173  1.00 27.59  ? 61  GLN F CG  1 
ATOM   10439 C CD  . GLN F  2 61  ? -17.460 8.991   41.848  1.00 34.13  ? 61  GLN F CD  1 
ATOM   10440 O OE1 . GLN F  2 61  ? -16.639 8.742   40.960  1.00 32.88  ? 61  GLN F OE1 1 
ATOM   10441 N NE2 . GLN F  2 61  ? -18.054 8.038   42.565  1.00 33.81  ? 61  GLN F NE2 1 
ATOM   10442 N N   . GLN F  2 62  ? -17.183 13.745  44.793  1.00 17.57  ? 62  GLN F N   1 
ATOM   10443 C CA  . GLN F  2 62  ? -16.856 14.282  46.103  1.00 16.33  ? 62  GLN F CA  1 
ATOM   10444 C C   . GLN F  2 62  ? -16.618 13.141  47.086  1.00 15.77  ? 62  GLN F C   1 
ATOM   10445 O O   . GLN F  2 62  ? -17.361 12.161  47.102  1.00 15.52  ? 62  GLN F O   1 
ATOM   10446 C CB  . GLN F  2 62  ? -17.960 15.212  46.604  1.00 15.96  ? 62  GLN F CB  1 
ATOM   10447 C CG  . GLN F  2 62  ? -17.671 15.827  47.960  1.00 14.73  ? 62  GLN F CG  1 
ATOM   10448 C CD  . GLN F  2 62  ? -18.287 17.195  48.128  1.00 17.84  ? 62  GLN F CD  1 
ATOM   10449 O OE1 . GLN F  2 62  ? -17.886 18.157  47.466  1.00 20.34  ? 62  GLN F OE1 1 
ATOM   10450 N NE2 . GLN F  2 62  ? -19.256 17.297  49.027  1.00 13.74  ? 62  GLN F NE2 1 
ATOM   10451 N N   . PHE F  2 63  ? -15.563 13.268  47.884  1.00 15.20  ? 63  PHE F N   1 
ATOM   10452 C CA  . PHE F  2 63  ? -15.289 12.323  48.958  1.00 14.73  ? 63  PHE F CA  1 
ATOM   10453 C C   . PHE F  2 63  ? -15.145 13.063  50.275  1.00 14.64  ? 63  PHE F C   1 
ATOM   10454 O O   . PHE F  2 63  ? -14.489 14.107  50.344  1.00 14.66  ? 63  PHE F O   1 
ATOM   10455 C CB  . PHE F  2 63  ? -14.028 11.505  48.666  1.00 14.77  ? 63  PHE F CB  1 
ATOM   10456 C CG  . PHE F  2 63  ? -14.224 10.439  47.627  1.00 14.29  ? 63  PHE F CG  1 
ATOM   10457 C CD1 . PHE F  2 63  ? -14.592 9.148   47.997  1.00 15.48  ? 63  PHE F CD1 1 
ATOM   10458 C CD2 . PHE F  2 63  ? -14.038 10.722  46.277  1.00 13.76  ? 63  PHE F CD2 1 
ATOM   10459 C CE1 . PHE F  2 63  ? -14.777 8.155   47.039  1.00 15.12  ? 63  PHE F CE1 1 
ATOM   10460 C CE2 . PHE F  2 63  ? -14.222 9.737   45.311  1.00 14.37  ? 63  PHE F CE2 1 
ATOM   10461 C CZ  . PHE F  2 63  ? -14.591 8.452   45.693  1.00 16.77  ? 63  PHE F CZ  1 
ATOM   10462 N N   . GLU F  2 64  ? -15.771 12.524  51.315  1.00 14.50  ? 64  GLU F N   1 
ATOM   10463 C CA  . GLU F  2 64  ? -15.723 13.139  52.631  1.00 14.99  ? 64  GLU F CA  1 
ATOM   10464 C C   . GLU F  2 64  ? -14.613 12.531  53.471  1.00 14.96  ? 64  GLU F C   1 
ATOM   10465 O O   . GLU F  2 64  ? -14.003 11.528  53.092  1.00 15.62  ? 64  GLU F O   1 
ATOM   10466 C CB  . GLU F  2 64  ? -17.061 12.990  53.357  1.00 15.03  ? 64  GLU F CB  1 
ATOM   10467 C CG  . GLU F  2 64  ? -18.241 13.667  52.678  1.00 16.87  ? 64  GLU F CG  1 
ATOM   10468 C CD  . GLU F  2 64  ? -19.516 13.561  53.497  1.00 21.70  ? 64  GLU F CD  1 
ATOM   10469 O OE1 . GLU F  2 64  ? -19.486 12.923  54.577  1.00 19.03  ? 64  GLU F OE1 1 
ATOM   10470 O OE2 . GLU F  2 64  ? -20.547 14.126  53.063  1.00 23.78  ? 64  GLU F OE2 1 
ATOM   10471 N N   . LEU F  2 65  ? -14.361 13.158  54.613  1.00 14.70  ? 65  LEU F N   1 
ATOM   10472 C CA  . LEU F  2 65  ? -13.405 12.671  55.586  1.00 14.38  ? 65  LEU F CA  1 
ATOM   10473 C C   . LEU F  2 65  ? -14.026 11.480  56.312  1.00 14.01  ? 65  LEU F C   1 
ATOM   10474 O O   . LEU F  2 65  ? -15.141 11.581  56.807  1.00 14.37  ? 65  LEU F O   1 
ATOM   10475 C CB  . LEU F  2 65  ? -13.119 13.787  56.588  1.00 14.40  ? 65  LEU F CB  1 
ATOM   10476 C CG  . LEU F  2 65  ? -11.716 14.176  57.049  1.00 14.39  ? 65  LEU F CG  1 
ATOM   10477 C CD1 . LEU F  2 65  ? -11.831 14.685  58.467  1.00 17.28  ? 65  LEU F CD1 1 
ATOM   10478 C CD2 . LEU F  2 65  ? -10.724 13.037  56.990  1.00 19.69  ? 65  LEU F CD2 1 
ATOM   10479 N N   . ILE F  2 66  ? -13.321 10.354  56.363  1.00 14.93  ? 66  ILE F N   1 
ATOM   10480 C CA  . ILE F  2 66  ? -13.781 9.183   57.131  1.00 16.00  ? 66  ILE F CA  1 
ATOM   10481 C C   . ILE F  2 66  ? -12.774 8.838   58.218  1.00 16.23  ? 66  ILE F C   1 
ATOM   10482 O O   . ILE F  2 66  ? -12.801 7.754   58.799  1.00 15.99  ? 66  ILE F O   1 
ATOM   10483 C CB  . ILE F  2 66  ? -14.002 7.931   56.240  1.00 16.46  ? 66  ILE F CB  1 
ATOM   10484 C CG1 . ILE F  2 66  ? -12.842 7.751   55.251  1.00 16.22  ? 66  ILE F CG1 1 
ATOM   10485 C CG2 . ILE F  2 66  ? -15.360 7.999   55.533  1.00 16.02  ? 66  ILE F CG2 1 
ATOM   10486 C CD1 . ILE F  2 66  ? -12.722 6.342   54.694  1.00 23.03  ? 66  ILE F CD1 1 
ATOM   10487 N N   . ASP F  2 67  ? -11.909 9.801   58.500  1.00 17.00  ? 67  ASP F N   1 
ATOM   10488 C CA  . ASP F  2 67  ? -10.669 9.578   59.211  1.00 17.61  ? 67  ASP F CA  1 
ATOM   10489 C C   . ASP F  2 67  ? -10.494 10.788  60.116  1.00 17.10  ? 67  ASP F C   1 
ATOM   10490 O O   . ASP F  2 67  ? -11.126 11.823  59.893  1.00 17.82  ? 67  ASP F O   1 
ATOM   10491 C CB  . ASP F  2 67  ? -9.536  9.541   58.176  1.00 18.39  ? 67  ASP F CB  1 
ATOM   10492 C CG  . ASP F  2 67  ? -8.533  8.430   58.422  1.00 20.92  ? 67  ASP F CG  1 
ATOM   10493 O OD1 . ASP F  2 67  ? -8.869  7.446   59.114  1.00 27.46  ? 67  ASP F OD1 1 
ATOM   10494 O OD2 . ASP F  2 67  ? -7.401  8.539   57.903  1.00 24.42  ? 67  ASP F OD2 1 
ATOM   10495 N N   . ASN F  2 68  ? -9.652  10.681  61.135  1.00 15.78  ? 68  ASN F N   1 
ATOM   10496 C CA  . ASN F  2 68  ? -9.375  11.851  61.956  1.00 14.97  ? 68  ASN F CA  1 
ATOM   10497 C C   . ASN F  2 68  ? -7.896  12.045  62.259  1.00 15.25  ? 68  ASN F C   1 
ATOM   10498 O O   . ASN F  2 68  ? -7.250  11.207  62.889  1.00 15.12  ? 68  ASN F O   1 
ATOM   10499 C CB  . ASN F  2 68  ? -10.228 11.864  63.229  1.00 14.51  ? 68  ASN F CB  1 
ATOM   10500 C CG  . ASN F  2 68  ? -10.390 13.264  63.814  1.00 13.66  ? 68  ASN F CG  1 
ATOM   10501 O OD1 . ASN F  2 68  ? -9.418  14.007  63.983  1.00 10.82  ? 68  ASN F OD1 1 
ATOM   10502 N ND2 . ASN F  2 68  ? -11.625 13.626  64.130  1.00 10.82  ? 68  ASN F ND2 1 
ATOM   10503 N N   . GLU F  2 69  ? -7.388  13.180  61.795  1.00 15.61  ? 69  GLU F N   1 
ATOM   10504 C CA  . GLU F  2 69  ? -5.983  13.539  61.884  1.00 16.31  ? 69  GLU F CA  1 
ATOM   10505 C C   . GLU F  2 69  ? -5.616  14.061  63.272  1.00 16.93  ? 69  GLU F C   1 
ATOM   10506 O O   . GLU F  2 69  ? -4.482  13.894  63.727  1.00 16.86  ? 69  GLU F O   1 
ATOM   10507 C CB  . GLU F  2 69  ? -5.701  14.612  60.842  1.00 16.25  ? 69  GLU F CB  1 
ATOM   10508 C CG  . GLU F  2 69  ? -4.258  14.782  60.453  1.00 16.89  ? 69  GLU F CG  1 
ATOM   10509 C CD  . GLU F  2 69  ? -4.102  15.778  59.326  1.00 18.56  ? 69  GLU F CD  1 
ATOM   10510 O OE1 . GLU F  2 69  ? -3.247  16.680  59.446  1.00 18.21  ? 69  GLU F OE1 1 
ATOM   10511 O OE2 . GLU F  2 69  ? -4.849  15.665  58.326  1.00 19.09  ? 69  GLU F OE2 1 
ATOM   10512 N N   . PHE F  2 70  ? -6.580  14.695  63.936  1.00 17.37  ? 70  PHE F N   1 
ATOM   10513 C CA  . PHE F  2 70  ? -6.347  15.312  65.239  1.00 17.44  ? 70  PHE F CA  1 
ATOM   10514 C C   . PHE F  2 70  ? -6.765  14.401  66.388  1.00 18.57  ? 70  PHE F C   1 
ATOM   10515 O O   . PHE F  2 70  ? -6.173  14.438  67.465  1.00 18.51  ? 70  PHE F O   1 
ATOM   10516 C CB  . PHE F  2 70  ? -7.088  16.648  65.342  1.00 16.93  ? 70  PHE F CB  1 
ATOM   10517 C CG  . PHE F  2 70  ? -6.834  17.589  64.188  1.00 13.34  ? 70  PHE F CG  1 
ATOM   10518 C CD1 . PHE F  2 70  ? -7.887  18.290  63.610  1.00 8.68   ? 70  PHE F CD1 1 
ATOM   10519 C CD2 . PHE F  2 70  ? -5.547  17.780  63.685  1.00 9.39   ? 70  PHE F CD2 1 
ATOM   10520 C CE1 . PHE F  2 70  ? -7.664  19.168  62.555  1.00 7.74   ? 70  PHE F CE1 1 
ATOM   10521 C CE2 . PHE F  2 70  ? -5.317  18.654  62.628  1.00 5.83   ? 70  PHE F CE2 1 
ATOM   10522 C CZ  . PHE F  2 70  ? -6.377  19.350  62.063  1.00 6.98   ? 70  PHE F CZ  1 
ATOM   10523 N N   . ASN F  2 71  ? -7.795  13.594  66.155  1.00 20.17  ? 71  ASN F N   1 
ATOM   10524 C CA  . ASN F  2 71  ? -8.265  12.631  67.141  1.00 21.93  ? 71  ASN F CA  1 
ATOM   10525 C C   . ASN F  2 71  ? -8.263  11.213  66.584  1.00 22.43  ? 71  ASN F C   1 
ATOM   10526 O O   . ASN F  2 71  ? -9.140  10.848  65.801  1.00 22.26  ? 71  ASN F O   1 
ATOM   10527 C CB  . ASN F  2 71  ? -9.663  13.009  67.637  1.00 22.46  ? 71  ASN F CB  1 
ATOM   10528 C CG  . ASN F  2 71  ? -9.628  13.974  68.807  1.00 25.71  ? 71  ASN F CG  1 
ATOM   10529 O OD1 . ASN F  2 71  ? -9.266  15.145  68.663  1.00 27.78  ? 71  ASN F OD1 1 
ATOM   10530 N ND2 . ASN F  2 71  ? -10.021 13.486  69.979  1.00 29.89  ? 71  ASN F ND2 1 
ATOM   10531 N N   . GLU F  2 72  ? -7.270  10.421  66.986  1.00 23.24  ? 72  GLU F N   1 
ATOM   10532 C CA  . GLU F  2 72  ? -7.138  9.037   66.519  1.00 23.85  ? 72  GLU F CA  1 
ATOM   10533 C C   . GLU F  2 72  ? -8.445  8.266   66.722  1.00 23.20  ? 72  GLU F C   1 
ATOM   10534 O O   . GLU F  2 72  ? -8.958  8.179   67.840  1.00 23.08  ? 72  GLU F O   1 
ATOM   10535 C CB  . GLU F  2 72  ? -5.971  8.334   67.233  1.00 24.60  ? 72  GLU F CB  1 
ATOM   10536 C CG  . GLU F  2 72  ? -5.655  6.908   66.741  1.00 27.39  ? 72  GLU F CG  1 
ATOM   10537 C CD  . GLU F  2 72  ? -4.665  6.854   65.573  1.00 29.48  ? 72  GLU F CD  1 
ATOM   10538 O OE1 . GLU F  2 72  ? -4.477  7.875   64.872  1.00 29.91  ? 72  GLU F OE1 1 
ATOM   10539 O OE2 . GLU F  2 72  ? -4.076  5.772   65.353  1.00 27.37  ? 72  GLU F OE2 1 
ATOM   10540 N N   . ILE F  2 73  ? -8.991  7.746   65.625  1.00 22.79  ? 73  ILE F N   1 
ATOM   10541 C CA  . ILE F  2 73  ? -10.180 6.893   65.666  1.00 21.70  ? 73  ILE F CA  1 
ATOM   10542 C C   . ILE F  2 73  ? -9.749  5.474   66.017  1.00 22.32  ? 73  ILE F C   1 
ATOM   10543 O O   . ILE F  2 73  ? -8.555  5.161   65.954  1.00 22.40  ? 73  ILE F O   1 
ATOM   10544 C CB  . ILE F  2 73  ? -10.950 6.899   64.320  1.00 21.31  ? 73  ILE F CB  1 
ATOM   10545 C CG1 . ILE F  2 73  ? -10.086 6.319   63.192  1.00 18.73  ? 73  ILE F CG1 1 
ATOM   10546 C CG2 . ILE F  2 73  ? -11.439 8.309   63.988  1.00 18.73  ? 73  ILE F CG2 1 
ATOM   10547 C CD1 . ILE F  2 73  ? -10.861 5.850   61.984  1.00 12.93  ? 73  ILE F CD1 1 
ATOM   10548 N N   . GLU F  2 74  ? -10.706 4.622   66.384  1.00 22.58  ? 74  GLU F N   1 
ATOM   10549 C CA  . GLU F  2 74  ? -10.399 3.240   66.759  1.00 23.51  ? 74  GLU F CA  1 
ATOM   10550 C C   . GLU F  2 74  ? -9.493  2.586   65.711  1.00 23.13  ? 74  GLU F C   1 
ATOM   10551 O O   . GLU F  2 74  ? -9.782  2.649   64.511  1.00 22.94  ? 74  GLU F O   1 
ATOM   10552 C CB  . GLU F  2 74  ? -11.681 2.426   66.945  1.00 24.22  ? 74  GLU F CB  1 
ATOM   10553 C CG  . GLU F  2 74  ? -11.461 1.068   67.617  1.00 29.72  ? 74  GLU F CG  1 
ATOM   10554 C CD  . GLU F  2 74  ? -12.556 0.052   67.305  1.00 36.30  ? 74  GLU F CD  1 
ATOM   10555 O OE1 . GLU F  2 74  ? -12.915 -0.731  68.212  1.00 37.03  ? 74  GLU F OE1 1 
ATOM   10556 O OE2 . GLU F  2 74  ? -13.055 0.026   66.158  1.00 39.08  ? 74  GLU F OE2 1 
ATOM   10557 N N   . GLN F  2 75  ? -8.396  1.978   66.173  1.00 22.90  ? 75  GLN F N   1 
ATOM   10558 C CA  . GLN F  2 75  ? -7.391  1.375   65.282  1.00 22.95  ? 75  GLN F CA  1 
ATOM   10559 C C   . GLN F  2 75  ? -7.957  0.290   64.372  1.00 22.57  ? 75  GLN F C   1 
ATOM   10560 O O   . GLN F  2 75  ? -7.516  0.148   63.231  1.00 22.42  ? 75  GLN F O   1 
ATOM   10561 C CB  . GLN F  2 75  ? -6.198  0.814   66.064  1.00 23.27  ? 75  GLN F CB  1 
ATOM   10562 C CG  . GLN F  2 75  ? -5.135  1.837   66.443  1.00 23.40  ? 75  GLN F CG  1 
ATOM   10563 C CD  . GLN F  2 75  ? -5.309  2.381   67.851  1.00 25.43  ? 75  GLN F CD  1 
ATOM   10564 O OE1 . GLN F  2 75  ? -6.210  1.972   68.588  1.00 24.50  ? 75  GLN F OE1 1 
ATOM   10565 N NE2 . GLN F  2 75  ? -4.434  3.306   68.234  1.00 27.89  ? 75  GLN F NE2 1 
ATOM   10566 N N   . GLN F  2 76  ? -8.917  -0.476  64.890  1.00 22.27  ? 76  GLN F N   1 
ATOM   10567 C CA  . GLN F  2 76  ? -9.624  -1.488  64.108  1.00 21.81  ? 76  GLN F CA  1 
ATOM   10568 C C   . GLN F  2 76  ? -10.169 -0.883  62.808  1.00 20.31  ? 76  GLN F C   1 
ATOM   10569 O O   . GLN F  2 76  ? -9.841  -1.357  61.720  1.00 20.68  ? 76  GLN F O   1 
ATOM   10570 C CB  . GLN F  2 76  ? -10.745 -2.118  64.945  1.00 22.25  ? 76  GLN F CB  1 
ATOM   10571 C CG  . GLN F  2 76  ? -11.512 -3.256  64.275  1.00 26.50  ? 76  GLN F CG  1 
ATOM   10572 C CD  . GLN F  2 76  ? -10.739 -4.568  64.246  1.00 31.55  ? 76  GLN F CD  1 
ATOM   10573 O OE1 . GLN F  2 76  ? -9.816  -4.743  63.447  1.00 33.89  ? 76  GLN F OE1 1 
ATOM   10574 N NE2 . GLN F  2 76  ? -11.131 -5.506  65.105  1.00 29.80  ? 76  GLN F NE2 1 
ATOM   10575 N N   . ILE F  2 77  ? -10.970 0.176   62.930  1.00 18.10  ? 77  ILE F N   1 
ATOM   10576 C CA  . ILE F  2 77  ? -11.553 0.860   61.774  1.00 16.14  ? 77  ILE F CA  1 
ATOM   10577 C C   . ILE F  2 77  ? -10.478 1.616   60.987  1.00 14.98  ? 77  ILE F C   1 
ATOM   10578 O O   . ILE F  2 77  ? -10.471 1.594   59.754  1.00 14.16  ? 77  ILE F O   1 
ATOM   10579 C CB  . ILE F  2 77  ? -12.698 1.819   62.186  1.00 15.84  ? 77  ILE F CB  1 
ATOM   10580 C CG1 . ILE F  2 77  ? -13.680 1.114   63.129  1.00 19.20  ? 77  ILE F CG1 1 
ATOM   10581 C CG2 . ILE F  2 77  ? -13.434 2.337   60.958  1.00 14.42  ? 77  ILE F CG2 1 
ATOM   10582 C CD1 . ILE F  2 77  ? -14.686 2.039   63.837  1.00 22.02  ? 77  ILE F CD1 1 
ATOM   10583 N N   . GLY F  2 78  ? -9.571  2.271   61.709  1.00 14.24  ? 78  GLY F N   1 
ATOM   10584 C CA  . GLY F  2 78  ? -8.441  2.977   61.103  1.00 14.03  ? 78  GLY F CA  1 
ATOM   10585 C C   . GLY F  2 78  ? -7.621  2.121   60.155  1.00 14.33  ? 78  GLY F C   1 
ATOM   10586 O O   . GLY F  2 78  ? -7.384  2.509   59.009  1.00 14.62  ? 78  GLY F O   1 
ATOM   10587 N N   . ASN F  2 79  ? -7.199  0.950   60.625  1.00 15.00  ? 79  ASN F N   1 
ATOM   10588 C CA  . ASN F  2 79  ? -6.427  0.016   59.801  1.00 15.32  ? 79  ASN F CA  1 
ATOM   10589 C C   . ASN F  2 79  ? -7.168  -0.478  58.560  1.00 15.45  ? 79  ASN F C   1 
ATOM   10590 O O   . ASN F  2 79  ? -6.539  -0.743  57.535  1.00 16.14  ? 79  ASN F O   1 
ATOM   10591 C CB  . ASN F  2 79  ? -5.907  -1.161  60.630  1.00 15.20  ? 79  ASN F CB  1 
ATOM   10592 C CG  . ASN F  2 79  ? -4.571  -0.861  61.291  1.00 17.27  ? 79  ASN F CG  1 
ATOM   10593 O OD1 . ASN F  2 79  ? -3.645  -0.359  60.649  1.00 19.73  ? 79  ASN F OD1 1 
ATOM   10594 N ND2 . ASN F  2 79  ? -4.462  -1.175  62.578  1.00 16.04  ? 79  ASN F ND2 1 
ATOM   10595 N N   . VAL F  2 80  ? -8.494  -0.595  58.654  1.00 14.75  ? 80  VAL F N   1 
ATOM   10596 C CA  . VAL F  2 80  ? -9.327  -0.985  57.511  1.00 13.70  ? 80  VAL F CA  1 
ATOM   10597 C C   . VAL F  2 80  ? -9.344  0.123   56.463  1.00 13.68  ? 80  VAL F C   1 
ATOM   10598 O O   . VAL F  2 80  ? -9.154  -0.140  55.271  1.00 13.50  ? 80  VAL F O   1 
ATOM   10599 C CB  . VAL F  2 80  ? -10.773 -1.344  57.939  1.00 13.91  ? 80  VAL F CB  1 
ATOM   10600 C CG1 . VAL F  2 80  ? -11.670 -1.561  56.724  1.00 11.89  ? 80  VAL F CG1 1 
ATOM   10601 C CG2 . VAL F  2 80  ? -10.772 -2.581  58.820  1.00 12.65  ? 80  VAL F CG2 1 
ATOM   10602 N N   . ILE F  2 81  ? -9.559  1.357   56.917  1.00 13.91  ? 81  ILE F N   1 
ATOM   10603 C CA  . ILE F  2 81  ? -9.522  2.528   56.042  1.00 14.00  ? 81  ILE F CA  1 
ATOM   10604 C C   . ILE F  2 81  ? -8.158  2.637   55.361  1.00 14.75  ? 81  ILE F C   1 
ATOM   10605 O O   . ILE F  2 81  ? -8.088  2.726   54.137  1.00 14.80  ? 81  ILE F O   1 
ATOM   10606 C CB  . ILE F  2 81  ? -9.859  3.830   56.807  1.00 13.77  ? 81  ILE F CB  1 
ATOM   10607 C CG1 . ILE F  2 81  ? -11.332 3.833   57.222  1.00 13.23  ? 81  ILE F CG1 1 
ATOM   10608 C CG2 . ILE F  2 81  ? -9.546  5.060   55.955  1.00 13.17  ? 81  ILE F CG2 1 
ATOM   10609 C CD1 . ILE F  2 81  ? -11.641 4.751   58.381  1.00 12.77  ? 81  ILE F CD1 1 
ATOM   10610 N N   . ASN F  2 82  ? -7.086  2.604   56.155  1.00 15.87  ? 82  ASN F N   1 
ATOM   10611 C CA  . ASN F  2 82  ? -5.718  2.669   55.629  1.00 17.08  ? 82  ASN F CA  1 
ATOM   10612 C C   . ASN F  2 82  ? -5.439  1.572   54.599  1.00 16.57  ? 82  ASN F C   1 
ATOM   10613 O O   . ASN F  2 82  ? -4.797  1.829   53.578  1.00 16.69  ? 82  ASN F O   1 
ATOM   10614 C CB  . ASN F  2 82  ? -4.681  2.642   56.764  1.00 18.12  ? 82  ASN F CB  1 
ATOM   10615 C CG  . ASN F  2 82  ? -4.606  3.965   57.536  1.00 24.84  ? 82  ASN F CG  1 
ATOM   10616 O OD1 . ASN F  2 82  ? -5.522  4.790   57.475  1.00 27.49  ? 82  ASN F OD1 1 
ATOM   10617 N ND2 . ASN F  2 82  ? -3.504  4.164   58.269  1.00 37.37  ? 82  ASN F ND2 1 
ATOM   10618 N N   . TRP F  2 83  ? -5.944  0.365   54.866  1.00 15.90  ? 83  TRP F N   1 
ATOM   10619 C CA  . TRP F  2 83  ? -5.847  -0.765  53.938  1.00 14.92  ? 83  TRP F CA  1 
ATOM   10620 C C   . TRP F  2 83  ? -6.563  -0.456  52.624  1.00 14.05  ? 83  TRP F C   1 
ATOM   10621 O O   . TRP F  2 83  ? -5.977  -0.599  51.550  1.00 13.66  ? 83  TRP F O   1 
ATOM   10622 C CB  . TRP F  2 83  ? -6.419  -2.039  54.573  1.00 15.64  ? 83  TRP F CB  1 
ATOM   10623 C CG  . TRP F  2 83  ? -6.102  -3.307  53.823  1.00 17.36  ? 83  TRP F CG  1 
ATOM   10624 C CD1 . TRP F  2 83  ? -5.011  -4.112  53.998  1.00 19.87  ? 83  TRP F CD1 1 
ATOM   10625 C CD2 . TRP F  2 83  ? -6.885  -3.916  52.787  1.00 20.97  ? 83  TRP F CD2 1 
ATOM   10626 N NE1 . TRP F  2 83  ? -5.062  -5.181  53.134  1.00 19.67  ? 83  TRP F NE1 1 
ATOM   10627 C CE2 . TRP F  2 83  ? -6.200  -5.086  52.378  1.00 22.70  ? 83  TRP F CE2 1 
ATOM   10628 C CE3 . TRP F  2 83  ? -8.095  -3.587  52.162  1.00 22.64  ? 83  TRP F CE3 1 
ATOM   10629 C CZ2 . TRP F  2 83  ? -6.685  -5.927  51.367  1.00 25.04  ? 83  TRP F CZ2 1 
ATOM   10630 C CZ3 . TRP F  2 83  ? -8.578  -4.424  51.158  1.00 24.15  ? 83  TRP F CZ3 1 
ATOM   10631 C CH2 . TRP F  2 83  ? -7.872  -5.581  50.772  1.00 25.07  ? 83  TRP F CH2 1 
ATOM   10632 N N   . THR F  2 84  ? -7.821  -0.018  52.724  1.00 13.49  ? 84  THR F N   1 
ATOM   10633 C CA  . THR F  2 84  ? -8.643  0.344   51.560  1.00 12.26  ? 84  THR F CA  1 
ATOM   10634 C C   . THR F  2 84  ? -7.992  1.455   50.734  1.00 12.17  ? 84  THR F C   1 
ATOM   10635 O O   . THR F  2 84  ? -7.822  1.317   49.522  1.00 12.60  ? 84  THR F O   1 
ATOM   10636 C CB  . THR F  2 84  ? -10.064 0.788   51.987  1.00 11.82  ? 84  THR F CB  1 
ATOM   10637 O OG1 . THR F  2 84  ? -10.648 -0.209  52.831  1.00 11.03  ? 84  THR F OG1 1 
ATOM   10638 C CG2 . THR F  2 84  ? -10.963 1.000   50.774  1.00 11.28  ? 84  THR F CG2 1 
ATOM   10639 N N   . ARG F  2 85  ? -7.625  2.543   51.406  1.00 11.93  ? 85  ARG F N   1 
ATOM   10640 C CA  . ARG F  2 85  ? -6.950  3.680   50.779  1.00 11.87  ? 85  ARG F CA  1 
ATOM   10641 C C   . ARG F  2 85  ? -5.697  3.249   50.012  1.00 11.42  ? 85  ARG F C   1 
ATOM   10642 O O   . ARG F  2 85  ? -5.535  3.601   48.847  1.00 11.59  ? 85  ARG F O   1 
ATOM   10643 C CB  . ARG F  2 85  ? -6.616  4.736   51.837  1.00 11.54  ? 85  ARG F CB  1 
ATOM   10644 C CG  . ARG F  2 85  ? -6.167  6.073   51.289  1.00 14.30  ? 85  ARG F CG  1 
ATOM   10645 C CD  . ARG F  2 85  ? -6.271  7.147   52.360  1.00 20.87  ? 85  ARG F CD  1 
ATOM   10646 N NE  . ARG F  2 85  ? -7.516  7.907   52.247  1.00 23.46  ? 85  ARG F NE  1 
ATOM   10647 C CZ  . ARG F  2 85  ? -8.147  8.487   53.266  1.00 24.43  ? 85  ARG F CZ  1 
ATOM   10648 N NH1 . ARG F  2 85  ? -7.668  8.388   54.504  1.00 20.69  ? 85  ARG F NH1 1 
ATOM   10649 N NH2 . ARG F  2 85  ? -9.272  9.156   53.046  1.00 23.91  ? 85  ARG F NH2 1 
ATOM   10650 N N   . ASP F  2 86  ? -4.830  2.473   50.661  1.00 11.85  ? 86  ASP F N   1 
ATOM   10651 C CA  . ASP F  2 86  ? -3.622  1.958   50.017  1.00 12.55  ? 86  ASP F CA  1 
ATOM   10652 C C   . ASP F  2 86  ? -3.945  1.078   48.807  1.00 12.28  ? 86  ASP F C   1 
ATOM   10653 O O   . ASP F  2 86  ? -3.271  1.166   47.778  1.00 12.58  ? 86  ASP F O   1 
ATOM   10654 C CB  . ASP F  2 86  ? -2.733  1.206   51.017  1.00 13.24  ? 86  ASP F CB  1 
ATOM   10655 C CG  . ASP F  2 86  ? -1.961  2.142   51.950  1.00 16.26  ? 86  ASP F CG  1 
ATOM   10656 O OD1 . ASP F  2 86  ? -2.018  3.379   51.766  1.00 20.24  ? 86  ASP F OD1 1 
ATOM   10657 O OD2 . ASP F  2 86  ? -1.288  1.634   52.874  1.00 18.76  ? 86  ASP F OD2 1 
ATOM   10658 N N   . ALA F  2 87  ? -4.979  0.245   48.930  1.00 11.39  ? 87  ALA F N   1 
ATOM   10659 C CA  . ALA F  2 87  ? -5.439  -0.582  47.813  1.00 10.95  ? 87  ALA F CA  1 
ATOM   10660 C C   . ALA F  2 87  ? -5.925  0.267   46.632  1.00 11.08  ? 87  ALA F C   1 
ATOM   10661 O O   . ALA F  2 87  ? -5.664  -0.073  45.474  1.00 10.90  ? 87  ALA F O   1 
ATOM   10662 C CB  . ALA F  2 87  ? -6.520  -1.549  48.265  1.00 10.73  ? 87  ALA F CB  1 
ATOM   10663 N N   . MET F  2 88  ? -6.618  1.368   46.932  1.00 10.75  ? 88  MET F N   1 
ATOM   10664 C CA  . MET F  2 88  ? -7.046  2.328   45.907  1.00 10.74  ? 88  MET F CA  1 
ATOM   10665 C C   . MET F  2 88  ? -5.845  2.985   45.229  1.00 11.41  ? 88  MET F C   1 
ATOM   10666 O O   . MET F  2 88  ? -5.825  3.135   44.004  1.00 11.93  ? 88  MET F O   1 
ATOM   10667 C CB  . MET F  2 88  ? -7.968  3.395   46.500  1.00 10.38  ? 88  MET F CB  1 
ATOM   10668 C CG  . MET F  2 88  ? -9.268  2.859   47.066  1.00 10.42  ? 88  MET F CG  1 
ATOM   10669 S SD  . MET F  2 88  ? -10.255 2.027   45.815  1.00 14.59  ? 88  MET F SD  1 
ATOM   10670 C CE  . MET F  2 88  ? -11.313 1.003   46.834  1.00 17.65  ? 88  MET F CE  1 
ATOM   10671 N N   . THR F  2 89  ? -4.848  3.364   46.029  1.00 11.15  ? 89  THR F N   1 
ATOM   10672 C CA  . THR F  2 89  ? -3.584  3.886   45.513  1.00 11.55  ? 89  THR F CA  1 
ATOM   10673 C C   . THR F  2 89  ? -2.937  2.892   44.536  1.00 12.02  ? 89  THR F C   1 
ATOM   10674 O O   . THR F  2 89  ? -2.465  3.285   43.472  1.00 12.83  ? 89  THR F O   1 
ATOM   10675 C CB  . THR F  2 89  ? -2.614  4.265   46.670  1.00 12.06  ? 89  THR F CB  1 
ATOM   10676 O OG1 . THR F  2 89  ? -3.154  5.376   47.401  1.00 12.00  ? 89  THR F OG1 1 
ATOM   10677 C CG2 . THR F  2 89  ? -1.221  4.638   46.146  1.00 10.03  ? 89  THR F CG2 1 
ATOM   10678 N N   . GLU F  2 90  ? -2.948  1.608   44.894  1.00 11.77  ? 90  GLU F N   1 
ATOM   10679 C CA  . GLU F  2 90  ? -2.400  0.546   44.048  1.00 11.52  ? 90  GLU F CA  1 
ATOM   10680 C C   . GLU F  2 90  ? -3.166  0.381   42.729  1.00 11.48  ? 90  GLU F C   1 
ATOM   10681 O O   . GLU F  2 90  ? -2.569  0.086   41.689  1.00 11.22  ? 90  GLU F O   1 
ATOM   10682 C CB  . GLU F  2 90  ? -2.379  -0.777  44.816  1.00 11.72  ? 90  GLU F CB  1 
ATOM   10683 C CG  . GLU F  2 90  ? -1.633  -1.911  44.122  1.00 13.36  ? 90  GLU F CG  1 
ATOM   10684 C CD  . GLU F  2 90  ? -1.612  -3.193  44.941  1.00 17.90  ? 90  GLU F CD  1 
ATOM   10685 O OE1 . GLU F  2 90  ? -2.685  -3.621  45.427  1.00 14.04  ? 90  GLU F OE1 1 
ATOM   10686 O OE2 . GLU F  2 90  ? -0.517  -3.779  45.090  1.00 21.37  ? 90  GLU F OE2 1 
ATOM   10687 N N   . ILE F  2 91  ? -4.481  0.574   42.778  1.00 10.80  ? 91  ILE F N   1 
ATOM   10688 C CA  . ILE F  2 91  ? -5.327  0.402   41.602  1.00 10.13  ? 91  ILE F CA  1 
ATOM   10689 C C   . ILE F  2 91  ? -5.204  1.588   40.645  1.00 10.44  ? 91  ILE F C   1 
ATOM   10690 O O   . ILE F  2 91  ? -5.003  1.406   39.439  1.00 9.84   ? 91  ILE F O   1 
ATOM   10691 C CB  . ILE F  2 91  ? -6.794  0.130   42.004  1.00 10.07  ? 91  ILE F CB  1 
ATOM   10692 C CG1 . ILE F  2 91  ? -6.919  -1.310  42.510  1.00 13.02  ? 91  ILE F CG1 1 
ATOM   10693 C CG2 . ILE F  2 91  ? -7.734  0.325   40.826  1.00 10.53  ? 91  ILE F CG2 1 
ATOM   10694 C CD1 . ILE F  2 91  ? -8.135  -1.587  43.371  1.00 10.30  ? 91  ILE F CD1 1 
ATOM   10695 N N   . TRP F  2 92  ? -5.307  2.801   41.184  1.00 10.56  ? 92  TRP F N   1 
ATOM   10696 C CA  . TRP F  2 92  ? -5.212  3.999   40.359  1.00 10.29  ? 92  TRP F CA  1 
ATOM   10697 C C   . TRP F  2 92  ? -3.806  4.197   39.792  1.00 10.95  ? 92  TRP F C   1 
ATOM   10698 O O   . TRP F  2 92  ? -3.664  4.640   38.647  1.00 11.63  ? 92  TRP F O   1 
ATOM   10699 C CB  . TRP F  2 92  ? -5.713  5.233   41.109  1.00 9.24   ? 92  TRP F CB  1 
ATOM   10700 C CG  . TRP F  2 92  ? -7.207  5.241   41.234  1.00 11.11  ? 92  TRP F CG  1 
ATOM   10701 C CD1 . TRP F  2 92  ? -7.934  5.058   42.373  1.00 10.99  ? 92  TRP F CD1 1 
ATOM   10702 C CD2 . TRP F  2 92  ? -8.162  5.410   40.172  1.00 9.81   ? 92  TRP F CD2 1 
ATOM   10703 N NE1 . TRP F  2 92  ? -9.278  5.118   42.092  1.00 10.17  ? 92  TRP F NE1 1 
ATOM   10704 C CE2 . TRP F  2 92  ? -9.445  5.333   40.749  1.00 10.31  ? 92  TRP F CE2 1 
ATOM   10705 C CE3 . TRP F  2 92  ? -8.053  5.628   38.792  1.00 10.50  ? 92  TRP F CE3 1 
ATOM   10706 C CZ2 . TRP F  2 92  ? -10.616 5.464   39.995  1.00 13.31  ? 92  TRP F CZ2 1 
ATOM   10707 C CZ3 . TRP F  2 92  ? -9.214  5.754   38.042  1.00 10.92  ? 92  TRP F CZ3 1 
ATOM   10708 C CH2 . TRP F  2 92  ? -10.480 5.670   38.646  1.00 11.64  ? 92  TRP F CH2 1 
ATOM   10709 N N   . SER F  2 93  ? -2.780  3.847   40.572  1.00 9.46   ? 93  SER F N   1 
ATOM   10710 C CA  . SER F  2 93  ? -1.405  3.916   40.083  1.00 8.93   ? 93  SER F CA  1 
ATOM   10711 C C   . SER F  2 93  ? -1.215  3.010   38.866  1.00 9.07   ? 93  SER F C   1 
ATOM   10712 O O   . SER F  2 93  ? -0.595  3.412   37.877  1.00 8.76   ? 93  SER F O   1 
ATOM   10713 C CB  . SER F  2 93  ? -0.403  3.568   41.182  1.00 8.98   ? 93  SER F CB  1 
ATOM   10714 O OG  . SER F  2 93  ? -0.420  4.540   42.214  1.00 7.69   ? 93  SER F OG  1 
ATOM   10715 N N   . TYR F  2 94  ? -1.767  1.799   38.942  1.00 8.82   ? 94  TYR F N   1 
ATOM   10716 C CA  . TYR F  2 94  ? -1.780  0.873   37.811  1.00 8.46   ? 94  TYR F CA  1 
ATOM   10717 C C   . TYR F  2 94  ? -2.570  1.461   36.633  1.00 8.91   ? 94  TYR F C   1 
ATOM   10718 O O   . TYR F  2 94  ? -2.035  1.581   35.532  1.00 9.36   ? 94  TYR F O   1 
ATOM   10719 C CB  . TYR F  2 94  ? -2.327  -0.495  38.240  1.00 7.75   ? 94  TYR F CB  1 
ATOM   10720 C CG  . TYR F  2 94  ? -2.668  -1.435  37.101  1.00 8.30   ? 94  TYR F CG  1 
ATOM   10721 C CD1 . TYR F  2 94  ? -1.729  -2.340  36.611  1.00 8.87   ? 94  TYR F CD1 1 
ATOM   10722 C CD2 . TYR F  2 94  ? -3.939  -1.427  36.523  1.00 7.61   ? 94  TYR F CD2 1 
ATOM   10723 C CE1 . TYR F  2 94  ? -2.043  -3.206  35.570  1.00 8.17   ? 94  TYR F CE1 1 
ATOM   10724 C CE2 . TYR F  2 94  ? -4.259  -2.278  35.483  1.00 8.17   ? 94  TYR F CE2 1 
ATOM   10725 C CZ  . TYR F  2 94  ? -3.311  -3.169  35.009  1.00 10.13  ? 94  TYR F CZ  1 
ATOM   10726 O OH  . TYR F  2 94  ? -3.637  -4.017  33.971  1.00 11.72  ? 94  TYR F OH  1 
ATOM   10727 N N   . ASN F  2 95  ? -3.827  1.834   36.874  1.00 9.74   ? 95  ASN F N   1 
ATOM   10728 C CA  . ASN F  2 95  ? -4.687  2.430   35.843  1.00 10.56  ? 95  ASN F CA  1 
ATOM   10729 C C   . ASN F  2 95  ? -4.019  3.583   35.112  1.00 10.35  ? 95  ASN F C   1 
ATOM   10730 O O   . ASN F  2 95  ? -4.059  3.650   33.886  1.00 11.15  ? 95  ASN F O   1 
ATOM   10731 C CB  . ASN F  2 95  ? -6.013  2.919   36.445  1.00 10.84  ? 95  ASN F CB  1 
ATOM   10732 C CG  . ASN F  2 95  ? -6.966  1.786   36.779  1.00 13.89  ? 95  ASN F CG  1 
ATOM   10733 O OD1 . ASN F  2 95  ? -6.661  0.607   36.577  1.00 18.16  ? 95  ASN F OD1 1 
ATOM   10734 N ND2 . ASN F  2 95  ? -8.133  2.142   37.296  1.00 17.32  ? 95  ASN F ND2 1 
ATOM   10735 N N   . ALA F  2 96  ? -3.405  4.477   35.885  1.00 10.11  ? 96  ALA F N   1 
ATOM   10736 C CA  . ALA F  2 96  ? -2.744  5.673   35.371  1.00 9.59   ? 96  ALA F CA  1 
ATOM   10737 C C   . ALA F  2 96  ? -1.527  5.341   34.516  1.00 10.28  ? 96  ALA F C   1 
ATOM   10738 O O   . ALA F  2 96  ? -1.357  5.894   33.431  1.00 10.21  ? 96  ALA F O   1 
ATOM   10739 C CB  . ALA F  2 96  ? -2.343  6.572   36.522  1.00 8.89   ? 96  ALA F CB  1 
ATOM   10740 N N   . GLU F  2 97  ? -0.685  4.440   35.019  1.00 11.65  ? 97  GLU F N   1 
ATOM   10741 C CA  . GLU F  2 97  ? 0.507   3.990   34.309  1.00 13.26  ? 97  GLU F CA  1 
ATOM   10742 C C   . GLU F  2 97  ? 0.125   3.320   32.991  1.00 13.57  ? 97  GLU F C   1 
ATOM   10743 O O   . GLU F  2 97  ? 0.748   3.576   31.953  1.00 14.42  ? 97  GLU F O   1 
ATOM   10744 C CB  . GLU F  2 97  ? 1.305   3.012   35.181  1.00 14.08  ? 97  GLU F CB  1 
ATOM   10745 C CG  . GLU F  2 97  ? 2.685   2.635   34.635  1.00 18.37  ? 97  GLU F CG  1 
ATOM   10746 C CD  . GLU F  2 97  ? 3.823   3.381   35.306  1.00 22.67  ? 97  GLU F CD  1 
ATOM   10747 O OE1 . GLU F  2 97  ? 3.933   3.324   36.552  1.00 22.50  ? 97  GLU F OE1 1 
ATOM   10748 O OE2 . GLU F  2 97  ? 4.625   4.008   34.581  1.00 26.23  ? 97  GLU F OE2 1 
ATOM   10749 N N   . LEU F  2 98  ? -0.903  2.472   33.039  1.00 12.56  ? 98  LEU F N   1 
ATOM   10750 C CA  . LEU F  2 98  ? -1.361  1.748   31.864  1.00 12.30  ? 98  LEU F CA  1 
ATOM   10751 C C   . LEU F  2 98  ? -2.036  2.679   30.866  1.00 13.06  ? 98  LEU F C   1 
ATOM   10752 O O   . LEU F  2 98  ? -1.804  2.563   29.663  1.00 12.87  ? 98  LEU F O   1 
ATOM   10753 C CB  . LEU F  2 98  ? -2.304  0.606   32.257  1.00 12.34  ? 98  LEU F CB  1 
ATOM   10754 C CG  . LEU F  2 98  ? -2.882  -0.266  31.136  1.00 11.00  ? 98  LEU F CG  1 
ATOM   10755 C CD1 . LEU F  2 98  ? -1.790  -1.049  30.419  1.00 11.85  ? 98  LEU F CD1 1 
ATOM   10756 C CD2 . LEU F  2 98  ? -3.938  -1.201  31.689  1.00 11.27  ? 98  LEU F CD2 1 
ATOM   10757 N N   . LEU F  2 99  ? -2.867  3.593   31.370  1.00 13.43  ? 99  LEU F N   1 
ATOM   10758 C CA  . LEU F  2 99  ? -3.553  4.564   30.526  1.00 13.70  ? 99  LEU F CA  1 
ATOM   10759 C C   . LEU F  2 99  ? -2.556  5.359   29.692  1.00 14.19  ? 99  LEU F C   1 
ATOM   10760 O O   . LEU F  2 99  ? -2.683  5.440   28.470  1.00 14.64  ? 99  LEU F O   1 
ATOM   10761 C CB  . LEU F  2 99  ? -4.413  5.518   31.363  1.00 13.54  ? 99  LEU F CB  1 
ATOM   10762 C CG  . LEU F  2 99  ? -5.171  6.619   30.608  1.00 13.35  ? 99  LEU F CG  1 
ATOM   10763 C CD1 . LEU F  2 99  ? -6.254  6.025   29.721  1.00 11.60  ? 99  LEU F CD1 1 
ATOM   10764 C CD2 . LEU F  2 99  ? -5.770  7.627   31.572  1.00 11.76  ? 99  LEU F CD2 1 
ATOM   10765 N N   . VAL F  2 100 ? -1.557  5.925   30.359  1.00 13.70  ? 100 VAL F N   1 
ATOM   10766 C CA  . VAL F  2 100 ? -0.574  6.766   29.689  1.00 13.56  ? 100 VAL F CA  1 
ATOM   10767 C C   . VAL F  2 100 ? 0.272   5.950   28.708  1.00 13.88  ? 100 VAL F C   1 
ATOM   10768 O O   . VAL F  2 100 ? 0.515   6.393   27.586  1.00 14.64  ? 100 VAL F O   1 
ATOM   10769 C CB  . VAL F  2 100 ? 0.308   7.533   30.703  1.00 13.12  ? 100 VAL F CB  1 
ATOM   10770 C CG1 . VAL F  2 100 ? 1.316   8.393   29.988  1.00 13.59  ? 100 VAL F CG1 1 
ATOM   10771 C CG2 . VAL F  2 100 ? -0.554  8.407   31.597  1.00 11.40  ? 100 VAL F CG2 1 
ATOM   10772 N N   . ALA F  2 101 ? 0.697   4.758   29.123  1.00 13.63  ? 101 ALA F N   1 
ATOM   10773 C CA  . ALA F  2 101 ? 1.479   3.877   28.254  1.00 13.63  ? 101 ALA F CA  1 
ATOM   10774 C C   . ALA F  2 101 ? 0.705   3.506   26.987  1.00 14.36  ? 101 ALA F C   1 
ATOM   10775 O O   . ALA F  2 101 ? 1.221   3.646   25.879  1.00 15.00  ? 101 ALA F O   1 
ATOM   10776 C CB  . ALA F  2 101 ? 1.923   2.629   29.006  1.00 12.92  ? 101 ALA F CB  1 
ATOM   10777 N N   . MET F  2 102 ? -0.535  3.051   27.160  1.00 15.03  ? 102 MET F N   1 
ATOM   10778 C CA  . MET F  2 102 ? -1.400  2.681   26.046  1.00 16.06  ? 102 MET F CA  1 
ATOM   10779 C C   . MET F  2 102 ? -1.659  3.867   25.115  1.00 16.17  ? 102 MET F C   1 
ATOM   10780 O O   . MET F  2 102 ? -1.510  3.747   23.895  1.00 16.73  ? 102 MET F O   1 
ATOM   10781 C CB  . MET F  2 102 ? -2.720  2.119   26.571  1.00 17.23  ? 102 MET F CB  1 
ATOM   10782 C CG  . MET F  2 102 ? -3.676  1.629   25.503  1.00 21.65  ? 102 MET F CG  1 
ATOM   10783 S SD  . MET F  2 102 ? -5.392  1.841   26.010  1.00 34.93  ? 102 MET F SD  1 
ATOM   10784 C CE  . MET F  2 102 ? -5.663  3.563   25.595  1.00 32.66  ? 102 MET F CE  1 
ATOM   10785 N N   . GLU F  2 103 ? -2.034  5.007   25.694  1.00 15.26  ? 103 GLU F N   1 
ATOM   10786 C CA  . GLU F  2 103 ? -2.288  6.217   24.916  1.00 15.06  ? 103 GLU F CA  1 
ATOM   10787 C C   . GLU F  2 103 ? -1.062  6.644   24.109  1.00 14.96  ? 103 GLU F C   1 
ATOM   10788 O O   . GLU F  2 103 ? -1.180  6.981   22.932  1.00 15.30  ? 103 GLU F O   1 
ATOM   10789 C CB  . GLU F  2 103 ? -2.754  7.367   25.815  1.00 16.00  ? 103 GLU F CB  1 
ATOM   10790 C CG  . GLU F  2 103 ? -4.138  7.189   26.462  1.00 19.13  ? 103 GLU F CG  1 
ATOM   10791 C CD  . GLU F  2 103 ? -5.302  7.416   25.510  1.00 24.57  ? 103 GLU F CD  1 
ATOM   10792 O OE1 . GLU F  2 103 ? -5.105  7.394   24.277  1.00 29.55  ? 103 GLU F OE1 1 
ATOM   10793 O OE2 . GLU F  2 103 ? -6.430  7.609   26.001  1.00 25.98  ? 103 GLU F OE2 1 
ATOM   10794 N N   . ASN F  2 104 ? 0.111   6.618   24.738  1.00 14.62  ? 104 ASN F N   1 
ATOM   10795 C CA  . ASN F  2 104 ? 1.344   7.021   24.064  1.00 14.29  ? 104 ASN F CA  1 
ATOM   10796 C C   . ASN F  2 104 ? 1.703   6.113   22.890  1.00 14.55  ? 104 ASN F C   1 
ATOM   10797 O O   . ASN F  2 104 ? 2.136   6.593   21.839  1.00 15.29  ? 104 ASN F O   1 
ATOM   10798 C CB  . ASN F  2 104 ? 2.504   7.105   25.054  1.00 14.40  ? 104 ASN F CB  1 
ATOM   10799 C CG  . ASN F  2 104 ? 2.333   8.222   26.073  1.00 13.79  ? 104 ASN F CG  1 
ATOM   10800 O OD1 . ASN F  2 104 ? 1.501   9.117   25.914  1.00 12.25  ? 104 ASN F OD1 1 
ATOM   10801 N ND2 . ASN F  2 104 ? 3.130   8.170   27.132  1.00 16.30  ? 104 ASN F ND2 1 
ATOM   10802 N N   . GLN F  2 105 ? 1.510   4.807   23.074  1.00 14.07  ? 105 GLN F N   1 
ATOM   10803 C CA  . GLN F  2 105 ? 1.697   3.824   22.008  1.00 13.60  ? 105 GLN F CA  1 
ATOM   10804 C C   . GLN F  2 105 ? 0.857   4.199   20.797  1.00 14.08  ? 105 GLN F C   1 
ATOM   10805 O O   . GLN F  2 105 ? 1.354   4.222   19.666  1.00 14.49  ? 105 GLN F O   1 
ATOM   10806 C CB  . GLN F  2 105 ? 1.282   2.432   22.491  1.00 13.60  ? 105 GLN F CB  1 
ATOM   10807 C CG  . GLN F  2 105 ? 1.664   1.294   21.551  1.00 11.09  ? 105 GLN F CG  1 
ATOM   10808 C CD  . GLN F  2 105 ? 3.150   0.992   21.585  1.00 12.41  ? 105 GLN F CD  1 
ATOM   10809 O OE1 . GLN F  2 105 ? 3.738   0.840   22.659  1.00 10.92  ? 105 GLN F OE1 1 
ATOM   10810 N NE2 . GLN F  2 105 ? 3.766   0.902   20.410  1.00 10.23  ? 105 GLN F NE2 1 
ATOM   10811 N N   . HIS F  2 106 ? -0.414  4.498   21.060  1.00 13.92  ? 106 HIS F N   1 
ATOM   10812 C CA  . HIS F  2 106 ? -1.388  4.825   20.029  1.00 13.50  ? 106 HIS F CA  1 
ATOM   10813 C C   . HIS F  2 106 ? -1.053  6.135   19.318  1.00 13.78  ? 106 HIS F C   1 
ATOM   10814 O O   . HIS F  2 106 ? -1.018  6.180   18.088  1.00 13.86  ? 106 HIS F O   1 
ATOM   10815 C CB  . HIS F  2 106 ? -2.790  4.876   20.638  1.00 13.08  ? 106 HIS F CB  1 
ATOM   10816 C CG  . HIS F  2 106 ? -3.863  5.216   19.654  1.00 13.01  ? 106 HIS F CG  1 
ATOM   10817 N ND1 . HIS F  2 106 ? -4.588  6.384   19.721  1.00 15.68  ? 106 HIS F ND1 1 
ATOM   10818 C CD2 . HIS F  2 106 ? -4.334  4.542   18.579  1.00 13.87  ? 106 HIS F CD2 1 
ATOM   10819 C CE1 . HIS F  2 106 ? -5.463  6.416   18.732  1.00 15.48  ? 106 HIS F CE1 1 
ATOM   10820 N NE2 . HIS F  2 106 ? -5.328  5.310   18.023  1.00 16.68  ? 106 HIS F NE2 1 
ATOM   10821 N N   . THR F  2 107 ? -0.796  7.184   20.102  1.00 13.75  ? 107 THR F N   1 
ATOM   10822 C CA  . THR F  2 107 ? -0.424  8.508   19.589  1.00 12.76  ? 107 THR F CA  1 
ATOM   10823 C C   . THR F  2 107 ? 0.748   8.441   18.604  1.00 13.77  ? 107 THR F C   1 
ATOM   10824 O O   . THR F  2 107 ? 0.718   9.078   17.549  1.00 14.04  ? 107 THR F O   1 
ATOM   10825 C CB  . THR F  2 107 ? -0.080  9.470   20.749  1.00 12.00  ? 107 THR F CB  1 
ATOM   10826 O OG1 . THR F  2 107 ? -1.210  9.591   21.616  1.00 7.80   ? 107 THR F OG1 1 
ATOM   10827 C CG2 . THR F  2 107 ? 0.293   10.848  20.229  1.00 10.83  ? 107 THR F CG2 1 
ATOM   10828 N N   . ILE F  2 108 ? 1.771   7.664   18.952  1.00 14.17  ? 108 ILE F N   1 
ATOM   10829 C CA  . ILE F  2 108 ? 2.917   7.462   18.069  1.00 14.64  ? 108 ILE F CA  1 
ATOM   10830 C C   . ILE F  2 108 ? 2.494   6.752   16.775  1.00 15.70  ? 108 ILE F C   1 
ATOM   10831 O O   . ILE F  2 108 ? 2.841   7.195   15.675  1.00 16.39  ? 108 ILE F O   1 
ATOM   10832 C CB  . ILE F  2 108 ? 4.076   6.725   18.792  1.00 14.18  ? 108 ILE F CB  1 
ATOM   10833 C CG1 . ILE F  2 108 ? 4.705   7.655   19.828  1.00 12.04  ? 108 ILE F CG1 1 
ATOM   10834 C CG2 . ILE F  2 108 ? 5.148   6.272   17.809  1.00 11.38  ? 108 ILE F CG2 1 
ATOM   10835 C CD1 . ILE F  2 108 ? 5.297   6.940   21.008  1.00 13.64  ? 108 ILE F CD1 1 
ATOM   10836 N N   . ASP F  2 109 ? 1.724   5.675   16.912  1.00 15.77  ? 109 ASP F N   1 
ATOM   10837 C CA  . ASP F  2 109 ? 1.243   4.921   15.757  1.00 16.10  ? 109 ASP F CA  1 
ATOM   10838 C C   . ASP F  2 109 ? 0.267   5.729   14.898  1.00 16.46  ? 109 ASP F C   1 
ATOM   10839 O O   . ASP F  2 109 ? 0.264   5.617   13.669  1.00 16.50  ? 109 ASP F O   1 
ATOM   10840 C CB  . ASP F  2 109 ? 0.622   3.598   16.208  1.00 16.02  ? 109 ASP F CB  1 
ATOM   10841 C CG  . ASP F  2 109 ? 1.661   2.616   16.733  1.00 18.36  ? 109 ASP F CG  1 
ATOM   10842 O OD1 . ASP F  2 109 ? 1.329   1.825   17.640  1.00 17.92  ? 109 ASP F OD1 1 
ATOM   10843 O OD2 . ASP F  2 109 ? 2.815   2.633   16.242  1.00 21.68  ? 109 ASP F OD2 1 
ATOM   10844 N N   . LEU F  2 110 ? -0.546  6.546   15.559  1.00 16.48  ? 110 LEU F N   1 
ATOM   10845 C CA  . LEU F  2 110 ? -1.509  7.417   14.900  1.00 16.62  ? 110 LEU F CA  1 
ATOM   10846 C C   . LEU F  2 110 ? -0.798  8.438   14.008  1.00 16.93  ? 110 LEU F C   1 
ATOM   10847 O O   . LEU F  2 110 ? -1.166  8.620   12.843  1.00 17.49  ? 110 LEU F O   1 
ATOM   10848 C CB  . LEU F  2 110 ? -2.369  8.094   15.971  1.00 17.12  ? 110 LEU F CB  1 
ATOM   10849 C CG  . LEU F  2 110 ? -3.262  9.322   15.795  1.00 20.00  ? 110 LEU F CG  1 
ATOM   10850 C CD1 . LEU F  2 110 ? -4.178  9.399   17.006  1.00 21.08  ? 110 LEU F CD1 1 
ATOM   10851 C CD2 . LEU F  2 110 ? -2.462  10.615  15.668  1.00 19.81  ? 110 LEU F CD2 1 
ATOM   10852 N N   . ALA F  2 111 ? 0.225   9.088   14.559  1.00 16.22  ? 111 ALA F N   1 
ATOM   10853 C CA  . ALA F  2 111 ? 1.011   10.078  13.829  1.00 15.64  ? 111 ALA F CA  1 
ATOM   10854 C C   . ALA F  2 111 ? 1.715   9.457   12.621  1.00 15.37  ? 111 ALA F C   1 
ATOM   10855 O O   . ALA F  2 111 ? 1.709   10.022  11.521  1.00 15.62  ? 111 ALA F O   1 
ATOM   10856 C CB  . ALA F  2 111 ? 2.016   10.724  14.753  1.00 15.48  ? 111 ALA F CB  1 
ATOM   10857 N N   . ASP F  2 112 ? 2.308   8.287   12.849  1.00 14.59  ? 112 ASP F N   1 
ATOM   10858 C CA  . ASP F  2 112 ? 2.975   7.495   11.826  1.00 13.98  ? 112 ASP F CA  1 
ATOM   10859 C C   . ASP F  2 112 ? 2.004   7.172   10.688  1.00 13.51  ? 112 ASP F C   1 
ATOM   10860 O O   . ASP F  2 112 ? 2.341   7.317   9.512   1.00 13.52  ? 112 ASP F O   1 
ATOM   10861 C CB  . ASP F  2 112 ? 3.513   6.212   12.468  1.00 14.10  ? 112 ASP F CB  1 
ATOM   10862 C CG  . ASP F  2 112 ? 4.357   5.379   11.525  1.00 15.82  ? 112 ASP F CG  1 
ATOM   10863 O OD1 . ASP F  2 112 ? 4.933   5.926   10.564  1.00 16.89  ? 112 ASP F OD1 1 
ATOM   10864 O OD2 . ASP F  2 112 ? 4.455   4.160   11.765  1.00 21.63  ? 112 ASP F OD2 1 
ATOM   10865 N N   . SER F  2 113 ? 0.796   6.754   11.061  1.00 13.00  ? 113 SER F N   1 
ATOM   10866 C CA  . SER F  2 113 ? -0.292  6.490   10.127  1.00 12.14  ? 113 SER F CA  1 
ATOM   10867 C C   . SER F  2 113 ? -0.565  7.670   9.188   1.00 12.46  ? 113 SER F C   1 
ATOM   10868 O O   . SER F  2 113 ? -0.665  7.481   7.978   1.00 11.65  ? 113 SER F O   1 
ATOM   10869 C CB  . SER F  2 113 ? -1.562  6.125   10.903  1.00 11.60  ? 113 SER F CB  1 
ATOM   10870 O OG  . SER F  2 113 ? -2.682  5.999   10.047  1.00 10.46  ? 113 SER F OG  1 
ATOM   10871 N N   . GLU F  2 114 ? -0.678  8.876   9.753   1.00 13.45  ? 114 GLU F N   1 
ATOM   10872 C CA  . GLU F  2 114 ? -0.974  10.088  8.979   1.00 13.78  ? 114 GLU F CA  1 
ATOM   10873 C C   . GLU F  2 114 ? 0.086   10.369  7.920   1.00 13.86  ? 114 GLU F C   1 
ATOM   10874 O O   . GLU F  2 114 ? -0.237  10.772  6.798   1.00 12.83  ? 114 GLU F O   1 
ATOM   10875 C CB  . GLU F  2 114 ? -1.126  11.305  9.893   1.00 13.71  ? 114 GLU F CB  1 
ATOM   10876 C CG  . GLU F  2 114 ? -2.362  11.282  10.789  1.00 17.38  ? 114 GLU F CG  1 
ATOM   10877 C CD  . GLU F  2 114 ? -3.678  11.182  10.024  1.00 19.02  ? 114 GLU F CD  1 
ATOM   10878 O OE1 . GLU F  2 114 ? -3.809  11.780  8.930   1.00 19.13  ? 114 GLU F OE1 1 
ATOM   10879 O OE2 . GLU F  2 114 ? -4.591  10.499  10.534  1.00 21.00  ? 114 GLU F OE2 1 
ATOM   10880 N N   . MET F  2 115 ? 1.346   10.153  8.294   1.00 14.32  ? 115 MET F N   1 
ATOM   10881 C CA  . MET F  2 115 ? 2.475   10.301  7.385   1.00 14.73  ? 115 MET F CA  1 
ATOM   10882 C C   . MET F  2 115 ? 2.321   9.344   6.205   1.00 15.78  ? 115 MET F C   1 
ATOM   10883 O O   . MET F  2 115 ? 2.431   9.752   5.047   1.00 16.92  ? 115 MET F O   1 
ATOM   10884 C CB  . MET F  2 115 ? 3.783   10.034  8.134   1.00 14.13  ? 115 MET F CB  1 
ATOM   10885 C CG  . MET F  2 115 ? 5.054   10.214  7.321   1.00 14.29  ? 115 MET F CG  1 
ATOM   10886 S SD  . MET F  2 115 ? 5.449   11.926  6.916   1.00 12.41  ? 115 MET F SD  1 
ATOM   10887 C CE  . MET F  2 115 ? 4.779   12.060  5.256   1.00 11.04  ? 115 MET F CE  1 
ATOM   10888 N N   . SER F  2 116 ? 2.044   8.079   6.512   1.00 16.03  ? 116 SER F N   1 
ATOM   10889 C CA  . SER F  2 116 ? 1.873   7.048   5.499   1.00 16.15  ? 116 SER F CA  1 
ATOM   10890 C C   . SER F  2 116 ? 0.707   7.365   4.556   1.00 16.70  ? 116 SER F C   1 
ATOM   10891 O O   . SER F  2 116 ? 0.844   7.244   3.336   1.00 16.64  ? 116 SER F O   1 
ATOM   10892 C CB  . SER F  2 116 ? 1.678   5.685   6.160   1.00 15.44  ? 116 SER F CB  1 
ATOM   10893 O OG  . SER F  2 116 ? 1.502   4.673   5.187   1.00 18.96  ? 116 SER F OG  1 
ATOM   10894 N N   . LYS F  2 117 ? -0.423  7.787   5.126   1.00 16.59  ? 117 LYS F N   1 
ATOM   10895 C CA  . LYS F  2 117 ? -1.618  8.137   4.352   1.00 16.33  ? 117 LYS F CA  1 
ATOM   10896 C C   . LYS F  2 117 ? -1.347  9.262   3.364   1.00 16.15  ? 117 LYS F C   1 
ATOM   10897 O O   . LYS F  2 117 ? -1.853  9.245   2.241   1.00 16.19  ? 117 LYS F O   1 
ATOM   10898 C CB  . LYS F  2 117 ? -2.773  8.529   5.274   1.00 15.72  ? 117 LYS F CB  1 
ATOM   10899 C CG  . LYS F  2 117 ? -3.313  7.376   6.101   1.00 18.52  ? 117 LYS F CG  1 
ATOM   10900 C CD  . LYS F  2 117 ? -4.653  7.701   6.735   1.00 22.18  ? 117 LYS F CD  1 
ATOM   10901 C CE  . LYS F  2 117 ? -4.514  8.609   7.940   1.00 21.97  ? 117 LYS F CE  1 
ATOM   10902 N NZ  . LYS F  2 117 ? -5.825  8.829   8.608   1.00 20.66  ? 117 LYS F NZ  1 
ATOM   10903 N N   . LEU F  2 118 ? -0.544  10.231  3.797   1.00 15.94  ? 118 LEU F N   1 
ATOM   10904 C CA  . LEU F  2 118 ? -0.162  11.365  2.965   1.00 15.94  ? 118 LEU F CA  1 
ATOM   10905 C C   . LEU F  2 118 ? 0.783   10.917  1.854   1.00 15.89  ? 118 LEU F C   1 
ATOM   10906 O O   . LEU F  2 118 ? 0.641   11.332  0.701   1.00 16.25  ? 118 LEU F O   1 
ATOM   10907 C CB  . LEU F  2 118 ? 0.487   12.460  3.818   1.00 15.61  ? 118 LEU F CB  1 
ATOM   10908 C CG  . LEU F  2 118 ? 0.988   13.731  3.129   1.00 15.19  ? 118 LEU F CG  1 
ATOM   10909 C CD1 . LEU F  2 118 ? -0.121  14.455  2.371   1.00 16.88  ? 118 LEU F CD1 1 
ATOM   10910 C CD2 . LEU F  2 118 ? 1.640   14.656  4.139   1.00 18.61  ? 118 LEU F CD2 1 
ATOM   10911 N N   . TYR F  2 119 ? 1.740   10.068  2.213   1.00 14.89  ? 119 TYR F N   1 
ATOM   10912 C CA  . TYR F  2 119 ? 2.672   9.487   1.256   1.00 14.39  ? 119 TYR F CA  1 
ATOM   10913 C C   . TYR F  2 119 ? 1.931   8.640   0.208   1.00 14.41  ? 119 TYR F C   1 
ATOM   10914 O O   . TYR F  2 119 ? 2.235   8.721   -0.983  1.00 13.64  ? 119 TYR F O   1 
ATOM   10915 C CB  . TYR F  2 119 ? 3.727   8.673   2.009   1.00 13.72  ? 119 TYR F CB  1 
ATOM   10916 C CG  . TYR F  2 119 ? 4.725   7.931   1.155   1.00 13.26  ? 119 TYR F CG  1 
ATOM   10917 C CD1 . TYR F  2 119 ? 5.900   8.548   0.718   1.00 15.43  ? 119 TYR F CD1 1 
ATOM   10918 C CD2 . TYR F  2 119 ? 4.516   6.597   0.813   1.00 12.95  ? 119 TYR F CD2 1 
ATOM   10919 C CE1 . TYR F  2 119 ? 6.832   7.855   -0.059  1.00 15.06  ? 119 TYR F CE1 1 
ATOM   10920 C CE2 . TYR F  2 119 ? 5.437   5.896   0.039   1.00 14.79  ? 119 TYR F CE2 1 
ATOM   10921 C CZ  . TYR F  2 119 ? 6.589   6.529   -0.394  1.00 15.23  ? 119 TYR F CZ  1 
ATOM   10922 O OH  . TYR F  2 119 ? 7.492   5.828   -1.157  1.00 15.00  ? 119 TYR F OH  1 
ATOM   10923 N N   . GLU F  2 120 ? 0.952   7.851   0.655   1.00 14.73  ? 120 GLU F N   1 
ATOM   10924 C CA  . GLU F  2 120 ? 0.151   7.017   -0.245  1.00 15.52  ? 120 GLU F CA  1 
ATOM   10925 C C   . GLU F  2 120 ? -0.764  7.853   -1.137  1.00 15.98  ? 120 GLU F C   1 
ATOM   10926 O O   . GLU F  2 120 ? -0.956  7.534   -2.314  1.00 16.63  ? 120 GLU F O   1 
ATOM   10927 C CB  . GLU F  2 120 ? -0.669  5.978   0.532   1.00 15.29  ? 120 GLU F CB  1 
ATOM   10928 C CG  . GLU F  2 120 ? 0.145   4.831   1.129   1.00 17.67  ? 120 GLU F CG  1 
ATOM   10929 C CD  . GLU F  2 120 ? 0.810   3.936   0.090   1.00 22.87  ? 120 GLU F CD  1 
ATOM   10930 O OE1 . GLU F  2 120 ? 1.911   3.414   0.385   1.00 23.56  ? 120 GLU F OE1 1 
ATOM   10931 O OE2 . GLU F  2 120 ? 0.240   3.751   -1.013  1.00 24.95  ? 120 GLU F OE2 1 
ATOM   10932 N N   . ARG F  2 121 ? -1.328  8.917   -0.573  1.00 16.14  ? 121 ARG F N   1 
ATOM   10933 C CA  . ARG F  2 121 ? -2.104  9.880   -1.345  1.00 16.40  ? 121 ARG F CA  1 
ATOM   10934 C C   . ARG F  2 121 ? -1.261  10.344  -2.540  1.00 15.64  ? 121 ARG F C   1 
ATOM   10935 O O   . ARG F  2 121 ? -1.682  10.217  -3.692  1.00 15.74  ? 121 ARG F O   1 
ATOM   10936 C CB  . ARG F  2 121 ? -2.526  11.046  -0.439  1.00 16.60  ? 121 ARG F CB  1 
ATOM   10937 C CG  . ARG F  2 121 ? -3.153  12.265  -1.115  1.00 21.19  ? 121 ARG F CG  1 
ATOM   10938 C CD  . ARG F  2 121 ? -3.490  13.321  -0.044  1.00 29.49  ? 121 ARG F CD  1 
ATOM   10939 N NE  . ARG F  2 121 ? -3.279  14.728  -0.423  1.00 35.07  ? 121 ARG F NE  1 
ATOM   10940 C CZ  . ARG F  2 121 ? -2.363  15.191  -1.279  1.00 37.50  ? 121 ARG F CZ  1 
ATOM   10941 N NH1 . ARG F  2 121 ? -1.512  14.376  -1.896  1.00 39.29  ? 121 ARG F NH1 1 
ATOM   10942 N NH2 . ARG F  2 121 ? -2.295  16.495  -1.518  1.00 36.20  ? 121 ARG F NH2 1 
ATOM   10943 N N   . VAL F  2 122 ? -0.054  10.825  -2.255  1.00 14.85  ? 122 VAL F N   1 
ATOM   10944 C CA  . VAL F  2 122 ? 0.868   11.318  -3.279  1.00 14.49  ? 122 VAL F CA  1 
ATOM   10945 C C   . VAL F  2 122 ? 1.261   10.240  -4.295  1.00 14.69  ? 122 VAL F C   1 
ATOM   10946 O O   . VAL F  2 122 ? 1.392   10.529  -5.487  1.00 15.11  ? 122 VAL F O   1 
ATOM   10947 C CB  . VAL F  2 122 ? 2.128   11.966  -2.642  1.00 14.55  ? 122 VAL F CB  1 
ATOM   10948 C CG1 . VAL F  2 122 ? 3.118   12.413  -3.705  1.00 14.73  ? 122 VAL F CG1 1 
ATOM   10949 C CG2 . VAL F  2 122 ? 1.734   13.157  -1.781  1.00 12.62  ? 122 VAL F CG2 1 
ATOM   10950 N N   . LYS F  2 123 ? 1.434   9.003   -3.833  1.00 15.02  ? 123 LYS F N   1 
ATOM   10951 C CA  . LYS F  2 123 ? 1.774   7.897   -4.732  1.00 15.01  ? 123 LYS F CA  1 
ATOM   10952 C C   . LYS F  2 123 ? 0.692   7.691   -5.793  1.00 14.46  ? 123 LYS F C   1 
ATOM   10953 O O   . LYS F  2 123 ? 0.983   7.685   -6.992  1.00 14.22  ? 123 LYS F O   1 
ATOM   10954 C CB  . LYS F  2 123 ? 2.015   6.597   -3.958  1.00 15.15  ? 123 LYS F CB  1 
ATOM   10955 C CG  . LYS F  2 123 ? 2.594   5.478   -4.825  1.00 17.88  ? 123 LYS F CG  1 
ATOM   10956 C CD  . LYS F  2 123 ? 2.644   4.162   -4.075  1.00 23.72  ? 123 LYS F CD  1 
ATOM   10957 C CE  . LYS F  2 123 ? 3.124   3.034   -4.969  1.00 25.24  ? 123 LYS F CE  1 
ATOM   10958 N NZ  . LYS F  2 123 ? 3.338   1.780   -4.191  1.00 29.37  ? 123 LYS F NZ  1 
ATOM   10959 N N   . LYS F  2 124 ? -0.549  7.534   -5.337  1.00 13.88  ? 124 LYS F N   1 
ATOM   10960 C CA  . LYS F  2 124 ? -1.692  7.345   -6.225  1.00 13.72  ? 124 LYS F CA  1 
ATOM   10961 C C   . LYS F  2 124 ? -1.899  8.548   -7.135  1.00 14.22  ? 124 LYS F C   1 
ATOM   10962 O O   . LYS F  2 124 ? -2.317  8.406   -8.287  1.00 15.24  ? 124 LYS F O   1 
ATOM   10963 C CB  . LYS F  2 124 ? -2.959  7.068   -5.414  1.00 13.28  ? 124 LYS F CB  1 
ATOM   10964 C CG  . LYS F  2 124 ? -3.034  5.653   -4.886  1.00 13.21  ? 124 LYS F CG  1 
ATOM   10965 C CD  . LYS F  2 124 ? -4.030  5.517   -3.764  1.00 16.06  ? 124 LYS F CD  1 
ATOM   10966 C CE  . LYS F  2 124 ? -3.551  4.473   -2.766  1.00 21.01  ? 124 LYS F CE  1 
ATOM   10967 N NZ  . LYS F  2 124 ? -4.301  4.544   -1.485  1.00 25.71  ? 124 LYS F NZ  1 
ATOM   10968 N N   . GLN F  2 125 ? -1.590  9.728   -6.609  1.00 13.84  ? 125 GLN F N   1 
ATOM   10969 C CA  . GLN F  2 125 ? -1.711  10.975  -7.351  1.00 13.57  ? 125 GLN F CA  1 
ATOM   10970 C C   . GLN F  2 125 ? -0.759  10.994  -8.548  1.00 12.94  ? 125 GLN F C   1 
ATOM   10971 O O   . GLN F  2 125 ? -1.153  11.352  -9.658  1.00 13.26  ? 125 GLN F O   1 
ATOM   10972 C CB  . GLN F  2 125 ? -1.415  12.149  -6.420  1.00 13.39  ? 125 GLN F CB  1 
ATOM   10973 C CG  . GLN F  2 125 ? -2.094  13.452  -6.792  1.00 15.06  ? 125 GLN F CG  1 
ATOM   10974 C CD  . GLN F  2 125 ? -1.720  14.583  -5.844  1.00 19.52  ? 125 GLN F CD  1 
ATOM   10975 O OE1 . GLN F  2 125 ? -1.449  14.361  -4.658  1.00 20.61  ? 125 GLN F OE1 1 
ATOM   10976 N NE2 . GLN F  2 125 ? -1.700  15.805  -6.363  1.00 18.72  ? 125 GLN F NE2 1 
ATOM   10977 N N   . LEU F  2 126 ? 0.483   10.581  -8.318  1.00 12.04  ? 126 LEU F N   1 
ATOM   10978 C CA  . LEU F  2 126 ? 1.528   10.666  -9.334  1.00 11.09  ? 126 LEU F CA  1 
ATOM   10979 C C   . LEU F  2 126 ? 1.436   9.597   -10.422 1.00 11.27  ? 126 LEU F C   1 
ATOM   10980 O O   . LEU F  2 126 ? 2.097   9.710   -11.456 1.00 11.75  ? 126 LEU F O   1 
ATOM   10981 C CB  . LEU F  2 126 ? 2.909   10.649  -8.677  1.00 11.07  ? 126 LEU F CB  1 
ATOM   10982 C CG  . LEU F  2 126 ? 3.281   11.910  -7.891  1.00 11.10  ? 126 LEU F CG  1 
ATOM   10983 C CD1 . LEU F  2 126 ? 4.499   11.666  -7.019  1.00 5.40   ? 126 LEU F CD1 1 
ATOM   10984 C CD2 . LEU F  2 126 ? 3.514   13.089  -8.823  1.00 10.49  ? 126 LEU F CD2 1 
ATOM   10985 N N   . ARG F  2 127 ? 0.616   8.570   -10.187 1.00 10.92  ? 127 ARG F N   1 
ATOM   10986 C CA  . ARG F  2 127 ? 0.388   7.486   -11.153 1.00 9.82   ? 127 ARG F CA  1 
ATOM   10987 C C   . ARG F  2 127 ? 1.697   6.952   -11.738 1.00 9.57   ? 127 ARG F C   1 
ATOM   10988 O O   . ARG F  2 127 ? 2.629   6.643   -10.991 1.00 9.52   ? 127 ARG F O   1 
ATOM   10989 C CB  . ARG F  2 127 ? -0.567  7.933   -12.273 1.00 9.52   ? 127 ARG F CB  1 
ATOM   10990 C CG  . ARG F  2 127 ? -1.985  8.236   -11.825 1.00 8.26   ? 127 ARG F CG  1 
ATOM   10991 C CD  . ARG F  2 127 ? -2.759  6.971   -11.481 1.00 7.79   ? 127 ARG F CD  1 
ATOM   10992 N NE  . ARG F  2 127 ? -3.246  6.281   -12.673 1.00 9.21   ? 127 ARG F NE  1 
ATOM   10993 C CZ  . ARG F  2 127 ? -4.441  6.476   -13.228 1.00 8.60   ? 127 ARG F CZ  1 
ATOM   10994 N NH1 . ARG F  2 127 ? -5.296  7.346   -12.699 1.00 6.42   ? 127 ARG F NH1 1 
ATOM   10995 N NH2 . ARG F  2 127 ? -4.784  5.793   -14.316 1.00 3.63   ? 127 ARG F NH2 1 
ATOM   10996 N N   . GLU F  2 128 ? 1.763   6.875   -13.069 1.00 8.57   ? 128 GLU F N   1 
ATOM   10997 C CA  . GLU F  2 128 ? 2.931   6.349   -13.779 1.00 7.86   ? 128 GLU F CA  1 
ATOM   10998 C C   . GLU F  2 128 ? 3.935   7.448   -14.155 1.00 8.09   ? 128 GLU F C   1 
ATOM   10999 O O   . GLU F  2 128 ? 4.717   7.294   -15.094 1.00 8.19   ? 128 GLU F O   1 
ATOM   11000 C CB  . GLU F  2 128 ? 2.489   5.586   -15.032 1.00 7.45   ? 128 GLU F CB  1 
ATOM   11001 C CG  . GLU F  2 128 ? 1.510   4.446   -14.779 1.00 7.34   ? 128 GLU F CG  1 
ATOM   11002 C CD  . GLU F  2 128 ? 2.091   3.330   -13.924 1.00 9.50   ? 128 GLU F CD  1 
ATOM   11003 O OE1 . GLU F  2 128 ? 3.246   2.914   -14.170 1.00 6.82   ? 128 GLU F OE1 1 
ATOM   11004 O OE2 . GLU F  2 128 ? 1.383   2.863   -13.006 1.00 9.38   ? 128 GLU F OE2 1 
ATOM   11005 N N   . ASN F  2 129 ? 3.917   8.550   -13.412 1.00 8.08   ? 129 ASN F N   1 
ATOM   11006 C CA  . ASN F  2 129 ? 4.791   9.678   -13.696 1.00 7.75   ? 129 ASN F CA  1 
ATOM   11007 C C   . ASN F  2 129 ? 5.991   9.754   -12.764 1.00 7.94   ? 129 ASN F C   1 
ATOM   11008 O O   . ASN F  2 129 ? 6.910   10.553  -12.982 1.00 8.01   ? 129 ASN F O   1 
ATOM   11009 C CB  . ASN F  2 129 ? 3.999   10.988  -13.666 1.00 7.63   ? 129 ASN F CB  1 
ATOM   11010 C CG  . ASN F  2 129 ? 2.992   11.089  -14.800 1.00 9.33   ? 129 ASN F CG  1 
ATOM   11011 O OD1 . ASN F  2 129 ? 2.847   10.171  -15.603 1.00 12.27  ? 129 ASN F OD1 1 
ATOM   11012 N ND2 . ASN F  2 129 ? 2.294   12.213  -14.869 1.00 11.71  ? 129 ASN F ND2 1 
ATOM   11013 N N   . ALA F  2 130 ? 5.982   8.917   -11.731 1.00 7.92   ? 130 ALA F N   1 
ATOM   11014 C CA  . ALA F  2 130 ? 7.047   8.918   -10.734 1.00 8.86   ? 130 ALA F CA  1 
ATOM   11015 C C   . ALA F  2 130 ? 7.366   7.518   -10.233 1.00 9.49   ? 130 ALA F C   1 
ATOM   11016 O O   . ALA F  2 130 ? 6.566   6.596   -10.386 1.00 8.90   ? 130 ALA F O   1 
ATOM   11017 C CB  . ALA F  2 130 ? 6.675   9.824   -9.566  1.00 9.44   ? 130 ALA F CB  1 
ATOM   11018 N N   . GLU F  2 131 ? 8.548   7.370   -9.641  1.00 10.67  ? 131 GLU F N   1 
ATOM   11019 C CA  . GLU F  2 131 ? 8.946   6.118   -9.004  1.00 11.88  ? 131 GLU F CA  1 
ATOM   11020 C C   . GLU F  2 131 ? 9.415   6.387   -7.580  1.00 12.99  ? 131 GLU F C   1 
ATOM   11021 O O   . GLU F  2 131 ? 9.896   7.480   -7.278  1.00 13.66  ? 131 GLU F O   1 
ATOM   11022 C CB  . GLU F  2 131 ? 10.045  5.419   -9.806  1.00 11.67  ? 131 GLU F CB  1 
ATOM   11023 C CG  . GLU F  2 131 ? 9.585   4.842   -11.145 1.00 10.31  ? 131 GLU F CG  1 
ATOM   11024 C CD  . GLU F  2 131 ? 10.676  4.058   -11.854 1.00 11.26  ? 131 GLU F CD  1 
ATOM   11025 O OE1 . GLU F  2 131 ? 11.645  3.629   -11.189 1.00 15.14  ? 131 GLU F OE1 1 
ATOM   11026 O OE2 . GLU F  2 131 ? 10.565  3.860   -13.079 1.00 6.96   ? 131 GLU F OE2 1 
ATOM   11027 N N   . GLU F  2 132 ? 9.268   5.391   -6.711  1.00 13.77  ? 132 GLU F N   1 
ATOM   11028 C CA  . GLU F  2 132 ? 9.622   5.539   -5.299  1.00 14.11  ? 132 GLU F CA  1 
ATOM   11029 C C   . GLU F  2 132 ? 11.121  5.393   -5.048  1.00 14.62  ? 132 GLU F C   1 
ATOM   11030 O O   . GLU F  2 132 ? 11.768  4.472   -5.554  1.00 14.59  ? 132 GLU F O   1 
ATOM   11031 C CB  . GLU F  2 132 ? 8.840   4.547   -4.440  1.00 13.91  ? 132 GLU F CB  1 
ATOM   11032 C CG  . GLU F  2 132 ? 7.371   4.899   -4.284  1.00 15.53  ? 132 GLU F CG  1 
ATOM   11033 C CD  . GLU F  2 132 ? 6.557   3.762   -3.702  1.00 18.23  ? 132 GLU F CD  1 
ATOM   11034 O OE1 . GLU F  2 132 ? 6.282   2.788   -4.434  1.00 19.74  ? 132 GLU F OE1 1 
ATOM   11035 O OE2 . GLU F  2 132 ? 6.187   3.845   -2.513  1.00 20.28  ? 132 GLU F OE2 1 
ATOM   11036 N N   . ASP F  2 133 ? 11.656  6.328   -4.270  1.00 15.00  ? 133 ASP F N   1 
ATOM   11037 C CA  . ASP F  2 133 ? 13.049  6.318   -3.852  1.00 15.01  ? 133 ASP F CA  1 
ATOM   11038 C C   . ASP F  2 133 ? 13.288  5.170   -2.879  1.00 13.94  ? 133 ASP F C   1 
ATOM   11039 O O   . ASP F  2 133 ? 14.202  4.364   -3.064  1.00 14.45  ? 133 ASP F O   1 
ATOM   11040 C CB  . ASP F  2 133 ? 13.383  7.645   -3.166  1.00 16.17  ? 133 ASP F CB  1 
ATOM   11041 C CG  . ASP F  2 133 ? 14.865  7.966   -3.192  1.00 22.48  ? 133 ASP F CG  1 
ATOM   11042 O OD1 . ASP F  2 133 ? 15.536  7.671   -4.207  1.00 29.84  ? 133 ASP F OD1 1 
ATOM   11043 O OD2 . ASP F  2 133 ? 15.359  8.540   -2.200  1.00 29.20  ? 133 ASP F OD2 1 
ATOM   11044 N N   . GLY F  2 134 ? 12.437  5.094   -1.859  1.00 12.31  ? 134 GLY F N   1 
ATOM   11045 C CA  . GLY F  2 134 ? 12.616  4.167   -0.753  1.00 10.11  ? 134 GLY F CA  1 
ATOM   11046 C C   . GLY F  2 134 ? 12.868  4.923   0.539   1.00 9.11   ? 134 GLY F C   1 
ATOM   11047 O O   . GLY F  2 134 ? 12.798  4.345   1.628   1.00 9.46   ? 134 GLY F O   1 
ATOM   11048 N N   . THR F  2 135 ? 13.152  6.219   0.415   1.00 7.64   ? 135 THR F N   1 
ATOM   11049 C CA  . THR F  2 135 ? 13.449  7.072   1.565   1.00 6.60   ? 135 THR F CA  1 
ATOM   11050 C C   . THR F  2 135 ? 12.319  8.065   1.849   1.00 6.75   ? 135 THR F C   1 
ATOM   11051 O O   . THR F  2 135 ? 12.450  8.943   2.709   1.00 6.56   ? 135 THR F O   1 
ATOM   11052 C CB  . THR F  2 135 ? 14.761  7.865   1.370   1.00 6.38   ? 135 THR F CB  1 
ATOM   11053 O OG1 . THR F  2 135 ? 14.584  8.831   0.329   1.00 4.76   ? 135 THR F OG1 1 
ATOM   11054 C CG2 . THR F  2 135 ? 15.925  6.941   1.023   1.00 5.98   ? 135 THR F CG2 1 
ATOM   11055 N N   . GLY F  2 136 ? 11.216  7.923   1.120   1.00 6.89   ? 136 GLY F N   1 
ATOM   11056 C CA  . GLY F  2 136 ? 10.075  8.822   1.254   1.00 6.96   ? 136 GLY F CA  1 
ATOM   11057 C C   . GLY F  2 136 ? 9.959   9.814   0.112   1.00 7.84   ? 136 GLY F C   1 
ATOM   11058 O O   . GLY F  2 136 ? 9.080   10.678  0.125   1.00 8.57   ? 136 GLY F O   1 
ATOM   11059 N N   . CYS F  2 137 ? 10.844  9.692   -0.877  1.00 8.16   ? 137 CYS F N   1 
ATOM   11060 C CA  . CYS F  2 137 ? 10.860  10.602  -2.024  1.00 7.94   ? 137 CYS F CA  1 
ATOM   11061 C C   . CYS F  2 137 ? 10.240  9.964   -3.266  1.00 8.77   ? 137 CYS F C   1 
ATOM   11062 O O   . CYS F  2 137 ? 10.265  8.741   -3.433  1.00 8.90   ? 137 CYS F O   1 
ATOM   11063 C CB  . CYS F  2 137 ? 12.293  11.056  -2.330  1.00 7.41   ? 137 CYS F CB  1 
ATOM   11064 S SG  . CYS F  2 137 ? 13.094  11.990  -1.009  0.60 4.59   ? 137 CYS F SG  1 
ATOM   11065 N N   . PHE F  2 138 ? 9.675   10.801  -4.131  1.00 9.31   ? 138 PHE F N   1 
ATOM   11066 C CA  . PHE F  2 138 ? 9.186   10.343  -5.424  1.00 9.87   ? 138 PHE F CA  1 
ATOM   11067 C C   . PHE F  2 138 ? 10.023  10.927  -6.549  1.00 10.84  ? 138 PHE F C   1 
ATOM   11068 O O   . PHE F  2 138 ? 10.026  12.139  -6.765  1.00 11.41  ? 138 PHE F O   1 
ATOM   11069 C CB  . PHE F  2 138 ? 7.717   10.712  -5.608  1.00 9.20   ? 138 PHE F CB  1 
ATOM   11070 C CG  . PHE F  2 138 ? 6.790   9.936   -4.728  1.00 9.39   ? 138 PHE F CG  1 
ATOM   11071 C CD1 . PHE F  2 138 ? 6.363   10.463  -3.513  1.00 8.13   ? 138 PHE F CD1 1 
ATOM   11072 C CD2 . PHE F  2 138 ? 6.347   8.671   -5.107  1.00 9.50   ? 138 PHE F CD2 1 
ATOM   11073 C CE1 . PHE F  2 138 ? 5.507   9.744   -2.689  1.00 9.18   ? 138 PHE F CE1 1 
ATOM   11074 C CE2 . PHE F  2 138 ? 5.486   7.942   -4.288  1.00 11.21  ? 138 PHE F CE2 1 
ATOM   11075 C CZ  . PHE F  2 138 ? 5.065   8.480   -3.075  1.00 9.85   ? 138 PHE F CZ  1 
ATOM   11076 N N   . GLU F  2 139 ? 10.748  10.065  -7.255  1.00 12.17  ? 139 GLU F N   1 
ATOM   11077 C CA  . GLU F  2 139 ? 11.517  10.501  -8.416  1.00 13.62  ? 139 GLU F CA  1 
ATOM   11078 C C   . GLU F  2 139 ? 10.599  10.754  -9.609  1.00 13.68  ? 139 GLU F C   1 
ATOM   11079 O O   . GLU F  2 139 ? 10.019  9.825   -10.174 1.00 13.90  ? 139 GLU F O   1 
ATOM   11080 C CB  . GLU F  2 139 ? 12.665  9.535   -8.732  1.00 13.49  ? 139 GLU F CB  1 
ATOM   11081 C CG  . GLU F  2 139 ? 13.961  9.949   -8.033  1.00 18.93  ? 139 GLU F CG  1 
ATOM   11082 C CD  . GLU F  2 139 ? 14.991  8.836   -7.908  1.00 23.63  ? 139 GLU F CD  1 
ATOM   11083 O OE1 . GLU F  2 139 ? 15.652  8.774   -6.848  1.00 23.28  ? 139 GLU F OE1 1 
ATOM   11084 O OE2 . GLU F  2 139 ? 15.152  8.037   -8.860  1.00 26.94  ? 139 GLU F OE2 1 
ATOM   11085 N N   . ILE F  2 140 ? 10.453  12.031  -9.949  1.00 14.10  ? 140 ILE F N   1 
ATOM   11086 C CA  . ILE F  2 140 ? 9.542   12.482  -10.993 1.00 14.44  ? 140 ILE F CA  1 
ATOM   11087 C C   . ILE F  2 140 ? 10.243  12.434  -12.346 1.00 14.95  ? 140 ILE F C   1 
ATOM   11088 O O   . ILE F  2 140 ? 11.310  13.024  -12.521 1.00 15.30  ? 140 ILE F O   1 
ATOM   11089 C CB  . ILE F  2 140 ? 9.029   13.917  -10.694 1.00 14.46  ? 140 ILE F CB  1 
ATOM   11090 C CG1 . ILE F  2 140 ? 8.256   13.949  -9.371  1.00 12.04  ? 140 ILE F CG1 1 
ATOM   11091 C CG2 . ILE F  2 140 ? 8.158   14.438  -11.829 1.00 15.18  ? 140 ILE F CG2 1 
ATOM   11092 C CD1 . ILE F  2 140 ? 8.164   15.321  -8.741  1.00 7.38   ? 140 ILE F CD1 1 
ATOM   11093 N N   . PHE F  2 141 ? 9.636   11.730  -13.298 1.00 16.12  ? 141 PHE F N   1 
ATOM   11094 C CA  . PHE F  2 141 ? 10.248  11.512  -14.614 1.00 16.67  ? 141 PHE F CA  1 
ATOM   11095 C C   . PHE F  2 141 ? 9.793   12.505  -15.690 1.00 17.27  ? 141 PHE F C   1 
ATOM   11096 O O   . PHE F  2 141 ? 9.758   12.184  -16.879 1.00 17.71  ? 141 PHE F O   1 
ATOM   11097 C CB  . PHE F  2 141 ? 10.060  10.058  -15.056 1.00 16.04  ? 141 PHE F CB  1 
ATOM   11098 C CG  . PHE F  2 141 ? 10.934  9.093   -14.310 1.00 16.38  ? 141 PHE F CG  1 
ATOM   11099 C CD1 . PHE F  2 141 ? 10.527  8.565   -13.090 1.00 15.00  ? 141 PHE F CD1 1 
ATOM   11100 C CD2 . PHE F  2 141 ? 12.178  8.724   -14.819 1.00 17.03  ? 141 PHE F CD2 1 
ATOM   11101 C CE1 . PHE F  2 141 ? 11.342  7.679   -12.387 1.00 15.58  ? 141 PHE F CE1 1 
ATOM   11102 C CE2 . PHE F  2 141 ? 13.001  7.835   -14.126 1.00 16.97  ? 141 PHE F CE2 1 
ATOM   11103 C CZ  . PHE F  2 141 ? 12.581  7.312   -12.907 1.00 17.13  ? 141 PHE F CZ  1 
ATOM   11104 N N   . HIS F  2 142 ? 9.452   13.714  -15.255 1.00 17.69  ? 142 HIS F N   1 
ATOM   11105 C CA  . HIS F  2 142 ? 9.180   14.827  -16.160 1.00 18.13  ? 142 HIS F CA  1 
ATOM   11106 C C   . HIS F  2 142 ? 9.633   16.130  -15.506 1.00 18.94  ? 142 HIS F C   1 
ATOM   11107 O O   . HIS F  2 142 ? 9.956   16.153  -14.315 1.00 19.56  ? 142 HIS F O   1 
ATOM   11108 C CB  . HIS F  2 142 ? 7.697   14.873  -16.558 1.00 18.16  ? 142 HIS F CB  1 
ATOM   11109 C CG  . HIS F  2 142 ? 6.760   15.134  -15.419 1.00 15.71  ? 142 HIS F CG  1 
ATOM   11110 N ND1 . HIS F  2 142 ? 6.403   16.405  -15.026 1.00 14.82  ? 142 HIS F ND1 1 
ATOM   11111 C CD2 . HIS F  2 142 ? 6.092   14.287  -14.602 1.00 15.87  ? 142 HIS F CD2 1 
ATOM   11112 C CE1 . HIS F  2 142 ? 5.564   16.330  -14.008 1.00 15.55  ? 142 HIS F CE1 1 
ATOM   11113 N NE2 . HIS F  2 142 ? 5.356   15.056  -13.734 1.00 14.66  ? 142 HIS F NE2 1 
ATOM   11114 N N   . LYS F  2 143 ? 9.680   17.209  -16.277 1.00 19.42  ? 143 LYS F N   1 
ATOM   11115 C CA  . LYS F  2 143 ? 10.068  18.496  -15.710 1.00 20.26  ? 143 LYS F CA  1 
ATOM   11116 C C   . LYS F  2 143 ? 8.875   19.122  -14.995 1.00 20.03  ? 143 LYS F C   1 
ATOM   11117 O O   . LYS F  2 143 ? 7.809   19.315  -15.585 1.00 20.49  ? 143 LYS F O   1 
ATOM   11118 C CB  . LYS F  2 143 ? 10.682  19.420  -16.768 1.00 20.51  ? 143 LYS F CB  1 
ATOM   11119 C CG  . LYS F  2 143 ? 11.939  18.827  -17.406 1.00 23.40  ? 143 LYS F CG  1 
ATOM   11120 C CD  . LYS F  2 143 ? 12.871  19.883  -17.987 1.00 28.10  ? 143 LYS F CD  1 
ATOM   11121 C CE  . LYS F  2 143 ? 14.131  19.224  -18.551 1.00 29.37  ? 143 LYS F CE  1 
ATOM   11122 N NZ  . LYS F  2 143 ? 15.130  20.214  -19.047 1.00 30.27  ? 143 LYS F NZ  1 
ATOM   11123 N N   . CYS F  2 144 ? 9.064   19.403  -13.708 1.00 19.46  ? 144 CYS F N   1 
ATOM   11124 C CA  . CYS F  2 144 ? 7.992   19.849  -12.829 1.00 18.11  ? 144 CYS F CA  1 
ATOM   11125 C C   . CYS F  2 144 ? 8.390   21.169  -12.166 1.00 17.37  ? 144 CYS F C   1 
ATOM   11126 O O   . CYS F  2 144 ? 9.106   21.178  -11.159 1.00 17.62  ? 144 CYS F O   1 
ATOM   11127 C CB  . CYS F  2 144 ? 7.701   18.759  -11.784 1.00 17.84  ? 144 CYS F CB  1 
ATOM   11128 S SG  . CYS F  2 144 ? 6.175   18.917  -10.805 1.00 18.38  ? 144 CYS F SG  1 
ATOM   11129 N N   . ASP F  2 145 ? 7.936   22.282  -12.744 1.00 16.32  ? 145 ASP F N   1 
ATOM   11130 C CA  . ASP F  2 145 ? 8.251   23.613  -12.212 1.00 15.05  ? 145 ASP F CA  1 
ATOM   11131 C C   . ASP F  2 145 ? 7.522   23.907  -10.898 1.00 14.69  ? 145 ASP F C   1 
ATOM   11132 O O   . ASP F  2 145 ? 6.726   23.095  -10.430 1.00 14.62  ? 145 ASP F O   1 
ATOM   11133 C CB  . ASP F  2 145 ? 8.028   24.722  -13.264 1.00 15.17  ? 145 ASP F CB  1 
ATOM   11134 C CG  . ASP F  2 145 ? 6.585   24.800  -13.788 1.00 14.10  ? 145 ASP F CG  1 
ATOM   11135 O OD1 . ASP F  2 145 ? 5.697   24.046  -13.338 1.00 10.09  ? 145 ASP F OD1 1 
ATOM   11136 O OD2 . ASP F  2 145 ? 6.343   25.648  -14.672 1.00 12.39  ? 145 ASP F OD2 1 
ATOM   11137 N N   . ASP F  2 146 ? 7.808   25.060  -10.300 1.00 14.63  ? 146 ASP F N   1 
ATOM   11138 C CA  . ASP F  2 146 ? 7.210   25.428  -9.015  1.00 14.59  ? 146 ASP F CA  1 
ATOM   11139 C C   . ASP F  2 146 ? 5.679   25.343  -9.000  1.00 14.10  ? 146 ASP F C   1 
ATOM   11140 O O   . ASP F  2 146 ? 5.087   24.993  -7.975  1.00 13.18  ? 146 ASP F O   1 
ATOM   11141 C CB  . ASP F  2 146 ? 7.685   26.819  -8.574  1.00 14.56  ? 146 ASP F CB  1 
ATOM   11142 C CG  . ASP F  2 146 ? 9.087   26.801  -7.969  1.00 15.73  ? 146 ASP F CG  1 
ATOM   11143 O OD1 . ASP F  2 146 ? 9.715   25.720  -7.904  1.00 15.87  ? 146 ASP F OD1 1 
ATOM   11144 O OD2 . ASP F  2 146 ? 9.565   27.878  -7.552  1.00 17.25  ? 146 ASP F OD2 1 
ATOM   11145 N N   . GLN F  2 147 ? 5.055   25.651  -10.140 1.00 14.25  ? 147 GLN F N   1 
ATOM   11146 C CA  . GLN F  2 147 ? 3.599   25.575  -10.295 1.00 14.58  ? 147 GLN F CA  1 
ATOM   11147 C C   . GLN F  2 147 ? 3.151   24.113  -10.346 1.00 14.39  ? 147 GLN F C   1 
ATOM   11148 O O   . GLN F  2 147 ? 2.092   23.758  -9.822  1.00 13.92  ? 147 GLN F O   1 
ATOM   11149 C CB  . GLN F  2 147 ? 3.122   26.305  -11.562 1.00 14.71  ? 147 GLN F CB  1 
ATOM   11150 C CG  . GLN F  2 147 ? 4.077   27.365  -12.144 1.00 18.35  ? 147 GLN F CG  1 
ATOM   11151 C CD  . GLN F  2 147 ? 4.235   28.603  -11.272 1.00 23.00  ? 147 GLN F CD  1 
ATOM   11152 O OE1 . GLN F  2 147 ? 3.318   28.999  -10.548 1.00 25.53  ? 147 GLN F OE1 1 
ATOM   11153 N NE2 . GLN F  2 147 ? 5.408   29.225  -11.344 1.00 23.34  ? 147 GLN F NE2 1 
ATOM   11154 N N   . CYS F  2 148 ? 3.970   23.277  -10.984 1.00 14.17  ? 148 CYS F N   1 
ATOM   11155 C CA  . CYS F  2 148 ? 3.723   21.839  -11.079 1.00 13.90  ? 148 CYS F CA  1 
ATOM   11156 C C   . CYS F  2 148 ? 3.882   21.170  -9.715  1.00 13.39  ? 148 CYS F C   1 
ATOM   11157 O O   . CYS F  2 148 ? 3.137   20.246  -9.381  1.00 13.37  ? 148 CYS F O   1 
ATOM   11158 C CB  . CYS F  2 148 ? 4.660   21.208  -12.116 1.00 13.30  ? 148 CYS F CB  1 
ATOM   11159 S SG  . CYS F  2 148 ? 4.720   19.398  -12.156 1.00 18.30  ? 148 CYS F SG  1 
ATOM   11160 N N   . MET F  2 149 ? 4.854   21.639  -8.935  1.00 12.89  ? 149 MET F N   1 
ATOM   11161 C CA  . MET F  2 149 ? 5.077   21.117  -7.589  1.00 12.80  ? 149 MET F CA  1 
ATOM   11162 C C   . MET F  2 149 ? 3.918   21.463  -6.662  1.00 13.39  ? 149 MET F C   1 
ATOM   11163 O O   . MET F  2 149 ? 3.511   20.639  -5.838  1.00 14.09  ? 149 MET F O   1 
ATOM   11164 C CB  . MET F  2 149 ? 6.398   21.624  -7.004  1.00 12.58  ? 149 MET F CB  1 
ATOM   11165 C CG  . MET F  2 149 ? 7.646   21.037  -7.650  1.00 12.02  ? 149 MET F CG  1 
ATOM   11166 S SD  . MET F  2 149 ? 7.872   19.276  -7.339  1.00 10.33  ? 149 MET F SD  1 
ATOM   11167 C CE  . MET F  2 149 ? 9.368   18.960  -8.268  1.00 6.76   ? 149 MET F CE  1 
ATOM   11168 N N   . GLU F  2 150 ? 3.382   22.672  -6.804  1.00 13.87  ? 150 GLU F N   1 
ATOM   11169 C CA  . GLU F  2 150 ? 2.253   23.102  -5.985  1.00 15.27  ? 150 GLU F CA  1 
ATOM   11170 C C   . GLU F  2 150 ? 0.986   22.312  -6.309  1.00 15.26  ? 150 GLU F C   1 
ATOM   11171 O O   . GLU F  2 150 ? 0.175   22.043  -5.419  1.00 15.52  ? 150 GLU F O   1 
ATOM   11172 C CB  . GLU F  2 150 ? 1.990   24.601  -6.135  1.00 15.74  ? 150 GLU F CB  1 
ATOM   11173 C CG  . GLU F  2 150 ? 1.279   25.205  -4.926  1.00 19.51  ? 150 GLU F CG  1 
ATOM   11174 C CD  . GLU F  2 150 ? 0.320   26.329  -5.285  1.00 27.09  ? 150 GLU F CD  1 
ATOM   11175 O OE1 . GLU F  2 150 ? 0.636   27.144  -6.185  1.00 28.50  ? 150 GLU F OE1 1 
ATOM   11176 O OE2 . GLU F  2 150 ? -0.756  26.399  -4.650  1.00 30.87  ? 150 GLU F OE2 1 
ATOM   11177 N N   . SER F  2 151 ? 0.828   21.940  -7.580  1.00 15.32  ? 151 SER F N   1 
ATOM   11178 C CA  . SER F  2 151 ? -0.327  21.164  -8.029  1.00 15.26  ? 151 SER F CA  1 
ATOM   11179 C C   . SER F  2 151 ? -0.357  19.798  -7.351  1.00 14.98  ? 151 SER F C   1 
ATOM   11180 O O   . SER F  2 151 ? -1.426  19.299  -6.989  1.00 14.56  ? 151 SER F O   1 
ATOM   11181 C CB  . SER F  2 151 ? -0.341  21.021  -9.558  1.00 15.38  ? 151 SER F CB  1 
ATOM   11182 O OG  . SER F  2 151 ? 0.617   20.081  -10.011 1.00 15.89  ? 151 SER F OG  1 
ATOM   11183 N N   . ILE F  2 152 ? 0.827   19.214  -7.175  1.00 15.20  ? 152 ILE F N   1 
ATOM   11184 C CA  . ILE F  2 152 ? 0.985   17.972  -6.423  1.00 15.41  ? 152 ILE F CA  1 
ATOM   11185 C C   . ILE F  2 152 ? 0.580   18.188  -4.966  1.00 16.04  ? 152 ILE F C   1 
ATOM   11186 O O   . ILE F  2 152 ? -0.125  17.359  -4.386  1.00 17.09  ? 152 ILE F O   1 
ATOM   11187 C CB  . ILE F  2 152 ? 2.433   17.430  -6.497  1.00 15.25  ? 152 ILE F CB  1 
ATOM   11188 C CG1 . ILE F  2 152 ? 2.825   17.145  -7.952  1.00 14.70  ? 152 ILE F CG1 1 
ATOM   11189 C CG2 . ILE F  2 152 ? 2.583   16.178  -5.632  1.00 14.54  ? 152 ILE F CG2 1 
ATOM   11190 C CD1 . ILE F  2 152 ? 4.288   16.741  -8.164  1.00 12.89  ? 152 ILE F CD1 1 
ATOM   11191 N N   . ARG F  2 153 ? 1.012   19.308  -4.390  1.00 16.32  ? 153 ARG F N   1 
ATOM   11192 C CA  . ARG F  2 153 ? 0.710   19.619  -2.994  1.00 16.84  ? 153 ARG F CA  1 
ATOM   11193 C C   . ARG F  2 153 ? -0.781  19.838  -2.738  1.00 18.03  ? 153 ARG F C   1 
ATOM   11194 O O   . ARG F  2 153 ? -1.338  19.235  -1.822  1.00 18.61  ? 153 ARG F O   1 
ATOM   11195 C CB  . ARG F  2 153 ? 1.528   20.816  -2.497  1.00 16.49  ? 153 ARG F CB  1 
ATOM   11196 C CG  . ARG F  2 153 ? 3.005   20.509  -2.266  1.00 13.33  ? 153 ARG F CG  1 
ATOM   11197 C CD  . ARG F  2 153 ? 3.683   21.592  -1.437  1.00 11.30  ? 153 ARG F CD  1 
ATOM   11198 N NE  . ARG F  2 153 ? 3.616   22.905  -2.076  1.00 10.47  ? 153 ARG F NE  1 
ATOM   11199 C CZ  . ARG F  2 153 ? 4.517   23.379  -2.931  1.00 8.51   ? 153 ARG F CZ  1 
ATOM   11200 N NH1 . ARG F  2 153 ? 5.585   22.660  -3.259  1.00 7.25   ? 153 ARG F NH1 1 
ATOM   11201 N NH2 . ARG F  2 153 ? 4.349   24.583  -3.457  1.00 9.12   ? 153 ARG F NH2 1 
ATOM   11202 N N   . ASN F  2 154 ? -1.428  20.682  -3.543  1.00 19.01  ? 154 ASN F N   1 
ATOM   11203 C CA  . ASN F  2 154 ? -2.859  20.963  -3.342  1.00 19.68  ? 154 ASN F CA  1 
ATOM   11204 C C   . ASN F  2 154 ? -3.819  20.123  -4.200  1.00 18.91  ? 154 ASN F C   1 
ATOM   11205 O O   . ASN F  2 154 ? -4.958  20.526  -4.450  1.00 17.86  ? 154 ASN F O   1 
ATOM   11206 C CB  . ASN F  2 154 ? -3.165  22.476  -3.416  1.00 20.12  ? 154 ASN F CB  1 
ATOM   11207 C CG  . ASN F  2 154 ? -3.050  23.049  -4.824  1.00 23.45  ? 154 ASN F CG  1 
ATOM   11208 O OD1 . ASN F  2 154 ? -2.593  22.385  -5.758  1.00 27.01  ? 154 ASN F OD1 1 
ATOM   11209 N ND2 . ASN F  2 154 ? -3.473  24.301  -4.979  1.00 26.26  ? 154 ASN F ND2 1 
ATOM   11210 N N   . ASN F  2 155 ? -3.333  18.958  -4.636  1.00 19.32  ? 155 ASN F N   1 
ATOM   11211 C CA  . ASN F  2 155 ? -4.150  17.903  -5.261  1.00 19.69  ? 155 ASN F CA  1 
ATOM   11212 C C   . ASN F  2 155 ? -4.893  18.314  -6.546  1.00 19.05  ? 155 ASN F C   1 
ATOM   11213 O O   . ASN F  2 155 ? -6.093  18.065  -6.689  1.00 19.33  ? 155 ASN F O   1 
ATOM   11214 C CB  . ASN F  2 155 ? -5.114  17.298  -4.222  1.00 20.67  ? 155 ASN F CB  1 
ATOM   11215 C CG  . ASN F  2 155 ? -5.607  15.908  -4.603  1.00 24.77  ? 155 ASN F CG  1 
ATOM   11216 O OD1 . ASN F  2 155 ? -4.823  15.034  -4.986  1.00 29.91  ? 155 ASN F OD1 1 
ATOM   11217 N ND2 . ASN F  2 155 ? -6.914  15.694  -4.478  1.00 24.52  ? 155 ASN F ND2 1 
ATOM   11218 N N   . THR F  2 156 ? -4.169  18.940  -7.474  1.00 17.64  ? 156 THR F N   1 
ATOM   11219 C CA  . THR F  2 156 ? -4.736  19.370  -8.757  1.00 16.11  ? 156 THR F CA  1 
ATOM   11220 C C   . THR F  2 156 ? -3.904  18.884  -9.948  1.00 15.62  ? 156 THR F C   1 
ATOM   11221 O O   . THR F  2 156 ? -4.308  19.032  -11.105 1.00 14.39  ? 156 THR F O   1 
ATOM   11222 C CB  . THR F  2 156 ? -4.876  20.901  -8.845  1.00 16.54  ? 156 THR F CB  1 
ATOM   11223 O OG1 . THR F  2 156 ? -3.574  21.499  -8.790  1.00 15.62  ? 156 THR F OG1 1 
ATOM   11224 C CG2 . THR F  2 156 ? -5.762  21.446  -7.714  1.00 14.26  ? 156 THR F CG2 1 
ATOM   11225 N N   . TYR F  2 157 ? -2.737  18.319  -9.640  1.00 15.26  ? 157 TYR F N   1 
ATOM   11226 C CA  . TYR F  2 157 ? -1.852  17.659  -10.601 1.00 14.51  ? 157 TYR F CA  1 
ATOM   11227 C C   . TYR F  2 157 ? -2.599  16.682  -11.521 1.00 14.23  ? 157 TYR F C   1 
ATOM   11228 O O   . TYR F  2 157 ? -3.237  15.741  -11.049 1.00 14.19  ? 157 TYR F O   1 
ATOM   11229 C CB  . TYR F  2 157 ? -0.760  16.925  -9.813  1.00 14.22  ? 157 TYR F CB  1 
ATOM   11230 C CG  . TYR F  2 157 ? 0.233   16.137  -10.632 1.00 15.07  ? 157 TYR F CG  1 
ATOM   11231 C CD1 . TYR F  2 157 ? 1.394   16.735  -11.110 1.00 16.49  ? 157 TYR F CD1 1 
ATOM   11232 C CD2 . TYR F  2 157 ? 0.028   14.785  -10.907 1.00 15.72  ? 157 TYR F CD2 1 
ATOM   11233 C CE1 . TYR F  2 157 ? 2.320   16.016  -11.853 1.00 17.33  ? 157 TYR F CE1 1 
ATOM   11234 C CE2 . TYR F  2 157 ? 0.948   14.056  -11.655 1.00 16.74  ? 157 TYR F CE2 1 
ATOM   11235 C CZ  . TYR F  2 157 ? 2.091   14.681  -12.123 1.00 16.19  ? 157 TYR F CZ  1 
ATOM   11236 O OH  . TYR F  2 157 ? 3.013   13.977  -12.858 1.00 15.58  ? 157 TYR F OH  1 
ATOM   11237 N N   . ASP F  2 158 ? -2.518  16.920  -12.830 1.00 14.05  ? 158 ASP F N   1 
ATOM   11238 C CA  . ASP F  2 158 ? -3.116  16.033  -13.832 1.00 13.82  ? 158 ASP F CA  1 
ATOM   11239 C C   . ASP F  2 158 ? -2.032  15.161  -14.467 1.00 13.62  ? 158 ASP F C   1 
ATOM   11240 O O   . ASP F  2 158 ? -1.238  15.637  -15.287 1.00 13.35  ? 158 ASP F O   1 
ATOM   11241 C CB  . ASP F  2 158 ? -3.867  16.846  -14.901 1.00 13.77  ? 158 ASP F CB  1 
ATOM   11242 C CG  . ASP F  2 158 ? -4.551  15.967  -15.961 1.00 15.57  ? 158 ASP F CG  1 
ATOM   11243 O OD1 . ASP F  2 158 ? -4.683  14.738  -15.759 1.00 18.32  ? 158 ASP F OD1 1 
ATOM   11244 O OD2 . ASP F  2 158 ? -4.969  16.514  -17.007 1.00 12.13  ? 158 ASP F OD2 1 
ATOM   11245 N N   . HIS F  2 159 ? -2.018  13.883  -14.089 1.00 13.61  ? 159 HIS F N   1 
ATOM   11246 C CA  . HIS F  2 159 ? -0.998  12.928  -14.542 1.00 13.65  ? 159 HIS F CA  1 
ATOM   11247 C C   . HIS F  2 159 ? -0.969  12.732  -16.060 1.00 13.85  ? 159 HIS F C   1 
ATOM   11248 O O   . HIS F  2 159 ? 0.083   12.433  -16.627 1.00 13.63  ? 159 HIS F O   1 
ATOM   11249 C CB  . HIS F  2 159 ? -1.158  11.577  -13.829 1.00 13.71  ? 159 HIS F CB  1 
ATOM   11250 C CG  . HIS F  2 159 ? -2.289  10.741  -14.347 1.00 12.51  ? 159 HIS F CG  1 
ATOM   11251 N ND1 . HIS F  2 159 ? -2.103  9.719   -15.253 1.00 12.56  ? 159 HIS F ND1 1 
ATOM   11252 C CD2 . HIS F  2 159 ? -3.617  10.775  -14.087 1.00 13.24  ? 159 HIS F CD2 1 
ATOM   11253 C CE1 . HIS F  2 159 ? -3.267  9.159   -15.528 1.00 12.12  ? 159 HIS F CE1 1 
ATOM   11254 N NE2 . HIS F  2 159 ? -4.203  9.781   -14.833 1.00 11.70  ? 159 HIS F NE2 1 
ATOM   11255 N N   . THR F  2 160 ? -2.129  12.901  -16.697 1.00 14.04  ? 160 THR F N   1 
ATOM   11256 C CA  . THR F  2 160 ? -2.282  12.771  -18.147 1.00 14.31  ? 160 THR F CA  1 
ATOM   11257 C C   . THR F  2 160 ? -1.391  13.762  -18.892 1.00 14.20  ? 160 THR F C   1 
ATOM   11258 O O   . THR F  2 160 ? -0.770  13.415  -19.900 1.00 14.42  ? 160 THR F O   1 
ATOM   11259 C CB  . THR F  2 160 ? -3.753  12.997  -18.575 1.00 14.87  ? 160 THR F CB  1 
ATOM   11260 O OG1 . THR F  2 160 ? -4.624  12.200  -17.760 1.00 14.66  ? 160 THR F OG1 1 
ATOM   11261 C CG2 . THR F  2 160 ? -3.962  12.631  -20.049 1.00 17.24  ? 160 THR F CG2 1 
ATOM   11262 N N   . GLN F  2 161 ? -1.323  14.987  -18.375 1.00 13.95  ? 161 GLN F N   1 
ATOM   11263 C CA  . GLN F  2 161 ? -0.552  16.068  -18.989 1.00 13.21  ? 161 GLN F CA  1 
ATOM   11264 C C   . GLN F  2 161 ? 0.925   15.701  -19.170 1.00 12.40  ? 161 GLN F C   1 
ATOM   11265 O O   . GLN F  2 161 ? 1.572   16.156  -20.117 1.00 12.73  ? 161 GLN F O   1 
ATOM   11266 C CB  . GLN F  2 161 ? -0.700  17.347  -18.155 1.00 13.16  ? 161 GLN F CB  1 
ATOM   11267 C CG  . GLN F  2 161 ? -0.134  18.606  -18.803 1.00 15.65  ? 161 GLN F CG  1 
ATOM   11268 C CD  . GLN F  2 161 ? -0.435  19.876  -18.018 1.00 18.05  ? 161 GLN F CD  1 
ATOM   11269 O OE1 . GLN F  2 161 ? -0.585  19.856  -16.793 1.00 13.54  ? 161 GLN F OE1 1 
ATOM   11270 N NE2 . GLN F  2 161 ? -0.521  20.994  -18.731 1.00 21.38  ? 161 GLN F NE2 1 
ATOM   11271 N N   . TYR F  2 162 ? 1.436   14.857  -18.275 1.00 11.13  ? 162 TYR F N   1 
ATOM   11272 C CA  . TYR F  2 162 ? 2.859   14.531  -18.228 1.00 9.86   ? 162 TYR F CA  1 
ATOM   11273 C C   . TYR F  2 162 ? 3.181   13.071  -18.561 1.00 9.76   ? 162 TYR F C   1 
ATOM   11274 O O   . TYR F  2 162 ? 4.358   12.695  -18.615 1.00 9.81   ? 162 TYR F O   1 
ATOM   11275 C CB  . TYR F  2 162 ? 3.419   14.855  -16.839 1.00 9.93   ? 162 TYR F CB  1 
ATOM   11276 C CG  . TYR F  2 162 ? 3.188   16.273  -16.358 1.00 9.66   ? 162 TYR F CG  1 
ATOM   11277 C CD1 . TYR F  2 162 ? 3.902   17.344  -16.901 1.00 8.85   ? 162 TYR F CD1 1 
ATOM   11278 C CD2 . TYR F  2 162 ? 2.274   16.540  -15.339 1.00 8.28   ? 162 TYR F CD2 1 
ATOM   11279 C CE1 . TYR F  2 162 ? 3.703   18.643  -16.450 1.00 8.65   ? 162 TYR F CE1 1 
ATOM   11280 C CE2 . TYR F  2 162 ? 2.065   17.837  -14.882 1.00 8.48   ? 162 TYR F CE2 1 
ATOM   11281 C CZ  . TYR F  2 162 ? 2.784   18.881  -15.442 1.00 11.43  ? 162 TYR F CZ  1 
ATOM   11282 O OH  . TYR F  2 162 ? 2.584   20.166  -14.993 1.00 16.13  ? 162 TYR F OH  1 
ATOM   11283 N N   . ARG F  2 163 ? 2.149   12.255  -18.781 1.00 9.31   ? 163 ARG F N   1 
ATOM   11284 C CA  . ARG F  2 163 ? 2.321   10.800  -18.927 1.00 9.06   ? 163 ARG F CA  1 
ATOM   11285 C C   . ARG F  2 163 ? 3.228   10.372  -20.087 1.00 9.21   ? 163 ARG F C   1 
ATOM   11286 O O   . ARG F  2 163 ? 4.149   9.577   -19.888 1.00 9.45   ? 163 ARG F O   1 
ATOM   11287 C CB  . ARG F  2 163 ? 0.968   10.085  -19.008 1.00 9.07   ? 163 ARG F CB  1 
ATOM   11288 C CG  . ARG F  2 163 ? 1.071   8.568   -18.932 1.00 7.55   ? 163 ARG F CG  1 
ATOM   11289 C CD  . ARG F  2 163 ? -0.291  7.937   -18.886 1.00 6.76   ? 163 ARG F CD  1 
ATOM   11290 N NE  . ARG F  2 163 ? -0.232  6.488   -19.037 1.00 9.80   ? 163 ARG F NE  1 
ATOM   11291 C CZ  . ARG F  2 163 ? -0.475  5.618   -18.060 1.00 13.44  ? 163 ARG F CZ  1 
ATOM   11292 N NH1 . ARG F  2 163 ? -0.797  6.046   -16.846 1.00 15.17  ? 163 ARG F NH1 1 
ATOM   11293 N NH2 . ARG F  2 163 ? -0.402  4.314   -18.300 1.00 12.59  ? 163 ARG F NH2 1 
ATOM   11294 N N   . THR F  2 164 ? 2.961   10.893  -21.283 1.00 8.96   ? 164 THR F N   1 
ATOM   11295 C CA  . THR F  2 164 ? 3.794   10.627  -22.456 1.00 9.83   ? 164 THR F CA  1 
ATOM   11296 C C   . THR F  2 164 ? 5.267   10.931  -22.152 1.00 10.61  ? 164 THR F C   1 
ATOM   11297 O O   . THR F  2 164 ? 6.152   10.119  -22.433 1.00 10.06  ? 164 THR F O   1 
ATOM   11298 C CB  . THR F  2 164 ? 3.327   11.465  -23.674 1.00 10.05  ? 164 THR F CB  1 
ATOM   11299 O OG1 . THR F  2 164 ? 1.947   11.197  -23.944 1.00 10.49  ? 164 THR F OG1 1 
ATOM   11300 C CG2 . THR F  2 164 ? 4.146   11.147  -24.916 1.00 10.12  ? 164 THR F CG2 1 
ATOM   11301 N N   . GLU F  2 165 ? 5.508   12.100  -21.563 1.00 11.55  ? 165 GLU F N   1 
ATOM   11302 C CA  . GLU F  2 165 ? 6.849   12.549  -21.213 1.00 12.32  ? 165 GLU F CA  1 
ATOM   11303 C C   . GLU F  2 165 ? 7.507   11.629  -20.185 1.00 13.27  ? 165 GLU F C   1 
ATOM   11304 O O   . GLU F  2 165 ? 8.674   11.255  -20.331 1.00 13.20  ? 165 GLU F O   1 
ATOM   11305 C CB  . GLU F  2 165 ? 6.781   13.973  -20.669 1.00 12.28  ? 165 GLU F CB  1 
ATOM   11306 C CG  . GLU F  2 165 ? 8.127   14.635  -20.460 1.00 11.89  ? 165 GLU F CG  1 
ATOM   11307 C CD  . GLU F  2 165 ? 8.002   15.994  -19.815 1.00 12.85  ? 165 GLU F CD  1 
ATOM   11308 O OE1 . GLU F  2 165 ? 8.991   16.445  -19.198 1.00 13.45  ? 165 GLU F OE1 1 
ATOM   11309 O OE2 . GLU F  2 165 ? 6.913   16.605  -19.914 1.00 14.11  ? 165 GLU F OE2 1 
ATOM   11310 N N   . SER F  2 166 ? 6.746   11.270  -19.154 1.00 14.04  ? 166 SER F N   1 
ATOM   11311 C CA  . SER F  2 166 ? 7.243   10.428  -18.070 1.00 14.36  ? 166 SER F CA  1 
ATOM   11312 C C   . SER F  2 166 ? 7.646   9.034   -18.538 1.00 14.37  ? 166 SER F C   1 
ATOM   11313 O O   . SER F  2 166 ? 8.773   8.598   -18.286 1.00 14.57  ? 166 SER F O   1 
ATOM   11314 C CB  . SER F  2 166 ? 6.211   10.341  -16.947 1.00 14.45  ? 166 SER F CB  1 
ATOM   11315 O OG  . SER F  2 166 ? 6.115   11.577  -16.262 1.00 14.89  ? 166 SER F OG  1 
ATOM   11316 N N   . LEU F  2 167 ? 6.736   8.352   -19.233 1.00 14.13  ? 167 LEU F N   1 
ATOM   11317 C CA  . LEU F  2 167 ? 6.959   6.970   -19.664 1.00 13.92  ? 167 LEU F CA  1 
ATOM   11318 C C   . LEU F  2 167 ? 8.208   6.797   -20.524 1.00 14.91  ? 167 LEU F C   1 
ATOM   11319 O O   . LEU F  2 167 ? 8.960   5.841   -20.334 1.00 15.33  ? 167 LEU F O   1 
ATOM   11320 C CB  . LEU F  2 167 ? 5.727   6.399   -20.377 1.00 13.08  ? 167 LEU F CB  1 
ATOM   11321 C CG  . LEU F  2 167 ? 4.511   6.031   -19.518 1.00 11.05  ? 167 LEU F CG  1 
ATOM   11322 C CD1 . LEU F  2 167 ? 3.359   5.575   -20.396 1.00 7.24   ? 167 LEU F CD1 1 
ATOM   11323 C CD2 . LEU F  2 167 ? 4.848   4.961   -18.479 1.00 5.98   ? 167 LEU F CD2 1 
ATOM   11324 N N   . GLN F  2 168 ? 8.436   7.723   -21.454 1.00 15.68  ? 168 GLN F N   1 
ATOM   11325 C CA  . GLN F  2 168 ? 9.621   7.650   -22.312 1.00 16.53  ? 168 GLN F CA  1 
ATOM   11326 C C   . GLN F  2 168 ? 10.919  7.968   -21.566 1.00 16.07  ? 168 GLN F C   1 
ATOM   11327 O O   . GLN F  2 168 ? 11.992  7.516   -21.964 1.00 16.50  ? 168 GLN F O   1 
ATOM   11328 C CB  . GLN F  2 168 ? 9.463   8.496   -23.584 1.00 17.02  ? 168 GLN F CB  1 
ATOM   11329 C CG  . GLN F  2 168 ? 9.199   9.976   -23.371 1.00 20.75  ? 168 GLN F CG  1 
ATOM   11330 C CD  . GLN F  2 168 ? 8.774   10.682  -24.647 1.00 23.43  ? 168 GLN F CD  1 
ATOM   11331 O OE1 . GLN F  2 168 ? 7.753   11.371  -24.675 1.00 26.86  ? 168 GLN F OE1 1 
ATOM   11332 N NE2 . GLN F  2 168 ? 9.551   10.510  -25.712 1.00 24.18  ? 168 GLN F NE2 1 
ATOM   11333 N N   . ASN F  2 169 ? 10.813  8.731   -20.482 1.00 15.67  ? 169 ASN F N   1 
ATOM   11334 C CA  . ASN F  2 169 ? 11.955  8.984   -19.609 1.00 15.13  ? 169 ASN F CA  1 
ATOM   11335 C C   . ASN F  2 169 ? 12.243  7.807   -18.685 1.00 15.30  ? 169 ASN F C   1 
ATOM   11336 O O   . ASN F  2 169 ? 13.330  7.720   -18.110 1.00 14.81  ? 169 ASN F O   1 
ATOM   11337 C CB  . ASN F  2 169 ? 11.745  10.262  -18.789 1.00 15.19  ? 169 ASN F CB  1 
ATOM   11338 C CG  . ASN F  2 169 ? 12.222  11.520  -19.510 1.00 14.87  ? 169 ASN F CG  1 
ATOM   11339 O OD1 . ASN F  2 169 ? 12.944  11.454  -20.507 1.00 15.77  ? 169 ASN F OD1 1 
ATOM   11340 N ND2 . ASN F  2 169 ? 11.824  12.675  -18.996 1.00 14.16  ? 169 ASN F ND2 1 
ATOM   11341 N N   . ARG F  2 170 ? 11.268  6.904   -18.553 1.00 15.65  ? 170 ARG F N   1 
ATOM   11342 C CA  . ARG F  2 170 ? 11.383  5.735   -17.671 1.00 15.60  ? 170 ARG F CA  1 
ATOM   11343 C C   . ARG F  2 170 ? 11.980  4.486   -18.333 1.00 16.28  ? 170 ARG F C   1 
ATOM   11344 O O   . ARG F  2 170 ? 12.238  3.491   -17.651 1.00 16.29  ? 170 ARG F O   1 
ATOM   11345 C CB  . ARG F  2 170 ? 10.028  5.390   -17.046 1.00 15.28  ? 170 ARG F CB  1 
ATOM   11346 C CG  . ARG F  2 170 ? 9.591   6.330   -15.938 1.00 14.93  ? 170 ARG F CG  1 
ATOM   11347 C CD  . ARG F  2 170 ? 8.887   5.575   -14.822 1.00 16.54  ? 170 ARG F CD  1 
ATOM   11348 N NE  . ARG F  2 170 ? 7.482   5.282   -15.104 1.00 14.34  ? 170 ARG F NE  1 
ATOM   11349 C CZ  . ARG F  2 170 ? 6.768   4.336   -14.494 1.00 12.02  ? 170 ARG F CZ  1 
ATOM   11350 N NH1 . ARG F  2 170 ? 7.316   3.553   -13.565 1.00 7.47   ? 170 ARG F NH1 1 
ATOM   11351 N NH2 . ARG F  2 170 ? 5.498   4.163   -14.824 1.00 8.66   ? 170 ARG F NH2 1 
ATOM   11352 N N   . ILE F  2 171 ? 12.200  4.535   -19.647 1.00 17.09  ? 171 ILE F N   1 
ATOM   11353 C CA  . ILE F  2 171 ? 12.759  3.389   -20.381 1.00 18.04  ? 171 ILE F CA  1 
ATOM   11354 C C   . ILE F  2 171 ? 14.282  3.494   -20.550 1.00 17.84  ? 171 ILE F C   1 
ATOM   11355 O O   . ILE F  2 171 ? 14.814  4.543   -20.924 1.00 18.09  ? 171 ILE F O   1 
ATOM   11356 C CB  . ILE F  2 171 ? 12.076  3.177   -21.775 1.00 18.21  ? 171 ILE F CB  1 
ATOM   11357 C CG1 . ILE F  2 171 ? 10.540  3.229   -21.679 1.00 18.18  ? 171 ILE F CG1 1 
ATOM   11358 C CG2 . ILE F  2 171 ? 12.556  1.879   -22.434 1.00 19.77  ? 171 ILE F CG2 1 
ATOM   11359 C CD1 . ILE F  2 171 ? 9.895   2.207   -20.749 1.00 14.74  ? 171 ILE F CD1 1 
HETATM 11360 C C1  . SIA G  3 .   ? -46.666 -6.500  81.002  1.00 57.91  ? 1   SIA A C1  1 
HETATM 11361 C C2  . SIA G  3 .   ? -46.835 -6.478  82.508  1.00 57.28  ? 1   SIA A C2  1 
HETATM 11362 C C3  . SIA G  3 .   ? -47.582 -7.738  82.981  1.00 52.94  ? 1   SIA A C3  1 
HETATM 11363 C C4  . SIA G  3 .   ? -46.725 -9.006  82.997  1.00 50.02  ? 1   SIA A C4  1 
HETATM 11364 C C5  . SIA G  3 .   ? -45.342 -8.774  83.597  1.00 49.76  ? 1   SIA A C5  1 
HETATM 11365 C C6  . SIA G  3 .   ? -44.675 -7.521  83.026  1.00 50.76  ? 1   SIA A C6  1 
HETATM 11366 C C7  . SIA G  3 .   ? -43.326 -7.229  83.693  1.00 48.54  ? 1   SIA A C7  1 
HETATM 11367 C C8  . SIA G  3 .   ? -42.698 -5.916  83.237  1.00 46.18  ? 1   SIA A C8  1 
HETATM 11368 C C9  . SIA G  3 .   ? -41.194 -5.981  83.448  1.00 44.92  ? 1   SIA A C9  1 
HETATM 11369 C C10 . SIA G  3 .   ? -43.934 -10.667 84.304  1.00 47.98  ? 1   SIA A C10 1 
HETATM 11370 C C11 . SIA G  3 .   ? -44.201 -10.310 85.739  1.00 50.28  ? 1   SIA A C11 1 
HETATM 11371 N N5  . SIA G  3 .   ? -44.494 -9.925  83.350  1.00 47.26  ? 1   SIA A N5  1 
HETATM 11372 O O1A . SIA G  3 .   ? -47.592 -6.971  80.305  1.00 58.64  ? 1   SIA A O1A 1 
HETATM 11373 O O1B . SIA G  3 .   ? -45.623 -6.027  80.498  1.00 58.52  ? 1   SIA A O1B 1 
HETATM 11374 O O4  . SIA G  3 .   ? -47.386 -10.018 83.766  1.00 46.92  ? 1   SIA A O4  1 
HETATM 11375 O O6  . SIA G  3 .   ? -45.544 -6.384  83.141  1.00 53.86  ? 1   SIA A O6  1 
HETATM 11376 O O7  . SIA G  3 .   ? -43.460 -7.202  85.121  1.00 49.36  ? 1   SIA A O7  1 
HETATM 11377 O O8  . SIA G  3 .   ? -42.972 -5.664  81.854  1.00 48.36  ? 1   SIA A O8  1 
HETATM 11378 O O9  . SIA G  3 .   ? -40.612 -4.725  83.095  1.00 41.43  ? 1   SIA A O9  1 
HETATM 11379 O O10 . SIA G  3 .   ? -43.231 -11.615 84.014  1.00 51.34  ? 1   SIA A O10 1 
HETATM 11380 C C1  . GAL H  4 .   ? -49.185 -3.094  85.336  1.00 73.08  ? 2   GAL A C1  1 
HETATM 11381 C C2  . GAL H  4 .   ? -49.154 -4.007  84.108  1.00 70.17  ? 2   GAL A C2  1 
HETATM 11382 C C3  . GAL H  4 .   ? -47.895 -4.880  84.063  1.00 67.97  ? 2   GAL A C3  1 
HETATM 11383 C C4  . GAL H  4 .   ? -46.639 -4.041  84.345  1.00 68.97  ? 2   GAL A C4  1 
HETATM 11384 C C5  . GAL H  4 .   ? -46.835 -3.141  85.569  1.00 69.16  ? 2   GAL A C5  1 
HETATM 11385 C C6  . GAL H  4 .   ? -45.619 -2.253  85.812  1.00 70.24  ? 2   GAL A C6  1 
HETATM 11386 O O2  . GAL H  4 .   ? -50.301 -4.830  84.064  1.00 69.22  ? 2   GAL A O2  1 
HETATM 11387 O O3  . GAL H  4 .   ? -47.888 -5.519  82.791  1.00 64.48  ? 2   GAL A O3  1 
HETATM 11388 O O4  . GAL H  4 .   ? -46.305 -3.270  83.208  1.00 69.37  ? 2   GAL A O4  1 
HETATM 11389 O O5  . GAL H  4 .   ? -47.987 -2.338  85.388  1.00 71.34  ? 2   GAL A O5  1 
HETATM 11390 O O6  . GAL H  4 .   ? -45.633 -1.767  87.136  1.00 69.56  ? 2   GAL A O6  1 
HETATM 11391 C C1  . NAG I  5 .   ? -52.637 0.448   87.115  1.00 84.82  ? 3   NAG A C1  1 
HETATM 11392 C C2  . NAG I  5 .   ? -51.318 1.049   86.638  1.00 84.88  ? 3   NAG A C2  1 
HETATM 11393 C C3  . NAG I  5 .   ? -50.491 0.020   85.857  1.00 83.47  ? 3   NAG A C3  1 
HETATM 11394 C C4  . NAG I  5 .   ? -50.539 -1.420  86.402  1.00 81.62  ? 3   NAG A C4  1 
HETATM 11395 C C5  . NAG I  5 .   ? -51.836 -1.776  87.153  1.00 82.20  ? 3   NAG A C5  1 
HETATM 11396 C C6  . NAG I  5 .   ? -51.624 -2.946  88.109  1.00 81.63  ? 3   NAG A C6  1 
HETATM 11397 C C7  . NAG I  5 .   ? -51.161 3.449   86.122  1.00 88.53  ? 3   NAG A C7  1 
HETATM 11398 C C8  . NAG I  5 .   ? -51.526 4.535   85.151  1.00 88.31  ? 3   NAG A C8  1 
HETATM 11399 N N2  . NAG I  5 .   ? -51.577 2.218   85.813  1.00 86.86  ? 3   NAG A N2  1 
HETATM 11400 O O1  . NAG I  5 .   ? -53.361 1.392   87.875  1.00 84.89  ? 3   NAG A O1  1 
HETATM 11401 O O3  . NAG I  5 .   ? -49.147 0.448   85.803  1.00 82.87  ? 3   NAG A O3  1 
HETATM 11402 O O4  . NAG I  5 .   ? -50.391 -2.295  85.295  1.00 78.21  ? 3   NAG A O4  1 
HETATM 11403 O O5  . NAG I  5 .   ? -52.352 -0.690  87.903  1.00 83.80  ? 3   NAG A O5  1 
HETATM 11404 O O6  . NAG I  5 .   ? -52.023 -4.143  87.481  1.00 79.63  ? 3   NAG A O6  1 
HETATM 11405 O O7  . NAG I  5 .   ? -50.514 3.724   87.134  1.00 88.90  ? 3   NAG A O7  1 
HETATM 11406 C C1  . NAG J  5 .   ? -27.615 -3.296  14.942  1.00 56.13  ? 331 NAG A C1  1 
HETATM 11407 C C2  . NAG J  5 .   ? -27.624 -4.736  14.411  1.00 63.99  ? 331 NAG A C2  1 
HETATM 11408 C C3  . NAG J  5 .   ? -28.703 -5.595  15.085  1.00 65.17  ? 331 NAG A C3  1 
HETATM 11409 C C4  . NAG J  5 .   ? -28.852 -5.344  16.593  1.00 66.88  ? 331 NAG A C4  1 
HETATM 11410 C C5  . NAG J  5 .   ? -28.656 -3.879  17.002  1.00 66.74  ? 331 NAG A C5  1 
HETATM 11411 C C6  . NAG J  5 .   ? -28.466 -3.764  18.515  1.00 68.01  ? 331 NAG A C6  1 
HETATM 11412 C C7  . NAG J  5 .   ? -28.639 -4.266  12.152  1.00 66.94  ? 331 NAG A C7  1 
HETATM 11413 C C8  . NAG J  5 .   ? -28.459 -4.529  10.686  1.00 66.68  ? 331 NAG A C8  1 
HETATM 11414 N N2  . NAG J  5 .   ? -27.712 -4.816  12.950  1.00 65.22  ? 331 NAG A N2  1 
HETATM 11415 O O3  . NAG J  5 .   ? -28.389 -6.956  14.882  1.00 62.95  ? 331 NAG A O3  1 
HETATM 11416 O O4  . NAG J  5 .   ? -30.133 -5.772  17.008  1.00 69.07  ? 331 NAG A O4  1 
HETATM 11417 O O5  . NAG J  5 .   ? -27.531 -3.314  16.353  1.00 62.36  ? 331 NAG A O5  1 
HETATM 11418 O O6  . NAG J  5 .   ? -28.069 -2.454  18.865  1.00 68.17  ? 331 NAG A O6  1 
HETATM 11419 O O7  . NAG J  5 .   ? -29.592 -3.582  12.534  1.00 68.32  ? 331 NAG A O7  1 
HETATM 11420 C C1  . NAG K  5 .   ? -24.798 6.595   52.777  1.00 52.31  ? 183 NAG B C1  1 
HETATM 11421 C C2  . NAG K  5 .   ? -25.410 7.271   54.006  1.00 60.10  ? 183 NAG B C2  1 
HETATM 11422 C C3  . NAG K  5 .   ? -26.934 7.096   54.069  1.00 63.71  ? 183 NAG B C3  1 
HETATM 11423 C C4  . NAG K  5 .   ? -27.677 7.175   52.723  1.00 67.37  ? 183 NAG B C4  1 
HETATM 11424 C C5  . NAG K  5 .   ? -26.841 6.632   51.555  1.00 63.49  ? 183 NAG B C5  1 
HETATM 11425 C C6  . NAG K  5 .   ? -27.398 7.035   50.191  1.00 64.37  ? 183 NAG B C6  1 
HETATM 11426 C C7  . NAG K  5 .   ? -24.335 7.531   56.210  1.00 56.68  ? 183 NAG B C7  1 
HETATM 11427 C C8  . NAG K  5 .   ? -23.766 6.815   57.397  1.00 55.68  ? 183 NAG B C8  1 
HETATM 11428 N N2  . NAG K  5 .   ? -24.815 6.755   55.231  1.00 58.28  ? 183 NAG B N2  1 
HETATM 11429 O O3  . NAG K  5 .   ? -27.457 8.071   54.946  1.00 64.37  ? 183 NAG B O3  1 
HETATM 11430 O O4  . NAG K  5 .   ? -28.871 6.410   52.838  1.00 76.77  ? 183 NAG B O4  1 
HETATM 11431 O O5  . NAG K  5 .   ? -25.494 7.064   51.637  1.00 59.12  ? 183 NAG B O5  1 
HETATM 11432 O O6  . NAG K  5 .   ? -26.453 6.765   49.177  1.00 65.51  ? 183 NAG B O6  1 
HETATM 11433 O O7  . NAG K  5 .   ? -24.337 8.763   56.186  1.00 55.75  ? 183 NAG B O7  1 
HETATM 11434 C C1  . NAG L  5 .   ? -30.120 7.135   52.652  1.00 84.69  ? 184 NAG B C1  1 
HETATM 11435 C C2  . NAG L  5 .   ? -30.651 7.724   53.975  1.00 88.62  ? 184 NAG B C2  1 
HETATM 11436 C C3  . NAG L  5 .   ? -31.819 8.721   53.822  1.00 89.55  ? 184 NAG B C3  1 
HETATM 11437 C C4  . NAG L  5 .   ? -31.907 9.441   52.468  1.00 89.86  ? 184 NAG B C4  1 
HETATM 11438 C C5  . NAG L  5 .   ? -31.435 8.540   51.323  1.00 89.54  ? 184 NAG B C5  1 
HETATM 11439 C C6  . NAG L  5 .   ? -31.493 9.219   49.954  1.00 89.89  ? 184 NAG B C6  1 
HETATM 11440 C C7  . NAG L  5 .   ? -31.876 5.655   54.714  1.00 93.91  ? 184 NAG B C7  1 
HETATM 11441 C C8  . NAG L  5 .   ? -32.072 4.720   55.873  1.00 93.59  ? 184 NAG B C8  1 
HETATM 11442 N N2  . NAG L  5 .   ? -31.018 6.673   54.926  1.00 92.40  ? 184 NAG B N2  1 
HETATM 11443 O O3  . NAG L  5 .   ? -31.734 9.684   54.851  1.00 87.89  ? 184 NAG B O3  1 
HETATM 11444 O O4  . NAG L  5 .   ? -33.247 9.838   52.255  1.00 90.08  ? 184 NAG B O4  1 
HETATM 11445 O O5  . NAG L  5 .   ? -30.122 8.099   51.612  1.00 87.63  ? 184 NAG B O5  1 
HETATM 11446 O O6  . NAG L  5 .   ? -30.277 9.880   49.674  1.00 90.45  ? 184 NAG B O6  1 
HETATM 11447 O O7  . NAG L  5 .   ? -32.492 5.448   53.657  1.00 94.91  ? 184 NAG B O7  1 
HETATM 11448 C C1  . GOL M  6 .   ? -4.688  0.243   20.858  1.00 45.41  ? 185 GOL B C1  1 
HETATM 11449 O O1  . GOL M  6 .   ? -3.810  -0.467  21.705  1.00 42.98  ? 185 GOL B O1  1 
HETATM 11450 C C2  . GOL M  6 .   ? -4.725  -0.395  19.469  1.00 46.14  ? 185 GOL B C2  1 
HETATM 11451 O O2  . GOL M  6 .   ? -5.092  -1.756  19.572  1.00 43.53  ? 185 GOL B O2  1 
HETATM 11452 C C3  . GOL M  6 .   ? -5.745  0.356   18.615  1.00 44.82  ? 185 GOL B C3  1 
HETATM 11453 O O3  . GOL M  6 .   ? -5.605  0.005   17.257  1.00 40.35  ? 185 GOL B O3  1 
HETATM 11454 C C1  . GOL N  6 .   ? -13.456 -8.243  28.959  1.00 50.71  ? 186 GOL B C1  1 
HETATM 11455 O O1  . GOL N  6 .   ? -13.409 -6.878  29.303  1.00 50.23  ? 186 GOL B O1  1 
HETATM 11456 C C2  . GOL N  6 .   ? -12.080 -8.874  29.144  1.00 51.08  ? 186 GOL B C2  1 
HETATM 11457 O O2  . GOL N  6 .   ? -11.635 -8.679  30.471  1.00 50.99  ? 186 GOL B O2  1 
HETATM 11458 C C3  . GOL N  6 .   ? -12.196 -10.367 28.859  1.00 51.44  ? 186 GOL B C3  1 
HETATM 11459 O O3  . GOL N  6 .   ? -11.233 -10.751 27.904  1.00 52.40  ? 186 GOL B O3  1 
HETATM 11460 C C1  . SIA O  3 .   ? -7.260  -20.567 93.196  1.00 115.24 ? 1   SIA C C1  1 
HETATM 11461 C C2  . SIA O  3 .   ? -7.782  -19.839 94.424  1.00 115.38 ? 1   SIA C C2  1 
HETATM 11462 C C3  . SIA O  3 .   ? -6.634  -19.678 95.433  1.00 114.36 ? 1   SIA C C3  1 
HETATM 11463 C C4  . SIA O  3 .   ? -5.733  -18.486 95.119  1.00 113.66 ? 1   SIA C C4  1 
HETATM 11464 C C5  . SIA O  3 .   ? -6.561  -17.217 94.934  1.00 112.99 ? 1   SIA C C5  1 
HETATM 11465 C C6  . SIA O  3 .   ? -7.643  -17.406 93.861  1.00 113.03 ? 1   SIA C C6  1 
HETATM 11466 C C7  . SIA O  3 .   ? -8.522  -16.145 93.737  1.00 111.42 ? 1   SIA C C7  1 
HETATM 11467 C C8  . SIA O  3 .   ? -9.718  -16.286 92.782  1.00 110.35 ? 1   SIA C C8  1 
HETATM 11468 C C9  . SIA O  3 .   ? -10.455 -14.955 92.621  1.00 109.17 ? 1   SIA C C9  1 
HETATM 11469 C C10 . SIA O  3 .   ? -5.445  -15.063 95.431  1.00 111.25 ? 1   SIA C C10 1 
HETATM 11470 C C11 . SIA O  3 .   ? -6.101  -15.058 96.784  1.00 111.66 ? 1   SIA C C11 1 
HETATM 11471 N N5  . SIA O  3 .   ? -5.693  -16.092 94.613  1.00 111.56 ? 1   SIA C N5  1 
HETATM 11472 O O1A . SIA O  3 .   ? -6.649  -19.939 92.301  1.00 114.46 ? 1   SIA C O1A 1 
HETATM 11473 O O1B . SIA O  3 .   ? -7.456  -21.800 93.119  1.00 114.77 ? 1   SIA C O1B 1 
HETATM 11474 O O4  . SIA O  3 .   ? -4.795  -18.299 96.183  1.00 113.69 ? 1   SIA C O4  1 
HETATM 11475 O O6  . SIA O  3 .   ? -8.441  -18.586 94.110  1.00 114.38 ? 1   SIA C O6  1 
HETATM 11476 O O7  . SIA O  3 .   ? -8.993  -15.747 95.043  1.00 111.22 ? 1   SIA C O7  1 
HETATM 11477 O O8  . SIA O  3 .   ? -9.271  -16.725 91.488  1.00 110.27 ? 1   SIA C O8  1 
HETATM 11478 O O9  . SIA O  3 .   ? -11.875 -15.147 92.734  1.00 107.45 ? 1   SIA C O9  1 
HETATM 11479 O O10 . SIA O  3 .   ? -4.707  -14.153 95.093  1.00 110.72 ? 1   SIA C O10 1 
HETATM 11480 C C1  . GAL P  4 .   ? -10.239 -22.740 97.173  1.00 118.85 ? 2   GAL C C1  1 
HETATM 11481 C C2  . GAL P  4 .   ? -9.615  -22.205 95.882  1.00 118.65 ? 2   GAL C C2  1 
HETATM 11482 C C3  . GAL P  4 .   ? -9.479  -20.676 95.911  1.00 118.41 ? 2   GAL C C3  1 
HETATM 11483 C C4  . GAL P  4 .   ? -10.752 -19.990 96.427  1.00 119.14 ? 2   GAL C C4  1 
HETATM 11484 C C5  . GAL P  4 .   ? -11.335 -20.696 97.659  1.00 119.49 ? 2   GAL C C5  1 
HETATM 11485 C C6  . GAL P  4 .   ? -12.684 -20.105 98.071  1.00 118.84 ? 2   GAL C C6  1 
HETATM 11486 O O2  . GAL P  4 .   ? -8.351  -22.801 95.701  1.00 118.31 ? 2   GAL C O2  1 
HETATM 11487 O O3  . GAL P  4 .   ? -9.182  -20.171 94.617  1.00 117.38 ? 2   GAL C O3  1 
HETATM 11488 O O4  . GAL P  4 .   ? -11.718 -19.928 95.395  1.00 118.47 ? 2   GAL C O4  1 
HETATM 11489 O O5  . GAL P  4 .   ? -11.471 -22.088 97.421  1.00 119.74 ? 2   GAL C O5  1 
HETATM 11490 O O6  . GAL P  4 .   ? -12.926 -20.377 99.435  1.00 118.35 ? 2   GAL C O6  1 
HETATM 11491 C C1  . NAG Q  5 .   ? 9.131   -19.162 25.134  1.00 59.45  ? 331 NAG C C1  1 
HETATM 11492 C C2  . NAG Q  5 .   ? 10.641  -19.271 24.918  1.00 67.63  ? 331 NAG C C2  1 
HETATM 11493 C C3  . NAG Q  5 .   ? 11.372  -19.762 26.171  1.00 70.36  ? 331 NAG C C3  1 
HETATM 11494 C C4  . NAG Q  5 .   ? 10.830  -19.209 27.503  1.00 73.29  ? 331 NAG C C4  1 
HETATM 11495 C C5  . NAG Q  5 .   ? 9.302   -19.056 27.478  1.00 70.66  ? 331 NAG C C5  1 
HETATM 11496 C C6  . NAG Q  5 .   ? 8.774   -18.285 28.685  1.00 70.67  ? 331 NAG C C6  1 
HETATM 11497 C C7  . NAG Q  5 .   ? 11.472  -19.728 22.655  1.00 67.67  ? 331 NAG C C7  1 
HETATM 11498 C C8  . NAG Q  5 .   ? 11.710  -20.769 21.603  1.00 66.80  ? 331 NAG C C8  1 
HETATM 11499 N N2  . NAG Q  5 .   ? 10.934  -20.156 23.800  1.00 67.33  ? 331 NAG C N2  1 
HETATM 11500 O O3  . NAG Q  5 .   ? 12.736  -19.427 26.039  1.00 71.37  ? 331 NAG C O3  1 
HETATM 11501 O O4  . NAG Q  5 .   ? 11.188  -20.079 28.569  1.00 78.67  ? 331 NAG C O4  1 
HETATM 11502 O O5  . NAG Q  5 .   ? 8.880   -18.398 26.296  1.00 66.15  ? 331 NAG C O5  1 
HETATM 11503 O O6  . NAG Q  5 .   ? 7.535   -18.835 29.082  1.00 68.17  ? 331 NAG C O6  1 
HETATM 11504 O O7  . NAG Q  5 .   ? 11.771  -18.553 22.432  1.00 67.58  ? 331 NAG C O7  1 
HETATM 11505 C C1  . NAG R  5 .   ? 12.365  -19.627 29.279  1.00 82.91  ? 332 NAG C C1  1 
HETATM 11506 C C2  . NAG R  5 .   ? 12.290  -20.049 30.750  1.00 83.70  ? 332 NAG C C2  1 
HETATM 11507 C C3  . NAG R  5 .   ? 13.568  -19.673 31.510  1.00 85.12  ? 332 NAG C C3  1 
HETATM 11508 C C4  . NAG R  5 .   ? 14.840  -20.061 30.754  1.00 86.15  ? 332 NAG C C4  1 
HETATM 11509 C C5  . NAG R  5 .   ? 14.761  -19.658 29.277  1.00 86.13  ? 332 NAG C C5  1 
HETATM 11510 C C6  . NAG R  5 .   ? 15.931  -20.220 28.476  1.00 86.42  ? 332 NAG C C6  1 
HETATM 11511 C C7  . NAG R  5 .   ? 10.025  -20.099 31.711  1.00 79.57  ? 332 NAG C C7  1 
HETATM 11512 C C8  . NAG R  5 .   ? 8.959   -19.290 32.393  1.00 77.74  ? 332 NAG C C8  1 
HETATM 11513 N N2  . NAG R  5 .   ? 11.145  -19.440 31.406  1.00 81.71  ? 332 NAG C N2  1 
HETATM 11514 O O3  . NAG R  5 .   ? 13.581  -20.298 32.775  1.00 85.27  ? 332 NAG C O3  1 
HETATM 11515 O O4  . NAG R  5 .   ? 15.946  -19.447 31.383  1.00 86.16  ? 332 NAG C O4  1 
HETATM 11516 O O5  . NAG R  5 .   ? 13.557  -20.131 28.697  1.00 85.30  ? 332 NAG C O5  1 
HETATM 11517 O O6  . NAG R  5 .   ? 15.969  -19.609 27.205  1.00 85.66  ? 332 NAG C O6  1 
HETATM 11518 O O7  . NAG R  5 .   ? 9.835   -21.292 31.464  1.00 76.12  ? 332 NAG C O7  1 
HETATM 11519 C C1  . NAG S  5 .   ? -14.998 -13.421 56.130  1.00 44.96  ? 183 NAG D C1  1 
HETATM 11520 C C2  . NAG S  5 .   ? -15.832 -14.097 57.230  1.00 51.78  ? 183 NAG D C2  1 
HETATM 11521 C C3  . NAG S  5 .   ? -15.090 -15.236 57.953  1.00 53.15  ? 183 NAG D C3  1 
HETATM 11522 C C4  . NAG S  5 .   ? -14.255 -16.110 57.010  1.00 54.10  ? 183 NAG D C4  1 
HETATM 11523 C C5  . NAG S  5 .   ? -13.424 -15.227 56.073  1.00 54.42  ? 183 NAG D C5  1 
HETATM 11524 C C6  . NAG S  5 .   ? -12.571 -16.038 55.097  1.00 55.11  ? 183 NAG D C6  1 
HETATM 11525 C C7  . NAG S  5 .   ? -17.526 -12.661 58.305  1.00 50.48  ? 183 NAG D C7  1 
HETATM 11526 C C8  . NAG S  5 .   ? -17.770 -11.626 59.362  1.00 48.12  ? 183 NAG D C8  1 
HETATM 11527 N N2  . NAG S  5 .   ? -16.265 -13.094 58.194  1.00 51.22  ? 183 NAG D N2  1 
HETATM 11528 O O3  . NAG S  5 .   ? -16.025 -16.050 58.628  1.00 53.81  ? 183 NAG D O3  1 
HETATM 11529 O O4  . NAG S  5 .   ? -13.429 -16.987 57.750  1.00 53.04  ? 183 NAG D O4  1 
HETATM 11530 O O5  . NAG S  5 .   ? -14.300 -14.379 55.346  1.00 51.39  ? 183 NAG D O5  1 
HETATM 11531 O O6  . NAG S  5 .   ? -13.388 -16.629 54.109  1.00 56.08  ? 183 NAG D O6  1 
HETATM 11532 O O7  . NAG S  5 .   ? -18.465 -13.057 57.609  1.00 50.44  ? 183 NAG D O7  1 
HETATM 11533 C C1  . GOL T  6 .   ? 1.946   0.018   32.277  1.00 45.53  ? 184 GOL D C1  1 
HETATM 11534 O O1  . GOL T  6 .   ? 3.302   0.317   32.054  1.00 45.17  ? 184 GOL D O1  1 
HETATM 11535 C C2  . GOL T  6 .   ? 1.841   -0.806  33.549  1.00 49.75  ? 184 GOL D C2  1 
HETATM 11536 O O2  . GOL T  6 .   ? 0.583   -0.597  34.155  1.00 53.65  ? 184 GOL D O2  1 
HETATM 11537 C C3  . GOL T  6 .   ? 2.027   -2.273  33.192  1.00 50.37  ? 184 GOL D C3  1 
HETATM 11538 O O3  . GOL T  6 .   ? 1.045   -3.049  33.836  1.00 52.31  ? 184 GOL D O3  1 
HETATM 11539 C C1  . SIA U  3 .   ? -15.365 24.059  90.582  1.00 69.15  ? 1   SIA E C1  1 
HETATM 11540 C C2  . SIA U  3 .   ? -15.895 23.762  91.977  1.00 70.54  ? 1   SIA E C2  1 
HETATM 11541 C C3  . SIA U  3 .   ? -16.794 24.918  92.446  1.00 67.62  ? 1   SIA E C3  1 
HETATM 11542 C C4  . SIA U  3 .   ? -18.138 24.933  91.716  1.00 66.66  ? 1   SIA E C4  1 
HETATM 11543 C C5  . SIA U  3 .   ? -18.818 23.570  91.805  1.00 66.52  ? 1   SIA E C5  1 
HETATM 11544 C C6  . SIA U  3 .   ? -17.890 22.458  91.310  1.00 65.24  ? 1   SIA E C6  1 
HETATM 11545 C C7  . SIA U  3 .   ? -18.525 21.066  91.464  1.00 62.40  ? 1   SIA E C7  1 
HETATM 11546 C C8  . SIA U  3 .   ? -17.585 19.925  91.072  1.00 61.83  ? 1   SIA E C8  1 
HETATM 11547 C C9  . SIA U  3 .   ? -18.364 18.626  90.889  1.00 60.67  ? 1   SIA E C9  1 
HETATM 11548 C C10 . SIA U  3 .   ? -21.264 23.425  91.610  1.00 64.74  ? 1   SIA E C10 1 
HETATM 11549 C C11 . SIA U  3 .   ? -21.330 23.309  93.107  1.00 65.29  ? 1   SIA E C11 1 
HETATM 11550 N N5  . SIA U  3 .   ? -20.060 23.552  91.052  1.00 65.24  ? 1   SIA E N5  1 
HETATM 11551 O O1A . SIA U  3 .   ? -15.203 25.249  90.219  1.00 65.58  ? 1   SIA E O1A 1 
HETATM 11552 O O1B . SIA U  3 .   ? -15.091 23.096  89.830  1.00 66.51  ? 1   SIA E O1B 1 
HETATM 11553 O O4  . SIA U  3 .   ? -18.987 25.940  92.275  1.00 65.94  ? 1   SIA E O4  1 
HETATM 11554 O O6  . SIA U  3 .   ? -16.623 22.515  91.992  1.00 68.08  ? 1   SIA E O6  1 
HETATM 11555 O O7  . SIA U  3 .   ? -18.975 20.854  92.811  1.00 61.37  ? 1   SIA E O7  1 
HETATM 11556 O O8  . SIA U  3 .   ? -16.889 20.241  89.860  1.00 62.89  ? 1   SIA E O8  1 
HETATM 11557 O O9  . SIA U  3 .   ? -17.464 17.536  90.649  1.00 59.48  ? 1   SIA E O9  1 
HETATM 11558 O O10 . SIA U  3 .   ? -22.272 23.410  90.925  1.00 65.72  ? 1   SIA E O10 1 
HETATM 11559 C C1  . GAL V  4 .   ? -13.635 23.592  96.194  1.00 88.18  ? 2   GAL E C1  1 
HETATM 11560 C C2  . GAL V  4 .   ? -13.706 23.730  94.669  1.00 85.23  ? 2   GAL E C2  1 
HETATM 11561 C C3  . GAL V  4 .   ? -14.985 23.091  94.116  1.00 82.99  ? 2   GAL E C3  1 
HETATM 11562 C C4  . GAL V  4 .   ? -15.228 21.701  94.719  1.00 84.90  ? 2   GAL E C4  1 
HETATM 11563 C C5  . GAL V  4 .   ? -15.063 21.706  96.241  1.00 86.63  ? 2   GAL E C5  1 
HETATM 11564 C C6  . GAL V  4 .   ? -15.217 20.312  96.847  1.00 86.59  ? 2   GAL E C6  1 
HETATM 11565 O O2  . GAL V  4 .   ? -13.667 25.093  94.311  1.00 83.50  ? 2   GAL E O2  1 
HETATM 11566 O O3  . GAL V  4 .   ? -14.907 22.981  92.702  1.00 78.23  ? 2   GAL E O3  1 
HETATM 11567 O O4  . GAL V  4 .   ? -14.316 20.786  94.152  1.00 85.62  ? 2   GAL E O4  1 
HETATM 11568 O O5  . GAL V  4 .   ? -13.788 22.230  96.566  1.00 88.50  ? 2   GAL E O5  1 
HETATM 11569 O O6  . GAL V  4 .   ? -16.584 19.985  96.967  1.00 87.13  ? 2   GAL E O6  1 
HETATM 11570 C C1  . NAG W  5 .   ? -9.972  24.073  99.974  1.00 95.42  ? 3   NAG E C1  1 
HETATM 11571 C C2  . NAG W  5 .   ? -9.787  22.902  99.010  1.00 96.60  ? 3   NAG E C2  1 
HETATM 11572 C C3  . NAG W  5 .   ? -10.544 23.167  97.706  1.00 95.82  ? 3   NAG E C3  1 
HETATM 11573 C C4  . NAG W  5 .   ? -11.983 23.659  97.924  1.00 94.33  ? 3   NAG E C4  1 
HETATM 11574 C C5  . NAG W  5 .   ? -12.107 24.656  99.089  1.00 94.55  ? 3   NAG E C5  1 
HETATM 11575 C C6  . NAG W  5 .   ? -13.556 24.819  99.538  1.00 94.05  ? 3   NAG E C6  1 
HETATM 11576 C C7  . NAG W  5 .   ? -7.817  21.462  98.639  1.00 98.69  ? 3   NAG E C7  1 
HETATM 11577 C C8  . NAG W  5 .   ? -6.341  21.439  98.362  1.00 98.17  ? 3   NAG E C8  1 
HETATM 11578 N N2  . NAG W  5 .   ? -8.374  22.673  98.744  1.00 98.42  ? 3   NAG E N2  1 
HETATM 11579 O O1  . NAG W  5 .   ? -9.316  23.806  101.193 1.00 94.25  ? 3   NAG E O1  1 
HETATM 11580 O O3  . NAG W  5 .   ? -10.564 21.991  96.927  1.00 95.91  ? 3   NAG E O3  1 
HETATM 11581 O O4  . NAG W  5 .   ? -12.443 24.237  96.711  1.00 91.55  ? 3   NAG E O4  1 
HETATM 11582 O O5  . NAG W  5 .   ? -11.352 24.253  100.219 1.00 94.94  ? 3   NAG E O5  1 
HETATM 11583 O O6  . NAG W  5 .   ? -14.106 25.977  98.950  1.00 93.10  ? 3   NAG E O6  1 
HETATM 11584 O O7  . NAG W  5 .   ? -8.436  20.401  98.754  1.00 97.98  ? 3   NAG E O7  1 
HETATM 11585 C C1  . NAG X  5 .   ? 3.348   21.289  23.952  1.00 52.45  ? 331 NAG E C1  1 
HETATM 11586 C C2  . NAG X  5 .   ? 2.940   22.736  23.630  1.00 61.28  ? 331 NAG E C2  1 
HETATM 11587 C C3  . NAG X  5 .   ? 3.527   23.731  24.644  1.00 62.38  ? 331 NAG E C3  1 
HETATM 11588 C C4  . NAG X  5 .   ? 3.260   23.255  26.073  1.00 62.81  ? 331 NAG E C4  1 
HETATM 11589 C C5  . NAG X  5 .   ? 3.826   21.836  26.230  1.00 60.34  ? 331 NAG E C5  1 
HETATM 11590 C C6  . NAG X  5 .   ? 3.755   21.309  27.668  1.00 59.11  ? 331 NAG E C6  1 
HETATM 11591 C C7  . NAG X  5 .   ? 4.502   23.196  21.718  1.00 64.21  ? 331 NAG E C7  1 
HETATM 11592 C C8  . NAG X  5 .   ? 4.539   23.564  20.264  1.00 64.25  ? 331 NAG E C8  1 
HETATM 11593 N N2  . NAG X  5 .   ? 3.275   23.082  22.249  1.00 62.40  ? 331 NAG E N2  1 
HETATM 11594 O O3  . NAG X  5 .   ? 2.987   25.021  24.443  1.00 64.11  ? 331 NAG E O3  1 
HETATM 11595 O O4  . NAG X  5 .   ? 3.818   24.160  27.008  1.00 66.04  ? 331 NAG E O4  1 
HETATM 11596 O O5  . NAG X  5 .   ? 3.162   20.960  25.325  1.00 57.66  ? 331 NAG E O5  1 
HETATM 11597 O O6  . NAG X  5 .   ? 2.456   20.862  27.991  1.00 58.12  ? 331 NAG E O6  1 
HETATM 11598 O O7  . NAG X  5 .   ? 5.562   23.025  22.331  1.00 64.18  ? 331 NAG E O7  1 
HETATM 11599 C C1  . NAG Y  5 .   ? -3.242  5.352   59.060  1.00 54.01  ? 183 NAG F C1  1 
HETATM 11600 C C2  . NAG Y  5 .   ? -2.815  5.059   60.509  1.00 60.33  ? 183 NAG F C2  1 
HETATM 11601 C C3  . NAG Y  5 .   ? -2.406  6.336   61.255  1.00 61.02  ? 183 NAG F C3  1 
HETATM 11602 C C4  . NAG Y  5 .   ? -1.392  7.148   60.451  1.00 61.68  ? 183 NAG F C4  1 
HETATM 11603 C C5  . NAG Y  5 .   ? -1.935  7.405   59.042  1.00 61.49  ? 183 NAG F C5  1 
HETATM 11604 C C6  . NAG Y  5 .   ? -0.895  8.139   58.196  1.00 62.54  ? 183 NAG F C6  1 
HETATM 11605 C C7  . NAG Y  5 .   ? -3.682  3.240   61.940  1.00 59.98  ? 183 NAG F C7  1 
HETATM 11606 C C8  . NAG Y  5 .   ? -4.895  2.688   62.633  1.00 60.08  ? 183 NAG F C8  1 
HETATM 11607 N N2  . NAG Y  5 .   ? -3.868  4.369   61.244  1.00 60.09  ? 183 NAG F N2  1 
HETATM 11608 O O3  . NAG Y  5 .   ? -1.856  6.014   62.515  1.00 61.66  ? 183 NAG F O3  1 
HETATM 11609 O O4  . NAG Y  5 .   ? -1.102  8.366   61.113  1.00 60.65  ? 183 NAG F O4  1 
HETATM 11610 O O5  . NAG Y  5 .   ? -2.279  6.177   58.407  1.00 58.71  ? 183 NAG F O5  1 
HETATM 11611 O O6  . NAG Y  5 .   ? -1.332  8.235   56.858  1.00 62.92  ? 183 NAG F O6  1 
HETATM 11612 O O7  . NAG Y  5 .   ? -2.604  2.648   62.038  1.00 58.12  ? 183 NAG F O7  1 
HETATM 11613 C C1  . GOL Z  6 .   ? -10.663 8.719   30.711  1.00 42.42  ? 184 GOL F C1  1 
HETATM 11614 O O1  . GOL Z  6 .   ? -9.425  8.244   31.185  1.00 46.47  ? 184 GOL F O1  1 
HETATM 11615 C C2  . GOL Z  6 .   ? -11.359 7.601   29.952  1.00 40.72  ? 184 GOL F C2  1 
HETATM 11616 O O2  . GOL Z  6 .   ? -11.997 6.734   30.867  1.00 44.59  ? 184 GOL F O2  1 
HETATM 11617 C C3  . GOL Z  6 .   ? -12.389 8.228   29.027  1.00 35.38  ? 184 GOL F C3  1 
HETATM 11618 O O3  . GOL Z  6 .   ? -12.298 7.575   27.789  1.00 30.38  ? 184 GOL F O3  1 
HETATM 11619 O O   . HOH AA 7 .   ? -17.289 -13.721 81.505  1.00 2.00   ? 6   HOH A O   1 
HETATM 11620 O O   . HOH AA 7 .   ? -47.282 -17.320 76.350  1.00 15.95  ? 224 HOH A O   1 
HETATM 11621 O O   . HOH AA 7 .   ? -27.368 -31.175 73.206  1.00 8.60   ? 226 HOH A O   1 
HETATM 11622 O O   . HOH AA 7 .   ? -27.972 -12.204 50.867  1.00 30.41  ? 332 HOH A O   1 
HETATM 11623 O O   . HOH AA 7 .   ? -26.167 -3.577  66.426  1.00 23.85  ? 333 HOH A O   1 
HETATM 11624 O O   . HOH AA 7 .   ? -42.369 -2.873  36.254  1.00 2.00   ? 334 HOH A O   1 
HETATM 11625 O O   . HOH AA 7 .   ? -20.457 -1.809  9.797   1.00 2.00   ? 335 HOH A O   1 
HETATM 11626 O O   . HOH AA 7 .   ? -33.058 -25.562 87.239  1.00 7.40   ? 336 HOH A O   1 
HETATM 11627 O O   . HOH AA 7 .   ? -30.890 10.675  12.916  1.00 28.22  ? 337 HOH A O   1 
HETATM 11628 O O   . HOH AA 7 .   ? -29.750 -7.978  28.017  1.00 14.31  ? 338 HOH A O   1 
HETATM 11629 O O   . HOH AA 7 .   ? -43.824 -15.800 51.557  1.00 23.10  ? 339 HOH A O   1 
HETATM 11630 O O   . HOH AA 7 .   ? -29.367 -10.955 93.536  1.00 2.00   ? 340 HOH A O   1 
HETATM 11631 O O   . HOH AA 7 .   ? -19.767 4.157   6.114   1.00 2.00   ? 341 HOH A O   1 
HETATM 11632 O O   . HOH AA 7 .   ? -36.859 1.736   92.219  1.00 2.25   ? 342 HOH A O   1 
HETATM 11633 O O   . HOH AA 7 .   ? -40.129 -7.658  56.801  1.00 11.30  ? 343 HOH A O   1 
HETATM 11634 O O   . HOH AA 7 .   ? -45.344 -15.076 49.414  1.00 12.41  ? 344 HOH A O   1 
HETATM 11635 O O   . HOH AA 7 .   ? -30.339 0.023   28.850  1.00 19.62  ? 345 HOH A O   1 
HETATM 11636 O O   . HOH AA 7 .   ? -35.096 2.872   89.812  1.00 5.38   ? 346 HOH A O   1 
HETATM 11637 O O   . HOH AA 7 .   ? -44.071 -21.370 85.440  1.00 13.31  ? 347 HOH A O   1 
HETATM 11638 O O   . HOH AA 7 .   ? -14.324 3.640   -4.347  1.00 19.42  ? 348 HOH A O   1 
HETATM 11639 O O   . HOH AA 7 .   ? -37.520 -6.030  57.488  1.00 26.90  ? 349 HOH A O   1 
HETATM 11640 O O   . HOH AA 7 .   ? -18.177 -17.897 68.948  1.00 17.86  ? 350 HOH A O   1 
HETATM 11641 O O   . HOH AA 7 .   ? -24.045 -3.896  40.888  1.00 8.35   ? 351 HOH A O   1 
HETATM 11642 O O   . HOH AA 7 .   ? -24.496 -23.438 58.670  1.00 12.03  ? 352 HOH A O   1 
HETATM 11643 O O   . HOH AA 7 .   ? -18.611 -24.265 77.220  1.00 13.76  ? 353 HOH A O   1 
HETATM 11644 O O   . HOH AA 7 .   ? -36.170 -23.061 43.357  1.00 16.51  ? 354 HOH A O   1 
HETATM 11645 O O   . HOH AA 7 .   ? -29.102 -1.162  61.481  1.00 20.44  ? 355 HOH A O   1 
HETATM 11646 O O   . HOH AA 7 .   ? -36.249 -15.104 39.637  1.00 10.90  ? 356 HOH A O   1 
HETATM 11647 O O   . HOH AA 7 .   ? -44.438 -5.670  62.889  1.00 18.32  ? 357 HOH A O   1 
HETATM 11648 O O   . HOH AA 7 .   ? -15.501 -16.141 82.576  1.00 9.20   ? 358 HOH A O   1 
HETATM 11649 O O   . HOH AA 7 .   ? -19.208 -0.356  41.010  1.00 15.17  ? 359 HOH A O   1 
HETATM 11650 O O   . HOH AA 7 .   ? -32.388 -6.781  91.982  1.00 12.68  ? 360 HOH A O   1 
HETATM 11651 O O   . HOH AA 7 .   ? -26.849 8.819   17.404  1.00 23.71  ? 361 HOH A O   1 
HETATM 11652 O O   . HOH AA 7 .   ? -25.936 -2.547  81.040  1.00 5.38   ? 362 HOH A O   1 
HETATM 11653 O O   . HOH AA 7 .   ? -40.720 -25.717 75.743  1.00 8.88   ? 363 HOH A O   1 
HETATM 11654 O O   . HOH AA 7 .   ? -14.636 -19.112 77.222  1.00 17.54  ? 364 HOH A O   1 
HETATM 11655 O O   . HOH AA 7 .   ? -34.982 2.118   30.490  1.00 19.86  ? 365 HOH A O   1 
HETATM 11656 O O   . HOH AA 7 .   ? -43.563 -16.180 32.060  1.00 4.85   ? 366 HOH A O   1 
HETATM 11657 O O   . HOH AA 7 .   ? -37.497 -7.175  73.242  1.00 14.07  ? 367 HOH A O   1 
HETATM 11658 O O   . HOH AA 7 .   ? -26.489 6.334   43.067  1.00 19.03  ? 368 HOH A O   1 
HETATM 11659 O O   . HOH AA 7 .   ? -25.234 2.962   -2.977  1.00 2.00   ? 369 HOH A O   1 
HETATM 11660 O O   . HOH AA 7 .   ? -26.388 -22.005 55.083  1.00 21.58  ? 370 HOH A O   1 
HETATM 11661 O O   . HOH AA 7 .   ? -38.043 1.439   37.945  1.00 10.28  ? 371 HOH A O   1 
HETATM 11662 O O   . HOH AA 7 .   ? -37.244 -4.057  64.929  1.00 25.92  ? 372 HOH A O   1 
HETATM 11663 O O   . HOH AA 7 .   ? -41.638 -17.030 79.438  1.00 22.45  ? 373 HOH A O   1 
HETATM 11664 O O   . HOH AA 7 .   ? -31.420 -10.834 36.696  1.00 18.47  ? 374 HOH A O   1 
HETATM 11665 O O   . HOH AA 7 .   ? -42.148 -18.379 52.934  1.00 15.51  ? 375 HOH A O   1 
HETATM 11666 O O   . HOH AA 7 .   ? -46.081 -12.852 83.297  1.00 15.39  ? 376 HOH A O   1 
HETATM 11667 O O   . HOH AA 7 .   ? -43.308 -10.647 34.004  1.00 18.16  ? 377 HOH A O   1 
HETATM 11668 O O   . HOH BA 7 .   ? -20.514 -11.649 -19.901 1.00 2.00   ? 187 HOH B O   1 
HETATM 11669 O O   . HOH BA 7 .   ? -9.050  -0.365  33.140  1.00 19.17  ? 188 HOH B O   1 
HETATM 11670 O O   . HOH BA 7 .   ? -7.673  -7.020  11.861  1.00 24.73  ? 189 HOH B O   1 
HETATM 11671 O O   . HOH BA 7 .   ? -17.212 -4.083  -21.371 1.00 2.00   ? 190 HOH B O   1 
HETATM 11672 O O   . HOH BA 7 .   ? -6.716  8.224   3.105   1.00 2.00   ? 191 HOH B O   1 
HETATM 11673 O O   . HOH BA 7 .   ? -2.831  -1.085  -9.924  1.00 14.84  ? 192 HOH B O   1 
HETATM 11674 O O   . HOH BA 7 .   ? -30.546 5.123   2.856   1.00 16.73  ? 193 HOH B O   1 
HETATM 11675 O O   . HOH BA 7 .   ? -20.841 -9.231  33.085  1.00 24.16  ? 194 HOH B O   1 
HETATM 11676 O O   . HOH BA 7 .   ? -15.312 -13.376 -0.952  1.00 8.14   ? 195 HOH B O   1 
HETATM 11677 O O   . HOH BA 7 .   ? -22.410 4.728   48.368  1.00 10.77  ? 196 HOH B O   1 
HETATM 11678 O O   . HOH BA 7 .   ? -16.340 -11.220 -3.969  1.00 8.10   ? 197 HOH B O   1 
HETATM 11679 O O   . HOH BA 7 .   ? -10.635 9.478   8.378   1.00 22.29  ? 198 HOH B O   1 
HETATM 11680 O O   . HOH BA 7 .   ? -4.729  0.352   1.209   1.00 23.03  ? 199 HOH B O   1 
HETATM 11681 O O   . HOH BA 7 .   ? -2.192  4.983   -21.364 1.00 14.68  ? 200 HOH B O   1 
HETATM 11682 O O   . HOH BA 7 .   ? -9.610  -14.486 -16.332 1.00 9.21   ? 201 HOH B O   1 
HETATM 11683 O O   . HOH BA 7 .   ? -22.464 -4.529  -16.086 1.00 8.41   ? 202 HOH B O   1 
HETATM 11684 O O   . HOH BA 7 .   ? 0.069   -8.271  -15.612 1.00 9.92   ? 203 HOH B O   1 
HETATM 11685 O O   . HOH BA 7 .   ? -8.042  -10.967 0.930   1.00 14.43  ? 204 HOH B O   1 
HETATM 11686 O O   . HOH BA 7 .   ? -16.433 6.334   26.247  1.00 11.77  ? 205 HOH B O   1 
HETATM 11687 O O   . HOH BA 7 .   ? -15.537 6.277   3.166   1.00 2.52   ? 206 HOH B O   1 
HETATM 11688 O O   . HOH BA 7 .   ? -29.920 -1.458  -2.747  1.00 2.00   ? 207 HOH B O   1 
HETATM 11689 O O   . HOH BA 7 .   ? -7.308  8.958   -15.253 1.00 11.34  ? 208 HOH B O   1 
HETATM 11690 O O   . HOH BA 7 .   ? -8.294  9.029   10.872  1.00 6.73   ? 209 HOH B O   1 
HETATM 11691 O O   . HOH BA 7 .   ? -0.512  -5.395  1.442   1.00 19.50  ? 210 HOH B O   1 
HETATM 11692 O O   . HOH BA 7 .   ? -17.493 1.938   -18.982 1.00 4.59   ? 211 HOH B O   1 
HETATM 11693 O O   . HOH BA 7 .   ? -19.992 4.366   -6.779  1.00 18.04  ? 212 HOH B O   1 
HETATM 11694 O O   . HOH BA 7 .   ? 0.269   -12.953 -21.029 1.00 13.17  ? 213 HOH B O   1 
HETATM 11695 O O   . HOH BA 7 .   ? -9.119  2.362   -19.434 1.00 11.11  ? 214 HOH B O   1 
HETATM 11696 O O   . HOH BA 7 .   ? -12.444 -13.739 -2.237  1.00 28.97  ? 215 HOH B O   1 
HETATM 11697 O O   . HOH BA 7 .   ? -10.730 11.025  43.241  1.00 16.95  ? 216 HOH B O   1 
HETATM 11698 O O   . HOH BA 7 .   ? -27.847 -9.206  50.725  1.00 14.54  ? 217 HOH B O   1 
HETATM 11699 O O   . HOH BA 7 .   ? -27.588 1.909   56.632  1.00 11.76  ? 218 HOH B O   1 
HETATM 11700 O O   . HOH BA 7 .   ? 0.532   -3.721  -9.159  1.00 8.56   ? 219 HOH B O   1 
HETATM 11701 O O   . HOH BA 7 .   ? -6.498  1.939   32.898  1.00 17.15  ? 220 HOH B O   1 
HETATM 11702 O O   . HOH BA 7 .   ? -7.696  -13.465 -9.257  1.00 6.10   ? 221 HOH B O   1 
HETATM 11703 O O   . HOH BA 7 .   ? -16.442 -1.517  19.680  1.00 12.11  ? 222 HOH B O   1 
HETATM 11704 O O   . HOH BA 7 .   ? -25.277 -4.338  -15.862 1.00 9.39   ? 223 HOH B O   1 
HETATM 11705 O O   . HOH BA 7 .   ? -1.464  -16.622 -13.900 1.00 12.31  ? 233 HOH B O   1 
HETATM 11706 O O   . HOH BA 7 .   ? -7.378  -8.070  -26.763 1.00 8.99   ? 256 HOH B O   1 
HETATM 11707 O O   . HOH BA 7 .   ? -2.329  -3.735  -9.935  1.00 8.96   ? 266 HOH B O   1 
HETATM 11708 O O   . HOH BA 7 .   ? -25.518 7.947   63.917  1.00 21.24  ? 282 HOH B O   1 
HETATM 11709 O O   . HOH BA 7 .   ? -6.111  9.005   -2.638  1.00 2.00   ? 366 HOH B O   1 
HETATM 11710 O O   . HOH BA 7 .   ? -11.502 -0.860  31.404  1.00 14.60  ? 368 HOH B O   1 
HETATM 11711 O O   . HOH BA 7 .   ? -3.357  -5.917  2.601   1.00 16.25  ? 371 HOH B O   1 
HETATM 11712 O O   . HOH CA 7 .   ? -12.558 -4.601  82.881  1.00 10.09  ? 222 HOH C O   1 
HETATM 11713 O O   . HOH CA 7 .   ? -12.886 -13.133 23.114  1.00 17.21  ? 333 HOH C O   1 
HETATM 11714 O O   . HOH CA 7 .   ? -10.120 7.540   76.647  1.00 3.43   ? 334 HOH C O   1 
HETATM 11715 O O   . HOH CA 7 .   ? 2.884   -25.906 22.853  1.00 11.50  ? 335 HOH C O   1 
HETATM 11716 O O   . HOH CA 7 .   ? 0.988   -32.249 19.317  1.00 15.34  ? 336 HOH C O   1 
HETATM 11717 O O   . HOH CA 7 .   ? 13.342  -0.858  73.930  1.00 2.00   ? 337 HOH C O   1 
HETATM 11718 O O   . HOH CA 7 .   ? 5.634   -15.520 0.367   1.00 2.00   ? 338 HOH C O   1 
HETATM 11719 O O   . HOH CA 7 .   ? -16.860 -12.504 38.136  1.00 28.58  ? 339 HOH C O   1 
HETATM 11720 O O   . HOH CA 7 .   ? 9.377   -9.371  84.716  1.00 2.82   ? 340 HOH C O   1 
HETATM 11721 O O   . HOH CA 7 .   ? 7.499   0.775   65.293  1.00 8.64   ? 341 HOH C O   1 
HETATM 11722 O O   . HOH CA 7 .   ? 13.758  -5.425  65.348  1.00 8.33   ? 342 HOH C O   1 
HETATM 11723 O O   . HOH CA 7 .   ? -14.800 -15.153 99.805  1.00 14.85  ? 343 HOH C O   1 
HETATM 11724 O O   . HOH CA 7 .   ? 2.855   -31.497 21.358  1.00 12.48  ? 344 HOH C O   1 
HETATM 11725 O O   . HOH CA 7 .   ? 7.582   7.899   86.291  1.00 2.00   ? 345 HOH C O   1 
HETATM 11726 O O   . HOH CA 7 .   ? 11.890  -17.805 66.983  1.00 2.86   ? 346 HOH C O   1 
HETATM 11727 O O   . HOH CA 7 .   ? -7.597  -17.637 48.500  1.00 19.76  ? 347 HOH C O   1 
HETATM 11728 O O   . HOH CA 7 .   ? -2.499  -22.816 61.815  1.00 12.05  ? 348 HOH C O   1 
HETATM 11729 O O   . HOH CA 7 .   ? -5.999  -7.892  44.702  1.00 16.41  ? 349 HOH C O   1 
HETATM 11730 O O   . HOH CA 7 .   ? -5.712  -8.367  62.311  1.00 11.66  ? 350 HOH C O   1 
HETATM 11731 O O   . HOH CA 7 .   ? 1.126   -10.122 24.434  1.00 5.60   ? 351 HOH C O   1 
HETATM 11732 O O   . HOH CA 7 .   ? -4.406  -17.664 29.483  1.00 10.13  ? 352 HOH C O   1 
HETATM 11733 O O   . HOH CA 7 .   ? 2.129   -6.454  59.867  1.00 20.12  ? 353 HOH C O   1 
HETATM 11734 O O   . HOH CA 7 .   ? -3.545  -22.001 54.688  1.00 15.39  ? 354 HOH C O   1 
HETATM 11735 O O   . HOH CA 7 .   ? -3.437  -15.593 54.687  1.00 17.70  ? 355 HOH C O   1 
HETATM 11736 O O   . HOH CA 7 .   ? 14.401  11.232  82.371  1.00 2.00   ? 356 HOH C O   1 
HETATM 11737 O O   . HOH CA 7 .   ? 1.507   -17.980 68.468  1.00 21.70  ? 357 HOH C O   1 
HETATM 11738 O O   . HOH CA 7 .   ? -6.906  -22.114 45.030  1.00 5.76   ? 358 HOH C O   1 
HETATM 11739 O O   . HOH CA 7 .   ? 0.747   -16.555 7.608   1.00 2.00   ? 359 HOH C O   1 
HETATM 11740 O O   . HOH CA 7 .   ? -4.224  -25.131 58.228  1.00 13.41  ? 360 HOH C O   1 
HETATM 11741 O O   . HOH CA 7 .   ? 14.200  11.180  79.655  1.00 2.00   ? 361 HOH C O   1 
HETATM 11742 O O   . HOH CA 7 .   ? 10.816  -8.488  57.643  1.00 16.74  ? 362 HOH C O   1 
HETATM 11743 O O   . HOH CA 7 .   ? -6.860  -19.859 50.893  1.00 15.29  ? 363 HOH C O   1 
HETATM 11744 O O   . HOH CA 7 .   ? 12.816  -22.663 26.988  1.00 37.37  ? 364 HOH C O   1 
HETATM 11745 O O   . HOH CA 7 .   ? -1.987  -17.063 68.216  1.00 10.82  ? 365 HOH C O   1 
HETATM 11746 O O   . HOH CA 7 .   ? -1.932  -23.552 8.664   1.00 5.70   ? 366 HOH C O   1 
HETATM 11747 O O   . HOH CA 7 .   ? 14.608  -1.598  77.147  1.00 2.86   ? 367 HOH C O   1 
HETATM 11748 O O   . HOH CA 7 .   ? -7.012  -19.512 44.487  1.00 23.77  ? 368 HOH C O   1 
HETATM 11749 O O   . HOH CA 7 .   ? 7.063   -14.861 17.072  1.00 2.00   ? 369 HOH C O   1 
HETATM 11750 O O   . HOH CA 7 .   ? 0.921   -6.982  48.310  1.00 4.80   ? 370 HOH C O   1 
HETATM 11751 O O   . HOH CA 7 .   ? 13.021  -13.933 53.605  1.00 16.50  ? 371 HOH C O   1 
HETATM 11752 O O   . HOH CA 7 .   ? 11.561  -13.717 41.925  1.00 20.75  ? 372 HOH C O   1 
HETATM 11753 O O   . HOH CA 7 .   ? -0.302  -22.175 63.308  1.00 9.52   ? 373 HOH C O   1 
HETATM 11754 O O   . HOH CA 7 .   ? 5.113   -23.322 3.028   1.00 21.11  ? 374 HOH C O   1 
HETATM 11755 O O   . HOH CA 7 .   ? 0.515   -5.068  61.624  1.00 7.77   ? 375 HOH C O   1 
HETATM 11756 O O   . HOH CA 7 .   ? 2.965   -9.519  100.675 1.00 8.89   ? 376 HOH C O   1 
HETATM 11757 O O   . HOH CA 7 .   ? 0.328   -24.887 54.878  1.00 12.45  ? 377 HOH C O   1 
HETATM 11758 O O   . HOH DA 7 .   ? 8.905   -1.395  28.918  1.00 6.64   ? 185 HOH D O   1 
HETATM 11759 O O   . HOH DA 7 .   ? 6.805   -1.252  47.902  1.00 24.65  ? 186 HOH D O   1 
HETATM 11760 O O   . HOH DA 7 .   ? 9.863   0.615   3.014   1.00 3.41   ? 187 HOH D O   1 
HETATM 11761 O O   . HOH DA 7 .   ? -3.959  -7.953  53.937  1.00 16.07  ? 188 HOH D O   1 
HETATM 11762 O O   . HOH DA 7 .   ? 2.170   -5.076  3.112   1.00 10.13  ? 189 HOH D O   1 
HETATM 11763 O O   . HOH DA 7 .   ? 5.892   -1.896  14.812  1.00 30.73  ? 190 HOH D O   1 
HETATM 11764 O O   . HOH DA 7 .   ? 14.173  -0.531  -11.680 1.00 10.52  ? 191 HOH D O   1 
HETATM 11765 O O   . HOH DA 7 .   ? 20.747  -6.450  -16.471 1.00 2.00   ? 192 HOH D O   1 
HETATM 11766 O O   . HOH DA 7 .   ? 10.381  -4.932  9.926   1.00 2.00   ? 193 HOH D O   1 
HETATM 11767 O O   . HOH DA 7 .   ? 4.666   -0.109  44.410  1.00 18.13  ? 194 HOH D O   1 
HETATM 11768 O O   . HOH DA 7 .   ? -15.840 -4.746  42.562  1.00 7.20   ? 195 HOH D O   1 
HETATM 11769 O O   . HOH DA 7 .   ? -18.203 -3.400  43.650  1.00 19.46  ? 196 HOH D O   1 
HETATM 11770 O O   . HOH DA 7 .   ? -4.473  -17.365 1.474   1.00 24.22  ? 197 HOH D O   1 
HETATM 11771 O O   . HOH DA 7 .   ? -4.765  -8.540  16.782  1.00 18.11  ? 198 HOH D O   1 
HETATM 11772 O O   . HOH DA 7 .   ? 20.547  -24.047 -3.437  1.00 2.00   ? 199 HOH D O   1 
HETATM 11773 O O   . HOH DA 7 .   ? 21.214  -10.114 -14.897 1.00 2.00   ? 200 HOH D O   1 
HETATM 11774 O O   . HOH DA 7 .   ? 26.419  -16.042 -7.021  1.00 2.00   ? 201 HOH D O   1 
HETATM 11775 O O   . HOH DA 7 .   ? 9.643   -1.458  31.521  1.00 18.52  ? 202 HOH D O   1 
HETATM 11776 O O   . HOH DA 7 .   ? 23.084  -7.026  -6.993  1.00 4.39   ? 203 HOH D O   1 
HETATM 11777 O O   . HOH DA 7 .   ? 17.351  0.177   -5.429  1.00 4.48   ? 204 HOH D O   1 
HETATM 11778 O O   . HOH DA 7 .   ? -6.202  -3.579  32.571  1.00 19.66  ? 205 HOH D O   1 
HETATM 11779 O O   . HOH DA 7 .   ? -1.985  -6.745  61.327  1.00 15.12  ? 206 HOH D O   1 
HETATM 11780 O O   . HOH DA 7 .   ? 5.194   1.671   3.140   1.00 2.00   ? 207 HOH D O   1 
HETATM 11781 O O   . HOH DA 7 .   ? 18.811  -7.945  8.950   1.00 18.12  ? 231 HOH D O   1 
HETATM 11782 O O   . HOH DA 7 .   ? 0.938   -11.940 14.006  1.00 2.00   ? 236 HOH D O   1 
HETATM 11783 O O   . HOH DA 7 .   ? 27.089  -6.114  2.543   1.00 2.00   ? 259 HOH D O   1 
HETATM 11784 O O   . HOH DA 7 .   ? 0.605   -0.146  50.560  1.00 15.95  ? 262 HOH D O   1 
HETATM 11785 O O   . HOH DA 7 .   ? 15.239  -9.256  -24.518 1.00 13.56  ? 277 HOH D O   1 
HETATM 11786 O O   . HOH DA 7 .   ? -21.129 -2.456  45.840  1.00 2.00   ? 365 HOH D O   1 
HETATM 11787 O O   . HOH EA 7 .   ? -10.245 20.584  66.128  1.00 5.53   ? 5   HOH E O   1 
HETATM 11788 O O   . HOH EA 7 .   ? -16.682 7.934   71.213  1.00 15.07  ? 143 HOH E O   1 
HETATM 11789 O O   . HOH EA 7 .   ? 8.857   13.151  33.809  1.00 4.35   ? 223 HOH E O   1 
HETATM 11790 O O   . HOH EA 7 .   ? -10.326 23.463  65.500  1.00 4.60   ? 228 HOH E O   1 
HETATM 11791 O O   . HOH EA 7 .   ? -3.726  21.732  35.914  1.00 5.83   ? 332 HOH E O   1 
HETATM 11792 O O   . HOH EA 7 .   ? -31.104 28.972  89.751  1.00 11.19  ? 333 HOH E O   1 
HETATM 11793 O O   . HOH EA 7 .   ? -26.292 24.946  52.353  1.00 19.77  ? 334 HOH E O   1 
HETATM 11794 O O   . HOH EA 7 .   ? -6.236  6.562   44.872  1.00 2.00   ? 335 HOH E O   1 
HETATM 11795 O O   . HOH EA 7 .   ? 11.569  12.155  2.303   1.00 2.94   ? 336 HOH E O   1 
HETATM 11796 O O   . HOH EA 7 .   ? -8.848  22.893  40.689  1.00 2.28   ? 337 HOH E O   1 
HETATM 11797 O O   . HOH EA 7 .   ? -28.056 8.390   68.732  1.00 27.79  ? 338 HOH E O   1 
HETATM 11798 O O   . HOH EA 7 .   ? -24.689 7.951   69.697  1.00 9.77   ? 339 HOH E O   1 
HETATM 11799 O O   . HOH EA 7 .   ? -19.193 6.080   72.313  1.00 14.41  ? 340 HOH E O   1 
HETATM 11800 O O   . HOH EA 7 .   ? -25.061 9.799   96.358  1.00 8.94   ? 341 HOH E O   1 
HETATM 11801 O O   . HOH EA 7 .   ? -18.710 14.414  57.021  1.00 4.26   ? 342 HOH E O   1 
HETATM 11802 O O   . HOH EA 7 .   ? -15.446 20.537  46.902  1.00 13.96  ? 343 HOH E O   1 
HETATM 11803 O O   . HOH EA 7 .   ? -25.002 26.813  54.741  1.00 18.96  ? 344 HOH E O   1 
HETATM 11804 O O   . HOH EA 7 .   ? 4.035   22.165  45.660  1.00 10.35  ? 345 HOH E O   1 
HETATM 11805 O O   . HOH EA 7 .   ? 8.963   9.624   30.702  1.00 17.19  ? 346 HOH E O   1 
HETATM 11806 O O   . HOH EA 7 .   ? -22.434 15.217  101.279 1.00 2.00   ? 347 HOH E O   1 
HETATM 11807 O O   . HOH EA 7 .   ? -27.602 20.528  69.691  1.00 2.00   ? 348 HOH E O   1 
HETATM 11808 O O   . HOH EA 7 .   ? -32.347 9.563   95.177  1.00 2.00   ? 349 HOH E O   1 
HETATM 11809 O O   . HOH EA 7 .   ? -10.813 31.134  64.537  1.00 2.74   ? 350 HOH E O   1 
HETATM 11810 O O   . HOH EA 7 .   ? -33.971 6.519   91.031  1.00 4.35   ? 351 HOH E O   1 
HETATM 11811 O O   . HOH EA 7 .   ? -10.717 18.535  40.887  1.00 21.77  ? 352 HOH E O   1 
HETATM 11812 O O   . HOH EA 7 .   ? -32.624 12.259  98.548  1.00 11.12  ? 353 HOH E O   1 
HETATM 11813 O O   . HOH EA 7 .   ? -6.189  28.604  61.908  1.00 11.39  ? 354 HOH E O   1 
HETATM 11814 O O   . HOH EA 7 .   ? -10.972 12.390  47.452  1.00 23.80  ? 355 HOH E O   1 
HETATM 11815 O O   . HOH EA 7 .   ? -4.241  22.519  62.446  1.00 10.55  ? 356 HOH E O   1 
HETATM 11816 O O   . HOH EA 7 .   ? -6.538  29.041  66.443  1.00 11.69  ? 357 HOH E O   1 
HETATM 11817 O O   . HOH EA 7 .   ? 2.928   11.691  48.123  1.00 10.85  ? 358 HOH E O   1 
HETATM 11818 O O   . HOH EA 7 .   ? 16.160  18.841  -10.711 1.00 2.68   ? 359 HOH E O   1 
HETATM 11819 O O   . HOH EA 7 .   ? -33.052 0.715   81.109  1.00 20.53  ? 360 HOH E O   1 
HETATM 11820 O O   . HOH EA 7 .   ? -26.525 7.368   92.131  1.00 9.10   ? 361 HOH E O   1 
HETATM 11821 O O   . HOH EA 7 .   ? -31.364 19.548  61.178  1.00 11.30  ? 362 HOH E O   1 
HETATM 11822 O O   . HOH EA 7 .   ? -0.329  19.187  31.891  1.00 2.00   ? 363 HOH E O   1 
HETATM 11823 O O   . HOH EA 7 .   ? 2.122   20.076  36.601  1.00 22.37  ? 364 HOH E O   1 
HETATM 11824 O O   . HOH EA 7 .   ? -25.809 33.734  66.915  1.00 7.42   ? 365 HOH E O   1 
HETATM 11825 O O   . HOH EA 7 .   ? -13.535 31.730  60.017  1.00 6.91   ? 366 HOH E O   1 
HETATM 11826 O O   . HOH EA 7 .   ? -6.079  31.606  58.222  1.00 2.97   ? 367 HOH E O   1 
HETATM 11827 O O   . HOH EA 7 .   ? -11.653 14.637  85.910  1.00 8.88   ? 368 HOH E O   1 
HETATM 11828 O O   . HOH EA 7 .   ? 5.073   8.674   29.900  1.00 2.00   ? 369 HOH E O   1 
HETATM 11829 O O   . HOH EA 7 .   ? -2.179  13.471  55.009  1.00 19.32  ? 370 HOH E O   1 
HETATM 11830 O O   . HOH EA 7 .   ? 6.898   2.240   21.546  1.00 2.00   ? 371 HOH E O   1 
HETATM 11831 O O   . HOH EA 7 .   ? -41.057 10.779  74.487  1.00 2.00   ? 372 HOH E O   1 
HETATM 11832 O O   . HOH EA 7 .   ? -8.868  18.978  67.761  1.00 3.04   ? 373 HOH E O   1 
HETATM 11833 O O   . HOH EA 7 .   ? -12.729 19.736  65.839  1.00 2.17   ? 374 HOH E O   1 
HETATM 11834 O O   . HOH EA 7 .   ? -23.799 7.220   82.123  1.00 4.73   ? 375 HOH E O   1 
HETATM 11835 O O   . HOH EA 7 .   ? -22.306 9.221   81.115  1.00 6.78   ? 376 HOH E O   1 
HETATM 11836 O O   . HOH EA 7 .   ? -18.704 16.785  99.058  1.00 2.43   ? 377 HOH E O   1 
HETATM 11837 O O   . HOH EA 7 .   ? -40.805 22.284  75.167  1.00 11.22  ? 378 HOH E O   1 
HETATM 11838 O O   . HOH EA 7 .   ? -36.231 6.705   92.984  1.00 4.17   ? 379 HOH E O   1 
HETATM 11839 O O   . HOH EA 7 .   ? -28.996 17.456  87.777  1.00 19.00  ? 380 HOH E O   1 
HETATM 11840 O O   . HOH EA 7 .   ? -2.353  32.542  46.540  1.00 7.18   ? 381 HOH E O   1 
HETATM 11841 O O   . HOH EA 7 .   ? -40.832 12.507  61.386  1.00 18.79  ? 382 HOH E O   1 
HETATM 11842 O O   . HOH EA 7 .   ? -0.291  10.271  24.212  1.00 4.50   ? 383 HOH E O   1 
HETATM 11843 O O   . HOH FA 7 .   ? -4.397  7.348   -1.252  1.00 2.00   ? 185 HOH F O   1 
HETATM 11844 O O   . HOH FA 7 .   ? -0.970  3.641   4.525   1.00 21.77  ? 186 HOH F O   1 
HETATM 11845 O O   . HOH FA 7 .   ? -7.746  8.497   62.793  1.00 4.87   ? 187 HOH F O   1 
HETATM 11846 O O   . HOH FA 7 .   ? -2.026  1.152   58.885  1.00 8.98   ? 188 HOH F O   1 
HETATM 11847 O O   . HOH FA 7 .   ? 15.954  11.039  1.063   1.00 3.16   ? 189 HOH F O   1 
HETATM 11848 O O   . HOH FA 7 .   ? 8.262   0.196   15.285  1.00 13.55  ? 190 HOH F O   1 
HETATM 11849 O O   . HOH FA 7 .   ? -5.380  -5.533  46.566  1.00 2.24   ? 191 HOH F O   1 
HETATM 11850 O O   . HOH FA 7 .   ? 4.111   6.286   -7.826  1.00 11.28  ? 192 HOH F O   1 
HETATM 11851 O O   . HOH FA 7 .   ? 0.889   8.437   -15.518 1.00 11.62  ? 193 HOH F O   1 
HETATM 11852 O O   . HOH FA 7 .   ? -3.862  10.497  -10.112 1.00 6.39   ? 194 HOH F O   1 
HETATM 11853 O O   . HOH FA 7 .   ? 0.264   0.094   41.652  1.00 2.00   ? 195 HOH F O   1 
HETATM 11854 O O   . HOH FA 7 .   ? -4.824  7.864   11.900  1.00 22.02  ? 196 HOH F O   1 
HETATM 11855 O O   . HOH FA 7 .   ? -10.604 17.155  18.060  1.00 21.33  ? 197 HOH F O   1 
HETATM 11856 O O   . HOH FA 7 .   ? -11.690 4.990   43.390  1.00 8.04   ? 198 HOH F O   1 
HETATM 11857 O O   . HOH FA 7 .   ? 6.823   2.423   18.516  1.00 4.11   ? 199 HOH F O   1 
HETATM 11858 O O   . HOH FA 7 .   ? -3.371  -1.393  57.451  1.00 3.67   ? 200 HOH F O   1 
HETATM 11859 O O   . HOH FA 7 .   ? 1.161   13.220  -21.782 1.00 7.49   ? 201 HOH F O   1 
HETATM 11860 O O   . HOH FA 7 .   ? 6.119   28.428  13.324  1.00 2.00   ? 202 HOH F O   1 
HETATM 11861 O O   . HOH FA 7 .   ? -3.130  5.064   2.888   1.00 15.69  ? 203 HOH F O   1 
HETATM 11862 O O   . HOH FA 7 .   ? 11.117  14.487  7.441   1.00 2.00   ? 204 HOH F O   1 
HETATM 11863 O O   . HOH FA 7 .   ? -0.816  4.399   -11.910 1.00 13.08  ? 205 HOH F O   1 
HETATM 11864 O O   . HOH FA 7 .   ? -0.878  19.740  -13.873 1.00 10.34  ? 206 HOH F O   1 
HETATM 11865 O O   . HOH FA 7 .   ? -5.387  -2.743  45.214  1.00 10.11  ? 245 HOH F O   1 
HETATM 11866 O O   . HOH FA 7 .   ? 7.127   6.228   14.799  1.00 15.74  ? 250 HOH F O   1 
HETATM 11867 O O   . HOH FA 7 .   ? -15.171 15.953  54.715  1.00 10.85  ? 257 HOH F O   1 
HETATM 11868 O O   . HOH FA 7 .   ? -13.316 -0.483  53.145  1.00 7.05   ? 272 HOH F O   1 
HETATM 11869 O O   . HOH FA 7 .   ? 12.284  25.362  -6.503  1.00 23.28  ? 273 HOH F O   1 
HETATM 11870 O O   . HOH FA 7 .   ? -10.451 10.498  55.280  1.00 14.23  ? 278 HOH F O   1 
HETATM 11871 O O   . HOH FA 7 .   ? -17.487 10.548  55.769  1.00 3.68   ? 284 HOH F O   1 
HETATM 11872 O O   . HOH FA 7 .   ? -13.807 11.860  36.712  1.00 17.80  ? 321 HOH F O   1 
HETATM 11873 O O   . HOH FA 7 .   ? -8.695  19.887  26.433  1.00 16.37  ? 327 HOH F O   1 
HETATM 11874 O O   . HOH FA 7 .   ? -4.293  10.219  -4.271  1.00 2.00   ? 367 HOH F O   1 
HETATM 11875 O O   . HOH FA 7 .   ? -13.397 15.620  21.834  1.00 2.00   ? 369 HOH F 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   ALA 1   7   ?   ?   ?   A . n 
A 1 2   ASP 2   8   ?   ?   ?   A . n 
A 1 3   PRO 3   9   ?   ?   ?   A . n 
A 1 4   GLY 4   10  10  GLY GLY A . n 
A 1 5   ASP 5   11  11  ASP ASP A . n 
A 1 6   LYS 6   12  12  LYS LYS A . n 
A 1 7   ILE 7   13  13  ILE ILE A . n 
A 1 8   CYS 8   14  14  CYS CYS A . n 
A 1 9   LEU 9   15  15  LEU LEU A . n 
A 1 10  GLY 10  16  16  GLY GLY A . n 
A 1 11  HIS 11  17  17  HIS HIS A . n 
A 1 12  HIS 12  18  18  HIS HIS A . n 
A 1 13  ALA 13  19  19  ALA ALA A . n 
A 1 14  VAL 14  20  20  VAL VAL A . n 
A 1 15  ALA 15  21  21  ALA ALA A . n 
A 1 16  ASN 16  22  22  ASN ASN A . n 
A 1 17  GLY 17  23  23  GLY GLY A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  LYS 19  25  25  LYS LYS A . n 
A 1 20  VAL 20  26  26  VAL VAL A . n 
A 1 21  ASN 21  27  27  ASN ASN A . n 
A 1 22  THR 22  28  28  THR THR A . n 
A 1 23  LEU 23  29  29  LEU LEU A . n 
A 1 24  THR 24  30  30  THR THR A . n 
A 1 25  GLU 25  31  31  GLU GLU A . n 
A 1 26  ARG 26  32  32  ARG ARG A . n 
A 1 27  GLY 27  33  33  GLY GLY A . n 
A 1 28  ILE 28  34  34  ILE ILE A . n 
A 1 29  GLU 29  35  35  GLU GLU A . n 
A 1 30  VAL 30  36  36  VAL VAL A . n 
A 1 31  VAL 31  37  37  VAL VAL A . n 
A 1 32  ASN 32  38  38  ASN ASN A . n 
A 1 33  ALA 33  39  39  ALA ALA A . n 
A 1 34  THR 34  40  40  THR THR A . n 
A 1 35  GLU 35  41  41  GLU GLU A . n 
A 1 36  THR 36  42  42  THR THR A . n 
A 1 37  VAL 37  43  43  VAL VAL A . n 
A 1 38  GLU 38  44  44  GLU GLU A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ASN 41  47  47  ASN ASN A . n 
A 1 42  ILE 42  48  48  ILE ILE A . n 
A 1 43  LYS 43  49  49  LYS LYS A . n 
A 1 44  LYS 44  50  50  LYS LYS A . n 
A 1 45  ILE 45  51  51  ILE ILE A . n 
A 1 46  CYS 46  52  52  CYS CYS A . n 
A 1 47  THR 47  53  53  THR THR A . n 
A 1 48  GLN 48  54  54  GLN GLN A . n 
A 1 49  GLY 49  55  55  GLY GLY A . n 
A 1 50  LYS 50  56  56  LYS LYS A . n 
A 1 51  ARG 51  57  57  ARG ARG A . n 
A 1 52  PRO 52  58  58  PRO PRO A . n 
A 1 53  THR 53  59  59  THR THR A . n 
A 1 54  ASP 54  60  60  ASP ASP A . n 
A 1 55  LEU 55  61  61  LEU LEU A . n 
A 1 56  GLY 56  62  62  GLY GLY A . n 
A 1 57  GLN 57  63  63  GLN GLN A . n 
A 1 58  CYS 58  64  64  CYS CYS A . n 
A 1 59  GLY 59  65  65  GLY GLY A . n 
A 1 60  LEU 60  66  66  LEU LEU A . n 
A 1 61  LEU 61  67  67  LEU LEU A . n 
A 1 62  GLY 62  68  68  GLY GLY A . n 
A 1 63  THR 63  69  69  THR THR A . n 
A 1 64  LEU 64  70  70  LEU LEU A . n 
A 1 65  ILE 65  71  71  ILE ILE A . n 
A 1 66  GLY 66  72  72  GLY GLY A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  PRO 68  74  74  PRO PRO A . n 
A 1 69  GLN 69  75  75  GLN GLN A . n 
A 1 70  CYS 70  76  76  CYS CYS A . n 
A 1 71  ASP 71  77  77  ASP ASP A . n 
A 1 72  GLN 72  78  78  GLN GLN A . n 
A 1 73  PHE 73  79  79  PHE PHE A . n 
A 1 74  LEU 74  80  80  LEU LEU A . n 
A 1 75  GLU 75  81  81  GLU GLU A . n 
A 1 76  PHE 76  82  82  PHE PHE A . n 
A 1 77  SER 77  83  83  SER SER A . n 
A 1 78  SER 78  84  84  SER SER A . n 
A 1 79  ASP 79  85  85  ASP ASP A . n 
A 1 80  LEU 80  86  86  LEU LEU A . n 
A 1 81  ILE 81  87  87  ILE ILE A . n 
A 1 82  ILE 82  88  88  ILE ILE A . n 
A 1 83  GLU 83  89  89  GLU GLU A . n 
A 1 84  ARG 84  90  90  ARG ARG A . n 
A 1 85  ARG 85  91  91  ARG ARG A . n 
A 1 86  GLU 86  92  92  GLU GLU A . n 
A 1 87  GLY 87  93  93  GLY GLY A . n 
A 1 88  THR 88  94  94  THR THR A . n 
A 1 89  ASP 89  95  95  ASP ASP A . n 
A 1 90  ILE 90  96  96  ILE ILE A . n 
A 1 91  CYS 91  97  97  CYS CYS A . n 
A 1 92  TYR 92  98  98  TYR TYR A . n 
A 1 93  PRO 93  99  99  PRO PRO A . n 
A 1 94  GLY 94  100 100 GLY GLY A . n 
A 1 95  ARG 95  101 101 ARG ARG A . n 
A 1 96  PHE 96  102 102 PHE PHE A . n 
A 1 97  THR 97  103 103 THR THR A . n 
A 1 98  ASN 98  104 104 ASN ASN A . n 
A 1 99  GLU 99  105 105 GLU GLU A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 SER 101 107 107 SER SER A . n 
A 1 102 LEU 102 108 108 LEU LEU A . n 
A 1 103 ARG 103 109 109 ARG ARG A . n 
A 1 104 GLN 104 110 110 GLN GLN A . n 
A 1 105 ILE 105 111 111 ILE ILE A . n 
A 1 106 LEU 106 112 112 LEU LEU A . n 
A 1 107 ARG 107 113 113 ARG ARG A . n 
A 1 108 ARG 108 114 114 ARG ARG A . n 
A 1 109 SER 109 115 115 SER SER A . n 
A 1 110 GLY 110 116 116 GLY GLY A . n 
A 1 111 GLY 111 117 117 GLY GLY A . n 
A 1 112 ILE 112 118 118 ILE ILE A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 LYS 114 120 120 LYS LYS A . n 
A 1 115 GLU 115 121 121 GLU GLU A . n 
A 1 116 SER 116 122 122 SER SER A . n 
A 1 117 MET 117 123 123 MET MET A . n 
A 1 118 GLY 118 124 124 GLY GLY A . n 
A 1 119 PHE 119 125 125 PHE PHE A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 TYR 121 127 127 TYR TYR A . n 
A 1 122 SER 122 128 128 SER SER A . n 
A 1 123 GLY 123 129 129 GLY GLY A . n 
A 1 124 ILE 124 130 130 ILE ILE A . n 
A 1 125 ARG 125 131 131 ARG ARG A . n 
A 1 126 THR 126 132 132 THR THR A . n 
A 1 127 ASN 127 133 133 ASN ASN A . n 
A 1 128 GLY 128 134 134 GLY GLY A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 THR 130 136 136 THR THR A . n 
A 1 131 SER 131 137 137 SER SER A . n 
A 1 132 ALA 132 138 138 ALA ALA A . n 
A 1 133 CYS 133 139 139 CYS CYS A . n 
A 1 134 THR 134 140 140 THR THR A . n 
A 1 135 ARG 135 141 141 ARG ARG A . n 
A 1 136 SER 136 142 142 SER SER A . n 
A 1 137 GLY 137 144 144 GLY GLY A . n 
A 1 138 SER 138 145 145 SER SER A . n 
A 1 139 SER 139 146 146 SER SER A . n 
A 1 140 PHE 140 147 147 PHE PHE A . n 
A 1 141 TYR 141 148 148 TYR TYR A . n 
A 1 142 ALA 142 149 149 ALA ALA A . n 
A 1 143 GLU 143 150 150 GLU GLU A . n 
A 1 144 MET 144 151 151 MET MET A . n 
A 1 145 LYS 145 152 152 LYS LYS A . n 
A 1 146 TRP 146 153 153 TRP TRP A . n 
A 1 147 LEU 147 154 154 LEU LEU A . n 
A 1 148 LEU 148 155 155 LEU LEU A . n 
A 1 149 SER 149 156 156 SER SER A . n 
A 1 150 ASN 150 157 157 ASN ASN A . n 
A 1 151 SER 151 158 158 SER SER A . n 
A 1 152 ASP 152 158 158 ASP ASP A A n 
A 1 153 ASN 153 158 158 ASN ASN A B n 
A 1 154 ALA 154 159 159 ALA ALA A . n 
A 1 155 ALA 155 160 160 ALA ALA A . n 
A 1 156 PHE 156 161 161 PHE PHE A . n 
A 1 157 PRO 157 162 162 PRO PRO A . n 
A 1 158 GLN 158 163 163 GLN GLN A . n 
A 1 159 MET 159 164 164 MET MET A . n 
A 1 160 THR 160 165 165 THR THR A . n 
A 1 161 LYS 161 166 166 LYS LYS A . n 
A 1 162 ALA 162 167 167 ALA ALA A . n 
A 1 163 TYR 163 168 168 TYR TYR A . n 
A 1 164 ARG 164 169 169 ARG ARG A . n 
A 1 165 ASN 165 170 170 ASN ASN A . n 
A 1 166 PRO 166 171 171 PRO PRO A . n 
A 1 167 ARG 167 172 172 ARG ARG A . n 
A 1 168 ASN 168 173 173 ASN ASN A . n 
A 1 169 LYS 169 174 174 LYS LYS A . n 
A 1 170 PRO 170 175 175 PRO PRO A . n 
A 1 171 ALA 171 176 176 ALA ALA A . n 
A 1 172 LEU 172 177 177 LEU LEU A . n 
A 1 173 ILE 173 178 178 ILE ILE A . n 
A 1 174 ILE 174 179 179 ILE ILE A . n 
A 1 175 TRP 175 180 180 TRP TRP A . n 
A 1 176 GLY 176 181 181 GLY GLY A . n 
A 1 177 VAL 177 182 182 VAL VAL A . n 
A 1 178 HIS 178 183 183 HIS HIS A . n 
A 1 179 HIS 179 184 184 HIS HIS A . n 
A 1 180 SER 180 185 185 SER SER A . n 
A 1 181 GLU 181 186 186 GLU GLU A . n 
A 1 182 SER 182 187 187 SER SER A . n 
A 1 183 VAL 183 188 188 VAL VAL A . n 
A 1 184 SER 184 189 189 SER SER A . n 
A 1 185 GLU 185 190 190 GLU GLU A . n 
A 1 186 GLN 186 191 191 GLN GLN A . n 
A 1 187 THR 187 192 192 THR THR A . n 
A 1 188 LYS 188 193 193 LYS LYS A . n 
A 1 189 LEU 189 194 194 LEU LEU A . n 
A 1 190 TYR 190 195 195 TYR TYR A . n 
A 1 191 GLY 191 196 196 GLY GLY A . n 
A 1 192 SER 192 197 197 SER SER A . n 
A 1 193 GLY 193 198 198 GLY GLY A . n 
A 1 194 ASN 194 199 199 ASN ASN A . n 
A 1 195 LYS 195 200 200 LYS LYS A . n 
A 1 196 LEU 196 201 201 LEU LEU A . n 
A 1 197 ILE 197 202 202 ILE ILE A . n 
A 1 198 THR 198 203 203 THR THR A . n 
A 1 199 VAL 199 204 204 VAL VAL A . n 
A 1 200 ARG 200 205 205 ARG ARG A . n 
A 1 201 SER 201 206 206 SER SER A . n 
A 1 202 SER 202 207 207 SER SER A . n 
A 1 203 LYS 203 208 208 LYS LYS A . n 
A 1 204 TYR 204 209 209 TYR TYR A . n 
A 1 205 GLN 205 210 210 GLN GLN A . n 
A 1 206 GLN 206 211 211 GLN GLN A . n 
A 1 207 SER 207 212 212 SER SER A . n 
A 1 208 PHE 208 213 213 PHE PHE A . n 
A 1 209 THR 209 214 214 THR THR A . n 
A 1 210 PRO 210 215 215 PRO PRO A . n 
A 1 211 ASN 211 216 216 ASN ASN A . n 
A 1 212 PRO 212 217 217 PRO PRO A . n 
A 1 213 GLY 213 218 218 GLY GLY A . n 
A 1 214 ALA 214 219 219 ALA ALA A . n 
A 1 215 ARG 215 220 220 ARG ARG A . n 
A 1 216 ARG 216 229 229 ARG ARG A . n 
A 1 217 ILE 217 230 230 ILE ILE A . n 
A 1 218 ASP 218 231 231 ASP ASP A . n 
A 1 219 PHE 219 232 232 PHE PHE A . n 
A 1 220 HIS 220 233 233 HIS HIS A . n 
A 1 221 TRP 221 234 234 TRP TRP A . n 
A 1 222 LEU 222 235 235 LEU LEU A . n 
A 1 223 LEU 223 236 236 LEU LEU A . n 
A 1 224 LEU 224 237 237 LEU LEU A . n 
A 1 225 ASP 225 238 238 ASP ASP A . n 
A 1 226 PRO 226 239 239 PRO PRO A . n 
A 1 227 ASN 227 240 240 ASN ASN A . n 
A 1 228 ASP 228 241 241 ASP ASP A . n 
A 1 229 THR 229 242 242 THR THR A . n 
A 1 230 VAL 230 243 243 VAL VAL A . n 
A 1 231 THR 231 244 244 THR THR A . n 
A 1 232 PHE 232 245 245 PHE PHE A . n 
A 1 233 THR 233 246 246 THR THR A . n 
A 1 234 PHE 234 247 247 PHE PHE A . n 
A 1 235 ASN 235 248 248 ASN ASN A . n 
A 1 236 GLY 236 249 249 GLY GLY A . n 
A 1 237 ALA 237 250 250 ALA ALA A . n 
A 1 238 PHE 238 251 251 PHE PHE A . n 
A 1 239 ILE 239 252 252 ILE ILE A . n 
A 1 240 ALA 240 253 253 ALA ALA A . n 
A 1 241 PRO 241 254 254 PRO PRO A . n 
A 1 242 ASP 242 255 255 ASP ASP A . n 
A 1 243 ARG 243 256 256 ARG ARG A . n 
A 1 244 THR 244 257 257 THR THR A . n 
A 1 245 SER 245 258 258 SER SER A . n 
A 1 246 PHE 246 259 259 PHE PHE A . n 
A 1 247 PHE 247 260 260 PHE PHE A . n 
A 1 248 ARG 248 261 261 ARG ARG A . n 
A 1 249 GLY 249 263 263 GLY GLY A . n 
A 1 250 GLU 250 264 264 GLU GLU A . n 
A 1 251 SER 251 265 265 SER SER A . n 
A 1 252 LEU 252 266 266 LEU LEU A . n 
A 1 253 GLY 253 267 267 GLY GLY A . n 
A 1 254 VAL 254 268 268 VAL VAL A . n 
A 1 255 GLN 255 269 269 GLN GLN A . n 
A 1 256 SER 256 270 270 SER SER A . n 
A 1 257 ASP 257 271 271 ASP ASP A . n 
A 1 258 ALA 258 272 272 ALA ALA A . n 
A 1 259 PRO 259 273 273 PRO PRO A . n 
A 1 260 LEU 260 274 274 LEU LEU A . n 
A 1 261 ASP 261 275 275 ASP ASP A . n 
A 1 262 SER 262 276 276 SER SER A . n 
A 1 263 SER 263 276 276 SER SER A A n 
A 1 264 CYS 264 277 277 CYS CYS A . n 
A 1 265 ARG 265 278 278 ARG ARG A . n 
A 1 266 GLY 266 279 279 GLY GLY A . n 
A 1 267 ASP 267 280 280 ASP ASP A . n 
A 1 268 CYS 268 281 281 CYS CYS A . n 
A 1 269 PHE 269 282 282 PHE PHE A . n 
A 1 270 HIS 270 283 283 HIS HIS A . n 
A 1 271 SER 271 284 284 SER SER A . n 
A 1 272 GLY 272 285 285 GLY GLY A . n 
A 1 273 GLY 273 286 286 GLY GLY A . n 
A 1 274 THR 274 287 287 THR THR A . n 
A 1 275 ILE 275 288 288 ILE ILE A . n 
A 1 276 VAL 276 289 289 VAL VAL A . n 
A 1 277 SER 277 290 290 SER SER A . n 
A 1 278 SER 278 291 291 SER SER A . n 
A 1 279 LEU 279 292 292 LEU LEU A . n 
A 1 280 PRO 280 293 293 PRO PRO A . n 
A 1 281 PHE 281 294 294 PHE PHE A . n 
A 1 282 GLN 282 295 295 GLN GLN A . n 
A 1 283 ASN 283 296 296 ASN ASN A . n 
A 1 284 ILE 284 297 297 ILE ILE A . n 
A 1 285 ASN 285 298 298 ASN ASN A . n 
A 1 286 SER 286 299 299 SER SER A . n 
A 1 287 ARG 287 300 300 ARG ARG A . n 
A 1 288 THR 288 301 301 THR THR A . n 
A 1 289 VAL 289 302 302 VAL VAL A . n 
A 1 290 GLY 290 303 303 GLY GLY A . n 
A 1 291 LYS 291 304 304 LYS LYS A . n 
A 1 292 CYS 292 305 305 CYS CYS A . n 
A 1 293 PRO 293 306 306 PRO PRO A . n 
A 1 294 ARG 294 307 307 ARG ARG A . n 
A 1 295 TYR 295 308 308 TYR TYR A . n 
A 1 296 VAL 296 309 309 VAL VAL A . n 
A 1 297 LYS 297 310 310 LYS LYS A . n 
A 1 298 GLN 298 311 311 GLN GLN A . n 
A 1 299 LYS 299 312 312 LYS LYS A . n 
A 1 300 SER 300 313 313 SER SER A . n 
A 1 301 LEU 301 314 314 LEU LEU A . n 
A 1 302 LEU 302 315 315 LEU LEU A . n 
A 1 303 LEU 303 316 316 LEU LEU A . n 
A 1 304 ALA 304 317 317 ALA ALA A . n 
A 1 305 THR 305 318 318 THR THR A . n 
A 1 306 GLY 306 319 319 GLY GLY A . n 
A 1 307 MET 307 320 320 MET MET A . n 
A 1 308 ARG 308 321 321 ARG ARG A . n 
A 1 309 ASN 309 322 322 ASN ASN A . n 
A 1 310 VAL 310 323 323 VAL VAL A . n 
A 1 311 PRO 311 324 324 PRO PRO A . n 
A 1 312 GLU 312 325 325 GLU GLU A . n 
A 1 313 LYS 313 326 326 LYS LYS A . n 
A 1 314 PRO 314 327 ?   ?   ?   A . n 
A 1 315 LYS 315 328 ?   ?   ?   A . n 
A 1 316 PRO 316 329 ?   ?   ?   A . n 
A 1 317 ARG 317 330 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  ASN 12  12  12  ASN ASN B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  GLU 15  15  15  GLU GLU B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  LEU 17  17  17  LEU LEU B . n 
B 2 18  ILE 18  18  18  ILE ILE B . n 
B 2 19  ASN 19  19  19  ASN ASN B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  PHE 24  24  24  PHE PHE B . n 
B 2 25  ARG 25  25  25  ARG ARG B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  GLN 27  27  27  GLN GLN B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  ALA 29  29  29  ALA ALA B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  GLU 32  32  32  GLU GLU B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  THR 34  34  34  THR THR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  TYR 38  38  38  TYR TYR B . n 
B 2 39  LYS 39  39  39  LYS LYS B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  SER 43  43  43  SER SER B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLN 47  47  47  GLN GLN B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  GLY 50  50  50  GLY GLY B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  LEU 52  52  52  LEU LEU B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  ARG 54  54  54  ARG ARG B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  THR 59  59  59  THR THR B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  GLN 61  61  61  GLN GLN B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  GLU 64  64  64  GLU GLU B . n 
B 2 65  LEU 65  65  65  LEU LEU B . n 
B 2 66  ILE 66  66  66  ILE ILE B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  ASN 68  68  68  ASN ASN B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  GLU 72  72  72  GLU GLU B . n 
B 2 73  ILE 73  73  73  ILE ILE B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  GLN 75  75  75  GLN GLN B . n 
B 2 76  GLN 76  76  76  GLN GLN B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  GLY 78  78  78  GLY GLY B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  VAL 80  80  80  VAL VAL B . n 
B 2 81  ILE 81  81  81  ILE ILE B . n 
B 2 82  ASN 82  82  82  ASN ASN B . n 
B 2 83  TRP 83  83  83  TRP TRP B . n 
B 2 84  THR 84  84  84  THR THR B . n 
B 2 85  ARG 85  85  85  ARG ARG B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  MET 88  88  88  MET MET B . n 
B 2 89  THR 89  89  89  THR THR B . n 
B 2 90  GLU 90  90  90  GLU GLU B . n 
B 2 91  ILE 91  91  91  ILE ILE B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  SER 93  93  93  SER SER B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 ALA 101 101 101 ALA ALA B . n 
B 2 102 MET 102 102 102 MET MET B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLN 105 105 105 GLN GLN B . n 
B 2 106 HIS 106 106 106 HIS HIS B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 ILE 108 108 108 ILE ILE B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 LEU 110 110 110 LEU LEU B . n 
B 2 111 ALA 111 111 111 ALA ALA B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 GLU 114 114 114 GLU GLU B . n 
B 2 115 MET 115 115 115 MET MET B . n 
B 2 116 SER 116 116 116 SER SER B . n 
B 2 117 LYS 117 117 117 LYS LYS B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 GLU 120 120 120 GLU GLU B . n 
B 2 121 ARG 121 121 121 ARG ARG B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 LYS 123 123 123 LYS LYS B . n 
B 2 124 LYS 124 124 124 LYS LYS B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 ARG 127 127 127 ARG ARG B . n 
B 2 128 GLU 128 128 128 GLU GLU B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 GLU 131 131 131 GLU GLU B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 ASP 133 133 133 ASP ASP B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 THR 135 135 135 THR THR B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 PHE 141 141 141 PHE PHE B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ASP 146 146 146 ASP ASP B . n 
B 2 147 GLN 147 147 147 GLN GLN B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 ILE 152 152 152 ILE ILE B . n 
B 2 153 ARG 153 153 153 ARG ARG B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 ASN 155 155 155 ASN ASN B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 HIS 159 159 159 HIS HIS B . n 
B 2 160 THR 160 160 160 THR THR B . n 
B 2 161 GLN 161 161 161 GLN GLN B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 ARG 163 163 163 ARG ARG B . n 
B 2 164 THR 164 164 164 THR THR B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 SER 166 166 166 SER SER B . n 
B 2 167 LEU 167 167 167 LEU LEU B . n 
B 2 168 GLN 168 168 168 GLN GLN B . n 
B 2 169 ASN 169 169 169 ASN ASN B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 ILE 171 171 171 ILE ILE B . n 
B 2 172 GLN 172 172 172 GLN GLN B . n 
B 2 173 ILE 173 173 173 ILE ILE B . n 
B 2 174 ASP 174 174 174 ASP ASP B . n 
B 2 175 SER 175 175 175 SER SER B . n 
B 2 176 GLY 176 176 176 GLY GLY B . n 
B 2 177 ARG 177 177 ?   ?   ?   B . n 
B 2 178 LEU 178 178 ?   ?   ?   B . n 
B 2 179 VAL 179 179 ?   ?   ?   B . n 
B 2 180 PRO 180 180 ?   ?   ?   B . n 
B 2 181 ARG 181 181 ?   ?   ?   B . n 
B 2 182 GLY 182 182 ?   ?   ?   B . n 
C 1 1   ALA 1   7   ?   ?   ?   C . n 
C 1 2   ASP 2   8   ?   ?   ?   C . n 
C 1 3   PRO 3   9   ?   ?   ?   C . n 
C 1 4   GLY 4   10  ?   ?   ?   C . n 
C 1 5   ASP 5   11  11  ASP ASP C . n 
C 1 6   LYS 6   12  12  LYS LYS C . n 
C 1 7   ILE 7   13  13  ILE ILE C . n 
C 1 8   CYS 8   14  14  CYS CYS C . n 
C 1 9   LEU 9   15  15  LEU LEU C . n 
C 1 10  GLY 10  16  16  GLY GLY C . n 
C 1 11  HIS 11  17  17  HIS HIS C . n 
C 1 12  HIS 12  18  18  HIS HIS C . n 
C 1 13  ALA 13  19  19  ALA ALA C . n 
C 1 14  VAL 14  20  20  VAL VAL C . n 
C 1 15  ALA 15  21  21  ALA ALA C . n 
C 1 16  ASN 16  22  22  ASN ASN C . n 
C 1 17  GLY 17  23  23  GLY GLY C . n 
C 1 18  THR 18  24  24  THR THR C . n 
C 1 19  LYS 19  25  25  LYS LYS C . n 
C 1 20  VAL 20  26  26  VAL VAL C . n 
C 1 21  ASN 21  27  27  ASN ASN C . n 
C 1 22  THR 22  28  28  THR THR C . n 
C 1 23  LEU 23  29  29  LEU LEU C . n 
C 1 24  THR 24  30  30  THR THR C . n 
C 1 25  GLU 25  31  31  GLU GLU C . n 
C 1 26  ARG 26  32  32  ARG ARG C . n 
C 1 27  GLY 27  33  33  GLY GLY C . n 
C 1 28  ILE 28  34  34  ILE ILE C . n 
C 1 29  GLU 29  35  35  GLU GLU C . n 
C 1 30  VAL 30  36  36  VAL VAL C . n 
C 1 31  VAL 31  37  37  VAL VAL C . n 
C 1 32  ASN 32  38  38  ASN ASN C . n 
C 1 33  ALA 33  39  39  ALA ALA C . n 
C 1 34  THR 34  40  40  THR THR C . n 
C 1 35  GLU 35  41  41  GLU GLU C . n 
C 1 36  THR 36  42  42  THR THR C . n 
C 1 37  VAL 37  43  43  VAL VAL C . n 
C 1 38  GLU 38  44  44  GLU GLU C . n 
C 1 39  THR 39  45  45  THR THR C . n 
C 1 40  THR 40  46  46  THR THR C . n 
C 1 41  ASN 41  47  47  ASN ASN C . n 
C 1 42  ILE 42  48  48  ILE ILE C . n 
C 1 43  LYS 43  49  49  LYS LYS C . n 
C 1 44  LYS 44  50  50  LYS LYS C . n 
C 1 45  ILE 45  51  51  ILE ILE C . n 
C 1 46  CYS 46  52  52  CYS CYS C . n 
C 1 47  THR 47  53  53  THR THR C . n 
C 1 48  GLN 48  54  54  GLN GLN C . n 
C 1 49  GLY 49  55  55  GLY GLY C . n 
C 1 50  LYS 50  56  56  LYS LYS C . n 
C 1 51  ARG 51  57  57  ARG ARG C . n 
C 1 52  PRO 52  58  58  PRO PRO C . n 
C 1 53  THR 53  59  59  THR THR C . n 
C 1 54  ASP 54  60  60  ASP ASP C . n 
C 1 55  LEU 55  61  61  LEU LEU C . n 
C 1 56  GLY 56  62  62  GLY GLY C . n 
C 1 57  GLN 57  63  63  GLN GLN C . n 
C 1 58  CYS 58  64  64  CYS CYS C . n 
C 1 59  GLY 59  65  65  GLY GLY C . n 
C 1 60  LEU 60  66  66  LEU LEU C . n 
C 1 61  LEU 61  67  67  LEU LEU C . n 
C 1 62  GLY 62  68  68  GLY GLY C . n 
C 1 63  THR 63  69  69  THR THR C . n 
C 1 64  LEU 64  70  70  LEU LEU C . n 
C 1 65  ILE 65  71  71  ILE ILE C . n 
C 1 66  GLY 66  72  72  GLY GLY C . n 
C 1 67  PRO 67  73  73  PRO PRO C . n 
C 1 68  PRO 68  74  74  PRO PRO C . n 
C 1 69  GLN 69  75  75  GLN GLN C . n 
C 1 70  CYS 70  76  76  CYS CYS C . n 
C 1 71  ASP 71  77  77  ASP ASP C . n 
C 1 72  GLN 72  78  78  GLN GLN C . n 
C 1 73  PHE 73  79  79  PHE PHE C . n 
C 1 74  LEU 74  80  80  LEU LEU C . n 
C 1 75  GLU 75  81  81  GLU GLU C . n 
C 1 76  PHE 76  82  82  PHE PHE C . n 
C 1 77  SER 77  83  83  SER SER C . n 
C 1 78  SER 78  84  84  SER SER C . n 
C 1 79  ASP 79  85  85  ASP ASP C . n 
C 1 80  LEU 80  86  86  LEU LEU C . n 
C 1 81  ILE 81  87  87  ILE ILE C . n 
C 1 82  ILE 82  88  88  ILE ILE C . n 
C 1 83  GLU 83  89  89  GLU GLU C . n 
C 1 84  ARG 84  90  90  ARG ARG C . n 
C 1 85  ARG 85  91  91  ARG ARG C . n 
C 1 86  GLU 86  92  92  GLU GLU C . n 
C 1 87  GLY 87  93  93  GLY GLY C . n 
C 1 88  THR 88  94  94  THR THR C . n 
C 1 89  ASP 89  95  95  ASP ASP C . n 
C 1 90  ILE 90  96  96  ILE ILE C . n 
C 1 91  CYS 91  97  97  CYS CYS C . n 
C 1 92  TYR 92  98  98  TYR TYR C . n 
C 1 93  PRO 93  99  99  PRO PRO C . n 
C 1 94  GLY 94  100 100 GLY GLY C . n 
C 1 95  ARG 95  101 101 ARG ARG C . n 
C 1 96  PHE 96  102 102 PHE PHE C . n 
C 1 97  THR 97  103 103 THR THR C . n 
C 1 98  ASN 98  104 104 ASN ASN C . n 
C 1 99  GLU 99  105 105 GLU GLU C . n 
C 1 100 GLU 100 106 106 GLU GLU C . n 
C 1 101 SER 101 107 107 SER SER C . n 
C 1 102 LEU 102 108 108 LEU LEU C . n 
C 1 103 ARG 103 109 109 ARG ARG C . n 
C 1 104 GLN 104 110 110 GLN GLN C . n 
C 1 105 ILE 105 111 111 ILE ILE C . n 
C 1 106 LEU 106 112 112 LEU LEU C . n 
C 1 107 ARG 107 113 113 ARG ARG C . n 
C 1 108 ARG 108 114 114 ARG ARG C . n 
C 1 109 SER 109 115 115 SER SER C . n 
C 1 110 GLY 110 116 116 GLY GLY C . n 
C 1 111 GLY 111 117 117 GLY GLY C . n 
C 1 112 ILE 112 118 118 ILE ILE C . n 
C 1 113 GLY 113 119 119 GLY GLY C . n 
C 1 114 LYS 114 120 120 LYS LYS C . n 
C 1 115 GLU 115 121 121 GLU GLU C . n 
C 1 116 SER 116 122 122 SER SER C . n 
C 1 117 MET 117 123 123 MET MET C . n 
C 1 118 GLY 118 124 124 GLY GLY C . n 
C 1 119 PHE 119 125 125 PHE PHE C . n 
C 1 120 THR 120 126 126 THR THR C . n 
C 1 121 TYR 121 127 127 TYR TYR C . n 
C 1 122 SER 122 128 128 SER SER C . n 
C 1 123 GLY 123 129 129 GLY GLY C . n 
C 1 124 ILE 124 130 130 ILE ILE C . n 
C 1 125 ARG 125 131 131 ARG ARG C . n 
C 1 126 THR 126 132 132 THR THR C . n 
C 1 127 ASN 127 133 133 ASN ASN C . n 
C 1 128 GLY 128 134 134 GLY GLY C . n 
C 1 129 ALA 129 135 135 ALA ALA C . n 
C 1 130 THR 130 136 136 THR THR C . n 
C 1 131 SER 131 137 137 SER SER C . n 
C 1 132 ALA 132 138 138 ALA ALA C . n 
C 1 133 CYS 133 139 139 CYS CYS C . n 
C 1 134 THR 134 140 140 THR THR C . n 
C 1 135 ARG 135 141 141 ARG ARG C . n 
C 1 136 SER 136 142 142 SER SER C . n 
C 1 137 GLY 137 144 144 GLY GLY C . n 
C 1 138 SER 138 145 145 SER SER C . n 
C 1 139 SER 139 146 146 SER SER C . n 
C 1 140 PHE 140 147 147 PHE PHE C . n 
C 1 141 TYR 141 148 148 TYR TYR C . n 
C 1 142 ALA 142 149 149 ALA ALA C . n 
C 1 143 GLU 143 150 150 GLU GLU C . n 
C 1 144 MET 144 151 151 MET MET C . n 
C 1 145 LYS 145 152 152 LYS LYS C . n 
C 1 146 TRP 146 153 153 TRP TRP C . n 
C 1 147 LEU 147 154 154 LEU LEU C . n 
C 1 148 LEU 148 155 155 LEU LEU C . n 
C 1 149 SER 149 156 156 SER SER C . n 
C 1 150 ASN 150 157 157 ASN ASN C . n 
C 1 151 SER 151 158 158 SER SER C . n 
C 1 152 ASP 152 158 158 ASP ASP C A n 
C 1 153 ASN 153 158 158 ASN ASN C B n 
C 1 154 ALA 154 159 159 ALA ALA C . n 
C 1 155 ALA 155 160 160 ALA ALA C . n 
C 1 156 PHE 156 161 161 PHE PHE C . n 
C 1 157 PRO 157 162 162 PRO PRO C . n 
C 1 158 GLN 158 163 163 GLN GLN C . n 
C 1 159 MET 159 164 164 MET MET C . n 
C 1 160 THR 160 165 165 THR THR C . n 
C 1 161 LYS 161 166 166 LYS LYS C . n 
C 1 162 ALA 162 167 167 ALA ALA C . n 
C 1 163 TYR 163 168 168 TYR TYR C . n 
C 1 164 ARG 164 169 169 ARG ARG C . n 
C 1 165 ASN 165 170 170 ASN ASN C . n 
C 1 166 PRO 166 171 171 PRO PRO C . n 
C 1 167 ARG 167 172 172 ARG ARG C . n 
C 1 168 ASN 168 173 173 ASN ASN C . n 
C 1 169 LYS 169 174 174 LYS LYS C . n 
C 1 170 PRO 170 175 175 PRO PRO C . n 
C 1 171 ALA 171 176 176 ALA ALA C . n 
C 1 172 LEU 172 177 177 LEU LEU C . n 
C 1 173 ILE 173 178 178 ILE ILE C . n 
C 1 174 ILE 174 179 179 ILE ILE C . n 
C 1 175 TRP 175 180 180 TRP TRP C . n 
C 1 176 GLY 176 181 181 GLY GLY C . n 
C 1 177 VAL 177 182 182 VAL VAL C . n 
C 1 178 HIS 178 183 183 HIS HIS C . n 
C 1 179 HIS 179 184 184 HIS HIS C . n 
C 1 180 SER 180 185 185 SER SER C . n 
C 1 181 GLU 181 186 186 GLU GLU C . n 
C 1 182 SER 182 187 187 SER SER C . n 
C 1 183 VAL 183 188 188 VAL VAL C . n 
C 1 184 SER 184 189 189 SER SER C . n 
C 1 185 GLU 185 190 190 GLU GLU C . n 
C 1 186 GLN 186 191 191 GLN GLN C . n 
C 1 187 THR 187 192 192 THR THR C . n 
C 1 188 LYS 188 193 193 LYS LYS C . n 
C 1 189 LEU 189 194 194 LEU LEU C . n 
C 1 190 TYR 190 195 195 TYR TYR C . n 
C 1 191 GLY 191 196 196 GLY GLY C . n 
C 1 192 SER 192 197 197 SER SER C . n 
C 1 193 GLY 193 198 198 GLY GLY C . n 
C 1 194 ASN 194 199 199 ASN ASN C . n 
C 1 195 LYS 195 200 200 LYS LYS C . n 
C 1 196 LEU 196 201 201 LEU LEU C . n 
C 1 197 ILE 197 202 202 ILE ILE C . n 
C 1 198 THR 198 203 203 THR THR C . n 
C 1 199 VAL 199 204 204 VAL VAL C . n 
C 1 200 ARG 200 205 205 ARG ARG C . n 
C 1 201 SER 201 206 206 SER SER C . n 
C 1 202 SER 202 207 207 SER SER C . n 
C 1 203 LYS 203 208 208 LYS LYS C . n 
C 1 204 TYR 204 209 209 TYR TYR C . n 
C 1 205 GLN 205 210 210 GLN GLN C . n 
C 1 206 GLN 206 211 211 GLN GLN C . n 
C 1 207 SER 207 212 212 SER SER C . n 
C 1 208 PHE 208 213 213 PHE PHE C . n 
C 1 209 THR 209 214 214 THR THR C . n 
C 1 210 PRO 210 215 215 PRO PRO C . n 
C 1 211 ASN 211 216 216 ASN ASN C . n 
C 1 212 PRO 212 217 217 PRO PRO C . n 
C 1 213 GLY 213 218 218 GLY GLY C . n 
C 1 214 ALA 214 219 219 ALA ALA C . n 
C 1 215 ARG 215 220 220 ARG ARG C . n 
C 1 216 ARG 216 229 229 ARG ARG C . n 
C 1 217 ILE 217 230 230 ILE ILE C . n 
C 1 218 ASP 218 231 231 ASP ASP C . n 
C 1 219 PHE 219 232 232 PHE PHE C . n 
C 1 220 HIS 220 233 233 HIS HIS C . n 
C 1 221 TRP 221 234 234 TRP TRP C . n 
C 1 222 LEU 222 235 235 LEU LEU C . n 
C 1 223 LEU 223 236 236 LEU LEU C . n 
C 1 224 LEU 224 237 237 LEU LEU C . n 
C 1 225 ASP 225 238 238 ASP ASP C . n 
C 1 226 PRO 226 239 239 PRO PRO C . n 
C 1 227 ASN 227 240 240 ASN ASN C . n 
C 1 228 ASP 228 241 241 ASP ASP C . n 
C 1 229 THR 229 242 242 THR THR C . n 
C 1 230 VAL 230 243 243 VAL VAL C . n 
C 1 231 THR 231 244 244 THR THR C . n 
C 1 232 PHE 232 245 245 PHE PHE C . n 
C 1 233 THR 233 246 246 THR THR C . n 
C 1 234 PHE 234 247 247 PHE PHE C . n 
C 1 235 ASN 235 248 248 ASN ASN C . n 
C 1 236 GLY 236 249 249 GLY GLY C . n 
C 1 237 ALA 237 250 250 ALA ALA C . n 
C 1 238 PHE 238 251 251 PHE PHE C . n 
C 1 239 ILE 239 252 252 ILE ILE C . n 
C 1 240 ALA 240 253 253 ALA ALA C . n 
C 1 241 PRO 241 254 254 PRO PRO C . n 
C 1 242 ASP 242 255 255 ASP ASP C . n 
C 1 243 ARG 243 256 256 ARG ARG C . n 
C 1 244 THR 244 257 257 THR THR C . n 
C 1 245 SER 245 258 258 SER SER C . n 
C 1 246 PHE 246 259 259 PHE PHE C . n 
C 1 247 PHE 247 260 260 PHE PHE C . n 
C 1 248 ARG 248 261 261 ARG ARG C . n 
C 1 249 GLY 249 263 263 GLY GLY C . n 
C 1 250 GLU 250 264 264 GLU GLU C . n 
C 1 251 SER 251 265 265 SER SER C . n 
C 1 252 LEU 252 266 266 LEU LEU C . n 
C 1 253 GLY 253 267 267 GLY GLY C . n 
C 1 254 VAL 254 268 268 VAL VAL C . n 
C 1 255 GLN 255 269 269 GLN GLN C . n 
C 1 256 SER 256 270 270 SER SER C . n 
C 1 257 ASP 257 271 271 ASP ASP C . n 
C 1 258 ALA 258 272 272 ALA ALA C . n 
C 1 259 PRO 259 273 273 PRO PRO C . n 
C 1 260 LEU 260 274 274 LEU LEU C . n 
C 1 261 ASP 261 275 275 ASP ASP C . n 
C 1 262 SER 262 276 276 SER SER C . n 
C 1 263 SER 263 276 276 SER SER C A n 
C 1 264 CYS 264 277 277 CYS CYS C . n 
C 1 265 ARG 265 278 278 ARG ARG C . n 
C 1 266 GLY 266 279 279 GLY GLY C . n 
C 1 267 ASP 267 280 280 ASP ASP C . n 
C 1 268 CYS 268 281 281 CYS CYS C . n 
C 1 269 PHE 269 282 282 PHE PHE C . n 
C 1 270 HIS 270 283 283 HIS HIS C . n 
C 1 271 SER 271 284 284 SER SER C . n 
C 1 272 GLY 272 285 285 GLY GLY C . n 
C 1 273 GLY 273 286 286 GLY GLY C . n 
C 1 274 THR 274 287 287 THR THR C . n 
C 1 275 ILE 275 288 288 ILE ILE C . n 
C 1 276 VAL 276 289 289 VAL VAL C . n 
C 1 277 SER 277 290 290 SER SER C . n 
C 1 278 SER 278 291 291 SER SER C . n 
C 1 279 LEU 279 292 292 LEU LEU C . n 
C 1 280 PRO 280 293 293 PRO PRO C . n 
C 1 281 PHE 281 294 294 PHE PHE C . n 
C 1 282 GLN 282 295 295 GLN GLN C . n 
C 1 283 ASN 283 296 296 ASN ASN C . n 
C 1 284 ILE 284 297 297 ILE ILE C . n 
C 1 285 ASN 285 298 298 ASN ASN C . n 
C 1 286 SER 286 299 299 SER SER C . n 
C 1 287 ARG 287 300 300 ARG ARG C . n 
C 1 288 THR 288 301 301 THR THR C . n 
C 1 289 VAL 289 302 302 VAL VAL C . n 
C 1 290 GLY 290 303 303 GLY GLY C . n 
C 1 291 LYS 291 304 304 LYS LYS C . n 
C 1 292 CYS 292 305 305 CYS CYS C . n 
C 1 293 PRO 293 306 306 PRO PRO C . n 
C 1 294 ARG 294 307 307 ARG ARG C . n 
C 1 295 TYR 295 308 308 TYR TYR C . n 
C 1 296 VAL 296 309 309 VAL VAL C . n 
C 1 297 LYS 297 310 310 LYS LYS C . n 
C 1 298 GLN 298 311 311 GLN GLN C . n 
C 1 299 LYS 299 312 312 LYS LYS C . n 
C 1 300 SER 300 313 313 SER SER C . n 
C 1 301 LEU 301 314 314 LEU LEU C . n 
C 1 302 LEU 302 315 315 LEU LEU C . n 
C 1 303 LEU 303 316 316 LEU LEU C . n 
C 1 304 ALA 304 317 317 ALA ALA C . n 
C 1 305 THR 305 318 318 THR THR C . n 
C 1 306 GLY 306 319 319 GLY GLY C . n 
C 1 307 MET 307 320 320 MET MET C . n 
C 1 308 ARG 308 321 321 ARG ARG C . n 
C 1 309 ASN 309 322 322 ASN ASN C . n 
C 1 310 VAL 310 323 323 VAL VAL C . n 
C 1 311 PRO 311 324 324 PRO PRO C . n 
C 1 312 GLU 312 325 325 GLU GLU C . n 
C 1 313 LYS 313 326 326 LYS LYS C . n 
C 1 314 PRO 314 327 ?   ?   ?   C . n 
C 1 315 LYS 315 328 ?   ?   ?   C . n 
C 1 316 PRO 316 329 ?   ?   ?   C . n 
C 1 317 ARG 317 330 ?   ?   ?   C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  ASN 12  12  12  ASN ASN D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  GLU 15  15  15  GLU GLU D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  LEU 17  17  17  LEU LEU D . n 
D 2 18  ILE 18  18  18  ILE ILE D . n 
D 2 19  ASN 19  19  19  ASN ASN D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  PHE 24  24  24  PHE PHE D . n 
D 2 25  ARG 25  25  25  ARG ARG D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  GLN 27  27  27  GLN GLN D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  ALA 29  29  29  ALA ALA D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  GLU 32  32  32  GLU GLU D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  THR 34  34  34  THR THR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  TYR 38  38  38  TYR TYR D . n 
D 2 39  LYS 39  39  39  LYS LYS D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  THR 41  41  41  THR THR D . n 
D 2 42  GLN 42  42  42  GLN GLN D . n 
D 2 43  SER 43  43  43  SER SER D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLN 47  47  47  GLN GLN D . n 
D 2 48  ILE 48  48  48  ILE ILE D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  GLY 50  50  50  GLY GLY D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  LEU 52  52  52  LEU LEU D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  ARG 54  54  54  ARG ARG D . n 
D 2 55  LEU 55  55  55  LEU LEU D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  GLY 57  57  57  GLY GLY D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  THR 59  59  59  THR THR D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  GLN 61  61  61  GLN GLN D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  GLU 64  64  64  GLU GLU D . n 
D 2 65  LEU 65  65  65  LEU LEU D . n 
D 2 66  ILE 66  66  66  ILE ILE D . n 
D 2 67  ASP 67  67  67  ASP ASP D . n 
D 2 68  ASN 68  68  68  ASN ASN D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  ASN 71  71  71  ASN ASN D . n 
D 2 72  GLU 72  72  72  GLU GLU D . n 
D 2 73  ILE 73  73  73  ILE ILE D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  GLN 75  75  75  GLN GLN D . n 
D 2 76  GLN 76  76  76  GLN GLN D . n 
D 2 77  ILE 77  77  77  ILE ILE D . n 
D 2 78  GLY 78  78  78  GLY GLY D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  VAL 80  80  80  VAL VAL D . n 
D 2 81  ILE 81  81  81  ILE ILE D . n 
D 2 82  ASN 82  82  82  ASN ASN D . n 
D 2 83  TRP 83  83  83  TRP TRP D . n 
D 2 84  THR 84  84  84  THR THR D . n 
D 2 85  ARG 85  85  85  ARG ARG D . n 
D 2 86  ASP 86  86  86  ASP ASP D . n 
D 2 87  ALA 87  87  87  ALA ALA D . n 
D 2 88  MET 88  88  88  MET MET D . n 
D 2 89  THR 89  89  89  THR THR D . n 
D 2 90  GLU 90  90  90  GLU GLU D . n 
D 2 91  ILE 91  91  91  ILE ILE D . n 
D 2 92  TRP 92  92  92  TRP TRP D . n 
D 2 93  SER 93  93  93  SER SER D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  ASN 95  95  95  ASN ASN D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  GLU 97  97  97  GLU GLU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 ALA 101 101 101 ALA ALA D . n 
D 2 102 MET 102 102 102 MET MET D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 ASN 104 104 104 ASN ASN D . n 
D 2 105 GLN 105 105 105 GLN GLN D . n 
D 2 106 HIS 106 106 106 HIS HIS D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 ILE 108 108 108 ILE ILE D . n 
D 2 109 ASP 109 109 109 ASP ASP D . n 
D 2 110 LEU 110 110 110 LEU LEU D . n 
D 2 111 ALA 111 111 111 ALA ALA D . n 
D 2 112 ASP 112 112 112 ASP ASP D . n 
D 2 113 SER 113 113 113 SER SER D . n 
D 2 114 GLU 114 114 114 GLU GLU D . n 
D 2 115 MET 115 115 115 MET MET D . n 
D 2 116 SER 116 116 116 SER SER D . n 
D 2 117 LYS 117 117 117 LYS LYS D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 TYR 119 119 119 TYR TYR D . n 
D 2 120 GLU 120 120 120 GLU GLU D . n 
D 2 121 ARG 121 121 121 ARG ARG D . n 
D 2 122 VAL 122 122 122 VAL VAL D . n 
D 2 123 LYS 123 123 123 LYS LYS D . n 
D 2 124 LYS 124 124 124 LYS LYS D . n 
D 2 125 GLN 125 125 125 GLN GLN D . n 
D 2 126 LEU 126 126 126 LEU LEU D . n 
D 2 127 ARG 127 127 127 ARG ARG D . n 
D 2 128 GLU 128 128 128 GLU GLU D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 ALA 130 130 130 ALA ALA D . n 
D 2 131 GLU 131 131 131 GLU GLU D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 ASP 133 133 133 ASP ASP D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 THR 135 135 135 THR THR D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 ILE 140 140 140 ILE ILE D . n 
D 2 141 PHE 141 141 141 PHE PHE D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASP 146 146 146 ASP ASP D . n 
D 2 147 GLN 147 147 147 GLN GLN D . n 
D 2 148 CYS 148 148 148 CYS CYS D . n 
D 2 149 MET 149 149 149 MET MET D . n 
D 2 150 GLU 150 150 150 GLU GLU D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 ILE 152 152 152 ILE ILE D . n 
D 2 153 ARG 153 153 153 ARG ARG D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 ASN 155 155 155 ASN ASN D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 HIS 159 159 159 HIS HIS D . n 
D 2 160 THR 160 160 160 THR THR D . n 
D 2 161 GLN 161 161 161 GLN GLN D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 ARG 163 163 163 ARG ARG D . n 
D 2 164 THR 164 164 164 THR THR D . n 
D 2 165 GLU 165 165 165 GLU GLU D . n 
D 2 166 SER 166 166 166 SER SER D . n 
D 2 167 LEU 167 167 167 LEU LEU D . n 
D 2 168 GLN 168 168 168 GLN GLN D . n 
D 2 169 ASN 169 169 169 ASN ASN D . n 
D 2 170 ARG 170 170 170 ARG ARG D . n 
D 2 171 ILE 171 171 171 ILE ILE D . n 
D 2 172 GLN 172 172 172 GLN GLN D . n 
D 2 173 ILE 173 173 ?   ?   ?   D . n 
D 2 174 ASP 174 174 ?   ?   ?   D . n 
D 2 175 SER 175 175 ?   ?   ?   D . n 
D 2 176 GLY 176 176 ?   ?   ?   D . n 
D 2 177 ARG 177 177 ?   ?   ?   D . n 
D 2 178 LEU 178 178 ?   ?   ?   D . n 
D 2 179 VAL 179 179 ?   ?   ?   D . n 
D 2 180 PRO 180 180 ?   ?   ?   D . n 
D 2 181 ARG 181 181 ?   ?   ?   D . n 
D 2 182 GLY 182 182 ?   ?   ?   D . n 
E 1 1   ALA 1   7   ?   ?   ?   E . n 
E 1 2   ASP 2   8   ?   ?   ?   E . n 
E 1 3   PRO 3   9   ?   ?   ?   E . n 
E 1 4   GLY 4   10  10  GLY GLY E . n 
E 1 5   ASP 5   11  11  ASP ASP E . n 
E 1 6   LYS 6   12  12  LYS LYS E . n 
E 1 7   ILE 7   13  13  ILE ILE E . n 
E 1 8   CYS 8   14  14  CYS CYS E . n 
E 1 9   LEU 9   15  15  LEU LEU E . n 
E 1 10  GLY 10  16  16  GLY GLY E . n 
E 1 11  HIS 11  17  17  HIS HIS E . n 
E 1 12  HIS 12  18  18  HIS HIS E . n 
E 1 13  ALA 13  19  19  ALA ALA E . n 
E 1 14  VAL 14  20  20  VAL VAL E . n 
E 1 15  ALA 15  21  21  ALA ALA E . n 
E 1 16  ASN 16  22  22  ASN ASN E . n 
E 1 17  GLY 17  23  23  GLY GLY E . n 
E 1 18  THR 18  24  24  THR THR E . n 
E 1 19  LYS 19  25  25  LYS LYS E . n 
E 1 20  VAL 20  26  26  VAL VAL E . n 
E 1 21  ASN 21  27  27  ASN ASN E . n 
E 1 22  THR 22  28  28  THR THR E . n 
E 1 23  LEU 23  29  29  LEU LEU E . n 
E 1 24  THR 24  30  30  THR THR E . n 
E 1 25  GLU 25  31  31  GLU GLU E . n 
E 1 26  ARG 26  32  32  ARG ARG E . n 
E 1 27  GLY 27  33  33  GLY GLY E . n 
E 1 28  ILE 28  34  34  ILE ILE E . n 
E 1 29  GLU 29  35  35  GLU GLU E . n 
E 1 30  VAL 30  36  36  VAL VAL E . n 
E 1 31  VAL 31  37  37  VAL VAL E . n 
E 1 32  ASN 32  38  38  ASN ASN E . n 
E 1 33  ALA 33  39  39  ALA ALA E . n 
E 1 34  THR 34  40  40  THR THR E . n 
E 1 35  GLU 35  41  41  GLU GLU E . n 
E 1 36  THR 36  42  42  THR THR E . n 
E 1 37  VAL 37  43  43  VAL VAL E . n 
E 1 38  GLU 38  44  44  GLU GLU E . n 
E 1 39  THR 39  45  45  THR THR E . n 
E 1 40  THR 40  46  46  THR THR E . n 
E 1 41  ASN 41  47  47  ASN ASN E . n 
E 1 42  ILE 42  48  48  ILE ILE E . n 
E 1 43  LYS 43  49  49  LYS LYS E . n 
E 1 44  LYS 44  50  50  LYS LYS E . n 
E 1 45  ILE 45  51  51  ILE ILE E . n 
E 1 46  CYS 46  52  52  CYS CYS E . n 
E 1 47  THR 47  53  53  THR THR E . n 
E 1 48  GLN 48  54  54  GLN GLN E . n 
E 1 49  GLY 49  55  55  GLY GLY E . n 
E 1 50  LYS 50  56  56  LYS LYS E . n 
E 1 51  ARG 51  57  57  ARG ARG E . n 
E 1 52  PRO 52  58  58  PRO PRO E . n 
E 1 53  THR 53  59  59  THR THR E . n 
E 1 54  ASP 54  60  60  ASP ASP E . n 
E 1 55  LEU 55  61  61  LEU LEU E . n 
E 1 56  GLY 56  62  62  GLY GLY E . n 
E 1 57  GLN 57  63  63  GLN GLN E . n 
E 1 58  CYS 58  64  64  CYS CYS E . n 
E 1 59  GLY 59  65  65  GLY GLY E . n 
E 1 60  LEU 60  66  66  LEU LEU E . n 
E 1 61  LEU 61  67  67  LEU LEU E . n 
E 1 62  GLY 62  68  68  GLY GLY E . n 
E 1 63  THR 63  69  69  THR THR E . n 
E 1 64  LEU 64  70  70  LEU LEU E . n 
E 1 65  ILE 65  71  71  ILE ILE E . n 
E 1 66  GLY 66  72  72  GLY GLY E . n 
E 1 67  PRO 67  73  73  PRO PRO E . n 
E 1 68  PRO 68  74  74  PRO PRO E . n 
E 1 69  GLN 69  75  75  GLN GLN E . n 
E 1 70  CYS 70  76  76  CYS CYS E . n 
E 1 71  ASP 71  77  77  ASP ASP E . n 
E 1 72  GLN 72  78  78  GLN GLN E . n 
E 1 73  PHE 73  79  79  PHE PHE E . n 
E 1 74  LEU 74  80  80  LEU LEU E . n 
E 1 75  GLU 75  81  81  GLU GLU E . n 
E 1 76  PHE 76  82  82  PHE PHE E . n 
E 1 77  SER 77  83  83  SER SER E . n 
E 1 78  SER 78  84  84  SER SER E . n 
E 1 79  ASP 79  85  85  ASP ASP E . n 
E 1 80  LEU 80  86  86  LEU LEU E . n 
E 1 81  ILE 81  87  87  ILE ILE E . n 
E 1 82  ILE 82  88  88  ILE ILE E . n 
E 1 83  GLU 83  89  89  GLU GLU E . n 
E 1 84  ARG 84  90  90  ARG ARG E . n 
E 1 85  ARG 85  91  91  ARG ARG E . n 
E 1 86  GLU 86  92  92  GLU GLU E . n 
E 1 87  GLY 87  93  93  GLY GLY E . n 
E 1 88  THR 88  94  94  THR THR E . n 
E 1 89  ASP 89  95  95  ASP ASP E . n 
E 1 90  ILE 90  96  96  ILE ILE E . n 
E 1 91  CYS 91  97  97  CYS CYS E . n 
E 1 92  TYR 92  98  98  TYR TYR E . n 
E 1 93  PRO 93  99  99  PRO PRO E . n 
E 1 94  GLY 94  100 100 GLY GLY E . n 
E 1 95  ARG 95  101 101 ARG ARG E . n 
E 1 96  PHE 96  102 102 PHE PHE E . n 
E 1 97  THR 97  103 103 THR THR E . n 
E 1 98  ASN 98  104 104 ASN ASN E . n 
E 1 99  GLU 99  105 105 GLU GLU E . n 
E 1 100 GLU 100 106 106 GLU GLU E . n 
E 1 101 SER 101 107 107 SER SER E . n 
E 1 102 LEU 102 108 108 LEU LEU E . n 
E 1 103 ARG 103 109 109 ARG ARG E . n 
E 1 104 GLN 104 110 110 GLN GLN E . n 
E 1 105 ILE 105 111 111 ILE ILE E . n 
E 1 106 LEU 106 112 112 LEU LEU E . n 
E 1 107 ARG 107 113 113 ARG ARG E . n 
E 1 108 ARG 108 114 114 ARG ARG E . n 
E 1 109 SER 109 115 115 SER SER E . n 
E 1 110 GLY 110 116 116 GLY GLY E . n 
E 1 111 GLY 111 117 117 GLY GLY E . n 
E 1 112 ILE 112 118 118 ILE ILE E . n 
E 1 113 GLY 113 119 119 GLY GLY E . n 
E 1 114 LYS 114 120 120 LYS LYS E . n 
E 1 115 GLU 115 121 121 GLU GLU E . n 
E 1 116 SER 116 122 122 SER SER E . n 
E 1 117 MET 117 123 123 MET MET E . n 
E 1 118 GLY 118 124 124 GLY GLY E . n 
E 1 119 PHE 119 125 125 PHE PHE E . n 
E 1 120 THR 120 126 126 THR THR E . n 
E 1 121 TYR 121 127 127 TYR TYR E . n 
E 1 122 SER 122 128 128 SER SER E . n 
E 1 123 GLY 123 129 129 GLY GLY E . n 
E 1 124 ILE 124 130 130 ILE ILE E . n 
E 1 125 ARG 125 131 131 ARG ARG E . n 
E 1 126 THR 126 132 132 THR THR E . n 
E 1 127 ASN 127 133 133 ASN ASN E . n 
E 1 128 GLY 128 134 134 GLY GLY E . n 
E 1 129 ALA 129 135 135 ALA ALA E . n 
E 1 130 THR 130 136 136 THR THR E . n 
E 1 131 SER 131 137 137 SER SER E . n 
E 1 132 ALA 132 138 138 ALA ALA E . n 
E 1 133 CYS 133 139 139 CYS CYS E . n 
E 1 134 THR 134 140 140 THR THR E . n 
E 1 135 ARG 135 141 141 ARG ARG E . n 
E 1 136 SER 136 142 142 SER SER E . n 
E 1 137 GLY 137 144 144 GLY GLY E . n 
E 1 138 SER 138 145 145 SER SER E . n 
E 1 139 SER 139 146 146 SER SER E . n 
E 1 140 PHE 140 147 147 PHE PHE E . n 
E 1 141 TYR 141 148 148 TYR TYR E . n 
E 1 142 ALA 142 149 149 ALA ALA E . n 
E 1 143 GLU 143 150 150 GLU GLU E . n 
E 1 144 MET 144 151 151 MET MET E . n 
E 1 145 LYS 145 152 152 LYS LYS E . n 
E 1 146 TRP 146 153 153 TRP TRP E . n 
E 1 147 LEU 147 154 154 LEU LEU E . n 
E 1 148 LEU 148 155 155 LEU LEU E . n 
E 1 149 SER 149 156 156 SER SER E . n 
E 1 150 ASN 150 157 157 ASN ASN E . n 
E 1 151 SER 151 158 158 SER SER E . n 
E 1 152 ASP 152 158 158 ASP ASP E A n 
E 1 153 ASN 153 158 158 ASN ASN E B n 
E 1 154 ALA 154 159 159 ALA ALA E . n 
E 1 155 ALA 155 160 160 ALA ALA E . n 
E 1 156 PHE 156 161 161 PHE PHE E . n 
E 1 157 PRO 157 162 162 PRO PRO E . n 
E 1 158 GLN 158 163 163 GLN GLN E . n 
E 1 159 MET 159 164 164 MET MET E . n 
E 1 160 THR 160 165 165 THR THR E . n 
E 1 161 LYS 161 166 166 LYS LYS E . n 
E 1 162 ALA 162 167 167 ALA ALA E . n 
E 1 163 TYR 163 168 168 TYR TYR E . n 
E 1 164 ARG 164 169 169 ARG ARG E . n 
E 1 165 ASN 165 170 170 ASN ASN E . n 
E 1 166 PRO 166 171 171 PRO PRO E . n 
E 1 167 ARG 167 172 172 ARG ARG E . n 
E 1 168 ASN 168 173 173 ASN ASN E . n 
E 1 169 LYS 169 174 174 LYS LYS E . n 
E 1 170 PRO 170 175 175 PRO PRO E . n 
E 1 171 ALA 171 176 176 ALA ALA E . n 
E 1 172 LEU 172 177 177 LEU LEU E . n 
E 1 173 ILE 173 178 178 ILE ILE E . n 
E 1 174 ILE 174 179 179 ILE ILE E . n 
E 1 175 TRP 175 180 180 TRP TRP E . n 
E 1 176 GLY 176 181 181 GLY GLY E . n 
E 1 177 VAL 177 182 182 VAL VAL E . n 
E 1 178 HIS 178 183 183 HIS HIS E . n 
E 1 179 HIS 179 184 184 HIS HIS E . n 
E 1 180 SER 180 185 185 SER SER E . n 
E 1 181 GLU 181 186 186 GLU GLU E . n 
E 1 182 SER 182 187 187 SER SER E . n 
E 1 183 VAL 183 188 188 VAL VAL E . n 
E 1 184 SER 184 189 189 SER SER E . n 
E 1 185 GLU 185 190 190 GLU GLU E . n 
E 1 186 GLN 186 191 191 GLN GLN E . n 
E 1 187 THR 187 192 192 THR THR E . n 
E 1 188 LYS 188 193 193 LYS LYS E . n 
E 1 189 LEU 189 194 194 LEU LEU E . n 
E 1 190 TYR 190 195 195 TYR TYR E . n 
E 1 191 GLY 191 196 196 GLY GLY E . n 
E 1 192 SER 192 197 197 SER SER E . n 
E 1 193 GLY 193 198 198 GLY GLY E . n 
E 1 194 ASN 194 199 199 ASN ASN E . n 
E 1 195 LYS 195 200 200 LYS LYS E . n 
E 1 196 LEU 196 201 201 LEU LEU E . n 
E 1 197 ILE 197 202 202 ILE ILE E . n 
E 1 198 THR 198 203 203 THR THR E . n 
E 1 199 VAL 199 204 204 VAL VAL E . n 
E 1 200 ARG 200 205 205 ARG ARG E . n 
E 1 201 SER 201 206 206 SER SER E . n 
E 1 202 SER 202 207 207 SER SER E . n 
E 1 203 LYS 203 208 208 LYS LYS E . n 
E 1 204 TYR 204 209 209 TYR TYR E . n 
E 1 205 GLN 205 210 210 GLN GLN E . n 
E 1 206 GLN 206 211 211 GLN GLN E . n 
E 1 207 SER 207 212 212 SER SER E . n 
E 1 208 PHE 208 213 213 PHE PHE E . n 
E 1 209 THR 209 214 214 THR THR E . n 
E 1 210 PRO 210 215 215 PRO PRO E . n 
E 1 211 ASN 211 216 216 ASN ASN E . n 
E 1 212 PRO 212 217 217 PRO PRO E . n 
E 1 213 GLY 213 218 218 GLY GLY E . n 
E 1 214 ALA 214 219 219 ALA ALA E . n 
E 1 215 ARG 215 220 220 ARG ARG E . n 
E 1 216 ARG 216 229 229 ARG ARG E . n 
E 1 217 ILE 217 230 230 ILE ILE E . n 
E 1 218 ASP 218 231 231 ASP ASP E . n 
E 1 219 PHE 219 232 232 PHE PHE E . n 
E 1 220 HIS 220 233 233 HIS HIS E . n 
E 1 221 TRP 221 234 234 TRP TRP E . n 
E 1 222 LEU 222 235 235 LEU LEU E . n 
E 1 223 LEU 223 236 236 LEU LEU E . n 
E 1 224 LEU 224 237 237 LEU LEU E . n 
E 1 225 ASP 225 238 238 ASP ASP E . n 
E 1 226 PRO 226 239 239 PRO PRO E . n 
E 1 227 ASN 227 240 240 ASN ASN E . n 
E 1 228 ASP 228 241 241 ASP ASP E . n 
E 1 229 THR 229 242 242 THR THR E . n 
E 1 230 VAL 230 243 243 VAL VAL E . n 
E 1 231 THR 231 244 244 THR THR E . n 
E 1 232 PHE 232 245 245 PHE PHE E . n 
E 1 233 THR 233 246 246 THR THR E . n 
E 1 234 PHE 234 247 247 PHE PHE E . n 
E 1 235 ASN 235 248 248 ASN ASN E . n 
E 1 236 GLY 236 249 249 GLY GLY E . n 
E 1 237 ALA 237 250 250 ALA ALA E . n 
E 1 238 PHE 238 251 251 PHE PHE E . n 
E 1 239 ILE 239 252 252 ILE ILE E . n 
E 1 240 ALA 240 253 253 ALA ALA E . n 
E 1 241 PRO 241 254 254 PRO PRO E . n 
E 1 242 ASP 242 255 255 ASP ASP E . n 
E 1 243 ARG 243 256 256 ARG ARG E . n 
E 1 244 THR 244 257 257 THR THR E . n 
E 1 245 SER 245 258 258 SER SER E . n 
E 1 246 PHE 246 259 259 PHE PHE E . n 
E 1 247 PHE 247 260 260 PHE PHE E . n 
E 1 248 ARG 248 261 261 ARG ARG E . n 
E 1 249 GLY 249 263 263 GLY GLY E . n 
E 1 250 GLU 250 264 264 GLU GLU E . n 
E 1 251 SER 251 265 265 SER SER E . n 
E 1 252 LEU 252 266 266 LEU LEU E . n 
E 1 253 GLY 253 267 267 GLY GLY E . n 
E 1 254 VAL 254 268 268 VAL VAL E . n 
E 1 255 GLN 255 269 269 GLN GLN E . n 
E 1 256 SER 256 270 270 SER SER E . n 
E 1 257 ASP 257 271 271 ASP ASP E . n 
E 1 258 ALA 258 272 272 ALA ALA E . n 
E 1 259 PRO 259 273 273 PRO PRO E . n 
E 1 260 LEU 260 274 274 LEU LEU E . n 
E 1 261 ASP 261 275 275 ASP ASP E . n 
E 1 262 SER 262 276 276 SER SER E . n 
E 1 263 SER 263 276 276 SER SER E A n 
E 1 264 CYS 264 277 277 CYS CYS E . n 
E 1 265 ARG 265 278 278 ARG ARG E . n 
E 1 266 GLY 266 279 279 GLY GLY E . n 
E 1 267 ASP 267 280 280 ASP ASP E . n 
E 1 268 CYS 268 281 281 CYS CYS E . n 
E 1 269 PHE 269 282 282 PHE PHE E . n 
E 1 270 HIS 270 283 283 HIS HIS E . n 
E 1 271 SER 271 284 284 SER SER E . n 
E 1 272 GLY 272 285 285 GLY GLY E . n 
E 1 273 GLY 273 286 286 GLY GLY E . n 
E 1 274 THR 274 287 287 THR THR E . n 
E 1 275 ILE 275 288 288 ILE ILE E . n 
E 1 276 VAL 276 289 289 VAL VAL E . n 
E 1 277 SER 277 290 290 SER SER E . n 
E 1 278 SER 278 291 291 SER SER E . n 
E 1 279 LEU 279 292 292 LEU LEU E . n 
E 1 280 PRO 280 293 293 PRO PRO E . n 
E 1 281 PHE 281 294 294 PHE PHE E . n 
E 1 282 GLN 282 295 295 GLN GLN E . n 
E 1 283 ASN 283 296 296 ASN ASN E . n 
E 1 284 ILE 284 297 297 ILE ILE E . n 
E 1 285 ASN 285 298 298 ASN ASN E . n 
E 1 286 SER 286 299 299 SER SER E . n 
E 1 287 ARG 287 300 300 ARG ARG E . n 
E 1 288 THR 288 301 301 THR THR E . n 
E 1 289 VAL 289 302 302 VAL VAL E . n 
E 1 290 GLY 290 303 303 GLY GLY E . n 
E 1 291 LYS 291 304 304 LYS LYS E . n 
E 1 292 CYS 292 305 305 CYS CYS E . n 
E 1 293 PRO 293 306 306 PRO PRO E . n 
E 1 294 ARG 294 307 307 ARG ARG E . n 
E 1 295 TYR 295 308 308 TYR TYR E . n 
E 1 296 VAL 296 309 309 VAL VAL E . n 
E 1 297 LYS 297 310 310 LYS LYS E . n 
E 1 298 GLN 298 311 311 GLN GLN E . n 
E 1 299 LYS 299 312 312 LYS LYS E . n 
E 1 300 SER 300 313 313 SER SER E . n 
E 1 301 LEU 301 314 314 LEU LEU E . n 
E 1 302 LEU 302 315 315 LEU LEU E . n 
E 1 303 LEU 303 316 316 LEU LEU E . n 
E 1 304 ALA 304 317 317 ALA ALA E . n 
E 1 305 THR 305 318 318 THR THR E . n 
E 1 306 GLY 306 319 319 GLY GLY E . n 
E 1 307 MET 307 320 320 MET MET E . n 
E 1 308 ARG 308 321 321 ARG ARG E . n 
E 1 309 ASN 309 322 322 ASN ASN E . n 
E 1 310 VAL 310 323 323 VAL VAL E . n 
E 1 311 PRO 311 324 324 PRO PRO E . n 
E 1 312 GLU 312 325 325 GLU GLU E . n 
E 1 313 LYS 313 326 ?   ?   ?   E . n 
E 1 314 PRO 314 327 ?   ?   ?   E . n 
E 1 315 LYS 315 328 ?   ?   ?   E . n 
E 1 316 PRO 316 329 ?   ?   ?   E . n 
E 1 317 ARG 317 330 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  ASN 12  12  12  ASN ASN F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLU 15  15  15  GLU GLU F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  LEU 17  17  17  LEU LEU F . n 
F 2 18  ILE 18  18  18  ILE ILE F . n 
F 2 19  ASN 19  19  19  ASN ASN F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  PHE 24  24  24  PHE PHE F . n 
F 2 25  ARG 25  25  25  ARG ARG F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  GLN 27  27  27  GLN GLN F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  ALA 29  29  29  ALA ALA F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  GLU 32  32  32  GLU GLU F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  THR 34  34  34  THR THR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  TYR 38  38  38  TYR TYR F . n 
F 2 39  LYS 39  39  39  LYS LYS F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  SER 43  43  43  SER SER F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLN 47  47  47  GLN GLN F . n 
F 2 48  ILE 48  48  48  ILE ILE F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  GLY 50  50  50  GLY GLY F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  LEU 52  52  52  LEU LEU F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  ARG 54  54  54  ARG ARG F . n 
F 2 55  LEU 55  55  55  LEU LEU F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  GLY 57  57  57  GLY GLY F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  THR 59  59  59  THR THR F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  GLN 61  61  61  GLN GLN F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  LEU 65  65  65  LEU LEU F . n 
F 2 66  ILE 66  66  66  ILE ILE F . n 
F 2 67  ASP 67  67  67  ASP ASP F . n 
F 2 68  ASN 68  68  68  ASN ASN F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  GLU 72  72  72  GLU GLU F . n 
F 2 73  ILE 73  73  73  ILE ILE F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  GLN 75  75  75  GLN GLN F . n 
F 2 76  GLN 76  76  76  GLN GLN F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLY 78  78  78  GLY GLY F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  VAL 80  80  80  VAL VAL F . n 
F 2 81  ILE 81  81  81  ILE ILE F . n 
F 2 82  ASN 82  82  82  ASN ASN F . n 
F 2 83  TRP 83  83  83  TRP TRP F . n 
F 2 84  THR 84  84  84  THR THR F . n 
F 2 85  ARG 85  85  85  ARG ARG F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  ALA 87  87  87  ALA ALA F . n 
F 2 88  MET 88  88  88  MET MET F . n 
F 2 89  THR 89  89  89  THR THR F . n 
F 2 90  GLU 90  90  90  GLU GLU F . n 
F 2 91  ILE 91  91  91  ILE ILE F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  SER 93  93  93  SER SER F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 ALA 101 101 101 ALA ALA F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLN 105 105 105 GLN GLN F . n 
F 2 106 HIS 106 106 106 HIS HIS F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 ILE 108 108 108 ILE ILE F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 LEU 110 110 110 LEU LEU F . n 
F 2 111 ALA 111 111 111 ALA ALA F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 GLU 114 114 114 GLU GLU F . n 
F 2 115 MET 115 115 115 MET MET F . n 
F 2 116 SER 116 116 116 SER SER F . n 
F 2 117 LYS 117 117 117 LYS LYS F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 GLU 120 120 120 GLU GLU F . n 
F 2 121 ARG 121 121 121 ARG ARG F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 LYS 123 123 123 LYS LYS F . n 
F 2 124 LYS 124 124 124 LYS LYS F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 GLU 128 128 128 GLU GLU F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 GLU 131 131 131 GLU GLU F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 ASP 133 133 133 ASP ASP F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 THR 135 135 135 THR THR F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 ILE 140 140 140 ILE ILE F . n 
F 2 141 PHE 141 141 141 PHE PHE F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASP 146 146 146 ASP ASP F . n 
F 2 147 GLN 147 147 147 GLN GLN F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 ILE 152 152 152 ILE ILE F . n 
F 2 153 ARG 153 153 153 ARG ARG F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 ASN 155 155 155 ASN ASN F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 HIS 159 159 159 HIS HIS F . n 
F 2 160 THR 160 160 160 THR THR F . n 
F 2 161 GLN 161 161 161 GLN GLN F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 ARG 163 163 163 ARG ARG F . n 
F 2 164 THR 164 164 164 THR THR F . n 
F 2 165 GLU 165 165 165 GLU GLU F . n 
F 2 166 SER 166 166 166 SER SER F . n 
F 2 167 LEU 167 167 167 LEU LEU F . n 
F 2 168 GLN 168 168 168 GLN GLN F . n 
F 2 169 ASN 169 169 169 ASN ASN F . n 
F 2 170 ARG 170 170 170 ARG ARG F . n 
F 2 171 ILE 171 171 171 ILE ILE F . n 
F 2 172 GLN 172 172 ?   ?   ?   F . n 
F 2 173 ILE 173 173 ?   ?   ?   F . n 
F 2 174 ASP 174 174 ?   ?   ?   F . n 
F 2 175 SER 175 175 ?   ?   ?   F . n 
F 2 176 GLY 176 176 ?   ?   ?   F . n 
F 2 177 ARG 177 177 ?   ?   ?   F . n 
F 2 178 LEU 178 178 ?   ?   ?   F . n 
F 2 179 VAL 179 179 ?   ?   ?   F . n 
F 2 180 PRO 180 180 ?   ?   ?   F . n 
F 2 181 ARG 181 181 ?   ?   ?   F . n 
F 2 182 GLY 182 182 ?   ?   ?   F . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 32 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 
2 C ASN 32 C ASN 38 ? ASN 'GLYCOSYLATION SITE' 
3 E ASN 32 E ASN 38 ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 82 D ASN 82 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 82 B ASN 82 ? ASN 'GLYCOSYLATION SITE' 
6 F ASN 82 F ASN 82 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,G,H,I,J,K,L,M,N,AA,BA 
2 1 C,D,O,P,Q,R,S,T,CA,DA     
3 1 E,F,U,V,W,X,Y,Z,EA,FA     
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 8240  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  23720 ? 
2 'ABSA (A^2)' 7740  ? 
2 MORE         -24   ? 
2 'SSA (A^2)'  23450 ? 
3 'ABSA (A^2)' 7920  ? 
3 MORE         -24   ? 
3 'SSA (A^2)'  23230 ? 
# 
_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 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-09-22 
2 'Structure model' 1 1 2011-07-13 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -31.1624 -10.2513 56.8864 0.0259 0.0494 0.1041 -0.0072 -0.0295 -0.0192 0.4596 0.3765 3.9383 0.1784 
-1.0968 -0.5467 -0.0287 0.0431  -0.0244 0.0532  -0.0267 -0.0230 0.1020  -0.1684 0.0554  
'X-RAY DIFFRACTION' 2 ? refined -13.7374 -3.0426  9.2457  0.0271 0.0599 0.0779 0.0137  -0.0183 -0.0052 0.2661 0.3491 4.5567 
-0.0055 -0.9187 0.3142  -0.0272 0.0591  -0.0079 -0.0667 -0.0222 0.0840  -0.0061 -0.1310 0.0494  
'X-RAY DIFFRACTION' 3 ? refined -0.0572  -9.3681  66.2300 0.1595 0.1433 0.1671 0.1176  -0.0375 -0.0425 0.6949 0.4561 2.9099 
-0.2486 -0.3577 -0.0115 -0.1229 -0.2585 0.1183  0.1554  0.1157  -0.0454 0.0231  0.0242  0.0072  
'X-RAY DIFFRACTION' 4 ? refined 5.6005   -9.0145  15.3223 0.0943 0.1284 0.1587 0.0819  0.0123  -0.0110 0.6705 0.3902 4.7325 
-0.0359 -1.1237 0.0883  -0.0561 0.0141  -0.1327 -0.0101 0.0032  -0.0604 0.2667  0.4864  0.0529  
'X-RAY DIFFRACTION' 5 ? refined -16.6730 18.0843  62.3485 0.1601 0.0479 0.1480 -0.0331 0.0243  -0.0052 0.7246 0.1269 2.8445 
-0.0850 -1.0144 0.1759  -0.0251 -0.0899 0.0459  0.0154  0.0660  0.0064  -0.0542 0.1482  -0.0409 
'X-RAY DIFFRACTION' 6 ? refined 0.4112   11.4490  14.3638 0.0642 0.0550 0.1090 -0.0364 0.0067  0.0220  0.6811 0.4397 5.9692 0.1935 
-1.2792 0.1237  0.0217  -0.0188 0.0203  -0.0724 -0.0179 -0.0495 -0.4360 0.4176  -0.0038 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A -10 ? ? A 9999 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B -10 ? ? B 9999 ? ? ? ? 
'X-RAY DIFFRACTION' 3 3 C -10 ? ? C 9999 ? ? ? ? 
'X-RAY DIFFRACTION' 4 4 D -10 ? ? D 9999 ? ? ? ? 
'X-RAY DIFFRACTION' 5 5 E -10 ? ? E 9999 ? ? ? ? 
'X-RAY DIFFRACTION' 6 6 F -10 ? ? F 9999 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
PHASER   phasing           .        ? 2 
REFMAC   refinement        5.5.0044 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_pdbx_entry_details.entry_id             3M5H 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
'THE CONFLICTS IN THE SEQUENCE IS BECAUSE THE AUTHORS USED THE GENEBANK SEQUENCE ACC55270.1 WHICH IS A SLIGHTLY DIFFERENT STRAIN' 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
# 
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 LYS A 49  ? ? -77.82  41.71   
2  1 ASN A 133 ? ? -94.74  40.75   
3  1 CYS A 139 ? ? -115.51 61.47   
4  1 ARG A 141 ? ? -166.57 81.45   
5  1 SER A 142 ? ? 65.17   67.00   
6  1 SER A 146 ? ? -120.59 -154.92 
7  1 ASN A 158 B ? 80.01   -10.13  
8  1 SER A 207 ? ? -69.53  0.27    
9  1 ARG A 220 ? ? -31.77  119.12  
10 1 ASN A 240 ? ? 77.90   -11.29  
11 1 ALA B 5   ? ? -91.28  -73.26  
12 1 LYS B 58  ? ? -47.03  152.18  
13 1 ARG B 127 ? ? 55.85   -109.35 
14 1 GLN B 172 ? ? -96.70  54.65   
15 1 LYS C 49  ? ? -79.12  39.00   
16 1 ARG C 141 ? ? -154.28 87.46   
17 1 SER C 146 ? ? -145.21 -150.04 
18 1 TYR C 195 ? ? -119.23 -155.40 
19 1 LYS C 208 ? ? -142.60 24.40   
20 1 ALA D 5   ? ? -85.25  -76.64  
21 1 ASN D 28  ? ? -137.47 -154.23 
22 1 ARG D 127 ? ? 52.00   -121.98 
23 1 LYS E 49  ? ? -74.15  46.82   
24 1 ARG E 141 ? ? -156.50 78.15   
25 1 TYR E 195 ? ? -121.00 -163.74 
26 1 SER E 206 ? ? -117.96 -166.78 
27 1 ARG E 220 ? ? 58.78   77.39   
28 1 ASN E 240 ? ? 64.22   -5.33   
29 1 ALA E 250 ? ? 53.95   19.32   
30 1 ALA F 5   ? ? -94.12  -66.76  
31 1 ASN F 28  ? ? -149.87 -157.30 
32 1 ARG F 127 ? ? 46.91   -129.07 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    E 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     331 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     C 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     GAL 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      2 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O1 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    L 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    GAL 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     2 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O1 
# 
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 A ALA 7   ? A ALA 1   
2  1 Y 1 A ASP 8   ? A ASP 2   
3  1 Y 1 A PRO 9   ? A PRO 3   
4  1 Y 1 A PRO 327 ? A PRO 314 
5  1 Y 1 A LYS 328 ? A LYS 315 
6  1 Y 1 A PRO 329 ? A PRO 316 
7  1 Y 1 A ARG 330 ? A ARG 317 
8  1 Y 1 B ARG 177 ? B ARG 177 
9  1 Y 1 B LEU 178 ? B LEU 178 
10 1 Y 1 B VAL 179 ? B VAL 179 
11 1 Y 1 B PRO 180 ? B PRO 180 
12 1 Y 1 B ARG 181 ? B ARG 181 
13 1 Y 1 B GLY 182 ? B GLY 182 
14 1 Y 1 C ALA 7   ? C ALA 1   
15 1 Y 1 C ASP 8   ? C ASP 2   
16 1 Y 1 C PRO 9   ? C PRO 3   
17 1 Y 1 C GLY 10  ? C GLY 4   
18 1 Y 1 C PRO 327 ? C PRO 314 
19 1 Y 1 C LYS 328 ? C LYS 315 
20 1 Y 1 C PRO 329 ? C PRO 316 
21 1 Y 1 C ARG 330 ? C ARG 317 
22 1 Y 1 D ILE 173 ? D ILE 173 
23 1 Y 1 D ASP 174 ? D ASP 174 
24 1 Y 1 D SER 175 ? D SER 175 
25 1 Y 1 D GLY 176 ? D GLY 176 
26 1 Y 1 D ARG 177 ? D ARG 177 
27 1 Y 1 D LEU 178 ? D LEU 178 
28 1 Y 1 D VAL 179 ? D VAL 179 
29 1 Y 1 D PRO 180 ? D PRO 180 
30 1 Y 1 D ARG 181 ? D ARG 181 
31 1 Y 1 D GLY 182 ? D GLY 182 
32 1 Y 1 E ALA 7   ? E ALA 1   
33 1 Y 1 E ASP 8   ? E ASP 2   
34 1 Y 1 E PRO 9   ? E PRO 3   
35 1 Y 1 E LYS 326 ? E LYS 313 
36 1 Y 1 E PRO 327 ? E PRO 314 
37 1 Y 1 E LYS 328 ? E LYS 315 
38 1 Y 1 E PRO 329 ? E PRO 316 
39 1 Y 1 E ARG 330 ? E ARG 317 
40 1 Y 1 F GLN 172 ? F GLN 172 
41 1 Y 1 F ILE 173 ? F ILE 173 
42 1 Y 1 F ASP 174 ? F ASP 174 
43 1 Y 1 F SER 175 ? F SER 175 
44 1 Y 1 F GLY 176 ? F GLY 176 
45 1 Y 1 F ARG 177 ? F ARG 177 
46 1 Y 1 F LEU 178 ? F LEU 178 
47 1 Y 1 F VAL 179 ? F VAL 179 
48 1 Y 1 F PRO 180 ? F PRO 180 
49 1 Y 1 F ARG 181 ? F ARG 181 
50 1 Y 1 F GLY 182 ? F GLY 182 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'O-SIALIC ACID'        SIA 
4 BETA-D-GALACTOSE       GAL 
5 N-ACETYL-D-GLUCOSAMINE NAG 
6 GLYCEROL               GOL 
7 water                  HOH 
# 
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 
G  3 SIA 1  1   1   SIA SIA A . 
H  4 GAL 2  2   2   GAL GAL A . 
I  5 NAG 3  3   3   NAG NAG A . 
J  5 NAG 1  331 1   NAG NAG A . 
K  5 NAG 1  183 1   NAG NAG B . 
L  5 NAG 2  184 2   NAG NAG B . 
M  6 GOL 1  185 1   GOL GOL B . 
N  6 GOL 1  186 4   GOL GOL B . 
O  3 SIA 1  1   1   SIA SIA C . 
P  4 GAL 2  2   2   GAL GAL C . 
Q  5 NAG 1  331 1   NAG NAG C . 
R  5 NAG 2  332 2   NAG NAG C . 
S  5 NAG 1  183 1   NAG NAG D . 
T  6 GOL 1  184 3   GOL GOL D . 
U  3 SIA 1  1   1   SIA SIA E . 
V  4 GAL 2  2   2   GAL GAL E . 
W  5 NAG 3  3   3   NAG NAG E . 
X  5 NAG 1  331 1   NAG NAG E . 
Y  5 NAG 1  183 1   NAG NAG F . 
Z  6 GOL 1  184 2   GOL GOL F . 
AA 7 HOH 1  6   6   HOH HOH A . 
AA 7 HOH 2  224 224 HOH HOH A . 
AA 7 HOH 3  226 226 HOH HOH A . 
AA 7 HOH 4  332 9   HOH HOH A . 
AA 7 HOH 5  333 12  HOH HOH A . 
AA 7 HOH 6  334 15  HOH HOH A . 
AA 7 HOH 7  335 29  HOH HOH A . 
AA 7 HOH 8  336 30  HOH HOH A . 
AA 7 HOH 9  337 33  HOH HOH A . 
AA 7 HOH 10 338 39  HOH HOH A . 
AA 7 HOH 11 339 42  HOH HOH A . 
AA 7 HOH 12 340 47  HOH HOH A . 
AA 7 HOH 13 341 48  HOH HOH A . 
AA 7 HOH 14 342 50  HOH HOH A . 
AA 7 HOH 15 343 56  HOH HOH A . 
AA 7 HOH 16 344 57  HOH HOH A . 
AA 7 HOH 17 345 61  HOH HOH A . 
AA 7 HOH 18 346 71  HOH HOH A . 
AA 7 HOH 19 347 74  HOH HOH A . 
AA 7 HOH 20 348 75  HOH HOH A . 
AA 7 HOH 21 349 349 HOH HOH A . 
AA 7 HOH 22 350 350 HOH HOH A . 
AA 7 HOH 23 351 77  HOH HOH A . 
AA 7 HOH 24 352 352 HOH HOH A . 
AA 7 HOH 25 353 85  HOH HOH A . 
AA 7 HOH 26 354 93  HOH HOH A . 
AA 7 HOH 27 355 98  HOH HOH A . 
AA 7 HOH 28 356 103 HOH HOH A . 
AA 7 HOH 29 357 105 HOH HOH A . 
AA 7 HOH 30 358 106 HOH HOH A . 
AA 7 HOH 31 359 110 HOH HOH A . 
AA 7 HOH 32 360 131 HOH HOH A . 
AA 7 HOH 33 361 132 HOH HOH A . 
AA 7 HOH 34 362 134 HOH HOH A . 
AA 7 HOH 35 363 139 HOH HOH A . 
AA 7 HOH 36 364 142 HOH HOH A . 
AA 7 HOH 37 365 145 HOH HOH A . 
AA 7 HOH 38 366 156 HOH HOH A . 
AA 7 HOH 39 367 161 HOH HOH A . 
AA 7 HOH 40 368 169 HOH HOH A . 
AA 7 HOH 41 369 170 HOH HOH A . 
AA 7 HOH 42 370 189 HOH HOH A . 
AA 7 HOH 43 371 213 HOH HOH A . 
AA 7 HOH 44 372 251 HOH HOH A . 
AA 7 HOH 45 373 253 HOH HOH A . 
AA 7 HOH 46 374 254 HOH HOH A . 
AA 7 HOH 47 375 260 HOH HOH A . 
AA 7 HOH 48 376 279 HOH HOH A . 
AA 7 HOH 49 377 287 HOH HOH A . 
BA 7 HOH 1  187 3   HOH HOH B . 
BA 7 HOH 2  188 4   HOH HOH B . 
BA 7 HOH 3  189 11  HOH HOH B . 
BA 7 HOH 4  190 13  HOH HOH B . 
BA 7 HOH 5  191 27  HOH HOH B . 
BA 7 HOH 6  192 28  HOH HOH B . 
BA 7 HOH 7  193 37  HOH HOH B . 
BA 7 HOH 8  194 41  HOH HOH B . 
BA 7 HOH 9  195 53  HOH HOH B . 
BA 7 HOH 10 196 54  HOH HOH B . 
BA 7 HOH 11 197 55  HOH HOH B . 
BA 7 HOH 12 198 58  HOH HOH B . 
BA 7 HOH 13 199 62  HOH HOH B . 
BA 7 HOH 14 200 72  HOH HOH B . 
BA 7 HOH 15 201 89  HOH HOH B . 
BA 7 HOH 16 202 94  HOH HOH B . 
BA 7 HOH 17 203 101 HOH HOH B . 
BA 7 HOH 18 204 104 HOH HOH B . 
BA 7 HOH 19 205 112 HOH HOH B . 
BA 7 HOH 20 206 114 HOH HOH B . 
BA 7 HOH 21 207 119 HOH HOH B . 
BA 7 HOH 22 208 120 HOH HOH B . 
BA 7 HOH 23 209 121 HOH HOH B . 
BA 7 HOH 24 210 129 HOH HOH B . 
BA 7 HOH 25 211 135 HOH HOH B . 
BA 7 HOH 26 212 212 HOH HOH B . 
BA 7 HOH 27 213 137 HOH HOH B . 
BA 7 HOH 28 214 141 HOH HOH B . 
BA 7 HOH 29 215 151 HOH HOH B . 
BA 7 HOH 30 216 152 HOH HOH B . 
BA 7 HOH 31 217 160 HOH HOH B . 
BA 7 HOH 32 218 164 HOH HOH B . 
BA 7 HOH 33 219 166 HOH HOH B . 
BA 7 HOH 34 220 171 HOH HOH B . 
BA 7 HOH 35 221 174 HOH HOH B . 
BA 7 HOH 36 222 179 HOH HOH B . 
BA 7 HOH 37 223 184 HOH HOH B . 
BA 7 HOH 38 233 233 HOH HOH B . 
BA 7 HOH 39 256 256 HOH HOH B . 
BA 7 HOH 40 266 266 HOH HOH B . 
BA 7 HOH 41 282 282 HOH HOH B . 
BA 7 HOH 42 366 366 HOH HOH B . 
BA 7 HOH 43 368 368 HOH HOH B . 
BA 7 HOH 44 371 371 HOH HOH B . 
CA 7 HOH 1  222 222 HOH HOH C . 
CA 7 HOH 2  333 31  HOH HOH C . 
CA 7 HOH 3  334 36  HOH HOH C . 
CA 7 HOH 4  335 38  HOH HOH C . 
CA 7 HOH 5  336 44  HOH HOH C . 
CA 7 HOH 6  337 51  HOH HOH C . 
CA 7 HOH 7  338 60  HOH HOH C . 
CA 7 HOH 8  339 66  HOH HOH C . 
CA 7 HOH 9  340 70  HOH HOH C . 
CA 7 HOH 10 341 73  HOH HOH C . 
CA 7 HOH 11 342 80  HOH HOH C . 
CA 7 HOH 12 343 81  HOH HOH C . 
CA 7 HOH 13 344 86  HOH HOH C . 
CA 7 HOH 14 345 91  HOH HOH C . 
CA 7 HOH 15 346 95  HOH HOH C . 
CA 7 HOH 16 347 99  HOH HOH C . 
CA 7 HOH 17 348 348 HOH HOH C . 
CA 7 HOH 18 349 108 HOH HOH C . 
CA 7 HOH 19 350 113 HOH HOH C . 
CA 7 HOH 20 351 116 HOH HOH C . 
CA 7 HOH 21 352 128 HOH HOH C . 
CA 7 HOH 22 353 353 HOH HOH C . 
CA 7 HOH 23 354 146 HOH HOH C . 
CA 7 HOH 24 355 154 HOH HOH C . 
CA 7 HOH 25 356 159 HOH HOH C . 
CA 7 HOH 26 357 172 HOH HOH C . 
CA 7 HOH 27 358 358 HOH HOH C . 
CA 7 HOH 28 359 175 HOH HOH C . 
CA 7 HOH 29 360 191 HOH HOH C . 
CA 7 HOH 30 361 192 HOH HOH C . 
CA 7 HOH 31 362 197 HOH HOH C . 
CA 7 HOH 32 363 363 HOH HOH C . 
CA 7 HOH 33 364 198 HOH HOH C . 
CA 7 HOH 34 365 203 HOH HOH C . 
CA 7 HOH 35 366 207 HOH HOH C . 
CA 7 HOH 36 367 210 HOH HOH C . 
CA 7 HOH 37 368 215 HOH HOH C . 
CA 7 HOH 38 369 237 HOH HOH C . 
CA 7 HOH 39 370 370 HOH HOH C . 
CA 7 HOH 40 371 241 HOH HOH C . 
CA 7 HOH 41 372 372 HOH HOH C . 
CA 7 HOH 42 373 247 HOH HOH C . 
CA 7 HOH 43 374 280 HOH HOH C . 
CA 7 HOH 44 375 283 HOH HOH C . 
CA 7 HOH 45 376 285 HOH HOH C . 
CA 7 HOH 46 377 300 HOH HOH C . 
DA 7 HOH 1  185 20  HOH HOH D . 
DA 7 HOH 2  186 22  HOH HOH D . 
DA 7 HOH 3  187 23  HOH HOH D . 
DA 7 HOH 4  188 188 HOH HOH D . 
DA 7 HOH 5  189 26  HOH HOH D . 
DA 7 HOH 6  190 32  HOH HOH D . 
DA 7 HOH 7  191 63  HOH HOH D . 
DA 7 HOH 8  192 65  HOH HOH D . 
DA 7 HOH 9  193 68  HOH HOH D . 
DA 7 HOH 10 194 194 HOH HOH D . 
DA 7 HOH 11 195 84  HOH HOH D . 
DA 7 HOH 12 196 97  HOH HOH D . 
DA 7 HOH 13 197 111 HOH HOH D . 
DA 7 HOH 14 198 115 HOH HOH D . 
DA 7 HOH 15 199 199 HOH HOH D . 
DA 7 HOH 16 200 127 HOH HOH D . 
DA 7 HOH 17 201 138 HOH HOH D . 
DA 7 HOH 18 202 202 HOH HOH D . 
DA 7 HOH 19 203 140 HOH HOH D . 
DA 7 HOH 20 204 147 HOH HOH D . 
DA 7 HOH 21 205 148 HOH HOH D . 
DA 7 HOH 22 206 176 HOH HOH D . 
DA 7 HOH 23 207 180 HOH HOH D . 
DA 7 HOH 24 231 231 HOH HOH D . 
DA 7 HOH 25 236 236 HOH HOH D . 
DA 7 HOH 26 259 259 HOH HOH D . 
DA 7 HOH 27 262 262 HOH HOH D . 
DA 7 HOH 28 277 277 HOH HOH D . 
DA 7 HOH 29 365 365 HOH HOH D . 
EA 7 HOH 1  5   5   HOH HOH E . 
EA 7 HOH 2  143 143 HOH HOH E . 
EA 7 HOH 3  223 223 HOH HOH E . 
EA 7 HOH 4  228 228 HOH HOH E . 
EA 7 HOH 5  332 10  HOH HOH E . 
EA 7 HOH 6  333 17  HOH HOH E . 
EA 7 HOH 7  334 19  HOH HOH E . 
EA 7 HOH 8  335 24  HOH HOH E . 
EA 7 HOH 9  336 34  HOH HOH E . 
EA 7 HOH 10 337 40  HOH HOH E . 
EA 7 HOH 11 338 43  HOH HOH E . 
EA 7 HOH 12 339 45  HOH HOH E . 
EA 7 HOH 13 340 46  HOH HOH E . 
EA 7 HOH 14 341 52  HOH HOH E . 
EA 7 HOH 15 342 59  HOH HOH E . 
EA 7 HOH 16 343 64  HOH HOH E . 
EA 7 HOH 17 344 67  HOH HOH E . 
EA 7 HOH 18 345 76  HOH HOH E . 
EA 7 HOH 19 346 78  HOH HOH E . 
EA 7 HOH 20 347 83  HOH HOH E . 
EA 7 HOH 21 348 88  HOH HOH E . 
EA 7 HOH 22 349 90  HOH HOH E . 
EA 7 HOH 23 350 96  HOH HOH E . 
EA 7 HOH 24 351 351 HOH HOH E . 
EA 7 HOH 25 352 122 HOH HOH E . 
EA 7 HOH 26 353 123 HOH HOH E . 
EA 7 HOH 27 354 126 HOH HOH E . 
EA 7 HOH 28 355 130 HOH HOH E . 
EA 7 HOH 29 356 136 HOH HOH E . 
EA 7 HOH 30 357 144 HOH HOH E . 
EA 7 HOH 31 358 149 HOH HOH E . 
EA 7 HOH 32 359 163 HOH HOH E . 
EA 7 HOH 33 360 165 HOH HOH E . 
EA 7 HOH 34 361 167 HOH HOH E . 
EA 7 HOH 35 362 168 HOH HOH E . 
EA 7 HOH 36 363 173 HOH HOH E . 
EA 7 HOH 37 364 364 HOH HOH E . 
EA 7 HOH 38 365 186 HOH HOH E . 
EA 7 HOH 39 366 187 HOH HOH E . 
EA 7 HOH 40 367 193 HOH HOH E . 
EA 7 HOH 41 368 195 HOH HOH E . 
EA 7 HOH 42 369 196 HOH HOH E . 
EA 7 HOH 43 370 209 HOH HOH E . 
EA 7 HOH 44 371 232 HOH HOH E . 
EA 7 HOH 45 372 249 HOH HOH E . 
EA 7 HOH 46 373 373 HOH HOH E . 
EA 7 HOH 47 374 374 HOH HOH E . 
EA 7 HOH 48 375 375 HOH HOH E . 
EA 7 HOH 49 376 376 HOH HOH E . 
EA 7 HOH 50 377 377 HOH HOH E . 
EA 7 HOH 51 378 258 HOH HOH E . 
EA 7 HOH 52 379 267 HOH HOH E . 
EA 7 HOH 53 380 268 HOH HOH E . 
EA 7 HOH 54 381 271 HOH HOH E . 
EA 7 HOH 55 382 289 HOH HOH E . 
EA 7 HOH 56 383 304 HOH HOH E . 
FA 7 HOH 1  185 2   HOH HOH F . 
FA 7 HOH 2  186 7   HOH HOH F . 
FA 7 HOH 3  187 21  HOH HOH F . 
FA 7 HOH 4  188 35  HOH HOH F . 
FA 7 HOH 5  189 69  HOH HOH F . 
FA 7 HOH 6  190 79  HOH HOH F . 
FA 7 HOH 7  191 82  HOH HOH F . 
FA 7 HOH 8  192 87  HOH HOH F . 
FA 7 HOH 9  193 92  HOH HOH F . 
FA 7 HOH 10 194 100 HOH HOH F . 
FA 7 HOH 11 195 102 HOH HOH F . 
FA 7 HOH 12 196 107 HOH HOH F . 
FA 7 HOH 13 197 109 HOH HOH F . 
FA 7 HOH 14 198 117 HOH HOH F . 
FA 7 HOH 15 199 125 HOH HOH F . 
FA 7 HOH 16 200 150 HOH HOH F . 
FA 7 HOH 17 201 157 HOH HOH F . 
FA 7 HOH 18 202 158 HOH HOH F . 
FA 7 HOH 19 203 162 HOH HOH F . 
FA 7 HOH 20 204 177 HOH HOH F . 
FA 7 HOH 21 205 205 HOH HOH F . 
FA 7 HOH 22 206 178 HOH HOH F . 
FA 7 HOH 23 245 245 HOH HOH F . 
FA 7 HOH 24 250 250 HOH HOH F . 
FA 7 HOH 25 257 257 HOH HOH F . 
FA 7 HOH 26 272 272 HOH HOH F . 
FA 7 HOH 27 273 273 HOH HOH F . 
FA 7 HOH 28 278 278 HOH HOH F . 
FA 7 HOH 29 284 284 HOH HOH F . 
FA 7 HOH 30 321 321 HOH HOH F . 
FA 7 HOH 31 327 327 HOH HOH F . 
FA 7 HOH 32 367 367 HOH HOH F . 
FA 7 HOH 33 369 369 HOH HOH F . 
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