data_2PMS
# 
_entry.id   2PMS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2PMS         
RCSB  RCSB042550   
WWPDB D_1000042550 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1H43 'N-lobe of human lactoferrin' unspecified 
PDB 1H44 'N-lobe of human lactoferrin' unspecified 
PDB 1H45 'N-lobe of human lactoferrin' unspecified 
PDB 1LCT 'N-lobe of human lactoferrin' unspecified 
PDB 1EH3 'N-lobe of human lactoferrin' unspecified 
# 
_pdbx_database_status.entry_id                        2PMS 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2007-04-23 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chattopadhyay, D.' 1 
'Senkovich, O.'     2 
'Cook, W.J.'        3 
# 
_citation.id                        primary 
_citation.title                     
;Structure of a Complex of Human Lactoferrin N-lobe with Pneumococcal Surface Protein A Provides Insight into Microbial Defense Mechanism.
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            370 
_citation.page_first                701 
_citation.page_last                 713 
_citation.year                      2007 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17543335 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2007.04.075 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Senkovich, O.'      1 
primary 'Cook, W.J.'         2 
primary 'Mirza, S.'          3 
primary 'Hollingshead, S.K.' 4 
primary 'Protasevich, I.I.'  5 
primary 'Briles, D.E.'       6 
primary 'Chattopadhyay, D.'  7 
# 
_cell.entry_id           2PMS 
_cell.length_a           130.180 
_cell.length_b           130.180 
_cell.length_c           80.800 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_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                         2PMS 
_symmetry.space_group_name_H-M             'P 32' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                145 
_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 Lactotransferrin                        38279.402 2  3.4.21.- ? 'N-terminal lobe'            ? 
2 polymer     man 'PNEUMOCOCCAL SURFACE PROTEIN A (PSPA)' 14120.603 2  ?        ? 'Lactoferrin-binding domain' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                  221.208   2  ?        ? ?                            ? 
4 non-polymer syn 'CARBONATE ION'                         60.009    2  ?        ? ?                            ? 
5 non-polymer syn 'FE (III) ION'                          55.845    2  ?        ? ?                            ? 
6 non-polymer syn 'SULFATE ION'                           96.063    6  ?        ? ?                            ? 
7 non-polymer syn 'ZINC ION'                              65.409    2  ?        ? ?                            ? 
8 water       nat water                                   18.015    24 ?        ? ?                            ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Lactoferrin, Talalactoferrin alfa' 
# 
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 
;GRRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAA
EVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVP
GADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPV
DKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLY
LGSGYFTAIQNLRKSEEEVAARRA
;
;GRRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAA
EVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVP
GADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPV
DKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLY
LGSGYFTAIQNLRKSEEEVAARRA
;
A,B ? 
2 'polypeptide(L)' no no 
;GSHMDAEEVAPQAKIAELENQVHRLEQELKEIDESESEDYAKEGFRAPLQSKLDAKKAKLSKLEELSDKIDELDAEIAKL
EDQLKAAEENNNVEDYFKEGLEKTIAAKKAELEKTEADLKKAVNE
;
;GSHMDAEEVAPQAKIAELENQVHRLEQELKEIDESESEDYAKEGFRAPLQSKLDAKKAKLSKLEELSDKIDELDAEIAKL
EDQLKAAEENNNVEDYFKEGLEKTIAAKKAELEKTEADLKKAVNE
;
C,D ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ARG n 
1 3   ARG n 
1 4   ARG n 
1 5   ARG n 
1 6   SER n 
1 7   VAL n 
1 8   GLN n 
1 9   TRP n 
1 10  CYS n 
1 11  ALA n 
1 12  VAL n 
1 13  SER n 
1 14  GLN n 
1 15  PRO n 
1 16  GLU n 
1 17  ALA n 
1 18  THR n 
1 19  LYS n 
1 20  CYS n 
1 21  PHE n 
1 22  GLN n 
1 23  TRP n 
1 24  GLN n 
1 25  ARG n 
1 26  ASN n 
1 27  MET n 
1 28  ARG n 
1 29  ARG n 
1 30  VAL n 
1 31  ARG n 
1 32  GLY n 
1 33  PRO n 
1 34  PRO n 
1 35  VAL n 
1 36  SER n 
1 37  CYS n 
1 38  ILE n 
1 39  LYS n 
1 40  ARG n 
1 41  ASP n 
1 42  SER n 
1 43  PRO n 
1 44  ILE n 
1 45  GLN n 
1 46  CYS n 
1 47  ILE n 
1 48  GLN n 
1 49  ALA n 
1 50  ILE n 
1 51  ALA n 
1 52  GLU n 
1 53  ASN n 
1 54  ARG n 
1 55  ALA n 
1 56  ASP n 
1 57  ALA n 
1 58  VAL n 
1 59  THR n 
1 60  LEU n 
1 61  ASP n 
1 62  GLY n 
1 63  GLY n 
1 64  PHE n 
1 65  ILE n 
1 66  TYR n 
1 67  GLU n 
1 68  ALA n 
1 69  GLY n 
1 70  LEU n 
1 71  ALA n 
1 72  PRO n 
1 73  TYR n 
1 74  LYS n 
1 75  LEU n 
1 76  ARG n 
1 77  PRO n 
1 78  VAL n 
1 79  ALA n 
1 80  ALA n 
1 81  GLU n 
1 82  VAL n 
1 83  TYR n 
1 84  GLY n 
1 85  THR n 
1 86  GLU n 
1 87  ARG n 
1 88  GLN n 
1 89  PRO n 
1 90  ARG n 
1 91  THR n 
1 92  HIS n 
1 93  TYR n 
1 94  TYR n 
1 95  ALA n 
1 96  VAL n 
1 97  ALA n 
1 98  VAL n 
1 99  VAL n 
1 100 LYS n 
1 101 LYS n 
1 102 GLY n 
1 103 GLY n 
1 104 SER n 
1 105 PHE n 
1 106 GLN n 
1 107 LEU n 
1 108 ASN n 
1 109 GLU n 
1 110 LEU n 
1 111 GLN n 
1 112 GLY n 
1 113 LEU n 
1 114 LYS n 
1 115 SER n 
1 116 CYS n 
1 117 HIS n 
1 118 THR n 
1 119 GLY n 
1 120 LEU n 
1 121 ARG n 
1 122 ARG n 
1 123 THR n 
1 124 ALA n 
1 125 GLY n 
1 126 TRP n 
1 127 ASN n 
1 128 VAL n 
1 129 PRO n 
1 130 ILE n 
1 131 GLY n 
1 132 THR n 
1 133 LEU n 
1 134 ARG n 
1 135 PRO n 
1 136 PHE n 
1 137 LEU n 
1 138 ASN n 
1 139 TRP n 
1 140 THR n 
1 141 GLY n 
1 142 PRO n 
1 143 PRO n 
1 144 GLU n 
1 145 PRO n 
1 146 ILE n 
1 147 GLU n 
1 148 ALA n 
1 149 ALA n 
1 150 VAL n 
1 151 ALA n 
1 152 ARG n 
1 153 PHE n 
1 154 PHE n 
1 155 SER n 
1 156 ALA n 
1 157 SER n 
1 158 CYS n 
1 159 VAL n 
1 160 PRO n 
1 161 GLY n 
1 162 ALA n 
1 163 ASP n 
1 164 LYS n 
1 165 GLY n 
1 166 GLN n 
1 167 PHE n 
1 168 PRO n 
1 169 ASN n 
1 170 LEU n 
1 171 CYS n 
1 172 ARG n 
1 173 LEU n 
1 174 CYS n 
1 175 ALA n 
1 176 GLY n 
1 177 THR n 
1 178 GLY n 
1 179 GLU n 
1 180 ASN n 
1 181 LYS n 
1 182 CYS n 
1 183 ALA n 
1 184 PHE n 
1 185 SER n 
1 186 SER n 
1 187 GLN n 
1 188 GLU n 
1 189 PRO n 
1 190 TYR n 
1 191 PHE n 
1 192 SER n 
1 193 TYR n 
1 194 SER n 
1 195 GLY n 
1 196 ALA n 
1 197 PHE n 
1 198 LYS n 
1 199 CYS n 
1 200 LEU n 
1 201 ARG n 
1 202 ASP n 
1 203 GLY n 
1 204 ALA n 
1 205 GLY n 
1 206 ASP n 
1 207 VAL n 
1 208 ALA n 
1 209 PHE n 
1 210 ILE n 
1 211 ARG n 
1 212 GLU n 
1 213 SER n 
1 214 THR n 
1 215 VAL n 
1 216 PHE n 
1 217 GLU n 
1 218 ASP n 
1 219 LEU n 
1 220 SER n 
1 221 ASP n 
1 222 GLU n 
1 223 ALA n 
1 224 GLU n 
1 225 ARG n 
1 226 ASP n 
1 227 GLU n 
1 228 TYR n 
1 229 GLU n 
1 230 LEU n 
1 231 LEU n 
1 232 CYS n 
1 233 PRO n 
1 234 ASP n 
1 235 ASN n 
1 236 THR n 
1 237 ARG n 
1 238 LYS n 
1 239 PRO n 
1 240 VAL n 
1 241 ASP n 
1 242 LYS n 
1 243 PHE n 
1 244 LYS n 
1 245 ASP n 
1 246 CYS n 
1 247 HIS n 
1 248 LEU n 
1 249 ALA n 
1 250 ARG n 
1 251 VAL n 
1 252 PRO n 
1 253 SER n 
1 254 HIS n 
1 255 ALA n 
1 256 VAL n 
1 257 VAL n 
1 258 ALA n 
1 259 ARG n 
1 260 SER n 
1 261 VAL n 
1 262 ASN n 
1 263 GLY n 
1 264 LYS n 
1 265 GLU n 
1 266 ASP n 
1 267 ALA n 
1 268 ILE n 
1 269 TRP n 
1 270 ASN n 
1 271 LEU n 
1 272 LEU n 
1 273 ARG n 
1 274 GLN n 
1 275 ALA n 
1 276 GLN n 
1 277 GLU n 
1 278 LYS n 
1 279 PHE n 
1 280 GLY n 
1 281 LYS n 
1 282 ASP n 
1 283 LYS n 
1 284 SER n 
1 285 PRO n 
1 286 LYS n 
1 287 PHE n 
1 288 GLN n 
1 289 LEU n 
1 290 PHE n 
1 291 GLY n 
1 292 SER n 
1 293 PRO n 
1 294 SER n 
1 295 GLY n 
1 296 GLN n 
1 297 LYS n 
1 298 ASP n 
1 299 LEU n 
1 300 LEU n 
1 301 PHE n 
1 302 LYS n 
1 303 ASP n 
1 304 SER n 
1 305 ALA n 
1 306 ILE n 
1 307 GLY n 
1 308 PHE n 
1 309 SER n 
1 310 ARG n 
1 311 VAL n 
1 312 PRO n 
1 313 PRO n 
1 314 ARG n 
1 315 ILE n 
1 316 ASP n 
1 317 SER n 
1 318 GLY n 
1 319 LEU n 
1 320 TYR n 
1 321 LEU n 
1 322 GLY n 
1 323 SER n 
1 324 GLY n 
1 325 TYR n 
1 326 PHE n 
1 327 THR n 
1 328 ALA n 
1 329 ILE n 
1 330 GLN n 
1 331 ASN n 
1 332 LEU n 
1 333 ARG n 
1 334 LYS n 
1 335 SER n 
1 336 GLU n 
1 337 GLU n 
1 338 GLU n 
1 339 VAL n 
1 340 ALA n 
1 341 ALA n 
1 342 ARG n 
1 343 ARG n 
1 344 ALA n 
2 1   GLY n 
2 2   SER n 
2 3   HIS n 
2 4   MET n 
2 5   ASP n 
2 6   ALA n 
2 7   GLU n 
2 8   GLU n 
2 9   VAL n 
2 10  ALA n 
2 11  PRO n 
2 12  GLN n 
2 13  ALA n 
2 14  LYS n 
2 15  ILE n 
2 16  ALA n 
2 17  GLU n 
2 18  LEU n 
2 19  GLU n 
2 20  ASN n 
2 21  GLN n 
2 22  VAL n 
2 23  HIS n 
2 24  ARG n 
2 25  LEU n 
2 26  GLU n 
2 27  GLN n 
2 28  GLU n 
2 29  LEU n 
2 30  LYS n 
2 31  GLU n 
2 32  ILE n 
2 33  ASP n 
2 34  GLU n 
2 35  SER n 
2 36  GLU n 
2 37  SER n 
2 38  GLU n 
2 39  ASP n 
2 40  TYR n 
2 41  ALA n 
2 42  LYS n 
2 43  GLU n 
2 44  GLY n 
2 45  PHE n 
2 46  ARG n 
2 47  ALA n 
2 48  PRO n 
2 49  LEU n 
2 50  GLN n 
2 51  SER n 
2 52  LYS n 
2 53  LEU n 
2 54  ASP n 
2 55  ALA n 
2 56  LYS n 
2 57  LYS n 
2 58  ALA n 
2 59  LYS n 
2 60  LEU n 
2 61  SER n 
2 62  LYS n 
2 63  LEU n 
2 64  GLU n 
2 65  GLU n 
2 66  LEU n 
2 67  SER n 
2 68  ASP n 
2 69  LYS n 
2 70  ILE n 
2 71  ASP n 
2 72  GLU n 
2 73  LEU n 
2 74  ASP n 
2 75  ALA n 
2 76  GLU n 
2 77  ILE n 
2 78  ALA n 
2 79  LYS n 
2 80  LEU n 
2 81  GLU n 
2 82  ASP n 
2 83  GLN n 
2 84  LEU n 
2 85  LYS n 
2 86  ALA n 
2 87  ALA n 
2 88  GLU n 
2 89  GLU n 
2 90  ASN n 
2 91  ASN n 
2 92  ASN n 
2 93  VAL n 
2 94  GLU n 
2 95  ASP n 
2 96  TYR n 
2 97  PHE n 
2 98  LYS n 
2 99  GLU n 
2 100 GLY n 
2 101 LEU n 
2 102 GLU n 
2 103 LYS n 
2 104 THR n 
2 105 ILE n 
2 106 ALA n 
2 107 ALA n 
2 108 LYS n 
2 109 LYS n 
2 110 ALA n 
2 111 GLU n 
2 112 LEU n 
2 113 GLU n 
2 114 LYS n 
2 115 THR n 
2 116 GLU n 
2 117 ALA n 
2 118 ASP n 
2 119 LEU n 
2 120 LYS n 
2 121 LYS n 
2 122 ALA n 
2 123 VAL n 
2 124 ASN n 
2 125 GLU 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 ? ? ? human Homo          'LTF, LF' ? ?   ? ? ? ? 'Homo sapiens'             9606 ? ? ? ? ? ? ? ? 'Insect cells' ?      
?           ? ? ?                  ? ? Hi5         ? ? ? ? ? ? ? Virus   ? ? ? pAcGP67-A ? ? 
2 1 sample ? ? ? ?     Streptococcus pspA      ? Rx1 ? ? ? ? 'Streptococcus pneumoniae' 1313 ? ? ? ? ? ? ? ? 
'Escherichia coli BL21(DE3)' 469008 Escherichia ? ? 'Escherichia coli' ? ? 'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pET15b    ? ? 
# 
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 Q5EK51_HUMAN Q5EK51 1 
;GRRRRSVQWCAVSQPEATKCFQWQRNMRRVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAA
EVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRNAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVP
GADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPV
DKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLY
LGSGYFTAIQNLRKSEEEVAARRA
;
20  ? 
2 UNP Q8DRI0_STRR6 Q8DRI0 2 
;DAEEVAPQAKIAELENQVHRLEQELKEIDESESEDYAKEGFRAPLQSKLDAKKAKLSKLEELSDKIDELDAEIAKLEDQL
KAAEENNNVEDYFKEGLEKTIAAKKAELEKTEADLKKAVNE
;
199 ? 
# 
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 2PMS A 1 ? 344 ? Q5EK51 20  ? 363 ? 1   344 
2 1 2PMS B 1 ? 344 ? Q5EK51 20  ? 363 ? 1   344 
3 2 2PMS C 5 ? 125 ? Q8DRI0 199 ? 319 ? 168 288 
4 2 2PMS D 5 ? 125 ? Q8DRI0 199 ? 319 ? 168 288 
# 
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 2PMS THR A 123 ? UNP Q5EK51 ASN 142 CONFLICT         123 1  
2 2PMS THR B 123 ? UNP Q5EK51 ASN 142 CONFLICT         123 2  
3 2PMS GLY C 1   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 164 3  
3 2PMS SER C 2   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 165 4  
3 2PMS HIS C 3   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 166 5  
3 2PMS MET C 4   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 167 6  
4 2PMS GLY D 1   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 164 7  
4 2PMS SER D 2   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 165 8  
4 2PMS HIS D 3   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 166 9  
4 2PMS MET D 4   ? UNP Q8DRI0 ?   ?   'EXPRESSION TAG' 167 10 
# 
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 
CO3 non-polymer         . 'CARBONATE ION'        ? 'C O3 -2'        60.009  
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
FE  non-polymer         . 'FE (III) ION'         ? 'Fe 3'           55.845  
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
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 
SO4 non-polymer         . 'SULFATE ION'          ? 'O4 S -2'        96.063  
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 
ZN  non-polymer         . 'ZINC ION'             ? 'Zn 2'           65.409  
# 
_exptl.entry_id          2PMS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.77 
_exptl_crystal.density_percent_sol   67.37 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
'30% (v/v) PEG 400, 0.2 M Lithium Sulfate, 0.1 M Sodium Cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_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                   'ADSC QUANTUM 210' 
_diffrn_detector.pdbx_collection_date   2006-08-14 
_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                    'Si 111 CHANNEL' 
_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 17-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_wavelength             1.0 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     2PMS 
_reflns.observed_criterion_sigma_I   1 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             15.000 
_reflns.d_resolution_high            2.91 
_reflns.number_obs                   33481 
_reflns.number_all                   33745 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            0.098 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        7.000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.900 
_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_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.91 
_reflns_shell.d_res_low              3.00 
_reflns_shell.percent_possible_all   100.00 
_reflns_shell.Rmerge_I_obs           0.359 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    3.0 
_reflns_shell.pdbx_redundancy        2.90 
_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_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2PMS 
_refine.ls_number_reflns_obs                     30285 
_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                             15.00 
_refine.ls_d_res_high                            2.91 
_refine.ls_percent_reflns_obs                    95.23 
_refine.ls_R_factor_obs                          0.20541 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20309 
_refine.ls_R_factor_R_free                       0.24906 
_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                  1615 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.912 
_refine.correlation_coeff_Fo_to_Fc_free          0.869 
_refine.B_iso_mean                               31.893 
_refine.aniso_B[1][1]                            0.94 
_refine.aniso_B[2][2]                            0.94 
_refine.aniso_B[3][3]                            -1.41 
_refine.aniso_B[1][2]                            0.47 
_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                      'PDB entry 1H45' 
_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                       1.070 
_refine.pdbx_overall_ESU_R_Free                  0.360 
_refine.overall_SU_ML                            0.269 
_refine.overall_SU_B                             29.137 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6902 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.number_atoms_solvent             24 
_refine_hist.number_atoms_total               6996 
_refine_hist.d_res_high                       2.91 
_refine_hist.d_res_low                        15.00 
# 
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             0.009  0.022  ? 7114 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.167  1.981  ? 9602 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       4.990  5.000  ? 872  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       40.014 24.235 ? 340  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.282 15.000 ? 1248 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.864 15.000 ? 56   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.080  0.200  ? 1016 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.003  0.020  ? 5436 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.196  0.200  ? 3024 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.301  0.200  ? 4855 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.122  0.200  ? 183  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.111  0.200  ? 8    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.244  0.200  ? 77   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.137  0.200  ? 8    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined 0.096  0.200  ? 1    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.461  1.500  ? 4539 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.786  2.000  ? 7018 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.062  3.000  ? 2900 'X-RAY DIFFRACTION' ? 
r_scangle_it                 1.808  4.500  ? 2584 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 A 2581 0.13 0.50 'medium positional' 1 'X-RAY DIFFRACTION' 1 ? ? ? 
1 C 862  0.15 0.50 'medium positional' 2 'X-RAY DIFFRACTION' 2 ? ? ? 
1 A 2581 0.16 2.00 'medium thermal'    1 'X-RAY DIFFRACTION' 3 ? ? ? 
1 C 862  0.17 2.00 'medium thermal'    2 'X-RAY DIFFRACTION' 4 ? ? ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.906 
_refine_ls_shell.d_res_low                        2.979 
_refine_ls_shell.number_reflns_R_work             2033 
_refine_ls_shell.R_factor_R_work                  0.262 
_refine_ls_shell.percent_reflns_obs               89.87 
_refine_ls_shell.R_factor_R_free                  0.333 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             113 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 'A B' 
1 2 'C D' 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 A 4   A 333 1 4 A ARG 4 ? A ARG 333 ? 1 ? 
1 B 4   B 333 2 4 B ARG 4 ? B ARG 333 ? 1 ? 
1 C 164 C 288 1 4 C GLY 1 ? C GLU 125 ? 2 ? 
1 D 164 D 288 2 4 D GLY 1 ? D GLU 125 ? 2 ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
1 'A B' 
2 'C D' 
# 
_struct.entry_id                  2PMS 
_struct.title                     
'Crystal structure of the complex of human lactoferrin N-lobe and lactoferrin-binding domain of pneumococcal surface protein A' 
_struct.pdbx_descriptor           'Lactotransferrin (E.C.3.4.21.-), PNEUMOCOCCAL SURFACE PROTEIN A (PSPA)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2PMS 
_struct_keywords.pdbx_keywords   'METAL TRANSPORT, HYDROLASE' 
_struct_keywords.text            'lactoferrin, pneumococcal surface protein A, protein-protein complex, METAL TRANSPORT, HYDROLASE' 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
P N N 6 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 8 ? 
T N N 8 ? 
U N N 8 ? 
V N N 8 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
1 
;The biological assembly is a dimer containing one of each entities (lactoferrin and pspA). Asymmetric unit contains 2 copies of biological unit.
;
2 ? 
# 
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  SER A 13  ? VAL A 30  ? SER A 13  VAL A 30  1 ? 18 
HELX_P HELX_P2  2  SER A 42  ? GLU A 52  ? SER A 42  GLU A 52  1 ? 11 
HELX_P HELX_P3  3  ASP A 61  ? LEU A 70  ? ASP A 61  LEU A 70  1 ? 10 
HELX_P HELX_P4  4  TRP A 126 ? ARG A 134 ? TRP A 126 ARG A 134 1 ? 9  
HELX_P HELX_P5  5  PRO A 135 ? LEU A 137 ? PRO A 135 LEU A 137 5 ? 3  
HELX_P HELX_P6  6  PRO A 145 ? PHE A 154 ? PRO A 145 PHE A 154 1 ? 10 
HELX_P HELX_P7  7  PHE A 167 ? CYS A 171 ? PHE A 167 CYS A 171 5 ? 5  
HELX_P HELX_P8  8  THR A 177 ? LYS A 181 ? THR A 177 LYS A 181 5 ? 5  
HELX_P HELX_P9  9  PHE A 191 ? ASP A 202 ? PHE A 191 ASP A 202 1 ? 12 
HELX_P HELX_P10 10 SER A 213 ? LEU A 219 ? SER A 213 LEU A 219 1 ? 7  
HELX_P HELX_P11 11 ASP A 221 ? ASP A 226 ? ASP A 221 ASP A 226 1 ? 6  
HELX_P HELX_P12 12 ASP A 241 ? CYS A 246 ? ASP A 241 CYS A 246 5 ? 6  
HELX_P HELX_P13 13 LYS A 264 ? GLY A 280 ? LYS A 264 GLY A 280 1 ? 17 
HELX_P HELX_P14 14 ASP A 316 ? ARG A 333 ? ASP A 316 ARG A 333 1 ? 18 
HELX_P HELX_P15 15 SER B 13  ? VAL B 30  ? SER B 13  VAL B 30  1 ? 18 
HELX_P HELX_P16 16 SER B 42  ? GLU B 52  ? SER B 42  GLU B 52  1 ? 11 
HELX_P HELX_P17 17 ASP B 61  ? LEU B 70  ? ASP B 61  LEU B 70  1 ? 10 
HELX_P HELX_P18 18 GLN B 106 ? LEU B 110 ? GLN B 106 LEU B 110 5 ? 5  
HELX_P HELX_P19 19 TRP B 126 ? ARG B 134 ? TRP B 126 ARG B 134 1 ? 9  
HELX_P HELX_P20 20 PRO B 135 ? LEU B 137 ? PRO B 135 LEU B 137 5 ? 3  
HELX_P HELX_P21 21 PRO B 145 ? PHE B 154 ? PRO B 145 PHE B 154 1 ? 10 
HELX_P HELX_P22 22 PHE B 167 ? CYS B 171 ? PHE B 167 CYS B 171 5 ? 5  
HELX_P HELX_P23 23 THR B 177 ? LYS B 181 ? THR B 177 LYS B 181 5 ? 5  
HELX_P HELX_P24 24 PHE B 191 ? ASP B 202 ? PHE B 191 ASP B 202 1 ? 12 
HELX_P HELX_P25 25 SER B 213 ? LEU B 219 ? SER B 213 LEU B 219 1 ? 7  
HELX_P HELX_P26 26 ASP B 221 ? ASP B 226 ? ASP B 221 ASP B 226 1 ? 6  
HELX_P HELX_P27 27 LYS B 242 ? CYS B 246 ? LYS B 242 CYS B 246 5 ? 5  
HELX_P HELX_P28 28 LYS B 264 ? GLY B 280 ? LYS B 264 GLY B 280 1 ? 17 
HELX_P HELX_P29 29 ASP B 316 ? ARG B 333 ? ASP B 316 ARG B 333 1 ? 18 
HELX_P HELX_P30 30 MET C 4   ? ALA C 10  ? MET C 167 ALA C 173 1 ? 7  
HELX_P HELX_P31 31 ALA C 10  ? LEU C 29  ? ALA C 173 LEU C 192 1 ? 20 
HELX_P HELX_P32 32 ALA C 47  ? ALA C 86  ? ALA C 210 ALA C 249 1 ? 40 
HELX_P HELX_P33 33 GLU C 94  ? VAL C 123 ? GLU C 257 VAL C 286 1 ? 30 
HELX_P HELX_P34 34 ASP D 5   ? ALA D 10  ? ASP D 168 ALA D 173 1 ? 6  
HELX_P HELX_P35 35 ALA D 10  ? ILE D 32  ? ALA D 173 ILE D 195 1 ? 23 
HELX_P HELX_P36 36 PRO D 48  ? ALA D 86  ? PRO D 211 ALA D 249 1 ? 39 
HELX_P HELX_P37 37 GLU D 94  ? VAL D 123 ? GLU D 257 VAL D 286 1 ? 30 
# 
_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 10  SG  ? ? ? 1_555 A CYS 46  SG  ? ? A CYS 10  A CYS 46  1_555 ? ? ? ? ? ? ? 2.062 ? 
disulf2  disulf ? ? A CYS 20  SG  ? ? ? 1_555 A CYS 37  SG  ? ? A CYS 20  A CYS 37  1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf3  disulf ? ? A CYS 116 SG  ? ? ? 1_555 A CYS 199 SG  ? ? A CYS 116 A CYS 199 1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf4  disulf ? ? A CYS 158 SG  ? ? ? 1_555 A CYS 174 SG  ? ? A CYS 158 A CYS 174 1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf5  disulf ? ? A CYS 171 SG  ? ? ? 1_555 A CYS 182 SG  ? ? A CYS 171 A CYS 182 1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf6  disulf ? ? A CYS 232 SG  ? ? ? 1_555 A CYS 246 SG  ? ? A CYS 232 A CYS 246 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf7  disulf ? ? B CYS 10  SG  ? ? ? 1_555 B CYS 46  SG  ? ? B CYS 10  B CYS 46  1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf8  disulf ? ? B CYS 20  SG  ? ? ? 1_555 B CYS 37  SG  ? ? B CYS 20  B CYS 37  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf9  disulf ? ? B CYS 116 SG  ? ? ? 1_555 B CYS 199 SG  ? ? B CYS 116 B CYS 199 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf10 disulf ? ? B CYS 158 SG  ? ? ? 1_555 B CYS 174 SG  ? ? B CYS 158 B CYS 174 1_555 ? ? ? ? ? ? ? 2.074 ? 
disulf11 disulf ? ? B CYS 171 SG  ? ? ? 1_555 B CYS 182 SG  ? ? B CYS 171 B CYS 182 1_555 ? ? ? ? ? ? ? 2.073 ? 
disulf12 disulf ? ? B CYS 232 SG  ? ? ? 1_555 B CYS 246 SG  ? ? B CYS 232 B CYS 246 1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc1  metalc ? ? A ASP 61  OD1 ? ? ? 1_555 G FE  .   FE  ? ? A ASP 61  A FE  347 1_555 ? ? ? ? ? ? ? 1.916 ? 
metalc2  metalc ? ? A TYR 93  OH  ? ? ? 1_555 G FE  .   FE  ? ? A TYR 93  A FE  347 1_555 ? ? ? ? ? ? ? 2.136 ? 
covale1  covale ? ? A ASN 138 ND2 ? ? ? 1_555 E NAG .   C1  ? ? A ASN 138 A NAG 345 1_555 ? ? ? ? ? ? ? 1.461 ? 
metalc3  metalc ? ? A TYR 193 OH  ? ? ? 1_555 G FE  .   FE  ? ? A TYR 193 A FE  347 1_555 ? ? ? ? ? ? ? 1.879 ? 
metalc4  metalc ? ? A HIS 254 NE2 ? ? ? 1_555 G FE  .   FE  ? ? A HIS 254 A FE  347 1_555 ? ? ? ? ? ? ? 2.221 ? 
metalc5  metalc ? ? B ASP 61  OD1 ? ? ? 1_555 M FE  .   FE  ? ? B ASP 61  B FE  347 1_555 ? ? ? ? ? ? ? 1.929 ? 
metalc6  metalc ? ? B TYR 93  OH  ? ? ? 1_555 M FE  .   FE  ? ? B TYR 93  B FE  347 1_555 ? ? ? ? ? ? ? 2.145 ? 
covale2  covale ? ? B ASN 138 ND2 ? ? ? 1_555 K NAG .   C1  ? ? B ASN 138 B NAG 345 1_555 ? ? ? ? ? ? ? 1.458 ? 
metalc7  metalc ? ? B TYR 193 OH  ? ? ? 1_555 M FE  .   FE  ? ? B TYR 193 B FE  347 1_555 ? ? ? ? ? ? ? 1.830 ? 
metalc8  metalc ? ? B HIS 254 NE2 ? ? ? 1_555 M FE  .   FE  ? ? B HIS 254 B FE  347 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc9  metalc ? ? C HIS 3   NE2 ? ? ? 1_555 Q ZN  .   ZN  ? ? C HIS 166 C ZN  502 1_555 ? ? ? ? ? ? ? 2.045 ? 
metalc10 metalc ? ? C ASP 5   OD1 ? ? ? 1_555 Q ZN  .   ZN  ? ? C ASP 168 C ZN  502 1_555 ? ? ? ? ? ? ? 2.204 ? 
metalc11 metalc ? ? F CO3 .   O1  ? ? ? 1_555 G FE  .   FE  ? ? A CO3 346 A FE  347 1_555 ? ? ? ? ? ? ? 1.805 ? 
metalc12 metalc ? ? F CO3 .   O2  ? ? ? 1_555 G FE  .   FE  ? ? A CO3 346 A FE  347 1_555 ? ? ? ? ? ? ? 2.651 ? 
metalc13 metalc ? ? L CO3 .   O1  ? ? ? 1_555 M FE  .   FE  ? ? B CO3 346 B FE  347 1_555 ? ? ? ? ? ? ? 1.865 ? 
metalc14 metalc ? ? L CO3 .   O2  ? ? ? 1_555 M FE  .   FE  ? ? B CO3 346 B FE  347 1_555 ? ? ? ? ? ? ? 2.562 ? 
metalc15 metalc ? ? A HIS 247 NE2 ? ? ? 1_555 R ZN  .   ZN  ? ? A HIS 247 D ZN  501 1_555 ? ? ? ? ? ? ? 1.900 ? 
metalc16 metalc ? ? D HIS 3   NE2 ? ? ? 1_555 R ZN  .   ZN  ? ? D HIS 166 D ZN  501 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc17 metalc ? ? D ASP 5   OD1 ? ? ? 1_555 R ZN  .   ZN  ? ? D ASP 168 D ZN  501 1_555 ? ? ? ? ? ? ? 2.202 ? 
metalc18 metalc ? ? D ASP 5   OD2 ? ? ? 1_555 R ZN  .   ZN  ? ? D ASP 168 D ZN  501 1_555 ? ? ? ? ? ? ? 2.385 ? 
metalc19 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 C ASP 5   OD2 ? ? C ZN  502 C ASP 168 1_555 ? ? ? ? ? ? ? 2.482 ? 
metalc20 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 D GLU 99  OE1 ? ? C ZN  502 D GLU 262 3_554 ? ? ? ? ? ? ? 2.755 ? 
metalc21 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 D GLU 99  OE2 ? ? C ZN  502 D GLU 262 3_554 ? ? ? ? ? ? ? 1.914 ? 
metalc22 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 B HIS 247 NE2 ? ? C ZN  502 B HIS 247 1_554 ? ? ? ? ? ? ? 1.944 ? 
metalc23 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 C GLU 99  OE2 ? ? D ZN  501 C GLU 262 3_565 ? ? ? ? ? ? ? 2.057 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 71  A . ? ALA 71  A PRO 72  A ? PRO 72  A 1 1.01 
2 PRO 142 A . ? PRO 142 A PRO 143 A ? PRO 143 A 1 8.29 
3 ALA 71  B . ? ALA 71  B PRO 72  B ? PRO 72  B 1 1.75 
4 PRO 142 B . ? PRO 142 B PRO 143 B ? PRO 143 B 1 6.39 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 4 ? 
C ? 4 ? 
D ? 6 ? 
E ? 6 ? 
F ? 2 ? 
G ? 4 ? 
H ? 4 ? 
I ? 6 ? 
J ? 5 ? 
# 
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 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
D 5 6 ? anti-parallel 
E 1 2 ? parallel      
E 2 3 ? parallel      
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
E 5 6 ? anti-parallel 
F 1 2 ? parallel      
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? parallel      
I 2 3 ? parallel      
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
I 5 6 ? anti-parallel 
J 1 2 ? parallel      
J 2 3 ? parallel      
J 3 4 ? anti-parallel 
J 4 5 ? 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 VAL A 7   ? ALA A 11  ? VAL A 7   ALA A 11  
A 2 VAL A 35  ? LYS A 39  ? VAL A 35  LYS A 39  
B 1 VAL A 58  ? LEU A 60  ? VAL A 58  LEU A 60  
B 2 ALA A 255 ? ARG A 259 ? ALA A 255 ARG A 259 
B 3 LEU A 75  ? THR A 85  ? LEU A 75  THR A 85  
B 4 GLN A 88  ? ARG A 90  ? GLN A 88  ARG A 90  
C 1 VAL A 58  ? LEU A 60  ? VAL A 58  LEU A 60  
C 2 ALA A 255 ? ARG A 259 ? ALA A 255 ARG A 259 
C 3 LEU A 75  ? THR A 85  ? LEU A 75  THR A 85  
C 4 GLY A 307 ? ARG A 310 ? GLY A 307 ARG A 310 
D 1 ALA A 156 ? CYS A 158 ? ALA A 156 CYS A 158 
D 2 LYS A 114 ? HIS A 117 ? LYS A 114 HIS A 117 
D 3 VAL A 207 ? ARG A 211 ? VAL A 207 ARG A 211 
D 4 HIS A 92  ? LYS A 100 ? HIS A 92  LYS A 100 
D 5 TYR A 228 ? CYS A 232 ? TYR A 228 CYS A 232 
D 6 THR A 236 ? PRO A 239 ? THR A 236 PRO A 239 
E 1 ALA A 156 ? CYS A 158 ? ALA A 156 CYS A 158 
E 2 LYS A 114 ? HIS A 117 ? LYS A 114 HIS A 117 
E 3 VAL A 207 ? ARG A 211 ? VAL A 207 ARG A 211 
E 4 HIS A 92  ? LYS A 100 ? HIS A 92  LYS A 100 
E 5 ALA A 249 ? PRO A 252 ? ALA A 249 PRO A 252 
E 6 HIS D 3   ? MET D 4   ? HIS D 166 MET D 167 
F 1 VAL B 7   ? ALA B 11  ? VAL B 7   ALA B 11  
F 2 VAL B 35  ? LYS B 39  ? VAL B 35  LYS B 39  
G 1 VAL B 58  ? LEU B 60  ? VAL B 58  LEU B 60  
G 2 ALA B 255 ? ARG B 259 ? ALA B 255 ARG B 259 
G 3 LEU B 75  ? GLY B 84  ? LEU B 75  GLY B 84  
G 4 PRO B 89  ? ARG B 90  ? PRO B 89  ARG B 90  
H 1 VAL B 58  ? LEU B 60  ? VAL B 58  LEU B 60  
H 2 ALA B 255 ? ARG B 259 ? ALA B 255 ARG B 259 
H 3 LEU B 75  ? GLY B 84  ? LEU B 75  GLY B 84  
H 4 GLY B 307 ? ARG B 310 ? GLY B 307 ARG B 310 
I 1 ALA B 156 ? CYS B 158 ? ALA B 156 CYS B 158 
I 2 LYS B 114 ? HIS B 117 ? LYS B 114 HIS B 117 
I 3 VAL B 207 ? ARG B 211 ? VAL B 207 ARG B 211 
I 4 HIS B 92  ? LYS B 100 ? HIS B 92  LYS B 100 
I 5 TYR B 228 ? LEU B 231 ? TYR B 228 LEU B 231 
I 6 ARG B 237 ? PRO B 239 ? ARG B 237 PRO B 239 
J 1 ALA B 156 ? CYS B 158 ? ALA B 156 CYS B 158 
J 2 LYS B 114 ? HIS B 117 ? LYS B 114 HIS B 117 
J 3 VAL B 207 ? ARG B 211 ? VAL B 207 ARG B 211 
J 4 HIS B 92  ? LYS B 100 ? HIS B 92  LYS B 100 
J 5 ALA B 249 ? PRO B 252 ? ALA B 249 PRO B 252 
# 
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 N ALA A 11  ? N ALA A 11  O ILE A 38  ? O ILE A 38  
B 1 2 N VAL A 58  ? N VAL A 58  O VAL A 257 ? O VAL A 257 
B 2 3 O ALA A 258 ? O ALA A 258 N ARG A 76  ? N ARG A 76  
B 3 4 N TYR A 83  ? N TYR A 83  O ARG A 90  ? O ARG A 90  
C 1 2 N VAL A 58  ? N VAL A 58  O VAL A 257 ? O VAL A 257 
C 2 3 O ALA A 258 ? O ALA A 258 N ARG A 76  ? N ARG A 76  
C 3 4 N ALA A 80  ? N ALA A 80  O SER A 309 ? O SER A 309 
D 1 2 O ALA A 156 ? O ALA A 156 N SER A 115 ? N SER A 115 
D 2 3 N CYS A 116 ? N CYS A 116 O VAL A 207 ? O VAL A 207 
D 3 4 O ALA A 208 ? O ALA A 208 N VAL A 98  ? N VAL A 98  
D 4 5 N VAL A 99  ? N VAL A 99  O GLU A 229 ? O GLU A 229 
D 5 6 N CYS A 232 ? N CYS A 232 O THR A 236 ? O THR A 236 
E 1 2 O ALA A 156 ? O ALA A 156 N SER A 115 ? N SER A 115 
E 2 3 N CYS A 116 ? N CYS A 116 O VAL A 207 ? O VAL A 207 
E 3 4 O ALA A 208 ? O ALA A 208 N VAL A 98  ? N VAL A 98  
E 4 5 N TYR A 93  ? N TYR A 93  O VAL A 251 ? O VAL A 251 
E 5 6 N ARG A 250 ? N ARG A 250 O HIS D 3   ? O HIS D 166 
F 1 2 N TRP B 9   ? N TRP B 9   O SER B 36  ? O SER B 36  
G 1 2 N LEU B 60  ? N LEU B 60  O ALA B 255 ? O ALA B 255 
G 2 3 O VAL B 256 ? O VAL B 256 N VAL B 78  ? N VAL B 78  
G 3 4 N TYR B 83  ? N TYR B 83  O ARG B 90  ? O ARG B 90  
H 1 2 N LEU B 60  ? N LEU B 60  O ALA B 255 ? O ALA B 255 
H 2 3 O VAL B 256 ? O VAL B 256 N VAL B 78  ? N VAL B 78  
H 3 4 N ALA B 80  ? N ALA B 80  O SER B 309 ? O SER B 309 
I 1 2 O CYS B 158 ? O CYS B 158 N HIS B 117 ? N HIS B 117 
I 2 3 N CYS B 116 ? N CYS B 116 O PHE B 209 ? O PHE B 209 
I 3 4 O ILE B 210 ? O ILE B 210 N VAL B 96  ? N VAL B 96  
I 4 5 N VAL B 99  ? N VAL B 99  O GLU B 229 ? O GLU B 229 
I 5 6 N LEU B 230 ? N LEU B 230 O LYS B 238 ? O LYS B 238 
J 1 2 O CYS B 158 ? O CYS B 158 N HIS B 117 ? N HIS B 117 
J 2 3 N CYS B 116 ? N CYS B 116 O PHE B 209 ? O PHE B 209 
J 3 4 O ILE B 210 ? O ILE B 210 N VAL B 96  ? N VAL B 96  
J 4 5 N TYR B 93  ? N TYR B 93  O VAL B 251 ? O VAL B 251 
# 
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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 345' 
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 345' 
AC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE CO3 A 346' 
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE FE A 347'  
AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 348' 
AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 349' 
AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 350' 
AC8 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE CO3 B 346' 
AC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE FE B 347'  
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 B 348' 
BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 349' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 350' 
BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 501'  
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 502'  
# 
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 3 GLN A 111 ? GLN A 111 . ? 1_555 ? 
2  AC1 3 LEU A 137 ? LEU A 137 . ? 1_555 ? 
3  AC1 3 ASN A 138 ? ASN A 138 . ? 1_555 ? 
4  AC2 3 GLN B 111 ? GLN B 111 . ? 1_555 ? 
5  AC2 3 LEU B 137 ? LEU B 137 . ? 1_555 ? 
6  AC2 3 ASN B 138 ? ASN B 138 . ? 1_555 ? 
7  AC3 9 ASP A 61  ? ASP A 61  . ? 1_555 ? 
8  AC3 9 TYR A 93  ? TYR A 93  . ? 1_555 ? 
9  AC3 9 THR A 118 ? THR A 118 . ? 1_555 ? 
10 AC3 9 ARG A 122 ? ARG A 122 . ? 1_555 ? 
11 AC3 9 THR A 123 ? THR A 123 . ? 1_555 ? 
12 AC3 9 ALA A 124 ? ALA A 124 . ? 1_555 ? 
13 AC3 9 GLY A 125 ? GLY A 125 . ? 1_555 ? 
14 AC3 9 TYR A 193 ? TYR A 193 . ? 1_555 ? 
15 AC3 9 FE  G .   ? FE  A 347 . ? 1_555 ? 
16 AC4 5 ASP A 61  ? ASP A 61  . ? 1_555 ? 
17 AC4 5 TYR A 93  ? TYR A 93  . ? 1_555 ? 
18 AC4 5 TYR A 193 ? TYR A 193 . ? 1_555 ? 
19 AC4 5 HIS A 254 ? HIS A 254 . ? 1_555 ? 
20 AC4 5 CO3 F .   ? CO3 A 346 . ? 1_555 ? 
21 AC5 6 GLN A 22  ? GLN A 22  . ? 1_555 ? 
22 AC5 6 ARG A 25  ? ARG A 25  . ? 1_555 ? 
23 AC5 6 ASN A 26  ? ASN A 26  . ? 1_555 ? 
24 AC5 6 HOH S .   ? HOH A 417 . ? 1_555 ? 
25 AC5 6 ARG B 134 ? ARG B 134 . ? 1_554 ? 
26 AC5 6 ASN B 331 ? ASN B 331 . ? 1_554 ? 
27 AC6 3 ARG A 90  ? ARG A 90  . ? 1_555 ? 
28 AC6 3 THR A 91  ? THR A 91  . ? 1_555 ? 
29 AC6 3 HIS A 92  ? HIS A 92  . ? 1_555 ? 
30 AC7 5 ARG A 29  ? ARG A 29  . ? 1_555 ? 
31 AC7 5 PHE A 279 ? PHE A 279 . ? 1_555 ? 
32 AC7 5 SER A 284 ? SER A 284 . ? 1_555 ? 
33 AC7 5 PRO A 285 ? PRO A 285 . ? 1_555 ? 
34 AC7 5 LYS A 286 ? LYS A 286 . ? 1_555 ? 
35 AC8 9 ASP B 61  ? ASP B 61  . ? 1_555 ? 
36 AC8 9 TYR B 93  ? TYR B 93  . ? 1_555 ? 
37 AC8 9 THR B 118 ? THR B 118 . ? 1_555 ? 
38 AC8 9 ARG B 122 ? ARG B 122 . ? 1_555 ? 
39 AC8 9 THR B 123 ? THR B 123 . ? 1_555 ? 
40 AC8 9 ALA B 124 ? ALA B 124 . ? 1_555 ? 
41 AC8 9 GLY B 125 ? GLY B 125 . ? 1_555 ? 
42 AC8 9 TYR B 193 ? TYR B 193 . ? 1_555 ? 
43 AC8 9 FE  M .   ? FE  B 347 . ? 1_555 ? 
44 AC9 5 ASP B 61  ? ASP B 61  . ? 1_555 ? 
45 AC9 5 TYR B 93  ? TYR B 93  . ? 1_555 ? 
46 AC9 5 TYR B 193 ? TYR B 193 . ? 1_555 ? 
47 AC9 5 HIS B 254 ? HIS B 254 . ? 1_555 ? 
48 AC9 5 CO3 L .   ? CO3 B 346 . ? 1_555 ? 
49 BC1 5 ARG A 134 ? ARG A 134 . ? 1_555 ? 
50 BC1 5 ASN A 331 ? ASN A 331 . ? 1_555 ? 
51 BC1 5 GLN B 22  ? GLN B 22  . ? 1_555 ? 
52 BC1 5 ARG B 25  ? ARG B 25  . ? 1_555 ? 
53 BC1 5 ASN B 26  ? ASN B 26  . ? 1_555 ? 
54 BC2 3 ARG B 90  ? ARG B 90  . ? 1_555 ? 
55 BC2 3 THR B 91  ? THR B 91  . ? 1_555 ? 
56 BC2 3 HIS B 92  ? HIS B 92  . ? 1_555 ? 
57 BC3 4 ARG B 29  ? ARG B 29  . ? 1_555 ? 
58 BC3 4 PHE B 279 ? PHE B 279 . ? 1_555 ? 
59 BC3 4 SER B 284 ? SER B 284 . ? 1_555 ? 
60 BC3 4 LYS B 286 ? LYS B 286 . ? 1_555 ? 
61 BC4 4 HIS A 247 ? HIS A 247 . ? 1_555 ? 
62 BC4 4 GLU C 99  ? GLU C 262 . ? 3_565 ? 
63 BC4 4 HIS D 3   ? HIS D 166 . ? 1_555 ? 
64 BC4 4 ASP D 5   ? ASP D 168 . ? 1_555 ? 
65 BC5 4 HIS B 247 ? HIS B 247 . ? 1_554 ? 
66 BC5 4 HIS C 3   ? HIS C 166 . ? 1_555 ? 
67 BC5 4 ASP C 5   ? ASP C 168 . ? 1_555 ? 
68 BC5 4 GLU D 99  ? GLU D 262 . ? 3_554 ? 
# 
_atom_sites.entry_id                    2PMS 
_atom_sites.fract_transf_matrix[1][1]   0.007682 
_atom_sites.fract_transf_matrix[1][2]   0.004435 
_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]   0.008870 
_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]   0.012376 
_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  
FE 
N  
O  
S  
ZN 
# 
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   . ARG A 1 3   ? 27.862  41.478 37.252  1.00 36.48 ? 3   ARG A N   1 
ATOM   2    C  CA  . ARG A 1 3   ? 26.420  41.871 37.121  1.00 36.64 ? 3   ARG A CA  1 
ATOM   3    C  C   . ARG A 1 3   ? 26.241  43.394 37.300  1.00 36.14 ? 3   ARG A C   1 
ATOM   4    O  O   . ARG A 1 3   ? 26.816  43.990 38.215  1.00 36.19 ? 3   ARG A O   1 
ATOM   5    C  CB  . ARG A 1 3   ? 25.572  41.092 38.144  1.00 37.01 ? 3   ARG A CB  1 
ATOM   6    C  CG  . ARG A 1 3   ? 24.460  40.201 37.548  1.00 37.71 ? 3   ARG A CG  1 
ATOM   7    C  CD  . ARG A 1 3   ? 23.059  40.752 37.802  1.00 39.78 ? 3   ARG A CD  1 
ATOM   8    N  NE  . ARG A 1 3   ? 22.637  40.653 39.207  1.00 41.70 ? 3   ARG A NE  1 
ATOM   9    C  CZ  . ARG A 1 3   ? 21.604  41.309 39.751  1.00 42.39 ? 3   ARG A CZ  1 
ATOM   10   N  NH1 . ARG A 1 3   ? 20.848  42.131 39.023  1.00 42.47 ? 3   ARG A NH1 1 
ATOM   11   N  NH2 . ARG A 1 3   ? 21.323  41.149 41.039  1.00 42.01 ? 3   ARG A NH2 1 
ATOM   12   N  N   . ARG A 1 4   ? 25.442  44.011 36.430  1.00 35.50 ? 4   ARG A N   1 
ATOM   13   C  CA  . ARG A 1 4   ? 25.264  45.472 36.421  1.00 34.81 ? 4   ARG A CA  1 
ATOM   14   C  C   . ARG A 1 4   ? 24.592  46.040 37.680  1.00 34.17 ? 4   ARG A C   1 
ATOM   15   O  O   . ARG A 1 4   ? 23.829  45.346 38.360  1.00 34.03 ? 4   ARG A O   1 
ATOM   16   C  CB  . ARG A 1 4   ? 24.537  45.940 35.144  1.00 34.92 ? 4   ARG A CB  1 
ATOM   17   C  CG  . ARG A 1 4   ? 23.312  45.113 34.739  1.00 35.22 ? 4   ARG A CG  1 
ATOM   18   C  CD  . ARG A 1 4   ? 22.390  45.862 33.763  1.00 35.22 ? 4   ARG A CD  1 
ATOM   19   N  NE  . ARG A 1 4   ? 22.788  45.760 32.352  1.00 35.88 ? 4   ARG A NE  1 
ATOM   20   C  CZ  . ARG A 1 4   ? 22.466  44.753 31.536  1.00 35.52 ? 4   ARG A CZ  1 
ATOM   21   N  NH1 . ARG A 1 4   ? 21.762  43.724 31.977  1.00 36.00 ? 4   ARG A NH1 1 
ATOM   22   N  NH2 . ARG A 1 4   ? 22.868  44.756 30.274  1.00 35.18 ? 4   ARG A NH2 1 
ATOM   23   N  N   . ARG A 1 5   ? 24.890  47.309 37.970  1.00 33.50 ? 5   ARG A N   1 
ATOM   24   C  CA  . ARG A 1 5   ? 24.389  48.008 39.161  1.00 33.06 ? 5   ARG A CA  1 
ATOM   25   C  C   . ARG A 1 5   ? 22.955  48.560 39.053  1.00 32.16 ? 5   ARG A C   1 
ATOM   26   O  O   . ARG A 1 5   ? 22.377  48.934 40.074  1.00 32.52 ? 5   ARG A O   1 
ATOM   27   C  CB  . ARG A 1 5   ? 25.345  49.136 39.564  1.00 33.12 ? 5   ARG A CB  1 
ATOM   28   C  CG  . ARG A 1 5   ? 26.721  48.684 40.069  1.00 33.94 ? 5   ARG A CG  1 
ATOM   29   C  CD  . ARG A 1 5   ? 27.730  49.849 40.083  1.00 34.40 ? 5   ARG A CD  1 
ATOM   30   N  NE  . ARG A 1 5   ? 27.952  50.410 38.742  1.00 37.85 ? 5   ARG A NE  1 
ATOM   31   C  CZ  . ARG A 1 5   ? 28.764  51.433 38.459  1.00 38.79 ? 5   ARG A CZ  1 
ATOM   32   N  NH1 . ARG A 1 5   ? 29.453  52.033 39.421  1.00 39.66 ? 5   ARG A NH1 1 
ATOM   33   N  NH2 . ARG A 1 5   ? 28.890  51.863 37.205  1.00 38.61 ? 5   ARG A NH2 1 
ATOM   34   N  N   . SER A 1 6   ? 22.396  48.600 37.836  1.00 31.05 ? 6   SER A N   1 
ATOM   35   C  CA  . SER A 1 6   ? 21.019  49.067 37.547  1.00 29.66 ? 6   SER A CA  1 
ATOM   36   C  C   . SER A 1 6   ? 19.923  48.036 37.906  1.00 28.71 ? 6   SER A C   1 
ATOM   37   O  O   . SER A 1 6   ? 20.234  46.941 38.383  1.00 28.37 ? 6   SER A O   1 
ATOM   38   C  CB  . SER A 1 6   ? 20.910  49.444 36.066  1.00 29.84 ? 6   SER A CB  1 
ATOM   39   O  OG  . SER A 1 6   ? 20.747  48.295 35.235  1.00 30.42 ? 6   SER A OG  1 
ATOM   40   N  N   . VAL A 1 7   ? 18.652  48.377 37.667  1.00 27.56 ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 17.532  47.495 38.049  1.00 26.84 ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 17.203  46.441 36.994  1.00 26.51 ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 16.894  46.777 35.854  1.00 27.07 ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 16.238  48.273 38.408  1.00 26.77 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 15.099  47.305 38.714  1.00 26.35 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 16.464  49.169 39.600  1.00 26.45 ? 7   VAL A CG2 1 
ATOM   47   N  N   . GLN A 1 8   ? 17.246  45.169 37.389  1.00 25.68 ? 8   GLN A N   1 
ATOM   48   C  CA  . GLN A 1 8   ? 17.026  44.062 36.467  1.00 24.71 ? 8   GLN A CA  1 
ATOM   49   C  C   . GLN A 1 8   ? 15.712  43.328 36.722  1.00 24.16 ? 8   GLN A C   1 
ATOM   50   O  O   . GLN A 1 8   ? 15.507  42.726 37.781  1.00 23.71 ? 8   GLN A O   1 
ATOM   51   C  CB  . GLN A 1 8   ? 18.186  43.091 36.548  1.00 24.97 ? 8   GLN A CB  1 
ATOM   52   C  CG  . GLN A 1 8   ? 19.491  43.637 36.057  1.00 25.38 ? 8   GLN A CG  1 
ATOM   53   C  CD  . GLN A 1 8   ? 20.366  42.537 35.495  1.00 27.41 ? 8   GLN A CD  1 
ATOM   54   O  OE1 . GLN A 1 8   ? 20.782  41.633 36.217  1.00 28.16 ? 8   GLN A OE1 1 
ATOM   55   N  NE2 . GLN A 1 8   ? 20.632  42.595 34.194  1.00 27.53 ? 8   GLN A NE2 1 
ATOM   56   N  N   . TRP A 1 9   ? 14.833  43.374 35.725  1.00 23.78 ? 9   TRP A N   1 
ATOM   57   C  CA  . TRP A 1 9   ? 13.462  42.886 35.852  1.00 23.22 ? 9   TRP A CA  1 
ATOM   58   C  C   . TRP A 1 9   ? 13.307  41.448 35.385  1.00 23.56 ? 9   TRP A C   1 
ATOM   59   O  O   . TRP A 1 9   ? 13.979  41.008 34.459  1.00 23.70 ? 9   TRP A O   1 
ATOM   60   C  CB  . TRP A 1 9   ? 12.503  43.777 35.073  1.00 22.20 ? 9   TRP A CB  1 
ATOM   61   C  CG  . TRP A 1 9   ? 11.162  43.739 35.665  1.00 22.03 ? 9   TRP A CG  1 
ATOM   62   C  CD1 . TRP A 1 9   ? 10.176  42.817 35.427  1.00 21.26 ? 9   TRP A CD1 1 
ATOM   63   C  CD2 . TRP A 1 9   ? 10.641  44.640 36.643  1.00 22.03 ? 9   TRP A CD2 1 
ATOM   64   N  NE1 . TRP A 1 9   ? 9.076   43.093 36.201  1.00 21.09 ? 9   TRP A NE1 1 
ATOM   65   C  CE2 . TRP A 1 9   ? 9.332   44.210 36.952  1.00 21.60 ? 9   TRP A CE2 1 
ATOM   66   C  CE3 . TRP A 1 9   ? 11.152  45.774 37.287  1.00 20.84 ? 9   TRP A CE3 1 
ATOM   67   C  CZ2 . TRP A 1 9   ? 8.531   44.878 37.870  1.00 21.92 ? 9   TRP A CZ2 1 
ATOM   68   C  CZ3 . TRP A 1 9   ? 10.365  46.423 38.204  1.00 20.59 ? 9   TRP A CZ3 1 
ATOM   69   C  CH2 . TRP A 1 9   ? 9.069   45.981 38.487  1.00 21.53 ? 9   TRP A CH2 1 
ATOM   70   N  N   . CYS A 1 10  ? 12.395  40.723 36.018  1.00 24.30 ? 10  CYS A N   1 
ATOM   71   C  CA  . CYS A 1 10  ? 12.198  39.320 35.706  1.00 24.40 ? 10  CYS A CA  1 
ATOM   72   C  C   . CYS A 1 10  ? 10.973  39.070 34.824  1.00 24.48 ? 10  CYS A C   1 
ATOM   73   O  O   . CYS A 1 10  ? 9.845   39.385 35.213  1.00 24.78 ? 10  CYS A O   1 
ATOM   74   C  CB  . CYS A 1 10  ? 12.113  38.516 36.994  1.00 24.37 ? 10  CYS A CB  1 
ATOM   75   S  SG  . CYS A 1 10  ? 12.689  36.828 36.789  1.00 25.94 ? 10  CYS A SG  1 
ATOM   76   N  N   . ALA A 1 11  ? 11.199  38.509 33.634  1.00 24.39 ? 11  ALA A N   1 
ATOM   77   C  CA  . ALA A 1 11  ? 10.103  38.146 32.725  1.00 24.40 ? 11  ALA A CA  1 
ATOM   78   C  C   . ALA A 1 11  ? 9.813   36.640 32.737  1.00 24.48 ? 11  ALA A C   1 
ATOM   79   O  O   . ALA A 1 11  ? 10.727  35.822 32.607  1.00 24.70 ? 11  ALA A O   1 
ATOM   80   C  CB  . ALA A 1 11  ? 10.397  38.626 31.315  1.00 24.15 ? 11  ALA A CB  1 
ATOM   81   N  N   . VAL A 1 12  ? 8.544   36.274 32.883  1.00 24.38 ? 12  VAL A N   1 
ATOM   82   C  CA  . VAL A 1 12  ? 8.184   34.863 32.997  1.00 24.51 ? 12  VAL A CA  1 
ATOM   83   C  C   . VAL A 1 12  ? 7.840   34.176 31.670  1.00 24.79 ? 12  VAL A C   1 
ATOM   84   O  O   . VAL A 1 12  ? 7.419   33.022 31.678  1.00 25.09 ? 12  VAL A O   1 
ATOM   85   C  CB  . VAL A 1 12  ? 7.042   34.605 34.049  1.00 24.68 ? 12  VAL A CB  1 
ATOM   86   C  CG1 . VAL A 1 12  ? 7.456   35.082 35.450  1.00 24.50 ? 12  VAL A CG1 1 
ATOM   87   C  CG2 . VAL A 1 12  ? 5.701   35.231 33.617  1.00 24.40 ? 12  VAL A CG2 1 
ATOM   88   N  N   . SER A 1 13  ? 8.029   34.866 30.544  1.00 25.01 ? 13  SER A N   1 
ATOM   89   C  CA  . SER A 1 13  ? 7.696   34.319 29.218  1.00 25.16 ? 13  SER A CA  1 
ATOM   90   C  C   . SER A 1 13  ? 8.315   35.154 28.110  1.00 25.61 ? 13  SER A C   1 
ATOM   91   O  O   . SER A 1 13  ? 8.700   36.299 28.338  1.00 25.88 ? 13  SER A O   1 
ATOM   92   C  CB  . SER A 1 13  ? 6.180   34.296 29.007  1.00 25.37 ? 13  SER A CB  1 
ATOM   93   O  OG  . SER A 1 13  ? 5.669   35.591 28.703  1.00 24.61 ? 13  SER A OG  1 
ATOM   94   N  N   . GLN A 1 14  ? 8.386   34.595 26.904  1.00 25.96 ? 14  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 14  ? 8.949   35.319 25.768  1.00 26.19 ? 14  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 14  ? 8.218   36.657 25.487  1.00 26.06 ? 14  GLN A C   1 
ATOM   97   O  O   . GLN A 1 14  ? 8.870   37.705 25.370  1.00 26.04 ? 14  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 14  ? 9.029   34.412 24.532  1.00 26.47 ? 14  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 14  ? 9.128   35.124 23.174  1.00 28.07 ? 14  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 14  ? 10.418  35.923 22.975  1.00 31.03 ? 14  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 14  ? 11.327  35.924 23.821  1.00 32.40 ? 14  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 14  ? 10.500  36.614 21.841  1.00 32.03 ? 14  GLN A NE2 1 
ATOM   103  N  N   . PRO A 1 15  ? 6.870   36.632 25.378  1.00 25.81 ? 15  PRO A N   1 
ATOM   104  C  CA  . PRO A 1 15  ? 6.140   37.889 25.199  1.00 25.39 ? 15  PRO A CA  1 
ATOM   105  C  C   . PRO A 1 15  ? 6.417   38.948 26.266  1.00 24.92 ? 15  PRO A C   1 
ATOM   106  O  O   . PRO A 1 15  ? 6.442   40.138 25.944  1.00 25.18 ? 15  PRO A O   1 
ATOM   107  C  CB  . PRO A 1 15  ? 4.675   37.442 25.246  1.00 25.30 ? 15  PRO A CB  1 
ATOM   108  C  CG  . PRO A 1 15  ? 4.712   36.072 24.713  1.00 25.59 ? 15  PRO A CG  1 
ATOM   109  C  CD  . PRO A 1 15  ? 5.944   35.484 25.345  1.00 25.87 ? 15  PRO A CD  1 
ATOM   110  N  N   . GLU A 1 16  ? 6.610   38.524 27.514  1.00 24.18 ? 16  GLU A N   1 
ATOM   111  C  CA  . GLU A 1 16  ? 6.942   39.450 28.590  1.00 23.49 ? 16  GLU A CA  1 
ATOM   112  C  C   . GLU A 1 16  ? 8.310   40.047 28.333  1.00 22.69 ? 16  GLU A C   1 
ATOM   113  O  O   . GLU A 1 16  ? 8.487   41.252 28.461  1.00 23.09 ? 16  GLU A O   1 
ATOM   114  C  CB  . GLU A 1 16  ? 6.895   38.785 29.976  1.00 23.49 ? 16  GLU A CB  1 
ATOM   115  C  CG  . GLU A 1 16  ? 5.543   38.867 30.687  1.00 23.86 ? 16  GLU A CG  1 
ATOM   116  C  CD  . GLU A 1 16  ? 5.627   38.806 32.226  1.00 24.70 ? 16  GLU A CD  1 
ATOM   117  O  OE1 . GLU A 1 16  ? 6.737   38.705 32.806  1.00 27.01 ? 16  GLU A OE1 1 
ATOM   118  O  OE2 . GLU A 1 16  ? 4.561   38.862 32.874  1.00 26.35 ? 16  GLU A OE2 1 
ATOM   119  N  N   . ALA A 1 17  ? 9.273   39.220 27.947  1.00 21.67 ? 17  ALA A N   1 
ATOM   120  C  CA  . ALA A 1 17  ? 10.607  39.729 27.649  1.00 21.02 ? 17  ALA A CA  1 
ATOM   121  C  C   . ALA A 1 17  ? 10.604  40.817 26.564  1.00 20.79 ? 17  ALA A C   1 
ATOM   122  O  O   . ALA A 1 17  ? 11.377  41.763 26.644  1.00 20.92 ? 17  ALA A O   1 
ATOM   123  C  CB  . ALA A 1 17  ? 11.532  38.611 27.276  1.00 20.79 ? 17  ALA A CB  1 
ATOM   124  N  N   . THR A 1 18  ? 9.726   40.683 25.569  1.00 20.62 ? 18  THR A N   1 
ATOM   125  C  CA  . THR A 1 18  ? 9.645   41.621 24.448  1.00 20.07 ? 18  THR A CA  1 
ATOM   126  C  C   . THR A 1 18  ? 9.152   42.981 24.906  1.00 20.23 ? 18  THR A C   1 
ATOM   127  O  O   . THR A 1 18  ? 9.636   44.010 24.421  1.00 20.34 ? 18  THR A O   1 
ATOM   128  C  CB  . THR A 1 18  ? 8.726   41.089 23.324  1.00 19.91 ? 18  THR A CB  1 
ATOM   129  O  OG1 . THR A 1 18  ? 9.276   39.876 22.801  1.00 20.41 ? 18  THR A OG1 1 
ATOM   130  C  CG2 . THR A 1 18  ? 8.579   42.100 22.192  1.00 18.75 ? 18  THR A CG2 1 
ATOM   131  N  N   . LYS A 1 19  ? 8.193   42.983 25.833  1.00 20.15 ? 19  LYS A N   1 
ATOM   132  C  CA  . LYS A 1 19  ? 7.655   44.229 26.360  1.00 20.50 ? 19  LYS A CA  1 
ATOM   133  C  C   . LYS A 1 19  ? 8.721   44.888 27.205  1.00 20.84 ? 19  LYS A C   1 
ATOM   134  O  O   . LYS A 1 19  ? 8.905   46.101 27.190  1.00 21.06 ? 19  LYS A O   1 
ATOM   135  C  CB  . LYS A 1 19  ? 6.410   43.987 27.212  1.00 20.26 ? 19  LYS A CB  1 
ATOM   136  C  CG  . LYS A 1 19  ? 5.959   45.232 27.964  1.00 19.59 ? 19  LYS A CG  1 
ATOM   137  C  CD  . LYS A 1 19  ? 4.550   45.106 28.451  1.00 19.31 ? 19  LYS A CD  1 
ATOM   138  C  CE  . LYS A 1 19  ? 4.274   46.133 29.518  1.00 18.80 ? 19  LYS A CE  1 
ATOM   139  N  NZ  . LYS A 1 19  ? 2.830   46.141 29.855  1.00 19.26 ? 19  LYS A NZ  1 
ATOM   140  N  N   . CYS A 1 20  ? 9.425   44.049 27.939  1.00 21.52 ? 20  CYS A N   1 
ATOM   141  C  CA  . CYS A 1 20  ? 10.436  44.486 28.846  1.00 21.24 ? 20  CYS A CA  1 
ATOM   142  C  C   . CYS A 1 20  ? 11.627  45.074 28.077  1.00 20.65 ? 20  CYS A C   1 
ATOM   143  O  O   . CYS A 1 20  ? 12.214  46.073 28.497  1.00 20.20 ? 20  CYS A O   1 
ATOM   144  C  CB  . CYS A 1 20  ? 10.815  43.302 29.719  1.00 21.85 ? 20  CYS A CB  1 
ATOM   145  S  SG  . CYS A 1 20  ? 11.835  43.728 31.103  1.00 23.94 ? 20  CYS A SG  1 
ATOM   146  N  N   . PHE A 1 21  ? 11.951  44.475 26.933  1.00 20.27 ? 21  PHE A N   1 
ATOM   147  C  CA  . PHE A 1 21  ? 12.940  45.050 26.009  1.00 19.89 ? 21  PHE A CA  1 
ATOM   148  C  C   . PHE A 1 21  ? 12.527  46.437 25.538  1.00 19.89 ? 21  PHE A C   1 
ATOM   149  O  O   . PHE A 1 21  ? 13.360  47.351 25.448  1.00 20.09 ? 21  PHE A O   1 
ATOM   150  C  CB  . PHE A 1 21  ? 13.165  44.156 24.790  1.00 19.32 ? 21  PHE A CB  1 
ATOM   151  C  CG  . PHE A 1 21  ? 13.918  42.892 25.089  1.00 18.79 ? 21  PHE A CG  1 
ATOM   152  C  CD1 . PHE A 1 21  ? 14.857  42.843 26.109  1.00 18.52 ? 21  PHE A CD1 1 
ATOM   153  C  CD2 . PHE A 1 21  ? 13.702  41.751 24.327  1.00 18.71 ? 21  PHE A CD2 1 
ATOM   154  C  CE1 . PHE A 1 21  ? 15.554  41.668 26.382  1.00 18.41 ? 21  PHE A CE1 1 
ATOM   155  C  CE2 . PHE A 1 21  ? 14.400  40.574 24.587  1.00 18.80 ? 21  PHE A CE2 1 
ATOM   156  C  CZ  . PHE A 1 21  ? 15.326  40.534 25.618  1.00 18.52 ? 21  PHE A CZ  1 
ATOM   157  N  N   . GLN A 1 22  ? 11.236  46.585 25.239  1.00 19.63 ? 22  GLN A N   1 
ATOM   158  C  CA  . GLN A 1 22  ? 10.674  47.860 24.793  1.00 19.04 ? 22  GLN A CA  1 
ATOM   159  C  C   . GLN A 1 22  ? 10.719  48.891 25.908  1.00 18.59 ? 22  GLN A C   1 
ATOM   160  O  O   . GLN A 1 22  ? 10.983  50.068 25.664  1.00 18.52 ? 22  GLN A O   1 
ATOM   161  C  CB  . GLN A 1 22  ? 9.241   47.665 24.322  1.00 18.99 ? 22  GLN A CB  1 
ATOM   162  C  CG  . GLN A 1 22  ? 8.618   48.907 23.741  1.00 19.60 ? 22  GLN A CG  1 
ATOM   163  C  CD  . GLN A 1 22  ? 7.376   48.608 22.926  1.00 20.39 ? 22  GLN A CD  1 
ATOM   164  O  OE1 . GLN A 1 22  ? 6.544   47.771 23.304  1.00 18.96 ? 22  GLN A OE1 1 
ATOM   165  N  NE2 . GLN A 1 22  ? 7.246   49.292 21.790  1.00 21.13 ? 22  GLN A NE2 1 
ATOM   166  N  N   . TRP A 1 23  ? 10.460  48.433 27.131  1.00 18.09 ? 23  TRP A N   1 
ATOM   167  C  CA  . TRP A 1 23  ? 10.511  49.278 28.309  1.00 17.71 ? 23  TRP A CA  1 
ATOM   168  C  C   . TRP A 1 23  ? 11.911  49.876 28.468  1.00 17.85 ? 23  TRP A C   1 
ATOM   169  O  O   . TRP A 1 23  ? 12.060  51.089 28.629  1.00 17.89 ? 23  TRP A O   1 
ATOM   170  C  CB  . TRP A 1 23  ? 10.099  48.473 29.529  1.00 17.34 ? 23  TRP A CB  1 
ATOM   171  C  CG  . TRP A 1 23  ? 9.977   49.248 30.796  1.00 17.04 ? 23  TRP A CG  1 
ATOM   172  C  CD1 . TRP A 1 23  ? 9.920   50.606 30.939  1.00 16.65 ? 23  TRP A CD1 1 
ATOM   173  C  CD2 . TRP A 1 23  ? 9.853   48.699 32.111  1.00 16.40 ? 23  TRP A CD2 1 
ATOM   174  N  NE1 . TRP A 1 23  ? 9.786   50.936 32.267  1.00 16.48 ? 23  TRP A NE1 1 
ATOM   175  C  CE2 . TRP A 1 23  ? 9.736   49.783 33.007  1.00 16.46 ? 23  TRP A CE2 1 
ATOM   176  C  CE3 . TRP A 1 23  ? 9.835   47.394 32.620  1.00 16.20 ? 23  TRP A CE3 1 
ATOM   177  C  CZ2 . TRP A 1 23  ? 9.607   49.601 34.388  1.00 16.92 ? 23  TRP A CZ2 1 
ATOM   178  C  CZ3 . TRP A 1 23  ? 9.702   47.213 33.995  1.00 16.89 ? 23  TRP A CZ3 1 
ATOM   179  C  CH2 . TRP A 1 23  ? 9.589   48.311 34.860  1.00 17.08 ? 23  TRP A CH2 1 
ATOM   180  N  N   . GLN A 1 24  ? 12.929  49.023 28.382  1.00 17.77 ? 24  GLN A N   1 
ATOM   181  C  CA  . GLN A 1 24  ? 14.319  49.465 28.342  1.00 17.63 ? 24  GLN A CA  1 
ATOM   182  C  C   . GLN A 1 24  ? 14.609  50.499 27.239  1.00 17.81 ? 24  GLN A C   1 
ATOM   183  O  O   . GLN A 1 24  ? 15.182  51.537 27.539  1.00 17.87 ? 24  GLN A O   1 
ATOM   184  C  CB  . GLN A 1 24  ? 15.235  48.257 28.194  1.00 17.59 ? 24  GLN A CB  1 
ATOM   185  C  CG  . GLN A 1 24  ? 16.722  48.563 28.214  1.00 17.59 ? 24  GLN A CG  1 
ATOM   186  C  CD  . GLN A 1 24  ? 17.548  47.322 28.023  1.00 17.92 ? 24  GLN A CD  1 
ATOM   187  O  OE1 . GLN A 1 24  ? 17.112  46.374 27.378  1.00 20.52 ? 24  GLN A OE1 1 
ATOM   188  N  NE2 . GLN A 1 24  ? 18.743  47.309 28.584  1.00 17.94 ? 24  GLN A NE2 1 
ATOM   189  N  N   . ARG A 1 25  ? 14.232  50.222 25.983  1.00 18.10 ? 25  ARG A N   1 
ATOM   190  C  CA  . ARG A 1 25  ? 14.470  51.172 24.876  1.00 18.51 ? 25  ARG A CA  1 
ATOM   191  C  C   . ARG A 1 25  ? 13.839  52.529 25.153  1.00 19.03 ? 25  ARG A C   1 
ATOM   192  O  O   . ARG A 1 25  ? 14.457  53.567 24.904  1.00 19.20 ? 25  ARG A O   1 
ATOM   193  C  CB  . ARG A 1 25  ? 13.964  50.648 23.525  1.00 18.48 ? 25  ARG A CB  1 
ATOM   194  C  CG  . ARG A 1 25  ? 14.800  49.522 22.904  1.00 18.73 ? 25  ARG A CG  1 
ATOM   195  C  CD  . ARG A 1 25  ? 14.438  49.237 21.435  1.00 18.21 ? 25  ARG A CD  1 
ATOM   196  N  NE  . ARG A 1 25  ? 13.011  48.990 21.208  1.00 18.14 ? 25  ARG A NE  1 
ATOM   197  C  CZ  . ARG A 1 25  ? 12.349  47.883 21.567  1.00 18.97 ? 25  ARG A CZ  1 
ATOM   198  N  NH1 . ARG A 1 25  ? 12.957  46.879 22.196  1.00 18.98 ? 25  ARG A NH1 1 
ATOM   199  N  NH2 . ARG A 1 25  ? 11.054  47.778 21.307  1.00 18.82 ? 25  ARG A NH2 1 
ATOM   200  N  N   . ASN A 1 26  ? 12.617  52.516 25.684  1.00 19.52 ? 26  ASN A N   1 
ATOM   201  C  CA  . ASN A 1 26  ? 11.891  53.753 25.964  1.00 19.81 ? 26  ASN A CA  1 
ATOM   202  C  C   . ASN A 1 26  ? 12.414  54.553 27.156  1.00 20.10 ? 26  ASN A C   1 
ATOM   203  O  O   . ASN A 1 26  ? 12.441  55.787 27.103  1.00 20.21 ? 26  ASN A O   1 
ATOM   204  C  CB  . ASN A 1 26  ? 10.389  53.499 26.077  1.00 19.62 ? 26  ASN A CB  1 
ATOM   205  C  CG  . ASN A 1 26  ? 9.726   53.410 24.724  1.00 19.35 ? 26  ASN A CG  1 
ATOM   206  O  OD1 . ASN A 1 26  ? 9.528   54.409 24.042  1.00 18.66 ? 26  ASN A OD1 1 
ATOM   207  N  ND2 . ASN A 1 26  ? 9.397   52.203 24.320  1.00 20.73 ? 26  ASN A ND2 1 
ATOM   208  N  N   . MET A 1 27  ? 12.840  53.858 28.210  1.00 20.09 ? 27  MET A N   1 
ATOM   209  C  CA  . MET A 1 27  ? 13.409  54.519 29.372  1.00 20.41 ? 27  MET A CA  1 
ATOM   210  C  C   . MET A 1 27  ? 14.701  55.222 29.007  1.00 21.03 ? 27  MET A C   1 
ATOM   211  O  O   . MET A 1 27  ? 15.021  56.264 29.561  1.00 21.35 ? 27  MET A O   1 
ATOM   212  C  CB  . MET A 1 27  ? 13.680  53.527 30.495  1.00 20.21 ? 27  MET A CB  1 
ATOM   213  C  CG  . MET A 1 27  ? 12.449  53.040 31.227  1.00 20.19 ? 27  MET A CG  1 
ATOM   214  S  SD  . MET A 1 27  ? 11.429  54.330 31.972  1.00 21.10 ? 27  MET A SD  1 
ATOM   215  C  CE  . MET A 1 27  ? 12.415  54.891 33.346  1.00 20.03 ? 27  MET A CE  1 
ATOM   216  N  N   . ARG A 1 28  ? 15.442  54.649 28.069  1.00 21.81 ? 28  ARG A N   1 
ATOM   217  C  CA  . ARG A 1 28  ? 16.723  55.201 27.673  1.00 22.58 ? 28  ARG A CA  1 
ATOM   218  C  C   . ARG A 1 28  ? 16.525  56.420 26.761  1.00 22.89 ? 28  ARG A C   1 
ATOM   219  O  O   . ARG A 1 28  ? 17.282  57.398 26.834  1.00 22.86 ? 28  ARG A O   1 
ATOM   220  C  CB  . ARG A 1 28  ? 17.577  54.124 26.997  1.00 22.63 ? 28  ARG A CB  1 
ATOM   221  C  CG  . ARG A 1 28  ? 18.992  54.578 26.733  1.00 24.29 ? 28  ARG A CG  1 
ATOM   222  C  CD  . ARG A 1 28  ? 19.958  53.447 26.422  1.00 26.39 ? 28  ARG A CD  1 
ATOM   223  N  NE  . ARG A 1 28  ? 21.283  54.015 26.183  1.00 27.90 ? 28  ARG A NE  1 
ATOM   224  C  CZ  . ARG A 1 28  ? 21.896  54.058 25.003  1.00 29.03 ? 28  ARG A CZ  1 
ATOM   225  N  NH1 . ARG A 1 28  ? 21.324  53.523 23.928  1.00 28.67 ? 28  ARG A NH1 1 
ATOM   226  N  NH2 . ARG A 1 28  ? 23.102  54.621 24.908  1.00 29.30 ? 28  ARG A NH2 1 
ATOM   227  N  N   . ARG A 1 29  ? 15.495  56.347 25.916  1.00 23.43 ? 29  ARG A N   1 
ATOM   228  C  CA  . ARG A 1 29  ? 15.163  57.405 24.958  1.00 23.50 ? 29  ARG A CA  1 
ATOM   229  C  C   . ARG A 1 29  ? 14.709  58.682 25.647  1.00 23.90 ? 29  ARG A C   1 
ATOM   230  O  O   . ARG A 1 29  ? 14.952  59.762 25.129  1.00 24.34 ? 29  ARG A O   1 
ATOM   231  C  CB  . ARG A 1 29  ? 14.094  56.921 23.972  1.00 23.46 ? 29  ARG A CB  1 
ATOM   232  C  CG  . ARG A 1 29  ? 13.569  57.962 22.979  1.00 22.86 ? 29  ARG A CG  1 
ATOM   233  C  CD  . ARG A 1 29  ? 12.383  57.417 22.171  1.00 23.26 ? 29  ARG A CD  1 
ATOM   234  N  NE  . ARG A 1 29  ? 11.324  56.859 23.023  1.00 23.26 ? 29  ARG A NE  1 
ATOM   235  C  CZ  . ARG A 1 29  ? 10.246  57.525 23.440  1.00 23.07 ? 29  ARG A CZ  1 
ATOM   236  N  NH1 . ARG A 1 29  ? 10.049  58.787 23.082  1.00 23.24 ? 29  ARG A NH1 1 
ATOM   237  N  NH2 . ARG A 1 29  ? 9.355   56.924 24.217  1.00 22.31 ? 29  ARG A NH2 1 
ATOM   238  N  N   . VAL A 1 30  ? 14.064  58.565 26.806  1.00 24.21 ? 30  VAL A N   1 
ATOM   239  C  CA  . VAL A 1 30  ? 13.543  59.745 27.513  1.00 24.56 ? 30  VAL A CA  1 
ATOM   240  C  C   . VAL A 1 30  ? 14.376  60.146 28.732  1.00 25.04 ? 30  VAL A C   1 
ATOM   241  O  O   . VAL A 1 30  ? 13.897  60.891 29.590  1.00 24.95 ? 30  VAL A O   1 
ATOM   242  C  CB  . VAL A 1 30  ? 12.027  59.612 27.902  1.00 24.56 ? 30  VAL A CB  1 
ATOM   243  C  CG1 . VAL A 1 30  ? 11.156  59.394 26.657  1.00 24.75 ? 30  VAL A CG1 1 
ATOM   244  C  CG2 . VAL A 1 30  ? 11.799  58.512 28.935  1.00 24.02 ? 30  VAL A CG2 1 
ATOM   245  N  N   . ARG A 1 31  ? 15.611  59.641 28.797  1.00 25.78 ? 31  ARG A N   1 
ATOM   246  C  CA  . ARG A 1 31  ? 16.594  60.012 29.831  1.00 26.59 ? 31  ARG A CA  1 
ATOM   247  C  C   . ARG A 1 31  ? 16.163  59.692 31.260  1.00 26.57 ? 31  ARG A C   1 
ATOM   248  O  O   . ARG A 1 31  ? 16.355  60.507 32.165  1.00 26.80 ? 31  ARG A O   1 
ATOM   249  C  CB  . ARG A 1 31  ? 16.967  61.501 29.731  1.00 26.81 ? 31  ARG A CB  1 
ATOM   250  C  CG  . ARG A 1 31  ? 18.319  61.784 29.103  1.00 29.26 ? 31  ARG A CG  1 
ATOM   251  C  CD  . ARG A 1 31  ? 18.243  62.188 27.625  1.00 32.70 ? 31  ARG A CD  1 
ATOM   252  N  NE  . ARG A 1 31  ? 18.353  61.046 26.712  1.00 35.31 ? 31  ARG A NE  1 
ATOM   253  C  CZ  . ARG A 1 31  ? 18.841  61.112 25.469  1.00 37.09 ? 31  ARG A CZ  1 
ATOM   254  N  NH1 . ARG A 1 31  ? 19.286  62.270 24.977  1.00 37.38 ? 31  ARG A NH1 1 
ATOM   255  N  NH2 . ARG A 1 31  ? 18.893  60.015 24.715  1.00 37.36 ? 31  ARG A NH2 1 
ATOM   256  N  N   . GLY A 1 32  ? 15.582  58.514 31.458  1.00 26.55 ? 32  GLY A N   1 
ATOM   257  C  CA  . GLY A 1 32  ? 15.142  58.082 32.788  1.00 26.65 ? 32  GLY A CA  1 
ATOM   258  C  C   . GLY A 1 32  ? 15.972  56.921 33.315  1.00 26.68 ? 32  GLY A C   1 
ATOM   259  O  O   . GLY A 1 32  ? 16.966  56.543 32.696  1.00 27.18 ? 32  GLY A O   1 
ATOM   260  N  N   . PRO A 1 33  ? 15.573  56.341 34.460  1.00 26.36 ? 33  PRO A N   1 
ATOM   261  C  CA  . PRO A 1 33  ? 16.323  55.248 35.086  1.00 26.03 ? 33  PRO A CA  1 
ATOM   262  C  C   . PRO A 1 33  ? 16.301  53.982 34.239  1.00 25.85 ? 33  PRO A C   1 
ATOM   263  O  O   . PRO A 1 33  ? 15.254  53.624 33.710  1.00 26.07 ? 33  PRO A O   1 
ATOM   264  C  CB  . PRO A 1 33  ? 15.562  55.002 36.388  1.00 26.04 ? 33  PRO A CB  1 
ATOM   265  C  CG  . PRO A 1 33  ? 14.736  56.218 36.589  1.00 26.31 ? 33  PRO A CG  1 
ATOM   266  C  CD  . PRO A 1 33  ? 14.381  56.698 35.240  1.00 26.22 ? 33  PRO A CD  1 
ATOM   267  N  N   . PRO A 1 34  ? 17.446  53.290 34.129  1.00 25.52 ? 34  PRO A N   1 
ATOM   268  C  CA  . PRO A 1 34  ? 17.525  52.127 33.238  1.00 25.18 ? 34  PRO A CA  1 
ATOM   269  C  C   . PRO A 1 34  ? 16.895  50.855 33.823  1.00 24.82 ? 34  PRO A C   1 
ATOM   270  O  O   . PRO A 1 34  ? 16.907  50.657 35.040  1.00 24.84 ? 34  PRO A O   1 
ATOM   271  C  CB  . PRO A 1 34  ? 19.031  51.942 33.038  1.00 24.96 ? 34  PRO A CB  1 
ATOM   272  C  CG  . PRO A 1 34  ? 19.651  52.505 34.277  1.00 25.50 ? 34  PRO A CG  1 
ATOM   273  C  CD  . PRO A 1 34  ? 18.713  53.539 34.843  1.00 25.49 ? 34  PRO A CD  1 
ATOM   274  N  N   . VAL A 1 35  ? 16.344  50.018 32.946  1.00 24.45 ? 35  VAL A N   1 
ATOM   275  C  CA  . VAL A 1 35  ? 15.849  48.691 33.305  1.00 24.21 ? 35  VAL A CA  1 
ATOM   276  C  C   . VAL A 1 35  ? 16.284  47.673 32.247  1.00 24.46 ? 35  VAL A C   1 
ATOM   277  O  O   . VAL A 1 35  ? 16.150  47.925 31.062  1.00 24.41 ? 35  VAL A O   1 
ATOM   278  C  CB  . VAL A 1 35  ? 14.306  48.672 33.491  1.00 24.04 ? 35  VAL A CB  1 
ATOM   279  C  CG1 . VAL A 1 35  ? 13.580  49.132 32.234  1.00 23.48 ? 35  VAL A CG1 1 
ATOM   280  C  CG2 . VAL A 1 35  ? 13.832  47.294 33.906  1.00 23.76 ? 35  VAL A CG2 1 
ATOM   281  N  N   . SER A 1 36  ? 16.834  46.541 32.668  1.00 24.77 ? 36  SER A N   1 
ATOM   282  C  CA  . SER A 1 36  ? 17.138  45.463 31.728  1.00 25.27 ? 36  SER A CA  1 
ATOM   283  C  C   . SER A 1 36  ? 16.252  44.272 32.067  1.00 25.45 ? 36  SER A C   1 
ATOM   284  O  O   . SER A 1 36  ? 15.443  44.363 32.986  1.00 25.45 ? 36  SER A O   1 
ATOM   285  C  CB  . SER A 1 36  ? 18.623  45.087 31.769  1.00 25.31 ? 36  SER A CB  1 
ATOM   286  O  OG  . SER A 1 36  ? 18.965  44.461 32.996  1.00 25.57 ? 36  SER A OG  1 
ATOM   287  N  N   . CYS A 1 37  ? 16.389  43.167 31.339  1.00 25.70 ? 37  CYS A N   1 
ATOM   288  C  CA  . CYS A 1 37  ? 15.487  42.032 31.551  1.00 26.41 ? 37  CYS A CA  1 
ATOM   289  C  C   . CYS A 1 37  ? 16.180  40.687 31.675  1.00 25.86 ? 37  CYS A C   1 
ATOM   290  O  O   . CYS A 1 37  ? 17.172  40.410 31.002  1.00 25.93 ? 37  CYS A O   1 
ATOM   291  C  CB  . CYS A 1 37  ? 14.365  42.011 30.498  1.00 26.60 ? 37  CYS A CB  1 
ATOM   292  S  SG  . CYS A 1 37  ? 13.679  43.738 30.229  1.00 31.21 ? 37  CYS A SG  1 
ATOM   293  N  N   . ILE A 1 38  ? 15.648  39.879 32.582  1.00 25.44 ? 38  ILE A N   1 
ATOM   294  C  CA  . ILE A 1 38  ? 16.134  38.549 32.851  1.00 25.22 ? 38  ILE A CA  1 
ATOM   295  C  C   . ILE A 1 38  ? 15.005  37.598 32.495  1.00 25.46 ? 38  ILE A C   1 
ATOM   296  O  O   . ILE A 1 38  ? 13.854  37.835 32.859  1.00 25.44 ? 38  ILE A O   1 
ATOM   297  C  CB  . ILE A 1 38  ? 16.535  38.411 34.337  1.00 25.17 ? 38  ILE A CB  1 
ATOM   298  C  CG1 . ILE A 1 38  ? 17.689  39.366 34.671  1.00 24.79 ? 38  ILE A CG1 1 
ATOM   299  C  CG2 . ILE A 1 38  ? 16.897  36.976 34.690  1.00 24.61 ? 38  ILE A CG2 1 
ATOM   300  C  CD1 . ILE A 1 38  ? 18.953  39.151 33.852  1.00 23.03 ? 38  ILE A CD1 1 
ATOM   301  N  N   . LYS A 1 39  ? 15.332  36.533 31.770  1.00 25.79 ? 39  LYS A N   1 
ATOM   302  C  CA  . LYS A 1 39  ? 14.321  35.615 31.264  1.00 26.19 ? 39  LYS A CA  1 
ATOM   303  C  C   . LYS A 1 39  ? 14.242  34.321 32.064  1.00 26.60 ? 39  LYS A C   1 
ATOM   304  O  O   . LYS A 1 39  ? 15.222  33.590 32.182  1.00 26.55 ? 39  LYS A O   1 
ATOM   305  C  CB  . LYS A 1 39  ? 14.563  35.302 29.785  1.00 26.28 ? 39  LYS A CB  1 
ATOM   306  C  CG  . LYS A 1 39  ? 14.514  36.515 28.857  1.00 26.19 ? 39  LYS A CG  1 
ATOM   307  C  CD  . LYS A 1 39  ? 14.457  36.090 27.389  1.00 26.05 ? 39  LYS A CD  1 
ATOM   308  C  CE  . LYS A 1 39  ? 15.694  35.316 26.970  1.00 25.57 ? 39  LYS A CE  1 
ATOM   309  N  NZ  . LYS A 1 39  ? 15.595  34.922 25.557  1.00 25.79 ? 39  LYS A NZ  1 
ATOM   310  N  N   . ARG A 1 40  ? 13.059  34.054 32.608  1.00 27.21 ? 40  ARG A N   1 
ATOM   311  C  CA  . ARG A 1 40  ? 12.760  32.802 33.291  1.00 27.84 ? 40  ARG A CA  1 
ATOM   312  C  C   . ARG A 1 40  ? 11.397  32.275 32.814  1.00 28.92 ? 40  ARG A C   1 
ATOM   313  O  O   . ARG A 1 40  ? 10.755  32.903 31.965  1.00 29.12 ? 40  ARG A O   1 
ATOM   314  C  CB  . ARG A 1 40  ? 12.784  33.001 34.809  1.00 27.42 ? 40  ARG A CB  1 
ATOM   315  C  CG  . ARG A 1 40  ? 14.148  33.353 35.391  1.00 25.93 ? 40  ARG A CG  1 
ATOM   316  C  CD  . ARG A 1 40  ? 15.147  32.226 35.187  1.00 23.52 ? 40  ARG A CD  1 
ATOM   317  N  NE  . ARG A 1 40  ? 16.403  32.447 35.894  1.00 21.84 ? 40  ARG A NE  1 
ATOM   318  C  CZ  . ARG A 1 40  ? 17.447  33.104 35.395  1.00 21.63 ? 40  ARG A CZ  1 
ATOM   319  N  NH1 . ARG A 1 40  ? 17.395  33.625 34.178  1.00 20.87 ? 40  ARG A NH1 1 
ATOM   320  N  NH2 . ARG A 1 40  ? 18.549  33.247 36.119  1.00 22.14 ? 40  ARG A NH2 1 
ATOM   321  N  N   . ASP A 1 41  ? 10.960  31.134 33.356  1.00 29.96 ? 41  ASP A N   1 
ATOM   322  C  CA  . ASP A 1 41  ? 9.747   30.457 32.871  1.00 30.93 ? 41  ASP A CA  1 
ATOM   323  C  C   . ASP A 1 41  ? 8.589   30.390 33.863  1.00 30.82 ? 41  ASP A C   1 
ATOM   324  O  O   . ASP A 1 41  ? 7.485   29.976 33.504  1.00 31.10 ? 41  ASP A O   1 
ATOM   325  C  CB  . ASP A 1 41  ? 10.085  29.049 32.371  1.00 31.51 ? 41  ASP A CB  1 
ATOM   326  C  CG  . ASP A 1 41  ? 10.884  29.069 31.072  1.00 34.54 ? 41  ASP A CG  1 
ATOM   327  O  OD1 . ASP A 1 41  ? 10.454  29.760 30.109  1.00 37.57 ? 41  ASP A OD1 1 
ATOM   328  O  OD2 . ASP A 1 41  ? 11.942  28.393 31.009  1.00 37.17 ? 41  ASP A OD2 1 
ATOM   329  N  N   . SER A 1 42  ? 8.830   30.789 35.104  1.00 30.58 ? 42  SER A N   1 
ATOM   330  C  CA  . SER A 1 42  ? 7.782   30.751 36.111  1.00 30.47 ? 42  SER A CA  1 
ATOM   331  C  C   . SER A 1 42  ? 8.082   31.717 37.242  1.00 30.17 ? 42  SER A C   1 
ATOM   332  O  O   . SER A 1 42  ? 9.255   31.996 37.526  1.00 30.34 ? 42  SER A O   1 
ATOM   333  C  CB  . SER A 1 42  ? 7.643   29.339 36.682  1.00 30.57 ? 42  SER A CB  1 
ATOM   334  O  OG  . SER A 1 42  ? 8.849   28.930 37.299  1.00 31.09 ? 42  SER A OG  1 
ATOM   335  N  N   . PRO A 1 43  ? 7.027   32.216 37.910  1.00 29.69 ? 43  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 43  ? 7.250   33.071 39.067  1.00 29.20 ? 43  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 43  ? 8.252   32.468 40.060  1.00 28.89 ? 43  PRO A C   1 
ATOM   338  O  O   . PRO A 1 43  ? 9.125   33.189 40.539  1.00 29.00 ? 43  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 43  ? 5.851   33.221 39.687  1.00 29.19 ? 43  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 43  ? 4.955   32.278 38.947  1.00 29.44 ? 43  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 43  ? 5.593   32.029 37.625  1.00 29.71 ? 43  PRO A CD  1 
ATOM   342  N  N   . ILE A 1 44  ? 8.156   31.166 40.343  1.00 28.47 ? 44  ILE A N   1 
ATOM   343  C  CA  . ILE A 1 44  ? 9.088   30.520 41.273  1.00 28.15 ? 44  ILE A CA  1 
ATOM   344  C  C   . ILE A 1 44  ? 10.519  30.786 40.847  1.00 27.95 ? 44  ILE A C   1 
ATOM   345  O  O   . ILE A 1 44  ? 11.352  31.179 41.668  1.00 28.05 ? 44  ILE A O   1 
ATOM   346  C  CB  . ILE A 1 44  ? 8.876   28.986 41.383  1.00 28.36 ? 44  ILE A CB  1 
ATOM   347  C  CG1 . ILE A 1 44  ? 7.556   28.657 42.094  1.00 29.04 ? 44  ILE A CG1 1 
ATOM   348  C  CG2 . ILE A 1 44  ? 10.036  28.333 42.130  1.00 27.98 ? 44  ILE A CG2 1 
ATOM   349  C  CD1 . ILE A 1 44  ? 7.517   29.061 43.575  1.00 29.39 ? 44  ILE A CD1 1 
ATOM   350  N  N   . GLN A 1 45  ? 10.790  30.579 39.556  1.00 27.50 ? 45  GLN A N   1 
ATOM   351  C  CA  . GLN A 1 45  ? 12.126  30.775 38.999  1.00 26.83 ? 45  GLN A CA  1 
ATOM   352  C  C   . GLN A 1 45  ? 12.566  32.227 39.104  1.00 26.26 ? 45  GLN A C   1 
ATOM   353  O  O   . GLN A 1 45  ? 13.734  32.512 39.367  1.00 26.32 ? 45  GLN A O   1 
ATOM   354  C  CB  . GLN A 1 45  ? 12.200  30.285 37.555  1.00 26.74 ? 45  GLN A CB  1 
ATOM   355  C  CG  . GLN A 1 45  ? 12.639  28.846 37.442  1.00 27.41 ? 45  GLN A CG  1 
ATOM   356  C  CD  . GLN A 1 45  ? 12.741  28.374 36.008  1.00 29.25 ? 45  GLN A CD  1 
ATOM   357  O  OE1 . GLN A 1 45  ? 13.703  27.703 35.632  1.00 30.77 ? 45  GLN A OE1 1 
ATOM   358  N  NE2 . GLN A 1 45  ? 11.752  28.724 35.195  1.00 30.07 ? 45  GLN A NE2 1 
ATOM   359  N  N   . CYS A 1 46  ? 11.627  33.142 38.914  1.00 25.39 ? 46  CYS A N   1 
ATOM   360  C  CA  . CYS A 1 46  ? 11.912  34.543 39.115  1.00 25.00 ? 46  CYS A CA  1 
ATOM   361  C  C   . CYS A 1 46  ? 12.204  34.878 40.566  1.00 24.35 ? 46  CYS A C   1 
ATOM   362  O  O   . CYS A 1 46  ? 13.070  35.705 40.833  1.00 24.39 ? 46  CYS A O   1 
ATOM   363  C  CB  . CYS A 1 46  ? 10.759  35.383 38.607  1.00 25.19 ? 46  CYS A CB  1 
ATOM   364  S  SG  . CYS A 1 46  ? 10.954  35.717 36.881  1.00 27.48 ? 46  CYS A SG  1 
ATOM   365  N  N   . ILE A 1 47  ? 11.479  34.245 41.492  1.00 23.52 ? 47  ILE A N   1 
ATOM   366  C  CA  . ILE A 1 47  ? 11.709  34.433 42.923  1.00 22.67 ? 47  ILE A CA  1 
ATOM   367  C  C   . ILE A 1 47  ? 13.110  33.938 43.278  1.00 23.04 ? 47  ILE A C   1 
ATOM   368  O  O   . ILE A 1 47  ? 13.870  34.650 43.936  1.00 23.39 ? 47  ILE A O   1 
ATOM   369  C  CB  . ILE A 1 47  ? 10.613  33.756 43.811  1.00 22.72 ? 47  ILE A CB  1 
ATOM   370  C  CG1 . ILE A 1 47  ? 9.246   34.427 43.603  1.00 22.13 ? 47  ILE A CG1 1 
ATOM   371  C  CG2 . ILE A 1 47  ? 10.990  33.821 45.281  1.00 21.66 ? 47  ILE A CG2 1 
ATOM   372  C  CD1 . ILE A 1 47  ? 8.047   33.598 44.036  1.00 21.54 ? 47  ILE A CD1 1 
ATOM   373  N  N   . GLN A 1 48  ? 13.456  32.735 42.821  1.00 22.86 ? 48  GLN A N   1 
ATOM   374  C  CA  . GLN A 1 48  ? 14.798  32.189 43.022  1.00 22.87 ? 48  GLN A CA  1 
ATOM   375  C  C   . GLN A 1 48  ? 15.886  33.075 42.409  1.00 22.65 ? 48  GLN A C   1 
ATOM   376  O  O   . GLN A 1 48  ? 16.978  33.205 42.968  1.00 22.72 ? 48  GLN A O   1 
ATOM   377  C  CB  . GLN A 1 48  ? 14.904  30.786 42.427  1.00 23.02 ? 48  GLN A CB  1 
ATOM   378  C  CG  . GLN A 1 48  ? 13.995  29.757 43.078  1.00 24.46 ? 48  GLN A CG  1 
ATOM   379  C  CD  . GLN A 1 48  ? 13.809  28.512 42.231  1.00 25.90 ? 48  GLN A CD  1 
ATOM   380  O  OE1 . GLN A 1 48  ? 14.174  28.478 41.044  1.00 26.20 ? 48  GLN A OE1 1 
ATOM   381  N  NE2 . GLN A 1 48  ? 13.233  27.475 42.837  1.00 26.23 ? 48  GLN A NE2 1 
ATOM   382  N  N   . ALA A 1 49  ? 15.588  33.672 41.258  1.00 22.18 ? 49  ALA A N   1 
ATOM   383  C  CA  . ALA A 1 49  ? 16.548  34.509 40.568  1.00 21.92 ? 49  ALA A CA  1 
ATOM   384  C  C   . ALA A 1 49  ? 16.857  35.752 41.380  1.00 21.99 ? 49  ALA A C   1 
ATOM   385  O  O   . ALA A 1 49  ? 18.026  36.127 41.517  1.00 22.27 ? 49  ALA A O   1 
ATOM   386  C  CB  . ALA A 1 49  ? 16.042  34.884 39.199  1.00 22.00 ? 49  ALA A CB  1 
ATOM   387  N  N   . ILE A 1 50  ? 15.819  36.383 41.925  1.00 21.90 ? 50  ILE A N   1 
ATOM   388  C  CA  . ILE A 1 50  ? 16.004  37.580 42.745  1.00 22.08 ? 50  ILE A CA  1 
ATOM   389  C  C   . ILE A 1 50  ? 16.680  37.240 44.075  1.00 22.48 ? 50  ILE A C   1 
ATOM   390  O  O   . ILE A 1 50  ? 17.542  37.982 44.542  1.00 22.49 ? 50  ILE A O   1 
ATOM   391  C  CB  . ILE A 1 50  ? 14.688  38.337 42.991  1.00 21.88 ? 50  ILE A CB  1 
ATOM   392  C  CG1 . ILE A 1 50  ? 14.027  38.706 41.669  1.00 21.41 ? 50  ILE A CG1 1 
ATOM   393  C  CG2 . ILE A 1 50  ? 14.951  39.607 43.779  1.00 22.39 ? 50  ILE A CG2 1 
ATOM   394  C  CD1 . ILE A 1 50  ? 12.588  39.121 41.800  1.00 20.55 ? 50  ILE A CD1 1 
ATOM   395  N  N   . ALA A 1 51  ? 16.297  36.109 44.666  1.00 23.02 ? 51  ALA A N   1 
ATOM   396  C  CA  . ALA A 1 51  ? 16.915  35.619 45.900  1.00 23.37 ? 51  ALA A CA  1 
ATOM   397  C  C   . ALA A 1 51  ? 18.408  35.385 45.729  1.00 23.86 ? 51  ALA A C   1 
ATOM   398  O  O   . ALA A 1 51  ? 19.193  35.691 46.627  1.00 23.84 ? 51  ALA A O   1 
ATOM   399  C  CB  . ALA A 1 51  ? 16.254  34.344 46.345  1.00 23.26 ? 51  ALA A CB  1 
ATOM   400  N  N   . GLU A 1 52  ? 18.781  34.851 44.565  1.00 24.41 ? 52  GLU A N   1 
ATOM   401  C  CA  . GLU A 1 52  ? 20.144  34.410 44.293  1.00 25.18 ? 52  GLU A CA  1 
ATOM   402  C  C   . GLU A 1 52  ? 20.984  35.481 43.586  1.00 24.80 ? 52  GLU A C   1 
ATOM   403  O  O   . GLU A 1 52  ? 22.092  35.213 43.115  1.00 24.70 ? 52  GLU A O   1 
ATOM   404  C  CB  . GLU A 1 52  ? 20.118  33.088 43.517  1.00 24.98 ? 52  GLU A CB  1 
ATOM   405  C  CG  . GLU A 1 52  ? 19.822  31.868 44.401  1.00 26.56 ? 52  GLU A CG  1 
ATOM   406  C  CD  . GLU A 1 52  ? 19.350  30.636 43.618  1.00 27.35 ? 52  GLU A CD  1 
ATOM   407  O  OE1 . GLU A 1 52  ? 19.702  30.502 42.418  1.00 29.48 ? 52  GLU A OE1 1 
ATOM   408  O  OE2 . GLU A 1 52  ? 18.625  29.796 44.215  1.00 29.80 ? 52  GLU A OE2 1 
ATOM   409  N  N   . ASN A 1 53  ? 20.447  36.699 43.551  1.00 24.75 ? 53  ASN A N   1 
ATOM   410  C  CA  . ASN A 1 53  ? 21.125  37.873 42.993  1.00 24.69 ? 53  ASN A CA  1 
ATOM   411  C  C   . ASN A 1 53  ? 21.407  37.745 41.496  1.00 24.26 ? 53  ASN A C   1 
ATOM   412  O  O   . ASN A 1 53  ? 22.509  38.026 41.020  1.00 24.15 ? 53  ASN A O   1 
ATOM   413  C  CB  . ASN A 1 53  ? 22.393  38.233 43.793  1.00 25.00 ? 53  ASN A CB  1 
ATOM   414  C  CG  . ASN A 1 53  ? 22.659  39.746 43.824  1.00 26.41 ? 53  ASN A CG  1 
ATOM   415  O  OD1 . ASN A 1 53  ? 23.194  40.331 42.872  1.00 26.78 ? 53  ASN A OD1 1 
ATOM   416  N  ND2 . ASN A 1 53  ? 22.281  40.383 44.930  1.00 27.74 ? 53  ASN A ND2 1 
ATOM   417  N  N   . ARG A 1 54  ? 20.390  37.307 40.763  1.00 23.84 ? 54  ARG A N   1 
ATOM   418  C  CA  . ARG A 1 54  ? 20.462  37.240 39.310  1.00 23.34 ? 54  ARG A CA  1 
ATOM   419  C  C   . ARG A 1 54  ? 19.448  38.182 38.694  1.00 22.70 ? 54  ARG A C   1 
ATOM   420  O  O   . ARG A 1 54  ? 19.481  38.432 37.493  1.00 22.77 ? 54  ARG A O   1 
ATOM   421  C  CB  . ARG A 1 54  ? 20.224  35.813 38.811  1.00 23.65 ? 54  ARG A CB  1 
ATOM   422  C  CG  . ARG A 1 54  ? 21.483  34.985 38.598  1.00 24.33 ? 54  ARG A CG  1 
ATOM   423  C  CD  . ARG A 1 54  ? 21.942  34.330 39.877  1.00 26.25 ? 54  ARG A CD  1 
ATOM   424  N  NE  . ARG A 1 54  ? 23.052  33.413 39.645  1.00 28.22 ? 54  ARG A NE  1 
ATOM   425  C  CZ  . ARG A 1 54  ? 23.469  32.501 40.521  1.00 29.53 ? 54  ARG A CZ  1 
ATOM   426  N  NH1 . ARG A 1 54  ? 22.865  32.371 41.697  1.00 29.94 ? 54  ARG A NH1 1 
ATOM   427  N  NH2 . ARG A 1 54  ? 24.490  31.708 40.219  1.00 29.90 ? 54  ARG A NH2 1 
ATOM   428  N  N   . ALA A 1 55  ? 18.544  38.687 39.528  1.00 21.87 ? 55  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 55  ? 17.545  39.665 39.131  1.00 21.18 ? 55  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 55  ? 17.195  40.469 40.365  1.00 21.00 ? 55  ALA A C   1 
ATOM   431  O  O   . ALA A 1 55  ? 17.630  40.130 41.465  1.00 20.75 ? 55  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 55  ? 16.315  38.973 38.583  1.00 21.18 ? 55  ALA A CB  1 
ATOM   433  N  N   . ASP A 1 56  ? 16.400  41.521 40.192  1.00 20.96 ? 56  ASP A N   1 
ATOM   434  C  CA  . ASP A 1 56  ? 16.059  42.413 41.303  1.00 20.98 ? 56  ASP A CA  1 
ATOM   435  C  C   . ASP A 1 56  ? 14.558  42.523 41.585  1.00 20.93 ? 56  ASP A C   1 
ATOM   436  O  O   . ASP A 1 56  ? 14.155  42.694 42.730  1.00 20.82 ? 56  ASP A O   1 
ATOM   437  C  CB  . ASP A 1 56  ? 16.640  43.812 41.057  1.00 21.00 ? 56  ASP A CB  1 
ATOM   438  C  CG  . ASP A 1 56  ? 18.158  43.801 40.865  1.00 21.71 ? 56  ASP A CG  1 
ATOM   439  O  OD1 . ASP A 1 56  ? 18.883  43.357 41.793  1.00 22.21 ? 56  ASP A OD1 1 
ATOM   440  O  OD2 . ASP A 1 56  ? 18.625  44.258 39.792  1.00 20.83 ? 56  ASP A OD2 1 
ATOM   441  N  N   . ALA A 1 57  ? 13.730  42.425 40.548  1.00 21.10 ? 57  ALA A N   1 
ATOM   442  C  CA  . ALA A 1 57  ? 12.317  42.770 40.692  1.00 20.98 ? 57  ALA A CA  1 
ATOM   443  C  C   . ALA A 1 57  ? 11.346  41.978 39.802  1.00 20.94 ? 57  ALA A C   1 
ATOM   444  O  O   . ALA A 1 57  ? 11.642  41.707 38.639  1.00 20.85 ? 57  ALA A O   1 
ATOM   445  C  CB  . ALA A 1 57  ? 12.139  44.264 40.477  1.00 20.78 ? 57  ALA A CB  1 
ATOM   446  N  N   . VAL A 1 58  ? 10.187  41.630 40.372  1.00 20.92 ? 58  VAL A N   1 
ATOM   447  C  CA  . VAL A 1 58  ? 9.072   40.996 39.645  1.00 20.85 ? 58  VAL A CA  1 
ATOM   448  C  C   . VAL A 1 58  ? 7.705   41.241 40.332  1.00 21.08 ? 58  VAL A C   1 
ATOM   449  O  O   . VAL A 1 58  ? 7.627   41.328 41.562  1.00 21.28 ? 58  VAL A O   1 
ATOM   450  C  CB  . VAL A 1 58  ? 9.301   39.474 39.468  1.00 20.63 ? 58  VAL A CB  1 
ATOM   451  C  CG1 . VAL A 1 58  ? 9.163   38.744 40.808  1.00 20.33 ? 58  VAL A CG1 1 
ATOM   452  C  CG2 . VAL A 1 58  ? 8.340   38.905 38.436  1.00 20.18 ? 58  VAL A CG2 1 
ATOM   453  N  N   . THR A 1 59  ? 6.641   41.342 39.531  1.00 20.89 ? 59  THR A N   1 
ATOM   454  C  CA  . THR A 1 59  ? 5.286   41.531 40.038  1.00 20.73 ? 59  THR A CA  1 
ATOM   455  C  C   . THR A 1 59  ? 4.584   40.180 40.230  1.00 21.20 ? 59  THR A C   1 
ATOM   456  O  O   . THR A 1 59  ? 4.351   39.436 39.263  1.00 21.57 ? 59  THR A O   1 
ATOM   457  C  CB  . THR A 1 59  ? 4.453   42.382 39.085  1.00 20.37 ? 59  THR A CB  1 
ATOM   458  O  OG1 . THR A 1 59  ? 5.256   43.442 38.569  1.00 21.27 ? 59  THR A OG1 1 
ATOM   459  C  CG2 . THR A 1 59  ? 3.277   42.980 39.797  1.00 20.00 ? 59  THR A CG2 1 
ATOM   460  N  N   . LEU A 1 60  ? 4.229   39.879 41.477  1.00 20.94 ? 60  LEU A N   1 
ATOM   461  C  CA  . LEU A 1 60  ? 3.631   38.600 41.817  1.00 20.42 ? 60  LEU A CA  1 
ATOM   462  C  C   . LEU A 1 60  ? 2.237   38.796 42.340  1.00 20.81 ? 60  LEU A C   1 
ATOM   463  O  O   . LEU A 1 60  ? 1.926   39.840 42.899  1.00 20.97 ? 60  LEU A O   1 
ATOM   464  C  CB  . LEU A 1 60  ? 4.447   37.894 42.896  1.00 19.98 ? 60  LEU A CB  1 
ATOM   465  C  CG  . LEU A 1 60  ? 5.898   37.572 42.575  1.00 18.87 ? 60  LEU A CG  1 
ATOM   466  C  CD1 . LEU A 1 60  ? 6.598   37.163 43.847  1.00 17.65 ? 60  LEU A CD1 1 
ATOM   467  C  CD2 . LEU A 1 60  ? 5.993   36.500 41.520  1.00 16.98 ? 60  LEU A CD2 1 
ATOM   468  N  N   . ASP A 1 61  ? 1.410   37.774 42.148  1.00 21.24 ? 61  ASP A N   1 
ATOM   469  C  CA  . ASP A 1 61  ? 0.107   37.673 42.767  1.00 21.65 ? 61  ASP A CA  1 
ATOM   470  C  C   . ASP A 1 61  ? 0.279   37.334 44.250  1.00 21.64 ? 61  ASP A C   1 
ATOM   471  O  O   . ASP A 1 61  ? 1.319   36.807 44.652  1.00 21.69 ? 61  ASP A O   1 
ATOM   472  C  CB  . ASP A 1 61  ? -0.704  36.583 42.058  1.00 22.10 ? 61  ASP A CB  1 
ATOM   473  C  CG  . ASP A 1 61  ? -1.968  36.208 42.813  1.00 23.80 ? 61  ASP A CG  1 
ATOM   474  O  OD1 . ASP A 1 61  ? -2.970  36.964 42.742  1.00 25.17 ? 61  ASP A OD1 1 
ATOM   475  O  OD2 . ASP A 1 61  ? -1.945  35.160 43.496  1.00 26.16 ? 61  ASP A OD2 1 
ATOM   476  N  N   . GLY A 1 62  ? -0.748  37.613 45.050  1.00 21.75 ? 62  GLY A N   1 
ATOM   477  C  CA  . GLY A 1 62  ? -0.701  37.401 46.495  1.00 22.31 ? 62  GLY A CA  1 
ATOM   478  C  C   . GLY A 1 62  ? -0.196  36.022 46.881  1.00 22.79 ? 62  GLY A C   1 
ATOM   479  O  O   . GLY A 1 62  ? 0.575   35.874 47.841  1.00 22.59 ? 62  GLY A O   1 
ATOM   480  N  N   . GLY A 1 63  ? -0.623  35.016 46.116  1.00 22.97 ? 63  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 63  ? -0.226  33.634 46.354  1.00 23.35 ? 63  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 63  ? 1.279   33.431 46.257  1.00 23.64 ? 63  GLY A C   1 
ATOM   483  O  O   . GLY A 1 63  ? 1.854   32.619 47.001  1.00 23.55 ? 63  GLY A O   1 
ATOM   484  N  N   . PHE A 1 64  ? 1.917   34.175 45.347  1.00 23.67 ? 64  PHE A N   1 
ATOM   485  C  CA  . PHE A 1 64  ? 3.373   34.094 45.172  1.00 23.40 ? 64  PHE A CA  1 
ATOM   486  C  C   . PHE A 1 64  ? 4.186   35.072 46.014  1.00 23.02 ? 64  PHE A C   1 
ATOM   487  O  O   . PHE A 1 64  ? 5.360   34.816 46.285  1.00 22.58 ? 64  PHE A O   1 
ATOM   488  C  CB  . PHE A 1 64  ? 3.751   34.095 43.689  1.00 23.47 ? 64  PHE A CB  1 
ATOM   489  C  CG  . PHE A 1 64  ? 3.381   32.814 43.012  1.00 24.08 ? 64  PHE A CG  1 
ATOM   490  C  CD1 . PHE A 1 64  ? 2.125   32.657 42.430  1.00 25.18 ? 64  PHE A CD1 1 
ATOM   491  C  CD2 . PHE A 1 64  ? 4.253   31.726 43.035  1.00 24.10 ? 64  PHE A CD2 1 
ATOM   492  C  CE1 . PHE A 1 64  ? 1.759   31.439 41.832  1.00 25.44 ? 64  PHE A CE1 1 
ATOM   493  C  CE2 . PHE A 1 64  ? 3.902   30.515 42.450  1.00 24.19 ? 64  PHE A CE2 1 
ATOM   494  C  CZ  . PHE A 1 64  ? 2.652   30.365 41.851  1.00 24.43 ? 64  PHE A CZ  1 
ATOM   495  N  N   . ILE A 1 65  ? 3.547   36.159 46.452  1.00 22.83 ? 65  ILE A N   1 
ATOM   496  C  CA  . ILE A 1 65  ? 4.117   37.039 47.472  1.00 22.75 ? 65  ILE A CA  1 
ATOM   497  C  C   . ILE A 1 65  ? 4.309   36.235 48.765  1.00 23.17 ? 65  ILE A C   1 
ATOM   498  O  O   . ILE A 1 65  ? 5.364   36.322 49.411  1.00 23.33 ? 65  ILE A O   1 
ATOM   499  C  CB  . ILE A 1 65  ? 3.217   38.263 47.738  1.00 22.69 ? 65  ILE A CB  1 
ATOM   500  C  CG1 . ILE A 1 65  ? 3.212   39.211 46.536  1.00 22.03 ? 65  ILE A CG1 1 
ATOM   501  C  CG2 . ILE A 1 65  ? 3.672   39.019 48.985  1.00 22.80 ? 65  ILE A CG2 1 
ATOM   502  C  CD1 . ILE A 1 65  ? 1.981   40.086 46.475  1.00 19.96 ? 65  ILE A CD1 1 
ATOM   503  N  N   . TYR A 1 66  ? 3.291   35.449 49.131  1.00 23.37 ? 66  TYR A N   1 
ATOM   504  C  CA  . TYR A 1 66  ? 3.375   34.573 50.294  1.00 23.41 ? 66  TYR A CA  1 
ATOM   505  C  C   . TYR A 1 66  ? 4.513   33.594 50.083  1.00 23.38 ? 66  TYR A C   1 
ATOM   506  O  O   . TYR A 1 66  ? 5.349   33.416 50.957  1.00 23.87 ? 66  TYR A O   1 
ATOM   507  C  CB  . TYR A 1 66  ? 2.061   33.811 50.552  1.00 23.33 ? 66  TYR A CB  1 
ATOM   508  C  CG  . TYR A 1 66  ? 2.214   32.697 51.585  1.00 23.49 ? 66  TYR A CG  1 
ATOM   509  C  CD1 . TYR A 1 66  ? 2.092   32.958 52.948  1.00 23.64 ? 66  TYR A CD1 1 
ATOM   510  C  CD2 . TYR A 1 66  ? 2.512   31.388 51.197  1.00 23.56 ? 66  TYR A CD2 1 
ATOM   511  C  CE1 . TYR A 1 66  ? 2.252   31.940 53.904  1.00 23.75 ? 66  TYR A CE1 1 
ATOM   512  C  CE2 . TYR A 1 66  ? 2.673   30.369 52.143  1.00 23.22 ? 66  TYR A CE2 1 
ATOM   513  C  CZ  . TYR A 1 66  ? 2.544   30.650 53.493  1.00 23.25 ? 66  TYR A CZ  1 
ATOM   514  O  OH  . TYR A 1 66  ? 2.705   29.647 54.428  1.00 22.51 ? 66  TYR A OH  1 
ATOM   515  N  N   . GLU A 1 67  ? 4.535   32.964 48.919  1.00 23.40 ? 67  GLU A N   1 
ATOM   516  C  CA  . GLU A 1 67  ? 5.571   32.002 48.583  1.00 23.58 ? 67  GLU A CA  1 
ATOM   517  C  C   . GLU A 1 67  ? 6.983   32.595 48.694  1.00 23.17 ? 67  GLU A C   1 
ATOM   518  O  O   . GLU A 1 67  ? 7.880   31.968 49.270  1.00 23.38 ? 67  GLU A O   1 
ATOM   519  C  CB  . GLU A 1 67  ? 5.333   31.457 47.176  1.00 23.82 ? 67  GLU A CB  1 
ATOM   520  C  CG  . GLU A 1 67  ? 5.873   30.059 46.964  1.00 25.41 ? 67  GLU A CG  1 
ATOM   521  C  CD  . GLU A 1 67  ? 5.023   28.994 47.632  1.00 27.28 ? 67  GLU A CD  1 
ATOM   522  O  OE1 . GLU A 1 67  ? 3.837   28.856 47.251  1.00 26.98 ? 67  GLU A OE1 1 
ATOM   523  O  OE2 . GLU A 1 67  ? 5.551   28.290 48.530  1.00 28.56 ? 67  GLU A OE2 1 
ATOM   524  N  N   . ALA A 1 68  ? 7.155   33.806 48.166  1.00 22.64 ? 68  ALA A N   1 
ATOM   525  C  CA  . ALA A 1 68  ? 8.448   34.480 48.104  1.00 22.37 ? 68  ALA A CA  1 
ATOM   526  C  C   . ALA A 1 68  ? 8.900   35.040 49.435  1.00 22.54 ? 68  ALA A C   1 
ATOM   527  O  O   . ALA A 1 68  ? 10.040  35.478 49.566  1.00 22.66 ? 68  ALA A O   1 
ATOM   528  C  CB  . ALA A 1 68  ? 8.397   35.590 47.103  1.00 22.53 ? 68  ALA A CB  1 
ATOM   529  N  N   . GLY A 1 69  ? 8.006   35.049 50.417  1.00 22.54 ? 69  GLY A N   1 
ATOM   530  C  CA  . GLY A 1 69  ? 8.359   35.504 51.757  1.00 22.34 ? 69  GLY A CA  1 
ATOM   531  C  C   . GLY A 1 69  ? 9.093   34.463 52.578  1.00 22.32 ? 69  GLY A C   1 
ATOM   532  O  O   . GLY A 1 69  ? 9.820   34.806 53.516  1.00 22.41 ? 69  GLY A O   1 
ATOM   533  N  N   . LEU A 1 70  ? 8.908   33.190 52.224  1.00 22.26 ? 70  LEU A N   1 
ATOM   534  C  CA  . LEU A 1 70  ? 9.481   32.079 52.985  1.00 22.21 ? 70  LEU A CA  1 
ATOM   535  C  C   . LEU A 1 70  ? 10.982  31.943 52.776  1.00 22.33 ? 70  LEU A C   1 
ATOM   536  O  O   . LEU A 1 70  ? 11.542  32.538 51.865  1.00 22.44 ? 70  LEU A O   1 
ATOM   537  C  CB  . LEU A 1 70  ? 8.809   30.769 52.594  1.00 22.01 ? 70  LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 70  ? 7.291   30.680 52.457  1.00 22.20 ? 70  LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 70  ? 6.906   29.316 51.878  1.00 21.73 ? 70  LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 70  ? 6.581   30.935 53.786  1.00 22.07 ? 70  LEU A CD2 1 
ATOM   541  N  N   . ALA A 1 71  ? 11.632  31.155 53.626  1.00 22.62 ? 71  ALA A N   1 
ATOM   542  C  CA  . ALA A 1 71  ? 13.012  30.753 53.384  1.00 22.95 ? 71  ALA A CA  1 
ATOM   543  C  C   . ALA A 1 71  ? 13.065  29.785 52.188  1.00 23.29 ? 71  ALA A C   1 
ATOM   544  O  O   . ALA A 1 71  ? 12.103  29.057 51.937  1.00 23.17 ? 71  ALA A O   1 
ATOM   545  C  CB  . ALA A 1 71  ? 13.603  30.115 54.622  1.00 22.77 ? 71  ALA A CB  1 
ATOM   546  N  N   . PRO A 1 72  ? 14.187  29.776 51.440  1.00 23.65 ? 72  PRO A N   1 
ATOM   547  C  CA  . PRO A 1 72  ? 15.372  30.598 51.683  1.00 23.81 ? 72  PRO A CA  1 
ATOM   548  C  C   . PRO A 1 72  ? 15.325  31.904 50.912  1.00 23.87 ? 72  PRO A C   1 
ATOM   549  O  O   . PRO A 1 72  ? 16.359  32.525 50.708  1.00 24.27 ? 72  PRO A O   1 
ATOM   550  C  CB  . PRO A 1 72  ? 16.514  29.715 51.162  1.00 23.74 ? 72  PRO A CB  1 
ATOM   551  C  CG  . PRO A 1 72  ? 15.870  28.840 50.091  1.00 23.74 ? 72  PRO A CG  1 
ATOM   552  C  CD  . PRO A 1 72  ? 14.363  28.902 50.263  1.00 23.56 ? 72  PRO A CD  1 
ATOM   553  N  N   . TYR A 1 73  ? 14.137  32.317 50.493  1.00 23.89 ? 73  TYR A N   1 
ATOM   554  C  CA  . TYR A 1 73  ? 14.005  33.486 49.627  1.00 24.36 ? 73  TYR A CA  1 
ATOM   555  C  C   . TYR A 1 73  ? 13.926  34.812 50.393  1.00 24.69 ? 73  TYR A C   1 
ATOM   556  O  O   . TYR A 1 73  ? 14.785  35.675 50.224  1.00 24.83 ? 73  TYR A O   1 
ATOM   557  C  CB  . TYR A 1 73  ? 12.818  33.317 48.674  1.00 24.29 ? 73  TYR A CB  1 
ATOM   558  C  CG  . TYR A 1 73  ? 12.762  31.957 47.996  1.00 24.19 ? 73  TYR A CG  1 
ATOM   559  C  CD1 . TYR A 1 73  ? 13.885  31.423 47.365  1.00 23.35 ? 73  TYR A CD1 1 
ATOM   560  C  CD2 . TYR A 1 73  ? 11.579  31.213 47.969  1.00 23.82 ? 73  TYR A CD2 1 
ATOM   561  C  CE1 . TYR A 1 73  ? 13.841  30.192 46.741  1.00 22.95 ? 73  TYR A CE1 1 
ATOM   562  C  CE2 . TYR A 1 73  ? 11.528  29.971 47.336  1.00 23.51 ? 73  TYR A CE2 1 
ATOM   563  C  CZ  . TYR A 1 73  ? 12.669  29.477 46.727  1.00 23.42 ? 73  TYR A CZ  1 
ATOM   564  O  OH  . TYR A 1 73  ? 12.646  28.265 46.097  1.00 24.59 ? 73  TYR A OH  1 
ATOM   565  N  N   . LYS A 1 74  ? 12.904  34.963 51.235  1.00 25.15 ? 74  LYS A N   1 
ATOM   566  C  CA  . LYS A 1 74  ? 12.731  36.157 52.076  1.00 25.58 ? 74  LYS A CA  1 
ATOM   567  C  C   . LYS A 1 74  ? 12.679  37.459 51.266  1.00 25.43 ? 74  LYS A C   1 
ATOM   568  O  O   . LYS A 1 74  ? 13.479  38.374 51.458  1.00 25.44 ? 74  LYS A O   1 
ATOM   569  C  CB  . LYS A 1 74  ? 13.806  36.215 53.167  1.00 25.75 ? 74  LYS A CB  1 
ATOM   570  C  CG  . LYS A 1 74  ? 13.765  35.046 54.139  1.00 27.24 ? 74  LYS A CG  1 
ATOM   571  C  CD  . LYS A 1 74  ? 12.643  35.211 55.171  1.00 30.06 ? 74  LYS A CD  1 
ATOM   572  C  CE  . LYS A 1 74  ? 12.840  34.302 56.394  1.00 31.29 ? 74  LYS A CE  1 
ATOM   573  N  NZ  . LYS A 1 74  ? 14.190  34.476 57.020  1.00 31.84 ? 74  LYS A NZ  1 
ATOM   574  N  N   . LEU A 1 75  ? 11.727  37.516 50.345  1.00 25.31 ? 75  LEU A N   1 
ATOM   575  C  CA  . LEU A 1 75  ? 11.506  38.703 49.538  1.00 25.13 ? 75  LEU A CA  1 
ATOM   576  C  C   . LEU A 1 75  ? 10.358  39.511 50.129  1.00 24.94 ? 75  LEU A C   1 
ATOM   577  O  O   . LEU A 1 75  ? 9.475   38.961 50.789  1.00 24.87 ? 75  LEU A O   1 
ATOM   578  C  CB  . LEU A 1 75  ? 11.213  38.327 48.077  1.00 25.02 ? 75  LEU A CB  1 
ATOM   579  C  CG  . LEU A 1 75  ? 12.218  37.458 47.311  1.00 25.30 ? 75  LEU A CG  1 
ATOM   580  C  CD1 . LEU A 1 75  ? 11.890  37.441 45.822  1.00 25.35 ? 75  LEU A CD1 1 
ATOM   581  C  CD2 . LEU A 1 75  ? 13.656  37.911 47.523  1.00 25.86 ? 75  LEU A CD2 1 
ATOM   582  N  N   . ARG A 1 76  ? 10.377  40.817 49.898  1.00 24.75 ? 76  ARG A N   1 
ATOM   583  C  CA  . ARG A 1 76  ? 9.327   41.681 50.408  1.00 24.96 ? 76  ARG A CA  1 
ATOM   584  C  C   . ARG A 1 76  ? 8.694   42.498 49.288  1.00 24.57 ? 76  ARG A C   1 
ATOM   585  O  O   . ARG A 1 76  ? 9.353   42.792 48.294  1.00 24.63 ? 76  ARG A O   1 
ATOM   586  C  CB  . ARG A 1 76  ? 9.850   42.583 51.537  1.00 24.99 ? 76  ARG A CB  1 
ATOM   587  C  CG  . ARG A 1 76  ? 10.946  43.565 51.153  1.00 25.53 ? 76  ARG A CG  1 
ATOM   588  C  CD  . ARG A 1 76  ? 11.278  44.496 52.312  1.00 26.05 ? 76  ARG A CD  1 
ATOM   589  N  NE  . ARG A 1 76  ? 10.124  45.298 52.710  1.00 28.97 ? 76  ARG A NE  1 
ATOM   590  C  CZ  . ARG A 1 76  ? 9.817   46.492 52.206  1.00 30.45 ? 76  ARG A CZ  1 
ATOM   591  N  NH1 . ARG A 1 76  ? 10.586  47.052 51.275  1.00 31.48 ? 76  ARG A NH1 1 
ATOM   592  N  NH2 . ARG A 1 76  ? 8.735   47.133 52.637  1.00 31.11 ? 76  ARG A NH2 1 
ATOM   593  N  N   . PRO A 1 77  ? 7.398   42.831 49.429  1.00 24.21 ? 77  PRO A N   1 
ATOM   594  C  CA  . PRO A 1 77  ? 6.757   43.710 48.472  1.00 23.91 ? 77  PRO A CA  1 
ATOM   595  C  C   . PRO A 1 77  ? 7.279   45.105 48.690  1.00 23.95 ? 77  PRO A C   1 
ATOM   596  O  O   . PRO A 1 77  ? 7.359   45.554 49.839  1.00 23.99 ? 77  PRO A O   1 
ATOM   597  C  CB  . PRO A 1 77  ? 5.282   43.653 48.872  1.00 23.87 ? 77  PRO A CB  1 
ATOM   598  C  CG  . PRO A 1 77  ? 5.154   42.471 49.752  1.00 24.20 ? 77  PRO A CG  1 
ATOM   599  C  CD  . PRO A 1 77  ? 6.456   42.387 50.465  1.00 24.09 ? 77  PRO A CD  1 
ATOM   600  N  N   . VAL A 1 78  ? 7.648   45.768 47.596  1.00 23.93 ? 78  VAL A N   1 
ATOM   601  C  CA  . VAL A 1 78  ? 8.202   47.125 47.636  1.00 23.74 ? 78  VAL A CA  1 
ATOM   602  C  C   . VAL A 1 78  ? 7.236   48.144 47.027  1.00 23.83 ? 78  VAL A C   1 
ATOM   603  O  O   . VAL A 1 78  ? 7.250   49.320 47.392  1.00 23.78 ? 78  VAL A O   1 
ATOM   604  C  CB  . VAL A 1 78  ? 9.587   47.214 46.933  1.00 23.72 ? 78  VAL A CB  1 
ATOM   605  C  CG1 . VAL A 1 78  ? 10.627  46.372 47.671  1.00 23.72 ? 78  VAL A CG1 1 
ATOM   606  C  CG2 . VAL A 1 78  ? 9.498   46.789 45.479  1.00 23.31 ? 78  VAL A CG2 1 
ATOM   607  N  N   . ALA A 1 79  ? 6.387   47.682 46.114  1.00 23.85 ? 79  ALA A N   1 
ATOM   608  C  CA  . ALA A 1 79  ? 5.454   48.557 45.421  1.00 23.99 ? 79  ALA A CA  1 
ATOM   609  C  C   . ALA A 1 79  ? 4.215   47.791 45.003  1.00 24.21 ? 79  ALA A C   1 
ATOM   610  O  O   . ALA A 1 79  ? 4.306   46.732 44.396  1.00 24.42 ? 79  ALA A O   1 
ATOM   611  C  CB  . ALA A 1 79  ? 6.117   49.177 44.220  1.00 23.90 ? 79  ALA A CB  1 
ATOM   612  N  N   . ALA A 1 80  ? 3.054   48.337 45.333  1.00 24.71 ? 80  ALA A N   1 
ATOM   613  C  CA  . ALA A 1 80  ? 1.790   47.683 45.035  1.00 25.32 ? 80  ALA A CA  1 
ATOM   614  C  C   . ALA A 1 80  ? 1.170   48.236 43.758  1.00 25.98 ? 80  ALA A C   1 
ATOM   615  O  O   . ALA A 1 80  ? 1.352   49.412 43.427  1.00 26.34 ? 80  ALA A O   1 
ATOM   616  C  CB  . ALA A 1 80  ? 0.847   47.862 46.187  1.00 25.23 ? 80  ALA A CB  1 
ATOM   617  N  N   . GLU A 1 81  ? 0.441   47.396 43.032  1.00 26.42 ? 81  GLU A N   1 
ATOM   618  C  CA  . GLU A 1 81  ? -0.337  47.897 41.908  1.00 27.25 ? 81  GLU A CA  1 
ATOM   619  C  C   . GLU A 1 81  ? -1.564  48.647 42.404  1.00 27.03 ? 81  GLU A C   1 
ATOM   620  O  O   . GLU A 1 81  ? -2.149  48.313 43.442  1.00 27.18 ? 81  GLU A O   1 
ATOM   621  C  CB  . GLU A 1 81  ? -0.730  46.783 40.944  1.00 27.10 ? 81  GLU A CB  1 
ATOM   622  C  CG  . GLU A 1 81  ? 0.315   46.518 39.865  1.00 28.28 ? 81  GLU A CG  1 
ATOM   623  C  CD  . GLU A 1 81  ? 0.008   45.293 39.005  1.00 29.23 ? 81  GLU A CD  1 
ATOM   624  O  OE1 . GLU A 1 81  ? -1.046  44.631 39.213  1.00 31.79 ? 81  GLU A OE1 1 
ATOM   625  O  OE2 . GLU A 1 81  ? 0.835   44.989 38.115  1.00 32.14 ? 81  GLU A OE2 1 
ATOM   626  N  N   . VAL A 1 82  ? -1.921  49.683 41.664  1.00 26.89 ? 82  VAL A N   1 
ATOM   627  C  CA  . VAL A 1 82  ? -3.052  50.504 41.985  1.00 27.04 ? 82  VAL A CA  1 
ATOM   628  C  C   . VAL A 1 82  ? -4.058  50.278 40.872  1.00 27.74 ? 82  VAL A C   1 
ATOM   629  O  O   . VAL A 1 82  ? -3.773  50.556 39.703  1.00 28.16 ? 82  VAL A O   1 
ATOM   630  C  CB  . VAL A 1 82  ? -2.632  51.975 42.039  1.00 26.91 ? 82  VAL A CB  1 
ATOM   631  C  CG1 . VAL A 1 82  ? -3.833  52.881 42.226  1.00 26.97 ? 82  VAL A CG1 1 
ATOM   632  C  CG2 . VAL A 1 82  ? -1.621  52.189 43.141  1.00 26.76 ? 82  VAL A CG2 1 
ATOM   633  N  N   . TYR A 1 83  ? -5.226  49.747 41.221  1.00 28.29 ? 83  TYR A N   1 
ATOM   634  C  CA  . TYR A 1 83  ? -6.281  49.527 40.234  1.00 28.59 ? 83  TYR A CA  1 
ATOM   635  C  C   . TYR A 1 83  ? -7.351  50.585 40.380  1.00 29.57 ? 83  TYR A C   1 
ATOM   636  O  O   . TYR A 1 83  ? -7.252  51.462 41.245  1.00 29.69 ? 83  TYR A O   1 
ATOM   637  C  CB  . TYR A 1 83  ? -6.911  48.149 40.397  1.00 27.92 ? 83  TYR A CB  1 
ATOM   638  C  CG  . TYR A 1 83  ? -5.928  47.024 40.595  1.00 27.24 ? 83  TYR A CG  1 
ATOM   639  C  CD1 . TYR A 1 83  ? -4.888  46.806 39.693  1.00 25.96 ? 83  TYR A CD1 1 
ATOM   640  C  CD2 . TYR A 1 83  ? -6.060  46.154 41.677  1.00 26.85 ? 83  TYR A CD2 1 
ATOM   641  C  CE1 . TYR A 1 83  ? -3.995  45.763 39.876  1.00 26.55 ? 83  TYR A CE1 1 
ATOM   642  C  CE2 . TYR A 1 83  ? -5.176  45.109 41.866  1.00 26.77 ? 83  TYR A CE2 1 
ATOM   643  C  CZ  . TYR A 1 83  ? -4.146  44.920 40.967  1.00 27.13 ? 83  TYR A CZ  1 
ATOM   644  O  OH  . TYR A 1 83  ? -3.269  43.888 41.170  1.00 27.29 ? 83  TYR A OH  1 
ATOM   645  N  N   . GLY A 1 84  ? -8.376  50.488 39.535  1.00 30.78 ? 84  GLY A N   1 
ATOM   646  C  CA  . GLY A 1 84  ? -9.540  51.373 39.593  1.00 31.72 ? 84  GLY A CA  1 
ATOM   647  C  C   . GLY A 1 84  ? -9.439  52.507 38.599  1.00 32.59 ? 84  GLY A C   1 
ATOM   648  O  O   . GLY A 1 84  ? -9.223  52.283 37.408  1.00 32.67 ? 84  GLY A O   1 
ATOM   649  N  N   . THR A 1 85  ? -9.595  53.728 39.096  1.00 33.54 ? 85  THR A N   1 
ATOM   650  C  CA  . THR A 1 85  ? -9.549  54.924 38.258  1.00 34.63 ? 85  THR A CA  1 
ATOM   651  C  C   . THR A 1 85  ? -8.812  56.032 38.980  1.00 35.16 ? 85  THR A C   1 
ATOM   652  O  O   . THR A 1 85  ? -8.721  56.019 40.212  1.00 35.42 ? 85  THR A O   1 
ATOM   653  C  CB  . THR A 1 85  ? -10.952 55.428 37.928  1.00 34.76 ? 85  THR A CB  1 
ATOM   654  O  OG1 . THR A 1 85  ? -11.788 55.278 39.085  1.00 34.99 ? 85  THR A OG1 1 
ATOM   655  C  CG2 . THR A 1 85  ? -11.540 54.640 36.754  1.00 35.23 ? 85  THR A CG2 1 
ATOM   656  N  N   . GLU A 1 86  ? -8.303  56.999 38.220  1.00 35.74 ? 86  GLU A N   1 
ATOM   657  C  CA  . GLU A 1 86  ? -7.434  58.024 38.795  1.00 36.35 ? 86  GLU A CA  1 
ATOM   658  C  C   . GLU A 1 86  ? -8.077  58.747 39.988  1.00 36.20 ? 86  GLU A C   1 
ATOM   659  O  O   . GLU A 1 86  ? -7.386  59.109 40.948  1.00 36.14 ? 86  GLU A O   1 
ATOM   660  C  CB  . GLU A 1 86  ? -6.964  59.024 37.736  1.00 36.47 ? 86  GLU A CB  1 
ATOM   661  C  CG  . GLU A 1 86  ? -5.495  59.421 37.904  1.00 38.06 ? 86  GLU A CG  1 
ATOM   662  C  CD  . GLU A 1 86  ? -5.300  60.925 38.065  1.00 40.15 ? 86  GLU A CD  1 
ATOM   663  O  OE1 . GLU A 1 86  ? -4.709  61.560 37.158  1.00 40.23 ? 86  GLU A OE1 1 
ATOM   664  O  OE2 . GLU A 1 86  ? -5.745  61.470 39.104  1.00 40.94 ? 86  GLU A OE2 1 
ATOM   665  N  N   . ARG A 1 87  ? -9.396  58.921 39.929  1.00 36.20 ? 87  ARG A N   1 
ATOM   666  C  CA  . ARG A 1 87  ? -10.130 59.659 40.960  1.00 36.23 ? 87  ARG A CA  1 
ATOM   667  C  C   . ARG A 1 87  ? -10.623 58.775 42.107  1.00 35.69 ? 87  ARG A C   1 
ATOM   668  O  O   . ARG A 1 87  ? -10.855 59.264 43.211  1.00 35.58 ? 87  ARG A O   1 
ATOM   669  C  CB  . ARG A 1 87  ? -11.286 60.455 40.336  1.00 36.61 ? 87  ARG A CB  1 
ATOM   670  C  CG  . ARG A 1 87  ? -12.546 59.646 39.975  1.00 38.14 ? 87  ARG A CG  1 
ATOM   671  C  CD  . ARG A 1 87  ? -13.262 60.204 38.720  1.00 41.15 ? 87  ARG A CD  1 
ATOM   672  N  NE  . ARG A 1 87  ? -13.175 61.668 38.581  1.00 42.43 ? 87  ARG A NE  1 
ATOM   673  C  CZ  . ARG A 1 87  ? -13.735 62.379 37.599  1.00 42.71 ? 87  ARG A CZ  1 
ATOM   674  N  NH1 . ARG A 1 87  ? -14.444 61.777 36.651  1.00 43.08 ? 87  ARG A NH1 1 
ATOM   675  N  NH2 . ARG A 1 87  ? -13.590 63.700 37.567  1.00 42.56 ? 87  ARG A NH2 1 
ATOM   676  N  N   . GLN A 1 88  ? -10.764 57.478 41.832  1.00 35.03 ? 88  GLN A N   1 
ATOM   677  C  CA  . GLN A 1 88  ? -11.227 56.495 42.807  1.00 34.24 ? 88  GLN A CA  1 
ATOM   678  C  C   . GLN A 1 88  ? -10.320 55.236 42.716  1.00 33.49 ? 88  GLN A C   1 
ATOM   679  O  O   . GLN A 1 88  ? -10.698 54.217 42.128  1.00 33.25 ? 88  GLN A O   1 
ATOM   680  C  CB  . GLN A 1 88  ? -12.721 56.204 42.565  1.00 34.30 ? 88  GLN A CB  1 
ATOM   681  C  CG  . GLN A 1 88  ? -13.402 55.222 43.533  1.00 35.73 ? 88  GLN A CG  1 
ATOM   682  C  CD  . GLN A 1 88  ? -13.750 55.823 44.892  1.00 37.26 ? 88  GLN A CD  1 
ATOM   683  O  OE1 . GLN A 1 88  ? -14.385 56.878 44.983  1.00 38.03 ? 88  GLN A OE1 1 
ATOM   684  N  NE2 . GLN A 1 88  ? -13.354 55.132 45.958  1.00 37.15 ? 88  GLN A NE2 1 
ATOM   685  N  N   . PRO A 1 89  ? -9.103  55.322 43.291  1.00 32.82 ? 89  PRO A N   1 
ATOM   686  C  CA  . PRO A 1 89  ? -8.063  54.302 43.158  1.00 32.48 ? 89  PRO A CA  1 
ATOM   687  C  C   . PRO A 1 89  ? -8.095  53.202 44.224  1.00 32.03 ? 89  PRO A C   1 
ATOM   688  O  O   . PRO A 1 89  ? -8.259  53.497 45.404  1.00 31.95 ? 89  PRO A O   1 
ATOM   689  C  CB  . PRO A 1 89  ? -6.767  55.115 43.287  1.00 32.57 ? 89  PRO A CB  1 
ATOM   690  C  CG  . PRO A 1 89  ? -7.149  56.390 43.992  1.00 32.37 ? 89  PRO A CG  1 
ATOM   691  C  CD  . PRO A 1 89  ? -8.642  56.446 44.124  1.00 32.76 ? 89  PRO A CD  1 
ATOM   692  N  N   . ARG A 1 90  ? -7.903  51.952 43.800  1.00 31.48 ? 90  ARG A N   1 
ATOM   693  C  CA  . ARG A 1 90  ? -7.997  50.788 44.688  1.00 31.06 ? 90  ARG A CA  1 
ATOM   694  C  C   . ARG A 1 90  ? -6.649  50.094 44.862  1.00 29.88 ? 90  ARG A C   1 
ATOM   695  O  O   . ARG A 1 90  ? -5.896  49.944 43.900  1.00 29.83 ? 90  ARG A O   1 
ATOM   696  C  CB  . ARG A 1 90  ? -9.000  49.761 44.143  1.00 31.53 ? 90  ARG A CB  1 
ATOM   697  C  CG  . ARG A 1 90  ? -10.383 50.298 43.710  1.00 34.47 ? 90  ARG A CG  1 
ATOM   698  C  CD  . ARG A 1 90  ? -11.581 49.955 44.659  1.00 38.87 ? 90  ARG A CD  1 
ATOM   699  N  NE  . ARG A 1 90  ? -11.484 48.694 45.431  1.00 43.42 ? 90  ARG A NE  1 
ATOM   700  C  CZ  . ARG A 1 90  ? -11.363 47.451 44.934  1.00 45.34 ? 90  ARG A CZ  1 
ATOM   701  N  NH1 . ARG A 1 90  ? -11.301 46.417 45.774  1.00 45.90 ? 90  ARG A NH1 1 
ATOM   702  N  NH2 . ARG A 1 90  ? -11.279 47.222 43.619  1.00 45.57 ? 90  ARG A NH2 1 
ATOM   703  N  N   . THR A 1 91  ? -6.357  49.662 46.087  1.00 28.48 ? 91  THR A N   1 
ATOM   704  C  CA  . THR A 1 91  ? -5.134  48.905 46.385  1.00 27.31 ? 91  THR A CA  1 
ATOM   705  C  C   . THR A 1 91  ? -5.461  47.456 46.746  1.00 26.36 ? 91  THR A C   1 
ATOM   706  O  O   . THR A 1 91  ? -4.588  46.676 47.136  1.00 26.16 ? 91  THR A O   1 
ATOM   707  C  CB  . THR A 1 91  ? -4.301  49.564 47.506  1.00 27.37 ? 91  THR A CB  1 
ATOM   708  O  OG1 . THR A 1 91  ? -5.174  50.078 48.517  1.00 27.66 ? 91  THR A OG1 1 
ATOM   709  C  CG2 . THR A 1 91  ? -3.462  50.709 46.945  1.00 27.11 ? 91  THR A CG2 1 
ATOM   710  N  N   . HIS A 1 92  ? -6.736  47.114 46.587  1.00 25.22 ? 92  HIS A N   1 
ATOM   711  C  CA  . HIS A 1 92  ? -7.260  45.796 46.900  1.00 23.93 ? 92  HIS A CA  1 
ATOM   712  C  C   . HIS A 1 92  ? -8.066  45.325 45.706  1.00 23.23 ? 92  HIS A C   1 
ATOM   713  O  O   . HIS A 1 92  ? -8.331  46.105 44.786  1.00 23.32 ? 92  HIS A O   1 
ATOM   714  C  CB  . HIS A 1 92  ? -8.162  45.859 48.143  1.00 24.03 ? 92  HIS A CB  1 
ATOM   715  C  CG  . HIS A 1 92  ? -7.455  46.290 49.396  1.00 23.65 ? 92  HIS A CG  1 
ATOM   716  N  ND1 . HIS A 1 92  ? -7.107  47.600 49.648  1.00 22.90 ? 92  HIS A ND1 1 
ATOM   717  C  CD2 . HIS A 1 92  ? -7.039  45.583 50.472  1.00 24.75 ? 92  HIS A CD2 1 
ATOM   718  C  CE1 . HIS A 1 92  ? -6.502  47.679 50.820  1.00 24.20 ? 92  HIS A CE1 1 
ATOM   719  N  NE2 . HIS A 1 92  ? -6.455  46.470 51.348  1.00 25.08 ? 92  HIS A NE2 1 
ATOM   720  N  N   . TYR A 1 93  ? -8.425  44.044 45.704  1.00 22.22 ? 93  TYR A N   1 
ATOM   721  C  CA  . TYR A 1 93  ? -9.402  43.520 44.757  1.00 21.32 ? 93  TYR A CA  1 
ATOM   722  C  C   . TYR A 1 93  ? -10.227 42.422 45.383  1.00 21.11 ? 93  TYR A C   1 
ATOM   723  O  O   . TYR A 1 93  ? -9.855  41.867 46.422  1.00 21.26 ? 93  TYR A O   1 
ATOM   724  C  CB  . TYR A 1 93  ? -8.770  43.070 43.432  1.00 21.03 ? 93  TYR A CB  1 
ATOM   725  C  CG  . TYR A 1 93  ? -7.787  41.919 43.472  1.00 20.49 ? 93  TYR A CG  1 
ATOM   726  C  CD1 . TYR A 1 93  ? -6.466  42.117 43.874  1.00 19.70 ? 93  TYR A CD1 1 
ATOM   727  C  CD2 . TYR A 1 93  ? -8.161  40.639 43.047  1.00 19.89 ? 93  TYR A CD2 1 
ATOM   728  C  CE1 . TYR A 1 93  ? -5.552  41.062 43.886  1.00 19.87 ? 93  TYR A CE1 1 
ATOM   729  C  CE2 . TYR A 1 93  ? -7.245  39.570 43.051  1.00 18.93 ? 93  TYR A CE2 1 
ATOM   730  C  CZ  . TYR A 1 93  ? -5.944  39.794 43.468  1.00 19.95 ? 93  TYR A CZ  1 
ATOM   731  O  OH  . TYR A 1 93  ? -5.022  38.765 43.487  1.00 20.67 ? 93  TYR A OH  1 
ATOM   732  N  N   . TYR A 1 94  ? -11.362 42.128 44.762  1.00 20.83 ? 94  TYR A N   1 
ATOM   733  C  CA  . TYR A 1 94  ? -12.251 41.104 45.268  1.00 20.48 ? 94  TYR A CA  1 
ATOM   734  C  C   . TYR A 1 94  ? -12.071 39.873 44.441  1.00 20.63 ? 94  TYR A C   1 
ATOM   735  O  O   . TYR A 1 94  ? -12.068 39.937 43.210  1.00 20.62 ? 94  TYR A O   1 
ATOM   736  C  CB  . TYR A 1 94  ? -13.700 41.549 45.199  1.00 20.28 ? 94  TYR A CB  1 
ATOM   737  C  CG  . TYR A 1 94  ? -14.009 42.732 46.075  1.00 20.39 ? 94  TYR A CG  1 
ATOM   738  C  CD1 . TYR A 1 94  ? -14.093 44.013 45.540  1.00 20.41 ? 94  TYR A CD1 1 
ATOM   739  C  CD2 . TYR A 1 94  ? -14.205 42.579 47.439  1.00 19.44 ? 94  TYR A CD2 1 
ATOM   740  C  CE1 . TYR A 1 94  ? -14.372 45.108 46.342  1.00 20.18 ? 94  TYR A CE1 1 
ATOM   741  C  CE2 . TYR A 1 94  ? -14.493 43.661 48.241  1.00 20.18 ? 94  TYR A CE2 1 
ATOM   742  C  CZ  . TYR A 1 94  ? -14.575 44.929 47.689  1.00 20.18 ? 94  TYR A CZ  1 
ATOM   743  O  OH  . TYR A 1 94  ? -14.857 46.019 48.489  1.00 20.25 ? 94  TYR A OH  1 
ATOM   744  N  N   . ALA A 1 95  ? -11.880 38.755 45.129  1.00 20.76 ? 95  ALA A N   1 
ATOM   745  C  CA  . ALA A 1 95  ? -11.939 37.459 44.497  1.00 21.11 ? 95  ALA A CA  1 
ATOM   746  C  C   . ALA A 1 95  ? -13.399 37.018 44.523  1.00 21.39 ? 95  ALA A C   1 
ATOM   747  O  O   . ALA A 1 95  ? -14.053 37.048 45.579  1.00 21.48 ? 95  ALA A O   1 
ATOM   748  C  CB  . ALA A 1 95  ? -11.072 36.481 45.236  1.00 21.15 ? 95  ALA A CB  1 
ATOM   749  N  N   . VAL A 1 96  ? -13.912 36.643 43.356  1.00 21.46 ? 96  VAL A N   1 
ATOM   750  C  CA  . VAL A 1 96  ? -15.307 36.225 43.214  1.00 21.85 ? 96  VAL A CA  1 
ATOM   751  C  C   . VAL A 1 96  ? -15.423 34.834 42.566  1.00 22.10 ? 96  VAL A C   1 
ATOM   752  O  O   . VAL A 1 96  ? -14.444 34.297 42.016  1.00 22.10 ? 96  VAL A O   1 
ATOM   753  C  CB  . VAL A 1 96  ? -16.135 37.249 42.374  1.00 21.90 ? 96  VAL A CB  1 
ATOM   754  C  CG1 . VAL A 1 96  ? -16.202 38.616 43.049  1.00 21.30 ? 96  VAL A CG1 1 
ATOM   755  C  CG2 . VAL A 1 96  ? -15.577 37.368 40.957  1.00 21.92 ? 96  VAL A CG2 1 
ATOM   756  N  N   . ALA A 1 97  ? -16.621 34.257 42.627  1.00 22.09 ? 97  ALA A N   1 
ATOM   757  C  CA  . ALA A 1 97  ? -16.910 33.049 41.867  1.00 22.20 ? 97  ALA A CA  1 
ATOM   758  C  C   . ALA A 1 97  ? -18.022 33.314 40.844  1.00 22.45 ? 97  ALA A C   1 
ATOM   759  O  O   . ALA A 1 97  ? -19.153 33.623 41.208  1.00 21.92 ? 97  ALA A O   1 
ATOM   760  C  CB  . ALA A 1 97  ? -17.264 31.920 42.790  1.00 22.07 ? 97  ALA A CB  1 
ATOM   761  N  N   . VAL A 1 98  ? -17.677 33.193 39.563  1.00 23.17 ? 98  VAL A N   1 
ATOM   762  C  CA  . VAL A 1 98  ? -18.567 33.562 38.462  1.00 24.19 ? 98  VAL A CA  1 
ATOM   763  C  C   . VAL A 1 98  ? -19.241 32.342 37.831  1.00 24.90 ? 98  VAL A C   1 
ATOM   764  O  O   . VAL A 1 98  ? -18.571 31.402 37.402  1.00 25.11 ? 98  VAL A O   1 
ATOM   765  C  CB  . VAL A 1 98  ? -17.802 34.356 37.377  1.00 24.21 ? 98  VAL A CB  1 
ATOM   766  C  CG1 . VAL A 1 98  ? -18.699 34.666 36.185  1.00 24.62 ? 98  VAL A CG1 1 
ATOM   767  C  CG2 . VAL A 1 98  ? -17.252 35.643 37.956  1.00 24.22 ? 98  VAL A CG2 1 
ATOM   768  N  N   . VAL A 1 99  ? -20.571 32.369 37.781  1.00 25.77 ? 99  VAL A N   1 
ATOM   769  C  CA  . VAL A 1 99  ? -21.368 31.260 37.239  1.00 26.34 ? 99  VAL A CA  1 
ATOM   770  C  C   . VAL A 1 99  ? -22.280 31.743 36.127  1.00 27.33 ? 99  VAL A C   1 
ATOM   771  O  O   . VAL A 1 99  ? -22.479 32.949 35.965  1.00 27.69 ? 99  VAL A O   1 
ATOM   772  C  CB  . VAL A 1 99  ? -22.226 30.577 38.322  1.00 25.87 ? 99  VAL A CB  1 
ATOM   773  C  CG1 . VAL A 1 99  ? -21.341 29.937 39.355  1.00 25.93 ? 99  VAL A CG1 1 
ATOM   774  C  CG2 . VAL A 1 99  ? -23.169 31.561 38.975  1.00 25.51 ? 99  VAL A CG2 1 
ATOM   775  N  N   . LYS A 1 100 ? -22.832 30.809 35.357  1.00 28.51 ? 100 LYS A N   1 
ATOM   776  C  CA  . LYS A 1 100 ? -23.794 31.163 34.316  1.00 29.60 ? 100 LYS A CA  1 
ATOM   777  C  C   . LYS A 1 100 ? -25.178 31.395 34.916  1.00 30.13 ? 100 LYS A C   1 
ATOM   778  O  O   . LYS A 1 100 ? -25.619 30.651 35.805  1.00 30.11 ? 100 LYS A O   1 
ATOM   779  C  CB  . LYS A 1 100 ? -23.857 30.076 33.248  1.00 29.71 ? 100 LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 100 ? -22.780 30.177 32.182  1.00 31.15 ? 100 LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 100 ? -22.716 28.890 31.346  1.00 33.43 ? 100 LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 100 ? -21.691 28.992 30.209  1.00 33.76 ? 100 LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 100 ? -22.215 29.754 29.039  1.00 34.16 ? 100 LYS A NZ  1 
ATOM   784  N  N   . LYS A 1 101 ? -25.852 32.437 34.443  1.00 30.88 ? 101 LYS A N   1 
ATOM   785  C  CA  . LYS A 1 101 ? -27.235 32.671 34.829  1.00 31.93 ? 101 LYS A CA  1 
ATOM   786  C  C   . LYS A 1 101 ? -28.137 31.582 34.223  1.00 32.22 ? 101 LYS A C   1 
ATOM   787  O  O   . LYS A 1 101 ? -27.948 31.171 33.072  1.00 32.17 ? 101 LYS A O   1 
ATOM   788  C  CB  . LYS A 1 101 ? -27.694 34.070 34.407  1.00 31.89 ? 101 LYS A CB  1 
ATOM   789  C  CG  . LYS A 1 101 ? -29.034 34.485 35.020  1.00 32.62 ? 101 LYS A CG  1 
ATOM   790  C  CD  . LYS A 1 101 ? -29.368 35.946 34.748  1.00 32.69 ? 101 LYS A CD  1 
ATOM   791  C  CE  . LYS A 1 101 ? -30.641 36.354 35.482  1.00 34.23 ? 101 LYS A CE  1 
ATOM   792  N  NZ  . LYS A 1 101 ? -31.034 37.761 35.179  1.00 34.90 ? 101 LYS A NZ  1 
ATOM   793  N  N   . GLY A 1 102 ? -29.100 31.111 35.012  1.00 32.64 ? 102 GLY A N   1 
ATOM   794  C  CA  . GLY A 1 102 ? -29.986 30.032 34.585  1.00 33.15 ? 102 GLY A CA  1 
ATOM   795  C  C   . GLY A 1 102 ? -30.053 28.900 35.592  1.00 33.50 ? 102 GLY A C   1 
ATOM   796  O  O   . GLY A 1 102 ? -31.141 28.449 35.950  1.00 33.61 ? 102 GLY A O   1 
ATOM   797  N  N   . GLY A 1 103 ? -28.890 28.438 36.050  1.00 33.77 ? 103 GLY A N   1 
ATOM   798  C  CA  . GLY A 1 103 ? -28.811 27.369 37.048  1.00 33.96 ? 103 GLY A CA  1 
ATOM   799  C  C   . GLY A 1 103 ? -29.223 27.867 38.417  1.00 34.18 ? 103 GLY A C   1 
ATOM   800  O  O   . GLY A 1 103 ? -29.487 29.058 38.596  1.00 34.19 ? 103 GLY A O   1 
ATOM   801  N  N   . SER A 1 104 ? -29.286 26.965 39.390  1.00 34.41 ? 104 SER A N   1 
ATOM   802  C  CA  . SER A 1 104 ? -29.635 27.372 40.751  1.00 34.73 ? 104 SER A CA  1 
ATOM   803  C  C   . SER A 1 104 ? -28.739 26.776 41.846  1.00 34.90 ? 104 SER A C   1 
ATOM   804  O  O   . SER A 1 104 ? -29.106 26.789 43.033  1.00 34.88 ? 104 SER A O   1 
ATOM   805  C  CB  . SER A 1 104 ? -31.118 27.117 41.038  1.00 34.77 ? 104 SER A CB  1 
ATOM   806  O  OG  . SER A 1 104 ? -31.461 25.774 40.763  1.00 35.26 ? 104 SER A OG  1 
ATOM   807  N  N   . PHE A 1 105 ? -27.565 26.272 41.452  1.00 34.86 ? 105 PHE A N   1 
ATOM   808  C  CA  . PHE A 1 105 ? -26.573 25.820 42.432  1.00 34.79 ? 105 PHE A CA  1 
ATOM   809  C  C   . PHE A 1 105 ? -25.939 26.999 43.165  1.00 35.06 ? 105 PHE A C   1 
ATOM   810  O  O   . PHE A 1 105 ? -25.688 28.049 42.566  1.00 35.14 ? 105 PHE A O   1 
ATOM   811  C  CB  . PHE A 1 105 ? -25.514 24.864 41.837  1.00 34.55 ? 105 PHE A CB  1 
ATOM   812  C  CG  . PHE A 1 105 ? -24.690 25.449 40.716  1.00 33.96 ? 105 PHE A CG  1 
ATOM   813  C  CD1 . PHE A 1 105 ? -23.562 26.209 40.985  1.00 32.89 ? 105 PHE A CD1 1 
ATOM   814  C  CD2 . PHE A 1 105 ? -25.023 25.196 39.386  1.00 33.74 ? 105 PHE A CD2 1 
ATOM   815  C  CE1 . PHE A 1 105 ? -22.803 26.733 39.954  1.00 32.88 ? 105 PHE A CE1 1 
ATOM   816  C  CE2 . PHE A 1 105 ? -24.267 25.718 38.346  1.00 33.07 ? 105 PHE A CE2 1 
ATOM   817  C  CZ  . PHE A 1 105 ? -23.155 26.488 38.629  1.00 33.49 ? 105 PHE A CZ  1 
ATOM   818  N  N   . GLN A 1 106 ? -25.720 26.820 44.466  1.00 35.20 ? 106 GLN A N   1 
ATOM   819  C  CA  . GLN A 1 106 ? -25.158 27.855 45.328  1.00 35.26 ? 106 GLN A CA  1 
ATOM   820  C  C   . GLN A 1 106 ? -23.744 27.479 45.748  1.00 35.39 ? 106 GLN A C   1 
ATOM   821  O  O   . GLN A 1 106 ? -23.285 26.383 45.440  1.00 35.58 ? 106 GLN A O   1 
ATOM   822  C  CB  . GLN A 1 106 ? -26.053 28.059 46.557  1.00 35.24 ? 106 GLN A CB  1 
ATOM   823  C  CG  . GLN A 1 106 ? -27.422 28.658 46.250  1.00 35.28 ? 106 GLN A CG  1 
ATOM   824  C  CD  . GLN A 1 106 ? -27.348 29.965 45.467  1.00 35.50 ? 106 GLN A CD  1 
ATOM   825  O  OE1 . GLN A 1 106 ? -26.395 30.736 45.598  1.00 36.31 ? 106 GLN A OE1 1 
ATOM   826  N  NE2 . GLN A 1 106 ? -28.358 30.215 44.648  1.00 35.42 ? 106 GLN A NE2 1 
ATOM   827  N  N   . LEU A 1 107 ? -23.054 28.375 46.453  1.00 35.45 ? 107 LEU A N   1 
ATOM   828  C  CA  . LEU A 1 107 ? -21.673 28.119 46.870  1.00 35.55 ? 107 LEU A CA  1 
ATOM   829  C  C   . LEU A 1 107 ? -21.483 26.811 47.650  1.00 35.52 ? 107 LEU A C   1 
ATOM   830  O  O   . LEU A 1 107 ? -20.390 26.249 47.668  1.00 35.63 ? 107 LEU A O   1 
ATOM   831  C  CB  . LEU A 1 107 ? -21.121 29.298 47.677  1.00 35.68 ? 107 LEU A CB  1 
ATOM   832  C  CG  . LEU A 1 107 ? -19.591 29.435 47.738  1.00 35.58 ? 107 LEU A CG  1 
ATOM   833  C  CD1 . LEU A 1 107 ? -19.012 29.859 46.395  1.00 35.10 ? 107 LEU A CD1 1 
ATOM   834  C  CD2 . LEU A 1 107 ? -19.185 30.417 48.816  1.00 35.60 ? 107 LEU A CD2 1 
ATOM   835  N  N   . ASN A 1 108 ? -22.544 26.330 48.283  1.00 35.53 ? 108 ASN A N   1 
ATOM   836  C  CA  . ASN A 1 108 ? -22.475 25.095 49.068  1.00 35.76 ? 108 ASN A CA  1 
ATOM   837  C  C   . ASN A 1 108 ? -22.870 23.846 48.284  1.00 35.84 ? 108 ASN A C   1 
ATOM   838  O  O   . ASN A 1 108 ? -22.911 22.744 48.833  1.00 35.80 ? 108 ASN A O   1 
ATOM   839  C  CB  . ASN A 1 108 ? -23.298 25.215 50.361  1.00 35.72 ? 108 ASN A CB  1 
ATOM   840  C  CG  . ASN A 1 108 ? -24.792 25.472 50.114  1.00 35.95 ? 108 ASN A CG  1 
ATOM   841  O  OD1 . ASN A 1 108 ? -25.580 25.426 51.055  1.00 36.29 ? 108 ASN A OD1 1 
ATOM   842  N  ND2 . ASN A 1 108 ? -25.181 25.748 48.867  1.00 35.61 ? 108 ASN A ND2 1 
ATOM   843  N  N   . GLU A 1 109 ? -23.150 24.032 46.998  1.00 35.90 ? 109 GLU A N   1 
ATOM   844  C  CA  . GLU A 1 109 ? -23.629 22.959 46.130  1.00 36.07 ? 109 GLU A CA  1 
ATOM   845  C  C   . GLU A 1 109 ? -22.704 22.779 44.935  1.00 35.45 ? 109 GLU A C   1 
ATOM   846  O  O   . GLU A 1 109 ? -23.160 22.525 43.818  1.00 35.50 ? 109 GLU A O   1 
ATOM   847  C  CB  . GLU A 1 109 ? -25.052 23.266 45.648  1.00 36.00 ? 109 GLU A CB  1 
ATOM   848  C  CG  . GLU A 1 109 ? -26.101 23.303 46.765  1.00 37.42 ? 109 GLU A CG  1 
ATOM   849  C  CD  . GLU A 1 109 ? -27.379 24.041 46.381  1.00 37.52 ? 109 GLU A CD  1 
ATOM   850  O  OE1 . GLU A 1 109 ? -27.429 24.609 45.265  1.00 39.03 ? 109 GLU A OE1 1 
ATOM   851  O  OE2 . GLU A 1 109 ? -28.330 24.056 47.202  1.00 39.32 ? 109 GLU A OE2 1 
ATOM   852  N  N   . LEU A 1 110 ? -21.403 22.903 45.170  1.00 34.88 ? 110 LEU A N   1 
ATOM   853  C  CA  . LEU A 1 110 ? -20.450 22.872 44.073  1.00 34.44 ? 110 LEU A CA  1 
ATOM   854  C  C   . LEU A 1 110 ? -19.858 21.491 43.823  1.00 34.29 ? 110 LEU A C   1 
ATOM   855  O  O   . LEU A 1 110 ? -19.156 21.293 42.828  1.00 34.37 ? 110 LEU A O   1 
ATOM   856  C  CB  . LEU A 1 110 ? -19.343 23.914 44.277  1.00 34.44 ? 110 LEU A CB  1 
ATOM   857  C  CG  . LEU A 1 110 ? -19.721 25.372 44.007  1.00 33.79 ? 110 LEU A CG  1 
ATOM   858  C  CD1 . LEU A 1 110 ? -18.676 26.301 44.592  1.00 33.61 ? 110 LEU A CD1 1 
ATOM   859  C  CD2 . LEU A 1 110 ? -19.885 25.616 42.522  1.00 33.10 ? 110 LEU A CD2 1 
ATOM   860  N  N   . GLN A 1 111 ? -20.149 20.538 44.708  1.00 33.87 ? 111 GLN A N   1 
ATOM   861  C  CA  . GLN A 1 111 ? -19.610 19.188 44.567  1.00 33.70 ? 111 GLN A CA  1 
ATOM   862  C  C   . GLN A 1 111 ? -20.110 18.503 43.297  1.00 33.52 ? 111 GLN A C   1 
ATOM   863  O  O   . GLN A 1 111 ? -21.304 18.522 42.996  1.00 33.77 ? 111 GLN A O   1 
ATOM   864  C  CB  . GLN A 1 111 ? -19.941 18.333 45.781  1.00 33.72 ? 111 GLN A CB  1 
ATOM   865  C  CG  . GLN A 1 111 ? -19.372 16.926 45.684  1.00 34.49 ? 111 GLN A CG  1 
ATOM   866  C  CD  . GLN A 1 111 ? -19.779 16.046 46.843  1.00 35.72 ? 111 GLN A CD  1 
ATOM   867  O  OE1 . GLN A 1 111 ? -20.136 16.537 47.917  1.00 36.38 ? 111 GLN A OE1 1 
ATOM   868  N  NE2 . GLN A 1 111 ? -19.720 14.734 46.637  1.00 35.42 ? 111 GLN A NE2 1 
ATOM   869  N  N   . GLY A 1 112 ? -19.183 17.907 42.553  1.00 33.13 ? 112 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 112 ? -19.511 17.218 41.311  1.00 32.54 ? 112 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 112 ? -19.801 18.140 40.140  1.00 32.18 ? 112 GLY A C   1 
ATOM   872  O  O   . GLY A 1 112 ? -20.388 17.716 39.143  1.00 32.32 ? 112 GLY A O   1 
ATOM   873  N  N   . LEU A 1 113 ? -19.400 19.401 40.251  1.00 31.52 ? 113 LEU A N   1 
ATOM   874  C  CA  . LEU A 1 113 ? -19.527 20.322 39.135  1.00 31.18 ? 113 LEU A CA  1 
ATOM   875  C  C   . LEU A 1 113 ? -18.143 20.636 38.585  1.00 30.96 ? 113 LEU A C   1 
ATOM   876  O  O   . LEU A 1 113 ? -17.139 20.311 39.209  1.00 30.98 ? 113 LEU A O   1 
ATOM   877  C  CB  . LEU A 1 113 ? -20.250 21.595 39.561  1.00 31.30 ? 113 LEU A CB  1 
ATOM   878  C  CG  . LEU A 1 113 ? -21.578 21.469 40.309  1.00 31.65 ? 113 LEU A CG  1 
ATOM   879  C  CD1 . LEU A 1 113 ? -22.093 22.864 40.639  1.00 31.42 ? 113 LEU A CD1 1 
ATOM   880  C  CD2 . LEU A 1 113 ? -22.625 20.657 39.516  1.00 31.65 ? 113 LEU A CD2 1 
ATOM   881  N  N   . LYS A 1 114 ? -18.091 21.259 37.416  1.00 30.67 ? 114 LYS A N   1 
ATOM   882  C  CA  . LYS A 1 114 ? -16.822 21.508 36.744  1.00 30.73 ? 114 LYS A CA  1 
ATOM   883  C  C   . LYS A 1 114 ? -16.308 22.922 37.025  1.00 30.31 ? 114 LYS A C   1 
ATOM   884  O  O   . LYS A 1 114 ? -17.053 23.881 36.884  1.00 30.49 ? 114 LYS A O   1 
ATOM   885  C  CB  . LYS A 1 114 ? -16.963 21.238 35.240  1.00 30.62 ? 114 LYS A CB  1 
ATOM   886  C  CG  . LYS A 1 114 ? -17.105 19.745 34.889  1.00 31.33 ? 114 LYS A CG  1 
ATOM   887  C  CD  . LYS A 1 114 ? -17.519 19.500 33.420  1.00 31.32 ? 114 LYS A CD  1 
ATOM   888  C  CE  . LYS A 1 114 ? -19.031 19.399 33.262  1.00 31.96 ? 114 LYS A CE  1 
ATOM   889  N  NZ  . LYS A 1 114 ? -19.500 20.280 32.158  1.00 31.85 ? 114 LYS A NZ  1 
ATOM   890  N  N   . SER A 1 115 ? -15.042 23.051 37.420  1.00 29.93 ? 115 SER A N   1 
ATOM   891  C  CA  . SER A 1 115 ? -14.504 24.356 37.837  1.00 29.91 ? 115 SER A CA  1 
ATOM   892  C  C   . SER A 1 115 ? -13.351 24.893 36.984  1.00 30.08 ? 115 SER A C   1 
ATOM   893  O  O   . SER A 1 115 ? -12.584 24.132 36.390  1.00 30.28 ? 115 SER A O   1 
ATOM   894  C  CB  . SER A 1 115 ? -14.081 24.326 39.311  1.00 29.66 ? 115 SER A CB  1 
ATOM   895  O  OG  . SER A 1 115 ? -12.884 23.595 39.488  1.00 28.95 ? 115 SER A OG  1 
ATOM   896  N  N   . CYS A 1 116 ? -13.239 26.215 36.931  1.00 29.92 ? 116 CYS A N   1 
ATOM   897  C  CA  . CYS A 1 116 ? -12.106 26.852 36.284  1.00 29.96 ? 116 CYS A CA  1 
ATOM   898  C  C   . CYS A 1 116 ? -11.369 27.703 37.309  1.00 29.59 ? 116 CYS A C   1 
ATOM   899  O  O   . CYS A 1 116 ? -11.984 28.326 38.177  1.00 29.78 ? 116 CYS A O   1 
ATOM   900  C  CB  . CYS A 1 116 ? -12.549 27.678 35.074  1.00 30.02 ? 116 CYS A CB  1 
ATOM   901  S  SG  . CYS A 1 116 ? -13.752 26.830 34.015  1.00 31.80 ? 116 CYS A SG  1 
ATOM   902  N  N   . HIS A 1 117 ? -10.046 27.696 37.212  1.00 29.04 ? 117 HIS A N   1 
ATOM   903  C  CA  . HIS A 1 117 ? -9.167  28.348 38.168  1.00 28.23 ? 117 HIS A CA  1 
ATOM   904  C  C   . HIS A 1 117 ? -8.075  29.067 37.384  1.00 27.97 ? 117 HIS A C   1 
ATOM   905  O  O   . HIS A 1 117 ? -7.671  28.604 36.319  1.00 28.15 ? 117 HIS A O   1 
ATOM   906  C  CB  . HIS A 1 117 ? -8.522  27.305 39.086  1.00 28.12 ? 117 HIS A CB  1 
ATOM   907  C  CG  . HIS A 1 117 ? -9.500  26.443 39.830  1.00 27.72 ? 117 HIS A CG  1 
ATOM   908  N  ND1 . HIS A 1 117 ? -9.928  26.729 41.109  1.00 27.30 ? 117 HIS A ND1 1 
ATOM   909  C  CD2 . HIS A 1 117 ? -10.113 25.288 39.484  1.00 27.30 ? 117 HIS A CD2 1 
ATOM   910  C  CE1 . HIS A 1 117 ? -10.765 25.795 41.516  1.00 25.94 ? 117 HIS A CE1 1 
ATOM   911  N  NE2 . HIS A 1 117 ? -10.896 24.910 40.548  1.00 26.85 ? 117 HIS A NE2 1 
ATOM   912  N  N   . THR A 1 118 ? -7.585  30.182 37.911  1.00 27.49 ? 118 THR A N   1 
ATOM   913  C  CA  . THR A 1 118 ? -6.525  30.948 37.251  1.00 26.98 ? 118 THR A CA  1 
ATOM   914  C  C   . THR A 1 118 ? -5.214  30.159 37.171  1.00 26.74 ? 118 THR A C   1 
ATOM   915  O  O   . THR A 1 118 ? -4.459  30.274 36.202  1.00 26.77 ? 118 THR A O   1 
ATOM   916  C  CB  . THR A 1 118 ? -6.271  32.282 37.972  1.00 27.00 ? 118 THR A CB  1 
ATOM   917  O  OG1 . THR A 1 118 ? -5.754  32.018 39.278  1.00 27.11 ? 118 THR A OG1 1 
ATOM   918  C  CG2 . THR A 1 118 ? -7.565  33.087 38.102  1.00 26.63 ? 118 THR A CG2 1 
ATOM   919  N  N   . GLY A 1 119 ? -4.960  29.350 38.193  1.00 26.48 ? 119 GLY A N   1 
ATOM   920  C  CA  . GLY A 1 119 ? -3.735  28.568 38.288  1.00 26.05 ? 119 GLY A CA  1 
ATOM   921  C  C   . GLY A 1 119 ? -3.460  28.157 39.717  1.00 25.92 ? 119 GLY A C   1 
ATOM   922  O  O   . GLY A 1 119 ? -4.001  28.734 40.661  1.00 25.56 ? 119 GLY A O   1 
ATOM   923  N  N   . LEU A 1 120 ? -2.605  27.158 39.878  1.00 26.15 ? 120 LEU A N   1 
ATOM   924  C  CA  . LEU A 1 120 ? -2.308  26.614 41.196  1.00 26.57 ? 120 LEU A CA  1 
ATOM   925  C  C   . LEU A 1 120 ? -1.619  27.627 42.122  1.00 26.97 ? 120 LEU A C   1 
ATOM   926  O  O   . LEU A 1 120 ? -0.679  28.315 41.721  1.00 26.70 ? 120 LEU A O   1 
ATOM   927  C  CB  . LEU A 1 120 ? -1.491  25.322 41.063  1.00 26.52 ? 120 LEU A CB  1 
ATOM   928  C  CG  . LEU A 1 120 ? -1.343  24.442 42.305  1.00 26.39 ? 120 LEU A CG  1 
ATOM   929  C  CD1 . LEU A 1 120 ? -2.679  23.868 42.730  1.00 26.95 ? 120 LEU A CD1 1 
ATOM   930  C  CD2 . LEU A 1 120 ? -0.348  23.335 42.046  1.00 26.29 ? 120 LEU A CD2 1 
ATOM   931  N  N   . ARG A 1 121 ? -2.127  27.709 43.352  1.00 27.49 ? 121 ARG A N   1 
ATOM   932  C  CA  . ARG A 1 121 ? -1.626  28.605 44.415  1.00 28.51 ? 121 ARG A CA  1 
ATOM   933  C  C   . ARG A 1 121 ? -1.742  30.111 44.161  1.00 28.11 ? 121 ARG A C   1 
ATOM   934  O  O   . ARG A 1 121 ? -1.105  30.896 44.862  1.00 28.41 ? 121 ARG A O   1 
ATOM   935  C  CB  . ARG A 1 121 ? -0.209  28.220 44.886  1.00 28.18 ? 121 ARG A CB  1 
ATOM   936  C  CG  . ARG A 1 121 ? -0.164  26.872 45.617  1.00 30.04 ? 121 ARG A CG  1 
ATOM   937  C  CD  . ARG A 1 121 ? 1.248   26.426 46.018  1.00 31.08 ? 121 ARG A CD  1 
ATOM   938  N  NE  . ARG A 1 121 ? 2.275   26.757 45.016  1.00 37.37 ? 121 ARG A NE  1 
ATOM   939  C  CZ  . ARG A 1 121 ? 3.390   26.048 44.803  1.00 39.11 ? 121 ARG A CZ  1 
ATOM   940  N  NH1 . ARG A 1 121 ? 3.629   24.940 45.514  1.00 38.98 ? 121 ARG A NH1 1 
ATOM   941  N  NH2 . ARG A 1 121 ? 4.267   26.442 43.872  1.00 38.86 ? 121 ARG A NH2 1 
ATOM   942  N  N   . ARG A 1 122 ? -2.564  30.515 43.188  1.00 27.85 ? 122 ARG A N   1 
ATOM   943  C  CA  . ARG A 1 122 ? -2.911  31.930 42.991  1.00 27.26 ? 122 ARG A CA  1 
ATOM   944  C  C   . ARG A 1 122 ? -4.028  32.305 43.951  1.00 26.92 ? 122 ARG A C   1 
ATOM   945  O  O   . ARG A 1 122 ? -4.667  31.426 44.538  1.00 26.97 ? 122 ARG A O   1 
ATOM   946  C  CB  . ARG A 1 122 ? -3.370  32.186 41.564  1.00 27.32 ? 122 ARG A CB  1 
ATOM   947  C  CG  . ARG A 1 122 ? -2.333  31.908 40.502  1.00 28.79 ? 122 ARG A CG  1 
ATOM   948  C  CD  . ARG A 1 122 ? -1.679  33.181 40.023  1.00 31.70 ? 122 ARG A CD  1 
ATOM   949  N  NE  . ARG A 1 122 ? -2.599  33.987 39.221  1.00 34.78 ? 122 ARG A NE  1 
ATOM   950  C  CZ  . ARG A 1 122 ? -2.477  34.223 37.914  1.00 36.04 ? 122 ARG A CZ  1 
ATOM   951  N  NH1 . ARG A 1 122 ? -1.458  33.717 37.221  1.00 36.07 ? 122 ARG A NH1 1 
ATOM   952  N  NH2 . ARG A 1 122 ? -3.378  34.984 37.298  1.00 36.00 ? 122 ARG A NH2 1 
ATOM   953  N  N   . THR A 1 123 ? -4.279  33.605 44.094  1.00 26.54 ? 123 THR A N   1 
ATOM   954  C  CA  . THR A 1 123 ? -5.189  34.119 45.125  1.00 26.18 ? 123 THR A CA  1 
ATOM   955  C  C   . THR A 1 123 ? -6.666  33.866 44.829  1.00 25.96 ? 123 THR A C   1 
ATOM   956  O  O   . THR A 1 123 ? -7.306  33.049 45.508  1.00 25.91 ? 123 THR A O   1 
ATOM   957  C  CB  . THR A 1 123 ? -4.942  35.603 45.382  1.00 26.20 ? 123 THR A CB  1 
ATOM   958  O  OG1 . THR A 1 123 ? -3.593  35.769 45.818  1.00 26.94 ? 123 THR A OG1 1 
ATOM   959  C  CG2 . THR A 1 123 ? -5.891  36.157 46.462  1.00 26.66 ? 123 THR A CG2 1 
ATOM   960  N  N   . ALA A 1 124 ? -7.194  34.557 43.819  1.00 25.46 ? 124 ALA A N   1 
ATOM   961  C  CA  . ALA A 1 124 ? -8.597  34.438 43.442  1.00 25.04 ? 124 ALA A CA  1 
ATOM   962  C  C   . ALA A 1 124 ? -8.950  33.065 42.886  1.00 24.95 ? 124 ALA A C   1 
ATOM   963  O  O   . ALA A 1 124 ? -10.115 32.640 42.968  1.00 24.80 ? 124 ALA A O   1 
ATOM   964  C  CB  . ALA A 1 124 ? -8.955  35.489 42.445  1.00 25.16 ? 124 ALA A CB  1 
ATOM   965  N  N   . GLY A 1 125 ? -7.948  32.380 42.332  1.00 24.54 ? 125 GLY A N   1 
ATOM   966  C  CA  . GLY A 1 125 ? -8.170  31.129 41.612  1.00 24.24 ? 125 GLY A CA  1 
ATOM   967  C  C   . GLY A 1 125 ? -7.945  29.848 42.399  1.00 23.91 ? 125 GLY A C   1 
ATOM   968  O  O   . GLY A 1 125 ? -8.402  28.776 41.990  1.00 23.36 ? 125 GLY A O   1 
ATOM   969  N  N   . TRP A 1 126 ? -7.241  29.946 43.524  1.00 23.59 ? 126 TRP A N   1 
ATOM   970  C  CA  . TRP A 1 126 ? -6.972  28.750 44.322  1.00 23.41 ? 126 TRP A CA  1 
ATOM   971  C  C   . TRP A 1 126 ? -7.104  28.976 45.823  1.00 23.60 ? 126 TRP A C   1 
ATOM   972  O  O   . TRP A 1 126 ? -7.930  28.329 46.473  1.00 23.56 ? 126 TRP A O   1 
ATOM   973  C  CB  . TRP A 1 126 ? -5.596  28.186 43.993  1.00 23.18 ? 126 TRP A CB  1 
ATOM   974  C  CG  . TRP A 1 126 ? -5.290  26.931 44.717  1.00 22.60 ? 126 TRP A CG  1 
ATOM   975  C  CD1 . TRP A 1 126 ? -4.552  26.800 45.853  1.00 22.35 ? 126 TRP A CD1 1 
ATOM   976  C  CD2 . TRP A 1 126 ? -5.707  25.618 44.349  1.00 22.37 ? 126 TRP A CD2 1 
ATOM   977  N  NE1 . TRP A 1 126 ? -4.488  25.483 46.223  1.00 22.69 ? 126 TRP A NE1 1 
ATOM   978  C  CE2 . TRP A 1 126 ? -5.185  24.733 45.313  1.00 22.08 ? 126 TRP A CE2 1 
ATOM   979  C  CE3 . TRP A 1 126 ? -6.468  25.100 43.292  1.00 22.09 ? 126 TRP A CE3 1 
ATOM   980  C  CZ2 . TRP A 1 126 ? -5.401  23.363 45.259  1.00 22.30 ? 126 TRP A CZ2 1 
ATOM   981  C  CZ3 . TRP A 1 126 ? -6.694  23.744 43.242  1.00 22.48 ? 126 TRP A CZ3 1 
ATOM   982  C  CH2 . TRP A 1 126 ? -6.160  22.885 44.221  1.00 22.80 ? 126 TRP A CH2 1 
ATOM   983  N  N   . ASN A 1 127 ? -6.296  29.895 46.360  1.00 23.55 ? 127 ASN A N   1 
ATOM   984  C  CA  . ASN A 1 127 ? -6.221  30.125 47.798  1.00 23.50 ? 127 ASN A CA  1 
ATOM   985  C  C   . ASN A 1 127 ? -7.539  30.592 48.403  1.00 23.52 ? 127 ASN A C   1 
ATOM   986  O  O   . ASN A 1 127 ? -7.881  30.221 49.515  1.00 23.61 ? 127 ASN A O   1 
ATOM   987  C  CB  . ASN A 1 127 ? -5.099  31.109 48.138  1.00 23.61 ? 127 ASN A CB  1 
ATOM   988  C  CG  . ASN A 1 127 ? -3.700  30.522 47.932  1.00 23.77 ? 127 ASN A CG  1 
ATOM   989  O  OD1 . ASN A 1 127 ? -2.710  31.265 47.922  1.00 24.16 ? 127 ASN A OD1 1 
ATOM   990  N  ND2 . ASN A 1 127 ? -3.609  29.195 47.783  1.00 22.74 ? 127 ASN A ND2 1 
ATOM   991  N  N   . VAL A 1 128 ? -8.285  31.402 47.669  1.00 23.73 ? 128 VAL A N   1 
ATOM   992  C  CA  . VAL A 1 128 ? -9.595  31.826 48.148  1.00 23.91 ? 128 VAL A CA  1 
ATOM   993  C  C   . VAL A 1 128 ? -10.683 30.738 47.965  1.00 24.33 ? 128 VAL A C   1 
ATOM   994  O  O   . VAL A 1 128 ? -11.281 30.316 48.959  1.00 24.52 ? 128 VAL A O   1 
ATOM   995  C  CB  . VAL A 1 128 ? -10.003 33.183 47.563  1.00 23.69 ? 128 VAL A CB  1 
ATOM   996  C  CG1 . VAL A 1 128 ? -11.393 33.551 48.011  1.00 23.79 ? 128 VAL A CG1 1 
ATOM   997  C  CG2 . VAL A 1 128 ? -9.022  34.231 47.997  1.00 23.39 ? 128 VAL A CG2 1 
ATOM   998  N  N   . PRO A 1 129 ? -10.929 30.260 46.719  1.00 24.52 ? 129 PRO A N   1 
ATOM   999  C  CA  . PRO A 1 129 ? -11.928 29.189 46.563  1.00 24.77 ? 129 PRO A CA  1 
ATOM   1000 C  C   . PRO A 1 129 ? -11.638 27.935 47.392  1.00 24.92 ? 129 PRO A C   1 
ATOM   1001 O  O   . PRO A 1 129 ? -12.523 27.475 48.104  1.00 25.22 ? 129 PRO A O   1 
ATOM   1002 C  CB  . PRO A 1 129 ? -11.868 28.847 45.067  1.00 24.62 ? 129 PRO A CB  1 
ATOM   1003 C  CG  . PRO A 1 129 ? -10.600 29.384 44.599  1.00 24.61 ? 129 PRO A CG  1 
ATOM   1004 C  CD  . PRO A 1 129 ? -10.350 30.622 45.417  1.00 24.46 ? 129 PRO A CD  1 
ATOM   1005 N  N   . ILE A 1 130 ? -10.422 27.396 47.310  1.00 24.95 ? 130 ILE A N   1 
ATOM   1006 C  CA  . ILE A 1 130 ? -10.085 26.179 48.051  1.00 25.16 ? 130 ILE A CA  1 
ATOM   1007 C  C   . ILE A 1 130 ? -10.071 26.421 49.569  1.00 25.60 ? 130 ILE A C   1 
ATOM   1008 O  O   . ILE A 1 130 ? -10.491 25.562 50.344  1.00 25.75 ? 130 ILE A O   1 
ATOM   1009 C  CB  . ILE A 1 130 ? -8.765  25.517 47.549  1.00 25.04 ? 130 ILE A CB  1 
ATOM   1010 C  CG1 . ILE A 1 130 ? -8.862  25.169 46.060  1.00 24.69 ? 130 ILE A CG1 1 
ATOM   1011 C  CG2 . ILE A 1 130 ? -8.408  24.274 48.368  1.00 24.79 ? 130 ILE A CG2 1 
ATOM   1012 C  CD1 . ILE A 1 130 ? -10.088 24.363 45.662  1.00 23.78 ? 130 ILE A CD1 1 
ATOM   1013 N  N   . GLY A 1 131 ? -9.607  27.592 49.992  1.00 25.85 ? 131 GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 131 ? -9.740  27.979 51.390  1.00 26.37 ? 131 GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 131 ? -11.201 27.995 51.813  1.00 26.73 ? 131 GLY A C   1 
ATOM   1016 O  O   . GLY A 1 131 ? -11.542 27.497 52.874  1.00 26.72 ? 131 GLY A O   1 
ATOM   1017 N  N   . THR A 1 132 ? -12.056 28.564 50.967  1.00 27.31 ? 132 THR A N   1 
ATOM   1018 C  CA  . THR A 1 132 ? -13.486 28.682 51.227  1.00 28.19 ? 132 THR A CA  1 
ATOM   1019 C  C   . THR A 1 132 ? -14.185 27.326 51.296  1.00 28.89 ? 132 THR A C   1 
ATOM   1020 O  O   . THR A 1 132 ? -15.072 27.128 52.119  1.00 28.94 ? 132 THR A O   1 
ATOM   1021 C  CB  . THR A 1 132 ? -14.162 29.548 50.135  1.00 28.19 ? 132 THR A CB  1 
ATOM   1022 O  OG1 . THR A 1 132 ? -13.694 30.892 50.252  1.00 28.88 ? 132 THR A OG1 1 
ATOM   1023 C  CG2 . THR A 1 132 ? -15.693 29.541 50.253  1.00 28.06 ? 132 THR A CG2 1 
ATOM   1024 N  N   . LEU A 1 133 ? -13.784 26.398 50.432  1.00 29.64 ? 133 LEU A N   1 
ATOM   1025 C  CA  . LEU A 1 133 ? -14.489 25.134 50.287  1.00 30.42 ? 133 LEU A CA  1 
ATOM   1026 C  C   . LEU A 1 133 ? -13.921 23.988 51.123  1.00 31.34 ? 133 LEU A C   1 
ATOM   1027 O  O   . LEU A 1 133 ? -14.521 22.921 51.186  1.00 31.54 ? 133 LEU A O   1 
ATOM   1028 C  CB  . LEU A 1 133 ? -14.543 24.732 48.814  1.00 30.04 ? 133 LEU A CB  1 
ATOM   1029 C  CG  . LEU A 1 133 ? -15.477 25.551 47.924  1.00 29.61 ? 133 LEU A CG  1 
ATOM   1030 C  CD1 . LEU A 1 133 ? -15.074 25.415 46.472  1.00 29.16 ? 133 LEU A CD1 1 
ATOM   1031 C  CD2 . LEU A 1 133 ? -16.913 25.127 48.112  1.00 29.69 ? 133 LEU A CD2 1 
ATOM   1032 N  N   . ARG A 1 134 ? -12.784 24.214 51.775  1.00 32.48 ? 134 ARG A N   1 
ATOM   1033 C  CA  . ARG A 1 134 ? -12.068 23.160 52.506  1.00 33.65 ? 134 ARG A CA  1 
ATOM   1034 C  C   . ARG A 1 134 ? -12.945 22.316 53.457  1.00 34.89 ? 134 ARG A C   1 
ATOM   1035 O  O   . ARG A 1 134 ? -12.785 21.087 53.512  1.00 34.93 ? 134 ARG A O   1 
ATOM   1036 C  CB  . ARG A 1 134 ? -10.859 23.741 53.243  1.00 33.48 ? 134 ARG A CB  1 
ATOM   1037 C  CG  . ARG A 1 134 ? -10.021 22.715 53.982  1.00 33.47 ? 134 ARG A CG  1 
ATOM   1038 C  CD  . ARG A 1 134 ? -8.720  23.318 54.504  1.00 33.44 ? 134 ARG A CD  1 
ATOM   1039 N  NE  . ARG A 1 134 ? -8.929  24.380 55.487  1.00 32.92 ? 134 ARG A NE  1 
ATOM   1040 C  CZ  . ARG A 1 134 ? -9.152  24.172 56.783  1.00 31.90 ? 134 ARG A CZ  1 
ATOM   1041 N  NH1 . ARG A 1 134 ? -9.212  22.935 57.266  1.00 31.01 ? 134 ARG A NH1 1 
ATOM   1042 N  NH2 . ARG A 1 134 ? -9.332  25.205 57.596  1.00 30.77 ? 134 ARG A NH2 1 
ATOM   1043 N  N   . PRO A 1 135 ? -13.864 22.965 54.210  1.00 35.96 ? 135 PRO A N   1 
ATOM   1044 C  CA  . PRO A 1 135 ? -14.799 22.210 55.052  1.00 36.77 ? 135 PRO A CA  1 
ATOM   1045 C  C   . PRO A 1 135 ? -15.770 21.285 54.300  1.00 37.67 ? 135 PRO A C   1 
ATOM   1046 O  O   . PRO A 1 135 ? -16.511 20.544 54.946  1.00 37.89 ? 135 PRO A O   1 
ATOM   1047 C  CB  . PRO A 1 135 ? -15.584 23.311 55.780  1.00 36.71 ? 135 PRO A CB  1 
ATOM   1048 C  CG  . PRO A 1 135 ? -14.726 24.518 55.699  1.00 36.33 ? 135 PRO A CG  1 
ATOM   1049 C  CD  . PRO A 1 135 ? -14.069 24.418 54.366  1.00 35.98 ? 135 PRO A CD  1 
ATOM   1050 N  N   . PHE A 1 136 ? -15.783 21.330 52.969  1.00 38.71 ? 136 PHE A N   1 
ATOM   1051 C  CA  . PHE A 1 136 ? -16.600 20.397 52.185  1.00 40.03 ? 136 PHE A CA  1 
ATOM   1052 C  C   . PHE A 1 136 ? -15.755 19.277 51.585  1.00 40.72 ? 136 PHE A C   1 
ATOM   1053 O  O   . PHE A 1 136 ? -16.271 18.207 51.266  1.00 40.84 ? 136 PHE A O   1 
ATOM   1054 C  CB  . PHE A 1 136 ? -17.382 21.108 51.071  1.00 40.19 ? 136 PHE A CB  1 
ATOM   1055 C  CG  . PHE A 1 136 ? -18.384 22.122 51.567  1.00 41.32 ? 136 PHE A CG  1 
ATOM   1056 C  CD1 . PHE A 1 136 ? -19.154 21.880 52.703  1.00 42.65 ? 136 PHE A CD1 1 
ATOM   1057 C  CD2 . PHE A 1 136 ? -18.573 23.316 50.885  1.00 42.20 ? 136 PHE A CD2 1 
ATOM   1058 C  CE1 . PHE A 1 136 ? -20.083 22.825 53.161  1.00 42.67 ? 136 PHE A CE1 1 
ATOM   1059 C  CE2 . PHE A 1 136 ? -19.500 24.262 51.333  1.00 42.31 ? 136 PHE A CE2 1 
ATOM   1060 C  CZ  . PHE A 1 136 ? -20.255 24.014 52.468  1.00 41.97 ? 136 PHE A CZ  1 
ATOM   1061 N  N   . LEU A 1 137 ? -14.454 19.524 51.467  1.00 41.68 ? 137 LEU A N   1 
ATOM   1062 C  CA  . LEU A 1 137 ? -13.539 18.650 50.734  1.00 42.53 ? 137 LEU A CA  1 
ATOM   1063 C  C   . LEU A 1 137 ? -13.295 17.287 51.382  1.00 43.49 ? 137 LEU A C   1 
ATOM   1064 O  O   . LEU A 1 137 ? -12.782 16.374 50.721  1.00 43.55 ? 137 LEU A O   1 
ATOM   1065 C  CB  . LEU A 1 137 ? -12.193 19.356 50.516  1.00 42.35 ? 137 LEU A CB  1 
ATOM   1066 C  CG  . LEU A 1 137 ? -12.128 20.671 49.740  1.00 41.60 ? 137 LEU A CG  1 
ATOM   1067 C  CD1 . LEU A 1 137 ? -10.696 21.155 49.680  1.00 41.28 ? 137 LEU A CD1 1 
ATOM   1068 C  CD2 . LEU A 1 137 ? -12.696 20.518 48.348  1.00 40.80 ? 137 LEU A CD2 1 
ATOM   1069 N  N   . ASN A 1 138 ? -13.664 17.158 52.659  1.00 44.72 ? 138 ASN A N   1 
ATOM   1070 C  CA  . ASN A 1 138 ? -13.391 15.953 53.463  1.00 45.97 ? 138 ASN A CA  1 
ATOM   1071 C  C   . ASN A 1 138 ? -11.888 15.607 53.461  1.00 46.07 ? 138 ASN A C   1 
ATOM   1072 O  O   . ASN A 1 138 ? -11.511 14.441 53.332  1.00 46.24 ? 138 ASN A O   1 
ATOM   1073 C  CB  . ASN A 1 138 ? -14.245 14.738 53.005  1.00 46.36 ? 138 ASN A CB  1 
ATOM   1074 C  CG  . ASN A 1 138 ? -15.765 14.939 53.201  1.00 48.75 ? 138 ASN A CG  1 
ATOM   1075 O  OD1 . ASN A 1 138 ? -16.204 15.879 53.871  1.00 48.84 ? 138 ASN A OD1 1 
ATOM   1076 N  ND2 . ASN A 1 138 ? -16.566 14.010 52.628  1.00 52.95 ? 138 ASN A ND2 1 
ATOM   1077 N  N   . TRP A 1 139 ? -11.040 16.626 53.605  1.00 46.33 ? 139 TRP A N   1 
ATOM   1078 C  CA  . TRP A 1 139 ? -9.587  16.448 53.505  1.00 46.65 ? 139 TRP A CA  1 
ATOM   1079 C  C   . TRP A 1 139 ? -8.923  16.031 54.819  1.00 47.13 ? 139 TRP A C   1 
ATOM   1080 O  O   . TRP A 1 139 ? -9.184  16.616 55.869  1.00 47.11 ? 139 TRP A O   1 
ATOM   1081 C  CB  . TRP A 1 139 ? -8.930  17.712 52.951  1.00 46.36 ? 139 TRP A CB  1 
ATOM   1082 C  CG  . TRP A 1 139 ? -7.440  17.595 52.726  1.00 46.13 ? 139 TRP A CG  1 
ATOM   1083 C  CD1 . TRP A 1 139 ? -6.777  16.574 52.104  1.00 45.93 ? 139 TRP A CD1 1 
ATOM   1084 C  CD2 . TRP A 1 139 ? -6.442  18.553 53.092  1.00 46.01 ? 139 TRP A CD2 1 
ATOM   1085 N  NE1 . TRP A 1 139 ? -5.426  16.827 52.075  1.00 45.47 ? 139 TRP A NE1 1 
ATOM   1086 C  CE2 . TRP A 1 139 ? -5.191  18.035 52.673  1.00 45.54 ? 139 TRP A CE2 1 
ATOM   1087 C  CE3 . TRP A 1 139 ? -6.480  19.799 53.740  1.00 45.93 ? 139 TRP A CE3 1 
ATOM   1088 C  CZ2 . TRP A 1 139 ? -3.990  18.715 52.882  1.00 45.93 ? 139 TRP A CZ2 1 
ATOM   1089 C  CZ3 . TRP A 1 139 ? -5.283  20.480 53.949  1.00 46.09 ? 139 TRP A CZ3 1 
ATOM   1090 C  CH2 . TRP A 1 139 ? -4.053  19.935 53.518  1.00 46.27 ? 139 TRP A CH2 1 
ATOM   1091 N  N   . THR A 1 140 ? -8.048  15.029 54.737  1.00 47.83 ? 140 THR A N   1 
ATOM   1092 C  CA  . THR A 1 140 ? -7.416  14.422 55.919  1.00 48.43 ? 140 THR A CA  1 
ATOM   1093 C  C   . THR A 1 140 ? -6.072  15.049 56.327  1.00 48.92 ? 140 THR A C   1 
ATOM   1094 O  O   . THR A 1 140 ? -5.671  14.949 57.490  1.00 48.96 ? 140 THR A O   1 
ATOM   1095 C  CB  . THR A 1 140 ? -7.227  12.880 55.746  1.00 48.38 ? 140 THR A CB  1 
ATOM   1096 O  OG1 . THR A 1 140 ? -6.381  12.610 54.619  1.00 48.14 ? 140 THR A OG1 1 
ATOM   1097 C  CG2 . THR A 1 140 ? -8.566  12.184 55.552  1.00 48.10 ? 140 THR A CG2 1 
ATOM   1098 N  N   . GLY A 1 141 ? -5.398  15.700 55.375  1.00 49.52 ? 141 GLY A N   1 
ATOM   1099 C  CA  . GLY A 1 141 ? -4.028  16.210 55.561  1.00 50.13 ? 141 GLY A CA  1 
ATOM   1100 C  C   . GLY A 1 141 ? -2.992  15.217 55.034  1.00 50.62 ? 141 GLY A C   1 
ATOM   1101 O  O   . GLY A 1 141 ? -3.370  14.154 54.517  1.00 50.66 ? 141 GLY A O   1 
ATOM   1102 N  N   . PRO A 1 142 ? -1.678  15.542 55.164  1.00 50.87 ? 142 PRO A N   1 
ATOM   1103 C  CA  . PRO A 1 142 ? -0.602  14.591 54.805  1.00 50.89 ? 142 PRO A CA  1 
ATOM   1104 C  C   . PRO A 1 142 ? -0.800  13.225 55.494  1.00 50.92 ? 142 PRO A C   1 
ATOM   1105 O  O   . PRO A 1 142 ? -1.235  13.189 56.648  1.00 51.03 ? 142 PRO A O   1 
ATOM   1106 C  CB  . PRO A 1 142 ? 0.674   15.278 55.320  1.00 50.86 ? 142 PRO A CB  1 
ATOM   1107 C  CG  . PRO A 1 142 ? 0.197   16.389 56.227  1.00 50.98 ? 142 PRO A CG  1 
ATOM   1108 C  CD  . PRO A 1 142 ? -1.126  16.813 55.667  1.00 50.84 ? 142 PRO A CD  1 
ATOM   1109 N  N   . PRO A 1 143 ? -0.487  12.105 54.801  1.00 50.83 ? 143 PRO A N   1 
ATOM   1110 C  CA  . PRO A 1 143 ? 0.189   11.985 53.496  1.00 50.60 ? 143 PRO A CA  1 
ATOM   1111 C  C   . PRO A 1 143 ? -0.702  12.235 52.262  1.00 50.17 ? 143 PRO A C   1 
ATOM   1112 O  O   . PRO A 1 143 ? -0.387  11.736 51.173  1.00 50.31 ? 143 PRO A O   1 
ATOM   1113 C  CB  . PRO A 1 143 ? 0.716   10.534 53.494  1.00 50.60 ? 143 PRO A CB  1 
ATOM   1114 C  CG  . PRO A 1 143 ? 0.209   9.889  54.779  1.00 50.88 ? 143 PRO A CG  1 
ATOM   1115 C  CD  . PRO A 1 143 ? -0.852  10.781 55.337  1.00 50.79 ? 143 PRO A CD  1 
ATOM   1116 N  N   . GLU A 1 144 ? -1.787  12.995 52.428  1.00 49.29 ? 144 GLU A N   1 
ATOM   1117 C  CA  . GLU A 1 144 ? -2.634  13.381 51.302  1.00 48.39 ? 144 GLU A CA  1 
ATOM   1118 C  C   . GLU A 1 144 ? -2.455  14.861 50.960  1.00 47.62 ? 144 GLU A C   1 
ATOM   1119 O  O   . GLU A 1 144 ? -2.695  15.726 51.810  1.00 47.74 ? 144 GLU A O   1 
ATOM   1120 C  CB  . GLU A 1 144 ? -4.111  13.064 51.569  1.00 48.35 ? 144 GLU A CB  1 
ATOM   1121 C  CG  . GLU A 1 144 ? -5.017  13.354 50.370  1.00 48.40 ? 144 GLU A CG  1 
ATOM   1122 C  CD  . GLU A 1 144 ? -6.506  13.241 50.674  1.00 48.54 ? 144 GLU A CD  1 
ATOM   1123 O  OE1 . GLU A 1 144 ? -6.955  13.693 51.754  1.00 48.63 ? 144 GLU A OE1 1 
ATOM   1124 O  OE2 . GLU A 1 144 ? -7.235  12.706 49.810  1.00 48.41 ? 144 GLU A OE2 1 
ATOM   1125 N  N   . PRO A 1 145 ? -2.017  15.154 49.716  1.00 46.72 ? 145 PRO A N   1 
ATOM   1126 C  CA  . PRO A 1 145 ? -1.966  16.529 49.213  1.00 45.93 ? 145 PRO A CA  1 
ATOM   1127 C  C   . PRO A 1 145 ? -3.369  17.073 48.974  1.00 45.10 ? 145 PRO A C   1 
ATOM   1128 O  O   . PRO A 1 145 ? -4.271  16.312 48.625  1.00 44.84 ? 145 PRO A O   1 
ATOM   1129 C  CB  . PRO A 1 145 ? -1.208  16.394 47.888  1.00 45.97 ? 145 PRO A CB  1 
ATOM   1130 C  CG  . PRO A 1 145 ? -1.409  14.986 47.466  1.00 46.18 ? 145 PRO A CG  1 
ATOM   1131 C  CD  . PRO A 1 145 ? -1.525  14.180 48.722  1.00 46.63 ? 145 PRO A CD  1 
ATOM   1132 N  N   . ILE A 1 146 ? -3.552  18.377 49.161  1.00 44.33 ? 146 ILE A N   1 
ATOM   1133 C  CA  . ILE A 1 146 ? -4.881  18.976 49.022  1.00 43.54 ? 146 ILE A CA  1 
ATOM   1134 C  C   . ILE A 1 146 ? -5.450  18.836 47.603  1.00 43.23 ? 146 ILE A C   1 
ATOM   1135 O  O   . ILE A 1 146 ? -6.670  18.825 47.414  1.00 43.27 ? 146 ILE A O   1 
ATOM   1136 C  CB  . ILE A 1 146 ? -4.921  20.452 49.494  1.00 43.43 ? 146 ILE A CB  1 
ATOM   1137 C  CG1 . ILE A 1 146 ? -6.363  20.865 49.800  1.00 42.86 ? 146 ILE A CG1 1 
ATOM   1138 C  CG2 . ILE A 1 146 ? -4.270  21.377 48.476  1.00 42.96 ? 146 ILE A CG2 1 
ATOM   1139 C  CD1 . ILE A 1 146 ? -6.475  21.944 50.824  1.00 42.53 ? 146 ILE A CD1 1 
ATOM   1140 N  N   . GLU A 1 147 ? -4.559  18.710 46.624  1.00 42.53 ? 147 GLU A N   1 
ATOM   1141 C  CA  . GLU A 1 147 ? -4.950  18.581 45.232  1.00 41.98 ? 147 GLU A CA  1 
ATOM   1142 C  C   . GLU A 1 147 ? -5.824  17.358 44.984  1.00 41.45 ? 147 GLU A C   1 
ATOM   1143 O  O   . GLU A 1 147 ? -6.700  17.390 44.120  1.00 41.34 ? 147 GLU A O   1 
ATOM   1144 C  CB  . GLU A 1 147 ? -3.711  18.556 44.345  1.00 42.12 ? 147 GLU A CB  1 
ATOM   1145 C  CG  . GLU A 1 147 ? -3.117  19.930 44.105  1.00 43.20 ? 147 GLU A CG  1 
ATOM   1146 C  CD  . GLU A 1 147 ? -1.624  19.987 44.379  1.00 44.50 ? 147 GLU A CD  1 
ATOM   1147 O  OE1 . GLU A 1 147 ? -1.222  19.713 45.530  1.00 44.80 ? 147 GLU A OE1 1 
ATOM   1148 O  OE2 . GLU A 1 147 ? -0.855  20.322 43.449  1.00 45.12 ? 147 GLU A OE2 1 
ATOM   1149 N  N   . ALA A 1 148 ? -5.599  16.294 45.756  1.00 40.88 ? 148 ALA A N   1 
ATOM   1150 C  CA  . ALA A 1 148 ? -6.387  15.058 45.643  1.00 40.26 ? 148 ALA A CA  1 
ATOM   1151 C  C   . ALA A 1 148 ? -7.853  15.252 46.043  1.00 39.77 ? 148 ALA A C   1 
ATOM   1152 O  O   . ALA A 1 148 ? -8.758  14.859 45.305  1.00 39.59 ? 148 ALA A O   1 
ATOM   1153 C  CB  . ALA A 1 148 ? -5.745  13.920 46.450  1.00 40.03 ? 148 ALA A CB  1 
ATOM   1154 N  N   . ALA A 1 149 ? -8.073  15.867 47.203  1.00 39.28 ? 149 ALA A N   1 
ATOM   1155 C  CA  . ALA A 1 149 ? -9.421  16.091 47.729  1.00 39.01 ? 149 ALA A CA  1 
ATOM   1156 C  C   . ALA A 1 149 ? -10.260 17.011 46.829  1.00 38.92 ? 149 ALA A C   1 
ATOM   1157 O  O   . ALA A 1 149 ? -11.469 16.793 46.664  1.00 38.91 ? 149 ALA A O   1 
ATOM   1158 C  CB  . ALA A 1 149 ? -9.350  16.635 49.145  1.00 38.81 ? 149 ALA A CB  1 
ATOM   1159 N  N   . VAL A 1 150 ? -9.607  18.030 46.259  1.00 38.54 ? 150 VAL A N   1 
ATOM   1160 C  CA  . VAL A 1 150 ? -10.204 18.923 45.262  1.00 38.11 ? 150 VAL A CA  1 
ATOM   1161 C  C   . VAL A 1 150 ? -10.561 18.145 44.001  1.00 37.96 ? 150 VAL A C   1 
ATOM   1162 O  O   . VAL A 1 150 ? -11.624 18.359 43.409  1.00 37.81 ? 150 VAL A O   1 
ATOM   1163 C  CB  . VAL A 1 150 ? -9.238  20.066 44.884  1.00 38.16 ? 150 VAL A CB  1 
ATOM   1164 C  CG1 . VAL A 1 150 ? -9.878  21.013 43.877  1.00 37.88 ? 150 VAL A CG1 1 
ATOM   1165 C  CG2 . VAL A 1 150 ? -8.793  20.829 46.130  1.00 38.07 ? 150 VAL A CG2 1 
ATOM   1166 N  N   . ALA A 1 151 ? -9.666  17.239 43.606  1.00 37.85 ? 151 ALA A N   1 
ATOM   1167 C  CA  . ALA A 1 151 ? -9.885  16.346 42.463  1.00 37.56 ? 151 ALA A CA  1 
ATOM   1168 C  C   . ALA A 1 151 ? -11.030 15.372 42.701  1.00 37.34 ? 151 ALA A C   1 
ATOM   1169 O  O   . ALA A 1 151 ? -11.685 14.953 41.744  1.00 37.40 ? 151 ALA A O   1 
ATOM   1170 C  CB  . ALA A 1 151 ? -8.613  15.590 42.107  1.00 37.53 ? 151 ALA A CB  1 
ATOM   1171 N  N   . ARG A 1 152 ? -11.264 15.000 43.962  1.00 37.06 ? 152 ARG A N   1 
ATOM   1172 C  CA  . ARG A 1 152 ? -12.449 14.198 44.306  1.00 36.81 ? 152 ARG A CA  1 
ATOM   1173 C  C   . ARG A 1 152 ? -13.694 15.083 44.350  1.00 36.51 ? 152 ARG A C   1 
ATOM   1174 O  O   . ARG A 1 152 ? -14.771 14.650 43.944  1.00 36.50 ? 152 ARG A O   1 
ATOM   1175 C  CB  . ARG A 1 152 ? -12.283 13.441 45.632  1.00 36.68 ? 152 ARG A CB  1 
ATOM   1176 C  CG  . ARG A 1 152 ? -11.078 12.486 45.686  1.00 37.21 ? 152 ARG A CG  1 
ATOM   1177 C  CD  . ARG A 1 152 ? -11.115 11.508 46.879  1.00 37.08 ? 152 ARG A CD  1 
ATOM   1178 N  NE  . ARG A 1 152 ? -11.723 12.070 48.094  1.00 37.60 ? 152 ARG A NE  1 
ATOM   1179 C  CZ  . ARG A 1 152 ? -11.064 12.700 49.069  1.00 37.11 ? 152 ARG A CZ  1 
ATOM   1180 N  NH1 . ARG A 1 152 ? -9.750  12.876 48.997  1.00 36.84 ? 152 ARG A NH1 1 
ATOM   1181 N  NH2 . ARG A 1 152 ? -11.729 13.159 50.123  1.00 36.39 ? 152 ARG A NH2 1 
ATOM   1182 N  N   . PHE A 1 153 ? -13.527 16.325 44.813  1.00 36.13 ? 153 PHE A N   1 
ATOM   1183 C  CA  . PHE A 1 153 ? -14.641 17.256 45.020  1.00 35.80 ? 153 PHE A CA  1 
ATOM   1184 C  C   . PHE A 1 153 ? -15.351 17.678 43.733  1.00 35.71 ? 153 PHE A C   1 
ATOM   1185 O  O   . PHE A 1 153 ? -16.539 17.412 43.576  1.00 35.87 ? 153 PHE A O   1 
ATOM   1186 C  CB  . PHE A 1 153 ? -14.178 18.484 45.799  1.00 35.75 ? 153 PHE A CB  1 
ATOM   1187 C  CG  . PHE A 1 153 ? -15.291 19.411 46.184  1.00 35.54 ? 153 PHE A CG  1 
ATOM   1188 C  CD1 . PHE A 1 153 ? -16.145 19.095 47.239  1.00 35.78 ? 153 PHE A CD1 1 
ATOM   1189 C  CD2 . PHE A 1 153 ? -15.485 20.605 45.501  1.00 35.19 ? 153 PHE A CD2 1 
ATOM   1190 C  CE1 . PHE A 1 153 ? -17.185 19.954 47.603  1.00 35.62 ? 153 PHE A CE1 1 
ATOM   1191 C  CE2 . PHE A 1 153 ? -16.517 21.476 45.856  1.00 35.38 ? 153 PHE A CE2 1 
ATOM   1192 C  CZ  . PHE A 1 153 ? -17.370 21.150 46.911  1.00 35.59 ? 153 PHE A CZ  1 
ATOM   1193 N  N   . PHE A 1 154 ? -14.634 18.350 42.835  1.00 35.51 ? 154 PHE A N   1 
ATOM   1194 C  CA  . PHE A 1 154 ? -15.163 18.686 41.514  1.00 35.29 ? 154 PHE A CA  1 
ATOM   1195 C  C   . PHE A 1 154 ? -15.074 17.461 40.610  1.00 35.34 ? 154 PHE A C   1 
ATOM   1196 O  O   . PHE A 1 154 ? -14.149 16.662 40.738  1.00 35.44 ? 154 PHE A O   1 
ATOM   1197 C  CB  . PHE A 1 154 ? -14.377 19.845 40.882  1.00 35.14 ? 154 PHE A CB  1 
ATOM   1198 C  CG  . PHE A 1 154 ? -14.400 21.115 41.688  1.00 34.77 ? 154 PHE A CG  1 
ATOM   1199 C  CD1 . PHE A 1 154 ? -15.589 21.805 41.902  1.00 34.68 ? 154 PHE A CD1 1 
ATOM   1200 C  CD2 . PHE A 1 154 ? -13.229 21.629 42.226  1.00 34.34 ? 154 PHE A CD2 1 
ATOM   1201 C  CE1 . PHE A 1 154 ? -15.608 22.976 42.655  1.00 34.00 ? 154 PHE A CE1 1 
ATOM   1202 C  CE2 . PHE A 1 154 ? -13.242 22.798 42.979  1.00 33.57 ? 154 PHE A CE2 1 
ATOM   1203 C  CZ  . PHE A 1 154 ? -14.431 23.469 43.190  1.00 33.83 ? 154 PHE A CZ  1 
ATOM   1204 N  N   . SER A 1 155 ? -16.025 17.306 39.694  1.00 35.35 ? 155 SER A N   1 
ATOM   1205 C  CA  . SER A 1 155 ? -15.965 16.193 38.746  1.00 35.34 ? 155 SER A CA  1 
ATOM   1206 C  C   . SER A 1 155 ? -14.794 16.370 37.777  1.00 35.32 ? 155 SER A C   1 
ATOM   1207 O  O   . SER A 1 155 ? -14.125 15.403 37.415  1.00 35.38 ? 155 SER A O   1 
ATOM   1208 C  CB  . SER A 1 155 ? -17.293 16.007 37.997  1.00 35.29 ? 155 SER A CB  1 
ATOM   1209 O  OG  . SER A 1 155 ? -17.548 17.070 37.099  1.00 35.27 ? 155 SER A OG  1 
ATOM   1210 N  N   . ALA A 1 156 ? -14.548 17.618 37.385  1.00 35.20 ? 156 ALA A N   1 
ATOM   1211 C  CA  . ALA A 1 156 ? -13.456 17.970 36.480  1.00 35.02 ? 156 ALA A CA  1 
ATOM   1212 C  C   . ALA A 1 156 ? -13.130 19.446 36.654  1.00 34.91 ? 156 ALA A C   1 
ATOM   1213 O  O   . ALA A 1 156 ? -13.986 20.228 37.053  1.00 34.97 ? 156 ALA A O   1 
ATOM   1214 C  CB  . ALA A 1 156 ? -13.837 17.677 35.040  1.00 34.86 ? 156 ALA A CB  1 
ATOM   1215 N  N   . SER A 1 157 ? -11.891 19.826 36.362  1.00 34.74 ? 157 SER A N   1 
ATOM   1216 C  CA  . SER A 1 157 ? -11.480 21.216 36.507  1.00 34.71 ? 157 SER A CA  1 
ATOM   1217 C  C   . SER A 1 157 ? -10.296 21.585 35.611  1.00 34.66 ? 157 SER A C   1 
ATOM   1218 O  O   . SER A 1 157 ? -9.649  20.709 35.039  1.00 34.73 ? 157 SER A O   1 
ATOM   1219 C  CB  . SER A 1 157 ? -11.173 21.522 37.978  1.00 34.66 ? 157 SER A CB  1 
ATOM   1220 O  OG  . SER A 1 157 ? -10.850 20.339 38.692  1.00 35.09 ? 157 SER A OG  1 
ATOM   1221 N  N   . CYS A 1 158 ? -10.051 22.886 35.456  1.00 34.57 ? 158 CYS A N   1 
ATOM   1222 C  CA  . CYS A 1 158 ? -8.778  23.359 34.938  1.00 34.06 ? 158 CYS A CA  1 
ATOM   1223 C  C   . CYS A 1 158 ? -8.051  24.134 36.027  1.00 33.48 ? 158 CYS A C   1 
ATOM   1224 O  O   . CYS A 1 158 ? -8.515  25.171 36.485  1.00 33.43 ? 158 CYS A O   1 
ATOM   1225 C  CB  . CYS A 1 158 ? -8.927  24.206 33.670  1.00 34.35 ? 158 CYS A CB  1 
ATOM   1226 S  SG  . CYS A 1 158 ? -7.303  24.706 32.935  1.00 35.60 ? 158 CYS A SG  1 
ATOM   1227 N  N   . VAL A 1 159 ? -6.920  23.589 36.453  1.00 32.89 ? 159 VAL A N   1 
ATOM   1228 C  CA  . VAL A 1 159 ? -6.060  24.208 37.441  1.00 32.29 ? 159 VAL A CA  1 
ATOM   1229 C  C   . VAL A 1 159 ? -4.665  24.233 36.817  1.00 32.21 ? 159 VAL A C   1 
ATOM   1230 O  O   . VAL A 1 159 ? -3.874  23.307 37.023  1.00 32.07 ? 159 VAL A O   1 
ATOM   1231 C  CB  . VAL A 1 159 ? -6.060  23.415 38.776  1.00 32.09 ? 159 VAL A CB  1 
ATOM   1232 C  CG1 . VAL A 1 159 ? -5.299  24.161 39.869  1.00 31.85 ? 159 VAL A CG1 1 
ATOM   1233 C  CG2 . VAL A 1 159 ? -7.470  23.156 39.229  1.00 31.77 ? 159 VAL A CG2 1 
ATOM   1234 N  N   . PRO A 1 160 ? -4.364  25.286 36.026  1.00 31.97 ? 160 PRO A N   1 
ATOM   1235 C  CA  . PRO A 1 160 ? -3.070  25.377 35.359  1.00 31.82 ? 160 PRO A CA  1 
ATOM   1236 C  C   . PRO A 1 160 ? -1.931  25.289 36.356  1.00 32.08 ? 160 PRO A C   1 
ATOM   1237 O  O   . PRO A 1 160 ? -1.973  25.912 37.410  1.00 32.10 ? 160 PRO A O   1 
ATOM   1238 C  CB  . PRO A 1 160 ? -3.110  26.758 34.719  1.00 31.59 ? 160 PRO A CB  1 
ATOM   1239 C  CG  . PRO A 1 160 ? -4.554  27.039 34.530  1.00 31.41 ? 160 PRO A CG  1 
ATOM   1240 C  CD  . PRO A 1 160 ? -5.218  26.447 35.718  1.00 31.76 ? 160 PRO A CD  1 
ATOM   1241 N  N   . GLY A 1 161 ? -0.926  24.498 36.029  1.00 32.72 ? 161 GLY A N   1 
ATOM   1242 C  CA  . GLY A 1 161 ? 0.220   24.340 36.909  1.00 33.81 ? 161 GLY A CA  1 
ATOM   1243 C  C   . GLY A 1 161 ? 0.086   23.179 37.876  1.00 34.60 ? 161 GLY A C   1 
ATOM   1244 O  O   . GLY A 1 161 ? 1.037   22.848 38.587  1.00 34.76 ? 161 GLY A O   1 
ATOM   1245 N  N   . ALA A 1 162 ? -1.094  22.562 37.915  1.00 35.38 ? 162 ALA A N   1 
ATOM   1246 C  CA  . ALA A 1 162 ? -1.295  21.361 38.719  1.00 36.04 ? 162 ALA A CA  1 
ATOM   1247 C  C   . ALA A 1 162 ? -0.521  20.212 38.110  1.00 36.67 ? 162 ALA A C   1 
ATOM   1248 O  O   . ALA A 1 162 ? -0.372  20.130 36.887  1.00 36.55 ? 162 ALA A O   1 
ATOM   1249 C  CB  . ALA A 1 162 ? -2.760  21.015 38.813  1.00 35.94 ? 162 ALA A CB  1 
ATOM   1250 N  N   . ASP A 1 163 ? -0.018  19.339 38.976  1.00 37.67 ? 163 ASP A N   1 
ATOM   1251 C  CA  . ASP A 1 163 ? 0.729   18.170 38.547  1.00 38.53 ? 163 ASP A CA  1 
ATOM   1252 C  C   . ASP A 1 163 ? -0.190  17.242 37.770  1.00 38.88 ? 163 ASP A C   1 
ATOM   1253 O  O   . ASP A 1 163 ? -1.089  16.621 38.343  1.00 39.09 ? 163 ASP A O   1 
ATOM   1254 C  CB  . ASP A 1 163 ? 1.315   17.443 39.755  1.00 38.73 ? 163 ASP A CB  1 
ATOM   1255 C  CG  . ASP A 1 163 ? 2.321   16.369 39.366  1.00 39.99 ? 163 ASP A CG  1 
ATOM   1256 O  OD1 . ASP A 1 163 ? 1.959   15.392 38.662  1.00 40.44 ? 163 ASP A OD1 1 
ATOM   1257 O  OD2 . ASP A 1 163 ? 3.486   16.499 39.792  1.00 41.73 ? 163 ASP A OD2 1 
ATOM   1258 N  N   . LYS A 1 164 ? 0.046   17.158 36.464  1.00 39.30 ? 164 LYS A N   1 
ATOM   1259 C  CA  . LYS A 1 164 ? -0.773  16.346 35.570  1.00 39.78 ? 164 LYS A CA  1 
ATOM   1260 C  C   . LYS A 1 164 ? -0.597  14.847 35.818  1.00 39.50 ? 164 LYS A C   1 
ATOM   1261 O  O   . LYS A 1 164 ? -1.510  14.066 35.558  1.00 39.54 ? 164 LYS A O   1 
ATOM   1262 C  CB  . LYS A 1 164 ? -0.443  16.681 34.120  1.00 39.79 ? 164 LYS A CB  1 
ATOM   1263 C  CG  . LYS A 1 164 ? -1.603  16.498 33.145  1.00 40.58 ? 164 LYS A CG  1 
ATOM   1264 C  CD  . LYS A 1 164 ? -1.160  16.776 31.702  1.00 40.94 ? 164 LYS A CD  1 
ATOM   1265 C  CE  . LYS A 1 164 ? -0.472  18.144 31.559  1.00 42.06 ? 164 LYS A CE  1 
ATOM   1266 N  NZ  . LYS A 1 164 ? 0.144   18.368 30.211  1.00 42.60 ? 164 LYS A NZ  1 
ATOM   1267 N  N   . GLY A 1 165 ? 0.577   14.461 36.314  1.00 39.42 ? 165 GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 165 ? 0.870   13.071 36.653  1.00 39.32 ? 165 GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 165 ? -0.065  12.501 37.711  1.00 39.35 ? 165 GLY A C   1 
ATOM   1270 O  O   . GLY A 1 165 ? -0.795  11.551 37.442  1.00 39.22 ? 165 GLY A O   1 
ATOM   1271 N  N   . GLN A 1 166 ? -0.062  13.094 38.905  1.00 39.41 ? 166 GLN A N   1 
ATOM   1272 C  CA  . GLN A 1 166 ? -0.845  12.577 40.044  1.00 39.42 ? 166 GLN A CA  1 
ATOM   1273 C  C   . GLN A 1 166 ? -2.303  13.042 40.069  1.00 38.91 ? 166 GLN A C   1 
ATOM   1274 O  O   . GLN A 1 166 ? -3.147  12.406 40.693  1.00 38.68 ? 166 GLN A O   1 
ATOM   1275 C  CB  . GLN A 1 166 ? -0.200  12.969 41.379  1.00 39.75 ? 166 GLN A CB  1 
ATOM   1276 C  CG  . GLN A 1 166 ? 1.319   12.856 41.450  1.00 41.14 ? 166 GLN A CG  1 
ATOM   1277 C  CD  . GLN A 1 166 ? 1.924   13.881 42.408  1.00 42.72 ? 166 GLN A CD  1 
ATOM   1278 O  OE1 . GLN A 1 166 ? 1.441   14.063 43.531  1.00 43.12 ? 166 GLN A OE1 1 
ATOM   1279 N  NE2 . GLN A 1 166 ? 2.983   14.559 41.962  1.00 42.88 ? 166 GLN A NE2 1 
ATOM   1280 N  N   . PHE A 1 167 ? -2.591  14.162 39.413  1.00 38.62 ? 167 PHE A N   1 
ATOM   1281 C  CA  . PHE A 1 167 ? -3.919  14.772 39.487  1.00 38.33 ? 167 PHE A CA  1 
ATOM   1282 C  C   . PHE A 1 167 ? -4.458  15.061 38.090  1.00 38.33 ? 167 PHE A C   1 
ATOM   1283 O  O   . PHE A 1 167 ? -4.623  16.218 37.723  1.00 38.33 ? 167 PHE A O   1 
ATOM   1284 C  CB  . PHE A 1 167 ? -3.872  16.062 40.326  1.00 38.00 ? 167 PHE A CB  1 
ATOM   1285 C  CG  . PHE A 1 167 ? -3.082  15.931 41.602  1.00 37.75 ? 167 PHE A CG  1 
ATOM   1286 C  CD1 . PHE A 1 167 ? -3.620  15.288 42.712  1.00 37.38 ? 167 PHE A CD1 1 
ATOM   1287 C  CD2 . PHE A 1 167 ? -1.794  16.439 41.691  1.00 37.60 ? 167 PHE A CD2 1 
ATOM   1288 C  CE1 . PHE A 1 167 ? -2.885  15.158 43.891  1.00 36.94 ? 167 PHE A CE1 1 
ATOM   1289 C  CE2 . PHE A 1 167 ? -1.052  16.308 42.870  1.00 37.32 ? 167 PHE A CE2 1 
ATOM   1290 C  CZ  . PHE A 1 167 ? -1.600  15.666 43.965  1.00 37.08 ? 167 PHE A CZ  1 
ATOM   1291 N  N   . PRO A 1 168 ? -4.753  14.007 37.304  1.00 38.54 ? 168 PRO A N   1 
ATOM   1292 C  CA  . PRO A 1 168 ? -5.140  14.265 35.913  1.00 38.66 ? 168 PRO A CA  1 
ATOM   1293 C  C   . PRO A 1 168 ? -6.508  14.933 35.819  1.00 38.79 ? 168 PRO A C   1 
ATOM   1294 O  O   . PRO A 1 168 ? -6.814  15.572 34.808  1.00 39.12 ? 168 PRO A O   1 
ATOM   1295 C  CB  . PRO A 1 168 ? -5.174  12.866 35.284  1.00 38.56 ? 168 PRO A CB  1 
ATOM   1296 C  CG  . PRO A 1 168 ? -5.392  11.938 36.416  1.00 38.38 ? 168 PRO A CG  1 
ATOM   1297 C  CD  . PRO A 1 168 ? -4.779  12.568 37.633  1.00 38.47 ? 168 PRO A CD  1 
ATOM   1298 N  N   . ASN A 1 169 ? -7.295  14.794 36.886  1.00 38.77 ? 169 ASN A N   1 
ATOM   1299 C  CA  . ASN A 1 169 ? -8.658  15.318 36.980  1.00 38.57 ? 169 ASN A CA  1 
ATOM   1300 C  C   . ASN A 1 169 ? -8.727  16.835 37.218  1.00 38.26 ? 169 ASN A C   1 
ATOM   1301 O  O   . ASN A 1 169 ? -9.787  17.454 37.076  1.00 38.09 ? 169 ASN A O   1 
ATOM   1302 C  CB  . ASN A 1 169 ? -9.416  14.564 38.082  1.00 38.72 ? 169 ASN A CB  1 
ATOM   1303 C  CG  . ASN A 1 169 ? -10.917 14.642 37.912  1.00 39.15 ? 169 ASN A CG  1 
ATOM   1304 O  OD1 . ASN A 1 169 ? -11.444 14.337 36.845  1.00 39.76 ? 169 ASN A OD1 1 
ATOM   1305 N  ND2 . ASN A 1 169 ? -11.615 15.055 38.964  1.00 39.62 ? 169 ASN A ND2 1 
ATOM   1306 N  N   . LEU A 1 170 ? -7.594  17.422 37.593  1.00 38.04 ? 170 LEU A N   1 
ATOM   1307 C  CA  . LEU A 1 170 ? -7.479  18.866 37.732  1.00 37.85 ? 170 LEU A CA  1 
ATOM   1308 C  C   . LEU A 1 170 ? -7.041  19.493 36.419  1.00 38.14 ? 170 LEU A C   1 
ATOM   1309 O  O   . LEU A 1 170 ? -7.106  20.706 36.261  1.00 38.22 ? 170 LEU A O   1 
ATOM   1310 C  CB  . LEU A 1 170 ? -6.474  19.236 38.820  1.00 37.55 ? 170 LEU A CB  1 
ATOM   1311 C  CG  . LEU A 1 170 ? -6.772  18.955 40.292  1.00 37.34 ? 170 LEU A CG  1 
ATOM   1312 C  CD1 . LEU A 1 170 ? -5.587  19.398 41.141  1.00 36.83 ? 170 LEU A CD1 1 
ATOM   1313 C  CD2 . LEU A 1 170 ? -8.063  19.613 40.775  1.00 36.59 ? 170 LEU A CD2 1 
ATOM   1314 N  N   . CYS A 1 171 ? -6.591  18.671 35.479  1.00 38.49 ? 171 CYS A N   1 
ATOM   1315 C  CA  . CYS A 1 171 ? -6.145  19.183 34.193  1.00 39.04 ? 171 CYS A CA  1 
ATOM   1316 C  C   . CYS A 1 171 ? -7.090  18.873 33.047  1.00 39.03 ? 171 CYS A C   1 
ATOM   1317 O  O   . CYS A 1 171 ? -6.969  19.472 31.971  1.00 39.24 ? 171 CYS A O   1 
ATOM   1318 C  CB  . CYS A 1 171 ? -4.747  18.674 33.865  1.00 39.20 ? 171 CYS A CB  1 
ATOM   1319 S  SG  . CYS A 1 171 ? -3.491  19.350 34.951  1.00 40.99 ? 171 CYS A SG  1 
ATOM   1320 N  N   . ARG A 1 172 ? -8.026  17.952 33.285  1.00 38.83 ? 172 ARG A N   1 
ATOM   1321 C  CA  . ARG A 1 172 ? -8.925  17.453 32.242  1.00 38.97 ? 172 ARG A CA  1 
ATOM   1322 C  C   . ARG A 1 172 ? -9.528  18.573 31.398  1.00 38.54 ? 172 ARG A C   1 
ATOM   1323 O  O   . ARG A 1 172 ? -9.437  18.545 30.165  1.00 38.47 ? 172 ARG A O   1 
ATOM   1324 C  CB  . ARG A 1 172 ? -10.036 16.580 32.842  1.00 38.83 ? 172 ARG A CB  1 
ATOM   1325 C  CG  . ARG A 1 172 ? -10.770 15.717 31.806  1.00 39.72 ? 172 ARG A CG  1 
ATOM   1326 C  CD  . ARG A 1 172 ? -11.867 14.806 32.411  1.00 40.10 ? 172 ARG A CD  1 
ATOM   1327 N  NE  . ARG A 1 172 ? -11.433 14.097 33.622  1.00 42.45 ? 172 ARG A NE  1 
ATOM   1328 C  CZ  . ARG A 1 172 ? -10.555 13.095 33.653  1.00 42.73 ? 172 ARG A CZ  1 
ATOM   1329 N  NH1 . ARG A 1 172 ? -9.985  12.656 32.535  1.00 43.01 ? 172 ARG A NH1 1 
ATOM   1330 N  NH2 . ARG A 1 172 ? -10.236 12.536 34.813  1.00 42.69 ? 172 ARG A NH2 1 
ATOM   1331 N  N   . LEU A 1 173 ? -10.109 19.564 32.074  1.00 38.18 ? 173 LEU A N   1 
ATOM   1332 C  CA  . LEU A 1 173 ? -10.856 20.638 31.419  1.00 37.90 ? 173 LEU A CA  1 
ATOM   1333 C  C   . LEU A 1 173 ? -10.029 21.630 30.606  1.00 37.87 ? 173 LEU A C   1 
ATOM   1334 O  O   . LEU A 1 173 ? -10.586 22.361 29.788  1.00 37.89 ? 173 LEU A O   1 
ATOM   1335 C  CB  . LEU A 1 173 ? -11.705 21.401 32.438  1.00 37.74 ? 173 LEU A CB  1 
ATOM   1336 C  CG  . LEU A 1 173 ? -12.975 20.742 32.966  1.00 37.85 ? 173 LEU A CG  1 
ATOM   1337 C  CD1 . LEU A 1 173 ? -13.800 21.778 33.680  1.00 37.96 ? 173 LEU A CD1 1 
ATOM   1338 C  CD2 . LEU A 1 173 ? -13.797 20.081 31.861  1.00 37.75 ? 173 LEU A CD2 1 
ATOM   1339 N  N   . CYS A 1 174 ? -8.715  21.660 30.824  1.00 37.86 ? 174 CYS A N   1 
ATOM   1340 C  CA  . CYS A 1 174 ? -7.849  22.643 30.173  1.00 37.98 ? 174 CYS A CA  1 
ATOM   1341 C  C   . CYS A 1 174 ? -7.833  22.524 28.636  1.00 38.10 ? 174 CYS A C   1 
ATOM   1342 O  O   . CYS A 1 174 ? -8.023  21.436 28.079  1.00 37.94 ? 174 CYS A O   1 
ATOM   1343 C  CB  . CYS A 1 174 ? -6.436  22.592 30.764  1.00 37.90 ? 174 CYS A CB  1 
ATOM   1344 S  SG  . CYS A 1 174 ? -6.310  22.925 32.586  1.00 38.71 ? 174 CYS A SG  1 
ATOM   1345 N  N   . ALA A 1 175 ? -7.623  23.656 27.966  1.00 38.36 ? 175 ALA A N   1 
ATOM   1346 C  CA  . ALA A 1 175 ? -7.709  23.740 26.506  1.00 38.64 ? 175 ALA A CA  1 
ATOM   1347 C  C   . ALA A 1 175 ? -6.352  23.688 25.802  1.00 39.12 ? 175 ALA A C   1 
ATOM   1348 O  O   . ALA A 1 175 ? -6.284  23.777 24.576  1.00 39.35 ? 175 ALA A O   1 
ATOM   1349 C  CB  . ALA A 1 175 ? -8.476  24.991 26.091  1.00 38.36 ? 175 ALA A CB  1 
ATOM   1350 N  N   . GLY A 1 176 ? -5.275  23.537 26.567  1.00 39.71 ? 176 GLY A N   1 
ATOM   1351 C  CA  . GLY A 1 176 ? -3.925  23.517 25.999  1.00 40.42 ? 176 GLY A CA  1 
ATOM   1352 C  C   . GLY A 1 176 ? -3.671  22.375 25.032  1.00 40.94 ? 176 GLY A C   1 
ATOM   1353 O  O   . GLY A 1 176 ? -4.195  21.272 25.208  1.00 40.96 ? 176 GLY A O   1 
ATOM   1354 N  N   . THR A 1 177 ? -2.860  22.642 24.013  1.00 41.44 ? 177 THR A N   1 
ATOM   1355 C  CA  . THR A 1 177 ? -2.500  21.626 23.028  1.00 42.24 ? 177 THR A CA  1 
ATOM   1356 C  C   . THR A 1 177 ? -1.271  20.851 23.495  1.00 42.41 ? 177 THR A C   1 
ATOM   1357 O  O   . THR A 1 177 ? -0.286  21.456 23.927  1.00 42.37 ? 177 THR A O   1 
ATOM   1358 C  CB  . THR A 1 177 ? -2.197  22.262 21.654  1.00 42.39 ? 177 THR A CB  1 
ATOM   1359 O  OG1 . THR A 1 177 ? -3.005  23.434 21.481  1.00 43.48 ? 177 THR A OG1 1 
ATOM   1360 C  CG2 . THR A 1 177 ? -2.463  21.276 20.514  1.00 42.08 ? 177 THR A CG2 1 
ATOM   1361 N  N   . GLY A 1 178 ? -1.343  19.520 23.407  1.00 42.64 ? 178 GLY A N   1 
ATOM   1362 C  CA  . GLY A 1 178 ? -0.230  18.627 23.763  1.00 42.86 ? 178 GLY A CA  1 
ATOM   1363 C  C   . GLY A 1 178 ? 0.380   18.877 25.134  1.00 43.06 ? 178 GLY A C   1 
ATOM   1364 O  O   . GLY A 1 178 ? -0.321  18.856 26.146  1.00 43.15 ? 178 GLY A O   1 
ATOM   1365 N  N   . GLU A 1 179 ? 1.688   19.136 25.160  1.00 43.14 ? 179 GLU A N   1 
ATOM   1366 C  CA  . GLU A 1 179 ? 2.431   19.340 26.414  1.00 43.23 ? 179 GLU A CA  1 
ATOM   1367 C  C   . GLU A 1 179 ? 2.240   20.726 27.022  1.00 42.73 ? 179 GLU A C   1 
ATOM   1368 O  O   . GLU A 1 179 ? 2.766   21.027 28.093  1.00 42.72 ? 179 GLU A O   1 
ATOM   1369 C  CB  . GLU A 1 179 ? 3.921   19.019 26.228  1.00 43.46 ? 179 GLU A CB  1 
ATOM   1370 C  CG  . GLU A 1 179 ? 4.211   17.576 25.740  1.00 45.45 ? 179 GLU A CG  1 
ATOM   1371 C  CD  . GLU A 1 179 ? 3.622   16.478 26.647  1.00 47.82 ? 179 GLU A CD  1 
ATOM   1372 O  OE1 . GLU A 1 179 ? 2.390   16.231 26.597  1.00 48.56 ? 179 GLU A OE1 1 
ATOM   1373 O  OE2 . GLU A 1 179 ? 4.401   15.842 27.395  1.00 48.69 ? 179 GLU A OE2 1 
ATOM   1374 N  N   . ASN A 1 180 ? 1.474   21.562 26.333  1.00 42.23 ? 180 ASN A N   1 
ATOM   1375 C  CA  . ASN A 1 180 ? 1.071   22.857 26.855  1.00 41.72 ? 180 ASN A CA  1 
ATOM   1376 C  C   . ASN A 1 180 ? -0.274  22.791 27.580  1.00 41.24 ? 180 ASN A C   1 
ATOM   1377 O  O   . ASN A 1 180 ? -0.775  23.800 28.066  1.00 41.16 ? 180 ASN A O   1 
ATOM   1378 C  CB  . ASN A 1 180 ? 1.020   23.887 25.725  1.00 41.98 ? 180 ASN A CB  1 
ATOM   1379 C  CG  . ASN A 1 180 ? 2.390   24.217 25.179  1.00 42.06 ? 180 ASN A CG  1 
ATOM   1380 O  OD1 . ASN A 1 180 ? 3.235   24.770 25.886  1.00 42.44 ? 180 ASN A OD1 1 
ATOM   1381 N  ND2 . ASN A 1 180 ? 2.617   23.885 23.910  1.00 41.98 ? 180 ASN A ND2 1 
ATOM   1382 N  N   . LYS A 1 181 ? -0.857  21.599 27.641  1.00 40.83 ? 181 LYS A N   1 
ATOM   1383 C  CA  . LYS A 1 181 ? -2.081  21.386 28.398  1.00 40.39 ? 181 LYS A CA  1 
ATOM   1384 C  C   . LYS A 1 181 ? -1.784  21.598 29.880  1.00 39.92 ? 181 LYS A C   1 
ATOM   1385 O  O   . LYS A 1 181 ? -0.789  21.088 30.399  1.00 39.80 ? 181 LYS A O   1 
ATOM   1386 C  CB  . LYS A 1 181 ? -2.622  19.978 28.141  1.00 40.51 ? 181 LYS A CB  1 
ATOM   1387 C  CG  . LYS A 1 181 ? -4.089  19.798 28.478  1.00 41.22 ? 181 LYS A CG  1 
ATOM   1388 C  CD  . LYS A 1 181 ? -4.670  18.547 27.827  1.00 42.36 ? 181 LYS A CD  1 
ATOM   1389 C  CE  . LYS A 1 181 ? -6.146  18.358 28.199  1.00 43.21 ? 181 LYS A CE  1 
ATOM   1390 N  NZ  . LYS A 1 181 ? -6.771  17.171 27.532  1.00 43.65 ? 181 LYS A NZ  1 
ATOM   1391 N  N   . CYS A 1 182 ? -2.623  22.393 30.541  1.00 39.57 ? 182 CYS A N   1 
ATOM   1392 C  CA  . CYS A 1 182 ? -2.541  22.608 31.992  1.00 39.00 ? 182 CYS A CA  1 
ATOM   1393 C  C   . CYS A 1 182 ? -1.263  23.334 32.428  1.00 38.34 ? 182 CYS A C   1 
ATOM   1394 O  O   . CYS A 1 182 ? -0.926  23.357 33.614  1.00 38.16 ? 182 CYS A O   1 
ATOM   1395 C  CB  . CYS A 1 182 ? -2.670  21.264 32.719  1.00 39.33 ? 182 CYS A CB  1 
ATOM   1396 S  SG  . CYS A 1 182 ? -3.290  21.332 34.403  1.00 40.05 ? 182 CYS A SG  1 
ATOM   1397 N  N   . ALA A 1 183 ? -0.569  23.929 31.457  1.00 37.50 ? 183 ALA A N   1 
ATOM   1398 C  CA  . ALA A 1 183 ? 0.669   24.668 31.686  1.00 36.69 ? 183 ALA A CA  1 
ATOM   1399 C  C   . ALA A 1 183 ? 0.413   25.923 32.504  1.00 36.29 ? 183 ALA A C   1 
ATOM   1400 O  O   . ALA A 1 183 ? -0.659  26.511 32.421  1.00 36.43 ? 183 ALA A O   1 
ATOM   1401 C  CB  . ALA A 1 183 ? 1.304   25.036 30.359  1.00 36.58 ? 183 ALA A CB  1 
ATOM   1402 N  N   . PHE A 1 184 ? 1.396   26.342 33.293  1.00 35.81 ? 184 PHE A N   1 
ATOM   1403 C  CA  . PHE A 1 184 ? 1.258   27.573 34.060  1.00 35.21 ? 184 PHE A CA  1 
ATOM   1404 C  C   . PHE A 1 184 ? 1.757   28.767 33.250  1.00 35.07 ? 184 PHE A C   1 
ATOM   1405 O  O   . PHE A 1 184 ? 2.746   29.399 33.622  1.00 35.24 ? 184 PHE A O   1 
ATOM   1406 C  CB  . PHE A 1 184 ? 2.005   27.466 35.391  1.00 35.08 ? 184 PHE A CB  1 
ATOM   1407 C  CG  . PHE A 1 184 ? 1.574   28.479 36.409  1.00 35.28 ? 184 PHE A CG  1 
ATOM   1408 C  CD1 . PHE A 1 184 ? 0.528   28.207 37.277  1.00 35.46 ? 184 PHE A CD1 1 
ATOM   1409 C  CD2 . PHE A 1 184 ? 2.207   29.710 36.501  1.00 35.33 ? 184 PHE A CD2 1 
ATOM   1410 C  CE1 . PHE A 1 184 ? 0.122   29.149 38.208  1.00 35.14 ? 184 PHE A CE1 1 
ATOM   1411 C  CE2 . PHE A 1 184 ? 1.804   30.652 37.435  1.00 34.84 ? 184 PHE A CE2 1 
ATOM   1412 C  CZ  . PHE A 1 184 ? 0.765   30.372 38.286  1.00 34.72 ? 184 PHE A CZ  1 
ATOM   1413 N  N   . SER A 1 185 ? 1.073   29.071 32.146  1.00 34.71 ? 185 SER A N   1 
ATOM   1414 C  CA  . SER A 1 185 ? 1.484   30.147 31.246  1.00 34.59 ? 185 SER A CA  1 
ATOM   1415 C  C   . SER A 1 185 ? 0.440   30.392 30.170  1.00 34.67 ? 185 SER A C   1 
ATOM   1416 O  O   . SER A 1 185 ? -0.539  29.665 30.097  1.00 35.06 ? 185 SER A O   1 
ATOM   1417 C  CB  . SER A 1 185 ? 2.805   29.792 30.568  1.00 34.67 ? 185 SER A CB  1 
ATOM   1418 O  OG  . SER A 1 185 ? 2.584   28.902 29.490  1.00 34.28 ? 185 SER A OG  1 
ATOM   1419 N  N   . SER A 1 186 ? 0.680   31.396 29.323  1.00 34.67 ? 186 SER A N   1 
ATOM   1420 C  CA  . SER A 1 186 ? -0.213  31.768 28.215  1.00 34.86 ? 186 SER A CA  1 
ATOM   1421 C  C   . SER A 1 186 ? -0.393  30.701 27.140  1.00 34.74 ? 186 SER A C   1 
ATOM   1422 O  O   . SER A 1 186 ? -1.345  30.768 26.364  1.00 34.75 ? 186 SER A O   1 
ATOM   1423 C  CB  . SER A 1 186 ? 0.276   33.046 27.547  1.00 35.03 ? 186 SER A CB  1 
ATOM   1424 O  OG  . SER A 1 186 ? 0.255   34.119 28.469  1.00 36.46 ? 186 SER A OG  1 
ATOM   1425 N  N   . GLN A 1 187 ? 0.530   29.740 27.081  1.00 34.65 ? 187 GLN A N   1 
ATOM   1426 C  CA  . GLN A 1 187 ? 0.387   28.554 26.224  1.00 34.59 ? 187 GLN A CA  1 
ATOM   1427 C  C   . GLN A 1 187 ? -0.918  27.815 26.528  1.00 33.86 ? 187 GLN A C   1 
ATOM   1428 O  O   . GLN A 1 187 ? -1.506  27.189 25.644  1.00 33.68 ? 187 GLN A O   1 
ATOM   1429 C  CB  . GLN A 1 187 ? 1.558   27.571 26.417  1.00 35.02 ? 187 GLN A CB  1 
ATOM   1430 C  CG  . GLN A 1 187 ? 2.959   28.174 26.382  1.00 36.91 ? 187 GLN A CG  1 
ATOM   1431 C  CD  . GLN A 1 187 ? 3.416   28.535 24.983  1.00 40.18 ? 187 GLN A CD  1 
ATOM   1432 O  OE1 . GLN A 1 187 ? 2.604   28.678 24.060  1.00 41.71 ? 187 GLN A OE1 1 
ATOM   1433 N  NE2 . GLN A 1 187 ? 4.732   28.686 24.813  1.00 41.60 ? 187 GLN A NE2 1 
ATOM   1434 N  N   . GLU A 1 188 ? -1.340  27.867 27.791  1.00 33.01 ? 188 GLU A N   1 
ATOM   1435 C  CA  . GLU A 1 188 ? -2.629  27.340 28.187  1.00 32.32 ? 188 GLU A CA  1 
ATOM   1436 C  C   . GLU A 1 188 ? -3.658  28.436 27.991  1.00 31.99 ? 188 GLU A C   1 
ATOM   1437 O  O   . GLU A 1 188 ? -3.593  29.466 28.656  1.00 32.04 ? 188 GLU A O   1 
ATOM   1438 C  CB  . GLU A 1 188 ? -2.611  26.884 29.641  1.00 32.25 ? 188 GLU A CB  1 
ATOM   1439 C  CG  . GLU A 1 188 ? -3.997  26.585 30.228  1.00 31.87 ? 188 GLU A CG  1 
ATOM   1440 C  CD  . GLU A 1 188 ? -4.751  25.524 29.457  1.00 30.50 ? 188 GLU A CD  1 
ATOM   1441 O  OE1 . GLU A 1 188 ? -4.160  24.474 29.158  1.00 30.89 ? 188 GLU A OE1 1 
ATOM   1442 O  OE2 . GLU A 1 188 ? -5.936  25.739 29.154  1.00 29.61 ? 188 GLU A OE2 1 
ATOM   1443 N  N   . PRO A 1 189 ? -4.597  28.235 27.052  1.00 31.59 ? 189 PRO A N   1 
ATOM   1444 C  CA  . PRO A 1 189 ? -5.597  29.264 26.811  1.00 31.20 ? 189 PRO A CA  1 
ATOM   1445 C  C   . PRO A 1 189 ? -6.504  29.558 28.004  1.00 30.94 ? 189 PRO A C   1 
ATOM   1446 O  O   . PRO A 1 189 ? -7.122  30.617 28.025  1.00 31.27 ? 189 PRO A O   1 
ATOM   1447 C  CB  . PRO A 1 189 ? -6.392  28.713 25.622  1.00 31.36 ? 189 PRO A CB  1 
ATOM   1448 C  CG  . PRO A 1 189 ? -5.452  27.728 24.960  1.00 31.51 ? 189 PRO A CG  1 
ATOM   1449 C  CD  . PRO A 1 189 ? -4.751  27.099 26.126  1.00 31.58 ? 189 PRO A CD  1 
ATOM   1450 N  N   . TYR A 1 190 ? -6.576  28.670 28.995  1.00 30.42 ? 190 TYR A N   1 
ATOM   1451 C  CA  . TYR A 1 190 ? -7.405  28.955 30.177  1.00 30.11 ? 190 TYR A CA  1 
ATOM   1452 C  C   . TYR A 1 190 ? -6.628  29.458 31.399  1.00 29.75 ? 190 TYR A C   1 
ATOM   1453 O  O   . TYR A 1 190 ? -7.145  29.453 32.518  1.00 29.60 ? 190 TYR A O   1 
ATOM   1454 C  CB  . TYR A 1 190 ? -8.290  27.758 30.564  1.00 30.38 ? 190 TYR A CB  1 
ATOM   1455 C  CG  . TYR A 1 190 ? -9.349  27.371 29.549  1.00 30.34 ? 190 TYR A CG  1 
ATOM   1456 C  CD1 . TYR A 1 190 ? -9.843  28.300 28.628  1.00 30.45 ? 190 TYR A CD1 1 
ATOM   1457 C  CD2 . TYR A 1 190 ? -9.879  26.080 29.533  1.00 30.09 ? 190 TYR A CD2 1 
ATOM   1458 C  CE1 . TYR A 1 190 ? -10.812 27.945 27.700  1.00 30.57 ? 190 TYR A CE1 1 
ATOM   1459 C  CE2 . TYR A 1 190 ? -10.854 25.716 28.615  1.00 30.55 ? 190 TYR A CE2 1 
ATOM   1460 C  CZ  . TYR A 1 190 ? -11.313 26.654 27.699  1.00 30.57 ? 190 TYR A CZ  1 
ATOM   1461 O  OH  . TYR A 1 190 ? -12.274 26.303 26.782  1.00 30.37 ? 190 TYR A OH  1 
ATOM   1462 N  N   . PHE A 1 191 ? -5.400  29.912 31.168  1.00 29.48 ? 191 PHE A N   1 
ATOM   1463 C  CA  . PHE A 1 191 ? -4.521  30.413 32.227  1.00 28.94 ? 191 PHE A CA  1 
ATOM   1464 C  C   . PHE A 1 191 ? -4.895  31.811 32.646  1.00 28.76 ? 191 PHE A C   1 
ATOM   1465 O  O   . PHE A 1 191 ? -5.353  32.612 31.833  1.00 28.90 ? 191 PHE A O   1 
ATOM   1466 C  CB  . PHE A 1 191 ? -3.065  30.394 31.762  1.00 28.71 ? 191 PHE A CB  1 
ATOM   1467 C  CG  . PHE A 1 191 ? -2.102  30.993 32.742  1.00 28.53 ? 191 PHE A CG  1 
ATOM   1468 C  CD1 . PHE A 1 191 ? -1.764  30.324 33.907  1.00 29.04 ? 191 PHE A CD1 1 
ATOM   1469 C  CD2 . PHE A 1 191 ? -1.524  32.231 32.496  1.00 28.46 ? 191 PHE A CD2 1 
ATOM   1470 C  CE1 . PHE A 1 191 ? -0.863  30.886 34.815  1.00 28.73 ? 191 PHE A CE1 1 
ATOM   1471 C  CE2 . PHE A 1 191 ? -0.631  32.797 33.393  1.00 27.63 ? 191 PHE A CE2 1 
ATOM   1472 C  CZ  . PHE A 1 191 ? -0.298  32.122 34.551  1.00 28.15 ? 191 PHE A CZ  1 
ATOM   1473 N  N   . SER A 1 192 ? -4.683  32.083 33.929  1.00 28.64 ? 192 SER A N   1 
ATOM   1474 C  CA  . SER A 1 192 ? -4.938  33.385 34.557  1.00 28.62 ? 192 SER A CA  1 
ATOM   1475 C  C   . SER A 1 192 ? -6.399  33.832 34.588  1.00 28.49 ? 192 SER A C   1 
ATOM   1476 O  O   . SER A 1 192 ? -7.299  33.102 34.165  1.00 28.41 ? 192 SER A O   1 
ATOM   1477 C  CB  . SER A 1 192 ? -4.072  34.482 33.943  1.00 28.57 ? 192 SER A CB  1 
ATOM   1478 O  OG  . SER A 1 192 ? -4.221  35.679 34.689  1.00 29.37 ? 192 SER A OG  1 
ATOM   1479 N  N   . TYR A 1 193 ? -6.613  35.040 35.107  1.00 28.38 ? 193 TYR A N   1 
ATOM   1480 C  CA  . TYR A 1 193 ? -7.937  35.624 35.224  1.00 28.42 ? 193 TYR A CA  1 
ATOM   1481 C  C   . TYR A 1 193 ? -8.714  35.458 33.923  1.00 28.80 ? 193 TYR A C   1 
ATOM   1482 O  O   . TYR A 1 193 ? -9.771  34.821 33.884  1.00 28.61 ? 193 TYR A O   1 
ATOM   1483 C  CB  . TYR A 1 193 ? -7.835  37.113 35.544  1.00 28.05 ? 193 TYR A CB  1 
ATOM   1484 C  CG  . TYR A 1 193 ? -7.211  37.487 36.873  1.00 27.70 ? 193 TYR A CG  1 
ATOM   1485 C  CD1 . TYR A 1 193 ? -7.771  37.082 38.079  1.00 27.26 ? 193 TYR A CD1 1 
ATOM   1486 C  CD2 . TYR A 1 193 ? -6.086  38.310 36.921  1.00 27.87 ? 193 TYR A CD2 1 
ATOM   1487 C  CE1 . TYR A 1 193 ? -7.201  37.462 39.302  1.00 27.51 ? 193 TYR A CE1 1 
ATOM   1488 C  CE2 . TYR A 1 193 ? -5.518  38.697 38.130  1.00 27.09 ? 193 TYR A CE2 1 
ATOM   1489 C  CZ  . TYR A 1 193 ? -6.074  38.276 39.314  1.00 27.48 ? 193 TYR A CZ  1 
ATOM   1490 O  OH  . TYR A 1 193 ? -5.494  38.666 40.506  1.00 27.38 ? 193 TYR A OH  1 
ATOM   1491 N  N   . SER A 1 194 ? -8.157  36.022 32.854  1.00 29.32 ? 194 SER A N   1 
ATOM   1492 C  CA  . SER A 1 194 ? -8.828  36.080 31.560  1.00 29.65 ? 194 SER A CA  1 
ATOM   1493 C  C   . SER A 1 194 ? -9.143  34.689 31.005  1.00 29.63 ? 194 SER A C   1 
ATOM   1494 O  O   . SER A 1 194 ? -10.228 34.466 30.456  1.00 29.82 ? 194 SER A O   1 
ATOM   1495 C  CB  . SER A 1 194 ? -7.981  36.886 30.575  1.00 29.67 ? 194 SER A CB  1 
ATOM   1496 O  OG  . SER A 1 194 ? -8.781  37.346 29.502  1.00 30.81 ? 194 SER A OG  1 
ATOM   1497 N  N   . GLY A 1 195 ? -8.194  33.764 31.168  1.00 29.49 ? 195 GLY A N   1 
ATOM   1498 C  CA  . GLY A 1 195 ? -8.340  32.397 30.698  1.00 29.24 ? 195 GLY A CA  1 
ATOM   1499 C  C   . GLY A 1 195 ? -9.425  31.640 31.436  1.00 29.46 ? 195 GLY A C   1 
ATOM   1500 O  O   . GLY A 1 195 ? -10.236 30.955 30.819  1.00 29.58 ? 195 GLY A O   1 
ATOM   1501 N  N   . ALA A 1 196 ? -9.449  31.762 32.761  1.00 29.47 ? 196 ALA A N   1 
ATOM   1502 C  CA  . ALA A 1 196 ? -10.408 31.016 33.570  1.00 29.52 ? 196 ALA A CA  1 
ATOM   1503 C  C   . ALA A 1 196 ? -11.843 31.378 33.216  1.00 29.69 ? 196 ALA A C   1 
ATOM   1504 O  O   . ALA A 1 196 ? -12.706 30.503 33.150  1.00 29.89 ? 196 ALA A O   1 
ATOM   1505 C  CB  . ALA A 1 196 ? -10.152 31.223 35.046  1.00 29.46 ? 196 ALA A CB  1 
ATOM   1506 N  N   . PHE A 1 197 ? -12.092 32.663 32.985  1.00 29.87 ? 197 PHE A N   1 
ATOM   1507 C  CA  . PHE A 1 197 ? -13.390 33.122 32.491  1.00 29.99 ? 197 PHE A CA  1 
ATOM   1508 C  C   . PHE A 1 197 ? -13.722 32.495 31.116  1.00 30.51 ? 197 PHE A C   1 
ATOM   1509 O  O   . PHE A 1 197 ? -14.868 32.093 30.872  1.00 30.62 ? 197 PHE A O   1 
ATOM   1510 C  CB  . PHE A 1 197 ? -13.432 34.661 32.448  1.00 29.61 ? 197 PHE A CB  1 
ATOM   1511 C  CG  . PHE A 1 197 ? -14.815 35.243 32.248  1.00 28.89 ? 197 PHE A CG  1 
ATOM   1512 C  CD1 . PHE A 1 197 ? -15.883 34.859 33.061  1.00 28.54 ? 197 PHE A CD1 1 
ATOM   1513 C  CD2 . PHE A 1 197 ? -15.039 36.195 31.262  1.00 27.86 ? 197 PHE A CD2 1 
ATOM   1514 C  CE1 . PHE A 1 197 ? -17.152 35.401 32.878  1.00 28.34 ? 197 PHE A CE1 1 
ATOM   1515 C  CE2 . PHE A 1 197 ? -16.301 36.742 31.073  1.00 27.70 ? 197 PHE A CE2 1 
ATOM   1516 C  CZ  . PHE A 1 197 ? -17.358 36.347 31.882  1.00 28.37 ? 197 PHE A CZ  1 
ATOM   1517 N  N   . LYS A 1 198 ? -12.725 32.385 30.234  1.00 30.75 ? 198 LYS A N   1 
ATOM   1518 C  CA  . LYS A 1 198 ? -12.948 31.768 28.930  1.00 31.20 ? 198 LYS A CA  1 
ATOM   1519 C  C   . LYS A 1 198 ? -13.374 30.318 29.081  1.00 30.99 ? 198 LYS A C   1 
ATOM   1520 O  O   . LYS A 1 198 ? -14.233 29.848 28.350  1.00 30.96 ? 198 LYS A O   1 
ATOM   1521 C  CB  . LYS A 1 198 ? -11.710 31.866 28.036  1.00 31.60 ? 198 LYS A CB  1 
ATOM   1522 C  CG  . LYS A 1 198 ? -12.065 31.956 26.551  1.00 33.25 ? 198 LYS A CG  1 
ATOM   1523 C  CD  . LYS A 1 198 ? -11.015 31.328 25.641  1.00 36.17 ? 198 LYS A CD  1 
ATOM   1524 C  CE  . LYS A 1 198 ? -11.584 31.178 24.224  1.00 38.30 ? 198 LYS A CE  1 
ATOM   1525 N  NZ  . LYS A 1 198 ? -10.848 30.193 23.366  1.00 39.56 ? 198 LYS A NZ  1 
ATOM   1526 N  N   . CYS A 1 199 ? -12.771 29.624 30.042  1.00 31.22 ? 199 CYS A N   1 
ATOM   1527 C  CA  . CYS A 1 199 ? -13.146 28.254 30.400  1.00 31.32 ? 199 CYS A CA  1 
ATOM   1528 C  C   . CYS A 1 199 ? -14.622 28.139 30.797  1.00 31.30 ? 199 CYS A C   1 
ATOM   1529 O  O   . CYS A 1 199 ? -15.253 27.106 30.576  1.00 31.22 ? 199 CYS A O   1 
ATOM   1530 C  CB  . CYS A 1 199 ? -12.237 27.745 31.525  1.00 31.35 ? 199 CYS A CB  1 
ATOM   1531 S  SG  . CYS A 1 199 ? -12.723 26.197 32.345  1.00 31.70 ? 199 CYS A SG  1 
ATOM   1532 N  N   . LEU A 1 200 ? -15.164 29.200 31.384  1.00 31.45 ? 200 LEU A N   1 
ATOM   1533 C  CA  . LEU A 1 200 ? -16.586 29.244 31.703  1.00 31.87 ? 200 LEU A CA  1 
ATOM   1534 C  C   . LEU A 1 200 ? -17.427 29.646 30.491  1.00 32.15 ? 200 LEU A C   1 
ATOM   1535 O  O   . LEU A 1 200 ? -18.457 29.028 30.216  1.00 32.34 ? 200 LEU A O   1 
ATOM   1536 C  CB  . LEU A 1 200 ? -16.867 30.190 32.874  1.00 31.86 ? 200 LEU A CB  1 
ATOM   1537 C  CG  . LEU A 1 200 ? -18.350 30.358 33.227  1.00 31.82 ? 200 LEU A CG  1 
ATOM   1538 C  CD1 . LEU A 1 200 ? -18.879 29.136 33.962  1.00 31.95 ? 200 LEU A CD1 1 
ATOM   1539 C  CD2 . LEU A 1 200 ? -18.587 31.621 34.036  1.00 32.11 ? 200 LEU A CD2 1 
ATOM   1540 N  N   . ARG A 1 201 ? -16.987 30.681 29.781  1.00 32.35 ? 201 ARG A N   1 
ATOM   1541 C  CA  . ARG A 1 201 ? -17.684 31.162 28.591  1.00 32.82 ? 201 ARG A CA  1 
ATOM   1542 C  C   . ARG A 1 201 ? -17.907 30.087 27.519  1.00 32.73 ? 201 ARG A C   1 
ATOM   1543 O  O   . ARG A 1 201 ? -18.986 30.025 26.926  1.00 32.83 ? 201 ARG A O   1 
ATOM   1544 C  CB  . ARG A 1 201 ? -16.948 32.354 27.978  1.00 33.16 ? 201 ARG A CB  1 
ATOM   1545 C  CG  . ARG A 1 201 ? -17.150 33.665 28.721  1.00 34.44 ? 201 ARG A CG  1 
ATOM   1546 C  CD  . ARG A 1 201 ? -16.844 34.827 27.812  1.00 36.47 ? 201 ARG A CD  1 
ATOM   1547 N  NE  . ARG A 1 201 ? -15.442 34.812 27.417  1.00 38.38 ? 201 ARG A NE  1 
ATOM   1548 C  CZ  . ARG A 1 201 ? -14.981 35.223 26.240  1.00 39.63 ? 201 ARG A CZ  1 
ATOM   1549 N  NH1 . ARG A 1 201 ? -15.809 35.685 25.307  1.00 39.83 ? 201 ARG A NH1 1 
ATOM   1550 N  NH2 . ARG A 1 201 ? -13.678 35.159 25.995  1.00 40.82 ? 201 ARG A NH2 1 
ATOM   1551 N  N   . ASP A 1 202 ? -16.897 29.247 27.277  1.00 32.52 ? 202 ASP A N   1 
ATOM   1552 C  CA  . ASP A 1 202 ? -16.967 28.210 26.235  1.00 32.18 ? 202 ASP A CA  1 
ATOM   1553 C  C   . ASP A 1 202 ? -17.909 27.059 26.598  1.00 32.04 ? 202 ASP A C   1 
ATOM   1554 O  O   . ASP A 1 202 ? -18.191 26.189 25.775  1.00 32.04 ? 202 ASP A O   1 
ATOM   1555 C  CB  . ASP A 1 202 ? -15.566 27.683 25.905  1.00 32.04 ? 202 ASP A CB  1 
ATOM   1556 C  CG  . ASP A 1 202 ? -14.668 28.745 25.272  1.00 32.08 ? 202 ASP A CG  1 
ATOM   1557 O  OD1 . ASP A 1 202 ? -15.112 29.897 25.102  1.00 31.55 ? 202 ASP A OD1 1 
ATOM   1558 O  OD2 . ASP A 1 202 ? -13.505 28.431 24.940  1.00 32.81 ? 202 ASP A OD2 1 
ATOM   1559 N  N   . GLY A 1 203 ? -18.395 27.071 27.836  1.00 31.92 ? 203 GLY A N   1 
ATOM   1560 C  CA  . GLY A 1 203 ? -19.307 26.047 28.328  1.00 31.76 ? 203 GLY A CA  1 
ATOM   1561 C  C   . GLY A 1 203 ? -18.561 24.855 28.886  1.00 31.50 ? 203 GLY A C   1 
ATOM   1562 O  O   . GLY A 1 203 ? -19.158 23.822 29.190  1.00 31.67 ? 203 GLY A O   1 
ATOM   1563 N  N   . ALA A 1 204 ? -17.248 25.003 29.021  1.00 31.12 ? 204 ALA A N   1 
ATOM   1564 C  CA  . ALA A 1 204 ? -16.404 23.923 29.496  1.00 30.69 ? 204 ALA A CA  1 
ATOM   1565 C  C   . ALA A 1 204 ? -16.511 23.738 31.004  1.00 30.35 ? 204 ALA A C   1 
ATOM   1566 O  O   . ALA A 1 204 ? -16.435 22.617 31.494  1.00 30.42 ? 204 ALA A O   1 
ATOM   1567 C  CB  . ALA A 1 204 ? -14.973 24.161 29.086  1.00 30.82 ? 204 ALA A CB  1 
ATOM   1568 N  N   . GLY A 1 205 ? -16.685 24.837 31.731  1.00 29.93 ? 205 GLY A N   1 
ATOM   1569 C  CA  . GLY A 1 205 ? -16.835 24.782 33.181  1.00 29.62 ? 205 GLY A CA  1 
ATOM   1570 C  C   . GLY A 1 205 ? -18.196 25.237 33.679  1.00 29.44 ? 205 GLY A C   1 
ATOM   1571 O  O   . GLY A 1 205 ? -19.076 25.585 32.892  1.00 29.52 ? 205 GLY A O   1 
ATOM   1572 N  N   . ASP A 1 206 ? -18.360 25.232 34.998  1.00 29.24 ? 206 ASP A N   1 
ATOM   1573 C  CA  . ASP A 1 206 ? -19.588 25.690 35.641  1.00 29.24 ? 206 ASP A CA  1 
ATOM   1574 C  C   . ASP A 1 206 ? -19.353 26.889 36.556  1.00 28.95 ? 206 ASP A C   1 
ATOM   1575 O  O   . ASP A 1 206 ? -20.260 27.683 36.776  1.00 28.95 ? 206 ASP A O   1 
ATOM   1576 C  CB  . ASP A 1 206 ? -20.223 24.557 36.445  1.00 29.49 ? 206 ASP A CB  1 
ATOM   1577 C  CG  . ASP A 1 206 ? -20.704 23.419 35.568  1.00 30.45 ? 206 ASP A CG  1 
ATOM   1578 O  OD1 . ASP A 1 206 ? -21.635 23.645 34.761  1.00 31.36 ? 206 ASP A OD1 1 
ATOM   1579 O  OD2 . ASP A 1 206 ? -20.159 22.297 35.693  1.00 31.54 ? 206 ASP A OD2 1 
ATOM   1580 N  N   . VAL A 1 207 ? -18.140 27.003 37.092  1.00 28.58 ? 207 VAL A N   1 
ATOM   1581 C  CA  . VAL A 1 207 ? -17.775 28.106 37.978  1.00 28.17 ? 207 VAL A CA  1 
ATOM   1582 C  C   . VAL A 1 207 ? -16.361 28.599 37.664  1.00 28.13 ? 207 VAL A C   1 
ATOM   1583 O  O   . VAL A 1 207 ? -15.449 27.805 37.400  1.00 28.37 ? 207 VAL A O   1 
ATOM   1584 C  CB  . VAL A 1 207 ? -17.944 27.731 39.492  1.00 28.21 ? 207 VAL A CB  1 
ATOM   1585 C  CG1 . VAL A 1 207 ? -17.034 26.579 39.892  1.00 27.84 ? 207 VAL A CG1 1 
ATOM   1586 C  CG2 . VAL A 1 207 ? -17.726 28.943 40.403  1.00 27.48 ? 207 VAL A CG2 1 
ATOM   1587 N  N   . ALA A 1 208 ? -16.206 29.919 37.667  1.00 27.79 ? 208 ALA A N   1 
ATOM   1588 C  CA  . ALA A 1 208 ? -14.940 30.569 37.371  1.00 27.23 ? 208 ALA A CA  1 
ATOM   1589 C  C   . ALA A 1 208 ? -14.517 31.318 38.616  1.00 27.09 ? 208 ALA A C   1 
ATOM   1590 O  O   . ALA A 1 208 ? -15.281 32.144 39.139  1.00 27.16 ? 208 ALA A O   1 
ATOM   1591 C  CB  . ALA A 1 208 ? -15.095 31.524 36.207  1.00 27.07 ? 208 ALA A CB  1 
ATOM   1592 N  N   . PHE A 1 209 ? -13.316 30.999 39.103  1.00 26.56 ? 209 PHE A N   1 
ATOM   1593 C  CA  . PHE A 1 209 ? -12.756 31.620 40.292  1.00 25.87 ? 209 PHE A CA  1 
ATOM   1594 C  C   . PHE A 1 209 ? -11.756 32.671 39.876  1.00 26.12 ? 209 PHE A C   1 
ATOM   1595 O  O   . PHE A 1 209 ? -10.604 32.372 39.585  1.00 26.24 ? 209 PHE A O   1 
ATOM   1596 C  CB  . PHE A 1 209 ? -12.118 30.576 41.197  1.00 25.31 ? 209 PHE A CB  1 
ATOM   1597 C  CG  . PHE A 1 209 ? -13.104 29.624 41.796  1.00 24.67 ? 209 PHE A CG  1 
ATOM   1598 C  CD1 . PHE A 1 209 ? -14.103 30.077 42.641  1.00 23.69 ? 209 PHE A CD1 1 
ATOM   1599 C  CD2 . PHE A 1 209 ? -13.040 28.273 41.515  1.00 24.86 ? 209 PHE A CD2 1 
ATOM   1600 C  CE1 . PHE A 1 209 ? -15.017 29.200 43.196  1.00 23.31 ? 209 PHE A CE1 1 
ATOM   1601 C  CE2 . PHE A 1 209 ? -13.954 27.386 42.077  1.00 24.14 ? 209 PHE A CE2 1 
ATOM   1602 C  CZ  . PHE A 1 209 ? -14.941 27.854 42.914  1.00 23.77 ? 209 PHE A CZ  1 
ATOM   1603 N  N   . ILE A 1 210 ? -12.224 33.911 39.846  1.00 26.55 ? 210 ILE A N   1 
ATOM   1604 C  CA  . ILE A 1 210 ? -11.457 35.028 39.326  1.00 26.83 ? 210 ILE A CA  1 
ATOM   1605 C  C   . ILE A 1 210 ? -11.712 36.290 40.129  1.00 27.37 ? 210 ILE A C   1 
ATOM   1606 O  O   . ILE A 1 210 ? -12.339 36.254 41.188  1.00 27.60 ? 210 ILE A O   1 
ATOM   1607 C  CB  . ILE A 1 210 ? -11.768 35.302 37.820  1.00 26.85 ? 210 ILE A CB  1 
ATOM   1608 C  CG1 . ILE A 1 210 ? -13.287 35.391 37.581  1.00 26.63 ? 210 ILE A CG1 1 
ATOM   1609 C  CG2 . ILE A 1 210 ? -11.096 34.246 36.939  1.00 26.72 ? 210 ILE A CG2 1 
ATOM   1610 C  CD1 . ILE A 1 210 ? -13.709 35.705 36.152  1.00 26.45 ? 210 ILE A CD1 1 
ATOM   1611 N  N   . ARG A 1 211 ? -11.219 37.401 39.588  1.00 27.82 ? 211 ARG A N   1 
ATOM   1612 C  CA  . ARG A 1 211 ? -11.231 38.704 40.216  1.00 28.12 ? 211 ARG A CA  1 
ATOM   1613 C  C   . ARG A 1 211 ? -12.480 39.455 39.734  1.00 28.68 ? 211 ARG A C   1 
ATOM   1614 O  O   . ARG A 1 211 ? -13.022 39.144 38.673  1.00 28.81 ? 211 ARG A O   1 
ATOM   1615 C  CB  . ARG A 1 211 ? -9.919  39.400 39.833  1.00 27.95 ? 211 ARG A CB  1 
ATOM   1616 C  CG  . ARG A 1 211 ? -9.925  40.905 39.682  1.00 28.43 ? 211 ARG A CG  1 
ATOM   1617 C  CD  . ARG A 1 211 ? -8.723  41.391 38.907  1.00 28.08 ? 211 ARG A CD  1 
ATOM   1618 N  NE  . ARG A 1 211 ? -7.468  41.008 39.539  1.00 29.15 ? 211 ARG A NE  1 
ATOM   1619 C  CZ  . ARG A 1 211 ? -6.587  41.857 40.065  1.00 30.20 ? 211 ARG A CZ  1 
ATOM   1620 N  NH1 . ARG A 1 211 ? -6.813  43.166 40.041  1.00 30.61 ? 211 ARG A NH1 1 
ATOM   1621 N  NH2 . ARG A 1 211 ? -5.463  41.396 40.603  1.00 29.42 ? 211 ARG A NH2 1 
ATOM   1622 N  N   . GLU A 1 212 ? -12.945 40.429 40.511  1.00 29.25 ? 212 GLU A N   1 
ATOM   1623 C  CA  . GLU A 1 212 ? -14.192 41.120 40.195  1.00 29.98 ? 212 GLU A CA  1 
ATOM   1624 C  C   . GLU A 1 212 ? -14.207 41.871 38.850  1.00 30.43 ? 212 GLU A C   1 
ATOM   1625 O  O   . GLU A 1 212 ? -15.256 41.992 38.229  1.00 30.86 ? 212 GLU A O   1 
ATOM   1626 C  CB  . GLU A 1 212 ? -14.607 42.047 41.343  1.00 30.02 ? 212 GLU A CB  1 
ATOM   1627 C  CG  . GLU A 1 212 ? -14.153 43.505 41.220  1.00 31.29 ? 212 GLU A CG  1 
ATOM   1628 C  CD  . GLU A 1 212 ? -12.710 43.737 41.649  1.00 32.55 ? 212 GLU A CD  1 
ATOM   1629 O  OE1 . GLU A 1 212 ? -12.479 44.613 42.516  1.00 33.33 ? 212 GLU A OE1 1 
ATOM   1630 O  OE2 . GLU A 1 212 ? -11.807 43.055 41.119  1.00 32.28 ? 212 GLU A OE2 1 
ATOM   1631 N  N   . SER A 1 213 ? -13.061 42.363 38.389  1.00 30.68 ? 213 SER A N   1 
ATOM   1632 C  CA  . SER A 1 213 ? -13.052 43.220 37.207  1.00 30.99 ? 213 SER A CA  1 
ATOM   1633 C  C   . SER A 1 213 ? -12.982 42.451 35.893  1.00 31.32 ? 213 SER A C   1 
ATOM   1634 O  O   . SER A 1 213 ? -13.250 43.006 34.832  1.00 31.37 ? 213 SER A O   1 
ATOM   1635 C  CB  . SER A 1 213 ? -11.903 44.212 37.288  1.00 30.98 ? 213 SER A CB  1 
ATOM   1636 O  OG  . SER A 1 213 ? -10.675 43.524 37.408  1.00 31.57 ? 213 SER A OG  1 
ATOM   1637 N  N   . THR A 1 214 ? -12.624 41.174 35.963  1.00 31.87 ? 214 THR A N   1 
ATOM   1638 C  CA  . THR A 1 214 ? -12.426 40.360 34.762  1.00 32.24 ? 214 THR A CA  1 
ATOM   1639 C  C   . THR A 1 214 ? -13.654 40.357 33.855  1.00 32.64 ? 214 THR A C   1 
ATOM   1640 O  O   . THR A 1 214 ? -13.540 40.620 32.661  1.00 32.80 ? 214 THR A O   1 
ATOM   1641 C  CB  . THR A 1 214 ? -11.981 38.933 35.119  1.00 31.99 ? 214 THR A CB  1 
ATOM   1642 O  OG1 . THR A 1 214 ? -10.713 39.009 35.778  1.00 33.06 ? 214 THR A OG1 1 
ATOM   1643 C  CG2 . THR A 1 214 ? -11.832 38.072 33.883  1.00 31.25 ? 214 THR A CG2 1 
ATOM   1644 N  N   . VAL A 1 215 ? -14.823 40.085 34.423  1.00 33.05 ? 215 VAL A N   1 
ATOM   1645 C  CA  . VAL A 1 215 ? -16.049 40.024 33.627  1.00 33.48 ? 215 VAL A CA  1 
ATOM   1646 C  C   . VAL A 1 215 ? -16.327 41.343 32.875  1.00 33.77 ? 215 VAL A C   1 
ATOM   1647 O  O   . VAL A 1 215 ? -16.877 41.327 31.780  1.00 33.58 ? 215 VAL A O   1 
ATOM   1648 C  CB  . VAL A 1 215 ? -17.273 39.493 34.464  1.00 33.45 ? 215 VAL A CB  1 
ATOM   1649 C  CG1 . VAL A 1 215 ? -17.541 40.360 35.699  1.00 33.78 ? 215 VAL A CG1 1 
ATOM   1650 C  CG2 . VAL A 1 215 ? -18.520 39.352 33.604  1.00 33.24 ? 215 VAL A CG2 1 
ATOM   1651 N  N   . PHE A 1 216 ? -15.908 42.469 33.450  1.00 34.43 ? 216 PHE A N   1 
ATOM   1652 C  CA  . PHE A 1 216 ? -16.060 43.769 32.802  1.00 35.20 ? 216 PHE A CA  1 
ATOM   1653 C  C   . PHE A 1 216 ? -14.998 44.022 31.741  1.00 36.38 ? 216 PHE A C   1 
ATOM   1654 O  O   . PHE A 1 216 ? -15.239 44.742 30.781  1.00 36.60 ? 216 PHE A O   1 
ATOM   1655 C  CB  . PHE A 1 216 ? -16.020 44.886 33.830  1.00 34.60 ? 216 PHE A CB  1 
ATOM   1656 C  CG  . PHE A 1 216 ? -17.161 44.857 34.782  1.00 34.31 ? 216 PHE A CG  1 
ATOM   1657 C  CD1 . PHE A 1 216 ? -18.351 45.498 34.474  1.00 33.97 ? 216 PHE A CD1 1 
ATOM   1658 C  CD2 . PHE A 1 216 ? -17.055 44.187 35.992  1.00 34.31 ? 216 PHE A CD2 1 
ATOM   1659 C  CE1 . PHE A 1 216 ? -19.421 45.473 35.363  1.00 34.04 ? 216 PHE A CE1 1 
ATOM   1660 C  CE2 . PHE A 1 216 ? -18.121 44.154 36.887  1.00 33.85 ? 216 PHE A CE2 1 
ATOM   1661 C  CZ  . PHE A 1 216 ? -19.304 44.795 36.571  1.00 34.03 ? 216 PHE A CZ  1 
ATOM   1662 N  N   . GLU A 1 217 ? -13.820 43.439 31.929  1.00 37.88 ? 217 GLU A N   1 
ATOM   1663 C  CA  . GLU A 1 217 ? -12.717 43.587 30.991  1.00 39.51 ? 217 GLU A CA  1 
ATOM   1664 C  C   . GLU A 1 217 ? -12.964 42.817 29.697  1.00 39.81 ? 217 GLU A C   1 
ATOM   1665 O  O   . GLU A 1 217 ? -12.649 43.308 28.614  1.00 40.07 ? 217 GLU A O   1 
ATOM   1666 C  CB  . GLU A 1 217 ? -11.406 43.107 31.628  1.00 39.44 ? 217 GLU A CB  1 
ATOM   1667 C  CG  . GLU A 1 217 ? -10.763 44.091 32.611  1.00 40.83 ? 217 GLU A CG  1 
ATOM   1668 C  CD  . GLU A 1 217 ? -9.778  43.419 33.584  1.00 41.45 ? 217 GLU A CD  1 
ATOM   1669 O  OE1 . GLU A 1 217 ? -9.278  42.304 33.275  1.00 44.00 ? 217 GLU A OE1 1 
ATOM   1670 O  OE2 . GLU A 1 217 ? -9.508  44.009 34.664  1.00 43.16 ? 217 GLU A OE2 1 
ATOM   1671 N  N   . ASP A 1 218 ? -13.520 41.613 29.813  1.00 40.51 ? 218 ASP A N   1 
ATOM   1672 C  CA  . ASP A 1 218 ? -13.688 40.725 28.668  1.00 41.35 ? 218 ASP A CA  1 
ATOM   1673 C  C   . ASP A 1 218 ? -14.999 40.971 27.922  1.00 41.72 ? 218 ASP A C   1 
ATOM   1674 O  O   . ASP A 1 218 ? -15.074 40.789 26.711  1.00 41.82 ? 218 ASP A O   1 
ATOM   1675 C  CB  . ASP A 1 218 ? -13.579 39.254 29.096  1.00 41.56 ? 218 ASP A CB  1 
ATOM   1676 C  CG  . ASP A 1 218 ? -12.141 38.829 29.448  1.00 42.71 ? 218 ASP A CG  1 
ATOM   1677 O  OD1 . ASP A 1 218 ? -11.316 39.688 29.838  1.00 43.78 ? 218 ASP A OD1 1 
ATOM   1678 O  OD2 . ASP A 1 218 ? -11.838 37.615 29.347  1.00 43.80 ? 218 ASP A OD2 1 
ATOM   1679 N  N   . LEU A 1 219 ? -16.031 41.388 28.640  1.00 42.35 ? 219 LEU A N   1 
ATOM   1680 C  CA  . LEU A 1 219 ? -17.330 41.614 28.018  1.00 43.10 ? 219 LEU A CA  1 
ATOM   1681 C  C   . LEU A 1 219 ? -17.764 43.075 28.066  1.00 43.66 ? 219 LEU A C   1 
ATOM   1682 O  O   . LEU A 1 219 ? -18.098 43.615 29.131  1.00 43.73 ? 219 LEU A O   1 
ATOM   1683 C  CB  . LEU A 1 219 ? -18.391 40.708 28.635  1.00 43.07 ? 219 LEU A CB  1 
ATOM   1684 C  CG  . LEU A 1 219 ? -18.133 39.213 28.456  1.00 43.57 ? 219 LEU A CG  1 
ATOM   1685 C  CD1 . LEU A 1 219 ? -19.285 38.419 29.049  1.00 43.68 ? 219 LEU A CD1 1 
ATOM   1686 C  CD2 . LEU A 1 219 ? -17.908 38.857 26.982  1.00 43.56 ? 219 LEU A CD2 1 
ATOM   1687 N  N   . SER A 1 220 ? -17.760 43.699 26.891  1.00 44.21 ? 220 SER A N   1 
ATOM   1688 C  CA  . SER A 1 220 ? -18.055 45.119 26.753  1.00 44.69 ? 220 SER A CA  1 
ATOM   1689 C  C   . SER A 1 220 ? -19.550 45.438 26.821  1.00 44.95 ? 220 SER A C   1 
ATOM   1690 O  O   . SER A 1 220 ? -19.933 46.501 27.308  1.00 44.94 ? 220 SER A O   1 
ATOM   1691 C  CB  . SER A 1 220 ? -17.445 45.659 25.458  1.00 44.73 ? 220 SER A CB  1 
ATOM   1692 O  OG  . SER A 1 220 ? -17.535 44.700 24.417  1.00 45.21 ? 220 SER A OG  1 
ATOM   1693 N  N   . ASP A 1 221 ? -20.389 44.521 26.346  1.00 45.23 ? 221 ASP A N   1 
ATOM   1694 C  CA  . ASP A 1 221 ? -21.824 44.776 26.296  1.00 45.68 ? 221 ASP A CA  1 
ATOM   1695 C  C   . ASP A 1 221 ? -22.563 44.321 27.557  1.00 45.86 ? 221 ASP A C   1 
ATOM   1696 O  O   . ASP A 1 221 ? -22.456 43.161 27.968  1.00 45.90 ? 221 ASP A O   1 
ATOM   1697 C  CB  . ASP A 1 221 ? -22.443 44.142 25.047  1.00 45.87 ? 221 ASP A CB  1 
ATOM   1698 C  CG  . ASP A 1 221 ? -23.950 44.369 24.956  1.00 46.48 ? 221 ASP A CG  1 
ATOM   1699 O  OD1 . ASP A 1 221 ? -24.410 45.511 25.179  1.00 47.29 ? 221 ASP A OD1 1 
ATOM   1700 O  OD2 . ASP A 1 221 ? -24.679 43.401 24.655  1.00 47.07 ? 221 ASP A OD2 1 
ATOM   1701 N  N   . GLU A 1 222 ? -23.333 45.244 28.139  1.00 45.99 ? 222 GLU A N   1 
ATOM   1702 C  CA  . GLU A 1 222 ? -24.124 45.001 29.360  1.00 46.14 ? 222 GLU A CA  1 
ATOM   1703 C  C   . GLU A 1 222 ? -25.102 43.826 29.240  1.00 45.71 ? 222 GLU A C   1 
ATOM   1704 O  O   . GLU A 1 222 ? -25.370 43.137 30.222  1.00 45.73 ? 222 GLU A O   1 
ATOM   1705 C  CB  . GLU A 1 222 ? -24.883 46.275 29.780  1.00 46.10 ? 222 GLU A CB  1 
ATOM   1706 C  CG  . GLU A 1 222 ? -26.113 46.590 28.918  1.00 46.91 ? 222 GLU A CG  1 
ATOM   1707 C  CD  . GLU A 1 222 ? -26.781 47.909 29.268  1.00 46.98 ? 222 GLU A CD  1 
ATOM   1708 O  OE1 . GLU A 1 222 ? -26.378 48.950 28.694  1.00 47.56 ? 222 GLU A OE1 1 
ATOM   1709 O  OE2 . GLU A 1 222 ? -27.726 47.897 30.095  1.00 47.74 ? 222 GLU A OE2 1 
ATOM   1710 N  N   . ALA A 1 223 ? -25.632 43.612 28.038  1.00 45.42 ? 223 ALA A N   1 
ATOM   1711 C  CA  . ALA A 1 223 ? -26.595 42.546 27.800  1.00 45.02 ? 223 ALA A CA  1 
ATOM   1712 C  C   . ALA A 1 223 ? -25.924 41.185 27.903  1.00 44.79 ? 223 ALA A C   1 
ATOM   1713 O  O   . ALA A 1 223 ? -26.568 40.206 28.282  1.00 44.75 ? 223 ALA A O   1 
ATOM   1714 C  CB  . ALA A 1 223 ? -27.264 42.718 26.449  1.00 44.96 ? 223 ALA A CB  1 
ATOM   1715 N  N   . GLU A 1 224 ? -24.633 41.132 27.572  1.00 44.48 ? 224 GLU A N   1 
ATOM   1716 C  CA  . GLU A 1 224 ? -23.847 39.909 27.712  1.00 44.28 ? 224 GLU A CA  1 
ATOM   1717 C  C   . GLU A 1 224 ? -23.511 39.648 29.172  1.00 43.84 ? 224 GLU A C   1 
ATOM   1718 O  O   . GLU A 1 224 ? -23.518 38.502 29.618  1.00 43.89 ? 224 GLU A O   1 
ATOM   1719 C  CB  . GLU A 1 224 ? -22.574 39.967 26.870  1.00 44.34 ? 224 GLU A CB  1 
ATOM   1720 C  CG  . GLU A 1 224 ? -22.747 39.440 25.449  1.00 45.79 ? 224 GLU A CG  1 
ATOM   1721 C  CD  . GLU A 1 224 ? -21.785 40.084 24.442  1.00 48.00 ? 224 GLU A CD  1 
ATOM   1722 O  OE1 . GLU A 1 224 ? -20.644 40.438 24.830  1.00 48.87 ? 224 GLU A OE1 1 
ATOM   1723 O  OE2 . GLU A 1 224 ? -22.173 40.238 23.258  1.00 47.89 ? 224 GLU A OE2 1 
ATOM   1724 N  N   . ARG A 1 225 ? -23.235 40.716 29.915  1.00 43.33 ? 225 ARG A N   1 
ATOM   1725 C  CA  . ARG A 1 225 ? -22.908 40.605 31.337  1.00 42.86 ? 225 ARG A CA  1 
ATOM   1726 C  C   . ARG A 1 225 ? -24.117 40.246 32.198  1.00 42.51 ? 225 ARG A C   1 
ATOM   1727 O  O   . ARG A 1 225 ? -23.959 39.674 33.275  1.00 42.49 ? 225 ARG A O   1 
ATOM   1728 C  CB  . ARG A 1 225 ? -22.258 41.889 31.844  1.00 42.83 ? 225 ARG A CB  1 
ATOM   1729 C  CG  . ARG A 1 225 ? -20.874 42.146 31.267  1.00 42.82 ? 225 ARG A CG  1 
ATOM   1730 C  CD  . ARG A 1 225 ? -20.160 43.253 32.023  1.00 42.82 ? 225 ARG A CD  1 
ATOM   1731 N  NE  . ARG A 1 225 ? -20.936 44.491 32.040  1.00 43.05 ? 225 ARG A NE  1 
ATOM   1732 C  CZ  . ARG A 1 225 ? -20.738 45.518 31.219  1.00 43.21 ? 225 ARG A CZ  1 
ATOM   1733 N  NH1 . ARG A 1 225 ? -19.778 45.481 30.297  1.00 42.79 ? 225 ARG A NH1 1 
ATOM   1734 N  NH2 . ARG A 1 225 ? -21.507 46.591 31.325  1.00 43.34 ? 225 ARG A NH2 1 
ATOM   1735 N  N   . ASP A 1 226 ? -25.315 40.585 31.719  1.00 42.16 ? 226 ASP A N   1 
ATOM   1736 C  CA  . ASP A 1 226 ? -26.573 40.172 32.350  1.00 41.78 ? 226 ASP A CA  1 
ATOM   1737 C  C   . ASP A 1 226 ? -26.784 38.658 32.264  1.00 41.32 ? 226 ASP A C   1 
ATOM   1738 O  O   . ASP A 1 226 ? -27.684 38.118 32.908  1.00 41.14 ? 226 ASP A O   1 
ATOM   1739 C  CB  . ASP A 1 226 ? -27.769 40.908 31.724  1.00 42.04 ? 226 ASP A CB  1 
ATOM   1740 C  CG  . ASP A 1 226 ? -28.146 42.193 32.475  1.00 42.94 ? 226 ASP A CG  1 
ATOM   1741 O  OD1 . ASP A 1 226 ? -28.496 43.197 31.809  1.00 43.42 ? 226 ASP A OD1 1 
ATOM   1742 O  OD2 . ASP A 1 226 ? -28.108 42.203 33.727  1.00 43.70 ? 226 ASP A OD2 1 
ATOM   1743 N  N   . GLU A 1 227 ? -25.946 37.986 31.473  1.00 40.88 ? 227 GLU A N   1 
ATOM   1744 C  CA  . GLU A 1 227 ? -25.999 36.529 31.309  1.00 40.71 ? 227 GLU A CA  1 
ATOM   1745 C  C   . GLU A 1 227 ? -25.097 35.771 32.298  1.00 39.91 ? 227 GLU A C   1 
ATOM   1746 O  O   . GLU A 1 227 ? -24.986 34.547 32.233  1.00 39.83 ? 227 GLU A O   1 
ATOM   1747 C  CB  . GLU A 1 227 ? -25.690 36.134 29.854  1.00 40.60 ? 227 GLU A CB  1 
ATOM   1748 C  CG  . GLU A 1 227 ? -26.848 36.431 28.875  1.00 41.66 ? 227 GLU A CG  1 
ATOM   1749 C  CD  . GLU A 1 227 ? -26.532 36.081 27.406  1.00 41.98 ? 227 GLU A CD  1 
ATOM   1750 O  OE1 . GLU A 1 227 ? -27.485 35.687 26.663  1.00 43.41 ? 227 GLU A OE1 1 
ATOM   1751 O  OE2 . GLU A 1 227 ? -25.348 36.214 26.985  1.00 43.42 ? 227 GLU A OE2 1 
ATOM   1752 N  N   . TYR A 1 228 ? -24.477 36.507 33.220  1.00 39.25 ? 228 TYR A N   1 
ATOM   1753 C  CA  . TYR A 1 228 ? -23.606 35.926 34.245  1.00 38.47 ? 228 TYR A CA  1 
ATOM   1754 C  C   . TYR A 1 228 ? -23.975 36.411 35.649  1.00 38.12 ? 228 TYR A C   1 
ATOM   1755 O  O   . TYR A 1 228 ? -24.565 37.486 35.817  1.00 37.98 ? 228 TYR A O   1 
ATOM   1756 C  CB  . TYR A 1 228 ? -22.136 36.235 33.953  1.00 38.35 ? 228 TYR A CB  1 
ATOM   1757 C  CG  . TYR A 1 228 ? -21.620 35.590 32.698  1.00 38.32 ? 228 TYR A CG  1 
ATOM   1758 C  CD1 . TYR A 1 228 ? -21.060 34.315 32.726  1.00 38.81 ? 228 TYR A CD1 1 
ATOM   1759 C  CD2 . TYR A 1 228 ? -21.694 36.250 31.476  1.00 38.60 ? 228 TYR A CD2 1 
ATOM   1760 C  CE1 . TYR A 1 228 ? -20.586 33.709 31.560  1.00 38.85 ? 228 TYR A CE1 1 
ATOM   1761 C  CE2 . TYR A 1 228 ? -21.231 35.654 30.305  1.00 38.68 ? 228 TYR A CE2 1 
ATOM   1762 C  CZ  . TYR A 1 228 ? -20.675 34.387 30.353  1.00 38.43 ? 228 TYR A CZ  1 
ATOM   1763 O  OH  . TYR A 1 228 ? -20.215 33.809 29.194  1.00 37.86 ? 228 TYR A OH  1 
ATOM   1764 N  N   . GLU A 1 229 ? -23.615 35.605 36.647  1.00 37.48 ? 229 GLU A N   1 
ATOM   1765 C  CA  . GLU A 1 229 ? -23.902 35.888 38.043  1.00 37.00 ? 229 GLU A CA  1 
ATOM   1766 C  C   . GLU A 1 229 ? -22.686 35.586 38.904  1.00 36.65 ? 229 GLU A C   1 
ATOM   1767 O  O   . GLU A 1 229 ? -21.769 34.866 38.488  1.00 36.37 ? 229 GLU A O   1 
ATOM   1768 C  CB  . GLU A 1 229 ? -25.055 35.017 38.533  1.00 36.92 ? 229 GLU A CB  1 
ATOM   1769 C  CG  . GLU A 1 229 ? -26.440 35.411 38.052  1.00 37.40 ? 229 GLU A CG  1 
ATOM   1770 C  CD  . GLU A 1 229 ? -27.534 34.537 38.667  1.00 37.56 ? 229 GLU A CD  1 
ATOM   1771 O  OE1 . GLU A 1 229 ? -28.360 35.072 39.436  1.00 38.45 ? 229 GLU A OE1 1 
ATOM   1772 O  OE2 . GLU A 1 229 ? -27.565 33.316 38.396  1.00 37.70 ? 229 GLU A OE2 1 
ATOM   1773 N  N   . LEU A 1 230 ? -22.696 36.136 40.116  1.00 36.27 ? 230 LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 230 ? -21.726 35.780 41.142  1.00 35.78 ? 230 LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 230 ? -22.398 34.912 42.194  1.00 35.78 ? 230 LEU A C   1 
ATOM   1776 O  O   . LEU A 1 230 ? -23.622 34.941 42.342  1.00 35.90 ? 230 LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 230 ? -21.161 37.031 41.796  1.00 35.60 ? 230 LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 230 ? -20.635 38.131 40.876  1.00 35.20 ? 230 LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 230 ? -20.585 39.443 41.620  1.00 34.88 ? 230 LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 230 ? -19.267 37.782 40.346  1.00 35.27 ? 230 LEU A CD2 1 
ATOM   1781 N  N   . LEU A 1 231 ? -21.598 34.123 42.904  1.00 35.75 ? 231 LEU A N   1 
ATOM   1782 C  CA  . LEU A 1 231 ? -22.077 33.346 44.041  1.00 35.65 ? 231 LEU A CA  1 
ATOM   1783 C  C   . LEU A 1 231 ? -21.690 34.078 45.314  1.00 35.98 ? 231 LEU A C   1 
ATOM   1784 O  O   . LEU A 1 231 ? -20.513 34.342 45.552  1.00 36.09 ? 231 LEU A O   1 
ATOM   1785 C  CB  . LEU A 1 231 ? -21.468 31.940 44.053  1.00 35.44 ? 231 LEU A CB  1 
ATOM   1786 C  CG  . LEU A 1 231 ? -21.760 30.964 42.911  1.00 34.70 ? 231 LEU A CG  1 
ATOM   1787 C  CD1 . LEU A 1 231 ? -21.152 29.605 43.216  1.00 33.09 ? 231 LEU A CD1 1 
ATOM   1788 C  CD2 . LEU A 1 231 ? -23.251 30.846 42.663  1.00 33.91 ? 231 LEU A CD2 1 
ATOM   1789 N  N   . CYS A 1 232 ? -22.679 34.422 46.126  1.00 36.30 ? 232 CYS A N   1 
ATOM   1790 C  CA  . CYS A 1 232 ? -22.406 35.048 47.411  1.00 36.85 ? 232 CYS A CA  1 
ATOM   1791 C  C   . CYS A 1 232 ? -22.213 33.949 48.453  1.00 36.79 ? 232 CYS A C   1 
ATOM   1792 O  O   . CYS A 1 232 ? -22.797 32.868 48.325  1.00 36.86 ? 232 CYS A O   1 
ATOM   1793 C  CB  . CYS A 1 232 ? -23.538 36.002 47.802  1.00 36.85 ? 232 CYS A CB  1 
ATOM   1794 S  SG  . CYS A 1 232 ? -24.151 37.073 46.435  1.00 38.60 ? 232 CYS A SG  1 
ATOM   1795 N  N   . PRO A 1 233 ? -21.393 34.214 49.487  1.00 36.79 ? 233 PRO A N   1 
ATOM   1796 C  CA  . PRO A 1 233 ? -21.080 33.142 50.427  1.00 36.82 ? 233 PRO A CA  1 
ATOM   1797 C  C   . PRO A 1 233 ? -22.214 32.874 51.416  1.00 36.92 ? 233 PRO A C   1 
ATOM   1798 O  O   . PRO A 1 233 ? -22.131 31.943 52.221  1.00 37.13 ? 233 PRO A O   1 
ATOM   1799 C  CB  . PRO A 1 233 ? -19.823 33.645 51.144  1.00 36.71 ? 233 PRO A CB  1 
ATOM   1800 C  CG  . PRO A 1 233 ? -19.517 34.997 50.551  1.00 36.73 ? 233 PRO A CG  1 
ATOM   1801 C  CD  . PRO A 1 233 ? -20.732 35.473 49.859  1.00 36.64 ? 233 PRO A CD  1 
ATOM   1802 N  N   . ASP A 1 234 ? -23.272 33.676 51.342  1.00 36.96 ? 234 ASP A N   1 
ATOM   1803 C  CA  . ASP A 1 234 ? -24.493 33.410 52.102  1.00 36.95 ? 234 ASP A CA  1 
ATOM   1804 C  C   . ASP A 1 234 ? -25.399 32.438 51.339  1.00 36.63 ? 234 ASP A C   1 
ATOM   1805 O  O   . ASP A 1 234 ? -26.549 32.211 51.727  1.00 36.50 ? 234 ASP A O   1 
ATOM   1806 C  CB  . ASP A 1 234 ? -25.230 34.717 52.442  1.00 36.96 ? 234 ASP A CB  1 
ATOM   1807 C  CG  . ASP A 1 234 ? -25.761 35.441 51.211  1.00 37.42 ? 234 ASP A CG  1 
ATOM   1808 O  OD1 . ASP A 1 234 ? -25.614 34.933 50.077  1.00 38.73 ? 234 ASP A OD1 1 
ATOM   1809 O  OD2 . ASP A 1 234 ? -26.332 36.535 51.383  1.00 37.61 ? 234 ASP A OD2 1 
ATOM   1810 N  N   . ASN A 1 235 ? -24.849 31.872 50.263  1.00 36.44 ? 235 ASN A N   1 
ATOM   1811 C  CA  . ASN A 1 235 ? -25.551 30.953 49.354  1.00 36.36 ? 235 ASN A CA  1 
ATOM   1812 C  C   . ASN A 1 235 ? -26.701 31.621 48.580  1.00 36.20 ? 235 ASN A C   1 
ATOM   1813 O  O   . ASN A 1 235 ? -27.788 31.050 48.428  1.00 36.15 ? 235 ASN A O   1 
ATOM   1814 C  CB  . ASN A 1 235 ? -25.988 29.658 50.072  1.00 36.42 ? 235 ASN A CB  1 
ATOM   1815 C  CG  . ASN A 1 235 ? -24.821 28.937 50.761  1.00 36.67 ? 235 ASN A CG  1 
ATOM   1816 O  OD1 . ASN A 1 235 ? -23.658 29.104 50.386  1.00 37.47 ? 235 ASN A OD1 1 
ATOM   1817 N  ND2 . ASN A 1 235 ? -25.134 28.138 51.772  1.00 36.46 ? 235 ASN A ND2 1 
ATOM   1818 N  N   . THR A 1 236 ? -26.434 32.834 48.093  1.00 36.01 ? 236 THR A N   1 
ATOM   1819 C  CA  . THR A 1 236 ? -27.342 33.569 47.206  1.00 35.76 ? 236 THR A CA  1 
ATOM   1820 C  C   . THR A 1 236 ? -26.618 33.881 45.892  1.00 35.22 ? 236 THR A C   1 
ATOM   1821 O  O   . THR A 1 236 ? -25.385 33.888 45.841  1.00 35.17 ? 236 THR A O   1 
ATOM   1822 C  CB  . THR A 1 236 ? -27.828 34.895 47.862  1.00 36.00 ? 236 THR A CB  1 
ATOM   1823 O  OG1 . THR A 1 236 ? -28.229 34.643 49.214  1.00 36.49 ? 236 THR A OG1 1 
ATOM   1824 C  CG2 . THR A 1 236 ? -29.012 35.522 47.093  1.00 36.31 ? 236 THR A CG2 1 
ATOM   1825 N  N   . ARG A 1 237 ? -27.390 34.109 44.832  1.00 34.57 ? 237 ARG A N   1 
ATOM   1826 C  CA  . ARG A 1 237 ? -26.853 34.578 43.561  1.00 34.01 ? 237 ARG A CA  1 
ATOM   1827 C  C   . ARG A 1 237 ? -27.194 36.047 43.380  1.00 33.87 ? 237 ARG A C   1 
ATOM   1828 O  O   . ARG A 1 237 ? -28.303 36.479 43.714  1.00 33.73 ? 237 ARG A O   1 
ATOM   1829 C  CB  . ARG A 1 237 ? -27.426 33.775 42.390  1.00 34.03 ? 237 ARG A CB  1 
ATOM   1830 C  CG  . ARG A 1 237 ? -26.945 32.337 42.294  1.00 33.32 ? 237 ARG A CG  1 
ATOM   1831 C  CD  . ARG A 1 237 ? -27.346 31.711 40.969  1.00 32.45 ? 237 ARG A CD  1 
ATOM   1832 N  NE  . ARG A 1 237 ? -26.759 30.385 40.804  1.00 31.83 ? 237 ARG A NE  1 
ATOM   1833 C  CZ  . ARG A 1 237 ? -26.381 29.861 39.642  1.00 31.64 ? 237 ARG A CZ  1 
ATOM   1834 N  NH1 . ARG A 1 237 ? -26.515 30.540 38.509  1.00 31.45 ? 237 ARG A NH1 1 
ATOM   1835 N  NH2 . ARG A 1 237 ? -25.854 28.649 39.617  1.00 32.15 ? 237 ARG A NH2 1 
ATOM   1836 N  N   . LYS A 1 238 ? -26.237 36.805 42.851  1.00 33.59 ? 238 LYS A N   1 
ATOM   1837 C  CA  . LYS A 1 238 ? -26.416 38.230 42.589  1.00 33.61 ? 238 LYS A CA  1 
ATOM   1838 C  C   . LYS A 1 238 ? -25.789 38.624 41.254  1.00 33.43 ? 238 LYS A C   1 
ATOM   1839 O  O   . LYS A 1 238 ? -24.865 37.956 40.787  1.00 33.56 ? 238 LYS A O   1 
ATOM   1840 C  CB  . LYS A 1 238 ? -25.807 39.059 43.723  1.00 33.53 ? 238 LYS A CB  1 
ATOM   1841 C  CG  . LYS A 1 238 ? -26.723 39.233 44.920  1.00 33.83 ? 238 LYS A CG  1 
ATOM   1842 C  CD  . LYS A 1 238 ? -26.075 40.078 46.008  1.00 34.16 ? 238 LYS A CD  1 
ATOM   1843 C  CE  . LYS A 1 238 ? -26.795 39.925 47.352  1.00 34.67 ? 238 LYS A CE  1 
ATOM   1844 N  NZ  . LYS A 1 238 ? -26.583 38.575 47.954  1.00 35.23 ? 238 LYS A NZ  1 
ATOM   1845 N  N   . PRO A 1 239 ? -26.278 39.717 40.633  1.00 33.37 ? 239 PRO A N   1 
ATOM   1846 C  CA  . PRO A 1 239 ? -25.687 40.166 39.364  1.00 33.30 ? 239 PRO A CA  1 
ATOM   1847 C  C   . PRO A 1 239 ? -24.229 40.564 39.552  1.00 33.09 ? 239 PRO A C   1 
ATOM   1848 O  O   . PRO A 1 239 ? -23.848 40.960 40.653  1.00 33.09 ? 239 PRO A O   1 
ATOM   1849 C  CB  . PRO A 1 239 ? -26.524 41.398 38.991  1.00 33.39 ? 239 PRO A CB  1 
ATOM   1850 C  CG  . PRO A 1 239 ? -27.776 41.294 39.808  1.00 33.49 ? 239 PRO A CG  1 
ATOM   1851 C  CD  . PRO A 1 239 ? -27.386 40.589 41.066  1.00 33.42 ? 239 PRO A CD  1 
ATOM   1852 N  N   . VAL A 1 240 ? -23.431 40.468 38.488  1.00 33.02 ? 240 VAL A N   1 
ATOM   1853 C  CA  . VAL A 1 240 ? -21.969 40.669 38.583  1.00 32.74 ? 240 VAL A CA  1 
ATOM   1854 C  C   . VAL A 1 240 ? -21.518 42.042 39.077  1.00 32.76 ? 240 VAL A C   1 
ATOM   1855 O  O   . VAL A 1 240 ? -20.433 42.162 39.647  1.00 32.88 ? 240 VAL A O   1 
ATOM   1856 C  CB  . VAL A 1 240 ? -21.204 40.327 37.269  1.00 32.56 ? 240 VAL A CB  1 
ATOM   1857 C  CG1 . VAL A 1 240 ? -21.309 38.846 36.967  1.00 32.50 ? 240 VAL A CG1 1 
ATOM   1858 C  CG2 . VAL A 1 240 ? -21.683 41.183 36.097  1.00 31.99 ? 240 VAL A CG2 1 
ATOM   1859 N  N   . ASP A 1 241 ? -22.335 43.069 38.861  1.00 32.73 ? 241 ASP A N   1 
ATOM   1860 C  CA  . ASP A 1 241 ? -21.939 44.411 39.265  1.00 32.80 ? 241 ASP A CA  1 
ATOM   1861 C  C   . ASP A 1 241 ? -22.191 44.643 40.752  1.00 32.67 ? 241 ASP A C   1 
ATOM   1862 O  O   . ASP A 1 241 ? -21.822 45.680 41.296  1.00 32.72 ? 241 ASP A O   1 
ATOM   1863 C  CB  . ASP A 1 241 ? -22.534 45.508 38.352  1.00 32.82 ? 241 ASP A CB  1 
ATOM   1864 C  CG  . ASP A 1 241 ? -24.008 45.799 38.620  1.00 33.54 ? 241 ASP A CG  1 
ATOM   1865 O  OD1 . ASP A 1 241 ? -24.706 44.976 39.250  1.00 35.11 ? 241 ASP A OD1 1 
ATOM   1866 O  OD2 . ASP A 1 241 ? -24.478 46.870 38.174  1.00 33.96 ? 241 ASP A OD2 1 
ATOM   1867 N  N   . LYS A 1 242 ? -22.787 43.651 41.408  1.00 32.40 ? 242 LYS A N   1 
ATOM   1868 C  CA  . LYS A 1 242 ? -23.002 43.717 42.846  1.00 32.41 ? 242 LYS A CA  1 
ATOM   1869 C  C   . LYS A 1 242 ? -21.920 42.944 43.612  1.00 32.25 ? 242 LYS A C   1 
ATOM   1870 O  O   . LYS A 1 242 ? -22.209 42.291 44.616  1.00 32.24 ? 242 LYS A O   1 
ATOM   1871 C  CB  . LYS A 1 242 ? -24.410 43.227 43.213  1.00 32.36 ? 242 LYS A CB  1 
ATOM   1872 C  CG  . LYS A 1 242 ? -25.543 43.995 42.539  1.00 33.29 ? 242 LYS A CG  1 
ATOM   1873 C  CD  . LYS A 1 242 ? -25.711 45.402 43.097  1.00 35.27 ? 242 LYS A CD  1 
ATOM   1874 C  CE  . LYS A 1 242 ? -26.722 45.428 44.239  1.00 36.97 ? 242 LYS A CE  1 
ATOM   1875 N  NZ  . LYS A 1 242 ? -26.662 46.713 45.007  1.00 38.10 ? 242 LYS A NZ  1 
ATOM   1876 N  N   . PHE A 1 243 ? -20.675 43.043 43.146  1.00 32.01 ? 243 PHE A N   1 
ATOM   1877 C  CA  . PHE A 1 243 ? -19.553 42.313 43.748  1.00 31.84 ? 243 PHE A CA  1 
ATOM   1878 C  C   . PHE A 1 243 ? -19.154 42.710 45.183  1.00 32.05 ? 243 PHE A C   1 
ATOM   1879 O  O   . PHE A 1 243 ? -18.656 41.863 45.932  1.00 32.21 ? 243 PHE A O   1 
ATOM   1880 C  CB  . PHE A 1 243 ? -18.331 42.296 42.822  1.00 31.54 ? 243 PHE A CB  1 
ATOM   1881 C  CG  . PHE A 1 243 ? -17.844 43.650 42.420  1.00 31.21 ? 243 PHE A CG  1 
ATOM   1882 C  CD1 . PHE A 1 243 ? -16.929 44.334 43.203  1.00 30.92 ? 243 PHE A CD1 1 
ATOM   1883 C  CD2 . PHE A 1 243 ? -18.292 44.241 41.242  1.00 31.23 ? 243 PHE A CD2 1 
ATOM   1884 C  CE1 . PHE A 1 243 ? -16.474 45.592 42.822  1.00 31.14 ? 243 PHE A CE1 1 
ATOM   1885 C  CE2 . PHE A 1 243 ? -17.843 45.498 40.857  1.00 30.64 ? 243 PHE A CE2 1 
ATOM   1886 C  CZ  . PHE A 1 243 ? -16.932 46.172 41.647  1.00 30.90 ? 243 PHE A CZ  1 
ATOM   1887 N  N   . LYS A 1 244 ? -19.372 43.968 45.571  1.00 31.98 ? 244 LYS A N   1 
ATOM   1888 C  CA  . LYS A 1 244 ? -19.098 44.392 46.949  1.00 32.28 ? 244 LYS A CA  1 
ATOM   1889 C  C   . LYS A 1 244 ? -19.942 43.602 47.951  1.00 32.35 ? 244 LYS A C   1 
ATOM   1890 O  O   . LYS A 1 244 ? -19.446 43.206 49.003  1.00 32.52 ? 244 LYS A O   1 
ATOM   1891 C  CB  . LYS A 1 244 ? -19.309 45.895 47.141  1.00 32.11 ? 244 LYS A CB  1 
ATOM   1892 C  CG  . LYS A 1 244 ? -18.433 46.779 46.254  1.00 32.85 ? 244 LYS A CG  1 
ATOM   1893 C  CD  . LYS A 1 244 ? -18.746 48.263 46.451  1.00 33.09 ? 244 LYS A CD  1 
ATOM   1894 C  CE  . LYS A 1 244 ? -18.381 49.113 45.218  1.00 34.98 ? 244 LYS A CE  1 
ATOM   1895 N  NZ  . LYS A 1 244 ? -19.540 49.412 44.313  1.00 34.45 ? 244 LYS A NZ  1 
ATOM   1896 N  N   . ASP A 1 245 ? -21.207 43.357 47.613  1.00 32.58 ? 245 ASP A N   1 
ATOM   1897 C  CA  . ASP A 1 245 ? -22.102 42.551 48.460  1.00 32.66 ? 245 ASP A CA  1 
ATOM   1898 C  C   . ASP A 1 245 ? -22.017 41.049 48.145  1.00 32.32 ? 245 ASP A C   1 
ATOM   1899 O  O   . ASP A 1 245 ? -22.729 40.240 48.747  1.00 32.26 ? 245 ASP A O   1 
ATOM   1900 C  CB  . ASP A 1 245 ? -23.558 43.026 48.327  1.00 33.04 ? 245 ASP A CB  1 
ATOM   1901 C  CG  . ASP A 1 245 ? -23.706 44.545 48.446  1.00 34.46 ? 245 ASP A CG  1 
ATOM   1902 O  OD1 . ASP A 1 245 ? -23.034 45.156 49.307  1.00 35.47 ? 245 ASP A OD1 1 
ATOM   1903 O  OD2 . ASP A 1 245 ? -24.513 45.130 47.681  1.00 35.96 ? 245 ASP A OD2 1 
ATOM   1904 N  N   . CYS A 1 246 ? -21.137 40.680 47.212  1.00 32.05 ? 246 CYS A N   1 
ATOM   1905 C  CA  . CYS A 1 246 ? -21.084 39.309 46.701  1.00 31.17 ? 246 CYS A CA  1 
ATOM   1906 C  C   . CYS A 1 246 ? -19.689 38.877 46.223  1.00 30.24 ? 246 CYS A C   1 
ATOM   1907 O  O   . CYS A 1 246 ? -19.474 38.609 45.035  1.00 30.23 ? 246 CYS A O   1 
ATOM   1908 C  CB  . CYS A 1 246 ? -22.113 39.139 45.582  1.00 31.59 ? 246 CYS A CB  1 
ATOM   1909 S  SG  . CYS A 1 246 ? -22.531 37.443 45.232  1.00 32.86 ? 246 CYS A SG  1 
ATOM   1910 N  N   . HIS A 1 247 ? -18.745 38.805 47.156  1.00 28.95 ? 247 HIS A N   1 
ATOM   1911 C  CA  . HIS A 1 247 ? -17.402 38.315 46.856  1.00 27.67 ? 247 HIS A CA  1 
ATOM   1912 C  C   . HIS A 1 247 ? -17.017 37.238 47.851  1.00 27.26 ? 247 HIS A C   1 
ATOM   1913 O  O   . HIS A 1 247 ? -17.752 36.968 48.793  1.00 27.54 ? 247 HIS A O   1 
ATOM   1914 C  CB  . HIS A 1 247 ? -16.392 39.451 46.905  1.00 27.19 ? 247 HIS A CB  1 
ATOM   1915 C  CG  . HIS A 1 247 ? -16.360 40.161 48.219  1.00 26.12 ? 247 HIS A CG  1 
ATOM   1916 N  ND1 . HIS A 1 247 ? -17.012 41.355 48.434  1.00 24.98 ? 247 HIS A ND1 1 
ATOM   1917 C  CD2 . HIS A 1 247 ? -15.759 39.845 49.389  1.00 24.90 ? 247 HIS A CD2 1 
ATOM   1918 C  CE1 . HIS A 1 247 ? -16.807 41.748 49.677  1.00 24.21 ? 247 HIS A CE1 1 
ATOM   1919 N  NE2 . HIS A 1 247 ? -16.053 40.848 50.279  1.00 24.34 ? 247 HIS A NE2 1 
ATOM   1920 N  N   . LEU A 1 248 ? -15.857 36.631 47.644  1.00 26.51 ? 248 LEU A N   1 
ATOM   1921 C  CA  . LEU A 1 248 ? -15.386 35.561 48.505  1.00 25.71 ? 248 LEU A CA  1 
ATOM   1922 C  C   . LEU A 1 248 ? -14.237 36.018 49.398  1.00 25.65 ? 248 LEU A C   1 
ATOM   1923 O  O   . LEU A 1 248 ? -14.003 35.456 50.466  1.00 25.63 ? 248 LEU A O   1 
ATOM   1924 C  CB  . LEU A 1 248 ? -14.973 34.356 47.656  1.00 25.57 ? 248 LEU A CB  1 
ATOM   1925 C  CG  . LEU A 1 248 ? -15.970 33.205 47.439  1.00 24.26 ? 248 LEU A CG  1 
ATOM   1926 C  CD1 . LEU A 1 248 ? -17.419 33.641 47.542  1.00 22.66 ? 248 LEU A CD1 1 
ATOM   1927 C  CD2 . LEU A 1 248 ? -15.702 32.525 46.109  1.00 23.36 ? 248 LEU A CD2 1 
ATOM   1928 N  N   . ALA A 1 249 ? -13.523 37.044 48.951  1.00 25.57 ? 249 ALA A N   1 
ATOM   1929 C  CA  . ALA A 1 249 ? -12.475 37.660 49.744  1.00 25.26 ? 249 ALA A CA  1 
ATOM   1930 C  C   . ALA A 1 249 ? -12.135 39.036 49.187  1.00 25.15 ? 249 ALA A C   1 
ATOM   1931 O  O   . ALA A 1 249 ? -12.287 39.278 47.987  1.00 25.47 ? 249 ALA A O   1 
ATOM   1932 C  CB  . ALA A 1 249 ? -11.245 36.780 49.755  1.00 25.10 ? 249 ALA A CB  1 
ATOM   1933 N  N   . ARG A 1 250 ? -11.708 39.938 50.070  1.00 24.77 ? 250 ARG A N   1 
ATOM   1934 C  CA  . ARG A 1 250 ? -11.024 41.156 49.667  1.00 24.37 ? 250 ARG A CA  1 
ATOM   1935 C  C   . ARG A 1 250 ? -9.572  40.941 49.999  1.00 24.29 ? 250 ARG A C   1 
ATOM   1936 O  O   . ARG A 1 250 ? -9.248  40.575 51.123  1.00 24.69 ? 250 ARG A O   1 
ATOM   1937 C  CB  . ARG A 1 250 ? -11.534 42.390 50.421  1.00 24.33 ? 250 ARG A CB  1 
ATOM   1938 C  CG  . ARG A 1 250 ? -10.576 43.581 50.274  1.00 24.32 ? 250 ARG A CG  1 
ATOM   1939 C  CD  . ARG A 1 250 ? -11.206 44.916 50.540  1.00 23.80 ? 250 ARG A CD  1 
ATOM   1940 N  NE  . ARG A 1 250 ? -11.411 45.115 51.966  1.00 23.55 ? 250 ARG A NE  1 
ATOM   1941 C  CZ  . ARG A 1 250 ? -12.246 46.010 52.480  1.00 23.52 ? 250 ARG A CZ  1 
ATOM   1942 N  NH1 . ARG A 1 250 ? -12.957 46.808 51.686  1.00 22.94 ? 250 ARG A NH1 1 
ATOM   1943 N  NH2 . ARG A 1 250 ? -12.379 46.098 53.793  1.00 23.46 ? 250 ARG A NH2 1 
ATOM   1944 N  N   . VAL A 1 251 ? -8.699  41.178 49.029  1.00 24.13 ? 251 VAL A N   1 
ATOM   1945 C  CA  . VAL A 1 251 ? -7.273  40.911 49.184  1.00 23.98 ? 251 VAL A CA  1 
ATOM   1946 C  C   . VAL A 1 251 ? -6.463  42.060 48.599  1.00 23.89 ? 251 VAL A C   1 
ATOM   1947 O  O   . VAL A 1 251 ? -6.942  42.726 47.686  1.00 24.25 ? 251 VAL A O   1 
ATOM   1948 C  CB  . VAL A 1 251 ? -6.886  39.616 48.459  1.00 24.16 ? 251 VAL A CB  1 
ATOM   1949 C  CG1 . VAL A 1 251 ? -7.470  38.392 49.195  1.00 24.59 ? 251 VAL A CG1 1 
ATOM   1950 C  CG2 . VAL A 1 251 ? -7.334  39.661 46.989  1.00 23.72 ? 251 VAL A CG2 1 
ATOM   1951 N  N   . PRO A 1 252 ? -5.228  42.291 49.103  1.00 23.57 ? 252 PRO A N   1 
ATOM   1952 C  CA  . PRO A 1 252 ? -4.443  43.401 48.571  1.00 22.77 ? 252 PRO A CA  1 
ATOM   1953 C  C   . PRO A 1 252 ? -3.940  43.059 47.189  1.00 22.05 ? 252 PRO A C   1 
ATOM   1954 O  O   . PRO A 1 252 ? -3.804  41.894 46.853  1.00 21.78 ? 252 PRO A O   1 
ATOM   1955 C  CB  . PRO A 1 252 ? -3.270  43.508 49.542  1.00 22.76 ? 252 PRO A CB  1 
ATOM   1956 C  CG  . PRO A 1 252 ? -3.109  42.145 50.091  1.00 23.41 ? 252 PRO A CG  1 
ATOM   1957 C  CD  . PRO A 1 252 ? -4.488  41.549 50.145  1.00 23.77 ? 252 PRO A CD  1 
ATOM   1958 N  N   . SER A 1 253 ? -3.670  44.083 46.397  1.00 21.62 ? 253 SER A N   1 
ATOM   1959 C  CA  . SER A 1 253 ? -3.273  43.897 45.019  1.00 21.17 ? 253 SER A CA  1 
ATOM   1960 C  C   . SER A 1 253 ? -1.916  43.215 44.874  1.00 20.79 ? 253 SER A C   1 
ATOM   1961 O  O   . SER A 1 253 ? -1.135  43.126 45.810  1.00 20.33 ? 253 SER A O   1 
ATOM   1962 C  CB  . SER A 1 253 ? -3.275  45.243 44.290  1.00 21.19 ? 253 SER A CB  1 
ATOM   1963 O  OG  . SER A 1 253 ? -2.421  46.181 44.922  1.00 21.83 ? 253 SER A OG  1 
ATOM   1964 N  N   . HIS A 1 254 ? -1.667  42.723 43.671  1.00 20.90 ? 254 HIS A N   1 
ATOM   1965 C  CA  . HIS A 1 254 ? -0.349  42.272 43.248  1.00 20.81 ? 254 HIS A CA  1 
ATOM   1966 C  C   . HIS A 1 254 ? 0.721   43.320 43.572  1.00 20.92 ? 254 HIS A C   1 
ATOM   1967 O  O   . HIS A 1 254 ? 0.433   44.526 43.639  1.00 21.02 ? 254 HIS A O   1 
ATOM   1968 C  CB  . HIS A 1 254 ? -0.388  41.987 41.751  1.00 20.46 ? 254 HIS A CB  1 
ATOM   1969 C  CG  . HIS A 1 254 ? -1.316  40.872 41.376  1.00 20.78 ? 254 HIS A CG  1 
ATOM   1970 N  ND1 . HIS A 1 254 ? -1.327  40.302 40.121  1.00 20.90 ? 254 HIS A ND1 1 
ATOM   1971 C  CD2 . HIS A 1 254 ? -2.251  40.207 42.098  1.00 20.85 ? 254 HIS A CD2 1 
ATOM   1972 C  CE1 . HIS A 1 254 ? -2.229  39.337 40.085  1.00 21.51 ? 254 HIS A CE1 1 
ATOM   1973 N  NE2 . HIS A 1 254 ? -2.804  39.259 41.272  1.00 21.19 ? 254 HIS A NE2 1 
ATOM   1974 N  N   . ALA A 1 255 ? 1.950   42.863 43.788  1.00 20.64 ? 255 ALA A N   1 
ATOM   1975 C  CA  . ALA A 1 255 ? 3.037   43.772 44.118  1.00 20.49 ? 255 ALA A CA  1 
ATOM   1976 C  C   . ALA A 1 255 ? 4.364   43.327 43.516  1.00 20.71 ? 255 ALA A C   1 
ATOM   1977 O  O   . ALA A 1 255 ? 4.617   42.130 43.337  1.00 20.87 ? 255 ALA A O   1 
ATOM   1978 C  CB  . ALA A 1 255 ? 3.161   43.907 45.613  1.00 20.37 ? 255 ALA A CB  1 
ATOM   1979 N  N   . VAL A 1 256 ? 5.206   44.302 43.190  1.00 20.45 ? 256 VAL A N   1 
ATOM   1980 C  CA  . VAL A 1 256 ? 6.588   44.019 42.852  1.00 20.46 ? 256 VAL A CA  1 
ATOM   1981 C  C   . VAL A 1 256 ? 7.296   43.537 44.128  1.00 20.66 ? 256 VAL A C   1 
ATOM   1982 O  O   . VAL A 1 256 ? 7.137   44.141 45.200  1.00 21.05 ? 256 VAL A O   1 
ATOM   1983 C  CB  . VAL A 1 256 ? 7.300   45.280 42.309  1.00 20.38 ? 256 VAL A CB  1 
ATOM   1984 C  CG1 . VAL A 1 256 ? 8.736   44.964 41.905  1.00 20.30 ? 256 VAL A CG1 1 
ATOM   1985 C  CG2 . VAL A 1 256 ? 6.537   45.872 41.134  1.00 20.45 ? 256 VAL A CG2 1 
ATOM   1986 N  N   . VAL A 1 257 ? 8.065   42.454 44.030  1.00 20.28 ? 257 VAL A N   1 
ATOM   1987 C  CA  . VAL A 1 257 ? 8.914   42.058 45.155  1.00 19.75 ? 257 VAL A CA  1 
ATOM   1988 C  C   . VAL A 1 257 ? 10.387  42.217 44.861  1.00 19.69 ? 257 VAL A C   1 
ATOM   1989 O  O   . VAL A 1 257 ? 10.798  42.230 43.705  1.00 19.75 ? 257 VAL A O   1 
ATOM   1990 C  CB  . VAL A 1 257 ? 8.672   40.627 45.613  1.00 19.60 ? 257 VAL A CB  1 
ATOM   1991 C  CG1 . VAL A 1 257 ? 7.287   40.504 46.223  1.00 19.56 ? 257 VAL A CG1 1 
ATOM   1992 C  CG2 . VAL A 1 257 ? 8.902   39.661 44.468  1.00 19.18 ? 257 VAL A CG2 1 
ATOM   1993 N  N   . ALA A 1 258 ? 11.161  42.343 45.937  1.00 19.82 ? 258 ALA A N   1 
ATOM   1994 C  CA  . ALA A 1 258 ? 12.612  42.506 45.898  1.00 19.96 ? 258 ALA A CA  1 
ATOM   1995 C  C   . ALA A 1 258 ? 13.206  41.892 47.159  1.00 19.95 ? 258 ALA A C   1 
ATOM   1996 O  O   . ALA A 1 258 ? 12.474  41.560 48.080  1.00 19.53 ? 258 ALA A O   1 
ATOM   1997 C  CB  . ALA A 1 258 ? 12.981  43.982 45.798  1.00 19.63 ? 258 ALA A CB  1 
ATOM   1998 N  N   . ARG A 1 259 ? 14.528  41.743 47.185  1.00 20.54 ? 259 ARG A N   1 
ATOM   1999 C  CA  . ARG A 1 259 ? 15.233  41.196 48.340  1.00 21.25 ? 259 ARG A CA  1 
ATOM   2000 C  C   . ARG A 1 259 ? 14.992  42.041 49.586  1.00 22.25 ? 259 ARG A C   1 
ATOM   2001 O  O   . ARG A 1 259 ? 14.889  43.269 49.497  1.00 22.48 ? 259 ARG A O   1 
ATOM   2002 C  CB  . ARG A 1 259 ? 16.741  41.098 48.068  1.00 21.11 ? 259 ARG A CB  1 
ATOM   2003 C  CG  . ARG A 1 259 ? 17.153  39.935 47.173  1.00 20.88 ? 259 ARG A CG  1 
ATOM   2004 C  CD  . ARG A 1 259 ? 18.671  39.870 46.925  1.00 20.43 ? 259 ARG A CD  1 
ATOM   2005 N  NE  . ARG A 1 259 ? 19.190  41.083 46.300  1.00 19.19 ? 259 ARG A NE  1 
ATOM   2006 C  CZ  . ARG A 1 259 ? 18.983  41.434 45.032  1.00 19.41 ? 259 ARG A CZ  1 
ATOM   2007 N  NH1 . ARG A 1 259 ? 18.255  40.674 44.227  1.00 20.24 ? 259 ARG A NH1 1 
ATOM   2008 N  NH2 . ARG A 1 259 ? 19.490  42.563 44.567  1.00 19.33 ? 259 ARG A NH2 1 
ATOM   2009 N  N   . SER A 1 260 ? 14.897  41.374 50.737  1.00 23.31 ? 260 SER A N   1 
ATOM   2010 C  CA  . SER A 1 260 ? 14.811  42.050 52.034  1.00 24.51 ? 260 SER A CA  1 
ATOM   2011 C  C   . SER A 1 260 ? 16.078  42.820 52.375  1.00 25.06 ? 260 SER A C   1 
ATOM   2012 O  O   . SER A 1 260 ? 16.007  43.839 53.051  1.00 25.54 ? 260 SER A O   1 
ATOM   2013 C  CB  . SER A 1 260 ? 14.500  41.061 53.159  1.00 24.48 ? 260 SER A CB  1 
ATOM   2014 O  OG  . SER A 1 260 ? 13.128  40.694 53.147  1.00 25.82 ? 260 SER A OG  1 
ATOM   2015 N  N   . VAL A 1 261 ? 17.230  42.322 51.927  1.00 25.75 ? 261 VAL A N   1 
ATOM   2016 C  CA  . VAL A 1 261 ? 18.524  42.983 52.154  1.00 26.35 ? 261 VAL A CA  1 
ATOM   2017 C  C   . VAL A 1 261 ? 19.239  43.147 50.806  1.00 26.94 ? 261 VAL A C   1 
ATOM   2018 O  O   . VAL A 1 261 ? 19.316  42.188 50.026  1.00 27.34 ? 261 VAL A O   1 
ATOM   2019 C  CB  . VAL A 1 261 ? 19.414  42.185 53.147  1.00 26.19 ? 261 VAL A CB  1 
ATOM   2020 C  CG1 . VAL A 1 261 ? 20.689  42.948 53.471  1.00 26.24 ? 261 VAL A CG1 1 
ATOM   2021 C  CG2 . VAL A 1 261 ? 18.654  41.870 54.437  1.00 26.26 ? 261 VAL A CG2 1 
ATOM   2022 N  N   . ASN A 1 262 ? 19.752  44.352 50.535  1.00 27.28 ? 262 ASN A N   1 
ATOM   2023 C  CA  . ASN A 1 262 ? 20.334  44.699 49.221  1.00 27.64 ? 262 ASN A CA  1 
ATOM   2024 C  C   . ASN A 1 262 ? 19.369  44.426 48.073  1.00 27.43 ? 262 ASN A C   1 
ATOM   2025 O  O   . ASN A 1 262 ? 19.721  43.791 47.076  1.00 27.32 ? 262 ASN A O   1 
ATOM   2026 C  CB  . ASN A 1 262 ? 21.669  43.987 48.993  1.00 27.89 ? 262 ASN A CB  1 
ATOM   2027 C  CG  . ASN A 1 262 ? 22.621  44.181 50.144  1.00 29.47 ? 262 ASN A CG  1 
ATOM   2028 O  OD1 . ASN A 1 262 ? 23.082  45.298 50.395  1.00 31.68 ? 262 ASN A OD1 1 
ATOM   2029 N  ND2 . ASN A 1 262 ? 22.916  43.098 50.869  1.00 30.34 ? 262 ASN A ND2 1 
ATOM   2030 N  N   . GLY A 1 263 ? 18.143  44.908 48.241  1.00 27.32 ? 263 GLY A N   1 
ATOM   2031 C  CA  . GLY A 1 263 ? 17.090  44.704 47.271  1.00 27.29 ? 263 GLY A CA  1 
ATOM   2032 C  C   . GLY A 1 263 ? 17.037  45.749 46.180  1.00 27.40 ? 263 GLY A C   1 
ATOM   2033 O  O   . GLY A 1 263 ? 16.287  45.587 45.223  1.00 27.57 ? 263 GLY A O   1 
ATOM   2034 N  N   . LYS A 1 264 ? 17.834  46.812 46.319  1.00 27.46 ? 264 LYS A N   1 
ATOM   2035 C  CA  . LYS A 1 264 ? 17.819  47.962 45.401  1.00 27.55 ? 264 LYS A CA  1 
ATOM   2036 C  C   . LYS A 1 264 ? 16.496  48.722 45.487  1.00 28.08 ? 264 LYS A C   1 
ATOM   2037 O  O   . LYS A 1 264 ? 16.055  49.311 44.493  1.00 28.29 ? 264 LYS A O   1 
ATOM   2038 C  CB  . LYS A 1 264 ? 18.073  47.530 43.945  1.00 27.27 ? 264 LYS A CB  1 
ATOM   2039 C  CG  . LYS A 1 264 ? 19.438  46.928 43.671  1.00 27.15 ? 264 LYS A CG  1 
ATOM   2040 C  CD  . LYS A 1 264 ? 19.639  46.650 42.181  1.00 27.27 ? 264 LYS A CD  1 
ATOM   2041 C  CE  . LYS A 1 264 ? 21.111  46.439 41.849  1.00 26.72 ? 264 LYS A CE  1 
ATOM   2042 N  NZ  . LYS A 1 264 ? 21.336  45.614 40.629  1.00 25.75 ? 264 LYS A NZ  1 
ATOM   2043 N  N   . GLU A 1 265 ? 15.868  48.703 46.666  1.00 28.39 ? 265 GLU A N   1 
ATOM   2044 C  CA  . GLU A 1 265 ? 14.489  49.190 46.838  1.00 29.16 ? 265 GLU A CA  1 
ATOM   2045 C  C   . GLU A 1 265 ? 14.293  50.604 46.293  1.00 28.17 ? 265 GLU A C   1 
ATOM   2046 O  O   . GLU A 1 265 ? 13.356  50.854 45.541  1.00 28.03 ? 265 GLU A O   1 
ATOM   2047 C  CB  . GLU A 1 265 ? 14.042  49.123 48.306  1.00 29.11 ? 265 GLU A CB  1 
ATOM   2048 C  CG  . GLU A 1 265 ? 14.246  47.760 48.988  1.00 31.51 ? 265 GLU A CG  1 
ATOM   2049 C  CD  . GLU A 1 265 ? 13.690  47.685 50.439  1.00 32.23 ? 265 GLU A CD  1 
ATOM   2050 O  OE1 . GLU A 1 265 ? 13.390  48.749 51.046  1.00 35.64 ? 265 GLU A OE1 1 
ATOM   2051 O  OE2 . GLU A 1 265 ? 13.561  46.546 50.975  1.00 35.58 ? 265 GLU A OE2 1 
ATOM   2052 N  N   . ASP A 1 266 ? 15.189  51.517 46.665  1.00 27.69 ? 266 ASP A N   1 
ATOM   2053 C  CA  . ASP A 1 266 ? 15.135  52.897 46.179  1.00 27.08 ? 266 ASP A CA  1 
ATOM   2054 C  C   . ASP A 1 266 ? 15.156  52.968 44.662  1.00 26.27 ? 266 ASP A C   1 
ATOM   2055 O  O   . ASP A 1 266 ? 14.310  53.620 44.058  1.00 26.31 ? 266 ASP A O   1 
ATOM   2056 C  CB  . ASP A 1 266 ? 16.281  53.729 46.753  1.00 27.31 ? 266 ASP A CB  1 
ATOM   2057 C  CG  . ASP A 1 266 ? 15.904  54.435 48.043  1.00 28.47 ? 266 ASP A CG  1 
ATOM   2058 O  OD1 . ASP A 1 266 ? 15.038  53.913 48.787  1.00 28.66 ? 266 ASP A OD1 1 
ATOM   2059 O  OD2 . ASP A 1 266 ? 16.477  55.519 48.311  1.00 30.09 ? 266 ASP A OD2 1 
ATOM   2060 N  N   . ALA A 1 267 ? 16.118  52.279 44.059  1.00 25.36 ? 267 ALA A N   1 
ATOM   2061 C  CA  . ALA A 1 267 ? 16.243  52.220 42.616  1.00 24.63 ? 267 ALA A CA  1 
ATOM   2062 C  C   . ALA A 1 267 ? 14.993  51.662 41.918  1.00 24.33 ? 267 ALA A C   1 
ATOM   2063 O  O   . ALA A 1 267 ? 14.587  52.176 40.879  1.00 24.61 ? 267 ALA A O   1 
ATOM   2064 C  CB  . ALA A 1 267 ? 17.466  51.430 42.237  1.00 24.62 ? 267 ALA A CB  1 
ATOM   2065 N  N   . ILE A 1 268 ? 14.380  50.623 42.476  1.00 23.54 ? 268 ILE A N   1 
ATOM   2066 C  CA  . ILE A 1 268 ? 13.170  50.083 41.876  1.00 23.06 ? 268 ILE A CA  1 
ATOM   2067 C  C   . ILE A 1 268 ? 12.058  51.117 41.891  1.00 22.91 ? 268 ILE A C   1 
ATOM   2068 O  O   . ILE A 1 268 ? 11.405  51.338 40.878  1.00 22.84 ? 268 ILE A O   1 
ATOM   2069 C  CB  . ILE A 1 268 ? 12.690  48.798 42.576  1.00 23.15 ? 268 ILE A CB  1 
ATOM   2070 C  CG1 . ILE A 1 268 ? 13.628  47.643 42.242  1.00 23.00 ? 268 ILE A CG1 1 
ATOM   2071 C  CG2 . ILE A 1 268 ? 11.258  48.452 42.162  1.00 21.80 ? 268 ILE A CG2 1 
ATOM   2072 C  CD1 . ILE A 1 268 ? 13.663  46.572 43.290  1.00 23.17 ? 268 ILE A CD1 1 
ATOM   2073 N  N   . TRP A 1 269 ? 11.848  51.742 43.046  1.00 22.86 ? 269 TRP A N   1 
ATOM   2074 C  CA  . TRP A 1 269 ? 10.800  52.747 43.187  1.00 22.72 ? 269 TRP A CA  1 
ATOM   2075 C  C   . TRP A 1 269 ? 11.063  53.953 42.297  1.00 22.75 ? 269 TRP A C   1 
ATOM   2076 O  O   . TRP A 1 269 ? 10.148  54.511 41.711  1.00 22.81 ? 269 TRP A O   1 
ATOM   2077 C  CB  . TRP A 1 269 ? 10.613  53.200 44.644  1.00 22.43 ? 269 TRP A CB  1 
ATOM   2078 C  CG  . TRP A 1 269 ? 9.571   54.253 44.725  1.00 21.78 ? 269 TRP A CG  1 
ATOM   2079 C  CD1 . TRP A 1 269 ? 9.765   55.583 44.924  1.00 20.83 ? 269 TRP A CD1 1 
ATOM   2080 C  CD2 . TRP A 1 269 ? 8.164   54.074 44.523  1.00 21.51 ? 269 TRP A CD2 1 
ATOM   2081 N  NE1 . TRP A 1 269 ? 8.564   56.246 44.888  1.00 20.72 ? 269 TRP A NE1 1 
ATOM   2082 C  CE2 . TRP A 1 269 ? 7.563   55.343 44.642  1.00 21.05 ? 269 TRP A CE2 1 
ATOM   2083 C  CE3 . TRP A 1 269 ? 7.351   52.959 44.267  1.00 21.69 ? 269 TRP A CE3 1 
ATOM   2084 C  CZ2 . TRP A 1 269 ? 6.182   55.535 44.515  1.00 21.61 ? 269 TRP A CZ2 1 
ATOM   2085 C  CZ3 . TRP A 1 269 ? 5.972   53.148 44.140  1.00 21.73 ? 269 TRP A CZ3 1 
ATOM   2086 C  CH2 . TRP A 1 269 ? 5.404   54.428 44.266  1.00 21.81 ? 269 TRP A CH2 1 
ATOM   2087 N  N   . ASN A 1 270 ? 12.317  54.356 42.195  1.00 23.05 ? 270 ASN A N   1 
ATOM   2088 C  CA  . ASN A 1 270 ? 12.649  55.462 41.326  1.00 23.51 ? 270 ASN A CA  1 
ATOM   2089 C  C   . ASN A 1 270 ? 12.276  55.163 39.881  1.00 23.56 ? 270 ASN A C   1 
ATOM   2090 O  O   . ASN A 1 270 ? 11.729  56.009 39.189  1.00 23.80 ? 270 ASN A O   1 
ATOM   2091 C  CB  . ASN A 1 270 ? 14.127  55.820 41.425  1.00 23.48 ? 270 ASN A CB  1 
ATOM   2092 C  CG  . ASN A 1 270 ? 14.444  57.095 40.696  1.00 23.84 ? 270 ASN A CG  1 
ATOM   2093 O  OD1 . ASN A 1 270 ? 15.219  57.101 39.744  1.00 24.73 ? 270 ASN A OD1 1 
ATOM   2094 N  ND2 . ASN A 1 270 ? 13.812  58.184 41.110  1.00 24.20 ? 270 ASN A ND2 1 
ATOM   2095 N  N   . LEU A 1 271 ? 12.583  53.949 39.444  1.00 23.88 ? 271 LEU A N   1 
ATOM   2096 C  CA  . LEU A 1 271 ? 12.203  53.455 38.124  1.00 24.04 ? 271 LEU A CA  1 
ATOM   2097 C  C   . LEU A 1 271 ? 10.689  53.446 37.925  1.00 24.29 ? 271 LEU A C   1 
ATOM   2098 O  O   . LEU A 1 271 ? 10.203  53.915 36.903  1.00 24.62 ? 271 LEU A O   1 
ATOM   2099 C  CB  . LEU A 1 271 ? 12.779  52.053 37.913  1.00 23.87 ? 271 LEU A CB  1 
ATOM   2100 C  CG  . LEU A 1 271 ? 12.312  51.123 36.799  1.00 24.04 ? 271 LEU A CG  1 
ATOM   2101 C  CD1 . LEU A 1 271 ? 12.424  51.743 35.402  1.00 24.03 ? 271 LEU A CD1 1 
ATOM   2102 C  CD2 . LEU A 1 271 ? 13.138  49.861 36.899  1.00 23.74 ? 271 LEU A CD2 1 
ATOM   2103 N  N   . LEU A 1 272 ? 9.954   52.920 38.905  1.00 24.42 ? 272 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 272 ? 8.505   52.777 38.784  1.00 24.33 ? 272 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 272 ? 7.793   54.130 38.806  1.00 24.74 ? 272 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 272 ? 6.872   54.366 38.034  1.00 24.83 ? 272 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 272 ? 7.954   51.810 39.840  1.00 23.84 ? 272 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 272 ? 8.421   50.343 39.777  1.00 23.08 ? 272 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 272 ? 7.947   49.591 40.995  1.00 23.09 ? 272 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 272 ? 7.976   49.608 38.528  1.00 20.48 ? 272 LEU A CD2 1 
ATOM   2111 N  N   . ARG A 1 273 ? 8.243   55.031 39.665  1.00 25.46 ? 273 ARG A N   1 
ATOM   2112 C  CA  . ARG A 1 273 ? 7.659   56.367 39.736  1.00 26.31 ? 273 ARG A CA  1 
ATOM   2113 C  C   . ARG A 1 273 ? 7.876   57.090 38.412  1.00 26.66 ? 273 ARG A C   1 
ATOM   2114 O  O   . ARG A 1 273 ? 6.979   57.761 37.898  1.00 26.86 ? 273 ARG A O   1 
ATOM   2115 C  CB  . ARG A 1 273 ? 8.294   57.172 40.870  1.00 26.12 ? 273 ARG A CB  1 
ATOM   2116 C  CG  . ARG A 1 273 ? 7.576   58.476 41.186  1.00 27.67 ? 273 ARG A CG  1 
ATOM   2117 C  CD  . ARG A 1 273 ? 8.568   59.634 41.375  1.00 30.12 ? 273 ARG A CD  1 
ATOM   2118 N  NE  . ARG A 1 273 ? 9.705   59.231 42.201  1.00 31.05 ? 273 ARG A NE  1 
ATOM   2119 C  CZ  . ARG A 1 273 ? 10.953  59.659 42.037  1.00 31.25 ? 273 ARG A CZ  1 
ATOM   2120 N  NH1 . ARG A 1 273 ? 11.253  60.517 41.065  1.00 30.55 ? 273 ARG A NH1 1 
ATOM   2121 N  NH2 . ARG A 1 273 ? 11.903  59.215 42.851  1.00 31.29 ? 273 ARG A NH2 1 
ATOM   2122 N  N   . GLN A 1 274 ? 9.080   56.941 37.871  1.00 27.03 ? 274 GLN A N   1 
ATOM   2123 C  CA  . GLN A 1 274 ? 9.485   57.677 36.705  1.00 27.30 ? 274 GLN A CA  1 
ATOM   2124 C  C   . GLN A 1 274 ? 8.888   57.037 35.458  1.00 27.43 ? 274 GLN A C   1 
ATOM   2125 O  O   . GLN A 1 274 ? 8.542   57.733 34.506  1.00 27.56 ? 274 GLN A O   1 
ATOM   2126 C  CB  . GLN A 1 274 ? 11.005  57.746 36.642  1.00 27.37 ? 274 GLN A CB  1 
ATOM   2127 C  CG  . GLN A 1 274 ? 11.538  59.111 36.212  1.00 28.84 ? 274 GLN A CG  1 
ATOM   2128 C  CD  . GLN A 1 274 ? 12.850  59.475 36.895  1.00 30.09 ? 274 GLN A CD  1 
ATOM   2129 O  OE1 . GLN A 1 274 ? 13.015  59.264 38.102  1.00 29.84 ? 274 GLN A OE1 1 
ATOM   2130 N  NE2 . GLN A 1 274 ? 13.789  60.032 36.124  1.00 30.61 ? 274 GLN A NE2 1 
ATOM   2131 N  N   . ALA A 1 275 ? 8.735   55.720 35.469  1.00 27.55 ? 275 ALA A N   1 
ATOM   2132 C  CA  . ALA A 1 275 ? 8.115   55.040 34.339  1.00 28.08 ? 275 ALA A CA  1 
ATOM   2133 C  C   . ALA A 1 275 ? 6.615   55.285 34.295  1.00 28.53 ? 275 ALA A C   1 
ATOM   2134 O  O   . ALA A 1 275 ? 6.025   55.302 33.219  1.00 28.77 ? 275 ALA A O   1 
ATOM   2135 C  CB  . ALA A 1 275 ? 8.404   53.560 34.367  1.00 28.19 ? 275 ALA A CB  1 
ATOM   2136 N  N   . GLN A 1 276 ? 6.008   55.470 35.465  1.00 28.95 ? 276 GLN A N   1 
ATOM   2137 C  CA  . GLN A 1 276 ? 4.582   55.781 35.568  1.00 29.41 ? 276 GLN A CA  1 
ATOM   2138 C  C   . GLN A 1 276 ? 4.253   57.168 35.012  1.00 29.22 ? 276 GLN A C   1 
ATOM   2139 O  O   . GLN A 1 276 ? 3.278   57.325 34.290  1.00 29.16 ? 276 GLN A O   1 
ATOM   2140 C  CB  . GLN A 1 276 ? 4.117   55.674 37.018  1.00 29.16 ? 276 GLN A CB  1 
ATOM   2141 C  CG  . GLN A 1 276 ? 2.637   55.896 37.238  1.00 29.74 ? 276 GLN A CG  1 
ATOM   2142 C  CD  . GLN A 1 276 ? 2.258   55.837 38.710  1.00 30.84 ? 276 GLN A CD  1 
ATOM   2143 O  OE1 . GLN A 1 276 ? 3.071   55.483 39.568  1.00 33.09 ? 276 GLN A OE1 1 
ATOM   2144 N  NE2 . GLN A 1 276 ? 1.015   56.183 39.011  1.00 33.03 ? 276 GLN A NE2 1 
ATOM   2145 N  N   . GLU A 1 277 ? 5.060   58.170 35.346  1.00 29.26 ? 277 GLU A N   1 
ATOM   2146 C  CA  . GLU A 1 277 ? 4.789   59.532 34.895  1.00 29.75 ? 277 GLU A CA  1 
ATOM   2147 C  C   . GLU A 1 277 ? 4.980   59.626 33.391  1.00 28.91 ? 277 GLU A C   1 
ATOM   2148 O  O   . GLU A 1 277 ? 4.250   60.339 32.712  1.00 28.79 ? 277 GLU A O   1 
ATOM   2149 C  CB  . GLU A 1 277 ? 5.676   60.556 35.615  1.00 29.73 ? 277 GLU A CB  1 
ATOM   2150 C  CG  . GLU A 1 277 ? 7.166   60.269 35.467  1.00 31.40 ? 277 GLU A CG  1 
ATOM   2151 C  CD  . GLU A 1 277 ? 8.078   61.376 35.980  1.00 31.76 ? 277 GLU A CD  1 
ATOM   2152 O  OE1 . GLU A 1 277 ? 7.708   62.078 36.961  1.00 34.01 ? 277 GLU A OE1 1 
ATOM   2153 O  OE2 . GLU A 1 277 ? 9.188   61.516 35.403  1.00 33.75 ? 277 GLU A OE2 1 
ATOM   2154 N  N   . LYS A 1 278 ? 5.952   58.882 32.877  1.00 28.38 ? 278 LYS A N   1 
ATOM   2155 C  CA  . LYS A 1 278 ? 6.254   58.923 31.460  1.00 27.83 ? 278 LYS A CA  1 
ATOM   2156 C  C   . LYS A 1 278 ? 5.427   57.948 30.612  1.00 27.54 ? 278 LYS A C   1 
ATOM   2157 O  O   . LYS A 1 278 ? 5.094   58.261 29.471  1.00 27.50 ? 278 LYS A O   1 
ATOM   2158 C  CB  . LYS A 1 278 ? 7.762   58.765 31.218  1.00 27.87 ? 278 LYS A CB  1 
ATOM   2159 C  CG  . LYS A 1 278 ? 8.588   60.070 31.341  1.00 28.16 ? 278 LYS A CG  1 
ATOM   2160 C  CD  . LYS A 1 278 ? 7.950   61.232 30.566  1.00 29.55 ? 278 LYS A CD  1 
ATOM   2161 C  CE  . LYS A 1 278 ? 8.952   61.997 29.703  1.00 30.12 ? 278 LYS A CE  1 
ATOM   2162 N  NZ  . LYS A 1 278 ? 9.738   62.968 30.494  1.00 30.87 ? 278 LYS A NZ  1 
ATOM   2163 N  N   . PHE A 1 279 ? 5.078   56.783 31.164  1.00 27.22 ? 279 PHE A N   1 
ATOM   2164 C  CA  . PHE A 1 279 ? 4.390   55.740 30.381  1.00 26.92 ? 279 PHE A CA  1 
ATOM   2165 C  C   . PHE A 1 279 ? 3.152   55.097 31.031  1.00 27.20 ? 279 PHE A C   1 
ATOM   2166 O  O   . PHE A 1 279 ? 2.716   54.018 30.619  1.00 27.21 ? 279 PHE A O   1 
ATOM   2167 C  CB  . PHE A 1 279 ? 5.392   54.671 29.923  1.00 26.37 ? 279 PHE A CB  1 
ATOM   2168 C  CG  . PHE A 1 279 ? 6.615   55.234 29.246  1.00 25.62 ? 279 PHE A CG  1 
ATOM   2169 C  CD1 . PHE A 1 279 ? 6.529   55.816 27.990  1.00 24.16 ? 279 PHE A CD1 1 
ATOM   2170 C  CD2 . PHE A 1 279 ? 7.854   55.187 29.873  1.00 25.41 ? 279 PHE A CD2 1 
ATOM   2171 C  CE1 . PHE A 1 279 ? 7.656   56.344 27.370  1.00 23.93 ? 279 PHE A CE1 1 
ATOM   2172 C  CE2 . PHE A 1 279 ? 8.985   55.708 29.252  1.00 24.61 ? 279 PHE A CE2 1 
ATOM   2173 C  CZ  . PHE A 1 279 ? 8.881   56.285 27.999  1.00 24.31 ? 279 PHE A CZ  1 
ATOM   2174 N  N   . GLY A 1 280 ? 2.574   55.766 32.026  1.00 27.63 ? 280 GLY A N   1 
ATOM   2175 C  CA  . GLY A 1 280 ? 1.324   55.319 32.652  1.00 28.25 ? 280 GLY A CA  1 
ATOM   2176 C  C   . GLY A 1 280 ? 0.089   55.675 31.837  1.00 28.82 ? 280 GLY A C   1 
ATOM   2177 O  O   . GLY A 1 280 ? 0.184   55.934 30.640  1.00 28.74 ? 280 GLY A O   1 
ATOM   2178 N  N   . LYS A 1 281 ? -1.070  55.714 32.487  1.00 29.46 ? 281 LYS A N   1 
ATOM   2179 C  CA  . LYS A 1 281 ? -2.329  55.842 31.761  1.00 30.49 ? 281 LYS A CA  1 
ATOM   2180 C  C   . LYS A 1 281 ? -2.448  57.152 30.976  1.00 30.67 ? 281 LYS A C   1 
ATOM   2181 O  O   . LYS A 1 281 ? -2.305  58.245 31.538  1.00 30.84 ? 281 LYS A O   1 
ATOM   2182 C  CB  . LYS A 1 281 ? -3.525  55.648 32.697  1.00 31.21 ? 281 LYS A CB  1 
ATOM   2183 C  CG  . LYS A 1 281 ? -4.769  55.101 31.985  1.00 32.74 ? 281 LYS A CG  1 
ATOM   2184 C  CD  . LYS A 1 281 ? -6.070  55.484 32.712  1.00 35.86 ? 281 LYS A CD  1 
ATOM   2185 C  CE  . LYS A 1 281 ? -7.315  55.329 31.807  1.00 35.46 ? 281 LYS A CE  1 
ATOM   2186 N  NZ  . LYS A 1 281 ? -7.449  56.434 30.796  1.00 36.23 ? 281 LYS A NZ  1 
ATOM   2187 N  N   . ASP A 1 282 ? -2.702  57.021 29.673  1.00 30.83 ? 282 ASP A N   1 
ATOM   2188 C  CA  . ASP A 1 282 ? -2.809  58.160 28.725  1.00 30.99 ? 282 ASP A CA  1 
ATOM   2189 C  C   . ASP A 1 282 ? -1.569  59.061 28.640  1.00 30.43 ? 282 ASP A C   1 
ATOM   2190 O  O   . ASP A 1 282 ? -1.655  60.192 28.171  1.00 30.44 ? 282 ASP A O   1 
ATOM   2191 C  CB  . ASP A 1 282 ? -4.065  59.011 28.997  1.00 31.30 ? 282 ASP A CB  1 
ATOM   2192 C  CG  . ASP A 1 282 ? -5.363  58.215 28.878  1.00 33.21 ? 282 ASP A CG  1 
ATOM   2193 O  OD1 . ASP A 1 282 ? -5.426  57.243 28.083  1.00 35.40 ? 282 ASP A OD1 1 
ATOM   2194 O  OD2 . ASP A 1 282 ? -6.333  58.572 29.586  1.00 34.72 ? 282 ASP A OD2 1 
ATOM   2195 N  N   . LYS A 1 283 ? -0.418  58.549 29.062  1.00 29.94 ? 283 LYS A N   1 
ATOM   2196 C  CA  . LYS A 1 283 ? 0.781   59.372 29.192  1.00 29.36 ? 283 LYS A CA  1 
ATOM   2197 C  C   . LYS A 1 283 ? 1.572   59.510 27.907  1.00 29.01 ? 283 LYS A C   1 
ATOM   2198 O  O   . LYS A 1 283 ? 2.189   60.544 27.676  1.00 28.94 ? 283 LYS A O   1 
ATOM   2199 C  CB  . LYS A 1 283 ? 1.687   58.836 30.305  1.00 29.33 ? 283 LYS A CB  1 
ATOM   2200 C  CG  . LYS A 1 283 ? 1.121   59.001 31.713  1.00 29.31 ? 283 LYS A CG  1 
ATOM   2201 C  CD  . LYS A 1 283 ? 0.930   60.462 32.094  1.00 28.60 ? 283 LYS A CD  1 
ATOM   2202 C  CE  . LYS A 1 283 ? 0.384   60.571 33.494  1.00 28.54 ? 283 LYS A CE  1 
ATOM   2203 N  NZ  . LYS A 1 283 ? 0.486   61.965 33.978  1.00 28.64 ? 283 LYS A NZ  1 
ATOM   2204 N  N   . SER A 1 284 ? 1.567   58.465 27.086  1.00 28.78 ? 284 SER A N   1 
ATOM   2205 C  CA  . SER A 1 284 ? 2.379   58.432 25.873  1.00 28.53 ? 284 SER A CA  1 
ATOM   2206 C  C   . SER A 1 284 ? 1.787   57.538 24.800  1.00 28.27 ? 284 SER A C   1 
ATOM   2207 O  O   . SER A 1 284 ? 1.369   56.414 25.083  1.00 28.48 ? 284 SER A O   1 
ATOM   2208 C  CB  . SER A 1 284 ? 3.798   57.944 26.179  1.00 28.65 ? 284 SER A CB  1 
ATOM   2209 O  OG  . SER A 1 284 ? 4.527   57.710 24.980  1.00 28.51 ? 284 SER A OG  1 
ATOM   2210 N  N   . PRO A 1 285 ? 1.788   58.017 23.549  1.00 27.94 ? 285 PRO A N   1 
ATOM   2211 C  CA  . PRO A 1 285 ? 1.361   57.142 22.466  1.00 27.60 ? 285 PRO A CA  1 
ATOM   2212 C  C   . PRO A 1 285 ? 2.438   56.100 22.151  1.00 27.23 ? 285 PRO A C   1 
ATOM   2213 O  O   . PRO A 1 285 ? 2.121   55.014 21.653  1.00 27.60 ? 285 PRO A O   1 
ATOM   2214 C  CB  . PRO A 1 285 ? 1.180   58.101 21.277  1.00 27.65 ? 285 PRO A CB  1 
ATOM   2215 C  CG  . PRO A 1 285 ? 1.365   59.500 21.831  1.00 27.88 ? 285 PRO A CG  1 
ATOM   2216 C  CD  . PRO A 1 285 ? 2.183   59.350 23.064  1.00 27.89 ? 285 PRO A CD  1 
ATOM   2217 N  N   . LYS A 1 286 ? 3.693   56.422 22.461  1.00 26.39 ? 286 LYS A N   1 
ATOM   2218 C  CA  . LYS A 1 286 ? 4.824   55.599 22.039  1.00 25.49 ? 286 LYS A CA  1 
ATOM   2219 C  C   . LYS A 1 286 ? 4.946   54.277 22.788  1.00 24.69 ? 286 LYS A C   1 
ATOM   2220 O  O   . LYS A 1 286 ? 5.164   53.244 22.161  1.00 24.35 ? 286 LYS A O   1 
ATOM   2221 C  CB  . LYS A 1 286 ? 6.129   56.400 22.075  1.00 25.62 ? 286 LYS A CB  1 
ATOM   2222 C  CG  . LYS A 1 286 ? 6.146   57.535 21.050  1.00 26.09 ? 286 LYS A CG  1 
ATOM   2223 C  CD  . LYS A 1 286 ? 7.476   58.262 21.020  1.00 27.09 ? 286 LYS A CD  1 
ATOM   2224 C  CE  . LYS A 1 286 ? 7.351   59.573 20.268  1.00 27.69 ? 286 LYS A CE  1 
ATOM   2225 N  NZ  . LYS A 1 286 ? 8.644   60.304 20.236  1.00 28.65 ? 286 LYS A NZ  1 
ATOM   2226 N  N   . PHE A 1 287 ? 4.788   54.310 24.113  1.00 23.98 ? 287 PHE A N   1 
ATOM   2227 C  CA  . PHE A 1 287 ? 4.855   53.092 24.941  1.00 23.36 ? 287 PHE A CA  1 
ATOM   2228 C  C   . PHE A 1 287 ? 3.882   53.087 26.142  1.00 23.24 ? 287 PHE A C   1 
ATOM   2229 O  O   . PHE A 1 287 ? 3.572   54.133 26.709  1.00 23.16 ? 287 PHE A O   1 
ATOM   2230 C  CB  . PHE A 1 287 ? 6.310   52.813 25.368  1.00 23.01 ? 287 PHE A CB  1 
ATOM   2231 C  CG  . PHE A 1 287 ? 6.460   51.693 26.370  1.00 22.05 ? 287 PHE A CG  1 
ATOM   2232 C  CD1 . PHE A 1 287 ? 6.178   50.386 26.021  1.00 20.50 ? 287 PHE A CD1 1 
ATOM   2233 C  CD2 . PHE A 1 287 ? 6.889   51.960 27.665  1.00 21.33 ? 287 PHE A CD2 1 
ATOM   2234 C  CE1 . PHE A 1 287 ? 6.306   49.366 26.942  1.00 20.20 ? 287 PHE A CE1 1 
ATOM   2235 C  CE2 . PHE A 1 287 ? 7.025   50.942 28.592  1.00 20.73 ? 287 PHE A CE2 1 
ATOM   2236 C  CZ  . PHE A 1 287 ? 6.734   49.643 28.225  1.00 21.35 ? 287 PHE A CZ  1 
ATOM   2237 N  N   . GLN A 1 288 ? 3.389   51.904 26.501  1.00 23.29 ? 288 GLN A N   1 
ATOM   2238 C  CA  . GLN A 1 288 ? 2.498   51.750 27.646  1.00 23.77 ? 288 GLN A CA  1 
ATOM   2239 C  C   . GLN A 1 288 ? 2.989   50.717 28.624  1.00 23.81 ? 288 GLN A C   1 
ATOM   2240 O  O   . GLN A 1 288 ? 3.113   49.541 28.289  1.00 24.24 ? 288 GLN A O   1 
ATOM   2241 C  CB  . GLN A 1 288 ? 1.123   51.334 27.193  1.00 23.76 ? 288 GLN A CB  1 
ATOM   2242 C  CG  . GLN A 1 288 ? 0.409   52.411 26.477  1.00 26.08 ? 288 GLN A CG  1 
ATOM   2243 C  CD  . GLN A 1 288 ? -0.286  51.875 25.278  1.00 28.83 ? 288 GLN A CD  1 
ATOM   2244 O  OE1 . GLN A 1 288 ? 0.269   51.898 24.178  1.00 30.12 ? 288 GLN A OE1 1 
ATOM   2245 N  NE2 . GLN A 1 288 ? -1.499  51.344 25.474  1.00 29.55 ? 288 GLN A NE2 1 
ATOM   2246 N  N   . LEU A 1 289 ? 3.245   51.158 29.844  1.00 23.79 ? 289 LEU A N   1 
ATOM   2247 C  CA  . LEU A 1 289 ? 3.724   50.282 30.879  1.00 23.75 ? 289 LEU A CA  1 
ATOM   2248 C  C   . LEU A 1 289 ? 2.610   49.323 31.271  1.00 24.09 ? 289 LEU A C   1 
ATOM   2249 O  O   . LEU A 1 289 ? 2.871   48.164 31.582  1.00 24.21 ? 289 LEU A O   1 
ATOM   2250 C  CB  . LEU A 1 289 ? 4.172   51.110 32.083  1.00 23.73 ? 289 LEU A CB  1 
ATOM   2251 C  CG  . LEU A 1 289 ? 4.948   50.394 33.184  1.00 23.59 ? 289 LEU A CG  1 
ATOM   2252 C  CD1 . LEU A 1 289 ? 6.332   49.989 32.690  1.00 23.47 ? 289 LEU A CD1 1 
ATOM   2253 C  CD2 . LEU A 1 289 ? 5.046   51.281 34.399  1.00 23.05 ? 289 LEU A CD2 1 
ATOM   2254 N  N   . PHE A 1 290 ? 1.369   49.815 31.254  1.00 24.28 ? 290 PHE A N   1 
ATOM   2255 C  CA  . PHE A 1 290 ? 0.218   49.025 31.684  1.00 24.31 ? 290 PHE A CA  1 
ATOM   2256 C  C   . PHE A 1 290 ? -0.640  48.604 30.492  1.00 24.43 ? 290 PHE A C   1 
ATOM   2257 O  O   . PHE A 1 290 ? -1.869  48.689 30.520  1.00 25.03 ? 290 PHE A O   1 
ATOM   2258 C  CB  . PHE A 1 290 ? -0.638  49.789 32.710  1.00 24.22 ? 290 PHE A CB  1 
ATOM   2259 C  CG  . PHE A 1 290 ? 0.118   50.272 33.917  1.00 24.03 ? 290 PHE A CG  1 
ATOM   2260 C  CD1 . PHE A 1 290 ? 0.711   49.375 34.798  1.00 24.12 ? 290 PHE A CD1 1 
ATOM   2261 C  CD2 . PHE A 1 290 ? 0.203   51.630 34.194  1.00 23.87 ? 290 PHE A CD2 1 
ATOM   2262 C  CE1 . PHE A 1 290 ? 1.400   49.825 35.920  1.00 23.52 ? 290 PHE A CE1 1 
ATOM   2263 C  CE2 . PHE A 1 290 ? 0.892   52.089 35.315  1.00 22.99 ? 290 PHE A CE2 1 
ATOM   2264 C  CZ  . PHE A 1 290 ? 1.494   51.184 36.172  1.00 23.21 ? 290 PHE A CZ  1 
ATOM   2265 N  N   . GLY A 1 291 ? 0.005   48.139 29.439  1.00 24.27 ? 291 GLY A N   1 
ATOM   2266 C  CA  . GLY A 1 291 ? -0.725  47.670 28.275  1.00 23.92 ? 291 GLY A CA  1 
ATOM   2267 C  C   . GLY A 1 291 ? 0.018   46.551 27.592  1.00 23.66 ? 291 GLY A C   1 
ATOM   2268 O  O   . GLY A 1 291 ? 1.252   46.496 27.619  1.00 23.62 ? 291 GLY A O   1 
ATOM   2269 N  N   . SER A 1 292 ? -0.741  45.661 26.971  1.00 23.35 ? 292 SER A N   1 
ATOM   2270 C  CA  . SER A 1 292 ? -0.170  44.515 26.297  1.00 22.97 ? 292 SER A CA  1 
ATOM   2271 C  C   . SER A 1 292 ? -0.644  44.478 24.860  1.00 22.74 ? 292 SER A C   1 
ATOM   2272 O  O   . SER A 1 292 ? -1.753  44.910 24.569  1.00 22.47 ? 292 SER A O   1 
ATOM   2273 C  CB  . SER A 1 292 ? -0.546  43.228 27.033  1.00 22.84 ? 292 SER A CB  1 
ATOM   2274 O  OG  . SER A 1 292 ? 0.031   43.213 28.333  1.00 22.87 ? 292 SER A OG  1 
ATOM   2275 N  N   . PRO A 1 293 ? 0.204   43.979 23.945  1.00 22.77 ? 293 PRO A N   1 
ATOM   2276 C  CA  . PRO A 1 293 ? -0.278  43.818 22.574  1.00 22.80 ? 293 PRO A CA  1 
ATOM   2277 C  C   . PRO A 1 293 ? -1.487  42.881 22.493  1.00 22.90 ? 293 PRO A C   1 
ATOM   2278 O  O   . PRO A 1 293 ? -1.772  42.151 23.441  1.00 22.43 ? 293 PRO A O   1 
ATOM   2279 C  CB  . PRO A 1 293 ? 0.929   43.245 21.821  1.00 22.69 ? 293 PRO A CB  1 
ATOM   2280 C  CG  . PRO A 1 293 ? 1.926   42.868 22.847  1.00 22.82 ? 293 PRO A CG  1 
ATOM   2281 C  CD  . PRO A 1 293 ? 1.614   43.582 24.109  1.00 22.61 ? 293 PRO A CD  1 
ATOM   2282 N  N   . SER A 1 294 ? -2.204  42.939 21.372  1.00 23.30 ? 294 SER A N   1 
ATOM   2283 C  CA  . SER A 1 294 ? -3.345  42.064 21.121  1.00 23.74 ? 294 SER A CA  1 
ATOM   2284 C  C   . SER A 1 294 ? -2.941  40.593 21.218  1.00 23.95 ? 294 SER A C   1 
ATOM   2285 O  O   . SER A 1 294 ? -1.894  40.192 20.705  1.00 24.00 ? 294 SER A O   1 
ATOM   2286 C  CB  . SER A 1 294 ? -3.943  42.364 19.747  1.00 23.66 ? 294 SER A CB  1 
ATOM   2287 O  OG  . SER A 1 294 ? -4.971  41.447 19.423  1.00 24.24 ? 294 SER A OG  1 
ATOM   2288 N  N   . GLY A 1 295 ? -3.766  39.801 21.894  1.00 24.29 ? 295 GLY A N   1 
ATOM   2289 C  CA  . GLY A 1 295 ? -3.485  38.378 22.080  1.00 24.72 ? 295 GLY A CA  1 
ATOM   2290 C  C   . GLY A 1 295 ? -2.574  38.052 23.251  1.00 25.04 ? 295 GLY A C   1 
ATOM   2291 O  O   . GLY A 1 295 ? -2.236  36.893 23.463  1.00 25.20 ? 295 GLY A O   1 
ATOM   2292 N  N   . GLN A 1 296 ? -2.174  39.073 24.004  1.00 25.26 ? 296 GLN A N   1 
ATOM   2293 C  CA  . GLN A 1 296 ? -1.375  38.898 25.210  1.00 25.66 ? 296 GLN A CA  1 
ATOM   2294 C  C   . GLN A 1 296 ? -2.107  39.571 26.354  1.00 25.81 ? 296 GLN A C   1 
ATOM   2295 O  O   . GLN A 1 296 ? -2.798  40.561 26.137  1.00 26.00 ? 296 GLN A O   1 
ATOM   2296 C  CB  . GLN A 1 296 ? 0.009   39.540 25.053  1.00 26.03 ? 296 GLN A CB  1 
ATOM   2297 C  CG  . GLN A 1 296 ? 0.879   38.995 23.923  1.00 26.69 ? 296 GLN A CG  1 
ATOM   2298 C  CD  . GLN A 1 296 ? 1.166   37.510 24.076  1.00 28.61 ? 296 GLN A CD  1 
ATOM   2299 O  OE1 . GLN A 1 296 ? 1.119   36.954 25.187  1.00 27.66 ? 296 GLN A OE1 1 
ATOM   2300 N  NE2 . GLN A 1 296 ? 1.465   36.852 22.951  1.00 29.16 ? 296 GLN A NE2 1 
ATOM   2301 N  N   . LYS A 1 297 ? -1.959  39.052 27.569  1.00 25.92 ? 297 LYS A N   1 
ATOM   2302 C  CA  . LYS A 1 297 ? -2.662  39.623 28.709  1.00 26.34 ? 297 LYS A CA  1 
ATOM   2303 C  C   . LYS A 1 297 ? -1.706  39.945 29.831  1.00 26.24 ? 297 LYS A C   1 
ATOM   2304 O  O   . LYS A 1 297 ? -0.829  39.146 30.143  1.00 26.36 ? 297 LYS A O   1 
ATOM   2305 C  CB  . LYS A 1 297 ? -3.716  38.655 29.238  1.00 26.66 ? 297 LYS A CB  1 
ATOM   2306 C  CG  . LYS A 1 297 ? -4.906  38.421 28.330  1.00 29.23 ? 297 LYS A CG  1 
ATOM   2307 C  CD  . LYS A 1 297 ? -5.900  39.590 28.348  1.00 32.74 ? 297 LYS A CD  1 
ATOM   2308 C  CE  . LYS A 1 297 ? -7.034  39.360 27.329  1.00 34.23 ? 297 LYS A CE  1 
ATOM   2309 N  NZ  . LYS A 1 297 ? -7.835  40.604 27.099  1.00 35.40 ? 297 LYS A NZ  1 
ATOM   2310 N  N   . ASP A 1 298 ? -1.884  41.115 30.439  1.00 26.09 ? 298 ASP A N   1 
ATOM   2311 C  CA  . ASP A 1 298 ? -1.192  41.470 31.681  1.00 26.26 ? 298 ASP A CA  1 
ATOM   2312 C  C   . ASP A 1 298 ? 0.323   41.175 31.710  1.00 25.74 ? 298 ASP A C   1 
ATOM   2313 O  O   . ASP A 1 298 ? 0.827   40.569 32.657  1.00 25.41 ? 298 ASP A O   1 
ATOM   2314 C  CB  . ASP A 1 298 ? -1.884  40.795 32.877  1.00 26.59 ? 298 ASP A CB  1 
ATOM   2315 C  CG  . ASP A 1 298 ? -3.328  41.260 33.075  1.00 28.34 ? 298 ASP A CG  1 
ATOM   2316 O  OD1 . ASP A 1 298 ? -3.697  42.362 32.603  1.00 29.41 ? 298 ASP A OD1 1 
ATOM   2317 O  OD2 . ASP A 1 298 ? -4.100  40.516 33.724  1.00 30.94 ? 298 ASP A OD2 1 
ATOM   2318 N  N   . LEU A 1 299 ? 1.040   41.620 30.680  1.00 25.19 ? 299 LEU A N   1 
ATOM   2319 C  CA  . LEU A 1 299 ? 2.489   41.456 30.627  1.00 24.64 ? 299 LEU A CA  1 
ATOM   2320 C  C   . LEU A 1 299 ? 3.190   42.386 31.622  1.00 24.81 ? 299 LEU A C   1 
ATOM   2321 O  O   . LEU A 1 299 ? 3.054   43.612 31.542  1.00 24.78 ? 299 LEU A O   1 
ATOM   2322 C  CB  . LEU A 1 299 ? 3.005   41.692 29.204  1.00 24.40 ? 299 LEU A CB  1 
ATOM   2323 C  CG  . LEU A 1 299 ? 2.496   40.801 28.049  1.00 24.02 ? 299 LEU A CG  1 
ATOM   2324 C  CD1 . LEU A 1 299 ? 3.129   41.204 26.720  1.00 23.96 ? 299 LEU A CD1 1 
ATOM   2325 C  CD2 . LEU A 1 299 ? 2.712   39.320 28.286  1.00 22.02 ? 299 LEU A CD2 1 
ATOM   2326 N  N   . LEU A 1 300 ? 3.930   41.789 32.561  1.00 24.90 ? 300 LEU A N   1 
ATOM   2327 C  CA  . LEU A 1 300 ? 4.686   42.510 33.617  1.00 24.99 ? 300 LEU A CA  1 
ATOM   2328 C  C   . LEU A 1 300 ? 3.806   43.151 34.684  1.00 25.03 ? 300 LEU A C   1 
ATOM   2329 O  O   . LEU A 1 300 ? 4.086   43.027 35.875  1.00 25.23 ? 300 LEU A O   1 
ATOM   2330 C  CB  . LEU A 1 300 ? 5.640   43.570 33.047  1.00 24.80 ? 300 LEU A CB  1 
ATOM   2331 C  CG  . LEU A 1 300 ? 6.655   43.156 31.989  1.00 25.15 ? 300 LEU A CG  1 
ATOM   2332 C  CD1 . LEU A 1 300 ? 7.345   44.387 31.419  1.00 25.91 ? 300 LEU A CD1 1 
ATOM   2333 C  CD2 . LEU A 1 300 ? 7.664   42.185 32.574  1.00 26.45 ? 300 LEU A CD2 1 
ATOM   2334 N  N   . PHE A 1 301 ? 2.769   43.864 34.259  1.00 24.90 ? 301 PHE A N   1 
ATOM   2335 C  CA  . PHE A 1 301 ? 1.826   44.464 35.196  1.00 24.99 ? 301 PHE A CA  1 
ATOM   2336 C  C   . PHE A 1 301 ? 0.415   44.251 34.682  1.00 25.40 ? 301 PHE A C   1 
ATOM   2337 O  O   . PHE A 1 301 ? 0.214   44.003 33.483  1.00 25.48 ? 301 PHE A O   1 
ATOM   2338 C  CB  . PHE A 1 301 ? 2.102   45.959 35.401  1.00 24.67 ? 301 PHE A CB  1 
ATOM   2339 C  CG  . PHE A 1 301 ? 3.544   46.284 35.651  1.00 24.02 ? 301 PHE A CG  1 
ATOM   2340 C  CD1 . PHE A 1 301 ? 4.091   46.145 36.920  1.00 23.64 ? 301 PHE A CD1 1 
ATOM   2341 C  CD2 . PHE A 1 301 ? 4.356   46.732 34.613  1.00 23.34 ? 301 PHE A CD2 1 
ATOM   2342 C  CE1 . PHE A 1 301 ? 5.429   46.439 37.155  1.00 23.36 ? 301 PHE A CE1 1 
ATOM   2343 C  CE2 . PHE A 1 301 ? 5.696   47.029 34.831  1.00 22.94 ? 301 PHE A CE2 1 
ATOM   2344 C  CZ  . PHE A 1 301 ? 6.234   46.888 36.104  1.00 23.84 ? 301 PHE A CZ  1 
ATOM   2345 N  N   . LYS A 1 302 ? -0.555  44.331 35.589  1.00 25.72 ? 302 LYS A N   1 
ATOM   2346 C  CA  . LYS A 1 302 ? -1.968  44.198 35.237  1.00 26.35 ? 302 LYS A CA  1 
ATOM   2347 C  C   . LYS A 1 302 ? -2.338  45.273 34.207  1.00 26.39 ? 302 LYS A C   1 
ATOM   2348 O  O   . LYS A 1 302 ? -1.939  46.419 34.348  1.00 26.26 ? 302 LYS A O   1 
ATOM   2349 C  CB  . LYS A 1 302 ? -2.819  44.331 36.507  1.00 26.49 ? 302 LYS A CB  1 
ATOM   2350 C  CG  . LYS A 1 302 ? -4.302  44.030 36.353  1.00 26.96 ? 302 LYS A CG  1 
ATOM   2351 C  CD  . LYS A 1 302 ? -4.581  42.544 36.349  1.00 27.78 ? 302 LYS A CD  1 
ATOM   2352 C  CE  . LYS A 1 302 ? -6.032  42.289 36.033  1.00 29.76 ? 302 LYS A CE  1 
ATOM   2353 N  NZ  . LYS A 1 302 ? -6.395  42.943 34.724  1.00 32.59 ? 302 LYS A NZ  1 
ATOM   2354 N  N   . ASP A 1 303 ? -3.076  44.905 33.167  1.00 26.83 ? 303 ASP A N   1 
ATOM   2355 C  CA  . ASP A 1 303 ? -3.391  45.862 32.095  1.00 27.71 ? 303 ASP A CA  1 
ATOM   2356 C  C   . ASP A 1 303 ? -4.239  47.056 32.569  1.00 27.89 ? 303 ASP A C   1 
ATOM   2357 O  O   . ASP A 1 303 ? -4.027  48.197 32.139  1.00 27.80 ? 303 ASP A O   1 
ATOM   2358 C  CB  . ASP A 1 303 ? -4.057  45.154 30.913  1.00 27.96 ? 303 ASP A CB  1 
ATOM   2359 C  CG  . ASP A 1 303 ? -3.107  44.205 30.182  1.00 29.46 ? 303 ASP A CG  1 
ATOM   2360 O  OD1 . ASP A 1 303 ? -1.869  44.416 30.254  1.00 32.13 ? 303 ASP A OD1 1 
ATOM   2361 O  OD2 . ASP A 1 303 ? -3.597  43.248 29.535  1.00 29.54 ? 303 ASP A OD2 1 
ATOM   2362 N  N   . SER A 1 304 ? -5.174  46.782 33.479  1.00 27.87 ? 304 SER A N   1 
ATOM   2363 C  CA  . SER A 1 304 ? -6.066  47.797 34.022  1.00 27.58 ? 304 SER A CA  1 
ATOM   2364 C  C   . SER A 1 304 ? -5.443  48.537 35.213  1.00 27.22 ? 304 SER A C   1 
ATOM   2365 O  O   . SER A 1 304 ? -6.098  49.370 35.844  1.00 27.37 ? 304 SER A O   1 
ATOM   2366 C  CB  . SER A 1 304 ? -7.395  47.150 34.431  1.00 28.02 ? 304 SER A CB  1 
ATOM   2367 O  OG  . SER A 1 304 ? -7.201  46.189 35.466  1.00 28.72 ? 304 SER A OG  1 
ATOM   2368 N  N   . ALA A 1 305 ? -4.191  48.223 35.532  1.00 26.66 ? 305 ALA A N   1 
ATOM   2369 C  CA  . ALA A 1 305 ? -3.450  48.984 36.538  1.00 26.18 ? 305 ALA A CA  1 
ATOM   2370 C  C   . ALA A 1 305 ? -3.249  50.420 36.059  1.00 25.92 ? 305 ALA A C   1 
ATOM   2371 O  O   . ALA A 1 305 ? -3.054  50.660 34.866  1.00 25.91 ? 305 ALA A O   1 
ATOM   2372 C  CB  . ALA A 1 305 ? -2.111  48.332 36.831  1.00 26.01 ? 305 ALA A CB  1 
ATOM   2373 N  N   . ILE A 1 306 ? -3.304  51.368 36.992  1.00 25.60 ? 306 ILE A N   1 
ATOM   2374 C  CA  . ILE A 1 306 ? -3.146  52.789 36.663  1.00 25.24 ? 306 ILE A CA  1 
ATOM   2375 C  C   . ILE A 1 306 ? -1.916  53.414 37.311  1.00 25.07 ? 306 ILE A C   1 
ATOM   2376 O  O   . ILE A 1 306 ? -1.574  54.568 37.026  1.00 25.38 ? 306 ILE A O   1 
ATOM   2377 C  CB  . ILE A 1 306 ? -4.389  53.613 37.033  1.00 25.13 ? 306 ILE A CB  1 
ATOM   2378 C  CG1 . ILE A 1 306 ? -4.544  53.705 38.558  1.00 25.22 ? 306 ILE A CG1 1 
ATOM   2379 C  CG2 . ILE A 1 306 ? -5.634  53.024 36.350  1.00 25.23 ? 306 ILE A CG2 1 
ATOM   2380 C  CD1 . ILE A 1 306 ? -5.445  54.850 39.013  1.00 25.57 ? 306 ILE A CD1 1 
ATOM   2381 N  N   . GLY A 1 307 ? -1.250  52.656 38.176  1.00 24.60 ? 307 GLY A N   1 
ATOM   2382 C  CA  . GLY A 1 307 ? -0.046  53.145 38.826  1.00 24.21 ? 307 GLY A CA  1 
ATOM   2383 C  C   . GLY A 1 307 ? 0.456   52.266 39.944  1.00 24.01 ? 307 GLY A C   1 
ATOM   2384 O  O   . GLY A 1 307 ? 0.021   51.129 40.100  1.00 23.71 ? 307 GLY A O   1 
ATOM   2385 N  N   . PHE A 1 308 ? 1.389   52.807 40.718  1.00 24.09 ? 308 PHE A N   1 
ATOM   2386 C  CA  . PHE A 1 308 ? 1.991   52.079 41.817  1.00 24.13 ? 308 PHE A CA  1 
ATOM   2387 C  C   . PHE A 1 308 ? 1.824   52.854 43.089  1.00 24.18 ? 308 PHE A C   1 
ATOM   2388 O  O   . PHE A 1 308 ? 1.633   54.063 43.070  1.00 24.22 ? 308 PHE A O   1 
ATOM   2389 C  CB  . PHE A 1 308 ? 3.483   51.852 41.569  1.00 24.33 ? 308 PHE A CB  1 
ATOM   2390 C  CG  . PHE A 1 308 ? 3.781   51.124 40.292  1.00 24.02 ? 308 PHE A CG  1 
ATOM   2391 C  CD1 . PHE A 1 308 ? 3.503   49.765 40.172  1.00 23.86 ? 308 PHE A CD1 1 
ATOM   2392 C  CD2 . PHE A 1 308 ? 4.335   51.801 39.210  1.00 23.95 ? 308 PHE A CD2 1 
ATOM   2393 C  CE1 . PHE A 1 308 ? 3.775   49.084 38.992  1.00 24.81 ? 308 PHE A CE1 1 
ATOM   2394 C  CE2 . PHE A 1 308 ? 4.613   51.142 38.025  1.00 24.72 ? 308 PHE A CE2 1 
ATOM   2395 C  CZ  . PHE A 1 308 ? 4.332   49.773 37.910  1.00 25.32 ? 308 PHE A CZ  1 
ATOM   2396 N  N   . SER A 1 309 ? 1.892   52.134 44.197  1.00 24.46 ? 309 SER A N   1 
ATOM   2397 C  CA  . SER A 1 309 ? 1.884   52.732 45.519  1.00 24.52 ? 309 SER A CA  1 
ATOM   2398 C  C   . SER A 1 309 ? 3.011   52.109 46.330  1.00 24.82 ? 309 SER A C   1 
ATOM   2399 O  O   . SER A 1 309 ? 3.101   50.879 46.446  1.00 24.85 ? 309 SER A O   1 
ATOM   2400 C  CB  . SER A 1 309 ? 0.539   52.497 46.194  1.00 24.23 ? 309 SER A CB  1 
ATOM   2401 O  OG  . SER A 1 309 ? 0.592   52.868 47.551  1.00 23.95 ? 309 SER A OG  1 
ATOM   2402 N  N   . ARG A 1 310 ? 3.878   52.956 46.877  1.00 25.09 ? 310 ARG A N   1 
ATOM   2403 C  CA  . ARG A 1 310 ? 5.027   52.464 47.628  1.00 25.30 ? 310 ARG A CA  1 
ATOM   2404 C  C   . ARG A 1 310 ? 4.620   51.727 48.914  1.00 25.41 ? 310 ARG A C   1 
ATOM   2405 O  O   . ARG A 1 310 ? 3.730   52.166 49.654  1.00 25.43 ? 310 ARG A O   1 
ATOM   2406 C  CB  . ARG A 1 310 ? 6.029   53.587 47.918  1.00 25.01 ? 310 ARG A CB  1 
ATOM   2407 C  CG  . ARG A 1 310 ? 7.380   53.049 48.361  1.00 25.49 ? 310 ARG A CG  1 
ATOM   2408 C  CD  . ARG A 1 310 ? 8.485   54.055 48.235  1.00 26.37 ? 310 ARG A CD  1 
ATOM   2409 N  NE  . ARG A 1 310 ? 9.807   53.438 48.376  1.00 26.83 ? 310 ARG A NE  1 
ATOM   2410 C  CZ  . ARG A 1 310 ? 10.950  54.123 48.445  1.00 26.72 ? 310 ARG A CZ  1 
ATOM   2411 N  NH1 . ARG A 1 310 ? 10.941  55.454 48.397  1.00 25.47 ? 310 ARG A NH1 1 
ATOM   2412 N  NH2 . ARG A 1 310 ? 12.105  53.477 48.567  1.00 26.36 ? 310 ARG A NH2 1 
ATOM   2413 N  N   . VAL A 1 311 ? 5.266   50.590 49.151  1.00 25.46 ? 311 VAL A N   1 
ATOM   2414 C  CA  . VAL A 1 311 ? 5.062   49.834 50.375  1.00 25.52 ? 311 VAL A CA  1 
ATOM   2415 C  C   . VAL A 1 311 ? 6.010   50.355 51.449  1.00 26.08 ? 311 VAL A C   1 
ATOM   2416 O  O   . VAL A 1 311 ? 7.228   50.258 51.294  1.00 25.98 ? 311 VAL A O   1 
ATOM   2417 C  CB  . VAL A 1 311 ? 5.276   48.334 50.148  1.00 25.21 ? 311 VAL A CB  1 
ATOM   2418 C  CG1 . VAL A 1 311 ? 5.220   47.581 51.463  1.00 25.10 ? 311 VAL A CG1 1 
ATOM   2419 C  CG2 . VAL A 1 311 ? 4.238   47.809 49.192  1.00 24.52 ? 311 VAL A CG2 1 
ATOM   2420 N  N   . PRO A 1 312 ? 5.449   50.908 52.546  1.00 26.80 ? 312 PRO A N   1 
ATOM   2421 C  CA  . PRO A 1 312 ? 6.230   51.473 53.658  1.00 27.23 ? 312 PRO A CA  1 
ATOM   2422 C  C   . PRO A 1 312 ? 7.358   50.535 54.090  1.00 27.90 ? 312 PRO A C   1 
ATOM   2423 O  O   . PRO A 1 312 ? 7.232   49.323 53.922  1.00 27.91 ? 312 PRO A O   1 
ATOM   2424 C  CB  . PRO A 1 312 ? 5.192   51.613 54.777  1.00 27.07 ? 312 PRO A CB  1 
ATOM   2425 C  CG  . PRO A 1 312 ? 3.900   51.814 54.066  1.00 26.86 ? 312 PRO A CG  1 
ATOM   2426 C  CD  . PRO A 1 312 ? 3.994   51.005 52.791  1.00 26.81 ? 312 PRO A CD  1 
ATOM   2427 N  N   . PRO A 1 313 ? 8.456   51.088 54.646  1.00 28.71 ? 313 PRO A N   1 
ATOM   2428 C  CA  . PRO A 1 313 ? 9.680   50.310 54.914  1.00 29.03 ? 313 PRO A CA  1 
ATOM   2429 C  C   . PRO A 1 313 ? 9.527   49.043 55.777  1.00 29.36 ? 313 PRO A C   1 
ATOM   2430 O  O   . PRO A 1 313 ? 10.011  47.991 55.371  1.00 29.58 ? 313 PRO A O   1 
ATOM   2431 C  CB  . PRO A 1 313 ? 10.605  51.327 55.598  1.00 28.89 ? 313 PRO A CB  1 
ATOM   2432 C  CG  . PRO A 1 313 ? 9.683   52.402 56.102  1.00 28.97 ? 313 PRO A CG  1 
ATOM   2433 C  CD  . PRO A 1 313 ? 8.616   52.495 55.062  1.00 28.76 ? 313 PRO A CD  1 
ATOM   2434 N  N   . ARG A 1 314 ? 8.866   49.123 56.930  1.00 29.56 ? 314 ARG A N   1 
ATOM   2435 C  CA  . ARG A 1 314 ? 8.889   48.001 57.887  1.00 30.11 ? 314 ARG A CA  1 
ATOM   2436 C  C   . ARG A 1 314 ? 7.844   46.912 57.631  1.00 29.78 ? 314 ARG A C   1 
ATOM   2437 O  O   . ARG A 1 314 ? 7.401   46.232 58.559  1.00 29.84 ? 314 ARG A O   1 
ATOM   2438 C  CB  . ARG A 1 314 ? 8.777   48.510 59.334  1.00 30.68 ? 314 ARG A CB  1 
ATOM   2439 C  CG  . ARG A 1 314 ? 10.090  49.067 59.944  1.00 32.77 ? 314 ARG A CG  1 
ATOM   2440 C  CD  . ARG A 1 314 ? 10.880  47.994 60.706  1.00 35.54 ? 314 ARG A CD  1 
ATOM   2441 N  NE  . ARG A 1 314 ? 11.214  48.444 62.062  1.00 37.71 ? 314 ARG A NE  1 
ATOM   2442 C  CZ  . ARG A 1 314 ? 10.554  48.100 63.174  1.00 38.30 ? 314 ARG A CZ  1 
ATOM   2443 N  NH1 . ARG A 1 314 ? 9.510   47.271 63.131  1.00 37.82 ? 314 ARG A NH1 1 
ATOM   2444 N  NH2 . ARG A 1 314 ? 10.951  48.587 64.344  1.00 38.18 ? 314 ARG A NH2 1 
ATOM   2445 N  N   . ILE A 1 315 ? 7.470   46.730 56.373  1.00 29.28 ? 315 ILE A N   1 
ATOM   2446 C  CA  . ILE A 1 315 ? 6.418   45.799 56.040  1.00 28.90 ? 315 ILE A CA  1 
ATOM   2447 C  C   . ILE A 1 315 ? 6.995   44.668 55.221  1.00 28.71 ? 315 ILE A C   1 
ATOM   2448 O  O   . ILE A 1 315 ? 7.554   44.897 54.153  1.00 28.98 ? 315 ILE A O   1 
ATOM   2449 C  CB  . ILE A 1 315 ? 5.240   46.514 55.331  1.00 28.81 ? 315 ILE A CB  1 
ATOM   2450 C  CG1 . ILE A 1 315 ? 4.431   47.294 56.379  1.00 29.17 ? 315 ILE A CG1 1 
ATOM   2451 C  CG2 . ILE A 1 315 ? 4.361   45.529 54.551  1.00 27.92 ? 315 ILE A CG2 1 
ATOM   2452 C  CD1 . ILE A 1 315 ? 3.041   47.755 55.931  1.00 29.88 ? 315 ILE A CD1 1 
ATOM   2453 N  N   . ASP A 1 316 ? 6.881   43.454 55.762  1.00 28.40 ? 316 ASP A N   1 
ATOM   2454 C  CA  . ASP A 1 316 ? 7.304   42.219 55.095  1.00 27.92 ? 316 ASP A CA  1 
ATOM   2455 C  C   . ASP A 1 316 ? 6.120   41.586 54.372  1.00 27.44 ? 316 ASP A C   1 
ATOM   2456 O  O   . ASP A 1 316 ? 5.042   42.173 54.332  1.00 27.57 ? 316 ASP A O   1 
ATOM   2457 C  CB  . ASP A 1 316 ? 7.896   41.238 56.109  1.00 28.11 ? 316 ASP A CB  1 
ATOM   2458 C  CG  . ASP A 1 316 ? 6.963   40.965 57.281  1.00 28.89 ? 316 ASP A CG  1 
ATOM   2459 O  OD1 . ASP A 1 316 ? 5.727   40.919 57.077  1.00 29.17 ? 316 ASP A OD1 1 
ATOM   2460 O  OD2 . ASP A 1 316 ? 7.473   40.791 58.412  1.00 30.29 ? 316 ASP A OD2 1 
ATOM   2461 N  N   . SER A 1 317 ? 6.307   40.392 53.814  1.00 26.73 ? 317 SER A N   1 
ATOM   2462 C  CA  . SER A 1 317 ? 5.257   39.777 53.011  1.00 26.01 ? 317 SER A CA  1 
ATOM   2463 C  C   . SER A 1 317 ? 3.994   39.502 53.824  1.00 25.67 ? 317 SER A C   1 
ATOM   2464 O  O   . SER A 1 317 ? 2.885   39.803 53.382  1.00 25.68 ? 317 SER A O   1 
ATOM   2465 C  CB  . SER A 1 317 ? 5.758   38.502 52.349  1.00 25.88 ? 317 SER A CB  1 
ATOM   2466 O  OG  . SER A 1 317 ? 5.765   37.445 53.278  1.00 26.17 ? 317 SER A OG  1 
ATOM   2467 N  N   . GLY A 1 318 ? 4.171   38.934 55.015  1.00 25.44 ? 318 GLY A N   1 
ATOM   2468 C  CA  . GLY A 1 318 ? 3.052   38.619 55.905  1.00 24.75 ? 318 GLY A CA  1 
ATOM   2469 C  C   . GLY A 1 318 ? 2.206   39.834 56.236  1.00 24.29 ? 318 GLY A C   1 
ATOM   2470 O  O   . GLY A 1 318 ? 0.982   39.779 56.147  1.00 24.39 ? 318 GLY A O   1 
ATOM   2471 N  N   . LEU A 1 319 ? 2.866   40.929 56.613  1.00 23.74 ? 319 LEU A N   1 
ATOM   2472 C  CA  . LEU A 1 319 ? 2.189   42.191 56.903  1.00 23.16 ? 319 LEU A CA  1 
ATOM   2473 C  C   . LEU A 1 319 ? 1.559   42.809 55.656  1.00 22.78 ? 319 LEU A C   1 
ATOM   2474 O  O   . LEU A 1 319 ? 0.477   43.383 55.734  1.00 22.92 ? 319 LEU A O   1 
ATOM   2475 C  CB  . LEU A 1 319 ? 3.135   43.192 57.571  1.00 22.99 ? 319 LEU A CB  1 
ATOM   2476 C  CG  . LEU A 1 319 ? 3.536   42.912 59.020  1.00 23.05 ? 319 LEU A CG  1 
ATOM   2477 C  CD1 . LEU A 1 319 ? 4.691   43.800 59.443  1.00 22.94 ? 319 LEU A CD1 1 
ATOM   2478 C  CD2 . LEU A 1 319 ? 2.353   43.074 59.973  1.00 23.30 ? 319 LEU A CD2 1 
ATOM   2479 N  N   . TYR A 1 320 ? 2.221   42.694 54.509  1.00 22.30 ? 320 TYR A N   1 
ATOM   2480 C  CA  . TYR A 1 320 ? 1.622   43.178 53.266  1.00 22.06 ? 320 TYR A CA  1 
ATOM   2481 C  C   . TYR A 1 320 ? 0.305   42.480 52.960  1.00 21.95 ? 320 TYR A C   1 
ATOM   2482 O  O   . TYR A 1 320 ? -0.671  43.143 52.655  1.00 22.33 ? 320 TYR A O   1 
ATOM   2483 C  CB  . TYR A 1 320 ? 2.562   43.084 52.054  1.00 21.80 ? 320 TYR A CB  1 
ATOM   2484 C  CG  . TYR A 1 320 ? 1.890   43.583 50.801  1.00 21.82 ? 320 TYR A CG  1 
ATOM   2485 C  CD1 . TYR A 1 320 ? 1.768   44.954 50.553  1.00 22.18 ? 320 TYR A CD1 1 
ATOM   2486 C  CD2 . TYR A 1 320 ? 1.325   42.690 49.877  1.00 22.06 ? 320 TYR A CD2 1 
ATOM   2487 C  CE1 . TYR A 1 320 ? 1.121   45.429 49.397  1.00 22.01 ? 320 TYR A CE1 1 
ATOM   2488 C  CE2 . TYR A 1 320 ? 0.672   43.152 48.721  1.00 20.72 ? 320 TYR A CE2 1 
ATOM   2489 C  CZ  . TYR A 1 320 ? 0.581   44.518 48.494  1.00 21.70 ? 320 TYR A CZ  1 
ATOM   2490 O  OH  . TYR A 1 320 ? -0.060  44.987 47.379  1.00 22.47 ? 320 TYR A OH  1 
ATOM   2491 N  N   . LEU A 1 321 ? 0.274   41.153 53.048  1.00 21.73 ? 321 LEU A N   1 
ATOM   2492 C  CA  . LEU A 1 321 ? -0.929  40.401 52.690  1.00 21.67 ? 321 LEU A CA  1 
ATOM   2493 C  C   . LEU A 1 321 ? -2.084  40.580 53.668  1.00 21.44 ? 321 LEU A C   1 
ATOM   2494 O  O   . LEU A 1 321 ? -3.211  40.181 53.386  1.00 21.26 ? 321 LEU A O   1 
ATOM   2495 C  CB  . LEU A 1 321 ? -0.623  38.910 52.496  1.00 21.74 ? 321 LEU A CB  1 
ATOM   2496 C  CG  . LEU A 1 321 ? 0.197   38.558 51.255  1.00 21.72 ? 321 LEU A CG  1 
ATOM   2497 C  CD1 . LEU A 1 321 ? 0.554   37.080 51.244  1.00 21.70 ? 321 LEU A CD1 1 
ATOM   2498 C  CD2 . LEU A 1 321 ? -0.549  38.957 49.989  1.00 22.16 ? 321 LEU A CD2 1 
ATOM   2499 N  N   . GLY A 1 322 ? -1.801  41.178 54.815  1.00 21.47 ? 322 GLY A N   1 
ATOM   2500 C  CA  . GLY A 1 322 ? -2.821  41.386 55.831  1.00 21.74 ? 322 GLY A CA  1 
ATOM   2501 C  C   . GLY A 1 322 ? -3.137  40.138 56.636  1.00 21.99 ? 322 GLY A C   1 
ATOM   2502 O  O   . GLY A 1 322 ? -3.271  39.039 56.095  1.00 21.93 ? 322 GLY A O   1 
ATOM   2503 N  N   . SER A 1 323 ? -3.254  40.332 57.944  1.00 22.38 ? 323 SER A N   1 
ATOM   2504 C  CA  . SER A 1 323 ? -3.647  39.299 58.908  1.00 22.56 ? 323 SER A CA  1 
ATOM   2505 C  C   . SER A 1 323 ? -4.593  38.220 58.357  1.00 22.47 ? 323 SER A C   1 
ATOM   2506 O  O   . SER A 1 323 ? -4.278  37.033 58.402  1.00 22.57 ? 323 SER A O   1 
ATOM   2507 C  CB  . SER A 1 323 ? -4.284  39.991 60.118  1.00 22.70 ? 323 SER A CB  1 
ATOM   2508 O  OG  . SER A 1 323 ? -4.573  39.077 61.150  1.00 23.81 ? 323 SER A OG  1 
ATOM   2509 N  N   . GLY A 1 324 ? -5.740  38.647 57.825  1.00 22.53 ? 324 GLY A N   1 
ATOM   2510 C  CA  . GLY A 1 324 ? -6.800  37.746 57.365  1.00 21.93 ? 324 GLY A CA  1 
ATOM   2511 C  C   . GLY A 1 324 ? -6.411  36.765 56.282  1.00 21.77 ? 324 GLY A C   1 
ATOM   2512 O  O   . GLY A 1 324 ? -6.641  35.579 56.425  1.00 21.94 ? 324 GLY A O   1 
ATOM   2513 N  N   . TYR A 1 325 ? -5.827  37.253 55.193  1.00 21.74 ? 325 TYR A N   1 
ATOM   2514 C  CA  . TYR A 1 325 ? -5.430  36.377 54.083  1.00 21.40 ? 325 TYR A CA  1 
ATOM   2515 C  C   . TYR A 1 325 ? -4.174  35.584 54.447  1.00 21.21 ? 325 TYR A C   1 
ATOM   2516 O  O   . TYR A 1 325 ? -4.073  34.402 54.130  1.00 21.45 ? 325 TYR A O   1 
ATOM   2517 C  CB  . TYR A 1 325 ? -5.259  37.186 52.782  1.00 21.53 ? 325 TYR A CB  1 
ATOM   2518 C  CG  . TYR A 1 325 ? -4.831  36.411 51.562  1.00 21.27 ? 325 TYR A CG  1 
ATOM   2519 C  CD1 . TYR A 1 325 ? -5.390  35.181 51.255  1.00 22.33 ? 325 TYR A CD1 1 
ATOM   2520 C  CD2 . TYR A 1 325 ? -3.877  36.927 50.696  1.00 22.45 ? 325 TYR A CD2 1 
ATOM   2521 C  CE1 . TYR A 1 325 ? -4.991  34.462 50.122  1.00 23.37 ? 325 TYR A CE1 1 
ATOM   2522 C  CE2 . TYR A 1 325 ? -3.467  36.230 49.553  1.00 23.15 ? 325 TYR A CE2 1 
ATOM   2523 C  CZ  . TYR A 1 325 ? -4.032  34.996 49.269  1.00 23.73 ? 325 TYR A CZ  1 
ATOM   2524 O  OH  . TYR A 1 325 ? -3.642  34.293 48.145  1.00 22.56 ? 325 TYR A OH  1 
ATOM   2525 N  N   . PHE A 1 326 ? -3.240  36.223 55.142  1.00 20.81 ? 326 PHE A N   1 
ATOM   2526 C  CA  . PHE A 1 326 ? -2.020  35.563 55.585  1.00 20.67 ? 326 PHE A CA  1 
ATOM   2527 C  C   . PHE A 1 326 ? -2.306  34.397 56.531  1.00 21.08 ? 326 PHE A C   1 
ATOM   2528 O  O   . PHE A 1 326 ? -1.681  33.346 56.412  1.00 21.32 ? 326 PHE A O   1 
ATOM   2529 C  CB  . PHE A 1 326 ? -1.078  36.570 56.245  1.00 20.26 ? 326 PHE A CB  1 
ATOM   2530 C  CG  . PHE A 1 326 ? 0.304   36.045 56.485  1.00 19.55 ? 326 PHE A CG  1 
ATOM   2531 C  CD1 . PHE A 1 326 ? 1.075   35.556 55.432  1.00 18.81 ? 326 PHE A CD1 1 
ATOM   2532 C  CD2 . PHE A 1 326 ? 0.852   36.062 57.767  1.00 19.20 ? 326 PHE A CD2 1 
ATOM   2533 C  CE1 . PHE A 1 326 ? 2.365   35.072 55.651  1.00 18.06 ? 326 PHE A CE1 1 
ATOM   2534 C  CE2 . PHE A 1 326 ? 2.144   35.589 57.997  1.00 18.45 ? 326 PHE A CE2 1 
ATOM   2535 C  CZ  . PHE A 1 326 ? 2.901   35.093 56.932  1.00 18.81 ? 326 PHE A CZ  1 
ATOM   2536 N  N   . THR A 1 327 ? -3.248  34.568 57.460  1.00 21.44 ? 327 THR A N   1 
ATOM   2537 C  CA  . THR A 1 327 ? -3.655  33.457 58.327  1.00 21.92 ? 327 THR A CA  1 
ATOM   2538 C  C   . THR A 1 327 ? -4.315  32.351 57.505  1.00 22.33 ? 327 THR A C   1 
ATOM   2539 O  O   . THR A 1 327 ? -4.089  31.173 57.767  1.00 22.53 ? 327 THR A O   1 
ATOM   2540 C  CB  . THR A 1 327 ? -4.617  33.882 59.479  1.00 21.86 ? 327 THR A CB  1 
ATOM   2541 O  OG1 . THR A 1 327 ? -4.104  35.031 60.164  1.00 22.05 ? 327 THR A OG1 1 
ATOM   2542 C  CG2 . THR A 1 327 ? -4.777  32.756 60.489  1.00 21.52 ? 327 THR A CG2 1 
ATOM   2543 N  N   . ALA A 1 328 ? -5.110  32.743 56.509  1.00 22.88 ? 328 ALA A N   1 
ATOM   2544 C  CA  . ALA A 1 328 ? -5.902  31.811 55.701  1.00 23.45 ? 328 ALA A CA  1 
ATOM   2545 C  C   . ALA A 1 328 ? -5.053  30.845 54.871  1.00 24.00 ? 328 ALA A C   1 
ATOM   2546 O  O   . ALA A 1 328 ? -5.348  29.646 54.821  1.00 24.20 ? 328 ALA A O   1 
ATOM   2547 C  CB  . ALA A 1 328 ? -6.873  32.567 54.810  1.00 23.33 ? 328 ALA A CB  1 
ATOM   2548 N  N   . ILE A 1 329 ? -4.016  31.369 54.218  1.00 24.39 ? 329 ILE A N   1 
ATOM   2549 C  CA  . ILE A 1 329 ? -3.061  30.539 53.493  1.00 24.83 ? 329 ILE A CA  1 
ATOM   2550 C  C   . ILE A 1 329 ? -2.446  29.494 54.432  1.00 25.54 ? 329 ILE A C   1 
ATOM   2551 O  O   . ILE A 1 329 ? -2.449  28.296 54.126  1.00 25.39 ? 329 ILE A O   1 
ATOM   2552 C  CB  . ILE A 1 329 ? -1.943  31.382 52.852  1.00 24.55 ? 329 ILE A CB  1 
ATOM   2553 C  CG1 . ILE A 1 329 ? -2.517  32.315 51.795  1.00 25.00 ? 329 ILE A CG1 1 
ATOM   2554 C  CG2 . ILE A 1 329 ? -0.931  30.497 52.181  1.00 24.85 ? 329 ILE A CG2 1 
ATOM   2555 C  CD1 . ILE A 1 329 ? -1.594  33.441 51.397  1.00 25.06 ? 329 ILE A CD1 1 
ATOM   2556 N  N   . GLN A 1 330 ? -1.928  29.942 55.574  1.00 26.39 ? 330 GLN A N   1 
ATOM   2557 C  CA  . GLN A 1 330 ? -1.275  29.026 56.514  1.00 27.52 ? 330 GLN A CA  1 
ATOM   2558 C  C   . GLN A 1 330 ? -2.239  27.944 56.940  1.00 28.19 ? 330 GLN A C   1 
ATOM   2559 O  O   . GLN A 1 330 ? -1.865  26.792 57.109  1.00 28.52 ? 330 GLN A O   1 
ATOM   2560 C  CB  . GLN A 1 330 ? -0.764  29.756 57.747  1.00 27.39 ? 330 GLN A CB  1 
ATOM   2561 C  CG  . GLN A 1 330 ? 0.328   30.766 57.474  1.00 27.62 ? 330 GLN A CG  1 
ATOM   2562 C  CD  . GLN A 1 330 ? 0.759   31.469 58.735  1.00 27.65 ? 330 GLN A CD  1 
ATOM   2563 O  OE1 . GLN A 1 330 ? 0.647   32.690 58.844  1.00 27.43 ? 330 GLN A OE1 1 
ATOM   2564 N  NE2 . GLN A 1 330 ? 1.232   30.696 59.715  1.00 27.65 ? 330 GLN A NE2 1 
ATOM   2565 N  N   . ASN A 1 331 ? -3.493  28.340 57.098  1.00 29.25 ? 331 ASN A N   1 
ATOM   2566 C  CA  . ASN A 1 331 ? -4.568  27.454 57.504  1.00 29.89 ? 331 ASN A CA  1 
ATOM   2567 C  C   . ASN A 1 331 ? -4.892  26.439 56.410  1.00 30.05 ? 331 ASN A C   1 
ATOM   2568 O  O   . ASN A 1 331 ? -5.298  25.326 56.690  1.00 30.09 ? 331 ASN A O   1 
ATOM   2569 C  CB  . ASN A 1 331 ? -5.794  28.303 57.819  1.00 29.96 ? 331 ASN A CB  1 
ATOM   2570 C  CG  . ASN A 1 331 ? -6.773  27.603 58.705  1.00 30.54 ? 331 ASN A CG  1 
ATOM   2571 O  OD1 . ASN A 1 331 ? -6.393  26.845 59.601  1.00 30.39 ? 331 ASN A OD1 1 
ATOM   2572 N  ND2 . ASN A 1 331 ? -8.058  27.867 58.476  1.00 31.44 ? 331 ASN A ND2 1 
ATOM   2573 N  N   . LEU A 1 332 ? -4.698  26.847 55.162  1.00 30.59 ? 332 LEU A N   1 
ATOM   2574 C  CA  . LEU A 1 332 ? -4.931  26.003 53.994  1.00 30.86 ? 332 LEU A CA  1 
ATOM   2575 C  C   . LEU A 1 332 ? -3.815  24.971 53.801  1.00 31.53 ? 332 LEU A C   1 
ATOM   2576 O  O   . LEU A 1 332 ? -3.984  24.020 53.034  1.00 31.91 ? 332 LEU A O   1 
ATOM   2577 C  CB  . LEU A 1 332 ? -5.060  26.890 52.745  1.00 30.71 ? 332 LEU A CB  1 
ATOM   2578 C  CG  . LEU A 1 332 ? -5.350  26.320 51.363  1.00 30.18 ? 332 LEU A CG  1 
ATOM   2579 C  CD1 . LEU A 1 332 ? -6.662  25.584 51.389  1.00 30.89 ? 332 LEU A CD1 1 
ATOM   2580 C  CD2 . LEU A 1 332 ? -5.408  27.427 50.347  1.00 30.17 ? 332 LEU A CD2 1 
ATOM   2581 N  N   . ARG A 1 333 ? -2.688  25.150 54.495  1.00 31.95 ? 333 ARG A N   1 
ATOM   2582 C  CA  . ARG A 1 333 ? -1.506  24.294 54.301  1.00 32.43 ? 333 ARG A CA  1 
ATOM   2583 C  C   . ARG A 1 333 ? -1.083  23.462 55.539  1.00 32.89 ? 333 ARG A C   1 
ATOM   2584 O  O   . ARG A 1 333 ? -0.164  22.639 55.437  1.00 33.13 ? 333 ARG A O   1 
ATOM   2585 C  CB  . ARG A 1 333 ? -0.319  25.120 53.781  1.00 32.53 ? 333 ARG A CB  1 
ATOM   2586 C  CG  . ARG A 1 333 ? -0.586  25.910 52.481  1.00 33.04 ? 333 ARG A CG  1 
ATOM   2587 C  CD  . ARG A 1 333 ? 0.712   26.403 51.820  1.00 32.35 ? 333 ARG A CD  1 
ATOM   2588 N  NE  . ARG A 1 333 ? 0.458   27.169 50.600  1.00 31.66 ? 333 ARG A NE  1 
ATOM   2589 C  CZ  . ARG A 1 333 ? 1.397   27.789 49.882  1.00 31.49 ? 333 ARG A CZ  1 
ATOM   2590 N  NH1 . ARG A 1 333 ? 2.673   27.739 50.239  1.00 30.70 ? 333 ARG A NH1 1 
ATOM   2591 N  NH2 . ARG A 1 333 ? 1.059   28.462 48.791  1.00 31.24 ? 333 ARG A NH2 1 
ATOM   2592 N  N   . ARG B 1 3   ? -26.606 34.371 76.622  1.00 37.92 ? 3   ARG B N   1 
ATOM   2593 C  CA  . ARG B 1 3   ? -25.475 33.578 77.205  1.00 37.72 ? 3   ARG B CA  1 
ATOM   2594 C  C   . ARG B 1 3   ? -25.865 32.105 77.384  1.00 37.29 ? 3   ARG B C   1 
ATOM   2595 O  O   . ARG B 1 3   ? -26.955 31.797 77.898  1.00 37.29 ? 3   ARG B O   1 
ATOM   2596 C  CB  . ARG B 1 3   ? -25.015 34.185 78.535  1.00 37.81 ? 3   ARG B CB  1 
ATOM   2597 C  CG  . ARG B 1 3   ? -24.033 35.349 78.394  1.00 38.36 ? 3   ARG B CG  1 
ATOM   2598 C  CD  . ARG B 1 3   ? -22.589 34.895 78.603  1.00 39.43 ? 3   ARG B CD  1 
ATOM   2599 N  NE  . ARG B 1 3   ? -22.297 34.547 80.000  1.00 40.05 ? 3   ARG B NE  1 
ATOM   2600 C  CZ  . ARG B 1 3   ? -21.418 33.619 80.387  1.00 40.48 ? 3   ARG B CZ  1 
ATOM   2601 N  NH1 . ARG B 1 3   ? -20.727 32.913 79.491  1.00 40.22 ? 3   ARG B NH1 1 
ATOM   2602 N  NH2 . ARG B 1 3   ? -21.237 33.384 81.683  1.00 40.40 ? 3   ARG B NH2 1 
ATOM   2603 N  N   . ARG B 1 4   ? -24.962 31.211 76.945  1.00 36.45 ? 4   ARG B N   1 
ATOM   2604 C  CA  . ARG B 1 4   ? -25.217 29.771 76.979  1.00 35.38 ? 4   ARG B CA  1 
ATOM   2605 C  C   . ARG B 1 4   ? -24.509 29.116 78.166  1.00 34.65 ? 4   ARG B C   1 
ATOM   2606 O  O   . ARG B 1 4   ? -23.720 29.763 78.859  1.00 34.49 ? 4   ARG B O   1 
ATOM   2607 C  CB  . ARG B 1 4   ? -24.808 29.115 75.636  1.00 35.58 ? 4   ARG B CB  1 
ATOM   2608 C  CG  . ARG B 1 4   ? -23.286 28.903 75.421  1.00 35.37 ? 4   ARG B CG  1 
ATOM   2609 C  CD  . ARG B 1 4   ? -22.665 29.908 74.430  1.00 35.84 ? 4   ARG B CD  1 
ATOM   2610 N  NE  . ARG B 1 4   ? -22.798 29.502 73.018  1.00 36.01 ? 4   ARG B NE  1 
ATOM   2611 C  CZ  . ARG B 1 4   ? -22.521 30.296 71.981  1.00 35.77 ? 4   ARG B CZ  1 
ATOM   2612 N  NH1 . ARG B 1 4   ? -22.099 31.540 72.181  1.00 36.14 ? 4   ARG B NH1 1 
ATOM   2613 N  NH2 . ARG B 1 4   ? -22.670 29.858 70.735  1.00 35.51 ? 4   ARG B NH2 1 
ATOM   2614 N  N   . ARG B 1 5   ? -24.791 27.831 78.386  1.00 33.84 ? 5   ARG B N   1 
ATOM   2615 C  CA  . ARG B 1 5   ? -24.234 27.078 79.518  1.00 33.11 ? 5   ARG B CA  1 
ATOM   2616 C  C   . ARG B 1 5   ? -22.842 26.443 79.287  1.00 32.30 ? 5   ARG B C   1 
ATOM   2617 O  O   . ARG B 1 5   ? -22.262 25.898 80.226  1.00 32.73 ? 5   ARG B O   1 
ATOM   2618 C  CB  . ARG B 1 5   ? -25.234 26.022 79.996  1.00 33.37 ? 5   ARG B CB  1 
ATOM   2619 C  CG  . ARG B 1 5   ? -26.569 26.590 80.491  1.00 34.34 ? 5   ARG B CG  1 
ATOM   2620 C  CD  . ARG B 1 5   ? -27.656 25.511 80.540  1.00 36.21 ? 5   ARG B CD  1 
ATOM   2621 N  NE  . ARG B 1 5   ? -27.780 24.801 79.260  1.00 38.44 ? 5   ARG B NE  1 
ATOM   2622 C  CZ  . ARG B 1 5   ? -28.680 23.852 78.997  1.00 39.12 ? 5   ARG B CZ  1 
ATOM   2623 N  NH1 . ARG B 1 5   ? -29.563 23.486 79.923  1.00 39.98 ? 5   ARG B NH1 1 
ATOM   2624 N  NH2 . ARG B 1 5   ? -28.704 23.268 77.802  1.00 38.88 ? 5   ARG B NH2 1 
ATOM   2625 N  N   . SER B 1 6   ? -22.315 26.527 78.059  1.00 31.05 ? 6   SER B N   1 
ATOM   2626 C  CA  . SER B 1 6   ? -20.946 26.096 77.708  1.00 29.41 ? 6   SER B CA  1 
ATOM   2627 C  C   . SER B 1 6   ? -19.882 27.090 78.202  1.00 28.37 ? 6   SER B C   1 
ATOM   2628 O  O   . SER B 1 6   ? -20.213 28.152 78.725  1.00 27.82 ? 6   SER B O   1 
ATOM   2629 C  CB  . SER B 1 6   ? -20.825 25.918 76.184  1.00 29.63 ? 6   SER B CB  1 
ATOM   2630 O  OG  . SER B 1 6   ? -20.344 27.095 75.523  1.00 29.70 ? 6   SER B OG  1 
ATOM   2631 N  N   . VAL B 1 7   ? -18.607 26.750 78.024  1.00 27.39 ? 7   VAL B N   1 
ATOM   2632 C  CA  . VAL B 1 7   ? -17.520 27.631 78.452  1.00 26.75 ? 7   VAL B CA  1 
ATOM   2633 C  C   . VAL B 1 7   ? -17.247 28.712 77.416  1.00 26.36 ? 7   VAL B C   1 
ATOM   2634 O  O   . VAL B 1 7   ? -17.038 28.410 76.243  1.00 26.79 ? 7   VAL B O   1 
ATOM   2635 C  CB  . VAL B 1 7   ? -16.215 26.865 78.755  1.00 26.75 ? 7   VAL B CB  1 
ATOM   2636 C  CG1 . VAL B 1 7   ? -15.061 27.845 78.975  1.00 26.73 ? 7   VAL B CG1 1 
ATOM   2637 C  CG2 . VAL B 1 7   ? -16.383 25.989 79.984  1.00 26.34 ? 7   VAL B CG2 1 
ATOM   2638 N  N   . GLN B 1 8   ? -17.243 29.969 77.850  1.00 25.59 ? 8   GLN B N   1 
ATOM   2639 C  CA  . GLN B 1 8   ? -17.040 31.079 76.931  1.00 24.82 ? 8   GLN B CA  1 
ATOM   2640 C  C   . GLN B 1 8   ? -15.725 31.808 77.197  1.00 24.28 ? 8   GLN B C   1 
ATOM   2641 O  O   . GLN B 1 8   ? -15.501 32.351 78.286  1.00 23.94 ? 8   GLN B O   1 
ATOM   2642 C  CB  . GLN B 1 8   ? -18.231 32.025 76.969  1.00 25.03 ? 8   GLN B CB  1 
ATOM   2643 C  CG  . GLN B 1 8   ? -19.469 31.456 76.322  1.00 25.45 ? 8   GLN B CG  1 
ATOM   2644 C  CD  . GLN B 1 8   ? -20.355 32.533 75.719  1.00 27.43 ? 8   GLN B CD  1 
ATOM   2645 O  OE1 . GLN B 1 8   ? -20.987 33.307 76.439  1.00 28.43 ? 8   GLN B OE1 1 
ATOM   2646 N  NE2 . GLN B 1 8   ? -20.409 32.586 74.390  1.00 27.54 ? 8   GLN B NE2 1 
ATOM   2647 N  N   . TRP B 1 9   ? -14.864 31.809 76.182  1.00 23.59 ? 9   TRP B N   1 
ATOM   2648 C  CA  . TRP B 1 9   ? -13.490 32.264 76.318  1.00 23.01 ? 9   TRP B CA  1 
ATOM   2649 C  C   . TRP B 1 9   ? -13.307 33.675 75.808  1.00 23.38 ? 9   TRP B C   1 
ATOM   2650 O  O   . TRP B 1 9   ? -13.956 34.096 74.856  1.00 23.69 ? 9   TRP B O   1 
ATOM   2651 C  CB  . TRP B 1 9   ? -12.546 31.340 75.571  1.00 22.07 ? 9   TRP B CB  1 
ATOM   2652 C  CG  . TRP B 1 9   ? -11.179 31.397 76.119  1.00 21.69 ? 9   TRP B CG  1 
ATOM   2653 C  CD1 . TRP B 1 9   ? -10.205 32.300 75.809  1.00 20.60 ? 9   TRP B CD1 1 
ATOM   2654 C  CD2 . TRP B 1 9   ? -10.617 30.521 77.101  1.00 21.58 ? 9   TRP B CD2 1 
ATOM   2655 N  NE1 . TRP B 1 9   ? -9.073  32.043 76.537  1.00 20.31 ? 9   TRP B NE1 1 
ATOM   2656 C  CE2 . TRP B 1 9   ? -9.296  30.952 77.334  1.00 21.19 ? 9   TRP B CE2 1 
ATOM   2657 C  CE3 . TRP B 1 9   ? -11.099 29.408 77.800  1.00 20.48 ? 9   TRP B CE3 1 
ATOM   2658 C  CZ2 . TRP B 1 9   ? -8.453  30.307 78.234  1.00 21.69 ? 9   TRP B CZ2 1 
ATOM   2659 C  CZ3 . TRP B 1 9   ? -10.270 28.780 78.696  1.00 20.23 ? 9   TRP B CZ3 1 
ATOM   2660 C  CH2 . TRP B 1 9   ? -8.964  29.226 78.908  1.00 21.37 ? 9   TRP B CH2 1 
ATOM   2661 N  N   . CYS B 1 10  ? -12.393 34.399 76.434  1.00 23.90 ? 10  CYS B N   1 
ATOM   2662 C  CA  . CYS B 1 10  ? -12.211 35.793 76.126  1.00 23.98 ? 10  CYS B CA  1 
ATOM   2663 C  C   . CYS B 1 10  ? -10.982 36.066 75.255  1.00 24.06 ? 10  CYS B C   1 
ATOM   2664 O  O   . CYS B 1 10  ? -9.862  35.704 75.617  1.00 24.04 ? 10  CYS B O   1 
ATOM   2665 C  CB  . CYS B 1 10  ? -12.155 36.580 77.417  1.00 24.07 ? 10  CYS B CB  1 
ATOM   2666 S  SG  . CYS B 1 10  ? -12.747 38.238 77.199  1.00 25.26 ? 10  CYS B SG  1 
ATOM   2667 N  N   . ALA B 1 11  ? -11.210 36.693 74.098  1.00 24.15 ? 11  ALA B N   1 
ATOM   2668 C  CA  . ALA B 1 11  ? -10.136 37.067 73.169  1.00 24.15 ? 11  ALA B CA  1 
ATOM   2669 C  C   . ALA B 1 11  ? -9.830  38.562 73.242  1.00 24.30 ? 11  ALA B C   1 
ATOM   2670 O  O   . ALA B 1 11  ? -10.740 39.393 73.246  1.00 24.58 ? 11  ALA B O   1 
ATOM   2671 C  CB  . ALA B 1 11  ? -10.495 36.674 71.749  1.00 23.79 ? 11  ALA B CB  1 
ATOM   2672 N  N   . VAL B 1 12  ? -8.550  38.905 73.284  1.00 24.27 ? 12  VAL B N   1 
ATOM   2673 C  CA  . VAL B 1 12  ? -8.159  40.305 73.401  1.00 24.57 ? 12  VAL B CA  1 
ATOM   2674 C  C   . VAL B 1 12  ? -7.854  41.000 72.063  1.00 24.84 ? 12  VAL B C   1 
ATOM   2675 O  O   . VAL B 1 12  ? -7.446  42.161 72.064  1.00 25.02 ? 12  VAL B O   1 
ATOM   2676 C  CB  . VAL B 1 12  ? -6.978  40.512 74.422  1.00 24.72 ? 12  VAL B CB  1 
ATOM   2677 C  CG1 . VAL B 1 12  ? -7.333  39.933 75.802  1.00 24.69 ? 12  VAL B CG1 1 
ATOM   2678 C  CG2 . VAL B 1 12  ? -5.661  39.922 73.900  1.00 24.29 ? 12  VAL B CG2 1 
ATOM   2679 N  N   . SER B 1 13  ? -8.071  40.311 70.938  1.00 25.14 ? 13  SER B N   1 
ATOM   2680 C  CA  . SER B 1 13  ? -7.710  40.828 69.601  1.00 25.38 ? 13  SER B CA  1 
ATOM   2681 C  C   . SER B 1 13  ? -8.289  39.973 68.473  1.00 25.78 ? 13  SER B C   1 
ATOM   2682 O  O   . SER B 1 13  ? -8.541  38.787 68.673  1.00 26.23 ? 13  SER B O   1 
ATOM   2683 C  CB  . SER B 1 13  ? -6.183  40.879 69.439  1.00 25.36 ? 13  SER B CB  1 
ATOM   2684 O  OG  . SER B 1 13  ? -5.635  39.589 69.213  1.00 24.53 ? 13  SER B OG  1 
ATOM   2685 N  N   . GLN B 1 14  ? -8.466  40.558 67.284  1.00 25.96 ? 14  GLN B N   1 
ATOM   2686 C  CA  . GLN B 1 14  ? -9.010  39.810 66.142  1.00 26.20 ? 14  GLN B CA  1 
ATOM   2687 C  C   . GLN B 1 14  ? -8.268  38.486 65.830  1.00 25.87 ? 14  GLN B C   1 
ATOM   2688 O  O   . GLN B 1 14  ? -8.915  37.462 65.604  1.00 25.76 ? 14  GLN B O   1 
ATOM   2689 C  CB  . GLN B 1 14  ? -9.148  40.700 64.892  1.00 26.63 ? 14  GLN B CB  1 
ATOM   2690 C  CG  . GLN B 1 14  ? -9.369  39.946 63.551  1.00 28.36 ? 14  GLN B CG  1 
ATOM   2691 C  CD  . GLN B 1 14  ? -10.794 39.389 63.362  1.00 31.55 ? 14  GLN B CD  1 
ATOM   2692 O  OE1 . GLN B 1 14  ? -11.460 38.958 64.316  1.00 32.87 ? 14  GLN B OE1 1 
ATOM   2693 N  NE2 . GLN B 1 14  ? -11.256 39.378 62.109  1.00 32.44 ? 14  GLN B NE2 1 
ATOM   2694 N  N   . PRO B 1 15  ? -6.918  38.505 65.786  1.00 25.65 ? 15  PRO B N   1 
ATOM   2695 C  CA  . PRO B 1 15  ? -6.197  37.239 65.626  1.00 25.26 ? 15  PRO B CA  1 
ATOM   2696 C  C   . PRO B 1 15  ? -6.510  36.189 66.693  1.00 24.75 ? 15  PRO B C   1 
ATOM   2697 O  O   . PRO B 1 15  ? -6.612  35.003 66.365  1.00 24.88 ? 15  PRO B O   1 
ATOM   2698 C  CB  . PRO B 1 15  ? -4.725  37.666 65.689  1.00 25.26 ? 15  PRO B CB  1 
ATOM   2699 C  CG  . PRO B 1 15  ? -4.739  39.054 65.162  1.00 25.52 ? 15  PRO B CG  1 
ATOM   2700 C  CD  . PRO B 1 15  ? -5.978  39.644 65.792  1.00 25.78 ? 15  PRO B CD  1 
ATOM   2701 N  N   . GLU B 1 16  ? -6.661  36.611 67.946  1.00 24.01 ? 16  GLU B N   1 
ATOM   2702 C  CA  . GLU B 1 16  ? -7.037  35.679 69.003  1.00 23.29 ? 16  GLU B CA  1 
ATOM   2703 C  C   . GLU B 1 16  ? -8.400  35.096 68.700  1.00 22.67 ? 16  GLU B C   1 
ATOM   2704 O  O   . GLU B 1 16  ? -8.563  33.877 68.710  1.00 23.08 ? 16  GLU B O   1 
ATOM   2705 C  CB  . GLU B 1 16  ? -7.016  36.323 70.393  1.00 23.31 ? 16  GLU B CB  1 
ATOM   2706 C  CG  . GLU B 1 16  ? -5.634  36.350 71.027  1.00 24.28 ? 16  GLU B CG  1 
ATOM   2707 C  CD  . GLU B 1 16  ? -5.650  36.370 72.556  1.00 25.58 ? 16  GLU B CD  1 
ATOM   2708 O  OE1 . GLU B 1 16  ? -6.701  36.674 73.161  1.00 26.61 ? 16  GLU B OE1 1 
ATOM   2709 O  OE2 . GLU B 1 16  ? -4.595  36.083 73.159  1.00 26.32 ? 16  GLU B OE2 1 
ATOM   2710 N  N   . ALA B 1 17  ? -9.370  35.952 68.401  1.00 21.58 ? 17  ALA B N   1 
ATOM   2711 C  CA  . ALA B 1 17  ? -10.696 35.474 68.047  1.00 21.01 ? 17  ALA B CA  1 
ATOM   2712 C  C   . ALA B 1 17  ? -10.640 34.373 66.974  1.00 20.89 ? 17  ALA B C   1 
ATOM   2713 O  O   . ALA B 1 17  ? -11.342 33.365 67.083  1.00 20.97 ? 17  ALA B O   1 
ATOM   2714 C  CB  . ALA B 1 17  ? -11.563 36.613 67.596  1.00 20.85 ? 17  ALA B CB  1 
ATOM   2715 N  N   . THR B 1 18  ? -9.786  34.555 65.963  1.00 20.57 ? 18  THR B N   1 
ATOM   2716 C  CA  . THR B 1 18  ? -9.664  33.602 64.856  1.00 20.07 ? 18  THR B CA  1 
ATOM   2717 C  C   . THR B 1 18  ? -9.170  32.239 65.335  1.00 20.06 ? 18  THR B C   1 
ATOM   2718 O  O   . THR B 1 18  ? -9.670  31.203 64.891  1.00 19.88 ? 18  THR B O   1 
ATOM   2719 C  CB  . THR B 1 18  ? -8.751  34.141 63.718  1.00 19.92 ? 18  THR B CB  1 
ATOM   2720 O  OG1 . THR B 1 18  ? -9.318  35.337 63.174  1.00 19.92 ? 18  THR B OG1 1 
ATOM   2721 C  CG2 . THR B 1 18  ? -8.597  33.115 62.593  1.00 19.06 ? 18  THR B CG2 1 
ATOM   2722 N  N   . LYS B 1 19  ? -8.196  32.244 66.240  1.00 20.19 ? 19  LYS B N   1 
ATOM   2723 C  CA  . LYS B 1 19  ? -7.626  31.000 66.744  1.00 20.64 ? 19  LYS B CA  1 
ATOM   2724 C  C   . LYS B 1 19  ? -8.681  30.307 67.578  1.00 20.98 ? 19  LYS B C   1 
ATOM   2725 O  O   . LYS B 1 19  ? -8.801  29.081 67.590  1.00 21.22 ? 19  LYS B O   1 
ATOM   2726 C  CB  . LYS B 1 19  ? -6.379  31.254 67.597  1.00 20.34 ? 19  LYS B CB  1 
ATOM   2727 C  CG  . LYS B 1 19  ? -5.915  30.001 68.329  1.00 20.28 ? 19  LYS B CG  1 
ATOM   2728 C  CD  . LYS B 1 19  ? -4.528  30.137 68.892  1.00 20.55 ? 19  LYS B CD  1 
ATOM   2729 C  CE  . LYS B 1 19  ? -4.201  28.918 69.724  1.00 20.54 ? 19  LYS B CE  1 
ATOM   2730 N  NZ  . LYS B 1 19  ? -2.818  28.985 70.266  1.00 21.39 ? 19  LYS B NZ  1 
ATOM   2731 N  N   . CYS B 1 20  ? -9.455  31.131 68.260  1.00 21.50 ? 20  CYS B N   1 
ATOM   2732 C  CA  . CYS B 1 20  ? -10.428 30.672 69.201  1.00 21.30 ? 20  CYS B CA  1 
ATOM   2733 C  C   . CYS B 1 20  ? -11.645 30.078 68.481  1.00 20.87 ? 20  CYS B C   1 
ATOM   2734 O  O   . CYS B 1 20  ? -12.220 29.097 68.944  1.00 20.71 ? 20  CYS B O   1 
ATOM   2735 C  CB  . CYS B 1 20  ? -10.777 31.837 70.116  1.00 21.85 ? 20  CYS B CB  1 
ATOM   2736 S  SG  . CYS B 1 20  ? -11.813 31.387 71.466  1.00 23.35 ? 20  CYS B SG  1 
ATOM   2737 N  N   . PHE B 1 21  ? -12.013 30.652 67.335  1.00 20.45 ? 21  PHE B N   1 
ATOM   2738 C  CA  . PHE B 1 21  ? -13.002 30.029 66.446  1.00 19.96 ? 21  PHE B CA  1 
ATOM   2739 C  C   . PHE B 1 21  ? -12.532 28.651 65.996  1.00 20.04 ? 21  PHE B C   1 
ATOM   2740 O  O   . PHE B 1 21  ? -13.325 27.702 65.935  1.00 20.35 ? 21  PHE B O   1 
ATOM   2741 C  CB  . PHE B 1 21  ? -13.280 30.883 65.206  1.00 19.31 ? 21  PHE B CB  1 
ATOM   2742 C  CG  . PHE B 1 21  ? -13.975 32.193 65.494  1.00 18.89 ? 21  PHE B CG  1 
ATOM   2743 C  CD1 . PHE B 1 21  ? -14.874 32.318 66.547  1.00 18.23 ? 21  PHE B CD1 1 
ATOM   2744 C  CD2 . PHE B 1 21  ? -13.750 33.300 64.680  1.00 18.93 ? 21  PHE B CD2 1 
ATOM   2745 C  CE1 . PHE B 1 21  ? -15.512 33.526 66.806  1.00 17.31 ? 21  PHE B CE1 1 
ATOM   2746 C  CE2 . PHE B 1 21  ? -14.395 34.511 64.928  1.00 18.70 ? 21  PHE B CE2 1 
ATOM   2747 C  CZ  . PHE B 1 21  ? -15.276 34.618 65.997  1.00 18.02 ? 21  PHE B CZ  1 
ATOM   2748 N  N   . GLN B 1 22  ? -11.239 28.547 65.677  1.00 19.88 ? 22  GLN B N   1 
ATOM   2749 C  CA  . GLN B 1 22  ? -10.641 27.289 65.208  1.00 19.28 ? 22  GLN B CA  1 
ATOM   2750 C  C   . GLN B 1 22  ? -10.664 26.256 66.323  1.00 18.70 ? 22  GLN B C   1 
ATOM   2751 O  O   . GLN B 1 22  ? -10.881 25.060 66.084  1.00 18.33 ? 22  GLN B O   1 
ATOM   2752 C  CB  . GLN B 1 22  ? -9.212  27.518 64.722  1.00 19.16 ? 22  GLN B CB  1 
ATOM   2753 C  CG  . GLN B 1 22  ? -8.605  26.324 63.992  1.00 19.52 ? 22  GLN B CG  1 
ATOM   2754 C  CD  . GLN B 1 22  ? -7.208  26.601 63.435  1.00 19.74 ? 22  GLN B CD  1 
ATOM   2755 O  OE1 . GLN B 1 22  ? -6.465  27.464 63.930  1.00 19.08 ? 22  GLN B OE1 1 
ATOM   2756 N  NE2 . GLN B 1 22  ? -6.846  25.862 62.395  1.00 20.88 ? 22  GLN B NE2 1 
ATOM   2757 N  N   . TRP B 1 23  ? -10.450 26.732 67.543  1.00 18.15 ? 23  TRP B N   1 
ATOM   2758 C  CA  . TRP B 1 23  ? -10.512 25.872 68.705  1.00 18.00 ? 23  TRP B CA  1 
ATOM   2759 C  C   . TRP B 1 23  ? -11.929 25.294 68.848  1.00 18.31 ? 23  TRP B C   1 
ATOM   2760 O  O   . TRP B 1 23  ? -12.098 24.084 69.050  1.00 18.52 ? 23  TRP B O   1 
ATOM   2761 C  CB  . TRP B 1 23  ? -10.077 26.645 69.930  1.00 17.56 ? 23  TRP B CB  1 
ATOM   2762 C  CG  . TRP B 1 23  ? -9.969  25.855 71.181  1.00 17.30 ? 23  TRP B CG  1 
ATOM   2763 C  CD1 . TRP B 1 23  ? -9.942  24.493 71.311  1.00 16.83 ? 23  TRP B CD1 1 
ATOM   2764 C  CD2 . TRP B 1 23  ? -9.831  26.389 72.497  1.00 16.33 ? 23  TRP B CD2 1 
ATOM   2765 N  NE1 . TRP B 1 23  ? -9.817  24.149 72.634  1.00 16.36 ? 23  TRP B NE1 1 
ATOM   2766 C  CE2 . TRP B 1 23  ? -9.739  25.295 73.383  1.00 16.55 ? 23  TRP B CE2 1 
ATOM   2767 C  CE3 . TRP B 1 23  ? -9.784  27.689 73.014  1.00 15.87 ? 23  TRP B CE3 1 
ATOM   2768 C  CZ2 . TRP B 1 23  ? -9.606  25.461 74.766  1.00 17.25 ? 23  TRP B CZ2 1 
ATOM   2769 C  CZ3 . TRP B 1 23  ? -9.651  27.857 74.377  1.00 17.27 ? 23  TRP B CZ3 1 
ATOM   2770 C  CH2 . TRP B 1 23  ? -9.560  26.745 75.244  1.00 17.55 ? 23  TRP B CH2 1 
ATOM   2771 N  N   . GLN B 1 24  ? -12.937 26.148 68.687  1.00 18.15 ? 24  GLN B N   1 
ATOM   2772 C  CA  . GLN B 1 24  ? -14.330 25.714 68.674  1.00 18.12 ? 24  GLN B CA  1 
ATOM   2773 C  C   . GLN B 1 24  ? -14.663 24.673 67.579  1.00 18.49 ? 24  GLN B C   1 
ATOM   2774 O  O   . GLN B 1 24  ? -15.291 23.657 67.879  1.00 18.42 ? 24  GLN B O   1 
ATOM   2775 C  CB  . GLN B 1 24  ? -15.234 26.934 68.554  1.00 17.94 ? 24  GLN B CB  1 
ATOM   2776 C  CG  . GLN B 1 24  ? -16.715 26.658 68.543  1.00 17.75 ? 24  GLN B CG  1 
ATOM   2777 C  CD  . GLN B 1 24  ? -17.498 27.919 68.306  1.00 18.83 ? 24  GLN B CD  1 
ATOM   2778 O  OE1 . GLN B 1 24  ? -17.025 28.837 67.626  1.00 20.83 ? 24  GLN B OE1 1 
ATOM   2779 N  NE2 . GLN B 1 24  ? -18.696 27.990 68.869  1.00 18.63 ? 24  GLN B NE2 1 
ATOM   2780 N  N   . ARG B 1 25  ? -14.253 24.922 66.328  1.00 18.86 ? 25  ARG B N   1 
ATOM   2781 C  CA  . ARG B 1 25  ? -14.523 23.979 65.232  1.00 19.17 ? 25  ARG B CA  1 
ATOM   2782 C  C   . ARG B 1 25  ? -13.922 22.622 65.527  1.00 19.89 ? 25  ARG B C   1 
ATOM   2783 O  O   . ARG B 1 25  ? -14.543 21.594 65.252  1.00 20.61 ? 25  ARG B O   1 
ATOM   2784 C  CB  . ARG B 1 25  ? -14.001 24.482 63.887  1.00 19.02 ? 25  ARG B CB  1 
ATOM   2785 C  CG  . ARG B 1 25  ? -14.796 25.651 63.306  1.00 19.38 ? 25  ARG B CG  1 
ATOM   2786 C  CD  . ARG B 1 25  ? -14.440 25.945 61.857  1.00 18.73 ? 25  ARG B CD  1 
ATOM   2787 N  NE  . ARG B 1 25  ? -13.018 26.250 61.669  1.00 18.99 ? 25  ARG B NE  1 
ATOM   2788 C  CZ  . ARG B 1 25  ? -12.448 27.437 61.891  1.00 19.56 ? 25  ARG B CZ  1 
ATOM   2789 N  NH1 . ARG B 1 25  ? -13.160 28.468 62.331  1.00 20.32 ? 25  ARG B NH1 1 
ATOM   2790 N  NH2 . ARG B 1 25  ? -11.151 27.601 61.681  1.00 19.53 ? 25  ARG B NH2 1 
ATOM   2791 N  N   . ASN B 1 26  ? -12.726 22.615 66.111  1.00 20.36 ? 26  ASN B N   1 
ATOM   2792 C  CA  . ASN B 1 26  ? -12.016 21.365 66.368  1.00 20.45 ? 26  ASN B CA  1 
ATOM   2793 C  C   . ASN B 1 26  ? -12.535 20.559 67.555  1.00 20.63 ? 26  ASN B C   1 
ATOM   2794 O  O   . ASN B 1 26  ? -12.592 19.333 67.484  1.00 20.87 ? 26  ASN B O   1 
ATOM   2795 C  CB  . ASN B 1 26  ? -10.514 21.610 66.473  1.00 20.23 ? 26  ASN B CB  1 
ATOM   2796 C  CG  . ASN B 1 26  ? -9.881  21.833 65.122  1.00 20.01 ? 26  ASN B CG  1 
ATOM   2797 O  OD1 . ASN B 1 26  ? -9.786  20.923 64.299  1.00 18.72 ? 26  ASN B OD1 1 
ATOM   2798 N  ND2 . ASN B 1 26  ? -9.457  23.056 64.879  1.00 20.99 ? 26  ASN B ND2 1 
ATOM   2799 N  N   . MET B 1 27  ? -12.917 21.238 68.633  1.00 20.63 ? 27  MET B N   1 
ATOM   2800 C  CA  . MET B 1 27  ? -13.458 20.558 69.800  1.00 20.91 ? 27  MET B CA  1 
ATOM   2801 C  C   . MET B 1 27  ? -14.764 19.863 69.453  1.00 21.32 ? 27  MET B C   1 
ATOM   2802 O  O   . MET B 1 27  ? -15.066 18.791 69.966  1.00 21.38 ? 27  MET B O   1 
ATOM   2803 C  CB  . MET B 1 27  ? -13.692 21.540 70.939  1.00 20.85 ? 27  MET B CB  1 
ATOM   2804 C  CG  . MET B 1 27  ? -12.428 22.090 71.567  1.00 20.91 ? 27  MET B CG  1 
ATOM   2805 S  SD  . MET B 1 27  ? -11.339 20.854 72.308  1.00 22.48 ? 27  MET B SD  1 
ATOM   2806 C  CE  . MET B 1 27  ? -12.329 20.205 73.652  1.00 20.49 ? 27  MET B CE  1 
ATOM   2807 N  N   . ARG B 1 28  ? -15.527 20.487 68.565  1.00 22.02 ? 28  ARG B N   1 
ATOM   2808 C  CA  . ARG B 1 28  ? -16.794 19.944 68.102  1.00 22.60 ? 28  ARG B CA  1 
ATOM   2809 C  C   . ARG B 1 28  ? -16.557 18.753 67.165  1.00 22.78 ? 28  ARG B C   1 
ATOM   2810 O  O   . ARG B 1 28  ? -17.234 17.728 67.270  1.00 22.70 ? 28  ARG B O   1 
ATOM   2811 C  CB  . ARG B 1 28  ? -17.619 21.047 67.427  1.00 22.56 ? 28  ARG B CB  1 
ATOM   2812 C  CG  . ARG B 1 28  ? -18.949 20.571 66.912  1.00 24.15 ? 28  ARG B CG  1 
ATOM   2813 C  CD  . ARG B 1 28  ? -19.995 21.670 66.832  1.00 26.21 ? 28  ARG B CD  1 
ATOM   2814 N  NE  . ARG B 1 28  ? -21.274 21.081 66.443  1.00 27.33 ? 28  ARG B NE  1 
ATOM   2815 C  CZ  . ARG B 1 28  ? -21.863 21.252 65.263  1.00 28.52 ? 28  ARG B CZ  1 
ATOM   2816 N  NH1 . ARG B 1 28  ? -21.311 22.033 64.339  1.00 28.04 ? 28  ARG B NH1 1 
ATOM   2817 N  NH2 . ARG B 1 28  ? -23.024 20.650 65.016  1.00 29.18 ? 28  ARG B NH2 1 
ATOM   2818 N  N   . ARG B 1 29  ? -15.576 18.894 66.271  1.00 23.30 ? 29  ARG B N   1 
ATOM   2819 C  CA  . ARG B 1 29  ? -15.215 17.853 65.298  1.00 23.44 ? 29  ARG B CA  1 
ATOM   2820 C  C   . ARG B 1 29  ? -14.781 16.547 65.951  1.00 23.74 ? 29  ARG B C   1 
ATOM   2821 O  O   . ARG B 1 29  ? -14.936 15.489 65.345  1.00 23.88 ? 29  ARG B O   1 
ATOM   2822 C  CB  . ARG B 1 29  ? -14.119 18.359 64.356  1.00 23.46 ? 29  ARG B CB  1 
ATOM   2823 C  CG  . ARG B 1 29  ? -13.594 17.342 63.335  1.00 23.16 ? 29  ARG B CG  1 
ATOM   2824 C  CD  . ARG B 1 29  ? -12.400 17.893 62.539  1.00 23.37 ? 29  ARG B CD  1 
ATOM   2825 N  NE  . ARG B 1 29  ? -11.324 18.406 63.397  1.00 23.49 ? 29  ARG B NE  1 
ATOM   2826 C  CZ  . ARG B 1 29  ? -10.282 17.695 63.828  1.00 23.28 ? 29  ARG B CZ  1 
ATOM   2827 N  NH1 . ARG B 1 29  ? -10.147 16.421 63.486  1.00 23.25 ? 29  ARG B NH1 1 
ATOM   2828 N  NH2 . ARG B 1 29  ? -9.367  18.263 64.609  1.00 22.69 ? 29  ARG B NH2 1 
ATOM   2829 N  N   . VAL B 1 30  ? -14.245 16.626 67.173  1.00 24.13 ? 30  VAL B N   1 
ATOM   2830 C  CA  . VAL B 1 30  ? -13.759 15.438 67.904  1.00 24.53 ? 30  VAL B CA  1 
ATOM   2831 C  C   . VAL B 1 30  ? -14.563 15.099 69.170  1.00 24.92 ? 30  VAL B C   1 
ATOM   2832 O  O   . VAL B 1 30  ? -14.087 14.366 70.039  1.00 24.68 ? 30  VAL B O   1 
ATOM   2833 C  CB  . VAL B 1 30  ? -12.228 15.509 68.228  1.00 24.54 ? 30  VAL B CB  1 
ATOM   2834 C  CG1 . VAL B 1 30  ? -11.410 15.720 66.948  1.00 25.07 ? 30  VAL B CG1 1 
ATOM   2835 C  CG2 . VAL B 1 30  ? -11.913 16.584 69.267  1.00 24.03 ? 30  VAL B CG2 1 
ATOM   2836 N  N   . ARG B 1 31  ? -15.775 15.648 69.261  1.00 25.69 ? 31  ARG B N   1 
ATOM   2837 C  CA  . ARG B 1 31  ? -16.745 15.304 70.308  1.00 26.46 ? 31  ARG B CA  1 
ATOM   2838 C  C   . ARG B 1 31  ? -16.289 15.607 71.741  1.00 26.37 ? 31  ARG B C   1 
ATOM   2839 O  O   . ARG B 1 31  ? -16.687 14.915 72.686  1.00 26.33 ? 31  ARG B O   1 
ATOM   2840 C  CB  . ARG B 1 31  ? -17.166 13.829 70.190  1.00 26.83 ? 31  ARG B CB  1 
ATOM   2841 C  CG  . ARG B 1 31  ? -18.429 13.582 69.371  1.00 29.33 ? 31  ARG B CG  1 
ATOM   2842 C  CD  . ARG B 1 31  ? -18.158 13.111 67.938  1.00 33.07 ? 31  ARG B CD  1 
ATOM   2843 N  NE  . ARG B 1 31  ? -18.269 14.196 66.952  1.00 35.89 ? 31  ARG B NE  1 
ATOM   2844 C  CZ  . ARG B 1 31  ? -18.678 14.036 65.687  1.00 37.61 ? 31  ARG B CZ  1 
ATOM   2845 N  NH1 . ARG B 1 31  ? -19.040 12.832 65.237  1.00 37.85 ? 31  ARG B NH1 1 
ATOM   2846 N  NH2 . ARG B 1 31  ? -18.736 15.088 64.868  1.00 37.67 ? 31  ARG B NH2 1 
ATOM   2847 N  N   . GLY B 1 32  ? -15.458 16.636 71.896  1.00 26.32 ? 32  GLY B N   1 
ATOM   2848 C  CA  . GLY B 1 32  ? -15.012 17.086 73.219  1.00 26.32 ? 32  GLY B CA  1 
ATOM   2849 C  C   . GLY B 1 32  ? -15.878 18.221 73.745  1.00 26.32 ? 32  GLY B C   1 
ATOM   2850 O  O   . GLY B 1 32  ? -16.865 18.587 73.105  1.00 26.73 ? 32  GLY B O   1 
ATOM   2851 N  N   . PRO B 1 33  ? -15.522 18.789 74.913  1.00 26.00 ? 33  PRO B N   1 
ATOM   2852 C  CA  . PRO B 1 33  ? -16.273 19.901 75.509  1.00 25.72 ? 33  PRO B CA  1 
ATOM   2853 C  C   . PRO B 1 33  ? -16.276 21.121 74.600  1.00 25.66 ? 33  PRO B C   1 
ATOM   2854 O  O   . PRO B 1 33  ? -15.268 21.388 73.943  1.00 25.90 ? 33  PRO B O   1 
ATOM   2855 C  CB  . PRO B 1 33  ? -15.483 20.223 76.773  1.00 25.72 ? 33  PRO B CB  1 
ATOM   2856 C  CG  . PRO B 1 33  ? -14.706 18.996 77.057  1.00 26.05 ? 33  PRO B CG  1 
ATOM   2857 C  CD  . PRO B 1 33  ? -14.381 18.388 75.747  1.00 25.85 ? 33  PRO B CD  1 
ATOM   2858 N  N   . PRO B 1 34  ? -17.397 21.863 74.555  1.00 25.40 ? 34  PRO B N   1 
ATOM   2859 C  CA  . PRO B 1 34  ? -17.471 23.026 73.663  1.00 25.02 ? 34  PRO B CA  1 
ATOM   2860 C  C   . PRO B 1 34  ? -16.866 24.302 74.253  1.00 24.68 ? 34  PRO B C   1 
ATOM   2861 O  O   . PRO B 1 34  ? -16.982 24.548 75.461  1.00 24.63 ? 34  PRO B O   1 
ATOM   2862 C  CB  . PRO B 1 34  ? -18.975 23.200 73.435  1.00 24.71 ? 34  PRO B CB  1 
ATOM   2863 C  CG  . PRO B 1 34  ? -19.613 22.632 74.657  1.00 25.40 ? 34  PRO B CG  1 
ATOM   2864 C  CD  . PRO B 1 34  ? -18.647 21.664 75.312  1.00 25.43 ? 34  PRO B CD  1 
ATOM   2865 N  N   . VAL B 1 35  ? -16.225 25.090 73.389  1.00 24.35 ? 35  VAL B N   1 
ATOM   2866 C  CA  . VAL B 1 35  ? -15.750 26.430 73.722  1.00 24.29 ? 35  VAL B CA  1 
ATOM   2867 C  C   . VAL B 1 35  ? -16.228 27.437 72.665  1.00 24.64 ? 35  VAL B C   1 
ATOM   2868 O  O   . VAL B 1 35  ? -16.261 27.125 71.483  1.00 24.69 ? 35  VAL B O   1 
ATOM   2869 C  CB  . VAL B 1 35  ? -14.206 26.467 73.876  1.00 24.20 ? 35  VAL B CB  1 
ATOM   2870 C  CG1 . VAL B 1 35  ? -13.503 26.071 72.586  1.00 23.94 ? 35  VAL B CG1 1 
ATOM   2871 C  CG2 . VAL B 1 35  ? -13.733 27.832 74.345  1.00 23.89 ? 35  VAL B CG2 1 
ATOM   2872 N  N   . SER B 1 36  ? -16.629 28.630 73.093  1.00 24.91 ? 36  SER B N   1 
ATOM   2873 C  CA  . SER B 1 36  ? -16.975 29.700 72.154  1.00 25.21 ? 36  SER B CA  1 
ATOM   2874 C  C   . SER B 1 36  ? -16.214 30.942 72.569  1.00 25.52 ? 36  SER B C   1 
ATOM   2875 O  O   . SER B 1 36  ? -15.546 30.931 73.604  1.00 25.56 ? 36  SER B O   1 
ATOM   2876 C  CB  . SER B 1 36  ? -18.485 29.960 72.117  1.00 25.17 ? 36  SER B CB  1 
ATOM   2877 O  OG  . SER B 1 36  ? -19.005 30.207 73.412  1.00 25.33 ? 36  SER B OG  1 
ATOM   2878 N  N   . CYS B 1 37  ? -16.303 32.009 71.775  1.00 25.81 ? 37  CYS B N   1 
ATOM   2879 C  CA  . CYS B 1 37  ? -15.440 33.169 71.998  1.00 26.36 ? 37  CYS B CA  1 
ATOM   2880 C  C   . CYS B 1 37  ? -16.167 34.500 72.106  1.00 25.79 ? 37  CYS B C   1 
ATOM   2881 O  O   . CYS B 1 37  ? -17.139 34.760 71.404  1.00 25.67 ? 37  CYS B O   1 
ATOM   2882 C  CB  . CYS B 1 37  ? -14.313 33.209 70.953  1.00 26.53 ? 37  CYS B CB  1 
ATOM   2883 S  SG  . CYS B 1 37  ? -13.656 31.480 70.592  1.00 31.08 ? 37  CYS B SG  1 
ATOM   2884 N  N   . ILE B 1 38  ? -15.681 35.320 73.028  1.00 25.56 ? 38  ILE B N   1 
ATOM   2885 C  CA  . ILE B 1 38  ? -16.161 36.668 73.233  1.00 25.39 ? 38  ILE B CA  1 
ATOM   2886 C  C   . ILE B 1 38  ? -15.008 37.592 72.870  1.00 25.71 ? 38  ILE B C   1 
ATOM   2887 O  O   . ILE B 1 38  ? -13.866 37.332 73.251  1.00 25.87 ? 38  ILE B O   1 
ATOM   2888 C  CB  . ILE B 1 38  ? -16.587 36.871 74.705  1.00 25.23 ? 38  ILE B CB  1 
ATOM   2889 C  CG1 . ILE B 1 38  ? -17.674 35.862 75.092  1.00 24.73 ? 38  ILE B CG1 1 
ATOM   2890 C  CG2 . ILE B 1 38  ? -17.058 38.298 74.964  1.00 24.80 ? 38  ILE B CG2 1 
ATOM   2891 C  CD1 . ILE B 1 38  ? -18.952 35.966 74.290  1.00 22.94 ? 38  ILE B CD1 1 
ATOM   2892 N  N   . LYS B 1 39  ? -15.296 38.657 72.124  1.00 26.02 ? 39  LYS B N   1 
ATOM   2893 C  CA  . LYS B 1 39  ? -14.250 39.571 71.660  1.00 26.42 ? 39  LYS B CA  1 
ATOM   2894 C  C   . LYS B 1 39  ? -14.166 40.869 72.472  1.00 26.87 ? 39  LYS B C   1 
ATOM   2895 O  O   . LYS B 1 39  ? -15.149 41.597 72.621  1.00 26.64 ? 39  LYS B O   1 
ATOM   2896 C  CB  . LYS B 1 39  ? -14.408 39.880 70.166  1.00 26.48 ? 39  LYS B CB  1 
ATOM   2897 C  CG  . LYS B 1 39  ? -14.586 38.637 69.280  1.00 26.54 ? 39  LYS B CG  1 
ATOM   2898 C  CD  . LYS B 1 39  ? -14.568 38.977 67.784  1.00 26.12 ? 39  LYS B CD  1 
ATOM   2899 C  CE  . LYS B 1 39  ? -15.732 39.852 67.379  1.00 25.35 ? 39  LYS B CE  1 
ATOM   2900 N  NZ  . LYS B 1 39  ? -15.839 39.919 65.916  1.00 25.39 ? 39  LYS B NZ  1 
ATOM   2901 N  N   . ARG B 1 40  ? -12.970 41.136 72.993  1.00 27.41 ? 40  ARG B N   1 
ATOM   2902 C  CA  . ARG B 1 40  ? -12.666 42.365 73.712  1.00 27.99 ? 40  ARG B CA  1 
ATOM   2903 C  C   . ARG B 1 40  ? -11.319 42.908 73.233  1.00 29.04 ? 40  ARG B C   1 
ATOM   2904 O  O   . ARG B 1 40  ? -10.669 42.280 72.393  1.00 29.28 ? 40  ARG B O   1 
ATOM   2905 C  CB  . ARG B 1 40  ? -12.653 42.118 75.222  1.00 27.57 ? 40  ARG B CB  1 
ATOM   2906 C  CG  . ARG B 1 40  ? -14.015 41.785 75.828  1.00 26.32 ? 40  ARG B CG  1 
ATOM   2907 C  CD  . ARG B 1 40  ? -15.013 42.935 75.680  1.00 23.86 ? 40  ARG B CD  1 
ATOM   2908 N  NE  . ARG B 1 40  ? -16.261 42.671 76.390  1.00 22.44 ? 40  ARG B NE  1 
ATOM   2909 C  CZ  . ARG B 1 40  ? -17.325 42.072 75.858  1.00 21.86 ? 40  ARG B CZ  1 
ATOM   2910 N  NH1 . ARG B 1 40  ? -17.306 41.665 74.596  1.00 21.00 ? 40  ARG B NH1 1 
ATOM   2911 N  NH2 . ARG B 1 40  ? -18.413 41.872 76.594  1.00 21.85 ? 40  ARG B NH2 1 
ATOM   2912 N  N   . ASP B 1 41  ? -10.911 44.068 73.760  1.00 30.07 ? 41  ASP B N   1 
ATOM   2913 C  CA  . ASP B 1 41  ? -9.715  44.783 73.286  1.00 30.99 ? 41  ASP B CA  1 
ATOM   2914 C  C   . ASP B 1 41  ? -8.561  44.820 74.267  1.00 31.00 ? 41  ASP B C   1 
ATOM   2915 O  O   . ASP B 1 41  ? -7.453  45.216 73.895  1.00 31.35 ? 41  ASP B O   1 
ATOM   2916 C  CB  . ASP B 1 41  ? -10.055 46.228 72.926  1.00 31.58 ? 41  ASP B CB  1 
ATOM   2917 C  CG  . ASP B 1 41  ? -10.639 46.364 71.540  1.00 34.28 ? 41  ASP B CG  1 
ATOM   2918 O  OD1 . ASP B 1 41  ? -10.420 45.457 70.697  1.00 37.36 ? 41  ASP B OD1 1 
ATOM   2919 O  OD2 . ASP B 1 41  ? -11.315 47.391 71.290  1.00 36.83 ? 41  ASP B OD2 1 
ATOM   2920 N  N   . SER B 1 42  ? -8.818  44.451 75.517  1.00 30.76 ? 42  SER B N   1 
ATOM   2921 C  CA  . SER B 1 42  ? -7.794  44.519 76.554  1.00 30.65 ? 42  SER B CA  1 
ATOM   2922 C  C   . SER B 1 42  ? -8.061  43.506 77.657  1.00 30.26 ? 42  SER B C   1 
ATOM   2923 O  O   . SER B 1 42  ? -9.221  43.156 77.908  1.00 30.37 ? 42  SER B O   1 
ATOM   2924 C  CB  . SER B 1 42  ? -7.725  45.928 77.153  1.00 30.72 ? 42  SER B CB  1 
ATOM   2925 O  OG  . SER B 1 42  ? -9.019  46.396 77.508  1.00 31.53 ? 42  SER B OG  1 
ATOM   2926 N  N   . PRO B 1 43  ? -6.990  43.029 78.320  1.00 29.67 ? 43  PRO B N   1 
ATOM   2927 C  CA  . PRO B 1 43  ? -7.175  42.152 79.467  1.00 29.13 ? 43  PRO B CA  1 
ATOM   2928 C  C   . PRO B 1 43  ? -8.237  42.683 80.435  1.00 28.80 ? 43  PRO B C   1 
ATOM   2929 O  O   . PRO B 1 43  ? -9.076  41.909 80.890  1.00 28.66 ? 43  PRO B O   1 
ATOM   2930 C  CB  . PRO B 1 43  ? -5.789  42.115 80.130  1.00 29.13 ? 43  PRO B CB  1 
ATOM   2931 C  CG  . PRO B 1 43  ? -4.888  42.966 79.303  1.00 29.50 ? 43  PRO B CG  1 
ATOM   2932 C  CD  . PRO B 1 43  ? -5.566  43.252 78.011  1.00 29.65 ? 43  PRO B CD  1 
ATOM   2933 N  N   . ILE B 1 44  ? -8.213  43.988 80.720  1.00 28.48 ? 44  ILE B N   1 
ATOM   2934 C  CA  . ILE B 1 44  ? -9.182  44.604 81.629  1.00 28.18 ? 44  ILE B CA  1 
ATOM   2935 C  C   . ILE B 1 44  ? -10.600 44.336 81.165  1.00 27.93 ? 44  ILE B C   1 
ATOM   2936 O  O   . ILE B 1 44  ? -11.445 43.917 81.958  1.00 28.00 ? 44  ILE B O   1 
ATOM   2937 C  CB  . ILE B 1 44  ? -8.957  46.139 81.791  1.00 28.39 ? 44  ILE B CB  1 
ATOM   2938 C  CG1 . ILE B 1 44  ? -7.726  46.417 82.660  1.00 28.97 ? 44  ILE B CG1 1 
ATOM   2939 C  CG2 . ILE B 1 44  ? -10.191 46.836 82.395  1.00 28.07 ? 44  ILE B CG2 1 
ATOM   2940 C  CD1 . ILE B 1 44  ? -7.791  45.809 84.062  1.00 29.22 ? 44  ILE B CD1 1 
ATOM   2941 N  N   . GLN B 1 45  ? -10.851 44.565 79.877  1.00 27.49 ? 45  GLN B N   1 
ATOM   2942 C  CA  . GLN B 1 45  ? -12.182 44.364 79.308  1.00 27.14 ? 45  GLN B CA  1 
ATOM   2943 C  C   . GLN B 1 45  ? -12.603 42.901 79.399  1.00 26.30 ? 45  GLN B C   1 
ATOM   2944 O  O   . GLN B 1 45  ? -13.775 42.603 79.607  1.00 26.26 ? 45  GLN B O   1 
ATOM   2945 C  CB  . GLN B 1 45  ? -12.272 44.901 77.871  1.00 26.87 ? 45  GLN B CB  1 
ATOM   2946 C  CG  . GLN B 1 45  ? -12.631 46.371 77.809  1.00 27.19 ? 45  GLN B CG  1 
ATOM   2947 C  CD  . GLN B 1 45  ? -12.914 46.860 76.399  1.00 28.44 ? 45  GLN B CD  1 
ATOM   2948 O  OE1 . GLN B 1 45  ? -13.920 47.540 76.148  1.00 30.57 ? 45  GLN B OE1 1 
ATOM   2949 N  NE2 . GLN B 1 45  ? -12.026 46.525 75.467  1.00 30.26 ? 45  GLN B NE2 1 
ATOM   2950 N  N   . CYS B 1 46  ? -11.635 42.000 79.269  1.00 25.44 ? 46  CYS B N   1 
ATOM   2951 C  CA  . CYS B 1 46  ? -11.882 40.588 79.473  1.00 24.99 ? 46  CYS B CA  1 
ATOM   2952 C  C   . CYS B 1 46  ? -12.155 40.215 80.929  1.00 24.33 ? 46  CYS B C   1 
ATOM   2953 O  O   . CYS B 1 46  ? -12.969 39.333 81.184  1.00 24.27 ? 46  CYS B O   1 
ATOM   2954 C  CB  . CYS B 1 46  ? -10.729 39.772 78.916  1.00 25.00 ? 46  CYS B CB  1 
ATOM   2955 S  SG  . CYS B 1 46  ? -11.007 39.357 77.190  1.00 27.77 ? 46  CYS B SG  1 
ATOM   2956 N  N   . ILE B 1 47  ? -11.478 40.885 81.869  1.00 23.56 ? 47  ILE B N   1 
ATOM   2957 C  CA  . ILE B 1 47  ? -11.717 40.696 83.299  1.00 22.69 ? 47  ILE B CA  1 
ATOM   2958 C  C   . ILE B 1 47  ? -13.114 41.195 83.671  1.00 22.99 ? 47  ILE B C   1 
ATOM   2959 O  O   . ILE B 1 47  ? -13.857 40.496 84.370  1.00 23.35 ? 47  ILE B O   1 
ATOM   2960 C  CB  . ILE B 1 47  ? -10.626 41.360 84.202  1.00 22.69 ? 47  ILE B CB  1 
ATOM   2961 C  CG1 . ILE B 1 47  ? -9.241  40.756 83.928  1.00 22.65 ? 47  ILE B CG1 1 
ATOM   2962 C  CG2 . ILE B 1 47  ? -10.946 41.143 85.663  1.00 21.67 ? 47  ILE B CG2 1 
ATOM   2963 C  CD1 . ILE B 1 47  ? -8.046  41.567 84.439  1.00 21.85 ? 47  ILE B CD1 1 
ATOM   2964 N  N   . GLN B 1 48  ? -13.477 42.385 83.195  1.00 22.75 ? 48  GLN B N   1 
ATOM   2965 C  CA  . GLN B 1 48  ? -14.817 42.938 83.416  1.00 22.69 ? 48  GLN B CA  1 
ATOM   2966 C  C   . GLN B 1 48  ? -15.911 42.072 82.800  1.00 22.52 ? 48  GLN B C   1 
ATOM   2967 O  O   . GLN B 1 48  ? -17.001 41.936 83.362  1.00 22.60 ? 48  GLN B O   1 
ATOM   2968 C  CB  . GLN B 1 48  ? -14.915 44.340 82.842  1.00 22.76 ? 48  GLN B CB  1 
ATOM   2969 C  CG  . GLN B 1 48  ? -13.990 45.335 83.507  1.00 24.31 ? 48  GLN B CG  1 
ATOM   2970 C  CD  . GLN B 1 48  ? -13.986 46.674 82.814  1.00 25.73 ? 48  GLN B CD  1 
ATOM   2971 O  OE1 . GLN B 1 48  ? -14.330 46.783 81.630  1.00 26.18 ? 48  GLN B OE1 1 
ATOM   2972 N  NE2 . GLN B 1 48  ? -13.592 47.708 83.546  1.00 26.23 ? 48  GLN B NE2 1 
ATOM   2973 N  N   . ALA B 1 49  ? -15.612 41.491 81.642  1.00 22.18 ? 49  ALA B N   1 
ATOM   2974 C  CA  . ALA B 1 49  ? -16.552 40.634 80.952  1.00 21.87 ? 49  ALA B CA  1 
ATOM   2975 C  C   . ALA B 1 49  ? -16.830 39.401 81.779  1.00 21.94 ? 49  ALA B C   1 
ATOM   2976 O  O   . ALA B 1 49  ? -17.992 39.025 81.943  1.00 22.34 ? 49  ALA B O   1 
ATOM   2977 C  CB  . ALA B 1 49  ? -16.027 40.250 79.593  1.00 21.98 ? 49  ALA B CB  1 
ATOM   2978 N  N   . ILE B 1 50  ? -15.782 38.779 82.316  1.00 21.78 ? 50  ILE B N   1 
ATOM   2979 C  CA  . ILE B 1 50  ? -15.971 37.595 83.157  1.00 21.99 ? 50  ILE B CA  1 
ATOM   2980 C  C   . ILE B 1 50  ? -16.671 37.946 84.483  1.00 22.46 ? 50  ILE B C   1 
ATOM   2981 O  O   . ILE B 1 50  ? -17.584 37.231 84.922  1.00 22.33 ? 50  ILE B O   1 
ATOM   2982 C  CB  . ILE B 1 50  ? -14.664 36.829 83.400  1.00 21.67 ? 50  ILE B CB  1 
ATOM   2983 C  CG1 . ILE B 1 50  ? -14.134 36.260 82.089  1.00 21.18 ? 50  ILE B CG1 1 
ATOM   2984 C  CG2 . ILE B 1 50  ? -14.897 35.675 84.365  1.00 22.19 ? 50  ILE B CG2 1 
ATOM   2985 C  CD1 . ILE B 1 50  ? -12.666 35.918 82.121  1.00 20.40 ? 50  ILE B CD1 1 
ATOM   2986 N  N   . ALA B 1 51  ? -16.258 39.059 85.094  1.00 22.84 ? 51  ALA B N   1 
ATOM   2987 C  CA  . ALA B 1 51  ? -16.898 39.572 86.305  1.00 23.15 ? 51  ALA B CA  1 
ATOM   2988 C  C   . ALA B 1 51  ? -18.392 39.776 86.102  1.00 23.61 ? 51  ALA B C   1 
ATOM   2989 O  O   . ALA B 1 51  ? -19.193 39.417 86.964  1.00 23.63 ? 51  ALA B O   1 
ATOM   2990 C  CB  . ALA B 1 51  ? -16.259 40.867 86.733  1.00 22.99 ? 51  ALA B CB  1 
ATOM   2991 N  N   . GLU B 1 52  ? -18.758 40.340 84.952  1.00 24.14 ? 52  GLU B N   1 
ATOM   2992 C  CA  . GLU B 1 52  ? -20.142 40.727 84.691  1.00 24.67 ? 52  GLU B CA  1 
ATOM   2993 C  C   . GLU B 1 52  ? -20.969 39.642 83.990  1.00 24.54 ? 52  GLU B C   1 
ATOM   2994 O  O   . GLU B 1 52  ? -22.090 39.884 83.558  1.00 24.45 ? 52  GLU B O   1 
ATOM   2995 C  CB  . GLU B 1 52  ? -20.188 42.062 83.947  1.00 24.78 ? 52  GLU B CB  1 
ATOM   2996 C  CG  . GLU B 1 52  ? -19.979 43.255 84.872  1.00 26.71 ? 52  GLU B CG  1 
ATOM   2997 C  CD  . GLU B 1 52  ? -19.359 44.456 84.166  1.00 29.59 ? 52  GLU B CD  1 
ATOM   2998 O  OE1 . GLU B 1 52  ? -19.666 44.665 82.967  1.00 30.71 ? 52  GLU B OE1 1 
ATOM   2999 O  OE2 . GLU B 1 52  ? -18.564 45.191 84.810  1.00 30.34 ? 52  GLU B OE2 1 
ATOM   3000 N  N   . ASN B 1 53  ? -20.411 38.441 83.917  1.00 24.60 ? 53  ASN B N   1 
ATOM   3001 C  CA  . ASN B 1 53  ? -21.094 37.278 83.362  1.00 24.55 ? 53  ASN B CA  1 
ATOM   3002 C  C   . ASN B 1 53  ? -21.382 37.413 81.870  1.00 24.14 ? 53  ASN B C   1 
ATOM   3003 O  O   . ASN B 1 53  ? -22.481 37.099 81.389  1.00 24.11 ? 53  ASN B O   1 
ATOM   3004 C  CB  . ASN B 1 53  ? -22.356 36.926 84.166  1.00 24.83 ? 53  ASN B CB  1 
ATOM   3005 C  CG  . ASN B 1 53  ? -22.585 35.417 84.256  1.00 26.47 ? 53  ASN B CG  1 
ATOM   3006 O  OD1 . ASN B 1 53  ? -23.159 34.796 83.351  1.00 27.25 ? 53  ASN B OD1 1 
ATOM   3007 N  ND2 . ASN B 1 53  ? -22.125 34.820 85.354  1.00 28.06 ? 53  ASN B ND2 1 
ATOM   3008 N  N   . ARG B 1 54  ? -20.378 37.893 81.144  1.00 23.65 ? 54  ARG B N   1 
ATOM   3009 C  CA  . ARG B 1 54  ? -20.427 37.914 79.689  1.00 23.20 ? 54  ARG B CA  1 
ATOM   3010 C  C   . ARG B 1 54  ? -19.455 36.892 79.133  1.00 22.49 ? 54  ARG B C   1 
ATOM   3011 O  O   . ARG B 1 54  ? -19.596 36.466 77.996  1.00 22.53 ? 54  ARG B O   1 
ATOM   3012 C  CB  . ARG B 1 54  ? -20.108 39.303 79.125  1.00 23.43 ? 54  ARG B CB  1 
ATOM   3013 C  CG  . ARG B 1 54  ? -20.867 40.469 79.751  1.00 24.54 ? 54  ARG B CG  1 
ATOM   3014 C  CD  . ARG B 1 54  ? -22.343 40.499 79.387  1.00 26.63 ? 54  ARG B CD  1 
ATOM   3015 N  NE  . ARG B 1 54  ? -22.945 41.811 79.648  1.00 29.14 ? 54  ARG B NE  1 
ATOM   3016 C  CZ  . ARG B 1 54  ? -23.344 42.252 80.844  1.00 30.42 ? 54  ARG B CZ  1 
ATOM   3017 N  NH1 . ARG B 1 54  ? -23.203 41.501 81.928  1.00 30.38 ? 54  ARG B NH1 1 
ATOM   3018 N  NH2 . ARG B 1 54  ? -23.883 43.463 80.962  1.00 30.93 ? 54  ARG B NH2 1 
ATOM   3019 N  N   . ALA B 1 55  ? -18.467 36.516 79.942  1.00 21.80 ? 55  ALA B N   1 
ATOM   3020 C  CA  . ALA B 1 55  ? -17.500 35.482 79.590  1.00 21.28 ? 55  ALA B CA  1 
ATOM   3021 C  C   . ALA B 1 55  ? -17.165 34.675 80.833  1.00 21.15 ? 55  ALA B C   1 
ATOM   3022 O  O   . ALA B 1 55  ? -17.579 35.027 81.932  1.00 21.03 ? 55  ALA B O   1 
ATOM   3023 C  CB  . ALA B 1 55  ? -16.251 36.098 79.008  1.00 21.18 ? 55  ALA B CB  1 
ATOM   3024 N  N   . ASP B 1 56  ? -16.408 33.597 80.660  1.00 21.12 ? 56  ASP B N   1 
ATOM   3025 C  CA  . ASP B 1 56  ? -16.080 32.710 81.774  1.00 21.06 ? 56  ASP B CA  1 
ATOM   3026 C  C   . ASP B 1 56  ? -14.583 32.584 82.035  1.00 20.94 ? 56  ASP B C   1 
ATOM   3027 O  O   . ASP B 1 56  ? -14.172 32.399 83.171  1.00 20.87 ? 56  ASP B O   1 
ATOM   3028 C  CB  . ASP B 1 56  ? -16.669 31.316 81.539  1.00 21.23 ? 56  ASP B CB  1 
ATOM   3029 C  CG  . ASP B 1 56  ? -18.173 31.340 81.304  1.00 22.05 ? 56  ASP B CG  1 
ATOM   3030 O  OD1 . ASP B 1 56  ? -18.920 31.727 82.239  1.00 22.64 ? 56  ASP B OD1 1 
ATOM   3031 O  OD2 . ASP B 1 56  ? -18.605 30.953 80.188  1.00 21.73 ? 56  ASP B OD2 1 
ATOM   3032 N  N   . ALA B 1 57  ? -13.764 32.676 80.992  1.00 21.04 ? 57  ALA B N   1 
ATOM   3033 C  CA  . ALA B 1 57  ? -12.345 32.365 81.145  1.00 21.11 ? 57  ALA B CA  1 
ATOM   3034 C  C   . ALA B 1 57  ? -11.396 33.131 80.211  1.00 21.18 ? 57  ALA B C   1 
ATOM   3035 O  O   . ALA B 1 57  ? -11.762 33.477 79.084  1.00 20.98 ? 57  ALA B O   1 
ATOM   3036 C  CB  . ALA B 1 57  ? -12.129 30.860 81.026  1.00 21.08 ? 57  ALA B CB  1 
ATOM   3037 N  N   . VAL B 1 58  ? -10.182 33.389 80.719  1.00 21.22 ? 58  VAL B N   1 
ATOM   3038 C  CA  . VAL B 1 58  ? -9.090  34.047 79.989  1.00 21.07 ? 58  VAL B CA  1 
ATOM   3039 C  C   . VAL B 1 58  ? -7.736  33.805 80.696  1.00 21.29 ? 58  VAL B C   1 
ATOM   3040 O  O   . VAL B 1 58  ? -7.674  33.766 81.933  1.00 21.69 ? 58  VAL B O   1 
ATOM   3041 C  CB  . VAL B 1 58  ? -9.335  35.573 79.862  1.00 20.84 ? 58  VAL B CB  1 
ATOM   3042 C  CG1 . VAL B 1 58  ? -9.162  36.265 81.213  1.00 20.79 ? 58  VAL B CG1 1 
ATOM   3043 C  CG2 . VAL B 1 58  ? -8.400  36.183 78.843  1.00 20.71 ? 58  VAL B CG2 1 
ATOM   3044 N  N   . THR B 1 59  ? -6.666  33.647 79.914  1.00 21.04 ? 59  THR B N   1 
ATOM   3045 C  CA  . THR B 1 59  ? -5.303  33.574 80.449  1.00 20.81 ? 59  THR B CA  1 
ATOM   3046 C  C   . THR B 1 59  ? -4.684  34.973 80.625  1.00 21.05 ? 59  THR B C   1 
ATOM   3047 O  O   . THR B 1 59  ? -4.664  35.794 79.696  1.00 21.00 ? 59  THR B O   1 
ATOM   3048 C  CB  . THR B 1 59  ? -4.377  32.762 79.546  1.00 20.61 ? 59  THR B CB  1 
ATOM   3049 O  OG1 . THR B 1 59  ? -5.127  31.769 78.845  1.00 21.50 ? 59  THR B OG1 1 
ATOM   3050 C  CG2 . THR B 1 59  ? -3.317  32.089 80.359  1.00 20.34 ? 59  THR B CG2 1 
ATOM   3051 N  N   . LEU B 1 60  ? -4.167  35.224 81.825  1.00 20.99 ? 60  LEU B N   1 
ATOM   3052 C  CA  . LEU B 1 60  ? -3.625  36.524 82.186  1.00 20.57 ? 60  LEU B CA  1 
ATOM   3053 C  C   . LEU B 1 60  ? -2.236  36.364 82.740  1.00 20.77 ? 60  LEU B C   1 
ATOM   3054 O  O   . LEU B 1 60  ? -1.935  35.369 83.368  1.00 20.68 ? 60  LEU B O   1 
ATOM   3055 C  CB  . LEU B 1 60  ? -4.489  37.197 83.253  1.00 20.20 ? 60  LEU B CB  1 
ATOM   3056 C  CG  . LEU B 1 60  ? -5.921  37.567 82.886  1.00 19.36 ? 60  LEU B CG  1 
ATOM   3057 C  CD1 . LEU B 1 60  ? -6.686  37.918 84.149  1.00 17.66 ? 60  LEU B CD1 1 
ATOM   3058 C  CD2 . LEU B 1 60  ? -5.953  38.695 81.880  1.00 17.37 ? 60  LEU B CD2 1 
ATOM   3059 N  N   . ASP B 1 61  ? -1.401  37.366 82.495  1.00 21.33 ? 61  ASP B N   1 
ATOM   3060 C  CA  . ASP B 1 61  ? -0.111  37.490 83.129  1.00 21.77 ? 61  ASP B CA  1 
ATOM   3061 C  C   . ASP B 1 61  ? -0.319  37.790 84.614  1.00 21.87 ? 61  ASP B C   1 
ATOM   3062 O  O   . ASP B 1 61  ? -1.388  38.275 85.016  1.00 21.94 ? 61  ASP B O   1 
ATOM   3063 C  CB  . ASP B 1 61  ? 0.673   38.613 82.452  1.00 22.11 ? 61  ASP B CB  1 
ATOM   3064 C  CG  . ASP B 1 61  ? 1.947   38.961 83.190  1.00 24.07 ? 61  ASP B CG  1 
ATOM   3065 O  OD1 . ASP B 1 61  ? 2.975   38.263 83.005  1.00 25.43 ? 61  ASP B OD1 1 
ATOM   3066 O  OD2 . ASP B 1 61  ? 1.908   39.933 83.977  1.00 26.87 ? 61  ASP B OD2 1 
ATOM   3067 N  N   . GLY B 1 62  ? 0.699   37.509 85.425  1.00 21.94 ? 62  GLY B N   1 
ATOM   3068 C  CA  . GLY B 1 62  ? 0.615   37.707 86.874  1.00 22.36 ? 62  GLY B CA  1 
ATOM   3069 C  C   . GLY B 1 62  ? 0.194   39.113 87.280  1.00 22.57 ? 62  GLY B C   1 
ATOM   3070 O  O   . GLY B 1 62  ? -0.503  39.299 88.285  1.00 22.38 ? 62  GLY B O   1 
ATOM   3071 N  N   . GLY B 1 63  ? 0.618   40.101 86.493  1.00 22.59 ? 63  GLY B N   1 
ATOM   3072 C  CA  . GLY B 1 63  ? 0.278   41.492 86.751  1.00 22.99 ? 63  GLY B CA  1 
ATOM   3073 C  C   . GLY B 1 63  ? -1.218  41.720 86.685  1.00 23.31 ? 63  GLY B C   1 
ATOM   3074 O  O   . GLY B 1 63  ? -1.780  42.474 87.489  1.00 23.36 ? 63  GLY B O   1 
ATOM   3075 N  N   . PHE B 1 64  ? -1.867  41.051 85.730  1.00 23.48 ? 64  PHE B N   1 
ATOM   3076 C  CA  . PHE B 1 64  ? -3.320  41.155 85.566  1.00 23.06 ? 64  PHE B CA  1 
ATOM   3077 C  C   . PHE B 1 64  ? -4.122  40.163 86.402  1.00 22.52 ? 64  PHE B C   1 
ATOM   3078 O  O   . PHE B 1 64  ? -5.296  40.397 86.668  1.00 21.87 ? 64  PHE B O   1 
ATOM   3079 C  CB  . PHE B 1 64  ? -3.698  41.157 84.081  1.00 23.17 ? 64  PHE B CB  1 
ATOM   3080 C  CG  . PHE B 1 64  ? -3.362  42.445 83.418  1.00 23.70 ? 64  PHE B CG  1 
ATOM   3081 C  CD1 . PHE B 1 64  ? -2.110  42.646 82.862  1.00 24.92 ? 64  PHE B CD1 1 
ATOM   3082 C  CD2 . PHE B 1 64  ? -4.265  43.501 83.434  1.00 24.77 ? 64  PHE B CD2 1 
ATOM   3083 C  CE1 . PHE B 1 64  ? -1.772  43.875 82.284  1.00 25.47 ? 64  PHE B CE1 1 
ATOM   3084 C  CE2 . PHE B 1 64  ? -3.944  44.732 82.859  1.00 24.92 ? 64  PHE B CE2 1 
ATOM   3085 C  CZ  . PHE B 1 64  ? -2.697  44.921 82.287  1.00 24.73 ? 64  PHE B CZ  1 
ATOM   3086 N  N   . ILE B 1 65  ? -3.475  39.081 86.835  1.00 22.38 ? 65  ILE B N   1 
ATOM   3087 C  CA  . ILE B 1 65  ? -4.061  38.189 87.833  1.00 22.51 ? 65  ILE B CA  1 
ATOM   3088 C  C   . ILE B 1 65  ? -4.262  38.981 89.129  1.00 22.86 ? 65  ILE B C   1 
ATOM   3089 O  O   . ILE B 1 65  ? -5.327  38.896 89.757  1.00 23.18 ? 65  ILE B O   1 
ATOM   3090 C  CB  . ILE B 1 65  ? -3.193  36.932 88.093  1.00 22.44 ? 65  ILE B CB  1 
ATOM   3091 C  CG1 . ILE B 1 65  ? -3.138  36.035 86.855  1.00 22.01 ? 65  ILE B CG1 1 
ATOM   3092 C  CG2 . ILE B 1 65  ? -3.736  36.127 89.267  1.00 22.47 ? 65  ILE B CG2 1 
ATOM   3093 C  CD1 . ILE B 1 65  ? -2.065  34.971 86.926  1.00 20.45 ? 65  ILE B CD1 1 
ATOM   3094 N  N   . TYR B 1 66  ? -3.250  39.763 89.512  1.00 23.00 ? 66  TYR B N   1 
ATOM   3095 C  CA  . TYR B 1 66  ? -3.361  40.642 90.671  1.00 23.15 ? 66  TYR B CA  1 
ATOM   3096 C  C   . TYR B 1 66  ? -4.496  41.632 90.470  1.00 23.24 ? 66  TYR B C   1 
ATOM   3097 O  O   . TYR B 1 66  ? -5.309  41.836 91.357  1.00 24.02 ? 66  TYR B O   1 
ATOM   3098 C  CB  . TYR B 1 66  ? -2.056  41.390 90.956  1.00 23.06 ? 66  TYR B CB  1 
ATOM   3099 C  CG  . TYR B 1 66  ? -2.225  42.488 91.984  1.00 23.12 ? 66  TYR B CG  1 
ATOM   3100 C  CD1 . TYR B 1 66  ? -2.186  42.209 93.344  1.00 23.34 ? 66  TYR B CD1 1 
ATOM   3101 C  CD2 . TYR B 1 66  ? -2.452  43.803 91.594  1.00 23.63 ? 66  TYR B CD2 1 
ATOM   3102 C  CE1 . TYR B 1 66  ? -2.356  43.221 94.300  1.00 23.96 ? 66  TYR B CE1 1 
ATOM   3103 C  CE2 . TYR B 1 66  ? -2.627  44.822 92.537  1.00 23.89 ? 66  TYR B CE2 1 
ATOM   3104 C  CZ  . TYR B 1 66  ? -2.577  44.528 93.891  1.00 23.74 ? 66  TYR B CZ  1 
ATOM   3105 O  OH  . TYR B 1 66  ? -2.751  45.538 94.825  1.00 22.90 ? 66  TYR B OH  1 
ATOM   3106 N  N   . GLU B 1 67  ? -4.542  42.245 89.301  1.00 23.32 ? 67  GLU B N   1 
ATOM   3107 C  CA  . GLU B 1 67  ? -5.588  43.194 88.961  1.00 23.37 ? 67  GLU B CA  1 
ATOM   3108 C  C   . GLU B 1 67  ? -6.989  42.575 89.025  1.00 22.89 ? 67  GLU B C   1 
ATOM   3109 O  O   . GLU B 1 67  ? -7.924  43.201 89.536  1.00 22.98 ? 67  GLU B O   1 
ATOM   3110 C  CB  . GLU B 1 67  ? -5.324  43.743 87.562  1.00 23.76 ? 67  GLU B CB  1 
ATOM   3111 C  CG  . GLU B 1 67  ? -5.815  45.148 87.357  1.00 25.19 ? 67  GLU B CG  1 
ATOM   3112 C  CD  . GLU B 1 67  ? -4.974  46.153 88.095  1.00 26.73 ? 67  GLU B CD  1 
ATOM   3113 O  OE1 . GLU B 1 67  ? -3.759  46.253 87.800  1.00 26.63 ? 67  GLU B OE1 1 
ATOM   3114 O  OE2 . GLU B 1 67  ? -5.537  46.840 88.975  1.00 28.38 ? 67  GLU B OE2 1 
ATOM   3115 N  N   . ALA B 1 68  ? -7.113  41.348 88.518  1.00 22.44 ? 68  ALA B N   1 
ATOM   3116 C  CA  . ALA B 1 68  ? -8.390  40.641 88.424  1.00 22.23 ? 68  ALA B CA  1 
ATOM   3117 C  C   . ALA B 1 68  ? -8.853  40.093 89.758  1.00 22.47 ? 68  ALA B C   1 
ATOM   3118 O  O   . ALA B 1 68  ? -10.019 39.716 89.906  1.00 22.66 ? 68  ALA B O   1 
ATOM   3119 C  CB  . ALA B 1 68  ? -8.291  39.525 87.442  1.00 22.14 ? 68  ALA B CB  1 
ATOM   3120 N  N   . GLY B 1 69  ? -7.939  40.035 90.722  1.00 22.31 ? 69  GLY B N   1 
ATOM   3121 C  CA  . GLY B 1 69  ? -8.291  39.640 92.073  1.00 22.18 ? 69  GLY B CA  1 
ATOM   3122 C  C   . GLY B 1 69  ? -9.020  40.708 92.868  1.00 22.35 ? 69  GLY B C   1 
ATOM   3123 O  O   . GLY B 1 69  ? -9.731  40.385 93.822  1.00 22.59 ? 69  GLY B O   1 
ATOM   3124 N  N   . LEU B 1 70  ? -8.850  41.978 92.493  1.00 22.19 ? 70  LEU B N   1 
ATOM   3125 C  CA  . LEU B 1 70  ? -9.418  43.089 93.259  1.00 22.18 ? 70  LEU B CA  1 
ATOM   3126 C  C   . LEU B 1 70  ? -10.926 43.227 93.086  1.00 22.42 ? 70  LEU B C   1 
ATOM   3127 O  O   . LEU B 1 70  ? -11.515 42.614 92.200  1.00 22.59 ? 70  LEU B O   1 
ATOM   3128 C  CB  . LEU B 1 70  ? -8.749  44.397 92.867  1.00 21.99 ? 70  LEU B CB  1 
ATOM   3129 C  CG  . LEU B 1 70  ? -7.238  44.538 93.009  1.00 22.22 ? 70  LEU B CG  1 
ATOM   3130 C  CD1 . LEU B 1 70  ? -6.781  45.865 92.389  1.00 22.05 ? 70  LEU B CD1 1 
ATOM   3131 C  CD2 . LEU B 1 70  ? -6.800  44.435 94.461  1.00 22.13 ? 70  LEU B CD2 1 
ATOM   3132 N  N   . ALA B 1 71  ? -11.549 44.032 93.941  1.00 22.67 ? 71  ALA B N   1 
ATOM   3133 C  CA  . ALA B 1 71  ? -12.948 44.401 93.758  1.00 23.06 ? 71  ALA B CA  1 
ATOM   3134 C  C   . ALA B 1 71  ? -13.079 45.368 92.567  1.00 23.41 ? 71  ALA B C   1 
ATOM   3135 O  O   . ALA B 1 71  ? -12.158 46.144 92.298  1.00 23.24 ? 71  ALA B O   1 
ATOM   3136 C  CB  . ALA B 1 71  ? -13.498 45.021 95.023  1.00 22.85 ? 71  ALA B CB  1 
ATOM   3137 N  N   . PRO B 1 72  ? -14.219 45.324 91.841  1.00 23.82 ? 72  PRO B N   1 
ATOM   3138 C  CA  . PRO B 1 72  ? -15.384 44.467 92.084  1.00 23.96 ? 72  PRO B CA  1 
ATOM   3139 C  C   . PRO B 1 72  ? -15.331 43.172 91.271  1.00 24.01 ? 72  PRO B C   1 
ATOM   3140 O  O   . PRO B 1 72  ? -16.371 42.565 91.006  1.00 24.07 ? 72  PRO B O   1 
ATOM   3141 C  CB  . PRO B 1 72  ? -16.546 45.342 91.605  1.00 23.89 ? 72  PRO B CB  1 
ATOM   3142 C  CG  . PRO B 1 72  ? -15.939 46.158 90.462  1.00 23.82 ? 72  PRO B CG  1 
ATOM   3143 C  CD  . PRO B 1 72  ? -14.429 46.190 90.661  1.00 23.69 ? 72  PRO B CD  1 
ATOM   3144 N  N   . TYR B 1 73  ? -14.133 42.759 90.882  1.00 24.08 ? 73  TYR B N   1 
ATOM   3145 C  CA  . TYR B 1 73  ? -13.985 41.581 90.029  1.00 24.58 ? 73  TYR B CA  1 
ATOM   3146 C  C   . TYR B 1 73  ? -13.881 40.265 90.814  1.00 24.99 ? 73  TYR B C   1 
ATOM   3147 O  O   . TYR B 1 73  ? -14.700 39.362 90.616  1.00 25.18 ? 73  TYR B O   1 
ATOM   3148 C  CB  . TYR B 1 73  ? -12.803 41.750 89.078  1.00 24.35 ? 73  TYR B CB  1 
ATOM   3149 C  CG  . TYR B 1 73  ? -12.725 43.111 88.408  1.00 24.02 ? 73  TYR B CG  1 
ATOM   3150 C  CD1 . TYR B 1 73  ? -13.836 43.677 87.781  1.00 23.37 ? 73  TYR B CD1 1 
ATOM   3151 C  CD2 . TYR B 1 73  ? -11.525 43.817 88.378  1.00 23.74 ? 73  TYR B CD2 1 
ATOM   3152 C  CE1 . TYR B 1 73  ? -13.755 44.920 87.160  1.00 23.21 ? 73  TYR B CE1 1 
ATOM   3153 C  CE2 . TYR B 1 73  ? -11.434 45.058 87.756  1.00 23.37 ? 73  TYR B CE2 1 
ATOM   3154 C  CZ  . TYR B 1 73  ? -12.550 45.598 87.152  1.00 23.37 ? 73  TYR B CZ  1 
ATOM   3155 O  OH  . TYR B 1 73  ? -12.445 46.816 86.539  1.00 23.99 ? 73  TYR B OH  1 
ATOM   3156 N  N   . LYS B 1 74  ? -12.892 40.163 91.705  1.00 25.42 ? 74  LYS B N   1 
ATOM   3157 C  CA  . LYS B 1 74  ? -12.708 38.969 92.550  1.00 25.83 ? 74  LYS B CA  1 
ATOM   3158 C  C   . LYS B 1 74  ? -12.695 37.681 91.716  1.00 25.73 ? 74  LYS B C   1 
ATOM   3159 O  O   . LYS B 1 74  ? -13.517 36.778 91.887  1.00 25.68 ? 74  LYS B O   1 
ATOM   3160 C  CB  . LYS B 1 74  ? -13.759 38.917 93.669  1.00 26.01 ? 74  LYS B CB  1 
ATOM   3161 C  CG  . LYS B 1 74  ? -13.697 40.099 94.634  1.00 27.42 ? 74  LYS B CG  1 
ATOM   3162 C  CD  . LYS B 1 74  ? -12.297 40.219 95.243  1.00 29.69 ? 74  LYS B CD  1 
ATOM   3163 C  CE  . LYS B 1 74  ? -12.178 41.365 96.227  1.00 31.31 ? 74  LYS B CE  1 
ATOM   3164 N  NZ  . LYS B 1 74  ? -12.986 41.117 97.453  1.00 32.51 ? 74  LYS B NZ  1 
ATOM   3165 N  N   . LEU B 1 75  ? -11.763 37.644 90.774  1.00 25.64 ? 75  LEU B N   1 
ATOM   3166 C  CA  . LEU B 1 75  ? -11.576 36.492 89.923  1.00 25.36 ? 75  LEU B CA  1 
ATOM   3167 C  C   . LEU B 1 75  ? -10.423 35.706 90.508  1.00 25.27 ? 75  LEU B C   1 
ATOM   3168 O  O   . LEU B 1 75  ? -9.548  36.272 91.167  1.00 25.52 ? 75  LEU B O   1 
ATOM   3169 C  CB  . LEU B 1 75  ? -11.280 36.916 88.474  1.00 25.18 ? 75  LEU B CB  1 
ATOM   3170 C  CG  . LEU B 1 75  ? -12.317 37.748 87.696  1.00 25.35 ? 75  LEU B CG  1 
ATOM   3171 C  CD1 . LEU B 1 75  ? -12.003 37.738 86.203  1.00 24.36 ? 75  LEU B CD1 1 
ATOM   3172 C  CD2 . LEU B 1 75  ? -13.772 37.300 87.941  1.00 25.00 ? 75  LEU B CD2 1 
ATOM   3173 N  N   . ARG B 1 76  ? -10.423 34.402 90.291  1.00 24.92 ? 76  ARG B N   1 
ATOM   3174 C  CA  . ARG B 1 76  ? -9.352  33.585 90.805  1.00 24.92 ? 76  ARG B CA  1 
ATOM   3175 C  C   . ARG B 1 76  ? -8.751  32.780 89.673  1.00 24.59 ? 76  ARG B C   1 
ATOM   3176 O  O   . ARG B 1 76  ? -9.428  32.521 88.682  1.00 24.67 ? 76  ARG B O   1 
ATOM   3177 C  CB  . ARG B 1 76  ? -9.843  32.688 91.947  1.00 24.97 ? 76  ARG B CB  1 
ATOM   3178 C  CG  . ARG B 1 76  ? -10.888 31.639 91.587  1.00 25.24 ? 76  ARG B CG  1 
ATOM   3179 C  CD  . ARG B 1 76  ? -11.150 30.722 92.772  1.00 25.99 ? 76  ARG B CD  1 
ATOM   3180 N  NE  . ARG B 1 76  ? -9.956  29.954 93.117  1.00 28.91 ? 76  ARG B NE  1 
ATOM   3181 C  CZ  . ARG B 1 76  ? -9.656  28.755 92.622  1.00 30.19 ? 76  ARG B CZ  1 
ATOM   3182 N  NH1 . ARG B 1 76  ? -10.477 28.158 91.767  1.00 31.02 ? 76  ARG B NH1 1 
ATOM   3183 N  NH2 . ARG B 1 76  ? -8.532  28.148 92.989  1.00 31.04 ? 76  ARG B NH2 1 
ATOM   3184 N  N   . PRO B 1 77  ? -7.462  32.421 89.792  1.00 24.22 ? 77  PRO B N   1 
ATOM   3185 C  CA  . PRO B 1 77  ? -6.887  31.535 88.807  1.00 23.82 ? 77  PRO B CA  1 
ATOM   3186 C  C   . PRO B 1 77  ? -7.385  30.133 89.048  1.00 23.62 ? 77  PRO B C   1 
ATOM   3187 O  O   . PRO B 1 77  ? -7.587  29.743 90.203  1.00 23.44 ? 77  PRO B O   1 
ATOM   3188 C  CB  . PRO B 1 77  ? -5.389  31.633 89.078  1.00 23.71 ? 77  PRO B CB  1 
ATOM   3189 C  CG  . PRO B 1 77  ? -5.274  32.038 90.452  1.00 24.00 ? 77  PRO B CG  1 
ATOM   3190 C  CD  . PRO B 1 77  ? -6.481  32.826 90.811  1.00 24.16 ? 77  PRO B CD  1 
ATOM   3191 N  N   . VAL B 1 78  ? -7.596  29.398 87.958  1.00 23.57 ? 78  VAL B N   1 
ATOM   3192 C  CA  . VAL B 1 78  ? -8.131  28.035 88.013  1.00 23.51 ? 78  VAL B CA  1 
ATOM   3193 C  C   . VAL B 1 78  ? -7.159  27.014 87.416  1.00 23.80 ? 78  VAL B C   1 
ATOM   3194 O  O   . VAL B 1 78  ? -7.171  25.825 87.799  1.00 23.87 ? 78  VAL B O   1 
ATOM   3195 C  CB  . VAL B 1 78  ? -9.511  27.914 87.319  1.00 23.38 ? 78  VAL B CB  1 
ATOM   3196 C  CG1 . VAL B 1 78  ? -10.560 28.733 88.059  1.00 23.53 ? 78  VAL B CG1 1 
ATOM   3197 C  CG2 . VAL B 1 78  ? -9.429  28.336 85.878  1.00 22.71 ? 78  VAL B CG2 1 
ATOM   3198 N  N   . ALA B 1 79  ? -6.311  27.480 86.499  1.00 23.60 ? 79  ALA B N   1 
ATOM   3199 C  CA  . ALA B 1 79  ? -5.353  26.611 85.834  1.00 23.58 ? 79  ALA B CA  1 
ATOM   3200 C  C   . ALA B 1 79  ? -4.110  27.374 85.409  1.00 23.74 ? 79  ALA B C   1 
ATOM   3201 O  O   . ALA B 1 79  ? -4.189  28.370 84.706  1.00 23.69 ? 79  ALA B O   1 
ATOM   3202 C  CB  . ALA B 1 79  ? -5.997  25.928 84.650  1.00 23.37 ? 79  ALA B CB  1 
ATOM   3203 N  N   . ALA B 1 80  ? -2.959  26.896 85.855  1.00 24.40 ? 80  ALA B N   1 
ATOM   3204 C  CA  . ALA B 1 80  ? -1.684  27.500 85.495  1.00 25.30 ? 80  ALA B CA  1 
ATOM   3205 C  C   . ALA B 1 80  ? -1.152  26.949 84.170  1.00 26.12 ? 80  ALA B C   1 
ATOM   3206 O  O   . ALA B 1 80  ? -1.388  25.776 83.828  1.00 26.81 ? 80  ALA B O   1 
ATOM   3207 C  CB  . ALA B 1 80  ? -0.691  27.255 86.585  1.00 25.15 ? 80  ALA B CB  1 
ATOM   3208 N  N   . GLU B 1 81  ? -0.441  27.781 83.418  1.00 26.41 ? 81  GLU B N   1 
ATOM   3209 C  CA  . GLU B 1 81  ? 0.310   27.272 82.274  1.00 27.20 ? 81  GLU B CA  1 
ATOM   3210 C  C   . GLU B 1 81  ? 1.530   26.516 82.776  1.00 26.79 ? 81  GLU B C   1 
ATOM   3211 O  O   . GLU B 1 81  ? 2.158   26.901 83.765  1.00 26.80 ? 81  GLU B O   1 
ATOM   3212 C  CB  . GLU B 1 81  ? 0.742   28.399 81.331  1.00 27.23 ? 81  GLU B CB  1 
ATOM   3213 C  CG  . GLU B 1 81  ? -0.357  28.898 80.400  1.00 28.20 ? 81  GLU B CG  1 
ATOM   3214 C  CD  . GLU B 1 81  ? 0.100   30.008 79.445  1.00 29.20 ? 81  GLU B CD  1 
ATOM   3215 O  OE1 . GLU B 1 81  ? 1.108   30.718 79.726  1.00 31.90 ? 81  GLU B OE1 1 
ATOM   3216 O  OE2 . GLU B 1 81  ? -0.570  30.177 78.399  1.00 32.36 ? 81  GLU B OE2 1 
ATOM   3217 N  N   . VAL B 1 82  ? 1.847   25.428 82.096  1.00 26.66 ? 82  VAL B N   1 
ATOM   3218 C  CA  . VAL B 1 82  ? 3.019   24.651 82.404  1.00 26.75 ? 82  VAL B CA  1 
ATOM   3219 C  C   . VAL B 1 82  ? 4.029   24.933 81.305  1.00 27.44 ? 82  VAL B C   1 
ATOM   3220 O  O   . VAL B 1 82  ? 3.741   24.696 80.131  1.00 27.85 ? 82  VAL B O   1 
ATOM   3221 C  CB  . VAL B 1 82  ? 2.670   23.167 82.421  1.00 26.49 ? 82  VAL B CB  1 
ATOM   3222 C  CG1 . VAL B 1 82  ? 3.884   22.328 82.767  1.00 26.69 ? 82  VAL B CG1 1 
ATOM   3223 C  CG2 . VAL B 1 82  ? 1.551   22.911 83.401  1.00 26.54 ? 82  VAL B CG2 1 
ATOM   3224 N  N   . TYR B 1 83  ? 5.201   25.454 81.663  1.00 27.99 ? 83  TYR B N   1 
ATOM   3225 C  CA  . TYR B 1 83  ? 6.264   25.658 80.672  1.00 28.50 ? 83  TYR B CA  1 
ATOM   3226 C  C   . TYR B 1 83  ? 7.311   24.554 80.759  1.00 29.47 ? 83  TYR B C   1 
ATOM   3227 O  O   . TYR B 1 83  ? 7.162   23.608 81.538  1.00 29.48 ? 83  TYR B O   1 
ATOM   3228 C  CB  . TYR B 1 83  ? 6.931   27.019 80.840  1.00 27.94 ? 83  TYR B CB  1 
ATOM   3229 C  CG  . TYR B 1 83  ? 5.975   28.175 81.044  1.00 27.54 ? 83  TYR B CG  1 
ATOM   3230 C  CD1 . TYR B 1 83  ? 4.938   28.423 80.145  1.00 26.21 ? 83  TYR B CD1 1 
ATOM   3231 C  CD2 . TYR B 1 83  ? 6.132   29.041 82.125  1.00 27.06 ? 83  TYR B CD2 1 
ATOM   3232 C  CE1 . TYR B 1 83  ? 4.077   29.484 80.330  1.00 26.29 ? 83  TYR B CE1 1 
ATOM   3233 C  CE2 . TYR B 1 83  ? 5.281   30.107 82.312  1.00 26.74 ? 83  TYR B CE2 1 
ATOM   3234 C  CZ  . TYR B 1 83  ? 4.254   30.321 81.416  1.00 27.12 ? 83  TYR B CZ  1 
ATOM   3235 O  OH  . TYR B 1 83  ? 3.401   31.376 81.621  1.00 27.61 ? 83  TYR B OH  1 
ATOM   3236 N  N   . GLY B 1 84  ? 8.367   24.684 79.953  1.00 30.73 ? 84  GLY B N   1 
ATOM   3237 C  CA  . GLY B 1 84  ? 9.505   23.754 79.963  1.00 31.63 ? 84  GLY B CA  1 
ATOM   3238 C  C   . GLY B 1 84  ? 9.347   22.597 79.000  1.00 32.39 ? 84  GLY B C   1 
ATOM   3239 O  O   . GLY B 1 84  ? 9.004   22.790 77.838  1.00 32.39 ? 84  GLY B O   1 
ATOM   3240 N  N   . THR B 1 85  ? 9.596   21.387 79.487  1.00 33.30 ? 85  THR B N   1 
ATOM   3241 C  CA  . THR B 1 85  ? 9.483   20.187 78.660  1.00 34.46 ? 85  THR B CA  1 
ATOM   3242 C  C   . THR B 1 85  ? 8.704   19.100 79.378  1.00 34.95 ? 85  THR B C   1 
ATOM   3243 O  O   . THR B 1 85  ? 8.631   19.103 80.609  1.00 35.12 ? 85  THR B O   1 
ATOM   3244 C  CB  . THR B 1 85  ? 10.862  19.637 78.288  1.00 34.65 ? 85  THR B CB  1 
ATOM   3245 O  OG1 . THR B 1 85  ? 11.750  19.787 79.406  1.00 34.87 ? 85  THR B OG1 1 
ATOM   3246 C  CG2 . THR B 1 85  ? 11.422  20.387 77.077  1.00 35.36 ? 85  THR B CG2 1 
ATOM   3247 N  N   . GLU B 1 86  ? 8.136   18.166 78.615  1.00 35.53 ? 86  GLU B N   1 
ATOM   3248 C  CA  . GLU B 1 86  ? 7.304   17.111 79.199  1.00 36.23 ? 86  GLU B CA  1 
ATOM   3249 C  C   . GLU B 1 86  ? 8.006   16.403 80.377  1.00 36.08 ? 86  GLU B C   1 
ATOM   3250 O  O   . GLU B 1 86  ? 7.349   15.983 81.338  1.00 35.95 ? 86  GLU B O   1 
ATOM   3251 C  CB  . GLU B 1 86  ? 6.840   16.104 78.131  1.00 36.40 ? 86  GLU B CB  1 
ATOM   3252 C  CG  . GLU B 1 86  ? 5.682   15.188 78.586  1.00 38.13 ? 86  GLU B CG  1 
ATOM   3253 C  CD  . GLU B 1 86  ? 5.726   13.788 77.950  1.00 40.90 ? 86  GLU B CD  1 
ATOM   3254 O  OE1 . GLU B 1 86  ? 5.130   13.592 76.860  1.00 41.39 ? 86  GLU B OE1 1 
ATOM   3255 O  OE2 . GLU B 1 86  ? 6.350   12.875 78.554  1.00 41.78 ? 86  GLU B OE2 1 
ATOM   3256 N  N   . ARG B 1 87  ? 9.335   16.311 80.305  1.00 36.09 ? 87  ARG B N   1 
ATOM   3257 C  CA  . ARG B 1 87  ? 10.138  15.608 81.319  1.00 36.23 ? 87  ARG B CA  1 
ATOM   3258 C  C   . ARG B 1 87  ? 10.673  16.504 82.441  1.00 35.68 ? 87  ARG B C   1 
ATOM   3259 O  O   . ARG B 1 87  ? 10.902  16.036 83.555  1.00 35.63 ? 87  ARG B O   1 
ATOM   3260 C  CB  . ARG B 1 87  ? 11.274  14.800 80.667  1.00 36.54 ? 87  ARG B CB  1 
ATOM   3261 C  CG  . ARG B 1 87  ? 12.159  15.579 79.680  1.00 38.36 ? 87  ARG B CG  1 
ATOM   3262 C  CD  . ARG B 1 87  ? 12.471  14.746 78.412  1.00 41.18 ? 87  ARG B CD  1 
ATOM   3263 N  NE  . ARG B 1 87  ? 13.163  13.477 78.700  1.00 42.43 ? 87  ARG B NE  1 
ATOM   3264 C  CZ  . ARG B 1 87  ? 13.265  12.451 77.850  1.00 42.75 ? 87  ARG B CZ  1 
ATOM   3265 N  NH1 . ARG B 1 87  ? 12.718  12.516 76.640  1.00 43.13 ? 87  ARG B NH1 1 
ATOM   3266 N  NH2 . ARG B 1 87  ? 13.912  11.347 78.213  1.00 42.58 ? 87  ARG B NH2 1 
ATOM   3267 N  N   . GLN B 1 88  ? 10.863  17.785 82.144  1.00 34.99 ? 88  GLN B N   1 
ATOM   3268 C  CA  . GLN B 1 88  ? 11.277  18.762 83.143  1.00 34.27 ? 88  GLN B CA  1 
ATOM   3269 C  C   . GLN B 1 88  ? 10.322  19.977 83.065  1.00 33.61 ? 88  GLN B C   1 
ATOM   3270 O  O   . GLN B 1 88  ? 10.648  21.002 82.456  1.00 33.35 ? 88  GLN B O   1 
ATOM   3271 C  CB  . GLN B 1 88  ? 12.755  19.133 82.924  1.00 34.38 ? 88  GLN B CB  1 
ATOM   3272 C  CG  . GLN B 1 88  ? 13.408  20.005 84.013  1.00 35.56 ? 88  GLN B CG  1 
ATOM   3273 C  CD  . GLN B 1 88  ? 13.704  19.259 85.313  1.00 36.92 ? 88  GLN B CD  1 
ATOM   3274 O  OE1 . GLN B 1 88  ? 13.975  18.056 85.312  1.00 37.96 ? 88  GLN B OE1 1 
ATOM   3275 N  NE2 . GLN B 1 88  ? 13.666  19.981 86.429  1.00 36.69 ? 88  GLN B NE2 1 
ATOM   3276 N  N   . PRO B 1 89  ? 9.124   19.851 83.676  1.00 33.00 ? 89  PRO B N   1 
ATOM   3277 C  CA  . PRO B 1 89  ? 8.045   20.837 83.556  1.00 32.67 ? 89  PRO B CA  1 
ATOM   3278 C  C   . PRO B 1 89  ? 8.101   21.948 84.605  1.00 32.34 ? 89  PRO B C   1 
ATOM   3279 O  O   . PRO B 1 89  ? 8.450   21.694 85.756  1.00 32.27 ? 89  PRO B O   1 
ATOM   3280 C  CB  . PRO B 1 89  ? 6.779   19.993 83.750  1.00 32.65 ? 89  PRO B CB  1 
ATOM   3281 C  CG  . PRO B 1 89  ? 7.217   18.788 84.526  1.00 32.59 ? 89  PRO B CG  1 
ATOM   3282 C  CD  . PRO B 1 89  ? 8.727   18.731 84.547  1.00 32.97 ? 89  PRO B CD  1 
ATOM   3283 N  N   . ARG B 1 90  ? 7.743   23.165 84.203  1.00 31.85 ? 90  ARG B N   1 
ATOM   3284 C  CA  . ARG B 1 90  ? 7.867   24.340 85.065  1.00 31.85 ? 90  ARG B CA  1 
ATOM   3285 C  C   . ARG B 1 90  ? 6.545   25.088 85.213  1.00 30.16 ? 90  ARG B C   1 
ATOM   3286 O  O   . ARG B 1 90  ? 5.814   25.258 84.239  1.00 30.12 ? 90  ARG B O   1 
ATOM   3287 C  CB  . ARG B 1 90  ? 8.956   25.284 84.535  1.00 31.73 ? 90  ARG B CB  1 
ATOM   3288 C  CG  . ARG B 1 90  ? 10.354  24.643 84.426  1.00 34.21 ? 90  ARG B CG  1 
ATOM   3289 C  CD  . ARG B 1 90  ? 11.496  25.669 84.263  1.00 35.32 ? 90  ARG B CD  1 
ATOM   3290 N  NE  . ARG B 1 90  ? 11.654  26.536 85.441  1.00 42.37 ? 90  ARG B NE  1 
ATOM   3291 C  CZ  . ARG B 1 90  ? 11.473  27.864 85.454  1.00 44.44 ? 90  ARG B CZ  1 
ATOM   3292 N  NH1 . ARG B 1 90  ? 11.134  28.524 84.340  1.00 44.96 ? 90  ARG B NH1 1 
ATOM   3293 N  NH2 . ARG B 1 90  ? 11.644  28.539 86.592  1.00 45.29 ? 90  ARG B NH2 1 
ATOM   3294 N  N   . THR B 1 91  ? 6.243   25.518 86.436  1.00 28.66 ? 91  THR B N   1 
ATOM   3295 C  CA  . THR B 1 91  ? 5.052   26.324 86.720  1.00 27.37 ? 91  THR B CA  1 
ATOM   3296 C  C   . THR B 1 91  ? 5.441   27.738 87.144  1.00 26.39 ? 91  THR B C   1 
ATOM   3297 O  O   . THR B 1 91  ? 4.590   28.549 87.509  1.00 26.31 ? 91  THR B O   1 
ATOM   3298 C  CB  . THR B 1 91  ? 4.152   25.688 87.808  1.00 27.41 ? 91  THR B CB  1 
ATOM   3299 O  OG1 . THR B 1 91  ? 4.956   25.240 88.906  1.00 27.30 ? 91  THR B OG1 1 
ATOM   3300 C  CG2 . THR B 1 91  ? 3.378   24.511 87.244  1.00 27.33 ? 91  THR B CG2 1 
ATOM   3301 N  N   . HIS B 1 92  ? 6.739   28.014 87.098  1.00 25.07 ? 92  HIS B N   1 
ATOM   3302 C  CA  . HIS B 1 92  ? 7.279   29.320 87.437  1.00 23.90 ? 92  HIS B CA  1 
ATOM   3303 C  C   . HIS B 1 92  ? 8.097   29.778 86.238  1.00 23.19 ? 92  HIS B C   1 
ATOM   3304 O  O   . HIS B 1 92  ? 8.374   28.979 85.329  1.00 23.31 ? 92  HIS B O   1 
ATOM   3305 C  CB  . HIS B 1 92  ? 8.177   29.237 88.683  1.00 23.90 ? 92  HIS B CB  1 
ATOM   3306 C  CG  . HIS B 1 92  ? 7.468   28.818 89.943  1.00 23.66 ? 92  HIS B CG  1 
ATOM   3307 N  ND1 . HIS B 1 92  ? 6.874   27.584 90.100  1.00 23.07 ? 92  HIS B ND1 1 
ATOM   3308 C  CD2 . HIS B 1 92  ? 7.311   29.457 91.128  1.00 24.64 ? 92  HIS B CD2 1 
ATOM   3309 C  CE1 . HIS B 1 92  ? 6.355   27.495 91.313  1.00 24.48 ? 92  HIS B CE1 1 
ATOM   3310 N  NE2 . HIS B 1 92  ? 6.608   28.618 91.962  1.00 24.43 ? 92  HIS B NE2 1 
ATOM   3311 N  N   . TYR B 1 93  ? 8.459   31.058 86.213  1.00 22.00 ? 93  TYR B N   1 
ATOM   3312 C  CA  . TYR B 1 93  ? 9.411   31.565 85.227  1.00 21.22 ? 93  TYR B CA  1 
ATOM   3313 C  C   . TYR B 1 93  ? 10.236  32.698 85.806  1.00 21.16 ? 93  TYR B C   1 
ATOM   3314 O  O   . TYR B 1 93  ? 9.824   33.329 86.788  1.00 21.36 ? 93  TYR B O   1 
ATOM   3315 C  CB  . TYR B 1 93  ? 8.737   31.966 83.900  1.00 20.97 ? 93  TYR B CB  1 
ATOM   3316 C  CG  . TYR B 1 93  ? 7.778   33.149 83.909  1.00 20.19 ? 93  TYR B CG  1 
ATOM   3317 C  CD1 . TYR B 1 93  ? 6.443   32.987 84.298  1.00 19.99 ? 93  TYR B CD1 1 
ATOM   3318 C  CD2 . TYR B 1 93  ? 8.182   34.412 83.467  1.00 19.66 ? 93  TYR B CD2 1 
ATOM   3319 C  CE1 . TYR B 1 93  ? 5.540   34.063 84.288  1.00 19.79 ? 93  TYR B CE1 1 
ATOM   3320 C  CE2 . TYR B 1 93  ? 7.278   35.510 83.442  1.00 19.60 ? 93  TYR B CE2 1 
ATOM   3321 C  CZ  . TYR B 1 93  ? 5.961   35.320 83.854  1.00 20.10 ? 93  TYR B CZ  1 
ATOM   3322 O  OH  . TYR B 1 93  ? 5.053   36.362 83.848  1.00 20.42 ? 93  TYR B OH  1 
ATOM   3323 N  N   . TYR B 1 94  ? 11.405  32.945 85.216  1.00 20.69 ? 94  TYR B N   1 
ATOM   3324 C  CA  . TYR B 1 94  ? 12.271  34.019 85.682  1.00 20.34 ? 94  TYR B CA  1 
ATOM   3325 C  C   . TYR B 1 94  ? 12.087  35.272 84.860  1.00 20.26 ? 94  TYR B C   1 
ATOM   3326 O  O   . TYR B 1 94  ? 12.092  35.225 83.633  1.00 20.33 ? 94  TYR B O   1 
ATOM   3327 C  CB  . TYR B 1 94  ? 13.736  33.601 85.664  1.00 20.18 ? 94  TYR B CB  1 
ATOM   3328 C  CG  . TYR B 1 94  ? 14.047  32.412 86.544  1.00 20.55 ? 94  TYR B CG  1 
ATOM   3329 C  CD1 . TYR B 1 94  ? 14.149  31.131 86.004  1.00 20.23 ? 94  TYR B CD1 1 
ATOM   3330 C  CD2 . TYR B 1 94  ? 14.234  32.562 87.913  1.00 19.95 ? 94  TYR B CD2 1 
ATOM   3331 C  CE1 . TYR B 1 94  ? 14.428  30.043 86.799  1.00 20.05 ? 94  TYR B CE1 1 
ATOM   3332 C  CE2 . TYR B 1 94  ? 14.520  31.471 88.715  1.00 20.43 ? 94  TYR B CE2 1 
ATOM   3333 C  CZ  . TYR B 1 94  ? 14.613  30.210 88.151  1.00 20.18 ? 94  TYR B CZ  1 
ATOM   3334 O  OH  . TYR B 1 94  ? 14.897  29.113 88.938  1.00 20.21 ? 94  TYR B OH  1 
ATOM   3335 N  N   . ALA B 1 95  ? 11.900  36.391 85.551  1.00 20.19 ? 95  ALA B N   1 
ATOM   3336 C  CA  . ALA B 1 95  ? 11.965  37.692 84.920  1.00 20.50 ? 95  ALA B CA  1 
ATOM   3337 C  C   . ALA B 1 95  ? 13.431  38.104 84.879  1.00 20.89 ? 95  ALA B C   1 
ATOM   3338 O  O   . ALA B 1 95  ? 14.141  38.011 85.889  1.00 21.01 ? 95  ALA B O   1 
ATOM   3339 C  CB  . ALA B 1 95  ? 11.155  38.691 85.690  1.00 20.33 ? 95  ALA B CB  1 
ATOM   3340 N  N   . VAL B 1 96  ? 13.891  38.524 83.705  1.00 21.15 ? 96  VAL B N   1 
ATOM   3341 C  CA  . VAL B 1 96  ? 15.284  38.943 83.533  1.00 21.67 ? 96  VAL B CA  1 
ATOM   3342 C  C   . VAL B 1 96  ? 15.417  40.342 82.903  1.00 21.92 ? 96  VAL B C   1 
ATOM   3343 O  O   . VAL B 1 96  ? 14.451  40.897 82.359  1.00 21.93 ? 96  VAL B O   1 
ATOM   3344 C  CB  . VAL B 1 96  ? 16.109  37.917 82.688  1.00 21.75 ? 96  VAL B CB  1 
ATOM   3345 C  CG1 . VAL B 1 96  ? 16.170  36.549 83.363  1.00 21.28 ? 96  VAL B CG1 1 
ATOM   3346 C  CG2 . VAL B 1 96  ? 15.559  37.807 81.269  1.00 21.68 ? 96  VAL B CG2 1 
ATOM   3347 N  N   . ALA B 1 97  ? 16.623  40.899 82.979  1.00 21.98 ? 97  ALA B N   1 
ATOM   3348 C  CA  . ALA B 1 97  ? 16.945  42.109 82.240  1.00 22.16 ? 97  ALA B CA  1 
ATOM   3349 C  C   . ALA B 1 97  ? 18.049  41.827 81.207  1.00 22.43 ? 97  ALA B C   1 
ATOM   3350 O  O   . ALA B 1 97  ? 19.187  41.544 81.565  1.00 21.88 ? 97  ALA B O   1 
ATOM   3351 C  CB  . ALA B 1 97  ? 17.338  43.208 83.187  1.00 22.00 ? 97  ALA B CB  1 
ATOM   3352 N  N   . VAL B 1 98  ? 17.683  41.905 79.928  1.00 23.19 ? 98  VAL B N   1 
ATOM   3353 C  CA  . VAL B 1 98  ? 18.551  41.531 78.813  1.00 24.16 ? 98  VAL B CA  1 
ATOM   3354 C  C   . VAL B 1 98  ? 19.235  42.756 78.218  1.00 25.03 ? 98  VAL B C   1 
ATOM   3355 O  O   . VAL B 1 98  ? 18.580  43.745 77.891  1.00 25.33 ? 98  VAL B O   1 
ATOM   3356 C  CB  . VAL B 1 98  ? 17.746  40.820 77.702  1.00 24.23 ? 98  VAL B CB  1 
ATOM   3357 C  CG1 . VAL B 1 98  ? 18.613  40.556 76.476  1.00 24.53 ? 98  VAL B CG1 1 
ATOM   3358 C  CG2 . VAL B 1 98  ? 17.158  39.518 78.216  1.00 24.06 ? 98  VAL B CG2 1 
ATOM   3359 N  N   . VAL B 1 99  ? 20.554  42.681 78.075  1.00 25.95 ? 99  VAL B N   1 
ATOM   3360 C  CA  . VAL B 1 99  ? 21.351  43.794 77.557  1.00 26.77 ? 99  VAL B CA  1 
ATOM   3361 C  C   . VAL B 1 99  ? 22.256  43.335 76.422  1.00 27.75 ? 99  VAL B C   1 
ATOM   3362 O  O   . VAL B 1 99  ? 22.518  42.136 76.285  1.00 28.15 ? 99  VAL B O   1 
ATOM   3363 C  CB  . VAL B 1 99  ? 22.230  44.423 78.655  1.00 26.48 ? 99  VAL B CB  1 
ATOM   3364 C  CG1 . VAL B 1 99  ? 21.372  45.168 79.642  1.00 26.79 ? 99  VAL B CG1 1 
ATOM   3365 C  CG2 . VAL B 1 99  ? 23.063  43.368 79.363  1.00 26.32 ? 99  VAL B CG2 1 
ATOM   3366 N  N   . LYS B 1 100 ? 22.732  44.280 75.610  1.00 28.77 ? 100 LYS B N   1 
ATOM   3367 C  CA  . LYS B 1 100 ? 23.722  43.961 74.585  1.00 29.76 ? 100 LYS B CA  1 
ATOM   3368 C  C   . LYS B 1 100 ? 25.105  43.809 75.209  1.00 30.32 ? 100 LYS B C   1 
ATOM   3369 O  O   . LYS B 1 100 ? 25.504  44.614 76.061  1.00 30.45 ? 100 LYS B O   1 
ATOM   3370 C  CB  . LYS B 1 100 ? 23.723  45.013 73.479  1.00 29.79 ? 100 LYS B CB  1 
ATOM   3371 C  CG  . LYS B 1 100 ? 22.792  44.672 72.319  1.00 31.04 ? 100 LYS B CG  1 
ATOM   3372 C  CD  . LYS B 1 100 ? 22.476  45.905 71.465  1.00 33.41 ? 100 LYS B CD  1 
ATOM   3373 C  CE  . LYS B 1 100 ? 21.720  45.540 70.180  1.00 33.57 ? 100 LYS B CE  1 
ATOM   3374 N  NZ  . LYS B 1 100 ? 22.636  45.110 69.074  1.00 33.43 ? 100 LYS B NZ  1 
ATOM   3375 N  N   . LYS B 1 101 ? 25.819  42.759 74.806  1.00 31.02 ? 101 LYS B N   1 
ATOM   3376 C  CA  . LYS B 1 101 ? 27.178  42.513 75.293  1.00 31.92 ? 101 LYS B CA  1 
ATOM   3377 C  C   . LYS B 1 101 ? 28.126  43.582 74.754  1.00 32.28 ? 101 LYS B C   1 
ATOM   3378 O  O   . LYS B 1 101 ? 27.917  44.109 73.655  1.00 32.40 ? 101 LYS B O   1 
ATOM   3379 C  CB  . LYS B 1 101 ? 27.654  41.115 74.885  1.00 31.85 ? 101 LYS B CB  1 
ATOM   3380 C  CG  . LYS B 1 101 ? 28.913  40.645 75.600  1.00 32.31 ? 101 LYS B CG  1 
ATOM   3381 C  CD  . LYS B 1 101 ? 29.263  39.203 75.247  1.00 32.57 ? 101 LYS B CD  1 
ATOM   3382 C  CE  . LYS B 1 101 ? 30.486  38.728 76.035  1.00 34.18 ? 101 LYS B CE  1 
ATOM   3383 N  NZ  . LYS B 1 101 ? 30.933  37.355 75.648  1.00 34.66 ? 101 LYS B NZ  1 
ATOM   3384 N  N   . GLY B 1 102 ? 29.159  43.903 75.532  1.00 32.70 ? 102 GLY B N   1 
ATOM   3385 C  CA  . GLY B 1 102 ? 30.139  44.917 75.139  1.00 33.09 ? 102 GLY B CA  1 
ATOM   3386 C  C   . GLY B 1 102 ? 30.184  46.095 76.095  1.00 33.39 ? 102 GLY B C   1 
ATOM   3387 O  O   . GLY B 1 102 ? 31.261  46.607 76.405  1.00 33.35 ? 102 GLY B O   1 
ATOM   3388 N  N   . GLY B 1 103 ? 29.010  46.520 76.566  1.00 33.70 ? 103 GLY B N   1 
ATOM   3389 C  CA  . GLY B 1 103 ? 28.890  47.632 77.518  1.00 33.89 ? 103 GLY B CA  1 
ATOM   3390 C  C   . GLY B 1 103 ? 29.291  47.241 78.926  1.00 33.97 ? 103 GLY B C   1 
ATOM   3391 O  O   . GLY B 1 103 ? 29.602  46.081 79.194  1.00 33.96 ? 103 GLY B O   1 
ATOM   3392 N  N   . SER B 1 104 ? 29.283  48.207 79.837  1.00 34.21 ? 104 SER B N   1 
ATOM   3393 C  CA  . SER B 1 104 ? 29.727  47.942 81.207  1.00 34.56 ? 104 SER B CA  1 
ATOM   3394 C  C   . SER B 1 104 ? 28.755  48.425 82.295  1.00 34.77 ? 104 SER B C   1 
ATOM   3395 O  O   . SER B 1 104 ? 29.082  48.378 83.495  1.00 34.79 ? 104 SER B O   1 
ATOM   3396 C  CB  . SER B 1 104 ? 31.132  48.510 81.434  1.00 34.50 ? 104 SER B CB  1 
ATOM   3397 O  OG  . SER B 1 104 ? 31.206  49.852 80.989  1.00 34.50 ? 104 SER B OG  1 
ATOM   3398 N  N   . PHE B 1 105 ? 27.565  48.877 81.888  1.00 34.74 ? 105 PHE B N   1 
ATOM   3399 C  CA  . PHE B 1 105 ? 26.567  49.312 82.866  1.00 34.73 ? 105 PHE B CA  1 
ATOM   3400 C  C   . PHE B 1 105 ? 25.941  48.131 83.579  1.00 35.01 ? 105 PHE B C   1 
ATOM   3401 O  O   . PHE B 1 105 ? 25.680  47.091 82.969  1.00 35.04 ? 105 PHE B O   1 
ATOM   3402 C  CB  . PHE B 1 105 ? 25.508  50.280 82.286  1.00 34.46 ? 105 PHE B CB  1 
ATOM   3403 C  CG  . PHE B 1 105 ? 24.637  49.697 81.198  1.00 33.98 ? 105 PHE B CG  1 
ATOM   3404 C  CD1 . PHE B 1 105 ? 25.001  49.809 79.859  1.00 33.54 ? 105 PHE B CD1 1 
ATOM   3405 C  CD2 . PHE B 1 105 ? 23.432  49.090 81.505  1.00 33.30 ? 105 PHE B CD2 1 
ATOM   3406 C  CE1 . PHE B 1 105 ? 24.203  49.295 78.850  1.00 32.57 ? 105 PHE B CE1 1 
ATOM   3407 C  CE2 . PHE B 1 105 ? 22.628  48.576 80.501  1.00 33.30 ? 105 PHE B CE2 1 
ATOM   3408 C  CZ  . PHE B 1 105 ? 23.017  48.680 79.169  1.00 33.49 ? 105 PHE B CZ  1 
ATOM   3409 N  N   . GLN B 1 106 ? 25.747  48.293 84.884  1.00 35.22 ? 106 GLN B N   1 
ATOM   3410 C  CA  . GLN B 1 106 ? 25.143  47.263 85.712  1.00 35.27 ? 106 GLN B CA  1 
ATOM   3411 C  C   . GLN B 1 106 ? 23.715  47.659 86.070  1.00 35.42 ? 106 GLN B C   1 
ATOM   3412 O  O   . GLN B 1 106 ? 23.250  48.732 85.671  1.00 35.35 ? 106 GLN B O   1 
ATOM   3413 C  CB  . GLN B 1 106 ? 25.989  47.037 86.967  1.00 35.23 ? 106 GLN B CB  1 
ATOM   3414 C  CG  . GLN B 1 106 ? 27.419  46.606 86.678  1.00 35.30 ? 106 GLN B CG  1 
ATOM   3415 C  CD  . GLN B 1 106 ? 27.493  45.372 85.800  1.00 35.44 ? 106 GLN B CD  1 
ATOM   3416 O  OE1 . GLN B 1 106 ? 26.667  44.466 85.909  1.00 36.35 ? 106 GLN B OE1 1 
ATOM   3417 N  NE2 . GLN B 1 106 ? 28.482  45.332 84.924  1.00 35.24 ? 106 GLN B NE2 1 
ATOM   3418 N  N   . LEU B 1 107 ? 23.016  46.799 86.812  1.00 35.47 ? 107 LEU B N   1 
ATOM   3419 C  CA  . LEU B 1 107 ? 21.647  47.098 87.224  1.00 35.54 ? 107 LEU B CA  1 
ATOM   3420 C  C   . LEU B 1 107 ? 21.518  48.454 87.944  1.00 35.53 ? 107 LEU B C   1 
ATOM   3421 O  O   . LEU B 1 107 ? 20.525  49.162 87.779  1.00 35.58 ? 107 LEU B O   1 
ATOM   3422 C  CB  . LEU B 1 107 ? 21.082  45.962 88.079  1.00 35.55 ? 107 LEU B CB  1 
ATOM   3423 C  CG  . LEU B 1 107 ? 19.554  45.787 88.102  1.00 35.49 ? 107 LEU B CG  1 
ATOM   3424 C  CD1 . LEU B 1 107 ? 18.990  45.293 86.770  1.00 34.56 ? 107 LEU B CD1 1 
ATOM   3425 C  CD2 . LEU B 1 107 ? 19.160  44.845 89.216  1.00 35.60 ? 107 LEU B CD2 1 
ATOM   3426 N  N   . ASN B 1 108 ? 22.535  48.819 88.716  1.00 35.51 ? 108 ASN B N   1 
ATOM   3427 C  CA  . ASN B 1 108 ? 22.529  50.081 89.456  1.00 35.71 ? 108 ASN B CA  1 
ATOM   3428 C  C   . ASN B 1 108 ? 22.857  51.316 88.619  1.00 35.83 ? 108 ASN B C   1 
ATOM   3429 O  O   . ASN B 1 108 ? 22.754  52.442 89.099  1.00 35.87 ? 108 ASN B O   1 
ATOM   3430 C  CB  . ASN B 1 108 ? 23.453  50.003 90.682  1.00 35.70 ? 108 ASN B CB  1 
ATOM   3431 C  CG  . ASN B 1 108 ? 24.887  49.587 90.336  1.00 36.01 ? 108 ASN B CG  1 
ATOM   3432 O  OD1 . ASN B 1 108 ? 25.710  49.414 91.230  1.00 36.26 ? 108 ASN B OD1 1 
ATOM   3433 N  ND2 . ASN B 1 108 ? 25.188  49.427 89.052  1.00 36.12 ? 108 ASN B ND2 1 
ATOM   3434 N  N   . GLU B 1 109 ? 23.245  51.101 87.368  1.00 35.96 ? 109 GLU B N   1 
ATOM   3435 C  CA  . GLU B 1 109 ? 23.687  52.193 86.493  1.00 36.13 ? 109 GLU B CA  1 
ATOM   3436 C  C   . GLU B 1 109 ? 22.724  52.404 85.316  1.00 35.47 ? 109 GLU B C   1 
ATOM   3437 O  O   . GLU B 1 109 ? 23.136  52.801 84.224  1.00 35.43 ? 109 GLU B O   1 
ATOM   3438 C  CB  . GLU B 1 109 ? 25.132  51.938 86.008  1.00 36.01 ? 109 GLU B CB  1 
ATOM   3439 C  CG  . GLU B 1 109 ? 26.173  51.985 87.136  1.00 37.31 ? 109 GLU B CG  1 
ATOM   3440 C  CD  . GLU B 1 109 ? 27.454  51.194 86.852  1.00 37.46 ? 109 GLU B CD  1 
ATOM   3441 O  OE1 . GLU B 1 109 ? 28.375  51.736 86.201  1.00 39.09 ? 109 GLU B OE1 1 
ATOM   3442 O  OE2 . GLU B 1 109 ? 27.555  50.038 87.320  1.00 39.51 ? 109 GLU B OE2 1 
ATOM   3443 N  N   . LEU B 1 110 ? 21.437  52.154 85.547  1.00 34.93 ? 110 LEU B N   1 
ATOM   3444 C  CA  . LEU B 1 110 ? 20.457  52.216 84.463  1.00 34.55 ? 110 LEU B CA  1 
ATOM   3445 C  C   . LEU B 1 110 ? 19.877  53.607 84.209  1.00 34.38 ? 110 LEU B C   1 
ATOM   3446 O  O   . LEU B 1 110 ? 19.110  53.795 83.263  1.00 34.51 ? 110 LEU B O   1 
ATOM   3447 C  CB  . LEU B 1 110 ? 19.332  51.196 84.674  1.00 34.40 ? 110 LEU B CB  1 
ATOM   3448 C  CG  . LEU B 1 110 ? 19.691  49.728 84.436  1.00 33.90 ? 110 LEU B CG  1 
ATOM   3449 C  CD1 . LEU B 1 110 ? 18.556  48.831 84.908  1.00 33.96 ? 110 LEU B CD1 1 
ATOM   3450 C  CD2 . LEU B 1 110 ? 20.009  49.465 82.983  1.00 32.81 ? 110 LEU B CD2 1 
ATOM   3451 N  N   . GLN B 1 111 ? 20.246  54.577 85.039  1.00 33.94 ? 111 GLN B N   1 
ATOM   3452 C  CA  . GLN B 1 111 ? 19.696  55.919 84.919  1.00 33.76 ? 111 GLN B CA  1 
ATOM   3453 C  C   . GLN B 1 111 ? 20.146  56.606 83.634  1.00 33.59 ? 111 GLN B C   1 
ATOM   3454 O  O   . GLN B 1 111 ? 21.302  56.487 83.224  1.00 33.80 ? 111 GLN B O   1 
ATOM   3455 C  CB  . GLN B 1 111 ? 20.085  56.754 86.123  1.00 33.83 ? 111 GLN B CB  1 
ATOM   3456 C  CG  . GLN B 1 111 ? 19.496  58.145 86.127  1.00 34.50 ? 111 GLN B CG  1 
ATOM   3457 C  CD  . GLN B 1 111 ? 20.008  58.963 87.287  1.00 36.08 ? 111 GLN B CD  1 
ATOM   3458 O  OE1 . GLN B 1 111 ? 20.468  58.411 88.294  1.00 36.56 ? 111 GLN B OE1 1 
ATOM   3459 N  NE2 . GLN B 1 111 ? 19.936  60.287 87.160  1.00 35.99 ? 111 GLN B NE2 1 
ATOM   3460 N  N   . GLY B 1 112 ? 19.217  57.318 83.002  1.00 33.20 ? 112 GLY B N   1 
ATOM   3461 C  CA  . GLY B 1 112 ? 19.485  58.030 81.757  1.00 32.51 ? 112 GLY B CA  1 
ATOM   3462 C  C   . GLY B 1 112 ? 19.699  57.130 80.553  1.00 32.04 ? 112 GLY B C   1 
ATOM   3463 O  O   . GLY B 1 112 ? 20.175  57.588 79.514  1.00 32.04 ? 112 GLY B O   1 
ATOM   3464 N  N   . LEU B 1 113 ? 19.359  55.853 80.686  1.00 31.36 ? 113 LEU B N   1 
ATOM   3465 C  CA  . LEU B 1 113 ? 19.471  54.933 79.567  1.00 31.09 ? 113 LEU B CA  1 
ATOM   3466 C  C   . LEU B 1 113 ? 18.090  54.575 79.026  1.00 30.88 ? 113 LEU B C   1 
ATOM   3467 O  O   . LEU B 1 113 ? 17.079  54.914 79.631  1.00 30.83 ? 113 LEU B O   1 
ATOM   3468 C  CB  . LEU B 1 113 ? 20.241  53.683 79.974  1.00 31.15 ? 113 LEU B CB  1 
ATOM   3469 C  CG  . LEU B 1 113 ? 21.631  53.874 80.574  1.00 31.36 ? 113 LEU B CG  1 
ATOM   3470 C  CD1 . LEU B 1 113 ? 22.136  52.513 81.040  1.00 31.16 ? 113 LEU B CD1 1 
ATOM   3471 C  CD2 . LEU B 1 113 ? 22.618  54.543 79.592  1.00 30.64 ? 113 LEU B CD2 1 
ATOM   3472 N  N   . LYS B 1 114 ? 18.054  53.892 77.887  1.00 30.58 ? 114 LYS B N   1 
ATOM   3473 C  CA  . LYS B 1 114 ? 16.796  53.605 77.204  1.00 30.65 ? 114 LYS B CA  1 
ATOM   3474 C  C   . LYS B 1 114 ? 16.280  52.191 77.478  1.00 30.19 ? 114 LYS B C   1 
ATOM   3475 O  O   . LYS B 1 114 ? 16.987  51.219 77.236  1.00 30.24 ? 114 LYS B O   1 
ATOM   3476 C  CB  . LYS B 1 114 ? 16.949  53.865 75.699  1.00 30.59 ? 114 LYS B CB  1 
ATOM   3477 C  CG  . LYS B 1 114 ? 16.984  55.361 75.346  1.00 31.32 ? 114 LYS B CG  1 
ATOM   3478 C  CD  . LYS B 1 114 ? 17.425  55.648 73.902  1.00 31.22 ? 114 LYS B CD  1 
ATOM   3479 C  CE  . LYS B 1 114 ? 18.928  55.826 73.800  1.00 31.66 ? 114 LYS B CE  1 
ATOM   3480 N  NZ  . LYS B 1 114 ? 19.381  55.631 72.411  1.00 31.80 ? 114 LYS B NZ  1 
ATOM   3481 N  N   . SER B 1 115 ? 15.049  52.078 77.973  1.00 29.89 ? 115 SER B N   1 
ATOM   3482 C  CA  . SER B 1 115 ? 14.495  50.764 78.344  1.00 29.90 ? 115 SER B CA  1 
ATOM   3483 C  C   . SER B 1 115 ? 13.389  50.222 77.417  1.00 30.05 ? 115 SER B C   1 
ATOM   3484 O  O   . SER B 1 115 ? 12.722  50.980 76.707  1.00 30.15 ? 115 SER B O   1 
ATOM   3485 C  CB  . SER B 1 115 ? 14.019  50.759 79.803  1.00 29.70 ? 115 SER B CB  1 
ATOM   3486 O  OG  . SER B 1 115 ? 12.834  51.513 79.972  1.00 28.80 ? 115 SER B OG  1 
ATOM   3487 N  N   . CYS B 1 116 ? 13.223  48.901 77.420  1.00 29.85 ? 116 CYS B N   1 
ATOM   3488 C  CA  . CYS B 1 116 ? 12.139  48.256 76.700  1.00 29.95 ? 116 CYS B CA  1 
ATOM   3489 C  C   . CYS B 1 116 ? 11.373  47.388 77.675  1.00 29.62 ? 116 CYS B C   1 
ATOM   3490 O  O   . CYS B 1 116 ? 11.962  46.590 78.397  1.00 29.91 ? 116 CYS B O   1 
ATOM   3491 C  CB  . CYS B 1 116 ? 12.658  47.402 75.543  1.00 30.01 ? 116 CYS B CB  1 
ATOM   3492 S  SG  . CYS B 1 116 ? 13.815  48.232 74.446  1.00 31.78 ? 116 CYS B SG  1 
ATOM   3493 N  N   . HIS B 1 117 ? 10.057  47.556 77.685  1.00 29.19 ? 117 HIS B N   1 
ATOM   3494 C  CA  . HIS B 1 117 ? 9.172   46.840 78.591  1.00 28.51 ? 117 HIS B CA  1 
ATOM   3495 C  C   . HIS B 1 117 ? 8.074   46.140 77.791  1.00 28.38 ? 117 HIS B C   1 
ATOM   3496 O  O   . HIS B 1 117 ? 7.668   46.626 76.730  1.00 28.34 ? 117 HIS B O   1 
ATOM   3497 C  CB  . HIS B 1 117 ? 8.537   47.831 79.561  1.00 28.43 ? 117 HIS B CB  1 
ATOM   3498 C  CG  . HIS B 1 117 ? 9.524   48.694 80.285  1.00 28.09 ? 117 HIS B CG  1 
ATOM   3499 N  ND1 . HIS B 1 117 ? 9.979   48.404 81.554  1.00 27.41 ? 117 HIS B ND1 1 
ATOM   3500 C  CD2 . HIS B 1 117 ? 10.135  49.846 79.921  1.00 27.61 ? 117 HIS B CD2 1 
ATOM   3501 C  CE1 . HIS B 1 117 ? 10.826  49.340 81.940  1.00 26.97 ? 117 HIS B CE1 1 
ATOM   3502 N  NE2 . HIS B 1 117 ? 10.941  50.224 80.966  1.00 27.54 ? 117 HIS B NE2 1 
ATOM   3503 N  N   . THR B 1 118 ? 7.587   45.011 78.303  1.00 27.97 ? 118 THR B N   1 
ATOM   3504 C  CA  . THR B 1 118 ? 6.525   44.242 77.637  1.00 27.43 ? 118 THR B CA  1 
ATOM   3505 C  C   . THR B 1 118 ? 5.218   45.016 77.580  1.00 27.09 ? 118 THR B C   1 
ATOM   3506 O  O   . THR B 1 118 ? 4.446   44.875 76.623  1.00 27.35 ? 118 THR B O   1 
ATOM   3507 C  CB  . THR B 1 118 ? 6.251   42.907 78.348  1.00 27.49 ? 118 THR B CB  1 
ATOM   3508 O  OG1 . THR B 1 118 ? 5.746   43.168 79.660  1.00 27.99 ? 118 THR B OG1 1 
ATOM   3509 C  CG2 . THR B 1 118 ? 7.526   42.069 78.460  1.00 27.36 ? 118 THR B CG2 1 
ATOM   3510 N  N   . GLY B 1 119 ? 4.982   45.833 78.604  1.00 26.68 ? 119 GLY B N   1 
ATOM   3511 C  CA  . GLY B 1 119 ? 3.748   46.596 78.738  1.00 26.28 ? 119 GLY B CA  1 
ATOM   3512 C  C   . GLY B 1 119 ? 3.455   46.985 80.174  1.00 26.09 ? 119 GLY B C   1 
ATOM   3513 O  O   . GLY B 1 119 ? 3.888   46.317 81.109  1.00 25.57 ? 119 GLY B O   1 
ATOM   3514 N  N   . LEU B 1 120 ? 2.704   48.069 80.341  1.00 26.34 ? 120 LEU B N   1 
ATOM   3515 C  CA  . LEU B 1 120 ? 2.359   48.587 81.659  1.00 26.69 ? 120 LEU B CA  1 
ATOM   3516 C  C   . LEU B 1 120 ? 1.625   47.559 82.509  1.00 27.14 ? 120 LEU B C   1 
ATOM   3517 O  O   . LEU B 1 120 ? 0.674   46.926 82.052  1.00 26.95 ? 120 LEU B O   1 
ATOM   3518 C  CB  . LEU B 1 120 ? 1.525   49.863 81.532  1.00 26.62 ? 120 LEU B CB  1 
ATOM   3519 C  CG  . LEU B 1 120 ? 1.329   50.704 82.794  1.00 26.23 ? 120 LEU B CG  1 
ATOM   3520 C  CD1 . LEU B 1 120 ? 2.549   51.558 83.093  1.00 26.26 ? 120 LEU B CD1 1 
ATOM   3521 C  CD2 . LEU B 1 120 ? 0.108   51.576 82.644  1.00 25.92 ? 120 LEU B CD2 1 
ATOM   3522 N  N   . ARG B 1 121 ? 2.107   47.407 83.742  1.00 27.78 ? 121 ARG B N   1 
ATOM   3523 C  CA  . ARG B 1 121 ? 1.554   46.514 84.777  1.00 28.71 ? 121 ARG B CA  1 
ATOM   3524 C  C   . ARG B 1 121 ? 1.724   45.010 84.555  1.00 28.28 ? 121 ARG B C   1 
ATOM   3525 O  O   . ARG B 1 121 ? 1.145   44.217 85.299  1.00 28.49 ? 121 ARG B O   1 
ATOM   3526 C  CB  . ARG B 1 121 ? 0.108   46.884 85.163  1.00 28.34 ? 121 ARG B CB  1 
ATOM   3527 C  CG  . ARG B 1 121 ? 0.009   48.231 85.888  1.00 29.93 ? 121 ARG B CG  1 
ATOM   3528 C  CD  . ARG B 1 121 ? -1.420  48.615 86.319  1.00 31.34 ? 121 ARG B CD  1 
ATOM   3529 N  NE  . ARG B 1 121 ? -2.460  48.225 85.347  1.00 37.59 ? 121 ARG B NE  1 
ATOM   3530 C  CZ  . ARG B 1 121 ? -3.573  48.924 85.091  1.00 39.11 ? 121 ARG B CZ  1 
ATOM   3531 N  NH1 . ARG B 1 121 ? -3.803  50.084 85.719  1.00 38.95 ? 121 ARG B NH1 1 
ATOM   3532 N  NH2 . ARG B 1 121 ? -4.454  48.469 84.192  1.00 38.79 ? 121 ARG B NH2 1 
ATOM   3533 N  N   . ARG B 1 122 ? 2.535   44.615 83.571  1.00 28.06 ? 122 ARG B N   1 
ATOM   3534 C  CA  . ARG B 1 122 ? 2.913   43.202 83.396  1.00 27.73 ? 122 ARG B CA  1 
ATOM   3535 C  C   . ARG B 1 122 ? 4.020   42.831 84.377  1.00 27.40 ? 122 ARG B C   1 
ATOM   3536 O  O   . ARG B 1 122 ? 4.661   43.711 84.962  1.00 27.44 ? 122 ARG B O   1 
ATOM   3537 C  CB  . ARG B 1 122 ? 3.401   42.931 81.978  1.00 27.83 ? 122 ARG B CB  1 
ATOM   3538 C  CG  . ARG B 1 122 ? 2.433   43.301 80.874  1.00 29.56 ? 122 ARG B CG  1 
ATOM   3539 C  CD  . ARG B 1 122 ? 1.695   42.094 80.351  1.00 32.55 ? 122 ARG B CD  1 
ATOM   3540 N  NE  . ARG B 1 122 ? 2.570   41.190 79.599  1.00 35.57 ? 122 ARG B NE  1 
ATOM   3541 C  CZ  . ARG B 1 122 ? 2.434   40.889 78.307  1.00 36.48 ? 122 ARG B CZ  1 
ATOM   3542 N  NH1 . ARG B 1 122 ? 1.445   41.427 77.590  1.00 36.65 ? 122 ARG B NH1 1 
ATOM   3543 N  NH2 . ARG B 1 122 ? 3.283   40.036 77.734  1.00 35.52 ? 122 ARG B NH2 1 
ATOM   3544 N  N   . THR B 1 123 ? 4.266   41.529 84.529  1.00 27.02 ? 123 THR B N   1 
ATOM   3545 C  CA  . THR B 1 123 ? 5.183   41.009 85.549  1.00 26.59 ? 123 THR B CA  1 
ATOM   3546 C  C   . THR B 1 123 ? 6.663   41.243 85.249  1.00 26.28 ? 123 THR B C   1 
ATOM   3547 O  O   . THR B 1 123 ? 7.330   41.996 85.965  1.00 26.44 ? 123 THR B O   1 
ATOM   3548 C  CB  . THR B 1 123 ? 4.927   39.533 85.806  1.00 26.54 ? 123 THR B CB  1 
ATOM   3549 O  OG1 . THR B 1 123 ? 3.560   39.369 86.179  1.00 27.34 ? 123 THR B OG1 1 
ATOM   3550 C  CG2 . THR B 1 123 ? 5.812   39.016 86.932  1.00 26.66 ? 123 THR B CG2 1 
ATOM   3551 N  N   . ALA B 1 124 ? 7.167   40.611 84.195  1.00 25.80 ? 124 ALA B N   1 
ATOM   3552 C  CA  . ALA B 1 124 ? 8.563   40.755 83.801  1.00 25.40 ? 124 ALA B CA  1 
ATOM   3553 C  C   . ALA B 1 124 ? 8.877   42.133 83.239  1.00 25.33 ? 124 ALA B C   1 
ATOM   3554 O  O   . ALA B 1 124 ? 10.025  42.596 83.341  1.00 25.21 ? 124 ALA B O   1 
ATOM   3555 C  CB  . ALA B 1 124 ? 8.916   39.718 82.791  1.00 25.57 ? 124 ALA B CB  1 
ATOM   3556 N  N   . GLY B 1 125 ? 7.860   42.771 82.650  1.00 24.97 ? 125 GLY B N   1 
ATOM   3557 C  CA  . GLY B 1 125 ? 8.031   44.028 81.921  1.00 24.67 ? 125 GLY B CA  1 
ATOM   3558 C  C   . GLY B 1 125 ? 7.927   45.315 82.725  1.00 24.41 ? 125 GLY B C   1 
ATOM   3559 O  O   . GLY B 1 125 ? 8.513   46.336 82.354  1.00 24.16 ? 125 GLY B O   1 
ATOM   3560 N  N   . TRP B 1 126 ? 7.181   45.278 83.825  1.00 24.14 ? 126 TRP B N   1 
ATOM   3561 C  CA  . TRP B 1 126 ? 6.970   46.478 84.634  1.00 23.71 ? 126 TRP B CA  1 
ATOM   3562 C  C   . TRP B 1 126 ? 7.131   46.214 86.128  1.00 23.90 ? 126 TRP B C   1 
ATOM   3563 O  O   . TRP B 1 126 ? 8.027   46.778 86.758  1.00 23.83 ? 126 TRP B O   1 
ATOM   3564 C  CB  . TRP B 1 126 ? 5.590   47.053 84.358  1.00 23.24 ? 126 TRP B CB  1 
ATOM   3565 C  CG  . TRP B 1 126 ? 5.299   48.290 85.111  1.00 22.63 ? 126 TRP B CG  1 
ATOM   3566 C  CD1 . TRP B 1 126 ? 4.586   48.396 86.262  1.00 22.24 ? 126 TRP B CD1 1 
ATOM   3567 C  CD2 . TRP B 1 126 ? 5.696   49.614 84.756  1.00 22.31 ? 126 TRP B CD2 1 
ATOM   3568 N  NE1 . TRP B 1 126 ? 4.519   49.706 86.657  1.00 22.30 ? 126 TRP B NE1 1 
ATOM   3569 C  CE2 . TRP B 1 126 ? 5.189   50.478 85.747  1.00 21.94 ? 126 TRP B CE2 1 
ATOM   3570 C  CE3 . TRP B 1 126 ? 6.435   50.156 83.694  1.00 21.78 ? 126 TRP B CE3 1 
ATOM   3571 C  CZ2 . TRP B 1 126 ? 5.395   51.854 85.715  1.00 22.14 ? 126 TRP B CZ2 1 
ATOM   3572 C  CZ3 . TRP B 1 126 ? 6.652   51.520 83.666  1.00 22.38 ? 126 TRP B CZ3 1 
ATOM   3573 C  CH2 . TRP B 1 126 ? 6.129   52.359 84.672  1.00 22.61 ? 126 TRP B CH2 1 
ATOM   3574 N  N   . ASN B 1 127 ? 6.263   45.350 86.673  1.00 23.83 ? 127 ASN B N   1 
ATOM   3575 C  CA  . ASN B 1 127 ? 6.182   45.094 88.113  1.00 23.64 ? 127 ASN B CA  1 
ATOM   3576 C  C   . ASN B 1 127 ? 7.501   44.657 88.747  1.00 23.52 ? 127 ASN B C   1 
ATOM   3577 O  O   . ASN B 1 127 ? 7.818   45.059 89.860  1.00 23.26 ? 127 ASN B O   1 
ATOM   3578 C  CB  . ASN B 1 127 ? 5.092   44.060 88.424  1.00 23.81 ? 127 ASN B CB  1 
ATOM   3579 C  CG  . ASN B 1 127 ? 3.675   44.636 88.359  1.00 24.10 ? 127 ASN B CG  1 
ATOM   3580 O  OD1 . ASN B 1 127 ? 2.695   43.878 88.395  1.00 24.32 ? 127 ASN B OD1 1 
ATOM   3581 N  ND2 . ASN B 1 127 ? 3.556   45.965 88.276  1.00 23.12 ? 127 ASN B ND2 1 
ATOM   3582 N  N   . VAL B 1 128 ? 8.266   43.833 88.042  1.00 23.55 ? 128 VAL B N   1 
ATOM   3583 C  CA  . VAL B 1 128 ? 9.550   43.390 88.570  1.00 23.76 ? 128 VAL B CA  1 
ATOM   3584 C  C   . VAL B 1 128 ? 10.652  44.460 88.443  1.00 24.38 ? 128 VAL B C   1 
ATOM   3585 O  O   . VAL B 1 128 ? 11.215  44.875 89.470  1.00 24.66 ? 128 VAL B O   1 
ATOM   3586 C  CB  . VAL B 1 128 ? 9.993   42.055 87.977  1.00 23.55 ? 128 VAL B CB  1 
ATOM   3587 C  CG1 . VAL B 1 128 ? 11.391  41.746 88.418  1.00 23.49 ? 128 VAL B CG1 1 
ATOM   3588 C  CG2 . VAL B 1 128 ? 9.049   40.958 88.412  1.00 22.87 ? 128 VAL B CG2 1 
ATOM   3589 N  N   . PRO B 1 129 ? 10.958  44.928 87.206  1.00 24.51 ? 129 PRO B N   1 
ATOM   3590 C  CA  . PRO B 1 129 ? 11.958  45.988 87.093  1.00 24.62 ? 129 PRO B CA  1 
ATOM   3591 C  C   . PRO B 1 129 ? 11.616  47.231 87.915  1.00 24.84 ? 129 PRO B C   1 
ATOM   3592 O  O   . PRO B 1 129 ? 12.467  47.703 88.652  1.00 25.27 ? 129 PRO B O   1 
ATOM   3593 C  CB  . PRO B 1 129 ? 11.966  46.319 85.594  1.00 24.42 ? 129 PRO B CB  1 
ATOM   3594 C  CG  . PRO B 1 129 ? 10.697  45.806 85.084  1.00 24.47 ? 129 PRO B CG  1 
ATOM   3595 C  CD  . PRO B 1 129 ? 10.442  44.559 85.881  1.00 24.57 ? 129 PRO B CD  1 
ATOM   3596 N  N   . ILE B 1 130 ? 10.392  47.746 87.812  1.00 25.00 ? 130 ILE B N   1 
ATOM   3597 C  CA  . ILE B 1 130 ? 10.045  48.972 88.527  1.00 25.14 ? 130 ILE B CA  1 
ATOM   3598 C  C   . ILE B 1 130 ? 10.023  48.746 90.043  1.00 25.67 ? 130 ILE B C   1 
ATOM   3599 O  O   . ILE B 1 130 ? 10.432  49.619 90.809  1.00 26.14 ? 130 ILE B O   1 
ATOM   3600 C  CB  . ILE B 1 130 ? 8.739   49.647 88.003  1.00 25.07 ? 130 ILE B CB  1 
ATOM   3601 C  CG1 . ILE B 1 130 ? 8.832   49.936 86.503  1.00 24.26 ? 130 ILE B CG1 1 
ATOM   3602 C  CG2 . ILE B 1 130 ? 8.421   50.942 88.769  1.00 24.91 ? 130 ILE B CG2 1 
ATOM   3603 C  CD1 . ILE B 1 130 ? 10.090  50.626 86.063  1.00 23.79 ? 130 ILE B CD1 1 
ATOM   3604 N  N   . GLY B 1 131 ? 9.579   47.573 90.477  1.00 25.86 ? 131 GLY B N   1 
ATOM   3605 C  CA  . GLY B 1 131 ? 9.727   47.202 91.882  1.00 26.31 ? 131 GLY B CA  1 
ATOM   3606 C  C   . GLY B 1 131 ? 11.189  47.172 92.300  1.00 26.64 ? 131 GLY B C   1 
ATOM   3607 O  O   . GLY B 1 131 ? 11.536  47.629 93.381  1.00 26.47 ? 131 GLY B O   1 
ATOM   3608 N  N   . THR B 1 132 ? 12.030  46.624 91.425  1.00 27.25 ? 132 THR B N   1 
ATOM   3609 C  CA  . THR B 1 132 ? 13.474  46.493 91.634  1.00 28.12 ? 132 THR B CA  1 
ATOM   3610 C  C   . THR B 1 132 ? 14.212  47.839 91.636  1.00 28.67 ? 132 THR B C   1 
ATOM   3611 O  O   . THR B 1 132 ? 15.199  48.006 92.351  1.00 28.60 ? 132 THR B O   1 
ATOM   3612 C  CB  . THR B 1 132 ? 14.086  45.556 90.543  1.00 27.99 ? 132 THR B CB  1 
ATOM   3613 O  OG1 . THR B 1 132 ? 13.775  44.200 90.862  1.00 28.64 ? 132 THR B OG1 1 
ATOM   3614 C  CG2 . THR B 1 132 ? 15.610  45.695 90.423  1.00 28.05 ? 132 THR B CG2 1 
ATOM   3615 N  N   . LEU B 1 133 ? 13.742  48.788 90.834  1.00 29.35 ? 133 LEU B N   1 
ATOM   3616 C  CA  . LEU B 1 133 ? 14.458  50.044 90.657  1.00 30.30 ? 133 LEU B CA  1 
ATOM   3617 C  C   . LEU B 1 133 ? 13.907  51.186 91.497  1.00 31.30 ? 133 LEU B C   1 
ATOM   3618 O  O   . LEU B 1 133 ? 14.507  52.252 91.547  1.00 31.37 ? 133 LEU B O   1 
ATOM   3619 C  CB  . LEU B 1 133 ? 14.486  50.445 89.185  1.00 29.87 ? 133 LEU B CB  1 
ATOM   3620 C  CG  . LEU B 1 133 ? 15.405  49.632 88.274  1.00 29.58 ? 133 LEU B CG  1 
ATOM   3621 C  CD1 . LEU B 1 133 ? 15.141  49.953 86.810  1.00 28.84 ? 133 LEU B CD1 1 
ATOM   3622 C  CD2 . LEU B 1 133 ? 16.853  49.891 88.617  1.00 29.67 ? 133 LEU B CD2 1 
ATOM   3623 N  N   . ARG B 1 134 ? 12.781  50.953 92.173  1.00 32.62 ? 134 ARG B N   1 
ATOM   3624 C  CA  . ARG B 1 134 ? 12.075  52.008 92.918  1.00 33.75 ? 134 ARG B CA  1 
ATOM   3625 C  C   . ARG B 1 134 ? 12.974  52.831 93.866  1.00 34.91 ? 134 ARG B C   1 
ATOM   3626 O  O   . ARG B 1 134 ? 12.828  54.060 93.931  1.00 34.98 ? 134 ARG B O   1 
ATOM   3627 C  CB  . ARG B 1 134 ? 10.854  51.439 93.653  1.00 33.51 ? 134 ARG B CB  1 
ATOM   3628 C  CG  . ARG B 1 134 ? 10.001  52.484 94.360  1.00 33.56 ? 134 ARG B CG  1 
ATOM   3629 C  CD  . ARG B 1 134 ? 8.713   51.890 94.936  1.00 33.41 ? 134 ARG B CD  1 
ATOM   3630 N  NE  . ARG B 1 134 ? 8.952   50.767 95.842  1.00 32.67 ? 134 ARG B NE  1 
ATOM   3631 C  CZ  . ARG B 1 134 ? 9.224   50.892 97.139  1.00 32.17 ? 134 ARG B CZ  1 
ATOM   3632 N  NH1 . ARG B 1 134 ? 9.307   52.098 97.701  1.00 31.16 ? 134 ARG B NH1 1 
ATOM   3633 N  NH2 . ARG B 1 134 ? 9.432   49.805 97.871  1.00 30.97 ? 134 ARG B NH2 1 
ATOM   3634 N  N   . PRO B 1 135 ? 13.904  52.167 94.596  1.00 35.95 ? 135 PRO B N   1 
ATOM   3635 C  CA  . PRO B 1 135 ? 14.853  52.912 95.430  1.00 36.84 ? 135 PRO B CA  1 
ATOM   3636 C  C   . PRO B 1 135 ? 15.853  53.799 94.666  1.00 37.78 ? 135 PRO B C   1 
ATOM   3637 O  O   . PRO B 1 135 ? 16.649  54.489 95.302  1.00 38.07 ? 135 PRO B O   1 
ATOM   3638 C  CB  . PRO B 1 135 ? 15.605  51.804 96.185  1.00 36.73 ? 135 PRO B CB  1 
ATOM   3639 C  CG  . PRO B 1 135 ? 14.740  50.601 96.078  1.00 36.23 ? 135 PRO B CG  1 
ATOM   3640 C  CD  . PRO B 1 135 ? 14.115  50.714 94.732  1.00 35.88 ? 135 PRO B CD  1 
ATOM   3641 N  N   . PHE B 1 136 ? 15.826  53.779 93.335  1.00 38.81 ? 136 PHE B N   1 
ATOM   3642 C  CA  . PHE B 1 136 ? 16.648  54.697 92.537  1.00 40.09 ? 136 PHE B CA  1 
ATOM   3643 C  C   . PHE B 1 136 ? 15.796  55.800 91.910  1.00 40.81 ? 136 PHE B C   1 
ATOM   3644 O  O   . PHE B 1 136 ? 16.318  56.808 91.435  1.00 40.97 ? 136 PHE B O   1 
ATOM   3645 C  CB  . PHE B 1 136 ? 17.444  53.954 91.451  1.00 40.17 ? 136 PHE B CB  1 
ATOM   3646 C  CG  . PHE B 1 136 ? 18.404  52.926 91.992  1.00 41.35 ? 136 PHE B CG  1 
ATOM   3647 C  CD1 . PHE B 1 136 ? 19.534  53.313 92.715  1.00 42.23 ? 136 PHE B CD1 1 
ATOM   3648 C  CD2 . PHE B 1 136 ? 18.179  51.563 91.783  1.00 42.44 ? 136 PHE B CD2 1 
ATOM   3649 C  CE1 . PHE B 1 136 ? 20.423  52.358 93.231  1.00 42.52 ? 136 PHE B CE1 1 
ATOM   3650 C  CE2 . PHE B 1 136 ? 19.062  50.595 92.294  1.00 42.24 ? 136 PHE B CE2 1 
ATOM   3651 C  CZ  . PHE B 1 136 ? 20.185  50.995 93.015  1.00 42.13 ? 136 PHE B CZ  1 
ATOM   3652 N  N   . LEU B 1 137 ? 14.481  55.615 91.941  1.00 41.77 ? 137 LEU B N   1 
ATOM   3653 C  CA  . LEU B 1 137 ? 13.561  56.465 91.196  1.00 42.65 ? 137 LEU B CA  1 
ATOM   3654 C  C   . LEU B 1 137 ? 13.332  57.837 91.818  1.00 43.61 ? 137 LEU B C   1 
ATOM   3655 O  O   . LEU B 1 137 ? 12.805  58.738 91.156  1.00 43.69 ? 137 LEU B O   1 
ATOM   3656 C  CB  . LEU B 1 137 ? 12.215  55.756 91.001  1.00 42.44 ? 137 LEU B CB  1 
ATOM   3657 C  CG  . LEU B 1 137 ? 12.135  54.491 90.147  1.00 41.60 ? 137 LEU B CG  1 
ATOM   3658 C  CD1 . LEU B 1 137 ? 10.683  54.097 89.991  1.00 41.29 ? 137 LEU B CD1 1 
ATOM   3659 C  CD2 . LEU B 1 137 ? 12.786  54.675 88.792  1.00 40.57 ? 137 LEU B CD2 1 
ATOM   3660 N  N   . ASN B 1 138 ? 13.731  57.992 93.081  1.00 44.87 ? 138 ASN B N   1 
ATOM   3661 C  CA  . ASN B 1 138 ? 13.457  59.209 93.855  1.00 46.09 ? 138 ASN B CA  1 
ATOM   3662 C  C   . ASN B 1 138 ? 11.953  59.540 93.819  1.00 46.17 ? 138 ASN B C   1 
ATOM   3663 O  O   . ASN B 1 138 ? 11.564  60.691 93.623  1.00 46.31 ? 138 ASN B O   1 
ATOM   3664 C  CB  . ASN B 1 138 ? 14.309  60.406 93.359  1.00 46.57 ? 138 ASN B CB  1 
ATOM   3665 C  CG  . ASN B 1 138 ? 15.826  60.213 93.568  1.00 48.89 ? 138 ASN B CG  1 
ATOM   3666 O  OD1 . ASN B 1 138 ? 16.259  59.419 94.409  1.00 48.70 ? 138 ASN B OD1 1 
ATOM   3667 N  ND2 . ASN B 1 138 ? 16.634  60.989 92.808  1.00 53.05 ? 138 ASN B ND2 1 
ATOM   3668 N  N   . TRP B 1 139 ? 11.115  58.521 94.002  1.00 46.44 ? 139 TRP B N   1 
ATOM   3669 C  CA  . TRP B 1 139 ? 9.662   58.681 93.883  1.00 46.79 ? 139 TRP B CA  1 
ATOM   3670 C  C   . TRP B 1 139 ? 9.004   59.177 95.177  1.00 47.30 ? 139 TRP B C   1 
ATOM   3671 O  O   . TRP B 1 139 ? 9.303   58.679 96.264  1.00 47.37 ? 139 TRP B O   1 
ATOM   3672 C  CB  . TRP B 1 139 ? 9.017   57.378 93.399  1.00 46.39 ? 139 TRP B CB  1 
ATOM   3673 C  CG  . TRP B 1 139 ? 7.533   57.476 93.141  1.00 46.08 ? 139 TRP B CG  1 
ATOM   3674 C  CD1 . TRP B 1 139 ? 6.877   58.458 92.452  1.00 45.79 ? 139 TRP B CD1 1 
ATOM   3675 C  CD2 . TRP B 1 139 ? 6.530   56.540 93.549  1.00 45.86 ? 139 TRP B CD2 1 
ATOM   3676 N  NE1 . TRP B 1 139 ? 5.528   58.200 92.419  1.00 45.33 ? 139 TRP B NE1 1 
ATOM   3677 C  CE2 . TRP B 1 139 ? 5.287   57.028 93.083  1.00 45.38 ? 139 TRP B CE2 1 
ATOM   3678 C  CE3 . TRP B 1 139 ? 6.560   55.337 94.273  1.00 45.95 ? 139 TRP B CE3 1 
ATOM   3679 C  CZ2 . TRP B 1 139 ? 4.085   56.358 93.313  1.00 45.76 ? 139 TRP B CZ2 1 
ATOM   3680 C  CZ3 . TRP B 1 139 ? 5.363   54.668 94.506  1.00 45.95 ? 139 TRP B CZ3 1 
ATOM   3681 C  CH2 . TRP B 1 139 ? 4.140   55.181 94.023  1.00 46.15 ? 139 TRP B CH2 1 
ATOM   3682 N  N   . THR B 1 140 ? 8.100   60.149 95.045  1.00 47.92 ? 140 THR B N   1 
ATOM   3683 C  CA  . THR B 1 140 ? 7.474   60.800 96.207  1.00 48.52 ? 140 THR B CA  1 
ATOM   3684 C  C   . THR B 1 140 ? 6.108   60.216 96.625  1.00 48.97 ? 140 THR B C   1 
ATOM   3685 O  O   . THR B 1 140 ? 5.597   60.541 97.704  1.00 49.02 ? 140 THR B O   1 
ATOM   3686 C  CB  . THR B 1 140 ? 7.355   62.354 96.019  1.00 48.47 ? 140 THR B CB  1 
ATOM   3687 O  OG1 . THR B 1 140 ? 6.494   62.658 94.912  1.00 48.31 ? 140 THR B OG1 1 
ATOM   3688 C  CG2 . THR B 1 140 ? 8.722   62.986 95.787  1.00 48.18 ? 140 THR B CG2 1 
ATOM   3689 N  N   . GLY B 1 141 ? 5.540   59.345 95.786  1.00 49.46 ? 141 GLY B N   1 
ATOM   3690 C  CA  . GLY B 1 141 ? 4.176   58.824 95.984  1.00 50.00 ? 141 GLY B CA  1 
ATOM   3691 C  C   . GLY B 1 141 ? 3.137   59.781 95.406  1.00 50.44 ? 141 GLY B C   1 
ATOM   3692 O  O   . GLY B 1 141 ? 3.505   60.763 94.751  1.00 50.46 ? 141 GLY B O   1 
ATOM   3693 N  N   . PRO B 1 142 ? 1.830   59.512 95.642  1.00 50.75 ? 142 PRO B N   1 
ATOM   3694 C  CA  . PRO B 1 142 ? 0.771   60.446 95.204  1.00 50.87 ? 142 PRO B CA  1 
ATOM   3695 C  C   . PRO B 1 142 ? 0.979   61.859 95.785  1.00 50.92 ? 142 PRO B C   1 
ATOM   3696 O  O   . PRO B 1 142 ? 1.521   61.985 96.887  1.00 51.05 ? 142 PRO B O   1 
ATOM   3697 C  CB  . PRO B 1 142 ? -0.518  59.814 95.751  1.00 50.87 ? 142 PRO B CB  1 
ATOM   3698 C  CG  . PRO B 1 142 ? -0.063  58.846 96.807  1.00 51.10 ? 142 PRO B CG  1 
ATOM   3699 C  CD  . PRO B 1 142 ? 1.265   58.336 96.326  1.00 50.80 ? 142 PRO B CD  1 
ATOM   3700 N  N   . PRO B 1 143 ? 0.563   62.919 95.054  1.00 50.80 ? 143 PRO B N   1 
ATOM   3701 C  CA  . PRO B 1 143 ? -0.199  62.923 93.792  1.00 50.54 ? 143 PRO B CA  1 
ATOM   3702 C  C   . PRO B 1 143 ? 0.557   62.327 92.601  1.00 50.08 ? 143 PRO B C   1 
ATOM   3703 O  O   . PRO B 1 143 ? -0.077  61.908 91.628  1.00 50.28 ? 143 PRO B O   1 
ATOM   3704 C  CB  . PRO B 1 143 ? -0.477  64.417 93.539  1.00 50.55 ? 143 PRO B CB  1 
ATOM   3705 C  CG  . PRO B 1 143 ? -0.180  65.109 94.835  1.00 50.92 ? 143 PRO B CG  1 
ATOM   3706 C  CD  . PRO B 1 143 ? 0.888   64.289 95.490  1.00 50.81 ? 143 PRO B CD  1 
ATOM   3707 N  N   . GLU B 1 144 ? 1.889   62.289 92.682  1.00 49.27 ? 144 GLU B N   1 
ATOM   3708 C  CA  . GLU B 1 144 ? 2.720   61.787 91.586  1.00 48.39 ? 144 GLU B CA  1 
ATOM   3709 C  C   . GLU B 1 144 ? 2.473   60.296 91.305  1.00 47.59 ? 144 GLU B C   1 
ATOM   3710 O  O   . GLU B 1 144 ? 2.616   59.461 92.205  1.00 47.65 ? 144 GLU B O   1 
ATOM   3711 C  CB  . GLU B 1 144 ? 4.209   62.064 91.856  1.00 48.39 ? 144 GLU B CB  1 
ATOM   3712 C  CG  . GLU B 1 144 ? 5.126   61.754 90.674  1.00 48.39 ? 144 GLU B CG  1 
ATOM   3713 C  CD  . GLU B 1 144 ? 6.602   62.006 90.962  1.00 48.49 ? 144 GLU B CD  1 
ATOM   3714 O  OE1 . GLU B 1 144 ? 7.155   61.434 91.934  1.00 48.17 ? 144 GLU B OE1 1 
ATOM   3715 O  OE2 . GLU B 1 144 ? 7.215   62.773 90.191  1.00 48.55 ? 144 GLU B OE2 1 
ATOM   3716 N  N   . PRO B 1 145 ? 2.078   59.963 90.059  1.00 46.71 ? 145 PRO B N   1 
ATOM   3717 C  CA  . PRO B 1 145 ? 1.980   58.557 89.678  1.00 45.96 ? 145 PRO B CA  1 
ATOM   3718 C  C   . PRO B 1 145 ? 3.377   58.013 89.449  1.00 45.07 ? 145 PRO B C   1 
ATOM   3719 O  O   . PRO B 1 145 ? 4.267   58.765 89.055  1.00 44.75 ? 145 PRO B O   1 
ATOM   3720 C  CB  . PRO B 1 145 ? 1.200   58.592 88.351  1.00 46.06 ? 145 PRO B CB  1 
ATOM   3721 C  CG  . PRO B 1 145 ? 0.765   60.017 88.152  1.00 46.22 ? 145 PRO B CG  1 
ATOM   3722 C  CD  . PRO B 1 145 ? 1.704   60.856 88.948  1.00 46.61 ? 145 PRO B CD  1 
ATOM   3723 N  N   . ILE B 1 146 ? 3.572   56.720 89.691  1.00 44.35 ? 146 ILE B N   1 
ATOM   3724 C  CA  . ILE B 1 146 ? 4.898   56.116 89.529  1.00 43.59 ? 146 ILE B CA  1 
ATOM   3725 C  C   . ILE B 1 146 ? 5.451   56.280 88.105  1.00 43.31 ? 146 ILE B C   1 
ATOM   3726 O  O   . ILE B 1 146 ? 6.668   56.295 87.899  1.00 43.35 ? 146 ILE B O   1 
ATOM   3727 C  CB  . ILE B 1 146 ? 4.925   54.635 89.969  1.00 43.45 ? 146 ILE B CB  1 
ATOM   3728 C  CG1 . ILE B 1 146 ? 6.364   54.199 90.250  1.00 42.86 ? 146 ILE B CG1 1 
ATOM   3729 C  CG2 . ILE B 1 146 ? 4.243   53.738 88.938  1.00 43.18 ? 146 ILE B CG2 1 
ATOM   3730 C  CD1 . ILE B 1 146 ? 6.469   53.142 91.292  1.00 42.54 ? 146 ILE B CD1 1 
ATOM   3731 N  N   . GLU B 1 147 ? 4.551   56.431 87.138  1.00 42.62 ? 147 GLU B N   1 
ATOM   3732 C  CA  . GLU B 1 147 ? 4.935   56.572 85.746  1.00 42.06 ? 147 GLU B CA  1 
ATOM   3733 C  C   . GLU B 1 147 ? 5.815   57.795 85.511  1.00 41.49 ? 147 GLU B C   1 
ATOM   3734 O  O   . GLU B 1 147 ? 6.725   57.751 84.683  1.00 41.40 ? 147 GLU B O   1 
ATOM   3735 C  CB  . GLU B 1 147 ? 3.694   56.593 84.859  1.00 42.15 ? 147 GLU B CB  1 
ATOM   3736 C  CG  . GLU B 1 147 ? 3.057   55.220 84.677  1.00 43.11 ? 147 GLU B CG  1 
ATOM   3737 C  CD  . GLU B 1 147 ? 1.556   55.222 84.932  1.00 44.41 ? 147 GLU B CD  1 
ATOM   3738 O  OE1 . GLU B 1 147 ? 1.154   55.490 86.086  1.00 44.65 ? 147 GLU B OE1 1 
ATOM   3739 O  OE2 . GLU B 1 147 ? 0.781   54.944 83.984  1.00 44.77 ? 147 GLU B OE2 1 
ATOM   3740 N  N   . ALA B 1 148 ? 5.563   58.868 86.260  1.00 40.85 ? 148 ALA B N   1 
ATOM   3741 C  CA  . ALA B 1 148 ? 6.330   60.112 86.119  1.00 40.25 ? 148 ALA B CA  1 
ATOM   3742 C  C   . ALA B 1 148 ? 7.786   59.953 86.561  1.00 39.83 ? 148 ALA B C   1 
ATOM   3743 O  O   . ALA B 1 148 ? 8.696   60.445 85.892  1.00 39.74 ? 148 ALA B O   1 
ATOM   3744 C  CB  . ALA B 1 148 ? 5.652   61.266 86.868  1.00 40.06 ? 148 ALA B CB  1 
ATOM   3745 N  N   . ALA B 1 149 ? 7.996   59.252 87.674  1.00 39.27 ? 149 ALA B N   1 
ATOM   3746 C  CA  . ALA B 1 149 ? 9.334   59.033 88.217  1.00 38.85 ? 149 ALA B CA  1 
ATOM   3747 C  C   . ALA B 1 149 ? 10.171  58.128 87.311  1.00 38.77 ? 149 ALA B C   1 
ATOM   3748 O  O   . ALA B 1 149 ? 11.387  58.331 87.171  1.00 38.75 ? 149 ALA B O   1 
ATOM   3749 C  CB  . ALA B 1 149 ? 9.247   58.461 89.611  1.00 38.66 ? 149 ALA B CB  1 
ATOM   3750 N  N   . VAL B 1 150 ? 9.511   57.135 86.707  1.00 38.42 ? 150 VAL B N   1 
ATOM   3751 C  CA  . VAL B 1 150 ? 10.126  56.253 85.712  1.00 38.05 ? 150 VAL B CA  1 
ATOM   3752 C  C   . VAL B 1 150 ? 10.456  57.040 84.448  1.00 37.93 ? 150 VAL B C   1 
ATOM   3753 O  O   . VAL B 1 150 ? 11.510  56.836 83.842  1.00 37.87 ? 150 VAL B O   1 
ATOM   3754 C  CB  . VAL B 1 150 ? 9.207   55.063 85.339  1.00 38.07 ? 150 VAL B CB  1 
ATOM   3755 C  CG1 . VAL B 1 150 ? 9.903   54.121 84.361  1.00 37.79 ? 150 VAL B CG1 1 
ATOM   3756 C  CG2 . VAL B 1 150 ? 8.772   54.300 86.582  1.00 37.91 ? 150 VAL B CG2 1 
ATOM   3757 N  N   . ALA B 1 151 ? 9.552   57.942 84.066  1.00 37.79 ? 151 ALA B N   1 
ATOM   3758 C  CA  . ALA B 1 151 ? 9.751   58.818 82.905  1.00 37.55 ? 151 ALA B CA  1 
ATOM   3759 C  C   . ALA B 1 151 ? 10.886  59.810 83.118  1.00 37.35 ? 151 ALA B C   1 
ATOM   3760 O  O   . ALA B 1 151 ? 11.463  60.303 82.148  1.00 37.40 ? 151 ALA B O   1 
ATOM   3761 C  CB  . ALA B 1 151 ? 8.466   59.552 82.550  1.00 37.56 ? 151 ALA B CB  1 
ATOM   3762 N  N   . ARG B 1 152 ? 11.199  60.109 84.379  1.00 37.11 ? 152 ARG B N   1 
ATOM   3763 C  CA  . ARG B 1 152 ? 12.370  60.930 84.700  1.00 36.86 ? 152 ARG B CA  1 
ATOM   3764 C  C   . ARG B 1 152 ? 13.639  60.080 84.728  1.00 36.59 ? 152 ARG B C   1 
ATOM   3765 O  O   . ARG B 1 152 ? 14.709  60.564 84.362  1.00 36.62 ? 152 ARG B O   1 
ATOM   3766 C  CB  . ARG B 1 152 ? 12.209  61.664 86.037  1.00 36.84 ? 152 ARG B CB  1 
ATOM   3767 C  CG  . ARG B 1 152 ? 11.110  62.730 86.073  1.00 37.15 ? 152 ARG B CG  1 
ATOM   3768 C  CD  . ARG B 1 152 ? 11.271  63.689 87.265  1.00 37.13 ? 152 ARG B CD  1 
ATOM   3769 N  NE  . ARG B 1 152 ? 11.721  63.010 88.486  1.00 37.84 ? 152 ARG B NE  1 
ATOM   3770 C  CZ  . ARG B 1 152 ? 10.917  62.483 89.408  1.00 37.59 ? 152 ARG B CZ  1 
ATOM   3771 N  NH1 . ARG B 1 152 ? 9.599   62.544 89.266  1.00 37.76 ? 152 ARG B NH1 1 
ATOM   3772 N  NH2 . ARG B 1 152 ? 11.432  61.890 90.478  1.00 36.88 ? 152 ARG B NH2 1 
ATOM   3773 N  N   . PHE B 1 153 ? 13.505  58.817 85.146  1.00 36.18 ? 153 PHE B N   1 
ATOM   3774 C  CA  . PHE B 1 153 ? 14.646  57.916 85.349  1.00 35.79 ? 153 PHE B CA  1 
ATOM   3775 C  C   . PHE B 1 153 ? 15.341  57.480 84.056  1.00 35.68 ? 153 PHE B C   1 
ATOM   3776 O  O   . PHE B 1 153 ? 16.552  57.630 83.929  1.00 35.84 ? 153 PHE B O   1 
ATOM   3777 C  CB  . PHE B 1 153 ? 14.222  56.700 86.170  1.00 35.70 ? 153 PHE B CB  1 
ATOM   3778 C  CG  . PHE B 1 153 ? 15.358  55.794 86.561  1.00 35.62 ? 153 PHE B CG  1 
ATOM   3779 C  CD1 . PHE B 1 153 ? 16.188  56.116 87.636  1.00 35.77 ? 153 PHE B CD1 1 
ATOM   3780 C  CD2 . PHE B 1 153 ? 15.585  54.603 85.873  1.00 35.38 ? 153 PHE B CD2 1 
ATOM   3781 C  CE1 . PHE B 1 153 ? 17.241  55.268 88.010  1.00 35.59 ? 153 PHE B CE1 1 
ATOM   3782 C  CE2 . PHE B 1 153 ? 16.630  53.747 86.237  1.00 35.22 ? 153 PHE B CE2 1 
ATOM   3783 C  CZ  . PHE B 1 153 ? 17.459  54.080 87.310  1.00 35.44 ? 153 PHE B CZ  1 
ATOM   3784 N  N   . PHE B 1 154 ? 14.581  56.926 83.117  1.00 35.50 ? 154 PHE B N   1 
ATOM   3785 C  CA  . PHE B 1 154 ? 15.110  56.568 81.801  1.00 35.36 ? 154 PHE B CA  1 
ATOM   3786 C  C   . PHE B 1 154 ? 15.034  57.778 80.864  1.00 35.40 ? 154 PHE B C   1 
ATOM   3787 O  O   . PHE B 1 154 ? 14.109  58.586 80.959  1.00 35.43 ? 154 PHE B O   1 
ATOM   3788 C  CB  . PHE B 1 154 ? 14.328  55.387 81.198  1.00 35.33 ? 154 PHE B CB  1 
ATOM   3789 C  CG  . PHE B 1 154 ? 14.391  54.114 82.018  1.00 35.09 ? 154 PHE B CG  1 
ATOM   3790 C  CD1 . PHE B 1 154 ? 15.585  53.410 82.158  1.00 34.91 ? 154 PHE B CD1 1 
ATOM   3791 C  CD2 . PHE B 1 154 ? 13.249  53.609 82.629  1.00 34.90 ? 154 PHE B CD2 1 
ATOM   3792 C  CE1 . PHE B 1 154 ? 15.644  52.239 82.913  1.00 34.15 ? 154 PHE B CE1 1 
ATOM   3793 C  CE2 . PHE B 1 154 ? 13.300  52.437 83.384  1.00 34.21 ? 154 PHE B CE2 1 
ATOM   3794 C  CZ  . PHE B 1 154 ? 14.499  51.753 83.522  1.00 34.22 ? 154 PHE B CZ  1 
ATOM   3795 N  N   . SER B 1 155 ? 15.998  57.910 79.957  1.00 35.39 ? 155 SER B N   1 
ATOM   3796 C  CA  . SER B 1 155 ? 15.983  59.028 79.009  1.00 35.35 ? 155 SER B CA  1 
ATOM   3797 C  C   . SER B 1 155 ? 14.833  58.865 78.025  1.00 35.33 ? 155 SER B C   1 
ATOM   3798 O  O   . SER B 1 155 ? 14.257  59.845 77.560  1.00 35.47 ? 155 SER B O   1 
ATOM   3799 C  CB  . SER B 1 155 ? 17.316  59.155 78.268  1.00 35.34 ? 155 SER B CB  1 
ATOM   3800 O  OG  . SER B 1 155 ? 17.580  58.015 77.472  1.00 35.38 ? 155 SER B OG  1 
ATOM   3801 N  N   . ALA B 1 156 ? 14.513  57.610 77.725  1.00 35.28 ? 156 ALA B N   1 
ATOM   3802 C  CA  . ALA B 1 156 ? 13.401  57.239 76.859  1.00 35.01 ? 156 ALA B CA  1 
ATOM   3803 C  C   . ALA B 1 156 ? 13.082  55.778 77.131  1.00 34.90 ? 156 ALA B C   1 
ATOM   3804 O  O   . ALA B 1 156 ? 13.894  55.070 77.728  1.00 34.89 ? 156 ALA B O   1 
ATOM   3805 C  CB  . ALA B 1 156 ? 13.770  57.436 75.405  1.00 34.90 ? 156 ALA B CB  1 
ATOM   3806 N  N   . SER B 1 157 ? 11.901  55.332 76.708  1.00 34.72 ? 157 SER B N   1 
ATOM   3807 C  CA  . SER B 1 157 ? 11.508  53.931 76.854  1.00 34.57 ? 157 SER B CA  1 
ATOM   3808 C  C   . SER B 1 157 ? 10.270  53.570 76.033  1.00 34.42 ? 157 SER B C   1 
ATOM   3809 O  O   . SER B 1 157 ? 9.534   54.451 75.589  1.00 34.54 ? 157 SER B O   1 
ATOM   3810 C  CB  . SER B 1 157 ? 11.286  53.591 78.326  1.00 34.46 ? 157 SER B CB  1 
ATOM   3811 O  OG  . SER B 1 157 ? 10.867  54.731 79.055  1.00 35.04 ? 157 SER B OG  1 
ATOM   3812 N  N   . CYS B 1 158 ? 10.073  52.275 75.799  1.00 34.20 ? 158 CYS B N   1 
ATOM   3813 C  CA  . CYS B 1 158 ? 8.794   51.790 75.323  1.00 33.74 ? 158 CYS B CA  1 
ATOM   3814 C  C   . CYS B 1 158 ? 8.084   51.040 76.440  1.00 33.21 ? 158 CYS B C   1 
ATOM   3815 O  O   . CYS B 1 158 ? 8.601   50.062 76.970  1.00 33.30 ? 158 CYS B O   1 
ATOM   3816 C  CB  . CYS B 1 158 ? 8.926   50.908 74.083  1.00 34.02 ? 158 CYS B CB  1 
ATOM   3817 S  SG  . CYS B 1 158 ? 7.296   50.509 73.329  1.00 35.10 ? 158 CYS B SG  1 
ATOM   3818 N  N   . VAL B 1 159 ? 6.908   51.538 76.803  1.00 32.63 ? 159 VAL B N   1 
ATOM   3819 C  CA  . VAL B 1 159 ? 6.051   50.947 77.822  1.00 32.04 ? 159 VAL B CA  1 
ATOM   3820 C  C   . VAL B 1 159 ? 4.644   50.901 77.221  1.00 31.97 ? 159 VAL B C   1 
ATOM   3821 O  O   . VAL B 1 159 ? 3.854   51.837 77.411  1.00 31.86 ? 159 VAL B O   1 
ATOM   3822 C  CB  . VAL B 1 159 ? 6.043   51.788 79.130  1.00 31.91 ? 159 VAL B CB  1 
ATOM   3823 C  CG1 . VAL B 1 159 ? 5.359   51.036 80.258  1.00 31.29 ? 159 VAL B CG1 1 
ATOM   3824 C  CG2 . VAL B 1 159 ? 7.450   52.171 79.531  1.00 31.50 ? 159 VAL B CG2 1 
ATOM   3825 N  N   . PRO B 1 160 ? 4.332   49.830 76.462  1.00 31.72 ? 160 PRO B N   1 
ATOM   3826 C  CA  . PRO B 1 160 ? 3.031   49.724 75.814  1.00 31.52 ? 160 PRO B CA  1 
ATOM   3827 C  C   . PRO B 1 160 ? 1.911   49.821 76.825  1.00 31.78 ? 160 PRO B C   1 
ATOM   3828 O  O   . PRO B 1 160 ? 2.006   49.272 77.918  1.00 31.68 ? 160 PRO B O   1 
ATOM   3829 C  CB  . PRO B 1 160 ? 3.076   48.339 75.199  1.00 31.34 ? 160 PRO B CB  1 
ATOM   3830 C  CG  . PRO B 1 160 ? 4.518   48.099 74.961  1.00 31.11 ? 160 PRO B CG  1 
ATOM   3831 C  CD  . PRO B 1 160 ? 5.177   48.664 76.155  1.00 31.51 ? 160 PRO B CD  1 
ATOM   3832 N  N   . GLY B 1 161 ? 0.866   50.545 76.468  1.00 32.34 ? 161 GLY B N   1 
ATOM   3833 C  CA  . GLY B 1 161 ? -0.253  50.746 77.374  1.00 33.56 ? 161 GLY B CA  1 
ATOM   3834 C  C   . GLY B 1 161 ? -0.135  52.021 78.187  1.00 34.51 ? 161 GLY B C   1 
ATOM   3835 O  O   . GLY B 1 161 ? -1.138  52.539 78.690  1.00 34.76 ? 161 GLY B O   1 
ATOM   3836 N  N   . ALA B 1 162 ? 1.089   52.535 78.317  1.00 35.27 ? 162 ALA B N   1 
ATOM   3837 C  CA  . ALA B 1 162 ? 1.327   53.783 79.041  1.00 35.87 ? 162 ALA B CA  1 
ATOM   3838 C  C   . ALA B 1 162 ? 0.522   54.916 78.436  1.00 36.39 ? 162 ALA B C   1 
ATOM   3839 O  O   . ALA B 1 162 ? 0.386   55.008 77.214  1.00 36.31 ? 162 ALA B O   1 
ATOM   3840 C  CB  . ALA B 1 162 ? 2.799   54.128 79.041  1.00 35.81 ? 162 ALA B CB  1 
ATOM   3841 N  N   . ASP B 1 163 ? -0.026  55.760 79.305  1.00 37.29 ? 163 ASP B N   1 
ATOM   3842 C  CA  . ASP B 1 163 ? -0.751  56.949 78.876  1.00 38.24 ? 163 ASP B CA  1 
ATOM   3843 C  C   . ASP B 1 163 ? 0.207   57.853 78.116  1.00 38.55 ? 163 ASP B C   1 
ATOM   3844 O  O   . ASP B 1 163 ? 1.195   58.326 78.675  1.00 38.85 ? 163 ASP B O   1 
ATOM   3845 C  CB  . ASP B 1 163 ? -1.343  57.680 80.084  1.00 38.42 ? 163 ASP B CB  1 
ATOM   3846 C  CG  . ASP B 1 163 ? -2.256  58.843 79.693  1.00 39.77 ? 163 ASP B CG  1 
ATOM   3847 O  OD1 . ASP B 1 163 ? -1.945  59.589 78.736  1.00 40.69 ? 163 ASP B OD1 1 
ATOM   3848 O  OD2 . ASP B 1 163 ? -3.290  59.028 80.369  1.00 41.56 ? 163 ASP B OD2 1 
ATOM   3849 N  N   . LYS B 1 164 ? -0.088  58.078 76.839  1.00 38.88 ? 164 LYS B N   1 
ATOM   3850 C  CA  . LYS B 1 164 ? 0.790   58.854 75.972  1.00 39.22 ? 164 LYS B CA  1 
ATOM   3851 C  C   . LYS B 1 164 ? 0.615   60.355 76.201  1.00 39.11 ? 164 LYS B C   1 
ATOM   3852 O  O   . LYS B 1 164 ? 1.530   61.140 75.954  1.00 38.96 ? 164 LYS B O   1 
ATOM   3853 C  CB  . LYS B 1 164 ? 0.529   58.500 74.511  1.00 39.40 ? 164 LYS B CB  1 
ATOM   3854 C  CG  . LYS B 1 164 ? 1.778   58.520 73.637  1.00 40.42 ? 164 LYS B CG  1 
ATOM   3855 C  CD  . LYS B 1 164 ? 1.436   58.580 72.145  1.00 42.11 ? 164 LYS B CD  1 
ATOM   3856 C  CE  . LYS B 1 164 ? 0.682   57.337 71.659  1.00 42.86 ? 164 LYS B CE  1 
ATOM   3857 N  NZ  . LYS B 1 164 ? 0.427   57.362 70.182  1.00 43.18 ? 164 LYS B NZ  1 
ATOM   3858 N  N   . GLY B 1 165 ? -0.567  60.736 76.677  1.00 39.13 ? 165 GLY B N   1 
ATOM   3859 C  CA  . GLY B 1 165 ? -0.885  62.124 76.988  1.00 39.15 ? 165 GLY B CA  1 
ATOM   3860 C  C   . GLY B 1 165 ? -0.097  62.721 78.145  1.00 39.20 ? 165 GLY B C   1 
ATOM   3861 O  O   . GLY B 1 165 ? 0.273   63.890 78.094  1.00 39.23 ? 165 GLY B O   1 
ATOM   3862 N  N   . GLN B 1 166 ? 0.166   61.934 79.187  1.00 39.19 ? 166 GLN B N   1 
ATOM   3863 C  CA  . GLN B 1 166 ? 0.865   62.450 80.376  1.00 39.23 ? 166 GLN B CA  1 
ATOM   3864 C  C   . GLN B 1 166 ? 2.324   62.009 80.459  1.00 38.82 ? 166 GLN B C   1 
ATOM   3865 O  O   . GLN B 1 166 ? 3.134   62.646 81.130  1.00 38.63 ? 166 GLN B O   1 
ATOM   3866 C  CB  . GLN B 1 166 ? 0.153   62.028 81.664  1.00 39.48 ? 166 GLN B CB  1 
ATOM   3867 C  CG  . GLN B 1 166 ? -1.359  62.194 81.660  1.00 40.98 ? 166 GLN B CG  1 
ATOM   3868 C  CD  . GLN B 1 166 ? -2.044  61.256 82.645  1.00 42.57 ? 166 GLN B CD  1 
ATOM   3869 O  OE1 . GLN B 1 166 ? -1.480  60.916 83.690  1.00 43.16 ? 166 GLN B OE1 1 
ATOM   3870 N  NE2 . GLN B 1 166 ? -3.266  60.832 82.315  1.00 42.53 ? 166 GLN B NE2 1 
ATOM   3871 N  N   . PHE B 1 167 ? 2.652   60.903 79.799  1.00 38.55 ? 167 PHE B N   1 
ATOM   3872 C  CA  . PHE B 1 167 ? 4.000   60.348 79.870  1.00 38.27 ? 167 PHE B CA  1 
ATOM   3873 C  C   . PHE B 1 167 ? 4.534   60.061 78.469  1.00 38.25 ? 167 PHE B C   1 
ATOM   3874 O  O   . PHE B 1 167 ? 4.751   58.908 78.122  1.00 38.25 ? 167 PHE B O   1 
ATOM   3875 C  CB  . PHE B 1 167 ? 4.014   59.072 80.726  1.00 37.97 ? 167 PHE B CB  1 
ATOM   3876 C  CG  . PHE B 1 167 ? 3.178   59.165 81.975  1.00 37.80 ? 167 PHE B CG  1 
ATOM   3877 C  CD1 . PHE B 1 167 ? 3.635   59.863 83.088  1.00 37.43 ? 167 PHE B CD1 1 
ATOM   3878 C  CD2 . PHE B 1 167 ? 1.929   58.561 82.038  1.00 37.41 ? 167 PHE B CD2 1 
ATOM   3879 C  CE1 . PHE B 1 167 ? 2.858   59.958 84.240  1.00 36.99 ? 167 PHE B CE1 1 
ATOM   3880 C  CE2 . PHE B 1 167 ? 1.148   58.654 83.190  1.00 37.07 ? 167 PHE B CE2 1 
ATOM   3881 C  CZ  . PHE B 1 167 ? 1.612   59.353 84.288  1.00 37.01 ? 167 PHE B CZ  1 
ATOM   3882 N  N   . PRO B 1 168 ? 4.774   61.114 77.661  1.00 38.45 ? 168 PRO B N   1 
ATOM   3883 C  CA  . PRO B 1 168 ? 5.165   60.854 76.270  1.00 38.57 ? 168 PRO B CA  1 
ATOM   3884 C  C   . PRO B 1 168 ? 6.546   60.211 76.187  1.00 38.67 ? 168 PRO B C   1 
ATOM   3885 O  O   . PRO B 1 168 ? 6.930   59.692 75.135  1.00 39.03 ? 168 PRO B O   1 
ATOM   3886 C  CB  . PRO B 1 168 ? 5.186   62.252 75.637  1.00 38.51 ? 168 PRO B CB  1 
ATOM   3887 C  CG  . PRO B 1 168 ? 5.401   63.189 76.775  1.00 38.36 ? 168 PRO B CG  1 
ATOM   3888 C  CD  . PRO B 1 168 ? 4.740   62.559 77.968  1.00 38.46 ? 168 PRO B CD  1 
ATOM   3889 N  N   . ASN B 1 169 ? 7.262   60.239 77.309  1.00 38.58 ? 169 ASN B N   1 
ATOM   3890 C  CA  . ASN B 1 169 ? 8.638   59.774 77.402  1.00 38.40 ? 169 ASN B CA  1 
ATOM   3891 C  C   . ASN B 1 169 ? 8.727   58.263 77.628  1.00 38.15 ? 169 ASN B C   1 
ATOM   3892 O  O   . ASN B 1 169 ? 9.794   57.659 77.491  1.00 38.02 ? 169 ASN B O   1 
ATOM   3893 C  CB  . ASN B 1 169 ? 9.354   60.540 78.519  1.00 38.49 ? 169 ASN B CB  1 
ATOM   3894 C  CG  . ASN B 1 169 ? 10.847  60.578 78.325  1.00 38.82 ? 169 ASN B CG  1 
ATOM   3895 O  OD1 . ASN B 1 169 ? 11.345  61.217 77.401  1.00 39.03 ? 169 ASN B OD1 1 
ATOM   3896 N  ND2 . ASN B 1 169 ? 11.574  59.885 79.192  1.00 39.75 ? 169 ASN B ND2 1 
ATOM   3897 N  N   . LEU B 1 170 ? 7.592   57.667 77.982  1.00 37.96 ? 170 LEU B N   1 
ATOM   3898 C  CA  . LEU B 1 170 ? 7.473   56.227 78.126  1.00 37.79 ? 170 LEU B CA  1 
ATOM   3899 C  C   . LEU B 1 170 ? 6.995   55.600 76.829  1.00 38.02 ? 170 LEU B C   1 
ATOM   3900 O  O   . LEU B 1 170 ? 6.895   54.386 76.729  1.00 37.97 ? 170 LEU B O   1 
ATOM   3901 C  CB  . LEU B 1 170 ? 6.495   55.875 79.244  1.00 37.58 ? 170 LEU B CB  1 
ATOM   3902 C  CG  . LEU B 1 170 ? 6.831   56.200 80.700  1.00 37.30 ? 170 LEU B CG  1 
ATOM   3903 C  CD1 . LEU B 1 170 ? 5.700   55.718 81.591  1.00 36.94 ? 170 LEU B CD1 1 
ATOM   3904 C  CD2 . LEU B 1 170 ? 8.162   55.603 81.144  1.00 36.42 ? 170 LEU B CD2 1 
ATOM   3905 N  N   . CYS B 1 171 ? 6.697   56.427 75.836  1.00 38.50 ? 171 CYS B N   1 
ATOM   3906 C  CA  . CYS B 1 171 ? 6.231   55.926 74.552  1.00 39.23 ? 171 CYS B CA  1 
ATOM   3907 C  C   . CYS B 1 171 ? 7.154   56.270 73.398  1.00 39.22 ? 171 CYS B C   1 
ATOM   3908 O  O   . CYS B 1 171 ? 7.018   55.700 72.308  1.00 39.40 ? 171 CYS B O   1 
ATOM   3909 C  CB  . CYS B 1 171 ? 4.824   56.431 74.251  1.00 39.30 ? 171 CYS B CB  1 
ATOM   3910 S  SG  . CYS B 1 171 ? 3.569   55.702 75.315  1.00 41.73 ? 171 CYS B SG  1 
ATOM   3911 N  N   . ARG B 1 172 ? 8.088   57.191 73.643  1.00 39.06 ? 172 ARG B N   1 
ATOM   3912 C  CA  . ARG B 1 172 ? 8.971   57.715 72.601  1.00 39.26 ? 172 ARG B CA  1 
ATOM   3913 C  C   . ARG B 1 172 ? 9.632   56.601 71.797  1.00 38.75 ? 172 ARG B C   1 
ATOM   3914 O  O   . ARG B 1 172 ? 9.658   56.652 70.562  1.00 38.70 ? 172 ARG B O   1 
ATOM   3915 C  CB  . ARG B 1 172 ? 10.035  58.643 73.199  1.00 39.17 ? 172 ARG B CB  1 
ATOM   3916 C  CG  . ARG B 1 172 ? 10.775  59.494 72.160  1.00 39.96 ? 172 ARG B CG  1 
ATOM   3917 C  CD  . ARG B 1 172 ? 11.832  60.428 72.789  1.00 40.48 ? 172 ARG B CD  1 
ATOM   3918 N  NE  . ARG B 1 172 ? 11.350  61.080 74.014  1.00 43.08 ? 172 ARG B NE  1 
ATOM   3919 C  CZ  . ARG B 1 172 ? 10.462  62.075 74.056  1.00 43.35 ? 172 ARG B CZ  1 
ATOM   3920 N  NH1 . ARG B 1 172 ? 9.933   62.564 72.936  1.00 43.53 ? 172 ARG B NH1 1 
ATOM   3921 N  NH2 . ARG B 1 172 ? 10.093  62.578 75.228  1.00 43.16 ? 172 ARG B NH2 1 
ATOM   3922 N  N   . LEU B 1 173 ? 10.132  55.591 72.511  1.00 38.33 ? 173 LEU B N   1 
ATOM   3923 C  CA  . LEU B 1 173 ? 10.883  54.483 71.913  1.00 37.97 ? 173 LEU B CA  1 
ATOM   3924 C  C   . LEU B 1 173 ? 10.075  53.493 71.083  1.00 37.85 ? 173 LEU B C   1 
ATOM   3925 O  O   . LEU B 1 173 ? 10.656  52.704 70.341  1.00 37.87 ? 173 LEU B O   1 
ATOM   3926 C  CB  . LEU B 1 173 ? 11.650  53.712 72.985  1.00 37.68 ? 173 LEU B CB  1 
ATOM   3927 C  CG  . LEU B 1 173 ? 13.002  54.240 73.451  1.00 37.74 ? 173 LEU B CG  1 
ATOM   3928 C  CD1 . LEU B 1 173 ? 13.848  53.053 73.851  1.00 38.06 ? 173 LEU B CD1 1 
ATOM   3929 C  CD2 . LEU B 1 173 ? 13.728  55.081 72.393  1.00 37.80 ? 173 LEU B CD2 1 
ATOM   3930 N  N   . CYS B 1 174 ? 8.751   53.530 71.204  1.00 37.82 ? 174 CYS B N   1 
ATOM   3931 C  CA  . CYS B 1 174 ? 7.893   52.545 70.546  1.00 37.98 ? 174 CYS B CA  1 
ATOM   3932 C  C   . CYS B 1 174 ? 7.884   52.635 69.010  1.00 38.10 ? 174 CYS B C   1 
ATOM   3933 O  O   . CYS B 1 174 ? 8.204   53.683 68.428  1.00 38.10 ? 174 CYS B O   1 
ATOM   3934 C  CB  . CYS B 1 174 ? 6.482   52.596 71.130  1.00 37.80 ? 174 CYS B CB  1 
ATOM   3935 S  SG  . CYS B 1 174 ? 6.424   52.351 72.946  1.00 38.72 ? 174 CYS B SG  1 
ATOM   3936 N  N   . ALA B 1 175 ? 7.523   51.525 68.369  1.00 38.27 ? 175 ALA B N   1 
ATOM   3937 C  CA  . ALA B 1 175 ? 7.644   51.377 66.922  1.00 38.52 ? 175 ALA B CA  1 
ATOM   3938 C  C   . ALA B 1 175 ? 6.312   51.467 66.180  1.00 38.94 ? 175 ALA B C   1 
ATOM   3939 O  O   . ALA B 1 175 ? 6.286   51.513 64.950  1.00 39.14 ? 175 ALA B O   1 
ATOM   3940 C  CB  . ALA B 1 175 ? 8.353   50.073 66.587  1.00 38.31 ? 175 ALA B CB  1 
ATOM   3941 N  N   . GLY B 1 176 ? 5.209   51.498 66.918  1.00 39.50 ? 176 GLY B N   1 
ATOM   3942 C  CA  . GLY B 1 176 ? 3.876   51.519 66.310  1.00 40.23 ? 176 GLY B CA  1 
ATOM   3943 C  C   . GLY B 1 176 ? 3.634   52.697 65.385  1.00 40.77 ? 176 GLY B C   1 
ATOM   3944 O  O   . GLY B 1 176 ? 4.275   53.744 65.513  1.00 40.71 ? 176 GLY B O   1 
ATOM   3945 N  N   . THR B 1 177 ? 2.703   52.523 64.452  1.00 41.31 ? 177 THR B N   1 
ATOM   3946 C  CA  . THR B 1 177 ? 2.370   53.574 63.495  1.00 42.04 ? 177 THR B CA  1 
ATOM   3947 C  C   . THR B 1 177 ? 1.174   54.383 63.980  1.00 42.18 ? 177 THR B C   1 
ATOM   3948 O  O   . THR B 1 177 ? 0.166   53.812 64.396  1.00 42.17 ? 177 THR B O   1 
ATOM   3949 C  CB  . THR B 1 177 ? 2.042   52.988 62.104  1.00 42.16 ? 177 THR B CB  1 
ATOM   3950 O  OG1 . THR B 1 177 ? 2.750   51.756 61.924  1.00 43.14 ? 177 THR B OG1 1 
ATOM   3951 C  CG2 . THR B 1 177 ? 2.421   53.965 60.992  1.00 42.09 ? 177 THR B CG2 1 
ATOM   3952 N  N   . GLY B 1 178 ? 1.299   55.710 63.924  1.00 42.47 ? 178 GLY B N   1 
ATOM   3953 C  CA  . GLY B 1 178 ? 0.208   56.633 64.266  1.00 42.78 ? 178 GLY B CA  1 
ATOM   3954 C  C   . GLY B 1 178 ? -0.474  56.355 65.597  1.00 42.93 ? 178 GLY B C   1 
ATOM   3955 O  O   . GLY B 1 178 ? 0.173   56.357 66.643  1.00 43.08 ? 178 GLY B O   1 
ATOM   3956 N  N   . GLU B 1 179 ? -1.781  56.100 65.552  1.00 42.94 ? 179 GLU B N   1 
ATOM   3957 C  CA  . GLU B 1 179 ? -2.570  55.864 66.767  1.00 43.05 ? 179 GLU B CA  1 
ATOM   3958 C  C   . GLU B 1 179 ? -2.358  54.476 67.357  1.00 42.60 ? 179 GLU B C   1 
ATOM   3959 O  O   . GLU B 1 179 ? -2.961  54.131 68.367  1.00 42.69 ? 179 GLU B O   1 
ATOM   3960 C  CB  . GLU B 1 179 ? -4.064  56.135 66.529  1.00 43.29 ? 179 GLU B CB  1 
ATOM   3961 C  CG  . GLU B 1 179 ? -4.393  57.589 66.092  1.00 45.21 ? 179 GLU B CG  1 
ATOM   3962 C  CD  . GLU B 1 179 ? -3.771  58.676 66.991  1.00 46.93 ? 179 GLU B CD  1 
ATOM   3963 O  OE1 . GLU B 1 179 ? -2.968  59.494 66.480  1.00 47.58 ? 179 GLU B OE1 1 
ATOM   3964 O  OE2 . GLU B 1 179 ? -4.087  58.719 68.201  1.00 47.39 ? 179 GLU B OE2 1 
ATOM   3965 N  N   . ASN B 1 180 ? -1.491  53.690 66.731  1.00 42.18 ? 180 ASN B N   1 
ATOM   3966 C  CA  . ASN B 1 180 ? -1.110  52.385 67.256  1.00 41.72 ? 180 ASN B CA  1 
ATOM   3967 C  C   . ASN B 1 180 ? 0.234   52.413 67.969  1.00 41.25 ? 180 ASN B C   1 
ATOM   3968 O  O   . ASN B 1 180 ? 0.681   51.398 68.499  1.00 41.19 ? 180 ASN B O   1 
ATOM   3969 C  CB  . ASN B 1 180 ? -1.086  51.344 66.138  1.00 41.98 ? 180 ASN B CB  1 
ATOM   3970 C  CG  . ASN B 1 180 ? -2.471  50.897 65.734  1.00 42.30 ? 180 ASN B CG  1 
ATOM   3971 O  OD1 . ASN B 1 180 ? -3.190  50.276 66.522  1.00 42.95 ? 180 ASN B OD1 1 
ATOM   3972 N  ND2 . ASN B 1 180 ? -2.854  51.204 64.499  1.00 42.56 ? 180 ASN B ND2 1 
ATOM   3973 N  N   . LYS B 1 181 ? 0.876   53.578 67.973  1.00 40.80 ? 181 LYS B N   1 
ATOM   3974 C  CA  . LYS B 1 181 ? 2.133   53.761 68.686  1.00 40.36 ? 181 LYS B CA  1 
ATOM   3975 C  C   . LYS B 1 181 ? 1.893   53.601 70.185  1.00 39.93 ? 181 LYS B C   1 
ATOM   3976 O  O   . LYS B 1 181 ? 0.992   54.229 70.745  1.00 39.85 ? 181 LYS B O   1 
ATOM   3977 C  CB  . LYS B 1 181 ? 2.727   55.134 68.367  1.00 40.51 ? 181 LYS B CB  1 
ATOM   3978 C  CG  . LYS B 1 181 ? 4.160   55.324 68.824  1.00 41.07 ? 181 LYS B CG  1 
ATOM   3979 C  CD  . LYS B 1 181 ? 4.800   56.525 68.156  1.00 42.14 ? 181 LYS B CD  1 
ATOM   3980 C  CE  . LYS B 1 181 ? 6.316   56.528 68.358  1.00 43.13 ? 181 LYS B CE  1 
ATOM   3981 N  NZ  . LYS B 1 181 ? 6.979   57.665 67.641  1.00 43.86 ? 181 LYS B NZ  1 
ATOM   3982 N  N   . CYS B 1 182 ? 2.677   52.726 70.815  1.00 39.53 ? 182 CYS B N   1 
ATOM   3983 C  CA  . CYS B 1 182 ? 2.635   52.509 72.270  1.00 38.97 ? 182 CYS B CA  1 
ATOM   3984 C  C   . CYS B 1 182 ? 1.315   51.894 72.768  1.00 38.24 ? 182 CYS B C   1 
ATOM   3985 O  O   . CYS B 1 182 ? 1.002   51.960 73.961  1.00 38.03 ? 182 CYS B O   1 
ATOM   3986 C  CB  . CYS B 1 182 ? 2.946   53.826 72.996  1.00 39.29 ? 182 CYS B CB  1 
ATOM   3987 S  SG  . CYS B 1 182 ? 3.415   53.718 74.733  1.00 39.86 ? 182 CYS B SG  1 
ATOM   3988 N  N   . ALA B 1 183 ? 0.563   51.290 71.847  1.00 37.37 ? 183 ALA B N   1 
ATOM   3989 C  CA  . ALA B 1 183 ? -0.684  50.589 72.162  1.00 36.74 ? 183 ALA B CA  1 
ATOM   3990 C  C   . ALA B 1 183 ? -0.424  49.284 72.895  1.00 36.28 ? 183 ALA B C   1 
ATOM   3991 O  O   . ALA B 1 183 ? 0.577   48.622 72.652  1.00 36.43 ? 183 ALA B O   1 
ATOM   3992 C  CB  . ALA B 1 183 ? -1.464  50.313 70.892  1.00 36.83 ? 183 ALA B CB  1 
ATOM   3993 N  N   . PHE B 1 184 ? -1.333  48.898 73.780  1.00 35.76 ? 184 PHE B N   1 
ATOM   3994 C  CA  . PHE B 1 184 ? -1.183  47.644 74.516  1.00 35.23 ? 184 PHE B CA  1 
ATOM   3995 C  C   . PHE B 1 184 ? -1.679  46.453 73.694  1.00 35.08 ? 184 PHE B C   1 
ATOM   3996 O  O   . PHE B 1 184 ? -2.658  45.816 74.067  1.00 35.20 ? 184 PHE B O   1 
ATOM   3997 C  CB  . PHE B 1 184 ? -1.938  47.731 75.844  1.00 35.11 ? 184 PHE B CB  1 
ATOM   3998 C  CG  . PHE B 1 184 ? -1.499  46.727 76.862  1.00 35.02 ? 184 PHE B CG  1 
ATOM   3999 C  CD1 . PHE B 1 184 ? -0.445  47.009 77.720  1.00 35.20 ? 184 PHE B CD1 1 
ATOM   4000 C  CD2 . PHE B 1 184 ? -2.144  45.502 76.978  1.00 35.36 ? 184 PHE B CD2 1 
ATOM   4001 C  CE1 . PHE B 1 184 ? -0.034  46.080 78.666  1.00 35.15 ? 184 PHE B CE1 1 
ATOM   4002 C  CE2 . PHE B 1 184 ? -1.744  44.567 77.926  1.00 34.89 ? 184 PHE B CE2 1 
ATOM   4003 C  CZ  . PHE B 1 184 ? -0.689  44.855 78.769  1.00 35.01 ? 184 PHE B CZ  1 
ATOM   4004 N  N   . SER B 1 185 ? -1.002  46.156 72.582  1.00 34.84 ? 185 SER B N   1 
ATOM   4005 C  CA  . SER B 1 185 ? -1.436  45.105 71.652  1.00 34.82 ? 185 SER B CA  1 
ATOM   4006 C  C   . SER B 1 185 ? -0.404  44.832 70.561  1.00 34.99 ? 185 SER B C   1 
ATOM   4007 O  O   . SER B 1 185 ? 0.575   45.562 70.439  1.00 35.26 ? 185 SER B O   1 
ATOM   4008 C  CB  . SER B 1 185 ? -2.762  45.485 70.985  1.00 34.93 ? 185 SER B CB  1 
ATOM   4009 O  OG  . SER B 1 185 ? -2.552  46.401 69.922  1.00 34.47 ? 185 SER B OG  1 
ATOM   4010 N  N   . SER B 1 186 ? -0.657  43.800 69.750  1.00 35.04 ? 186 SER B N   1 
ATOM   4011 C  CA  . SER B 1 186 ? 0.236   43.391 68.658  1.00 35.08 ? 186 SER B CA  1 
ATOM   4012 C  C   . SER B 1 186 ? 0.419   44.441 67.569  1.00 34.96 ? 186 SER B C   1 
ATOM   4013 O  O   . SER B 1 186 ? 1.378   44.372 66.803  1.00 35.07 ? 186 SER B O   1 
ATOM   4014 C  CB  . SER B 1 186 ? -0.254  42.094 68.030  1.00 35.16 ? 186 SER B CB  1 
ATOM   4015 O  OG  . SER B 1 186 ? -0.038  41.020 68.927  1.00 36.22 ? 186 SER B OG  1 
ATOM   4016 N  N   . GLN B 1 187 ? -0.507  45.394 67.499  1.00 34.74 ? 187 GLN B N   1 
ATOM   4017 C  CA  . GLN B 1 187 ? -0.386  46.563 66.624  1.00 34.69 ? 187 GLN B CA  1 
ATOM   4018 C  C   . GLN B 1 187 ? 0.915   47.341 66.887  1.00 34.07 ? 187 GLN B C   1 
ATOM   4019 O  O   . GLN B 1 187 ? 1.461   47.984 65.985  1.00 33.92 ? 187 GLN B O   1 
ATOM   4020 C  CB  . GLN B 1 187 ? -1.580  47.510 66.828  1.00 35.16 ? 187 GLN B CB  1 
ATOM   4021 C  CG  . GLN B 1 187 ? -2.962  46.857 66.772  1.00 36.71 ? 187 GLN B CG  1 
ATOM   4022 C  CD  . GLN B 1 187 ? -3.480  46.697 65.359  1.00 39.43 ? 187 GLN B CD  1 
ATOM   4023 O  OE1 . GLN B 1 187 ? -2.728  46.824 64.387  1.00 41.20 ? 187 GLN B OE1 1 
ATOM   4024 N  NE2 . GLN B 1 187 ? -4.779  46.423 65.231  1.00 40.56 ? 187 GLN B NE2 1 
ATOM   4025 N  N   . GLU B 1 188 ? 1.383   47.302 68.136  1.00 33.20 ? 188 GLU B N   1 
ATOM   4026 C  CA  . GLU B 1 188 ? 2.681   47.846 68.494  1.00 32.34 ? 188 GLU B CA  1 
ATOM   4027 C  C   . GLU B 1 188 ? 3.689   46.715 68.372  1.00 31.94 ? 188 GLU B C   1 
ATOM   4028 O  O   . GLU B 1 188 ? 3.599   45.738 69.101  1.00 32.05 ? 188 GLU B O   1 
ATOM   4029 C  CB  . GLU B 1 188 ? 2.646   48.401 69.917  1.00 32.30 ? 188 GLU B CB  1 
ATOM   4030 C  CG  . GLU B 1 188 ? 4.015   48.663 70.559  1.00 31.75 ? 188 GLU B CG  1 
ATOM   4031 C  CD  . GLU B 1 188 ? 4.838   49.696 69.819  1.00 30.16 ? 188 GLU B CD  1 
ATOM   4032 O  OE1 . GLU B 1 188 ? 4.308   50.783 69.533  1.00 30.38 ? 188 GLU B OE1 1 
ATOM   4033 O  OE2 . GLU B 1 188 ? 6.017   49.423 69.533  1.00 29.06 ? 188 GLU B OE2 1 
ATOM   4034 N  N   . PRO B 1 189 ? 4.630   46.818 67.419  1.00 31.59 ? 189 PRO B N   1 
ATOM   4035 C  CA  . PRO B 1 189 ? 5.577   45.720 67.232  1.00 31.32 ? 189 PRO B CA  1 
ATOM   4036 C  C   . PRO B 1 189 ? 6.502   45.466 68.423  1.00 31.10 ? 189 PRO B C   1 
ATOM   4037 O  O   . PRO B 1 189 ? 7.106   44.397 68.484  1.00 31.40 ? 189 PRO B O   1 
ATOM   4038 C  CB  . PRO B 1 189 ? 6.379   46.146 65.992  1.00 31.42 ? 189 PRO B CB  1 
ATOM   4039 C  CG  . PRO B 1 189 ? 5.524   47.175 65.312  1.00 31.41 ? 189 PRO B CG  1 
ATOM   4040 C  CD  . PRO B 1 189 ? 4.847   47.894 66.437  1.00 31.58 ? 189 PRO B CD  1 
ATOM   4041 N  N   . TYR B 1 190 ? 6.607   46.413 69.358  1.00 30.57 ? 190 TYR B N   1 
ATOM   4042 C  CA  . TYR B 1 190 ? 7.420   46.195 70.565  1.00 30.26 ? 190 TYR B CA  1 
ATOM   4043 C  C   . TYR B 1 190 ? 6.626   45.721 71.790  1.00 29.94 ? 190 TYR B C   1 
ATOM   4044 O  O   . TYR B 1 190 ? 7.123   45.772 72.914  1.00 29.90 ? 190 TYR B O   1 
ATOM   4045 C  CB  . TYR B 1 190 ? 8.254   47.433 70.940  1.00 30.37 ? 190 TYR B CB  1 
ATOM   4046 C  CG  . TYR B 1 190 ? 9.335   47.829 69.951  1.00 30.38 ? 190 TYR B CG  1 
ATOM   4047 C  CD1 . TYR B 1 190 ? 9.757   46.955 68.946  1.00 30.56 ? 190 TYR B CD1 1 
ATOM   4048 C  CD2 . TYR B 1 190 ? 9.956   49.074 70.046  1.00 29.92 ? 190 TYR B CD2 1 
ATOM   4049 C  CE1 . TYR B 1 190 ? 10.745  47.323 68.047  1.00 30.67 ? 190 TYR B CE1 1 
ATOM   4050 C  CE2 . TYR B 1 190 ? 10.949  49.448 69.160  1.00 30.47 ? 190 TYR B CE2 1 
ATOM   4051 C  CZ  . TYR B 1 190 ? 11.338  48.570 68.159  1.00 30.61 ? 190 TYR B CZ  1 
ATOM   4052 O  OH  . TYR B 1 190 ? 12.324  48.936 67.274  1.00 29.99 ? 190 TYR B OH  1 
ATOM   4053 N  N   . PHE B 1 191 ? 5.403   45.255 71.563  1.00 29.58 ? 191 PHE B N   1 
ATOM   4054 C  CA  . PHE B 1 191 ? 4.529   44.782 72.635  1.00 29.27 ? 191 PHE B CA  1 
ATOM   4055 C  C   . PHE B 1 191 ? 4.862   43.351 73.031  1.00 29.19 ? 191 PHE B C   1 
ATOM   4056 O  O   . PHE B 1 191 ? 5.306   42.547 72.205  1.00 29.25 ? 191 PHE B O   1 
ATOM   4057 C  CB  . PHE B 1 191 ? 3.063   44.898 72.208  1.00 29.00 ? 191 PHE B CB  1 
ATOM   4058 C  CG  . PHE B 1 191 ? 2.091   44.240 73.146  1.00 28.91 ? 191 PHE B CG  1 
ATOM   4059 C  CD1 . PHE B 1 191 ? 1.680   44.881 74.312  1.00 29.27 ? 191 PHE B CD1 1 
ATOM   4060 C  CD2 . PHE B 1 191 ? 1.572   42.979 72.859  1.00 28.30 ? 191 PHE B CD2 1 
ATOM   4061 C  CE1 . PHE B 1 191 ? 0.760   44.268 75.180  1.00 28.74 ? 191 PHE B CE1 1 
ATOM   4062 C  CE2 . PHE B 1 191 ? 0.666   42.361 73.718  1.00 27.35 ? 191 PHE B CE2 1 
ATOM   4063 C  CZ  . PHE B 1 191 ? 0.259   43.011 74.878  1.00 28.21 ? 191 PHE B CZ  1 
ATOM   4064 N  N   . SER B 1 192 ? 4.636   43.056 74.308  1.00 28.99 ? 192 SER B N   1 
ATOM   4065 C  CA  . SER B 1 192 ? 4.903   41.747 74.916  1.00 28.89 ? 192 SER B CA  1 
ATOM   4066 C  C   . SER B 1 192 ? 6.362   41.297 74.880  1.00 28.73 ? 192 SER B C   1 
ATOM   4067 O  O   . SER B 1 192 ? 7.225   41.993 74.348  1.00 28.90 ? 192 SER B O   1 
ATOM   4068 C  CB  . SER B 1 192 ? 4.005   40.661 74.338  1.00 28.85 ? 192 SER B CB  1 
ATOM   4069 O  OG  . SER B 1 192 ? 4.020   39.541 75.201  1.00 29.35 ? 192 SER B OG  1 
ATOM   4070 N  N   . TYR B 1 193 ? 6.619   40.127 75.458  1.00 28.45 ? 193 TYR B N   1 
ATOM   4071 C  CA  . TYR B 1 193 ? 7.967   39.589 75.585  1.00 28.37 ? 193 TYR B CA  1 
ATOM   4072 C  C   . TYR B 1 193 ? 8.802   39.798 74.324  1.00 28.60 ? 193 TYR B C   1 
ATOM   4073 O  O   . TYR B 1 193 ? 9.810   40.507 74.329  1.00 28.27 ? 193 TYR B O   1 
ATOM   4074 C  CB  . TYR B 1 193 ? 7.903   38.097 75.903  1.00 28.07 ? 193 TYR B CB  1 
ATOM   4075 C  CG  . TYR B 1 193 ? 7.278   37.729 77.234  1.00 27.42 ? 193 TYR B CG  1 
ATOM   4076 C  CD1 . TYR B 1 193 ? 7.808   38.190 78.428  1.00 26.86 ? 193 TYR B CD1 1 
ATOM   4077 C  CD2 . TYR B 1 193 ? 6.180   36.873 77.294  1.00 27.35 ? 193 TYR B CD2 1 
ATOM   4078 C  CE1 . TYR B 1 193 ? 7.242   37.830 79.650  1.00 27.63 ? 193 TYR B CE1 1 
ATOM   4079 C  CE2 . TYR B 1 193 ? 5.611   36.506 78.510  1.00 26.98 ? 193 TYR B CE2 1 
ATOM   4080 C  CZ  . TYR B 1 193 ? 6.147   36.982 79.686  1.00 27.27 ? 193 TYR B CZ  1 
ATOM   4081 O  OH  . TYR B 1 193 ? 5.593   36.624 80.900  1.00 27.10 ? 193 TYR B OH  1 
ATOM   4082 N  N   . SER B 1 194 ? 8.343   39.187 73.238  1.00 29.18 ? 194 SER B N   1 
ATOM   4083 C  CA  . SER B 1 194 ? 9.042   39.210 71.957  1.00 29.53 ? 194 SER B CA  1 
ATOM   4084 C  C   . SER B 1 194 ? 9.279   40.627 71.421  1.00 29.56 ? 194 SER B C   1 
ATOM   4085 O  O   . SER B 1 194 ? 10.338  40.919 70.848  1.00 29.73 ? 194 SER B O   1 
ATOM   4086 C  CB  . SER B 1 194 ? 8.248   38.393 70.938  1.00 29.53 ? 194 SER B CB  1 
ATOM   4087 O  OG  . SER B 1 194 ? 9.056   38.080 69.823  1.00 29.89 ? 194 SER B OG  1 
ATOM   4088 N  N   . GLY B 1 195 ? 8.284   41.493 71.608  1.00 29.46 ? 195 GLY B N   1 
ATOM   4089 C  CA  . GLY B 1 195 ? 8.344   42.856 71.118  1.00 29.12 ? 195 GLY B CA  1 
ATOM   4090 C  C   . GLY B 1 195 ? 9.388   43.652 71.854  1.00 29.10 ? 195 GLY B C   1 
ATOM   4091 O  O   . GLY B 1 195 ? 10.097  44.442 71.254  1.00 29.30 ? 195 GLY B O   1 
ATOM   4092 N  N   . ALA B 1 196 ? 9.484   43.444 73.161  1.00 29.23 ? 196 ALA B N   1 
ATOM   4093 C  CA  . ALA B 1 196 ? 10.444  44.176 73.977  1.00 29.32 ? 196 ALA B CA  1 
ATOM   4094 C  C   . ALA B 1 196 ? 11.867  43.751 73.654  1.00 29.58 ? 196 ALA B C   1 
ATOM   4095 O  O   . ALA B 1 196 ? 12.759  44.594 73.573  1.00 29.94 ? 196 ALA B O   1 
ATOM   4096 C  CB  . ALA B 1 196 ? 10.154  43.999 75.445  1.00 29.20 ? 196 ALA B CB  1 
ATOM   4097 N  N   . PHE B 1 197 ? 12.086  42.453 73.462  1.00 29.73 ? 197 PHE B N   1 
ATOM   4098 C  CA  . PHE B 1 197 ? 13.392  41.975 73.008  1.00 29.80 ? 197 PHE B CA  1 
ATOM   4099 C  C   . PHE B 1 197 ? 13.764  42.634 71.664  1.00 30.27 ? 197 PHE B C   1 
ATOM   4100 O  O   . PHE B 1 197 ? 14.901  43.083 71.474  1.00 30.46 ? 197 PHE B O   1 
ATOM   4101 C  CB  . PHE B 1 197 ? 13.420  40.438 72.927  1.00 29.35 ? 197 PHE B CB  1 
ATOM   4102 C  CG  . PHE B 1 197 ? 14.796  39.851 72.668  1.00 28.69 ? 197 PHE B CG  1 
ATOM   4103 C  CD1 . PHE B 1 197 ? 15.901  40.243 73.423  1.00 28.29 ? 197 PHE B CD1 1 
ATOM   4104 C  CD2 . PHE B 1 197 ? 14.977  38.886 71.683  1.00 27.89 ? 197 PHE B CD2 1 
ATOM   4105 C  CE1 . PHE B 1 197 ? 17.164  39.699 73.183  1.00 28.27 ? 197 PHE B CE1 1 
ATOM   4106 C  CE2 . PHE B 1 197 ? 16.229  38.334 71.444  1.00 27.77 ? 197 PHE B CE2 1 
ATOM   4107 C  CZ  . PHE B 1 197 ? 17.325  38.743 72.191  1.00 28.21 ? 197 PHE B CZ  1 
ATOM   4108 N  N   . LYS B 1 198 ? 12.793  42.716 70.756  1.00 30.50 ? 198 LYS B N   1 
ATOM   4109 C  CA  . LYS B 1 198 ? 12.995  43.339 69.459  1.00 30.96 ? 198 LYS B CA  1 
ATOM   4110 C  C   . LYS B 1 198 ? 13.369  44.809 69.597  1.00 30.86 ? 198 LYS B C   1 
ATOM   4111 O  O   . LYS B 1 198 ? 14.240  45.297 68.879  1.00 30.80 ? 198 LYS B O   1 
ATOM   4112 C  CB  . LYS B 1 198 ? 11.741  43.190 68.608  1.00 31.28 ? 198 LYS B CB  1 
ATOM   4113 C  CG  . LYS B 1 198 ? 11.955  43.475 67.135  1.00 33.04 ? 198 LYS B CG  1 
ATOM   4114 C  CD  . LYS B 1 198 ? 10.666  43.278 66.363  1.00 36.04 ? 198 LYS B CD  1 
ATOM   4115 C  CE  . LYS B 1 198 ? 10.814  43.739 64.927  1.00 38.23 ? 198 LYS B CE  1 
ATOM   4116 N  NZ  . LYS B 1 198 ? 9.606   43.333 64.159  1.00 39.76 ? 198 LYS B NZ  1 
ATOM   4117 N  N   . CYS B 1 199 ? 12.712  45.502 70.523  1.00 31.03 ? 199 CYS B N   1 
ATOM   4118 C  CA  . CYS B 1 199 ? 13.045  46.884 70.856  1.00 31.18 ? 199 CYS B CA  1 
ATOM   4119 C  C   . CYS B 1 199 ? 14.530  47.045 71.180  1.00 31.26 ? 199 CYS B C   1 
ATOM   4120 O  O   . CYS B 1 199 ? 15.113  48.098 70.916  1.00 31.31 ? 199 CYS B O   1 
ATOM   4121 C  CB  . CYS B 1 199 ? 12.181  47.371 72.021  1.00 31.33 ? 199 CYS B CB  1 
ATOM   4122 S  SG  . CYS B 1 199 ? 12.707  48.910 72.863  1.00 31.55 ? 199 CYS B SG  1 
ATOM   4123 N  N   . LEU B 1 200 ? 15.132  45.996 71.739  1.00 31.42 ? 200 LEU B N   1 
ATOM   4124 C  CA  . LEU B 1 200 ? 16.558  45.992 72.064  1.00 31.77 ? 200 LEU B CA  1 
ATOM   4125 C  C   . LEU B 1 200 ? 17.437  45.595 70.876  1.00 32.08 ? 200 LEU B C   1 
ATOM   4126 O  O   . LEU B 1 200 ? 18.465  46.238 70.616  1.00 32.17 ? 200 LEU B O   1 
ATOM   4127 C  CB  . LEU B 1 200 ? 16.845  45.069 73.254  1.00 31.76 ? 200 LEU B CB  1 
ATOM   4128 C  CG  . LEU B 1 200 ? 18.316  44.825 73.615  1.00 31.59 ? 200 LEU B CG  1 
ATOM   4129 C  CD1 . LEU B 1 200 ? 18.917  46.015 74.333  1.00 31.70 ? 200 LEU B CD1 1 
ATOM   4130 C  CD2 . LEU B 1 200 ? 18.471  43.574 74.451  1.00 32.13 ? 200 LEU B CD2 1 
ATOM   4131 N  N   . ARG B 1 201 ? 17.038  44.537 70.173  1.00 32.27 ? 201 ARG B N   1 
ATOM   4132 C  CA  . ARG B 1 201 ? 17.807  44.014 69.044  1.00 32.77 ? 201 ARG B CA  1 
ATOM   4133 C  C   . ARG B 1 201 ? 18.064  45.059 67.953  1.00 32.71 ? 201 ARG B C   1 
ATOM   4134 O  O   . ARG B 1 201 ? 19.155  45.093 67.370  1.00 32.71 ? 201 ARG B O   1 
ATOM   4135 C  CB  . ARG B 1 201 ? 17.126  42.780 68.440  1.00 33.07 ? 201 ARG B CB  1 
ATOM   4136 C  CG  . ARG B 1 201 ? 17.075  41.584 69.382  1.00 34.42 ? 201 ARG B CG  1 
ATOM   4137 C  CD  . ARG B 1 201 ? 16.877  40.280 68.641  1.00 36.43 ? 201 ARG B CD  1 
ATOM   4138 N  NE  . ARG B 1 201 ? 15.547  40.205 68.048  1.00 38.54 ? 201 ARG B NE  1 
ATOM   4139 C  CZ  . ARG B 1 201 ? 15.308  40.151 66.743  1.00 39.43 ? 201 ARG B CZ  1 
ATOM   4140 N  NH1 . ARG B 1 201 ? 16.315  40.139 65.872  1.00 39.98 ? 201 ARG B NH1 1 
ATOM   4141 N  NH2 . ARG B 1 201 ? 14.058  40.097 66.311  1.00 40.20 ? 201 ARG B NH2 1 
ATOM   4142 N  N   . ASP B 1 202 ? 17.063  45.906 67.692  1.00 32.53 ? 202 ASP B N   1 
ATOM   4143 C  CA  . ASP B 1 202 ? 17.143  46.939 66.651  1.00 32.24 ? 202 ASP B CA  1 
ATOM   4144 C  C   . ASP B 1 202 ? 18.116  48.062 67.010  1.00 32.16 ? 202 ASP B C   1 
ATOM   4145 O  O   . ASP B 1 202 ? 18.611  48.781 66.135  1.00 32.22 ? 202 ASP B O   1 
ATOM   4146 C  CB  . ASP B 1 202 ? 15.752  47.494 66.346  1.00 32.10 ? 202 ASP B CB  1 
ATOM   4147 C  CG  . ASP B 1 202 ? 14.793  46.422 65.841  1.00 32.28 ? 202 ASP B CG  1 
ATOM   4148 O  OD1 . ASP B 1 202 ? 15.251  45.307 65.518  1.00 31.81 ? 202 ASP B OD1 1 
ATOM   4149 O  OD2 . ASP B 1 202 ? 13.574  46.691 65.761  1.00 32.96 ? 202 ASP B OD2 1 
ATOM   4150 N  N   . GLY B 1 203 ? 18.397  48.190 68.301  1.00 32.01 ? 203 GLY B N   1 
ATOM   4151 C  CA  . GLY B 1 203 ? 19.345  49.173 68.790  1.00 31.89 ? 203 GLY B CA  1 
ATOM   4152 C  C   . GLY B 1 203 ? 18.621  50.345 69.407  1.00 31.72 ? 203 GLY B C   1 
ATOM   4153 O  O   . GLY B 1 203 ? 19.248  51.287 69.891  1.00 32.11 ? 203 GLY B O   1 
ATOM   4154 N  N   . ALA B 1 204 ? 17.295  50.280 69.397  1.00 31.31 ? 204 ALA B N   1 
ATOM   4155 C  CA  . ALA B 1 204 ? 16.478  51.371 69.901  1.00 30.90 ? 204 ALA B CA  1 
ATOM   4156 C  C   . ALA B 1 204 ? 16.596  51.540 71.413  1.00 30.50 ? 204 ALA B C   1 
ATOM   4157 O  O   . ALA B 1 204 ? 16.547  52.660 71.911  1.00 30.55 ? 204 ALA B O   1 
ATOM   4158 C  CB  . ALA B 1 204 ? 15.036  51.177 69.493  1.00 31.13 ? 204 ALA B CB  1 
ATOM   4159 N  N   . GLY B 1 205 ? 16.754  50.431 72.131  1.00 30.05 ? 205 GLY B N   1 
ATOM   4160 C  CA  . GLY B 1 205 ? 16.893  50.461 73.585  1.00 29.77 ? 205 GLY B CA  1 
ATOM   4161 C  C   . GLY B 1 205 ? 18.205  49.889 74.091  1.00 29.61 ? 205 GLY B C   1 
ATOM   4162 O  O   . GLY B 1 205 ? 19.009  49.373 73.320  1.00 29.80 ? 205 GLY B O   1 
ATOM   4163 N  N   . ASP B 1 206 ? 18.418  49.974 75.397  1.00 29.35 ? 206 ASP B N   1 
ATOM   4164 C  CA  . ASP B 1 206 ? 19.638  49.468 76.012  1.00 29.24 ? 206 ASP B CA  1 
ATOM   4165 C  C   . ASP B 1 206 ? 19.383  48.265 76.917  1.00 28.96 ? 206 ASP B C   1 
ATOM   4166 O  O   . ASP B 1 206 ? 20.305  47.501 77.198  1.00 28.99 ? 206 ASP B O   1 
ATOM   4167 C  CB  . ASP B 1 206 ? 20.322  50.573 76.819  1.00 29.52 ? 206 ASP B CB  1 
ATOM   4168 C  CG  . ASP B 1 206 ? 20.737  51.760 75.962  1.00 30.61 ? 206 ASP B CG  1 
ATOM   4169 O  OD1 . ASP B 1 206 ? 21.495  51.560 74.981  1.00 31.62 ? 206 ASP B OD1 1 
ATOM   4170 O  OD2 . ASP B 1 206 ? 20.313  52.898 76.282  1.00 31.51 ? 206 ASP B OD2 1 
ATOM   4171 N  N   . VAL B 1 207 ? 18.140  48.106 77.372  1.00 28.44 ? 207 VAL B N   1 
ATOM   4172 C  CA  . VAL B 1 207 ? 17.777  47.041 78.306  1.00 27.97 ? 207 VAL B CA  1 
ATOM   4173 C  C   . VAL B 1 207 ? 16.354  46.556 78.068  1.00 27.82 ? 207 VAL B C   1 
ATOM   4174 O  O   . VAL B 1 207 ? 15.427  47.352 77.926  1.00 28.04 ? 207 VAL B O   1 
ATOM   4175 C  CB  . VAL B 1 207 ? 17.994  47.462 79.805  1.00 28.19 ? 207 VAL B CB  1 
ATOM   4176 C  CG1 . VAL B 1 207 ? 17.290  48.776 80.135  1.00 27.87 ? 207 VAL B CG1 1 
ATOM   4177 C  CG2 . VAL B 1 207 ? 17.572  46.350 80.777  1.00 27.49 ? 207 VAL B CG2 1 
ATOM   4178 N  N   . ALA B 1 208 ? 16.203  45.236 78.013  1.00 27.55 ? 208 ALA B N   1 
ATOM   4179 C  CA  . ALA B 1 208 ? 14.921  44.590 77.764  1.00 26.90 ? 208 ALA B CA  1 
ATOM   4180 C  C   . ALA B 1 208 ? 14.499  43.848 79.021  1.00 26.70 ? 208 ALA B C   1 
ATOM   4181 O  O   . ALA B 1 208 ? 15.229  42.981 79.511  1.00 26.74 ? 208 ALA B O   1 
ATOM   4182 C  CB  . ALA B 1 208 ? 15.040  43.632 76.597  1.00 26.73 ? 208 ALA B CB  1 
ATOM   4183 N  N   . PHE B 1 209 ? 13.336  44.218 79.555  1.00 26.30 ? 209 PHE B N   1 
ATOM   4184 C  CA  . PHE B 1 209 ? 12.763  43.563 80.727  1.00 25.74 ? 209 PHE B CA  1 
ATOM   4185 C  C   . PHE B 1 209 ? 11.765  42.517 80.284  1.00 25.94 ? 209 PHE B C   1 
ATOM   4186 O  O   . PHE B 1 209 ? 10.626  42.826 79.952  1.00 26.03 ? 209 PHE B O   1 
ATOM   4187 C  CB  . PHE B 1 209 ? 12.113  44.581 81.652  1.00 25.21 ? 209 PHE B CB  1 
ATOM   4188 C  CG  . PHE B 1 209 ? 13.088  45.530 82.269  1.00 24.65 ? 209 PHE B CG  1 
ATOM   4189 C  CD1 . PHE B 1 209 ? 14.118  45.064 83.070  1.00 23.56 ? 209 PHE B CD1 1 
ATOM   4190 C  CD2 . PHE B 1 209 ? 12.981  46.894 82.046  1.00 25.20 ? 209 PHE B CD2 1 
ATOM   4191 C  CE1 . PHE B 1 209 ? 15.020  45.936 83.644  1.00 23.49 ? 209 PHE B CE1 1 
ATOM   4192 C  CE2 . PHE B 1 209 ? 13.885  47.788 82.627  1.00 24.28 ? 209 PHE B CE2 1 
ATOM   4193 C  CZ  . PHE B 1 209 ? 14.906  47.303 83.421  1.00 24.18 ? 209 PHE B CZ  1 
ATOM   4194 N  N   . ILE B 1 210 ? 12.221  41.272 80.257  1.00 26.41 ? 210 ILE B N   1 
ATOM   4195 C  CA  . ILE B 1 210 ? 11.438  40.167 79.725  1.00 26.83 ? 210 ILE B CA  1 
ATOM   4196 C  C   . ILE B 1 210 ? 11.667  38.914 80.554  1.00 27.46 ? 210 ILE B C   1 
ATOM   4197 O  O   . ILE B 1 210 ? 12.244  38.980 81.645  1.00 27.70 ? 210 ILE B O   1 
ATOM   4198 C  CB  . ILE B 1 210 ? 11.762  39.883 78.231  1.00 26.74 ? 210 ILE B CB  1 
ATOM   4199 C  CG1 . ILE B 1 210 ? 13.272  39.683 78.035  1.00 26.68 ? 210 ILE B CG1 1 
ATOM   4200 C  CG2 . ILE B 1 210 ? 11.225  41.006 77.350  1.00 26.76 ? 210 ILE B CG2 1 
ATOM   4201 C  CD1 . ILE B 1 210 ? 13.707  39.381 76.616  1.00 26.51 ? 210 ILE B CD1 1 
ATOM   4202 N  N   . ARG B 1 211 ? 11.205  37.785 80.015  1.00 27.95 ? 211 ARG B N   1 
ATOM   4203 C  CA  . ARG B 1 211 ? 11.248  36.479 80.657  1.00 28.34 ? 211 ARG B CA  1 
ATOM   4204 C  C   . ARG B 1 211 ? 12.435  35.683 80.084  1.00 28.80 ? 211 ARG B C   1 
ATOM   4205 O  O   . ARG B 1 211 ? 12.841  35.934 78.949  1.00 28.91 ? 211 ARG B O   1 
ATOM   4206 C  CB  . ARG B 1 211 ? 9.896   35.803 80.400  1.00 28.20 ? 211 ARG B CB  1 
ATOM   4207 C  CG  . ARG B 1 211 ? 9.908   34.311 80.122  1.00 28.77 ? 211 ARG B CG  1 
ATOM   4208 C  CD  . ARG B 1 211 ? 8.731   33.884 79.284  1.00 28.39 ? 211 ARG B CD  1 
ATOM   4209 N  NE  . ARG B 1 211 ? 7.441   34.177 79.907  1.00 29.67 ? 211 ARG B NE  1 
ATOM   4210 C  CZ  . ARG B 1 211 ? 6.586   33.257 80.352  1.00 30.29 ? 211 ARG B CZ  1 
ATOM   4211 N  NH1 . ARG B 1 211 ? 6.884   31.964 80.261  1.00 31.35 ? 211 ARG B NH1 1 
ATOM   4212 N  NH2 . ARG B 1 211 ? 5.425   33.625 80.879  1.00 28.79 ? 211 ARG B NH2 1 
ATOM   4213 N  N   . GLU B 1 212 ? 12.991  34.742 80.854  1.00 29.25 ? 212 GLU B N   1 
ATOM   4214 C  CA  . GLU B 1 212 ? 14.204  34.004 80.437  1.00 30.03 ? 212 GLU B CA  1 
ATOM   4215 C  C   . GLU B 1 212 ? 14.165  33.325 79.076  1.00 30.44 ? 212 GLU B C   1 
ATOM   4216 O  O   . GLU B 1 212 ? 15.104  33.460 78.296  1.00 31.15 ? 212 GLU B O   1 
ATOM   4217 C  CB  . GLU B 1 212 ? 14.667  32.983 81.478  1.00 30.05 ? 212 GLU B CB  1 
ATOM   4218 C  CG  . GLU B 1 212 ? 13.649  32.585 82.521  1.00 31.77 ? 212 GLU B CG  1 
ATOM   4219 C  CD  . GLU B 1 212 ? 12.650  31.548 82.058  1.00 32.88 ? 212 GLU B CD  1 
ATOM   4220 O  OE1 . GLU B 1 212 ? 12.735  30.389 82.529  1.00 33.60 ? 212 GLU B OE1 1 
ATOM   4221 O  OE2 . GLU B 1 212 ? 11.771  31.898 81.245  1.00 33.03 ? 212 GLU B OE2 1 
ATOM   4222 N  N   . SER B 1 213 ? 13.094  32.603 78.781  1.00 30.57 ? 213 SER B N   1 
ATOM   4223 C  CA  . SER B 1 213 ? 13.033  31.814 77.560  1.00 30.91 ? 213 SER B CA  1 
ATOM   4224 C  C   . SER B 1 213 ? 12.883  32.615 76.256  1.00 31.29 ? 213 SER B C   1 
ATOM   4225 O  O   . SER B 1 213 ? 12.875  32.035 75.171  1.00 31.34 ? 213 SER B O   1 
ATOM   4226 C  CB  . SER B 1 213 ? 11.899  30.818 77.676  1.00 30.85 ? 213 SER B CB  1 
ATOM   4227 O  OG  . SER B 1 213 ? 10.729  31.493 78.082  1.00 31.77 ? 213 SER B OG  1 
ATOM   4228 N  N   . THR B 1 214 ? 12.768  33.935 76.348  1.00 31.76 ? 214 THR B N   1 
ATOM   4229 C  CA  . THR B 1 214 ? 12.553  34.757 75.156  1.00 32.17 ? 214 THR B CA  1 
ATOM   4230 C  C   . THR B 1 214 ? 13.773  34.765 74.240  1.00 32.69 ? 214 THR B C   1 
ATOM   4231 O  O   . THR B 1 214 ? 13.673  34.428 73.059  1.00 32.80 ? 214 THR B O   1 
ATOM   4232 C  CB  . THR B 1 214 ? 12.107  36.170 75.532  1.00 31.93 ? 214 THR B CB  1 
ATOM   4233 O  OG1 . THR B 1 214 ? 10.772  36.094 76.044  1.00 32.89 ? 214 THR B OG1 1 
ATOM   4234 C  CG2 . THR B 1 214 ? 12.122  37.090 74.331  1.00 31.15 ? 214 THR B CG2 1 
ATOM   4235 N  N   . VAL B 1 215 ? 14.927  35.127 74.786  1.00 33.26 ? 215 VAL B N   1 
ATOM   4236 C  CA  . VAL B 1 215 ? 16.157  35.146 73.999  1.00 33.72 ? 215 VAL B CA  1 
ATOM   4237 C  C   . VAL B 1 215 ? 16.369  33.825 73.229  1.00 34.08 ? 215 VAL B C   1 
ATOM   4238 O  O   . VAL B 1 215 ? 16.844  33.847 72.101  1.00 34.09 ? 215 VAL B O   1 
ATOM   4239 C  CB  . VAL B 1 215 ? 17.401  35.588 74.854  1.00 33.60 ? 215 VAL B CB  1 
ATOM   4240 C  CG1 . VAL B 1 215 ? 17.630  34.665 76.051  1.00 33.84 ? 215 VAL B CG1 1 
ATOM   4241 C  CG2 . VAL B 1 215 ? 18.655  35.703 73.997  1.00 33.45 ? 215 VAL B CG2 1 
ATOM   4242 N  N   . PHE B 1 216 ? 15.972  32.698 73.822  1.00 34.74 ? 216 PHE B N   1 
ATOM   4243 C  CA  . PHE B 1 216 ? 16.129  31.381 73.189  1.00 35.41 ? 216 PHE B CA  1 
ATOM   4244 C  C   . PHE B 1 216 ? 15.088  31.097 72.122  1.00 36.44 ? 216 PHE B C   1 
ATOM   4245 O  O   . PHE B 1 216 ? 15.351  30.360 71.175  1.00 36.39 ? 216 PHE B O   1 
ATOM   4246 C  CB  . PHE B 1 216 ? 16.067  30.278 74.229  1.00 34.81 ? 216 PHE B CB  1 
ATOM   4247 C  CG  . PHE B 1 216 ? 17.181  30.320 75.205  1.00 34.54 ? 216 PHE B CG  1 
ATOM   4248 C  CD1 . PHE B 1 216 ? 18.380  29.684 74.932  1.00 34.23 ? 216 PHE B CD1 1 
ATOM   4249 C  CD2 . PHE B 1 216 ? 17.039  30.998 76.408  1.00 34.72 ? 216 PHE B CD2 1 
ATOM   4250 C  CE1 . PHE B 1 216 ? 19.426  29.720 75.846  1.00 34.29 ? 216 PHE B CE1 1 
ATOM   4251 C  CE2 . PHE B 1 216 ? 18.080  31.041 77.327  1.00 34.43 ? 216 PHE B CE2 1 
ATOM   4252 C  CZ  . PHE B 1 216 ? 19.275  30.403 77.044  1.00 34.12 ? 216 PHE B CZ  1 
ATOM   4253 N  N   . GLU B 1 217 ? 13.900  31.665 72.304  1.00 37.93 ? 217 GLU B N   1 
ATOM   4254 C  CA  . GLU B 1 217 ? 12.797  31.508 71.368  1.00 39.52 ? 217 GLU B CA  1 
ATOM   4255 C  C   . GLU B 1 217 ? 13.012  32.368 70.123  1.00 39.79 ? 217 GLU B C   1 
ATOM   4256 O  O   . GLU B 1 217 ? 12.697  31.945 69.014  1.00 39.94 ? 217 GLU B O   1 
ATOM   4257 C  CB  . GLU B 1 217 ? 11.466  31.877 72.041  1.00 39.45 ? 217 GLU B CB  1 
ATOM   4258 C  CG  . GLU B 1 217 ? 10.873  30.790 72.962  1.00 40.75 ? 217 GLU B CG  1 
ATOM   4259 C  CD  . GLU B 1 217 ? 9.822   31.330 73.960  1.00 41.46 ? 217 GLU B CD  1 
ATOM   4260 O  OE1 . GLU B 1 217 ? 9.179   32.374 73.679  1.00 43.74 ? 217 GLU B OE1 1 
ATOM   4261 O  OE2 . GLU B 1 217 ? 9.636   30.699 75.033  1.00 43.60 ? 217 GLU B OE2 1 
ATOM   4262 N  N   . ASP B 1 218 ? 13.552  33.570 70.305  1.00 40.50 ? 218 ASP B N   1 
ATOM   4263 C  CA  . ASP B 1 218 ? 13.709  34.504 69.196  1.00 41.30 ? 218 ASP B CA  1 
ATOM   4264 C  C   . ASP B 1 218 ? 14.980  34.248 68.402  1.00 41.71 ? 218 ASP B C   1 
ATOM   4265 O  O   . ASP B 1 218 ? 15.009  34.455 67.194  1.00 41.87 ? 218 ASP B O   1 
ATOM   4266 C  CB  . ASP B 1 218 ? 13.666  35.955 69.689  1.00 41.50 ? 218 ASP B CB  1 
ATOM   4267 C  CG  . ASP B 1 218 ? 12.235  36.471 69.913  1.00 42.52 ? 218 ASP B CG  1 
ATOM   4268 O  OD1 . ASP B 1 218 ? 11.345  35.670 70.285  1.00 43.53 ? 218 ASP B OD1 1 
ATOM   4269 O  OD2 . ASP B 1 218 ? 12.004  37.693 69.729  1.00 43.61 ? 218 ASP B OD2 1 
ATOM   4270 N  N   . LEU B 1 219 ? 16.028  33.799 69.080  1.00 42.40 ? 219 LEU B N   1 
ATOM   4271 C  CA  . LEU B 1 219 ? 17.309  33.549 68.426  1.00 43.11 ? 219 LEU B CA  1 
ATOM   4272 C  C   . LEU B 1 219 ? 17.768  32.102 68.600  1.00 43.70 ? 219 LEU B C   1 
ATOM   4273 O  O   . LEU B 1 219 ? 18.188  31.678 69.691  1.00 43.66 ? 219 LEU B O   1 
ATOM   4274 C  CB  . LEU B 1 219 ? 18.378  34.525 68.920  1.00 43.10 ? 219 LEU B CB  1 
ATOM   4275 C  CG  . LEU B 1 219 ? 18.052  36.019 68.833  1.00 43.43 ? 219 LEU B CG  1 
ATOM   4276 C  CD1 . LEU B 1 219 ? 19.200  36.834 69.398  1.00 43.52 ? 219 LEU B CD1 1 
ATOM   4277 C  CD2 . LEU B 1 219 ? 17.726  36.448 67.402  1.00 43.63 ? 219 LEU B CD2 1 
ATOM   4278 N  N   . SER B 1 220 ? 17.687  31.357 67.499  1.00 44.32 ? 220 SER B N   1 
ATOM   4279 C  CA  . SER B 1 220 ? 17.978  29.929 67.488  1.00 44.78 ? 220 SER B CA  1 
ATOM   4280 C  C   . SER B 1 220 ? 19.455  29.620 67.253  1.00 44.97 ? 220 SER B C   1 
ATOM   4281 O  O   . SER B 1 220 ? 19.858  28.457 67.276  1.00 45.00 ? 220 SER B O   1 
ATOM   4282 C  CB  . SER B 1 220 ? 17.101  29.220 66.450  1.00 44.83 ? 220 SER B CB  1 
ATOM   4283 O  OG  . SER B 1 220 ? 17.063  29.951 65.237  1.00 45.15 ? 220 SER B OG  1 
ATOM   4284 N  N   . ASP B 1 221 ? 20.266  30.651 67.039  1.00 45.26 ? 221 ASP B N   1 
ATOM   4285 C  CA  . ASP B 1 221 ? 21.694  30.438 66.841  1.00 45.67 ? 221 ASP B CA  1 
ATOM   4286 C  C   . ASP B 1 221 ? 22.544  30.882 68.037  1.00 45.77 ? 221 ASP B C   1 
ATOM   4287 O  O   . ASP B 1 221 ? 22.495  32.044 68.451  1.00 45.78 ? 221 ASP B O   1 
ATOM   4288 C  CB  . ASP B 1 221 ? 22.175  31.109 65.554  1.00 45.79 ? 221 ASP B CB  1 
ATOM   4289 C  CG  . ASP B 1 221 ? 23.639  30.823 65.264  1.00 46.41 ? 221 ASP B CG  1 
ATOM   4290 O  OD1 . ASP B 1 221 ? 24.001  29.633 65.138  1.00 47.21 ? 221 ASP B OD1 1 
ATOM   4291 O  OD2 . ASP B 1 221 ? 24.430  31.786 65.169  1.00 46.94 ? 221 ASP B OD2 1 
ATOM   4292 N  N   . GLU B 1 222 ? 23.334  29.946 68.565  1.00 45.87 ? 222 GLU B N   1 
ATOM   4293 C  CA  . GLU B 1 222 ? 24.213  30.180 69.724  1.00 46.05 ? 222 GLU B CA  1 
ATOM   4294 C  C   . GLU B 1 222 ? 25.163  31.366 69.558  1.00 45.67 ? 222 GLU B C   1 
ATOM   4295 O  O   . GLU B 1 222 ? 25.465  32.060 70.530  1.00 45.69 ? 222 GLU B O   1 
ATOM   4296 C  CB  . GLU B 1 222 ? 25.016  28.912 70.073  1.00 46.12 ? 222 GLU B CB  1 
ATOM   4297 C  CG  . GLU B 1 222 ? 25.785  28.285 68.891  1.00 46.81 ? 222 GLU B CG  1 
ATOM   4298 C  CD  . GLU B 1 222 ? 26.966  27.411 69.317  1.00 46.82 ? 222 GLU B CD  1 
ATOM   4299 O  OE1 . GLU B 1 222 ? 27.312  26.475 68.559  1.00 47.42 ? 222 GLU B OE1 1 
ATOM   4300 O  OE2 . GLU B 1 222 ? 27.554  27.659 70.396  1.00 47.69 ? 222 GLU B OE2 1 
ATOM   4301 N  N   . ALA B 1 223 ? 25.629  31.593 68.332  1.00 45.40 ? 223 ALA B N   1 
ATOM   4302 C  CA  . ALA B 1 223 ? 26.550  32.690 68.049  1.00 45.09 ? 223 ALA B CA  1 
ATOM   4303 C  C   . ALA B 1 223 ? 25.871  34.050 68.208  1.00 44.91 ? 223 ALA B C   1 
ATOM   4304 O  O   . ALA B 1 223 ? 26.537  35.043 68.504  1.00 44.90 ? 223 ALA B O   1 
ATOM   4305 C  CB  . ALA B 1 223 ? 27.155  32.542 66.661  1.00 44.99 ? 223 ALA B CB  1 
ATOM   4306 N  N   . GLU B 1 224 ? 24.552  34.087 68.017  1.00 44.60 ? 224 GLU B N   1 
ATOM   4307 C  CA  . GLU B 1 224 ? 23.777  35.316 68.179  1.00 44.40 ? 224 GLU B CA  1 
ATOM   4308 C  C   . GLU B 1 224 ? 23.446  35.573 69.639  1.00 44.04 ? 224 GLU B C   1 
ATOM   4309 O  O   . GLU B 1 224 ? 23.431  36.722 70.080  1.00 44.19 ? 224 GLU B O   1 
ATOM   4310 C  CB  . GLU B 1 224 ? 22.494  35.274 67.353  1.00 44.46 ? 224 GLU B CB  1 
ATOM   4311 C  CG  . GLU B 1 224 ? 22.647  35.802 65.938  1.00 45.83 ? 224 GLU B CG  1 
ATOM   4312 C  CD  . GLU B 1 224 ? 21.765  35.064 64.925  1.00 48.05 ? 224 GLU B CD  1 
ATOM   4313 O  OE1 . GLU B 1 224 ? 20.656  34.604 65.299  1.00 48.74 ? 224 GLU B OE1 1 
ATOM   4314 O  OE2 . GLU B 1 224 ? 22.188  34.943 63.747  1.00 48.19 ? 224 GLU B OE2 1 
ATOM   4315 N  N   . ARG B 1 225 ? 23.179  34.506 70.387  1.00 43.53 ? 225 ARG B N   1 
ATOM   4316 C  CA  . ARG B 1 225 ? 22.867  34.629 71.810  1.00 43.08 ? 225 ARG B CA  1 
ATOM   4317 C  C   . ARG B 1 225 ? 24.109  34.963 72.636  1.00 42.76 ? 225 ARG B C   1 
ATOM   4318 O  O   . ARG B 1 225 ? 23.996  35.486 73.745  1.00 42.73 ? 225 ARG B O   1 
ATOM   4319 C  CB  . ARG B 1 225 ? 22.200  33.361 72.337  1.00 43.13 ? 225 ARG B CB  1 
ATOM   4320 C  CG  . ARG B 1 225 ? 20.828  33.072 71.739  1.00 43.08 ? 225 ARG B CG  1 
ATOM   4321 C  CD  . ARG B 1 225 ? 20.168  31.881 72.434  1.00 43.12 ? 225 ARG B CD  1 
ATOM   4322 N  NE  . ARG B 1 225 ? 21.052  30.717 72.484  1.00 43.14 ? 225 ARG B NE  1 
ATOM   4323 C  CZ  . ARG B 1 225 ? 20.934  29.643 71.709  1.00 43.28 ? 225 ARG B CZ  1 
ATOM   4324 N  NH1 . ARG B 1 225 ? 19.952  29.555 70.814  1.00 43.04 ? 225 ARG B NH1 1 
ATOM   4325 N  NH2 . ARG B 1 225 ? 21.804  28.651 71.838  1.00 43.06 ? 225 ARG B NH2 1 
ATOM   4326 N  N   . ASP B 1 226 ? 25.286  34.658 72.086  1.00 42.43 ? 226 ASP B N   1 
ATOM   4327 C  CA  . ASP B 1 226 ? 26.571  35.089 72.656  1.00 41.95 ? 226 ASP B CA  1 
ATOM   4328 C  C   . ASP B 1 226 ? 26.733  36.610 72.615  1.00 41.43 ? 226 ASP B C   1 
ATOM   4329 O  O   . ASP B 1 226 ? 27.578  37.162 73.319  1.00 41.27 ? 226 ASP B O   1 
ATOM   4330 C  CB  . ASP B 1 226 ? 27.749  34.423 71.925  1.00 42.11 ? 226 ASP B CB  1 
ATOM   4331 C  CG  . ASP B 1 226 ? 28.287  33.184 72.649  1.00 42.69 ? 226 ASP B CG  1 
ATOM   4332 O  OD1 . ASP B 1 226 ? 27.787  32.834 73.742  1.00 43.18 ? 226 ASP B OD1 1 
ATOM   4333 O  OD2 . ASP B 1 226 ? 29.230  32.557 72.116  1.00 43.29 ? 226 ASP B OD2 1 
ATOM   4334 N  N   . GLU B 1 227 ? 25.914  37.273 71.795  1.00 40.95 ? 227 GLU B N   1 
ATOM   4335 C  CA  . GLU B 1 227 ? 25.944  38.733 71.646  1.00 40.77 ? 227 GLU B CA  1 
ATOM   4336 C  C   . GLU B 1 227 ? 25.092  39.436 72.705  1.00 39.89 ? 227 GLU B C   1 
ATOM   4337 O  O   . GLU B 1 227 ? 25.041  40.665 72.754  1.00 39.89 ? 227 GLU B O   1 
ATOM   4338 C  CB  . GLU B 1 227 ? 25.513  39.162 70.228  1.00 40.71 ? 227 GLU B CB  1 
ATOM   4339 C  CG  . GLU B 1 227 ? 26.216  38.403 69.090  1.00 41.80 ? 227 GLU B CG  1 
ATOM   4340 C  CD  . GLU B 1 227 ? 26.175  39.126 67.738  1.00 42.08 ? 227 GLU B CD  1 
ATOM   4341 O  OE1 . GLU B 1 227 ? 27.116  39.909 67.453  1.00 43.80 ? 227 GLU B OE1 1 
ATOM   4342 O  OE2 . GLU B 1 227 ? 25.227  38.883 66.946  1.00 43.20 ? 227 GLU B OE2 1 
ATOM   4343 N  N   . TYR B 1 228 ? 24.441  38.651 73.558  1.00 39.18 ? 228 TYR B N   1 
ATOM   4344 C  CA  . TYR B 1 228 ? 23.571  39.187 74.602  1.00 38.33 ? 228 TYR B CA  1 
ATOM   4345 C  C   . TYR B 1 228 ? 23.966  38.726 76.003  1.00 37.94 ? 228 TYR B C   1 
ATOM   4346 O  O   . TYR B 1 228 ? 24.619  37.689 76.174  1.00 37.79 ? 228 TYR B O   1 
ATOM   4347 C  CB  . TYR B 1 228 ? 22.111  38.850 74.305  1.00 38.09 ? 228 TYR B CB  1 
ATOM   4348 C  CG  . TYR B 1 228 ? 21.606  39.551 73.078  1.00 38.10 ? 228 TYR B CG  1 
ATOM   4349 C  CD1 . TYR B 1 228 ? 21.158  40.868 73.143  1.00 38.32 ? 228 TYR B CD1 1 
ATOM   4350 C  CD2 . TYR B 1 228 ? 21.599  38.912 71.839  1.00 38.55 ? 228 TYR B CD2 1 
ATOM   4351 C  CE1 . TYR B 1 228 ? 20.698  41.533 72.006  1.00 38.54 ? 228 TYR B CE1 1 
ATOM   4352 C  CE2 . TYR B 1 228 ? 21.146  39.570 70.689  1.00 38.51 ? 228 TYR B CE2 1 
ATOM   4353 C  CZ  . TYR B 1 228 ? 20.695  40.880 70.783  1.00 38.23 ? 228 TYR B CZ  1 
ATOM   4354 O  OH  . TYR B 1 228 ? 20.245  41.536 69.663  1.00 37.60 ? 228 TYR B OH  1 
ATOM   4355 N  N   . GLU B 1 229 ? 23.565  39.518 76.995  1.00 37.33 ? 229 GLU B N   1 
ATOM   4356 C  CA  . GLU B 1 229 ? 23.893  39.274 78.389  1.00 36.65 ? 229 GLU B CA  1 
ATOM   4357 C  C   . GLU B 1 229 ? 22.703  39.581 79.277  1.00 36.30 ? 229 GLU B C   1 
ATOM   4358 O  O   . GLU B 1 229 ? 21.748  40.239 78.851  1.00 36.11 ? 229 GLU B O   1 
ATOM   4359 C  CB  . GLU B 1 229 ? 25.056  40.158 78.814  1.00 36.64 ? 229 GLU B CB  1 
ATOM   4360 C  CG  . GLU B 1 229 ? 26.421  39.668 78.385  1.00 37.19 ? 229 GLU B CG  1 
ATOM   4361 C  CD  . GLU B 1 229 ? 27.546  40.504 78.980  1.00 37.76 ? 229 GLU B CD  1 
ATOM   4362 O  OE1 . GLU B 1 229 ? 28.284  39.979 79.838  1.00 38.29 ? 229 GLU B OE1 1 
ATOM   4363 O  OE2 . GLU B 1 229 ? 27.687  41.687 78.601  1.00 37.54 ? 229 GLU B OE2 1 
ATOM   4364 N  N   . LEU B 1 230 ? 22.777  39.097 80.514  1.00 35.88 ? 230 LEU B N   1 
ATOM   4365 C  CA  . LEU B 1 230 ? 21.796  39.401 81.548  1.00 35.34 ? 230 LEU B CA  1 
ATOM   4366 C  C   . LEU B 1 230 ? 22.417  40.275 82.623  1.00 35.34 ? 230 LEU B C   1 
ATOM   4367 O  O   . LEU B 1 230 ? 23.632  40.261 82.812  1.00 35.46 ? 230 LEU B O   1 
ATOM   4368 C  CB  . LEU B 1 230 ? 21.274  38.118 82.178  1.00 35.12 ? 230 LEU B CB  1 
ATOM   4369 C  CG  . LEU B 1 230 ? 20.687  37.081 81.227  1.00 34.64 ? 230 LEU B CG  1 
ATOM   4370 C  CD1 . LEU B 1 230 ? 20.292  35.846 81.990  1.00 34.24 ? 230 LEU B CD1 1 
ATOM   4371 C  CD2 . LEU B 1 230 ? 19.500  37.643 80.495  1.00 34.86 ? 230 LEU B CD2 1 
ATOM   4372 N  N   . LEU B 1 231 ? 21.583  41.048 83.315  1.00 35.32 ? 231 LEU B N   1 
ATOM   4373 C  CA  . LEU B 1 231 ? 22.035  41.858 84.441  1.00 35.25 ? 231 LEU B CA  1 
ATOM   4374 C  C   . LEU B 1 231 ? 21.651  41.179 85.748  1.00 35.67 ? 231 LEU B C   1 
ATOM   4375 O  O   . LEU B 1 231 ? 20.482  40.863 85.975  1.00 35.59 ? 231 LEU B O   1 
ATOM   4376 C  CB  . LEU B 1 231 ? 21.436  43.263 84.389  1.00 34.94 ? 231 LEU B CB  1 
ATOM   4377 C  CG  . LEU B 1 231 ? 21.780  44.172 83.215  1.00 34.19 ? 231 LEU B CG  1 
ATOM   4378 C  CD1 . LEU B 1 231 ? 21.119  45.516 83.422  1.00 32.61 ? 231 LEU B CD1 1 
ATOM   4379 C  CD2 . LEU B 1 231 ? 23.283  44.319 83.050  1.00 33.66 ? 231 LEU B CD2 1 
ATOM   4380 N  N   . CYS B 1 232 ? 22.644  40.940 86.598  1.00 36.12 ? 232 CYS B N   1 
ATOM   4381 C  CA  . CYS B 1 232 ? 22.408  40.291 87.882  1.00 36.62 ? 232 CYS B CA  1 
ATOM   4382 C  C   . CYS B 1 232 ? 22.213  41.345 88.964  1.00 36.58 ? 232 CYS B C   1 
ATOM   4383 O  O   . CYS B 1 232 ? 22.847  42.401 88.921  1.00 36.56 ? 232 CYS B O   1 
ATOM   4384 C  CB  . CYS B 1 232 ? 23.556  39.344 88.238  1.00 36.49 ? 232 CYS B CB  1 
ATOM   4385 S  SG  . CYS B 1 232 ? 24.112  38.245 86.878  1.00 38.31 ? 232 CYS B SG  1 
ATOM   4386 N  N   . PRO B 1 233 ? 21.339  41.058 89.944  1.00 36.61 ? 233 PRO B N   1 
ATOM   4387 C  CA  . PRO B 1 233 ? 20.976  42.051 90.944  1.00 36.61 ? 233 PRO B CA  1 
ATOM   4388 C  C   . PRO B 1 233 ? 22.095  42.276 91.950  1.00 36.69 ? 233 PRO B C   1 
ATOM   4389 O  O   . PRO B 1 233 ? 21.966  43.112 92.847  1.00 36.89 ? 233 PRO B O   1 
ATOM   4390 C  CB  . PRO B 1 233 ? 19.752  41.431 91.631  1.00 36.68 ? 233 PRO B CB  1 
ATOM   4391 C  CG  . PRO B 1 233 ? 19.405  40.211 90.836  1.00 36.47 ? 233 PRO B CG  1 
ATOM   4392 C  CD  . PRO B 1 233 ? 20.653  39.779 90.182  1.00 36.54 ? 233 PRO B CD  1 
ATOM   4393 N  N   . ASP B 1 234 ? 23.180  41.525 91.801  1.00 36.68 ? 234 ASP B N   1 
ATOM   4394 C  CA  . ASP B 1 234 ? 24.394  41.763 92.571  1.00 36.74 ? 234 ASP B CA  1 
ATOM   4395 C  C   . ASP B 1 234 ? 25.353  42.652 91.774  1.00 36.38 ? 234 ASP B C   1 
ATOM   4396 O  O   . ASP B 1 234 ? 26.527  42.773 92.108  1.00 36.14 ? 234 ASP B O   1 
ATOM   4397 C  CB  . ASP B 1 234 ? 25.051  40.433 92.972  1.00 36.90 ? 234 ASP B CB  1 
ATOM   4398 C  CG  . ASP B 1 234 ? 25.611  39.662 91.784  1.00 37.54 ? 234 ASP B CG  1 
ATOM   4399 O  OD1 . ASP B 1 234 ? 25.406  40.070 90.617  1.00 39.24 ? 234 ASP B OD1 1 
ATOM   4400 O  OD2 . ASP B 1 234 ? 26.270  38.633 92.022  1.00 37.84 ? 234 ASP B OD2 1 
ATOM   4401 N  N   . ASN B 1 235 ? 24.817  43.261 90.717  1.00 36.32 ? 235 ASN B N   1 
ATOM   4402 C  CA  . ASN B 1 235 ? 25.546  44.166 89.813  1.00 36.23 ? 235 ASN B CA  1 
ATOM   4403 C  C   . ASN B 1 235 ? 26.686  43.512 89.017  1.00 35.98 ? 235 ASN B C   1 
ATOM   4404 O  O   . ASN B 1 235 ? 27.752  44.102 88.831  1.00 35.88 ? 235 ASN B O   1 
ATOM   4405 C  CB  . ASN B 1 235 ? 25.974  45.459 90.536  1.00 36.31 ? 235 ASN B CB  1 
ATOM   4406 C  CG  . ASN B 1 235 ? 24.787  46.199 91.164  1.00 36.47 ? 235 ASN B CG  1 
ATOM   4407 O  OD1 . ASN B 1 235 ? 23.640  46.044 90.736  1.00 36.62 ? 235 ASN B OD1 1 
ATOM   4408 N  ND2 . ASN B 1 235 ? 25.063  46.996 92.187  1.00 36.16 ? 235 ASN B ND2 1 
ATOM   4409 N  N   . THR B 1 236 ? 26.427  42.294 88.539  1.00 35.89 ? 236 THR B N   1 
ATOM   4410 C  CA  . THR B 1 236 ? 27.314  41.587 87.609  1.00 35.63 ? 236 THR B CA  1 
ATOM   4411 C  C   . THR B 1 236 ? 26.597  41.333 86.270  1.00 35.18 ? 236 THR B C   1 
ATOM   4412 O  O   . THR B 1 236 ? 25.370  41.455 86.174  1.00 35.09 ? 236 THR B O   1 
ATOM   4413 C  CB  . THR B 1 236 ? 27.799  40.230 88.194  1.00 35.83 ? 236 THR B CB  1 
ATOM   4414 O  OG1 . THR B 1 236 ? 27.826  40.296 89.625  1.00 36.11 ? 236 THR B OG1 1 
ATOM   4415 C  CG2 . THR B 1 236 ? 29.203  39.866 87.672  1.00 35.92 ? 236 THR B CG2 1 
ATOM   4416 N  N   . ARG B 1 237 ? 27.376  41.006 85.240  1.00 34.60 ? 237 ARG B N   1 
ATOM   4417 C  CA  . ARG B 1 237 ? 26.836  40.570 83.957  1.00 34.06 ? 237 ARG B CA  1 
ATOM   4418 C  C   . ARG B 1 237 ? 27.156  39.095 83.755  1.00 33.88 ? 237 ARG B C   1 
ATOM   4419 O  O   . ARG B 1 237 ? 28.244  38.633 84.114  1.00 33.79 ? 237 ARG B O   1 
ATOM   4420 C  CB  . ARG B 1 237 ? 27.419  41.389 82.798  1.00 34.06 ? 237 ARG B CB  1 
ATOM   4421 C  CG  . ARG B 1 237 ? 26.970  42.845 82.730  1.00 33.53 ? 237 ARG B CG  1 
ATOM   4422 C  CD  . ARG B 1 237 ? 27.216  43.428 81.343  1.00 32.50 ? 237 ARG B CD  1 
ATOM   4423 N  NE  . ARG B 1 237 ? 26.670  44.776 81.199  1.00 31.85 ? 237 ARG B NE  1 
ATOM   4424 C  CZ  . ARG B 1 237 ? 26.298  45.324 80.044  1.00 31.97 ? 237 ARG B CZ  1 
ATOM   4425 N  NH1 . ARG B 1 237 ? 26.399  44.646 78.907  1.00 32.00 ? 237 ARG B NH1 1 
ATOM   4426 N  NH2 . ARG B 1 237 ? 25.811  46.557 80.025  1.00 32.17 ? 237 ARG B NH2 1 
ATOM   4427 N  N   . LYS B 1 238 ? 26.204  38.367 83.177  1.00 33.60 ? 238 LYS B N   1 
ATOM   4428 C  CA  . LYS B 1 238 ? 26.339  36.933 82.934  1.00 33.39 ? 238 LYS B CA  1 
ATOM   4429 C  C   . LYS B 1 238 ? 25.709  36.526 81.605  1.00 33.19 ? 238 LYS B C   1 
ATOM   4430 O  O   . LYS B 1 238 ? 24.773  37.179 81.137  1.00 33.08 ? 238 LYS B O   1 
ATOM   4431 C  CB  . LYS B 1 238 ? 25.705  36.137 84.080  1.00 33.39 ? 238 LYS B CB  1 
ATOM   4432 C  CG  . LYS B 1 238 ? 26.671  35.818 85.196  1.00 33.77 ? 238 LYS B CG  1 
ATOM   4433 C  CD  . LYS B 1 238 ? 25.978  35.192 86.393  1.00 34.46 ? 238 LYS B CD  1 
ATOM   4434 C  CE  . LYS B 1 238 ? 26.901  35.146 87.613  1.00 34.76 ? 238 LYS B CE  1 
ATOM   4435 N  NZ  . LYS B 1 238 ? 27.374  36.510 88.033  1.00 35.63 ? 238 LYS B NZ  1 
ATOM   4436 N  N   . PRO B 1 239 ? 26.215  35.437 80.992  1.00 33.14 ? 239 PRO B N   1 
ATOM   4437 C  CA  . PRO B 1 239 ? 25.633  34.918 79.742  1.00 33.08 ? 239 PRO B CA  1 
ATOM   4438 C  C   . PRO B 1 239 ? 24.155  34.569 79.913  1.00 32.99 ? 239 PRO B C   1 
ATOM   4439 O  O   . PRO B 1 239 ? 23.721  34.251 81.022  1.00 33.04 ? 239 PRO B O   1 
ATOM   4440 C  CB  . PRO B 1 239 ? 26.443  33.646 79.473  1.00 33.17 ? 239 PRO B CB  1 
ATOM   4441 C  CG  . PRO B 1 239 ? 27.712  33.823 80.244  1.00 33.28 ? 239 PRO B CG  1 
ATOM   4442 C  CD  . PRO B 1 239 ? 27.365  34.633 81.446  1.00 32.99 ? 239 PRO B CD  1 
ATOM   4443 N  N   . VAL B 1 240 ? 23.393  34.613 78.823  1.00 32.99 ? 240 VAL B N   1 
ATOM   4444 C  CA  . VAL B 1 240 ? 21.929  34.470 78.898  1.00 32.72 ? 240 VAL B CA  1 
ATOM   4445 C  C   . VAL B 1 240 ? 21.429  33.139 79.458  1.00 32.81 ? 240 VAL B C   1 
ATOM   4446 O  O   . VAL B 1 240 ? 20.331  33.080 80.003  1.00 33.04 ? 240 VAL B O   1 
ATOM   4447 C  CB  . VAL B 1 240 ? 21.208  34.771 77.548  1.00 32.58 ? 240 VAL B CB  1 
ATOM   4448 C  CG1 . VAL B 1 240 ? 21.331  36.239 77.195  1.00 32.11 ? 240 VAL B CG1 1 
ATOM   4449 C  CG2 . VAL B 1 240 ? 21.726  33.878 76.423  1.00 32.28 ? 240 VAL B CG2 1 
ATOM   4450 N  N   . ASP B 1 241 ? 22.224  32.080 79.327  1.00 32.81 ? 241 ASP B N   1 
ATOM   4451 C  CA  . ASP B 1 241 ? 21.779  30.764 79.768  1.00 32.92 ? 241 ASP B CA  1 
ATOM   4452 C  C   . ASP B 1 241 ? 22.044  30.540 81.251  1.00 32.84 ? 241 ASP B C   1 
ATOM   4453 O  O   . ASP B 1 241 ? 21.547  29.578 81.841  1.00 32.85 ? 241 ASP B O   1 
ATOM   4454 C  CB  . ASP B 1 241 ? 22.360  29.637 78.896  1.00 32.97 ? 241 ASP B CB  1 
ATOM   4455 C  CG  . ASP B 1 241 ? 23.861  29.491 79.032  1.00 33.93 ? 241 ASP B CG  1 
ATOM   4456 O  OD1 . ASP B 1 241 ? 24.556  30.498 79.287  1.00 35.67 ? 241 ASP B OD1 1 
ATOM   4457 O  OD2 . ASP B 1 241 ? 24.354  28.355 78.860  1.00 35.06 ? 241 ASP B OD2 1 
ATOM   4458 N  N   . LYS B 1 242 ? 22.805  31.444 81.859  1.00 32.64 ? 242 LYS B N   1 
ATOM   4459 C  CA  . LYS B 1 242 ? 23.028  31.370 83.296  1.00 32.68 ? 242 LYS B CA  1 
ATOM   4460 C  C   . LYS B 1 242 ? 21.965  32.175 84.049  1.00 32.50 ? 242 LYS B C   1 
ATOM   4461 O  O   . LYS B 1 242 ? 22.272  32.871 85.018  1.00 32.61 ? 242 LYS B O   1 
ATOM   4462 C  CB  . LYS B 1 242 ? 24.455  31.805 83.663  1.00 32.62 ? 242 LYS B CB  1 
ATOM   4463 C  CG  . LYS B 1 242 ? 25.564  30.970 83.004  1.00 33.46 ? 242 LYS B CG  1 
ATOM   4464 C  CD  . LYS B 1 242 ? 25.718  29.580 83.618  1.00 34.97 ? 242 LYS B CD  1 
ATOM   4465 C  CE  . LYS B 1 242 ? 26.723  29.587 84.768  1.00 36.53 ? 242 LYS B CE  1 
ATOM   4466 N  NZ  . LYS B 1 242 ? 26.595  28.375 85.638  1.00 37.29 ? 242 LYS B NZ  1 
ATOM   4467 N  N   . PHE B 1 243 ? 20.712  32.053 83.609  1.00 32.25 ? 243 PHE B N   1 
ATOM   4468 C  CA  . PHE B 1 243 ? 19.599  32.818 84.182  1.00 32.10 ? 243 PHE B CA  1 
ATOM   4469 C  C   . PHE B 1 243 ? 19.176  32.433 85.610  1.00 32.33 ? 243 PHE B C   1 
ATOM   4470 O  O   . PHE B 1 243 ? 18.722  33.299 86.367  1.00 32.49 ? 243 PHE B O   1 
ATOM   4471 C  CB  . PHE B 1 243 ? 18.390  32.860 83.235  1.00 31.70 ? 243 PHE B CB  1 
ATOM   4472 C  CG  . PHE B 1 243 ? 17.877  31.515 82.827  1.00 31.35 ? 243 PHE B CG  1 
ATOM   4473 C  CD1 . PHE B 1 243 ? 16.853  30.904 83.537  1.00 30.98 ? 243 PHE B CD1 1 
ATOM   4474 C  CD2 . PHE B 1 243 ? 18.403  30.862 81.712  1.00 31.33 ? 243 PHE B CD2 1 
ATOM   4475 C  CE1 . PHE B 1 243 ? 16.366  29.658 83.145  1.00 31.21 ? 243 PHE B CE1 1 
ATOM   4476 C  CE2 . PHE B 1 243 ? 17.925  29.611 81.318  1.00 30.73 ? 243 PHE B CE2 1 
ATOM   4477 C  CZ  . PHE B 1 243 ? 16.906  29.009 82.038  1.00 30.85 ? 243 PHE B CZ  1 
ATOM   4478 N  N   . LYS B 1 244 ? 19.331  31.159 85.981  1.00 32.29 ? 244 LYS B N   1 
ATOM   4479 C  CA  . LYS B 1 244 ? 19.053  30.723 87.354  1.00 32.48 ? 244 LYS B CA  1 
ATOM   4480 C  C   . LYS B 1 244 ? 19.895  31.514 88.347  1.00 32.37 ? 244 LYS B C   1 
ATOM   4481 O  O   . LYS B 1 244 ? 19.445  31.827 89.440  1.00 32.55 ? 244 LYS B O   1 
ATOM   4482 C  CB  . LYS B 1 244 ? 19.297  29.224 87.536  1.00 32.44 ? 244 LYS B CB  1 
ATOM   4483 C  CG  . LYS B 1 244 ? 18.374  28.315 86.712  1.00 33.05 ? 244 LYS B CG  1 
ATOM   4484 C  CD  . LYS B 1 244 ? 18.682  26.826 86.948  1.00 33.28 ? 244 LYS B CD  1 
ATOM   4485 C  CE  . LYS B 1 244 ? 18.141  25.913 85.825  1.00 34.45 ? 244 LYS B CE  1 
ATOM   4486 N  NZ  . LYS B 1 244 ? 19.121  25.666 84.714  1.00 34.52 ? 244 LYS B NZ  1 
ATOM   4487 N  N   . ASP B 1 245 ? 21.114  31.851 87.945  1.00 32.58 ? 245 ASP B N   1 
ATOM   4488 C  CA  . ASP B 1 245 ? 22.041  32.615 88.780  1.00 32.63 ? 245 ASP B CA  1 
ATOM   4489 C  C   . ASP B 1 245 ? 21.957  34.120 88.526  1.00 32.24 ? 245 ASP B C   1 
ATOM   4490 O  O   . ASP B 1 245 ? 22.622  34.907 89.201  1.00 32.18 ? 245 ASP B O   1 
ATOM   4491 C  CB  . ASP B 1 245 ? 23.476  32.132 88.539  1.00 33.03 ? 245 ASP B CB  1 
ATOM   4492 C  CG  . ASP B 1 245 ? 23.721  30.720 89.061  1.00 34.56 ? 245 ASP B CG  1 
ATOM   4493 O  OD1 . ASP B 1 245 ? 23.508  30.490 90.274  1.00 35.93 ? 245 ASP B OD1 1 
ATOM   4494 O  OD2 . ASP B 1 245 ? 24.144  29.847 88.264  1.00 35.92 ? 245 ASP B OD2 1 
ATOM   4495 N  N   . CYS B 1 246 ? 21.140  34.517 87.552  1.00 31.90 ? 246 CYS B N   1 
ATOM   4496 C  CA  . CYS B 1 246 ? 21.083  35.913 87.128  1.00 31.07 ? 246 CYS B CA  1 
ATOM   4497 C  C   . CYS B 1 246 ? 19.682  36.352 86.698  1.00 30.14 ? 246 CYS B C   1 
ATOM   4498 O  O   . CYS B 1 246 ? 19.435  36.632 85.519  1.00 30.06 ? 246 CYS B O   1 
ATOM   4499 C  CB  . CYS B 1 246 ? 22.091  36.155 86.004  1.00 31.48 ? 246 CYS B CB  1 
ATOM   4500 S  SG  . CYS B 1 246 ? 22.456  37.885 85.719  1.00 32.75 ? 246 CYS B SG  1 
ATOM   4501 N  N   . HIS B 1 247 ? 18.765  36.409 87.659  1.00 28.86 ? 247 HIS B N   1 
ATOM   4502 C  CA  . HIS B 1 247 ? 17.407  36.866 87.378  1.00 27.68 ? 247 HIS B CA  1 
ATOM   4503 C  C   . HIS B 1 247 ? 16.968  37.910 88.385  1.00 27.15 ? 247 HIS B C   1 
ATOM   4504 O  O   . HIS B 1 247 ? 17.611  38.097 89.408  1.00 27.45 ? 247 HIS B O   1 
ATOM   4505 C  CB  . HIS B 1 247 ? 16.425  35.700 87.352  1.00 27.30 ? 247 HIS B CB  1 
ATOM   4506 C  CG  . HIS B 1 247 ? 16.352  34.947 88.640  1.00 26.24 ? 247 HIS B CG  1 
ATOM   4507 N  ND1 . HIS B 1 247 ? 17.166  33.873 88.918  1.00 25.07 ? 247 HIS B ND1 1 
ATOM   4508 C  CD2 . HIS B 1 247 ? 15.551  35.102 89.719  1.00 25.06 ? 247 HIS B CD2 1 
ATOM   4509 C  CE1 . HIS B 1 247 ? 16.873  33.401 90.115  1.00 24.38 ? 247 HIS B CE1 1 
ATOM   4510 N  NE2 . HIS B 1 247 ? 15.897  34.130 90.624  1.00 24.28 ? 247 HIS B NE2 1 
ATOM   4511 N  N   . LEU B 1 248 ? 15.866  38.581 88.083  1.00 26.25 ? 248 LEU B N   1 
ATOM   4512 C  CA  . LEU B 1 248 ? 15.363  39.655 88.913  1.00 25.31 ? 248 LEU B CA  1 
ATOM   4513 C  C   . LEU B 1 248 ? 14.252  39.189 89.836  1.00 25.27 ? 248 LEU B C   1 
ATOM   4514 O  O   . LEU B 1 248 ? 14.033  39.775 90.896  1.00 25.37 ? 248 LEU B O   1 
ATOM   4515 C  CB  . LEU B 1 248 ? 14.866  40.790 88.027  1.00 25.32 ? 248 LEU B CB  1 
ATOM   4516 C  CG  . LEU B 1 248 ? 15.763  42.006 87.789  1.00 24.64 ? 248 LEU B CG  1 
ATOM   4517 C  CD1 . LEU B 1 248 ? 17.241  41.649 87.761  1.00 22.98 ? 248 LEU B CD1 1 
ATOM   4518 C  CD2 . LEU B 1 248 ? 15.326  42.735 86.515  1.00 24.62 ? 248 LEU B CD2 1 
ATOM   4519 N  N   . ALA B 1 249 ? 13.551  38.139 89.421  1.00 25.17 ? 249 ALA B N   1 
ATOM   4520 C  CA  . ALA B 1 249 ? 12.498  37.522 90.216  1.00 25.06 ? 249 ALA B CA  1 
ATOM   4521 C  C   . ALA B 1 249 ? 12.098  36.150 89.648  1.00 25.02 ? 249 ALA B C   1 
ATOM   4522 O  O   . ALA B 1 249 ? 12.277  35.897 88.450  1.00 25.14 ? 249 ALA B O   1 
ATOM   4523 C  CB  . ALA B 1 249 ? 11.300  38.438 90.273  1.00 25.01 ? 249 ALA B CB  1 
ATOM   4524 N  N   . ARG B 1 250 ? 11.592  35.265 90.518  1.00 24.71 ? 250 ARG B N   1 
ATOM   4525 C  CA  . ARG B 1 250 ? 10.906  34.031 90.101  1.00 24.14 ? 250 ARG B CA  1 
ATOM   4526 C  C   . ARG B 1 250 ? 9.439   34.198 90.413  1.00 24.05 ? 250 ARG B C   1 
ATOM   4527 O  O   . ARG B 1 250 ? 9.075   34.470 91.550  1.00 24.48 ? 250 ARG B O   1 
ATOM   4528 C  CB  . ARG B 1 250 ? 11.435  32.784 90.825  1.00 24.07 ? 250 ARG B CB  1 
ATOM   4529 C  CG  . ARG B 1 250 ? 10.582  31.535 90.545  1.00 23.95 ? 250 ARG B CG  1 
ATOM   4530 C  CD  . ARG B 1 250 ? 11.212  30.230 90.982  1.00 23.97 ? 250 ARG B CD  1 
ATOM   4531 N  NE  . ARG B 1 250 ? 11.375  30.155 92.432  1.00 24.04 ? 250 ARG B NE  1 
ATOM   4532 C  CZ  . ARG B 1 250 ? 12.175  29.292 93.057  1.00 23.90 ? 250 ARG B CZ  1 
ATOM   4533 N  NH1 . ARG B 1 250 ? 12.895  28.409 92.366  1.00 23.56 ? 250 ARG B NH1 1 
ATOM   4534 N  NH2 . ARG B 1 250 ? 12.266  29.317 94.378  1.00 23.50 ? 250 ARG B NH2 1 
ATOM   4535 N  N   . VAL B 1 251 ? 8.596   34.034 89.406  1.00 23.85 ? 251 VAL B N   1 
ATOM   4536 C  CA  . VAL B 1 251 ? 7.172   34.284 89.566  1.00 23.78 ? 251 VAL B CA  1 
ATOM   4537 C  C   . VAL B 1 251 ? 6.386   33.129 88.970  1.00 23.89 ? 251 VAL B C   1 
ATOM   4538 O  O   . VAL B 1 251 ? 6.880   32.467 88.054  1.00 24.25 ? 251 VAL B O   1 
ATOM   4539 C  CB  . VAL B 1 251 ? 6.749   35.606 88.886  1.00 23.85 ? 251 VAL B CB  1 
ATOM   4540 C  CG1 . VAL B 1 251 ? 7.362   36.813 89.618  1.00 24.05 ? 251 VAL B CG1 1 
ATOM   4541 C  CG2 . VAL B 1 251 ? 7.127   35.605 87.404  1.00 23.50 ? 251 VAL B CG2 1 
ATOM   4542 N  N   . PRO B 1 252 ? 5.154   32.887 89.471  1.00 23.66 ? 252 PRO B N   1 
ATOM   4543 C  CA  . PRO B 1 252 ? 4.406   31.752 88.952  1.00 22.82 ? 252 PRO B CA  1 
ATOM   4544 C  C   . PRO B 1 252 ? 3.916   32.090 87.569  1.00 22.12 ? 252 PRO B C   1 
ATOM   4545 O  O   . PRO B 1 252 ? 3.824   33.260 87.211  1.00 21.71 ? 252 PRO B O   1 
ATOM   4546 C  CB  . PRO B 1 252 ? 3.230   31.628 89.917  1.00 22.86 ? 252 PRO B CB  1 
ATOM   4547 C  CG  . PRO B 1 252 ? 3.029   32.999 90.447  1.00 23.68 ? 252 PRO B CG  1 
ATOM   4548 C  CD  . PRO B 1 252 ? 4.383   33.646 90.479  1.00 23.91 ? 252 PRO B CD  1 
ATOM   4549 N  N   . SER B 1 253 ? 3.616   31.058 86.800  1.00 21.65 ? 253 SER B N   1 
ATOM   4550 C  CA  . SER B 1 253 ? 3.245   31.225 85.419  1.00 21.36 ? 253 SER B CA  1 
ATOM   4551 C  C   . SER B 1 253 ? 1.888   31.896 85.261  1.00 21.05 ? 253 SER B C   1 
ATOM   4552 O  O   . SER B 1 253 ? 1.065   31.884 86.169  1.00 20.75 ? 253 SER B O   1 
ATOM   4553 C  CB  . SER B 1 253 ? 3.261   29.872 84.709  1.00 21.32 ? 253 SER B CB  1 
ATOM   4554 O  OG  . SER B 1 253 ? 2.342   28.976 85.289  1.00 21.80 ? 253 SER B OG  1 
ATOM   4555 N  N   . HIS B 1 254 ? 1.682   32.496 84.092  1.00 20.99 ? 254 HIS B N   1 
ATOM   4556 C  CA  . HIS B 1 254 ? 0.365   32.940 83.652  1.00 20.81 ? 254 HIS B CA  1 
ATOM   4557 C  C   . HIS B 1 254 ? -0.721  31.889 83.934  1.00 20.86 ? 254 HIS B C   1 
ATOM   4558 O  O   . HIS B 1 254 ? -0.446  30.681 83.996  1.00 20.92 ? 254 HIS B O   1 
ATOM   4559 C  CB  . HIS B 1 254 ? 0.397   33.278 82.161  1.00 20.51 ? 254 HIS B CB  1 
ATOM   4560 C  CG  . HIS B 1 254 ? 1.351   34.380 81.807  1.00 20.68 ? 254 HIS B CG  1 
ATOM   4561 N  ND1 . HIS B 1 254 ? 1.543   34.805 80.511  1.00 20.63 ? 254 HIS B ND1 1 
ATOM   4562 C  CD2 . HIS B 1 254 ? 2.181   35.129 82.574  1.00 20.83 ? 254 HIS B CD2 1 
ATOM   4563 C  CE1 . HIS B 1 254 ? 2.430   35.785 80.497  1.00 20.68 ? 254 HIS B CE1 1 
ATOM   4564 N  NE2 . HIS B 1 254 ? 2.836   35.999 81.735  1.00 20.08 ? 254 HIS B NE2 1 
ATOM   4565 N  N   . ALA B 1 255 ? -1.953  32.351 84.117  1.00 20.69 ? 255 ALA B N   1 
ATOM   4566 C  CA  . ALA B 1 255 ? -3.038  31.456 84.481  1.00 20.50 ? 255 ALA B CA  1 
ATOM   4567 C  C   . ALA B 1 255 ? -4.354  31.875 83.866  1.00 20.52 ? 255 ALA B C   1 
ATOM   4568 O  O   . ALA B 1 255 ? -4.576  33.060 83.584  1.00 20.56 ? 255 ALA B O   1 
ATOM   4569 C  CB  . ALA B 1 255 ? -3.171  31.379 85.986  1.00 20.37 ? 255 ALA B CB  1 
ATOM   4570 N  N   . VAL B 1 256 ? -5.217  30.886 83.652  1.00 20.30 ? 256 VAL B N   1 
ATOM   4571 C  CA  . VAL B 1 256 ? -6.606  31.135 83.318  1.00 20.19 ? 256 VAL B CA  1 
ATOM   4572 C  C   . VAL B 1 256 ? -7.332  31.561 84.591  1.00 20.30 ? 256 VAL B C   1 
ATOM   4573 O  O   . VAL B 1 256 ? -7.166  30.945 85.648  1.00 20.36 ? 256 VAL B O   1 
ATOM   4574 C  CB  . VAL B 1 256 ? -7.277  29.890 82.744  1.00 20.07 ? 256 VAL B CB  1 
ATOM   4575 C  CG1 . VAL B 1 256 ? -8.724  30.183 82.372  1.00 20.25 ? 256 VAL B CG1 1 
ATOM   4576 C  CG2 . VAL B 1 256 ? -6.515  29.402 81.533  1.00 20.65 ? 256 VAL B CG2 1 
ATOM   4577 N  N   . VAL B 1 257 ? -8.118  32.628 84.494  1.00 20.26 ? 257 VAL B N   1 
ATOM   4578 C  CA  . VAL B 1 257 ? -8.913  33.078 85.625  1.00 19.92 ? 257 VAL B CA  1 
ATOM   4579 C  C   . VAL B 1 257 ? -10.390 32.975 85.329  1.00 19.93 ? 257 VAL B C   1 
ATOM   4580 O  O   . VAL B 1 257 ? -10.797 32.930 84.170  1.00 20.18 ? 257 VAL B O   1 
ATOM   4581 C  CB  . VAL B 1 257 ? -8.598  34.516 86.016  1.00 19.89 ? 257 VAL B CB  1 
ATOM   4582 C  CG1 . VAL B 1 257 ? -7.162  34.618 86.510  1.00 19.87 ? 257 VAL B CG1 1 
ATOM   4583 C  CG2 . VAL B 1 257 ? -8.882  35.459 84.849  1.00 19.65 ? 257 VAL B CG2 1 
ATOM   4584 N  N   . ALA B 1 258 ? -11.177 32.949 86.400  1.00 20.03 ? 258 ALA B N   1 
ATOM   4585 C  CA  . ALA B 1 258 ? -12.628 32.784 86.347  1.00 20.08 ? 258 ALA B CA  1 
ATOM   4586 C  C   . ALA B 1 258 ? -13.238 33.406 87.593  1.00 19.91 ? 258 ALA B C   1 
ATOM   4587 O  O   . ALA B 1 258 ? -12.518 33.795 88.503  1.00 19.34 ? 258 ALA B O   1 
ATOM   4588 C  CB  . ALA B 1 258 ? -13.001 31.291 86.256  1.00 19.67 ? 258 ALA B CB  1 
ATOM   4589 N  N   . ARG B 1 259 ? -14.563 33.496 87.620  1.00 20.46 ? 259 ARG B N   1 
ATOM   4590 C  CA  . ARG B 1 259 ? -15.290 33.985 88.786  1.00 21.07 ? 259 ARG B CA  1 
ATOM   4591 C  C   . ARG B 1 259 ? -15.014 33.125 90.021  1.00 21.92 ? 259 ARG B C   1 
ATOM   4592 O  O   . ARG B 1 259 ? -14.774 31.922 89.907  1.00 22.16 ? 259 ARG B O   1 
ATOM   4593 C  CB  . ARG B 1 259 ? -16.799 34.053 88.503  1.00 20.72 ? 259 ARG B CB  1 
ATOM   4594 C  CG  . ARG B 1 259 ? -17.217 35.197 87.591  1.00 20.09 ? 259 ARG B CG  1 
ATOM   4595 C  CD  . ARG B 1 259 ? -18.713 35.176 87.265  1.00 20.28 ? 259 ARG B CD  1 
ATOM   4596 N  NE  . ARG B 1 259 ? -19.125 33.916 86.652  1.00 18.77 ? 259 ARG B NE  1 
ATOM   4597 C  CZ  . ARG B 1 259 ? -18.982 33.624 85.366  1.00 18.73 ? 259 ARG B CZ  1 
ATOM   4598 N  NH1 . ARG B 1 259 ? -18.442 34.502 84.537  1.00 20.12 ? 259 ARG B NH1 1 
ATOM   4599 N  NH2 . ARG B 1 259 ? -19.367 32.447 84.905  1.00 18.67 ? 259 ARG B NH2 1 
ATOM   4600 N  N   . SER B 1 260 ? -15.025 33.764 91.191  1.00 22.98 ? 260 SER B N   1 
ATOM   4601 C  CA  . SER B 1 260 ? -14.938 33.068 92.476  1.00 24.14 ? 260 SER B CA  1 
ATOM   4602 C  C   . SER B 1 260 ? -16.203 32.272 92.774  1.00 24.76 ? 260 SER B C   1 
ATOM   4603 O  O   . SER B 1 260 ? -16.146 31.269 93.479  1.00 25.19 ? 260 SER B O   1 
ATOM   4604 C  CB  . SER B 1 260 ? -14.687 34.058 93.616  1.00 23.99 ? 260 SER B CB  1 
ATOM   4605 O  OG  . SER B 1 260 ? -13.336 34.481 93.624  1.00 24.90 ? 260 SER B OG  1 
ATOM   4606 N  N   . VAL B 1 261 ? -17.336 32.737 92.249  1.00 25.44 ? 261 VAL B N   1 
ATOM   4607 C  CA  . VAL B 1 261 ? -18.640 32.107 92.468  1.00 26.07 ? 261 VAL B CA  1 
ATOM   4608 C  C   . VAL B 1 261 ? -19.370 31.947 91.127  1.00 26.58 ? 261 VAL B C   1 
ATOM   4609 O  O   . VAL B 1 261 ? -19.510 32.917 90.371  1.00 26.68 ? 261 VAL B O   1 
ATOM   4610 C  CB  . VAL B 1 261 ? -19.524 32.930 93.457  1.00 26.03 ? 261 VAL B CB  1 
ATOM   4611 C  CG1 . VAL B 1 261 ? -20.737 32.117 93.908  1.00 25.72 ? 261 VAL B CG1 1 
ATOM   4612 C  CG2 . VAL B 1 261 ? -18.715 33.390 94.668  1.00 25.97 ? 261 VAL B CG2 1 
ATOM   4613 N  N   . ASN B 1 262 ? -19.845 30.732 90.850  1.00 26.98 ? 262 ASN B N   1 
ATOM   4614 C  CA  . ASN B 1 262 ? -20.410 30.385 89.540  1.00 27.45 ? 262 ASN B CA  1 
ATOM   4615 C  C   . ASN B 1 262 ? -19.434 30.728 88.422  1.00 27.29 ? 262 ASN B C   1 
ATOM   4616 O  O   . ASN B 1 262 ? -19.773 31.436 87.470  1.00 27.20 ? 262 ASN B O   1 
ATOM   4617 C  CB  . ASN B 1 262 ? -21.761 31.062 89.318  1.00 27.76 ? 262 ASN B CB  1 
ATOM   4618 C  CG  . ASN B 1 262 ? -22.673 30.902 90.503  1.00 29.39 ? 262 ASN B CG  1 
ATOM   4619 O  OD1 . ASN B 1 262 ? -23.218 29.819 90.735  1.00 31.70 ? 262 ASN B OD1 1 
ATOM   4620 N  ND2 . ASN B 1 262 ? -22.836 31.977 91.281  1.00 30.34 ? 262 ASN B ND2 1 
ATOM   4621 N  N   . GLY B 1 263 ? -18.211 30.227 88.575  1.00 27.18 ? 263 GLY B N   1 
ATOM   4622 C  CA  . GLY B 1 263 ? -17.155 30.430 87.610  1.00 27.04 ? 263 GLY B CA  1 
ATOM   4623 C  C   . GLY B 1 263 ? -17.153 29.412 86.489  1.00 27.14 ? 263 GLY B C   1 
ATOM   4624 O  O   . GLY B 1 263 ? -16.545 29.655 85.457  1.00 27.36 ? 263 GLY B O   1 
ATOM   4625 N  N   . LYS B 1 264 ? -17.843 28.287 86.682  1.00 27.20 ? 264 LYS B N   1 
ATOM   4626 C  CA  . LYS B 1 264 ? -17.778 27.135 85.770  1.00 27.37 ? 264 LYS B CA  1 
ATOM   4627 C  C   . LYS B 1 264 ? -16.419 26.434 85.871  1.00 27.93 ? 264 LYS B C   1 
ATOM   4628 O  O   . LYS B 1 264 ? -15.926 25.875 84.877  1.00 28.06 ? 264 LYS B O   1 
ATOM   4629 C  CB  . LYS B 1 264 ? -18.045 27.538 84.310  1.00 27.06 ? 264 LYS B CB  1 
ATOM   4630 C  CG  . LYS B 1 264 ? -19.434 28.054 84.015  1.00 27.02 ? 264 LYS B CG  1 
ATOM   4631 C  CD  . LYS B 1 264 ? -19.589 28.394 82.536  1.00 27.09 ? 264 LYS B CD  1 
ATOM   4632 C  CE  . LYS B 1 264 ? -21.049 28.620 82.165  1.00 26.50 ? 264 LYS B CE  1 
ATOM   4633 N  NZ  . LYS B 1 264 ? -21.214 29.602 81.056  1.00 25.37 ? 264 LYS B NZ  1 
ATOM   4634 N  N   . GLU B 1 265 ? -15.820 26.461 87.064  1.00 28.21 ? 265 GLU B N   1 
ATOM   4635 C  CA  . GLU B 1 265 ? -14.456 25.959 87.264  1.00 29.00 ? 265 GLU B CA  1 
ATOM   4636 C  C   . GLU B 1 265 ? -14.280 24.541 86.732  1.00 28.01 ? 265 GLU B C   1 
ATOM   4637 O  O   . GLU B 1 265 ? -13.326 24.257 86.016  1.00 28.00 ? 265 GLU B O   1 
ATOM   4638 C  CB  . GLU B 1 265 ? -14.033 26.041 88.736  1.00 28.87 ? 265 GLU B CB  1 
ATOM   4639 C  CG  . GLU B 1 265 ? -13.802 27.472 89.239  1.00 31.28 ? 265 GLU B CG  1 
ATOM   4640 C  CD  . GLU B 1 265 ? -13.403 27.571 90.735  1.00 31.96 ? 265 GLU B CD  1 
ATOM   4641 O  OE1 . GLU B 1 265 ? -13.086 26.520 91.357  1.00 35.68 ? 265 GLU B OE1 1 
ATOM   4642 O  OE2 . GLU B 1 265 ? -13.404 28.710 91.287  1.00 34.68 ? 265 GLU B OE2 1 
ATOM   4643 N  N   . ASP B 1 266 ? -15.216 23.664 87.072  1.00 27.54 ? 266 ASP B N   1 
ATOM   4644 C  CA  . ASP B 1 266 ? -15.188 22.287 86.599  1.00 27.12 ? 266 ASP B CA  1 
ATOM   4645 C  C   . ASP B 1 266 ? -15.209 22.184 85.081  1.00 26.51 ? 266 ASP B C   1 
ATOM   4646 O  O   . ASP B 1 266 ? -14.403 21.460 84.492  1.00 26.50 ? 266 ASP B O   1 
ATOM   4647 C  CB  . ASP B 1 266 ? -16.355 21.505 87.180  1.00 27.40 ? 266 ASP B CB  1 
ATOM   4648 C  CG  . ASP B 1 266 ? -15.961 20.695 88.391  1.00 28.59 ? 266 ASP B CG  1 
ATOM   4649 O  OD1 . ASP B 1 266 ? -15.105 21.173 89.178  1.00 28.85 ? 266 ASP B OD1 1 
ATOM   4650 O  OD2 . ASP B 1 266 ? -16.509 19.573 88.548  1.00 30.04 ? 266 ASP B OD2 1 
ATOM   4651 N  N   . ALA B 1 267 ? -16.128 22.920 84.460  1.00 25.65 ? 267 ALA B N   1 
ATOM   4652 C  CA  . ALA B 1 267 ? -16.271 22.918 83.015  1.00 24.73 ? 267 ALA B CA  1 
ATOM   4653 C  C   . ALA B 1 267 ? -15.041 23.504 82.317  1.00 24.34 ? 267 ALA B C   1 
ATOM   4654 O  O   . ALA B 1 267 ? -14.636 23.025 81.262  1.00 24.52 ? 267 ALA B O   1 
ATOM   4655 C  CB  . ALA B 1 267 ? -17.527 23.646 82.612  1.00 24.47 ? 267 ALA B CB  1 
ATOM   4656 N  N   . ILE B 1 268 ? -14.438 24.529 82.902  1.00 23.63 ? 268 ILE B N   1 
ATOM   4657 C  CA  . ILE B 1 268 ? -13.231 25.084 82.320  1.00 23.12 ? 268 ILE B CA  1 
ATOM   4658 C  C   . ILE B 1 268 ? -12.133 24.034 82.317  1.00 22.98 ? 268 ILE B C   1 
ATOM   4659 O  O   . ILE B 1 268 ? -11.533 23.771 81.279  1.00 23.01 ? 268 ILE B O   1 
ATOM   4660 C  CB  . ILE B 1 268 ? -12.767 26.356 83.050  1.00 23.08 ? 268 ILE B CB  1 
ATOM   4661 C  CG1 . ILE B 1 268 ? -13.733 27.499 82.749  1.00 23.01 ? 268 ILE B CG1 1 
ATOM   4662 C  CG2 . ILE B 1 268 ? -11.342 26.729 82.646  1.00 21.95 ? 268 ILE B CG2 1 
ATOM   4663 C  CD1 . ILE B 1 268 ? -13.865 28.496 83.859  1.00 23.06 ? 268 ILE B CD1 1 
ATOM   4664 N  N   . TRP B 1 269 ? -11.885 23.424 83.472  1.00 22.87 ? 269 TRP B N   1 
ATOM   4665 C  CA  . TRP B 1 269 ? -10.808 22.446 83.587  1.00 22.76 ? 269 TRP B CA  1 
ATOM   4666 C  C   . TRP B 1 269 ? -11.039 21.243 82.670  1.00 22.82 ? 269 TRP B C   1 
ATOM   4667 O  O   . TRP B 1 269 ? -10.109 20.734 82.060  1.00 22.74 ? 269 TRP B O   1 
ATOM   4668 C  CB  . TRP B 1 269 ? -10.584 22.003 85.041  1.00 22.45 ? 269 TRP B CB  1 
ATOM   4669 C  CG  . TRP B 1 269 ? -9.579  20.906 85.119  1.00 21.97 ? 269 TRP B CG  1 
ATOM   4670 C  CD1 . TRP B 1 269 ? -9.827  19.586 85.342  1.00 21.04 ? 269 TRP B CD1 1 
ATOM   4671 C  CD2 . TRP B 1 269 ? -8.169  21.020 84.900  1.00 21.56 ? 269 TRP B CD2 1 
ATOM   4672 N  NE1 . TRP B 1 269 ? -8.658  18.871 85.300  1.00 21.07 ? 269 TRP B NE1 1 
ATOM   4673 C  CE2 . TRP B 1 269 ? -7.623  19.726 85.028  1.00 21.36 ? 269 TRP B CE2 1 
ATOM   4674 C  CE3 . TRP B 1 269 ? -7.313  22.091 84.616  1.00 21.74 ? 269 TRP B CE3 1 
ATOM   4675 C  CZ2 . TRP B 1 269 ? -6.253  19.470 84.882  1.00 21.64 ? 269 TRP B CZ2 1 
ATOM   4676 C  CZ3 . TRP B 1 269 ? -5.944  21.837 84.476  1.00 21.71 ? 269 TRP B CZ3 1 
ATOM   4677 C  CH2 . TRP B 1 269 ? -5.433  20.538 84.608  1.00 21.83 ? 269 TRP B CH2 1 
ATOM   4678 N  N   . ASN B 1 270 ? -12.286 20.807 82.562  1.00 23.21 ? 270 ASN B N   1 
ATOM   4679 C  CA  . ASN B 1 270 ? -12.623 19.704 81.679  1.00 23.57 ? 270 ASN B CA  1 
ATOM   4680 C  C   . ASN B 1 270 ? -12.314 20.021 80.222  1.00 23.84 ? 270 ASN B C   1 
ATOM   4681 O  O   . ASN B 1 270 ? -11.893 19.155 79.464  1.00 24.10 ? 270 ASN B O   1 
ATOM   4682 C  CB  . ASN B 1 270 ? -14.090 19.321 81.826  1.00 23.42 ? 270 ASN B CB  1 
ATOM   4683 C  CG  . ASN B 1 270 ? -14.414 18.033 81.114  1.00 23.84 ? 270 ASN B CG  1 
ATOM   4684 O  OD1 . ASN B 1 270 ? -15.262 17.997 80.225  1.00 24.45 ? 270 ASN B OD1 1 
ATOM   4685 N  ND2 . ASN B 1 270 ? -13.712 16.969 81.475  1.00 24.22 ? 270 ASN B ND2 1 
ATOM   4686 N  N   . LEU B 1 271 ? -12.537 21.272 79.839  1.00 24.31 ? 271 LEU B N   1 
ATOM   4687 C  CA  . LEU B 1 271 ? -12.187 21.766 78.513  1.00 24.48 ? 271 LEU B CA  1 
ATOM   4688 C  C   . LEU B 1 271 ? -10.677 21.747 78.295  1.00 24.65 ? 271 LEU B C   1 
ATOM   4689 O  O   . LEU B 1 271 ? -10.208 21.278 77.262  1.00 24.97 ? 271 LEU B O   1 
ATOM   4690 C  CB  . LEU B 1 271 ? -12.732 23.186 78.321  1.00 24.31 ? 271 LEU B CB  1 
ATOM   4691 C  CG  . LEU B 1 271 ? -12.306 24.031 77.120  1.00 24.63 ? 271 LEU B CG  1 
ATOM   4692 C  CD1 . LEU B 1 271 ? -12.655 23.359 75.780  1.00 24.64 ? 271 LEU B CD1 1 
ATOM   4693 C  CD2 . LEU B 1 271 ? -12.960 25.404 77.239  1.00 24.38 ? 271 LEU B CD2 1 
ATOM   4694 N  N   . LEU B 1 272 ? -9.926  22.252 79.269  1.00 24.65 ? 272 LEU B N   1 
ATOM   4695 C  CA  . LEU B 1 272 ? -8.487  22.388 79.125  1.00 24.63 ? 272 LEU B CA  1 
ATOM   4696 C  C   . LEU B 1 272 ? -7.787  21.023 79.177  1.00 25.16 ? 272 LEU B C   1 
ATOM   4697 O  O   . LEU B 1 272 ? -6.852  20.762 78.417  1.00 25.30 ? 272 LEU B O   1 
ATOM   4698 C  CB  . LEU B 1 272 ? -7.932  23.379 80.161  1.00 24.29 ? 272 LEU B CB  1 
ATOM   4699 C  CG  . LEU B 1 272 ? -8.454  24.831 80.108  1.00 23.30 ? 272 LEU B CG  1 
ATOM   4700 C  CD1 . LEU B 1 272 ? -7.995  25.620 81.317  1.00 23.21 ? 272 LEU B CD1 1 
ATOM   4701 C  CD2 . LEU B 1 272 ? -8.038  25.560 78.853  1.00 20.80 ? 272 LEU B CD2 1 
ATOM   4702 N  N   . ARG B 1 273 ? -8.264  20.136 80.041  1.00 25.69 ? 273 ARG B N   1 
ATOM   4703 C  CA  . ARG B 1 273 ? -7.702  18.788 80.124  1.00 26.43 ? 273 ARG B CA  1 
ATOM   4704 C  C   . ARG B 1 273 ? -7.908  18.034 78.812  1.00 26.70 ? 273 ARG B C   1 
ATOM   4705 O  O   . ARG B 1 273 ? -7.042  17.276 78.363  1.00 26.90 ? 273 ARG B O   1 
ATOM   4706 C  CB  . ARG B 1 273 ? -8.342  17.999 81.268  1.00 26.32 ? 273 ARG B CB  1 
ATOM   4707 C  CG  . ARG B 1 273 ? -7.610  16.710 81.618  1.00 27.82 ? 273 ARG B CG  1 
ATOM   4708 C  CD  . ARG B 1 273 ? -8.573  15.524 81.706  1.00 30.51 ? 273 ARG B CD  1 
ATOM   4709 N  NE  . ARG B 1 273 ? -9.650  15.786 82.655  1.00 31.49 ? 273 ARG B NE  1 
ATOM   4710 C  CZ  . ARG B 1 273 ? -10.919 15.445 82.466  1.00 31.62 ? 273 ARG B CZ  1 
ATOM   4711 N  NH1 . ARG B 1 273 ? -11.285 14.823 81.349  1.00 31.37 ? 273 ARG B NH1 1 
ATOM   4712 N  NH2 . ARG B 1 273 ? -11.820 15.741 83.398  1.00 31.47 ? 273 ARG B NH2 1 
ATOM   4713 N  N   . GLN B 1 274 ? -9.068  18.241 78.208  1.00 27.00 ? 274 GLN B N   1 
ATOM   4714 C  CA  . GLN B 1 274 ? -9.436  17.491 77.043  1.00 27.38 ? 274 GLN B CA  1 
ATOM   4715 C  C   . GLN B 1 274 ? -8.821  18.139 75.814  1.00 27.55 ? 274 GLN B C   1 
ATOM   4716 O  O   . GLN B 1 274 ? -8.433  17.447 74.873  1.00 27.74 ? 274 GLN B O   1 
ATOM   4717 C  CB  . GLN B 1 274 ? -10.948 17.406 76.943  1.00 27.41 ? 274 GLN B CB  1 
ATOM   4718 C  CG  . GLN B 1 274 ? -11.439 16.034 76.529  1.00 29.12 ? 274 GLN B CG  1 
ATOM   4719 C  CD  . GLN B 1 274 ? -12.709 15.637 77.254  1.00 30.76 ? 274 GLN B CD  1 
ATOM   4720 O  OE1 . GLN B 1 274 ? -12.890 15.960 78.436  1.00 30.56 ? 274 GLN B OE1 1 
ATOM   4721 N  NE2 . GLN B 1 274 ? -13.601 14.930 76.551  1.00 31.26 ? 274 GLN B NE2 1 
ATOM   4722 N  N   . ALA B 1 275 ? -8.702  19.462 75.836  1.00 27.70 ? 275 ALA B N   1 
ATOM   4723 C  CA  . ALA B 1 275 ? -8.052  20.175 74.747  1.00 28.20 ? 275 ALA B CA  1 
ATOM   4724 C  C   . ALA B 1 275 ? -6.552  19.921 74.749  1.00 28.67 ? 275 ALA B C   1 
ATOM   4725 O  O   . ALA B 1 275 ? -5.913  19.938 73.696  1.00 28.88 ? 275 ALA B O   1 
ATOM   4726 C  CB  . ALA B 1 275 ? -8.335  21.653 74.824  1.00 28.29 ? 275 ALA B CB  1 
ATOM   4727 N  N   . GLN B 1 276 ? -5.993  19.686 75.932  1.00 29.11 ? 276 GLN B N   1 
ATOM   4728 C  CA  . GLN B 1 276 ? -4.577  19.353 76.049  1.00 29.63 ? 276 GLN B CA  1 
ATOM   4729 C  C   . GLN B 1 276 ? -4.265  17.978 75.453  1.00 29.41 ? 276 GLN B C   1 
ATOM   4730 O  O   . GLN B 1 276 ? -3.291  17.833 74.727  1.00 29.44 ? 276 GLN B O   1 
ATOM   4731 C  CB  . GLN B 1 276 ? -4.123  19.412 77.507  1.00 29.48 ? 276 GLN B CB  1 
ATOM   4732 C  CG  . GLN B 1 276 ? -2.619  19.372 77.694  1.00 30.12 ? 276 GLN B CG  1 
ATOM   4733 C  CD  . GLN B 1 276 ? -2.217  19.342 79.157  1.00 30.87 ? 276 GLN B CD  1 
ATOM   4734 O  OE1 . GLN B 1 276 ? -2.832  19.993 80.006  1.00 32.93 ? 276 GLN B OE1 1 
ATOM   4735 N  NE2 . GLN B 1 276 ? -1.174  18.590 79.458  1.00 32.51 ? 276 GLN B NE2 1 
ATOM   4736 N  N   . GLU B 1 277 ? -5.083  16.973 75.749  1.00 29.40 ? 277 GLU B N   1 
ATOM   4737 C  CA  . GLU B 1 277 ? -4.782  15.627 75.276  1.00 30.01 ? 277 GLU B CA  1 
ATOM   4738 C  C   . GLU B 1 277 ? -5.008  15.507 73.772  1.00 29.13 ? 277 GLU B C   1 
ATOM   4739 O  O   . GLU B 1 277 ? -4.291  14.779 73.089  1.00 28.95 ? 277 GLU B O   1 
ATOM   4740 C  CB  . GLU B 1 277 ? -5.527  14.537 76.077  1.00 30.02 ? 277 GLU B CB  1 
ATOM   4741 C  CG  . GLU B 1 277 ? -7.060  14.514 75.928  1.00 31.84 ? 277 GLU B CG  1 
ATOM   4742 C  CD  . GLU B 1 277 ? -7.753  13.432 76.792  1.00 32.28 ? 277 GLU B CD  1 
ATOM   4743 O  OE1 . GLU B 1 277 ? -7.316  13.175 77.950  1.00 34.36 ? 277 GLU B OE1 1 
ATOM   4744 O  OE2 . GLU B 1 277 ? -8.759  12.851 76.312  1.00 34.67 ? 277 GLU B OE2 1 
ATOM   4745 N  N   . LYS B 1 278 ? -5.978  16.255 73.259  1.00 28.67 ? 278 LYS B N   1 
ATOM   4746 C  CA  . LYS B 1 278 ? -6.306  16.198 71.842  1.00 28.14 ? 278 LYS B CA  1 
ATOM   4747 C  C   . LYS B 1 278 ? -5.526  17.169 70.949  1.00 27.86 ? 278 LYS B C   1 
ATOM   4748 O  O   . LYS B 1 278 ? -5.314  16.883 69.774  1.00 27.87 ? 278 LYS B O   1 
ATOM   4749 C  CB  . LYS B 1 278 ? -7.819  16.324 71.623  1.00 28.13 ? 278 LYS B CB  1 
ATOM   4750 C  CG  . LYS B 1 278 ? -8.604  15.000 71.738  1.00 28.47 ? 278 LYS B CG  1 
ATOM   4751 C  CD  . LYS B 1 278 ? -7.913  13.837 71.010  1.00 29.77 ? 278 LYS B CD  1 
ATOM   4752 C  CE  . LYS B 1 278 ? -8.902  12.910 70.309  1.00 30.58 ? 278 LYS B CE  1 
ATOM   4753 N  NZ  . LYS B 1 278 ? -9.752  12.170 71.281  1.00 31.56 ? 278 LYS B NZ  1 
ATOM   4754 N  N   . PHE B 1 279 ? -5.096  18.306 71.493  1.00 27.56 ? 279 PHE B N   1 
ATOM   4755 C  CA  . PHE B 1 279 ? -4.419  19.327 70.679  1.00 27.29 ? 279 PHE B CA  1 
ATOM   4756 C  C   . PHE B 1 279 ? -3.176  19.948 71.325  1.00 27.66 ? 279 PHE B C   1 
ATOM   4757 O  O   . PHE B 1 279 ? -2.747  21.036 70.931  1.00 27.70 ? 279 PHE B O   1 
ATOM   4758 C  CB  . PHE B 1 279 ? -5.406  20.424 70.256  1.00 26.66 ? 279 PHE B CB  1 
ATOM   4759 C  CG  . PHE B 1 279 ? -6.643  19.904 69.571  1.00 25.66 ? 279 PHE B CG  1 
ATOM   4760 C  CD1 . PHE B 1 279 ? -6.579  19.381 68.291  1.00 23.75 ? 279 PHE B CD1 1 
ATOM   4761 C  CD2 . PHE B 1 279 ? -7.872  19.941 70.213  1.00 24.99 ? 279 PHE B CD2 1 
ATOM   4762 C  CE1 . PHE B 1 279 ? -7.709  18.907 67.666  1.00 23.63 ? 279 PHE B CE1 1 
ATOM   4763 C  CE2 . PHE B 1 279 ? -9.005  19.471 69.589  1.00 24.15 ? 279 PHE B CE2 1 
ATOM   4764 C  CZ  . PHE B 1 279 ? -8.924  18.952 68.312  1.00 24.30 ? 279 PHE B CZ  1 
ATOM   4765 N  N   . GLY B 1 280 ? -2.597  19.259 72.307  1.00 28.05 ? 280 GLY B N   1 
ATOM   4766 C  CA  . GLY B 1 280 ? -1.376  19.725 72.967  1.00 28.65 ? 280 GLY B CA  1 
ATOM   4767 C  C   . GLY B 1 280 ? -0.145  19.438 72.128  1.00 29.22 ? 280 GLY B C   1 
ATOM   4768 O  O   . GLY B 1 280 ? -0.262  19.146 70.932  1.00 29.13 ? 280 GLY B O   1 
ATOM   4769 N  N   . LYS B 1 281 ? 1.032   19.490 72.751  1.00 29.73 ? 281 LYS B N   1 
ATOM   4770 C  CA  . LYS B 1 281 ? 2.281   19.372 72.004  1.00 30.52 ? 281 LYS B CA  1 
ATOM   4771 C  C   . LYS B 1 281 ? 2.413   18.041 71.268  1.00 30.72 ? 281 LYS B C   1 
ATOM   4772 O  O   . LYS B 1 281 ? 2.252   16.976 71.873  1.00 31.08 ? 281 LYS B O   1 
ATOM   4773 C  CB  . LYS B 1 281 ? 3.495   19.610 72.899  1.00 30.74 ? 281 LYS B CB  1 
ATOM   4774 C  CG  . LYS B 1 281 ? 4.722   19.993 72.086  1.00 32.40 ? 281 LYS B CG  1 
ATOM   4775 C  CD  . LYS B 1 281 ? 5.959   20.276 72.928  1.00 35.20 ? 281 LYS B CD  1 
ATOM   4776 C  CE  . LYS B 1 281 ? 7.191   20.455 72.027  1.00 36.30 ? 281 LYS B CE  1 
ATOM   4777 N  NZ  . LYS B 1 281 ? 7.387   19.301 71.073  1.00 36.94 ? 281 LYS B NZ  1 
ATOM   4778 N  N   . ASP B 1 282 ? 2.699   18.118 69.965  1.00 30.79 ? 282 ASP B N   1 
ATOM   4779 C  CA  . ASP B 1 282 ? 2.852   16.940 69.085  1.00 31.02 ? 282 ASP B CA  1 
ATOM   4780 C  C   . ASP B 1 282 ? 1.609   16.032 68.981  1.00 30.53 ? 282 ASP B C   1 
ATOM   4781 O  O   . ASP B 1 282 ? 1.717   14.893 68.527  1.00 30.50 ? 282 ASP B O   1 
ATOM   4782 C  CB  . ASP B 1 282 ? 4.077   16.087 69.484  1.00 31.46 ? 282 ASP B CB  1 
ATOM   4783 C  CG  . ASP B 1 282 ? 5.399   16.859 69.421  1.00 33.54 ? 282 ASP B CG  1 
ATOM   4784 O  OD1 . ASP B 1 282 ? 5.601   17.677 68.486  1.00 36.23 ? 282 ASP B OD1 1 
ATOM   4785 O  OD2 . ASP B 1 282 ? 6.250   16.631 70.314  1.00 34.74 ? 282 ASP B OD2 1 
ATOM   4786 N  N   . LYS B 1 283 ? 0.439   16.534 69.373  1.00 29.91 ? 283 LYS B N   1 
ATOM   4787 C  CA  . LYS B 1 283 ? -0.760  15.696 69.466  1.00 29.26 ? 283 LYS B CA  1 
ATOM   4788 C  C   . LYS B 1 283 ? -1.560  15.593 68.174  1.00 28.84 ? 283 LYS B C   1 
ATOM   4789 O  O   . LYS B 1 283 ? -2.118  14.548 67.879  1.00 28.72 ? 283 LYS B O   1 
ATOM   4790 C  CB  . LYS B 1 283 ? -1.669  16.178 70.600  1.00 29.38 ? 283 LYS B CB  1 
ATOM   4791 C  CG  . LYS B 1 283 ? -1.054  16.087 71.996  1.00 29.22 ? 283 LYS B CG  1 
ATOM   4792 C  CD  . LYS B 1 283 ? -0.943  14.662 72.494  1.00 28.37 ? 283 LYS B CD  1 
ATOM   4793 C  CE  . LYS B 1 283 ? -0.412  14.654 73.908  1.00 28.63 ? 283 LYS B CE  1 
ATOM   4794 N  NZ  . LYS B 1 283 ? -0.778  13.398 74.615  1.00 28.87 ? 283 LYS B NZ  1 
ATOM   4795 N  N   . SER B 1 284 ? -1.626  16.684 67.419  1.00 28.69 ? 284 SER B N   1 
ATOM   4796 C  CA  . SER B 1 284 ? -2.408  16.738 66.178  1.00 28.27 ? 284 SER B CA  1 
ATOM   4797 C  C   . SER B 1 284 ? -1.817  17.687 65.145  1.00 28.00 ? 284 SER B C   1 
ATOM   4798 O  O   . SER B 1 284 ? -1.471  18.831 65.463  1.00 27.81 ? 284 SER B O   1 
ATOM   4799 C  CB  . SER B 1 284 ? -3.856  17.160 66.449  1.00 28.35 ? 284 SER B CB  1 
ATOM   4800 O  OG  . SER B 1 284 ? -4.477  17.645 65.267  1.00 27.66 ? 284 SER B OG  1 
ATOM   4801 N  N   . PRO B 1 285 ? -1.728  17.218 63.892  1.00 27.73 ? 285 PRO B N   1 
ATOM   4802 C  CA  . PRO B 1 285 ? -1.321  18.086 62.795  1.00 27.43 ? 285 PRO B CA  1 
ATOM   4803 C  C   . PRO B 1 285 ? -2.404  19.122 62.489  1.00 27.07 ? 285 PRO B C   1 
ATOM   4804 O  O   . PRO B 1 285 ? -2.096  20.201 61.972  1.00 27.55 ? 285 PRO B O   1 
ATOM   4805 C  CB  . PRO B 1 285 ? -1.170  17.119 61.606  1.00 27.49 ? 285 PRO B CB  1 
ATOM   4806 C  CG  . PRO B 1 285 ? -1.200  15.739 62.193  1.00 27.72 ? 285 PRO B CG  1 
ATOM   4807 C  CD  . PRO B 1 285 ? -2.008  15.844 63.439  1.00 27.64 ? 285 PRO B CD  1 
ATOM   4808 N  N   . LYS B 1 286 ? -3.655  18.804 62.821  1.00 26.15 ? 286 LYS B N   1 
ATOM   4809 C  CA  . LYS B 1 286 ? -4.785  19.629 62.409  1.00 25.15 ? 286 LYS B CA  1 
ATOM   4810 C  C   . LYS B 1 286 ? -4.858  20.955 63.142  1.00 24.36 ? 286 LYS B C   1 
ATOM   4811 O  O   . LYS B 1 286 ? -4.944  21.995 62.504  1.00 24.04 ? 286 LYS B O   1 
ATOM   4812 C  CB  . LYS B 1 286 ? -6.095  18.851 62.505  1.00 25.12 ? 286 LYS B CB  1 
ATOM   4813 C  CG  . LYS B 1 286 ? -6.274  17.885 61.337  1.00 25.99 ? 286 LYS B CG  1 
ATOM   4814 C  CD  . LYS B 1 286 ? -7.364  16.867 61.606  1.00 26.98 ? 286 LYS B CD  1 
ATOM   4815 C  CE  . LYS B 1 286 ? -7.247  15.689 60.669  1.00 26.87 ? 286 LYS B CE  1 
ATOM   4816 N  NZ  . LYS B 1 286 ? -7.961  14.533 61.246  1.00 27.35 ? 286 LYS B NZ  1 
ATOM   4817 N  N   . PHE B 1 287 ? -4.796  20.911 64.470  1.00 23.69 ? 287 PHE B N   1 
ATOM   4818 C  CA  . PHE B 1 287 ? -4.864  22.113 65.298  1.00 23.06 ? 287 PHE B CA  1 
ATOM   4819 C  C   . PHE B 1 287 ? -3.920  22.075 66.513  1.00 23.05 ? 287 PHE B C   1 
ATOM   4820 O  O   . PHE B 1 287 ? -3.713  21.028 67.116  1.00 22.97 ? 287 PHE B O   1 
ATOM   4821 C  CB  . PHE B 1 287 ? -6.316  22.375 65.725  1.00 22.68 ? 287 PHE B CB  1 
ATOM   4822 C  CG  . PHE B 1 287 ? -6.468  23.492 66.726  1.00 21.96 ? 287 PHE B CG  1 
ATOM   4823 C  CD1 . PHE B 1 287 ? -6.307  24.811 66.342  1.00 20.27 ? 287 PHE B CD1 1 
ATOM   4824 C  CD2 . PHE B 1 287 ? -6.764  23.214 68.058  1.00 21.24 ? 287 PHE B CD2 1 
ATOM   4825 C  CE1 . PHE B 1 287 ? -6.433  25.830 67.259  1.00 20.03 ? 287 PHE B CE1 1 
ATOM   4826 C  CE2 . PHE B 1 287 ? -6.893  24.236 68.979  1.00 20.57 ? 287 PHE B CE2 1 
ATOM   4827 C  CZ  . PHE B 1 287 ? -6.728  25.543 68.575  1.00 20.91 ? 287 PHE B CZ  1 
ATOM   4828 N  N   . GLN B 1 288 ? -3.348  23.222 66.863  1.00 23.37 ? 288 GLN B N   1 
ATOM   4829 C  CA  . GLN B 1 288 ? -2.485  23.320 68.037  1.00 23.89 ? 288 GLN B CA  1 
ATOM   4830 C  C   . GLN B 1 288 ? -2.953  24.384 68.983  1.00 23.86 ? 288 GLN B C   1 
ATOM   4831 O  O   . GLN B 1 288 ? -3.069  25.548 68.616  1.00 24.20 ? 288 GLN B O   1 
ATOM   4832 C  CB  . GLN B 1 288 ? -1.064  23.647 67.645  1.00 23.95 ? 288 GLN B CB  1 
ATOM   4833 C  CG  . GLN B 1 288 ? -0.437  22.599 66.805  1.00 25.87 ? 288 GLN B CG  1 
ATOM   4834 C  CD  . GLN B 1 288 ? 0.216   23.204 65.610  1.00 28.45 ? 288 GLN B CD  1 
ATOM   4835 O  OE1 . GLN B 1 288 ? -0.189  22.937 64.476  1.00 29.53 ? 288 GLN B OE1 1 
ATOM   4836 N  NE2 . GLN B 1 288 ? 1.216   24.061 65.847  1.00 28.87 ? 288 GLN B NE2 1 
ATOM   4837 N  N   . LEU B 1 289 ? -3.196  23.972 70.214  1.00 23.91 ? 289 LEU B N   1 
ATOM   4838 C  CA  . LEU B 1 289 ? -3.654  24.866 71.248  1.00 23.99 ? 289 LEU B CA  1 
ATOM   4839 C  C   . LEU B 1 289 ? -2.533  25.842 71.614  1.00 24.04 ? 289 LEU B C   1 
ATOM   4840 O  O   . LEU B 1 289 ? -2.780  27.024 71.835  1.00 23.82 ? 289 LEU B O   1 
ATOM   4841 C  CB  . LEU B 1 289 ? -4.088  24.036 72.466  1.00 23.96 ? 289 LEU B CB  1 
ATOM   4842 C  CG  . LEU B 1 289 ? -4.940  24.699 73.543  1.00 23.99 ? 289 LEU B CG  1 
ATOM   4843 C  CD1 . LEU B 1 289 ? -6.308  25.103 72.985  1.00 23.67 ? 289 LEU B CD1 1 
ATOM   4844 C  CD2 . LEU B 1 289 ? -5.080  23.744 74.711  1.00 23.89 ? 289 LEU B CD2 1 
ATOM   4845 N  N   . PHE B 1 290 ? -1.304  25.330 71.657  1.00 24.19 ? 290 PHE B N   1 
ATOM   4846 C  CA  . PHE B 1 290 ? -0.145  26.106 72.085  1.00 24.54 ? 290 PHE B CA  1 
ATOM   4847 C  C   . PHE B 1 290 ? 0.708   26.602 70.894  1.00 24.80 ? 290 PHE B C   1 
ATOM   4848 O  O   . PHE B 1 290 ? 1.940   26.649 70.953  1.00 25.29 ? 290 PHE B O   1 
ATOM   4849 C  CB  . PHE B 1 290 ? 0.708   25.290 73.073  1.00 24.32 ? 290 PHE B CB  1 
ATOM   4850 C  CG  . PHE B 1 290 ? -0.047  24.794 74.278  1.00 24.14 ? 290 PHE B CG  1 
ATOM   4851 C  CD1 . PHE B 1 290 ? -0.615  25.684 75.187  1.00 24.46 ? 290 PHE B CD1 1 
ATOM   4852 C  CD2 . PHE B 1 290 ? -0.161  23.436 74.527  1.00 23.59 ? 290 PHE B CD2 1 
ATOM   4853 C  CE1 . PHE B 1 290 ? -1.304  25.220 76.313  1.00 23.62 ? 290 PHE B CE1 1 
ATOM   4854 C  CE2 . PHE B 1 290 ? -0.841  22.968 75.652  1.00 22.73 ? 290 PHE B CE2 1 
ATOM   4855 C  CZ  . PHE B 1 290 ? -1.418  23.860 76.536  1.00 22.90 ? 290 PHE B CZ  1 
ATOM   4856 N  N   . GLY B 1 291 ? 0.045   26.984 69.813  1.00 24.71 ? 291 GLY B N   1 
ATOM   4857 C  CA  . GLY B 1 291 ? 0.738   27.514 68.652  1.00 24.11 ? 291 GLY B CA  1 
ATOM   4858 C  C   . GLY B 1 291 ? -0.039  28.656 68.045  1.00 23.81 ? 291 GLY B C   1 
ATOM   4859 O  O   . GLY B 1 291 ? -1.273  28.692 68.106  1.00 23.76 ? 291 GLY B O   1 
ATOM   4860 N  N   . SER B 1 292 ? 0.699   29.591 67.458  1.00 23.48 ? 292 SER B N   1 
ATOM   4861 C  CA  . SER B 1 292 ? 0.128   30.734 66.762  1.00 22.97 ? 292 SER B CA  1 
ATOM   4862 C  C   . SER B 1 292 ? 0.625   30.736 65.325  1.00 22.76 ? 292 SER B C   1 
ATOM   4863 O  O   . SER B 1 292 ? 1.757   30.341 65.069  1.00 22.50 ? 292 SER B O   1 
ATOM   4864 C  CB  . SER B 1 292 ? 0.542   32.030 67.457  1.00 22.84 ? 292 SER B CB  1 
ATOM   4865 O  OG  . SER B 1 292 ? 0.188   32.009 68.834  1.00 22.81 ? 292 SER B OG  1 
ATOM   4866 N  N   . PRO B 1 293 ? -0.221  31.169 64.374  1.00 22.78 ? 293 PRO B N   1 
ATOM   4867 C  CA  . PRO B 1 293 ? 0.268   31.307 62.994  1.00 22.81 ? 293 PRO B CA  1 
ATOM   4868 C  C   . PRO B 1 293 ? 1.488   32.238 62.885  1.00 22.93 ? 293 PRO B C   1 
ATOM   4869 O  O   . PRO B 1 293 ? 1.797   32.964 63.829  1.00 22.81 ? 293 PRO B O   1 
ATOM   4870 C  CB  . PRO B 1 293 ? -0.934  31.886 62.242  1.00 22.73 ? 293 PRO B CB  1 
ATOM   4871 C  CG  . PRO B 1 293 ? -1.899  32.326 63.286  1.00 22.78 ? 293 PRO B CG  1 
ATOM   4872 C  CD  . PRO B 1 293 ? -1.645  31.518 64.504  1.00 22.52 ? 293 PRO B CD  1 
ATOM   4873 N  N   . SER B 1 294 ? 2.188   32.187 61.754  1.00 23.16 ? 294 SER B N   1 
ATOM   4874 C  CA  . SER B 1 294 ? 3.336   33.059 61.510  1.00 23.48 ? 294 SER B CA  1 
ATOM   4875 C  C   . SER B 1 294 ? 2.927   34.525 61.627  1.00 23.72 ? 294 SER B C   1 
ATOM   4876 O  O   . SER B 1 294 ? 1.880   34.921 61.118  1.00 23.74 ? 294 SER B O   1 
ATOM   4877 C  CB  . SER B 1 294 ? 3.932   32.778 60.127  1.00 23.44 ? 294 SER B CB  1 
ATOM   4878 O  OG  . SER B 1 294 ? 5.055   33.602 59.855  1.00 23.45 ? 294 SER B OG  1 
ATOM   4879 N  N   . GLY B 1 295 ? 3.748   35.318 62.311  1.00 24.13 ? 295 GLY B N   1 
ATOM   4880 C  CA  . GLY B 1 295 ? 3.492   36.752 62.469  1.00 24.74 ? 295 GLY B CA  1 
ATOM   4881 C  C   . GLY B 1 295 ? 2.606   37.117 63.653  1.00 25.26 ? 295 GLY B C   1 
ATOM   4882 O  O   . GLY B 1 295 ? 2.321   38.297 63.875  1.00 25.30 ? 295 GLY B O   1 
ATOM   4883 N  N   . GLN B 1 296 ? 2.172   36.101 64.402  1.00 25.51 ? 296 GLN B N   1 
ATOM   4884 C  CA  . GLN B 1 296 ? 1.362   36.263 65.611  1.00 25.90 ? 296 GLN B CA  1 
ATOM   4885 C  C   . GLN B 1 296 ? 2.055   35.527 66.741  1.00 25.98 ? 296 GLN B C   1 
ATOM   4886 O  O   . GLN B 1 296 ? 2.722   34.521 66.496  1.00 25.95 ? 296 GLN B O   1 
ATOM   4887 C  CB  . GLN B 1 296 ? -0.027  35.640 65.428  1.00 26.13 ? 296 GLN B CB  1 
ATOM   4888 C  CG  . GLN B 1 296 ? -0.818  36.122 64.231  1.00 26.86 ? 296 GLN B CG  1 
ATOM   4889 C  CD  . GLN B 1 296 ? -1.187  37.588 64.339  1.00 28.97 ? 296 GLN B CD  1 
ATOM   4890 O  OE1 . GLN B 1 296 ? -1.330  38.136 65.450  1.00 28.35 ? 296 GLN B OE1 1 
ATOM   4891 N  NE2 . GLN B 1 296 ? -1.346  38.241 63.181  1.00 29.19 ? 296 GLN B NE2 1 
ATOM   4892 N  N   . LYS B 1 297 ? 1.889   36.005 67.976  1.00 26.15 ? 297 LYS B N   1 
ATOM   4893 C  CA  . LYS B 1 297 ? 2.566   35.383 69.120  1.00 26.32 ? 297 LYS B CA  1 
ATOM   4894 C  C   . LYS B 1 297 ? 1.658   35.155 70.298  1.00 26.05 ? 297 LYS B C   1 
ATOM   4895 O  O   . LYS B 1 297 ? 0.876   36.031 70.662  1.00 26.05 ? 297 LYS B O   1 
ATOM   4896 C  CB  . LYS B 1 297 ? 3.774   36.199 69.570  1.00 26.45 ? 297 LYS B CB  1 
ATOM   4897 C  CG  . LYS B 1 297 ? 4.820   36.332 68.498  1.00 29.03 ? 297 LYS B CG  1 
ATOM   4898 C  CD  . LYS B 1 297 ? 6.235   36.259 69.036  1.00 32.64 ? 297 LYS B CD  1 
ATOM   4899 C  CE  . LYS B 1 297 ? 7.244   36.284 67.881  1.00 33.64 ? 297 LYS B CE  1 
ATOM   4900 N  NZ  . LYS B 1 297 ? 7.206   34.999 67.131  1.00 34.66 ? 297 LYS B NZ  1 
ATOM   4901 N  N   . ASP B 1 298 ? 1.773   33.968 70.887  1.00 25.86 ? 298 ASP B N   1 
ATOM   4902 C  CA  . ASP B 1 298 ? 1.115   33.654 72.147  1.00 26.09 ? 298 ASP B CA  1 
ATOM   4903 C  C   . ASP B 1 298 ? -0.382  33.972 72.144  1.00 25.52 ? 298 ASP B C   1 
ATOM   4904 O  O   . ASP B 1 298 ? -0.888  34.639 73.047  1.00 25.31 ? 298 ASP B O   1 
ATOM   4905 C  CB  . ASP B 1 298 ? 1.795   34.401 73.307  1.00 26.51 ? 298 ASP B CB  1 
ATOM   4906 C  CG  . ASP B 1 298 ? 3.268   34.041 73.475  1.00 28.55 ? 298 ASP B CG  1 
ATOM   4907 O  OD1 . ASP B 1 298 ? 3.722   32.983 72.966  1.00 29.52 ? 298 ASP B OD1 1 
ATOM   4908 O  OD2 . ASP B 1 298 ? 3.974   34.838 74.145  1.00 31.48 ? 298 ASP B OD2 1 
ATOM   4909 N  N   . LEU B 1 299 ? -1.087  33.489 71.129  1.00 24.99 ? 299 LEU B N   1 
ATOM   4910 C  CA  . LEU B 1 299 ? -2.525  33.683 71.050  1.00 24.57 ? 299 LEU B CA  1 
ATOM   4911 C  C   . LEU B 1 299 ? -3.248  32.761 72.047  1.00 24.76 ? 299 LEU B C   1 
ATOM   4912 O  O   . LEU B 1 299 ? -3.066  31.538 72.025  1.00 24.83 ? 299 LEU B O   1 
ATOM   4913 C  CB  . LEU B 1 299 ? -3.008  33.448 69.616  1.00 24.37 ? 299 LEU B CB  1 
ATOM   4914 C  CG  . LEU B 1 299 ? -2.408  34.263 68.450  1.00 23.77 ? 299 LEU B CG  1 
ATOM   4915 C  CD1 . LEU B 1 299 ? -3.094  33.928 67.126  1.00 23.14 ? 299 LEU B CD1 1 
ATOM   4916 C  CD2 . LEU B 1 299 ? -2.443  35.765 68.686  1.00 22.12 ? 299 LEU B CD2 1 
ATOM   4917 N  N   . LEU B 1 300 ? -4.048  33.360 72.931  1.00 24.70 ? 300 LEU B N   1 
ATOM   4918 C  CA  . LEU B 1 300 ? -4.814  32.640 73.968  1.00 24.78 ? 300 LEU B CA  1 
ATOM   4919 C  C   . LEU B 1 300 ? -3.953  32.010 75.055  1.00 24.92 ? 300 LEU B C   1 
ATOM   4920 O  O   . LEU B 1 300 ? -4.282  32.115 76.239  1.00 25.04 ? 300 LEU B O   1 
ATOM   4921 C  CB  . LEU B 1 300 ? -5.726  31.568 73.370  1.00 24.77 ? 300 LEU B CB  1 
ATOM   4922 C  CG  . LEU B 1 300 ? -6.792  32.006 72.376  1.00 25.08 ? 300 LEU B CG  1 
ATOM   4923 C  CD1 . LEU B 1 300 ? -7.318  30.808 71.625  1.00 25.24 ? 300 LEU B CD1 1 
ATOM   4924 C  CD2 . LEU B 1 300 ? -7.909  32.722 73.107  1.00 26.63 ? 300 LEU B CD2 1 
ATOM   4925 N  N   . PHE B 1 301 ? -2.878  31.333 74.652  1.00 24.92 ? 301 PHE B N   1 
ATOM   4926 C  CA  . PHE B 1 301 ? -1.906  30.764 75.592  1.00 25.02 ? 301 PHE B CA  1 
ATOM   4927 C  C   . PHE B 1 301 ? -0.501  30.992 75.071  1.00 25.49 ? 301 PHE B C   1 
ATOM   4928 O  O   . PHE B 1 301 ? -0.310  31.245 73.872  1.00 25.76 ? 301 PHE B O   1 
ATOM   4929 C  CB  . PHE B 1 301 ? -2.131  29.264 75.799  1.00 24.65 ? 301 PHE B CB  1 
ATOM   4930 C  CG  . PHE B 1 301 ? -3.543  28.900 76.101  1.00 23.82 ? 301 PHE B CG  1 
ATOM   4931 C  CD1 . PHE B 1 301 ? -4.048  29.041 77.381  1.00 23.37 ? 301 PHE B CD1 1 
ATOM   4932 C  CD2 . PHE B 1 301 ? -4.371  28.414 75.099  1.00 23.70 ? 301 PHE B CD2 1 
ATOM   4933 C  CE1 . PHE B 1 301 ? -5.366  28.712 77.664  1.00 23.44 ? 301 PHE B CE1 1 
ATOM   4934 C  CE2 . PHE B 1 301 ? -5.689  28.080 75.361  1.00 23.55 ? 301 PHE B CE2 1 
ATOM   4935 C  CZ  . PHE B 1 301 ? -6.189  28.227 76.650  1.00 24.30 ? 301 PHE B CZ  1 
ATOM   4936 N  N   . LYS B 1 302 ? 0.478   30.891 75.965  1.00 25.84 ? 302 LYS B N   1 
ATOM   4937 C  CA  . LYS B 1 302 ? 1.892   31.021 75.598  1.00 26.52 ? 302 LYS B CA  1 
ATOM   4938 C  C   . LYS B 1 302 ? 2.284   29.931 74.590  1.00 26.61 ? 302 LYS B C   1 
ATOM   4939 O  O   . LYS B 1 302 ? 1.835   28.795 74.697  1.00 26.46 ? 302 LYS B O   1 
ATOM   4940 C  CB  . LYS B 1 302 ? 2.762   30.950 76.863  1.00 26.71 ? 302 LYS B CB  1 
ATOM   4941 C  CG  . LYS B 1 302 ? 4.261   31.204 76.672  1.00 27.14 ? 302 LYS B CG  1 
ATOM   4942 C  CD  . LYS B 1 302 ? 4.583   32.683 76.546  1.00 28.06 ? 302 LYS B CD  1 
ATOM   4943 C  CE  . LYS B 1 302 ? 6.057   32.928 76.770  1.00 29.39 ? 302 LYS B CE  1 
ATOM   4944 N  NZ  . LYS B 1 302 ? 6.888   32.107 75.828  1.00 32.75 ? 302 LYS B NZ  1 
ATOM   4945 N  N   . ASP B 1 303 ? 3.107   30.278 73.606  1.00 27.03 ? 303 ASP B N   1 
ATOM   4946 C  CA  . ASP B 1 303 ? 3.441   29.334 72.540  1.00 27.61 ? 303 ASP B CA  1 
ATOM   4947 C  C   . ASP B 1 303 ? 4.279   28.147 73.036  1.00 27.91 ? 303 ASP B C   1 
ATOM   4948 O  O   . ASP B 1 303 ? 4.098   27.010 72.587  1.00 27.96 ? 303 ASP B O   1 
ATOM   4949 C  CB  . ASP B 1 303 ? 4.129   30.054 71.378  1.00 27.73 ? 303 ASP B CB  1 
ATOM   4950 C  CG  . ASP B 1 303 ? 3.173   30.961 70.590  1.00 29.05 ? 303 ASP B CG  1 
ATOM   4951 O  OD1 . ASP B 1 303 ? 1.955   30.686 70.560  1.00 31.84 ? 303 ASP B OD1 1 
ATOM   4952 O  OD2 . ASP B 1 303 ? 3.634   31.957 69.994  1.00 29.31 ? 303 ASP B OD2 1 
ATOM   4953 N  N   . SER B 1 304 ? 5.179   28.411 73.981  1.00 27.98 ? 304 SER B N   1 
ATOM   4954 C  CA  . SER B 1 304 ? 6.077   27.380 74.490  1.00 27.65 ? 304 SER B CA  1 
ATOM   4955 C  C   . SER B 1 304 ? 5.448   26.627 75.670  1.00 27.44 ? 304 SER B C   1 
ATOM   4956 O  O   . SER B 1 304 ? 6.068   25.727 76.253  1.00 27.63 ? 304 SER B O   1 
ATOM   4957 C  CB  . SER B 1 304 ? 7.417   28.003 74.895  1.00 27.90 ? 304 SER B CB  1 
ATOM   4958 O  OG  . SER B 1 304 ? 7.282   28.770 76.084  1.00 28.27 ? 304 SER B OG  1 
ATOM   4959 N  N   . ALA B 1 305 ? 4.223   27.000 76.032  1.00 26.78 ? 305 ALA B N   1 
ATOM   4960 C  CA  . ALA B 1 305 ? 3.475   26.240 77.025  1.00 26.29 ? 305 ALA B CA  1 
ATOM   4961 C  C   . ALA B 1 305 ? 3.259   24.805 76.525  1.00 26.01 ? 305 ALA B C   1 
ATOM   4962 O  O   . ALA B 1 305 ? 2.967   24.587 75.347  1.00 25.96 ? 305 ALA B O   1 
ATOM   4963 C  CB  . ALA B 1 305 ? 2.146   26.917 77.341  1.00 25.99 ? 305 ALA B CB  1 
ATOM   4964 N  N   . ILE B 1 306 ? 3.417   23.839 77.427  1.00 25.79 ? 306 ILE B N   1 
ATOM   4965 C  CA  . ILE B 1 306 ? 3.238   22.416 77.104  1.00 25.35 ? 306 ILE B CA  1 
ATOM   4966 C  C   . ILE B 1 306 ? 1.990   21.789 77.729  1.00 25.06 ? 306 ILE B C   1 
ATOM   4967 O  O   . ILE B 1 306 ? 1.647   20.657 77.399  1.00 25.33 ? 306 ILE B O   1 
ATOM   4968 C  CB  . ILE B 1 306 ? 4.460   21.582 77.520  1.00 25.33 ? 306 ILE B CB  1 
ATOM   4969 C  CG1 . ILE B 1 306 ? 4.672   21.667 79.043  1.00 25.21 ? 306 ILE B CG1 1 
ATOM   4970 C  CG2 . ILE B 1 306 ? 5.696   22.033 76.734  1.00 25.34 ? 306 ILE B CG2 1 
ATOM   4971 C  CD1 . ILE B 1 306 ? 5.419   20.485 79.633  1.00 25.53 ? 306 ILE B CD1 1 
ATOM   4972 N  N   . GLY B 1 307 ? 1.322   22.511 78.626  1.00 24.62 ? 307 GLY B N   1 
ATOM   4973 C  CA  . GLY B 1 307 ? 0.109   22.000 79.268  1.00 24.22 ? 307 GLY B CA  1 
ATOM   4974 C  C   . GLY B 1 307 ? -0.472  22.888 80.351  1.00 23.98 ? 307 GLY B C   1 
ATOM   4975 O  O   . GLY B 1 307 ? -0.116  24.058 80.470  1.00 23.86 ? 307 GLY B O   1 
ATOM   4976 N  N   . PHE B 1 308 ? -1.382  22.322 81.138  1.00 23.98 ? 308 PHE B N   1 
ATOM   4977 C  CA  . PHE B 1 308 ? -2.026  23.046 82.225  1.00 23.98 ? 308 PHE B CA  1 
ATOM   4978 C  C   . PHE B 1 308 ? -1.890  22.281 83.506  1.00 24.10 ? 308 PHE B C   1 
ATOM   4979 O  O   . PHE B 1 308 ? -1.845  21.055 83.506  1.00 24.18 ? 308 PHE B O   1 
ATOM   4980 C  CB  . PHE B 1 308 ? -3.514  23.258 81.941  1.00 24.01 ? 308 PHE B CB  1 
ATOM   4981 C  CG  . PHE B 1 308 ? -3.780  24.003 80.677  1.00 23.63 ? 308 PHE B CG  1 
ATOM   4982 C  CD1 . PHE B 1 308 ? -3.453  25.354 80.572  1.00 23.49 ? 308 PHE B CD1 1 
ATOM   4983 C  CD2 . PHE B 1 308 ? -4.334  23.351 79.583  1.00 23.56 ? 308 PHE B CD2 1 
ATOM   4984 C  CE1 . PHE B 1 308 ? -3.678  26.052 79.400  1.00 23.91 ? 308 PHE B CE1 1 
ATOM   4985 C  CE2 . PHE B 1 308 ? -4.566  24.032 78.401  1.00 24.35 ? 308 PHE B CE2 1 
ATOM   4986 C  CZ  . PHE B 1 308 ? -4.237  25.392 78.307  1.00 24.89 ? 308 PHE B CZ  1 
ATOM   4987 N  N   . SER B 1 309 ? -1.821  23.021 84.603  1.00 24.32 ? 309 SER B N   1 
ATOM   4988 C  CA  . SER B 1 309 ? -1.852  22.428 85.929  1.00 24.42 ? 309 SER B CA  1 
ATOM   4989 C  C   . SER B 1 309 ? -3.000  23.041 86.706  1.00 24.50 ? 309 SER B C   1 
ATOM   4990 O  O   . SER B 1 309 ? -3.079  24.262 86.830  1.00 24.61 ? 309 SER B O   1 
ATOM   4991 C  CB  . SER B 1 309 ? -0.531  22.679 86.648  1.00 24.35 ? 309 SER B CB  1 
ATOM   4992 O  OG  . SER B 1 309 ? -0.585  22.209 87.976  1.00 24.29 ? 309 SER B OG  1 
ATOM   4993 N  N   . ARG B 1 310 ? -3.893  22.198 87.220  1.00 24.68 ? 310 ARG B N   1 
ATOM   4994 C  CA  . ARG B 1 310 ? -5.038  22.690 87.981  1.00 24.87 ? 310 ARG B CA  1 
ATOM   4995 C  C   . ARG B 1 310 ? -4.631  23.425 89.267  1.00 24.89 ? 310 ARG B C   1 
ATOM   4996 O  O   . ARG B 1 310 ? -3.800  22.947 90.033  1.00 24.75 ? 310 ARG B O   1 
ATOM   4997 C  CB  . ARG B 1 310 ? -6.042  21.571 88.281  1.00 24.63 ? 310 ARG B CB  1 
ATOM   4998 C  CG  . ARG B 1 310 ? -7.410  22.124 88.680  1.00 25.35 ? 310 ARG B CG  1 
ATOM   4999 C  CD  . ARG B 1 310 ? -8.514  21.101 88.640  1.00 26.23 ? 310 ARG B CD  1 
ATOM   5000 N  NE  . ARG B 1 310 ? -9.834  21.724 88.771  1.00 26.35 ? 310 ARG B NE  1 
ATOM   5001 C  CZ  . ARG B 1 310 ? -10.987 21.051 88.827  1.00 26.31 ? 310 ARG B CZ  1 
ATOM   5002 N  NH1 . ARG B 1 310 ? -11.004 19.718 88.773  1.00 25.01 ? 310 ARG B NH1 1 
ATOM   5003 N  NH2 . ARG B 1 310 ? -12.131 21.717 88.939  1.00 25.87 ? 310 ARG B NH2 1 
ATOM   5004 N  N   . VAL B 1 311 ? -5.212  24.602 89.474  1.00 25.07 ? 311 VAL B N   1 
ATOM   5005 C  CA  . VAL B 1 311 ? -5.000  25.357 90.700  1.00 25.34 ? 311 VAL B CA  1 
ATOM   5006 C  C   . VAL B 1 311 ? -5.933  24.813 91.771  1.00 25.99 ? 311 VAL B C   1 
ATOM   5007 O  O   . VAL B 1 311 ? -7.146  24.808 91.579  1.00 26.06 ? 311 VAL B O   1 
ATOM   5008 C  CB  . VAL B 1 311 ? -5.243  26.862 90.485  1.00 24.94 ? 311 VAL B CB  1 
ATOM   5009 C  CG1 . VAL B 1 311 ? -5.266  27.613 91.800  1.00 24.72 ? 311 VAL B CG1 1 
ATOM   5010 C  CG2 . VAL B 1 311 ? -4.179  27.422 89.597  1.00 24.61 ? 311 VAL B CG2 1 
ATOM   5011 N  N   . PRO B 1 312 ? -5.372  24.360 92.910  1.00 26.79 ? 312 PRO B N   1 
ATOM   5012 C  CA  . PRO B 1 312 ? -6.199  23.792 93.987  1.00 27.33 ? 312 PRO B CA  1 
ATOM   5013 C  C   . PRO B 1 312 ? -7.309  24.757 94.406  1.00 28.04 ? 312 PRO B C   1 
ATOM   5014 O  O   . PRO B 1 312 ? -7.179  25.965 94.201  1.00 27.99 ? 312 PRO B O   1 
ATOM   5015 C  CB  . PRO B 1 312 ? -5.205  23.608 95.144  1.00 27.17 ? 312 PRO B CB  1 
ATOM   5016 C  CG  . PRO B 1 312 ? -3.860  23.533 94.501  1.00 26.86 ? 312 PRO B CG  1 
ATOM   5017 C  CD  . PRO B 1 312 ? -3.935  24.374 93.257  1.00 26.80 ? 312 PRO B CD  1 
ATOM   5018 N  N   . PRO B 1 313 ? -8.400  24.234 94.993  1.00 28.95 ? 313 PRO B N   1 
ATOM   5019 C  CA  . PRO B 1 313 ? -9.448  25.149 95.470  1.00 29.33 ? 313 PRO B CA  1 
ATOM   5020 C  C   . PRO B 1 313 ? -8.976  25.854 96.744  1.00 29.65 ? 313 PRO B C   1 
ATOM   5021 O  O   . PRO B 1 313 ? -8.055  25.364 97.417  1.00 29.72 ? 313 PRO B O   1 
ATOM   5022 C  CB  . PRO B 1 313 ? -10.612 24.204 95.782  1.00 29.29 ? 313 PRO B CB  1 
ATOM   5023 C  CG  . PRO B 1 313 ? -9.926  22.909 96.196  1.00 29.12 ? 313 PRO B CG  1 
ATOM   5024 C  CD  . PRO B 1 313 ? -8.722  22.818 95.281  1.00 29.10 ? 313 PRO B CD  1 
ATOM   5025 N  N   . ARG B 1 314 ? -9.603  26.982 97.072  1.00 29.96 ? 314 ARG B N   1 
ATOM   5026 C  CA  . ARG B 1 314 ? -9.260  27.778 98.274  1.00 30.43 ? 314 ARG B CA  1 
ATOM   5027 C  C   . ARG B 1 314 ? -8.050  28.667 98.033  1.00 29.99 ? 314 ARG B C   1 
ATOM   5028 O  O   . ARG B 1 314 ? -7.629  29.407 98.921  1.00 30.18 ? 314 ARG B O   1 
ATOM   5029 C  CB  . ARG B 1 314 ? -9.028  26.908 99.534  1.00 30.77 ? 314 ARG B CB  1 
ATOM   5030 C  CG  . ARG B 1 314 ? -10.280 26.222 100.128 1.00 32.53 ? 314 ARG B CG  1 
ATOM   5031 C  CD  . ARG B 1 314 ? -10.997 27.100 101.157 1.00 35.44 ? 314 ARG B CD  1 
ATOM   5032 N  NE  . ARG B 1 314 ? -11.372 26.343 102.360 1.00 37.81 ? 314 ARG B NE  1 
ATOM   5033 C  CZ  . ARG B 1 314 ? -10.780 26.451 103.557 1.00 38.54 ? 314 ARG B CZ  1 
ATOM   5034 N  NH1 . ARG B 1 314 ? -9.770  27.303 103.749 1.00 38.64 ? 314 ARG B NH1 1 
ATOM   5035 N  NH2 . ARG B 1 314 ? -11.205 25.703 104.574 1.00 38.05 ? 314 ARG B NH2 1 
ATOM   5036 N  N   . ILE B 1 315 ? -7.488  28.592 96.834  1.00 29.46 ? 315 ILE B N   1 
ATOM   5037 C  CA  . ILE B 1 315 ? -6.398  29.474 96.483  1.00 28.93 ? 315 ILE B CA  1 
ATOM   5038 C  C   . ILE B 1 315 ? -6.988  30.607 95.672  1.00 28.82 ? 315 ILE B C   1 
ATOM   5039 O  O   . ILE B 1 315 ? -7.625  30.367 94.649  1.00 29.07 ? 315 ILE B O   1 
ATOM   5040 C  CB  . ILE B 1 315 ? -5.255  28.729 95.751  1.00 28.90 ? 315 ILE B CB  1 
ATOM   5041 C  CG1 . ILE B 1 315 ? -4.471  27.894 96.772  1.00 29.15 ? 315 ILE B CG1 1 
ATOM   5042 C  CG2 . ILE B 1 315 ? -4.334  29.703 95.006  1.00 27.91 ? 315 ILE B CG2 1 
ATOM   5043 C  CD1 . ILE B 1 315 ? -3.071  27.489 96.334  1.00 31.11 ? 315 ILE B CD1 1 
ATOM   5044 N  N   . ASP B 1 316 ? -6.817  31.830 96.175  1.00 28.42 ? 316 ASP B N   1 
ATOM   5045 C  CA  . ASP B 1 316 ? -7.222  33.049 95.476  1.00 27.93 ? 316 ASP B CA  1 
ATOM   5046 C  C   . ASP B 1 316 ? -6.029  33.662 94.754  1.00 27.45 ? 316 ASP B C   1 
ATOM   5047 O  O   . ASP B 1 316 ? -4.953  33.075 94.733  1.00 27.45 ? 316 ASP B O   1 
ATOM   5048 C  CB  . ASP B 1 316 ? -7.845  34.060 96.443  1.00 28.16 ? 316 ASP B CB  1 
ATOM   5049 C  CG  . ASP B 1 316 ? -6.993  34.302 97.686  1.00 28.96 ? 316 ASP B CG  1 
ATOM   5050 O  OD1 . ASP B 1 316 ? -5.747  34.309 97.597  1.00 29.28 ? 316 ASP B OD1 1 
ATOM   5051 O  OD2 . ASP B 1 316 ? -7.586  34.491 98.769  1.00 31.29 ? 316 ASP B OD2 1 
ATOM   5052 N  N   . SER B 1 317 ? -6.219  34.847 94.179  1.00 26.82 ? 317 SER B N   1 
ATOM   5053 C  CA  . SER B 1 317 ? -5.179  35.484 93.389  1.00 26.16 ? 317 SER B CA  1 
ATOM   5054 C  C   . SER B 1 317 ? -3.933  35.751 94.221  1.00 25.83 ? 317 SER B C   1 
ATOM   5055 O  O   . SER B 1 317 ? -2.818  35.475 93.785  1.00 26.08 ? 317 SER B O   1 
ATOM   5056 C  CB  . SER B 1 317 ? -5.694  36.781 92.803  1.00 26.04 ? 317 SER B CB  1 
ATOM   5057 O  OG  . SER B 1 317 ? -5.900  37.711 93.841  1.00 26.75 ? 317 SER B OG  1 
ATOM   5058 N  N   . GLY B 1 318 ? -4.133  36.293 95.418  1.00 25.47 ? 318 GLY B N   1 
ATOM   5059 C  CA  . GLY B 1 318 ? -3.044  36.548 96.354  1.00 24.66 ? 318 GLY B CA  1 
ATOM   5060 C  C   . GLY B 1 318 ? -2.216  35.314 96.633  1.00 24.18 ? 318 GLY B C   1 
ATOM   5061 O  O   . GLY B 1 318 ? -0.999  35.338 96.462  1.00 24.39 ? 318 GLY B O   1 
ATOM   5062 N  N   . LEU B 1 319 ? -2.875  34.232 97.046  1.00 23.65 ? 319 LEU B N   1 
ATOM   5063 C  CA  . LEU B 1 319 ? -2.197  32.963 97.329  1.00 23.14 ? 319 LEU B CA  1 
ATOM   5064 C  C   . LEU B 1 319 ? -1.565  32.346 96.083  1.00 22.75 ? 319 LEU B C   1 
ATOM   5065 O  O   . LEU B 1 319 ? -0.516  31.718 96.164  1.00 22.92 ? 319 LEU B O   1 
ATOM   5066 C  CB  . LEU B 1 319 ? -3.145  31.957 97.983  1.00 22.94 ? 319 LEU B CB  1 
ATOM   5067 C  CG  . LEU B 1 319 ? -3.581  32.230 99.421  1.00 23.17 ? 319 LEU B CG  1 
ATOM   5068 C  CD1 . LEU B 1 319 ? -4.817  31.404 99.782  1.00 23.78 ? 319 LEU B CD1 1 
ATOM   5069 C  CD2 . LEU B 1 319 ? -2.451  31.984 100.414 1.00 22.79 ? 319 LEU B CD2 1 
ATOM   5070 N  N   . TYR B 1 320 ? -2.197  32.526 94.932  1.00 22.24 ? 320 TYR B N   1 
ATOM   5071 C  CA  . TYR B 1 320 ? -1.613  32.039 93.694  1.00 21.99 ? 320 TYR B CA  1 
ATOM   5072 C  C   . TYR B 1 320 ? -0.282  32.709 93.378  1.00 22.05 ? 320 TYR B C   1 
ATOM   5073 O  O   . TYR B 1 320 ? 0.698   32.018 93.112  1.00 22.51 ? 320 TYR B O   1 
ATOM   5074 C  CB  . TYR B 1 320 ? -2.568  32.159 92.501  1.00 21.67 ? 320 TYR B CB  1 
ATOM   5075 C  CG  . TYR B 1 320 ? -1.930  31.661 91.235  1.00 21.19 ? 320 TYR B CG  1 
ATOM   5076 C  CD1 . TYR B 1 320 ? -1.943  30.307 90.913  1.00 20.93 ? 320 TYR B CD1 1 
ATOM   5077 C  CD2 . TYR B 1 320 ? -1.274  32.541 90.375  1.00 21.19 ? 320 TYR B CD2 1 
ATOM   5078 C  CE1 . TYR B 1 320 ? -1.332  29.844 89.744  1.00 20.97 ? 320 TYR B CE1 1 
ATOM   5079 C  CE2 . TYR B 1 320 ? -0.660  32.092 89.215  1.00 20.24 ? 320 TYR B CE2 1 
ATOM   5080 C  CZ  . TYR B 1 320 ? -0.694  30.750 88.909  1.00 20.88 ? 320 TYR B CZ  1 
ATOM   5081 O  OH  . TYR B 1 320 ? -0.075  30.318 87.775  1.00 21.70 ? 320 TYR B OH  1 
ATOM   5082 N  N   . LEU B 1 321 ? -0.246  34.041 93.401  1.00 21.83 ? 321 LEU B N   1 
ATOM   5083 C  CA  . LEU B 1 321 ? 0.978   34.784 93.081  1.00 21.65 ? 321 LEU B CA  1 
ATOM   5084 C  C   . LEU B 1 321 ? 2.093   34.616 94.113  1.00 21.50 ? 321 LEU B C   1 
ATOM   5085 O  O   . LEU B 1 321 ? 3.223   35.044 93.883  1.00 21.30 ? 321 LEU B O   1 
ATOM   5086 C  CB  . LEU B 1 321 ? 0.685   36.271 92.873  1.00 21.70 ? 321 LEU B CB  1 
ATOM   5087 C  CG  . LEU B 1 321 ? -0.158  36.636 91.653  1.00 21.75 ? 321 LEU B CG  1 
ATOM   5088 C  CD1 . LEU B 1 321 ? -0.522  38.115 91.690  1.00 21.82 ? 321 LEU B CD1 1 
ATOM   5089 C  CD2 . LEU B 1 321 ? 0.561   36.273 90.370  1.00 21.71 ? 321 LEU B CD2 1 
ATOM   5090 N  N   . GLY B 1 322 ? 1.773   33.998 95.243  1.00 21.54 ? 322 GLY B N   1 
ATOM   5091 C  CA  . GLY B 1 322 ? 2.752   33.772 96.299  1.00 21.83 ? 322 GLY B CA  1 
ATOM   5092 C  C   . GLY B 1 322 ? 3.103   35.001 97.123  1.00 22.06 ? 322 GLY B C   1 
ATOM   5093 O  O   . GLY B 1 322 ? 3.185   36.119 96.609  1.00 22.08 ? 322 GLY B O   1 
ATOM   5094 N  N   . SER B 1 323 ? 3.313   34.771 98.415  1.00 22.40 ? 323 SER B N   1 
ATOM   5095 C  CA  . SER B 1 323 ? 3.728   35.790 99.386  1.00 22.55 ? 323 SER B CA  1 
ATOM   5096 C  C   . SER B 1 323 ? 4.612   36.907 98.806  1.00 22.47 ? 323 SER B C   1 
ATOM   5097 O  O   . SER B 1 323 ? 4.229   38.074 98.797  1.00 22.55 ? 323 SER B O   1 
ATOM   5098 C  CB  . SER B 1 323 ? 4.461   35.088 100.530 1.00 22.62 ? 323 SER B CB  1 
ATOM   5099 O  OG  . SER B 1 323 ? 4.557   35.904 101.673 1.00 23.58 ? 323 SER B OG  1 
ATOM   5100 N  N   . GLY B 1 324 ? 5.781   36.525 98.298  1.00 22.55 ? 324 GLY B N   1 
ATOM   5101 C  CA  . GLY B 1 324 ? 6.813   37.458 97.855  1.00 22.15 ? 324 GLY B CA  1 
ATOM   5102 C  C   . GLY B 1 324 ? 6.417   38.446 96.781  1.00 22.05 ? 324 GLY B C   1 
ATOM   5103 O  O   . GLY B 1 324 ? 6.608   39.640 96.953  1.00 22.19 ? 324 GLY B O   1 
ATOM   5104 N  N   . TYR B 1 325 ? 5.881   37.952 95.667  1.00 22.08 ? 325 TYR B N   1 
ATOM   5105 C  CA  . TYR B 1 325 ? 5.481   38.813 94.539  1.00 21.62 ? 325 TYR B CA  1 
ATOM   5106 C  C   . TYR B 1 325 ? 4.202   39.584 94.873  1.00 21.24 ? 325 TYR B C   1 
ATOM   5107 O  O   . TYR B 1 325 ? 4.091   40.764 94.557  1.00 21.18 ? 325 TYR B O   1 
ATOM   5108 C  CB  . TYR B 1 325 ? 5.349   37.984 93.247  1.00 21.82 ? 325 TYR B CB  1 
ATOM   5109 C  CG  . TYR B 1 325 ? 4.877   38.713 92.007  1.00 21.83 ? 325 TYR B CG  1 
ATOM   5110 C  CD1 . TYR B 1 325 ? 5.448   39.907 91.609  1.00 22.10 ? 325 TYR B CD1 1 
ATOM   5111 C  CD2 . TYR B 1 325 ? 3.871   38.173 91.210  1.00 23.13 ? 325 TYR B CD2 1 
ATOM   5112 C  CE1 . TYR B 1 325 ? 5.005   40.575 90.464  1.00 23.58 ? 325 TYR B CE1 1 
ATOM   5113 C  CE2 . TYR B 1 325 ? 3.420   38.819 90.050  1.00 23.50 ? 325 TYR B CE2 1 
ATOM   5114 C  CZ  . TYR B 1 325 ? 3.989   40.023 89.680  1.00 24.13 ? 325 TYR B CZ  1 
ATOM   5115 O  OH  . TYR B 1 325 ? 3.546   40.676 88.532  1.00 22.98 ? 325 TYR B OH  1 
ATOM   5116 N  N   . PHE B 1 326 ? 3.263   38.925 95.548  1.00 20.80 ? 326 PHE B N   1 
ATOM   5117 C  CA  . PHE B 1 326 ? 2.017   39.559 95.956  1.00 20.61 ? 326 PHE B CA  1 
ATOM   5118 C  C   . PHE B 1 326 ? 2.278   40.727 96.896  1.00 21.14 ? 326 PHE B C   1 
ATOM   5119 O  O   . PHE B 1 326 ? 1.642   41.767 96.776  1.00 21.70 ? 326 PHE B O   1 
ATOM   5120 C  CB  . PHE B 1 326 ? 1.085   38.539 96.610  1.00 20.07 ? 326 PHE B CB  1 
ATOM   5121 C  CG  . PHE B 1 326 ? -0.292  39.064 96.907  1.00 19.29 ? 326 PHE B CG  1 
ATOM   5122 C  CD1 . PHE B 1 326 ? -1.062  39.665 95.907  1.00 18.63 ? 326 PHE B CD1 1 
ATOM   5123 C  CD2 . PHE B 1 326 ? -0.837  38.932 98.181  1.00 18.72 ? 326 PHE B CD2 1 
ATOM   5124 C  CE1 . PHE B 1 326 ? -2.347  40.146 96.172  1.00 17.00 ? 326 PHE B CE1 1 
ATOM   5125 C  CE2 . PHE B 1 326 ? -2.123  39.407 98.458  1.00 18.46 ? 326 PHE B CE2 1 
ATOM   5126 C  CZ  . PHE B 1 326 ? -2.879  40.015 97.443  1.00 18.44 ? 326 PHE B CZ  1 
ATOM   5127 N  N   . THR B 1 327 ? 3.220   40.570 97.822  1.00 21.46 ? 327 THR B N   1 
ATOM   5128 C  CA  . THR B 1 327 ? 3.609   41.682 98.689  1.00 21.90 ? 327 THR B CA  1 
ATOM   5129 C  C   . THR B 1 327 ? 4.290   42.790 97.884  1.00 22.15 ? 327 THR B C   1 
ATOM   5130 O  O   . THR B 1 327 ? 4.093   43.959 98.169  1.00 22.33 ? 327 THR B O   1 
ATOM   5131 C  CB  . THR B 1 327 ? 4.528   41.233 99.873  1.00 21.89 ? 327 THR B CB  1 
ATOM   5132 O  OG1 . THR B 1 327 ? 3.879   40.212 100.642 1.00 22.14 ? 327 THR B OG1 1 
ATOM   5133 C  CG2 . THR B 1 327 ? 4.830   42.400 100.800 1.00 21.77 ? 327 THR B CG2 1 
ATOM   5134 N  N   . ALA B 1 328 ? 5.072   42.408 96.876  1.00 22.80 ? 328 ALA B N   1 
ATOM   5135 C  CA  . ALA B 1 328 ? 5.881   43.342 96.088  1.00 23.41 ? 328 ALA B CA  1 
ATOM   5136 C  C   . ALA B 1 328 ? 5.050   44.286 95.215  1.00 24.06 ? 328 ALA B C   1 
ATOM   5137 O  O   . ALA B 1 328 ? 5.390   45.464 95.078  1.00 24.51 ? 328 ALA B O   1 
ATOM   5138 C  CB  . ALA B 1 328 ? 6.886   42.590 95.242  1.00 23.22 ? 328 ALA B CB  1 
ATOM   5139 N  N   . ILE B 1 329 ? 3.974   43.774 94.624  1.00 24.46 ? 329 ILE B N   1 
ATOM   5140 C  CA  . ILE B 1 329 ? 3.045   44.607 93.875  1.00 24.89 ? 329 ILE B CA  1 
ATOM   5141 C  C   . ILE B 1 329 ? 2.452   45.675 94.801  1.00 25.53 ? 329 ILE B C   1 
ATOM   5142 O  O   . ILE B 1 329 ? 2.458   46.867 94.472  1.00 25.39 ? 329 ILE B O   1 
ATOM   5143 C  CB  . ILE B 1 329 ? 1.916   43.772 93.221  1.00 24.72 ? 329 ILE B CB  1 
ATOM   5144 C  CG1 . ILE B 1 329 ? 2.486   42.811 92.183  1.00 25.08 ? 329 ILE B CG1 1 
ATOM   5145 C  CG2 . ILE B 1 329 ? 0.934   44.669 92.517  1.00 24.96 ? 329 ILE B CG2 1 
ATOM   5146 C  CD1 . ILE B 1 329 ? 1.590   41.636 91.848  1.00 24.68 ? 329 ILE B CD1 1 
ATOM   5147 N  N   . GLN B 1 330 ? 1.949   45.246 95.959  1.00 26.43 ? 330 GLN B N   1 
ATOM   5148 C  CA  . GLN B 1 330 ? 1.302   46.164 96.907  1.00 27.48 ? 330 GLN B CA  1 
ATOM   5149 C  C   . GLN B 1 330 ? 2.281   47.240 97.347  1.00 28.19 ? 330 GLN B C   1 
ATOM   5150 O  O   . GLN B 1 330 ? 1.917   48.403 97.473  1.00 28.47 ? 330 GLN B O   1 
ATOM   5151 C  CB  . GLN B 1 330 ? 0.748   45.421 98.125  1.00 27.28 ? 330 GLN B CB  1 
ATOM   5152 C  CG  . GLN B 1 330 ? -0.296  44.354 97.795  1.00 27.38 ? 330 GLN B CG  1 
ATOM   5153 C  CD  . GLN B 1 330 ? -0.753  43.581 99.023  1.00 27.51 ? 330 GLN B CD  1 
ATOM   5154 O  OE1 . GLN B 1 330 ? -0.660  42.352 99.068  1.00 27.11 ? 330 GLN B OE1 1 
ATOM   5155 N  NE2 . GLN B 1 330 ? -1.232  44.302 100.033 1.00 27.41 ? 330 GLN B NE2 1 
ATOM   5156 N  N   . ASN B 1 331 ? 3.529   46.829 97.554  1.00 29.17 ? 331 ASN B N   1 
ATOM   5157 C  CA  . ASN B 1 331 ? 4.636   47.711 97.901  1.00 29.73 ? 331 ASN B CA  1 
ATOM   5158 C  C   . ASN B 1 331 ? 4.901   48.744 96.814  1.00 29.95 ? 331 ASN B C   1 
ATOM   5159 O  O   . ASN B 1 331 ? 5.211   49.887 97.098  1.00 30.06 ? 331 ASN B O   1 
ATOM   5160 C  CB  . ASN B 1 331 ? 5.889   46.870 98.100  1.00 29.85 ? 331 ASN B CB  1 
ATOM   5161 C  CG  . ASN B 1 331 ? 6.876   47.512 99.029  1.00 30.39 ? 331 ASN B CG  1 
ATOM   5162 O  OD1 . ASN B 1 331 ? 6.497   48.212 99.970  1.00 30.43 ? 331 ASN B OD1 1 
ATOM   5163 N  ND2 . ASN B 1 331 ? 8.164   47.265 98.783  1.00 30.61 ? 331 ASN B ND2 1 
ATOM   5164 N  N   . LEU B 1 332 ? 4.769   48.319 95.567  1.00 30.46 ? 332 LEU B N   1 
ATOM   5165 C  CA  . LEU B 1 332 ? 4.955   49.176 94.399  1.00 30.90 ? 332 LEU B CA  1 
ATOM   5166 C  C   . LEU B 1 332 ? 3.794   50.156 94.172  1.00 31.48 ? 332 LEU B C   1 
ATOM   5167 O  O   . LEU B 1 332 ? 3.892   51.050 93.325  1.00 31.72 ? 332 LEU B O   1 
ATOM   5168 C  CB  . LEU B 1 332 ? 5.135   48.282 93.164  1.00 30.78 ? 332 LEU B CB  1 
ATOM   5169 C  CG  . LEU B 1 332 ? 5.398   48.830 91.771  1.00 30.14 ? 332 LEU B CG  1 
ATOM   5170 C  CD1 . LEU B 1 332 ? 6.763   49.461 91.716  1.00 30.43 ? 332 LEU B CD1 1 
ATOM   5171 C  CD2 . LEU B 1 332 ? 5.315   47.695 90.802  1.00 30.42 ? 332 LEU B CD2 1 
ATOM   5172 N  N   . ARG B 1 333 ? 2.707   49.995 94.925  1.00 31.98 ? 333 ARG B N   1 
ATOM   5173 C  CA  . ARG B 1 333 ? 1.469   50.736 94.651  1.00 32.66 ? 333 ARG B CA  1 
ATOM   5174 C  C   . ARG B 1 333 ? 0.887   51.575 95.816  1.00 33.20 ? 333 ARG B C   1 
ATOM   5175 O  O   . ARG B 1 333 ? -0.057  52.340 95.590  1.00 33.51 ? 333 ARG B O   1 
ATOM   5176 C  CB  . ARG B 1 333 ? 0.419   49.795 94.033  1.00 32.58 ? 333 ARG B CB  1 
ATOM   5177 C  CG  . ARG B 1 333 ? 0.501   49.749 92.495  1.00 33.21 ? 333 ARG B CG  1 
ATOM   5178 C  CD  . ARG B 1 333 ? 0.306   48.365 91.867  1.00 32.22 ? 333 ARG B CD  1 
ATOM   5179 N  NE  . ARG B 1 333 ? -1.085  48.079 91.517  1.00 31.73 ? 333 ARG B NE  1 
ATOM   5180 C  CZ  . ARG B 1 333 ? -1.469  47.437 90.412  1.00 31.47 ? 333 ARG B CZ  1 
ATOM   5181 N  NH1 . ARG B 1 333 ? -0.572  47.027 89.515  1.00 31.43 ? 333 ARG B NH1 1 
ATOM   5182 N  NH2 . ARG B 1 333 ? -2.755  47.215 90.191  1.00 30.21 ? 333 ARG B NH2 1 
ATOM   5183 N  N   . GLY C 2 1   ? 6.034   28.661 13.243  1.00 7.40  ? 164 GLY C N   1 
ATOM   5184 C  CA  . GLY C 2 1   ? 6.122   29.677 14.328  1.00 11.34 ? 164 GLY C CA  1 
ATOM   5185 C  C   . GLY C 2 1   ? 6.572   30.907 13.582  1.00 12.35 ? 164 GLY C C   1 
ATOM   5186 O  O   . GLY C 2 1   ? 6.613   30.787 12.362  1.00 13.34 ? 164 GLY C O   1 
ATOM   5187 N  N   . SER C 2 2   ? 6.908   32.046 14.257  1.00 12.46 ? 165 SER C N   1 
ATOM   5188 C  CA  . SER C 2 2   ? 7.473   33.285 13.593  1.00 12.83 ? 165 SER C CA  1 
ATOM   5189 C  C   . SER C 2 2   ? 8.384   34.279 14.414  1.00 13.43 ? 165 SER C C   1 
ATOM   5190 O  O   . SER C 2 2   ? 8.233   34.406 15.633  1.00 13.53 ? 165 SER C O   1 
ATOM   5191 C  CB  . SER C 2 2   ? 6.349   34.091 12.948  1.00 12.68 ? 165 SER C CB  1 
ATOM   5192 O  OG  . SER C 2 2   ? 5.840   35.056 13.857  1.00 12.48 ? 165 SER C OG  1 
ATOM   5193 N  N   . HIS C 2 3   ? 9.288   35.007 13.734  1.00 13.80 ? 166 HIS C N   1 
ATOM   5194 C  CA  . HIS C 2 3   ? 10.202  35.989 14.389  1.00 14.46 ? 166 HIS C CA  1 
ATOM   5195 C  C   . HIS C 2 3   ? 10.811  37.084 13.480  1.00 15.72 ? 166 HIS C C   1 
ATOM   5196 O  O   . HIS C 2 3   ? 10.917  36.889 12.270  1.00 15.61 ? 166 HIS C O   1 
ATOM   5197 C  CB  . HIS C 2 3   ? 11.344  35.278 15.142  1.00 14.65 ? 166 HIS C CB  1 
ATOM   5198 C  CG  . HIS C 2 3   ? 12.400  34.683 14.250  1.00 14.27 ? 166 HIS C CG  1 
ATOM   5199 N  ND1 . HIS C 2 3   ? 12.469  33.332 13.977  1.00 13.31 ? 166 HIS C ND1 1 
ATOM   5200 C  CD2 . HIS C 2 3   ? 13.433  35.254 13.583  1.00 13.95 ? 166 HIS C CD2 1 
ATOM   5201 C  CE1 . HIS C 2 3   ? 13.487  33.100 13.169  1.00 13.69 ? 166 HIS C CE1 1 
ATOM   5202 N  NE2 . HIS C 2 3   ? 14.089  34.249 12.914  1.00 14.12 ? 166 HIS C NE2 1 
ATOM   5203 N  N   . MET C 2 4   ? 11.228  38.213 14.080  1.00 17.18 ? 167 MET C N   1 
ATOM   5204 C  CA  . MET C 2 4   ? 11.938  39.319 13.378  1.00 18.81 ? 167 MET C CA  1 
ATOM   5205 C  C   . MET C 2 4   ? 13.381  39.424 13.850  1.00 19.58 ? 167 MET C C   1 
ATOM   5206 O  O   . MET C 2 4   ? 13.623  39.861 14.976  1.00 19.93 ? 167 MET C O   1 
ATOM   5207 C  CB  . MET C 2 4   ? 11.273  40.674 13.645  1.00 18.31 ? 167 MET C CB  1 
ATOM   5208 C  CG  . MET C 2 4   ? 9.928   40.911 12.954  1.00 19.68 ? 167 MET C CG  1 
ATOM   5209 S  SD  . MET C 2 4   ? 9.876   42.117 11.587  1.00 20.26 ? 167 MET C SD  1 
ATOM   5210 C  CE  . MET C 2 4   ? 10.528  43.609 12.339  1.00 19.74 ? 167 MET C CE  1 
ATOM   5211 N  N   . ASP C 2 5   ? 14.331  39.060 12.985  1.00 20.85 ? 168 ASP C N   1 
ATOM   5212 C  CA  . ASP C 2 5   ? 15.757  38.914 13.357  1.00 22.03 ? 168 ASP C CA  1 
ATOM   5213 C  C   . ASP C 2 5   ? 16.468  40.145 13.931  1.00 22.98 ? 168 ASP C C   1 
ATOM   5214 O  O   . ASP C 2 5   ? 17.328  40.005 14.794  1.00 22.93 ? 168 ASP C O   1 
ATOM   5215 C  CB  . ASP C 2 5   ? 16.570  38.355 12.190  1.00 21.79 ? 168 ASP C CB  1 
ATOM   5216 C  CG  . ASP C 2 5   ? 16.268  36.907 11.922  1.00 22.65 ? 168 ASP C CG  1 
ATOM   5217 O  OD1 . ASP C 2 5   ? 16.752  36.036 12.674  1.00 23.38 ? 168 ASP C OD1 1 
ATOM   5218 O  OD2 . ASP C 2 5   ? 15.536  36.620 10.953  1.00 24.39 ? 168 ASP C OD2 1 
ATOM   5219 N  N   . ALA C 2 6   ? 16.128  41.337 13.449  1.00 24.53 ? 169 ALA C N   1 
ATOM   5220 C  CA  . ALA C 2 6   ? 16.723  42.571 13.982  1.00 26.09 ? 169 ALA C CA  1 
ATOM   5221 C  C   . ALA C 2 6   ? 16.473  42.738 15.487  1.00 27.35 ? 169 ALA C C   1 
ATOM   5222 O  O   . ALA C 2 6   ? 17.345  43.228 16.216  1.00 27.53 ? 169 ALA C O   1 
ATOM   5223 C  CB  . ALA C 2 6   ? 16.218  43.783 13.219  1.00 25.90 ? 169 ALA C CB  1 
ATOM   5224 N  N   . GLU C 2 7   ? 15.284  42.323 15.938  1.00 28.85 ? 170 GLU C N   1 
ATOM   5225 C  CA  . GLU C 2 7   ? 14.909  42.330 17.361  1.00 30.16 ? 170 GLU C CA  1 
ATOM   5226 C  C   . GLU C 2 7   ? 15.706  41.341 18.186  1.00 30.47 ? 170 GLU C C   1 
ATOM   5227 O  O   . GLU C 2 7   ? 16.011  41.607 19.345  1.00 31.05 ? 170 GLU C O   1 
ATOM   5228 C  CB  . GLU C 2 7   ? 13.432  41.996 17.536  1.00 30.24 ? 170 GLU C CB  1 
ATOM   5229 C  CG  . GLU C 2 7   ? 12.556  43.203 17.705  1.00 32.85 ? 170 GLU C CG  1 
ATOM   5230 C  CD  . GLU C 2 7   ? 11.088  42.879 17.493  1.00 36.81 ? 170 GLU C CD  1 
ATOM   5231 O  OE1 . GLU C 2 7   ? 10.607  41.864 18.063  1.00 37.71 ? 170 GLU C OE1 1 
ATOM   5232 O  OE2 . GLU C 2 7   ? 10.417  43.643 16.752  1.00 38.67 ? 170 GLU C OE2 1 
ATOM   5233 N  N   . GLU C 2 8   ? 16.026  40.196 17.592  1.00 30.63 ? 171 GLU C N   1 
ATOM   5234 C  CA  . GLU C 2 8   ? 16.702  39.124 18.302  1.00 30.75 ? 171 GLU C CA  1 
ATOM   5235 C  C   . GLU C 2 8   ? 18.209  39.322 18.318  1.00 30.48 ? 171 GLU C C   1 
ATOM   5236 O  O   . GLU C 2 8   ? 18.929  38.652 19.059  1.00 30.57 ? 171 GLU C O   1 
ATOM   5237 C  CB  . GLU C 2 8   ? 16.345  37.778 17.670  1.00 31.07 ? 171 GLU C CB  1 
ATOM   5238 C  CG  . GLU C 2 8   ? 14.856  37.413 17.742  1.00 32.66 ? 171 GLU C CG  1 
ATOM   5239 C  CD  . GLU C 2 8   ? 14.364  37.123 19.172  1.00 36.00 ? 171 GLU C CD  1 
ATOM   5240 O  OE1 . GLU C 2 8   ? 15.198  37.020 20.121  1.00 36.67 ? 171 GLU C OE1 1 
ATOM   5241 O  OE2 . GLU C 2 8   ? 13.125  37.000 19.340  1.00 37.05 ? 171 GLU C OE2 1 
ATOM   5242 N  N   . VAL C 2 9   ? 18.674  40.260 17.504  1.00 30.38 ? 172 VAL C N   1 
ATOM   5243 C  CA  . VAL C 2 9   ? 20.100  40.479 17.281  1.00 30.24 ? 172 VAL C CA  1 
ATOM   5244 C  C   . VAL C 2 9   ? 20.634  41.758 17.943  1.00 30.39 ? 172 VAL C C   1 
ATOM   5245 O  O   . VAL C 2 9   ? 21.849  41.956 18.020  1.00 30.51 ? 172 VAL C O   1 
ATOM   5246 C  CB  . VAL C 2 9   ? 20.444  40.387 15.759  1.00 29.94 ? 172 VAL C CB  1 
ATOM   5247 C  CG1 . VAL C 2 9   ? 20.934  41.712 15.199  1.00 30.04 ? 172 VAL C CG1 1 
ATOM   5248 C  CG2 . VAL C 2 9   ? 21.428  39.260 15.510  1.00 29.54 ? 172 VAL C CG2 1 
ATOM   5249 N  N   . ALA C 2 10  ? 19.723  42.611 18.423  1.00 30.59 ? 173 ALA C N   1 
ATOM   5250 C  CA  . ALA C 2 10  ? 20.084  43.789 19.219  1.00 30.57 ? 173 ALA C CA  1 
ATOM   5251 C  C   . ALA C 2 10  ? 20.782  43.324 20.494  1.00 30.76 ? 173 ALA C C   1 
ATOM   5252 O  O   . ALA C 2 10  ? 20.439  42.263 21.040  1.00 30.70 ? 173 ALA C O   1 
ATOM   5253 C  CB  . ALA C 2 10  ? 18.854  44.607 19.559  1.00 30.38 ? 173 ALA C CB  1 
ATOM   5254 N  N   . PRO C 2 11  ? 21.762  44.112 20.979  1.00 30.85 ? 174 PRO C N   1 
ATOM   5255 C  CA  . PRO C 2 11  ? 22.570  43.659 22.111  1.00 30.71 ? 174 PRO C CA  1 
ATOM   5256 C  C   . PRO C 2 11  ? 21.746  43.342 23.364  1.00 30.69 ? 174 PRO C C   1 
ATOM   5257 O  O   . PRO C 2 11  ? 22.072  42.400 24.087  1.00 30.81 ? 174 PRO C O   1 
ATOM   5258 C  CB  . PRO C 2 11  ? 23.521  44.834 22.359  1.00 30.68 ? 174 PRO C CB  1 
ATOM   5259 C  CG  . PRO C 2 11  ? 23.551  45.587 21.071  1.00 30.64 ? 174 PRO C CG  1 
ATOM   5260 C  CD  . PRO C 2 11  ? 22.175  45.450 20.514  1.00 30.82 ? 174 PRO C CD  1 
ATOM   5261 N  N   . GLN C 2 12  ? 20.681  44.101 23.611  1.00 30.55 ? 175 GLN C N   1 
ATOM   5262 C  CA  . GLN C 2 12  ? 19.831  43.844 24.774  1.00 30.64 ? 175 GLN C CA  1 
ATOM   5263 C  C   . GLN C 2 12  ? 19.362  42.391 24.774  1.00 29.88 ? 175 GLN C C   1 
ATOM   5264 O  O   . GLN C 2 12  ? 19.457  41.714 25.789  1.00 29.88 ? 175 GLN C O   1 
ATOM   5265 C  CB  . GLN C 2 12  ? 18.641  44.815 24.828  1.00 30.51 ? 175 GLN C CB  1 
ATOM   5266 C  CG  . GLN C 2 12  ? 17.560  44.550 23.767  1.00 31.86 ? 175 GLN C CG  1 
ATOM   5267 C  CD  . GLN C 2 12  ? 16.438  45.579 23.751  1.00 31.95 ? 175 GLN C CD  1 
ATOM   5268 O  OE1 . GLN C 2 12  ? 15.903  45.908 22.682  1.00 33.98 ? 175 GLN C OE1 1 
ATOM   5269 N  NE2 . GLN C 2 12  ? 16.073  46.092 24.928  1.00 32.52 ? 175 GLN C NE2 1 
ATOM   5270 N  N   . ALA C 2 13  ? 18.903  41.919 23.617  1.00 29.44 ? 176 ALA C N   1 
ATOM   5271 C  CA  . ALA C 2 13  ? 18.368  40.573 23.458  1.00 29.41 ? 176 ALA C CA  1 
ATOM   5272 C  C   . ALA C 2 13  ? 19.445  39.484 23.529  1.00 29.53 ? 176 ALA C C   1 
ATOM   5273 O  O   . ALA C 2 13  ? 19.236  38.429 24.138  1.00 29.43 ? 176 ALA C O   1 
ATOM   5274 C  CB  . ALA C 2 13  ? 17.592  40.463 22.159  1.00 29.20 ? 176 ALA C CB  1 
ATOM   5275 N  N   . LYS C 2 14  ? 20.592  39.733 22.907  1.00 29.49 ? 177 LYS C N   1 
ATOM   5276 C  CA  . LYS C 2 14  ? 21.667  38.763 22.949  1.00 29.65 ? 177 LYS C CA  1 
ATOM   5277 C  C   . LYS C 2 14  ? 22.192  38.583 24.376  1.00 29.46 ? 177 LYS C C   1 
ATOM   5278 O  O   . LYS C 2 14  ? 22.420  37.458 24.808  1.00 29.81 ? 177 LYS C O   1 
ATOM   5279 C  CB  . LYS C 2 14  ? 22.778  39.116 21.963  1.00 29.74 ? 177 LYS C CB  1 
ATOM   5280 C  CG  . LYS C 2 14  ? 22.368  39.008 20.490  1.00 31.56 ? 177 LYS C CG  1 
ATOM   5281 C  CD  . LYS C 2 14  ? 22.858  37.729 19.795  1.00 35.74 ? 177 LYS C CD  1 
ATOM   5282 C  CE  . LYS C 2 14  ? 22.255  36.420 20.378  1.00 39.15 ? 177 LYS C CE  1 
ATOM   5283 N  NZ  . LYS C 2 14  ? 20.749  36.395 20.544  1.00 40.56 ? 177 LYS C NZ  1 
ATOM   5284 N  N   . ILE C 2 15  ? 22.353  39.669 25.125  1.00 29.13 ? 178 ILE C N   1 
ATOM   5285 C  CA  . ILE C 2 15  ? 22.791  39.534 26.515  1.00 28.80 ? 178 ILE C CA  1 
ATOM   5286 C  C   . ILE C 2 15  ? 21.784  38.699 27.312  1.00 29.00 ? 178 ILE C C   1 
ATOM   5287 O  O   . ILE C 2 15  ? 22.165  37.762 28.010  1.00 28.92 ? 178 ILE C O   1 
ATOM   5288 C  CB  . ILE C 2 15  ? 23.054  40.897 27.207  1.00 28.79 ? 178 ILE C CB  1 
ATOM   5289 C  CG1 . ILE C 2 15  ? 24.105  41.702 26.433  1.00 28.76 ? 178 ILE C CG1 1 
ATOM   5290 C  CG2 . ILE C 2 15  ? 23.523  40.685 28.637  1.00 27.82 ? 178 ILE C CG2 1 
ATOM   5291 C  CD1 . ILE C 2 15  ? 24.126  43.192 26.755  1.00 28.38 ? 178 ILE C CD1 1 
ATOM   5292 N  N   . ALA C 2 16  ? 20.500  39.015 27.176  1.00 29.27 ? 179 ALA C N   1 
ATOM   5293 C  CA  . ALA C 2 16  ? 19.457  38.327 27.941  1.00 29.62 ? 179 ALA C CA  1 
ATOM   5294 C  C   . ALA C 2 16  ? 19.389  36.819 27.664  1.00 29.91 ? 179 ALA C C   1 
ATOM   5295 O  O   . ALA C 2 16  ? 19.163  36.024 28.580  1.00 29.76 ? 179 ALA C O   1 
ATOM   5296 C  CB  . ALA C 2 16  ? 18.098  38.987 27.706  1.00 29.44 ? 179 ALA C CB  1 
ATOM   5297 N  N   . GLU C 2 17  ? 19.587  36.433 26.405  1.00 30.43 ? 180 GLU C N   1 
ATOM   5298 C  CA  . GLU C 2 17  ? 19.563  35.023 26.025  1.00 31.01 ? 180 GLU C CA  1 
ATOM   5299 C  C   . GLU C 2 17  ? 20.823  34.322 26.532  1.00 30.88 ? 180 GLU C C   1 
ATOM   5300 O  O   . GLU C 2 17  ? 20.772  33.167 26.961  1.00 31.06 ? 180 GLU C O   1 
ATOM   5301 C  CB  . GLU C 2 17  ? 19.359  34.858 24.509  1.00 31.18 ? 180 GLU C CB  1 
ATOM   5302 C  CG  . GLU C 2 17  ? 19.473  33.425 23.933  1.00 33.69 ? 180 GLU C CG  1 
ATOM   5303 C  CD  . GLU C 2 17  ? 18.649  32.330 24.676  1.00 36.59 ? 180 GLU C CD  1 
ATOM   5304 O  OE1 . GLU C 2 17  ? 17.632  32.668 25.346  1.00 36.80 ? 180 GLU C OE1 1 
ATOM   5305 O  OE2 . GLU C 2 17  ? 19.028  31.123 24.564  1.00 35.92 ? 180 GLU C OE2 1 
ATOM   5306 N  N   . LEU C 2 18  ? 21.944  35.036 26.517  1.00 30.84 ? 181 LEU C N   1 
ATOM   5307 C  CA  . LEU C 2 18  ? 23.183  34.499 27.066  1.00 30.62 ? 181 LEU C CA  1 
ATOM   5308 C  C   . LEU C 2 18  ? 23.060  34.181 28.564  1.00 30.86 ? 181 LEU C C   1 
ATOM   5309 O  O   . LEU C 2 18  ? 23.502  33.119 29.006  1.00 30.91 ? 181 LEU C O   1 
ATOM   5310 C  CB  . LEU C 2 18  ? 24.368  35.429 26.784  1.00 30.16 ? 181 LEU C CB  1 
ATOM   5311 C  CG  . LEU C 2 18  ? 25.740  34.938 27.255  1.00 29.94 ? 181 LEU C CG  1 
ATOM   5312 C  CD1 . LEU C 2 18  ? 26.119  33.597 26.652  1.00 29.44 ? 181 LEU C CD1 1 
ATOM   5313 C  CD2 . LEU C 2 18  ? 26.790  35.941 26.923  1.00 30.58 ? 181 LEU C CD2 1 
ATOM   5314 N  N   . GLU C 2 19  ? 22.443  35.074 29.339  1.00 31.07 ? 182 GLU C N   1 
ATOM   5315 C  CA  . GLU C 2 19  ? 22.353  34.854 30.792  1.00 31.36 ? 182 GLU C CA  1 
ATOM   5316 C  C   . GLU C 2 19  ? 21.357  33.758 31.133  1.00 31.16 ? 182 GLU C C   1 
ATOM   5317 O  O   . GLU C 2 19  ? 21.481  33.100 32.170  1.00 31.03 ? 182 GLU C O   1 
ATOM   5318 C  CB  . GLU C 2 19  ? 22.097  36.161 31.580  1.00 31.45 ? 182 GLU C CB  1 
ATOM   5319 C  CG  . GLU C 2 19  ? 20.671  36.436 32.019  1.00 32.39 ? 182 GLU C CG  1 
ATOM   5320 C  CD  . GLU C 2 19  ? 20.239  35.633 33.244  1.00 34.20 ? 182 GLU C CD  1 
ATOM   5321 O  OE1 . GLU C 2 19  ? 21.007  35.548 34.235  1.00 33.69 ? 182 GLU C OE1 1 
ATOM   5322 O  OE2 . GLU C 2 19  ? 19.114  35.082 33.207  1.00 35.06 ? 182 GLU C OE2 1 
ATOM   5323 N  N   . ASN C 2 20  ? 20.381  33.570 30.246  1.00 31.23 ? 183 ASN C N   1 
ATOM   5324 C  CA  . ASN C 2 20  ? 19.478  32.429 30.311  1.00 31.26 ? 183 ASN C CA  1 
ATOM   5325 C  C   . ASN C 2 20  ? 20.229  31.127 30.059  1.00 31.11 ? 183 ASN C C   1 
ATOM   5326 O  O   . ASN C 2 20  ? 20.007  30.135 30.753  1.00 30.88 ? 183 ASN C O   1 
ATOM   5327 C  CB  . ASN C 2 20  ? 18.342  32.579 29.301  1.00 31.24 ? 183 ASN C CB  1 
ATOM   5328 C  CG  . ASN C 2 20  ? 17.231  31.570 29.525  1.00 32.28 ? 183 ASN C CG  1 
ATOM   5329 O  OD1 . ASN C 2 20  ? 17.024  30.667 28.711  1.00 33.82 ? 183 ASN C OD1 1 
ATOM   5330 N  ND2 . ASN C 2 20  ? 16.515  31.709 30.639  1.00 32.68 ? 183 ASN C ND2 1 
ATOM   5331 N  N   . GLN C 2 21  ? 21.124  31.145 29.074  1.00 31.19 ? 184 GLN C N   1 
ATOM   5332 C  CA  . GLN C 2 21  ? 21.929  29.974 28.736  1.00 31.63 ? 184 GLN C CA  1 
ATOM   5333 C  C   . GLN C 2 21  ? 22.837  29.564 29.898  1.00 31.93 ? 184 GLN C C   1 
ATOM   5334 O  O   . GLN C 2 21  ? 22.987  28.376 30.194  1.00 32.00 ? 184 GLN C O   1 
ATOM   5335 C  CB  . GLN C 2 21  ? 22.751  30.221 27.472  1.00 31.54 ? 184 GLN C CB  1 
ATOM   5336 C  CG  . GLN C 2 21  ? 21.965  30.121 26.169  1.00 31.63 ? 184 GLN C CG  1 
ATOM   5337 C  CD  . GLN C 2 21  ? 22.746  30.652 24.964  1.00 31.87 ? 184 GLN C CD  1 
ATOM   5338 O  OE1 . GLN C 2 21  ? 23.949  30.405 24.821  1.00 31.03 ? 184 GLN C OE1 1 
ATOM   5339 N  NE2 . GLN C 2 21  ? 22.056  31.383 24.090  1.00 32.48 ? 184 GLN C NE2 1 
ATOM   5340 N  N   . VAL C 2 22  ? 23.429  30.557 30.556  1.00 32.23 ? 185 VAL C N   1 
ATOM   5341 C  CA  . VAL C 2 22  ? 24.222  30.328 31.752  1.00 32.46 ? 185 VAL C CA  1 
ATOM   5342 C  C   . VAL C 2 22  ? 23.340  29.704 32.828  1.00 33.03 ? 185 VAL C C   1 
ATOM   5343 O  O   . VAL C 2 22  ? 23.734  28.728 33.456  1.00 33.38 ? 185 VAL C O   1 
ATOM   5344 C  CB  . VAL C 2 22  ? 24.899  31.632 32.247  1.00 32.33 ? 185 VAL C CB  1 
ATOM   5345 C  CG1 . VAL C 2 22  ? 25.510  31.453 33.630  1.00 31.91 ? 185 VAL C CG1 1 
ATOM   5346 C  CG2 . VAL C 2 22  ? 25.965  32.081 31.254  1.00 31.94 ? 185 VAL C CG2 1 
ATOM   5347 N  N   . HIS C 2 23  ? 22.141  30.245 33.013  1.00 33.74 ? 186 HIS C N   1 
ATOM   5348 C  CA  . HIS C 2 23  ? 21.215  29.721 34.006  1.00 34.51 ? 186 HIS C CA  1 
ATOM   5349 C  C   . HIS C 2 23  ? 20.871  28.263 33.734  1.00 35.44 ? 186 HIS C C   1 
ATOM   5350 O  O   . HIS C 2 23  ? 20.945  27.435 34.644  1.00 35.64 ? 186 HIS C O   1 
ATOM   5351 C  CB  . HIS C 2 23  ? 19.939  30.570 34.088  1.00 34.26 ? 186 HIS C CB  1 
ATOM   5352 C  CG  . HIS C 2 23  ? 18.845  29.943 34.904  1.00 33.58 ? 186 HIS C CG  1 
ATOM   5353 N  ND1 . HIS C 2 23  ? 18.992  29.635 36.240  1.00 32.46 ? 186 HIS C ND1 1 
ATOM   5354 C  CD2 . HIS C 2 23  ? 17.587  29.569 34.569  1.00 32.66 ? 186 HIS C CD2 1 
ATOM   5355 C  CE1 . HIS C 2 23  ? 17.873  29.098 36.692  1.00 32.24 ? 186 HIS C CE1 1 
ATOM   5356 N  NE2 . HIS C 2 23  ? 17.003  29.049 35.699  1.00 32.30 ? 186 HIS C NE2 1 
ATOM   5357 N  N   . ARG C 2 24  ? 20.509  27.951 32.490  1.00 36.51 ? 187 ARG C N   1 
ATOM   5358 C  CA  . ARG C 2 24  ? 20.122  26.588 32.117  1.00 37.76 ? 187 ARG C CA  1 
ATOM   5359 C  C   . ARG C 2 24  ? 21.286  25.626 32.284  1.00 38.07 ? 187 ARG C C   1 
ATOM   5360 O  O   . ARG C 2 24  ? 21.096  24.484 32.703  1.00 38.08 ? 187 ARG C O   1 
ATOM   5361 C  CB  . ARG C 2 24  ? 19.577  26.528 30.685  1.00 37.44 ? 187 ARG C CB  1 
ATOM   5362 C  CG  . ARG C 2 24  ? 18.120  26.917 30.567  1.00 38.31 ? 187 ARG C CG  1 
ATOM   5363 C  CD  . ARG C 2 24  ? 17.617  26.903 29.121  1.00 39.57 ? 187 ARG C CD  1 
ATOM   5364 N  NE  . ARG C 2 24  ? 16.415  27.737 28.984  1.00 44.55 ? 187 ARG C NE  1 
ATOM   5365 C  CZ  . ARG C 2 24  ? 15.548  27.713 27.966  1.00 46.06 ? 187 ARG C CZ  1 
ATOM   5366 N  NH1 . ARG C 2 24  ? 15.702  26.878 26.936  1.00 45.88 ? 187 ARG C NH1 1 
ATOM   5367 N  NH2 . ARG C 2 24  ? 14.504  28.544 27.986  1.00 46.93 ? 187 ARG C NH2 1 
ATOM   5368 N  N   . LEU C 2 25  ? 22.488  26.103 31.968  1.00 38.92 ? 188 LEU C N   1 
ATOM   5369 C  CA  . LEU C 2 25  ? 23.693  25.291 32.072  1.00 39.70 ? 188 LEU C CA  1 
ATOM   5370 C  C   . LEU C 2 25  ? 23.994  24.863 33.495  1.00 40.47 ? 188 LEU C C   1 
ATOM   5371 O  O   . LEU C 2 25  ? 24.194  23.681 33.745  1.00 40.64 ? 188 LEU C O   1 
ATOM   5372 C  CB  . LEU C 2 25  ? 24.903  26.011 31.486  1.00 39.55 ? 188 LEU C CB  1 
ATOM   5373 C  CG  . LEU C 2 25  ? 25.148  25.918 29.982  1.00 39.50 ? 188 LEU C CG  1 
ATOM   5374 C  CD1 . LEU C 2 25  ? 26.345  26.781 29.608  1.00 38.80 ? 188 LEU C CD1 1 
ATOM   5375 C  CD2 . LEU C 2 25  ? 25.356  24.474 29.541  1.00 39.60 ? 188 LEU C CD2 1 
ATOM   5376 N  N   . GLU C 2 26  ? 24.025  25.807 34.431  1.00 41.56 ? 189 GLU C N   1 
ATOM   5377 C  CA  . GLU C 2 26  ? 24.330  25.441 35.813  1.00 42.84 ? 189 GLU C CA  1 
ATOM   5378 C  C   . GLU C 2 26  ? 23.168  24.742 36.516  1.00 43.77 ? 189 GLU C C   1 
ATOM   5379 O  O   . GLU C 2 26  ? 23.350  24.145 37.575  1.00 43.90 ? 189 GLU C O   1 
ATOM   5380 C  CB  . GLU C 2 26  ? 24.884  26.617 36.619  1.00 42.61 ? 189 GLU C CB  1 
ATOM   5381 C  CG  . GLU C 2 26  ? 24.027  27.845 36.668  1.00 43.08 ? 189 GLU C CG  1 
ATOM   5382 C  CD  . GLU C 2 26  ? 24.819  29.075 37.080  1.00 43.98 ? 189 GLU C CD  1 
ATOM   5383 O  OE1 . GLU C 2 26  ? 26.056  28.967 37.247  1.00 43.51 ? 189 GLU C OE1 1 
ATOM   5384 O  OE2 . GLU C 2 26  ? 24.205  30.157 37.229  1.00 44.93 ? 189 GLU C OE2 1 
ATOM   5385 N  N   . GLN C 2 27  ? 21.990  24.792 35.902  1.00 45.15 ? 190 GLN C N   1 
ATOM   5386 C  CA  . GLN C 2 27  ? 20.829  24.055 36.387  1.00 46.50 ? 190 GLN C CA  1 
ATOM   5387 C  C   . GLN C 2 27  ? 20.936  22.600 35.951  1.00 47.40 ? 190 GLN C C   1 
ATOM   5388 O  O   . GLN C 2 27  ? 20.707  21.691 36.747  1.00 47.50 ? 190 GLN C O   1 
ATOM   5389 C  CB  . GLN C 2 27  ? 19.525  24.688 35.876  1.00 46.54 ? 190 GLN C CB  1 
ATOM   5390 C  CG  . GLN C 2 27  ? 18.281  24.426 36.748  1.00 47.15 ? 190 GLN C CG  1 
ATOM   5391 C  CD  . GLN C 2 27  ? 18.326  25.127 38.110  1.00 47.27 ? 190 GLN C CD  1 
ATOM   5392 O  OE1 . GLN C 2 27  ? 18.762  26.272 38.219  1.00 47.93 ? 190 GLN C OE1 1 
ATOM   5393 N  NE2 . GLN C 2 27  ? 17.864  24.438 39.149  1.00 46.91 ? 190 GLN C NE2 1 
ATOM   5394 N  N   . GLU C 2 28  ? 21.298  22.385 34.688  1.00 48.71 ? 191 GLU C N   1 
ATOM   5395 C  CA  . GLU C 2 28  ? 21.517  21.038 34.164  1.00 50.09 ? 191 GLU C CA  1 
ATOM   5396 C  C   . GLU C 2 28  ? 22.847  20.485 34.695  1.00 50.69 ? 191 GLU C C   1 
ATOM   5397 O  O   . GLU C 2 28  ? 23.140  19.298 34.552  1.00 50.92 ? 191 GLU C O   1 
ATOM   5398 C  CB  . GLU C 2 28  ? 21.463  21.032 32.625  1.00 50.21 ? 191 GLU C CB  1 
ATOM   5399 C  CG  . GLU C 2 28  ? 21.117  19.666 31.973  1.00 52.04 ? 191 GLU C CG  1 
ATOM   5400 C  CD  . GLU C 2 28  ? 19.597  19.340 31.910  1.00 53.85 ? 191 GLU C CD  1 
ATOM   5401 O  OE1 . GLU C 2 28  ? 18.797  20.217 31.493  1.00 53.43 ? 191 GLU C OE1 1 
ATOM   5402 O  OE2 . GLU C 2 28  ? 19.216  18.183 32.247  1.00 53.60 ? 191 GLU C OE2 1 
ATOM   5403 N  N   . LEU C 2 29  ? 23.634  21.352 35.328  1.00 51.63 ? 192 LEU C N   1 
ATOM   5404 C  CA  . LEU C 2 29  ? 24.887  20.959 35.971  1.00 52.60 ? 192 LEU C CA  1 
ATOM   5405 C  C   . LEU C 2 29  ? 24.671  20.633 37.449  1.00 53.55 ? 192 LEU C C   1 
ATOM   5406 O  O   . LEU C 2 29  ? 25.584  20.167 38.134  1.00 53.70 ? 192 LEU C O   1 
ATOM   5407 C  CB  . LEU C 2 29  ? 25.920  22.072 35.823  1.00 52.46 ? 192 LEU C CB  1 
ATOM   5408 C  CG  . LEU C 2 29  ? 27.404  21.736 35.908  1.00 52.39 ? 192 LEU C CG  1 
ATOM   5409 C  CD1 . LEU C 2 29  ? 27.773  20.623 34.935  1.00 52.38 ? 192 LEU C CD1 1 
ATOM   5410 C  CD2 . LEU C 2 29  ? 28.209  22.991 35.624  1.00 52.44 ? 192 LEU C CD2 1 
ATOM   5411 N  N   . LYS C 2 30  ? 23.459  20.902 37.929  1.00 54.67 ? 193 LYS C N   1 
ATOM   5412 C  CA  . LYS C 2 30  ? 23.018  20.497 39.261  1.00 55.75 ? 193 LYS C CA  1 
ATOM   5413 C  C   . LYS C 2 30  ? 22.341  19.124 39.154  1.00 56.40 ? 193 LYS C C   1 
ATOM   5414 O  O   . LYS C 2 30  ? 22.713  18.180 39.859  1.00 56.52 ? 193 LYS C O   1 
ATOM   5415 C  CB  . LYS C 2 30  ? 22.056  21.542 39.834  1.00 55.65 ? 193 LYS C CB  1 
ATOM   5416 C  CG  . LYS C 2 30  ? 21.467  21.208 41.202  1.00 56.09 ? 193 LYS C CG  1 
ATOM   5417 C  CD  . LYS C 2 30  ? 20.389  22.220 41.626  1.00 56.09 ? 193 LYS C CD  1 
ATOM   5418 C  CE  . LYS C 2 30  ? 20.985  23.530 42.141  1.00 55.84 ? 193 LYS C CE  1 
ATOM   5419 N  NZ  . LYS C 2 30  ? 19.929  24.432 42.664  1.00 55.70 ? 193 LYS C NZ  1 
ATOM   5420 N  N   . GLU C 2 31  ? 21.357  19.039 38.254  1.00 57.23 ? 194 GLU C N   1 
ATOM   5421 C  CA  . GLU C 2 31  ? 20.658  17.798 37.869  1.00 57.97 ? 194 GLU C CA  1 
ATOM   5422 C  C   . GLU C 2 31  ? 21.600  16.588 37.748  1.00 58.26 ? 194 GLU C C   1 
ATOM   5423 O  O   . GLU C 2 31  ? 21.163  15.444 37.873  1.00 58.23 ? 194 GLU C O   1 
ATOM   5424 C  CB  . GLU C 2 31  ? 19.944  18.037 36.527  1.00 57.99 ? 194 GLU C CB  1 
ATOM   5425 C  CG  . GLU C 2 31  ? 18.681  17.213 36.245  1.00 58.24 ? 194 GLU C CG  1 
ATOM   5426 C  CD  . GLU C 2 31  ? 17.895  17.742 35.032  1.00 58.25 ? 194 GLU C CD  1 
ATOM   5427 O  OE1 . GLU C 2 31  ? 17.853  18.977 34.832  1.00 58.20 ? 194 GLU C OE1 1 
ATOM   5428 O  OE2 . GLU C 2 31  ? 17.320  16.929 34.274  1.00 58.56 ? 194 GLU C OE2 1 
ATOM   5429 N  N   . ILE C 2 32  ? 22.885  16.862 37.509  1.00 58.71 ? 195 ILE C N   1 
ATOM   5430 C  CA  . ILE C 2 32  ? 23.916  15.835 37.313  1.00 59.04 ? 195 ILE C CA  1 
ATOM   5431 C  C   . ILE C 2 32  ? 24.655  15.448 38.603  1.00 59.38 ? 195 ILE C C   1 
ATOM   5432 O  O   . ILE C 2 32  ? 24.911  14.264 38.845  1.00 59.51 ? 195 ILE C O   1 
ATOM   5433 C  CB  . ILE C 2 32  ? 24.910  16.242 36.175  1.00 59.00 ? 195 ILE C CB  1 
ATOM   5434 C  CG1 . ILE C 2 32  ? 24.403  15.718 34.822  1.00 58.99 ? 195 ILE C CG1 1 
ATOM   5435 C  CG2 . ILE C 2 32  ? 26.334  15.746 36.455  1.00 58.84 ? 195 ILE C CG2 1 
ATOM   5436 C  CD1 . ILE C 2 32  ? 25.226  16.154 33.610  1.00 59.00 ? 195 ILE C CD1 1 
ATOM   5437 N  N   . ASP C 2 33  ? 24.984  16.436 39.433  1.00 59.79 ? 196 ASP C N   1 
ATOM   5438 C  CA  . ASP C 2 33  ? 25.694  16.177 40.692  1.00 60.21 ? 196 ASP C CA  1 
ATOM   5439 C  C   . ASP C 2 33  ? 24.796  15.569 41.777  1.00 60.36 ? 196 ASP C C   1 
ATOM   5440 O  O   . ASP C 2 33  ? 25.203  15.448 42.935  1.00 60.34 ? 196 ASP C O   1 
ATOM   5441 C  CB  . ASP C 2 33  ? 26.375  17.454 41.197  1.00 60.32 ? 196 ASP C CB  1 
ATOM   5442 C  CG  . ASP C 2 33  ? 27.661  17.760 40.451  1.00 60.67 ? 196 ASP C CG  1 
ATOM   5443 O  OD1 . ASP C 2 33  ? 28.712  17.191 40.818  1.00 60.80 ? 196 ASP C OD1 1 
ATOM   5444 O  OD2 . ASP C 2 33  ? 27.620  18.570 39.499  1.00 60.95 ? 196 ASP C OD2 1 
ATOM   5445 N  N   . GLU C 2 34  ? 23.584  15.179 41.384  1.00 60.61 ? 197 GLU C N   1 
ATOM   5446 C  CA  . GLU C 2 34  ? 22.609  14.573 42.289  1.00 60.83 ? 197 GLU C CA  1 
ATOM   5447 C  C   . GLU C 2 34  ? 22.021  13.286 41.687  1.00 60.77 ? 197 GLU C C   1 
ATOM   5448 O  O   . GLU C 2 34  ? 20.837  12.978 41.825  1.00 60.79 ? 197 GLU C O   1 
ATOM   5449 C  CB  . GLU C 2 34  ? 21.507  15.588 42.644  1.00 60.87 ? 197 GLU C CB  1 
ATOM   5450 C  CG  . GLU C 2 34  ? 21.951  16.701 43.619  1.00 61.07 ? 197 GLU C CG  1 
ATOM   5451 C  CD  . GLU C 2 34  ? 20.992  17.894 43.671  1.00 61.11 ? 197 GLU C CD  1 
ATOM   5452 O  OE1 . GLU C 2 34  ? 19.762  17.692 43.550  1.00 61.44 ? 197 GLU C OE1 1 
ATOM   5453 O  OE2 . GLU C 2 34  ? 21.473  19.040 43.841  1.00 60.91 ? 197 GLU C OE2 1 
ATOM   5454 N  N   . ALA C 2 47  ? 31.116  17.394 33.344  1.00 47.62 ? 210 ALA C N   1 
ATOM   5455 C  CA  . ALA C 2 47  ? 32.447  18.078 33.410  1.00 47.84 ? 210 ALA C CA  1 
ATOM   5456 C  C   . ALA C 2 47  ? 32.855  18.861 32.145  1.00 47.88 ? 210 ALA C C   1 
ATOM   5457 O  O   . ALA C 2 47  ? 33.497  19.905 32.263  1.00 47.87 ? 210 ALA C O   1 
ATOM   5458 C  CB  . ALA C 2 47  ? 33.542  17.088 33.805  1.00 47.92 ? 210 ALA C CB  1 
ATOM   5459 N  N   . PRO C 2 48  ? 32.521  18.354 30.932  1.00 47.91 ? 211 PRO C N   1 
ATOM   5460 C  CA  . PRO C 2 48  ? 32.806  19.188 29.759  1.00 47.70 ? 211 PRO C CA  1 
ATOM   5461 C  C   . PRO C 2 48  ? 31.808  20.337 29.611  1.00 47.49 ? 211 PRO C C   1 
ATOM   5462 O  O   . PRO C 2 48  ? 32.076  21.294 28.883  1.00 47.74 ? 211 PRO C O   1 
ATOM   5463 C  CB  . PRO C 2 48  ? 32.678  18.210 28.587  1.00 47.71 ? 211 PRO C CB  1 
ATOM   5464 C  CG  . PRO C 2 48  ? 31.719  17.188 29.056  1.00 47.88 ? 211 PRO C CG  1 
ATOM   5465 C  CD  . PRO C 2 48  ? 31.926  17.057 30.545  1.00 48.03 ? 211 PRO C CD  1 
ATOM   5466 N  N   . LEU C 2 49  ? 30.668  20.238 30.296  1.00 47.02 ? 212 LEU C N   1 
ATOM   5467 C  CA  . LEU C 2 49  ? 29.707  21.339 30.358  1.00 46.46 ? 212 LEU C CA  1 
ATOM   5468 C  C   . LEU C 2 49  ? 30.264  22.500 31.179  1.00 45.91 ? 212 LEU C C   1 
ATOM   5469 O  O   . LEU C 2 49  ? 29.887  23.647 30.957  1.00 46.05 ? 212 LEU C O   1 
ATOM   5470 C  CB  . LEU C 2 49  ? 28.360  20.880 30.939  1.00 46.54 ? 212 LEU C CB  1 
ATOM   5471 C  CG  . LEU C 2 49  ? 27.446  19.985 30.088  1.00 46.83 ? 212 LEU C CG  1 
ATOM   5472 C  CD1 . LEU C 2 49  ? 26.362  19.370 30.952  1.00 46.96 ? 212 LEU C CD1 1 
ATOM   5473 C  CD2 . LEU C 2 49  ? 26.823  20.722 28.895  1.00 47.19 ? 212 LEU C CD2 1 
ATOM   5474 N  N   . GLN C 2 50  ? 31.158  22.190 32.119  1.00 45.12 ? 213 GLN C N   1 
ATOM   5475 C  CA  . GLN C 2 50  ? 31.789  23.189 32.984  1.00 44.35 ? 213 GLN C CA  1 
ATOM   5476 C  C   . GLN C 2 50  ? 32.670  24.149 32.192  1.00 43.91 ? 213 GLN C C   1 
ATOM   5477 O  O   . GLN C 2 50  ? 32.711  25.342 32.493  1.00 43.92 ? 213 GLN C O   1 
ATOM   5478 C  CB  . GLN C 2 50  ? 32.594  22.509 34.103  1.00 44.33 ? 213 GLN C CB  1 
ATOM   5479 C  CG  . GLN C 2 50  ? 33.293  23.459 35.088  1.00 44.18 ? 213 GLN C CG  1 
ATOM   5480 C  CD  . GLN C 2 50  ? 32.327  24.257 35.956  1.00 43.87 ? 213 GLN C CD  1 
ATOM   5481 O  OE1 . GLN C 2 50  ? 31.422  23.700 36.581  1.00 43.81 ? 213 GLN C OE1 1 
ATOM   5482 N  NE2 . GLN C 2 50  ? 32.528  25.567 36.006  1.00 43.12 ? 213 GLN C NE2 1 
ATOM   5483 N  N   . SER C 2 51  ? 33.362  23.629 31.181  1.00 43.37 ? 214 SER C N   1 
ATOM   5484 C  CA  . SER C 2 51  ? 34.221  24.450 30.326  1.00 42.83 ? 214 SER C CA  1 
ATOM   5485 C  C   . SER C 2 51  ? 33.374  25.342 29.423  1.00 42.13 ? 214 SER C C   1 
ATOM   5486 O  O   . SER C 2 51  ? 33.693  26.515 29.227  1.00 41.95 ? 214 SER C O   1 
ATOM   5487 C  CB  . SER C 2 51  ? 35.162  23.577 29.491  1.00 42.98 ? 214 SER C CB  1 
ATOM   5488 O  OG  . SER C 2 51  ? 34.460  22.948 28.432  1.00 43.41 ? 214 SER C OG  1 
ATOM   5489 N  N   . LYS C 2 52  ? 32.295  24.775 28.884  1.00 41.34 ? 215 LYS C N   1 
ATOM   5490 C  CA  . LYS C 2 52  ? 31.303  25.545 28.130  1.00 40.56 ? 215 LYS C CA  1 
ATOM   5491 C  C   . LYS C 2 52  ? 30.696  26.641 29.012  1.00 39.74 ? 215 LYS C C   1 
ATOM   5492 O  O   . LYS C 2 52  ? 30.573  27.785 28.577  1.00 39.65 ? 215 LYS C O   1 
ATOM   5493 C  CB  . LYS C 2 52  ? 30.203  24.632 27.572  1.00 40.64 ? 215 LYS C CB  1 
ATOM   5494 C  CG  . LYS C 2 52  ? 29.361  25.269 26.468  1.00 41.31 ? 215 LYS C CG  1 
ATOM   5495 C  CD  . LYS C 2 52  ? 27.961  24.655 26.362  1.00 42.67 ? 215 LYS C CD  1 
ATOM   5496 C  CE  . LYS C 2 52  ? 27.979  23.236 25.769  1.00 44.28 ? 215 LYS C CE  1 
ATOM   5497 N  NZ  . LYS C 2 52  ? 26.638  22.562 25.814  1.00 44.78 ? 215 LYS C NZ  1 
ATOM   5498 N  N   . LEU C 2 53  ? 30.335  26.282 30.246  1.00 38.72 ? 216 LEU C N   1 
ATOM   5499 C  CA  . LEU C 2 53  ? 29.801  27.232 31.219  1.00 38.13 ? 216 LEU C CA  1 
ATOM   5500 C  C   . LEU C 2 53  ? 30.793  28.368 31.464  1.00 37.92 ? 216 LEU C C   1 
ATOM   5501 O  O   . LEU C 2 53  ? 30.461  29.535 31.255  1.00 37.89 ? 216 LEU C O   1 
ATOM   5502 C  CB  . LEU C 2 53  ? 29.417  26.537 32.538  1.00 37.94 ? 216 LEU C CB  1 
ATOM   5503 C  CG  . LEU C 2 53  ? 28.813  27.398 33.661  1.00 38.02 ? 216 LEU C CG  1 
ATOM   5504 C  CD1 . LEU C 2 53  ? 27.402  27.852 33.348  1.00 37.12 ? 216 LEU C CD1 1 
ATOM   5505 C  CD2 . LEU C 2 53  ? 28.829  26.682 34.986  1.00 37.80 ? 216 LEU C CD2 1 
ATOM   5506 N  N   . ASP C 2 54  ? 32.011  28.015 31.872  1.00 37.62 ? 217 ASP C N   1 
ATOM   5507 C  CA  . ASP C 2 54  ? 33.061  28.991 32.169  1.00 37.41 ? 217 ASP C CA  1 
ATOM   5508 C  C   . ASP C 2 54  ? 33.232  30.052 31.083  1.00 37.06 ? 217 ASP C C   1 
ATOM   5509 O  O   . ASP C 2 54  ? 33.469  31.219 31.394  1.00 36.89 ? 217 ASP C O   1 
ATOM   5510 C  CB  . ASP C 2 54  ? 34.399  28.283 32.422  1.00 37.68 ? 217 ASP C CB  1 
ATOM   5511 C  CG  . ASP C 2 54  ? 34.519  27.713 33.838  1.00 38.28 ? 217 ASP C CG  1 
ATOM   5512 O  OD1 . ASP C 2 54  ? 33.810  28.191 34.752  1.00 39.16 ? 217 ASP C OD1 1 
ATOM   5513 O  OD2 . ASP C 2 54  ? 35.340  26.787 34.039  1.00 39.11 ? 217 ASP C OD2 1 
ATOM   5514 N  N   . ALA C 2 55  ? 33.106  29.640 29.820  1.00 36.86 ? 218 ALA C N   1 
ATOM   5515 C  CA  . ALA C 2 55  ? 33.224  30.546 28.671  1.00 36.75 ? 218 ALA C CA  1 
ATOM   5516 C  C   . ALA C 2 55  ? 32.046  31.505 28.579  1.00 36.82 ? 218 ALA C C   1 
ATOM   5517 O  O   . ALA C 2 55  ? 32.243  32.719 28.506  1.00 37.00 ? 218 ALA C O   1 
ATOM   5518 C  CB  . ALA C 2 55  ? 33.372  29.767 27.375  1.00 36.54 ? 218 ALA C CB  1 
ATOM   5519 N  N   . LYS C 2 56  ? 30.828  30.964 28.584  1.00 36.63 ? 219 LYS C N   1 
ATOM   5520 C  CA  . LYS C 2 56  ? 29.626  31.791 28.545  1.00 36.62 ? 219 LYS C CA  1 
ATOM   5521 C  C   . LYS C 2 56  ? 29.606  32.784 29.703  1.00 36.42 ? 219 LYS C C   1 
ATOM   5522 O  O   . LYS C 2 56  ? 29.201  33.931 29.522  1.00 36.37 ? 219 LYS C O   1 
ATOM   5523 C  CB  . LYS C 2 56  ? 28.352  30.940 28.573  1.00 36.82 ? 219 LYS C CB  1 
ATOM   5524 C  CG  . LYS C 2 56  ? 28.196  29.942 27.424  1.00 37.49 ? 219 LYS C CG  1 
ATOM   5525 C  CD  . LYS C 2 56  ? 27.970  30.611 26.059  1.00 38.88 ? 219 LYS C CD  1 
ATOM   5526 C  CE  . LYS C 2 56  ? 27.512  29.603 24.995  1.00 38.09 ? 219 LYS C CE  1 
ATOM   5527 N  NZ  . LYS C 2 56  ? 26.227  28.948 25.376  1.00 38.29 ? 219 LYS C NZ  1 
ATOM   5528 N  N   . LYS C 2 57  ? 30.044  32.336 30.882  1.00 36.20 ? 220 LYS C N   1 
ATOM   5529 C  CA  . LYS C 2 57  ? 30.144  33.196 32.067  1.00 36.15 ? 220 LYS C CA  1 
ATOM   5530 C  C   . LYS C 2 57  ? 31.149  34.320 31.880  1.00 35.82 ? 220 LYS C C   1 
ATOM   5531 O  O   . LYS C 2 57  ? 30.880  35.467 32.246  1.00 35.81 ? 220 LYS C O   1 
ATOM   5532 C  CB  . LYS C 2 57  ? 30.498  32.388 33.316  1.00 36.28 ? 220 LYS C CB  1 
ATOM   5533 C  CG  . LYS C 2 57  ? 29.303  32.066 34.195  1.00 37.52 ? 220 LYS C CG  1 
ATOM   5534 C  CD  . LYS C 2 57  ? 29.729  31.485 35.538  1.00 39.35 ? 220 LYS C CD  1 
ATOM   5535 C  CE  . LYS C 2 57  ? 28.600  31.591 36.562  1.00 40.53 ? 220 LYS C CE  1 
ATOM   5536 N  NZ  . LYS C 2 57  ? 28.814  30.675 37.723  1.00 41.45 ? 220 LYS C NZ  1 
ATOM   5537 N  N   . ALA C 2 58  ? 32.304  33.984 31.312  1.00 35.48 ? 221 ALA C N   1 
ATOM   5538 C  CA  . ALA C 2 58  ? 33.318  34.979 30.993  1.00 35.23 ? 221 ALA C CA  1 
ATOM   5539 C  C   . ALA C 2 58  ? 32.779  35.950 29.945  1.00 35.08 ? 221 ALA C C   1 
ATOM   5540 O  O   . ALA C 2 58  ? 32.887  37.165 30.101  1.00 35.05 ? 221 ALA C O   1 
ATOM   5541 C  CB  . ALA C 2 58  ? 34.590  34.308 30.505  1.00 35.13 ? 221 ALA C CB  1 
ATOM   5542 N  N   . LYS C 2 59  ? 32.176  35.410 28.889  1.00 34.84 ? 222 LYS C N   1 
ATOM   5543 C  CA  . LYS C 2 59  ? 31.639  36.239 27.828  1.00 34.59 ? 222 LYS C CA  1 
ATOM   5544 C  C   . LYS C 2 59  ? 30.554  37.154 28.367  1.00 34.61 ? 222 LYS C C   1 
ATOM   5545 O  O   . LYS C 2 59  ? 30.492  38.319 27.977  1.00 34.88 ? 222 LYS C O   1 
ATOM   5546 C  CB  . LYS C 2 59  ? 31.104  35.395 26.670  1.00 34.60 ? 222 LYS C CB  1 
ATOM   5547 C  CG  . LYS C 2 59  ? 30.834  36.212 25.419  1.00 34.46 ? 222 LYS C CG  1 
ATOM   5548 C  CD  . LYS C 2 59  ? 29.849  35.544 24.486  1.00 34.36 ? 222 LYS C CD  1 
ATOM   5549 C  CE  . LYS C 2 59  ? 29.254  36.571 23.530  1.00 34.56 ? 222 LYS C CE  1 
ATOM   5550 N  NZ  . LYS C 2 59  ? 28.762  35.959 22.268  1.00 33.85 ? 222 LYS C NZ  1 
ATOM   5551 N  N   . LEU C 2 60  ? 29.719  36.633 29.271  1.00 34.55 ? 223 LEU C N   1 
ATOM   5552 C  CA  . LEU C 2 60  ? 28.616  37.401 29.855  1.00 34.45 ? 223 LEU C CA  1 
ATOM   5553 C  C   . LEU C 2 60  ? 29.122  38.563 30.713  1.00 34.98 ? 223 LEU C C   1 
ATOM   5554 O  O   . LEU C 2 60  ? 28.587  39.676 30.653  1.00 34.86 ? 223 LEU C O   1 
ATOM   5555 C  CB  . LEU C 2 60  ? 27.678  36.496 30.665  1.00 34.32 ? 223 LEU C CB  1 
ATOM   5556 C  CG  . LEU C 2 60  ? 26.404  37.153 31.214  1.00 33.73 ? 223 LEU C CG  1 
ATOM   5557 C  CD1 . LEU C 2 60  ? 25.480  37.583 30.090  1.00 32.80 ? 223 LEU C CD1 1 
ATOM   5558 C  CD2 . LEU C 2 60  ? 25.678  36.249 32.191  1.00 33.59 ? 223 LEU C CD2 1 
ATOM   5559 N  N   . SER C 2 61  ? 30.158  38.284 31.502  1.00 35.66 ? 224 SER C N   1 
ATOM   5560 C  CA  . SER C 2 61  ? 30.853  39.282 32.322  1.00 36.20 ? 224 SER C CA  1 
ATOM   5561 C  C   . SER C 2 61  ? 31.340  40.510 31.519  1.00 36.74 ? 224 SER C C   1 
ATOM   5562 O  O   . SER C 2 61  ? 31.139  41.656 31.946  1.00 36.65 ? 224 SER C O   1 
ATOM   5563 C  CB  . SER C 2 61  ? 32.009  38.606 33.064  1.00 35.85 ? 224 SER C CB  1 
ATOM   5564 O  OG  . SER C 2 61  ? 32.943  39.547 33.538  1.00 36.03 ? 224 SER C OG  1 
ATOM   5565 N  N   . LYS C 2 62  ? 31.967  40.261 30.365  1.00 37.41 ? 225 LYS C N   1 
ATOM   5566 C  CA  . LYS C 2 62  ? 32.421  41.319 29.458  1.00 38.21 ? 225 LYS C CA  1 
ATOM   5567 C  C   . LYS C 2 62  ? 31.260  42.138 28.910  1.00 38.63 ? 225 LYS C C   1 
ATOM   5568 O  O   . LYS C 2 62  ? 31.375  43.353 28.761  1.00 38.83 ? 225 LYS C O   1 
ATOM   5569 C  CB  . LYS C 2 62  ? 33.220  40.739 28.287  1.00 38.19 ? 225 LYS C CB  1 
ATOM   5570 C  CG  . LYS C 2 62  ? 34.668  40.369 28.600  1.00 38.71 ? 225 LYS C CG  1 
ATOM   5571 C  CD  . LYS C 2 62  ? 35.377  39.838 27.348  1.00 38.74 ? 225 LYS C CD  1 
ATOM   5572 C  CE  . LYS C 2 62  ? 36.768  39.264 27.666  1.00 39.95 ? 225 LYS C CE  1 
ATOM   5573 N  NZ  . LYS C 2 62  ? 36.700  37.944 28.366  1.00 39.64 ? 225 LYS C NZ  1 
ATOM   5574 N  N   . LEU C 2 63  ? 30.149  41.471 28.602  1.00 39.20 ? 226 LEU C N   1 
ATOM   5575 C  CA  . LEU C 2 63  ? 28.956  42.149 28.094  1.00 39.67 ? 226 LEU C CA  1 
ATOM   5576 C  C   . LEU C 2 63  ? 28.218  42.937 29.181  1.00 40.11 ? 226 LEU C C   1 
ATOM   5577 O  O   . LEU C 2 63  ? 27.569  43.945 28.895  1.00 40.13 ? 226 LEU C O   1 
ATOM   5578 C  CB  . LEU C 2 63  ? 28.014  41.150 27.419  1.00 39.62 ? 226 LEU C CB  1 
ATOM   5579 C  CG  . LEU C 2 63  ? 28.533  40.399 26.185  1.00 39.72 ? 226 LEU C CG  1 
ATOM   5580 C  CD1 . LEU C 2 63  ? 27.544  39.329 25.742  1.00 39.39 ? 226 LEU C CD1 1 
ATOM   5581 C  CD2 . LEU C 2 63  ? 28.830  41.346 25.036  1.00 39.65 ? 226 LEU C CD2 1 
ATOM   5582 N  N   . GLU C 2 64  ? 28.322  42.481 30.424  1.00 40.77 ? 227 GLU C N   1 
ATOM   5583 C  CA  . GLU C 2 64  ? 27.735  43.201 31.553  1.00 41.60 ? 227 GLU C CA  1 
ATOM   5584 C  C   . GLU C 2 64  ? 28.506  44.470 31.926  1.00 41.43 ? 227 GLU C C   1 
ATOM   5585 O  O   . GLU C 2 64  ? 27.915  45.530 32.134  1.00 41.26 ? 227 GLU C O   1 
ATOM   5586 C  CB  . GLU C 2 64  ? 27.566  42.277 32.763  1.00 41.84 ? 227 GLU C CB  1 
ATOM   5587 C  CG  . GLU C 2 64  ? 26.351  41.340 32.660  1.00 44.60 ? 227 GLU C CG  1 
ATOM   5588 C  CD  . GLU C 2 64  ? 25.009  42.090 32.565  1.00 48.36 ? 227 GLU C CD  1 
ATOM   5589 O  OE1 . GLU C 2 64  ? 24.705  42.659 31.488  1.00 49.51 ? 227 GLU C OE1 1 
ATOM   5590 O  OE2 . GLU C 2 64  ? 24.249  42.100 33.567  1.00 50.59 ? 227 GLU C OE2 1 
ATOM   5591 N  N   . GLU C 2 65  ? 29.828  44.358 31.991  1.00 41.55 ? 228 GLU C N   1 
ATOM   5592 C  CA  . GLU C 2 65  ? 30.683  45.495 32.302  1.00 41.60 ? 228 GLU C CA  1 
ATOM   5593 C  C   . GLU C 2 65  ? 30.496  46.641 31.310  1.00 41.00 ? 228 GLU C C   1 
ATOM   5594 O  O   . GLU C 2 65  ? 30.576  47.803 31.707  1.00 41.10 ? 228 GLU C O   1 
ATOM   5595 C  CB  . GLU C 2 65  ? 32.151  45.069 32.360  1.00 41.48 ? 228 GLU C CB  1 
ATOM   5596 C  CG  . GLU C 2 65  ? 33.063  46.105 32.991  1.00 42.42 ? 228 GLU C CG  1 
ATOM   5597 C  CD  . GLU C 2 65  ? 34.541  45.775 32.822  1.00 42.88 ? 228 GLU C CD  1 
ATOM   5598 O  OE1 . GLU C 2 65  ? 35.052  44.895 33.554  1.00 44.59 ? 228 GLU C OE1 1 
ATOM   5599 O  OE2 . GLU C 2 65  ? 35.199  46.409 31.964  1.00 44.51 ? 228 GLU C OE2 1 
ATOM   5600 N  N   . LEU C 2 66  ? 30.247  46.315 30.039  1.00 40.44 ? 229 LEU C N   1 
ATOM   5601 C  CA  . LEU C 2 66  ? 30.033  47.326 28.994  1.00 39.98 ? 229 LEU C CA  1 
ATOM   5602 C  C   . LEU C 2 66  ? 28.681  48.004 29.141  1.00 40.00 ? 229 LEU C C   1 
ATOM   5603 O  O   . LEU C 2 66  ? 28.565  49.218 28.981  1.00 39.97 ? 229 LEU C O   1 
ATOM   5604 C  CB  . LEU C 2 66  ? 30.146  46.726 27.587  1.00 39.77 ? 229 LEU C CB  1 
ATOM   5605 C  CG  . LEU C 2 66  ? 31.499  46.302 26.996  1.00 39.21 ? 229 LEU C CG  1 
ATOM   5606 C  CD1 . LEU C 2 66  ? 31.284  45.605 25.671  1.00 37.77 ? 229 LEU C CD1 1 
ATOM   5607 C  CD2 . LEU C 2 66  ? 32.452  47.476 26.824  1.00 38.88 ? 229 LEU C CD2 1 
ATOM   5608 N  N   . SER C 2 67  ? 27.660  47.211 29.445  1.00 40.05 ? 230 SER C N   1 
ATOM   5609 C  CA  . SER C 2 67  ? 26.305  47.722 29.603  1.00 40.10 ? 230 SER C CA  1 
ATOM   5610 C  C   . SER C 2 67  ? 26.203  48.623 30.818  1.00 40.05 ? 230 SER C C   1 
ATOM   5611 O  O   . SER C 2 67  ? 25.517  49.644 30.782  1.00 40.11 ? 230 SER C O   1 
ATOM   5612 C  CB  . SER C 2 67  ? 25.312  46.569 29.730  1.00 40.20 ? 230 SER C CB  1 
ATOM   5613 O  OG  . SER C 2 67  ? 25.200  45.848 28.518  1.00 40.43 ? 230 SER C OG  1 
ATOM   5614 N  N   . ASP C 2 68  ? 26.886  48.231 31.889  1.00 40.07 ? 231 ASP C N   1 
ATOM   5615 C  CA  . ASP C 2 68  ? 26.977  49.028 33.108  1.00 40.34 ? 231 ASP C CA  1 
ATOM   5616 C  C   . ASP C 2 68  ? 27.670  50.365 32.832  1.00 40.12 ? 231 ASP C C   1 
ATOM   5617 O  O   . ASP C 2 68  ? 27.279  51.389 33.384  1.00 40.28 ? 231 ASP C O   1 
ATOM   5618 C  CB  . ASP C 2 68  ? 27.722  48.239 34.197  1.00 40.76 ? 231 ASP C CB  1 
ATOM   5619 C  CG  . ASP C 2 68  ? 27.645  48.893 35.585  1.00 41.89 ? 231 ASP C CG  1 
ATOM   5620 O  OD1 . ASP C 2 68  ? 26.627  49.551 35.923  1.00 43.13 ? 231 ASP C OD1 1 
ATOM   5621 O  OD2 . ASP C 2 68  ? 28.616  48.719 36.354  1.00 43.04 ? 231 ASP C OD2 1 
ATOM   5622 N  N   . LYS C 2 69  ? 28.686  50.348 31.969  1.00 39.80 ? 232 LYS C N   1 
ATOM   5623 C  CA  . LYS C 2 69  ? 29.373  51.565 31.566  1.00 39.52 ? 232 LYS C CA  1 
ATOM   5624 C  C   . LYS C 2 69  ? 28.462  52.457 30.735  1.00 39.26 ? 232 LYS C C   1 
ATOM   5625 O  O   . LYS C 2 69  ? 28.480  53.672 30.890  1.00 39.26 ? 232 LYS C O   1 
ATOM   5626 C  CB  . LYS C 2 69  ? 30.645  51.254 30.782  1.00 39.64 ? 232 LYS C CB  1 
ATOM   5627 C  CG  . LYS C 2 69  ? 31.698  52.341 30.907  1.00 40.37 ? 232 LYS C CG  1 
ATOM   5628 C  CD  . LYS C 2 69  ? 32.707  52.312 29.768  1.00 42.30 ? 232 LYS C CD  1 
ATOM   5629 C  CE  . LYS C 2 69  ? 33.857  53.290 30.050  1.00 44.16 ? 232 LYS C CE  1 
ATOM   5630 N  NZ  . LYS C 2 69  ? 34.761  53.536 28.881  1.00 44.20 ? 232 LYS C NZ  1 
ATOM   5631 N  N   . ILE C 2 70  ? 27.671  51.851 29.854  1.00 39.09 ? 233 ILE C N   1 
ATOM   5632 C  CA  . ILE C 2 70  ? 26.685  52.590 29.064  1.00 38.89 ? 233 ILE C CA  1 
ATOM   5633 C  C   . ILE C 2 70  ? 25.634  53.232 29.979  1.00 39.13 ? 233 ILE C C   1 
ATOM   5634 O  O   . ILE C 2 70  ? 25.245  54.391 29.775  1.00 38.90 ? 233 ILE C O   1 
ATOM   5635 C  CB  . ILE C 2 70  ? 26.047  51.696 27.977  1.00 38.88 ? 233 ILE C CB  1 
ATOM   5636 C  CG1 . ILE C 2 70  ? 27.109  51.320 26.935  1.00 38.60 ? 233 ILE C CG1 1 
ATOM   5637 C  CG2 . ILE C 2 70  ? 24.856  52.398 27.311  1.00 38.50 ? 233 ILE C CG2 1 
ATOM   5638 C  CD1 . ILE C 2 70  ? 26.687  50.250 25.969  1.00 38.10 ? 233 ILE C CD1 1 
ATOM   5639 N  N   . ASP C 2 71  ? 25.204  52.478 30.992  1.00 39.39 ? 234 ASP C N   1 
ATOM   5640 C  CA  . ASP C 2 71  ? 24.345  52.999 32.056  1.00 39.85 ? 234 ASP C CA  1 
ATOM   5641 C  C   . ASP C 2 71  ? 25.012  54.193 32.770  1.00 39.67 ? 234 ASP C C   1 
ATOM   5642 O  O   . ASP C 2 71  ? 24.408  55.266 32.904  1.00 39.65 ? 234 ASP C O   1 
ATOM   5643 C  CB  . ASP C 2 71  ? 24.012  51.890 33.070  1.00 40.33 ? 234 ASP C CB  1 
ATOM   5644 C  CG  . ASP C 2 71  ? 23.057  50.808 32.509  1.00 42.30 ? 234 ASP C CG  1 
ATOM   5645 O  OD1 . ASP C 2 71  ? 22.299  51.081 31.535  1.00 43.55 ? 234 ASP C OD1 1 
ATOM   5646 O  OD2 . ASP C 2 71  ? 23.060  49.677 33.075  1.00 43.66 ? 234 ASP C OD2 1 
ATOM   5647 N  N   . GLU C 2 72  ? 26.259  53.989 33.207  1.00 39.24 ? 235 GLU C N   1 
ATOM   5648 C  CA  . GLU C 2 72  ? 27.066  54.993 33.897  1.00 39.02 ? 235 GLU C CA  1 
ATOM   5649 C  C   . GLU C 2 72  ? 27.125  56.300 33.102  1.00 38.21 ? 235 GLU C C   1 
ATOM   5650 O  O   . GLU C 2 72  ? 26.818  57.366 33.630  1.00 38.24 ? 235 GLU C O   1 
ATOM   5651 C  CB  . GLU C 2 72  ? 28.481  54.437 34.142  1.00 38.92 ? 235 GLU C CB  1 
ATOM   5652 C  CG  . GLU C 2 72  ? 29.384  55.237 35.114  1.00 40.34 ? 235 GLU C CG  1 
ATOM   5653 C  CD  . GLU C 2 72  ? 30.906  54.990 34.900  1.00 40.75 ? 235 GLU C CD  1 
ATOM   5654 O  OE1 . GLU C 2 72  ? 31.345  53.805 34.846  1.00 41.49 ? 235 GLU C OE1 1 
ATOM   5655 O  OE2 . GLU C 2 72  ? 31.661  55.997 34.793  1.00 42.74 ? 235 GLU C OE2 1 
ATOM   5656 N  N   . LEU C 2 73  ? 27.495  56.205 31.828  1.00 37.58 ? 236 LEU C N   1 
ATOM   5657 C  CA  . LEU C 2 73  ? 27.699  57.385 30.980  1.00 36.98 ? 236 LEU C CA  1 
ATOM   5658 C  C   . LEU C 2 73  ? 26.421  58.174 30.732  1.00 36.81 ? 236 LEU C C   1 
ATOM   5659 O  O   . LEU C 2 73  ? 26.427  59.399 30.805  1.00 36.57 ? 236 LEU C O   1 
ATOM   5660 C  CB  . LEU C 2 73  ? 28.343  57.002 29.641  1.00 36.71 ? 236 LEU C CB  1 
ATOM   5661 C  CG  . LEU C 2 73  ? 29.763  56.440 29.661  1.00 36.37 ? 236 LEU C CG  1 
ATOM   5662 C  CD1 . LEU C 2 73  ? 30.165  55.949 28.288  1.00 36.28 ? 236 LEU C CD1 1 
ATOM   5663 C  CD2 . LEU C 2 73  ? 30.760  57.460 30.173  1.00 36.41 ? 236 LEU C CD2 1 
ATOM   5664 N  N   . ASP C 2 74  ? 25.334  57.468 30.440  1.00 36.84 ? 237 ASP C N   1 
ATOM   5665 C  CA  . ASP C 2 74  ? 24.040  58.102 30.227  1.00 37.12 ? 237 ASP C CA  1 
ATOM   5666 C  C   . ASP C 2 74  ? 23.639  58.979 31.404  1.00 36.74 ? 237 ASP C C   1 
ATOM   5667 O  O   . ASP C 2 74  ? 23.106  60.073 31.220  1.00 36.64 ? 237 ASP C O   1 
ATOM   5668 C  CB  . ASP C 2 74  ? 22.958  57.055 29.955  1.00 37.58 ? 237 ASP C CB  1 
ATOM   5669 C  CG  . ASP C 2 74  ? 22.688  56.852 28.461  1.00 39.36 ? 237 ASP C CG  1 
ATOM   5670 O  OD1 . ASP C 2 74  ? 23.129  57.696 27.626  1.00 41.11 ? 237 ASP C OD1 1 
ATOM   5671 O  OD2 . ASP C 2 74  ? 22.013  55.846 28.129  1.00 40.21 ? 237 ASP C OD2 1 
ATOM   5672 N  N   . ALA C 2 75  ? 23.912  58.500 32.611  1.00 36.60 ? 238 ALA C N   1 
ATOM   5673 C  CA  . ALA C 2 75  ? 23.625  59.272 33.819  1.00 36.49 ? 238 ALA C CA  1 
ATOM   5674 C  C   . ALA C 2 75  ? 24.535  60.485 33.912  1.00 36.31 ? 238 ALA C C   1 
ATOM   5675 O  O   . ALA C 2 75  ? 24.065  61.588 34.189  1.00 36.23 ? 238 ALA C O   1 
ATOM   5676 C  CB  . ALA C 2 75  ? 23.758  58.402 35.064  1.00 36.36 ? 238 ALA C CB  1 
ATOM   5677 N  N   . GLU C 2 76  ? 25.829  60.268 33.673  1.00 36.21 ? 239 GLU C N   1 
ATOM   5678 C  CA  . GLU C 2 76  ? 26.817  61.337 33.709  1.00 36.41 ? 239 GLU C CA  1 
ATOM   5679 C  C   . GLU C 2 76  ? 26.441  62.433 32.702  1.00 36.09 ? 239 GLU C C   1 
ATOM   5680 O  O   . GLU C 2 76  ? 26.437  63.619 33.038  1.00 35.94 ? 239 GLU C O   1 
ATOM   5681 C  CB  . GLU C 2 76  ? 28.234  60.785 33.465  1.00 36.31 ? 239 GLU C CB  1 
ATOM   5682 C  CG  . GLU C 2 76  ? 28.959  60.273 34.733  1.00 37.04 ? 239 GLU C CG  1 
ATOM   5683 C  CD  . GLU C 2 76  ? 30.104  59.266 34.453  1.00 37.59 ? 239 GLU C CD  1 
ATOM   5684 O  OE1 . GLU C 2 76  ? 30.620  59.206 33.309  1.00 38.75 ? 239 GLU C OE1 1 
ATOM   5685 O  OE2 . GLU C 2 76  ? 30.494  58.525 35.391  1.00 38.85 ? 239 GLU C OE2 1 
ATOM   5686 N  N   . ILE C 2 77  ? 26.082  62.028 31.486  1.00 35.90 ? 240 ILE C N   1 
ATOM   5687 C  CA  . ILE C 2 77  ? 25.723  62.976 30.434  1.00 35.79 ? 240 ILE C CA  1 
ATOM   5688 C  C   . ILE C 2 77  ? 24.478  63.762 30.841  1.00 36.13 ? 240 ILE C C   1 
ATOM   5689 O  O   . ILE C 2 77  ? 24.410  64.985 30.656  1.00 35.99 ? 240 ILE C O   1 
ATOM   5690 C  CB  . ILE C 2 77  ? 25.547  62.266 29.061  1.00 35.68 ? 240 ILE C CB  1 
ATOM   5691 C  CG1 . ILE C 2 77  ? 26.895  61.701 28.589  1.00 35.62 ? 240 ILE C CG1 1 
ATOM   5692 C  CG2 . ILE C 2 77  ? 24.973  63.224 28.017  1.00 35.56 ? 240 ILE C CG2 1 
ATOM   5693 C  CD1 . ILE C 2 77  ? 26.865  60.908 27.301  1.00 35.51 ? 240 ILE C CD1 1 
ATOM   5694 N  N   . ALA C 2 78  ? 23.516  63.042 31.419  1.00 36.58 ? 241 ALA C N   1 
ATOM   5695 C  CA  . ALA C 2 78  ? 22.237  63.601 31.861  1.00 36.84 ? 241 ALA C CA  1 
ATOM   5696 C  C   . ALA C 2 78  ? 22.399  64.687 32.911  1.00 37.18 ? 241 ALA C C   1 
ATOM   5697 O  O   . ALA C 2 78  ? 21.714  65.708 32.838  1.00 37.25 ? 241 ALA C O   1 
ATOM   5698 C  CB  . ALA C 2 78  ? 21.334  62.501 32.391  1.00 36.92 ? 241 ALA C CB  1 
ATOM   5699 N  N   . LYS C 2 79  ? 23.291  64.462 33.883  1.00 37.49 ? 242 LYS C N   1 
ATOM   5700 C  CA  . LYS C 2 79  ? 23.536  65.439 34.953  1.00 37.80 ? 242 LYS C CA  1 
ATOM   5701 C  C   . LYS C 2 79  ? 24.261  66.654 34.422  1.00 37.60 ? 242 LYS C C   1 
ATOM   5702 O  O   . LYS C 2 79  ? 23.941  67.786 34.792  1.00 37.73 ? 242 LYS C O   1 
ATOM   5703 C  CB  . LYS C 2 79  ? 24.293  64.825 36.136  1.00 38.17 ? 242 LYS C CB  1 
ATOM   5704 C  CG  . LYS C 2 79  ? 23.420  63.863 36.948  1.00 39.79 ? 242 LYS C CG  1 
ATOM   5705 C  CD  . LYS C 2 79  ? 23.898  63.642 38.393  1.00 41.57 ? 242 LYS C CD  1 
ATOM   5706 C  CE  . LYS C 2 79  ? 23.091  62.513 39.077  1.00 41.09 ? 242 LYS C CE  1 
ATOM   5707 N  NZ  . LYS C 2 79  ? 23.435  61.144 38.541  1.00 41.95 ? 242 LYS C NZ  1 
ATOM   5708 N  N   . LEU C 2 80  ? 25.211  66.414 33.525  1.00 37.37 ? 243 LEU C N   1 
ATOM   5709 C  CA  . LEU C 2 80  ? 25.973  67.490 32.918  1.00 37.16 ? 243 LEU C CA  1 
ATOM   5710 C  C   . LEU C 2 80  ? 25.094  68.419 32.083  1.00 37.37 ? 243 LEU C C   1 
ATOM   5711 O  O   . LEU C 2 80  ? 25.140  69.634 32.265  1.00 37.34 ? 243 LEU C O   1 
ATOM   5712 C  CB  . LEU C 2 80  ? 27.140  66.936 32.103  1.00 36.85 ? 243 LEU C CB  1 
ATOM   5713 C  CG  . LEU C 2 80  ? 28.274  66.289 32.905  1.00 36.26 ? 243 LEU C CG  1 
ATOM   5714 C  CD1 . LEU C 2 80  ? 29.290  65.693 31.959  1.00 36.16 ? 243 LEU C CD1 1 
ATOM   5715 C  CD2 . LEU C 2 80  ? 28.946  67.252 33.887  1.00 35.15 ? 243 LEU C CD2 1 
ATOM   5716 N  N   . GLU C 2 81  ? 24.280  67.847 31.196  1.00 37.76 ? 244 GLU C N   1 
ATOM   5717 C  CA  . GLU C 2 81  ? 23.351  68.631 30.373  1.00 38.30 ? 244 GLU C CA  1 
ATOM   5718 C  C   . GLU C 2 81  ? 22.415  69.516 31.199  1.00 38.41 ? 244 GLU C C   1 
ATOM   5719 O  O   . GLU C 2 81  ? 22.061  70.616 30.778  1.00 38.34 ? 244 GLU C O   1 
ATOM   5720 C  CB  . GLU C 2 81  ? 22.540  67.720 29.458  1.00 38.39 ? 244 GLU C CB  1 
ATOM   5721 C  CG  . GLU C 2 81  ? 23.150  67.540 28.085  1.00 39.70 ? 244 GLU C CG  1 
ATOM   5722 C  CD  . GLU C 2 81  ? 22.704  66.250 27.410  1.00 41.96 ? 244 GLU C CD  1 
ATOM   5723 O  OE1 . GLU C 2 81  ? 22.751  66.191 26.159  1.00 42.64 ? 244 GLU C OE1 1 
ATOM   5724 O  OE2 . GLU C 2 81  ? 22.312  65.296 28.127  1.00 42.68 ? 244 GLU C OE2 1 
ATOM   5725 N  N   . ASP C 2 82  ? 22.025  69.024 32.371  1.00 38.69 ? 245 ASP C N   1 
ATOM   5726 C  CA  . ASP C 2 82  ? 21.198  69.781 33.290  1.00 39.02 ? 245 ASP C CA  1 
ATOM   5727 C  C   . ASP C 2 82  ? 22.007  70.878 33.959  1.00 38.99 ? 245 ASP C C   1 
ATOM   5728 O  O   . ASP C 2 82  ? 21.563  72.024 34.026  1.00 39.23 ? 245 ASP C O   1 
ATOM   5729 C  CB  . ASP C 2 82  ? 20.568  68.854 34.325  1.00 39.41 ? 245 ASP C CB  1 
ATOM   5730 C  CG  . ASP C 2 82  ? 19.244  68.271 33.849  1.00 40.62 ? 245 ASP C CG  1 
ATOM   5731 O  OD1 . ASP C 2 82  ? 18.293  69.060 33.665  1.00 41.94 ? 245 ASP C OD1 1 
ATOM   5732 O  OD2 . ASP C 2 82  ? 19.148  67.034 33.663  1.00 41.28 ? 245 ASP C OD2 1 
ATOM   5733 N  N   . GLN C 2 83  ? 23.198  70.536 34.443  1.00 38.89 ? 246 GLN C N   1 
ATOM   5734 C  CA  . GLN C 2 83  ? 24.119  71.544 34.953  1.00 38.69 ? 246 GLN C CA  1 
ATOM   5735 C  C   . GLN C 2 83  ? 24.261  72.665 33.938  1.00 38.79 ? 246 GLN C C   1 
ATOM   5736 O  O   . GLN C 2 83  ? 24.132  73.837 34.277  1.00 38.74 ? 246 GLN C O   1 
ATOM   5737 C  CB  . GLN C 2 83  ? 25.489  70.945 35.208  1.00 38.47 ? 246 GLN C CB  1 
ATOM   5738 C  CG  . GLN C 2 83  ? 25.705  70.421 36.586  1.00 38.03 ? 246 GLN C CG  1 
ATOM   5739 C  CD  . GLN C 2 83  ? 27.176  70.229 36.866  1.00 38.28 ? 246 GLN C CD  1 
ATOM   5740 O  OE1 . GLN C 2 83  ? 27.935  71.199 36.964  1.00 37.79 ? 246 GLN C OE1 1 
ATOM   5741 N  NE2 . GLN C 2 83  ? 27.595  68.974 36.984  1.00 38.25 ? 246 GLN C NE2 1 
ATOM   5742 N  N   . LEU C 2 84  ? 24.511  72.283 32.687  1.00 39.00 ? 247 LEU C N   1 
ATOM   5743 C  CA  . LEU C 2 84  ? 24.685  73.231 31.601  1.00 39.17 ? 247 LEU C CA  1 
ATOM   5744 C  C   . LEU C 2 84  ? 23.412  74.024 31.304  1.00 39.81 ? 247 LEU C C   1 
ATOM   5745 O  O   . LEU C 2 84  ? 23.470  75.247 31.174  1.00 39.79 ? 247 LEU C O   1 
ATOM   5746 C  CB  . LEU C 2 84  ? 25.202  72.531 30.340  1.00 38.97 ? 247 LEU C CB  1 
ATOM   5747 C  CG  . LEU C 2 84  ? 25.536  73.414 29.135  1.00 38.35 ? 247 LEU C CG  1 
ATOM   5748 C  CD1 . LEU C 2 84  ? 26.625  74.420 29.463  1.00 37.55 ? 247 LEU C CD1 1 
ATOM   5749 C  CD2 . LEU C 2 84  ? 25.931  72.564 27.948  1.00 38.58 ? 247 LEU C CD2 1 
ATOM   5750 N  N   . LYS C 2 85  ? 22.271  73.341 31.215  1.00 40.49 ? 248 LYS C N   1 
ATOM   5751 C  CA  . LYS C 2 85  ? 21.001  74.010 30.906  1.00 41.40 ? 248 LYS C CA  1 
ATOM   5752 C  C   . LYS C 2 85  ? 20.689  75.161 31.880  1.00 41.77 ? 248 LYS C C   1 
ATOM   5753 O  O   . LYS C 2 85  ? 19.927  76.066 31.541  1.00 41.89 ? 248 LYS C O   1 
ATOM   5754 C  CB  . LYS C 2 85  ? 19.841  73.006 30.793  1.00 41.52 ? 248 LYS C CB  1 
ATOM   5755 C  CG  . LYS C 2 85  ? 18.608  73.524 30.036  1.00 42.51 ? 248 LYS C CG  1 
ATOM   5756 C  CD  . LYS C 2 85  ? 17.393  73.692 30.966  1.00 44.94 ? 248 LYS C CD  1 
ATOM   5757 C  CE  . LYS C 2 85  ? 16.735  75.089 30.845  1.00 46.12 ? 248 LYS C CE  1 
ATOM   5758 N  NZ  . LYS C 2 85  ? 16.102  75.394 29.518  1.00 46.07 ? 248 LYS C NZ  1 
ATOM   5759 N  N   . ALA C 2 86  ? 21.295  75.131 33.067  1.00 42.25 ? 249 ALA C N   1 
ATOM   5760 C  CA  . ALA C 2 86  ? 21.351  76.305 33.939  1.00 42.93 ? 249 ALA C CA  1 
ATOM   5761 C  C   . ALA C 2 86  ? 22.469  77.265 33.474  1.00 43.53 ? 249 ALA C C   1 
ATOM   5762 O  O   . ALA C 2 86  ? 23.565  77.312 34.046  1.00 43.35 ? 249 ALA C O   1 
ATOM   5763 C  CB  . ALA C 2 86  ? 21.553  75.880 35.384  1.00 42.97 ? 249 ALA C CB  1 
ATOM   5764 N  N   . ALA C 2 87  ? 22.177  78.016 32.411  1.00 44.41 ? 250 ALA C N   1 
ATOM   5765 C  CA  . ALA C 2 87  ? 23.153  78.895 31.763  1.00 44.99 ? 250 ALA C CA  1 
ATOM   5766 C  C   . ALA C 2 87  ? 22.720  80.355 31.852  1.00 45.65 ? 250 ALA C C   1 
ATOM   5767 O  O   . ALA C 2 87  ? 22.053  80.867 30.940  1.00 45.72 ? 250 ALA C O   1 
ATOM   5768 C  CB  . ALA C 2 87  ? 23.349  78.486 30.303  1.00 44.81 ? 250 ALA C CB  1 
ATOM   5769 N  N   . GLU C 2 88  ? 23.066  80.990 32.979  1.00 46.42 ? 251 GLU C N   1 
ATOM   5770 C  CA  . GLU C 2 88  ? 22.975  82.459 33.218  1.00 46.89 ? 251 GLU C CA  1 
ATOM   5771 C  C   . GLU C 2 88  ? 24.128  82.829 34.159  1.00 47.16 ? 251 GLU C C   1 
ATOM   5772 O  O   . GLU C 2 88  ? 24.427  84.005 34.389  1.00 46.89 ? 251 GLU C O   1 
ATOM   5773 C  CB  . GLU C 2 88  ? 21.651  82.855 33.891  1.00 46.88 ? 251 GLU C CB  1 
ATOM   5774 C  CG  . GLU C 2 88  ? 20.357  82.398 33.188  1.00 47.17 ? 251 GLU C CG  1 
ATOM   5775 C  CD  . GLU C 2 88  ? 19.898  81.012 33.631  1.00 47.13 ? 251 GLU C CD  1 
ATOM   5776 O  OE1 . GLU C 2 88  ? 19.860  80.761 34.858  1.00 47.35 ? 251 GLU C OE1 1 
ATOM   5777 O  OE2 . GLU C 2 88  ? 19.573  80.177 32.752  1.00 46.43 ? 251 GLU C OE2 1 
ATOM   5778 N  N   . GLU C 2 89  ? 24.786  81.768 34.636  1.00 47.66 ? 252 GLU C N   1 
ATOM   5779 C  CA  . GLU C 2 89  ? 25.591  81.690 35.870  1.00 47.74 ? 252 GLU C CA  1 
ATOM   5780 C  C   . GLU C 2 89  ? 24.762  81.818 37.152  1.00 47.82 ? 252 GLU C C   1 
ATOM   5781 O  O   . GLU C 2 89  ? 24.836  82.811 37.875  1.00 47.87 ? 252 GLU C O   1 
ATOM   5782 C  CB  . GLU C 2 89  ? 26.814  82.608 35.874  1.00 47.71 ? 252 GLU C CB  1 
ATOM   5783 C  CG  . GLU C 2 89  ? 28.005  81.928 36.534  1.00 47.79 ? 252 GLU C CG  1 
ATOM   5784 C  CD  . GLU C 2 89  ? 28.354  80.597 35.862  1.00 47.91 ? 252 GLU C CD  1 
ATOM   5785 O  OE1 . GLU C 2 89  ? 28.035  79.533 36.432  1.00 46.63 ? 252 GLU C OE1 1 
ATOM   5786 O  OE2 . GLU C 2 89  ? 28.929  80.614 34.749  1.00 48.52 ? 252 GLU C OE2 1 
ATOM   5787 N  N   . GLU C 2 94  ? 31.531  81.193 35.558  1.00 27.85 ? 257 GLU C N   1 
ATOM   5788 C  CA  . GLU C 2 94  ? 31.944  81.956 34.342  1.00 28.12 ? 257 GLU C CA  1 
ATOM   5789 C  C   . GLU C 2 94  ? 31.841  81.136 33.053  1.00 27.40 ? 257 GLU C C   1 
ATOM   5790 O  O   . GLU C 2 94  ? 31.475  79.962 33.075  1.00 27.11 ? 257 GLU C O   1 
ATOM   5791 C  CB  . GLU C 2 94  ? 33.369  82.530 34.503  1.00 28.75 ? 257 GLU C CB  1 
ATOM   5792 C  CG  . GLU C 2 94  ? 34.547  81.600 34.067  1.00 30.51 ? 257 GLU C CG  1 
ATOM   5793 C  CD  . GLU C 2 94  ? 34.894  80.521 35.096  1.00 33.34 ? 257 GLU C CD  1 
ATOM   5794 O  OE1 . GLU C 2 94  ? 34.426  80.610 36.260  1.00 35.21 ? 257 GLU C OE1 1 
ATOM   5795 O  OE2 . GLU C 2 94  ? 35.643  79.578 34.741  1.00 34.19 ? 257 GLU C OE2 1 
ATOM   5796 N  N   . ASP C 2 95  ? 32.190  81.778 31.940  1.00 26.75 ? 258 ASP C N   1 
ATOM   5797 C  CA  . ASP C 2 95  ? 32.066  81.198 30.615  1.00 26.09 ? 258 ASP C CA  1 
ATOM   5798 C  C   . ASP C 2 95  ? 33.011  80.018 30.356  1.00 25.89 ? 258 ASP C C   1 
ATOM   5799 O  O   . ASP C 2 95  ? 32.701  79.155 29.540  1.00 26.11 ? 258 ASP C O   1 
ATOM   5800 C  CB  . ASP C 2 95  ? 32.256  82.281 29.553  1.00 25.79 ? 258 ASP C CB  1 
ATOM   5801 C  CG  . ASP C 2 95  ? 31.674  81.893 28.217  1.00 25.80 ? 258 ASP C CG  1 
ATOM   5802 O  OD1 . ASP C 2 95  ? 30.429  81.813 28.096  1.00 26.45 ? 258 ASP C OD1 1 
ATOM   5803 O  OD2 . ASP C 2 95  ? 32.460  81.670 27.278  1.00 25.56 ? 258 ASP C OD2 1 
ATOM   5804 N  N   . TYR C 2 96  ? 34.154  79.979 31.040  1.00 25.63 ? 259 TYR C N   1 
ATOM   5805 C  CA  . TYR C 2 96  ? 35.138  78.903 30.838  1.00 25.18 ? 259 TYR C CA  1 
ATOM   5806 C  C   . TYR C 2 96  ? 34.727  77.633 31.559  1.00 25.11 ? 259 TYR C C   1 
ATOM   5807 O  O   . TYR C 2 96  ? 34.981  76.532 31.079  1.00 25.27 ? 259 TYR C O   1 
ATOM   5808 C  CB  . TYR C 2 96  ? 36.539  79.329 31.281  1.00 24.98 ? 259 TYR C CB  1 
ATOM   5809 C  CG  . TYR C 2 96  ? 37.642  78.390 30.837  1.00 24.73 ? 259 TYR C CG  1 
ATOM   5810 C  CD1 . TYR C 2 96  ? 38.065  78.359 29.505  1.00 24.70 ? 259 TYR C CD1 1 
ATOM   5811 C  CD2 . TYR C 2 96  ? 38.274  77.543 31.743  1.00 24.00 ? 259 TYR C CD2 1 
ATOM   5812 C  CE1 . TYR C 2 96  ? 39.075  77.505 29.089  1.00 24.06 ? 259 TYR C CE1 1 
ATOM   5813 C  CE2 . TYR C 2 96  ? 39.288  76.684 31.331  1.00 23.78 ? 259 TYR C CE2 1 
ATOM   5814 C  CZ  . TYR C 2 96  ? 39.680  76.673 30.003  1.00 23.96 ? 259 TYR C CZ  1 
ATOM   5815 O  OH  . TYR C 2 96  ? 40.682  75.830 29.582  1.00 24.52 ? 259 TYR C OH  1 
ATOM   5816 N  N   . PHE C 2 97  ? 34.099  77.792 32.718  1.00 25.11 ? 260 PHE C N   1 
ATOM   5817 C  CA  . PHE C 2 97  ? 33.462  76.676 33.403  1.00 25.21 ? 260 PHE C CA  1 
ATOM   5818 C  C   . PHE C 2 97  ? 32.374  76.068 32.503  1.00 25.11 ? 260 PHE C C   1 
ATOM   5819 O  O   . PHE C 2 97  ? 32.282  74.847 32.388  1.00 25.31 ? 260 PHE C O   1 
ATOM   5820 C  CB  . PHE C 2 97  ? 32.888  77.128 34.756  1.00 25.42 ? 260 PHE C CB  1 
ATOM   5821 C  CG  . PHE C 2 97  ? 32.264  76.023 35.549  1.00 25.73 ? 260 PHE C CG  1 
ATOM   5822 C  CD1 . PHE C 2 97  ? 33.047  75.195 36.344  1.00 26.43 ? 260 PHE C CD1 1 
ATOM   5823 C  CD2 . PHE C 2 97  ? 30.885  75.802 35.497  1.00 26.34 ? 260 PHE C CD2 1 
ATOM   5824 C  CE1 . PHE C 2 97  ? 32.461  74.155 37.077  1.00 27.17 ? 260 PHE C CE1 1 
ATOM   5825 C  CE2 . PHE C 2 97  ? 30.292  74.767 36.226  1.00 26.05 ? 260 PHE C CE2 1 
ATOM   5826 C  CZ  . PHE C 2 97  ? 31.079  73.944 37.017  1.00 26.29 ? 260 PHE C CZ  1 
ATOM   5827 N  N   . LYS C 2 98  ? 31.570  76.927 31.868  1.00 24.89 ? 261 LYS C N   1 
ATOM   5828 C  CA  . LYS C 2 98  ? 30.565  76.519 30.878  1.00 24.74 ? 261 LYS C CA  1 
ATOM   5829 C  C   . LYS C 2 98  ? 31.173  75.694 29.755  1.00 24.12 ? 261 LYS C C   1 
ATOM   5830 O  O   . LYS C 2 98  ? 30.709  74.592 29.470  1.00 24.13 ? 261 LYS C O   1 
ATOM   5831 C  CB  . LYS C 2 98  ? 29.867  77.744 30.281  1.00 24.68 ? 261 LYS C CB  1 
ATOM   5832 C  CG  . LYS C 2 98  ? 28.380  77.844 30.580  1.00 25.35 ? 261 LYS C CG  1 
ATOM   5833 C  CD  . LYS C 2 98  ? 27.769  79.146 30.037  1.00 26.15 ? 261 LYS C CD  1 
ATOM   5834 C  CE  . LYS C 2 98  ? 27.935  79.311 28.521  1.00 28.62 ? 261 LYS C CE  1 
ATOM   5835 N  NZ  . LYS C 2 98  ? 27.408  78.145 27.722  1.00 29.49 ? 261 LYS C NZ  1 
ATOM   5836 N  N   . GLU C 2 99  ? 32.209  76.234 29.122  1.00 23.52 ? 262 GLU C N   1 
ATOM   5837 C  CA  . GLU C 2 99  ? 32.914  75.533 28.063  1.00 23.33 ? 262 GLU C CA  1 
ATOM   5838 C  C   . GLU C 2 99  ? 33.487  74.221 28.598  1.00 23.25 ? 262 GLU C C   1 
ATOM   5839 O  O   . GLU C 2 99  ? 33.451  73.191 27.916  1.00 23.11 ? 262 GLU C O   1 
ATOM   5840 C  CB  . GLU C 2 99  ? 34.011  76.422 27.481  1.00 23.36 ? 262 GLU C CB  1 
ATOM   5841 C  CG  . GLU C 2 99  ? 34.862  75.766 26.417  1.00 23.28 ? 262 GLU C CG  1 
ATOM   5842 C  CD  . GLU C 2 99  ? 35.657  76.775 25.622  1.00 24.01 ? 262 GLU C CD  1 
ATOM   5843 O  OE1 . GLU C 2 99  ? 35.040  77.540 24.849  1.00 24.08 ? 262 GLU C OE1 1 
ATOM   5844 O  OE2 . GLU C 2 99  ? 36.901  76.801 25.758  1.00 24.28 ? 262 GLU C OE2 1 
ATOM   5845 N  N   . GLY C 2 100 ? 33.991  74.273 29.829  1.00 23.02 ? 263 GLY C N   1 
ATOM   5846 C  CA  . GLY C 2 100 ? 34.447  73.088 30.537  1.00 23.12 ? 263 GLY C CA  1 
ATOM   5847 C  C   . GLY C 2 100 ? 33.389  72.000 30.589  1.00 23.22 ? 263 GLY C C   1 
ATOM   5848 O  O   . GLY C 2 100 ? 33.706  70.817 30.467  1.00 23.22 ? 263 GLY C O   1 
ATOM   5849 N  N   . LEU C 2 101 ? 32.130  72.404 30.762  1.00 23.33 ? 264 LEU C N   1 
ATOM   5850 C  CA  . LEU C 2 101 ? 31.002  71.472 30.763  1.00 23.23 ? 264 LEU C CA  1 
ATOM   5851 C  C   . LEU C 2 101 ? 30.740  70.990 29.355  1.00 23.18 ? 264 LEU C C   1 
ATOM   5852 O  O   . LEU C 2 101 ? 30.598  69.788 29.129  1.00 22.96 ? 264 LEU C O   1 
ATOM   5853 C  CB  . LEU C 2 101 ? 29.746  72.128 31.331  1.00 23.13 ? 264 LEU C CB  1 
ATOM   5854 C  CG  . LEU C 2 101 ? 29.739  72.339 32.842  1.00 23.39 ? 264 LEU C CG  1 
ATOM   5855 C  CD1 . LEU C 2 101 ? 28.758  73.432 33.246  1.00 23.41 ? 264 LEU C CD1 1 
ATOM   5856 C  CD2 . LEU C 2 101 ? 29.415  71.026 33.531  1.00 23.86 ? 264 LEU C CD2 1 
ATOM   5857 N  N   . GLU C 2 102 ? 30.702  71.932 28.413  1.00 23.28 ? 265 GLU C N   1 
ATOM   5858 C  CA  . GLU C 2 102 ? 30.429  71.610 27.012  1.00 23.77 ? 265 GLU C CA  1 
ATOM   5859 C  C   . GLU C 2 102 ? 31.410  70.556 26.521  1.00 23.76 ? 265 GLU C C   1 
ATOM   5860 O  O   . GLU C 2 102 ? 30.992  69.545 25.945  1.00 23.76 ? 265 GLU C O   1 
ATOM   5861 C  CB  . GLU C 2 102 ? 30.480  72.856 26.128  1.00 23.64 ? 265 GLU C CB  1 
ATOM   5862 C  CG  . GLU C 2 102 ? 29.410  73.890 26.460  1.00 24.01 ? 265 GLU C CG  1 
ATOM   5863 C  CD  . GLU C 2 102 ? 29.686  75.259 25.830  1.00 24.38 ? 265 GLU C CD  1 
ATOM   5864 O  OE1 . GLU C 2 102 ? 30.174  75.298 24.678  1.00 25.10 ? 265 GLU C OE1 1 
ATOM   5865 O  OE2 . GLU C 2 102 ? 29.402  76.294 26.482  1.00 24.33 ? 265 GLU C OE2 1 
ATOM   5866 N  N   . LYS C 2 103 ? 32.701  70.792 26.784  1.00 23.70 ? 266 LYS C N   1 
ATOM   5867 C  CA  . LYS C 2 103 ? 33.773  69.856 26.444  1.00 23.78 ? 266 LYS C CA  1 
ATOM   5868 C  C   . LYS C 2 103 ? 33.521  68.480 27.043  1.00 23.57 ? 266 LYS C C   1 
ATOM   5869 O  O   . LYS C 2 103 ? 33.673  67.472 26.361  1.00 23.75 ? 266 LYS C O   1 
ATOM   5870 C  CB  . LYS C 2 103 ? 35.136  70.355 26.939  1.00 23.74 ? 266 LYS C CB  1 
ATOM   5871 C  CG  . LYS C 2 103 ? 35.776  71.504 26.168  1.00 24.26 ? 266 LYS C CG  1 
ATOM   5872 C  CD  . LYS C 2 103 ? 37.218  71.686 26.652  1.00 24.50 ? 266 LYS C CD  1 
ATOM   5873 C  CE  . LYS C 2 103 ? 37.636  73.153 26.789  1.00 25.61 ? 266 LYS C CE  1 
ATOM   5874 N  NZ  . LYS C 2 103 ? 38.313  73.674 25.563  1.00 26.28 ? 266 LYS C NZ  1 
ATOM   5875 N  N   . THR C 2 104 ? 33.147  68.440 28.319  1.00 23.35 ? 267 THR C N   1 
ATOM   5876 C  CA  . THR C 2 104 ? 32.963  67.169 29.008  1.00 23.40 ? 267 THR C CA  1 
ATOM   5877 C  C   . THR C 2 104 ? 31.772  66.400 28.456  1.00 23.57 ? 267 THR C C   1 
ATOM   5878 O  O   . THR C 2 104 ? 31.870  65.200 28.248  1.00 23.58 ? 267 THR C O   1 
ATOM   5879 C  CB  . THR C 2 104 ? 32.826  67.355 30.516  1.00 23.24 ? 267 THR C CB  1 
ATOM   5880 O  OG1 . THR C 2 104 ? 33.854  68.237 30.958  1.00 23.87 ? 267 THR C OG1 1 
ATOM   5881 C  CG2 . THR C 2 104 ? 32.986  66.040 31.244  1.00 22.58 ? 267 THR C CG2 1 
ATOM   5882 N  N   . ILE C 2 105 ? 30.661  67.092 28.207  1.00 23.84 ? 268 ILE C N   1 
ATOM   5883 C  CA  . ILE C 2 105 ? 29.491  66.473 27.578  1.00 23.98 ? 268 ILE C CA  1 
ATOM   5884 C  C   . ILE C 2 105 ? 29.872  65.785 26.260  1.00 24.10 ? 268 ILE C C   1 
ATOM   5885 O  O   . ILE C 2 105 ? 29.603  64.599 26.078  1.00 24.13 ? 268 ILE C O   1 
ATOM   5886 C  CB  . ILE C 2 105 ? 28.341  67.488 27.387  1.00 23.89 ? 268 ILE C CB  1 
ATOM   5887 C  CG1 . ILE C 2 105 ? 27.845  67.954 28.753  1.00 23.69 ? 268 ILE C CG1 1 
ATOM   5888 C  CG2 . ILE C 2 105 ? 27.186  66.876 26.592  1.00 23.87 ? 268 ILE C CG2 1 
ATOM   5889 C  CD1 . ILE C 2 105 ? 26.807  69.058 28.705  1.00 23.67 ? 268 ILE C CD1 1 
ATOM   5890 N  N   . ALA C 2 106 ? 30.527  66.529 25.373  1.00 24.41 ? 269 ALA C N   1 
ATOM   5891 C  CA  . ALA C 2 106 ? 31.050  65.998 24.105  1.00 24.85 ? 269 ALA C CA  1 
ATOM   5892 C  C   . ALA C 2 106 ? 31.947  64.754 24.260  1.00 24.96 ? 269 ALA C C   1 
ATOM   5893 O  O   . ALA C 2 106 ? 31.741  63.748 23.581  1.00 24.88 ? 269 ALA C O   1 
ATOM   5894 C  CB  . ALA C 2 106 ? 31.785  67.102 23.333  1.00 24.57 ? 269 ALA C CB  1 
ATOM   5895 N  N   . ALA C 2 107 ? 32.930  64.838 25.155  1.00 25.36 ? 270 ALA C N   1 
ATOM   5896 C  CA  . ALA C 2 107 ? 33.855  63.732 25.439  1.00 25.93 ? 270 ALA C CA  1 
ATOM   5897 C  C   . ALA C 2 107 ? 33.140  62.445 25.833  1.00 26.24 ? 270 ALA C C   1 
ATOM   5898 O  O   . ALA C 2 107 ? 33.390  61.389 25.249  1.00 26.46 ? 270 ALA C O   1 
ATOM   5899 C  CB  . ALA C 2 107 ? 34.857  64.130 26.531  1.00 25.81 ? 270 ALA C CB  1 
ATOM   5900 N  N   . LYS C 2 108 ? 32.258  62.549 26.824  1.00 26.59 ? 271 LYS C N   1 
ATOM   5901 C  CA  . LYS C 2 108 ? 31.462  61.431 27.303  1.00 26.95 ? 271 LYS C CA  1 
ATOM   5902 C  C   . LYS C 2 108 ? 30.623  60.835 26.174  1.00 27.40 ? 271 LYS C C   1 
ATOM   5903 O  O   . LYS C 2 108 ? 30.482  59.607 26.082  1.00 27.25 ? 271 LYS C O   1 
ATOM   5904 C  CB  . LYS C 2 108 ? 30.544  61.879 28.442  1.00 26.93 ? 271 LYS C CB  1 
ATOM   5905 C  CG  . LYS C 2 108 ? 31.246  62.511 29.627  1.00 26.98 ? 271 LYS C CG  1 
ATOM   5906 C  CD  . LYS C 2 108 ? 31.606  61.514 30.703  1.00 27.79 ? 271 LYS C CD  1 
ATOM   5907 C  CE  . LYS C 2 108 ? 32.530  62.164 31.721  1.00 28.98 ? 271 LYS C CE  1 
ATOM   5908 N  NZ  . LYS C 2 108 ? 32.665  61.374 32.970  1.00 29.61 ? 271 LYS C NZ  1 
ATOM   5909 N  N   . LYS C 2 109 ? 30.074  61.707 25.324  1.00 27.80 ? 272 LYS C N   1 
ATOM   5910 C  CA  . LYS C 2 109 ? 29.257  61.284 24.190  1.00 28.33 ? 272 LYS C CA  1 
ATOM   5911 C  C   . LYS C 2 109 ? 30.056  60.489 23.167  1.00 28.97 ? 272 LYS C C   1 
ATOM   5912 O  O   . LYS C 2 109 ? 29.569  59.486 22.648  1.00 29.08 ? 272 LYS C O   1 
ATOM   5913 C  CB  . LYS C 2 109 ? 28.584  62.475 23.521  1.00 28.16 ? 272 LYS C CB  1 
ATOM   5914 C  CG  . LYS C 2 109 ? 27.230  62.812 24.095  1.00 28.32 ? 272 LYS C CG  1 
ATOM   5915 C  CD  . LYS C 2 109 ? 26.618  63.989 23.359  1.00 28.26 ? 272 LYS C CD  1 
ATOM   5916 C  CE  . LYS C 2 109 ? 25.176  64.218 23.774  1.00 28.67 ? 272 LYS C CE  1 
ATOM   5917 N  NZ  . LYS C 2 109 ? 24.686  65.550 23.327  1.00 28.83 ? 272 LYS C NZ  1 
ATOM   5918 N  N   . ALA C 2 110 ? 31.277  60.937 22.879  1.00 29.78 ? 273 ALA C N   1 
ATOM   5919 C  CA  . ALA C 2 110 ? 32.182  60.186 22.012  1.00 30.67 ? 273 ALA C CA  1 
ATOM   5920 C  C   . ALA C 2 110 ? 32.526  58.838 22.651  1.00 31.39 ? 273 ALA C C   1 
ATOM   5921 O  O   . ALA C 2 110 ? 32.626  57.830 21.960  1.00 31.57 ? 273 ALA C O   1 
ATOM   5922 C  CB  . ALA C 2 110 ? 33.442  60.984 21.726  1.00 30.43 ? 273 ALA C CB  1 
ATOM   5923 N  N   . GLU C 2 111 ? 32.693  58.833 23.972  1.00 32.29 ? 274 GLU C N   1 
ATOM   5924 C  CA  . GLU C 2 111 ? 32.942  57.611 24.731  1.00 33.40 ? 274 GLU C CA  1 
ATOM   5925 C  C   . GLU C 2 111 ? 31.733  56.666 24.685  1.00 33.76 ? 274 GLU C C   1 
ATOM   5926 O  O   . GLU C 2 111 ? 31.876  55.467 24.443  1.00 33.73 ? 274 GLU C O   1 
ATOM   5927 C  CB  . GLU C 2 111 ? 33.313  57.952 26.178  1.00 33.24 ? 274 GLU C CB  1 
ATOM   5928 C  CG  . GLU C 2 111 ? 33.995  56.811 26.931  1.00 34.15 ? 274 GLU C CG  1 
ATOM   5929 C  CD  . GLU C 2 111 ? 34.518  57.211 28.313  1.00 34.54 ? 274 GLU C CD  1 
ATOM   5930 O  OE1 . GLU C 2 111 ? 34.765  58.418 28.567  1.00 34.80 ? 274 GLU C OE1 1 
ATOM   5931 O  OE2 . GLU C 2 111 ? 34.689  56.293 29.148  1.00 36.42 ? 274 GLU C OE2 1 
ATOM   5932 N  N   . LEU C 2 112 ? 30.546  57.216 24.916  1.00 34.43 ? 275 LEU C N   1 
ATOM   5933 C  CA  . LEU C 2 112 ? 29.317  56.460 24.773  1.00 35.12 ? 275 LEU C CA  1 
ATOM   5934 C  C   . LEU C 2 112 ? 29.240  55.810 23.394  1.00 35.96 ? 275 LEU C C   1 
ATOM   5935 O  O   . LEU C 2 112 ? 28.941  54.626 23.282  1.00 36.27 ? 275 LEU C O   1 
ATOM   5936 C  CB  . LEU C 2 112 ? 28.105  57.360 25.017  1.00 34.96 ? 275 LEU C CB  1 
ATOM   5937 C  CG  . LEU C 2 112 ? 26.723  56.705 25.000  1.00 34.79 ? 275 LEU C CG  1 
ATOM   5938 C  CD1 . LEU C 2 112 ? 26.682  55.452 25.869  1.00 34.41 ? 275 LEU C CD1 1 
ATOM   5939 C  CD2 . LEU C 2 112 ? 25.653  57.699 25.431  1.00 34.84 ? 275 LEU C CD2 1 
ATOM   5940 N  N   . GLU C 2 113 ? 29.535  56.585 22.355  1.00 36.79 ? 276 GLU C N   1 
ATOM   5941 C  CA  . GLU C 2 113 ? 29.484  56.109 20.976  1.00 37.56 ? 276 GLU C CA  1 
ATOM   5942 C  C   . GLU C 2 113 ? 30.499  54.979 20.694  1.00 37.79 ? 276 GLU C C   1 
ATOM   5943 O  O   . GLU C 2 113 ? 30.230  54.105 19.869  1.00 37.96 ? 276 GLU C O   1 
ATOM   5944 C  CB  . GLU C 2 113 ? 29.634  57.302 20.020  1.00 37.72 ? 276 GLU C CB  1 
ATOM   5945 C  CG  . GLU C 2 113 ? 29.430  57.013 18.529  1.00 39.63 ? 276 GLU C CG  1 
ATOM   5946 C  CD  . GLU C 2 113 ? 30.753  56.938 17.747  1.00 42.03 ? 276 GLU C CD  1 
ATOM   5947 O  OE1 . GLU C 2 113 ? 31.663  57.760 18.032  1.00 42.97 ? 276 GLU C OE1 1 
ATOM   5948 O  OE2 . GLU C 2 113 ? 30.882  56.066 16.847  1.00 42.17 ? 276 GLU C OE2 1 
ATOM   5949 N  N   . LYS C 2 114 ? 31.640  54.984 21.388  1.00 38.23 ? 277 LYS C N   1 
ATOM   5950 C  CA  . LYS C 2 114 ? 32.631  53.900 21.277  1.00 38.75 ? 277 LYS C CA  1 
ATOM   5951 C  C   . LYS C 2 114 ? 32.263  52.653 22.074  1.00 39.03 ? 277 LYS C C   1 
ATOM   5952 O  O   . LYS C 2 114 ? 32.527  51.534 21.639  1.00 39.02 ? 277 LYS C O   1 
ATOM   5953 C  CB  . LYS C 2 114 ? 34.017  54.365 21.711  1.00 38.71 ? 277 LYS C CB  1 
ATOM   5954 C  CG  . LYS C 2 114 ? 34.959  54.634 20.559  1.00 40.18 ? 277 LYS C CG  1 
ATOM   5955 C  CD  . LYS C 2 114 ? 36.305  55.183 21.047  1.00 41.76 ? 277 LYS C CD  1 
ATOM   5956 C  CE  . LYS C 2 114 ? 36.830  56.305 20.135  1.00 42.15 ? 277 LYS C CE  1 
ATOM   5957 N  NZ  . LYS C 2 114 ? 36.061  57.584 20.329  1.00 41.96 ? 277 LYS C NZ  1 
ATOM   5958 N  N   . THR C 2 115 ? 31.668  52.852 23.247  1.00 39.37 ? 278 THR C N   1 
ATOM   5959 C  CA  . THR C 2 115 ? 31.330  51.751 24.136  1.00 39.57 ? 278 THR C CA  1 
ATOM   5960 C  C   . THR C 2 115 ? 30.180  50.938 23.576  1.00 40.00 ? 278 THR C C   1 
ATOM   5961 O  O   . THR C 2 115 ? 30.151  49.722 23.736  1.00 39.92 ? 278 THR C O   1 
ATOM   5962 C  CB  . THR C 2 115 ? 30.991  52.258 25.537  1.00 39.39 ? 278 THR C CB  1 
ATOM   5963 O  OG1 . THR C 2 115 ? 32.023  53.145 25.966  1.00 39.55 ? 278 THR C OG1 1 
ATOM   5964 C  CG2 . THR C 2 115 ? 30.905  51.114 26.522  1.00 39.43 ? 278 THR C CG2 1 
ATOM   5965 N  N   . GLU C 2 116 ? 29.242  51.610 22.912  1.00 40.75 ? 279 GLU C N   1 
ATOM   5966 C  CA  . GLU C 2 116 ? 28.112  50.933 22.270  1.00 41.62 ? 279 GLU C CA  1 
ATOM   5967 C  C   . GLU C 2 116 ? 28.564  50.112 21.061  1.00 41.79 ? 279 GLU C C   1 
ATOM   5968 O  O   . GLU C 2 116 ? 28.045  49.020 20.821  1.00 41.96 ? 279 GLU C O   1 
ATOM   5969 C  CB  . GLU C 2 116 ? 26.993  51.919 21.894  1.00 41.50 ? 279 GLU C CB  1 
ATOM   5970 C  CG  . GLU C 2 116 ? 26.078  52.290 23.069  1.00 42.23 ? 279 GLU C CG  1 
ATOM   5971 C  CD  . GLU C 2 116 ? 24.804  53.025 22.646  1.00 42.54 ? 279 GLU C CD  1 
ATOM   5972 O  OE1 . GLU C 2 116 ? 24.833  54.272 22.520  1.00 43.10 ? 279 GLU C OE1 1 
ATOM   5973 O  OE2 . GLU C 2 116 ? 23.762  52.354 22.470  1.00 44.11 ? 279 GLU C OE2 1 
ATOM   5974 N  N   . ALA C 2 117 ? 29.537  50.638 20.319  1.00 42.12 ? 280 ALA C N   1 
ATOM   5975 C  CA  . ALA C 2 117 ? 30.156  49.912 19.213  1.00 42.47 ? 280 ALA C CA  1 
ATOM   5976 C  C   . ALA C 2 117 ? 30.995  48.740 19.725  1.00 42.75 ? 280 ALA C C   1 
ATOM   5977 O  O   . ALA C 2 117 ? 30.974  47.658 19.138  1.00 42.72 ? 280 ALA C O   1 
ATOM   5978 C  CB  . ALA C 2 117 ? 31.000  50.851 18.371  1.00 42.59 ? 280 ALA C CB  1 
ATOM   5979 N  N   . ASP C 2 118 ? 31.724  48.968 20.819  1.00 43.26 ? 281 ASP C N   1 
ATOM   5980 C  CA  . ASP C 2 118 ? 32.449  47.916 21.542  1.00 43.89 ? 281 ASP C CA  1 
ATOM   5981 C  C   . ASP C 2 118 ? 31.540  46.756 21.928  1.00 44.30 ? 281 ASP C C   1 
ATOM   5982 O  O   . ASP C 2 118 ? 31.989  45.608 21.999  1.00 44.35 ? 281 ASP C O   1 
ATOM   5983 C  CB  . ASP C 2 118 ? 33.081  48.476 22.823  1.00 44.02 ? 281 ASP C CB  1 
ATOM   5984 C  CG  . ASP C 2 118 ? 34.530  48.921 22.637  1.00 44.35 ? 281 ASP C CG  1 
ATOM   5985 O  OD1 . ASP C 2 118 ? 35.226  49.094 23.664  1.00 44.35 ? 281 ASP C OD1 1 
ATOM   5986 O  OD2 . ASP C 2 118 ? 34.975  49.101 21.482  1.00 44.69 ? 281 ASP C OD2 1 
ATOM   5987 N  N   . LEU C 2 119 ? 30.271  47.077 22.189  1.00 44.79 ? 282 LEU C N   1 
ATOM   5988 C  CA  . LEU C 2 119 ? 29.257  46.106 22.596  1.00 45.19 ? 282 LEU C CA  1 
ATOM   5989 C  C   . LEU C 2 119 ? 28.685  45.347 21.399  1.00 45.97 ? 282 LEU C C   1 
ATOM   5990 O  O   . LEU C 2 119 ? 28.666  44.115 21.401  1.00 46.16 ? 282 LEU C O   1 
ATOM   5991 C  CB  . LEU C 2 119 ? 28.140  46.806 23.381  1.00 45.06 ? 282 LEU C CB  1 
ATOM   5992 C  CG  . LEU C 2 119 ? 26.873  46.054 23.799  1.00 44.57 ? 282 LEU C CG  1 
ATOM   5993 C  CD1 . LEU C 2 119 ? 27.158  45.043 24.885  1.00 44.41 ? 282 LEU C CD1 1 
ATOM   5994 C  CD2 . LEU C 2 119 ? 25.825  47.039 24.264  1.00 44.58 ? 282 LEU C CD2 1 
ATOM   5995 N  N   . LYS C 2 120 ? 28.230  46.080 20.381  1.00 46.71 ? 283 LYS C N   1 
ATOM   5996 C  CA  . LYS C 2 120 ? 27.661  45.472 19.171  1.00 47.51 ? 283 LYS C CA  1 
ATOM   5997 C  C   . LYS C 2 120 ? 28.621  44.452 18.574  1.00 48.03 ? 283 LYS C C   1 
ATOM   5998 O  O   . LYS C 2 120 ? 28.198  43.424 18.041  1.00 47.96 ? 283 LYS C O   1 
ATOM   5999 C  CB  . LYS C 2 120 ? 27.323  46.542 18.131  1.00 47.39 ? 283 LYS C CB  1 
ATOM   6000 C  CG  . LYS C 2 120 ? 26.151  46.179 17.214  1.00 47.65 ? 283 LYS C CG  1 
ATOM   6001 C  CD  . LYS C 2 120 ? 25.668  47.370 16.359  1.00 47.67 ? 283 LYS C CD  1 
ATOM   6002 C  CE  . LYS C 2 120 ? 25.215  48.581 17.200  1.00 47.68 ? 283 LYS C CE  1 
ATOM   6003 N  NZ  . LYS C 2 120 ? 24.278  48.230 18.315  1.00 47.07 ? 283 LYS C NZ  1 
ATOM   6004 N  N   . LYS C 2 121 ? 29.913  44.747 18.688  1.00 48.86 ? 284 LYS C N   1 
ATOM   6005 C  CA  . LYS C 2 121 ? 30.967  43.867 18.213  1.00 49.76 ? 284 LYS C CA  1 
ATOM   6006 C  C   . LYS C 2 121 ? 31.164  42.664 19.137  1.00 50.16 ? 284 LYS C C   1 
ATOM   6007 O  O   . LYS C 2 121 ? 31.220  41.527 18.672  1.00 50.32 ? 284 LYS C O   1 
ATOM   6008 C  CB  . LYS C 2 121 ? 32.279  44.642 18.047  1.00 49.81 ? 284 LYS C CB  1 
ATOM   6009 C  CG  . LYS C 2 121 ? 33.296  43.921 17.180  1.00 50.63 ? 284 LYS C CG  1 
ATOM   6010 C  CD  . LYS C 2 121 ? 34.654  44.589 17.217  1.00 51.76 ? 284 LYS C CD  1 
ATOM   6011 C  CE  . LYS C 2 121 ? 35.661  43.800 16.387  1.00 52.09 ? 284 LYS C CE  1 
ATOM   6012 N  NZ  . LYS C 2 121 ? 37.051  44.313 16.554  1.00 52.21 ? 284 LYS C NZ  1 
ATOM   6013 N  N   . ALA C 2 122 ? 31.260  42.916 20.441  1.00 50.77 ? 285 ALA C N   1 
ATOM   6014 C  CA  . ALA C 2 122 ? 31.509  41.852 21.420  1.00 51.44 ? 285 ALA C CA  1 
ATOM   6015 C  C   . ALA C 2 122 ? 30.377  40.839 21.449  1.00 51.93 ? 285 ALA C C   1 
ATOM   6016 O  O   . ALA C 2 122 ? 30.562  39.686 21.844  1.00 51.94 ? 285 ALA C O   1 
ATOM   6017 C  CB  . ALA C 2 122 ? 31.710  42.444 22.805  1.00 51.32 ? 285 ALA C CB  1 
ATOM   6018 N  N   . VAL C 2 123 ? 29.205  41.285 21.012  1.00 52.64 ? 286 VAL C N   1 
ATOM   6019 C  CA  . VAL C 2 123 ? 27.989  40.500 21.113  1.00 53.33 ? 286 VAL C CA  1 
ATOM   6020 C  C   . VAL C 2 123 ? 27.938  39.385 20.043  1.00 53.92 ? 286 VAL C C   1 
ATOM   6021 O  O   . VAL C 2 123 ? 27.036  38.539 20.052  1.00 54.04 ? 286 VAL C O   1 
ATOM   6022 C  CB  . VAL C 2 123 ? 26.729  41.430 21.165  1.00 53.17 ? 286 VAL C CB  1 
ATOM   6023 C  CG1 . VAL C 2 123 ? 26.062  41.590 19.794  1.00 53.43 ? 286 VAL C CG1 1 
ATOM   6024 C  CG2 . VAL C 2 123 ? 25.753  40.932 22.198  1.00 52.80 ? 286 VAL C CG2 1 
ATOM   6025 N  N   . ASN C 2 124 ? 28.915  39.395 19.135  1.00 54.62 ? 287 ASN C N   1 
ATOM   6026 C  CA  . ASN C 2 124 ? 29.221  38.230 18.294  1.00 55.39 ? 287 ASN C CA  1 
ATOM   6027 C  C   . ASN C 2 124 ? 30.659  37.809 18.583  1.00 55.99 ? 287 ASN C C   1 
ATOM   6028 O  O   . ASN C 2 124 ? 31.593  38.292 17.930  1.00 56.05 ? 287 ASN C O   1 
ATOM   6029 C  CB  . ASN C 2 124 ? 29.069  38.531 16.795  1.00 55.29 ? 287 ASN C CB  1 
ATOM   6030 C  CG  . ASN C 2 124 ? 27.940  39.502 16.487  1.00 55.32 ? 287 ASN C CG  1 
ATOM   6031 O  OD1 . ASN C 2 124 ? 28.089  40.377 15.637  1.00 55.28 ? 287 ASN C OD1 1 
ATOM   6032 N  ND2 . ASN C 2 124 ? 26.807  39.347 17.161  1.00 55.16 ? 287 ASN C ND2 1 
ATOM   6033 N  N   . GLU C 2 125 ? 30.838  36.934 19.576  1.00 56.67 ? 288 GLU C N   1 
ATOM   6034 C  CA  . GLU C 2 125 ? 32.180  36.522 20.025  1.00 57.23 ? 288 GLU C CA  1 
ATOM   6035 C  C   . GLU C 2 125 ? 32.236  35.101 20.601  1.00 57.28 ? 288 GLU C C   1 
ATOM   6036 O  O   . GLU C 2 125 ? 33.002  34.262 20.122  1.00 57.31 ? 288 GLU C O   1 
ATOM   6037 C  CB  . GLU C 2 125 ? 32.750  37.528 21.043  1.00 57.45 ? 288 GLU C CB  1 
ATOM   6038 C  CG  . GLU C 2 125 ? 34.220  37.299 21.410  1.00 58.28 ? 288 GLU C CG  1 
ATOM   6039 C  CD  . GLU C 2 125 ? 35.148  37.397 20.204  1.00 59.14 ? 288 GLU C CD  1 
ATOM   6040 O  OE1 . GLU C 2 125 ? 35.623  36.338 19.729  1.00 59.23 ? 288 GLU C OE1 1 
ATOM   6041 O  OE2 . GLU C 2 125 ? 35.387  38.530 19.727  1.00 59.30 ? 288 GLU C OE2 1 
ATOM   6042 O  OXT . GLU C 2 125 ? 31.539  34.761 21.562  1.00 57.33 ? 288 GLU C OXT 1 
ATOM   6043 N  N   . GLY D 2 1   ? -5.959  46.543 53.596  1.00 7.18  ? 164 GLY D N   1 
ATOM   6044 C  CA  . GLY D 2 1   ? -6.059  45.517 54.670  1.00 11.20 ? 164 GLY D CA  1 
ATOM   6045 C  C   . GLY D 2 1   ? -6.641  44.328 53.948  1.00 12.12 ? 164 GLY D C   1 
ATOM   6046 O  O   . GLY D 2 1   ? -6.755  44.467 52.736  1.00 12.75 ? 164 GLY D O   1 
ATOM   6047 N  N   . SER D 2 2   ? -7.022  43.207 54.638  1.00 12.49 ? 165 SER D N   1 
ATOM   6048 C  CA  . SER D 2 2   ? -7.571  41.946 53.980  1.00 12.93 ? 165 SER D CA  1 
ATOM   6049 C  C   . SER D 2 2   ? -8.462  40.928 54.783  1.00 13.70 ? 165 SER D C   1 
ATOM   6050 O  O   . SER D 2 2   ? -8.253  40.733 55.986  1.00 14.03 ? 165 SER D O   1 
ATOM   6051 C  CB  . SER D 2 2   ? -6.425  41.132 53.366  1.00 12.89 ? 165 SER D CB  1 
ATOM   6052 O  OG  . SER D 2 2   ? -6.104  39.994 54.170  1.00 11.84 ? 165 SER D OG  1 
ATOM   6053 N  N   . HIS D 2 3   ? -9.388  40.225 54.098  1.00 14.20 ? 166 HIS D N   1 
ATOM   6054 C  CA  . HIS D 2 3   ? -10.279 39.202 54.740  1.00 14.73 ? 166 HIS D CA  1 
ATOM   6055 C  C   . HIS D 2 3   ? -10.888 38.087 53.833  1.00 15.95 ? 166 HIS D C   1 
ATOM   6056 O  O   . HIS D 2 3   ? -11.005 38.263 52.623  1.00 15.75 ? 166 HIS D O   1 
ATOM   6057 C  CB  . HIS D 2 3   ? -11.424 39.889 55.496  1.00 14.78 ? 166 HIS D CB  1 
ATOM   6058 C  CG  . HIS D 2 3   ? -12.458 40.512 54.602  1.00 14.81 ? 166 HIS D CG  1 
ATOM   6059 N  ND1 . HIS D 2 3   ? -12.474 41.860 54.307  1.00 14.00 ? 166 HIS D ND1 1 
ATOM   6060 C  CD2 . HIS D 2 3   ? -13.511 39.969 53.939  1.00 14.57 ? 166 HIS D CD2 1 
ATOM   6061 C  CE1 . HIS D 2 3   ? -13.486 42.119 53.496  1.00 14.38 ? 166 HIS D CE1 1 
ATOM   6062 N  NE2 . HIS D 2 3   ? -14.130 40.990 53.256  1.00 14.54 ? 166 HIS D NE2 1 
ATOM   6063 N  N   . MET D 2 4   ? -11.295 36.960 54.442  1.00 17.43 ? 167 MET D N   1 
ATOM   6064 C  CA  . MET D 2 4   ? -12.018 35.852 53.756  1.00 18.84 ? 167 MET D CA  1 
ATOM   6065 C  C   . MET D 2 4   ? -13.463 35.746 54.243  1.00 19.82 ? 167 MET D C   1 
ATOM   6066 O  O   . MET D 2 4   ? -13.688 35.415 55.405  1.00 20.25 ? 167 MET D O   1 
ATOM   6067 C  CB  . MET D 2 4   ? -11.352 34.509 54.035  1.00 18.55 ? 167 MET D CB  1 
ATOM   6068 C  CG  . MET D 2 4   ? -9.942  34.359 53.500  1.00 20.24 ? 167 MET D CG  1 
ATOM   6069 S  SD  . MET D 2 4   ? -9.750  33.357 51.999  1.00 22.43 ? 167 MET D SD  1 
ATOM   6070 C  CE  . MET D 2 4   ? -10.408 31.760 52.497  1.00 20.48 ? 167 MET D CE  1 
ATOM   6071 N  N   . ASP D 2 5   ? -14.434 35.988 53.360  1.00 21.01 ? 168 ASP D N   1 
ATOM   6072 C  CA  . ASP D 2 5   ? -15.840 36.146 53.765  1.00 22.17 ? 168 ASP D CA  1 
ATOM   6073 C  C   . ASP D 2 5   ? -16.540 34.919 54.337  1.00 23.15 ? 168 ASP D C   1 
ATOM   6074 O  O   . ASP D 2 5   ? -17.369 35.055 55.225  1.00 23.24 ? 168 ASP D O   1 
ATOM   6075 C  CB  . ASP D 2 5   ? -16.682 36.742 52.639  1.00 22.11 ? 168 ASP D CB  1 
ATOM   6076 C  CG  . ASP D 2 5   ? -16.362 38.197 52.391  1.00 22.96 ? 168 ASP D CG  1 
ATOM   6077 O  OD1 . ASP D 2 5   ? -17.121 39.076 52.853  1.00 23.38 ? 168 ASP D OD1 1 
ATOM   6078 O  OD2 . ASP D 2 5   ? -15.330 38.475 51.751  1.00 24.81 ? 168 ASP D OD2 1 
ATOM   6079 N  N   . ALA D 2 6   ? -16.226 33.728 53.836  1.00 24.70 ? 169 ALA D N   1 
ATOM   6080 C  CA  . ALA D 2 6   ? -16.793 32.492 54.404  1.00 26.14 ? 169 ALA D CA  1 
ATOM   6081 C  C   . ALA D 2 6   ? -16.533 32.353 55.920  1.00 27.35 ? 169 ALA D C   1 
ATOM   6082 O  O   . ALA D 2 6   ? -17.399 31.876 56.665  1.00 27.42 ? 169 ALA D O   1 
ATOM   6083 C  CB  . ALA D 2 6   ? -16.275 31.276 53.658  1.00 25.94 ? 169 ALA D CB  1 
ATOM   6084 N  N   . GLU D 2 7   ? -15.342 32.775 56.357  1.00 28.79 ? 170 GLU D N   1 
ATOM   6085 C  CA  . GLU D 2 7   ? -14.963 32.801 57.778  1.00 30.07 ? 170 GLU D CA  1 
ATOM   6086 C  C   . GLU D 2 7   ? -15.760 33.785 58.607  1.00 30.41 ? 170 GLU D C   1 
ATOM   6087 O  O   . GLU D 2 7   ? -16.123 33.482 59.742  1.00 31.06 ? 170 GLU D O   1 
ATOM   6088 C  CB  . GLU D 2 7   ? -13.500 33.157 57.935  1.00 30.17 ? 170 GLU D CB  1 
ATOM   6089 C  CG  . GLU D 2 7   ? -12.622 31.979 58.181  1.00 32.80 ? 170 GLU D CG  1 
ATOM   6090 C  CD  . GLU D 2 7   ? -11.168 32.334 57.998  1.00 36.96 ? 170 GLU D CD  1 
ATOM   6091 O  OE1 . GLU D 2 7   ? -10.738 33.384 58.550  1.00 38.05 ? 170 GLU D OE1 1 
ATOM   6092 O  OE2 . GLU D 2 7   ? -10.463 31.571 57.289  1.00 39.00 ? 170 GLU D OE2 1 
ATOM   6093 N  N   . GLU D 2 8   ? -16.010 34.965 58.044  1.00 30.51 ? 171 GLU D N   1 
ATOM   6094 C  CA  . GLU D 2 8   ? -16.719 36.032 58.739  1.00 30.51 ? 171 GLU D CA  1 
ATOM   6095 C  C   . GLU D 2 8   ? -18.242 35.845 58.716  1.00 30.25 ? 171 GLU D C   1 
ATOM   6096 O  O   . GLU D 2 8   ? -18.974 36.488 59.472  1.00 30.15 ? 171 GLU D O   1 
ATOM   6097 C  CB  . GLU D 2 8   ? -16.329 37.377 58.125  1.00 30.78 ? 171 GLU D CB  1 
ATOM   6098 C  CG  . GLU D 2 8   ? -14.840 37.722 58.226  1.00 32.14 ? 171 GLU D CG  1 
ATOM   6099 C  CD  . GLU D 2 8   ? -14.379 38.079 59.653  1.00 35.38 ? 171 GLU D CD  1 
ATOM   6100 O  OE1 . GLU D 2 8   ? -15.167 37.941 60.633  1.00 35.85 ? 171 GLU D OE1 1 
ATOM   6101 O  OE2 . GLU D 2 8   ? -13.205 38.503 59.792  1.00 36.55 ? 171 GLU D OE2 1 
ATOM   6102 N  N   . VAL D 2 9   ? -18.704 34.950 57.852  1.00 30.22 ? 172 VAL D N   1 
ATOM   6103 C  CA  . VAL D 2 9   ? -20.129 34.724 57.630  1.00 30.28 ? 172 VAL D CA  1 
ATOM   6104 C  C   . VAL D 2 9   ? -20.639 33.465 58.339  1.00 30.47 ? 172 VAL D C   1 
ATOM   6105 O  O   . VAL D 2 9   ? -21.848 33.211 58.362  1.00 30.76 ? 172 VAL D O   1 
ATOM   6106 C  CB  . VAL D 2 9   ? -20.455 34.713 56.104  1.00 30.10 ? 172 VAL D CB  1 
ATOM   6107 C  CG1 . VAL D 2 9   ? -21.648 33.824 55.772  1.00 30.33 ? 172 VAL D CG1 1 
ATOM   6108 C  CG2 . VAL D 2 9   ? -20.687 36.127 55.616  1.00 29.72 ? 172 VAL D CG2 1 
ATOM   6109 N  N   . ALA D 2 10  ? -19.720 32.691 58.919  1.00 30.53 ? 173 ALA D N   1 
ATOM   6110 C  CA  . ALA D 2 10  ? -20.077 31.516 59.717  1.00 30.45 ? 173 ALA D CA  1 
ATOM   6111 C  C   . ALA D 2 10  ? -20.829 31.957 60.966  1.00 30.57 ? 173 ALA D C   1 
ATOM   6112 O  O   . ALA D 2 10  ? -20.531 33.012 61.536  1.00 30.44 ? 173 ALA D O   1 
ATOM   6113 C  CB  . ALA D 2 10  ? -18.838 30.715 60.101  1.00 30.31 ? 173 ALA D CB  1 
ATOM   6114 N  N   . PRO D 2 11  ? -21.806 31.146 61.402  1.00 30.70 ? 174 PRO D N   1 
ATOM   6115 C  CA  . PRO D 2 11  ? -22.614 31.508 62.559  1.00 30.61 ? 174 PRO D CA  1 
ATOM   6116 C  C   . PRO D 2 11  ? -21.769 31.852 63.796  1.00 30.68 ? 174 PRO D C   1 
ATOM   6117 O  O   . PRO D 2 11  ? -22.051 32.839 64.483  1.00 30.68 ? 174 PRO D O   1 
ATOM   6118 C  CB  . PRO D 2 11  ? -23.447 30.248 62.801  1.00 30.60 ? 174 PRO D CB  1 
ATOM   6119 C  CG  . PRO D 2 11  ? -23.525 29.591 61.471  1.00 30.64 ? 174 PRO D CG  1 
ATOM   6120 C  CD  . PRO D 2 11  ? -22.198 29.837 60.844  1.00 30.64 ? 174 PRO D CD  1 
ATOM   6121 N  N   . GLN D 2 12  ? -20.735 31.060 64.067  1.00 30.66 ? 175 GLN D N   1 
ATOM   6122 C  CA  . GLN D 2 12  ? -19.882 31.301 65.226  1.00 30.87 ? 175 GLN D CA  1 
ATOM   6123 C  C   . GLN D 2 12  ? -19.396 32.752 65.257  1.00 30.31 ? 175 GLN D C   1 
ATOM   6124 O  O   . GLN D 2 12  ? -19.416 33.388 66.313  1.00 30.22 ? 175 GLN D O   1 
ATOM   6125 C  CB  . GLN D 2 12  ? -18.702 30.324 65.251  1.00 30.80 ? 175 GLN D CB  1 
ATOM   6126 C  CG  . GLN D 2 12  ? -17.637 30.572 64.174  1.00 31.94 ? 175 GLN D CG  1 
ATOM   6127 C  CD  . GLN D 2 12  ? -16.590 29.460 64.079  1.00 32.21 ? 175 GLN D CD  1 
ATOM   6128 O  OE1 . GLN D 2 12  ? -16.057 29.185 62.993  1.00 34.05 ? 175 GLN D OE1 1 
ATOM   6129 N  NE2 . GLN D 2 12  ? -16.288 28.820 65.210  1.00 32.62 ? 175 GLN D NE2 1 
ATOM   6130 N  N   . ALA D 2 13  ? -19.008 33.262 64.086  1.00 29.83 ? 176 ALA D N   1 
ATOM   6131 C  CA  . ALA D 2 13  ? -18.445 34.603 63.928  1.00 29.46 ? 176 ALA D CA  1 
ATOM   6132 C  C   . ALA D 2 13  ? -19.486 35.712 63.999  1.00 29.50 ? 176 ALA D C   1 
ATOM   6133 O  O   . ALA D 2 13  ? -19.249 36.739 64.634  1.00 29.57 ? 176 ALA D O   1 
ATOM   6134 C  CB  . ALA D 2 13  ? -17.666 34.703 62.632  1.00 29.23 ? 176 ALA D CB  1 
ATOM   6135 N  N   . LYS D 2 14  ? -20.627 35.521 63.342  1.00 29.50 ? 177 LYS D N   1 
ATOM   6136 C  CA  . LYS D 2 14  ? -21.694 36.521 63.387  1.00 29.71 ? 177 LYS D CA  1 
ATOM   6137 C  C   . LYS D 2 14  ? -22.259 36.643 64.804  1.00 29.48 ? 177 LYS D C   1 
ATOM   6138 O  O   . LYS D 2 14  ? -22.648 37.725 65.232  1.00 29.64 ? 177 LYS D O   1 
ATOM   6139 C  CB  . LYS D 2 14  ? -22.801 36.216 62.375  1.00 29.73 ? 177 LYS D CB  1 
ATOM   6140 C  CG  . LYS D 2 14  ? -22.395 36.390 60.906  1.00 31.82 ? 177 LYS D CG  1 
ATOM   6141 C  CD  . LYS D 2 14  ? -22.964 37.662 60.241  1.00 35.90 ? 177 LYS D CD  1 
ATOM   6142 C  CE  . LYS D 2 14  ? -22.316 38.982 60.754  1.00 38.94 ? 177 LYS D CE  1 
ATOM   6143 N  NZ  . LYS D 2 14  ? -20.802 39.008 60.758  1.00 40.33 ? 177 LYS D NZ  1 
ATOM   6144 N  N   . ILE D 2 15  ? -22.288 35.538 65.539  1.00 29.24 ? 178 ILE D N   1 
ATOM   6145 C  CA  . ILE D 2 15  ? -22.738 35.580 66.921  1.00 28.89 ? 178 ILE D CA  1 
ATOM   6146 C  C   . ILE D 2 15  ? -21.771 36.439 67.730  1.00 28.92 ? 178 ILE D C   1 
ATOM   6147 O  O   . ILE D 2 15  ? -22.195 37.328 68.457  1.00 28.99 ? 178 ILE D O   1 
ATOM   6148 C  CB  . ILE D 2 15  ? -22.907 34.157 67.529  1.00 29.01 ? 178 ILE D CB  1 
ATOM   6149 C  CG1 . ILE D 2 15  ? -24.109 33.447 66.893  1.00 28.80 ? 178 ILE D CG1 1 
ATOM   6150 C  CG2 . ILE D 2 15  ? -23.090 34.228 69.035  1.00 28.45 ? 178 ILE D CG2 1 
ATOM   6151 C  CD1 . ILE D 2 15  ? -24.136 31.944 67.086  1.00 28.45 ? 178 ILE D CD1 1 
ATOM   6152 N  N   . ALA D 2 16  ? -20.474 36.203 67.564  1.00 29.12 ? 179 ALA D N   1 
ATOM   6153 C  CA  . ALA D 2 16  ? -19.454 36.909 68.350  1.00 29.44 ? 179 ALA D CA  1 
ATOM   6154 C  C   . ALA D 2 16  ? -19.378 38.416 68.068  1.00 29.78 ? 179 ALA D C   1 
ATOM   6155 O  O   . ALA D 2 16  ? -19.129 39.202 68.983  1.00 29.58 ? 179 ALA D O   1 
ATOM   6156 C  CB  . ALA D 2 16  ? -18.084 36.251 68.179  1.00 29.09 ? 179 ALA D CB  1 
ATOM   6157 N  N   . GLU D 2 17  ? -19.592 38.811 66.812  1.00 30.30 ? 180 GLU D N   1 
ATOM   6158 C  CA  . GLU D 2 17  ? -19.585 40.225 66.446  1.00 30.98 ? 180 GLU D CA  1 
ATOM   6159 C  C   . GLU D 2 17  ? -20.862 40.915 66.934  1.00 30.98 ? 180 GLU D C   1 
ATOM   6160 O  O   . GLU D 2 17  ? -20.843 42.101 67.290  1.00 31.06 ? 180 GLU D O   1 
ATOM   6161 C  CB  . GLU D 2 17  ? -19.376 40.410 64.935  1.00 31.28 ? 180 GLU D CB  1 
ATOM   6162 C  CG  . GLU D 2 17  ? -19.391 41.872 64.414  1.00 33.71 ? 180 GLU D CG  1 
ATOM   6163 C  CD  . GLU D 2 17  ? -18.434 42.848 65.170  1.00 36.89 ? 180 GLU D CD  1 
ATOM   6164 O  OE1 . GLU D 2 17  ? -17.363 42.402 65.680  1.00 37.12 ? 180 GLU D OE1 1 
ATOM   6165 O  OE2 . GLU D 2 17  ? -18.761 44.070 65.235  1.00 36.17 ? 180 GLU D OE2 1 
ATOM   6166 N  N   . LEU D 2 18  ? -21.961 40.164 66.973  1.00 30.99 ? 181 LEU D N   1 
ATOM   6167 C  CA  . LEU D 2 18  ? -23.214 40.682 67.509  1.00 30.75 ? 181 LEU D CA  1 
ATOM   6168 C  C   . LEU D 2 18  ? -23.118 40.968 69.013  1.00 30.98 ? 181 LEU D C   1 
ATOM   6169 O  O   . LEU D 2 18  ? -23.611 42.002 69.476  1.00 31.06 ? 181 LEU D O   1 
ATOM   6170 C  CB  . LEU D 2 18  ? -24.382 39.746 67.196  1.00 30.37 ? 181 LEU D CB  1 
ATOM   6171 C  CG  . LEU D 2 18  ? -25.775 40.215 67.621  1.00 30.12 ? 181 LEU D CG  1 
ATOM   6172 C  CD1 . LEU D 2 18  ? -26.192 41.490 66.911  1.00 29.87 ? 181 LEU D CD1 1 
ATOM   6173 C  CD2 . LEU D 2 18  ? -26.781 39.142 67.363  1.00 30.30 ? 181 LEU D CD2 1 
ATOM   6174 N  N   . GLU D 2 19  ? -22.472 40.080 69.771  1.00 31.02 ? 182 GLU D N   1 
ATOM   6175 C  CA  . GLU D 2 19  ? -22.361 40.291 71.221  1.00 31.26 ? 182 GLU D CA  1 
ATOM   6176 C  C   . GLU D 2 19  ? -21.401 41.424 71.544  1.00 31.08 ? 182 GLU D C   1 
ATOM   6177 O  O   . GLU D 2 19  ? -21.532 42.073 72.580  1.00 31.03 ? 182 GLU D O   1 
ATOM   6178 C  CB  . GLU D 2 19  ? -22.012 38.991 71.977  1.00 31.41 ? 182 GLU D CB  1 
ATOM   6179 C  CG  . GLU D 2 19  ? -20.584 38.850 72.501  1.00 32.36 ? 182 GLU D CG  1 
ATOM   6180 C  CD  . GLU D 2 19  ? -20.320 39.631 73.793  1.00 34.27 ? 182 GLU D CD  1 
ATOM   6181 O  OE1 . GLU D 2 19  ? -21.056 39.447 74.791  1.00 33.97 ? 182 GLU D OE1 1 
ATOM   6182 O  OE2 . GLU D 2 19  ? -19.358 40.433 73.805  1.00 35.31 ? 182 GLU D OE2 1 
ATOM   6183 N  N   . ASN D 2 20  ? -20.444 41.648 70.647  1.00 31.18 ? 183 ASN D N   1 
ATOM   6184 C  CA  . ASN D 2 20  ? -19.527 42.774 70.739  1.00 31.24 ? 183 ASN D CA  1 
ATOM   6185 C  C   . ASN D 2 20  ? -20.262 44.061 70.411  1.00 31.24 ? 183 ASN D C   1 
ATOM   6186 O  O   . ASN D 2 20  ? -20.060 45.074 71.079  1.00 31.18 ? 183 ASN D O   1 
ATOM   6187 C  CB  . ASN D 2 20  ? -18.337 42.590 69.797  1.00 31.34 ? 183 ASN D CB  1 
ATOM   6188 C  CG  . ASN D 2 20  ? -17.249 43.633 70.015  1.00 32.05 ? 183 ASN D CG  1 
ATOM   6189 O  OD1 . ASN D 2 20  ? -17.050 44.521 69.188  1.00 32.97 ? 183 ASN D OD1 1 
ATOM   6190 N  ND2 . ASN D 2 20  ? -16.539 43.527 71.131  1.00 32.80 ? 183 ASN D ND2 1 
ATOM   6191 N  N   . GLN D 2 21  ? -21.118 44.014 69.389  1.00 31.27 ? 184 GLN D N   1 
ATOM   6192 C  CA  . GLN D 2 21  ? -21.979 45.148 69.052  1.00 31.53 ? 184 GLN D CA  1 
ATOM   6193 C  C   . GLN D 2 21  ? -22.852 45.557 70.246  1.00 31.71 ? 184 GLN D C   1 
ATOM   6194 O  O   . GLN D 2 21  ? -22.986 46.742 70.551  1.00 31.65 ? 184 GLN D O   1 
ATOM   6195 C  CB  . GLN D 2 21  ? -22.841 44.843 67.823  1.00 31.42 ? 184 GLN D CB  1 
ATOM   6196 C  CG  . GLN D 2 21  ? -22.135 45.030 66.476  1.00 31.67 ? 184 GLN D CG  1 
ATOM   6197 C  CD  . GLN D 2 21  ? -22.942 44.475 65.295  1.00 31.64 ? 184 GLN D CD  1 
ATOM   6198 O  OE1 . GLN D 2 21  ? -24.132 44.751 65.150  1.00 31.42 ? 184 GLN D OE1 1 
ATOM   6199 N  NE2 . GLN D 2 21  ? -22.285 43.692 64.449  1.00 32.26 ? 184 GLN D NE2 1 
ATOM   6200 N  N   . VAL D 2 22  ? -23.422 44.569 70.929  1.00 32.08 ? 185 VAL D N   1 
ATOM   6201 C  CA  . VAL D 2 22  ? -24.214 44.814 72.129  1.00 32.45 ? 185 VAL D CA  1 
ATOM   6202 C  C   . VAL D 2 22  ? -23.349 45.416 73.243  1.00 33.09 ? 185 VAL D C   1 
ATOM   6203 O  O   . VAL D 2 22  ? -23.781 46.333 73.936  1.00 33.30 ? 185 VAL D O   1 
ATOM   6204 C  CB  . VAL D 2 22  ? -24.927 43.528 72.602  1.00 32.22 ? 185 VAL D CB  1 
ATOM   6205 C  CG1 . VAL D 2 22  ? -25.654 43.758 73.909  1.00 31.95 ? 185 VAL D CG1 1 
ATOM   6206 C  CG2 . VAL D 2 22  ? -25.907 43.054 71.544  1.00 32.04 ? 185 VAL D CG2 1 
ATOM   6207 N  N   . HIS D 2 23  ? -22.127 44.912 73.396  1.00 33.82 ? 186 HIS D N   1 
ATOM   6208 C  CA  . HIS D 2 23  ? -21.199 45.437 74.384  1.00 34.51 ? 186 HIS D CA  1 
ATOM   6209 C  C   . HIS D 2 23  ? -20.862 46.890 74.089  1.00 35.45 ? 186 HIS D C   1 
ATOM   6210 O  O   . HIS D 2 23  ? -20.930 47.725 74.985  1.00 35.77 ? 186 HIS D O   1 
ATOM   6211 C  CB  . HIS D 2 23  ? -19.923 44.588 74.454  1.00 34.27 ? 186 HIS D CB  1 
ATOM   6212 C  CG  . HIS D 2 23  ? -18.818 45.215 75.253  1.00 33.36 ? 186 HIS D CG  1 
ATOM   6213 N  ND1 . HIS D 2 23  ? -18.920 45.454 76.608  1.00 31.99 ? 186 HIS D ND1 1 
ATOM   6214 C  CD2 . HIS D 2 23  ? -17.589 45.651 74.886  1.00 32.50 ? 186 HIS D CD2 1 
ATOM   6215 C  CE1 . HIS D 2 23  ? -17.802 46.011 77.040  1.00 32.08 ? 186 HIS D CE1 1 
ATOM   6216 N  NE2 . HIS D 2 23  ? -16.979 46.142 76.015  1.00 32.22 ? 186 HIS D NE2 1 
ATOM   6217 N  N   . ARG D 2 24  ? -20.509 47.184 72.839  1.00 36.58 ? 187 ARG D N   1 
ATOM   6218 C  CA  . ARG D 2 24  ? -20.149 48.544 72.425  1.00 37.98 ? 187 ARG D CA  1 
ATOM   6219 C  C   . ARG D 2 24  ? -21.311 49.520 72.587  1.00 38.32 ? 187 ARG D C   1 
ATOM   6220 O  O   . ARG D 2 24  ? -21.102 50.684 72.935  1.00 38.43 ? 187 ARG D O   1 
ATOM   6221 C  CB  . ARG D 2 24  ? -19.628 48.574 70.978  1.00 37.75 ? 187 ARG D CB  1 
ATOM   6222 C  CG  . ARG D 2 24  ? -18.152 48.231 70.834  1.00 38.60 ? 187 ARG D CG  1 
ATOM   6223 C  CD  . ARG D 2 24  ? -17.662 48.267 69.373  1.00 39.80 ? 187 ARG D CD  1 
ATOM   6224 N  NE  . ARG D 2 24  ? -16.437 47.464 69.204  1.00 44.61 ? 187 ARG D NE  1 
ATOM   6225 C  CZ  . ARG D 2 24  ? -15.545 47.575 68.209  1.00 45.98 ? 187 ARG D CZ  1 
ATOM   6226 N  NH1 . ARG D 2 24  ? -15.689 48.478 67.239  1.00 45.91 ? 187 ARG D NH1 1 
ATOM   6227 N  NH2 . ARG D 2 24  ? -14.484 46.767 68.191  1.00 46.96 ? 187 ARG D NH2 1 
ATOM   6228 N  N   . LEU D 2 25  ? -22.531 49.043 72.347  1.00 39.13 ? 188 LEU D N   1 
ATOM   6229 C  CA  . LEU D 2 25  ? -23.716 49.891 72.450  1.00 39.90 ? 188 LEU D CA  1 
ATOM   6230 C  C   . LEU D 2 25  ? -23.968 50.359 73.870  1.00 40.68 ? 188 LEU D C   1 
ATOM   6231 O  O   . LEU D 2 25  ? -24.011 51.559 74.114  1.00 40.95 ? 188 LEU D O   1 
ATOM   6232 C  CB  . LEU D 2 25  ? -24.960 49.198 71.897  1.00 39.72 ? 188 LEU D CB  1 
ATOM   6233 C  CG  . LEU D 2 25  ? -25.120 49.125 70.380  1.00 39.65 ? 188 LEU D CG  1 
ATOM   6234 C  CD1 . LEU D 2 25  ? -26.337 48.283 70.025  1.00 39.09 ? 188 LEU D CD1 1 
ATOM   6235 C  CD2 . LEU D 2 25  ? -25.211 50.511 69.763  1.00 39.85 ? 188 LEU D CD2 1 
ATOM   6236 N  N   . GLU D 2 26  ? -24.123 49.426 74.808  1.00 41.75 ? 189 GLU D N   1 
ATOM   6237 C  CA  . GLU D 2 26  ? -24.398 49.806 76.195  1.00 42.92 ? 189 GLU D CA  1 
ATOM   6238 C  C   . GLU D 2 26  ? -23.219 50.518 76.850  1.00 43.76 ? 189 GLU D C   1 
ATOM   6239 O  O   . GLU D 2 26  ? -23.395 51.242 77.827  1.00 43.82 ? 189 GLU D O   1 
ATOM   6240 C  CB  . GLU D 2 26  ? -24.896 48.626 77.032  1.00 42.72 ? 189 GLU D CB  1 
ATOM   6241 C  CG  . GLU D 2 26  ? -24.027 47.400 77.001  1.00 43.30 ? 189 GLU D CG  1 
ATOM   6242 C  CD  . GLU D 2 26  ? -24.722 46.177 77.581  1.00 44.42 ? 189 GLU D CD  1 
ATOM   6243 O  OE1 . GLU D 2 26  ? -25.968 46.076 77.479  1.00 44.24 ? 189 GLU D OE1 1 
ATOM   6244 O  OE2 . GLU D 2 26  ? -24.017 45.304 78.134  1.00 45.35 ? 189 GLU D OE2 1 
ATOM   6245 N  N   . GLN D 2 27  ? -22.030 50.335 76.283  1.00 45.08 ? 190 GLN D N   1 
ATOM   6246 C  CA  . GLN D 2 27  ? -20.843 51.060 76.719  1.00 46.47 ? 190 GLN D CA  1 
ATOM   6247 C  C   . GLN D 2 27  ? -20.906 52.513 76.262  1.00 47.34 ? 190 GLN D C   1 
ATOM   6248 O  O   . GLN D 2 27  ? -20.589 53.418 77.031  1.00 47.44 ? 190 GLN D O   1 
ATOM   6249 C  CB  . GLN D 2 27  ? -19.565 50.379 76.212  1.00 46.52 ? 190 GLN D CB  1 
ATOM   6250 C  CG  . GLN D 2 27  ? -18.322 50.605 77.089  1.00 47.17 ? 190 GLN D CG  1 
ATOM   6251 C  CD  . GLN D 2 27  ? -18.464 50.038 78.507  1.00 47.42 ? 190 GLN D CD  1 
ATOM   6252 O  OE1 . GLN D 2 27  ? -19.018 48.956 78.707  1.00 48.26 ? 190 GLN D OE1 1 
ATOM   6253 N  NE2 . GLN D 2 27  ? -17.956 50.771 79.491  1.00 47.04 ? 190 GLN D NE2 1 
ATOM   6254 N  N   . GLU D 2 28  ? -21.323 52.731 75.014  1.00 48.58 ? 191 GLU D N   1 
ATOM   6255 C  CA  . GLU D 2 28  ? -21.550 54.080 74.491  1.00 49.91 ? 191 GLU D CA  1 
ATOM   6256 C  C   . GLU D 2 28  ? -22.823 54.663 75.125  1.00 50.53 ? 191 GLU D C   1 
ATOM   6257 O  O   . GLU D 2 28  ? -23.034 55.876 75.132  1.00 50.65 ? 191 GLU D O   1 
ATOM   6258 C  CB  . GLU D 2 28  ? -21.626 54.062 72.952  1.00 49.95 ? 191 GLU D CB  1 
ATOM   6259 C  CG  . GLU D 2 28  ? -21.459 55.440 72.243  1.00 51.82 ? 191 GLU D CG  1 
ATOM   6260 C  CD  . GLU D 2 28  ? -19.995 55.963 72.161  1.00 53.65 ? 191 GLU D CD  1 
ATOM   6261 O  OE1 . GLU D 2 28  ? -19.070 55.155 71.877  1.00 53.51 ? 191 GLU D OE1 1 
ATOM   6262 O  OE2 . GLU D 2 28  ? -19.784 57.195 72.354  1.00 52.88 ? 191 GLU D OE2 1 
ATOM   6263 N  N   . LEU D 2 29  ? -23.648 53.781 75.684  1.00 51.54 ? 192 LEU D N   1 
ATOM   6264 C  CA  . LEU D 2 29  ? -24.883 54.154 76.368  1.00 52.49 ? 192 LEU D CA  1 
ATOM   6265 C  C   . LEU D 2 29  ? -24.656 54.361 77.869  1.00 53.41 ? 192 LEU D C   1 
ATOM   6266 O  O   . LEU D 2 29  ? -25.592 54.647 78.619  1.00 53.51 ? 192 LEU D O   1 
ATOM   6267 C  CB  . LEU D 2 29  ? -25.936 53.077 76.124  1.00 52.35 ? 192 LEU D CB  1 
ATOM   6268 C  CG  . LEU D 2 29  ? -27.406 53.296 76.448  1.00 52.23 ? 192 LEU D CG  1 
ATOM   6269 C  CD1 . LEU D 2 29  ? -27.919 54.573 75.813  1.00 52.29 ? 192 LEU D CD1 1 
ATOM   6270 C  CD2 . LEU D 2 29  ? -28.180 52.095 75.950  1.00 52.36 ? 192 LEU D CD2 1 
ATOM   6271 N  N   . LYS D 2 30  ? -23.405 54.196 78.294  1.00 54.56 ? 193 LYS D N   1 
ATOM   6272 C  CA  . LYS D 2 30  ? -22.959 54.570 79.635  1.00 55.61 ? 193 LYS D CA  1 
ATOM   6273 C  C   . LYS D 2 30  ? -22.250 55.925 79.541  1.00 56.21 ? 193 LYS D C   1 
ATOM   6274 O  O   . LYS D 2 30  ? -22.609 56.867 80.252  1.00 56.38 ? 193 LYS D O   1 
ATOM   6275 C  CB  . LYS D 2 30  ? -22.023 53.504 80.206  1.00 55.55 ? 193 LYS D CB  1 
ATOM   6276 C  CG  . LYS D 2 30  ? -21.750 53.622 81.704  1.00 56.00 ? 193 LYS D CG  1 
ATOM   6277 C  CD  . LYS D 2 30  ? -20.801 52.518 82.209  1.00 55.99 ? 193 LYS D CD  1 
ATOM   6278 C  CE  . LYS D 2 30  ? -21.496 51.158 82.350  1.00 56.09 ? 193 LYS D CE  1 
ATOM   6279 N  NZ  . LYS D 2 30  ? -20.566 50.101 82.844  1.00 56.09 ? 193 LYS D NZ  1 
ATOM   6280 N  N   . GLU D 2 31  ? -21.254 56.003 78.649  1.00 56.99 ? 194 GLU D N   1 
ATOM   6281 C  CA  . GLU D 2 31  ? -20.556 57.249 78.261  1.00 57.78 ? 194 GLU D CA  1 
ATOM   6282 C  C   . GLU D 2 31  ? -21.497 58.469 78.257  1.00 58.12 ? 194 GLU D C   1 
ATOM   6283 O  O   . GLU D 2 31  ? -21.124 59.555 78.709  1.00 58.08 ? 194 GLU D O   1 
ATOM   6284 C  CB  . GLU D 2 31  ? -19.924 57.058 76.867  1.00 57.75 ? 194 GLU D CB  1 
ATOM   6285 C  CG  . GLU D 2 31  ? -18.693 57.916 76.527  1.00 57.91 ? 194 GLU D CG  1 
ATOM   6286 C  CD  . GLU D 2 31  ? -17.973 57.454 75.239  1.00 58.10 ? 194 GLU D CD  1 
ATOM   6287 O  OE1 . GLU D 2 31  ? -17.999 56.242 74.922  1.00 58.04 ? 194 GLU D OE1 1 
ATOM   6288 O  OE2 . GLU D 2 31  ? -17.370 58.302 74.542  1.00 58.45 ? 194 GLU D OE2 1 
ATOM   6289 N  N   . ILE D 2 32  ? -22.718 58.257 77.758  1.00 58.61 ? 195 ILE D N   1 
ATOM   6290 C  CA  . ILE D 2 32  ? -23.757 59.286 77.650  1.00 58.94 ? 195 ILE D CA  1 
ATOM   6291 C  C   . ILE D 2 32  ? -24.374 59.698 78.997  1.00 59.33 ? 195 ILE D C   1 
ATOM   6292 O  O   . ILE D 2 32  ? -24.484 60.894 79.289  1.00 59.50 ? 195 ILE D O   1 
ATOM   6293 C  CB  . ILE D 2 32  ? -24.856 58.866 76.614  1.00 58.87 ? 195 ILE D CB  1 
ATOM   6294 C  CG1 . ILE D 2 32  ? -24.481 59.380 75.216  1.00 58.88 ? 195 ILE D CG1 1 
ATOM   6295 C  CG2 . ILE D 2 32  ? -26.252 59.353 77.026  1.00 58.56 ? 195 ILE D CG2 1 
ATOM   6296 C  CD1 . ILE D 2 32  ? -25.356 58.852 74.079  1.00 58.84 ? 195 ILE D CD1 1 
ATOM   6297 N  N   . ASP D 2 33  ? -24.755 58.718 79.815  1.00 59.71 ? 196 ASP D N   1 
ATOM   6298 C  CA  . ASP D 2 33  ? -25.461 58.989 81.076  1.00 60.15 ? 196 ASP D CA  1 
ATOM   6299 C  C   . ASP D 2 33  ? -24.632 59.708 82.144  1.00 60.35 ? 196 ASP D C   1 
ATOM   6300 O  O   . ASP D 2 33  ? -25.131 60.008 83.231  1.00 60.38 ? 196 ASP D O   1 
ATOM   6301 C  CB  . ASP D 2 33  ? -26.062 57.701 81.634  1.00 60.22 ? 196 ASP D CB  1 
ATOM   6302 C  CG  . ASP D 2 33  ? -27.352 57.332 80.948  1.00 60.59 ? 196 ASP D CG  1 
ATOM   6303 O  OD1 . ASP D 2 33  ? -28.377 57.990 81.236  1.00 60.68 ? 196 ASP D OD1 1 
ATOM   6304 O  OD2 . ASP D 2 33  ? -27.336 56.395 80.115  1.00 60.68 ? 196 ASP D OD2 1 
ATOM   6305 N  N   . GLU D 2 34  ? -23.374 59.992 81.817  1.00 60.65 ? 197 GLU D N   1 
ATOM   6306 C  CA  . GLU D 2 34  ? -22.482 60.742 82.695  1.00 60.79 ? 197 GLU D CA  1 
ATOM   6307 C  C   . GLU D 2 34  ? -21.943 61.982 81.969  1.00 60.74 ? 197 GLU D C   1 
ATOM   6308 O  O   . GLU D 2 34  ? -21.099 61.912 81.075  1.00 60.70 ? 197 GLU D O   1 
ATOM   6309 C  CB  . GLU D 2 34  ? -21.354 59.830 83.209  1.00 60.90 ? 197 GLU D CB  1 
ATOM   6310 C  CG  . GLU D 2 34  ? -21.827 58.777 84.240  1.00 61.19 ? 197 GLU D CG  1 
ATOM   6311 C  CD  . GLU D 2 34  ? -20.995 57.496 84.239  1.00 61.43 ? 197 GLU D CD  1 
ATOM   6312 O  OE1 . GLU D 2 34  ? -19.748 57.582 84.194  1.00 61.63 ? 197 GLU D OE1 1 
ATOM   6313 O  OE2 . GLU D 2 34  ? -21.596 56.397 84.291  1.00 61.22 ? 197 GLU D OE2 1 
ATOM   6314 N  N   . ALA D 2 47  ? -30.765 57.892 73.941  1.00 47.99 ? 210 ALA D N   1 
ATOM   6315 C  CA  . ALA D 2 47  ? -32.207 57.511 74.054  1.00 48.11 ? 210 ALA D CA  1 
ATOM   6316 C  C   . ALA D 2 47  ? -32.734 56.624 72.905  1.00 48.12 ? 210 ALA D C   1 
ATOM   6317 O  O   . ALA D 2 47  ? -33.433 55.645 73.173  1.00 48.25 ? 210 ALA D O   1 
ATOM   6318 C  CB  . ALA D 2 47  ? -33.087 58.761 74.237  1.00 48.16 ? 210 ALA D CB  1 
ATOM   6319 N  N   . PRO D 2 48  ? -32.413 56.955 71.628  1.00 48.05 ? 211 PRO D N   1 
ATOM   6320 C  CA  . PRO D 2 48  ? -32.919 56.104 70.549  1.00 47.85 ? 211 PRO D CA  1 
ATOM   6321 C  C   . PRO D 2 48  ? -31.989 54.930 70.241  1.00 47.65 ? 211 PRO D C   1 
ATOM   6322 O  O   . PRO D 2 48  ? -32.348 54.057 69.447  1.00 47.85 ? 211 PRO D O   1 
ATOM   6323 C  CB  . PRO D 2 48  ? -32.966 57.057 69.358  1.00 47.87 ? 211 PRO D CB  1 
ATOM   6324 C  CG  . PRO D 2 48  ? -31.799 57.961 69.581  1.00 48.05 ? 211 PRO D CG  1 
ATOM   6325 C  CD  . PRO D 2 48  ? -31.611 58.076 71.088  1.00 48.18 ? 211 PRO D CD  1 
ATOM   6326 N  N   . LEU D 2 49  ? -30.802 54.926 70.851  1.00 47.21 ? 212 LEU D N   1 
ATOM   6327 C  CA  . LEU D 2 49  ? -29.870 53.799 70.767  1.00 46.65 ? 212 LEU D CA  1 
ATOM   6328 C  C   . LEU D 2 49  ? -30.384 52.628 71.605  1.00 46.21 ? 212 LEU D C   1 
ATOM   6329 O  O   . LEU D 2 49  ? -30.036 51.474 71.350  1.00 46.09 ? 212 LEU D O   1 
ATOM   6330 C  CB  . LEU D 2 49  ? -28.470 54.201 71.251  1.00 46.67 ? 212 LEU D CB  1 
ATOM   6331 C  CG  . LEU D 2 49  ? -27.640 55.194 70.432  1.00 46.96 ? 212 LEU D CG  1 
ATOM   6332 C  CD1 . LEU D 2 49  ? -26.529 55.766 71.290  1.00 46.87 ? 212 LEU D CD1 1 
ATOM   6333 C  CD2 . LEU D 2 49  ? -27.066 54.564 69.154  1.00 47.60 ? 212 LEU D CD2 1 
ATOM   6334 N  N   . GLN D 2 50  ? -31.207 52.946 72.605  1.00 45.56 ? 213 GLN D N   1 
ATOM   6335 C  CA  . GLN D 2 50  ? -31.817 51.955 73.483  1.00 44.89 ? 213 GLN D CA  1 
ATOM   6336 C  C   . GLN D 2 50  ? -32.659 50.971 72.681  1.00 44.54 ? 213 GLN D C   1 
ATOM   6337 O  O   . GLN D 2 50  ? -32.605 49.762 72.918  1.00 44.47 ? 213 GLN D O   1 
ATOM   6338 C  CB  . GLN D 2 50  ? -32.672 52.646 74.553  1.00 44.85 ? 213 GLN D CB  1 
ATOM   6339 C  CG  . GLN D 2 50  ? -33.371 51.700 75.538  1.00 44.78 ? 213 GLN D CG  1 
ATOM   6340 C  CD  . GLN D 2 50  ? -32.403 50.899 76.397  1.00 44.55 ? 213 GLN D CD  1 
ATOM   6341 O  OE1 . GLN D 2 50  ? -31.343 51.390 76.792  1.00 44.41 ? 213 GLN D OE1 1 
ATOM   6342 N  NE2 . GLN D 2 50  ? -32.771 49.658 76.696  1.00 43.92 ? 213 GLN D NE2 1 
ATOM   6343 N  N   . SER D 2 51  ? -33.423 51.501 71.726  1.00 44.11 ? 214 SER D N   1 
ATOM   6344 C  CA  . SER D 2 51  ? -34.304 50.688 70.885  1.00 43.56 ? 214 SER D CA  1 
ATOM   6345 C  C   . SER D 2 51  ? -33.510 49.852 69.883  1.00 42.87 ? 214 SER D C   1 
ATOM   6346 O  O   . SER D 2 51  ? -33.949 48.771 69.496  1.00 42.83 ? 214 SER D O   1 
ATOM   6347 C  CB  . SER D 2 51  ? -35.337 51.562 70.166  1.00 43.70 ? 214 SER D CB  1 
ATOM   6348 O  OG  . SER D 2 51  ? -34.704 52.450 69.258  1.00 44.23 ? 214 SER D OG  1 
ATOM   6349 N  N   . LYS D 2 52  ? -32.349 50.354 69.465  1.00 42.00 ? 215 LYS D N   1 
ATOM   6350 C  CA  . LYS D 2 52  ? -31.433 49.558 68.647  1.00 41.36 ? 215 LYS D CA  1 
ATOM   6351 C  C   . LYS D 2 52  ? -30.783 48.450 69.486  1.00 40.43 ? 215 LYS D C   1 
ATOM   6352 O  O   . LYS D 2 52  ? -30.678 47.311 69.035  1.00 40.43 ? 215 LYS D O   1 
ATOM   6353 C  CB  . LYS D 2 52  ? -30.370 50.436 67.977  1.00 41.29 ? 215 LYS D CB  1 
ATOM   6354 C  CG  . LYS D 2 52  ? -29.593 49.720 66.875  1.00 41.64 ? 215 LYS D CG  1 
ATOM   6355 C  CD  . LYS D 2 52  ? -28.722 50.674 66.070  1.00 42.25 ? 215 LYS D CD  1 
ATOM   6356 C  CE  . LYS D 2 52  ? -27.297 50.750 66.610  1.00 43.72 ? 215 LYS D CE  1 
ATOM   6357 N  NZ  . LYS D 2 52  ? -26.532 51.909 66.042  1.00 44.41 ? 215 LYS D NZ  1 
ATOM   6358 N  N   . LEU D 2 53  ? -30.362 48.796 70.704  1.00 39.54 ? 216 LEU D N   1 
ATOM   6359 C  CA  . LEU D 2 53  ? -29.792 47.837 71.652  1.00 38.58 ? 216 LEU D CA  1 
ATOM   6360 C  C   . LEU D 2 53  ? -30.778 46.711 71.946  1.00 38.33 ? 216 LEU D C   1 
ATOM   6361 O  O   . LEU D 2 53  ? -30.430 45.535 71.845  1.00 38.34 ? 216 LEU D O   1 
ATOM   6362 C  CB  . LEU D 2 53  ? -29.362 48.536 72.954  1.00 38.44 ? 216 LEU D CB  1 
ATOM   6363 C  CG  . LEU D 2 53  ? -28.900 47.679 74.142  1.00 37.99 ? 216 LEU D CG  1 
ATOM   6364 C  CD1 . LEU D 2 53  ? -27.473 47.209 73.961  1.00 37.64 ? 216 LEU D CD1 1 
ATOM   6365 C  CD2 . LEU D 2 53  ? -29.037 48.424 75.454  1.00 38.17 ? 216 LEU D CD2 1 
ATOM   6366 N  N   . ASP D 2 54  ? -32.010 47.076 72.288  1.00 37.86 ? 217 ASP D N   1 
ATOM   6367 C  CA  . ASP D 2 54  ? -33.039 46.095 72.598  1.00 37.61 ? 217 ASP D CA  1 
ATOM   6368 C  C   . ASP D 2 54  ? -33.229 45.081 71.472  1.00 37.24 ? 217 ASP D C   1 
ATOM   6369 O  O   . ASP D 2 54  ? -33.427 43.894 71.735  1.00 37.17 ? 217 ASP D O   1 
ATOM   6370 C  CB  . ASP D 2 54  ? -34.365 46.787 72.932  1.00 37.83 ? 217 ASP D CB  1 
ATOM   6371 C  CG  . ASP D 2 54  ? -34.400 47.354 74.353  1.00 38.50 ? 217 ASP D CG  1 
ATOM   6372 O  OD1 . ASP D 2 54  ? -33.652 46.849 75.223  1.00 39.27 ? 217 ASP D OD1 1 
ATOM   6373 O  OD2 . ASP D 2 54  ? -35.188 48.301 74.600  1.00 39.18 ? 217 ASP D OD2 1 
ATOM   6374 N  N   . ALA D 2 55  ? -33.156 45.548 70.227  1.00 36.87 ? 218 ALA D N   1 
ATOM   6375 C  CA  . ALA D 2 55  ? -33.299 44.672 69.063  1.00 36.72 ? 218 ALA D CA  1 
ATOM   6376 C  C   . ALA D 2 55  ? -32.134 43.700 68.953  1.00 36.70 ? 218 ALA D C   1 
ATOM   6377 O  O   . ALA D 2 55  ? -32.338 42.492 68.819  1.00 36.75 ? 218 ALA D O   1 
ATOM   6378 C  CB  . ALA D 2 55  ? -33.428 45.482 67.792  1.00 36.60 ? 218 ALA D CB  1 
ATOM   6379 N  N   . LYS D 2 56  ? -30.917 44.231 69.020  1.00 36.47 ? 219 LYS D N   1 
ATOM   6380 C  CA  . LYS D 2 56  ? -29.726 43.403 68.948  1.00 36.50 ? 219 LYS D CA  1 
ATOM   6381 C  C   . LYS D 2 56  ? -29.689 42.379 70.077  1.00 36.25 ? 219 LYS D C   1 
ATOM   6382 O  O   . LYS D 2 56  ? -29.304 41.234 69.853  1.00 36.19 ? 219 LYS D O   1 
ATOM   6383 C  CB  . LYS D 2 56  ? -28.463 44.263 68.973  1.00 36.71 ? 219 LYS D CB  1 
ATOM   6384 C  CG  . LYS D 2 56  ? -28.351 45.285 67.839  1.00 37.52 ? 219 LYS D CG  1 
ATOM   6385 C  CD  . LYS D 2 56  ? -27.961 44.654 66.498  1.00 38.74 ? 219 LYS D CD  1 
ATOM   6386 C  CE  . LYS D 2 56  ? -27.458 45.702 65.507  1.00 38.78 ? 219 LYS D CE  1 
ATOM   6387 N  NZ  . LYS D 2 56  ? -26.215 46.383 65.990  1.00 38.88 ? 219 LYS D NZ  1 
ATOM   6388 N  N   . LYS D 2 57  ? -30.099 42.799 71.277  1.00 36.03 ? 220 LYS D N   1 
ATOM   6389 C  CA  . LYS D 2 57  ? -30.148 41.928 72.459  1.00 35.94 ? 220 LYS D CA  1 
ATOM   6390 C  C   . LYS D 2 57  ? -31.170 40.817 72.319  1.00 35.70 ? 220 LYS D C   1 
ATOM   6391 O  O   . LYS D 2 57  ? -30.943 39.693 72.774  1.00 35.71 ? 220 LYS D O   1 
ATOM   6392 C  CB  . LYS D 2 57  ? -30.465 42.728 73.719  1.00 36.08 ? 220 LYS D CB  1 
ATOM   6393 C  CG  . LYS D 2 57  ? -29.283 42.941 74.642  1.00 37.18 ? 220 LYS D CG  1 
ATOM   6394 C  CD  . LYS D 2 57  ? -29.715 43.636 75.917  1.00 38.79 ? 220 LYS D CD  1 
ATOM   6395 C  CE  . LYS D 2 57  ? -28.613 43.614 76.960  1.00 40.07 ? 220 LYS D CE  1 
ATOM   6396 N  NZ  . LYS D 2 57  ? -28.855 44.669 77.986  1.00 41.11 ? 220 LYS D NZ  1 
ATOM   6397 N  N   . ALA D 2 58  ? -32.302 41.151 71.706  1.00 35.48 ? 221 ALA D N   1 
ATOM   6398 C  CA  . ALA D 2 58  ? -33.340 40.179 71.418  1.00 35.14 ? 221 ALA D CA  1 
ATOM   6399 C  C   . ALA D 2 58  ? -32.848 39.231 70.337  1.00 35.05 ? 221 ALA D C   1 
ATOM   6400 O  O   . ALA D 2 58  ? -33.070 38.025 70.427  1.00 35.24 ? 221 ALA D O   1 
ATOM   6401 C  CB  . ALA D 2 58  ? -34.619 40.868 70.990  1.00 35.04 ? 221 ALA D CB  1 
ATOM   6402 N  N   . LYS D 2 59  ? -32.162 39.765 69.328  1.00 34.82 ? 222 LYS D N   1 
ATOM   6403 C  CA  . LYS D 2 59  ? -31.644 38.921 68.263  1.00 34.57 ? 222 LYS D CA  1 
ATOM   6404 C  C   . LYS D 2 59  ? -30.579 37.986 68.793  1.00 34.62 ? 222 LYS D C   1 
ATOM   6405 O  O   . LYS D 2 59  ? -30.557 36.814 68.417  1.00 34.83 ? 222 LYS D O   1 
ATOM   6406 C  CB  . LYS D 2 59  ? -31.088 39.726 67.091  1.00 34.57 ? 222 LYS D CB  1 
ATOM   6407 C  CG  . LYS D 2 59  ? -30.864 38.859 65.854  1.00 34.42 ? 222 LYS D CG  1 
ATOM   6408 C  CD  . LYS D 2 59  ? -29.772 39.380 64.939  1.00 34.22 ? 222 LYS D CD  1 
ATOM   6409 C  CE  . LYS D 2 59  ? -29.656 38.496 63.704  1.00 34.30 ? 222 LYS D CE  1 
ATOM   6410 N  NZ  . LYS D 2 59  ? -28.951 39.171 62.585  1.00 33.45 ? 222 LYS D NZ  1 
ATOM   6411 N  N   . LEU D 2 60  ? -29.711 38.501 69.667  1.00 34.60 ? 223 LEU D N   1 
ATOM   6412 C  CA  . LEU D 2 60  ? -28.624 37.708 70.248  1.00 34.64 ? 223 LEU D CA  1 
ATOM   6413 C  C   . LEU D 2 60  ? -29.177 36.580 71.119  1.00 35.19 ? 223 LEU D C   1 
ATOM   6414 O  O   . LEU D 2 60  ? -28.723 35.434 71.043  1.00 35.04 ? 223 LEU D O   1 
ATOM   6415 C  CB  . LEU D 2 60  ? -27.657 38.599 71.039  1.00 34.49 ? 223 LEU D CB  1 
ATOM   6416 C  CG  . LEU D 2 60  ? -26.437 37.940 71.700  1.00 34.15 ? 223 LEU D CG  1 
ATOM   6417 C  CD1 . LEU D 2 60  ? -25.478 37.331 70.674  1.00 33.38 ? 223 LEU D CD1 1 
ATOM   6418 C  CD2 . LEU D 2 60  ? -25.707 38.918 72.603  1.00 33.98 ? 223 LEU D CD2 1 
ATOM   6419 N  N   . SER D 2 61  ? -30.180 36.920 71.925  1.00 35.97 ? 224 SER D N   1 
ATOM   6420 C  CA  . SER D 2 61  ? -30.913 35.961 72.756  1.00 36.47 ? 224 SER D CA  1 
ATOM   6421 C  C   . SER D 2 61  ? -31.385 34.718 71.979  1.00 36.93 ? 224 SER D C   1 
ATOM   6422 O  O   . SER D 2 61  ? -31.185 33.585 72.436  1.00 36.89 ? 224 SER D O   1 
ATOM   6423 C  CB  . SER D 2 61  ? -32.087 36.674 73.424  1.00 36.16 ? 224 SER D CB  1 
ATOM   6424 O  OG  . SER D 2 61  ? -33.001 35.755 73.971  1.00 36.54 ? 224 SER D OG  1 
ATOM   6425 N  N   . LYS D 2 62  ? -31.994 34.940 70.811  1.00 37.59 ? 225 LYS D N   1 
ATOM   6426 C  CA  . LYS D 2 62  ? -32.446 33.862 69.925  1.00 38.26 ? 225 LYS D CA  1 
ATOM   6427 C  C   . LYS D 2 62  ? -31.293 33.020 69.393  1.00 38.65 ? 225 LYS D C   1 
ATOM   6428 O  O   . LYS D 2 62  ? -31.431 31.806 69.253  1.00 38.77 ? 225 LYS D O   1 
ATOM   6429 C  CB  . LYS D 2 62  ? -33.245 34.418 68.744  1.00 38.28 ? 225 LYS D CB  1 
ATOM   6430 C  CG  . LYS D 2 62  ? -34.701 34.757 69.049  1.00 38.79 ? 225 LYS D CG  1 
ATOM   6431 C  CD  . LYS D 2 62  ? -35.436 35.221 67.781  1.00 38.71 ? 225 LYS D CD  1 
ATOM   6432 C  CE  . LYS D 2 62  ? -36.889 35.637 68.068  1.00 39.37 ? 225 LYS D CE  1 
ATOM   6433 N  NZ  . LYS D 2 62  ? -36.996 36.992 68.695  1.00 39.16 ? 225 LYS D NZ  1 
ATOM   6434 N  N   . LEU D 2 63  ? -30.167 33.663 69.089  1.00 39.17 ? 226 LEU D N   1 
ATOM   6435 C  CA  . LEU D 2 63  ? -28.994 32.961 68.555  1.00 39.72 ? 226 LEU D CA  1 
ATOM   6436 C  C   . LEU D 2 63  ? -28.241 32.154 69.621  1.00 40.22 ? 226 LEU D C   1 
ATOM   6437 O  O   . LEU D 2 63  ? -27.670 31.102 69.331  1.00 40.19 ? 226 LEU D O   1 
ATOM   6438 C  CB  . LEU D 2 63  ? -28.044 33.941 67.865  1.00 39.60 ? 226 LEU D CB  1 
ATOM   6439 C  CG  . LEU D 2 63  ? -28.582 34.745 66.682  1.00 39.59 ? 226 LEU D CG  1 
ATOM   6440 C  CD1 . LEU D 2 63  ? -27.527 35.729 66.203  1.00 39.28 ? 226 LEU D CD1 1 
ATOM   6441 C  CD2 . LEU D 2 63  ? -29.045 33.841 65.540  1.00 39.44 ? 226 LEU D CD2 1 
ATOM   6442 N  N   . GLU D 2 64  ? -28.238 32.660 70.849  1.00 40.91 ? 227 GLU D N   1 
ATOM   6443 C  CA  . GLU D 2 64  ? -27.664 31.942 71.981  1.00 41.71 ? 227 GLU D CA  1 
ATOM   6444 C  C   . GLU D 2 64  ? -28.468 30.688 72.364  1.00 41.55 ? 227 GLU D C   1 
ATOM   6445 O  O   . GLU D 2 64  ? -27.894 29.644 72.679  1.00 41.40 ? 227 GLU D O   1 
ATOM   6446 C  CB  . GLU D 2 64  ? -27.510 32.884 73.182  1.00 41.99 ? 227 GLU D CB  1 
ATOM   6447 C  CG  . GLU D 2 64  ? -26.322 33.855 73.075  1.00 44.64 ? 227 GLU D CG  1 
ATOM   6448 C  CD  . GLU D 2 64  ? -24.968 33.142 72.959  1.00 48.61 ? 227 GLU D CD  1 
ATOM   6449 O  OE1 . GLU D 2 64  ? -24.560 32.803 71.824  1.00 50.40 ? 227 GLU D OE1 1 
ATOM   6450 O  OE2 . GLU D 2 64  ? -24.303 32.919 74.002  1.00 50.71 ? 227 GLU D OE2 1 
ATOM   6451 N  N   . GLU D 2 65  ? -29.793 30.798 72.324  1.00 41.64 ? 228 GLU D N   1 
ATOM   6452 C  CA  . GLU D 2 65  ? -30.677 29.687 72.663  1.00 41.73 ? 228 GLU D CA  1 
ATOM   6453 C  C   . GLU D 2 65  ? -30.473 28.506 71.713  1.00 41.22 ? 228 GLU D C   1 
ATOM   6454 O  O   . GLU D 2 65  ? -30.467 27.359 72.156  1.00 41.29 ? 228 GLU D O   1 
ATOM   6455 C  CB  . GLU D 2 65  ? -32.136 30.143 72.656  1.00 41.62 ? 228 GLU D CB  1 
ATOM   6456 C  CG  . GLU D 2 65  ? -33.080 29.240 73.440  1.00 42.53 ? 228 GLU D CG  1 
ATOM   6457 C  CD  . GLU D 2 65  ? -34.558 29.488 73.112  1.00 42.93 ? 228 GLU D CD  1 
ATOM   6458 O  OE1 . GLU D 2 65  ? -35.076 30.597 73.392  1.00 44.14 ? 228 GLU D OE1 1 
ATOM   6459 O  OE2 . GLU D 2 65  ? -35.206 28.560 72.578  1.00 44.39 ? 228 GLU D OE2 1 
ATOM   6460 N  N   . LEU D 2 66  ? -30.298 28.800 70.421  1.00 40.75 ? 229 LEU D N   1 
ATOM   6461 C  CA  . LEU D 2 66  ? -30.050 27.783 69.392  1.00 40.14 ? 229 LEU D CA  1 
ATOM   6462 C  C   . LEU D 2 66  ? -28.680 27.144 69.547  1.00 40.08 ? 229 LEU D C   1 
ATOM   6463 O  O   . LEU D 2 66  ? -28.535 25.934 69.385  1.00 40.08 ? 229 LEU D O   1 
ATOM   6464 C  CB  . LEU D 2 66  ? -30.177 28.372 67.982  1.00 39.87 ? 229 LEU D CB  1 
ATOM   6465 C  CG  . LEU D 2 66  ? -31.547 28.825 67.453  1.00 39.69 ? 229 LEU D CG  1 
ATOM   6466 C  CD1 . LEU D 2 66  ? -31.385 29.578 66.148  1.00 38.05 ? 229 LEU D CD1 1 
ATOM   6467 C  CD2 . LEU D 2 66  ? -32.525 27.660 67.280  1.00 39.27 ? 229 LEU D CD2 1 
ATOM   6468 N  N   . SER D 2 67  ? -27.680 27.964 69.854  1.00 40.13 ? 230 SER D N   1 
ATOM   6469 C  CA  . SER D 2 67  ? -26.305 27.495 70.019  1.00 40.21 ? 230 SER D CA  1 
ATOM   6470 C  C   . SER D 2 67  ? -26.193 26.570 71.214  1.00 40.25 ? 230 SER D C   1 
ATOM   6471 O  O   . SER D 2 67  ? -25.521 25.538 71.150  1.00 40.31 ? 230 SER D O   1 
ATOM   6472 C  CB  . SER D 2 67  ? -25.355 28.675 70.213  1.00 40.25 ? 230 SER D CB  1 
ATOM   6473 O  OG  . SER D 2 67  ? -25.346 29.527 69.087  1.00 40.49 ? 230 SER D OG  1 
ATOM   6474 N  N   . ASP D 2 68  ? -26.852 26.960 72.302  1.00 40.37 ? 231 ASP D N   1 
ATOM   6475 C  CA  . ASP D 2 68  ? -26.936 26.157 73.518  1.00 40.61 ? 231 ASP D CA  1 
ATOM   6476 C  C   . ASP D 2 68  ? -27.580 24.795 73.225  1.00 40.26 ? 231 ASP D C   1 
ATOM   6477 O  O   . ASP D 2 68  ? -27.132 23.777 73.740  1.00 40.28 ? 231 ASP D O   1 
ATOM   6478 C  CB  . ASP D 2 68  ? -27.715 26.926 74.600  1.00 40.98 ? 231 ASP D CB  1 
ATOM   6479 C  CG  . ASP D 2 68  ? -27.751 26.199 75.946  1.00 42.20 ? 231 ASP D CG  1 
ATOM   6480 O  OD1 . ASP D 2 68  ? -26.689 26.063 76.605  1.00 43.35 ? 231 ASP D OD1 1 
ATOM   6481 O  OD2 . ASP D 2 68  ? -28.857 25.782 76.353  1.00 43.31 ? 231 ASP D OD2 1 
ATOM   6482 N  N   . LYS D 2 69  ? -28.613 24.789 72.381  1.00 39.97 ? 232 LYS D N   1 
ATOM   6483 C  CA  . LYS D 2 69  ? -29.289 23.559 71.974  1.00 39.58 ? 232 LYS D CA  1 
ATOM   6484 C  C   . LYS D 2 69  ? -28.396 22.676 71.113  1.00 39.23 ? 232 LYS D C   1 
ATOM   6485 O  O   . LYS D 2 69  ? -28.415 21.457 71.256  1.00 39.31 ? 232 LYS D O   1 
ATOM   6486 C  CB  . LYS D 2 69  ? -30.595 23.854 71.236  1.00 39.65 ? 232 LYS D CB  1 
ATOM   6487 C  CG  . LYS D 2 69  ? -31.516 22.648 71.154  1.00 40.35 ? 232 LYS D CG  1 
ATOM   6488 C  CD  . LYS D 2 69  ? -32.737 22.903 70.287  1.00 42.21 ? 232 LYS D CD  1 
ATOM   6489 C  CE  . LYS D 2 69  ? -33.790 21.813 70.525  1.00 43.86 ? 232 LYS D CE  1 
ATOM   6490 N  NZ  . LYS D 2 69  ? -34.875 21.787 69.494  1.00 43.94 ? 232 LYS D NZ  1 
ATOM   6491 N  N   . ILE D 2 70  ? -27.624 23.288 70.219  1.00 38.94 ? 233 ILE D N   1 
ATOM   6492 C  CA  . ILE D 2 70  ? -26.627 22.557 69.437  1.00 38.61 ? 233 ILE D CA  1 
ATOM   6493 C  C   . ILE D 2 70  ? -25.629 21.885 70.375  1.00 38.69 ? 233 ILE D C   1 
ATOM   6494 O  O   . ILE D 2 70  ? -25.247 20.736 70.150  1.00 38.44 ? 233 ILE D O   1 
ATOM   6495 C  CB  . ILE D 2 70  ? -25.917 23.467 68.407  1.00 38.69 ? 233 ILE D CB  1 
ATOM   6496 C  CG1 . ILE D 2 70  ? -26.907 23.888 67.313  1.00 38.79 ? 233 ILE D CG1 1 
ATOM   6497 C  CG2 . ILE D 2 70  ? -24.716 22.767 67.787  1.00 38.23 ? 233 ILE D CG2 1 
ATOM   6498 C  CD1 . ILE D 2 70  ? -26.340 24.847 66.289  1.00 38.40 ? 233 ILE D CD1 1 
ATOM   6499 N  N   . ASP D 2 71  ? -25.238 22.594 71.435  1.00 39.00 ? 234 ASP D N   1 
ATOM   6500 C  CA  . ASP D 2 71  ? -24.372 22.031 72.481  1.00 39.50 ? 234 ASP D CA  1 
ATOM   6501 C  C   . ASP D 2 71  ? -25.057 20.866 73.219  1.00 39.30 ? 234 ASP D C   1 
ATOM   6502 O  O   . ASP D 2 71  ? -24.479 19.780 73.344  1.00 39.21 ? 234 ASP D O   1 
ATOM   6503 C  CB  . ASP D 2 71  ? -23.941 23.107 73.492  1.00 40.00 ? 234 ASP D CB  1 
ATOM   6504 C  CG  . ASP D 2 71  ? -23.072 24.218 72.872  1.00 41.64 ? 234 ASP D CG  1 
ATOM   6505 O  OD1 . ASP D 2 71  ? -22.469 24.006 71.784  1.00 42.67 ? 234 ASP D OD1 1 
ATOM   6506 O  OD2 . ASP D 2 71  ? -22.990 25.309 73.504  1.00 42.60 ? 234 ASP D OD2 1 
ATOM   6507 N  N   . GLU D 2 72  ? -26.285 21.101 73.696  1.00 38.95 ? 235 GLU D N   1 
ATOM   6508 C  CA  . GLU D 2 72  ? -27.082 20.089 74.384  1.00 38.71 ? 235 GLU D CA  1 
ATOM   6509 C  C   . GLU D 2 72  ? -27.174 18.834 73.522  1.00 37.95 ? 235 GLU D C   1 
ATOM   6510 O  O   . GLU D 2 72  ? -26.963 17.722 74.003  1.00 37.89 ? 235 GLU D O   1 
ATOM   6511 C  CB  . GLU D 2 72  ? -28.485 20.627 74.710  1.00 38.56 ? 235 GLU D CB  1 
ATOM   6512 C  CG  . GLU D 2 72  ? -29.279 19.781 75.744  1.00 40.17 ? 235 GLU D CG  1 
ATOM   6513 C  CD  . GLU D 2 72  ? -30.819 19.944 75.658  1.00 40.31 ? 235 GLU D CD  1 
ATOM   6514 O  OE1 . GLU D 2 72  ? -31.331 21.078 75.863  1.00 41.52 ? 235 GLU D OE1 1 
ATOM   6515 O  OE2 . GLU D 2 72  ? -31.515 18.923 75.405  1.00 41.62 ? 235 GLU D OE2 1 
ATOM   6516 N  N   . LEU D 2 73  ? -27.462 19.026 72.240  1.00 37.38 ? 236 LEU D N   1 
ATOM   6517 C  CA  . LEU D 2 73  ? -27.657 17.915 71.311  1.00 36.84 ? 236 LEU D CA  1 
ATOM   6518 C  C   . LEU D 2 73  ? -26.410 17.078 71.087  1.00 36.68 ? 236 LEU D C   1 
ATOM   6519 O  O   . LEU D 2 73  ? -26.461 15.859 71.195  1.00 36.40 ? 236 LEU D O   1 
ATOM   6520 C  CB  . LEU D 2 73  ? -28.207 18.410 69.976  1.00 36.48 ? 236 LEU D CB  1 
ATOM   6521 C  CG  . LEU D 2 73  ? -29.713 18.611 69.987  1.00 36.06 ? 236 LEU D CG  1 
ATOM   6522 C  CD1 . LEU D 2 73  ? -30.141 19.401 68.772  1.00 36.49 ? 236 LEU D CD1 1 
ATOM   6523 C  CD2 . LEU D 2 73  ? -30.412 17.282 70.035  1.00 35.53 ? 236 LEU D CD2 1 
ATOM   6524 N  N   . ASP D 2 74  ? -25.298 17.736 70.775  1.00 36.75 ? 237 ASP D N   1 
ATOM   6525 C  CA  . ASP D 2 74  ? -24.036 17.039 70.568  1.00 37.08 ? 237 ASP D CA  1 
ATOM   6526 C  C   . ASP D 2 74  ? -23.623 16.190 71.777  1.00 36.64 ? 237 ASP D C   1 
ATOM   6527 O  O   . ASP D 2 74  ? -23.116 15.088 71.617  1.00 36.51 ? 237 ASP D O   1 
ATOM   6528 C  CB  . ASP D 2 74  ? -22.928 18.014 70.149  1.00 37.48 ? 237 ASP D CB  1 
ATOM   6529 C  CG  . ASP D 2 74  ? -22.812 18.157 68.620  1.00 39.70 ? 237 ASP D CG  1 
ATOM   6530 O  OD1 . ASP D 2 74  ? -23.050 17.152 67.889  1.00 41.57 ? 237 ASP D OD1 1 
ATOM   6531 O  OD2 . ASP D 2 74  ? -22.466 19.269 68.146  1.00 40.95 ? 237 ASP D OD2 1 
ATOM   6532 N  N   . ALA D 2 75  ? -23.874 16.691 72.981  1.00 36.50 ? 238 ALA D N   1 
ATOM   6533 C  CA  . ALA D 2 75  ? -23.593 15.931 74.202  1.00 36.37 ? 238 ALA D CA  1 
ATOM   6534 C  C   . ALA D 2 75  ? -24.513 14.724 74.328  1.00 36.28 ? 238 ALA D C   1 
ATOM   6535 O  O   . ALA D 2 75  ? -24.037 13.609 74.567  1.00 36.28 ? 238 ALA D O   1 
ATOM   6536 C  CB  . ALA D 2 75  ? -23.697 16.824 75.440  1.00 36.16 ? 238 ALA D CB  1 
ATOM   6537 N  N   . GLU D 2 76  ? -25.818 14.961 74.163  1.00 36.14 ? 239 GLU D N   1 
ATOM   6538 C  CA  . GLU D 2 76  ? -26.829 13.908 74.190  1.00 36.37 ? 239 GLU D CA  1 
ATOM   6539 C  C   . GLU D 2 76  ? -26.476 12.813 73.180  1.00 35.99 ? 239 GLU D C   1 
ATOM   6540 O  O   . GLU D 2 76  ? -26.553 11.626 73.492  1.00 35.93 ? 239 GLU D O   1 
ATOM   6541 C  CB  . GLU D 2 76  ? -28.231 14.480 73.913  1.00 36.27 ? 239 GLU D CB  1 
ATOM   6542 C  CG  . GLU D 2 76  ? -29.026 14.923 75.161  1.00 37.32 ? 239 GLU D CG  1 
ATOM   6543 C  CD  . GLU D 2 76  ? -30.129 15.985 74.876  1.00 37.79 ? 239 GLU D CD  1 
ATOM   6544 O  OE1 . GLU D 2 76  ? -30.428 16.282 73.690  1.00 38.81 ? 239 GLU D OE1 1 
ATOM   6545 O  OE2 . GLU D 2 76  ? -30.703 16.528 75.856  1.00 39.27 ? 239 GLU D OE2 1 
ATOM   6546 N  N   . ILE D 2 77  ? -26.060 13.222 71.984  1.00 35.78 ? 240 ILE D N   1 
ATOM   6547 C  CA  . ILE D 2 77  ? -25.713 12.283 70.925  1.00 35.64 ? 240 ILE D CA  1 
ATOM   6548 C  C   . ILE D 2 77  ? -24.448 11.520 71.294  1.00 36.02 ? 240 ILE D C   1 
ATOM   6549 O  O   . ILE D 2 77  ? -24.350 10.312 71.055  1.00 36.08 ? 240 ILE D O   1 
ATOM   6550 C  CB  . ILE D 2 77  ? -25.590 12.990 69.544  1.00 35.61 ? 240 ILE D CB  1 
ATOM   6551 C  CG1 . ILE D 2 77  ? -26.974 13.467 69.084  1.00 35.33 ? 240 ILE D CG1 1 
ATOM   6552 C  CG2 . ILE D 2 77  ? -24.973 12.055 68.498  1.00 35.32 ? 240 ILE D CG2 1 
ATOM   6553 C  CD1 . ILE D 2 77  ? -26.995 14.335 67.857  1.00 35.27 ? 240 ILE D CD1 1 
ATOM   6554 N  N   . ALA D 2 78  ? -23.502 12.228 71.909  1.00 36.40 ? 241 ALA D N   1 
ATOM   6555 C  CA  . ALA D 2 78  ? -22.214 11.655 72.304  1.00 36.66 ? 241 ALA D CA  1 
ATOM   6556 C  C   . ALA D 2 78  ? -22.348 10.587 73.374  1.00 36.89 ? 241 ALA D C   1 
ATOM   6557 O  O   . ALA D 2 78  ? -21.591 9.617  73.356  1.00 36.81 ? 241 ALA D O   1 
ATOM   6558 C  CB  . ALA D 2 78  ? -21.259 12.745 72.773  1.00 36.87 ? 241 ALA D CB  1 
ATOM   6559 N  N   . LYS D 2 79  ? -23.289 10.779 74.305  1.00 37.17 ? 242 LYS D N   1 
ATOM   6560 C  CA  . LYS D 2 79  ? -23.580 9.773  75.337  1.00 37.53 ? 242 LYS D CA  1 
ATOM   6561 C  C   . LYS D 2 79  ? -24.288 8.567  74.753  1.00 37.38 ? 242 LYS D C   1 
ATOM   6562 O  O   . LYS D 2 79  ? -23.934 7.426  75.057  1.00 37.64 ? 242 LYS D O   1 
ATOM   6563 C  CB  . LYS D 2 79  ? -24.388 10.353 76.501  1.00 37.77 ? 242 LYS D CB  1 
ATOM   6564 C  CG  . LYS D 2 79  ? -23.546 11.237 77.405  1.00 39.50 ? 242 LYS D CG  1 
ATOM   6565 C  CD  . LYS D 2 79  ? -24.058 11.311 78.851  1.00 41.22 ? 242 LYS D CD  1 
ATOM   6566 C  CE  . LYS D 2 79  ? -23.316 12.410 79.640  1.00 40.90 ? 242 LYS D CE  1 
ATOM   6567 N  NZ  . LYS D 2 79  ? -23.570 13.796 79.083  1.00 41.93 ? 242 LYS D NZ  1 
ATOM   6568 N  N   . LEU D 2 80  ? -25.274 8.823  73.900  1.00 36.99 ? 243 LEU D N   1 
ATOM   6569 C  CA  . LEU D 2 80  ? -26.032 7.755  73.288  1.00 36.78 ? 243 LEU D CA  1 
ATOM   6570 C  C   . LEU D 2 80  ? -25.153 6.828  72.452  1.00 36.95 ? 243 LEU D C   1 
ATOM   6571 O  O   . LEU D 2 80  ? -25.247 5.611  72.579  1.00 36.71 ? 243 LEU D O   1 
ATOM   6572 C  CB  . LEU D 2 80  ? -27.183 8.320  72.462  1.00 36.62 ? 243 LEU D CB  1 
ATOM   6573 C  CG  . LEU D 2 80  ? -28.352 8.948  73.229  1.00 36.16 ? 243 LEU D CG  1 
ATOM   6574 C  CD1 . LEU D 2 80  ? -29.372 9.502  72.250  1.00 35.71 ? 243 LEU D CD1 1 
ATOM   6575 C  CD2 . LEU D 2 80  ? -29.011 7.978  74.217  1.00 35.31 ? 243 LEU D CD2 1 
ATOM   6576 N  N   . GLU D 2 81  ? -24.286 7.410  71.624  1.00 37.40 ? 244 GLU D N   1 
ATOM   6577 C  CA  . GLU D 2 81  ? -23.372 6.639  70.775  1.00 37.93 ? 244 GLU D CA  1 
ATOM   6578 C  C   . GLU D 2 81  ? -22.411 5.788  71.588  1.00 38.12 ? 244 GLU D C   1 
ATOM   6579 O  O   . GLU D 2 81  ? -22.074 4.665  71.197  1.00 38.13 ? 244 GLU D O   1 
ATOM   6580 C  CB  . GLU D 2 81  ? -22.594 7.554  69.839  1.00 37.90 ? 244 GLU D CB  1 
ATOM   6581 C  CG  . GLU D 2 81  ? -23.326 7.836  68.546  1.00 39.45 ? 244 GLU D CG  1 
ATOM   6582 C  CD  . GLU D 2 81  ? -22.647 8.896  67.688  1.00 41.40 ? 244 GLU D CD  1 
ATOM   6583 O  OE1 . GLU D 2 81  ? -22.710 8.770  66.442  1.00 42.05 ? 244 GLU D OE1 1 
ATOM   6584 O  OE2 . GLU D 2 81  ? -22.057 9.850  68.251  1.00 42.03 ? 244 GLU D OE2 1 
ATOM   6585 N  N   . ASP D 2 82  ? -21.985 6.323  72.724  1.00 38.35 ? 245 ASP D N   1 
ATOM   6586 C  CA  . ASP D 2 82  ? -21.110 5.592  73.606  1.00 38.76 ? 245 ASP D CA  1 
ATOM   6587 C  C   . ASP D 2 82  ? -21.835 4.447  74.274  1.00 38.75 ? 245 ASP D C   1 
ATOM   6588 O  O   . ASP D 2 82  ? -21.334 3.328  74.284  1.00 39.03 ? 245 ASP D O   1 
ATOM   6589 C  CB  . ASP D 2 82  ? -20.459 6.517  74.630  1.00 39.10 ? 245 ASP D CB  1 
ATOM   6590 C  CG  . ASP D 2 82  ? -19.122 7.063  74.144  1.00 40.33 ? 245 ASP D CG  1 
ATOM   6591 O  OD1 . ASP D 2 82  ? -18.325 6.251  73.620  1.00 41.84 ? 245 ASP D OD1 1 
ATOM   6592 O  OD2 . ASP D 2 82  ? -18.865 8.287  74.280  1.00 40.73 ? 245 ASP D OD2 1 
ATOM   6593 N  N   . GLN D 2 83  ? -23.024 4.694  74.809  1.00 38.73 ? 246 GLN D N   1 
ATOM   6594 C  CA  . GLN D 2 83  ? -23.731 3.593  75.453  1.00 38.77 ? 246 GLN D CA  1 
ATOM   6595 C  C   . GLN D 2 83  ? -24.244 2.564  74.443  1.00 38.82 ? 246 GLN D C   1 
ATOM   6596 O  O   . GLN D 2 83  ? -24.337 1.384  74.763  1.00 38.90 ? 246 GLN D O   1 
ATOM   6597 C  CB  . GLN D 2 83  ? -24.792 4.068  76.455  1.00 38.58 ? 246 GLN D CB  1 
ATOM   6598 C  CG  . GLN D 2 83  ? -26.086 4.537  75.884  1.00 38.41 ? 246 GLN D CG  1 
ATOM   6599 C  CD  . GLN D 2 83  ? -27.152 4.669  76.949  1.00 38.36 ? 246 GLN D CD  1 
ATOM   6600 O  OE1 . GLN D 2 83  ? -27.678 3.671  77.449  1.00 37.99 ? 246 GLN D OE1 1 
ATOM   6601 N  NE2 . GLN D 2 83  ? -27.482 5.905  77.300  1.00 38.28 ? 246 GLN D NE2 1 
ATOM   6602 N  N   . LEU D 2 84  ? -24.527 2.999  73.219  1.00 39.04 ? 247 LEU D N   1 
ATOM   6603 C  CA  . LEU D 2 84  ? -24.794 2.061  72.135  1.00 39.25 ? 247 LEU D CA  1 
ATOM   6604 C  C   . LEU D 2 84  ? -23.547 1.236  71.818  1.00 39.81 ? 247 LEU D C   1 
ATOM   6605 O  O   . LEU D 2 84  ? -23.643 0.026  71.627  1.00 39.70 ? 247 LEU D O   1 
ATOM   6606 C  CB  . LEU D 2 84  ? -25.291 2.771  70.872  1.00 38.96 ? 247 LEU D CB  1 
ATOM   6607 C  CG  . LEU D 2 84  ? -25.570 1.862  69.669  1.00 38.21 ? 247 LEU D CG  1 
ATOM   6608 C  CD1 . LEU D 2 84  ? -26.836 1.058  69.871  1.00 37.87 ? 247 LEU D CD1 1 
ATOM   6609 C  CD2 . LEU D 2 84  ? -25.644 2.651  68.384  1.00 37.79 ? 247 LEU D CD2 1 
ATOM   6610 N  N   . LYS D 2 85  ? -22.384 1.886  71.770  1.00 40.51 ? 248 LYS D N   1 
ATOM   6611 C  CA  . LYS D 2 85  ? -21.133 1.185  71.468  1.00 41.36 ? 248 LYS D CA  1 
ATOM   6612 C  C   . LYS D 2 85  ? -20.893 -0.013 72.405  1.00 41.70 ? 248 LYS D C   1 
ATOM   6613 O  O   . LYS D 2 85  ? -20.252 -0.981 72.008  1.00 41.88 ? 248 LYS D O   1 
ATOM   6614 C  CB  . LYS D 2 85  ? -19.935 2.149  71.445  1.00 41.50 ? 248 LYS D CB  1 
ATOM   6615 C  CG  . LYS D 2 85  ? -18.796 1.740  70.503  1.00 42.35 ? 248 LYS D CG  1 
ATOM   6616 C  CD  . LYS D 2 85  ? -17.748 0.886  71.230  1.00 45.16 ? 248 LYS D CD  1 
ATOM   6617 C  CE  . LYS D 2 85  ? -17.095 -0.154 70.288  1.00 45.85 ? 248 LYS D CE  1 
ATOM   6618 N  NZ  . LYS D 2 85  ? -15.875 0.399  69.593  1.00 46.35 ? 248 LYS D NZ  1 
ATOM   6619 N  N   . ALA D 2 86  ? -21.422 0.042  73.626  1.00 42.16 ? 249 ALA D N   1 
ATOM   6620 C  CA  . ALA D 2 86  ? -21.500 -1.142 74.481  1.00 42.89 ? 249 ALA D CA  1 
ATOM   6621 C  C   . ALA D 2 86  ? -22.556 -2.134 73.946  1.00 43.56 ? 249 ALA D C   1 
ATOM   6622 O  O   . ALA D 2 86  ? -23.675 -2.217 74.461  1.00 43.45 ? 249 ALA D O   1 
ATOM   6623 C  CB  . ALA D 2 86  ? -21.813 -0.734 75.910  1.00 42.93 ? 249 ALA D CB  1 
ATOM   6624 N  N   . ALA D 2 87  ? -22.190 -2.880 72.902  1.00 44.47 ? 250 ALA D N   1 
ATOM   6625 C  CA  . ALA D 2 87  ? -23.138 -3.725 72.161  1.00 45.08 ? 250 ALA D CA  1 
ATOM   6626 C  C   . ALA D 2 87  ? -22.744 -5.198 72.213  1.00 45.78 ? 250 ALA D C   1 
ATOM   6627 O  O   . ALA D 2 87  ? -22.070 -5.699 71.300  1.00 45.87 ? 250 ALA D O   1 
ATOM   6628 C  CB  . ALA D 2 87  ? -23.251 -3.253 70.708  1.00 44.89 ? 250 ALA D CB  1 
ATOM   6629 N  N   . GLU D 2 88  ? -23.133 -5.853 73.318  1.00 46.55 ? 251 GLU D N   1 
ATOM   6630 C  CA  . GLU D 2 88  ? -23.098 -7.329 73.545  1.00 46.93 ? 251 GLU D CA  1 
ATOM   6631 C  C   . GLU D 2 88  ? -24.260 -7.625 74.499  1.00 47.23 ? 251 GLU D C   1 
ATOM   6632 O  O   . GLU D 2 88  ? -24.793 -8.738 74.566  1.00 46.96 ? 251 GLU D O   1 
ATOM   6633 C  CB  . GLU D 2 88  ? -21.799 -7.784 74.228  1.00 46.77 ? 251 GLU D CB  1 
ATOM   6634 C  CG  . GLU D 2 88  ? -20.483 -7.368 73.554  1.00 47.06 ? 251 GLU D CG  1 
ATOM   6635 C  CD  . GLU D 2 88  ? -19.994 -5.988 73.986  1.00 46.88 ? 251 GLU D CD  1 
ATOM   6636 O  OE1 . GLU D 2 88  ? -20.055 -5.675 75.198  1.00 46.90 ? 251 GLU D OE1 1 
ATOM   6637 O  OE2 . GLU D 2 88  ? -19.543 -5.220 73.105  1.00 46.28 ? 251 GLU D OE2 1 
ATOM   6638 N  N   . GLU D 2 89  ? -24.639 -6.551 75.198  1.00 47.79 ? 252 GLU D N   1 
ATOM   6639 C  CA  . GLU D 2 89  ? -25.494 -6.485 76.394  1.00 47.88 ? 252 GLU D CA  1 
ATOM   6640 C  C   . GLU D 2 89  ? -24.694 -6.577 77.699  1.00 48.00 ? 252 GLU D C   1 
ATOM   6641 O  O   . GLU D 2 89  ? -25.120 -7.222 78.653  1.00 48.25 ? 252 GLU D O   1 
ATOM   6642 C  CB  . GLU D 2 89  ? -26.679 -7.452 76.372  1.00 47.80 ? 252 GLU D CB  1 
ATOM   6643 C  CG  . GLU D 2 89  ? -27.922 -6.801 76.950  1.00 47.69 ? 252 GLU D CG  1 
ATOM   6644 C  CD  . GLU D 2 89  ? -28.302 -5.539 76.189  1.00 47.60 ? 252 GLU D CD  1 
ATOM   6645 O  OE1 . GLU D 2 89  ? -27.941 -4.432 76.643  1.00 46.54 ? 252 GLU D OE1 1 
ATOM   6646 O  OE2 . GLU D 2 89  ? -28.940 -5.658 75.120  1.00 47.93 ? 252 GLU D OE2 1 
ATOM   6647 N  N   . GLU D 2 94  ? -31.268 -6.657 75.931  1.00 28.45 ? 257 GLU D N   1 
ATOM   6648 C  CA  . GLU D 2 94  ? -32.395 -6.682 74.955  1.00 28.86 ? 257 GLU D CA  1 
ATOM   6649 C  C   . GLU D 2 94  ? -32.006 -6.020 73.634  1.00 27.77 ? 257 GLU D C   1 
ATOM   6650 O  O   . GLU D 2 94  ? -31.463 -4.918 73.619  1.00 27.53 ? 257 GLU D O   1 
ATOM   6651 C  CB  . GLU D 2 94  ? -33.628 -5.988 75.557  1.00 28.97 ? 257 GLU D CB  1 
ATOM   6652 C  CG  . GLU D 2 94  ? -34.913 -6.044 74.701  1.00 30.13 ? 257 GLU D CG  1 
ATOM   6653 C  CD  . GLU D 2 94  ? -36.113 -5.396 75.405  1.00 30.98 ? 257 GLU D CD  1 
ATOM   6654 O  OE1 . GLU D 2 94  ? -36.005 -4.214 75.835  1.00 33.60 ? 257 GLU D OE1 1 
ATOM   6655 O  OE2 . GLU D 2 94  ? -37.168 -6.070 75.533  1.00 33.29 ? 257 GLU D OE2 1 
ATOM   6656 N  N   . ASP D 2 95  ? -32.301 -6.699 72.530  1.00 26.96 ? 258 ASP D N   1 
ATOM   6657 C  CA  . ASP D 2 95  ? -32.030 -6.164 71.200  1.00 26.17 ? 258 ASP D CA  1 
ATOM   6658 C  C   . ASP D 2 95  ? -32.909 -4.950 70.881  1.00 25.98 ? 258 ASP D C   1 
ATOM   6659 O  O   . ASP D 2 95  ? -32.487 -4.057 70.157  1.00 26.21 ? 258 ASP D O   1 
ATOM   6660 C  CB  . ASP D 2 95  ? -32.197 -7.256 70.140  1.00 25.77 ? 258 ASP D CB  1 
ATOM   6661 C  CG  . ASP D 2 95  ? -31.686 -6.838 68.773  1.00 25.36 ? 258 ASP D CG  1 
ATOM   6662 O  OD1 . ASP D 2 95  ? -30.479 -6.531 68.635  1.00 25.31 ? 258 ASP D OD1 1 
ATOM   6663 O  OD2 . ASP D 2 95  ? -32.494 -6.835 67.822  1.00 24.73 ? 258 ASP D OD2 1 
ATOM   6664 N  N   . TYR D 2 96  ? -34.142 -4.911 71.458  1.00 20.00 ? 259 TYR D N   1 
ATOM   6665 C  CA  . TYR D 2 96  ? -35.070 -3.815 71.210  1.00 20.00 ? 259 TYR D CA  1 
ATOM   6666 C  C   . TYR D 2 96  ? -34.616 -2.540 71.914  1.00 20.00 ? 259 TYR D C   1 
ATOM   6667 O  O   . TYR D 2 96  ? -34.812 -1.444 71.401  1.00 34.11 ? 259 TYR D O   1 
ATOM   6668 C  CB  . TYR D 2 96  ? -36.481 -4.192 71.664  1.00 20.00 ? 259 TYR D CB  1 
ATOM   6669 C  CG  . TYR D 2 96  ? -37.510 -3.108 71.432  1.00 20.00 ? 259 TYR D CG  1 
ATOM   6670 C  CD1 . TYR D 2 96  ? -38.035 -2.882 70.166  1.00 20.00 ? 259 TYR D CD1 1 
ATOM   6671 C  CD2 . TYR D 2 96  ? -37.954 -2.312 72.479  1.00 20.00 ? 259 TYR D CD2 1 
ATOM   6672 C  CE1 . TYR D 2 96  ? -38.975 -1.893 69.949  1.00 20.00 ? 259 TYR D CE1 1 
ATOM   6673 C  CE2 . TYR D 2 96  ? -38.895 -1.319 72.271  1.00 20.00 ? 259 TYR D CE2 1 
ATOM   6674 C  CZ  . TYR D 2 96  ? -39.401 -1.115 71.006  1.00 20.00 ? 259 TYR D CZ  1 
ATOM   6675 O  OH  . TYR D 2 96  ? -40.336 -0.128 70.793  1.00 20.00 ? 259 TYR D OH  1 
ATOM   6676 N  N   . PHE D 2 97  ? -34.025 -2.713 73.089  1.00 25.15 ? 260 PHE D N   1 
ATOM   6677 C  CA  . PHE D 2 97  ? -33.447 -1.587 73.784  1.00 25.36 ? 260 PHE D CA  1 
ATOM   6678 C  C   . PHE D 2 97  ? -32.354 -0.955 72.906  1.00 25.40 ? 260 PHE D C   1 
ATOM   6679 O  O   . PHE D 2 97  ? -32.285 0.271  72.791  1.00 25.80 ? 260 PHE D O   1 
ATOM   6680 C  CB  . PHE D 2 97  ? -32.917 -2.014 75.157  1.00 25.66 ? 260 PHE D CB  1 
ATOM   6681 C  CG  . PHE D 2 97  ? -32.311 -0.898 75.939  1.00 25.94 ? 260 PHE D CG  1 
ATOM   6682 C  CD1 . PHE D 2 97  ? -33.121 0.028  76.595  1.00 26.89 ? 260 PHE D CD1 1 
ATOM   6683 C  CD2 . PHE D 2 97  ? -30.927 -0.756 76.010  1.00 26.56 ? 260 PHE D CD2 1 
ATOM   6684 C  CE1 . PHE D 2 97  ? -32.558 1.085  77.322  1.00 27.19 ? 260 PHE D CE1 1 
ATOM   6685 C  CE2 . PHE D 2 97  ? -30.349 0.296  76.731  1.00 27.04 ? 260 PHE D CE2 1 
ATOM   6686 C  CZ  . PHE D 2 97  ? -31.168 1.219  77.391  1.00 26.85 ? 260 PHE D CZ  1 
ATOM   6687 N  N   . LYS D 2 98  ? -31.520 -1.794 72.283  1.00 25.13 ? 261 LYS D N   1 
ATOM   6688 C  CA  . LYS D 2 98  ? -30.545 -1.353 71.279  1.00 24.80 ? 261 LYS D CA  1 
ATOM   6689 C  C   . LYS D 2 98  ? -31.196 -0.515 70.193  1.00 24.37 ? 261 LYS D C   1 
ATOM   6690 O  O   . LYS D 2 98  ? -30.758 0.604  69.933  1.00 24.42 ? 261 LYS D O   1 
ATOM   6691 C  CB  . LYS D 2 98  ? -29.849 -2.550 70.628  1.00 24.99 ? 261 LYS D CB  1 
ATOM   6692 C  CG  . LYS D 2 98  ? -28.371 -2.669 70.924  1.00 25.93 ? 261 LYS D CG  1 
ATOM   6693 C  CD  . LYS D 2 98  ? -27.880 -4.116 70.756  1.00 28.51 ? 261 LYS D CD  1 
ATOM   6694 C  CE  . LYS D 2 98  ? -27.912 -4.606 69.299  1.00 29.63 ? 261 LYS D CE  1 
ATOM   6695 N  NZ  . LYS D 2 98  ? -27.105 -3.747 68.375  1.00 30.75 ? 261 LYS D NZ  1 
ATOM   6696 N  N   . GLU D 2 99  ? -32.235 -1.064 69.562  1.00 23.79 ? 262 GLU D N   1 
ATOM   6697 C  CA  . GLU D 2 99  ? -32.975 -0.364 68.519  1.00 23.57 ? 262 GLU D CA  1 
ATOM   6698 C  C   . GLU D 2 99  ? -33.510 0.958  69.065  1.00 23.54 ? 262 GLU D C   1 
ATOM   6699 O  O   . GLU D 2 99  ? -33.424 1.995  68.401  1.00 23.55 ? 262 GLU D O   1 
ATOM   6700 C  CB  . GLU D 2 99  ? -34.107 -1.240 67.986  1.00 23.57 ? 262 GLU D CB  1 
ATOM   6701 C  CG  . GLU D 2 99  ? -34.858 -0.666 66.801  1.00 23.52 ? 262 GLU D CG  1 
ATOM   6702 C  CD  . GLU D 2 99  ? -35.644 -1.727 66.055  1.00 24.14 ? 262 GLU D CD  1 
ATOM   6703 O  OE1 . GLU D 2 99  ? -35.033 -2.488 65.276  1.00 24.20 ? 262 GLU D OE1 1 
ATOM   6704 O  OE2 . GLU D 2 99  ? -36.881 -1.806 66.236  1.00 24.52 ? 262 GLU D OE2 1 
ATOM   6705 N  N   . GLY D 2 100 ? -34.032 0.912  70.289  1.00 23.37 ? 263 GLY D N   1 
ATOM   6706 C  CA  . GLY D 2 100 ? -34.432 2.112  71.013  1.00 23.34 ? 263 GLY D CA  1 
ATOM   6707 C  C   . GLY D 2 100 ? -33.386 3.210  70.949  1.00 23.35 ? 263 GLY D C   1 
ATOM   6708 O  O   . GLY D 2 100 ? -33.717 4.363  70.680  1.00 23.51 ? 263 GLY D O   1 
ATOM   6709 N  N   . LEU D 2 101 ? -32.124 2.851  71.183  1.00 23.33 ? 264 LEU D N   1 
ATOM   6710 C  CA  . LEU D 2 101 ? -31.019 3.809  71.133  1.00 23.16 ? 264 LEU D CA  1 
ATOM   6711 C  C   . LEU D 2 101 ? -30.782 4.266  69.711  1.00 23.12 ? 264 LEU D C   1 
ATOM   6712 O  O   . LEU D 2 101 ? -30.614 5.463  69.464  1.00 23.05 ? 264 LEU D O   1 
ATOM   6713 C  CB  . LEU D 2 101 ? -29.731 3.209  71.700  1.00 22.99 ? 264 LEU D CB  1 
ATOM   6714 C  CG  . LEU D 2 101 ? -29.702 2.961  73.203  1.00 23.04 ? 264 LEU D CG  1 
ATOM   6715 C  CD1 . LEU D 2 101 ? -28.652 1.929  73.578  1.00 23.31 ? 264 LEU D CD1 1 
ATOM   6716 C  CD2 . LEU D 2 101 ? -29.451 4.259  73.916  1.00 23.62 ? 264 LEU D CD2 1 
ATOM   6717 N  N   . GLU D 2 102 ? -30.781 3.313  68.781  1.00 23.05 ? 265 GLU D N   1 
ATOM   6718 C  CA  . GLU D 2 102 ? -30.514 3.620  67.380  1.00 23.56 ? 265 GLU D CA  1 
ATOM   6719 C  C   . GLU D 2 102 ? -31.510 4.662  66.909  1.00 23.55 ? 265 GLU D C   1 
ATOM   6720 O  O   . GLU D 2 102 ? -31.111 5.680  66.338  1.00 23.54 ? 265 GLU D O   1 
ATOM   6721 C  CB  . GLU D 2 102 ? -30.582 2.367  66.507  1.00 23.41 ? 265 GLU D CB  1 
ATOM   6722 C  CG  . GLU D 2 102 ? -29.500 1.337  66.820  1.00 24.05 ? 265 GLU D CG  1 
ATOM   6723 C  CD  . GLU D 2 102 ? -29.771 -0.032 66.189  1.00 24.42 ? 265 GLU D CD  1 
ATOM   6724 O  OE1 . GLU D 2 102 ? -30.300 -0.070 65.052  1.00 25.42 ? 265 GLU D OE1 1 
ATOM   6725 O  OE2 . GLU D 2 102 ? -29.442 -1.067 66.826  1.00 24.70 ? 265 GLU D OE2 1 
ATOM   6726 N  N   . LYS D 2 103 ? -32.795 4.408  67.187  1.00 23.50 ? 266 LYS D N   1 
ATOM   6727 C  CA  . LYS D 2 103 ? -33.882 5.325  66.859  1.00 23.51 ? 266 LYS D CA  1 
ATOM   6728 C  C   . LYS D 2 103 ? -33.617 6.710  67.434  1.00 23.32 ? 266 LYS D C   1 
ATOM   6729 O  O   . LYS D 2 103 ? -33.754 7.716  66.740  1.00 23.29 ? 266 LYS D O   1 
ATOM   6730 C  CB  . LYS D 2 103 ? -35.219 4.809  67.401  1.00 23.50 ? 266 LYS D CB  1 
ATOM   6731 C  CG  . LYS D 2 103 ? -35.859 3.638  66.651  1.00 24.15 ? 266 LYS D CG  1 
ATOM   6732 C  CD  . LYS D 2 103 ? -37.309 3.438  67.126  1.00 24.20 ? 266 LYS D CD  1 
ATOM   6733 C  CE  . LYS D 2 103 ? -37.684 1.960  67.324  1.00 25.22 ? 266 LYS D CE  1 
ATOM   6734 N  NZ  . LYS D 2 103 ? -38.195 1.298  66.079  1.00 26.00 ? 266 LYS D NZ  1 
ATOM   6735 N  N   . THR D 2 104 ? -33.232 6.751  68.703  1.00 23.19 ? 267 THR D N   1 
ATOM   6736 C  CA  . THR D 2 104 ? -33.050 8.012  69.409  1.00 23.44 ? 267 THR D CA  1 
ATOM   6737 C  C   . THR D 2 104 ? -31.836 8.786  68.906  1.00 23.68 ? 267 THR D C   1 
ATOM   6738 O  O   . THR D 2 104 ? -31.912 10.001 68.743  1.00 23.50 ? 267 THR D O   1 
ATOM   6739 C  CB  . THR D 2 104 ? -32.958 7.787  70.920  1.00 23.39 ? 267 THR D CB  1 
ATOM   6740 O  OG1 . THR D 2 104 ? -33.932 6.810  71.292  1.00 24.26 ? 267 THR D OG1 1 
ATOM   6741 C  CG2 . THR D 2 104 ? -33.232 9.069  71.688  1.00 22.56 ? 267 THR D CG2 1 
ATOM   6742 N  N   . ILE D 2 105 ? -30.726 8.088  68.657  1.00 23.97 ? 268 ILE D N   1 
ATOM   6743 C  CA  . ILE D 2 105 ? -29.556 8.709  68.030  1.00 24.16 ? 268 ILE D CA  1 
ATOM   6744 C  C   . ILE D 2 105 ? -29.935 9.384  66.707  1.00 24.31 ? 268 ILE D C   1 
ATOM   6745 O  O   . ILE D 2 105 ? -29.684 10.572 66.530  1.00 24.57 ? 268 ILE D O   1 
ATOM   6746 C  CB  . ILE D 2 105 ? -28.422 7.699  67.813  1.00 24.18 ? 268 ILE D CB  1 
ATOM   6747 C  CG1 . ILE D 2 105 ? -27.893 7.215  69.160  1.00 23.81 ? 268 ILE D CG1 1 
ATOM   6748 C  CG2 . ILE D 2 105 ? -27.293 8.305  66.971  1.00 24.40 ? 268 ILE D CG2 1 
ATOM   6749 C  CD1 . ILE D 2 105 ? -26.756 6.217  69.045  1.00 23.79 ? 268 ILE D CD1 1 
ATOM   6750 N  N   . ALA D 2 106 ? -30.562 8.631  65.805  1.00 24.52 ? 269 ALA D N   1 
ATOM   6751 C  CA  . ALA D 2 106 ? -31.035 9.155  64.513  1.00 24.82 ? 269 ALA D CA  1 
ATOM   6752 C  C   . ALA D 2 106 ? -31.951 10.390 64.607  1.00 24.96 ? 269 ALA D C   1 
ATOM   6753 O  O   . ALA D 2 106 ? -31.781 11.343 63.848  1.00 24.94 ? 269 ALA D O   1 
ATOM   6754 C  CB  . ALA D 2 106 ? -31.709 8.050  63.711  1.00 24.60 ? 269 ALA D CB  1 
ATOM   6755 N  N   . ALA D 2 107 ? -32.913 10.357 65.526  1.00 25.39 ? 270 ALA D N   1 
ATOM   6756 C  CA  . ALA D 2 107 ? -33.828 11.484 65.773  1.00 25.95 ? 270 ALA D CA  1 
ATOM   6757 C  C   . ALA D 2 107 ? -33.094 12.751 66.196  1.00 26.43 ? 270 ALA D C   1 
ATOM   6758 O  O   . ALA D 2 107 ? -33.338 13.834 65.652  1.00 26.65 ? 270 ALA D O   1 
ATOM   6759 C  CB  . ALA D 2 107 ? -34.860 11.113 66.834  1.00 25.86 ? 270 ALA D CB  1 
ATOM   6760 N  N   . LYS D 2 108 ? -32.197 12.601 67.170  1.00 26.93 ? 271 LYS D N   1 
ATOM   6761 C  CA  . LYS D 2 108 ? -31.409 13.705 67.697  1.00 27.12 ? 271 LYS D CA  1 
ATOM   6762 C  C   . LYS D 2 108 ? -30.541 14.296 66.595  1.00 27.51 ? 271 LYS D C   1 
ATOM   6763 O  O   . LYS D 2 108 ? -30.373 15.518 66.521  1.00 27.47 ? 271 LYS D O   1 
ATOM   6764 C  CB  . LYS D 2 108 ? -30.531 13.240 68.860  1.00 27.02 ? 271 LYS D CB  1 
ATOM   6765 C  CG  . LYS D 2 108 ? -31.269 12.677 70.054  1.00 26.89 ? 271 LYS D CG  1 
ATOM   6766 C  CD  . LYS D 2 108 ? -31.708 13.747 71.021  1.00 27.75 ? 271 LYS D CD  1 
ATOM   6767 C  CE  . LYS D 2 108 ? -32.323 13.120 72.264  1.00 28.93 ? 271 LYS D CE  1 
ATOM   6768 N  NZ  . LYS D 2 108 ? -32.615 14.142 73.303  1.00 29.72 ? 271 LYS D NZ  1 
ATOM   6769 N  N   . LYS D 2 109 ? -30.000 13.423 65.744  1.00 27.89 ? 272 LYS D N   1 
ATOM   6770 C  CA  . LYS D 2 109 ? -29.181 13.850 64.615  1.00 28.52 ? 272 LYS D CA  1 
ATOM   6771 C  C   . LYS D 2 109 ? -29.992 14.649 63.612  1.00 29.10 ? 272 LYS D C   1 
ATOM   6772 O  O   . LYS D 2 109 ? -29.497 15.624 63.063  1.00 29.26 ? 272 LYS D O   1 
ATOM   6773 C  CB  . LYS D 2 109 ? -28.522 12.664 63.927  1.00 28.34 ? 272 LYS D CB  1 
ATOM   6774 C  CG  . LYS D 2 109 ? -27.166 12.302 64.489  1.00 28.62 ? 272 LYS D CG  1 
ATOM   6775 C  CD  . LYS D 2 109 ? -26.537 11.167 63.683  1.00 28.62 ? 272 LYS D CD  1 
ATOM   6776 C  CE  . LYS D 2 109 ? -25.176 10.768 64.240  1.00 28.52 ? 272 LYS D CE  1 
ATOM   6777 N  NZ  . LYS D 2 109 ? -24.808 9.380  63.847  1.00 28.40 ? 272 LYS D NZ  1 
ATOM   6778 N  N   . ALA D 2 110 ? -31.236 14.237 63.378  1.00 29.98 ? 273 ALA D N   1 
ATOM   6779 C  CA  . ALA D 2 110 ? -32.138 14.982 62.502  1.00 30.76 ? 273 ALA D CA  1 
ATOM   6780 C  C   . ALA D 2 110 ? -32.476 16.321 63.140  1.00 31.43 ? 273 ALA D C   1 
ATOM   6781 O  O   . ALA D 2 110 ? -32.556 17.340 62.455  1.00 31.47 ? 273 ALA D O   1 
ATOM   6782 C  CB  . ALA D 2 110 ? -33.399 14.189 62.227  1.00 30.61 ? 273 ALA D CB  1 
ATOM   6783 N  N   . GLU D 2 111 ? -32.659 16.315 64.458  1.00 32.32 ? 274 GLU D N   1 
ATOM   6784 C  CA  . GLU D 2 111 ? -32.933 17.543 65.192  1.00 33.50 ? 274 GLU D CA  1 
ATOM   6785 C  C   . GLU D 2 111 ? -31.742 18.504 65.132  1.00 33.79 ? 274 GLU D C   1 
ATOM   6786 O  O   . GLU D 2 111 ? -31.908 19.700 64.895  1.00 33.81 ? 274 GLU D O   1 
ATOM   6787 C  CB  . GLU D 2 111 ? -33.325 17.240 66.641  1.00 33.35 ? 274 GLU D CB  1 
ATOM   6788 C  CG  . GLU D 2 111 ? -34.066 18.402 67.317  1.00 34.33 ? 274 GLU D CG  1 
ATOM   6789 C  CD  . GLU D 2 111 ? -34.632 18.058 68.692  1.00 34.59 ? 274 GLU D CD  1 
ATOM   6790 O  OE1 . GLU D 2 111 ? -34.736 16.851 69.034  1.00 35.25 ? 274 GLU D OE1 1 
ATOM   6791 O  OE2 . GLU D 2 111 ? -34.979 19.012 69.431  1.00 35.88 ? 274 GLU D OE2 1 
ATOM   6792 N  N   . LEU D 2 112 ? -30.543 17.968 65.331  1.00 34.55 ? 275 LEU D N   1 
ATOM   6793 C  CA  . LEU D 2 112 ? -29.322 18.750 65.229  1.00 35.30 ? 275 LEU D CA  1 
ATOM   6794 C  C   . LEU D 2 112 ? -29.211 19.415 63.855  1.00 36.09 ? 275 LEU D C   1 
ATOM   6795 O  O   . LEU D 2 112 ? -28.789 20.564 63.743  1.00 36.40 ? 275 LEU D O   1 
ATOM   6796 C  CB  . LEU D 2 112 ? -28.108 17.867 65.515  1.00 34.97 ? 275 LEU D CB  1 
ATOM   6797 C  CG  . LEU D 2 112 ? -26.708 18.481 65.476  1.00 34.99 ? 275 LEU D CG  1 
ATOM   6798 C  CD1 . LEU D 2 112 ? -26.604 19.749 66.318  1.00 34.65 ? 275 LEU D CD1 1 
ATOM   6799 C  CD2 . LEU D 2 112 ? -25.678 17.449 65.920  1.00 35.20 ? 275 LEU D CD2 1 
ATOM   6800 N  N   . GLU D 2 113 ? -29.616 18.691 62.820  1.00 36.90 ? 276 GLU D N   1 
ATOM   6801 C  CA  . GLU D 2 113 ? -29.561 19.182 61.456  1.00 37.82 ? 276 GLU D CA  1 
ATOM   6802 C  C   . GLU D 2 113 ? -30.563 20.327 61.215  1.00 38.12 ? 276 GLU D C   1 
ATOM   6803 O  O   . GLU D 2 113 ? -30.229 21.314 60.559  1.00 38.17 ? 276 GLU D O   1 
ATOM   6804 C  CB  . GLU D 2 113 ? -29.801 18.018 60.498  1.00 38.06 ? 276 GLU D CB  1 
ATOM   6805 C  CG  . GLU D 2 113 ? -29.711 18.364 59.020  1.00 39.85 ? 276 GLU D CG  1 
ATOM   6806 C  CD  . GLU D 2 113 ? -30.839 17.734 58.213  1.00 41.86 ? 276 GLU D CD  1 
ATOM   6807 O  OE1 . GLU D 2 113 ? -31.382 16.687 58.645  1.00 42.62 ? 276 GLU D OE1 1 
ATOM   6808 O  OE2 . GLU D 2 113 ? -31.189 18.297 57.150  1.00 42.65 ? 276 GLU D OE2 1 
ATOM   6809 N  N   . LYS D 2 114 ? -31.779 20.196 61.744  1.00 38.59 ? 277 LYS D N   1 
ATOM   6810 C  CA  . LYS D 2 114 ? -32.782 21.259 61.635  1.00 39.29 ? 277 LYS D CA  1 
ATOM   6811 C  C   . LYS D 2 114 ? -32.441 22.475 62.476  1.00 39.40 ? 277 LYS D C   1 
ATOM   6812 O  O   . LYS D 2 114 ? -32.831 23.587 62.134  1.00 39.50 ? 277 LYS D O   1 
ATOM   6813 C  CB  . LYS D 2 114 ? -34.179 20.770 62.014  1.00 39.16 ? 277 LYS D CB  1 
ATOM   6814 C  CG  . LYS D 2 114 ? -35.133 20.649 60.827  1.00 40.21 ? 277 LYS D CG  1 
ATOM   6815 C  CD  . LYS D 2 114 ? -36.549 20.254 61.278  1.00 40.41 ? 277 LYS D CD  1 
ATOM   6816 C  CE  . LYS D 2 114 ? -37.205 19.253 60.317  1.00 41.36 ? 277 LYS D CE  1 
ATOM   6817 N  NZ  . LYS D 2 114 ? -36.548 17.906 60.415  1.00 41.67 ? 277 LYS D NZ  1 
ATOM   6818 N  N   . THR D 2 115 ? -31.724 22.261 63.576  1.00 39.65 ? 278 THR D N   1 
ATOM   6819 C  CA  . THR D 2 115 ? -31.369 23.352 64.472  1.00 39.92 ? 278 THR D CA  1 
ATOM   6820 C  C   . THR D 2 115 ? -30.194 24.173 63.939  1.00 40.28 ? 278 THR D C   1 
ATOM   6821 O  O   . THR D 2 115 ? -30.138 25.382 64.152  1.00 40.10 ? 278 THR D O   1 
ATOM   6822 C  CB  . THR D 2 115 ? -31.116 22.833 65.896  1.00 39.81 ? 278 THR D CB  1 
ATOM   6823 O  OG1 . THR D 2 115 ? -32.324 22.248 66.387  1.00 39.80 ? 278 THR D OG1 1 
ATOM   6824 C  CG2 . THR D 2 115 ? -30.714 23.958 66.840  1.00 39.93 ? 278 THR D CG2 1 
ATOM   6825 N  N   . GLU D 2 116 ? -29.273 23.515 63.239  1.00 41.04 ? 279 GLU D N   1 
ATOM   6826 C  CA  . GLU D 2 116 ? -28.124 24.191 62.618  1.00 41.91 ? 279 GLU D CA  1 
ATOM   6827 C  C   . GLU D 2 116 ? -28.517 25.037 61.409  1.00 42.07 ? 279 GLU D C   1 
ATOM   6828 O  O   . GLU D 2 116 ? -27.983 26.131 61.219  1.00 42.16 ? 279 GLU D O   1 
ATOM   6829 C  CB  . GLU D 2 116 ? -27.035 23.192 62.227  1.00 41.68 ? 279 GLU D CB  1 
ATOM   6830 C  CG  . GLU D 2 116 ? -26.028 22.923 63.322  1.00 42.47 ? 279 GLU D CG  1 
ATOM   6831 C  CD  . GLU D 2 116 ? -24.917 21.982 62.882  1.00 42.91 ? 279 GLU D CD  1 
ATOM   6832 O  OE1 . GLU D 2 116 ? -25.168 20.755 62.773  1.00 43.74 ? 279 GLU D OE1 1 
ATOM   6833 O  OE2 . GLU D 2 116 ? -23.784 22.470 62.663  1.00 44.41 ? 279 GLU D OE2 1 
ATOM   6834 N  N   . ALA D 2 117 ? -29.436 24.518 60.594  1.00 42.44 ? 280 ALA D N   1 
ATOM   6835 C  CA  . ALA D 2 117 ? -29.998 25.259 59.469  1.00 42.75 ? 280 ALA D CA  1 
ATOM   6836 C  C   . ALA D 2 117 ? -30.850 26.410 59.994  1.00 43.01 ? 280 ALA D C   1 
ATOM   6837 O  O   . ALA D 2 117 ? -30.792 27.525 59.479  1.00 43.05 ? 280 ALA D O   1 
ATOM   6838 C  CB  . ALA D 2 117 ? -30.822 24.335 58.585  1.00 42.76 ? 280 ALA D CB  1 
ATOM   6839 N  N   . ASP D 2 118 ? -31.625 26.116 61.035  1.00 43.53 ? 281 ASP D N   1 
ATOM   6840 C  CA  . ASP D 2 118 ? -32.410 27.096 61.777  1.00 44.04 ? 281 ASP D CA  1 
ATOM   6841 C  C   . ASP D 2 118 ? -31.533 28.265 62.229  1.00 44.36 ? 281 ASP D C   1 
ATOM   6842 O  O   . ASP D 2 118 ? -31.977 29.415 62.238  1.00 44.42 ? 281 ASP D O   1 
ATOM   6843 C  CB  . ASP D 2 118 ? -33.033 26.412 63.001  1.00 44.14 ? 281 ASP D CB  1 
ATOM   6844 C  CG  . ASP D 2 118 ? -34.427 26.921 63.327  1.00 44.47 ? 281 ASP D CG  1 
ATOM   6845 O  OD1 . ASP D 2 118 ? -34.569 28.129 63.623  1.00 45.11 ? 281 ASP D OD1 1 
ATOM   6846 O  OD2 . ASP D 2 118 ? -35.377 26.104 63.313  1.00 44.19 ? 281 ASP D OD2 1 
ATOM   6847 N  N   . LEU D 2 119 ? -30.290 27.953 62.595  1.00 44.85 ? 282 LEU D N   1 
ATOM   6848 C  CA  . LEU D 2 119 ? -29.310 28.942 63.046  1.00 45.43 ? 282 LEU D CA  1 
ATOM   6849 C  C   . LEU D 2 119 ? -28.691 29.731 61.887  1.00 46.19 ? 282 LEU D C   1 
ATOM   6850 O  O   . LEU D 2 119 ? -28.614 30.963 61.942  1.00 46.38 ? 282 LEU D O   1 
ATOM   6851 C  CB  . LEU D 2 119 ? -28.211 28.259 63.862  1.00 45.15 ? 282 LEU D CB  1 
ATOM   6852 C  CG  . LEU D 2 119 ? -26.960 29.044 64.258  1.00 44.52 ? 282 LEU D CG  1 
ATOM   6853 C  CD1 . LEU D 2 119 ? -27.237 29.979 65.415  1.00 44.11 ? 282 LEU D CD1 1 
ATOM   6854 C  CD2 . LEU D 2 119 ? -25.860 28.080 64.613  1.00 43.79 ? 282 LEU D CD2 1 
ATOM   6855 N  N   . LYS D 2 120 ? -28.252 29.018 60.849  1.00 46.92 ? 283 LYS D N   1 
ATOM   6856 C  CA  . LYS D 2 120 ? -27.631 29.633 59.674  1.00 47.65 ? 283 LYS D CA  1 
ATOM   6857 C  C   . LYS D 2 120 ? -28.582 30.619 59.026  1.00 48.08 ? 283 LYS D C   1 
ATOM   6858 O  O   . LYS D 2 120 ? -28.159 31.654 58.517  1.00 47.97 ? 283 LYS D O   1 
ATOM   6859 C  CB  . LYS D 2 120 ? -27.211 28.567 58.665  1.00 47.58 ? 283 LYS D CB  1 
ATOM   6860 C  CG  . LYS D 2 120 ? -26.200 29.040 57.621  1.00 47.88 ? 283 LYS D CG  1 
ATOM   6861 C  CD  . LYS D 2 120 ? -25.549 27.857 56.890  1.00 47.95 ? 283 LYS D CD  1 
ATOM   6862 C  CE  . LYS D 2 120 ? -24.284 27.357 57.595  1.00 48.05 ? 283 LYS D CE  1 
ATOM   6863 N  NZ  . LYS D 2 120 ? -24.515 26.881 58.995  1.00 47.52 ? 283 LYS D NZ  1 
ATOM   6864 N  N   . LYS D 2 121 ? -29.868 30.286 59.064  1.00 48.94 ? 284 LYS D N   1 
ATOM   6865 C  CA  . LYS D 2 121 ? -30.911 31.180 58.590  1.00 49.94 ? 284 LYS D CA  1 
ATOM   6866 C  C   . LYS D 2 121 ? -31.067 32.384 59.521  1.00 50.38 ? 284 LYS D C   1 
ATOM   6867 O  O   . LYS D 2 121 ? -30.973 33.528 59.080  1.00 50.48 ? 284 LYS D O   1 
ATOM   6868 C  CB  . LYS D 2 121 ? -32.243 30.438 58.450  1.00 49.93 ? 284 LYS D CB  1 
ATOM   6869 C  CG  . LYS D 2 121 ? -33.327 31.271 57.797  1.00 50.64 ? 284 LYS D CG  1 
ATOM   6870 C  CD  . LYS D 2 121 ? -34.684 30.604 57.882  1.00 51.82 ? 284 LYS D CD  1 
ATOM   6871 C  CE  . LYS D 2 121 ? -35.716 31.398 57.093  1.00 51.94 ? 284 LYS D CE  1 
ATOM   6872 N  NZ  . LYS D 2 121 ? -37.103 30.936 57.360  1.00 52.15 ? 284 LYS D NZ  1 
ATOM   6873 N  N   . ALA D 2 122 ? -31.286 32.118 60.807  1.00 51.05 ? 285 ALA D N   1 
ATOM   6874 C  CA  . ALA D 2 122 ? -31.571 33.174 61.783  1.00 51.72 ? 285 ALA D CA  1 
ATOM   6875 C  C   . ALA D 2 122 ? -30.451 34.197 61.863  1.00 52.17 ? 285 ALA D C   1 
ATOM   6876 O  O   . ALA D 2 122 ? -30.673 35.351 62.242  1.00 52.21 ? 285 ALA D O   1 
ATOM   6877 C  CB  . ALA D 2 122 ? -31.835 32.575 63.158  1.00 51.68 ? 285 ALA D CB  1 
ATOM   6878 N  N   . VAL D 2 123 ? -29.251 33.768 61.485  1.00 52.78 ? 286 VAL D N   1 
ATOM   6879 C  CA  . VAL D 2 123 ? -28.063 34.604 61.599  1.00 53.38 ? 286 VAL D CA  1 
ATOM   6880 C  C   . VAL D 2 123 ? -28.023 35.721 60.523  1.00 54.00 ? 286 VAL D C   1 
ATOM   6881 O  O   . VAL D 2 123 ? -27.071 36.512 60.460  1.00 54.14 ? 286 VAL D O   1 
ATOM   6882 C  CB  . VAL D 2 123 ? -26.776 33.726 61.693  1.00 53.20 ? 286 VAL D CB  1 
ATOM   6883 C  CG1 . VAL D 2 123 ? -26.103 33.540 60.331  1.00 53.42 ? 286 VAL D CG1 1 
ATOM   6884 C  CG2 . VAL D 2 123 ? -25.823 34.295 62.714  1.00 52.83 ? 286 VAL D CG2 1 
ATOM   6885 N  N   . ASN D 2 124 ? -29.068 35.774 59.690  1.00 54.62 ? 287 ASN D N   1 
ATOM   6886 C  CA  . ASN D 2 124 ? -29.362 36.940 58.846  1.00 55.26 ? 287 ASN D CA  1 
ATOM   6887 C  C   . ASN D 2 124 ? -30.801 37.399 59.094  1.00 55.79 ? 287 ASN D C   1 
ATOM   6888 O  O   . ASN D 2 124 ? -31.705 37.053 58.327  1.00 55.71 ? 287 ASN D O   1 
ATOM   6889 C  CB  . ASN D 2 124 ? -29.184 36.638 57.351  1.00 55.15 ? 287 ASN D CB  1 
ATOM   6890 C  CG  . ASN D 2 124 ? -28.109 35.609 57.072  1.00 55.26 ? 287 ASN D CG  1 
ATOM   6891 O  OD1 . ASN D 2 124 ? -28.330 34.674 56.305  1.00 55.59 ? 287 ASN D OD1 1 
ATOM   6892 N  ND2 . ASN D 2 124 ? -26.940 35.776 57.677  1.00 55.01 ? 287 ASN D ND2 1 
ATOM   6893 N  N   . GLU D 2 125 ? -31.012 38.159 60.171  1.00 56.49 ? 288 GLU D N   1 
ATOM   6894 C  CA  . GLU D 2 125 ? -32.362 38.628 60.544  1.00 57.14 ? 288 GLU D CA  1 
ATOM   6895 C  C   . GLU D 2 125 ? -32.453 40.125 60.870  1.00 57.25 ? 288 GLU D C   1 
ATOM   6896 O  O   . GLU D 2 125 ? -33.236 40.844 60.242  1.00 57.33 ? 288 GLU D O   1 
ATOM   6897 C  CB  . GLU D 2 125 ? -32.944 37.803 61.708  1.00 57.31 ? 288 GLU D CB  1 
ATOM   6898 C  CG  . GLU D 2 125 ? -33.552 36.448 61.311  1.00 58.02 ? 288 GLU D CG  1 
ATOM   6899 C  CD  . GLU D 2 125 ? -34.744 36.551 60.354  1.00 58.61 ? 288 GLU D CD  1 
ATOM   6900 O  OE1 . GLU D 2 125 ? -35.403 37.617 60.298  1.00 58.70 ? 288 GLU D OE1 1 
ATOM   6901 O  OE2 . GLU D 2 125 ? -35.022 35.548 59.660  1.00 58.72 ? 288 GLU D OE2 1 
ATOM   6902 O  OXT . GLU D 2 125 ? -31.775 40.647 61.765  1.00 57.29 ? 288 GLU D OXT 1 
HETATM 6903 C  C1  . NAG E 3 .   ? -17.884 14.452 52.179  1.00 57.28 ? 345 NAG A C1  1 
HETATM 6904 C  C2  . NAG E 3 .   ? -18.191 13.910 50.766  1.00 59.32 ? 345 NAG A C2  1 
HETATM 6905 C  C3  . NAG E 3 .   ? -19.669 14.047 50.319  1.00 59.59 ? 345 NAG A C3  1 
HETATM 6906 C  C4  . NAG E 3 .   ? -20.676 13.735 51.429  1.00 59.62 ? 345 NAG A C4  1 
HETATM 6907 C  C5  . NAG E 3 .   ? -20.241 14.405 52.743  1.00 59.97 ? 345 NAG A C5  1 
HETATM 6908 C  C6  . NAG E 3 .   ? -21.163 14.002 53.892  1.00 60.98 ? 345 NAG A C6  1 
HETATM 6909 C  C7  . NAG E 3 .   ? -16.372 13.949 49.107  1.00 62.13 ? 345 NAG A C7  1 
HETATM 6910 C  C8  . NAG E 3 .   ? -15.060 14.662 48.921  1.00 62.27 ? 345 NAG A C8  1 
HETATM 6911 N  N2  . NAG E 3 .   ? -17.312 14.583 49.821  1.00 60.62 ? 345 NAG A N2  1 
HETATM 6912 O  O3  . NAG E 3 .   ? -19.991 13.222 49.211  1.00 59.06 ? 345 NAG A O3  1 
HETATM 6913 O  O4  . NAG E 3 .   ? -21.980 14.121 51.017  1.00 58.00 ? 345 NAG A O4  1 
HETATM 6914 O  O5  . NAG E 3 .   ? -18.900 14.054 53.092  1.00 58.86 ? 345 NAG A O5  1 
HETATM 6915 O  O6  . NAG E 3 .   ? -20.842 12.693 54.322  1.00 61.44 ? 345 NAG A O6  1 
HETATM 6916 O  O7  . NAG E 3 .   ? -16.536 12.836 48.597  1.00 62.59 ? 345 NAG A O7  1 
HETATM 6917 C  C   . CO3 F 4 .   ? -5.295  35.446 41.055  1.00 21.36 ? 346 CO3 A C   1 
HETATM 6918 O  O1  . CO3 F 4 .   ? -5.515  36.374 41.946  1.00 21.07 ? 346 CO3 A O1  1 
HETATM 6919 O  O2  . CO3 F 4 .   ? -4.494  35.694 40.057  1.00 21.25 ? 346 CO3 A O2  1 
HETATM 6920 O  O3  . CO3 F 4 .   ? -5.884  34.288 41.159  1.00 21.71 ? 346 CO3 A O3  1 
HETATM 6921 FE FE  . FE  G 5 .   ? -4.380  37.758 41.716  1.00 18.58 ? 347 FE  A FE  1 
HETATM 6922 S  S   . SO4 H 6 .   ? 10.100  51.179 20.504  1.00 27.81 ? 348 SO4 A S   1 
HETATM 6923 O  O1  . SO4 H 6 .   ? 10.093  52.267 19.525  1.00 25.89 ? 348 SO4 A O1  1 
HETATM 6924 O  O2  . SO4 H 6 .   ? 9.130   51.404 21.573  1.00 26.05 ? 348 SO4 A O2  1 
HETATM 6925 O  O3  . SO4 H 6 .   ? 11.450  51.065 21.063  1.00 26.43 ? 348 SO4 A O3  1 
HETATM 6926 O  O4  . SO4 H 6 .   ? 9.711   49.936 19.839  1.00 27.09 ? 348 SO4 A O4  1 
HETATM 6927 S  S   . SO4 I 6 .   ? -9.282  49.750 48.410  1.00 73.44 ? 349 SO4 A S   1 
HETATM 6928 O  O1  . SO4 I 6 .   ? -10.042 48.593 48.894  1.00 73.33 ? 349 SO4 A O1  1 
HETATM 6929 O  O2  . SO4 I 6 .   ? -8.163  49.264 47.617  1.00 73.59 ? 349 SO4 A O2  1 
HETATM 6930 O  O3  . SO4 I 6 .   ? -10.137 50.585 47.569  1.00 73.50 ? 349 SO4 A O3  1 
HETATM 6931 O  O4  . SO4 I 6 .   ? -8.766  50.563 49.516  1.00 73.17 ? 349 SO4 A O4  1 
HETATM 6932 S  S   . SO4 J 6 .   ? 6.859   59.911 24.778  1.00 72.21 ? 350 SO4 A S   1 
HETATM 6933 O  O1  . SO4 J 6 .   ? 7.129   58.484 24.618  1.00 72.34 ? 350 SO4 A O1  1 
HETATM 6934 O  O2  . SO4 J 6 .   ? 7.087   60.255 26.180  1.00 72.07 ? 350 SO4 A O2  1 
HETATM 6935 O  O3  . SO4 J 6 .   ? 5.469   60.197 24.414  1.00 72.42 ? 350 SO4 A O3  1 
HETATM 6936 O  O4  . SO4 J 6 .   ? 7.745   60.685 23.909  1.00 71.67 ? 350 SO4 A O4  1 
HETATM 6937 C  C1  . NAG K 3 .   ? 17.984  60.494 92.565  1.00 57.74 ? 345 NAG B C1  1 
HETATM 6938 C  C2  . NAG K 3 .   ? 18.352  61.006 91.156  1.00 60.16 ? 345 NAG B C2  1 
HETATM 6939 C  C3  . NAG K 3 .   ? 19.866  60.998 90.825  1.00 60.27 ? 345 NAG B C3  1 
HETATM 6940 C  C4  . NAG K 3 .   ? 20.778  61.343 92.004  1.00 60.27 ? 345 NAG B C4  1 
HETATM 6941 C  C5  . NAG K 3 .   ? 20.281  60.665 93.294  1.00 60.35 ? 345 NAG B C5  1 
HETATM 6942 C  C6  . NAG K 3 .   ? 21.101  61.081 94.519  1.00 61.23 ? 345 NAG B C6  1 
HETATM 6943 C  C7  . NAG K 3 .   ? 16.578  60.671 89.472  1.00 63.55 ? 345 NAG B C7  1 
HETATM 6944 C  C8  . NAG K 3 .   ? 15.506  59.675 89.125  1.00 63.83 ? 345 NAG B C8  1 
HETATM 6945 N  N2  . NAG K 3 .   ? 17.628  60.211 90.171  1.00 61.66 ? 345 NAG B N2  1 
HETATM 6946 O  O3  . NAG K 3 .   ? 20.190  61.885 89.766  1.00 59.86 ? 345 NAG B O3  1 
HETATM 6947 O  O4  . NAG K 3 .   ? 22.112  60.984 91.669  1.00 59.34 ? 345 NAG B O4  1 
HETATM 6948 O  O5  . NAG K 3 .   ? 18.908  60.966 93.539  1.00 59.11 ? 345 NAG B O5  1 
HETATM 6949 O  O6  . NAG K 3 .   ? 20.825  62.426 94.868  1.00 61.28 ? 345 NAG B O6  1 
HETATM 6950 O  O7  . NAG K 3 .   ? 16.452  61.844 89.100  1.00 64.35 ? 345 NAG B O7  1 
HETATM 6951 C  C   . CO3 L 4 .   ? 5.206   39.774 81.446  1.00 21.59 ? 346 CO3 B C   1 
HETATM 6952 O  O1  . CO3 L 4 .   ? 5.428   38.952 82.430  1.00 21.27 ? 346 CO3 B O1  1 
HETATM 6953 O  O2  . CO3 L 4 .   ? 4.401   39.421 80.492  1.00 21.41 ? 346 CO3 B O2  1 
HETATM 6954 O  O3  . CO3 L 4 .   ? 5.795   40.931 81.402  1.00 22.25 ? 346 CO3 B O3  1 
HETATM 6955 FE FE  . FE  M 5 .   ? 4.438   37.411 82.081  1.00 18.71 ? 347 FE  B FE  1 
HETATM 6956 S  S   . SO4 N 6 .   ? -10.090 24.014 60.989  1.00 27.52 ? 348 SO4 B S   1 
HETATM 6957 O  O1  . SO4 N 6 .   ? -10.280 23.068 59.890  1.00 26.75 ? 348 SO4 B O1  1 
HETATM 6958 O  O2  . SO4 N 6 .   ? -9.165  23.474 61.980  1.00 26.99 ? 348 SO4 B O2  1 
HETATM 6959 O  O3  . SO4 N 6 .   ? -11.397 24.268 61.591  1.00 26.41 ? 348 SO4 B O3  1 
HETATM 6960 O  O4  . SO4 N 6 .   ? -9.500  25.254 60.491  1.00 26.74 ? 348 SO4 B O4  1 
HETATM 6961 S  S   . SO4 O 6 .   ? 9.232   25.292 88.715  1.00 65.54 ? 349 SO4 B S   1 
HETATM 6962 O  O1  . SO4 O 6 .   ? 9.964   26.475 89.178  1.00 65.83 ? 349 SO4 B O1  1 
HETATM 6963 O  O2  . SO4 O 6 .   ? 7.930   25.700 88.202  1.00 65.68 ? 349 SO4 B O2  1 
HETATM 6964 O  O3  . SO4 O 6 .   ? 10.009  24.664 87.654  1.00 65.74 ? 349 SO4 B O3  1 
HETATM 6965 O  O4  . SO4 O 6 .   ? 9.024   24.330 89.801  1.00 65.42 ? 349 SO4 B O4  1 
HETATM 6966 S  S   . SO4 P 6 .   ? -6.837  15.188 65.145  1.00 63.26 ? 350 SO4 B S   1 
HETATM 6967 O  O1  . SO4 P 6 .   ? -7.570  16.447 65.239  1.00 63.62 ? 350 SO4 B O1  1 
HETATM 6968 O  O2  . SO4 P 6 .   ? -6.344  14.835 66.477  1.00 63.12 ? 350 SO4 B O2  1 
HETATM 6969 O  O3  . SO4 P 6 .   ? -5.699  15.338 64.237  1.00 63.77 ? 350 SO4 B O3  1 
HETATM 6970 O  O4  . SO4 P 6 .   ? -7.739  14.158 64.632  1.00 62.66 ? 350 SO4 B O4  1 
HETATM 6971 ZN ZN  . ZN  Q 7 .   ? 15.776  34.285 11.758  1.00 20.00 ? 502 ZN  C ZN  1 
HETATM 6972 ZN ZN  . ZN  R 7 .   ? -15.877 40.759 52.169  1.00 16.70 ? 501 ZN  D ZN  1 
HETATM 6973 O  O   . HOH S 8 .   ? 21.676  37.505 36.355  1.00 2.58  ? 406 HOH A O   1 
HETATM 6974 O  O   . HOH S 8 .   ? -0.030  30.464 47.310  1.00 21.29 ? 407 HOH A O   1 
HETATM 6975 O  O   . HOH S 8 .   ? 10.975  44.463 21.836  1.00 15.68 ? 410 HOH A O   1 
HETATM 6976 O  O   . HOH S 8 .   ? 6.490   41.898 36.486  1.00 17.16 ? 414 HOH A O   1 
HETATM 6977 O  O   . HOH S 8 .   ? 16.087  42.810 44.880  1.00 16.39 ? 416 HOH A O   1 
HETATM 6978 O  O   . HOH S 8 .   ? 11.972  53.646 22.505  1.00 45.66 ? 417 HOH A O   1 
HETATM 6979 O  O   . HOH S 8 .   ? 5.482   34.820 53.248  1.00 22.90 ? 418 HOH A O   1 
HETATM 6980 O  O   . HOH S 8 .   ? 0.606   45.687 31.380  1.00 15.08 ? 421 HOH A O   1 
HETATM 6981 O  O   . HOH T 8 .   ? -21.756 37.515 76.744  1.00 13.24 ? 405 HOH B O   1 
HETATM 6982 O  O   . HOH T 8 .   ? -0.069  44.766 87.649  1.00 24.59 ? 408 HOH B O   1 
HETATM 6983 O  O   . HOH T 8 .   ? -10.932 30.417 62.394  1.00 22.31 ? 409 HOH B O   1 
HETATM 6984 O  O   . HOH T 8 .   ? -6.449  33.427 76.981  1.00 15.25 ? 413 HOH B O   1 
HETATM 6985 O  O   . HOH T 8 .   ? -8.887  20.100 61.566  1.00 34.04 ? 415 HOH B O   1 
HETATM 6986 O  O   . HOH T 8 .   ? -1.590  19.424 68.230  1.00 29.79 ? 419 HOH B O   1 
HETATM 6987 O  O   . HOH T 8 .   ? -0.406  22.657 70.817  1.00 18.15 ? 422 HOH B O   1 
HETATM 6988 O  O   . HOH T 8 .   ? -5.247  46.705 75.024  1.00 17.70 ? 423 HOH B O   1 
HETATM 6989 O  O   . HOH T 8 .   ? -7.280  36.441 75.698  1.00 29.95 ? 424 HOH B O   1 
HETATM 6990 O  O   . HOH T 8 .   ? -16.083 32.324 85.216  1.00 13.24 ? 425 HOH B O   1 
HETATM 6991 O  O   . HOH U 8 .   ? 13.762  30.453 29.923  1.00 43.52 ? 402 HOH C O   1 
HETATM 6992 O  O   . HOH U 8 .   ? 17.918  36.111 31.015  1.00 11.54 ? 404 HOH C O   1 
HETATM 6993 O  O   . HOH U 8 .   ? 19.940  46.710 22.572  1.00 12.02 ? 412 HOH C O   1 
HETATM 6994 O  O   . HOH V 8 .   ? -13.584 44.942 70.632  1.00 33.43 ? 401 HOH D O   1 
HETATM 6995 O  O   . HOH V 8 .   ? -18.036 39.111 71.479  1.00 17.53 ? 403 HOH D O   1 
HETATM 6996 O  O   . HOH V 8 .   ? -19.866 28.352 62.960  1.00 6.24  ? 411 HOH D 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   GLY 1   1   ?   ?   ?   A . n 
A 1 2   ARG 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ARG 5   5   5   ARG ARG A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  GLU 16  16  16  GLU GLU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  TRP 23  23  23  TRP TRP A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  MET 27  27  27  MET MET A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  GLY 32  32  32  GLY GLY A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  TYR 83  83  83  TYR TYR A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 GLY 112 112 112 GLY GLY A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 CYS 116 116 116 CYS CYS A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 TRP 126 126 126 TRP TRP A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 TRP 139 139 139 TRP TRP A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 CYS 158 158 158 CYS CYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 CYS 171 171 171 CYS CYS A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 CYS 174 174 174 CYS CYS A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 CYS 182 182 182 CYS CYS A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 PHE 191 191 191 PHE PHE A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 CYS 199 199 199 CYS CYS A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ASP 206 206 206 ASP ASP A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 ILE 210 210 210 ILE ILE A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 TYR 228 228 228 TYR TYR A . n 
A 1 229 GLU 229 229 229 GLU GLU A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 CYS 232 232 232 CYS CYS A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 CYS 246 246 246 CYS CYS A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 ARG 250 250 250 ARG ARG A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 HIS 254 254 254 HIS HIS A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ALA 258 258 258 ALA ALA A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 TRP 269 269 269 TRP TRP A . n 
A 1 270 ASN 270 270 270 ASN ASN A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 GLN 274 274 274 GLN GLN A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 GLN 276 276 276 GLN GLN A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 PHE 287 287 287 PHE PHE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 PHE 290 290 290 PHE PHE A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 SER 294 294 294 SER SER A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 GLN 296 296 296 GLN GLN A . n 
A 1 297 LYS 297 297 297 LYS LYS A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 LYS 302 302 302 LYS LYS A . n 
A 1 303 ASP 303 303 303 ASP ASP A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 PRO 312 312 312 PRO PRO A . n 
A 1 313 PRO 313 313 313 PRO PRO A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 ASP 316 316 316 ASP ASP A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 GLY 318 318 318 GLY GLY A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 TYR 320 320 320 TYR TYR A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 TYR 325 325 325 TYR TYR A . n 
A 1 326 PHE 326 326 326 PHE PHE A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 ILE 329 329 329 ILE ILE A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LYS 334 334 ?   ?   ?   A . n 
A 1 335 SER 335 335 ?   ?   ?   A . n 
A 1 336 GLU 336 336 ?   ?   ?   A . n 
A 1 337 GLU 337 337 ?   ?   ?   A . n 
A 1 338 GLU 338 338 ?   ?   ?   A . n 
A 1 339 VAL 339 339 ?   ?   ?   A . n 
A 1 340 ALA 340 340 ?   ?   ?   A . n 
A 1 341 ALA 341 341 ?   ?   ?   A . n 
A 1 342 ARG 342 342 ?   ?   ?   A . n 
A 1 343 ARG 343 343 ?   ?   ?   A . n 
A 1 344 ALA 344 344 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   ARG 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   3   ARG ARG B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   ARG 5   5   5   ARG ARG B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   GLN 8   8   8   GLN GLN B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  CYS 10  10  10  CYS CYS B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  GLU 16  16  16  GLU GLU B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  CYS 20  20  20  CYS CYS B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  TRP 23  23  23  TRP TRP B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  MET 27  27  27  MET MET B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  ARG 29  29  29  ARG ARG B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  GLY 32  32  32  GLY GLY B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  CYS 37  37  37  CYS CYS B . n 
B 1 38  ILE 38  38  38  ILE ILE B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLN 45  45  45  GLN GLN B . n 
B 1 46  CYS 46  46  46  CYS CYS B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  GLU 52  52  52  GLU GLU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  TYR 66  66  66  TYR TYR B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  PRO 72  72  72  PRO PRO B . n 
B 1 73  TYR 73  73  73  TYR TYR B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  TYR 83  83  83  TYR TYR B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  GLN 88  88  88  GLN GLN B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  THR 91  91  91  THR THR B . n 
B 1 92  HIS 92  92  92  HIS HIS B . n 
B 1 93  TYR 93  93  93  TYR TYR B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LYS 101 101 101 LYS LYS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 GLN 106 106 106 GLN GLN B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 GLY 112 112 112 GLY GLY B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 LYS 114 114 114 LYS LYS B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 CYS 116 116 116 CYS CYS B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 GLY 119 119 119 GLY GLY B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 TRP 126 126 126 TRP TRP B . n 
B 1 127 ASN 127 127 127 ASN ASN B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ARG 134 134 134 ARG ARG B . n 
B 1 135 PRO 135 135 135 PRO PRO B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 ASN 138 138 138 ASN ASN B . n 
B 1 139 TRP 139 139 139 TRP TRP B . n 
B 1 140 THR 140 140 140 THR THR B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 PRO 142 142 142 PRO PRO B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 PRO 145 145 145 PRO PRO B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 PHE 153 153 153 PHE PHE B . n 
B 1 154 PHE 154 154 154 PHE PHE B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 CYS 158 158 158 CYS CYS B . n 
B 1 159 VAL 159 159 159 VAL VAL B . n 
B 1 160 PRO 160 160 160 PRO PRO B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 ALA 162 162 162 ALA ALA B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 GLN 166 166 166 GLN GLN B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 ASN 169 169 169 ASN ASN B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 CYS 171 171 171 CYS CYS B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 CYS 174 174 174 CYS CYS B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 THR 177 177 177 THR THR B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 LYS 181 181 181 LYS LYS B . n 
B 1 182 CYS 182 182 182 CYS CYS B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 SER 186 186 186 SER SER B . n 
B 1 187 GLN 187 187 187 GLN GLN B . n 
B 1 188 GLU 188 188 188 GLU GLU B . n 
B 1 189 PRO 189 189 189 PRO PRO B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 PHE 191 191 191 PHE PHE B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 PHE 197 197 197 PHE PHE B . n 
B 1 198 LYS 198 198 198 LYS LYS B . n 
B 1 199 CYS 199 199 199 CYS CYS B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ARG 201 201 201 ARG ARG B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 GLY 203 203 203 GLY GLY B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 ASP 206 206 206 ASP ASP B . n 
B 1 207 VAL 207 207 207 VAL VAL B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 PHE 209 209 209 PHE PHE B . n 
B 1 210 ILE 210 210 210 ILE ILE B . n 
B 1 211 ARG 211 211 211 ARG ARG B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 GLU 222 222 222 GLU GLU B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 GLU 224 224 224 GLU GLU B . n 
B 1 225 ARG 225 225 225 ARG ARG B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 TYR 228 228 228 TYR TYR B . n 
B 1 229 GLU 229 229 229 GLU GLU B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 CYS 232 232 232 CYS CYS B . n 
B 1 233 PRO 233 233 233 PRO PRO B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 ARG 237 237 237 ARG ARG B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 VAL 240 240 240 VAL VAL B . n 
B 1 241 ASP 241 241 241 ASP ASP B . n 
B 1 242 LYS 242 242 242 LYS LYS B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 LYS 244 244 244 LYS LYS B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 CYS 246 246 246 CYS CYS B . n 
B 1 247 HIS 247 247 247 HIS HIS B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 ALA 249 249 249 ALA ALA B . n 
B 1 250 ARG 250 250 250 ARG ARG B . n 
B 1 251 VAL 251 251 251 VAL VAL B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 SER 253 253 253 SER SER B . n 
B 1 254 HIS 254 254 254 HIS HIS B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 ALA 258 258 258 ALA ALA B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 ALA 267 267 267 ALA ALA B . n 
B 1 268 ILE 268 268 268 ILE ILE B . n 
B 1 269 TRP 269 269 269 TRP TRP B . n 
B 1 270 ASN 270 270 270 ASN ASN B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 ARG 273 273 273 ARG ARG B . n 
B 1 274 GLN 274 274 274 GLN GLN B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 GLN 276 276 276 GLN GLN B . n 
B 1 277 GLU 277 277 277 GLU GLU B . n 
B 1 278 LYS 278 278 278 LYS LYS B . n 
B 1 279 PHE 279 279 279 PHE PHE B . n 
B 1 280 GLY 280 280 280 GLY GLY B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 ASP 282 282 282 ASP ASP B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 PHE 287 287 287 PHE PHE B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 PHE 290 290 290 PHE PHE B . n 
B 1 291 GLY 291 291 291 GLY GLY B . n 
B 1 292 SER 292 292 292 SER SER B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 SER 294 294 294 SER SER B . n 
B 1 295 GLY 295 295 295 GLY GLY B . n 
B 1 296 GLN 296 296 296 GLN GLN B . n 
B 1 297 LYS 297 297 297 LYS LYS B . n 
B 1 298 ASP 298 298 298 ASP ASP B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 PHE 301 301 301 PHE PHE B . n 
B 1 302 LYS 302 302 302 LYS LYS B . n 
B 1 303 ASP 303 303 303 ASP ASP B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 GLY 307 307 307 GLY GLY B . n 
B 1 308 PHE 308 308 308 PHE PHE B . n 
B 1 309 SER 309 309 309 SER SER B . n 
B 1 310 ARG 310 310 310 ARG ARG B . n 
B 1 311 VAL 311 311 311 VAL VAL B . n 
B 1 312 PRO 312 312 312 PRO PRO B . n 
B 1 313 PRO 313 313 313 PRO PRO B . n 
B 1 314 ARG 314 314 314 ARG ARG B . n 
B 1 315 ILE 315 315 315 ILE ILE B . n 
B 1 316 ASP 316 316 316 ASP ASP B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 GLY 318 318 318 GLY GLY B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 TYR 320 320 320 TYR TYR B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 GLY 322 322 322 GLY GLY B . n 
B 1 323 SER 323 323 323 SER SER B . n 
B 1 324 GLY 324 324 324 GLY GLY B . n 
B 1 325 TYR 325 325 325 TYR TYR B . n 
B 1 326 PHE 326 326 326 PHE PHE B . n 
B 1 327 THR 327 327 327 THR THR B . n 
B 1 328 ALA 328 328 328 ALA ALA B . n 
B 1 329 ILE 329 329 329 ILE ILE B . n 
B 1 330 GLN 330 330 330 GLN GLN B . n 
B 1 331 ASN 331 331 331 ASN ASN B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 LYS 334 334 ?   ?   ?   B . n 
B 1 335 SER 335 335 ?   ?   ?   B . n 
B 1 336 GLU 336 336 ?   ?   ?   B . n 
B 1 337 GLU 337 337 ?   ?   ?   B . n 
B 1 338 GLU 338 338 ?   ?   ?   B . n 
B 1 339 VAL 339 339 ?   ?   ?   B . n 
B 1 340 ALA 340 340 ?   ?   ?   B . n 
B 1 341 ALA 341 341 ?   ?   ?   B . n 
B 1 342 ARG 342 342 ?   ?   ?   B . n 
B 1 343 ARG 343 343 ?   ?   ?   B . n 
B 1 344 ALA 344 344 ?   ?   ?   B . n 
C 2 1   GLY 1   164 164 GLY GLY C . n 
C 2 2   SER 2   165 165 SER SER C . n 
C 2 3   HIS 3   166 166 HIS HIS C . n 
C 2 4   MET 4   167 167 MET MET C . n 
C 2 5   ASP 5   168 168 ASP ASP C . n 
C 2 6   ALA 6   169 169 ALA ALA C . n 
C 2 7   GLU 7   170 170 GLU GLU C . n 
C 2 8   GLU 8   171 171 GLU GLU C . n 
C 2 9   VAL 9   172 172 VAL VAL C . n 
C 2 10  ALA 10  173 173 ALA ALA C . n 
C 2 11  PRO 11  174 174 PRO PRO C . n 
C 2 12  GLN 12  175 175 GLN GLN C . n 
C 2 13  ALA 13  176 176 ALA ALA C . n 
C 2 14  LYS 14  177 177 LYS LYS C . n 
C 2 15  ILE 15  178 178 ILE ILE C . n 
C 2 16  ALA 16  179 179 ALA ALA C . n 
C 2 17  GLU 17  180 180 GLU GLU C . n 
C 2 18  LEU 18  181 181 LEU LEU C . n 
C 2 19  GLU 19  182 182 GLU GLU C . n 
C 2 20  ASN 20  183 183 ASN ASN C . n 
C 2 21  GLN 21  184 184 GLN GLN C . n 
C 2 22  VAL 22  185 185 VAL VAL C . n 
C 2 23  HIS 23  186 186 HIS HIS C . n 
C 2 24  ARG 24  187 187 ARG ARG C . n 
C 2 25  LEU 25  188 188 LEU LEU C . n 
C 2 26  GLU 26  189 189 GLU GLU C . n 
C 2 27  GLN 27  190 190 GLN GLN C . n 
C 2 28  GLU 28  191 191 GLU GLU C . n 
C 2 29  LEU 29  192 192 LEU LEU C . n 
C 2 30  LYS 30  193 193 LYS LYS C . n 
C 2 31  GLU 31  194 194 GLU GLU C . n 
C 2 32  ILE 32  195 195 ILE ILE C . n 
C 2 33  ASP 33  196 196 ASP ASP C . n 
C 2 34  GLU 34  197 197 GLU GLU C . n 
C 2 35  SER 35  198 ?   ?   ?   C . n 
C 2 36  GLU 36  199 ?   ?   ?   C . n 
C 2 37  SER 37  200 ?   ?   ?   C . n 
C 2 38  GLU 38  201 ?   ?   ?   C . n 
C 2 39  ASP 39  202 ?   ?   ?   C . n 
C 2 40  TYR 40  203 ?   ?   ?   C . n 
C 2 41  ALA 41  204 ?   ?   ?   C . n 
C 2 42  LYS 42  205 ?   ?   ?   C . n 
C 2 43  GLU 43  206 ?   ?   ?   C . n 
C 2 44  GLY 44  207 ?   ?   ?   C . n 
C 2 45  PHE 45  208 ?   ?   ?   C . n 
C 2 46  ARG 46  209 ?   ?   ?   C . n 
C 2 47  ALA 47  210 210 ALA ALA C . n 
C 2 48  PRO 48  211 211 PRO PRO C . n 
C 2 49  LEU 49  212 212 LEU LEU C . n 
C 2 50  GLN 50  213 213 GLN GLN C . n 
C 2 51  SER 51  214 214 SER SER C . n 
C 2 52  LYS 52  215 215 LYS LYS C . n 
C 2 53  LEU 53  216 216 LEU LEU C . n 
C 2 54  ASP 54  217 217 ASP ASP C . n 
C 2 55  ALA 55  218 218 ALA ALA C . n 
C 2 56  LYS 56  219 219 LYS LYS C . n 
C 2 57  LYS 57  220 220 LYS LYS C . n 
C 2 58  ALA 58  221 221 ALA ALA C . n 
C 2 59  LYS 59  222 222 LYS LYS C . n 
C 2 60  LEU 60  223 223 LEU LEU C . n 
C 2 61  SER 61  224 224 SER SER C . n 
C 2 62  LYS 62  225 225 LYS LYS C . n 
C 2 63  LEU 63  226 226 LEU LEU C . n 
C 2 64  GLU 64  227 227 GLU GLU C . n 
C 2 65  GLU 65  228 228 GLU GLU C . n 
C 2 66  LEU 66  229 229 LEU LEU C . n 
C 2 67  SER 67  230 230 SER SER C . n 
C 2 68  ASP 68  231 231 ASP ASP C . n 
C 2 69  LYS 69  232 232 LYS LYS C . n 
C 2 70  ILE 70  233 233 ILE ILE C . n 
C 2 71  ASP 71  234 234 ASP ASP C . n 
C 2 72  GLU 72  235 235 GLU GLU C . n 
C 2 73  LEU 73  236 236 LEU LEU C . n 
C 2 74  ASP 74  237 237 ASP ASP C . n 
C 2 75  ALA 75  238 238 ALA ALA C . n 
C 2 76  GLU 76  239 239 GLU GLU C . n 
C 2 77  ILE 77  240 240 ILE ILE C . n 
C 2 78  ALA 78  241 241 ALA ALA C . n 
C 2 79  LYS 79  242 242 LYS LYS C . n 
C 2 80  LEU 80  243 243 LEU LEU C . n 
C 2 81  GLU 81  244 244 GLU GLU C . n 
C 2 82  ASP 82  245 245 ASP ASP C . n 
C 2 83  GLN 83  246 246 GLN GLN C . n 
C 2 84  LEU 84  247 247 LEU LEU C . n 
C 2 85  LYS 85  248 248 LYS LYS C . n 
C 2 86  ALA 86  249 249 ALA ALA C . n 
C 2 87  ALA 87  250 250 ALA ALA C . n 
C 2 88  GLU 88  251 251 GLU GLU C . n 
C 2 89  GLU 89  252 252 GLU GLU C . n 
C 2 90  ASN 90  253 ?   ?   ?   C . n 
C 2 91  ASN 91  254 ?   ?   ?   C . n 
C 2 92  ASN 92  255 ?   ?   ?   C . n 
C 2 93  VAL 93  256 ?   ?   ?   C . n 
C 2 94  GLU 94  257 257 GLU GLU C . n 
C 2 95  ASP 95  258 258 ASP ASP C . n 
C 2 96  TYR 96  259 259 TYR TYR C . n 
C 2 97  PHE 97  260 260 PHE PHE C . n 
C 2 98  LYS 98  261 261 LYS LYS C . n 
C 2 99  GLU 99  262 262 GLU GLU C . n 
C 2 100 GLY 100 263 263 GLY GLY C . n 
C 2 101 LEU 101 264 264 LEU LEU C . n 
C 2 102 GLU 102 265 265 GLU GLU C . n 
C 2 103 LYS 103 266 266 LYS LYS C . n 
C 2 104 THR 104 267 267 THR THR C . n 
C 2 105 ILE 105 268 268 ILE ILE C . n 
C 2 106 ALA 106 269 269 ALA ALA C . n 
C 2 107 ALA 107 270 270 ALA ALA C . n 
C 2 108 LYS 108 271 271 LYS LYS C . n 
C 2 109 LYS 109 272 272 LYS LYS C . n 
C 2 110 ALA 110 273 273 ALA ALA C . n 
C 2 111 GLU 111 274 274 GLU GLU C . n 
C 2 112 LEU 112 275 275 LEU LEU C . n 
C 2 113 GLU 113 276 276 GLU GLU C . n 
C 2 114 LYS 114 277 277 LYS LYS C . n 
C 2 115 THR 115 278 278 THR THR C . n 
C 2 116 GLU 116 279 279 GLU GLU C . n 
C 2 117 ALA 117 280 280 ALA ALA C . n 
C 2 118 ASP 118 281 281 ASP ASP C . n 
C 2 119 LEU 119 282 282 LEU LEU C . n 
C 2 120 LYS 120 283 283 LYS LYS C . n 
C 2 121 LYS 121 284 284 LYS LYS C . n 
C 2 122 ALA 122 285 285 ALA ALA C . n 
C 2 123 VAL 123 286 286 VAL VAL C . n 
C 2 124 ASN 124 287 287 ASN ASN C . n 
C 2 125 GLU 125 288 288 GLU GLU C . n 
D 2 1   GLY 1   164 164 GLY GLY D . n 
D 2 2   SER 2   165 165 SER SER D . n 
D 2 3   HIS 3   166 166 HIS HIS D . n 
D 2 4   MET 4   167 167 MET MET D . n 
D 2 5   ASP 5   168 168 ASP ASP D . n 
D 2 6   ALA 6   169 169 ALA ALA D . n 
D 2 7   GLU 7   170 170 GLU GLU D . n 
D 2 8   GLU 8   171 171 GLU GLU D . n 
D 2 9   VAL 9   172 172 VAL VAL D . n 
D 2 10  ALA 10  173 173 ALA ALA D . n 
D 2 11  PRO 11  174 174 PRO PRO D . n 
D 2 12  GLN 12  175 175 GLN GLN D . n 
D 2 13  ALA 13  176 176 ALA ALA D . n 
D 2 14  LYS 14  177 177 LYS LYS D . n 
D 2 15  ILE 15  178 178 ILE ILE D . n 
D 2 16  ALA 16  179 179 ALA ALA D . n 
D 2 17  GLU 17  180 180 GLU GLU D . n 
D 2 18  LEU 18  181 181 LEU LEU D . n 
D 2 19  GLU 19  182 182 GLU GLU D . n 
D 2 20  ASN 20  183 183 ASN ASN D . n 
D 2 21  GLN 21  184 184 GLN GLN D . n 
D 2 22  VAL 22  185 185 VAL VAL D . n 
D 2 23  HIS 23  186 186 HIS HIS D . n 
D 2 24  ARG 24  187 187 ARG ARG D . n 
D 2 25  LEU 25  188 188 LEU LEU D . n 
D 2 26  GLU 26  189 189 GLU GLU D . n 
D 2 27  GLN 27  190 190 GLN GLN D . n 
D 2 28  GLU 28  191 191 GLU GLU D . n 
D 2 29  LEU 29  192 192 LEU LEU D . n 
D 2 30  LYS 30  193 193 LYS LYS D . n 
D 2 31  GLU 31  194 194 GLU GLU D . n 
D 2 32  ILE 32  195 195 ILE ILE D . n 
D 2 33  ASP 33  196 196 ASP ASP D . n 
D 2 34  GLU 34  197 197 GLU GLU D . n 
D 2 35  SER 35  198 ?   ?   ?   D . n 
D 2 36  GLU 36  199 ?   ?   ?   D . n 
D 2 37  SER 37  200 ?   ?   ?   D . n 
D 2 38  GLU 38  201 ?   ?   ?   D . n 
D 2 39  ASP 39  202 ?   ?   ?   D . n 
D 2 40  TYR 40  203 ?   ?   ?   D . n 
D 2 41  ALA 41  204 ?   ?   ?   D . n 
D 2 42  LYS 42  205 ?   ?   ?   D . n 
D 2 43  GLU 43  206 ?   ?   ?   D . n 
D 2 44  GLY 44  207 ?   ?   ?   D . n 
D 2 45  PHE 45  208 ?   ?   ?   D . n 
D 2 46  ARG 46  209 ?   ?   ?   D . n 
D 2 47  ALA 47  210 210 ALA ALA D . n 
D 2 48  PRO 48  211 211 PRO PRO D . n 
D 2 49  LEU 49  212 212 LEU LEU D . n 
D 2 50  GLN 50  213 213 GLN GLN D . n 
D 2 51  SER 51  214 214 SER SER D . n 
D 2 52  LYS 52  215 215 LYS LYS D . n 
D 2 53  LEU 53  216 216 LEU LEU D . n 
D 2 54  ASP 54  217 217 ASP ASP D . n 
D 2 55  ALA 55  218 218 ALA ALA D . n 
D 2 56  LYS 56  219 219 LYS LYS D . n 
D 2 57  LYS 57  220 220 LYS LYS D . n 
D 2 58  ALA 58  221 221 ALA ALA D . n 
D 2 59  LYS 59  222 222 LYS LYS D . n 
D 2 60  LEU 60  223 223 LEU LEU D . n 
D 2 61  SER 61  224 224 SER SER D . n 
D 2 62  LYS 62  225 225 LYS LYS D . n 
D 2 63  LEU 63  226 226 LEU LEU D . n 
D 2 64  GLU 64  227 227 GLU GLU D . n 
D 2 65  GLU 65  228 228 GLU GLU D . n 
D 2 66  LEU 66  229 229 LEU LEU D . n 
D 2 67  SER 67  230 230 SER SER D . n 
D 2 68  ASP 68  231 231 ASP ASP D . n 
D 2 69  LYS 69  232 232 LYS LYS D . n 
D 2 70  ILE 70  233 233 ILE ILE D . n 
D 2 71  ASP 71  234 234 ASP ASP D . n 
D 2 72  GLU 72  235 235 GLU GLU D . n 
D 2 73  LEU 73  236 236 LEU LEU D . n 
D 2 74  ASP 74  237 237 ASP ASP D . n 
D 2 75  ALA 75  238 238 ALA ALA D . n 
D 2 76  GLU 76  239 239 GLU GLU D . n 
D 2 77  ILE 77  240 240 ILE ILE D . n 
D 2 78  ALA 78  241 241 ALA ALA D . n 
D 2 79  LYS 79  242 242 LYS LYS D . n 
D 2 80  LEU 80  243 243 LEU LEU D . n 
D 2 81  GLU 81  244 244 GLU GLU D . n 
D 2 82  ASP 82  245 245 ASP ASP D . n 
D 2 83  GLN 83  246 246 GLN GLN D . n 
D 2 84  LEU 84  247 247 LEU LEU D . n 
D 2 85  LYS 85  248 248 LYS LYS D . n 
D 2 86  ALA 86  249 249 ALA ALA D . n 
D 2 87  ALA 87  250 250 ALA ALA D . n 
D 2 88  GLU 88  251 251 GLU GLU D . n 
D 2 89  GLU 89  252 252 GLU GLU D . n 
D 2 90  ASN 90  253 ?   ?   ?   D . n 
D 2 91  ASN 91  254 ?   ?   ?   D . n 
D 2 92  ASN 92  255 ?   ?   ?   D . n 
D 2 93  VAL 93  256 ?   ?   ?   D . n 
D 2 94  GLU 94  257 257 GLU GLU D . n 
D 2 95  ASP 95  258 258 ASP ASP D . n 
D 2 96  TYR 96  259 259 TYR TYR D . n 
D 2 97  PHE 97  260 260 PHE PHE D . n 
D 2 98  LYS 98  261 261 LYS LYS D . n 
D 2 99  GLU 99  262 262 GLU GLU D . n 
D 2 100 GLY 100 263 263 GLY GLY D . n 
D 2 101 LEU 101 264 264 LEU LEU D . n 
D 2 102 GLU 102 265 265 GLU GLU D . n 
D 2 103 LYS 103 266 266 LYS LYS D . n 
D 2 104 THR 104 267 267 THR THR D . n 
D 2 105 ILE 105 268 268 ILE ILE D . n 
D 2 106 ALA 106 269 269 ALA ALA D . n 
D 2 107 ALA 107 270 270 ALA ALA D . n 
D 2 108 LYS 108 271 271 LYS LYS D . n 
D 2 109 LYS 109 272 272 LYS LYS D . n 
D 2 110 ALA 110 273 273 ALA ALA D . n 
D 2 111 GLU 111 274 274 GLU GLU D . n 
D 2 112 LEU 112 275 275 LEU LEU D . n 
D 2 113 GLU 113 276 276 GLU GLU D . n 
D 2 114 LYS 114 277 277 LYS LYS D . n 
D 2 115 THR 115 278 278 THR THR D . n 
D 2 116 GLU 116 279 279 GLU GLU D . n 
D 2 117 ALA 117 280 280 ALA ALA D . n 
D 2 118 ASP 118 281 281 ASP ASP D . n 
D 2 119 LEU 119 282 282 LEU LEU D . n 
D 2 120 LYS 120 283 283 LYS LYS D . n 
D 2 121 LYS 121 284 284 LYS LYS D . n 
D 2 122 ALA 122 285 285 ALA ALA D . n 
D 2 123 VAL 123 286 286 VAL VAL D . n 
D 2 124 ASN 124 287 287 ASN ASN D . n 
D 2 125 GLU 125 288 288 GLU GLU D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 NAG 1  345 340 NAG NAG A . 
F 4 CO3 1  346 339 CO3 CO3 A . 
G 5 FE  1  347 334 FE  FE  A . 
H 6 SO4 1  348 335 SO4 SO4 A . 
I 6 SO4 1  349 336 SO4 SO4 A . 
J 6 SO4 1  350 337 SO4 SO4 A . 
K 3 NAG 1  345 340 NAG NAG B . 
L 4 CO3 1  346 339 CO3 CO3 B . 
M 5 FE  1  347 334 FE  FE  B . 
N 6 SO4 1  348 335 SO4 SO4 B . 
O 6 SO4 1  349 336 SO4 SO4 B . 
P 6 SO4 1  350 337 SO4 SO4 B . 
Q 7 ZN  1  502 502 ZN  ZN  C . 
R 7 ZN  1  501 501 ZN  ZN  D . 
S 8 HOH 1  406 406 HOH HOH A . 
S 8 HOH 2  407 407 HOH HOH A . 
S 8 HOH 3  410 410 HOH HOH A . 
S 8 HOH 4  414 414 HOH HOH A . 
S 8 HOH 5  416 416 HOH HOH A . 
S 8 HOH 6  417 417 HOH HOH A . 
S 8 HOH 7  418 418 HOH HOH A . 
S 8 HOH 8  421 421 HOH HOH A . 
T 8 HOH 1  405 405 HOH HOH B . 
T 8 HOH 2  408 408 HOH HOH B . 
T 8 HOH 3  409 409 HOH HOH B . 
T 8 HOH 4  413 413 HOH HOH B . 
T 8 HOH 5  415 415 HOH HOH B . 
T 8 HOH 6  419 419 HOH HOH B . 
T 8 HOH 7  422 422 HOH HOH B . 
T 8 HOH 8  423 423 HOH HOH B . 
T 8 HOH 9  424 424 HOH HOH B . 
T 8 HOH 10 425 425 HOH HOH B . 
U 8 HOH 1  402 402 HOH HOH C . 
U 8 HOH 2  404 404 HOH HOH C . 
U 8 HOH 3  412 412 HOH HOH C . 
V 8 HOH 1  401 401 HOH HOH D . 
V 8 HOH 2  403 403 HOH HOH D . 
V 8 HOH 3  411 411 HOH HOH D . 
# 
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 138 A ASN 138 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 138 B ASN 138 ? 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_defined_assembly ? dimeric 2 
2 author_defined_assembly ? 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,C,E,F,G,H,I,J,Q,S,U 
2 1 B,D,K,L,M,N,O,P,R,T,V 
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 61  ? A ASP 61  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 OH  ? A TYR 93  ? A TYR 93  ? 1_555 88.4  ? 
2  OD1 ? A ASP 61  ? A ASP 61  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 OH  ? A TYR 193 ? A TYR 193 ? 1_555 169.0 ? 
3  OH  ? A TYR 93  ? A TYR 93  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 OH  ? A TYR 193 ? A TYR 193 ? 1_555 97.3  ? 
4  OD1 ? A ASP 61  ? A ASP 61  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 NE2 ? A HIS 254 ? A HIS 254 ? 1_555 82.2  ? 
5  OH  ? A TYR 93  ? A TYR 93  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 NE2 ? A HIS 254 ? A HIS 254 ? 1_555 93.5  ? 
6  OH  ? A TYR 193 ? A TYR 193 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 NE2 ? A HIS 254 ? A HIS 254 ? 1_555 88.0  ? 
7  OD1 ? A ASP 61  ? A ASP 61  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O1  ? F CO3 .   ? A CO3 346 ? 1_555 94.4  ? 
8  OH  ? A TYR 93  ? A TYR 93  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O1  ? F CO3 .   ? A CO3 346 ? 1_555 93.8  ? 
9  OH  ? A TYR 193 ? A TYR 193 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O1  ? F CO3 .   ? A CO3 346 ? 1_555 94.6  ? 
10 NE2 ? A HIS 254 ? A HIS 254 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O1  ? F CO3 .   ? A CO3 346 ? 1_555 171.9 ? 
11 OD1 ? A ASP 61  ? A ASP 61  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O2  ? F CO3 .   ? A CO3 346 ? 1_555 92.5  ? 
12 OH  ? A TYR 93  ? A TYR 93  ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O2  ? F CO3 .   ? A CO3 346 ? 1_555 150.8 ? 
13 OH  ? A TYR 193 ? A TYR 193 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O2  ? F CO3 .   ? A CO3 346 ? 1_555 87.0  ? 
14 NE2 ? A HIS 254 ? A HIS 254 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O2  ? F CO3 .   ? A CO3 346 ? 1_555 115.6 ? 
15 O1  ? F CO3 .   ? A CO3 346 ? 1_555 FE ? G FE . ? A FE 347 ? 1_555 O2  ? F CO3 .   ? A CO3 346 ? 1_555 57.0  ? 
16 OD1 ? B ASP 61  ? B ASP 61  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 OH  ? B TYR 93  ? B TYR 93  ? 1_555 92.2  ? 
17 OD1 ? B ASP 61  ? B ASP 61  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 OH  ? B TYR 193 ? B TYR 193 ? 1_555 168.0 ? 
18 OH  ? B TYR 93  ? B TYR 93  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 OH  ? B TYR 193 ? B TYR 193 ? 1_555 98.1  ? 
19 OD1 ? B ASP 61  ? B ASP 61  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 NE2 ? B HIS 254 ? B HIS 254 ? 1_555 78.7  ? 
20 OH  ? B TYR 93  ? B TYR 93  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 NE2 ? B HIS 254 ? B HIS 254 ? 1_555 91.4  ? 
21 OH  ? B TYR 193 ? B TYR 193 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 NE2 ? B HIS 254 ? B HIS 254 ? 1_555 94.8  ? 
22 OD1 ? B ASP 61  ? B ASP 61  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O1  ? L CO3 .   ? B CO3 346 ? 1_555 87.0  ? 
23 OH  ? B TYR 93  ? B TYR 93  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O1  ? L CO3 .   ? B CO3 346 ? 1_555 95.6  ? 
24 OH  ? B TYR 193 ? B TYR 193 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O1  ? L CO3 .   ? B CO3 346 ? 1_555 98.1  ? 
25 NE2 ? B HIS 254 ? B HIS 254 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O1  ? L CO3 .   ? B CO3 346 ? 1_555 164.3 ? 
26 OD1 ? B ASP 61  ? B ASP 61  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O2  ? L CO3 .   ? B CO3 346 ? 1_555 86.5  ? 
27 OH  ? B TYR 93  ? B TYR 93  ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O2  ? L CO3 .   ? B CO3 346 ? 1_555 154.0 ? 
28 OH  ? B TYR 193 ? B TYR 193 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O2  ? L CO3 .   ? B CO3 346 ? 1_555 86.9  ? 
29 NE2 ? B HIS 254 ? B HIS 254 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O2  ? L CO3 .   ? B CO3 346 ? 1_555 113.7 ? 
30 O1  ? L CO3 .   ? B CO3 346 ? 1_555 FE ? M FE . ? B FE 347 ? 1_555 O2  ? L CO3 .   ? B CO3 346 ? 1_555 58.4  ? 
31 NE2 ? C HIS 3   ? C HIS 166 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OD1 ? C ASP 5   ? C ASP 168 ? 1_555 98.3  ? 
32 NE2 ? C HIS 3   ? C HIS 166 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OD2 ? C ASP 5   ? C ASP 168 ? 1_555 96.9  ? 
33 OD1 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OD2 ? C ASP 5   ? C ASP 168 ? 1_555 55.3  ? 
34 NE2 ? C HIS 3   ? C HIS 166 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE1 ? D GLU 99  ? D GLU 262 ? 3_554 86.0  ? 
35 OD1 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE1 ? D GLU 99  ? D GLU 262 ? 3_554 153.9 ? 
36 OD2 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE1 ? D GLU 99  ? D GLU 262 ? 3_554 150.1 ? 
37 NE2 ? C HIS 3   ? C HIS 166 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE2 ? D GLU 99  ? D GLU 262 ? 3_554 106.3 ? 
38 OD1 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE2 ? D GLU 99  ? D GLU 262 ? 3_554 102.2 ? 
39 OD2 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE2 ? D GLU 99  ? D GLU 262 ? 3_554 150.2 ? 
40 OE1 ? D GLU 99  ? D GLU 262 ? 3_554 ZN ? Q ZN . ? C ZN 502 ? 1_555 OE2 ? D GLU 99  ? D GLU 262 ? 3_554 52.3  ? 
41 NE2 ? C HIS 3   ? C HIS 166 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 NE2 ? B HIS 247 ? B HIS 247 ? 1_554 127.7 ? 
42 OD1 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 NE2 ? B HIS 247 ? B HIS 247 ? 1_554 116.7 ? 
43 OD2 ? C ASP 5   ? C ASP 168 ? 1_555 ZN ? Q ZN . ? C ZN 502 ? 1_555 NE2 ? B HIS 247 ? B HIS 247 ? 1_554 76.0  ? 
44 OE1 ? D GLU 99  ? D GLU 262 ? 3_554 ZN ? Q ZN . ? C ZN 502 ? 1_555 NE2 ? B HIS 247 ? B HIS 247 ? 1_554 78.8  ? 
45 OE2 ? D GLU 99  ? D GLU 262 ? 3_554 ZN ? Q ZN . ? C ZN 502 ? 1_555 NE2 ? B HIS 247 ? B HIS 247 ? 1_554 102.8 ? 
46 NE2 ? A HIS 247 ? A HIS 247 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 NE2 ? D HIS 3   ? D HIS 166 ? 1_555 126.5 ? 
47 NE2 ? A HIS 247 ? A HIS 247 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OD1 ? D ASP 5   ? D ASP 168 ? 1_555 107.0 ? 
48 NE2 ? D HIS 3   ? D HIS 166 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OD1 ? D ASP 5   ? D ASP 168 ? 1_555 113.5 ? 
49 NE2 ? A HIS 247 ? A HIS 247 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OD2 ? D ASP 5   ? D ASP 168 ? 1_555 83.8  ? 
50 NE2 ? D HIS 3   ? D HIS 166 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OD2 ? D ASP 5   ? D ASP 168 ? 1_555 90.3  ? 
51 OD1 ? D ASP 5   ? D ASP 168 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OD2 ? D ASP 5   ? D ASP 168 ? 1_555 56.8  ? 
52 NE2 ? A HIS 247 ? A HIS 247 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OE2 ? C GLU 99  ? C GLU 262 ? 3_565 99.4  ? 
53 NE2 ? D HIS 3   ? D HIS 166 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OE2 ? C GLU 99  ? C GLU 262 ? 3_565 104.5 ? 
54 OD1 ? D ASP 5   ? D ASP 168 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OE2 ? C GLU 99  ? C GLU 262 ? 3_565 102.0 ? 
55 OD2 ? D ASP 5   ? D ASP 168 ? 1_555 ZN ? R ZN . ? D ZN 501 ? 1_555 OE2 ? C GLU 99  ? C GLU 262 ? 3_565 158.1 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-06-19 
2 'Structure model' 1 1 2007-10-16 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-18 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Advisory                    
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_software.classification'       
2 4 'Structure model' '_software.contact_author'       
3 4 'Structure model' '_software.contact_author_email' 
4 4 'Structure model' '_software.date'                 
5 4 'Structure model' '_software.language'             
6 4 'Structure model' '_software.location'             
7 4 'Structure model' '_software.name'                 
8 4 'Structure model' '_software.type'                 
9 4 'Structure model' '_software.version'              
# 
loop_
_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] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined -2.6760  37.1650 39.7170 -0.0180 -0.2054 -0.1392 0.0103 -0.0107 -0.0371 2.4845 1.7357 2.2503 1.3340 -1.1131 -0.4011 
-0.0684 0.0539 -0.0254 -0.0343 -0.0144 0.0287  0.0825  -0.0653 0.0827  'X-RAY DIFFRACTION' 
2 ? refined 2.6780   37.9960 80.1130 -0.0194 -0.1977 -0.1475 0.0068 0.0287  0.0288  2.4638 1.8147 2.1574 1.2662 1.0970  0.1835  
-0.0324 0.0481 0.0085  -0.0232 -0.0154 -0.0484 -0.0754 0.0981  0.0478  'X-RAY DIFFRACTION' 
3 ? refined 26.2610  47.1860 28.4060 -0.0463 -0.1063 0.0215  0.0395 0.0304  -0.0009 0.9983 5.2925 0.7298 1.6107 0.1714  1.5287  
-0.0690 0.1035 -0.1131 0.0543  0.1744  -0.4984 -0.0508 0.2522  -0.1054 'X-RAY DIFFRACTION' 
4 ? refined -26.2780 27.9790 68.8210 -0.0760 -0.0899 0.0352  0.0202 -0.0353 0.0006  0.9161 5.1629 0.7815 1.6731 -0.1830 -1.3455 
-0.0058 0.0476 0.1070  -0.0719 0.0493  0.5058  0.0378  -0.2477 -0.0435 'X-RAY DIFFRACTION' 
# 
loop_
_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.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 4   A 4 A 333 A 333 ? 'X-RAY DIFFRACTION' ? 
2 2 B 4   B 4 B 333 B 333 ? 'X-RAY DIFFRACTION' ? 
3 3 C 164 C 1 C 288 C 125 ? 'X-RAY DIFFRACTION' ? 
4 4 D 164 D 1 D 288 D 125 ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       .        ?                package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .        ?                package 'Zbyszek Otwinowski' zbyszek@mix.swmed.edu    'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
REFMAC      5.2.0019 ?                program 'Murshudov, G.N.'    ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 3 
PDB_EXTRACT 2.000    'April. 3, 2006' package PDB                  sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 4 
HKL-2000    .        ?                ?       ?                    ?                        'data collection' ? ?          ? 5 
HKL-2000    .        ?                ?       ?                    ?                        'data reduction'  ? ?          ? 6 
MOLREP      .        ?                ?       ?                    ?                        phasing           ? ?          ? 7 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NE2 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HIS 
_pdbx_validate_symm_contact.auth_seq_id_1     92 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    N 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    GLY 
_pdbx_validate_symm_contact.auth_seq_id_2     164 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_556 
_pdbx_validate_symm_contact.dist              2.16 
# 
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 TRP A 126 ? ? -138.87 -60.00  
2  1 PRO A 143 ? ? -79.57  24.64   
3  1 SER A 192 ? ? 64.51   -177.19 
4  1 LYS A 242 ? ? -98.36  39.39   
5  1 CYS A 246 ? ? -151.13 64.96   
6  1 HIS A 254 ? ? -48.93  151.83  
7  1 PHE A 290 ? ? -107.58 44.97   
8  1 LEU A 300 ? ? 70.95   -47.62  
9  1 PRO A 312 ? ? -46.76  152.36  
10 1 TRP B 126 ? ? -134.82 -62.68  
11 1 SER B 192 ? ? 61.11   178.40  
12 1 LYS B 242 ? ? -90.52  42.35   
13 1 HIS B 254 ? ? -43.66  152.33  
14 1 LYS B 264 ? ? 70.65   31.86   
15 1 ASP B 282 ? ? 59.84   17.22   
16 1 LEU B 300 ? ? 68.29   -45.84  
17 1 ARG B 314 ? ? 81.12   -0.79   
18 1 GLU C 251 ? ? -147.66 -7.62   
19 1 GLU D 251 ? ? -149.80 -21.96  
# 
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 GLY 1   ? A GLY 1   
2  1 Y 1 A ARG 2   ? A ARG 2   
3  1 Y 1 A LYS 334 ? A LYS 334 
4  1 Y 1 A SER 335 ? A SER 335 
5  1 Y 1 A GLU 336 ? A GLU 336 
6  1 Y 1 A GLU 337 ? A GLU 337 
7  1 Y 1 A GLU 338 ? A GLU 338 
8  1 Y 1 A VAL 339 ? A VAL 339 
9  1 Y 1 A ALA 340 ? A ALA 340 
10 1 Y 1 A ALA 341 ? A ALA 341 
11 1 Y 1 A ARG 342 ? A ARG 342 
12 1 Y 1 A ARG 343 ? A ARG 343 
13 1 Y 1 A ALA 344 ? A ALA 344 
14 1 Y 1 B GLY 1   ? B GLY 1   
15 1 Y 1 B ARG 2   ? B ARG 2   
16 1 Y 1 B LYS 334 ? B LYS 334 
17 1 Y 1 B SER 335 ? B SER 335 
18 1 Y 1 B GLU 336 ? B GLU 336 
19 1 Y 1 B GLU 337 ? B GLU 337 
20 1 Y 1 B GLU 338 ? B GLU 338 
21 1 Y 1 B VAL 339 ? B VAL 339 
22 1 Y 1 B ALA 340 ? B ALA 340 
23 1 Y 1 B ALA 341 ? B ALA 341 
24 1 Y 1 B ARG 342 ? B ARG 342 
25 1 Y 1 B ARG 343 ? B ARG 343 
26 1 Y 1 B ALA 344 ? B ALA 344 
27 1 Y 1 C SER 198 ? C SER 35  
28 1 Y 1 C GLU 199 ? C GLU 36  
29 1 Y 1 C SER 200 ? C SER 37  
30 1 Y 1 C GLU 201 ? C GLU 38  
31 1 Y 1 C ASP 202 ? C ASP 39  
32 1 Y 1 C TYR 203 ? C TYR 40  
33 1 Y 1 C ALA 204 ? C ALA 41  
34 1 Y 1 C LYS 205 ? C LYS 42  
35 1 Y 1 C GLU 206 ? C GLU 43  
36 1 Y 1 C GLY 207 ? C GLY 44  
37 1 Y 1 C PHE 208 ? C PHE 45  
38 1 Y 1 C ARG 209 ? C ARG 46  
39 1 Y 1 C ASN 253 ? C ASN 90  
40 1 Y 1 C ASN 254 ? C ASN 91  
41 1 Y 1 C ASN 255 ? C ASN 92  
42 1 Y 1 C VAL 256 ? C VAL 93  
43 1 Y 1 D SER 198 ? D SER 35  
44 1 Y 1 D GLU 199 ? D GLU 36  
45 1 Y 1 D SER 200 ? D SER 37  
46 1 Y 1 D GLU 201 ? D GLU 38  
47 1 Y 1 D ASP 202 ? D ASP 39  
48 1 Y 1 D TYR 203 ? D TYR 40  
49 1 Y 1 D ALA 204 ? D ALA 41  
50 1 Y 1 D LYS 205 ? D LYS 42  
51 1 Y 1 D GLU 206 ? D GLU 43  
52 1 Y 1 D GLY 207 ? D GLY 44  
53 1 Y 1 D PHE 208 ? D PHE 45  
54 1 Y 1 D ARG 209 ? D ARG 46  
55 1 Y 1 D ASN 253 ? D ASN 90  
56 1 Y 1 D ASN 254 ? D ASN 91  
57 1 Y 1 D ASN 255 ? D ASN 92  
58 1 Y 1 D VAL 256 ? D VAL 93  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 'CARBONATE ION'        CO3 
5 'FE (III) ION'         FE  
6 'SULFATE ION'          SO4 
7 'ZINC ION'             ZN  
8 water                  HOH 
# 
