data_9GR8
# 
_entry.id   9GR8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GR8         pdb_00009gr8 10.2210/pdb9gr8/pdb 
WWPDB D_1292141671 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GR8 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michael.hothorn@unige.ch 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Hothorn 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3597-5698 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lee, K.'     1 ?                   
'Raia, P.'    2 ?                   
'Hothorn, M.' 3 0000-0002-3597-5698 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1753 
_citation.page_last                 1753 
_citation.title                     'A small signaling domain controls PPIP5K phosphatase activity in phosphate homeostasis.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56937-0 
_citation.pdbx_database_id_PubMed   39966396 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Raia, P.'             1 0000-0003-3469-1922 
primary 'Lee, K.'              2 0000-0002-7761-5586 
primary 'Bartsch, S.M.'        3 0000-0002-2215-7901 
primary 'Rico-Resendiz, F.'    4 ?                   
primary 'Portugal-Calisto, D.' 5 ?                   
primary 'Vadas, O.'            6 0000-0003-3511-6479 
primary 'Panse, V.G.'          7 0000-0002-4770-7068 
primary 'Fiedler, D.'          8 0000-0002-0798-946X 
primary 'Hothorn, M.'          9 0000-0002-3597-5698 
# 
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 'Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase' 38652.219 1   2.7.4.24 ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                                 427.201   1   ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                             62.068    5   ?        ? ? ? 
4 water       nat water                                                                      18.015    371 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'InsP6 and PP-IP5 kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GAKVGKIGVCAMDAKVLSKPMRHILNRLIEHGEFETVIFGDKVILDERIENWPTCDFLISFFSSGFPLDKAIKYVKLRKP
FIINDLIMQKILWDRRLCLQVLEAYNVPTPPRLEISRDGGPRANEELRAKLREHGVEVKPVEEPEWKMVDDDTLEVDGKT
MTKPFVEKPVDGEDHNIYIYYHSKNGGGGRRLFRKVGNKSSEFDPTLVHPRTEGSYIYEQFMDTDNFEDVKAYTIGENFC
HAETRKSPVVDGIVRRNTHGKEVRYITELSDEEKTIAGKVSKAFSQMICGFDLLRVSGKSYVIDVNGFSFVKDNKAYYDS
CANILRSTFIEAKKKMD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAKVGKIGVCAMDAKVLSKPMRHILNRLIEHGEFETVIFGDKVILDERIENWPTCDFLISFFSSGFPLDKAIKYVKLRKP
FIINDLIMQKILWDRRLCLQVLEAYNVPTPPRLEISRDGGPRANEELRAKLREHGVEVKPVEEPEWKMVDDDTLEVDGKT
MTKPFVEKPVDGEDHNIYIYYHSKNGGGGRRLFRKVGNKSSEFDPTLVHPRTEGSYIYEQFMDTDNFEDVKAYTIGENFC
HAETRKSPVVDGIVRRNTHGKEVRYITELSDEEKTIAGKVSKAFSQMICGFDLLRVSGKSYVIDVNGFSFVKDNKAYYDS
CANILRSTFIEAKKKMD
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE" ADP 
3 1,2-ETHANEDIOL             EDO 
4 water                      HOH 
# 
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   ALA n 
1 3   LYS n 
1 4   VAL n 
1 5   GLY n 
1 6   LYS n 
1 7   ILE n 
1 8   GLY n 
1 9   VAL n 
1 10  CYS n 
1 11  ALA n 
1 12  MET n 
1 13  ASP n 
1 14  ALA n 
1 15  LYS n 
1 16  VAL n 
1 17  LEU n 
1 18  SER n 
1 19  LYS n 
1 20  PRO n 
1 21  MET n 
1 22  ARG n 
1 23  HIS n 
1 24  ILE n 
1 25  LEU n 
1 26  ASN n 
1 27  ARG n 
1 28  LEU n 
1 29  ILE n 
1 30  GLU n 
1 31  HIS n 
1 32  GLY n 
1 33  GLU n 
1 34  PHE n 
1 35  GLU n 
1 36  THR n 
1 37  VAL n 
1 38  ILE n 
1 39  PHE n 
1 40  GLY n 
1 41  ASP n 
1 42  LYS n 
1 43  VAL n 
1 44  ILE n 
1 45  LEU n 
1 46  ASP n 
1 47  GLU n 
1 48  ARG n 
1 49  ILE n 
1 50  GLU n 
1 51  ASN n 
1 52  TRP n 
1 53  PRO n 
1 54  THR n 
1 55  CYS n 
1 56  ASP n 
1 57  PHE n 
1 58  LEU n 
1 59  ILE n 
1 60  SER n 
1 61  PHE n 
1 62  PHE n 
1 63  SER n 
1 64  SER n 
1 65  GLY n 
1 66  PHE n 
1 67  PRO n 
1 68  LEU n 
1 69  ASP n 
1 70  LYS n 
1 71  ALA n 
1 72  ILE n 
1 73  LYS n 
1 74  TYR n 
1 75  VAL n 
1 76  LYS n 
1 77  LEU n 
1 78  ARG n 
1 79  LYS n 
1 80  PRO n 
1 81  PHE n 
1 82  ILE n 
1 83  ILE n 
1 84  ASN n 
1 85  ASP n 
1 86  LEU n 
1 87  ILE n 
1 88  MET n 
1 89  GLN n 
1 90  LYS n 
1 91  ILE n 
1 92  LEU n 
1 93  TRP n 
1 94  ASP n 
1 95  ARG n 
1 96  ARG n 
1 97  LEU n 
1 98  CYS n 
1 99  LEU n 
1 100 GLN n 
1 101 VAL n 
1 102 LEU n 
1 103 GLU n 
1 104 ALA n 
1 105 TYR n 
1 106 ASN n 
1 107 VAL n 
1 108 PRO n 
1 109 THR n 
1 110 PRO n 
1 111 PRO n 
1 112 ARG n 
1 113 LEU n 
1 114 GLU n 
1 115 ILE n 
1 116 SER n 
1 117 ARG n 
1 118 ASP n 
1 119 GLY n 
1 120 GLY n 
1 121 PRO n 
1 122 ARG n 
1 123 ALA n 
1 124 ASN n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 ARG n 
1 129 ALA n 
1 130 LYS n 
1 131 LEU n 
1 132 ARG n 
1 133 GLU n 
1 134 HIS n 
1 135 GLY n 
1 136 VAL n 
1 137 GLU n 
1 138 VAL n 
1 139 LYS n 
1 140 PRO n 
1 141 VAL n 
1 142 GLU n 
1 143 GLU n 
1 144 PRO n 
1 145 GLU n 
1 146 TRP n 
1 147 LYS n 
1 148 MET n 
1 149 VAL n 
1 150 ASP n 
1 151 ASP n 
1 152 ASP n 
1 153 THR n 
1 154 LEU n 
1 155 GLU n 
1 156 VAL n 
1 157 ASP n 
1 158 GLY n 
1 159 LYS n 
1 160 THR n 
1 161 MET n 
1 162 THR n 
1 163 LYS n 
1 164 PRO n 
1 165 PHE n 
1 166 VAL n 
1 167 GLU n 
1 168 LYS n 
1 169 PRO n 
1 170 VAL n 
1 171 ASP n 
1 172 GLY n 
1 173 GLU n 
1 174 ASP n 
1 175 HIS n 
1 176 ASN n 
1 177 ILE n 
1 178 TYR n 
1 179 ILE n 
1 180 TYR n 
1 181 TYR n 
1 182 HIS n 
1 183 SER n 
1 184 LYS n 
1 185 ASN n 
1 186 GLY n 
1 187 GLY n 
1 188 GLY n 
1 189 GLY n 
1 190 ARG n 
1 191 ARG n 
1 192 LEU n 
1 193 PHE n 
1 194 ARG n 
1 195 LYS n 
1 196 VAL n 
1 197 GLY n 
1 198 ASN n 
1 199 LYS n 
1 200 SER n 
1 201 SER n 
1 202 GLU n 
1 203 PHE n 
1 204 ASP n 
1 205 PRO n 
1 206 THR n 
1 207 LEU n 
1 208 VAL n 
1 209 HIS n 
1 210 PRO n 
1 211 ARG n 
1 212 THR n 
1 213 GLU n 
1 214 GLY n 
1 215 SER n 
1 216 TYR n 
1 217 ILE n 
1 218 TYR n 
1 219 GLU n 
1 220 GLN n 
1 221 PHE n 
1 222 MET n 
1 223 ASP n 
1 224 THR n 
1 225 ASP n 
1 226 ASN n 
1 227 PHE n 
1 228 GLU n 
1 229 ASP n 
1 230 VAL n 
1 231 LYS n 
1 232 ALA n 
1 233 TYR n 
1 234 THR n 
1 235 ILE n 
1 236 GLY n 
1 237 GLU n 
1 238 ASN n 
1 239 PHE n 
1 240 CYS n 
1 241 HIS n 
1 242 ALA n 
1 243 GLU n 
1 244 THR n 
1 245 ARG n 
1 246 LYS n 
1 247 SER n 
1 248 PRO n 
1 249 VAL n 
1 250 VAL n 
1 251 ASP n 
1 252 GLY n 
1 253 ILE n 
1 254 VAL n 
1 255 ARG n 
1 256 ARG n 
1 257 ASN n 
1 258 THR n 
1 259 HIS n 
1 260 GLY n 
1 261 LYS n 
1 262 GLU n 
1 263 VAL n 
1 264 ARG n 
1 265 TYR n 
1 266 ILE n 
1 267 THR n 
1 268 GLU n 
1 269 LEU n 
1 270 SER n 
1 271 ASP n 
1 272 GLU n 
1 273 GLU n 
1 274 LYS n 
1 275 THR n 
1 276 ILE n 
1 277 ALA n 
1 278 GLY n 
1 279 LYS n 
1 280 VAL n 
1 281 SER n 
1 282 LYS n 
1 283 ALA n 
1 284 PHE n 
1 285 SER n 
1 286 GLN n 
1 287 MET n 
1 288 ILE n 
1 289 CYS n 
1 290 GLY n 
1 291 PHE n 
1 292 ASP n 
1 293 LEU n 
1 294 LEU n 
1 295 ARG n 
1 296 VAL n 
1 297 SER n 
1 298 GLY n 
1 299 LYS n 
1 300 SER n 
1 301 TYR n 
1 302 VAL n 
1 303 ILE n 
1 304 ASP n 
1 305 VAL n 
1 306 ASN n 
1 307 GLY n 
1 308 PHE n 
1 309 SER n 
1 310 PHE n 
1 311 VAL n 
1 312 LYS n 
1 313 ASP n 
1 314 ASN n 
1 315 LYS n 
1 316 ALA n 
1 317 TYR n 
1 318 TYR n 
1 319 ASP n 
1 320 SER n 
1 321 CYS n 
1 322 ALA n 
1 323 ASN n 
1 324 ILE n 
1 325 LEU n 
1 326 ARG n 
1 327 SER n 
1 328 THR n 
1 329 PHE n 
1 330 ILE n 
1 331 GLU n 
1 332 ALA n 
1 333 LYS n 
1 334 LYS n 
1 335 LYS n 
1 336 MET n 
1 337 ASP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   337 
_entity_src_gen.gene_src_common_name               
;brewer's yeast
;
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'VIP1, YLR410W' 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_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      'Trichoplusia ni' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7111 
_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            Tnao 
_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                   ? 
# 
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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ?                 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                    ?                 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                   ?                 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ?                 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ?                 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                   ?                 'C3 H7 N O2 S'      121.158 
EDO non-polymer         . 1,2-ETHANEDIOL             'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
GLN 'L-peptide linking' y GLUTAMINE                  ?                 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ?                 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ?                 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                  ?                 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                      ?                 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ?                 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                    ?                 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                     ?                 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                 ?                 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE              ?                 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                    ?                 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                     ?                 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                  ?                 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                 ?                 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                   ?                 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                     ?                 'C5 H11 N O2'       117.146 
# 
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   184 184 GLY GLY A . n 
A 1 2   ALA 2   185 185 ALA ALA A . n 
A 1 3   LYS 3   186 186 LYS LYS A . n 
A 1 4   VAL 4   187 187 VAL VAL A . n 
A 1 5   GLY 5   188 188 GLY GLY A . n 
A 1 6   LYS 6   189 189 LYS LYS A . n 
A 1 7   ILE 7   190 190 ILE ILE A . n 
A 1 8   GLY 8   191 191 GLY GLY A . n 
A 1 9   VAL 9   192 192 VAL VAL A . n 
A 1 10  CYS 10  193 193 CYS CYS A . n 
A 1 11  ALA 11  194 194 ALA ALA A . n 
A 1 12  MET 12  195 195 MET MET A . n 
A 1 13  ASP 13  196 196 ASP ASP A . n 
A 1 14  ALA 14  197 197 ALA ALA A . n 
A 1 15  LYS 15  198 198 LYS LYS A . n 
A 1 16  VAL 16  199 199 VAL VAL A . n 
A 1 17  LEU 17  200 200 LEU LEU A . n 
A 1 18  SER 18  201 201 SER SER A . n 
A 1 19  LYS 19  202 202 LYS LYS A . n 
A 1 20  PRO 20  203 203 PRO PRO A . n 
A 1 21  MET 21  204 204 MET MET A . n 
A 1 22  ARG 22  205 205 ARG ARG A . n 
A 1 23  HIS 23  206 206 HIS HIS A . n 
A 1 24  ILE 24  207 207 ILE ILE A . n 
A 1 25  LEU 25  208 208 LEU LEU A . n 
A 1 26  ASN 26  209 209 ASN ASN A . n 
A 1 27  ARG 27  210 210 ARG ARG A . n 
A 1 28  LEU 28  211 211 LEU LEU A . n 
A 1 29  ILE 29  212 212 ILE ILE A . n 
A 1 30  GLU 30  213 213 GLU GLU A . n 
A 1 31  HIS 31  214 214 HIS HIS A . n 
A 1 32  GLY 32  215 215 GLY GLY A . n 
A 1 33  GLU 33  216 216 GLU GLU A . n 
A 1 34  PHE 34  217 217 PHE PHE A . n 
A 1 35  GLU 35  218 218 GLU GLU A . n 
A 1 36  THR 36  219 219 THR THR A . n 
A 1 37  VAL 37  220 220 VAL VAL A . n 
A 1 38  ILE 38  221 221 ILE ILE A . n 
A 1 39  PHE 39  222 222 PHE PHE A . n 
A 1 40  GLY 40  223 223 GLY GLY A . n 
A 1 41  ASP 41  224 224 ASP ASP A . n 
A 1 42  LYS 42  225 225 LYS LYS A . n 
A 1 43  VAL 43  226 226 VAL VAL A . n 
A 1 44  ILE 44  227 227 ILE ILE A . n 
A 1 45  LEU 45  228 228 LEU LEU A . n 
A 1 46  ASP 46  229 229 ASP ASP A . n 
A 1 47  GLU 47  230 230 GLU GLU A . n 
A 1 48  ARG 48  231 231 ARG ARG A . n 
A 1 49  ILE 49  232 232 ILE ILE A . n 
A 1 50  GLU 50  233 233 GLU GLU A . n 
A 1 51  ASN 51  234 234 ASN ASN A . n 
A 1 52  TRP 52  235 235 TRP TRP A . n 
A 1 53  PRO 53  236 236 PRO PRO A . n 
A 1 54  THR 54  237 237 THR THR A . n 
A 1 55  CYS 55  238 238 CYS CYS A . n 
A 1 56  ASP 56  239 239 ASP ASP A . n 
A 1 57  PHE 57  240 240 PHE PHE A . n 
A 1 58  LEU 58  241 241 LEU LEU A . n 
A 1 59  ILE 59  242 242 ILE ILE A . n 
A 1 60  SER 60  243 243 SER SER A . n 
A 1 61  PHE 61  244 244 PHE PHE A . n 
A 1 62  PHE 62  245 245 PHE PHE A . n 
A 1 63  SER 63  246 246 SER SER A . n 
A 1 64  SER 64  247 247 SER SER A . n 
A 1 65  GLY 65  248 248 GLY GLY A . n 
A 1 66  PHE 66  249 249 PHE PHE A . n 
A 1 67  PRO 67  250 250 PRO PRO A . n 
A 1 68  LEU 68  251 251 LEU LEU A . n 
A 1 69  ASP 69  252 252 ASP ASP A . n 
A 1 70  LYS 70  253 253 LYS LYS A . n 
A 1 71  ALA 71  254 254 ALA ALA A . n 
A 1 72  ILE 72  255 255 ILE ILE A . n 
A 1 73  LYS 73  256 256 LYS LYS A . n 
A 1 74  TYR 74  257 257 TYR TYR A . n 
A 1 75  VAL 75  258 258 VAL VAL A . n 
A 1 76  LYS 76  259 259 LYS LYS A . n 
A 1 77  LEU 77  260 260 LEU LEU A . n 
A 1 78  ARG 78  261 261 ARG ARG A . n 
A 1 79  LYS 79  262 262 LYS LYS A . n 
A 1 80  PRO 80  263 263 PRO PRO A . n 
A 1 81  PHE 81  264 264 PHE PHE A . n 
A 1 82  ILE 82  265 265 ILE ILE A . n 
A 1 83  ILE 83  266 266 ILE ILE A . n 
A 1 84  ASN 84  267 267 ASN ASN A . n 
A 1 85  ASP 85  268 268 ASP ASP A . n 
A 1 86  LEU 86  269 269 LEU LEU A . n 
A 1 87  ILE 87  270 270 ILE ILE A . n 
A 1 88  MET 88  271 271 MET MET A . n 
A 1 89  GLN 89  272 272 GLN GLN A . n 
A 1 90  LYS 90  273 273 LYS LYS A . n 
A 1 91  ILE 91  274 274 ILE ILE A . n 
A 1 92  LEU 92  275 275 LEU LEU A . n 
A 1 93  TRP 93  276 276 TRP TRP A . n 
A 1 94  ASP 94  277 277 ASP ASP A . n 
A 1 95  ARG 95  278 278 ARG ARG A . n 
A 1 96  ARG 96  279 279 ARG ARG A . n 
A 1 97  LEU 97  280 280 LEU LEU A . n 
A 1 98  CYS 98  281 281 CYS CYS A . n 
A 1 99  LEU 99  282 282 LEU LEU A . n 
A 1 100 GLN 100 283 283 GLN GLN A . n 
A 1 101 VAL 101 284 284 VAL VAL A . n 
A 1 102 LEU 102 285 285 LEU LEU A . n 
A 1 103 GLU 103 286 286 GLU GLU A . n 
A 1 104 ALA 104 287 287 ALA ALA A . n 
A 1 105 TYR 105 288 288 TYR TYR A . n 
A 1 106 ASN 106 289 289 ASN ASN A . n 
A 1 107 VAL 107 290 290 VAL VAL A . n 
A 1 108 PRO 108 291 291 PRO PRO A . n 
A 1 109 THR 109 292 292 THR THR A . n 
A 1 110 PRO 110 293 293 PRO PRO A . n 
A 1 111 PRO 111 294 294 PRO PRO A . n 
A 1 112 ARG 112 295 295 ARG ARG A . n 
A 1 113 LEU 113 296 296 LEU LEU A . n 
A 1 114 GLU 114 297 297 GLU GLU A . n 
A 1 115 ILE 115 298 298 ILE ILE A . n 
A 1 116 SER 116 299 299 SER SER A . n 
A 1 117 ARG 117 300 300 ARG ARG A . n 
A 1 118 ASP 118 301 301 ASP ASP A . n 
A 1 119 GLY 119 302 302 GLY GLY A . n 
A 1 120 GLY 120 303 303 GLY GLY A . n 
A 1 121 PRO 121 304 304 PRO PRO A . n 
A 1 122 ARG 122 305 305 ARG ARG A . n 
A 1 123 ALA 123 306 306 ALA ALA A . n 
A 1 124 ASN 124 307 307 ASN ASN A . n 
A 1 125 GLU 125 308 308 GLU GLU A . n 
A 1 126 GLU 126 309 309 GLU GLU A . n 
A 1 127 LEU 127 310 310 LEU LEU A . n 
A 1 128 ARG 128 311 311 ARG ARG A . n 
A 1 129 ALA 129 312 312 ALA ALA A . n 
A 1 130 LYS 130 313 313 LYS LYS A . n 
A 1 131 LEU 131 314 314 LEU LEU A . n 
A 1 132 ARG 132 315 315 ARG ARG A . n 
A 1 133 GLU 133 316 316 GLU GLU A . n 
A 1 134 HIS 134 317 317 HIS HIS A . n 
A 1 135 GLY 135 318 318 GLY GLY A . n 
A 1 136 VAL 136 319 319 VAL VAL A . n 
A 1 137 GLU 137 320 320 GLU GLU A . n 
A 1 138 VAL 138 321 321 VAL VAL A . n 
A 1 139 LYS 139 322 322 LYS LYS A . n 
A 1 140 PRO 140 323 323 PRO PRO A . n 
A 1 141 VAL 141 324 324 VAL VAL A . n 
A 1 142 GLU 142 325 325 GLU GLU A . n 
A 1 143 GLU 143 326 326 GLU GLU A . n 
A 1 144 PRO 144 327 327 PRO PRO A . n 
A 1 145 GLU 145 328 328 GLU GLU A . n 
A 1 146 TRP 146 329 329 TRP TRP A . n 
A 1 147 LYS 147 330 330 LYS LYS A . n 
A 1 148 MET 148 331 331 MET MET A . n 
A 1 149 VAL 149 332 332 VAL VAL A . n 
A 1 150 ASP 150 333 333 ASP ASP A . n 
A 1 151 ASP 151 334 334 ASP ASP A . n 
A 1 152 ASP 152 335 335 ASP ASP A . n 
A 1 153 THR 153 336 336 THR THR A . n 
A 1 154 LEU 154 337 337 LEU LEU A . n 
A 1 155 GLU 155 338 338 GLU GLU A . n 
A 1 156 VAL 156 339 339 VAL VAL A . n 
A 1 157 ASP 157 340 340 ASP ASP A . n 
A 1 158 GLY 158 341 341 GLY GLY A . n 
A 1 159 LYS 159 342 342 LYS LYS A . n 
A 1 160 THR 160 343 343 THR THR A . n 
A 1 161 MET 161 344 344 MET MET A . n 
A 1 162 THR 162 345 345 THR THR A . n 
A 1 163 LYS 163 346 346 LYS LYS A . n 
A 1 164 PRO 164 347 347 PRO PRO A . n 
A 1 165 PHE 165 348 348 PHE PHE A . n 
A 1 166 VAL 166 349 349 VAL VAL A . n 
A 1 167 GLU 167 350 350 GLU GLU A . n 
A 1 168 LYS 168 351 351 LYS LYS A . n 
A 1 169 PRO 169 352 352 PRO PRO A . n 
A 1 170 VAL 170 353 353 VAL VAL A . n 
A 1 171 ASP 171 354 354 ASP ASP A . n 
A 1 172 GLY 172 355 355 GLY GLY A . n 
A 1 173 GLU 173 356 356 GLU GLU A . n 
A 1 174 ASP 174 357 357 ASP ASP A . n 
A 1 175 HIS 175 358 358 HIS HIS A . n 
A 1 176 ASN 176 359 359 ASN ASN A . n 
A 1 177 ILE 177 360 360 ILE ILE A . n 
A 1 178 TYR 178 361 361 TYR TYR A . n 
A 1 179 ILE 179 362 362 ILE ILE A . n 
A 1 180 TYR 180 363 363 TYR TYR A . n 
A 1 181 TYR 181 364 364 TYR TYR A . n 
A 1 182 HIS 182 365 365 HIS HIS A . n 
A 1 183 SER 183 366 366 SER SER A . n 
A 1 184 LYS 184 367 367 LYS LYS A . n 
A 1 185 ASN 185 368 368 ASN ASN A . n 
A 1 186 GLY 186 369 369 GLY GLY A . n 
A 1 187 GLY 187 370 370 GLY GLY A . n 
A 1 188 GLY 188 371 371 GLY GLY A . n 
A 1 189 GLY 189 372 372 GLY GLY A . n 
A 1 190 ARG 190 373 373 ARG ARG A . n 
A 1 191 ARG 191 374 374 ARG ARG A . n 
A 1 192 LEU 192 375 375 LEU LEU A . n 
A 1 193 PHE 193 376 376 PHE PHE A . n 
A 1 194 ARG 194 377 377 ARG ARG A . n 
A 1 195 LYS 195 378 378 LYS LYS A . n 
A 1 196 VAL 196 379 379 VAL VAL A . n 
A 1 197 GLY 197 380 380 GLY GLY A . n 
A 1 198 ASN 198 381 381 ASN ASN A . n 
A 1 199 LYS 199 382 382 LYS LYS A . n 
A 1 200 SER 200 383 383 SER SER A . n 
A 1 201 SER 201 384 384 SER SER A . n 
A 1 202 GLU 202 385 385 GLU GLU A . n 
A 1 203 PHE 203 386 386 PHE PHE A . n 
A 1 204 ASP 204 387 387 ASP ASP A . n 
A 1 205 PRO 205 388 388 PRO PRO A . n 
A 1 206 THR 206 389 389 THR THR A . n 
A 1 207 LEU 207 390 390 LEU LEU A . n 
A 1 208 VAL 208 391 391 VAL VAL A . n 
A 1 209 HIS 209 392 392 HIS HIS A . n 
A 1 210 PRO 210 393 393 PRO PRO A . n 
A 1 211 ARG 211 394 394 ARG ARG A . n 
A 1 212 THR 212 395 395 THR THR A . n 
A 1 213 GLU 213 396 396 GLU GLU A . n 
A 1 214 GLY 214 397 397 GLY GLY A . n 
A 1 215 SER 215 398 398 SER SER A . n 
A 1 216 TYR 216 399 399 TYR TYR A . n 
A 1 217 ILE 217 400 400 ILE ILE A . n 
A 1 218 TYR 218 401 401 TYR TYR A . n 
A 1 219 GLU 219 402 402 GLU GLU A . n 
A 1 220 GLN 220 403 403 GLN GLN A . n 
A 1 221 PHE 221 404 404 PHE PHE A . n 
A 1 222 MET 222 405 405 MET MET A . n 
A 1 223 ASP 223 406 406 ASP ASP A . n 
A 1 224 THR 224 407 407 THR THR A . n 
A 1 225 ASP 225 408 408 ASP ASP A . n 
A 1 226 ASN 226 409 409 ASN ASN A . n 
A 1 227 PHE 227 410 410 PHE PHE A . n 
A 1 228 GLU 228 411 411 GLU GLU A . n 
A 1 229 ASP 229 412 412 ASP ASP A . n 
A 1 230 VAL 230 413 413 VAL VAL A . n 
A 1 231 LYS 231 414 414 LYS LYS A . n 
A 1 232 ALA 232 415 415 ALA ALA A . n 
A 1 233 TYR 233 416 416 TYR TYR A . n 
A 1 234 THR 234 417 417 THR THR A . n 
A 1 235 ILE 235 418 418 ILE ILE A . n 
A 1 236 GLY 236 419 419 GLY GLY A . n 
A 1 237 GLU 237 420 420 GLU GLU A . n 
A 1 238 ASN 238 421 421 ASN ASN A . n 
A 1 239 PHE 239 422 422 PHE PHE A . n 
A 1 240 CYS 240 423 423 CYS CYS A . n 
A 1 241 HIS 241 424 424 HIS HIS A . n 
A 1 242 ALA 242 425 425 ALA ALA A . n 
A 1 243 GLU 243 426 426 GLU GLU A . n 
A 1 244 THR 244 427 427 THR THR A . n 
A 1 245 ARG 245 428 428 ARG ARG A . n 
A 1 246 LYS 246 429 429 LYS LYS A . n 
A 1 247 SER 247 430 430 SER SER A . n 
A 1 248 PRO 248 431 431 PRO PRO A . n 
A 1 249 VAL 249 432 432 VAL VAL A . n 
A 1 250 VAL 250 433 433 VAL VAL A . n 
A 1 251 ASP 251 434 434 ASP ASP A . n 
A 1 252 GLY 252 435 435 GLY GLY A . n 
A 1 253 ILE 253 436 436 ILE ILE A . n 
A 1 254 VAL 254 437 437 VAL VAL A . n 
A 1 255 ARG 255 438 438 ARG ARG A . n 
A 1 256 ARG 256 439 439 ARG ARG A . n 
A 1 257 ASN 257 440 440 ASN ASN A . n 
A 1 258 THR 258 441 441 THR THR A . n 
A 1 259 HIS 259 442 442 HIS HIS A . n 
A 1 260 GLY 260 443 443 GLY GLY A . n 
A 1 261 LYS 261 444 444 LYS LYS A . n 
A 1 262 GLU 262 445 445 GLU GLU A . n 
A 1 263 VAL 263 446 446 VAL VAL A . n 
A 1 264 ARG 264 447 447 ARG ARG A . n 
A 1 265 TYR 265 448 448 TYR TYR A . n 
A 1 266 ILE 266 449 449 ILE ILE A . n 
A 1 267 THR 267 450 450 THR THR A . n 
A 1 268 GLU 268 451 451 GLU GLU A . n 
A 1 269 LEU 269 452 452 LEU LEU A . n 
A 1 270 SER 270 453 453 SER SER A . n 
A 1 271 ASP 271 454 454 ASP ASP A . n 
A 1 272 GLU 272 455 455 GLU GLU A . n 
A 1 273 GLU 273 456 456 GLU GLU A . n 
A 1 274 LYS 274 457 457 LYS LYS A . n 
A 1 275 THR 275 458 458 THR THR A . n 
A 1 276 ILE 276 459 459 ILE ILE A . n 
A 1 277 ALA 277 460 460 ALA ALA A . n 
A 1 278 GLY 278 461 461 GLY GLY A . n 
A 1 279 LYS 279 462 462 LYS LYS A . n 
A 1 280 VAL 280 463 463 VAL VAL A . n 
A 1 281 SER 281 464 464 SER SER A . n 
A 1 282 LYS 282 465 465 LYS LYS A . n 
A 1 283 ALA 283 466 466 ALA ALA A . n 
A 1 284 PHE 284 467 467 PHE PHE A . n 
A 1 285 SER 285 468 468 SER SER A . n 
A 1 286 GLN 286 469 469 GLN GLN A . n 
A 1 287 MET 287 470 470 MET MET A . n 
A 1 288 ILE 288 471 471 ILE ILE A . n 
A 1 289 CYS 289 472 472 CYS CYS A . n 
A 1 290 GLY 290 473 473 GLY GLY A . n 
A 1 291 PHE 291 474 474 PHE PHE A . n 
A 1 292 ASP 292 475 475 ASP ASP A . n 
A 1 293 LEU 293 476 476 LEU LEU A . n 
A 1 294 LEU 294 477 477 LEU LEU A . n 
A 1 295 ARG 295 478 478 ARG ARG A . n 
A 1 296 VAL 296 479 479 VAL VAL A . n 
A 1 297 SER 297 480 480 SER SER A . n 
A 1 298 GLY 298 481 481 GLY GLY A . n 
A 1 299 LYS 299 482 482 LYS LYS A . n 
A 1 300 SER 300 483 483 SER SER A . n 
A 1 301 TYR 301 484 484 TYR TYR A . n 
A 1 302 VAL 302 485 485 VAL VAL A . n 
A 1 303 ILE 303 486 486 ILE ILE A . n 
A 1 304 ASP 304 487 487 ASP ASP A . n 
A 1 305 VAL 305 488 488 VAL VAL A . n 
A 1 306 ASN 306 489 489 ASN ASN A . n 
A 1 307 GLY 307 490 490 GLY GLY A . n 
A 1 308 PHE 308 491 491 PHE PHE A . n 
A 1 309 SER 309 492 492 SER SER A . n 
A 1 310 PHE 310 493 493 PHE PHE A . n 
A 1 311 VAL 311 494 494 VAL VAL A . n 
A 1 312 LYS 312 495 495 LYS LYS A . n 
A 1 313 ASP 313 496 496 ASP ASP A . n 
A 1 314 ASN 314 497 497 ASN ASN A . n 
A 1 315 LYS 315 498 498 LYS LYS A . n 
A 1 316 ALA 316 499 499 ALA ALA A . n 
A 1 317 TYR 317 500 500 TYR TYR A . n 
A 1 318 TYR 318 501 501 TYR TYR A . n 
A 1 319 ASP 319 502 502 ASP ASP A . n 
A 1 320 SER 320 503 503 SER SER A . n 
A 1 321 CYS 321 504 504 CYS CYS A . n 
A 1 322 ALA 322 505 505 ALA ALA A . n 
A 1 323 ASN 323 506 506 ASN ASN A . n 
A 1 324 ILE 324 507 507 ILE ILE A . n 
A 1 325 LEU 325 508 508 LEU LEU A . n 
A 1 326 ARG 326 509 509 ARG ARG A . n 
A 1 327 SER 327 510 510 SER SER A . n 
A 1 328 THR 328 511 511 THR THR A . n 
A 1 329 PHE 329 512 512 PHE PHE A . n 
A 1 330 ILE 330 513 513 ILE ILE A . n 
A 1 331 GLU 331 514 514 GLU GLU A . n 
A 1 332 ALA 332 515 515 ALA ALA A . n 
A 1 333 LYS 333 516 516 LYS LYS A . n 
A 1 334 LYS 334 517 517 LYS LYS A . n 
A 1 335 LYS 335 518 518 LYS LYS A . n 
A 1 336 MET 336 519 519 MET MET A . n 
A 1 337 ASP 337 520 520 ASP ASP A . 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 
B 2 ADP 1   600  600 ADP ADP A . 
C 3 EDO 1   601  601 EDO EDO A . 
D 3 EDO 1   602  602 EDO EDO A . 
E 3 EDO 1   603  603 EDO EDO A . 
F 3 EDO 1   604  604 EDO EDO A . 
G 3 EDO 1   605  605 EDO EDO A . 
H 4 HOH 1   701  257 HOH HOH A . 
H 4 HOH 2   702  295 HOH HOH A . 
H 4 HOH 3   703  296 HOH HOH A . 
H 4 HOH 4   704  294 HOH HOH A . 
H 4 HOH 5   705  299 HOH HOH A . 
H 4 HOH 6   706  298 HOH HOH A . 
H 4 HOH 7   707  193 HOH HOH A . 
H 4 HOH 8   708  302 HOH HOH A . 
H 4 HOH 9   709  138 HOH HOH A . 
H 4 HOH 10  710  290 HOH HOH A . 
H 4 HOH 11  711  205 HOH HOH A . 
H 4 HOH 12  712  337 HOH HOH A . 
H 4 HOH 13  713  352 HOH HOH A . 
H 4 HOH 14  714  334 HOH HOH A . 
H 4 HOH 15  715  341 HOH HOH A . 
H 4 HOH 16  716  186 HOH HOH A . 
H 4 HOH 17  717  321 HOH HOH A . 
H 4 HOH 18  718  43  HOH HOH A . 
H 4 HOH 19  719  128 HOH HOH A . 
H 4 HOH 20  720  369 HOH HOH A . 
H 4 HOH 21  721  329 HOH HOH A . 
H 4 HOH 22  722  318 HOH HOH A . 
H 4 HOH 23  723  73  HOH HOH A . 
H 4 HOH 24  724  366 HOH HOH A . 
H 4 HOH 25  725  307 HOH HOH A . 
H 4 HOH 26  726  18  HOH HOH A . 
H 4 HOH 27  727  111 HOH HOH A . 
H 4 HOH 28  728  340 HOH HOH A . 
H 4 HOH 29  729  277 HOH HOH A . 
H 4 HOH 30  730  283 HOH HOH A . 
H 4 HOH 31  731  306 HOH HOH A . 
H 4 HOH 32  732  71  HOH HOH A . 
H 4 HOH 33  733  238 HOH HOH A . 
H 4 HOH 34  734  268 HOH HOH A . 
H 4 HOH 35  735  262 HOH HOH A . 
H 4 HOH 36  736  344 HOH HOH A . 
H 4 HOH 37  737  107 HOH HOH A . 
H 4 HOH 38  738  26  HOH HOH A . 
H 4 HOH 39  739  184 HOH HOH A . 
H 4 HOH 40  740  161 HOH HOH A . 
H 4 HOH 41  741  147 HOH HOH A . 
H 4 HOH 42  742  151 HOH HOH A . 
H 4 HOH 43  743  326 HOH HOH A . 
H 4 HOH 44  744  169 HOH HOH A . 
H 4 HOH 45  745  8   HOH HOH A . 
H 4 HOH 46  746  250 HOH HOH A . 
H 4 HOH 47  747  5   HOH HOH A . 
H 4 HOH 48  748  230 HOH HOH A . 
H 4 HOH 49  749  192 HOH HOH A . 
H 4 HOH 50  750  15  HOH HOH A . 
H 4 HOH 51  751  162 HOH HOH A . 
H 4 HOH 52  752  170 HOH HOH A . 
H 4 HOH 53  753  132 HOH HOH A . 
H 4 HOH 54  754  181 HOH HOH A . 
H 4 HOH 55  755  215 HOH HOH A . 
H 4 HOH 56  756  135 HOH HOH A . 
H 4 HOH 57  757  183 HOH HOH A . 
H 4 HOH 58  758  104 HOH HOH A . 
H 4 HOH 59  759  49  HOH HOH A . 
H 4 HOH 60  760  47  HOH HOH A . 
H 4 HOH 61  761  72  HOH HOH A . 
H 4 HOH 62  762  198 HOH HOH A . 
H 4 HOH 63  763  165 HOH HOH A . 
H 4 HOH 64  764  99  HOH HOH A . 
H 4 HOH 65  765  300 HOH HOH A . 
H 4 HOH 66  766  126 HOH HOH A . 
H 4 HOH 67  767  129 HOH HOH A . 
H 4 HOH 68  768  117 HOH HOH A . 
H 4 HOH 69  769  109 HOH HOH A . 
H 4 HOH 70  770  29  HOH HOH A . 
H 4 HOH 71  771  19  HOH HOH A . 
H 4 HOH 72  772  11  HOH HOH A . 
H 4 HOH 73  773  85  HOH HOH A . 
H 4 HOH 74  774  232 HOH HOH A . 
H 4 HOH 75  775  12  HOH HOH A . 
H 4 HOH 76  776  286 HOH HOH A . 
H 4 HOH 77  777  36  HOH HOH A . 
H 4 HOH 78  778  28  HOH HOH A . 
H 4 HOH 79  779  3   HOH HOH A . 
H 4 HOH 80  780  105 HOH HOH A . 
H 4 HOH 81  781  164 HOH HOH A . 
H 4 HOH 82  782  10  HOH HOH A . 
H 4 HOH 83  783  74  HOH HOH A . 
H 4 HOH 84  784  16  HOH HOH A . 
H 4 HOH 85  785  67  HOH HOH A . 
H 4 HOH 86  786  187 HOH HOH A . 
H 4 HOH 87  787  2   HOH HOH A . 
H 4 HOH 88  788  20  HOH HOH A . 
H 4 HOH 89  789  233 HOH HOH A . 
H 4 HOH 90  790  62  HOH HOH A . 
H 4 HOH 91  791  284 HOH HOH A . 
H 4 HOH 92  792  322 HOH HOH A . 
H 4 HOH 93  793  50  HOH HOH A . 
H 4 HOH 94  794  124 HOH HOH A . 
H 4 HOH 95  795  102 HOH HOH A . 
H 4 HOH 96  796  84  HOH HOH A . 
H 4 HOH 97  797  144 HOH HOH A . 
H 4 HOH 98  798  177 HOH HOH A . 
H 4 HOH 99  799  336 HOH HOH A . 
H 4 HOH 100 800  143 HOH HOH A . 
H 4 HOH 101 801  66  HOH HOH A . 
H 4 HOH 102 802  42  HOH HOH A . 
H 4 HOH 103 803  56  HOH HOH A . 
H 4 HOH 104 804  38  HOH HOH A . 
H 4 HOH 105 805  224 HOH HOH A . 
H 4 HOH 106 806  145 HOH HOH A . 
H 4 HOH 107 807  292 HOH HOH A . 
H 4 HOH 108 808  14  HOH HOH A . 
H 4 HOH 109 809  52  HOH HOH A . 
H 4 HOH 110 810  133 HOH HOH A . 
H 4 HOH 111 811  311 HOH HOH A . 
H 4 HOH 112 812  27  HOH HOH A . 
H 4 HOH 113 813  79  HOH HOH A . 
H 4 HOH 114 814  282 HOH HOH A . 
H 4 HOH 115 815  61  HOH HOH A . 
H 4 HOH 116 816  317 HOH HOH A . 
H 4 HOH 117 817  188 HOH HOH A . 
H 4 HOH 118 818  37  HOH HOH A . 
H 4 HOH 119 819  7   HOH HOH A . 
H 4 HOH 120 820  86  HOH HOH A . 
H 4 HOH 121 821  44  HOH HOH A . 
H 4 HOH 122 822  6   HOH HOH A . 
H 4 HOH 123 823  57  HOH HOH A . 
H 4 HOH 124 824  119 HOH HOH A . 
H 4 HOH 125 825  220 HOH HOH A . 
H 4 HOH 126 826  240 HOH HOH A . 
H 4 HOH 127 827  136 HOH HOH A . 
H 4 HOH 128 828  31  HOH HOH A . 
H 4 HOH 129 829  303 HOH HOH A . 
H 4 HOH 130 830  241 HOH HOH A . 
H 4 HOH 131 831  259 HOH HOH A . 
H 4 HOH 132 832  163 HOH HOH A . 
H 4 HOH 133 833  365 HOH HOH A . 
H 4 HOH 134 834  4   HOH HOH A . 
H 4 HOH 135 835  90  HOH HOH A . 
H 4 HOH 136 836  24  HOH HOH A . 
H 4 HOH 137 837  293 HOH HOH A . 
H 4 HOH 138 838  81  HOH HOH A . 
H 4 HOH 139 839  360 HOH HOH A . 
H 4 HOH 140 840  213 HOH HOH A . 
H 4 HOH 141 841  171 HOH HOH A . 
H 4 HOH 142 842  46  HOH HOH A . 
H 4 HOH 143 843  34  HOH HOH A . 
H 4 HOH 144 844  115 HOH HOH A . 
H 4 HOH 145 845  353 HOH HOH A . 
H 4 HOH 146 846  125 HOH HOH A . 
H 4 HOH 147 847  1   HOH HOH A . 
H 4 HOH 148 848  320 HOH HOH A . 
H 4 HOH 149 849  287 HOH HOH A . 
H 4 HOH 150 850  92  HOH HOH A . 
H 4 HOH 151 851  158 HOH HOH A . 
H 4 HOH 152 852  260 HOH HOH A . 
H 4 HOH 153 853  305 HOH HOH A . 
H 4 HOH 154 854  32  HOH HOH A . 
H 4 HOH 155 855  113 HOH HOH A . 
H 4 HOH 156 856  23  HOH HOH A . 
H 4 HOH 157 857  191 HOH HOH A . 
H 4 HOH 158 858  200 HOH HOH A . 
H 4 HOH 159 859  266 HOH HOH A . 
H 4 HOH 160 860  59  HOH HOH A . 
H 4 HOH 161 861  194 HOH HOH A . 
H 4 HOH 162 862  176 HOH HOH A . 
H 4 HOH 163 863  173 HOH HOH A . 
H 4 HOH 164 864  35  HOH HOH A . 
H 4 HOH 165 865  110 HOH HOH A . 
H 4 HOH 166 866  239 HOH HOH A . 
H 4 HOH 167 867  316 HOH HOH A . 
H 4 HOH 168 868  88  HOH HOH A . 
H 4 HOH 169 869  53  HOH HOH A . 
H 4 HOH 170 870  51  HOH HOH A . 
H 4 HOH 171 871  195 HOH HOH A . 
H 4 HOH 172 872  33  HOH HOH A . 
H 4 HOH 173 873  41  HOH HOH A . 
H 4 HOH 174 874  252 HOH HOH A . 
H 4 HOH 175 875  80  HOH HOH A . 
H 4 HOH 176 876  116 HOH HOH A . 
H 4 HOH 177 877  22  HOH HOH A . 
H 4 HOH 178 878  357 HOH HOH A . 
H 4 HOH 179 879  103 HOH HOH A . 
H 4 HOH 180 880  189 HOH HOH A . 
H 4 HOH 181 881  118 HOH HOH A . 
H 4 HOH 182 882  308 HOH HOH A . 
H 4 HOH 183 883  297 HOH HOH A . 
H 4 HOH 184 884  180 HOH HOH A . 
H 4 HOH 185 885  167 HOH HOH A . 
H 4 HOH 186 886  160 HOH HOH A . 
H 4 HOH 187 887  55  HOH HOH A . 
H 4 HOH 188 888  345 HOH HOH A . 
H 4 HOH 189 889  159 HOH HOH A . 
H 4 HOH 190 890  139 HOH HOH A . 
H 4 HOH 191 891  325 HOH HOH A . 
H 4 HOH 192 892  78  HOH HOH A . 
H 4 HOH 193 893  267 HOH HOH A . 
H 4 HOH 194 894  190 HOH HOH A . 
H 4 HOH 195 895  25  HOH HOH A . 
H 4 HOH 196 896  288 HOH HOH A . 
H 4 HOH 197 897  166 HOH HOH A . 
H 4 HOH 198 898  175 HOH HOH A . 
H 4 HOH 199 899  39  HOH HOH A . 
H 4 HOH 200 900  87  HOH HOH A . 
H 4 HOH 201 901  120 HOH HOH A . 
H 4 HOH 202 902  235 HOH HOH A . 
H 4 HOH 203 903  359 HOH HOH A . 
H 4 HOH 204 904  155 HOH HOH A . 
H 4 HOH 205 905  178 HOH HOH A . 
H 4 HOH 206 906  364 HOH HOH A . 
H 4 HOH 207 907  356 HOH HOH A . 
H 4 HOH 208 908  76  HOH HOH A . 
H 4 HOH 209 909  54  HOH HOH A . 
H 4 HOH 210 910  153 HOH HOH A . 
H 4 HOH 211 911  245 HOH HOH A . 
H 4 HOH 212 912  106 HOH HOH A . 
H 4 HOH 213 913  58  HOH HOH A . 
H 4 HOH 214 914  60  HOH HOH A . 
H 4 HOH 215 915  248 HOH HOH A . 
H 4 HOH 216 916  91  HOH HOH A . 
H 4 HOH 217 917  17  HOH HOH A . 
H 4 HOH 218 918  112 HOH HOH A . 
H 4 HOH 219 919  304 HOH HOH A . 
H 4 HOH 220 920  156 HOH HOH A . 
H 4 HOH 221 921  251 HOH HOH A . 
H 4 HOH 222 922  179 HOH HOH A . 
H 4 HOH 223 923  273 HOH HOH A . 
H 4 HOH 224 924  258 HOH HOH A . 
H 4 HOH 225 925  142 HOH HOH A . 
H 4 HOH 226 926  255 HOH HOH A . 
H 4 HOH 227 927  131 HOH HOH A . 
H 4 HOH 228 928  70  HOH HOH A . 
H 4 HOH 229 929  65  HOH HOH A . 
H 4 HOH 230 930  21  HOH HOH A . 
H 4 HOH 231 931  9   HOH HOH A . 
H 4 HOH 232 932  69  HOH HOH A . 
H 4 HOH 233 933  217 HOH HOH A . 
H 4 HOH 234 934  256 HOH HOH A . 
H 4 HOH 235 935  272 HOH HOH A . 
H 4 HOH 236 936  154 HOH HOH A . 
H 4 HOH 237 937  226 HOH HOH A . 
H 4 HOH 238 938  123 HOH HOH A . 
H 4 HOH 239 939  218 HOH HOH A . 
H 4 HOH 240 940  45  HOH HOH A . 
H 4 HOH 241 941  48  HOH HOH A . 
H 4 HOH 242 942  371 HOH HOH A . 
H 4 HOH 243 943  83  HOH HOH A . 
H 4 HOH 244 944  328 HOH HOH A . 
H 4 HOH 245 945  130 HOH HOH A . 
H 4 HOH 246 946  204 HOH HOH A . 
H 4 HOH 247 947  122 HOH HOH A . 
H 4 HOH 248 948  97  HOH HOH A . 
H 4 HOH 249 949  82  HOH HOH A . 
H 4 HOH 250 950  150 HOH HOH A . 
H 4 HOH 251 951  95  HOH HOH A . 
H 4 HOH 252 952  227 HOH HOH A . 
H 4 HOH 253 953  209 HOH HOH A . 
H 4 HOH 254 954  13  HOH HOH A . 
H 4 HOH 255 955  68  HOH HOH A . 
H 4 HOH 256 956  323 HOH HOH A . 
H 4 HOH 257 957  30  HOH HOH A . 
H 4 HOH 258 958  263 HOH HOH A . 
H 4 HOH 259 959  313 HOH HOH A . 
H 4 HOH 260 960  362 HOH HOH A . 
H 4 HOH 261 961  355 HOH HOH A . 
H 4 HOH 262 962  64  HOH HOH A . 
H 4 HOH 263 963  63  HOH HOH A . 
H 4 HOH 264 964  285 HOH HOH A . 
H 4 HOH 265 965  211 HOH HOH A . 
H 4 HOH 266 966  134 HOH HOH A . 
H 4 HOH 267 967  216 HOH HOH A . 
H 4 HOH 268 968  291 HOH HOH A . 
H 4 HOH 269 969  315 HOH HOH A . 
H 4 HOH 270 970  343 HOH HOH A . 
H 4 HOH 271 971  281 HOH HOH A . 
H 4 HOH 272 972  347 HOH HOH A . 
H 4 HOH 273 973  254 HOH HOH A . 
H 4 HOH 274 974  319 HOH HOH A . 
H 4 HOH 275 975  314 HOH HOH A . 
H 4 HOH 276 976  264 HOH HOH A . 
H 4 HOH 277 977  236 HOH HOH A . 
H 4 HOH 278 978  370 HOH HOH A . 
H 4 HOH 279 979  197 HOH HOH A . 
H 4 HOH 280 980  350 HOH HOH A . 
H 4 HOH 281 981  221 HOH HOH A . 
H 4 HOH 282 982  108 HOH HOH A . 
H 4 HOH 283 983  185 HOH HOH A . 
H 4 HOH 284 984  330 HOH HOH A . 
H 4 HOH 285 985  310 HOH HOH A . 
H 4 HOH 286 986  265 HOH HOH A . 
H 4 HOH 287 987  247 HOH HOH A . 
H 4 HOH 288 988  261 HOH HOH A . 
H 4 HOH 289 989  331 HOH HOH A . 
H 4 HOH 290 990  228 HOH HOH A . 
H 4 HOH 291 991  96  HOH HOH A . 
H 4 HOH 292 992  101 HOH HOH A . 
H 4 HOH 293 993  309 HOH HOH A . 
H 4 HOH 294 994  210 HOH HOH A . 
H 4 HOH 295 995  174 HOH HOH A . 
H 4 HOH 296 996  274 HOH HOH A . 
H 4 HOH 297 997  289 HOH HOH A . 
H 4 HOH 298 998  279 HOH HOH A . 
H 4 HOH 299 999  351 HOH HOH A . 
H 4 HOH 300 1000 270 HOH HOH A . 
H 4 HOH 301 1001 335 HOH HOH A . 
H 4 HOH 302 1002 244 HOH HOH A . 
H 4 HOH 303 1003 223 HOH HOH A . 
H 4 HOH 304 1004 346 HOH HOH A . 
H 4 HOH 305 1005 149 HOH HOH A . 
H 4 HOH 306 1006 348 HOH HOH A . 
H 4 HOH 307 1007 94  HOH HOH A . 
H 4 HOH 308 1008 332 HOH HOH A . 
H 4 HOH 309 1009 40  HOH HOH A . 
H 4 HOH 310 1010 157 HOH HOH A . 
H 4 HOH 311 1011 114 HOH HOH A . 
H 4 HOH 312 1012 368 HOH HOH A . 
H 4 HOH 313 1013 206 HOH HOH A . 
H 4 HOH 314 1014 363 HOH HOH A . 
H 4 HOH 315 1015 89  HOH HOH A . 
H 4 HOH 316 1016 249 HOH HOH A . 
H 4 HOH 317 1017 148 HOH HOH A . 
H 4 HOH 318 1018 121 HOH HOH A . 
H 4 HOH 319 1019 146 HOH HOH A . 
H 4 HOH 320 1020 358 HOH HOH A . 
H 4 HOH 321 1021 214 HOH HOH A . 
H 4 HOH 322 1022 100 HOH HOH A . 
H 4 HOH 323 1023 168 HOH HOH A . 
H 4 HOH 324 1024 361 HOH HOH A . 
H 4 HOH 325 1025 152 HOH HOH A . 
H 4 HOH 326 1026 202 HOH HOH A . 
H 4 HOH 327 1027 208 HOH HOH A . 
H 4 HOH 328 1028 253 HOH HOH A . 
H 4 HOH 329 1029 327 HOH HOH A . 
H 4 HOH 330 1030 280 HOH HOH A . 
H 4 HOH 331 1031 93  HOH HOH A . 
H 4 HOH 332 1032 338 HOH HOH A . 
H 4 HOH 333 1033 271 HOH HOH A . 
H 4 HOH 334 1034 212 HOH HOH A . 
H 4 HOH 335 1035 269 HOH HOH A . 
H 4 HOH 336 1036 172 HOH HOH A . 
H 4 HOH 337 1037 201 HOH HOH A . 
H 4 HOH 338 1038 137 HOH HOH A . 
H 4 HOH 339 1039 246 HOH HOH A . 
H 4 HOH 340 1040 75  HOH HOH A . 
H 4 HOH 341 1041 349 HOH HOH A . 
H 4 HOH 342 1042 339 HOH HOH A . 
H 4 HOH 343 1043 222 HOH HOH A . 
H 4 HOH 344 1044 234 HOH HOH A . 
H 4 HOH 345 1045 127 HOH HOH A . 
H 4 HOH 346 1046 243 HOH HOH A . 
H 4 HOH 347 1047 324 HOH HOH A . 
H 4 HOH 348 1048 77  HOH HOH A . 
H 4 HOH 349 1049 301 HOH HOH A . 
H 4 HOH 350 1050 342 HOH HOH A . 
H 4 HOH 351 1051 199 HOH HOH A . 
H 4 HOH 352 1052 196 HOH HOH A . 
H 4 HOH 353 1053 278 HOH HOH A . 
H 4 HOH 354 1054 333 HOH HOH A . 
H 4 HOH 355 1055 141 HOH HOH A . 
H 4 HOH 356 1056 203 HOH HOH A . 
H 4 HOH 357 1057 140 HOH HOH A . 
H 4 HOH 358 1058 275 HOH HOH A . 
H 4 HOH 359 1059 207 HOH HOH A . 
H 4 HOH 360 1060 225 HOH HOH A . 
H 4 HOH 361 1061 237 HOH HOH A . 
H 4 HOH 362 1062 98  HOH HOH A . 
H 4 HOH 363 1063 182 HOH HOH A . 
H 4 HOH 364 1064 367 HOH HOH A . 
H 4 HOH 365 1065 229 HOH HOH A . 
H 4 HOH 366 1066 276 HOH HOH A . 
H 4 HOH 367 1067 231 HOH HOH A . 
H 4 HOH 368 1068 219 HOH HOH A . 
H 4 HOH 369 1069 242 HOH HOH A . 
H 4 HOH 370 1070 354 HOH HOH A . 
H 4 HOH 371 1071 312 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.21.1_5286: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.32 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GR8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     40.675 
_cell.length_a_esd                 ? 
_cell.length_b                     83.172 
_cell.length_b_esd                 ? 
_cell.length_c                     51.768 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9GR8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9GR8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.55 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.4 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '23 % [v/v] PEG 3,350, 0.1 M citric acid / BIS-Tris propane pH 6.4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000036 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000036 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GR8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.18 
_reflns.d_resolution_low                               43.86 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     220120 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     -3.0 
_reflns.percent_possible_obs                           97.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.104 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.18 
_reflns_shell.d_res_low                                     1.25 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.20 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             36388 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.02 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.547 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          93.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9GR8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.18 
_refine.ls_d_res_low                             43.86 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     215318 
_refine.ls_number_reflns_R_free                  10766 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.40 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1541 
_refine.ls_R_factor_R_free                       0.1829 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1526 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.55 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2715 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_refine_hist.number_atoms_solvent             371 
_refine_hist.number_atoms_total               3133 
_refine_hist.d_res_high                       1.18 
_refine_hist.d_res_low                        43.86 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  ? 2974 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.288  ? 4039 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.424 ? 1178 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.094  ? 431  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.014  ? 525  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.18 1.19  . . 305 5884 83.00  . . . . 0.3401 . . . . . . . . . . . 0.3555 
'X-RAY DIFFRACTION' 1.19 1.21  . . 323 6130 87.00  . . . . 0.3328 . . . . . . . . . . . 0.3527 
'X-RAY DIFFRACTION' 1.21 1.22  . . 333 6403 90.00  . . . . 0.3244 . . . . . . . . . . . 0.3363 
'X-RAY DIFFRACTION' 1.22 1.24  . . 335 6465 91.00  . . . . 0.2997 . . . . . . . . . . . 0.3156 
'X-RAY DIFFRACTION' 1.24 1.25  . . 345 6466 92.00  . . . . 0.2983 . . . . . . . . . . . 0.3081 
'X-RAY DIFFRACTION' 1.25 1.27  . . 346 6650 94.00  . . . . 0.2871 . . . . . . . . . . . 0.3077 
'X-RAY DIFFRACTION' 1.27 1.29  . . 349 6669 94.00  . . . . 0.2845 . . . . . . . . . . . 0.3213 
'X-RAY DIFFRACTION' 1.29 1.31  . . 355 6811 95.00  . . . . 0.2677 . . . . . . . . . . . 0.2935 
'X-RAY DIFFRACTION' 1.31 1.33  . . 358 6814 97.00  . . . . 0.2585 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 1.33 1.35  . . 359 6811 97.00  . . . . 0.2395 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 1.35 1.37  . . 359 6873 97.00  . . . . 0.2201 . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 1.37 1.40  . . 366 6892 97.00  . . . . 0.2166 . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 1.40 1.42  . . 360 6841 97.00  . . . . 0.2047 . . . . . . . . . . . 0.2265 
'X-RAY DIFFRACTION' 1.42 1.45  . . 369 6953 97.00  . . . . 0.1890 . . . . . . . . . . . 0.2370 
'X-RAY DIFFRACTION' 1.45 1.49  . . 363 6870 98.00  . . . . 0.1787 . . . . . . . . . . . 0.1992 
'X-RAY DIFFRACTION' 1.49 1.52  . . 368 6940 98.00  . . . . 0.1637 . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 1.52 1.56  . . 364 6932 98.00  . . . . 0.1595 . . . . . . . . . . . 0.1756 
'X-RAY DIFFRACTION' 1.56 1.60  . . 366 6922 98.00  . . . . 0.1526 . . . . . . . . . . . 0.1957 
'X-RAY DIFFRACTION' 1.60 1.65  . . 369 6951 99.00  . . . . 0.1432 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 1.65 1.70  . . 368 6991 98.00  . . . . 0.1347 . . . . . . . . . . . 0.1744 
'X-RAY DIFFRACTION' 1.70 1.76  . . 369 7007 99.00  . . . . 0.1298 . . . . . . . . . . . 0.1586 
'X-RAY DIFFRACTION' 1.76 1.83  . . 368 6963 99.00  . . . . 0.1206 . . . . . . . . . . . 0.1553 
'X-RAY DIFFRACTION' 1.83 1.91  . . 370 7044 99.00  . . . . 0.1142 . . . . . . . . . . . 0.1656 
'X-RAY DIFFRACTION' 1.91 2.02  . . 372 7025 99.00  . . . . 0.1211 . . . . . . . . . . . 0.1673 
'X-RAY DIFFRACTION' 2.02 2.14  . . 373 7036 99.00  . . . . 0.1117 . . . . . . . . . . . 0.1481 
'X-RAY DIFFRACTION' 2.14 2.31  . . 367 6985 100.00 . . . . 0.1097 . . . . . . . . . . . 0.1391 
'X-RAY DIFFRACTION' 2.31 2.54  . . 374 7060 99.00  . . . . 0.1197 . . . . . . . . . . . 0.1499 
'X-RAY DIFFRACTION' 2.54 2.91  . . 377 7084 100.00 . . . . 0.1338 . . . . . . . . . . . 0.1875 
'X-RAY DIFFRACTION' 2.91 3.66  . . 367 7010 100.00 . . . . 0.1357 . . . . . . . . . . . 0.1444 
'X-RAY DIFFRACTION' 3.66 43.86 . . 369 7070 100.00 . . . . 0.1459 . . . . . . . . . . . 0.1703 
# 
_struct.entry_id                     9GR8 
_struct.title                        
'Crystal structure of the N-terminal kinase domain from Saccharomyces cerevisiae Vip1 in complex with ADP.' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9GR8 
_struct_keywords.text            
;Inositol pyrophosphate, inositol pyrophosphate phosphatase, histidine acid phosphatase, phytase, enzyme mechanism, GAF domain, phosphate homeostasis, BIOSYNTHETIC PROTEIN
;
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    VIP1_YEAST 
_struct_ref.pdbx_db_accession          Q06685 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KVGKIGVCAMDAKVLSKPMRHILNRLIEHGEFETVIFGDKVILDERIENWPTCDFLISFFSSGFPLDKAIKYVKLRKPFI
INDLIMQKILWDRRLCLQVLEAYNVPTPPRLEISRDGGPRANEELRAKLREHGVEVKPVEEPEWKMVDDDTLEVDGKTMT
KPFVEKPVDGEDHNIYIYYHSKNGGGGRRLFRKVGNKSSEFDPTLVHPRTEGSYIYEQFMDTDNFEDVKAYTIGENFCHA
ETRKSPVVDGIVRRNTHGKEVRYITELSDEEKTIAGKVSKAFSQMICGFDLLRVSGKSYVIDVNGFSFVKDNKAYYDSCA
NILRSTFIEAKKKMD
;
_struct_ref.pdbx_align_begin           186 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GR8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 337 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q06685 
_struct_ref_seq.db_align_beg                  186 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  520 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       186 
_struct_ref_seq.pdbx_auth_seq_align_end       520 
# 
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 9GR8 GLY A 1 ? UNP Q06685 ? ? 'expression tag' 184 1 
1 9GR8 ALA A 2 ? UNP Q06685 ? ? 'expression tag' 185 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1540  ? 
1 MORE         5     ? 
1 'SSA (A^2)'  16400 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 MET A 12  ? LEU A 17  ? MET A 195 LEU A 200 1 ? 6  
HELX_P HELX_P2  AA2 SER A 18  ? GLU A 30  ? SER A 201 GLU A 213 1 ? 13 
HELX_P HELX_P3  AA3 GLY A 40  ? GLU A 47  ? GLY A 223 GLU A 230 1 ? 8  
HELX_P HELX_P4  AA4 ARG A 48  ? TRP A 52  ? ARG A 231 TRP A 235 5 ? 5  
HELX_P HELX_P5  AA5 PRO A 67  ? LYS A 79  ? PRO A 250 LYS A 262 1 ? 13 
HELX_P HELX_P6  AA6 LEU A 86  ? TRP A 93  ? LEU A 269 TRP A 276 5 ? 8  
HELX_P HELX_P7  AA7 ASP A 94  ? TYR A 105 ? ASP A 277 TYR A 288 1 ? 12 
HELX_P HELX_P8  AA8 ASN A 124 ? HIS A 134 ? ASN A 307 HIS A 317 1 ? 11 
HELX_P HELX_P9  AA9 HIS A 182 ? GLY A 186 ? HIS A 365 GLY A 369 5 ? 5  
HELX_P HELX_P10 AB1 THR A 224 ? ASN A 226 ? THR A 407 ASN A 409 5 ? 3  
HELX_P HELX_P11 AB2 SER A 270 ? SER A 285 ? SER A 453 SER A 468 1 ? 16 
HELX_P HELX_P12 AB3 ASN A 314 ? ASP A 337 ? ASN A 497 ASP A 520 1 ? 24 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LYS 
_struct_mon_prot_cis.label_seq_id           163 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LYS 
_struct_mon_prot_cis.auth_seq_id            346 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    164 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     347 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       6.07 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 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 
AA1 1 PHE A 34  ? ILE A 38  ? PHE A 217 ILE A 221 
AA1 2 GLY A 5   ? CYS A 10  ? GLY A 188 CYS A 193 
AA1 3 PHE A 57  ? SER A 60  ? PHE A 240 SER A 243 
AA1 4 PHE A 81  ? ILE A 82  ? PHE A 264 ILE A 265 
AA2 1 ARG A 112 ? ILE A 115 ? ARG A 295 ILE A 298 
AA2 2 TYR A 216 ? GLN A 220 ? TYR A 399 GLN A 403 
AA2 3 PHE A 165 ? PRO A 169 ? PHE A 348 PRO A 352 
AA2 4 TYR A 178 ? TYR A 180 ? TYR A 361 TYR A 363 
AA2 5 GLY A 189 ? LYS A 195 ? GLY A 372 LYS A 378 
AA2 6 ASN A 198 ? ASP A 204 ? ASN A 381 ASP A 387 
AA3 1 TRP A 146 ? ASP A 150 ? TRP A 329 ASP A 333 
AA3 2 THR A 153 ? VAL A 156 ? THR A 336 VAL A 339 
AA3 3 LYS A 159 ? THR A 162 ? LYS A 342 THR A 345 
AA4 1 TYR A 265 ? ILE A 266 ? TYR A 448 ILE A 449 
AA4 2 CYS A 240 ? LYS A 246 ? CYS A 423 LYS A 429 
AA4 3 GLU A 228 ? ILE A 235 ? GLU A 411 ILE A 418 
AA4 4 ILE A 288 ? VAL A 296 ? ILE A 471 VAL A 479 
AA4 5 LYS A 299 ? GLY A 307 ? LYS A 482 GLY A 490 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 35  ? O GLU A 218 N ILE A 7   ? N ILE A 190 
AA1 2 3 N GLY A 8   ? N GLY A 191 O ILE A 59  ? O ILE A 242 
AA1 3 4 N LEU A 58  ? N LEU A 241 O PHE A 81  ? O PHE A 264 
AA2 1 2 N LEU A 113 ? N LEU A 296 O TYR A 218 ? O TYR A 401 
AA2 2 3 O ILE A 217 ? O ILE A 400 N LYS A 168 ? N LYS A 351 
AA2 3 4 N GLU A 167 ? N GLU A 350 O TYR A 178 ? O TYR A 361 
AA2 4 5 N ILE A 179 ? N ILE A 362 O ARG A 190 ? O ARG A 373 
AA2 5 6 N LYS A 195 ? N LYS A 378 O ASN A 198 ? O ASN A 381 
AA3 1 2 N LYS A 147 ? N LYS A 330 O GLU A 155 ? O GLU A 338 
AA3 2 3 N VAL A 156 ? N VAL A 339 O LYS A 159 ? O LYS A 342 
AA4 1 2 O TYR A 265 ? O TYR A 448 N THR A 244 ? N THR A 427 
AA4 2 3 O GLU A 243 ? O GLU A 426 N LYS A 231 ? N LYS A 414 
AA4 3 4 N THR A 234 ? N THR A 417 O CYS A 289 ? O CYS A 472 
AA4 4 5 N VAL A 296 ? N VAL A 479 O LYS A 299 ? O LYS A 482 
# 
_pdbx_entry_details.entry_id                   9GR8 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 717 ? ? O A HOH 882 ? ? 2.14 
2 1 OD2 A ASP 487 ? A O A HOH 701 ? ? 2.16 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A PHE 512 ? ? CG  A PHE 512 ? ? CD2 A PHE 512 ? ? 127.02 120.80 6.22  0.70 N 
2 1 CG A PHE 512 ? ? CD2 A PHE 512 ? ? CE2 A PHE 512 ? ? 131.30 120.80 10.50 1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 222 ? ? -96.73  -67.70 
2 1 VAL A 391 ? ? -134.52 -38.33 
3 1 ASN A 409 ? ? 56.69   19.37  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     231 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.090 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1070 ? 6.59 . 
2 1 O ? A HOH 1071 ? 6.78 . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P N N 1   
ADP O1B    O N N 2   
ADP O2B    O N N 3   
ADP O3B    O N N 4   
ADP PA     P N S 5   
ADP O1A    O N N 6   
ADP O2A    O N N 7   
ADP O3A    O N N 8   
ADP "O5'"  O N N 9   
ADP "C5'"  C N N 10  
ADP "C4'"  C N R 11  
ADP "O4'"  O N N 12  
ADP "C3'"  C N S 13  
ADP "O3'"  O N N 14  
ADP "C2'"  C N R 15  
ADP "O2'"  O N N 16  
ADP "C1'"  C N R 17  
ADP N9     N Y N 18  
ADP C8     C Y N 19  
ADP N7     N Y N 20  
ADP C5     C Y N 21  
ADP C6     C Y N 22  
ADP N6     N N N 23  
ADP N1     N Y N 24  
ADP C2     C Y N 25  
ADP N3     N Y N 26  
ADP C4     C Y N 27  
ADP HOB2   H N N 28  
ADP HOB3   H N N 29  
ADP HOA2   H N N 30  
ADP "H5'1" H N N 31  
ADP "H5'2" H N N 32  
ADP "H4'"  H N N 33  
ADP "H3'"  H N N 34  
ADP "HO3'" H N N 35  
ADP "H2'"  H N N 36  
ADP "HO2'" H N N 37  
ADP "H1'"  H N N 38  
ADP H8     H N N 39  
ADP HN61   H N N 40  
ADP HN62   H N N 41  
ADP H2     H N N 42  
ALA N      N N N 43  
ALA CA     C N S 44  
ALA C      C N N 45  
ALA O      O N N 46  
ALA CB     C N N 47  
ALA OXT    O N N 48  
ALA H      H N N 49  
ALA H2     H N N 50  
ALA HA     H N N 51  
ALA HB1    H N N 52  
ALA HB2    H N N 53  
ALA HB3    H N N 54  
ALA HXT    H N N 55  
ARG N      N N N 56  
ARG CA     C N S 57  
ARG C      C N N 58  
ARG O      O N N 59  
ARG CB     C N N 60  
ARG CG     C N N 61  
ARG CD     C N N 62  
ARG NE     N N N 63  
ARG CZ     C N N 64  
ARG NH1    N N N 65  
ARG NH2    N N N 66  
ARG OXT    O N N 67  
ARG H      H N N 68  
ARG H2     H N N 69  
ARG HA     H N N 70  
ARG HB2    H N N 71  
ARG HB3    H N N 72  
ARG HG2    H N N 73  
ARG HG3    H N N 74  
ARG HD2    H N N 75  
ARG HD3    H N N 76  
ARG HE     H N N 77  
ARG HH11   H N N 78  
ARG HH12   H N N 79  
ARG HH21   H N N 80  
ARG HH22   H N N 81  
ARG HXT    H N N 82  
ASN N      N N N 83  
ASN CA     C N S 84  
ASN C      C N N 85  
ASN O      O N N 86  
ASN CB     C N N 87  
ASN CG     C N N 88  
ASN OD1    O N N 89  
ASN ND2    N N N 90  
ASN OXT    O N N 91  
ASN H      H N N 92  
ASN H2     H N N 93  
ASN HA     H N N 94  
ASN HB2    H N N 95  
ASN HB3    H N N 96  
ASN HD21   H N N 97  
ASN HD22   H N N 98  
ASN HXT    H N N 99  
ASP N      N N N 100 
ASP CA     C N S 101 
ASP C      C N N 102 
ASP O      O N N 103 
ASP CB     C N N 104 
ASP CG     C N N 105 
ASP OD1    O N N 106 
ASP OD2    O N N 107 
ASP OXT    O N N 108 
ASP H      H N N 109 
ASP H2     H N N 110 
ASP HA     H N N 111 
ASP HB2    H N N 112 
ASP HB3    H N N 113 
ASP HD2    H N N 114 
ASP HXT    H N N 115 
CYS N      N N N 116 
CYS CA     C N R 117 
CYS C      C N N 118 
CYS O      O N N 119 
CYS CB     C N N 120 
CYS SG     S N N 121 
CYS OXT    O N N 122 
CYS H      H N N 123 
CYS H2     H N N 124 
CYS HA     H N N 125 
CYS HB2    H N N 126 
CYS HB3    H N N 127 
CYS HG     H N N 128 
CYS HXT    H N N 129 
EDO C1     C N N 130 
EDO O1     O N N 131 
EDO C2     C N N 132 
EDO O2     O N N 133 
EDO H11    H N N 134 
EDO H12    H N N 135 
EDO HO1    H N N 136 
EDO H21    H N N 137 
EDO H22    H N N 138 
EDO HO2    H N N 139 
GLN N      N N N 140 
GLN CA     C N S 141 
GLN C      C N N 142 
GLN O      O N N 143 
GLN CB     C N N 144 
GLN CG     C N N 145 
GLN CD     C N N 146 
GLN OE1    O N N 147 
GLN NE2    N N N 148 
GLN OXT    O N N 149 
GLN H      H N N 150 
GLN H2     H N N 151 
GLN HA     H N N 152 
GLN HB2    H N N 153 
GLN HB3    H N N 154 
GLN HG2    H N N 155 
GLN HG3    H N N 156 
GLN HE21   H N N 157 
GLN HE22   H N N 158 
GLN HXT    H N N 159 
GLU N      N N N 160 
GLU CA     C N S 161 
GLU C      C N N 162 
GLU O      O N N 163 
GLU CB     C N N 164 
GLU CG     C N N 165 
GLU CD     C N N 166 
GLU OE1    O N N 167 
GLU OE2    O N N 168 
GLU OXT    O N N 169 
GLU H      H N N 170 
GLU H2     H N N 171 
GLU HA     H N N 172 
GLU HB2    H N N 173 
GLU HB3    H N N 174 
GLU HG2    H N N 175 
GLU HG3    H N N 176 
GLU HE2    H N N 177 
GLU HXT    H N N 178 
GLY N      N N N 179 
GLY CA     C N N 180 
GLY C      C N N 181 
GLY O      O N N 182 
GLY OXT    O N N 183 
GLY H      H N N 184 
GLY H2     H N N 185 
GLY HA2    H N N 186 
GLY HA3    H N N 187 
GLY HXT    H N N 188 
HIS N      N N N 189 
HIS CA     C N S 190 
HIS C      C N N 191 
HIS O      O N N 192 
HIS CB     C N N 193 
HIS CG     C Y N 194 
HIS ND1    N Y N 195 
HIS CD2    C Y N 196 
HIS CE1    C Y N 197 
HIS NE2    N Y N 198 
HIS OXT    O N N 199 
HIS H      H N N 200 
HIS H2     H N N 201 
HIS HA     H N N 202 
HIS HB2    H N N 203 
HIS HB3    H N N 204 
HIS HD1    H N N 205 
HIS HD2    H N N 206 
HIS HE1    H N N 207 
HIS HE2    H N N 208 
HIS HXT    H N N 209 
HOH O      O N N 210 
HOH H1     H N N 211 
HOH H2     H N N 212 
ILE N      N N N 213 
ILE CA     C N S 214 
ILE C      C N N 215 
ILE O      O N N 216 
ILE CB     C N S 217 
ILE CG1    C N N 218 
ILE CG2    C N N 219 
ILE CD1    C N N 220 
ILE OXT    O N N 221 
ILE H      H N N 222 
ILE H2     H N N 223 
ILE HA     H N N 224 
ILE HB     H N N 225 
ILE HG12   H N N 226 
ILE HG13   H N N 227 
ILE HG21   H N N 228 
ILE HG22   H N N 229 
ILE HG23   H N N 230 
ILE HD11   H N N 231 
ILE HD12   H N N 232 
ILE HD13   H N N 233 
ILE HXT    H N N 234 
LEU N      N N N 235 
LEU CA     C N S 236 
LEU C      C N N 237 
LEU O      O N N 238 
LEU CB     C N N 239 
LEU CG     C N N 240 
LEU CD1    C N N 241 
LEU CD2    C N N 242 
LEU OXT    O N N 243 
LEU H      H N N 244 
LEU H2     H N N 245 
LEU HA     H N N 246 
LEU HB2    H N N 247 
LEU HB3    H N N 248 
LEU HG     H N N 249 
LEU HD11   H N N 250 
LEU HD12   H N N 251 
LEU HD13   H N N 252 
LEU HD21   H N N 253 
LEU HD22   H N N 254 
LEU HD23   H N N 255 
LEU HXT    H N N 256 
LYS N      N N N 257 
LYS CA     C N S 258 
LYS C      C N N 259 
LYS O      O N N 260 
LYS CB     C N N 261 
LYS CG     C N N 262 
LYS CD     C N N 263 
LYS CE     C N N 264 
LYS NZ     N N N 265 
LYS OXT    O N N 266 
LYS H      H N N 267 
LYS H2     H N N 268 
LYS HA     H N N 269 
LYS HB2    H N N 270 
LYS HB3    H N N 271 
LYS HG2    H N N 272 
LYS HG3    H N N 273 
LYS HD2    H N N 274 
LYS HD3    H N N 275 
LYS HE2    H N N 276 
LYS HE3    H N N 277 
LYS HZ1    H N N 278 
LYS HZ2    H N N 279 
LYS HZ3    H N N 280 
LYS HXT    H N N 281 
MET N      N N N 282 
MET CA     C N S 283 
MET C      C N N 284 
MET O      O N N 285 
MET CB     C N N 286 
MET CG     C N N 287 
MET SD     S N N 288 
MET CE     C N N 289 
MET OXT    O N N 290 
MET H      H N N 291 
MET H2     H N N 292 
MET HA     H N N 293 
MET HB2    H N N 294 
MET HB3    H N N 295 
MET HG2    H N N 296 
MET HG3    H N N 297 
MET HE1    H N N 298 
MET HE2    H N N 299 
MET HE3    H N N 300 
MET HXT    H N N 301 
PHE N      N N N 302 
PHE CA     C N S 303 
PHE C      C N N 304 
PHE O      O N N 305 
PHE CB     C N N 306 
PHE CG     C Y N 307 
PHE CD1    C Y N 308 
PHE CD2    C Y N 309 
PHE CE1    C Y N 310 
PHE CE2    C Y N 311 
PHE CZ     C Y N 312 
PHE OXT    O N N 313 
PHE H      H N N 314 
PHE H2     H N N 315 
PHE HA     H N N 316 
PHE HB2    H N N 317 
PHE HB3    H N N 318 
PHE HD1    H N N 319 
PHE HD2    H N N 320 
PHE HE1    H N N 321 
PHE HE2    H N N 322 
PHE HZ     H N N 323 
PHE HXT    H N N 324 
PRO N      N N N 325 
PRO CA     C N S 326 
PRO C      C N N 327 
PRO O      O N N 328 
PRO CB     C N N 329 
PRO CG     C N N 330 
PRO CD     C N N 331 
PRO OXT    O N N 332 
PRO H      H N N 333 
PRO HA     H N N 334 
PRO HB2    H N N 335 
PRO HB3    H N N 336 
PRO HG2    H N N 337 
PRO HG3    H N N 338 
PRO HD2    H N N 339 
PRO HD3    H N N 340 
PRO HXT    H N N 341 
SER N      N N N 342 
SER CA     C N S 343 
SER C      C N N 344 
SER O      O N N 345 
SER CB     C N N 346 
SER OG     O N N 347 
SER OXT    O N N 348 
SER H      H N N 349 
SER H2     H N N 350 
SER HA     H N N 351 
SER HB2    H N N 352 
SER HB3    H N N 353 
SER HG     H N N 354 
SER HXT    H N N 355 
THR N      N N N 356 
THR CA     C N S 357 
THR C      C N N 358 
THR O      O N N 359 
THR CB     C N R 360 
THR OG1    O N N 361 
THR CG2    C N N 362 
THR OXT    O N N 363 
THR H      H N N 364 
THR H2     H N N 365 
THR HA     H N N 366 
THR HB     H N N 367 
THR HG1    H N N 368 
THR HG21   H N N 369 
THR HG22   H N N 370 
THR HG23   H N N 371 
THR HXT    H N N 372 
TRP N      N N N 373 
TRP CA     C N S 374 
TRP C      C N N 375 
TRP O      O N N 376 
TRP CB     C N N 377 
TRP CG     C Y N 378 
TRP CD1    C Y N 379 
TRP CD2    C Y N 380 
TRP NE1    N Y N 381 
TRP CE2    C Y N 382 
TRP CE3    C Y N 383 
TRP CZ2    C Y N 384 
TRP CZ3    C Y N 385 
TRP CH2    C Y N 386 
TRP OXT    O N N 387 
TRP H      H N N 388 
TRP H2     H N N 389 
TRP HA     H N N 390 
TRP HB2    H N N 391 
TRP HB3    H N N 392 
TRP HD1    H N N 393 
TRP HE1    H N N 394 
TRP HE3    H N N 395 
TRP HZ2    H N N 396 
TRP HZ3    H N N 397 
TRP HH2    H N N 398 
TRP HXT    H N N 399 
TYR N      N N N 400 
TYR CA     C N S 401 
TYR C      C N N 402 
TYR O      O N N 403 
TYR CB     C N N 404 
TYR CG     C Y N 405 
TYR CD1    C Y N 406 
TYR CD2    C Y N 407 
TYR CE1    C Y N 408 
TYR CE2    C Y N 409 
TYR CZ     C Y N 410 
TYR OH     O N N 411 
TYR OXT    O N N 412 
TYR H      H N N 413 
TYR H2     H N N 414 
TYR HA     H N N 415 
TYR HB2    H N N 416 
TYR HB3    H N N 417 
TYR HD1    H N N 418 
TYR HD2    H N N 419 
TYR HE1    H N N 420 
TYR HE2    H N N 421 
TYR HH     H N N 422 
TYR HXT    H N N 423 
VAL N      N N N 424 
VAL CA     C N S 425 
VAL C      C N N 426 
VAL O      O N N 427 
VAL CB     C N N 428 
VAL CG1    C N N 429 
VAL CG2    C N N 430 
VAL OXT    O N N 431 
VAL H      H N N 432 
VAL H2     H N N 433 
VAL HA     H N N 434 
VAL HB     H N N 435 
VAL HG11   H N N 436 
VAL HG12   H N N 437 
VAL HG13   H N N 438 
VAL HG21   H N N 439 
VAL HG22   H N N 440 
VAL HG23   H N N 441 
VAL HXT    H N N 442 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
EDO C1    O1     sing N N 127 
EDO C1    C2     sing N N 128 
EDO C1    H11    sing N N 129 
EDO C1    H12    sing N N 130 
EDO O1    HO1    sing N N 131 
EDO C2    O2     sing N N 132 
EDO C2    H21    sing N N 133 
EDO C2    H22    sing N N 134 
EDO O2    HO2    sing N N 135 
GLN N     CA     sing N N 136 
GLN N     H      sing N N 137 
GLN N     H2     sing N N 138 
GLN CA    C      sing N N 139 
GLN CA    CB     sing N N 140 
GLN CA    HA     sing N N 141 
GLN C     O      doub N N 142 
GLN C     OXT    sing N N 143 
GLN CB    CG     sing N N 144 
GLN CB    HB2    sing N N 145 
GLN CB    HB3    sing N N 146 
GLN CG    CD     sing N N 147 
GLN CG    HG2    sing N N 148 
GLN CG    HG3    sing N N 149 
GLN CD    OE1    doub N N 150 
GLN CD    NE2    sing N N 151 
GLN NE2   HE21   sing N N 152 
GLN NE2   HE22   sing N N 153 
GLN OXT   HXT    sing N N 154 
GLU N     CA     sing N N 155 
GLU N     H      sing N N 156 
GLU N     H2     sing N N 157 
GLU CA    C      sing N N 158 
GLU CA    CB     sing N N 159 
GLU CA    HA     sing N N 160 
GLU C     O      doub N N 161 
GLU C     OXT    sing N N 162 
GLU CB    CG     sing N N 163 
GLU CB    HB2    sing N N 164 
GLU CB    HB3    sing N N 165 
GLU CG    CD     sing N N 166 
GLU CG    HG2    sing N N 167 
GLU CG    HG3    sing N N 168 
GLU CD    OE1    doub N N 169 
GLU CD    OE2    sing N N 170 
GLU OE2   HE2    sing N N 171 
GLU OXT   HXT    sing N N 172 
GLY N     CA     sing N N 173 
GLY N     H      sing N N 174 
GLY N     H2     sing N N 175 
GLY CA    C      sing N N 176 
GLY CA    HA2    sing N N 177 
GLY CA    HA3    sing N N 178 
GLY C     O      doub N N 179 
GLY C     OXT    sing N N 180 
GLY OXT   HXT    sing N N 181 
HIS N     CA     sing N N 182 
HIS N     H      sing N N 183 
HIS N     H2     sing N N 184 
HIS CA    C      sing N N 185 
HIS CA    CB     sing N N 186 
HIS CA    HA     sing N N 187 
HIS C     O      doub N N 188 
HIS C     OXT    sing N N 189 
HIS CB    CG     sing N N 190 
HIS CB    HB2    sing N N 191 
HIS CB    HB3    sing N N 192 
HIS CG    ND1    sing Y N 193 
HIS CG    CD2    doub Y N 194 
HIS ND1   CE1    doub Y N 195 
HIS ND1   HD1    sing N N 196 
HIS CD2   NE2    sing Y N 197 
HIS CD2   HD2    sing N N 198 
HIS CE1   NE2    sing Y N 199 
HIS CE1   HE1    sing N N 200 
HIS NE2   HE2    sing N N 201 
HIS OXT   HXT    sing N N 202 
HOH O     H1     sing N N 203 
HOH O     H2     sing N N 204 
ILE N     CA     sing N N 205 
ILE N     H      sing N N 206 
ILE N     H2     sing N N 207 
ILE CA    C      sing N N 208 
ILE CA    CB     sing N N 209 
ILE CA    HA     sing N N 210 
ILE C     O      doub N N 211 
ILE C     OXT    sing N N 212 
ILE CB    CG1    sing N N 213 
ILE CB    CG2    sing N N 214 
ILE CB    HB     sing N N 215 
ILE CG1   CD1    sing N N 216 
ILE CG1   HG12   sing N N 217 
ILE CG1   HG13   sing N N 218 
ILE CG2   HG21   sing N N 219 
ILE CG2   HG22   sing N N 220 
ILE CG2   HG23   sing N N 221 
ILE CD1   HD11   sing N N 222 
ILE CD1   HD12   sing N N 223 
ILE CD1   HD13   sing N N 224 
ILE OXT   HXT    sing N N 225 
LEU N     CA     sing N N 226 
LEU N     H      sing N N 227 
LEU N     H2     sing N N 228 
LEU CA    C      sing N N 229 
LEU CA    CB     sing N N 230 
LEU CA    HA     sing N N 231 
LEU C     O      doub N N 232 
LEU C     OXT    sing N N 233 
LEU CB    CG     sing N N 234 
LEU CB    HB2    sing N N 235 
LEU CB    HB3    sing N N 236 
LEU CG    CD1    sing N N 237 
LEU CG    CD2    sing N N 238 
LEU CG    HG     sing N N 239 
LEU CD1   HD11   sing N N 240 
LEU CD1   HD12   sing N N 241 
LEU CD1   HD13   sing N N 242 
LEU CD2   HD21   sing N N 243 
LEU CD2   HD22   sing N N 244 
LEU CD2   HD23   sing N N 245 
LEU OXT   HXT    sing N N 246 
LYS N     CA     sing N N 247 
LYS N     H      sing N N 248 
LYS N     H2     sing N N 249 
LYS CA    C      sing N N 250 
LYS CA    CB     sing N N 251 
LYS CA    HA     sing N N 252 
LYS C     O      doub N N 253 
LYS C     OXT    sing N N 254 
LYS CB    CG     sing N N 255 
LYS CB    HB2    sing N N 256 
LYS CB    HB3    sing N N 257 
LYS CG    CD     sing N N 258 
LYS CG    HG2    sing N N 259 
LYS CG    HG3    sing N N 260 
LYS CD    CE     sing N N 261 
LYS CD    HD2    sing N N 262 
LYS CD    HD3    sing N N 263 
LYS CE    NZ     sing N N 264 
LYS CE    HE2    sing N N 265 
LYS CE    HE3    sing N N 266 
LYS NZ    HZ1    sing N N 267 
LYS NZ    HZ2    sing N N 268 
LYS NZ    HZ3    sing N N 269 
LYS OXT   HXT    sing N N 270 
MET N     CA     sing N N 271 
MET N     H      sing N N 272 
MET N     H2     sing N N 273 
MET CA    C      sing N N 274 
MET CA    CB     sing N N 275 
MET CA    HA     sing N N 276 
MET C     O      doub N N 277 
MET C     OXT    sing N N 278 
MET CB    CG     sing N N 279 
MET CB    HB2    sing N N 280 
MET CB    HB3    sing N N 281 
MET CG    SD     sing N N 282 
MET CG    HG2    sing N N 283 
MET CG    HG3    sing N N 284 
MET SD    CE     sing N N 285 
MET CE    HE1    sing N N 286 
MET CE    HE2    sing N N 287 
MET CE    HE3    sing N N 288 
MET OXT   HXT    sing N N 289 
PHE N     CA     sing N N 290 
PHE N     H      sing N N 291 
PHE N     H2     sing N N 292 
PHE CA    C      sing N N 293 
PHE CA    CB     sing N N 294 
PHE CA    HA     sing N N 295 
PHE C     O      doub N N 296 
PHE C     OXT    sing N N 297 
PHE CB    CG     sing N N 298 
PHE CB    HB2    sing N N 299 
PHE CB    HB3    sing N N 300 
PHE CG    CD1    doub Y N 301 
PHE CG    CD2    sing Y N 302 
PHE CD1   CE1    sing Y N 303 
PHE CD1   HD1    sing N N 304 
PHE CD2   CE2    doub Y N 305 
PHE CD2   HD2    sing N N 306 
PHE CE1   CZ     doub Y N 307 
PHE CE1   HE1    sing N N 308 
PHE CE2   CZ     sing Y N 309 
PHE CE2   HE2    sing N N 310 
PHE CZ    HZ     sing N N 311 
PHE OXT   HXT    sing N N 312 
PRO N     CA     sing N N 313 
PRO N     CD     sing N N 314 
PRO N     H      sing N N 315 
PRO CA    C      sing N N 316 
PRO CA    CB     sing N N 317 
PRO CA    HA     sing N N 318 
PRO C     O      doub N N 319 
PRO C     OXT    sing N N 320 
PRO CB    CG     sing N N 321 
PRO CB    HB2    sing N N 322 
PRO CB    HB3    sing N N 323 
PRO CG    CD     sing N N 324 
PRO CG    HG2    sing N N 325 
PRO CG    HG3    sing N N 326 
PRO CD    HD2    sing N N 327 
PRO CD    HD3    sing N N 328 
PRO OXT   HXT    sing N N 329 
SER N     CA     sing N N 330 
SER N     H      sing N N 331 
SER N     H2     sing N N 332 
SER CA    C      sing N N 333 
SER CA    CB     sing N N 334 
SER CA    HA     sing N N 335 
SER C     O      doub N N 336 
SER C     OXT    sing N N 337 
SER CB    OG     sing N N 338 
SER CB    HB2    sing N N 339 
SER CB    HB3    sing N N 340 
SER OG    HG     sing N N 341 
SER OXT   HXT    sing N N 342 
THR N     CA     sing N N 343 
THR N     H      sing N N 344 
THR N     H2     sing N N 345 
THR CA    C      sing N N 346 
THR CA    CB     sing N N 347 
THR CA    HA     sing N N 348 
THR C     O      doub N N 349 
THR C     OXT    sing N N 350 
THR CB    OG1    sing N N 351 
THR CB    CG2    sing N N 352 
THR CB    HB     sing N N 353 
THR OG1   HG1    sing N N 354 
THR CG2   HG21   sing N N 355 
THR CG2   HG22   sing N N 356 
THR CG2   HG23   sing N N 357 
THR OXT   HXT    sing N N 358 
TRP N     CA     sing N N 359 
TRP N     H      sing N N 360 
TRP N     H2     sing N N 361 
TRP CA    C      sing N N 362 
TRP CA    CB     sing N N 363 
TRP CA    HA     sing N N 364 
TRP C     O      doub N N 365 
TRP C     OXT    sing N N 366 
TRP CB    CG     sing N N 367 
TRP CB    HB2    sing N N 368 
TRP CB    HB3    sing N N 369 
TRP CG    CD1    doub Y N 370 
TRP CG    CD2    sing Y N 371 
TRP CD1   NE1    sing Y N 372 
TRP CD1   HD1    sing N N 373 
TRP CD2   CE2    doub Y N 374 
TRP CD2   CE3    sing Y N 375 
TRP NE1   CE2    sing Y N 376 
TRP NE1   HE1    sing N N 377 
TRP CE2   CZ2    sing Y N 378 
TRP CE3   CZ3    doub Y N 379 
TRP CE3   HE3    sing N N 380 
TRP CZ2   CH2    doub Y N 381 
TRP CZ2   HZ2    sing N N 382 
TRP CZ3   CH2    sing Y N 383 
TRP CZ3   HZ3    sing N N 384 
TRP CH2   HH2    sing N N 385 
TRP OXT   HXT    sing N N 386 
TYR N     CA     sing N N 387 
TYR N     H      sing N N 388 
TYR N     H2     sing N N 389 
TYR CA    C      sing N N 390 
TYR CA    CB     sing N N 391 
TYR CA    HA     sing N N 392 
TYR C     O      doub N N 393 
TYR C     OXT    sing N N 394 
TYR CB    CG     sing N N 395 
TYR CB    HB2    sing N N 396 
TYR CB    HB3    sing N N 397 
TYR CG    CD1    doub Y N 398 
TYR CG    CD2    sing Y N 399 
TYR CD1   CE1    sing Y N 400 
TYR CD1   HD1    sing N N 401 
TYR CD2   CE2    doub Y N 402 
TYR CD2   HD2    sing N N 403 
TYR CE1   CZ     doub Y N 404 
TYR CE1   HE1    sing N N 405 
TYR CE2   CZ     sing Y N 406 
TYR CE2   HE2    sing N N 407 
TYR CZ    OH     sing N N 408 
TYR OH    HH     sing N N 409 
TYR OXT   HXT    sing N N 410 
VAL N     CA     sing N N 411 
VAL N     H      sing N N 412 
VAL N     H2     sing N N 413 
VAL CA    C      sing N N 414 
VAL CA    CB     sing N N 415 
VAL CA    HA     sing N N 416 
VAL C     O      doub N N 417 
VAL C     OXT    sing N N 418 
VAL CB    CG1    sing N N 419 
VAL CB    CG2    sing N N 420 
VAL CB    HB     sing N N 421 
VAL CG1   HG11   sing N N 422 
VAL CG1   HG12   sing N N 423 
VAL CG1   HG13   sing N N 424 
VAL CG2   HG21   sing N N 425 
VAL CG2   HG22   sing N N 426 
VAL CG2   HG23   sing N N 427 
VAL OXT   HXT    sing N N 428 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation'      Switzerland     CRSII5_209412 1 
'Howard Hughes Medical Institute (HHMI)' 'United States' 55008733      2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3T9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GR8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.024585 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001857 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012023 
_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]   0.019372 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . GLY A 1 1   ? 42.780 32.640 70.449 1.00 50.21 ? 184  GLY A N      1 
ATOM   2    C CA     . GLY A 1 1   ? 41.600 32.058 71.067 1.00 47.65 ? 184  GLY A CA     1 
ATOM   3    C C      . GLY A 1 1   ? 41.505 30.555 70.874 1.00 44.08 ? 184  GLY A C      1 
ATOM   4    O O      . GLY A 1 1   ? 42.309 29.961 70.148 1.00 44.58 ? 184  GLY A O      1 
ATOM   5    H HA2    . GLY A 1 1   ? 41.618 32.241 72.019 1.00 57.18 ? 184  GLY A HA2    1 
ATOM   6    H HA3    . GLY A 1 1   ? 40.807 32.463 70.682 1.00 57.18 ? 184  GLY A HA3    1 
ATOM   7    N N      . ALA A 1 2   ? 40.525 29.934 71.532 1.00 41.35 ? 185  ALA A N      1 
ATOM   8    C CA     . ALA A 1 2   ? 40.331 28.498 71.405 1.00 37.21 ? 185  ALA A CA     1 
ATOM   9    C C      . ALA A 1 2   ? 39.865 28.156 69.994 1.00 32.34 ? 185  ALA A C      1 
ATOM   10   O O      . ALA A 1 2   ? 39.190 28.949 69.332 1.00 32.77 ? 185  ALA A O      1 
ATOM   11   C CB     . ALA A 1 2   ? 39.297 28.013 72.423 1.00 37.88 ? 185  ALA A CB     1 
ATOM   12   H H      . ALA A 1 2   ? 39.964 30.323 72.055 1.00 49.63 ? 185  ALA A H      1 
ATOM   13   H HA     . ALA A 1 2   ? 41.166 28.035 71.577 1.00 44.65 ? 185  ALA A HA     1 
ATOM   14   H HB1    . ALA A 1 2   ? 39.159 27.061 72.304 1.00 45.45 ? 185  ALA A HB1    1 
ATOM   15   H HB2    . ALA A 1 2   ? 39.627 28.191 73.318 1.00 45.45 ? 185  ALA A HB2    1 
ATOM   16   H HB3    . ALA A 1 2   ? 38.464 28.489 72.278 1.00 45.45 ? 185  ALA A HB3    1 
ATOM   17   N N      . LYS A 1 3   ? 40.229 26.960 69.538 1.00 29.24 ? 186  LYS A N      1 
ATOM   18   C CA     . LYS A 1 3   ? 39.885 26.533 68.193 1.00 26.17 ? 186  LYS A CA     1 
ATOM   19   C C      . LYS A 1 3   ? 38.369 26.479 68.039 1.00 22.98 ? 186  LYS A C      1 
ATOM   20   O O      . LYS A 1 3   ? 37.664 25.863 68.847 1.00 25.79 ? 186  LYS A O      1 
ATOM   21   C CB     . LYS A 1 3   ? 40.519 25.171 67.890 1.00 28.34 ? 186  LYS A CB     1 
ATOM   22   C CG     . LYS A 1 3   ? 40.290 24.610 66.495 1.00 31.01 ? 186  LYS A CG     1 
ATOM   23   C CD     . LYS A 1 3   ? 40.839 25.465 65.340 1.00 33.96 ? 186  LYS A CD     1 
ATOM   24   C CE     . LYS A 1 3   ? 42.362 25.549 65.296 1.00 36.37 ? 186  LYS A CE     1 
ATOM   25   N NZ     . LYS A 1 3   ? 43.040 24.210 65.152 1.00 36.46 ? 186  LYS A NZ     1 
ATOM   26   H H      . LYS A 1 3   ? 40.675 26.379 69.990 1.00 35.09 ? 186  LYS A H      1 
ATOM   27   H HA     . LYS A 1 3   ? 40.234 27.166 67.547 1.00 31.40 ? 186  LYS A HA     1 
ATOM   28   H HB2    . LYS A 1 3   ? 41.479 25.252 68.009 1.00 34.01 ? 186  LYS A HB2    1 
ATOM   29   H HB3    . LYS A 1 3   ? 40.160 24.525 68.519 1.00 34.01 ? 186  LYS A HB3    1 
ATOM   30   H HG2    . LYS A 1 3   ? 40.719 23.741 66.440 1.00 37.21 ? 186  LYS A HG2    1 
ATOM   31   H HG3    . LYS A 1 3   ? 39.334 24.517 66.356 1.00 37.21 ? 186  LYS A HG3    1 
ATOM   32   H HD2    . LYS A 1 3   ? 40.541 25.081 64.500 1.00 40.76 ? 186  LYS A HD2    1 
ATOM   33   H HD3    . LYS A 1 3   ? 40.497 26.368 65.432 1.00 40.76 ? 186  LYS A HD3    1 
ATOM   34   H HE2    . LYS A 1 3   ? 42.623 26.096 64.539 1.00 43.64 ? 186  LYS A HE2    1 
ATOM   35   H HE3    . LYS A 1 3   ? 42.676 25.952 66.120 1.00 43.64 ? 186  LYS A HE3    1 
ATOM   36   H HZ1    . LYS A 1 3   ? 43.923 24.309 65.207 1.00 43.75 ? 186  LYS A HZ1    1 
ATOM   37   H HZ2    . LYS A 1 3   ? 42.770 23.660 65.798 1.00 43.75 ? 186  LYS A HZ2    1 
ATOM   38   H HZ3    . LYS A 1 3   ? 42.839 23.850 64.363 1.00 43.75 ? 186  LYS A HZ3    1 
ATOM   39   N N      . VAL A 1 4   ? 37.878 27.151 67.004 1.00 18.39 ? 187  VAL A N      1 
ATOM   40   C CA     . VAL A 1 4   ? 36.464 27.140 66.646 1.00 16.77 ? 187  VAL A CA     1 
ATOM   41   C C      . VAL A 1 4   ? 36.197 26.066 65.616 1.00 17.41 ? 187  VAL A C      1 
ATOM   42   O O      . VAL A 1 4   ? 35.284 25.263 65.773 1.00 19.05 ? 187  VAL A O      1 
ATOM   43   C CB     . VAL A 1 4   ? 36.037 28.537 66.131 1.00 15.95 ? 187  VAL A CB     1 
ATOM   44   C CG1    . VAL A 1 4   ? 34.569 28.550 65.703 1.00 16.41 ? 187  VAL A CG1    1 
ATOM   45   C CG2    . VAL A 1 4   ? 36.281 29.595 67.218 1.00 18.19 ? 187  VAL A CG2    1 
ATOM   46   H H      . VAL A 1 4   ? 38.357 27.635 66.478 1.00 22.07 ? 187  VAL A H      1 
ATOM   47   H HA     . VAL A 1 4   ? 35.936 26.948 67.437 1.00 20.12 ? 187  VAL A HA     1 
ATOM   48   H HB     . VAL A 1 4   ? 36.573 28.753 65.352 1.00 19.14 ? 187  VAL A HB     1 
ATOM   49   H HG11   . VAL A 1 4   ? 34.338 29.439 65.391 1.00 19.69 ? 187  VAL A HG11   1 
ATOM   50   H HG12   . VAL A 1 4   ? 34.442 27.905 64.989 1.00 19.69 ? 187  VAL A HG12   1 
ATOM   51   H HG13   . VAL A 1 4   ? 34.016 28.313 66.464 1.00 19.69 ? 187  VAL A HG13   1 
ATOM   52   H HG21   . VAL A 1 4   ? 36.045 30.468 66.867 1.00 21.82 ? 187  VAL A HG21   1 
ATOM   53   H HG22   . VAL A 1 4   ? 35.730 29.388 67.989 1.00 21.82 ? 187  VAL A HG22   1 
ATOM   54   H HG23   . VAL A 1 4   ? 37.218 29.582 67.467 1.00 21.82 ? 187  VAL A HG23   1 
ATOM   55   N N      . GLY A 1 5   ? 36.986 26.037 64.554 1.00 14.96 ? 188  GLY A N      1 
ATOM   56   C CA     . GLY A 1 5   ? 36.836 24.965 63.588 1.00 13.87 ? 188  GLY A CA     1 
ATOM   57   C C      . GLY A 1 5   ? 37.600 25.225 62.297 1.00 12.60 ? 188  GLY A C      1 
ATOM   58   O O      . GLY A 1 5   ? 38.504 26.066 62.229 1.00 13.34 ? 188  GLY A O      1 
ATOM   59   H H      . GLY A 1 5   ? 37.601 26.612 64.375 1.00 17.95 ? 188  GLY A H      1 
ATOM   60   H HA2    . GLY A 1 5   ? 37.164 24.138 63.974 1.00 16.64 ? 188  GLY A HA2    1 
ATOM   61   H HA3    . GLY A 1 5   ? 35.896 24.861 63.370 1.00 16.64 ? 188  GLY A HA3    1 
ATOM   62   N N      . LYS A 1 6   ? 37.230 24.432 61.290 1.00 12.47 ? 189  LYS A N      1 
ATOM   63   C CA     . LYS A 1 6   ? 37.901 24.362 60.018 1.00 11.45 ? 189  LYS A CA     1 
ATOM   64   C C      . LYS A 1 6   ? 37.117 25.124 58.957 1.00 10.71 ? 189  LYS A C      1 
ATOM   65   O O      . LYS A 1 6   ? 35.933 24.841 58.749 1.00 11.60 ? 189  LYS A O      1 
ATOM   66   C CB     . LYS A 1 6   ? 37.995 22.898 59.582 1.00 12.11 ? 189  LYS A CB     1 
ATOM   67   C CG     . LYS A 1 6   ? 38.943 22.066 60.450 1.00 13.55 ? 189  LYS A CG     1 
ATOM   68   C CD     . LYS A 1 6   ? 38.732 20.564 60.211 1.00 16.60 ? 189  LYS A CD     1 
ATOM   69   C CE     . LYS A 1 6   ? 39.494 19.677 61.243 1.00 19.93 ? 189  LYS A CE     1 
ATOM   70   N NZ     . LYS A 1 6   ? 40.899 19.732 61.050 1.00 20.56 ? 189  LYS A NZ     1 
ATOM   71   H H      . LYS A 1 6   ? 36.556 23.900 61.334 1.00 14.97 ? 189  LYS A H      1 
ATOM   72   H HA     . LYS A 1 6   ? 38.781 24.762 60.097 1.00 13.74 ? 189  LYS A HA     1 
ATOM   73   H HB2    . LYS A 1 6   ? 37.113 22.497 59.637 1.00 14.53 ? 189  LYS A HB2    1 
ATOM   74   H HB3    . LYS A 1 6   ? 38.319 22.862 58.669 1.00 14.53 ? 189  LYS A HB3    1 
ATOM   75   H HG2    . LYS A 1 6   ? 39.862 22.286 60.228 1.00 16.26 ? 189  LYS A HG2    1 
ATOM   76   H HG3    . LYS A 1 6   ? 38.774 22.254 61.386 1.00 16.26 ? 189  LYS A HG3    1 
ATOM   77   H HD2    . LYS A 1 6   ? 37.786 20.362 60.283 1.00 19.93 ? 189  LYS A HD2    1 
ATOM   78   H HD3    . LYS A 1 6   ? 39.054 20.337 59.325 1.00 19.93 ? 189  LYS A HD3    1 
ATOM   79   H HE2    . LYS A 1 6   ? 39.298 19.990 62.140 1.00 23.91 ? 189  LYS A HE2    1 
ATOM   80   H HE3    . LYS A 1 6   ? 39.209 18.755 61.143 1.00 23.91 ? 189  LYS A HE3    1 
ATOM   81   H HZ1    . LYS A 1 6   ? 41.309 19.220 61.651 1.00 24.67 ? 189  LYS A HZ1    1 
ATOM   82   H HZ2    . LYS A 1 6   ? 41.106 19.442 60.234 1.00 24.67 ? 189  LYS A HZ2    1 
ATOM   83   H HZ3    . LYS A 1 6   ? 41.187 20.570 61.140 1.00 24.67 ? 189  LYS A HZ3    1 
ATOM   84   N N      . ILE A 1 7   ? 37.791 26.023 58.260 1.00 10.90 ? 190  ILE A N      1 
ATOM   85   C CA     . ILE A 1 7   ? 37.198 26.786 57.168 1.00 10.24 ? 190  ILE A CA     1 
ATOM   86   C C      . ILE A 1 7   ? 37.701 26.179 55.883 1.00 9.82  ? 190  ILE A C      1 
ATOM   87   O O      . ILE A 1 7   ? 38.893 26.225 55.572 1.00 12.14 ? 190  ILE A O      1 
ATOM   88   C CB     . ILE A 1 7   ? 37.599 28.271 57.209 1.00 12.27 ? 190  ILE A CB     1 
ATOM   89   C CG1    . ILE A 1 7   ? 37.207 28.923 58.526 1.00 11.91 ? 190  ILE A CG1    1 
ATOM   90   C CG2    . ILE A 1 7   ? 37.019 29.000 55.997 1.00 13.42 ? 190  ILE A CG2    1 
ATOM   91   C CD1    . ILE A 1 7   ? 37.774 30.344 58.718 1.00 12.96 ? 190  ILE A CD1    1 
ATOM   92   H H      . ILE A 1 7   ? 38.617 26.216 58.402 1.00 13.08 ? 190  ILE A H      1 
ATOM   93   H HA     . ILE A 1 7   ? 36.232 26.712 57.229 1.00 12.29 ? 190  ILE A HA     1 
ATOM   94   H HB     . ILE A 1 7   ? 38.566 28.332 57.160 1.00 14.73 ? 190  ILE A HB     1 
ATOM   95   H HG12   . ILE A 1 7   ? 36.240 28.983 58.567 1.00 14.29 ? 190  ILE A HG12   1 
ATOM   96   H HG13   . ILE A 1 7   ? 37.536 28.373 59.255 1.00 14.29 ? 190  ILE A HG13   1 
ATOM   97   H HG21   . ILE A 1 7   ? 37.270 29.936 56.041 1.00 16.10 ? 190  ILE A HG21   1 
ATOM   98   H HG22   . ILE A 1 7   ? 37.374 28.599 55.188 1.00 16.10 ? 190  ILE A HG22   1 
ATOM   99   H HG23   . ILE A 1 7   ? 36.053 28.916 56.011 1.00 16.10 ? 190  ILE A HG23   1 
ATOM   100  H HD11   . ILE A 1 7   ? 37.497 30.680 59.585 1.00 15.55 ? 190  ILE A HD11   1 
ATOM   101  H HD12   . ILE A 1 7   ? 38.742 30.307 58.672 1.00 15.55 ? 190  ILE A HD12   1 
ATOM   102  H HD13   . ILE A 1 7   ? 37.430 30.919 58.016 1.00 15.55 ? 190  ILE A HD13   1 
ATOM   103  N N      . GLY A 1 8   ? 36.804 25.581 55.122 1.00 11.53 ? 191  GLY A N      1 
ATOM   104  C CA     . GLY A 1 8   ? 37.140 25.092 53.818 1.00 12.30 ? 191  GLY A CA     1 
ATOM   105  C C      . GLY A 1 8   ? 36.887 26.164 52.782 1.00 11.05 ? 191  GLY A C      1 
ATOM   106  O O      . GLY A 1 8   ? 35.904 26.891 52.871 1.00 11.29 ? 191  GLY A O      1 
ATOM   107  H H      . GLY A 1 8   ? 35.985 25.448 55.349 1.00 13.83 ? 191  GLY A H      1 
ATOM   108  H HA2    . GLY A 1 8   ? 38.077 24.842 53.790 1.00 14.76 ? 191  GLY A HA2    1 
ATOM   109  H HA3    . GLY A 1 8   ? 36.600 24.315 53.606 1.00 14.76 ? 191  GLY A HA3    1 
ATOM   110  N N      . VAL A 1 9   ? 37.739 26.214 51.772 1.00 11.78 ? 192  VAL A N      1 
ATOM   111  C CA     . VAL A 1 9   ? 37.606 27.167 50.671 1.00 11.47 ? 192  VAL A CA     1 
ATOM   112  C C      . VAL A 1 9   ? 37.514 26.379 49.361 1.00 10.98 ? 192  VAL A C      1 
ATOM   113  O O      . VAL A 1 9   ? 38.526 26.001 48.767 1.00 12.98 ? 192  VAL A O      1 
ATOM   114  C CB     . VAL A 1 9   ? 38.710 28.224 50.662 1.00 14.76 ? 192  VAL A CB     1 
ATOM   115  C CG1    . VAL A 1 9   ? 38.317 29.263 49.645 1.00 18.16 ? 192  VAL A CG1    1 
ATOM   116  C CG2    . VAL A 1 9   ? 38.881 28.818 52.079 1.00 16.55 ? 192  VAL A CG2    1 
ATOM   117  H H      . VAL A 1 9   ? 38.420 25.695 51.696 1.00 14.14 ? 192  VAL A H      1 
ATOM   118  H HA     . VAL A 1 9   ? 36.761 27.634 50.767 1.00 13.76 ? 192  VAL A HA     1 
ATOM   119  H HB     . VAL A 1 9   ? 39.571 27.852 50.418 1.00 17.71 ? 192  VAL A HB     1 
ATOM   120  H HG11   . VAL A 1 9   ? 39.019 29.931 49.590 1.00 21.80 ? 192  VAL A HG11   1 
ATOM   121  H HG12   . VAL A 1 9   ? 38.200 28.834 48.784 1.00 21.80 ? 192  VAL A HG12   1 
ATOM   122  H HG13   . VAL A 1 9   ? 37.487 29.679 49.924 1.00 21.80 ? 192  VAL A HG13   1 
ATOM   123  H HG21   . VAL A 1 9   ? 39.584 29.486 52.058 1.00 19.86 ? 192  VAL A HG21   1 
ATOM   124  H HG22   . VAL A 1 9   ? 38.045 29.226 52.354 1.00 19.86 ? 192  VAL A HG22   1 
ATOM   125  H HG23   . VAL A 1 9   ? 39.120 28.106 52.693 1.00 19.86 ? 192  VAL A HG23   1 
ATOM   126  N N      . CYS A 1 10  ? 36.298 26.157 48.895 1.00 10.30 ? 193  CYS A N      1 
ATOM   127  C CA     . CYS A 1 10  ? 36.049 25.357 47.699 1.00 10.51 ? 193  CYS A CA     1 
ATOM   128  C C      . CYS A 1 10  ? 35.726 26.314 46.564 1.00 10.07 ? 193  CYS A C      1 
ATOM   129  O O      . CYS A 1 10  ? 34.580 26.712 46.350 1.00 10.22 ? 193  CYS A O      1 
ATOM   130  C CB     . CYS A 1 10  ? 34.928 24.359 47.934 1.00 11.18 ? 193  CYS A CB     1 
ATOM   131  S SG     . CYS A 1 10  ? 34.549 23.367 46.466 1.00 12.18 ? 193  CYS A SG     1 
ATOM   132  H H      . CYS A 1 10  ? 35.582 26.464 49.260 1.00 12.36 ? 193  CYS A H      1 
ATOM   133  H HA     . CYS A 1 10  ? 36.852 24.864 47.471 1.00 12.61 ? 193  CYS A HA     1 
ATOM   134  H HB2    . CYS A 1 10  ? 35.190 23.754 48.645 1.00 13.42 ? 193  CYS A HB2    1 
ATOM   135  H HB3    . CYS A 1 10  ? 34.125 24.841 48.186 1.00 13.42 ? 193  CYS A HB3    1 
ATOM   136  H HG     . CYS A 1 10  ? 33.635 22.631 46.717 1.00 14.62 ? 193  CYS A HG     1 
ATOM   137  N N      . ALA A 1 11  ? 36.774 26.736 45.885 1.00 10.12 ? 194  ALA A N      1 
ATOM   138  C CA     . ALA A 1 11  ? 36.708 27.667 44.759 1.00 10.40 ? 194  ALA A CA     1 
ATOM   139  C C      . ALA A 1 11  ? 37.961 27.455 43.928 1.00 9.72  ? 194  ALA A C      1 
ATOM   140  O O      . ALA A 1 11  ? 38.930 26.838 44.398 1.00 10.93 ? 194  ALA A O      1 
ATOM   141  C CB     . ALA A 1 11  ? 36.619 29.129 45.210 1.00 10.97 ? 194  ALA A CB     1 
ATOM   142  H H      . ALA A 1 11  ? 37.580 26.491 46.060 1.00 12.15 ? 194  ALA A H      1 
ATOM   143  H HA     . ALA A 1 11  ? 35.919 27.477 44.228 1.00 12.48 ? 194  ALA A HA     1 
ATOM   144  H HB1    . ALA A 1 11  ? 36.474 29.691 44.433 1.00 13.16 ? 194  ALA A HB1    1 
ATOM   145  H HB2    . ALA A 1 11  ? 35.878 29.223 45.829 1.00 13.16 ? 194  ALA A HB2    1 
ATOM   146  H HB3    . ALA A 1 11  ? 37.449 29.376 45.646 1.00 13.16 ? 194  ALA A HB3    1 
ATOM   147  N N      . MET A 1 12  ? 37.956 27.922 42.683 1.00 10.39 ? 195  MET A N      1 
ATOM   148  C CA     . MET A 1 12  ? 39.137 27.770 41.847 1.00 11.47 ? 195  MET A CA     1 
ATOM   149  C C      . MET A 1 12  ? 40.332 28.498 42.460 1.00 11.47 ? 195  MET A C      1 
ATOM   150  O O      . MET A 1 12  ? 40.197 29.571 43.067 1.00 12.22 ? 195  MET A O      1 
ATOM   151  C CB     . MET A 1 12  ? 38.898 28.266 40.422 1.00 13.10 ? 195  MET A CB     1 
ATOM   152  C CG     . MET A 1 12  ? 37.723 27.576 39.753 1.00 13.82 ? 195  MET A CG     1 
ATOM   153  S SD     . MET A 1 12  ? 37.835 25.772 39.678 1.00 15.92 ? 195  MET A SD     1 
ATOM   154  C CE     . MET A 1 12  ? 39.164 25.534 38.502 1.00 18.75 ? 195  MET A CE     1 
ATOM   155  H H      . MET A 1 12  ? 37.295 28.323 42.308 1.00 12.47 ? 195  MET A H      1 
ATOM   156  H HA     . MET A 1 12  ? 39.334 26.822 41.784 1.00 13.76 ? 195  MET A HA     1 
ATOM   157  H HB2    . MET A 1 12  ? 38.714 29.218 40.446 1.00 15.72 ? 195  MET A HB2    1 
ATOM   158  H HB3    . MET A 1 12  ? 39.691 28.094 39.891 1.00 15.72 ? 195  MET A HB3    1 
ATOM   159  H HG2    . MET A 1 12  ? 36.916 27.796 40.245 1.00 16.59 ? 195  MET A HG2    1 
ATOM   160  H HG3    . MET A 1 12  ? 37.655 27.900 38.841 1.00 16.59 ? 195  MET A HG3    1 
ATOM   161  H HE1    . MET A 1 12  ? 39.329 24.583 38.400 1.00 22.51 ? 195  MET A HE1    1 
ATOM   162  H HE2    . MET A 1 12  ? 38.905 25.918 37.650 1.00 22.51 ? 195  MET A HE2    1 
ATOM   163  H HE3    . MET A 1 12  ? 39.962 25.974 38.834 1.00 22.51 ? 195  MET A HE3    1 
ATOM   164  N N      . ASP A 1 13  ? 41.525 27.920 42.235 1.00 12.00 ? 196  ASP A N      1 
ATOM   165  C CA     . ASP A 1 13  ? 42.745 28.471 42.800 1.00 13.04 ? 196  ASP A CA     1 
ATOM   166  C C      . ASP A 1 13  ? 42.936 29.928 42.411 1.00 13.66 ? 196  ASP A C      1 
ATOM   167  O O      . ASP A 1 13  ? 43.480 30.715 43.198 1.00 14.75 ? 196  ASP A O      1 
ATOM   168  C CB     . ASP A 1 13  ? 43.938 27.629 42.361 1.00 15.27 ? 196  ASP A CB     1 
ATOM   169  C CG     . ASP A 1 13  ? 43.985 26.233 43.032 1.00 16.75 ? 196  ASP A CG     1 
ATOM   170  O OD1    . ASP A 1 13  ? 43.514 26.096 44.184 1.00 18.52 ? 196  ASP A OD1    1 
ATOM   171  O OD2    . ASP A 1 13  ? 44.615 25.306 42.443 1.00 17.61 ? 196  ASP A OD2    1 
ATOM   172  H H      . ASP A 1 13  ? 41.644 27.212 41.760 1.00 14.40 ? 196  ASP A H      1 
ATOM   173  H HA     . ASP A 1 13  ? 42.693 28.434 43.768 1.00 15.65 ? 196  ASP A HA     1 
ATOM   174  H HB2    . ASP A 1 13  ? 43.893 27.496 41.402 1.00 18.33 ? 196  ASP A HB2    1 
ATOM   175  H HB3    . ASP A 1 13  ? 44.755 28.098 42.593 1.00 18.33 ? 196  ASP A HB3    1 
ATOM   176  N N      . ALA A 1 14  ? 42.532 30.326 41.194 1.00 13.97 ? 197  ALA A N      1 
ATOM   177  C CA     . ALA A 1 14  ? 42.693 31.729 40.800 1.00 16.43 ? 197  ALA A CA     1 
ATOM   178  C C      . ALA A 1 14  ? 42.035 32.662 41.799 1.00 15.46 ? 197  ALA A C      1 
ATOM   179  O O      . ALA A 1 14  ? 42.505 33.781 42.012 1.00 18.08 ? 197  ALA A O      1 
ATOM   180  C CB     . ALA A 1 14  ? 42.080 31.957 39.417 1.00 18.44 ? 197  ALA A CB     1 
ATOM   181  H H      . ALA A 1 14  ? 42.173 29.819 40.599 1.00 16.76 ? 197  ALA A H      1 
ATOM   182  H HA     . ALA A 1 14  ? 43.642 31.930 40.761 1.00 19.72 ? 197  ALA A HA     1 
ATOM   183  H HB1    . ALA A 1 14  ? 42.189 32.890 39.174 1.00 22.13 ? 197  ALA A HB1    1 
ATOM   184  H HB2    . ALA A 1 14  ? 42.535 31.392 38.773 1.00 22.13 ? 197  ALA A HB2    1 
ATOM   185  H HB3    . ALA A 1 14  ? 41.138 31.731 39.449 1.00 22.13 ? 197  ALA A HB3    1 
ATOM   186  N N      . LYS A 1 15  ? 40.906 32.265 42.367 1.00 13.18 ? 198  LYS A N      1 
ATOM   187  C CA     . LYS A 1 15  ? 40.203 33.056 43.370 1.00 12.54 ? 198  LYS A CA     1 
ATOM   188  C C      . LYS A 1 15  ? 40.686 32.794 44.779 1.00 13.51 ? 198  LYS A C      1 
ATOM   189  O O      . LYS A 1 15  ? 40.749 33.722 45.585 1.00 14.61 ? 198  LYS A O      1 
ATOM   190  C CB     . LYS A 1 15  ? 38.681 32.865 43.250 1.00 15.04 ? 198  LYS A CB     1 
ATOM   191  C CG     . LYS A 1 15  ? 38.149 33.118 41.845 1.00 19.30 ? 198  LYS A CG     1 
ATOM   192  C CD     . LYS A 1 15  ? 38.401 34.522 41.347 1.00 24.21 ? 198  LYS A CD     1 
ATOM   193  C CE     . LYS A 1 15  ? 37.730 34.756 39.990 1.00 29.33 ? 198  LYS A CE     1 
ATOM   194  N NZ     . LYS A 1 15  ? 38.061 36.082 39.439 1.00 33.38 ? 198  LYS A NZ     1 
ATOM   195  H H      . LYS A 1 15  ? 40.514 31.521 42.186 1.00 15.81 ? 198  LYS A H      1 
ATOM   196  H HA     . LYS A 1 15  ? 40.377 33.993 43.192 1.00 15.05 ? 198  LYS A HA     1 
ATOM   197  H HB2    . LYS A 1 15  ? 38.460 31.953 43.493 1.00 18.05 ? 198  LYS A HB2    1 
ATOM   198  H HB3    . LYS A 1 15  ? 38.240 33.485 43.851 1.00 18.05 ? 198  LYS A HB3    1 
ATOM   199  H HG2    . LYS A 1 15  ? 38.582 32.504 41.231 1.00 23.16 ? 198  LYS A HG2    1 
ATOM   200  H HG3    . LYS A 1 15  ? 37.190 32.970 41.841 1.00 23.16 ? 198  LYS A HG3    1 
ATOM   201  H HD2    . LYS A 1 15  ? 38.038 35.159 41.982 1.00 29.06 ? 198  LYS A HD2    1 
ATOM   202  H HD3    . LYS A 1 15  ? 39.355 34.662 41.245 1.00 29.06 ? 198  LYS A HD3    1 
ATOM   203  H HE2    . LYS A 1 15  ? 38.033 34.082 39.362 1.00 35.20 ? 198  LYS A HE2    1 
ATOM   204  H HE3    . LYS A 1 15  ? 36.767 34.703 40.095 1.00 35.20 ? 198  LYS A HE3    1 
ATOM   205  H HZ1    . LYS A 1 15  ? 37.657 36.195 38.654 1.00 40.06 ? 198  LYS A HZ1    1 
ATOM   206  H HZ2    . LYS A 1 15  ? 37.791 36.720 39.998 1.00 40.06 ? 198  LYS A HZ2    1 
ATOM   207  H HZ3    . LYS A 1 15  ? 38.941 36.153 39.324 1.00 40.06 ? 198  LYS A HZ3    1 
ATOM   208  N N      . VAL A 1 16  ? 41.049 31.556 45.109 1.00 12.76 ? 199  VAL A N      1 
ATOM   209  C CA     . VAL A 1 16  ? 41.537 31.275 46.448 1.00 12.64 ? 199  VAL A CA     1 
ATOM   210  C C      . VAL A 1 16  ? 42.842 32.001 46.726 1.00 11.69 ? 199  VAL A C      1 
ATOM   211  O O      . VAL A 1 16  ? 43.123 32.363 47.880 1.00 13.20 ? 199  VAL A O      1 
ATOM   212  C CB     . VAL A 1 16  ? 41.706 29.748 46.608 1.00 13.87 ? 199  VAL A CB     1 
ATOM   213  C CG1    . VAL A 1 16  ? 42.286 29.446 47.997 1.00 15.83 ? 199  VAL A CG1    1 
ATOM   214  C CG2    . VAL A 1 16  ? 40.381 29.054 46.437 1.00 15.52 ? 199  VAL A CG2    1 
ATOM   215  H H      . VAL A 1 16  ? 41.021 30.876 44.583 1.00 15.31 ? 199  VAL A H      1 
ATOM   216  H HA     . VAL A 1 16  ? 40.887 31.597 47.091 1.00 15.17 ? 199  VAL A HA     1 
ATOM   217  H HB     . VAL A 1 16  ? 42.312 29.413 45.929 1.00 16.65 ? 199  VAL A HB     1 
ATOM   218  H HG11   . VAL A 1 16  ? 42.354 28.485 48.109 1.00 18.99 ? 199  VAL A HG11   1 
ATOM   219  H HG12   . VAL A 1 16  ? 43.165 29.850 48.066 1.00 18.99 ? 199  VAL A HG12   1 
ATOM   220  H HG13   . VAL A 1 16  ? 41.698 29.817 48.673 1.00 18.99 ? 199  VAL A HG13   1 
ATOM   221  H HG21   . VAL A 1 16  ? 40.522 28.094 46.456 1.00 18.62 ? 199  VAL A HG21   1 
ATOM   222  H HG22   . VAL A 1 16  ? 39.791 29.315 47.162 1.00 18.62 ? 199  VAL A HG22   1 
ATOM   223  H HG23   . VAL A 1 16  ? 39.995 29.315 45.586 1.00 18.62 ? 199  VAL A HG23   1 
ATOM   224  N N      . LEU A 1 17  ? 43.644 32.217 45.694 1.00 11.19 ? 200  LEU A N      1 
ATOM   225  C CA     . LEU A 1 17  ? 44.927 32.884 45.824 1.00 12.58 ? 200  LEU A CA     1 
ATOM   226  C C      . LEU A 1 17  ? 44.841 34.398 45.677 1.00 13.41 ? 200  LEU A C      1 
ATOM   227  O O      . LEU A 1 17  ? 45.880 35.052 45.659 1.00 14.29 ? 200  LEU A O      1 
ATOM   228  C CB     . LEU A 1 17  ? 45.900 32.298 44.797 1.00 13.91 ? 200  LEU A CB     1 
ATOM   229  C CG     . LEU A 1 17  ? 46.210 30.804 44.993 1.00 17.14 ? 200  LEU A CG     1 
ATOM   230  C CD1    . LEU A 1 17  ? 47.054 30.300 43.790 1.00 20.45 ? 200  LEU A CD1    1 
ATOM   231  C CD2    . LEU A 1 17  ? 46.890 30.588 46.328 1.00 19.15 ? 200  LEU A CD2    1 
ATOM   232  H H      . LEU A 1 17  ? 43.461 31.980 44.888 1.00 13.43 ? 200  LEU A H      1 
ATOM   233  H HA     . LEU A 1 17  ? 45.281 32.717 46.711 1.00 15.09 ? 200  LEU A HA     1 
ATOM   234  H HB2    . LEU A 1 17  ? 45.517 32.405 43.913 1.00 16.69 ? 200  LEU A HB2    1 
ATOM   235  H HB3    . LEU A 1 17  ? 46.739 32.782 44.856 1.00 16.69 ? 200  LEU A HB3    1 
ATOM   236  H HG     . LEU A 1 17  ? 45.398 30.275 45.015 1.00 20.57 ? 200  LEU A HG     1 
ATOM   237  H HD11   . LEU A 1 17  ? 47.250 29.358 43.915 1.00 24.54 ? 200  LEU A HD11   1 
ATOM   238  H HD12   . LEU A 1 17  ? 46.546 30.426 42.973 1.00 24.54 ? 200  LEU A HD12   1 
ATOM   239  H HD13   . LEU A 1 17  ? 47.879 30.807 43.748 1.00 24.54 ? 200  LEU A HD13   1 
ATOM   240  H HD21   . LEU A 1 17  ? 47.113 29.648 46.420 1.00 22.98 ? 200  LEU A HD21   1 
ATOM   241  H HD22   . LEU A 1 17  ? 47.697 31.124 46.362 1.00 22.98 ? 200  LEU A HD22   1 
ATOM   242  H HD23   . LEU A 1 17  ? 46.285 30.855 47.037 1.00 22.98 ? 200  LEU A HD23   1 
ATOM   243  N N      . SER A 1 18  ? 43.657 34.974 45.570 1.00 13.07 ? 201  SER A N      1 
ATOM   244  C CA     . SER A 1 18  ? 43.550 36.420 45.466 1.00 12.83 ? 201  SER A CA     1 
ATOM   245  C C      . SER A 1 18  ? 44.093 37.080 46.727 1.00 13.17 ? 201  SER A C      1 
ATOM   246  O O      . SER A 1 18  ? 44.104 36.493 47.808 1.00 12.87 ? 201  SER A O      1 
ATOM   247  C CB     . SER A 1 18  ? 42.082 36.804 45.291 1.00 13.64 ? 201  SER A CB     1 
ATOM   248  O OG     . SER A 1 18  ? 41.363 36.718 46.512 1.00 14.44 ? 201  SER A OG     1 
ATOM   249  H H      . SER A 1 18  ? 42.906 34.556 45.555 1.00 15.68 ? 201  SER A H      1 
ATOM   250  H HA     . SER A 1 18  ? 44.060 36.738 44.705 1.00 15.40 ? 201  SER A HA     1 
ATOM   251  H HB2    . SER A 1 18  ? 42.035 37.716 44.965 1.00 16.37 ? 201  SER A HB2    1 
ATOM   252  H HB3    . SER A 1 18  ? 41.676 36.201 44.648 1.00 16.37 ? 201  SER A HB3    1 
ATOM   253  H HG     . SER A 1 18  ? 40.537 36.737 46.362 1.00 17.33 ? 201  SER A HG     1 
ATOM   254  N N      . LYS A 1 19  ? 44.530 38.342 46.580 1.00 13.94 ? 202  LYS A N      1 
ATOM   255  C CA     . LYS A 1 19  ? 45.018 39.084 47.746 1.00 13.22 ? 202  LYS A CA     1 
ATOM   256  C C      . LYS A 1 19  ? 43.966 39.150 48.837 1.00 12.21 ? 202  LYS A C      1 
ATOM   257  O O      . LYS A 1 19  ? 44.272 38.866 50.008 1.00 11.90 ? 202  LYS A O      1 
ATOM   258  C CB     . LYS A 1 19  ? 45.478 40.492 47.346 1.00 15.53 ? 202  LYS A CB     1 
ATOM   259  C CG     . LYS A 1 19  ? 46.764 40.456 46.610 1.00 20.75 ? 202  LYS A CG     1 
ATOM   260  C CD     . LYS A 1 19  ? 47.425 41.809 46.533 1.00 26.73 ? 202  LYS A CD     1 
ATOM   261  C CE     . LYS A 1 19  ? 46.867 42.496 45.402 1.00 30.49 ? 202  LYS A CE     1 
ATOM   262  N NZ     . LYS A 1 19  ? 47.602 43.765 45.226 1.00 32.71 ? 202  LYS A NZ     1 
ATOM   263  H H      . LYS A 1 19  ? 44.553 38.775 45.837 1.00 16.73 ? 202  LYS A H      1 
ATOM   264  H HA     . LYS A 1 19  ? 45.798 38.615 48.083 1.00 15.87 ? 202  LYS A HA     1 
ATOM   265  H HB2    . LYS A 1 19  ? 44.809 40.896 46.771 1.00 18.63 ? 202  LYS A HB2    1 
ATOM   266  H HB3    . LYS A 1 19  ? 45.598 41.029 48.145 1.00 18.63 ? 202  LYS A HB3    1 
ATOM   267  H HG2    . LYS A 1 19  ? 47.372 39.851 47.064 1.00 24.90 ? 202  LYS A HG2    1 
ATOM   268  H HG3    . LYS A 1 19  ? 46.603 40.148 45.705 1.00 24.90 ? 202  LYS A HG3    1 
ATOM   269  H HD2    . LYS A 1 19  ? 47.245 42.318 47.339 1.00 32.08 ? 202  LYS A HD2    1 
ATOM   270  H HD3    . LYS A 1 19  ? 48.382 41.710 46.409 1.00 32.08 ? 202  LYS A HD3    1 
ATOM   271  H HE2    . LYS A 1 19  ? 46.965 41.957 44.602 1.00 36.59 ? 202  LYS A HE2    1 
ATOM   272  H HE3    . LYS A 1 19  ? 45.929 42.690 45.558 1.00 36.59 ? 202  LYS A HE3    1 
ATOM   273  H HZ1    . LYS A 1 19  ? 47.317 44.183 44.494 1.00 39.26 ? 202  LYS A HZ1    1 
ATOM   274  H HZ2    . LYS A 1 19  ? 47.470 44.293 45.931 1.00 39.26 ? 202  LYS A HZ2    1 
ATOM   275  H HZ3    . LYS A 1 19  ? 48.473 43.603 45.146 1.00 39.26 ? 202  LYS A HZ3    1 
ATOM   276  N N      . PRO A 1 20  ? 42.710 39.516 48.552 1.00 11.74 ? 203  PRO A N      1 
ATOM   277  C CA     . PRO A 1 20  ? 41.758 39.585 49.657 1.00 11.11 ? 203  PRO A CA     1 
ATOM   278  C C      . PRO A 1 20  ? 41.551 38.248 50.333 1.00 10.92 ? 203  PRO A C      1 
ATOM   279  O O      . PRO A 1 20  ? 41.443 38.173 51.555 1.00 11.48 ? 203  PRO A O      1 
ATOM   280  C CB     . PRO A 1 20  ? 40.472 40.123 49.002 1.00 14.06 ? 203  PRO A CB     1 
ATOM   281  C CG     . PRO A 1 20  ? 40.883 40.609 47.722 1.00 17.64 ? 203  PRO A CG     1 
ATOM   282  C CD     . PRO A 1 20  ? 42.194 40.097 47.309 1.00 13.83 ? 203  PRO A CD     1 
ATOM   283  H HA     . PRO A 1 20  ? 42.058 40.235 50.313 1.00 13.34 ? 203  PRO A HA     1 
ATOM   284  H HB2    . PRO A 1 20  ? 39.825 39.406 48.910 1.00 16.88 ? 203  PRO A HB2    1 
ATOM   285  H HB3    . PRO A 1 20  ? 40.101 40.838 49.542 1.00 16.88 ? 203  PRO A HB3    1 
ATOM   286  H HG2    . PRO A 1 20  ? 40.217 40.335 47.072 1.00 21.17 ? 203  PRO A HG2    1 
ATOM   287  H HG3    . PRO A 1 20  ? 40.921 41.577 47.770 1.00 21.17 ? 203  PRO A HG3    1 
ATOM   288  H HD2    . PRO A 1 20  ? 42.103 39.421 46.619 1.00 16.60 ? 203  PRO A HD2    1 
ATOM   289  H HD3    . PRO A 1 20  ? 42.766 40.816 46.996 1.00 16.60 ? 203  PRO A HD3    1 
ATOM   290  N N      . MET A 1 21  ? 41.421 37.171 49.558 1.00 10.31 ? 204  MET A N      1 
ATOM   291  C CA     . MET A 1 21  ? 41.214 35.880 50.199 1.00 10.58 ? 204  MET A CA     1 
ATOM   292  C C      . MET A 1 21  ? 42.376 35.503 51.093 1.00 9.69  ? 204  MET A C      1 
ATOM   293  O O      . MET A 1 21  ? 42.162 35.112 52.254 1.00 10.11 ? 204  MET A O      1 
ATOM   294  C CB     . MET A 1 21  ? 40.989 34.775 49.176 1.00 11.05 ? 204  MET A CB     1 
ATOM   295  C CG     . MET A 1 21  ? 40.642 33.417 49.803 1.00 11.38 ? 204  MET A CG     1 
ATOM   296  S SD     . MET A 1 21  ? 38.976 33.350 50.485 1.00 12.45 ? 204  MET A SD     1 
ATOM   297  C CE     . MET A 1 21  ? 38.015 33.159 48.984 1.00 13.05 ? 204  MET A CE     1 
ATOM   298  H H      . MET A 1 21  ? 41.447 37.164 48.698 1.00 12.37 ? 204  MET A H      1 
ATOM   299  H HA     . MET A 1 21  ? 40.406 35.962 50.729 1.00 12.70 ? 204  MET A HA     1 
ATOM   300  H HB2    . MET A 1 21  ? 40.255 35.031 48.596 1.00 13.26 ? 204  MET A HB2    1 
ATOM   301  H HB3    . MET A 1 21  ? 41.800 34.662 48.655 1.00 13.26 ? 204  MET A HB3    1 
ATOM   302  H HG2    . MET A 1 21  ? 40.712 32.730 49.121 1.00 13.66 ? 204  MET A HG2    1 
ATOM   303  H HG3    . MET A 1 21  ? 41.266 33.236 50.523 1.00 13.66 ? 204  MET A HG3    1 
ATOM   304  H HE1    . MET A 1 21  ? 37.072 33.184 49.207 1.00 15.66 ? 204  MET A HE1    1 
ATOM   305  H HE2    . MET A 1 21  ? 38.231 33.883 48.376 1.00 15.66 ? 204  MET A HE2    1 
ATOM   306  H HE3    . MET A 1 21  ? 38.235 32.307 48.575 1.00 15.66 ? 204  MET A HE3    1 
ATOM   307  N N      . ARG A 1 22  ? 43.599 35.728 50.632 1.00 10.40 ? 205  ARG A N      1 
ATOM   308  C CA     A ARG A 1 22  ? 44.744 35.376 51.460 0.70 10.50 ? 205  ARG A CA     1 
ATOM   309  C CA     B ARG A 1 22  ? 44.756 35.380 51.447 0.30 11.30 ? 205  ARG A CA     1 
ATOM   310  C C      . ARG A 1 22  ? 44.808 36.215 52.716 1.00 11.87 ? 205  ARG A C      1 
ATOM   311  O O      . ARG A 1 22  ? 45.097 35.697 53.798 1.00 12.88 ? 205  ARG A O      1 
ATOM   312  C CB     A ARG A 1 22  ? 46.019 35.504 50.651 0.70 12.56 ? 205  ARG A CB     1 
ATOM   313  C CB     B ARG A 1 22  ? 46.031 35.541 50.620 0.30 12.71 ? 205  ARG A CB     1 
ATOM   314  C CG     A ARG A 1 22  ? 46.115 34.373 49.636 0.70 14.69 ? 205  ARG A CG     1 
ATOM   315  C CG     B ARG A 1 22  ? 46.083 34.558 49.442 0.30 14.01 ? 205  ARG A CG     1 
ATOM   316  C CD     A ARG A 1 22  ? 47.411 34.296 48.925 0.70 15.96 ? 205  ARG A CD     1 
ATOM   317  C CD     B ARG A 1 22  ? 47.353 34.612 48.624 0.30 15.81 ? 205  ARG A CD     1 
ATOM   318  N NE     A ARG A 1 22  ? 47.662 35.521 48.176 0.70 16.67 ? 205  ARG A NE     1 
ATOM   319  N NE     B ARG A 1 22  ? 48.527 34.209 49.394 0.30 19.62 ? 205  ARG A NE     1 
ATOM   320  C CZ     A ARG A 1 22  ? 48.516 36.475 48.541 0.70 16.26 ? 205  ARG A CZ     1 
ATOM   321  C CZ     B ARG A 1 22  ? 48.862 32.957 49.691 0.30 22.03 ? 205  ARG A CZ     1 
ATOM   322  N NH1    A ARG A 1 22  ? 49.180 36.403 49.677 0.70 18.76 ? 205  ARG A NH1    1 
ATOM   323  N NH1    B ARG A 1 22  ? 48.107 31.924 49.334 0.30 22.70 ? 205  ARG A NH1    1 
ATOM   324  N NH2    A ARG A 1 22  ? 48.691 37.546 47.749 0.70 12.42 ? 205  ARG A NH2    1 
ATOM   325  N NH2    B ARG A 1 22  ? 49.980 32.733 50.375 0.30 24.24 ? 205  ARG A NH2    1 
ATOM   326  H H      A ARG A 1 22  ? 43.788 36.072 49.867 0.70 12.48 ? 205  ARG A H      1 
ATOM   327  H H      B ARG A 1 22  ? 43.784 36.073 49.866 0.30 12.48 ? 205  ARG A H      1 
ATOM   328  H HA     A ARG A 1 22  ? 44.656 34.451 51.739 0.70 12.60 ? 205  ARG A HA     1 
ATOM   329  H HA     B ARG A 1 22  ? 44.694 34.451 51.717 0.30 13.56 ? 205  ARG A HA     1 
ATOM   330  H HB2    A ARG A 1 22  ? 46.019 36.349 50.175 0.70 15.07 ? 205  ARG A HB2    1 
ATOM   331  H HB2    B ARG A 1 22  ? 46.068 36.443 50.265 0.30 15.25 ? 205  ARG A HB2    1 
ATOM   332  H HB3    A ARG A 1 22  ? 46.787 35.457 51.242 0.70 15.07 ? 205  ARG A HB3    1 
ATOM   333  H HB3    B ARG A 1 22  ? 46.801 35.376 51.187 0.30 15.25 ? 205  ARG A HB3    1 
ATOM   334  H HG2    A ARG A 1 22  ? 45.985 33.530 50.098 0.70 17.63 ? 205  ARG A HG2    1 
ATOM   335  H HG2    B ARG A 1 22  ? 45.999 33.656 49.788 0.30 16.81 ? 205  ARG A HG2    1 
ATOM   336  H HG3    A ARG A 1 22  ? 45.422 34.496 48.968 0.70 17.63 ? 205  ARG A HG3    1 
ATOM   337  H HG3    B ARG A 1 22  ? 45.344 34.754 48.844 0.30 16.81 ? 205  ARG A HG3    1 
ATOM   338  H HD2    A ARG A 1 22  ? 48.127 34.175 49.568 0.70 19.15 ? 205  ARG A HD2    1 
ATOM   339  H HD2    B ARG A 1 22  ? 47.269 34.013 47.866 0.30 18.98 ? 205  ARG A HD2    1 
ATOM   340  H HD3    A ARG A 1 22  ? 47.396 33.552 48.302 0.70 19.15 ? 205  ARG A HD3    1 
ATOM   341  H HD3    B ARG A 1 22  ? 47.493 35.521 48.314 0.30 18.98 ? 205  ARG A HD3    1 
ATOM   342  H HE     A ARG A 1 22  ? 47.226 35.637 47.444 0.70 20.01 ? 205  ARG A HE     1 
ATOM   343  H HE     B ARG A 1 22  ? 49.045 34.834 49.680 0.30 23.54 ? 205  ARG A HE     1 
ATOM   344  H HH11   A ARG A 1 22  ? 49.066 35.730 50.200 0.70 22.51 ? 205  ARG A HH11   1 
ATOM   345  H HH11   B ARG A 1 22  ? 47.377 32.055 48.898 0.30 27.24 ? 205  ARG A HH11   1 
ATOM   346  H HH12   A ARG A 1 22  ? 49.727 37.030 49.896 0.70 22.51 ? 205  ARG A HH12   1 
ATOM   347  H HH12   B ARG A 1 22  ? 48.347 31.124 49.539 0.30 27.24 ? 205  ARG A HH12   1 
ATOM   348  H HH21   A ARG A 1 22  ? 48.254 37.612 47.012 0.70 14.90 ? 205  ARG A HH21   1 
ATOM   349  H HH21   B ARG A 1 22  ? 50.474 33.393 50.619 0.30 29.08 ? 205  ARG A HH21   1 
ATOM   350  H HH22   A ARG A 1 22  ? 49.242 38.166 47.979 0.70 14.90 ? 205  ARG A HH22   1 
ATOM   351  H HH22   B ARG A 1 22  ? 50.209 31.928 50.574 0.30 29.08 ? 205  ARG A HH22   1 
ATOM   352  N N      . HIS A 1 23  ? 44.559 37.510 52.601 1.00 12.18 ? 206  HIS A N      1 
ATOM   353  C CA     A HIS A 1 23  ? 44.700 38.362 53.770 0.54 13.16 ? 206  HIS A CA     1 
ATOM   354  C CA     B HIS A 1 23  ? 44.666 38.427 53.738 0.46 12.86 ? 206  HIS A CA     1 
ATOM   355  C C      . HIS A 1 23  ? 43.564 38.181 54.767 1.00 11.61 ? 206  HIS A C      1 
ATOM   356  O O      . HIS A 1 23  ? 43.775 38.286 55.979 1.00 11.98 ? 206  HIS A O      1 
ATOM   357  C CB     A HIS A 1 23  ? 44.808 39.799 53.310 0.54 15.85 ? 206  HIS A CB     1 
ATOM   358  C CB     B HIS A 1 23  ? 44.627 39.886 53.232 0.46 15.32 ? 206  HIS A CB     1 
ATOM   359  C CG     A HIS A 1 23  ? 46.063 40.088 52.563 0.54 16.75 ? 206  HIS A CG     1 
ATOM   360  C CG     B HIS A 1 23  ? 45.954 40.381 52.751 0.46 16.65 ? 206  HIS A CG     1 
ATOM   361  N ND1    A HIS A 1 23  ? 47.311 39.769 53.053 0.54 19.76 ? 206  HIS A ND1    1 
ATOM   362  N ND1    B HIS A 1 23  ? 46.542 39.974 51.575 0.46 17.15 ? 206  HIS A ND1    1 
ATOM   363  C CD2    A HIS A 1 23  ? 46.266 40.690 51.371 0.54 16.37 ? 206  HIS A CD2    1 
ATOM   364  C CD2    B HIS A 1 23  ? 46.826 41.243 53.321 0.46 18.16 ? 206  HIS A CD2    1 
ATOM   365  C CE1    A HIS A 1 23  ? 48.231 40.168 52.192 0.54 20.09 ? 206  HIS A CE1    1 
ATOM   366  C CE1    B HIS A 1 23  ? 47.729 40.546 51.452 0.46 18.81 ? 206  HIS A CE1    1 
ATOM   367  N NE2    A HIS A 1 23  ? 47.630 40.783 51.190 0.54 20.16 ? 206  HIS A NE2    1 
ATOM   368  N NE2    B HIS A 1 23  ? 47.912 41.337 52.489 0.46 19.84 ? 206  HIS A NE2    1 
ATOM   369  H H      A HIS A 1 23  ? 44.314 37.909 51.879 0.54 14.61 ? 206  HIS A H      1 
ATOM   370  H H      B HIS A 1 23  ? 44.322 37.895 51.869 0.46 14.61 ? 206  HIS A H      1 
ATOM   371  H HA     A HIS A 1 23  ? 45.513 38.127 54.245 0.54 15.79 ? 206  HIS A HA     1 
ATOM   372  H HA     B HIS A 1 23  ? 45.516 38.279 54.182 0.46 15.43 ? 206  HIS A HA     1 
ATOM   373  H HB2    A HIS A 1 23  ? 44.060 39.997 52.724 0.54 19.03 ? 206  HIS A HB2    1 
ATOM   374  H HB2    B HIS A 1 23  ? 44.001 39.945 52.493 0.46 18.38 ? 206  HIS A HB2    1 
ATOM   375  H HB3    A HIS A 1 23  ? 44.783 40.379 54.087 0.54 19.03 ? 206  HIS A HB3    1 
ATOM   376  H HB3    B HIS A 1 23  ? 44.340 40.462 53.957 0.46 18.38 ? 206  HIS A HB3    1 
ATOM   377  H HD1    B HIS A 1 23  ? 46.192 39.431 51.007 0.46 20.58 ? 206  HIS A HD1    1 
ATOM   378  H HD2    A HIS A 1 23  ? 45.610 40.987 50.783 0.54 19.64 ? 206  HIS A HD2    1 
ATOM   379  H HD2    B HIS A 1 23  ? 46.710 41.691 54.128 0.46 21.79 ? 206  HIS A HD2    1 
ATOM   380  H HE1    A HIS A 1 23  ? 49.148 40.038 52.277 0.54 24.11 ? 206  HIS A HE1    1 
ATOM   381  H HE1    B HIS A 1 23  ? 48.329 40.414 50.754 0.46 22.58 ? 206  HIS A HE1    1 
ATOM   382  H HE2    A HIS A 1 23  ? 48.023 41.175 50.534 0.54 24.20 ? 206  HIS A HE2    1 
ATOM   383  N N      . ILE A 1 24  ? 42.372 37.851 54.296 1.00 10.50 ? 207  ILE A N      1 
ATOM   384  C CA     . ILE A 1 24  ? 41.263 37.585 55.190 1.00 10.54 ? 207  ILE A CA     1 
ATOM   385  C C      . ILE A 1 24  ? 41.437 36.240 55.884 1.00 11.31 ? 207  ILE A C      1 
ATOM   386  O O      . ILE A 1 24  ? 41.248 36.131 57.098 1.00 11.63 ? 207  ILE A O      1 
ATOM   387  C CB     . ILE A 1 24  ? 39.945 37.698 54.402 1.00 10.71 ? 207  ILE A CB     1 
ATOM   388  C CG1    . ILE A 1 24  ? 39.706 39.189 54.032 1.00 11.06 ? 207  ILE A CG1    1 
ATOM   389  C CG2    . ILE A 1 24  ? 38.769 37.195 55.227 1.00 10.90 ? 207  ILE A CG2    1 
ATOM   390  C CD1    . ILE A 1 24  ? 38.625 39.401 52.977 1.00 12.17 ? 207  ILE A CD1    1 
ATOM   391  H H      . ILE A 1 24  ? 42.179 37.775 53.461 1.00 12.60 ? 207  ILE A H      1 
ATOM   392  H HA     . ILE A 1 24  ? 41.244 38.248 55.897 1.00 12.65 ? 207  ILE A HA     1 
ATOM   393  H HB     . ILE A 1 24  ? 40.018 37.154 53.602 1.00 12.86 ? 207  ILE A HB     1 
ATOM   394  H HG12   . ILE A 1 24  ? 39.436 39.668 54.831 1.00 13.27 ? 207  ILE A HG12   1 
ATOM   395  H HG13   . ILE A 1 24  ? 40.532 39.560 53.686 1.00 13.27 ? 207  ILE A HG13   1 
ATOM   396  H HG21   . ILE A 1 24  ? 37.953 37.307 54.714 1.00 13.07 ? 207  ILE A HG21   1 
ATOM   397  H HG22   . ILE A 1 24  ? 38.905 36.256 55.430 1.00 13.07 ? 207  ILE A HG22   1 
ATOM   398  H HG23   . ILE A 1 24  ? 38.717 37.707 56.048 1.00 13.07 ? 207  ILE A HG23   1 
ATOM   399  H HD11   . ILE A 1 24  ? 38.542 40.350 52.795 1.00 14.60 ? 207  ILE A HD11   1 
ATOM   400  H HD12   . ILE A 1 24  ? 38.877 38.930 52.167 1.00 14.60 ? 207  ILE A HD12   1 
ATOM   401  H HD13   . ILE A 1 24  ? 37.783 39.054 53.312 1.00 14.60 ? 207  ILE A HD13   1 
ATOM   402  N N      . LEU A 1 25  ? 41.797 35.199 55.128 1.00 11.81 ? 208  LEU A N      1 
ATOM   403  C CA     . LEU A 1 25  ? 42.065 33.902 55.761 1.00 11.51 ? 208  LEU A CA     1 
ATOM   404  C C      . LEU A 1 25  ? 43.214 34.012 56.768 1.00 12.12 ? 208  LEU A C      1 
ATOM   405  O O      . LEU A 1 25  ? 43.173 33.411 57.847 1.00 13.45 ? 208  LEU A O      1 
ATOM   406  C CB     . LEU A 1 25  ? 42.391 32.863 54.687 1.00 12.50 ? 208  LEU A CB     1 
ATOM   407  C CG     . LEU A 1 25  ? 41.219 32.421 53.818 1.00 14.44 ? 208  LEU A CG     1 
ATOM   408  C CD1    . LEU A 1 25  ? 41.701 31.442 52.780 1.00 16.32 ? 208  LEU A CD1    1 
ATOM   409  C CD2    . LEU A 1 25  ? 40.030 31.870 54.660 1.00 16.38 ? 208  LEU A CD2    1 
ATOM   410  H H      . LEU A 1 25  ? 41.891 35.215 54.273 1.00 14.17 ? 208  LEU A H      1 
ATOM   411  H HA     . LEU A 1 25  ? 41.272 33.609 56.237 1.00 13.81 ? 208  LEU A HA     1 
ATOM   412  H HB2    . LEU A 1 25  ? 43.064 33.237 54.097 1.00 15.00 ? 208  LEU A HB2    1 
ATOM   413  H HB3    . LEU A 1 25  ? 42.739 32.071 55.127 1.00 15.00 ? 208  LEU A HB3    1 
ATOM   414  H HG     . LEU A 1 25  ? 40.858 33.193 53.354 1.00 17.33 ? 208  LEU A HG     1 
ATOM   415  H HD11   . LEU A 1 25  ? 40.950 31.169 52.231 1.00 19.59 ? 208  LEU A HD11   1 
ATOM   416  H HD12   . LEU A 1 25  ? 42.375 31.870 52.230 1.00 19.59 ? 208  LEU A HD12   1 
ATOM   417  H HD13   . LEU A 1 25  ? 42.081 30.669 53.228 1.00 19.59 ? 208  LEU A HD13   1 
ATOM   418  H HD21   . LEU A 1 25  ? 39.352 31.522 54.059 1.00 19.65 ? 208  LEU A HD21   1 
ATOM   419  H HD22   . LEU A 1 25  ? 40.354 31.162 55.238 1.00 19.65 ? 208  LEU A HD22   1 
ATOM   420  H HD23   . LEU A 1 25  ? 39.660 32.591 55.194 1.00 19.65 ? 208  LEU A HD23   1 
ATOM   421  N N      . ASN A 1 26  ? 44.243 34.806 56.458 1.00 12.68 ? 209  ASN A N      1 
ATOM   422  C CA     A ASN A 1 26  ? 45.338 34.926 57.406 0.59 13.69 ? 209  ASN A CA     1 
ATOM   423  C CA     B ASN A 1 26  ? 45.357 34.963 57.393 0.41 13.66 ? 209  ASN A CA     1 
ATOM   424  C C      . ASN A 1 26  ? 44.850 35.488 58.727 1.00 13.05 ? 209  ASN A C      1 
ATOM   425  O O      . ASN A 1 26  ? 45.288 35.041 59.802 1.00 14.63 ? 209  ASN A O      1 
ATOM   426  C CB     A ASN A 1 26  ? 46.470 35.780 56.866 0.59 16.62 ? 209  ASN A CB     1 
ATOM   427  C CB     B ASN A 1 26  ? 46.430 35.910 56.828 0.41 16.14 ? 209  ASN A CB     1 
ATOM   428  C CG     A ASN A 1 26  ? 47.672 35.696 57.742 0.59 18.88 ? 209  ASN A CG     1 
ATOM   429  C CG     B ASN A 1 26  ? 47.341 35.246 55.800 0.41 18.63 ? 209  ASN A CG     1 
ATOM   430  O OD1    A ASN A 1 26  ? 48.113 36.689 58.320 0.59 20.58 ? 209  ASN A OD1    1 
ATOM   431  O OD1    B ASN A 1 26  ? 47.386 34.023 55.676 0.41 17.80 ? 209  ASN A OD1    1 
ATOM   432  N ND2    A ASN A 1 26  ? 48.169 34.479 57.913 0.59 18.46 ? 209  ASN A ND2    1 
ATOM   433  N ND2    B ASN A 1 26  ? 48.078 36.060 55.061 0.41 22.36 ? 209  ASN A ND2    1 
ATOM   434  H H      A ASN A 1 26  ? 44.323 35.265 55.735 0.59 15.22 ? 209  ASN A H      1 
ATOM   435  H H      B ASN A 1 26  ? 44.318 35.255 55.729 0.41 15.22 ? 209  ASN A H      1 
ATOM   436  H HA     A ASN A 1 26  ? 45.698 34.037 57.547 0.59 16.43 ? 209  ASN A HA     1 
ATOM   437  H HA     B ASN A 1 26  ? 45.777 34.098 57.522 0.41 16.39 ? 209  ASN A HA     1 
ATOM   438  H HB2    A ASN A 1 26  ? 46.713 35.469 55.980 0.59 19.95 ? 209  ASN A HB2    1 
ATOM   439  H HB2    B ASN A 1 26  ? 45.992 36.660 56.397 0.41 19.37 ? 209  ASN A HB2    1 
ATOM   440  H HB3    A ASN A 1 26  ? 46.184 36.706 56.826 0.59 19.95 ? 209  ASN A HB3    1 
ATOM   441  H HB3    B ASN A 1 26  ? 46.986 36.226 57.558 0.41 19.37 ? 209  ASN A HB3    1 
ATOM   442  H HD21   A ASN A 1 26  ? 48.863 34.363 58.407 0.59 22.16 ? 209  ASN A HD21   1 
ATOM   443  H HD21   B ASN A 1 26  ? 48.609 35.738 54.466 0.41 26.84 ? 209  ASN A HD21   1 
ATOM   444  H HD22   A ASN A 1 26  ? 47.797 33.805 57.529 0.59 22.16 ? 209  ASN A HD22   1 
ATOM   445  H HD22   B ASN A 1 26  ? 48.026 36.911 55.176 0.41 26.84 ? 209  ASN A HD22   1 
ATOM   446  N N      . ARG A 1 27  ? 43.973 36.503 58.681 1.00 12.81 ? 210  ARG A N      1 
ATOM   447  C CA     . ARG A 1 27  ? 43.408 37.053 59.899 1.00 13.96 ? 210  ARG A CA     1 
ATOM   448  C C      . ARG A 1 27  ? 42.628 36.007 60.669 1.00 15.11 ? 210  ARG A C      1 
ATOM   449  O O      . ARG A 1 27  ? 42.628 36.008 61.904 1.00 16.07 ? 210  ARG A O      1 
ATOM   450  C CB     . ARG A 1 27  ? 42.532 38.252 59.546 1.00 14.10 ? 210  ARG A CB     1 
ATOM   451  C CG     . ARG A 1 27  ? 43.326 39.476 59.150 1.00 14.05 ? 210  ARG A CG     1 
ATOM   452  C CD     . ARG A 1 27  ? 42.397 40.428 58.410 1.00 13.85 ? 210  ARG A CD     1 
ATOM   453  N NE     . ARG A 1 27  ? 42.949 41.779 58.281 1.00 14.51 ? 210  ARG A NE     1 
ATOM   454  C CZ     . ARG A 1 27  ? 43.958 42.096 57.490 1.00 14.82 ? 210  ARG A CZ     1 
ATOM   455  N NH1    . ARG A 1 27  ? 44.555 41.193 56.734 1.00 14.82 ? 210  ARG A NH1    1 
ATOM   456  N NH2    . ARG A 1 27  ? 44.398 43.357 57.470 1.00 17.31 ? 210  ARG A NH2    1 
ATOM   457  H H      . ARG A 1 27  ? 43.698 36.882 57.959 1.00 15.37 ? 210  ARG A H      1 
ATOM   458  H HA     . ARG A 1 27  ? 44.119 37.363 60.482 1.00 16.75 ? 210  ARG A HA     1 
ATOM   459  H HB2    . ARG A 1 27  ? 41.960 38.013 58.800 1.00 16.92 ? 210  ARG A HB2    1 
ATOM   460  H HB3    . ARG A 1 27  ? 41.991 38.483 60.317 1.00 16.92 ? 210  ARG A HB3    1 
ATOM   461  H HG2    . ARG A 1 27  ? 43.671 39.919 59.941 1.00 16.86 ? 210  ARG A HG2    1 
ATOM   462  H HG3    . ARG A 1 27  ? 44.057 39.225 58.565 1.00 16.86 ? 210  ARG A HG3    1 
ATOM   463  H HD2    . ARG A 1 27  ? 42.239 40.083 57.517 1.00 16.62 ? 210  ARG A HD2    1 
ATOM   464  H HD3    . ARG A 1 27  ? 41.559 40.493 58.894 1.00 16.62 ? 210  ARG A HD3    1 
ATOM   465  H HE     . ARG A 1 27  ? 42.593 42.406 58.750 1.00 17.42 ? 210  ARG A HE     1 
ATOM   466  H HH11   . ARG A 1 27  ? 44.289 40.375 56.749 1.00 17.78 ? 210  ARG A HH11   1 
ATOM   467  H HH12   . ARG A 1 27  ? 45.210 41.423 56.227 1.00 17.78 ? 210  ARG A HH12   1 
ATOM   468  H HH21   . ARG A 1 27  ? 44.025 43.950 57.968 1.00 20.77 ? 210  ARG A HH21   1 
ATOM   469  H HH22   . ARG A 1 27  ? 45.054 43.575 56.959 1.00 20.77 ? 210  ARG A HH22   1 
ATOM   470  N N      . LEU A 1 28  ? 41.964 35.101 59.964 1.00 13.55 ? 211  LEU A N      1 
ATOM   471  C CA     . LEU A 1 28  ? 41.161 34.090 60.649 1.00 13.97 ? 211  LEU A CA     1 
ATOM   472  C C      . LEU A 1 28  ? 42.004 32.970 61.269 1.00 14.26 ? 211  LEU A C      1 
ATOM   473  O O      . LEU A 1 28  ? 41.589 32.393 62.278 1.00 14.81 ? 211  LEU A O      1 
ATOM   474  C CB     . LEU A 1 28  ? 40.135 33.502 59.674 1.00 13.00 ? 211  LEU A CB     1 
ATOM   475  C CG     . LEU A 1 28  ? 38.964 34.466 59.396 1.00 13.97 ? 211  LEU A CG     1 
ATOM   476  C CD1    . LEU A 1 28  ? 38.287 34.083 58.062 1.00 14.02 ? 211  LEU A CD1    1 
ATOM   477  C CD2    . LEU A 1 28  ? 37.966 34.491 60.486 1.00 16.46 ? 211  LEU A CD2    1 
ATOM   478  H H      . LEU A 1 28  ? 41.959 35.048 59.106 1.00 16.26 ? 211  LEU A H      1 
ATOM   479  H HA     . LEU A 1 28  ? 40.685 34.519 61.377 1.00 16.76 ? 211  LEU A HA     1 
ATOM   480  H HB2    . LEU A 1 28  ? 40.575 33.310 58.831 1.00 15.60 ? 211  LEU A HB2    1 
ATOM   481  H HB3    . LEU A 1 28  ? 39.771 32.686 60.052 1.00 15.60 ? 211  LEU A HB3    1 
ATOM   482  H HG     . LEU A 1 28  ? 39.326 35.364 59.339 1.00 16.76 ? 211  LEU A HG     1 
ATOM   483  H HD11   . LEU A 1 28  ? 37.533 34.675 57.910 1.00 16.82 ? 211  LEU A HD11   1 
ATOM   484  H HD12   . LEU A 1 28  ? 38.931 34.177 57.343 1.00 16.82 ? 211  LEU A HD12   1 
ATOM   485  H HD13   . LEU A 1 28  ? 37.981 33.164 58.115 1.00 16.82 ? 211  LEU A HD13   1 
ATOM   486  H HD21   . LEU A 1 28  ? 37.252 35.103 60.246 1.00 19.75 ? 211  LEU A HD21   1 
ATOM   487  H HD22   . LEU A 1 28  ? 37.609 33.598 60.608 1.00 19.75 ? 211  LEU A HD22   1 
ATOM   488  H HD23   . LEU A 1 28  ? 38.396 34.790 61.302 1.00 19.75 ? 211  LEU A HD23   1 
ATOM   489  N N      . ILE A 1 29  ? 43.193 32.700 60.745 1.00 14.34 ? 212  ILE A N      1 
ATOM   490  C CA     . ILE A 1 29  ? 44.019 31.630 61.284 1.00 16.43 ? 212  ILE A CA     1 
ATOM   491  C C      . ILE A 1 29  ? 45.064 32.123 62.268 1.00 18.42 ? 212  ILE A C      1 
ATOM   492  O O      . ILE A 1 29  ? 45.557 31.330 63.072 1.00 19.77 ? 212  ILE A O      1 
ATOM   493  C CB     . ILE A 1 29  ? 44.671 30.768 60.186 1.00 19.42 ? 212  ILE A CB     1 
ATOM   494  C CG1    . ILE A 1 29  ? 45.750 31.498 59.411 1.00 21.46 ? 212  ILE A CG1    1 
ATOM   495  C CG2    . ILE A 1 29  ? 43.615 30.215 59.254 1.00 19.44 ? 212  ILE A CG2    1 
ATOM   496  C CD1    . ILE A 1 29  ? 46.487 30.596 58.482 1.00 24.13 ? 212  ILE A CD1    1 
ATOM   497  H H      . ILE A 1 29  ? 43.542 33.120 60.080 1.00 17.21 ? 212  ILE A H      1 
ATOM   498  H HA     . ILE A 1 29  ? 43.426 31.037 61.771 1.00 19.72 ? 212  ILE A HA     1 
ATOM   499  H HB     . ILE A 1 29  ? 45.116 30.035 60.639 1.00 23.31 ? 212  ILE A HB     1 
ATOM   500  H HG12   . ILE A 1 29  ? 45.342 32.204 58.886 1.00 25.75 ? 212  ILE A HG12   1 
ATOM   501  H HG13   . ILE A 1 29  ? 46.389 31.876 60.036 1.00 25.75 ? 212  ILE A HG13   1 
ATOM   502  H HG21   . ILE A 1 29  ? 44.045 29.665 58.581 1.00 23.33 ? 212  ILE A HG21   1 
ATOM   503  H HG22   . ILE A 1 29  ? 42.989 29.681 59.768 1.00 23.33 ? 212  ILE A HG22   1 
ATOM   504  H HG23   . ILE A 1 29  ? 43.151 30.953 58.830 1.00 23.33 ? 212  ILE A HG23   1 
ATOM   505  H HD11   . ILE A 1 29  ? 47.215 31.089 58.074 1.00 28.95 ? 212  ILE A HD11   1 
ATOM   506  H HD12   . ILE A 1 29  ? 46.838 29.844 58.985 1.00 28.95 ? 212  ILE A HD12   1 
ATOM   507  H HD13   . ILE A 1 29  ? 45.876 30.280 57.798 1.00 28.95 ? 212  ILE A HD13   1 
ATOM   508  N N      . GLU A 1 30  ? 45.361 33.417 62.287 1.00 19.89 ? 213  GLU A N      1 
ATOM   509  C CA     . GLU A 1 30  ? 46.594 33.841 62.947 1.00 22.81 ? 213  GLU A CA     1 
ATOM   510  C C      . GLU A 1 30  ? 46.508 33.811 64.461 1.00 23.18 ? 213  GLU A C      1 
ATOM   511  O O      . GLU A 1 30  ? 47.561 33.843 65.105 1.00 25.00 ? 213  GLU A O      1 
ATOM   512  C CB     . GLU A 1 30  ? 47.044 35.197 62.442 1.00 25.79 ? 213  GLU A CB     1 
ATOM   513  C CG     . GLU A 1 30  ? 46.141 36.290 62.798 1.00 27.36 ? 213  GLU A CG     1 
ATOM   514  C CD     . GLU A 1 30  ? 46.699 37.605 62.281 1.00 31.67 ? 213  GLU A CD     1 
ATOM   515  O OE1    . GLU A 1 30  ? 47.936 37.683 62.177 1.00 35.54 ? 213  GLU A OE1    1 
ATOM   516  O OE2    . GLU A 1 30  ? 45.936 38.540 61.962 1.00 32.33 ? 213  GLU A OE2    1 
ATOM   517  H H      . GLU A 1 30  ? 44.887 34.045 61.939 1.00 23.87 ? 213  GLU A H      1 
ATOM   518  H HA     . GLU A 1 30  ? 47.292 33.213 62.703 1.00 27.38 ? 213  GLU A HA     1 
ATOM   519  H HB2    . GLU A 1 30  ? 47.914 35.397 62.819 1.00 30.95 ? 213  GLU A HB2    1 
ATOM   520  H HB3    . GLU A 1 30  ? 47.101 35.165 61.474 1.00 30.95 ? 213  GLU A HB3    1 
ATOM   521  H HG2    . GLU A 1 30  ? 45.271 36.141 62.397 1.00 32.83 ? 213  GLU A HG2    1 
ATOM   522  H HG3    . GLU A 1 30  ? 46.057 36.344 63.763 1.00 32.83 ? 213  GLU A HG3    1 
ATOM   523  N N      . HIS A 1 31  ? 45.320 33.770 65.059 1.00 22.60 ? 214  HIS A N      1 
ATOM   524  C CA     . HIS A 1 31  ? 45.200 33.616 66.499 1.00 23.34 ? 214  HIS A CA     1 
ATOM   525  C C      . HIS A 1 31  ? 44.770 32.217 66.908 1.00 22.51 ? 214  HIS A C      1 
ATOM   526  O O      . HIS A 1 31  ? 44.364 32.020 68.066 1.00 24.40 ? 214  HIS A O      1 
ATOM   527  C CB     . HIS A 1 31  ? 44.241 34.635 67.126 1.00 27.29 ? 214  HIS A CB     1 
ATOM   528  C CG     . HIS A 1 31  ? 44.458 36.041 66.671 1.00 30.14 ? 214  HIS A CG     1 
ATOM   529  N ND1    . HIS A 1 31  ? 45.583 36.758 67.005 1.00 32.17 ? 214  HIS A ND1    1 
ATOM   530  C CD2    . HIS A 1 31  ? 43.689 36.868 65.929 1.00 32.60 ? 214  HIS A CD2    1 
ATOM   531  C CE1    . HIS A 1 31  ? 45.504 37.963 66.471 1.00 32.94 ? 214  HIS A CE1    1 
ATOM   532  N NE2    . HIS A 1 31  ? 44.366 38.052 65.811 1.00 33.82 ? 214  HIS A NE2    1 
ATOM   533  H H      . HIS A 1 31  ? 44.568 33.830 64.646 1.00 27.12 ? 214  HIS A H      1 
ATOM   534  H HA     . HIS A 1 31  ? 46.081 33.798 66.861 1.00 28.01 ? 214  HIS A HA     1 
ATOM   535  H HB2    . HIS A 1 31  ? 43.332 34.388 66.895 1.00 32.75 ? 214  HIS A HB2    1 
ATOM   536  H HB3    . HIS A 1 31  ? 44.355 34.616 68.089 1.00 32.75 ? 214  HIS A HB3    1 
ATOM   537  H HD1    . HIS A 1 31  ? 46.234 36.468 67.485 1.00 38.61 ? 214  HIS A HD1    1 
ATOM   538  H HD2    . HIS A 1 31  ? 42.855 36.670 65.567 1.00 39.11 ? 214  HIS A HD2    1 
ATOM   539  H HE1    . HIS A 1 31  ? 46.143 38.634 66.548 1.00 39.53 ? 214  HIS A HE1    1 
ATOM   540  N N      . GLY A 1 32  ? 44.828 31.252 66.000 1.00 21.49 ? 215  GLY A N      1 
ATOM   541  C CA     . GLY A 1 32  ? 44.561 29.884 66.357 1.00 20.82 ? 215  GLY A CA     1 
ATOM   542  C C      . GLY A 1 32  ? 43.093 29.517 66.414 1.00 20.24 ? 215  GLY A C      1 
ATOM   543  O O      . GLY A 1 32  ? 42.770 28.387 66.779 1.00 21.57 ? 215  GLY A O      1 
ATOM   544  H H      . GLY A 1 32  ? 45.021 31.374 65.171 1.00 25.79 ? 215  GLY A H      1 
ATOM   545  H HA2    . GLY A 1 32  ? 44.986 29.305 65.706 1.00 24.98 ? 215  GLY A HA2    1 
ATOM   546  H HA3    . GLY A 1 32  ? 44.943 29.711 67.232 1.00 24.98 ? 215  GLY A HA3    1 
ATOM   547  N N      . GLU A 1 33  ? 42.181 30.426 66.049 1.00 19.99 ? 216  GLU A N      1 
ATOM   548  C CA     . GLU A 1 33  ? 40.761 30.103 66.186 1.00 19.09 ? 216  GLU A CA     1 
ATOM   549  C C      . GLU A 1 33  ? 40.234 29.276 65.028 1.00 17.15 ? 216  GLU A C      1 
ATOM   550  O O      . GLU A 1 33  ? 39.228 28.582 65.187 1.00 17.18 ? 216  GLU A O      1 
ATOM   551  C CB     . GLU A 1 33  ? 39.921 31.381 66.338 1.00 19.95 ? 216  GLU A CB     1 
ATOM   552  C CG     . GLU A 1 33  ? 40.150 32.055 67.678 1.00 22.20 ? 216  GLU A CG     1 
ATOM   553  C CD     . GLU A 1 33  ? 39.234 33.231 67.911 1.00 25.61 ? 216  GLU A CD     1 
ATOM   554  O OE1    . GLU A 1 33  ? 39.353 34.221 67.177 1.00 29.28 ? 216  GLU A OE1    1 
ATOM   555  O OE2    . GLU A 1 33  ? 38.406 33.172 68.843 1.00 26.48 ? 216  GLU A OE2    1 
ATOM   556  H H      . GLU A 1 33  ? 42.354 31.206 65.732 1.00 23.99 ? 216  GLU A H      1 
ATOM   557  H HA     . GLU A 1 33  ? 40.656 29.582 66.997 1.00 22.91 ? 216  GLU A HA     1 
ATOM   558  H HB2    . GLU A 1 33  ? 40.164 32.007 65.638 1.00 23.94 ? 216  GLU A HB2    1 
ATOM   559  H HB3    . GLU A 1 33  ? 38.980 31.154 66.268 1.00 23.94 ? 216  GLU A HB3    1 
ATOM   560  H HG2    . GLU A 1 33  ? 39.994 31.410 68.386 1.00 26.64 ? 216  GLU A HG2    1 
ATOM   561  H HG3    . GLU A 1 33  ? 41.064 32.376 67.718 1.00 26.64 ? 216  GLU A HG3    1 
ATOM   562  N N      . PHE A 1 34  ? 40.842 29.382 63.859 1.00 15.08 ? 217  PHE A N      1 
ATOM   563  C CA     . PHE A 1 34  ? 40.406 28.620 62.696 1.00 14.15 ? 217  PHE A CA     1 
ATOM   564  C C      . PHE A 1 34  ? 41.602 27.993 62.005 1.00 13.55 ? 217  PHE A C      1 
ATOM   565  O O      . PHE A 1 34  ? 42.716 28.485 62.099 1.00 14.83 ? 217  PHE A O      1 
ATOM   566  C CB     . PHE A 1 34  ? 39.630 29.498 61.699 1.00 13.51 ? 217  PHE A CB     1 
ATOM   567  C CG     . PHE A 1 34  ? 38.412 30.111 62.279 1.00 13.18 ? 217  PHE A CG     1 
ATOM   568  C CD1    . PHE A 1 34  ? 37.209 29.427 62.303 1.00 12.64 ? 217  PHE A CD1    1 
ATOM   569  C CD2    . PHE A 1 34  ? 38.474 31.366 62.848 1.00 14.02 ? 217  PHE A CD2    1 
ATOM   570  C CE1    . PHE A 1 34  ? 36.086 29.982 62.865 1.00 13.47 ? 217  PHE A CE1    1 
ATOM   571  C CE2    . PHE A 1 34  ? 37.358 31.920 63.409 1.00 14.68 ? 217  PHE A CE2    1 
ATOM   572  C CZ     . PHE A 1 34  ? 36.163 31.242 63.415 1.00 13.38 ? 217  PHE A CZ     1 
ATOM   573  H H      . PHE A 1 34  ? 41.517 29.894 63.710 1.00 18.09 ? 217  PHE A H      1 
ATOM   574  H HA     . PHE A 1 34  ? 39.823 27.904 62.993 1.00 16.98 ? 217  PHE A HA     1 
ATOM   575  H HB2    . PHE A 1 34  ? 40.208 30.215 61.396 1.00 16.21 ? 217  PHE A HB2    1 
ATOM   576  H HB3    . PHE A 1 34  ? 39.357 28.950 60.946 1.00 16.21 ? 217  PHE A HB3    1 
ATOM   577  H HD1    . PHE A 1 34  ? 37.160 28.576 61.931 1.00 15.17 ? 217  PHE A HD1    1 
ATOM   578  H HD2    . PHE A 1 34  ? 39.276 31.837 62.849 1.00 16.83 ? 217  PHE A HD2    1 
ATOM   579  H HE1    . PHE A 1 34  ? 35.283 29.513 62.875 1.00 16.17 ? 217  PHE A HE1    1 
ATOM   580  H HE2    . PHE A 1 34  ? 37.407 32.766 63.792 1.00 17.62 ? 217  PHE A HE2    1 
ATOM   581  H HZ     . PHE A 1 34  ? 35.407 31.634 63.789 1.00 16.05 ? 217  PHE A HZ     1 
ATOM   582  N N      . GLU A 1 35  ? 41.327 26.911 61.268 1.00 13.41 ? 218  GLU A N      1 
ATOM   583  C CA     . GLU A 1 35  ? 42.283 26.245 60.410 1.00 14.83 ? 218  GLU A CA     1 
ATOM   584  C C      . GLU A 1 35  ? 41.681 26.259 59.019 1.00 13.22 ? 218  GLU A C      1 
ATOM   585  O O      . GLU A 1 35  ? 40.490 25.994 58.882 1.00 14.96 ? 218  GLU A O      1 
ATOM   586  C CB     . GLU A 1 35  ? 42.389 24.734 60.821 1.00 18.22 ? 218  GLU A CB     1 
ATOM   587  C CG     . GLU A 1 35  ? 43.227 23.816 59.936 1.00 21.40 ? 218  GLU A CG     1 
ATOM   588  C CD     . GLU A 1 35  ? 42.943 22.348 60.148 1.00 22.75 ? 218  GLU A CD     1 
ATOM   589  O OE1    . GLU A 1 35  ? 42.326 21.986 61.191 1.00 23.22 ? 218  GLU A OE1    1 
ATOM   590  O OE2    . GLU A 1 35  ? 43.393 21.572 59.277 1.00 25.97 ? 218  GLU A OE2    1 
ATOM   591  H H      . GLU A 1 35  ? 40.554 26.535 61.254 1.00 16.10 ? 218  GLU A H      1 
ATOM   592  H HA     . GLU A 1 35  ? 43.153 26.672 60.445 1.00 17.80 ? 218  GLU A HA     1 
ATOM   593  H HB2    . GLU A 1 35  ? 42.775 24.695 61.710 1.00 21.86 ? 218  GLU A HB2    1 
ATOM   594  H HB3    . GLU A 1 35  ? 41.491 24.367 60.834 1.00 21.86 ? 218  GLU A HB3    1 
ATOM   595  H HG2    . GLU A 1 35  ? 43.042 24.022 59.007 1.00 25.69 ? 218  GLU A HG2    1 
ATOM   596  H HG3    . GLU A 1 35  ? 44.166 23.967 60.129 1.00 25.69 ? 218  GLU A HG3    1 
ATOM   597  N N      . THR A 1 36  ? 42.481 26.490 57.995 1.00 12.25 ? 219  THR A N      1 
ATOM   598  C CA     A THR A 1 36  ? 41.968 26.434 56.633 0.62 13.46 ? 219  THR A CA     1 
ATOM   599  C CA     B THR A 1 36  ? 42.037 26.459 56.605 0.38 13.61 ? 219  THR A CA     1 
ATOM   600  C C      . THR A 1 36  ? 42.160 25.047 56.037 1.00 13.91 ? 219  THR A C      1 
ATOM   601  O O      . THR A 1 36  ? 43.135 24.344 56.293 1.00 16.09 ? 219  THR A O      1 
ATOM   602  C CB     A THR A 1 36  ? 42.611 27.453 55.701 0.62 16.22 ? 219  THR A CB     1 
ATOM   603  C CB     B THR A 1 36  ? 42.937 27.373 55.766 0.38 16.17 ? 219  THR A CB     1 
ATOM   604  O OG1    A THR A 1 36  ? 44.034 27.346 55.780 0.62 17.11 ? 219  THR A OG1    1 
ATOM   605  O OG1    B THR A 1 36  ? 43.013 28.685 56.345 0.38 17.45 ? 219  THR A OG1    1 
ATOM   606  C CG2    A THR A 1 36  ? 42.170 28.870 56.047 0.62 16.91 ? 219  THR A CG2    1 
ATOM   607  C CG2    B THR A 1 36  ? 42.437 27.507 54.338 0.38 16.48 ? 219  THR A CG2    1 
ATOM   608  H H      A THR A 1 36  ? 43.317 26.681 58.059 0.62 14.70 ? 219  THR A H      1 
ATOM   609  H H      B THR A 1 36  ? 43.317 26.675 58.076 0.38 14.70 ? 219  THR A H      1 
ATOM   610  H HA     A THR A 1 36  ? 41.023 26.644 56.686 0.62 16.15 ? 219  THR A HA     1 
ATOM   611  H HA     B THR A 1 36  ? 41.112 26.747 56.556 0.38 16.34 ? 219  THR A HA     1 
ATOM   612  H HB     A THR A 1 36  ? 42.331 27.277 54.789 0.62 19.47 ? 219  THR A HB     1 
ATOM   613  H HB     B THR A 1 36  ? 43.820 26.972 55.746 0.38 19.40 ? 219  THR A HB     1 
ATOM   614  H HG1    A THR A 1 36  ? 44.280 26.586 55.519 0.62 20.53 ? 219  THR A HG1    1 
ATOM   615  H HG1    B THR A 1 36  ? 43.499 29.180 55.872 0.38 20.94 ? 219  THR A HG1    1 
ATOM   616  H HG21   A THR A 1 36  ? 42.590 29.504 55.445 0.62 20.29 ? 219  THR A HG21   1 
ATOM   617  H HG21   B THR A 1 36  ? 43.047 28.056 53.823 0.38 19.77 ? 219  THR A HG21   1 
ATOM   618  H HG22   A THR A 1 36  ? 41.206 28.946 55.962 0.62 20.29 ? 219  THR A HG22   1 
ATOM   619  H HG22   B THR A 1 36  ? 42.375 26.631 53.925 0.38 19.77 ? 219  THR A HG22   1 
ATOM   620  H HG23   A THR A 1 36  ? 42.424 29.083 56.958 0.62 20.29 ? 219  THR A HG23   1 
ATOM   621  H HG23   B THR A 1 36  ? 41.559 27.920 54.332 0.38 19.77 ? 219  THR A HG23   1 
ATOM   622  N N      . VAL A 1 37  ? 41.203 24.661 55.224 1.00 12.82 ? 220  VAL A N      1 
ATOM   623  C CA     . VAL A 1 37  ? 41.218 23.409 54.473 1.00 13.39 ? 220  VAL A CA     1 
ATOM   624  C C      . VAL A 1 37  ? 41.200 23.795 53.005 1.00 13.49 ? 220  VAL A C      1 
ATOM   625  O O      . VAL A 1 37  ? 40.200 24.316 52.499 1.00 14.66 ? 220  VAL A O      1 
ATOM   626  C CB     . VAL A 1 37  ? 40.013 22.537 54.826 1.00 12.58 ? 220  VAL A CB     1 
ATOM   627  C CG1    . VAL A 1 37  ? 39.889 21.295 53.944 1.00 13.24 ? 220  VAL A CG1    1 
ATOM   628  C CG2    . VAL A 1 37  ? 40.083 22.086 56.292 1.00 13.27 ? 220  VAL A CG2    1 
ATOM   629  H H      . VAL A 1 37  ? 40.495 25.126 55.078 1.00 15.38 ? 220  VAL A H      1 
ATOM   630  H HA     . VAL A 1 37  ? 42.028 22.907 54.659 1.00 16.07 ? 220  VAL A HA     1 
ATOM   631  H HB     . VAL A 1 37  ? 39.229 23.087 54.676 1.00 15.10 ? 220  VAL A HB     1 
ATOM   632  H HG11   . VAL A 1 37  ? 39.103 20.794 54.214 1.00 15.89 ? 220  VAL A HG11   1 
ATOM   633  H HG12   . VAL A 1 37  ? 39.802 21.573 53.019 1.00 15.89 ? 220  VAL A HG12   1 
ATOM   634  H HG13   . VAL A 1 37  ? 40.683 20.749 54.053 1.00 15.89 ? 220  VAL A HG13   1 
ATOM   635  H HG21   . VAL A 1 37  ? 39.305 21.543 56.493 1.00 15.92 ? 220  VAL A HG21   1 
ATOM   636  H HG22   . VAL A 1 37  ? 40.892 21.567 56.425 1.00 15.92 ? 220  VAL A HG22   1 
ATOM   637  H HG23   . VAL A 1 37  ? 40.096 22.870 56.863 1.00 15.92 ? 220  VAL A HG23   1 
ATOM   638  N N      . ILE A 1 38  ? 42.272 23.490 52.348 1.00 16.90 ? 221  ILE A N      1 
ATOM   639  C CA     . ILE A 1 38  ? 42.514 23.741 50.951 1.00 19.13 ? 221  ILE A CA     1 
ATOM   640  C C      . ILE A 1 38  ? 41.969 22.600 50.130 1.00 16.71 ? 221  ILE A C      1 
ATOM   641  O O      . ILE A 1 38  ? 42.070 21.402 50.521 1.00 16.78 ? 221  ILE A O      1 
ATOM   642  C CB     . ILE A 1 38  ? 44.029 23.880 50.716 1.00 25.41 ? 221  ILE A CB     1 
ATOM   643  C CG1    . ILE A 1 38  ? 44.553 25.138 51.409 1.00 31.07 ? 221  ILE A CG1    1 
ATOM   644  C CG2    . ILE A 1 38  ? 44.348 23.811 49.230 1.00 27.51 ? 221  ILE A CG2    1 
ATOM   645  C CD1    . ILE A 1 38  ? 43.630 26.415 51.341 1.00 32.16 ? 221  ILE A CD1    1 
ATOM   646  H H      . ILE A 1 38  ? 42.944 23.100 52.717 1.00 20.28 ? 221  ILE A H      1 
ATOM   647  H HA     . ILE A 1 38  ? 42.054 24.554 50.685 1.00 22.96 ? 221  ILE A HA     1 
ATOM   648  H HB     . ILE A 1 38  ? 44.495 23.132 51.122 1.00 30.50 ? 221  ILE A HB     1 
ATOM   649  H HG12   . ILE A 1 38  ? 44.685 24.932 52.348 1.00 37.28 ? 221  ILE A HG12   1 
ATOM   650  H HG13   . ILE A 1 38  ? 45.400 25.377 51.000 1.00 37.28 ? 221  ILE A HG13   1 
ATOM   651  H HG21   . ILE A 1 38  ? 45.216 24.216 49.075 1.00 33.01 ? 221  ILE A HG21   1 
ATOM   652  H HG22   . ILE A 1 38  ? 44.362 22.882 48.953 1.00 33.01 ? 221  ILE A HG22   1 
ATOM   653  H HG23   . ILE A 1 38  ? 43.665 24.293 48.738 1.00 33.01 ? 221  ILE A HG23   1 
ATOM   654  H HD11   . ILE A 1 38  ? 44.151 27.195 51.590 1.00 38.59 ? 221  ILE A HD11   1 
ATOM   655  H HD12   . ILE A 1 38  ? 43.296 26.516 50.436 1.00 38.59 ? 221  ILE A HD12   1 
ATOM   656  H HD13   . ILE A 1 38  ? 42.889 26.303 51.957 1.00 38.59 ? 221  ILE A HD13   1 
ATOM   657  N N      . PHE A 1 39  ? 41.294 22.964 49.033 1.00 14.59 ? 222  PHE A N      1 
ATOM   658  C CA     . PHE A 1 39  ? 40.777 21.967 48.118 1.00 11.08 ? 222  PHE A CA     1 
ATOM   659  C C      . PHE A 1 39  ? 41.768 21.803 46.978 1.00 12.37 ? 222  PHE A C      1 
ATOM   660  O O      . PHE A 1 39  ? 42.432 20.766 46.882 1.00 14.45 ? 222  PHE A O      1 
ATOM   661  C CB     . PHE A 1 39  ? 39.361 22.326 47.647 1.00 11.22 ? 222  PHE A CB     1 
ATOM   662  C CG     . PHE A 1 39  ? 38.284 22.080 48.660 1.00 11.36 ? 222  PHE A CG     1 
ATOM   663  C CD1    . PHE A 1 39  ? 38.262 22.784 49.837 1.00 13.56 ? 222  PHE A CD1    1 
ATOM   664  C CD2    . PHE A 1 39  ? 37.279 21.139 48.436 1.00 11.63 ? 222  PHE A CD2    1 
ATOM   665  C CE1    . PHE A 1 39  ? 37.291 22.566 50.805 1.00 13.15 ? 222  PHE A CE1    1 
ATOM   666  C CE2    . PHE A 1 39  ? 36.303 20.928 49.369 1.00 10.97 ? 222  PHE A CE2    1 
ATOM   667  C CZ     . PHE A 1 39  ? 36.280 21.628 50.581 1.00 11.66 ? 222  PHE A CZ     1 
ATOM   668  H H      . PHE A 1 39  ? 41.128 23.777 48.807 1.00 17.51 ? 222  PHE A H      1 
ATOM   669  H HA     . PHE A 1 39  ? 40.678 21.106 48.554 1.00 13.29 ? 222  PHE A HA     1 
ATOM   670  H HB2    . PHE A 1 39  ? 39.341 23.270 47.423 1.00 13.46 ? 222  PHE A HB2    1 
ATOM   671  H HB3    . PHE A 1 39  ? 39.153 21.794 46.863 1.00 13.46 ? 222  PHE A HB3    1 
ATOM   672  H HD1    . PHE A 1 39  ? 38.917 23.427 49.991 1.00 16.28 ? 222  PHE A HD1    1 
ATOM   673  H HD2    . PHE A 1 39  ? 37.273 20.649 47.645 1.00 13.95 ? 222  PHE A HD2    1 
ATOM   674  H HE1    . PHE A 1 39  ? 37.314 23.044 51.603 1.00 15.78 ? 222  PHE A HE1    1 
ATOM   675  H HE2    . PHE A 1 39  ? 35.636 20.304 49.194 1.00 13.17 ? 222  PHE A HE2    1 
ATOM   676  H HZ     . PHE A 1 39  ? 35.617 21.474 51.215 1.00 13.99 ? 222  PHE A HZ     1 
ATOM   677  N N      . GLY A 1 40  ? 41.906 22.844 46.148 1.00 13.45 ? 223  GLY A N      1 
ATOM   678  C CA     . GLY A 1 40  ? 42.826 22.834 45.031 1.00 13.38 ? 223  GLY A CA     1 
ATOM   679  C C      . GLY A 1 40  ? 42.152 22.390 43.745 1.00 12.41 ? 223  GLY A C      1 
ATOM   680  O O      . GLY A 1 40  ? 41.234 21.568 43.739 1.00 12.39 ? 223  GLY A O      1 
ATOM   681  H H      . GLY A 1 40  ? 41.466 23.578 46.220 1.00 16.14 ? 223  GLY A H      1 
ATOM   682  H HA2    . GLY A 1 40  ? 43.183 23.726 44.899 1.00 16.06 ? 223  GLY A HA2    1 
ATOM   683  H HA3    . GLY A 1 40  ? 43.557 22.226 45.221 1.00 16.06 ? 223  GLY A HA3    1 
ATOM   684  N N      . ASP A 1 41  ? 42.625 22.939 42.632 1.00 12.81 ? 224  ASP A N      1 
ATOM   685  C CA     . ASP A 1 41  ? 41.945 22.703 41.358 1.00 13.58 ? 224  ASP A CA     1 
ATOM   686  C C      . ASP A 1 41  ? 41.945 21.226 40.982 1.00 12.85 ? 224  ASP A C      1 
ATOM   687  O O      . ASP A 1 41  ? 40.957 20.742 40.435 1.00 13.40 ? 224  ASP A O      1 
ATOM   688  C CB     . ASP A 1 41  ? 42.536 23.512 40.204 1.00 13.68 ? 224  ASP A CB     1 
ATOM   689  C CG     . ASP A 1 41  ? 42.204 24.997 40.275 1.00 13.92 ? 224  ASP A CG     1 
ATOM   690  O OD1    . ASP A 1 41  ? 41.549 25.402 41.258 1.00 14.34 ? 224  ASP A OD1    1 
ATOM   691  O OD2    . ASP A 1 41  ? 42.630 25.702 39.349 1.00 16.45 ? 224  ASP A OD2    1 
ATOM   692  H H      . ASP A 1 41  ? 43.322 23.441 42.585 1.00 15.37 ? 224  ASP A H      1 
ATOM   693  H HA     . ASP A 1 41  ? 41.034 23.011 41.485 1.00 16.30 ? 224  ASP A HA     1 
ATOM   694  H HB2    . ASP A 1 41  ? 43.502 23.423 40.221 1.00 16.41 ? 224  ASP A HB2    1 
ATOM   695  H HB3    . ASP A 1 41  ? 42.185 23.169 39.368 1.00 16.41 ? 224  ASP A HB3    1 
ATOM   696  N N      . LYS A 1 42  ? 43.036 20.493 41.232 1.00 14.48 ? 225  LYS A N      1 
ATOM   697  C CA     . LYS A 1 42  ? 43.069 19.097 40.788 1.00 15.66 ? 225  LYS A CA     1 
ATOM   698  C C      . LYS A 1 42  ? 42.006 18.280 41.503 1.00 14.35 ? 225  LYS A C      1 
ATOM   699  O O      . LYS A 1 42  ? 41.307 17.473 40.877 1.00 14.08 ? 225  LYS A O      1 
ATOM   700  C CB     . LYS A 1 42  ? 44.458 18.518 41.042 1.00 18.63 ? 225  LYS A CB     1 
ATOM   701  C CG     . LYS A 1 42  ? 44.576 17.013 40.902 1.00 22.67 ? 225  LYS A CG     1 
ATOM   702  C CD     . LYS A 1 42  ? 44.432 16.597 39.467 1.00 27.44 ? 225  LYS A CD     1 
ATOM   703  C CE     . LYS A 1 42  ? 44.524 15.075 39.346 1.00 30.01 ? 225  LYS A CE     1 
ATOM   704  N NZ     . LYS A 1 42  ? 44.236 14.629 37.965 1.00 31.89 ? 225  LYS A NZ     1 
ATOM   705  H H      . LYS A 1 42  ? 43.740 20.770 41.640 1.00 17.37 ? 225  LYS A H      1 
ATOM   706  H HA     . LYS A 1 42  ? 42.892 19.053 39.836 1.00 18.79 ? 225  LYS A HA     1 
ATOM   707  H HB2    . LYS A 1 42  ? 45.075 18.915 40.407 1.00 22.36 ? 225  LYS A HB2    1 
ATOM   708  H HB3    . LYS A 1 42  ? 44.723 18.745 41.947 1.00 22.36 ? 225  LYS A HB3    1 
ATOM   709  H HG2    . LYS A 1 42  ? 45.446 16.725 41.221 1.00 27.20 ? 225  LYS A HG2    1 
ATOM   710  H HG3    . LYS A 1 42  ? 43.875 16.585 41.419 1.00 27.20 ? 225  LYS A HG3    1 
ATOM   711  H HD2    . LYS A 1 42  ? 43.569 16.884 39.129 1.00 32.92 ? 225  LYS A HD2    1 
ATOM   712  H HD3    . LYS A 1 42  ? 45.143 16.993 38.939 1.00 32.92 ? 225  LYS A HD3    1 
ATOM   713  H HE2    . LYS A 1 42  ? 45.419 14.787 39.581 1.00 36.02 ? 225  LYS A HE2    1 
ATOM   714  H HE3    . LYS A 1 42  ? 43.876 14.666 39.941 1.00 36.02 ? 225  LYS A HE3    1 
ATOM   715  H HZ1    . LYS A 1 42  ? 44.294 13.743 37.914 1.00 38.27 ? 225  LYS A HZ1    1 
ATOM   716  H HZ2    . LYS A 1 42  ? 43.416 14.880 37.729 1.00 38.27 ? 225  LYS A HZ2    1 
ATOM   717  H HZ3    . LYS A 1 42  ? 44.822 14.990 37.401 1.00 38.27 ? 225  LYS A HZ3    1 
ATOM   718  N N      . VAL A 1 43  ? 41.848 18.493 42.803 1.00 13.65 ? 226  VAL A N      1 
ATOM   719  C CA     . VAL A 1 43  ? 40.831 17.800 43.576 1.00 12.24 ? 226  VAL A CA     1 
ATOM   720  C C      . VAL A 1 43  ? 39.442 18.202 43.106 1.00 11.84 ? 226  VAL A C      1 
ATOM   721  O O      . VAL A 1 43  ? 38.580 17.363 42.852 1.00 11.62 ? 226  VAL A O      1 
ATOM   722  C CB     . VAL A 1 43  ? 41.035 18.047 45.080 1.00 14.61 ? 226  VAL A CB     1 
ATOM   723  C CG1    . VAL A 1 43  ? 39.834 17.655 45.859 1.00 17.32 ? 226  VAL A CG1    1 
ATOM   724  C CG2    . VAL A 1 43  ? 42.296 17.307 45.569 1.00 16.04 ? 226  VAL A CG2    1 
ATOM   725  H H      . VAL A 1 43  ? 42.323 19.040 43.266 1.00 16.38 ? 226  VAL A H      1 
ATOM   726  H HA     . VAL A 1 43  ? 40.921 16.846 43.427 1.00 14.69 ? 226  VAL A HA     1 
ATOM   727  H HB     . VAL A 1 43  ? 41.167 18.996 45.230 1.00 17.53 ? 226  VAL A HB     1 
ATOM   728  H HG11   . VAL A 1 43  ? 40.011 17.793 46.803 1.00 20.79 ? 226  VAL A HG11   1 
ATOM   729  H HG12   . VAL A 1 43  ? 39.084 18.202 45.579 1.00 20.79 ? 226  VAL A HG12   1 
ATOM   730  H HG13   . VAL A 1 43  ? 39.642 16.719 45.692 1.00 20.79 ? 226  VAL A HG13   1 
ATOM   731  H HG21   . VAL A 1 43  ? 42.368 17.407 46.531 1.00 19.25 ? 226  VAL A HG21   1 
ATOM   732  H HG22   . VAL A 1 43  ? 42.219 16.368 45.339 1.00 19.25 ? 226  VAL A HG22   1 
ATOM   733  H HG23   . VAL A 1 43  ? 43.075 17.691 45.137 1.00 19.25 ? 226  VAL A HG23   1 
ATOM   734  N N      . ILE A 1 44  ? 39.201 19.503 42.971 1.00 11.41 ? 227  ILE A N      1 
ATOM   735  C CA     . ILE A 1 44  ? 37.876 19.991 42.587 1.00 10.99 ? 227  ILE A CA     1 
ATOM   736  C C      . ILE A 1 44  ? 37.478 19.419 41.236 1.00 11.49 ? 227  ILE A C      1 
ATOM   737  O O      . ILE A 1 44  ? 36.349 18.956 41.052 1.00 12.16 ? 227  ILE A O      1 
ATOM   738  C CB     . ILE A 1 44  ? 37.847 21.536 42.594 1.00 10.78 ? 227  ILE A CB     1 
ATOM   739  C CG1    . ILE A 1 44  ? 37.920 22.061 44.031 1.00 12.40 ? 227  ILE A CG1    1 
ATOM   740  C CG2    . ILE A 1 44  ? 36.612 22.053 41.845 1.00 11.73 ? 227  ILE A CG2    1 
ATOM   741  C CD1    . ILE A 1 44  ? 38.207 23.570 44.126 1.00 12.63 ? 227  ILE A CD1    1 
ATOM   742  H H      . ILE A 1 44  ? 39.783 20.124 43.096 1.00 13.69 ? 227  ILE A H      1 
ATOM   743  H HA     . ILE A 1 44  ? 37.228 19.683 43.239 1.00 13.19 ? 227  ILE A HA     1 
ATOM   744  H HB     . ILE A 1 44  ? 38.628 21.870 42.124 1.00 12.94 ? 227  ILE A HB     1 
ATOM   745  H HG12   . ILE A 1 44  ? 37.070 21.894 44.467 1.00 14.88 ? 227  ILE A HG12   1 
ATOM   746  H HG13   . ILE A 1 44  ? 38.631 21.595 44.498 1.00 14.88 ? 227  ILE A HG13   1 
ATOM   747  H HG21   . ILE A 1 44  ? 36.605 23.022 41.878 1.00 14.08 ? 227  ILE A HG21   1 
ATOM   748  H HG22   . ILE A 1 44  ? 36.654 21.754 40.923 1.00 14.08 ? 227  ILE A HG22   1 
ATOM   749  H HG23   . ILE A 1 44  ? 35.814 21.702 42.270 1.00 14.08 ? 227  ILE A HG23   1 
ATOM   750  H HD11   . ILE A 1 44  ? 38.240 23.826 45.061 1.00 15.16 ? 227  ILE A HD11   1 
ATOM   751  H HD12   . ILE A 1 44  ? 39.059 23.757 43.702 1.00 15.16 ? 227  ILE A HD12   1 
ATOM   752  H HD13   . ILE A 1 44  ? 37.499 24.055 43.674 1.00 15.16 ? 227  ILE A HD13   1 
ATOM   753  N N      . LEU A 1 45  ? 38.387 19.445 40.276 1.00 11.82 ? 228  LEU A N      1 
ATOM   754  C CA     . LEU A 1 45  ? 38.071 19.063 38.901 1.00 13.76 ? 228  LEU A CA     1 
ATOM   755  C C      . LEU A 1 45  ? 38.050 17.555 38.727 1.00 14.90 ? 228  LEU A C      1 
ATOM   756  O O      . LEU A 1 45  ? 37.206 17.029 37.982 1.00 17.17 ? 228  LEU A O      1 
ATOM   757  C CB     . LEU A 1 45  ? 39.064 19.690 37.919 1.00 13.97 ? 228  LEU A CB     1 
ATOM   758  C CG     . LEU A 1 45  ? 38.953 21.212 37.847 1.00 15.40 ? 228  LEU A CG     1 
ATOM   759  C CD1    . LEU A 1 45  ? 40.082 21.742 37.017 1.00 17.00 ? 228  LEU A CD1    1 
ATOM   760  C CD2    . LEU A 1 45  ? 37.635 21.706 37.308 1.00 16.52 ? 228  LEU A CD2    1 
ATOM   761  H H      . LEU A 1 45  ? 39.206 19.682 40.390 1.00 14.18 ? 228  LEU A H      1 
ATOM   762  H HA     . LEU A 1 45  ? 37.189 19.407 38.690 1.00 16.51 ? 228  LEU A HA     1 
ATOM   763  H HB2    . LEU A 1 45  ? 39.966 19.469 38.200 1.00 16.76 ? 228  LEU A HB2    1 
ATOM   764  H HB3    . LEU A 1 45  ? 38.896 19.335 37.032 1.00 16.76 ? 228  LEU A HB3    1 
ATOM   765  H HG     . LEU A 1 45  ? 39.002 21.554 38.753 1.00 18.48 ? 228  LEU A HG     1 
ATOM   766  H HD11   . LEU A 1 45  ? 40.014 22.709 36.971 1.00 20.40 ? 228  LEU A HD11   1 
ATOM   767  H HD12   . LEU A 1 45  ? 40.923 21.489 37.430 1.00 20.40 ? 228  LEU A HD12   1 
ATOM   768  H HD13   . LEU A 1 45  ? 40.024 21.364 36.126 1.00 20.40 ? 228  LEU A HD13   1 
ATOM   769  H HD21   . LEU A 1 45  ? 37.633 22.676 37.317 1.00 19.82 ? 228  LEU A HD21   1 
ATOM   770  H HD22   . LEU A 1 45  ? 37.524 21.383 36.400 1.00 19.82 ? 228  LEU A HD22   1 
ATOM   771  H HD23   . LEU A 1 45  ? 36.919 21.368 37.868 1.00 19.82 ? 228  LEU A HD23   1 
ATOM   772  N N      . ASP A 1 46  ? 39.001 16.840 39.346 1.00 15.60 ? 229  ASP A N      1 
ATOM   773  C CA     . ASP A 1 46  ? 39.249 15.447 38.967 1.00 17.11 ? 229  ASP A CA     1 
ATOM   774  C C      . ASP A 1 46  ? 38.902 14.406 40.027 1.00 16.90 ? 229  ASP A C      1 
ATOM   775  O O      . ASP A 1 46  ? 38.800 13.227 39.691 1.00 21.10 ? 229  ASP A O      1 
ATOM   776  C CB     . ASP A 1 46  ? 40.729 15.254 38.581 1.00 20.34 ? 229  ASP A CB     1 
ATOM   777  C CG     . ASP A 1 46  ? 41.140 16.015 37.327 1.00 24.80 ? 229  ASP A CG     1 
ATOM   778  O OD1    . ASP A 1 46  ? 40.253 16.499 36.594 1.00 27.34 ? 229  ASP A OD1    1 
ATOM   779  O OD2    . ASP A 1 46  ? 42.371 16.136 37.075 1.00 28.66 ? 229  ASP A OD2    1 
ATOM   780  H H      . ASP A 1 46  ? 39.505 17.138 39.976 1.00 18.72 ? 229  ASP A H      1 
ATOM   781  H HA     . ASP A 1 46  ? 38.693 15.259 38.195 1.00 20.54 ? 229  ASP A HA     1 
ATOM   782  H HB2    . ASP A 1 46  ? 41.286 15.565 39.312 1.00 24.41 ? 229  ASP A HB2    1 
ATOM   783  H HB3    . ASP A 1 46  ? 40.889 14.311 38.421 1.00 24.41 ? 229  ASP A HB3    1 
ATOM   784  N N      . GLU A 1 47  ? 38.723 14.782 41.269 1.00 13.41 ? 230  GLU A N      1 
ATOM   785  C CA     A GLU A 1 47  ? 38.425 13.830 42.325 0.71 13.13 ? 230  GLU A CA     1 
ATOM   786  C CA     B GLU A 1 47  ? 38.428 13.825 42.323 0.29 11.52 ? 230  GLU A CA     1 
ATOM   787  C C      . GLU A 1 47  ? 36.931 13.792 42.602 1.00 11.60 ? 230  GLU A C      1 
ATOM   788  O O      . GLU A 1 47  ? 36.222 14.793 42.448 1.00 12.73 ? 230  GLU A O      1 
ATOM   789  C CB     A GLU A 1 47  ? 39.150 14.183 43.616 0.71 16.36 ? 230  GLU A CB     1 
ATOM   790  C CB     B GLU A 1 47  ? 39.190 14.148 43.612 0.29 11.01 ? 230  GLU A CB     1 
ATOM   791  C CG     A GLU A 1 47  ? 38.939 13.191 44.711 0.71 20.19 ? 230  GLU A CG     1 
ATOM   792  C CG     B GLU A 1 47  ? 40.717 13.953 43.526 0.29 12.22 ? 230  GLU A CG     1 
ATOM   793  C CD     A GLU A 1 47  ? 39.399 11.770 44.308 0.71 23.39 ? 230  GLU A CD     1 
ATOM   794  C CD     B GLU A 1 47  ? 41.372 13.783 44.910 0.29 18.11 ? 230  GLU A CD     1 
ATOM   795  O OE1    A GLU A 1 47  ? 40.633 11.570 44.402 0.71 26.00 ? 230  GLU A OE1    1 
ATOM   796  O OE1    B GLU A 1 47  ? 40.652 13.917 45.916 0.29 20.70 ? 230  GLU A OE1    1 
ATOM   797  O OE2    A GLU A 1 47  ? 38.580 10.862 43.877 0.71 21.40 ? 230  GLU A OE2    1 
ATOM   798  O OE2    B GLU A 1 47  ? 42.600 13.519 45.006 0.29 20.95 ? 230  GLU A OE2    1 
ATOM   799  H H      A GLU A 1 47  ? 38.770 15.597 41.537 0.71 16.09 ? 230  GLU A H      1 
ATOM   800  H H      B GLU A 1 47  ? 38.767 15.597 41.538 0.29 16.09 ? 230  GLU A H      1 
ATOM   801  H HA     A GLU A 1 47  ? 38.717 12.951 42.036 0.71 15.76 ? 230  GLU A HA     1 
ATOM   802  H HA     B GLU A 1 47  ? 38.709 12.943 42.031 0.29 13.83 ? 230  GLU A HA     1 
ATOM   803  H HB2    A GLU A 1 47  ? 40.102 14.229 43.437 0.71 19.63 ? 230  GLU A HB2    1 
ATOM   804  H HB2    B GLU A 1 47  ? 39.026 15.077 43.842 0.29 13.22 ? 230  GLU A HB2    1 
ATOM   805  H HB3    A GLU A 1 47  ? 38.829 15.043 43.929 0.71 19.63 ? 230  GLU A HB3    1 
ATOM   806  H HB3    B GLU A 1 47  ? 38.860 13.570 44.318 0.29 13.22 ? 230  GLU A HB3    1 
ATOM   807  H HG2    A GLU A 1 47  ? 39.448 13.464 45.490 0.71 24.23 ? 230  GLU A HG2    1 
ATOM   808  H HG2    B GLU A 1 47  ? 40.906 13.157 43.005 0.29 14.66 ? 230  GLU A HG2    1 
ATOM   809  H HG3    A GLU A 1 47  ? 37.994 13.153 44.928 0.71 24.23 ? 230  GLU A HG3    1 
ATOM   810  H HG3    B GLU A 1 47  ? 41.112 14.730 43.100 0.29 14.66 ? 230  GLU A HG3    1 
ATOM   811  N N      . ARG A 1 48  ? 36.466 12.638 43.032 1.00 12.40 ? 231  ARG A N      1 
ATOM   812  C CA     . ARG A 1 48  ? 35.063 12.494 43.361 1.00 13.09 ? 231  ARG A CA     1 
ATOM   813  C C      . ARG A 1 48  ? 34.728 13.247 44.630 1.00 10.98 ? 231  ARG A C      1 
ATOM   814  O O      . ARG A 1 48  ? 35.542 13.376 45.552 1.00 10.99 ? 231  ARG A O      1 
ATOM   815  C CB     . ARG A 1 48  ? 34.753 11.015 43.579 1.00 16.28 ? 231  ARG A CB     1 
ATOM   816  C CG     . ARG A 1 48  ? 34.841 10.267 42.245 1.00 20.06 ? 231  ARG A CG     1 
ATOM   817  C CD     . ARG A 1 48  ? 34.231 9.005  42.175 1.00 21.98 ? 231  ARG A CD     1 
ATOM   818  N NE     . ARG A 1 48  ? 32.884 8.880  42.729 1.00 20.13 ? 231  ARG A NE     1 
ATOM   819  C CZ     . ARG A 1 48  ? 32.419 7.658  42.913 1.00 18.36 ? 231  ARG A CZ     1 
ATOM   820  N NH1    . ARG A 1 48  ? 33.048 6.630  42.395 1.00 17.93 ? 231  ARG A NH1    1 
ATOM   821  N NH2    . ARG A 1 48  ? 31.386 7.451  43.719 1.00 22.52 ? 231  ARG A NH2    1 
ATOM   822  H H      . ARG A 1 48  ? 36.937 11.927 43.142 1.00 14.88 ? 231  ARG A H      1 
ATOM   823  H HA     . ARG A 1 48  ? 34.519 12.846 42.639 1.00 15.71 ? 231  ARG A HA     1 
ATOM   824  H HB2    . ARG A 1 48  ? 35.397 10.633 44.196 1.00 19.53 ? 231  ARG A HB2    1 
ATOM   825  H HB3    . ARG A 1 48  ? 33.855 10.917 43.934 1.00 19.53 ? 231  ARG A HB3    1 
ATOM   826  H HG2    . ARG A 1 48  ? 34.423 10.819 41.565 1.00 24.07 ? 231  ARG A HG2    1 
ATOM   827  H HG3    . ARG A 1 48  ? 35.779 10.137 42.036 1.00 24.07 ? 231  ARG A HG3    1 
ATOM   828  H HD2    . ARG A 1 48  ? 34.174 8.753  41.240 1.00 26.37 ? 231  ARG A HD2    1 
ATOM   829  H HD3    . ARG A 1 48  ? 34.792 8.376  42.655 1.00 26.37 ? 231  ARG A HD3    1 
ATOM   830  H HE     . ARG A 1 48  ? 32.415 9.573  42.928 1.00 24.16 ? 231  ARG A HE     1 
ATOM   831  H HH11   . ARG A 1 48  ? 33.765 6.751  41.936 1.00 21.52 ? 231  ARG A HH11   1 
ATOM   832  H HH12   . ARG A 1 48  ? 32.744 5.835  42.516 1.00 21.52 ? 231  ARG A HH12   1 
ATOM   833  H HH21   . ARG A 1 48  ? 31.017 8.114  44.124 1.00 27.02 ? 231  ARG A HH21   1 
ATOM   834  H HH22   . ARG A 1 48  ? 31.086 6.654  43.836 1.00 27.02 ? 231  ARG A HH22   1 
ATOM   835  N N      . ILE A 1 49  ? 33.485 13.717 44.696 1.00 10.64 ? 232  ILE A N      1 
ATOM   836  C CA     . ILE A 1 49  ? 33.090 14.557 45.829 1.00 10.15 ? 232  ILE A CA     1 
ATOM   837  C C      . ILE A 1 49  ? 33.189 13.855 47.168 1.00 9.45  ? 232  ILE A C      1 
ATOM   838  O O      . ILE A 1 49  ? 33.417 14.494 48.190 1.00 10.39 ? 232  ILE A O      1 
ATOM   839  C CB     . ILE A 1 49  ? 31.659 15.132 45.651 1.00 10.88 ? 232  ILE A CB     1 
ATOM   840  C CG1    . ILE A 1 49  ? 30.622 14.008 45.514 1.00 13.66 ? 232  ILE A CG1    1 
ATOM   841  C CG2    . ILE A 1 49  ? 31.636 16.092 44.482 1.00 12.30 ? 232  ILE A CG2    1 
ATOM   842  C CD1    . ILE A 1 49  ? 29.196 14.439 45.721 1.00 17.34 ? 232  ILE A CD1    1 
ATOM   843  H H      . ILE A 1 49  ? 32.867 13.569 44.116 1.00 12.77 ? 232  ILE A H      1 
ATOM   844  H HA     . ILE A 1 49  ? 33.731 15.286 45.825 1.00 12.18 ? 232  ILE A HA     1 
ATOM   845  H HB     . ILE A 1 49  ? 31.415 15.627 46.449 1.00 13.06 ? 232  ILE A HB     1 
ATOM   846  H HG12   . ILE A 1 49  ? 30.687 13.637 44.620 1.00 16.40 ? 232  ILE A HG12   1 
ATOM   847  H HG13   . ILE A 1 49  ? 30.819 13.325 46.173 1.00 16.40 ? 232  ILE A HG13   1 
ATOM   848  H HG21   . ILE A 1 49  ? 30.745 16.467 44.398 1.00 14.76 ? 232  ILE A HG21   1 
ATOM   849  H HG22   . ILE A 1 49  ? 32.279 16.800 44.641 1.00 14.76 ? 232  ILE A HG22   1 
ATOM   850  H HG23   . ILE A 1 49  ? 31.868 15.609 43.673 1.00 14.76 ? 232  ILE A HG23   1 
ATOM   851  H HD11   . ILE A 1 49  ? 28.610 13.686 45.548 1.00 20.81 ? 232  ILE A HD11   1 
ATOM   852  H HD12   . ILE A 1 49  ? 29.087 14.739 46.637 1.00 20.81 ? 232  ILE A HD12   1 
ATOM   853  H HD13   . ILE A 1 49  ? 28.993 15.164 45.109 1.00 20.81 ? 232  ILE A HD13   1 
ATOM   854  N N      . GLU A 1 50  ? 33.032 12.526 47.188 1.00 10.18 ? 233  GLU A N      1 
ATOM   855  C CA     . GLU A 1 50  ? 33.132 11.800 48.435 1.00 11.61 ? 233  GLU A CA     1 
ATOM   856  C C      . GLU A 1 50  ? 34.560 11.786 48.961 1.00 11.53 ? 233  GLU A C      1 
ATOM   857  O O      . GLU A 1 50  ? 34.774 11.422 50.118 1.00 12.97 ? 233  GLU A O      1 
ATOM   858  C CB     . GLU A 1 50  ? 32.683 10.340 48.236 1.00 12.94 ? 233  GLU A CB     1 
ATOM   859  C CG     . GLU A 1 50  ? 31.234 10.157 47.797 1.00 13.03 ? 233  GLU A CG     1 
ATOM   860  C CD     . GLU A 1 50  ? 31.033 10.154 46.300 1.00 14.55 ? 233  GLU A CD     1 
ATOM   861  O OE1    . GLU A 1 50  ? 31.894 10.557 45.517 1.00 15.07 ? 233  GLU A OE1    1 
ATOM   862  O OE2    . GLU A 1 50  ? 29.950 9.677  45.895 1.00 19.02 ? 233  GLU A OE2    1 
ATOM   863  H H      . GLU A 1 50  ? 32.869 12.038 46.499 1.00 12.22 ? 233  GLU A H      1 
ATOM   864  H HA     . GLU A 1 50  ? 32.550 12.224 49.085 1.00 13.93 ? 233  GLU A HA     1 
ATOM   865  H HB2    . GLU A 1 50  ? 33.245 9.937  47.556 1.00 15.53 ? 233  GLU A HB2    1 
ATOM   866  H HB3    . GLU A 1 50  ? 32.791 9.870  49.078 1.00 15.53 ? 233  GLU A HB3    1 
ATOM   867  H HG2    . GLU A 1 50  ? 30.912 9.308  48.137 1.00 15.64 ? 233  GLU A HG2    1 
ATOM   868  H HG3    . GLU A 1 50  ? 30.705 10.883 48.162 1.00 15.64 ? 233  GLU A HG3    1 
ATOM   869  N N      . ASN A 1 51  ? 35.529 12.121 48.115 1.00 10.33 ? 234  ASN A N      1 
ATOM   870  C CA     . ASN A 1 51  ? 36.921 12.207 48.508 1.00 11.39 ? 234  ASN A CA     1 
ATOM   871  C C      . ASN A 1 51  ? 37.412 13.626 48.712 1.00 10.63 ? 234  ASN A C      1 
ATOM   872  O O      . ASN A 1 51  ? 38.566 13.807 49.105 1.00 11.30 ? 234  ASN A O      1 
ATOM   873  C CB     . ASN A 1 51  ? 37.800 11.489 47.489 1.00 13.17 ? 234  ASN A CB     1 
ATOM   874  C CG     . ASN A 1 51  ? 37.562 10.005 47.454 1.00 14.87 ? 234  ASN A CG     1 
ATOM   875  O OD1    . ASN A 1 51  ? 37.193 9.417  48.458 1.00 16.88 ? 234  ASN A OD1    1 
ATOM   876  N ND2    . ASN A 1 51  ? 37.732 9.430  46.290 1.00 14.89 ? 234  ASN A ND2    1 
ATOM   877  H H      . ASN A 1 51  ? 35.397 12.307 47.286 1.00 12.40 ? 234  ASN A H      1 
ATOM   878  H HA     . ASN A 1 51  ? 37.022 11.752 49.359 1.00 13.67 ? 234  ASN A HA     1 
ATOM   879  H HB2    . ASN A 1 51  ? 37.613 11.843 46.606 1.00 15.80 ? 234  ASN A HB2    1 
ATOM   880  H HB3    . ASN A 1 51  ? 38.732 11.637 47.716 1.00 15.80 ? 234  ASN A HB3    1 
ATOM   881  H HD21   . ASN A 1 51  ? 37.610 8.583  46.207 1.00 17.86 ? 234  ASN A HD21   1 
ATOM   882  H HD22   . ASN A 1 51  ? 37.965 9.899  45.608 1.00 17.86 ? 234  ASN A HD22   1 
ATOM   883  N N      . TRP A 1 52  ? 36.599 14.649 48.440 1.00 10.03 ? 235  TRP A N      1 
ATOM   884  C CA     . TRP A 1 52  ? 37.011 15.989 48.754 1.00 9.50  ? 235  TRP A CA     1 
ATOM   885  C C      . TRP A 1 52  ? 37.235 16.108 50.262 1.00 9.27  ? 235  TRP A C      1 
ATOM   886  O O      . TRP A 1 52  ? 36.568 15.468 51.056 1.00 9.68  ? 235  TRP A O      1 
ATOM   887  C CB     . TRP A 1 52  ? 35.922 16.972 48.324 1.00 9.45  ? 235  TRP A CB     1 
ATOM   888  C CG     . TRP A 1 52  ? 35.816 17.194 46.859 1.00 9.36  ? 235  TRP A CG     1 
ATOM   889  C CD1    . TRP A 1 52  ? 36.439 16.550 45.852 1.00 9.70  ? 235  TRP A CD1    1 
ATOM   890  C CD2    . TRP A 1 52  ? 35.022 18.223 46.228 1.00 9.53  ? 235  TRP A CD2    1 
ATOM   891  N NE1    . TRP A 1 52  ? 36.076 17.058 44.634 1.00 10.32 ? 235  TRP A NE1    1 
ATOM   892  C CE2    . TRP A 1 52  ? 35.232 18.119 44.852 1.00 10.11 ? 235  TRP A CE2    1 
ATOM   893  C CE3    . TRP A 1 52  ? 34.191 19.210 46.709 1.00 10.02 ? 235  TRP A CE3    1 
ATOM   894  C CZ2    . TRP A 1 52  ? 34.608 18.968 43.930 1.00 10.28 ? 235  TRP A CZ2    1 
ATOM   895  C CZ3    . TRP A 1 52  ? 33.542 20.049 45.776 1.00 10.14 ? 235  TRP A CZ3    1 
ATOM   896  C CH2    . TRP A 1 52  ? 33.765 19.918 44.429 1.00 10.85 ? 235  TRP A CH2    1 
ATOM   897  H H      . TRP A 1 52  ? 35.821 14.582 48.080 1.00 12.03 ? 235  TRP A H      1 
ATOM   898  H HA     . TRP A 1 52  ? 37.835 16.207 48.291 1.00 11.40 ? 235  TRP A HA     1 
ATOM   899  H HB2    . TRP A 1 52  ? 35.066 16.634 48.630 1.00 11.34 ? 235  TRP A HB2    1 
ATOM   900  H HB3    . TRP A 1 52  ? 36.105 17.831 48.736 1.00 11.34 ? 235  TRP A HB3    1 
ATOM   901  H HD1    . TRP A 1 52  ? 37.039 15.850 45.970 1.00 11.63 ? 235  TRP A HD1    1 
ATOM   902  H HE1    . TRP A 1 52  ? 36.332 16.764 43.867 1.00 12.38 ? 235  TRP A HE1    1 
ATOM   903  H HE3    . TRP A 1 52  ? 34.060 19.321 47.623 1.00 12.02 ? 235  TRP A HE3    1 
ATOM   904  H HZ2    . TRP A 1 52  ? 34.761 18.887 43.016 1.00 12.33 ? 235  TRP A HZ2    1 
ATOM   905  H HZ3    . TRP A 1 52  ? 32.954 20.702 46.081 1.00 12.17 ? 235  TRP A HZ3    1 
ATOM   906  H HH2    . TRP A 1 52  ? 33.331 20.492 43.840 1.00 13.02 ? 235  TRP A HH2    1 
ATOM   907  N N      . PRO A 1 53  ? 38.159 16.970 50.691 1.00 9.66  ? 236  PRO A N      1 
ATOM   908  C CA     . PRO A 1 53  ? 38.353 17.191 52.117 1.00 9.76  ? 236  PRO A CA     1 
ATOM   909  C C      . PRO A 1 53  ? 37.107 17.814 52.702 1.00 9.51  ? 236  PRO A C      1 
ATOM   910  O O      . PRO A 1 53  ? 36.290 18.442 51.988 1.00 9.81  ? 236  PRO A O      1 
ATOM   911  C CB     . PRO A 1 53  ? 39.543 18.152 52.175 1.00 11.18 ? 236  PRO A CB     1 
ATOM   912  C CG     . PRO A 1 53  ? 39.470 18.910 50.846 1.00 11.32 ? 236  PRO A CG     1 
ATOM   913  C CD     . PRO A 1 53  ? 38.976 17.870 49.862 1.00 10.51 ? 236  PRO A CD     1 
ATOM   914  H HA     . PRO A 1 53  ? 38.585 16.375 52.587 1.00 11.71 ? 236  PRO A HA     1 
ATOM   915  H HB2    . PRO A 1 53  ? 39.450 18.755 52.929 1.00 13.42 ? 236  PRO A HB2    1 
ATOM   916  H HB3    . PRO A 1 53  ? 40.372 17.654 52.250 1.00 13.42 ? 236  PRO A HB3    1 
ATOM   917  H HG2    . PRO A 1 53  ? 38.847 19.650 50.916 1.00 13.59 ? 236  PRO A HG2    1 
ATOM   918  H HG3    . PRO A 1 53  ? 40.348 19.238 50.598 1.00 13.59 ? 236  PRO A HG3    1 
ATOM   919  H HD2    . PRO A 1 53  ? 38.438 18.281 49.168 1.00 12.61 ? 236  PRO A HD2    1 
ATOM   920  H HD3    . PRO A 1 53  ? 39.720 17.391 49.465 1.00 12.61 ? 236  PRO A HD3    1 
ATOM   921  N N      . THR A 1 54  ? 36.946 17.688 54.010 1.00 9.23  ? 237  THR A N      1 
ATOM   922  C CA     . THR A 1 54  ? 35.794 18.235 54.726 1.00 9.91  ? 237  THR A CA     1 
ATOM   923  C C      . THR A 1 54  ? 36.210 19.234 55.796 1.00 10.25 ? 237  THR A C      1 
ATOM   924  O O      . THR A 1 54  ? 37.392 19.379 56.169 1.00 10.57 ? 237  THR A O      1 
ATOM   925  C CB     . THR A 1 54  ? 34.890 17.129 55.276 1.00 11.00 ? 237  THR A CB     1 
ATOM   926  O OG1    . THR A 1 54  ? 35.648 16.336 56.181 1.00 10.59 ? 237  THR A OG1    1 
ATOM   927  C CG2    . THR A 1 54  ? 34.366 16.248 54.150 1.00 12.77 ? 237  THR A CG2    1 
ATOM   928  H H      . THR A 1 54  ? 37.502 17.278 54.522 1.00 11.08 ? 237  THR A H      1 
ATOM   929  H HA     . THR A 1 54  ? 35.258 18.749 54.101 1.00 11.89 ? 237  THR A HA     1 
ATOM   930  H HB     . THR A 1 54  ? 34.125 17.518 55.728 1.00 13.20 ? 237  THR A HB     1 
ATOM   931  H HG1    . THR A 1 54  ? 35.137 15.959 56.731 1.00 12.71 ? 237  THR A HG1    1 
ATOM   932  H HG21   . THR A 1 54  ? 33.751 15.587 54.505 1.00 15.33 ? 237  THR A HG21   1 
ATOM   933  H HG22   . THR A 1 54  ? 33.902 16.790 53.493 1.00 15.33 ? 237  THR A HG22   1 
ATOM   934  H HG23   . THR A 1 54  ? 35.104 15.791 53.716 1.00 15.33 ? 237  THR A HG23   1 
ATOM   935  N N      . CYS A 1 55  ? 35.216 19.999 56.234 1.00 10.26 ? 238  CYS A N      1 
ATOM   936  C CA     . CYS A 1 55  ? 35.426 21.152 57.087 1.00 11.48 ? 238  CYS A CA     1 
ATOM   937  C C      . CYS A 1 55  ? 34.147 21.419 57.885 1.00 11.81 ? 238  CYS A C      1 
ATOM   938  O O      . CYS A 1 55  ? 33.166 20.688 57.774 1.00 12.99 ? 238  CYS A O      1 
ATOM   939  C CB     . CYS A 1 55  ? 35.815 22.377 56.224 1.00 11.41 ? 238  CYS A CB     1 
ATOM   940  S SG     . CYS A 1 55  ? 34.488 22.983 55.152 1.00 13.40 ? 238  CYS A SG     1 
ATOM   941  H H      . CYS A 1 55  ? 34.388 19.864 56.043 1.00 12.31 ? 238  CYS A H      1 
ATOM   942  H HA     . CYS A 1 55  ? 36.135 20.961 57.722 1.00 13.78 ? 238  CYS A HA     1 
ATOM   943  H HB2    . CYS A 1 55  ? 36.072 23.103 56.814 1.00 13.69 ? 238  CYS A HB2    1 
ATOM   944  H HB3    . CYS A 1 55  ? 36.563 22.131 55.657 1.00 13.69 ? 238  CYS A HB3    1 
ATOM   945  H HG     . CYS A 1 55  ? 34.863 23.973 54.587 1.00 16.08 ? 238  CYS A HG     1 
ATOM   946  N N      . ASP A 1 56  ? 34.165 22.489 58.701 1.00 11.37 ? 239  ASP A N      1 
ATOM   947  C CA     . ASP A 1 56  ? 32.994 22.925 59.464 1.00 11.93 ? 239  ASP A CA     1 
ATOM   948  C C      . ASP A 1 56  ? 32.241 24.051 58.772 1.00 11.03 ? 239  ASP A C      1 
ATOM   949  O O      . ASP A 1 56  ? 31.018 24.047 58.743 1.00 11.84 ? 239  ASP A O      1 
ATOM   950  C CB     . ASP A 1 56  ? 33.406 23.385 60.868 1.00 12.52 ? 239  ASP A CB     1 
ATOM   951  C CG     . ASP A 1 56  ? 34.110 22.289 61.627 1.00 12.91 ? 239  ASP A CG     1 
ATOM   952  O OD1    . ASP A 1 56  ? 33.467 21.246 61.827 1.00 13.17 ? 239  ASP A OD1    1 
ATOM   953  O OD2    . ASP A 1 56  ? 35.286 22.449 61.958 1.00 14.00 ? 239  ASP A OD2    1 
ATOM   954  H H      . ASP A 1 56  ? 34.858 22.982 58.826 1.00 13.64 ? 239  ASP A H      1 
ATOM   955  H HA     . ASP A 1 56  ? 32.392 22.172 59.570 1.00 14.32 ? 239  ASP A HA     1 
ATOM   956  H HB2    . ASP A 1 56  ? 34.010 24.140 60.793 1.00 15.03 ? 239  ASP A HB2    1 
ATOM   957  H HB3    . ASP A 1 56  ? 32.615 23.641 61.367 1.00 15.03 ? 239  ASP A HB3    1 
ATOM   958  N N      . PHE A 1 57  ? 32.983 25.004 58.217 1.00 10.81 ? 240  PHE A N      1 
ATOM   959  C CA     . PHE A 1 57  ? 32.442 26.224 57.629 1.00 10.49 ? 240  PHE A CA     1 
ATOM   960  C C      . PHE A 1 57  ? 33.008 26.322 56.230 1.00 10.21 ? 240  PHE A C      1 
ATOM   961  O O      . PHE A 1 57  ? 34.242 26.359 56.046 1.00 11.85 ? 240  PHE A O      1 
ATOM   962  C CB     . PHE A 1 57  ? 32.908 27.444 58.438 1.00 11.49 ? 240  PHE A CB     1 
ATOM   963  C CG     . PHE A 1 57  ? 32.866 27.232 59.919 1.00 12.15 ? 240  PHE A CG     1 
ATOM   964  C CD1    . PHE A 1 57  ? 31.670 27.049 60.607 1.00 13.95 ? 240  PHE A CD1    1 
ATOM   965  C CD2    . PHE A 1 57  ? 34.057 27.163 60.647 1.00 11.75 ? 240  PHE A CD2    1 
ATOM   966  C CE1    . PHE A 1 57  ? 31.647 26.786 61.969 1.00 15.44 ? 240  PHE A CE1    1 
ATOM   967  C CE2    . PHE A 1 57  ? 34.022 26.907 62.030 1.00 12.83 ? 240  PHE A CE2    1 
ATOM   968  C CZ     . PHE A 1 57  ? 32.824 26.738 62.673 1.00 13.57 ? 240  PHE A CZ     1 
ATOM   969  H H      . PHE A 1 57  ? 33.840 24.964 58.167 1.00 12.97 ? 240  PHE A H      1 
ATOM   970  H HA     . PHE A 1 57  ? 31.473 26.198 57.603 1.00 12.59 ? 240  PHE A HA     1 
ATOM   971  H HB2    . PHE A 1 57  ? 33.824 27.649 58.193 1.00 13.79 ? 240  PHE A HB2    1 
ATOM   972  H HB3    . PHE A 1 57  ? 32.333 28.196 58.229 1.00 13.79 ? 240  PHE A HB3    1 
ATOM   973  H HD1    . PHE A 1 57  ? 30.866 27.104 60.143 1.00 16.74 ? 240  PHE A HD1    1 
ATOM   974  H HD2    . PHE A 1 57  ? 34.873 27.287 60.217 1.00 14.10 ? 240  PHE A HD2    1 
ATOM   975  H HE1    . PHE A 1 57  ? 30.837 26.642 62.403 1.00 18.52 ? 240  PHE A HE1    1 
ATOM   976  H HE2    . PHE A 1 57  ? 34.816 26.851 62.510 1.00 15.40 ? 240  PHE A HE2    1 
ATOM   977  H HZ     . PHE A 1 57  ? 32.809 26.591 63.591 1.00 16.29 ? 240  PHE A HZ     1 
ATOM   978  N N      . LEU A 1 58  ? 32.144 26.367 55.225 1.00 10.37 ? 241  LEU A N      1 
ATOM   979  C CA     . LEU A 1 58  ? 32.591 26.319 53.851 1.00 9.68  ? 241  LEU A CA     1 
ATOM   980  C C      . LEU A 1 58  ? 32.371 27.648 53.141 1.00 10.30 ? 241  LEU A C      1 
ATOM   981  O O      . LEU A 1 58  ? 31.252 28.191 53.140 1.00 11.74 ? 241  LEU A O      1 
ATOM   982  C CB     . LEU A 1 58  ? 31.843 25.234 53.051 1.00 11.42 ? 241  LEU A CB     1 
ATOM   983  C CG     . LEU A 1 58  ? 32.305 25.044 51.631 1.00 11.65 ? 241  LEU A CG     1 
ATOM   984  C CD1    . LEU A 1 58  ? 33.668 24.346 51.581 1.00 13.76 ? 241  LEU A CD1    1 
ATOM   985  C CD2    . LEU A 1 58  ? 31.271 24.237 50.845 1.00 12.33 ? 241  LEU A CD2    1 
ATOM   986  H H      . LEU A 1 58  ? 31.291 26.426 55.320 1.00 12.44 ? 241  LEU A H      1 
ATOM   987  H HA     . LEU A 1 58  ? 33.542 26.130 53.872 1.00 11.61 ? 241  LEU A HA     1 
ATOM   988  H HB2    . LEU A 1 58  ? 31.956 24.386 53.509 1.00 13.71 ? 241  LEU A HB2    1 
ATOM   989  H HB3    . LEU A 1 58  ? 30.903 25.471 53.021 1.00 13.71 ? 241  LEU A HB3    1 
ATOM   990  H HG     . LEU A 1 58  ? 32.403 25.916 51.217 1.00 13.98 ? 241  LEU A HG     1 
ATOM   991  H HD11   . LEU A 1 58  ? 33.951 24.271 50.656 1.00 16.51 ? 241  LEU A HD11   1 
ATOM   992  H HD12   . LEU A 1 58  ? 34.310 24.871 52.083 1.00 16.51 ? 241  LEU A HD12   1 
ATOM   993  H HD13   . LEU A 1 58  ? 33.584 23.462 51.974 1.00 16.51 ? 241  LEU A HD13   1 
ATOM   994  H HD21   . LEU A 1 58  ? 31.591 24.114 49.937 1.00 14.79 ? 241  LEU A HD21   1 
ATOM   995  H HD22   . LEU A 1 58  ? 31.151 23.376 51.273 1.00 14.79 ? 241  LEU A HD22   1 
ATOM   996  H HD23   . LEU A 1 58  ? 30.432 24.723 50.837 1.00 14.79 ? 241  LEU A HD23   1 
ATOM   997  N N      . ILE A 1 59  ? 33.423 28.179 52.558 1.00 10.12 ? 242  ILE A N      1 
ATOM   998  C CA     . ILE A 1 59  ? 33.339 29.315 51.631 1.00 10.28 ? 242  ILE A CA     1 
ATOM   999  C C      . ILE A 1 59  ? 33.465 28.749 50.218 1.00 10.18 ? 242  ILE A C      1 
ATOM   1000 O O      . ILE A 1 59  ? 34.468 28.096 49.897 1.00 11.26 ? 242  ILE A O      1 
ATOM   1001 C CB     . ILE A 1 59  ? 34.479 30.318 51.913 1.00 11.19 ? 242  ILE A CB     1 
ATOM   1002 C CG1    . ILE A 1 59  ? 34.403 30.845 53.350 1.00 12.42 ? 242  ILE A CG1    1 
ATOM   1003 C CG2    . ILE A 1 59  ? 34.474 31.409 50.853 1.00 12.72 ? 242  ILE A CG2    1 
ATOM   1004 C CD1    . ILE A 1 59  ? 35.554 31.758 53.766 1.00 14.08 ? 242  ILE A CD1    1 
ATOM   1005 H H      . ILE A 1 59  ? 34.227 27.898 52.678 1.00 12.15 ? 242  ILE A H      1 
ATOM   1006 H HA     . ILE A 1 59  ? 32.486 29.767 51.721 1.00 12.33 ? 242  ILE A HA     1 
ATOM   1007 H HB     . ILE A 1 59  ? 35.336 29.868 51.849 1.00 13.43 ? 242  ILE A HB     1 
ATOM   1008 H HG12   . ILE A 1 59  ? 33.581 31.351 53.447 1.00 14.91 ? 242  ILE A HG12   1 
ATOM   1009 H HG13   . ILE A 1 59  ? 34.399 30.087 53.955 1.00 14.91 ? 242  ILE A HG13   1 
ATOM   1010 H HG21   . ILE A 1 59  ? 35.131 32.082 51.089 1.00 15.27 ? 242  ILE A HG21   1 
ATOM   1011 H HG22   . ILE A 1 59  ? 34.697 31.017 49.994 1.00 15.27 ? 242  ILE A HG22   1 
ATOM   1012 H HG23   . ILE A 1 59  ? 33.591 31.808 50.815 1.00 15.27 ? 242  ILE A HG23   1 
ATOM   1013 H HD11   . ILE A 1 59  ? 35.412 32.049 54.681 1.00 16.90 ? 242  ILE A HD11   1 
ATOM   1014 H HD12   . ILE A 1 59  ? 36.387 31.265 53.702 1.00 16.90 ? 242  ILE A HD12   1 
ATOM   1015 H HD13   . ILE A 1 59  ? 35.578 32.526 53.175 1.00 16.90 ? 242  ILE A HD13   1 
ATOM   1016 N N      . SER A 1 60  ? 32.445 28.901 49.382 1.00 9.91  ? 243  SER A N      1 
ATOM   1017 C CA     . SER A 1 60  ? 32.451 28.278 48.059 1.00 9.54  ? 243  SER A CA     1 
ATOM   1018 C C      . SER A 1 60  ? 31.639 29.134 47.095 1.00 7.90  ? 243  SER A C      1 
ATOM   1019 O O      . SER A 1 60  ? 30.548 29.615 47.433 1.00 11.24 ? 243  SER A O      1 
ATOM   1020 C CB     . SER A 1 60  ? 31.876 26.849 48.125 1.00 10.06 ? 243  SER A CB     1 
ATOM   1021 O OG     . SER A 1 60  ? 31.924 26.204 46.879 1.00 10.76 ? 243  SER A OG     1 
ATOM   1022 H H      . SER A 1 60  ? 31.738 29.359 49.555 1.00 11.89 ? 243  SER A H      1 
ATOM   1023 H HA     . SER A 1 60  ? 33.359 28.233 47.721 1.00 11.45 ? 243  SER A HA     1 
ATOM   1024 H HB2    . SER A 1 60  ? 32.396 26.334 48.762 1.00 12.08 ? 243  SER A HB2    1 
ATOM   1025 H HB3    . SER A 1 60  ? 30.952 26.899 48.415 1.00 12.08 ? 243  SER A HB3    1 
ATOM   1026 H HG     . SER A 1 60  ? 32.721 26.126 46.627 1.00 12.92 ? 243  SER A HG     1 
ATOM   1027 N N      . PHE A 1 61  ? 32.166 29.303 45.910 1.00 7.44  ? 244  PHE A N      1 
ATOM   1028 C CA     . PHE A 1 61  ? 31.514 30.151 44.906 1.00 9.37  ? 244  PHE A CA     1 
ATOM   1029 C C      . PHE A 1 61  ? 32.047 29.864 43.520 1.00 10.99 ? 244  PHE A C      1 
ATOM   1030 O O      . PHE A 1 61  ? 33.180 29.414 43.335 1.00 10.76 ? 244  PHE A O      1 
ATOM   1031 C CB     . PHE A 1 61  ? 31.663 31.652 45.252 1.00 9.81  ? 244  PHE A CB     1 
ATOM   1032 C CG     . PHE A 1 61  ? 33.101 32.102 45.397 1.00 10.31 ? 244  PHE A CG     1 
ATOM   1033 C CD1    . PHE A 1 61  ? 33.733 31.955 46.632 1.00 11.69 ? 244  PHE A CD1    1 
ATOM   1034 C CD2    . PHE A 1 61  ? 33.826 32.573 44.325 1.00 11.77 ? 244  PHE A CD2    1 
ATOM   1035 C CE1    . PHE A 1 61  ? 35.070 32.312 46.802 1.00 13.29 ? 244  PHE A CE1    1 
ATOM   1036 C CE2    . PHE A 1 61  ? 35.171 32.932 44.500 1.00 13.56 ? 244  PHE A CE2    1 
ATOM   1037 C CZ     . PHE A 1 61  ? 35.778 32.773 45.743 1.00 13.90 ? 244  PHE A CZ     1 
ATOM   1038 H H      . PHE A 1 61  ? 32.901 28.942 45.647 1.00 8.93  ? 244  PHE A H      1 
ATOM   1039 H HA     . PHE A 1 61  ? 30.571 29.925 44.887 1.00 11.25 ? 244  PHE A HA     1 
ATOM   1040 H HB2    . PHE A 1 61  ? 31.258 32.178 44.544 1.00 11.78 ? 244  PHE A HB2    1 
ATOM   1041 H HB3    . PHE A 1 61  ? 31.211 31.825 46.093 1.00 11.78 ? 244  PHE A HB3    1 
ATOM   1042 H HD1    . PHE A 1 61  ? 33.255 31.614 47.353 1.00 14.03 ? 244  PHE A HD1    1 
ATOM   1043 H HD2    . PHE A 1 61  ? 33.426 32.653 43.490 1.00 14.13 ? 244  PHE A HD2    1 
ATOM   1044 H HE1    . PHE A 1 61  ? 35.473 32.234 47.637 1.00 15.95 ? 244  PHE A HE1    1 
ATOM   1045 H HE2    . PHE A 1 61  ? 35.657 33.277 43.786 1.00 16.27 ? 244  PHE A HE2    1 
ATOM   1046 H HZ     . PHE A 1 61  ? 36.677 32.986 45.847 1.00 16.68 ? 244  PHE A HZ     1 
ATOM   1047 N N      . PHE A 1 62  ? 31.180 30.133 42.529 1.00 12.06 ? 245  PHE A N      1 
ATOM   1048 C CA     . PHE A 1 62  ? 31.503 29.953 41.141 1.00 12.44 ? 245  PHE A CA     1 
ATOM   1049 C C      . PHE A 1 62  ? 32.414 31.041 40.597 1.00 13.49 ? 245  PHE A C      1 
ATOM   1050 O O      . PHE A 1 62  ? 32.277 32.225 40.931 1.00 16.10 ? 245  PHE A O      1 
ATOM   1051 C CB     . PHE A 1 62  ? 30.197 29.948 40.316 1.00 14.30 ? 245  PHE A CB     1 
ATOM   1052 C CG     . PHE A 1 62  ? 30.425 29.831 38.852 1.00 13.57 ? 245  PHE A CG     1 
ATOM   1053 C CD1    . PHE A 1 62  ? 30.640 28.582 38.266 1.00 13.26 ? 245  PHE A CD1    1 
ATOM   1054 C CD2    . PHE A 1 62  ? 30.473 30.963 38.041 1.00 15.88 ? 245  PHE A CD2    1 
ATOM   1055 C CE1    . PHE A 1 62  ? 30.900 28.472 36.937 1.00 16.25 ? 245  PHE A CE1    1 
ATOM   1056 C CE2    . PHE A 1 62  ? 30.769 30.845 36.698 1.00 17.34 ? 245  PHE A CE2    1 
ATOM   1057 C CZ     . PHE A 1 62  ? 30.954 29.603 36.147 1.00 17.65 ? 245  PHE A CZ     1 
ATOM   1058 H H      . PHE A 1 62  ? 30.382 30.428 42.657 1.00 14.48 ? 245  PHE A H      1 
ATOM   1059 H HA     . PHE A 1 62  ? 31.976 29.111 41.048 1.00 14.93 ? 245  PHE A HA     1 
ATOM   1060 H HB2    . PHE A 1 62  ? 29.654 29.194 40.594 1.00 17.16 ? 245  PHE A HB2    1 
ATOM   1061 H HB3    . PHE A 1 62  ? 29.722 30.778 40.477 1.00 17.16 ? 245  PHE A HB3    1 
ATOM   1062 H HD1    . PHE A 1 62  ? 30.605 27.816 38.792 1.00 15.91 ? 245  PHE A HD1    1 
ATOM   1063 H HD2    . PHE A 1 62  ? 30.305 31.802 38.406 1.00 19.05 ? 245  PHE A HD2    1 
ATOM   1064 H HE1    . PHE A 1 62  ? 31.042 27.634 36.559 1.00 19.50 ? 245  PHE A HE1    1 
ATOM   1065 H HE2    . PHE A 1 62  ? 30.842 31.606 36.169 1.00 20.81 ? 245  PHE A HE2    1 
ATOM   1066 H HZ     . PHE A 1 62  ? 31.118 29.523 35.235 1.00 21.18 ? 245  PHE A HZ     1 
ATOM   1067 N N      . SER A 1 63  ? 33.337 30.619 39.748 1.00 13.52 ? 246  SER A N      1 
ATOM   1068 C CA     . SER A 1 63  ? 34.080 31.443 38.810 1.00 14.39 ? 246  SER A CA     1 
ATOM   1069 C C      . SER A 1 63  ? 34.322 30.535 37.614 1.00 14.61 ? 246  SER A C      1 
ATOM   1070 O O      . SER A 1 63  ? 34.090 29.323 37.703 1.00 14.60 ? 246  SER A O      1 
ATOM   1071 C CB     . SER A 1 63  ? 35.379 31.987 39.396 1.00 16.26 ? 246  SER A CB     1 
ATOM   1072 O OG     . SER A 1 63  ? 36.231 30.967 39.825 1.00 16.79 ? 246  SER A OG     1 
ATOM   1073 H H      . SER A 1 63  ? 33.570 29.793 39.692 1.00 16.22 ? 246  SER A H      1 
ATOM   1074 H HA     . SER A 1 63  ? 33.576 32.230 38.549 1.00 17.27 ? 246  SER A HA     1 
ATOM   1075 H HB2    . SER A 1 63  ? 35.835 32.505 38.715 1.00 19.51 ? 246  SER A HB2    1 
ATOM   1076 H HB3    . SER A 1 63  ? 35.165 32.552 40.155 1.00 19.51 ? 246  SER A HB3    1 
ATOM   1077 H HG     . SER A 1 63  ? 36.412 30.455 39.184 1.00 20.14 ? 246  SER A HG     1 
ATOM   1078 N N      . SER A 1 64  ? 34.860 31.091 36.534 1.00 16.64 ? 247  SER A N      1 
ATOM   1079 C CA     . SER A 1 64  ? 35.067 30.351 35.289 1.00 18.36 ? 247  SER A CA     1 
ATOM   1080 C C      . SER A 1 64  ? 35.801 29.043 35.555 1.00 16.39 ? 247  SER A C      1 
ATOM   1081 O O      . SER A 1 64  ? 36.856 29.022 36.196 1.00 17.17 ? 247  SER A O      1 
ATOM   1082 C CB     . SER A 1 64  ? 35.878 31.222 34.324 1.00 23.96 ? 247  SER A CB     1 
ATOM   1083 O OG     . SER A 1 64  ? 36.243 30.502 33.177 1.00 30.03 ? 247  SER A OG     1 
ATOM   1084 H H      . SER A 1 64  ? 35.120 31.910 36.493 1.00 19.97 ? 247  SER A H      1 
ATOM   1085 H HA     . SER A 1 64  ? 34.211 30.138 34.886 1.00 22.03 ? 247  SER A HA     1 
ATOM   1086 H HB2    . SER A 1 64  ? 35.338 31.983 34.059 1.00 28.76 ? 247  SER A HB2    1 
ATOM   1087 H HB3    . SER A 1 64  ? 36.681 31.525 34.775 1.00 28.76 ? 247  SER A HB3    1 
ATOM   1088 H HG     . SER A 1 64  ? 36.656 31.003 32.643 1.00 36.04 ? 247  SER A HG     1 
ATOM   1089 N N      . GLY A 1 65  ? 35.231 27.937 35.063 1.00 16.54 ? 248  GLY A N      1 
ATOM   1090 C CA     . GLY A 1 65  ? 35.844 26.643 35.220 1.00 16.45 ? 248  GLY A CA     1 
ATOM   1091 C C      . GLY A 1 65  ? 35.401 25.852 36.422 1.00 14.37 ? 248  GLY A C      1 
ATOM   1092 O O      . GLY A 1 65  ? 35.712 24.651 36.503 1.00 14.82 ? 248  GLY A O      1 
ATOM   1093 H H      . GLY A 1 65  ? 34.485 27.925 34.635 1.00 19.84 ? 248  GLY A H      1 
ATOM   1094 H HA2    . GLY A 1 65  ? 35.648 26.112 34.432 1.00 19.74 ? 248  GLY A HA2    1 
ATOM   1095 H HA3    . GLY A 1 65  ? 36.804 26.764 35.287 1.00 19.74 ? 248  GLY A HA3    1 
ATOM   1096 N N      . PHE A 1 66  ? 34.663 26.445 37.339 1.00 12.60 ? 249  PHE A N      1 
ATOM   1097 C CA     . PHE A 1 66  ? 34.253 25.790 38.593 1.00 11.12 ? 249  PHE A CA     1 
ATOM   1098 C C      . PHE A 1 66  ? 33.086 24.851 38.327 1.00 11.57 ? 249  PHE A C      1 
ATOM   1099 O O      . PHE A 1 66  ? 32.088 25.274 37.731 1.00 12.18 ? 249  PHE A O      1 
ATOM   1100 C CB     . PHE A 1 66  ? 33.846 26.822 39.622 1.00 11.09 ? 249  PHE A CB     1 
ATOM   1101 C CG     . PHE A 1 66  ? 33.505 26.287 40.980 1.00 10.00 ? 249  PHE A CG     1 
ATOM   1102 C CD1    . PHE A 1 66  ? 34.512 25.787 41.811 1.00 9.70  ? 249  PHE A CD1    1 
ATOM   1103 C CD2    . PHE A 1 66  ? 32.214 26.233 41.440 1.00 9.97  ? 249  PHE A CD2    1 
ATOM   1104 C CE1    . PHE A 1 66  ? 34.185 25.344 43.095 1.00 8.98  ? 249  PHE A CE1    1 
ATOM   1105 C CE2    . PHE A 1 66  ? 31.910 25.812 42.709 1.00 10.03 ? 249  PHE A CE2    1 
ATOM   1106 C CZ     . PHE A 1 66  ? 32.928 25.354 43.561 1.00 10.23 ? 249  PHE A CZ     1 
ATOM   1107 H H      . PHE A 1 66  ? 34.371 27.251 37.269 1.00 15.12 ? 249  PHE A H      1 
ATOM   1108 H HA     . PHE A 1 66  ? 34.996 25.277 38.948 1.00 13.35 ? 249  PHE A HA     1 
ATOM   1109 H HB2    . PHE A 1 66  ? 34.581 27.445 39.735 1.00 13.31 ? 249  PHE A HB2    1 
ATOM   1110 H HB3    . PHE A 1 66  ? 33.063 27.289 39.291 1.00 13.31 ? 249  PHE A HB3    1 
ATOM   1111 H HD1    . PHE A 1 66  ? 35.391 25.750 41.512 1.00 11.64 ? 249  PHE A HD1    1 
ATOM   1112 H HD2    . PHE A 1 66  ? 31.523 26.490 40.874 1.00 11.96 ? 249  PHE A HD2    1 
ATOM   1113 H HE1    . PHE A 1 66  ? 34.864 25.030 43.647 1.00 10.77 ? 249  PHE A HE1    1 
ATOM   1114 H HE2    . PHE A 1 66  ? 31.029 25.829 43.006 1.00 12.04 ? 249  PHE A HE2    1 
ATOM   1115 H HZ     . PHE A 1 66  ? 32.736 25.067 44.425 1.00 12.28 ? 249  PHE A HZ     1 
ATOM   1116 N N      . PRO A 1 67  ? 33.150 23.601 38.793 1.00 10.92 ? 250  PRO A N      1 
ATOM   1117 C CA     . PRO A 1 67  ? 32.069 22.642 38.525 1.00 11.50 ? 250  PRO A CA     1 
ATOM   1118 C C      . PRO A 1 67  ? 30.985 22.807 39.586 1.00 11.41 ? 250  PRO A C      1 
ATOM   1119 O O      . PRO A 1 67  ? 30.949 22.126 40.601 1.00 11.90 ? 250  PRO A O      1 
ATOM   1120 C CB     . PRO A 1 67  ? 32.783 21.293 38.618 1.00 11.97 ? 250  PRO A CB     1 
ATOM   1121 C CG     . PRO A 1 67  ? 33.881 21.538 39.654 1.00 11.83 ? 250  PRO A CG     1 
ATOM   1122 C CD     . PRO A 1 67  ? 34.346 22.942 39.371 1.00 10.77 ? 250  PRO A CD     1 
ATOM   1123 H HA     . PRO A 1 67  ? 31.703 22.716 37.630 1.00 13.80 ? 250  PRO A HA     1 
ATOM   1124 H HB2    . PRO A 1 67  ? 32.166 20.606 38.914 1.00 14.37 ? 250  PRO A HB2    1 
ATOM   1125 H HB3    . PRO A 1 67  ? 33.159 21.053 37.757 1.00 14.37 ? 250  PRO A HB3    1 
ATOM   1126 H HG2    . PRO A 1 67  ? 33.518 21.464 40.550 1.00 14.20 ? 250  PRO A HG2    1 
ATOM   1127 H HG3    . PRO A 1 67  ? 34.602 20.900 39.534 1.00 14.20 ? 250  PRO A HG3    1 
ATOM   1128 H HD2    . PRO A 1 67  ? 34.620 23.385 40.189 1.00 12.93 ? 250  PRO A HD2    1 
ATOM   1129 H HD3    . PRO A 1 67  ? 35.078 22.940 38.734 1.00 12.93 ? 250  PRO A HD3    1 
ATOM   1130 N N      . LEU A 1 68  ? 30.098 23.799 39.333 1.00 11.68 ? 251  LEU A N      1 
ATOM   1131 C CA     . LEU A 1 68  ? 29.132 24.191 40.346 1.00 11.61 ? 251  LEU A CA     1 
ATOM   1132 C C      . LEU A 1 68  ? 28.208 23.035 40.749 1.00 10.75 ? 251  LEU A C      1 
ATOM   1133 O O      . LEU A 1 68  ? 27.907 22.862 41.924 1.00 11.07 ? 251  LEU A O      1 
ATOM   1134 C CB     . LEU A 1 68  ? 28.344 25.413 39.852 1.00 12.15 ? 251  LEU A CB     1 
ATOM   1135 C CG     . LEU A 1 68  ? 27.323 25.983 40.823 1.00 13.09 ? 251  LEU A CG     1 
ATOM   1136 C CD1    . LEU A 1 68  ? 27.920 26.394 42.136 1.00 14.14 ? 251  LEU A CD1    1 
ATOM   1137 C CD2    . LEU A 1 68  ? 26.626 27.202 40.206 1.00 15.66 ? 251  LEU A CD2    1 
ATOM   1138 H H      . LEU A 1 68  ? 30.048 24.241 38.597 1.00 14.02 ? 251  LEU A H      1 
ATOM   1139 H HA     . LEU A 1 68  ? 29.606 24.449 41.152 1.00 13.93 ? 251  LEU A HA     1 
ATOM   1140 H HB2    . LEU A 1 68  ? 28.976 26.120 39.652 1.00 14.58 ? 251  LEU A HB2    1 
ATOM   1141 H HB3    . LEU A 1 68  ? 27.865 25.159 39.048 1.00 14.58 ? 251  LEU A HB3    1 
ATOM   1142 H HG     . LEU A 1 68  ? 26.684 25.275 41.000 1.00 15.71 ? 251  LEU A HG     1 
ATOM   1143 H HD11   . LEU A 1 68  ? 27.221 26.761 42.700 1.00 16.97 ? 251  LEU A HD11   1 
ATOM   1144 H HD12   . LEU A 1 68  ? 28.313 25.616 42.561 1.00 16.97 ? 251  LEU A HD12   1 
ATOM   1145 H HD13   . LEU A 1 68  ? 28.603 27.064 41.976 1.00 16.97 ? 251  LEU A HD13   1 
ATOM   1146 H HD21   . LEU A 1 68  ? 25.979 27.551 40.839 1.00 18.79 ? 251  LEU A HD21   1 
ATOM   1147 H HD22   . LEU A 1 68  ? 27.292 27.879 40.007 1.00 18.79 ? 251  LEU A HD22   1 
ATOM   1148 H HD23   . LEU A 1 68  ? 26.177 26.930 39.390 1.00 18.79 ? 251  LEU A HD23   1 
ATOM   1149 N N      . ASP A 1 69  ? 27.698 22.284 39.775 1.00 11.77 ? 252  ASP A N      1 
ATOM   1150 C CA     . ASP A 1 69  ? 26.791 21.185 40.101 1.00 12.98 ? 252  ASP A CA     1 
ATOM   1151 C C      . ASP A 1 69  ? 27.477 20.150 40.981 1.00 12.18 ? 252  ASP A C      1 
ATOM   1152 O O      . ASP A 1 69  ? 26.866 19.583 41.894 1.00 12.95 ? 252  ASP A O      1 
ATOM   1153 C CB     . ASP A 1 69  ? 26.284 20.497 38.828 1.00 15.24 ? 252  ASP A CB     1 
ATOM   1154 C CG     . ASP A 1 69  ? 25.291 21.320 38.071 1.00 18.99 ? 252  ASP A CG     1 
ATOM   1155 O OD1    . ASP A 1 69  ? 24.843 22.366 38.558 1.00 20.72 ? 252  ASP A OD1    1 
ATOM   1156 O OD2    . ASP A 1 69  ? 24.939 20.901 36.957 1.00 22.61 ? 252  ASP A OD2    1 
ATOM   1157 H H      . ASP A 1 69  ? 27.856 22.387 38.936 1.00 14.13 ? 252  ASP A H      1 
ATOM   1158 H HA     . ASP A 1 69  ? 26.031 21.560 40.573 1.00 15.58 ? 252  ASP A HA     1 
ATOM   1159 H HB2    . ASP A 1 69  ? 27.037 20.325 38.242 1.00 18.29 ? 252  ASP A HB2    1 
ATOM   1160 H HB3    . ASP A 1 69  ? 25.855 19.662 39.072 1.00 18.29 ? 252  ASP A HB3    1 
ATOM   1161 N N      . LYS A 1 70  ? 28.756 19.904 40.723 1.00 13.05 ? 253  LYS A N      1 
ATOM   1162 C CA     . LYS A 1 70  ? 29.517 18.971 41.539 1.00 12.69 ? 253  LYS A CA     1 
ATOM   1163 C C      . LYS A 1 70  ? 29.672 19.498 42.965 1.00 11.58 ? 253  LYS A C      1 
ATOM   1164 O O      . LYS A 1 70  ? 29.446 18.774 43.930 1.00 12.29 ? 253  LYS A O      1 
ATOM   1165 C CB     . LYS A 1 70  ? 30.855 18.744 40.838 1.00 14.98 ? 253  LYS A CB     1 
ATOM   1166 C CG     . LYS A 1 70  ? 31.753 17.727 41.410 1.00 13.94 ? 253  LYS A CG     1 
ATOM   1167 C CD     . LYS A 1 70  ? 32.987 17.573 40.561 1.00 13.95 ? 253  LYS A CD     1 
ATOM   1168 C CE     . LYS A 1 70  ? 33.864 16.549 41.204 1.00 11.84 ? 253  LYS A CE     1 
ATOM   1169 N NZ     . LYS A 1 70  ? 35.145 16.448 40.537 1.00 11.94 ? 253  LYS A NZ     1 
ATOM   1170 H H      . LYS A 1 70  ? 29.205 20.262 40.083 1.00 15.66 ? 253  LYS A H      1 
ATOM   1171 H HA     . LYS A 1 70  ? 29.068 18.115 41.623 1.00 15.23 ? 253  LYS A HA     1 
ATOM   1172 H HB2    . LYS A 1 70  ? 30.671 18.474 39.925 1.00 17.98 ? 253  LYS A HB2    1 
ATOM   1173 H HB3    . LYS A 1 70  ? 31.341 19.584 40.845 1.00 17.98 ? 253  LYS A HB3    1 
ATOM   1174 H HG2    . LYS A 1 70  ? 32.024 17.997 42.301 1.00 16.73 ? 253  LYS A HG2    1 
ATOM   1175 H HG3    . LYS A 1 70  ? 31.295 16.873 41.446 1.00 16.73 ? 253  LYS A HG3    1 
ATOM   1176 H HD2    . LYS A 1 70  ? 32.745 17.273 39.671 1.00 16.74 ? 253  LYS A HD2    1 
ATOM   1177 H HD3    . LYS A 1 70  ? 33.464 18.416 40.508 1.00 16.74 ? 253  LYS A HD3    1 
ATOM   1178 H HE2    . LYS A 1 70  ? 34.022 16.798 42.129 1.00 14.21 ? 253  LYS A HE2    1 
ATOM   1179 H HE3    . LYS A 1 70  ? 33.430 15.683 41.163 1.00 14.21 ? 253  LYS A HE3    1 
ATOM   1180 H HZ1    . LYS A 1 70  ? 35.668 15.870 40.968 1.00 14.33 ? 253  LYS A HZ1    1 
ATOM   1181 H HZ2    . LYS A 1 70  ? 35.031 16.165 39.701 1.00 14.33 ? 253  LYS A HZ2    1 
ATOM   1182 H HZ3    . LYS A 1 70  ? 35.545 17.243 40.522 1.00 14.33 ? 253  LYS A HZ3    1 
ATOM   1183 N N      . ALA A 1 71  ? 29.959 20.803 43.124 1.00 11.41 ? 254  ALA A N      1 
ATOM   1184 C CA     . ALA A 1 71  ? 30.041 21.384 44.471 1.00 11.05 ? 254  ALA A CA     1 
ATOM   1185 C C      . ALA A 1 71  ? 28.708 21.349 45.217 1.00 9.63  ? 254  ALA A C      1 
ATOM   1186 O O      . ALA A 1 71  ? 28.654 21.143 46.446 1.00 9.92  ? 254  ALA A O      1 
ATOM   1187 C CB     . ALA A 1 71  ? 30.569 22.808 44.384 1.00 11.75 ? 254  ALA A CB     1 
ATOM   1188 H H      . ALA A 1 71  ? 30.107 21.357 42.484 1.00 13.69 ? 254  ALA A H      1 
ATOM   1189 H HA     . ALA A 1 71  ? 30.663 20.850 44.989 1.00 13.26 ? 254  ALA A HA     1 
ATOM   1190 H HB1    . ALA A 1 71  ? 30.604 23.187 45.276 1.00 14.10 ? 254  ALA A HB1    1 
ATOM   1191 H HB2    . ALA A 1 71  ? 31.458 22.792 43.996 1.00 14.10 ? 254  ALA A HB2    1 
ATOM   1192 H HB3    . ALA A 1 71  ? 29.974 23.332 43.825 1.00 14.10 ? 254  ALA A HB3    1 
ATOM   1193 N N      . ILE A 1 72  ? 27.591 21.543 44.488 1.00 10.28 ? 255  ILE A N      1 
ATOM   1194 C CA     . ILE A 1 72  ? 26.275 21.428 45.114 1.00 9.68  ? 255  ILE A CA     1 
ATOM   1195 C C      . ILE A 1 72  ? 26.076 20.018 45.669 1.00 9.59  ? 255  ILE A C      1 
ATOM   1196 O O      . ILE A 1 72  ? 25.551 19.846 46.776 1.00 10.14 ? 255  ILE A O      1 
ATOM   1197 C CB     . ILE A 1 72  ? 25.172 21.836 44.106 1.00 10.17 ? 255  ILE A CB     1 
ATOM   1198 C CG1    . ILE A 1 72  ? 25.262 23.352 43.811 1.00 10.47 ? 255  ILE A CG1    1 
ATOM   1199 C CG2    . ILE A 1 72  ? 23.800 21.415 44.586 1.00 11.27 ? 255  ILE A CG2    1 
ATOM   1200 C CD1    . ILE A 1 72  ? 24.487 23.814 42.571 1.00 11.32 ? 255  ILE A CD1    1 
ATOM   1201 H H      . ILE A 1 72  ? 27.576 21.738 43.651 1.00 12.34 ? 255  ILE A H      1 
ATOM   1202 H HA     . ILE A 1 72  ? 26.223 22.041 45.864 1.00 11.62 ? 255  ILE A HA     1 
ATOM   1203 H HB     . ILE A 1 72  ? 25.322 21.364 43.272 1.00 12.21 ? 255  ILE A HB     1 
ATOM   1204 H HG12   . ILE A 1 72  ? 24.907 23.836 44.573 1.00 12.57 ? 255  ILE A HG12   1 
ATOM   1205 H HG13   . ILE A 1 72  ? 26.194 23.584 43.675 1.00 12.57 ? 255  ILE A HG13   1 
ATOM   1206 H HG21   . ILE A 1 72  ? 23.139 21.687 43.931 1.00 13.52 ? 255  ILE A HG21   1 
ATOM   1207 H HG22   . ILE A 1 72  ? 23.784 20.450 44.690 1.00 13.52 ? 255  ILE A HG22   1 
ATOM   1208 H HG23   . ILE A 1 72  ? 23.618 21.843 45.437 1.00 13.52 ? 255  ILE A HG23   1 
ATOM   1209 H HD11   . ILE A 1 72  ? 24.651 24.760 42.431 1.00 13.58 ? 255  ILE A HD11   1 
ATOM   1210 H HD12   . ILE A 1 72  ? 24.791 23.308 41.802 1.00 13.58 ? 255  ILE A HD12   1 
ATOM   1211 H HD13   . ILE A 1 72  ? 23.540 23.660 42.715 1.00 13.58 ? 255  ILE A HD13   1 
ATOM   1212 N N      . LYS A 1 73  ? 26.459 18.994 44.885 1.00 11.23 ? 256  LYS A N      1 
ATOM   1213 C CA     . LYS A 1 73  ? 26.343 17.615 45.356 1.00 12.43 ? 256  LYS A CA     1 
ATOM   1214 C C      . LYS A 1 73  ? 27.221 17.370 46.594 1.00 10.96 ? 256  LYS A C      1 
ATOM   1215 O O      . LYS A 1 73  ? 26.817 16.684 47.537 1.00 11.11 ? 256  LYS A O      1 
ATOM   1216 C CB     . LYS A 1 73  ? 26.720 16.664 44.221 1.00 14.46 ? 256  LYS A CB     1 
ATOM   1217 C CG     . LYS A 1 73  ? 25.665 16.604 43.144 1.00 18.93 ? 256  LYS A CG     1 
ATOM   1218 C CD     . LYS A 1 73  ? 25.968 15.564 42.098 1.00 23.39 ? 256  LYS A CD     1 
ATOM   1219 C CE     . LYS A 1 73  ? 24.842 15.458 41.044 1.00 26.58 ? 256  LYS A CE     1 
ATOM   1220 N NZ     . LYS A 1 73  ? 24.750 16.697 40.206 1.00 28.73 ? 256  LYS A NZ     1 
ATOM   1221 H H      . LYS A 1 73  ? 26.783 19.075 44.093 1.00 13.48 ? 256  LYS A H      1 
ATOM   1222 H HA     . LYS A 1 73  ? 25.425 17.436 45.613 1.00 14.92 ? 256  LYS A HA     1 
ATOM   1223 H HB2    . LYS A 1 73  ? 27.548 16.967 43.816 1.00 17.35 ? 256  LYS A HB2    1 
ATOM   1224 H HB3    . LYS A 1 73  ? 26.835 15.771 44.581 1.00 17.35 ? 256  LYS A HB3    1 
ATOM   1225 H HG2    . LYS A 1 73  ? 24.811 16.384 43.548 1.00 22.72 ? 256  LYS A HG2    1 
ATOM   1226 H HG3    . LYS A 1 73  ? 25.611 17.467 42.704 1.00 22.72 ? 256  LYS A HG3    1 
ATOM   1227 H HD2    . LYS A 1 73  ? 26.789 15.801 41.640 1.00 28.07 ? 256  LYS A HD2    1 
ATOM   1228 H HD3    . LYS A 1 73  ? 26.064 14.699 42.526 1.00 28.07 ? 256  LYS A HD3    1 
ATOM   1229 H HE2    . LYS A 1 73  ? 25.021 14.707 40.458 1.00 31.89 ? 256  LYS A HE2    1 
ATOM   1230 H HE3    . LYS A 1 73  ? 23.992 15.332 41.495 1.00 31.89 ? 256  LYS A HE3    1 
ATOM   1231 H HZ1    . LYS A 1 73  ? 24.089 16.616 39.616 1.00 34.47 ? 256  LYS A HZ1    1 
ATOM   1232 H HZ2    . LYS A 1 73  ? 24.591 17.403 40.723 1.00 34.47 ? 256  LYS A HZ2    1 
ATOM   1233 H HZ3    . LYS A 1 73  ? 25.514 16.825 39.769 1.00 34.47 ? 256  LYS A HZ3    1 
ATOM   1234 N N      . TYR A 1 74  ? 28.423 17.973 46.627 1.00 10.15 ? 257  TYR A N      1 
ATOM   1235 C CA     . TYR A 1 74  ? 29.290 17.867 47.796 1.00 10.57 ? 257  TYR A CA     1 
ATOM   1236 C C      . TYR A 1 74  ? 28.605 18.445 49.015 1.00 9.81  ? 257  TYR A C      1 
ATOM   1237 O O      . TYR A 1 74  ? 28.649 17.884 50.121 1.00 10.31 ? 257  TYR A O      1 
ATOM   1238 C CB     . TYR A 1 74  ? 30.616 18.578 47.530 1.00 10.13 ? 257  TYR A CB     1 
ATOM   1239 C CG     . TYR A 1 74  ? 31.468 18.816 48.740 1.00 10.17 ? 257  TYR A CG     1 
ATOM   1240 C CD1    . TYR A 1 74  ? 32.253 17.786 49.289 1.00 10.16 ? 257  TYR A CD1    1 
ATOM   1241 C CD2    . TYR A 1 74  ? 31.499 20.053 49.322 1.00 11.42 ? 257  TYR A CD2    1 
ATOM   1242 C CE1    . TYR A 1 74  ? 33.052 18.027 50.372 1.00 10.86 ? 257  TYR A CE1    1 
ATOM   1243 C CE2    . TYR A 1 74  ? 32.310 20.305 50.422 1.00 10.77 ? 257  TYR A CE2    1 
ATOM   1244 C CZ     . TYR A 1 74  ? 33.095 19.278 50.940 1.00 10.79 ? 257  TYR A CZ     1 
ATOM   1245 O OH     . TYR A 1 74  ? 33.867 19.557 52.056 1.00 11.46 ? 257  TYR A OH     1 
ATOM   1246 H H      . TYR A 1 74  ? 28.751 18.444 45.987 1.00 12.18 ? 257  TYR A H      1 
ATOM   1247 H HA     . TYR A 1 74  ? 29.484 16.932 47.968 1.00 12.69 ? 257  TYR A HA     1 
ATOM   1248 H HB2    . TYR A 1 74  ? 31.134 18.039 46.912 1.00 12.16 ? 257  TYR A HB2    1 
ATOM   1249 H HB3    . TYR A 1 74  ? 30.425 19.444 47.136 1.00 12.16 ? 257  TYR A HB3    1 
ATOM   1250 H HD1    . TYR A 1 74  ? 32.229 16.936 48.912 1.00 12.20 ? 257  TYR A HD1    1 
ATOM   1251 H HD2    . TYR A 1 74  ? 30.970 20.735 48.976 1.00 13.71 ? 257  TYR A HD2    1 
ATOM   1252 H HE1    . TYR A 1 74  ? 33.569 17.340 50.727 1.00 13.03 ? 257  TYR A HE1    1 
ATOM   1253 H HE2    . TYR A 1 74  ? 32.329 21.151 50.808 1.00 12.92 ? 257  TYR A HE2    1 
ATOM   1254 H HH     . TYR A 1 74  ? 34.258 18.860 52.316 1.00 13.75 ? 257  TYR A HH     1 
ATOM   1255 N N      . VAL A 1 75  ? 28.027 19.650 48.857 1.00 10.62 ? 258  VAL A N      1 
ATOM   1256 C CA     . VAL A 1 75  ? 27.383 20.253 50.011 1.00 11.23 ? 258  VAL A CA     1 
ATOM   1257 C C      . VAL A 1 75  ? 26.185 19.426 50.481 1.00 11.38 ? 258  VAL A C      1 
ATOM   1258 O O      . VAL A 1 75  ? 25.941 19.289 51.690 1.00 12.69 ? 258  VAL A O      1 
ATOM   1259 C CB     . VAL A 1 75  ? 27.011 21.712 49.691 1.00 12.11 ? 258  VAL A CB     1 
ATOM   1260 C CG1    . VAL A 1 75  ? 26.068 22.274 50.722 1.00 14.36 ? 258  VAL A CG1    1 
ATOM   1261 C CG2    . VAL A 1 75  ? 28.309 22.529 49.558 1.00 12.17 ? 258  VAL A CG2    1 
ATOM   1262 H H      . VAL A 1 75  ? 28.002 20.106 48.129 1.00 12.74 ? 258  VAL A H      1 
ATOM   1263 H HA     . VAL A 1 75  ? 28.012 20.259 50.749 1.00 13.48 ? 258  VAL A HA     1 
ATOM   1264 H HB     . VAL A 1 75  ? 26.532 21.765 48.850 1.00 14.54 ? 258  VAL A HB     1 
ATOM   1265 H HG11   . VAL A 1 75  ? 25.872 23.198 50.500 1.00 17.23 ? 258  VAL A HG11   1 
ATOM   1266 H HG12   . VAL A 1 75  ? 25.250 21.753 50.718 1.00 17.23 ? 258  VAL A HG12   1 
ATOM   1267 H HG13   . VAL A 1 75  ? 26.488 22.224 51.595 1.00 17.23 ? 258  VAL A HG13   1 
ATOM   1268 H HG21   . VAL A 1 75  ? 28.085 23.442 49.320 1.00 14.60 ? 258  VAL A HG21   1 
ATOM   1269 H HG22   . VAL A 1 75  ? 28.780 22.514 50.407 1.00 14.60 ? 258  VAL A HG22   1 
ATOM   1270 H HG23   . VAL A 1 75  ? 28.862 22.133 48.867 1.00 14.60 ? 258  VAL A HG23   1 
ATOM   1271 N N      . LYS A 1 76  ? 25.405 18.871 49.542 1.00 12.12 ? 259  LYS A N      1 
ATOM   1272 C CA     . LYS A 1 76  ? 24.284 18.017 49.922 1.00 14.32 ? 259  LYS A CA     1 
ATOM   1273 C C      . LYS A 1 76  ? 24.770 16.817 50.727 1.00 13.64 ? 259  LYS A C      1 
ATOM   1274 O O      . LYS A 1 76  ? 24.091 16.393 51.680 1.00 15.25 ? 259  LYS A O      1 
ATOM   1275 C CB     . LYS A 1 76  ? 23.538 17.558 48.668 1.00 16.75 ? 259  LYS A CB     1 
ATOM   1276 C CG     . LYS A 1 76  ? 22.415 16.536 48.925 1.00 21.80 ? 259  LYS A CG     1 
ATOM   1277 C CD     . LYS A 1 76  ? 21.815 16.025 47.617 1.00 26.67 ? 259  LYS A CD     1 
ATOM   1278 C CE     . LYS A 1 76  ? 20.997 17.080 46.927 1.00 32.61 ? 259  LYS A CE     1 
ATOM   1279 N NZ     . LYS A 1 76  ? 19.716 17.351 47.671 1.00 36.62 ? 259  LYS A NZ     1 
ATOM   1280 H H      . LYS A 1 76  ? 25.506 18.973 48.694 1.00 14.55 ? 259  LYS A H      1 
ATOM   1281 H HA     . LYS A 1 76  ? 23.665 18.522 50.472 1.00 17.18 ? 259  LYS A HA     1 
ATOM   1282 H HB2    . LYS A 1 76  ? 23.136 18.334 48.247 1.00 20.10 ? 259  LYS A HB2    1 
ATOM   1283 H HB3    . LYS A 1 76  ? 24.176 17.146 48.064 1.00 20.10 ? 259  LYS A HB3    1 
ATOM   1284 H HG2    . LYS A 1 76  ? 22.775 15.778 49.412 1.00 26.17 ? 259  LYS A HG2    1 
ATOM   1285 H HG3    . LYS A 1 76  ? 21.709 16.956 49.441 1.00 26.17 ? 259  LYS A HG3    1 
ATOM   1286 H HD2    . LYS A 1 76  ? 22.530 15.758 47.019 1.00 32.01 ? 259  LYS A HD2    1 
ATOM   1287 H HD3    . LYS A 1 76  ? 21.238 15.268 47.804 1.00 32.01 ? 259  LYS A HD3    1 
ATOM   1288 H HE2    . LYS A 1 76  ? 21.505 17.905 46.883 1.00 39.13 ? 259  LYS A HE2    1 
ATOM   1289 H HE3    . LYS A 1 76  ? 20.773 16.780 46.032 1.00 39.13 ? 259  LYS A HE3    1 
ATOM   1290 H HZ1    . LYS A 1 76  ? 19.247 17.980 47.251 1.00 43.95 ? 259  LYS A HZ1    1 
ATOM   1291 H HZ2    . LYS A 1 76  ? 19.228 16.608 47.716 1.00 43.95 ? 259  LYS A HZ2    1 
ATOM   1292 H HZ3    . LYS A 1 76  ? 19.897 17.628 48.497 1.00 43.95 ? 259  LYS A HZ3    1 
ATOM   1293 N N      . LEU A 1 77  ? 25.907 16.230 50.317 1.00 11.38 ? 260  LEU A N      1 
ATOM   1294 C CA     . LEU A 1 77  ? 26.444 15.054 51.001 1.00 11.51 ? 260  LEU A CA     1 
ATOM   1295 C C      . LEU A 1 77  ? 27.002 15.406 52.369 1.00 11.34 ? 260  LEU A C      1 
ATOM   1296 O O      . LEU A 1 77  ? 26.742 14.721 53.359 1.00 13.52 ? 260  LEU A O      1 
ATOM   1297 C CB     . LEU A 1 77  ? 27.509 14.421 50.123 1.00 13.04 ? 260  LEU A CB     1 
ATOM   1298 C CG     . LEU A 1 77  ? 28.264 13.245 50.759 1.00 15.54 ? 260  LEU A CG     1 
ATOM   1299 C CD1    . LEU A 1 77  ? 27.341 12.009 50.957 1.00 17.36 ? 260  LEU A CD1    1 
ATOM   1300 C CD2    . LEU A 1 77  ? 29.437 12.862 49.868 1.00 16.50 ? 260  LEU A CD2    1 
ATOM   1301 H H      . LEU A 1 77  ? 26.380 16.494 49.650 1.00 13.65 ? 260  LEU A H      1 
ATOM   1302 H HA     . LEU A 1 77  ? 25.732 14.412 51.143 1.00 13.81 ? 260  LEU A HA     1 
ATOM   1303 H HB2    . LEU A 1 77  ? 27.083 14.091 49.317 1.00 15.65 ? 260  LEU A HB2    1 
ATOM   1304 H HB3    . LEU A 1 77  ? 28.164 15.100 49.899 1.00 15.65 ? 260  LEU A HB3    1 
ATOM   1305 H HG     . LEU A 1 77  ? 28.583 13.517 51.634 1.00 18.64 ? 260  LEU A HG     1 
ATOM   1306 H HD11   . LEU A 1 77  ? 27.853 11.294 51.366 1.00 20.83 ? 260  LEU A HD11   1 
ATOM   1307 H HD12   . LEU A 1 77  ? 26.600 12.256 51.533 1.00 20.83 ? 260  LEU A HD12   1 
ATOM   1308 H HD13   . LEU A 1 77  ? 27.006 11.723 50.093 1.00 20.83 ? 260  LEU A HD13   1 
ATOM   1309 H HD21   . LEU A 1 77  ? 29.904 12.110 50.265 1.00 19.80 ? 260  LEU A HD21   1 
ATOM   1310 H HD22   . LEU A 1 77  ? 29.101 12.617 48.991 1.00 19.80 ? 260  LEU A HD22   1 
ATOM   1311 H HD23   . LEU A 1 77  ? 30.037 13.620 49.792 1.00 19.80 ? 260  LEU A HD23   1 
ATOM   1312 N N      . ARG A 1 78  ? 27.820 16.468 52.441 1.00 11.19 ? 261  ARG A N      1 
ATOM   1313 C CA     . ARG A 1 78  ? 28.624 16.728 53.635 1.00 11.64 ? 261  ARG A CA     1 
ATOM   1314 C C      . ARG A 1 78  ? 28.029 17.778 54.567 1.00 11.91 ? 261  ARG A C      1 
ATOM   1315 O O      . ARG A 1 78  ? 28.393 17.824 55.748 1.00 13.55 ? 261  ARG A O      1 
ATOM   1316 C CB     . ARG A 1 78  ? 30.042 17.156 53.247 1.00 12.10 ? 261  ARG A CB     1 
ATOM   1317 C CG     . ARG A 1 78  ? 30.832 16.062 52.508 1.00 11.64 ? 261  ARG A CG     1 
ATOM   1318 C CD     . ARG A 1 78  ? 30.992 14.805 53.342 1.00 12.58 ? 261  ARG A CD     1 
ATOM   1319 N NE     . ARG A 1 78  ? 31.830 13.840 52.665 1.00 11.60 ? 261  ARG A NE     1 
ATOM   1320 C CZ     . ARG A 1 78  ? 31.642 12.525 52.683 1.00 12.19 ? 261  ARG A CZ     1 
ATOM   1321 N NH1    . ARG A 1 78  ? 30.641 11.986 53.366 1.00 13.25 ? 261  ARG A NH1    1 
ATOM   1322 N NH2    . ARG A 1 78  ? 32.467 11.737 51.988 1.00 12.77 ? 261  ARG A NH2    1 
ATOM   1323 H H      . ARG A 1 78  ? 27.923 17.047 51.813 1.00 13.43 ? 261  ARG A H      1 
ATOM   1324 H HA     . ARG A 1 78  ? 28.688 15.899 54.135 1.00 13.97 ? 261  ARG A HA     1 
ATOM   1325 H HB2    . ARG A 1 78  ? 29.987 17.929 52.664 1.00 14.52 ? 261  ARG A HB2    1 
ATOM   1326 H HB3    . ARG A 1 78  ? 30.531 17.383 54.053 1.00 14.52 ? 261  ARG A HB3    1 
ATOM   1327 H HG2    . ARG A 1 78  ? 30.362 15.826 51.693 1.00 13.97 ? 261  ARG A HG2    1 
ATOM   1328 H HG3    . ARG A 1 78  ? 31.717 16.397 52.295 1.00 13.97 ? 261  ARG A HG3    1 
ATOM   1329 H HD2    . ARG A 1 78  ? 31.406 15.029 54.190 1.00 15.10 ? 261  ARG A HD2    1 
ATOM   1330 H HD3    . ARG A 1 78  ? 30.122 14.404 53.493 1.00 15.10 ? 261  ARG A HD3    1 
ATOM   1331 H HE     . ARG A 1 78  ? 32.500 14.139 52.217 1.00 13.92 ? 261  ARG A HE     1 
ATOM   1332 H HH11   . ARG A 1 78  ? 30.100 12.490 53.806 1.00 15.90 ? 261  ARG A HH11   1 
ATOM   1333 H HH12   . ARG A 1 78  ? 30.532 11.133 53.368 1.00 15.90 ? 261  ARG A HH12   1 
ATOM   1334 H HH21   . ARG A 1 78  ? 33.111 12.083 51.535 1.00 15.33 ? 261  ARG A HH21   1 
ATOM   1335 H HH22   . ARG A 1 78  ? 32.354 10.885 51.993 1.00 15.33 ? 261  ARG A HH22   1 
ATOM   1336 N N      . LYS A 1 79  ? 27.137 18.604 54.064 1.00 12.17 ? 262  LYS A N      1 
ATOM   1337 C CA     . LYS A 1 79  ? 26.422 19.607 54.837 1.00 13.60 ? 262  LYS A CA     1 
ATOM   1338 C C      . LYS A 1 79  ? 27.248 20.469 55.790 1.00 13.33 ? 262  LYS A C      1 
ATOM   1339 O O      . LYS A 1 79  ? 26.848 20.672 56.939 1.00 15.02 ? 262  LYS A O      1 
ATOM   1340 C CB     . LYS A 1 79  ? 25.278 18.947 55.596 1.00 16.08 ? 262  LYS A CB     1 
ATOM   1341 C CG     . LYS A 1 79  ? 24.377 18.048 54.748 1.00 20.31 ? 262  LYS A CG     1 
ATOM   1342 C CD     . LYS A 1 79  ? 23.092 17.651 55.457 1.00 25.69 ? 262  LYS A CD     1 
ATOM   1343 C CE     . LYS A 1 79  ? 22.234 16.725 54.565 1.00 29.12 ? 262  LYS A CE     1 
ATOM   1344 N NZ     . LYS A 1 79  ? 21.896 17.339 53.235 1.00 32.59 ? 262  LYS A NZ     1 
ATOM   1345 H H      . LYS A 1 79  ? 26.913 18.606 53.233 1.00 14.60 ? 262  LYS A H      1 
ATOM   1346 H HA     . LYS A 1 79  ? 26.087 20.248 54.191 1.00 16.32 ? 262  LYS A HA     1 
ATOM   1347 H HB2    . LYS A 1 79  ? 25.653 18.399 56.303 1.00 19.30 ? 262  LYS A HB2    1 
ATOM   1348 H HB3    . LYS A 1 79  ? 24.719 19.642 55.977 1.00 19.30 ? 262  LYS A HB3    1 
ATOM   1349 H HG2    . LYS A 1 79  ? 24.136 18.520 53.936 1.00 24.37 ? 262  LYS A HG2    1 
ATOM   1350 H HG3    . LYS A 1 79  ? 24.860 17.235 54.529 1.00 24.37 ? 262  LYS A HG3    1 
ATOM   1351 H HD2    . LYS A 1 79  ? 23.307 17.176 56.275 1.00 30.83 ? 262  LYS A HD2    1 
ATOM   1352 H HD3    . LYS A 1 79  ? 22.576 18.446 55.661 1.00 30.83 ? 262  LYS A HD3    1 
ATOM   1353 H HE2    . LYS A 1 79  ? 22.724 15.905 54.399 1.00 34.94 ? 262  LYS A HE2    1 
ATOM   1354 H HE3    . LYS A 1 79  ? 21.402 16.529 55.023 1.00 34.94 ? 262  LYS A HE3    1 
ATOM   1355 H HZ1    . LYS A 1 79  ? 21.397 16.776 52.758 1.00 39.11 ? 262  LYS A HZ1    1 
ATOM   1356 H HZ2    . LYS A 1 79  ? 21.443 18.095 53.354 1.00 39.11 ? 262  LYS A HZ2    1 
ATOM   1357 H HZ3    . LYS A 1 79  ? 22.642 17.517 52.783 1.00 39.11 ? 262  LYS A HZ3    1 
ATOM   1358 N N      . PRO A 1 80  ? 28.348 21.059 55.327 1.00 12.27 ? 263  PRO A N      1 
ATOM   1359 C CA     . PRO A 1 80  ? 29.002 22.108 56.126 1.00 12.38 ? 263  PRO A CA     1 
ATOM   1360 C C      . PRO A 1 80  ? 28.096 23.325 56.208 1.00 11.79 ? 263  PRO A C      1 
ATOM   1361 O O      . PRO A 1 80  ? 27.170 23.505 55.415 1.00 12.77 ? 263  PRO A O      1 
ATOM   1362 C CB     . PRO A 1 80  ? 30.258 22.415 55.312 1.00 12.67 ? 263  PRO A CB     1 
ATOM   1363 C CG     . PRO A 1 80  ? 29.850 22.182 53.884 1.00 12.97 ? 263  PRO A CG     1 
ATOM   1364 C CD     . PRO A 1 80  ? 28.889 21.016 53.959 1.00 12.00 ? 263  PRO A CD     1 
ATOM   1365 H HA     . PRO A 1 80  ? 29.247 21.801 57.013 1.00 14.86 ? 263  PRO A HA     1 
ATOM   1366 H HB2    . PRO A 1 80  ? 30.527 23.337 55.452 1.00 15.21 ? 263  PRO A HB2    1 
ATOM   1367 H HB3    . PRO A 1 80  ? 30.976 21.817 55.571 1.00 15.21 ? 263  PRO A HB3    1 
ATOM   1368 H HG2    . PRO A 1 80  ? 29.414 22.972 53.528 1.00 15.57 ? 263  PRO A HG2    1 
ATOM   1369 H HG3    . PRO A 1 80  ? 30.627 21.962 53.346 1.00 15.57 ? 263  PRO A HG3    1 
ATOM   1370 H HD2    . PRO A 1 80  ? 28.177 21.122 53.309 1.00 14.40 ? 263  PRO A HD2    1 
ATOM   1371 H HD3    . PRO A 1 80  ? 29.358 20.181 53.805 1.00 14.40 ? 263  PRO A HD3    1 
ATOM   1372 N N      . PHE A 1 81  ? 28.432 24.214 57.129 1.00 12.02 ? 264  PHE A N      1 
ATOM   1373 C CA     . PHE A 1 81  ? 27.762 25.506 57.180 1.00 10.76 ? 264  PHE A CA     1 
ATOM   1374 C C      . PHE A 1 81  ? 28.212 26.333 56.004 1.00 10.88 ? 264  PHE A C      1 
ATOM   1375 O O      . PHE A 1 81  ? 29.411 26.411 55.715 1.00 12.70 ? 264  PHE A O      1 
ATOM   1376 C CB     . PHE A 1 81  ? 28.135 26.179 58.483 1.00 12.35 ? 264  PHE A CB     1 
ATOM   1377 C CG     . PHE A 1 81  ? 27.606 27.567 58.608 1.00 13.11 ? 264  PHE A CG     1 
ATOM   1378 C CD1    . PHE A 1 81  ? 26.275 27.794 58.955 1.00 15.92 ? 264  PHE A CD1    1 
ATOM   1379 C CD2    . PHE A 1 81  ? 28.418 28.669 58.392 1.00 13.81 ? 264  PHE A CD2    1 
ATOM   1380 C CE1    . PHE A 1 81  ? 25.781 29.099 59.081 1.00 17.20 ? 264  PHE A CE1    1 
ATOM   1381 C CE2    . PHE A 1 81  ? 27.928 29.946 58.501 1.00 15.04 ? 264  PHE A CE2    1 
ATOM   1382 C CZ     . PHE A 1 81  ? 26.632 30.159 58.863 1.00 16.11 ? 264  PHE A CZ     1 
ATOM   1383 H H      . PHE A 1 81  ? 29.037 24.098 57.729 1.00 14.42 ? 264  PHE A H      1 
ATOM   1384 H HA     . PHE A 1 81  ? 26.797 25.415 57.137 1.00 12.91 ? 264  PHE A HA     1 
ATOM   1385 H HB2    . PHE A 1 81  ? 27.777 25.657 59.218 1.00 14.82 ? 264  PHE A HB2    1 
ATOM   1386 H HB3    . PHE A 1 81  ? 29.102 26.223 58.547 1.00 14.82 ? 264  PHE A HB3    1 
ATOM   1387 H HD1    . PHE A 1 81  ? 25.709 27.072 59.105 1.00 19.10 ? 264  PHE A HD1    1 
ATOM   1388 H HD2    . PHE A 1 81  ? 29.311 28.541 58.168 1.00 16.57 ? 264  PHE A HD2    1 
ATOM   1389 H HE1    . PHE A 1 81  ? 24.892 29.247 59.308 1.00 20.65 ? 264  PHE A HE1    1 
ATOM   1390 H HE2    . PHE A 1 81  ? 28.484 30.671 58.327 1.00 18.04 ? 264  PHE A HE2    1 
ATOM   1391 H HZ     . PHE A 1 81  ? 26.319 31.029 58.965 1.00 19.33 ? 264  PHE A HZ     1 
ATOM   1392 N N      A ILE A 1 82  ? 27.263 26.940 55.304 0.58 12.36 ? 265  ILE A N      1 
ATOM   1393 N N      B ILE A 1 82  ? 27.263 26.955 55.314 0.42 12.31 ? 265  ILE A N      1 
ATOM   1394 C CA     A ILE A 1 82  ? 27.646 27.750 54.156 0.58 14.19 ? 265  ILE A CA     1 
ATOM   1395 C CA     B ILE A 1 82  ? 27.616 27.746 54.142 0.42 14.28 ? 265  ILE A CA     1 
ATOM   1396 C C      A ILE A 1 82  ? 27.166 29.193 54.342 0.58 15.18 ? 265  ILE A C      1 
ATOM   1397 C C      B ILE A 1 82  ? 27.147 29.189 54.322 0.42 15.20 ? 265  ILE A C      1 
ATOM   1398 O O      A ILE A 1 82  ? 26.213 29.481 55.077 0.58 17.70 ? 265  ILE A O      1 
ATOM   1399 O O      B ILE A 1 82  ? 26.170 29.477 55.024 0.42 17.65 ? 265  ILE A O      1 
ATOM   1400 C CB     A ILE A 1 82  ? 27.260 27.212 52.763 0.58 16.72 ? 265  ILE A CB     1 
ATOM   1401 C CB     B ILE A 1 82  ? 27.128 27.170 52.796 0.42 17.27 ? 265  ILE A CB     1 
ATOM   1402 C CG1    A ILE A 1 82  ? 25.758 27.175 52.654 0.58 17.25 ? 265  ILE A CG1    1 
ATOM   1403 C CG1    B ILE A 1 82  ? 25.618 27.241 52.725 0.42 18.70 ? 265  ILE A CG1    1 
ATOM   1404 C CG2    A ILE A 1 82  ? 27.868 25.807 52.459 0.58 16.71 ? 265  ILE A CG2    1 
ATOM   1405 C CG2    B ILE A 1 82  ? 27.594 25.707 52.581 0.42 18.04 ? 265  ILE A CG2    1 
ATOM   1406 C CD1    A ILE A 1 82  ? 25.270 26.688 51.310 0.58 18.05 ? 265  ILE A CD1    1 
ATOM   1407 C CD1    B ILE A 1 82  ? 25.085 28.504 52.078 0.42 21.52 ? 265  ILE A CD1    1 
ATOM   1408 H H      A ILE A 1 82  ? 26.420 26.898 55.469 0.58 14.83 ? 265  ILE A H      1 
ATOM   1409 H H      B ILE A 1 82  ? 26.424 26.933 55.502 0.42 14.78 ? 265  ILE A H      1 
ATOM   1410 H HA     A ILE A 1 82  ? 28.616 27.739 54.166 0.58 17.03 ? 265  ILE A HA     1 
ATOM   1411 H HA     B ILE A 1 82  ? 28.585 27.745 54.102 0.42 17.14 ? 265  ILE A HA     1 
ATOM   1412 H HB     A ILE A 1 82  ? 27.632 27.816 52.101 0.58 20.07 ? 265  ILE A HB     1 
ATOM   1413 H HB     B ILE A 1 82  ? 27.521 27.710 52.092 0.42 20.72 ? 265  ILE A HB     1 
ATOM   1414 H HG12   A ILE A 1 82  ? 25.409 26.577 53.333 0.58 20.70 ? 265  ILE A HG12   1 
ATOM   1415 H HG12   B ILE A 1 82  ? 25.296 26.487 52.207 0.42 22.45 ? 265  ILE A HG12   1 
ATOM   1416 H HG13   A ILE A 1 82  ? 25.411 28.070 52.791 0.58 20.70 ? 265  ILE A HG13   1 
ATOM   1417 H HG13   B ILE A 1 82  ? 25.263 27.200 53.626 0.42 22.45 ? 265  ILE A HG13   1 
ATOM   1418 H HG21   A ILE A 1 82  ? 27.915 25.684 51.498 0.58 20.06 ? 265  ILE A HG21   1 
ATOM   1419 H HG21   B ILE A 1 82  ? 27.502 25.480 51.643 0.42 21.65 ? 265  ILE A HG21   1 
ATOM   1420 H HG22   A ILE A 1 82  ? 28.757 25.758 52.843 0.58 20.06 ? 265  ILE A HG22   1 
ATOM   1421 H HG22   B ILE A 1 82  ? 28.523 25.628 52.851 0.42 21.65 ? 265  ILE A HG22   1 
ATOM   1422 H HG23   A ILE A 1 82  ? 27.300 25.126 52.853 0.58 20.06 ? 265  ILE A HG23   1 
ATOM   1423 H HG23   B ILE A 1 82  ? 27.042 25.118 53.119 0.42 21.65 ? 265  ILE A HG23   1 
ATOM   1424 H HD11   A ILE A 1 82  ? 24.328 26.898 51.221 0.58 21.67 ? 265  ILE A HD11   1 
ATOM   1425 H HD11   B ILE A 1 82  ? 24.568 29.000 52.732 0.42 25.83 ? 265  ILE A HD11   1 
ATOM   1426 H HD12   A ILE A 1 82  ? 25.775 27.132 50.611 0.58 21.67 ? 265  ILE A HD12   1 
ATOM   1427 H HD12   B ILE A 1 82  ? 25.832 29.041 51.770 0.42 25.83 ? 265  ILE A HD12   1 
ATOM   1428 H HD13   A ILE A 1 82  ? 25.403 25.729 51.255 0.58 21.67 ? 265  ILE A HD13   1 
ATOM   1429 H HD13   B ILE A 1 82  ? 24.521 28.261 51.327 0.42 25.83 ? 265  ILE A HD13   1 
ATOM   1430 N N      . ILE A 1 83  ? 27.893 30.103 53.715 1.00 13.61 ? 266  ILE A N      1 
ATOM   1431 C CA     . ILE A 1 83  ? 27.546 31.533 53.753 1.00 12.53 ? 266  ILE A CA     1 
ATOM   1432 C C      . ILE A 1 83  ? 26.975 32.045 52.441 1.00 11.88 ? 266  ILE A C      1 
ATOM   1433 O O      . ILE A 1 83  ? 26.252 33.056 52.463 1.00 12.30 ? 266  ILE A O      1 
ATOM   1434 C CB     . ILE A 1 83  ? 28.736 32.409 54.211 1.00 14.95 ? 266  ILE A CB     1 
ATOM   1435 C CG1    . ILE A 1 83  ? 29.902 32.306 53.235 1.00 15.05 ? 266  ILE A CG1    1 
ATOM   1436 C CG2    . ILE A 1 83  ? 29.133 32.055 55.622 1.00 17.46 ? 266  ILE A CG2    1 
ATOM   1437 C CD1    . ILE A 1 83  ? 31.028 33.356 53.493 1.00 16.85 ? 266  ILE A CD1    1 
ATOM   1438 H H      A ILE A 1 83  ? 28.597 29.927 53.255 0.58 16.34 ? 266  ILE A H      1 
ATOM   1439 H H      B ILE A 1 83  ? 28.608 29.928 53.271 0.42 16.34 ? 266  ILE A H      1 
ATOM   1440 H HA     . ILE A 1 83  ? 26.850 31.646 54.418 1.00 15.04 ? 266  ILE A HA     1 
ATOM   1441 H HB     . ILE A 1 83  ? 28.455 33.337 54.211 1.00 17.94 ? 266  ILE A HB     1 
ATOM   1442 H HG12   . ILE A 1 83  ? 30.296 31.423 53.310 1.00 18.06 ? 266  ILE A HG12   1 
ATOM   1443 H HG13   . ILE A 1 83  ? 29.568 32.444 52.334 1.00 18.06 ? 266  ILE A HG13   1 
ATOM   1444 H HG21   . ILE A 1 83  ? 29.841 32.653 55.910 1.00 20.95 ? 266  ILE A HG21   1 
ATOM   1445 H HG22   . ILE A 1 83  ? 28.362 32.152 56.201 1.00 20.95 ? 266  ILE A HG22   1 
ATOM   1446 H HG23   . ILE A 1 83  ? 29.448 31.137 55.640 1.00 20.95 ? 266  ILE A HG23   1 
ATOM   1447 H HD11   . ILE A 1 83  ? 31.746 33.213 52.857 1.00 20.22 ? 266  ILE A HD11   1 
ATOM   1448 H HD12   . ILE A 1 83  ? 30.661 34.247 53.382 1.00 20.22 ? 266  ILE A HD12   1 
ATOM   1449 H HD13   . ILE A 1 83  ? 31.361 33.246 54.398 1.00 20.22 ? 266  ILE A HD13   1 
ATOM   1450 N N      . ASN A 1 84  ? 27.286 31.405 51.314 1.00 11.49 ? 267  ASN A N      1 
ATOM   1451 C CA     . ASN A 1 84  ? 26.804 31.832 50.001 1.00 11.38 ? 267  ASN A CA     1 
ATOM   1452 C C      . ASN A 1 84  ? 26.129 30.603 49.393 1.00 12.31 ? 267  ASN A C      1 
ATOM   1453 O O      . ASN A 1 84  ? 26.791 29.620 49.068 1.00 14.13 ? 267  ASN A O      1 
ATOM   1454 C CB     . ASN A 1 84  ? 27.920 32.333 49.085 1.00 12.75 ? 267  ASN A CB     1 
ATOM   1455 C CG     . ASN A 1 84  ? 28.336 33.779 49.388 1.00 12.24 ? 267  ASN A CG     1 
ATOM   1456 O OD1    . ASN A 1 84  ? 28.660 34.142 50.504 1.00 14.00 ? 267  ASN A OD1    1 
ATOM   1457 N ND2    . ASN A 1 84  ? 28.305 34.589 48.384 1.00 11.42 ? 267  ASN A ND2    1 
ATOM   1458 H H      . ASN A 1 84  ? 27.784 30.705 51.284 1.00 13.79 ? 267  ASN A H      1 
ATOM   1459 H HA     . ASN A 1 84  ? 26.179 32.567 50.103 1.00 13.66 ? 267  ASN A HA     1 
ATOM   1460 H HB2    . ASN A 1 84  ? 28.700 31.767 49.199 1.00 15.30 ? 267  ASN A HB2    1 
ATOM   1461 H HB3    . ASN A 1 84  ? 27.614 32.296 48.165 1.00 15.30 ? 267  ASN A HB3    1 
ATOM   1462 H HD21   . ASN A 1 84  ? 28.527 35.413 48.489 1.00 13.71 ? 267  ASN A HD21   1 
ATOM   1463 H HD22   . ASN A 1 84  ? 28.062 34.305 47.609 1.00 13.71 ? 267  ASN A HD22   1 
ATOM   1464 N N      . ASP A 1 85  ? 24.807 30.629 49.239 1.00 11.36 ? 268  ASP A N      1 
ATOM   1465 C CA     . ASP A 1 85  ? 24.083 29.483 48.685 1.00 11.31 ? 268  ASP A CA     1 
ATOM   1466 C C      . ASP A 1 85  ? 24.569 29.192 47.268 1.00 11.31 ? 268  ASP A C      1 
ATOM   1467 O O      . ASP A 1 85  ? 24.645 30.072 46.414 1.00 13.11 ? 268  ASP A O      1 
ATOM   1468 C CB     . ASP A 1 85  ? 22.594 29.808 48.702 1.00 11.58 ? 268  ASP A CB     1 
ATOM   1469 C CG     . ASP A 1 85  ? 21.747 28.633 48.279 1.00 13.86 ? 268  ASP A CG     1 
ATOM   1470 O OD1    . ASP A 1 85  ? 21.527 28.402 47.092 1.00 14.90 ? 268  ASP A OD1    1 
ATOM   1471 O OD2    . ASP A 1 85  ? 21.442 27.836 49.167 1.00 17.01 ? 268  ASP A OD2    1 
ATOM   1472 H H      . ASP A 1 85  ? 24.305 31.296 49.446 1.00 13.63 ? 268  ASP A H      1 
ATOM   1473 H HA     . ASP A 1 85  ? 24.235 28.684 49.213 1.00 13.57 ? 268  ASP A HA     1 
ATOM   1474 H HB2    . ASP A 1 85  ? 22.334 30.059 49.602 1.00 13.90 ? 268  ASP A HB2    1 
ATOM   1475 H HB3    . ASP A 1 85  ? 22.421 30.540 48.090 1.00 13.90 ? 268  ASP A HB3    1 
ATOM   1476 N N      . LEU A 1 86  ? 24.923 27.925 46.997 1.00 10.94 ? 269  LEU A N      1 
ATOM   1477 C CA     . LEU A 1 86  ? 25.486 27.581 45.715 1.00 9.62  ? 269  LEU A CA     1 
ATOM   1478 C C      . LEU A 1 86  ? 24.420 27.519 44.620 1.00 9.65  ? 269  LEU A C      1 
ATOM   1479 O O      . LEU A 1 86  ? 24.691 27.901 43.474 1.00 10.30 ? 269  LEU A O      1 
ATOM   1480 C CB     . LEU A 1 86  ? 26.209 26.224 45.806 1.00 11.34 ? 269  LEU A CB     1 
ATOM   1481 C CG     . LEU A 1 86  ? 27.566 26.202 46.516 1.00 13.76 ? 269  LEU A CG     1 
ATOM   1482 C CD1    . LEU A 1 86  ? 28.065 24.749 46.568 1.00 16.26 ? 269  LEU A CD1    1 
ATOM   1483 C CD2    . LEU A 1 86  ? 28.555 27.080 45.793 1.00 15.59 ? 269  LEU A CD2    1 
ATOM   1484 H H      . LEU A 1 86  ? 24.843 27.264 47.542 1.00 13.13 ? 269  LEU A H      1 
ATOM   1485 H HA     . LEU A 1 86  ? 26.130 28.264 45.473 1.00 11.54 ? 269  LEU A HA     1 
ATOM   1486 H HB2    . LEU A 1 86  ? 25.630 25.610 46.285 1.00 13.61 ? 269  LEU A HB2    1 
ATOM   1487 H HB3    . LEU A 1 86  ? 26.358 25.904 44.903 1.00 13.61 ? 269  LEU A HB3    1 
ATOM   1488 H HG     . LEU A 1 86  ? 27.482 26.545 47.420 1.00 16.51 ? 269  LEU A HG     1 
ATOM   1489 H HD11   . LEU A 1 86  ? 28.941 24.730 46.983 1.00 19.51 ? 269  LEU A HD11   1 
ATOM   1490 H HD12   . LEU A 1 86  ? 27.441 24.219 47.089 1.00 19.51 ? 269  LEU A HD12   1 
ATOM   1491 H HD13   . LEU A 1 86  ? 28.120 24.401 45.664 1.00 19.51 ? 269  LEU A HD13   1 
ATOM   1492 H HD21   . LEU A 1 86  ? 29.429 26.972 46.199 1.00 18.71 ? 269  LEU A HD21   1 
ATOM   1493 H HD22   . LEU A 1 86  ? 28.588 26.817 44.860 1.00 18.71 ? 269  LEU A HD22   1 
ATOM   1494 H HD23   . LEU A 1 86  ? 28.268 28.004 45.867 1.00 18.71 ? 269  LEU A HD23   1 
ATOM   1495 N N      . ILE A 1 87  ? 23.249 26.951 44.936 1.00 10.71 ? 270  ILE A N      1 
ATOM   1496 C CA     . ILE A 1 87  ? 22.196 26.797 43.916 1.00 10.72 ? 270  ILE A CA     1 
ATOM   1497 C C      . ILE A 1 87  ? 21.760 28.175 43.397 1.00 10.24 ? 270  ILE A C      1 
ATOM   1498 O O      . ILE A 1 87  ? 21.613 28.387 42.193 1.00 10.57 ? 270  ILE A O      1 
ATOM   1499 C CB     . ILE A 1 87  ? 21.013 25.978 44.467 1.00 10.81 ? 270  ILE A CB     1 
ATOM   1500 C CG1    . ILE A 1 87  ? 21.436 24.529 44.764 1.00 11.48 ? 270  ILE A CG1    1 
ATOM   1501 C CG2    . ILE A 1 87  ? 19.824 25.994 43.553 1.00 11.17 ? 270  ILE A CG2    1 
ATOM   1502 C CD1    . ILE A 1 87  ? 20.559 23.832 45.695 1.00 13.65 ? 270  ILE A CD1    1 
ATOM   1503 H H      . ILE A 1 87  ? 23.041 26.653 45.715 1.00 12.85 ? 270  ILE A H      1 
ATOM   1504 H HA     . ILE A 1 87  ? 22.561 26.299 43.168 1.00 12.86 ? 270  ILE A HA     1 
ATOM   1505 H HB     . ILE A 1 87  ? 20.749 26.407 45.296 1.00 12.97 ? 270  ILE A HB     1 
ATOM   1506 H HG12   . ILE A 1 87  ? 21.440 24.030 43.932 1.00 13.78 ? 270  ILE A HG12   1 
ATOM   1507 H HG13   . ILE A 1 87  ? 22.327 24.538 45.149 1.00 13.78 ? 270  ILE A HG13   1 
ATOM   1508 H HG21   . ILE A 1 87  ? 19.167 25.359 43.879 1.00 13.41 ? 270  ILE A HG21   1 
ATOM   1509 H HG22   . ILE A 1 87  ? 19.445 26.886 43.544 1.00 13.41 ? 270  ILE A HG22   1 
ATOM   1510 H HG23   . ILE A 1 87  ? 20.109 25.746 42.660 1.00 13.41 ? 270  ILE A HG23   1 
ATOM   1511 H HD11   . ILE A 1 87  ? 20.868 22.918 45.795 1.00 16.38 ? 270  ILE A HD11   1 
ATOM   1512 H HD12   . ILE A 1 87  ? 20.584 24.286 46.552 1.00 16.38 ? 270  ILE A HD12   1 
ATOM   1513 H HD13   . ILE A 1 87  ? 19.655 23.839 45.343 1.00 16.38 ? 270  ILE A HD13   1 
ATOM   1514 N N      . MET A 1 88  ? 21.696 29.151 44.309 1.00 10.48 ? 271  MET A N      1 
ATOM   1515 C CA     . MET A 1 88  ? 21.295 30.492 43.910 1.00 10.79 ? 271  MET A CA     1 
ATOM   1516 C C      . MET A 1 88  ? 22.308 31.132 42.985 1.00 10.29 ? 271  MET A C      1 
ATOM   1517 O O      . MET A 1 88  ? 21.956 32.050 42.234 1.00 10.51 ? 271  MET A O      1 
ATOM   1518 C CB     . MET A 1 88  ? 21.054 31.393 45.125 1.00 11.48 ? 271  MET A CB     1 
ATOM   1519 C CG     . MET A 1 88  ? 19.731 31.106 45.806 1.00 12.98 ? 271  MET A CG     1 
ATOM   1520 S SD     . MET A 1 88  ? 18.231 31.355 44.879 1.00 13.11 ? 271  MET A SD     1 
ATOM   1521 C CE     . MET A 1 88  ? 18.164 33.144 44.897 1.00 13.01 ? 271  MET A CE     1 
ATOM   1522 H H      . MET A 1 88  ? 21.877 29.060 45.144 1.00 12.57 ? 271  MET A H      1 
ATOM   1523 H HA     . MET A 1 88  ? 20.444 30.419 43.452 1.00 12.95 ? 271  MET A HA     1 
ATOM   1524 H HB2    . MET A 1 88  ? 21.763 31.251 45.771 1.00 13.78 ? 271  MET A HB2    1 
ATOM   1525 H HB3    . MET A 1 88  ? 21.049 32.319 44.837 1.00 13.78 ? 271  MET A HB3    1 
ATOM   1526 H HG2    . MET A 1 88  ? 19.736 30.174 46.077 1.00 15.58 ? 271  MET A HG2    1 
ATOM   1527 H HG3    . MET A 1 88  ? 19.672 31.678 46.587 1.00 15.58 ? 271  MET A HG3    1 
ATOM   1528 H HE1    . MET A 1 88  ? 17.373 33.435 44.418 1.00 15.61 ? 271  MET A HE1    1 
ATOM   1529 H HE2    . MET A 1 88  ? 18.126 33.449 45.816 1.00 15.61 ? 271  MET A HE2    1 
ATOM   1530 H HE3    . MET A 1 88  ? 18.960 33.493 44.465 1.00 15.61 ? 271  MET A HE3    1 
ATOM   1531 N N      . GLN A 1 89  ? 23.570 30.696 43.036 1.00 10.50 ? 272  GLN A N      1 
ATOM   1532 C CA     . GLN A 1 89  ? 24.556 31.262 42.125 1.00 10.79 ? 272  GLN A CA     1 
ATOM   1533 C C      . GLN A 1 89  ? 24.223 30.996 40.668 1.00 11.53 ? 272  GLN A C      1 
ATOM   1534 O O      . GLN A 1 89  ? 24.645 31.748 39.794 1.00 12.56 ? 272  GLN A O      1 
ATOM   1535 C CB     . GLN A 1 89  ? 25.943 30.764 42.546 1.00 10.83 ? 272  GLN A CB     1 
ATOM   1536 C CG     . GLN A 1 89  ? 26.321 31.284 43.948 1.00 11.64 ? 272  GLN A CG     1 
ATOM   1537 C CD     . GLN A 1 89  ? 27.686 30.832 44.412 1.00 13.66 ? 272  GLN A CD     1 
ATOM   1538 O OE1    . GLN A 1 89  ? 28.580 30.659 43.603 1.00 18.21 ? 272  GLN A OE1    1 
ATOM   1539 N NE2    . GLN A 1 89  ? 27.842 30.660 45.700 1.00 13.77 ? 272  GLN A NE2    1 
ATOM   1540 H H      . GLN A 1 89  ? 23.868 30.094 43.573 1.00 12.59 ? 272  GLN A H      1 
ATOM   1541 H HA     . GLN A 1 89  ? 24.578 32.229 42.190 1.00 12.95 ? 272  GLN A HA     1 
ATOM   1542 H HB2    . GLN A 1 89  ? 25.943 29.794 42.568 1.00 13.00 ? 272  GLN A HB2    1 
ATOM   1543 H HB3    . GLN A 1 89  ? 26.605 31.082 41.912 1.00 13.00 ? 272  GLN A HB3    1 
ATOM   1544 H HG2    . GLN A 1 89  ? 26.319 32.254 43.934 1.00 13.97 ? 272  GLN A HG2    1 
ATOM   1545 H HG3    . GLN A 1 89  ? 25.668 30.961 44.589 1.00 13.97 ? 272  GLN A HG3    1 
ATOM   1546 H HE21   . GLN A 1 89  ? 27.185 30.804 46.236 1.00 16.52 ? 272  GLN A HE21   1 
ATOM   1547 H HE22   . GLN A 1 89  ? 28.602 30.403 46.010 1.00 16.52 ? 272  GLN A HE22   1 
ATOM   1548 N N      . LYS A 1 90  ? 23.417 29.969 40.392 1.00 11.66 ? 273  LYS A N      1 
ATOM   1549 C CA     . LYS A 1 90  ? 23.015 29.731 39.019 1.00 12.68 ? 273  LYS A CA     1 
ATOM   1550 C C      . LYS A 1 90  ? 22.162 30.848 38.456 1.00 13.93 ? 273  LYS A C      1 
ATOM   1551 O O      . LYS A 1 90  ? 22.114 31.040 37.237 1.00 15.36 ? 273  LYS A O      1 
ATOM   1552 C CB     . LYS A 1 90  ? 22.224 28.417 38.920 1.00 12.93 ? 273  LYS A CB     1 
ATOM   1553 C CG     . LYS A 1 90  ? 23.023 27.245 39.225 1.00 14.11 ? 273  LYS A CG     1 
ATOM   1554 C CD     . LYS A 1 90  ? 22.207 25.967 38.954 1.00 15.96 ? 273  LYS A CD     1 
ATOM   1555 C CE     . LYS A 1 90  ? 23.004 24.782 39.351 1.00 16.37 ? 273  LYS A CE     1 
ATOM   1556 N NZ     . LYS A 1 90  ? 22.318 23.509 38.913 1.00 17.47 ? 273  LYS A NZ     1 
ATOM   1557 H H      . LYS A 1 90  ? 23.101 29.415 40.969 1.00 14.00 ? 273  LYS A H      1 
ATOM   1558 H HA     . LYS A 1 90  ? 23.825 29.666 38.488 1.00 15.22 ? 273  LYS A HA     1 
ATOM   1559 H HB2    . LYS A 1 90  ? 21.486 28.447 39.548 1.00 15.52 ? 273  LYS A HB2    1 
ATOM   1560 H HB3    . LYS A 1 90  ? 21.886 28.321 38.016 1.00 15.52 ? 273  LYS A HB3    1 
ATOM   1561 H HG2    . LYS A 1 90  ? 23.815 27.234 38.665 1.00 16.93 ? 273  LYS A HG2    1 
ATOM   1562 H HG3    . LYS A 1 90  ? 23.279 27.258 40.161 1.00 16.93 ? 273  LYS A HG3    1 
ATOM   1563 H HD2    . LYS A 1 90  ? 21.388 25.982 39.473 1.00 19.15 ? 273  LYS A HD2    1 
ATOM   1564 H HD3    . LYS A 1 90  ? 21.999 25.903 38.008 1.00 19.15 ? 273  LYS A HD3    1 
ATOM   1565 H HE2    . LYS A 1 90  ? 23.877 24.823 38.931 1.00 19.65 ? 273  LYS A HE2    1 
ATOM   1566 H HE3    . LYS A 1 90  ? 23.100 24.765 40.316 1.00 19.65 ? 273  LYS A HE3    1 
ATOM   1567 H HZ1    . LYS A 1 90  ? 22.835 22.808 39.095 1.00 20.96 ? 273  LYS A HZ1    1 
ATOM   1568 H HZ2    . LYS A 1 90  ? 21.544 23.417 39.342 1.00 20.96 ? 273  LYS A HZ2    1 
ATOM   1569 H HZ3    . LYS A 1 90  ? 22.162 23.534 38.037 1.00 20.96 ? 273  LYS A HZ3    1 
ATOM   1570 N N      . ILE A 1 91  ? 21.407 31.534 39.303 1.00 11.82 ? 274  ILE A N      1 
ATOM   1571 C CA     . ILE A 1 91  ? 20.510 32.519 38.736 1.00 13.90 ? 274  ILE A CA     1 
ATOM   1572 C C      . ILE A 1 91  ? 21.238 33.751 38.272 1.00 13.33 ? 274  ILE A C      1 
ATOM   1573 O O      . ILE A 1 91  ? 20.718 34.514 37.453 1.00 14.11 ? 274  ILE A O      1 
ATOM   1574 C CB     . ILE A 1 91  ? 19.346 32.796 39.655 1.00 17.04 ? 274  ILE A CB     1 
ATOM   1575 C CG1    . ILE A 1 91  ? 19.721 33.712 40.723 1.00 16.62 ? 274  ILE A CG1    1 
ATOM   1576 C CG2    . ILE A 1 91  ? 18.637 31.526 40.112 1.00 19.02 ? 274  ILE A CG2    1 
ATOM   1577 C CD1    . ILE A 1 91  ? 18.498 34.371 41.174 1.00 18.04 ? 274  ILE A CD1    1 
ATOM   1578 H H      . ILE A 1 91  ? 21.397 31.450 40.159 1.00 14.19 ? 274  ILE A H      1 
ATOM   1579 H HA     . ILE A 1 91  ? 20.105 32.156 37.933 1.00 16.68 ? 274  ILE A HA     1 
ATOM   1580 H HB     . ILE A 1 91  ? 18.668 33.263 39.141 1.00 20.45 ? 274  ILE A HB     1 
ATOM   1581 H HG12   . ILE A 1 91  ? 20.117 33.224 41.462 1.00 19.94 ? 274  ILE A HG12   1 
ATOM   1582 H HG13   . ILE A 1 91  ? 20.345 34.377 40.393 1.00 19.94 ? 274  ILE A HG13   1 
ATOM   1583 H HG21   . ILE A 1 91  ? 17.743 31.754 40.412 1.00 22.82 ? 274  ILE A HG21   1 
ATOM   1584 H HG22   . ILE A 1 91  ? 18.587 30.906 39.368 1.00 22.82 ? 274  ILE A HG22   1 
ATOM   1585 H HG23   . ILE A 1 91  ? 19.139 31.128 40.841 1.00 22.82 ? 274  ILE A HG23   1 
ATOM   1586 H HD11   . ILE A 1 91  ? 18.644 34.735 42.061 1.00 21.64 ? 274  ILE A HD11   1 
ATOM   1587 H HD12   . ILE A 1 91  ? 18.278 35.085 40.555 1.00 21.64 ? 274  ILE A HD12   1 
ATOM   1588 H HD13   . ILE A 1 91  ? 17.779 33.720 41.198 1.00 21.64 ? 274  ILE A HD13   1 
ATOM   1589 N N      . LEU A 1 92  ? 22.473 33.954 38.753 1.00 13.98 ? 275  LEU A N      1 
ATOM   1590 C CA     . LEU A 1 92  ? 23.282 35.093 38.332 1.00 15.05 ? 275  LEU A CA     1 
ATOM   1591 C C      . LEU A 1 92  ? 23.575 35.051 36.846 1.00 15.25 ? 275  LEU A C      1 
ATOM   1592 O O      . LEU A 1 92  ? 23.917 36.059 36.257 1.00 17.75 ? 275  LEU A O      1 
ATOM   1593 C CB     . LEU A 1 92  ? 24.555 35.189 39.200 1.00 15.99 ? 275  LEU A CB     1 
ATOM   1594 C CG     . LEU A 1 92  ? 24.342 35.260 40.704 1.00 17.02 ? 275  LEU A CG     1 
ATOM   1595 C CD1    . LEU A 1 92  ? 25.720 35.286 41.411 1.00 18.42 ? 275  LEU A CD1    1 
ATOM   1596 C CD2    . LEU A 1 92  ? 23.483 36.490 41.007 1.00 17.38 ? 275  LEU A CD2    1 
ATOM   1597 H H      . LEU A 1 92  ? 22.862 33.443 39.325 1.00 16.78 ? 275  LEU A H      1 
ATOM   1598 H HA     . LEU A 1 92  ? 22.802 35.921 38.488 1.00 18.06 ? 275  LEU A HA     1 
ATOM   1599 H HB2    . LEU A 1 92  ? 25.099 34.405 39.025 1.00 19.19 ? 275  LEU A HB2    1 
ATOM   1600 H HB3    . LEU A 1 92  ? 25.036 35.990 38.941 1.00 19.19 ? 275  LEU A HB3    1 
ATOM   1601 H HG     . LEU A 1 92  ? 23.871 34.485 41.049 1.00 20.42 ? 275  LEU A HG     1 
ATOM   1602 H HD11   . LEU A 1 92  ? 25.583 35.286 42.372 1.00 22.11 ? 275  LEU A HD11   1 
ATOM   1603 H HD12   . LEU A 1 92  ? 26.225 34.500 41.149 1.00 22.11 ? 275  LEU A HD12   1 
ATOM   1604 H HD13   . LEU A 1 92  ? 26.197 36.088 41.145 1.00 22.11 ? 275  LEU A HD13   1 
ATOM   1605 H HD21   . LEU A 1 92  ? 23.410 36.596 41.969 1.00 20.85 ? 275  LEU A HD21   1 
ATOM   1606 H HD22   . LEU A 1 92  ? 23.904 37.273 40.620 1.00 20.85 ? 275  LEU A HD22   1 
ATOM   1607 H HD23   . LEU A 1 92  ? 22.602 36.364 40.621 1.00 20.85 ? 275  LEU A HD23   1 
ATOM   1608 N N      . TRP A 1 93  ? 23.370 33.899 36.214 1.00 14.92 ? 276  TRP A N      1 
ATOM   1609 C CA     . TRP A 1 93  ? 23.592 33.696 34.807 1.00 16.27 ? 276  TRP A CA     1 
ATOM   1610 C C      . TRP A 1 93  ? 22.426 34.148 33.946 1.00 15.60 ? 276  TRP A C      1 
ATOM   1611 O O      . TRP A 1 93  ? 22.579 34.188 32.723 1.00 18.26 ? 276  TRP A O      1 
ATOM   1612 C CB     . TRP A 1 93  ? 23.867 32.218 34.570 1.00 17.30 ? 276  TRP A CB     1 
ATOM   1613 C CG     . TRP A 1 93  ? 25.075 31.692 35.347 1.00 18.79 ? 276  TRP A CG     1 
ATOM   1614 C CD1    . TRP A 1 93  ? 26.115 32.397 35.873 1.00 20.59 ? 276  TRP A CD1    1 
ATOM   1615 C CD2    . TRP A 1 93  ? 25.300 30.331 35.678 1.00 18.69 ? 276  TRP A CD2    1 
ATOM   1616 N NE1    . TRP A 1 93  ? 26.993 31.536 36.491 1.00 21.13 ? 276  TRP A NE1    1 
ATOM   1617 C CE2    . TRP A 1 93  ? 26.503 30.263 36.409 1.00 19.80 ? 276  TRP A CE2    1 
ATOM   1618 C CE3    . TRP A 1 93  ? 24.593 29.138 35.416 1.00 20.37 ? 276  TRP A CE3    1 
ATOM   1619 C CZ2    . TRP A 1 93  ? 27.028 29.055 36.861 1.00 19.80 ? 276  TRP A CZ2    1 
ATOM   1620 C CZ3    . TRP A 1 93  ? 25.104 27.942 35.893 1.00 21.23 ? 276  TRP A CZ3    1 
ATOM   1621 C CH2    . TRP A 1 93  ? 26.326 27.908 36.589 1.00 20.76 ? 276  TRP A CH2    1 
ATOM   1622 H H      . TRP A 1 93  ? 23.088 33.188 36.607 1.00 17.90 ? 276  TRP A H      1 
ATOM   1623 H HA     . TRP A 1 93  ? 24.365 34.209 34.523 1.00 19.53 ? 276  TRP A HA     1 
ATOM   1624 H HB2    . TRP A 1 93  ? 23.090 31.707 34.846 1.00 20.76 ? 276  TRP A HB2    1 
ATOM   1625 H HB3    . TRP A 1 93  ? 24.038 32.079 33.626 1.00 20.76 ? 276  TRP A HB3    1 
ATOM   1626 H HD1    . TRP A 1 93  ? 26.216 33.320 35.822 1.00 24.71 ? 276  TRP A HD1    1 
ATOM   1627 H HE1    . TRP A 1 93  ? 27.732 31.762 36.869 1.00 25.35 ? 276  TRP A HE1    1 
ATOM   1628 H HE3    . TRP A 1 93  ? 23.799 29.155 34.933 1.00 24.45 ? 276  TRP A HE3    1 
ATOM   1629 H HZ2    . TRP A 1 93  ? 27.829 29.027 37.333 1.00 23.77 ? 276  TRP A HZ2    1 
ATOM   1630 H HZ3    . TRP A 1 93  ? 24.633 27.153 35.751 1.00 25.48 ? 276  TRP A HZ3    1 
ATOM   1631 H HH2    . TRP A 1 93  ? 26.666 27.089 36.871 1.00 24.91 ? 276  TRP A HH2    1 
ATOM   1632 N N      . ASP A 1 94  ? 21.259 34.406 34.525 1.00 12.91 ? 277  ASP A N      1 
ATOM   1633 C CA     . ASP A 1 94  ? 20.082 34.813 33.760 1.00 12.40 ? 277  ASP A CA     1 
ATOM   1634 C C      . ASP A 1 94  ? 19.497 36.083 34.356 1.00 11.58 ? 277  ASP A C      1 
ATOM   1635 O O      . ASP A 1 94  ? 18.966 36.082 35.467 1.00 11.53 ? 277  ASP A O      1 
ATOM   1636 C CB     . ASP A 1 94  ? 19.026 33.711 33.701 1.00 12.91 ? 277  ASP A CB     1 
ATOM   1637 C CG     . ASP A 1 94  ? 17.957 33.987 32.659 1.00 15.30 ? 277  ASP A CG     1 
ATOM   1638 O OD1    . ASP A 1 94  ? 17.414 35.103 32.575 1.00 14.72 ? 277  ASP A OD1    1 
ATOM   1639 O OD2    . ASP A 1 94  ? 17.645 33.075 31.890 1.00 19.52 ? 277  ASP A OD2    1 
ATOM   1640 H H      . ASP A 1 94  ? 21.120 34.351 35.372 1.00 15.49 ? 277  ASP A H      1 
ATOM   1641 H HA     . ASP A 1 94  ? 20.373 35.011 32.856 1.00 14.88 ? 277  ASP A HA     1 
ATOM   1642 H HB2    . ASP A 1 94  ? 19.456 32.871 33.475 1.00 15.50 ? 277  ASP A HB2    1 
ATOM   1643 H HB3    . ASP A 1 94  ? 18.592 33.640 34.566 1.00 15.50 ? 277  ASP A HB3    1 
ATOM   1644 N N      . ARG A 1 95  ? 19.659 37.185 33.638 1.00 11.61 ? 278  ARG A N      1 
ATOM   1645 C CA     A ARG A 1 95  ? 19.194 38.470 34.152 0.60 12.01 ? 278  ARG A CA     1 
ATOM   1646 C CA     B ARG A 1 95  ? 19.200 38.473 34.153 0.40 11.58 ? 278  ARG A CA     1 
ATOM   1647 C C      . ARG A 1 95  ? 17.716 38.450 34.494 1.00 11.81 ? 278  ARG A C      1 
ATOM   1648 O O      . ARG A 1 95  ? 17.285 39.145 35.404 1.00 12.39 ? 278  ARG A O      1 
ATOM   1649 C CB     A ARG A 1 95  ? 19.449 39.565 33.120 0.60 13.05 ? 278  ARG A CB     1 
ATOM   1650 C CB     B ARG A 1 95  ? 19.520 39.591 33.149 0.40 11.71 ? 278  ARG A CB     1 
ATOM   1651 C CG     A ARG A 1 95  ? 20.896 39.871 32.898 0.60 15.69 ? 278  ARG A CG     1 
ATOM   1652 C CG     B ARG A 1 95  ? 21.021 39.883 33.014 0.40 12.89 ? 278  ARG A CG     1 
ATOM   1653 C CD     A ARG A 1 95  ? 21.021 41.093 32.008 0.60 19.98 ? 278  ARG A CD     1 
ATOM   1654 C CD     B ARG A 1 95  ? 21.335 41.112 32.117 0.40 14.67 ? 278  ARG A CD     1 
ATOM   1655 N NE     A ARG A 1 95  ? 22.394 41.226 31.550 0.60 24.85 ? 278  ARG A NE     1 
ATOM   1656 N NE     B ARG A 1 95  ? 22.741 41.508 32.227 0.40 15.57 ? 278  ARG A NE     1 
ATOM   1657 C CZ     A ARG A 1 95  ? 23.324 41.918 32.190 0.60 28.53 ? 278  ARG A CZ     1 
ATOM   1658 C CZ     B ARG A 1 95  ? 23.698 41.182 31.359 0.40 16.33 ? 278  ARG A CZ     1 
ATOM   1659 N NH1    A ARG A 1 95  ? 23.040 42.606 33.289 0.60 30.62 ? 278  ARG A NH1    1 
ATOM   1660 N NH1    B ARG A 1 95  ? 23.416 40.687 30.167 0.40 17.23 ? 278  ARG A NH1    1 
ATOM   1661 N NH2    A ARG A 1 95  ? 24.576 41.882 31.746 0.60 30.75 ? 278  ARG A NH2    1 
ATOM   1662 N NH2    B ARG A 1 95  ? 24.974 41.374 31.690 0.40 17.96 ? 278  ARG A NH2    1 
ATOM   1663 H H      A ARG A 1 95  ? 20.029 37.220 32.863 0.60 13.94 ? 278  ARG A H      1 
ATOM   1664 H H      B ARG A 1 95  ? 20.027 37.219 32.861 0.40 13.94 ? 278  ARG A H      1 
ATOM   1665 H HA     A ARG A 1 95  ? 19.694 38.667 34.959 0.60 14.41 ? 278  ARG A HA     1 
ATOM   1666 H HA     B ARG A 1 95  ? 19.681 38.671 34.971 0.40 13.90 ? 278  ARG A HA     1 
ATOM   1667 H HB2    A ARG A 1 95  ? 19.074 39.284 32.271 0.60 15.66 ? 278  ARG A HB2    1 
ATOM   1668 H HB2    B ARG A 1 95  ? 19.188 39.332 32.276 0.40 14.05 ? 278  ARG A HB2    1 
ATOM   1669 H HB3    A ARG A 1 95  ? 19.018 40.380 33.421 0.60 15.66 ? 278  ARG A HB3    1 
ATOM   1670 H HB3    B ARG A 1 95  ? 19.085 40.407 33.442 0.40 14.05 ? 278  ARG A HB3    1 
ATOM   1671 H HG2    A ARG A 1 95  ? 21.328 40.056 33.747 0.60 18.83 ? 278  ARG A HG2    1 
ATOM   1672 H HG2    B ARG A 1 95  ? 21.388 40.057 33.895 0.40 15.47 ? 278  ARG A HG2    1 
ATOM   1673 H HG3    A ARG A 1 95  ? 21.329 39.120 32.463 0.60 18.83 ? 278  ARG A HG3    1 
ATOM   1674 H HG3    B ARG A 1 95  ? 21.456 39.110 32.620 0.40 15.47 ? 278  ARG A HG3    1 
ATOM   1675 H HD2    A ARG A 1 95  ? 20.441 40.997 31.236 0.60 23.98 ? 278  ARG A HD2    1 
ATOM   1676 H HD2    B ARG A 1 95  ? 21.152 40.890 31.191 0.40 17.61 ? 278  ARG A HD2    1 
ATOM   1677 H HD3    A ARG A 1 95  ? 20.779 41.889 32.507 0.60 23.98 ? 278  ARG A HD3    1 
ATOM   1678 H HD3    B ARG A 1 95  ? 20.784 41.861 32.394 0.40 17.61 ? 278  ARG A HD3    1 
ATOM   1679 H HE     A ARG A 1 95  ? 22.617 40.832 30.818 0.60 29.82 ? 278  ARG A HE     1 
ATOM   1680 H HE     B ARG A 1 95  ? 22.966 41.988 32.904 0.40 18.68 ? 278  ARG A HE     1 
ATOM   1681 H HH11   A ARG A 1 95  ? 22.238 42.608 33.600 0.60 36.75 ? 278  ARG A HH11   1 
ATOM   1682 H HH11   B ARG A 1 95  ? 22.597 40.567 29.933 0.40 20.67 ? 278  ARG A HH11   1 
ATOM   1683 H HH12   A ARG A 1 95  ? 23.658 43.049 33.691 0.60 36.75 ? 278  ARG A HH12   1 
ATOM   1684 H HH12   B ARG A 1 95  ? 24.052 40.484 29.624 0.40 20.67 ? 278  ARG A HH12   1 
ATOM   1685 H HH21   A ARG A 1 95  ? 24.772 41.414 31.052 0.60 36.90 ? 278  ARG A HH21   1 
ATOM   1686 H HH21   B ARG A 1 95  ? 25.174 41.706 32.458 0.40 21.55 ? 278  ARG A HH21   1 
ATOM   1687 H HH22   A ARG A 1 95  ? 25.189 42.326 32.152 0.60 36.90 ? 278  ARG A HH22   1 
ATOM   1688 H HH22   B ARG A 1 95  ? 25.598 41.167 31.135 0.40 21.55 ? 278  ARG A HH22   1 
ATOM   1689 N N      . ARG A 1 96  ? 16.918 37.671 33.770 1.00 11.78 ? 279  ARG A N      1 
ATOM   1690 C CA     . ARG A 1 96  ? 15.492 37.630 34.076 1.00 12.15 ? 279  ARG A CA     1 
ATOM   1691 C C      . ARG A 1 96  ? 15.226 37.067 35.469 1.00 12.08 ? 279  ARG A C      1 
ATOM   1692 O O      . ARG A 1 96  ? 14.400 37.595 36.220 1.00 12.96 ? 279  ARG A O      1 
ATOM   1693 C CB     . ARG A 1 96  ? 14.759 36.803 33.012 1.00 12.51 ? 279  ARG A CB     1 
ATOM   1694 C CG     . ARG A 1 96  ? 14.825 37.382 31.634 1.00 13.11 ? 279  ARG A CG     1 
ATOM   1695 C CD     . ARG A 1 96  ? 14.383 36.397 30.550 1.00 13.10 ? 279  ARG A CD     1 
ATOM   1696 N NE     . ARG A 1 96  ? 15.318 35.292 30.461 1.00 14.04 ? 279  ARG A NE     1 
ATOM   1697 C CZ     . ARG A 1 96  ? 15.284 34.395 29.491 1.00 15.28 ? 279  ARG A CZ     1 
ATOM   1698 N NH1    . ARG A 1 96  ? 14.419 34.499 28.503 1.00 16.67 ? 279  ARG A NH1    1 
ATOM   1699 N NH2    . ARG A 1 96  ? 16.147 33.382 29.507 1.00 15.75 ? 279  ARG A NH2    1 
ATOM   1700 H H      . ARG A 1 96  ? 17.168 37.172 33.116 1.00 14.14 ? 279  ARG A H      1 
ATOM   1701 H HA     . ARG A 1 96  ? 15.145 38.536 34.057 1.00 14.58 ? 279  ARG A HA     1 
ATOM   1702 H HB2    . ARG A 1 96  ? 15.155 35.918 32.979 1.00 15.01 ? 279  ARG A HB2    1 
ATOM   1703 H HB3    . ARG A 1 96  ? 13.823 36.739 33.259 1.00 15.01 ? 279  ARG A HB3    1 
ATOM   1704 H HG2    . ARG A 1 96  ? 14.243 38.156 31.589 1.00 15.73 ? 279  ARG A HG2    1 
ATOM   1705 H HG3    . ARG A 1 96  ? 15.740 37.642 31.446 1.00 15.73 ? 279  ARG A HG3    1 
ATOM   1706 H HD2    . ARG A 1 96  ? 13.506 36.044 30.768 1.00 15.72 ? 279  ARG A HD2    1 
ATOM   1707 H HD3    . ARG A 1 96  ? 14.355 36.849 29.692 1.00 15.72 ? 279  ARG A HD3    1 
ATOM   1708 H HE     . ARG A 1 96  ? 15.923 35.218 31.068 1.00 16.85 ? 279  ARG A HE     1 
ATOM   1709 H HH11   . ARG A 1 96  ? 13.866 35.158 28.482 1.00 20.01 ? 279  ARG A HH11   1 
ATOM   1710 H HH12   . ARG A 1 96  ? 14.407 33.909 27.878 1.00 20.01 ? 279  ARG A HH12   1 
ATOM   1711 H HH21   . ARG A 1 96  ? 16.720 33.316 30.144 1.00 18.90 ? 279  ARG A HH21   1 
ATOM   1712 H HH22   . ARG A 1 96  ? 16.131 32.794 28.879 1.00 18.90 ? 279  ARG A HH22   1 
ATOM   1713 N N      . LEU A 1 97  ? 15.924 35.989 35.835 1.00 12.29 ? 280  LEU A N      1 
ATOM   1714 C CA     . LEU A 1 97  ? 15.724 35.415 37.149 1.00 11.50 ? 280  LEU A CA     1 
ATOM   1715 C C      . LEU A 1 97  ? 16.241 36.351 38.234 1.00 9.15  ? 280  LEU A C      1 
ATOM   1716 O O      . LEU A 1 97  ? 15.637 36.455 39.303 1.00 9.92  ? 280  LEU A O      1 
ATOM   1717 C CB     . LEU A 1 97  ? 16.430 34.063 37.262 1.00 12.84 ? 280  LEU A CB     1 
ATOM   1718 C CG     . LEU A 1 97  ? 15.905 32.953 36.325 1.00 13.47 ? 280  LEU A CG     1 
ATOM   1719 C CD1    . LEU A 1 97  ? 16.712 31.656 36.467 1.00 15.25 ? 280  LEU A CD1    1 
ATOM   1720 C CD2    . LEU A 1 97  ? 14.449 32.680 36.614 1.00 13.91 ? 280  LEU A CD2    1 
ATOM   1721 H H      . LEU A 1 97  ? 16.505 35.585 35.347 1.00 14.75 ? 280  LEU A H      1 
ATOM   1722 H HA     . LEU A 1 97  ? 14.773 35.272 37.276 1.00 13.79 ? 280  LEU A HA     1 
ATOM   1723 H HB2    . LEU A 1 97  ? 17.369 34.193 37.057 1.00 15.41 ? 280  LEU A HB2    1 
ATOM   1724 H HB3    . LEU A 1 97  ? 16.330 33.743 38.172 1.00 15.41 ? 280  LEU A HB3    1 
ATOM   1725 H HG     . LEU A 1 97  ? 16.003 33.260 35.410 1.00 16.16 ? 280  LEU A HG     1 
ATOM   1726 H HD11   . LEU A 1 97  ? 16.326 30.979 35.888 1.00 18.30 ? 280  LEU A HD11   1 
ATOM   1727 H HD12   . LEU A 1 97  ? 17.632 31.826 36.209 1.00 18.30 ? 280  LEU A HD12   1 
ATOM   1728 H HD13   . LEU A 1 97  ? 16.676 31.361 37.390 1.00 18.30 ? 280  LEU A HD13   1 
ATOM   1729 H HD21   . LEU A 1 97  ? 14.145 31.955 36.045 1.00 16.69 ? 280  LEU A HD21   1 
ATOM   1730 H HD22   . LEU A 1 97  ? 14.354 32.431 37.546 1.00 16.69 ? 280  LEU A HD22   1 
ATOM   1731 H HD23   . LEU A 1 97  ? 13.935 33.481 36.431 1.00 16.69 ? 280  LEU A HD23   1 
ATOM   1732 N N      . CYS A 1 98  ? 17.382 37.015 37.988 1.00 10.47 ? 281  CYS A N      1 
ATOM   1733 C CA     A CYS A 1 98  ? 17.893 37.962 38.967 0.73 10.35 ? 281  CYS A CA     1 
ATOM   1734 C CA     B CYS A 1 98  ? 17.908 37.976 38.943 0.27 11.27 ? 281  CYS A CA     1 
ATOM   1735 C C      . CYS A 1 98  ? 16.886 39.067 39.237 1.00 10.41 ? 281  CYS A C      1 
ATOM   1736 O O      . CYS A 1 98  ? 16.652 39.426 40.402 1.00 10.49 ? 281  CYS A O      1 
ATOM   1737 C CB     A CYS A 1 98  ? 19.196 38.594 38.486 0.73 11.59 ? 281  CYS A CB     1 
ATOM   1738 C CB     B CYS A 1 98  ? 19.183 38.553 38.336 0.27 12.98 ? 281  CYS A CB     1 
ATOM   1739 S SG     A CYS A 1 98  ? 20.599 37.548 38.421 0.73 12.68 ? 281  CYS A SG     1 
ATOM   1740 S SG     B CYS A 1 98  ? 20.169 39.467 39.446 0.27 15.02 ? 281  CYS A SG     1 
ATOM   1741 H H      A CYS A 1 98  ? 17.861 36.931 37.279 0.73 12.57 ? 281  CYS A H      1 
ATOM   1742 H H      B CYS A 1 98  ? 17.860 36.921 37.279 0.27 12.57 ? 281  CYS A H      1 
ATOM   1743 H HA     A CYS A 1 98  ? 18.069 37.473 39.786 0.73 12.42 ? 281  CYS A HA     1 
ATOM   1744 H HA     B CYS A 1 98  ? 18.114 37.552 39.791 0.27 13.53 ? 281  CYS A HA     1 
ATOM   1745 H HB2    A CYS A 1 98  ? 19.052 38.933 37.588 0.73 13.91 ? 281  CYS A HB2    1 
ATOM   1746 H HB2    B CYS A 1 98  ? 19.723 37.821 38.000 0.27 15.58 ? 281  CYS A HB2    1 
ATOM   1747 H HB3    A CYS A 1 98  ? 19.415 39.325 39.085 0.73 13.91 ? 281  CYS A HB3    1 
ATOM   1748 H HB3    B CYS A 1 98  ? 18.936 39.145 37.609 0.27 15.58 ? 281  CYS A HB3    1 
ATOM   1749 H HG     A CYS A 1 98  ? 20.444 36.742 37.545 0.73 15.21 ? 281  CYS A HG     1 
ATOM   1750 H HG     B CYS A 1 98  ? 21.312 39.422 39.081 0.27 18.02 ? 281  CYS A HG     1 
ATOM   1751 N N      . LEU A 1 99  ? 16.252 39.587 38.182 1.00 11.63 ? 282  LEU A N      1 
ATOM   1752 C CA     . LEU A 1 99  ? 15.268 40.638 38.345 1.00 12.88 ? 282  LEU A CA     1 
ATOM   1753 C C      . LEU A 1 99  ? 14.022 40.131 39.058 1.00 12.34 ? 282  LEU A C      1 
ATOM   1754 O O      . LEU A 1 99  ? 13.437 40.844 39.876 1.00 13.52 ? 282  LEU A O      1 
ATOM   1755 C CB     . LEU A 1 99  ? 14.914 41.224 36.971 1.00 14.92 ? 282  LEU A CB     1 
ATOM   1756 C CG     . LEU A 1 99  ? 16.099 41.965 36.307 1.00 16.60 ? 282  LEU A CG     1 
ATOM   1757 C CD1    . LEU A 1 99  ? 15.893 42.277 34.815 1.00 18.77 ? 282  LEU A CD1    1 
ATOM   1758 C CD2    . LEU A 1 99  ? 16.442 43.286 37.065 1.00 18.55 ? 282  LEU A CD2    1 
ATOM   1759 H H      . LEU A 1 99  ? 16.379 39.344 37.367 1.00 13.95 ? 282  LEU A H      1 
ATOM   1760 H HA     . LEU A 1 99  ? 15.647 41.346 38.889 1.00 15.46 ? 282  LEU A HA     1 
ATOM   1761 H HB2    . LEU A 1 99  ? 14.642 40.503 36.382 1.00 17.91 ? 282  LEU A HB2    1 
ATOM   1762 H HB3    . LEU A 1 99  ? 14.186 41.857 37.078 1.00 17.91 ? 282  LEU A HB3    1 
ATOM   1763 H HG     . LEU A 1 99  ? 16.847 41.350 36.363 1.00 19.92 ? 282  LEU A HG     1 
ATOM   1764 H HD11   . LEU A 1 99  ? 16.660 42.773 34.488 1.00 22.53 ? 282  LEU A HD11   1 
ATOM   1765 H HD12   . LEU A 1 99  ? 15.806 41.443 34.327 1.00 22.53 ? 282  LEU A HD12   1 
ATOM   1766 H HD13   . LEU A 1 99  ? 15.087 42.806 34.711 1.00 22.53 ? 282  LEU A HD13   1 
ATOM   1767 H HD21   . LEU A 1 99  ? 17.173 43.731 36.609 1.00 22.26 ? 282  LEU A HD21   1 
ATOM   1768 H HD22   . LEU A 1 99  ? 15.659 43.859 37.072 1.00 22.26 ? 282  LEU A HD22   1 
ATOM   1769 H HD23   . LEU A 1 99  ? 16.701 43.071 37.975 1.00 22.26 ? 282  LEU A HD23   1 
ATOM   1770 N N      . GLN A 1 100 ? 13.612 38.891 38.775 1.00 12.68 ? 283  GLN A N      1 
ATOM   1771 C CA     . GLN A 1 100 ? 12.481 38.321 39.508 1.00 13.24 ? 283  GLN A CA     1 
ATOM   1772 C C      . GLN A 1 100 ? 12.796 38.240 41.010 1.00 11.60 ? 283  GLN A C      1 
ATOM   1773 O O      . GLN A 1 100 ? 11.957 38.547 41.854 1.00 11.85 ? 283  GLN A O      1 
ATOM   1774 C CB     . GLN A 1 100 ? 12.088 36.938 38.972 1.00 13.63 ? 283  GLN A CB     1 
ATOM   1775 C CG     . GLN A 1 100 ? 11.346 36.924 37.647 1.00 15.41 ? 283  GLN A CG     1 
ATOM   1776 C CD     . GLN A 1 100 ? 11.026 35.511 37.195 1.00 17.34 ? 283  GLN A CD     1 
ATOM   1777 O OE1    . GLN A 1 100 ? 11.675 34.996 36.311 1.00 19.13 ? 283  GLN A OE1    1 
ATOM   1778 N NE2    . GLN A 1 100 ? 10.021 34.882 37.804 1.00 18.92 ? 283  GLN A NE2    1 
ATOM   1779 H H      . GLN A 1 100 ? 13.961 38.375 38.182 1.00 15.22 ? 283  GLN A H      1 
ATOM   1780 H HA     . GLN A 1 100 ? 11.714 38.899 39.370 1.00 15.89 ? 283  GLN A HA     1 
ATOM   1781 H HB2    . GLN A 1 100 ? 12.898 36.419 38.852 1.00 16.36 ? 283  GLN A HB2    1 
ATOM   1782 H HB3    . GLN A 1 100 ? 11.514 36.511 39.626 1.00 16.36 ? 283  GLN A HB3    1 
ATOM   1783 H HG2    . GLN A 1 100 ? 10.511 37.409 37.743 1.00 18.49 ? 283  GLN A HG2    1 
ATOM   1784 H HG3    . GLN A 1 100 ? 11.897 37.343 36.967 1.00 18.49 ? 283  GLN A HG3    1 
ATOM   1785 H HE21   . GLN A 1 100 ? 9.581  35.278 38.428 1.00 22.70 ? 283  GLN A HE21   1 
ATOM   1786 H HE22   . GLN A 1 100 ? 9.812  34.080 37.573 1.00 22.70 ? 283  GLN A HE22   1 
ATOM   1787 N N      . VAL A 1 101 ? 14.026 37.850 41.371 1.00 10.35 ? 284  VAL A N      1 
ATOM   1788 C CA     . VAL A 1 101 ? 14.356 37.748 42.783 1.00 10.72 ? 284  VAL A CA     1 
ATOM   1789 C C      . VAL A 1 101 ? 14.425 39.131 43.438 1.00 11.20 ? 284  VAL A C      1 
ATOM   1790 O O      . VAL A 1 101 ? 13.931 39.321 44.542 1.00 11.44 ? 284  VAL A O      1 
ATOM   1791 C CB     . VAL A 1 101 ? 15.679 36.967 42.943 1.00 10.01 ? 284  VAL A CB     1 
ATOM   1792 C CG1    . VAL A 1 101 ? 16.239 37.078 44.368 1.00 11.35 ? 284  VAL A CG1    1 
ATOM   1793 C CG2    . VAL A 1 101 ? 15.476 35.491 42.583 1.00 10.96 ? 284  VAL A CG2    1 
ATOM   1794 H H      . VAL A 1 101 ? 14.662 37.646 40.829 1.00 12.42 ? 284  VAL A H      1 
ATOM   1795 H HA     . VAL A 1 101 ? 13.649 37.260 43.234 1.00 12.86 ? 284  VAL A HA     1 
ATOM   1796 H HB     . VAL A 1 101 ? 16.327 37.359 42.338 1.00 12.01 ? 284  VAL A HB     1 
ATOM   1797 H HG11   . VAL A 1 101 ? 17.031 36.523 44.440 1.00 13.62 ? 284  VAL A HG11   1 
ATOM   1798 H HG12   . VAL A 1 101 ? 16.467 38.004 44.546 1.00 13.62 ? 284  VAL A HG12   1 
ATOM   1799 H HG13   . VAL A 1 101 ? 15.565 36.777 44.997 1.00 13.62 ? 284  VAL A HG13   1 
ATOM   1800 H HG21   . VAL A 1 101 ? 16.308 35.014 42.729 1.00 13.16 ? 284  VAL A HG21   1 
ATOM   1801 H HG22   . VAL A 1 101 ? 14.779 35.122 43.147 1.00 13.16 ? 284  VAL A HG22   1 
ATOM   1802 H HG23   . VAL A 1 101 ? 15.217 35.427 41.651 1.00 13.16 ? 284  VAL A HG23   1 
ATOM   1803 N N      . LEU A 1 102 ? 15.038 40.101 42.772 1.00 10.83 ? 285  LEU A N      1 
ATOM   1804 C CA     . LEU A 1 102 ? 15.064 41.458 43.307 1.00 11.31 ? 285  LEU A CA     1 
ATOM   1805 C C      . LEU A 1 102 ? 13.655 41.973 43.571 1.00 12.38 ? 285  LEU A C      1 
ATOM   1806 O O      . LEU A 1 102 ? 13.382 42.548 44.636 1.00 12.86 ? 285  LEU A O      1 
ATOM   1807 C CB     . LEU A 1 102 ? 15.793 42.351 42.322 1.00 11.94 ? 285  LEU A CB     1 
ATOM   1808 C CG     . LEU A 1 102 ? 17.321 42.167 42.270 1.00 12.63 ? 285  LEU A CG     1 
ATOM   1809 C CD1    . LEU A 1 102 ? 17.854 42.797 41.031 1.00 12.96 ? 285  LEU A CD1    1 
ATOM   1810 C CD2    . LEU A 1 102 ? 17.991 42.733 43.507 1.00 12.89 ? 285  LEU A CD2    1 
ATOM   1811 H H      . LEU A 1 102 ? 15.440 40.004 42.018 1.00 13.00 ? 285  LEU A H      1 
ATOM   1812 H HA     . LEU A 1 102 ? 15.539 41.468 44.153 1.00 13.57 ? 285  LEU A HA     1 
ATOM   1813 H HB2    . LEU A 1 102 ? 15.448 42.170 41.433 1.00 14.33 ? 285  LEU A HB2    1 
ATOM   1814 H HB3    . LEU A 1 102 ? 15.620 43.275 42.562 1.00 14.33 ? 285  LEU A HB3    1 
ATOM   1815 H HG     . LEU A 1 102 ? 17.530 41.220 42.251 1.00 15.15 ? 285  LEU A HG     1 
ATOM   1816 H HD11   . LEU A 1 102 ? 18.820 42.711 41.023 1.00 15.55 ? 285  LEU A HD11   1 
ATOM   1817 H HD12   . LEU A 1 102 ? 17.475 42.347 40.259 1.00 15.55 ? 285  LEU A HD12   1 
ATOM   1818 H HD13   . LEU A 1 102 ? 17.606 43.735 41.021 1.00 15.55 ? 285  LEU A HD13   1 
ATOM   1819 H HD21   . LEU A 1 102 ? 18.935 42.512 43.484 1.00 15.47 ? 285  LEU A HD21   1 
ATOM   1820 H HD22   . LEU A 1 102 ? 17.877 43.696 43.516 1.00 15.47 ? 285  LEU A HD22   1 
ATOM   1821 H HD23   . LEU A 1 102 ? 17.580 42.344 44.295 1.00 15.47 ? 285  LEU A HD23   1 
ATOM   1822 N N      . GLU A 1 103 ? 12.749 41.776 42.601 1.00 13.68 ? 286  GLU A N      1 
ATOM   1823 C CA     A GLU A 1 103 ? 11.394 42.266 42.796 0.46 15.23 ? 286  GLU A CA     1 
ATOM   1824 C CA     B GLU A 1 103 ? 11.366 42.222 42.752 0.54 14.05 ? 286  GLU A CA     1 
ATOM   1825 C C      . GLU A 1 103 ? 10.707 41.530 43.938 1.00 12.93 ? 286  GLU A C      1 
ATOM   1826 O O      . GLU A 1 103 ? 9.965  42.144 44.702 1.00 14.47 ? 286  GLU A O      1 
ATOM   1827 C CB     A GLU A 1 103 ? 10.566 42.188 41.519 0.46 18.40 ? 286  GLU A CB     1 
ATOM   1828 C CB     B GLU A 1 103 ? 10.603 41.929 41.453 0.54 15.41 ? 286  GLU A CB     1 
ATOM   1829 C CG     A GLU A 1 103 ? 9.091  42.541 41.766 0.46 21.48 ? 286  GLU A CG     1 
ATOM   1830 C CG     B GLU A 1 103 ? 9.068  41.937 41.526 0.54 19.32 ? 286  GLU A CG     1 
ATOM   1831 C CD     A GLU A 1 103 ? 8.882  43.976 42.277 0.46 24.00 ? 286  GLU A CD     1 
ATOM   1832 C CD     B GLU A 1 103 ? 8.409  41.558 40.178 0.54 24.15 ? 286  GLU A CD     1 
ATOM   1833 O OE1    A GLU A 1 103 ? 9.657  44.887 41.915 0.46 22.45 ? 286  GLU A OE1    1 
ATOM   1834 O OE1    B GLU A 1 103 ? 8.884  40.610 39.474 0.54 24.41 ? 286  GLU A OE1    1 
ATOM   1835 O OE2    A GLU A 1 103 ? 7.924  44.203 43.046 0.46 27.53 ? 286  GLU A OE2    1 
ATOM   1836 O OE2    B GLU A 1 103 ? 7.421  42.234 39.823 0.54 28.23 ? 286  GLU A OE2    1 
ATOM   1837 H H      A GLU A 1 103 ? 12.895 41.377 41.854 0.46 16.41 ? 286  GLU A H      1 
ATOM   1838 H H      B GLU A 1 103 ? 12.912 41.388 41.851 0.54 16.41 ? 286  GLU A H      1 
ATOM   1839 H HA     A GLU A 1 103 ? 11.452 43.208 43.022 0.46 18.27 ? 286  GLU A HA     1 
ATOM   1840 H HA     B GLU A 1 103 ? 11.339 43.178 42.913 0.54 16.86 ? 286  GLU A HA     1 
ATOM   1841 H HB2    A GLU A 1 103 ? 10.922 42.814 40.869 0.46 22.08 ? 286  GLU A HB2    1 
ATOM   1842 H HB2    B GLU A 1 103 ? 10.857 42.599 40.799 0.54 18.49 ? 286  GLU A HB2    1 
ATOM   1843 H HB3    A GLU A 1 103 ? 10.607 41.285 41.167 0.46 22.08 ? 286  GLU A HB3    1 
ATOM   1844 H HB3    B GLU A 1 103 ? 10.866 41.048 41.144 0.54 18.49 ? 286  GLU A HB3    1 
ATOM   1845 H HG2    A GLU A 1 103 ? 8.603  42.448 40.932 0.46 25.77 ? 286  GLU A HG2    1 
ATOM   1846 H HG2    B GLU A 1 103 ? 8.780  41.294 42.193 0.54 23.18 ? 286  GLU A HG2    1 
ATOM   1847 H HG3    A GLU A 1 103 ? 8.731  41.933 42.430 0.46 25.77 ? 286  GLU A HG3    1 
ATOM   1848 H HG3    B GLU A 1 103 ? 8.767  42.826 41.770 0.54 23.18 ? 286  GLU A HG3    1 
ATOM   1849 N N      . ALA A 1 104 ? 10.970 40.222 44.106 1.00 11.74 ? 287  ALA A N      1 
ATOM   1850 C CA     . ALA A 1 104 ? 10.322 39.490 45.178 1.00 11.85 ? 287  ALA A CA     1 
ATOM   1851 C C      . ALA A 1 104 ? 10.744 39.974 46.548 1.00 11.84 ? 287  ALA A C      1 
ATOM   1852 O O      . ALA A 1 104 ? 9.999  39.786 47.515 1.00 12.71 ? 287  ALA A O      1 
ATOM   1853 C CB     . ALA A 1 104 ? 10.664 38.002 45.047 1.00 12.17 ? 287  ALA A CB     1 
ATOM   1854 H H      . ALA A 1 104 ? 11.507 39.758 43.620 1.00 14.09 ? 287  ALA A H      1 
ATOM   1855 H HA     . ALA A 1 104 ? 9.362  39.608 45.101 1.00 14.22 ? 287  ALA A HA     1 
ATOM   1856 H HB1    . ALA A 1 104 ? 10.221 37.513 45.758 1.00 14.60 ? 287  ALA A HB1    1 
ATOM   1857 H HB2    . ALA A 1 104 ? 10.357 37.682 44.184 1.00 14.60 ? 287  ALA A HB2    1 
ATOM   1858 H HB3    . ALA A 1 104 ? 11.625 37.891 45.119 1.00 14.60 ? 287  ALA A HB3    1 
ATOM   1859 N N      . TYR A 1 105 ? 11.908 40.639 46.647 1.00 11.97 ? 288  TYR A N      1 
ATOM   1860 C CA     . TYR A 1 105 ? 12.423 41.165 47.902 1.00 12.44 ? 288  TYR A CA     1 
ATOM   1861 C C      . TYR A 1 105 ? 12.297 42.685 47.979 1.00 13.81 ? 288  TYR A C      1 
ATOM   1862 O O      . TYR A 1 105 ? 12.902 43.320 48.855 1.00 14.45 ? 288  TYR A O      1 
ATOM   1863 C CB     . TYR A 1 105 ? 13.855 40.689 48.142 1.00 12.20 ? 288  TYR A CB     1 
ATOM   1864 C CG     . TYR A 1 105 ? 13.864 39.248 48.609 1.00 12.19 ? 288  TYR A CG     1 
ATOM   1865 C CD1    . TYR A 1 105 ? 13.696 38.218 47.704 1.00 12.11 ? 288  TYR A CD1    1 
ATOM   1866 C CD2    . TYR A 1 105 ? 14.030 38.931 49.942 1.00 13.82 ? 288  TYR A CD2    1 
ATOM   1867 C CE1    . TYR A 1 105 ? 13.694 36.896 48.114 1.00 13.71 ? 288  TYR A CE1    1 
ATOM   1868 C CE2    . TYR A 1 105 ? 13.996 37.608 50.361 1.00 15.53 ? 288  TYR A CE2    1 
ATOM   1869 C CZ     . TYR A 1 105 ? 13.851 36.609 49.443 1.00 15.26 ? 288  TYR A CZ     1 
ATOM   1870 O OH     . TYR A 1 105 ? 13.856 35.291 49.845 1.00 17.62 ? 288  TYR A OH     1 
ATOM   1871 H H      . TYR A 1 105 ? 12.423 40.798 45.977 1.00 14.36 ? 288  TYR A H      1 
ATOM   1872 H HA     . TYR A 1 105 ? 11.902 40.805 48.637 1.00 14.93 ? 288  TYR A HA     1 
ATOM   1873 H HB2    . TYR A 1 105 ? 14.360 40.750 47.316 1.00 14.64 ? 288  TYR A HB2    1 
ATOM   1874 H HB3    . TYR A 1 105 ? 14.270 41.239 48.825 1.00 14.64 ? 288  TYR A HB3    1 
ATOM   1875 H HD1    . TYR A 1 105 ? 13.582 38.417 46.803 1.00 14.54 ? 288  TYR A HD1    1 
ATOM   1876 H HD2    . TYR A 1 105 ? 14.167 39.608 50.565 1.00 16.59 ? 288  TYR A HD2    1 
ATOM   1877 H HE1    . TYR A 1 105 ? 13.588 36.211 47.494 1.00 16.45 ? 288  TYR A HE1    1 
ATOM   1878 H HE2    . TYR A 1 105 ? 14.072 37.403 51.265 1.00 18.64 ? 288  TYR A HE2    1 
ATOM   1879 H HH     . TYR A 1 105 ? 13.933 34.788 49.177 1.00 21.14 ? 288  TYR A HH     1 
ATOM   1880 N N      . ASN A 1 106 ? 11.493 43.282 47.083 1.00 13.15 ? 289  ASN A N      1 
ATOM   1881 C CA     . ASN A 1 106 ? 11.217 44.729 47.154 1.00 14.83 ? 289  ASN A CA     1 
ATOM   1882 C C      . ASN A 1 106 ? 12.470 45.577 46.989 1.00 14.05 ? 289  ASN A C      1 
ATOM   1883 O O      . ASN A 1 106 ? 12.611 46.632 47.603 1.00 16.70 ? 289  ASN A O      1 
ATOM   1884 C CB     . ASN A 1 106 ? 10.466 45.076 48.445 1.00 19.58 ? 289  ASN A CB     1 
ATOM   1885 C CG     . ASN A 1 106 ? 9.037  44.615 48.420 1.00 26.10 ? 289  ASN A CG     1 
ATOM   1886 O OD1    . ASN A 1 106 ? 8.625  43.772 49.207 1.00 32.09 ? 289  ASN A OD1    1 
ATOM   1887 N ND2    . ASN A 1 106 ? 8.263  45.191 47.526 1.00 27.77 ? 289  ASN A ND2    1 
ATOM   1888 H H      . ASN A 1 106 ? 11.101 42.877 46.434 1.00 15.78 ? 289  ASN A H      1 
ATOM   1889 H HA     . ASN A 1 106 ? 10.648 44.958 46.402 1.00 17.79 ? 289  ASN A HA     1 
ATOM   1890 H HB2    . ASN A 1 106 ? 10.908 44.646 49.194 1.00 23.50 ? 289  ASN A HB2    1 
ATOM   1891 H HB3    . ASN A 1 106 ? 10.470 46.038 48.565 1.00 23.50 ? 289  ASN A HB3    1 
ATOM   1892 H HD21   . ASN A 1 106 ? 7.435  44.967 47.465 1.00 33.32 ? 289  ASN A HD21   1 
ATOM   1893 H HD22   . ASN A 1 106 ? 8.586  45.791 47.001 1.00 33.32 ? 289  ASN A HD22   1 
ATOM   1894 N N      . VAL A 1 107 ? 13.368 45.148 46.120 1.00 10.95 ? 290  VAL A N      1 
ATOM   1895 C CA     . VAL A 1 107 ? 14.552 45.922 45.762 1.00 11.35 ? 290  VAL A CA     1 
ATOM   1896 C C      . VAL A 1 107 ? 14.253 46.702 44.493 1.00 11.65 ? 290  VAL A C      1 
ATOM   1897 O O      . VAL A 1 107 ? 13.898 46.093 43.485 1.00 12.07 ? 290  VAL A O      1 
ATOM   1898 C CB     . VAL A 1 107 ? 15.781 45.021 45.550 1.00 11.28 ? 290  VAL A CB     1 
ATOM   1899 C CG1    . VAL A 1 107 ? 16.983 45.896 45.141 1.00 11.72 ? 290  VAL A CG1    1 
ATOM   1900 C CG2    . VAL A 1 107 ? 16.107 44.223 46.835 1.00 12.33 ? 290  VAL A CG2    1 
ATOM   1901 H H      . VAL A 1 107 ? 13.315 44.393 45.712 1.00 13.13 ? 290  VAL A H      1 
ATOM   1902 H HA     . VAL A 1 107 ? 14.744 46.549 46.477 1.00 13.62 ? 290  VAL A HA     1 
ATOM   1903 H HB     . VAL A 1 107 ? 15.594 44.380 44.846 1.00 13.54 ? 290  VAL A HB     1 
ATOM   1904 H HG11   . VAL A 1 107 ? 17.757 45.327 45.008 1.00 14.07 ? 290  VAL A HG11   1 
ATOM   1905 H HG12   . VAL A 1 107 ? 16.770 46.361 44.316 1.00 14.07 ? 290  VAL A HG12   1 
ATOM   1906 H HG13   . VAL A 1 107 ? 17.161 46.538 45.846 1.00 14.07 ? 290  VAL A HG13   1 
ATOM   1907 H HG21   . VAL A 1 107 ? 16.864 43.642 46.662 1.00 14.79 ? 290  VAL A HG21   1 
ATOM   1908 H HG22   . VAL A 1 107 ? 16.323 44.845 47.547 1.00 14.79 ? 290  VAL A HG22   1 
ATOM   1909 H HG23   . VAL A 1 107 ? 15.333 43.693 47.082 1.00 14.79 ? 290  VAL A HG23   1 
ATOM   1910 N N      . PRO A 1 108 ? 14.421 48.025 44.495 1.00 11.93 ? 291  PRO A N      1 
ATOM   1911 C CA     . PRO A 1 108 ? 14.056 48.807 43.303 1.00 12.17 ? 291  PRO A CA     1 
ATOM   1912 C C      . PRO A 1 108 ? 14.975 48.501 42.135 1.00 11.25 ? 291  PRO A C      1 
ATOM   1913 O O      . PRO A 1 108 ? 16.195 48.339 42.315 1.00 11.94 ? 291  PRO A O      1 
ATOM   1914 C CB     . PRO A 1 108 ? 14.174 50.257 43.772 1.00 15.23 ? 291  PRO A CB     1 
ATOM   1915 C CG     . PRO A 1 108 ? 15.080 50.209 44.924 1.00 19.11 ? 291  PRO A CG     1 
ATOM   1916 C CD     . PRO A 1 108 ? 14.845 48.902 45.607 1.00 13.99 ? 291  PRO A CD     1 
ATOM   1917 H HA     . PRO A 1 108 ? 13.138 48.634 43.041 1.00 14.60 ? 291  PRO A HA     1 
ATOM   1918 H HB2    . PRO A 1 108 ? 14.543 50.804 43.061 1.00 18.27 ? 291  PRO A HB2    1 
ATOM   1919 H HB3    . PRO A 1 108 ? 13.301 50.593 44.030 1.00 18.27 ? 291  PRO A HB3    1 
ATOM   1920 H HG2    . PRO A 1 108 ? 15.998 50.271 44.616 1.00 22.93 ? 291  PRO A HG2    1 
ATOM   1921 H HG3    . PRO A 1 108 ? 14.881 50.946 45.523 1.00 22.93 ? 291  PRO A HG3    1 
ATOM   1922 H HD2    . PRO A 1 108 ? 15.660 48.573 46.018 1.00 16.79 ? 291  PRO A HD2    1 
ATOM   1923 H HD3    . PRO A 1 108 ? 14.145 48.980 46.274 1.00 16.79 ? 291  PRO A HD3    1 
ATOM   1924 N N      . THR A 1 109 ? 14.389 48.435 40.935 1.00 12.19 ? 292  THR A N      1 
ATOM   1925 C CA     . THR A 1 109 ? 15.102 48.216 39.687 1.00 13.12 ? 292  THR A CA     1 
ATOM   1926 C C      . THR A 1 109 ? 14.554 49.194 38.659 1.00 12.22 ? 292  THR A C      1 
ATOM   1927 O O      . THR A 1 109 ? 13.429 49.682 38.821 1.00 12.82 ? 292  THR A O      1 
ATOM   1928 C CB     . THR A 1 109 ? 14.914 46.780 39.171 1.00 13.75 ? 292  THR A CB     1 
ATOM   1929 O OG1    . THR A 1 109 ? 13.499 46.490 39.060 1.00 15.49 ? 292  THR A OG1    1 
ATOM   1930 C CG2    . THR A 1 109 ? 15.593 45.796 40.085 1.00 14.23 ? 292  THR A CG2    1 
ATOM   1931 H H      . THR A 1 109 ? 13.540 48.520 40.820 1.00 14.63 ? 292  THR A H      1 
ATOM   1932 H HA     . THR A 1 109 ? 16.051 48.374 39.813 1.00 15.75 ? 292  THR A HA     1 
ATOM   1933 H HB     . THR A 1 109 ? 15.319 46.686 38.295 1.00 16.50 ? 292  THR A HB     1 
ATOM   1934 H HG1    . THR A 1 109 ? 13.131 46.560 39.812 1.00 18.58 ? 292  THR A HG1    1 
ATOM   1935 H HG21   . THR A 1 109 ? 15.459 44.893 39.758 1.00 17.08 ? 292  THR A HG21   1 
ATOM   1936 H HG22   . THR A 1 109 ? 16.545 45.980 40.121 1.00 17.08 ? 292  THR A HG22   1 
ATOM   1937 H HG23   . THR A 1 109 ? 15.225 45.866 40.980 1.00 17.08 ? 292  THR A HG23   1 
ATOM   1938 N N      . PRO A 1 110 ? 15.274 49.465 37.576 1.00 12.62 ? 293  PRO A N      1 
ATOM   1939 C CA     . PRO A 1 110 ? 14.740 50.432 36.571 1.00 13.63 ? 293  PRO A CA     1 
ATOM   1940 C C      . PRO A 1 110 ? 13.516 49.877 35.866 1.00 14.01 ? 293  PRO A C      1 
ATOM   1941 O O      . PRO A 1 110 ? 13.366 48.658 35.720 1.00 14.25 ? 293  PRO A O      1 
ATOM   1942 C CB     . PRO A 1 110 ? 15.891 50.578 35.569 1.00 15.24 ? 293  PRO A CB     1 
ATOM   1943 C CG     . PRO A 1 110 ? 17.137 50.211 36.359 1.00 15.29 ? 293  PRO A CG     1 
ATOM   1944 C CD     . PRO A 1 110 ? 16.662 49.066 37.253 1.00 13.81 ? 293  PRO A CD     1 
ATOM   1945 H HA     . PRO A 1 110 ? 14.537 51.280 36.996 1.00 16.36 ? 293  PRO A HA     1 
ATOM   1946 H HB2    . PRO A 1 110 ? 15.760 49.971 34.823 1.00 18.29 ? 293  PRO A HB2    1 
ATOM   1947 H HB3    . PRO A 1 110 ? 15.938 51.492 35.249 1.00 18.29 ? 293  PRO A HB3    1 
ATOM   1948 H HG2    . PRO A 1 110 ? 17.843 49.922 35.760 1.00 18.35 ? 293  PRO A HG2    1 
ATOM   1949 H HG3    . PRO A 1 110 ? 17.437 50.968 36.885 1.00 18.35 ? 293  PRO A HG3    1 
ATOM   1950 H HD2    . PRO A 1 110 ? 16.680 48.222 36.775 1.00 16.57 ? 293  PRO A HD2    1 
ATOM   1951 H HD3    . PRO A 1 110 ? 17.203 49.005 38.056 1.00 16.57 ? 293  PRO A HD3    1 
ATOM   1952 N N      . PRO A 1 111 ? 12.646 50.742 35.347 1.00 14.17 ? 294  PRO A N      1 
ATOM   1953 C CA     . PRO A 1 111 ? 11.593 50.276 34.436 1.00 15.41 ? 294  PRO A CA     1 
ATOM   1954 C C      . PRO A 1 111 ? 12.152 49.397 33.334 1.00 14.90 ? 294  PRO A C      1 
ATOM   1955 O O      . PRO A 1 111 ? 13.225 49.673 32.790 1.00 14.46 ? 294  PRO A O      1 
ATOM   1956 C CB     . PRO A 1 111 ? 11.060 51.593 33.853 1.00 16.56 ? 294  PRO A CB     1 
ATOM   1957 C CG     . PRO A 1 111 ? 11.312 52.595 34.948 1.00 17.82 ? 294  PRO A CG     1 
ATOM   1958 C CD     . PRO A 1 111 ? 12.640 52.212 35.493 1.00 16.79 ? 294  PRO A CD     1 
ATOM   1959 H HA     . PRO A 1 111 ? 10.903 49.798 34.921 1.00 18.49 ? 294  PRO A HA     1 
ATOM   1960 H HB2    . PRO A 1 111 ? 11.546 51.824 33.046 1.00 19.88 ? 294  PRO A HB2    1 
ATOM   1961 H HB3    . PRO A 1 111 ? 10.113 51.515 33.659 1.00 19.88 ? 294  PRO A HB3    1 
ATOM   1962 H HG2    . PRO A 1 111 ? 11.331 53.493 34.582 1.00 21.39 ? 294  PRO A HG2    1 
ATOM   1963 H HG3    . PRO A 1 111 ? 10.623 52.529 35.628 1.00 21.39 ? 294  PRO A HG3    1 
ATOM   1964 H HD2    . PRO A 1 111 ? 13.355 52.615 34.978 1.00 20.15 ? 294  PRO A HD2    1 
ATOM   1965 H HD3    . PRO A 1 111 ? 12.718 52.468 36.426 1.00 20.15 ? 294  PRO A HD3    1 
ATOM   1966 N N      . ARG A 1 112 ? 11.386 48.367 32.948 1.00 14.29 ? 295  ARG A N      1 
ATOM   1967 C CA     . ARG A 1 112 ? 11.870 47.493 31.901 1.00 13.50 ? 295  ARG A CA     1 
ATOM   1968 C C      . ARG A 1 112 ? 10.746 46.868 31.084 1.00 13.80 ? 295  ARG A C      1 
ATOM   1969 O O      . ARG A 1 112 ? 9.592  46.777 31.523 1.00 16.16 ? 295  ARG A O      1 
ATOM   1970 C CB     . ARG A 1 112 ? 12.710 46.355 32.465 1.00 15.07 ? 295  ARG A CB     1 
ATOM   1971 C CG     . ARG A 1 112 ? 11.944 45.489 33.417 1.00 17.65 ? 295  ARG A CG     1 
ATOM   1972 C CD     . ARG A 1 112 ? 12.774 44.257 33.715 1.00 20.16 ? 295  ARG A CD     1 
ATOM   1973 N NE     . ARG A 1 112 ? 12.108 43.371 34.656 1.00 22.61 ? 295  ARG A NE     1 
ATOM   1974 C CZ     . ARG A 1 112 ? 12.162 43.540 35.968 1.00 21.37 ? 295  ARG A CZ     1 
ATOM   1975 N NH1    . ARG A 1 112 ? 12.912 44.476 36.499 1.00 19.26 ? 295  ARG A NH1    1 
ATOM   1976 N NH2    . ARG A 1 112 ? 11.443 42.753 36.758 1.00 24.87 ? 295  ARG A NH2    1 
ATOM   1977 H H      . ARG A 1 112 ? 10.613 48.170 33.271 1.00 17.15 ? 295  ARG A H      1 
ATOM   1978 H HA     . ARG A 1 112 ? 12.386 48.060 31.307 1.00 16.20 ? 295  ARG A HA     1 
ATOM   1979 H HB2    . ARG A 1 112 ? 13.020 45.798 31.734 1.00 18.08 ? 295  ARG A HB2    1 
ATOM   1980 H HB3    . ARG A 1 112 ? 13.469 46.728 32.942 1.00 18.08 ? 295  ARG A HB3    1 
ATOM   1981 H HG2    . ARG A 1 112 ? 11.778 45.969 34.243 1.00 21.19 ? 295  ARG A HG2    1 
ATOM   1982 H HG3    . ARG A 1 112 ? 11.103 45.217 33.016 1.00 21.19 ? 295  ARG A HG3    1 
ATOM   1983 H HD2    . ARG A 1 112 ? 12.926 43.767 32.892 1.00 24.19 ? 295  ARG A HD2    1 
ATOM   1984 H HD3    . ARG A 1 112 ? 13.621 44.528 34.101 1.00 24.19 ? 295  ARG A HD3    1 
ATOM   1985 H HE     . ARG A 1 112 ? 11.658 42.706 34.346 1.00 27.13 ? 295  ARG A HE     1 
ATOM   1986 H HH11   . ARG A 1 112 ? 13.379 44.992 35.993 1.00 23.12 ? 295  ARG A HH11   1 
ATOM   1987 H HH12   . ARG A 1 112 ? 12.937 44.574 37.353 1.00 23.12 ? 295  ARG A HH12   1 
ATOM   1988 H HH21   . ARG A 1 112 ? 10.946 42.139 36.417 1.00 29.85 ? 295  ARG A HH21   1 
ATOM   1989 H HH22   . ARG A 1 112 ? 11.473 42.857 37.611 1.00 29.85 ? 295  ARG A HH22   1 
ATOM   1990 N N      . LEU A 1 113 ? 11.140 46.433 29.896 1.00 14.00 ? 296  LEU A N      1 
ATOM   1991 C CA     . LEU A 1 113 ? 10.389 45.496 29.059 1.00 15.33 ? 296  LEU A CA     1 
ATOM   1992 C C      . LEU A 1 113 ? 11.326 44.330 28.743 1.00 14.74 ? 296  LEU A C      1 
ATOM   1993 O O      . LEU A 1 113 ? 12.531 44.426 28.942 1.00 14.65 ? 296  LEU A O      1 
ATOM   1994 C CB     . LEU A 1 113 ? 9.938  46.134 27.737 1.00 16.85 ? 296  LEU A CB     1 
ATOM   1995 C CG     . LEU A 1 113 ? 9.058  47.366 27.815 1.00 18.95 ? 296  LEU A CG     1 
ATOM   1996 C CD1    . LEU A 1 113 ? 8.821  47.943 26.403 1.00 20.25 ? 296  LEU A CD1    1 
ATOM   1997 C CD2    . LEU A 1 113 ? 7.744  47.024 28.503 1.00 20.93 ? 296  LEU A CD2    1 
ATOM   1998 H H      . LEU A 1 113 ? 11.878 46.677 29.529 1.00 16.80 ? 296  LEU A H      1 
ATOM   1999 H HA     . LEU A 1 113 ? 9.594  45.200 29.529 1.00 18.40 ? 296  LEU A HA     1 
ATOM   2000 H HB2    . LEU A 1 113 ? 10.734 46.390 27.245 1.00 20.22 ? 296  LEU A HB2    1 
ATOM   2001 H HB3    . LEU A 1 113 ? 9.441  45.466 27.240 1.00 20.22 ? 296  LEU A HB3    1 
ATOM   2002 H HG     . LEU A 1 113 ? 9.498  48.053 28.340 1.00 22.74 ? 296  LEU A HG     1 
ATOM   2003 H HD11   . LEU A 1 113 ? 8.272  48.739 26.476 1.00 24.31 ? 296  LEU A HD11   1 
ATOM   2004 H HD12   . LEU A 1 113 ? 9.677  48.166 26.006 1.00 24.31 ? 296  LEU A HD12   1 
ATOM   2005 H HD13   . LEU A 1 113 ? 8.368  47.277 25.862 1.00 24.31 ? 296  LEU A HD13   1 
ATOM   2006 H HD21   . LEU A 1 113 ? 7.189  47.819 28.538 1.00 25.11 ? 296  LEU A HD21   1 
ATOM   2007 H HD22   . LEU A 1 113 ? 7.295  46.328 27.998 1.00 25.11 ? 296  LEU A HD22   1 
ATOM   2008 H HD23   . LEU A 1 113 ? 7.930  46.711 29.402 1.00 25.11 ? 296  LEU A HD23   1 
ATOM   2009 N N      . GLU A 1 114 ? 10.773 43.217 28.254 1.00 15.61 ? 297  GLU A N      1 
ATOM   2010 C CA     . GLU A 1 114 ? 11.582 42.041 27.949 1.00 15.49 ? 297  GLU A CA     1 
ATOM   2011 C C      . GLU A 1 114 ? 11.120 41.439 26.636 1.00 16.00 ? 297  GLU A C      1 
ATOM   2012 O O      . GLU A 1 114 ? 9.910  41.374 26.380 1.00 17.50 ? 297  GLU A O      1 
ATOM   2013 C CB     . GLU A 1 114 ? 11.455 40.949 29.032 1.00 16.28 ? 297  GLU A CB     1 
ATOM   2014 C CG     . GLU A 1 114 ? 11.957 41.417 30.404 1.00 17.95 ? 297  GLU A CG     1 
ATOM   2015 C CD     . GLU A 1 114 ? 12.061 40.346 31.469 1.00 19.19 ? 297  GLU A CD     1 
ATOM   2016 O OE1    . GLU A 1 114 ? 11.741 39.158 31.217 1.00 20.56 ? 297  GLU A OE1    1 
ATOM   2017 O OE2    . GLU A 1 114 ? 12.493 40.718 32.587 1.00 18.95 ? 297  GLU A OE2    1 
ATOM   2018 H H      . GLU A 1 114 ? 9.934  43.122 28.092 1.00 18.73 ? 297  GLU A H      1 
ATOM   2019 H HA     . GLU A 1 114 ? 12.509 42.319 27.880 1.00 18.59 ? 297  GLU A HA     1 
ATOM   2020 H HB2    . GLU A 1 114 ? 10.522 40.700 29.122 1.00 19.53 ? 297  GLU A HB2    1 
ATOM   2021 H HB3    . GLU A 1 114 ? 11.980 40.178 28.766 1.00 19.53 ? 297  GLU A HB3    1 
ATOM   2022 H HG2    . GLU A 1 114 ? 12.843 41.795 30.291 1.00 21.55 ? 297  GLU A HG2    1 
ATOM   2023 H HG3    . GLU A 1 114 ? 11.347 42.093 30.737 1.00 21.55 ? 297  GLU A HG3    1 
ATOM   2024 N N      . ILE A 1 115 ? 12.060 41.001 25.798 1.00 15.67 ? 298  ILE A N      1 
ATOM   2025 C CA     . ILE A 1 115 ? 11.738 40.243 24.579 1.00 16.26 ? 298  ILE A CA     1 
ATOM   2026 C C      . ILE A 1 115 ? 12.529 38.950 24.647 1.00 16.84 ? 298  ILE A C      1 
ATOM   2027 O O      . ILE A 1 115 ? 13.729 38.927 24.351 1.00 17.44 ? 298  ILE A O      1 
ATOM   2028 C CB     . ILE A 1 115 ? 12.043 41.016 23.294 1.00 17.60 ? 298  ILE A CB     1 
ATOM   2029 C CG1    . ILE A 1 115 ? 11.275 42.332 23.242 1.00 18.44 ? 298  ILE A CG1    1 
ATOM   2030 C CG2    . ILE A 1 115 ? 11.644 40.163 22.096 1.00 19.81 ? 298  ILE A CG2    1 
ATOM   2031 C CD1    . ILE A 1 115 ? 11.648 43.229 22.057 1.00 19.16 ? 298  ILE A CD1    1 
ATOM   2032 H H      . ILE A 1 115 ? 12.902 41.131 25.914 1.00 18.80 ? 298  ILE A H      1 
ATOM   2033 H HA     . ILE A 1 115 ? 10.793 40.026 24.580 1.00 19.51 ? 298  ILE A HA     1 
ATOM   2034 H HB     . ILE A 1 115 ? 12.993 41.215 23.278 1.00 21.13 ? 298  ILE A HB     1 
ATOM   2035 H HG12   . ILE A 1 115 ? 10.327 42.136 23.176 1.00 22.13 ? 298  ILE A HG12   1 
ATOM   2036 H HG13   . ILE A 1 115 ? 11.454 42.829 24.056 1.00 22.13 ? 298  ILE A HG13   1 
ATOM   2037 H HG21   . ILE A 1 115 ? 11.890 40.628 21.281 1.00 23.78 ? 298  ILE A HG21   1 
ATOM   2038 H HG22   . ILE A 1 115 ? 12.108 39.313 22.146 1.00 23.78 ? 298  ILE A HG22   1 
ATOM   2039 H HG23   . ILE A 1 115 ? 10.685 40.018 22.118 1.00 23.78 ? 298  ILE A HG23   1 
ATOM   2040 H HD11   . ILE A 1 115 ? 11.136 44.052 22.111 1.00 23.00 ? 298  ILE A HD11   1 
ATOM   2041 H HD12   . ILE A 1 115 ? 12.597 43.427 22.097 1.00 23.00 ? 298  ILE A HD12   1 
ATOM   2042 H HD13   . ILE A 1 115 ? 11.441 42.764 21.232 1.00 23.00 ? 298  ILE A HD13   1 
ATOM   2043 N N      . SER A 1 116 ? 11.863 37.874 25.059 1.00 17.70 ? 299  SER A N      1 
ATOM   2044 C CA     . SER A 1 116 ? 12.494 36.566 25.170 1.00 17.90 ? 299  SER A CA     1 
ATOM   2045 C C      . SER A 1 116 ? 12.129 35.720 23.956 1.00 18.51 ? 299  SER A C      1 
ATOM   2046 O O      . SER A 1 116 ? 10.944 35.592 23.623 1.00 19.32 ? 299  SER A O      1 
ATOM   2047 C CB     . SER A 1 116 ? 12.021 35.838 26.420 1.00 19.10 ? 299  SER A CB     1 
ATOM   2048 O OG     . SER A 1 116 ? 12.584 36.425 27.580 1.00 18.65 ? 299  SER A OG     1 
ATOM   2049 H H      . SER A 1 116 ? 11.033 37.879 25.282 1.00 21.24 ? 299  SER A H      1 
ATOM   2050 H HA     . SER A 1 116 ? 13.456 36.686 25.209 1.00 21.48 ? 299  SER A HA     1 
ATOM   2051 H HB2    . SER A 1 116 ? 11.055 35.895 26.473 1.00 22.92 ? 299  SER A HB2    1 
ATOM   2052 H HB3    . SER A 1 116 ? 12.297 34.910 26.369 1.00 22.92 ? 299  SER A HB3    1 
ATOM   2053 H HG     . SER A 1 116 ? 12.320 37.219 27.658 1.00 22.39 ? 299  SER A HG     1 
ATOM   2054 N N      . ARG A 1 117 ? 13.143 35.176 23.275 1.00 19.14 ? 300  ARG A N      1 
ATOM   2055 C CA     . ARG A 1 117 ? 12.945 34.294 22.118 1.00 20.14 ? 300  ARG A CA     1 
ATOM   2056 C C      . ARG A 1 117 ? 13.392 32.850 22.370 1.00 20.89 ? 300  ARG A C      1 
ATOM   2057 O O      . ARG A 1 117 ? 13.372 32.024 21.451 1.00 23.64 ? 300  ARG A O      1 
ATOM   2058 C CB     . ARG A 1 117 ? 13.693 34.851 20.904 1.00 21.29 ? 300  ARG A CB     1 
ATOM   2059 C CG     . ARG A 1 117 ? 13.251 36.242 20.466 1.00 23.34 ? 300  ARG A CG     1 
ATOM   2060 C CD     . ARG A 1 117 ? 13.893 36.681 19.172 1.00 25.43 ? 300  ARG A CD     1 
ATOM   2061 N NE     . ARG A 1 117 ? 13.400 37.996 18.768 1.00 25.94 ? 300  ARG A NE     1 
ATOM   2062 C CZ     . ARG A 1 117 ? 13.840 39.161 19.227 1.00 24.64 ? 300  ARG A CZ     1 
ATOM   2063 N NH1    . ARG A 1 117 ? 14.791 39.228 20.138 1.00 24.20 ? 300  ARG A NH1    1 
ATOM   2064 N NH2    . ARG A 1 117 ? 13.305 40.282 18.759 1.00 25.24 ? 300  ARG A NH2    1 
ATOM   2065 H H      . ARG A 1 117 ? 13.971 35.305 23.467 1.00 22.96 ? 300  ARG A H      1 
ATOM   2066 H HA     . ARG A 1 117 ? 11.996 34.273 21.921 1.00 24.16 ? 300  ARG A HA     1 
ATOM   2067 H HB2    . ARG A 1 117 ? 14.638 34.899 21.120 1.00 25.54 ? 300  ARG A HB2    1 
ATOM   2068 H HB3    . ARG A 1 117 ? 13.554 34.251 20.155 1.00 25.54 ? 300  ARG A HB3    1 
ATOM   2069 H HG2    . ARG A 1 117 ? 12.290 36.243 20.338 1.00 28.01 ? 300  ARG A HG2    1 
ATOM   2070 H HG3    . ARG A 1 117 ? 13.495 36.882 21.152 1.00 28.01 ? 300  ARG A HG3    1 
ATOM   2071 H HD2    . ARG A 1 117 ? 14.854 36.735 19.289 1.00 30.51 ? 300  ARG A HD2    1 
ATOM   2072 H HD3    . ARG A 1 117 ? 13.679 36.044 18.472 1.00 30.51 ? 300  ARG A HD3    1 
ATOM   2073 H HE     . ARG A 1 117 ? 12.770 38.017 18.183 1.00 31.12 ? 300  ARG A HE     1 
ATOM   2074 H HH11   . ARG A 1 117 ? 15.140 38.506 20.449 1.00 29.05 ? 300  ARG A HH11   1 
ATOM   2075 H HH12   . ARG A 1 117 ? 15.061 39.993 20.422 1.00 29.05 ? 300  ARG A HH12   1 
ATOM   2076 H HH21   . ARG A 1 117 ? 12.682 40.246 18.167 1.00 30.28 ? 300  ARG A HH21   1 
ATOM   2077 H HH22   . ARG A 1 117 ? 13.581 41.044 19.048 1.00 30.28 ? 300  ARG A HH22   1 
ATOM   2078 N N      . ASP A 1 118 ? 13.791 32.536 23.594 1.00 19.72 ? 301  ASP A N      1 
ATOM   2079 C CA     . ASP A 1 118 ? 14.365 31.240 23.940 1.00 20.61 ? 301  ASP A CA     1 
ATOM   2080 C C      . ASP A 1 118 ? 13.404 30.356 24.715 1.00 21.74 ? 301  ASP A C      1 
ATOM   2081 O O      . ASP A 1 118 ? 13.809 29.295 25.200 1.00 23.92 ? 301  ASP A O      1 
ATOM   2082 C CB     . ASP A 1 118 ? 15.654 31.457 24.751 1.00 20.72 ? 301  ASP A CB     1 
ATOM   2083 C CG     . ASP A 1 118 ? 15.429 32.171 26.085 1.00 20.08 ? 301  ASP A CG     1 
ATOM   2084 O OD1    . ASP A 1 118 ? 14.300 32.639 26.379 1.00 19.55 ? 301  ASP A OD1    1 
ATOM   2085 O OD2    . ASP A 1 118 ? 16.415 32.228 26.865 1.00 20.93 ? 301  ASP A OD2    1 
ATOM   2086 H H      . ASP A 1 118 ? 13.739 33.072 24.264 1.00 23.66 ? 301  ASP A H      1 
ATOM   2087 H HA     . ASP A 1 118 ? 14.588 30.768 23.122 1.00 24.73 ? 301  ASP A HA     1 
ATOM   2088 H HB2    . ASP A 1 118 ? 16.053 30.593 24.941 1.00 24.87 ? 301  ASP A HB2    1 
ATOM   2089 H HB3    . ASP A 1 118 ? 16.266 31.996 24.226 1.00 24.87 ? 301  ASP A HB3    1 
ATOM   2090 N N      . GLY A 1 119 ? 12.163 30.784 24.882 1.00 21.57 ? 302  GLY A N      1 
ATOM   2091 C CA     . GLY A 1 119 ? 11.192 30.071 25.673 1.00 22.59 ? 302  GLY A CA     1 
ATOM   2092 C C      . GLY A 1 119 ? 11.174 30.401 27.152 1.00 21.77 ? 302  GLY A C      1 
ATOM   2093 O O      . GLY A 1 119 ? 10.345 29.841 27.876 1.00 22.51 ? 302  GLY A O      1 
ATOM   2094 H H      . GLY A 1 119 ? 11.854 31.508 24.535 1.00 25.88 ? 302  GLY A H      1 
ATOM   2095 H HA2    . GLY A 1 119 ? 10.309 30.262 25.320 1.00 27.11 ? 302  GLY A HA2    1 
ATOM   2096 H HA3    . GLY A 1 119 ? 11.367 29.120 25.588 1.00 27.11 ? 302  GLY A HA3    1 
ATOM   2097 N N      . GLY A 1 120 ? 12.043 31.301 27.622 1.00 18.80 ? 303  GLY A N      1 
ATOM   2098 C CA     . GLY A 1 120 ? 12.131 31.649 29.022 1.00 17.53 ? 303  GLY A CA     1 
ATOM   2099 C C      . GLY A 1 120 ? 13.311 30.972 29.694 1.00 16.59 ? 303  GLY A C      1 
ATOM   2100 O O      . GLY A 1 120 ? 13.977 30.115 29.099 1.00 17.19 ? 303  GLY A O      1 
ATOM   2101 H H      . GLY A 1 120 ? 12.602 31.729 27.128 1.00 22.56 ? 303  GLY A H      1 
ATOM   2102 H HA2    . GLY A 1 120 ? 12.235 32.609 29.111 1.00 21.03 ? 303  GLY A HA2    1 
ATOM   2103 H HA3    . GLY A 1 120 ? 11.319 31.375 29.476 1.00 21.03 ? 303  GLY A HA3    1 
ATOM   2104 N N      . PRO A 1 121 ? 13.573 31.338 30.956 1.00 16.58 ? 304  PRO A N      1 
ATOM   2105 C CA     . PRO A 1 121 ? 14.694 30.732 31.685 1.00 15.88 ? 304  PRO A CA     1 
ATOM   2106 C C      . PRO A 1 121 ? 14.473 29.256 31.887 1.00 16.08 ? 304  PRO A C      1 
ATOM   2107 O O      . PRO A 1 121 ? 13.353 28.804 32.064 1.00 17.61 ? 304  PRO A O      1 
ATOM   2108 C CB     . PRO A 1 121 ? 14.657 31.425 33.051 1.00 18.23 ? 304  PRO A CB     1 
ATOM   2109 C CG     . PRO A 1 121 ? 13.773 32.584 32.921 1.00 18.39 ? 304  PRO A CG     1 
ATOM   2110 C CD     . PRO A 1 121 ? 12.868 32.360 31.756 1.00 18.02 ? 304  PRO A CD     1 
ATOM   2111 H HA     . PRO A 1 121 ? 15.527 30.909 31.220 1.00 19.06 ? 304  PRO A HA     1 
ATOM   2112 H HB2    . PRO A 1 121 ? 14.313 30.808 33.716 1.00 21.88 ? 304  PRO A HB2    1 
ATOM   2113 H HB3    . PRO A 1 121 ? 15.553 31.707 33.293 1.00 21.88 ? 304  PRO A HB3    1 
ATOM   2114 H HG2    . PRO A 1 121 ? 13.253 32.678 33.734 1.00 22.07 ? 304  PRO A HG2    1 
ATOM   2115 H HG3    . PRO A 1 121 ? 14.311 33.378 32.777 1.00 22.07 ? 304  PRO A HG3    1 
ATOM   2116 H HD2    . PRO A 1 121 ? 12.005 32.031 32.050 1.00 21.62 ? 304  PRO A HD2    1 
ATOM   2117 H HD3    . PRO A 1 121 ? 12.756 33.177 31.246 1.00 21.62 ? 304  PRO A HD3    1 
ATOM   2118 N N      . ARG A 1 122 ? 15.566 28.519 31.935 1.00 17.02 ? 305  ARG A N      1 
ATOM   2119 C CA     . ARG A 1 122 ? 15.517 27.100 32.218 1.00 17.63 ? 305  ARG A CA     1 
ATOM   2120 C C      . ARG A 1 122 ? 15.953 26.865 33.651 1.00 16.72 ? 305  ARG A C      1 
ATOM   2121 O O      . ARG A 1 122 ? 16.797 27.587 34.189 1.00 17.48 ? 305  ARG A O      1 
ATOM   2122 C CB     . ARG A 1 122 ? 16.435 26.352 31.251 1.00 20.08 ? 305  ARG A CB     1 
ATOM   2123 C CG     . ARG A 1 122 ? 16.102 26.453 29.763 1.00 24.75 ? 305  ARG A CG     1 
ATOM   2124 C CD     . ARG A 1 122 ? 14.772 25.818 29.406 1.00 29.31 ? 305  ARG A CD     1 
ATOM   2125 N NE     . ARG A 1 122 ? 14.640 25.567 27.972 1.00 33.37 ? 305  ARG A NE     1 
ATOM   2126 C CZ     . ARG A 1 122 ? 14.225 26.470 27.093 1.00 34.36 ? 305  ARG A CZ     1 
ATOM   2127 N NH1    . ARG A 1 122 ? 13.882 27.702 27.462 1.00 33.03 ? 305  ARG A NH1    1 
ATOM   2128 N NH2    . ARG A 1 122 ? 14.162 26.136 25.810 1.00 36.60 ? 305  ARG A NH2    1 
ATOM   2129 H H      . ARG A 1 122 ? 16.360 28.823 31.804 1.00 20.43 ? 305  ARG A H      1 
ATOM   2130 H HA     . ARG A 1 122 ? 14.617 26.753 32.114 1.00 21.16 ? 305  ARG A HA     1 
ATOM   2131 H HB2    . ARG A 1 122 ? 17.335 26.698 31.363 1.00 24.10 ? 305  ARG A HB2    1 
ATOM   2132 H HB3    . ARG A 1 122 ? 16.411 25.410 31.482 1.00 24.10 ? 305  ARG A HB3    1 
ATOM   2133 H HG2    . ARG A 1 122 ? 16.061 27.390 29.512 1.00 29.70 ? 305  ARG A HG2    1 
ATOM   2134 H HG3    . ARG A 1 122 ? 16.793 26.003 29.253 1.00 29.70 ? 305  ARG A HG3    1 
ATOM   2135 H HD2    . ARG A 1 122 ? 14.691 24.969 29.869 1.00 35.17 ? 305  ARG A HD2    1 
ATOM   2136 H HD3    . ARG A 1 122 ? 14.053 26.412 29.675 1.00 35.17 ? 305  ARG A HD3    1 
ATOM   2137 H HE     . ARG A 1 122 ? 14.845 24.784 27.680 1.00 40.04 ? 305  ARG A HE     1 
ATOM   2138 H HH11   . ARG A 1 122 ? 13.926 27.930 28.290 1.00 39.63 ? 305  ARG A HH11   1 
ATOM   2139 H HH12   . ARG A 1 122 ? 13.616 28.269 26.873 1.00 39.63 ? 305  ARG A HH12   1 
ATOM   2140 H HH21   . ARG A 1 122 ? 14.388 25.344 25.560 1.00 43.92 ? 305  ARG A HH21   1 
ATOM   2141 H HH22   . ARG A 1 122 ? 13.895 26.710 25.229 1.00 43.92 ? 305  ARG A HH22   1 
ATOM   2142 N N      . ALA A 1 123 ? 15.361 25.842 34.257 1.00 15.11 ? 306  ALA A N      1 
ATOM   2143 C CA     . ALA A 1 123 ? 15.677 25.498 35.638 1.00 14.50 ? 306  ALA A CA     1 
ATOM   2144 C C      . ALA A 1 123 ? 15.274 24.055 35.884 1.00 14.27 ? 306  ALA A C      1 
ATOM   2145 O O      . ALA A 1 123 ? 14.141 23.661 35.583 1.00 16.57 ? 306  ALA A O      1 
ATOM   2146 C CB     . ALA A 1 123 ? 14.949 26.415 36.628 1.00 14.58 ? 306  ALA A CB     1 
ATOM   2147 H H      . ALA A 1 123 ? 14.774 25.332 33.890 1.00 18.14 ? 306  ALA A H      1 
ATOM   2148 H HA     . ALA A 1 123 ? 16.632 25.591 35.776 1.00 17.40 ? 306  ALA A HA     1 
ATOM   2149 H HB1    . ALA A 1 123 ? 15.195 26.162 37.531 1.00 17.50 ? 306  ALA A HB1    1 
ATOM   2150 H HB2    . ALA A 1 123 ? 15.210 27.333 36.458 1.00 17.50 ? 306  ALA A HB2    1 
ATOM   2151 H HB3    . ALA A 1 123 ? 13.992 26.315 36.506 1.00 17.50 ? 306  ALA A HB3    1 
ATOM   2152 N N      . ASN A 1 124 ? 16.179 23.290 36.485 1.00 14.29 ? 307  ASN A N      1 
ATOM   2153 C CA     . ASN A 1 124 ? 15.801 21.960 36.977 1.00 13.61 ? 307  ASN A CA     1 
ATOM   2154 C C      . ASN A 1 124 ? 15.000 22.077 38.276 1.00 12.16 ? 307  ASN A C      1 
ATOM   2155 O O      . ASN A 1 124 ? 14.805 23.155 38.845 1.00 12.10 ? 307  ASN A O      1 
ATOM   2156 C CB     . ASN A 1 124 ? 17.004 21.019 37.052 1.00 15.16 ? 307  ASN A CB     1 
ATOM   2157 C CG     . ASN A 1 124 ? 18.027 21.396 38.090 1.00 16.56 ? 307  ASN A CG     1 
ATOM   2158 O OD1    . ASN A 1 124 ? 17.822 22.221 38.956 1.00 14.71 ? 307  ASN A OD1    1 
ATOM   2159 N ND2    . ASN A 1 124 ? 19.153 20.679 38.055 1.00 20.41 ? 307  ASN A ND2    1 
ATOM   2160 H H      . ASN A 1 124 ? 16.999 23.508 36.620 1.00 17.14 ? 307  ASN A H      1 
ATOM   2161 H HA     . ASN A 1 124 ? 15.207 21.531 36.341 1.00 16.34 ? 307  ASN A HA     1 
ATOM   2162 H HB2    . ASN A 1 124 ? 16.686 20.128 37.264 1.00 18.19 ? 307  ASN A HB2    1 
ATOM   2163 H HB3    . ASN A 1 124 ? 17.449 21.017 36.190 1.00 18.19 ? 307  ASN A HB3    1 
ATOM   2164 H HD21   . ASN A 1 124 ? 19.782 20.839 38.619 1.00 24.50 ? 307  ASN A HD21   1 
ATOM   2165 H HD22   . ASN A 1 124 ? 19.249 20.057 37.469 1.00 24.50 ? 307  ASN A HD22   1 
ATOM   2166 N N      . GLU A 1 125 ? 14.495 20.944 38.743 1.00 12.82 ? 308  GLU A N      1 
ATOM   2167 C CA     . GLU A 1 125 ? 13.609 20.960 39.887 1.00 13.05 ? 308  GLU A CA     1 
ATOM   2168 C C      . GLU A 1 125 ? 14.315 21.465 41.128 1.00 11.69 ? 308  GLU A C      1 
ATOM   2169 O O      . GLU A 1 125 ? 13.710 22.179 41.919 1.00 12.26 ? 308  GLU A O      1 
ATOM   2170 C CB     . GLU A 1 125 ? 12.958 19.592 40.117 1.00 14.05 ? 308  GLU A CB     1 
ATOM   2171 C CG     . GLU A 1 125 ? 12.040 19.522 41.325 1.00 16.38 ? 308  GLU A CG     1 
ATOM   2172 C CD     . GLU A 1 125 ? 10.864 20.506 41.309 1.00 19.60 ? 308  GLU A CD     1 
ATOM   2173 O OE1    . GLU A 1 125 ? 10.532 21.084 40.249 1.00 20.68 ? 308  GLU A OE1    1 
ATOM   2174 O OE2    . GLU A 1 125 ? 10.314 20.758 42.411 1.00 22.09 ? 308  GLU A OE2    1 
ATOM   2175 H H      . GLU A 1 125 ? 14.650 20.163 38.417 1.00 15.38 ? 308  GLU A H      1 
ATOM   2176 H HA     . GLU A 1 125 ? 12.883 21.573 39.696 1.00 15.66 ? 308  GLU A HA     1 
ATOM   2177 H HB2    . GLU A 1 125 ? 12.429 19.366 39.335 1.00 16.86 ? 308  GLU A HB2    1 
ATOM   2178 H HB3    . GLU A 1 125 ? 13.659 18.933 40.244 1.00 16.86 ? 308  GLU A HB3    1 
ATOM   2179 H HG2    . GLU A 1 125 ? 11.668 18.628 41.377 1.00 19.66 ? 308  GLU A HG2    1 
ATOM   2180 H HG3    . GLU A 1 125 ? 12.564 19.711 42.119 1.00 19.66 ? 308  GLU A HG3    1 
ATOM   2181 N N      . GLU A 1 126 ? 15.596 21.138 41.293 1.00 11.42 ? 309  GLU A N      1 
ATOM   2182 C CA     . GLU A 1 126 ? 16.331 21.649 42.440 1.00 11.80 ? 309  GLU A CA     1 
ATOM   2183 C C      . GLU A 1 126 ? 16.377 23.183 42.433 1.00 11.82 ? 309  GLU A C      1 
ATOM   2184 O O      . GLU A 1 126 ? 16.191 23.821 43.484 1.00 12.45 ? 309  GLU A O      1 
ATOM   2185 C CB     . GLU A 1 126 ? 17.747 21.066 42.438 1.00 12.02 ? 309  GLU A CB     1 
ATOM   2186 C CG     . GLU A 1 126 ? 18.694 21.659 43.467 1.00 13.15 ? 309  GLU A CG     1 
ATOM   2187 C CD     . GLU A 1 126 ? 20.079 21.084 43.318 1.00 14.27 ? 309  GLU A CD     1 
ATOM   2188 O OE1    . GLU A 1 126 ? 20.784 21.545 42.403 1.00 15.33 ? 309  GLU A OE1    1 
ATOM   2189 O OE2    . GLU A 1 126 ? 20.434 20.129 44.054 1.00 16.08 ? 309  GLU A OE2    1 
ATOM   2190 H H      . GLU A 1 126 ? 16.051 20.634 40.765 1.00 13.70 ? 309  GLU A H      1 
ATOM   2191 H HA     . GLU A 1 126 ? 15.885 21.370 43.255 1.00 14.16 ? 309  GLU A HA     1 
ATOM   2192 H HB2    . GLU A 1 126 ? 17.687 20.114 42.615 1.00 14.42 ? 309  GLU A HB2    1 
ATOM   2193 H HB3    . GLU A 1 126 ? 18.139 21.217 41.563 1.00 14.42 ? 309  GLU A HB3    1 
ATOM   2194 H HG2    . GLU A 1 126 ? 18.745 22.620 43.344 1.00 15.78 ? 309  GLU A HG2    1 
ATOM   2195 H HG3    . GLU A 1 126 ? 18.371 21.456 44.359 1.00 15.78 ? 309  GLU A HG3    1 
ATOM   2196 N N      . LEU A 1 127 ? 16.621 23.769 41.277 1.00 11.60 ? 310  LEU A N      1 
ATOM   2197 C CA     . LEU A 1 127 ? 16.670 25.221 41.182 1.00 10.79 ? 310  LEU A CA     1 
ATOM   2198 C C      . LEU A 1 127 ? 15.279 25.814 41.345 1.00 11.42 ? 310  LEU A C      1 
ATOM   2199 O O      . LEU A 1 127 ? 15.108 26.840 42.003 1.00 11.57 ? 310  LEU A O      1 
ATOM   2200 C CB     . LEU A 1 127 ? 17.329 25.616 39.865 1.00 12.07 ? 310  LEU A CB     1 
ATOM   2201 C CG     . LEU A 1 127 ? 17.426 27.136 39.626 1.00 12.11 ? 310  LEU A CG     1 
ATOM   2202 C CD1    . LEU A 1 127 ? 18.139 27.892 40.770 1.00 12.95 ? 310  LEU A CD1    1 
ATOM   2203 C CD2    . LEU A 1 127 ? 18.113 27.427 38.341 1.00 13.03 ? 310  LEU A CD2    1 
ATOM   2204 H H      . LEU A 1 127 ? 16.762 23.357 40.536 1.00 13.92 ? 310  LEU A H      1 
ATOM   2205 H HA     . LEU A 1 127 ? 17.216 25.592 41.893 1.00 12.95 ? 310  LEU A HA     1 
ATOM   2206 H HB2    . LEU A 1 127 ? 18.231 25.259 39.853 1.00 14.49 ? 310  LEU A HB2    1 
ATOM   2207 H HB3    . LEU A 1 127 ? 16.812 25.237 39.137 1.00 14.49 ? 310  LEU A HB3    1 
ATOM   2208 H HG     . LEU A 1 127 ? 16.514 27.465 39.592 1.00 14.53 ? 310  LEU A HG     1 
ATOM   2209 H HD11   . LEU A 1 127 ? 18.154 28.839 40.562 1.00 15.54 ? 310  LEU A HD11   1 
ATOM   2210 H HD12   . LEU A 1 127 ? 17.655 27.743 41.597 1.00 15.54 ? 310  LEU A HD12   1 
ATOM   2211 H HD13   . LEU A 1 127 ? 19.046 27.558 40.853 1.00 15.54 ? 310  LEU A HD13   1 
ATOM   2212 H HD21   . LEU A 1 127 ? 18.122 28.386 38.197 1.00 15.63 ? 310  LEU A HD21   1 
ATOM   2213 H HD22   . LEU A 1 127 ? 19.022 27.091 38.386 1.00 15.63 ? 310  LEU A HD22   1 
ATOM   2214 H HD23   . LEU A 1 127 ? 17.634 26.989 37.620 1.00 15.63 ? 310  LEU A HD23   1 
ATOM   2215 N N      . ARG A 1 128 ? 14.264 25.166 40.771 1.00 11.41 ? 311  ARG A N      1 
ATOM   2216 C CA     . ARG A 1 128 ? 12.888 25.647 40.962 1.00 11.66 ? 311  ARG A CA     1 
ATOM   2217 C C      . ARG A 1 128 ? 12.490 25.652 42.437 1.00 11.86 ? 311  ARG A C      1 
ATOM   2218 O O      . ARG A 1 128 ? 11.886 26.614 42.929 1.00 13.25 ? 311  ARG A O      1 
ATOM   2219 C CB     . ARG A 1 128 ? 11.908 24.804 40.155 1.00 11.93 ? 311  ARG A CB     1 
ATOM   2220 C CG     . ARG A 1 128 ? 12.100 24.964 38.691 1.00 13.92 ? 311  ARG A CG     1 
ATOM   2221 C CD     . ARG A 1 128 ? 11.310 23.945 37.861 1.00 16.42 ? 311  ARG A CD     1 
ATOM   2222 N NE     . ARG A 1 128 ? 11.569 24.172 36.447 1.00 19.72 ? 311  ARG A NE     1 
ATOM   2223 C CZ     . ARG A 1 128 ? 10.935 25.066 35.693 1.00 23.04 ? 311  ARG A CZ     1 
ATOM   2224 N NH1    . ARG A 1 128 ? 9.846  25.692 36.127 1.00 21.75 ? 311  ARG A NH1    1 
ATOM   2225 N NH2    . ARG A 1 128 ? 11.419 25.355 34.485 1.00 24.50 ? 311  ARG A NH2    1 
ATOM   2226 H H      . ARG A 1 128 ? 14.338 24.464 40.280 1.00 13.70 ? 311  ARG A H      1 
ATOM   2227 H HA     . ARG A 1 128 ? 12.843 26.559 40.634 1.00 14.00 ? 311  ARG A HA     1 
ATOM   2228 H HB2    . ARG A 1 128 ? 12.036 23.868 40.377 1.00 14.32 ? 311  ARG A HB2    1 
ATOM   2229 H HB3    . ARG A 1 128 ? 11.002 25.075 40.373 1.00 14.32 ? 311  ARG A HB3    1 
ATOM   2230 H HG2    . ARG A 1 128 ? 11.807 25.851 38.430 1.00 16.70 ? 311  ARG A HG2    1 
ATOM   2231 H HG3    . ARG A 1 128 ? 13.041 24.851 38.483 1.00 16.70 ? 311  ARG A HG3    1 
ATOM   2232 H HD2    . ARG A 1 128 ? 11.589 23.045 38.092 1.00 19.71 ? 311  ARG A HD2    1 
ATOM   2233 H HD3    . ARG A 1 128 ? 10.360 24.051 38.028 1.00 19.71 ? 311  ARG A HD3    1 
ATOM   2234 H HE     . ARG A 1 128 ? 12.177 23.694 36.071 1.00 23.66 ? 311  ARG A HE     1 
ATOM   2235 H HH11   . ARG A 1 128 ? 9.536  25.522 36.912 1.00 26.10 ? 311  ARG A HH11   1 
ATOM   2236 H HH12   . ARG A 1 128 ? 9.451  26.266 35.624 1.00 26.10 ? 311  ARG A HH12   1 
ATOM   2237 H HH21   . ARG A 1 128 ? 12.132 24.966 34.203 1.00 29.40 ? 311  ARG A HH21   1 
ATOM   2238 H HH22   . ARG A 1 128 ? 11.019 25.931 33.988 1.00 29.40 ? 311  ARG A HH22   1 
ATOM   2239 N N      . ALA A 1 129 ? 12.835 24.587 43.176 1.00 12.01 ? 312  ALA A N      1 
ATOM   2240 C CA     . ALA A 1 129 ? 12.470 24.514 44.576 1.00 13.68 ? 312  ALA A CA     1 
ATOM   2241 C C      . ALA A 1 129 ? 13.194 25.590 45.367 1.00 13.45 ? 312  ALA A C      1 
ATOM   2242 O O      . ALA A 1 129 ? 12.602 26.217 46.245 1.00 14.59 ? 312  ALA A O      1 
ATOM   2243 C CB     . ALA A 1 129 ? 12.783 23.119 45.138 1.00 14.38 ? 312  ALA A CB     1 
ATOM   2244 H H      . ALA A 1 129 ? 13.274 23.907 42.885 1.00 14.41 ? 312  ALA A H      1 
ATOM   2245 H HA     . ALA A 1 129 ? 11.515 24.654 44.666 1.00 16.42 ? 312  ALA A HA     1 
ATOM   2246 H HB1    . ALA A 1 129 ? 12.570 23.105 46.084 1.00 17.26 ? 312  ALA A HB1    1 
ATOM   2247 H HB2    . ALA A 1 129 ? 12.247 22.462 44.667 1.00 17.26 ? 312  ALA A HB2    1 
ATOM   2248 H HB3    . ALA A 1 129 ? 13.726 22.931 45.009 1.00 17.26 ? 312  ALA A HB3    1 
ATOM   2249 N N      . LYS A 1 130 ? 14.476 25.822 45.070 1.00 12.11 ? 313  LYS A N      1 
ATOM   2250 C CA     . LYS A 1 130 ? 15.210 26.897 45.734 1.00 12.13 ? 313  LYS A CA     1 
ATOM   2251 C C      . LYS A 1 130 ? 14.581 28.245 45.447 1.00 11.86 ? 313  LYS A C      1 
ATOM   2252 O O      . LYS A 1 130 ? 14.430 29.061 46.368 1.00 13.58 ? 313  LYS A O      1 
ATOM   2253 C CB     . LYS A 1 130 ? 16.668 26.847 45.287 1.00 12.46 ? 313  LYS A CB     1 
ATOM   2254 C CG     . LYS A 1 130 ? 17.562 27.919 45.897 1.00 13.34 ? 313  LYS A CG     1 
ATOM   2255 C CD     . LYS A 1 130 ? 17.755 27.797 47.375 1.00 15.17 ? 313  LYS A CD     1 
ATOM   2256 C CE     . LYS A 1 130 ? 18.456 26.475 47.737 1.00 16.25 ? 313  LYS A CE     1 
ATOM   2257 N NZ     . LYS A 1 130 ? 18.888 26.470 49.164 1.00 18.12 ? 313  LYS A NZ     1 
ATOM   2258 H H      . LYS A 1 130 ? 14.936 25.378 44.495 1.00 14.54 ? 313  LYS A H      1 
ATOM   2259 H HA     . LYS A 1 130 ? 15.186 26.773 46.696 1.00 14.55 ? 313  LYS A HA     1 
ATOM   2260 H HB2    . LYS A 1 130 ? 17.036 25.985 45.534 1.00 14.95 ? 313  LYS A HB2    1 
ATOM   2261 H HB3    . LYS A 1 130 ? 16.698 26.957 44.323 1.00 14.95 ? 313  LYS A HB3    1 
ATOM   2262 H HG2    . LYS A 1 130 ? 18.437 27.865 45.482 1.00 16.01 ? 313  LYS A HG2    1 
ATOM   2263 H HG3    . LYS A 1 130 ? 17.167 28.788 45.725 1.00 16.01 ? 313  LYS A HG3    1 
ATOM   2264 H HD2    . LYS A 1 130 ? 18.305 28.531 47.690 1.00 18.20 ? 313  LYS A HD2    1 
ATOM   2265 H HD3    . LYS A 1 130 ? 16.891 27.817 47.816 1.00 18.20 ? 313  LYS A HD3    1 
ATOM   2266 H HE2    . LYS A 1 130 ? 17.842 25.736 47.600 1.00 19.50 ? 313  LYS A HE2    1 
ATOM   2267 H HE3    . LYS A 1 130 ? 19.240 26.362 47.178 1.00 19.50 ? 313  LYS A HE3    1 
ATOM   2268 H HZ1    . LYS A 1 130 ? 19.202 25.667 49.384 1.00 21.75 ? 313  LYS A HZ1    1 
ATOM   2269 H HZ2    . LYS A 1 130 ? 19.529 27.075 49.290 1.00 21.75 ? 313  LYS A HZ2    1 
ATOM   2270 H HZ3    . LYS A 1 130 ? 18.199 26.666 49.692 1.00 21.75 ? 313  LYS A HZ3    1 
ATOM   2271 N N      . LEU A 1 131 ? 14.209 28.490 44.194 1.00 12.34 ? 314  LEU A N      1 
ATOM   2272 C CA     . LEU A 1 131 ? 13.574 29.749 43.854 1.00 12.57 ? 314  LEU A CA     1 
ATOM   2273 C C      . LEU A 1 131 ? 12.233 29.923 44.531 1.00 13.10 ? 314  LEU A C      1 
ATOM   2274 O O      . LEU A 1 131 ? 11.868 31.048 44.893 1.00 12.94 ? 314  LEU A O      1 
ATOM   2275 C CB     . LEU A 1 131 ? 13.475 29.894 42.355 1.00 12.12 ? 314  LEU A CB     1 
ATOM   2276 C CG     . LEU A 1 131 ? 14.800 30.335 41.732 1.00 12.22 ? 314  LEU A CG     1 
ATOM   2277 C CD1    . LEU A 1 131 ? 14.747 30.200 40.244 1.00 13.68 ? 314  LEU A CD1    1 
ATOM   2278 C CD2    . LEU A 1 131 ? 15.162 31.792 42.118 1.00 14.37 ? 314  LEU A CD2    1 
ATOM   2279 H H      . LEU A 1 131 ? 14.312 27.949 43.533 1.00 14.81 ? 314  LEU A H      1 
ATOM   2280 H HA     . LEU A 1 131 ? 14.134 30.471 44.179 1.00 15.09 ? 314  LEU A HA     1 
ATOM   2281 H HB2    . LEU A 1 131 ? 13.227 29.039 41.968 1.00 14.55 ? 314  LEU A HB2    1 
ATOM   2282 H HB3    . LEU A 1 131 ? 12.803 30.561 42.143 1.00 14.55 ? 314  LEU A HB3    1 
ATOM   2283 H HG     . LEU A 1 131 ? 15.500 29.758 42.078 1.00 14.66 ? 314  LEU A HG     1 
ATOM   2284 H HD11   . LEU A 1 131 ? 15.593 30.492 39.870 1.00 16.41 ? 314  LEU A HD11   1 
ATOM   2285 H HD12   . LEU A 1 131 ? 14.588 29.271 40.017 1.00 16.41 ? 314  LEU A HD12   1 
ATOM   2286 H HD13   . LEU A 1 131 ? 14.026 30.753 39.903 1.00 16.41 ? 314  LEU A HD13   1 
ATOM   2287 H HD21   . LEU A 1 131 ? 15.981 32.045 41.663 1.00 17.24 ? 314  LEU A HD21   1 
ATOM   2288 H HD22   . LEU A 1 131 ? 14.439 32.379 41.848 1.00 17.24 ? 314  LEU A HD22   1 
ATOM   2289 H HD23   . LEU A 1 131 ? 15.288 31.842 43.078 1.00 17.24 ? 314  LEU A HD23   1 
ATOM   2290 N N      . ARG A 1 132 ? 11.469 28.843 44.689 1.00 13.74 ? 315  ARG A N      1 
ATOM   2291 C CA     . ARG A 1 132 ? 10.202 28.977 45.403 1.00 13.63 ? 315  ARG A CA     1 
ATOM   2292 C C      . ARG A 1 132 ? 10.437 29.477 46.826 1.00 14.04 ? 315  ARG A C      1 
ATOM   2293 O O      . ARG A 1 132 ? 9.654  30.278 47.334 1.00 15.68 ? 315  ARG A O      1 
ATOM   2294 C CB     . ARG A 1 132 ? 9.386  27.684 45.406 1.00 15.53 ? 315  ARG A CB     1 
ATOM   2295 C CG     . ARG A 1 132 ? 8.781  27.337 44.051 1.00 17.53 ? 315  ARG A CG     1 
ATOM   2296 C CD     . ARG A 1 132 ? 7.755  26.206 44.184 1.00 19.59 ? 315  ARG A CD     1 
ATOM   2297 N NE     . ARG A 1 132 ? 8.382  24.925 44.472 1.00 21.77 ? 315  ARG A NE     1 
ATOM   2298 C CZ     . ARG A 1 132 ? 8.778  24.059 43.542 1.00 22.15 ? 315  ARG A CZ     1 
ATOM   2299 N NH1    . ARG A 1 132 ? 8.639  24.316 42.250 1.00 22.79 ? 315  ARG A NH1    1 
ATOM   2300 N NH2    . ARG A 1 132 ? 9.331  22.915 43.919 1.00 22.03 ? 315  ARG A NH2    1 
ATOM   2301 H H      . ARG A 1 132 ? 11.653 28.053 44.404 1.00 16.49 ? 315  ARG A H      1 
ATOM   2302 H HA     . ARG A 1 132 ? 9.658  29.621 44.923 1.00 16.36 ? 315  ARG A HA     1 
ATOM   2303 H HB2    . ARG A 1 132 ? 9.965  26.951 45.668 1.00 18.64 ? 315  ARG A HB2    1 
ATOM   2304 H HB3    . ARG A 1 132 ? 8.659  27.775 46.040 1.00 18.64 ? 315  ARG A HB3    1 
ATOM   2305 H HG2    . ARG A 1 132 ? 8.334  28.117 43.687 1.00 21.03 ? 315  ARG A HG2    1 
ATOM   2306 H HG3    . ARG A 1 132 ? 9.483  27.045 43.448 1.00 21.03 ? 315  ARG A HG3    1 
ATOM   2307 H HD2    . ARG A 1 132 ? 7.145  26.414 44.909 1.00 23.51 ? 315  ARG A HD2    1 
ATOM   2308 H HD3    . ARG A 1 132 ? 7.265  26.122 43.351 1.00 23.51 ? 315  ARG A HD3    1 
ATOM   2309 H HE     . ARG A 1 132 ? 8.505  24.714 45.296 1.00 26.12 ? 315  ARG A HE     1 
ATOM   2310 H HH11   . ARG A 1 132 ? 8.286  25.057 41.995 1.00 27.35 ? 315  ARG A HH11   1 
ATOM   2311 H HH12   . ARG A 1 132 ? 8.901  23.741 41.667 1.00 27.35 ? 315  ARG A HH12   1 
ATOM   2312 H HH21   . ARG A 1 132 ? 9.430  22.740 44.755 1.00 26.43 ? 315  ARG A HH21   1 
ATOM   2313 H HH22   . ARG A 1 132 ? 9.590  22.347 43.328 1.00 26.43 ? 315  ARG A HH22   1 
ATOM   2314 N N      . GLU A 1 133 ? 11.544 29.069 47.464 1.00 14.48 ? 316  GLU A N      1 
ATOM   2315 C CA     . GLU A 1 133 ? 11.854 29.552 48.800 1.00 15.82 ? 316  GLU A CA     1 
ATOM   2316 C C      . GLU A 1 133 ? 12.157 31.048 48.787 1.00 15.97 ? 316  GLU A C      1 
ATOM   2317 O O      . GLU A 1 133 ? 12.105 31.691 49.826 1.00 19.96 ? 316  GLU A O      1 
ATOM   2318 C CB     . GLU A 1 133 ? 13.108 28.877 49.370 1.00 20.09 ? 316  GLU A CB     1 
ATOM   2319 C CG     . GLU A 1 133 ? 13.078 27.403 49.626 1.00 26.04 ? 316  GLU A CG     1 
ATOM   2320 C CD     . GLU A 1 133 ? 14.468 26.910 50.115 1.00 31.68 ? 316  GLU A CD     1 
ATOM   2321 O OE1    . GLU A 1 133 ? 14.976 27.446 51.119 1.00 34.33 ? 316  GLU A OE1    1 
ATOM   2322 O OE2    . GLU A 1 133 ? 15.084 26.036 49.481 1.00 34.00 ? 316  GLU A OE2    1 
ATOM   2323 H H      . GLU A 1 133 ? 12.121 28.519 47.142 1.00 17.37 ? 316  GLU A H      1 
ATOM   2324 H HA     . GLU A 1 133 ? 11.092 29.342 49.363 1.00 18.99 ? 316  GLU A HA     1 
ATOM   2325 H HB2    . GLU A 1 133 ? 13.833 29.032 48.745 1.00 24.11 ? 316  GLU A HB2    1 
ATOM   2326 H HB3    . GLU A 1 133 ? 13.307 29.299 50.221 1.00 24.11 ? 316  GLU A HB3    1 
ATOM   2327 H HG2    . GLU A 1 133 ? 12.421 27.205 50.311 1.00 31.25 ? 316  GLU A HG2    1 
ATOM   2328 H HG3    . GLU A 1 133 ? 12.854 26.935 48.806 1.00 31.25 ? 316  GLU A HG3    1 
ATOM   2329 N N      . HIS A 1 134 ? 12.485 31.582 47.627 1.00 12.91 ? 317  HIS A N      1 
ATOM   2330 C CA     A HIS A 1 134 ? 12.787 33.000 47.423 0.54 13.02 ? 317  HIS A CA     1 
ATOM   2331 C CA     B HIS A 1 134 ? 12.750 33.006 47.460 0.46 13.19 ? 317  HIS A CA     1 
ATOM   2332 C C      . HIS A 1 134 ? 11.655 33.735 46.700 1.00 13.57 ? 317  HIS A C      1 
ATOM   2333 O O      . HIS A 1 134 ? 11.871 34.832 46.151 1.00 15.60 ? 317  HIS A O      1 
ATOM   2334 C CB     A HIS A 1 134 ? 14.120 33.168 46.677 0.54 12.98 ? 317  HIS A CB     1 
ATOM   2335 C CB     B HIS A 1 134 ? 14.072 33.134 46.756 0.46 13.85 ? 317  HIS A CB     1 
ATOM   2336 C CG     A HIS A 1 134 ? 15.309 32.615 47.415 0.54 13.22 ? 317  HIS A CG     1 
ATOM   2337 C CG     B HIS A 1 134 ? 15.234 32.778 47.616 0.46 15.49 ? 317  HIS A CG     1 
ATOM   2338 N ND1    A HIS A 1 134 ? 16.299 33.405 47.979 0.54 13.86 ? 317  HIS A ND1    1 
ATOM   2339 N ND1    B HIS A 1 134 ? 15.793 33.680 48.491 0.46 16.98 ? 317  HIS A ND1    1 
ATOM   2340 C CD2    A HIS A 1 134 ? 15.643 31.334 47.714 0.54 13.79 ? 317  HIS A CD2    1 
ATOM   2341 C CD2    B HIS A 1 134 ? 15.933 31.626 47.766 0.46 15.24 ? 317  HIS A CD2    1 
ATOM   2342 C CE1    A HIS A 1 134 ? 17.176 32.630 48.593 0.54 15.42 ? 317  HIS A CE1    1 
ATOM   2343 C CE1    B HIS A 1 134 ? 16.798 33.109 49.129 0.46 16.04 ? 317  HIS A CE1    1 
ATOM   2344 N NE2    A HIS A 1 134 ? 16.803 31.372 48.447 0.54 15.53 ? 317  HIS A NE2    1 
ATOM   2345 N NE2    B HIS A 1 134 ? 16.941 31.884 48.673 0.46 14.65 ? 317  HIS A NE2    1 
ATOM   2346 H H      A HIS A 1 134 ? 12.546 31.126 46.900 0.54 15.50 ? 317  HIS A H      1 
ATOM   2347 H H      B HIS A 1 134 ? 12.565 31.131 46.899 0.46 15.50 ? 317  HIS A H      1 
ATOM   2348 H HA     A HIS A 1 134 ? 12.892 33.420 48.292 0.54 15.63 ? 317  HIS A HA     1 
ATOM   2349 H HA     B HIS A 1 134 ? 12.794 33.439 48.327 0.46 15.83 ? 317  HIS A HA     1 
ATOM   2350 H HB2    A HIS A 1 134 ? 14.060 32.706 45.826 0.54 15.58 ? 317  HIS A HB2    1 
ATOM   2351 H HB2    B HIS A 1 134 ? 14.077 32.542 45.988 0.46 16.62 ? 317  HIS A HB2    1 
ATOM   2352 H HB3    A HIS A 1 134 ? 14.277 34.114 46.530 0.54 15.58 ? 317  HIS A HB3    1 
ATOM   2353 H HB3    B HIS A 1 134 ? 14.186 34.053 46.467 0.46 16.62 ? 317  HIS A HB3    1 
ATOM   2354 H HD1    A HIS A 1 134 ? 16.337 34.263 47.936 0.54 16.63 ? 317  HIS A HD1    1 
ATOM   2355 H HD2    A HIS A 1 134 ? 15.172 30.570 47.468 0.54 16.55 ? 317  HIS A HD2    1 
ATOM   2356 H HD2    B HIS A 1 134 ? 15.767 30.817 47.338 0.46 18.29 ? 317  HIS A HD2    1 
ATOM   2357 H HE1    A HIS A 1 134 ? 17.930 32.922 49.052 0.54 18.51 ? 317  HIS A HE1    1 
ATOM   2358 H HE1    B HIS A 1 134 ? 17.318 33.506 49.789 0.46 19.25 ? 317  HIS A HE1    1 
ATOM   2359 H HE2    B HIS A 1 134 ? 17.560 31.333 48.903 0.46 17.58 ? 317  HIS A HE2    1 
ATOM   2360 N N      . GLY A 1 135 ? 10.463 33.154 46.665 1.00 14.09 ? 318  GLY A N      1 
ATOM   2361 C CA     . GLY A 1 135 ? 9.314  33.851 46.143 1.00 14.16 ? 318  GLY A CA     1 
ATOM   2362 C C      . GLY A 1 135 ? 9.225  33.944 44.653 1.00 13.01 ? 318  GLY A C      1 
ATOM   2363 O O      . GLY A 1 135 ? 8.536  34.838 44.134 1.00 14.43 ? 318  GLY A O      1 
ATOM   2364 H H      . GLY A 1 135 ? 10.300 32.356 46.939 1.00 16.90 ? 318  GLY A H      1 
ATOM   2365 H HA2    . GLY A 1 135 ? 8.514  33.398 46.454 1.00 16.99 ? 318  GLY A HA2    1 
ATOM   2366 H HA3    . GLY A 1 135 ? 9.320  34.756 46.492 1.00 16.99 ? 318  GLY A HA3    1 
ATOM   2367 N N      . VAL A 1 136 ? 9.859  33.029 43.939 1.00 12.81 ? 319  VAL A N      1 
ATOM   2368 C CA     . VAL A 1 136 ? 9.943  33.117 42.494 1.00 12.43 ? 319  VAL A CA     1 
ATOM   2369 C C      . VAL A 1 136 ? 9.493  31.816 41.854 1.00 12.26 ? 319  VAL A C      1 
ATOM   2370 O O      . VAL A 1 136 ? 10.014 30.749 42.175 1.00 12.51 ? 319  VAL A O      1 
ATOM   2371 C CB     . VAL A 1 136 ? 11.380 33.495 42.080 1.00 12.46 ? 319  VAL A CB     1 
ATOM   2372 C CG1    . VAL A 1 136 ? 11.549 33.356 40.591 1.00 14.57 ? 319  VAL A CG1    1 
ATOM   2373 C CG2    . VAL A 1 136 ? 11.700 34.929 42.502 1.00 13.32 ? 319  VAL A CG2    1 
ATOM   2374 H H      . VAL A 1 136 ? 10.251 32.340 44.274 1.00 15.37 ? 319  VAL A H      1 
ATOM   2375 H HA     . VAL A 1 136 ? 9.322  33.788 42.168 1.00 14.91 ? 319  VAL A HA     1 
ATOM   2376 H HB     . VAL A 1 136 ? 11.998 32.894 42.525 1.00 14.95 ? 319  VAL A HB     1 
ATOM   2377 H HG11   . VAL A 1 136 ? 12.442 33.646 40.346 1.00 17.49 ? 319  VAL A HG11   1 
ATOM   2378 H HG12   . VAL A 1 136 ? 11.425 32.426 40.344 1.00 17.49 ? 319  VAL A HG12   1 
ATOM   2379 H HG13   . VAL A 1 136 ? 10.888 33.907 40.145 1.00 17.49 ? 319  VAL A HG13   1 
ATOM   2380 H HG21   . VAL A 1 136 ? 12.623 35.127 42.276 1.00 15.99 ? 319  VAL A HG21   1 
ATOM   2381 H HG22   . VAL A 1 136 ? 11.107 35.536 42.032 1.00 15.99 ? 319  VAL A HG22   1 
ATOM   2382 H HG23   . VAL A 1 136 ? 11.568 35.014 43.460 1.00 15.99 ? 319  VAL A HG23   1 
ATOM   2383 N N      . GLU A 1 137 ? 8.608  31.931 40.880 1.00 13.52 ? 320  GLU A N      1 
ATOM   2384 C CA     . GLU A 1 137 ? 8.190  30.852 39.997 1.00 13.36 ? 320  GLU A CA     1 
ATOM   2385 C C      . GLU A 1 137 ? 8.858  31.020 38.638 1.00 14.01 ? 320  GLU A C      1 
ATOM   2386 O O      . GLU A 1 137 ? 8.851  32.100 38.075 1.00 16.36 ? 320  GLU A O      1 
ATOM   2387 C CB     . GLU A 1 137 ? 6.675  30.847 39.808 1.00 15.51 ? 320  GLU A CB     1 
ATOM   2388 C CG     . GLU A 1 137 ? 6.226  29.722 38.884 1.00 18.26 ? 320  GLU A CG     1 
ATOM   2389 C CD     . GLU A 1 137 ? 4.765  29.687 38.625 1.00 22.37 ? 320  GLU A CD     1 
ATOM   2390 O OE1    . GLU A 1 137 ? 4.168  30.770 38.476 1.00 23.30 ? 320  GLU A OE1    1 
ATOM   2391 O OE2    . GLU A 1 137 ? 4.215  28.568 38.542 1.00 26.21 ? 320  GLU A OE2    1 
ATOM   2392 H H      . GLU A 1 137 ? 8.208  32.670 40.698 1.00 16.22 ? 320  GLU A H      1 
ATOM   2393 H HA     . GLU A 1 137 ? 8.461  30.007 40.387 1.00 16.03 ? 320  GLU A HA     1 
ATOM   2394 H HB2    . GLU A 1 137 ? 6.246  30.724 40.669 1.00 18.61 ? 320  GLU A HB2    1 
ATOM   2395 H HB3    . GLU A 1 137 ? 6.399  31.691 39.417 1.00 18.61 ? 320  GLU A HB3    1 
ATOM   2396 H HG2    . GLU A 1 137 ? 6.673  29.826 38.029 1.00 21.91 ? 320  GLU A HG2    1 
ATOM   2397 H HG3    . GLU A 1 137 ? 6.473  28.874 39.286 1.00 21.91 ? 320  GLU A HG3    1 
ATOM   2398 N N      . VAL A 1 138 ? 9.434  29.957 38.110 1.00 14.87 ? 321  VAL A N      1 
ATOM   2399 C CA     . VAL A 1 138 ? 10.018 29.944 36.782 1.00 15.77 ? 321  VAL A CA     1 
ATOM   2400 C C      . VAL A 1 138 ? 8.931  29.529 35.821 1.00 18.71 ? 321  VAL A C      1 
ATOM   2401 O O      . VAL A 1 138 ? 8.323  28.457 35.982 1.00 19.53 ? 321  VAL A O      1 
ATOM   2402 C CB     . VAL A 1 138 ? 11.221 28.993 36.694 1.00 15.78 ? 321  VAL A CB     1 
ATOM   2403 C CG1    . VAL A 1 138 ? 11.824 29.033 35.289 1.00 17.52 ? 321  VAL A CG1    1 
ATOM   2404 C CG2    . VAL A 1 138 ? 12.269 29.388 37.723 1.00 16.75 ? 321  VAL A CG2    1 
ATOM   2405 H H      . VAL A 1 138 ? 9.503  29.202 38.516 1.00 17.85 ? 321  VAL A H      1 
ATOM   2406 H HA     . VAL A 1 138 ? 10.330 30.834 36.555 1.00 18.92 ? 321  VAL A HA     1 
ATOM   2407 H HB     . VAL A 1 138 ? 10.927 28.087 36.878 1.00 18.94 ? 321  VAL A HB     1 
ATOM   2408 H HG11   . VAL A 1 138 ? 12.642 28.513 35.282 1.00 21.03 ? 321  VAL A HG11   1 
ATOM   2409 H HG12   . VAL A 1 138 ? 11.187 28.658 34.661 1.00 21.03 ? 321  VAL A HG12   1 
ATOM   2410 H HG13   . VAL A 1 138 ? 12.016 29.955 35.054 1.00 21.03 ? 321  VAL A HG13   1 
ATOM   2411 H HG21   . VAL A 1 138 ? 13.021 28.778 37.658 1.00 20.11 ? 321  VAL A HG21   1 
ATOM   2412 H HG22   . VAL A 1 138 ? 12.562 30.295 37.543 1.00 20.11 ? 321  VAL A HG22   1 
ATOM   2413 H HG23   . VAL A 1 138 ? 11.877 29.337 38.609 1.00 20.11 ? 321  VAL A HG23   1 
ATOM   2414 N N      . LYS A 1 139 ? 8.691  30.366 34.826 1.00 21.05 ? 322  LYS A N      1 
ATOM   2415 C CA     . LYS A 1 139 ? 7.562  30.252 33.917 1.00 24.86 ? 322  LYS A CA     1 
ATOM   2416 C C      . LYS A 1 139 ? 8.044  30.187 32.472 1.00 23.39 ? 322  LYS A C      1 
ATOM   2417 O O      . LYS A 1 139 ? 8.928  30.942 32.087 1.00 21.80 ? 322  LYS A O      1 
ATOM   2418 C CB     . LYS A 1 139 ? 6.656  31.507 34.065 1.00 30.57 ? 322  LYS A CB     1 
ATOM   2419 C CG     . LYS A 1 139 ? 6.159  31.798 35.503 1.00 34.71 ? 322  LYS A CG     1 
ATOM   2420 C CD     . LYS A 1 139 ? 5.769  33.278 35.707 1.00 37.95 ? 322  LYS A CD     1 
ATOM   2421 C CE     . LYS A 1 139 ? 6.069  33.749 37.151 1.00 37.96 ? 322  LYS A CE     1 
ATOM   2422 N NZ     . LYS A 1 139 ? 4.913  33.519 38.116 1.00 36.95 ? 322  LYS A NZ     1 
ATOM   2423 H H      . LYS A 1 139 ? 9.191  31.042 34.646 1.00 25.27 ? 322  LYS A H      1 
ATOM   2424 H HA     . LYS A 1 139 ? 7.057  29.448 34.114 1.00 29.83 ? 322  LYS A HA     1 
ATOM   2425 H HB2    . LYS A 1 139 ? 7.158  32.283 33.770 1.00 36.69 ? 322  LYS A HB2    1 
ATOM   2426 H HB3    . LYS A 1 139 ? 5.873  31.387 33.507 1.00 36.69 ? 322  LYS A HB3    1 
ATOM   2427 H HG2    . LYS A 1 139 ? 5.377  31.254 35.684 1.00 41.66 ? 322  LYS A HG2    1 
ATOM   2428 H HG3    . LYS A 1 139 ? 6.865  31.583 36.132 1.00 41.66 ? 322  LYS A HG3    1 
ATOM   2429 H HD2    . LYS A 1 139 ? 6.278  33.832 35.094 1.00 45.55 ? 322  LYS A HD2    1 
ATOM   2430 H HD3    . LYS A 1 139 ? 4.820  33.386 35.542 1.00 45.55 ? 322  LYS A HD3    1 
ATOM   2431 H HE2    . LYS A 1 139 ? 6.837  33.261 37.486 1.00 45.55 ? 322  LYS A HE2    1 
ATOM   2432 H HE3    . LYS A 1 139 ? 6.259  34.700 37.137 1.00 45.55 ? 322  LYS A HE3    1 
ATOM   2433 H HZ1    . LYS A 1 139 ? 5.209  33.539 38.955 1.00 44.34 ? 322  LYS A HZ1    1 
ATOM   2434 H HZ2    . LYS A 1 139 ? 4.298  34.154 38.011 1.00 44.34 ? 322  LYS A HZ2    1 
ATOM   2435 H HZ3    . LYS A 1 139 ? 4.540  32.726 37.961 1.00 44.34 ? 322  LYS A HZ3    1 
ATOM   2436 N N      . PRO A 1 140 ? 7.476  29.318 31.648 1.00 25.32 ? 323  PRO A N      1 
ATOM   2437 C CA     . PRO A 1 140 ? 7.744  29.412 30.207 1.00 26.89 ? 323  PRO A CA     1 
ATOM   2438 C C      . PRO A 1 140 ? 7.124  30.676 29.646 1.00 25.68 ? 323  PRO A C      1 
ATOM   2439 O O      . PRO A 1 140 ? 6.064  31.120 30.083 1.00 27.58 ? 323  PRO A O      1 
ATOM   2440 C CB     . PRO A 1 140 ? 7.066  28.168 29.629 1.00 30.14 ? 323  PRO A CB     1 
ATOM   2441 C CG     . PRO A 1 140 ? 6.033  27.779 30.644 1.00 31.39 ? 323  PRO A CG     1 
ATOM   2442 C CD     . PRO A 1 140 ? 6.539  28.226 31.980 1.00 28.74 ? 323  PRO A CD     1 
ATOM   2443 H HA     . PRO A 1 140 ? 8.694  29.377 30.017 1.00 32.26 ? 323  PRO A HA     1 
ATOM   2444 H HB2    . PRO A 1 140 ? 6.652  28.383 28.779 1.00 36.17 ? 323  PRO A HB2    1 
ATOM   2445 H HB3    . PRO A 1 140 ? 7.720  27.461 29.511 1.00 36.17 ? 323  PRO A HB3    1 
ATOM   2446 H HG2    . PRO A 1 140 ? 5.194  28.218 30.435 1.00 37.67 ? 323  PRO A HG2    1 
ATOM   2447 H HG3    . PRO A 1 140 ? 5.916  26.816 30.631 1.00 37.67 ? 323  PRO A HG3    1 
ATOM   2448 H HD2    . PRO A 1 140 ? 5.812  28.553 32.532 1.00 34.49 ? 323  PRO A HD2    1 
ATOM   2449 H HD3    . PRO A 1 140 ? 7.000  27.503 32.434 1.00 34.49 ? 323  PRO A HD3    1 
ATOM   2450 N N      . VAL A 1 141 ? 7.789  31.269 28.674 1.00 24.29 ? 324  VAL A N      1 
ATOM   2451 C CA     . VAL A 1 141 ? 7.202  32.432 28.013 1.00 26.20 ? 324  VAL A CA     1 
ATOM   2452 C C      . VAL A 1 141 ? 7.453  32.373 26.524 1.00 25.40 ? 324  VAL A C      1 
ATOM   2453 O O      . VAL A 1 141 ? 8.535  31.993 26.065 1.00 24.87 ? 324  VAL A O      1 
ATOM   2454 C CB     . VAL A 1 141 ? 7.685  33.763 28.604 1.00 28.61 ? 324  VAL A CB     1 
ATOM   2455 C CG1    . VAL A 1 141 ? 7.200  33.877 30.039 1.00 32.72 ? 324  VAL A CG1    1 
ATOM   2456 C CG2    . VAL A 1 141 ? 9.183  33.849 28.453 1.00 27.89 ? 324  VAL A CG2    1 
ATOM   2457 H H      . VAL A 1 141 ? 8.561  31.028 28.383 1.00 29.15 ? 324  VAL A H      1 
ATOM   2458 H HA     . VAL A 1 141 ? 6.242  32.381 28.144 1.00 31.44 ? 324  VAL A HA     1 
ATOM   2459 H HB     . VAL A 1 141 ? 7.316  34.526 28.133 1.00 34.33 ? 324  VAL A HB     1 
ATOM   2460 H HG11   . VAL A 1 141 ? 7.478  34.734 30.400 1.00 39.27 ? 324  VAL A HG11   1 
ATOM   2461 H HG12   . VAL A 1 141 ? 6.232  33.812 30.052 1.00 39.27 ? 324  VAL A HG12   1 
ATOM   2462 H HG13   . VAL A 1 141 ? 7.587  33.157 30.562 1.00 39.27 ? 324  VAL A HG13   1 
ATOM   2463 H HG21   . VAL A 1 141 ? 9.494  34.675 28.857 1.00 33.47 ? 324  VAL A HG21   1 
ATOM   2464 H HG22   . VAL A 1 141 ? 9.590  33.090 28.898 1.00 33.47 ? 324  VAL A HG22   1 
ATOM   2465 H HG23   . VAL A 1 141 ? 9.406  33.838 27.509 1.00 33.47 ? 324  VAL A HG23   1 
ATOM   2466 N N      . GLU A 1 142 ? 6.458  32.802 25.776 1.00 26.39 ? 325  GLU A N      1 
ATOM   2467 C CA     . GLU A 1 142 ? 6.564  32.884 24.330 1.00 26.84 ? 325  GLU A CA     1 
ATOM   2468 C C      . GLU A 1 142 ? 7.117  34.242 23.937 1.00 24.92 ? 325  GLU A C      1 
ATOM   2469 O O      . GLU A 1 142 ? 7.168  35.171 24.743 1.00 23.76 ? 325  GLU A O      1 
ATOM   2470 C CB     . GLU A 1 142 ? 5.199  32.677 23.672 1.00 29.39 ? 325  GLU A CB     1 
ATOM   2471 C CG     . GLU A 1 142 ? 4.568  31.337 23.938 1.00 33.21 ? 325  GLU A CG     1 
ATOM   2472 C CD     . GLU A 1 142 ? 5.208  30.181 23.172 1.00 37.99 ? 325  GLU A CD     1 
ATOM   2473 O OE1    . GLU A 1 142 ? 6.052  30.416 22.277 1.00 37.85 ? 325  GLU A OE1    1 
ATOM   2474 O OE2    . GLU A 1 142 ? 4.854  29.021 23.479 1.00 41.00 ? 325  GLU A OE2    1 
ATOM   2475 H H      . GLU A 1 142 ? 5.697  33.056 26.084 1.00 31.67 ? 325  GLU A H      1 
ATOM   2476 H HA     . GLU A 1 142 ? 7.160  32.190 24.007 1.00 32.21 ? 325  GLU A HA     1 
ATOM   2477 H HB2    . GLU A 1 142 ? 4.591  33.356 24.004 1.00 35.26 ? 325  GLU A HB2    1 
ATOM   2478 H HB3    . GLU A 1 142 ? 5.303  32.765 22.712 1.00 35.26 ? 325  GLU A HB3    1 
ATOM   2479 H HG2    . GLU A 1 142 ? 4.644  31.140 24.885 1.00 39.85 ? 325  GLU A HG2    1 
ATOM   2480 H HG3    . GLU A 1 142 ? 3.633  31.377 23.682 1.00 39.85 ? 325  GLU A HG3    1 
ATOM   2481 N N      . GLU A 1 143 ? 7.608  34.321 22.716 1.00 26.54 ? 326  GLU A N      1 
ATOM   2482 C CA     . GLU A 1 143 ? 8.065  35.598 22.201 1.00 27.37 ? 326  GLU A CA     1 
ATOM   2483 C C      . GLU A 1 143 ? 6.874  36.546 22.200 1.00 24.77 ? 326  GLU A C      1 
ATOM   2484 O O      . GLU A 1 143 ? 5.794  36.168 21.714 1.00 26.43 ? 326  GLU A O      1 
ATOM   2485 C CB     . GLU A 1 143 ? 8.624  35.462 20.785 1.00 31.08 ? 326  GLU A CB     1 
ATOM   2486 C CG     . GLU A 1 143 ? 9.171  36.780 20.258 1.00 35.13 ? 326  GLU A CG     1 
ATOM   2487 C CD     . GLU A 1 143 ? 9.756  36.676 18.860 1.00 39.86 ? 326  GLU A CD     1 
ATOM   2488 O OE1    . GLU A 1 143 ? 10.223 35.581 18.479 1.00 40.60 ? 326  GLU A OE1    1 
ATOM   2489 O OE2    . GLU A 1 143 ? 9.775  37.709 18.160 1.00 42.51 ? 326  GLU A OE2    1 
ATOM   2490 H H      . GLU A 1 143 ? 7.687  33.661 22.171 1.00 31.85 ? 326  GLU A H      1 
ATOM   2491 H HA     . GLU A 1 143 ? 8.780  35.948 22.755 1.00 32.85 ? 326  GLU A HA     1 
ATOM   2492 H HB2    . GLU A 1 143 ? 9.345  34.813 20.789 1.00 37.29 ? 326  GLU A HB2    1 
ATOM   2493 H HB3    . GLU A 1 143 ? 7.916  35.168 20.191 1.00 37.29 ? 326  GLU A HB3    1 
ATOM   2494 H HG2    . GLU A 1 143 ? 8.452  37.430 20.232 1.00 42.16 ? 326  GLU A HG2    1 
ATOM   2495 H HG3    . GLU A 1 143 ? 9.874  37.087 20.852 1.00 42.16 ? 326  GLU A HG3    1 
ATOM   2496 N N      . PRO A 1 144 ? 7.008  37.753 22.736 1.00 23.93 ? 327  PRO A N      1 
ATOM   2497 C CA     . PRO A 1 144 ? 5.892  38.701 22.727 1.00 23.42 ? 327  PRO A CA     1 
ATOM   2498 C C      . PRO A 1 144 ? 5.696  39.333 21.351 1.00 25.00 ? 327  PRO A C      1 
ATOM   2499 O O      . PRO A 1 144 ? 6.579  39.326 20.495 1.00 26.90 ? 327  PRO A O      1 
ATOM   2500 C CB     . PRO A 1 144 ? 6.355  39.783 23.715 1.00 22.63 ? 327  PRO A CB     1 
ATOM   2501 C CG     . PRO A 1 144 ? 7.833  39.782 23.555 1.00 24.32 ? 327  PRO A CG     1 
ATOM   2502 C CD     . PRO A 1 144 ? 8.209  38.338 23.370 1.00 24.18 ? 327  PRO A CD     1 
ATOM   2503 H HA     . PRO A 1 144 ? 5.077  38.268 23.025 1.00 28.10 ? 327  PRO A HA     1 
ATOM   2504 H HB2    . PRO A 1 144 ? 5.974  40.643 23.476 1.00 27.16 ? 327  PRO A HB2    1 
ATOM   2505 H HB3    . PRO A 1 144 ? 6.097  39.547 24.619 1.00 27.16 ? 327  PRO A HB3    1 
ATOM   2506 H HG2    . PRO A 1 144 ? 8.081  40.306 22.777 1.00 29.18 ? 327  PRO A HG2    1 
ATOM   2507 H HG3    . PRO A 1 144 ? 8.251  40.150 24.349 1.00 29.18 ? 327  PRO A HG3    1 
ATOM   2508 H HD2    . PRO A 1 144 ? 8.982  38.254 22.790 1.00 29.02 ? 327  PRO A HD2    1 
ATOM   2509 H HD3    . PRO A 1 144 ? 8.389  37.916 24.225 1.00 29.02 ? 327  PRO A HD3    1 
ATOM   2510 N N      . GLU A 1 145 ? 4.531  39.950 21.185 1.00 26.58 ? 328  GLU A N      1 
ATOM   2511 C CA     . GLU A 1 145 ? 4.324  40.907 20.100 1.00 28.07 ? 328  GLU A CA     1 
ATOM   2512 C C      . GLU A 1 145 ? 5.130  42.160 20.416 1.00 26.95 ? 328  GLU A C      1 
ATOM   2513 O O      . GLU A 1 145 ? 5.101  42.634 21.559 1.00 29.30 ? 328  GLU A O      1 
ATOM   2514 C CB     . GLU A 1 145 ? 2.844  41.292 19.989 1.00 32.19 ? 328  GLU A CB     1 
ATOM   2515 C CG     . GLU A 1 145 ? 2.535  42.307 18.875 1.00 38.65 ? 328  GLU A CG     1 
ATOM   2516 C CD     . GLU A 1 145 ? 2.871  43.783 19.228 1.00 45.97 ? 328  GLU A CD     1 
ATOM   2517 O OE1    . GLU A 1 145 ? 2.654  44.208 20.386 1.00 48.28 ? 328  GLU A OE1    1 
ATOM   2518 O OE2    . GLU A 1 145 ? 3.333  44.535 18.331 1.00 49.27 ? 328  GLU A OE2    1 
ATOM   2519 H H      . GLU A 1 145 ? 3.842  39.833 21.687 1.00 31.90 ? 328  GLU A H      1 
ATOM   2520 H HA     . GLU A 1 145 ? 4.602  40.516 19.257 1.00 33.69 ? 328  GLU A HA     1 
ATOM   2521 H HB2    . GLU A 1 145 ? 2.329  40.491 19.807 1.00 38.63 ? 328  GLU A HB2    1 
ATOM   2522 H HB3    . GLU A 1 145 ? 2.562  41.684 20.830 1.00 38.63 ? 328  GLU A HB3    1 
ATOM   2523 H HG2    . GLU A 1 145 ? 3.054  42.070 18.090 1.00 46.38 ? 328  GLU A HG2    1 
ATOM   2524 H HG3    . GLU A 1 145 ? 1.588  42.264 18.673 1.00 46.38 ? 328  GLU A HG3    1 
ATOM   2525 N N      . TRP A 1 146 ? 5.847  42.680 19.425 1.00 25.31 ? 329  TRP A N      1 
ATOM   2526 C CA     . TRP A 1 146 ? 6.632  43.899 19.634 1.00 24.61 ? 329  TRP A CA     1 
ATOM   2527 C C      . TRP A 1 146 ? 6.880  44.619 18.314 1.00 25.28 ? 329  TRP A C      1 
ATOM   2528 O O      . TRP A 1 146 ? 6.895  44.021 17.234 1.00 25.90 ? 329  TRP A O      1 
ATOM   2529 C CB     . TRP A 1 146 ? 7.959  43.577 20.329 1.00 23.93 ? 329  TRP A CB     1 
ATOM   2530 C CG     . TRP A 1 146 ? 8.922  42.889 19.424 1.00 23.68 ? 329  TRP A CG     1 
ATOM   2531 C CD1    . TRP A 1 146 ? 9.020  41.531 19.200 1.00 25.39 ? 329  TRP A CD1    1 
ATOM   2532 C CD2    . TRP A 1 146 ? 9.936  43.502 18.626 1.00 24.86 ? 329  TRP A CD2    1 
ATOM   2533 N NE1    . TRP A 1 146 ? 10.024 41.285 18.297 1.00 26.76 ? 329  TRP A NE1    1 
ATOM   2534 C CE2    . TRP A 1 146 ? 10.596 42.478 17.932 1.00 26.79 ? 329  TRP A CE2    1 
ATOM   2535 C CE3    . TRP A 1 146 ? 10.329 44.834 18.403 1.00 25.40 ? 329  TRP A CE3    1 
ATOM   2536 C CZ2    . TRP A 1 146 ? 11.644 42.735 17.050 1.00 28.29 ? 329  TRP A CZ2    1 
ATOM   2537 C CZ3    . TRP A 1 146 ? 11.354 45.082 17.522 1.00 26.90 ? 329  TRP A CZ3    1 
ATOM   2538 C CH2    . TRP A 1 146 ? 12.011 44.044 16.864 1.00 28.17 ? 329  TRP A CH2    1 
ATOM   2539 H H      . TRP A 1 146 ? 5.896  42.353 18.631 1.00 30.37 ? 329  TRP A H      1 
ATOM   2540 H HA     . TRP A 1 146 ? 6.113  44.506 20.185 1.00 29.53 ? 329  TRP A HA     1 
ATOM   2541 H HB2    . TRP A 1 146 ? 8.367  44.403 20.633 1.00 28.72 ? 329  TRP A HB2    1 
ATOM   2542 H HB3    . TRP A 1 146 ? 7.788  42.994 21.086 1.00 28.72 ? 329  TRP A HB3    1 
ATOM   2543 H HD1    . TRP A 1 146 ? 8.488  40.881 19.599 1.00 30.47 ? 329  TRP A HD1    1 
ATOM   2544 H HE1    . TRP A 1 146 ? 10.256 40.510 18.007 1.00 32.12 ? 329  TRP A HE1    1 
ATOM   2545 H HE3    . TRP A 1 146 ? 9.904  45.533 18.844 1.00 30.49 ? 329  TRP A HE3    1 
ATOM   2546 H HZ2    . TRP A 1 146 ? 12.079 42.045 16.604 1.00 33.94 ? 329  TRP A HZ2    1 
ATOM   2547 H HZ3    . TRP A 1 146 ? 11.615 45.960 17.362 1.00 32.28 ? 329  TRP A HZ3    1 
ATOM   2548 H HH2    . TRP A 1 146 ? 12.712 44.243 16.286 1.00 33.81 ? 329  TRP A HH2    1 
ATOM   2549 N N      . LYS A 1 147 ? 7.122  45.925 18.425 1.00 23.03 ? 330  LYS A N      1 
ATOM   2550 C CA     . LYS A 1 147 ? 7.503  46.725 17.278 1.00 23.76 ? 330  LYS A CA     1 
ATOM   2551 C C      . LYS A 1 147 ? 8.062  48.038 17.796 1.00 23.72 ? 330  LYS A C      1 
ATOM   2552 O O      . LYS A 1 147 ? 7.775  48.452 18.918 1.00 24.59 ? 330  LYS A O      1 
ATOM   2553 C CB     . LYS A 1 147 ? 6.308  47.001 16.351 1.00 26.68 ? 330  LYS A CB     1 
ATOM   2554 C CG     . LYS A 1 147 ? 5.218  47.806 16.996 1.00 29.42 ? 330  LYS A CG     1 
ATOM   2555 C CD     . LYS A 1 147 ? 4.019  47.949 16.030 1.00 34.83 ? 330  LYS A CD     1 
ATOM   2556 C CE     . LYS A 1 147 ? 2.884  48.701 16.708 1.00 37.97 ? 330  LYS A CE     1 
ATOM   2557 N NZ     . LYS A 1 147 ? 1.660  48.752 15.871 1.00 39.48 ? 330  LYS A NZ     1 
ATOM   2558 H H      . LYS A 1 147 ? 7.071  46.367 19.160 1.00 27.63 ? 330  LYS A H      1 
ATOM   2559 H HA     . LYS A 1 147 ? 8.183  46.257 16.768 1.00 28.52 ? 330  LYS A HA     1 
ATOM   2560 H HB2    . LYS A 1 147 ? 6.621  47.493 15.576 1.00 32.01 ? 330  LYS A HB2    1 
ATOM   2561 H HB3    . LYS A 1 147 ? 5.926  46.153 16.074 1.00 32.01 ? 330  LYS A HB3    1 
ATOM   2562 H HG2    . LYS A 1 147 ? 4.915  47.359 17.802 1.00 35.30 ? 330  LYS A HG2    1 
ATOM   2563 H HG3    . LYS A 1 147 ? 5.550  48.691 17.212 1.00 35.30 ? 330  LYS A HG3    1 
ATOM   2564 H HD2    . LYS A 1 147 ? 4.293  48.445 15.243 1.00 41.80 ? 330  LYS A HD2    1 
ATOM   2565 H HD3    . LYS A 1 147 ? 3.699  47.070 15.775 1.00 41.80 ? 330  LYS A HD3    1 
ATOM   2566 H HE2    . LYS A 1 147 ? 2.662  48.257 17.541 1.00 45.57 ? 330  LYS A HE2    1 
ATOM   2567 H HE3    . LYS A 1 147 ? 3.167  49.612 16.883 1.00 45.57 ? 330  LYS A HE3    1 
ATOM   2568 H HZ1    . LYS A 1 147 ? 1.015  49.189 16.302 1.00 47.38 ? 330  LYS A HZ1    1 
ATOM   2569 H HZ2    . LYS A 1 147 ? 1.832  49.172 15.106 1.00 47.38 ? 330  LYS A HZ2    1 
ATOM   2570 H HZ3    . LYS A 1 147 ? 1.380  47.927 15.691 1.00 47.38 ? 330  LYS A HZ3    1 
ATOM   2571 N N      . MET A 1 148 ? 8.794  48.713 16.926 1.00 24.37 ? 331  MET A N      1 
ATOM   2572 C CA     . MET A 1 148 ? 9.139  50.118 17.126 1.00 24.27 ? 331  MET A CA     1 
ATOM   2573 C C      . MET A 1 148 ? 7.968  50.926 16.573 1.00 24.35 ? 331  MET A C      1 
ATOM   2574 O O      . MET A 1 148 ? 7.722  50.927 15.358 1.00 27.17 ? 331  MET A O      1 
ATOM   2575 C CB     . MET A 1 148 ? 10.439 50.458 16.412 1.00 24.00 ? 331  MET A CB     1 
ATOM   2576 C CG     . MET A 1 148 ? 11.674 49.797 17.026 1.00 23.97 ? 331  MET A CG     1 
ATOM   2577 S SD     . MET A 1 148 ? 11.962 50.175 18.775 1.00 22.76 ? 331  MET A SD     1 
ATOM   2578 C CE     . MET A 1 148 ? 12.417 51.923 18.667 1.00 22.04 ? 331  MET A CE     1 
ATOM   2579 H H      . MET A 1 148 ? 9.109  48.378 16.199 1.00 29.25 ? 331  MET A H      1 
ATOM   2580 H HA     . MET A 1 148 ? 9.274  50.311 18.067 1.00 29.12 ? 331  MET A HA     1 
ATOM   2581 H HB2    . MET A 1 148 ? 10.373 50.164 15.490 1.00 28.80 ? 331  MET A HB2    1 
ATOM   2582 H HB3    . MET A 1 148 ? 10.570 51.419 16.445 1.00 28.80 ? 331  MET A HB3    1 
ATOM   2583 H HG2    . MET A 1 148 ? 11.577 48.835 16.949 1.00 28.76 ? 331  MET A HG2    1 
ATOM   2584 H HG3    . MET A 1 148 ? 12.456 50.092 16.533 1.00 28.76 ? 331  MET A HG3    1 
ATOM   2585 H HE1    . MET A 1 148 ? 12.616 52.253 19.557 1.00 26.44 ? 331  MET A HE1    1 
ATOM   2586 H HE2    . MET A 1 148 ? 13.198 52.012 18.099 1.00 26.44 ? 331  MET A HE2    1 
ATOM   2587 H HE3    . MET A 1 148 ? 11.675 52.420 18.288 1.00 26.44 ? 331  MET A HE3    1 
ATOM   2588 N N      . VAL A 1 149 ? 7.204  51.548 17.465 1.00 24.55 ? 332  VAL A N      1 
ATOM   2589 C CA     . VAL A 1 149 ? 6.108  52.429 17.052 1.00 26.68 ? 332  VAL A CA     1 
ATOM   2590 C C      . VAL A 1 149 ? 6.621  53.599 16.224 1.00 27.18 ? 332  VAL A C      1 
ATOM   2591 O O      . VAL A 1 149 ? 5.967  54.027 15.254 1.00 28.02 ? 332  VAL A O      1 
ATOM   2592 C CB     . VAL A 1 149 ? 5.346  52.910 18.304 1.00 29.22 ? 332  VAL A CB     1 
ATOM   2593 C CG1    . VAL A 1 149 ? 4.236  53.859 17.925 1.00 32.49 ? 332  VAL A CG1    1 
ATOM   2594 C CG2    . VAL A 1 149 ? 4.749  51.724 19.060 1.00 32.41 ? 332  VAL A CG2    1 
ATOM   2595 H H      . VAL A 1 149 ? 7.297  51.480 18.317 1.00 29.46 ? 332  VAL A H      1 
ATOM   2596 H HA     . VAL A 1 149 ? 5.501  51.927 16.486 1.00 32.02 ? 332  VAL A HA     1 
ATOM   2597 H HB     . VAL A 1 149 ? 5.976  53.373 18.878 1.00 35.06 ? 332  VAL A HB     1 
ATOM   2598 H HG11   . VAL A 1 149 ? 3.764  54.129 18.729 1.00 38.99 ? 332  VAL A HG11   1 
ATOM   2599 H HG12   . VAL A 1 149 ? 4.619  54.636 17.489 1.00 38.99 ? 332  VAL A HG12   1 
ATOM   2600 H HG13   . VAL A 1 149 ? 3.627  53.407 17.321 1.00 38.99 ? 332  VAL A HG13   1 
ATOM   2601 H HG21   . VAL A 1 149 ? 4.286  52.051 19.847 1.00 38.89 ? 332  VAL A HG21   1 
ATOM   2602 H HG22   . VAL A 1 149 ? 4.126  51.260 18.479 1.00 38.89 ? 332  VAL A HG22   1 
ATOM   2603 H HG23   . VAL A 1 149 ? 5.465  51.124 19.323 1.00 38.89 ? 332  VAL A HG23   1 
ATOM   2604 N N      . ASP A 1 150 ? 7.739  54.191 16.640 1.00 26.14 ? 333  ASP A N      1 
ATOM   2605 C CA     . ASP A 1 150 ? 8.494  55.201 15.894 1.00 26.54 ? 333  ASP A CA     1 
ATOM   2606 C C      . ASP A 1 150 ? 9.959  54.992 16.287 1.00 25.33 ? 333  ASP A C      1 
ATOM   2607 O O      . ASP A 1 150 ? 10.285 54.050 17.009 1.00 24.91 ? 333  ASP A O      1 
ATOM   2608 C CB     . ASP A 1 150 ? 7.969  56.620 16.148 1.00 28.07 ? 333  ASP A CB     1 
ATOM   2609 C CG     . ASP A 1 150 ? 7.939  56.982 17.610 1.00 29.67 ? 333  ASP A CG     1 
ATOM   2610 O OD1    . ASP A 1 150 ? 8.910  56.647 18.310 1.00 27.88 ? 333  ASP A OD1    1 
ATOM   2611 O OD2    . ASP A 1 150 ? 6.977  57.644 18.067 1.00 32.72 ? 333  ASP A OD2    1 
ATOM   2612 H H      . ASP A 1 150 ? 8.106  54.014 17.398 1.00 31.36 ? 333  ASP A H      1 
ATOM   2613 H HA     . ASP A 1 150 ? 8.403  55.074 14.937 1.00 31.84 ? 333  ASP A HA     1 
ATOM   2614 H HB2    . ASP A 1 150 ? 8.545  57.255 15.694 1.00 33.69 ? 333  ASP A HB2    1 
ATOM   2615 H HB3    . ASP A 1 150 ? 7.065  56.687 15.804 1.00 33.69 ? 333  ASP A HB3    1 
ATOM   2616 N N      . ASP A 1 151 ? 10.862 55.843 15.804 1.00 24.76 ? 334  ASP A N      1 
ATOM   2617 C CA     . ASP A 1 151 ? 12.282 55.585 16.047 1.00 24.86 ? 334  ASP A CA     1 
ATOM   2618 C C      . ASP A 1 151 ? 12.640 55.662 17.535 1.00 22.10 ? 334  ASP A C      1 
ATOM   2619 O O      . ASP A 1 151 ? 13.709 55.181 17.934 1.00 21.58 ? 334  ASP A O      1 
ATOM   2620 C CB     . ASP A 1 151 ? 13.185 56.609 15.335 1.00 26.74 ? 334  ASP A CB     1 
ATOM   2621 C CG     . ASP A 1 151 ? 13.399 56.322 13.833 1.00 29.29 ? 334  ASP A CG     1 
ATOM   2622 O OD1    . ASP A 1 151 ? 12.949 55.283 13.313 1.00 30.27 ? 334  ASP A OD1    1 
ATOM   2623 O OD2    . ASP A 1 151 ? 14.044 57.169 13.164 1.00 30.39 ? 334  ASP A OD2    1 
ATOM   2624 H H      . ASP A 1 151 ? 10.687 56.551 15.349 1.00 29.71 ? 334  ASP A H      1 
ATOM   2625 H HA     . ASP A 1 151 ? 12.459 54.700 15.691 1.00 29.83 ? 334  ASP A HA     1 
ATOM   2626 H HB2    . ASP A 1 151 ? 12.781 57.487 15.413 1.00 32.09 ? 334  ASP A HB2    1 
ATOM   2627 H HB3    . ASP A 1 151 ? 14.056 56.606 15.763 1.00 32.09 ? 334  ASP A HB3    1 
ATOM   2628 N N      . ASP A 1 152 ? 11.780 56.270 18.354 1.00 22.40 ? 335  ASP A N      1 
ATOM   2629 C CA     . ASP A 1 152 ? 12.071 56.519 19.750 1.00 23.00 ? 335  ASP A CA     1 
ATOM   2630 C C      . ASP A 1 152 ? 11.262 55.669 20.720 1.00 21.17 ? 335  ASP A C      1 
ATOM   2631 O O      . ASP A 1 152 ? 11.443 55.799 21.940 1.00 21.87 ? 335  ASP A O      1 
ATOM   2632 C CB     . ASP A 1 152 ? 11.820 57.997 20.060 1.00 23.78 ? 335  ASP A CB     1 
ATOM   2633 C CG     . ASP A 1 152 ? 12.824 58.887 19.406 1.00 23.57 ? 335  ASP A CG     1 
ATOM   2634 O OD1    . ASP A 1 152 ? 14.035 58.585 19.493 1.00 23.43 ? 335  ASP A OD1    1 
ATOM   2635 O OD2    . ASP A 1 152 ? 12.399 59.907 18.768 1.00 26.38 ? 335  ASP A OD2    1 
ATOM   2636 H H      . ASP A 1 152 ? 11.005 56.552 18.111 1.00 26.89 ? 335  ASP A H      1 
ATOM   2637 H HA     . ASP A 1 152 ? 13.006 56.309 19.901 1.00 27.61 ? 335  ASP A HA     1 
ATOM   2638 H HB2    . ASP A 1 152 ? 10.940 58.245 19.737 1.00 28.53 ? 335  ASP A HB2    1 
ATOM   2639 H HB3    . ASP A 1 152 ? 11.872 58.135 21.019 1.00 28.53 ? 335  ASP A HB3    1 
ATOM   2640 N N      . THR A 1 153 ? 10.395 54.780 20.232 1.00 21.23 ? 336  THR A N      1 
ATOM   2641 C CA     . THR A 1 153 ? 9.411  54.151 21.098 1.00 21.79 ? 336  THR A CA     1 
ATOM   2642 C C      . THR A 1 153 ? 9.308  52.672 20.775 1.00 20.68 ? 336  THR A C      1 
ATOM   2643 O O      . THR A 1 153 ? 8.884  52.300 19.676 1.00 20.75 ? 336  THR A O      1 
ATOM   2644 C CB     . THR A 1 153 ? 8.041  54.807 20.923 1.00 25.23 ? 336  THR A CB     1 
ATOM   2645 O OG1    . THR A 1 153 ? 8.169  56.236 21.010 1.00 26.89 ? 336  THR A OG1    1 
ATOM   2646 C CG2    . THR A 1 153 ? 7.093  54.291 21.983 1.00 26.61 ? 336  THR A CG2    1 
ATOM   2647 H H      . THR A 1 153 ? 10.361 54.530 19.410 1.00 25.47 ? 336  THR A H      1 
ATOM   2648 H HA     . THR A 1 153 ? 9.707  54.240 22.018 1.00 26.15 ? 336  THR A HA     1 
ATOM   2649 H HB     . THR A 1 153 ? 7.671  54.590 20.053 1.00 30.27 ? 336  THR A HB     1 
ATOM   2650 H HG1    . THR A 1 153 ? 8.625  56.524 20.366 1.00 32.26 ? 336  THR A HG1    1 
ATOM   2651 H HG21   . THR A 1 153 ? 6.234  54.734 21.903 1.00 31.93 ? 336  THR A HG21   1 
ATOM   2652 H HG22   . THR A 1 153 ? 6.966  53.335 21.877 1.00 31.93 ? 336  THR A HG22   1 
ATOM   2653 H HG23   . THR A 1 153 ? 7.456  54.465 22.866 1.00 31.93 ? 336  THR A HG23   1 
ATOM   2654 N N      . LEU A 1 154 ? 9.623  51.833 21.756 1.00 19.11 ? 337  LEU A N      1 
ATOM   2655 C CA     . LEU A 1 154 ? 9.463  50.386 21.648 1.00 18.55 ? 337  LEU A CA     1 
ATOM   2656 C C      . LEU A 1 154 ? 8.148  49.987 22.308 1.00 19.97 ? 337  LEU A C      1 
ATOM   2657 O O      . LEU A 1 154 ? 7.798  50.492 23.373 1.00 21.10 ? 337  LEU A O      1 
ATOM   2658 C CB     . LEU A 1 154 ? 10.634 49.705 22.368 1.00 18.08 ? 337  LEU A CB     1 
ATOM   2659 C CG     . LEU A 1 154 ? 10.558 48.185 22.562 1.00 17.63 ? 337  LEU A CG     1 
ATOM   2660 C CD1    . LEU A 1 154 ? 10.599 47.493 21.223 1.00 18.87 ? 337  LEU A CD1    1 
ATOM   2661 C CD2    . LEU A 1 154 ? 11.732 47.734 23.485 1.00 17.81 ? 337  LEU A CD2    1 
ATOM   2662 H H      . LEU A 1 154 ? 9.940  52.084 22.515 1.00 22.94 ? 337  LEU A H      1 
ATOM   2663 H HA     . LEU A 1 154 ? 9.444  50.098 20.722 1.00 22.26 ? 337  LEU A HA     1 
ATOM   2664 H HB2    . LEU A 1 154 ? 11.440 49.883 21.859 1.00 21.70 ? 337  LEU A HB2    1 
ATOM   2665 H HB3    . LEU A 1 154 ? 10.708 50.097 23.252 1.00 21.70 ? 337  LEU A HB3    1 
ATOM   2666 H HG     . LEU A 1 154 ? 9.724  47.931 22.988 1.00 21.16 ? 337  LEU A HG     1 
ATOM   2667 H HD11   . LEU A 1 154 ? 10.565 46.534 21.362 1.00 22.65 ? 337  LEU A HD11   1 
ATOM   2668 H HD12   . LEU A 1 154 ? 9.835  47.778 20.697 1.00 22.65 ? 337  LEU A HD12   1 
ATOM   2669 H HD13   . LEU A 1 154 ? 11.421 47.733 20.769 1.00 22.65 ? 337  LEU A HD13   1 
ATOM   2670 H HD21   . LEU A 1 154 ? 11.688 46.772 23.606 1.00 21.37 ? 337  LEU A HD21   1 
ATOM   2671 H HD22   . LEU A 1 154 ? 12.574 47.976 23.067 1.00 21.37 ? 337  LEU A HD22   1 
ATOM   2672 H HD23   . LEU A 1 154 ? 11.649 48.179 24.343 1.00 21.37 ? 337  LEU A HD23   1 
ATOM   2673 N N      . GLU A 1 155 ? 7.411  49.074 21.676 1.00 21.01 ? 338  GLU A N      1 
ATOM   2674 C CA     . GLU A 1 155 ? 6.196  48.514 22.256 1.00 23.12 ? 338  GLU A CA     1 
ATOM   2675 C C      . GLU A 1 155 ? 6.356  47.003 22.346 1.00 22.38 ? 338  GLU A C      1 
ATOM   2676 O O      . GLU A 1 155 ? 6.795  46.368 21.384 1.00 23.00 ? 338  GLU A O      1 
ATOM   2677 C CB     . GLU A 1 155 ? 4.989  48.916 21.382 1.00 28.12 ? 338  GLU A CB     1 
ATOM   2678 C CG     . GLU A 1 155 ? 3.667  48.284 21.781 1.00 34.57 ? 338  GLU A CG     1 
ATOM   2679 C CD     . GLU A 1 155 ? 2.527  48.664 20.854 1.00 41.30 ? 338  GLU A CD     1 
ATOM   2680 O OE1    . GLU A 1 155 ? 2.050  49.809 20.938 1.00 42.99 ? 338  GLU A OE1    1 
ATOM   2681 O OE2    . GLU A 1 155 ? 2.119  47.809 20.041 1.00 44.45 ? 338  GLU A OE2    1 
ATOM   2682 H H      . GLU A 1 155 ? 7.600  48.760 20.898 1.00 25.21 ? 338  GLU A H      1 
ATOM   2683 H HA     . GLU A 1 155 ? 6.040  48.837 23.157 1.00 27.74 ? 338  GLU A HA     1 
ATOM   2684 H HB2    . GLU A 1 155 ? 4.879  49.879 21.436 1.00 33.74 ? 338  GLU A HB2    1 
ATOM   2685 H HB3    . GLU A 1 155 ? 5.172  48.654 20.466 1.00 33.74 ? 338  GLU A HB3    1 
ATOM   2686 H HG2    . GLU A 1 155 ? 3.761  47.318 21.761 1.00 41.49 ? 338  GLU A HG2    1 
ATOM   2687 H HG3    . GLU A 1 155 ? 3.435  48.576 22.676 1.00 41.49 ? 338  GLU A HG3    1 
ATOM   2688 N N      . VAL A 1 156 ? 6.047  46.449 23.516 1.00 21.84 ? 339  VAL A N      1 
ATOM   2689 C CA     . VAL A 1 156 ? 6.071  45.005 23.750 1.00 21.36 ? 339  VAL A CA     1 
ATOM   2690 C C      . VAL A 1 156 ? 4.744  44.624 24.380 1.00 23.17 ? 339  VAL A C      1 
ATOM   2691 O O      . VAL A 1 156 ? 4.422  45.078 25.484 1.00 23.10 ? 339  VAL A O      1 
ATOM   2692 C CB     . VAL A 1 156 ? 7.232  44.586 24.666 1.00 20.42 ? 339  VAL A CB     1 
ATOM   2693 C CG1    . VAL A 1 156 ? 7.184  43.106 24.899 1.00 21.60 ? 339  VAL A CG1    1 
ATOM   2694 C CG2    . VAL A 1 156 ? 8.557  44.957 24.035 1.00 19.80 ? 339  VAL A CG2    1 
ATOM   2695 H H      . VAL A 1 156 ? 5.813  46.901 24.209 1.00 26.21 ? 339  VAL A H      1 
ATOM   2696 H HA     . VAL A 1 156 ? 6.165  44.542 22.902 1.00 25.63 ? 339  VAL A HA     1 
ATOM   2697 H HB     . VAL A 1 156 ? 7.151  45.046 25.515 1.00 24.50 ? 339  VAL A HB     1 
ATOM   2698 H HG11   . VAL A 1 156 ? 7.914  42.855 25.487 1.00 25.92 ? 339  VAL A HG11   1 
ATOM   2699 H HG12   . VAL A 1 156 ? 6.335  42.879 25.310 1.00 25.92 ? 339  VAL A HG12   1 
ATOM   2700 H HG13   . VAL A 1 156 ? 7.272  42.649 24.048 1.00 25.92 ? 339  VAL A HG13   1 
ATOM   2701 H HG21   . VAL A 1 156 ? 9.275  44.695 24.632 1.00 23.77 ? 339  VAL A HG21   1 
ATOM   2702 H HG22   . VAL A 1 156 ? 8.644  44.493 23.188 1.00 23.77 ? 339  VAL A HG22   1 
ATOM   2703 H HG23   . VAL A 1 156 ? 8.580  45.916 23.890 1.00 23.77 ? 339  VAL A HG23   1 
ATOM   2704 N N      . ASP A 1 157 ? 3.974  43.783 23.681 1.00 24.69 ? 340  ASP A N      1 
ATOM   2705 C CA     . ASP A 1 157 ? 2.656  43.341 24.148 1.00 27.02 ? 340  ASP A CA     1 
ATOM   2706 C C      . ASP A 1 157 ? 1.827  44.517 24.665 1.00 28.53 ? 340  ASP A C      1 
ATOM   2707 O O      . ASP A 1 157 ? 1.149  44.439 25.694 1.00 30.40 ? 340  ASP A O      1 
ATOM   2708 C CB     . ASP A 1 157 ? 2.774  42.236 25.194 1.00 28.34 ? 340  ASP A CB     1 
ATOM   2709 C CG     . ASP A 1 157 ? 3.079  40.871 24.584 1.00 30.68 ? 340  ASP A CG     1 
ATOM   2710 O OD1    . ASP A 1 157 ? 2.752  40.642 23.392 1.00 31.56 ? 340  ASP A OD1    1 
ATOM   2711 O OD2    . ASP A 1 157 ? 3.631  40.020 25.310 1.00 32.35 ? 340  ASP A OD2    1 
ATOM   2712 H H      . ASP A 1 157 ? 4.197  43.449 22.920 1.00 29.63 ? 340  ASP A H      1 
ATOM   2713 H HA     . ASP A 1 157 ? 2.179  42.968 23.390 1.00 32.43 ? 340  ASP A HA     1 
ATOM   2714 H HB2    . ASP A 1 157 ? 3.492  42.457 25.808 1.00 34.00 ? 340  ASP A HB2    1 
ATOM   2715 H HB3    . ASP A 1 157 ? 1.935  42.167 25.677 1.00 34.00 ? 340  ASP A HB3    1 
ATOM   2716 N N      . GLY A 1 158 ? 1.898  45.628 23.951 1.00 28.38 ? 341  GLY A N      1 
ATOM   2717 C CA     . GLY A 1 158 ? 1.061  46.765 24.241 1.00 29.92 ? 341  GLY A CA     1 
ATOM   2718 C C      . GLY A 1 158 ? 1.632  47.765 25.219 1.00 31.72 ? 341  GLY A C      1 
ATOM   2719 O O      . GLY A 1 158 ? 1.082  48.863 25.329 1.00 33.76 ? 341  GLY A O      1 
ATOM   2720 H H      . GLY A 1 158 ? 2.431  45.743 23.286 1.00 34.06 ? 341  GLY A H      1 
ATOM   2721 H HA2    . GLY A 1 158 ? 0.884  47.235 23.412 1.00 35.90 ? 341  GLY A HA2    1 
ATOM   2722 H HA3    . GLY A 1 158 ? 0.223  46.444 24.607 1.00 35.90 ? 341  GLY A HA3    1 
ATOM   2723 N N      . LYS A 1 159 ? 2.727  47.443 25.911 1.00 30.43 ? 342  LYS A N      1 
ATOM   2724 C CA     . LYS A 1 159 ? 3.381  48.379 26.821 1.00 30.13 ? 342  LYS A CA     1 
ATOM   2725 C C      . LYS A 1 159 ? 4.522  49.056 26.082 1.00 26.67 ? 342  LYS A C      1 
ATOM   2726 O O      . LYS A 1 159 ? 5.230  48.410 25.310 1.00 27.42 ? 342  LYS A O      1 
ATOM   2727 C CB     . LYS A 1 159 ? 3.948  47.670 28.056 1.00 33.62 ? 342  LYS A CB     1 
ATOM   2728 C CG     . LYS A 1 159 ? 2.910  47.524 29.156 1.00 40.12 ? 342  LYS A CG     1 
ATOM   2729 C CD     . LYS A 1 159 ? 3.435  46.791 30.369 1.00 45.84 ? 342  LYS A CD     1 
ATOM   2730 C CE     . LYS A 1 159 ? 2.555  47.074 31.580 1.00 50.62 ? 342  LYS A CE     1 
ATOM   2731 N NZ     . LYS A 1 159 ? 1.116  47.275 31.211 1.00 53.58 ? 342  LYS A NZ     1 
ATOM   2732 H H      . LYS A 1 159 ? 3.114  46.676 25.869 1.00 36.52 ? 342  LYS A H      1 
ATOM   2733 H HA     . LYS A 1 159 ? 2.735  49.037 27.122 1.00 36.16 ? 342  LYS A HA     1 
ATOM   2734 H HB2    . LYS A 1 159 ? 4.250  46.783 27.804 1.00 40.35 ? 342  LYS A HB2    1 
ATOM   2735 H HB3    . LYS A 1 159 ? 4.691  48.186 28.407 1.00 40.35 ? 342  LYS A HB3    1 
ATOM   2736 H HG2    . LYS A 1 159 ? 2.625  48.407 29.440 1.00 48.15 ? 342  LYS A HG2    1 
ATOM   2737 H HG3    . LYS A 1 159 ? 2.152  47.026 28.811 1.00 48.15 ? 342  LYS A HG3    1 
ATOM   2738 H HD2    . LYS A 1 159 ? 3.431  45.836 30.199 1.00 55.01 ? 342  LYS A HD2    1 
ATOM   2739 H HD3    . LYS A 1 159 ? 4.337  47.089 30.565 1.00 55.01 ? 342  LYS A HD3    1 
ATOM   2740 H HE2    . LYS A 1 159 ? 2.606  46.323 32.192 1.00 60.74 ? 342  LYS A HE2    1 
ATOM   2741 H HE3    . LYS A 1 159 ? 2.869  47.880 32.018 1.00 60.74 ? 342  LYS A HE3    1 
ATOM   2742 H HZ1    . LYS A 1 159 ? 0.640  47.472 31.937 1.00 64.30 ? 342  LYS A HZ1    1 
ATOM   2743 H HZ2    . LYS A 1 159 ? 1.042  47.943 30.627 1.00 64.30 ? 342  LYS A HZ2    1 
ATOM   2744 H HZ3    . LYS A 1 159 ? 0.789  46.533 30.843 1.00 64.30 ? 342  LYS A HZ3    1 
ATOM   2745 N N      . THR A 1 160 ? 4.721  50.348 26.320 1.00 25.80 ? 343  THR A N      1 
ATOM   2746 C CA     . THR A 1 160 ? 5.769  51.053 25.594 1.00 24.74 ? 343  THR A CA     1 
ATOM   2747 C C      . THR A 1 160 ? 6.892  51.547 26.501 1.00 22.01 ? 343  THR A C      1 
ATOM   2748 O O      . THR A 1 160 ? 6.733  51.736 27.707 1.00 24.71 ? 343  THR A O      1 
ATOM   2749 C CB     . THR A 1 160 ? 5.199  52.261 24.830 1.00 27.88 ? 343  THR A CB     1 
ATOM   2750 O OG1    . THR A 1 160 ? 4.666  53.182 25.781 1.00 31.90 ? 343  THR A OG1    1 
ATOM   2751 C CG2    . THR A 1 160 ? 4.112  51.819 23.899 1.00 27.53 ? 343  THR A CG2    1 
ATOM   2752 H H      . THR A 1 160 ? 4.275  50.822 26.881 1.00 30.96 ? 343  THR A H      1 
ATOM   2753 H HA     . THR A 1 160 ? 6.156  50.417 24.972 1.00 29.68 ? 343  THR A HA     1 
ATOM   2754 H HB     . THR A 1 160 ? 5.892  52.688 24.303 1.00 33.46 ? 343  THR A HB     1 
ATOM   2755 H HG1    . THR A 1 160 ? 4.377  53.866 25.388 1.00 38.28 ? 343  THR A HG1    1 
ATOM   2756 H HG21   . THR A 1 160 ? 3.776  52.579 23.398 1.00 33.04 ? 343  THR A HG21   1 
ATOM   2757 H HG22   . THR A 1 160 ? 4.456  51.160 23.276 1.00 33.04 ? 343  THR A HG22   1 
ATOM   2758 H HG23   . THR A 1 160 ? 3.383  51.426 24.403 1.00 33.04 ? 343  THR A HG23   1 
ATOM   2759 N N      . MET A 1 161 ? 8.047  51.750 25.882 1.00 19.25 ? 344  MET A N      1 
ATOM   2760 C CA     A MET A 1 161 ? 9.169  52.403 26.538 0.78 20.02 ? 344  MET A CA     1 
ATOM   2761 C CA     B MET A 1 161 ? 9.202  52.362 26.527 0.22 19.37 ? 344  MET A CA     1 
ATOM   2762 C C      . MET A 1 161 ? 9.801  53.345 25.536 1.00 20.11 ? 344  MET A C      1 
ATOM   2763 O O      . MET A 1 161 ? 10.097 52.962 24.403 1.00 19.93 ? 344  MET A O      1 
ATOM   2764 C CB     A MET A 1 161 ? 10.211 51.394 27.017 0.78 19.72 ? 344  MET A CB     1 
ATOM   2765 C CB     B MET A 1 161 ? 10.243 51.290 26.878 0.22 18.71 ? 344  MET A CB     1 
ATOM   2766 C CG     A MET A 1 161 ? 11.436 52.078 27.632 0.78 20.77 ? 344  MET A CG     1 
ATOM   2767 C CG     B MET A 1 161 ? 11.591 51.833 27.323 0.22 18.98 ? 344  MET A CG     1 
ATOM   2768 S SD     A MET A 1 161 ? 12.583 50.877 28.306 0.78 20.48 ? 344  MET A SD     1 
ATOM   2769 S SD     B MET A 1 161 ? 11.703 52.115 29.093 0.22 18.32 ? 344  MET A SD     1 
ATOM   2770 C CE     A MET A 1 161 ? 11.603 50.443 29.718 0.78 18.62 ? 344  MET A CE     1 
ATOM   2771 C CE     B MET A 1 161 ? 11.542 50.455 29.725 0.22 16.36 ? 344  MET A CE     1 
ATOM   2772 H H      A MET A 1 161 ? 8.207  51.516 25.070 0.78 23.10 ? 344  MET A H      1 
ATOM   2773 H H      B MET A 1 161 ? 8.192  51.536 25.062 0.22 23.10 ? 344  MET A H      1 
ATOM   2774 H HA     A MET A 1 161 ? 8.852  52.890 27.314 0.78 24.03 ? 344  MET A HA     1 
ATOM   2775 H HA     B MET A 1 161 ? 8.942  52.820 27.342 0.22 23.24 ? 344  MET A HA     1 
ATOM   2776 H HB2    A MET A 1 161 ? 9.813  50.822 27.691 0.78 23.66 ? 344  MET A HB2    1 
ATOM   2777 H HB2    B MET A 1 161 ? 9.893  50.747 27.603 0.22 22.45 ? 344  MET A HB2    1 
ATOM   2778 H HB3    A MET A 1 161 ? 10.508 50.862 26.262 0.78 23.66 ? 344  MET A HB3    1 
ATOM   2779 H HB3    B MET A 1 161 ? 10.394 50.739 26.094 0.22 22.45 ? 344  MET A HB3    1 
ATOM   2780 H HG2    A MET A 1 161 ? 11.896 52.591 26.949 0.78 24.93 ? 344  MET A HG2    1 
ATOM   2781 H HG2    B MET A 1 161 ? 12.281 51.196 27.080 0.22 22.77 ? 344  MET A HG2    1 
ATOM   2782 H HG3    A MET A 1 161 ? 11.150 52.664 28.351 0.78 24.93 ? 344  MET A HG3    1 
ATOM   2783 H HG3    B MET A 1 161 ? 11.750 52.680 26.877 0.22 22.77 ? 344  MET A HG3    1 
ATOM   2784 H HE1    A MET A 1 161 ? 12.106 49.829 30.276 0.78 22.35 ? 344  MET A HE1    1 
ATOM   2785 H HE1    B MET A 1 161 ? 11.629 50.476 30.691 0.22 19.63 ? 344  MET A HE1    1 
ATOM   2786 H HE2    A MET A 1 161 ? 11.395 51.249 30.217 0.78 22.35 ? 344  MET A HE2    1 
ATOM   2787 H HE2    B MET A 1 161 ? 10.671 50.107 29.479 0.22 19.63 ? 344  MET A HE2    1 
ATOM   2788 H HE3    A MET A 1 161 ? 10.784 50.020 29.416 0.78 22.35 ? 344  MET A HE3    1 
ATOM   2789 H HE3    B MET A 1 161 ? 12.241 49.902 29.342 0.22 19.63 ? 344  MET A HE3    1 
ATOM   2790 N N      . THR A 1 162 ? 10.024 54.585 25.972 1.00 20.43 ? 345  THR A N      1 
ATOM   2791 C CA     . THR A 1 162 ? 10.643 55.602 25.143 1.00 20.61 ? 345  THR A CA     1 
ATOM   2792 C C      . THR A 1 162 ? 12.137 55.642 25.420 1.00 19.48 ? 345  THR A C      1 
ATOM   2793 O O      . THR A 1 162 ? 12.585 55.478 26.567 1.00 19.79 ? 345  THR A O      1 
ATOM   2794 C CB     . THR A 1 162 ? 9.997  56.959 25.429 1.00 23.21 ? 345  THR A CB     1 
ATOM   2795 O OG1    . THR A 1 162 ? 8.585  56.859 25.178 1.00 26.44 ? 345  THR A OG1    1 
ATOM   2796 C CG2    . THR A 1 162 ? 10.587 58.071 24.554 1.00 25.02 ? 345  THR A CG2    1 
ATOM   2797 H H      . THR A 1 162 ? 9.819  54.861 26.760 1.00 24.51 ? 345  THR A H      1 
ATOM   2798 H HA     . THR A 1 162 ? 10.526 55.402 24.201 1.00 24.74 ? 345  THR A HA     1 
ATOM   2799 H HB     . THR A 1 162 ? 10.164 57.201 26.354 1.00 27.85 ? 345  THR A HB     1 
ATOM   2800 H HG1    . THR A 1 162 ? 8.211  57.593 25.340 1.00 31.73 ? 345  THR A HG1    1 
ATOM   2801 H HG21   . THR A 1 162 ? 10.114 58.903 24.711 1.00 30.02 ? 345  THR A HG21   1 
ATOM   2802 H HG22   . THR A 1 162 ? 11.525 58.198 24.766 1.00 30.02 ? 345  THR A HG22   1 
ATOM   2803 H HG23   . THR A 1 162 ? 10.505 57.834 23.617 1.00 30.02 ? 345  THR A HG23   1 
ATOM   2804 N N      . LYS A 1 163 ? 12.903 55.842 24.362 1.00 17.86 ? 346  LYS A N      1 
ATOM   2805 C CA     . LYS A 1 163 ? 14.339 56.058 24.491 1.00 17.15 ? 346  LYS A CA     1 
ATOM   2806 C C      . LYS A 1 163 ? 14.637 57.274 25.358 1.00 17.57 ? 346  LYS A C      1 
ATOM   2807 O O      . LYS A 1 163 ? 13.847 58.217 25.410 1.00 19.14 ? 346  LYS A O      1 
ATOM   2808 C CB     . LYS A 1 163 ? 14.960 56.209 23.111 1.00 16.55 ? 346  LYS A CB     1 
ATOM   2809 C CG     . LYS A 1 163 ? 14.940 54.910 22.311 1.00 16.99 ? 346  LYS A CG     1 
ATOM   2810 C CD     . LYS A 1 163 ? 15.610 55.083 20.958 1.00 18.00 ? 346  LYS A CD     1 
ATOM   2811 C CE     . LYS A 1 163 ? 15.452 53.811 20.098 1.00 20.43 ? 346  LYS A CE     1 
ATOM   2812 N NZ     . LYS A 1 163 ? 15.994 54.063 18.728 1.00 20.93 ? 346  LYS A NZ     1 
ATOM   2813 H H      . LYS A 1 163 ? 12.618 55.858 23.550 1.00 21.43 ? 346  LYS A H      1 
ATOM   2814 H HA     . LYS A 1 163 ? 14.745 55.294 24.930 1.00 20.58 ? 346  LYS A HA     1 
ATOM   2815 H HB2    . LYS A 1 163 ? 14.464 56.877 22.612 1.00 19.87 ? 346  LYS A HB2    1 
ATOM   2816 H HB3    . LYS A 1 163 ? 15.884 56.488 23.209 1.00 19.87 ? 346  LYS A HB3    1 
ATOM   2817 H HG2    . LYS A 1 163 ? 15.416 54.223 22.802 1.00 20.39 ? 346  LYS A HG2    1 
ATOM   2818 H HG3    . LYS A 1 163 ? 14.021 54.637 22.164 1.00 20.39 ? 346  LYS A HG3    1 
ATOM   2819 H HD2    . LYS A 1 163 ? 15.200 55.825 20.487 1.00 21.60 ? 346  LYS A HD2    1 
ATOM   2820 H HD3    . LYS A 1 163 ? 16.556 55.253 21.085 1.00 21.60 ? 346  LYS A HD3    1 
ATOM   2821 H HE2    . LYS A 1 163 ? 15.945 53.079 20.501 1.00 24.51 ? 346  LYS A HE2    1 
ATOM   2822 H HE3    . LYS A 1 163 ? 14.513 53.578 20.025 1.00 24.51 ? 346  LYS A HE3    1 
ATOM   2823 H HZ1    . LYS A 1 163 ? 15.868 53.348 18.214 1.00 25.11 ? 346  LYS A HZ1    1 
ATOM   2824 H HZ2    . LYS A 1 163 ? 15.580 54.760 18.361 1.00 25.11 ? 346  LYS A HZ2    1 
ATOM   2825 H HZ3    . LYS A 1 163 ? 16.866 54.236 18.774 1.00 25.11 ? 346  LYS A HZ3    1 
ATOM   2826 N N      . PRO A 1 164 ? 15.801 57.289 26.017 1.00 16.48 ? 347  PRO A N      1 
ATOM   2827 C CA     . PRO A 1 164 ? 16.888 56.302 25.895 1.00 15.28 ? 347  PRO A CA     1 
ATOM   2828 C C      . PRO A 1 164 ? 16.631 55.029 26.683 1.00 13.84 ? 347  PRO A C      1 
ATOM   2829 O O      . PRO A 1 164 ? 16.034 55.022 27.769 1.00 14.17 ? 347  PRO A O      1 
ATOM   2830 C CB     . PRO A 1 164 ? 18.103 57.069 26.449 1.00 16.47 ? 347  PRO A CB     1 
ATOM   2831 C CG     . PRO A 1 164 ? 17.492 58.058 27.448 1.00 17.81 ? 347  PRO A CG     1 
ATOM   2832 C CD     . PRO A 1 164 ? 16.187 58.463 26.820 1.00 18.18 ? 347  PRO A CD     1 
ATOM   2833 H HA     . PRO A 1 164 ? 17.024 56.081 24.960 1.00 18.34 ? 347  PRO A HA     1 
ATOM   2834 H HB2    . PRO A 1 164 ? 18.712 56.456 26.890 1.00 19.77 ? 347  PRO A HB2    1 
ATOM   2835 H HB3    . PRO A 1 164 ? 18.562 57.533 25.731 1.00 19.77 ? 347  PRO A HB3    1 
ATOM   2836 H HG2    . PRO A 1 164 ? 17.348 57.622 28.302 1.00 21.38 ? 347  PRO A HG2    1 
ATOM   2837 H HG3    . PRO A 1 164 ? 18.078 58.823 27.560 1.00 21.38 ? 347  PRO A HG3    1 
ATOM   2838 H HD2    . PRO A 1 164 ? 15.521 58.647 27.501 1.00 21.81 ? 347  PRO A HD2    1 
ATOM   2839 H HD3    . PRO A 1 164 ? 16.306 59.241 26.253 1.00 21.81 ? 347  PRO A HD3    1 
ATOM   2840 N N      . PHE A 1 165 ? 17.095 53.911 26.138 1.00 14.43 ? 348  PHE A N      1 
ATOM   2841 C CA     . PHE A 1 165 ? 16.966 52.617 26.805 1.00 14.12 ? 348  PHE A CA     1 
ATOM   2842 C C      . PHE A 1 165 ? 18.201 51.765 26.539 1.00 13.26 ? 348  PHE A C      1 
ATOM   2843 O O      . PHE A 1 165 ? 19.003 52.030 25.644 1.00 14.77 ? 348  PHE A O      1 
ATOM   2844 C CB     . PHE A 1 165 ? 15.618 51.933 26.555 1.00 15.44 ? 348  PHE A CB     1 
ATOM   2845 C CG     . PHE A 1 165 ? 15.246 51.652 25.128 1.00 16.14 ? 348  PHE A CG     1 
ATOM   2846 C CD1    . PHE A 1 165 ? 16.008 50.825 24.330 1.00 16.10 ? 348  PHE A CD1    1 
ATOM   2847 C CD2    . PHE A 1 165 ? 14.048 52.154 24.618 1.00 17.30 ? 348  PHE A CD2    1 
ATOM   2848 C CE1    . PHE A 1 165 ? 15.607 50.509 23.057 1.00 16.49 ? 348  PHE A CE1    1 
ATOM   2849 C CE2    . PHE A 1 165 ? 13.641 51.831 23.343 1.00 18.09 ? 348  PHE A CE2    1 
ATOM   2850 C CZ     . PHE A 1 165 ? 14.424 51.011 22.565 1.00 17.21 ? 348  PHE A CZ     1 
ATOM   2851 H H      . PHE A 1 165 ? 17.492 53.873 25.376 1.00 17.32 ? 348  PHE A H      1 
ATOM   2852 H HA     . PHE A 1 165 ? 16.972 52.742 27.767 1.00 16.95 ? 348  PHE A HA     1 
ATOM   2853 H HB2    . PHE A 1 165 ? 15.626 51.080 27.016 1.00 18.53 ? 348  PHE A HB2    1 
ATOM   2854 H HB3    . PHE A 1 165 ? 14.922 52.502 26.920 1.00 18.53 ? 348  PHE A HB3    1 
ATOM   2855 H HD1    . PHE A 1 165 ? 16.805 50.476 24.659 1.00 19.32 ? 348  PHE A HD1    1 
ATOM   2856 H HD2    . PHE A 1 165 ? 13.520 52.711 25.144 1.00 20.76 ? 348  PHE A HD2    1 
ATOM   2857 H HE1    . PHE A 1 165 ? 16.133 49.955 22.527 1.00 19.79 ? 348  PHE A HE1    1 
ATOM   2858 H HE2    . PHE A 1 165 ? 12.840 52.166 23.010 1.00 21.71 ? 348  PHE A HE2    1 
ATOM   2859 H HZ     . PHE A 1 165 ? 14.152 50.795 21.701 1.00 20.65 ? 348  PHE A HZ     1 
ATOM   2860 N N      . VAL A 1 166 ? 18.350 50.738 27.377 1.00 13.72 ? 349  VAL A N      1 
ATOM   2861 C CA     . VAL A 1 166 ? 19.527 49.896 27.464 1.00 13.70 ? 349  VAL A CA     1 
ATOM   2862 C C      . VAL A 1 166 ? 19.060 48.469 27.183 1.00 14.32 ? 349  VAL A C      1 
ATOM   2863 O O      . VAL A 1 166 ? 18.193 47.955 27.899 1.00 14.60 ? 349  VAL A O      1 
ATOM   2864 C CB     . VAL A 1 166 ? 20.132 50.001 28.875 1.00 14.73 ? 349  VAL A CB     1 
ATOM   2865 C CG1    . VAL A 1 166 ? 21.371 49.149 28.990 1.00 16.32 ? 349  VAL A CG1    1 
ATOM   2866 C CG2    . VAL A 1 166 ? 20.384 51.489 29.196 1.00 16.40 ? 349  VAL A CG2    1 
ATOM   2867 H H      . VAL A 1 166 ? 17.741 50.501 27.936 1.00 16.47 ? 349  VAL A H      1 
ATOM   2868 H HA     . VAL A 1 166 ? 20.194 50.142 26.804 1.00 16.44 ? 349  VAL A HA     1 
ATOM   2869 H HB     . VAL A 1 166 ? 19.518 49.656 29.541 1.00 17.68 ? 349  VAL A HB     1 
ATOM   2870 H HG11   . VAL A 1 166 ? 21.731 49.235 29.887 1.00 19.59 ? 349  VAL A HG11   1 
ATOM   2871 H HG12   . VAL A 1 166 ? 21.136 48.224 28.815 1.00 19.59 ? 349  VAL A HG12   1 
ATOM   2872 H HG13   . VAL A 1 166 ? 22.025 49.453 28.341 1.00 19.59 ? 349  VAL A HG13   1 
ATOM   2873 H HG21   . VAL A 1 166 ? 20.845 51.555 30.046 1.00 19.68 ? 349  VAL A HG21   1 
ATOM   2874 H HG22   . VAL A 1 166 ? 20.929 51.876 28.493 1.00 19.68 ? 349  VAL A HG22   1 
ATOM   2875 H HG23   . VAL A 1 166 ? 19.532 51.950 29.245 1.00 19.68 ? 349  VAL A HG23   1 
ATOM   2876 N N      . GLU A 1 167 ? 19.660 47.848 26.182 1.00 14.20 ? 350  GLU A N      1 
ATOM   2877 C CA     . GLU A 1 167 ? 19.314 46.495 25.728 1.00 13.10 ? 350  GLU A CA     1 
ATOM   2878 C C      . GLU A 1 167 ? 20.389 45.534 26.208 1.00 14.05 ? 350  GLU A C      1 
ATOM   2879 O O      . GLU A 1 167 ? 21.536 45.611 25.760 1.00 15.29 ? 350  GLU A O      1 
ATOM   2880 C CB     . GLU A 1 167 ? 19.222 46.474 24.209 1.00 14.76 ? 350  GLU A CB     1 
ATOM   2881 C CG     . GLU A 1 167 ? 18.910 45.090 23.572 1.00 15.37 ? 350  GLU A CG     1 
ATOM   2882 C CD     . GLU A 1 167 ? 19.014 45.190 22.060 1.00 16.81 ? 350  GLU A CD     1 
ATOM   2883 O OE1    . GLU A 1 167 ? 20.095 45.632 21.602 1.00 17.56 ? 350  GLU A OE1    1 
ATOM   2884 O OE2    . GLU A 1 167 ? 18.042 44.847 21.332 1.00 18.38 ? 350  GLU A OE2    1 
ATOM   2885 H H      . GLU A 1 167 ? 20.299 48.199 25.725 1.00 17.04 ? 350  GLU A H      1 
ATOM   2886 H HA     . GLU A 1 167 ? 18.465 46.225 26.111 1.00 15.72 ? 350  GLU A HA     1 
ATOM   2887 H HB2    . GLU A 1 167 ? 18.515 47.081 23.939 1.00 17.71 ? 350  GLU A HB2    1 
ATOM   2888 H HB3    . GLU A 1 167 ? 20.071 46.772 23.849 1.00 17.71 ? 350  GLU A HB3    1 
ATOM   2889 H HG2    . GLU A 1 167 ? 19.549 44.432 23.887 1.00 18.45 ? 350  GLU A HG2    1 
ATOM   2890 H HG3    . GLU A 1 167 ? 18.009 44.816 23.806 1.00 18.45 ? 350  GLU A HG3    1 
ATOM   2891 N N      . LYS A 1 168 ? 20.007 44.622 27.102 1.00 14.01 ? 351  LYS A N      1 
ATOM   2892 C CA     . LYS A 1 168 ? 20.953 43.705 27.705 1.00 14.63 ? 351  LYS A CA     1 
ATOM   2893 C C      . LYS A 1 168 ? 20.605 42.263 27.347 1.00 14.91 ? 351  LYS A C      1 
ATOM   2894 O O      . LYS A 1 168 ? 19.456 41.835 27.553 1.00 14.23 ? 351  LYS A O      1 
ATOM   2895 C CB     . LYS A 1 168 ? 20.907 43.811 29.228 1.00 15.09 ? 351  LYS A CB     1 
ATOM   2896 C CG     . LYS A 1 168 ? 21.065 45.223 29.780 1.00 15.68 ? 351  LYS A CG     1 
ATOM   2897 C CD     . LYS A 1 168 ? 21.130 45.191 31.315 1.00 17.02 ? 351  LYS A CD     1 
ATOM   2898 C CE     . LYS A 1 168 ? 21.091 46.596 31.838 1.00 17.00 ? 351  LYS A CE     1 
ATOM   2899 N NZ     . LYS A 1 168 ? 21.244 46.611 33.284 1.00 17.29 ? 351  LYS A NZ     1 
ATOM   2900 H H      . LYS A 1 168 ? 19.197 44.520 27.373 1.00 16.81 ? 351  LYS A H      1 
ATOM   2901 H HA     . LYS A 1 168 ? 21.838 43.922 27.372 1.00 17.56 ? 351  LYS A HA     1 
ATOM   2902 H HB2    . LYS A 1 168 ? 20.050 43.474 29.533 1.00 18.11 ? 351  LYS A HB2    1 
ATOM   2903 H HB3    . LYS A 1 168 ? 21.625 43.273 29.596 1.00 18.11 ? 351  LYS A HB3    1 
ATOM   2904 H HG2    . LYS A 1 168 ? 21.886 45.615 29.443 1.00 18.82 ? 351  LYS A HG2    1 
ATOM   2905 H HG3    . LYS A 1 168 ? 20.305 45.764 29.513 1.00 18.82 ? 351  LYS A HG3    1 
ATOM   2906 H HD2    . LYS A 1 168 ? 20.370 44.703 31.667 1.00 20.42 ? 351  LYS A HD2    1 
ATOM   2907 H HD3    . LYS A 1 168 ? 21.956 44.771 31.601 1.00 20.42 ? 351  LYS A HD3    1 
ATOM   2908 H HE2    . LYS A 1 168 ? 21.816 47.108 31.446 1.00 20.40 ? 351  LYS A HE2    1 
ATOM   2909 H HE3    . LYS A 1 168 ? 20.239 47.002 31.614 1.00 20.40 ? 351  LYS A HE3    1 
ATOM   2910 H HZ1    . LYS A 1 168 ? 21.219 47.449 33.584 1.00 20.74 ? 351  LYS A HZ1    1 
ATOM   2911 H HZ2    . LYS A 1 168 ? 20.586 46.148 33.664 1.00 20.74 ? 351  LYS A HZ2    1 
ATOM   2912 H HZ3    . LYS A 1 168 ? 22.023 46.246 33.512 1.00 20.74 ? 351  LYS A HZ3    1 
ATOM   2913 N N      . PRO A 1 169 ? 21.566 41.463 26.889 1.00 15.44 ? 352  PRO A N      1 
ATOM   2914 C CA     . PRO A 1 169 ? 21.304 40.021 26.703 1.00 16.01 ? 352  PRO A CA     1 
ATOM   2915 C C      . PRO A 1 169 ? 20.860 39.402 28.013 1.00 14.46 ? 352  PRO A C      1 
ATOM   2916 O O      . PRO A 1 169 ? 21.330 39.787 29.076 1.00 15.62 ? 352  PRO A O      1 
ATOM   2917 C CB     . PRO A 1 169 ? 22.674 39.468 26.288 1.00 18.01 ? 352  PRO A CB     1 
ATOM   2918 C CG     . PRO A 1 169 ? 23.408 40.670 25.740 1.00 18.98 ? 352  PRO A CG     1 
ATOM   2919 C CD     . PRO A 1 169 ? 22.958 41.830 26.562 1.00 17.16 ? 352  PRO A CD     1 
ATOM   2920 H HA     . PRO A 1 169 ? 20.650 39.863 26.004 1.00 19.21 ? 352  PRO A HA     1 
ATOM   2921 H HB2    . PRO A 1 169 ? 23.132 39.099 27.059 1.00 21.61 ? 352  PRO A HB2    1 
ATOM   2922 H HB3    . PRO A 1 169 ? 22.565 38.784 25.608 1.00 21.61 ? 352  PRO A HB3    1 
ATOM   2923 H HG2    . PRO A 1 169 ? 24.365 40.537 25.828 1.00 22.78 ? 352  PRO A HG2    1 
ATOM   2924 H HG3    . PRO A 1 169 ? 23.176 40.798 24.807 1.00 22.78 ? 352  PRO A HG3    1 
ATOM   2925 H HD2    . PRO A 1 169 ? 23.493 41.917 27.366 1.00 20.60 ? 352  PRO A HD2    1 
ATOM   2926 H HD3    . PRO A 1 169 ? 22.990 42.653 26.050 1.00 20.60 ? 352  PRO A HD3    1 
ATOM   2927 N N      . VAL A 1 170 ? 19.955 38.421 27.947 1.00 14.68 ? 353  VAL A N      1 
ATOM   2928 C CA     . VAL A 1 170 ? 19.543 37.760 29.178 1.00 15.33 ? 353  VAL A CA     1 
ATOM   2929 C C      . VAL A 1 170 ? 20.686 36.965 29.837 1.00 15.86 ? 353  VAL A C      1 
ATOM   2930 O O      . VAL A 1 170 ? 20.682 36.799 31.067 1.00 15.88 ? 353  VAL A O      1 
ATOM   2931 C CB     . VAL A 1 170 ? 18.290 36.871 28.972 1.00 16.46 ? 353  VAL A CB     1 
ATOM   2932 C CG1    . VAL A 1 170 ? 17.080 37.691 28.543 1.00 16.95 ? 353  VAL A CG1    1 
ATOM   2933 C CG2    . VAL A 1 170 ? 18.543 35.708 28.000 1.00 18.24 ? 353  VAL A CG2    1 
ATOM   2934 H H      . VAL A 1 170 ? 19.582 38.134 27.227 1.00 17.61 ? 353  VAL A H      1 
ATOM   2935 H HA     . VAL A 1 170 ? 19.288 38.465 29.794 1.00 18.39 ? 353  VAL A HA     1 
ATOM   2936 H HB     . VAL A 1 170 ? 18.087 36.475 29.833 1.00 19.76 ? 353  VAL A HB     1 
ATOM   2937 H HG11   . VAL A 1 170 ? 16.329 37.095 28.399 1.00 20.35 ? 353  VAL A HG11   1 
ATOM   2938 H HG12   . VAL A 1 170 ? 16.867 38.329 29.242 1.00 20.35 ? 353  VAL A HG12   1 
ATOM   2939 H HG13   . VAL A 1 170 ? 17.292 38.161 27.721 1.00 20.35 ? 353  VAL A HG13   1 
ATOM   2940 H HG21   . VAL A 1 170 ? 17.718 35.213 27.877 1.00 21.88 ? 353  VAL A HG21   1 
ATOM   2941 H HG22   . VAL A 1 170 ? 18.843 36.066 27.150 1.00 21.88 ? 353  VAL A HG22   1 
ATOM   2942 H HG23   . VAL A 1 170 ? 19.225 35.127 28.373 1.00 21.88 ? 353  VAL A HG23   1 
ATOM   2943 N N      . ASP A 1 171 ? 21.699 36.563 29.077 1.00 17.45 ? 354  ASP A N      1 
ATOM   2944 C CA     . ASP A 1 171 ? 22.877 35.902 29.647 1.00 19.71 ? 354  ASP A CA     1 
ATOM   2945 C C      . ASP A 1 171 ? 23.657 36.916 30.474 1.00 20.41 ? 354  ASP A C      1 
ATOM   2946 O O      . ASP A 1 171 ? 24.213 37.866 29.926 1.00 20.45 ? 354  ASP A O      1 
ATOM   2947 C CB     . ASP A 1 171 ? 23.737 35.340 28.518 1.00 23.42 ? 354  ASP A CB     1 
ATOM   2948 C CG     . ASP A 1 171 ? 24.930 34.552 29.021 1.00 28.53 ? 354  ASP A CG     1 
ATOM   2949 O OD1    . ASP A 1 171 ? 25.316 34.670 30.207 1.00 27.84 ? 354  ASP A OD1    1 
ATOM   2950 O OD2    . ASP A 1 171 ? 25.503 33.830 28.203 1.00 33.58 ? 354  ASP A OD2    1 
ATOM   2951 H H      . ASP A 1 171 ? 21.733 36.660 28.223 1.00 20.94 ? 354  ASP A H      1 
ATOM   2952 H HA     . ASP A 1 171 ? 22.606 35.172 30.225 1.00 23.65 ? 354  ASP A HA     1 
ATOM   2953 H HB2    . ASP A 1 171 ? 23.196 34.747 27.974 1.00 28.11 ? 354  ASP A HB2    1 
ATOM   2954 H HB3    . ASP A 1 171 ? 24.070 36.074 27.978 1.00 28.11 ? 354  ASP A HB3    1 
ATOM   2955 N N      . GLY A 1 172 ? 23.732 36.680 31.792 1.00 20.96 ? 355  GLY A N      1 
ATOM   2956 C CA     . GLY A 1 172 ? 24.364 37.603 32.711 1.00 23.63 ? 355  GLY A CA     1 
ATOM   2957 C C      . GLY A 1 172 ? 25.851 37.755 32.497 1.00 26.37 ? 355  GLY A C      1 
ATOM   2958 O O      . GLY A 1 172 ? 26.436 38.737 32.965 1.00 28.58 ? 355  GLY A O      1 
ATOM   2959 H H      . GLY A 1 172 ? 23.415 35.978 32.175 1.00 25.15 ? 355  GLY A H      1 
ATOM   2960 H HA2    . GLY A 1 172 ? 23.955 38.477 32.610 1.00 28.36 ? 355  GLY A HA2    1 
ATOM   2961 H HA3    . GLY A 1 172 ? 24.222 37.292 33.618 1.00 28.36 ? 355  GLY A HA3    1 
ATOM   2962 N N      . GLU A 1 173 ? 26.470 36.834 31.762 1.00 26.90 ? 356  GLU A N      1 
ATOM   2963 C CA     . GLU A 1 173 ? 27.887 36.923 31.442 1.00 30.77 ? 356  GLU A CA     1 
ATOM   2964 C C      . GLU A 1 173 ? 28.166 37.543 30.075 1.00 29.01 ? 356  GLU A C      1 
ATOM   2965 O O      . GLU A 1 173 ? 29.333 37.727 29.727 1.00 30.31 ? 356  GLU A O      1 
ATOM   2966 C CB     . GLU A 1 173 ? 28.541 35.541 31.572 1.00 35.50 ? 356  GLU A CB     1 
ATOM   2967 C CG     . GLU A 1 173 ? 28.228 34.875 32.933 1.00 40.70 ? 356  GLU A CG     1 
ATOM   2968 C CD     . GLU A 1 173 ? 29.063 33.639 33.258 1.00 45.00 ? 356  GLU A CD     1 
ATOM   2969 O OE1    . GLU A 1 173 ? 28.808 32.557 32.669 1.00 45.53 ? 356  GLU A OE1    1 
ATOM   2970 O OE2    . GLU A 1 173 ? 29.959 33.746 34.135 1.00 46.90 ? 356  GLU A OE2    1 
ATOM   2971 H H      . GLU A 1 173 ? 26.083 36.140 31.434 1.00 32.28 ? 356  GLU A H      1 
ATOM   2972 H HA     . GLU A 1 173 ? 28.318 37.502 32.090 1.00 36.92 ? 356  GLU A HA     1 
ATOM   2973 H HB2    . GLU A 1 173 ? 28.207 34.963 30.868 1.00 42.60 ? 356  GLU A HB2    1 
ATOM   2974 H HB3    . GLU A 1 173 ? 29.504 35.635 31.495 1.00 42.60 ? 356  GLU A HB3    1 
ATOM   2975 H HG2    . GLU A 1 173 ? 28.387 35.525 33.636 1.00 48.85 ? 356  GLU A HG2    1 
ATOM   2976 H HG3    . GLU A 1 173 ? 27.297 34.605 32.936 1.00 48.85 ? 356  GLU A HG3    1 
ATOM   2977 N N      . ASP A 1 174 ? 27.133 37.896 29.313 1.00 27.81 ? 357  ASP A N      1 
ATOM   2978 C CA     . ASP A 1 174 ? 27.282 38.589 28.036 1.00 26.05 ? 357  ASP A CA     1 
ATOM   2979 C C      . ASP A 1 174 ? 27.186 40.096 28.300 1.00 25.30 ? 357  ASP A C      1 
ATOM   2980 O O      . ASP A 1 174 ? 26.135 40.601 28.717 1.00 25.14 ? 357  ASP A O      1 
ATOM   2981 C CB     . ASP A 1 174 ? 26.198 38.076 27.086 1.00 25.30 ? 357  ASP A CB     1 
ATOM   2982 C CG     . ASP A 1 174 ? 26.333 38.612 25.675 1.00 25.92 ? 357  ASP A CG     1 
ATOM   2983 O OD1    . ASP A 1 174 ? 27.033 39.628 25.489 1.00 25.09 ? 357  ASP A OD1    1 
ATOM   2984 O OD2    . ASP A 1 174 ? 25.701 38.026 24.754 1.00 26.41 ? 357  ASP A OD2    1 
ATOM   2985 H H      . ASP A 1 174 ? 26.313 37.741 29.521 1.00 33.37 ? 357  ASP A H      1 
ATOM   2986 H HA     . ASP A 1 174 ? 28.149 38.429 27.630 1.00 31.26 ? 357  ASP A HA     1 
ATOM   2987 H HB2    . ASP A 1 174 ? 26.250 37.109 27.043 1.00 30.36 ? 357  ASP A HB2    1 
ATOM   2988 H HB3    . ASP A 1 174 ? 25.330 38.347 27.425 1.00 30.36 ? 357  ASP A HB3    1 
ATOM   2989 N N      . HIS A 1 175 ? 28.292 40.817 28.094 1.00 24.55 ? 358  HIS A N      1 
ATOM   2990 C CA     . HIS A 1 175 ? 28.315 42.259 28.339 1.00 24.36 ? 358  HIS A CA     1 
ATOM   2991 C C      . HIS A 1 175 ? 28.208 43.080 27.057 1.00 22.92 ? 358  HIS A C      1 
ATOM   2992 O O      . HIS A 1 175 ? 28.524 44.281 27.055 1.00 22.33 ? 358  HIS A O      1 
ATOM   2993 C CB     . HIS A 1 175 ? 29.528 42.619 29.193 1.00 28.15 ? 358  HIS A CB     1 
ATOM   2994 C CG     . HIS A 1 175 ? 29.450 42.053 30.575 1.00 32.68 ? 358  HIS A CG     1 
ATOM   2995 N ND1    . HIS A 1 175 ? 28.953 42.770 31.644 1.00 34.33 ? 358  HIS A ND1    1 
ATOM   2996 C CD2    . HIS A 1 175 ? 29.763 40.826 31.055 1.00 34.83 ? 358  HIS A CD2    1 
ATOM   2997 C CE1    . HIS A 1 175 ? 28.988 42.015 32.730 1.00 35.90 ? 358  HIS A CE1    1 
ATOM   2998 N NE2    . HIS A 1 175 ? 29.465 40.827 32.397 1.00 36.24 ? 358  HIS A NE2    1 
ATOM   2999 H H      . HIS A 1 175 ? 29.037 40.493 27.814 1.00 29.46 ? 358  HIS A H      1 
ATOM   3000 H HA     . HIS A 1 175 ? 27.538 42.513 28.861 1.00 29.24 ? 358  HIS A HA     1 
ATOM   3001 H HB2    . HIS A 1 175 ? 30.328 42.269 28.769 1.00 33.78 ? 358  HIS A HB2    1 
ATOM   3002 H HB3    . HIS A 1 175 ? 29.588 43.584 29.266 1.00 33.78 ? 358  HIS A HB3    1 
ATOM   3003 H HD1    . HIS A 1 175 ? 28.665 43.580 31.609 1.00 41.19 ? 358  HIS A HD1    1 
ATOM   3004 H HD2    . HIS A 1 175 ? 30.115 40.116 30.568 1.00 41.80 ? 358  HIS A HD2    1 
ATOM   3005 H HE1    . HIS A 1 175 ? 28.723 42.275 33.582 1.00 43.08 ? 358  HIS A HE1    1 
ATOM   3006 N N      . ASN A 1 176 ? 27.694 42.466 25.988 1.00 22.17 ? 359  ASN A N      1 
ATOM   3007 C CA     . ASN A 1 176 ? 27.376 43.160 24.747 1.00 21.81 ? 359  ASN A CA     1 
ATOM   3008 C C      . ASN A 1 176 ? 26.043 43.880 24.926 1.00 19.01 ? 359  ASN A C      1 
ATOM   3009 O O      . ASN A 1 176 ? 24.994 43.467 24.438 1.00 18.99 ? 359  ASN A O      1 
ATOM   3010 C CB     . ASN A 1 176 ? 27.316 42.187 23.584 1.00 26.23 ? 359  ASN A CB     1 
ATOM   3011 C CG     . ASN A 1 176 ? 28.671 41.659 23.204 1.00 29.66 ? 359  ASN A CG     1 
ATOM   3012 O OD1    . ASN A 1 176 ? 29.548 42.418 22.782 1.00 30.53 ? 359  ASN A OD1    1 
ATOM   3013 N ND2    . ASN A 1 176 ? 28.859 40.350 23.351 1.00 31.21 ? 359  ASN A ND2    1 
ATOM   3014 H H      . ASN A 1 176 ? 27.517 41.625 25.961 1.00 26.60 ? 359  ASN A H      1 
ATOM   3015 H HA     . ASN A 1 176 ? 28.069 43.816 24.568 1.00 26.18 ? 359  ASN A HA     1 
ATOM   3016 H HB2    . ASN A 1 176 ? 26.757 41.434 23.830 1.00 31.47 ? 359  ASN A HB2    1 
ATOM   3017 H HB3    . ASN A 1 176 ? 26.942 42.639 22.812 1.00 31.47 ? 359  ASN A HB3    1 
ATOM   3018 H HD21   . ASN A 1 176 ? 29.617 39.999 23.147 1.00 37.45 ? 359  ASN A HD21   1 
ATOM   3019 H HD22   . ASN A 1 176 ? 28.222 39.855 23.649 1.00 37.45 ? 359  ASN A HD22   1 
ATOM   3020 N N      . ILE A 1 177 ? 26.107 44.995 25.612 1.00 19.22 ? 360  ILE A N      1 
ATOM   3021 C CA     . ILE A 1 177 ? 24.945 45.781 25.977 1.00 17.30 ? 360  ILE A CA     1 
ATOM   3022 C C      . ILE A 1 177 ? 24.902 46.980 25.041 1.00 17.12 ? 360  ILE A C      1 
ATOM   3023 O O      . ILE A 1 177 ? 25.930 47.621 24.806 1.00 18.10 ? 360  ILE A O      1 
ATOM   3024 C CB     . ILE A 1 177 ? 25.054 46.197 27.450 1.00 16.84 ? 360  ILE A CB     1 
ATOM   3025 C CG1    . ILE A 1 177 ? 24.827 44.973 28.374 1.00 18.10 ? 360  ILE A CG1    1 
ATOM   3026 C CG2    . ILE A 1 177 ? 24.084 47.300 27.799 1.00 16.70 ? 360  ILE A CG2    1 
ATOM   3027 C CD1    . ILE A 1 177 ? 25.164 45.223 29.821 1.00 19.76 ? 360  ILE A CD1    1 
ATOM   3028 H H      . ILE A 1 177 ? 26.844 45.336 25.893 1.00 23.07 ? 360  ILE A H      1 
ATOM   3029 H HA     . ILE A 1 177 ? 24.120 45.283 25.861 1.00 20.76 ? 360  ILE A HA     1 
ATOM   3030 H HB     . ILE A 1 177 ? 25.951 46.540 27.586 1.00 20.21 ? 360  ILE A HB     1 
ATOM   3031 H HG12   . ILE A 1 177 ? 23.892 44.719 28.329 1.00 21.72 ? 360  ILE A HG12   1 
ATOM   3032 H HG13   . ILE A 1 177 ? 25.385 44.242 28.064 1.00 21.72 ? 360  ILE A HG13   1 
ATOM   3033 H HG21   . ILE A 1 177 ? 24.162 47.501 28.745 1.00 20.04 ? 360  ILE A HG21   1 
ATOM   3034 H HG22   . ILE A 1 177 ? 24.299 48.087 27.274 1.00 20.04 ? 360  ILE A HG22   1 
ATOM   3035 H HG23   . ILE A 1 177 ? 23.183 47.003 27.597 1.00 20.04 ? 360  ILE A HG23   1 
ATOM   3036 H HD11   . ILE A 1 177 ? 25.031 44.403 30.322 1.00 23.72 ? 360  ILE A HD11   1 
ATOM   3037 H HD12   . ILE A 1 177 ? 26.090 45.504 29.886 1.00 23.72 ? 360  ILE A HD12   1 
ATOM   3038 H HD13   . ILE A 1 177 ? 24.582 45.919 30.165 1.00 23.72 ? 360  ILE A HD13   1 
ATOM   3039 N N      . TYR A 1 178 ? 23.725 47.279 24.503 1.00 16.26 ? 361  TYR A N      1 
ATOM   3040 C CA     . TYR A 1 178 ? 23.571 48.365 23.552 1.00 15.99 ? 361  TYR A CA     1 
ATOM   3041 C C      . TYR A 1 178 ? 22.741 49.466 24.198 1.00 15.51 ? 361  TYR A C      1 
ATOM   3042 O O      . TYR A 1 178 ? 21.738 49.200 24.867 1.00 16.52 ? 361  TYR A O      1 
ATOM   3043 C CB     . TYR A 1 178 ? 22.879 47.922 22.268 1.00 16.87 ? 361  TYR A CB     1 
ATOM   3044 C CG     . TYR A 1 178 ? 23.641 47.032 21.317 1.00 18.98 ? 361  TYR A CG     1 
ATOM   3045 C CD1    . TYR A 1 178 ? 24.811 46.378 21.678 1.00 19.60 ? 361  TYR A CD1    1 
ATOM   3046 C CD2    . TYR A 1 178 ? 23.156 46.829 20.036 1.00 20.55 ? 361  TYR A CD2    1 
ATOM   3047 C CE1    . TYR A 1 178 ? 25.460 45.562 20.785 1.00 21.67 ? 361  TYR A CE1    1 
ATOM   3048 C CE2    . TYR A 1 178 ? 23.795 46.009 19.145 1.00 21.39 ? 361  TYR A CE2    1 
ATOM   3049 C CZ     . TYR A 1 178 ? 24.961 45.367 19.525 1.00 23.08 ? 361  TYR A CZ     1 
ATOM   3050 O OH     . TYR A 1 178 ? 25.628 44.540 18.644 1.00 25.08 ? 361  TYR A OH     1 
ATOM   3051 H H      . TYR A 1 178 ? 22.994 46.861 24.679 1.00 19.51 ? 361  TYR A H      1 
ATOM   3052 H HA     . TYR A 1 178 ? 24.449 48.700 23.312 1.00 19.19 ? 361  TYR A HA     1 
ATOM   3053 H HB2    . TYR A 1 178 ? 22.078 47.437 22.519 1.00 20.24 ? 361  TYR A HB2    1 
ATOM   3054 H HB3    . TYR A 1 178 ? 22.643 48.720 21.771 1.00 20.24 ? 361  TYR A HB3    1 
ATOM   3055 H HD1    . TYR A 1 178 ? 25.159 46.494 22.533 1.00 23.52 ? 361  TYR A HD1    1 
ATOM   3056 H HD2    . TYR A 1 178 ? 22.376 47.261 19.773 1.00 24.67 ? 361  TYR A HD2    1 
ATOM   3057 H HE1    . TYR A 1 178 ? 26.248 45.137 21.038 1.00 26.01 ? 361  TYR A HE1    1 
ATOM   3058 H HE2    . TYR A 1 178 ? 23.448 45.883 18.292 1.00 25.67 ? 361  TYR A HE2    1 
ATOM   3059 H HH     . TYR A 1 178 ? 25.232 44.532 17.903 1.00 30.10 ? 361  TYR A HH     1 
ATOM   3060 N N      . ILE A 1 179 ? 23.156 50.711 23.993 1.00 16.71 ? 362  ILE A N      1 
ATOM   3061 C CA     . ILE A 1 179 ? 22.425 51.880 24.461 1.00 16.82 ? 362  ILE A CA     1 
ATOM   3062 C C      . ILE A 1 179 ? 21.810 52.560 23.239 1.00 16.27 ? 362  ILE A C      1 
ATOM   3063 O O      . ILE A 1 179 ? 22.495 52.771 22.244 1.00 17.69 ? 362  ILE A O      1 
ATOM   3064 C CB     . ILE A 1 179 ? 23.354 52.894 25.162 1.00 19.22 ? 362  ILE A CB     1 
ATOM   3065 C CG1    . ILE A 1 179 ? 24.312 52.216 26.141 1.00 23.34 ? 362  ILE A CG1    1 
ATOM   3066 C CG2    . ILE A 1 179 ? 22.516 53.993 25.835 1.00 20.68 ? 362  ILE A CG2    1 
ATOM   3067 C CD1    . ILE A 1 179 ? 23.627 51.602 27.257 1.00 23.65 ? 362  ILE A CD1    1 
ATOM   3068 H H      . ILE A 1 179 ? 23.880 50.908 23.572 1.00 20.05 ? 362  ILE A H      1 
ATOM   3069 H HA     . ILE A 1 179 ? 21.736 51.588 25.078 1.00 20.18 ? 362  ILE A HA     1 
ATOM   3070 H HB     . ILE A 1 179 ? 23.915 53.307 24.486 1.00 23.06 ? 362  ILE A HB     1 
ATOM   3071 H HG12   . ILE A 1 179 ? 24.805 51.524 25.673 1.00 28.01 ? 362  ILE A HG12   1 
ATOM   3072 H HG13   . ILE A 1 179 ? 24.925 52.880 26.493 1.00 28.01 ? 362  ILE A HG13   1 
ATOM   3073 H HG21   . ILE A 1 179 ? 23.104 54.570 26.346 1.00 24.82 ? 362  ILE A HG21   1 
ATOM   3074 H HG22   . ILE A 1 179 ? 22.061 54.508 25.149 1.00 24.82 ? 362  ILE A HG22   1 
ATOM   3075 H HG23   . ILE A 1 179 ? 21.865 53.578 26.423 1.00 24.82 ? 362  ILE A HG23   1 
ATOM   3076 H HD11   . ILE A 1 179 ? 24.283 51.201 27.848 1.00 28.38 ? 362  ILE A HD11   1 
ATOM   3077 H HD12   . ILE A 1 179 ? 23.125 52.283 27.733 1.00 28.38 ? 362  ILE A HD12   1 
ATOM   3078 H HD13   . ILE A 1 179 ? 23.024 50.921 26.921 1.00 28.38 ? 362  ILE A HD13   1 
ATOM   3079 N N      . TYR A 1 180 ? 20.525 52.908 23.313 1.00 15.14 ? 363  TYR A N      1 
ATOM   3080 C CA     . TYR A 1 180 ? 19.791 53.546 22.207 1.00 15.47 ? 363  TYR A CA     1 
ATOM   3081 C C      . TYR A 1 180 ? 19.337 54.926 22.677 1.00 15.60 ? 363  TYR A C      1 
ATOM   3082 O O      . TYR A 1 180 ? 18.559 55.037 23.643 1.00 15.89 ? 363  TYR A O      1 
ATOM   3083 C CB     . TYR A 1 180 ? 18.581 52.706 21.813 1.00 15.50 ? 363  TYR A CB     1 
ATOM   3084 C CG     . TYR A 1 180 ? 18.884 51.317 21.270 1.00 15.35 ? 363  TYR A CG     1 
ATOM   3085 C CD1    . TYR A 1 180 ? 19.157 50.254 22.107 1.00 16.08 ? 363  TYR A CD1    1 
ATOM   3086 C CD2    . TYR A 1 180 ? 18.896 51.106 19.910 1.00 16.34 ? 363  TYR A CD2    1 
ATOM   3087 C CE1    . TYR A 1 180 ? 19.429 48.995 21.583 1.00 17.07 ? 363  TYR A CE1    1 
ATOM   3088 C CE2    . TYR A 1 180 ? 19.166 49.890 19.388 1.00 16.00 ? 363  TYR A CE2    1 
ATOM   3089 C CZ     . TYR A 1 180 ? 19.429 48.817 20.236 1.00 17.11 ? 363  TYR A CZ     1 
ATOM   3090 O OH     . TYR A 1 180 ? 19.707 47.577 19.701 1.00 19.47 ? 363  TYR A OH     1 
ATOM   3091 H H      . TYR A 1 180 ? 20.039 52.783 24.011 1.00 18.16 ? 363  TYR A H      1 
ATOM   3092 H HA     . TYR A 1 180 ? 20.377 53.645 21.441 1.00 18.56 ? 363  TYR A HA     1 
ATOM   3093 H HB2    . TYR A 1 180 ? 18.022 52.591 22.597 1.00 18.60 ? 363  TYR A HB2    1 
ATOM   3094 H HB3    . TYR A 1 180 ? 18.091 53.183 21.124 1.00 18.60 ? 363  TYR A HB3    1 
ATOM   3095 H HD1    . TYR A 1 180 ? 19.158 50.380 23.029 1.00 19.30 ? 363  TYR A HD1    1 
ATOM   3096 H HD2    . TYR A 1 180 ? 18.714 51.816 19.338 1.00 19.61 ? 363  TYR A HD2    1 
ATOM   3097 H HE1    . TYR A 1 180 ? 19.611 48.281 22.150 1.00 20.49 ? 363  TYR A HE1    1 
ATOM   3098 H HE2    . TYR A 1 180 ? 19.176 49.769 18.466 1.00 19.20 ? 363  TYR A HE2    1 
ATOM   3099 H HH     . TYR A 1 180 ? 19.821 47.017 20.316 1.00 23.36 ? 363  TYR A HH     1 
ATOM   3100 N N      . TYR A 1 181 ? 19.878 55.956 22.046 1.00 15.04 ? 364  TYR A N      1 
ATOM   3101 C CA     . TYR A 1 181 ? 19.599 57.332 22.440 1.00 15.69 ? 364  TYR A CA     1 
ATOM   3102 C C      . TYR A 1 181 ? 18.361 57.844 21.723 1.00 16.86 ? 364  TYR A C      1 
ATOM   3103 O O      . TYR A 1 181 ? 18.073 57.468 20.584 1.00 17.74 ? 364  TYR A O      1 
ATOM   3104 C CB     . TYR A 1 181 ? 20.781 58.256 22.115 1.00 16.67 ? 364  TYR A CB     1 
ATOM   3105 C CG     . TYR A 1 181 ? 22.078 57.823 22.754 1.00 15.93 ? 364  TYR A CG     1 
ATOM   3106 C CD1    . TYR A 1 181 ? 22.203 57.727 24.131 1.00 16.59 ? 364  TYR A CD1    1 
ATOM   3107 C CD2    . TYR A 1 181 ? 23.182 57.488 21.977 1.00 18.24 ? 364  TYR A CD2    1 
ATOM   3108 C CE1    . TYR A 1 181 ? 23.422 57.292 24.721 1.00 18.64 ? 364  TYR A CE1    1 
ATOM   3109 C CE2    . TYR A 1 181 ? 24.379 57.063 22.549 1.00 20.57 ? 364  TYR A CE2    1 
ATOM   3110 C CZ     . TYR A 1 181 ? 24.486 56.955 23.922 1.00 19.83 ? 364  TYR A CZ     1 
ATOM   3111 O OH     . TYR A 1 181 ? 25.684 56.553 24.488 1.00 21.34 ? 364  TYR A OH     1 
ATOM   3112 H H      . TYR A 1 181 ? 20.415 55.885 21.379 1.00 18.05 ? 364  TYR A H      1 
ATOM   3113 H HA     . TYR A 1 181 ? 19.449 57.358 23.398 1.00 18.83 ? 364  TYR A HA     1 
ATOM   3114 H HB2    . TYR A 1 181 ? 20.913 58.268 21.154 1.00 20.01 ? 364  TYR A HB2    1 
ATOM   3115 H HB3    . TYR A 1 181 ? 20.576 59.149 22.433 1.00 20.01 ? 364  TYR A HB3    1 
ATOM   3116 H HD1    . TYR A 1 181 ? 21.482 57.948 24.675 1.00 19.90 ? 364  TYR A HD1    1 
ATOM   3117 H HD2    . TYR A 1 181 ? 23.120 57.550 21.052 1.00 21.89 ? 364  TYR A HD2    1 
ATOM   3118 H HE1    . TYR A 1 181 ? 23.499 57.237 25.646 1.00 22.37 ? 364  TYR A HE1    1 
ATOM   3119 H HE2    . TYR A 1 181 ? 25.105 56.852 22.007 1.00 24.68 ? 364  TYR A HE2    1 
ATOM   3120 H HH     . TYR A 1 181 ? 25.609 56.518 25.324 1.00 25.61 ? 364  TYR A HH     1 
ATOM   3121 N N      . HIS A 1 182 ? 17.679 58.777 22.370 1.00 17.59 ? 365  HIS A N      1 
ATOM   3122 C CA     . HIS A 1 182 ? 16.539 59.438 21.756 1.00 18.99 ? 365  HIS A CA     1 
ATOM   3123 C C      . HIS A 1 182 ? 16.987 60.367 20.625 1.00 19.77 ? 365  HIS A C      1 
ATOM   3124 O O      . HIS A 1 182 ? 18.033 61.018 20.696 1.00 19.21 ? 365  HIS A O      1 
ATOM   3125 C CB     . HIS A 1 182 ? 15.802 60.189 22.858 1.00 19.93 ? 365  HIS A CB     1 
ATOM   3126 C CG     . HIS A 1 182 ? 14.437 60.637 22.475 1.00 20.89 ? 365  HIS A CG     1 
ATOM   3127 N ND1    . HIS A 1 182 ? 14.205 61.661 21.578 1.00 21.81 ? 365  HIS A ND1    1 
ATOM   3128 C CD2    . HIS A 1 182 ? 13.225 60.179 22.862 1.00 21.98 ? 365  HIS A CD2    1 
ATOM   3129 C CE1    . HIS A 1 182 ? 12.903 61.782 21.413 1.00 22.58 ? 365  HIS A CE1    1 
ATOM   3130 N NE2    . HIS A 1 182 ? 12.285 60.916 22.193 1.00 22.93 ? 365  HIS A NE2    1 
ATOM   3131 H H      . HIS A 1 182 ? 17.856 59.047 23.167 1.00 21.11 ? 365  HIS A H      1 
ATOM   3132 H HA     . HIS A 1 182 ? 15.932 58.802 21.346 1.00 22.79 ? 365  HIS A HA     1 
ATOM   3133 H HB2    . HIS A 1 182 ? 15.716 59.605 23.628 1.00 23.91 ? 365  HIS A HB2    1 
ATOM   3134 H HB3    . HIS A 1 182 ? 16.316 60.976 23.095 1.00 23.91 ? 365  HIS A HB3    1 
ATOM   3135 H HD2    . HIS A 1 182 ? 13.061 59.493 23.469 1.00 26.37 ? 365  HIS A HD2    1 
ATOM   3136 H HE1    . HIS A 1 182 ? 12.487 62.383 20.838 1.00 27.10 ? 365  HIS A HE1    1 
ATOM   3137 H HE2    . HIS A 1 182 ? 11.433 60.828 22.269 1.00 27.52 ? 365  HIS A HE2    1 
ATOM   3138 N N      . SER A 1 183 ? 16.190 60.410 19.565 1.00 21.39 ? 366  SER A N      1 
ATOM   3139 C CA     . SER A 1 183 ? 16.511 61.245 18.403 1.00 22.59 ? 366  SER A CA     1 
ATOM   3140 C C      . SER A 1 183 ? 16.759 62.706 18.764 1.00 23.26 ? 366  SER A C      1 
ATOM   3141 O O      . SER A 1 183 ? 17.562 63.369 18.099 1.00 25.52 ? 366  SER A O      1 
ATOM   3142 C CB     . SER A 1 183 ? 15.380 61.159 17.384 1.00 23.39 ? 366  SER A CB     1 
ATOM   3143 O OG     . SER A 1 183 ? 14.204 61.741 17.934 1.00 22.69 ? 366  SER A OG     1 
ATOM   3144 H H      . SER A 1 183 ? 15.457 59.967 19.487 1.00 25.67 ? 366  SER A H      1 
ATOM   3145 H HA     . SER A 1 183 ? 17.328 60.903 18.008 1.00 27.10 ? 366  SER A HA     1 
ATOM   3146 H HB2    . SER A 1 183 ? 15.633 61.642 16.581 1.00 28.07 ? 366  SER A HB2    1 
ATOM   3147 H HB3    . SER A 1 183 ? 15.210 60.228 17.171 1.00 28.07 ? 366  SER A HB3    1 
ATOM   3148 H HG     . SER A 1 183 ? 13.983 61.334 18.635 1.00 27.22 ? 366  SER A HG     1 
ATOM   3149 N N      . LYS A 1 184 ? 16.079 63.232 19.792 1.00 22.07 ? 367  LYS A N      1 
ATOM   3150 C CA     A LYS A 1 184 ? 16.243 64.627 20.180 0.59 23.21 ? 367  LYS A CA     1 
ATOM   3151 C CA     B LYS A 1 184 ? 16.235 64.628 20.188 0.41 23.35 ? 367  LYS A CA     1 
ATOM   3152 C C      . LYS A 1 184 ? 17.464 64.871 21.049 1.00 23.32 ? 367  LYS A C      1 
ATOM   3153 O O      . LYS A 1 184 ? 17.762 66.034 21.368 1.00 23.19 ? 367  LYS A O      1 
ATOM   3154 C CB     A LYS A 1 184 ? 14.971 65.091 20.881 0.59 25.88 ? 367  LYS A CB     1 
ATOM   3155 C CB     B LYS A 1 184 ? 14.997 65.102 20.950 0.41 25.44 ? 367  LYS A CB     1 
ATOM   3156 C CG     A LYS A 1 184 ? 13.766 64.931 19.955 0.59 28.07 ? 367  LYS A CG     1 
ATOM   3157 C CG     B LYS A 1 184 ? 14.994 64.765 22.424 0.41 27.69 ? 367  LYS A CG     1 
ATOM   3158 C CD     A LYS A 1 184 ? 12.481 65.497 20.523 0.59 31.23 ? 367  LYS A CD     1 
ATOM   3159 C CD     B LYS A 1 184 ? 13.674 65.154 23.080 0.41 29.81 ? 367  LYS A CD     1 
ATOM   3160 C CE     A LYS A 1 184 ? 11.376 65.482 19.472 0.59 34.91 ? 367  LYS A CE     1 
ATOM   3161 C CE     B LYS A 1 184 ? 13.464 64.391 24.385 0.41 30.98 ? 367  LYS A CE     1 
ATOM   3162 N NZ     A LYS A 1 184 ? 10.061 65.897 20.037 0.59 36.61 ? 367  LYS A NZ     1 
ATOM   3163 N NZ     B LYS A 1 184 ? 12.137 64.696 24.988 0.41 31.48 ? 367  LYS A NZ     1 
ATOM   3164 H H      A LYS A 1 184 ? 15.518 62.796 20.277 0.59 26.48 ? 367  LYS A H      1 
ATOM   3165 H H      B LYS A 1 184 ? 15.519 62.794 20.276 0.41 26.48 ? 367  LYS A H      1 
ATOM   3166 H HA     A LYS A 1 184 ? 16.366 65.174 19.389 0.59 27.85 ? 367  LYS A HA     1 
ATOM   3167 H HA     B LYS A 1 184 ? 16.321 65.162 19.383 0.41 28.02 ? 367  LYS A HA     1 
ATOM   3168 H HB2    A LYS A 1 184 ? 14.825 64.556 21.676 0.59 31.06 ? 367  LYS A HB2    1 
ATOM   3169 H HB2    B LYS A 1 184 ? 14.938 66.067 20.871 0.41 30.53 ? 367  LYS A HB2    1 
ATOM   3170 H HB3    A LYS A 1 184 ? 15.056 66.027 21.121 0.59 31.06 ? 367  LYS A HB3    1 
ATOM   3171 H HB3    B LYS A 1 184 ? 14.215 64.688 20.553 0.41 30.53 ? 367  LYS A HB3    1 
ATOM   3172 H HG2    A LYS A 1 184 ? 13.948 65.391 19.121 0.59 33.68 ? 367  LYS A HG2    1 
ATOM   3173 H HG2    B LYS A 1 184 ? 15.120 63.809 22.535 0.41 33.22 ? 367  LYS A HG2    1 
ATOM   3174 H HG3    A LYS A 1 184 ? 13.623 63.986 19.788 0.59 33.68 ? 367  LYS A HG3    1 
ATOM   3175 H HG3    B LYS A 1 184 ? 15.709 65.248 22.866 0.41 33.22 ? 367  LYS A HG3    1 
ATOM   3176 H HD2    A LYS A 1 184 ? 12.195 64.961 21.279 0.59 37.48 ? 367  LYS A HD2    1 
ATOM   3177 H HD2    B LYS A 1 184 ? 13.679 66.103 23.277 0.41 35.78 ? 367  LYS A HD2    1 
ATOM   3178 H HD3    A LYS A 1 184 ? 12.626 66.414 20.804 0.59 37.48 ? 367  LYS A HD3    1 
ATOM   3179 H HD3    B LYS A 1 184 ? 12.941 64.943 22.480 0.41 35.78 ? 367  LYS A HD3    1 
ATOM   3180 H HE2    A LYS A 1 184 ? 11.607 66.096 18.758 0.59 41.90 ? 367  LYS A HE2    1 
ATOM   3181 H HE2    B LYS A 1 184 ? 13.508 63.438 24.210 0.41 37.17 ? 367  LYS A HE2    1 
ATOM   3182 H HE3    A LYS A 1 184 ? 11.284 64.583 19.119 0.59 41.90 ? 367  LYS A HE3    1 
ATOM   3183 H HE3    B LYS A 1 184 ? 14.153 64.644 25.019 0.41 37.17 ? 367  LYS A HE3    1 
ATOM   3184 H HZ1    A LYS A 1 184 ? 9.440  65.891 19.400 0.59 43.93 ? 367  LYS A HZ1    1 
ATOM   3185 H HZ1    B LYS A 1 184 ? 12.023 64.218 25.730 0.41 37.78 ? 367  LYS A HZ1    1 
ATOM   3186 H HZ2    A LYS A 1 184 ? 9.817  65.336 20.684 0.59 43.93 ? 367  LYS A HZ2    1 
ATOM   3187 H HZ2    B LYS A 1 184 ? 12.087 65.561 25.192 0.41 37.78 ? 367  LYS A HZ2    1 
ATOM   3188 H HZ3    A LYS A 1 184 ? 10.121 66.718 20.375 0.59 43.93 ? 367  LYS A HZ3    1 
ATOM   3189 H HZ3    B LYS A 1 184 ? 11.488 64.497 24.413 0.41 37.78 ? 367  LYS A HZ3    1 
ATOM   3190 N N      . ASN A 1 185 ? 18.161 63.828 21.428 1.00 22.87 ? 368  ASN A N      1 
ATOM   3191 C CA     A ASN A 1 185 ? 19.488 63.918 22.010 0.51 22.62 ? 368  ASN A CA     1 
ATOM   3192 C CA     B ASN A 1 185 ? 19.488 63.909 22.015 0.49 22.78 ? 368  ASN A CA     1 
ATOM   3193 C C      . ASN A 1 185 ? 20.543 63.406 21.031 1.00 23.30 ? 368  ASN A C      1 
ATOM   3194 O O      . ASN A 1 185 ? 21.555 62.833 21.432 1.00 25.93 ? 368  ASN A O      1 
ATOM   3195 C CB     A ASN A 1 185 ? 19.539 63.165 23.338 0.51 23.94 ? 368  ASN A CB     1 
ATOM   3196 C CB     B ASN A 1 185 ? 19.556 63.128 23.328 0.49 24.29 ? 368  ASN A CB     1 
ATOM   3197 C CG     A ASN A 1 185 ? 20.183 63.976 24.425 0.51 28.31 ? 368  ASN A CG     1 
ATOM   3198 C CG     B ASN A 1 185 ? 20.858 63.350 24.060 0.49 28.57 ? 368  ASN A CG     1 
ATOM   3199 O OD1    A ASN A 1 185 ? 21.077 64.786 24.159 0.51 30.61 ? 368  ASN A OD1    1 
ATOM   3200 O OD1    B ASN A 1 185 ? 21.472 64.411 23.925 0.49 31.01 ? 368  ASN A OD1    1 
ATOM   3201 N ND2    A ASN A 1 185 ? 19.728 63.790 25.653 0.51 29.25 ? 368  ASN A ND2    1 
ATOM   3202 N ND2    B ASN A 1 185 ? 21.304 62.353 24.818 0.49 28.97 ? 368  ASN A ND2    1 
ATOM   3203 H H      A ASN A 1 185 ? 17.880 63.018 21.358 0.51 27.45 ? 368  ASN A H      1 
ATOM   3204 H H      B ASN A 1 185 ? 17.879 63.019 21.355 0.49 27.45 ? 368  ASN A H      1 
ATOM   3205 H HA     A ASN A 1 185 ? 19.698 64.844 22.207 0.51 27.14 ? 368  ASN A HA     1 
ATOM   3206 H HA     B ASN A 1 185 ? 19.683 64.835 22.228 0.49 27.34 ? 368  ASN A HA     1 
ATOM   3207 H HB2    A ASN A 1 185 ? 18.635 62.950 23.616 0.51 28.72 ? 368  ASN A HB2    1 
ATOM   3208 H HB2    B ASN A 1 185 ? 18.832 63.414 23.906 0.49 29.15 ? 368  ASN A HB2    1 
ATOM   3209 H HB3    A ASN A 1 185 ? 20.053 62.351 23.223 0.51 28.72 ? 368  ASN A HB3    1 
ATOM   3210 H HB3    B ASN A 1 185 ? 19.475 62.180 23.138 0.49 29.15 ? 368  ASN A HB3    1 
ATOM   3211 H HD21   A ASN A 1 185 ? 20.066 64.232 26.308 0.51 35.10 ? 368  ASN A HD21   1 
ATOM   3212 H HD21   B ASN A 1 185 ? 22.042 62.440 25.251 0.49 34.76 ? 368  ASN A HD21   1 
ATOM   3213 H HD22   A ASN A 1 185 ? 19.094 63.227 25.795 0.51 35.10 ? 368  ASN A HD22   1 
ATOM   3214 H HD22   B ASN A 1 185 ? 20.856 61.622 24.874 0.49 34.76 ? 368  ASN A HD22   1 
ATOM   3215 N N      . GLY A 1 186 ? 20.294 63.551 19.745 1.00 23.70 ? 369  GLY A N      1 
ATOM   3216 C CA     . GLY A 1 186 ? 21.268 63.141 18.755 1.00 24.48 ? 369  GLY A CA     1 
ATOM   3217 C C      . GLY A 1 186 ? 21.051 61.768 18.160 1.00 24.65 ? 369  GLY A C      1 
ATOM   3218 O O      . GLY A 1 186 ? 21.674 61.453 17.137 1.00 25.28 ? 369  GLY A O      1 
ATOM   3219 H H      . GLY A 1 186 ? 19.570 63.883 19.421 1.00 28.45 ? 369  GLY A H      1 
ATOM   3220 H HA2    . GLY A 1 186 ? 21.255 63.782 18.026 1.00 29.38 ? 369  GLY A HA2    1 
ATOM   3221 H HA3    . GLY A 1 186 ? 22.146 63.147 19.165 1.00 29.38 ? 369  GLY A HA3    1 
ATOM   3222 N N      . GLY A 1 187 ? 20.194 60.950 18.763 1.00 21.90 ? 370  GLY A N      1 
ATOM   3223 C CA     . GLY A 1 187 ? 19.871 59.650 18.188 1.00 20.66 ? 370  GLY A CA     1 
ATOM   3224 C C      . GLY A 1 187 ? 21.079 58.730 18.138 1.00 19.75 ? 370  GLY A C      1 
ATOM   3225 O O      . GLY A 1 187 ? 22.081 58.917 18.815 1.00 20.69 ? 370  GLY A O      1 
ATOM   3226 H H      . GLY A 1 187 ? 19.789 61.121 19.502 1.00 26.29 ? 370  GLY A H      1 
ATOM   3227 H HA2    . GLY A 1 187 ? 19.183 59.223 18.722 1.00 24.80 ? 370  GLY A HA2    1 
ATOM   3228 H HA3    . GLY A 1 187 ? 19.540 59.771 17.284 1.00 24.80 ? 370  GLY A HA3    1 
ATOM   3229 N N      . GLY A 1 188 ? 20.959 57.722 17.290 1.00 19.03 ? 371  GLY A N      1 
ATOM   3230 C CA     . GLY A 1 188 ? 21.959 56.698 17.251 1.00 18.31 ? 371  GLY A CA     1 
ATOM   3231 C C      . GLY A 1 188 ? 22.024 55.959 18.587 1.00 16.61 ? 371  GLY A C      1 
ATOM   3232 O O      . GLY A 1 188 ? 21.122 56.019 19.444 1.00 17.31 ? 371  GLY A O      1 
ATOM   3233 H H      . GLY A 1 188 ? 20.310 57.616 16.735 1.00 22.84 ? 371  GLY A H      1 
ATOM   3234 H HA2    . GLY A 1 188 ? 21.749 56.061 16.550 1.00 21.98 ? 371  GLY A HA2    1 
ATOM   3235 H HA3    . GLY A 1 188 ? 22.826 57.093 17.069 1.00 21.98 ? 371  GLY A HA3    1 
ATOM   3236 N N      . GLY A 1 189 ? 23.127 55.235 18.757 1.00 17.08 ? 372  GLY A N      1 
ATOM   3237 C CA     . GLY A 1 189 ? 23.312 54.383 19.922 1.00 18.07 ? 372  GLY A CA     1 
ATOM   3238 C C      . GLY A 1 189 ? 24.780 54.077 20.128 1.00 18.95 ? 372  GLY A C      1 
ATOM   3239 O O      . GLY A 1 189 ? 25.647 54.514 19.371 1.00 19.63 ? 372  GLY A O      1 
ATOM   3240 H H      . GLY A 1 189 ? 23.788 55.221 18.206 1.00 20.50 ? 372  GLY A H      1 
ATOM   3241 H HA2    . GLY A 1 189 ? 22.971 54.828 20.713 1.00 21.68 ? 372  GLY A HA2    1 
ATOM   3242 H HA3    . GLY A 1 189 ? 22.833 53.548 19.798 1.00 21.68 ? 372  GLY A HA3    1 
ATOM   3243 N N      . ARG A 1 190 ? 25.044 53.255 21.138 1.00 18.68 ? 373  ARG A N      1 
ATOM   3244 C CA     . ARG A 1 190 ? 26.402 52.915 21.513 1.00 19.70 ? 373  ARG A CA     1 
ATOM   3245 C C      . ARG A 1 190 ? 26.405 51.439 21.857 1.00 19.12 ? 373  ARG A C      1 
ATOM   3246 O O      . ARG A 1 190 ? 25.562 50.987 22.628 1.00 20.37 ? 373  ARG A O      1 
ATOM   3247 C CB     . ARG A 1 190 ? 26.813 53.745 22.733 1.00 22.38 ? 373  ARG A CB     1 
ATOM   3248 C CG     . ARG A 1 190 ? 28.195 53.501 23.220 1.00 24.55 ? 373  ARG A CG     1 
ATOM   3249 C CD     . ARG A 1 190 ? 28.542 54.522 24.301 1.00 25.00 ? 373  ARG A CD     1 
ATOM   3250 N NE     . ARG A 1 190 ? 28.533 55.891 23.788 1.00 26.02 ? 373  ARG A NE     1 
ATOM   3251 C CZ     . ARG A 1 190 ? 29.542 56.455 23.132 1.00 30.13 ? 373  ARG A CZ     1 
ATOM   3252 N NH1    . ARG A 1 190 ? 30.644 55.775 22.833 1.00 32.96 ? 373  ARG A NH1    1 
ATOM   3253 N NH2    . ARG A 1 190 ? 29.446 57.730 22.766 1.00 31.49 ? 373  ARG A NH2    1 
ATOM   3254 H H      . ARG A 1 190 ? 24.443 52.879 21.624 1.00 22.42 ? 373  ARG A H      1 
ATOM   3255 H HA     . ARG A 1 190 ? 27.034 53.078 20.795 1.00 23.65 ? 373  ARG A HA     1 
ATOM   3256 H HB2    . ARG A 1 190 ? 26.747 54.684 22.501 1.00 26.86 ? 373  ARG A HB2    1 
ATOM   3257 H HB3    . ARG A 1 190 ? 26.207 53.540 23.462 1.00 26.86 ? 373  ARG A HB3    1 
ATOM   3258 H HG2    . ARG A 1 190 ? 28.258 52.610 23.599 1.00 29.47 ? 373  ARG A HG2    1 
ATOM   3259 H HG3    . ARG A 1 190 ? 28.823 53.595 22.487 1.00 29.47 ? 373  ARG A HG3    1 
ATOM   3260 H HD2    . ARG A 1 190 ? 27.889 54.463 25.016 1.00 30.00 ? 373  ARG A HD2    1 
ATOM   3261 H HD3    . ARG A 1 190 ? 29.429 54.334 24.644 1.00 30.00 ? 373  ARG A HD3    1 
ATOM   3262 H HE     . ARG A 1 190 ? 27.827 56.365 23.921 1.00 31.23 ? 373  ARG A HE     1 
ATOM   3263 H HH11   . ARG A 1 190 ? 30.717 54.950 23.065 1.00 39.56 ? 373  ARG A HH11   1 
ATOM   3264 H HH12   . ARG A 1 190 ? 31.285 56.159 22.407 1.00 39.56 ? 373  ARG A HH12   1 
ATOM   3265 H HH21   . ARG A 1 190 ? 28.738 58.180 22.955 1.00 37.79 ? 373  ARG A HH21   1 
ATOM   3266 H HH22   . ARG A 1 190 ? 30.093 58.105 22.340 1.00 37.79 ? 373  ARG A HH22   1 
ATOM   3267 N N      . ARG A 1 191 ? 27.336 50.696 21.273 1.00 19.46 ? 374  ARG A N      1 
ATOM   3268 C CA     . ARG A 1 191 ? 27.560 49.305 21.625 1.00 20.83 ? 374  ARG A CA     1 
ATOM   3269 C C      . ARG A 1 191 ? 28.689 49.242 22.647 1.00 21.71 ? 374  ARG A C      1 
ATOM   3270 O O      . ARG A 1 191 ? 29.808 49.718 22.379 1.00 23.90 ? 374  ARG A O      1 
ATOM   3271 C CB     . ARG A 1 191 ? 27.931 48.506 20.382 1.00 20.56 ? 374  ARG A CB     1 
ATOM   3272 C CG     . ARG A 1 191 ? 26.864 48.496 19.277 1.00 19.54 ? 374  ARG A CG     1 
ATOM   3273 C CD     . ARG A 1 191 ? 27.339 47.667 18.108 1.00 21.70 ? 374  ARG A CD     1 
ATOM   3274 N NE     . ARG A 1 191 ? 26.319 47.462 17.091 1.00 23.91 ? 374  ARG A NE     1 
ATOM   3275 C CZ     . ARG A 1 191 ? 26.050 48.347 16.142 1.00 26.12 ? 374  ARG A CZ     1 
ATOM   3276 N NH1    . ARG A 1 191 ? 26.680 49.501 16.093 1.00 25.83 ? 374  ARG A NH1    1 
ATOM   3277 N NH2    . ARG A 1 191 ? 25.135 48.058 15.216 1.00 27.67 ? 374  ARG A NH2    1 
ATOM   3278 H H      . ARG A 1 191 ? 27.861 50.984 20.656 1.00 23.36 ? 374  ARG A H      1 
ATOM   3279 H HA     . ARG A 1 191 ? 26.758 48.925 22.018 1.00 25.00 ? 374  ARG A HA     1 
ATOM   3280 H HB2    . ARG A 1 191 ? 28.739 48.885 20.003 1.00 24.67 ? 374  ARG A HB2    1 
ATOM   3281 H HB3    . ARG A 1 191 ? 28.088 47.585 20.644 1.00 24.67 ? 374  ARG A HB3    1 
ATOM   3282 H HG2    . ARG A 1 191 ? 26.043 48.109 19.620 1.00 23.45 ? 374  ARG A HG2    1 
ATOM   3283 H HG3    . ARG A 1 191 ? 26.701 49.402 18.971 1.00 23.45 ? 374  ARG A HG3    1 
ATOM   3284 H HD2    . ARG A 1 191 ? 28.089 48.117 17.689 1.00 26.04 ? 374  ARG A HD2    1 
ATOM   3285 H HD3    . ARG A 1 191 ? 27.614 46.796 18.432 1.00 26.04 ? 374  ARG A HD3    1 
ATOM   3286 H HE     . ARG A 1 191 ? 25.869 46.730 17.106 1.00 28.70 ? 374  ARG A HE     1 
ATOM   3287 H HH11   . ARG A 1 191 ? 27.278 49.691 16.682 1.00 30.99 ? 374  ARG A HH11   1 
ATOM   3288 H HH12   . ARG A 1 191 ? 26.495 50.066 15.472 1.00 30.99 ? 374  ARG A HH12   1 
ATOM   3289 H HH21   . ARG A 1 191 ? 24.725 47.302 15.238 1.00 33.20 ? 374  ARG A HH21   1 
ATOM   3290 H HH22   . ARG A 1 191 ? 24.954 48.627 14.597 1.00 33.20 ? 374  ARG A HH22   1 
ATOM   3291 N N      . LEU A 1 192 ? 28.387 48.695 23.815 1.00 20.99 ? 375  LEU A N      1 
ATOM   3292 C CA     . LEU A 1 192 ? 29.398 48.430 24.820 1.00 23.01 ? 375  LEU A CA     1 
ATOM   3293 C C      . LEU A 1 192 ? 29.886 46.997 24.647 1.00 26.00 ? 375  LEU A C      1 
ATOM   3294 O O      . LEU A 1 192 ? 29.127 46.104 24.251 1.00 26.48 ? 375  LEU A O      1 
ATOM   3295 C CB     . LEU A 1 192 ? 28.810 48.575 26.215 1.00 23.63 ? 375  LEU A CB     1 
ATOM   3296 C CG     . LEU A 1 192 ? 27.943 49.788 26.494 1.00 25.05 ? 375  LEU A CG     1 
ATOM   3297 C CD1    . LEU A 1 192 ? 27.417 49.719 27.914 1.00 25.65 ? 375  LEU A CD1    1 
ATOM   3298 C CD2    . LEU A 1 192 ? 28.714 51.076 26.284 1.00 27.19 ? 375  LEU A CD2    1 
ATOM   3299 H H      . LEU A 1 192 ? 27.592 48.465 24.050 1.00 25.19 ? 375  LEU A H      1 
ATOM   3300 H HA     . LEU A 1 192 ? 30.136 49.054 24.729 1.00 27.61 ? 375  LEU A HA     1 
ATOM   3301 H HB2    . LEU A 1 192 ? 28.261 47.794 26.387 1.00 28.35 ? 375  LEU A HB2    1 
ATOM   3302 H HB3    . LEU A 1 192 ? 29.547 48.607 26.845 1.00 28.35 ? 375  LEU A HB3    1 
ATOM   3303 H HG     . LEU A 1 192 ? 27.196 49.792 25.874 1.00 30.06 ? 375  LEU A HG     1 
ATOM   3304 H HD11   . LEU A 1 192 ? 26.852 50.490 28.080 1.00 30.78 ? 375  LEU A HD11   1 
ATOM   3305 H HD12   . LEU A 1 192 ? 26.902 48.904 28.022 1.00 30.78 ? 375  LEU A HD12   1 
ATOM   3306 H HD13   . LEU A 1 192 ? 28.167 49.720 28.529 1.00 30.78 ? 375  LEU A HD13   1 
ATOM   3307 H HD21   . LEU A 1 192 ? 28.129 51.828 26.468 1.00 32.63 ? 375  LEU A HD21   1 
ATOM   3308 H HD22   . LEU A 1 192 ? 29.473 51.092 26.888 1.00 32.63 ? 375  LEU A HD22   1 
ATOM   3309 H HD23   . LEU A 1 192 ? 29.022 51.114 25.365 1.00 32.63 ? 375  LEU A HD23   1 
ATOM   3310 N N      . PHE A 1 193 ? 31.160 46.783 24.932 1.00 31.50 ? 376  PHE A N      1 
ATOM   3311 C CA     . PHE A 1 193 ? 31.711 45.444 24.841 1.00 36.93 ? 376  PHE A CA     1 
ATOM   3312 C C      . PHE A 1 193 ? 32.884 45.336 25.794 1.00 39.58 ? 376  PHE A C      1 
ATOM   3313 O O      . PHE A 1 193 ? 33.319 46.324 26.389 1.00 37.64 ? 376  PHE A O      1 
ATOM   3314 C CB     . PHE A 1 193 ? 32.093 45.050 23.400 1.00 40.17 ? 376  PHE A CB     1 
ATOM   3315 C CG     . PHE A 1 193 ? 32.833 46.105 22.649 1.00 42.26 ? 376  PHE A CG     1 
ATOM   3316 C CD1    . PHE A 1 193 ? 32.146 47.094 21.964 1.00 42.96 ? 376  PHE A CD1    1 
ATOM   3317 C CD2    . PHE A 1 193 ? 34.219 46.096 22.594 1.00 44.14 ? 376  PHE A CD2    1 
ATOM   3318 C CE1    . PHE A 1 193 ? 32.826 48.071 21.263 1.00 44.23 ? 376  PHE A CE1    1 
ATOM   3319 C CE2    . PHE A 1 193 ? 34.908 47.072 21.883 1.00 45.03 ? 376  PHE A CE2    1 
ATOM   3320 C CZ     . PHE A 1 193 ? 34.207 48.060 21.220 1.00 45.33 ? 376  PHE A CZ     1 
ATOM   3321 H H      . PHE A 1 193 ? 31.718 47.390 25.178 1.00 37.80 ? 376  PHE A H      1 
ATOM   3322 H HA     . PHE A 1 193 ? 31.035 44.808 25.125 1.00 44.32 ? 376  PHE A HA     1 
ATOM   3323 H HB2    . PHE A 1 193 ? 32.659 44.263 23.434 1.00 48.20 ? 376  PHE A HB2    1 
ATOM   3324 H HB3    . PHE A 1 193 ? 31.281 44.854 22.907 1.00 48.20 ? 376  PHE A HB3    1 
ATOM   3325 H HD1    . PHE A 1 193 ? 31.216 47.100 21.977 1.00 51.56 ? 376  PHE A HD1    1 
ATOM   3326 H HD2    . PHE A 1 193 ? 34.693 45.430 23.038 1.00 52.97 ? 376  PHE A HD2    1 
ATOM   3327 H HE1    . PHE A 1 193 ? 32.353 48.737 20.818 1.00 53.08 ? 376  PHE A HE1    1 
ATOM   3328 H HE2    . PHE A 1 193 ? 35.838 47.059 21.853 1.00 54.04 ? 376  PHE A HE2    1 
ATOM   3329 H HZ     . PHE A 1 193 ? 34.664 48.716 20.746 1.00 54.39 ? 376  PHE A HZ     1 
ATOM   3330 N N      . ARG A 1 194 ? 33.381 44.106 25.937 1.00 43.78 ? 377  ARG A N      1 
ATOM   3331 C CA     . ARG A 1 194 ? 34.504 43.780 26.801 1.00 47.97 ? 377  ARG A CA     1 
ATOM   3332 C C      . ARG A 1 194 ? 35.505 42.930 26.034 1.00 50.29 ? 377  ARG A C      1 
ATOM   3333 O O      . ARG A 1 194 ? 35.121 42.012 25.304 1.00 49.90 ? 377  ARG A O      1 
ATOM   3334 C CB     . ARG A 1 194 ? 34.035 42.970 28.009 1.00 50.09 ? 377  ARG A CB     1 
ATOM   3335 C CG     . ARG A 1 194 ? 33.138 43.728 28.941 1.00 52.36 ? 377  ARG A CG     1 
ATOM   3336 C CD     . ARG A 1 194 ? 33.872 44.056 30.217 1.00 55.38 ? 377  ARG A CD     1 
ATOM   3337 N NE     . ARG A 1 194 ? 33.504 43.140 31.287 1.00 57.67 ? 377  ARG A NE     1 
ATOM   3338 C CZ     . ARG A 1 194 ? 32.431 43.289 32.048 1.00 59.15 ? 377  ARG A CZ     1 
ATOM   3339 N NH1    . ARG A 1 194 ? 31.606 44.313 31.885 1.00 60.14 ? 377  ARG A NH1    1 
ATOM   3340 N NH2    . ARG A 1 194 ? 32.173 42.387 32.991 1.00 59.19 ? 377  ARG A NH2    1 
ATOM   3341 H H      . ARG A 1 194 ? 33.067 43.419 25.525 1.00 52.54 ? 377  ARG A H      1 
ATOM   3342 H HA     . ARG A 1 194 ? 34.932 44.600 27.093 1.00 57.57 ? 377  ARG A HA     1 
ATOM   3343 H HB2    . ARG A 1 194 ? 33.544 42.196 27.692 1.00 60.11 ? 377  ARG A HB2    1 
ATOM   3344 H HB3    . ARG A 1 194 ? 34.813 42.686 28.514 1.00 60.11 ? 377  ARG A HB3    1 
ATOM   3345 H HG2    . ARG A 1 194 ? 32.858 44.557 28.522 1.00 62.83 ? 377  ARG A HG2    1 
ATOM   3346 H HG3    . ARG A 1 194 ? 32.363 43.188 29.160 1.00 62.83 ? 377  ARG A HG3    1 
ATOM   3347 H HD2    . ARG A 1 194 ? 34.828 43.984 30.066 1.00 66.46 ? 377  ARG A HD2    1 
ATOM   3348 H HD3    . ARG A 1 194 ? 33.648 44.958 30.495 1.00 66.46 ? 377  ARG A HD3    1 
ATOM   3349 H HE     . ARG A 1 194 ? 34.013 42.462 31.432 1.00 69.20 ? 377  ARG A HE     1 
ATOM   3350 H HH11   . ARG A 1 194 ? 31.763 44.898 31.274 1.00 72.17 ? 377  ARG A HH11   1 
ATOM   3351 H HH12   . ARG A 1 194 ? 30.914 44.393 32.389 1.00 72.17 ? 377  ARG A HH12   1 
ATOM   3352 H HH21   . ARG A 1 194 ? 32.700 41.717 33.101 1.00 71.02 ? 377  ARG A HH21   1 
ATOM   3353 H HH22   . ARG A 1 194 ? 31.479 42.475 33.491 1.00 71.02 ? 377  ARG A HH22   1 
ATOM   3354 N N      . LYS A 1 195 ? 36.789 43.232 26.213 1.00 53.30 ? 378  LYS A N      1 
ATOM   3355 C CA     . LYS A 1 195 ? 37.881 42.477 25.601 1.00 56.65 ? 378  LYS A CA     1 
ATOM   3356 C C      . LYS A 1 195 ? 38.776 41.980 26.728 1.00 56.03 ? 378  LYS A C      1 
ATOM   3357 O O      . LYS A 1 195 ? 39.642 42.717 27.209 1.00 55.55 ? 378  LYS A O      1 
ATOM   3358 C CB     . LYS A 1 195 ? 38.671 43.344 24.628 1.00 60.92 ? 378  LYS A CB     1 
ATOM   3359 C CG     . LYS A 1 195 ? 37.924 43.715 23.362 1.00 65.50 ? 378  LYS A CG     1 
ATOM   3360 C CD     . LYS A 1 195 ? 38.780 44.604 22.473 1.00 68.82 ? 378  LYS A CD     1 
ATOM   3361 C CE     . LYS A 1 195 ? 38.047 44.995 21.204 1.00 71.11 ? 378  LYS A CE     1 
ATOM   3362 N NZ     . LYS A 1 195 ? 38.926 45.813 20.323 1.00 72.64 ? 378  LYS A NZ     1 
ATOM   3363 H H      . LYS A 1 195 ? 37.061 43.888 26.699 1.00 63.96 ? 378  LYS A H      1 
ATOM   3364 H HA     . LYS A 1 195 ? 37.517 41.719 25.116 1.00 67.98 ? 378  LYS A HA     1 
ATOM   3365 H HB2    . LYS A 1 195 ? 38.914 44.169 25.078 1.00 73.11 ? 378  LYS A HB2    1 
ATOM   3366 H HB3    . LYS A 1 195 ? 39.471 42.862 24.366 1.00 73.11 ? 378  LYS A HB3    1 
ATOM   3367 H HG2    . LYS A 1 195 ? 37.701 42.910 22.870 1.00 78.60 ? 378  LYS A HG2    1 
ATOM   3368 H HG3    . LYS A 1 195 ? 37.115 44.198 23.593 1.00 78.60 ? 378  LYS A HG3    1 
ATOM   3369 H HD2    . LYS A 1 195 ? 39.009 45.415 22.954 1.00 82.58 ? 378  LYS A HD2    1 
ATOM   3370 H HD3    . LYS A 1 195 ? 39.587 44.127 22.224 1.00 82.58 ? 378  LYS A HD3    1 
ATOM   3371 H HE2    . LYS A 1 195 ? 37.785 44.195 20.722 1.00 85.34 ? 378  LYS A HE2    1 
ATOM   3372 H HE3    . LYS A 1 195 ? 37.263 45.518 21.431 1.00 85.34 ? 378  LYS A HE3    1 
ATOM   3373 H HZ1    . LYS A 1 195 ? 38.511 45.984 19.554 1.00 87.17 ? 378  LYS A HZ1    1 
ATOM   3374 H HZ2    . LYS A 1 195 ? 39.125 46.584 20.722 1.00 87.17 ? 378  LYS A HZ2    1 
ATOM   3375 H HZ3    . LYS A 1 195 ? 39.681 45.373 20.152 1.00 87.17 ? 378  LYS A HZ3    1 
ATOM   3376 N N      . VAL A 1 196 ? 38.565 40.736 27.152 1.00 55.68 ? 379  VAL A N      1 
ATOM   3377 C CA     . VAL A 1 196 ? 39.342 40.143 28.235 1.00 54.70 ? 379  VAL A CA     1 
ATOM   3378 C C      . VAL A 1 196 ? 39.284 41.038 29.466 1.00 53.51 ? 379  VAL A C      1 
ATOM   3379 O O      . VAL A 1 196 ? 40.320 41.384 30.046 1.00 54.54 ? 379  VAL A O      1 
ATOM   3380 C CB     . VAL A 1 196 ? 40.797 39.890 27.800 1.00 55.72 ? 379  VAL A CB     1 
ATOM   3381 C CG1    . VAL A 1 196 ? 41.452 38.895 28.726 1.00 55.96 ? 379  VAL A CG1    1 
ATOM   3382 C CG2    . VAL A 1 196 ? 40.844 39.404 26.360 1.00 56.36 ? 379  VAL A CG2    1 
ATOM   3383 H H      . VAL A 1 196 ? 37.969 40.209 26.824 1.00 66.82 ? 379  VAL A H      1 
ATOM   3384 H HA     . VAL A 1 196 ? 38.941 39.292 28.472 1.00 65.64 ? 379  VAL A HA     1 
ATOM   3385 H HB     . VAL A 1 196 ? 41.294 40.721 27.850 1.00 66.87 ? 379  VAL A HB     1 
ATOM   3386 H HG11   . VAL A 1 196 ? 42.360 38.734 28.425 1.00 67.16 ? 379  VAL A HG11   1 
ATOM   3387 H HG12   . VAL A 1 196 ? 41.461 39.259 29.625 1.00 67.16 ? 379  VAL A HG12   1 
ATOM   3388 H HG13   . VAL A 1 196 ? 40.947 38.068 28.710 1.00 67.16 ? 379  VAL A HG13   1 
ATOM   3389 H HG21   . VAL A 1 196 ? 41.760 39.180 26.132 1.00 67.63 ? 379  VAL A HG21   1 
ATOM   3390 H HG22   . VAL A 1 196 ? 40.281 38.619 26.273 1.00 67.63 ? 379  VAL A HG22   1 
ATOM   3391 H HG23   . VAL A 1 196 ? 40.521 40.109 25.778 1.00 67.63 ? 379  VAL A HG23   1 
ATOM   3392 N N      . GLY A 1 197 ? 38.074 41.413 29.875 1.00 51.90 ? 380  GLY A N      1 
ATOM   3393 C CA     . GLY A 1 197 ? 37.870 42.263 31.028 1.00 51.50 ? 380  GLY A CA     1 
ATOM   3394 C C      . GLY A 1 197 ? 38.010 43.743 30.763 1.00 50.71 ? 380  GLY A C      1 
ATOM   3395 O O      . GLY A 1 197 ? 37.656 44.553 31.633 1.00 50.73 ? 380  GLY A O      1 
ATOM   3396 H H      . GLY A 1 197 ? 37.342 41.180 29.487 1.00 62.28 ? 380  GLY A H      1 
ATOM   3397 H HA2    . GLY A 1 197 ? 36.978 42.108 31.374 1.00 61.80 ? 380  GLY A HA2    1 
ATOM   3398 H HA3    . GLY A 1 197 ? 38.519 42.022 31.708 1.00 61.80 ? 380  GLY A HA3    1 
ATOM   3399 N N      . ASN A 1 198 ? 38.510 44.124 29.598 1.00 49.22 ? 381  ASN A N      1 
ATOM   3400 C CA     . ASN A 1 198 ? 38.739 45.519 29.263 1.00 46.79 ? 381  ASN A CA     1 
ATOM   3401 C C      . ASN A 1 198 ? 37.501 46.058 28.560 1.00 42.96 ? 381  ASN A C      1 
ATOM   3402 O O      . ASN A 1 198 ? 37.085 45.534 27.521 1.00 42.62 ? 381  ASN A O      1 
ATOM   3403 C CB     . ASN A 1 198 ? 39.988 45.615 28.392 1.00 47.41 ? 381  ASN A CB     1 
ATOM   3404 C CG     . ASN A 1 198 ? 41.184 44.929 29.030 1.00 49.44 ? 381  ASN A CG     1 
ATOM   3405 O OD1    . ASN A 1 198 ? 41.369 44.995 30.246 1.00 50.42 ? 381  ASN A OD1    1 
ATOM   3406 N ND2    . ASN A 1 198 ? 41.999 44.265 28.216 1.00 49.12 ? 381  ASN A ND2    1 
ATOM   3407 H H      . ASN A 1 198 ? 38.730 43.580 28.969 1.00 59.07 ? 381  ASN A H      1 
ATOM   3408 H HA     . ASN A 1 198 ? 38.878 46.061 30.055 1.00 56.15 ? 381  ASN A HA     1 
ATOM   3409 H HB2    . ASN A 1 198 ? 39.815 45.190 27.538 1.00 56.89 ? 381  ASN A HB2    1 
ATOM   3410 H HB3    . ASN A 1 198 ? 40.212 46.550 28.259 1.00 56.89 ? 381  ASN A HB3    1 
ATOM   3411 H HD21   . ASN A 1 198 ? 42.689 43.861 28.534 1.00 58.95 ? 381  ASN A HD21   1 
ATOM   3412 H HD22   . ASN A 1 198 ? 41.837 44.239 27.372 1.00 58.95 ? 381  ASN A HD22   1 
ATOM   3413 N N      . LYS A 1 199 ? 36.921 47.106 29.137 1.00 41.00 ? 382  LYS A N      1 
ATOM   3414 C CA     . LYS A 1 199 ? 35.687 47.693 28.651 1.00 41.30 ? 382  LYS A CA     1 
ATOM   3415 C C      . LYS A 1 199 ? 35.960 48.716 27.556 1.00 40.30 ? 382  LYS A C      1 
ATOM   3416 O O      . LYS A 1 199 ? 36.944 49.462 27.611 1.00 39.64 ? 382  LYS A O      1 
ATOM   3417 C CB     . LYS A 1 199 ? 34.965 48.383 29.808 1.00 44.31 ? 382  LYS A CB     1 
ATOM   3418 C CG     . LYS A 1 199 ? 34.638 47.490 30.995 1.00 46.68 ? 382  LYS A CG     1 
ATOM   3419 C CD     . LYS A 1 199 ? 34.238 48.332 32.206 1.00 49.14 ? 382  LYS A CD     1 
ATOM   3420 C CE     . LYS A 1 199 ? 33.715 47.474 33.344 1.00 51.15 ? 382  LYS A CE     1 
ATOM   3421 N NZ     . LYS A 1 199 ? 33.299 48.299 34.517 1.00 52.69 ? 382  LYS A NZ     1 
ATOM   3422 H H      . LYS A 1 199 ? 37.236 47.503 29.832 1.00 49.20 ? 382  LYS A H      1 
ATOM   3423 H HA     . LYS A 1 199 ? 35.125 46.996 28.276 1.00 49.56 ? 382  LYS A HA     1 
ATOM   3424 H HB2    . LYS A 1 199 ? 35.527 49.103 30.134 1.00 53.17 ? 382  LYS A HB2    1 
ATOM   3425 H HB3    . LYS A 1 199 ? 34.127 48.741 29.476 1.00 53.17 ? 382  LYS A HB3    1 
ATOM   3426 H HG2    . LYS A 1 199 ? 33.899 46.905 30.767 1.00 56.01 ? 382  LYS A HG2    1 
ATOM   3427 H HG3    . LYS A 1 199 ? 35.419 46.963 31.229 1.00 56.01 ? 382  LYS A HG3    1 
ATOM   3428 H HD2    . LYS A 1 199 ? 35.013 48.821 32.525 1.00 58.97 ? 382  LYS A HD2    1 
ATOM   3429 H HD3    . LYS A 1 199 ? 33.538 48.952 31.947 1.00 58.97 ? 382  LYS A HD3    1 
ATOM   3430 H HE2    . LYS A 1 199 ? 32.944 46.972 33.038 1.00 61.38 ? 382  LYS A HE2    1 
ATOM   3431 H HE3    . LYS A 1 199 ? 34.413 46.866 33.633 1.00 61.38 ? 382  LYS A HE3    1 
ATOM   3432 H HZ1    . LYS A 1 199 ? 32.973 47.774 35.158 1.00 63.23 ? 382  LYS A HZ1    1 
ATOM   3433 H HZ2    . LYS A 1 199 ? 33.999 48.746 34.837 1.00 63.23 ? 382  LYS A HZ2    1 
ATOM   3434 H HZ3    . LYS A 1 199 ? 32.672 48.880 34.272 1.00 63.23 ? 382  LYS A HZ3    1 
ATOM   3435 N N      . SER A 1 200 ? 35.072 48.742 26.561 1.00 39.30 ? 383  SER A N      1 
ATOM   3436 C CA     . SER A 1 200 ? 35.126 49.711 25.475 1.00 39.36 ? 383  SER A CA     1 
ATOM   3437 C C      . SER A 1 200 ? 33.714 49.939 24.962 1.00 36.54 ? 383  SER A C      1 
ATOM   3438 O O      . SER A 1 200 ? 32.773 49.241 25.350 1.00 34.88 ? 383  SER A O      1 
ATOM   3439 C CB     . SER A 1 200 ? 35.997 49.220 24.318 1.00 43.20 ? 383  SER A CB     1 
ATOM   3440 O OG     . SER A 1 200 ? 37.348 49.082 24.719 1.00 46.94 ? 383  SER A OG     1 
ATOM   3441 H H      . SER A 1 200 ? 34.413 48.194 26.493 1.00 47.16 ? 383  SER A H      1 
ATOM   3442 H HA     . SER A 1 200 ? 35.493 50.539 25.823 1.00 47.23 ? 383  SER A HA     1 
ATOM   3443 H HB2    . SER A 1 200 ? 35.667 48.358 24.020 1.00 51.84 ? 383  SER A HB2    1 
ATOM   3444 H HB3    . SER A 1 200 ? 35.948 49.863 23.593 1.00 51.84 ? 383  SER A HB3    1 
ATOM   3445 H HG     . SER A 1 200 ? 37.821 48.857 24.062 1.00 56.32 ? 383  SER A HG     1 
ATOM   3446 N N      . SER A 1 201 ? 33.573 50.915 24.066 1.00 35.77 ? 384  SER A N      1 
ATOM   3447 C CA     . SER A 1 201 ? 32.286 51.188 23.438 1.00 35.30 ? 384  SER A CA     1 
ATOM   3448 C C      . SER A 1 201 ? 32.521 51.923 22.126 1.00 35.83 ? 384  SER A C      1 
ATOM   3449 O O      . SER A 1 201 ? 33.613 52.439 21.872 1.00 38.01 ? 384  SER A O      1 
ATOM   3450 C CB     . SER A 1 201 ? 31.379 52.012 24.356 1.00 35.59 ? 384  SER A CB     1 
ATOM   3451 O OG     . SER A 1 201 ? 31.907 53.313 24.528 1.00 36.77 ? 384  SER A OG     1 
ATOM   3452 H H      . SER A 1 201 ? 34.209 51.433 23.807 1.00 42.93 ? 384  SER A H      1 
ATOM   3453 H HA     . SER A 1 201 ? 31.844 50.347 23.240 1.00 42.36 ? 384  SER A HA     1 
ATOM   3454 H HB2    . SER A 1 201 ? 30.497 52.077 23.957 1.00 42.71 ? 384  SER A HB2    1 
ATOM   3455 H HB3    . SER A 1 201 ? 31.320 51.576 25.220 1.00 42.71 ? 384  SER A HB3    1 
ATOM   3456 H HG     . SER A 1 201 ? 32.682 53.269 24.848 1.00 44.12 ? 384  SER A HG     1 
ATOM   3457 N N      . GLU A 1 202 ? 31.484 51.954 21.293 1.00 35.07 ? 385  GLU A N      1 
ATOM   3458 C CA     . GLU A 1 202 ? 31.543 52.631 20.005 1.00 34.47 ? 385  GLU A CA     1 
ATOM   3459 C C      . GLU A 1 202 ? 30.183 53.243 19.689 1.00 29.31 ? 385  GLU A C      1 
ATOM   3460 O O      . GLU A 1 202 ? 29.158 52.565 19.795 1.00 28.15 ? 385  GLU A O      1 
ATOM   3461 C CB     . GLU A 1 202 ? 31.920 51.650 18.894 1.00 39.39 ? 385  GLU A CB     1 
ATOM   3462 C CG     . GLU A 1 202 ? 30.857 50.590 18.625 1.00 42.75 ? 385  GLU A CG     1 
ATOM   3463 C CD     . GLU A 1 202 ? 29.991 50.912 17.419 1.00 42.98 ? 385  GLU A CD     1 
ATOM   3464 O OE1    . GLU A 1 202 ? 30.557 51.364 16.397 1.00 47.20 ? 385  GLU A OE1    1 
ATOM   3465 O OE2    . GLU A 1 202 ? 28.752 50.715 17.498 1.00 36.95 ? 385  GLU A OE2    1 
ATOM   3466 H H      . GLU A 1 202 ? 30.724 51.585 21.456 1.00 42.09 ? 385  GLU A H      1 
ATOM   3467 H HA     . GLU A 1 202 ? 32.201 53.342 20.052 1.00 41.37 ? 385  GLU A HA     1 
ATOM   3468 H HB2    . GLU A 1 202 ? 32.058 52.146 18.072 1.00 47.27 ? 385  GLU A HB2    1 
ATOM   3469 H HB3    . GLU A 1 202 ? 32.738 51.192 19.146 1.00 47.27 ? 385  GLU A HB3    1 
ATOM   3470 H HG2    . GLU A 1 202 ? 31.294 49.740 18.461 1.00 51.31 ? 385  GLU A HG2    1 
ATOM   3471 H HG3    . GLU A 1 202 ? 30.278 50.521 19.400 1.00 51.31 ? 385  GLU A HG3    1 
ATOM   3472 N N      . PHE A 1 203 ? 30.186 54.519 19.315 1.00 26.93 ? 386  PHE A N      1 
ATOM   3473 C CA     . PHE A 1 203 ? 28.972 55.230 18.919 1.00 25.57 ? 386  PHE A CA     1 
ATOM   3474 C C      . PHE A 1 203 ? 28.645 54.957 17.448 1.00 26.39 ? 386  PHE A C      1 
ATOM   3475 O O      . PHE A 1 203 ? 29.520 55.017 16.579 1.00 30.06 ? 386  PHE A O      1 
ATOM   3476 C CB     . PHE A 1 203 ? 29.145 56.758 19.087 1.00 26.78 ? 386  PHE A CB     1 
ATOM   3477 C CG     . PHE A 1 203 ? 27.933 57.550 18.637 1.00 26.70 ? 386  PHE A CG     1 
ATOM   3478 C CD1    . PHE A 1 203 ? 26.800 57.602 19.435 1.00 26.73 ? 386  PHE A CD1    1 
ATOM   3479 C CD2    . PHE A 1 203 ? 27.925 58.225 17.423 1.00 28.01 ? 386  PHE A CD2    1 
ATOM   3480 C CE1    . PHE A 1 203 ? 25.659 58.288 19.025 1.00 25.26 ? 386  PHE A CE1    1 
ATOM   3481 C CE2    . PHE A 1 203 ? 26.802 58.929 17.010 1.00 27.23 ? 386  PHE A CE2    1 
ATOM   3482 C CZ     . PHE A 1 203 ? 25.662 58.924 17.796 1.00 25.07 ? 386  PHE A CZ     1 
ATOM   3483 H H      . PHE A 1 203 ? 30.893 55.008 19.281 1.00 32.32 ? 386  PHE A H      1 
ATOM   3484 H HA     . PHE A 1 203 ? 28.245 54.923 19.484 1.00 30.69 ? 386  PHE A HA     1 
ATOM   3485 H HB2    . PHE A 1 203 ? 29.299 56.956 20.023 1.00 32.14 ? 386  PHE A HB2    1 
ATOM   3486 H HB3    . PHE A 1 203 ? 29.904 57.048 18.557 1.00 32.14 ? 386  PHE A HB3    1 
ATOM   3487 H HD1    . PHE A 1 203 ? 26.802 57.171 20.259 1.00 32.08 ? 386  PHE A HD1    1 
ATOM   3488 H HD2    . PHE A 1 203 ? 28.680 58.204 16.880 1.00 33.61 ? 386  PHE A HD2    1 
ATOM   3489 H HE1    . PHE A 1 203 ? 24.906 58.319 19.570 1.00 30.31 ? 386  PHE A HE1    1 
ATOM   3490 H HE2    . PHE A 1 203 ? 26.816 59.403 16.210 1.00 32.68 ? 386  PHE A HE2    1 
ATOM   3491 H HZ     . PHE A 1 203 ? 24.892 59.351 17.495 1.00 30.09 ? 386  PHE A HZ     1 
ATOM   3492 N N      . ASP A 1 204 ? 27.371 54.720 17.162 1.00 23.72 ? 387  ASP A N      1 
ATOM   3493 C CA     . ASP A 1 204 ? 26.903 54.447 15.801 1.00 23.45 ? 387  ASP A CA     1 
ATOM   3494 C C      . ASP A 1 204 ? 25.673 55.302 15.544 1.00 23.32 ? 387  ASP A C      1 
ATOM   3495 O O      . ASP A 1 204 ? 24.617 55.077 16.172 1.00 21.87 ? 387  ASP A O      1 
ATOM   3496 C CB     . ASP A 1 204 ? 26.592 52.957 15.686 1.00 23.26 ? 387  ASP A CB     1 
ATOM   3497 C CG     . ASP A 1 204 ? 26.120 52.557 14.305 1.00 25.76 ? 387  ASP A CG     1 
ATOM   3498 O OD1    . ASP A 1 204 ? 25.864 53.440 13.466 1.00 26.07 ? 387  ASP A OD1    1 
ATOM   3499 O OD2    . ASP A 1 204 ? 25.977 51.333 14.081 1.00 26.97 ? 387  ASP A OD2    1 
ATOM   3500 H H      . ASP A 1 204 ? 26.742 54.712 17.748 1.00 28.46 ? 387  ASP A H      1 
ATOM   3501 H HA     . ASP A 1 204 ? 27.568 54.684 15.135 1.00 28.15 ? 387  ASP A HA     1 
ATOM   3502 H HB2    . ASP A 1 204 ? 27.395 52.451 15.885 1.00 27.92 ? 387  ASP A HB2    1 
ATOM   3503 H HB3    . ASP A 1 204 ? 25.892 52.731 16.318 1.00 27.92 ? 387  ASP A HB3    1 
ATOM   3504 N N      . PRO A 1 205 ? 25.756 56.305 14.668 1.00 25.11 ? 388  PRO A N      1 
ATOM   3505 C CA     . PRO A 1 205 ? 24.592 57.170 14.457 1.00 26.79 ? 388  PRO A CA     1 
ATOM   3506 C C      . PRO A 1 205 ? 23.391 56.445 13.888 1.00 29.62 ? 388  PRO A C      1 
ATOM   3507 O O      . PRO A 1 205 ? 22.299 57.017 13.897 1.00 31.69 ? 388  PRO A O      1 
ATOM   3508 C CB     . PRO A 1 205 ? 25.112 58.240 13.483 1.00 27.43 ? 388  PRO A CB     1 
ATOM   3509 C CG     . PRO A 1 205 ? 26.198 57.525 12.741 1.00 27.92 ? 388  PRO A CG     1 
ATOM   3510 C CD     . PRO A 1 205 ? 26.863 56.627 13.748 1.00 26.88 ? 388  PRO A CD     1 
ATOM   3511 H HA     . PRO A 1 205 ? 24.343 57.595 15.292 1.00 32.15 ? 388  PRO A HA     1 
ATOM   3512 H HB2    . PRO A 1 205 ? 24.403 58.526 12.885 1.00 32.92 ? 388  PRO A HB2    1 
ATOM   3513 H HB3    . PRO A 1 205 ? 25.460 59.002 13.973 1.00 32.92 ? 388  PRO A HB3    1 
ATOM   3514 H HG2    . PRO A 1 205 ? 25.813 57.005 12.019 1.00 33.51 ? 388  PRO A HG2    1 
ATOM   3515 H HG3    . PRO A 1 205 ? 26.830 58.170 12.386 1.00 33.51 ? 388  PRO A HG3    1 
ATOM   3516 H HD2    . PRO A 1 205 ? 27.209 55.825 13.325 1.00 32.26 ? 388  PRO A HD2    1 
ATOM   3517 H HD3    . PRO A 1 205 ? 27.578 57.091 14.211 1.00 32.26 ? 388  PRO A HD3    1 
ATOM   3518 N N      . THR A 1 206 ? 23.564 55.239 13.347 1.00 28.75 ? 389  THR A N      1 
ATOM   3519 C CA     . THR A 1 206 ? 22.504 54.492 12.682 1.00 28.94 ? 389  THR A CA     1 
ATOM   3520 C C      . THR A 1 206 ? 21.861 53.417 13.560 1.00 26.19 ? 389  THR A C      1 
ATOM   3521 O O      . THR A 1 206 ? 20.949 52.726 13.089 1.00 26.98 ? 389  THR A O      1 
ATOM   3522 C CB     . THR A 1 206 ? 23.065 53.800 11.429 1.00 31.75 ? 389  THR A CB     1 
ATOM   3523 O OG1    . THR A 1 206 ? 23.783 52.607 11.813 1.00 31.70 ? 389  THR A OG1    1 
ATOM   3524 C CG2    . THR A 1 206 ? 23.985 54.725 10.661 1.00 34.61 ? 389  THR A CG2    1 
ATOM   3525 H H      . THR A 1 206 ? 24.315 54.819 13.355 1.00 34.50 ? 389  THR A H      1 
ATOM   3526 H HA     . THR A 1 206 ? 21.816 55.127 12.427 1.00 34.73 ? 389  THR A HA     1 
ATOM   3527 H HB     . THR A 1 206 ? 22.330 53.559 10.843 1.00 38.10 ? 389  THR A HB     1 
ATOM   3528 H HG1    . THR A 1 206 ? 24.426 52.808 12.315 1.00 38.03 ? 389  THR A HG1    1 
ATOM   3529 H HG21   . THR A 1 206 ? 24.273 54.298 9.839  1.00 41.53 ? 389  THR A HG21   1 
ATOM   3530 H HG22   . THR A 1 206 ? 23.521 55.548 10.442 1.00 41.53 ? 389  THR A HG22   1 
ATOM   3531 H HG23   . THR A 1 206 ? 24.765 54.936 11.197 1.00 41.53 ? 389  THR A HG23   1 
ATOM   3532 N N      . LEU A 1 207 ? 22.324 53.227 14.796 1.00 22.91 ? 390  LEU A N      1 
ATOM   3533 C CA     . LEU A 1 207 ? 21.781 52.197 15.668 1.00 22.44 ? 390  LEU A CA     1 
ATOM   3534 C C      . LEU A 1 207 ? 20.457 52.709 16.216 1.00 20.19 ? 390  LEU A C      1 
ATOM   3535 O O      . LEU A 1 207 ? 20.426 53.568 17.102 1.00 20.84 ? 390  LEU A O      1 
ATOM   3536 C CB     . LEU A 1 207 ? 22.799 51.880 16.753 1.00 22.51 ? 390  LEU A CB     1 
ATOM   3537 C CG     . LEU A 1 207 ? 22.383 50.825 17.776 1.00 22.98 ? 390  LEU A CG     1 
ATOM   3538 C CD1    . LEU A 1 207 ? 21.917 49.498 17.153 1.00 23.86 ? 390  LEU A CD1    1 
ATOM   3539 C CD2    . LEU A 1 207 ? 23.541 50.538 18.754 1.00 23.84 ? 390  LEU A CD2    1 
ATOM   3540 H H      . LEU A 1 207 ? 22.957 53.688 15.151 1.00 27.49 ? 390  LEU A H      1 
ATOM   3541 H HA     . LEU A 1 207 ? 21.599 51.372 15.191 1.00 26.92 ? 390  LEU A HA     1 
ATOM   3542 H HB2    . LEU A 1 207 ? 23.608 51.560 16.324 1.00 27.01 ? 390  LEU A HB2    1 
ATOM   3543 H HB3    . LEU A 1 207 ? 22.984 52.697 17.242 1.00 27.01 ? 390  LEU A HB3    1 
ATOM   3544 H HG     . LEU A 1 207 ? 21.621 51.195 18.249 1.00 27.57 ? 390  LEU A HG     1 
ATOM   3545 H HD11   . LEU A 1 207 ? 21.693 48.877 17.864 1.00 28.63 ? 390  LEU A HD11   1 
ATOM   3546 H HD12   . LEU A 1 207 ? 21.136 49.665 16.601 1.00 28.63 ? 390  LEU A HD12   1 
ATOM   3547 H HD13   . LEU A 1 207 ? 22.634 49.135 16.610 1.00 28.63 ? 390  LEU A HD13   1 
ATOM   3548 H HD21   . LEU A 1 207 ? 23.242 49.897 19.418 1.00 28.61 ? 390  LEU A HD21   1 
ATOM   3549 H HD22   . LEU A 1 207 ? 24.291 50.175 18.258 1.00 28.61 ? 390  LEU A HD22   1 
ATOM   3550 H HD23   . LEU A 1 207 ? 23.801 51.366 19.188 1.00 28.61 ? 390  LEU A HD23   1 
ATOM   3551 N N      . VAL A 1 208 ? 19.365 52.128 15.741 1.00 21.30 ? 391  VAL A N      1 
ATOM   3552 C CA     . VAL A 1 208 ? 18.029 52.624 16.033 1.00 21.84 ? 391  VAL A CA     1 
ATOM   3553 C C      . VAL A 1 208 ? 17.039 51.532 16.422 1.00 21.75 ? 391  VAL A C      1 
ATOM   3554 O O      . VAL A 1 208 ? 16.195 51.738 17.303 1.00 21.34 ? 391  VAL A O      1 
ATOM   3555 C CB     . VAL A 1 208 ? 17.510 53.420 14.819 1.00 25.39 ? 391  VAL A CB     1 
ATOM   3556 C CG1    . VAL A 1 208 ? 16.152 54.002 15.117 1.00 26.45 ? 391  VAL A CG1    1 
ATOM   3557 C CG2    . VAL A 1 208 ? 18.498 54.491 14.425 1.00 29.22 ? 391  VAL A CG2    1 
ATOM   3558 H H      . VAL A 1 208 ? 19.371 51.430 15.238 1.00 25.57 ? 391  VAL A H      1 
ATOM   3559 H HA     . VAL A 1 208 ? 18.097 53.184 16.822 1.00 26.21 ? 391  VAL A HA     1 
ATOM   3560 H HB     . VAL A 1 208 ? 17.414 52.821 14.062 1.00 30.47 ? 391  VAL A HB     1 
ATOM   3561 H HG11   . VAL A 1 208 ? 15.879 54.562 14.373 1.00 31.74 ? 391  VAL A HG11   1 
ATOM   3562 H HG12   . VAL A 1 208 ? 15.518 53.278 15.237 1.00 31.74 ? 391  VAL A HG12   1 
ATOM   3563 H HG13   . VAL A 1 208 ? 16.207 54.532 15.927 1.00 31.74 ? 391  VAL A HG13   1 
ATOM   3564 H HG21   . VAL A 1 208 ? 18.107 55.039 13.727 1.00 35.06 ? 391  VAL A HG21   1 
ATOM   3565 H HG22   . VAL A 1 208 ? 18.699 55.036 15.201 1.00 35.06 ? 391  VAL A HG22   1 
ATOM   3566 H HG23   . VAL A 1 208 ? 19.308 54.068 14.098 1.00 35.06 ? 391  VAL A HG23   1 
ATOM   3567 N N      . HIS A 1 209 ? 17.112 50.362 15.779 1.00 23.87 ? 392  HIS A N      1 
ATOM   3568 C CA     A HIS A 1 209 ? 16.148 49.308 16.066 0.66 23.98 ? 392  HIS A CA     1 
ATOM   3569 C CA     B HIS A 1 209 ? 16.142 49.317 16.082 0.34 24.15 ? 392  HIS A CA     1 
ATOM   3570 C C      . HIS A 1 209 ? 16.796 48.194 16.889 1.00 23.61 ? 392  HIS A C      1 
ATOM   3571 O O      . HIS A 1 209 ? 17.998 47.951 16.765 1.00 24.89 ? 392  HIS A O      1 
ATOM   3572 C CB     A HIS A 1 209 ? 15.612 48.751 14.746 0.66 27.74 ? 392  HIS A CB     1 
ATOM   3573 C CB     B HIS A 1 209 ? 15.454 48.731 14.840 0.34 26.44 ? 392  HIS A CB     1 
ATOM   3574 C CG     A HIS A 1 209 ? 14.953 49.789 13.887 0.66 31.34 ? 392  HIS A CG     1 
ATOM   3575 C CG     B HIS A 1 209 ? 16.388 48.148 13.825 0.34 28.83 ? 392  HIS A CG     1 
ATOM   3576 N ND1    A HIS A 1 209 ? 13.643 50.180 14.065 0.66 32.75 ? 392  HIS A ND1    1 
ATOM   3577 N ND1    B HIS A 1 209 ? 16.811 48.852 12.720 0.34 30.17 ? 392  HIS A ND1    1 
ATOM   3578 C CD2    A HIS A 1 209 ? 15.423 50.525 12.852 0.66 32.11 ? 392  HIS A CD2    1 
ATOM   3579 C CD2    B HIS A 1 209 ? 16.938 46.915 13.719 0.34 30.04 ? 392  HIS A CD2    1 
ATOM   3580 C CE1    A HIS A 1 209 ? 13.334 51.107 13.176 0.66 31.66 ? 392  HIS A CE1    1 
ATOM   3581 C CE1    B HIS A 1 209 ? 17.605 48.089 11.990 0.34 30.55 ? 392  HIS A CE1    1 
ATOM   3582 N NE2    A HIS A 1 209 ? 14.394 51.330 12.423 0.66 32.23 ? 392  HIS A NE2    1 
ATOM   3583 N NE2    B HIS A 1 209 ? 17.699 46.909 12.573 0.34 30.35 ? 392  HIS A NE2    1 
ATOM   3584 H H      A HIS A 1 209 ? 17.700 50.164 15.184 0.66 28.64 ? 392  HIS A H      1 
ATOM   3585 H H      B HIS A 1 209 ? 17.697 50.161 15.182 0.34 28.64 ? 392  HIS A H      1 
ATOM   3586 H HA     A HIS A 1 209 ? 15.404 49.647 16.589 0.66 28.78 ? 392  HIS A HA     1 
ATOM   3587 H HA     B HIS A 1 209 ? 15.433 49.713 16.612 0.34 28.99 ? 392  HIS A HA     1 
ATOM   3588 H HB2    A HIS A 1 209 ? 16.349 48.373 14.242 0.66 33.29 ? 392  HIS A HB2    1 
ATOM   3589 H HB2    B HIS A 1 209 ? 14.854 48.024 15.125 0.34 31.73 ? 392  HIS A HB2    1 
ATOM   3590 H HB3    A HIS A 1 209 ? 14.955 48.064 14.939 0.66 33.29 ? 392  HIS A HB3    1 
ATOM   3591 H HB3    B HIS A 1 209 ? 14.953 49.437 14.404 0.34 31.73 ? 392  HIS A HB3    1 
ATOM   3592 H HD2    A HIS A 1 209 ? 16.282 50.492 12.497 0.66 38.53 ? 392  HIS A HD2    1 
ATOM   3593 H HD2    B HIS A 1 209 ? 16.823 46.205 14.309 0.34 36.05 ? 392  HIS A HD2    1 
ATOM   3594 H HE1    A HIS A 1 209 ? 12.510 51.530 13.095 0.66 38.00 ? 392  HIS A HE1    1 
ATOM   3595 H HE1    B HIS A 1 209 ? 18.027 48.341 11.200 0.34 36.66 ? 392  HIS A HE1    1 
ATOM   3596 H HE2    A HIS A 1 209 ? 14.435 51.888 11.771 0.66 38.67 ? 392  HIS A HE2    1 
ATOM   3597 H HE2    B HIS A 1 209 ? 18.160 46.243 12.283 0.34 36.42 ? 392  HIS A HE2    1 
ATOM   3598 N N      . PRO A 1 210 ? 16.026 47.525 17.754 1.00 23.02 ? 393  PRO A N      1 
ATOM   3599 C CA     . PRO A 1 210 ? 16.576 46.451 18.583 1.00 22.66 ? 393  PRO A CA     1 
ATOM   3600 C C      . PRO A 1 210 ? 17.159 45.304 17.777 1.00 22.61 ? 393  PRO A C      1 
ATOM   3601 O O      . PRO A 1 210 ? 16.844 45.091 16.613 1.00 23.22 ? 393  PRO A O      1 
ATOM   3602 C CB     . PRO A 1 210 ? 15.355 45.952 19.370 1.00 24.71 ? 393  PRO A CB     1 
ATOM   3603 C CG     . PRO A 1 210 ? 14.367 47.052 19.344 1.00 25.86 ? 393  PRO A CG     1 
ATOM   3604 C CD     . PRO A 1 210 ? 14.597 47.776 18.037 1.00 24.44 ? 393  PRO A CD     1 
ATOM   3605 H HA     . PRO A 1 210 ? 17.258 46.818 19.168 1.00 27.19 ? 393  PRO A HA     1 
ATOM   3606 H HB2    . PRO A 1 210 ? 14.995 45.159 18.943 1.00 29.66 ? 393  PRO A HB2    1 
ATOM   3607 H HB3    . PRO A 1 210 ? 15.616 45.749 20.282 1.00 29.66 ? 393  PRO A HB3    1 
ATOM   3608 H HG2    . PRO A 1 210 ? 13.469 46.687 19.382 1.00 31.04 ? 393  PRO A HG2    1 
ATOM   3609 H HG3    . PRO A 1 210 ? 14.516 47.645 20.097 1.00 31.04 ? 393  PRO A HG3    1 
ATOM   3610 H HD2    . PRO A 1 210 ? 14.036 47.408 17.336 1.00 29.33 ? 393  PRO A HD2    1 
ATOM   3611 H HD3    . PRO A 1 210 ? 14.425 48.726 18.135 1.00 29.33 ? 393  PRO A HD3    1 
ATOM   3612 N N      . ARG A 1 211 ? 18.007 44.537 18.441 1.00 21.51 ? 394  ARG A N      1 
ATOM   3613 C CA     . ARG A 1 211 ? 18.505 43.293 17.857 1.00 22.16 ? 394  ARG A CA     1 
ATOM   3614 C C      . ARG A 1 211 ? 17.345 42.317 17.651 1.00 25.19 ? 394  ARG A C      1 
ATOM   3615 O O      . ARG A 1 211 ? 16.392 42.289 18.432 1.00 27.27 ? 394  ARG A O      1 
ATOM   3616 C CB     . ARG A 1 211 ? 19.586 42.700 18.761 1.00 22.62 ? 394  ARG A CB     1 
ATOM   3617 C CG     . ARG A 1 211 ? 20.928 43.363 18.553 1.00 22.78 ? 394  ARG A CG     1 
ATOM   3618 C CD     . ARG A 1 211 ? 21.991 42.914 19.539 1.00 21.68 ? 394  ARG A CD     1 
ATOM   3619 N NE     . ARG A 1 211 ? 21.848 43.554 20.847 1.00 21.21 ? 394  ARG A NE     1 
ATOM   3620 C CZ     . ARG A 1 211 ? 22.656 43.348 21.885 1.00 20.44 ? 394  ARG A CZ     1 
ATOM   3621 N NH1    . ARG A 1 211 ? 23.615 42.433 21.841 1.00 21.66 ? 394  ARG A NH1    1 
ATOM   3622 N NH2    . ARG A 1 211 ? 22.480 44.056 23.005 1.00 18.67 ? 394  ARG A NH2    1 
ATOM   3623 H H      . ARG A 1 211 ? 18.312 44.708 19.227 1.00 25.82 ? 394  ARG A H      1 
ATOM   3624 H HA     . ARG A 1 211 ? 18.908 43.457 16.990 1.00 26.60 ? 394  ARG A HA     1 
ATOM   3625 H HB2    . ARG A 1 211 ? 19.328 42.823 19.688 1.00 27.15 ? 394  ARG A HB2    1 
ATOM   3626 H HB3    . ARG A 1 211 ? 19.681 41.755 18.565 1.00 27.15 ? 394  ARG A HB3    1 
ATOM   3627 H HG2    . ARG A 1 211 ? 21.245 43.152 17.661 1.00 27.34 ? 394  ARG A HG2    1 
ATOM   3628 H HG3    . ARG A 1 211 ? 20.821 44.322 18.649 1.00 27.34 ? 394  ARG A HG3    1 
ATOM   3629 H HD2    . ARG A 1 211 ? 21.922 41.954 19.665 1.00 26.01 ? 394  ARG A HD2    1 
ATOM   3630 H HD3    . ARG A 1 211 ? 22.866 43.140 19.188 1.00 26.01 ? 394  ARG A HD3    1 
ATOM   3631 H HE     . ARG A 1 211 ? 21.195 44.103 20.953 1.00 25.45 ? 394  ARG A HE     1 
ATOM   3632 H HH11   . ARG A 1 211 ? 23.724 41.958 21.132 1.00 26.00 ? 394  ARG A HH11   1 
ATOM   3633 H HH12   . ARG A 1 211 ? 24.127 42.313 22.521 1.00 26.00 ? 394  ARG A HH12   1 
ATOM   3634 H HH21   . ARG A 1 211 ? 21.849 44.638 23.050 1.00 22.41 ? 394  ARG A HH21   1 
ATOM   3635 H HH22   . ARG A 1 211 ? 22.997 43.929 23.680 1.00 22.41 ? 394  ARG A HH22   1 
ATOM   3636 N N      . THR A 1 212 ? 17.390 41.581 16.546 1.00 28.46 ? 395  THR A N      1 
ATOM   3637 C CA     . THR A 1 212 ? 16.270 40.738 16.138 1.00 31.58 ? 395  THR A CA     1 
ATOM   3638 C C      . THR A 1 212 ? 16.509 39.264 16.413 1.00 33.52 ? 395  THR A C      1 
ATOM   3639 O O      . THR A 1 212 ? 15.599 38.464 16.212 1.00 34.85 ? 395  THR A O      1 
ATOM   3640 C CB     . THR A 1 212 ? 15.946 40.916 14.650 1.00 34.71 ? 395  THR A CB     1 
ATOM   3641 O OG1    . THR A 1 212 ? 17.096 40.582 13.864 1.00 36.34 ? 395  THR A OG1    1 
ATOM   3642 C CG2    . THR A 1 212 ? 15.524 42.347 14.388 1.00 36.27 ? 395  THR A CG2    1 
ATOM   3643 H H      . THR A 1 212 ? 18.063 41.551 16.012 1.00 34.15 ? 395  THR A H      1 
ATOM   3644 H HA     . THR A 1 212 ? 15.490 41.025 16.637 1.00 37.90 ? 395  THR A HA     1 
ATOM   3645 H HB     . THR A 1 212 ? 15.218 40.331 14.389 1.00 41.65 ? 395  THR A HB     1 
ATOM   3646 H HG1    . THR A 1 212 ? 16.932 40.701 13.049 1.00 43.61 ? 395  THR A HG1    1 
ATOM   3647 H HG21   . THR A 1 212 ? 15.308 42.463 13.450 1.00 43.52 ? 395  THR A HG21   1 
ATOM   3648 H HG22   . THR A 1 212 ? 14.742 42.564 14.920 1.00 43.52 ? 395  THR A HG22   1 
ATOM   3649 H HG23   . THR A 1 212 ? 16.243 42.953 14.624 1.00 43.52 ? 395  THR A HG23   1 
ATOM   3650 N N      . GLU A 1 213 ? 17.713 38.893 16.811 1.00 34.95 ? 396  GLU A N      1 
ATOM   3651 C CA     A GLU A 1 213 ? 18.006 37.548 17.279 0.63 36.37 ? 396  GLU A CA     1 
ATOM   3652 C CA     B GLU A 1 213 ? 18.018 37.548 17.273 0.37 36.41 ? 396  GLU A CA     1 
ATOM   3653 C C      . GLU A 1 213 ? 18.561 37.657 18.688 1.00 32.97 ? 396  GLU A C      1 
ATOM   3654 O O      . GLU A 1 213 ? 19.267 38.618 19.012 1.00 31.87 ? 396  GLU A O      1 
ATOM   3655 C CB     A GLU A 1 213 ? 19.001 36.864 16.351 0.63 41.70 ? 396  GLU A CB     1 
ATOM   3656 C CB     B GLU A 1 213 ? 19.059 36.861 16.388 0.37 41.80 ? 396  GLU A CB     1 
ATOM   3657 C CG     A GLU A 1 213 ? 18.569 36.984 14.894 0.63 46.91 ? 396  GLU A CG     1 
ATOM   3658 C CG     B GLU A 1 213 ? 19.368 35.436 16.830 0.37 46.94 ? 396  GLU A CG     1 
ATOM   3659 C CD     A GLU A 1 213 ? 19.159 35.918 14.009 0.63 51.20 ? 396  GLU A CD     1 
ATOM   3660 C CD     B GLU A 1 213 ? 19.851 34.551 15.695 0.37 50.90 ? 396  GLU A CD     1 
ATOM   3661 O OE1    A GLU A 1 213 ? 20.295 35.476 14.285 0.63 52.97 ? 396  GLU A OE1    1 
ATOM   3662 O OE1    B GLU A 1 213 ? 20.664 35.022 14.871 0.37 52.33 ? 396  GLU A OE1    1 
ATOM   3663 O OE2    A GLU A 1 213 ? 18.477 35.516 13.041 0.63 52.32 ? 396  GLU A OE2    1 
ATOM   3664 O OE2    B GLU A 1 213 ? 19.405 33.386 15.622 0.37 52.06 ? 396  GLU A OE2    1 
ATOM   3665 H H      A GLU A 1 213 ? 18.396 39.416 16.820 0.63 41.94 ? 396  GLU A H      1 
ATOM   3666 H H      B GLU A 1 213 ? 18.394 39.419 16.823 0.37 41.94 ? 396  GLU A H      1 
ATOM   3667 H HA     A GLU A 1 213 ? 17.207 36.998 17.302 0.63 43.64 ? 396  GLU A HA     1 
ATOM   3668 H HA     B GLU A 1 213 ? 17.216 37.003 17.259 0.37 43.70 ? 396  GLU A HA     1 
ATOM   3669 H HB2    A GLU A 1 213 ? 19.871 37.282 16.448 0.63 50.04 ? 396  GLU A HB2    1 
ATOM   3670 H HB2    B GLU A 1 213 ? 18.725 36.826 15.478 0.37 50.16 ? 396  GLU A HB2    1 
ATOM   3671 H HB3    A GLU A 1 213 ? 19.058 35.923 16.578 0.63 50.04 ? 396  GLU A HB3    1 
ATOM   3672 H HB3    B GLU A 1 213 ? 19.884 37.370 16.419 0.37 50.16 ? 396  GLU A HB3    1 
ATOM   3673 H HG2    A GLU A 1 213 ? 17.603 36.910 14.846 0.63 56.29 ? 396  GLU A HG2    1 
ATOM   3674 H HG2    B GLU A 1 213 ? 20.063 35.460 17.506 0.37 56.33 ? 396  GLU A HG2    1 
ATOM   3675 H HG3    A GLU A 1 213 ? 18.853 37.845 14.552 0.63 56.29 ? 396  GLU A HG3    1 
ATOM   3676 H HG3    B GLU A 1 213 ? 18.562 35.039 17.197 0.37 56.33 ? 396  GLU A HG3    1 
ATOM   3677 N N      . GLY A 1 214 ? 18.215 36.688 19.518 1.00 28.41 ? 397  GLY A N      1 
ATOM   3678 C CA     . GLY A 1 214 ? 18.603 36.653 20.913 1.00 25.44 ? 397  GLY A CA     1 
ATOM   3679 C C      . GLY A 1 214 ? 17.428 36.996 21.820 1.00 23.53 ? 397  GLY A C      1 
ATOM   3680 O O      . GLY A 1 214 ? 16.306 37.227 21.372 1.00 24.03 ? 397  GLY A O      1 
ATOM   3681 H H      . GLY A 1 214 ? 17.735 36.013 19.286 1.00 34.09 ? 397  GLY A H      1 
ATOM   3682 H HA2    . GLY A 1 214 ? 18.922 35.766 21.141 1.00 30.53 ? 397  GLY A HA2    1 
ATOM   3683 H HA3    . GLY A 1 214 ? 19.313 37.294 21.070 1.00 30.53 ? 397  GLY A HA3    1 
ATOM   3684 N N      . SER A 1 215 ? 17.726 37.071 23.112 1.00 20.63 ? 398  SER A N      1 
ATOM   3685 C CA     . SER A 1 215 ? 16.732 37.406 24.125 1.00 18.03 ? 398  SER A CA     1 
ATOM   3686 C C      . SER A 1 215 ? 17.280 38.535 24.978 1.00 16.96 ? 398  SER A C      1 
ATOM   3687 O O      . SER A 1 215 ? 18.444 38.484 25.389 1.00 17.43 ? 398  SER A O      1 
ATOM   3688 C CB     . SER A 1 215 ? 16.420 36.192 25.006 1.00 18.85 ? 398  SER A CB     1 
ATOM   3689 O OG     . SER A 1 215 ? 15.791 35.180 24.262 1.00 19.16 ? 398  SER A OG     1 
ATOM   3690 H H      . SER A 1 215 ? 18.511 36.929 23.433 1.00 24.75 ? 398  SER A H      1 
ATOM   3691 H HA     . SER A 1 215 ? 15.910 37.700 23.701 1.00 21.63 ? 398  SER A HA     1 
ATOM   3692 H HB2    . SER A 1 215 ? 17.250 35.846 25.371 1.00 22.62 ? 398  SER A HB2    1 
ATOM   3693 H HB3    . SER A 1 215 ? 15.830 36.468 25.725 1.00 22.62 ? 398  SER A HB3    1 
ATOM   3694 H HG     . SER A 1 215 ? 16.273 34.960 23.610 1.00 23.00 ? 398  SER A HG     1 
ATOM   3695 N N      . TYR A 1 216 ? 16.448 39.549 25.234 1.00 16.45 ? 399  TYR A N      1 
ATOM   3696 C CA     . TYR A 1 216 ? 16.950 40.772 25.837 1.00 15.85 ? 399  TYR A CA     1 
ATOM   3697 C C      . TYR A 1 216 ? 16.004 41.335 26.888 1.00 15.61 ? 399  TYR A C      1 
ATOM   3698 O O      . TYR A 1 216 ? 14.780 41.202 26.811 1.00 16.40 ? 399  TYR A O      1 
ATOM   3699 C CB     . TYR A 1 216 ? 17.202 41.881 24.766 1.00 16.07 ? 399  TYR A CB     1 
ATOM   3700 C CG     . TYR A 1 216 ? 18.089 41.419 23.641 1.00 17.44 ? 399  TYR A CG     1 
ATOM   3701 C CD1    . TYR A 1 216 ? 19.465 41.466 23.791 1.00 17.37 ? 399  TYR A CD1    1 
ATOM   3702 C CD2    . TYR A 1 216 ? 17.569 40.855 22.467 1.00 17.44 ? 399  TYR A CD2    1 
ATOM   3703 C CE1    . TYR A 1 216 ? 20.302 41.009 22.826 1.00 19.12 ? 399  TYR A CE1    1 
ATOM   3704 C CE2    . TYR A 1 216 ? 18.413 40.400 21.471 1.00 19.27 ? 399  TYR A CE2    1 
ATOM   3705 C CZ     . TYR A 1 216 ? 19.790 40.467 21.674 1.00 20.52 ? 399  TYR A CZ     1 
ATOM   3706 O OH     . TYR A 1 216 ? 20.664 40.010 20.734 1.00 23.38 ? 399  TYR A OH     1 
ATOM   3707 H H      . TYR A 1 216 ? 15.604 39.546 25.067 1.00 19.74 ? 399  TYR A H      1 
ATOM   3708 H HA     . TYR A 1 216 ? 17.776 40.541 26.290 1.00 19.02 ? 399  TYR A HA     1 
ATOM   3709 H HB2    . TYR A 1 216 ? 16.351 42.151 24.386 1.00 19.29 ? 399  TYR A HB2    1 
ATOM   3710 H HB3    . TYR A 1 216 ? 17.630 42.640 25.193 1.00 19.29 ? 399  TYR A HB3    1 
ATOM   3711 H HD1    . TYR A 1 216 ? 19.825 41.820 24.572 1.00 20.85 ? 399  TYR A HD1    1 
ATOM   3712 H HD2    . TYR A 1 216 ? 16.648 40.787 22.357 1.00 20.93 ? 399  TYR A HD2    1 
ATOM   3713 H HE1    . TYR A 1 216 ? 21.223 41.063 22.945 1.00 22.95 ? 399  TYR A HE1    1 
ATOM   3714 H HE2    . TYR A 1 216 ? 18.068 40.054 20.680 1.00 23.12 ? 399  TYR A HE2    1 
ATOM   3715 H HH     . TYR A 1 216 ? 20.243 39.666 20.093 1.00 28.05 ? 399  TYR A HH     1 
ATOM   3716 N N      . ILE A 1 217 ? 16.613 42.087 27.812 1.00 15.32 ? 400  ILE A N      1 
ATOM   3717 C CA     . ILE A 1 217 ? 15.956 43.022 28.720 1.00 15.93 ? 400  ILE A CA     1 
ATOM   3718 C C      . ILE A 1 217 ? 16.147 44.420 28.140 1.00 14.32 ? 400  ILE A C      1 
ATOM   3719 O O      . ILE A 1 217 ? 17.231 44.742 27.662 1.00 15.88 ? 400  ILE A O      1 
ATOM   3720 C CB     . ILE A 1 217 ? 16.628 42.998 30.118 1.00 19.59 ? 400  ILE A CB     1 
ATOM   3721 C CG1    . ILE A 1 217 ? 16.788 41.582 30.662 1.00 24.19 ? 400  ILE A CG1    1 
ATOM   3722 C CG2    . ILE A 1 217 ? 15.895 43.957 31.078 1.00 20.53 ? 400  ILE A CG2    1 
ATOM   3723 C CD1    . ILE A 1 217 ? 15.594 41.056 31.014 1.00 21.68 ? 400  ILE A CD1    1 
ATOM   3724 H H      . ILE A 1 217 ? 17.464 42.068 27.936 1.00 18.39 ? 400  ILE A H      1 
ATOM   3725 H HA     . ILE A 1 217 ? 15.017 42.790 28.797 1.00 19.12 ? 400  ILE A HA     1 
ATOM   3726 H HB     . ILE A 1 217 ? 17.536 43.326 30.025 1.00 23.50 ? 400  ILE A HB     1 
ATOM   3727 H HG12   . ILE A 1 217 ? 17.183 41.017 29.980 1.00 29.02 ? 400  ILE A HG12   1 
ATOM   3728 H HG13   . ILE A 1 217 ? 17.357 41.601 31.447 1.00 29.02 ? 400  ILE A HG13   1 
ATOM   3729 H HG21   . ILE A 1 217 ? 16.106 43.711 31.992 1.00 24.63 ? 400  ILE A HG21   1 
ATOM   3730 H HG22   . ILE A 1 217 ? 16.190 44.865 30.904 1.00 24.63 ? 400  ILE A HG22   1 
ATOM   3731 H HG23   . ILE A 1 217 ? 14.940 43.885 30.928 1.00 24.63 ? 400  ILE A HG23   1 
ATOM   3732 H HD11   . ILE A 1 217 ? 15.728 40.145 31.319 1.00 26.01 ? 400  ILE A HD11   1 
ATOM   3733 H HD12   . ILE A 1 217 ? 15.211 41.591 31.727 1.00 26.01 ? 400  ILE A HD12   1 
ATOM   3734 H HD13   . ILE A 1 217 ? 15.006 41.063 30.242 1.00 26.01 ? 400  ILE A HD13   1 
ATOM   3735 N N      . TYR A 1 218 ? 15.095 45.247 28.170 1.00 13.58 ? 401  TYR A N      1 
ATOM   3736 C CA     . TYR A 1 218 ? 15.165 46.675 27.801 1.00 14.12 ? 401  TYR A CA     1 
ATOM   3737 C C      . TYR A 1 218 ? 14.904 47.485 29.065 1.00 13.89 ? 401  TYR A C      1 
ATOM   3738 O O      . TYR A 1 218 ? 13.779 47.499 29.563 1.00 15.99 ? 401  TYR A O      1 
ATOM   3739 C CB     . TYR A 1 218 ? 14.118 47.025 26.719 1.00 15.39 ? 401  TYR A CB     1 
ATOM   3740 C CG     . TYR A 1 218 ? 14.437 46.276 25.443 1.00 15.02 ? 401  TYR A CG     1 
ATOM   3741 C CD1    . TYR A 1 218 ? 14.013 44.960 25.267 1.00 15.44 ? 401  TYR A CD1    1 
ATOM   3742 C CD2    . TYR A 1 218 ? 15.272 46.824 24.480 1.00 15.58 ? 401  TYR A CD2    1 
ATOM   3743 C CE1    . TYR A 1 218 ? 14.404 44.222 24.182 1.00 16.75 ? 401  TYR A CE1    1 
ATOM   3744 C CE2    . TYR A 1 218 ? 15.656 46.097 23.374 1.00 16.12 ? 401  TYR A CE2    1 
ATOM   3745 C CZ     . TYR A 1 218 ? 15.233 44.772 23.255 1.00 16.76 ? 401  TYR A CZ     1 
ATOM   3746 O OH     . TYR A 1 218 ? 15.627 44.000 22.228 1.00 17.21 ? 401  TYR A OH     1 
ATOM   3747 H H      . TYR A 1 218 ? 14.307 45.000 28.407 1.00 16.30 ? 401  TYR A H      1 
ATOM   3748 H HA     . TYR A 1 218 ? 16.047 46.878 27.453 1.00 16.94 ? 401  TYR A HA     1 
ATOM   3749 H HB2    . TYR A 1 218 ? 13.234 46.766 27.023 1.00 18.47 ? 401  TYR A HB2    1 
ATOM   3750 H HB3    . TYR A 1 218 ? 14.141 47.978 26.538 1.00 18.47 ? 401  TYR A HB3    1 
ATOM   3751 H HD1    . TYR A 1 218 ? 13.453 44.574 25.901 1.00 18.53 ? 401  TYR A HD1    1 
ATOM   3752 H HD2    . TYR A 1 218 ? 15.578 47.696 24.583 1.00 18.69 ? 401  TYR A HD2    1 
ATOM   3753 H HE1    . TYR A 1 218 ? 14.103 43.348 24.079 1.00 20.10 ? 401  TYR A HE1    1 
ATOM   3754 H HE2    . TYR A 1 218 ? 16.188 46.484 22.717 1.00 19.34 ? 401  TYR A HE2    1 
ATOM   3755 H HH     . TYR A 1 218 ? 16.222 44.395 21.784 1.00 20.66 ? 401  TYR A HH     1 
ATOM   3756 N N      . GLU A 1 219 ? 15.918 48.161 29.588 1.00 13.73 ? 402  GLU A N      1 
ATOM   3757 C CA     . GLU A 1 219 ? 15.734 48.966 30.782 1.00 14.64 ? 402  GLU A CA     1 
ATOM   3758 C C      . GLU A 1 219 ? 15.766 50.435 30.411 1.00 14.74 ? 402  GLU A C      1 
ATOM   3759 O O      . GLU A 1 219 ? 16.542 50.838 29.556 1.00 16.31 ? 402  GLU A O      1 
ATOM   3760 C CB     . GLU A 1 219 ? 16.850 48.766 31.820 1.00 15.67 ? 402  GLU A CB     1 
ATOM   3761 C CG     . GLU A 1 219 ? 16.666 47.556 32.646 1.00 16.66 ? 402  GLU A CG     1 
ATOM   3762 C CD     . GLU A 1 219 ? 17.704 47.456 33.746 1.00 17.27 ? 402  GLU A CD     1 
ATOM   3763 O OE1    . GLU A 1 219 ? 18.797 48.136 33.715 1.00 17.67 ? 402  GLU A OE1    1 
ATOM   3764 O OE2    . GLU A 1 219 ? 17.393 46.666 34.653 1.00 17.89 ? 402  GLU A OE2    1 
ATOM   3765 H H      . GLU A 1 219 ? 16.716 48.168 29.269 1.00 16.48 ? 402  GLU A H      1 
ATOM   3766 H HA     . GLU A 1 219 ? 14.884 48.710 31.172 1.00 17.57 ? 402  GLU A HA     1 
ATOM   3767 H HB2    . GLU A 1 219 ? 17.698 48.685 31.357 1.00 18.80 ? 402  GLU A HB2    1 
ATOM   3768 H HB3    . GLU A 1 219 ? 16.868 49.533 32.413 1.00 18.80 ? 402  GLU A HB3    1 
ATOM   3769 H HG2    . GLU A 1 219 ? 15.788 47.583 33.060 1.00 19.99 ? 402  GLU A HG2    1 
ATOM   3770 H HG3    . GLU A 1 219 ? 16.743 46.770 32.083 1.00 19.99 ? 402  GLU A HG3    1 
ATOM   3771 N N      . GLN A 1 220 ? 14.928 51.225 31.060 1.00 14.54 ? 403  GLN A N      1 
ATOM   3772 C CA     A GLN A 1 220 ? 15.024 52.667 30.902 0.55 15.81 ? 403  GLN A CA     1 
ATOM   3773 C CA     B GLN A 1 220 ? 15.018 52.674 30.919 0.45 15.42 ? 403  GLN A CA     1 
ATOM   3774 C C      . GLN A 1 220 ? 16.432 53.118 31.258 1.00 15.71 ? 403  GLN A C      1 
ATOM   3775 O O      . GLN A 1 220 ? 16.995 52.696 32.287 1.00 15.74 ? 403  GLN A O      1 
ATOM   3776 C CB     A GLN A 1 220 ? 14.015 53.342 31.809 0.55 18.62 ? 403  GLN A CB     1 
ATOM   3777 C CB     B GLN A 1 220 ? 14.033 53.358 31.863 0.45 17.19 ? 403  GLN A CB     1 
ATOM   3778 C CG     A GLN A 1 220 ? 13.804 54.799 31.429 0.55 21.00 ? 403  GLN A CG     1 
ATOM   3779 C CG     B GLN A 1 220 ? 14.221 54.898 31.871 0.45 18.93 ? 403  GLN A CG     1 
ATOM   3780 C CD     A GLN A 1 220 ? 12.918 54.942 30.205 0.55 23.88 ? 403  GLN A CD     1 
ATOM   3781 C CD     B GLN A 1 220 ? 13.289 55.644 32.815 0.45 21.84 ? 403  GLN A CD     1 
ATOM   3782 O OE1    A GLN A 1 220 ? 11.720 54.642 30.251 0.55 24.28 ? 403  GLN A OE1    1 
ATOM   3783 O OE1    B GLN A 1 220 ? 12.360 55.069 33.373 0.45 23.71 ? 403  GLN A OE1    1 
ATOM   3784 N NE2    A GLN A 1 220 ? 13.503 55.392 29.099 0.55 24.33 ? 403  GLN A NE2    1 
ATOM   3785 N NE2    B GLN A 1 220 ? 13.533 56.935 32.988 0.45 23.65 ? 403  GLN A NE2    1 
ATOM   3786 H H      A GLN A 1 220 ? 14.305 50.958 31.589 0.55 17.45 ? 403  GLN A H      1 
ATOM   3787 H H      B GLN A 1 220 ? 14.303 50.954 31.584 0.45 17.45 ? 403  GLN A H      1 
ATOM   3788 H HA     A GLN A 1 220 ? 14.832 52.921 29.985 0.55 18.97 ? 403  GLN A HA     1 
ATOM   3789 H HA     B GLN A 1 220 ? 14.796 52.932 30.010 0.45 18.51 ? 403  GLN A HA     1 
ATOM   3790 H HB2    A GLN A 1 220 ? 13.164 52.882 31.738 0.55 22.35 ? 403  GLN A HB2    1 
ATOM   3791 H HB2    B GLN A 1 220 ? 13.127 53.163 31.577 0.45 20.63 ? 403  GLN A HB2    1 
ATOM   3792 H HB3    A GLN A 1 220 ? 14.336 53.309 32.724 0.55 22.35 ? 403  GLN A HB3    1 
ATOM   3793 H HB3    B GLN A 1 220 ? 14.174 53.029 32.765 0.45 20.63 ? 403  GLN A HB3    1 
ATOM   3794 H HG2    A GLN A 1 220 ? 13.378 55.263 32.167 0.55 25.20 ? 403  GLN A HG2    1 
ATOM   3795 H HG2    B GLN A 1 220 ? 15.131 55.097 32.141 0.45 22.71 ? 403  GLN A HG2    1 
ATOM   3796 H HG3    A GLN A 1 220 ? 14.662 55.206 31.232 0.55 25.20 ? 403  GLN A HG3    1 
ATOM   3797 H HG3    B GLN A 1 220 ? 14.059 55.233 30.976 0.45 22.71 ? 403  GLN A HG3    1 
ATOM   3798 H HE21   A GLN A 1 220 ? 14.341 55.586 29.104 0.55 29.20 ? 403  GLN A HE21   1 
ATOM   3799 H HE21   B GLN A 1 220 ? 14.190 57.308 32.576 0.45 28.38 ? 403  GLN A HE21   1 
ATOM   3800 H HE22   A GLN A 1 220 ? 13.043 55.491 28.379 0.55 29.20 ? 403  GLN A HE22   1 
ATOM   3801 H HE22   B GLN A 1 220 ? 13.035 57.401 33.512 0.45 28.38 ? 403  GLN A HE22   1 
ATOM   3802 N N      . PHE A 1 221 ? 17.000 53.953 30.404 1.00 15.85 ? 404  PHE A N      1 
ATOM   3803 C CA     . PHE A 1 221 ? 18.306 54.534 30.644 1.00 17.81 ? 404  PHE A CA     1 
ATOM   3804 C C      . PHE A 1 221 ? 18.140 55.538 31.769 1.00 17.87 ? 404  PHE A C      1 
ATOM   3805 O O      . PHE A 1 221 ? 17.376 56.508 31.628 1.00 20.98 ? 404  PHE A O      1 
ATOM   3806 C CB     . PHE A 1 221 ? 18.742 55.226 29.355 1.00 20.57 ? 404  PHE A CB     1 
ATOM   3807 C CG     . PHE A 1 221 ? 20.027 55.965 29.446 1.00 24.23 ? 404  PHE A CG     1 
ATOM   3808 C CD1    . PHE A 1 221 ? 20.077 57.246 29.995 1.00 25.84 ? 404  PHE A CD1    1 
ATOM   3809 C CD2    . PHE A 1 221 ? 21.163 55.435 28.897 1.00 25.87 ? 404  PHE A CD2    1 
ATOM   3810 C CE1    . PHE A 1 221 ? 21.252 57.954 30.039 1.00 27.15 ? 404  PHE A CE1    1 
ATOM   3811 C CE2    . PHE A 1 221 ? 22.365 56.156 28.949 1.00 28.72 ? 404  PHE A CE2    1 
ATOM   3812 C CZ     . PHE A 1 221 ? 22.398 57.401 29.520 1.00 29.06 ? 404  PHE A CZ     1 
ATOM   3813 H H      . PHE A 1 221 ? 16.642 54.203 29.663 1.00 19.03 ? 404  PHE A H      1 
ATOM   3814 H HA     . PHE A 1 221 ? 18.976 53.878 30.892 1.00 21.37 ? 404  PHE A HA     1 
ATOM   3815 H HB2    . PHE A 1 221 ? 18.842 54.554 28.663 1.00 24.68 ? 404  PHE A HB2    1 
ATOM   3816 H HB3    . PHE A 1 221 ? 18.057 55.864 29.101 1.00 24.68 ? 404  PHE A HB3    1 
ATOM   3817 H HD1    . PHE A 1 221 ? 19.301 57.627 30.337 1.00 31.01 ? 404  PHE A HD1    1 
ATOM   3818 H HD2    . PHE A 1 221 ? 21.138 54.598 28.492 1.00 31.04 ? 404  PHE A HD2    1 
ATOM   3819 H HE1    . PHE A 1 221 ? 21.272 58.803 30.417 1.00 32.59 ? 404  PHE A HE1    1 
ATOM   3820 H HE2    . PHE A 1 221 ? 23.142 55.788 28.594 1.00 34.47 ? 404  PHE A HE2    1 
ATOM   3821 H HZ     . PHE A 1 221 ? 23.199 57.872 29.557 1.00 34.87 ? 404  PHE A HZ     1 
ATOM   3822 N N      . MET A 1 222 ? 18.818 55.325 32.873 1.00 17.30 ? 405  MET A N      1 
ATOM   3823 C CA     . MET A 1 222 ? 18.724 56.221 34.018 1.00 18.76 ? 405  MET A CA     1 
ATOM   3824 C C      . MET A 1 222 ? 19.816 57.277 33.928 1.00 19.24 ? 405  MET A C      1 
ATOM   3825 O O      . MET A 1 222 ? 20.962 56.989 33.563 1.00 20.58 ? 405  MET A O      1 
ATOM   3826 C CB     . MET A 1 222 ? 18.832 55.417 35.323 1.00 19.56 ? 405  MET A CB     1 
ATOM   3827 C CG     . MET A 1 222 ? 17.843 54.227 35.389 1.00 19.81 ? 405  MET A CG     1 
ATOM   3828 S SD     . MET A 1 222 ? 16.099 54.542 34.994 1.00 22.56 ? 405  MET A SD     1 
ATOM   3829 C CE     . MET A 1 222 ? 15.800 55.615 36.389 1.00 24.77 ? 405  MET A CE     1 
ATOM   3830 H H      . MET A 1 222 ? 19.351 54.660 32.992 1.00 20.76 ? 405  MET A H      1 
ATOM   3831 H HA     . MET A 1 222 ? 17.863 56.669 34.028 1.00 22.51 ? 405  MET A HA     1 
ATOM   3832 H HB2    . MET A 1 222 ? 19.732 55.062 35.400 1.00 23.47 ? 405  MET A HB2    1 
ATOM   3833 H HB3    . MET A 1 222 ? 18.643 56.005 36.071 1.00 23.47 ? 405  MET A HB3    1 
ATOM   3834 H HG2    . MET A 1 222 ? 18.150 53.552 34.764 1.00 23.78 ? 405  MET A HG2    1 
ATOM   3835 H HG3    . MET A 1 222 ? 17.863 53.877 36.293 1.00 23.78 ? 405  MET A HG3    1 
ATOM   3836 H HE1    . MET A 1 222 ? 14.873 55.899 36.376 1.00 29.72 ? 405  MET A HE1    1 
ATOM   3837 H HE2    . MET A 1 222 ? 15.986 55.129 37.207 1.00 29.72 ? 405  MET A HE2    1 
ATOM   3838 H HE3    . MET A 1 222 ? 16.383 56.388 36.323 1.00 29.72 ? 405  MET A HE3    1 
ATOM   3839 N N      . ASP A 1 223 ? 19.428 58.516 34.202 1.00 20.03 ? 406  ASP A N      1 
ATOM   3840 C CA     . ASP A 1 223 ? 20.355 59.648 34.223 1.00 21.29 ? 406  ASP A CA     1 
ATOM   3841 C C      . ASP A 1 223 ? 20.997 59.713 35.605 1.00 20.03 ? 406  ASP A C      1 
ATOM   3842 O O      . ASP A 1 223 ? 20.422 60.269 36.543 1.00 20.90 ? 406  ASP A O      1 
ATOM   3843 C CB     . ASP A 1 223 ? 19.616 60.956 33.925 1.00 25.89 ? 406  ASP A CB     1 
ATOM   3844 C CG     . ASP A 1 223 ? 19.167 61.085 32.469 1.00 31.97 ? 406  ASP A CG     1 
ATOM   3845 O OD1    . ASP A 1 223 ? 19.888 60.613 31.560 1.00 35.65 ? 406  ASP A OD1    1 
ATOM   3846 O OD2    . ASP A 1 223 ? 18.094 61.698 32.233 1.00 35.72 ? 406  ASP A OD2    1 
ATOM   3847 H H      . ASP A 1 223 ? 18.616 58.734 34.384 1.00 24.03 ? 406  ASP A H      1 
ATOM   3848 H HA     . ASP A 1 223 ? 21.043 59.506 33.554 1.00 25.55 ? 406  ASP A HA     1 
ATOM   3849 H HB2    . ASP A 1 223 ? 18.825 61.002 34.485 1.00 31.06 ? 406  ASP A HB2    1 
ATOM   3850 H HB3    . ASP A 1 223 ? 20.205 61.700 34.121 1.00 31.06 ? 406  ASP A HB3    1 
ATOM   3851 N N      . THR A 1 224 ? 22.204 59.169 35.730 1.00 18.29 ? 407  THR A N      1 
ATOM   3852 C CA     . THR A 1 224 ? 22.758 58.931 37.058 1.00 17.86 ? 407  THR A CA     1 
ATOM   3853 C C      . THR A 1 224 ? 23.562 60.122 37.548 1.00 18.60 ? 407  THR A C      1 
ATOM   3854 O O      . THR A 1 224 ? 24.078 60.946 36.768 1.00 19.61 ? 407  THR A O      1 
ATOM   3855 C CB     . THR A 1 224 ? 23.601 57.658 37.136 1.00 18.43 ? 407  THR A CB     1 
ATOM   3856 O OG1    . THR A 1 224 ? 24.831 57.867 36.439 1.00 18.81 ? 407  THR A OG1    1 
ATOM   3857 C CG2    . THR A 1 224 ? 22.855 56.474 36.563 1.00 20.68 ? 407  THR A CG2    1 
ATOM   3858 H H      . THR A 1 224 ? 22.710 58.936 35.076 1.00 21.95 ? 407  THR A H      1 
ATOM   3859 H HA     . THR A 1 224 ? 22.009 58.802 37.660 1.00 21.43 ? 407  THR A HA     1 
ATOM   3860 H HB     . THR A 1 224 ? 23.796 57.448 38.063 1.00 22.11 ? 407  THR A HB     1 
ATOM   3861 H HG1    . THR A 1 224 ? 25.323 57.191 36.517 1.00 22.57 ? 407  THR A HG1    1 
ATOM   3862 H HG21   . THR A 1 224 ? 23.390 55.670 36.652 1.00 24.82 ? 407  THR A HG21   1 
ATOM   3863 H HG22   . THR A 1 224 ? 22.018 56.349 37.038 1.00 24.82 ? 407  THR A HG22   1 
ATOM   3864 H HG23   . THR A 1 224 ? 22.665 56.624 35.624 1.00 24.82 ? 407  THR A HG23   1 
ATOM   3865 N N      . ASP A 1 225 ? 23.613 60.251 38.858 1.00 18.46 ? 408  ASP A N      1 
ATOM   3866 C CA     . ASP A 1 225 ? 24.357 61.358 39.438 1.00 19.21 ? 408  ASP A CA     1 
ATOM   3867 C C      . ASP A 1 225 ? 25.819 61.275 39.004 1.00 20.01 ? 408  ASP A C      1 
ATOM   3868 O O      . ASP A 1 225 ? 26.462 60.221 39.124 1.00 19.99 ? 408  ASP A O      1 
ATOM   3869 C CB     . ASP A 1 225 ? 24.310 61.275 40.954 1.00 19.35 ? 408  ASP A CB     1 
ATOM   3870 C CG     . ASP A 1 225 ? 22.952 61.506 41.549 1.00 21.69 ? 408  ASP A CG     1 
ATOM   3871 O OD1    . ASP A 1 225 ? 21.949 61.768 40.844 1.00 23.14 ? 408  ASP A OD1    1 
ATOM   3872 O OD2    . ASP A 1 225 ? 22.911 61.423 42.798 1.00 22.88 ? 408  ASP A OD2    1 
ATOM   3873 H H      . ASP A 1 225 ? 23.236 59.725 39.424 1.00 22.15 ? 408  ASP A H      1 
ATOM   3874 H HA     . ASP A 1 225 ? 23.965 62.196 39.145 1.00 23.06 ? 408  ASP A HA     1 
ATOM   3875 H HB2    . ASP A 1 225 ? 24.601 60.390 41.224 1.00 23.22 ? 408  ASP A HB2    1 
ATOM   3876 H HB3    . ASP A 1 225 ? 24.908 61.946 41.319 1.00 23.22 ? 408  ASP A HB3    1 
ATOM   3877 N N      . ASN A 1 226 ? 26.352 62.385 38.526 1.00 20.31 ? 409  ASN A N      1 
ATOM   3878 C CA     . ASN A 1 226 ? 27.734 62.503 38.062 1.00 21.11 ? 409  ASN A CA     1 
ATOM   3879 C C      . ASN A 1 226 ? 28.101 61.512 36.960 1.00 19.70 ? 409  ASN A C      1 
ATOM   3880 O O      . ASN A 1 226 ? 29.300 61.300 36.691 1.00 20.43 ? 409  ASN A O      1 
ATOM   3881 C CB     . ASN A 1 226 ? 28.754 62.383 39.191 1.00 22.41 ? 409  ASN A CB     1 
ATOM   3882 C CG     . ASN A 1 226 ? 28.305 63.083 40.426 1.00 23.65 ? 409  ASN A CG     1 
ATOM   3883 O OD1    . ASN A 1 226 ? 28.113 64.296 40.410 1.00 25.40 ? 409  ASN A OD1    1 
ATOM   3884 N ND2    . ASN A 1 226 ? 28.128 62.333 41.499 1.00 24.24 ? 409  ASN A ND2    1 
ATOM   3885 H H      . ASN A 1 226 ? 25.916 63.123 38.455 1.00 24.37 ? 409  ASN A H      1 
ATOM   3886 H HA     . ASN A 1 226 ? 27.800 63.396 37.689 1.00 25.33 ? 409  ASN A HA     1 
ATOM   3887 H HB2    . ASN A 1 226 ? 28.884 61.446 39.404 1.00 26.90 ? 409  ASN A HB2    1 
ATOM   3888 H HB3    . ASN A 1 226 ? 29.593 62.778 38.906 1.00 26.90 ? 409  ASN A HB3    1 
ATOM   3889 H HD21   . ASN A 1 226 ? 27.869 62.691 42.237 1.00 29.08 ? 409  ASN A HD21   1 
ATOM   3890 H HD22   . ASN A 1 226 ? 28.272 61.486 41.460 1.00 29.08 ? 409  ASN A HD22   1 
ATOM   3891 N N      . PHE A 1 227 ? 27.102 60.949 36.270 1.00 19.16 ? 410  PHE A N      1 
ATOM   3892 C CA     . PHE A 1 227 ? 27.333 59.931 35.238 1.00 20.44 ? 410  PHE A CA     1 
ATOM   3893 C C      . PHE A 1 227 ? 28.119 58.746 35.812 1.00 18.07 ? 410  PHE A C      1 
ATOM   3894 O O      . PHE A 1 227 ? 28.938 58.141 35.128 1.00 19.79 ? 410  PHE A O      1 
ATOM   3895 C CB     . PHE A 1 227 ? 28.067 60.496 34.021 1.00 25.36 ? 410  PHE A CB     1 
ATOM   3896 C CG     . PHE A 1 227 ? 27.384 61.660 33.366 1.00 30.06 ? 410  PHE A CG     1 
ATOM   3897 C CD1    . PHE A 1 227 ? 26.010 61.693 33.197 1.00 31.45 ? 410  PHE A CD1    1 
ATOM   3898 C CD2    . PHE A 1 227 ? 28.134 62.717 32.903 1.00 33.77 ? 410  PHE A CD2    1 
ATOM   3899 C CE1    . PHE A 1 227 ? 25.397 62.767 32.570 1.00 34.14 ? 410  PHE A CE1    1 
ATOM   3900 C CE2    . PHE A 1 227 ? 27.525 63.807 32.290 1.00 36.12 ? 410  PHE A CE2    1 
ATOM   3901 C CZ     . PHE A 1 227 ? 26.153 63.815 32.124 1.00 36.01 ? 410  PHE A CZ     1 
ATOM   3902 H H      . PHE A 1 227 ? 26.271 61.143 36.382 1.00 23.00 ? 410  PHE A H      1 
ATOM   3903 H HA     . PHE A 1 227 ? 26.465 59.618 34.940 1.00 24.52 ? 410  PHE A HA     1 
ATOM   3904 H HB2    . PHE A 1 227 ? 28.947 60.792 34.301 1.00 30.44 ? 410  PHE A HB2    1 
ATOM   3905 H HB3    . PHE A 1 227 ? 28.149 59.793 33.357 1.00 30.44 ? 410  PHE A HB3    1 
ATOM   3906 H HD1    . PHE A 1 227 ? 25.492 60.986 33.507 1.00 37.74 ? 410  PHE A HD1    1 
ATOM   3907 H HD2    . PHE A 1 227 ? 29.058 62.702 33.000 1.00 40.52 ? 410  PHE A HD2    1 
ATOM   3908 H HE1    . PHE A 1 227 ? 24.474 62.774 32.454 1.00 40.97 ? 410  PHE A HE1    1 
ATOM   3909 H HE2    . PHE A 1 227 ? 28.037 64.525 31.995 1.00 43.35 ? 410  PHE A HE2    1 
ATOM   3910 H HZ     . PHE A 1 227 ? 25.742 64.537 31.706 1.00 43.21 ? 410  PHE A HZ     1 
ATOM   3911 N N      . GLU A 1 228 ? 27.860 58.397 37.070 1.00 16.21 ? 411  GLU A N      1 
ATOM   3912 C CA     . GLU A 1 228 ? 28.576 57.330 37.742 1.00 15.62 ? 411  GLU A CA     1 
ATOM   3913 C C      . GLU A 1 228 ? 27.647 56.154 38.035 1.00 16.01 ? 411  GLU A C      1 
ATOM   3914 O O      . GLU A 1 228 ? 26.423 56.234 37.941 1.00 17.45 ? 411  GLU A O      1 
ATOM   3915 C CB     . GLU A 1 228 ? 29.182 57.822 39.052 1.00 16.04 ? 411  GLU A CB     1 
ATOM   3916 C CG     . GLU A 1 228 ? 30.324 58.778 38.824 1.00 19.07 ? 411  GLU A CG     1 
ATOM   3917 C CD     . GLU A 1 228 ? 30.827 59.366 40.095 1.00 21.68 ? 411  GLU A CD     1 
ATOM   3918 O OE1    . GLU A 1 228 ? 30.041 59.695 40.988 1.00 21.88 ? 411  GLU A OE1    1 
ATOM   3919 O OE2    . GLU A 1 228 ? 32.046 59.469 40.221 1.00 25.36 ? 411  GLU A OE2    1 
ATOM   3920 H H      . GLU A 1 228 ? 27.262 58.774 37.559 1.00 19.45 ? 411  GLU A H      1 
ATOM   3921 H HA     . GLU A 1 228 ? 29.287 57.020 37.161 1.00 18.74 ? 411  GLU A HA     1 
ATOM   3922 H HB2    . GLU A 1 228 ? 28.499 58.283 39.565 1.00 19.25 ? 411  GLU A HB2    1 
ATOM   3923 H HB3    . GLU A 1 228 ? 29.517 57.062 39.552 1.00 19.25 ? 411  GLU A HB3    1 
ATOM   3924 H HG2    . GLU A 1 228 ? 31.057 58.303 38.401 1.00 22.88 ? 411  GLU A HG2    1 
ATOM   3925 H HG3    . GLU A 1 228 ? 30.024 59.502 38.253 1.00 22.88 ? 411  GLU A HG3    1 
ATOM   3926 N N      . ASP A 1 229 ? 28.292 55.049 38.331 1.00 15.50 ? 412  ASP A N      1 
ATOM   3927 C CA     A ASP A 1 229 ? 27.651 53.853 38.851 0.66 14.55 ? 412  ASP A CA     1 
ATOM   3928 C CA     B ASP A 1 229 ? 27.691 53.818 38.827 0.34 15.47 ? 412  ASP A CA     1 
ATOM   3929 C C      . ASP A 1 229 ? 28.237 53.600 40.236 1.00 12.85 ? 412  ASP A C      1 
ATOM   3930 O O      . ASP A 1 229 ? 29.363 54.005 40.531 1.00 14.25 ? 412  ASP A O      1 
ATOM   3931 C CB     A ASP A 1 229 ? 27.959 52.628 37.982 0.66 17.65 ? 412  ASP A CB     1 
ATOM   3932 C CB     B ASP A 1 229 ? 28.145 52.663 37.905 0.34 18.51 ? 412  ASP A CB     1 
ATOM   3933 C CG     A ASP A 1 229 ? 27.637 52.861 36.551 0.66 20.84 ? 412  ASP A CG     1 
ATOM   3934 C CG     B ASP A 1 229 ? 27.718 51.300 38.399 0.34 21.55 ? 412  ASP A CG     1 
ATOM   3935 O OD1    A ASP A 1 229 ? 26.527 53.356 36.259 0.66 20.61 ? 412  ASP A OD1    1 
ATOM   3936 O OD1    B ASP A 1 229 ? 28.380 50.723 39.278 0.34 22.56 ? 412  ASP A OD1    1 
ATOM   3937 O OD2    A ASP A 1 229 ? 28.483 52.513 35.713 0.66 22.49 ? 412  ASP A OD2    1 
ATOM   3938 O OD2    B ASP A 1 229 ? 26.711 50.788 37.889 0.34 23.60 ? 412  ASP A OD2    1 
ATOM   3939 H H      A ASP A 1 229 ? 29.142 54.957 38.237 0.66 18.61 ? 412  ASP A H      1 
ATOM   3940 H H      B ASP A 1 229 ? 29.144 54.974 38.250 0.34 18.61 ? 412  ASP A H      1 
ATOM   3941 H HA     A ASP A 1 229 ? 26.689 53.970 38.887 0.66 17.46 ? 412  ASP A HA     1 
ATOM   3942 H HA     B ASP A 1 229 ? 26.722 53.845 38.859 0.34 18.56 ? 412  ASP A HA     1 
ATOM   3943 H HB2    A ASP A 1 229 ? 28.904 52.420 38.050 0.66 21.18 ? 412  ASP A HB2    1 
ATOM   3944 H HB2    B ASP A 1 229 ? 27.759 52.794 37.024 0.34 22.21 ? 412  ASP A HB2    1 
ATOM   3945 H HB3    A ASP A 1 229 ? 27.431 51.876 38.293 0.66 21.18 ? 412  ASP A HB3    1 
ATOM   3946 H HB3    B ASP A 1 229 ? 29.113 52.669 37.847 0.34 22.21 ? 412  ASP A HB3    1 
ATOM   3947 N N      . VAL A 1 230 ? 27.467 52.997 41.122 1.00 11.24 ? 413  VAL A N      1 
ATOM   3948 C CA     . VAL A 1 230 ? 27.950 52.610 42.446 1.00 11.48 ? 413  VAL A CA     1 
ATOM   3949 C C      . VAL A 1 230 ? 28.191 51.107 42.479 1.00 10.36 ? 413  VAL A C      1 
ATOM   3950 O O      . VAL A 1 230 ? 27.283 50.305 42.226 1.00 11.98 ? 413  VAL A O      1 
ATOM   3951 C CB     . VAL A 1 230 ? 26.971 53.033 43.542 1.00 13.02 ? 413  VAL A CB     1 
ATOM   3952 C CG1    . VAL A 1 230 ? 27.473 52.562 44.920 1.00 13.21 ? 413  VAL A CG1    1 
ATOM   3953 C CG2    . VAL A 1 230 ? 26.695 54.541 43.502 1.00 14.15 ? 413  VAL A CG2    1 
ATOM   3954 H H      . VAL A 1 230 ? 26.643 52.794 40.982 1.00 13.49 ? 413  VAL A H      1 
ATOM   3955 H HA     . VAL A 1 230 ? 28.803 53.046 42.601 1.00 13.77 ? 413  VAL A HA     1 
ATOM   3956 H HB     . VAL A 1 230 ? 26.117 52.601 43.384 1.00 15.62 ? 413  VAL A HB     1 
ATOM   3957 H HG11   . VAL A 1 230 ? 26.869 52.891 45.605 1.00 15.85 ? 413  VAL A HG11   1 
ATOM   3958 H HG12   . VAL A 1 230 ? 27.493 51.593 44.935 1.00 15.85 ? 413  VAL A HG12   1 
ATOM   3959 H HG13   . VAL A 1 230 ? 28.365 52.914 45.069 1.00 15.85 ? 413  VAL A HG13   1 
ATOM   3960 H HG21   . VAL A 1 230 ? 26.017 54.756 44.161 1.00 16.98 ? 413  VAL A HG21   1 
ATOM   3961 H HG22   . VAL A 1 230 ? 27.515 55.018 43.703 1.00 16.98 ? 413  VAL A HG22   1 
ATOM   3962 H HG23   . VAL A 1 230 ? 26.382 54.781 42.616 1.00 16.98 ? 413  VAL A HG23   1 
ATOM   3963 N N      . LYS A 1 231 ? 29.397 50.686 42.817 1.00 10.68 ? 414  LYS A N      1 
ATOM   3964 C CA     . LYS A 1 231 ? 29.722 49.300 43.093 1.00 11.40 ? 414  LYS A CA     1 
ATOM   3965 C C      . LYS A 1 231 ? 29.638 49.086 44.593 1.00 10.31 ? 414  LYS A C      1 
ATOM   3966 O O      . LYS A 1 231 ? 30.364 49.749 45.361 1.00 10.61 ? 414  LYS A O      1 
ATOM   3967 C CB     . LYS A 1 231 ? 31.131 49.005 42.593 1.00 15.16 ? 414  LYS A CB     1 
ATOM   3968 C CG     . LYS A 1 231 ? 31.274 49.190 41.089 1.00 23.64 ? 414  LYS A CG     1 
ATOM   3969 C CD     . LYS A 1 231 ? 32.237 48.208 40.431 1.00 32.40 ? 414  LYS A CD     1 
ATOM   3970 C CE     . LYS A 1 231 ? 31.733 46.783 40.552 1.00 35.60 ? 414  LYS A CE     1 
ATOM   3971 N NZ     . LYS A 1 231 ? 30.866 46.271 39.397 1.00 36.96 ? 414  LYS A NZ     1 
ATOM   3972 H H      . LYS A 1 231 ? 30.075 51.209 42.897 1.00 12.82 ? 414  LYS A H      1 
ATOM   3973 H HA     . LYS A 1 231 ? 29.095 48.701 42.657 1.00 13.68 ? 414  LYS A HA     1 
ATOM   3974 H HB2    . LYS A 1 231 ? 31.753 49.607 43.030 1.00 18.20 ? 414  LYS A HB2    1 
ATOM   3975 H HB3    . LYS A 1 231 ? 31.356 48.085 42.805 1.00 18.20 ? 414  LYS A HB3    1 
ATOM   3976 H HG2    . LYS A 1 231 ? 30.405 49.070 40.676 1.00 28.37 ? 414  LYS A HG2    1 
ATOM   3977 H HG3    . LYS A 1 231 ? 31.603 50.086 40.915 1.00 28.37 ? 414  LYS A HG3    1 
ATOM   3978 H HD2    . LYS A 1 231 ? 32.325 48.423 39.490 1.00 38.88 ? 414  LYS A HD2    1 
ATOM   3979 H HD3    . LYS A 1 231 ? 33.103 48.265 40.867 1.00 38.88 ? 414  LYS A HD3    1 
ATOM   3980 H HE2    . LYS A 1 231 ? 32.502 46.194 40.614 1.00 42.72 ? 414  LYS A HE2    1 
ATOM   3981 H HE3    . LYS A 1 231 ? 31.199 46.717 41.359 1.00 42.72 ? 414  LYS A HE3    1 
ATOM   3982 H HZ1    . LYS A 1 231 ? 30.597 45.440 39.564 1.00 44.35 ? 414  LYS A HZ1    1 
ATOM   3983 H HZ2    . LYS A 1 231 ? 30.152 46.792 39.299 1.00 44.35 ? 414  LYS A HZ2    1 
ATOM   3984 H HZ3    . LYS A 1 231 ? 31.334 46.276 38.640 1.00 44.35 ? 414  LYS A HZ3    1 
ATOM   3985 N N      . ALA A 1 232 ? 28.772 48.161 45.003 1.00 9.81  ? 415  ALA A N      1 
ATOM   3986 C CA     . ALA A 1 232 ? 28.526 47.871 46.393 1.00 9.89  ? 415  ALA A CA     1 
ATOM   3987 C C      . ALA A 1 232 ? 28.968 46.457 46.743 1.00 9.66  ? 415  ALA A C      1 
ATOM   3988 O O      . ALA A 1 232 ? 28.883 45.554 45.927 1.00 10.29 ? 415  ALA A O      1 
ATOM   3989 C CB     . ALA A 1 232 ? 27.033 48.047 46.737 1.00 10.92 ? 415  ALA A CB     1 
ATOM   3990 H H      . ALA A 1 232 ? 28.304 47.676 44.468 1.00 11.78 ? 415  ALA A H      1 
ATOM   3991 H HA     . ALA A 1 232 ? 29.048 48.481 46.937 1.00 11.87 ? 415  ALA A HA     1 
ATOM   3992 H HB1    . ALA A 1 232 ? 26.884 47.761 47.652 1.00 13.11 ? 415  ALA A HB1    1 
ATOM   3993 H HB2    . ALA A 1 232 ? 26.795 48.982 46.640 1.00 13.11 ? 415  ALA A HB2    1 
ATOM   3994 H HB3    . ALA A 1 232 ? 26.504 47.506 46.131 1.00 13.11 ? 415  ALA A HB3    1 
ATOM   3995 N N      . TYR A 1 233 ? 29.394 46.292 47.983 1.00 9.83  ? 416  TYR A N      1 
ATOM   3996 C CA     . TYR A 1 233 ? 30.010 45.051 48.467 1.00 10.80 ? 416  TYR A CA     1 
ATOM   3997 C C      . TYR A 1 233 ? 29.479 44.731 49.850 1.00 11.99 ? 416  TYR A C      1 
ATOM   3998 O O      . TYR A 1 233 ? 29.826 45.417 50.825 1.00 14.60 ? 416  TYR A O      1 
ATOM   3999 C CB     . TYR A 1 233 ? 31.538 45.227 48.547 1.00 11.27 ? 416  TYR A CB     1 
ATOM   4000 C CG     . TYR A 1 233 ? 32.203 45.582 47.263 1.00 12.47 ? 416  TYR A CG     1 
ATOM   4001 C CD1    . TYR A 1 233 ? 32.274 46.913 46.847 1.00 12.58 ? 416  TYR A CD1    1 
ATOM   4002 C CD2    . TYR A 1 233 ? 32.782 44.619 46.454 1.00 15.46 ? 416  TYR A CD2    1 
ATOM   4003 C CE1    . TYR A 1 233 ? 32.928 47.248 45.668 1.00 14.74 ? 416  TYR A CE1    1 
ATOM   4004 C CE2    . TYR A 1 233 ? 33.418 44.930 45.300 1.00 17.79 ? 416  TYR A CE2    1 
ATOM   4005 C CZ     . TYR A 1 233 ? 33.497 46.258 44.891 1.00 16.78 ? 416  TYR A CZ     1 
ATOM   4006 O OH     . TYR A 1 233 ? 34.123 46.574 43.706 1.00 21.18 ? 416  TYR A OH     1 
ATOM   4007 H H      . TYR A 1 233 ? 29.340 46.900 48.589 1.00 11.80 ? 416  TYR A H      1 
ATOM   4008 H HA     . TYR A 1 233 ? 29.770 44.325 47.869 1.00 12.96 ? 416  TYR A HA     1 
ATOM   4009 H HB2    . TYR A 1 233 ? 31.732 45.935 49.180 1.00 13.52 ? 416  TYR A HB2    1 
ATOM   4010 H HB3    . TYR A 1 233 ? 31.926 44.392 48.854 1.00 13.52 ? 416  TYR A HB3    1 
ATOM   4011 H HD1    . TYR A 1 233 ? 31.881 47.580 47.363 1.00 15.10 ? 416  TYR A HD1    1 
ATOM   4012 H HD2    . TYR A 1 233 ? 32.733 43.727 46.712 1.00 18.55 ? 416  TYR A HD2    1 
ATOM   4013 H HE1    . TYR A 1 233 ? 32.982 48.137 45.403 1.00 17.68 ? 416  TYR A HE1    1 
ATOM   4014 H HE2    . TYR A 1 233 ? 33.801 44.259 44.782 1.00 21.35 ? 416  TYR A HE2    1 
ATOM   4015 H HH     . TYR A 1 233 ? 34.086 47.402 43.573 1.00 25.42 ? 416  TYR A HH     1 
ATOM   4016 N N      . THR A 1 234 ? 28.703 43.642 49.982 1.00 9.76  ? 417  THR A N      1 
ATOM   4017 C CA     . THR A 1 234 ? 28.099 43.293 51.246 1.00 9.93  ? 417  THR A CA     1 
ATOM   4018 C C      . THR A 1 234 ? 28.943 42.275 52.001 1.00 10.14 ? 417  THR A C      1 
ATOM   4019 O O      . THR A 1 234 ? 29.639 41.445 51.400 1.00 11.16 ? 417  THR A O      1 
ATOM   4020 C CB     . THR A 1 234 ? 26.703 42.677 51.062 1.00 10.98 ? 417  THR A CB     1 
ATOM   4021 O OG1    . THR A 1 234 ? 26.768 41.336 50.531 1.00 11.02 ? 417  THR A OG1    1 
ATOM   4022 C CG2    . THR A 1 234 ? 25.832 43.528 50.156 1.00 11.68 ? 417  THR A CG2    1 
ATOM   4023 H H      . THR A 1 234 ? 28.519 43.097 49.342 1.00 11.71 ? 417  THR A H      1 
ATOM   4024 H HA     . THR A 1 234 ? 28.031 44.110 51.765 1.00 11.91 ? 417  THR A HA     1 
ATOM   4025 H HB     . THR A 1 234 ? 26.293 42.637 51.940 1.00 13.18 ? 417  THR A HB     1 
ATOM   4026 H HG1    . THR A 1 234 ? 27.001 40.799 51.134 1.00 13.22 ? 417  THR A HG1    1 
ATOM   4027 H HG21   . THR A 1 234 ? 24.933 43.165 50.124 1.00 14.01 ? 417  THR A HG21   1 
ATOM   4028 H HG22   . THR A 1 234 ? 25.792 44.437 50.492 1.00 14.01 ? 417  THR A HG22   1 
ATOM   4029 H HG23   . THR A 1 234 ? 26.199 43.541 49.258 1.00 14.01 ? 417  THR A HG23   1 
ATOM   4030 N N      . ILE A 1 235 ? 28.808 42.300 53.320 1.00 10.58 ? 418  ILE A N      1 
ATOM   4031 C CA     . ILE A 1 235 ? 29.263 41.193 54.186 1.00 12.58 ? 418  ILE A CA     1 
ATOM   4032 C C      . ILE A 1 235 ? 28.111 40.961 55.153 1.00 13.00 ? 418  ILE A C      1 
ATOM   4033 O O      . ILE A 1 235 ? 28.067 41.541 56.240 1.00 13.63 ? 418  ILE A O      1 
ATOM   4034 C CB     . ILE A 1 235 ? 30.572 41.474 54.941 1.00 12.96 ? 418  ILE A CB     1 
ATOM   4035 C CG1    . ILE A 1 235 ? 31.689 41.940 54.012 1.00 13.57 ? 418  ILE A CG1    1 
ATOM   4036 C CG2    . ILE A 1 235 ? 30.996 40.152 55.651 1.00 13.72 ? 418  ILE A CG2    1 
ATOM   4037 C CD1    . ILE A 1 235 ? 32.947 42.412 54.750 1.00 15.05 ? 418  ILE A CD1    1 
ATOM   4038 H H      . ILE A 1 235 ? 28.451 42.952 53.753 1.00 12.69 ? 418  ILE A H      1 
ATOM   4039 H HA     . ILE A 1 235 ? 29.416 40.403 53.645 1.00 15.10 ? 418  ILE A HA     1 
ATOM   4040 H HB     . ILE A 1 235 ? 30.420 42.191 55.576 1.00 15.55 ? 418  ILE A HB     1 
ATOM   4041 H HG12   . ILE A 1 235 ? 31.943 41.203 53.435 1.00 16.28 ? 418  ILE A HG12   1 
ATOM   4042 H HG13   . ILE A 1 235 ? 31.363 42.682 53.479 1.00 16.28 ? 418  ILE A HG13   1 
ATOM   4043 H HG21   . ILE A 1 235 ? 31.781 40.324 56.195 1.00 16.47 ? 418  ILE A HG21   1 
ATOM   4044 H HG22   . ILE A 1 235 ? 30.266 39.846 56.211 1.00 16.47 ? 418  ILE A HG22   1 
ATOM   4045 H HG23   . ILE A 1 235 ? 31.200 39.484 54.978 1.00 16.47 ? 418  ILE A HG23   1 
ATOM   4046 H HD11   . ILE A 1 235 ? 33.627 42.645 54.099 1.00 18.06 ? 418  ILE A HD11   1 
ATOM   4047 H HD12   . ILE A 1 235 ? 32.725 43.187 55.289 1.00 18.06 ? 418  ILE A HD12   1 
ATOM   4048 H HD13   . ILE A 1 235 ? 33.266 41.694 55.320 1.00 18.06 ? 418  ILE A HD13   1 
ATOM   4049 N N      . GLY A 1 236 ? 27.168 40.128 54.750 1.00 13.95 ? 419  GLY A N      1 
ATOM   4050 C CA     . GLY A 1 236 ? 25.935 39.986 55.450 1.00 14.50 ? 419  GLY A CA     1 
ATOM   4051 C C      . GLY A 1 236 ? 25.027 41.178 55.247 1.00 14.90 ? 419  GLY A C      1 
ATOM   4052 O O      . GLY A 1 236 ? 25.251 42.020 54.387 1.00 17.26 ? 419  GLY A O      1 
ATOM   4053 H H      . GLY A 1 236 ? 27.231 39.626 54.054 1.00 16.74 ? 419  GLY A H      1 
ATOM   4054 H HA2    . GLY A 1 236 ? 25.475 39.193 55.135 1.00 17.40 ? 419  GLY A HA2    1 
ATOM   4055 H HA3    . GLY A 1 236 ? 26.112 39.893 56.399 1.00 17.40 ? 419  GLY A HA3    1 
ATOM   4056 N N      . GLU A 1 237 ? 23.965 41.218 56.058 1.00 14.84 ? 420  GLU A N      1 
ATOM   4057 C CA     . GLU A 1 237 ? 22.895 42.189 55.903 1.00 15.89 ? 420  GLU A CA     1 
ATOM   4058 C C      . GLU A 1 237 ? 23.182 43.513 56.592 1.00 15.99 ? 420  GLU A C      1 
ATOM   4059 O O      . GLU A 1 237 ? 22.434 44.466 56.367 1.00 17.34 ? 420  GLU A O      1 
ATOM   4060 C CB     . GLU A 1 237 ? 21.586 41.578 56.416 1.00 19.08 ? 420  GLU A CB     1 
ATOM   4061 C CG     . GLU A 1 237 ? 21.038 40.440 55.548 1.00 21.74 ? 420  GLU A CG     1 
ATOM   4062 C CD     . GLU A 1 237 ? 19.720 39.871 56.056 1.00 28.02 ? 420  GLU A CD     1 
ATOM   4063 O OE1    . GLU A 1 237 ? 18.790 40.653 56.363 1.00 29.25 ? 420  GLU A OE1    1 
ATOM   4064 O OE2    . GLU A 1 237 ? 19.615 38.634 56.102 1.00 31.84 ? 420  GLU A OE2    1 
ATOM   4065 H H      . GLU A 1 237 ? 23.845 40.680 56.718 1.00 17.81 ? 420  GLU A H      1 
ATOM   4066 H HA     . GLU A 1 237 ? 22.774 42.395 54.963 1.00 19.07 ? 420  GLU A HA     1 
ATOM   4067 H HB2    . GLU A 1 237 ? 21.738 41.222 57.305 1.00 22.90 ? 420  GLU A HB2    1 
ATOM   4068 H HB3    . GLU A 1 237 ? 20.911 42.274 56.448 1.00 22.90 ? 420  GLU A HB3    1 
ATOM   4069 H HG2    . GLU A 1 237 ? 20.890 40.774 54.649 1.00 26.09 ? 420  GLU A HG2    1 
ATOM   4070 H HG3    . GLU A 1 237 ? 21.686 39.718 55.531 1.00 26.09 ? 420  GLU A HG3    1 
ATOM   4071 N N      . ASN A 1 238 ? 24.261 43.623 57.370 1.00 15.47 ? 421  ASN A N      1 
ATOM   4072 C CA     . ASN A 1 238 ? 24.517 44.822 58.166 1.00 17.14 ? 421  ASN A CA     1 
ATOM   4073 C C      . ASN A 1 238 ? 25.902 45.411 57.918 1.00 15.88 ? 421  ASN A C      1 
ATOM   4074 O O      . ASN A 1 238 ? 26.415 46.164 58.772 1.00 17.80 ? 421  ASN A O      1 
ATOM   4075 C CB     . ASN A 1 238 ? 24.344 44.486 59.643 1.00 20.45 ? 421  ASN A CB     1 
ATOM   4076 C CG     . ASN A 1 238 ? 22.929 44.088 59.970 1.00 25.23 ? 421  ASN A CG     1 
ATOM   4077 O OD1    . ASN A 1 238 ? 22.641 42.978 60.436 1.00 29.92 ? 421  ASN A OD1    1 
ATOM   4078 N ND2    . ASN A 1 238 ? 22.026 44.987 59.691 1.00 25.57 ? 421  ASN A ND2    1 
ATOM   4079 H H      . ASN A 1 238 ? 24.861 43.013 57.454 1.00 18.56 ? 421  ASN A H      1 
ATOM   4080 H HA     . ASN A 1 238 ? 23.881 45.510 57.915 1.00 20.57 ? 421  ASN A HA     1 
ATOM   4081 H HB2    . ASN A 1 238 ? 24.927 43.745 59.871 1.00 24.55 ? 421  ASN A HB2    1 
ATOM   4082 H HB3    . ASN A 1 238 ? 24.571 45.264 60.176 1.00 24.55 ? 421  ASN A HB3    1 
ATOM   4083 H HD21   . ASN A 1 238 ? 21.196 44.827 59.852 1.00 30.69 ? 421  ASN A HD21   1 
ATOM   4084 H HD22   . ASN A 1 238 ? 22.260 45.739 59.346 1.00 30.69 ? 421  ASN A HD22   1 
ATOM   4085 N N      . PHE A 1 239 ? 26.499 45.126 56.763 1.00 14.51 ? 422  PHE A N      1 
ATOM   4086 C CA     . PHE A 1 239 ? 27.766 45.717 56.364 1.00 11.91 ? 422  PHE A CA     1 
ATOM   4087 C C      . PHE A 1 239 ? 27.754 45.905 54.864 1.00 11.76 ? 422  PHE A C      1 
ATOM   4088 O O      . PHE A 1 239 ? 27.456 44.951 54.124 1.00 12.05 ? 422  PHE A O      1 
ATOM   4089 C CB     . PHE A 1 239 ? 28.945 44.828 56.781 1.00 12.63 ? 422  PHE A CB     1 
ATOM   4090 C CG     . PHE A 1 239 ? 30.268 45.333 56.308 1.00 13.53 ? 422  PHE A CG     1 
ATOM   4091 C CD1    . PHE A 1 239 ? 30.652 45.218 54.980 1.00 13.94 ? 422  PHE A CD1    1 
ATOM   4092 C CD2    . PHE A 1 239 ? 31.104 46.012 57.179 1.00 15.65 ? 422  PHE A CD2    1 
ATOM   4093 C CE1    . PHE A 1 239 ? 31.837 45.728 54.535 1.00 14.24 ? 422  PHE A CE1    1 
ATOM   4094 C CE2    . PHE A 1 239 ? 32.334 46.503 56.761 1.00 16.43 ? 422  PHE A CE2    1 
ATOM   4095 C CZ     . PHE A 1 239 ? 32.693 46.389 55.420 1.00 16.24 ? 422  PHE A CZ     1 
ATOM   4096 H H      . PHE A 1 239 ? 26.179 44.580 56.180 1.00 17.42 ? 422  PHE A H      1 
ATOM   4097 H HA     . PHE A 1 239 ? 27.875 46.584 56.786 1.00 14.29 ? 422  PHE A HA     1 
ATOM   4098 H HB2    . PHE A 1 239 ? 28.974 44.780 57.749 1.00 15.16 ? 422  PHE A HB2    1 
ATOM   4099 H HB3    . PHE A 1 239 ? 28.816 43.942 56.409 1.00 15.16 ? 422  PHE A HB3    1 
ATOM   4100 H HD1    . PHE A 1 239 ? 30.090 44.785 54.379 1.00 16.73 ? 422  PHE A HD1    1 
ATOM   4101 H HD2    . PHE A 1 239 ? 30.836 46.143 58.060 1.00 18.78 ? 422  PHE A HD2    1 
ATOM   4102 H HE1    . PHE A 1 239 ? 32.076 45.635 53.641 1.00 17.08 ? 422  PHE A HE1    1 
ATOM   4103 H HE2    . PHE A 1 239 ? 32.911 46.903 57.370 1.00 19.71 ? 422  PHE A HE2    1 
ATOM   4104 H HZ     . PHE A 1 239 ? 33.495 46.750 55.117 1.00 19.49 ? 422  PHE A HZ     1 
ATOM   4105 N N      . CYS A 1 240 ? 28.123 47.110 54.401 1.00 12.25 ? 423  CYS A N      1 
ATOM   4106 C CA     A CYS A 1 240 ? 28.296 47.313 52.973 0.82 13.08 ? 423  CYS A CA     1 
ATOM   4107 C CA     B CYS A 1 240 ? 28.262 47.340 52.973 0.18 13.68 ? 423  CYS A CA     1 
ATOM   4108 C C      . CYS A 1 240 ? 29.295 48.424 52.724 1.00 13.41 ? 423  CYS A C      1 
ATOM   4109 O O      . CYS A 1 240 ? 29.196 49.503 53.309 1.00 17.73 ? 423  CYS A O      1 
ATOM   4110 C CB     A CYS A 1 240 ? 26.986 47.674 52.271 0.82 13.93 ? 423  CYS A CB     1 
ATOM   4111 C CB     B CYS A 1 240 ? 26.924 47.796 52.397 0.18 15.78 ? 423  CYS A CB     1 
ATOM   4112 S SG     A CYS A 1 240 ? 26.993 47.746 50.459 0.82 14.63 ? 423  CYS A SG     1 
ATOM   4113 S SG     B CYS A 1 240 ? 26.118 49.020 53.467 0.18 17.38 ? 423  CYS A SG     1 
ATOM   4114 H H      A CYS A 1 240 ? 28.272 47.802 54.890 0.82 14.70 ? 423  CYS A H      1 
ATOM   4115 H H      B CYS A 1 240 ? 28.293 47.793 54.894 0.18 14.70 ? 423  CYS A H      1 
ATOM   4116 H HA     A CYS A 1 240 ? 28.639 46.484 52.603 0.82 15.69 ? 423  CYS A HA     1 
ATOM   4117 H HA     B CYS A 1 240 ? 28.564 46.526 52.541 0.18 16.42 ? 423  CYS A HA     1 
ATOM   4118 H HB2    A CYS A 1 240 ? 26.323 47.012 52.522 0.82 16.72 ? 423  CYS A HB2    1 
ATOM   4119 H HB2    B CYS A 1 240 ? 27.071 48.200 51.528 0.18 18.94 ? 423  CYS A HB2    1 
ATOM   4120 H HB3    A CYS A 1 240 ? 26.713 48.551 52.584 0.82 16.72 ? 423  CYS A HB3    1 
ATOM   4121 H HB3    B CYS A 1 240 ? 26.335 47.030 52.312 0.18 18.94 ? 423  CYS A HB3    1 
ATOM   4122 H HG     A CYS A 1 240 ? 27.826 48.533 50.102 0.82 17.56 ? 423  CYS A HG     1 
ATOM   4123 H HG     B CYS A 1 240 ? 26.907 49.883 53.737 0.18 20.85 ? 423  CYS A HG     1 
ATOM   4124 N N      . HIS A 1 241 ? 30.217 48.163 51.833 1.00 12.19 ? 424  HIS A N      1 
ATOM   4125 C CA     . HIS A 1 241 ? 31.190 49.138 51.374 1.00 11.20 ? 424  HIS A CA     1 
ATOM   4126 C C      . HIS A 1 241 ? 30.819 49.538 49.958 1.00 11.27 ? 424  HIS A C      1 
ATOM   4127 O O      . HIS A 1 241 ? 30.349 48.694 49.184 1.00 13.51 ? 424  HIS A O      1 
ATOM   4128 C CB     . HIS A 1 241 ? 32.558 48.467 51.389 1.00 12.78 ? 424  HIS A CB     1 
ATOM   4129 C CG     . HIS A 1 241 ? 33.667 49.371 50.962 1.00 13.80 ? 424  HIS A CG     1 
ATOM   4130 N ND1    . HIS A 1 241 ? 34.221 50.360 51.768 1.00 15.48 ? 424  HIS A ND1    1 
ATOM   4131 C CD2    . HIS A 1 241 ? 34.296 49.454 49.771 1.00 13.44 ? 424  HIS A CD2    1 
ATOM   4132 C CE1    . HIS A 1 241 ? 35.205 50.940 51.105 1.00 15.72 ? 424  HIS A CE1    1 
ATOM   4133 N NE2    . HIS A 1 241 ? 35.269 50.415 49.893 1.00 14.24 ? 424  HIS A NE2    1 
ATOM   4134 H H      . HIS A 1 241 ? 30.310 47.394 51.459 1.00 14.63 ? 424  HIS A H      1 
ATOM   4135 H HA     . HIS A 1 241 ? 31.215 49.939 51.920 1.00 13.43 ? 424  HIS A HA     1 
ATOM   4136 H HB2    . HIS A 1 241 ? 32.750 48.167 52.292 1.00 15.33 ? 424  HIS A HB2    1 
ATOM   4137 H HB3    . HIS A 1 241 ? 32.542 47.709 50.784 1.00 15.33 ? 424  HIS A HB3    1 
ATOM   4138 H HD2    . HIS A 1 241 ? 34.106 48.954 49.010 1.00 16.13 ? 424  HIS A HD2    1 
ATOM   4139 H HE1    . HIS A 1 241 ? 35.761 51.607 51.436 1.00 18.86 ? 424  HIS A HE1    1 
ATOM   4140 H HE2    . HIS A 1 241 ? 35.830 50.640 49.281 1.00 17.09 ? 424  HIS A HE2    1 
ATOM   4141 N N      . ALA A 1 242 ? 31.050 50.782 49.576 1.00 10.24 ? 425  ALA A N      1 
ATOM   4142 C CA     . ALA A 1 242 ? 30.651 51.206 48.234 1.00 10.03 ? 425  ALA A CA     1 
ATOM   4143 C C      . ALA A 1 242 ? 31.645 52.168 47.612 1.00 9.58  ? 425  ALA A C      1 
ATOM   4144 O O      . ALA A 1 242 ? 32.237 53.022 48.323 1.00 11.49 ? 425  ALA A O      1 
ATOM   4145 C CB     . ALA A 1 242 ? 29.294 51.897 48.266 1.00 11.70 ? 425  ALA A CB     1 
ATOM   4146 H H      . ALA A 1 242 ? 31.426 51.386 50.059 1.00 12.29 ? 425  ALA A H      1 
ATOM   4147 H HA     . ALA A 1 242 ? 30.630 50.413 47.676 1.00 12.04 ? 425  ALA A HA     1 
ATOM   4148 H HB1    . ALA A 1 242 ? 29.060 52.175 47.367 1.00 14.04 ? 425  ALA A HB1    1 
ATOM   4149 H HB2    . ALA A 1 242 ? 28.631 51.274 48.603 1.00 14.04 ? 425  ALA A HB2    1 
ATOM   4150 H HB3    . ALA A 1 242 ? 29.347 52.671 48.849 1.00 14.04 ? 425  ALA A HB3    1 
ATOM   4151 N N      . GLU A 1 243 ? 31.776 52.126 46.293 1.00 9.41  ? 426  GLU A N      1 
ATOM   4152 C CA     . GLU A 1 243 ? 32.647 52.982 45.514 1.00 10.85 ? 426  GLU A CA     1 
ATOM   4153 C C      . GLU A 1 243 ? 31.938 53.417 44.253 1.00 11.30 ? 426  GLU A C      1 
ATOM   4154 O O      . GLU A 1 243 ? 31.162 52.649 43.686 1.00 13.95 ? 426  GLU A O      1 
ATOM   4155 C CB     . GLU A 1 243 ? 33.918 52.224 45.146 1.00 13.13 ? 426  GLU A CB     1 
ATOM   4156 C CG     . GLU A 1 243 ? 34.628 51.743 46.403 1.00 15.96 ? 426  GLU A CG     1 
ATOM   4157 C CD     . GLU A 1 243 ? 35.875 50.901 46.216 1.00 20.20 ? 426  GLU A CD     1 
ATOM   4158 O OE1    . GLU A 1 243 ? 36.117 50.453 45.052 1.00 23.21 ? 426  GLU A OE1    1 
ATOM   4159 O OE2    . GLU A 1 243 ? 36.591 50.656 47.269 1.00 22.06 ? 426  GLU A OE2    1 
ATOM   4160 H H      . GLU A 1 243 ? 31.341 51.574 45.798 1.00 11.29 ? 426  GLU A H      1 
ATOM   4161 H HA     . GLU A 1 243 ? 32.872 53.780 46.017 1.00 13.02 ? 426  GLU A HA     1 
ATOM   4162 H HB2    . GLU A 1 243 ? 33.691 51.452 44.603 1.00 15.75 ? 426  GLU A HB2    1 
ATOM   4163 H HB3    . GLU A 1 243 ? 34.516 52.810 44.656 1.00 15.75 ? 426  GLU A HB3    1 
ATOM   4164 H HG2    . GLU A 1 243 ? 34.891 52.524 46.914 1.00 19.15 ? 426  GLU A HG2    1 
ATOM   4165 H HG3    . GLU A 1 243 ? 34.002 51.207 46.914 1.00 19.15 ? 426  GLU A HG3    1 
ATOM   4166 N N      . THR A 1 244 ? 32.178 54.621 43.828 1.00 11.15 ? 427  THR A N      1 
ATOM   4167 C CA     . THR A 1 244 ? 31.686 55.096 42.535 1.00 11.94 ? 427  THR A CA     1 
ATOM   4168 C C      . THR A 1 244 ? 32.719 54.899 41.427 1.00 12.81 ? 427  THR A C      1 
ATOM   4169 O O      . THR A 1 244 ? 33.945 54.972 41.649 1.00 13.57 ? 427  THR A O      1 
ATOM   4170 C CB     . THR A 1 244 ? 31.255 56.562 42.544 1.00 13.10 ? 427  THR A CB     1 
ATOM   4171 O OG1    . THR A 1 244 ? 32.391 57.363 42.845 1.00 14.84 ? 427  THR A OG1    1 
ATOM   4172 C CG2    . THR A 1 244 ? 30.198 56.808 43.553 1.00 14.64 ? 427  THR A CG2    1 
ATOM   4173 H H      . THR A 1 244 ? 32.631 55.207 44.266 1.00 13.38 ? 427  THR A H      1 
ATOM   4174 H HA     . THR A 1 244 ? 30.900 54.563 42.338 1.00 14.33 ? 427  THR A HA     1 
ATOM   4175 H HB     . THR A 1 244 ? 30.890 56.801 41.678 1.00 15.72 ? 427  THR A HB     1 
ATOM   4176 H HG1    . THR A 1 244 ? 32.192 58.177 42.784 1.00 17.80 ? 427  THR A HG1    1 
ATOM   4177 H HG21   . THR A 1 244 ? 29.944 57.744 43.546 1.00 17.57 ? 427  THR A HG21   1 
ATOM   4178 H HG22   . THR A 1 244 ? 29.417 56.268 43.354 1.00 17.57 ? 427  THR A HG22   1 
ATOM   4179 H HG23   . THR A 1 244 ? 30.523 56.577 44.437 1.00 17.57 ? 427  THR A HG23   1 
ATOM   4180 N N      . ARG A 1 245 ? 32.213 54.725 40.194 1.00 13.99 ? 428  ARG A N      1 
ATOM   4181 C CA     . ARG A 1 245 ? 33.032 54.741 39.001 1.00 15.96 ? 428  ARG A CA     1 
ATOM   4182 C C      . ARG A 1 245 ? 32.265 55.457 37.900 1.00 15.55 ? 428  ARG A C      1 
ATOM   4183 O O      . ARG A 1 245 ? 31.042 55.450 37.877 1.00 15.22 ? 428  ARG A O      1 
ATOM   4184 C CB     . ARG A 1 245 ? 33.431 53.334 38.532 1.00 21.41 ? 428  ARG A CB     1 
ATOM   4185 C CG     . ARG A 1 245 ? 32.297 52.375 38.515 1.00 29.02 ? 428  ARG A CG     1 
ATOM   4186 C CD     . ARG A 1 245 ? 32.642 51.115 37.752 1.00 38.21 ? 428  ARG A CD     1 
ATOM   4187 N NE     . ARG A 1 245 ? 31.476 50.724 36.968 1.00 44.35 ? 428  ARG A NE     1 
ATOM   4188 C CZ     . ARG A 1 245 ? 31.213 51.192 35.756 1.00 47.14 ? 428  ARG A CZ     1 
ATOM   4189 N NH1    . ARG A 1 245 ? 32.083 51.953 35.102 1.00 48.55 ? 428  ARG A NH1    1 
ATOM   4190 N NH2    . ARG A 1 245 ? 30.048 50.910 35.194 1.00 47.63 ? 428  ARG A NH2    1 
ATOM   4191 H H      . ARG A 1 245 ? 31.379 54.594 40.033 1.00 16.79 ? 428  ARG A H      1 
ATOM   4192 H HA     . ARG A 1 245 ? 33.853 55.224 39.184 1.00 19.16 ? 428  ARG A HA     1 
ATOM   4193 H HB2    . ARG A 1 245 ? 33.785 53.393 37.631 1.00 25.70 ? 428  ARG A HB2    1 
ATOM   4194 H HB3    . ARG A 1 245 ? 34.108 52.984 39.132 1.00 25.70 ? 428  ARG A HB3    1 
ATOM   4195 H HG2    . ARG A 1 245 ? 32.074 52.127 39.426 1.00 34.83 ? 428  ARG A HG2    1 
ATOM   4196 H HG3    . ARG A 1 245 ? 31.532 52.790 38.087 1.00 34.83 ? 428  ARG A HG3    1 
ATOM   4197 H HD2    . ARG A 1 245 ? 33.387 51.281 37.154 1.00 45.85 ? 428  ARG A HD2    1 
ATOM   4198 H HD3    . ARG A 1 245 ? 32.865 50.401 38.370 1.00 45.85 ? 428  ARG A HD3    1 
ATOM   4199 H HE     . ARG A 1 245 ? 30.928 50.157 37.311 1.00 53.23 ? 428  ARG A HE     1 
ATOM   4200 H HH11   . ARG A 1 245 ? 32.838 52.152 35.464 1.00 58.26 ? 428  ARG A HH11   1 
ATOM   4201 H HH12   . ARG A 1 245 ? 31.892 52.246 34.316 1.00 58.26 ? 428  ARG A HH12   1 
ATOM   4202 H HH21   . ARG A 1 245 ? 29.473 50.428 35.615 1.00 57.16 ? 428  ARG A HH21   1 
ATOM   4203 H HH22   . ARG A 1 245 ? 29.866 51.208 34.408 1.00 57.16 ? 428  ARG A HH22   1 
ATOM   4204 N N      . LYS A 1 246 ? 32.998 56.077 36.995 1.00 16.34 ? 429  LYS A N      1 
ATOM   4205 C CA     . LYS A 1 246 ? 32.390 56.739 35.844 1.00 17.67 ? 429  LYS A CA     1 
ATOM   4206 C C      . LYS A 1 246 ? 31.817 55.710 34.876 1.00 17.71 ? 429  LYS A C      1 
ATOM   4207 O O      . LYS A 1 246 ? 32.499 54.769 34.454 1.00 19.55 ? 429  LYS A O      1 
ATOM   4208 C CB     . LYS A 1 246 ? 33.460 57.617 35.176 1.00 19.87 ? 429  LYS A CB     1 
ATOM   4209 C CG     . LYS A 1 246 ? 33.099 58.189 33.819 1.00 23.51 ? 429  LYS A CG     1 
ATOM   4210 C CD     . LYS A 1 246 ? 32.091 59.310 33.862 1.00 28.56 ? 429  LYS A CD     1 
ATOM   4211 C CE     . LYS A 1 246 ? 31.973 59.985 32.474 1.00 31.16 ? 429  LYS A CE     1 
ATOM   4212 N NZ     . LYS A 1 246 ? 31.806 59.010 31.328 1.00 32.61 ? 429  LYS A NZ     1 
ATOM   4213 H H      . LYS A 1 246 ? 33.856 56.133 37.018 1.00 19.61 ? 429  LYS A H      1 
ATOM   4214 H HA     . LYS A 1 246 ? 31.648 57.302 36.117 1.00 21.21 ? 429  LYS A HA     1 
ATOM   4215 H HB2    . LYS A 1 246 ? 33.646 58.367 35.762 1.00 23.85 ? 429  LYS A HB2    1 
ATOM   4216 H HB3    . LYS A 1 246 ? 34.261 57.082 35.057 1.00 23.85 ? 429  LYS A HB3    1 
ATOM   4217 H HG2    . LYS A 1 246 ? 33.904 58.535 33.403 1.00 28.21 ? 429  LYS A HG2    1 
ATOM   4218 H HG3    . LYS A 1 246 ? 32.723 57.479 33.274 1.00 28.21 ? 429  LYS A HG3    1 
ATOM   4219 H HD2    . LYS A 1 246 ? 31.222 58.957 34.110 1.00 34.27 ? 429  LYS A HD2    1 
ATOM   4220 H HD3    . LYS A 1 246 ? 32.375 59.977 34.507 1.00 34.27 ? 429  LYS A HD3    1 
ATOM   4221 H HE2    . LYS A 1 246 ? 31.199 60.570 32.478 1.00 37.40 ? 429  LYS A HE2    1 
ATOM   4222 H HE3    . LYS A 1 246 ? 32.778 60.500 32.308 1.00 37.40 ? 429  LYS A HE3    1 
ATOM   4223 H HZ1    . LYS A 1 246 ? 31.729 59.453 30.560 1.00 39.13 ? 429  LYS A HZ1    1 
ATOM   4224 H HZ2    . LYS A 1 246 ? 32.514 58.472 31.281 1.00 39.13 ? 429  LYS A HZ2    1 
ATOM   4225 H HZ3    . LYS A 1 246 ? 31.076 58.516 31.452 1.00 39.13 ? 429  LYS A HZ3    1 
ATOM   4226 N N      . SER A 1 247 ? 30.568 55.902 34.505 1.00 17.57 ? 430  SER A N      1 
ATOM   4227 C CA     . SER A 1 247 ? 29.917 55.041 33.539 1.00 18.88 ? 430  SER A CA     1 
ATOM   4228 C C      . SER A 1 247 ? 30.157 55.564 32.128 1.00 19.46 ? 430  SER A C      1 
ATOM   4229 O O      . SER A 1 247 ? 30.086 56.775 31.891 1.00 19.43 ? 430  SER A O      1 
ATOM   4230 C CB     . SER A 1 247 ? 28.421 55.052 33.777 1.00 19.41 ? 430  SER A CB     1 
ATOM   4231 O OG     . SER A 1 247 ? 27.764 54.397 32.709 1.00 21.80 ? 430  SER A OG     1 
ATOM   4232 H H      . SER A 1 247 ? 30.065 56.533 34.801 1.00 21.09 ? 430  SER A H      1 
ATOM   4233 H HA     . SER A 1 247 ? 30.264 54.139 33.616 1.00 22.65 ? 430  SER A HA     1 
ATOM   4234 H HB2    . SER A 1 247 ? 28.225 54.588 34.607 1.00 23.30 ? 430  SER A HB2    1 
ATOM   4235 H HB3    . SER A 1 247 ? 28.111 55.969 33.829 1.00 23.30 ? 430  SER A HB3    1 
ATOM   4236 H HG     . SER A 1 247 ? 28.095 53.633 32.593 1.00 26.16 ? 430  SER A HG     1 
ATOM   4237 N N      . PRO A 1 248 ? 30.389 54.669 31.166 1.00 21.37 ? 431  PRO A N      1 
ATOM   4238 C CA     . PRO A 1 248 ? 30.528 55.092 29.762 1.00 23.54 ? 431  PRO A CA     1 
ATOM   4239 C C      . PRO A 1 248 ? 29.214 55.267 29.015 1.00 23.42 ? 431  PRO A C      1 
ATOM   4240 O O      . PRO A 1 248 ? 29.237 55.517 27.799 1.00 25.45 ? 431  PRO A O      1 
ATOM   4241 C CB     . PRO A 1 248 ? 31.330 53.936 29.135 1.00 25.32 ? 431  PRO A CB     1 
ATOM   4242 C CG     . PRO A 1 248 ? 30.896 52.740 29.923 1.00 24.36 ? 431  PRO A CG     1 
ATOM   4243 C CD     . PRO A 1 248 ? 30.656 53.230 31.352 1.00 22.18 ? 431  PRO A CD     1 
ATOM   4244 H HA     . PRO A 1 248 ? 31.038 55.916 29.720 1.00 28.25 ? 431  PRO A HA     1 
ATOM   4245 H HB2    . PRO A 1 248 ? 31.103 53.841 28.197 1.00 30.38 ? 431  PRO A HB2    1 
ATOM   4246 H HB3    . PRO A 1 248 ? 32.281 54.097 29.232 1.00 30.38 ? 431  PRO A HB3    1 
ATOM   4247 H HG2    . PRO A 1 248 ? 30.080 52.379 29.543 1.00 29.23 ? 431  PRO A HG2    1 
ATOM   4248 H HG3    . PRO A 1 248 ? 31.596 52.069 29.905 1.00 29.23 ? 431  PRO A HG3    1 
ATOM   4249 H HD2    . PRO A 1 248 ? 29.891 52.784 31.748 1.00 26.62 ? 431  PRO A HD2    1 
ATOM   4250 H HD3    . PRO A 1 248 ? 31.442 53.092 31.904 1.00 26.62 ? 431  PRO A HD3    1 
ATOM   4251 N N      . VAL A 1 249 ? 28.058 55.122 29.663 1.00 21.66 ? 432  VAL A N      1 
ATOM   4252 C CA     . VAL A 1 249 ? 26.845 54.978 28.860 1.00 23.17 ? 432  VAL A CA     1 
ATOM   4253 C C      . VAL A 1 249 ? 26.485 56.254 28.108 1.00 25.97 ? 432  VAL A C      1 
ATOM   4254 O O      . VAL A 1 249 ? 25.867 56.181 27.046 1.00 26.61 ? 432  VAL A O      1 
ATOM   4255 C CB     . VAL A 1 249 ? 25.646 54.419 29.647 1.00 23.16 ? 432  VAL A CB     1 
ATOM   4256 C CG1    . VAL A 1 249 ? 25.940 53.026 30.096 1.00 24.07 ? 432  VAL A CG1    1 
ATOM   4257 C CG2    . VAL A 1 249 ? 25.228 55.319 30.773 1.00 24.86 ? 432  VAL A CG2    1 
ATOM   4258 H H      . VAL A 1 249 ? 27.954 55.104 30.517 1.00 25.99 ? 432  VAL A H      1 
ATOM   4259 H HA     . VAL A 1 249 ? 27.067 54.304 28.199 1.00 27.81 ? 432  VAL A HA     1 
ATOM   4260 H HB     . VAL A 1 249 ? 24.876 54.383 29.058 1.00 27.79 ? 432  VAL A HB     1 
ATOM   4261 H HG11   . VAL A 1 249 ? 25.173 52.683 30.582 1.00 28.88 ? 432  VAL A HG11   1 
ATOM   4262 H HG12   . VAL A 1 249 ? 26.114 52.474 29.319 1.00 28.88 ? 432  VAL A HG12   1 
ATOM   4263 H HG13   . VAL A 1 249 ? 26.718 53.039 30.674 1.00 28.88 ? 432  VAL A HG13   1 
ATOM   4264 H HG21   . VAL A 1 249 ? 24.433 54.954 31.191 1.00 29.83 ? 432  VAL A HG21   1 
ATOM   4265 H HG22   . VAL A 1 249 ? 25.949 55.370 31.421 1.00 29.83 ? 432  VAL A HG22   1 
ATOM   4266 H HG23   . VAL A 1 249 ? 25.040 56.202 30.418 1.00 29.83 ? 432  VAL A HG23   1 
ATOM   4267 N N      . VAL A 1 250 ? 26.843 57.431 28.630 1.00 27.58 ? 433  VAL A N      1 
ATOM   4268 C CA     . VAL A 1 250 ? 26.477 58.678 27.963 1.00 30.59 ? 433  VAL A CA     1 
ATOM   4269 C C      . VAL A 1 250 ? 27.463 59.007 26.858 1.00 31.69 ? 433  VAL A C      1 
ATOM   4270 O O      . VAL A 1 250 ? 27.066 59.352 25.743 1.00 32.79 ? 433  VAL A O      1 
ATOM   4271 C CB     . VAL A 1 250 ? 26.383 59.820 28.990 1.00 33.87 ? 433  VAL A CB     1 
ATOM   4272 C CG1    . VAL A 1 250 ? 26.373 61.193 28.290 1.00 36.23 ? 433  VAL A CG1    1 
ATOM   4273 C CG2    . VAL A 1 250 ? 25.170 59.621 29.876 1.00 34.78 ? 433  VAL A CG2    1 
ATOM   4274 H H      . VAL A 1 250 ? 27.290 57.532 29.357 1.00 33.10 ? 433  VAL A H      1 
ATOM   4275 H HA     . VAL A 1 250 ? 25.604 58.563 27.557 1.00 36.71 ? 433  VAL A HA     1 
ATOM   4276 H HB     . VAL A 1 250 ? 27.168 59.808 29.560 1.00 40.64 ? 433  VAL A HB     1 
ATOM   4277 H HG11   . VAL A 1 250 ? 26.225 61.885 28.953 1.00 43.48 ? 433  VAL A HG11   1 
ATOM   4278 H HG12   . VAL A 1 250 ? 27.228 61.331 27.852 1.00 43.48 ? 433  VAL A HG12   1 
ATOM   4279 H HG13   . VAL A 1 250 ? 25.660 61.208 27.633 1.00 43.48 ? 433  VAL A HG13   1 
ATOM   4280 H HG21   . VAL A 1 250 ? 25.109 60.361 30.500 1.00 41.73 ? 433  VAL A HG21   1 
ATOM   4281 H HG22   . VAL A 1 250 ? 24.375 59.591 29.320 1.00 41.73 ? 433  VAL A HG22   1 
ATOM   4282 H HG23   . VAL A 1 250 ? 25.266 58.786 30.361 1.00 41.73 ? 433  VAL A HG23   1 
ATOM   4283 N N      . ASP A 1 251 ? 28.759 58.923 27.145 1.00 33.79 ? 434  ASP A N      1 
ATOM   4284 C CA     . ASP A 1 251 ? 29.768 59.500 26.267 1.00 36.64 ? 434  ASP A CA     1 
ATOM   4285 C C      . ASP A 1 251 ? 30.862 58.522 25.864 1.00 35.95 ? 434  ASP A C      1 
ATOM   4286 O O      . ASP A 1 251 ? 31.826 58.931 25.213 1.00 37.42 ? 434  ASP A O      1 
ATOM   4287 C CB     . ASP A 1 251 ? 30.404 60.726 26.935 1.00 40.20 ? 434  ASP A CB     1 
ATOM   4288 C CG     . ASP A 1 251 ? 31.105 60.386 28.251 1.00 42.82 ? 434  ASP A CG     1 
ATOM   4289 O OD1    . ASP A 1 251 ? 31.129 59.197 28.657 1.00 42.61 ? 434  ASP A OD1    1 
ATOM   4290 O OD2    . ASP A 1 251 ? 31.642 61.317 28.891 1.00 45.57 ? 434  ASP A OD2    1 
ATOM   4291 H H      . ASP A 1 251 ? 29.078 58.536 27.844 1.00 40.55 ? 434  ASP A H      1 
ATOM   4292 H HA     . ASP A 1 251 ? 29.327 59.779 25.449 1.00 43.97 ? 434  ASP A HA     1 
ATOM   4293 H HB2    . ASP A 1 251 ? 31.063 61.107 26.333 1.00 48.25 ? 434  ASP A HB2    1 
ATOM   4294 H HB3    . ASP A 1 251 ? 29.711 61.378 27.124 1.00 48.25 ? 434  ASP A HB3    1 
ATOM   4295 N N      . GLY A 1 252 ? 30.755 57.258 26.242 1.00 35.10 ? 435  GLY A N      1 
ATOM   4296 C CA     . GLY A 1 252 ? 31.763 56.285 25.881 1.00 35.93 ? 435  GLY A CA     1 
ATOM   4297 C C      . GLY A 1 252 ? 33.037 56.350 26.690 1.00 38.15 ? 435  GLY A C      1 
ATOM   4298 O O      . GLY A 1 252 ? 33.934 55.527 26.462 1.00 40.32 ? 435  GLY A O      1 
ATOM   4299 H H      . GLY A 1 252 ? 30.106 56.942 26.709 1.00 42.12 ? 435  GLY A H      1 
ATOM   4300 H HA2    . GLY A 1 252 ? 31.389 55.397 25.991 1.00 43.12 ? 435  GLY A HA2    1 
ATOM   4301 H HA3    . GLY A 1 252 ? 31.999 56.415 24.949 1.00 43.12 ? 435  GLY A HA3    1 
ATOM   4302 N N      . ILE A 1 253 ? 33.133 57.257 27.655 1.00 36.77 ? 436  ILE A N      1 
ATOM   4303 C CA     . ILE A 1 253 ? 34.379 57.491 28.376 1.00 38.15 ? 436  ILE A CA     1 
ATOM   4304 C C      . ILE A 1 253 ? 34.420 56.653 29.651 1.00 35.96 ? 436  ILE A C      1 
ATOM   4305 O O      . ILE A 1 253 ? 33.565 56.793 30.538 1.00 34.95 ? 436  ILE A O      1 
ATOM   4306 C CB     . ILE A 1 253 ? 34.550 58.985 28.695 1.00 42.45 ? 436  ILE A CB     1 
ATOM   4307 C CG1    . ILE A 1 253 ? 34.568 59.836 27.419 1.00 44.99 ? 436  ILE A CG1    1 
ATOM   4308 C CG2    . ILE A 1 253 ? 35.817 59.207 29.499 1.00 43.17 ? 436  ILE A CG2    1 
ATOM   4309 C CD1    . ILE A 1 253 ? 35.762 59.629 26.528 1.00 45.96 ? 436  ILE A CD1    1 
ATOM   4310 H H      . ILE A 1 253 ? 32.482 57.756 27.913 1.00 44.13 ? 436  ILE A H      1 
ATOM   4311 H HA     . ILE A 1 253 ? 35.113 57.193 27.817 1.00 45.78 ? 436  ILE A HA     1 
ATOM   4312 H HB     . ILE A 1 253 ? 33.785 59.263 29.223 1.00 50.94 ? 436  ILE A HB     1 
ATOM   4313 H HG12   . ILE A 1 253 ? 33.777 59.623 26.898 1.00 53.99 ? 436  ILE A HG12   1 
ATOM   4314 H HG13   . ILE A 1 253 ? 34.555 60.771 27.674 1.00 53.99 ? 436  ILE A HG13   1 
ATOM   4315 H HG21   . ILE A 1 253 ? 35.966 60.160 29.596 1.00 51.80 ? 436  ILE A HG21   1 
ATOM   4316 H HG22   . ILE A 1 253 ? 35.712 58.798 30.372 1.00 51.80 ? 436  ILE A HG22   1 
ATOM   4317 H HG23   . ILE A 1 253 ? 36.563 58.801 29.031 1.00 51.80 ? 436  ILE A HG23   1 
ATOM   4318 H HD11   . ILE A 1 253 ? 35.668 60.186 25.739 1.00 55.15 ? 436  ILE A HD11   1 
ATOM   4319 H HD12   . ILE A 1 253 ? 36.564 59.876 27.013 1.00 55.15 ? 436  ILE A HD12   1 
ATOM   4320 H HD13   . ILE A 1 253 ? 35.805 58.695 26.270 1.00 55.15 ? 436  ILE A HD13   1 
ATOM   4321 N N      . VAL A 1 254 ? 35.447 55.801 29.754 1.00 35.51 ? 437  VAL A N      1 
ATOM   4322 C CA     . VAL A 1 254 ? 35.841 55.131 30.992 1.00 35.76 ? 437  VAL A CA     1 
ATOM   4323 C C      . VAL A 1 254 ? 37.078 55.838 31.533 1.00 34.76 ? 437  VAL A C      1 
ATOM   4324 O O      . VAL A 1 254 ? 37.950 56.261 30.760 1.00 37.76 ? 437  VAL A O      1 
ATOM   4325 C CB     . VAL A 1 254 ? 36.138 53.648 30.693 1.00 39.61 ? 437  VAL A CB     1 
ATOM   4326 C CG1    . VAL A 1 254 ? 36.662 52.929 31.921 1.00 42.26 ? 437  VAL A CG1    1 
ATOM   4327 C CG2    . VAL A 1 254 ? 34.898 52.956 30.149 1.00 41.24 ? 437  VAL A CG2    1 
ATOM   4328 H H      . VAL A 1 254 ? 35.949 55.588 29.090 1.00 42.61 ? 437  VAL A H      1 
ATOM   4329 H HA     . VAL A 1 254 ? 35.139 55.188 31.660 1.00 42.91 ? 437  VAL A HA     1 
ATOM   4330 H HB     . VAL A 1 254 ? 36.831 53.607 30.015 1.00 47.53 ? 437  VAL A HB     1 
ATOM   4331 H HG11   . VAL A 1 254 ? 36.858 52.008 31.688 1.00 50.71 ? 437  VAL A HG11   1 
ATOM   4332 H HG12   . VAL A 1 254 ? 37.470 53.372 32.225 1.00 50.71 ? 437  VAL A HG12   1 
ATOM   4333 H HG13   . VAL A 1 254 ? 35.987 52.958 32.616 1.00 50.71 ? 437  VAL A HG13   1 
ATOM   4334 H HG21   . VAL A 1 254 ? 35.113 52.030 29.953 1.00 49.49 ? 437  VAL A HG21   1 
ATOM   4335 H HG22   . VAL A 1 254 ? 34.195 52.997 30.817 1.00 49.49 ? 437  VAL A HG22   1 
ATOM   4336 H HG23   . VAL A 1 254 ? 34.613 53.408 29.340 1.00 49.49 ? 437  VAL A HG23   1 
ATOM   4337 N N      . ARG A 1 255 ? 37.169 55.972 32.854 1.00 32.12 ? 438  ARG A N      1 
ATOM   4338 C CA     . ARG A 1 255 ? 38.322 56.607 33.488 1.00 32.33 ? 438  ARG A CA     1 
ATOM   4339 C C      . ARG A 1 255 ? 39.223 55.528 34.067 1.00 28.74 ? 438  ARG A C      1 
ATOM   4340 O O      . ARG A 1 255 ? 38.776 54.703 34.865 1.00 27.23 ? 438  ARG A O      1 
ATOM   4341 C CB     . ARG A 1 255 ? 37.884 57.584 34.581 1.00 37.00 ? 438  ARG A CB     1 
ATOM   4342 C CG     . ARG A 1 255 ? 37.160 58.822 34.028 1.00 41.61 ? 438  ARG A CG     1 
ATOM   4343 C CD     . ARG A 1 255 ? 38.138 59.890 33.536 1.00 46.82 ? 438  ARG A CD     1 
ATOM   4344 N NE     . ARG A 1 255 ? 37.478 60.911 32.729 1.00 50.18 ? 438  ARG A NE     1 
ATOM   4345 C CZ     . ARG A 1 255 ? 37.851 61.260 31.504 1.00 51.29 ? 438  ARG A CZ     1 
ATOM   4346 N NH1    . ARG A 1 255 ? 38.940 60.758 30.944 1.00 50.74 ? 438  ARG A NH1    1 
ATOM   4347 N NH2    . ARG A 1 255 ? 37.117 62.140 30.830 1.00 53.15 ? 438  ARG A NH2    1 
ATOM   4348 H H      . ARG A 1 255 ? 36.570 55.700 33.409 1.00 38.55 ? 438  ARG A H      1 
ATOM   4349 H HA     . ARG A 1 255 ? 38.821 57.104 32.821 1.00 38.79 ? 438  ARG A HA     1 
ATOM   4350 H HB2    . ARG A 1 255 ? 37.278 57.129 35.186 1.00 44.40 ? 438  ARG A HB2    1 
ATOM   4351 H HB3    . ARG A 1 255 ? 38.669 57.888 35.063 1.00 44.40 ? 438  ARG A HB3    1 
ATOM   4352 H HG2    . ARG A 1 255 ? 36.601 58.557 33.281 1.00 49.93 ? 438  ARG A HG2    1 
ATOM   4353 H HG3    . ARG A 1 255 ? 36.614 59.212 34.729 1.00 49.93 ? 438  ARG A HG3    1 
ATOM   4354 H HD2    . ARG A 1 255 ? 38.545 60.325 34.301 1.00 56.19 ? 438  ARG A HD2    1 
ATOM   4355 H HD3    . ARG A 1 255 ? 38.821 59.469 32.992 1.00 56.19 ? 438  ARG A HD3    1 
ATOM   4356 H HE     . ARG A 1 255 ? 36.800 61.315 33.071 1.00 60.22 ? 438  ARG A HE     1 
ATOM   4357 H HH11   . ARG A 1 255 ? 39.424 60.192 31.374 1.00 60.89 ? 438  ARG A HH11   1 
ATOM   4358 H HH12   . ARG A 1 255 ? 39.164 60.998 30.149 1.00 60.89 ? 438  ARG A HH12   1 
ATOM   4359 H HH21   . ARG A 1 255 ? 36.411 62.475 31.188 1.00 63.78 ? 438  ARG A HH21   1 
ATOM   4360 H HH22   . ARG A 1 255 ? 37.349 62.374 30.035 1.00 63.78 ? 438  ARG A HH22   1 
ATOM   4361 N N      . ARG A 1 256 ? 40.484 55.523 33.653 1.00 28.35 ? 439  ARG A N      1 
ATOM   4362 C CA     . ARG A 1 256 ? 41.452 54.575 34.168 1.00 28.74 ? 439  ARG A CA     1 
ATOM   4363 C C      . ARG A 1 256 ? 42.676 55.311 34.687 1.00 27.97 ? 439  ARG A C      1 
ATOM   4364 O O      . ARG A 1 256 ? 43.022 56.392 34.202 1.00 30.12 ? 439  ARG A O      1 
ATOM   4365 C CB     . ARG A 1 256 ? 41.894 53.605 33.071 1.00 31.11 ? 439  ARG A CB     1 
ATOM   4366 C CG     . ARG A 1 256 ? 40.792 52.710 32.575 1.00 35.07 ? 439  ARG A CG     1 
ATOM   4367 C CD     . ARG A 1 256 ? 41.332 51.696 31.574 1.00 39.71 ? 439  ARG A CD     1 
ATOM   4368 N NE     . ARG A 1 256 ? 40.275 50.828 31.073 1.00 43.48 ? 439  ARG A NE     1 
ATOM   4369 C CZ     . ARG A 1 256 ? 39.482 51.139 30.057 1.00 47.36 ? 439  ARG A CZ     1 
ATOM   4370 N NH1    . ARG A 1 256 ? 39.594 52.295 29.423 1.00 49.06 ? 439  ARG A NH1    1 
ATOM   4371 N NH2    . ARG A 1 256 ? 38.556 50.268 29.668 1.00 48.86 ? 439  ARG A NH2    1 
ATOM   4372 H H      . ARG A 1 256 ? 40.802 56.066 33.067 1.00 34.02 ? 439  ARG A H      1 
ATOM   4373 H HA     . ARG A 1 256 ? 41.058 54.080 34.903 1.00 34.48 ? 439  ARG A HA     1 
ATOM   4374 H HB2    . ARG A 1 256 ? 42.223 54.116 32.316 1.00 37.33 ? 439  ARG A HB2    1 
ATOM   4375 H HB3    . ARG A 1 256 ? 42.600 53.039 33.422 1.00 37.33 ? 439  ARG A HB3    1 
ATOM   4376 H HG2    . ARG A 1 256 ? 40.403 52.228 33.322 1.00 42.09 ? 439  ARG A HG2    1 
ATOM   4377 H HG3    . ARG A 1 256 ? 40.112 53.245 32.136 1.00 42.09 ? 439  ARG A HG3    1 
ATOM   4378 H HD2    . ARG A 1 256 ? 41.725 52.165 30.822 1.00 47.66 ? 439  ARG A HD2    1 
ATOM   4379 H HD3    . ARG A 1 256 ? 42.001 51.143 32.007 1.00 47.66 ? 439  ARG A HD3    1 
ATOM   4380 H HE     . ARG A 1 256 ? 40.158 50.069 31.459 1.00 52.17 ? 439  ARG A HE     1 
ATOM   4381 H HH11   . ARG A 1 256 ? 40.191 52.864 29.668 1.00 58.88 ? 439  ARG A HH11   1 
ATOM   4382 H HH12   . ARG A 1 256 ? 39.071 52.478 28.766 1.00 58.88 ? 439  ARG A HH12   1 
ATOM   4383 H HH21   . ARG A 1 256 ? 38.476 49.514 30.075 1.00 58.64 ? 439  ARG A HH21   1 
ATOM   4384 H HH22   . ARG A 1 256 ? 38.036 50.459 29.010 1.00 58.64 ? 439  ARG A HH22   1 
ATOM   4385 N N      . ASN A 1 257 ? 43.331 54.708 35.678 1.00 25.51 ? 440  ASN A N      1 
ATOM   4386 C CA     . ASN A 1 257 ? 44.593 55.223 36.199 1.00 26.32 ? 440  ASN A CA     1 
ATOM   4387 C C      . ASN A 1 257 ? 45.728 54.792 35.270 1.00 27.67 ? 440  ASN A C      1 
ATOM   4388 O O      . ASN A 1 257 ? 45.516 54.131 34.239 1.00 26.86 ? 440  ASN A O      1 
ATOM   4389 C CB     . ASN A 1 257 ? 44.773 54.833 37.669 1.00 26.36 ? 440  ASN A CB     1 
ATOM   4390 C CG     . ASN A 1 257 ? 45.073 53.357 37.874 1.00 25.50 ? 440  ASN A CG     1 
ATOM   4391 O OD1    . ASN A 1 257 ? 45.367 52.638 36.940 1.00 24.33 ? 440  ASN A OD1    1 
ATOM   4392 N ND2    . ASN A 1 257 ? 44.977 52.908 39.113 1.00 26.99 ? 440  ASN A ND2    1 
ATOM   4393 H H      . ASN A 1 257 ? 43.061 53.992 36.070 1.00 30.61 ? 440  ASN A H      1 
ATOM   4394 H HA     . ASN A 1 257 ? 44.594 56.193 36.201 1.00 31.59 ? 440  ASN A HA     1 
ATOM   4395 H HB2    . ASN A 1 257 ? 45.512 55.340 38.039 1.00 31.63 ? 440  ASN A HB2    1 
ATOM   4396 H HB3    . ASN A 1 257 ? 43.956 55.039 38.149 1.00 31.63 ? 440  ASN A HB3    1 
ATOM   4397 H HD21   . ASN A 1 257 ? 45.136 52.080 39.284 1.00 32.39 ? 440  ASN A HD21   1 
ATOM   4398 H HD22   . ASN A 1 257 ? 44.755 53.443 39.749 1.00 32.39 ? 440  ASN A HD22   1 
ATOM   4399 N N      . THR A 1 258 ? 46.957 55.182 35.628 1.00 29.43 ? 441  THR A N      1 
ATOM   4400 C CA     . THR A 1 258 ? 48.085 54.944 34.734 1.00 31.30 ? 441  THR A CA     1 
ATOM   4401 C C      . THR A 1 258 ? 48.362 53.454 34.581 1.00 29.06 ? 441  THR A C      1 
ATOM   4402 O O      . THR A 1 258 ? 48.921 53.026 33.559 1.00 28.99 ? 441  THR A O      1 
ATOM   4403 C CB     . THR A 1 258 ? 49.352 55.671 35.228 1.00 35.54 ? 441  THR A CB     1 
ATOM   4404 O OG1    . THR A 1 258 ? 49.699 55.237 36.548 1.00 38.05 ? 441  THR A OG1    1 
ATOM   4405 C CG2    . THR A 1 258 ? 49.124 57.203 35.220 1.00 38.47 ? 441  THR A CG2    1 
ATOM   4406 H H      . THR A 1 258 ? 47.156 55.577 36.366 1.00 35.32 ? 441  THR A H      1 
ATOM   4407 H HA     . THR A 1 258 ? 47.864 55.311 33.864 1.00 37.56 ? 441  THR A HA     1 
ATOM   4408 H HB     . THR A 1 258 ? 50.091 55.464 34.635 1.00 42.65 ? 441  THR A HB     1 
ATOM   4409 H HG1    . THR A 1 258 ? 49.069 55.401 37.079 1.00 45.66 ? 441  THR A HG1    1 
ATOM   4410 H HG21   . THR A 1 258 ? 49.920 57.658 35.535 1.00 46.17 ? 441  THR A HG21   1 
ATOM   4411 H HG22   . THR A 1 258 ? 48.923 57.504 34.320 1.00 46.17 ? 441  THR A HG22   1 
ATOM   4412 H HG23   . THR A 1 258 ? 48.381 57.430 35.801 1.00 46.17 ? 441  THR A HG23   1 
ATOM   4413 N N      . HIS A 1 259 ? 47.980 52.660 35.581 1.00 27.15 ? 442  HIS A N      1 
ATOM   4414 C CA     . HIS A 1 259 ? 48.131 51.212 35.525 1.00 25.57 ? 442  HIS A CA     1 
ATOM   4415 C C      . HIS A 1 259 ? 47.009 50.528 34.751 1.00 26.71 ? 442  HIS A C      1 
ATOM   4416 O O      . HIS A 1 259 ? 47.010 49.298 34.663 1.00 28.16 ? 442  HIS A O      1 
ATOM   4417 C CB     . HIS A 1 259 ? 48.230 50.619 36.948 1.00 24.94 ? 442  HIS A CB     1 
ATOM   4418 C CG     . HIS A 1 259 ? 49.567 50.837 37.590 1.00 24.44 ? 442  HIS A CG     1 
ATOM   4419 N ND1    . HIS A 1 259 ? 49.921 52.021 38.207 1.00 25.47 ? 442  HIS A ND1    1 
ATOM   4420 C CD2    . HIS A 1 259 ? 50.643 50.024 37.710 1.00 24.32 ? 442  HIS A CD2    1 
ATOM   4421 C CE1    . HIS A 1 259 ? 51.166 51.937 38.649 1.00 23.97 ? 442  HIS A CE1    1 
ATOM   4422 N NE2    . HIS A 1 259 ? 51.624 50.736 38.359 1.00 24.28 ? 442  HIS A NE2    1 
ATOM   4423 H H      . HIS A 1 259 ? 47.626 52.943 36.312 1.00 32.58 ? 442  HIS A H      1 
ATOM   4424 H HA     . HIS A 1 259 ? 48.966 51.010 35.075 1.00 30.69 ? 442  HIS A HA     1 
ATOM   4425 H HB2    . HIS A 1 259 ? 47.558 51.037 37.509 1.00 29.93 ? 442  HIS A HB2    1 
ATOM   4426 H HB3    . HIS A 1 259 ? 48.074 49.663 36.900 1.00 29.93 ? 442  HIS A HB3    1 
ATOM   4427 H HD1    . HIS A 1 259 ? 49.410 52.707 38.292 1.00 30.56 ? 442  HIS A HD1    1 
ATOM   4428 H HD2    . HIS A 1 259 ? 50.706 49.146 37.410 1.00 29.19 ? 442  HIS A HD2    1 
ATOM   4429 H HE1    . HIS A 1 259 ? 51.635 52.610 39.088 1.00 28.76 ? 442  HIS A HE1    1 
ATOM   4430 N N      . GLY A 1 260 ? 46.079 51.278 34.170 1.00 26.40 ? 443  GLY A N      1 
ATOM   4431 C CA     . GLY A 1 260 ? 44.998 50.685 33.410 1.00 27.88 ? 443  GLY A CA     1 
ATOM   4432 C C      . GLY A 1 260 ? 43.816 50.225 34.225 1.00 29.10 ? 443  GLY A C      1 
ATOM   4433 O O      . GLY A 1 260 ? 42.928 49.565 33.682 1.00 30.56 ? 443  GLY A O      1 
ATOM   4434 H H      . GLY A 1 260 ? 46.055 52.137 34.203 1.00 31.68 ? 443  GLY A H      1 
ATOM   4435 H HA2    . GLY A 1 260 ? 44.676 51.337 32.768 1.00 33.46 ? 443  GLY A HA2    1 
ATOM   4436 H HA3    . GLY A 1 260 ? 45.343 49.915 32.932 1.00 33.46 ? 443  GLY A HA3    1 
ATOM   4437 N N      . LYS A 1 261 ? 43.774 50.524 35.510 1.00 28.18 ? 444  LYS A N      1 
ATOM   4438 C CA     . LYS A 1 261 ? 42.677 50.077 36.352 1.00 28.17 ? 444  LYS A CA     1 
ATOM   4439 C C      . LYS A 1 261 ? 41.612 51.157 36.406 1.00 24.28 ? 444  LYS A C      1 
ATOM   4440 O O      . LYS A 1 261 ? 41.915 52.354 36.401 1.00 22.38 ? 444  LYS A O      1 
ATOM   4441 C CB     . LYS A 1 261 ? 43.175 49.727 37.756 1.00 33.86 ? 444  LYS A CB     1 
ATOM   4442 C CG     . LYS A 1 261 ? 44.374 48.780 37.754 1.00 39.39 ? 444  LYS A CG     1 
ATOM   4443 C CD     . LYS A 1 261 ? 44.207 47.646 36.751 1.00 45.56 ? 444  LYS A CD     1 
ATOM   4444 C CE     . LYS A 1 261 ? 45.550 46.992 36.385 1.00 49.44 ? 444  LYS A CE     1 
ATOM   4445 N NZ     . LYS A 1 261 ? 45.791 47.004 34.901 1.00 51.08 ? 444  LYS A NZ     1 
ATOM   4446 H H      . LYS A 1 261 ? 44.371 50.986 35.922 1.00 33.82 ? 444  LYS A H      1 
ATOM   4447 H HA     . LYS A 1 261 ? 42.278 49.274 35.983 1.00 33.81 ? 444  LYS A HA     1 
ATOM   4448 H HB2    . LYS A 1 261 ? 43.440 50.544 38.207 1.00 40.64 ? 444  LYS A HB2    1 
ATOM   4449 H HB3    . LYS A 1 261 ? 42.456 49.297 38.245 1.00 40.64 ? 444  LYS A HB3    1 
ATOM   4450 H HG2    . LYS A 1 261 ? 45.173 49.277 37.518 1.00 47.26 ? 444  LYS A HG2    1 
ATOM   4451 H HG3    . LYS A 1 261 ? 44.475 48.390 38.637 1.00 47.26 ? 444  LYS A HG3    1 
ATOM   4452 H HD2    . LYS A 1 261 ? 43.633 46.964 37.133 1.00 54.68 ? 444  LYS A HD2    1 
ATOM   4453 H HD3    . LYS A 1 261 ? 43.810 47.996 35.938 1.00 54.68 ? 444  LYS A HD3    1 
ATOM   4454 H HE2    . LYS A 1 261 ? 46.271 47.480 36.814 1.00 59.33 ? 444  LYS A HE2    1 
ATOM   4455 H HE3    . LYS A 1 261 ? 45.549 46.070 36.685 1.00 59.33 ? 444  LYS A HE3    1 
ATOM   4456 H HZ1    . LYS A 1 261 ? 46.589 46.655 34.720 1.00 61.30 ? 444  LYS A HZ1    1 
ATOM   4457 H HZ2    . LYS A 1 261 ? 45.165 46.526 34.487 1.00 61.30 ? 444  LYS A HZ2    1 
ATOM   4458 H HZ3    . LYS A 1 261 ? 45.765 47.840 34.595 1.00 61.30 ? 444  LYS A HZ3    1 
ATOM   4459 N N      . GLU A 1 262 ? 40.360 50.731 36.436 1.00 23.56 ? 445  GLU A N      1 
ATOM   4460 C CA     . GLU A 1 262 ? 39.285 51.704 36.503 1.00 23.33 ? 445  GLU A CA     1 
ATOM   4461 C C      . GLU A 1 262 ? 39.403 52.547 37.770 1.00 20.54 ? 445  GLU A C      1 
ATOM   4462 O O      . GLU A 1 262 ? 39.607 52.030 38.872 1.00 22.23 ? 445  GLU A O      1 
ATOM   4463 C CB     . GLU A 1 262 ? 37.942 50.990 36.475 1.00 27.27 ? 445  GLU A CB     1 
ATOM   4464 C CG     . GLU A 1 262 ? 36.781 51.925 36.273 1.00 32.31 ? 445  GLU A CG     1 
ATOM   4465 C CD     . GLU A 1 262 ? 35.592 51.214 35.666 1.00 37.87 ? 445  GLU A CD     1 
ATOM   4466 O OE1    . GLU A 1 262 ? 35.309 50.091 36.113 1.00 38.36 ? 445  GLU A OE1    1 
ATOM   4467 O OE2    . GLU A 1 262 ? 34.960 51.764 34.737 1.00 40.89 ? 445  GLU A OE2    1 
ATOM   4468 H H      . GLU A 1 262 ? 40.112 49.908 36.418 1.00 28.27 ? 445  GLU A H      1 
ATOM   4469 H HA     . GLU A 1 262 ? 39.339 52.296 35.736 1.00 27.99 ? 445  GLU A HA     1 
ATOM   4470 H HB2    . GLU A 1 262 ? 37.940 50.350 35.746 1.00 32.72 ? 445  GLU A HB2    1 
ATOM   4471 H HB3    . GLU A 1 262 ? 37.812 50.531 37.320 1.00 32.72 ? 445  GLU A HB3    1 
ATOM   4472 H HG2    . GLU A 1 262 ? 36.511 52.291 37.130 1.00 38.77 ? 445  GLU A HG2    1 
ATOM   4473 H HG3    . GLU A 1 262 ? 37.046 52.641 35.675 1.00 38.77 ? 445  GLU A HG3    1 
ATOM   4474 N N      . VAL A 1 263 ? 39.256 53.855 37.610 1.00 20.88 ? 446  VAL A N      1 
ATOM   4475 C CA     . VAL A 1 263 ? 39.298 54.752 38.756 1.00 19.40 ? 446  VAL A CA     1 
ATOM   4476 C C      . VAL A 1 263 ? 38.034 54.567 39.581 1.00 17.20 ? 446  VAL A C      1 
ATOM   4477 O O      . VAL A 1 263 ? 36.927 54.430 39.045 1.00 18.78 ? 446  VAL A O      1 
ATOM   4478 C CB     . VAL A 1 263 ? 39.432 56.198 38.253 1.00 21.25 ? 446  VAL A CB     1 
ATOM   4479 C CG1    . VAL A 1 263 ? 39.295 57.175 39.396 1.00 23.34 ? 446  VAL A CG1    1 
ATOM   4480 C CG2    . VAL A 1 263 ? 40.751 56.394 37.551 1.00 22.15 ? 446  VAL A CG2    1 
ATOM   4481 H H      . VAL A 1 263 ? 39.132 54.247 36.854 1.00 25.06 ? 446  VAL A H      1 
ATOM   4482 H HA     . VAL A 1 263 ? 40.059 54.544 39.321 1.00 23.28 ? 446  VAL A HA     1 
ATOM   4483 H HB     . VAL A 1 263 ? 38.720 56.371 37.618 1.00 25.50 ? 446  VAL A HB     1 
ATOM   4484 H HG11   . VAL A 1 263 ? 39.447 58.074 39.064 1.00 28.00 ? 446  VAL A HG11   1 
ATOM   4485 H HG12   . VAL A 1 263 ? 38.400 57.106 39.765 1.00 28.00 ? 446  VAL A HG12   1 
ATOM   4486 H HG13   . VAL A 1 263 ? 39.950 56.959 40.078 1.00 28.00 ? 446  VAL A HG13   1 
ATOM   4487 H HG21   . VAL A 1 263 ? 40.808 57.310 37.237 1.00 26.58 ? 446  VAL A HG21   1 
ATOM   4488 H HG22   . VAL A 1 263 ? 41.471 56.213 38.176 1.00 26.58 ? 446  VAL A HG22   1 
ATOM   4489 H HG23   . VAL A 1 263 ? 40.803 55.782 36.800 1.00 26.58 ? 446  VAL A HG23   1 
ATOM   4490 N N      . ARG A 1 264 ? 38.176 54.527 40.894 1.00 16.35 ? 447  ARG A N      1 
ATOM   4491 C CA     . ARG A 1 264 ? 37.035 54.376 41.785 1.00 16.62 ? 447  ARG A CA     1 
ATOM   4492 C C      . ARG A 1 264 ? 37.208 55.304 42.982 1.00 13.87 ? 447  ARG A C      1 
ATOM   4493 O O      . ARG A 1 264 ? 38.331 55.572 43.411 1.00 16.24 ? 447  ARG A O      1 
ATOM   4494 C CB     . ARG A 1 264 ? 36.923 52.938 42.282 1.00 23.41 ? 447  ARG A CB     1 
ATOM   4495 C CG     . ARG A 1 264 ? 36.752 51.900 41.205 1.00 30.32 ? 447  ARG A CG     1 
ATOM   4496 C CD     . ARG A 1 264 ? 35.434 51.178 41.311 1.00 34.55 ? 447  ARG A CD     1 
ATOM   4497 N NE     . ARG A 1 264 ? 35.237 50.317 40.151 1.00 36.70 ? 447  ARG A NE     1 
ATOM   4498 C CZ     . ARG A 1 264 ? 35.538 49.029 40.105 1.00 40.16 ? 447  ARG A CZ     1 
ATOM   4499 N NH1    . ARG A 1 264 ? 35.884 48.360 41.191 1.00 41.40 ? 447  ARG A NH1    1 
ATOM   4500 N NH2    . ARG A 1 264 ? 35.478 48.392 38.939 1.00 41.95 ? 447  ARG A NH2    1 
ATOM   4501 H H      . ARG A 1 264 ? 38.931 54.587 41.301 1.00 19.62 ? 447  ARG A H      1 
ATOM   4502 H HA     . ARG A 1 264 ? 36.219 54.618 41.319 1.00 19.95 ? 447  ARG A HA     1 
ATOM   4503 H HB2    . ARG A 1 264 ? 37.732 52.719 42.770 1.00 28.09 ? 447  ARG A HB2    1 
ATOM   4504 H HB3    . ARG A 1 264 ? 36.154 52.876 42.869 1.00 28.09 ? 447  ARG A HB3    1 
ATOM   4505 H HG2    . ARG A 1 264 ? 36.791 52.331 40.338 1.00 36.38 ? 447  ARG A HG2    1 
ATOM   4506 H HG3    . ARG A 1 264 ? 37.462 51.243 41.281 1.00 36.38 ? 447  ARG A HG3    1 
ATOM   4507 H HD2    . ARG A 1 264 ? 35.426 50.629 42.110 1.00 41.46 ? 447  ARG A HD2    1 
ATOM   4508 H HD3    . ARG A 1 264 ? 34.711 51.824 41.345 1.00 41.46 ? 447  ARG A HD3    1 
ATOM   4509 H HE     . ARG A 1 264 ? 34.900 50.673 39.444 1.00 44.04 ? 447  ARG A HE     1 
ATOM   4510 H HH11   . ARG A 1 264 ? 35.918 48.762 41.951 1.00 49.68 ? 447  ARG A HH11   1 
ATOM   4511 H HH12   . ARG A 1 264 ? 36.076 47.524 41.138 1.00 49.68 ? 447  ARG A HH12   1 
ATOM   4512 H HH21   . ARG A 1 264 ? 35.246 48.817 38.228 1.00 50.35 ? 447  ARG A HH21   1 
ATOM   4513 H HH22   . ARG A 1 264 ? 35.671 47.555 38.896 1.00 50.35 ? 447  ARG A HH22   1 
ATOM   4514 N N      . TYR A 1 265 ? 36.098 55.796 43.509 1.00 11.95 ? 448  TYR A N      1 
ATOM   4515 C CA     . TYR A 1 265 ? 36.100 56.670 44.675 1.00 11.47 ? 448  TYR A CA     1 
ATOM   4516 C C      . TYR A 1 265 ? 35.214 56.096 45.772 1.00 11.15 ? 448  TYR A C      1 
ATOM   4517 O O      . TYR A 1 265 ? 34.066 55.693 45.512 1.00 12.53 ? 448  TYR A O      1 
ATOM   4518 C CB     . TYR A 1 265 ? 35.590 58.070 44.310 1.00 12.51 ? 448  TYR A CB     1 
ATOM   4519 C CG     . TYR A 1 265 ? 36.454 58.778 43.307 1.00 13.00 ? 448  TYR A CG     1 
ATOM   4520 C CD1    . TYR A 1 265 ? 36.281 58.617 41.939 1.00 13.76 ? 448  TYR A CD1    1 
ATOM   4521 C CD2    . TYR A 1 265 ? 37.455 59.659 43.726 1.00 13.76 ? 448  TYR A CD2    1 
ATOM   4522 C CE1    . TYR A 1 265 ? 37.076 59.243 41.025 1.00 15.03 ? 448  TYR A CE1    1 
ATOM   4523 C CE2    . TYR A 1 265 ? 38.224 60.329 42.800 1.00 15.16 ? 448  TYR A CE2    1 
ATOM   4524 C CZ     . TYR A 1 265 ? 38.042 60.115 41.456 1.00 14.71 ? 448  TYR A CZ     1 
ATOM   4525 O OH     . TYR A 1 265 ? 38.802 60.757 40.512 1.00 16.70 ? 448  TYR A OH     1 
ATOM   4526 H H      . TYR A 1 265 ? 35.310 55.635 43.202 1.00 14.34 ? 448  TYR A H      1 
ATOM   4527 H HA     . TYR A 1 265 ? 37.007 56.728 45.013 1.00 13.77 ? 448  TYR A HA     1 
ATOM   4528 H HB2    . TYR A 1 265 ? 34.700 57.990 43.932 1.00 15.01 ? 448  TYR A HB2    1 
ATOM   4529 H HB3    . TYR A 1 265 ? 35.561 58.613 45.113 1.00 15.01 ? 448  TYR A HB3    1 
ATOM   4530 H HD1    . TYR A 1 265 ? 35.600 58.062 41.635 1.00 16.51 ? 448  TYR A HD1    1 
ATOM   4531 H HD2    . TYR A 1 265 ? 37.603 59.793 44.635 1.00 16.51 ? 448  TYR A HD2    1 
ATOM   4532 H HE1    . TYR A 1 265 ? 36.964 59.080 40.116 1.00 18.03 ? 448  TYR A HE1    1 
ATOM   4533 H HE2    . TYR A 1 265 ? 38.872 60.931 43.087 1.00 18.19 ? 448  TYR A HE2    1 
ATOM   4534 H HH     . TYR A 1 265 ? 39.319 61.305 40.884 1.00 20.04 ? 448  TYR A HH     1 
ATOM   4535 N N      . ILE A 1 266 ? 35.743 55.937 46.981 1.00 10.46 ? 449  ILE A N      1 
ATOM   4536 C CA     . ILE A 1 266 ? 34.899 55.480 48.069 1.00 10.54 ? 449  ILE A CA     1 
ATOM   4537 C C      . ILE A 1 266 ? 33.809 56.503 48.315 1.00 10.36 ? 449  ILE A C      1 
ATOM   4538 O O      . ILE A 1 266 ? 34.076 57.707 48.353 1.00 10.16 ? 449  ILE A O      1 
ATOM   4539 C CB     . ILE A 1 266 ? 35.754 55.216 49.324 1.00 10.64 ? 449  ILE A CB     1 
ATOM   4540 C CG1    . ILE A 1 266 ? 36.789 54.112 49.039 1.00 11.09 ? 449  ILE A CG1    1 
ATOM   4541 C CG2    . ILE A 1 266 ? 34.875 54.888 50.513 1.00 10.51 ? 449  ILE A CG2    1 
ATOM   4542 C CD1    . ILE A 1 266 ? 37.796 53.906 50.145 1.00 12.71 ? 449  ILE A CD1    1 
ATOM   4543 H H      . ILE A 1 266 ? 36.564 56.084 47.189 1.00 12.56 ? 449  ILE A H      1 
ATOM   4544 H HA     . ILE A 1 266 ? 34.471 54.643 47.829 1.00 12.65 ? 449  ILE A HA     1 
ATOM   4545 H HB     . ILE A 1 266 ? 36.243 56.024 49.547 1.00 12.77 ? 449  ILE A HB     1 
ATOM   4546 H HG12   . ILE A 1 266 ? 36.320 53.273 48.909 1.00 13.31 ? 449  ILE A HG12   1 
ATOM   4547 H HG13   . ILE A 1 266 ? 37.279 54.346 48.235 1.00 13.31 ? 449  ILE A HG13   1 
ATOM   4548 H HG21   . ILE A 1 266 ? 35.438 54.649 51.266 1.00 12.61 ? 449  ILE A HG21   1 
ATOM   4549 H HG22   . ILE A 1 266 ? 34.339 55.666 50.734 1.00 12.61 ? 449  ILE A HG22   1 
ATOM   4550 H HG23   . ILE A 1 266 ? 34.297 54.143 50.283 1.00 12.61 ? 449  ILE A HG23   1 
ATOM   4551 H HD11   . ILE A 1 266 ? 38.402 53.193 49.891 1.00 15.25 ? 449  ILE A HD11   1 
ATOM   4552 H HD12   . ILE A 1 266 ? 38.291 54.730 50.278 1.00 15.25 ? 449  ILE A HD12   1 
ATOM   4553 H HD13   . ILE A 1 266 ? 37.326 53.668 50.959 1.00 15.25 ? 449  ILE A HD13   1 
ATOM   4554 N N      . THR A 1 267 ? 32.578 56.022 48.526 1.00 10.67 ? 450  THR A N      1 
ATOM   4555 C CA     . THR A 1 267 ? 31.428 56.862 48.769 1.00 11.90 ? 450  THR A CA     1 
ATOM   4556 C C      . THR A 1 267 ? 30.680 56.366 49.971 1.00 13.36 ? 450  THR A C      1 
ATOM   4557 O O      . THR A 1 267 ? 30.657 55.157 50.215 1.00 18.69 ? 450  THR A O      1 
ATOM   4558 C CB     . THR A 1 267 ? 30.525 56.928 47.517 1.00 11.46 ? 450  THR A CB     1 
ATOM   4559 O OG1    . THR A 1 267 ? 29.533 57.952 47.652 1.00 12.17 ? 450  THR A OG1    1 
ATOM   4560 C CG2    . THR A 1 267 ? 29.784 55.623 47.241 1.00 11.92 ? 450  THR A CG2    1 
ATOM   4561 H H      . THR A 1 267 ? 32.389 55.183 48.531 1.00 12.80 ? 450  THR A H      1 
ATOM   4562 H HA     . THR A 1 267 ? 31.704 57.768 48.976 1.00 14.28 ? 450  THR A HA     1 
ATOM   4563 H HB     . THR A 1 267 ? 31.116 57.112 46.771 1.00 13.75 ? 450  THR A HB     1 
ATOM   4564 H HG1    . THR A 1 267 ? 29.887 58.657 47.941 1.00 14.61 ? 450  THR A HG1    1 
ATOM   4565 H HG21   . THR A 1 267 ? 29.233 55.715 46.448 1.00 14.31 ? 450  THR A HG21   1 
ATOM   4566 H HG22   . THR A 1 267 ? 30.420 54.904 47.100 1.00 14.31 ? 450  THR A HG22   1 
ATOM   4567 H HG23   . THR A 1 267 ? 29.216 55.397 47.994 1.00 14.31 ? 450  THR A HG23   1 
ATOM   4568 N N      . GLU A 1 268 ? 29.977 57.262 50.647 1.00 12.67 ? 451  GLU A N      1 
ATOM   4569 C CA     . GLU A 1 268 ? 29.116 56.951 51.788 1.00 13.38 ? 451  GLU A CA     1 
ATOM   4570 C C      . GLU A 1 268 ? 27.735 56.521 51.283 1.00 13.16 ? 451  GLU A C      1 
ATOM   4571 O O      . GLU A 1 268 ? 27.181 57.156 50.391 1.00 14.75 ? 451  GLU A O      1 
ATOM   4572 C CB     . GLU A 1 268 ? 28.974 58.204 52.669 1.00 15.37 ? 451  GLU A CB     1 
ATOM   4573 C CG     . GLU A 1 268 ? 30.322 58.677 53.212 1.00 15.92 ? 451  GLU A CG     1 
ATOM   4574 C CD     . GLU A 1 268 ? 30.248 59.891 54.156 1.00 17.45 ? 451  GLU A CD     1 
ATOM   4575 O OE1    . GLU A 1 268 ? 29.157 60.412 54.493 1.00 20.03 ? 451  GLU A OE1    1 
ATOM   4576 O OE2    . GLU A 1 268 ? 31.329 60.346 54.612 1.00 16.21 ? 451  GLU A OE2    1 
ATOM   4577 H H      . GLU A 1 268 ? 29.978 58.101 50.459 1.00 15.21 ? 451  GLU A H      1 
ATOM   4578 H HA     . GLU A 1 268 ? 29.494 56.231 52.318 1.00 16.06 ? 451  GLU A HA     1 
ATOM   4579 H HB2    . GLU A 1 268 ? 28.590 58.922 52.142 1.00 18.44 ? 451  GLU A HB2    1 
ATOM   4580 H HB3    . GLU A 1 268 ? 28.398 58.000 53.422 1.00 18.44 ? 451  GLU A HB3    1 
ATOM   4581 H HG2    . GLU A 1 268 ? 30.728 57.948 53.707 1.00 19.10 ? 451  GLU A HG2    1 
ATOM   4582 H HG3    . GLU A 1 268 ? 30.886 58.925 52.463 1.00 19.10 ? 451  GLU A HG3    1 
ATOM   4583 N N      . LEU A 1 269 ? 27.186 55.476 51.871 1.00 14.09 ? 452  LEU A N      1 
ATOM   4584 C CA     . LEU A 1 269 ? 25.829 55.041 51.565 1.00 14.58 ? 452  LEU A CA     1 
ATOM   4585 C C      . LEU A 1 269 ? 24.818 55.702 52.488 1.00 16.38 ? 452  LEU A C      1 
ATOM   4586 O O      . LEU A 1 269 ? 25.046 55.872 53.692 1.00 17.39 ? 452  LEU A O      1 
ATOM   4587 C CB     . LEU A 1 269 ? 25.700 53.530 51.739 1.00 15.35 ? 452  LEU A CB     1 
ATOM   4588 C CG     . LEU A 1 269 ? 26.488 52.694 50.731 1.00 15.29 ? 452  LEU A CG     1 
ATOM   4589 C CD1    . LEU A 1 269 ? 26.317 51.197 51.054 1.00 20.27 ? 452  LEU A CD1    1 
ATOM   4590 C CD2    . LEU A 1 269 ? 26.158 52.952 49.244 1.00 14.44 ? 452  LEU A CD2    1 
ATOM   4591 H H      . LEU A 1 269 ? 27.581 54.992 52.461 1.00 16.91 ? 452  LEU A H      1 
ATOM   4592 H HA     . LEU A 1 269 ? 25.633 55.289 50.648 1.00 17.50 ? 452  LEU A HA     1 
ATOM   4593 H HB2    . LEU A 1 269 ? 26.019 53.295 52.624 1.00 18.42 ? 452  LEU A HB2    1 
ATOM   4594 H HB3    . LEU A 1 269 ? 24.765 53.290 51.649 1.00 18.42 ? 452  LEU A HB3    1 
ATOM   4595 H HG     . LEU A 1 269 ? 27.413 52.970 50.825 1.00 18.35 ? 452  LEU A HG     1 
ATOM   4596 H HD11   . LEU A 1 269 ? 26.765 50.673 50.371 1.00 24.32 ? 452  LEU A HD11   1 
ATOM   4597 H HD12   . LEU A 1 269 ? 26.711 51.014 51.921 1.00 24.32 ? 452  LEU A HD12   1 
ATOM   4598 H HD13   . LEU A 1 269 ? 25.371 50.982 51.068 1.00 24.32 ? 452  LEU A HD13   1 
ATOM   4599 H HD21   . LEU A 1 269 ? 26.682 52.349 48.695 1.00 17.33 ? 452  LEU A HD21   1 
ATOM   4600 H HD22   . LEU A 1 269 ? 25.212 52.795 49.098 1.00 17.33 ? 452  LEU A HD22   1 
ATOM   4601 H HD23   . LEU A 1 269 ? 26.378 53.872 49.027 1.00 17.33 ? 452  LEU A HD23   1 
ATOM   4602 N N      . SER A 1 270 ? 23.666 56.029 51.921 1.00 15.29 ? 453  SER A N      1 
ATOM   4603 C CA     . SER A 1 270 ? 22.546 56.466 52.724 1.00 16.87 ? 453  SER A CA     1 
ATOM   4604 C C      . SER A 1 270 ? 21.960 55.281 53.491 1.00 15.60 ? 453  SER A C      1 
ATOM   4605 O O      . SER A 1 270 ? 22.210 54.121 53.168 1.00 13.63 ? 453  SER A O      1 
ATOM   4606 C CB     . SER A 1 270 ? 21.488 57.099 51.829 1.00 17.16 ? 453  SER A CB     1 
ATOM   4607 O OG     . SER A 1 270 ? 20.909 56.067 51.037 1.00 16.07 ? 453  SER A OG     1 
ATOM   4608 H H      . SER A 1 270 ? 23.511 56.006 51.076 1.00 18.35 ? 453  SER A H      1 
ATOM   4609 H HA     . SER A 1 270 ? 22.837 57.129 53.370 1.00 20.25 ? 453  SER A HA     1 
ATOM   4610 H HB2    . SER A 1 270 ? 20.803 57.515 52.376 1.00 20.60 ? 453  SER A HB2    1 
ATOM   4611 H HB3    . SER A 1 270 ? 21.900 57.762 51.253 1.00 20.60 ? 453  SER A HB3    1 
ATOM   4612 H HG     . SER A 1 270 ? 20.302 56.384 50.551 1.00 19.28 ? 453  SER A HG     1 
ATOM   4613 N N      . ASP A 1 271 ? 21.124 55.561 54.495 1.00 17.67 ? 454  ASP A N      1 
ATOM   4614 C CA     . ASP A 1 271 ? 20.450 54.479 55.208 1.00 19.15 ? 454  ASP A CA     1 
ATOM   4615 C C      . ASP A 1 271 ? 19.597 53.656 54.245 1.00 16.33 ? 454  ASP A C      1 
ATOM   4616 O O      . ASP A 1 271 ? 19.543 52.422 54.350 1.00 16.15 ? 454  ASP A O      1 
ATOM   4617 C CB     . ASP A 1 271 ? 19.597 55.007 56.358 1.00 21.68 ? 454  ASP A CB     1 
ATOM   4618 C CG     . ASP A 1 271 ? 20.419 55.444 57.572 1.00 25.48 ? 454  ASP A CG     1 
ATOM   4619 O OD1    . ASP A 1 271 ? 21.671 55.325 57.561 1.00 26.07 ? 454  ASP A OD1    1 
ATOM   4620 O OD2    . ASP A 1 271 ? 19.795 55.947 58.532 1.00 28.23 ? 454  ASP A OD2    1 
ATOM   4621 H H      . ASP A 1 271 ? 20.935 56.352 54.776 1.00 21.20 ? 454  ASP A H      1 
ATOM   4622 H HA     . ASP A 1 271 ? 21.127 53.907 55.602 1.00 22.98 ? 454  ASP A HA     1 
ATOM   4623 H HB2    . ASP A 1 271 ? 19.093 55.776 56.048 1.00 26.01 ? 454  ASP A HB2    1 
ATOM   4624 H HB3    . ASP A 1 271 ? 18.990 54.307 56.646 1.00 26.01 ? 454  ASP A HB3    1 
ATOM   4625 N N      . GLU A 1 272 ? 18.940 54.316 53.290 1.00 15.93 ? 455  GLU A N      1 
ATOM   4626 C CA     A GLU A 1 272 ? 18.128 53.582 52.331 0.55 15.30 ? 455  GLU A CA     1 
ATOM   4627 C CA     B GLU A 1 272 ? 18.126 53.582 52.324 0.45 16.19 ? 455  GLU A CA     1 
ATOM   4628 C C      . GLU A 1 272 ? 18.983 52.635 51.496 1.00 13.65 ? 455  GLU A C      1 
ATOM   4629 O O      . GLU A 1 272 ? 18.573 51.501 51.219 1.00 13.91 ? 455  GLU A O      1 
ATOM   4630 C CB     A GLU A 1 272 ? 17.371 54.589 51.475 0.55 16.16 ? 455  GLU A CB     1 
ATOM   4631 C CB     B GLU A 1 272 ? 17.354 54.538 51.410 0.45 19.51 ? 455  GLU A CB     1 
ATOM   4632 C CG     A GLU A 1 272 ? 16.373 55.397 52.283 0.55 18.89 ? 455  GLU A CG     1 
ATOM   4633 C CG     B GLU A 1 272 ? 17.034 53.931 50.036 0.45 25.36 ? 455  GLU A CG     1 
ATOM   4634 C CD     A GLU A 1 272 ? 16.885 56.729 52.885 0.55 23.34 ? 455  GLU A CD     1 
ATOM   4635 C CD     B GLU A 1 272 ? 15.942 54.662 49.286 0.45 31.12 ? 455  GLU A CD     1 
ATOM   4636 O OE1    A GLU A 1 272 ? 18.098 56.999 53.132 0.55 20.82 ? 455  GLU A OE1    1 
ATOM   4637 O OE1    B GLU A 1 272 ? 15.628 55.819 49.650 0.45 33.07 ? 455  GLU A OE1    1 
ATOM   4638 O OE2    A GLU A 1 272 ? 15.973 57.534 53.121 0.55 27.14 ? 455  GLU A OE2    1 
ATOM   4639 O OE2    B GLU A 1 272 ? 15.384 54.067 48.336 0.45 33.19 ? 455  GLU A OE2    1 
ATOM   4640 H H      A GLU A 1 272 ? 18.950 55.169 53.180 0.55 19.12 ? 455  GLU A H      1 
ATOM   4641 H H      B GLU A 1 272 ? 18.949 55.169 53.182 0.45 19.12 ? 455  GLU A H      1 
ATOM   4642 H HA     A GLU A 1 272 ? 17.477 53.027 52.787 0.55 18.36 ? 455  GLU A HA     1 
ATOM   4643 H HA     B GLU A 1 272 ? 17.473 53.061 52.817 0.45 19.42 ? 455  GLU A HA     1 
ATOM   4644 H HB2    A GLU A 1 272 ? 18.004 55.205 51.074 0.55 19.40 ? 455  GLU A HB2    1 
ATOM   4645 H HB2    B GLU A 1 272 ? 16.515 54.771 51.837 0.45 23.41 ? 455  GLU A HB2    1 
ATOM   4646 H HB3    A GLU A 1 272 ? 16.886 54.115 50.782 0.55 19.40 ? 455  GLU A HB3    1 
ATOM   4647 H HB3    B GLU A 1 272 ? 17.887 55.335 51.268 0.45 23.41 ? 455  GLU A HB3    1 
ATOM   4648 H HG2    A GLU A 1 272 ? 15.625 55.616 51.706 0.55 22.66 ? 455  GLU A HG2    1 
ATOM   4649 H HG2    B GLU A 1 272 ? 17.835 53.956 49.490 0.45 30.43 ? 455  GLU A HG2    1 
ATOM   4650 H HG3    A GLU A 1 272 ? 16.071 54.849 53.024 0.55 22.66 ? 455  GLU A HG3    1 
ATOM   4651 H HG3    B GLU A 1 272 ? 16.745 53.014 50.159 0.45 30.43 ? 455  GLU A HG3    1 
ATOM   4652 N N      . GLU A 1 273 ? 20.169 53.087 51.085 1.00 12.23 ? 456  GLU A N      1 
ATOM   4653 C CA     . GLU A 1 273 ? 21.070 52.242 50.312 1.00 11.60 ? 456  GLU A CA     1 
ATOM   4654 C C      . GLU A 1 273 ? 21.618 51.098 51.143 1.00 11.24 ? 456  GLU A C      1 
ATOM   4655 O O      . GLU A 1 273 ? 21.771 49.987 50.639 1.00 11.27 ? 456  GLU A O      1 
ATOM   4656 C CB     . GLU A 1 273 ? 22.206 53.068 49.719 1.00 13.00 ? 456  GLU A CB     1 
ATOM   4657 C CG     . GLU A 1 273 ? 21.759 53.996 48.610 1.00 13.91 ? 456  GLU A CG     1 
ATOM   4658 C CD     . GLU A 1 273 ? 22.772 55.024 48.203 1.00 15.90 ? 456  GLU A CD     1 
ATOM   4659 O OE1    . GLU A 1 273 ? 23.642 55.417 49.017 1.00 15.80 ? 456  GLU A OE1    1 
ATOM   4660 O OE2    . GLU A 1 273 ? 22.675 55.450 47.033 1.00 18.39 ? 456  GLU A OE2    1 
ATOM   4661 H H      . GLU A 1 273 ? 20.473 53.877 51.241 1.00 14.68 ? 456  GLU A H      1 
ATOM   4662 H HA     . GLU A 1 273 ? 20.572 51.861 49.573 1.00 13.92 ? 456  GLU A HA     1 
ATOM   4663 H HB2    . GLU A 1 273 ? 22.599 53.610 50.420 1.00 15.60 ? 456  GLU A HB2    1 
ATOM   4664 H HB3    . GLU A 1 273 ? 22.872 52.466 49.352 1.00 15.60 ? 456  GLU A HB3    1 
ATOM   4665 H HG2    . GLU A 1 273 ? 21.554 53.463 47.826 1.00 16.69 ? 456  GLU A HG2    1 
ATOM   4666 H HG3    . GLU A 1 273 ? 20.966 54.470 48.906 1.00 16.69 ? 456  GLU A HG3    1 
ATOM   4667 N N      . LYS A 1 274 ? 21.851 51.328 52.434 1.00 11.81 ? 457  LYS A N      1 
ATOM   4668 C CA     . LYS A 1 274 ? 22.282 50.232 53.292 1.00 12.47 ? 457  LYS A CA     1 
ATOM   4669 C C      . LYS A 1 274 ? 21.177 49.187 53.415 1.00 12.21 ? 457  LYS A C      1 
ATOM   4670 O O      . LYS A 1 274 ? 21.446 47.977 53.455 1.00 12.55 ? 457  LYS A O      1 
ATOM   4671 C CB     . LYS A 1 274 ? 22.687 50.761 54.673 1.00 13.87 ? 457  LYS A CB     1 
ATOM   4672 C CG     . LYS A 1 274 ? 23.957 51.575 54.660 1.00 15.17 ? 457  LYS A CG     1 
ATOM   4673 C CD     . LYS A 1 274 ? 24.277 52.180 56.049 1.00 19.66 ? 457  LYS A CD     1 
ATOM   4674 C CE     . LYS A 1 274 ? 25.545 52.958 56.013 1.00 23.96 ? 457  LYS A CE     1 
ATOM   4675 N NZ     . LYS A 1 274 ? 25.791 53.673 57.315 1.00 27.40 ? 457  LYS A NZ     1 
ATOM   4676 H H      . LYS A 1 274 ? 21.769 52.089 52.826 1.00 14.17 ? 457  LYS A H      1 
ATOM   4677 H HA     . LYS A 1 274 ? 23.065 49.811 52.902 1.00 14.97 ? 457  LYS A HA     1 
ATOM   4678 H HB2    . LYS A 1 274 ? 21.975 51.326 55.012 1.00 16.64 ? 457  LYS A HB2    1 
ATOM   4679 H HB3    . LYS A 1 274 ? 22.824 50.007 55.268 1.00 16.64 ? 457  LYS A HB3    1 
ATOM   4680 H HG2    . LYS A 1 274 ? 24.698 51.006 54.400 1.00 18.20 ? 457  LYS A HG2    1 
ATOM   4681 H HG3    . LYS A 1 274 ? 23.862 52.305 54.028 1.00 18.20 ? 457  LYS A HG3    1 
ATOM   4682 H HD2    . LYS A 1 274 ? 23.559 52.775 56.316 1.00 23.60 ? 457  LYS A HD2    1 
ATOM   4683 H HD3    . LYS A 1 274 ? 24.374 51.465 56.698 1.00 23.60 ? 457  LYS A HD3    1 
ATOM   4684 H HE2    . LYS A 1 274 ? 26.287 52.355 55.851 1.00 28.75 ? 457  LYS A HE2    1 
ATOM   4685 H HE3    . LYS A 1 274 ? 25.495 53.620 55.306 1.00 28.75 ? 457  LYS A HE3    1 
ATOM   4686 H HZ1    . LYS A 1 274 ? 26.577 54.090 57.290 1.00 32.88 ? 457  LYS A HZ1    1 
ATOM   4687 H HZ2    . LYS A 1 274 ? 25.150 54.274 57.459 1.00 32.88 ? 457  LYS A HZ2    1 
ATOM   4688 H HZ3    . LYS A 1 274 ? 25.795 53.090 57.987 1.00 32.88 ? 457  LYS A HZ3    1 
ATOM   4689 N N      . THR A 1 275 ? 19.937 49.635 53.521 1.00 12.81 ? 458  THR A N      1 
ATOM   4690 C CA     . THR A 1 275 ? 18.810 48.707 53.559 1.00 13.31 ? 458  THR A CA     1 
ATOM   4691 C C      . THR A 1 275 ? 18.728 47.899 52.263 1.00 12.10 ? 458  THR A C      1 
ATOM   4692 O O      . THR A 1 275 ? 18.553 46.667 52.284 1.00 12.26 ? 458  THR A O      1 
ATOM   4693 C CB     . THR A 1 275 ? 17.532 49.502 53.856 1.00 15.16 ? 458  THR A CB     1 
ATOM   4694 O OG1    . THR A 1 275 ? 17.586 50.060 55.176 1.00 17.77 ? 458  THR A OG1    1 
ATOM   4695 C CG2    . THR A 1 275 ? 16.321 48.616 53.774 1.00 16.75 ? 458  THR A CG2    1 
ATOM   4696 H H      . THR A 1 275 ? 19.716 50.465 53.573 1.00 15.37 ? 458  THR A H      1 
ATOM   4697 H HA     . THR A 1 275 ? 18.917 48.058 54.273 1.00 15.98 ? 458  THR A HA     1 
ATOM   4698 H HB     . THR A 1 275 ? 17.455 50.212 53.199 1.00 18.19 ? 458  THR A HB     1 
ATOM   4699 H HG1    . THR A 1 275 ? 18.252 50.567 55.246 1.00 21.33 ? 458  THR A HG1    1 
ATOM   4700 H HG21   . THR A 1 275 ? 15.521 49.128 53.974 1.00 20.10 ? 458  THR A HG21   1 
ATOM   4701 H HG22   . THR A 1 275 ? 16.241 48.245 52.882 1.00 20.10 ? 458  THR A HG22   1 
ATOM   4702 H HG23   . THR A 1 275 ? 16.397 47.890 54.412 1.00 20.10 ? 458  THR A HG23   1 
ATOM   4703 N N      . ILE A 1 276 ? 18.896 48.563 51.117 1.00 11.93 ? 459  ILE A N      1 
ATOM   4704 C CA     . ILE A 1 276 ? 18.910 47.843 49.845 1.00 11.47 ? 459  ILE A CA     1 
ATOM   4705 C C      . ILE A 1 276 ? 20.006 46.783 49.825 1.00 10.56 ? 459  ILE A C      1 
ATOM   4706 O O      . ILE A 1 276 ? 19.793 45.634 49.371 1.00 11.11 ? 459  ILE A O      1 
ATOM   4707 C CB     . ILE A 1 276 ? 19.070 48.829 48.678 1.00 12.32 ? 459  ILE A CB     1 
ATOM   4708 C CG1    . ILE A 1 276 ? 17.760 49.600 48.480 1.00 13.03 ? 459  ILE A CG1    1 
ATOM   4709 C CG2    . ILE A 1 276 ? 19.499 48.155 47.413 1.00 13.70 ? 459  ILE A CG2    1 
ATOM   4710 C CD1    . ILE A 1 276 ? 17.866 50.799 47.558 1.00 15.05 ? 459  ILE A CD1    1 
ATOM   4711 H H      . ILE A 1 276 ? 19.002 49.413 51.050 1.00 14.31 ? 459  ILE A H      1 
ATOM   4712 H HA     . ILE A 1 276 ? 18.059 47.386 49.750 1.00 13.76 ? 459  ILE A HA     1 
ATOM   4713 H HB     . ILE A 1 276 ? 19.779 49.449 48.908 1.00 14.79 ? 459  ILE A HB     1 
ATOM   4714 H HG12   . ILE A 1 276 ? 17.101 48.997 48.101 1.00 15.63 ? 459  ILE A HG12   1 
ATOM   4715 H HG13   . ILE A 1 276 ? 17.457 49.921 49.344 1.00 15.63 ? 459  ILE A HG13   1 
ATOM   4716 H HG21   . ILE A 1 276 ? 19.564 48.818 46.708 1.00 16.44 ? 459  ILE A HG21   1 
ATOM   4717 H HG22   . ILE A 1 276 ? 20.364 47.738 47.554 1.00 16.44 ? 459  ILE A HG22   1 
ATOM   4718 H HG23   . ILE A 1 276 ? 18.842 47.482 47.175 1.00 16.44 ? 459  ILE A HG23   1 
ATOM   4719 H HD11   . ILE A 1 276 ? 17.002 51.236 47.507 1.00 18.06 ? 459  ILE A HD11   1 
ATOM   4720 H HD12   . ILE A 1 276 ? 18.527 51.413 47.915 1.00 18.06 ? 459  ILE A HD12   1 
ATOM   4721 H HD13   . ILE A 1 276 ? 18.137 50.496 46.677 1.00 18.06 ? 459  ILE A HD13   1 
ATOM   4722 N N      . ALA A 1 277 ? 21.216 47.158 50.285 1.00 10.36 ? 460  ALA A N      1 
ATOM   4723 C CA     . ALA A 1 277 ? 22.326 46.200 50.303 1.00 10.63 ? 460  ALA A CA     1 
ATOM   4724 C C      . ALA A 1 277 ? 21.992 44.951 51.112 1.00 11.40 ? 460  ALA A C      1 
ATOM   4725 O O      . ALA A 1 277 ? 22.284 43.840 50.673 1.00 11.35 ? 460  ALA A O      1 
ATOM   4726 C CB     . ALA A 1 277 ? 23.582 46.891 50.834 1.00 11.68 ? 460  ALA A CB     1 
ATOM   4727 H H      . ALA A 1 277 ? 21.410 47.941 50.584 1.00 12.43 ? 460  ALA A H      1 
ATOM   4728 H HA     . ALA A 1 277 ? 22.501 45.905 49.396 1.00 12.76 ? 460  ALA A HA     1 
ATOM   4729 H HB1    . ALA A 1 277 ? 24.297 46.239 50.901 1.00 14.01 ? 460  ALA A HB1    1 
ATOM   4730 H HB2    . ALA A 1 277 ? 23.837 47.598 50.220 1.00 14.01 ? 460  ALA A HB2    1 
ATOM   4731 H HB3    . ALA A 1 277 ? 23.391 47.265 51.708 1.00 14.01 ? 460  ALA A HB3    1 
ATOM   4732 N N      . GLY A 1 278 ? 21.427 45.119 52.304 1.00 12.45 ? 461  GLY A N      1 
ATOM   4733 C CA     . GLY A 1 278 ? 21.027 43.983 53.108 1.00 12.63 ? 461  GLY A CA     1 
ATOM   4734 C C      . GLY A 1 278 ? 20.001 43.119 52.404 1.00 12.04 ? 461  GLY A C      1 
ATOM   4735 O O      . GLY A 1 278 ? 20.048 41.877 52.488 1.00 12.74 ? 461  GLY A O      1 
ATOM   4736 H H      . GLY A 1 278 ? 21.266 45.882 52.667 1.00 14.94 ? 461  GLY A H      1 
ATOM   4737 H HA2    . GLY A 1 278 ? 21.805 43.437 53.303 1.00 15.15 ? 461  GLY A HA2    1 
ATOM   4738 H HA3    . GLY A 1 278 ? 20.644 44.297 53.942 1.00 15.15 ? 461  GLY A HA3    1 
ATOM   4739 N N      . LYS A 1 279 ? 19.043 43.763 51.726 1.00 11.93 ? 462  LYS A N      1 
ATOM   4740 C CA     . LYS A 1 279 ? 18.024 43.027 50.966 1.00 11.92 ? 462  LYS A CA     1 
ATOM   4741 C C      . LYS A 1 279 ? 18.638 42.219 49.830 1.00 12.16 ? 462  LYS A C      1 
ATOM   4742 O O      . LYS A 1 279 ? 18.202 41.106 49.573 1.00 12.12 ? 462  LYS A O      1 
ATOM   4743 C CB     . LYS A 1 279 ? 16.955 43.993 50.445 1.00 12.61 ? 462  LYS A CB     1 
ATOM   4744 C CG     . LYS A 1 279 ? 15.989 44.560 51.408 1.00 15.68 ? 462  LYS A CG     1 
ATOM   4745 C CD     . LYS A 1 279 ? 15.032 45.494 50.611 1.00 18.17 ? 462  LYS A CD     1 
ATOM   4746 C CE     . LYS A 1 279 ? 13.814 45.934 51.330 1.00 22.70 ? 462  LYS A CE     1 
ATOM   4747 N NZ     . LYS A 1 279 ? 13.125 47.019 50.520 1.00 25.62 ? 462  LYS A NZ     1 
ATOM   4748 H H      . LYS A 1 279 ? 18.961 44.618 51.690 1.00 14.32 ? 462  LYS A H      1 
ATOM   4749 H HA     . LYS A 1 279 ? 17.588 42.397 51.562 1.00 14.30 ? 462  LYS A HA     1 
ATOM   4750 H HB2    . LYS A 1 279 ? 17.413 44.746 50.039 1.00 15.14 ? 462  LYS A HB2    1 
ATOM   4751 H HB3    . LYS A 1 279 ? 16.433 43.522 49.777 1.00 15.14 ? 462  LYS A HB3    1 
ATOM   4752 H HG2    . LYS A 1 279 ? 15.474 43.852 51.825 1.00 18.82 ? 462  LYS A HG2    1 
ATOM   4753 H HG3    . LYS A 1 279 ? 16.452 45.077 52.086 1.00 18.82 ? 462  LYS A HG3    1 
ATOM   4754 H HD2    . LYS A 1 279 ? 15.522 46.294 50.363 1.00 21.81 ? 462  LYS A HD2    1 
ATOM   4755 H HD3    . LYS A 1 279 ? 14.740 45.024 49.814 1.00 21.81 ? 462  LYS A HD3    1 
ATOM   4756 H HE2    . LYS A 1 279 ? 13.206 45.186 51.438 1.00 27.25 ? 462  LYS A HE2    1 
ATOM   4757 H HE3    . LYS A 1 279 ? 14.055 46.293 52.199 1.00 27.25 ? 462  LYS A HE3    1 
ATOM   4758 H HZ1    . LYS A 1 279 ? 12.387 47.289 50.938 1.00 30.75 ? 462  LYS A HZ1    1 
ATOM   4759 H HZ2    . LYS A 1 279 ? 13.670 47.715 50.417 1.00 30.75 ? 462  LYS A HZ2    1 
ATOM   4760 H HZ3    . LYS A 1 279 ? 12.903 46.705 49.717 1.00 30.75 ? 462  LYS A HZ3    1 
ATOM   4761 N N      . VAL A 1 280 ? 19.640 42.746 49.121 1.00 11.07 ? 463  VAL A N      1 
ATOM   4762 C CA     . VAL A 1 280 ? 20.284 42.016 48.031 1.00 10.70 ? 463  VAL A CA     1 
ATOM   4763 C C      . VAL A 1 280 ? 20.967 40.775 48.573 1.00 10.52 ? 463  VAL A C      1 
ATOM   4764 O O      . VAL A 1 280 ? 20.790 39.670 48.064 1.00 10.51 ? 463  VAL A O      1 
ATOM   4765 C CB     . VAL A 1 280 ? 21.278 42.914 47.273 1.00 11.28 ? 463  VAL A CB     1 
ATOM   4766 C CG1    . VAL A 1 280 ? 22.081 42.090 46.322 1.00 11.03 ? 463  VAL A CG1    1 
ATOM   4767 C CG2    . VAL A 1 280 ? 20.535 44.059 46.522 1.00 11.67 ? 463  VAL A CG2    1 
ATOM   4768 H H      . VAL A 1 280 ? 19.967 43.530 49.252 1.00 13.28 ? 463  VAL A H      1 
ATOM   4769 H HA     . VAL A 1 280 ? 19.598 41.743 47.402 1.00 12.83 ? 463  VAL A HA     1 
ATOM   4770 H HB     . VAL A 1 280 ? 21.880 43.327 47.912 1.00 13.54 ? 463  VAL A HB     1 
ATOM   4771 H HG11   . VAL A 1 280 ? 22.598 42.680 45.752 1.00 13.24 ? 463  VAL A HG11   1 
ATOM   4772 H HG12   . VAL A 1 280 ? 22.675 41.514 46.828 1.00 13.24 ? 463  VAL A HG12   1 
ATOM   4773 H HG13   . VAL A 1 280 ? 21.479 41.553 45.783 1.00 13.24 ? 463  VAL A HG13   1 
ATOM   4774 H HG21   . VAL A 1 280 ? 21.186 44.594 46.040 1.00 14.01 ? 463  VAL A HG21   1 
ATOM   4775 H HG22   . VAL A 1 280 ? 19.901 43.670 45.900 1.00 14.01 ? 463  VAL A HG22   1 
ATOM   4776 H HG23   . VAL A 1 280 ? 20.068 44.610 47.169 1.00 14.01 ? 463  VAL A HG23   1 
ATOM   4777 N N      . SER A 1 281 ? 21.710 40.931 49.670 1.00 10.09 ? 464  SER A N      1 
ATOM   4778 C CA     . SER A 1 281 ? 22.393 39.798 50.273 1.00 10.38 ? 464  SER A CA     1 
ATOM   4779 C C      . SER A 1 281 ? 21.395 38.717 50.667 1.00 11.21 ? 464  SER A C      1 
ATOM   4780 O O      . SER A 1 281 ? 21.600 37.521 50.391 1.00 11.70 ? 464  SER A O      1 
ATOM   4781 C CB     . SER A 1 281 ? 23.206 40.278 51.474 1.00 11.31 ? 464  SER A CB     1 
ATOM   4782 O OG     . SER A 1 281 ? 23.814 39.188 52.157 1.00 12.04 ? 464  SER A OG     1 
ATOM   4783 H H      . SER A 1 281 ? 21.830 41.678 50.079 1.00 12.11 ? 464  SER A H      1 
ATOM   4784 H HA     . SER A 1 281 ? 23.011 39.407 49.635 1.00 12.45 ? 464  SER A HA     1 
ATOM   4785 H HB2    . SER A 1 281 ? 23.900 40.880 51.163 1.00 13.58 ? 464  SER A HB2    1 
ATOM   4786 H HB3    . SER A 1 281 ? 22.615 40.743 52.087 1.00 13.58 ? 464  SER A HB3    1 
ATOM   4787 H HG     . SER A 1 281 ? 24.297 38.750 51.627 1.00 14.45 ? 464  SER A HG     1 
ATOM   4788 N N      . LYS A 1 282 ? 20.305 39.119 51.327 1.00 11.42 ? 465  LYS A N      1 
ATOM   4789 C CA     . LYS A 1 282 ? 19.268 38.188 51.755 1.00 11.66 ? 465  LYS A CA     1 
ATOM   4790 C C      . LYS A 1 282 ? 18.567 37.540 50.573 1.00 10.52 ? 465  LYS A C      1 
ATOM   4791 O O      . LYS A 1 282 ? 18.328 36.316 50.553 1.00 12.50 ? 465  LYS A O      1 
ATOM   4792 C CB     . LYS A 1 282 ? 18.254 38.943 52.599 1.00 13.61 ? 465  LYS A CB     1 
ATOM   4793 C CG     . LYS A 1 282 ? 17.156 38.067 53.149 1.00 17.65 ? 465  LYS A CG     1 
ATOM   4794 C CD     . LYS A 1 282 ? 16.272 38.844 54.118 1.00 23.89 ? 465  LYS A CD     1 
ATOM   4795 C CE     . LYS A 1 282 ? 15.215 37.941 54.735 1.00 31.71 ? 465  LYS A CE     1 
ATOM   4796 N NZ     . LYS A 1 282 ? 14.488 38.609 55.840 1.00 37.19 ? 465  LYS A NZ     1 
ATOM   4797 H H      . LYS A 1 282 ? 20.143 39.937 51.541 1.00 13.70 ? 465  LYS A H      1 
ATOM   4798 H HA     . LYS A 1 282 ? 19.677 37.483 52.279 1.00 13.99 ? 465  LYS A HA     1 
ATOM   4799 H HB2    . LYS A 1 282 ? 18.713 39.350 53.350 1.00 16.33 ? 465  LYS A HB2    1 
ATOM   4800 H HB3    . LYS A 1 282 ? 17.840 39.629 52.053 1.00 16.33 ? 465  LYS A HB3    1 
ATOM   4801 H HG2    . LYS A 1 282 ? 16.604 37.745 52.420 1.00 21.19 ? 465  LYS A HG2    1 
ATOM   4802 H HG3    . LYS A 1 282 ? 17.549 37.318 53.624 1.00 21.19 ? 465  LYS A HG3    1 
ATOM   4803 H HD2    . LYS A 1 282 ? 16.818 39.209 54.832 1.00 28.67 ? 465  LYS A HD2    1 
ATOM   4804 H HD3    . LYS A 1 282 ? 15.824 39.561 53.643 1.00 28.67 ? 465  LYS A HD3    1 
ATOM   4805 H HE2    . LYS A 1 282 ? 14.569 37.694 54.054 1.00 38.05 ? 465  LYS A HE2    1 
ATOM   4806 H HE3    . LYS A 1 282 ? 15.642 37.147 55.091 1.00 38.05 ? 465  LYS A HE3    1 
ATOM   4807 H HZ1    . LYS A 1 282 ? 13.880 38.057 56.183 1.00 44.63 ? 465  LYS A HZ1    1 
ATOM   4808 H HZ2    . LYS A 1 282 ? 15.058 38.845 56.481 1.00 44.63 ? 465  LYS A HZ2    1 
ATOM   4809 H HZ3    . LYS A 1 282 ? 14.076 39.338 55.537 1.00 44.63 ? 465  LYS A HZ3    1 
ATOM   4810 N N      . ALA A 1 283 ? 18.175 38.349 49.605 1.00 10.36 ? 466  ALA A N      1 
ATOM   4811 C CA     . ALA A 1 283 ? 17.378 37.860 48.478 1.00 11.08 ? 466  ALA A CA     1 
ATOM   4812 C C      . ALA A 1 283 ? 18.094 36.759 47.720 1.00 10.14 ? 466  ALA A C      1 
ATOM   4813 O O      . ALA A 1 283 ? 17.451 35.823 47.225 1.00 10.73 ? 466  ALA A O      1 
ATOM   4814 C CB     . ALA A 1 283 ? 17.095 39.031 47.550 1.00 10.94 ? 466  ALA A CB     1 
ATOM   4815 H H      . ALA A 1 283 ? 18.353 39.190 49.570 1.00 12.44 ? 466  ALA A H      1 
ATOM   4816 H HA     . ALA A 1 283 ? 16.543 37.492 48.808 1.00 13.29 ? 466  ALA A HA     1 
ATOM   4817 H HB1    . ALA A 1 283 ? 16.481 38.743 46.856 1.00 13.13 ? 466  ALA A HB1    1 
ATOM   4818 H HB2    . ALA A 1 283 ? 16.699 39.752 48.063 1.00 13.13 ? 466  ALA A HB2    1 
ATOM   4819 H HB3    . ALA A 1 283 ? 17.928 39.327 47.151 1.00 13.13 ? 466  ALA A HB3    1 
ATOM   4820 N N      . PHE A 1 284 ? 19.414 36.880 47.547 1.00 9.46  ? 467  PHE A N      1 
ATOM   4821 C CA     . PHE A 1 284 ? 20.223 35.927 46.789 1.00 9.74  ? 467  PHE A CA     1 
ATOM   4822 C C      . PHE A 1 284 ? 20.905 34.904 47.696 1.00 9.82  ? 467  PHE A C      1 
ATOM   4823 O O      . PHE A 1 284 ? 21.575 33.983 47.212 1.00 10.76 ? 467  PHE A O      1 
ATOM   4824 C CB     . PHE A 1 284 ? 21.257 36.627 45.879 1.00 10.25 ? 467  PHE A CB     1 
ATOM   4825 C CG     . PHE A 1 284 ? 20.618 37.359 44.751 1.00 10.27 ? 467  PHE A CG     1 
ATOM   4826 C CD1    . PHE A 1 284 ? 20.043 38.605 44.939 1.00 9.97  ? 467  PHE A CD1    1 
ATOM   4827 C CD2    . PHE A 1 284 ? 20.514 36.772 43.534 1.00 12.81 ? 467  PHE A CD2    1 
ATOM   4828 C CE1    . PHE A 1 284 ? 19.376 39.248 43.928 1.00 11.05 ? 467  PHE A CE1    1 
ATOM   4829 C CE2    . PHE A 1 284 ? 19.855 37.431 42.469 1.00 13.02 ? 467  PHE A CE2    1 
ATOM   4830 C CZ     . PHE A 1 284 ? 19.278 38.656 42.682 1.00 12.03 ? 467  PHE A CZ     1 
ATOM   4831 H H      . PHE A 1 284 ? 19.877 37.528 47.871 1.00 11.35 ? 467  PHE A H      1 
ATOM   4832 H HA     . PHE A 1 284 ? 19.635 35.452 46.181 1.00 11.69 ? 467  PHE A HA     1 
ATOM   4833 H HB2    . PHE A 1 284 ? 21.762 37.266 46.406 1.00 12.29 ? 467  PHE A HB2    1 
ATOM   4834 H HB3    . PHE A 1 284 ? 21.854 35.960 45.506 1.00 12.29 ? 467  PHE A HB3    1 
ATOM   4835 H HD1    . PHE A 1 284 ? 20.111 39.016 45.771 1.00 11.96 ? 467  PHE A HD1    1 
ATOM   4836 H HD2    . PHE A 1 284 ? 20.880 35.928 43.397 1.00 15.38 ? 467  PHE A HD2    1 
ATOM   4837 H HE1    . PHE A 1 284 ? 18.991 40.081 44.080 1.00 13.26 ? 467  PHE A HE1    1 
ATOM   4838 H HE2    . PHE A 1 284 ? 19.814 37.034 41.629 1.00 15.62 ? 467  PHE A HE2    1 
ATOM   4839 H HZ     . PHE A 1 284 ? 18.823 39.086 41.994 1.00 14.44 ? 467  PHE A HZ     1 
ATOM   4840 N N      . SER A 1 285 ? 20.690 35.025 49.006 1.00 9.92  ? 468  SER A N      1 
ATOM   4841 C CA     . SER A 1 285 ? 21.385 34.183 49.990 1.00 11.23 ? 468  SER A CA     1 
ATOM   4842 C C      . SER A 1 285 ? 22.896 34.163 49.767 1.00 10.32 ? 468  SER A C      1 
ATOM   4843 O O      . SER A 1 285 ? 23.547 33.114 49.839 1.00 11.85 ? 468  SER A O      1 
ATOM   4844 C CB     . SER A 1 285 ? 20.833 32.749 50.022 1.00 12.52 ? 468  SER A CB     1 
ATOM   4845 O OG     . SER A 1 285 ? 19.483 32.750 50.488 1.00 14.25 ? 468  SER A OG     1 
ATOM   4846 H H      . SER A 1 285 ? 20.143 35.589 49.355 1.00 11.91 ? 468  SER A H      1 
ATOM   4847 H HA     . SER A 1 285 ? 21.221 34.585 50.857 1.00 13.48 ? 468  SER A HA     1 
ATOM   4848 H HB2    . SER A 1 285 ? 20.860 32.378 49.126 1.00 15.02 ? 468  SER A HB2    1 
ATOM   4849 H HB3    . SER A 1 285 ? 21.376 32.213 50.620 1.00 15.02 ? 468  SER A HB3    1 
ATOM   4850 H HG     . SER A 1 285 ? 19.189 31.964 50.519 1.00 17.10 ? 468  SER A HG     1 
ATOM   4851 N N      . GLN A 1 286 ? 23.437 35.340 49.518 1.00 9.35  ? 469  GLN A N      1 
ATOM   4852 C CA     . GLN A 1 286 ? 24.878 35.524 49.304 1.00 10.36 ? 469  GLN A CA     1 
ATOM   4853 C C      . GLN A 1 286 ? 25.398 36.437 50.399 1.00 10.33 ? 469  GLN A C      1 
ATOM   4854 O O      . GLN A 1 286 ? 25.232 37.655 50.310 1.00 11.12 ? 469  GLN A O      1 
ATOM   4855 C CB     . GLN A 1 286 ? 25.201 36.111 47.928 1.00 10.34 ? 469  GLN A CB     1 
ATOM   4856 C CG     . GLN A 1 286 ? 24.640 35.321 46.727 1.00 10.05 ? 469  GLN A CG     1 
ATOM   4857 C CD     . GLN A 1 286 ? 25.144 33.896 46.624 1.00 10.39 ? 469  GLN A CD     1 
ATOM   4858 O OE1    . GLN A 1 286 ? 26.333 33.640 46.471 1.00 11.70 ? 469  GLN A OE1    1 
ATOM   4859 N NE2    . GLN A 1 286 ? 24.223 32.944 46.640 1.00 11.13 ? 469  GLN A NE2    1 
ATOM   4860 H H      . GLN A 1 286 ? 22.986 36.071 49.466 1.00 11.22 ? 469  GLN A H      1 
ATOM   4861 H HA     . GLN A 1 286 ? 25.302 34.653 49.366 1.00 12.43 ? 469  GLN A HA     1 
ATOM   4862 H HB2    . GLN A 1 286 ? 24.832 37.007 47.884 1.00 12.41 ? 469  GLN A HB2    1 
ATOM   4863 H HB3    . GLN A 1 286 ? 26.166 36.144 47.829 1.00 12.41 ? 469  GLN A HB3    1 
ATOM   4864 H HG2    . GLN A 1 286 ? 23.674 35.285 46.804 1.00 12.06 ? 469  GLN A HG2    1 
ATOM   4865 H HG3    . GLN A 1 286 ? 24.891 35.781 45.910 1.00 12.06 ? 469  GLN A HG3    1 
ATOM   4866 H HE21   . GLN A 1 286 ? 23.391 33.152 46.707 1.00 13.36 ? 469  GLN A HE21   1 
ATOM   4867 H HE22   . GLN A 1 286 ? 24.457 32.118 46.584 1.00 13.36 ? 469  GLN A HE22   1 
ATOM   4868 N N      . MET A 1 287 ? 26.013 35.892 51.421 1.00 9.92  ? 470  MET A N      1 
ATOM   4869 C CA     . MET A 1 287 ? 26.511 36.748 52.491 1.00 11.09 ? 470  MET A CA     1 
ATOM   4870 C C      . MET A 1 287 ? 27.504 37.765 51.950 1.00 10.72 ? 470  MET A C      1 
ATOM   4871 O O      . MET A 1 287 ? 27.393 38.979 52.219 1.00 11.09 ? 470  MET A O      1 
ATOM   4872 C CB     . MET A 1 287 ? 27.184 35.892 53.578 1.00 13.02 ? 470  MET A CB     1 
ATOM   4873 C CG     . MET A 1 287 ? 27.681 36.716 54.743 1.00 15.27 ? 470  MET A CG     1 
ATOM   4874 S SD     . MET A 1 287 ? 28.402 35.665 56.025 1.00 18.07 ? 470  MET A SD     1 
ATOM   4875 C CE     . MET A 1 287 ? 28.723 36.928 57.227 1.00 22.66 ? 470  MET A CE     1 
ATOM   4876 H H      . MET A 1 287 ? 26.156 35.050 51.526 1.00 11.91 ? 470  MET A H      1 
ATOM   4877 H HA     . MET A 1 287 ? 25.758 37.211 52.889 1.00 13.31 ? 470  MET A HA     1 
ATOM   4878 H HB2    . MET A 1 287 ? 26.541 35.249 53.917 1.00 15.63 ? 470  MET A HB2    1 
ATOM   4879 H HB3    . MET A 1 287 ? 27.943 35.429 53.191 1.00 15.63 ? 470  MET A HB3    1 
ATOM   4880 H HG2    . MET A 1 287 ? 28.363 37.333 54.433 1.00 18.33 ? 470  MET A HG2    1 
ATOM   4881 H HG3    . MET A 1 287 ? 26.940 37.207 55.130 1.00 18.33 ? 470  MET A HG3    1 
ATOM   4882 H HE1    . MET A 1 287 ? 29.146 36.527 58.002 1.00 27.19 ? 470  MET A HE1    1 
ATOM   4883 H HE2    . MET A 1 287 ? 29.311 37.593 56.837 1.00 27.19 ? 470  MET A HE2    1 
ATOM   4884 H HE3    . MET A 1 287 ? 27.883 37.339 57.485 1.00 27.19 ? 470  MET A HE3    1 
ATOM   4885 N N      . ILE A 1 288 ? 28.487 37.297 51.200 1.00 10.62 ? 471  ILE A N      1 
ATOM   4886 C CA     . ILE A 1 288 ? 29.477 38.154 50.558 1.00 10.49 ? 471  ILE A CA     1 
ATOM   4887 C C      . ILE A 1 288 ? 29.012 38.369 49.141 1.00 10.70 ? 471  ILE A C      1 
ATOM   4888 O O      . ILE A 1 288 ? 28.915 37.417 48.371 1.00 12.07 ? 471  ILE A O      1 
ATOM   4889 C CB     . ILE A 1 288 ? 30.872 37.531 50.671 1.00 12.04 ? 471  ILE A CB     1 
ATOM   4890 C CG1    . ILE A 1 288 ? 31.283 37.400 52.210 1.00 14.40 ? 471  ILE A CG1    1 
ATOM   4891 C CG2    . ILE A 1 288 ? 31.880 38.364 49.936 1.00 13.00 ? 471  ILE A CG2    1 
ATOM   4892 C CD1    . ILE A 1 288 ? 32.620 36.815 52.560 1.00 17.04 ? 471  ILE A CD1    1 
ATOM   4893 H H      . ILE A 1 288 ? 28.608 36.460 51.041 1.00 12.75 ? 471  ILE A H      1 
ATOM   4894 H HA     . ILE A 1 288 ? 29.520 39.030 50.972 1.00 12.59 ? 471  ILE A HA     1 
ATOM   4895 H HB     . ILE A 1 288 ? 30.851 36.648 50.270 1.00 14.45 ? 471  ILE A HB     1 
ATOM   4896 H HG12   . ILE A 1 288 ? 31.266 38.292 52.592 1.00 17.28 ? 471  ILE A HG12   1 
ATOM   4897 H HG13   . ILE A 1 288 ? 30.618 36.842 52.642 1.00 17.28 ? 471  ILE A HG13   1 
ATOM   4898 H HG21   . ILE A 1 288 ? 32.730 37.897 49.929 1.00 15.60 ? 471  ILE A HG21   1 
ATOM   4899 H HG22   . ILE A 1 288 ? 31.572 38.503 49.027 1.00 15.60 ? 471  ILE A HG22   1 
ATOM   4900 H HG23   . ILE A 1 288 ? 31.975 39.217 50.388 1.00 15.60 ? 471  ILE A HG23   1 
ATOM   4901 H HD11   . ILE A 1 288 ? 32.703 36.772 53.525 1.00 20.45 ? 471  ILE A HD11   1 
ATOM   4902 H HD12   . ILE A 1 288 ? 32.683 35.923 52.182 1.00 20.45 ? 471  ILE A HD12   1 
ATOM   4903 H HD13   . ILE A 1 288 ? 33.318 37.380 52.192 1.00 20.45 ? 471  ILE A HD13   1 
ATOM   4904 N N      . CYS A 1 289 ? 28.653 39.600 48.783 1.00 10.61 ? 472  CYS A N      1 
ATOM   4905 C CA     . CYS A 1 289 ? 27.975 39.812 47.517 1.00 11.51 ? 472  CYS A CA     1 
ATOM   4906 C C      . CYS A 1 289 ? 28.298 41.193 46.965 1.00 11.48 ? 472  CYS A C      1 
ATOM   4907 O O      . CYS A 1 289 ? 28.209 42.185 47.689 1.00 14.20 ? 472  CYS A O      1 
ATOM   4908 C CB     . CYS A 1 289 ? 26.452 39.716 47.703 1.00 12.45 ? 472  CYS A CB     1 
ATOM   4909 S SG     . CYS A 1 289 ? 25.522 39.486 46.162 1.00 12.81 ? 472  CYS A SG     1 
ATOM   4910 H H      . CYS A 1 289 ? 28.789 40.309 49.249 1.00 12.73 ? 472  CYS A H      1 
ATOM   4911 H HA     . CYS A 1 289 ? 28.290 39.146 46.887 1.00 13.82 ? 472  CYS A HA     1 
ATOM   4912 H HB2    . CYS A 1 289 ? 26.258 38.960 48.279 1.00 14.94 ? 472  CYS A HB2    1 
ATOM   4913 H HB3    . CYS A 1 289 ? 26.138 40.536 48.115 1.00 14.94 ? 472  CYS A HB3    1 
ATOM   4914 H HG     . CYS A 1 289 ? 24.349 39.451 46.416 1.00 15.37 ? 472  CYS A HG     1 
ATOM   4915 N N      . GLY A 1 290 ? 28.632 41.247 45.701 1.00 10.46 ? 473  GLY A N      1 
ATOM   4916 C CA     . GLY A 1 290 ? 28.749 42.500 44.971 1.00 10.46 ? 473  GLY A CA     1 
ATOM   4917 C C      . GLY A 1 290 ? 27.505 42.776 44.155 1.00 9.90  ? 473  GLY A C      1 
ATOM   4918 O O      . GLY A 1 290 ? 26.860 41.847 43.644 1.00 11.05 ? 473  GLY A O      1 
ATOM   4919 H H      . GLY A 1 290 ? 28.804 40.554 45.221 1.00 12.55 ? 473  GLY A H      1 
ATOM   4920 H HA2    . GLY A 1 290 ? 28.878 43.230 45.597 1.00 12.56 ? 473  GLY A HA2    1 
ATOM   4921 H HA3    . GLY A 1 290 ? 29.510 42.458 44.372 1.00 12.56 ? 473  GLY A HA3    1 
ATOM   4922 N N      . PHE A 1 291 ? 27.148 44.046 44.005 1.00 9.55  ? 474  PHE A N      1 
ATOM   4923 C CA     . PHE A 1 291 ? 26.037 44.436 43.155 1.00 9.55  ? 474  PHE A CA     1 
ATOM   4924 C C      . PHE A 1 291 ? 26.268 45.862 42.712 1.00 9.51  ? 474  PHE A C      1 
ATOM   4925 O O      . PHE A 1 291 ? 27.101 46.596 43.278 1.00 10.33 ? 474  PHE A O      1 
ATOM   4926 C CB     . PHE A 1 291 ? 24.660 44.250 43.813 1.00 11.53 ? 474  PHE A CB     1 
ATOM   4927 C CG     . PHE A 1 291 ? 24.363 45.174 44.955 1.00 10.59 ? 474  PHE A CG     1 
ATOM   4928 C CD1    . PHE A 1 291 ? 24.725 44.827 46.240 1.00 10.52 ? 474  PHE A CD1    1 
ATOM   4929 C CD2    . PHE A 1 291 ? 23.670 46.366 44.754 1.00 11.32 ? 474  PHE A CD2    1 
ATOM   4930 C CE1    . PHE A 1 291 ? 24.458 45.678 47.304 1.00 11.58 ? 474  PHE A CE1    1 
ATOM   4931 C CE2    . PHE A 1 291 ? 23.379 47.200 45.797 1.00 11.71 ? 474  PHE A CE2    1 
ATOM   4932 C CZ     . PHE A 1 291 ? 23.749 46.861 47.085 1.00 11.68 ? 474  PHE A CZ     1 
ATOM   4933 H H      . PHE A 1 291 ? 27.540 44.707 44.391 1.00 11.46 ? 474  PHE A H      1 
ATOM   4934 H HA     . PHE A 1 291 ? 26.026 43.866 42.370 1.00 11.46 ? 474  PHE A HA     1 
ATOM   4935 H HB2    . PHE A 1 291 ? 23.978 44.394 43.140 1.00 13.84 ? 474  PHE A HB2    1 
ATOM   4936 H HB3    . PHE A 1 291 ? 24.605 43.343 44.154 1.00 13.84 ? 474  PHE A HB3    1 
ATOM   4937 H HD1    . PHE A 1 291 ? 25.153 44.016 46.395 1.00 12.62 ? 474  PHE A HD1    1 
ATOM   4938 H HD2    . PHE A 1 291 ? 23.402 46.599 43.895 1.00 13.59 ? 474  PHE A HD2    1 
ATOM   4939 H HE1    . PHE A 1 291 ? 24.751 45.461 48.160 1.00 13.89 ? 474  PHE A HE1    1 
ATOM   4940 H HE2    . PHE A 1 291 ? 22.930 47.999 45.639 1.00 14.05 ? 474  PHE A HE2    1 
ATOM   4941 H HZ     . PHE A 1 291 ? 23.527 47.415 47.798 1.00 14.02 ? 474  PHE A HZ     1 
ATOM   4942 N N      . ASP A 1 292 ? 25.585 46.250 41.656 1.00 10.65 ? 475  ASP A N      1 
ATOM   4943 C CA     . ASP A 1 292 ? 25.694 47.585 41.121 1.00 11.80 ? 475  ASP A CA     1 
ATOM   4944 C C      . ASP A 1 292 ? 24.409 48.344 41.301 1.00 10.11 ? 475  ASP A C      1 
ATOM   4945 O O      . ASP A 1 292 ? 23.322 47.827 41.014 1.00 10.63 ? 475  ASP A O      1 
ATOM   4946 C CB     . ASP A 1 292 ? 26.027 47.564 39.644 1.00 16.38 ? 475  ASP A CB     1 
ATOM   4947 C CG     . ASP A 1 292 ? 27.477 47.128 39.398 1.00 25.01 ? 475  ASP A CG     1 
ATOM   4948 O OD1    . ASP A 1 292 ? 28.420 47.961 39.483 1.00 29.65 ? 475  ASP A OD1    1 
ATOM   4949 O OD2    . ASP A 1 292 ? 27.664 45.961 39.128 1.00 27.08 ? 475  ASP A OD2    1 
ATOM   4950 H H      . ASP A 1 292 ? 25.040 45.745 41.223 1.00 12.77 ? 475  ASP A H      1 
ATOM   4951 H HA     . ASP A 1 292 ? 26.399 48.043 41.605 1.00 14.16 ? 475  ASP A HA     1 
ATOM   4952 H HB2    . ASP A 1 292 ? 25.440 46.938 39.192 1.00 19.66 ? 475  ASP A HB2    1 
ATOM   4953 H HB3    . ASP A 1 292 ? 25.909 48.454 39.276 1.00 19.66 ? 475  ASP A HB3    1 
ATOM   4954 N N      . LEU A 1 293 ? 24.550 49.583 41.701 1.00 11.07 ? 476  LEU A N      1 
ATOM   4955 C CA     . LEU A 1 293 ? 23.432 50.450 41.988 1.00 13.06 ? 476  LEU A CA     1 
ATOM   4956 C C      . LEU A 1 293 ? 23.613 51.764 41.259 1.00 12.01 ? 476  LEU A C      1 
ATOM   4957 O O      . LEU A 1 293 ? 24.739 52.268 41.096 1.00 13.79 ? 476  LEU A O      1 
ATOM   4958 C CB     . LEU A 1 293 ? 23.420 50.645 43.513 1.00 19.02 ? 476  LEU A CB     1 
ATOM   4959 C CG     . LEU A 1 293 ? 22.422 51.580 44.166 1.00 23.17 ? 476  LEU A CG     1 
ATOM   4960 C CD1    . LEU A 1 293 ? 22.015 51.157 45.536 1.00 26.84 ? 476  LEU A CD1    1 
ATOM   4961 C CD2    . LEU A 1 293 ? 23.047 53.001 44.128 1.00 21.54 ? 476  LEU A CD2    1 
ATOM   4962 H H      . LEU A 1 293 ? 25.313 49.962 41.820 1.00 13.28 ? 476  LEU A H      1 
ATOM   4963 H HA     . LEU A 1 293 ? 22.581 50.099 41.683 1.00 15.67 ? 476  LEU A HA     1 
ATOM   4964 H HB2    . LEU A 1 293 ? 23.266 49.773 43.909 1.00 22.83 ? 476  LEU A HB2    1 
ATOM   4965 H HB3    . LEU A 1 293 ? 24.297 50.974 43.764 1.00 22.83 ? 476  LEU A HB3    1 
ATOM   4966 H HG     . LEU A 1 293 ? 21.582 51.573 43.681 1.00 27.81 ? 476  LEU A HG     1 
ATOM   4967 H HD11   . LEU A 1 293 ? 21.393 51.808 45.897 1.00 32.21 ? 476  LEU A HD11   1 
ATOM   4968 H HD12   . LEU A 1 293 ? 21.589 50.287 45.484 1.00 32.21 ? 476  LEU A HD12   1 
ATOM   4969 H HD13   . LEU A 1 293 ? 22.803 51.106 46.099 1.00 32.21 ? 476  LEU A HD13   1 
ATOM   4970 H HD21   . LEU A 1 293 ? 22.676 53.529 44.853 1.00 25.85 ? 476  LEU A HD21   1 
ATOM   4971 H HD22   . LEU A 1 293 ? 24.008 52.926 44.233 1.00 25.85 ? 476  LEU A HD22   1 
ATOM   4972 H HD23   . LEU A 1 293 ? 22.838 53.415 43.276 1.00 25.85 ? 476  LEU A HD23   1 
ATOM   4973 N N      . LEU A 1 294 ? 22.501 52.323 40.828 1.00 11.90 ? 477  LEU A N      1 
ATOM   4974 C CA     . LEU A 1 294 ? 22.467 53.624 40.181 1.00 12.51 ? 477  LEU A CA     1 
ATOM   4975 C C      . LEU A 1 294 ? 21.754 54.632 41.064 1.00 13.55 ? 477  LEU A C      1 
ATOM   4976 O O      . LEU A 1 294 ? 20.643 54.376 41.548 1.00 15.45 ? 477  LEU A O      1 
ATOM   4977 C CB     . LEU A 1 294 ? 21.711 53.549 38.849 1.00 14.68 ? 477  LEU A CB     1 
ATOM   4978 C CG     . LEU A 1 294 ? 22.320 52.586 37.853 1.00 17.00 ? 477  LEU A CG     1 
ATOM   4979 C CD1    . LEU A 1 294 ? 21.535 52.670 36.527 1.00 17.85 ? 477  LEU A CD1    1 
ATOM   4980 C CD2    . LEU A 1 294 ? 23.822 52.791 37.621 1.00 17.89 ? 477  LEU A CD2    1 
ATOM   4981 H H      . LEU A 1 294 ? 21.725 51.958 40.900 1.00 14.28 ? 477  LEU A H      1 
ATOM   4982 H HA     . LEU A 1 294 ? 23.381 53.915 40.034 1.00 15.02 ? 477  LEU A HA     1 
ATOM   4983 H HB2    . LEU A 1 294 ? 20.802 53.259 39.024 1.00 17.62 ? 477  LEU A HB2    1 
ATOM   4984 H HB3    . LEU A 1 294 ? 21.706 54.430 38.444 1.00 17.62 ? 477  LEU A HB3    1 
ATOM   4985 H HG     . LEU A 1 294 ? 22.252 51.692 38.224 1.00 20.40 ? 477  LEU A HG     1 
ATOM   4986 H HD11   . LEU A 1 294 ? 21.966 52.104 35.867 1.00 21.43 ? 477  LEU A HD11   1 
ATOM   4987 H HD12   . LEU A 1 294 ? 20.626 52.367 36.679 1.00 21.43 ? 477  LEU A HD12   1 
ATOM   4988 H HD13   . LEU A 1 294 ? 21.530 53.590 36.220 1.00 21.43 ? 477  LEU A HD13   1 
ATOM   4989 H HD21   . LEU A 1 294 ? 24.131 52.146 36.965 1.00 21.46 ? 477  LEU A HD21   1 
ATOM   4990 H HD22   . LEU A 1 294 ? 23.971 53.692 37.296 1.00 21.46 ? 477  LEU A HD22   1 
ATOM   4991 H HD23   . LEU A 1 294 ? 24.291 52.660 38.460 1.00 21.46 ? 477  LEU A HD23   1 
ATOM   4992 N N      . ARG A 1 295 ? 22.380 55.795 41.231 1.00 13.12 ? 478  ARG A N      1 
ATOM   4993 C CA     . ARG A 1 295 ? 21.813 56.904 41.988 1.00 13.26 ? 478  ARG A CA     1 
ATOM   4994 C C      . ARG A 1 295 ? 21.225 57.918 41.013 1.00 13.48 ? 478  ARG A C      1 
ATOM   4995 O O      . ARG A 1 295 ? 21.920 58.377 40.117 1.00 15.51 ? 478  ARG A O      1 
ATOM   4996 C CB     . ARG A 1 295 ? 22.912 57.607 42.784 1.00 14.07 ? 478  ARG A CB     1 
ATOM   4997 C CG     . ARG A 1 295 ? 23.402 56.836 43.979 1.00 13.44 ? 478  ARG A CG     1 
ATOM   4998 C CD     . ARG A 1 295 ? 24.623 57.488 44.583 1.00 13.25 ? 478  ARG A CD     1 
ATOM   4999 N NE     . ARG A 1 295 ? 24.896 56.858 45.861 1.00 12.69 ? 478  ARG A NE     1 
ATOM   5000 C CZ     . ARG A 1 295 ? 25.986 57.066 46.588 1.00 13.33 ? 478  ARG A CZ     1 
ATOM   5001 N NH1    . ARG A 1 295 ? 26.990 57.781 46.125 1.00 13.91 ? 478  ARG A NH1    1 
ATOM   5002 N NH2    . ARG A 1 295 ? 26.073 56.512 47.791 1.00 13.91 ? 478  ARG A NH2    1 
ATOM   5003 H H      . ARG A 1 295 ? 23.156 55.969 40.905 1.00 15.74 ? 478  ARG A H      1 
ATOM   5004 H HA     . ARG A 1 295 ? 21.121 56.567 42.579 1.00 15.91 ? 478  ARG A HA     1 
ATOM   5005 H HB2    . ARG A 1 295 ? 23.671 57.756 42.198 1.00 16.89 ? 478  ARG A HB2    1 
ATOM   5006 H HB3    . ARG A 1 295 ? 22.568 58.456 43.103 1.00 16.89 ? 478  ARG A HB3    1 
ATOM   5007 H HG2    . ARG A 1 295 ? 22.705 56.807 44.653 1.00 16.13 ? 478  ARG A HG2    1 
ATOM   5008 H HG3    . ARG A 1 295 ? 23.638 55.935 43.707 1.00 16.13 ? 478  ARG A HG3    1 
ATOM   5009 H HD2    . ARG A 1 295 ? 25.388 57.367 43.999 1.00 15.90 ? 478  ARG A HD2    1 
ATOM   5010 H HD3    . ARG A 1 295 ? 24.459 58.434 44.723 1.00 15.90 ? 478  ARG A HD3    1 
ATOM   5011 H HE     . ARG A 1 295 ? 24.309 56.310 46.169 1.00 15.23 ? 478  ARG A HE     1 
ATOM   5012 H HH11   . ARG A 1 295 ? 26.948 58.124 45.337 1.00 16.70 ? 478  ARG A HH11   1 
ATOM   5013 H HH12   . ARG A 1 295 ? 27.689 57.906 46.610 1.00 16.70 ? 478  ARG A HH12   1 
ATOM   5014 H HH21   . ARG A 1 295 ? 25.429 56.027 48.089 1.00 16.69 ? 478  ARG A HH21   1 
ATOM   5015 H HH22   . ARG A 1 295 ? 26.774 56.639 48.273 1.00 16.69 ? 478  ARG A HH22   1 
ATOM   5016 N N      . VAL A 1 296 ? 19.946 58.213 41.170 1.00 15.85 ? 479  VAL A N      1 
ATOM   5017 C CA     . VAL A 1 296 ? 19.220 59.104 40.265 1.00 21.03 ? 479  VAL A CA     1 
ATOM   5018 C C      . VAL A 1 296 ? 18.456 60.074 41.154 1.00 24.26 ? 479  VAL A C      1 
ATOM   5019 O O      . VAL A 1 296 ? 17.321 59.803 41.552 1.00 24.22 ? 479  VAL A O      1 
ATOM   5020 C CB     . VAL A 1 296 ? 18.255 58.341 39.360 1.00 24.15 ? 479  VAL A CB     1 
ATOM   5021 C CG1    . VAL A 1 296 ? 17.650 59.277 38.331 1.00 26.45 ? 479  VAL A CG1    1 
ATOM   5022 C CG2    . VAL A 1 296 ? 18.952 57.231 38.699 1.00 24.70 ? 479  VAL A CG2    1 
ATOM   5023 H H      . VAL A 1 296 ? 19.460 57.903 41.808 1.00 19.02 ? 479  VAL A H      1 
ATOM   5024 H HA     . VAL A 1 296 ? 19.848 59.601 39.717 1.00 25.24 ? 479  VAL A HA     1 
ATOM   5025 H HB     . VAL A 1 296 ? 17.535 57.974 39.896 1.00 28.98 ? 479  VAL A HB     1 
ATOM   5026 H HG11   . VAL A 1 296 ? 17.032 58.777 37.775 1.00 31.74 ? 479  VAL A HG11   1 
ATOM   5027 H HG12   . VAL A 1 296 ? 17.180 59.990 38.790 1.00 31.74 ? 479  VAL A HG12   1 
ATOM   5028 H HG13   . VAL A 1 296 ? 18.361 59.648 37.785 1.00 31.74 ? 479  VAL A HG13   1 
ATOM   5029 H HG21   . VAL A 1 296 ? 18.332 56.775 38.109 1.00 29.64 ? 479  VAL A HG21   1 
ATOM   5030 H HG22   . VAL A 1 296 ? 19.696 57.586 38.187 1.00 29.64 ? 479  VAL A HG22   1 
ATOM   5031 H HG23   . VAL A 1 296 ? 19.279 56.617 39.375 1.00 29.64 ? 479  VAL A HG23   1 
ATOM   5032 N N      . SER A 1 297 ? 19.076 61.205 41.466 1.00 27.69 ? 480  SER A N      1 
ATOM   5033 C CA     . SER A 1 297 ? 18.378 62.330 42.088 1.00 31.95 ? 480  SER A CA     1 
ATOM   5034 C C      . SER A 1 297 ? 17.504 61.863 43.254 1.00 32.49 ? 480  SER A C      1 
ATOM   5035 O O      . SER A 1 297 ? 16.299 62.120 43.317 1.00 35.21 ? 480  SER A O      1 
ATOM   5036 C CB     . SER A 1 297 ? 17.554 63.120 41.056 1.00 37.76 ? 480  SER A CB     1 
ATOM   5037 O OG     . SER A 1 297 ? 18.370 63.660 40.017 1.00 40.96 ? 480  SER A OG     1 
ATOM   5038 H H      . SER A 1 297 ? 19.912 61.350 41.327 1.00 33.23 ? 480  SER A H      1 
ATOM   5039 H HA     . SER A 1 297 ? 19.050 62.929 42.449 1.00 38.33 ? 480  SER A HA     1 
ATOM   5040 H HB2    . SER A 1 297 ? 16.899 62.525 40.659 1.00 45.32 ? 480  SER A HB2    1 
ATOM   5041 H HB3    . SER A 1 297 ? 17.106 63.851 41.510 1.00 45.32 ? 480  SER A HB3    1 
ATOM   5042 H HG     . SER A 1 297 ? 17.892 64.058 39.453 1.00 49.15 ? 480  SER A HG     1 
ATOM   5043 N N      . GLY A 1 298 ? 18.149 61.218 44.211 1.00 29.82 ? 481  GLY A N      1 
ATOM   5044 C CA     . GLY A 1 298 ? 17.502 60.803 45.430 1.00 28.13 ? 481  GLY A CA     1 
ATOM   5045 C C      . GLY A 1 298 ? 16.910 59.411 45.432 1.00 27.33 ? 481  GLY A C      1 
ATOM   5046 O O      . GLY A 1 298 ? 16.524 58.932 46.507 1.00 31.54 ? 481  GLY A O      1 
ATOM   5047 H H      . GLY A 1 298 ? 18.982 61.006 44.171 1.00 35.79 ? 481  GLY A H      1 
ATOM   5048 H HA2    . GLY A 1 298 ? 18.152 60.843 46.149 1.00 33.75 ? 481  GLY A HA2    1 
ATOM   5049 H HA3    . GLY A 1 298 ? 16.782 61.424 45.620 1.00 33.75 ? 481  GLY A HA3    1 
ATOM   5050 N N      . LYS A 1 299 ? 16.802 58.751 44.277 1.00 23.41 ? 482  LYS A N      1 
ATOM   5051 C CA     . LYS A 1 299 ? 16.342 57.371 44.195 1.00 23.01 ? 482  LYS A CA     1 
ATOM   5052 C C      . LYS A 1 299 ? 17.508 56.474 43.783 1.00 19.59 ? 482  LYS A C      1 
ATOM   5053 O O      . LYS A 1 299 ? 18.404 56.883 43.050 1.00 19.81 ? 482  LYS A O      1 
ATOM   5054 C CB     . LYS A 1 299 ? 15.202 57.247 43.186 1.00 27.17 ? 482  LYS A CB     1 
ATOM   5055 C CG     . LYS A 1 299 ? 13.990 58.144 43.477 1.00 32.88 ? 482  LYS A CG     1 
ATOM   5056 C CD     . LYS A 1 299 ? 12.845 57.839 42.527 1.00 36.59 ? 482  LYS A CD     1 
ATOM   5057 C CE     . LYS A 1 299 ? 11.630 58.713 42.787 1.00 41.23 ? 482  LYS A CE     1 
ATOM   5058 N NZ     . LYS A 1 299 ? 11.647 59.370 44.125 1.00 44.88 ? 482  LYS A NZ     1 
ATOM   5059 H H      . LYS A 1 299 ? 16.994 59.094 43.512 1.00 28.10 ? 482  LYS A H      1 
ATOM   5060 H HA     . LYS A 1 299 ? 16.016 57.069 45.057 1.00 27.61 ? 482  LYS A HA     1 
ATOM   5061 H HB2    . LYS A 1 299 ? 15.539 57.486 42.309 1.00 32.61 ? 482  LYS A HB2    1 
ATOM   5062 H HB3    . LYS A 1 299 ? 14.891 56.328 43.183 1.00 32.61 ? 482  LYS A HB3    1 
ATOM   5063 H HG2    . LYS A 1 299 ? 13.684 57.991 44.384 1.00 39.46 ? 482  LYS A HG2    1 
ATOM   5064 H HG3    . LYS A 1 299 ? 14.242 59.074 43.364 1.00 39.46 ? 482  LYS A HG3    1 
ATOM   5065 H HD2    . LYS A 1 299 ? 13.138 57.994 41.615 1.00 43.90 ? 482  LYS A HD2    1 
ATOM   5066 H HD3    . LYS A 1 299 ? 12.579 56.913 42.637 1.00 43.90 ? 482  LYS A HD3    1 
ATOM   5067 H HE2    . LYS A 1 299 ? 11.595 59.410 42.114 1.00 49.48 ? 482  LYS A HE2    1 
ATOM   5068 H HE3    . LYS A 1 299 ? 10.832 58.163 42.737 1.00 49.48 ? 482  LYS A HE3    1 
ATOM   5069 H HZ1    . LYS A 1 299 ? 10.892 59.822 44.251 1.00 53.86 ? 482  LYS A HZ1    1 
ATOM   5070 H HZ2    . LYS A 1 299 ? 11.727 58.756 44.764 1.00 53.86 ? 482  LYS A HZ2    1 
ATOM   5071 H HZ3    . LYS A 1 299 ? 12.334 59.934 44.178 1.00 53.86 ? 482  LYS A HZ3    1 
ATOM   5072 N N      . SER A 1 300 ? 17.489 55.236 44.234 1.00 19.94 ? 483  SER A N      1 
ATOM   5073 C CA     A SER A 1 300 ? 18.551 54.284 43.903 0.62 18.29 ? 483  SER A CA     1 
ATOM   5074 C CA     B SER A 1 300 ? 18.536 54.264 43.928 0.38 19.04 ? 483  SER A CA     1 
ATOM   5075 C C      . SER A 1 300 ? 17.901 53.035 43.296 1.00 18.69 ? 483  SER A C      1 
ATOM   5076 O O      . SER A 1 300 ? 16.793 52.652 43.661 1.00 24.18 ? 483  SER A O      1 
ATOM   5077 C CB     A SER A 1 300 ? 19.532 54.046 45.144 0.62 19.11 ? 483  SER A CB     1 
ATOM   5078 C CB     B SER A 1 300 ? 19.286 53.846 45.206 0.38 19.54 ? 483  SER A CB     1 
ATOM   5079 O OG     A SER A 1 300 ? 20.299 55.211 45.485 0.62 18.18 ? 483  SER A OG     1 
ATOM   5080 O OG     B SER A 1 300 ? 18.677 54.374 46.364 0.38 16.43 ? 483  SER A OG     1 
ATOM   5081 H H      A SER A 1 300 ? 16.871 54.913 44.737 0.62 23.92 ? 483  SER A H      1 
ATOM   5082 H H      B SER A 1 300 ? 16.865 54.919 44.733 0.38 23.92 ? 483  SER A H      1 
ATOM   5083 H HA     A SER A 1 300 ? 19.150 54.607 43.211 0.62 21.95 ? 483  SER A HA     1 
ATOM   5084 H HA     B SER A 1 300 ? 19.173 54.649 43.306 0.38 22.85 ? 483  SER A HA     1 
ATOM   5085 H HB2    A SER A 1 300 ? 18.998 53.794 45.913 0.62 22.94 ? 483  SER A HB2    1 
ATOM   5086 H HB2    B SER A 1 300 ? 19.285 52.878 45.266 0.38 23.45 ? 483  SER A HB2    1 
ATOM   5087 H HB3    A SER A 1 300 ? 20.146 53.330 44.917 0.62 22.94 ? 483  SER A HB3    1 
ATOM   5088 H HB3    B SER A 1 300 ? 20.197 54.174 45.154 0.38 23.45 ? 483  SER A HB3    1 
ATOM   5089 H HG     A SER A 1 300 ? 20.774 55.054 46.160 0.62 21.81 ? 483  SER A HG     1 
ATOM   5090 H HG     B SER A 1 300 ? 19.083 54.106 47.050 0.38 19.72 ? 483  SER A HG     1 
ATOM   5091 N N      . TYR A 1 301 ? 18.574 52.458 42.319 1.00 14.01 ? 484  TYR A N      1 
ATOM   5092 C CA     . TYR A 1 301 ? 18.064 51.304 41.575 1.00 13.12 ? 484  TYR A CA     1 
ATOM   5093 C C      . TYR A 1 301 ? 19.192 50.291 41.450 1.00 12.45 ? 484  TYR A C      1 
ATOM   5094 O O      . TYR A 1 301 ? 20.314 50.649 41.086 1.00 13.71 ? 484  TYR A O      1 
ATOM   5095 C CB     . TYR A 1 301 ? 17.668 51.700 40.145 1.00 14.51 ? 484  TYR A CB     1 
ATOM   5096 C CG     . TYR A 1 301 ? 16.609 52.735 40.078 1.00 17.03 ? 484  TYR A CG     1 
ATOM   5097 C CD1    . TYR A 1 301 ? 15.297 52.378 40.064 1.00 19.64 ? 484  TYR A CD1    1 
ATOM   5098 C CD2    . TYR A 1 301 ? 16.936 54.092 40.022 1.00 19.57 ? 484  TYR A CD2    1 
ATOM   5099 C CE1    . TYR A 1 301 ? 14.293 53.334 39.987 1.00 21.80 ? 484  TYR A CE1    1 
ATOM   5100 C CE2    . TYR A 1 301 ? 15.957 55.071 39.970 1.00 21.86 ? 484  TYR A CE2    1 
ATOM   5101 C CZ     . TYR A 1 301 ? 14.636 54.679 39.957 1.00 22.85 ? 484  TYR A CZ     1 
ATOM   5102 O OH     . TYR A 1 301 ? 13.629 55.648 39.894 1.00 26.65 ? 484  TYR A OH     1 
ATOM   5103 H H      . TYR A 1 301 ? 19.350 52.718 42.055 1.00 16.81 ? 484  TYR A H      1 
ATOM   5104 H HA     . TYR A 1 301 ? 17.302 50.928 42.041 1.00 15.75 ? 484  TYR A HA     1 
ATOM   5105 H HB2    . TYR A 1 301 ? 18.451 52.049 39.690 1.00 17.41 ? 484  TYR A HB2    1 
ATOM   5106 H HB3    . TYR A 1 301 ? 17.341 50.912 39.683 1.00 17.41 ? 484  TYR A HB3    1 
ATOM   5107 H HD1    . TYR A 1 301 ? 15.069 51.478 40.106 1.00 23.56 ? 484  TYR A HD1    1 
ATOM   5108 H HD2    . TYR A 1 301 ? 17.831 54.344 40.021 1.00 23.48 ? 484  TYR A HD2    1 
ATOM   5109 H HE1    . TYR A 1 301 ? 13.400 53.076 39.956 1.00 26.16 ? 484  TYR A HE1    1 
ATOM   5110 H HE2    . TYR A 1 301 ? 16.187 55.971 39.944 1.00 26.23 ? 484  TYR A HE2    1 
ATOM   5111 H HH     . TYR A 1 301 ? 13.969 56.413 39.831 1.00 31.98 ? 484  TYR A HH     1 
ATOM   5112 N N      . VAL A 1 302 ? 18.886 49.029 41.681 1.00 11.34 ? 485  VAL A N      1 
ATOM   5113 C CA     . VAL A 1 302 ? 19.858 47.963 41.486 1.00 11.23 ? 485  VAL A CA     1 
ATOM   5114 C C      . VAL A 1 302 ? 19.763 47.510 40.036 1.00 10.58 ? 485  VAL A C      1 
ATOM   5115 O O      . VAL A 1 302 ? 18.652 47.306 39.513 1.00 13.23 ? 485  VAL A O      1 
ATOM   5116 C CB     . VAL A 1 302 ? 19.632 46.808 42.466 1.00 11.01 ? 485  VAL A CB     1 
ATOM   5117 C CG1    . VAL A 1 302 ? 20.555 45.643 42.136 1.00 11.68 ? 485  VAL A CG1    1 
ATOM   5118 C CG2    . VAL A 1 302 ? 19.882 47.305 43.867 1.00 11.84 ? 485  VAL A CG2    1 
ATOM   5119 H H      . VAL A 1 302 ? 18.116 48.758 41.954 1.00 13.61 ? 485  VAL A H      1 
ATOM   5120 H HA     . VAL A 1 302 ? 20.754 48.297 41.649 1.00 13.47 ? 485  VAL A HA     1 
ATOM   5121 H HB     . VAL A 1 302 ? 18.719 46.488 42.398 1.00 13.22 ? 485  VAL A HB     1 
ATOM   5122 H HG11   . VAL A 1 302 ? 20.460 44.962 42.821 1.00 14.02 ? 485  VAL A HG11   1 
ATOM   5123 H HG12   . VAL A 1 302 ? 20.307 45.279 41.272 1.00 14.02 ? 485  VAL A HG12   1 
ATOM   5124 H HG13   . VAL A 1 302 ? 21.470 45.962 42.111 1.00 14.02 ? 485  VAL A HG13   1 
ATOM   5125 H HG21   . VAL A 1 302 ? 19.678 46.595 44.496 1.00 14.21 ? 485  VAL A HG21   1 
ATOM   5126 H HG22   . VAL A 1 302 ? 20.814 47.562 43.950 1.00 14.21 ? 485  VAL A HG22   1 
ATOM   5127 H HG23   . VAL A 1 302 ? 19.312 48.071 44.037 1.00 14.21 ? 485  VAL A HG23   1 
ATOM   5128 N N      . ILE A 1 303 ? 20.906 47.366 39.371 1.00 11.87 ? 486  ILE A N      1 
ATOM   5129 C CA     . ILE A 1 303 ? 20.926 46.954 37.986 1.00 13.78 ? 486  ILE A CA     1 
ATOM   5130 C C      . ILE A 1 303 ? 21.605 45.613 37.775 1.00 15.84 ? 486  ILE A C      1 
ATOM   5131 O O      . ILE A 1 303 ? 21.297 44.923 36.787 1.00 20.06 ? 486  ILE A O      1 
ATOM   5132 C CB     . ILE A 1 303 ? 21.500 48.028 37.046 1.00 13.80 ? 486  ILE A CB     1 
ATOM   5133 C CG1    . ILE A 1 303 ? 22.882 48.517 37.496 1.00 14.08 ? 486  ILE A CG1    1 
ATOM   5134 C CG2    . ILE A 1 303 ? 20.531 49.159 36.910 1.00 14.76 ? 486  ILE A CG2    1 
ATOM   5135 C CD1    . ILE A 1 303 ? 23.653 49.042 36.429 1.00 16.51 ? 486  ILE A CD1    1 
ATOM   5136 H H      . ILE A 1 303 ? 21.685 47.503 39.709 1.00 14.25 ? 486  ILE A H      1 
ATOM   5137 H HA     . ILE A 1 303 ? 20.003 46.846 37.705 1.00 16.53 ? 486  ILE A HA     1 
ATOM   5138 H HB     . ILE A 1 303 ? 21.629 47.621 36.175 1.00 16.56 ? 486  ILE A HB     1 
ATOM   5139 H HG12   . ILE A 1 303 ? 22.769 49.217 38.158 1.00 16.90 ? 486  ILE A HG12   1 
ATOM   5140 H HG13   . ILE A 1 303 ? 23.371 47.772 37.881 1.00 16.90 ? 486  ILE A HG13   1 
ATOM   5141 H HG21   . ILE A 1 303 ? 20.783 49.701 36.145 1.00 17.71 ? 486  ILE A HG21   1 
ATOM   5142 H HG22   . ILE A 1 303 ? 19.640 48.798 36.781 1.00 17.71 ? 486  ILE A HG22   1 
ATOM   5143 H HG23   . ILE A 1 303 ? 20.557 49.696 37.718 1.00 17.71 ? 486  ILE A HG23   1 
ATOM   5144 H HD11   . ILE A 1 303 ? 24.552 49.221 36.746 1.00 19.81 ? 486  ILE A HD11   1 
ATOM   5145 H HD12   . ILE A 1 303 ? 23.679 48.393 35.708 1.00 19.81 ? 486  ILE A HD12   1 
ATOM   5146 H HD13   . ILE A 1 303 ? 23.242 49.865 36.118 1.00 19.81 ? 486  ILE A HD13   1 
ATOM   5147 N N      . ASP A 1 304 ? 22.472 45.173 38.659 1.00 13.75 ? 487  ASP A N      1 
ATOM   5148 C CA     A ASP A 1 304 ? 23.202 43.923 38.467 0.57 13.63 ? 487  ASP A CA     1 
ATOM   5149 C CA     B ASP A 1 304 ? 23.062 43.862 38.479 0.43 14.90 ? 487  ASP A CA     1 
ATOM   5150 C C      . ASP A 1 304 ? 23.542 43.352 39.820 1.00 12.73 ? 487  ASP A C      1 
ATOM   5151 O O      . ASP A 1 304 ? 23.797 44.105 40.749 1.00 12.66 ? 487  ASP A O      1 
ATOM   5152 C CB     A ASP A 1 304 ? 24.528 44.174 37.762 0.57 16.90 ? 487  ASP A CB     1 
ATOM   5153 C CB     B ASP A 1 304 ? 24.131 43.864 37.374 0.43 18.62 ? 487  ASP A CB     1 
ATOM   5154 C CG     A ASP A 1 304 ? 24.357 44.410 36.316 0.57 23.82 ? 487  ASP A CG     1 
ATOM   5155 C CG     B ASP A 1 304 ? 25.530 43.850 37.898 0.43 23.12 ? 487  ASP A CG     1 
ATOM   5156 O OD1    A ASP A 1 304 ? 24.037 43.444 35.583 0.57 27.03 ? 487  ASP A OD1    1 
ATOM   5157 O OD1    B ASP A 1 304 ? 25.808 44.556 38.881 0.43 23.53 ? 487  ASP A OD1    1 
ATOM   5158 O OD2    A ASP A 1 304 ? 24.481 45.585 35.941 0.57 26.67 ? 487  ASP A OD2    1 
ATOM   5159 O OD2    B ASP A 1 304 ? 26.358 43.122 37.294 0.43 25.72 ? 487  ASP A OD2    1 
ATOM   5160 H H      A ASP A 1 304 ? 22.663 45.580 39.392 0.57 16.50 ? 487  ASP A H      1 
ATOM   5161 H H      B ASP A 1 304 ? 22.730 45.603 39.358 0.43 16.50 ? 487  ASP A H      1 
ATOM   5162 H HA     A ASP A 1 304 ? 22.647 43.309 37.961 0.57 16.36 ? 487  ASP A HA     1 
ATOM   5163 H HA     B ASP A 1 304 ? 22.396 43.221 38.185 0.43 17.88 ? 487  ASP A HA     1 
ATOM   5164 H HB2    A ASP A 1 304 ? 24.949 44.958 38.148 0.57 20.29 ? 487  ASP A HB2    1 
ATOM   5165 H HB2    B ASP A 1 304 ? 24.013 43.075 36.823 0.43 22.34 ? 487  ASP A HB2    1 
ATOM   5166 H HB3    A ASP A 1 304 ? 25.100 43.399 37.876 0.57 20.29 ? 487  ASP A HB3    1 
ATOM   5167 H HB3    B ASP A 1 304 ? 24.024 44.664 36.836 0.43 22.34 ? 487  ASP A HB3    1 
ATOM   5168 N N      . VAL A 1 305 ? 23.597 42.038 39.905 1.00 11.72 ? 488  VAL A N      1 
ATOM   5169 C CA     . VAL A 1 305 ? 24.051 41.327 41.089 1.00 11.75 ? 488  VAL A CA     1 
ATOM   5170 C C      . VAL A 1 305 ? 25.135 40.367 40.638 1.00 12.73 ? 488  VAL A C      1 
ATOM   5171 O O      . VAL A 1 305 ? 24.901 39.544 39.749 1.00 14.21 ? 488  VAL A O      1 
ATOM   5172 C CB     . VAL A 1 305 ? 22.918 40.588 41.801 1.00 12.49 ? 488  VAL A CB     1 
ATOM   5173 C CG1    . VAL A 1 305 ? 23.434 39.843 42.998 1.00 13.07 ? 488  VAL A CG1    1 
ATOM   5174 C CG2    . VAL A 1 305 ? 21.802 41.570 42.144 1.00 13.58 ? 488  VAL A CG2    1 
ATOM   5175 H H      . VAL A 1 305 ? 23.366 41.512 39.264 1.00 14.07 ? 488  VAL A H      1 
ATOM   5176 H HA     . VAL A 1 305 ? 24.431 41.953 41.724 1.00 14.10 ? 488  VAL A HA     1 
ATOM   5177 H HB     . VAL A 1 305 ? 22.537 39.915 41.215 1.00 14.99 ? 488  VAL A HB     1 
ATOM   5178 H HG11   . VAL A 1 305 ? 22.689 39.414 43.448 1.00 15.69 ? 488  VAL A HG11   1 
ATOM   5179 H HG12   . VAL A 1 305 ? 24.071 39.174 42.702 1.00 15.69 ? 488  VAL A HG12   1 
ATOM   5180 H HG13   . VAL A 1 305 ? 23.867 40.470 43.598 1.00 15.69 ? 488  VAL A HG13   1 
ATOM   5181 H HG21   . VAL A 1 305 ? 21.105 41.100 42.629 1.00 16.30 ? 488  VAL A HG21   1 
ATOM   5182 H HG22   . VAL A 1 305 ? 22.165 42.281 42.694 1.00 16.30 ? 488  VAL A HG22   1 
ATOM   5183 H HG23   . VAL A 1 305 ? 21.442 41.939 41.322 1.00 16.30 ? 488  VAL A HG23   1 
ATOM   5184 N N      . ASN A 1 306 ? 26.330 40.509 41.194 1.00 12.83 ? 489  ASN A N      1 
ATOM   5185 C CA     . ASN A 1 306 ? 27.484 39.765 40.706 1.00 14.58 ? 489  ASN A CA     1 
ATOM   5186 C C      . ASN A 1 306 ? 27.889 38.598 41.577 1.00 14.19 ? 489  ASN A C      1 
ATOM   5187 O O      . ASN A 1 306 ? 28.717 37.788 41.150 1.00 16.77 ? 489  ASN A O      1 
ATOM   5188 C CB     . ASN A 1 306 ? 28.673 40.700 40.538 1.00 19.31 ? 489  ASN A CB     1 
ATOM   5189 C CG     . ASN A 1 306 ? 28.318 41.872 39.696 1.00 27.95 ? 489  ASN A CG     1 
ATOM   5190 O OD1    . ASN A 1 306 ? 28.526 43.034 40.065 1.00 31.42 ? 489  ASN A OD1    1 
ATOM   5191 N ND2    . ASN A 1 306 ? 27.718 41.575 38.555 1.00 29.55 ? 489  ASN A ND2    1 
ATOM   5192 H H      . ASN A 1 306 ? 26.499 41.031 41.856 1.00 15.39 ? 489  ASN A H      1 
ATOM   5193 H HA     . ASN A 1 306 ? 27.255 39.399 39.837 1.00 17.49 ? 489  ASN A HA     1 
ATOM   5194 H HB2    . ASN A 1 306 ? 28.956 41.022 41.408 1.00 23.18 ? 489  ASN A HB2    1 
ATOM   5195 H HB3    . ASN A 1 306 ? 29.401 40.223 40.108 1.00 23.18 ? 489  ASN A HB3    1 
ATOM   5196 H HD21   . ASN A 1 306 ? 27.483 42.203 38.017 1.00 35.46 ? 489  ASN A HD21   1 
ATOM   5197 H HD22   . ASN A 1 306 ? 27.564 40.754 38.351 1.00 35.46 ? 489  ASN A HD22   1 
ATOM   5198 N N      . GLY A 1 307 ? 27.339 38.472 42.749 1.00 13.33 ? 490  GLY A N      1 
ATOM   5199 C CA     . GLY A 1 307 ? 27.692 37.366 43.625 1.00 13.79 ? 490  GLY A CA     1 
ATOM   5200 C C      . GLY A 1 307 ? 28.994 37.634 44.366 1.00 11.93 ? 490  GLY A C      1 
ATOM   5201 O O      . GLY A 1 307 ? 29.387 38.775 44.564 1.00 12.68 ? 490  GLY A O      1 
ATOM   5202 H H      . GLY A 1 307 ? 26.752 39.010 43.075 1.00 16.00 ? 490  GLY A H      1 
ATOM   5203 H HA2    . GLY A 1 307 ? 26.987 37.231 44.278 1.00 16.55 ? 490  GLY A HA2    1 
ATOM   5204 H HA3    . GLY A 1 307 ? 27.796 36.557 43.100 1.00 16.55 ? 490  GLY A HA3    1 
ATOM   5205 N N      . PHE A 1 308 ? 29.627 36.570 44.822 1.00 11.51 ? 491  PHE A N      1 
ATOM   5206 C CA     . PHE A 1 308 ? 30.774 36.658 45.718 1.00 10.63 ? 491  PHE A CA     1 
ATOM   5207 C C      . PHE A 1 308 ? 31.823 37.625 45.197 1.00 10.75 ? 491  PHE A C      1 
ATOM   5208 O O      . PHE A 1 308 ? 32.343 37.475 44.084 1.00 12.61 ? 491  PHE A O      1 
ATOM   5209 C CB     . PHE A 1 308 ? 31.393 35.259 45.856 1.00 11.87 ? 491  PHE A CB     1 
ATOM   5210 C CG     . PHE A 1 308 ? 32.320 35.149 47.026 1.00 12.30 ? 491  PHE A CG     1 
ATOM   5211 C CD1    . PHE A 1 308 ? 33.612 35.678 46.945 1.00 12.69 ? 491  PHE A CD1    1 
ATOM   5212 C CD2    . PHE A 1 308 ? 31.899 34.609 48.200 1.00 13.17 ? 491  PHE A CD2    1 
ATOM   5213 C CE1    . PHE A 1 308 ? 34.492 35.614 48.065 1.00 13.47 ? 491  PHE A CE1    1 
ATOM   5214 C CE2    . PHE A 1 308 ? 32.766 34.542 49.315 1.00 14.02 ? 491  PHE A CE2    1 
ATOM   5215 C CZ     . PHE A 1 308 ? 34.035 35.051 49.223 1.00 13.00 ? 491  PHE A CZ     1 
ATOM   5216 H H      . PHE A 1 308 ? 29.411 35.761 44.625 1.00 13.81 ? 491  PHE A H      1 
ATOM   5217 H HA     . PHE A 1 308 ? 30.474 36.980 46.582 1.00 12.75 ? 491  PHE A HA     1 
ATOM   5218 H HB2    . PHE A 1 308 ? 30.683 34.610 45.974 1.00 14.25 ? 491  PHE A HB2    1 
ATOM   5219 H HB3    . PHE A 1 308 ? 31.898 35.057 45.053 1.00 14.25 ? 491  PHE A HB3    1 
ATOM   5220 H HD1    . PHE A 1 308 ? 33.900 36.074 46.154 1.00 15.23 ? 491  PHE A HD1    1 
ATOM   5221 H HD2    . PHE A 1 308 ? 31.032 34.280 48.271 1.00 15.81 ? 491  PHE A HD2    1 
ATOM   5222 H HE1    . PHE A 1 308 ? 35.358 35.948 48.008 1.00 16.17 ? 491  PHE A HE1    1 
ATOM   5223 H HE2    . PHE A 1 308 ? 32.476 34.153 50.109 1.00 16.83 ? 491  PHE A HE2    1 
ATOM   5224 H HZ     . PHE A 1 308 ? 34.596 35.012 49.963 1.00 15.60 ? 491  PHE A HZ     1 
ATOM   5225 N N      . SER A 1 309 ? 32.133 38.642 46.000 1.00 10.87 ? 492  SER A N      1 
ATOM   5226 C CA     . SER A 1 309 ? 33.056 39.697 45.571 1.00 12.20 ? 492  SER A CA     1 
ATOM   5227 C C      . SER A 1 309 ? 33.630 40.346 46.812 1.00 11.03 ? 492  SER A C      1 
ATOM   5228 O O      . SER A 1 309 ? 32.896 40.773 47.698 1.00 11.91 ? 492  SER A O      1 
ATOM   5229 C CB     . SER A 1 309 ? 32.300 40.752 44.759 1.00 15.66 ? 492  SER A CB     1 
ATOM   5230 O OG     . SER A 1 309 ? 33.219 41.683 44.261 1.00 20.43 ? 492  SER A OG     1 
ATOM   5231 H H      . SER A 1 309 ? 31.824 38.746 46.795 1.00 13.04 ? 492  SER A H      1 
ATOM   5232 H HA     . SER A 1 309 ? 33.772 39.316 45.038 1.00 14.64 ? 492  SER A HA     1 
ATOM   5233 H HB2    . SER A 1 309 ? 31.840 40.323 44.020 1.00 18.80 ? 492  SER A HB2    1 
ATOM   5234 H HB3    . SER A 1 309 ? 31.659 41.203 45.331 1.00 18.80 ? 492  SER A HB3    1 
ATOM   5235 H HG     . SER A 1 309 ? 32.815 42.293 43.850 1.00 24.52 ? 492  SER A HG     1 
ATOM   5236 N N      . PHE A 1 310 ? 34.949 40.363 46.904 1.00 11.98 ? 493  PHE A N      1 
ATOM   5237 C CA     . PHE A 1 310 ? 35.650 41.084 47.960 1.00 12.16 ? 493  PHE A CA     1 
ATOM   5238 C C      . PHE A 1 310 ? 36.100 42.459 47.461 1.00 13.89 ? 493  PHE A C      1 
ATOM   5239 O O      . PHE A 1 310 ? 36.348 42.664 46.279 1.00 15.06 ? 493  PHE A O      1 
ATOM   5240 C CB     . PHE A 1 310 ? 36.936 40.328 48.283 1.00 13.32 ? 493  PHE A CB     1 
ATOM   5241 C CG     . PHE A 1 310 ? 36.797 39.055 49.089 1.00 12.93 ? 493  PHE A CG     1 
ATOM   5242 C CD1    . PHE A 1 310 ? 35.993 38.959 50.205 1.00 14.25 ? 493  PHE A CD1    1 
ATOM   5243 C CD2    . PHE A 1 310 ? 37.630 37.967 48.818 1.00 15.24 ? 493  PHE A CD2    1 
ATOM   5244 C CE1    . PHE A 1 310 ? 35.990 37.801 50.988 1.00 17.39 ? 493  PHE A CE1    1 
ATOM   5245 C CE2    . PHE A 1 310 ? 37.601 36.835 49.599 1.00 16.28 ? 493  PHE A CE2    1 
ATOM   5246 C CZ     . PHE A 1 310 ? 36.838 36.761 50.683 1.00 16.13 ? 493  PHE A CZ     1 
ATOM   5247 H H      . PHE A 1 310 ? 35.474 39.956 46.357 1.00 14.38 ? 493  PHE A H      1 
ATOM   5248 H HA     . PHE A 1 310 ? 35.066 41.177 48.729 1.00 14.59 ? 493  PHE A HA     1 
ATOM   5249 H HB2    . PHE A 1 310 ? 37.360 40.086 47.444 1.00 15.98 ? 493  PHE A HB2    1 
ATOM   5250 H HB3    . PHE A 1 310 ? 37.514 40.921 48.788 1.00 15.98 ? 493  PHE A HB3    1 
ATOM   5251 H HD1    . PHE A 1 310 ? 35.446 39.673 50.440 1.00 17.10 ? 493  PHE A HD1    1 
ATOM   5252 H HD2    . PHE A 1 310 ? 38.215 38.009 48.097 1.00 18.29 ? 493  PHE A HD2    1 
ATOM   5253 H HE1    . PHE A 1 310 ? 35.415 37.733 51.715 1.00 20.86 ? 493  PHE A HE1    1 
ATOM   5254 H HE2    . PHE A 1 310 ? 38.127 36.106 49.362 1.00 19.54 ? 493  PHE A HE2    1 
ATOM   5255 H HZ     . PHE A 1 310 ? 36.877 36.012 51.232 1.00 19.36 ? 493  PHE A HZ     1 
ATOM   5256 N N      . VAL A 1 311 ? 36.294 43.362 48.380 1.00 13.12 ? 494  VAL A N      1 
ATOM   5257 C CA     . VAL A 1 311 ? 37.048 44.575 48.100 1.00 12.93 ? 494  VAL A CA     1 
ATOM   5258 C C      . VAL A 1 311 ? 38.526 44.227 48.193 1.00 14.13 ? 494  VAL A C      1 
ATOM   5259 O O      . VAL A 1 311 ? 38.946 43.553 49.131 1.00 15.70 ? 494  VAL A O      1 
ATOM   5260 C CB     . VAL A 1 311 ? 36.673 45.664 49.114 1.00 13.19 ? 494  VAL A CB     1 
ATOM   5261 C CG1    . VAL A 1 311 ? 37.496 46.929 48.924 1.00 15.51 ? 494  VAL A CG1    1 
ATOM   5262 C CG2    . VAL A 1 311 ? 35.145 45.981 49.053 1.00 14.04 ? 494  VAL A CG2    1 
ATOM   5263 H H      . VAL A 1 311 ? 36.002 43.306 49.187 1.00 15.75 ? 494  VAL A H      1 
ATOM   5264 H HA     . VAL A 1 311 ? 36.847 44.904 47.210 1.00 15.52 ? 494  VAL A HA     1 
ATOM   5265 H HB     . VAL A 1 311 ? 36.878 45.322 49.998 1.00 15.83 ? 494  VAL A HB     1 
ATOM   5266 H HG11   . VAL A 1 311 ? 37.189 47.602 49.551 1.00 18.62 ? 494  VAL A HG11   1 
ATOM   5267 H HG12   . VAL A 1 311 ? 38.430 46.726 49.087 1.00 18.62 ? 494  VAL A HG12   1 
ATOM   5268 H HG13   . VAL A 1 311 ? 37.381 47.247 48.015 1.00 18.62 ? 494  VAL A HG13   1 
ATOM   5269 H HG21   . VAL A 1 311 ? 34.929 46.630 49.741 1.00 16.85 ? 494  VAL A HG21   1 
ATOM   5270 H HG22   . VAL A 1 311 ? 34.932 46.344 48.179 1.00 16.85 ? 494  VAL A HG22   1 
ATOM   5271 H HG23   . VAL A 1 311 ? 34.646 45.163 49.202 1.00 16.85 ? 494  VAL A HG23   1 
ATOM   5272 N N      . LYS A 1 312 ? 39.317 44.698 47.230 1.00 15.21 ? 495  LYS A N      1 
ATOM   5273 C CA     . LYS A 1 312 ? 40.760 44.504 47.228 1.00 16.78 ? 495  LYS A CA     1 
ATOM   5274 C C      . LYS A 1 312 ? 41.497 45.679 47.855 1.00 16.01 ? 495  LYS A C      1 
ATOM   5275 O O      . LYS A 1 312 ? 41.118 46.846 47.679 1.00 16.72 ? 495  LYS A O      1 
ATOM   5276 C CB     . LYS A 1 312 ? 41.257 44.339 45.797 1.00 23.42 ? 495  LYS A CB     1 
ATOM   5277 C CG     . LYS A 1 312 ? 42.719 43.960 45.675 1.00 33.08 ? 495  LYS A CG     1 
ATOM   5278 C CD     . LYS A 1 312 ? 43.011 43.132 44.421 1.00 40.93 ? 495  LYS A CD     1 
ATOM   5279 C CE     . LYS A 1 312 ? 42.136 43.500 43.227 1.00 46.32 ? 495  LYS A CE     1 
ATOM   5280 N NZ     . LYS A 1 312 ? 42.242 44.917 42.811 1.00 49.19 ? 495  LYS A NZ     1 
ATOM   5281 H H      . LYS A 1 312 ? 39.032 45.142 46.551 1.00 18.25 ? 495  LYS A H      1 
ATOM   5282 H HA     . LYS A 1 312 ? 40.959 43.713 47.753 1.00 20.13 ? 495  LYS A HA     1 
ATOM   5283 H HB2    . LYS A 1 312 ? 40.737 43.641 45.369 1.00 28.10 ? 495  LYS A HB2    1 
ATOM   5284 H HB3    . LYS A 1 312 ? 41.133 45.179 45.328 1.00 28.10 ? 495  LYS A HB3    1 
ATOM   5285 H HG2    . LYS A 1 312 ? 43.253 44.768 45.632 1.00 39.69 ? 495  LYS A HG2    1 
ATOM   5286 H HG3    . LYS A 1 312 ? 42.975 43.434 46.449 1.00 39.69 ? 495  LYS A HG3    1 
ATOM   5287 H HD2    . LYS A 1 312 ? 43.936 43.270 44.164 1.00 49.12 ? 495  LYS A HD2    1 
ATOM   5288 H HD3    . LYS A 1 312 ? 42.859 42.195 44.622 1.00 49.12 ? 495  LYS A HD3    1 
ATOM   5289 H HE2    . LYS A 1 312 ? 42.396 42.951 42.471 1.00 55.59 ? 495  LYS A HE2    1 
ATOM   5290 H HE3    . LYS A 1 312 ? 41.209 43.330 43.457 1.00 55.59 ? 495  LYS A HE3    1 
ATOM   5291 H HZ1    . LYS A 1 312 ? 41.647 45.092 42.173 1.00 59.03 ? 495  LYS A HZ1    1 
ATOM   5292 H HZ2    . LYS A 1 312 ? 42.087 45.451 43.505 1.00 59.03 ? 495  LYS A HZ2    1 
ATOM   5293 H HZ3    . LYS A 1 312 ? 43.058 45.081 42.497 1.00 59.03 ? 495  LYS A HZ3    1 
ATOM   5294 N N      . ASP A 1 313 ? 42.564 45.361 48.592 1.00 15.84 ? 496  ASP A N      1 
ATOM   5295 C CA     . ASP A 1 313 ? 43.557 46.340 49.028 1.00 15.55 ? 496  ASP A CA     1 
ATOM   5296 C C      . ASP A 1 313 ? 42.952 47.356 49.997 1.00 16.64 ? 496  ASP A C      1 
ATOM   5297 O O      . ASP A 1 313 ? 43.294 48.529 49.977 1.00 20.77 ? 496  ASP A O      1 
ATOM   5298 C CB     . ASP A 1 313 ? 44.240 47.029 47.847 1.00 18.04 ? 496  ASP A CB     1 
ATOM   5299 C CG     . ASP A 1 313 ? 44.996 46.075 46.960 1.00 22.00 ? 496  ASP A CG     1 
ATOM   5300 O OD1    . ASP A 1 313 ? 45.589 45.082 47.434 1.00 24.18 ? 496  ASP A OD1    1 
ATOM   5301 O OD2    . ASP A 1 313 ? 45.028 46.337 45.748 1.00 23.72 ? 496  ASP A OD2    1 
ATOM   5302 H H      . ASP A 1 313 ? 42.738 44.562 48.858 1.00 19.00 ? 496  ASP A H      1 
ATOM   5303 H HA     . ASP A 1 313 ? 44.249 45.863 49.513 1.00 18.67 ? 496  ASP A HA     1 
ATOM   5304 H HB2    . ASP A 1 313 ? 43.565 47.467 47.306 1.00 21.65 ? 496  ASP A HB2    1 
ATOM   5305 H HB3    . ASP A 1 313 ? 44.870 47.684 48.186 1.00 21.65 ? 496  ASP A HB3    1 
ATOM   5306 N N      . ASN A 1 314 ? 42.054 46.921 50.870 1.00 15.20 ? 497  ASN A N      1 
ATOM   5307 C CA     . ASN A 1 314 ? 41.491 47.797 51.886 1.00 13.56 ? 497  ASN A CA     1 
ATOM   5308 C C      . ASN A 1 314 ? 41.585 47.071 53.218 1.00 12.82 ? 497  ASN A C      1 
ATOM   5309 O O      . ASN A 1 314 ? 40.860 46.094 53.455 1.00 12.30 ? 497  ASN A O      1 
ATOM   5310 C CB     . ASN A 1 314 ? 40.053 48.177 51.530 1.00 12.57 ? 497  ASN A CB     1 
ATOM   5311 C CG     . ASN A 1 314 ? 39.467 49.158 52.494 1.00 12.28 ? 497  ASN A CG     1 
ATOM   5312 O OD1    . ASN A 1 314 ? 39.524 48.977 53.716 1.00 12.78 ? 497  ASN A OD1    1 
ATOM   5313 N ND2    . ASN A 1 314 ? 38.899 50.250 51.957 1.00 13.49 ? 497  ASN A ND2    1 
ATOM   5314 H H      . ASN A 1 314 ? 41.753 46.116 50.894 1.00 18.24 ? 497  ASN A H      1 
ATOM   5315 H HA     . ASN A 1 314 ? 42.003 48.619 51.958 1.00 16.27 ? 497  ASN A HA     1 
ATOM   5316 H HB2    . ASN A 1 314 ? 40.040 48.578 50.646 1.00 15.09 ? 497  ASN A HB2    1 
ATOM   5317 H HB3    . ASN A 1 314 ? 39.502 47.378 51.540 1.00 15.09 ? 497  ASN A HB3    1 
ATOM   5318 H HD21   . ASN A 1 314 ? 38.547 50.847 52.467 1.00 16.19 ? 497  ASN A HD21   1 
ATOM   5319 H HD22   . ASN A 1 314 ? 38.887 50.354 51.104 1.00 16.19 ? 497  ASN A HD22   1 
ATOM   5320 N N      . LYS A 1 315 ? 42.490 47.537 54.062 1.00 13.41 ? 498  LYS A N      1 
ATOM   5321 C CA     . LYS A 1 315 ? 42.763 46.873 55.322 1.00 14.52 ? 498  LYS A CA     1 
ATOM   5322 C C      . LYS A 1 315 ? 41.556 46.859 56.248 1.00 13.47 ? 498  LYS A C      1 
ATOM   5323 O O      . LYS A 1 315 ? 41.362 45.899 57.007 1.00 13.75 ? 498  LYS A O      1 
ATOM   5324 C CB     . LYS A 1 315 ? 43.926 47.607 56.002 1.00 18.72 ? 498  LYS A CB     1 
ATOM   5325 C CG     . LYS A 1 315 ? 44.316 47.097 57.352 1.00 23.21 ? 498  LYS A CG     1 
ATOM   5326 C CD     . LYS A 1 315 ? 45.569 47.851 57.889 1.00 28.41 ? 498  LYS A CD     1 
ATOM   5327 C CE     . LYS A 1 315 ? 46.683 48.022 56.833 1.00 35.67 ? 498  LYS A CE     1 
ATOM   5328 N NZ     . LYS A 1 315 ? 46.948 46.852 55.934 1.00 40.27 ? 498  LYS A NZ     1 
ATOM   5329 H H      . LYS A 1 315 ? 42.965 48.242 53.928 1.00 16.09 ? 498  LYS A H      1 
ATOM   5330 H HA     . LYS A 1 315 ? 42.998 45.948 55.147 1.00 17.43 ? 498  LYS A HA     1 
ATOM   5331 H HB2    . LYS A 1 315 ? 44.707 47.535 55.430 1.00 22.47 ? 498  LYS A HB2    1 
ATOM   5332 H HB3    . LYS A 1 315 ? 43.677 48.539 56.107 1.00 22.47 ? 498  LYS A HB3    1 
ATOM   5333 H HG2    . LYS A 1 315 ? 43.585 47.234 57.974 1.00 27.86 ? 498  LYS A HG2    1 
ATOM   5334 H HG3    . LYS A 1 315 ? 44.528 46.152 57.292 1.00 27.86 ? 498  LYS A HG3    1 
ATOM   5335 H HD2    . LYS A 1 315 ? 45.301 48.735 58.183 1.00 34.09 ? 498  LYS A HD2    1 
ATOM   5336 H HD3    . LYS A 1 315 ? 45.940 47.352 58.633 1.00 34.09 ? 498  LYS A HD3    1 
ATOM   5337 H HE2    . LYS A 1 315 ? 46.443 48.768 56.262 1.00 42.81 ? 498  LYS A HE2    1 
ATOM   5338 H HE3    . LYS A 1 315 ? 47.511 48.213 57.299 1.00 42.81 ? 498  LYS A HE3    1 
ATOM   5339 H HZ1    . LYS A 1 315 ? 47.623 47.038 55.384 1.00 48.33 ? 498  LYS A HZ1    1 
ATOM   5340 H HZ2    . LYS A 1 315 ? 47.159 46.137 56.419 1.00 48.33 ? 498  LYS A HZ2    1 
ATOM   5341 H HZ3    . LYS A 1 315 ? 46.224 46.670 55.450 1.00 48.33 ? 498  LYS A HZ3    1 
ATOM   5342 N N      . ALA A 1 316 ? 40.750 47.923 56.235 1.00 12.15 ? 499  ALA A N      1 
ATOM   5343 C CA     . ALA A 1 316 ? 39.571 47.949 57.084 1.00 12.09 ? 499  ALA A CA     1 
ATOM   5344 C C      . ALA A 1 316 ? 38.542 46.917 56.627 1.00 12.10 ? 499  ALA A C      1 
ATOM   5345 O O      . ALA A 1 316 ? 37.896 46.271 57.442 1.00 12.43 ? 499  ALA A O      1 
ATOM   5346 C CB     . ALA A 1 316 ? 38.948 49.356 57.114 1.00 13.18 ? 499  ALA A CB     1 
ATOM   5347 H H      . ALA A 1 316 ? 40.865 48.626 55.753 1.00 14.58 ? 499  ALA A H      1 
ATOM   5348 H HA     . ALA A 1 316 ? 39.841 47.731 57.989 1.00 14.51 ? 499  ALA A HA     1 
ATOM   5349 H HB1    . ALA A 1 316 ? 38.186 49.352 57.714 1.00 15.81 ? 499  ALA A HB1    1 
ATOM   5350 H HB2    . ALA A 1 316 ? 39.613 49.989 57.429 1.00 15.81 ? 499  ALA A HB2    1 
ATOM   5351 H HB3    . ALA A 1 316 ? 38.663 49.595 56.218 1.00 15.81 ? 499  ALA A HB3    1 
ATOM   5352 N N      . TYR A 1 317 ? 38.347 46.791 55.323 1.00 11.14 ? 500  TYR A N      1 
ATOM   5353 C CA     . TYR A 1 317 ? 37.470 45.740 54.816 1.00 10.83 ? 500  TYR A CA     1 
ATOM   5354 C C      . TYR A 1 317 ? 37.989 44.367 55.226 1.00 11.26 ? 500  TYR A C      1 
ATOM   5355 O O      . TYR A 1 317 ? 37.212 43.505 55.634 1.00 11.36 ? 500  TYR A O      1 
ATOM   5356 C CB     . TYR A 1 317 ? 37.347 45.871 53.300 1.00 11.85 ? 500  TYR A CB     1 
ATOM   5357 C CG     . TYR A 1 317 ? 36.476 44.799 52.673 1.00 11.43 ? 500  TYR A CG     1 
ATOM   5358 C CD1    . TYR A 1 317 ? 37.011 43.564 52.376 1.00 11.98 ? 500  TYR A CD1    1 
ATOM   5359 C CD2    . TYR A 1 317 ? 35.126 44.989 52.432 1.00 11.84 ? 500  TYR A CD2    1 
ATOM   5360 C CE1    . TYR A 1 317 ? 36.250 42.556 51.826 1.00 11.73 ? 500  TYR A CE1    1 
ATOM   5361 C CE2    . TYR A 1 317 ? 34.343 43.983 51.833 1.00 12.12 ? 500  TYR A CE2    1 
ATOM   5362 C CZ     . TYR A 1 317 ? 34.927 42.753 51.571 1.00 12.05 ? 500  TYR A CZ     1 
ATOM   5363 O OH     . TYR A 1 317 ? 34.193 41.735 51.042 1.00 14.24 ? 500  TYR A OH     1 
ATOM   5364 H H      . TYR A 1 317 ? 38.703 47.290 54.719 1.00 13.37 ? 500  TYR A H      1 
ATOM   5365 H HA     . TYR A 1 317 ? 36.581 45.840 55.190 1.00 13.00 ? 500  TYR A HA     1 
ATOM   5366 H HB2    . TYR A 1 317 ? 36.956 46.733 53.091 1.00 14.22 ? 500  TYR A HB2    1 
ATOM   5367 H HB3    . TYR A 1 317 ? 38.231 45.803 52.907 1.00 14.22 ? 500  TYR A HB3    1 
ATOM   5368 H HD1    . TYR A 1 317 ? 37.910 43.407 52.551 1.00 14.37 ? 500  TYR A HD1    1 
ATOM   5369 H HD2    . TYR A 1 317 ? 34.728 45.795 52.671 1.00 14.21 ? 500  TYR A HD2    1 
ATOM   5370 H HE1    . TYR A 1 317 ? 36.641 41.736 51.629 1.00 14.08 ? 500  TYR A HE1    1 
ATOM   5371 H HE2    . TYR A 1 317 ? 33.452 44.141 51.618 1.00 14.55 ? 500  TYR A HE2    1 
ATOM   5372 H HH     . TYR A 1 317 ? 33.409 41.995 50.889 1.00 17.09 ? 500  TYR A HH     1 
ATOM   5373 N N      . TYR A 1 318 ? 39.294 44.136 55.076 1.00 11.06 ? 501  TYR A N      1 
ATOM   5374 C CA     . TYR A 1 318 ? 39.845 42.830 55.455 1.00 10.97 ? 501  TYR A CA     1 
ATOM   5375 C C      . TYR A 1 318 ? 39.561 42.563 56.931 1.00 11.12 ? 501  TYR A C      1 
ATOM   5376 O O      . TYR A 1 318 ? 39.155 41.453 57.307 1.00 11.77 ? 501  TYR A O      1 
ATOM   5377 C CB     . TYR A 1 318 ? 41.353 42.778 55.220 1.00 11.80 ? 501  TYR A CB     1 
ATOM   5378 C CG     . TYR A 1 318 ? 41.857 42.860 53.807 1.00 11.75 ? 501  TYR A CG     1 
ATOM   5379 C CD1    . TYR A 1 318 ? 41.039 42.669 52.689 1.00 11.87 ? 501  TYR A CD1    1 
ATOM   5380 C CD2    . TYR A 1 318 ? 43.197 43.115 53.567 1.00 13.71 ? 501  TYR A CD2    1 
ATOM   5381 C CE1    . TYR A 1 318 ? 41.539 42.738 51.434 1.00 12.98 ? 501  TYR A CE1    1 
ATOM   5382 C CE2    . TYR A 1 318 ? 43.698 43.137 52.306 1.00 14.17 ? 501  TYR A CE2    1 
ATOM   5383 C CZ     . TYR A 1 318 ? 42.875 42.938 51.237 1.00 13.50 ? 501  TYR A CZ     1 
ATOM   5384 O OH     . TYR A 1 318 ? 43.333 42.906 49.950 1.00 14.69 ? 501  TYR A OH     1 
ATOM   5385 H H      . TYR A 1 318 ? 39.866 44.699 54.767 1.00 13.28 ? 501  TYR A H      1 
ATOM   5386 H HA     . TYR A 1 318 ? 39.433 42.150 54.899 1.00 13.17 ? 501  TYR A HA     1 
ATOM   5387 H HB2    . TYR A 1 318 ? 41.751 43.521 55.700 1.00 14.16 ? 501  TYR A HB2    1 
ATOM   5388 H HB3    . TYR A 1 318 ? 41.677 41.938 55.581 1.00 14.16 ? 501  TYR A HB3    1 
ATOM   5389 H HD1    . TYR A 1 318 ? 40.135 42.491 52.810 1.00 14.25 ? 501  TYR A HD1    1 
ATOM   5390 H HD2    . TYR A 1 318 ? 43.766 43.274 54.286 1.00 16.45 ? 501  TYR A HD2    1 
ATOM   5391 H HE1    . TYR A 1 318 ? 40.971 42.649 50.704 1.00 15.57 ? 501  TYR A HE1    1 
ATOM   5392 H HE2    . TYR A 1 318 ? 44.605 43.289 52.171 1.00 17.00 ? 501  TYR A HE2    1 
ATOM   5393 H HH     . TYR A 1 318 ? 44.165 43.017 49.938 1.00 17.63 ? 501  TYR A HH     1 
ATOM   5394 N N      . ASP A 1 319 ? 39.834 43.554 57.800 1.00 12.08 ? 502  ASP A N      1 
ATOM   5395 C CA     . ASP A 1 319 ? 39.572 43.365 59.216 1.00 13.02 ? 502  ASP A CA     1 
ATOM   5396 C C      . ASP A 1 319 ? 38.090 43.075 59.475 1.00 12.34 ? 502  ASP A C      1 
ATOM   5397 O O      . ASP A 1 319 ? 37.750 42.190 60.284 1.00 13.26 ? 502  ASP A O      1 
ATOM   5398 C CB     . ASP A 1 319 ? 40.001 44.595 60.027 1.00 13.62 ? 502  ASP A CB     1 
ATOM   5399 C CG     . ASP A 1 319 ? 41.515 44.815 60.080 1.00 16.22 ? 502  ASP A CG     1 
ATOM   5400 O OD1    . ASP A 1 319 ? 42.292 43.916 59.741 1.00 17.51 ? 502  ASP A OD1    1 
ATOM   5401 O OD2    . ASP A 1 319 ? 41.913 45.941 60.481 1.00 18.39 ? 502  ASP A OD2    1 
ATOM   5402 H H      . ASP A 1 319 ? 40.162 44.320 57.591 1.00 14.50 ? 502  ASP A H      1 
ATOM   5403 H HA     . ASP A 1 319 ? 40.101 42.607 59.511 1.00 15.62 ? 502  ASP A HA     1 
ATOM   5404 H HB2    . ASP A 1 319 ? 39.603 45.384 59.627 1.00 16.34 ? 502  ASP A HB2    1 
ATOM   5405 H HB3    . ASP A 1 319 ? 39.687 44.491 60.939 1.00 16.34 ? 502  ASP A HB3    1 
ATOM   5406 N N      . SER A 1 320 ? 37.194 43.864 58.859 1.00 11.78 ? 503  SER A N      1 
ATOM   5407 C CA     . SER A 1 320 ? 35.765 43.670 59.113 1.00 11.45 ? 503  SER A CA     1 
ATOM   5408 C C      . SER A 1 320 ? 35.288 42.323 58.595 1.00 12.28 ? 503  SER A C      1 
ATOM   5409 O O      . SER A 1 320 ? 34.494 41.648 59.251 1.00 12.70 ? 503  SER A O      1 
ATOM   5410 C CB     . SER A 1 320 ? 34.961 44.748 58.408 1.00 13.23 ? 503  SER A CB     1 
ATOM   5411 O OG     . SER A 1 320 ? 35.220 46.036 59.003 1.00 15.46 ? 503  SER A OG     1 
ATOM   5412 H H      . SER A 1 320 ? 37.384 44.497 58.308 1.00 14.14 ? 503  SER A H      1 
ATOM   5413 H HA     . SER A 1 320 ? 35.624 43.724 60.071 1.00 13.74 ? 503  SER A HA     1 
ATOM   5414 H HB2    . SER A 1 320 ? 35.215 44.773 57.472 1.00 15.87 ? 503  SER A HB2    1 
ATOM   5415 H HB3    . SER A 1 320 ? 34.016 44.544 58.490 1.00 15.87 ? 503  SER A HB3    1 
ATOM   5416 H HG     . SER A 1 320 ? 35.074 46.005 59.830 1.00 18.55 ? 503  SER A HG     1 
ATOM   5417 N N      . CYS A 1 321 ? 35.781 41.916 57.435 1.00 11.55 ? 504  CYS A N      1 
ATOM   5418 C CA     . CYS A 1 321 ? 35.352 40.629 56.879 1.00 11.49 ? 504  CYS A CA     1 
ATOM   5419 C C      . CYS A 1 321 ? 35.771 39.487 57.798 1.00 11.10 ? 504  CYS A C      1 
ATOM   5420 O O      . CYS A 1 321 ? 34.981 38.592 58.082 1.00 11.34 ? 504  CYS A O      1 
ATOM   5421 C CB     . CYS A 1 321 ? 35.886 40.449 55.473 1.00 11.85 ? 504  CYS A CB     1 
ATOM   5422 S SG     . CYS A 1 321 ? 35.064 39.094 54.597 1.00 12.60 ? 504  CYS A SG     1 
ATOM   5423 H H      . CYS A 1 321 ? 36.351 42.350 56.958 1.00 13.85 ? 504  CYS A H      1 
ATOM   5424 H HA     . CYS A 1 321 ? 34.385 40.617 56.808 1.00 13.79 ? 504  CYS A HA     1 
ATOM   5425 H HB2    . CYS A 1 321 ? 35.741 41.266 54.970 1.00 14.22 ? 504  CYS A HB2    1 
ATOM   5426 H HB3    . CYS A 1 321 ? 36.834 40.250 55.516 1.00 14.22 ? 504  CYS A HB3    1 
ATOM   5427 H HG     . CYS A 1 321 ? 35.579 38.954 53.523 1.00 15.12 ? 504  CYS A HG     1 
ATOM   5428 N N      . ALA A 1 322 ? 37.019 39.510 58.265 1.00 11.23 ? 505  ALA A N      1 
ATOM   5429 C CA     . ALA A 1 322 ? 37.463 38.478 59.206 1.00 12.15 ? 505  ALA A CA     1 
ATOM   5430 C C      . ALA A 1 322 ? 36.614 38.496 60.472 1.00 12.41 ? 505  ALA A C      1 
ATOM   5431 O O      . ALA A 1 322 ? 36.212 37.445 60.982 1.00 13.51 ? 505  ALA A O      1 
ATOM   5432 C CB     . ALA A 1 322 ? 38.933 38.648 59.555 1.00 12.67 ? 505  ALA A CB     1 
ATOM   5433 H H      . ALA A 1 322 ? 37.614 40.096 58.060 1.00 13.47 ? 505  ALA A H      1 
ATOM   5434 H HA     . ALA A 1 322 ? 37.367 37.615 58.775 1.00 14.58 ? 505  ALA A HA     1 
ATOM   5435 H HB1    . ALA A 1 322 ? 39.212 37.908 60.116 1.00 15.20 ? 505  ALA A HB1    1 
ATOM   5436 H HB2    . ALA A 1 322 ? 39.453 38.657 58.737 1.00 15.20 ? 505  ALA A HB2    1 
ATOM   5437 H HB3    . ALA A 1 322 ? 39.050 39.486 60.030 1.00 15.20 ? 505  ALA A HB3    1 
ATOM   5438 N N      . ASN A 1 323 ? 36.339 39.693 61.014 1.00 12.31 ? 506  ASN A N      1 
ATOM   5439 C CA     A ASN A 1 323 ? 35.583 39.782 62.252 0.64 12.89 ? 506  ASN A CA     1 
ATOM   5440 C CA     B ASN A 1 323 ? 35.587 39.783 62.256 0.36 12.98 ? 506  ASN A CA     1 
ATOM   5441 C C      . ASN A 1 323 ? 34.165 39.276 62.086 1.00 12.64 ? 506  ASN A C      1 
ATOM   5442 O O      . ASN A 1 323 ? 33.653 38.573 62.957 1.00 13.28 ? 506  ASN A O      1 
ATOM   5443 C CB     A ASN A 1 323 ? 35.585 41.241 62.739 0.64 16.11 ? 506  ASN A CB     1 
ATOM   5444 C CB     B ASN A 1 323 ? 35.579 41.237 62.750 0.36 15.27 ? 506  ASN A CB     1 
ATOM   5445 C CG     A ASN A 1 323 ? 36.877 41.621 63.434 0.64 21.84 ? 506  ASN A CG     1 
ATOM   5446 C CG     B ASN A 1 323 ? 35.280 41.338 64.235 0.36 20.13 ? 506  ASN A CG     1 
ATOM   5447 O OD1    A ASN A 1 323 ? 37.649 40.763 63.868 0.64 24.04 ? 506  ASN A OD1    1 
ATOM   5448 O OD1    B ASN A 1 323 ? 35.684 40.470 65.012 0.36 23.11 ? 506  ASN A OD1    1 
ATOM   5449 N ND2    A ASN A 1 323 ? 37.114 42.908 63.543 0.64 24.24 ? 506  ASN A ND2    1 
ATOM   5450 N ND2    B ASN A 1 323 ? 34.573 42.380 64.637 0.36 22.18 ? 506  ASN A ND2    1 
ATOM   5451 H H      A ASN A 1 323 ? 36.577 40.450 60.684 0.64 14.77 ? 506  ASN A H      1 
ATOM   5452 H H      B ASN A 1 323 ? 36.575 40.450 60.682 0.36 14.77 ? 506  ASN A H      1 
ATOM   5453 H HA     A ASN A 1 323 ? 36.009 39.226 62.923 0.64 15.47 ? 506  ASN A HA     1 
ATOM   5454 H HA     B ASN A 1 323 ? 36.022 39.231 62.924 0.36 15.58 ? 506  ASN A HA     1 
ATOM   5455 H HB2    A ASN A 1 323 ? 35.469 41.829 61.977 0.64 19.33 ? 506  ASN A HB2    1 
ATOM   5456 H HB2    B ASN A 1 323 ? 36.451 41.631 62.590 0.36 18.32 ? 506  ASN A HB2    1 
ATOM   5457 H HB3    A ASN A 1 323 ? 34.858 41.365 63.368 0.64 19.33 ? 506  ASN A HB3    1 
ATOM   5458 H HB3    B ASN A 1 323 ? 34.897 41.732 62.270 0.36 18.32 ? 506  ASN A HB3    1 
ATOM   5459 H HD21   A ASN A 1 323 ? 37.832 43.182 63.928 0.64 29.09 ? 506  ASN A HD21   1 
ATOM   5460 H HD21   B ASN A 1 323 ? 34.381 42.474 65.470 0.36 26.61 ? 506  ASN A HD21   1 
ATOM   5461 H HD22   A ASN A 1 323 ? 36.551 43.478 63.229 0.64 29.09 ? 506  ASN A HD22   1 
ATOM   5462 H HD22   B ASN A 1 323 ? 34.304 42.963 64.066 0.36 26.61 ? 506  ASN A HD22   1 
ATOM   5463 N N      . ILE A 1 324 ? 33.512 39.639 60.983 1.00 11.66 ? 507  ILE A N      1 
ATOM   5464 C CA     . ILE A 1 324 ? 32.136 39.196 60.765 1.00 11.60 ? 507  ILE A CA     1 
ATOM   5465 C C      . ILE A 1 324 ? 32.085 37.680 60.493 1.00 11.86 ? 507  ILE A C      1 
ATOM   5466 O O      . ILE A 1 324 ? 31.224 36.977 61.024 1.00 13.45 ? 507  ILE A O      1 
ATOM   5467 C CB     . ILE A 1 324 ? 31.501 40.011 59.621 1.00 11.93 ? 507  ILE A CB     1 
ATOM   5468 C CG1    . ILE A 1 324 ? 31.367 41.501 60.030 1.00 14.68 ? 507  ILE A CG1    1 
ATOM   5469 C CG2    . ILE A 1 324 ? 30.175 39.431 59.262 1.00 12.80 ? 507  ILE A CG2    1 
ATOM   5470 C CD1    . ILE A 1 324 ? 31.110 42.435 58.847 1.00 14.42 ? 507  ILE A CD1    1 
ATOM   5471 H H      . ILE A 1 324 ? 33.836 40.131 60.357 1.00 14.00 ? 507  ILE A H      1 
ATOM   5472 H HA     . ILE A 1 324 ? 31.625 39.359 61.573 1.00 13.92 ? 507  ILE A HA     1 
ATOM   5473 H HB     . ILE A 1 324 ? 32.078 39.965 58.843 1.00 14.32 ? 507  ILE A HB     1 
ATOM   5474 H HG12   . ILE A 1 324 ? 30.624 41.591 60.647 1.00 17.62 ? 507  ILE A HG12   1 
ATOM   5475 H HG13   . ILE A 1 324 ? 32.190 41.783 60.458 1.00 17.62 ? 507  ILE A HG13   1 
ATOM   5476 H HG21   . ILE A 1 324 ? 29.751 40.000 58.601 1.00 15.36 ? 507  ILE A HG21   1 
ATOM   5477 H HG22   . ILE A 1 324 ? 30.308 38.542 58.897 1.00 15.36 ? 507  ILE A HG22   1 
ATOM   5478 H HG23   . ILE A 1 324 ? 29.625 39.383 60.059 1.00 15.36 ? 507  ILE A HG23   1 
ATOM   5479 H HD11   . ILE A 1 324 ? 31.029 43.344 59.175 1.00 17.31 ? 507  ILE A HD11   1 
ATOM   5480 H HD12   . ILE A 1 324 ? 31.854 42.372 58.228 1.00 17.31 ? 507  ILE A HD12   1 
ATOM   5481 H HD13   . ILE A 1 324 ? 30.289 42.167 58.406 1.00 17.31 ? 507  ILE A HD13   1 
ATOM   5482 N N      . LEU A 1 325 ? 33.003 37.161 59.672 1.00 10.77 ? 508  LEU A N      1 
ATOM   5483 C CA     . LEU A 1 325 ? 33.045 35.708 59.459 1.00 10.73 ? 508  LEU A CA     1 
ATOM   5484 C C      . LEU A 1 325 ? 33.320 34.983 60.762 1.00 11.60 ? 508  LEU A C      1 
ATOM   5485 O O      . LEU A 1 325 ? 32.683 33.974 61.049 1.00 12.51 ? 508  LEU A O      1 
ATOM   5486 C CB     . LEU A 1 325 ? 34.080 35.371 58.397 1.00 11.42 ? 508  LEU A CB     1 
ATOM   5487 C CG     . LEU A 1 325 ? 33.775 35.759 56.961 1.00 12.63 ? 508  LEU A CG     1 
ATOM   5488 C CD1    . LEU A 1 325 ? 34.920 35.456 55.996 1.00 14.49 ? 508  LEU A CD1    1 
ATOM   5489 C CD2    . LEU A 1 325 ? 32.489 35.057 56.504 1.00 14.37 ? 508  LEU A CD2    1 
ATOM   5490 H H      . LEU A 1 325 ? 33.594 37.611 59.240 1.00 12.92 ? 508  LEU A H      1 
ATOM   5491 H HA     . LEU A 1 325 ? 32.186 35.400 59.128 1.00 12.87 ? 508  LEU A HA     1 
ATOM   5492 H HB2    . LEU A 1 325 ? 34.906 35.819 58.638 1.00 13.71 ? 508  LEU A HB2    1 
ATOM   5493 H HB3    . LEU A 1 325 ? 34.210 34.410 58.405 1.00 13.71 ? 508  LEU A HB3    1 
ATOM   5494 H HG     . LEU A 1 325 ? 33.654 36.721 56.934 1.00 15.16 ? 508  LEU A HG     1 
ATOM   5495 H HD11   . LEU A 1 325 ? 34.669 35.749 55.106 1.00 17.38 ? 508  LEU A HD11   1 
ATOM   5496 H HD12   . LEU A 1 325 ? 35.714 35.930 56.289 1.00 17.38 ? 508  LEU A HD12   1 
ATOM   5497 H HD13   . LEU A 1 325 ? 35.087 34.501 55.995 1.00 17.38 ? 508  LEU A HD13   1 
ATOM   5498 H HD21   . LEU A 1 325 ? 32.381 35.185 55.549 1.00 17.25 ? 508  LEU A HD21   1 
ATOM   5499 H HD22   . LEU A 1 325 ? 32.558 34.110 56.705 1.00 17.25 ? 508  LEU A HD22   1 
ATOM   5500 H HD23   . LEU A 1 325 ? 31.734 35.441 56.977 1.00 17.25 ? 508  LEU A HD23   1 
ATOM   5501 N N      . ARG A 1 326 ? 34.248 35.489 61.551 1.00 10.58 ? 509  ARG A N      1 
ATOM   5502 C CA     . ARG A 1 326 ? 34.523 34.864 62.848 1.00 12.22 ? 509  ARG A CA     1 
ATOM   5503 C C      . ARG A 1 326 ? 33.266 34.762 63.707 1.00 12.69 ? 509  ARG A C      1 
ATOM   5504 O O      . ARG A 1 326 ? 32.941 33.683 64.228 1.00 13.95 ? 509  ARG A O      1 
ATOM   5505 C CB     . ARG A 1 326 ? 35.579 35.679 63.607 1.00 13.67 ? 509  ARG A CB     1 
ATOM   5506 C CG     . ARG A 1 326 ? 35.791 35.232 65.037 1.00 14.90 ? 509  ARG A CG     1 
ATOM   5507 C CD     . ARG A 1 326 ? 36.847 36.106 65.735 1.00 18.10 ? 509  ARG A CD     1 
ATOM   5508 N NE     . ARG A 1 326 ? 37.075 35.676 67.110 1.00 22.30 ? 509  ARG A NE     1 
ATOM   5509 C CZ     . ARG A 1 326 ? 36.284 35.943 68.142 1.00 24.13 ? 509  ARG A CZ     1 
ATOM   5510 N NH1    . ARG A 1 326 ? 35.269 36.795 68.039 1.00 24.59 ? 509  ARG A NH1    1 
ATOM   5511 N NH2    . ARG A 1 326 ? 36.516 35.338 69.310 1.00 25.10 ? 509  ARG A NH2    1 
ATOM   5512 H H      . ARG A 1 326 ? 34.727 36.180 61.371 1.00 12.70 ? 509  ARG A H      1 
ATOM   5513 H HA     . ARG A 1 326 ? 34.860 33.970 62.679 1.00 14.67 ? 509  ARG A HA     1 
ATOM   5514 H HB2    . ARG A 1 326 ? 36.427 35.597 63.143 1.00 16.40 ? 509  ARG A HB2    1 
ATOM   5515 H HB3    . ARG A 1 326 ? 35.300 36.608 63.626 1.00 16.40 ? 509  ARG A HB3    1 
ATOM   5516 H HG2    . ARG A 1 326 ? 34.957 35.307 65.527 1.00 17.88 ? 509  ARG A HG2    1 
ATOM   5517 H HG3    . ARG A 1 326 ? 36.100 34.312 65.046 1.00 17.88 ? 509  ARG A HG3    1 
ATOM   5518 H HD2    . ARG A 1 326 ? 37.686 36.043 65.253 1.00 21.72 ? 509  ARG A HD2    1 
ATOM   5519 H HD3    . ARG A 1 326 ? 36.541 37.026 65.751 1.00 21.72 ? 509  ARG A HD3    1 
ATOM   5520 H HE     . ARG A 1 326 ? 37.782 35.210 67.265 1.00 26.76 ? 509  ARG A HE     1 
ATOM   5521 H HH11   . ARG A 1 326 ? 35.112 37.188 67.291 1.00 29.51 ? 509  ARG A HH11   1 
ATOM   5522 H HH12   . ARG A 1 326 ? 34.769 36.953 68.721 1.00 29.51 ? 509  ARG A HH12   1 
ATOM   5523 H HH21   . ARG A 1 326 ? 37.171 34.785 69.385 1.00 30.12 ? 509  ARG A HH21   1 
ATOM   5524 H HH22   . ARG A 1 326 ? 36.012 35.501 69.987 1.00 30.12 ? 509  ARG A HH22   1 
ATOM   5525 N N      . SER A 1 327 ? 32.521 35.878 63.846 1.00 12.69 ? 510  SER A N      1 
ATOM   5526 C CA     A SER A 1 327 ? 31.313 35.860 64.666 0.47 13.19 ? 510  SER A CA     1 
ATOM   5527 C CA     B SER A 1 327 ? 31.316 35.857 64.668 0.26 12.49 ? 510  SER A CA     1 
ATOM   5528 C CA     C SER A 1 327 ? 31.317 35.857 64.667 0.27 13.35 ? 510  SER A CA     1 
ATOM   5529 C C      . SER A 1 327 ? 30.278 34.911 64.076 1.00 12.88 ? 510  SER A C      1 
ATOM   5530 O O      . SER A 1 327 ? 29.587 34.182 64.815 1.00 14.97 ? 510  SER A O      1 
ATOM   5531 C CB     A SER A 1 327 ? 30.711 37.272 64.795 0.47 15.47 ? 510  SER A CB     1 
ATOM   5532 C CB     B SER A 1 327 ? 30.744 37.276 64.797 0.26 13.20 ? 510  SER A CB     1 
ATOM   5533 C CB     C SER A 1 327 ? 30.745 37.274 64.792 0.27 15.43 ? 510  SER A CB     1 
ATOM   5534 O OG     A SER A 1 327 ? 31.555 38.109 65.539 0.47 17.42 ? 510  SER A OG     1 
ATOM   5535 O OG     B SER A 1 327 ? 30.640 37.885 63.527 0.26 14.58 ? 510  SER A OG     1 
ATOM   5536 O OG     C SER A 1 327 ? 29.675 37.301 65.717 0.27 17.38 ? 510  SER A OG     1 
ATOM   5537 H H      A SER A 1 327 ? 32.696 36.637 63.481 0.47 15.23 ? 510  SER A H      1 
ATOM   5538 H H      B SER A 1 327 ? 32.695 36.637 63.481 0.26 15.23 ? 510  SER A H      1 
ATOM   5539 H H      C SER A 1 327 ? 32.695 36.637 63.481 0.27 15.23 ? 510  SER A H      1 
ATOM   5540 H HA     A SER A 1 327 ? 31.555 35.560 65.556 0.47 15.83 ? 510  SER A HA     1 
ATOM   5541 H HA     B SER A 1 327 ? 31.542 35.545 65.558 0.26 14.99 ? 510  SER A HA     1 
ATOM   5542 H HA     C SER A 1 327 ? 31.543 35.545 65.557 0.27 16.02 ? 510  SER A HA     1 
ATOM   5543 H HB2    A SER A 1 327 ? 30.595 37.648 63.908 0.47 18.56 ? 510  SER A HB2    1 
ATOM   5544 H HB2    B SER A 1 327 ? 29.862 37.227 65.198 0.26 15.84 ? 510  SER A HB2    1 
ATOM   5545 H HB2    C SER A 1 327 ? 31.444 37.872 65.099 0.27 18.52 ? 510  SER A HB2    1 
ATOM   5546 H HB3    A SER A 1 327 ? 29.852 37.210 65.243 0.47 18.56 ? 510  SER A HB3    1 
ATOM   5547 H HB3    B SER A 1 327 ? 31.334 37.806 65.355 0.26 15.84 ? 510  SER A HB3    1 
ATOM   5548 H HB3    C SER A 1 327 ? 30.419 37.562 63.924 0.27 18.52 ? 510  SER A HB3    1 
ATOM   5549 H HG     A SER A 1 327 ? 32.282 38.220 65.132 0.47 20.91 ? 510  SER A HG     1 
ATOM   5550 H HG     B SER A 1 327 ? 30.145 37.426 63.027 0.26 17.50 ? 510  SER A HG     1 
ATOM   5551 H HG     C SER A 1 327 ? 29.948 37.069 66.477 0.27 20.85 ? 510  SER A HG     1 
ATOM   5552 N N      . THR A 1 328 ? 30.141 34.923 62.745 1.00 13.04 ? 511  THR A N      1 
ATOM   5553 C CA     . THR A 1 328 ? 29.165 34.062 62.079 1.00 12.96 ? 511  THR A CA     1 
ATOM   5554 C C      . THR A 1 328 ? 29.492 32.594 62.334 1.00 13.53 ? 511  THR A C      1 
ATOM   5555 O O      . THR A 1 328 ? 28.598 31.788 62.603 1.00 14.05 ? 511  THR A O      1 
ATOM   5556 C CB     . THR A 1 328 ? 29.177 34.371 60.582 1.00 13.63 ? 511  THR A CB     1 
ATOM   5557 O OG1    . THR A 1 328 ? 28.838 35.732 60.348 1.00 15.42 ? 511  THR A OG1    1 
ATOM   5558 C CG2    . THR A 1 328 ? 28.195 33.536 59.806 1.00 13.51 ? 511  THR A CG2    1 
ATOM   5559 H H      . THR A 1 328 ? 30.599 35.418 62.210 1.00 15.65 ? 511  THR A H      1 
ATOM   5560 H HA     . THR A 1 328 ? 28.274 34.234 62.420 1.00 15.55 ? 511  THR A HA     1 
ATOM   5561 H HB     . THR A 1 328 ? 30.073 34.173 60.269 1.00 16.35 ? 511  THR A HB     1 
ATOM   5562 H HG1    . THR A 1 328 ? 29.350 36.235 60.784 1.00 18.51 ? 511  THR A HG1    1 
ATOM   5563 H HG21   . THR A 1 328 ? 28.203 33.797 58.872 1.00 16.22 ? 511  THR A HG21   1 
ATOM   5564 H HG22   . THR A 1 328 ? 28.431 32.598 59.874 1.00 16.22 ? 511  THR A HG22   1 
ATOM   5565 H HG23   . THR A 1 328 ? 27.300 33.662 60.160 1.00 16.22 ? 511  THR A HG23   1 
ATOM   5566 N N      . PHE A 1 329 ? 30.769 32.229 62.243 1.00 13.13 ? 512  PHE A N      1 
ATOM   5567 C CA     . PHE A 1 329 ? 31.139 30.824 62.439 1.00 12.89 ? 512  PHE A CA     1 
ATOM   5568 C C      . PHE A 1 329 ? 31.031 30.414 63.886 1.00 14.44 ? 512  PHE A C      1 
ATOM   5569 O O      . PHE A 1 329 ? 30.670 29.276 64.164 1.00 15.05 ? 512  PHE A O      1 
ATOM   5570 C CB     . PHE A 1 329 ? 32.540 30.597 61.856 1.00 9.50  ? 512  PHE A CB     1 
ATOM   5571 C CG     . PHE A 1 329 ? 32.679 30.831 60.409 1.00 8.82  ? 512  PHE A CG     1 
ATOM   5572 C CD1    . PHE A 1 329 ? 31.555 30.778 59.514 1.00 11.64 ? 512  PHE A CD1    1 
ATOM   5573 C CD2    . PHE A 1 329 ? 33.895 31.091 59.687 1.00 6.66  ? 512  PHE A CD2    1 
ATOM   5574 C CE1    . PHE A 1 329 ? 31.735 30.973 58.143 1.00 11.83 ? 512  PHE A CE1    1 
ATOM   5575 C CE2    . PHE A 1 329 ? 34.125 31.267 58.386 1.00 8.09  ? 512  PHE A CE2    1 
ATOM   5576 C CZ     . PHE A 1 329 ? 33.009 31.235 57.569 1.00 12.73 ? 512  PHE A CZ     1 
ATOM   5577 H H      . PHE A 1 329 ? 31.425 32.758 62.073 1.00 15.76 ? 512  PHE A H      1 
ATOM   5578 H HA     . PHE A 1 329 ? 30.527 30.244 61.960 1.00 15.47 ? 512  PHE A HA     1 
ATOM   5579 H HB2    . PHE A 1 329 ? 33.156 31.197 62.305 1.00 11.40 ? 512  PHE A HB2    1 
ATOM   5580 H HB3    . PHE A 1 329 ? 32.793 29.676 62.024 1.00 11.40 ? 512  PHE A HB3    1 
ATOM   5581 H HD1    . PHE A 1 329 ? 30.704 30.613 59.850 1.00 13.97 ? 512  PHE A HD1    1 
ATOM   5582 H HD2    . PHE A 1 329 ? 34.654 31.147 60.222 1.00 8.00  ? 512  PHE A HD2    1 
ATOM   5583 H HE1    . PHE A 1 329 ? 30.993 30.929 57.584 1.00 14.20 ? 512  PHE A HE1    1 
ATOM   5584 H HE2    . PHE A 1 329 ? 34.981 31.402 58.049 1.00 9.71  ? 512  PHE A HE2    1 
ATOM   5585 H HZ     . PHE A 1 329 ? 33.091 31.384 56.655 1.00 15.28 ? 512  PHE A HZ     1 
ATOM   5586 N N      . ILE A 1 330 ? 31.426 31.275 64.808 1.00 13.78 ? 513  ILE A N      1 
ATOM   5587 C CA     . ILE A 1 330 ? 31.217 30.979 66.219 1.00 15.47 ? 513  ILE A CA     1 
ATOM   5588 C C      . ILE A 1 330 ? 29.748 30.696 66.502 1.00 17.44 ? 513  ILE A C      1 
ATOM   5589 O O      . ILE A 1 330 ? 29.410 29.745 67.219 1.00 19.64 ? 513  ILE A O      1 
ATOM   5590 C CB     . ILE A 1 330 ? 31.785 32.109 67.095 1.00 15.99 ? 513  ILE A CB     1 
ATOM   5591 C CG1    . ILE A 1 330 ? 33.319 32.030 67.092 1.00 16.60 ? 513  ILE A CG1    1 
ATOM   5592 C CG2    . ILE A 1 330 ? 31.266 32.016 68.469 1.00 18.11 ? 513  ILE A CG2    1 
ATOM   5593 C CD1    . ILE A 1 330 ? 34.005 33.259 67.664 1.00 17.75 ? 513  ILE A CD1    1 
ATOM   5594 H H      . ILE A 1 330 ? 31.812 32.027 64.650 1.00 16.54 ? 513  ILE A H      1 
ATOM   5595 H HA     . ILE A 1 330 ? 31.707 30.171 66.440 1.00 18.57 ? 513  ILE A HA     1 
ATOM   5596 H HB     . ILE A 1 330 ? 31.506 32.962 66.728 1.00 19.19 ? 513  ILE A HB     1 
ATOM   5597 H HG12   . ILE A 1 330 ? 33.592 31.267 67.625 1.00 19.93 ? 513  ILE A HG12   1 
ATOM   5598 H HG13   . ILE A 1 330 ? 33.623 31.922 66.177 1.00 19.93 ? 513  ILE A HG13   1 
ATOM   5599 H HG21   . ILE A 1 330 ? 31.714 32.676 69.022 1.00 21.74 ? 513  ILE A HG21   1 
ATOM   5600 H HG22   . ILE A 1 330 ? 30.311 32.188 68.458 1.00 21.74 ? 513  ILE A HG22   1 
ATOM   5601 H HG23   . ILE A 1 330 ? 31.437 31.125 68.813 1.00 21.74 ? 513  ILE A HG23   1 
ATOM   5602 H HD11   . ILE A 1 330 ? 34.966 33.129 67.630 1.00 21.30 ? 513  ILE A HD11   1 
ATOM   5603 H HD12   . ILE A 1 330 ? 33.758 34.034 67.134 1.00 21.30 ? 513  ILE A HD12   1 
ATOM   5604 H HD13   . ILE A 1 330 ? 33.720 33.382 68.583 1.00 21.30 ? 513  ILE A HD13   1 
ATOM   5605 N N      . GLU A 1 331 ? 28.851 31.516 65.954 1.00 18.04 ? 514  GLU A N      1 
ATOM   5606 C CA     . GLU A 1 331 ? 27.434 31.287 66.178 1.00 20.47 ? 514  GLU A CA     1 
ATOM   5607 C C      . GLU A 1 331 ? 26.986 29.998 65.507 1.00 19.99 ? 514  GLU A C      1 
ATOM   5608 O O      . GLU A 1 331 ? 26.168 29.250 66.064 1.00 22.60 ? 514  GLU A O      1 
ATOM   5609 C CB     . GLU A 1 331 ? 26.667 32.490 65.639 1.00 22.61 ? 514  GLU A CB     1 
ATOM   5610 C CG     . GLU A 1 331 ? 25.142 32.364 65.716 1.00 28.94 ? 514  GLU A CG     1 
ATOM   5611 C CD     . GLU A 1 331 ? 24.624 32.040 67.119 1.00 38.62 ? 514  GLU A CD     1 
ATOM   5612 O OE1    . GLU A 1 331 ? 25.077 32.711 68.087 1.00 41.41 ? 514  GLU A OE1    1 
ATOM   5613 O OE2    . GLU A 1 331 ? 23.762 31.117 67.240 1.00 41.53 ? 514  GLU A OE2    1 
ATOM   5614 H H      . GLU A 1 331 ? 29.037 32.195 65.461 1.00 21.65 ? 514  GLU A H      1 
ATOM   5615 H HA     . GLU A 1 331 ? 27.245 31.199 67.126 1.00 24.57 ? 514  GLU A HA     1 
ATOM   5616 H HB2    . GLU A 1 331 ? 26.922 33.273 66.152 1.00 27.13 ? 514  GLU A HB2    1 
ATOM   5617 H HB3    . GLU A 1 331 ? 26.903 32.613 64.706 1.00 27.13 ? 514  GLU A HB3    1 
ATOM   5618 H HG2    . GLU A 1 331 ? 24.744 33.205 65.440 1.00 34.73 ? 514  GLU A HG2    1 
ATOM   5619 H HG3    . GLU A 1 331 ? 24.856 31.652 65.123 1.00 34.73 ? 514  GLU A HG3    1 
ATOM   5620 N N      . ALA A 1 332 ? 27.510 29.723 64.314 1.00 18.20 ? 515  ALA A N      1 
ATOM   5621 C CA     . ALA A 1 332 ? 27.128 28.496 63.624 1.00 18.54 ? 515  ALA A CA     1 
ATOM   5622 C C      . ALA A 1 332 ? 27.559 27.282 64.426 1.00 21.01 ? 515  ALA A C      1 
ATOM   5623 O O      . ALA A 1 332 ? 26.797 26.320 64.560 1.00 22.73 ? 515  ALA A O      1 
ATOM   5624 C CB     . ALA A 1 332 ? 27.717 28.452 62.224 1.00 17.62 ? 515  ALA A CB     1 
ATOM   5625 H H      . ALA A 1 332 ? 28.074 30.217 63.894 1.00 21.84 ? 515  ALA A H      1 
ATOM   5626 H HA     . ALA A 1 332 ? 26.163 28.480 63.526 1.00 22.25 ? 515  ALA A HA     1 
ATOM   5627 H HB1    . ALA A 1 332 ? 27.454 27.622 61.797 1.00 21.14 ? 515  ALA A HB1    1 
ATOM   5628 H HB2    . ALA A 1 332 ? 27.379 29.206 61.716 1.00 21.14 ? 515  ALA A HB2    1 
ATOM   5629 H HB3    . ALA A 1 332 ? 28.683 28.501 62.286 1.00 21.14 ? 515  ALA A HB3    1 
ATOM   5630 N N      . LYS A 1 333 ? 28.750 27.342 65.023 1.00 21.45 ? 516  LYS A N      1 
ATOM   5631 C CA     . LYS A 1 333 ? 29.216 26.243 65.848 1.00 25.05 ? 516  LYS A CA     1 
ATOM   5632 C C      . LYS A 1 333 ? 28.348 26.068 67.097 1.00 27.89 ? 516  LYS A C      1 
ATOM   5633 O O      . LYS A 1 333 ? 28.045 24.937 67.491 1.00 29.58 ? 516  LYS A O      1 
ATOM   5634 C CB     . LYS A 1 333 ? 30.658 26.506 66.259 1.00 25.58 ? 516  LYS A CB     1 
ATOM   5635 C CG     . LYS A 1 333 ? 31.135 25.437 67.218 1.00 30.28 ? 516  LYS A CG     1 
ATOM   5636 C CD     . LYS A 1 333 ? 32.520 25.654 67.692 1.00 33.94 ? 516  LYS A CD     1 
ATOM   5637 C CE     . LYS A 1 333 ? 32.995 24.470 68.543 1.00 35.37 ? 516  LYS A CE     1 
ATOM   5638 N NZ     . LYS A 1 333 ? 34.422 24.642 68.864 1.00 37.80 ? 516  LYS A NZ     1 
ATOM   5639 H H      . LYS A 1 333 ? 29.297 28.002 64.964 1.00 25.74 ? 516  LYS A H      1 
ATOM   5640 H HA     . LYS A 1 333 ? 29.171 25.423 65.333 1.00 30.06 ? 516  LYS A HA     1 
ATOM   5641 H HB2    . LYS A 1 333 ? 31.227 26.495 65.474 1.00 30.69 ? 516  LYS A HB2    1 
ATOM   5642 H HB3    . LYS A 1 333 ? 30.718 27.368 66.700 1.00 30.69 ? 516  LYS A HB3    1 
ATOM   5643 H HG2    . LYS A 1 333 ? 30.553 25.428 67.994 1.00 36.34 ? 516  LYS A HG2    1 
ATOM   5644 H HG3    . LYS A 1 333 ? 31.105 24.577 66.771 1.00 36.34 ? 516  LYS A HG3    1 
ATOM   5645 H HD2    . LYS A 1 333 ? 33.113 25.743 66.930 1.00 40.73 ? 516  LYS A HD2    1 
ATOM   5646 H HD3    . LYS A 1 333 ? 32.555 26.457 68.235 1.00 40.73 ? 516  LYS A HD3    1 
ATOM   5647 H HE2    . LYS A 1 333 ? 32.489 24.435 69.370 1.00 42.45 ? 516  LYS A HE2    1 
ATOM   5648 H HE3    . LYS A 1 333 ? 32.882 23.643 68.049 1.00 42.45 ? 516  LYS A HE3    1 
ATOM   5649 H HZ1    . LYS A 1 333 ? 34.710 23.953 69.348 1.00 45.36 ? 516  LYS A HZ1    1 
ATOM   5650 H HZ2    . LYS A 1 333 ? 34.899 24.688 68.115 1.00 45.36 ? 516  LYS A HZ2    1 
ATOM   5651 H HZ3    . LYS A 1 333 ? 34.541 25.391 69.330 1.00 45.36 ? 516  LYS A HZ3    1 
ATOM   5652 N N      . LYS A 1 334 ? 27.976 27.172 67.750 1.00 31.34 ? 517  LYS A N      1 
ATOM   5653 C CA     . LYS A 1 334 ? 27.086 27.106 68.903 1.00 35.38 ? 517  LYS A CA     1 
ATOM   5654 C C      . LYS A 1 334 ? 25.797 26.389 68.544 1.00 37.26 ? 517  LYS A C      1 
ATOM   5655 O O      . LYS A 1 334 ? 25.335 25.516 69.281 1.00 39.06 ? 517  LYS A O      1 
ATOM   5656 C CB     . LYS A 1 334 ? 26.783 28.517 69.418 1.00 38.61 ? 517  LYS A CB     1 
ATOM   5657 C CG     . LYS A 1 334 ? 27.754 29.002 70.480 1.00 42.30 ? 517  LYS A CG     1 
ATOM   5658 C CD     . LYS A 1 334 ? 27.751 30.518 70.608 1.00 44.93 ? 517  LYS A CD     1 
ATOM   5659 C CE     . LYS A 1 334 ? 28.965 31.002 71.392 1.00 46.30 ? 517  LYS A CE     1 
ATOM   5660 N NZ     . LYS A 1 334 ? 29.014 32.486 71.475 1.00 47.10 ? 517  LYS A NZ     1 
ATOM   5661 H H      . LYS A 1 334 ? 28.226 27.969 67.544 1.00 37.61 ? 517  LYS A H      1 
ATOM   5662 H HA     . LYS A 1 334 ? 27.528 26.614 69.613 1.00 42.46 ? 517  LYS A HA     1 
ATOM   5663 H HB2    . LYS A 1 334 ? 26.826 29.136 68.672 1.00 46.33 ? 517  LYS A HB2    1 
ATOM   5664 H HB3    . LYS A 1 334 ? 25.894 28.524 69.804 1.00 46.33 ? 517  LYS A HB3    1 
ATOM   5665 H HG2    . LYS A 1 334 ? 27.502 28.625 71.338 1.00 50.76 ? 517  LYS A HG2    1 
ATOM   5666 H HG3    . LYS A 1 334 ? 28.652 28.720 70.245 1.00 50.76 ? 517  LYS A HG3    1 
ATOM   5667 H HD2    . LYS A 1 334 ? 27.777 30.917 69.724 1.00 53.92 ? 517  LYS A HD2    1 
ATOM   5668 H HD3    . LYS A 1 334 ? 26.951 30.802 71.076 1.00 53.92 ? 517  LYS A HD3    1 
ATOM   5669 H HE2    . LYS A 1 334 ? 28.925 30.648 72.294 1.00 55.56 ? 517  LYS A HE2    1 
ATOM   5670 H HE3    . LYS A 1 334 ? 29.773 30.696 70.951 1.00 55.56 ? 517  LYS A HE3    1 
ATOM   5671 H HZ1    . LYS A 1 334 ? 29.723 32.742 71.948 1.00 56.52 ? 517  LYS A HZ1    1 
ATOM   5672 H HZ2    . LYS A 1 334 ? 29.069 32.836 70.659 1.00 56.52 ? 517  LYS A HZ2    1 
ATOM   5673 H HZ3    . LYS A 1 334 ? 28.278 32.793 71.871 1.00 56.52 ? 517  LYS A HZ3    1 
ATOM   5674 N N      . LYS A 1 335 ? 25.198 26.737 67.407 1.00 38.43 ? 518  LYS A N      1 
ATOM   5675 C CA     . LYS A 1 335 ? 23.968 26.058 67.019 1.00 42.31 ? 518  LYS A CA     1 
ATOM   5676 C C      . LYS A 1 335 ? 24.194 24.562 66.858 1.00 43.86 ? 518  LYS A C      1 
ATOM   5677 O O      . LYS A 1 335 ? 23.341 23.754 67.237 1.00 44.87 ? 518  LYS A O      1 
ATOM   5678 C CB     . LYS A 1 335 ? 23.403 26.661 65.739 1.00 45.29 ? 518  LYS A CB     1 
ATOM   5679 C CG     . LYS A 1 335 ? 22.688 27.974 65.962 1.00 49.30 ? 518  LYS A CG     1 
ATOM   5680 C CD     . LYS A 1 335 ? 22.105 28.489 64.658 1.00 53.06 ? 518  LYS A CD     1 
ATOM   5681 C CE     . LYS A 1 335 ? 21.856 29.982 64.722 1.00 56.16 ? 518  LYS A CE     1 
ATOM   5682 N NZ     . LYS A 1 335 ? 21.023 30.319 65.906 1.00 58.40 ? 518  LYS A NZ     1 
ATOM   5683 H H      . LYS A 1 335 ? 25.474 27.342 66.862 1.00 46.12 ? 518  LYS A H      1 
ATOM   5684 H HA     . LYS A 1 335 ? 23.309 26.190 67.718 1.00 50.77 ? 518  LYS A HA     1 
ATOM   5685 H HB2    . LYS A 1 335 ? 24.132 26.820 65.119 1.00 54.35 ? 518  LYS A HB2    1 
ATOM   5686 H HB3    . LYS A 1 335 ? 22.768 26.038 65.352 1.00 54.35 ? 518  LYS A HB3    1 
ATOM   5687 H HG2    . LYS A 1 335 ? 21.965 27.847 66.596 1.00 59.16 ? 518  LYS A HG2    1 
ATOM   5688 H HG3    . LYS A 1 335 ? 23.315 28.632 66.302 1.00 59.16 ? 518  LYS A HG3    1 
ATOM   5689 H HD2    . LYS A 1 335 ? 22.727 28.313 63.935 1.00 63.68 ? 518  LYS A HD2    1 
ATOM   5690 H HD3    . LYS A 1 335 ? 21.260 28.045 64.485 1.00 63.68 ? 518  LYS A HD3    1 
ATOM   5691 H HE2    . LYS A 1 335 ? 22.702 30.450 64.795 1.00 67.39 ? 518  LYS A HE2    1 
ATOM   5692 H HE3    . LYS A 1 335 ? 21.387 30.268 63.922 1.00 67.39 ? 518  LYS A HE3    1 
ATOM   5693 H HZ1    . LYS A 1 335 ? 20.854 31.192 65.921 1.00 70.08 ? 518  LYS A HZ1    1 
ATOM   5694 H HZ2    . LYS A 1 335 ? 20.252 29.876 65.872 1.00 70.08 ? 518  LYS A HZ2    1 
ATOM   5695 H HZ3    . LYS A 1 335 ? 21.451 30.094 66.653 1.00 70.08 ? 518  LYS A HZ3    1 
ATOM   5696 N N      . MET A 1 336 ? 25.339 24.163 66.315 1.00 43.96 ? 519  MET A N      1 
ATOM   5697 C CA     . MET A 1 336 ? 25.578 22.733 66.187 1.00 44.45 ? 519  MET A CA     1 
ATOM   5698 C C      . MET A 1 336 ? 26.064 22.119 67.496 1.00 47.54 ? 519  MET A C      1 
ATOM   5699 O O      . MET A 1 336 ? 25.677 20.994 67.838 1.00 52.36 ? 519  MET A O      1 
ATOM   5700 C CB     . MET A 1 336 ? 26.622 22.446 65.114 1.00 42.04 ? 519  MET A CB     1 
ATOM   5701 C CG     . MET A 1 336 ? 26.741 23.449 64.025 1.00 42.31 ? 519  MET A CG     1 
ATOM   5702 S SD     . MET A 1 336 ? 27.931 22.843 62.816 1.00 43.45 ? 519  MET A SD     1 
ATOM   5703 C CE     . MET A 1 336 ? 28.400 24.335 61.962 1.00 37.44 ? 519  MET A CE     1 
ATOM   5704 H H      . MET A 1 336 ? 25.965 24.676 66.025 1.00 52.76 ? 519  MET A H      1 
ATOM   5705 H HA     . MET A 1 336 ? 24.737 22.331 65.920 1.00 53.34 ? 519  MET A HA     1 
ATOM   5706 H HB2    . MET A 1 336 ? 27.489 22.389 65.545 1.00 50.45 ? 519  MET A HB2    1 
ATOM   5707 H HB3    . MET A 1 336 ? 26.401 21.598 64.698 1.00 50.45 ? 519  MET A HB3    1 
ATOM   5708 H HG2    . MET A 1 336 ? 25.882 23.571 63.591 1.00 50.78 ? 519  MET A HG2    1 
ATOM   5709 H HG3    . MET A 1 336 ? 27.054 24.294 64.384 1.00 50.78 ? 519  MET A HG3    1 
ATOM   5710 H HE1    . MET A 1 336 ? 29.055 24.116 61.280 1.00 44.93 ? 519  MET A HE1    1 
ATOM   5711 H HE2    . MET A 1 336 ? 27.613 24.724 61.551 1.00 44.93 ? 519  MET A HE2    1 
ATOM   5712 H HE3    . MET A 1 336 ? 28.783 24.957 62.600 1.00 44.93 ? 519  MET A HE3    1 
ATOM   5713 N N      . ASP A 1 337 ? 26.934 22.833 68.214 1.00 44.13 ? 520  ASP A N      1 
ATOM   5714 C CA     . ASP A 1 337 ? 27.573 22.340 69.435 1.00 39.60 ? 520  ASP A CA     1 
ATOM   5715 C C      . ASP A 1 337 ? 27.197 23.201 70.622 1.00 38.74 ? 520  ASP A C      1 
ATOM   5716 O O      . ASP A 1 337 ? 28.078 23.831 71.227 1.00 40.81 ? 520  ASP A O      1 
ATOM   5717 C CB     . ASP A 1 337 ? 29.101 22.369 69.290 1.00 37.96 ? 520  ASP A CB     1 
ATOM   5718 C CG     . ASP A 1 337 ? 29.578 21.497 68.166 1.00 40.07 ? 520  ASP A CG     1 
ATOM   5719 O OD1    . ASP A 1 337 ? 28.767 20.637 67.740 1.00 41.50 ? 520  ASP A OD1    1 
ATOM   5720 O OD2    . ASP A 1 337 ? 30.737 21.653 67.708 1.00 42.68 ? 520  ASP A OD2    1 
ATOM   5721 H H      . ASP A 1 337 ? 27.179 23.631 68.008 1.00 52.95 ? 520  ASP A H      1 
ATOM   5722 H HA     . ASP A 1 337 ? 27.280 21.428 69.590 1.00 47.52 ? 520  ASP A HA     1 
ATOM   5723 H HB2    . ASP A 1 337 ? 29.386 23.279 69.110 1.00 45.56 ? 520  ASP A HB2    1 
ATOM   5724 H HB3    . ASP A 1 337 ? 29.505 22.052 70.112 1.00 45.56 ? 520  ASP A HB3    1 
HETATM 5725 P PB     . ADP B 2 .   ? 29.468 46.064 34.797 1.00 49.05 ? 600  ADP A PB     1 
HETATM 5726 O O1B    . ADP B 2 .   ? 28.572 44.950 35.302 1.00 51.90 ? 600  ADP A O1B    1 
HETATM 5727 O O2B    . ADP B 2 .   ? 30.663 45.573 34.011 1.00 51.58 ? 600  ADP A O2B    1 
HETATM 5728 O O3B    . ADP B 2 .   ? 29.747 47.197 35.764 1.00 51.38 ? 600  ADP A O3B    1 
HETATM 5729 P PA     . ADP B 2 .   ? 27.537 46.181 32.658 1.00 31.16 ? 600  ADP A PA     1 
HETATM 5730 O O1A    . ADP B 2 .   ? 26.492 45.356 33.401 1.00 34.40 ? 600  ADP A O1A    1 
HETATM 5731 O O2A    . ADP B 2 .   ? 28.373 45.529 31.560 1.00 30.14 ? 600  ADP A O2A    1 
HETATM 5732 O O3A    . ADP B 2 .   ? 28.622 46.833 33.668 1.00 37.96 ? 600  ADP A O3A    1 
HETATM 5733 O "O5'"  . ADP B 2 .   ? 26.785 47.523 32.198 1.00 26.05 ? 600  ADP A "O5'"  1 
HETATM 5734 C "C5'"  . ADP B 2 .   ? 27.421 48.407 31.310 1.00 23.44 ? 600  ADP A "C5'"  1 
HETATM 5735 C "C4'"  . ADP B 2 .   ? 27.202 49.812 31.795 1.00 20.06 ? 600  ADP A "C4'"  1 
HETATM 5736 O "O4'"  . ADP B 2 .   ? 25.819 50.148 31.626 1.00 18.91 ? 600  ADP A "O4'"  1 
HETATM 5737 C "C3'"  . ADP B 2 .   ? 27.551 50.064 33.260 1.00 20.88 ? 600  ADP A "C3'"  1 
HETATM 5738 O "O3'"  . ADP B 2 .   ? 28.287 51.280 33.317 1.00 22.60 ? 600  ADP A "O3'"  1 
HETATM 5739 C "C2'"  . ADP B 2 .   ? 26.195 50.251 33.933 1.00 20.00 ? 600  ADP A "C2'"  1 
HETATM 5740 O "O2'"  . ADP B 2 .   ? 26.163 51.182 35.021 1.00 23.49 ? 600  ADP A "O2'"  1 
HETATM 5741 C "C1'"  . ADP B 2 .   ? 25.334 50.793 32.799 1.00 18.38 ? 600  ADP A "C1'"  1 
HETATM 5742 N N9     . ADP B 2 .   ? 23.894 50.566 32.906 1.00 16.34 ? 600  ADP A N9     1 
HETATM 5743 C C8     . ADP B 2 .   ? 23.299 49.367 32.853 1.00 15.93 ? 600  ADP A C8     1 
HETATM 5744 N N7     . ADP B 2 .   ? 21.999 49.521 32.959 1.00 15.09 ? 600  ADP A N7     1 
HETATM 5745 C C5     . ADP B 2 .   ? 21.724 50.831 33.017 1.00 14.39 ? 600  ADP A C5     1 
HETATM 5746 C C6     . ADP B 2 .   ? 20.517 51.626 33.077 1.00 14.40 ? 600  ADP A C6     1 
HETATM 5747 N N6     . ADP B 2 .   ? 19.313 51.033 33.115 1.00 15.40 ? 600  ADP A N6     1 
HETATM 5748 N N1     . ADP B 2 .   ? 20.627 52.957 33.064 1.00 14.72 ? 600  ADP A N1     1 
HETATM 5749 C C2     . ADP B 2 .   ? 21.839 53.543 33.053 1.00 14.79 ? 600  ADP A C2     1 
HETATM 5750 N N3     . ADP B 2 .   ? 23.015 52.884 32.980 1.00 15.49 ? 600  ADP A N3     1 
HETATM 5751 C C4     . ADP B 2 .   ? 22.981 51.547 32.952 1.00 14.86 ? 600  ADP A C4     1 
HETATM 5752 H "H5'1" . ADP B 2 .   ? 28.490 48.188 31.264 1.00 28.13 ? 600  ADP A "H5'1" 1 
HETATM 5753 H "H5'2" . ADP B 2 .   ? 27.010 48.289 30.305 1.00 28.13 ? 600  ADP A "H5'2" 1 
HETATM 5754 H "H4'"  . ADP B 2 .   ? 27.880 50.433 31.194 1.00 24.08 ? 600  ADP A "H4'"  1 
HETATM 5755 H "H3'"  . ADP B 2 .   ? 28.145 49.269 33.732 1.00 25.05 ? 600  ADP A "H3'"  1 
HETATM 5756 H "H2'"  . ADP B 2 .   ? 25.872 49.307 34.394 1.00 24.01 ? 600  ADP A "H2'"  1 
HETATM 5757 H "HO2'" . ADP B 2 .   ? 26.677 50.832 35.761 1.00 28.19 ? 600  ADP A "HO2'" 1 
HETATM 5758 H "H1'"  . ADP B 2 .   ? 25.434 51.887 32.819 1.00 22.05 ? 600  ADP A "H1'"  1 
HETATM 5759 H H8     . ADP B 2 .   ? 23.809 48.419 32.739 1.00 19.12 ? 600  ADP A H8     1 
HETATM 5760 H HN61   . ADP B 2 .   ? 18.482 51.579 33.189 1.00 18.48 ? 600  ADP A HN61   1 
HETATM 5761 H HN62   . ADP B 2 .   ? 19.263 50.037 33.090 1.00 18.48 ? 600  ADP A HN62   1 
HETATM 5762 H H2     . ADP B 2 .   ? 21.873 54.625 33.107 1.00 17.75 ? 600  ADP A H2     1 
HETATM 5763 C C1     . EDO C 3 .   ? 13.820 63.748 15.598 1.00 38.70 ? 601  EDO A C1     1 
HETATM 5764 O O1     . EDO C 3 .   ? 13.028 63.855 16.754 1.00 34.21 ? 601  EDO A O1     1 
HETATM 5765 C C2     . EDO C 3 .   ? 15.212 64.279 15.774 1.00 42.07 ? 601  EDO A C2     1 
HETATM 5766 O O2     . EDO C 3 .   ? 15.124 65.652 15.613 1.00 41.72 ? 601  EDO A O2     1 
HETATM 5767 H H11    . EDO C 3 .   ? 13.891 62.821 15.320 1.00 46.44 ? 601  EDO A H11    1 
HETATM 5768 H H12    . EDO C 3 .   ? 13.412 64.230 14.861 1.00 46.44 ? 601  EDO A H12    1 
HETATM 5769 H HO1    . EDO C 3 .   ? 12.253 63.558 16.572 1.00 41.05 ? 601  EDO A HO1    1 
HETATM 5770 H H21    . EDO C 3 .   ? 15.794 63.856 15.124 1.00 50.48 ? 601  EDO A H21    1 
HETATM 5771 H H22    . EDO C 3 .   ? 15.538 64.019 16.650 1.00 50.48 ? 601  EDO A H22    1 
HETATM 5772 H HO2    . EDO C 3 .   ? 15.911 65.972 15.636 1.00 50.07 ? 601  EDO A HO2    1 
HETATM 5773 C C1     . EDO D 3 .   ? 45.328 27.029 61.590 1.00 32.27 ? 602  EDO A C1     1 
HETATM 5774 O O1     . EDO D 3 .   ? 46.617 26.873 61.040 1.00 30.16 ? 602  EDO A O1     1 
HETATM 5775 C C2     . EDO D 3 .   ? 45.325 27.227 63.073 1.00 33.15 ? 602  EDO A C2     1 
HETATM 5776 O O2     . EDO D 3 .   ? 45.086 28.578 63.387 1.00 31.31 ? 602  EDO A O2     1 
HETATM 5777 H H11    . EDO D 3 .   ? 44.879 27.791 61.191 1.00 38.73 ? 602  EDO A H11    1 
HETATM 5778 H H12    . EDO D 3 .   ? 44.781 26.251 61.398 1.00 38.73 ? 602  EDO A H12    1 
HETATM 5779 H HO1    . EDO D 3 .   ? 46.757 27.519 60.506 1.00 36.19 ? 602  EDO A HO1    1 
HETATM 5780 H H21    . EDO D 3 .   ? 44.649 26.639 63.445 1.00 39.77 ? 602  EDO A H21    1 
HETATM 5781 H H22    . EDO D 3 .   ? 46.181 26.919 63.410 1.00 39.77 ? 602  EDO A H22    1 
HETATM 5782 H HO2    . EDO D 3 .   ? 44.462 28.860 62.883 1.00 37.58 ? 602  EDO A HO2    1 
HETATM 5783 C C1     . EDO E 3 .   ? 6.452  34.578 41.834 1.00 25.42 ? 603  EDO A C1     1 
HETATM 5784 O O1     . EDO E 3 .   ? 6.988  34.295 40.564 1.00 22.61 ? 603  EDO A O1     1 
HETATM 5785 C C2     . EDO E 3 .   ? 5.055  35.137 41.774 1.00 27.95 ? 603  EDO A C2     1 
HETATM 5786 O O2     . EDO E 3 .   ? 4.271  34.469 40.792 1.00 27.36 ? 603  EDO A O2     1 
HETATM 5787 H H11    . EDO E 3 .   ? 7.008  35.218 42.305 1.00 30.51 ? 603  EDO A H11    1 
HETATM 5788 H H12    . EDO E 3 .   ? 6.427  33.776 42.380 1.00 30.51 ? 603  EDO A H12    1 
HETATM 5789 H HO1    . EDO E 3 .   ? 7.069  35.028 40.141 1.00 27.14 ? 603  EDO A HO1    1 
HETATM 5790 H H21    . EDO E 3 .   ? 5.133  36.087 41.592 1.00 33.54 ? 603  EDO A H21    1 
HETATM 5791 H H22    . EDO E 3 .   ? 4.673  35.053 42.662 1.00 33.54 ? 603  EDO A H22    1 
HETATM 5792 H HO2    . EDO E 3 .   ? 3.494  34.815 40.793 1.00 32.83 ? 603  EDO A HO2    1 
HETATM 5793 C C1     . EDO F 3 .   ? 32.775 50.030 54.552 1.00 25.85 ? 604  EDO A C1     1 
HETATM 5794 O O1     . EDO F 3 .   ? 32.789 51.345 54.130 1.00 30.17 ? 604  EDO A O1     1 
HETATM 5795 C C2     . EDO F 3 .   ? 32.209 50.099 55.941 1.00 30.93 ? 604  EDO A C2     1 
HETATM 5796 O O2     . EDO F 3 .   ? 30.800 50.148 55.832 1.00 36.52 ? 604  EDO A O2     1 
HETATM 5797 H H11    . EDO F 3 .   ? 32.223 49.463 53.990 1.00 31.02 ? 604  EDO A H11    1 
HETATM 5798 H H12    . EDO F 3 .   ? 33.659 49.632 54.566 1.00 31.02 ? 604  EDO A H12    1 
HETATM 5799 H HO1    . EDO F 3 .   ? 33.046 51.360 53.320 1.00 36.21 ? 604  EDO A HO1    1 
HETATM 5800 H H21    . EDO F 3 .   ? 32.520 49.324 56.435 1.00 37.12 ? 604  EDO A H21    1 
HETATM 5801 H H22    . EDO F 3 .   ? 32.579 50.879 56.382 1.00 37.12 ? 604  EDO A H22    1 
HETATM 5802 H HO2    . EDO F 3 .   ? 30.486 50.417 56.575 1.00 43.83 ? 604  EDO A HO2    1 
HETATM 5803 C C1     . EDO G 3 .   ? 34.121 11.804 57.103 1.00 33.83 ? 605  EDO A C1     1 
HETATM 5804 O O1     . EDO G 3 .   ? 33.349 11.328 58.173 1.00 35.11 ? 605  EDO A O1     1 
HETATM 5805 C C2     . EDO G 3 .   ? 33.168 12.143 55.989 1.00 33.38 ? 605  EDO A C2     1 
HETATM 5806 O O2     . EDO G 3 .   ? 32.436 13.303 56.365 1.00 34.46 ? 605  EDO A O2     1 
HETATM 5807 H H11    . EDO G 3 .   ? 34.631 12.592 57.347 1.00 40.60 ? 605  EDO A H11    1 
HETATM 5808 H H12    . EDO G 3 .   ? 34.759 11.142 56.794 1.00 40.60 ? 605  EDO A H12    1 
HETATM 5809 H HO1    . EDO G 3 .   ? 33.868 11.181 58.830 1.00 42.13 ? 605  EDO A HO1    1 
HETATM 5810 H H21    . EDO G 3 .   ? 33.685 12.275 55.179 1.00 40.06 ? 605  EDO A H21    1 
HETATM 5811 H H22    . EDO G 3 .   ? 32.597 11.375 55.834 1.00 40.06 ? 605  EDO A H22    1 
HETATM 5812 H HO2    . EDO G 3 .   ? 31.861 13.460 55.760 1.00 41.35 ? 605  EDO A HO2    1 
HETATM 5813 O O      . HOH H 4 .   ? 23.938 46.069 33.906 1.00 24.19 ? 701  HOH A O      1 
HETATM 5814 H H1     . HOH H 4 .   ? 24.783 45.996 33.970 0.01 29.03 ? 701  HOH A H1     1 
HETATM 5815 H H2     . HOH H 4 .   ? 23.759 46.767 34.356 0.01 29.03 ? 701  HOH A H2     1 
HETATM 5816 O O      . HOH H 4 .   ? 15.041 24.257 48.098 1.00 25.77 ? 702  HOH A O      1 
HETATM 5817 H H1     . HOH H 4 .   ? 14.697 25.034 48.096 0.02 30.92 ? 702  HOH A H1     1 
HETATM 5818 H H2     . HOH H 4 .   ? 15.870 24.402 47.981 0.01 30.92 ? 702  HOH A H2     1 
HETATM 5819 O O      . HOH H 4 .   ? 33.563 57.800 40.114 1.00 24.41 ? 703  HOH A O      1 
HETATM 5820 H H1     . HOH H 4 .   ? 33.482 57.885 39.273 0.01 29.30 ? 703  HOH A H1     1 
HETATM 5821 H H2     . HOH H 4 .   ? 32.910 58.229 40.436 0.01 29.30 ? 703  HOH A H2     1 
HETATM 5822 O O      . HOH H 4 .   ? 8.752  41.510 49.296 1.00 25.74 ? 704  HOH A O      1 
HETATM 5823 H H1     . HOH H 4 .   ? 8.125  42.067 49.157 0.01 30.89 ? 704  HOH A H1     1 
HETATM 5824 H H2     . HOH H 4 .   ? 8.844  41.119 48.546 0.01 30.89 ? 704  HOH A H2     1 
HETATM 5825 O O      . HOH H 4 .   ? 41.762 22.593 63.325 1.00 33.22 ? 705  HOH A O      1 
HETATM 5826 H H1     . HOH H 4 .   ? 42.516 22.840 63.035 0.01 39.87 ? 705  HOH A H1     1 
HETATM 5827 H H2     . HOH H 4 .   ? 41.203 23.120 62.959 0.01 39.87 ? 705  HOH A H2     1 
HETATM 5828 O O      . HOH H 4 .   ? 40.885 34.964 65.632 1.00 31.39 ? 706  HOH A O      1 
HETATM 5829 H H1     . HOH H 4 .   ? 40.086 34.734 65.456 0.01 37.67 ? 706  HOH A H1     1 
HETATM 5830 H H2     . HOH H 4 .   ? 41.357 34.457 65.142 0.01 37.67 ? 706  HOH A H2     1 
HETATM 5831 O O      . HOH H 4 .   ? 38.945 38.875 63.344 1.00 39.81 ? 707  HOH A O      1 
HETATM 5832 H H1     . HOH H 4 .   ? 39.549 39.472 63.365 0.01 47.77 ? 707  HOH A H1     1 
HETATM 5833 H H2     . HOH H 4 .   ? 38.292 39.255 62.955 0.01 47.77 ? 707  HOH A H2     1 
HETATM 5834 O O      . HOH H 4 .   ? 46.405 33.061 53.735 1.00 37.01 ? 708  HOH A O      1 
HETATM 5835 H H1     . HOH H 4 .   ? 47.085 33.564 53.653 0.01 44.41 ? 708  HOH A H1     1 
HETATM 5836 H H2     . HOH H 4 .   ? 45.749 33.600 53.733 0.01 44.41 ? 708  HOH A H2     1 
HETATM 5837 O O      . HOH H 4 .   ? 7.428  31.981 21.125 1.00 51.17 ? 709  HOH A O      1 
HETATM 5838 H H1     . HOH H 4 .   ? 6.644  31.691 21.001 0.01 61.41 ? 709  HOH A H1     1 
HETATM 5839 H H2     . HOH H 4 .   ? 7.325  32.807 21.012 0.01 61.41 ? 709  HOH A H2     1 
HETATM 5840 O O      . HOH H 4 .   ? 34.369 38.624 65.743 1.00 22.67 ? 710  HOH A O      1 
HETATM 5841 H H1     . HOH H 4 .   ? 35.163 38.331 65.701 0.04 27.21 ? 710  HOH A H1     1 
HETATM 5842 H H2     . HOH H 4 .   ? 34.029 38.229 66.409 0.03 27.21 ? 710  HOH A H2     1 
HETATM 5843 O O      . HOH H 4 .   ? 23.204 54.224 59.037 1.00 46.41 ? 711  HOH A O      1 
HETATM 5844 H H1     . HOH H 4 .   ? 23.847 54.698 59.325 0.01 55.70 ? 711  HOH A H1     1 
HETATM 5845 H H2     . HOH H 4 .   ? 22.516 54.569 59.398 0.01 55.70 ? 711  HOH A H2     1 
HETATM 5846 O O      . HOH H 4 .   ? 35.523 42.351 43.747 1.00 46.33 ? 712  HOH A O      1 
HETATM 5847 H H1     . HOH H 4 .   ? 36.167 42.905 43.757 0.01 55.59 ? 712  HOH A H1     1 
HETATM 5848 H H2     . HOH H 4 .   ? 34.835 42.838 43.638 0.01 55.59 ? 712  HOH A H2     1 
HETATM 5849 O O      . HOH H 4 .   ? 10.133 55.052 32.315 1.00 49.49 ? 713  HOH A O      1 
HETATM 5850 H H1     . HOH H 4 .   ? 10.620 55.713 32.096 0.01 59.39 ? 713  HOH A H1     1 
HETATM 5851 H H2     . HOH H 4 .   ? 9.345  55.369 32.316 0.01 59.39 ? 713  HOH A H2     1 
HETATM 5852 O O      . HOH H 4 .   ? 9.301  23.412 46.341 1.00 40.32 ? 714  HOH A O      1 
HETATM 5853 H H1     . HOH H 4 .   ? 9.995  23.888 46.456 0.01 48.39 ? 714  HOH A H1     1 
HETATM 5854 H H2     . HOH H 4 .   ? 8.963  23.352 47.119 0.01 48.39 ? 714  HOH A H2     1 
HETATM 5855 O O      . HOH H 4 .   ? 22.458 47.426 59.569 1.00 50.74 ? 715  HOH A O      1 
HETATM 5856 H H1     . HOH H 4 .   ? 23.124 47.836 59.903 0.01 60.89 ? 715  HOH A H1     1 
HETATM 5857 H H2     . HOH H 4 .   ? 21.819 47.980 59.643 0.01 60.89 ? 715  HOH A H2     1 
HETATM 5858 O O      . HOH H 4 .   ? 25.948 42.964 33.835 1.00 37.35 ? 716  HOH A O      1 
HETATM 5859 H H1     . HOH H 4 .   ? 26.764 43.016 34.070 0.01 44.83 ? 716  HOH A H1     1 
HETATM 5860 H H2     . HOH H 4 .   ? 25.646 43.746 33.973 0.01 44.83 ? 716  HOH A H2     1 
HETATM 5861 O O      . HOH H 4 .   ? 30.785 33.851 42.114 1.00 35.05 ? 717  HOH A O      1 
HETATM 5862 H H1     . HOH H 4 .   ? 31.587 33.570 42.082 0.01 42.06 ? 717  HOH A H1     1 
HETATM 5863 H H2     . HOH H 4 .   ? 30.865 34.676 42.299 0.01 42.06 ? 717  HOH A H2     1 
HETATM 5864 O O      . HOH H 4 .   ? 8.620  22.701 40.016 1.00 26.82 ? 718  HOH A O      1 
HETATM 5865 H H1     . HOH H 4 .   ? 9.365  23.015 39.752 0.01 32.18 ? 718  HOH A H1     1 
HETATM 5866 H H2     . HOH H 4 .   ? 8.058  23.298 39.796 0.01 32.18 ? 718  HOH A H2     1 
HETATM 5867 O O      . HOH H 4 .   ? 43.007 24.958 36.974 1.00 36.91 ? 719  HOH A O      1 
HETATM 5868 H H1     . HOH H 4 .   ? 43.690 25.463 36.995 0.01 44.29 ? 719  HOH A H1     1 
HETATM 5869 H H2     . HOH H 4 .   ? 42.352 25.501 36.995 0.01 44.29 ? 719  HOH A H2     1 
HETATM 5870 O O      . HOH H 4 .   ? 29.587 32.564 30.272 1.00 53.16 ? 720  HOH A O      1 
HETATM 5871 H H1     . HOH H 4 .   ? 30.114 33.231 30.271 0.01 63.80 ? 720  HOH A H1     1 
HETATM 5872 H H2     . HOH H 4 .   ? 28.832 32.901 30.073 0.01 63.80 ? 720  HOH A H2     1 
HETATM 5873 O O      . HOH H 4 .   ? 20.458 58.689 13.466 1.00 44.63 ? 721  HOH A O      1 
HETATM 5874 H H1     . HOH H 4 .   ? 21.159 59.153 13.592 0.01 53.56 ? 721  HOH A H1     1 
HETATM 5875 H H2     . HOH H 4 .   ? 19.830 59.261 13.460 0.01 53.56 ? 721  HOH A H2     1 
HETATM 5876 O O      . HOH H 4 .   ? 39.528 41.365 62.282 1.00 38.45 ? 722  HOH A O      1 
HETATM 5877 H H1     . HOH H 4 .   ? 40.021 41.834 62.792 0.01 46.15 ? 722  HOH A H1     1 
HETATM 5878 H H2     . HOH H 4 .   ? 39.099 41.945 61.830 0.01 46.15 ? 722  HOH A H2     1 
HETATM 5879 O O      . HOH H 4 .   ? 14.865 42.009 20.443 1.00 23.95 ? 723  HOH A O      1 
HETATM 5880 H H1     . HOH H 4 .   ? 15.530 42.536 20.461 0.01 28.75 ? 723  HOH A H1     1 
HETATM 5881 H H2     . HOH H 4 .   ? 14.191 42.527 20.460 0.01 28.75 ? 723  HOH A H2     1 
HETATM 5882 O O      . HOH H 4 .   ? 7.521  57.774 23.052 1.00 44.90 ? 724  HOH A O      1 
HETATM 5883 H H1     . HOH H 4 .   ? 8.226  58.249 23.072 0.01 53.88 ? 724  HOH A H1     1 
HETATM 5884 H H2     . HOH H 4 .   ? 6.891  58.343 23.024 0.01 53.88 ? 724  HOH A H2     1 
HETATM 5885 O O      . HOH H 4 .   ? 24.606 18.496 36.111 1.00 37.17 ? 725  HOH A O      1 
HETATM 5886 H H1     . HOH H 4 .   ? 25.391 18.822 36.145 0.01 44.61 ? 725  HOH A H1     1 
HETATM 5887 H H2     . HOH H 4 .   ? 24.280 18.825 35.399 0.01 44.61 ? 725  HOH A H2     1 
HETATM 5888 O O      . HOH H 4 .   ? 19.462 45.150 34.844 1.00 19.83 ? 726  HOH A O      1 
HETATM 5889 H H1     . HOH H 4 .   ? 19.925 45.197 35.556 0.01 23.80 ? 726  HOH A H1     1 
HETATM 5890 H H2     . HOH H 4 .   ? 18.665 45.273 35.110 0.01 23.80 ? 726  HOH A H2     1 
HETATM 5891 O O      . HOH H 4 .   ? 25.027 39.420 22.691 1.00 35.66 ? 727  HOH A O      1 
HETATM 5892 H H1     . HOH H 4 .   ? 25.802 39.767 22.650 0.01 42.79 ? 727  HOH A H1     1 
HETATM 5893 H H2     . HOH H 4 .   ? 24.524 40.066 22.915 0.01 42.79 ? 727  HOH A H2     1 
HETATM 5894 O O      . HOH H 4 .   ? 32.354 50.357 27.647 1.00 47.45 ? 728  HOH A O      1 
HETATM 5895 H H1     . HOH H 4 .   ? 33.018 50.889 27.627 0.01 56.94 ? 728  HOH A H1     1 
HETATM 5896 H H2     . HOH H 4 .   ? 31.679 50.873 27.626 0.01 56.94 ? 728  HOH A H2     1 
HETATM 5897 O O      . HOH H 4 .   ? 17.833 27.914 51.038 1.00 48.46 ? 729  HOH A O      1 
HETATM 5898 H H1     . HOH H 4 .   ? 18.547 28.111 51.455 0.01 58.16 ? 729  HOH A H1     1 
HETATM 5899 H H2     . HOH H 4 .   ? 17.236 28.380 51.424 0.01 58.16 ? 729  HOH A H2     1 
HETATM 5900 O O      . HOH H 4 .   ? 44.164 20.282 51.564 1.00 35.25 ? 730  HOH A O      1 
HETATM 5901 H H1     . HOH H 4 .   ? 44.842 20.794 51.554 0.01 42.30 ? 730  HOH A H1     1 
HETATM 5902 H H2     . HOH H 4 .   ? 43.503 20.817 51.537 0.01 42.30 ? 730  HOH A H2     1 
HETATM 5903 O O      . HOH H 4 .   ? 48.211 54.149 38.385 1.00 35.87 ? 731  HOH A O      1 
HETATM 5904 H H1     . HOH H 4 .   ? 48.679 54.421 39.040 0.01 43.04 ? 731  HOH A H1     1 
HETATM 5905 H H2     . HOH H 4 .   ? 47.573 54.710 38.344 0.01 43.04 ? 731  HOH A H2     1 
HETATM 5906 O O      . HOH H 4 .   ? 39.689 56.772 45.285 1.00 29.61 ? 732  HOH A O      1 
HETATM 5907 H H1     . HOH H 4 .   ? 40.430 57.186 45.319 0.01 35.53 ? 732  HOH A H1     1 
HETATM 5908 H H2     . HOH H 4 .   ? 39.211 57.247 44.767 0.01 35.53 ? 732  HOH A H2     1 
HETATM 5909 O O      . HOH H 4 .   ? 34.746 44.716 41.980 1.00 39.42 ? 733  HOH A O      1 
HETATM 5910 H H1     . HOH H 4 .   ? 35.410 45.247 41.996 0.01 47.31 ? 733  HOH A H1     1 
HETATM 5911 H H2     . HOH H 4 .   ? 34.072 45.232 41.996 0.01 47.31 ? 733  HOH A H2     1 
HETATM 5912 O O      . HOH H 4 .   ? 28.846 10.056 43.558 1.00 43.38 ? 734  HOH A O      1 
HETATM 5913 H H1     . HOH H 4 .   ? 29.454 10.382 44.054 0.01 52.05 ? 734  HOH A H1     1 
HETATM 5914 H H2     . HOH H 4 .   ? 28.186 10.579 43.674 0.01 52.05 ? 734  HOH A H2     1 
HETATM 5915 O O      . HOH H 4 .   ? 37.021 11.312 39.683 1.00 43.57 ? 735  HOH A O      1 
HETATM 5916 H H1     . HOH H 4 .   ? 37.320 12.103 39.755 0.01 52.28 ? 735  HOH A H1     1 
HETATM 5917 H H2     . HOH H 4 .   ? 36.182 11.400 39.792 0.01 52.28 ? 735  HOH A H2     1 
HETATM 5918 O O      . HOH H 4 .   ? 21.636 20.037 38.576 1.00 40.65 ? 736  HOH A O      1 
HETATM 5919 H H1     . HOH H 4 .   ? 21.867 19.719 39.329 0.01 48.78 ? 736  HOH A H1     1 
HETATM 5920 H H2     . HOH H 4 .   ? 21.877 20.851 38.614 0.01 48.78 ? 736  HOH A H2     1 
HETATM 5921 O O      . HOH H 4 .   ? 10.812 28.974 31.447 1.00 24.17 ? 737  HOH A O      1 
HETATM 5922 H H1     . HOH H 4 .   ? 11.656 29.065 31.388 0.01 29.00 ? 737  HOH A H1     1 
HETATM 5923 H H2     . HOH H 4 .   ? 10.513 29.762 31.341 0.01 29.00 ? 737  HOH A H2     1 
HETATM 5924 O O      . HOH H 4 .   ? 45.878 43.494 49.508 1.00 21.05 ? 738  HOH A O      1 
HETATM 5925 H H1     . HOH H 4 .   ? 46.726 43.520 49.570 0.01 25.26 ? 738  HOH A H1     1 
HETATM 5926 H H2     . HOH H 4 .   ? 45.688 44.176 49.037 0.01 25.26 ? 738  HOH A H2     1 
HETATM 5927 O O      . HOH H 4 .   ? 23.931 64.310 23.002 1.00 47.68 ? 739  HOH A O      1 
HETATM 5928 H H1     . HOH H 4 .   ? 24.614 64.811 22.929 0.01 57.22 ? 739  HOH A H1     1 
HETATM 5929 H H2     . HOH H 4 .   ? 23.276 64.846 22.928 0.01 57.22 ? 739  HOH A H2     1 
HETATM 5930 O O      . HOH H 4 .   ? 21.111 57.382 60.306 1.00 31.74 ? 740  HOH A O      1 
HETATM 5931 H H1     . HOH H 4 .   ? 21.781 57.905 60.304 0.01 38.09 ? 740  HOH A H1     1 
HETATM 5932 H H2     . HOH H 4 .   ? 20.444 57.910 60.303 0.01 38.09 ? 740  HOH A H2     1 
HETATM 5933 O O      . HOH H 4 .   ? 28.849 15.537 56.976 1.00 41.68 ? 741  HOH A O      1 
HETATM 5934 H H1     . HOH H 4 .   ? 29.520 16.059 56.983 0.01 50.02 ? 741  HOH A H1     1 
HETATM 5935 H H2     . HOH H 4 .   ? 28.181 16.061 56.983 0.01 50.02 ? 741  HOH A H2     1 
HETATM 5936 O O      . HOH H 4 .   ? 21.891 28.202 51.739 1.00 40.26 ? 742  HOH A O      1 
HETATM 5937 H H1     . HOH H 4 .   ? 21.992 29.033 51.596 0.01 48.31 ? 742  HOH A H1     1 
HETATM 5938 H H2     . HOH H 4 .   ? 21.050 28.107 51.814 0.01 48.31 ? 742  HOH A H2     1 
HETATM 5939 O O      . HOH H 4 .   ? 9.943  60.869 18.752 1.00 41.52 ? 743  HOH A O      1 
HETATM 5940 H H1     . HOH H 4 .   ? 10.612 61.394 18.754 0.01 49.82 ? 743  HOH A H1     1 
HETATM 5941 H H2     . HOH H 4 .   ? 9.274  61.393 18.754 0.01 49.82 ? 743  HOH A H2     1 
HETATM 5942 O O      . HOH H 4 .   ? 21.044 62.231 38.410 1.00 30.29 ? 744  HOH A O      1 
HETATM 5943 H H1     . HOH H 4 .   ? 21.710 62.760 38.406 0.01 36.35 ? 744  HOH A H1     1 
HETATM 5944 H H2     . HOH H 4 .   ? 20.372 62.753 38.406 0.01 36.35 ? 744  HOH A H2     1 
HETATM 5945 O O      . HOH H 4 .   ? 31.856 42.124 49.874 1.00 10.88 ? 745  HOH A O      1 
HETATM 5946 H H1     . HOH H 4 .   ? 32.277 42.158 49.139 0.04 13.06 ? 745  HOH A H1     1 
HETATM 5947 H H2     . HOH H 4 .   ? 31.092 42.452 49.687 0.01 13.06 ? 745  HOH A H2     1 
HETATM 5948 O O      . HOH H 4 .   ? 18.446 29.649 34.337 1.00 33.48 ? 746  HOH A O      1 
HETATM 5949 H H1     . HOH H 4 .   ? 19.043 30.105 33.940 0.01 40.18 ? 746  HOH A H1     1 
HETATM 5950 H H2     . HOH H 4 .   ? 17.725 30.069 34.178 0.01 40.18 ? 746  HOH A H2     1 
HETATM 5951 O O      . HOH H 4 .   ? 1.621  28.351 39.017 1.00 13.48 ? 747  HOH A O      1 
HETATM 5952 H H1     . HOH H 4 .   ? 1.394  28.413 38.200 0.06 16.18 ? 747  HOH A H1     1 
HETATM 5953 H H2     . HOH H 4 .   ? 2.247  28.924 39.104 0.02 16.18 ? 747  HOH A H2     1 
HETATM 5954 O O      . HOH H 4 .   ? 26.596 37.124 60.544 1.00 42.25 ? 748  HOH A O      1 
HETATM 5955 H H1     . HOH H 4 .   ? 27.261 37.652 60.506 0.01 50.70 ? 748  HOH A H1     1 
HETATM 5956 H H2     . HOH H 4 .   ? 25.923 37.641 60.506 0.01 50.70 ? 748  HOH A H2     1 
HETATM 5957 O O      . HOH H 4 .   ? 37.415 31.166 70.256 1.00 36.88 ? 749  HOH A O      1 
HETATM 5958 H H1     . HOH H 4 .   ? 38.202 31.476 70.185 0.01 44.26 ? 749  HOH A H1     1 
HETATM 5959 H H2     . HOH H 4 .   ? 36.951 31.658 69.741 0.01 44.26 ? 749  HOH A H2     1 
HETATM 5960 O O      . HOH H 4 .   ? 28.925 28.068 49.289 1.00 18.99 ? 750  HOH A O      1 
HETATM 5961 H H1     . HOH H 4 .   ? 29.591 28.580 49.154 0.01 22.78 ? 750  HOH A H1     1 
HETATM 5962 H H2     . HOH H 4 .   ? 28.281 28.604 49.429 0.03 22.78 ? 750  HOH A H2     1 
HETATM 5963 O O      . HOH H 4 .   ? 19.244 57.112 49.259 1.00 27.78 ? 751  HOH A O      1 
HETATM 5964 H H1     . HOH H 4 .   ? 19.789 57.701 48.977 0.01 33.34 ? 751  HOH A H1     1 
HETATM 5965 H H2     . HOH H 4 .   ? 18.495 57.515 49.262 0.01 33.34 ? 751  HOH A H2     1 
HETATM 5966 O O      . HOH H 4 .   ? 4.864  40.676 27.563 1.00 34.23 ? 752  HOH A O      1 
HETATM 5967 H H1     . HOH H 4 .   ? 5.246  41.314 27.152 0.01 41.08 ? 752  HOH A H1     1 
HETATM 5968 H H2     . HOH H 4 .   ? 4.047  40.910 27.587 0.01 41.08 ? 752  HOH A H2     1 
HETATM 5969 O O      . HOH H 4 .   ? 18.572 34.636 52.591 1.00 40.05 ? 753  HOH A O      1 
HETATM 5970 H H1     . HOH H 4 .   ? 19.212 34.845 53.110 0.01 48.06 ? 753  HOH A H1     1 
HETATM 5971 H H2     . HOH H 4 .   ? 18.501 33.794 52.687 0.01 48.06 ? 753  HOH A H2     1 
HETATM 5972 O O      . HOH H 4 .   ? 18.879 32.264 25.883 1.00 38.14 ? 754  HOH A O      1 
HETATM 5973 H H1     . HOH H 4 .   ? 19.550 32.686 25.578 0.01 45.76 ? 754  HOH A H1     1 
HETATM 5974 H H2     . HOH H 4 .   ? 18.241 32.825 25.817 0.01 45.76 ? 754  HOH A H2     1 
HETATM 5975 O O      . HOH H 4 .   ? 27.480 33.373 69.010 1.00 38.32 ? 755  HOH A O      1 
HETATM 5976 H H1     . HOH H 4 .   ? 28.158 33.885 69.039 0.01 45.99 ? 755  HOH A H1     1 
HETATM 5977 H H2     . HOH H 4 .   ? 26.819 33.906 69.038 0.01 45.99 ? 755  HOH A H2     1 
HETATM 5978 O O      . HOH H 4 .   ? 14.392 34.763 52.401 1.00 35.03 ? 756  HOH A O      1 
HETATM 5979 H H1     . HOH H 4 .   ? 15.057 35.292 52.411 0.01 42.04 ? 756  HOH A H1     1 
HETATM 5980 H H2     . HOH H 4 .   ? 13.718 35.279 52.411 0.01 42.04 ? 756  HOH A H2     1 
HETATM 5981 O O      . HOH H 4 .   ? 15.545 57.929 30.312 1.00 35.06 ? 757  HOH A O      1 
HETATM 5982 H H1     . HOH H 4 .   ? 16.212 58.456 30.320 0.01 42.07 ? 757  HOH A H1     1 
HETATM 5983 H H2     . HOH H 4 .   ? 14.872 58.450 30.320 0.01 42.07 ? 757  HOH A H2     1 
HETATM 5984 O O      . HOH H 4 .   ? 28.670 44.876 21.930 1.00 31.40 ? 758  HOH A O      1 
HETATM 5985 H H1     . HOH H 4 .   ? 29.360 45.365 21.846 0.01 37.68 ? 758  HOH A H1     1 
HETATM 5986 H H2     . HOH H 4 .   ? 28.041 45.431 22.072 0.01 37.68 ? 758  HOH A H2     1 
HETATM 5987 O O      . HOH H 4 .   ? 22.351 60.235 14.864 1.00 21.78 ? 759  HOH A O      1 
HETATM 5988 H H1     . HOH H 4 .   ? 23.072 60.684 14.833 0.01 26.13 ? 759  HOH A H1     1 
HETATM 5989 H H2     . HOH H 4 .   ? 21.848 60.693 15.375 0.01 26.13 ? 759  HOH A H2     1 
HETATM 5990 O O      . HOH H 4 .   ? 10.856 37.474 29.325 1.00 22.12 ? 760  HOH A O      1 
HETATM 5991 H H1     . HOH H 4 .   ? 11.549 37.949 29.459 0.04 26.55 ? 760  HOH A H1     1 
HETATM 5992 H H2     . HOH H 4 .   ? 10.256 37.856 29.791 0.01 26.55 ? 760  HOH A H2     1 
HETATM 5993 O O      . HOH H 4 .   ? 25.301 54.282 34.074 1.00 22.73 ? 761  HOH A O      1 
HETATM 5994 H H1     . HOH H 4 .   ? 25.716 54.999 34.261 0.01 27.27 ? 761  HOH A H1     1 
HETATM 5995 H H2     . HOH H 4 .   ? 24.485 54.517 34.051 0.01 27.27 ? 761  HOH A H2     1 
HETATM 5996 O O      . HOH H 4 .   ? 20.974 60.687 44.489 1.00 33.57 ? 762  HOH A O      1 
HETATM 5997 H H1     . HOH H 4 .   ? 21.817 60.637 44.391 0.01 40.28 ? 762  HOH A H1     1 
HETATM 5998 H H2     . HOH H 4 .   ? 20.870 61.323 45.043 0.01 40.28 ? 762  HOH A H2     1 
HETATM 5999 O O      . HOH H 4 .   ? 17.314 33.788 22.560 1.00 31.96 ? 763  HOH A O      1 
HETATM 6000 H H1     . HOH H 4 .   ? 17.997 34.291 22.606 0.01 38.36 ? 763  HOH A H1     1 
HETATM 6001 H H2     . HOH H 4 .   ? 17.063 33.855 21.750 0.01 38.36 ? 763  HOH A H2     1 
HETATM 6002 O O      . HOH H 4 .   ? 43.723 18.926 59.502 1.00 25.50 ? 764  HOH A O      1 
HETATM 6003 H H1     . HOH H 4 .   ? 44.083 19.644 59.226 0.01 30.61 ? 764  HOH A H1     1 
HETATM 6004 H H2     . HOH H 4 .   ? 43.280 19.167 60.185 0.01 30.61 ? 764  HOH A H2     1 
HETATM 6005 O O      . HOH H 4 .   ? 18.147 30.445 31.986 1.00 29.85 ? 765  HOH A O      1 
HETATM 6006 H H1     . HOH H 4 .   ? 18.895 30.847 31.947 0.01 35.82 ? 765  HOH A H1     1 
HETATM 6007 H H2     . HOH H 4 .   ? 17.597 31.058 32.195 0.01 35.82 ? 765  HOH A H2     1 
HETATM 6008 O O      . HOH H 4 .   ? 24.105 35.884 24.970 1.00 30.44 ? 766  HOH A O      1 
HETATM 6009 H H1     . HOH H 4 .   ? 24.817 36.340 24.881 0.01 36.53 ? 766  HOH A H1     1 
HETATM 6010 H H2     . HOH H 4 .   ? 23.532 36.308 24.507 0.01 36.53 ? 766  HOH A H2     1 
HETATM 6011 O O      . HOH H 4 .   ? 16.751 68.517 21.233 1.00 32.35 ? 767  HOH A O      1 
HETATM 6012 H H1     . HOH H 4 .   ? 17.424 69.036 21.255 0.01 38.81 ? 767  HOH A H1     1 
HETATM 6013 H H2     . HOH H 4 .   ? 16.084 69.043 21.254 0.01 38.81 ? 767  HOH A H2     1 
HETATM 6014 O O      . HOH H 4 .   ? 8.319  36.484 39.758 1.00 24.95 ? 768  HOH A O      1 
HETATM 6015 H H1     . HOH H 4 .   ? 8.995  37.000 39.749 0.01 29.95 ? 768  HOH A H1     1 
HETATM 6016 H H2     . HOH H 4 .   ? 7.657  37.016 39.746 0.01 29.95 ? 768  HOH A H2     1 
HETATM 6017 O O      . HOH H 4 .   ? 20.204 45.969 56.489 1.00 32.42 ? 769  HOH A O      1 
HETATM 6018 H H1     . HOH H 4 .   ? 20.882 46.481 56.489 0.01 38.91 ? 769  HOH A H1     1 
HETATM 6019 H H2     . HOH H 4 .   ? 19.543 46.504 56.518 0.01 38.91 ? 769  HOH A H2     1 
HETATM 6020 O O      . HOH H 4 .   ? 42.509 33.062 64.719 1.00 21.15 ? 770  HOH A O      1 
HETATM 6021 H H1     . HOH H 4 .   ? 42.746 33.688 64.193 0.01 25.38 ? 770  HOH A H1     1 
HETATM 6022 H H2     . HOH H 4 .   ? 41.905 32.649 64.285 0.01 25.38 ? 770  HOH A H2     1 
HETATM 6023 O O      . HOH H 4 .   ? 29.700 29.404 51.303 1.00 15.27 ? 771  HOH A O      1 
HETATM 6024 H H1     . HOH H 4 .   ? 30.380 29.342 50.799 0.04 18.33 ? 771  HOH A H1     1 
HETATM 6025 H H2     . HOH H 4 .   ? 29.079 29.637 50.773 0.00 18.33 ? 771  HOH A H2     1 
HETATM 6026 O O      . HOH H 4 .   ? 26.537 41.990 58.412 1.00 16.25 ? 772  HOH A O      1 
HETATM 6027 H H1     . HOH H 4 .   ? 26.572 41.502 57.612 0.01 19.51 ? 772  HOH A H1     1 
HETATM 6028 H H2     . HOH H 4 .   ? 27.435 41.919 58.779 0.02 19.51 ? 772  HOH A H2     1 
HETATM 6029 O O      . HOH H 4 .   ? 25.444 57.019 33.956 1.00 25.14 ? 773  HOH A O      1 
HETATM 6030 H H1     . HOH H 4 .   ? 26.075 57.589 33.957 0.01 30.17 ? 773  HOH A H1     1 
HETATM 6031 H H2     . HOH H 4 .   ? 24.775 57.452 34.253 0.01 30.17 ? 773  HOH A H2     1 
HETATM 6032 O O      . HOH H 4 .   ? 41.101 49.539 47.787 1.00 41.20 ? 774  HOH A O      1 
HETATM 6033 H H1     . HOH H 4 .   ? 41.774 50.040 47.921 0.01 49.44 ? 774  HOH A H1     1 
HETATM 6034 H H2     . HOH H 4 .   ? 40.466 50.083 47.637 0.01 49.44 ? 774  HOH A H2     1 
HETATM 6035 O O      . HOH H 4 .   ? 24.961 56.026 40.484 1.00 15.67 ? 775  HOH A O      1 
HETATM 6036 H H1     . HOH H 4 .   ? 24.304 56.674 40.169 0.03 18.80 ? 775  HOH A H1     1 
HETATM 6037 H H2     . HOH H 4 .   ? 24.941 55.540 41.295 0.01 18.80 ? 775  HOH A H2     1 
HETATM 6038 O O      . HOH H 4 .   ? 14.191 58.190 39.188 1.00 49.93 ? 776  HOH A O      1 
HETATM 6039 H H1     . HOH H 4 .   ? 14.847 58.729 39.165 0.01 59.92 ? 776  HOH A H1     1 
HETATM 6040 H H2     . HOH H 4 .   ? 13.508 58.694 39.165 0.01 59.92 ? 776  HOH A H2     1 
HETATM 6041 O O      . HOH H 4 .   ? 38.098 30.725 37.882 1.00 21.05 ? 777  HOH A O      1 
HETATM 6042 H H1     . HOH H 4 .   ? 38.728 31.275 38.037 0.01 25.26 ? 777  HOH A H1     1 
HETATM 6043 H H2     . HOH H 4 .   ? 37.493 31.203 37.527 0.01 25.26 ? 777  HOH A H2     1 
HETATM 6044 O O      . HOH H 4 .   ? 12.327 39.064 34.714 1.00 17.59 ? 778  HOH A O      1 
HETATM 6045 H H1     . HOH H 4 .   ? 12.979 39.604 34.772 0.01 21.11 ? 778  HOH A H1     1 
HETATM 6046 H H2     . HOH H 4 .   ? 11.916 39.313 34.013 0.01 21.11 ? 778  HOH A H2     1 
HETATM 6047 O O      . HOH H 4 .   ? 7.091  36.925 45.053 1.00 13.24 ? 779  HOH A O      1 
HETATM 6048 H H1     . HOH H 4 .   ? 7.431  36.814 44.171 0.05 15.89 ? 779  HOH A H1     1 
HETATM 6049 H H2     . HOH H 4 .   ? 6.423  37.572 45.047 0.04 15.89 ? 779  HOH A H2     1 
HETATM 6050 O O      . HOH H 4 .   ? 44.970 26.013 46.456 1.00 39.96 ? 780  HOH A O      1 
HETATM 6051 H H1     . HOH H 4 .   ? 45.454 26.418 46.924 0.01 47.95 ? 780  HOH A H1     1 
HETATM 6052 H H2     . HOH H 4 .   ? 45.613 25.524 46.237 0.01 47.95 ? 780  HOH A H2     1 
HETATM 6053 O O      . HOH H 4 .   ? 9.600  55.239 28.685 1.00 33.01 ? 781  HOH A O      1 
HETATM 6054 H H1     . HOH H 4 .   ? 10.279 55.751 28.681 0.01 39.61 ? 781  HOH A H1     1 
HETATM 6055 H H2     . HOH H 4 .   ? 8.940  55.774 28.678 0.01 39.61 ? 781  HOH A H2     1 
HETATM 6056 O O      . HOH H 4 .   ? 20.045 23.238 40.430 1.00 17.10 ? 782  HOH A O      1 
HETATM 6057 H H1     . HOH H 4 .   ? 20.434 23.601 41.091 0.01 20.52 ? 782  HOH A H1     1 
HETATM 6058 H H2     . HOH H 4 .   ? 19.218 23.349 40.591 0.01 20.52 ? 782  HOH A H2     1 
HETATM 6059 O O      . HOH H 4 .   ? 36.876 21.218 63.765 1.00 28.61 ? 783  HOH A O      1 
HETATM 6060 H H1     . HOH H 4 .   ? 37.499 21.566 63.305 0.01 34.33 ? 783  HOH A H1     1 
HETATM 6061 H H2     . HOH H 4 .   ? 36.209 21.727 63.626 0.01 34.33 ? 783  HOH A H2     1 
HETATM 6062 O O      . HOH H 4 .   ? 10.501 28.332 41.066 1.00 18.85 ? 784  HOH A O      1 
HETATM 6063 H H1     . HOH H 4 .   ? 11.171 28.854 41.035 0.01 22.62 ? 784  HOH A H1     1 
HETATM 6064 H H2     . HOH H 4 .   ? 9.938  28.749 41.548 0.01 22.62 ? 784  HOH A H2     1 
HETATM 6065 O O      . HOH H 4 .   ? 35.865 55.681 36.895 1.00 24.71 ? 785  HOH A O      1 
HETATM 6066 H H1     . HOH H 4 .   ? 36.674 55.436 36.972 0.01 29.65 ? 785  HOH A H1     1 
HETATM 6067 H H2     . HOH H 4 .   ? 35.912 56.529 36.856 0.01 29.65 ? 785  HOH A H2     1 
HETATM 6068 O O      . HOH H 4 .   ? 38.896 35.568 46.280 1.00 24.09 ? 786  HOH A O      1 
HETATM 6069 H H1     . HOH H 4 .   ? 38.893 35.358 45.456 0.01 28.91 ? 786  HOH A H1     1 
HETATM 6070 H H2     . HOH H 4 .   ? 38.105 35.841 46.426 0.01 28.91 ? 786  HOH A H2     1 
HETATM 6071 O O      . HOH H 4 .   ? 33.552 59.966 46.952 1.00 11.63 ? 787  HOH A O      1 
HETATM 6072 H H1     . HOH H 4 .   ? 33.077 59.728 47.716 0.06 13.96 ? 787  HOH A H1     1 
HETATM 6073 H H2     . HOH H 4 .   ? 33.738 60.801 47.008 0.02 13.96 ? 787  HOH A H2     1 
HETATM 6074 O O      . HOH H 4 .   ? 24.177 19.001 41.520 1.00 17.90 ? 788  HOH A O      1 
HETATM 6075 H H1     . HOH H 4 .   ? 24.787 19.595 41.507 0.01 21.48 ? 788  HOH A H1     1 
HETATM 6076 H H2     . HOH H 4 .   ? 23.458 19.447 41.438 0.05 21.48 ? 788  HOH A H2     1 
HETATM 6077 O O      . HOH H 4 .   ? 40.946 14.850 49.894 1.00 39.26 ? 789  HOH A O      1 
HETATM 6078 H H1     . HOH H 4 .   ? 41.253 14.866 50.686 0.01 47.12 ? 789  HOH A H1     1 
HETATM 6079 H H2     . HOH H 4 .   ? 40.182 15.216 49.961 0.01 47.12 ? 789  HOH A H2     1 
HETATM 6080 O O      . HOH H 4 .   ? 22.397 18.337 43.494 1.00 20.61 ? 790  HOH A O      1 
HETATM 6081 H H1     . HOH H 4 .   ? 23.151 18.707 43.375 0.01 24.74 ? 790  HOH A H1     1 
HETATM 6082 H H2     . HOH H 4 .   ? 21.848 18.986 43.486 0.01 24.74 ? 790  HOH A H2     1 
HETATM 6083 O O      . HOH H 4 .   ? 27.096 59.675 49.378 1.00 41.72 ? 791  HOH A O      1 
HETATM 6084 H H1     . HOH H 4 .   ? 27.814 60.129 49.344 0.01 50.06 ? 791  HOH A H1     1 
HETATM 6085 H H2     . HOH H 4 .   ? 26.495 60.226 49.139 0.01 50.06 ? 791  HOH A H2     1 
HETATM 6086 O O      . HOH H 4 .   ? 14.510 49.334 50.178 1.00 40.88 ? 792  HOH A O      1 
HETATM 6087 H H1     . HOH H 4 .   ? 15.221 49.768 50.010 0.01 49.06 ? 792  HOH A H1     1 
HETATM 6088 H H2     . HOH H 4 .   ? 13.895 49.918 50.131 0.01 49.06 ? 792  HOH A H2     1 
HETATM 6089 O O      . HOH H 4 .   ? 35.246 54.459 34.505 1.00 25.49 ? 793  HOH A O      1 
HETATM 6090 H H1     . HOH H 4 .   ? 35.661 54.767 35.180 0.02 30.59 ? 793  HOH A H1     1 
HETATM 6091 H H2     . HOH H 4 .   ? 34.513 54.891 34.503 0.04 30.59 ? 793  HOH A H2     1 
HETATM 6092 O O      . HOH H 4 .   ? 28.952 46.219 28.992 1.00 30.18 ? 794  HOH A O      1 
HETATM 6093 H H1     . HOH H 4 .   ? 28.703 45.406 29.017 0.01 36.22 ? 794  HOH A H1     1 
HETATM 6094 H H2     . HOH H 4 .   ? 29.662 46.208 29.465 0.01 36.22 ? 794  HOH A H2     1 
HETATM 6095 O O      . HOH H 4 .   ? 31.098 10.931 42.901 1.00 27.89 ? 795  HOH A O      1 
HETATM 6096 H H1     . HOH H 4 .   ? 31.744 11.466 43.037 0.01 33.47 ? 795  HOH A H1     1 
HETATM 6097 H H2     . HOH H 4 .   ? 30.496 11.419 42.553 0.01 33.47 ? 795  HOH A H2     1 
HETATM 6098 O O      . HOH H 4 .   ? 23.243 58.384 33.033 1.00 26.65 ? 796  HOH A O      1 
HETATM 6099 H H1     . HOH H 4 .   ? 23.940 58.864 32.953 0.01 31.98 ? 796  HOH A H1     1 
HETATM 6100 H H2     . HOH H 4 .   ? 22.758 58.618 32.375 0.01 31.98 ? 796  HOH A H2     1 
HETATM 6101 O O      . HOH H 4 .   ? 31.213 36.551 41.780 1.00 25.94 ? 797  HOH A O      1 
HETATM 6102 H H1     . HOH H 4 .   ? 31.880 37.078 41.784 0.01 31.12 ? 797  HOH A H1     1 
HETATM 6103 H H2     . HOH H 4 .   ? 30.539 37.069 41.784 0.01 31.12 ? 797  HOH A H2     1 
HETATM 6104 O O      . HOH H 4 .   ? 34.371 22.538 35.418 1.00 34.31 ? 798  HOH A O      1 
HETATM 6105 H H1     . HOH H 4 .   ? 35.050 23.044 35.485 0.01 41.18 ? 798  HOH A H1     1 
HETATM 6106 H H2     . HOH H 4 .   ? 33.738 23.001 35.746 0.01 41.18 ? 798  HOH A H2     1 
HETATM 6107 O O      . HOH H 4 .   ? 22.384 32.190 30.876 1.00 40.56 ? 799  HOH A O      1 
HETATM 6108 H H1     . HOH H 4 .   ? 23.045 32.719 30.956 0.01 48.67 ? 799  HOH A H1     1 
HETATM 6109 H H2     . HOH H 4 .   ? 21.765 32.569 31.318 0.01 48.67 ? 799  HOH A H2     1 
HETATM 6110 O O      . HOH H 4 .   ? 30.727 20.001 58.787 1.00 33.02 ? 800  HOH A O      1 
HETATM 6111 H H1     . HOH H 4 .   ? 31.414 20.422 58.520 0.01 39.63 ? 800  HOH A H1     1 
HETATM 6112 H H2     . HOH H 4 .   ? 30.107 20.582 58.760 0.01 39.63 ? 800  HOH A H2     1 
HETATM 6113 O O      . HOH H 4 .   ? 45.380 26.741 58.611 1.00 24.32 ? 801  HOH A O      1 
HETATM 6114 H H1     . HOH H 4 .   ? 45.124 26.254 59.254 0.01 29.19 ? 801  HOH A H1     1 
HETATM 6115 H H2     . HOH H 4 .   ? 45.755 27.409 58.971 0.02 29.19 ? 801  HOH A H2     1 
HETATM 6116 O O      . HOH H 4 .   ? 11.517 47.323 37.220 1.00 20.97 ? 802  HOH A O      1 
HETATM 6117 H H1     . HOH H 4 .   ? 11.909 48.046 37.430 0.01 25.16 ? 802  HOH A H1     1 
HETATM 6118 H H2     . HOH H 4 .   ? 10.881 47.265 37.781 0.01 25.16 ? 802  HOH A H2     1 
HETATM 6119 O O      . HOH H 4 .   ? 23.206 60.954 20.243 1.00 28.73 ? 803  HOH A O      1 
HETATM 6120 H H1     . HOH H 4 .   ? 22.437 61.269 20.234 0.04 34.47 ? 803  HOH A H1     1 
HETATM 6121 H H2     . HOH H 4 .   ? 23.030 60.123 20.132 0.01 34.47 ? 803  HOH A H2     1 
HETATM 6122 O O      . HOH H 4 .   ? 41.193 25.645 48.301 1.00 18.70 ? 804  HOH A O      1 
HETATM 6123 H H1     . HOH H 4 .   ? 41.863 26.167 48.302 0.01 22.44 ? 804  HOH A H1     1 
HETATM 6124 H H2     . HOH H 4 .   ? 40.525 26.169 48.301 0.01 22.44 ? 804  HOH A H2     1 
HETATM 6125 O O      . HOH H 4 .   ? 24.043 55.976 56.374 1.00 35.66 ? 805  HOH A O      1 
HETATM 6126 H H1     . HOH H 4 .   ? 24.701 56.513 56.406 0.01 42.80 ? 805  HOH A H1     1 
HETATM 6127 H H2     . HOH H 4 .   ? 23.362 56.485 56.406 0.01 42.80 ? 805  HOH A H2     1 
HETATM 6128 O O      . HOH H 4 .   ? 24.739 22.724 54.442 1.00 30.61 ? 806  HOH A O      1 
HETATM 6129 H H1     . HOH H 4 .   ? 25.409 23.247 54.451 0.01 36.73 ? 806  HOH A H1     1 
HETATM 6130 H H2     . HOH H 4 .   ? 24.071 23.251 54.449 0.01 36.73 ? 806  HOH A H2     1 
HETATM 6131 O O      . HOH H 4 .   ? 12.359 45.366 41.342 1.00 18.15 ? 807  HOH A O      1 
HETATM 6132 H H1     . HOH H 4 .   ? 12.990 45.767 41.746 0.01 21.78 ? 807  HOH A H1     1 
HETATM 6133 H H2     . HOH H 4 .   ? 11.721 45.929 41.348 0.01 21.78 ? 807  HOH A H2     1 
HETATM 6134 O O      . HOH H 4 .   ? 24.699 44.584 53.603 1.00 16.04 ? 808  HOH A O      1 
HETATM 6135 H H1     . HOH H 4 .   ? 25.368 45.109 53.605 0.04 19.25 ? 808  HOH A H1     1 
HETATM 6136 H H2     . HOH H 4 .   ? 24.029 45.108 53.608 0.04 19.25 ? 808  HOH A H2     1 
HETATM 6137 O O      . HOH H 4 .   ? 42.639 50.913 51.157 1.00 21.69 ? 809  HOH A O      1 
HETATM 6138 H H1     . HOH H 4 .   ? 43.485 50.990 51.165 0.01 26.02 ? 809  HOH A H1     1 
HETATM 6139 H H2     . HOH H 4 .   ? 42.470 50.597 50.386 0.01 26.02 ? 809  HOH A H2     1 
HETATM 6140 O O      . HOH H 4 .   ? 7.165  38.515 17.933 1.00 37.00 ? 810  HOH A O      1 
HETATM 6141 H H1     . HOH H 4 .   ? 7.827  39.047 17.935 0.01 44.40 ? 810  HOH A H1     1 
HETATM 6142 H H2     . HOH H 4 .   ? 6.486  39.025 17.956 0.01 44.40 ? 810  HOH A H2     1 
HETATM 6143 O O      . HOH H 4 .   ? 23.692 32.808 53.413 1.00 37.61 ? 811  HOH A O      1 
HETATM 6144 H H1     . HOH H 4 .   ? 24.172 33.508 53.425 0.01 45.13 ? 811  HOH A H1     1 
HETATM 6145 H H2     . HOH H 4 .   ? 22.925 33.080 53.660 0.01 45.13 ? 811  HOH A H2     1 
HETATM 6146 O O      . HOH H 4 .   ? 41.165 25.541 45.487 1.00 18.96 ? 812  HOH A O      1 
HETATM 6147 H H1     . HOH H 4 .   ? 41.834 26.062 45.482 0.01 22.75 ? 812  HOH A H1     1 
HETATM 6148 H H2     . HOH H 4 .   ? 40.496 26.065 45.481 0.01 22.75 ? 812  HOH A H2     1 
HETATM 6149 O O      . HOH H 4 .   ? 46.169 23.451 43.739 1.00 22.95 ? 813  HOH A O      1 
HETATM 6150 H H1     . HOH H 4 .   ? 46.709 24.108 43.724 0.01 27.55 ? 813  HOH A H1     1 
HETATM 6151 H H2     . HOH H 4 .   ? 45.402 23.818 43.733 0.01 27.55 ? 813  HOH A H2     1 
HETATM 6152 O O      . HOH H 4 .   ? 22.534 61.054 32.143 1.00 39.06 ? 814  HOH A O      1 
HETATM 6153 H H1     . HOH H 4 .   ? 23.085 61.435 31.620 0.01 46.87 ? 814  HOH A H1     1 
HETATM 6154 H H2     . HOH H 4 .   ? 21.857 61.569 32.136 0.01 46.87 ? 814  HOH A H2     1 
HETATM 6155 O O      . HOH H 4 .   ? 18.726 54.801 18.886 1.00 22.24 ? 815  HOH A O      1 
HETATM 6156 H H1     . HOH H 4 .   ? 18.234 55.369 18.487 0.04 26.69 ? 815  HOH A H1     1 
HETATM 6157 H H2     . HOH H 4 .   ? 19.050 55.237 19.538 0.02 26.69 ? 815  HOH A H2     1 
HETATM 6158 O O      . HOH H 4 .   ? 20.300 46.451 16.677 1.00 33.76 ? 816  HOH A O      1 
HETATM 6159 H H1     . HOH H 4 .   ? 20.991 46.946 16.668 0.01 40.51 ? 816  HOH A H1     1 
HETATM 6160 H H2     . HOH H 4 .   ? 19.652 47.000 16.686 0.01 40.51 ? 816  HOH A H2     1 
HETATM 6161 O O      . HOH H 4 .   ? 31.522 42.281 25.058 1.00 41.59 ? 817  HOH A O      1 
HETATM 6162 H H1     . HOH H 4 .   ? 31.658 42.202 24.223 0.01 49.91 ? 817  HOH A H1     1 
HETATM 6163 H H2     . HOH H 4 .   ? 30.725 42.573 25.108 0.01 49.91 ? 817  HOH A H2     1 
HETATM 6164 O O      . HOH H 4 .   ? 38.156 6.864  48.802 1.00 18.25 ? 818  HOH A O      1 
HETATM 6165 H H1     . HOH H 4 .   ? 38.957 6.827  49.037 0.04 21.90 ? 818  HOH A H1     1 
HETATM 6166 H H2     . HOH H 4 .   ? 38.174 6.665  47.977 0.01 21.90 ? 818  HOH A H2     1 
HETATM 6167 O O      . HOH H 4 .   ? 14.781 46.312 35.466 1.00 14.47 ? 819  HOH A O      1 
HETATM 6168 H H1     . HOH H 4 .   ? 14.124 46.987 35.331 0.06 17.37 ? 819  HOH A H1     1 
HETATM 6169 H H2     . HOH H 4 .   ? 15.390 46.633 36.095 0.02 17.37 ? 819  HOH A H2     1 
HETATM 6170 O O      . HOH H 4 .   ? 22.884 21.039 40.698 1.00 24.87 ? 820  HOH A O      1 
HETATM 6171 H H1     . HOH H 4 .   ? 23.550 21.567 40.694 0.01 29.85 ? 820  HOH A H1     1 
HETATM 6172 H H2     . HOH H 4 .   ? 22.211 21.558 40.723 0.01 29.85 ? 820  HOH A H2     1 
HETATM 6173 O O      . HOH H 4 .   ? 11.473 19.736 44.690 1.00 26.66 ? 821  HOH A O      1 
HETATM 6174 H H1     . HOH H 4 .   ? 11.876 20.294 45.190 0.01 31.99 ? 821  HOH A H1     1 
HETATM 6175 H H2     . HOH H 4 .   ? 10.665 19.997 44.698 0.01 31.99 ? 821  HOH A H2     1 
HETATM 6176 O O      . HOH H 4 .   ? 31.452 52.878 51.542 1.00 12.91 ? 822  HOH A O      1 
HETATM 6177 H H1     . HOH H 4 .   ? 32.123 53.402 51.541 0.05 15.49 ? 822  HOH A H1     1 
HETATM 6178 H H2     . HOH H 4 .   ? 30.784 53.401 51.540 0.01 15.49 ? 822  HOH A H2     1 
HETATM 6179 O O      . HOH H 4 .   ? 28.360 34.175 44.304 1.00 19.95 ? 823  HOH A O      1 
HETATM 6180 H H1     . HOH H 4 .   ? 29.045 34.210 43.802 0.04 23.95 ? 823  HOH A H1     1 
HETATM 6181 H H2     . HOH H 4 .   ? 27.722 34.448 43.814 0.03 23.95 ? 823  HOH A H2     1 
HETATM 6182 O O      . HOH H 4 .   ? 18.511 18.560 45.262 1.00 27.14 ? 824  HOH A O      1 
HETATM 6183 H H1     . HOH H 4 .   ? 19.181 19.081 45.255 0.01 32.57 ? 824  HOH A H1     1 
HETATM 6184 H H2     . HOH H 4 .   ? 17.842 19.084 45.255 0.01 32.57 ? 824  HOH A H2     1 
HETATM 6185 O O      . HOH H 4 .   ? 16.204 52.448 55.280 1.00 45.31 ? 825  HOH A O      1 
HETATM 6186 H H1     . HOH H 4 .   ? 16.898 52.938 55.281 0.01 54.38 ? 825  HOH A H1     1 
HETATM 6187 H H2     . HOH H 4 .   ? 15.586 52.969 55.543 0.01 54.38 ? 825  HOH A H2     1 
HETATM 6188 O O      . HOH H 4 .   ? 6.377  55.074 26.847 1.00 45.80 ? 826  HOH A O      1 
HETATM 6189 H H1     . HOH H 4 .   ? 7.047  55.598 26.841 0.01 54.96 ? 826  HOH A H1     1 
HETATM 6190 H H2     . HOH H 4 .   ? 5.709  55.600 26.841 0.01 54.96 ? 826  HOH A H2     1 
HETATM 6191 O O      . HOH H 4 .   ? 31.938 25.527 34.979 1.00 29.33 ? 827  HOH A O      1 
HETATM 6192 H H1     . HOH H 4 .   ? 32.630 26.022 34.955 0.01 35.20 ? 827  HOH A H1     1 
HETATM 6193 H H2     . HOH H 4 .   ? 31.293 26.072 34.890 0.01 35.20 ? 827  HOH A H2     1 
HETATM 6194 O O      . HOH H 4 .   ? 16.595 23.057 46.115 1.00 16.96 ? 828  HOH A O      1 
HETATM 6195 H H1     . HOH H 4 .   ? 17.265 23.579 46.114 0.04 20.36 ? 828  HOH A H1     1 
HETATM 6196 H H2     . HOH H 4 .   ? 15.926 23.583 46.110 0.01 20.36 ? 828  HOH A H2     1 
HETATM 6197 O O      . HOH H 4 .   ? 33.189 46.101 60.888 1.00 36.67 ? 829  HOH A O      1 
HETATM 6198 H H1     . HOH H 4 .   ? 33.450 45.680 61.579 0.01 44.01 ? 829  HOH A H1     1 
HETATM 6199 H H2     . HOH H 4 .   ? 33.711 46.769 60.846 0.01 44.01 ? 829  HOH A H2     1 
HETATM 6200 O O      . HOH H 4 .   ? 10.314 40.293 36.152 1.00 36.66 ? 830  HOH A O      1 
HETATM 6201 H H1     . HOH H 4 .   ? 11.063 40.123 35.786 0.01 43.99 ? 830  HOH A H1     1 
HETATM 6202 H H2     . HOH H 4 .   ? 9.830  40.566 35.509 0.01 43.99 ? 830  HOH A H2     1 
HETATM 6203 O O      . HOH H 4 .   ? 9.244  38.502 41.241 1.00 17.18 ? 831  HOH A O      1 
HETATM 6204 H H1     . HOH H 4 .   ? 9.888  39.021 41.040 0.01 20.62 ? 831  HOH A H1     1 
HETATM 6205 H H2     . HOH H 4 .   ? 8.550  38.954 41.050 0.01 20.62 ? 831  HOH A H2     1 
HETATM 6206 O O      . HOH H 4 .   ? 50.986 38.451 50.169 1.00 33.71 ? 832  HOH A O      1 
HETATM 6207 H H1     . HOH H 4 .   ? 51.684 38.936 50.194 0.01 40.45 ? 832  HOH A H1     1 
HETATM 6208 H H2     . HOH H 4 .   ? 50.347 39.010 50.206 0.01 40.45 ? 832  HOH A H2     1 
HETATM 6209 O O      . HOH H 4 .   ? 11.700 35.648 16.129 1.00 38.38 ? 833  HOH A O      1 
HETATM 6210 H H1     . HOH H 4 .   ? 12.536 35.777 16.044 0.01 46.06 ? 833  HOH A H1     1 
HETATM 6211 H H2     . HOH H 4 .   ? 11.444 36.293 16.620 0.01 46.06 ? 833  HOH A H2     1 
HETATM 6212 O O      . HOH H 4 .   ? 35.556 29.254 41.906 1.00 13.27 ? 834  HOH A O      1 
HETATM 6213 H H1     . HOH H 4 .   ? 35.445 30.068 42.350 0.04 15.92 ? 834  HOH A H1     1 
HETATM 6214 H H2     . HOH H 4 .   ? 36.320 29.004 42.062 0.00 15.92 ? 834  HOH A H2     1 
HETATM 6215 O O      . HOH H 4 .   ? 5.372  56.164 13.580 1.00 27.84 ? 835  HOH A O      1 
HETATM 6216 H H1     . HOH H 4 .   ? 6.064  56.614 13.788 0.01 33.41 ? 835  HOH A H1     1 
HETATM 6217 H H2     . HOH H 4 .   ? 4.738  56.726 13.638 0.01 33.41 ? 835  HOH A H2     1 
HETATM 6218 O O      . HOH H 4 .   ? 32.146 59.488 44.620 1.00 20.37 ? 836  HOH A O      1 
HETATM 6219 H H1     . HOH H 4 .   ? 32.936 59.807 44.630 0.02 24.45 ? 836  HOH A H1     1 
HETATM 6220 H H2     . HOH H 4 .   ? 31.693 60.055 45.061 0.01 24.45 ? 836  HOH A H2     1 
HETATM 6221 O O      . HOH H 4 .   ? 12.843 43.520 39.406 1.00 20.67 ? 837  HOH A O      1 
HETATM 6222 H H1     . HOH H 4 .   ? 13.398 44.161 39.337 0.01 24.80 ? 837  HOH A H1     1 
HETATM 6223 H H2     . HOH H 4 .   ? 12.088 43.889 39.287 0.01 24.80 ? 837  HOH A H2     1 
HETATM 6224 O O      . HOH H 4 .   ? 13.294 24.470 32.631 1.00 28.85 ? 838  HOH A O      1 
HETATM 6225 H H1     . HOH H 4 .   ? 12.706 24.004 32.228 0.01 34.62 ? 838  HOH A H1     1 
HETATM 6226 H H2     . HOH H 4 .   ? 13.954 23.940 32.711 0.01 34.62 ? 838  HOH A H2     1 
HETATM 6227 O O      . HOH H 4 .   ? 38.768 31.601 72.900 1.00 52.58 ? 839  HOH A O      1 
HETATM 6228 H H1     . HOH H 4 .   ? 39.121 31.978 73.575 0.01 63.10 ? 839  HOH A H1     1 
HETATM 6229 H H2     . HOH H 4 .   ? 37.997 31.956 72.850 0.01 63.10 ? 839  HOH A H2     1 
HETATM 6230 O O      . HOH H 4 .   ? 32.596 55.901 19.455 1.00 46.70 ? 840  HOH A O      1 
HETATM 6231 H H1     . HOH H 4 .   ? 33.408 56.152 19.449 0.01 56.04 ? 840  HOH A H1     1 
HETATM 6232 H H2     . HOH H 4 .   ? 32.158 56.627 19.522 0.01 56.04 ? 840  HOH A H2     1 
HETATM 6233 O O      . HOH H 4 .   ? 14.823 60.455 40.507 1.00 39.62 ? 841  HOH A O      1 
HETATM 6234 H H1     . HOH H 4 .   ? 15.523 60.774 40.145 0.01 47.54 ? 841  HOH A H1     1 
HETATM 6235 H H2     . HOH H 4 .   ? 14.278 61.107 40.509 0.01 47.54 ? 841  HOH A H2     1 
HETATM 6236 O O      . HOH H 4 .   ? 25.199 61.326 44.388 1.00 23.89 ? 842  HOH A O      1 
HETATM 6237 H H1     . HOH H 4 .   ? 25.844 61.879 44.423 0.01 28.67 ? 842  HOH A H1     1 
HETATM 6238 H H2     . HOH H 4 .   ? 24.506 61.818 44.394 0.01 28.67 ? 842  HOH A H2     1 
HETATM 6239 O O      . HOH H 4 .   ? 35.388 48.150 57.192 1.00 17.61 ? 843  HOH A O      1 
HETATM 6240 H H1     . HOH H 4 .   ? 36.044 48.145 57.732 0.01 21.14 ? 843  HOH A H1     1 
HETATM 6241 H H2     . HOH H 4 .   ? 34.759 48.509 57.639 0.04 21.14 ? 843  HOH A H2     1 
HETATM 6242 O O      . HOH H 4 .   ? 32.930 27.749 33.490 1.00 28.79 ? 844  HOH A O      1 
HETATM 6243 H H1     . HOH H 4 .   ? 33.349 28.175 32.885 0.01 34.55 ? 844  HOH A H1     1 
HETATM 6244 H H2     . HOH H 4 .   ? 32.150 28.088 33.476 0.01 34.55 ? 844  HOH A H2     1 
HETATM 6245 O O      . HOH H 4 .   ? 9.408  47.300 14.595 1.00 44.53 ? 845  HOH A O      1 
HETATM 6246 H H1     . HOH H 4 .   ? 9.909  47.926 14.314 0.01 53.44 ? 845  HOH A H1     1 
HETATM 6247 H H2     . HOH H 4 .   ? 8.635  47.516 14.317 0.01 53.44 ? 845  HOH A H2     1 
HETATM 6248 O O      . HOH H 4 .   ? 18.658 30.085 50.095 1.00 25.56 ? 846  HOH A O      1 
HETATM 6249 H H1     . HOH H 4 .   ? 19.469 29.899 50.269 0.01 30.67 ? 846  HOH A H1     1 
HETATM 6250 H H2     . HOH H 4 .   ? 18.284 30.095 50.859 0.01 30.67 ? 846  HOH A H2     1 
HETATM 6251 O O      . HOH H 4 .   ? 33.909 14.598 50.940 1.00 10.58 ? 847  HOH A O      1 
HETATM 6252 H H1     . HOH H 4 .   ? 34.579 14.790 51.472 0.01 12.70 ? 847  HOH A H1     1 
HETATM 6253 H H2     . HOH H 4 .   ? 34.167 14.749 50.077 0.04 12.70 ? 847  HOH A H2     1 
HETATM 6254 O O      . HOH H 4 .   ? 24.175 38.692 37.168 1.00 35.88 ? 848  HOH A O      1 
HETATM 6255 H H1     . HOH H 4 .   ? 24.555 39.339 37.567 0.01 43.06 ? 848  HOH A H1     1 
HETATM 6256 H H2     . HOH H 4 .   ? 23.449 39.024 36.878 0.01 43.06 ? 848  HOH A H2     1 
HETATM 6257 O O      . HOH H 4 .   ? 16.887 48.446 57.357 1.00 43.21 ? 849  HOH A O      1 
HETATM 6258 H H1     . HOH H 4 .   ? 17.556 48.971 57.371 0.01 51.86 ? 849  HOH A H1     1 
HETATM 6259 H H2     . HOH H 4 .   ? 16.216 48.968 57.370 0.01 51.86 ? 849  HOH A H2     1 
HETATM 6260 O O      . HOH H 4 .   ? 20.919 29.524 35.203 1.00 32.83 ? 850  HOH A O      1 
HETATM 6261 H H1     . HOH H 4 .   ? 21.628 29.956 35.381 0.01 39.40 ? 850  HOH A H1     1 
HETATM 6262 H H2     . HOH H 4 .   ? 20.311 29.948 35.620 0.01 39.40 ? 850  HOH A H2     1 
HETATM 6263 O O      . HOH H 4 .   ? 22.679 37.216 53.797 1.00 26.67 ? 851  HOH A O      1 
HETATM 6264 H H1     . HOH H 4 .   ? 23.344 37.745 53.782 0.01 32.01 ? 851  HOH A H1     1 
HETATM 6265 H H2     . HOH H 4 .   ? 22.004 37.733 53.808 0.01 32.01 ? 851  HOH A H2     1 
HETATM 6266 O O      . HOH H 4 .   ? 32.809 19.835 54.640 1.00 14.27 ? 852  HOH A O      1 
HETATM 6267 H H1     . HOH H 4 .   ? 33.379 20.357 54.282 0.04 17.12 ? 852  HOH A H1     1 
HETATM 6268 H H2     . HOH H 4 .   ? 32.058 20.172 54.417 0.00 17.12 ? 852  HOH A H2     1 
HETATM 6269 O O      . HOH H 4 .   ? 34.687 15.000 38.176 1.00 31.02 ? 853  HOH A O      1 
HETATM 6270 H H1     . HOH H 4 .   ? 35.403 15.306 37.837 0.01 37.23 ? 853  HOH A H1     1 
HETATM 6271 H H2     . HOH H 4 .   ? 34.090 15.554 37.932 0.01 37.23 ? 853  HOH A H2     1 
HETATM 6272 O O      . HOH H 4 .   ? 10.373 32.838 24.117 1.00 23.67 ? 854  HOH A O      1 
HETATM 6273 H H1     . HOH H 4 .   ? 10.878 33.124 23.498 0.01 28.41 ? 854  HOH A H1     1 
HETATM 6274 H H2     . HOH H 4 .   ? 9.746  33.410 24.151 0.02 28.41 ? 854  HOH A H2     1 
HETATM 6275 O O      . HOH H 4 .   ? 10.801 25.038 48.051 1.00 26.62 ? 855  HOH A O      1 
HETATM 6276 H H1     . HOH H 4 .   ? 11.450 25.502 47.759 0.01 31.95 ? 855  HOH A H1     1 
HETATM 6277 H H2     . HOH H 4 .   ? 10.141 25.572 48.028 0.01 31.95 ? 855  HOH A H2     1 
HETATM 6278 O O      . HOH H 4 .   ? 26.241 58.392 41.257 1.00 18.01 ? 856  HOH A O      1 
HETATM 6279 H H1     . HOH H 4 .   ? 26.134 59.199 41.488 0.01 21.61 ? 856  HOH A H1     1 
HETATM 6280 H H2     . HOH H 4 .   ? 25.945 57.945 41.918 0.01 21.61 ? 856  HOH A H2     1 
HETATM 6281 O O      . HOH H 4 .   ? 22.556 38.395 22.060 1.00 33.97 ? 857  HOH A O      1 
HETATM 6282 H H1     . HOH H 4 .   ? 23.269 38.770 21.790 0.01 40.76 ? 857  HOH A H1     1 
HETATM 6283 H H2     . HOH H 4 .   ? 22.204 38.974 22.573 0.01 40.76 ? 857  HOH A H2     1 
HETATM 6284 O O      . HOH H 4 .   ? 9.202  33.726 32.435 1.00 30.09 ? 858  HOH A O      1 
HETATM 6285 H H1     . HOH H 4 .   ? 9.896  34.208 32.528 0.01 36.11 ? 858  HOH A H1     1 
HETATM 6286 H H2     . HOH H 4 .   ? 8.562  34.286 32.433 0.01 36.11 ? 858  HOH A H2     1 
HETATM 6287 O O      . HOH H 4 .   ? 13.157 42.212 51.436 1.00 31.75 ? 859  HOH A O      1 
HETATM 6288 H H1     . HOH H 4 .   ? 13.685 42.655 50.938 0.01 38.10 ? 859  HOH A H1     1 
HETATM 6289 H H2     . HOH H 4 .   ? 12.445 42.678 51.441 0.01 38.10 ? 859  HOH A H2     1 
HETATM 6290 O O      . HOH H 4 .   ? 23.382 21.161 48.017 1.00 19.09 ? 860  HOH A O      1 
HETATM 6291 H H1     . HOH H 4 .   ? 24.103 21.612 48.040 0.01 22.91 ? 860  HOH A H1     1 
HETATM 6292 H H2     . HOH H 4 .   ? 22.778 21.732 48.192 0.01 22.91 ? 860  HOH A H2     1 
HETATM 6293 O O      . HOH H 4 .   ? 30.999 40.622 64.126 1.00 38.09 ? 861  HOH A O      1 
HETATM 6294 H H1     . HOH H 4 .   ? 31.663 41.153 64.123 0.01 45.70 ? 861  HOH A H1     1 
HETATM 6295 H H2     . HOH H 4 .   ? 30.325 41.139 64.123 0.01 45.70 ? 861  HOH A H2     1 
HETATM 6296 O O      . HOH H 4 .   ? 28.527 54.258 54.046 1.00 35.21 ? 862  HOH A O      1 
HETATM 6297 H H1     . HOH H 4 .   ? 29.232 54.730 53.993 0.01 42.25 ? 862  HOH A H1     1 
HETATM 6298 H H2     . HOH H 4 .   ? 27.994 54.738 54.502 0.01 42.25 ? 862  HOH A H2     1 
HETATM 6299 O O      . HOH H 4 .   ? 16.636 29.740 28.198 1.00 26.76 ? 863  HOH A O      1 
HETATM 6300 H H1     . HOH H 4 .   ? 17.307 30.261 28.183 0.01 32.11 ? 863  HOH A H1     1 
HETATM 6301 H H2     . HOH H 4 .   ? 15.969 30.267 28.183 0.01 32.11 ? 863  HOH A H2     1 
HETATM 6302 O O      . HOH H 4 .   ? 23.813 46.971 54.640 1.00 17.05 ? 864  HOH A O      1 
HETATM 6303 H H1     . HOH H 4 .   ? 24.483 47.494 54.634 0.01 20.46 ? 864  HOH A H1     1 
HETATM 6304 H H2     . HOH H 4 .   ? 23.143 47.495 54.635 0.01 20.46 ? 864  HOH A H2     1 
HETATM 6305 O O      . HOH H 4 .   ? 31.038 18.683 56.289 1.00 30.66 ? 865  HOH A O      1 
HETATM 6306 H H1     . HOH H 4 .   ? 31.566 18.202 56.873 0.01 36.79 ? 865  HOH A H1     1 
HETATM 6307 H H2     . HOH H 4 .   ? 30.744 18.256 55.508 0.01 36.79 ? 865  HOH A H2     1 
HETATM 6308 O O      . HOH H 4 .   ? 38.487 28.781 32.993 1.00 43.83 ? 866  HOH A O      1 
HETATM 6309 H H1     . HOH H 4 .   ? 39.127 29.340 32.993 0.01 52.60 ? 866  HOH A H1     1 
HETATM 6310 H H2     . HOH H 4 .   ? 37.791 29.265 33.048 0.01 52.60 ? 866  HOH A H2     1 
HETATM 6311 O O      . HOH H 4 .   ? 9.490  60.432 22.159 1.00 33.46 ? 867  HOH A O      1 
HETATM 6312 H H1     . HOH H 4 .   ? 9.408  61.218 21.843 0.01 40.16 ? 867  HOH A H1     1 
HETATM 6313 H H2     . HOH H 4 .   ? 8.690  60.146 22.199 0.01 40.16 ? 867  HOH A H2     1 
HETATM 6314 O O      . HOH H 4 .   ? 10.443 32.873 34.886 1.00 25.15 ? 868  HOH A O      1 
HETATM 6315 H H1     . HOH H 4 .   ? 11.113 33.396 34.887 0.01 30.18 ? 868  HOH A H1     1 
HETATM 6316 H H2     . HOH H 4 .   ? 9.775  33.397 34.887 0.01 30.18 ? 868  HOH A H2     1 
HETATM 6317 O O      . HOH H 4 .   ? 25.202 14.381 47.145 1.00 21.05 ? 869  HOH A O      1 
HETATM 6318 H H1     . HOH H 4 .   ? 24.692 15.046 47.282 0.04 25.26 ? 869  HOH A H1     1 
HETATM 6319 H H2     . HOH H 4 .   ? 25.433 14.463 46.331 0.02 25.26 ? 869  HOH A H2     1 
HETATM 6320 O O      . HOH H 4 .   ? 16.276 57.248 18.370 1.00 24.01 ? 870  HOH A O      1 
HETATM 6321 H H1     . HOH H 4 .   ? 16.942 57.776 18.373 0.01 28.82 ? 870  HOH A H1     1 
HETATM 6322 H H2     . HOH H 4 .   ? 15.603 57.767 18.373 0.02 28.82 ? 870  HOH A H2     1 
HETATM 6323 O O      . HOH H 4 .   ? 19.226 49.835 13.954 1.00 33.20 ? 871  HOH A O      1 
HETATM 6324 H H1     . HOH H 4 .   ? 20.056 49.997 13.869 0.01 39.83 ? 871  HOH A H1     1 
HETATM 6325 H H2     . HOH H 4 .   ? 18.855 50.374 13.412 0.01 39.83 ? 871  HOH A H2     1 
HETATM 6326 O O      . HOH H 4 .   ? 18.069 45.294 54.725 1.00 21.29 ? 872  HOH A O      1 
HETATM 6327 H H1     . HOH H 4 .   ? 18.899 45.446 54.829 0.02 25.55 ? 872  HOH A H1     1 
HETATM 6328 H H2     . HOH H 4 .   ? 17.750 46.047 54.494 0.01 25.55 ? 872  HOH A H2     1 
HETATM 6329 O O      . HOH H 4 .   ? 27.988 9.412  47.938 1.00 25.20 ? 873  HOH A O      1 
HETATM 6330 H H1     . HOH H 4 .   ? 28.492 10.097 47.931 0.01 30.25 ? 873  HOH A H1     1 
HETATM 6331 H H2     . HOH H 4 .   ? 27.262 9.691  47.593 0.01 30.25 ? 873  HOH A H2     1 
HETATM 6332 O O      . HOH H 4 .   ? 29.481 21.982 59.955 1.00 39.40 ? 874  HOH A O      1 
HETATM 6333 H H1     . HOH H 4 .   ? 30.092 22.573 59.945 0.01 47.28 ? 874  HOH A H1     1 
HETATM 6334 H H2     . HOH H 4 .   ? 28.776 22.414 59.757 0.01 47.28 ? 874  HOH A H2     1 
HETATM 6335 O O      . HOH H 4 .   ? 25.801 32.007 62.128 1.00 23.59 ? 875  HOH A O      1 
HETATM 6336 H H1     . HOH H 4 .   ? 26.477 32.525 62.129 0.01 28.31 ? 875  HOH A H1     1 
HETATM 6337 H H2     . HOH H 4 .   ? 25.138 32.539 62.123 0.01 28.31 ? 875  HOH A H2     1 
HETATM 6338 O O      . HOH H 4 .   ? 7.573  40.432 27.704 1.00 30.71 ? 876  HOH A O      1 
HETATM 6339 H H1     . HOH H 4 .   ? 8.278  40.903 27.764 0.01 36.85 ? 876  HOH A H1     1 
HETATM 6340 H H2     . HOH H 4 .   ? 7.017  40.833 28.206 0.01 36.85 ? 876  HOH A H2     1 
HETATM 6341 O O      . HOH H 4 .   ? 30.969 60.412 47.853 1.00 18.13 ? 877  HOH A O      1 
HETATM 6342 H H1     . HOH H 4 .   ? 31.499 61.075 47.900 0.01 21.75 ? 877  HOH A H1     1 
HETATM 6343 H H2     . HOH H 4 .   ? 30.198 60.765 47.851 0.02 21.75 ? 877  HOH A H2     1 
HETATM 6344 O O      . HOH H 4 .   ? 14.831 54.486 45.566 1.00 55.73 ? 878  HOH A O      1 
HETATM 6345 H H1     . HOH H 4 .   ? 15.302 55.004 46.048 0.01 66.88 ? 878  HOH A H1     1 
HETATM 6346 H H2     . HOH H 4 .   ? 14.058 54.840 45.586 0.01 66.88 ? 878  HOH A H2     1 
HETATM 6347 O O      . HOH H 4 .   ? 34.725 33.943 36.455 1.00 34.95 ? 879  HOH A O      1 
HETATM 6348 H H1     . HOH H 4 .   ? 35.401 34.458 36.457 0.01 41.94 ? 879  HOH A H1     1 
HETATM 6349 H H2     . HOH H 4 .   ? 34.061 34.473 36.457 0.01 41.94 ? 879  HOH A H2     1 
HETATM 6350 O O      . HOH H 4 .   ? 29.070 35.024 67.498 1.00 30.46 ? 880  HOH A O      1 
HETATM 6351 H H1     . HOH H 4 .   ? 29.776 35.424 67.751 0.01 36.56 ? 880  HOH A H1     1 
HETATM 6352 H H2     . HOH H 4 .   ? 28.476 35.633 67.509 0.01 36.56 ? 880  HOH A H2     1 
HETATM 6353 O O      . HOH H 4 .   ? 20.934 58.212 55.555 1.00 31.12 ? 881  HOH A O      1 
HETATM 6354 H H1     . HOH H 4 .   ? 21.611 58.705 55.699 0.01 37.34 ? 881  HOH A H1     1 
HETATM 6355 H H2     . HOH H 4 .   ? 20.282 58.758 55.546 0.01 37.34 ? 881  HOH A H2     1 
HETATM 6356 O O      . HOH H 4 .   ? 28.833 32.989 41.958 1.00 32.15 ? 882  HOH A O      1 
HETATM 6357 H H1     . HOH H 4 .   ? 28.807 32.468 42.624 0.01 38.58 ? 882  HOH A H1     1 
HETATM 6358 H H2     . HOH H 4 .   ? 28.476 33.710 42.230 0.01 38.58 ? 882  HOH A H2     1 
HETATM 6359 O O      . HOH H 4 .   ? 22.838 25.743 47.798 1.00 24.85 ? 883  HOH A O      1 
HETATM 6360 H H1     . HOH H 4 .   ? 23.128 26.266 48.400 0.01 29.82 ? 883  HOH A H1     1 
HETATM 6361 H H2     . HOH H 4 .   ? 22.018 25.955 47.719 0.01 29.82 ? 883  HOH A H2     1 
HETATM 6362 O O      . HOH H 4 .   ? 27.400 57.732 31.604 1.00 32.51 ? 884  HOH A O      1 
HETATM 6363 H H1     . HOH H 4 .   ? 28.103 58.211 31.607 0.01 39.01 ? 884  HOH A H1     1 
HETATM 6364 H H2     . HOH H 4 .   ? 26.800 58.249 31.911 0.01 39.01 ? 884  HOH A H2     1 
HETATM 6365 O O      . HOH H 4 .   ? 44.635 31.135 49.987 1.00 33.46 ? 885  HOH A O      1 
HETATM 6366 H H1     . HOH H 4 .   ? 44.455 31.707 49.385 0.01 40.16 ? 885  HOH A H1     1 
HETATM 6367 H H2     . HOH H 4 .   ? 43.906 30.710 50.088 0.01 40.16 ? 885  HOH A H2     1 
HETATM 6368 O O      . HOH H 4 .   ? 30.856 28.536 69.385 1.00 36.37 ? 886  HOH A O      1 
HETATM 6369 H H1     . HOH H 4 .   ? 31.550 28.444 68.903 0.01 43.65 ? 886  HOH A H1     1 
HETATM 6370 H H2     . HOH H 4 .   ? 30.443 29.186 69.022 0.01 43.65 ? 886  HOH A H2     1 
HETATM 6371 O O      . HOH H 4 .   ? 28.009 49.143 56.426 1.00 28.34 ? 887  HOH A O      1 
HETATM 6372 H H1     . HOH H 4 .   ? 28.055 49.827 55.896 0.01 34.00 ? 887  HOH A H1     1 
HETATM 6373 H H2     . HOH H 4 .   ? 27.370 49.336 56.988 0.01 34.00 ? 887  HOH A H2     1 
HETATM 6374 O O      . HOH H 4 .   ? 43.288 38.517 63.138 1.00 38.05 ? 888  HOH A O      1 
HETATM 6375 H H1     . HOH H 4 .   ? 43.965 39.030 63.128 0.01 45.66 ? 888  HOH A H1     1 
HETATM 6376 H H2     . HOH H 4 .   ? 42.627 39.052 63.128 0.01 45.66 ? 888  HOH A H2     1 
HETATM 6377 O O      . HOH H 4 .   ? 15.703 51.358 51.210 1.00 32.64 ? 889  HOH A O      1 
HETATM 6378 H H1     . HOH H 4 .   ? 16.029 51.388 51.994 0.01 39.17 ? 889  HOH A H1     1 
HETATM 6379 H H2     . HOH H 4 .   ? 14.892 51.588 51.317 0.01 39.17 ? 889  HOH A H2     1 
HETATM 6380 O O      . HOH H 4 .   ? 5.317  43.946 27.974 1.00 33.60 ? 890  HOH A O      1 
HETATM 6381 H H1     . HOH H 4 .   ? 5.883  44.549 27.773 0.01 40.32 ? 890  HOH A H1     1 
HETATM 6382 H H2     . HOH H 4 .   ? 4.571  44.351 27.950 0.01 40.32 ? 890  HOH A H2     1 
HETATM 6383 O O      . HOH H 4 .   ? 33.809 34.664 40.843 1.00 42.67 ? 891  HOH A O      1 
HETATM 6384 H H1     . HOH H 4 .   ? 34.245 34.818 40.129 0.01 51.20 ? 891  HOH A H1     1 
HETATM 6385 H H2     . HOH H 4 .   ? 33.806 33.817 40.905 0.01 51.20 ? 891  HOH A H2     1 
HETATM 6386 O O      . HOH H 4 .   ? 7.927  43.140 28.705 1.00 23.11 ? 892  HOH A O      1 
HETATM 6387 H H1     . HOH H 4 .   ? 8.232  43.295 29.483 0.01 27.74 ? 892  HOH A H1     1 
HETATM 6388 H H2     . HOH H 4 .   ? 7.084  43.181 28.803 0.01 27.74 ? 892  HOH A H2     1 
HETATM 6389 O O      . HOH H 4 .   ? 13.362 60.834 26.526 1.00 41.66 ? 893  HOH A O      1 
HETATM 6390 H H1     . HOH H 4 .   ? 14.024 61.367 26.550 0.01 49.99 ? 893  HOH A H1     1 
HETATM 6391 H H2     . HOH H 4 .   ? 12.686 61.349 26.550 0.01 49.99 ? 893  HOH A H2     1 
HETATM 6392 O O      . HOH H 4 .   ? 8.311  25.105 38.500 1.00 33.35 ? 894  HOH A O      1 
HETATM 6393 H H1     . HOH H 4 .   ? 8.897  25.567 38.909 0.01 40.01 ? 894  HOH A H1     1 
HETATM 6394 H H2     . HOH H 4 .   ? 7.616  25.594 38.518 0.01 40.01 ? 894  HOH A H2     1 
HETATM 6395 O O      . HOH H 4 .   ? 9.027  48.143 34.597 1.00 23.25 ? 895  HOH A O      1 
HETATM 6396 H H1     . HOH H 4 .   ? 9.294  48.274 35.393 0.01 27.90 ? 895  HOH A H1     1 
HETATM 6397 H H2     . HOH H 4 .   ? 8.344  48.644 34.522 0.01 27.90 ? 895  HOH A H2     1 
HETATM 6398 O O      . HOH H 4 .   ? 24.683 64.724 38.237 1.00 41.23 ? 896  HOH A O      1 
HETATM 6399 H H1     . HOH H 4 .   ? 25.352 65.249 38.252 0.01 49.48 ? 896  HOH A H1     1 
HETATM 6400 H H2     . HOH H 4 .   ? 24.013 65.247 38.252 0.01 49.48 ? 896  HOH A H2     1 
HETATM 6401 O O      . HOH H 4 .   ? 7.607  19.764 42.580 1.00 42.13 ? 897  HOH A O      1 
HETATM 6402 H H1     . HOH H 4 .   ? 8.176  20.393 42.636 0.01 50.55 ? 897  HOH A H1     1 
HETATM 6403 H H2     . HOH H 4 .   ? 6.894  20.106 42.891 0.01 50.55 ? 897  HOH A H2     1 
HETATM 6404 O O      . HOH H 4 .   ? 9.325  38.015 26.433 1.00 37.65 ? 898  HOH A O      1 
HETATM 6405 H H1     . HOH H 4 .   ? 9.803  38.593 26.831 0.01 45.18 ? 898  HOH A H1     1 
HETATM 6406 H H2     . HOH H 4 .   ? 8.541  38.343 26.460 0.01 45.18 ? 898  HOH A H2     1 
HETATM 6407 O O      . HOH H 4 .   ? 44.044 39.696 44.071 1.00 23.02 ? 899  HOH A O      1 
HETATM 6408 H H1     . HOH H 4 .   ? 44.619 40.311 44.176 0.01 27.62 ? 899  HOH A H1     1 
HETATM 6409 H H2     . HOH H 4 .   ? 43.325 40.033 44.376 0.01 27.62 ? 899  HOH A H2     1 
HETATM 6410 O O      . HOH H 4 .   ? 28.609 12.988 55.168 1.00 30.48 ? 900  HOH A O      1 
HETATM 6411 H H1     . HOH H 4 .   ? 28.343 12.765 54.393 0.02 36.58 ? 900  HOH A H1     1 
HETATM 6412 H H2     . HOH H 4 .   ? 28.204 12.457 55.691 0.01 36.58 ? 900  HOH A H2     1 
HETATM 6413 O O      . HOH H 4 .   ? 9.605  26.929 32.868 1.00 26.85 ? 901  HOH A O      1 
HETATM 6414 H H1     . HOH H 4 .   ? 10.303 27.316 32.577 0.01 32.22 ? 901  HOH A H1     1 
HETATM 6415 H H2     . HOH H 4 .   ? 9.144  27.560 33.201 0.01 32.22 ? 901  HOH A H2     1 
HETATM 6416 O O      . HOH H 4 .   ? 27.809 38.035 62.935 1.00 46.72 ? 902  HOH A O      1 
HETATM 6417 H H1     . HOH H 4 .   ? 28.424 38.621 62.935 0.01 56.07 ? 902  HOH A H1     1 
HETATM 6418 H H2     . HOH H 4 .   ? 27.093 38.489 62.869 0.01 56.07 ? 902  HOH A H2     1 
HETATM 6419 O O      . HOH H 4 .   ? 31.872 58.653 21.475 1.00 47.17 ? 903  HOH A O      1 
HETATM 6420 H H1     . HOH H 4 .   ? 32.663 58.961 21.415 0.01 56.61 ? 903  HOH A H1     1 
HETATM 6421 H H2     . HOH H 4 .   ? 31.391 59.257 21.119 0.01 56.61 ? 903  HOH A H2     1 
HETATM 6422 O O      . HOH H 4 .   ? 10.295 20.214 37.492 1.00 42.76 ? 904  HOH A O      1 
HETATM 6423 H H1     . HOH H 4 .   ? 10.924 20.706 37.781 0.01 51.32 ? 904  HOH A H1     1 
HETATM 6424 H H2     . HOH H 4 .   ? 9.613  20.721 37.515 0.01 51.32 ? 904  HOH A H2     1 
HETATM 6425 O O      . HOH H 4 .   ? 34.721 36.278 42.927 1.00 30.64 ? 905  HOH A O      1 
HETATM 6426 H H1     . HOH H 4 .   ? 35.456 36.515 43.281 0.01 36.77 ? 905  HOH A H1     1 
HETATM 6427 H H2     . HOH H 4 .   ? 34.220 36.958 43.025 0.01 36.77 ? 905  HOH A H2     1 
HETATM 6428 O O      . HOH H 4 .   ? 45.054 54.005 31.375 1.00 49.19 ? 906  HOH A O      1 
HETATM 6429 H H1     . HOH H 4 .   ? 44.789 54.768 31.108 0.01 59.03 ? 906  HOH A H1     1 
HETATM 6430 H H2     . HOH H 4 .   ? 44.726 53.943 32.158 0.01 59.03 ? 906  HOH A H2     1 
HETATM 6431 O O      . HOH H 4 .   ? 26.754 36.006 35.632 1.00 50.22 ? 907  HOH A O      1 
HETATM 6432 H H1     . HOH H 4 .   ? 27.422 36.530 35.616 0.01 60.27 ? 907  HOH A H1     1 
HETATM 6433 H H2     . HOH H 4 .   ? 26.084 36.530 35.616 0.01 60.27 ? 907  HOH A H2     1 
HETATM 6434 O O      . HOH H 4 .   ? 16.834 18.810 40.071 1.00 19.41 ? 908  HOH A O      1 
HETATM 6435 H H1     . HOH H 4 .   ? 17.446 19.337 39.806 0.01 23.30 ? 908  HOH A H1     1 
HETATM 6436 H H2     . HOH H 4 .   ? 16.197 18.945 39.525 0.01 23.30 ? 908  HOH A H2     1 
HETATM 6437 O O      . HOH H 4 .   ? 23.644 38.944 57.839 1.00 24.63 ? 909  HOH A O      1 
HETATM 6438 H H1     . HOH H 4 .   ? 24.388 39.227 58.138 0.01 29.56 ? 909  HOH A H1     1 
HETATM 6439 H H2     . HOH H 4 .   ? 23.068 39.435 58.227 0.01 29.56 ? 909  HOH A H2     1 
HETATM 6440 O O      . HOH H 4 .   ? 18.363 57.187 16.087 1.00 37.58 ? 910  HOH A O      1 
HETATM 6441 H H1     . HOH H 4 .   ? 18.679 57.461 15.347 0.01 45.10 ? 910  HOH A H1     1 
HETATM 6442 H H2     . HOH H 4 .   ? 17.548 57.427 16.062 0.01 45.10 ? 910  HOH A H2     1 
HETATM 6443 O O      . HOH H 4 .   ? 20.960 20.317 46.912 1.00 23.92 ? 911  HOH A O      1 
HETATM 6444 H H1     . HOH H 4 .   ? 21.618 20.813 46.703 0.01 28.70 ? 911  HOH A H1     1 
HETATM 6445 H H2     . HOH H 4 .   ? 20.290 20.837 46.863 0.01 28.70 ? 911  HOH A H2     1 
HETATM 6446 O O      . HOH H 4 .   ? 30.282 45.465 43.372 1.00 25.64 ? 912  HOH A O      1 
HETATM 6447 H H1     . HOH H 4 .   ? 30.984 45.939 43.448 0.01 30.77 ? 912  HOH A H1     1 
HETATM 6448 H H2     . HOH H 4 .   ? 29.649 46.032 43.383 0.01 30.77 ? 912  HOH A H2     1 
HETATM 6449 O O      . HOH H 4 .   ? 40.942 54.458 41.813 1.00 30.04 ? 913  HOH A O      1 
HETATM 6450 H H1     . HOH H 4 .   ? 41.178 54.810 40.977 0.01 36.05 ? 913  HOH A H1     1 
HETATM 6451 H H2     . HOH H 4 .   ? 40.792 54.930 42.559 0.01 36.05 ? 913  HOH A H2     1 
HETATM 6452 O O      . HOH H 4 .   ? 27.445 32.543 39.595 1.00 18.10 ? 914  HOH A O      1 
HETATM 6453 H H1     . HOH H 4 .   ? 27.965 33.215 39.598 0.04 21.72 ? 914  HOH A H1     1 
HETATM 6454 H H2     . HOH H 4 .   ? 26.668 32.884 39.639 0.01 21.72 ? 914  HOH A H2     1 
HETATM 6455 O O      . HOH H 4 .   ? 24.553 40.589 19.774 1.00 39.26 ? 915  HOH A O      1 
HETATM 6456 H H1     . HOH H 4 .   ? 25.175 41.168 19.759 0.01 47.11 ? 915  HOH A H1     1 
HETATM 6457 H H2     . HOH H 4 .   ? 23.938 40.938 19.302 0.01 47.11 ? 915  HOH A H2     1 
HETATM 6458 O O      . HOH H 4 .   ? 38.909 50.592 49.052 1.00 21.89 ? 916  HOH A O      1 
HETATM 6459 H H1     . HOH H 4 .   ? 39.530 51.159 49.181 0.01 26.27 ? 916  HOH A H1     1 
HETATM 6460 H H2     . HOH H 4 .   ? 38.202 51.062 49.048 0.01 26.27 ? 916  HOH A H2     1 
HETATM 6461 O O      . HOH H 4 .   ? 18.812 60.037 24.762 1.00 19.67 ? 917  HOH A O      1 
HETATM 6462 H H1     . HOH H 4 .   ? 19.166 59.676 24.079 0.04 23.60 ? 917  HOH A H1     1 
HETATM 6463 H H2     . HOH H 4 .   ? 19.407 60.579 25.022 0.01 23.60 ? 917  HOH A H2     1 
HETATM 6464 O O      . HOH H 4 .   ? 11.258 36.643 33.922 1.00 25.79 ? 918  HOH A O      1 
HETATM 6465 H H1     . HOH H 4 .   ? 11.812 37.225 34.199 0.01 30.95 ? 918  HOH A H1     1 
HETATM 6466 H H2     . HOH H 4 .   ? 10.515 37.055 33.914 0.01 30.95 ? 918  HOH A H2     1 
HETATM 6467 O O      . HOH H 4 .   ? 38.176 60.558 37.655 1.00 39.94 ? 919  HOH A O      1 
HETATM 6468 H H1     . HOH H 4 .   ? 38.835 61.096 37.662 0.01 47.93 ? 919  HOH A H1     1 
HETATM 6469 H H2     . HOH H 4 .   ? 37.498 61.071 37.662 0.01 47.93 ? 919  HOH A H2     1 
HETATM 6470 O O      . HOH H 4 .   ? 37.898 24.040 34.643 1.00 31.85 ? 920  HOH A O      1 
HETATM 6471 H H1     . HOH H 4 .   ? 38.544 24.520 34.371 0.01 38.22 ? 920  HOH A H1     1 
HETATM 6472 H H2     . HOH H 4 .   ? 37.209 24.433 34.336 0.01 38.22 ? 920  HOH A H2     1 
HETATM 6473 O O      . HOH H 4 .   ? 19.288 26.031 34.200 1.00 41.52 ? 921  HOH A O      1 
HETATM 6474 H H1     . HOH H 4 .   ? 19.770 26.285 33.546 0.01 49.83 ? 921  HOH A H1     1 
HETATM 6475 H H2     . HOH H 4 .   ? 18.765 25.458 33.852 0.01 49.83 ? 921  HOH A H2     1 
HETATM 6476 O O      . HOH H 4 .   ? 20.604 36.990 23.706 1.00 30.93 ? 922  HOH A O      1 
HETATM 6477 H H1     . HOH H 4 .   ? 21.452 37.039 23.665 0.01 37.11 ? 922  HOH A H1     1 
HETATM 6478 H H2     . HOH H 4 .   ? 20.374 37.735 24.045 0.01 37.11 ? 922  HOH A H2     1 
HETATM 6479 O O      . HOH H 4 .   ? 30.755 39.892 26.780 1.00 46.12 ? 923  HOH A O      1 
HETATM 6480 H H1     . HOH H 4 .   ? 31.515 40.271 26.793 0.01 55.34 ? 923  HOH A H1     1 
HETATM 6481 H H2     . HOH H 4 .   ? 30.325 40.318 26.183 0.01 55.34 ? 923  HOH A H2     1 
HETATM 6482 O O      . HOH H 4 .   ? 25.698 24.660 36.927 1.00 25.91 ? 924  HOH A O      1 
HETATM 6483 H H1     . HOH H 4 .   ? 26.470 25.013 36.945 0.01 31.09 ? 924  HOH A H1     1 
HETATM 6484 H H2     . HOH H 4 .   ? 25.168 25.324 36.936 0.02 31.09 ? 924  HOH A H2     1 
HETATM 6485 O O      . HOH H 4 .   ? 38.342 46.044 44.800 1.00 30.12 ? 925  HOH A O      1 
HETATM 6486 H H1     . HOH H 4 .   ? 39.004 46.578 44.807 0.01 36.14 ? 925  HOH A H1     1 
HETATM 6487 H H2     . HOH H 4 .   ? 37.666 46.560 44.807 0.01 36.14 ? 925  HOH A H2     1 
HETATM 6488 O O      . HOH H 4 .   ? 41.211 57.215 31.356 1.00 47.34 ? 926  HOH A O      1 
HETATM 6489 H H1     . HOH H 4 .   ? 41.882 57.736 31.375 0.01 56.81 ? 926  HOH A H1     1 
HETATM 6490 H H2     . HOH H 4 .   ? 40.544 57.742 31.375 0.01 56.81 ? 926  HOH A H2     1 
HETATM 6491 O O      . HOH H 4 .   ? 16.576 58.951 34.801 1.00 33.35 ? 927  HOH A O      1 
HETATM 6492 H H1     . HOH H 4 .   ? 16.899 59.651 35.159 0.01 40.02 ? 927  HOH A H1     1 
HETATM 6493 H H2     . HOH H 4 .   ? 15.744 59.115 34.746 0.01 40.02 ? 927  HOH A H2     1 
HETATM 6494 O O      . HOH H 4 .   ? 9.089  27.326 39.402 1.00 25.77 ? 928  HOH A O      1 
HETATM 6495 H H1     . HOH H 4 .   ? 9.918  27.429 39.557 0.01 30.92 ? 928  HOH A H1     1 
HETATM 6496 H H2     . HOH H 4 .   ? 8.709  27.778 40.014 0.01 30.92 ? 928  HOH A H2     1 
HETATM 6497 O O      . HOH H 4 .   ? 36.538 39.054 44.788 1.00 29.42 ? 929  HOH A O      1 
HETATM 6498 H H1     . HOH H 4 .   ? 37.246 39.525 44.767 0.01 35.31 ? 929  HOH A H1     1 
HETATM 6499 H H2     . HOH H 4 .   ? 35.963 39.533 44.385 0.01 35.31 ? 929  HOH A H2     1 
HETATM 6500 O O      . HOH H 4 .   ? 44.232 49.746 53.152 1.00 17.12 ? 930  HOH A O      1 
HETATM 6501 H H1     . HOH H 4 .   ? 44.864 50.312 53.150 0.01 20.54 ? 930  HOH A H1     1 
HETATM 6502 H H2     . HOH H 4 .   ? 43.529 50.223 53.119 0.01 20.54 ? 930  HOH A H2     1 
HETATM 6503 O O      . HOH H 4 .   ? 31.939 13.322 42.191 1.00 15.34 ? 931  HOH A O      1 
HETATM 6504 H H1     . HOH H 4 .   ? 32.601 13.840 42.071 0.01 18.41 ? 931  HOH A H1     1 
HETATM 6505 H H2     . HOH H 4 .   ? 31.300 13.846 42.393 0.04 18.41 ? 931  HOH A H2     1 
HETATM 6506 O O      . HOH H 4 .   ? 20.012 23.732 49.437 1.00 26.04 ? 932  HOH A O      1 
HETATM 6507 H H1     . HOH H 4 .   ? 20.086 23.875 48.602 0.01 31.24 ? 932  HOH A H1     1 
HETATM 6508 H H2     . HOH H 4 .   ? 20.331 24.436 49.786 0.01 31.24 ? 932  HOH A H2     1 
HETATM 6509 O O      . HOH H 4 .   ? 39.741 47.820 36.456 1.00 43.51 ? 933  HOH A O      1 
HETATM 6510 H H1     . HOH H 4 .   ? 40.522 47.862 36.788 0.01 52.22 ? 933  HOH A H1     1 
HETATM 6511 H H2     . HOH H 4 .   ? 39.241 48.115 37.077 0.01 52.22 ? 933  HOH A H2     1 
HETATM 6512 O O      . HOH H 4 .   ? 3.940  33.683 27.096 1.00 46.33 ? 934  HOH A O      1 
HETATM 6513 H H1     . HOH H 4 .   ? 4.496  34.282 27.329 0.01 55.60 ? 934  HOH A H1     1 
HETATM 6514 H H2     . HOH H 4 .   ? 3.187  34.076 27.135 0.01 55.60 ? 934  HOH A H2     1 
HETATM 6515 O O      . HOH H 4 .   ? 50.238 36.870 60.402 1.00 43.88 ? 935  HOH A O      1 
HETATM 6516 H H1     . HOH H 4 .   ? 50.907 37.393 60.398 0.01 52.66 ? 935  HOH A H1     1 
HETATM 6517 H H2     . HOH H 4 .   ? 49.569 37.394 60.398 0.01 52.66 ? 935  HOH A H2     1 
HETATM 6518 O O      . HOH H 4 .   ? 31.475 43.377 42.533 1.00 43.38 ? 936  HOH A O      1 
HETATM 6519 H H1     . HOH H 4 .   ? 31.440 43.866 43.226 0.01 52.06 ? 936  HOH A H1     1 
HETATM 6520 H H2     . HOH H 4 .   ? 32.279 43.110 42.531 0.01 52.06 ? 936  HOH A H2     1 
HETATM 6521 O O      . HOH H 4 .   ? 14.557 45.691 14.787 1.00 46.54 ? 937  HOH A O      1 
HETATM 6522 H H1     . HOH H 4 .   ? 14.961 45.748 15.534 0.01 55.85 ? 937  HOH A H1     1 
HETATM 6523 H H2     . HOH H 4 .   ? 13.753 45.889 14.974 0.01 55.85 ? 937  HOH A H2     1 
HETATM 6524 O O      . HOH H 4 .   ? 45.638 21.265 42.482 1.00 30.02 ? 938  HOH A O      1 
HETATM 6525 H H1     . HOH H 4 .   ? 46.270 21.538 41.985 0.01 36.03 ? 938  HOH A H1     1 
HETATM 6526 H H2     . HOH H 4 .   ? 45.174 21.964 42.623 0.01 36.03 ? 938  HOH A H2     1 
HETATM 6527 O O      . HOH H 4 .   ? 16.513 34.478 18.439 1.00 46.40 ? 939  HOH A O      1 
HETATM 6528 H H1     . HOH H 4 .   ? 16.385 34.838 17.680 0.01 55.68 ? 939  HOH A H1     1 
HETATM 6529 H H2     . HOH H 4 .   ? 15.798 34.645 18.868 0.01 55.68 ? 939  HOH A H2     1 
HETATM 6530 O O      . HOH H 4 .   ? 24.441 26.308 56.067 1.00 23.38 ? 940  HOH A O      1 
HETATM 6531 H H1     . HOH H 4 .   ? 24.676 26.626 56.819 0.01 28.06 ? 940  HOH A H1     1 
HETATM 6532 H H2     . HOH H 4 .   ? 23.610 26.480 56.022 0.03 28.06 ? 940  HOH A H2     1 
HETATM 6533 O O      . HOH H 4 .   ? 22.397 40.755 37.480 1.00 26.54 ? 941  HOH A O      1 
HETATM 6534 H H1     . HOH H 4 .   ? 22.053 41.068 38.191 0.03 31.85 ? 941  HOH A H1     1 
HETATM 6535 H H2     . HOH H 4 .   ? 21.864 40.132 37.257 0.01 31.85 ? 941  HOH A H2     1 
HETATM 6536 O O      . HOH H 4 .   ? 39.396 49.213 39.866 1.00 36.00 ? 942  HOH A O      1 
HETATM 6537 H H1     . HOH H 4 .   ? 40.062 49.740 39.862 0.01 43.20 ? 942  HOH A H1     1 
HETATM 6538 H H2     . HOH H 4 .   ? 38.722 49.732 39.862 0.01 43.20 ? 942  HOH A H2     1 
HETATM 6539 O O      . HOH H 4 .   ? 28.227 22.608 36.835 1.00 27.60 ? 943  HOH A O      1 
HETATM 6540 H H1     . HOH H 4 .   ? 28.920 23.095 36.901 0.01 33.12 ? 943  HOH A H1     1 
HETATM 6541 H H2     . HOH H 4 .   ? 27.584 23.163 36.851 0.01 33.12 ? 943  HOH A H2     1 
HETATM 6542 O O      . HOH H 4 .   ? 45.164 29.885 54.614 1.00 38.42 ? 944  HOH A O      1 
HETATM 6543 H H1     . HOH H 4 .   ? 45.856 30.380 54.607 0.01 46.11 ? 944  HOH A H1     1 
HETATM 6544 H H2     . HOH H 4 .   ? 44.520 30.432 54.526 0.01 46.11 ? 944  HOH A H2     1 
HETATM 6545 O O      . HOH H 4 .   ? 40.060 36.356 63.438 1.00 31.08 ? 945  HOH A O      1 
HETATM 6546 H H1     . HOH H 4 .   ? 40.731 36.879 63.432 0.01 37.30 ? 945  HOH A H1     1 
HETATM 6547 H H2     . HOH H 4 .   ? 39.392 36.882 63.432 0.01 37.30 ? 945  HOH A H2     1 
HETATM 6548 O O      . HOH H 4 .   ? 19.824 51.406 57.171 1.00 30.98 ? 946  HOH A O      1 
HETATM 6549 H H1     . HOH H 4 .   ? 20.490 51.934 57.148 0.01 37.18 ? 946  HOH A H1     1 
HETATM 6550 H H2     . HOH H 4 .   ? 19.150 51.925 57.149 0.01 37.18 ? 946  HOH A H2     1 
HETATM 6551 O O      . HOH H 4 .   ? 20.090 58.375 45.061 1.00 28.47 ? 947  HOH A O      1 
HETATM 6552 H H1     . HOH H 4 .   ? 20.869 58.715 45.070 0.01 34.16 ? 947  HOH A H1     1 
HETATM 6553 H H2     . HOH H 4 .   ? 19.582 59.035 44.891 0.01 34.16 ? 947  HOH A H2     1 
HETATM 6554 O O      . HOH H 4 .   ? 17.263 42.552 54.574 1.00 27.98 ? 948  HOH A O      1 
HETATM 6555 H H1     . HOH H 4 .   ? 17.935 43.073 54.573 0.01 33.58 ? 948  HOH A H1     1 
HETATM 6556 H H2     . HOH H 4 .   ? 16.596 43.079 54.573 0.01 33.58 ? 948  HOH A H2     1 
HETATM 6557 O O      . HOH H 4 .   ? 44.571 22.364 53.960 1.00 23.45 ? 949  HOH A O      1 
HETATM 6558 H H1     . HOH H 4 .   ? 45.382 22.578 53.826 0.01 28.14 ? 949  HOH A H1     1 
HETATM 6559 H H2     . HOH H 4 .   ? 44.301 22.932 54.532 0.01 28.14 ? 949  HOH A H2     1 
HETATM 6560 O O      . HOH H 4 .   ? 34.722 18.592 37.237 1.00 26.43 ? 950  HOH A O      1 
HETATM 6561 H H1     . HOH H 4 .   ? 35.469 18.997 37.237 0.01 31.71 ? 950  HOH A H1     1 
HETATM 6562 H H2     . HOH H 4 .   ? 34.171 19.180 36.966 0.01 31.71 ? 950  HOH A H2     1 
HETATM 6563 O O      . HOH H 4 .   ? 11.400 48.882 41.159 1.00 35.64 ? 951  HOH A O      1 
HETATM 6564 H H1     . HOH H 4 .   ? 11.805 49.605 41.350 0.01 42.77 ? 951  HOH A H1     1 
HETATM 6565 H H2     . HOH H 4 .   ? 10.580 49.106 41.146 0.01 42.77 ? 951  HOH A H2     1 
HETATM 6566 O O      . HOH H 4 .   ? 30.963 50.014 32.444 1.00 35.76 ? 952  HOH A O      1 
HETATM 6567 H H1     . HOH H 4 .   ? 31.630 50.541 32.434 0.01 42.91 ? 952  HOH A H1     1 
HETATM 6568 H H2     . HOH H 4 .   ? 30.292 50.531 32.377 0.01 42.91 ? 952  HOH A H2     1 
HETATM 6569 O O      . HOH H 4 .   ? 35.023 27.119 70.519 1.00 54.77 ? 953  HOH A O      1 
HETATM 6570 H H1     . HOH H 4 .   ? 35.578 27.762 70.552 0.01 65.73 ? 953  HOH A H1     1 
HETATM 6571 H H2     . HOH H 4 .   ? 34.391 27.366 71.029 0.01 65.73 ? 953  HOH A H2     1 
HETATM 6572 O O      . HOH H 4 .   ? 27.215 59.476 43.611 1.00 18.25 ? 954  HOH A O      1 
HETATM 6573 H H1     . HOH H 4 .   ? 27.092 58.927 42.850 0.01 21.90 ? 954  HOH A H1     1 
HETATM 6574 H H2     . HOH H 4 .   ? 27.692 60.287 43.440 0.01 21.90 ? 954  HOH A H2     1 
HETATM 6575 O O      . HOH H 4 .   ? 37.570 47.571 60.187 1.00 20.70 ? 955  HOH A O      1 
HETATM 6576 H H1     . HOH H 4 .   ? 38.170 47.933 59.707 0.01 24.84 ? 955  HOH A H1     1 
HETATM 6577 H H2     . HOH H 4 .   ? 36.905 48.095 60.111 0.01 24.84 ? 955  HOH A H2     1 
HETATM 6578 O O      . HOH H 4 .   ? 7.893  49.319 31.643 1.00 42.88 ? 956  HOH A O      1 
HETATM 6579 H H1     . HOH H 4 .   ? 8.605  49.709 31.900 0.01 51.46 ? 956  HOH A H1     1 
HETATM 6580 H H2     . HOH H 4 .   ? 7.264  49.738 32.033 0.01 51.46 ? 956  HOH A H2     1 
HETATM 6581 O O      . HOH H 4 .   ? 21.672 36.164 26.037 1.00 20.64 ? 957  HOH A O      1 
HETATM 6582 H H1     . HOH H 4 .   ? 22.096 35.439 25.910 0.01 24.77 ? 957  HOH A H1     1 
HETATM 6583 H H2     . HOH H 4 .   ? 20.896 36.003 25.730 0.01 24.77 ? 957  HOH A H2     1 
HETATM 6584 O O      . HOH H 4 .   ? 26.843 63.634 43.961 1.00 34.54 ? 958  HOH A O      1 
HETATM 6585 H H1     . HOH H 4 .   ? 27.517 64.152 43.935 0.01 41.45 ? 958  HOH A H1     1 
HETATM 6586 H H2     . HOH H 4 .   ? 26.178 64.163 43.935 0.01 41.45 ? 958  HOH A H2     1 
HETATM 6587 O O      . HOH H 4 .   ? 34.538 44.687 62.616 1.00 42.93 ? 959  HOH A O      1 
HETATM 6588 H H1     . HOH H 4 .   ? 35.317 45.019 62.689 0.01 51.51 ? 959  HOH A H1     1 
HETATM 6589 H H2     . HOH H 4 .   ? 34.109 45.031 63.264 0.01 51.51 ? 959  HOH A H2     1 
HETATM 6590 O O      . HOH H 4 .   ? 47.330 44.322 52.063 1.00 35.69 ? 960  HOH A O      1 
HETATM 6591 H H1     . HOH H 4 .   ? 47.871 44.949 51.877 0.01 42.83 ? 960  HOH A H1     1 
HETATM 6592 H H2     . HOH H 4 .   ? 46.628 44.517 51.627 0.01 42.83 ? 960  HOH A H2     1 
HETATM 6593 O O      . HOH H 4 .   ? 6.275  50.075 30.254 1.00 51.28 ? 961  HOH A O      1 
HETATM 6594 H H1     . HOH H 4 .   ? 6.624  50.066 29.479 0.01 61.54 ? 961  HOH A H1     1 
HETATM 6595 H H2     . HOH H 4 .   ? 5.684  50.684 30.204 0.01 61.54 ? 961  HOH A H2     1 
HETATM 6596 O O      . HOH H 4 .   ? 44.098 19.834 44.470 1.00 22.93 ? 962  HOH A O      1 
HETATM 6597 H H1     . HOH H 4 .   ? 44.213 20.463 43.910 0.01 27.51 ? 962  HOH A H1     1 
HETATM 6598 H H2     . HOH H 4 .   ? 43.342 20.009 44.818 0.02 27.51 ? 962  HOH A H2     1 
HETATM 6599 O O      . HOH H 4 .   ? 19.105 24.253 36.698 1.00 27.76 ? 963  HOH A O      1 
HETATM 6600 H H1     . HOH H 4 .   ? 19.370 24.440 37.484 0.01 33.31 ? 963  HOH A H1     1 
HETATM 6601 H H2     . HOH H 4 .   ? 18.702 24.957 36.446 0.02 33.31 ? 963  HOH A H2     1 
HETATM 6602 O O      . HOH H 4 .   ? 6.422  41.016 16.648 1.00 44.60 ? 964  HOH A O      1 
HETATM 6603 H H1     . HOH H 4 .   ? 5.889  40.551 16.177 0.01 53.53 ? 964  HOH A H1     1 
HETATM 6604 H H2     . HOH H 4 .   ? 7.027  40.463 16.876 0.01 53.53 ? 964  HOH A H2     1 
HETATM 6605 O O      . HOH H 4 .   ? 17.185 62.016 25.772 1.00 35.25 ? 965  HOH A O      1 
HETATM 6606 H H1     . HOH H 4 .   ? 17.144 62.810 25.472 0.01 42.30 ? 965  HOH A H1     1 
HETATM 6607 H H2     . HOH H 4 .   ? 16.371 61.784 25.850 0.01 42.30 ? 965  HOH A H2     1 
HETATM 6608 O O      . HOH H 4 .   ? 23.179 58.481 48.660 1.00 28.06 ? 966  HOH A O      1 
HETATM 6609 H H1     . HOH H 4 .   ? 23.845 59.009 48.630 0.01 33.67 ? 966  HOH A H1     1 
HETATM 6610 H H2     . HOH H 4 .   ? 22.505 58.999 48.646 0.01 33.67 ? 966  HOH A H2     1 
HETATM 6611 O O      . HOH H 4 .   ? 11.250 27.147 29.181 1.00 43.85 ? 967  HOH A O      1 
HETATM 6612 H H1     . HOH H 4 .   ? 11.918 27.673 29.179 0.01 52.62 ? 967  HOH A H1     1 
HETATM 6613 H H2     . HOH H 4 .   ? 10.579 27.667 29.178 0.01 52.62 ? 967  HOH A H2     1 
HETATM 6614 O O      . HOH H 4 .   ? 29.645 20.390 37.757 1.00 22.45 ? 968  HOH A O      1 
HETATM 6615 H H1     . HOH H 4 .   ? 29.053 19.843 37.291 0.03 26.94 ? 968  HOH A H1     1 
HETATM 6616 H H2     . HOH H 4 .   ? 30.423 19.860 38.031 0.01 26.94 ? 968  HOH A H2     1 
HETATM 6617 O O      . HOH H 4 .   ? 23.457 49.725 13.126 1.00 43.95 ? 969  HOH A O      1 
HETATM 6618 H H1     . HOH H 4 .   ? 23.051 50.385 13.481 0.01 52.75 ? 969  HOH A H1     1 
HETATM 6619 H H2     . HOH H 4 .   ? 24.244 49.792 13.440 0.01 52.75 ? 969  HOH A H2     1 
HETATM 6620 O O      . HOH H 4 .   ? 7.976  51.640 30.587 1.00 56.76 ? 970  HOH A O      1 
HETATM 6621 H H1     . HOH H 4 .   ? 8.683  51.607 30.124 0.01 68.11 ? 970  HOH A H1     1 
HETATM 6622 H H2     . HOH H 4 .   ? 7.900  50.862 30.900 0.01 68.11 ? 970  HOH A H2     1 
HETATM 6623 O O      . HOH H 4 .   ? 30.515 60.358 50.441 1.00 31.82 ? 971  HOH A O      1 
HETATM 6624 H H1     . HOH H 4 .   ? 31.158 60.913 50.438 0.01 38.18 ? 971  HOH A H1     1 
HETATM 6625 H H2     . HOH H 4 .   ? 29.839 60.824 50.226 0.01 38.18 ? 971  HOH A H2     1 
HETATM 6626 O O      . HOH H 4 .   ? 24.765 59.165 50.636 1.00 42.73 ? 972  HOH A O      1 
HETATM 6627 H H1     . HOH H 4 .   ? 25.416 59.672 50.836 0.01 51.27 ? 972  HOH A H1     1 
HETATM 6628 H H2     . HOH H 4 .   ? 24.098 59.691 50.602 0.01 51.27 ? 972  HOH A H2     1 
HETATM 6629 O O      . HOH H 4 .   ? 26.186 16.646 37.391 1.00 30.86 ? 973  HOH A O      1 
HETATM 6630 H H1     . HOH H 4 .   ? 26.822 17.157 37.153 0.01 37.03 ? 973  HOH A H1     1 
HETATM 6631 H H2     . HOH H 4 .   ? 25.512 17.164 37.427 0.01 37.03 ? 973  HOH A H2     1 
HETATM 6632 O O      . HOH H 4 .   ? 18.219 28.991 30.262 1.00 30.07 ? 974  HOH A O      1 
HETATM 6633 H H1     . HOH H 4 .   ? 18.893 29.509 30.260 0.01 36.08 ? 974  HOH A H1     1 
HETATM 6634 H H2     . HOH H 4 .   ? 17.555 29.519 30.226 0.01 36.08 ? 974  HOH A H2     1 
HETATM 6635 O O      . HOH H 4 .   ? 29.331 24.736 36.200 1.00 40.60 ? 975  HOH A O      1 
HETATM 6636 H H1     . HOH H 4 .   ? 30.032 25.198 36.327 0.01 48.72 ? 975  HOH A H1     1 
HETATM 6637 H H2     . HOH H 4 .   ? 28.723 25.165 36.610 0.01 48.72 ? 975  HOH A H2     1 
HETATM 6638 O O      . HOH H 4 .   ? 24.643 40.297 35.221 1.00 44.80 ? 976  HOH A O      1 
HETATM 6639 H H1     . HOH H 4 .   ? 24.279 40.871 35.733 0.01 53.77 ? 976  HOH A H1     1 
HETATM 6640 H H2     . HOH H 4 .   ? 24.948 39.712 35.756 0.01 53.77 ? 976  HOH A H2     1 
HETATM 6641 O O      . HOH H 4 .   ? 12.543 21.607 33.643 1.00 39.93 ? 977  HOH A O      1 
HETATM 6642 H H1     . HOH H 4 .   ? 13.026 22.250 33.918 0.01 47.91 ? 977  HOH A H1     1 
HETATM 6643 H H2     . HOH H 4 .   ? 11.756 21.930 33.644 0.01 47.91 ? 977  HOH A H2     1 
HETATM 6644 O O      . HOH H 4 .   ? 17.984 65.840 27.484 1.00 55.93 ? 978  HOH A O      1 
HETATM 6645 H H1     . HOH H 4 .   ? 18.628 66.386 27.383 0.01 67.12 ? 978  HOH A H1     1 
HETATM 6646 H H2     . HOH H 4 .   ? 17.291 66.323 27.387 0.01 67.12 ? 978  HOH A H2     1 
HETATM 6647 O O      . HOH H 4 .   ? 28.234 34.323 37.691 1.00 31.50 ? 979  HOH A O      1 
HETATM 6648 H H1     . HOH H 4 .   ? 28.904 34.847 37.685 0.01 37.80 ? 979  HOH A H1     1 
HETATM 6649 H H2     . HOH H 4 .   ? 27.565 34.848 37.686 0.01 37.80 ? 979  HOH A H2     1 
HETATM 6650 O O      . HOH H 4 .   ? 13.660 53.655 43.835 1.00 50.41 ? 980  HOH A O      1 
HETATM 6651 H H1     . HOH H 4 .   ? 14.346 54.132 43.678 0.01 60.49 ? 980  HOH A H1     1 
HETATM 6652 H H2     . HOH H 4 .   ? 13.007 54.170 43.659 0.01 60.49 ? 980  HOH A H2     1 
HETATM 6653 O O      . HOH H 4 .   ? 12.569 20.790 36.057 1.00 29.08 ? 981  HOH A O      1 
HETATM 6654 H H1     . HOH H 4 .   ? 12.976 21.517 35.887 0.01 34.90 ? 981  HOH A H1     1 
HETATM 6655 H H2     . HOH H 4 .   ? 11.757 20.962 35.876 0.01 34.90 ? 981  HOH A H2     1 
HETATM 6656 O O      . HOH H 4 .   ? 12.491 47.183 14.887 1.00 37.75 ? 982  HOH A O      1 
HETATM 6657 H H1     . HOH H 4 .   ? 12.609 48.009 15.051 0.01 45.30 ? 982  HOH A H1     1 
HETATM 6658 H H2     . HOH H 4 .   ? 11.693 47.037 15.141 0.01 45.30 ? 982  HOH A H2     1 
HETATM 6659 O O      . HOH H 4 .   ? 39.725 27.832 35.019 1.00 38.79 ? 983  HOH A O      1 
HETATM 6660 H H1     . HOH H 4 .   ? 40.391 28.358 35.018 0.01 46.55 ? 983  HOH A H1     1 
HETATM 6661 H H2     . HOH H 4 .   ? 39.052 28.352 35.018 0.01 46.55 ? 983  HOH A H2     1 
HETATM 6662 O O      . HOH H 4 .   ? 37.221 45.876 62.031 1.00 39.93 ? 984  HOH A O      1 
HETATM 6663 H H1     . HOH H 4 .   ? 37.960 46.294 62.005 0.01 47.92 ? 984  HOH A H1     1 
HETATM 6664 H H2     . HOH H 4 .   ? 36.640 46.478 61.877 0.01 47.92 ? 984  HOH A H2     1 
HETATM 6665 O O      . HOH H 4 .   ? 20.746 59.728 26.796 1.00 38.51 ? 985  HOH A O      1 
HETATM 6666 H H1     . HOH H 4 .   ? 20.659 59.458 27.597 0.01 46.21 ? 985  HOH A H1     1 
HETATM 6667 H H2     . HOH H 4 .   ? 19.947 59.857 26.541 0.01 46.21 ? 985  HOH A H2     1 
HETATM 6668 O O      . HOH H 4 .   ? 27.900 17.165 38.921 1.00 38.11 ? 986  HOH A O      1 
HETATM 6669 H H1     . HOH H 4 .   ? 28.636 17.588 38.920 0.01 45.74 ? 986  HOH A H1     1 
HETATM 6670 H H2     . HOH H 4 .   ? 27.324 17.755 39.129 0.01 45.74 ? 986  HOH A H2     1 
HETATM 6671 O O      . HOH H 4 .   ? 20.023 19.197 50.537 1.00 45.89 ? 987  HOH A O      1 
HETATM 6672 H H1     . HOH H 4 .   ? 20.779 19.518 50.318 0.01 55.07 ? 987  HOH A H1     1 
HETATM 6673 H H2     . HOH H 4 .   ? 19.498 19.863 50.495 0.01 55.07 ? 987  HOH A H2     1 
HETATM 6674 O O      . HOH H 4 .   ? 31.192 46.940 29.011 1.00 48.51 ? 988  HOH A O      1 
HETATM 6675 H H1     . HOH H 4 .   ? 31.971 46.600 29.025 0.01 58.22 ? 988  HOH A H1     1 
HETATM 6676 H H2     . HOH H 4 .   ? 31.332 47.773 28.933 0.01 58.22 ? 988  HOH A H2     1 
HETATM 6677 O O      . HOH H 4 .   ? 19.697 42.535 34.872 1.00 42.44 ? 989  HOH A O      1 
HETATM 6678 H H1     . HOH H 4 .   ? 20.243 43.075 34.506 0.01 50.93 ? 989  HOH A H1     1 
HETATM 6679 H H2     . HOH H 4 .   ? 18.972 42.975 34.916 0.01 50.93 ? 989  HOH A H2     1 
HETATM 6680 O O      . HOH H 4 .   ? 17.214 27.777 26.175 1.00 48.50 ? 990  HOH A O      1 
HETATM 6681 H H1     . HOH H 4 .   ? 17.877 28.306 26.126 0.01 58.20 ? 990  HOH A H1     1 
HETATM 6682 H H2     . HOH H 4 .   ? 16.537 28.291 26.128 0.01 58.20 ? 990  HOH A H2     1 
HETATM 6683 O O      . HOH H 4 .   ? 19.661 18.303 40.576 1.00 27.86 ? 991  HOH A O      1 
HETATM 6684 H H1     . HOH H 4 .   ? 20.369 18.769 40.638 0.01 33.44 ? 991  HOH A H1     1 
HETATM 6685 H H2     . HOH H 4 .   ? 19.079 18.758 40.996 0.01 33.44 ? 991  HOH A H2     1 
HETATM 6686 O O      . HOH H 4 .   ? 24.988 48.442 56.520 1.00 27.61 ? 992  HOH A O      1 
HETATM 6687 H H1     . HOH H 4 .   ? 25.491 49.027 56.874 0.03 33.13 ? 992  HOH A H1     1 
HETATM 6688 H H2     . HOH H 4 .   ? 24.210 48.781 56.575 0.01 33.13 ? 992  HOH A H2     1 
HETATM 6689 O O      . HOH H 4 .   ? 20.096 41.625 36.862 1.00 36.92 ? 993  HOH A O      1 
HETATM 6690 H H1     . HOH H 4 .   ? 20.157 42.455 36.695 0.01 44.30 ? 993  HOH A H1     1 
HETATM 6691 H H2     . HOH H 4 .   ? 19.262 41.497 36.965 0.01 44.30 ? 993  HOH A H2     1 
HETATM 6692 O O      . HOH H 4 .   ? 46.262 42.947 42.065 1.00 42.00 ? 994  HOH A O      1 
HETATM 6693 H H1     . HOH H 4 .   ? 46.854 43.546 41.956 0.01 50.41 ? 994  HOH A H1     1 
HETATM 6694 H H2     . HOH H 4 .   ? 45.528 43.374 42.023 0.01 50.41 ? 994  HOH A H2     1 
HETATM 6695 O O      . HOH H 4 .   ? 22.095 58.769 58.240 1.00 36.69 ? 995  HOH A O      1 
HETATM 6696 H H1     . HOH H 4 .   ? 22.761 59.299 58.237 0.01 44.03 ? 995  HOH A H1     1 
HETATM 6697 H H2     . HOH H 4 .   ? 21.423 59.291 58.237 0.01 44.03 ? 995  HOH A H2     1 
HETATM 6698 O O      . HOH H 4 .   ? 8.809  22.104 35.556 1.00 50.22 ? 996  HOH A O      1 
HETATM 6699 H H1     . HOH H 4 .   ? 9.476  22.631 35.554 0.01 60.27 ? 996  HOH A H1     1 
HETATM 6700 H H2     . HOH H 4 .   ? 8.137  22.624 35.554 0.01 60.27 ? 996  HOH A H2     1 
HETATM 6701 O O      . HOH H 4 .   ? 27.135 61.093 47.441 1.00 47.80 ? 997  HOH A O      1 
HETATM 6702 H H1     . HOH H 4 .   ? 27.948 61.341 47.418 0.01 57.36 ? 997  HOH A H1     1 
HETATM 6703 H H2     . HOH H 4 .   ? 26.723 61.771 47.745 0.01 57.36 ? 997  HOH A H2     1 
HETATM 6704 O O      . HOH H 4 .   ? 38.986 40.858 44.602 1.00 50.55 ? 998  HOH A O      1 
HETATM 6705 H H1     . HOH H 4 .   ? 39.619 41.366 44.856 0.01 60.66 ? 998  HOH A H1     1 
HETATM 6706 H H2     . HOH H 4 .   ? 38.310 41.372 44.574 0.01 60.66 ? 998  HOH A H2     1 
HETATM 6707 O O      . HOH H 4 .   ? 24.671 60.436 46.967 1.00 47.09 ? 999  HOH A O      1 
HETATM 6708 H H1     . HOH H 4 .   ? 25.276 60.736 46.450 0.01 56.51 ? 999  HOH A H1     1 
HETATM 6709 H H2     . HOH H 4 .   ? 24.004 60.940 46.813 0.01 56.51 ? 999  HOH A H2     1 
HETATM 6710 O O      . HOH H 4 .   ? 12.075 24.643 30.371 1.00 47.28 ? 1000 HOH A O      1 
HETATM 6711 H H1     . HOH H 4 .   ? 12.020 25.492 30.358 0.01 56.74 ? 1000 HOH A H1     1 
HETATM 6712 H H2     . HOH H 4 .   ? 11.275 24.386 30.239 0.01 56.74 ? 1000 HOH A H2     1 
HETATM 6713 O O      . HOH H 4 .   ? 20.570 32.790 29.753 1.00 46.00 ? 1001 HOH A O      1 
HETATM 6714 H H1     . HOH H 4 .   ? 21.130 33.327 29.408 0.01 55.21 ? 1001 HOH A H1     1 
HETATM 6715 H H2     . HOH H 4 .   ? 19.835 33.216 29.731 0.01 55.21 ? 1001 HOH A H2     1 
HETATM 6716 O O      . HOH H 4 .   ? 9.864  31.134 22.027 1.00 42.20 ? 1002 HOH A O      1 
HETATM 6717 H H1     . HOH H 4 .   ? 10.545 31.643 22.044 0.01 50.65 ? 1002 HOH A H1     1 
HETATM 6718 H H2     . HOH H 4 .   ? 9.237  31.623 22.328 0.01 50.65 ? 1002 HOH A H2     1 
HETATM 6719 O O      . HOH H 4 .   ? 33.200 49.118 59.112 1.00 37.88 ? 1003 HOH A O      1 
HETATM 6720 H H1     . HOH H 4 .   ? 33.840 49.675 59.126 0.01 45.46 ? 1003 HOH A H1     1 
HETATM 6721 H H2     . HOH H 4 .   ? 32.504 49.606 59.098 0.01 45.46 ? 1003 HOH A H2     1 
HETATM 6722 O O      . HOH H 4 .   ? 22.322 18.287 37.254 1.00 43.50 ? 1004 HOH A O      1 
HETATM 6723 H H1     . HOH H 4 .   ? 23.120 18.581 37.236 0.01 52.20 ? 1004 HOH A H1     1 
HETATM 6724 H H2     . HOH H 4 .   ? 21.872 18.893 36.865 0.01 52.20 ? 1004 HOH A H2     1 
HETATM 6725 O O      . HOH H 4 .   ? 15.156 17.644 42.519 1.00 33.45 ? 1005 HOH A O      1 
HETATM 6726 H H1     . HOH H 4 .   ? 15.806 18.183 42.422 0.01 40.13 ? 1005 HOH A H1     1 
HETATM 6727 H H2     . HOH H 4 .   ? 14.469 18.145 42.496 0.01 40.13 ? 1005 HOH A H2     1 
HETATM 6728 O O      . HOH H 4 .   ? 24.464 59.517 52.971 1.00 49.33 ? 1006 HOH A O      1 
HETATM 6729 H H1     . HOH H 4 .   ? 25.110 59.867 53.395 0.01 59.20 ? 1006 HOH A H1     1 
HETATM 6730 H H2     . HOH H 4 .   ? 23.944 59.239 53.583 0.01 59.20 ? 1006 HOH A H2     1 
HETATM 6731 O O      . HOH H 4 .   ? 11.083 35.496 31.506 1.00 24.94 ? 1007 HOH A O      1 
HETATM 6732 H H1     . HOH H 4 .   ? 11.551 36.070 31.924 0.01 29.93 ? 1007 HOH A H1     1 
HETATM 6733 H H2     . HOH H 4 .   ? 10.351 35.900 31.355 0.01 29.93 ? 1007 HOH A H2     1 
HETATM 6734 O O      . HOH H 4 .   ? 41.739 40.897 61.867 1.00 33.48 ? 1008 HOH A O      1 
HETATM 6735 H H1     . HOH H 4 .   ? 42.483 41.130 61.528 0.01 40.18 ? 1008 HOH A H1     1 
HETATM 6736 H H2     . HOH H 4 .   ? 41.198 40.924 61.212 0.01 40.18 ? 1008 HOH A H2     1 
HETATM 6737 O O      . HOH H 4 .   ? 7.502  39.052 43.278 1.00 17.25 ? 1009 HOH A O      1 
HETATM 6738 H H1     . HOH H 4 .   ? 8.314  39.241 43.115 0.01 20.71 ? 1009 HOH A H1     1 
HETATM 6739 H H2     . HOH H 4 .   ? 7.150  39.802 43.468 0.01 20.71 ? 1009 HOH A H2     1 
HETATM 6740 O O      . HOH H 4 .   ? 22.245 20.656 50.611 1.00 35.38 ? 1010 HOH A O      1 
HETATM 6741 H H1     . HOH H 4 .   ? 23.059 20.902 50.615 0.01 42.46 ? 1010 HOH A H1     1 
HETATM 6742 H H2     . HOH H 4 .   ? 21.811 21.384 50.672 0.01 42.46 ? 1010 HOH A H2     1 
HETATM 6743 O O      . HOH H 4 .   ? 38.715 33.252 36.983 1.00 32.20 ? 1011 HOH A O      1 
HETATM 6744 H H1     . HOH H 4 .   ? 39.388 33.771 36.976 0.01 38.64 ? 1011 HOH A H1     1 
HETATM 6745 H H2     . HOH H 4 .   ? 38.048 33.778 36.976 0.01 38.64 ? 1011 HOH A H2     1 
HETATM 6746 O O      . HOH H 4 .   ? 20.313 48.541 57.358 1.00 49.59 ? 1012 HOH A O      1 
HETATM 6747 H H1     . HOH H 4 .   ? 21.002 49.040 57.350 0.01 59.51 ? 1012 HOH A H1     1 
HETATM 6748 H H2     . HOH H 4 .   ? 19.664 49.090 57.349 0.01 59.51 ? 1012 HOH A H2     1 
HETATM 6749 O O      . HOH H 4 .   ? 24.054 30.077 62.749 1.00 40.10 ? 1013 HOH A O      1 
HETATM 6750 H H1     . HOH H 4 .   ? 24.748 30.568 62.748 0.01 48.13 ? 1013 HOH A H1     1 
HETATM 6751 H H2     . HOH H 4 .   ? 23.416 30.623 62.621 0.01 48.13 ? 1013 HOH A H2     1 
HETATM 6752 O O      . HOH H 4 .   ? 46.478 46.755 51.113 1.00 41.31 ? 1014 HOH A O      1 
HETATM 6753 H H1     . HOH H 4 .   ? 46.711 46.722 50.297 0.01 49.58 ? 1014 HOH A H1     1 
HETATM 6754 H H2     . HOH H 4 .   ? 46.335 47.586 51.243 0.01 49.58 ? 1014 HOH A H2     1 
HETATM 6755 O O      . HOH H 4 .   ? 40.539 29.345 37.187 1.00 21.35 ? 1015 HOH A O      1 
HETATM 6756 H H1     . HOH H 4 .   ? 41.165 29.914 37.114 0.01 25.63 ? 1015 HOH A H1     1 
HETATM 6757 H H2     . HOH H 4 .   ? 39.835 29.794 37.025 0.04 25.63 ? 1015 HOH A H2     1 
HETATM 6758 O O      . HOH H 4 .   ? 9.401  46.029 36.536 1.00 47.11 ? 1016 HOH A O      1 
HETATM 6759 H H1     . HOH H 4 .   ? 9.979  46.390 36.029 0.01 56.54 ? 1016 HOH A H1     1 
HETATM 6760 H H2     . HOH H 4 .   ? 8.763  46.591 36.551 0.01 56.54 ? 1016 HOH A H2     1 
HETATM 6761 O O      . HOH H 4 .   ? 14.180 19.221 44.361 1.00 30.94 ? 1017 HOH A O      1 
HETATM 6762 H H1     . HOH H 4 .   ? 14.930 19.620 44.347 0.01 37.13 ? 1017 HOH A H1     1 
HETATM 6763 H H2     . HOH H 4 .   ? 13.625 19.819 44.123 0.01 37.13 ? 1017 HOH A H2     1 
HETATM 6764 O O      . HOH H 4 .   ? 23.907 13.063 49.257 1.00 29.98 ? 1018 HOH A O      1 
HETATM 6765 H H1     . HOH H 4 .   ? 24.570 13.595 49.258 0.01 35.98 ? 1018 HOH A H1     1 
HETATM 6766 H H2     . HOH H 4 .   ? 23.231 13.577 49.256 0.01 35.98 ? 1018 HOH A H2     1 
HETATM 6767 O O      . HOH H 4 .   ? 35.635 49.499 60.779 1.00 30.24 ? 1019 HOH A O      1 
HETATM 6768 H H1     . HOH H 4 .   ? 36.309 50.008 60.684 0.01 36.29 ? 1019 HOH A H1     1 
HETATM 6769 H H2     . HOH H 4 .   ? 34.981 50.037 60.856 0.01 36.29 ? 1019 HOH A H2     1 
HETATM 6770 O O      . HOH H 4 .   ? 43.290 50.874 46.801 1.00 46.57 ? 1020 HOH A O      1 
HETATM 6771 H H1     . HOH H 4 .   ? 44.016 51.316 46.823 0.01 55.89 ? 1020 HOH A H1     1 
HETATM 6772 H H2     . HOH H 4 .   ? 42.693 51.467 46.683 0.01 55.89 ? 1020 HOH A H2     1 
HETATM 6773 O O      . HOH H 4 .   ? 22.074 34.650 53.183 1.00 35.88 ? 1021 HOH A O      1 
HETATM 6774 H H1     . HOH H 4 .   ? 22.675 35.251 53.174 0.01 43.05 ? 1021 HOH A H1     1 
HETATM 6775 H H2     . HOH H 4 .   ? 21.346 35.090 53.196 0.01 43.05 ? 1021 HOH A H2     1 
HETATM 6776 O O      . HOH H 4 .   ? 33.284 13.011 39.825 1.00 30.07 ? 1022 HOH A O      1 
HETATM 6777 H H1     . HOH H 4 .   ? 33.805 13.200 40.470 0.01 36.08 ? 1022 HOH A H1     1 
HETATM 6778 H H2     . HOH H 4 .   ? 32.576 13.447 40.000 0.01 36.08 ? 1022 HOH A H2     1 
HETATM 6779 O O      . HOH H 4 .   ? 27.831 42.995 60.719 1.00 33.24 ? 1023 HOH A O      1 
HETATM 6780 H H1     . HOH H 4 .   ? 28.502 43.517 60.720 0.01 39.89 ? 1023 HOH A H1     1 
HETATM 6781 H H2     . HOH H 4 .   ? 27.164 43.521 60.720 0.01 39.89 ? 1023 HOH A H2     1 
HETATM 6782 O O      . HOH H 4 .   ? 37.602 46.830 35.648 1.00 55.65 ? 1024 HOH A O      1 
HETATM 6783 H H1     . HOH H 4 .   ? 38.299 47.182 35.314 0.01 66.78 ? 1024 HOH A H1     1 
HETATM 6784 H H2     . HOH H 4 .   ? 37.022 47.449 35.613 0.01 66.78 ? 1024 HOH A H2     1 
HETATM 6785 O O      . HOH H 4 .   ? 21.030 33.491 26.539 1.00 31.45 ? 1025 HOH A O      1 
HETATM 6786 H H1     . HOH H 4 .   ? 21.847 33.717 26.572 0.01 37.74 ? 1025 HOH A H1     1 
HETATM 6787 H H2     . HOH H 4 .   ? 20.611 34.184 26.798 0.01 37.74 ? 1025 HOH A H2     1 
HETATM 6788 O O      . HOH H 4 .   ? 39.673 37.628 42.835 1.00 36.45 ? 1026 HOH A O      1 
HETATM 6789 H H1     . HOH H 4 .   ? 40.344 38.149 42.833 0.01 43.74 ? 1026 HOH A H1     1 
HETATM 6790 H H2     . HOH H 4 .   ? 39.005 38.155 42.833 0.01 43.74 ? 1026 HOH A H2     1 
HETATM 6791 O O      . HOH H 4 .   ? 14.539 51.990 53.252 1.00 47.20 ? 1027 HOH A O      1 
HETATM 6792 H H1     . HOH H 4 .   ? 15.016 52.629 53.546 0.01 56.65 ? 1027 HOH A H1     1 
HETATM 6793 H H2     . HOH H 4 .   ? 13.757 52.322 53.214 0.01 56.65 ? 1027 HOH A H2     1 
HETATM 6794 O O      . HOH H 4 .   ? 32.295 23.166 34.228 1.00 50.63 ? 1028 HOH A O      1 
HETATM 6795 H H1     . HOH H 4 .   ? 32.890 23.711 33.963 0.01 60.76 ? 1028 HOH A H1     1 
HETATM 6796 H H2     . HOH H 4 .   ? 31.575 23.616 34.197 0.01 60.76 ? 1028 HOH A H2     1 
HETATM 6797 O O      . HOH H 4 .   ? 45.506 31.258 52.475 1.00 47.06 ? 1029 HOH A O      1 
HETATM 6798 H H1     . HOH H 4 .   ? 46.173 31.784 52.447 0.01 56.47 ? 1029 HOH A H1     1 
HETATM 6799 H H2     . HOH H 4 .   ? 44.836 31.779 52.522 0.01 56.47 ? 1029 HOH A H2     1 
HETATM 6800 O O      . HOH H 4 .   ? 21.479 30.183 32.743 1.00 44.83 ? 1030 HOH A O      1 
HETATM 6801 H H1     . HOH H 4 .   ? 22.157 30.695 32.724 0.01 53.79 ? 1030 HOH A H1     1 
HETATM 6802 H H2     . HOH H 4 .   ? 20.820 30.720 32.745 0.01 53.79 ? 1030 HOH A H2     1 
HETATM 6803 O O      . HOH H 4 .   ? 17.914 59.565 15.146 1.00 35.75 ? 1031 HOH A O      1 
HETATM 6804 H H1     . HOH H 4 .   ? 17.754 60.256 15.606 0.01 42.90 ? 1031 HOH A H1     1 
HETATM 6805 H H2     . HOH H 4 .   ? 17.168 59.415 14.774 0.01 42.90 ? 1031 HOH A H2     1 
HETATM 6806 O O      . HOH H 4 .   ? 29.587 18.181 37.029 1.00 46.57 ? 1032 HOH A O      1 
HETATM 6807 H H1     . HOH H 4 .   ? 30.204 18.376 36.478 0.01 55.88 ? 1032 HOH A H1     1 
HETATM 6808 H H2     . HOH H 4 .   ? 28.869 18.350 36.604 0.01 55.88 ? 1032 HOH A H2     1 
HETATM 6809 O O      . HOH H 4 .   ? 24.383 24.459 58.376 1.00 43.21 ? 1033 HOH A O      1 
HETATM 6810 H H1     . HOH H 4 .   ? 25.021 25.011 58.479 0.01 51.86 ? 1033 HOH A H1     1 
HETATM 6811 H H2     . HOH H 4 .   ? 23.689 24.948 58.359 0.01 51.86 ? 1033 HOH A H2     1 
HETATM 6812 O O      . HOH H 4 .   ? 45.559 17.238 44.382 1.00 44.64 ? 1034 HOH A O      1 
HETATM 6813 H H1     . HOH H 4 .   ? 46.339 17.572 44.409 0.01 53.57 ? 1034 HOH A H1     1 
HETATM 6814 H H2     . HOH H 4 .   ? 45.076 17.865 44.072 0.01 53.57 ? 1034 HOH A H2     1 
HETATM 6815 O O      . HOH H 4 .   ? 26.376 11.824 46.584 1.00 49.75 ? 1035 HOH A O      1 
HETATM 6816 H H1     . HOH H 4 .   ? 27.038 12.356 46.632 0.01 59.70 ? 1035 HOH A H1     1 
HETATM 6817 H H2     . HOH H 4 .   ? 25.700 12.336 46.631 0.01 59.70 ? 1035 HOH A H2     1 
HETATM 6818 O O      . HOH H 4 .   ? 33.425 28.705 69.538 1.00 37.66 ? 1036 HOH A O      1 
HETATM 6819 H H1     . HOH H 4 .   ? 34.103 29.218 69.550 0.01 45.19 ? 1036 HOH A H1     1 
HETATM 6820 H H2     . HOH H 4 .   ? 33.068 28.821 70.300 0.01 45.19 ? 1036 HOH A H2     1 
HETATM 6821 O O      . HOH H 4 .   ? 25.812 39.469 59.471 1.00 34.73 ? 1037 HOH A O      1 
HETATM 6822 H H1     . HOH H 4 .   ? 26.605 39.726 59.641 0.01 41.68 ? 1037 HOH A H1     1 
HETATM 6823 H H2     . HOH H 4 .   ? 25.323 40.045 59.861 0.01 41.68 ? 1037 HOH A H2     1 
HETATM 6824 O O      . HOH H 4 .   ? 7.323  19.676 45.999 1.00 34.24 ? 1038 HOH A O      1 
HETATM 6825 H H1     . HOH H 4 .   ? 7.992  20.194 45.918 0.01 41.09 ? 1038 HOH A H1     1 
HETATM 6826 H H2     . HOH H 4 .   ? 6.680  20.118 45.661 0.01 41.09 ? 1038 HOH A H2     1 
HETATM 6827 O O      . HOH H 4 .   ? 5.828  22.547 39.444 1.00 44.39 ? 1039 HOH A O      1 
HETATM 6828 H H1     . HOH H 4 .   ? 6.216  22.934 38.794 0.01 53.27 ? 1039 HOH A H1     1 
HETATM 6829 H H2     . HOH H 4 .   ? 5.047  22.882 39.447 0.01 53.27 ? 1039 HOH A H2     1 
HETATM 6830 O O      . HOH H 4 .   ? 24.365 36.848 55.792 1.00 24.20 ? 1040 HOH A O      1 
HETATM 6831 H H1     . HOH H 4 .   ? 24.962 37.263 56.233 0.01 29.05 ? 1040 HOH A H1     1 
HETATM 6832 H H2     . HOH H 4 .   ? 23.693 37.368 55.817 0.01 29.05 ? 1040 HOH A H2     1 
HETATM 6833 O O      . HOH H 4 .   ? 8.258  38.061 28.696 1.00 43.23 ? 1041 HOH A O      1 
HETATM 6834 H H1     . HOH H 4 .   ? 8.745  38.755 28.639 0.01 51.88 ? 1041 HOH A H1     1 
HETATM 6835 H H2     . HOH H 4 .   ? 7.465  38.364 28.680 0.01 51.88 ? 1041 HOH A H2     1 
HETATM 6836 O O      . HOH H 4 .   ? 10.751 51.393 41.819 1.00 52.76 ? 1042 HOH A O      1 
HETATM 6837 H H1     . HOH H 4 .   ? 11.416 51.923 41.803 0.01 63.31 ? 1042 HOH A H1     1 
HETATM 6838 H H2     . HOH H 4 .   ? 10.077 51.909 41.803 0.01 63.31 ? 1042 HOH A H2     1 
HETATM 6839 O O      . HOH H 4 .   ? 16.013 20.283 46.072 1.00 34.96 ? 1043 HOH A O      1 
HETATM 6840 H H1     . HOH H 4 .   ? 16.685 20.804 46.071 0.01 41.95 ? 1043 HOH A H1     1 
HETATM 6841 H H2     . HOH H 4 .   ? 15.346 20.811 46.071 0.01 41.95 ? 1043 HOH A H2     1 
HETATM 6842 O O      . HOH H 4 .   ? 41.011 39.996 43.601 1.00 49.24 ? 1044 HOH A O      1 
HETATM 6843 H H1     . HOH H 4 .   ? 41.573 40.579 43.341 0.01 59.09 ? 1044 HOH A H1     1 
HETATM 6844 H H2     . HOH H 4 .   ? 40.282 40.238 43.236 0.01 59.09 ? 1044 HOH A H2     1 
HETATM 6845 O O      . HOH H 4 .   ? 46.282 23.368 46.286 1.00 29.77 ? 1045 HOH A O      1 
HETATM 6846 H H1     . HOH H 4 .   ? 46.898 23.958 46.283 0.01 35.73 ? 1045 HOH A H1     1 
HETATM 6847 H H2     . HOH H 4 .   ? 45.552 23.809 46.292 0.01 35.73 ? 1045 HOH A H2     1 
HETATM 6848 O O      . HOH H 4 .   ? 14.484 59.366 36.560 1.00 41.90 ? 1046 HOH A O      1 
HETATM 6849 H H1     . HOH H 4 .   ? 15.137 59.906 36.629 0.01 50.28 ? 1046 HOH A H1     1 
HETATM 6850 H H2     . HOH H 4 .   ? 13.799 59.870 36.575 0.01 50.28 ? 1046 HOH A H2     1 
HETATM 6851 O O      . HOH H 4 .   ? 15.251 45.066 54.857 1.00 49.81 ? 1047 HOH A O      1 
HETATM 6852 H H1     . HOH H 4 .   ? 15.722 45.721 54.589 0.01 59.77 ? 1047 HOH A H1     1 
HETATM 6853 H H2     . HOH H 4 .   ? 14.459 45.375 54.868 0.01 59.77 ? 1047 HOH A H2     1 
HETATM 6854 O O      . HOH H 4 .   ? 18.670 21.936 47.771 1.00 22.50 ? 1048 HOH A O      1 
HETATM 6855 H H1     . HOH H 4 .   ? 19.344 22.451 47.751 0.01 27.00 ? 1048 HOH A H1     1 
HETATM 6856 H H2     . HOH H 4 .   ? 18.005 22.465 47.772 0.01 27.00 ? 1048 HOH A H2     1 
HETATM 6857 O O      . HOH H 4 .   ? 22.889 23.559 49.323 1.00 30.38 ? 1049 HOH A O      1 
HETATM 6858 H H1     . HOH H 4 .   ? 23.298 24.103 49.832 0.01 36.46 ? 1049 HOH A H1     1 
HETATM 6859 H H2     . HOH H 4 .   ? 22.257 24.022 48.995 0.01 36.46 ? 1049 HOH A H2     1 
HETATM 6860 O O      . HOH H 4 .   ? 32.552 17.055 36.867 1.00 43.50 ? 1050 HOH A O      1 
HETATM 6861 H H1     . HOH H 4 .   ? 33.319 17.289 36.587 0.01 52.20 ? 1050 HOH A H1     1 
HETATM 6862 H H2     . HOH H 4 .   ? 32.075 17.752 36.762 0.01 52.20 ? 1050 HOH A H2     1 
HETATM 6863 O O      . HOH H 4 .   ? 34.862 30.888 70.657 1.00 41.16 ? 1051 HOH A O      1 
HETATM 6864 H H1     . HOH H 4 .   ? 35.399 31.179 71.249 0.01 49.39 ? 1051 HOH A H1     1 
HETATM 6865 H H2     . HOH H 4 .   ? 34.128 31.276 70.841 0.01 49.39 ? 1051 HOH A H2     1 
HETATM 6866 O O      . HOH H 4 .   ? 37.037 36.762 44.768 1.00 46.23 ? 1052 HOH A O      1 
HETATM 6867 H H1     . HOH H 4 .   ? 37.304 36.911 43.976 0.01 55.47 ? 1052 HOH A H1     1 
HETATM 6868 H H2     . HOH H 4 .   ? 37.091 37.521 45.150 0.01 55.47 ? 1052 HOH A H2     1 
HETATM 6869 O O      . HOH H 4 .   ? 23.439 27.638 61.571 1.00 42.45 ? 1053 HOH A O      1 
HETATM 6870 H H1     . HOH H 4 .   ? 24.104 28.169 61.579 0.01 50.94 ? 1053 HOH A H1     1 
HETATM 6871 H H2     . HOH H 4 .   ? 22.766 28.156 61.579 0.01 50.94 ? 1053 HOH A H2     1 
HETATM 6872 O O      . HOH H 4 .   ? 30.849 49.208 29.986 1.00 45.42 ? 1054 HOH A O      1 
HETATM 6873 H H1     . HOH H 4 .   ? 31.520 49.731 29.989 0.01 54.51 ? 1054 HOH A H1     1 
HETATM 6874 H H2     . HOH H 4 .   ? 30.182 49.733 29.989 0.01 54.51 ? 1054 HOH A H2     1 
HETATM 6875 O O      . HOH H 4 .   ? 34.901 20.041 35.213 1.00 33.98 ? 1055 HOH A O      1 
HETATM 6876 H H1     . HOH H 4 .   ? 35.569 20.567 35.212 0.01 40.77 ? 1055 HOH A H1     1 
HETATM 6877 H H2     . HOH H 4 .   ? 34.230 20.563 35.212 0.01 40.77 ? 1055 HOH A H2     1 
HETATM 6878 O O      . HOH H 4 .   ? 21.977 60.164 53.955 1.00 41.85 ? 1056 HOH A O      1 
HETATM 6879 H H1     . HOH H 4 .   ? 21.568 59.418 53.928 0.01 50.23 ? 1056 HOH A H1     1 
HETATM 6880 H H2     . HOH H 4 .   ? 22.361 60.212 53.198 0.01 50.23 ? 1056 HOH A H2     1 
HETATM 6881 O O      . HOH H 4 .   ? 30.646 55.696 55.072 1.00 36.18 ? 1057 HOH A O      1 
HETATM 6882 H H1     . HOH H 4 .   ? 31.373 56.137 55.076 0.01 43.41 ? 1057 HOH A H1     1 
HETATM 6883 H H2     . HOH H 4 .   ? 30.049 56.288 55.198 0.01 43.41 ? 1057 HOH A H2     1 
HETATM 6884 O O      . HOH H 4 .   ? 29.674 62.588 46.714 1.00 28.91 ? 1058 HOH A O      1 
HETATM 6885 H H1     . HOH H 4 .   ? 30.342 63.113 46.717 0.01 34.69 ? 1058 HOH A H1     1 
HETATM 6886 H H2     . HOH H 4 .   ? 29.002 63.109 46.715 0.01 34.69 ? 1058 HOH A H2     1 
HETATM 6887 O O      . HOH H 4 .   ? 29.404 14.477 41.941 1.00 35.64 ? 1059 HOH A O      1 
HETATM 6888 H H1     . HOH H 4 .   ? 29.730 15.243 41.773 0.01 42.77 ? 1059 HOH A H1     1 
HETATM 6889 H H2     . HOH H 4 .   ? 28.631 14.499 41.588 0.01 42.77 ? 1059 HOH A H2     1 
HETATM 6890 O O      . HOH H 4 .   ? 29.154 15.003 39.440 1.00 38.54 ? 1060 HOH A O      1 
HETATM 6891 H H1     . HOH H 4 .   ? 29.758 15.575 39.613 0.01 46.24 ? 1060 HOH A H1     1 
HETATM 6892 H H2     . HOH H 4 .   ? 28.430 15.442 39.504 0.01 46.24 ? 1060 HOH A H2     1 
HETATM 6893 O O      . HOH H 4 .   ? 27.545 12.668 42.959 1.00 40.90 ? 1061 HOH A O      1 
HETATM 6894 H H1     . HOH H 4 .   ? 28.071 13.270 43.246 0.01 49.09 ? 1061 HOH A H1     1 
HETATM 6895 H H2     . HOH H 4 .   ? 26.841 12.775 43.424 0.01 49.09 ? 1061 HOH A H2     1 
HETATM 6896 O O      . HOH H 4 .   ? 46.055 40.289 42.240 1.00 32.71 ? 1062 HOH A O      1 
HETATM 6897 H H1     . HOH H 4 .   ? 46.651 40.877 42.085 0.01 39.25 ? 1062 HOH A H1     1 
HETATM 6898 H H2     . HOH H 4 .   ? 45.329 40.731 42.237 0.01 39.25 ? 1062 HOH A H2     1 
HETATM 6899 O O      . HOH H 4 .   ? 40.389 25.166 35.078 1.00 38.61 ? 1063 HOH A O      1 
HETATM 6900 H H1     . HOH H 4 .   ? 41.182 25.474 35.078 0.01 46.34 ? 1063 HOH A H1     1 
HETATM 6901 H H2     . HOH H 4 .   ? 39.908 25.842 35.261 0.01 46.34 ? 1063 HOH A H2     1 
HETATM 6902 O O      . HOH H 4 .   ? 31.776 46.068 63.161 1.00 49.94 ? 1064 HOH A O      1 
HETATM 6903 H H1     . HOH H 4 .   ? 32.456 46.569 63.269 0.01 59.93 ? 1064 HOH A H1     1 
HETATM 6904 H H2     . HOH H 4 .   ? 31.118 46.594 63.273 0.01 59.93 ? 1064 HOH A H2     1 
HETATM 6905 O O      . HOH H 4 .   ? 21.761 26.794 34.528 1.00 39.26 ? 1065 HOH A O      1 
HETATM 6906 H H1     . HOH H 4 .   ? 22.600 26.924 34.528 0.01 47.11 ? 1065 HOH A H1     1 
HETATM 6907 H H2     . HOH H 4 .   ? 21.442 27.515 34.847 0.01 47.11 ? 1065 HOH A H2     1 
HETATM 6908 O O      . HOH H 4 .   ? 46.967 26.890 47.814 1.00 35.67 ? 1066 HOH A O      1 
HETATM 6909 H H1     . HOH H 4 .   ? 47.778 27.074 47.973 0.01 42.81 ? 1066 HOH A H1     1 
HETATM 6910 H H2     . HOH H 4 .   ? 46.813 27.359 47.125 0.01 42.81 ? 1066 HOH A H2     1 
HETATM 6911 O O      . HOH H 4 .   ? 42.805 30.913 36.112 1.00 40.76 ? 1067 HOH A O      1 
HETATM 6912 H H1     . HOH H 4 .   ? 43.486 31.422 36.118 0.01 48.91 ? 1067 HOH A H1     1 
HETATM 6913 H H2     . HOH H 4 .   ? 42.148 31.451 36.084 0.01 48.91 ? 1067 HOH A H2     1 
HETATM 6914 O O      . HOH H 4 .   ? 23.198 23.785 52.141 1.00 34.38 ? 1068 HOH A O      1 
HETATM 6915 H H1     . HOH H 4 .   ? 23.871 24.306 52.124 0.01 41.26 ? 1068 HOH A H1     1 
HETATM 6916 H H2     . HOH H 4 .   ? 22.533 24.313 52.124 0.01 41.26 ? 1068 HOH A H2     1 
HETATM 6917 O O      . HOH H 4 .   ? 4.865  20.502 46.720 1.00 39.95 ? 1069 HOH A O      1 
HETATM 6918 H H1     . HOH H 4 .   ? 5.417  21.087 46.994 0.01 47.94 ? 1069 HOH A H1     1 
HETATM 6919 H H2     . HOH H 4 .   ? 4.111  20.891 46.776 0.01 47.94 ? 1069 HOH A H2     1 
HETATM 6920 O O      . HOH H 4 .   ? 17.774 14.624 40.253 1.00 39.49 ? 1070 HOH A O      1 
HETATM 6921 H H1     . HOH H 4 .   ? 18.437 15.156 40.259 0.01 47.39 ? 1070 HOH A H1     1 
HETATM 6922 H H2     . HOH H 4 .   ? 17.098 15.141 40.259 0.01 47.39 ? 1070 HOH A H2     1 
HETATM 6923 O O      . HOH H 4 .   ? 21.489 62.219 55.823 1.00 36.07 ? 1071 HOH A O      1 
HETATM 6924 H H1     . HOH H 4 .   ? 22.156 62.745 55.826 0.01 43.29 ? 1071 HOH A H1     1 
HETATM 6925 H H2     . HOH H 4 .   ? 20.818 62.741 55.826 0.01 43.29 ? 1071 HOH A H2     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . GLY A 1   ? 0.9471 0.4915 0.4691 0.0049  -0.2479 -0.0665 184  GLY A N     
2    C CA    . GLY A 1   ? 0.8992 0.4756 0.4357 0.0044  -0.2675 -0.0647 184  GLY A CA    
3    C C     . GLY A 1   ? 0.8172 0.4537 0.4041 -0.0250 -0.2744 -0.0645 184  GLY A C     
4    O O     . GLY A 1   ? 0.8193 0.4475 0.4271 -0.0400 -0.2458 -0.0730 184  GLY A O     
7    N N     . ALA A 2   ? 0.7587 0.4359 0.3768 -0.0263 -0.2659 -0.0524 185  ALA A N     
8    C CA    . ALA A 2   ? 0.6665 0.4080 0.3393 -0.0419 -0.2391 -0.0323 185  ALA A CA    
9    C C     . ALA A 2   ? 0.5604 0.3517 0.3169 -0.0229 -0.2311 -0.0007 185  ALA A C     
10   O O     . ALA A 2   ? 0.6025 0.3380 0.3049 -0.0149 -0.2173 -0.0140 185  ALA A O     
11   C CB    . ALA A 2   ? 0.6705 0.4287 0.3401 -0.0597 -0.2301 -0.0523 185  ALA A CB    
17   N N     . LYS A 3   ? 0.4741 0.3111 0.3260 -0.0117 -0.1909 0.0300  186  LYS A N     
18   C CA    . LYS A 3   ? 0.4128 0.2611 0.3204 0.0029  -0.2025 0.0301  186  LYS A CA    
19   C C     . LYS A 3   ? 0.3733 0.2227 0.2774 -0.0111 -0.1528 0.0327  186  LYS A C     
20   O O     . LYS A 3   ? 0.4177 0.2450 0.3173 -0.0005 -0.1339 0.0511  186  LYS A O     
21   C CB    . LYS A 3   ? 0.4314 0.2684 0.3773 0.0432  -0.2125 0.0077  186  LYS A CB    
22   C CG    . LYS A 3   ? 0.4769 0.2751 0.4264 0.0787  -0.2047 -0.0113 186  LYS A CG    
23   C CD    . LYS A 3   ? 0.5218 0.2815 0.4873 0.1157  -0.2069 -0.0289 186  LYS A CD    
24   C CE    . LYS A 3   ? 0.5575 0.2949 0.5296 0.1107  -0.2119 -0.0519 186  LYS A CE    
25   N NZ    . LYS A 3   ? 0.5563 0.3014 0.5277 0.1422  -0.2431 -0.0471 186  LYS A NZ    
39   N N     . VAL A 4   ? 0.3014 0.1728 0.2246 -0.0071 -0.1189 0.0056  187  VAL A N     
40   C CA    . VAL A 4   ? 0.2702 0.1577 0.2094 -0.0102 -0.0730 -0.0157 187  VAL A CA    
41   C C     . VAL A 4   ? 0.2671 0.1535 0.2411 -0.0056 -0.0612 -0.0253 187  VAL A C     
42   O O     . VAL A 4   ? 0.2819 0.1755 0.2666 -0.0318 -0.0342 -0.0389 187  VAL A O     
43   C CB    . VAL A 4   ? 0.2343 0.1624 0.2093 -0.0129 -0.0734 -0.0185 187  VAL A CB    
44   C CG1   . VAL A 4   ? 0.2493 0.1632 0.2110 -0.0171 -0.0542 -0.0202 187  VAL A CG1   
45   C CG2   . VAL A 4   ? 0.2729 0.1791 0.2391 -0.0091 -0.0671 -0.0250 187  VAL A CG2   
55   N N     . GLY A 5   ? 0.2023 0.1253 0.2410 0.0076  -0.0946 -0.0150 188  GLY A N     
56   C CA    . GLY A 5   ? 0.1851 0.1065 0.2355 0.0091  -0.0994 0.0028  188  GLY A CA    
57   C C     . GLY A 5   ? 0.1592 0.1051 0.2145 0.0034  -0.0682 0.0026  188  GLY A C     
58   O O     . GLY A 5   ? 0.1581 0.1099 0.2390 0.0015  -0.0808 -0.0017 188  GLY A O     
62   N N     . LYS A 6   ? 0.1509 0.0952 0.2279 0.0231  -0.0897 -0.0025 189  LYS A N     
63   C CA    . LYS A 6   ? 0.1322 0.0863 0.2167 0.0159  -0.0763 0.0067  189  LYS A CA    
64   C C     . LYS A 6   ? 0.1077 0.0951 0.2044 0.0115  -0.0674 0.0090  189  LYS A C     
65   O O     . LYS A 6   ? 0.1192 0.1014 0.2201 0.0189  -0.0725 0.0019  189  LYS A O     
66   C CB    . LYS A 6   ? 0.1450 0.0884 0.2267 0.0221  -0.0860 -0.0007 189  LYS A CB    
67   C CG    . LYS A 6   ? 0.1741 0.0995 0.2412 0.0289  -0.0966 -0.0003 189  LYS A CG    
68   C CD    . LYS A 6   ? 0.2116 0.1133 0.3061 0.0169  -0.1314 0.0036  189  LYS A CD    
69   C CE    . LYS A 6   ? 0.2525 0.1333 0.3715 0.0027  -0.1680 0.0143  189  LYS A CE    
70   N NZ    . LYS A 6   ? 0.2576 0.1535 0.3701 0.0071  -0.1548 0.0412  189  LYS A NZ    
84   N N     . ILE A 7   ? 0.1092 0.0976 0.2074 0.0090  -0.0771 0.0087  190  ILE A N     
85   C CA    . ILE A 7   ? 0.1220 0.0952 0.1720 0.0198  -0.0546 0.0056  190  ILE A CA    
86   C C     . ILE A 7   ? 0.0977 0.1017 0.1740 0.0206  -0.0415 0.0097  190  ILE A C     
87   O O     . ILE A 7   ? 0.1147 0.1133 0.2335 0.0018  -0.0576 -0.0029 190  ILE A O     
88   C CB    . ILE A 7   ? 0.1724 0.0893 0.2048 0.0154  -0.0907 0.0096  190  ILE A CB    
89   C CG1   . ILE A 7   ? 0.1748 0.0894 0.1885 0.0014  -0.0826 0.0117  190  ILE A CG1   
90   C CG2   . ILE A 7   ? 0.2099 0.0914 0.2086 0.0128  -0.1137 0.0044  190  ILE A CG2   
91   C CD1   . ILE A 7   ? 0.1903 0.0953 0.2070 -0.0115 -0.0790 0.0119  190  ILE A CD1   
103  N N     . GLY A 8   ? 0.1262 0.0961 0.2158 0.0298  -0.0766 -0.0095 191  GLY A N     
104  C CA    . GLY A 8   ? 0.1453 0.1003 0.2218 0.0294  -0.0867 -0.0040 191  GLY A CA    
105  C C     . GLY A 8   ? 0.1190 0.0987 0.2022 0.0112  -0.0853 -0.0049 191  GLY A C     
106  O O     . GLY A 8   ? 0.0990 0.1099 0.2202 0.0164  -0.0641 0.0143  191  GLY A O     
110  N N     . VAL A 9   ? 0.1108 0.1187 0.2182 0.0174  -0.0786 -0.0022 192  VAL A N     
111  C CA    . VAL A 9   ? 0.0969 0.1264 0.2126 -0.0230 -0.0267 -0.0199 192  VAL A CA    
112  C C     . VAL A 9   ? 0.0854 0.1205 0.2113 -0.0125 -0.0346 -0.0125 192  VAL A C     
113  O O     . VAL A 9   ? 0.1175 0.1433 0.2325 -0.0315 -0.0376 -0.0361 192  VAL A O     
114  C CB    . VAL A 9   ? 0.1420 0.1544 0.2646 -0.0628 -0.0131 -0.0494 192  VAL A CB    
115  C CG1   . VAL A 9   ? 0.2373 0.1386 0.3144 -0.0861 0.0105  -0.0405 192  VAL A CG1   
116  C CG2   . VAL A 9   ? 0.1558 0.1902 0.2828 -0.0712 -0.0285 -0.0624 192  VAL A CG2   
126  N N     . CYS A 10  ? 0.0910 0.0979 0.2027 0.0011  -0.0580 -0.0054 193  CYS A N     
127  C CA    . CYS A 10  ? 0.1089 0.0848 0.2056 0.0030  -0.0645 0.0038  193  CYS A CA    
128  C C     . CYS A 10  ? 0.0957 0.0704 0.2167 -0.0042 -0.0704 0.0032  193  CYS A C     
129  O O     . CYS A 10  ? 0.1002 0.0662 0.2219 -0.0016 -0.0729 0.0074  193  CYS A O     
130  C CB    . CYS A 10  ? 0.1258 0.0791 0.2201 -0.0069 -0.0685 -0.0113 193  CYS A CB    
131  S SG    . CYS A 10  ? 0.1233 0.0804 0.2594 -0.0036 -0.0880 0.0016  193  CYS A SG    
137  N N     . ALA A 11  ? 0.0939 0.0782 0.2127 -0.0004 -0.0646 0.0131  194  ALA A N     
138  C CA    . ALA A 11  ? 0.0949 0.0942 0.2062 -0.0198 -0.0623 0.0109  194  ALA A CA    
139  C C     . ALA A 11  ? 0.0837 0.0957 0.1899 -0.0223 -0.0520 0.0032  194  ALA A C     
140  O O     . ALA A 11  ? 0.0869 0.1119 0.2166 0.0077  -0.0611 0.0085  194  ALA A O     
141  C CB    . ALA A 11  ? 0.1183 0.1095 0.1891 -0.0057 -0.0530 -0.0052 194  ALA A CB    
147  N N     . MET A 12  ? 0.0802 0.0990 0.2156 -0.0135 -0.0523 0.0024  195  MET A N     
148  C CA    . MET A 12  ? 0.0895 0.1146 0.2317 -0.0209 -0.0504 -0.0113 195  MET A CA    
149  C C     . MET A 12  ? 0.0824 0.1214 0.2323 -0.0022 -0.0332 -0.0132 195  MET A C     
150  O O     . MET A 12  ? 0.0894 0.1174 0.2575 -0.0068 -0.0570 -0.0154 195  MET A O     
151  C CB    . MET A 12  ? 0.1111 0.1456 0.2413 -0.0105 -0.0804 -0.0080 195  MET A CB    
152  C CG    . MET A 12  ? 0.1263 0.1620 0.2370 -0.0069 -0.0655 -0.0113 195  MET A CG    
153  S SD    . MET A 12  ? 0.1262 0.1806 0.2984 -0.0238 -0.0669 -0.0566 195  MET A SD    
154  C CE    . MET A 12  ? 0.1227 0.2281 0.3619 -0.0299 -0.0422 -0.0730 195  MET A CE    
164  N N     . ASP A 13  ? 0.0907 0.1471 0.2182 0.0010  -0.0381 -0.0188 196  ASP A N     
165  C CA    . ASP A 13  ? 0.0847 0.1733 0.2376 -0.0119 -0.0384 -0.0185 196  ASP A CA    
166  C C     . ASP A 13  ? 0.0836 0.1736 0.2618 -0.0152 -0.0442 -0.0154 196  ASP A C     
167  O O     . ASP A 13  ? 0.1039 0.1831 0.2736 -0.0301 -0.0545 -0.0337 196  ASP A O     
168  C CB    . ASP A 13  ? 0.1277 0.1841 0.2686 0.0001  -0.0510 -0.0082 196  ASP A CB    
169  C CG    . ASP A 13  ? 0.1049 0.2066 0.3252 0.0156  -0.0490 0.0091  196  ASP A CG    
170  O OD1   . ASP A 13  ? 0.1442 0.2116 0.3479 0.0004  -0.0588 0.0314  196  ASP A OD1   
171  O OD2   . ASP A 13  ? 0.1181 0.2228 0.3285 0.0183  -0.0373 0.0025  196  ASP A OD2   
176  N N     . ALA A 14  ? 0.1143 0.1592 0.2573 -0.0343 -0.0356 -0.0077 197  ALA A N     
177  C CA    . ALA A 14  ? 0.1602 0.1582 0.3061 -0.0185 -0.0184 0.0004  197  ALA A CA    
178  C C     . ALA A 14  ? 0.1220 0.1551 0.3104 -0.0238 -0.0275 -0.0029 197  ALA A C     
179  O O     . ALA A 14  ? 0.1665 0.1500 0.3707 -0.0613 -0.0065 -0.0198 197  ALA A O     
180  C CB    . ALA A 14  ? 0.2213 0.1562 0.3233 -0.0113 0.0284  -0.0030 197  ALA A CB    
186  N N     . LYS A 15  ? 0.1042 0.1561 0.2405 -0.0268 -0.0194 -0.0147 198  LYS A N     
187  C CA    . LYS A 15  ? 0.0740 0.1509 0.2516 -0.0257 -0.0208 -0.0020 198  LYS A CA    
188  C C     . LYS A 15  ? 0.1007 0.1337 0.2789 -0.0215 -0.0580 -0.0094 198  LYS A C     
189  O O     . LYS A 15  ? 0.1002 0.1351 0.3198 -0.0016 -0.0587 -0.0223 198  LYS A O     
190  C CB    . LYS A 15  ? 0.1117 0.1751 0.2848 -0.0175 -0.0775 -0.0030 198  LYS A CB    
191  C CG    . LYS A 15  ? 0.1637 0.2235 0.3461 -0.0141 -0.1188 0.0205  198  LYS A CG    
192  C CD    . LYS A 15  ? 0.2851 0.2675 0.3675 -0.0291 -0.1732 0.0513  198  LYS A CD    
193  C CE    . LYS A 15  ? 0.3818 0.3009 0.4320 -0.0658 -0.1827 0.0784  198  LYS A CE    
194  N NZ    . LYS A 15  ? 0.4543 0.3239 0.4904 -0.0927 -0.1704 0.0855  198  LYS A NZ    
208  N N     . VAL A 16  ? 0.0956 0.1160 0.2733 -0.0096 -0.0613 -0.0077 199  VAL A N     
209  C CA    . VAL A 16  ? 0.0989 0.1065 0.2749 -0.0162 -0.0519 -0.0119 199  VAL A CA    
210  C C     . VAL A 16  ? 0.0938 0.0996 0.2509 -0.0011 -0.0381 -0.0136 199  VAL A C     
211  O O     . VAL A 16  ? 0.1206 0.0973 0.2838 -0.0096 -0.0596 -0.0225 199  VAL A O     
212  C CB    . VAL A 16  ? 0.1456 0.1325 0.2491 -0.0518 -0.0370 -0.0007 199  VAL A CB    
213  C CG1   . VAL A 16  ? 0.1965 0.1556 0.2494 -0.0569 -0.0408 -0.0006 199  VAL A CG1   
214  C CG2   . VAL A 16  ? 0.1708 0.1616 0.2573 -0.0881 -0.0415 -0.0095 199  VAL A CG2   
224  N N     . LEU A 17  ? 0.0806 0.1092 0.2354 -0.0060 -0.0499 -0.0182 200  LEU A N     
225  C CA    . LEU A 17  ? 0.0919 0.1069 0.2792 -0.0093 -0.0528 -0.0118 200  LEU A CA    
226  C C     . LEU A 17  ? 0.0931 0.1064 0.3100 -0.0084 -0.0423 -0.0169 200  LEU A C     
227  O O     . LEU A 17  ? 0.1033 0.1263 0.3133 -0.0294 -0.0183 -0.0242 200  LEU A O     
228  C CB    . LEU A 17  ? 0.0970 0.1167 0.3148 -0.0145 -0.0478 0.0016  200  LEU A CB    
229  C CG    . LEU A 17  ? 0.1079 0.1418 0.4017 0.0050  -0.0386 0.0075  200  LEU A CG    
230  C CD1   . LEU A 17  ? 0.1440 0.1488 0.4842 0.0126  -0.0008 0.0028  200  LEU A CD1   
231  C CD2   . LEU A 17  ? 0.1480 0.1591 0.4206 0.0081  -0.0625 0.0518  200  LEU A CD2   
243  N N     . SER A 18  ? 0.1037 0.0960 0.2969 0.0041  -0.0578 -0.0046 201  SER A N     
244  C CA    . SER A 18  ? 0.1166 0.1012 0.2699 0.0026  -0.0676 0.0083  201  SER A CA    
245  C C     . SER A 18  ? 0.1107 0.1017 0.2880 0.0010  -0.0506 -0.0058 201  SER A C     
246  O O     . SER A 18  ? 0.0991 0.0849 0.3050 0.0019  -0.0521 -0.0057 201  SER A O     
247  C CB    . SER A 18  ? 0.1378 0.1148 0.2658 0.0147  -0.0454 0.0357  201  SER A CB    
248  O OG    . SER A 18  ? 0.1238 0.1259 0.2991 0.0060  -0.0481 0.0287  201  SER A OG    
254  N N     . LYS A 19  ? 0.1380 0.0948 0.2971 -0.0063 -0.0619 -0.0136 202  LYS A N     
255  C CA    . LYS A 19  ? 0.1234 0.0851 0.2940 -0.0108 -0.0536 -0.0002 202  LYS A CA    
256  C C     . LYS A 19  ? 0.1025 0.0799 0.2817 -0.0035 -0.0651 0.0023  202  LYS A C     
257  O O     . LYS A 19  ? 0.1026 0.0836 0.2659 -0.0065 -0.0704 0.0013  202  LYS A O     
258  C CB    . LYS A 19  ? 0.1718 0.0937 0.3246 -0.0300 -0.0271 -0.0024 202  LYS A CB    
259  C CG    . LYS A 19  ? 0.2516 0.1293 0.4075 -0.0489 0.0217  0.0127  202  LYS A CG    
260  C CD    . LYS A 19  ? 0.3685 0.1712 0.4760 -0.0595 0.0445  0.0126  202  LYS A CD    
261  C CE    . LYS A 19  ? 0.4806 0.1794 0.4987 -0.0824 0.0459  0.0359  202  LYS A CE    
262  N NZ    . LYS A 19  ? 0.5385 0.1788 0.5258 -0.0893 0.0426  0.0624  202  LYS A NZ    
276  N N     . PRO A 20  ? 0.0933 0.0950 0.2578 0.0031  -0.0642 0.0057  203  PRO A N     
277  C CA    . PRO A 20  ? 0.0877 0.0924 0.2423 0.0119  -0.0548 0.0010  203  PRO A CA    
278  C C     . PRO A 20  ? 0.0843 0.0798 0.2508 0.0032  -0.0555 -0.0111 203  PRO A C     
279  O O     . PRO A 20  ? 0.0899 0.0830 0.2633 -0.0007 -0.0532 -0.0222 203  PRO A O     
280  C CB    . PRO A 20  ? 0.1158 0.1159 0.3028 0.0168  -0.0664 0.0169  203  PRO A CB    
281  C CG    . PRO A 20  ? 0.1841 0.1482 0.3380 0.0350  -0.0726 0.0245  203  PRO A CG    
282  C CD    . PRO A 20  ? 0.1265 0.1100 0.2892 0.0076  -0.0567 0.0171  203  PRO A CD    
290  N N     . MET A 21  ? 0.0898 0.0755 0.2265 0.0052  -0.0651 -0.0140 204  MET A N     
291  C CA    . MET A 21  ? 0.0894 0.0808 0.2321 0.0022  -0.0634 -0.0145 204  MET A CA    
292  C C     . MET A 21  ? 0.0810 0.0861 0.2012 -0.0144 -0.0438 -0.0178 204  MET A C     
293  O O     . MET A 21  ? 0.0952 0.0982 0.1909 -0.0074 -0.0564 -0.0285 204  MET A O     
294  C CB    . MET A 21  ? 0.1050 0.0937 0.2214 -0.0080 -0.0676 -0.0069 204  MET A CB    
295  C CG    . MET A 21  ? 0.1042 0.0922 0.2361 -0.0014 -0.0775 -0.0004 204  MET A CG    
296  S SD    . MET A 21  ? 0.1055 0.0951 0.2727 -0.0021 -0.0730 -0.0024 204  MET A SD    
297  C CE    . MET A 21  ? 0.1231 0.1172 0.2556 -0.0063 -0.0873 -0.0178 204  MET A CE    
307  N N     . ARG A 22  ? 0.0877 0.0949 0.2126 0.0003  -0.0626 -0.0178 205  ARG A N     
308  C CA    A ARG A 22  ? 0.0770 0.1090 0.2132 0.0039  -0.0536 -0.0060 205  ARG A CA    
309  C CA    B ARG A 22  ? 0.0870 0.1225 0.2200 0.0041  -0.0630 -0.0109 205  ARG A CA    
310  C C     . ARG A 22  ? 0.0987 0.1178 0.2346 0.0052  -0.0728 -0.0094 205  ARG A C     
311  O O     . ARG A 22  ? 0.1119 0.1278 0.2498 0.0080  -0.0829 -0.0169 205  ARG A O     
312  C CB    A ARG A 22  ? 0.0937 0.1334 0.2503 -0.0091 -0.0594 -0.0212 205  ARG A CB    
313  C CB    B ARG A 22  ? 0.0908 0.1646 0.2276 0.0018  -0.0655 -0.0149 205  ARG A CB    
314  C CG    A ARG A 22  ? 0.1342 0.1489 0.2752 -0.0250 -0.0627 -0.0331 205  ARG A CG    
315  C CG    B ARG A 22  ? 0.1022 0.2034 0.2269 0.0007  -0.0756 -0.0118 205  ARG A CG    
316  C CD    A ARG A 22  ? 0.1449 0.1582 0.3034 -0.0290 -0.0370 -0.0272 205  ARG A CD    
317  C CD    B ARG A 22  ? 0.1148 0.2438 0.2424 -0.0139 -0.0845 -0.0039 205  ARG A CD    
318  N NE    A ARG A 22  ? 0.1816 0.1467 0.3054 -0.0209 0.0055  -0.0106 205  ARG A NE    
319  N NE    B ARG A 22  ? 0.1884 0.2789 0.2782 -0.0259 -0.0987 0.0107  205  ARG A NE    
320  C CZ    A ARG A 22  ? 0.1686 0.1634 0.2859 -0.0270 -0.0424 -0.0299 205  ARG A CZ    
321  C CZ    B ARG A 22  ? 0.2362 0.3059 0.2950 -0.0567 -0.0608 0.0140  205  ARG A CZ    
322  N NH1   A ARG A 22  ? 0.2297 0.1927 0.2905 -0.0389 -0.0717 -0.0233 205  ARG A NH1   
323  N NH1   B ARG A 22  ? 0.2558 0.3155 0.2912 -0.0934 -0.0087 0.0198  205  ARG A NH1   
324  N NH2   A ARG A 22  ? 0.0980 0.1278 0.2462 -0.0344 -0.0349 -0.0277 205  ARG A NH2   
325  N NH2   B ARG A 22  ? 0.2757 0.3201 0.3252 -0.0548 -0.0296 0.0089  205  ARG A NH2   
352  N N     . HIS A 23  ? 0.0962 0.1034 0.2632 0.0086  -0.0669 -0.0215 206  HIS A N     
353  C CA    A HIS A 23  ? 0.1134 0.1031 0.2837 0.0076  -0.0814 -0.0185 206  HIS A CA    
354  C CA    B HIS A 23  ? 0.1108 0.1033 0.2747 0.0033  -0.0789 -0.0220 206  HIS A CA    
355  C C     . HIS A 23  ? 0.1144 0.0878 0.2389 0.0122  -0.0782 -0.0199 206  HIS A C     
356  O O     . HIS A 23  ? 0.1069 0.1029 0.2454 0.0041  -0.0670 -0.0079 206  HIS A O     
357  C CB    A HIS A 23  ? 0.1541 0.1336 0.3148 -0.0262 -0.0671 -0.0213 206  HIS A CB    
358  C CB    B HIS A 23  ? 0.1516 0.1351 0.2955 -0.0400 -0.0550 -0.0355 206  HIS A CB    
359  C CG    A HIS A 23  ? 0.1321 0.1802 0.3242 -0.0428 -0.0647 -0.0241 206  HIS A CG    
360  C CG    B HIS A 23  ? 0.1538 0.1880 0.2908 -0.0703 -0.0341 -0.0569 206  HIS A CG    
361  N ND1   A HIS A 23  ? 0.1633 0.2256 0.3622 -0.0372 -0.0830 0.0150  206  HIS A ND1   
362  N ND1   B HIS A 23  ? 0.1514 0.2131 0.2872 -0.0680 -0.0385 -0.0697 206  HIS A ND1   
363  C CD2   A HIS A 23  ? 0.1262 0.1888 0.3071 -0.0619 -0.0323 -0.0319 206  HIS A CD2   
364  C CD2   B HIS A 23  ? 0.1827 0.2209 0.2864 -0.1052 -0.0212 -0.0519 206  HIS A CD2   
365  C CE1   A HIS A 23  ? 0.1476 0.2387 0.3771 -0.0563 -0.0671 0.0140  206  HIS A CE1   
366  C CE1   B HIS A 23  ? 0.1889 0.2351 0.2910 -0.0893 -0.0605 -0.0635 206  HIS A CE1   
367  N NE2   A HIS A 23  ? 0.1730 0.2227 0.3705 -0.0832 -0.0546 -0.0199 206  HIS A NE2   
368  N NE2   B HIS A 23  ? 0.2065 0.2446 0.3030 -0.1058 -0.0633 -0.0541 206  HIS A NE2   
383  N N     . ILE A 24  ? 0.0961 0.0803 0.2227 -0.0008 -0.0680 -0.0151 207  ILE A N     
384  C CA    . ILE A 24  ? 0.0917 0.0801 0.2288 0.0054  -0.0666 -0.0081 207  ILE A CA    
385  C C     . ILE A 24  ? 0.1151 0.0913 0.2233 -0.0057 -0.0817 -0.0102 207  ILE A C     
386  O O     . ILE A 24  ? 0.1092 0.0901 0.2429 0.0068  -0.0798 -0.0015 207  ILE A O     
387  C CB    . ILE A 24  ? 0.0867 0.0843 0.2362 0.0071  -0.0586 -0.0013 207  ILE A CB    
388  C CG1   . ILE A 24  ? 0.0976 0.0890 0.2338 0.0051  -0.0594 0.0039  207  ILE A CG1   
389  C CG2   . ILE A 24  ? 0.1058 0.0850 0.2233 0.0065  -0.0701 0.0079  207  ILE A CG2   
390  C CD1   . ILE A 24  ? 0.1028 0.0998 0.2598 0.0062  -0.0652 0.0239  207  ILE A CD1   
402  N N     . LEU A 25  ? 0.1246 0.0967 0.2276 -0.0050 -0.0888 0.0031  208  LEU A N     
403  C CA    . LEU A 25  ? 0.1130 0.0841 0.2402 0.0030  -0.0829 0.0041  208  LEU A CA    
404  C C     . LEU A 25  ? 0.1264 0.0889 0.2454 0.0049  -0.0931 -0.0013 208  LEU A C     
405  O O     . LEU A 25  ? 0.1541 0.0910 0.2662 0.0058  -0.1082 0.0024  208  LEU A O     
406  C CB    . LEU A 25  ? 0.1224 0.0828 0.2699 -0.0063 -0.0834 0.0097  208  LEU A CB    
407  C CG    . LEU A 25  ? 0.1445 0.1097 0.2946 -0.0153 -0.0990 -0.0017 208  LEU A CG    
408  C CD1   . LEU A 25  ? 0.1848 0.1073 0.3282 -0.0094 -0.0888 -0.0200 208  LEU A CD1   
409  C CD2   . LEU A 25  ? 0.1573 0.1452 0.3199 -0.0325 -0.0892 -0.0228 208  LEU A CD2   
421  N N     . ASN A 26  ? 0.1221 0.1130 0.2470 0.0076  -0.0888 0.0066  209  ASN A N     
422  C CA    A ASN A 26  ? 0.1202 0.1355 0.2646 0.0068  -0.0873 0.0126  209  ASN A CA    
423  C CA    B ASN A 26  ? 0.1175 0.1407 0.2610 0.0036  -0.0862 0.0134  209  ASN A CA    
424  C C     . ASN A 26  ? 0.1253 0.1246 0.2461 0.0092  -0.0916 0.0034  209  ASN A C     
425  O O     . ASN A 26  ? 0.1646 0.1312 0.2601 0.0059  -0.1174 -0.0001 209  ASN A O     
426  C CB    A ASN A 26  ? 0.1458 0.1715 0.3145 -0.0066 -0.1085 -0.0012 209  ASN A CB    
427  C CB    B ASN A 26  ? 0.1298 0.1890 0.2947 -0.0159 -0.0949 0.0113  209  ASN A CB    
428  C CG    A ASN A 26  ? 0.1659 0.2063 0.3452 -0.0035 -0.1142 -0.0096 209  ASN A CG    
429  C CG    B ASN A 26  ? 0.1671 0.2322 0.3085 -0.0145 -0.0661 0.0159  209  ASN A CG    
430  O OD1   A ASN A 26  ? 0.2017 0.2306 0.3496 -0.0125 -0.0837 -0.0341 209  ASN A OD1   
431  O OD1   B ASN A 26  ? 0.1508 0.2347 0.2911 0.0047  0.0059  0.0081  209  ASN A OD1   
432  N ND2   A ASN A 26  ? 0.1487 0.2159 0.3371 0.0046  -0.1107 -0.0075 209  ASN A ND2   
433  N ND2   B ASN A 26  ? 0.2432 0.2651 0.3416 -0.0070 -0.0839 0.0202  209  ASN A ND2   
446  N N     . ARG A 27  ? 0.1310 0.1156 0.2401 0.0088  -0.0852 -0.0081 210  ARG A N     
447  C CA    . ARG A 27  ? 0.1523 0.1131 0.2650 -0.0009 -0.1050 -0.0019 210  ARG A CA    
448  C C     . ARG A 27  ? 0.1665 0.1146 0.2930 -0.0018 -0.0928 -0.0105 210  ARG A C     
449  O O     . ARG A 27  ? 0.1972 0.1220 0.2914 -0.0411 -0.0776 -0.0202 210  ARG A O     
450  C CB    . ARG A 27  ? 0.1538 0.1074 0.2745 -0.0125 -0.1045 -0.0061 210  ARG A CB    
451  C CG    . ARG A 27  ? 0.1621 0.1049 0.2669 -0.0117 -0.1022 -0.0178 210  ARG A CG    
452  C CD    . ARG A 27  ? 0.1588 0.0929 0.2745 0.0124  -0.0952 -0.0155 210  ARG A CD    
453  N NE    . ARG A 27  ? 0.1734 0.0908 0.2874 0.0038  -0.1071 -0.0098 210  ARG A NE    
454  C CZ    . ARG A 27  ? 0.1587 0.1075 0.2969 -0.0018 -0.1042 -0.0112 210  ARG A CZ    
455  N NH1   . ARG A 27  ? 0.1375 0.1312 0.2945 0.0015  -0.0879 -0.0309 210  ARG A NH1   
456  N NH2   . ARG A 27  ? 0.2176 0.1131 0.3272 -0.0319 -0.1034 -0.0034 210  ARG A NH2   
470  N N     . LEU A 28  ? 0.1388 0.1065 0.2696 -0.0167 -0.0906 -0.0068 211  LEU A N     
471  C CA    . LEU A 28  ? 0.1561 0.1120 0.2627 -0.0257 -0.0859 0.0078  211  LEU A CA    
472  C C     . LEU A 28  ? 0.1562 0.1383 0.2473 -0.0213 -0.1051 0.0050  211  LEU A C     
473  O O     . LEU A 28  ? 0.1822 0.1591 0.2217 -0.0248 -0.0904 0.0189  211  LEU A O     
474  C CB    . LEU A 28  ? 0.1318 0.0979 0.2645 -0.0036 -0.0980 0.0108  211  LEU A CB    
475  C CG    . LEU A 28  ? 0.1393 0.1105 0.2810 0.0082  -0.0794 0.0079  211  LEU A CG    
476  C CD1   . LEU A 28  ? 0.1392 0.1174 0.2762 0.0362  -0.0797 -0.0099 211  LEU A CD1   
477  C CD2   . LEU A 28  ? 0.1931 0.1261 0.3062 0.0149  -0.0906 0.0252  211  LEU A CD2   
489  N N     . ILE A 29  ? 0.1562 0.1270 0.2618 -0.0008 -0.1132 0.0072  212  ILE A N     
490  C CA    . ILE A 29  ? 0.1941 0.1433 0.2871 0.0145  -0.1276 0.0184  212  ILE A CA    
491  C C     . ILE A 29  ? 0.2154 0.1700 0.3146 0.0060  -0.1431 0.0243  212  ILE A C     
492  O O     . ILE A 29  ? 0.2306 0.1891 0.3316 0.0077  -0.1526 0.0331  212  ILE A O     
493  C CB    . ILE A 29  ? 0.2764 0.1512 0.3105 0.0460  -0.1130 0.0207  212  ILE A CB    
494  C CG1   . ILE A 29  ? 0.3015 0.1767 0.3373 0.0668  -0.0700 0.0213  212  ILE A CG1   
495  C CG2   . ILE A 29  ? 0.3253 0.1341 0.2795 0.0232  -0.1207 0.0178  212  ILE A CG2   
496  C CD1   . ILE A 29  ? 0.3431 0.1873 0.3864 0.0511  0.0473  0.0283  212  ILE A CD1   
508  N N     . GLU A 30  ? 0.2443 0.1794 0.3323 -0.0202 -0.1659 0.0137  213  GLU A N     
509  C CA    . GLU A 30  ? 0.2783 0.2232 0.3655 -0.0325 -0.1858 0.0231  213  GLU A CA    
510  C C     . GLU A 30  ? 0.2949 0.2340 0.3520 -0.0371 -0.1874 0.0107  213  GLU A C     
511  O O     . GLU A 30  ? 0.2986 0.2665 0.3851 -0.0584 -0.1903 0.0168  213  GLU A O     
512  C CB    . GLU A 30  ? 0.3150 0.2507 0.4143 -0.0483 -0.2090 0.0394  213  GLU A CB    
513  C CG    . GLU A 30  ? 0.3160 0.2547 0.4688 -0.0528 -0.2166 0.0476  213  GLU A CG    
514  C CD    . GLU A 30  ? 0.3332 0.2839 0.5863 -0.0524 -0.1980 0.0751  213  GLU A CD    
515  O OE1   . GLU A 30  ? 0.3832 0.3193 0.6480 -0.0779 -0.1715 0.0727  213  GLU A OE1   
516  O OE2   . GLU A 30  ? 0.3314 0.2802 0.6170 -0.0373 -0.2191 0.0898  213  GLU A OE2   
523  N N     . HIS A 31  ? 0.3363 0.2158 0.3066 -0.0194 -0.1886 0.0024  214  HIS A N     
524  C CA    . HIS A 31  ? 0.3602 0.2166 0.3102 -0.0039 -0.1825 -0.0072 214  HIS A CA    
525  C C     . HIS A 31  ? 0.3550 0.2122 0.2884 -0.0025 -0.1877 -0.0153 214  HIS A C     
526  O O     . HIS A 31  ? 0.3857 0.2404 0.3010 -0.0001 -0.1937 -0.0200 214  HIS A O     
527  C CB    . HIS A 31  ? 0.4471 0.2264 0.3635 -0.0024 -0.1822 -0.0121 214  HIS A CB    
528  C CG    . HIS A 31  ? 0.4771 0.2435 0.4246 -0.0133 -0.2090 -0.0016 214  HIS A CG    
529  N ND1   . HIS A 31  ? 0.5134 0.2384 0.4707 -0.0410 -0.2225 -0.0041 214  HIS A ND1   
530  C CD2   . HIS A 31  ? 0.5003 0.2648 0.4735 -0.0189 -0.1835 -0.0077 214  HIS A CD2   
531  C CE1   . HIS A 31  ? 0.5123 0.2517 0.4877 -0.0198 -0.1981 -0.0096 214  HIS A CE1   
532  N NE2   . HIS A 31  ? 0.5165 0.2675 0.5011 -0.0193 -0.1560 -0.0152 214  HIS A NE2   
540  N N     . GLY A 32  ? 0.3178 0.1767 0.3223 0.0013  -0.1918 -0.0022 215  GLY A N     
541  C CA    . GLY A 32  ? 0.3109 0.1602 0.3201 0.0088  -0.1796 0.0012  215  GLY A CA    
542  C C     . GLY A 32  ? 0.2907 0.1631 0.3153 -0.0058 -0.1777 -0.0095 215  GLY A C     
543  O O     . GLY A 32  ? 0.3069 0.1772 0.3355 0.0040  -0.1423 0.0139  215  GLY A O     
547  N N     . GLU A 33  ? 0.2966 0.1655 0.2976 0.0042  -0.1746 -0.0200 216  GLU A N     
548  C CA    . GLU A 33  ? 0.2946 0.1662 0.2647 0.0116  -0.1382 -0.0335 216  GLU A CA    
549  C C     . GLU A 33  ? 0.2641 0.1431 0.2444 0.0211  -0.1400 -0.0094 216  GLU A C     
550  O O     . GLU A 33  ? 0.2582 0.1465 0.2483 0.0256  -0.0985 -0.0011 216  GLU A O     
551  C CB    . GLU A 33  ? 0.2914 0.1833 0.2835 0.0128  -0.1531 -0.0423 216  GLU A CB    
552  C CG    . GLU A 33  ? 0.3244 0.2091 0.3101 0.0444  -0.1357 -0.0251 216  GLU A CG    
553  C CD    . GLU A 33  ? 0.4003 0.2358 0.3370 0.0557  -0.0857 -0.0068 216  GLU A CD    
554  O OE1   . GLU A 33  ? 0.4680 0.2549 0.3897 0.0909  -0.0816 0.0055  216  GLU A OE1   
555  O OE2   . GLU A 33  ? 0.4325 0.2441 0.3296 0.0333  -0.0448 0.0029  216  GLU A OE2   
562  N N     . PHE A 34  ? 0.2044 0.1140 0.2546 0.0153  -0.1230 -0.0083 217  PHE A N     
563  C CA    . PHE A 34  ? 0.1800 0.1045 0.2534 0.0239  -0.1088 -0.0129 217  PHE A CA    
564  C C     . PHE A 34  ? 0.1567 0.1034 0.2548 0.0180  -0.1037 0.0003  217  PHE A C     
565  O O     . PHE A 34  ? 0.1600 0.1102 0.2935 0.0103  -0.1064 0.0057  217  PHE A O     
566  C CB    . PHE A 34  ? 0.1720 0.1014 0.2400 0.0209  -0.1084 -0.0042 217  PHE A CB    
567  C CG    . PHE A 34  ? 0.1665 0.1006 0.2338 0.0181  -0.1062 0.0008  217  PHE A CG    
568  C CD1   . PHE A 34  ? 0.1483 0.0982 0.2339 0.0202  -0.0917 0.0058  217  PHE A CD1   
569  C CD2   . PHE A 34  ? 0.1771 0.0937 0.2622 0.0075  -0.0988 -0.0087 217  PHE A CD2   
570  C CE1   . PHE A 34  ? 0.1668 0.0908 0.2544 0.0082  -0.1020 0.0124  217  PHE A CE1   
571  C CE2   . PHE A 34  ? 0.2211 0.0945 0.2423 0.0123  -0.0929 -0.0120 217  PHE A CE2   
572  C CZ    . PHE A 34  ? 0.1909 0.0793 0.2382 0.0072  -0.0928 0.0009  217  PHE A CZ    
582  N N     . GLU A 35  ? 0.1477 0.1118 0.2503 0.0135  -0.1063 -0.0107 218  GLU A N     
583  C CA    . GLU A 35  ? 0.1576 0.1297 0.2763 0.0267  -0.0952 -0.0131 218  GLU A CA    
584  C C     . GLU A 35  ? 0.1287 0.1374 0.2364 0.0077  -0.0764 -0.0050 218  GLU A C     
585  O O     . GLU A 35  ? 0.1340 0.1796 0.2551 -0.0013 -0.0875 0.0089  218  GLU A O     
586  C CB    . GLU A 35  ? 0.2239 0.1424 0.3260 0.0598  -0.1027 -0.0202 218  GLU A CB    
587  C CG    . GLU A 35  ? 0.2624 0.1625 0.3885 0.0288  -0.1417 0.0024  218  GLU A CG    
588  C CD    . GLU A 35  ? 0.2834 0.1829 0.3984 0.0392  -0.1528 0.0250  218  GLU A CD    
589  O OE1   . GLU A 35  ? 0.2669 0.2028 0.4127 0.0312  -0.1441 0.0530  218  GLU A OE1   
590  O OE2   . GLU A 35  ? 0.3433 0.1855 0.4579 0.0304  -0.0782 0.0041  218  GLU A OE2   
597  N N     . THR A 36  ? 0.1190 0.1160 0.2306 -0.0104 -0.0844 -0.0103 219  THR A N     
598  C CA    A THR A 36  ? 0.1533 0.1272 0.2310 -0.0204 -0.0959 -0.0070 219  THR A CA    
599  C CA    B THR A 36  ? 0.1519 0.1180 0.2475 -0.0173 -0.0920 -0.0058 219  THR A CA    
600  C C     . THR A 36  ? 0.1467 0.1291 0.2529 0.0117  -0.0847 -0.0165 219  THR A C     
601  O O     . THR A 36  ? 0.1509 0.1590 0.3014 0.0343  -0.1066 -0.0491 219  THR A O     
602  C CB    A THR A 36  ? 0.2035 0.1477 0.2653 -0.0292 -0.1018 0.0104  219  THR A CB    
603  C CB    B THR A 36  ? 0.2042 0.1197 0.2906 -0.0415 -0.1032 0.0090  219  THR A CB    
604  O OG1   A THR A 36  ? 0.1721 0.1905 0.2876 -0.0397 -0.0432 0.0206  219  THR A OG1   
605  O OG1   B THR A 36  ? 0.2165 0.1336 0.3131 -0.0533 -0.1061 0.0075  219  THR A OG1   
606  C CG2   A THR A 36  ? 0.2522 0.1273 0.2631 -0.0071 -0.1462 0.0107  219  THR A CG2   
607  C CG2   B THR A 36  ? 0.2213 0.1141 0.2908 -0.0527 -0.0846 0.0094  219  THR A CG2   
622  N N     . VAL A 37  ? 0.1286 0.1159 0.2426 -0.0036 -0.0829 -0.0198 220  VAL A N     
623  C CA    . VAL A 37  ? 0.1464 0.1185 0.2439 -0.0096 -0.0851 -0.0337 220  VAL A CA    
624  C C     . VAL A 37  ? 0.1285 0.1440 0.2402 -0.0070 -0.0670 -0.0489 220  VAL A C     
625  O O     . VAL A 37  ? 0.1856 0.1289 0.2426 0.0052  -0.0636 -0.0172 220  VAL A O     
626  C CB    . VAL A 37  ? 0.1320 0.1098 0.2363 -0.0026 -0.0691 -0.0152 220  VAL A CB    
627  C CG1   . VAL A 37  ? 0.1622 0.1038 0.2372 -0.0074 -0.0629 -0.0220 220  VAL A CG1   
628  C CG2   . VAL A 37  ? 0.1383 0.1127 0.2533 0.0029  -0.0544 -0.0175 220  VAL A CG2   
638  N N     . ILE A 38  ? 0.1732 0.2142 0.2548 -0.0663 -0.0324 -0.0351 221  ILE A N     
639  C CA    . ILE A 38  ? 0.1761 0.2779 0.2731 -0.1085 -0.0147 -0.0242 221  ILE A CA    
640  C C     . ILE A 38  ? 0.2026 0.2023 0.2300 -0.0510 -0.0698 0.0043  221  ILE A C     
641  O O     . ILE A 38  ? 0.1730 0.2073 0.2574 -0.0066 -0.0804 -0.0033 221  ILE A O     
642  C CB    . ILE A 38  ? 0.2384 0.3953 0.3320 -0.1570 -0.0265 -0.0540 221  ILE A CB    
643  C CG1   . ILE A 38  ? 0.3772 0.4084 0.3949 -0.1786 -0.0173 -0.0628 221  ILE A CG1   
644  C CG2   . ILE A 38  ? 0.2291 0.4540 0.3623 -0.1612 -0.0009 -0.0546 221  ILE A CG2   
645  C CD1   . ILE A 38  ? 0.4085 0.3952 0.4182 -0.2116 -0.0051 -0.0753 221  ILE A CD1   
657  N N     . PHE A 39  ? 0.1636 0.1518 0.2391 -0.0474 -0.0786 0.0125  222  PHE A N     
658  C CA    . PHE A 39  ? 0.0987 0.1101 0.2122 0.0011  -0.0704 0.0151  222  PHE A CA    
659  C C     . PHE A 39  ? 0.1055 0.1134 0.2511 0.0005  -0.0733 0.0200  222  PHE A C     
660  O O     . PHE A 39  ? 0.1413 0.1371 0.2706 0.0321  -0.0712 0.0209  222  PHE A O     
661  C CB    . PHE A 39  ? 0.1223 0.1082 0.1959 0.0186  -0.0442 0.0095  222  PHE A CB    
662  C CG    . PHE A 39  ? 0.1119 0.1099 0.2098 0.0250  -0.0723 0.0012  222  PHE A CG    
663  C CD1   . PHE A 39  ? 0.1300 0.1224 0.2631 0.0294  -0.0867 -0.0161 222  PHE A CD1   
664  C CD2   . PHE A 39  ? 0.1228 0.1023 0.2168 0.0316  -0.0740 -0.0077 222  PHE A CD2   
665  C CE1   . PHE A 39  ? 0.1108 0.1274 0.2615 0.0024  -0.0717 -0.0280 222  PHE A CE1   
666  C CE2   . PHE A 39  ? 0.1137 0.0981 0.2053 0.0351  -0.0631 -0.0125 222  PHE A CE2   
667  C CZ    . PHE A 39  ? 0.1135 0.1008 0.2287 0.0398  -0.0418 -0.0069 222  PHE A CZ    
677  N N     . GLY A 40  ? 0.1105 0.1094 0.2913 0.0020  -0.0769 0.0150  223  GLY A N     
678  C CA    . GLY A 40  ? 0.1056 0.1277 0.2754 0.0074  -0.0716 0.0183  223  GLY A CA    
679  C C     . GLY A 40  ? 0.1003 0.1246 0.2466 0.0088  -0.0603 0.0065  223  GLY A C     
680  O O     . GLY A 40  ? 0.1088 0.1083 0.2539 -0.0099 -0.0646 0.0139  223  GLY A O     
684  N N     . ASP A 41  ? 0.1087 0.1301 0.2479 0.0057  -0.0653 -0.0025 224  ASP A N     
685  C CA    . ASP A 41  ? 0.1353 0.1269 0.2541 -0.0155 -0.0594 0.0119  224  ASP A CA    
686  C C     . ASP A 41  ? 0.1169 0.1325 0.2389 -0.0114 -0.0535 0.0153  224  ASP A C     
687  O O     . ASP A 41  ? 0.1537 0.1251 0.2303 -0.0189 -0.0378 0.0020  224  ASP A O     
688  C CB    . ASP A 41  ? 0.1214 0.1221 0.2763 -0.0204 -0.0403 0.0204  224  ASP A CB    
689  C CG    . ASP A 41  ? 0.1351 0.1317 0.2622 -0.0279 -0.0424 0.0156  224  ASP A CG    
690  O OD1   . ASP A 41  ? 0.1551 0.1502 0.2398 -0.0062 -0.0167 0.0155  224  ASP A OD1   
691  O OD2   . ASP A 41  ? 0.1944 0.1147 0.3159 -0.0254 -0.0562 0.0204  224  ASP A OD2   
696  N N     . LYS A 42  ? 0.1376 0.1471 0.2655 -0.0101 -0.0454 0.0031  225  LYS A N     
697  C CA    . LYS A 42  ? 0.1615 0.1474 0.2862 0.0144  -0.0164 0.0122  225  LYS A CA    
698  C C     . LYS A 42  ? 0.1348 0.1304 0.2802 0.0220  -0.0235 0.0137  225  LYS A C     
699  O O     . LYS A 42  ? 0.1413 0.1294 0.2643 0.0134  -0.0121 -0.0035 225  LYS A O     
700  C CB    . LYS A 42  ? 0.1889 0.1798 0.3394 0.0555  0.0004  -0.0112 225  LYS A CB    
701  C CG    . LYS A 42  ? 0.2428 0.2305 0.3881 0.0783  0.0276  -0.0112 225  LYS A CG    
702  C CD    . LYS A 42  ? 0.3642 0.2656 0.4128 0.0823  0.0410  -0.0317 225  LYS A CD    
703  C CE    . LYS A 42  ? 0.4123 0.2860 0.4422 0.0971  0.0650  -0.0635 225  LYS A CE    
704  N NZ    . LYS A 42  ? 0.4398 0.3037 0.4682 0.1025  0.0904  -0.0747 225  LYS A NZ    
718  N N     . VAL A 43  ? 0.1124 0.1180 0.2885 0.0163  -0.0504 0.0007  226  VAL A N     
719  C CA    . VAL A 43  ? 0.0836 0.1288 0.2529 0.0100  -0.0429 0.0010  226  VAL A CA    
720  C C     . VAL A 43  ? 0.1171 0.1120 0.2210 0.0050  -0.0281 -0.0035 226  VAL A C     
721  O O     . VAL A 43  ? 0.1127 0.0980 0.2311 -0.0073 -0.0364 0.0010  226  VAL A O     
722  C CB    . VAL A 43  ? 0.1243 0.1697 0.2613 -0.0066 -0.0811 0.0234  226  VAL A CB    
723  C CG1   . VAL A 43  ? 0.1785 0.2009 0.2789 -0.0501 -0.0800 0.0205  226  VAL A CG1   
724  C CG2   . VAL A 43  ? 0.1532 0.1807 0.2756 0.0237  -0.0801 0.0221  226  VAL A CG2   
734  N N     . ILE A 44  ? 0.1010 0.1035 0.2292 0.0087  -0.0656 0.0010  227  ILE A N     
735  C CA    . ILE A 44  ? 0.1138 0.1097 0.1943 0.0062  -0.0457 0.0055  227  ILE A CA    
736  C C     . ILE A 44  ? 0.1134 0.1093 0.2139 0.0147  -0.0572 -0.0092 227  ILE A C     
737  O O     . ILE A 44  ? 0.1099 0.1053 0.2468 0.0016  -0.0607 -0.0205 227  ILE A O     
738  C CB    . ILE A 44  ? 0.0957 0.1104 0.2036 0.0140  -0.0428 -0.0011 227  ILE A CB    
739  C CG1   . ILE A 44  ? 0.1337 0.1156 0.2219 0.0168  -0.0706 -0.0061 227  ILE A CG1   
740  C CG2   . ILE A 44  ? 0.1120 0.1109 0.2231 0.0138  -0.0681 0.0033  227  ILE A CG2   
741  C CD1   . ILE A 44  ? 0.1325 0.1141 0.2336 0.0129  -0.0833 0.0002  227  ILE A CD1   
753  N N     . LEU A 45  ? 0.1287 0.1214 0.1991 0.0094  -0.0492 -0.0185 228  LEU A N     
754  C CA    . LEU A 45  ? 0.1635 0.1355 0.2238 0.0133  -0.0592 0.0001  228  LEU A CA    
755  C C     . LEU A 45  ? 0.1758 0.1340 0.2565 -0.0003 -0.0676 -0.0150 228  LEU A C     
756  O O     . LEU A 45  ? 0.2239 0.1467 0.2819 -0.0113 -0.0841 -0.0331 228  LEU A O     
757  C CB    . LEU A 45  ? 0.1583 0.1450 0.2276 0.0112  -0.0608 0.0023  228  LEU A CB    
758  C CG    . LEU A 45  ? 0.1868 0.1470 0.2515 0.0203  -0.0457 0.0175  228  LEU A CG    
759  C CD1   . LEU A 45  ? 0.2351 0.1505 0.2605 -0.0084 -0.0241 0.0235  228  LEU A CD1   
760  C CD2   . LEU A 45  ? 0.2069 0.1432 0.2777 0.0191  -0.0688 0.0186  228  LEU A CD2   
772  N N     . ASP A 46  ? 0.1962 0.1181 0.2786 0.0012  -0.0481 -0.0150 229  ASP A N     
773  C CA    . ASP A 46  ? 0.2377 0.1268 0.2859 -0.0012 -0.0111 -0.0133 229  ASP A CA    
774  C C     . ASP A 46  ? 0.2567 0.1062 0.2795 -0.0024 -0.0274 -0.0180 229  ASP A C     
775  O O     . ASP A 46  ? 0.4008 0.1079 0.2933 -0.0008 -0.0068 -0.0264 229  ASP A O     
776  C CB    . ASP A 46  ? 0.2376 0.1741 0.3613 0.0031  0.0680  0.0074  229  ASP A CB    
777  C CG    . ASP A 46  ? 0.3029 0.2382 0.4014 0.0262  0.1128  0.0209  229  ASP A CG    
778  O OD1   . ASP A 46  ? 0.4040 0.2561 0.3789 0.0432  0.0977  0.0186  229  ASP A OD1   
779  O OD2   . ASP A 46  ? 0.3570 0.2749 0.4571 0.0065  0.1322  0.0422  229  ASP A OD2   
784  N N     . GLU A 47  ? 0.1421 0.0974 0.2702 0.0084  -0.0404 -0.0158 230  GLU A N     
785  C CA    A GLU A 47  ? 0.1269 0.0981 0.2741 0.0073  -0.0510 -0.0087 230  GLU A CA    
786  C CA    B GLU A 47  ? 0.1061 0.0912 0.2407 0.0145  -0.0463 -0.0164 230  GLU A CA    
787  C C     . GLU A 47  ? 0.1171 0.0867 0.2372 0.0116  -0.0564 -0.0091 230  GLU A C     
788  O O     . GLU A 47  ? 0.1298 0.0985 0.2556 0.0195  -0.0677 -0.0053 230  GLU A O     
789  C CB    A GLU A 47  ? 0.1551 0.1322 0.3344 -0.0018 -0.0519 0.0046  230  GLU A CB    
790  C CB    B GLU A 47  ? 0.0816 0.1052 0.2318 0.0212  -0.0462 -0.0228 230  GLU A CB    
791  C CG    A GLU A 47  ? 0.1711 0.1795 0.4168 -0.0061 -0.0152 0.0211  230  GLU A CG    
792  C CG    B GLU A 47  ? 0.0761 0.1419 0.2464 0.0264  -0.0245 -0.0301 230  GLU A CG    
793  C CD    A GLU A 47  ? 0.1987 0.2094 0.4807 0.0470  0.0023  0.0491  230  GLU A CD    
794  C CD    B GLU A 47  ? 0.1438 0.2083 0.3360 0.0179  -0.0026 -0.0385 230  GLU A CD    
795  O OE1   A GLU A 47  ? 0.1607 0.2421 0.5854 0.0289  -0.0190 0.0183  230  GLU A OE1   
796  O OE1   B GLU A 47  ? 0.1744 0.2409 0.3714 -0.0007 0.0024  -0.0269 230  GLU A OE1   
797  O OE2   A GLU A 47  ? 0.2156 0.1932 0.4046 0.0809  0.0279  0.0902  230  GLU A OE2   
798  O OE2   B GLU A 47  ? 0.1967 0.2301 0.3694 0.0078  -0.0198 -0.0567 230  GLU A OE2   
811  N N     . ARG A 48  ? 0.1162 0.0864 0.2686 0.0019  -0.0632 -0.0139 231  ARG A N     
812  C CA    . ARG A 48  ? 0.1058 0.0991 0.2927 -0.0121 -0.0478 -0.0172 231  ARG A CA    
813  C C     . ARG A 48  ? 0.1045 0.0873 0.2257 0.0011  -0.0504 -0.0046 231  ARG A C     
814  O O     . ARG A 48  ? 0.1003 0.0837 0.2338 0.0029  -0.0723 0.0025  231  ARG A O     
815  C CB    . ARG A 48  ? 0.1536 0.1251 0.3399 -0.0249 -0.0118 -0.0715 231  ARG A CB    
816  C CG    . ARG A 48  ? 0.2392 0.1673 0.3558 -0.0347 0.0012  -0.0939 231  ARG A CG    
817  C CD    . ARG A 48  ? 0.2826 0.2065 0.3460 -0.0737 -0.0528 -0.0444 231  ARG A CD    
818  N NE    . ARG A 48  ? 0.2161 0.2076 0.3414 -0.0592 -0.1310 0.0034  231  ARG A NE    
819  C CZ    . ARG A 48  ? 0.1561 0.1809 0.3608 -0.0306 -0.0975 0.0152  231  ARG A CZ    
820  N NH1   . ARG A 48  ? 0.2051 0.1952 0.2812 -0.0397 -0.0660 -0.0279 231  ARG A NH1   
821  N NH2   . ARG A 48  ? 0.2076 0.1657 0.4824 -0.0194 -0.0162 0.0245  231  ARG A NH2   
835  N N     . ILE A 49  ? 0.1048 0.0971 0.2024 -0.0080 -0.0719 -0.0165 232  ILE A N     
836  C CA    . ILE A 49  ? 0.0960 0.0998 0.1901 -0.0108 -0.0667 -0.0109 232  ILE A CA    
837  C C     . ILE A 49  ? 0.0991 0.0853 0.1749 0.0017  -0.0419 -0.0155 232  ILE A C     
838  O O     . ILE A 49  ? 0.1117 0.0779 0.2052 0.0040  -0.0711 -0.0080 232  ILE A O     
839  C CB    . ILE A 49  ? 0.0817 0.1211 0.2108 0.0033  -0.0587 0.0032  232  ILE A CB    
840  C CG1   . ILE A 49  ? 0.1171 0.1446 0.2576 -0.0141 -0.0832 -0.0008 232  ILE A CG1   
841  C CG2   . ILE A 49  ? 0.1128 0.1214 0.2333 0.0065  -0.0698 0.0039  232  ILE A CG2   
842  C CD1   . ILE A 49  ? 0.1858 0.1538 0.3195 -0.0450 -0.0337 -0.0062 232  ILE A CD1   
854  N N     . GLU A 50  ? 0.1121 0.0796 0.1954 0.0046  -0.0516 -0.0133 233  GLU A N     
855  C CA    . GLU A 50  ? 0.1183 0.0777 0.2451 -0.0089 -0.0782 0.0009  233  GLU A CA    
856  C C     . GLU A 50  ? 0.1241 0.0701 0.2440 0.0075  -0.0579 0.0055  233  GLU A C     
857  O O     . GLU A 50  ? 0.1374 0.0817 0.2739 -0.0076 -0.0826 -0.0026 233  GLU A O     
858  C CB    . GLU A 50  ? 0.1191 0.0939 0.2789 -0.0161 -0.0694 -0.0054 233  GLU A CB    
859  C CG    . GLU A 50  ? 0.1064 0.1176 0.2712 -0.0093 -0.0624 0.0021  233  GLU A CG    
860  C CD    . GLU A 50  ? 0.1258 0.1474 0.2796 -0.0392 -0.0732 0.0021  233  GLU A CD    
861  O OE1   . GLU A 50  ? 0.1596 0.1231 0.2899 -0.0430 -0.0628 -0.0243 233  GLU A OE1   
862  O OE2   . GLU A 50  ? 0.1820 0.2145 0.3262 -0.0810 -0.0940 0.0293  233  GLU A OE2   
869  N N     . ASN A 51  ? 0.0996 0.0727 0.2205 0.0109  -0.0599 0.0054  234  ASN A N     
870  C CA    . ASN A 51  ? 0.1136 0.0786 0.2408 -0.0088 -0.0773 0.0064  234  ASN A CA    
871  C C     . ASN A 51  ? 0.1095 0.0777 0.2170 -0.0036 -0.0794 -0.0047 234  ASN A C     
872  O O     . ASN A 51  ? 0.1161 0.0811 0.2322 0.0033  -0.0865 -0.0060 234  ASN A O     
873  C CB    . ASN A 51  ? 0.1237 0.0887 0.2881 -0.0090 -0.0779 -0.0056 234  ASN A CB    
874  C CG    . ASN A 51  ? 0.1505 0.0917 0.3231 0.0078  -0.0780 -0.0030 234  ASN A CG    
875  O OD1   . ASN A 51  ? 0.2103 0.0894 0.3417 0.0146  -0.0283 0.0077  234  ASN A OD1   
876  N ND2   . ASN A 51  ? 0.1707 0.0872 0.3078 -0.0007 -0.0800 -0.0089 234  ASN A ND2   
883  N N     . TRP A 52  ? 0.1115 0.0708 0.1988 0.0067  -0.0815 -0.0084 235  TRP A N     
884  C CA    . TRP A 52  ? 0.0943 0.0666 0.2001 0.0066  -0.0693 -0.0075 235  TRP A CA    
885  C C     . TRP A 52  ? 0.0805 0.0732 0.1988 0.0039  -0.0572 0.0041  235  TRP A C     
886  O O     . TRP A 52  ? 0.0938 0.0837 0.1904 -0.0016 -0.0699 0.0018  235  TRP A O     
887  C CB    . TRP A 52  ? 0.0944 0.0628 0.2020 0.0076  -0.0700 -0.0159 235  TRP A CB    
888  C CG    . TRP A 52  ? 0.1008 0.0658 0.1891 0.0046  -0.0624 -0.0081 235  TRP A CG    
889  C CD1   . TRP A 52  ? 0.0941 0.0753 0.1991 0.0033  -0.0572 -0.0108 235  TRP A CD1   
890  C CD2   . TRP A 52  ? 0.0939 0.0636 0.2047 -0.0002 -0.0699 -0.0015 235  TRP A CD2   
891  N NE1   . TRP A 52  ? 0.0979 0.0746 0.2196 0.0128  -0.0602 0.0017  235  TRP A NE1   
892  C CE2   . TRP A 52  ? 0.1008 0.0717 0.2118 0.0022  -0.0729 0.0062  235  TRP A CE2   
893  C CE3   . TRP A 52  ? 0.0991 0.0751 0.2066 -0.0020 -0.0731 -0.0038 235  TRP A CE3   
894  C CZ2   . TRP A 52  ? 0.0907 0.0885 0.2114 -0.0025 -0.0670 0.0050  235  TRP A CZ2   
895  C CZ3   . TRP A 52  ? 0.0878 0.0801 0.2175 -0.0075 -0.0553 0.0010  235  TRP A CZ3   
896  C CH2   . TRP A 52  ? 0.0981 0.0874 0.2269 0.0024  -0.0705 0.0113  235  TRP A CH2   
907  N N     . PRO A 53  ? 0.0955 0.0732 0.1984 0.0088  -0.0626 0.0086  236  PRO A N     
908  C CA    . PRO A 53  ? 0.0909 0.0765 0.2034 0.0103  -0.0559 0.0127  236  PRO A CA    
909  C C     . PRO A 53  ? 0.0890 0.0717 0.2007 0.0161  -0.0479 0.0040  236  PRO A C     
910  O O     . PRO A 53  ? 0.1096 0.0778 0.1856 0.0213  -0.0668 -0.0033 236  PRO A O     
911  C CB    . PRO A 53  ? 0.1039 0.0732 0.2478 -0.0045 -0.0766 0.0092  236  PRO A CB    
912  C CG    . PRO A 53  ? 0.1040 0.0820 0.2443 -0.0145 -0.0681 0.0097  236  PRO A CG    
913  C CD    . PRO A 53  ? 0.1097 0.0746 0.2152 -0.0127 -0.0803 0.0191  236  PRO A CD    
921  N N     . THR A 54  ? 0.0940 0.0808 0.1760 0.0211  -0.0576 -0.0001 237  THR A N     
922  C CA    . THR A 54  ? 0.1108 0.0878 0.1781 0.0207  -0.0678 0.0060  237  THR A CA    
923  C C     . THR A 54  ? 0.1090 0.0870 0.1937 0.0158  -0.0749 -0.0032 237  THR A C     
924  O O     . THR A 54  ? 0.1065 0.0909 0.2044 0.0100  -0.0737 0.0088  237  THR A O     
925  C CB    . THR A 54  ? 0.1126 0.0905 0.2151 0.0098  -0.0794 0.0043  237  THR A CB    
926  O OG1   . THR A 54  ? 0.1000 0.0953 0.2072 0.0119  -0.0662 0.0146  237  THR A OG1   
927  C CG2   . THR A 54  ? 0.1407 0.0987 0.2461 0.0003  -0.1026 0.0059  237  THR A CG2   
935  N N     . CYS A 55  ? 0.1119 0.0743 0.2036 0.0219  -0.0682 -0.0160 238  CYS A N     
936  C CA    . CYS A 55  ? 0.1400 0.0742 0.2223 0.0125  -0.0769 -0.0112 238  CYS A CA    
937  C C     . CYS A 55  ? 0.1288 0.0816 0.2386 0.0165  -0.0774 -0.0001 238  CYS A C     
938  O O     . CYS A 55  ? 0.1330 0.0986 0.2621 0.0122  -0.0667 -0.0080 238  CYS A O     
939  C CB    . CYS A 55  ? 0.1289 0.0914 0.2132 0.0189  -0.0560 -0.0054 238  CYS A CB    
940  S SG    . CYS A 55  ? 0.1522 0.1182 0.2387 0.0356  -0.0803 0.0155  238  CYS A SG    
946  N N     . ASP A 56  ? 0.1114 0.0854 0.2353 0.0196  -0.0612 0.0035  239  ASP A N     
947  C CA    . ASP A 56  ? 0.1252 0.0957 0.2327 0.0309  -0.0531 0.0079  239  ASP A CA    
948  C C     . ASP A 56  ? 0.1145 0.0843 0.2203 0.0107  -0.0498 0.0013  239  ASP A C     
949  O O     . ASP A 56  ? 0.1142 0.1072 0.2287 0.0159  -0.0479 0.0041  239  ASP A O     
950  C CB    . ASP A 56  ? 0.1516 0.1027 0.2217 0.0292  -0.0667 -0.0022 239  ASP A CB    
951  C CG    . ASP A 56  ? 0.1538 0.1058 0.2310 -0.0053 -0.0667 -0.0047 239  ASP A CG    
952  O OD1   . ASP A 56  ? 0.1407 0.1032 0.2568 0.0178  -0.0643 0.0128  239  ASP A OD1   
953  O OD2   . ASP A 56  ? 0.1763 0.1034 0.2523 -0.0069 -0.0773 0.0238  239  ASP A OD2   
958  N N     . PHE A 57  ? 0.1180 0.0778 0.2151 0.0201  -0.0515 0.0173  240  PHE A N     
959  C CA    . PHE A 57  ? 0.1180 0.0871 0.1935 0.0364  -0.0524 -0.0007 240  PHE A CA    
960  C C     . PHE A 57  ? 0.0957 0.1003 0.1920 0.0395  -0.0406 -0.0042 240  PHE A C     
961  O O     . PHE A 57  ? 0.1067 0.1321 0.2117 0.0385  -0.0523 -0.0028 240  PHE A O     
962  C CB    . PHE A 57  ? 0.1650 0.0951 0.1767 0.0308  -0.0268 -0.0145 240  PHE A CB    
963  C CG    . PHE A 57  ? 0.1932 0.0856 0.1831 0.0187  -0.0315 -0.0164 240  PHE A CG    
964  C CD1   . PHE A 57  ? 0.1973 0.0948 0.2382 0.0418  -0.0801 -0.0139 240  PHE A CD1   
965  C CD2   . PHE A 57  ? 0.1631 0.0798 0.2038 0.0103  -0.0403 -0.0066 240  PHE A CD2   
966  C CE1   . PHE A 57  ? 0.1972 0.1089 0.2805 0.0242  -0.0986 -0.0113 240  PHE A CE1   
967  C CE2   . PHE A 57  ? 0.1795 0.0906 0.2175 0.0179  -0.0618 -0.0171 240  PHE A CE2   
968  C CZ    . PHE A 57  ? 0.1943 0.1009 0.2206 0.0196  -0.0833 -0.0010 240  PHE A CZ    
978  N N     . LEU A 58  ? 0.0880 0.0943 0.2118 0.0157  -0.0512 0.0085  241  LEU A N     
979  C CA    . LEU A 58  ? 0.0772 0.0881 0.2025 0.0044  -0.0514 0.0162  241  LEU A CA    
980  C C     . LEU A 58  ? 0.0905 0.0840 0.2170 0.0001  -0.0644 0.0159  241  LEU A C     
981  O O     . LEU A 58  ? 0.1107 0.0984 0.2372 0.0142  -0.0577 0.0332  241  LEU A O     
982  C CB    . LEU A 58  ? 0.1024 0.0979 0.2338 -0.0083 -0.0591 0.0313  241  LEU A CB    
983  C CG    . LEU A 58  ? 0.1029 0.1098 0.2299 -0.0207 -0.0651 0.0376  241  LEU A CG    
984  C CD1   . LEU A 58  ? 0.1109 0.1354 0.2767 -0.0212 -0.0770 0.0231  241  LEU A CD1   
985  C CD2   . LEU A 58  ? 0.1227 0.1040 0.2418 -0.0288 -0.0699 0.0116  241  LEU A CD2   
997  N N     . ILE A 59  ? 0.1032 0.0745 0.2071 0.0027  -0.0764 0.0007  242  ILE A N     
998  C CA    . ILE A 59  ? 0.0911 0.0886 0.2109 0.0003  -0.0611 0.0068  242  ILE A CA    
999  C C     . ILE A 59  ? 0.1047 0.0810 0.2014 0.0108  -0.0717 0.0041  242  ILE A C     
1000 O O     . ILE A 59  ? 0.1094 0.0984 0.2203 0.0080  -0.0812 -0.0095 242  ILE A O     
1001 C CB    . ILE A 59  ? 0.1159 0.1031 0.2063 -0.0118 -0.0581 0.0174  242  ILE A CB    
1002 C CG1   . ILE A 59  ? 0.1468 0.1127 0.2126 -0.0039 -0.0908 -0.0077 242  ILE A CG1   
1003 C CG2   . ILE A 59  ? 0.1775 0.1188 0.1873 -0.0310 -0.0792 0.0145  242  ILE A CG2   
1004 C CD1   . ILE A 59  ? 0.1799 0.1138 0.2416 0.0075  -0.0991 -0.0036 242  ILE A CD1   
1016 N N     . SER A 60  ? 0.0907 0.0814 0.2044 0.0202  -0.0467 -0.0029 243  SER A N     
1017 C CA    . SER A 60  ? 0.0870 0.0838 0.1919 0.0130  -0.0497 0.0018  243  SER A CA    
1018 C C     . SER A 60  ? 0.0704 0.0970 0.1330 -0.0019 -0.0251 -0.0112 243  SER A C     
1019 O O     . SER A 60  ? 0.0907 0.1188 0.2178 0.0127  -0.0538 -0.0015 243  SER A O     
1020 C CB    . SER A 60  ? 0.1128 0.0862 0.1835 -0.0007 -0.0341 0.0031  243  SER A CB    
1021 O OG    . SER A 60  ? 0.1011 0.1016 0.2064 0.0050  -0.0599 -0.0053 243  SER A OG    
1027 N N     . PHE A 61  ? 0.0555 0.0912 0.1362 0.0130  -0.0365 0.0045  244  PHE A N     
1028 C CA    . PHE A 61  ? 0.0824 0.0867 0.1871 0.0017  -0.0610 0.0031  244  PHE A CA    
1029 C C     . PHE A 61  ? 0.1145 0.0916 0.2115 0.0156  -0.0779 0.0007  244  PHE A C     
1030 O O     . PHE A 61  ? 0.1046 0.0919 0.2126 0.0140  -0.0729 -0.0050 244  PHE A O     
1031 C CB    . PHE A 61  ? 0.0910 0.0883 0.1937 0.0104  -0.0643 -0.0009 244  PHE A CB    
1032 C CG    . PHE A 61  ? 0.1094 0.0922 0.1903 -0.0004 -0.0507 -0.0023 244  PHE A CG    
1033 C CD1   . PHE A 61  ? 0.1093 0.0992 0.2358 -0.0095 -0.0734 0.0057  244  PHE A CD1   
1034 C CD2   . PHE A 61  ? 0.1145 0.1054 0.2276 0.0041  -0.0575 -0.0024 244  PHE A CD2   
1035 C CE1   . PHE A 61  ? 0.1393 0.1131 0.2528 -0.0138 -0.0783 0.0059  244  PHE A CE1   
1036 C CE2   . PHE A 61  ? 0.1312 0.1188 0.2653 -0.0202 -0.0607 0.0193  244  PHE A CE2   
1037 C CZ    . PHE A 61  ? 0.1367 0.1260 0.2655 -0.0232 -0.0828 0.0081  244  PHE A CZ    
1047 N N     . PHE A 62  ? 0.1282 0.1179 0.2124 0.0363  -0.0757 -0.0016 245  PHE A N     
1048 C CA    . PHE A 62  ? 0.1318 0.1265 0.2144 0.0205  -0.0883 0.0071  245  PHE A CA    
1049 C C     . PHE A 62  ? 0.1746 0.1153 0.2227 0.0233  -0.0749 0.0168  245  PHE A C     
1050 O O     . PHE A 62  ? 0.2627 0.1034 0.2457 0.0385  -0.0839 0.0159  245  PHE A O     
1051 C CB    . PHE A 62  ? 0.1505 0.1474 0.2457 0.0300  -0.0864 0.0108  245  PHE A CB    
1052 C CG    . PHE A 62  ? 0.1462 0.1426 0.2269 0.0328  -0.0926 0.0047  245  PHE A CG    
1053 C CD1   . PHE A 62  ? 0.1362 0.1442 0.2235 0.0223  -0.0939 0.0003  245  PHE A CD1   
1054 C CD2   . PHE A 62  ? 0.2244 0.1405 0.2385 0.0389  -0.1140 0.0048  245  PHE A CD2   
1055 C CE1   . PHE A 62  ? 0.2117 0.1578 0.2481 0.0322  -0.1217 -0.0020 245  PHE A CE1   
1056 C CE2   . PHE A 62  ? 0.2674 0.1538 0.2379 0.0266  -0.1081 0.0130  245  PHE A CE2   
1057 C CZ    . PHE A 62  ? 0.2455 0.1711 0.2542 0.0163  -0.1172 0.0001  245  PHE A CZ    
1067 N N     . SER A 63  ? 0.1553 0.1141 0.2444 0.0053  -0.0868 0.0254  246  SER A N     
1068 C CA    . SER A 63  ? 0.1763 0.1303 0.2403 -0.0184 -0.0726 0.0383  246  SER A CA    
1069 C C     . SER A 63  ? 0.1853 0.1369 0.2329 -0.0196 -0.0606 0.0257  246  SER A C     
1070 O O     . SER A 63  ? 0.1690 0.1168 0.2691 -0.0083 -0.0695 0.0198  246  SER A O     
1071 C CB    . SER A 63  ? 0.2146 0.1443 0.2589 -0.0458 -0.0466 0.0368  246  SER A CB    
1072 O OG    . SER A 63  ? 0.1900 0.1628 0.2851 -0.0540 -0.0812 0.0629  246  SER A OG    
1078 N N     . SER A 64  ? 0.2493 0.1573 0.2258 -0.0143 -0.0213 0.0259  247  SER A N     
1079 C CA    . SER A 64  ? 0.2654 0.1868 0.2454 0.0010  -0.0008 0.0326  247  SER A CA    
1080 C C     . SER A 64  ? 0.1910 0.1873 0.2446 -0.0003 -0.0382 0.0311  247  SER A C     
1081 O O     . SER A 64  ? 0.1923 0.1896 0.2707 -0.0132 -0.0359 0.0248  247  SER A O     
1082 C CB    . SER A 64  ? 0.3764 0.2330 0.3012 -0.0020 0.0148  0.0394  247  SER A CB    
1083 O OG    . SER A 64  ? 0.4925 0.2734 0.3753 0.0036  0.0124  0.0721  247  SER A OG    
1089 N N     . GLY A 65  ? 0.2020 0.1820 0.2444 0.0077  -0.0344 0.0323  248  GLY A N     
1090 C CA    . GLY A 65  ? 0.1720 0.1809 0.2722 0.0118  -0.0196 0.0150  248  GLY A CA    
1091 C C     . GLY A 65  ? 0.1438 0.1562 0.2463 -0.0107 -0.0463 0.0048  248  GLY A C     
1092 O O     . GLY A 65  ? 0.1707 0.1494 0.2433 0.0195  -0.0360 0.0083  248  GLY A O     
1096 N N     . PHE A 66  ? 0.1397 0.1386 0.2005 -0.0173 -0.0653 -0.0009 249  PHE A N     
1097 C CA    . PHE A 66  ? 0.1066 0.1301 0.1860 -0.0079 -0.0575 0.0023  249  PHE A CA    
1098 C C     . PHE A 66  ? 0.1122 0.1142 0.2134 0.0102  -0.0742 -0.0012 249  PHE A C     
1099 O O     . PHE A 66  ? 0.1300 0.1095 0.2233 -0.0020 -0.0851 -0.0093 249  PHE A O     
1100 C CB    . PHE A 66  ? 0.0920 0.1297 0.1998 -0.0160 -0.0638 -0.0093 249  PHE A CB    
1101 C CG    . PHE A 66  ? 0.0818 0.1075 0.1908 -0.0110 -0.0542 -0.0172 249  PHE A CG    
1102 C CD1   . PHE A 66  ? 0.0834 0.1215 0.1639 -0.0230 -0.0246 -0.0179 249  PHE A CD1   
1103 C CD2   . PHE A 66  ? 0.0874 0.0971 0.1944 -0.0127 -0.0487 0.0032  249  PHE A CD2   
1104 C CE1   . PHE A 66  ? 0.0840 0.1061 0.1511 -0.0131 -0.0234 -0.0051 249  PHE A CE1   
1105 C CE2   . PHE A 66  ? 0.0851 0.0925 0.2037 -0.0073 -0.0497 -0.0088 249  PHE A CE2   
1106 C CZ    . PHE A 66  ? 0.0764 0.0975 0.2149 -0.0088 -0.0434 -0.0176 249  PHE A CZ    
1116 N N     . PRO A 67  ? 0.1029 0.1104 0.2018 0.0078  -0.0743 -0.0068 250  PRO A N     
1117 C CA    . PRO A 67  ? 0.1003 0.1082 0.2285 -0.0014 -0.0687 -0.0040 250  PRO A CA    
1118 C C     . PRO A 67  ? 0.1093 0.1043 0.2199 -0.0050 -0.0813 0.0106  250  PRO A C     
1119 O O     . PRO A 67  ? 0.1080 0.1010 0.2433 -0.0021 -0.0768 0.0072  250  PRO A O     
1120 C CB    . PRO A 67  ? 0.0980 0.1084 0.2486 0.0079  -0.0460 -0.0097 250  PRO A CB    
1121 C CG    . PRO A 67  ? 0.0992 0.1070 0.2435 0.0047  -0.0519 -0.0029 250  PRO A CG    
1122 C CD    . PRO A 67  ? 0.0903 0.1087 0.2104 0.0073  -0.0656 0.0031  250  PRO A CD    
1130 N N     . LEU A 68  ? 0.1189 0.1109 0.2141 -0.0022 -0.0875 0.0063  251  LEU A N     
1131 C CA    . LEU A 68  ? 0.1007 0.1083 0.2321 -0.0066 -0.0648 0.0084  251  LEU A CA    
1132 C C     . LEU A 68  ? 0.0930 0.1038 0.2118 0.0109  -0.0674 -0.0042 251  LEU A C     
1133 O O     . LEU A 68  ? 0.1017 0.0988 0.2202 0.0087  -0.0750 -0.0065 251  LEU A O     
1134 C CB    . LEU A 68  ? 0.1159 0.1058 0.2399 -0.0024 -0.0831 0.0056  251  LEU A CB    
1135 C CG    . LEU A 68  ? 0.1229 0.1121 0.2625 0.0117  -0.0879 0.0030  251  LEU A CG    
1136 C CD1   . LEU A 68  ? 0.1320 0.1124 0.2929 0.0070  -0.0981 -0.0077 251  LEU A CD1   
1137 C CD2   . LEU A 68  ? 0.1517 0.1378 0.3055 0.0173  -0.0945 0.0323  251  LEU A CD2   
1149 N N     . ASP A 69  ? 0.1177 0.1109 0.2188 -0.0067 -0.0860 -0.0027 252  ASP A N     
1150 C CA    . ASP A 69  ? 0.1332 0.1189 0.2412 -0.0184 -0.0870 -0.0155 252  ASP A CA    
1151 C C     . ASP A 69  ? 0.1126 0.1123 0.2381 -0.0196 -0.0514 -0.0178 252  ASP A C     
1152 O O     . ASP A 69  ? 0.1324 0.1165 0.2431 -0.0110 -0.0583 -0.0242 252  ASP A O     
1153 C CB    . ASP A 69  ? 0.1664 0.1521 0.2607 -0.0210 -0.0947 -0.0277 252  ASP A CB    
1154 C CG    . ASP A 69  ? 0.2210 0.1883 0.3125 -0.0291 -0.1245 -0.0512 252  ASP A CG    
1155 O OD1   . ASP A 69  ? 0.2505 0.1910 0.3460 0.0155  -0.1649 -0.0540 252  ASP A OD1   
1156 O OD2   . ASP A 69  ? 0.3179 0.2117 0.3296 -0.0155 -0.1592 -0.0626 252  ASP A OD2   
1161 N N     . LYS A 70  ? 0.1190 0.1089 0.2680 -0.0105 -0.0437 -0.0160 253  LYS A N     
1162 C CA    . LYS A 70  ? 0.1085 0.1031 0.2708 -0.0084 -0.0565 0.0093  253  LYS A CA    
1163 C C     . LYS A 70  ? 0.0897 0.0971 0.2532 -0.0055 -0.0608 0.0228  253  LYS A C     
1164 O O     . LYS A 70  ? 0.1027 0.1008 0.2635 -0.0030 -0.0571 0.0313  253  LYS A O     
1165 C CB    . LYS A 70  ? 0.1389 0.1157 0.3147 -0.0129 -0.0483 0.0223  253  LYS A CB    
1166 C CG    . LYS A 70  ? 0.1173 0.1059 0.3066 0.0133  -0.0508 -0.0056 253  LYS A CG    
1167 C CD    . LYS A 70  ? 0.1124 0.1076 0.3100 0.0041  -0.0779 -0.0206 253  LYS A CD    
1168 C CE    . LYS A 70  ? 0.0909 0.0900 0.2690 0.0004  -0.0567 -0.0222 253  LYS A CE    
1169 N NZ    . LYS A 70  ? 0.0966 0.0894 0.2678 0.0129  -0.0605 -0.0110 253  LYS A NZ    
1183 N N     . ALA A 71  ? 0.0980 0.0824 0.2533 0.0036  -0.0594 0.0199  254  ALA A N     
1184 C CA    . ALA A 71  ? 0.0988 0.0779 0.2434 0.0088  -0.0577 0.0108  254  ALA A CA    
1185 C C     . ALA A 71  ? 0.0885 0.0630 0.2145 -0.0067 -0.0647 0.0161  254  ALA A C     
1186 O O     . ALA A 71  ? 0.0862 0.0687 0.2223 -0.0039 -0.0608 0.0163  254  ALA A O     
1187 C CB    . ALA A 71  ? 0.1105 0.0831 0.2530 -0.0069 -0.0817 0.0169  254  ALA A CB    
1193 N N     . ILE A 72  ? 0.0948 0.0751 0.2210 -0.0059 -0.0680 0.0008  255  ILE A N     
1194 C CA    . ILE A 72  ? 0.0867 0.0875 0.1937 -0.0004 -0.0646 0.0018  255  ILE A CA    
1195 C C     . ILE A 72  ? 0.0746 0.1037 0.1862 -0.0044 -0.0538 -0.0036 255  ILE A C     
1196 O O     . ILE A 72  ? 0.0820 0.1021 0.2014 0.0031  -0.0601 -0.0043 255  ILE A O     
1197 C CB    . ILE A 72  ? 0.0817 0.0846 0.2204 0.0056  -0.0564 0.0007  255  ILE A CB    
1198 C CG1   . ILE A 72  ? 0.1058 0.0852 0.2070 0.0039  -0.0784 -0.0017 255  ILE A CG1   
1199 C CG2   . ILE A 72  ? 0.0939 0.1035 0.2309 0.0079  -0.0674 0.0002  255  ILE A CG2   
1200 C CD1   . ILE A 72  ? 0.1057 0.1058 0.2186 0.0170  -0.0736 -0.0013 255  ILE A CD1   
1212 N N     . LYS A 73  ? 0.1025 0.1014 0.2230 -0.0052 -0.0763 0.0096  256  LYS A N     
1213 C CA    . LYS A 73  ? 0.1114 0.1081 0.2529 -0.0072 -0.0826 0.0097  256  LYS A CA    
1214 C C     . LYS A 73  ? 0.0845 0.0951 0.2368 -0.0101 -0.0570 0.0149  256  LYS A C     
1215 O O     . LYS A 73  ? 0.0834 0.0975 0.2412 -0.0102 -0.0543 0.0098  256  LYS A O     
1216 C CB    . LYS A 73  ? 0.1339 0.1385 0.2771 -0.0023 -0.1000 0.0010  256  LYS A CB    
1217 C CG    . LYS A 73  ? 0.2265 0.1856 0.3073 -0.0164 -0.1129 -0.0136 256  LYS A CG    
1218 C CD    . LYS A 73  ? 0.3399 0.2378 0.3112 -0.0315 -0.1118 -0.0494 256  LYS A CD    
1219 C CE    . LYS A 73  ? 0.4206 0.2686 0.3207 -0.0156 -0.0966 -0.0841 256  LYS A CE    
1220 N NZ    . LYS A 73  ? 0.4450 0.2769 0.3697 -0.0203 -0.0257 -0.1034 256  LYS A NZ    
1234 N N     . TYR A 74  ? 0.0900 0.0888 0.2070 -0.0122 -0.0654 0.0165  257  TYR A N     
1235 C CA    . TYR A 74  ? 0.0891 0.0886 0.2242 -0.0090 -0.0641 0.0164  257  TYR A CA    
1236 C C     . TYR A 74  ? 0.0854 0.0922 0.1954 -0.0184 -0.0582 0.0125  257  TYR A C     
1237 O O     . TYR A 74  ? 0.0906 0.0965 0.2046 -0.0100 -0.0663 0.0086  257  TYR A O     
1238 C CB    . TYR A 74  ? 0.0827 0.0806 0.2218 -0.0078 -0.0577 0.0119  257  TYR A CB    
1239 C CG    . TYR A 74  ? 0.0905 0.0672 0.2287 -0.0036 -0.0658 0.0084  257  TYR A CG    
1240 C CD1   . TYR A 74  ? 0.0881 0.0761 0.2221 -0.0035 -0.0619 0.0200  257  TYR A CD1   
1241 C CD2   . TYR A 74  ? 0.1072 0.0754 0.2515 -0.0028 -0.0791 0.0088  257  TYR A CD2   
1242 C CE1   . TYR A 74  ? 0.1042 0.0785 0.2301 0.0019  -0.0763 0.0055  257  TYR A CE1   
1243 C CE2   . TYR A 74  ? 0.1032 0.0868 0.2192 0.0085  -0.0732 0.0039  257  TYR A CE2   
1244 C CZ    . TYR A 74  ? 0.0997 0.0838 0.2265 0.0117  -0.0700 -0.0057 257  TYR A CZ    
1245 O OH    . TYR A 74  ? 0.1160 0.0945 0.2250 0.0131  -0.0817 -0.0006 257  TYR A OH    
1255 N N     . VAL A 75  ? 0.0931 0.0840 0.2264 -0.0032 -0.0684 0.0089  258  VAL A N     
1256 C CA    . VAL A 75  ? 0.0964 0.1047 0.2259 0.0135  -0.0646 0.0092  258  VAL A CA    
1257 C C     . VAL A 75  ? 0.0858 0.1089 0.2379 0.0154  -0.0503 0.0108  258  VAL A C     
1258 O O     . VAL A 75  ? 0.1179 0.1053 0.2592 0.0054  -0.0365 0.0045  258  VAL A O     
1259 C CB    . VAL A 75  ? 0.0971 0.1177 0.2456 0.0114  -0.0681 -0.0005 258  VAL A CB    
1260 C CG1   . VAL A 75  ? 0.1408 0.1252 0.2797 0.0174  -0.0817 0.0041  258  VAL A CG1   
1261 C CG2   . VAL A 75  ? 0.0943 0.1162 0.2519 -0.0042 -0.0664 0.0003  258  VAL A CG2   
1271 N N     . LYS A 76  ? 0.0916 0.1119 0.2572 0.0002  -0.0628 0.0122  259  LYS A N     
1272 C CA    . LYS A 76  ? 0.1060 0.1420 0.2961 -0.0077 -0.0730 0.0204  259  LYS A CA    
1273 C C     . LYS A 76  ? 0.1140 0.1231 0.2813 -0.0193 -0.0693 0.0018  259  LYS A C     
1274 O O     . LYS A 76  ? 0.1298 0.1292 0.3204 0.0001  -0.0494 0.0081  259  LYS A O     
1275 C CB    . LYS A 76  ? 0.1250 0.1924 0.3190 -0.0404 -0.0779 0.0379  259  LYS A CB    
1276 C CG    . LYS A 76  ? 0.1707 0.2627 0.3952 -0.0697 -0.0986 0.0282  259  LYS A CG    
1277 C CD    . LYS A 76  ? 0.2181 0.3254 0.4700 -0.0887 -0.0997 0.0350  259  LYS A CD    
1278 C CE    . LYS A 76  ? 0.3526 0.3697 0.5167 -0.0554 -0.0831 0.0601  259  LYS A CE    
1279 N NZ    . LYS A 76  ? 0.4312 0.4015 0.5590 -0.0254 -0.0678 0.0709  259  LYS A NZ    
1293 N N     . LEU A 77  ? 0.0905 0.1176 0.2243 -0.0260 -0.0547 0.0056  260  LEU A N     
1294 C CA    . LEU A 77  ? 0.0977 0.1118 0.2278 -0.0123 -0.0515 0.0130  260  LEU A CA    
1295 C C     . LEU A 77  ? 0.1031 0.1153 0.2125 -0.0244 -0.0382 0.0210  260  LEU A C     
1296 O O     . LEU A 77  ? 0.1457 0.1236 0.2444 -0.0366 -0.0516 0.0217  260  LEU A O     
1297 C CB    . LEU A 77  ? 0.1226 0.1158 0.2571 0.0023  -0.0667 -0.0043 260  LEU A CB    
1298 C CG    . LEU A 77  ? 0.1672 0.1267 0.2965 0.0013  -0.0841 -0.0084 260  LEU A CG    
1299 C CD1   . LEU A 77  ? 0.2128 0.1229 0.3240 -0.0122 -0.0568 0.0202  260  LEU A CD1   
1300 C CD2   . LEU A 77  ? 0.1895 0.1418 0.2957 0.0269  -0.1104 -0.0374 260  LEU A CD2   
1312 N N     . ARG A 78  ? 0.1032 0.0994 0.2226 -0.0166 -0.0534 0.0090  261  ARG A N     
1313 C CA    . ARG A 78  ? 0.1251 0.0919 0.2255 -0.0033 -0.0555 0.0089  261  ARG A CA    
1314 C C     . ARG A 78  ? 0.1314 0.0981 0.2232 -0.0055 -0.0362 -0.0073 261  ARG A C     
1315 O O     . ARG A 78  ? 0.1941 0.0886 0.2322 0.0075  -0.0340 0.0069  261  ARG A O     
1316 C CB    . ARG A 78  ? 0.1169 0.0954 0.2474 -0.0024 -0.0856 0.0144  261  ARG A CB    
1317 C CG    . ARG A 78  ? 0.1049 0.1018 0.2356 0.0166  -0.0662 0.0116  261  ARG A CG    
1318 C CD    . ARG A 78  ? 0.1142 0.1013 0.2626 0.0119  -0.0721 -0.0051 261  ARG A CD    
1319 N NE    . ARG A 78  ? 0.0959 0.1025 0.2424 0.0079  -0.0547 0.0138  261  ARG A NE    
1320 C CZ    . ARG A 78  ? 0.1184 0.1026 0.2422 0.0092  -0.0757 0.0015  261  ARG A CZ    
1321 N NH1   . ARG A 78  ? 0.1218 0.0964 0.2852 0.0084  -0.0366 0.0068  261  ARG A NH1   
1322 N NH2   . ARG A 78  ? 0.1271 0.1094 0.2490 0.0040  -0.0670 0.0045  261  ARG A NH2   
1336 N N     . LYS A 79  ? 0.1244 0.1133 0.2248 0.0037  -0.0523 -0.0085 262  LYS A N     
1337 C CA    . LYS A 79  ? 0.1172 0.1326 0.2671 0.0056  -0.0282 -0.0017 262  LYS A CA    
1338 C C     . LYS A 79  ? 0.1427 0.1056 0.2585 0.0084  -0.0277 0.0080  262  LYS A C     
1339 O O     . LYS A 79  ? 0.1790 0.1140 0.2778 -0.0083 -0.0316 0.0053  262  LYS A O     
1340 C CB    . LYS A 79  ? 0.1458 0.1757 0.2897 -0.0145 -0.0280 -0.0243 262  LYS A CB    
1341 C CG    . LYS A 79  ? 0.1736 0.2377 0.3605 -0.0554 0.0034  -0.0305 262  LYS A CG    
1342 C CD    . LYS A 79  ? 0.2613 0.2987 0.4163 -0.0967 0.0237  -0.0215 262  LYS A CD    
1343 C CE    . LYS A 79  ? 0.2887 0.3462 0.4715 -0.1089 0.0462  0.0118  262  LYS A CE    
1344 N NZ    . LYS A 79  ? 0.3130 0.3850 0.5404 -0.0791 0.0335  0.0143  262  LYS A NZ    
1358 N N     . PRO A 80  ? 0.1522 0.0770 0.2371 0.0096  -0.0262 0.0099  263  PRO A N     
1359 C CA    . PRO A 80  ? 0.1434 0.0861 0.2410 0.0051  -0.0586 0.0075  263  PRO A CA    
1360 C C     . PRO A 80  ? 0.1309 0.0961 0.2210 0.0087  -0.0444 -0.0011 263  PRO A C     
1361 O O     . PRO A 80  ? 0.1351 0.0989 0.2514 0.0000  -0.0643 -0.0038 263  PRO A O     
1362 C CB    . PRO A 80  ? 0.1590 0.0908 0.2319 0.0098  -0.0394 0.0033  263  PRO A CB    
1363 C CG    . PRO A 80  ? 0.1637 0.0916 0.2377 -0.0121 -0.0187 0.0034  263  PRO A CG    
1364 C CD    . PRO A 80  ? 0.1459 0.0769 0.2333 0.0055  -0.0325 0.0089  263  PRO A CD    
1372 N N     . PHE A 81  ? 0.1485 0.0862 0.2220 0.0213  -0.0489 -0.0071 264  PHE A N     
1373 C CA    . PHE A 81  ? 0.1259 0.0999 0.1830 0.0217  0.0057  -0.0061 264  PHE A CA    
1374 C C     . PHE A 81  ? 0.1018 0.1041 0.2077 0.0032  -0.0399 0.0029  264  PHE A C     
1375 O O     . PHE A 81  ? 0.1115 0.1391 0.2319 0.0023  -0.0346 0.0156  264  PHE A O     
1376 C CB    . PHE A 81  ? 0.1619 0.0983 0.2092 0.0333  -0.0187 0.0019  264  PHE A CB    
1377 C CG    . PHE A 81  ? 0.1551 0.1057 0.2373 0.0165  -0.0452 -0.0080 264  PHE A CG    
1378 C CD1   . PHE A 81  ? 0.1567 0.1227 0.3256 0.0147  -0.0352 -0.0172 264  PHE A CD1   
1379 C CD2   . PHE A 81  ? 0.1691 0.1068 0.2488 0.0069  -0.0586 -0.0201 264  PHE A CD2   
1380 C CE1   . PHE A 81  ? 0.1766 0.1292 0.3480 0.0342  -0.0367 -0.0341 264  PHE A CE1   
1381 C CE2   . PHE A 81  ? 0.1905 0.1114 0.2695 0.0143  -0.0634 -0.0294 264  PHE A CE2   
1382 C CZ    . PHE A 81  ? 0.1822 0.1233 0.3066 0.0299  -0.0543 -0.0386 264  PHE A CZ    
1392 N N     A ILE A 82  ? 0.1351 0.0897 0.2448 0.0079  -0.0701 0.0141  265  ILE A N     
1393 N N     B ILE A 82  ? 0.1349 0.0910 0.2421 0.0071  -0.0689 0.0128  265  ILE A N     
1394 C CA    A ILE A 82  ? 0.1801 0.0912 0.2679 0.0051  -0.0921 -0.0023 265  ILE A CA    
1395 C CA    B ILE A 82  ? 0.1822 0.0916 0.2689 0.0058  -0.0917 -0.0008 265  ILE A CA    
1396 C C     A ILE A 82  ? 0.1970 0.0907 0.2893 0.0088  -0.0918 -0.0031 265  ILE A C     
1397 C C     B ILE A 82  ? 0.1984 0.0904 0.2890 0.0095  -0.0898 -0.0017 265  ILE A C     
1398 O O     A ILE A 82  ? 0.2245 0.0951 0.3532 0.0130  -0.0552 -0.0058 265  ILE A O     
1399 O O     B ILE A 82  ? 0.2253 0.0945 0.3509 0.0132  -0.0544 -0.0037 265  ILE A O     
1400 C CB    A ILE A 82  ? 0.2122 0.1048 0.3185 0.0280  -0.0839 -0.0051 265  ILE A CB    
1401 C CB    B ILE A 82  ? 0.2303 0.1027 0.3232 0.0215  -0.0870 -0.0039 265  ILE A CB    
1402 C CG1   A ILE A 82  ? 0.1686 0.1128 0.3741 0.0245  -0.0782 -0.0331 265  ILE A CG1   
1403 C CG1   B ILE A 82  ? 0.2042 0.1199 0.3867 0.0185  -0.0790 -0.0232 265  ILE A CG1   
1404 C CG2   A ILE A 82  ? 0.2237 0.1183 0.2932 0.0480  -0.0887 0.0103  265  ILE A CG2   
1405 C CG2   B ILE A 82  ? 0.2745 0.1025 0.3087 0.0250  -0.0942 0.0033  265  ILE A CG2   
1406 C CD1   A ILE A 82  ? 0.1923 0.1175 0.3763 0.0031  -0.0839 -0.0453 265  ILE A CD1   
1407 C CD1   B ILE A 82  ? 0.2816 0.1303 0.4060 -0.0198 -0.0648 -0.0202 265  ILE A CD1   
1430 N N     . ILE A 83  ? 0.1886 0.0839 0.2449 0.0150  -0.0912 0.0055  266  ILE A N     
1431 C CA    . ILE A 83  ? 0.1709 0.0857 0.2198 0.0178  -0.0926 0.0067  266  ILE A CA    
1432 C C     . ILE A 83  ? 0.1297 0.0780 0.2440 0.0002  -0.0960 -0.0018 266  ILE A C     
1433 O O     . ILE A 83  ? 0.1318 0.0760 0.2595 0.0054  -0.0801 -0.0009 266  ILE A O     
1434 C CB    . ILE A 83  ? 0.2404 0.0956 0.2320 0.0040  -0.1405 -0.0024 266  ILE A CB    
1435 C CG1   . ILE A 83  ? 0.2038 0.1008 0.2672 -0.0098 -0.1315 0.0004  266  ILE A CG1   
1436 C CG2   . ILE A 83  ? 0.3212 0.1115 0.2307 0.0194  -0.1465 -0.0070 266  ILE A CG2   
1437 C CD1   . ILE A 83  ? 0.2072 0.1070 0.3260 0.0031  -0.1483 -0.0046 266  ILE A CD1   
1450 N N     . ASN A 84  ? 0.1332 0.0761 0.2275 0.0041  -0.0970 -0.0073 267  ASN A N     
1451 C CA    . ASN A 84  ? 0.1249 0.0841 0.2236 0.0047  -0.0909 -0.0144 267  ASN A CA    
1452 C C     . ASN A 84  ? 0.1400 0.0805 0.2475 0.0047  -0.1022 -0.0100 267  ASN A C     
1453 O O     . ASN A 84  ? 0.1469 0.0962 0.2941 0.0191  -0.1081 -0.0360 267  ASN A O     
1454 C CB    . ASN A 84  ? 0.1404 0.0882 0.2561 0.0011  -0.0957 -0.0136 267  ASN A CB    
1455 C CG    . ASN A 84  ? 0.1290 0.0995 0.2366 -0.0029 -0.0914 -0.0156 267  ASN A CG    
1456 O OD1   . ASN A 84  ? 0.1716 0.1144 0.2461 -0.0267 -0.0946 -0.0155 267  ASN A OD1   
1457 N ND2   . ASN A 84  ? 0.1155 0.0947 0.2239 0.0221  -0.0774 -0.0108 267  ASN A ND2   
1464 N N     . ASP A 85  ? 0.1242 0.0771 0.2304 -0.0002 -0.0910 -0.0044 268  ASP A N     
1465 C CA    . ASP A 85  ? 0.1306 0.0828 0.2165 0.0017  -0.0931 0.0062  268  ASP A CA    
1466 C C     . ASP A 85  ? 0.1157 0.0896 0.2244 -0.0008 -0.0860 -0.0005 268  ASP A C     
1467 O O     . ASP A 85  ? 0.1540 0.0859 0.2583 0.0174  -0.0616 -0.0025 268  ASP A O     
1468 C CB    . ASP A 85  ? 0.1226 0.1030 0.2147 -0.0135 -0.0757 0.0146  268  ASP A CB    
1469 C CG    . ASP A 85  ? 0.1566 0.1319 0.2382 -0.0411 -0.0771 0.0147  268  ASP A CG    
1470 O OD1   . ASP A 85  ? 0.1782 0.1261 0.2621 -0.0419 -0.0531 -0.0070 268  ASP A OD1   
1471 O OD2   . ASP A 85  ? 0.2102 0.1780 0.2582 -0.0549 -0.0551 -0.0017 268  ASP A OD2   
1476 N N     . LEU A 86  ? 0.1133 0.0908 0.2118 0.0020  -0.0829 0.0071  269  LEU A N     
1477 C CA    . LEU A 86  ? 0.0864 0.0878 0.1913 0.0010  -0.0644 -0.0002 269  LEU A CA    
1478 C C     . LEU A 86  ? 0.0749 0.0891 0.2029 -0.0038 -0.0508 -0.0111 269  LEU A C     
1479 O O     . LEU A 86  ? 0.0765 0.1043 0.2105 0.0050  -0.0533 -0.0106 269  LEU A O     
1480 C CB    . LEU A 86  ? 0.1129 0.1058 0.2124 0.0152  -0.0804 -0.0037 269  LEU A CB    
1481 C CG    . LEU A 86  ? 0.1432 0.1331 0.2466 0.0257  -0.0992 -0.0099 269  LEU A CG    
1482 C CD1   . LEU A 86  ? 0.1733 0.1497 0.2948 0.0538  -0.0940 -0.0061 269  LEU A CD1   
1483 C CD2   . LEU A 86  ? 0.1448 0.1547 0.2929 0.0268  -0.1048 -0.0346 269  LEU A CD2   
1495 N N     . ILE A 87  ? 0.0984 0.0995 0.2092 0.0082  -0.0730 -0.0107 270  ILE A N     
1496 C CA    . ILE A 87  ? 0.0947 0.1042 0.2084 -0.0009 -0.0705 -0.0042 270  ILE A CA    
1497 C C     . ILE A 87  ? 0.0819 0.1084 0.1990 -0.0108 -0.0575 -0.0034 270  ILE A C     
1498 O O     . ILE A 87  ? 0.0904 0.1090 0.2022 -0.0134 -0.0633 -0.0042 270  ILE A O     
1499 C CB    . ILE A 87  ? 0.0902 0.0987 0.2220 0.0009  -0.0661 -0.0052 270  ILE A CB    
1500 C CG1   . ILE A 87  ? 0.0945 0.1009 0.2409 0.0157  -0.0588 -0.0057 270  ILE A CG1   
1501 C CG2   . ILE A 87  ? 0.0910 0.1036 0.2300 0.0013  -0.0660 -0.0089 270  ILE A CG2   
1502 C CD1   . ILE A 87  ? 0.1189 0.1137 0.2863 -0.0009 -0.0654 0.0055  270  ILE A CD1   
1514 N N     . MET A 88  ? 0.0951 0.1068 0.1963 0.0039  -0.0709 -0.0041 271  MET A N     
1515 C CA    . MET A 88  ? 0.1029 0.0950 0.2122 0.0139  -0.0704 0.0048  271  MET A CA    
1516 C C     . MET A 88  ? 0.0916 0.0906 0.2089 0.0128  -0.0661 -0.0130 271  MET A C     
1517 O O     . MET A 88  ? 0.0939 0.0889 0.2165 0.0040  -0.0683 0.0056  271  MET A O     
1518 C CB    . MET A 88  ? 0.1078 0.0944 0.2343 -0.0024 -0.0803 0.0082  271  MET A CB    
1519 C CG    . MET A 88  ? 0.1398 0.0899 0.2637 -0.0106 -0.0748 -0.0018 271  MET A CG    
1520 S SD    . MET A 88  ? 0.1031 0.0949 0.3002 -0.0006 -0.0678 -0.0121 271  MET A SD    
1521 C CE    . MET A 88  ? 0.1269 0.0775 0.2900 -0.0023 -0.0562 -0.0009 271  MET A CE    
1531 N N     . GLN A 89  ? 0.0865 0.0994 0.2130 0.0072  -0.0627 -0.0048 272  GLN A N     
1532 C CA    . GLN A 89  ? 0.0924 0.1016 0.2162 0.0146  -0.0624 0.0040  272  GLN A CA    
1533 C C     . GLN A 89  ? 0.0919 0.1100 0.2365 -0.0005 -0.0665 0.0018  272  GLN A C     
1534 O O     . GLN A 89  ? 0.1139 0.1264 0.2370 -0.0181 -0.0807 0.0015  272  GLN A O     
1535 C CB    . GLN A 89  ? 0.0858 0.1085 0.2173 0.0113  -0.0587 0.0052  272  GLN A CB    
1536 C CG    . GLN A 89  ? 0.0846 0.1459 0.2119 0.0105  -0.0607 -0.0079 272  GLN A CG    
1537 C CD    . GLN A 89  ? 0.0954 0.2013 0.2225 0.0369  -0.0597 -0.0183 272  GLN A CD    
1538 O OE1   . GLN A 89  ? 0.1480 0.2897 0.2544 0.0663  -0.0850 0.0008  272  GLN A OE1   
1539 N NE2   . GLN A 89  ? 0.1133 0.1751 0.2349 0.0097  -0.0768 -0.0296 272  GLN A NE2   
1548 N N     . LYS A 90  ? 0.0994 0.1074 0.2365 -0.0136 -0.0590 -0.0208 273  LYS A N     
1549 C CA    . LYS A 90  ? 0.1290 0.1244 0.2285 -0.0282 -0.0644 -0.0173 273  LYS A CA    
1550 C C     . LYS A 90  ? 0.1392 0.1473 0.2429 -0.0371 -0.0841 -0.0113 273  LYS A C     
1551 O O     . LYS A 90  ? 0.1570 0.1619 0.2649 -0.0318 -0.0744 -0.0248 273  LYS A O     
1552 C CB    . LYS A 90  ? 0.1326 0.1151 0.2439 -0.0353 -0.0547 -0.0318 273  LYS A CB    
1553 C CG    . LYS A 90  ? 0.1340 0.1118 0.2905 -0.0274 -0.0322 -0.0306 273  LYS A CG    
1554 C CD    . LYS A 90  ? 0.1344 0.1287 0.3435 -0.0147 -0.0331 -0.0144 273  LYS A CD    
1555 C CE    . LYS A 90  ? 0.1578 0.1210 0.3434 -0.0277 -0.0389 -0.0171 273  LYS A CE    
1556 N NZ    . LYS A 90  ? 0.1850 0.1095 0.3694 -0.0262 -0.0579 -0.0166 273  LYS A NZ    
1570 N N     . ILE A 91  ? 0.1142 0.1247 0.2105 -0.0268 -0.0737 0.0191  274  ILE A N     
1571 C CA    . ILE A 91  ? 0.1331 0.1312 0.2638 -0.0083 -0.0973 0.0291  274  ILE A CA    
1572 C C     . ILE A 91  ? 0.1234 0.1242 0.2590 -0.0184 -0.0904 0.0292  274  ILE A C     
1573 O O     . ILE A 91  ? 0.1361 0.1270 0.2733 -0.0096 -0.1008 0.0226  274  ILE A O     
1574 C CB    . ILE A 91  ? 0.1626 0.1467 0.3384 0.0318  -0.0733 0.0479  274  ILE A CB    
1575 C CG1   . ILE A 91  ? 0.1356 0.1611 0.3349 0.0063  -0.0932 0.0315  274  ILE A CG1   
1576 C CG2   . ILE A 91  ? 0.1637 0.1607 0.3984 0.0171  -0.0358 0.0810  274  ILE A CG2   
1577 C CD1   . ILE A 91  ? 0.1292 0.1532 0.4030 -0.0016 -0.0816 0.0020  274  ILE A CD1   
1589 N N     . LEU A 92  ? 0.1437 0.1218 0.2659 -0.0345 -0.0945 0.0223  275  LEU A N     
1590 C CA    . LEU A 92  ? 0.1632 0.1199 0.2888 -0.0351 -0.1045 0.0213  275  LEU A CA    
1591 C C     . LEU A 92  ? 0.1507 0.1261 0.3028 -0.0294 -0.0904 0.0415  275  LEU A C     
1592 O O     . LEU A 92  ? 0.2094 0.1296 0.3356 -0.0113 -0.0496 0.0554  275  LEU A O     
1593 C CB    . LEU A 92  ? 0.1663 0.1319 0.3094 -0.0377 -0.0995 0.0078  275  LEU A CB    
1594 C CG    . LEU A 92  ? 0.1742 0.1562 0.3163 -0.0230 -0.1210 -0.0043 275  LEU A CG    
1595 C CD1   . LEU A 92  ? 0.1715 0.2012 0.3275 -0.0149 -0.1244 -0.0108 275  LEU A CD1   
1596 C CD2   . LEU A 92  ? 0.1886 0.1379 0.3339 -0.0080 -0.0929 -0.0045 275  LEU A CD2   
1608 N N     . TRP A 93  ? 0.1361 0.1367 0.2941 -0.0057 -0.0727 0.0305  276  TRP A N     
1609 C CA    . TRP A 93  ? 0.1506 0.1577 0.3102 0.0307  -0.0669 0.0284  276  TRP A CA    
1610 C C     . TRP A 93  ? 0.1648 0.1651 0.2631 0.0285  -0.0657 0.0351  276  TRP A C     
1611 O O     . TRP A 93  ? 0.2303 0.1944 0.2694 0.0650  -0.0274 0.0440  276  TRP A O     
1612 C CB    . TRP A 93  ? 0.1552 0.1744 0.3277 0.0540  -0.0751 0.0129  276  TRP A CB    
1613 C CG    . TRP A 93  ? 0.1794 0.2018 0.3330 0.0442  -0.0908 -0.0333 276  TRP A CG    
1614 C CD1   . TRP A 93  ? 0.1978 0.2184 0.3663 0.0551  -0.1070 -0.0570 276  TRP A CD1   
1615 C CD2   . TRP A 93  ? 0.1947 0.2075 0.3080 0.0725  -0.1142 -0.0286 276  TRP A CD2   
1616 N NE1   . TRP A 93  ? 0.2146 0.2297 0.3585 0.0590  -0.1240 -0.0586 276  TRP A NE1   
1617 C CE2   . TRP A 93  ? 0.2157 0.2238 0.3130 0.0739  -0.1122 -0.0397 276  TRP A CE2   
1618 C CE3   . TRP A 93  ? 0.2299 0.2030 0.3413 0.0715  -0.1009 -0.0051 276  TRP A CE3   
1619 C CZ2   . TRP A 93  ? 0.2118 0.2295 0.3113 0.0757  -0.1101 -0.0074 276  TRP A CZ2   
1620 C CZ3   . TRP A 93  ? 0.2419 0.2100 0.3550 0.0790  -0.0777 0.0144  276  TRP A CZ3   
1621 C CH2   . TRP A 93  ? 0.2383 0.2231 0.3275 0.0518  -0.1044 0.0176  276  TRP A CH2   
1632 N N     . ASP A 94  ? 0.1226 0.1383 0.2296 0.0228  -0.0509 0.0256  277  ASP A N     
1633 C CA    . ASP A 94  ? 0.1293 0.1216 0.2204 0.0236  -0.0362 0.0139  277  ASP A CA    
1634 C C     . ASP A 94  ? 0.1286 0.1091 0.2024 0.0232  -0.0610 -0.0003 277  ASP A C     
1635 O O     . ASP A 94  ? 0.1304 0.1085 0.1994 0.0240  -0.0751 -0.0009 277  ASP A O     
1636 C CB    . ASP A 94  ? 0.1560 0.1247 0.2101 0.0186  -0.0522 0.0075  277  ASP A CB    
1637 C CG    . ASP A 94  ? 0.1926 0.1335 0.2552 0.0247  -0.1156 -0.0065 277  ASP A CG    
1638 O OD1   . ASP A 94  ? 0.1944 0.1148 0.2504 0.0333  -0.0989 0.0055  277  ASP A OD1   
1639 O OD2   . ASP A 94  ? 0.3027 0.1530 0.2861 0.0544  -0.1592 -0.0239 277  ASP A OD2   
1644 N N     . ARG A 95  ? 0.1281 0.1083 0.2050 0.0051  -0.0585 0.0113  278  ARG A N     
1645 C CA    A ARG A 95  ? 0.1326 0.1161 0.2076 0.0082  -0.0696 0.0111  278  ARG A CA    
1646 C CA    B ARG A 95  ? 0.1168 0.1096 0.2138 0.0151  -0.0677 0.0038  278  ARG A CA    
1647 C C     . ARG A 95  ? 0.1222 0.1135 0.2131 0.0165  -0.0734 0.0068  278  ARG A C     
1648 O O     . ARG A 95  ? 0.1433 0.1148 0.2129 0.0068  -0.0727 0.0005  278  ARG A O     
1649 C CB    A ARG A 95  ? 0.1663 0.1227 0.2070 -0.0145 -0.0204 0.0180  278  ARG A CB    
1650 C CB    B ARG A 95  ? 0.1088 0.1061 0.2302 0.0078  -0.0377 -0.0070 278  ARG A CB    
1651 C CG    A ARG A 95  ? 0.2159 0.1449 0.2354 -0.0421 -0.0266 0.0315  278  ARG A CG    
1652 C CG    B ARG A 95  ? 0.1136 0.1115 0.2649 -0.0056 -0.0178 -0.0088 278  ARG A CG    
1653 C CD    A ARG A 95  ? 0.2956 0.1880 0.2758 -0.0778 -0.0361 0.0700  278  ARG A CD    
1654 C CD    B ARG A 95  ? 0.1365 0.1276 0.2936 -0.0280 0.0107  -0.0085 278  ARG A CD    
1655 N NE    A ARG A 95  ? 0.3910 0.2355 0.3179 -0.0688 -0.0756 0.1006  278  ARG A NE    
1656 N NE    B ARG A 95  ? 0.1290 0.1423 0.3204 -0.0433 -0.0162 -0.0231 278  ARG A NE    
1657 C CZ    A ARG A 95  ? 0.4732 0.2680 0.3430 -0.0539 -0.1278 0.1214  278  ARG A CZ    
1658 C CZ    B ARG A 95  ? 0.1334 0.1556 0.3315 -0.0472 -0.0340 -0.0318 278  ARG A CZ    
1659 N NH1   A ARG A 95  ? 0.5117 0.2642 0.3878 -0.0393 -0.1527 0.1167  278  ARG A NH1   
1660 N NH1   B ARG A 95  ? 0.1598 0.1656 0.3293 -0.0121 -0.0410 -0.0619 278  ARG A NH1   
1661 N NH2   A ARG A 95  ? 0.5210 0.2930 0.3544 -0.0495 -0.1424 0.1362  278  ARG A NH2   
1662 N NH2   B ARG A 95  ? 0.1546 0.1583 0.3697 -0.0454 -0.0309 -0.0113 278  ARG A NH2   
1689 N N     . ARG A 96  ? 0.1152 0.1196 0.2129 -0.0042 -0.0790 -0.0005 279  ARG A N     
1690 C CA    . ARG A 96  ? 0.1186 0.1196 0.2234 -0.0055 -0.0876 0.0019  279  ARG A CA    
1691 C C     . ARG A 96  ? 0.1175 0.1231 0.2184 -0.0042 -0.0851 -0.0130 279  ARG A C     
1692 O O     . ARG A 96  ? 0.1221 0.1373 0.2331 0.0099  -0.0793 0.0032  279  ARG A O     
1693 C CB    . ARG A 96  ? 0.1280 0.1146 0.2328 -0.0054 -0.0742 0.0077  279  ARG A CB    
1694 C CG    . ARG A 96  ? 0.1565 0.1175 0.2242 -0.0007 -0.0757 0.0104  279  ARG A CG    
1695 C CD    . ARG A 96  ? 0.1737 0.1125 0.2116 -0.0170 -0.0985 0.0041  279  ARG A CD    
1696 N NE    . ARG A 96  ? 0.2027 0.1052 0.2258 -0.0094 -0.0886 0.0133  279  ARG A NE    
1697 C CZ    . ARG A 96  ? 0.2247 0.1142 0.2417 -0.0003 -0.0909 0.0174  279  ARG A CZ    
1698 N NH1   . ARG A 96  ? 0.2543 0.1198 0.2595 -0.0004 -0.1203 0.0010  279  ARG A NH1   
1699 N NH2   . ARG A 96  ? 0.2452 0.1156 0.2377 -0.0125 -0.1146 0.0170  279  ARG A NH2   
1713 N N     . LEU A 97  ? 0.1263 0.1025 0.2382 0.0010  -0.0900 0.0081  280  LEU A N     
1714 C CA    . LEU A 97  ? 0.1243 0.0932 0.2194 -0.0039 -0.0865 0.0160  280  LEU A CA    
1715 C C     . LEU A 97  ? 0.0926 0.0997 0.1556 -0.0047 -0.0628 0.0187  280  LEU A C     
1716 O O     . LEU A 97  ? 0.1017 0.1070 0.1685 0.0082  -0.0537 0.0008  280  LEU A O     
1717 C CB    . LEU A 97  ? 0.1587 0.0968 0.2324 -0.0146 -0.0952 0.0110  280  LEU A CB    
1718 C CG    . LEU A 97  ? 0.1723 0.1082 0.2314 -0.0275 -0.0749 0.0016  280  LEU A CG    
1719 C CD1   . LEU A 97  ? 0.2380 0.1134 0.2282 -0.0079 -0.0526 0.0142  280  LEU A CD1   
1720 C CD2   . LEU A 97  ? 0.1850 0.1174 0.2262 -0.0155 -0.0848 -0.0122 280  LEU A CD2   
1732 N N     . CYS A 98  ? 0.1013 0.0983 0.1985 0.0058  -0.0740 0.0051  281  CYS A N     
1733 C CA    A CYS A 98  ? 0.0895 0.0941 0.2097 0.0085  -0.0596 -0.0047 281  CYS A CA    
1734 C CA    B CYS A 98  ? 0.1150 0.1134 0.2001 -0.0054 -0.0671 -0.0073 281  CYS A CA    
1735 C C     . CYS A 98  ? 0.1018 0.1005 0.1934 0.0074  -0.0538 0.0009  281  CYS A C     
1736 O O     . CYS A 98  ? 0.1084 0.0960 0.1943 0.0001  -0.0491 0.0039  281  CYS A O     
1737 C CB    A CYS A 98  ? 0.0949 0.1055 0.2402 0.0048  -0.0684 0.0013  281  CYS A CB    
1738 C CB    B CYS A 98  ? 0.1375 0.1486 0.2072 -0.0304 -0.0763 -0.0167 281  CYS A CB    
1739 S SG    A CYS A 98  ? 0.1020 0.1226 0.2572 0.0153  -0.0669 -0.0019 281  CYS A SG    
1740 S SG    B CYS A 98  ? 0.1689 0.1788 0.2230 -0.0438 -0.0625 -0.0152 281  CYS A SG    
1751 N N     . LEU A 99  ? 0.1236 0.1112 0.2071 0.0323  -0.0621 0.0095  282  LEU A N     
1752 C CA    . LEU A 99  ? 0.1358 0.1373 0.2166 0.0486  -0.0466 0.0258  282  LEU A CA    
1753 C C     . LEU A 99  ? 0.1123 0.1470 0.2098 0.0488  -0.0485 0.0198  282  LEU A C     
1754 O O     . LEU A 99  ? 0.1290 0.1583 0.2265 0.0477  -0.0183 0.0218  282  LEU A O     
1755 C CB    . LEU A 99  ? 0.1744 0.1617 0.2311 0.0640  -0.0224 0.0471  282  LEU A CB    
1756 C CG    . LEU A 99  ? 0.1999 0.1733 0.2575 0.0764  -0.0229 0.0597  282  LEU A CG    
1757 C CD1   . LEU A 99  ? 0.2567 0.1871 0.2696 0.0484  -0.0277 0.0618  282  LEU A CD1   
1758 C CD2   . LEU A 99  ? 0.2321 0.1809 0.2919 0.0537  0.0104  0.0548  282  LEU A CD2   
1770 N N     . GLN A 100 ? 0.1144 0.1397 0.2279 0.0306  -0.0694 0.0076  283  GLN A N     
1771 C CA    . GLN A 100 ? 0.1111 0.1585 0.2335 0.0279  -0.0639 0.0071  283  GLN A CA    
1772 C C     . GLN A 100 ? 0.1027 0.1290 0.2092 0.0104  -0.0503 0.0034  283  GLN A C     
1773 O O     . GLN A 100 ? 0.0910 0.1317 0.2277 -0.0030 -0.0664 0.0032  283  GLN A O     
1774 C CB    . GLN A 100 ? 0.1029 0.1954 0.2197 0.0058  -0.0766 0.0021  283  GLN A CB    
1775 C CG    . GLN A 100 ? 0.1001 0.2235 0.2621 -0.0259 -0.0659 -0.0094 283  GLN A CG    
1776 C CD    . GLN A 100 ? 0.1316 0.2378 0.2897 -0.0409 -0.0826 -0.0195 283  GLN A CD    
1777 O OE1   . GLN A 100 ? 0.1542 0.2448 0.3279 -0.0330 -0.0615 0.0025  283  GLN A OE1   
1778 N NE2   . GLN A 100 ? 0.1600 0.2361 0.3229 -0.0230 -0.1068 -0.0180 283  GLN A NE2   
1787 N N     . VAL A 101 ? 0.0853 0.1012 0.2069 0.0096  -0.0566 0.0004  284  VAL A N     
1788 C CA    . VAL A 101 ? 0.0893 0.1014 0.2167 -0.0066 -0.0645 -0.0013 284  VAL A CA    
1789 C C     . VAL A 101 ? 0.0996 0.1038 0.2222 -0.0079 -0.0734 0.0043  284  VAL A C     
1790 O O     . VAL A 101 ? 0.1022 0.0963 0.2362 -0.0037 -0.0726 -0.0038 284  VAL A O     
1791 C CB    . VAL A 101 ? 0.0847 0.0970 0.1986 -0.0001 -0.0627 0.0009  284  VAL A CB    
1792 C CG1   . VAL A 101 ? 0.0940 0.1096 0.2277 0.0042  -0.0555 -0.0008 284  VAL A CG1   
1793 C CG2   . VAL A 101 ? 0.1004 0.0954 0.2209 0.0015  -0.0563 0.0129  284  VAL A CG2   
1803 N N     . LEU A 102 ? 0.0967 0.0898 0.2253 -0.0087 -0.0388 0.0034  285  LEU A N     
1804 C CA    . LEU A 102 ? 0.1018 0.0961 0.2319 0.0050  -0.0065 -0.0011 285  LEU A CA    
1805 C C     . LEU A 102 ? 0.1047 0.1063 0.2595 -0.0044 -0.0190 -0.0029 285  LEU A C     
1806 O O     . LEU A 102 ? 0.1090 0.0966 0.2830 -0.0171 -0.0233 -0.0125 285  LEU A O     
1807 C CB    . LEU A 102 ? 0.1114 0.1043 0.2381 0.0004  -0.0138 -0.0080 285  LEU A CB    
1808 C CG    . LEU A 102 ? 0.1156 0.1143 0.2500 0.0057  -0.0285 -0.0056 285  LEU A CG    
1809 C CD1   . LEU A 102 ? 0.0976 0.1392 0.2557 0.0139  -0.0268 0.0234  285  LEU A CD1   
1810 C CD2   . LEU A 102 ? 0.1184 0.1000 0.2716 -0.0314 -0.0323 -0.0096 285  LEU A CD2   
1822 N N     . GLU A 103 ? 0.1124 0.1304 0.2770 0.0147  -0.0418 -0.0046 286  GLU A N     
1823 C CA    A GLU A 103 ? 0.1475 0.1543 0.2769 0.0277  -0.0309 -0.0042 286  GLU A CA    
1824 C CA    B GLU A 103 ? 0.1091 0.1636 0.2611 0.0416  -0.0445 0.0008  286  GLU A CA    
1825 C C     . GLU A 103 ? 0.0837 0.1518 0.2558 0.0298  -0.0356 0.0005  286  GLU A C     
1826 O O     . GLU A 103 ? 0.0925 0.1431 0.3145 0.0084  -0.0438 0.0029  286  GLU A O     
1827 C CB    A GLU A 103 ? 0.2096 0.1822 0.3075 0.0356  -0.0255 0.0088  286  GLU A CB    
1828 C CB    B GLU A 103 ? 0.1207 0.2093 0.2557 0.0615  -0.0563 0.0235  286  GLU A CB    
1829 C CG    A GLU A 103 ? 0.2508 0.2084 0.3569 0.0457  -0.0255 0.0152  286  GLU A CG    
1830 C CG    B GLU A 103 ? 0.1637 0.2447 0.3258 0.0655  -0.0753 0.0502  286  GLU A CG    
1831 C CD    A GLU A 103 ? 0.2719 0.2412 0.3991 0.0722  -0.0229 0.0118  286  GLU A CD    
1832 C CD    B GLU A 103 ? 0.2405 0.2791 0.3981 0.0539  -0.0821 0.0764  286  GLU A CD    
1833 O OE1   A GLU A 103 ? 0.1792 0.2620 0.4119 0.0677  -0.0942 0.0000  286  GLU A OE1   
1834 O OE1   B GLU A 103 ? 0.2485 0.2744 0.4046 0.0280  -0.1328 0.1035  286  GLU A OE1   
1835 O OE2   A GLU A 103 ? 0.3706 0.2494 0.4262 0.1077  0.0401  0.0158  286  GLU A OE2   
1836 O OE2   B GLU A 103 ? 0.3314 0.3107 0.4306 0.0438  -0.0609 0.0758  286  GLU A OE2   
1849 N N     . ALA A 104 ? 0.0815 0.1466 0.2182 0.0186  -0.0333 -0.0076 287  ALA A N     
1850 C CA    . ALA A 104 ? 0.0956 0.1403 0.2146 0.0127  -0.0343 -0.0223 287  ALA A CA    
1851 C C     . ALA A 104 ? 0.0898 0.1284 0.2318 0.0011  -0.0292 -0.0150 287  ALA A C     
1852 O O     . ALA A 104 ? 0.0946 0.1375 0.2510 -0.0266 -0.0420 -0.0330 287  ALA A O     
1853 C CB    . ALA A 104 ? 0.1027 0.1493 0.2104 0.0029  -0.0308 -0.0191 287  ALA A CB    
1859 N N     . TYR A 105 ? 0.0876 0.1244 0.2428 -0.0113 -0.0539 -0.0206 288  TYR A N     
1860 C CA    . TYR A 105 ? 0.1075 0.1309 0.2343 -0.0101 -0.0457 -0.0171 288  TYR A CA    
1861 C C     . TYR A 105 ? 0.1325 0.1329 0.2596 -0.0124 -0.0459 -0.0236 288  TYR A C     
1862 O O     . TYR A 105 ? 0.1515 0.1469 0.2506 -0.0245 -0.0296 -0.0251 288  TYR A O     
1863 C CB    . TYR A 105 ? 0.1196 0.1284 0.2158 -0.0148 -0.0629 -0.0085 288  TYR A CB    
1864 C CG    . TYR A 105 ? 0.1083 0.1353 0.2197 -0.0188 -0.0502 -0.0044 288  TYR A CG    
1865 C CD1   . TYR A 105 ? 0.0873 0.1383 0.2348 -0.0136 -0.0432 0.0004  288  TYR A CD1   
1866 C CD2   . TYR A 105 ? 0.1669 0.1392 0.2192 -0.0198 -0.0352 -0.0110 288  TYR A CD2   
1867 C CE1   . TYR A 105 ? 0.1211 0.1433 0.2565 -0.0133 -0.0493 -0.0030 288  TYR A CE1   
1868 C CE2   . TYR A 105 ? 0.2132 0.1415 0.2356 0.0041  -0.0463 -0.0019 288  TYR A CE2   
1869 C CZ    . TYR A 105 ? 0.1814 0.1424 0.2563 -0.0079 -0.0353 0.0038  288  TYR A CZ    
1870 O OH    . TYR A 105 ? 0.2613 0.1476 0.2607 -0.0205 -0.0394 0.0208  288  TYR A OH    
1880 N N     . ASN A 106 ? 0.1043 0.1164 0.2790 -0.0176 -0.0370 -0.0200 289  ASN A N     
1881 C CA    . ASN A 106 ? 0.1156 0.1203 0.3276 -0.0026 0.0029  -0.0158 289  ASN A CA    
1882 C C     . ASN A 106 ? 0.0986 0.1099 0.3254 -0.0049 -0.0273 -0.0178 289  ASN A C     
1883 O O     . ASN A 106 ? 0.1429 0.1169 0.3748 -0.0190 -0.0020 -0.0548 289  ASN A O     
1884 C CB    . ASN A 106 ? 0.1661 0.1621 0.4160 0.0134  0.0602  0.0008  289  ASN A CB    
1885 C CG    . ASN A 106 ? 0.2301 0.2281 0.5336 0.0277  0.0554  0.0541  289  ASN A CG    
1886 O OD1   . ASN A 106 ? 0.3369 0.2588 0.6236 0.0288  0.0187  0.0684  289  ASN A OD1   
1887 N ND2   . ASN A 106 ? 0.2284 0.2609 0.5658 -0.0187 -0.0276 0.0448  289  ASN A ND2   
1894 N N     . VAL A 107 ? 0.0720 0.0958 0.2482 -0.0072 -0.0339 -0.0023 290  VAL A N     
1895 C CA    . VAL A 107 ? 0.0799 0.1081 0.2433 -0.0071 -0.0470 -0.0079 290  VAL A CA    
1896 C C     . VAL A 107 ? 0.0888 0.1100 0.2438 0.0106  -0.0607 -0.0093 290  VAL A C     
1897 O O     . VAL A 107 ? 0.1078 0.1148 0.2360 -0.0059 -0.0723 -0.0144 290  VAL A O     
1898 C CB    . VAL A 107 ? 0.0855 0.1236 0.2197 -0.0145 -0.0419 0.0023  290  VAL A CB    
1899 C CG1   . VAL A 107 ? 0.0770 0.1145 0.2540 -0.0052 -0.0435 -0.0006 290  VAL A CG1   
1900 C CG2   . VAL A 107 ? 0.1053 0.1411 0.2221 -0.0025 -0.0333 0.0129  290  VAL A CG2   
1910 N N     . PRO A 108 ? 0.0979 0.0965 0.2590 0.0050  -0.0563 -0.0068 291  PRO A N     
1911 C CA    . PRO A 108 ? 0.1074 0.0999 0.2552 0.0005  -0.0476 0.0154  291  PRO A CA    
1912 C C     . PRO A 108 ? 0.0945 0.1022 0.2309 0.0046  -0.0674 0.0101  291  PRO A C     
1913 O O     . PRO A 108 ? 0.0942 0.1140 0.2455 -0.0075 -0.0672 0.0072  291  PRO A O     
1914 C CB    . PRO A 108 ? 0.1939 0.0990 0.2858 0.0131  -0.0621 0.0075  291  PRO A CB    
1915 C CG    . PRO A 108 ? 0.3159 0.1016 0.3087 0.0155  -0.0660 -0.0112 291  PRO A CG    
1916 C CD    . PRO A 108 ? 0.1588 0.0944 0.2785 0.0150  -0.0518 -0.0223 291  PRO A CD    
1924 N N     . THR A 109 ? 0.1183 0.1021 0.2428 0.0048  -0.0870 0.0047  292  THR A N     
1925 C CA    . THR A 109 ? 0.1300 0.1075 0.2613 0.0020  -0.0968 0.0015  292  THR A CA    
1926 C C     . THR A 109 ? 0.1069 0.1199 0.2377 0.0067  -0.0771 0.0119  292  THR A C     
1927 O O     . THR A 109 ? 0.1092 0.1213 0.2566 0.0145  -0.0754 0.0060  292  THR A O     
1928 C CB    . THR A 109 ? 0.1375 0.1057 0.2794 0.0060  -0.1010 0.0019  292  THR A CB    
1929 O OG1   . THR A 109 ? 0.1769 0.1103 0.3013 -0.0063 -0.1277 0.0014  292  THR A OG1   
1930 C CG2   . THR A 109 ? 0.1270 0.1014 0.3125 0.0037  -0.0926 -0.0011 292  THR A CG2   
1938 N N     . PRO A 110 ? 0.1127 0.1296 0.2373 0.0028  -0.0808 0.0228  293  PRO A N     
1939 C CA    . PRO A 110 ? 0.1291 0.1468 0.2421 0.0083  -0.0894 0.0277  293  PRO A CA    
1940 C C     . PRO A 110 ? 0.1314 0.1426 0.2586 0.0115  -0.0945 0.0107  293  PRO A C     
1941 O O     . PRO A 110 ? 0.1332 0.1342 0.2741 0.0037  -0.0993 0.0004  293  PRO A O     
1942 C CB    . PRO A 110 ? 0.1302 0.1786 0.2704 -0.0016 -0.0894 0.0489  293  PRO A CB    
1943 C CG    . PRO A 110 ? 0.1359 0.1820 0.2632 0.0072  -0.0963 0.0294  293  PRO A CG    
1944 C CD    . PRO A 110 ? 0.1111 0.1533 0.2605 0.0133  -0.0763 0.0207  293  PRO A CD    
1952 N N     . PRO A 111 ? 0.1337 0.1528 0.2522 0.0157  -0.0964 0.0021  294  PRO A N     
1953 C CA    . PRO A 111 ? 0.1418 0.1696 0.2743 0.0241  -0.0997 0.0036  294  PRO A CA    
1954 C C     . PRO A 111 ? 0.1502 0.1558 0.2602 0.0118  -0.1059 0.0153  294  PRO A C     
1955 O O     . PRO A 111 ? 0.1369 0.1419 0.2709 0.0095  -0.0979 0.0162  294  PRO A O     
1956 C CB    . PRO A 111 ? 0.1516 0.1872 0.2907 0.0384  -0.1004 0.0030  294  PRO A CB    
1957 C CG    . PRO A 111 ? 0.1747 0.1847 0.3179 0.0418  -0.1075 0.0056  294  PRO A CG    
1958 C CD    . PRO A 111 ? 0.1569 0.1644 0.3169 0.0330  -0.0978 -0.0021 294  PRO A CD    
1966 N N     . ARG A 112 ? 0.1408 0.1553 0.2469 -0.0031 -0.1027 0.0138  295  ARG A N     
1967 C CA    . ARG A 112 ? 0.1260 0.1492 0.2379 -0.0151 -0.0923 0.0189  295  ARG A CA    
1968 C C     . ARG A 112 ? 0.1118 0.1548 0.2580 -0.0172 -0.0811 0.0177  295  ARG A C     
1969 O O     . ARG A 112 ? 0.1416 0.1874 0.2853 -0.0067 -0.1053 -0.0008 295  ARG A O     
1970 C CB    . ARG A 112 ? 0.1528 0.1451 0.2748 -0.0122 -0.1120 0.0163  295  ARG A CB    
1971 C CG    . ARG A 112 ? 0.1904 0.1622 0.3183 -0.0130 -0.1318 0.0506  295  ARG A CG    
1972 C CD    . ARG A 112 ? 0.2508 0.1664 0.3488 -0.0447 -0.1674 0.0685  295  ARG A CD    
1973 N NE    . ARG A 112 ? 0.2957 0.1919 0.3716 -0.0565 -0.1801 0.0896  295  ARG A NE    
1974 C CZ    . ARG A 112 ? 0.2273 0.2168 0.3680 -0.0300 -0.1374 0.1111  295  ARG A CZ    
1975 N NH1   . ARG A 112 ? 0.1457 0.2284 0.3580 0.0029  -0.0814 0.0936  295  ARG A NH1   
1976 N NH2   . ARG A 112 ? 0.2793 0.2419 0.4239 -0.0270 -0.1304 0.1469  295  ARG A NH2   
1990 N N     . LEU A 113 ? 0.1288 0.1319 0.2714 -0.0156 -0.0950 0.0228  296  LEU A N     
1991 C CA    . LEU A 113 ? 0.1696 0.1285 0.2846 -0.0161 -0.1223 0.0170  296  LEU A CA    
1992 C C     . LEU A 113 ? 0.1572 0.1230 0.2799 -0.0208 -0.1114 0.0118  296  LEU A C     
1993 O O     . LEU A 113 ? 0.1510 0.1214 0.2843 -0.0222 -0.1032 0.0152  296  LEU A O     
1994 C CB    . LEU A 113 ? 0.1799 0.1481 0.3123 -0.0161 -0.1308 0.0165  296  LEU A CB    
1995 C CG    . LEU A 113 ? 0.2082 0.1774 0.3346 -0.0126 -0.1492 0.0217  296  LEU A CG    
1996 C CD1   . LEU A 113 ? 0.2475 0.1863 0.3359 0.0006  -0.1655 0.0265  296  LEU A CD1   
1997 C CD2   . LEU A 113 ? 0.2200 0.2050 0.3703 0.0127  -0.1553 0.0201  296  LEU A CD2   
2009 N N     . GLU A 114 ? 0.1825 0.1273 0.2833 -0.0260 -0.1249 0.0155  297  GLU A N     
2010 C CA    . GLU A 114 ? 0.1819 0.1414 0.2654 -0.0174 -0.1265 0.0199  297  GLU A CA    
2011 C C     . GLU A 114 ? 0.2095 0.1439 0.2547 -0.0252 -0.1334 0.0171  297  GLU A C     
2012 O O     . GLU A 114 ? 0.2163 0.1623 0.2866 -0.0260 -0.1449 0.0228  297  GLU A O     
2013 C CB    . GLU A 114 ? 0.2150 0.1528 0.2508 -0.0160 -0.1129 0.0124  297  GLU A CB    
2014 C CG    . GLU A 114 ? 0.2391 0.1700 0.2732 -0.0116 -0.1026 0.0303  297  GLU A CG    
2015 C CD    . GLU A 114 ? 0.2372 0.1765 0.3155 -0.0241 -0.1280 0.0336  297  GLU A CD    
2016 O OE1   . GLU A 114 ? 0.2834 0.1834 0.3144 -0.0082 -0.1056 0.0328  297  GLU A OE1   
2017 O OE2   . GLU A 114 ? 0.2347 0.1766 0.3087 -0.0220 -0.1015 0.0281  297  GLU A OE2   
2024 N N     . ILE A 115 ? 0.2394 0.1319 0.2242 -0.0264 -0.1271 0.0176  298  ILE A N     
2025 C CA    . ILE A 115 ? 0.2500 0.1410 0.2269 -0.0189 -0.1418 0.0133  298  ILE A CA    
2026 C C     . ILE A 115 ? 0.2640 0.1376 0.2384 -0.0393 -0.1291 0.0142  298  ILE A C     
2027 O O     . ILE A 115 ? 0.2641 0.1413 0.2573 -0.0371 -0.1177 0.0094  298  ILE A O     
2028 C CB    . ILE A 115 ? 0.2618 0.1516 0.2556 -0.0367 -0.1484 0.0111  298  ILE A CB    
2029 C CG1   . ILE A 115 ? 0.2843 0.1495 0.2671 -0.0385 -0.1584 0.0267  298  ILE A CG1   
2030 C CG2   . ILE A 115 ? 0.2986 0.1725 0.2819 -0.0404 -0.1449 0.0090  298  ILE A CG2   
2031 C CD1   . ILE A 115 ? 0.3197 0.1470 0.2616 -0.0390 -0.1547 0.0143  298  ILE A CD1   
2043 N N     . SER A 116 ? 0.3008 0.1293 0.2425 -0.0443 -0.1381 0.0222  299  SER A N     
2044 C CA    . SER A 116 ? 0.3137 0.1313 0.2352 -0.0498 -0.1308 0.0117  299  SER A CA    
2045 C C     . SER A 116 ? 0.3235 0.1470 0.2328 -0.0638 -0.1294 0.0059  299  SER A C     
2046 O O     . SER A 116 ? 0.3260 0.1583 0.2498 -0.0621 -0.1479 0.0130  299  SER A O     
2047 C CB    . SER A 116 ? 0.3503 0.1292 0.2463 -0.0370 -0.1494 0.0199  299  SER A CB    
2048 O OG    . SER A 116 ? 0.3243 0.1271 0.2575 -0.0257 -0.1648 0.0103  299  SER A OG    
2054 N N     . ARG A 117 ? 0.3608 0.1513 0.2151 -0.0612 -0.1095 -0.0091 300  ARG A N     
2055 C CA    . ARG A 117 ? 0.4318 0.1582 0.1752 -0.0503 -0.0947 -0.0126 300  ARG A CA    
2056 C C     . ARG A 117 ? 0.4386 0.1682 0.1871 -0.0494 -0.0899 -0.0190 300  ARG A C     
2057 O O     . ARG A 117 ? 0.4954 0.1761 0.2269 -0.0644 -0.1029 -0.0243 300  ARG A O     
2058 C CB    . ARG A 117 ? 0.4577 0.1617 0.1895 -0.0563 -0.0942 -0.0166 300  ARG A CB    
2059 C CG    . ARG A 117 ? 0.4787 0.1614 0.2468 -0.0559 -0.1066 0.0116  300  ARG A CG    
2060 C CD    . ARG A 117 ? 0.5134 0.1679 0.2849 -0.0549 -0.1174 0.0186  300  ARG A CD    
2061 N NE    . ARG A 117 ? 0.5247 0.1771 0.2838 -0.0823 -0.1402 0.0303  300  ARG A NE    
2062 C CZ    . ARG A 117 ? 0.4901 0.1962 0.2500 -0.0590 -0.1452 0.0316  300  ARG A CZ    
2063 N NH1   . ARG A 117 ? 0.4686 0.2109 0.2403 -0.0376 -0.1419 0.0003  300  ARG A NH1   
2064 N NH2   . ARG A 117 ? 0.5053 0.1994 0.2543 -0.0677 -0.1450 0.0399  300  ARG A NH2   
2078 N N     . ASP A 118 ? 0.4068 0.1678 0.1748 -0.0362 -0.0838 -0.0008 301  ASP A N     
2079 C CA    . ASP A 118 ? 0.4220 0.1511 0.2101 -0.0227 -0.0816 0.0017  301  ASP A CA    
2080 C C     . ASP A 118 ? 0.4496 0.1424 0.2340 -0.0122 -0.1349 0.0087  301  ASP A C     
2081 O O     . ASP A 118 ? 0.4888 0.1388 0.2812 -0.0043 -0.1117 0.0087  301  ASP A O     
2082 C CB    . ASP A 118 ? 0.4108 0.1436 0.2331 -0.0204 -0.0662 -0.0104 301  ASP A CB    
2083 C CG    . ASP A 118 ? 0.3701 0.1418 0.2510 -0.0306 -0.1183 -0.0144 301  ASP A CG    
2084 O OD1   . ASP A 118 ? 0.3665 0.1224 0.2540 -0.0330 -0.1256 0.0017  301  ASP A OD1   
2085 O OD2   . ASP A 118 ? 0.3572 0.1644 0.2739 -0.0141 -0.1106 -0.0278 301  ASP A OD2   
2090 N N     . GLY A 119 ? 0.4404 0.1445 0.2348 -0.0302 -0.1554 0.0057  302  GLY A N     
2091 C CA    . GLY A 119 ? 0.4507 0.1489 0.2589 -0.0353 -0.1501 0.0200  302  GLY A CA    
2092 C C     . GLY A 119 ? 0.4112 0.1627 0.2533 -0.0495 -0.1450 0.0209  302  GLY A C     
2093 O O     . GLY A 119 ? 0.4166 0.1770 0.2617 -0.0802 -0.1576 0.0197  302  GLY A O     
2097 N N     . GLY A 120 ? 0.3219 0.1555 0.2371 -0.0174 -0.1320 0.0164  303  GLY A N     
2098 C CA    . GLY A 120 ? 0.2656 0.1597 0.2408 0.0017  -0.1151 0.0115  303  GLY A CA    
2099 C C     . GLY A 120 ? 0.2388 0.1494 0.2422 -0.0137 -0.1032 -0.0044 303  GLY A C     
2100 O O     . GLY A 120 ? 0.2545 0.1518 0.2468 -0.0211 -0.0909 0.0016  303  GLY A O     
2104 N N     . PRO A 121 ? 0.2530 0.1451 0.2321 -0.0152 -0.1099 -0.0205 304  PRO A N     
2105 C CA    . PRO A 121 ? 0.2245 0.1469 0.2321 -0.0093 -0.0872 -0.0077 304  PRO A CA    
2106 C C     . PRO A 121 ? 0.2137 0.1575 0.2399 0.0008  -0.0647 0.0028  304  PRO A C     
2107 O O     . PRO A 121 ? 0.2131 0.1750 0.2811 0.0060  -0.0234 0.0073  304  PRO A O     
2108 C CB    . PRO A 121 ? 0.2833 0.1616 0.2479 -0.0107 -0.1151 0.0078  304  PRO A CB    
2109 C CG    . PRO A 121 ? 0.2859 0.1683 0.2446 -0.0018 -0.1224 -0.0082 304  PRO A CG    
2110 C CD    . PRO A 121 ? 0.2683 0.1620 0.2544 -0.0198 -0.1131 -0.0160 304  PRO A CD    
2118 N N     . ARG A 122 ? 0.2333 0.1536 0.2600 0.0027  -0.0642 0.0272  305  ARG A N     
2119 C CA    . ARG A 122 ? 0.2780 0.1604 0.2317 0.0056  -0.0523 0.0112  305  ARG A CA    
2120 C C     . ARG A 122 ? 0.2383 0.1374 0.2598 -0.0128 -0.0813 0.0063  305  ARG A C     
2121 O O     . ARG A 122 ? 0.2415 0.1390 0.2839 -0.0071 -0.0869 0.0298  305  ARG A O     
2122 C CB    . ARG A 122 ? 0.3672 0.2134 0.1826 0.0413  -0.0218 0.0082  305  ARG A CB    
2123 C CG    . ARG A 122 ? 0.4657 0.2515 0.2233 0.0377  -0.0431 0.0169  305  ARG A CG    
2124 C CD    . ARG A 122 ? 0.5883 0.2749 0.2506 0.0317  -0.1115 0.0211  305  ARG A CD    
2125 N NE    . ARG A 122 ? 0.7019 0.2795 0.2865 0.0367  -0.1102 0.0000  305  ARG A NE    
2126 C CZ    . ARG A 122 ? 0.7673 0.2707 0.2677 0.0426  -0.1185 -0.0175 305  ARG A CZ    
2127 N NH1   . ARG A 122 ? 0.7468 0.2483 0.2599 -0.0048 -0.1234 -0.0099 305  ARG A NH1   
2128 N NH2   . ARG A 122 ? 0.8259 0.2833 0.2814 0.0809  -0.1084 -0.0223 305  ARG A NH2   
2142 N N     . ALA A 123 ? 0.2055 0.1305 0.2384 -0.0027 -0.0671 -0.0110 306  ALA A N     
2143 C CA    . ALA A 123 ? 0.1868 0.1139 0.2504 0.0022  -0.0653 -0.0017 306  ALA A CA    
2144 C C     . ALA A 123 ? 0.1835 0.1085 0.2504 0.0026  -0.0389 -0.0067 306  ALA A C     
2145 O O     . ALA A 123 ? 0.2166 0.1172 0.2958 -0.0116 -0.0697 -0.0254 306  ALA A O     
2146 C CB    . ALA A 123 ? 0.1790 0.1108 0.2643 -0.0052 -0.0883 -0.0111 306  ALA A CB    
2152 N N     . ASN A 124 ? 0.1728 0.0982 0.2719 0.0298  -0.0406 -0.0113 307  ASN A N     
2153 C CA    . ASN A 124 ? 0.1771 0.0961 0.2442 0.0168  -0.0230 -0.0163 307  ASN A CA    
2154 C C     . ASN A 124 ? 0.1265 0.0910 0.2445 0.0043  -0.0479 -0.0024 307  ASN A C     
2155 O O     . ASN A 124 ? 0.1141 0.0896 0.2563 0.0123  -0.0495 -0.0011 307  ASN A O     
2156 C CB    . ASN A 124 ? 0.1928 0.1183 0.2649 0.0141  0.0358  -0.0047 307  ASN A CB    
2157 C CG    . ASN A 124 ? 0.1728 0.1328 0.3236 0.0552  -0.0267 0.0061  307  ASN A CG    
2158 O OD1   . ASN A 124 ? 0.1207 0.1041 0.3341 0.0131  -0.0275 -0.0076 307  ASN A OD1   
2159 N ND2   . ASN A 124 ? 0.2199 0.1749 0.3809 0.0993  0.0007  0.0013  307  ASN A ND2   
2166 N N     . GLU A 125 ? 0.1423 0.0808 0.2640 -0.0009 -0.0678 -0.0170 308  GLU A N     
2167 C CA    . GLU A 125 ? 0.1393 0.0941 0.2627 -0.0144 -0.0755 -0.0054 308  GLU A CA    
2168 C C     . GLU A 125 ? 0.1016 0.0930 0.2497 -0.0115 -0.0669 -0.0053 308  GLU A C     
2169 O O     . GLU A 125 ? 0.0997 0.1041 0.2622 -0.0130 -0.0503 -0.0214 308  GLU A O     
2170 C CB    . GLU A 125 ? 0.1691 0.1123 0.2524 -0.0248 -0.0723 -0.0164 308  GLU A CB    
2171 C CG    . GLU A 125 ? 0.1914 0.1337 0.2975 -0.0269 -0.0474 -0.0071 308  GLU A CG    
2172 C CD    . GLU A 125 ? 0.2102 0.1785 0.3560 -0.0366 -0.0666 0.0309  308  GLU A CD    
2173 O OE1   . GLU A 125 ? 0.1915 0.2208 0.3737 -0.0363 -0.0724 0.0440  308  GLU A OE1   
2174 O OE2   . GLU A 125 ? 0.2588 0.1897 0.3911 -0.0197 -0.0095 0.0609  308  GLU A OE2   
2181 N N     . GLU A 126 ? 0.1045 0.0722 0.2572 0.0027  -0.0622 -0.0059 309  GLU A N     
2182 C CA    . GLU A 126 ? 0.1086 0.0859 0.2538 -0.0110 -0.0739 0.0025  309  GLU A CA    
2183 C C     . GLU A 126 ? 0.0965 0.0881 0.2648 -0.0074 -0.0645 0.0014  309  GLU A C     
2184 O O     . GLU A 126 ? 0.1152 0.0829 0.2750 -0.0057 -0.0570 -0.0119 309  GLU A O     
2185 C CB    . GLU A 126 ? 0.1050 0.0960 0.2558 -0.0012 -0.0762 -0.0091 309  GLU A CB    
2186 C CG    . GLU A 126 ? 0.1256 0.1050 0.2692 0.0087  -0.0926 -0.0050 309  GLU A CG    
2187 C CD    . GLU A 126 ? 0.1147 0.1264 0.3011 -0.0042 -0.0823 0.0113  309  GLU A CD    
2188 O OE1   . GLU A 126 ? 0.1173 0.1469 0.3184 0.0013  -0.0770 0.0270  309  GLU A OE1   
2189 O OE2   . GLU A 126 ? 0.1472 0.1377 0.3263 0.0079  -0.0861 0.0214  309  GLU A OE2   
2196 N N     . LEU A 127 ? 0.1001 0.0745 0.2663 0.0009  -0.0707 -0.0048 310  LEU A N     
2197 C CA    . LEU A 127 ? 0.0815 0.0709 0.2576 0.0018  -0.0500 -0.0093 310  LEU A CA    
2198 C C     . LEU A 127 ? 0.0878 0.0795 0.2668 -0.0057 -0.0444 -0.0126 310  LEU A C     
2199 O O     . LEU A 127 ? 0.0998 0.0811 0.2588 -0.0061 -0.0571 -0.0165 310  LEU A O     
2200 C CB    . LEU A 127 ? 0.0889 0.0924 0.2776 -0.0025 -0.0301 -0.0162 310  LEU A CB    
2201 C CG    . LEU A 127 ? 0.0920 0.1056 0.2625 0.0041  -0.0629 -0.0073 310  LEU A CG    
2202 C CD1   . LEU A 127 ? 0.1027 0.1025 0.2868 -0.0062 -0.0702 0.0027  310  LEU A CD1   
2203 C CD2   . LEU A 127 ? 0.0948 0.1182 0.2821 -0.0028 -0.0279 -0.0098 310  LEU A CD2   
2215 N N     . ARG A 128 ? 0.0870 0.0806 0.2662 0.0003  -0.0554 -0.0079 311  ARG A N     
2216 C CA    . ARG A 128 ? 0.0874 0.0863 0.2696 -0.0034 -0.0524 -0.0090 311  ARG A CA    
2217 C C     . ARG A 128 ? 0.0989 0.0937 0.2583 -0.0121 -0.0621 -0.0052 311  ARG A C     
2218 O O     . ARG A 128 ? 0.0977 0.1053 0.3006 0.0070  -0.0450 -0.0241 311  ARG A O     
2219 C CB    . ARG A 128 ? 0.1000 0.1028 0.2507 0.0013  -0.0723 -0.0130 311  ARG A CB    
2220 C CG    . ARG A 128 ? 0.1352 0.1176 0.2762 -0.0015 -0.0957 -0.0009 311  ARG A CG    
2221 C CD    . ARG A 128 ? 0.2020 0.1332 0.2890 -0.0138 -0.1154 0.0106  311  ARG A CD    
2222 N NE    . ARG A 128 ? 0.2740 0.1571 0.3183 -0.0271 -0.1376 0.0120  311  ARG A NE    
2223 C CZ    . ARG A 128 ? 0.3140 0.1725 0.3891 -0.0361 -0.1593 0.0236  311  ARG A CZ    
2224 N NH1   . ARG A 128 ? 0.2460 0.1666 0.4140 -0.0369 -0.1698 0.0279  311  ARG A NH1   
2225 N NH2   . ARG A 128 ? 0.3330 0.1859 0.4122 -0.0400 -0.1697 0.0355  311  ARG A NH2   
2239 N N     . ALA A 129 ? 0.1060 0.0862 0.2642 -0.0192 -0.0476 -0.0038 312  ALA A N     
2240 C CA    . ALA A 129 ? 0.1477 0.0966 0.2758 -0.0350 -0.0456 -0.0145 312  ALA A CA    
2241 C C     . ALA A 129 ? 0.1379 0.0990 0.2741 -0.0276 -0.0692 -0.0047 312  ALA A C     
2242 O O     . ALA A 129 ? 0.1532 0.1190 0.2822 -0.0224 -0.0479 -0.0201 312  ALA A O     
2243 C CB    . ALA A 129 ? 0.1774 0.1003 0.2689 -0.0426 -0.0166 -0.0133 312  ALA A CB    
2249 N N     . LYS A 130 ? 0.1157 0.0848 0.2599 -0.0157 -0.0579 -0.0093 313  LYS A N     
2250 C CA    . LYS A 130 ? 0.1194 0.0869 0.2546 -0.0235 -0.0485 -0.0090 313  LYS A CA    
2251 C C     . LYS A 130 ? 0.0935 0.1060 0.2511 -0.0209 -0.0400 -0.0248 313  LYS A C     
2252 O O     . LYS A 130 ? 0.1383 0.1130 0.2648 -0.0150 -0.0502 -0.0463 313  LYS A O     
2253 C CB    . LYS A 130 ? 0.1228 0.0834 0.2674 -0.0155 -0.0621 -0.0065 313  LYS A CB    
2254 C CG    . LYS A 130 ? 0.1262 0.0969 0.2839 -0.0201 -0.0805 0.0134  313  LYS A CG    
2255 C CD    . LYS A 130 ? 0.1344 0.1285 0.3135 -0.0204 -0.0408 -0.0036 313  LYS A CD    
2256 C CE    . LYS A 130 ? 0.1728 0.1564 0.2882 -0.0324 -0.0563 -0.0001 313  LYS A CE    
2257 N NZ    . LYS A 130 ? 0.2183 0.1972 0.2733 -0.0434 -0.0611 0.0065  313  LYS A NZ    
2271 N N     . LEU A 131 ? 0.1008 0.0994 0.2687 -0.0125 -0.0586 -0.0148 314  LEU A N     
2272 C CA    . LEU A 131 ? 0.0951 0.0964 0.2863 -0.0064 -0.0562 -0.0109 314  LEU A CA    
2273 C C     . LEU A 131 ? 0.1056 0.0986 0.2935 -0.0187 -0.0461 -0.0090 314  LEU A C     
2274 O O     . LEU A 131 ? 0.1014 0.0883 0.3022 -0.0035 -0.0461 -0.0099 314  LEU A O     
2275 C CB    . LEU A 131 ? 0.0829 0.0926 0.2853 -0.0053 -0.0368 -0.0068 314  LEU A CB    
2276 C CG    . LEU A 131 ? 0.0902 0.1047 0.2695 0.0038  -0.0219 -0.0149 314  LEU A CG    
2277 C CD1   . LEU A 131 ? 0.1210 0.1178 0.2810 0.0242  -0.0234 -0.0160 314  LEU A CD1   
2278 C CD2   . LEU A 131 ? 0.1090 0.1089 0.3281 -0.0246 -0.0112 -0.0168 314  LEU A CD2   
2290 N N     . ARG A 132 ? 0.1075 0.1019 0.3127 -0.0180 -0.0319 -0.0228 315  ARG A N     
2291 C CA    . ARG A 132 ? 0.1115 0.1091 0.2976 -0.0170 -0.0082 -0.0338 315  ARG A CA    
2292 C C     . ARG A 132 ? 0.1478 0.1087 0.2769 -0.0209 0.0098  -0.0433 315  ARG A C     
2293 O O     . ARG A 132 ? 0.1582 0.1215 0.3162 -0.0299 -0.0052 -0.0502 315  ARG A O     
2294 C CB    . ARG A 132 ? 0.1308 0.1312 0.3282 -0.0299 -0.0334 -0.0469 315  ARG A CB    
2295 C CG    . ARG A 132 ? 0.1415 0.1379 0.3867 -0.0257 -0.0515 -0.0365 315  ARG A CG    
2296 C CD    . ARG A 132 ? 0.1474 0.1463 0.4509 -0.0266 -0.0467 -0.0072 315  ARG A CD    
2297 N NE    . ARG A 132 ? 0.1692 0.1671 0.4910 -0.0233 -0.0286 -0.0162 315  ARG A NE    
2298 C CZ    . ARG A 132 ? 0.1726 0.1654 0.5039 -0.0177 0.0143  -0.0366 315  ARG A CZ    
2299 N NH1   . ARG A 132 ? 0.1752 0.1752 0.5157 -0.0454 0.0114  -0.0217 315  ARG A NH1   
2300 N NH2   . ARG A 132 ? 0.1554 0.1749 0.5068 0.0148  -0.0064 -0.0489 315  ARG A NH2   
2314 N N     . GLU A 133 ? 0.1618 0.1186 0.2698 0.0002  0.0138  -0.0134 316  GLU A N     
2315 C CA    . GLU A 133 ? 0.1847 0.1423 0.2744 0.0087  0.0182  -0.0074 316  GLU A CA    
2316 C C     . GLU A 133 ? 0.1736 0.1458 0.2876 -0.0089 -0.0163 -0.0183 316  GLU A C     
2317 O O     . GLU A 133 ? 0.2912 0.1698 0.2974 -0.0118 -0.0085 -0.0240 316  GLU A O     
2318 C CB    . GLU A 133 ? 0.2896 0.1881 0.2858 0.0561  -0.0209 -0.0118 316  GLU A CB    
2319 C CG    . GLU A 133 ? 0.4173 0.2445 0.3278 0.0845  -0.0382 -0.0138 316  GLU A CG    
2320 C CD    . GLU A 133 ? 0.4912 0.3000 0.4126 0.1118  -0.0852 -0.0140 316  GLU A CD    
2321 O OE1   . GLU A 133 ? 0.4900 0.3376 0.4770 0.1466  -0.1114 -0.0023 316  GLU A OE1   
2322 O OE2   . GLU A 133 ? 0.5459 0.3087 0.4372 0.1031  -0.1025 -0.0085 316  GLU A OE2   
2329 N N     . HIS A 134 ? 0.0972 0.1311 0.2625 -0.0276 -0.0420 -0.0110 317  HIS A N     
2330 C CA    A HIS A 134 ? 0.1034 0.1307 0.2608 -0.0305 -0.0548 -0.0084 317  HIS A CA    
2331 C CA    B HIS A 134 ? 0.1051 0.1321 0.2642 -0.0308 -0.0551 -0.0106 317  HIS A CA    
2332 C C     . HIS A 134 ? 0.1140 0.1356 0.2661 -0.0255 -0.0523 -0.0160 317  HIS A C     
2333 O O     . HIS A 134 ? 0.1430 0.1460 0.3039 -0.0307 -0.0900 -0.0074 317  HIS A O     
2334 C CB    A HIS A 134 ? 0.1031 0.1275 0.2628 -0.0236 -0.0611 0.0061  317  HIS A CB    
2335 C CB    B HIS A 134 ? 0.1212 0.1280 0.2773 -0.0251 -0.0661 -0.0013 317  HIS A CB    
2336 C CG    A HIS A 134 ? 0.0975 0.1428 0.2622 -0.0231 -0.0612 0.0033  317  HIS A CG    
2337 C CG    B HIS A 134 ? 0.1588 0.1310 0.2989 -0.0240 -0.0803 -0.0032 317  HIS A CG    
2338 N ND1   A HIS A 134 ? 0.0851 0.1605 0.2810 -0.0145 -0.0443 0.0144  317  HIS A ND1   
2339 N ND1   B HIS A 134 ? 0.2031 0.1361 0.3062 -0.0371 -0.0969 -0.0103 317  HIS A ND1   
2340 C CD2   A HIS A 134 ? 0.1114 0.1525 0.2601 -0.0266 -0.0705 -0.0133 317  HIS A CD2   
2341 C CD2   B HIS A 134 ? 0.1429 0.1270 0.3092 -0.0074 -0.0755 -0.0012 317  HIS A CD2   
2342 C CE1   A HIS A 134 ? 0.1281 0.1639 0.2941 -0.0231 -0.0795 0.0025  317  HIS A CE1   
2343 C CE1   B HIS A 134 ? 0.1745 0.1268 0.3083 -0.0328 -0.0956 0.0022  317  HIS A CE1   
2344 N NE2   A HIS A 134 ? 0.1265 0.1645 0.2993 -0.0272 -0.0750 -0.0162 317  HIS A NE2   
2345 N NE2   B HIS A 134 ? 0.1332 0.1203 0.3032 -0.0141 -0.0833 0.0042  317  HIS A NE2   
2360 N N     . GLY A 135 ? 0.1036 0.1275 0.3042 -0.0083 -0.0546 -0.0386 318  GLY A N     
2361 C CA    . GLY A 135 ? 0.1115 0.1263 0.3002 -0.0004 -0.0547 -0.0490 318  GLY A CA    
2362 C C     . GLY A 135 ? 0.0860 0.1137 0.2949 0.0034  -0.0431 -0.0297 318  GLY A C     
2363 O O     . GLY A 135 ? 0.1012 0.1228 0.3243 0.0119  -0.0585 -0.0209 318  GLY A O     
2367 N N     . VAL A 136 ? 0.0906 0.1124 0.2837 -0.0031 -0.0216 -0.0364 319  VAL A N     
2368 C CA    . VAL A 136 ? 0.0770 0.1109 0.2844 -0.0061 -0.0190 -0.0168 319  VAL A CA    
2369 C C     . VAL A 136 ? 0.0807 0.1092 0.2760 -0.0103 -0.0382 0.0032  319  VAL A C     
2370 O O     . VAL A 136 ? 0.0907 0.1119 0.2728 -0.0033 -0.0479 -0.0006 319  VAL A O     
2371 C CB    . VAL A 136 ? 0.0756 0.1171 0.2807 -0.0060 -0.0253 -0.0104 319  VAL A CB    
2372 C CG1   . VAL A 136 ? 0.1209 0.1382 0.2947 -0.0308 -0.0093 0.0034  319  VAL A CG1   
2373 C CG2   . VAL A 136 ? 0.0988 0.1094 0.2981 -0.0144 -0.0318 -0.0233 319  VAL A CG2   
2383 N N     . GLU A 137 ? 0.1039 0.1090 0.3008 -0.0054 -0.0688 -0.0029 320  GLU A N     
2384 C CA    . GLU A 137 ? 0.0973 0.1203 0.2901 -0.0140 -0.0568 -0.0055 320  GLU A CA    
2385 C C     . GLU A 137 ? 0.1321 0.1218 0.2784 -0.0049 -0.0829 0.0118  320  GLU A C     
2386 O O     . GLU A 137 ? 0.1987 0.1178 0.3054 -0.0066 -0.0869 0.0177  320  GLU A O     
2387 C CB    . GLU A 137 ? 0.1419 0.1486 0.2988 -0.0440 -0.0597 -0.0037 320  GLU A CB    
2388 C CG    . GLU A 137 ? 0.1821 0.1953 0.3165 -0.0681 -0.0735 0.0011  320  GLU A CG    
2389 C CD    . GLU A 137 ? 0.1953 0.2571 0.3978 -0.0725 -0.0400 -0.0400 320  GLU A CD    
2390 O OE1   . GLU A 137 ? 0.1698 0.2880 0.4277 -0.0554 -0.0456 -0.0536 320  GLU A OE1   
2391 O OE2   . GLU A 137 ? 0.2216 0.2910 0.4835 -0.0978 0.0267  -0.0614 320  GLU A OE2   
2398 N N     . VAL A 138 ? 0.1370 0.1391 0.2891 0.0129  -0.0484 0.0416  321  VAL A N     
2399 C CA    . VAL A 138 ? 0.1404 0.1819 0.2770 0.0084  -0.0557 0.0446  321  VAL A CA    
2400 C C     . VAL A 138 ? 0.1710 0.2447 0.2954 0.0023  -0.0736 0.0482  321  VAL A C     
2401 O O     . VAL A 138 ? 0.1789 0.2440 0.3193 -0.0339 -0.1065 0.0313  321  VAL A O     
2402 C CB    . VAL A 138 ? 0.1418 0.1881 0.2698 -0.0107 -0.0609 0.0117  321  VAL A CB    
2403 C CG1   . VAL A 138 ? 0.1962 0.2180 0.2518 -0.0167 -0.0325 -0.0031 321  VAL A CG1   
2404 C CG2   . VAL A 138 ? 0.1436 0.1738 0.3193 -0.0201 -0.0677 -0.0207 321  VAL A CG2   
2414 N N     . LYS A 139 ? 0.1879 0.3044 0.3078 0.0294  -0.0909 0.0790  322  LYS A N     
2415 C CA    . LYS A 139 ? 0.2385 0.3488 0.3574 0.0296  -0.1121 0.0847  322  LYS A CA    
2416 C C     . LYS A 139 ? 0.2246 0.3433 0.3209 -0.0487 -0.1286 0.0839  322  LYS A C     
2417 O O     . LYS A 139 ? 0.2048 0.3482 0.2754 -0.0518 -0.0975 0.0534  322  LYS A O     
2418 C CB    . LYS A 139 ? 0.3531 0.3782 0.4305 0.1048  -0.0715 0.0871  322  LYS A CB    
2419 C CG    . LYS A 139 ? 0.4393 0.3962 0.4836 0.1450  -0.0356 0.0838  322  LYS A CG    
2420 C CD    . LYS A 139 ? 0.5373 0.4081 0.4968 0.1398  0.0176  0.0821  322  LYS A CD    
2421 C CE    . LYS A 139 ? 0.5333 0.4171 0.4921 0.1321  -0.0006 0.0921  322  LYS A CE    
2422 N NZ    . LYS A 139 ? 0.4991 0.4253 0.4796 0.1280  -0.0112 0.0911  322  LYS A NZ    
2436 N N     . PRO A 140 ? 0.2783 0.3258 0.3579 -0.1065 -0.1342 0.1032  323  PRO A N     
2437 C CA    . PRO A 140 ? 0.3324 0.3073 0.3820 -0.1221 -0.1407 0.0949  323  PRO A CA    
2438 C C     . PRO A 140 ? 0.3330 0.2856 0.3573 -0.1076 -0.1620 0.0990  323  PRO A C     
2439 O O     . PRO A 140 ? 0.3636 0.2928 0.3917 -0.0794 -0.1432 0.1296  323  PRO A O     
2440 C CB    . PRO A 140 ? 0.3974 0.3214 0.4265 -0.1183 -0.1197 0.0904  323  PRO A CB    
2441 C CG    . PRO A 140 ? 0.4210 0.3375 0.4343 -0.1064 -0.1096 0.0902  323  PRO A CG    
2442 C CD    . PRO A 140 ? 0.3605 0.3330 0.3986 -0.0999 -0.1178 0.1148  323  PRO A CD    
2450 N N     . VAL A 141 ? 0.3452 0.2658 0.3120 -0.1107 -0.1816 0.0952  324  VAL A N     
2451 C CA    . VAL A 141 ? 0.3923 0.2674 0.3358 -0.1231 -0.1455 0.0902  324  VAL A CA    
2452 C C     . VAL A 141 ? 0.3867 0.2450 0.3336 -0.1077 -0.1761 0.0653  324  VAL A C     
2453 O O     . VAL A 141 ? 0.3971 0.2232 0.3247 -0.0678 -0.1980 0.0673  324  VAL A O     
2454 C CB    . VAL A 141 ? 0.4178 0.3162 0.3532 -0.1278 -0.1166 0.0813  324  VAL A CB    
2455 C CG1   . VAL A 141 ? 0.4977 0.3465 0.3992 -0.0957 -0.0603 0.0784  324  VAL A CG1   
2456 C CG2   . VAL A 141 ? 0.3395 0.3257 0.3947 -0.1570 -0.1432 0.0401  324  VAL A CG2   
2466 N N     . GLU A 142 ? 0.3941 0.2672 0.3416 -0.1067 -0.1798 0.0595  325  GLU A N     
2467 C CA    . GLU A 142 ? 0.4073 0.2853 0.3274 -0.1152 -0.1807 0.0606  325  GLU A CA    
2468 C C     . GLU A 142 ? 0.3705 0.2722 0.3044 -0.0837 -0.1911 0.0671  325  GLU A C     
2469 O O     . GLU A 142 ? 0.3231 0.2725 0.3072 -0.0700 -0.1684 0.0743  325  GLU A O     
2470 C CB    . GLU A 142 ? 0.4290 0.3161 0.3716 -0.1517 -0.1884 0.0583  325  GLU A CB    
2471 C CG    . GLU A 142 ? 0.4809 0.3456 0.4354 -0.1524 -0.2145 0.0375  325  GLU A CG    
2472 C CD    . GLU A 142 ? 0.5775 0.3703 0.4958 -0.1223 -0.1865 0.0118  325  GLU A CD    
2473 O OE1   . GLU A 142 ? 0.5783 0.3791 0.4808 -0.1020 -0.2281 -0.0110 325  GLU A OE1   
2474 O OE2   . GLU A 142 ? 0.6268 0.3805 0.5507 -0.1166 -0.1671 -0.0047 325  GLU A OE2   
2481 N N     . GLU A 143 ? 0.4149 0.2741 0.3196 -0.0931 -0.2028 0.0670  326  GLU A N     
2482 C CA    . GLU A 143 ? 0.4208 0.2960 0.3234 -0.0959 -0.1994 0.0745  326  GLU A CA    
2483 C C     . GLU A 143 ? 0.3285 0.2624 0.3503 -0.0899 -0.1928 0.0770  326  GLU A C     
2484 O O     . GLU A 143 ? 0.3586 0.2529 0.3930 -0.0858 -0.2164 0.0819  326  GLU A O     
2485 C CB    . GLU A 143 ? 0.5021 0.3584 0.3204 -0.0993 -0.1706 0.0577  326  GLU A CB    
2486 C CG    . GLU A 143 ? 0.5864 0.4208 0.3277 -0.0886 -0.1205 0.0343  326  GLU A CG    
2487 C CD    . GLU A 143 ? 0.6636 0.4767 0.3743 -0.0725 -0.0904 -0.0022 326  GLU A CD    
2488 O OE1   . GLU A 143 ? 0.6951 0.4851 0.3626 -0.0813 -0.0898 -0.0576 326  GLU A OE1   
2489 O OE2   . GLU A 143 ? 0.6897 0.5120 0.4138 -0.0548 -0.0939 0.0100  326  GLU A OE2   
2496 N N     . PRO A 144 ? 0.3036 0.2578 0.3478 -0.1000 -0.1729 0.0665  327  PRO A N     
2497 C CA    . PRO A 144 ? 0.3015 0.2532 0.3352 -0.0919 -0.1773 0.0743  327  PRO A CA    
2498 C C     . PRO A 144 ? 0.3538 0.2521 0.3441 -0.1194 -0.1889 0.0939  327  PRO A C     
2499 O O     . PRO A 144 ? 0.4275 0.2471 0.3477 -0.1427 -0.1859 0.0984  327  PRO A O     
2500 C CB    . PRO A 144 ? 0.2718 0.2465 0.3418 -0.0967 -0.1583 0.0629  327  PRO A CB    
2501 C CG    . PRO A 144 ? 0.3124 0.2516 0.3601 -0.1092 -0.1615 0.0464  327  PRO A CG    
2502 C CD    . PRO A 144 ? 0.3066 0.2556 0.3567 -0.1071 -0.1668 0.0488  327  PRO A CD    
2510 N N     . GLU A 145 ? 0.3583 0.2636 0.3881 -0.1199 -0.2050 0.1056  328  GLU A N     
2511 C CA    . GLU A 145 ? 0.3750 0.2797 0.4120 -0.1282 -0.2169 0.1233  328  GLU A CA    
2512 C C     . GLU A 145 ? 0.3870 0.2618 0.3753 -0.1348 -0.2051 0.1080  328  GLU A C     
2513 O O     . GLU A 145 ? 0.4430 0.2571 0.4132 -0.1418 -0.2162 0.1024  328  GLU A O     
2514 C CB    . GLU A 145 ? 0.4247 0.3251 0.4734 -0.1484 -0.2439 0.1559  328  GLU A CB    
2515 C CG    . GLU A 145 ? 0.5431 0.3867 0.5388 -0.1491 -0.2479 0.1852  328  GLU A CG    
2516 C CD    . GLU A 145 ? 0.6816 0.4556 0.6096 -0.1180 -0.2126 0.2040  328  GLU A CD    
2517 O OE1   . GLU A 145 ? 0.7239 0.4886 0.6220 -0.0862 -0.2636 0.2137  328  GLU A OE1   
2518 O OE2   . GLU A 145 ? 0.7315 0.4791 0.6614 -0.1264 -0.1624 0.1946  328  GLU A OE2   
2525 N N     . TRP A 146 ? 0.3652 0.2448 0.3518 -0.1266 -0.1904 0.0949  329  TRP A N     
2526 C CA    . TRP A 146 ? 0.3684 0.2243 0.3424 -0.1149 -0.1906 0.0811  329  TRP A CA    
2527 C C     . TRP A 146 ? 0.4070 0.2237 0.3300 -0.1090 -0.1975 0.0761  329  TRP A C     
2528 O O     . TRP A 146 ? 0.4303 0.2292 0.3249 -0.1233 -0.2069 0.0890  329  TRP A O     
2529 C CB    . TRP A 146 ? 0.3500 0.2096 0.3498 -0.1026 -0.1938 0.0861  329  TRP A CB    
2530 C CG    . TRP A 146 ? 0.3569 0.2053 0.3377 -0.0901 -0.1984 0.0737  329  TRP A CG    
2531 C CD1   . TRP A 146 ? 0.4181 0.2154 0.3314 -0.0979 -0.1855 0.0634  329  TRP A CD1   
2532 C CD2   . TRP A 146 ? 0.3862 0.2135 0.3450 -0.0774 -0.2120 0.0593  329  TRP A CD2   
2533 N NE1   . TRP A 146 ? 0.4469 0.2199 0.3502 -0.0703 -0.2045 0.0362  329  TRP A NE1   
2534 C CE2   . TRP A 146 ? 0.4376 0.2190 0.3616 -0.0700 -0.1954 0.0499  329  TRP A CE2   
2535 C CE3   . TRP A 146 ? 0.3900 0.2190 0.3564 -0.0971 -0.2023 0.0543  329  TRP A CE3   
2536 C CZ2   . TRP A 146 ? 0.4603 0.2240 0.3906 -0.0862 -0.1845 0.0450  329  TRP A CZ2   
2537 C CZ3   . TRP A 146 ? 0.4217 0.2215 0.3791 -0.0816 -0.2134 0.0433  329  TRP A CZ3   
2538 C CH2   . TRP A 146 ? 0.4520 0.2206 0.3979 -0.0793 -0.1981 0.0431  329  TRP A CH2   
2549 N N     . LYS A 147 ? 0.3421 0.2207 0.3123 -0.0929 -0.1858 0.0741  330  LYS A N     
2550 C CA    . LYS A 147 ? 0.3330 0.2378 0.3322 -0.0842 -0.1910 0.0752  330  LYS A CA    
2551 C C     . LYS A 147 ? 0.3413 0.2247 0.3353 -0.0781 -0.1959 0.0746  330  LYS A C     
2552 O O     . LYS A 147 ? 0.3731 0.2138 0.3476 -0.0537 -0.2122 0.0557  330  LYS A O     
2553 C CB    . LYS A 147 ? 0.3397 0.2878 0.3862 -0.0799 -0.2081 0.0788  330  LYS A CB    
2554 C CG    . LYS A 147 ? 0.3403 0.3438 0.4337 -0.0296 -0.2169 0.0878  330  LYS A CG    
2555 C CD    . LYS A 147 ? 0.4006 0.4012 0.5219 -0.0025 -0.2252 0.1006  330  LYS A CD    
2556 C CE    . LYS A 147 ? 0.4173 0.4383 0.5874 0.0110  -0.2324 0.0984  330  LYS A CE    
2557 N NZ    . LYS A 147 ? 0.4210 0.4555 0.6238 -0.0084 -0.2300 0.0933  330  LYS A NZ    
2571 N N     . MET A 148 ? 0.3540 0.2340 0.3382 -0.0987 -0.1957 0.0769  331  MET A N     
2572 C CA    . MET A 148 ? 0.3502 0.2379 0.3340 -0.0994 -0.1929 0.0791  331  MET A CA    
2573 C C     . MET A 148 ? 0.3329 0.2573 0.3352 -0.0946 -0.1886 0.0725  331  MET A C     
2574 O O     . MET A 148 ? 0.3954 0.2948 0.3423 -0.0908 -0.2085 0.0441  331  MET A O     
2575 C CB    . MET A 148 ? 0.3380 0.2304 0.3437 -0.1003 -0.1884 0.0719  331  MET A CB    
2576 C CG    . MET A 148 ? 0.3284 0.2195 0.3629 -0.1024 -0.1839 0.0822  331  MET A CG    
2577 S SD    . MET A 148 ? 0.3116 0.1921 0.3612 -0.0818 -0.1903 0.0824  331  MET A SD    
2578 C CE    . MET A 148 ? 0.2874 0.1725 0.3775 -0.0647 -0.1873 0.0760  331  MET A CE    
2588 N N     . VAL A 149 ? 0.3038 0.2561 0.3730 -0.0818 -0.1901 0.0921  332  VAL A N     
2589 C CA    . VAL A 149 ? 0.3044 0.2736 0.4359 -0.0738 -0.2009 0.1121  332  VAL A CA    
2590 C C     . VAL A 149 ? 0.3562 0.2629 0.4136 -0.0810 -0.2185 0.1063  332  VAL A C     
2591 O O     . VAL A 149 ? 0.3819 0.2754 0.4074 -0.0683 -0.2264 0.0960  332  VAL A O     
2592 C CB    . VAL A 149 ? 0.2857 0.3064 0.5181 -0.0454 -0.1849 0.1428  332  VAL A CB    
2593 C CG1   . VAL A 149 ? 0.3312 0.3294 0.5739 -0.0291 -0.1691 0.1421  332  VAL A CG1   
2594 C CG2   . VAL A 149 ? 0.3558 0.3172 0.5586 -0.0469 -0.1447 0.1540  332  VAL A CG2   
2604 N N     . ASP A 150 ? 0.3647 0.2310 0.3975 -0.1063 -0.2164 0.1134  333  ASP A N     
2605 C CA    . ASP A 150 ? 0.3737 0.2276 0.4071 -0.0889 -0.2243 0.1019  333  ASP A CA    
2606 C C     . ASP A 150 ? 0.3702 0.2184 0.3741 -0.1043 -0.2123 0.1012  333  ASP A C     
2607 O O     . ASP A 150 ? 0.3720 0.2049 0.3696 -0.0993 -0.2128 0.0993  333  ASP A O     
2608 C CB    . ASP A 150 ? 0.3964 0.2465 0.4238 -0.0542 -0.2303 0.0953  333  ASP A CB    
2609 C CG    . ASP A 150 ? 0.3869 0.2683 0.4724 -0.0187 -0.2403 0.0760  333  ASP A CG    
2610 O OD1   . ASP A 150 ? 0.3537 0.2486 0.4571 -0.0394 -0.2261 0.0875  333  ASP A OD1   
2611 O OD2   . ASP A 150 ? 0.4110 0.3028 0.5297 0.0469  -0.2359 0.0650  333  ASP A OD2   
2616 N N     . ASP A 151 ? 0.3736 0.2268 0.3404 -0.1069 -0.1931 0.1130  334  ASP A N     
2617 C CA    . ASP A 151 ? 0.3786 0.2375 0.3285 -0.1061 -0.1962 0.1053  334  ASP A CA    
2618 C C     . ASP A 151 ? 0.3207 0.2134 0.3058 -0.0758 -0.1799 0.0778  334  ASP A C     
2619 O O     . ASP A 151 ? 0.2869 0.2118 0.3215 -0.0481 -0.1752 0.0692  334  ASP A O     
2620 C CB    . ASP A 151 ? 0.3874 0.2677 0.3610 -0.1233 -0.2059 0.1270  334  ASP A CB    
2621 C CG    . ASP A 151 ? 0.4342 0.2985 0.3802 -0.1272 -0.2103 0.1261  334  ASP A CG    
2622 O OD1   . ASP A 151 ? 0.4441 0.3122 0.3940 -0.1249 -0.2106 0.1276  334  ASP A OD1   
2623 O OD2   . ASP A 151 ? 0.4548 0.3125 0.3876 -0.1235 -0.2039 0.1299  334  ASP A OD2   
2628 N N     . ASP A 152 ? 0.3353 0.1874 0.3287 -0.0828 -0.1877 0.0894  335  ASP A N     
2629 C CA    . ASP A 152 ? 0.3241 0.1759 0.3742 -0.0720 -0.1976 0.0756  335  ASP A CA    
2630 C C     . ASP A 152 ? 0.2828 0.1700 0.3517 -0.0518 -0.1808 0.0719  335  ASP A C     
2631 O O     . ASP A 152 ? 0.2854 0.1838 0.3618 -0.0543 -0.1860 0.0637  335  ASP A O     
2632 C CB    . ASP A 152 ? 0.3284 0.1721 0.4030 -0.0596 -0.2088 0.0738  335  ASP A CB    
2633 C CG    . ASP A 152 ? 0.3100 0.1722 0.4136 -0.0586 -0.2059 0.0761  335  ASP A CG    
2634 O OD1   . ASP A 152 ? 0.3241 0.1734 0.3929 -0.0673 -0.2030 0.0757  335  ASP A OD1   
2635 O OD2   . ASP A 152 ? 0.3612 0.1908 0.4504 -0.0592 -0.2279 0.0814  335  ASP A OD2   
2640 N N     . THR A 153 ? 0.2736 0.1686 0.3645 -0.0421 -0.1771 0.0715  336  THR A N     
2641 C CA    . THR A 153 ? 0.2710 0.1908 0.3662 -0.0369 -0.1784 0.0684  336  THR A CA    
2642 C C     . THR A 153 ? 0.2588 0.1905 0.3366 -0.0461 -0.1674 0.0732  336  THR A C     
2643 O O     . THR A 153 ? 0.2769 0.1951 0.3165 -0.0565 -0.1701 0.0739  336  THR A O     
2644 C CB    . THR A 153 ? 0.3158 0.2087 0.4342 -0.0022 -0.1814 0.0730  336  THR A CB    
2645 O OG1   . THR A 153 ? 0.3207 0.2245 0.4765 0.0109  -0.1785 0.0875  336  THR A OG1   
2646 C CG2   . THR A 153 ? 0.3457 0.2117 0.4537 0.0175  -0.1699 0.0557  336  THR A CG2   
2654 N N     . LEU A 154 ? 0.2208 0.1805 0.3250 -0.0474 -0.1486 0.0750  337  LEU A N     
2655 C CA    . LEU A 154 ? 0.2036 0.1821 0.3192 -0.0383 -0.1397 0.0686  337  LEU A CA    
2656 C C     . LEU A 154 ? 0.2144 0.1996 0.3450 -0.0234 -0.1479 0.0634  337  LEU A C     
2657 O O     . LEU A 154 ? 0.2114 0.2089 0.3816 -0.0148 -0.1506 0.0560  337  LEU A O     
2658 C CB    . LEU A 154 ? 0.2069 0.1748 0.3054 -0.0370 -0.1403 0.0626  337  LEU A CB    
2659 C CG    . LEU A 154 ? 0.2163 0.1715 0.2823 -0.0261 -0.1395 0.0555  337  LEU A CG    
2660 C CD1   . LEU A 154 ? 0.2306 0.1720 0.3146 -0.0349 -0.1371 0.0573  337  LEU A CD1   
2661 C CD2   . LEU A 154 ? 0.2307 0.1776 0.2684 -0.0214 -0.1104 0.0378  337  LEU A CD2   
2673 N N     . GLU A 155 ? 0.2306 0.2135 0.3543 -0.0284 -0.1574 0.0679  338  GLU A N     
2674 C CA    . GLU A 155 ? 0.2533 0.2395 0.3857 -0.0233 -0.1684 0.0806  338  GLU A CA    
2675 C C     . GLU A 155 ? 0.2663 0.2189 0.3654 -0.0441 -0.1755 0.0778  338  GLU A C     
2676 O O     . GLU A 155 ? 0.3001 0.2067 0.3673 -0.0758 -0.1890 0.0789  338  GLU A O     
2677 C CB    . GLU A 155 ? 0.2857 0.2962 0.4865 -0.0118 -0.1849 0.1103  338  GLU A CB    
2678 C CG    . GLU A 155 ? 0.3726 0.3600 0.5811 0.0123  -0.2286 0.1107  338  GLU A CG    
2679 C CD    . GLU A 155 ? 0.5073 0.4142 0.6477 0.0033  -0.2378 0.0986  338  GLU A CD    
2680 O OE1   . GLU A 155 ? 0.5394 0.4273 0.6667 0.0151  -0.2379 0.1101  338  GLU A OE1   
2681 O OE2   . GLU A 155 ? 0.5616 0.4444 0.6830 -0.0185 -0.2405 0.0798  338  GLU A OE2   
2688 N N     . VAL A 156 ? 0.2499 0.2122 0.3679 -0.0522 -0.1656 0.0857  339  VAL A N     
2689 C CA    . VAL A 156 ? 0.2303 0.2176 0.3638 -0.0524 -0.1577 0.0827  339  VAL A CA    
2690 C C     . VAL A 156 ? 0.2358 0.2420 0.4026 -0.0616 -0.1584 0.1009  339  VAL A C     
2691 O O     . VAL A 156 ? 0.2159 0.2477 0.4144 -0.0524 -0.1448 0.1124  339  VAL A O     
2692 C CB    . VAL A 156 ? 0.2209 0.2161 0.3390 -0.0460 -0.1506 0.0729  339  VAL A CB    
2693 C CG1   . VAL A 156 ? 0.2573 0.2271 0.3364 -0.0437 -0.1690 0.0604  339  VAL A CG1   
2694 C CG2   . VAL A 156 ? 0.2268 0.2108 0.3150 -0.0455 -0.1395 0.0704  339  VAL A CG2   
2704 N N     . ASP A 157 ? 0.2266 0.2603 0.4513 -0.0785 -0.1494 0.1168  340  ASP A N     
2705 C CA    . ASP A 157 ? 0.2201 0.2904 0.5163 -0.0742 -0.1374 0.1367  340  ASP A CA    
2706 C C     . ASP A 157 ? 0.2393 0.3068 0.5382 -0.0540 -0.1273 0.1511  340  ASP A C     
2707 O O     . ASP A 157 ? 0.2756 0.3172 0.5624 -0.0373 -0.1140 0.1634  340  ASP A O     
2708 C CB    . ASP A 157 ? 0.2293 0.3029 0.5446 -0.0710 -0.1249 0.1487  340  ASP A CB    
2709 C CG    . ASP A 157 ? 0.2744 0.3200 0.5713 -0.0685 -0.1710 0.1476  340  ASP A CG    
2710 O OD1   . ASP A 157 ? 0.3025 0.3395 0.5572 -0.0739 -0.1957 0.1375  340  ASP A OD1   
2711 O OD2   . ASP A 157 ? 0.3062 0.3109 0.6121 -0.0518 -0.1863 0.1587  340  ASP A OD2   
2716 N N     . GLY A 158 ? 0.2303 0.3122 0.5361 -0.0543 -0.1549 0.1340  341  GLY A N     
2717 C CA    . GLY A 158 ? 0.2412 0.3374 0.5583 -0.0321 -0.1657 0.1147  341  GLY A CA    
2718 C C     . GLY A 158 ? 0.2756 0.3606 0.5690 -0.0155 -0.1666 0.0944  341  GLY A C     
2719 O O     . GLY A 158 ? 0.3182 0.3576 0.6069 0.0093  -0.1673 0.0819  341  GLY A O     
2723 N N     . LYS A 159 ? 0.2438 0.3836 0.5289 -0.0186 -0.1692 0.1014  342  LYS A N     
2724 C CA    . LYS A 159 ? 0.2444 0.4015 0.4992 -0.0011 -0.1499 0.1274  342  LYS A CA    
2725 C C     . LYS A 159 ? 0.2131 0.3428 0.4574 -0.0290 -0.1412 0.1103  342  LYS A C     
2726 O O     . LYS A 159 ? 0.2496 0.3194 0.4731 -0.0495 -0.1329 0.1031  342  LYS A O     
2727 C CB    . LYS A 159 ? 0.2968 0.4768 0.5040 0.0385  -0.1255 0.1574  342  LYS A CB    
2728 C CG    . LYS A 159 ? 0.4124 0.5472 0.5650 0.0648  -0.0875 0.1451  342  LYS A CG    
2729 C CD    . LYS A 159 ? 0.5092 0.6042 0.6286 0.0702  -0.0272 0.1208  342  LYS A CD    
2730 C CE    . LYS A 159 ? 0.5811 0.6463 0.6960 0.0683  -0.0031 0.0932  342  LYS A CE    
2731 N NZ    . LYS A 159 ? 0.6358 0.6691 0.7310 0.0651  0.0154  0.0776  342  LYS A NZ    
2745 N N     . THR A 160 ? 0.2261 0.3192 0.4352 -0.0067 -0.1228 0.1049  343  THR A N     
2746 C CA    . THR A 160 ? 0.2250 0.2995 0.4155 0.0050  -0.1356 0.1048  343  THR A CA    
2747 C C     . THR A 160 ? 0.1905 0.2747 0.3714 0.0088  -0.1153 0.0669  343  THR A C     
2748 O O     . THR A 160 ? 0.2215 0.2980 0.4195 0.0070  -0.0747 0.0528  343  THR A O     
2749 C CB    . THR A 160 ? 0.2778 0.3194 0.4623 0.0305  -0.1557 0.1050  343  THR A CB    
2750 O OG1   . THR A 160 ? 0.3749 0.3173 0.5201 0.0582  -0.1454 0.1034  343  THR A OG1   
2751 C CG2   . THR A 160 ? 0.2529 0.3417 0.4515 0.0217  -0.1625 0.0888  343  THR A CG2   
2759 N N     . MET A 161 ? 0.1724 0.2252 0.3339 -0.0121 -0.1253 0.0422  344  MET A N     
2760 C CA    A MET A 161 ? 0.2096 0.2129 0.3384 -0.0202 -0.1338 0.0393  344  MET A CA    
2761 C CA    B MET A 161 ? 0.2072 0.2034 0.3255 -0.0143 -0.1399 0.0323  344  MET A CA    
2762 C C     . MET A 161 ? 0.2364 0.1966 0.3314 -0.0195 -0.1472 0.0355  344  MET A C     
2763 O O     . MET A 161 ? 0.2505 0.1974 0.3095 -0.0361 -0.1285 0.0590  344  MET A O     
2764 C CB    A MET A 161 ? 0.2092 0.2240 0.3161 -0.0189 -0.1444 0.0472  344  MET A CB    
2765 C CB    B MET A 161 ? 0.2108 0.1947 0.3056 -0.0070 -0.1464 0.0207  344  MET A CB    
2766 C CG    A MET A 161 ? 0.2330 0.2352 0.3212 -0.0126 -0.1396 0.0549  344  MET A CG    
2767 C CG    B MET A 161 ? 0.2268 0.1864 0.3079 0.0056  -0.1477 0.0056  344  MET A CG    
2768 S SD    A MET A 161 ? 0.1973 0.2421 0.3389 -0.0070 -0.1330 0.0613  344  MET A SD    
2769 S SD    B MET A 161 ? 0.2179 0.1748 0.3037 0.0261  -0.1398 -0.0180 344  MET A SD    
2770 C CE    A MET A 161 ? 0.1895 0.2248 0.2934 -0.0092 -0.1207 0.0461  344  MET A CE    
2771 C CE    B MET A 161 ? 0.2018 0.1591 0.2609 0.0237  -0.1320 -0.0423 344  MET A CE    
2790 N N     . THR A 162 ? 0.2228 0.1824 0.3711 -0.0042 -0.1437 0.0239  345  THR A N     
2791 C CA    . THR A 162 ? 0.2113 0.1829 0.3892 0.0021  -0.1469 0.0422  345  THR A CA    
2792 C C     . THR A 162 ? 0.2355 0.1684 0.3365 -0.0013 -0.1502 0.0369  345  THR A C     
2793 O O     . THR A 162 ? 0.2279 0.1937 0.3305 -0.0019 -0.1425 0.0358  345  THR A O     
2794 C CB    . THR A 162 ? 0.2010 0.2168 0.4641 0.0223  -0.1204 0.0635  345  THR A CB    
2795 O OG1   . THR A 162 ? 0.2307 0.2334 0.5407 0.0252  -0.1192 0.0599  345  THR A OG1   
2796 C CG2   . THR A 162 ? 0.2487 0.2392 0.4628 0.0504  -0.1083 0.0941  345  THR A CG2   
2804 N N     . LYS A 163 ? 0.2265 0.1466 0.3057 0.0059  -0.1445 0.0283  346  LYS A N     
2805 C CA    . LYS A 163 ? 0.2158 0.1419 0.2939 -0.0005 -0.1365 0.0199  346  LYS A CA    
2806 C C     . LYS A 163 ? 0.2065 0.1393 0.3218 0.0102  -0.1390 0.0179  346  LYS A C     
2807 O O     . LYS A 163 ? 0.2238 0.1553 0.3482 0.0275  -0.1254 0.0061  346  LYS A O     
2808 C CB    . LYS A 163 ? 0.2101 0.1387 0.2803 -0.0072 -0.1044 0.0352  346  LYS A CB    
2809 C CG    . LYS A 163 ? 0.2473 0.1481 0.2504 -0.0446 -0.1118 0.0192  346  LYS A CG    
2810 C CD    . LYS A 163 ? 0.2647 0.1493 0.2700 -0.0531 -0.1508 0.0313  346  LYS A CD    
2811 C CE    . LYS A 163 ? 0.3074 0.1554 0.3135 -0.0567 -0.1701 0.0354  346  LYS A CE    
2812 N NZ    . LYS A 163 ? 0.2953 0.1662 0.3338 -0.0388 -0.1834 0.0386  346  LYS A NZ    
2826 N N     . PRO A 164 ? 0.1929 0.1251 0.3084 0.0014  -0.1221 0.0174  347  PRO A N     
2827 C CA    . PRO A 164 ? 0.1925 0.1238 0.2645 0.0041  -0.1184 0.0325  347  PRO A CA    
2828 C C     . PRO A 164 ? 0.1953 0.1174 0.2133 -0.0195 -0.1177 0.0340  347  PRO A C     
2829 O O     . PRO A 164 ? 0.2079 0.1216 0.2092 -0.0219 -0.0822 0.0226  347  PRO A O     
2830 C CB    . PRO A 164 ? 0.1935 0.1366 0.2960 -0.0080 -0.1233 0.0230  347  PRO A CB    
2831 C CG    . PRO A 164 ? 0.2242 0.1407 0.3121 -0.0187 -0.1372 0.0268  347  PRO A CG    
2832 C CD    . PRO A 164 ? 0.2387 0.1376 0.3145 -0.0163 -0.1432 0.0125  347  PRO A CD    
2840 N N     . PHE A 165 ? 0.1944 0.1116 0.2425 -0.0311 -0.1048 0.0293  348  PHE A N     
2841 C CA    . PHE A 165 ? 0.1758 0.1221 0.2388 -0.0300 -0.0826 0.0168  348  PHE A CA    
2842 C C     . PHE A 165 ? 0.1829 0.1237 0.1974 -0.0101 -0.0713 0.0260  348  PHE A C     
2843 O O     . PHE A 165 ? 0.1904 0.1354 0.2355 -0.0159 -0.0934 0.0443  348  PHE A O     
2844 C CB    . PHE A 165 ? 0.1742 0.1282 0.2845 -0.0384 -0.1079 0.0305  348  PHE A CB    
2845 C CG    . PHE A 165 ? 0.1817 0.1286 0.3029 -0.0296 -0.1176 0.0249  348  PHE A CG    
2846 C CD1   . PHE A 165 ? 0.1850 0.1343 0.2926 -0.0231 -0.1205 0.0100  348  PHE A CD1   
2847 C CD2   . PHE A 165 ? 0.2023 0.1276 0.3274 -0.0262 -0.1401 0.0236  348  PHE A CD2   
2848 C CE1   . PHE A 165 ? 0.1905 0.1421 0.2942 -0.0187 -0.1305 0.0126  348  PHE A CE1   
2849 C CE2   . PHE A 165 ? 0.2289 0.1321 0.3266 -0.0304 -0.1248 0.0356  348  PHE A CE2   
2850 C CZ    . PHE A 165 ? 0.2095 0.1375 0.3071 -0.0378 -0.1303 0.0267  348  PHE A CZ    
2860 N N     . VAL A 166 ? 0.1830 0.1253 0.2133 -0.0032 -0.0676 0.0275  349  VAL A N     
2861 C CA    . VAL A 166 ? 0.1626 0.1280 0.2300 -0.0032 -0.0799 0.0198  349  VAL A CA    
2862 C C     . VAL A 166 ? 0.1857 0.1278 0.2306 -0.0096 -0.0720 0.0227  349  VAL A C     
2863 O O     . VAL A 166 ? 0.1878 0.1361 0.2309 -0.0256 -0.0663 0.0035  349  VAL A O     
2864 C CB    . VAL A 166 ? 0.1612 0.1445 0.2541 -0.0259 -0.1132 0.0285  349  VAL A CB    
2865 C CG1   . VAL A 166 ? 0.1701 0.1606 0.2897 -0.0471 -0.0981 0.0264  349  VAL A CG1   
2866 C CG2   . VAL A 166 ? 0.2020 0.1679 0.2532 -0.0232 -0.1291 0.0228  349  VAL A CG2   
2876 N N     . GLU A 167 ? 0.1708 0.1142 0.2547 -0.0143 -0.0879 0.0203  350  GLU A N     
2877 C CA    . GLU A 167 ? 0.1521 0.1185 0.2272 -0.0101 -0.0354 0.0098  350  GLU A CA    
2878 C C     . GLU A 167 ? 0.1628 0.1312 0.2400 -0.0015 -0.0243 0.0174  350  GLU A C     
2879 O O     . GLU A 167 ? 0.1818 0.1340 0.2653 0.0100  -0.0467 0.0322  350  GLU A O     
2880 C CB    . GLU A 167 ? 0.2145 0.1225 0.2240 -0.0316 -0.0747 0.0219  350  GLU A CB    
2881 C CG    . GLU A 167 ? 0.2185 0.1350 0.2307 -0.0255 -0.0594 0.0146  350  GLU A CG    
2882 C CD    . GLU A 167 ? 0.2452 0.1486 0.2450 -0.0298 -0.0665 0.0049  350  GLU A CD    
2883 O OE1   . GLU A 167 ? 0.2583 0.1472 0.2618 -0.0347 -0.0639 0.0246  350  GLU A OE1   
2884 O OE2   . GLU A 167 ? 0.2988 0.1602 0.2395 -0.0198 -0.0970 0.0069  350  GLU A OE2   
2891 N N     . LYS A 168 ? 0.1668 0.1339 0.2316 -0.0069 -0.0470 0.0190  351  LYS A N     
2892 C CA    . LYS A 168 ? 0.1863 0.1309 0.2389 0.0115  -0.0474 0.0339  351  LYS A CA    
2893 C C     . LYS A 168 ? 0.2064 0.1279 0.2324 0.0028  -0.0572 0.0384  351  LYS A C     
2894 O O     . LYS A 168 ? 0.1831 0.1246 0.2332 0.0114  -0.0448 0.0294  351  LYS A O     
2895 C CB    . LYS A 168 ? 0.1740 0.1327 0.2668 0.0098  -0.0519 0.0264  351  LYS A CB    
2896 C CG    . LYS A 168 ? 0.1696 0.1496 0.2768 0.0150  -0.0602 -0.0059 351  LYS A CG    
2897 C CD    . LYS A 168 ? 0.2078 0.1637 0.2752 0.0138  -0.0988 -0.0208 351  LYS A CD    
2898 C CE    . LYS A 168 ? 0.2065 0.1742 0.2653 0.0092  -0.0599 0.0002  351  LYS A CE    
2899 N NZ    . LYS A 168 ? 0.2085 0.1841 0.2643 0.0085  -0.1076 -0.0002 351  LYS A NZ    
2913 N N     . PRO A 169 ? 0.1939 0.1271 0.2659 0.0047  -0.0686 0.0269  352  PRO A N     
2914 C CA    . PRO A 169 ? 0.2092 0.1279 0.2713 0.0054  -0.0463 0.0129  352  PRO A CA    
2915 C C     . PRO A 169 ? 0.1816 0.1269 0.2412 0.0197  -0.0453 0.0117  352  PRO A C     
2916 O O     . PRO A 169 ? 0.2182 0.1308 0.2447 0.0191  -0.0658 0.0217  352  PRO A O     
2917 C CB    . PRO A 169 ? 0.2397 0.1395 0.3051 0.0099  -0.0528 -0.0076 352  PRO A CB    
2918 C CG    . PRO A 169 ? 0.2379 0.1415 0.3419 0.0174  -0.0357 0.0031  352  PRO A CG    
2919 C CD    . PRO A 169 ? 0.2124 0.1368 0.3031 0.0129  -0.0446 0.0223  352  PRO A CD    
2927 N N     . VAL A 170 ? 0.1930 0.1320 0.2328 0.0009  -0.0245 0.0136  353  VAL A N     
2928 C CA    . VAL A 170 ? 0.2102 0.1318 0.2405 0.0112  -0.0335 0.0188  353  VAL A CA    
2929 C C     . VAL A 170 ? 0.1912 0.1467 0.2648 0.0376  -0.0372 0.0278  353  VAL A C     
2930 O O     . VAL A 170 ? 0.2208 0.1519 0.2309 0.0205  -0.0391 0.0229  353  VAL A O     
2931 C CB    . VAL A 170 ? 0.2487 0.1301 0.2469 -0.0116 -0.0353 0.0301  353  VAL A CB    
2932 C CG1   . VAL A 170 ? 0.2574 0.1382 0.2487 -0.0223 -0.0505 0.0438  353  VAL A CG1   
2933 C CG2   . VAL A 170 ? 0.2867 0.1234 0.2829 -0.0324 -0.0188 0.0211  353  VAL A CG2   
2943 N N     . ASP A 171 ? 0.2118 0.1604 0.2910 0.0412  -0.0353 0.0350  354  ASP A N     
2944 C CA    . ASP A 171 ? 0.2190 0.1941 0.3358 0.0629  -0.0285 0.0340  354  ASP A CA    
2945 C C     . ASP A 171 ? 0.2042 0.2128 0.3586 0.0389  -0.0409 0.0581  354  ASP A C     
2946 O O     . ASP A 171 ? 0.1820 0.2195 0.3757 0.0226  -0.0275 0.0680  354  ASP A O     
2947 C CB    . ASP A 171 ? 0.2752 0.2322 0.3826 0.0949  0.0364  0.0193  354  ASP A CB    
2948 C CG    . ASP A 171 ? 0.3397 0.2918 0.4525 0.1286  0.0332  0.0112  354  ASP A CG    
2949 O OD1   . ASP A 171 ? 0.3106 0.2986 0.4488 0.1618  0.0272  0.0478  354  ASP A OD1   
2950 O OD2   . ASP A 171 ? 0.4139 0.3366 0.5254 0.1367  0.0187  -0.0195 354  ASP A OD2   
2955 N N     . GLY A 172 ? 0.2041 0.2363 0.3560 0.0127  -0.0451 0.0599  355  GLY A N     
2956 C CA    . GLY A 172 ? 0.2019 0.2647 0.4315 0.0017  -0.0482 0.0690  355  GLY A CA    
2957 C C     . GLY A 172 ? 0.2098 0.2892 0.5029 0.0172  -0.0544 0.0761  355  GLY A C     
2958 O O     . GLY A 172 ? 0.2474 0.2908 0.5478 0.0219  -0.1033 0.0589  355  GLY A O     
2962 N N     . GLU A 173 ? 0.1866 0.3112 0.5245 0.0564  -0.0440 0.1104  356  GLU A N     
2963 C CA    . GLU A 173 ? 0.2425 0.3326 0.5940 0.0570  -0.0413 0.1352  356  GLU A CA    
2964 C C     . GLU A 173 ? 0.2075 0.3091 0.5858 0.0556  -0.0231 0.1422  356  GLU A C     
2965 O O     . GLU A 173 ? 0.2187 0.3125 0.6204 0.0647  0.0138  0.1585  356  GLU A O     
2966 C CB    . GLU A 173 ? 0.3201 0.3692 0.6597 0.0676  -0.0196 0.1561  356  GLU A CB    
2967 C CG    . GLU A 173 ? 0.4045 0.4066 0.7356 0.0642  -0.0417 0.1605  356  GLU A CG    
2968 C CD    . GLU A 173 ? 0.4681 0.4382 0.8037 0.0378  -0.0706 0.1455  356  GLU A CD    
2969 O OE1   . GLU A 173 ? 0.4768 0.4353 0.8181 0.0297  -0.0733 0.1410  356  GLU A OE1   
2970 O OE2   . GLU A 173 ? 0.4854 0.4584 0.8384 0.0147  -0.0928 0.1353  356  GLU A OE2   
2977 N N     . ASP A 174 ? 0.2386 0.2859 0.5323 0.0559  -0.0114 0.1203  357  ASP A N     
2978 C CA    . ASP A 174 ? 0.2212 0.2651 0.5036 0.0511  -0.0029 0.0963  357  ASP A CA    
2979 C C     . ASP A 174 ? 0.2113 0.2671 0.4832 0.0671  -0.0277 0.0924  357  ASP A C     
2980 O O     . ASP A 174 ? 0.2106 0.2749 0.4699 0.0702  -0.0346 0.0835  357  ASP A O     
2981 C CB    . ASP A 174 ? 0.2328 0.2508 0.4777 0.0543  0.0260  0.0721  357  ASP A CB    
2982 C CG    . ASP A 174 ? 0.2853 0.2370 0.4628 0.0377  0.0330  0.0517  357  ASP A CG    
2983 O OD1   . ASP A 174 ? 0.2773 0.2281 0.4479 0.0366  0.0351  0.0528  357  ASP A OD1   
2984 O OD2   . ASP A 174 ? 0.3022 0.2296 0.4717 0.0103  0.0576  0.0386  357  ASP A OD2   
2989 N N     . HIS A 175 ? 0.2214 0.2631 0.4483 0.0510  -0.0255 0.1084  358  HIS A N     
2990 C CA    . HIS A 175 ? 0.2115 0.2688 0.4455 0.0316  -0.0707 0.0901  358  HIS A CA    
2991 C C     . HIS A 175 ? 0.2033 0.2428 0.4249 0.0226  -0.0736 0.0653  358  HIS A C     
2992 O O     . HIS A 175 ? 0.1994 0.2413 0.4080 0.0109  -0.0427 0.0716  358  HIS A O     
2993 C CB    . HIS A 175 ? 0.3101 0.3066 0.4531 0.0418  -0.0815 0.0935  358  HIS A CB    
2994 C CG    . HIS A 175 ? 0.4437 0.3492 0.4488 0.0511  -0.0756 0.0799  358  HIS A CG    
2995 N ND1   . HIS A 175 ? 0.4803 0.3683 0.4558 0.0608  -0.0802 0.0942  358  HIS A ND1   
2996 C CD2   . HIS A 175 ? 0.5077 0.3658 0.4502 0.0535  -0.0856 0.0619  358  HIS A CD2   
2997 C CE1   . HIS A 175 ? 0.5267 0.3765 0.4608 0.0594  -0.0698 0.0925  358  HIS A CE1   
2998 N NE2   . HIS A 175 ? 0.5378 0.3745 0.4646 0.0607  -0.0807 0.0748  358  HIS A NE2   
3006 N N     . ASN A 176 ? 0.2007 0.2258 0.4159 0.0265  -0.0477 0.0497  359  ASN A N     
3007 C CA    . ASN A 176 ? 0.2071 0.2135 0.4084 -0.0024 -0.0312 0.0313  359  ASN A CA    
3008 C C     . ASN A 176 ? 0.1787 0.2030 0.3409 -0.0047 -0.0184 0.0337  359  ASN A C     
3009 O O     . ASN A 176 ? 0.1914 0.2022 0.3281 0.0035  -0.0175 0.0312  359  ASN A O     
3010 C CB    . ASN A 176 ? 0.2925 0.2177 0.4864 -0.0059 0.0445  0.0099  359  ASN A CB    
3011 C CG    . ASN A 176 ? 0.3667 0.2294 0.5309 0.0060  0.0891  0.0195  359  ASN A CG    
3012 O OD1   . ASN A 176 ? 0.3612 0.2548 0.5441 0.0217  0.1201  0.0310  359  ASN A OD1   
3013 N ND2   . ASN A 176 ? 0.4081 0.2188 0.5589 0.0128  0.1001  0.0140  359  ASN A ND2   
3020 N N     . ILE A 177 ? 0.2196 0.2030 0.3079 0.0201  -0.0353 0.0427  360  ILE A N     
3021 C CA    . ILE A 177 ? 0.1876 0.2008 0.2690 0.0305  -0.0396 0.0521  360  ILE A CA    
3022 C C     . ILE A 177 ? 0.2062 0.2006 0.2438 0.0019  -0.0404 0.0469  360  ILE A C     
3023 O O     . ILE A 177 ? 0.2341 0.2105 0.2433 -0.0250 -0.0339 0.0575  360  ILE A O     
3024 C CB    . ILE A 177 ? 0.1889 0.1986 0.2524 0.0245  -0.0301 0.0571  360  ILE A CB    
3025 C CG1   . ILE A 177 ? 0.2087 0.2154 0.2638 0.0309  -0.0373 0.0702  360  ILE A CG1   
3026 C CG2   . ILE A 177 ? 0.1995 0.1820 0.2531 0.0027  -0.0531 0.0413  360  ILE A CG2   
3027 C CD1   . ILE A 177 ? 0.2291 0.2273 0.2947 0.0173  -0.0613 0.0719  360  ILE A CD1   
3039 N N     . TYR A 178 ? 0.1963 0.1851 0.2364 0.0080  -0.0366 0.0506  361  TYR A N     
3040 C CA    . TYR A 178 ? 0.1811 0.1901 0.2366 0.0070  -0.0466 0.0525  361  TYR A CA    
3041 C C     . TYR A 178 ? 0.1569 0.1757 0.2567 -0.0044 -0.0423 0.0469  361  TYR A C     
3042 O O     . TYR A 178 ? 0.1828 0.1581 0.2870 -0.0148 -0.0229 0.0467  361  TYR A O     
3043 C CB    . TYR A 178 ? 0.2066 0.2107 0.2237 -0.0017 -0.0187 0.0557  361  TYR A CB    
3044 C CG    . TYR A 178 ? 0.2499 0.2357 0.2358 -0.0004 -0.0320 0.0452  361  TYR A CG    
3045 C CD1   . TYR A 178 ? 0.2782 0.2491 0.2174 0.0184  0.0176  0.0425  361  TYR A CD1   
3046 C CD2   . TYR A 178 ? 0.2855 0.2435 0.2521 -0.0198 -0.0384 0.0481  361  TYR A CD2   
3047 C CE1   . TYR A 178 ? 0.3064 0.2624 0.2548 0.0015  0.0367  0.0462  361  TYR A CE1   
3048 C CE2   . TYR A 178 ? 0.3039 0.2625 0.2465 -0.0202 0.0132  0.0529  361  TYR A CE2   
3049 C CZ    . TYR A 178 ? 0.3339 0.2664 0.2769 -0.0066 0.0307  0.0455  361  TYR A CZ    
3050 O OH    . TYR A 178 ? 0.3804 0.2741 0.2987 -0.0271 0.0338  0.0167  361  TYR A OH    
3060 N N     . ILE A 179 ? 0.1980 0.1817 0.2554 -0.0168 -0.0876 0.0597  362  ILE A N     
3061 C CA    . ILE A 179 ? 0.1946 0.1926 0.2520 -0.0206 -0.0760 0.0652  362  ILE A CA    
3062 C C     . ILE A 179 ? 0.2153 0.1788 0.2243 -0.0348 -0.0742 0.0597  362  ILE A C     
3063 O O     . ILE A 179 ? 0.2409 0.2003 0.2312 -0.0152 -0.0693 0.0660  362  ILE A O     
3064 C CB    . ILE A 179 ? 0.2055 0.2299 0.2949 -0.0313 -0.0970 0.0581  362  ILE A CB    
3065 C CG1   . ILE A 179 ? 0.2928 0.2695 0.3247 -0.0475 -0.0698 0.0661  362  ILE A CG1   
3066 C CG2   . ILE A 179 ? 0.2322 0.2370 0.3167 -0.0446 -0.0899 0.0438  362  ILE A CG2   
3067 C CD1   . ILE A 179 ? 0.2679 0.3006 0.3302 -0.0642 -0.0951 0.0713  362  ILE A CD1   
3079 N N     . TYR A 180 ? 0.2050 0.1562 0.2140 -0.0350 -0.0735 0.0478  363  TYR A N     
3080 C CA    . TYR A 180 ? 0.2317 0.1483 0.2079 -0.0479 -0.0881 0.0429  363  TYR A CA    
3081 C C     . TYR A 180 ? 0.2241 0.1472 0.2217 -0.0488 -0.0933 0.0513  363  TYR A C     
3082 O O     . TYR A 180 ? 0.2368 0.1333 0.2339 -0.0443 -0.0871 0.0489  363  TYR A O     
3083 C CB    . TYR A 180 ? 0.2273 0.1510 0.2106 -0.0614 -0.0948 0.0465  363  TYR A CB    
3084 C CG    . TYR A 180 ? 0.2306 0.1502 0.2024 -0.0622 -0.0751 0.0366  363  TYR A CG    
3085 C CD1   . TYR A 180 ? 0.2263 0.1542 0.2306 -0.0613 -0.0879 0.0279  363  TYR A CD1   
3086 C CD2   . TYR A 180 ? 0.2636 0.1510 0.2064 -0.0444 -0.0777 0.0262  363  TYR A CD2   
3087 C CE1   . TYR A 180 ? 0.2615 0.1615 0.2258 -0.0334 -0.0811 0.0285  363  TYR A CE1   
3088 C CE2   . TYR A 180 ? 0.2719 0.1485 0.1877 -0.0337 -0.0362 0.0217  363  TYR A CE2   
3089 C CZ    . TYR A 180 ? 0.2727 0.1589 0.2188 -0.0399 -0.0844 0.0268  363  TYR A CZ    
3090 O OH    . TYR A 180 ? 0.3163 0.1626 0.2609 -0.0496 -0.0678 0.0243  363  TYR A OH    
3100 N N     . TYR A 181 ? 0.2007 0.1517 0.2191 -0.0393 -0.0949 0.0447  364  TYR A N     
3101 C CA    . TYR A 181 ? 0.2171 0.1382 0.2410 -0.0471 -0.1170 0.0398  364  TYR A CA    
3102 C C     . TYR A 181 ? 0.2481 0.1287 0.2640 -0.0550 -0.1343 0.0514  364  TYR A C     
3103 O O     . TYR A 181 ? 0.2732 0.1327 0.2682 -0.0429 -0.1451 0.0423  364  TYR A O     
3104 C CB    . TYR A 181 ? 0.2208 0.1476 0.2653 -0.0431 -0.0806 0.0279  364  TYR A CB    
3105 C CG    . TYR A 181 ? 0.1917 0.1751 0.2387 -0.0439 -0.0762 0.0343  364  TYR A CG    
3106 C CD1   . TYR A 181 ? 0.1780 0.2006 0.2517 -0.0505 -0.0952 0.0354  364  TYR A CD1   
3107 C CD2   . TYR A 181 ? 0.2055 0.2040 0.2836 -0.0474 -0.0978 0.0351  364  TYR A CD2   
3108 C CE1   . TYR A 181 ? 0.1965 0.2281 0.2838 -0.0490 -0.1066 0.0374  364  TYR A CE1   
3109 C CE2   . TYR A 181 ? 0.2404 0.2316 0.3097 -0.0380 -0.1013 0.0299  364  TYR A CE2   
3110 C CZ    . TYR A 181 ? 0.2030 0.2428 0.3079 -0.0266 -0.1089 0.0360  364  TYR A CZ    
3111 O OH    . TYR A 181 ? 0.1941 0.2680 0.3488 -0.0114 -0.1074 0.0196  364  TYR A OH    
3121 N N     . HIS A 182 ? 0.2377 0.1404 0.2905 -0.0469 -0.1524 0.0547  365  HIS A N     
3122 C CA    . HIS A 182 ? 0.2515 0.1424 0.3278 -0.0319 -0.1676 0.0406  365  HIS A CA    
3123 C C     . HIS A 182 ? 0.2800 0.1474 0.3240 -0.0292 -0.1691 0.0530  365  HIS A C     
3124 O O     . HIS A 182 ? 0.2885 0.1280 0.3134 -0.0445 -0.1516 0.0418  365  HIS A O     
3125 C CB    . HIS A 182 ? 0.2724 0.1503 0.3345 -0.0063 -0.1612 0.0394  365  HIS A CB    
3126 C CG    . HIS A 182 ? 0.2690 0.1635 0.3612 -0.0125 -0.1725 0.0478  365  HIS A CG    
3127 N ND1   . HIS A 182 ? 0.2823 0.1711 0.3755 -0.0036 -0.1702 0.0527  365  HIS A ND1   
3128 C CD2   . HIS A 182 ? 0.2633 0.1847 0.3872 -0.0037 -0.1667 0.0596  365  HIS A CD2   
3129 C CE1   . HIS A 182 ? 0.2880 0.1908 0.3793 0.0145  -0.1581 0.0646  365  HIS A CE1   
3130 N NE2   . HIS A 182 ? 0.2834 0.1971 0.3909 0.0109  -0.1670 0.0608  365  HIS A NE2   
3138 N N     . SER A 183 ? 0.3084 0.1661 0.3383 -0.0464 -0.1737 0.0757  366  SER A N     
3139 C CA    . SER A 183 ? 0.3146 0.1749 0.3688 -0.0502 -0.1712 0.0691  366  SER A CA    
3140 C C     . SER A 183 ? 0.3145 0.1669 0.4025 -0.0355 -0.1473 0.0600  366  SER A C     
3141 O O     . SER A 183 ? 0.3551 0.1825 0.4321 -0.0363 -0.0750 0.0778  366  SER A O     
3142 C CB    . SER A 183 ? 0.2827 0.2019 0.4044 -0.0263 -0.1704 0.0817  366  SER A CB    
3143 O OG    . SER A 183 ? 0.2531 0.2096 0.3994 -0.0141 -0.1578 0.0889  366  SER A OG    
3149 N N     . LYS A 184 ? 0.2628 0.1491 0.4267 -0.0012 -0.1569 0.0400  367  LYS A N     
3150 C CA    A LYS A 184 ? 0.2600 0.1547 0.4673 -0.0050 -0.1399 0.0462  367  LYS A CA    
3151 C CA    B LYS A 184 ? 0.2839 0.1528 0.4506 -0.0166 -0.1283 0.0362  367  LYS A CA    
3152 C C     . LYS A 184 ? 0.2945 0.1524 0.4394 -0.0366 -0.1395 0.0381  367  LYS A C     
3153 O O     . LYS A 184 ? 0.3061 0.1426 0.4324 -0.0484 -0.1244 0.0230  367  LYS A O     
3154 C CB    A LYS A 184 ? 0.2830 0.1827 0.5179 0.0450  -0.1029 0.0359  367  LYS A CB    
3155 C CB    B LYS A 184 ? 0.3257 0.1734 0.4676 -0.0031 -0.0736 0.0138  367  LYS A CB    
3156 C CG    A LYS A 184 ? 0.2811 0.2346 0.5508 0.0767  -0.1170 0.0327  367  LYS A CG    
3157 C CG    B LYS A 184 ? 0.3570 0.2112 0.4839 -0.0038 -0.0450 0.0045  367  LYS A CG    
3158 C CD    A LYS A 184 ? 0.3047 0.2870 0.5950 0.0967  -0.1078 0.0182  367  LYS A CD    
3159 C CD    B LYS A 184 ? 0.3920 0.2482 0.4927 0.0015  -0.0190 0.0091  367  LYS A CD    
3160 C CE    A LYS A 184 ? 0.3565 0.3234 0.6468 0.0968  -0.0844 0.0063  367  LYS A CE    
3161 C CE    B LYS A 184 ? 0.4048 0.2754 0.4969 0.0028  0.0107  0.0150  367  LYS A CE    
3162 N NZ    A LYS A 184 ? 0.3807 0.3395 0.6709 0.0903  -0.0775 0.0015  367  LYS A NZ    
3163 N NZ    B LYS A 184 ? 0.4045 0.2879 0.5039 0.0004  0.0270  0.0177  367  LYS A NZ    
3190 N N     . ASN A 185 ? 0.3175 0.1749 0.3767 -0.0534 -0.1839 0.0514  368  ASN A N     
3191 C CA    A ASN A 185 ? 0.3365 0.1872 0.3358 -0.0717 -0.1757 0.0456  368  ASN A CA    
3192 C CA    B ASN A 185 ? 0.3391 0.1890 0.3376 -0.0708 -0.1724 0.0499  368  ASN A CA    
3193 C C     . ASN A 185 ? 0.3606 0.1988 0.3259 -0.0665 -0.1250 0.0352  368  ASN A C     
3194 O O     . ASN A 185 ? 0.3624 0.2631 0.3600 -0.0459 -0.1138 -0.0027 368  ASN A O     
3195 C CB    A ASN A 185 ? 0.3683 0.2082 0.3331 -0.0814 -0.1947 0.0523  368  ASN A CB    
3196 C CB    B ASN A 185 ? 0.3760 0.2100 0.3370 -0.0798 -0.1839 0.0649  368  ASN A CB    
3197 C CG    A ASN A 185 ? 0.4819 0.2501 0.3438 -0.0966 -0.1861 0.0472  368  ASN A CG    
3198 C CG    B ASN A 185 ? 0.4850 0.2455 0.3550 -0.0917 -0.1649 0.0718  368  ASN A CG    
3199 O OD1   A ASN A 185 ? 0.5201 0.2691 0.3741 -0.0999 -0.1875 0.0415  368  ASN A OD1   
3200 O OD1   B ASN A 185 ? 0.5219 0.2655 0.3908 -0.0961 -0.1687 0.0478  368  ASN A OD1   
3201 N ND2   A ASN A 185 ? 0.5338 0.2677 0.3099 -0.1071 -0.1893 0.0326  368  ASN A ND2   
3202 N ND2   B ASN A 185 ? 0.5126 0.2545 0.3337 -0.0954 -0.1769 0.0909  368  ASN A ND2   
3215 N N     . GLY A 186 ? 0.4323 0.1714 0.2971 -0.0826 -0.0427 0.0325  369  GLY A N     
3216 C CA    . GLY A 186 ? 0.4823 0.1675 0.2806 -0.0805 -0.0263 0.0438  369  GLY A CA    
3217 C C     . GLY A 186 ? 0.5071 0.1606 0.2692 -0.0404 -0.0212 0.0461  369  GLY A C     
3218 O O     . GLY A 186 ? 0.5314 0.1706 0.2587 -0.0100 -0.0375 0.0433  369  GLY A O     
3222 N N     . GLY A 187 ? 0.4420 0.1424 0.2480 -0.0410 -0.0978 0.0322  370  GLY A N     
3223 C CA    . GLY A 187 ? 0.3935 0.1413 0.2505 -0.0107 -0.1369 0.0111  370  GLY A CA    
3224 C C     . GLY A 187 ? 0.3661 0.1549 0.2294 -0.0132 -0.1324 0.0263  370  GLY A C     
3225 O O     . GLY A 187 ? 0.3688 0.1635 0.2541 -0.0572 -0.1108 0.0319  370  GLY A O     
3229 N N     . GLY A 188 ? 0.3404 0.1630 0.2199 -0.0086 -0.0856 -0.0004 371  GLY A N     
3230 C CA    . GLY A 188 ? 0.3353 0.1747 0.1860 -0.0237 -0.0406 0.0063  371  GLY A CA    
3231 C C     . GLY A 188 ? 0.2801 0.1761 0.1752 -0.0445 -0.0650 0.0216  371  GLY A C     
3232 O O     . GLY A 188 ? 0.3027 0.1586 0.1964 -0.0620 -0.0860 0.0368  371  GLY A O     
3236 N N     . GLY A 189 ? 0.2377 0.1993 0.2121 -0.0181 -0.0206 0.0563  372  GLY A N     
3237 C CA    . GLY A 189 ? 0.2380 0.2173 0.2313 -0.0025 -0.0400 0.0786  372  GLY A CA    
3238 C C     . GLY A 189 ? 0.2493 0.2331 0.2379 -0.0224 -0.0550 0.0802  372  GLY A C     
3239 O O     . GLY A 189 ? 0.2571 0.2336 0.2554 -0.0307 -0.0300 0.0815  372  GLY A O     
3243 N N     . ARG A 190 ? 0.2315 0.2353 0.2432 -0.0129 -0.0604 0.0719  373  ARG A N     
3244 C CA    . ARG A 190 ? 0.2531 0.2411 0.2546 0.0041  -0.0685 0.0627  373  ARG A CA    
3245 C C     . ARG A 190 ? 0.2020 0.2286 0.2960 0.0156  -0.0464 0.0569  373  ARG A C     
3246 O O     . ARG A 190 ? 0.2305 0.2208 0.3228 0.0145  -0.0402 0.0716  373  ARG A O     
3247 C CB    . ARG A 190 ? 0.2763 0.2684 0.3058 -0.0551 -0.0727 0.0616  373  ARG A CB    
3248 C CG    . ARG A 190 ? 0.2937 0.2974 0.3420 -0.0616 -0.0853 0.0547  373  ARG A CG    
3249 C CD    . ARG A 190 ? 0.2784 0.3139 0.3576 -0.0464 -0.0755 0.0428  373  ARG A CD    
3250 N NE    . ARG A 190 ? 0.3010 0.3319 0.3560 -0.0850 -0.0958 0.0408  373  ARG A NE    
3251 C CZ    . ARG A 190 ? 0.3868 0.3627 0.3954 -0.1080 -0.1162 0.0199  373  ARG A CZ    
3252 N NH1   . ARG A 190 ? 0.4201 0.3782 0.4543 -0.1272 -0.0636 0.0186  373  ARG A NH1   
3253 N NH2   . ARG A 190 ? 0.4508 0.3730 0.3728 -0.1079 -0.1525 0.0057  373  ARG A NH2   
3267 N N     . ARG A 191 ? 0.1851 0.2371 0.3175 0.0151  -0.0315 0.0630  374  ARG A N     
3268 C CA    . ARG A 191 ? 0.2150 0.2605 0.3162 0.0004  -0.0214 0.0712  374  ARG A CA    
3269 C C     . ARG A 191 ? 0.2259 0.2785 0.3205 -0.0183 -0.0367 0.0809  374  ARG A C     
3270 O O     . ARG A 191 ? 0.2711 0.2956 0.3415 -0.0089 -0.0529 0.1033  374  ARG A O     
3271 C CB    . ARG A 191 ? 0.2237 0.2697 0.2879 0.0202  -0.0019 0.0658  374  ARG A CB    
3272 C CG    . ARG A 191 ? 0.2208 0.2671 0.2546 0.0289  -0.0148 0.0510  374  ARG A CG    
3273 C CD    . ARG A 191 ? 0.3052 0.2659 0.2534 0.0308  -0.0248 0.0538  374  ARG A CD    
3274 N NE    . ARG A 191 ? 0.3735 0.2699 0.2653 0.0177  -0.0207 0.0437  374  ARG A NE    
3275 C CZ    . ARG A 191 ? 0.4526 0.2732 0.2666 0.0288  -0.0143 0.0139  374  ARG A CZ    
3276 N NH1   . ARG A 191 ? 0.4519 0.2546 0.2749 0.0197  0.0171  0.0171  374  ARG A NH1   
3277 N NH2   . ARG A 191 ? 0.4945 0.2901 0.2668 0.0485  -0.0090 -0.0090 374  ARG A NH2   
3291 N N     . LEU A 192 ? 0.1847 0.2799 0.3330 -0.0070 -0.0481 0.0789  375  LEU A N     
3292 C CA    . LEU A 192 ? 0.2149 0.3046 0.3549 -0.0111 -0.0503 0.0851  375  LEU A CA    
3293 C C     . LEU A 192 ? 0.2543 0.3228 0.4109 0.0082  -0.0887 0.0870  375  LEU A C     
3294 O O     . LEU A 192 ? 0.2873 0.3039 0.4151 0.0082  -0.0628 0.0938  375  LEU A O     
3295 C CB    . LEU A 192 ? 0.2475 0.3242 0.3262 -0.0424 -0.0454 0.0766  375  LEU A CB    
3296 C CG    . LEU A 192 ? 0.3001 0.3474 0.3044 -0.0472 -0.0421 0.0423  375  LEU A CG    
3297 C CD1   . LEU A 192 ? 0.3290 0.3680 0.2777 -0.0541 -0.0211 0.0387  375  LEU A CD1   
3298 C CD2   . LEU A 192 ? 0.3312 0.3475 0.3546 -0.0459 -0.0589 0.0202  375  LEU A CD2   
3310 N N     . PHE A 193 ? 0.3293 0.3802 0.4875 0.0304  -0.1079 0.0736  376  PHE A N     
3311 C CA    . PHE A 193 ? 0.3911 0.4417 0.5705 0.0542  -0.1353 0.0782  376  PHE A CA    
3312 C C     . PHE A 193 ? 0.4139 0.4746 0.6155 0.0607  -0.1938 0.0860  376  PHE A C     
3313 O O     . PHE A 193 ? 0.3925 0.4412 0.5965 0.0714  -0.2098 0.1009  376  PHE A O     
3314 C CB    . PHE A 193 ? 0.4285 0.4754 0.6224 0.0625  -0.0614 0.0814  376  PHE A CB    
3315 C CG    . PHE A 193 ? 0.4343 0.5037 0.6677 0.0720  -0.0072 0.0904  376  PHE A CG    
3316 C CD1   . PHE A 193 ? 0.4404 0.5121 0.6800 0.0863  0.0227  0.0910  376  PHE A CD1   
3317 C CD2   . PHE A 193 ? 0.4658 0.5179 0.6935 0.0700  -0.0067 0.1022  376  PHE A CD2   
3318 C CE1   . PHE A 193 ? 0.4671 0.5176 0.6960 0.0834  0.0251  0.0921  376  PHE A CE1   
3319 C CE2   . PHE A 193 ? 0.4813 0.5231 0.7068 0.0674  0.0073  0.1048  376  PHE A CE2   
3320 C CZ    . PHE A 193 ? 0.4946 0.5229 0.7048 0.0741  0.0124  0.0987  376  PHE A CZ    
3330 N N     . ARG A 194 ? 0.4431 0.5468 0.6737 0.0367  -0.2324 0.0775  377  ARG A N     
3331 C CA    . ARG A 194 ? 0.4652 0.6298 0.7279 -0.0053 -0.2367 0.0519  377  ARG A CA    
3332 C C     . ARG A 194 ? 0.4611 0.6802 0.7695 -0.0200 -0.2193 0.0373  377  ARG A C     
3333 O O     . ARG A 194 ? 0.4143 0.6871 0.7947 -0.0227 -0.2011 0.0296  377  ARG A O     
3334 C CB    . ARG A 194 ? 0.4977 0.6636 0.7420 -0.0293 -0.2183 0.0474  377  ARG A CB    
3335 C CG    . ARG A 194 ? 0.5276 0.6960 0.7660 -0.0352 -0.1761 0.0494  377  ARG A CG    
3336 C CD    . ARG A 194 ? 0.5787 0.7279 0.7978 -0.0331 -0.1357 0.0586  377  ARG A CD    
3337 N NE    . ARG A 194 ? 0.6107 0.7558 0.8248 -0.0400 -0.1060 0.0599  377  ARG A NE    
3338 C CZ    . ARG A 194 ? 0.6412 0.7765 0.8299 -0.0417 -0.0998 0.0614  377  ARG A CZ    
3339 N NH1   . ARG A 194 ? 0.6662 0.7833 0.8358 -0.0513 -0.0895 0.0540  377  ARG A NH1   
3340 N NH2   . ARG A 194 ? 0.6472 0.7835 0.8182 -0.0309 -0.1202 0.0713  377  ARG A NH2   
3354 N N     . LYS A 195 ? 0.5243 0.7203 0.7807 -0.0322 -0.2106 0.0467  378  LYS A N     
3355 C CA    . LYS A 195 ? 0.6052 0.7591 0.7882 -0.0323 -0.1809 0.0691  378  LYS A CA    
3356 C C     . LYS A 195 ? 0.5640 0.7586 0.8063 -0.0273 -0.1486 0.0799  378  LYS A C     
3357 O O     . LYS A 195 ? 0.5399 0.7543 0.8165 -0.0314 -0.1483 0.0709  378  LYS A O     
3358 C CB    . LYS A 195 ? 0.7319 0.7961 0.7870 -0.0262 -0.1682 0.0825  378  LYS A CB    
3359 C CG    . LYS A 195 ? 0.8669 0.8276 0.7943 -0.0289 -0.1313 0.0927  378  LYS A CG    
3360 C CD    . LYS A 195 ? 0.9712 0.8494 0.7943 -0.0282 -0.1117 0.1023  378  LYS A CD    
3361 C CE    . LYS A 195 ? 1.0431 0.8633 0.7957 -0.0237 -0.0908 0.1073  378  LYS A CE    
3362 N NZ    . LYS A 195 ? 1.0837 0.8710 0.8054 -0.0210 -0.0767 0.1054  378  LYS A NZ    
3376 N N     . VAL A 196 ? 0.5486 0.7608 0.8064 -0.0198 -0.1274 0.0968  379  VAL A N     
3377 C CA    . VAL A 196 ? 0.5236 0.7607 0.7941 -0.0036 -0.1073 0.1128  379  VAL A CA    
3378 C C     . VAL A 196 ? 0.5092 0.7430 0.7809 0.0011  -0.1086 0.1295  379  VAL A C     
3379 O O     . VAL A 196 ? 0.5349 0.7464 0.7912 0.0062  -0.1110 0.1281  379  VAL A O     
3380 C CB    . VAL A 196 ? 0.5404 0.7789 0.7980 0.0095  -0.0686 0.1047  379  VAL A CB    
3381 C CG1   . VAL A 196 ? 0.5460 0.7840 0.7965 0.0105  -0.0497 0.1032  379  VAL A CG1   
3382 C CG2   . VAL A 196 ? 0.5471 0.7876 0.8067 0.0171  -0.0585 0.1009  379  VAL A CG2   
3392 N N     . GLY A 197 ? 0.4852 0.7245 0.7623 0.0004  -0.0930 0.1391  380  GLY A N     
3393 C CA    . GLY A 197 ? 0.4844 0.7113 0.7612 0.0106  -0.0691 0.1353  380  GLY A CA    
3394 C C     . GLY A 197 ? 0.4724 0.7008 0.7538 0.0314  -0.0579 0.1253  380  GLY A C     
3395 O O     . GLY A 197 ? 0.4659 0.7011 0.7608 0.0406  -0.0546 0.1249  380  GLY A O     
3399 N N     . ASN A 198 ? 0.4463 0.6885 0.7355 0.0350  -0.0764 0.1127  381  ASN A N     
3400 C CA    . ASN A 198 ? 0.3820 0.6757 0.7203 0.0285  -0.1265 0.0945  381  ASN A CA    
3401 C C     . ASN A 198 ? 0.2974 0.6482 0.6867 -0.0066 -0.1430 0.1119  381  ASN A C     
3402 O O     . ASN A 198 ? 0.3188 0.6361 0.6646 -0.0191 -0.1329 0.1188  381  ASN A O     
3403 C CB    . ASN A 198 ? 0.3755 0.6912 0.7348 0.0495  -0.1660 0.0573  381  ASN A CB    
3404 C CG    . ASN A 198 ? 0.4239 0.7068 0.7478 0.0713  -0.1796 0.0326  381  ASN A CG    
3405 O OD1   . ASN A 198 ? 0.4516 0.7094 0.7547 0.0862  -0.1775 0.0220  381  ASN A OD1   
3406 N ND2   . ASN A 198 ? 0.4004 0.7167 0.7495 0.0709  -0.2197 0.0256  381  ASN A ND2   
3413 N N     . LYS A 199 ? 0.2515 0.6370 0.6693 -0.0182 -0.1490 0.1198  382  LYS A N     
3414 C CA    . LYS A 199 ? 0.2857 0.6265 0.6571 -0.0295 -0.1427 0.1310  382  LYS A CA    
3415 C C     . LYS A 199 ? 0.2980 0.5937 0.6395 -0.0518 -0.1243 0.1610  382  LYS A C     
3416 O O     . LYS A 199 ? 0.2707 0.5973 0.6384 -0.0633 -0.0944 0.1796  382  LYS A O     
3417 C CB    . LYS A 199 ? 0.3624 0.6496 0.6716 -0.0203 -0.1116 0.1073  382  LYS A CB    
3418 C CG    . LYS A 199 ? 0.4259 0.6688 0.6790 -0.0037 -0.0918 0.0892  382  LYS A CG    
3419 C CD    . LYS A 199 ? 0.4880 0.6868 0.6924 0.0043  -0.0689 0.0692  382  LYS A CD    
3420 C CE    . LYS A 199 ? 0.5330 0.7024 0.7082 0.0021  -0.0565 0.0511  382  LYS A CE    
3421 N NZ    . LYS A 199 ? 0.5643 0.7136 0.7241 -0.0044 -0.0517 0.0412  382  LYS A NZ    
3435 N N     . SER A 200 ? 0.3153 0.5581 0.6200 -0.0337 -0.1505 0.1735  383  SER A N     
3436 C CA    . SER A 200 ? 0.3471 0.5347 0.6139 -0.0525 -0.1445 0.1575  383  SER A CA    
3437 C C     . SER A 200 ? 0.3261 0.4989 0.5636 -0.0867 -0.1548 0.1520  383  SER A C     
3438 O O     . SER A 200 ? 0.2916 0.4793 0.5545 -0.0809 -0.1773 0.1528  383  SER A O     
3439 C CB    . SER A 200 ? 0.4299 0.5567 0.6548 -0.0413 -0.1428 0.1310  383  SER A CB    
3440 O OG    . SER A 200 ? 0.5168 0.5739 0.6928 -0.0344 -0.1286 0.1035  383  SER A OG    
3446 N N     . SER A 201 ? 0.3186 0.4945 0.5462 -0.0985 -0.1190 0.1464  384  SER A N     
3447 C CA    . SER A 201 ? 0.2797 0.4977 0.5638 -0.1123 -0.0753 0.1275  384  SER A CA    
3448 C C     . SER A 201 ? 0.3002 0.5038 0.5576 -0.0942 -0.0776 0.1331  384  SER A C     
3449 O O     . SER A 201 ? 0.3468 0.5180 0.5797 -0.0768 -0.0584 0.1438  384  SER A O     
3450 C CB    . SER A 201 ? 0.2637 0.4982 0.5905 -0.1179 -0.0395 0.1115  384  SER A CB    
3451 O OG    . SER A 201 ? 0.2945 0.4993 0.6034 -0.1048 -0.0291 0.1092  384  SER A OG    
3457 N N     . GLU A 202 ? 0.2963 0.4971 0.5394 -0.0752 -0.0560 0.1301  385  GLU A N     
3458 C CA    . GLU A 202 ? 0.3228 0.4968 0.4904 -0.0638 -0.0101 0.1266  385  GLU A CA    
3459 C C     . GLU A 202 ? 0.2740 0.4472 0.3927 -0.0478 -0.0121 0.1269  385  GLU A C     
3460 O O     . GLU A 202 ? 0.2882 0.4262 0.3553 -0.0332 -0.0139 0.1422  385  GLU A O     
3461 C CB    . GLU A 202 ? 0.4267 0.5465 0.5236 -0.0796 0.0002  0.1288  385  GLU A CB    
3462 C CG    . GLU A 202 ? 0.5017 0.5891 0.5338 -0.0777 -0.0055 0.1373  385  GLU A CG    
3463 C CD    . GLU A 202 ? 0.5232 0.6140 0.4961 -0.1045 0.0328  0.1446  385  GLU A CD    
3464 O OE1   . GLU A 202 ? 0.5866 0.6413 0.5657 -0.1046 0.0847  0.1356  385  GLU A OE1   
3465 O OE2   . GLU A 202 ? 0.4115 0.5994 0.3931 -0.1330 0.0247  0.1486  385  GLU A OE2   
3472 N N     . PHE A 203 ? 0.2841 0.4180 0.3213 -0.0571 -0.0058 0.1149  386  PHE A N     
3473 C CA    . PHE A 203 ? 0.2715 0.3858 0.3144 -0.0797 -0.0436 0.0601  386  PHE A CA    
3474 C C     . PHE A 203 ? 0.3209 0.3531 0.3290 -0.0660 -0.0075 0.0396  386  PHE A C     
3475 O O     . PHE A 203 ? 0.3713 0.3896 0.3814 -0.0667 0.0038  0.0094  386  PHE A O     
3476 C CB    . PHE A 203 ? 0.3363 0.3870 0.2944 -0.0946 -0.0250 0.0228  386  PHE A CB    
3477 C CG    . PHE A 203 ? 0.3634 0.3832 0.2682 -0.0870 0.0103  0.0123  386  PHE A CG    
3478 C CD1   . PHE A 203 ? 0.3696 0.3764 0.2699 -0.0904 0.0302  0.0057  386  PHE A CD1   
3479 C CD2   . PHE A 203 ? 0.3782 0.3861 0.3001 -0.0863 0.0315  0.0133  386  PHE A CD2   
3480 C CE1   . PHE A 203 ? 0.3573 0.3700 0.2325 -0.0986 0.1106  0.0129  386  PHE A CE1   
3481 C CE2   . PHE A 203 ? 0.3804 0.3804 0.2740 -0.0769 0.1162  0.0193  386  PHE A CE2   
3482 C CZ    . PHE A 203 ? 0.3560 0.3720 0.2248 -0.0709 0.1461  0.0143  386  PHE A CZ    
3492 N N     . ASP A 204 ? 0.3080 0.2826 0.3107 -0.0462 -0.0133 0.0483  387  ASP A N     
3493 C CA    . ASP A 204 ? 0.3308 0.2412 0.3193 -0.0282 -0.0181 0.0550  387  ASP A CA    
3494 C C     . ASP A 204 ? 0.3821 0.2242 0.2797 -0.0237 -0.0343 0.0669  387  ASP A C     
3495 O O     . ASP A 204 ? 0.3500 0.2091 0.2720 -0.0366 -0.0491 0.0758  387  ASP A O     
3496 C CB    . ASP A 204 ? 0.3293 0.2289 0.3258 -0.0146 -0.0374 0.0662  387  ASP A CB    
3497 C CG    . ASP A 204 ? 0.3957 0.2269 0.3563 -0.0161 -0.0634 0.0659  387  ASP A CG    
3498 O OD1   . ASP A 204 ? 0.3884 0.2381 0.3641 -0.0172 -0.0320 0.0807  387  ASP A OD1   
3499 O OD2   . ASP A 204 ? 0.4488 0.2117 0.3645 -0.0047 -0.1013 0.0468  387  ASP A OD2   
3504 N N     . PRO A 205 ? 0.4438 0.2308 0.2797 0.0302  0.0146  0.0777  388  PRO A N     
3505 C CA    . PRO A 205 ? 0.4776 0.2621 0.2783 0.0661  0.0177  0.0927  388  PRO A CA    
3506 C C     . PRO A 205 ? 0.5028 0.3241 0.2988 0.1162  -0.0272 0.0945  388  PRO A C     
3507 O O     . PRO A 205 ? 0.4976 0.3656 0.3411 0.1746  -0.0050 0.0990  388  PRO A O     
3508 C CB    . PRO A 205 ? 0.4927 0.2456 0.3042 0.0349  0.0594  0.1049  388  PRO A CB    
3509 C CG    . PRO A 205 ? 0.5015 0.2394 0.3201 0.0028  0.0652  0.0955  388  PRO A CG    
3510 C CD    . PRO A 205 ? 0.4662 0.2257 0.3295 -0.0032 0.0343  0.0918  388  PRO A CD    
3518 N N     . THR A 206 ? 0.4868 0.3334 0.2722 0.0783  -0.0503 0.0885  389  THR A N     
3519 C CA    . THR A 206 ? 0.4675 0.3672 0.2650 0.0302  -0.0496 0.0607  389  THR A CA    
3520 C C     . THR A 206 ? 0.4242 0.3468 0.2241 0.0021  -0.0688 0.0387  389  THR A C     
3521 O O     . THR A 206 ? 0.4244 0.3691 0.2319 0.0059  -0.0909 0.0348  389  THR A O     
3522 C CB    . THR A 206 ? 0.5064 0.4251 0.2749 -0.0091 -0.0156 0.0415  389  THR A CB    
3523 O OG1   . THR A 206 ? 0.4886 0.4476 0.2682 -0.0084 0.0483  0.0105  389  THR A OG1   
3524 C CG2   . THR A 206 ? 0.5405 0.4510 0.3237 -0.0307 -0.0072 0.0406  389  THR A CG2   
3532 N N     . LEU A 207 ? 0.3653 0.3005 0.2047 -0.0210 -0.0523 0.0302  390  LEU A N     
3533 C CA    . LEU A 207 ? 0.3593 0.2657 0.2276 -0.0347 -0.0648 0.0273  390  LEU A CA    
3534 C C     . LEU A 207 ? 0.3305 0.2473 0.1896 -0.0478 -0.0628 0.0345  390  LEU A C     
3535 O O     . LEU A 207 ? 0.3032 0.2475 0.2412 -0.0400 -0.0459 0.0164  390  LEU A O     
3536 C CB    . LEU A 207 ? 0.3860 0.2471 0.2223 -0.0097 -0.0662 0.0319  390  LEU A CB    
3537 C CG    . LEU A 207 ? 0.3799 0.2297 0.2635 0.0047  -0.1061 0.0233  390  LEU A CG    
3538 C CD1   . LEU A 207 ? 0.3730 0.2248 0.3089 0.0109  -0.1269 -0.0166 390  LEU A CD1   
3539 C CD2   . LEU A 207 ? 0.4008 0.2231 0.2820 0.0230  -0.0966 0.0486  390  LEU A CD2   
3551 N N     . VAL A 208 ? 0.3412 0.2396 0.2288 -0.0515 -0.1074 0.0460  391  VAL A N     
3552 C CA    . VAL A 208 ? 0.3411 0.2381 0.2509 -0.0582 -0.1301 0.0557  391  VAL A CA    
3553 C C     . VAL A 208 ? 0.3644 0.2246 0.2377 -0.0712 -0.1227 0.0467  391  VAL A C     
3554 O O     . VAL A 208 ? 0.3577 0.2235 0.2297 -0.0983 -0.0957 0.0304  391  VAL A O     
3555 C CB    . VAL A 208 ? 0.4021 0.2746 0.2881 -0.0484 -0.1111 0.0695  391  VAL A CB    
3556 C CG1   . VAL A 208 ? 0.4461 0.2848 0.2742 -0.0592 -0.1247 0.0713  391  VAL A CG1   
3557 C CG2   . VAL A 208 ? 0.4714 0.2985 0.3403 -0.0311 -0.0740 0.0717  391  VAL A CG2   
3567 N N     . HIS A 209 ? 0.3952 0.2301 0.2817 -0.0752 -0.1467 0.0331  392  HIS A N     
3568 C CA    A HIS A 209 ? 0.3754 0.2475 0.2885 -0.0715 -0.1787 0.0371  392  HIS A CA    
3569 C CA    B HIS A 209 ? 0.3826 0.2359 0.2994 -0.0682 -0.1395 0.0201  392  HIS A CA    
3570 C C     . HIS A 209 ? 0.3801 0.2243 0.2928 -0.0666 -0.1466 0.0174  392  HIS A C     
3571 O O     . HIS A 209 ? 0.4363 0.2127 0.2968 -0.0714 -0.1544 -0.0019 392  HIS A O     
3572 C CB    A HIS A 209 ? 0.4508 0.3007 0.3026 -0.0530 -0.1719 0.0665  392  HIS A CB    
3573 C CB    B HIS A 209 ? 0.4099 0.2648 0.3302 -0.0533 -0.0931 0.0110  392  HIS A CB    
3574 C CG    A HIS A 209 ? 0.4783 0.3529 0.3599 -0.0210 -0.1550 0.0766  392  HIS A CG    
3575 C CG    B HIS A 209 ? 0.4224 0.2955 0.3776 -0.0328 -0.0373 -0.0067 392  HIS A CG    
3576 N ND1   A HIS A 209 ? 0.4841 0.3775 0.3829 -0.0005 -0.1484 0.0696  392  HIS A ND1   
3577 N ND1   B HIS A 209 ? 0.4426 0.3108 0.3931 -0.0154 -0.0184 -0.0210 392  HIS A ND1   
3578 C CD2   A HIS A 209 ? 0.4873 0.3675 0.3654 -0.0151 -0.1575 0.0841  392  HIS A CD2   
3579 C CD2   B HIS A 209 ? 0.4327 0.3088 0.4002 -0.0404 -0.0223 -0.0169 392  HIS A CD2   
3580 C CE1   A HIS A 209 ? 0.4559 0.3783 0.3690 -0.0002 -0.1723 0.0739  392  HIS A CE1   
3581 C CE1   B HIS A 209 ? 0.4453 0.3160 0.3997 -0.0166 -0.0156 -0.0286 392  HIS A CE1   
3582 N NE2   A HIS A 209 ? 0.4660 0.3762 0.3824 -0.0023 -0.1699 0.0724  392  HIS A NE2   
3583 N NE2   B HIS A 209 ? 0.4407 0.3144 0.3983 -0.0339 -0.0082 -0.0259 392  HIS A NE2   
3598 N N     . PRO A 210 ? 0.3689 0.2207 0.2853 -0.0605 -0.1341 0.0151  393  PRO A N     
3599 C CA    . PRO A 210 ? 0.3688 0.2185 0.2738 -0.0554 -0.1286 0.0071  393  PRO A CA    
3600 C C     . PRO A 210 ? 0.3972 0.2103 0.2516 -0.0568 -0.0930 0.0087  393  PRO A C     
3601 O O     . PRO A 210 ? 0.4301 0.2112 0.2409 -0.0580 -0.0957 0.0089  393  PRO A O     
3602 C CB    . PRO A 210 ? 0.3982 0.2322 0.3087 -0.0365 -0.0941 0.0157  393  PRO A CB    
3603 C CG    . PRO A 210 ? 0.4024 0.2419 0.3385 -0.0433 -0.1184 0.0210  393  PRO A CG    
3604 C CD    . PRO A 210 ? 0.3899 0.2335 0.3055 -0.0546 -0.1263 0.0201  393  PRO A CD    
3612 N N     . ARG A 211 ? 0.3947 0.1992 0.2237 -0.0554 -0.0693 0.0161  394  ARG A N     
3613 C CA    . ARG A 211 ? 0.4160 0.1993 0.2270 -0.0652 -0.0523 0.0078  394  ARG A CA    
3614 C C     . ARG A 211 ? 0.4838 0.2111 0.2625 -0.0919 -0.0291 0.0076  394  ARG A C     
3615 O O     . ARG A 211 ? 0.5380 0.2118 0.2865 -0.1036 -0.0242 0.0183  394  ARG A O     
3616 C CB    . ARG A 211 ? 0.4113 0.1988 0.2496 -0.0263 -0.0667 0.0156  394  ARG A CB    
3617 C CG    . ARG A 211 ? 0.4005 0.2059 0.2594 -0.0344 -0.0485 0.0219  394  ARG A CG    
3618 C CD    . ARG A 211 ? 0.3556 0.2066 0.2615 -0.0382 -0.0284 0.0426  394  ARG A CD    
3619 N NE    . ARG A 211 ? 0.3661 0.1920 0.2478 -0.0364 0.0097  0.0522  394  ARG A NE    
3620 C CZ    . ARG A 211 ? 0.3350 0.1895 0.2522 -0.0009 0.0249  0.0286  394  ARG A CZ    
3621 N NH1   . ARG A 211 ? 0.3208 0.2031 0.2994 -0.0059 -0.0020 0.0259  394  ARG A NH1   
3622 N NH2   . ARG A 211 ? 0.2704 0.1817 0.2575 -0.0059 0.0245  0.0058  394  ARG A NH2   
3636 N N     . THR A 212 ? 0.5458 0.2278 0.3078 -0.0996 -0.0387 -0.0284 395  THR A N     
3637 C CA    . THR A 212 ? 0.6166 0.2603 0.3231 -0.0976 -0.0385 -0.0579 395  THR A CA    
3638 C C     . THR A 212 ? 0.6503 0.2637 0.3598 -0.0838 -0.0409 -0.0586 395  THR A C     
3639 O O     . THR A 212 ? 0.6545 0.2679 0.4017 -0.0951 -0.0450 -0.0531 395  THR A O     
3640 C CB    . THR A 212 ? 0.6622 0.3053 0.3515 -0.0892 -0.0692 -0.0622 395  THR A CB    
3641 O OG1   . THR A 212 ? 0.7168 0.3311 0.3331 -0.0658 -0.0824 -0.0658 395  THR A OG1   
3642 C CG2   . THR A 212 ? 0.6752 0.3138 0.3892 -0.0883 -0.1138 -0.0592 395  THR A CG2   
3650 N N     . GLU A 213 ? 0.6880 0.2768 0.3634 -0.0663 -0.0585 -0.0596 396  GLU A N     
3651 C CA    A GLU A 213 ? 0.7099 0.2916 0.3804 -0.0614 -0.0539 -0.0474 396  GLU A CA    
3652 C CA    B GLU A 213 ? 0.7077 0.2934 0.3826 -0.0590 -0.0540 -0.0505 396  GLU A CA    
3653 C C     . GLU A 213 ? 0.6464 0.2696 0.3370 -0.0617 -0.0751 -0.0442 396  GLU A C     
3654 O O     . GLU A 213 ? 0.6430 0.2579 0.3100 -0.0808 -0.0724 -0.0491 396  GLU A O     
3655 C CB    A GLU A 213 ? 0.7859 0.3319 0.4667 -0.0396 -0.0283 -0.0467 396  GLU A CB    
3656 C CB    B GLU A 213 ? 0.7842 0.3359 0.4682 -0.0382 -0.0281 -0.0491 396  GLU A CB    
3657 C CG    A GLU A 213 ? 0.8500 0.3765 0.5559 -0.0219 -0.0077 -0.0542 396  GLU A CG    
3658 C CG    B GLU A 213 ? 0.8496 0.3785 0.5557 -0.0195 -0.0066 -0.0542 396  GLU A CG    
3659 C CD    A GLU A 213 ? 0.8962 0.4156 0.6336 -0.0043 0.0114  -0.0481 396  GLU A CD    
3660 C CD    B GLU A 213 ? 0.8937 0.4127 0.6277 0.0001  0.0143  -0.0566 396  GLU A CD    
3661 O OE1   A GLU A 213 ? 0.9097 0.4325 0.6706 0.0052  0.0332  -0.0383 396  GLU A OE1   
3662 O OE1   B GLU A 213 ? 0.9034 0.4293 0.6556 0.0075  0.0295  -0.0514 396  GLU A OE1   
3663 O OE2   A GLU A 213 ? 0.9087 0.4267 0.6528 -0.0042 -0.0074 -0.0482 396  GLU A OE2   
3664 O OE2   B GLU A 213 ? 0.9092 0.4186 0.6503 0.0076  0.0146  -0.0601 396  GLU A OE2   
3677 N N     . GLY A 214 ? 0.5613 0.2326 0.2857 -0.0348 -0.1159 -0.0254 397  GLY A N     
3678 C CA    . GLY A 214 ? 0.5058 0.1995 0.2615 -0.0300 -0.0868 -0.0289 397  GLY A CA    
3679 C C     . GLY A 214 ? 0.4666 0.1741 0.2533 -0.0376 -0.0936 -0.0110 397  GLY A C     
3680 O O     . GLY A 214 ? 0.4761 0.1812 0.2560 -0.0479 -0.1246 0.0105  397  GLY A O     
3684 N N     . SER A 215 ? 0.3938 0.1544 0.2356 -0.0201 -0.0820 0.0003  398  SER A N     
3685 C CA    . SER A 215 ? 0.3105 0.1336 0.2410 -0.0281 -0.0686 -0.0050 398  SER A CA    
3686 C C     . SER A 215 ? 0.2508 0.1327 0.2611 -0.0105 -0.0785 0.0064  398  SER A C     
3687 O O     . SER A 215 ? 0.2511 0.1327 0.2787 -0.0014 -0.0803 0.0076  398  SER A O     
3688 C CB    . SER A 215 ? 0.3278 0.1236 0.2648 -0.0372 -0.0731 -0.0044 398  SER A CB    
3689 O OG    . SER A 215 ? 0.3178 0.1300 0.2805 -0.0375 -0.1029 0.0085  398  SER A OG    
3695 N N     . TYR A 216 ? 0.2299 0.1263 0.2689 -0.0158 -0.0905 0.0050  399  TYR A N     
3696 C CA    . TYR A 216 ? 0.2347 0.1111 0.2566 -0.0149 -0.0961 0.0156  399  TYR A CA    
3697 C C     . TYR A 216 ? 0.2048 0.1227 0.2659 -0.0195 -0.1131 0.0175  399  TYR A C     
3698 O O     . TYR A 216 ? 0.2126 0.1404 0.2702 -0.0309 -0.1097 0.0262  399  TYR A O     
3699 C CB    . TYR A 216 ? 0.2548 0.1053 0.2507 -0.0120 -0.0687 0.0249  399  TYR A CB    
3700 C CG    . TYR A 216 ? 0.3074 0.1240 0.2313 0.0018  -0.0488 0.0296  399  TYR A CG    
3701 C CD1   . TYR A 216 ? 0.2947 0.1449 0.2206 -0.0115 -0.0414 0.0331  399  TYR A CD1   
3702 C CD2   . TYR A 216 ? 0.3258 0.1341 0.2028 -0.0045 -0.0514 0.0258  399  TYR A CD2   
3703 C CE1   . TYR A 216 ? 0.3553 0.1727 0.1987 -0.0135 -0.0257 0.0185  399  TYR A CE1   
3704 C CE2   . TYR A 216 ? 0.3637 0.1511 0.2174 -0.0206 -0.0245 0.0095  399  TYR A CE2   
3705 C CZ    . TYR A 216 ? 0.3878 0.1777 0.2142 -0.0249 -0.0096 0.0028  399  TYR A CZ    
3706 O OH    . TYR A 216 ? 0.4298 0.2024 0.2561 -0.0306 -0.0143 -0.0011 399  TYR A OH    
3716 N N     . ILE A 217 ? 0.2078 0.1116 0.2629 -0.0165 -0.0968 0.0096  400  ILE A N     
3717 C CA    . ILE A 217 ? 0.2149 0.1131 0.2774 -0.0190 -0.0677 0.0292  400  ILE A CA    
3718 C C     . ILE A 217 ? 0.1736 0.1149 0.2557 -0.0283 -0.0786 0.0328  400  ILE A C     
3719 O O     . ILE A 217 ? 0.1830 0.1243 0.2962 -0.0173 -0.0594 0.0425  400  ILE A O     
3720 C CB    . ILE A 217 ? 0.3338 0.1336 0.2769 0.0228  -0.0486 0.0424  400  ILE A CB    
3721 C CG1   . ILE A 217 ? 0.4063 0.1668 0.3460 -0.0258 -0.0058 0.0165  400  ILE A CG1   
3722 C CG2   . ILE A 217 ? 0.3010 0.1680 0.3111 0.0220  -0.1449 0.0229  400  ILE A CG2   
3723 C CD1   . ILE A 217 ? 0.2849 0.1713 0.3676 -0.0848 -0.0106 -0.0096 400  ILE A CD1   
3735 N N     . TYR A 218 ? 0.1671 0.1076 0.2415 -0.0165 -0.0973 0.0147  401  TYR A N     
3736 C CA    . TYR A 218 ? 0.1639 0.1118 0.2608 -0.0192 -0.0910 0.0273  401  TYR A CA    
3737 C C     . TYR A 218 ? 0.1376 0.1208 0.2695 -0.0259 -0.0578 0.0265  401  TYR A C     
3738 O O     . TYR A 218 ? 0.1535 0.1413 0.3130 -0.0400 -0.0387 -0.0147 401  TYR A O     
3739 C CB    . TYR A 218 ? 0.1872 0.1153 0.2823 -0.0190 -0.1115 0.0282  401  TYR A CB    
3740 C CG    . TYR A 218 ? 0.1765 0.1308 0.2634 -0.0308 -0.1017 0.0241  401  TYR A CG    
3741 C CD1   . TYR A 218 ? 0.2057 0.1404 0.2407 -0.0193 -0.1131 0.0264  401  TYR A CD1   
3742 C CD2   . TYR A 218 ? 0.1986 0.1359 0.2575 -0.0282 -0.1003 0.0330  401  TYR A CD2   
3743 C CE1   . TYR A 218 ? 0.2358 0.1482 0.2526 -0.0226 -0.1217 0.0095  401  TYR A CE1   
3744 C CE2   . TYR A 218 ? 0.2344 0.1394 0.2387 -0.0301 -0.1037 0.0259  401  TYR A CE2   
3745 C CZ    . TYR A 218 ? 0.2501 0.1546 0.2324 -0.0268 -0.1111 0.0111  401  TYR A CZ    
3746 O OH    . TYR A 218 ? 0.2689 0.1688 0.2165 -0.0550 -0.0676 0.0168  401  TYR A OH    
3756 N N     . GLU A 219 ? 0.1308 0.1307 0.2604 -0.0086 -0.0948 0.0330  402  GLU A N     
3757 C CA    . GLU A 219 ? 0.1504 0.1421 0.2638 -0.0181 -0.1047 0.0334  402  GLU A CA    
3758 C C     . GLU A 219 ? 0.1622 0.1294 0.2684 -0.0250 -0.1110 0.0114  402  GLU A C     
3759 O O     . GLU A 219 ? 0.2061 0.1266 0.2873 -0.0233 -0.0859 0.0183  402  GLU A O     
3760 C CB    . GLU A 219 ? 0.1260 0.1655 0.3040 -0.0067 -0.0892 0.0406  402  GLU A CB    
3761 C CG    . GLU A 219 ? 0.1377 0.1971 0.2982 -0.0281 -0.0986 0.0231  402  GLU A CG    
3762 C CD    . GLU A 219 ? 0.1546 0.2058 0.2961 -0.0055 -0.1111 0.0399  402  GLU A CD    
3763 O OE1   . GLU A 219 ? 0.1560 0.2041 0.3115 0.0068  -0.1065 0.0464  402  GLU A OE1   
3764 O OE2   . GLU A 219 ? 0.1734 0.2167 0.2896 -0.0080 -0.1107 0.0522  402  GLU A OE2   
3771 N N     . GLN A 220 ? 0.1563 0.1324 0.2640 -0.0142 -0.1116 0.0029  403  GLN A N     
3772 C CA    A GLN A 220 ? 0.1775 0.1510 0.2722 -0.0118 -0.1218 0.0017  403  GLN A CA    
3773 C CA    B GLN A 220 ? 0.1809 0.1399 0.2653 -0.0051 -0.1225 0.0161  403  GLN A CA    
3774 C C     . GLN A 220 ? 0.1778 0.1443 0.2748 -0.0207 -0.1244 0.0153  403  GLN A C     
3775 O O     . GLN A 220 ? 0.1694 0.1453 0.2834 -0.0212 -0.1213 0.0353  403  GLN A O     
3776 C CB    A GLN A 220 ? 0.2128 0.1867 0.3082 0.0094  -0.0958 -0.0002 403  GLN A CB    
3777 C CB    B GLN A 220 ? 0.2245 0.1499 0.2789 0.0277  -0.0966 0.0422  403  GLN A CB    
3778 C CG    A GLN A 220 ? 0.2186 0.2215 0.3580 0.0209  -0.0985 -0.0055 403  GLN A CG    
3779 C CG    B GLN A 220 ? 0.2578 0.1529 0.3086 0.0530  -0.0679 0.0573  403  GLN A CG    
3780 C CD    A GLN A 220 ? 0.2602 0.2600 0.3873 0.0154  -0.0774 0.0015  403  GLN A CD    
3781 C CD    B GLN A 220 ? 0.3266 0.1571 0.3461 0.0674  -0.0334 0.0457  403  GLN A CD    
3782 O OE1   A GLN A 220 ? 0.2705 0.2570 0.3951 0.0238  -0.0657 0.0013  403  GLN A OE1   
3783 O OE1   B GLN A 220 ? 0.3759 0.1517 0.3733 0.0872  0.0209  0.0444  403  GLN A OE1   
3784 N NE2   A GLN A 220 ? 0.2312 0.2952 0.3983 0.0016  -0.0786 -0.0012 403  GLN A NE2   
3785 N NE2   B GLN A 220 ? 0.3632 0.1720 0.3636 0.0523  -0.0418 0.0194  403  GLN A NE2   
3802 N N     . PHE A 221 ? 0.1744 0.1534 0.2747 -0.0215 -0.1196 0.0114  404  PHE A N     
3803 C CA    . PHE A 221 ? 0.2358 0.1589 0.2822 -0.0259 -0.1301 0.0233  404  PHE A CA    
3804 C C     . PHE A 221 ? 0.2295 0.1300 0.3196 -0.0070 -0.1580 0.0091  404  PHE A C     
3805 O O     . PHE A 221 ? 0.2883 0.1329 0.3761 0.0188  -0.1803 -0.0224 404  PHE A O     
3806 C CB    . PHE A 221 ? 0.2473 0.2027 0.3316 -0.0584 -0.1377 0.0248  404  PHE A CB    
3807 C CG    . PHE A 221 ? 0.2789 0.2537 0.3883 -0.0629 -0.1681 0.0292  404  PHE A CG    
3808 C CD1   . PHE A 221 ? 0.2917 0.2760 0.4144 -0.1006 -0.1641 0.0241  404  PHE A CD1   
3809 C CD2   . PHE A 221 ? 0.2566 0.2754 0.4509 -0.0508 -0.1517 0.0180  404  PHE A CD2   
3810 C CE1   . PHE A 221 ? 0.2886 0.2989 0.4444 -0.0898 -0.1674 0.0365  404  PHE A CE1   
3811 C CE2   . PHE A 221 ? 0.3168 0.2873 0.4874 -0.0752 -0.1354 -0.0004 404  PHE A CE2   
3812 C CZ    . PHE A 221 ? 0.3194 0.3015 0.4832 -0.0874 -0.1435 0.0167  404  PHE A CZ    
3822 N N     . MET A 222 ? 0.2015 0.1273 0.3286 -0.0202 -0.1387 0.0080  405  MET A N     
3823 C CA    . MET A 222 ? 0.2071 0.1505 0.3552 -0.0098 -0.1387 0.0059  405  MET A CA    
3824 C C     . MET A 222 ? 0.2164 0.1582 0.3565 0.0081  -0.1565 -0.0087 405  MET A C     
3825 O O     . MET A 222 ? 0.2443 0.1649 0.3729 -0.0096 -0.1364 -0.0232 405  MET A O     
3826 C CB    . MET A 222 ? 0.2148 0.1733 0.3552 -0.0213 -0.1202 0.0112  405  MET A CB    
3827 C CG    . MET A 222 ? 0.1890 0.2101 0.3539 -0.0114 -0.1072 0.0045  405  MET A CG    
3828 S SD    . MET A 222 ? 0.2322 0.2429 0.3824 -0.0120 -0.0847 -0.0271 405  MET A SD    
3829 C CE    . MET A 222 ? 0.2896 0.2735 0.3780 -0.0239 -0.0982 -0.0527 405  MET A CE    
3839 N N     . ASP A 223 ? 0.2219 0.1624 0.3767 0.0047  -0.1600 -0.0193 406  ASP A N     
3840 C CA    . ASP A 223 ? 0.2541 0.1873 0.3678 0.0156  -0.1764 -0.0073 406  ASP A CA    
3841 C C     . ASP A 223 ? 0.2239 0.1755 0.3619 0.0243  -0.1550 -0.0085 406  ASP A C     
3842 O O     . ASP A 223 ? 0.2404 0.1857 0.3681 0.0266  -0.1541 -0.0132 406  ASP A O     
3843 C CB    . ASP A 223 ? 0.3371 0.2467 0.3999 0.0527  -0.1999 0.0124  406  ASP A CB    
3844 C CG    . ASP A 223 ? 0.4215 0.3196 0.4737 0.0955  -0.2125 0.0338  406  ASP A CG    
3845 O OD1   . ASP A 223 ? 0.5385 0.3414 0.4747 0.1014  -0.1781 0.0309  406  ASP A OD1   
3846 O OD2   . ASP A 223 ? 0.4461 0.3624 0.5488 0.1097  -0.2087 0.0517  406  ASP A OD2   
3851 N N     . THR A 224 ? 0.1841 0.1553 0.3557 0.0000  -0.1370 -0.0001 407  THR A N     
3852 C CA    . THR A 224 ? 0.2007 0.1460 0.3321 -0.0061 -0.1450 0.0153  407  THR A CA    
3853 C C     . THR A 224 ? 0.2235 0.1416 0.3416 -0.0169 -0.1505 0.0413  407  THR A C     
3854 O O     . THR A 224 ? 0.2566 0.1573 0.3315 -0.0202 -0.1670 0.0430  407  THR A O     
3855 C CB    . THR A 224 ? 0.2000 0.1484 0.3519 -0.0066 -0.1446 0.0162  407  THR A CB    
3856 O OG1   . THR A 224 ? 0.2047 0.1615 0.3486 -0.0041 -0.1350 0.0108  407  THR A OG1   
3857 C CG2   . THR A 224 ? 0.2192 0.1494 0.4173 -0.0204 -0.1409 0.0333  407  THR A CG2   
3865 N N     . ASP A 225 ? 0.2334 0.1245 0.3437 -0.0336 -0.1337 0.0339  408  ASP A N     
3866 C CA    . ASP A 225 ? 0.2469 0.1398 0.3435 -0.0397 -0.1355 -0.0003 408  ASP A CA    
3867 C C     . ASP A 225 ? 0.2367 0.1531 0.3706 -0.0399 -0.1586 0.0403  408  ASP A C     
3868 O O     . ASP A 225 ? 0.2240 0.1602 0.3755 -0.0389 -0.1592 0.0585  408  ASP A O     
3869 C CB    . ASP A 225 ? 0.2400 0.1564 0.3390 -0.0184 -0.1238 -0.0184 408  ASP A CB    
3870 C CG    . ASP A 225 ? 0.2530 0.1810 0.3904 -0.0040 -0.1229 -0.0070 408  ASP A CG    
3871 O OD1   . ASP A 225 ? 0.2530 0.1821 0.4441 -0.0100 -0.1289 -0.0212 408  ASP A OD1   
3872 O OD2   . ASP A 225 ? 0.2777 0.1957 0.3960 0.0019  -0.0945 0.0097  408  ASP A OD2   
3877 N N     . ASN A 226 ? 0.2229 0.1473 0.4015 -0.0388 -0.1541 0.0469  409  ASN A N     
3878 C CA    . ASN A 226 ? 0.2352 0.1642 0.4028 -0.0494 -0.1617 0.0599  409  ASN A CA    
3879 C C     . ASN A 226 ? 0.1994 0.1738 0.3754 -0.0344 -0.1434 0.0576  409  ASN A C     
3880 O O     . ASN A 226 ? 0.1927 0.1862 0.3975 -0.0428 -0.1130 0.0539  409  ASN A O     
3881 C CB    . ASN A 226 ? 0.2766 0.1727 0.4024 -0.0530 -0.1838 0.0513  409  ASN A CB    
3882 C CG    . ASN A 226 ? 0.2948 0.1923 0.4115 -0.0407 -0.1994 0.0369  409  ASN A CG    
3883 O OD1   . ASN A 226 ? 0.3281 0.1937 0.4434 -0.0285 -0.1750 0.0209  409  ASN A OD1   
3884 N ND2   . ASN A 226 ? 0.3087 0.2134 0.3989 -0.0482 -0.2010 0.0298  409  ASN A ND2   
3891 N N     . PHE A 227 ? 0.2097 0.1734 0.3451 -0.0407 -0.1206 0.0648  410  PHE A N     
3892 C CA    . PHE A 227 ? 0.2430 0.1914 0.3422 -0.0359 -0.1353 0.0482  410  PHE A CA    
3893 C C     . PHE A 227 ? 0.1975 0.1802 0.3092 -0.0259 -0.1292 0.0181  410  PHE A C     
3894 O O     . PHE A 227 ? 0.2160 0.1903 0.3457 -0.0143 -0.1061 0.0147  410  PHE A O     
3895 C CB    . PHE A 227 ? 0.3397 0.2197 0.4044 -0.0277 -0.1628 0.0879  410  PHE A CB    
3896 C CG    . PHE A 227 ? 0.3655 0.2599 0.5168 -0.0197 -0.1724 0.1356  410  PHE A CG    
3897 C CD1   . PHE A 227 ? 0.3581 0.2798 0.5573 -0.0043 -0.1897 0.1406  410  PHE A CD1   
3898 C CD2   . PHE A 227 ? 0.4077 0.2805 0.5949 -0.0178 -0.1521 0.1690  410  PHE A CD2   
3899 C CE1   . PHE A 227 ? 0.3971 0.2980 0.6023 0.0004  -0.1885 0.1541  410  PHE A CE1   
3900 C CE2   . PHE A 227 ? 0.4455 0.2974 0.6297 0.0019  -0.1536 0.1866  410  PHE A CE2   
3901 C CZ    . PHE A 227 ? 0.4329 0.3060 0.6294 0.0138  -0.1671 0.1787  410  PHE A CZ    
3911 N N     . GLU A 228 ? 0.1699 0.1611 0.2850 -0.0307 -0.1173 0.0107  411  GLU A N     
3912 C CA    . GLU A 228 ? 0.1660 0.1492 0.2784 -0.0178 -0.1177 0.0038  411  GLU A CA    
3913 C C     . GLU A 228 ? 0.1550 0.1526 0.3010 -0.0154 -0.1139 0.0098  411  GLU A C     
3914 O O     . GLU A 228 ? 0.1808 0.1569 0.3256 -0.0166 -0.1063 0.0303  411  GLU A O     
3915 C CB    . GLU A 228 ? 0.1809 0.1543 0.2743 -0.0337 -0.1112 -0.0147 411  GLU A CB    
3916 C CG    . GLU A 228 ? 0.2152 0.1804 0.3290 -0.0339 -0.1318 -0.0142 411  GLU A CG    
3917 C CD    . GLU A 228 ? 0.2325 0.2164 0.3751 -0.0366 -0.1420 -0.0355 411  GLU A CD    
3918 O OE1   . GLU A 228 ? 0.2916 0.1887 0.3510 -0.0146 -0.1588 -0.0183 411  GLU A OE1   
3919 O OE2   . GLU A 228 ? 0.2609 0.2853 0.4174 -0.0574 -0.1175 -0.1086 411  GLU A OE2   
3926 N N     . ASP A 229 ? 0.1415 0.1662 0.2815 -0.0405 -0.0782 0.0252  412  ASP A N     
3927 C CA    A ASP A 229 ? 0.1468 0.1768 0.2295 -0.0587 -0.0670 0.0158  412  ASP A CA    
3928 C CA    B ASP A 229 ? 0.1546 0.1841 0.2491 -0.0447 -0.0881 0.0266  412  ASP A CA    
3929 C C     . ASP A 229 ? 0.1313 0.1590 0.1980 -0.0333 -0.0877 0.0203  412  ASP A C     
3930 O O     . ASP A 229 ? 0.1376 0.1886 0.2152 -0.0581 -0.0813 0.0271  412  ASP A O     
3931 C CB    A ASP A 229 ? 0.2155 0.2293 0.2260 -0.0678 -0.0459 0.0072  412  ASP A CB    
3932 C CB    B ASP A 229 ? 0.1948 0.2419 0.2666 -0.0445 -0.1139 0.0387  412  ASP A CB    
3933 C CG    A ASP A 229 ? 0.2495 0.2688 0.2735 -0.0822 -0.0642 -0.0124 412  ASP A CG    
3934 C CG    B ASP A 229 ? 0.2169 0.2966 0.3053 -0.0544 -0.1406 0.0522  412  ASP A CG    
3935 O OD1   A ASP A 229 ? 0.2214 0.2791 0.2827 -0.0722 -0.0996 -0.0034 412  ASP A OD1   
3936 O OD1   B ASP A 229 ? 0.2410 0.3148 0.3015 -0.0602 -0.1502 0.0520  412  ASP A OD1   
3937 O OD2   A ASP A 229 ? 0.2734 0.2871 0.2940 -0.1227 -0.0754 -0.0403 412  ASP A OD2   
3938 O OD2   B ASP A 229 ? 0.2176 0.3232 0.3560 -0.0583 -0.1345 0.0781  412  ASP A OD2   
3947 N N     . VAL A 230 ? 0.1136 0.1119 0.2018 -0.0182 -0.0799 0.0052  413  VAL A N     
3948 C CA    . VAL A 230 ? 0.1264 0.0887 0.2211 -0.0260 -0.0777 0.0114  413  VAL A CA    
3949 C C     . VAL A 230 ? 0.1012 0.0837 0.2088 -0.0165 -0.0698 0.0095  413  VAL A C     
3950 O O     . VAL A 230 ? 0.1100 0.0883 0.2571 -0.0124 -0.0761 0.0074  413  VAL A O     
3951 C CB    . VAL A 230 ? 0.1485 0.0997 0.2465 -0.0178 -0.0913 0.0117  413  VAL A CB    
3952 C CG1   . VAL A 230 ? 0.1587 0.1294 0.2139 0.0006  -0.0562 -0.0029 413  VAL A CG1   
3953 C CG2   . VAL A 230 ? 0.1375 0.1005 0.2996 -0.0087 -0.0954 0.0132  413  VAL A CG2   
3963 N N     . LYS A 231 ? 0.1051 0.0834 0.2175 -0.0099 -0.0752 0.0022  414  LYS A N     
3964 C CA    . LYS A 231 ? 0.1169 0.0857 0.2307 -0.0206 -0.0677 0.0025  414  LYS A CA    
3965 C C     . LYS A 231 ? 0.0984 0.0685 0.2250 -0.0005 -0.0729 -0.0012 414  LYS A C     
3966 O O     . LYS A 231 ? 0.1137 0.0799 0.2098 -0.0143 -0.0718 -0.0052 414  LYS A O     
3967 C CB    . LYS A 231 ? 0.1439 0.1416 0.2908 0.0245  -0.0692 0.0080  414  LYS A CB    
3968 C CG    . LYS A 231 ? 0.3013 0.2295 0.3676 0.0345  -0.0375 0.0111  414  LYS A CG    
3969 C CD    . LYS A 231 ? 0.4713 0.3091 0.4508 0.0067  0.0037  -0.0214 414  LYS A CD    
3970 C CE    . LYS A 231 ? 0.5042 0.3537 0.4948 -0.0313 0.0264  -0.0645 414  LYS A CE    
3971 N NZ    . LYS A 231 ? 0.4913 0.3775 0.5357 -0.0558 0.0100  -0.0968 414  LYS A NZ    
3985 N N     . ALA A 232 ? 0.0968 0.0800 0.1962 -0.0066 -0.0664 -0.0119 415  ALA A N     
3986 C CA    . ALA A 232 ? 0.1022 0.0840 0.1896 -0.0030 -0.0727 -0.0122 415  ALA A CA    
3987 C C     . ALA A 232 ? 0.0963 0.0819 0.1891 -0.0148 -0.0624 -0.0058 415  ALA A C     
3988 O O     . ALA A 232 ? 0.1005 0.0964 0.1941 -0.0149 -0.0670 -0.0097 415  ALA A O     
3989 C CB    . ALA A 232 ? 0.0867 0.1025 0.2260 0.0180  -0.0566 -0.0127 415  ALA A CB    
3995 N N     . TYR A 233 ? 0.1099 0.0737 0.1900 -0.0123 -0.0695 -0.0061 416  TYR A N     
3996 C CA    . TYR A 233 ? 0.1078 0.0741 0.2287 0.0006  -0.0793 -0.0074 416  TYR A CA    
3997 C C     . TYR A 233 ? 0.1347 0.0761 0.2449 0.0094  -0.0775 -0.0040 416  TYR A C     
3998 O O     . TYR A 233 ? 0.1977 0.0979 0.2592 -0.0260 -0.0813 -0.0225 416  TYR A O     
3999 C CB    . TYR A 233 ? 0.1208 0.0757 0.2318 0.0045  -0.0896 -0.0071 416  TYR A CB    
4000 C CG    . TYR A 233 ? 0.1105 0.1062 0.2574 0.0064  -0.0816 -0.0067 416  TYR A CG    
4001 C CD1   . TYR A 233 ? 0.0899 0.1170 0.2712 0.0076  -0.0578 -0.0073 416  TYR A CD1   
4002 C CD2   . TYR A 233 ? 0.1403 0.1225 0.3246 0.0070  -0.0577 -0.0128 416  TYR A CD2   
4003 C CE1   . TYR A 233 ? 0.0959 0.1399 0.3242 0.0135  -0.0348 -0.0016 416  TYR A CE1   
4004 C CE2   . TYR A 233 ? 0.1860 0.1401 0.3500 0.0220  -0.0082 -0.0096 416  TYR A CE2   
4005 C CZ    . TYR A 233 ? 0.1712 0.1596 0.3068 0.0217  0.0743  -0.0002 416  TYR A CZ    
4006 O OH    . TYR A 233 ? 0.2750 0.1975 0.3324 0.0002  0.1269  -0.0092 416  TYR A OH    
4016 N N     . THR A 234 ? 0.0891 0.0674 0.2143 -0.0003 -0.0627 0.0112  417  THR A N     
4017 C CA    . THR A 234 ? 0.0918 0.0816 0.2039 -0.0014 -0.0540 -0.0115 417  THR A CA    
4018 C C     . THR A 234 ? 0.1033 0.0725 0.2096 -0.0035 -0.0608 -0.0228 417  THR A C     
4019 O O     . THR A 234 ? 0.1242 0.0676 0.2323 0.0017  -0.0698 -0.0083 417  THR A O     
4020 C CB    . THR A 234 ? 0.0977 0.0840 0.2356 -0.0116 -0.0592 0.0121  417  THR A CB    
4021 O OG1   . THR A 234 ? 0.0997 0.0864 0.2326 -0.0093 -0.0726 0.0102  417  THR A OG1   
4022 C CG2   . THR A 234 ? 0.0987 0.0913 0.2538 0.0073  -0.0620 0.0170  417  THR A CG2   
4030 N N     . ILE A 235 ? 0.1091 0.0747 0.2182 0.0123  -0.0580 -0.0227 418  ILE A N     
4031 C CA    . ILE A 235 ? 0.1459 0.0905 0.2418 0.0209  -0.0832 -0.0037 418  ILE A CA    
4032 C C     . ILE A 235 ? 0.1604 0.0917 0.2421 0.0175  -0.0779 -0.0112 418  ILE A C     
4033 O O     . ILE A 235 ? 0.1543 0.1191 0.2446 -0.0015 -0.0491 -0.0091 418  ILE A O     
4034 C CB    . ILE A 235 ? 0.1567 0.1049 0.2309 0.0145  -0.0717 0.0115  418  ILE A CB    
4035 C CG1   . ILE A 235 ? 0.1613 0.1228 0.2315 0.0225  -0.0643 0.0066  418  ILE A CG1   
4036 C CG2   . ILE A 235 ? 0.1710 0.1116 0.2390 0.0248  -0.0629 0.0282  418  ILE A CG2   
4037 C CD1   . ILE A 235 ? 0.1528 0.1526 0.2666 0.0154  -0.0932 0.0204  418  ILE A CD1   
4049 N N     . GLY A 236 ? 0.1575 0.0880 0.2845 -0.0029 -0.0782 -0.0063 419  GLY A N     
4050 C CA    . GLY A 236 ? 0.1631 0.0988 0.2893 -0.0083 -0.0735 -0.0013 419  GLY A CA    
4051 C C     . GLY A 236 ? 0.1529 0.1203 0.2931 -0.0048 -0.0794 0.0223  419  GLY A C     
4052 O O     . GLY A 236 ? 0.2294 0.1176 0.3090 0.0106  -0.0642 0.0284  419  GLY A O     
4056 N N     . GLU A 237 ? 0.1376 0.1439 0.2824 0.0032  -0.0594 0.0277  420  GLU A N     
4057 C CA    . GLU A 237 ? 0.1437 0.1749 0.2852 0.0028  -0.0439 0.0183  420  GLU A CA    
4058 C C     . GLU A 237 ? 0.1729 0.1671 0.2677 0.0274  -0.0350 0.0187  420  GLU A C     
4059 O O     . GLU A 237 ? 0.1956 0.1847 0.2788 0.0538  -0.0298 0.0243  420  GLU A O     
4060 C CB    . GLU A 237 ? 0.1797 0.2178 0.3277 -0.0112 -0.0629 0.0221  420  GLU A CB    
4061 C CG    . GLU A 237 ? 0.1736 0.2619 0.3906 -0.0462 -0.1024 0.0293  420  GLU A CG    
4062 C CD    . GLU A 237 ? 0.2881 0.3226 0.4539 -0.0689 -0.0898 0.0490  420  GLU A CD    
4063 O OE1   . GLU A 237 ? 0.3181 0.3585 0.4348 -0.0780 -0.0097 0.0415  420  GLU A OE1   
4064 O OE2   . GLU A 237 ? 0.3514 0.3398 0.5188 -0.1023 -0.1476 0.1076  420  GLU A OE2   
4071 N N     . ASN A 238 ? 0.1516 0.1507 0.2856 0.0195  -0.0345 -0.0078 421  ASN A N     
4072 C CA    . ASN A 238 ? 0.1797 0.1618 0.3099 0.0005  -0.0677 -0.0258 421  ASN A CA    
4073 C C     . ASN A 238 ? 0.1794 0.1362 0.2878 0.0015  -0.0618 -0.0331 421  ASN A C     
4074 O O     . ASN A 238 ? 0.2343 0.1545 0.2875 -0.0171 -0.0292 -0.0409 421  ASN A O     
4075 C CB    . ASN A 238 ? 0.2268 0.2127 0.3378 0.0010  -0.0292 -0.0215 421  ASN A CB    
4076 C CG    . ASN A 238 ? 0.3037 0.2799 0.3753 0.0062  0.0384  -0.0026 421  ASN A CG    
4077 O OD1   . ASN A 238 ? 0.3888 0.3113 0.4367 0.0029  0.0454  0.0090  421  ASN A OD1   
4078 N ND2   . ASN A 238 ? 0.2816 0.3086 0.3815 0.0204  0.0283  0.0029  421  ASN A ND2   
4085 N N     . PHE A 239 ? 0.1705 0.1090 0.2721 0.0027  -0.0698 -0.0236 422  PHE A N     
4086 C CA    . PHE A 239 ? 0.1335 0.0825 0.2366 -0.0076 -0.0437 -0.0055 422  PHE A CA    
4087 C C     . PHE A 239 ? 0.1175 0.0803 0.2493 -0.0125 -0.0430 -0.0012 422  PHE A C     
4088 O O     . PHE A 239 ? 0.1189 0.0838 0.2552 -0.0172 -0.0415 0.0054  422  PHE A O     
4089 C CB    . PHE A 239 ? 0.1339 0.0929 0.2533 -0.0059 -0.0491 0.0042  422  PHE A CB    
4090 C CG    . PHE A 239 ? 0.1336 0.0973 0.2834 0.0015  -0.0941 0.0168  422  PHE A CG    
4091 C CD1   . PHE A 239 ? 0.1259 0.0970 0.3068 -0.0042 -0.0926 0.0086  422  PHE A CD1   
4092 C CD2   . PHE A 239 ? 0.1637 0.1126 0.3184 -0.0112 -0.1198 0.0099  422  PHE A CD2   
4093 C CE1   . PHE A 239 ? 0.1279 0.1075 0.3056 0.0001  -0.0612 0.0003  422  PHE A CE1   
4094 C CE2   . PHE A 239 ? 0.1555 0.1295 0.3393 -0.0136 -0.1107 0.0069  422  PHE A CE2   
4095 C CZ    . PHE A 239 ? 0.1435 0.1247 0.3489 -0.0114 -0.0707 0.0001  422  PHE A CZ    
4105 N N     . CYS A 240 ? 0.1290 0.0779 0.2588 -0.0076 -0.0507 -0.0103 423  CYS A N     
4106 C CA    A CYS A 240 ? 0.1326 0.0921 0.2723 -0.0126 -0.0657 -0.0045 423  CYS A CA    
4107 C CA    B CYS A 240 ? 0.1481 0.0977 0.2743 -0.0018 -0.0601 -0.0098 423  CYS A CA    
4108 C C     . CYS A 240 ? 0.1357 0.0967 0.2773 -0.0245 -0.0576 -0.0188 423  CYS A C     
4109 O O     . CYS A 240 ? 0.2048 0.1168 0.3521 -0.0384 0.0097  -0.0573 423  CYS A O     
4110 C CB    A CYS A 240 ? 0.1217 0.1281 0.2796 -0.0077 -0.0900 0.0084  423  CYS A CB    
4111 C CB    B CYS A 240 ? 0.1838 0.1273 0.2886 0.0284  -0.0721 -0.0001 423  CYS A CB    
4112 S SG    A CYS A 240 ? 0.1229 0.1635 0.2696 -0.0039 -0.0876 0.0126  423  CYS A SG    
4113 S SG    B CYS A 240 ? 0.2139 0.1522 0.2943 0.0563  -0.0706 0.0037  423  CYS A SG    
4124 N N     . HIS A 241 ? 0.1346 0.0902 0.2385 -0.0243 -0.0848 0.0127  424  HIS A N     
4125 C CA    . HIS A 241 ? 0.1145 0.0916 0.2194 -0.0204 -0.0751 0.0046  424  HIS A CA    
4126 C C     . HIS A 241 ? 0.1194 0.0851 0.2240 -0.0153 -0.0760 -0.0045 424  HIS A C     
4127 O O     . HIS A 241 ? 0.1852 0.0982 0.2300 -0.0298 -0.0910 -0.0087 424  HIS A O     
4128 C CB    . HIS A 241 ? 0.1354 0.0907 0.2595 -0.0113 -0.0990 0.0124  424  HIS A CB    
4129 C CG    . HIS A 241 ? 0.1484 0.0905 0.2856 -0.0047 -0.1048 0.0005  424  HIS A CG    
4130 N ND1   . HIS A 241 ? 0.1652 0.1150 0.3082 -0.0189 -0.1126 0.0049  424  HIS A ND1   
4131 C CD2   . HIS A 241 ? 0.1296 0.0974 0.2838 0.0000  -0.0881 0.0039  424  HIS A CD2   
4132 C CE1   . HIS A 241 ? 0.1483 0.1240 0.3250 -0.0135 -0.0693 -0.0096 424  HIS A CE1   
4133 N NE2   . HIS A 241 ? 0.1258 0.1110 0.3044 -0.0175 -0.0396 0.0039  424  HIS A NE2   
4141 N N     . ALA A 242 ? 0.1082 0.0720 0.2090 -0.0144 -0.0739 0.0166  425  ALA A N     
4142 C CA    . ALA A 242 ? 0.0924 0.0851 0.2039 -0.0252 -0.0554 0.0202  425  ALA A CA    
4143 C C     . ALA A 242 ? 0.1010 0.0696 0.1934 -0.0142 -0.0666 0.0062  425  ALA A C     
4144 O O     . ALA A 242 ? 0.1357 0.0951 0.2059 -0.0227 -0.0835 -0.0027 425  ALA A O     
4145 C CB    . ALA A 242 ? 0.1029 0.1048 0.2368 -0.0017 -0.0738 0.0233  425  ALA A CB    
4151 N N     . GLU A 243 ? 0.1031 0.0761 0.1784 -0.0188 -0.0655 0.0031  426  GLU A N     
4152 C CA    . GLU A 243 ? 0.1082 0.0986 0.2056 -0.0271 -0.0692 0.0102  426  GLU A CA    
4153 C C     . GLU A 243 ? 0.1185 0.1114 0.1994 -0.0423 -0.0632 0.0085  426  GLU A C     
4154 O O     . GLU A 243 ? 0.1835 0.1307 0.2158 -0.0583 -0.0939 0.0183  426  GLU A O     
4155 C CB    . GLU A 243 ? 0.1149 0.1112 0.2728 -0.0006 -0.0743 0.0105  426  GLU A CB    
4156 C CG    . GLU A 243 ? 0.1185 0.1493 0.3388 0.0051  -0.0777 0.0127  426  GLU A CG    
4157 C CD    . GLU A 243 ? 0.1654 0.2017 0.4007 0.0371  -0.0231 0.0503  426  GLU A CD    
4158 O OE1   . GLU A 243 ? 0.2594 0.2281 0.3945 0.0719  0.0623  0.0478  426  GLU A OE1   
4159 O OE2   . GLU A 243 ? 0.1711 0.2098 0.4575 0.0220  -0.0690 0.0647  426  GLU A OE2   
4166 N N     . THR A 244 ? 0.1071 0.1124 0.2043 -0.0351 -0.0640 0.0109  427  THR A N     
4167 C CA    . THR A 244 ? 0.1220 0.1251 0.2066 -0.0359 -0.0777 0.0130  427  THR A CA    
4168 C C     . THR A 244 ? 0.1233 0.1531 0.2104 -0.0463 -0.0756 0.0185  427  THR A C     
4169 O O     . THR A 244 ? 0.1195 0.1680 0.2284 -0.0405 -0.0780 0.0168  427  THR A O     
4170 C CB    . THR A 244 ? 0.1357 0.1270 0.2351 -0.0346 -0.0848 0.0032  427  THR A CB    
4171 O OG1   . THR A 244 ? 0.1815 0.1207 0.2616 -0.0303 -0.1155 0.0084  427  THR A OG1   
4172 C CG2   . THR A 244 ? 0.1589 0.1332 0.2644 -0.0176 -0.0960 -0.0050 427  THR A CG2   
4180 N N     . ARG A 245 ? 0.1389 0.1812 0.2116 -0.0455 -0.0818 0.0068  428  ARG A N     
4181 C CA    . ARG A 245 ? 0.1451 0.2247 0.2369 -0.0286 -0.0756 0.0100  428  ARG A CA    
4182 C C     . ARG A 245 ? 0.1399 0.2180 0.2329 -0.0357 -0.0955 0.0268  428  ARG A C     
4183 O O     . ARG A 245 ? 0.1203 0.2059 0.2524 -0.0237 -0.0867 0.0185  428  ARG A O     
4184 C CB    . ARG A 245 ? 0.2051 0.2955 0.3131 -0.0191 -0.0885 0.0023  428  ARG A CB    
4185 C CG    . ARG A 245 ? 0.3043 0.3725 0.4261 -0.0451 -0.0886 -0.0123 428  ARG A CG    
4186 C CD    . ARG A 245 ? 0.4327 0.4639 0.5552 -0.0857 -0.1008 -0.0128 428  ARG A CD    
4187 N NE    . ARG A 245 ? 0.4906 0.5435 0.6513 -0.1282 -0.1303 0.0029  428  ARG A NE    
4188 C CZ    . ARG A 245 ? 0.4801 0.5968 0.7145 -0.1578 -0.1743 0.0203  428  ARG A CZ    
4189 N NH1   . ARG A 245 ? 0.4726 0.6069 0.7654 -0.1609 -0.1837 0.0230  428  ARG A NH1   
4190 N NH2   . ARG A 245 ? 0.4678 0.6233 0.7188 -0.1699 -0.1717 0.0308  428  ARG A NH2   
4204 N N     . LYS A 246 ? 0.1456 0.2341 0.2413 -0.0423 -0.0848 0.0466  429  LYS A N     
4205 C CA    . LYS A 246 ? 0.1564 0.2476 0.2676 -0.0623 -0.0979 0.0499  429  LYS A CA    
4206 C C     . LYS A 246 ? 0.1676 0.2520 0.2533 -0.0512 -0.0948 0.0201  429  LYS A C     
4207 O O     . LYS A 246 ? 0.1849 0.2808 0.2772 -0.0145 -0.0867 0.0040  429  LYS A O     
4208 C CB    . LYS A 246 ? 0.1834 0.2734 0.2984 -0.0521 -0.1203 0.0720  429  LYS A CB    
4209 C CG    . LYS A 246 ? 0.2607 0.3133 0.3194 -0.0465 -0.1327 0.0871  429  LYS A CG    
4210 C CD    . LYS A 246 ? 0.3851 0.3499 0.3503 -0.0570 -0.1334 0.0683  429  LYS A CD    
4211 C CE    . LYS A 246 ? 0.4552 0.3676 0.3614 -0.0701 -0.1881 0.0693  429  LYS A CE    
4212 N NZ    . LYS A 246 ? 0.4830 0.3769 0.3793 -0.0747 -0.2049 0.0693  429  LYS A NZ    
4226 N N     . SER A 247 ? 0.1718 0.2398 0.2563 -0.0518 -0.0938 0.0088  430  SER A N     
4227 C CA    . SER A 247 ? 0.1845 0.2567 0.2761 -0.0562 -0.0964 0.0056  430  SER A CA    
4228 C C     . SER A 247 ? 0.2089 0.2634 0.2674 -0.0392 -0.1063 0.0254  430  SER A C     
4229 O O     . SER A 247 ? 0.2044 0.2587 0.2754 -0.0430 -0.1053 0.0123  430  SER A O     
4230 C CB    . SER A 247 ? 0.1832 0.2822 0.2724 -0.0924 -0.0751 -0.0122 430  SER A CB    
4231 O OG    . SER A 247 ? 0.2368 0.3076 0.2840 -0.0955 -0.1082 -0.0122 430  SER A OG    
4237 N N     . PRO A 248 ? 0.2306 0.2834 0.2981 -0.0310 -0.1190 0.0473  431  PRO A N     
4238 C CA    . PRO A 248 ? 0.2879 0.2995 0.3073 -0.0285 -0.1245 0.0472  431  PRO A CA    
4239 C C     . PRO A 248 ? 0.3028 0.2892 0.2980 -0.0477 -0.1291 0.0465  431  PRO A C     
4240 O O     . PRO A 248 ? 0.3526 0.2884 0.3261 -0.0667 -0.1192 0.0390  431  PRO A O     
4241 C CB    . PRO A 248 ? 0.3183 0.3097 0.3340 -0.0157 -0.0980 0.0382  431  PRO A CB    
4242 C CG    . PRO A 248 ? 0.2994 0.3011 0.3251 -0.0096 -0.0873 0.0436  431  PRO A CG    
4243 C CD    . PRO A 248 ? 0.2534 0.2842 0.3054 -0.0307 -0.0993 0.0540  431  PRO A CD    
4251 N N     . VAL A 249 ? 0.2650 0.2779 0.2802 -0.0744 -0.1106 0.0482  432  VAL A N     
4252 C CA    . VAL A 249 ? 0.2934 0.2813 0.3059 -0.0860 -0.1450 0.0482  432  VAL A CA    
4253 C C     . VAL A 249 ? 0.3151 0.3103 0.3613 -0.0774 -0.1919 0.0758  432  VAL A C     
4254 O O     . VAL A 249 ? 0.3307 0.3304 0.3502 -0.0738 -0.1880 0.0702  432  VAL A O     
4255 C CB    . VAL A 249 ? 0.2960 0.2663 0.3178 -0.0770 -0.1719 0.0384  432  VAL A CB    
4256 C CG1   . VAL A 249 ? 0.3466 0.2500 0.3179 -0.0511 -0.1642 0.0448  432  VAL A CG1   
4257 C CG2   . VAL A 249 ? 0.3125 0.2803 0.3518 -0.0810 -0.1866 0.0533  432  VAL A CG2   
4267 N N     . VAL A 250 ? 0.3307 0.3209 0.3965 -0.0642 -0.2023 0.1078  433  VAL A N     
4268 C CA    . VAL A 250 ? 0.3891 0.3453 0.4282 -0.0564 -0.2175 0.1211  433  VAL A CA    
4269 C C     . VAL A 250 ? 0.4353 0.3749 0.3940 -0.0975 -0.2236 0.1376  433  VAL A C     
4270 O O     . VAL A 250 ? 0.4724 0.3813 0.3923 -0.1075 -0.2125 0.1643  433  VAL A O     
4271 C CB    . VAL A 250 ? 0.4413 0.3368 0.5089 -0.0139 -0.1502 0.1251  433  VAL A CB    
4272 C CG1   . VAL A 250 ? 0.4964 0.3333 0.5471 0.0067  -0.1099 0.1166  433  VAL A CG1   
4273 C CG2   . VAL A 250 ? 0.4509 0.3375 0.5331 0.0004  -0.1193 0.1376  433  VAL A CG2   
4283 N N     . ASP A 251 ? 0.4667 0.4093 0.4081 -0.1016 -0.2209 0.1168  434  ASP A N     
4284 C CA    . ASP A 251 ? 0.5238 0.4601 0.4083 -0.0860 -0.2433 0.0959  434  ASP A CA    
4285 C C     . ASP A 251 ? 0.4887 0.4887 0.3886 -0.0780 -0.2288 0.1077  434  ASP A C     
4286 O O     . ASP A 251 ? 0.5222 0.4920 0.4078 -0.1031 -0.1647 0.1186  434  ASP A O     
4287 C CB    . ASP A 251 ? 0.5993 0.4889 0.4395 -0.0836 -0.2664 0.0728  434  ASP A CB    
4288 C CG    . ASP A 251 ? 0.6715 0.5123 0.4434 -0.0829 -0.2875 0.0612  434  ASP A CG    
4289 O OD1   . ASP A 251 ? 0.6919 0.5205 0.4068 -0.0876 -0.2885 0.0594  434  ASP A OD1   
4290 O OD2   . ASP A 251 ? 0.7286 0.5234 0.4797 -0.0644 -0.2794 0.0583  434  ASP A OD2   
4295 N N     . GLY A 252 ? 0.4372 0.5155 0.3812 -0.0509 -0.2209 0.1184  435  GLY A N     
4296 C CA    . GLY A 252 ? 0.3996 0.5593 0.4066 -0.0230 -0.2123 0.1244  435  GLY A CA    
4297 C C     . GLY A 252 ? 0.3881 0.6081 0.4533 -0.0202 -0.1898 0.1212  435  GLY A C     
4298 O O     . GLY A 252 ? 0.3837 0.6331 0.5154 0.0097  -0.1718 0.1147  435  GLY A O     
4302 N N     . ILE A 253 ? 0.3644 0.6263 0.4066 -0.0555 -0.1949 0.1256  436  ILE A N     
4303 C CA    . ILE A 253 ? 0.4029 0.6548 0.3920 -0.0653 -0.1791 0.1416  436  ILE A CA    
4304 C C     . ILE A 253 ? 0.3597 0.6663 0.3405 -0.0731 -0.1513 0.1365  436  ILE A C     
4305 O O     . ILE A 253 ? 0.3365 0.6697 0.3219 -0.1058 -0.1029 0.1234  436  ILE A O     
4306 C CB    . ILE A 253 ? 0.4857 0.6736 0.4538 -0.0585 -0.1784 0.1504  436  ILE A CB    
4307 C CG1   . ILE A 253 ? 0.5341 0.6856 0.4898 -0.0494 -0.1474 0.1523  436  ILE A CG1   
4308 C CG2   . ILE A 253 ? 0.4979 0.6760 0.4664 -0.0541 -0.1964 0.1603  436  ILE A CG2   
4309 C CD1   . ILE A 253 ? 0.5457 0.6909 0.5098 -0.0406 -0.1585 0.1529  436  ILE A CD1   
4321 N N     . VAL A 254 ? 0.3418 0.6704 0.3372 -0.0436 -0.1389 0.1386  437  VAL A N     
4322 C CA    . VAL A 254 ? 0.3000 0.6741 0.3846 -0.0388 -0.1394 0.1226  437  VAL A CA    
4323 C C     . VAL A 254 ? 0.2665 0.6522 0.4020 -0.0435 -0.0865 0.1133  437  VAL A C     
4324 O O     . VAL A 254 ? 0.3272 0.6764 0.4313 -0.0716 -0.0690 0.0998  437  VAL A O     
4325 C CB    . VAL A 254 ? 0.3491 0.6987 0.4574 -0.0392 -0.1454 0.1040  437  VAL A CB    
4326 C CG1   . VAL A 254 ? 0.3892 0.7080 0.5086 -0.0404 -0.1169 0.0954  437  VAL A CG1   
4327 C CG2   . VAL A 254 ? 0.3750 0.7093 0.4828 -0.0335 -0.1529 0.0937  437  VAL A CG2   
4337 N N     . ARG A 255 ? 0.1967 0.6032 0.4208 0.0052  -0.0786 0.1229  438  ARG A N     
4338 C CA    . ARG A 255 ? 0.2121 0.5717 0.4446 0.0259  -0.0682 0.1274  438  ARG A CA    
4339 C C     . ARG A 255 ? 0.1634 0.5364 0.3923 0.0321  -0.0263 0.1296  438  ARG A C     
4340 O O     . ARG A 255 ? 0.1711 0.5121 0.3517 0.0525  -0.0288 0.1355  438  ARG A O     
4341 C CB    . ARG A 255 ? 0.2929 0.5806 0.5325 0.0487  -0.0824 0.1122  438  ARG A CB    
4342 C CG    . ARG A 255 ? 0.3702 0.6043 0.6066 0.0497  -0.1027 0.0801  438  ARG A CG    
4343 C CD    . ARG A 255 ? 0.4837 0.6378 0.6577 0.0429  -0.1004 0.0492  438  ARG A CD    
4344 N NE    . ARG A 255 ? 0.5637 0.6675 0.6757 0.0247  -0.0975 0.0265  438  ARG A NE    
4345 C CZ    . ARG A 255 ? 0.5862 0.6882 0.6746 0.0095  -0.1166 0.0120  438  ARG A CZ    
4346 N NH1   . ARG A 255 ? 0.5739 0.6920 0.6623 0.0042  -0.1168 0.0063  438  ARG A NH1   
4347 N NH2   . ARG A 255 ? 0.6240 0.7000 0.6957 0.0056  -0.1192 0.0063  438  ARG A NH2   
4361 N N     . ARG A 256 ? 0.1627 0.5235 0.3910 0.0336  -0.0228 0.1187  439  ARG A N     
4362 C CA    . ARG A 256 ? 0.1796 0.5028 0.4096 0.0278  -0.0813 0.0923  439  ARG A CA    
4363 C C     . ARG A 256 ? 0.1640 0.4521 0.4468 0.0552  -0.0631 0.0826  439  ARG A C     
4364 O O     . ARG A 256 ? 0.1716 0.4565 0.5165 0.0568  -0.0263 0.1100  439  ARG A O     
4365 C CB    . ARG A 256 ? 0.2361 0.5398 0.4061 -0.0165 -0.0882 0.0584  439  ARG A CB    
4366 C CG    . ARG A 256 ? 0.3135 0.5805 0.4388 -0.0409 -0.1179 0.0119  439  ARG A CG    
4367 C CD    . ARG A 256 ? 0.3885 0.6219 0.4987 -0.0605 -0.1187 -0.0228 439  ARG A CD    
4368 N NE    . ARG A 256 ? 0.4573 0.6536 0.5412 -0.0777 -0.1278 -0.0435 439  ARG A NE    
4369 C CZ    . ARG A 256 ? 0.5217 0.6774 0.6006 -0.0790 -0.1108 -0.0444 439  ARG A CZ    
4370 N NH1   . ARG A 256 ? 0.5580 0.6833 0.6230 -0.0636 -0.0804 -0.0396 439  ARG A NH1   
4371 N NH2   . ARG A 256 ? 0.5438 0.6871 0.6258 -0.0924 -0.1132 -0.0498 439  ARG A NH2   
4385 N N     . ASN A 257 ? 0.1636 0.4045 0.4012 0.0811  -0.0847 0.0362  440  ASN A N     
4386 C CA    . ASN A 257 ? 0.1891 0.3851 0.4261 0.0897  -0.0639 0.0256  440  ASN A CA    
4387 C C     . ASN A 257 ? 0.2000 0.3809 0.4705 0.0999  -0.0481 0.0472  440  ASN A C     
4388 O O     . ASN A 257 ? 0.1887 0.3816 0.4504 0.1125  -0.0381 0.0690  440  ASN A O     
4389 C CB    . ASN A 257 ? 0.2281 0.3778 0.3958 0.0765  -0.0877 0.0010  440  ASN A CB    
4390 C CG    . ASN A 257 ? 0.2343 0.3842 0.3506 0.0742  -0.0736 -0.0233 440  ASN A CG    
4391 O OD1   . ASN A 257 ? 0.1880 0.3898 0.3466 0.0745  -0.0759 -0.0137 440  ASN A OD1   
4392 N ND2   . ASN A 257 ? 0.3345 0.3902 0.3010 0.0747  -0.0331 -0.0562 440  ASN A ND2   
4399 N N     . THR A 258 ? 0.2141 0.3851 0.5193 0.0949  -0.0606 0.0366  441  THR A N     
4400 C CA    . THR A 258 ? 0.2347 0.4070 0.5476 0.0996  -0.0502 0.0249  441  THR A CA    
4401 C C     . THR A 258 ? 0.1982 0.4198 0.4861 0.1186  -0.0582 0.0301  441  THR A C     
4402 O O     . THR A 258 ? 0.2048 0.4423 0.4547 0.1248  -0.0682 0.0580  441  THR A O     
4403 C CB    . THR A 258 ? 0.2997 0.4264 0.6245 0.0900  -0.0502 0.0021  441  THR A CB    
4404 O OG1   . THR A 258 ? 0.3334 0.4406 0.6719 0.1023  -0.0406 -0.0193 441  THR A OG1   
4405 C CG2   . THR A 258 ? 0.3740 0.4349 0.6530 0.0548  -0.0496 -0.0124 441  THR A CG2   
4413 N N     . HIS A 259 ? 0.1640 0.4130 0.4548 0.0913  -0.0713 0.0036  442  HIS A N     
4414 C CA    . HIS A 259 ? 0.1661 0.4064 0.3992 0.0660  -0.0578 -0.0299 442  HIS A CA    
4415 C C     . HIS A 259 ? 0.2005 0.4239 0.3907 0.0685  -0.0621 -0.0693 442  HIS A C     
4416 O O     . HIS A 259 ? 0.2474 0.4151 0.4077 0.0714  -0.0715 -0.0916 442  HIS A O     
4417 C CB    . HIS A 259 ? 0.1756 0.3893 0.3829 0.0651  -0.0245 -0.0011 442  HIS A CB    
4418 C CG    . HIS A 259 ? 0.1684 0.3827 0.3776 0.0880  -0.0515 0.0298  442  HIS A CG    
4419 N ND1   . HIS A 259 ? 0.2098 0.3841 0.3738 0.0953  -0.0417 0.0454  442  HIS A ND1   
4420 C CD2   . HIS A 259 ? 0.1908 0.3822 0.3512 0.0803  -0.0557 0.0262  442  HIS A CD2   
4421 C CE1   . HIS A 259 ? 0.1885 0.3816 0.3407 0.0941  -0.0466 0.0486  442  HIS A CE1   
4422 N NE2   . HIS A 259 ? 0.1989 0.3795 0.3444 0.0858  -0.0550 0.0432  442  HIS A NE2   
4430 N N     . GLY A 260 ? 0.1794 0.4443 0.3794 0.0665  -0.0523 -0.0879 443  GLY A N     
4431 C CA    . GLY A 260 ? 0.2049 0.4627 0.3920 0.0438  -0.0437 -0.0880 443  GLY A CA    
4432 C C     . GLY A 260 ? 0.2016 0.4672 0.4370 0.0217  -0.0795 -0.0761 443  GLY A C     
4433 O O     . GLY A 260 ? 0.2116 0.4823 0.4672 -0.0195 -0.0892 -0.0767 443  GLY A O     
4437 N N     . LYS A 261 ? 0.1800 0.4494 0.4416 0.0220  -0.0685 -0.0714 444  LYS A N     
4438 C CA    . LYS A 261 ? 0.1967 0.4346 0.4392 0.0372  -0.0488 -0.0546 444  LYS A CA    
4439 C C     . LYS A 261 ? 0.1780 0.3884 0.3564 0.0264  -0.0618 -0.0481 444  LYS A C     
4440 O O     . LYS A 261 ? 0.1540 0.3658 0.3308 0.0387  -0.0222 -0.0174 444  LYS A O     
4441 C CB    . LYS A 261 ? 0.2867 0.4688 0.5313 0.0834  -0.0411 -0.0303 444  LYS A CB    
4442 C CG    . LYS A 261 ? 0.3826 0.5066 0.6074 0.1129  0.0096  -0.0319 444  LYS A CG    
4443 C CD    . LYS A 261 ? 0.5018 0.5466 0.6829 0.1050  0.0337  -0.0378 444  LYS A CD    
4444 C CE    . LYS A 261 ? 0.5659 0.5775 0.7353 0.0959  0.0531  -0.0449 444  LYS A CE    
4445 N NZ    . LYS A 261 ? 0.5966 0.5913 0.7530 0.0912  0.0564  -0.0497 444  LYS A NZ    
4459 N N     . GLU A 262 ? 0.1899 0.3744 0.3309 0.0144  -0.0710 -0.0578 445  GLU A N     
4460 C CA    . GLU A 262 ? 0.1712 0.3637 0.3515 0.0045  -0.0786 -0.0449 445  GLU A CA    
4461 C C     . GLU A 262 ? 0.1519 0.3383 0.2905 0.0087  -0.0395 -0.0204 445  GLU A C     
4462 O O     . GLU A 262 ? 0.1953 0.3368 0.3127 0.0147  -0.0397 0.0044  445  GLU A O     
4463 C CB    . GLU A 262 ? 0.1777 0.3804 0.4781 0.0071  -0.0632 -0.0370 445  GLU A CB    
4464 C CG    . GLU A 262 ? 0.2403 0.3960 0.5915 -0.0174 -0.0836 -0.0185 445  GLU A CG    
4465 C CD    . GLU A 262 ? 0.3147 0.4084 0.7160 -0.0459 -0.1030 0.0156  445  GLU A CD    
4466 O OE1   . GLU A 262 ? 0.2726 0.3936 0.7915 -0.0818 -0.0702 0.0312  445  GLU A OE1   
4467 O OE2   . GLU A 262 ? 0.3922 0.4262 0.7354 -0.0498 -0.1482 0.0277  445  GLU A OE2   
4474 N N     . VAL A 263 ? 0.1777 0.3217 0.2941 0.0100  -0.0251 -0.0009 446  VAL A N     
4475 C CA    . VAL A 263 ? 0.1378 0.3005 0.2990 0.0010  -0.0274 0.0074  446  VAL A CA    
4476 C C     . VAL A 263 ? 0.1096 0.2814 0.2625 0.0003  -0.0542 -0.0130 446  VAL A C     
4477 O O     . VAL A 263 ? 0.1420 0.3114 0.2602 0.0164  -0.0735 -0.0153 446  VAL A O     
4478 C CB    . VAL A 263 ? 0.1578 0.3054 0.3442 -0.0046 -0.0010 0.0260  446  VAL A CB    
4479 C CG1   . VAL A 263 ? 0.2049 0.3024 0.3795 0.0320  0.0587  0.0230  446  VAL A CG1   
4480 C CG2   . VAL A 263 ? 0.1724 0.3200 0.3493 -0.0220 -0.0325 0.0342  446  VAL A CG2   
4490 N N     . ARG A 264 ? 0.1408 0.2308 0.2496 -0.0315 -0.0712 -0.0349 447  ARG A N     
4491 C CA    . ARG A 264 ? 0.1535 0.1981 0.2801 -0.0457 -0.0594 -0.0427 447  ARG A CA    
4492 C C     . ARG A 264 ? 0.1138 0.1664 0.2470 -0.0435 -0.0581 -0.0236 447  ARG A C     
4493 O O     . ARG A 264 ? 0.1367 0.1863 0.2940 -0.0311 -0.0871 -0.0246 447  ARG A O     
4494 C CB    . ARG A 264 ? 0.2830 0.2190 0.3876 -0.0960 0.0276  -0.0910 447  ARG A CB    
4495 C CG    . ARG A 264 ? 0.4042 0.2718 0.4761 -0.1160 0.0434  -0.1057 447  ARG A CG    
4496 C CD    . ARG A 264 ? 0.4760 0.3227 0.5142 -0.1155 0.0154  -0.1172 447  ARG A CD    
4497 N NE    . ARG A 264 ? 0.5191 0.3474 0.5281 -0.1202 -0.0154 -0.1349 447  ARG A NE    
4498 C CZ    . ARG A 264 ? 0.5981 0.3798 0.5482 -0.0974 -0.0780 -0.1359 447  ARG A CZ    
4499 N NH1   . ARG A 264 ? 0.6404 0.3926 0.5401 -0.0860 -0.0941 -0.1122 447  ARG A NH1   
4500 N NH2   . ARG A 264 ? 0.6308 0.3900 0.5734 -0.0904 -0.1246 -0.1585 447  ARG A NH2   
4514 N N     . TYR A 265 ? 0.1093 0.1265 0.2184 -0.0255 -0.0716 -0.0048 448  TYR A N     
4515 C CA    . TYR A 265 ? 0.1205 0.1106 0.2049 -0.0208 -0.0821 0.0023  448  TYR A CA    
4516 C C     . TYR A 265 ? 0.1188 0.1118 0.1932 -0.0323 -0.0731 0.0037  448  TYR A C     
4517 O O     . TYR A 265 ? 0.1305 0.1485 0.1971 -0.0474 -0.0734 -0.0020 448  TYR A O     
4518 C CB    . TYR A 265 ? 0.1377 0.1078 0.2299 -0.0169 -0.0939 0.0004  448  TYR A CB    
4519 C CG    . TYR A 265 ? 0.1686 0.0958 0.2296 -0.0356 -0.0826 0.0085  448  TYR A CG    
4520 C CD1   . TYR A 265 ? 0.2218 0.0966 0.2045 -0.0545 -0.0686 0.0084  448  TYR A CD1   
4521 C CD2   . TYR A 265 ? 0.1619 0.0968 0.2641 -0.0331 -0.0798 0.0058  448  TYR A CD2   
4522 C CE1   . TYR A 265 ? 0.2206 0.1116 0.2389 -0.0536 -0.0938 0.0123  448  TYR A CE1   
4523 C CE2   . TYR A 265 ? 0.2024 0.1064 0.2674 -0.0473 -0.0785 0.0091  448  TYR A CE2   
4524 C CZ    . TYR A 265 ? 0.2086 0.1139 0.2365 -0.0559 -0.0682 0.0191  448  TYR A CZ    
4525 O OH    . TYR A 265 ? 0.2806 0.1259 0.2282 -0.0754 -0.0535 -0.0144 448  TYR A OH    
4535 N N     . ILE A 266 ? 0.1053 0.1002 0.1922 -0.0074 -0.0756 -0.0063 449  ILE A N     
4536 C CA    . ILE A 266 ? 0.1090 0.0856 0.2060 -0.0014 -0.0803 -0.0042 449  ILE A CA    
4537 C C     . ILE A 266 ? 0.1051 0.0830 0.2056 -0.0115 -0.0728 -0.0019 449  ILE A C     
4538 O O     . ILE A 266 ? 0.1017 0.0726 0.2118 -0.0066 -0.0741 0.0035  449  ILE A O     
4539 C CB    . ILE A 266 ? 0.1199 0.0902 0.1944 0.0099  -0.0859 -0.0117 449  ILE A CB    
4540 C CG1   . ILE A 266 ? 0.1152 0.0995 0.2067 0.0120  -0.0829 -0.0045 449  ILE A CG1   
4541 C CG2   . ILE A 266 ? 0.1224 0.0905 0.1866 0.0118  -0.0641 -0.0166 449  ILE A CG2   
4542 C CD1   . ILE A 266 ? 0.1373 0.0995 0.2461 0.0175  -0.0945 -0.0049 449  ILE A CD1   
4554 N N     . THR A 267 ? 0.1043 0.0782 0.2229 -0.0104 -0.0748 0.0078  450  THR A N     
4555 C CA    . THR A 267 ? 0.1112 0.0938 0.2471 0.0002  -0.0829 0.0018  450  THR A CA    
4556 C C     . THR A 267 ? 0.1169 0.1269 0.2638 0.0235  -0.0603 0.0286  450  THR A C     
4557 O O     . THR A 267 ? 0.2216 0.1516 0.3370 0.0542  0.0151  0.0607  450  THR A O     
4558 C CB    . THR A 267 ? 0.1076 0.1001 0.2277 -0.0063 -0.0751 -0.0166 450  THR A CB    
4559 O OG1   . THR A 267 ? 0.1081 0.0991 0.2555 -0.0021 -0.0800 0.0018  450  THR A OG1   
4560 C CG2   . THR A 267 ? 0.1074 0.1056 0.2402 -0.0138 -0.0683 -0.0187 450  THR A CG2   
4568 N N     . GLU A 268 ? 0.1235 0.1309 0.2273 -0.0175 -0.0738 0.0009  451  GLU A N     
4569 C CA    . GLU A 268 ? 0.1298 0.1433 0.2354 -0.0274 -0.0676 -0.0133 451  GLU A CA    
4570 C C     . GLU A 268 ? 0.1205 0.1456 0.2342 -0.0311 -0.0786 -0.0033 451  GLU A C     
4571 O O     . GLU A 268 ? 0.1414 0.1629 0.2562 -0.0340 -0.0953 0.0049  451  GLU A O     
4572 C CB    . GLU A 268 ? 0.1670 0.1691 0.2479 -0.0422 -0.0767 -0.0245 451  GLU A CB    
4573 C CG    . GLU A 268 ? 0.1549 0.1911 0.2589 -0.0365 -0.0523 -0.0494 451  GLU A CG    
4574 C CD    . GLU A 268 ? 0.1438 0.2067 0.3128 -0.0243 -0.0371 -0.0740 451  GLU A CD    
4575 O OE1   . GLU A 268 ? 0.1531 0.2518 0.3563 -0.0257 -0.0158 -0.1169 451  GLU A OE1   
4576 O OE2   . GLU A 268 ? 0.1418 0.1696 0.3046 -0.0272 -0.0648 -0.0485 451  GLU A OE2   
4583 N N     . LEU A 269 ? 0.1344 0.1521 0.2491 -0.0349 -0.0737 0.0144  452  LEU A N     
4584 C CA    . LEU A 269 ? 0.1530 0.1402 0.2609 -0.0469 -0.0717 -0.0008 452  LEU A CA    
4585 C C     . LEU A 269 ? 0.1823 0.1421 0.2981 -0.0526 -0.0748 -0.0201 452  LEU A C     
4586 O O     . LEU A 269 ? 0.1814 0.1708 0.3087 -0.0391 -0.0697 -0.0299 452  LEU A O     
4587 C CB    . LEU A 269 ? 0.1629 0.1361 0.2843 -0.0409 -0.0602 -0.0018 452  LEU A CB    
4588 C CG    . LEU A 269 ? 0.1611 0.1284 0.2916 -0.0243 -0.0207 0.0044  452  LEU A CG    
4589 C CD1   . LEU A 269 ? 0.3160 0.1216 0.3327 -0.0103 0.0221  0.0214  452  LEU A CD1   
4590 C CD2   . LEU A 269 ? 0.1279 0.1464 0.2746 -0.0021 -0.0406 -0.0136 452  LEU A CD2   
4602 N N     . SER A 270 ? 0.1574 0.1157 0.3081 -0.0268 -0.0861 -0.0134 453  SER A N     
4603 C CA    . SER A 270 ? 0.1859 0.1143 0.3411 -0.0128 -0.0473 -0.0202 453  SER A CA    
4604 C C     . SER A 270 ? 0.1568 0.1179 0.3180 -0.0230 -0.0224 -0.0528 453  SER A C     
4605 O O     . SER A 270 ? 0.1391 0.1016 0.2775 -0.0078 -0.0322 -0.0516 453  SER A O     
4606 C CB    . SER A 270 ? 0.1724 0.1045 0.3754 -0.0018 -0.0471 -0.0039 453  SER A CB    
4607 O OG    . SER A 270 ? 0.1508 0.1032 0.3567 0.0080  -0.0595 -0.0093 453  SER A OG    
4613 N N     . ASP A 271 ? 0.1912 0.1340 0.3463 0.0055  -0.0207 -0.0549 454  ASP A N     
4614 C CA    . ASP A 271 ? 0.2320 0.1543 0.3414 0.0011  -0.0030 -0.0650 454  ASP A CA    
4615 C C     . ASP A 271 ? 0.1653 0.1364 0.3189 0.0100  -0.0040 -0.0475 454  ASP A C     
4616 O O     . ASP A 271 ? 0.1743 0.1221 0.3175 -0.0003 -0.0038 -0.0438 454  ASP A O     
4617 C CB    . ASP A 271 ? 0.2681 0.2032 0.3525 -0.0075 -0.0002 -0.0845 454  ASP A CB    
4618 C CG    . ASP A 271 ? 0.3303 0.2638 0.3741 -0.0042 0.0104  -0.1098 454  ASP A CG    
4619 O OD1   . ASP A 271 ? 0.3351 0.2956 0.3600 -0.0219 0.0019  -0.1080 454  ASP A OD1   
4620 O OD2   . ASP A 271 ? 0.3887 0.2886 0.3955 -0.0054 -0.0040 -0.1243 454  ASP A OD2   
4625 N N     . GLU A 272 ? 0.1416 0.1342 0.3296 0.0295  -0.0249 -0.0435 455  GLU A N     
4626 C CA    A GLU A 272 ? 0.1149 0.1395 0.3271 0.0400  -0.0216 -0.0240 455  GLU A CA    
4627 C CA    B GLU A 272 ? 0.1201 0.1624 0.3326 0.0408  -0.0531 -0.0248 455  GLU A CA    
4628 C C     . GLU A 272 ? 0.0909 0.1321 0.2959 0.0247  -0.0352 -0.0154 455  GLU A C     
4629 O O     . GLU A 272 ? 0.1100 0.1265 0.2923 0.0012  -0.0555 -0.0147 455  GLU A O     
4630 C CB    A GLU A 272 ? 0.1287 0.1534 0.3322 0.0549  0.0031  -0.0194 455  GLU A CB    
4631 C CB    B GLU A 272 ? 0.1528 0.2242 0.3643 0.0510  -0.0925 -0.0184 455  GLU A CB    
4632 C CG    A GLU A 272 ? 0.1855 0.1633 0.3689 0.0716  0.0081  -0.0237 455  GLU A CG    
4633 C CG    B GLU A 272 ? 0.2485 0.2847 0.4304 0.0514  -0.1160 -0.0115 455  GLU A CG    
4634 C CD    A GLU A 272 ? 0.2771 0.1831 0.4268 0.0935  0.0500  -0.0266 455  GLU A CD    
4635 C CD    B GLU A 272 ? 0.3464 0.3368 0.4992 0.0485  -0.1142 -0.0094 455  GLU A CD    
4636 O OE1   A GLU A 272 ? 0.2381 0.1612 0.3918 0.0900  0.0203  -0.0205 455  GLU A OE1   
4637 O OE1   B GLU A 272 ? 0.3749 0.3559 0.5259 0.0637  -0.0993 -0.0047 455  GLU A OE1   
4638 O OE2   A GLU A 272 ? 0.3161 0.2220 0.4934 0.0973  0.1106  -0.0348 455  GLU A OE2   
4639 O OE2   B GLU A 272 ? 0.3758 0.3575 0.5278 0.0388  -0.1316 -0.0131 455  GLU A OE2   
4652 N N     . GLU A 273 ? 0.0866 0.1122 0.2660 0.0093  -0.0300 -0.0150 456  GLU A N     
4653 C CA    . GLU A 273 ? 0.0867 0.1077 0.2465 0.0087  -0.0460 -0.0140 456  GLU A CA    
4654 C C     . GLU A 273 ? 0.0854 0.0954 0.2464 0.0067  -0.0453 -0.0220 456  GLU A C     
4655 O O     . GLU A 273 ? 0.0972 0.0838 0.2475 -0.0019 -0.0603 -0.0248 456  GLU A O     
4656 C CB    . GLU A 273 ? 0.1094 0.1235 0.2611 0.0100  -0.0692 0.0006  456  GLU A CB    
4657 C CG    . GLU A 273 ? 0.1070 0.1334 0.2881 -0.0120 -0.0689 0.0117  456  GLU A CG    
4658 C CD    . GLU A 273 ? 0.1254 0.1523 0.3267 -0.0055 -0.0751 0.0329  456  GLU A CD    
4659 O OE1   . GLU A 273 ? 0.1476 0.1363 0.3167 -0.0082 -0.0708 0.0179  456  GLU A OE1   
4660 O OE2   . GLU A 273 ? 0.1690 0.1939 0.3360 -0.0382 -0.0849 0.0711  456  GLU A OE2   
4667 N N     . LYS A 274 ? 0.1240 0.0937 0.2312 0.0062  -0.0637 -0.0284 457  LYS A N     
4668 C CA    . LYS A 274 ? 0.1354 0.1045 0.2341 -0.0068 -0.0655 -0.0227 457  LYS A CA    
4669 C C     . LYS A 274 ? 0.1253 0.0995 0.2391 0.0121  -0.0528 -0.0246 457  LYS A C     
4670 O O     . LYS A 274 ? 0.1385 0.0956 0.2429 0.0104  -0.0571 -0.0218 457  LYS A O     
4671 C CB    . LYS A 274 ? 0.1523 0.1349 0.2399 -0.0131 -0.0700 -0.0178 457  LYS A CB    
4672 C CG    . LYS A 274 ? 0.1561 0.1659 0.2545 -0.0456 -0.0789 -0.0273 457  LYS A CG    
4673 C CD    . LYS A 274 ? 0.2417 0.2193 0.2862 -0.0790 -0.0780 -0.0508 457  LYS A CD    
4674 C CE    . LYS A 274 ? 0.3091 0.2764 0.3249 -0.0908 -0.0800 -0.0666 457  LYS A CE    
4675 N NZ    . LYS A 274 ? 0.3576 0.3168 0.3669 -0.0826 -0.0845 -0.0723 457  LYS A NZ    
4689 N N     . THR A 275 ? 0.1299 0.1147 0.2422 0.0105  -0.0485 -0.0218 458  THR A N     
4690 C CA    . THR A 275 ? 0.1164 0.1279 0.2617 0.0094  -0.0211 -0.0259 458  THR A CA    
4691 C C     . THR A 275 ? 0.1100 0.1080 0.2419 0.0135  -0.0439 -0.0262 458  THR A C     
4692 O O     . THR A 275 ? 0.1127 0.1006 0.2526 -0.0007 -0.0326 -0.0140 458  THR A O     
4693 C CB    . THR A 275 ? 0.1355 0.1684 0.2721 -0.0056 0.0370  -0.0342 458  THR A CB    
4694 O OG1   . THR A 275 ? 0.2051 0.1867 0.2836 -0.0201 0.0395  -0.0382 458  THR A OG1   
4695 C CG2   . THR A 275 ? 0.1387 0.1745 0.3233 0.0258  0.0646  -0.0170 458  THR A CG2   
4703 N N     . ILE A 276 ? 0.0971 0.1099 0.2463 0.0068  -0.0679 -0.0213 459  ILE A N     
4704 C CA    . ILE A 276 ? 0.0943 0.1108 0.2307 0.0016  -0.0686 -0.0141 459  ILE A CA    
4705 C C     . ILE A 276 ? 0.0801 0.1016 0.2197 0.0028  -0.0562 -0.0083 459  ILE A C     
4706 O O     . ILE A 276 ? 0.0924 0.0911 0.2386 -0.0089 -0.0552 -0.0203 459  ILE A O     
4707 C CB    . ILE A 276 ? 0.1118 0.1143 0.2423 0.0129  -0.0815 -0.0074 459  ILE A CB    
4708 C CG1   . ILE A 276 ? 0.1231 0.1170 0.2550 0.0296  -0.0796 -0.0126 459  ILE A CG1   
4709 C CG2   . ILE A 276 ? 0.1451 0.1199 0.2558 -0.0108 -0.0885 -0.0122 459  ILE A CG2   
4710 C CD1   . ILE A 276 ? 0.1609 0.1198 0.2914 0.0314  -0.1000 -0.0060 459  ILE A CD1   
4722 N N     . ALA A 277 ? 0.0796 0.1051 0.2090 0.0107  -0.0550 -0.0282 460  ALA A N     
4723 C CA    . ALA A 277 ? 0.0849 0.1025 0.2167 -0.0100 -0.0545 -0.0174 460  ALA A CA    
4724 C C     . ALA A 277 ? 0.0999 0.0972 0.2361 0.0024  -0.0735 -0.0119 460  ALA A C     
4725 O O     . ALA A 277 ? 0.0951 0.0885 0.2478 0.0038  -0.0615 -0.0339 460  ALA A O     
4726 C CB    . ALA A 277 ? 0.0969 0.1025 0.2444 -0.0102 -0.0643 -0.0114 460  ALA A CB    
4732 N N     . GLY A 278 ? 0.1197 0.0981 0.2555 0.0084  -0.0693 -0.0192 461  GLY A N     
4733 C CA    . GLY A 278 ? 0.1039 0.1094 0.2666 0.0119  -0.0729 -0.0096 461  GLY A CA    
4734 C C     . GLY A 278 ? 0.0977 0.0974 0.2625 0.0104  -0.0664 -0.0106 461  GLY A C     
4735 O O     . GLY A 278 ? 0.1222 0.0866 0.2754 0.0141  -0.0561 -0.0043 461  GLY A O     
4739 N N     . LYS A 279 ? 0.0969 0.0941 0.2626 0.0010  -0.0616 -0.0044 462  LYS A N     
4740 C CA    . LYS A 279 ? 0.0923 0.0997 0.2609 -0.0059 -0.0612 -0.0059 462  LYS A CA    
4741 C C     . LYS A 279 ? 0.0980 0.0929 0.2713 -0.0038 -0.0674 0.0076  462  LYS A C     
4742 O O     . LYS A 279 ? 0.1027 0.0915 0.2663 -0.0119 -0.0637 -0.0043 462  LYS A O     
4743 C CB    . LYS A 279 ? 0.0928 0.1097 0.2769 0.0018  -0.0546 -0.0258 462  LYS A CB    
4744 C CG    . LYS A 279 ? 0.1209 0.1430 0.3321 0.0094  -0.0166 -0.0327 462  LYS A CG    
4745 C CD    . LYS A 279 ? 0.1283 0.1825 0.3799 0.0063  -0.0077 -0.0300 462  LYS A CD    
4746 C CE    . LYS A 279 ? 0.1982 0.2343 0.4303 0.0047  -0.0228 -0.0080 462  LYS A CE    
4747 N NZ    . LYS A 279 ? 0.2514 0.2736 0.4486 0.0006  -0.0402 -0.0040 462  LYS A NZ    
4761 N N     . VAL A 280 ? 0.0952 0.0817 0.2437 -0.0019 -0.0683 -0.0035 463  VAL A N     
4762 C CA    . VAL A 280 ? 0.0881 0.0901 0.2283 0.0065  -0.0630 -0.0081 463  VAL A CA    
4763 C C     . VAL A 280 ? 0.0917 0.0848 0.2234 -0.0029 -0.0655 -0.0088 463  VAL A C     
4764 O O     . VAL A 280 ? 0.0920 0.0784 0.2292 -0.0009 -0.0610 -0.0198 463  VAL A O     
4765 C CB    . VAL A 280 ? 0.0856 0.0886 0.2545 0.0014  -0.0546 -0.0079 463  VAL A CB    
4766 C CG1   . VAL A 280 ? 0.0874 0.1026 0.2294 -0.0159 -0.0408 0.0089  463  VAL A CG1   
4767 C CG2   . VAL A 280 ? 0.1026 0.0798 0.2613 0.0024  -0.0679 -0.0077 463  VAL A CG2   
4777 N N     . SER A 281 ? 0.0964 0.0795 0.2076 0.0028  -0.0720 -0.0053 464  SER A N     
4778 C CA    . SER A 281 ? 0.0910 0.0909 0.2125 0.0053  -0.0664 0.0013  464  SER A CA    
4779 C C     . SER A 281 ? 0.1056 0.0967 0.2236 -0.0065 -0.0761 -0.0077 464  SER A C     
4780 O O     . SER A 281 ? 0.1085 0.0841 0.2521 -0.0029 -0.0710 -0.0104 464  SER A O     
4781 C CB    . SER A 281 ? 0.1120 0.1044 0.2136 0.0164  -0.0765 0.0048  464  SER A CB    
4782 O OG    . SER A 281 ? 0.1242 0.1057 0.2276 0.0055  -0.0751 -0.0110 464  SER A OG    
4788 N N     . LYS A 282 ? 0.1025 0.1066 0.2249 -0.0073 -0.0640 -0.0104 465  LYS A N     
4789 C CA    . LYS A 282 ? 0.1007 0.1228 0.2196 -0.0011 -0.0506 0.0016  465  LYS A CA    
4790 C C     . LYS A 282 ? 0.0851 0.1034 0.2114 -0.0011 -0.0457 -0.0025 465  LYS A C     
4791 O O     . LYS A 282 ? 0.1335 0.0970 0.2446 -0.0117 -0.0540 -0.0005 465  LYS A O     
4792 C CB    . LYS A 282 ? 0.1093 0.1611 0.2467 -0.0224 -0.0576 -0.0153 465  LYS A CB    
4793 C CG    . LYS A 282 ? 0.1531 0.2185 0.2993 -0.0500 -0.0216 -0.0284 465  LYS A CG    
4794 C CD    . LYS A 282 ? 0.2360 0.2794 0.3924 -0.0692 0.0221  -0.0379 465  LYS A CD    
4795 C CE    . LYS A 282 ? 0.3667 0.3343 0.5038 -0.0604 0.0393  -0.0634 465  LYS A CE    
4796 N NZ    . LYS A 282 ? 0.4711 0.3689 0.5732 -0.0491 0.0576  -0.0731 465  LYS A NZ    
4810 N N     . ALA A 283 ? 0.0749 0.0941 0.2249 -0.0048 -0.0456 -0.0137 466  ALA A N     
4811 C CA    . ALA A 283 ? 0.0892 0.0908 0.2410 -0.0063 -0.0560 -0.0172 466  ALA A CA    
4812 C C     . ALA A 283 ? 0.0767 0.0849 0.2237 -0.0070 -0.0397 -0.0072 466  ALA A C     
4813 O O     . ALA A 283 ? 0.0901 0.0832 0.2345 -0.0114 -0.0572 -0.0005 466  ALA A O     
4814 C CB    . ALA A 283 ? 0.0891 0.0991 0.2275 0.0002  -0.0622 -0.0205 466  ALA A CB    
4820 N N     . PHE A 284 ? 0.0580 0.1016 0.1999 -0.0022 -0.0219 -0.0116 467  PHE A N     
4821 C CA    . PHE A 284 ? 0.0610 0.1079 0.2014 0.0086  -0.0331 -0.0123 467  PHE A CA    
4822 C C     . PHE A 284 ? 0.0639 0.0957 0.2138 0.0027  -0.0352 -0.0130 467  PHE A C     
4823 O O     . PHE A 284 ? 0.0890 0.0955 0.2245 0.0044  -0.0638 -0.0198 467  PHE A O     
4824 C CB    . PHE A 284 ? 0.0718 0.1124 0.2052 0.0123  -0.0467 -0.0104 467  PHE A CB    
4825 C CG    . PHE A 284 ? 0.0817 0.1094 0.1992 0.0066  -0.0586 0.0057  467  PHE A CG    
4826 C CD1   . PHE A 284 ? 0.0856 0.0958 0.1974 -0.0091 -0.0620 0.0021  467  PHE A CD1   
4827 C CD2   . PHE A 284 ? 0.1318 0.1233 0.2319 0.0328  -0.0845 -0.0071 467  PHE A CD2   
4828 C CE1   . PHE A 284 ? 0.0942 0.1093 0.2166 -0.0069 -0.0696 0.0080  467  PHE A CE1   
4829 C CE2   . PHE A 284 ? 0.1207 0.1333 0.2408 0.0101  -0.0887 0.0006  467  PHE A CE2   
4830 C CZ    . PHE A 284 ? 0.1107 0.1243 0.2222 0.0117  -0.0772 0.0159  467  PHE A CZ    
4840 N N     . SER A 285 ? 0.0841 0.0827 0.2104 0.0041  -0.0381 -0.0050 468  SER A N     
4841 C CA    . SER A 285 ? 0.1049 0.0891 0.2330 -0.0066 -0.0676 -0.0004 468  SER A CA    
4842 C C     . SER A 285 ? 0.1014 0.0762 0.2147 -0.0021 -0.0700 -0.0102 468  SER A C     
4843 O O     . SER A 285 ? 0.1161 0.0798 0.2543 0.0082  -0.0759 0.0032  468  SER A O     
4844 C CB    . SER A 285 ? 0.1000 0.1056 0.2702 -0.0221 -0.0570 0.0122  468  SER A CB    
4845 O OG    . SER A 285 ? 0.1256 0.1123 0.3036 -0.0208 -0.0648 0.0211  468  SER A OG    
4851 N N     . GLN A 286 ? 0.0809 0.0614 0.2131 0.0002  -0.0580 0.0002  469  GLN A N     
4852 C CA    . GLN A 286 ? 0.0984 0.0780 0.2174 0.0063  -0.0723 -0.0042 469  GLN A CA    
4853 C C     . GLN A 286 ? 0.1085 0.0767 0.2073 -0.0060 -0.0778 -0.0023 469  GLN A C     
4854 O O     . GLN A 286 ? 0.1115 0.0707 0.2404 0.0015  -0.0833 -0.0032 469  GLN A O     
4855 C CB    . GLN A 286 ? 0.0841 0.0844 0.2244 -0.0027 -0.0593 -0.0027 469  GLN A CB    
4856 C CG    . GLN A 286 ? 0.0913 0.0841 0.2065 0.0007  -0.0665 0.0113  469  GLN A CG    
4857 C CD    . GLN A 286 ? 0.0932 0.0974 0.2042 0.0057  -0.0687 0.0009  469  GLN A CD    
4858 O OE1   . GLN A 286 ? 0.0906 0.1217 0.2325 0.0072  -0.0652 -0.0100 469  GLN A OE1   
4859 N NE2   . GLN A 286 ? 0.1051 0.0881 0.2298 0.0029  -0.0773 -0.0038 469  GLN A NE2   
4868 N N     . MET A 287 ? 0.0981 0.0780 0.2010 0.0028  -0.0699 -0.0045 470  MET A N     
4869 C CA    . MET A 287 ? 0.1135 0.0817 0.2262 0.0020  -0.0828 0.0069  470  MET A CA    
4870 C C     . MET A 287 ? 0.1154 0.0741 0.2181 0.0070  -0.0850 -0.0088 470  MET A C     
4871 O O     . MET A 287 ? 0.1216 0.0720 0.2280 0.0062  -0.0886 -0.0078 470  MET A O     
4872 C CB    . MET A 287 ? 0.1396 0.0943 0.2611 -0.0028 -0.1001 -0.0042 470  MET A CB    
4873 C CG    . MET A 287 ? 0.2113 0.1028 0.2663 0.0116  -0.1249 0.0081  470  MET A CG    
4874 S SD    . MET A 287 ? 0.2963 0.1175 0.2730 -0.0052 -0.1539 0.0066  470  MET A SD    
4875 C CE    . MET A 287 ? 0.4415 0.1385 0.2810 -0.0550 -0.0969 0.0025  470  MET A CE    
4885 N N     . ILE A 288 ? 0.1141 0.0664 0.2232 0.0014  -0.0730 -0.0092 471  ILE A N     
4886 C CA    . ILE A 288 ? 0.1062 0.0726 0.2200 0.0059  -0.0683 -0.0041 471  ILE A CA    
4887 C C     . ILE A 288 ? 0.1135 0.0745 0.2188 0.0120  -0.0751 -0.0066 471  ILE A C     
4888 O O     . ILE A 288 ? 0.1386 0.0880 0.2323 0.0153  -0.0888 -0.0174 471  ILE A O     
4889 C CB    . ILE A 288 ? 0.1156 0.0930 0.2490 0.0082  -0.0781 0.0131  471  ILE A CB    
4890 C CG1   . ILE A 288 ? 0.1200 0.1287 0.2986 0.0004  -0.0661 0.0625  471  ILE A CG1   
4891 C CG2   . ILE A 288 ? 0.1266 0.0908 0.2766 0.0041  -0.0863 0.0132  471  ILE A CG2   
4892 C CD1   . ILE A 288 ? 0.1415 0.1452 0.3610 -0.0018 -0.0930 0.0488  471  ILE A CD1   
4904 N N     . CYS A 289 ? 0.0997 0.0701 0.2334 -0.0066 -0.0734 0.0132  472  CYS A N     
4905 C CA    . CYS A 289 ? 0.1215 0.0791 0.2370 -0.0129 -0.0814 0.0061  472  CYS A CA    
4906 C C     . CYS A 289 ? 0.1348 0.0778 0.2239 -0.0092 -0.0897 -0.0008 472  CYS A C     
4907 O O     . CYS A 289 ? 0.2148 0.0879 0.2368 -0.0271 -0.0626 -0.0179 472  CYS A O     
4908 C CB    . CYS A 289 ? 0.1177 0.1078 0.2477 -0.0164 -0.0849 0.0124  472  CYS A CB    
4909 S SG    . CYS A 289 ? 0.1264 0.1076 0.2528 -0.0198 -0.0878 0.0078  472  CYS A SG    
4915 N N     . GLY A 290 ? 0.0973 0.0665 0.2338 -0.0011 -0.0719 0.0026  473  GLY A N     
4916 C CA    . GLY A 290 ? 0.1042 0.0666 0.2269 -0.0018 -0.0777 0.0036  473  GLY A CA    
4917 C C     . GLY A 290 ? 0.1000 0.0645 0.2118 0.0035  -0.0731 -0.0103 473  GLY A C     
4918 O O     . GLY A 290 ? 0.1236 0.0723 0.2242 -0.0017 -0.0897 -0.0013 473  GLY A O     
4922 N N     . PHE A 291 ? 0.0970 0.0637 0.2022 0.0021  -0.0719 -0.0069 474  PHE A N     
4923 C CA    . PHE A 291 ? 0.0813 0.0724 0.2093 0.0019  -0.0586 -0.0074 474  PHE A CA    
4924 C C     . PHE A 291 ? 0.0909 0.0701 0.2003 -0.0066 -0.0639 -0.0019 474  PHE A C     
4925 O O     . PHE A 291 ? 0.1087 0.0779 0.2061 -0.0064 -0.0770 -0.0045 474  PHE A O     
4926 C CB    . PHE A 291 ? 0.1103 0.0898 0.2381 -0.0143 -0.0781 0.0099  474  PHE A CB    
4927 C CG    . PHE A 291 ? 0.0997 0.0858 0.2171 -0.0173 -0.0690 0.0144  474  PHE A CG    
4928 C CD1   . PHE A 291 ? 0.1015 0.0785 0.2198 -0.0154 -0.0615 -0.0022 474  PHE A CD1   
4929 C CD2   . PHE A 291 ? 0.1009 0.1048 0.2246 -0.0185 -0.0696 0.0067  474  PHE A CD2   
4930 C CE1   . PHE A 291 ? 0.1095 0.0794 0.2511 0.0096  -0.0691 0.0005  474  PHE A CE1   
4931 C CE2   . PHE A 291 ? 0.0980 0.0981 0.2489 0.0033  -0.0703 0.0052  474  PHE A CE2   
4932 C CZ    . PHE A 291 ? 0.1033 0.0880 0.2526 0.0062  -0.0745 -0.0040 474  PHE A CZ    
4942 N N     . ASP A 292 ? 0.1152 0.0714 0.2180 -0.0063 -0.0853 0.0111  475  ASP A N     
4943 C CA    . ASP A 292 ? 0.1012 0.1001 0.2470 -0.0022 -0.0707 0.0158  475  ASP A CA    
4944 C C     . ASP A 292 ? 0.0994 0.0905 0.1942 -0.0029 -0.0730 0.0146  475  ASP A C     
4945 O O     . ASP A 292 ? 0.1060 0.0858 0.2122 -0.0147 -0.0743 0.0066  475  ASP A O     
4946 C CB    . ASP A 292 ? 0.1557 0.1645 0.3023 0.0049  -0.0495 0.0519  475  ASP A CB    
4947 C CG    . ASP A 292 ? 0.2441 0.2828 0.4236 0.0039  0.0105  0.0538  475  ASP A CG    
4948 O OD1   . ASP A 292 ? 0.2778 0.3583 0.4907 -0.0007 -0.0255 0.0153  475  ASP A OD1   
4949 O OD2   . ASP A 292 ? 0.2597 0.3117 0.4578 0.0538  0.0380  0.1279  475  ASP A OD2   
4954 N N     . LEU A 293 ? 0.1058 0.0835 0.2314 -0.0042 -0.0787 0.0043  476  LEU A N     
4955 C CA    . LEU A 293 ? 0.1344 0.0868 0.2751 0.0021  -0.0773 0.0173  476  LEU A CA    
4956 C C     . LEU A 293 ? 0.1126 0.0809 0.2631 -0.0084 -0.0830 0.0176  476  LEU A C     
4957 O O     . LEU A 293 ? 0.1264 0.0905 0.3071 -0.0094 -0.0923 0.0208  476  LEU A O     
4958 C CB    . LEU A 293 ? 0.2838 0.1213 0.3178 0.0318  -0.0027 0.0432  476  LEU A CB    
4959 C CG    . LEU A 293 ? 0.3869 0.1378 0.3559 0.0300  -0.0421 0.0212  476  LEU A CG    
4960 C CD1   . LEU A 293 ? 0.4144 0.1682 0.4374 0.0532  -0.0309 0.0217  476  LEU A CD1   
4961 C CD2   . LEU A 293 ? 0.3575 0.1246 0.3366 -0.0120 -0.1409 -0.0005 476  LEU A CD2   
4973 N N     . LEU A 294 ? 0.1088 0.0780 0.2656 -0.0036 -0.0800 0.0085  477  LEU A N     
4974 C CA    . LEU A 294 ? 0.1223 0.0897 0.2636 -0.0032 -0.0914 0.0052  477  LEU A CA    
4975 C C     . LEU A 294 ? 0.1319 0.0944 0.2885 -0.0035 -0.0969 -0.0022 477  LEU A C     
4976 O O     . LEU A 294 ? 0.1406 0.1061 0.3403 0.0010  -0.0740 -0.0100 477  LEU A O     
4977 C CB    . LEU A 294 ? 0.1576 0.1239 0.2765 -0.0137 -0.1128 0.0025  477  LEU A CB    
4978 C CG    . LEU A 294 ? 0.1965 0.1503 0.2993 0.0098  -0.1345 0.0129  477  LEU A CG    
4979 C CD1   . LEU A 294 ? 0.2156 0.1690 0.2939 0.0076  -0.1202 0.0176  477  LEU A CD1   
4980 C CD2   . LEU A 294 ? 0.2087 0.1579 0.3131 0.0146  -0.1251 0.0035  477  LEU A CD2   
4992 N N     . ARG A 295 ? 0.1316 0.0924 0.2746 0.0043  -0.0983 -0.0084 478  ARG A N     
4993 C CA    . ARG A 295 ? 0.1435 0.1003 0.2601 0.0114  -0.1004 0.0023  478  ARG A CA    
4994 C C     . ARG A 295 ? 0.1351 0.1077 0.2694 -0.0060 -0.1005 0.0075  478  ARG A C     
4995 O O     . ARG A 295 ? 0.1797 0.1285 0.2813 -0.0161 -0.1207 0.0199  478  ARG A O     
4996 C CB    . ARG A 295 ? 0.1588 0.1035 0.2725 0.0073  -0.1155 -0.0153 478  ARG A CB    
4997 C CG    . ARG A 295 ? 0.1525 0.0987 0.2597 0.0092  -0.1059 0.0044  478  ARG A CG    
4998 C CD    . ARG A 295 ? 0.1365 0.1039 0.2633 0.0054  -0.1011 -0.0033 478  ARG A CD    
4999 N NE    . ARG A 295 ? 0.1231 0.1080 0.2513 -0.0021 -0.0919 0.0044  478  ARG A NE    
5000 C CZ    . ARG A 295 ? 0.1291 0.1103 0.2671 -0.0094 -0.0917 0.0109  478  ARG A CZ    
5001 N NH1   . ARG A 295 ? 0.1446 0.1127 0.2715 -0.0124 -0.1049 0.0052  478  ARG A NH1   
5002 N NH2   . ARG A 295 ? 0.1521 0.1095 0.2671 -0.0049 -0.0900 0.0155  478  ARG A NH2   
5016 N N     . VAL A 296 ? 0.1525 0.1345 0.3154 0.0052  -0.1107 0.0153  479  VAL A N     
5017 C CA    . VAL A 296 ? 0.2148 0.1940 0.3904 0.0158  -0.1444 0.0229  479  VAL A CA    
5018 C C     . VAL A 296 ? 0.2671 0.1948 0.4600 0.0481  -0.0664 0.0272  479  VAL A C     
5019 O O     . VAL A 296 ? 0.2406 0.2013 0.4786 0.0583  -0.0758 0.0233  479  VAL A O     
5020 C CB    . VAL A 296 ? 0.2458 0.2868 0.3852 0.0026  -0.1753 0.0112  479  VAL A CB    
5021 C CG1   . VAL A 296 ? 0.2773 0.3346 0.3932 0.0165  -0.1866 0.0377  479  VAL A CG1   
5022 C CG2   . VAL A 296 ? 0.2555 0.3096 0.3736 -0.0163 -0.1457 -0.0514 479  VAL A CG2   
5032 N N     . SER A 297 ? 0.3295 0.2017 0.5212 0.1052  -0.0164 0.0407  480  SER A N     
5033 C CA    . SER A 297 ? 0.3999 0.2363 0.5777 0.1360  0.0215  0.0468  480  SER A CA    
5034 C C     . SER A 297 ? 0.3933 0.2348 0.6066 0.1020  0.0400  -0.0133 480  SER A C     
5035 O O     . SER A 297 ? 0.4102 0.2661 0.6615 0.1099  0.0584  -0.0003 480  SER A O     
5036 C CB    . SER A 297 ? 0.5123 0.2839 0.6388 0.1383  0.0206  0.0911  480  SER A CB    
5037 O OG    . SER A 297 ? 0.5594 0.3132 0.6838 0.1338  0.0120  0.1032  480  SER A OG    
5043 N N     . GLY A 298 ? 0.3719 0.2009 0.5605 0.0513  0.0371  -0.0753 481  GLY A N     
5044 C CA    . GLY A 298 ? 0.3425 0.1946 0.5317 0.0373  0.0454  -0.0986 481  GLY A CA    
5045 C C     . GLY A 298 ? 0.3320 0.1892 0.5175 0.0457  0.0311  -0.0690 481  GLY A C     
5046 O O     . GLY A 298 ? 0.4372 0.2148 0.5465 0.0654  0.0238  -0.0821 481  GLY A O     
5050 N N     . LYS A 299 ? 0.2414 0.1600 0.4883 0.0304  -0.0229 -0.0389 482  LYS A N     
5051 C CA    . LYS A 299 ? 0.2466 0.1559 0.4719 0.0472  -0.0288 -0.0308 482  LYS A CA    
5052 C C     . LYS A 299 ? 0.2325 0.1310 0.3810 0.0438  -0.0712 -0.0191 482  LYS A C     
5053 O O     . LYS A 299 ? 0.2117 0.1241 0.4169 0.0276  -0.0738 0.0050  482  LYS A O     
5054 C CB    . LYS A 299 ? 0.2721 0.2005 0.5600 0.0769  -0.0382 -0.0501 482  LYS A CB    
5055 C CG    . LYS A 299 ? 0.3618 0.2640 0.6238 0.0907  -0.0385 -0.0575 482  LYS A CG    
5056 C CD    . LYS A 299 ? 0.3960 0.3180 0.6762 0.1124  -0.0275 -0.0584 482  LYS A CD    
5057 C CE    . LYS A 299 ? 0.4892 0.3608 0.7167 0.1048  0.0094  -0.0660 482  LYS A CE    
5058 N NZ    . LYS A 299 ? 0.5662 0.3917 0.7475 0.0851  0.0189  -0.0646 482  LYS A NZ    
5072 N N     . SER A 300 ? 0.3007 0.1259 0.3310 0.0395  -0.0285 -0.0270 483  SER A N     
5073 C CA    A SER A 300 ? 0.2594 0.1196 0.3162 0.0256  -0.0759 -0.0222 483  SER A CA    
5074 C CA    B SER A 300 ? 0.2863 0.1237 0.3135 0.0480  -0.0348 -0.0280 483  SER A CA    
5075 C C     . SER A 300 ? 0.2455 0.1156 0.3490 0.0078  -0.0128 -0.0176 483  SER A C     
5076 O O     . SER A 300 ? 0.3381 0.1316 0.4492 -0.0188 0.1010  -0.0295 483  SER A O     
5077 C CB    A SER A 300 ? 0.2409 0.1334 0.3521 -0.0053 -0.1135 -0.0168 483  SER A CB    
5078 C CB    B SER A 300 ? 0.3019 0.1379 0.3028 0.0665  -0.0393 -0.0380 483  SER A CB    
5079 O OG    A SER A 300 ? 0.2128 0.1494 0.3286 -0.0155 -0.1423 0.0000  483  SER A OG    
5080 O OG    B SER A 300 ? 0.2262 0.1452 0.2531 0.0235  -0.0815 -0.0672 483  SER A OG    
5091 N N     . TYR A 301 ? 0.1379 0.0898 0.3048 0.0094  -0.0583 -0.0033 484  TYR A N     
5092 C CA    . TYR A 301 ? 0.1064 0.0974 0.2950 -0.0055 -0.0687 -0.0110 484  TYR A CA    
5093 C C     . TYR A 301 ? 0.1099 0.0916 0.2717 -0.0032 -0.0779 -0.0081 484  TYR A C     
5094 O O     . TYR A 301 ? 0.1149 0.0946 0.3116 -0.0058 -0.0761 -0.0031 484  TYR A O     
5095 C CB    . TYR A 301 ? 0.1089 0.1120 0.3304 -0.0036 -0.0680 -0.0119 484  TYR A CB    
5096 C CG    . TYR A 301 ? 0.1355 0.1306 0.3811 -0.0029 -0.0940 0.0038  484  TYR A CG    
5097 C CD1   . TYR A 301 ? 0.1720 0.1475 0.4267 0.0098  -0.1005 0.0120  484  TYR A CD1   
5098 C CD2   . TYR A 301 ? 0.1610 0.1523 0.4304 0.0109  -0.1051 0.0054  484  TYR A CD2   
5099 C CE1   . TYR A 301 ? 0.1927 0.1671 0.4687 0.0293  -0.1052 0.0147  484  TYR A CE1   
5100 C CE2   . TYR A 301 ? 0.1911 0.1684 0.4711 0.0289  -0.1077 0.0045  484  TYR A CE2   
5101 C CZ    . TYR A 301 ? 0.2086 0.1963 0.4633 0.0564  -0.0991 0.0198  484  TYR A CZ    
5102 O OH    . TYR A 301 ? 0.2651 0.2375 0.5102 0.1002  -0.0785 0.0352  484  TYR A OH    
5112 N N     . VAL A 302 ? 0.1019 0.0882 0.2410 0.0075  -0.0746 -0.0086 485  VAL A N     
5113 C CA    . VAL A 302 ? 0.0993 0.0990 0.2284 0.0045  -0.0734 -0.0015 485  VAL A CA    
5114 C C     . VAL A 302 ? 0.0836 0.1039 0.2148 -0.0031 -0.0602 -0.0019 485  VAL A C     
5115 O O     . VAL A 302 ? 0.1157 0.1333 0.2540 -0.0026 -0.0861 -0.0042 485  VAL A O     
5116 C CB    . VAL A 302 ? 0.0859 0.1061 0.2266 -0.0053 -0.0610 0.0012  485  VAL A CB    
5117 C CG1   . VAL A 302 ? 0.0881 0.1014 0.2546 -0.0168 -0.0525 0.0145  485  VAL A CG1   
5118 C CG2   . VAL A 302 ? 0.0869 0.1288 0.2344 0.0008  -0.0604 0.0160  485  VAL A CG2   
5128 N N     . ILE A 303 ? 0.1083 0.1262 0.2167 0.0054  -0.0804 -0.0009 486  ILE A N     
5129 C CA    . ILE A 303 ? 0.1390 0.1787 0.2059 0.0492  -0.0793 0.0001  486  ILE A CA    
5130 C C     . ILE A 303 ? 0.1611 0.1928 0.2479 0.0572  -0.1020 -0.0417 486  ILE A C     
5131 O O     . ILE A 303 ? 0.2579 0.2510 0.2534 0.0916  -0.1377 -0.0596 486  ILE A O     
5132 C CB    . ILE A 303 ? 0.1495 0.2303 0.1445 0.0505  -0.0397 0.0232  486  ILE A CB    
5133 C CG1   . ILE A 303 ? 0.1616 0.2743 0.0993 0.0323  -0.0099 0.0327  486  ILE A CG1   
5134 C CG2   . ILE A 303 ? 0.1581 0.2253 0.1774 0.0326  -0.0372 0.0363  486  ILE A CG2   
5135 C CD1   . ILE A 303 ? 0.1974 0.3060 0.1240 0.0456  0.0110  0.0594  486  ILE A CD1   
5147 N N     . ASP A 304 ? 0.1393 0.1555 0.2279 0.0427  -0.0906 -0.0222 487  ASP A N     
5148 C CA    A ASP A 304 ? 0.1399 0.1463 0.2320 0.0466  -0.0713 -0.0234 487  ASP A CA    
5149 C CA    B ASP A 304 ? 0.1737 0.1593 0.2333 0.0366  -0.0913 -0.0217 487  ASP A CA    
5150 C C     . ASP A 304 ? 0.1248 0.1197 0.2392 0.0157  -0.0916 -0.0220 487  ASP A C     
5151 O O     . ASP A 304 ? 0.1390 0.0967 0.2456 -0.0013 -0.0923 -0.0256 487  ASP A O     
5152 C CB    A ASP A 304 ? 0.2363 0.1728 0.2333 0.1001  0.0244  -0.0161 487  ASP A CB    
5153 C CB    B ASP A 304 ? 0.2549 0.2114 0.2412 0.0593  -0.0759 -0.0307 487  ASP A CB    
5154 C CG    A ASP A 304 ? 0.3850 0.1940 0.3261 0.1032  0.1055  0.0096  487  ASP A CG    
5155 C CG    B ASP A 304 ? 0.3078 0.2644 0.3062 0.0687  -0.0387 -0.0567 487  ASP A CG    
5156 O OD1   A ASP A 304 ? 0.4590 0.2053 0.3630 0.1171  0.1117  0.0201  487  ASP A OD1   
5157 O OD1   B ASP A 304 ? 0.2775 0.2758 0.3410 0.0457  -0.1032 -0.0540 487  ASP A OD1   
5158 O OD2   A ASP A 304 ? 0.4366 0.1991 0.3776 0.0832  0.1325  0.0312  487  ASP A OD2   
5159 O OD2   B ASP A 304 ? 0.3730 0.2900 0.3144 0.0829  -0.0155 -0.0872 487  ASP A OD2   
5168 N N     . VAL A 305 ? 0.1071 0.0923 0.2461 -0.0011 -0.0743 -0.0213 488  VAL A N     
5169 C CA    . VAL A 305 ? 0.1031 0.0987 0.2447 -0.0044 -0.0696 -0.0220 488  VAL A CA    
5170 C C     . VAL A 305 ? 0.1177 0.1063 0.2597 -0.0017 -0.0832 -0.0222 488  VAL A C     
5171 O O     . VAL A 305 ? 0.1351 0.1134 0.2915 0.0065  -0.0893 -0.0416 488  VAL A O     
5172 C CB    . VAL A 305 ? 0.1033 0.1129 0.2584 -0.0078 -0.0656 -0.0282 488  VAL A CB    
5173 C CG1   . VAL A 305 ? 0.1203 0.1139 0.2627 -0.0089 -0.0636 -0.0456 488  VAL A CG1   
5174 C CG2   . VAL A 305 ? 0.1164 0.1133 0.2866 -0.0080 -0.0518 -0.0236 488  VAL A CG2   
5184 N N     . ASN A 306 ? 0.1208 0.1118 0.2549 0.0168  -0.0884 -0.0217 489  ASN A N     
5185 C CA    . ASN A 306 ? 0.1088 0.1412 0.3040 0.0196  -0.0696 -0.0112 489  ASN A CA    
5186 C C     . ASN A 306 ? 0.1196 0.1279 0.2916 0.0234  -0.0824 -0.0252 489  ASN A C     
5187 O O     . ASN A 306 ? 0.1578 0.1502 0.3293 0.0494  -0.0604 -0.0249 489  ASN A O     
5188 C CB    . ASN A 306 ? 0.1572 0.1953 0.3815 0.0343  -0.0106 0.0315  489  ASN A CB    
5189 C CG    . ASN A 306 ? 0.3071 0.2559 0.4992 0.0087  0.0278  0.0327  489  ASN A CG    
5190 O OD1   . ASN A 306 ? 0.3368 0.2702 0.5868 -0.0094 0.0289  0.0416  489  ASN A OD1   
5191 N ND2   . ASN A 306 ? 0.3677 0.2784 0.4768 -0.0062 -0.0104 0.0267  489  ASN A ND2   
5198 N N     . GLY A 307 ? 0.1165 0.1146 0.2757 0.0104  -0.0855 -0.0166 490  GLY A N     
5199 C CA    . GLY A 307 ? 0.1267 0.1063 0.2912 -0.0001 -0.0942 -0.0027 490  GLY A CA    
5200 C C     . GLY A 307 ? 0.1097 0.0844 0.2593 0.0044  -0.0810 -0.0114 490  GLY A C     
5201 O O     . GLY A 307 ? 0.1296 0.0877 0.2648 0.0166  -0.0932 -0.0245 490  GLY A O     
5205 N N     . PHE A 308 ? 0.1100 0.0823 0.2451 0.0061  -0.0811 -0.0180 491  PHE A N     
5206 C CA    . PHE A 308 ? 0.0953 0.0852 0.2234 0.0021  -0.0704 -0.0089 491  PHE A CA    
5207 C C     . PHE A 308 ? 0.0924 0.0957 0.2204 -0.0054 -0.0679 0.0046  491  PHE A C     
5208 O O     . PHE A 308 ? 0.1285 0.1009 0.2498 -0.0192 -0.0592 0.0007  491  PHE A O     
5209 C CB    . PHE A 308 ? 0.1267 0.0758 0.2488 0.0046  -0.0943 -0.0084 491  PHE A CB    
5210 C CG    . PHE A 308 ? 0.1208 0.0808 0.2658 0.0040  -0.0896 -0.0053 491  PHE A CG    
5211 C CD1   . PHE A 308 ? 0.1197 0.0906 0.2721 0.0034  -0.0885 -0.0005 491  PHE A CD1   
5212 C CD2   . PHE A 308 ? 0.1362 0.0974 0.2671 0.0214  -0.0868 -0.0063 491  PHE A CD2   
5213 C CE1   . PHE A 308 ? 0.1155 0.1003 0.2963 0.0092  -0.0783 0.0012  491  PHE A CE1   
5214 C CE2   . PHE A 308 ? 0.1442 0.0998 0.2889 0.0195  -0.0850 -0.0001 491  PHE A CE2   
5215 C CZ    . PHE A 308 ? 0.1346 0.0958 0.2637 0.0132  -0.0740 -0.0082 491  PHE A CZ    
5225 N N     . SER A 309 ? 0.0948 0.0934 0.2248 -0.0101 -0.0666 -0.0013 492  SER A N     
5226 C CA    . SER A 309 ? 0.1111 0.1004 0.2523 -0.0171 -0.0740 0.0057  492  SER A CA    
5227 C C     . SER A 309 ? 0.0908 0.1111 0.2175 -0.0234 -0.0534 -0.0077 492  SER A C     
5228 O O     . SER A 309 ? 0.0959 0.1215 0.2353 -0.0170 -0.0585 -0.0191 492  SER A O     
5229 C CB    . SER A 309 ? 0.1721 0.1257 0.2975 -0.0375 -0.0911 0.0465  492  SER A CB    
5230 O OG    . SER A 309 ? 0.2625 0.1704 0.3435 -0.0577 -0.0749 0.0403  492  SER A OG    
5236 N N     . PHE A 310 ? 0.0935 0.1103 0.2517 0.0010  -0.0650 -0.0184 493  PHE A N     
5237 C CA    . PHE A 310 ? 0.1063 0.0973 0.2585 -0.0022 -0.0768 -0.0092 493  PHE A CA    
5238 C C     . PHE A 310 ? 0.1398 0.1222 0.2660 -0.0162 -0.0940 -0.0088 493  PHE A C     
5239 O O     . PHE A 310 ? 0.1697 0.1374 0.2651 -0.0379 -0.0590 -0.0149 493  PHE A O     
5240 C CB    . PHE A 310 ? 0.1154 0.1050 0.2857 0.0055  -0.0843 -0.0142 493  PHE A CB    
5241 C CG    . PHE A 310 ? 0.1092 0.0983 0.2841 0.0106  -0.0776 -0.0285 493  PHE A CG    
5242 C CD1   . PHE A 310 ? 0.1549 0.1022 0.2843 0.0170  -0.1134 -0.0268 493  PHE A CD1   
5243 C CD2   . PHE A 310 ? 0.1210 0.1089 0.3493 0.0113  -0.0806 -0.0274 493  PHE A CD2   
5244 C CE1   . PHE A 310 ? 0.2413 0.1139 0.3055 0.0140  -0.1366 -0.0361 493  PHE A CE1   
5245 C CE2   . PHE A 310 ? 0.1567 0.1077 0.3544 0.0150  -0.1158 -0.0324 493  PHE A CE2   
5246 C CZ    . PHE A 310 ? 0.1870 0.1097 0.3163 0.0124  -0.1332 -0.0272 493  PHE A CZ    
5256 N N     . VAL A 311 ? 0.1195 0.1200 0.2593 -0.0225 -0.0810 0.0045  494  VAL A N     
5257 C CA    . VAL A 311 ? 0.1254 0.1245 0.2416 -0.0196 -0.0882 0.0025  494  VAL A CA    
5258 C C     . VAL A 311 ? 0.1428 0.1512 0.2430 -0.0157 -0.0741 -0.0042 494  VAL A C     
5259 O O     . VAL A 311 ? 0.1306 0.1803 0.2858 0.0029  -0.0545 0.0320  494  VAL A O     
5260 C CB    . VAL A 311 ? 0.1304 0.1150 0.2559 -0.0049 -0.0965 -0.0011 494  VAL A CB    
5261 C CG1   . VAL A 311 ? 0.1826 0.1187 0.2883 -0.0263 -0.1124 -0.0037 494  VAL A CG1   
5262 C CG2   . VAL A 311 ? 0.1423 0.1005 0.2907 0.0009  -0.1050 0.0077  494  VAL A CG2   
5272 N N     . LYS A 312 ? 0.1440 0.1536 0.2804 -0.0286 -0.0662 -0.0238 495  LYS A N     
5273 C CA    . LYS A 312 ? 0.1552 0.1753 0.3071 -0.0453 -0.0314 -0.0470 495  LYS A CA    
5274 C C     . LYS A 312 ? 0.1398 0.1422 0.3264 -0.0238 -0.0610 -0.0317 495  LYS A C     
5275 O O     . LYS A 312 ? 0.1575 0.1415 0.3364 -0.0175 -0.0673 -0.0146 495  LYS A O     
5276 C CB    . LYS A 312 ? 0.2757 0.2511 0.3631 -0.0626 -0.0264 -0.0742 495  LYS A CB    
5277 C CG    . LYS A 312 ? 0.4823 0.3161 0.4585 -0.0635 -0.0272 -0.0702 495  LYS A CG    
5278 C CD    . LYS A 312 ? 0.6557 0.3650 0.5347 -0.0424 -0.0235 -0.0512 495  LYS A CD    
5279 C CE    . LYS A 312 ? 0.7697 0.3931 0.5973 -0.0219 -0.0260 -0.0271 495  LYS A CE    
5280 N NZ    . LYS A 312 ? 0.8294 0.4051 0.6346 -0.0212 -0.0152 -0.0152 495  LYS A NZ    
5294 N N     . ASP A 313 ? 0.1380 0.1189 0.3449 -0.0105 -0.0530 -0.0250 496  ASP A N     
5295 C CA    . ASP A 313 ? 0.1305 0.1303 0.3303 -0.0024 -0.0230 -0.0298 496  ASP A CA    
5296 C C     . ASP A 313 ? 0.1925 0.1171 0.3226 -0.0179 -0.0153 -0.0410 496  ASP A C     
5297 O O     . ASP A 313 ? 0.2710 0.1351 0.3832 -0.0622 0.0516  -0.0570 496  ASP A O     
5298 C CB    . ASP A 313 ? 0.1621 0.1642 0.3594 -0.0288 -0.0317 -0.0123 496  ASP A CB    
5299 C CG    . ASP A 313 ? 0.2405 0.2120 0.3835 -0.0145 0.0172  -0.0030 496  ASP A CG    
5300 O OD1   . ASP A 313 ? 0.2275 0.2279 0.4635 0.0273  0.0301  -0.0108 496  ASP A OD1   
5301 O OD2   . ASP A 313 ? 0.3195 0.2433 0.3386 -0.0147 0.0513  -0.0299 496  ASP A OD2   
5306 N N     . ASN A 314 ? 0.1734 0.0959 0.3085 -0.0086 -0.0366 -0.0208 497  ASN A N     
5307 C CA    . ASN A 314 ? 0.1331 0.0898 0.2925 -0.0126 -0.0636 -0.0178 497  ASN A CA    
5308 C C     . ASN A 314 ? 0.1111 0.0892 0.2869 0.0010  -0.0781 -0.0139 497  ASN A C     
5309 O O     . ASN A 314 ? 0.1090 0.0774 0.2811 0.0038  -0.0691 -0.0108 497  ASN A O     
5310 C CB    . ASN A 314 ? 0.1313 0.0778 0.2688 -0.0014 -0.0602 -0.0219 497  ASN A CB    
5311 C CG    . ASN A 314 ? 0.1303 0.0750 0.2616 -0.0034 -0.0641 -0.0133 497  ASN A CG    
5312 O OD1   . ASN A 314 ? 0.1449 0.0743 0.2666 0.0089  -0.0578 0.0016  497  ASN A OD1   
5313 N ND2   . ASN A 314 ? 0.1651 0.0810 0.2665 0.0051  -0.0870 -0.0152 497  ASN A ND2   
5320 N N     . LYS A 315 ? 0.1175 0.1148 0.2772 -0.0057 -0.0837 -0.0096 498  LYS A N     
5321 C CA    . LYS A 315 ? 0.1240 0.1368 0.2912 -0.0150 -0.0792 -0.0029 498  LYS A CA    
5322 C C     . LYS A 315 ? 0.1323 0.1016 0.2780 -0.0120 -0.0853 -0.0144 498  LYS A C     
5323 O O     . LYS A 315 ? 0.1310 0.1018 0.2897 -0.0083 -0.0893 -0.0116 498  LYS A O     
5324 C CB    . LYS A 315 ? 0.1608 0.2124 0.3383 -0.0107 -0.1033 0.0082  498  LYS A CB    
5325 C CG    . LYS A 315 ? 0.1874 0.2643 0.4304 -0.0343 -0.1124 0.0097  498  LYS A CG    
5326 C CD    . LYS A 315 ? 0.2431 0.3112 0.5251 -0.0711 -0.1260 0.0042  498  LYS A CD    
5327 C CE    . LYS A 315 ? 0.4019 0.3485 0.6052 -0.0873 -0.0832 -0.0123 498  LYS A CE    
5328 N NZ    . LYS A 315 ? 0.5060 0.3705 0.6539 -0.0854 -0.0847 -0.0288 498  LYS A NZ    
5342 N N     . ALA A 316 ? 0.1263 0.0810 0.2545 -0.0100 -0.0693 -0.0142 499  ALA A N     
5343 C CA    . ALA A 316 ? 0.1370 0.0767 0.2457 -0.0107 -0.0741 -0.0040 499  ALA A CA    
5344 C C     . ALA A 316 ? 0.1324 0.0792 0.2481 0.0115  -0.0746 0.0078  499  ALA A C     
5345 O O     . ALA A 316 ? 0.1333 0.0772 0.2620 0.0016  -0.0827 -0.0108 499  ALA A O     
5346 C CB    . ALA A 316 ? 0.1658 0.0786 0.2564 -0.0074 -0.0719 -0.0153 499  ALA A CB    
5352 N N     . TYR A 317 ? 0.0970 0.0774 0.2490 0.0053  -0.0684 -0.0037 500  TYR A N     
5353 C CA    . TYR A 317 ? 0.0956 0.0747 0.2414 0.0015  -0.0675 -0.0128 500  TYR A CA    
5354 C C     . TYR A 317 ? 0.0979 0.0808 0.2492 0.0034  -0.0701 -0.0156 500  TYR A C     
5355 O O     . TYR A 317 ? 0.1062 0.0833 0.2424 -0.0079 -0.0750 -0.0002 500  TYR A O     
5356 C CB    . TYR A 317 ? 0.1091 0.0886 0.2527 0.0034  -0.0808 -0.0109 500  TYR A CB    
5357 C CG    . TYR A 317 ? 0.1040 0.0812 0.2492 0.0060  -0.0725 0.0027  500  TYR A CG    
5358 C CD1   . TYR A 317 ? 0.1106 0.0869 0.2577 -0.0010 -0.0821 0.0018  500  TYR A CD1   
5359 C CD2   . TYR A 317 ? 0.1121 0.0806 0.2572 0.0083  -0.0772 -0.0029 500  TYR A CD2   
5360 C CE1   . TYR A 317 ? 0.1082 0.0818 0.2559 0.0123  -0.0681 -0.0026 500  TYR A CE1   
5361 C CE2   . TYR A 317 ? 0.1144 0.0861 0.2603 -0.0019 -0.0846 -0.0018 500  TYR A CE2   
5362 C CZ    . TYR A 317 ? 0.1046 0.0916 0.2619 0.0084  -0.0758 -0.0180 500  TYR A CZ    
5363 O OH    . TYR A 317 ? 0.1312 0.1102 0.2997 0.0246  -0.0939 -0.0522 500  TYR A OH    
5373 N N     . TYR A 318 ? 0.1037 0.0723 0.2445 0.0093  -0.0674 -0.0240 501  TYR A N     
5374 C CA    . TYR A 318 ? 0.1167 0.0789 0.2214 0.0027  -0.0637 -0.0245 501  TYR A CA    
5375 C C     . TYR A 318 ? 0.1095 0.0816 0.2314 0.0079  -0.0624 -0.0212 501  TYR A C     
5376 O O     . TYR A 318 ? 0.1270 0.0755 0.2447 0.0112  -0.0795 -0.0063 501  TYR A O     
5377 C CB    . TYR A 318 ? 0.1098 0.0935 0.2450 0.0140  -0.0805 -0.0280 501  TYR A CB    
5378 C CG    . TYR A 318 ? 0.1105 0.1024 0.2335 0.0124  -0.0816 -0.0225 501  TYR A CG    
5379 C CD1   . TYR A 318 ? 0.1111 0.1171 0.2230 0.0136  -0.0520 -0.0144 501  TYR A CD1   
5380 C CD2   . TYR A 318 ? 0.1180 0.1193 0.2837 -0.0080 -0.0788 -0.0185 501  TYR A CD2   
5381 C CE1   . TYR A 318 ? 0.1137 0.1256 0.2539 -0.0001 -0.0582 -0.0167 501  TYR A CE1   
5382 C CE2   . TYR A 318 ? 0.1191 0.1276 0.2917 0.0019  -0.0524 -0.0099 501  TYR A CE2   
5383 C CZ    . TYR A 318 ? 0.1360 0.1197 0.2575 0.0134  -0.0470 -0.0131 501  TYR A CZ    
5384 O OH    . TYR A 318 ? 0.1787 0.1157 0.2639 0.0135  -0.0378 -0.0102 501  TYR A OH    
5394 N N     . ASP A 319 ? 0.1247 0.0912 0.2432 0.0046  -0.0901 -0.0211 502  ASP A N     
5395 C CA    . ASP A 319 ? 0.1328 0.0977 0.2643 -0.0028 -0.0876 -0.0257 502  ASP A CA    
5396 C C     . ASP A 319 ? 0.1306 0.0919 0.2464 0.0014  -0.0953 -0.0122 502  ASP A C     
5397 O O     . ASP A 319 ? 0.1757 0.0886 0.2395 -0.0015 -0.0838 0.0035  502  ASP A O     
5398 C CB    . ASP A 319 ? 0.1358 0.1171 0.2646 0.0045  -0.0927 -0.0403 502  ASP A CB    
5399 C CG    . ASP A 319 ? 0.1551 0.1513 0.3099 0.0216  -0.1003 -0.0799 502  ASP A CG    
5400 O OD1   . ASP A 319 ? 0.1695 0.1629 0.3329 0.0317  -0.1124 -0.0893 502  ASP A OD1   
5401 O OD2   . ASP A 319 ? 0.1661 0.1707 0.3621 -0.0016 -0.0850 -0.0913 502  ASP A OD2   
5406 N N     . SER A 320 ? 0.1231 0.0879 0.2369 0.0025  -0.0857 -0.0024 503  SER A N     
5407 C CA    . SER A 320 ? 0.1071 0.0791 0.2491 -0.0089 -0.0655 0.0095  503  SER A CA    
5408 C C     . SER A 320 ? 0.1359 0.0828 0.2479 -0.0176 -0.0737 0.0122  503  SER A C     
5409 O O     . SER A 320 ? 0.1291 0.0818 0.2717 0.0030  -0.0754 0.0167  503  SER A O     
5410 C CB    . SER A 320 ? 0.1339 0.0826 0.2862 -0.0066 -0.0709 -0.0059 503  SER A CB    
5411 O OG    . SER A 320 ? 0.1779 0.0884 0.3213 0.0022  -0.0640 -0.0175 503  SER A OG    
5417 N N     . CYS A 321 ? 0.1267 0.0772 0.2349 -0.0143 -0.0819 0.0085  504  CYS A N     
5418 C CA    . CYS A 321 ? 0.1133 0.0712 0.2523 -0.0015 -0.0690 0.0015  504  CYS A CA    
5419 C C     . CYS A 321 ? 0.1091 0.0781 0.2347 0.0036  -0.0792 -0.0077 504  CYS A C     
5420 O O     . CYS A 321 ? 0.1212 0.0708 0.2389 -0.0025 -0.0805 0.0011  504  CYS A O     
5421 C CB    . CYS A 321 ? 0.1067 0.0807 0.2630 0.0013  -0.0779 -0.0002 504  CYS A CB    
5422 S SG    . CYS A 321 ? 0.1164 0.0992 0.2632 -0.0104 -0.0759 -0.0133 504  CYS A SG    
5428 N N     . ALA A 322 ? 0.1110 0.0846 0.2311 0.0146  -0.0755 -0.0049 505  ALA A N     
5429 C CA    . ALA A 322 ? 0.1180 0.0866 0.2573 0.0053  -0.0876 -0.0057 505  ALA A CA    
5430 C C     . ALA A 322 ? 0.1396 0.0897 0.2423 0.0090  -0.0936 -0.0012 505  ALA A C     
5431 O O     . ALA A 322 ? 0.1505 0.0965 0.2665 -0.0148 -0.0850 0.0139  505  ALA A O     
5432 C CB    . ALA A 322 ? 0.1347 0.0917 0.2550 0.0068  -0.0948 0.0063  505  ALA A CB    
5438 N N     . ASN A 323 ? 0.1488 0.0896 0.2293 0.0077  -0.0957 -0.0091 506  ASN A N     
5439 C CA    A ASN A 323 ? 0.1580 0.0979 0.2341 -0.0045 -0.0956 -0.0129 506  ASN A CA    
5440 C CA    B ASN A 323 ? 0.1659 0.1008 0.2267 0.0008  -0.0692 -0.0167 506  ASN A CA    
5441 C C     . ASN A 323 ? 0.1601 0.0954 0.2248 0.0041  -0.0735 -0.0184 506  ASN A C     
5442 O O     . ASN A 323 ? 0.1733 0.0973 0.2342 0.0092  -0.0794 0.0000  506  ASN A O     
5443 C CB    A ASN A 323 ? 0.2077 0.1284 0.2762 -0.0184 -0.0720 -0.0319 506  ASN A CB    
5444 C CB    B ASN A 323 ? 0.2036 0.1311 0.2455 -0.0054 -0.0136 -0.0290 506  ASN A CB    
5445 C CG    A ASN A 323 ? 0.3149 0.1708 0.3444 -0.0231 -0.0693 -0.0457 506  ASN A CG    
5446 C CG    B ASN A 323 ? 0.2947 0.1742 0.2960 -0.0108 0.0067  -0.0251 506  ASN A CG    
5447 O OD1   A ASN A 323 ? 0.3212 0.1874 0.4051 -0.0194 -0.1180 -0.0829 506  ASN A OD1   
5448 O OD1   B ASN A 323 ? 0.3564 0.2023 0.3196 -0.0269 0.0101  -0.0152 506  ASN A OD1   
5449 N ND2   A ASN A 323 ? 0.3762 0.1908 0.3541 -0.0541 -0.0573 -0.0407 506  ASN A ND2   
5450 N ND2   B ASN A 323 ? 0.3218 0.1909 0.3300 -0.0061 0.0130  -0.0268 506  ASN A ND2   
5463 N N     . ILE A 324 ? 0.1250 0.0944 0.2239 0.0081  -0.0817 -0.0079 507  ILE A N     
5464 C CA    . ILE A 324 ? 0.1194 0.0993 0.2222 0.0079  -0.0738 -0.0016 507  ILE A CA    
5465 C C     . ILE A 324 ? 0.1422 0.0887 0.2200 0.0057  -0.0539 0.0045  507  ILE A C     
5466 O O     . ILE A 324 ? 0.1537 0.0852 0.2724 0.0146  -0.0654 0.0186  507  ILE A O     
5467 C CB    . ILE A 324 ? 0.1063 0.1046 0.2425 0.0103  -0.0736 -0.0103 507  ILE A CB    
5468 C CG1   . ILE A 324 ? 0.1709 0.0978 0.2893 0.0288  -0.0848 -0.0112 507  ILE A CG1   
5469 C CG2   . ILE A 324 ? 0.1388 0.1205 0.2271 0.0141  -0.0560 -0.0197 507  ILE A CG2   
5470 C CD1   . ILE A 324 ? 0.1615 0.0978 0.2889 0.0263  -0.0861 -0.0051 507  ILE A CD1   
5482 N N     . LEU A 325 ? 0.1160 0.0872 0.2060 0.0013  -0.0537 0.0078  508  LEU A N     
5483 C CA    . LEU A 325 ? 0.1486 0.0850 0.1741 -0.0164 -0.0381 0.0021  508  LEU A CA    
5484 C C     . LEU A 325 ? 0.1581 0.0865 0.1964 -0.0066 -0.0431 -0.0044 508  LEU A C     
5485 O O     . LEU A 325 ? 0.1585 0.0794 0.2375 -0.0063 -0.0674 -0.0081 508  LEU A O     
5486 C CB    . LEU A 325 ? 0.1441 0.0850 0.2050 -0.0201 -0.0649 0.0053  508  LEU A CB    
5487 C CG    . LEU A 325 ? 0.1525 0.1209 0.2067 -0.0443 -0.0812 0.0270  508  LEU A CG    
5488 C CD1   . LEU A 325 ? 0.1947 0.1131 0.2427 -0.0198 -0.0839 0.0197  508  LEU A CD1   
5489 C CD2   . LEU A 325 ? 0.2286 0.1583 0.1594 -0.0838 -0.0719 0.0246  508  LEU A CD2   
5501 N N     . ARG A 326 ? 0.1238 0.0897 0.1887 -0.0007 -0.0367 0.0000  509  ARG A N     
5502 C CA    . ARG A 326 ? 0.1623 0.0945 0.2077 -0.0051 -0.0526 -0.0083 509  ARG A CA    
5503 C C     . ARG A 326 ? 0.1853 0.0966 0.2003 -0.0012 -0.0630 -0.0067 509  ARG A C     
5504 O O     . ARG A 326 ? 0.1995 0.1077 0.2230 -0.0059 -0.0772 -0.0057 509  ARG A O     
5505 C CB    . ARG A 326 ? 0.1800 0.1184 0.2211 0.0101  -0.0768 -0.0163 509  ARG A CB    
5506 C CG    . ARG A 326 ? 0.1695 0.1647 0.2319 0.0042  -0.0894 -0.0134 509  ARG A CG    
5507 C CD    . ARG A 326 ? 0.2446 0.2259 0.2174 -0.0035 -0.0985 -0.0130 509  ARG A CD    
5508 N NE    . ARG A 326 ? 0.3285 0.2559 0.2631 -0.0054 -0.1296 -0.0203 509  ARG A NE    
5509 C CZ    . ARG A 326 ? 0.3855 0.2576 0.2737 0.0058  -0.1087 -0.0382 509  ARG A CZ    
5510 N NH1   . ARG A 326 ? 0.4069 0.2481 0.2795 0.0378  -0.0737 -0.0420 509  ARG A NH1   
5511 N NH2   . ARG A 326 ? 0.4135 0.2670 0.2732 -0.0331 -0.1090 -0.0392 509  ARG A NH2   
5525 N N     . SER A 327 ? 0.1784 0.1143 0.1896 0.0086  -0.0334 -0.0071 510  SER A N     
5526 C CA    A SER A 327 ? 0.1929 0.1180 0.1904 0.0035  -0.0056 -0.0283 510  SER A CA    
5527 C CA    B SER A 327 ? 0.1895 0.1229 0.1622 -0.0023 0.0022  -0.0070 510  SER A CA    
5528 C CA    C SER A 327 ? 0.1902 0.1272 0.1900 -0.0024 -0.0040 -0.0036 510  SER A CA    
5529 C C     . SER A 327 ? 0.1734 0.1206 0.1957 0.0029  -0.0028 -0.0019 510  SER A C     
5530 O O     . SER A 327 ? 0.2110 0.1315 0.2266 0.0059  -0.0074 0.0029  510  SER A O     
5531 C CB    A SER A 327 ? 0.2343 0.1311 0.2224 -0.0198 0.0071  -0.0646 510  SER A CB    
5532 C CB    B SER A 327 ? 0.2290 0.1397 0.1331 -0.0313 0.0347  -0.0112 510  SER A CB    
5533 C CB    C SER A 327 ? 0.2297 0.1520 0.2048 -0.0303 0.0235  -0.0007 510  SER A CB    
5534 O OG    A SER A 327 ? 0.2594 0.1422 0.2605 -0.0151 -0.0067 -0.0775 510  SER A OG    
5535 O OG    B SER A 327 ? 0.2655 0.1519 0.1368 -0.0405 0.0372  -0.0080 510  SER A OG    
5536 O OG    C SER A 327 ? 0.2717 0.1701 0.2186 -0.0427 0.0316  0.0087  510  SER A OG    
5552 N N     . THR A 328 ? 0.1746 0.1061 0.2149 0.0099  -0.0150 -0.0048 511  THR A N     
5553 C CA    . THR A 328 ? 0.1412 0.1001 0.2511 0.0124  -0.0563 -0.0103 511  THR A CA    
5554 C C     . THR A 328 ? 0.1460 0.1096 0.2587 -0.0014 -0.0593 -0.0027 511  THR A C     
5555 O O     . THR A 328 ? 0.1571 0.1131 0.2637 -0.0016 -0.0449 0.0024  511  THR A O     
5556 C CB    . THR A 328 ? 0.1543 0.0998 0.2638 0.0151  -0.0676 -0.0143 511  THR A CB    
5557 O OG1   . THR A 328 ? 0.2008 0.0948 0.2906 0.0235  -0.0698 -0.0049 511  THR A OG1   
5558 C CG2   . THR A 328 ? 0.1832 0.0948 0.2356 -0.0048 -0.0643 0.0017  511  THR A CG2   
5566 N N     . PHE A 329 ? 0.1456 0.1033 0.2503 0.0036  -0.0583 0.0098  512  PHE A N     
5567 C CA    . PHE A 329 ? 0.1670 0.1171 0.2058 -0.0282 0.0038  0.0088  512  PHE A CA    
5568 C C     . PHE A 329 ? 0.1926 0.1255 0.2308 -0.0061 -0.0379 -0.0003 512  PHE A C     
5569 O O     . PHE A 329 ? 0.2251 0.1087 0.2383 -0.0077 -0.0512 0.0115  512  PHE A O     
5570 C CB    . PHE A 329 ? 0.1183 0.1365 0.1064 -0.0288 0.0519  0.0308  512  PHE A CB    
5571 C CG    . PHE A 329 ? 0.1310 0.1073 0.0968 -0.0070 0.0586  0.0237  512  PHE A CG    
5572 C CD1   . PHE A 329 ? 0.1704 0.1050 0.1669 0.0108  -0.0636 0.0072  512  PHE A CD1   
5573 C CD2   . PHE A 329 ? 0.0950 0.1029 0.0554 -0.0023 0.0391  0.0094  512  PHE A CD2   
5574 C CE1   . PHE A 329 ? 0.1580 0.0835 0.2082 0.0230  -0.0880 -0.0022 512  PHE A CE1   
5575 C CE2   . PHE A 329 ? 0.1224 0.1059 0.0794 0.0022  0.0545  0.0141  512  PHE A CE2   
5576 C CZ    . PHE A 329 ? 0.1867 0.0939 0.2033 0.0253  -0.0765 0.0013  512  PHE A CZ    
5586 N N     . ILE A 330 ? 0.1973 0.1420 0.1845 -0.0053 -0.0276 -0.0021 513  ILE A N     
5587 C CA    . ILE A 330 ? 0.2160 0.1729 0.1992 -0.0011 -0.0232 -0.0085 513  ILE A CA    
5588 C C     . ILE A 330 ? 0.2234 0.1857 0.2537 0.0009  -0.0300 0.0195  513  ILE A C     
5589 O O     . ILE A 330 ? 0.2671 0.2012 0.2779 -0.0033 -0.0137 0.0490  513  ILE A O     
5590 C CB    . ILE A 330 ? 0.2518 0.1909 0.1649 0.0091  -0.0328 -0.0039 513  ILE A CB    
5591 C CG1   . ILE A 330 ? 0.2514 0.1937 0.1859 -0.0085 -0.0627 0.0070  513  ILE A CG1   
5592 C CG2   . ILE A 330 ? 0.3255 0.2107 0.1522 0.0286  -0.0228 -0.0089 513  ILE A CG2   
5593 C CD1   . ILE A 330 ? 0.2748 0.1895 0.2101 -0.0126 -0.0518 -0.0054 513  ILE A CD1   
5605 N N     . GLU A 331 ? 0.2064 0.1985 0.2807 0.0023  -0.0128 0.0093  514  GLU A N     
5606 C CA    . GLU A 331 ? 0.2472 0.2205 0.3103 -0.0234 -0.0118 -0.0016 514  GLU A CA    
5607 C C     . GLU A 331 ? 0.2307 0.2102 0.3187 -0.0373 -0.0039 0.0224  514  GLU A C     
5608 O O     . GLU A 331 ? 0.2555 0.2265 0.3768 -0.0436 -0.0294 0.0237  514  GLU A O     
5609 C CB    . GLU A 331 ? 0.2466 0.2552 0.3574 -0.0216 -0.0063 -0.0300 514  GLU A CB    
5610 C CG    . GLU A 331 ? 0.3561 0.3114 0.4324 -0.0434 0.0433  -0.0445 514  GLU A CG    
5611 C CD    . GLU A 331 ? 0.5494 0.3770 0.5413 -0.0555 0.0475  -0.0534 514  GLU A CD    
5612 O OE1   . GLU A 331 ? 0.6092 0.3946 0.5698 -0.0500 0.0434  -0.0601 514  GLU A OE1   
5613 O OE2   . GLU A 331 ? 0.5839 0.4123 0.5820 -0.0671 0.0579  -0.0565 514  GLU A OE2   
5620 N N     . ALA A 332 ? 0.2106 0.1905 0.2906 -0.0358 -0.0064 0.0258  515  ALA A N     
5621 C CA    . ALA A 332 ? 0.2274 0.1891 0.2882 -0.0356 0.0139  0.0181  515  ALA A CA    
5622 C C     . ALA A 332 ? 0.2735 0.1905 0.3345 -0.0534 -0.0274 0.0569  515  ALA A C     
5623 O O     . ALA A 332 ? 0.3214 0.1941 0.3483 -0.0872 0.0158  0.0506  515  ALA A O     
5624 C CB    . ALA A 332 ? 0.2171 0.1866 0.2659 -0.0393 0.0043  -0.0148 515  ALA A CB    
5630 N N     . LYS A 333 ? 0.2883 0.1917 0.3350 -0.0436 -0.0601 0.0878  516  LYS A N     
5631 C CA    . LYS A 333 ? 0.3636 0.2295 0.3588 -0.0140 -0.0645 0.1170  516  LYS A CA    
5632 C C     . LYS A 333 ? 0.4283 0.2769 0.3547 -0.0463 -0.0072 0.1410  516  LYS A C     
5633 O O     . LYS A 333 ? 0.4641 0.2858 0.3740 -0.0714 0.0013  0.1379  516  LYS A O     
5634 C CB    . LYS A 333 ? 0.3364 0.2419 0.3937 -0.0036 -0.0880 0.1271  516  LYS A CB    
5635 C CG    . LYS A 333 ? 0.4079 0.2895 0.4534 0.0038  -0.0892 0.1325  516  LYS A CG    
5636 C CD    . LYS A 333 ? 0.4176 0.3457 0.5263 0.0304  -0.1069 0.1226  516  LYS A CD    
5637 C CE    . LYS A 333 ? 0.3812 0.3927 0.5702 0.0733  -0.1515 0.1166  516  LYS A CE    
5638 N NZ    . LYS A 333 ? 0.4066 0.4204 0.6093 0.0793  -0.1196 0.1116  516  LYS A NZ    
5652 N N     . LYS A 334 ? 0.4726 0.3395 0.3790 -0.0605 0.0481  0.1417  517  LYS A N     
5653 C CA    . LYS A 334 ? 0.5102 0.4003 0.4339 -0.0782 0.0788  0.1472  517  LYS A CA    
5654 C C     . LYS A 334 ? 0.4900 0.4409 0.4851 -0.0914 0.1026  0.1765  517  LYS A C     
5655 O O     . LYS A 334 ? 0.5247 0.4602 0.4993 -0.1088 0.0892  0.2036  517  LYS A O     
5656 C CB    . LYS A 334 ? 0.5797 0.4236 0.4637 -0.0748 0.0732  0.1172  517  LYS A CB    
5657 C CG    . LYS A 334 ? 0.6444 0.4464 0.5165 -0.0654 0.0574  0.1013  517  LYS A CG    
5658 C CD    . LYS A 334 ? 0.6945 0.4655 0.5473 -0.0600 0.0473  0.0722  517  LYS A CD    
5659 C CE    . LYS A 334 ? 0.7362 0.4767 0.5464 -0.0607 0.0491  0.0474  517  LYS A CE    
5660 N NZ    . LYS A 334 ? 0.7561 0.4831 0.5504 -0.0514 0.0446  0.0407  517  LYS A NZ    
5674 N N     . LYS A 335 ? 0.4740 0.4564 0.5299 -0.0877 0.1091  0.1692  518  LYS A N     
5675 C CA    . LYS A 335 ? 0.5274 0.4784 0.6018 -0.0876 0.0932  0.1504  518  LYS A CA    
5676 C C     . LYS A 335 ? 0.5789 0.4678 0.6200 -0.1082 0.0661  0.1501  518  LYS A C     
5677 O O     . LYS A 335 ? 0.6143 0.4626 0.6280 -0.1213 0.0625  0.1684  518  LYS A O     
5678 C CB    . LYS A 335 ? 0.5482 0.5127 0.6602 -0.0612 0.1107  0.1300  518  LYS A CB    
5679 C CG    . LYS A 335 ? 0.6121 0.5467 0.7144 -0.0169 0.1093  0.1052  518  LYS A CG    
5680 C CD    . LYS A 335 ? 0.6694 0.5773 0.7696 0.0244  0.1046  0.0750  518  LYS A CD    
5681 C CE    . LYS A 335 ? 0.7220 0.6005 0.8114 0.0389  0.1239  0.0447  518  LYS A CE    
5682 N NZ    . LYS A 335 ? 0.7636 0.6156 0.8397 0.0409  0.1373  0.0318  518  LYS A NZ    
5696 N N     . MET A 336 ? 0.5946 0.4643 0.6117 -0.1132 0.0600  0.1243  519  MET A N     
5697 C CA    . MET A 336 ? 0.6177 0.4662 0.6051 -0.0774 0.0186  0.0728  519  MET A CA    
5698 C C     . MET A 336 ? 0.7045 0.4806 0.6213 -0.0472 0.0168  0.0541  519  MET A C     
5699 O O     . MET A 336 ? 0.8100 0.4867 0.6927 -0.0376 0.0474  0.0436  519  MET A O     
5700 C CB    . MET A 336 ? 0.5521 0.4600 0.5853 -0.0650 0.0237  0.0544  519  MET A CB    
5701 C CG    . MET A 336 ? 0.5737 0.4593 0.5748 -0.0485 0.0154  0.0427  519  MET A CG    
5702 S SD    . MET A 336 ? 0.6478 0.4464 0.5569 -0.0599 0.0327  0.0574  519  MET A SD    
5703 C CE    . MET A 336 ? 0.5200 0.4185 0.4841 -0.0983 -0.0064 0.1135  519  MET A CE    
5713 N N     . ASP A 337 ? 0.6270 0.4898 0.5600 -0.0178 -0.0013 0.0604  520  ASP A N     
5714 C CA    . ASP A 337 ? 0.5101 0.4933 0.5013 0.0183  -0.0161 0.0684  520  ASP A CA    
5715 C C     . ASP A 337 ? 0.4724 0.5004 0.4991 0.0510  0.0095  0.0422  520  ASP A C     
5716 O O     . ASP A 337 ? 0.5149 0.5122 0.5236 0.0647  0.0064  0.0261  520  ASP A O     
5717 C CB    . ASP A 337 ? 0.4624 0.4949 0.4853 0.0118  -0.0346 0.0930  520  ASP A CB    
5718 C CG    . ASP A 337 ? 0.4867 0.5135 0.5225 0.0318  -0.0245 0.0742  520  ASP A CG    
5719 O OD1   . ASP A 337 ? 0.5177 0.5240 0.5354 0.0244  -0.0095 0.0480  520  ASP A OD1   
5720 O OD2   . ASP A 337 ? 0.5277 0.5239 0.5701 0.0444  0.0079  0.0747  520  ASP A OD2   
5725 P PB    . ADP B .   ? 0.5379 0.5862 0.7396 0.0237  -0.1261 0.0279  600  ADP A PB    
5726 O O1B   . ADP B .   ? 0.5841 0.6086 0.7793 -0.0094 -0.1105 0.0298  600  ADP A O1B   
5727 O O2B   . ADP B .   ? 0.5690 0.6156 0.7754 0.0310  -0.0800 0.0196  600  ADP A O2B   
5728 O O3B   . ADP B .   ? 0.5902 0.6104 0.7516 0.0402  -0.1145 0.0049  600  ADP A O3B   
5729 P PA    . ADP B .   ? 0.3019 0.3885 0.4937 0.0341  -0.0749 0.1025  600  ADP A PA    
5730 O O1A   . ADP B .   ? 0.3967 0.3914 0.5190 -0.0084 0.0369  0.1372  600  ADP A O1A   
5731 O O2A   . ADP B .   ? 0.2825 0.3734 0.4893 0.0837  -0.0397 0.0928  600  ADP A O2A   
5732 O O3A   . ADP B .   ? 0.3586 0.4868 0.5971 0.0356  -0.1677 0.0725  600  ADP A O3A   
5733 O "O5'" . ADP B .   ? 0.2467 0.3280 0.4154 0.0332  -0.0904 0.0751  600  ADP A "O5'" 
5734 C "C5'" . ADP B .   ? 0.2314 0.2945 0.3650 0.0119  -0.0819 0.0478  600  ADP A "C5'" 
5735 C "C4'" . ADP B .   ? 0.1762 0.2664 0.3198 -0.0012 -0.0699 0.0437  600  ADP A "C4'" 
5736 O "O4'" . ADP B .   ? 0.1636 0.2377 0.3174 -0.0262 -0.0745 0.0456  600  ADP A "O4'" 
5737 C "C3'" . ADP B .   ? 0.1943 0.2749 0.3242 -0.0264 -0.0963 0.0456  600  ADP A "C3'" 
5738 O "O3'" . ADP B .   ? 0.2443 0.2726 0.3418 -0.0302 -0.1148 0.0508  600  ADP A "O3'" 
5739 C "C2'" . ADP B .   ? 0.1588 0.2880 0.3134 -0.0269 -0.0836 0.0317  600  ADP A "C2'" 
5740 O "O2'" . ADP B .   ? 0.1968 0.3328 0.3631 0.0044  -0.1050 0.0001  600  ADP A "O2'" 
5741 C "C1'" . ADP B .   ? 0.1615 0.2404 0.2965 -0.0205 -0.0965 0.0398  600  ADP A "C1'" 
5742 N N9    . ADP B .   ? 0.1498 0.1919 0.2791 -0.0187 -0.1058 0.0344  600  ADP A N9    
5743 C C8    . ADP B .   ? 0.1560 0.1813 0.2682 -0.0172 -0.0557 0.0125  600  ADP A C8    
5744 N N7    . ADP B .   ? 0.1457 0.1707 0.2570 -0.0108 -0.0752 0.0173  600  ADP A N7    
5745 C C5    . ADP B .   ? 0.1616 0.1611 0.2242 -0.0146 -0.0697 0.0175  600  ADP A C5    
5746 C C6    . ADP B .   ? 0.1725 0.1442 0.2305 -0.0065 -0.0871 0.0107  600  ADP A C6    
5747 N N6    . ADP B .   ? 0.1727 0.1368 0.2758 -0.0101 -0.1218 0.0033  600  ADP A N6    
5748 N N1    . ADP B .   ? 0.1490 0.1463 0.2641 -0.0193 -0.0789 0.0080  600  ADP A N1    
5749 C C2    . ADP B .   ? 0.1491 0.1585 0.2546 -0.0139 -0.0444 0.0127  600  ADP A C2    
5750 N N3    . ADP B .   ? 0.1687 0.1620 0.2578 -0.0116 -0.0824 0.0143  600  ADP A N3    
5751 C C4    . ADP B .   ? 0.1538 0.1639 0.2471 -0.0185 -0.0932 0.0298  600  ADP A C4    
5763 C C1    . EDO C .   ? 0.5061 0.4487 0.5156 0.0780  -0.1225 0.0986  601  EDO A C1    
5764 O O1    . EDO C .   ? 0.4102 0.4156 0.4741 0.0937  -0.1681 0.0992  601  EDO A O1    
5765 C C2    . EDO C .   ? 0.6197 0.4673 0.5116 0.0498  -0.0523 0.1137  601  EDO A C2    
5766 O O2    . EDO C .   ? 0.6391 0.4687 0.4776 0.0700  -0.0154 0.1381  601  EDO A O2    
5773 C C1    . EDO D .   ? 0.3805 0.4269 0.4189 -0.0003 -0.0496 0.0410  602  EDO A C1    
5774 O O1    . EDO D .   ? 0.3019 0.4436 0.4005 0.0155  -0.0889 0.0194  602  EDO A O1    
5775 C C2    . EDO D .   ? 0.3984 0.4057 0.4554 0.0198  -0.0900 0.0522  602  EDO A C2    
5776 O O2    . EDO D .   ? 0.3330 0.3923 0.4646 0.0019  -0.1270 0.0600  602  EDO A O2    
5783 C C1    . EDO E .   ? 0.3193 0.2740 0.3727 0.0152  -0.0413 0.0125  603  EDO A C1    
5784 O O1    . EDO E .   ? 0.2376 0.2296 0.3921 0.0256  -0.0532 0.0113  603  EDO A O1    
5785 C C2    . EDO E .   ? 0.3425 0.3172 0.4025 -0.0170 -0.0077 -0.0160 603  EDO A C2    
5786 O O2    . EDO E .   ? 0.2818 0.3407 0.4172 -0.0743 -0.0169 -0.0127 603  EDO A O2    
5793 C C1    . EDO F .   ? 0.2873 0.3609 0.3342 0.0078  -0.1406 0.0171  604  EDO A C1    
5794 O O1    . EDO F .   ? 0.3823 0.3754 0.3889 0.0017  -0.1246 0.0086  604  EDO A O1    
5795 C C2    . EDO F .   ? 0.3628 0.3899 0.4226 0.0062  -0.0707 -0.0065 604  EDO A C2    
5796 O O2    . EDO F .   ? 0.4753 0.4298 0.4828 -0.0012 -0.0399 -0.0233 604  EDO A O2    
5803 C C1    . EDO G .   ? 0.3993 0.4606 0.4256 0.0418  0.0137  -0.0243 605  EDO A C1    
5804 O O1    . EDO G .   ? 0.4378 0.4637 0.4327 0.0342  0.0056  -0.0427 605  EDO A O1    
5805 C C2    . EDO G .   ? 0.3844 0.4663 0.4177 0.0340  -0.0530 -0.0251 605  EDO A C2    
5806 O O2    . EDO G .   ? 0.4035 0.4757 0.4302 -0.0033 -0.0757 -0.0459 605  EDO A O2    
5813 O O     . HOH H .   ? 0.2130 0.2941 0.4122 0.0487  -0.0872 0.0615  701  HOH A O     
5816 O O     . HOH H .   ? 0.3412 0.2652 0.3727 0.0553  -0.0005 0.0577  702  HOH A O     
5819 O O     . HOH H .   ? 0.2956 0.3333 0.2988 -0.0854 -0.0936 0.0014  703  HOH A O     
5822 O O     . HOH H .   ? 0.2940 0.2560 0.4282 -0.0422 0.0565  -0.0603 704  HOH A O     
5825 O O     . HOH H .   ? 0.3905 0.2749 0.5971 0.0792  -0.2003 0.0459  705  HOH A O     
5828 O O     . HOH H .   ? 0.3825 0.3350 0.4755 0.1089  -0.0666 0.0097  706  HOH A O     
5831 O O     . HOH H .   ? 0.4898 0.4191 0.6037 0.0739  -0.2606 0.0161  707  HOH A O     
5834 O O     . HOH H .   ? 0.5444 0.2910 0.5709 0.1227  -0.2585 -0.0165 708  HOH A O     
5837 O O     . HOH H .   ? 1.0951 0.3217 0.5276 -0.0091 -0.3791 0.0045  709  HOH A O     
5840 O O     . HOH H .   ? 0.3664 0.2051 0.2901 0.0642  -0.1236 -0.0255 710  HOH A O     
5843 O O     . HOH H .   ? 0.4371 0.7569 0.5696 0.0719  -0.1026 -0.2077 711  HOH A O     
5846 O O     . HOH H .   ? 0.6525 0.5414 0.5665 0.2257  -0.1253 -0.1273 712  HOH A O     
5849 O O     . HOH H .   ? 0.7898 0.5862 0.5046 0.2326  -0.1076 -0.0654 713  HOH A O     
5852 O O     . HOH H .   ? 0.4455 0.5940 0.4927 -0.1214 0.0520  -0.1198 714  HOH A O     
5855 O O     . HOH H .   ? 0.6485 0.6041 0.6755 -0.1098 0.1874  -0.1439 715  HOH A O     
5858 O O     . HOH H .   ? 0.4717 0.5037 0.4440 -0.1453 -0.1019 0.0065  716  HOH A O     
5861 O O     . HOH H .   ? 0.3980 0.3415 0.5925 0.0859  -0.0356 -0.0739 717  HOH A O     
5864 O O     . HOH H .   ? 0.1931 0.2665 0.5594 -0.0289 -0.0281 0.0243  718  HOH A O     
5867 O O     . HOH H .   ? 0.7068 0.3699 0.3257 -0.1130 0.2030  -0.0936 719  HOH A O     
5870 O O     . HOH H .   ? 0.6735 0.6728 0.6738 0.0018  -0.0007 0.0000  720  HOH A O     
5873 O O     . HOH H .   ? 0.8149 0.4690 0.4120 0.1706  0.1361  0.1391  721  HOH A O     
5876 O O     . HOH H .   ? 0.5831 0.4315 0.4466 -0.0474 -0.2463 0.0951  722  HOH A O     
5879 O O     . HOH H .   ? 0.3911 0.1864 0.3328 -0.0556 -0.1692 0.0343  723  HOH A O     
5882 O O     . HOH H .   ? 0.5686 0.5677 0.5698 0.0015  -0.0045 0.0011  724  HOH A O     
5885 O O     . HOH H .   ? 0.6440 0.2399 0.5286 0.0694  -0.2316 -0.0944 725  HOH A O     
5888 O O     . HOH H .   ? 0.2057 0.2029 0.3451 -0.0029 -0.1113 -0.0037 726  HOH A O     
5891 O O     . HOH H .   ? 0.4524 0.3744 0.5283 0.0054  -0.0268 0.0828  727  HOH A O     
5894 O O     . HOH H .   ? 0.4643 0.8375 0.5012 0.0106  -0.1109 -0.1480 728  HOH A O     
5897 O O     . HOH H .   ? 0.6678 0.4435 0.7302 -0.0791 0.0562  -0.0220 729  HOH A O     
5900 O O     . HOH H .   ? 0.2852 0.4216 0.6325 0.0524  -0.1524 0.1379  730  HOH A O     
5903 O O     . HOH H .   ? 0.2779 0.4046 0.6804 0.0848  -0.1704 -0.0025 731  HOH A O     
5906 O O     . HOH H .   ? 0.1876 0.5051 0.4325 0.0515  -0.0562 -0.2167 732  HOH A O     
5909 O O     . HOH H .   ? 0.5550 0.3448 0.5983 0.0808  0.0080  -0.1623 733  HOH A O     
5912 O O     . HOH H .   ? 0.4363 0.6734 0.5385 0.0835  -0.2729 0.0389  734  HOH A O     
5915 O O     . HOH H .   ? 0.7849 0.4913 0.3794 -0.2582 0.0216  -0.1159 735  HOH A O     
5918 O O     . HOH H .   ? 0.4279 0.3298 0.7870 0.1055  -0.2987 -0.1621 736  HOH A O     
5921 O O     . HOH H .   ? 0.2911 0.2916 0.3356 -0.0343 -0.0747 0.0291  737  HOH A O     
5924 O O     . HOH H .   ? 0.1565 0.2350 0.4084 0.0267  -0.0210 -0.0785 738  HOH A O     
5927 O O     . HOH H .   ? 0.6956 0.4911 0.6252 -0.1293 -0.3041 0.1752  739  HOH A O     
5930 O O     . HOH H .   ? 0.5879 0.2734 0.3449 -0.0602 -0.0309 -0.0828 740  HOH A O     
5933 O O     . HOH H .   ? 0.5565 0.3705 0.6568 0.0842  -0.1553 0.1514  741  HOH A O     
5936 O O     . HOH H .   ? 0.4017 0.7838 0.3443 -0.2003 -0.1310 0.0527  742  HOH A O     
5939 O O     . HOH H .   ? 0.3934 0.3900 0.7942 0.0656  -0.0916 0.2307  743  HOH A O     
5942 O O     . HOH H .   ? 0.3769 0.1820 0.5921 0.0351  -0.1798 -0.0436 744  HOH A O     
5945 O O     . HOH H .   ? 0.0929 0.0759 0.2448 0.0049  -0.0647 -0.0028 745  HOH A O     
5948 O O     . HOH H .   ? 0.2949 0.3625 0.6150 -0.0188 -0.0881 -0.1026 746  HOH A O     
5951 O O     . HOH H .   ? 0.1427 0.1302 0.2396 -0.0347 -0.0317 0.0037  747  HOH A O     
5954 O O     . HOH H .   ? 0.3412 0.5100 0.7541 0.2108  0.0093  0.0697  748  HOH A O     
5957 O O     . HOH H .   ? 0.7679 0.2914 0.3421 -0.0220 -0.1757 -0.0259 749  HOH A O     
5960 O O     . HOH H .   ? 0.1948 0.2499 0.2768 0.0840  -0.1085 -0.0252 750  HOH A O     
5963 O O     . HOH H .   ? 0.2942 0.3372 0.4244 0.0597  -0.1485 0.0833  751  HOH A O     
5966 O O     . HOH H .   ? 0.3134 0.5297 0.4578 0.0139  -0.1326 0.0322  752  HOH A O     
5969 O O     . HOH H .   ? 0.7896 0.2968 0.4355 0.0957  0.0831  0.1371  753  HOH A O     
5972 O O     . HOH H .   ? 0.4591 0.3863 0.6037 -0.0094 0.0335  -0.1035 754  HOH A O     
5975 O O     . HOH H .   ? 0.4927 0.5241 0.4395 -0.1085 0.0209  -0.0823 755  HOH A O     
5978 O O     . HOH H .   ? 0.5204 0.4216 0.3891 -0.0765 -0.0176 0.1677  756  HOH A O     
5981 O O     . HOH H .   ? 0.3849 0.4232 0.5242 0.1061  0.0114  0.1368  757  HOH A O     
5984 O O     . HOH H .   ? 0.3432 0.3245 0.5255 0.0250  -0.1466 0.0107  758  HOH A O     
5987 O O     . HOH H .   ? 0.3630 0.1598 0.3047 0.0133  -0.0771 0.0368  759  HOH A O     
5990 O O     . HOH H .   ? 0.3061 0.1683 0.3663 -0.0291 -0.1502 -0.0327 760  HOH A O     
5993 O O     . HOH H .   ? 0.2071 0.2311 0.4255 -0.0633 -0.1228 -0.0001 761  HOH A O     
5996 O O     . HOH H .   ? 0.3828 0.2929 0.5999 -0.0242 -0.0492 -0.0798 762  HOH A O     
5999 O O     . HOH H .   ? 0.5833 0.1617 0.4696 -0.0090 0.1034  -0.0027 763  HOH A O     
6002 O O     . HOH H .   ? 0.2353 0.1813 0.5526 0.0300  -0.1691 -0.0510 764  HOH A O     
6005 O O     . HOH H .   ? 0.4640 0.2073 0.4631 0.1249  -0.1023 0.0186  765  HOH A O     
6008 O O     . HOH H .   ? 0.4609 0.2240 0.4720 -0.0317 0.0609  -0.0063 766  HOH A O     
6011 O O     . HOH H .   ? 0.3325 0.2347 0.6619 -0.0117 0.0043  0.0837  767  HOH A O     
6014 O O     . HOH H .   ? 0.2666 0.3195 0.3622 -0.0990 -0.0515 -0.0545 768  HOH A O     
6017 O O     . HOH H .   ? 0.2925 0.4331 0.5064 0.1647  -0.1191 -0.0552 769  HOH A O     
6020 O O     . HOH H .   ? 0.2863 0.2096 0.3077 0.0332  -0.1668 0.0163  770  HOH A O     
6023 O O     . HOH H .   ? 0.1423 0.1038 0.3344 0.0113  -0.1010 -0.0120 771  HOH A O     
6026 O O     . HOH H .   ? 0.1912 0.1807 0.2458 0.0061  -0.0294 -0.0120 772  HOH A O     
6029 O O     . HOH H .   ? 0.2527 0.2565 0.4462 -0.0399 -0.1386 -0.0451 773  HOH A O     
6032 O O     . HOH H .   ? 0.5063 0.3075 0.7516 0.1002  0.2266  0.0676  774  HOH A O     
6035 O O     . HOH H .   ? 0.1571 0.1346 0.3037 0.0019  -0.1066 0.0061  775  HOH A O     
6038 O O     . HOH H .   ? 0.5917 0.3826 0.9230 0.1710  0.0681  0.1962  776  HOH A O     
6041 O O     . HOH H .   ? 0.1849 0.2331 0.3818 -0.0449 -0.0541 0.0804  777  HOH A O     
6044 O O     . HOH H .   ? 0.1817 0.1929 0.2938 0.0164  -0.0993 0.0050  778  HOH A O     
6047 O O     . HOH H .   ? 0.0963 0.1149 0.2920 -0.0159 -0.0492 -0.0106 779  HOH A O     
6050 O O     . HOH H .   ? 0.6197 0.4915 0.4073 0.2238  -0.1697 0.0578  780  HOH A O     
6053 O O     . HOH H .   ? 0.4761 0.2925 0.4856 0.0553  -0.0781 -0.0144 781  HOH A O     
6056 O O     . HOH H .   ? 0.1354 0.1359 0.3786 -0.0031 -0.0812 0.0440  782  HOH A O     
6059 O O     . HOH H .   ? 0.4296 0.2212 0.4362 -0.0339 -0.2219 0.0908  783  HOH A O     
6062 O O     . HOH H .   ? 0.1680 0.1590 0.3892 0.0085  -0.0883 -0.0554 784  HOH A O     
6065 O O     . HOH H .   ? 0.1354 0.4518 0.3518 -0.0302 -0.0436 0.0818  785  HOH A O     
6068 O O     . HOH H .   ? 0.2334 0.1837 0.4983 -0.0143 -0.1372 -0.0210 786  HOH A O     
6071 O O     . HOH H .   ? 0.1110 0.0777 0.2534 -0.0084 -0.0769 0.0064  787  HOH A O     
6074 O O     . HOH H .   ? 0.1798 0.1693 0.3312 -0.0397 -0.0551 -0.0535 788  HOH A O     
6077 O O     . HOH H .   ? 0.3322 0.3448 0.8150 -0.1010 -0.1476 -0.0073 789  HOH A O     
6080 O O     . HOH H .   ? 0.2048 0.1560 0.4226 -0.0169 0.0290  -0.0232 790  HOH A O     
6083 O O     . HOH H .   ? 0.5565 0.2535 0.7752 0.0796  0.0202  -0.0639 791  HOH A O     
6086 O O     . HOH H .   ? 0.2297 0.4349 0.8889 0.0081  0.0444  -0.0704 792  HOH A O     
6089 O O     . HOH H .   ? 0.2010 0.3872 0.3806 0.0128  -0.0830 0.0685  793  HOH A O     
6092 O O     . HOH H .   ? 0.4343 0.3212 0.3915 0.0053  -0.0322 0.0977  794  HOH A O     
6095 O O     . HOH H .   ? 0.4574 0.2043 0.3982 -0.0213 -0.1393 0.0293  795  HOH A O     
6098 O O     . HOH H .   ? 0.2906 0.2536 0.4686 -0.0438 -0.2057 0.0436  796  HOH A O     
6101 O O     . HOH H .   ? 0.2943 0.3274 0.3639 0.0597  -0.1091 -0.0624 797  HOH A O     
6104 O O     . HOH H .   ? 0.5151 0.3171 0.4717 -0.0657 -0.1673 0.0271  798  HOH A O     
6107 O O     . HOH H .   ? 0.5875 0.3781 0.5756 -0.0204 0.0244  -0.0063 799  HOH A O     
6110 O O     . HOH H .   ? 0.4873 0.3980 0.3695 0.0041  -0.0895 -0.0689 800  HOH A O     
6113 O O     . HOH H .   ? 0.1733 0.2508 0.5002 0.0208  -0.1063 -0.0970 801  HOH A O     
6116 O O     . HOH H .   ? 0.1909 0.1834 0.4225 0.0153  -0.0700 0.0482  802  HOH A O     
6119 O O     . HOH H .   ? 0.3507 0.3308 0.4101 -0.1205 -0.0316 -0.1031 803  HOH A O     
6122 O O     . HOH H .   ? 0.1621 0.1373 0.4111 -0.0021 -0.0819 0.0223  804  HOH A O     
6125 O O     . HOH H .   ? 0.4064 0.4904 0.4584 -0.0962 -0.0896 -0.0939 805  HOH A O     
6128 O O     . HOH H .   ? 0.1935 0.3667 0.6030 0.0032  -0.1151 -0.0668 806  HOH A O     
6131 O O     . HOH H .   ? 0.1889 0.1835 0.3173 -0.0093 -0.1078 0.0020  807  HOH A O     
6134 O O     . HOH H .   ? 0.1247 0.1485 0.3363 0.0152  -0.0574 0.0032  808  HOH A O     
6137 O O     . HOH H .   ? 0.2300 0.1195 0.4746 -0.0048 -0.0088 0.0093  809  HOH A O     
6140 O O     . HOH H .   ? 0.4840 0.5372 0.3848 -0.2188 -0.1344 -0.0136 810  HOH A O     
6143 O O     . HOH H .   ? 0.4075 0.4445 0.5770 0.0341  0.0833  0.1356  811  HOH A O     
6146 O O     . HOH H .   ? 0.1766 0.1656 0.3783 0.0347  -0.1127 0.0027  812  HOH A O     
6149 O O     . HOH H .   ? 0.1881 0.1988 0.4854 -0.0545 -0.1016 0.0604  813  HOH A O     
6152 O O     . HOH H .   ? 0.4925 0.3897 0.6019 -0.1709 -0.2700 0.2308  814  HOH A O     
6155 O O     . HOH H .   ? 0.2971 0.1892 0.3589 -0.0698 -0.1870 0.0714  815  HOH A O     
6158 O O     . HOH H .   ? 0.5580 0.2753 0.4495 -0.0521 0.0105  0.1093  816  HOH A O     
6161 O O     . HOH H .   ? 0.4641 0.3721 0.7443 -0.0189 -0.2056 -0.0760 817  HOH A O     
6164 O O     . HOH H .   ? 0.2074 0.1251 0.3609 0.0049  -0.0791 0.0185  818  HOH A O     
6167 O O     . HOH H .   ? 0.1350 0.1403 0.2748 -0.0085 -0.0765 0.0261  819  HOH A O     
6170 O O     . HOH H .   ? 0.3146 0.2016 0.4290 0.0337  -0.0602 -0.0170 820  HOH A O     
6173 O O     . HOH H .   ? 0.4378 0.1711 0.4042 -0.0598 0.0484  -0.0106 821  HOH A O     
6176 O O     . HOH H .   ? 0.1637 0.0881 0.2387 -0.0286 -0.0782 -0.0011 822  HOH A O     
6179 O O     . HOH H .   ? 0.2418 0.1511 0.3654 -0.0678 -0.0879 -0.0112 823  HOH A O     
6182 O O     . HOH H .   ? 0.2460 0.3039 0.4816 -0.0594 -0.1421 0.1168  824  HOH A O     
6185 O O     . HOH H .   ? 0.4533 0.4340 0.8345 0.1378  0.1866  -0.0309 825  HOH A O     
6188 O O     . HOH H .   ? 0.5587 0.3096 0.8721 0.0990  -0.2674 -0.0875 826  HOH A O     
6191 O O     . HOH H .   ? 0.4396 0.3255 0.3496 0.0324  -0.1915 -0.0093 827  HOH A O     
6194 O O     . HOH H .   ? 0.1936 0.1695 0.2816 0.0168  -0.0667 0.0186  828  HOH A O     
6197 O O     . HOH H .   ? 0.4730 0.3713 0.5493 -0.1165 0.1602  -0.1401 829  HOH A O     
6200 O O     . HOH H .   ? 0.2846 0.2371 0.8713 -0.0229 -0.0577 0.0049  830  HOH A O     
6203 O O     . HOH H .   ? 0.1195 0.2009 0.3325 0.0154  -0.0814 -0.0244 831  HOH A O     
6206 O O     . HOH H .   ? 0.3099 0.5342 0.4368 -0.2042 -0.0630 0.0105  832  HOH A O     
6209 O O     . HOH H .   ? 0.4876 0.4863 0.4846 0.0009  -0.0033 -0.0004 833  HOH A O     
6212 O O     . HOH H .   ? 0.1185 0.1276 0.2582 0.0000  -0.0819 0.0359  834  HOH A O     
6215 O O     . HOH H .   ? 0.3684 0.3397 0.3499 -0.0927 -0.1839 0.0623  835  HOH A O     
6218 O O     . HOH H .   ? 0.2444 0.1669 0.3629 0.0207  -0.1602 -0.0528 836  HOH A O     
6221 O O     . HOH H .   ? 0.2626 0.1344 0.3884 -0.0069 -0.0682 -0.0036 837  HOH A O     
6224 O O     . HOH H .   ? 0.4320 0.2626 0.4016 -0.1009 -0.1170 -0.0785 838  HOH A O     
6227 O O     . HOH H .   ? 0.6758 0.7366 0.5857 0.2696  0.0453  0.0594  839  HOH A O     
6230 O O     . HOH H .   ? 0.3460 0.4665 0.9621 -0.0654 0.0767  0.1378  840  HOH A O     
6233 O O     . HOH H .   ? 0.2705 0.5122 0.7227 -0.0145 -0.1692 0.1444  841  HOH A O     
6236 O O     . HOH H .   ? 0.2828 0.2507 0.3744 0.0369  -0.0903 0.0093  842  HOH A O     
6239 O O     . HOH H .   ? 0.1709 0.1173 0.3812 -0.0265 -0.0949 0.0384  843  HOH A O     
6242 O O     . HOH H .   ? 0.3345 0.4243 0.3354 0.0495  -0.1345 -0.1021 844  HOH A O     
6245 O O     . HOH H .   ? 0.8634 0.3613 0.4675 -0.2152 -0.1754 -0.0187 845  HOH A O     
6248 O O     . HOH H .   ? 0.3122 0.2336 0.4255 0.0082  -0.1268 -0.0339 846  HOH A O     
6251 O O     . HOH H .   ? 0.0921 0.0826 0.2275 -0.0010 -0.0675 0.0049  847  HOH A O     
6254 O O     . HOH H .   ? 0.6348 0.3131 0.4156 -0.1375 -0.0714 -0.0332 848  HOH A O     
6257 O O     . HOH H .   ? 0.5681 0.4171 0.6568 0.0381  0.0203  0.0934  849  HOH A O     
6260 O O     . HOH H .   ? 0.4333 0.3237 0.4906 -0.0503 -0.1698 -0.1490 850  HOH A O     
6263 O O     . HOH H .   ? 0.3911 0.2922 0.3302 -0.0933 -0.1119 0.1042  851  HOH A O     
6266 O O     . HOH H .   ? 0.1229 0.1901 0.2292 0.0451  -0.0798 -0.0305 852  HOH A O     
6269 O O     . HOH H .   ? 0.4838 0.3833 0.3118 -0.0800 -0.0061 -0.1082 853  HOH A O     
6272 O O     . HOH H .   ? 0.3990 0.1782 0.3224 -0.0591 -0.1611 0.0263  854  HOH A O     
6275 O O     . HOH H .   ? 0.3110 0.3091 0.3915 -0.0721 0.1163  -0.0087 855  HOH A O     
6278 O O     . HOH H .   ? 0.2413 0.1220 0.3210 -0.0181 -0.0893 0.0037  856  HOH A O     
6281 O O     . HOH H .   ? 0.4267 0.3045 0.5595 0.0475  0.0404  -0.0108 857  HOH A O     
6284 O O     . HOH H .   ? 0.2925 0.3057 0.5452 -0.0186 -0.1385 0.0845  858  HOH A O     
6287 O O     . HOH H .   ? 0.3637 0.2629 0.5800 -0.0087 -0.0090 -0.0757 859  HOH A O     
6290 O O     . HOH H .   ? 0.2025 0.1697 0.3532 0.0427  -0.1011 -0.0059 860  HOH A O     
6293 O O     . HOH H .   ? 0.7120 0.2010 0.5342 0.0761  -0.0823 0.0107  861  HOH A O     
6296 O O     . HOH H .   ? 0.3717 0.4249 0.5414 -0.1550 -0.2235 0.2290  862  HOH A O     
6299 O O     . HOH H .   ? 0.4133 0.2336 0.3700 0.0405  -0.0412 0.0632  863  HOH A O     
6302 O O     . HOH H .   ? 0.1647 0.1895 0.2936 0.0152  -0.1019 -0.0166 864  HOH A O     
6305 O O     . HOH H .   ? 0.2956 0.4852 0.3841 -0.1737 -0.1268 0.0654  865  HOH A O     
6308 O O     . HOH H .   ? 0.6099 0.5085 0.5472 0.1854  0.1286  0.1043  866  HOH A O     
6311 O O     . HOH H .   ? 0.2946 0.3969 0.5801 0.0651  -0.1404 0.0497  867  HOH A O     
6314 O O     . HOH H .   ? 0.3249 0.2117 0.4192 -0.0304 -0.0622 0.0165  868  HOH A O     
6317 O O     . HOH H .   ? 0.2373 0.1965 0.3662 -0.0842 -0.0957 -0.0243 869  HOH A O     
6320 O O     . HOH H .   ? 0.3192 0.2066 0.3867 -0.0731 -0.1961 0.0535  870  HOH A O     
6323 O O     . HOH H .   ? 0.5558 0.2824 0.4232 -0.0984 -0.0380 -0.0397 871  HOH A O     
6326 O O     . HOH H .   ? 0.3185 0.1721 0.3184 0.0005  -0.0123 -0.0084 872  HOH A O     
6329 O O     . HOH H .   ? 0.2632 0.2462 0.4484 0.0058  -0.1507 -0.0315 873  HOH A O     
6332 O O     . HOH H .   ? 0.2797 0.6349 0.5824 -0.0602 -0.0980 0.3267  874  HOH A O     
6335 O O     . HOH H .   ? 0.2013 0.2620 0.4331 -0.0032 -0.0633 0.0020  875  HOH A O     
6338 O O     . HOH H .   ? 0.3729 0.2914 0.5025 -0.0740 -0.2045 0.0454  876  HOH A O     
6341 O O     . HOH H .   ? 0.1354 0.1160 0.4375 0.0010  -0.0692 -0.0185 877  HOH A O     
6344 O O     . HOH H .   ? 0.4400 0.8996 0.7781 -0.1617 -0.0293 0.3695  878  HOH A O     
6347 O O     . HOH H .   ? 0.7205 0.2009 0.4065 0.0206  0.0157  0.0664  879  HOH A O     
6350 O O     . HOH H .   ? 0.4313 0.3503 0.3760 -0.0094 0.0768  -0.0187 880  HOH A O     
6353 O O     . HOH H .   ? 0.5022 0.1790 0.5012 0.0166  0.0779  -0.0982 881  HOH A O     
6356 O O     . HOH H .   ? 0.5114 0.2303 0.4799 -0.1024 -0.2015 0.0001  882  HOH A O     
6359 O O     . HOH H .   ? 0.4711 0.1827 0.2906 0.0640  -0.0872 0.0048  883  HOH A O     
6362 O O     . HOH H .   ? 0.3362 0.2701 0.6291 0.0012  -0.2221 0.0339  884  HOH A O     
6365 O O     . HOH H .   ? 0.4598 0.2498 0.5620 -0.0417 -0.2972 0.0660  885  HOH A O     
6368 O O     . HOH H .   ? 0.5768 0.3965 0.4089 -0.1288 -0.2117 0.1416  886  HOH A O     
6371 O O     . HOH H .   ? 0.6017 0.1815 0.2936 -0.0453 0.0685  -0.0582 887  HOH A O     
6374 O O     . HOH H .   ? 0.5852 0.4025 0.4580 0.0929  -0.2983 -0.0397 888  HOH A O     
6377 O O     . HOH H .   ? 0.2403 0.2763 0.7237 -0.0005 -0.0639 -0.1235 889  HOH A O     
6380 O O     . HOH H .   ? 0.3866 0.3441 0.5459 -0.0596 -0.2433 0.1498  890  HOH A O     
6383 O O     . HOH H .   ? 0.9175 0.2675 0.4364 -0.0909 0.2224  -0.0369 891  HOH A O     
6386 O O     . HOH H .   ? 0.1861 0.2338 0.4584 -0.0454 -0.1219 0.0215  892  HOH A O     
6389 O O     . HOH H .   ? 0.5359 0.4587 0.5883 0.2678  -0.1672 -0.1013 893  HOH A O     
6392 O O     . HOH H .   ? 0.2892 0.2691 0.7088 -0.0115 -0.1781 -0.0872 894  HOH A O     
6395 O O     . HOH H .   ? 0.1561 0.2464 0.4810 -0.0151 -0.0375 -0.0507 895  HOH A O     
6398 O O     . HOH H .   ? 0.5877 0.2583 0.7208 0.0731  -0.2443 0.0230  896  HOH A O     
6401 O O     . HOH H .   ? 0.2681 0.2676 1.0651 -0.0010 0.0037  0.0127  897  HOH A O     
6404 O O     . HOH H .   ? 0.2805 0.7072 0.4430 0.0738  -0.0723 0.1951  898  HOH A O     
6407 O O     . HOH H .   ? 0.3181 0.2294 0.3272 -0.0591 -0.0576 0.0734  899  HOH A O     
6410 O O     . HOH H .   ? 0.4252 0.2048 0.5283 0.0836  0.1898  0.0809  900  HOH A O     
6413 O O     . HOH H .   ? 0.3821 0.2831 0.3551 0.0098  -0.1477 0.0365  901  HOH A O     
6416 O O     . HOH H .   ? 0.6353 0.4082 0.7318 -0.1842 -0.1652 0.0318  902  HOH A O     
6419 O O     . HOH H .   ? 0.6438 0.5808 0.5679 -0.1149 -0.0323 0.0337  903  HOH A O     
6422 O O     . HOH H .   ? 0.6194 0.3404 0.6652 -0.1560 -0.3650 0.1568  904  HOH A O     
6425 O O     . HOH H .   ? 0.2817 0.3969 0.4859 0.0628  0.0050  0.0921  905  HOH A O     
6428 O O     . HOH H .   ? 0.6217 0.6241 0.6233 -0.0009 0.0002  0.0019  906  HOH A O     
6431 O O     . HOH H .   ? 0.5070 0.4127 0.9887 0.0233  0.1532  0.2151  907  HOH A O     
6434 O O     . HOH H .   ? 0.2439 0.1231 0.3707 0.0287  -0.0899 -0.0371 908  HOH A O     
6437 O O     . HOH H .   ? 0.2465 0.2981 0.3914 -0.0258 -0.0811 0.1450  909  HOH A O     
6440 O O     . HOH H .   ? 0.5194 0.3957 0.5130 -0.2457 -0.1408 0.1086  910  HOH A O     
6443 O O     . HOH H .   ? 0.2238 0.2036 0.4814 -0.0268 -0.1650 0.0539  911  HOH A O     
6446 O O     . HOH H .   ? 0.2853 0.2871 0.4021 -0.1167 0.0042  -0.0279 912  HOH A O     
6449 O O     . HOH H .   ? 0.1638 0.5544 0.4232 0.0462  -0.0429 -0.0619 913  HOH A O     
6452 O O     . HOH H .   ? 0.1406 0.1787 0.3684 -0.0001 -0.0627 -0.0113 914  HOH A O     
6455 O O     . HOH H .   ? 0.5080 0.4273 0.5565 0.1493  0.0437  -0.0190 915  HOH A O     
6458 O O     . HOH H .   ? 0.3633 0.1716 0.2970 0.0167  -0.0777 0.0340  916  HOH A O     
6461 O O     . HOH H .   ? 0.3219 0.1291 0.2964 -0.0441 -0.1583 0.0342  917  HOH A O     
6464 O O     . HOH H .   ? 0.2553 0.2147 0.5100 -0.0650 -0.0323 -0.0565 918  HOH A O     
6467 O O     . HOH H .   ? 0.7304 0.2760 0.5112 -0.0763 -0.2289 0.0264  919  HOH A O     
6470 O O     . HOH H .   ? 0.4935 0.2747 0.4421 0.1277  0.1066  0.0571  920  HOH A O     
6473 O O     . HOH H .   ? 0.3111 0.2921 0.9746 0.0381  0.0389  0.1335  921  HOH A O     
6476 O O     . HOH H .   ? 0.3821 0.5438 0.2493 0.0735  0.0374  0.1188  922  HOH A O     
6479 O O     . HOH H .   ? 0.2877 0.7122 0.7524 0.1942  0.0820  -0.0380 923  HOH A O     
6482 O O     . HOH H .   ? 0.2684 0.2166 0.4996 -0.0574 -0.0605 -0.0102 924  HOH A O     
6485 O O     . HOH H .   ? 0.3659 0.3356 0.4430 0.0159  -0.0794 0.1228  925  HOH A O     
6488 O O     . HOH H .   ? 0.3246 0.8883 0.5859 0.1418  0.0517  0.3396  926  HOH A O     
6491 O O     . HOH H .   ? 0.2315 0.3588 0.6769 0.0650  -0.1312 -0.0967 927  HOH A O     
6494 O O     . HOH H .   ? 0.4721 0.1644 0.3427 0.0346  -0.1227 -0.0243 928  HOH A O     
6497 O O     . HOH H .   ? 0.1701 0.4758 0.4721 0.0509  -0.0488 -0.1468 929  HOH A O     
6500 O O     . HOH H .   ? 0.1928 0.1268 0.3309 -0.0350 -0.0496 -0.0018 930  HOH A O     
6503 O O     . HOH H .   ? 0.1595 0.1423 0.2811 0.0269  -0.1044 -0.0394 931  HOH A O     
6506 O O     . HOH H .   ? 0.3540 0.2588 0.3766 -0.0040 -0.1230 0.0463  932  HOH A O     
6509 O O     . HOH H .   ? 0.5851 0.3003 0.7681 -0.0023 0.1671  -0.0392 933  HOH A O     
6512 O O     . HOH H .   ? 0.7192 0.3835 0.6578 0.0446  0.0337  0.1436  934  HOH A O     
6515 O O     . HOH H .   ? 0.6234 0.4916 0.5524 0.0012  -0.3395 -0.0024 935  HOH A O     
6518 O O     . HOH H .   ? 0.9192 0.2605 0.4688 0.0619  0.1684  0.0551  936  HOH A O     
6521 O O     . HOH H .   ? 0.7978 0.2756 0.6950 -0.0243 -0.2075 0.0387  937  HOH A O     
6524 O O     . HOH H .   ? 0.1990 0.2743 0.6675 0.0439  -0.0811 -0.0688 938  HOH A O     
6527 O O     . HOH H .   ? 0.6993 0.4707 0.5931 -0.1617 0.0460  -0.2257 939  HOH A O     
6530 O O     . HOH H .   ? 0.1310 0.3158 0.4417 -0.0406 -0.0486 0.0013  940  HOH A O     
6533 O O     . HOH H .   ? 0.4104 0.2262 0.3721 -0.0250 -0.1935 -0.0614 941  HOH A O     
6536 O O     . HOH H .   ? 0.4571 0.4535 0.4573 -0.0002 -0.0034 0.0005  942  HOH A O     
6539 O O     . HOH H .   ? 0.3315 0.4432 0.2741 -0.1310 -0.0725 -0.0381 943  HOH A O     
6542 O O     . HOH H .   ? 0.3861 0.4237 0.6502 -0.1304 -0.0461 0.0292  944  HOH A O     
6545 O O     . HOH H .   ? 0.3768 0.3073 0.4969 0.0277  -0.0381 0.0246  945  HOH A O     
6548 O O     . HOH H .   ? 0.3931 0.3066 0.4775 0.0110  0.0005  -0.0103 946  HOH A O     
6551 O O     . HOH H .   ? 0.3086 0.2571 0.5161 0.0178  -0.0836 -0.0993 947  HOH A O     
6554 O O     . HOH H .   ? 0.4423 0.3010 0.3200 -0.0775 0.0646  -0.0058 948  HOH A O     
6557 O O     . HOH H .   ? 0.1989 0.2673 0.4249 0.0290  -0.0341 -0.0613 949  HOH A O     
6560 O O     . HOH H .   ? 0.2716 0.2853 0.4473 0.0394  -0.1426 -0.0857 950  HOH A O     
6563 O O     . HOH H .   ? 0.2264 0.7147 0.4133 0.0342  -0.0561 0.1637  951  HOH A O     
6566 O O     . HOH H .   ? 0.3105 0.6584 0.3898 -0.1348 -0.0733 0.1290  952  HOH A O     
6569 O O     . HOH H .   ? 0.5517 1.0570 0.4726 0.1843  -0.0931 0.2209  953  HOH A O     
6572 O O     . HOH H .   ? 0.2072 0.1489 0.3374 -0.0568 -0.1228 0.0414  954  HOH A O     
6575 O O     . HOH H .   ? 0.2090 0.1964 0.3812 -0.0350 -0.0878 -0.0211 955  HOH A O     
6578 O O     . HOH H .   ? 0.2947 0.6335 0.7013 0.0974  -0.1556 -0.2448 956  HOH A O     
6581 O O     . HOH H .   ? 0.3519 0.1939 0.2386 0.0287  0.0034  0.0127  957  HOH A O     
6584 O O     . HOH H .   ? 0.3752 0.3371 0.6001 0.0820  -0.1863 -0.0214 958  HOH A O     
6587 O O     . HOH H .   ? 0.7072 0.3114 0.6126 0.0506  -0.0233 -0.0857 959  HOH A O     
6590 O O     . HOH H .   ? 0.4478 0.4511 0.4572 -0.0054 -0.0030 -0.0020 960  HOH A O     
6593 O O     . HOH H .   ? 0.4604 0.7187 0.7695 -0.1537 0.1087  0.0379  961  HOH A O     
6596 O O     . HOH H .   ? 0.2241 0.1796 0.4676 -0.0142 -0.1671 0.0274  962  HOH A O     
6599 O O     . HOH H .   ? 0.3480 0.2187 0.4882 -0.0062 0.0832  0.0399  963  HOH A O     
6602 O O     . HOH H .   ? 0.6358 0.5246 0.5345 -0.1039 -0.2853 0.0046  964  HOH A O     
6605 O O     . HOH H .   ? 0.4784 0.3260 0.5349 -0.0058 -0.1237 -0.0777 965  HOH A O     
6608 O O     . HOH H .   ? 0.3793 0.2459 0.4410 0.0010  -0.0568 -0.0629 966  HOH A O     
6611 O O     . HOH H .   ? 0.8480 0.3036 0.5145 -0.0213 -0.2914 0.0294  967  HOH A O     
6614 O O     . HOH H .   ? 0.1726 0.2940 0.3865 -0.0283 -0.1234 -0.0126 968  HOH A O     
6617 O O     . HOH H .   ? 0.7036 0.5608 0.4058 0.0977  -0.0120 -0.0209 969  HOH A O     
6620 O O     . HOH H .   ? 0.4980 0.7471 0.9116 0.2323  -0.1914 0.1789  970  HOH A O     
6623 O O     . HOH H .   ? 0.2230 0.5136 0.4725 -0.0040 -0.0254 0.2685  971  HOH A O     
6626 O O     . HOH H .   ? 0.5743 0.3314 0.7179 -0.2141 0.0545  0.0378  972  HOH A O     
6629 O O     . HOH H .   ? 0.4835 0.2666 0.4226 0.0985  -0.1490 -0.1556 973  HOH A O     
6632 O O     . HOH H .   ? 0.3777 0.2612 0.5036 0.0382  -0.1184 -0.0080 974  HOH A O     
6635 O O     . HOH H .   ? 0.5208 0.5079 0.5140 -0.0189 -0.1732 -0.0960 975  HOH A O     
6638 O O     . HOH H .   ? 0.6980 0.2856 0.7189 -0.0731 -0.1034 0.0457  976  HOH A O     
6641 O O     . HOH H .   ? 0.6186 0.2595 0.6391 -0.0662 -0.2741 -0.0234 977  HOH A O     
6644 O O     . HOH H .   ? 0.7084 0.7087 0.7081 -0.0009 -0.0002 -0.0004 978  HOH A O     
6647 O O     . HOH H .   ? 0.4219 0.3643 0.4107 -0.1319 -0.0429 -0.0307 979  HOH A O     
6650 O O     . HOH H .   ? 0.8125 0.2593 0.8435 0.1587  0.0093  -0.0419 980  HOH A O     
6653 O O     . HOH H .   ? 0.4020 0.2563 0.4468 0.0300  -0.0940 -0.1008 981  HOH A O     
6656 O O     . HOH H .   ? 0.6048 0.4257 0.4040 -0.1179 -0.1990 0.0185  982  HOH A O     
6659 O O     . HOH H .   ? 0.6877 0.4735 0.3127 -0.0431 -0.1192 0.0325  983  HOH A O     
6662 O O     . HOH H .   ? 0.4222 0.5388 0.5563 0.1097  0.0365  -0.0258 984  HOH A O     
6665 O O     . HOH H .   ? 0.5351 0.4256 0.5026 0.0619  -0.2831 -0.0708 985  HOH A O     
6668 O O     . HOH H .   ? 0.5147 0.3214 0.6122 -0.0092 -0.1354 -0.2101 986  HOH A O     
6671 O O     . HOH H .   ? 0.4956 0.4606 0.7876 0.1148  0.0644  0.2023  987  HOH A O     
6674 O O     . HOH H .   ? 0.4265 0.4942 0.9227 -0.0575 -0.1912 0.2448  988  HOH A O     
6677 O O     . HOH H .   ? 0.4742 0.4399 0.6985 0.0449  0.0853  -0.2047 989  HOH A O     
6680 O O     . HOH H .   ? 0.6386 0.5860 0.6183 0.0098  -0.0224 -0.1242 990  HOH A O     
6683 O O     . HOH H .   ? 0.3040 0.2954 0.4594 0.0617  -0.0777 -0.0639 991  HOH A O     
6686 O O     . HOH H .   ? 0.3781 0.2651 0.4058 0.0921  -0.1925 -0.0863 992  HOH A O     
6689 O O     . HOH H .   ? 0.3231 0.3477 0.7321 -0.0123 0.0051  0.1785  993  HOH A O     
6692 O O     . HOH H .   ? 0.2953 0.6672 0.6336 0.0372  -0.0419 0.1185  994  HOH A O     
6695 O O     . HOH H .   ? 0.4206 0.2958 0.6777 0.0764  -0.1282 -0.0805 995  HOH A O     
6698 O O     . HOH H .   ? 0.5271 0.4182 0.9631 -0.0710 -0.3630 0.0045  996  HOH A O     
6701 O O     . HOH H .   ? 0.4985 0.3928 0.9251 -0.0818 -0.1661 -0.1907 997  HOH A O     
6704 O O     . HOH H .   ? 0.4146 1.0140 0.4922 -0.1498 0.0014  0.0038  998  HOH A O     
6707 O O     . HOH H .   ? 0.5005 0.5476 0.7414 0.0706  0.0182  -0.1584 999  HOH A O     
6710 O O     . HOH H .   ? 0.8338 0.5049 0.4579 -0.3356 -0.1553 0.0197  1000 HOH A O     
6713 O O     . HOH H .   ? 0.7064 0.2714 0.7703 0.0524  -0.0551 0.0438  1001 HOH A O     
6716 O O     . HOH H .   ? 0.6509 0.4780 0.4748 -0.0359 -0.2914 -0.1012 1002 HOH A O     
6719 O O     . HOH H .   ? 0.4431 0.3500 0.6463 0.0291  0.0060  -0.1331 1003 HOH A O     
6722 O O     . HOH H .   ? 0.5439 0.5862 0.5227 0.3047  -0.1885 -0.1188 1004 HOH A O     
6725 O O     . HOH H .   ? 0.5943 0.2910 0.3856 0.1171  -0.0457 0.0442  1005 HOH A O     
6728 O O     . HOH H .   ? 0.6651 0.3878 0.8217 0.0362  0.2216  -0.0774 1006 HOH A O     
6731 O O     . HOH H .   ? 0.2724 0.2005 0.4748 -0.0340 -0.1275 0.0597  1007 HOH A O     
6734 O O     . HOH H .   ? 0.5219 0.3106 0.4398 -0.0067 -0.0271 -0.0371 1008 HOH A O     
6737 O O     . HOH H .   ? 0.1239 0.2193 0.3125 -0.0072 -0.0600 0.0070  1009 HOH A O     
6740 O O     . HOH H .   ? 0.3986 0.5167 0.4293 0.2455  -0.0293 0.0677  1010 HOH A O     
6743 O O     . HOH H .   ? 0.5338 0.2400 0.4498 -0.1027 -0.0806 0.0566  1011 HOH A O     
6746 O O     . HOH H .   ? 0.6286 0.6276 0.6281 0.0003  -0.0001 -0.0003 1012 HOH A O     
6749 O O     . HOH H .   ? 0.2313 0.6173 0.6753 -0.0636 0.0412  0.1139  1013 HOH A O     
6752 O O     . HOH H .   ? 0.5213 0.5247 0.5239 -0.0018 -0.0036 -0.0028 1014 HOH A O     
6755 O O     . HOH H .   ? 0.2182 0.2641 0.3292 0.0165  -0.0714 0.0404  1015 HOH A O     
6758 O O     . HOH H .   ? 0.3434 0.6123 0.8345 -0.1518 -0.1441 -0.1106 1016 HOH A O     
6761 O O     . HOH H .   ? 0.3678 0.2701 0.5380 -0.0860 -0.1161 0.1108  1017 HOH A O     
6764 O O     . HOH H .   ? 0.3595 0.3965 0.3832 -0.1042 -0.0047 0.0142  1018 HOH A O     
6767 O O     . HOH H .   ? 0.3071 0.1954 0.6466 0.0154  -0.0132 -0.0694 1019 HOH A O     
6770 O O     . HOH H .   ? 0.5273 0.3926 0.8497 -0.1399 0.0058  0.0653  1020 HOH A O     
6773 O O     . HOH H .   ? 0.6526 0.2814 0.4293 -0.1306 -0.2651 0.0459  1021 HOH A O     
6776 O O     . HOH H .   ? 0.4546 0.3531 0.3348 -0.0379 -0.1513 -0.0083 1022 HOH A O     
6779 O O     . HOH H .   ? 0.3340 0.5144 0.4147 0.0840  -0.1614 -0.1613 1023 HOH A O     
6782 O O     . HOH H .   ? 0.6792 0.7789 0.6566 -0.0815 -0.0717 -0.0198 1024 HOH A O     
6785 O O     . HOH H .   ? 0.4077 0.1860 0.6014 -0.0314 0.0116  -0.0357 1025 HOH A O     
6788 O O     . HOH H .   ? 0.3547 0.5828 0.4474 0.0737  -0.0391 0.0540  1026 HOH A O     
6791 O O     . HOH H .   ? 0.3192 0.5126 0.9619 0.1246  0.1139  0.0360  1027 HOH A O     
6794 O O     . HOH H .   ? 0.8701 0.4644 0.5895 0.1914  -0.3457 -0.1332 1028 HOH A O     
6797 O O     . HOH H .   ? 0.5695 0.5370 0.6816 0.1939  -0.2237 0.0803  1029 HOH A O     
6800 O O     . HOH H .   ? 0.6843 0.4285 0.5905 0.0008  -0.2945 -0.0239 1030 HOH A O     
6803 O O     . HOH H .   ? 0.5879 0.3993 0.3713 -0.2382 -0.1221 0.1501  1031 HOH A O     
6806 O O     . HOH H .   ? 0.5394 0.4134 0.8166 0.0043  -0.3096 -0.1797 1032 HOH A O     
6809 O O     . HOH H .   ? 0.5420 0.3570 0.7431 -0.1839 0.2232  -0.1177 1033 HOH A O     
6812 O O     . HOH H .   ? 0.2947 0.5831 0.8184 0.1013  0.0733  0.3020  1034 HOH A O     
6815 O O     . HOH H .   ? 0.4532 0.4831 0.9542 -0.1552 0.0824  -0.2785 1035 HOH A O     
6818 O O     . HOH H .   ? 0.4981 0.5122 0.4207 0.0297  0.0088  0.0088  1036 HOH A O     
6821 O O     . HOH H .   ? 0.4742 0.3185 0.5272 -0.0932 -0.2009 0.1246  1037 HOH A O     
6824 O O     . HOH H .   ? 0.2891 0.4418 0.5701 -0.0549 -0.0287 0.0825  1038 HOH A O     
6827 O O     . HOH H .   ? 0.2731 0.7781 0.6356 -0.1158 -0.0136 -0.0429 1039 HOH A O     
6830 O O     . HOH H .   ? 0.2464 0.2416 0.4318 -0.0423 -0.0774 0.0679  1040 HOH A O     
6833 O O     . HOH H .   ? 0.5580 0.2955 0.7893 -0.0707 -0.1040 0.0455  1041 HOH A O     
6836 O O     . HOH H .   ? 0.6277 0.7169 0.6601 0.3172  -0.0691 0.1264  1042 HOH A O     
6839 O O     . HOH H .   ? 0.5473 0.2622 0.5190 -0.0944 -0.1832 0.1398  1043 HOH A O     
6842 O O     . HOH H .   ? 0.6190 0.5486 0.7034 0.0891  -0.3233 0.1418  1044 HOH A O     
6845 O O     . HOH H .   ? 0.2484 0.5870 0.2960 -0.0124 -0.0736 0.0325  1045 HOH A O     
6848 O O     . HOH H .   ? 0.4435 0.5090 0.6397 0.0280  -0.1587 0.0264  1046 HOH A O     
6851 O O     . HOH H .   ? 0.6479 0.8424 0.4023 -0.0131 -0.1440 -0.0309 1047 HOH A O     
6854 O O     . HOH H .   ? 0.2487 0.2283 0.3781 -0.0397 -0.0913 0.0645  1048 HOH A O     
6857 O O     . HOH H .   ? 0.3817 0.2967 0.4760 0.0304  -0.1004 0.0557  1049 HOH A O     
6860 O O     . HOH H .   ? 0.7181 0.4898 0.4450 -0.0591 -0.2162 0.0064  1050 HOH A O     
6863 O O     . HOH H .   ? 0.5649 0.6000 0.3990 0.0295  -0.1557 -0.0635 1051 HOH A O     
6866 O O     . HOH H .   ? 0.5419 0.3041 0.9106 -0.0716 -0.1576 0.0819  1052 HOH A O     
6869 O O     . HOH H .   ? 0.4011 0.6331 0.5788 -0.1459 0.0618  0.1142  1053 HOH A O     
6872 O O     . HOH H .   ? 0.5598 0.5953 0.5708 0.0442  -0.0144 0.0987  1054 HOH A O     
6875 O O     . HOH H .   ? 0.5520 0.3647 0.3744 0.0552  -0.2177 -0.0581 1055 HOH A O     
6878 O O     . HOH H .   ? 0.5246 0.2787 0.7871 -0.0946 0.0956  -0.1585 1056 HOH A O     
6881 O O     . HOH H .   ? 0.4095 0.4597 0.5055 -0.1699 -0.1898 -0.0380 1057 HOH A O     
6884 O O     . HOH H .   ? 0.3449 0.3342 0.4195 0.1589  -0.1313 -0.0117 1058 HOH A O     
6887 O O     . HOH H .   ? 0.3213 0.3574 0.6755 0.0574  -0.2280 -0.0213 1059 HOH A O     
6890 O O     . HOH H .   ? 0.4586 0.5014 0.5043 -0.1003 -0.1596 -0.0490 1060 HOH A O     
6893 O O     . HOH H .   ? 0.4566 0.3877 0.7100 -0.0130 -0.3247 0.0314  1061 HOH A O     
6896 O O     . HOH H .   ? 0.2662 0.4636 0.5132 0.1189  -0.0931 0.1003  1062 HOH A O     
6899 O O     . HOH H .   ? 0.4258 0.6132 0.4283 0.0506  -0.0022 0.1301  1063 HOH A O     
6902 O O     . HOH H .   ? 0.6320 0.6329 0.6328 0.0019  0.0011  0.0003  1064 HOH A O     
6905 O O     . HOH H .   ? 0.4755 0.5155 0.5008 0.0338  -0.2467 -0.0771 1065 HOH A O     
6908 O O     . HOH H .   ? 0.3607 0.4349 0.5600 -0.0732 -0.1299 0.0410  1066 HOH A O     
6911 O O     . HOH H .   ? 0.5391 0.5529 0.4567 -0.0546 -0.1071 -0.0314 1067 HOH A O     
6914 O O     . HOH H .   ? 0.2137 0.6336 0.4593 0.0644  -0.0939 -0.1291 1068 HOH A O     
6917 O O     . HOH H .   ? 0.3350 0.4991 0.6840 0.0802  0.0777  0.3240  1069 HOH A O     
6920 O O     . HOH H .   ? 0.6044 0.5133 0.3830 -0.1292 -0.0057 -0.0029 1070 HOH A O     
6923 O O     . HOH H .   ? 0.5693 0.3025 0.4989 0.0529  -0.1212 -0.1146 1071 HOH A O     
# 
