data_9DAS
# 
_entry.id   9DAS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9DAS         pdb_00009das 10.2210/pdb9das/pdb 
WWPDB D_1000287341 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DAS 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9CSE is from the same protein.' 
_pdbx_database_related.db_id          9CSE 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              daviesp@queensu.ca 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Davies 
_pdbx_contact_author.name_mi            L. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8026-7818 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vance, T.D.R.' 1 0000-0002-7637-5891 
'Ye, Q.'        2 0000-0002-5757-9514 
'Davies, P.L.'  3 0000-0002-8026-7818 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Mbio 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2150-7511 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                e0315824 
_citation.page_last                 e0315824 
_citation.title                     
;Aeromonas hydrophila RTX adhesin has three ligand-binding domains that give the bacterium the potential to adhere to and aggregate a wide variety of cell types.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1128/mbio.03158-24 
_citation.pdbx_database_id_PubMed   40243363 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ye, Q.'          1  0000-0002-5757-9514 
primary 'Eves, R.'        2  0000-0003-0377-1073 
primary 'Vance, T.D.R.'   3  0000-0002-7637-5891 
primary 'Hansen, T.'      4  0000-0001-7515-9540 
primary 'Sage, A.P.'      5  0000-0002-4519-6970 
primary 'Petkovic, A.'    6  0000-0002-1769-4008 
primary 'Bradley, B.'     7  0009-0000-2970-0826 
primary 'Escobedo, C.'    8  0000-0002-7832-166X 
primary 'Graham, L.A.'    9  0000-0001-7478-1557 
primary 'Allingham, J.S.' 10 0000-0002-0918-3152 
primary 'Davies, P.L.'    11 0000-0002-8026-7818 
# 
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 'Flagellin hook IN motif family' 31514.334 2   ? ? ? ? 
2 non-polymer syn 'CALCIUM ION'                    40.078    12  ? ? ? ? 
3 non-polymer syn GLYCEROL                         92.094    1   ? ? ? ? 
4 water       nat water                            18.015    262 ? ? ? ? 
# 
_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       
;MASSHHHHHHSSGLVPRGSHMPGQNYNIAFMVDSSGSIGSSAMNTIKSQLAQVFSSLKASAGTDGAGTVNIFLVDFDTLA
NKSVSVNLKDSNALSQLQAILDSMDGSTNSGGGTNYEDVFKTTANWFNSSTVQGNTNAKNLTYFITDGQPTFYLENEGSD
PMIRDRSGTVNDVYLSNVIGTSYTYGQTYSVNGRTVVNGNGVVYDYNGNQIGYMRPDGAGRYVYATLAGTGNSTSSTTIA
NSVAGFGLLTGMGVTVEAIGLGANISYNDLKSYDSDGVIMTGVNASDLANAILGTSVNNLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASSHHHHHHSSGLVPRGSHMPGQNYNIAFMVDSSGSIGSSAMNTIKSQLAQVFSSLKASAGTDGAGTVNIFLVDFDTLA
NKSVSVNLKDSNALSQLQAILDSMDGSTNSGGGTNYEDVFKTTANWFNSSTVQGNTNAKNLTYFITDGQPTFYLENEGSD
PMIRDRSGTVNDVYLSNVIGTSYTYGQTYSVNGRTVVNGNGVVYDYNGNQIGYMRPDGAGRYVYATLAGTGNSTSSTTIA
NSVAGFGLLTGMGVTVEAIGLGANISYNDLKSYDSDGVIMTGVNASDLANAILGTSVNNLP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CALCIUM ION' CA  
3 GLYCEROL      GOL 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  PRO n 
1 23  GLY n 
1 24  GLN n 
1 25  ASN n 
1 26  TYR n 
1 27  ASN n 
1 28  ILE n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  VAL n 
1 33  ASP n 
1 34  SER n 
1 35  SER n 
1 36  GLY n 
1 37  SER n 
1 38  ILE n 
1 39  GLY n 
1 40  SER n 
1 41  SER n 
1 42  ALA n 
1 43  MET n 
1 44  ASN n 
1 45  THR n 
1 46  ILE n 
1 47  LYS n 
1 48  SER n 
1 49  GLN n 
1 50  LEU n 
1 51  ALA n 
1 52  GLN n 
1 53  VAL n 
1 54  PHE n 
1 55  SER n 
1 56  SER n 
1 57  LEU n 
1 58  LYS n 
1 59  ALA n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  THR n 
1 64  ASP n 
1 65  GLY n 
1 66  ALA n 
1 67  GLY n 
1 68  THR n 
1 69  VAL n 
1 70  ASN n 
1 71  ILE n 
1 72  PHE n 
1 73  LEU n 
1 74  VAL n 
1 75  ASP n 
1 76  PHE n 
1 77  ASP n 
1 78  THR n 
1 79  LEU n 
1 80  ALA n 
1 81  ASN n 
1 82  LYS n 
1 83  SER n 
1 84  VAL n 
1 85  SER n 
1 86  VAL n 
1 87  ASN n 
1 88  LEU n 
1 89  LYS n 
1 90  ASP n 
1 91  SER n 
1 92  ASN n 
1 93  ALA n 
1 94  LEU n 
1 95  SER n 
1 96  GLN n 
1 97  LEU n 
1 98  GLN n 
1 99  ALA n 
1 100 ILE n 
1 101 LEU n 
1 102 ASP n 
1 103 SER n 
1 104 MET n 
1 105 ASP n 
1 106 GLY n 
1 107 SER n 
1 108 THR n 
1 109 ASN n 
1 110 SER n 
1 111 GLY n 
1 112 GLY n 
1 113 GLY n 
1 114 THR n 
1 115 ASN n 
1 116 TYR n 
1 117 GLU n 
1 118 ASP n 
1 119 VAL n 
1 120 PHE n 
1 121 LYS n 
1 122 THR n 
1 123 THR n 
1 124 ALA n 
1 125 ASN n 
1 126 TRP n 
1 127 PHE n 
1 128 ASN n 
1 129 SER n 
1 130 SER n 
1 131 THR n 
1 132 VAL n 
1 133 GLN n 
1 134 GLY n 
1 135 ASN n 
1 136 THR n 
1 137 ASN n 
1 138 ALA n 
1 139 LYS n 
1 140 ASN n 
1 141 LEU n 
1 142 THR n 
1 143 TYR n 
1 144 PHE n 
1 145 ILE n 
1 146 THR n 
1 147 ASP n 
1 148 GLY n 
1 149 GLN n 
1 150 PRO n 
1 151 THR n 
1 152 PHE n 
1 153 TYR n 
1 154 LEU n 
1 155 GLU n 
1 156 ASN n 
1 157 GLU n 
1 158 GLY n 
1 159 SER n 
1 160 ASP n 
1 161 PRO n 
1 162 MET n 
1 163 ILE n 
1 164 ARG n 
1 165 ASP n 
1 166 ARG n 
1 167 SER n 
1 168 GLY n 
1 169 THR n 
1 170 VAL n 
1 171 ASN n 
1 172 ASP n 
1 173 VAL n 
1 174 TYR n 
1 175 LEU n 
1 176 SER n 
1 177 ASN n 
1 178 VAL n 
1 179 ILE n 
1 180 GLY n 
1 181 THR n 
1 182 SER n 
1 183 TYR n 
1 184 THR n 
1 185 TYR n 
1 186 GLY n 
1 187 GLN n 
1 188 THR n 
1 189 TYR n 
1 190 SER n 
1 191 VAL n 
1 192 ASN n 
1 193 GLY n 
1 194 ARG n 
1 195 THR n 
1 196 VAL n 
1 197 VAL n 
1 198 ASN n 
1 199 GLY n 
1 200 ASN n 
1 201 GLY n 
1 202 VAL n 
1 203 VAL n 
1 204 TYR n 
1 205 ASP n 
1 206 TYR n 
1 207 ASN n 
1 208 GLY n 
1 209 ASN n 
1 210 GLN n 
1 211 ILE n 
1 212 GLY n 
1 213 TYR n 
1 214 MET n 
1 215 ARG n 
1 216 PRO n 
1 217 ASP n 
1 218 GLY n 
1 219 ALA n 
1 220 GLY n 
1 221 ARG n 
1 222 TYR n 
1 223 VAL n 
1 224 TYR n 
1 225 ALA n 
1 226 THR n 
1 227 LEU n 
1 228 ALA n 
1 229 GLY n 
1 230 THR n 
1 231 GLY n 
1 232 ASN n 
1 233 SER n 
1 234 THR n 
1 235 SER n 
1 236 SER n 
1 237 THR n 
1 238 THR n 
1 239 ILE n 
1 240 ALA n 
1 241 ASN n 
1 242 SER n 
1 243 VAL n 
1 244 ALA n 
1 245 GLY n 
1 246 PHE n 
1 247 GLY n 
1 248 LEU n 
1 249 LEU n 
1 250 THR n 
1 251 GLY n 
1 252 MET n 
1 253 GLY n 
1 254 VAL n 
1 255 THR n 
1 256 VAL n 
1 257 GLU n 
1 258 ALA n 
1 259 ILE n 
1 260 GLY n 
1 261 LEU n 
1 262 GLY n 
1 263 ALA n 
1 264 ASN n 
1 265 ILE n 
1 266 SER n 
1 267 TYR n 
1 268 ASN n 
1 269 ASP n 
1 270 LEU n 
1 271 LYS n 
1 272 SER n 
1 273 TYR n 
1 274 ASP n 
1 275 SER n 
1 276 ASP n 
1 277 GLY n 
1 278 VAL n 
1 279 ILE n 
1 280 MET n 
1 281 THR n 
1 282 GLY n 
1 283 VAL n 
1 284 ASN n 
1 285 ALA n 
1 286 SER n 
1 287 ASP n 
1 288 LEU n 
1 289 ALA n 
1 290 ASN n 
1 291 ALA n 
1 292 ILE n 
1 293 LEU n 
1 294 GLY n 
1 295 THR n 
1 296 SER n 
1 297 VAL n 
1 298 ASN n 
1 299 ASN n 
1 300 LEU n 
1 301 PRO 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                   301 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 AHA_3491 
_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      'Aeromonas hydrophila' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     644 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 7966 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET-28a 
_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 
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 
CA  non-polymer         . 'CALCIUM ION'   ?                               'Ca 2'           40.078  
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
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   MET 1   4476 ?    ?   ?   A . n 
A 1 2   ALA 2   4477 ?    ?   ?   A . n 
A 1 3   SER 3   4478 ?    ?   ?   A . n 
A 1 4   SER 4   4479 ?    ?   ?   A . n 
A 1 5   HIS 5   4480 ?    ?   ?   A . n 
A 1 6   HIS 6   4481 ?    ?   ?   A . n 
A 1 7   HIS 7   4482 ?    ?   ?   A . n 
A 1 8   HIS 8   4483 ?    ?   ?   A . n 
A 1 9   HIS 9   4484 ?    ?   ?   A . n 
A 1 10  HIS 10  4485 ?    ?   ?   A . n 
A 1 11  SER 11  4486 ?    ?   ?   A . n 
A 1 12  SER 12  4487 ?    ?   ?   A . n 
A 1 13  GLY 13  4488 ?    ?   ?   A . n 
A 1 14  LEU 14  4489 ?    ?   ?   A . n 
A 1 15  VAL 15  4490 ?    ?   ?   A . n 
A 1 16  PRO 16  4491 ?    ?   ?   A . n 
A 1 17  ARG 17  4492 ?    ?   ?   A . n 
A 1 18  GLY 18  4493 ?    ?   ?   A . n 
A 1 19  SER 19  4494 ?    ?   ?   A . n 
A 1 20  HIS 20  4495 ?    ?   ?   A . n 
A 1 21  MET 21  4496 ?    ?   ?   A . n 
A 1 22  PRO 22  4497 ?    ?   ?   A . n 
A 1 23  GLY 23  4498 4498 GLY GLY A . n 
A 1 24  GLN 24  4499 4499 GLN GLN A . n 
A 1 25  ASN 25  4500 4500 ASN ASN A . n 
A 1 26  TYR 26  4501 4501 TYR TYR A . n 
A 1 27  ASN 27  4502 4502 ASN ASN A . n 
A 1 28  ILE 28  4503 4503 ILE ILE A . n 
A 1 29  ALA 29  4504 4504 ALA ALA A . n 
A 1 30  PHE 30  4505 4505 PHE PHE A . n 
A 1 31  MET 31  4506 4506 MET MET A . n 
A 1 32  VAL 32  4507 4507 VAL VAL A . n 
A 1 33  ASP 33  4508 4508 ASP ASP A . n 
A 1 34  SER 34  4509 4509 SER SER A . n 
A 1 35  SER 35  4510 4510 SER SER A . n 
A 1 36  GLY 36  4511 4511 GLY GLY A . n 
A 1 37  SER 37  4512 4512 SER SER A . n 
A 1 38  ILE 38  4513 4513 ILE ILE A . n 
A 1 39  GLY 39  4514 4514 GLY GLY A . n 
A 1 40  SER 40  4515 4515 SER SER A . n 
A 1 41  SER 41  4516 4516 SER SER A . n 
A 1 42  ALA 42  4517 4517 ALA ALA A . n 
A 1 43  MET 43  4518 4518 MET MET A . n 
A 1 44  ASN 44  4519 4519 ASN ASN A . n 
A 1 45  THR 45  4520 4520 THR THR A . n 
A 1 46  ILE 46  4521 4521 ILE ILE A . n 
A 1 47  LYS 47  4522 4522 LYS LYS A . n 
A 1 48  SER 48  4523 4523 SER SER A . n 
A 1 49  GLN 49  4524 4524 GLN GLN A . n 
A 1 50  LEU 50  4525 4525 LEU LEU A . n 
A 1 51  ALA 51  4526 4526 ALA ALA A . n 
A 1 52  GLN 52  4527 4527 GLN GLN A . n 
A 1 53  VAL 53  4528 4528 VAL VAL A . n 
A 1 54  PHE 54  4529 4529 PHE PHE A . n 
A 1 55  SER 55  4530 4530 SER SER A . n 
A 1 56  SER 56  4531 4531 SER SER A . n 
A 1 57  LEU 57  4532 4532 LEU LEU A . n 
A 1 58  LYS 58  4533 4533 LYS LYS A . n 
A 1 59  ALA 59  4534 4534 ALA ALA A . n 
A 1 60  SER 60  4535 4535 SER SER A . n 
A 1 61  ALA 61  4536 4536 ALA ALA A . n 
A 1 62  GLY 62  4537 4537 GLY GLY A . n 
A 1 63  THR 63  4538 4538 THR THR A . n 
A 1 64  ASP 64  4539 4539 ASP ASP A . n 
A 1 65  GLY 65  4540 4540 GLY GLY A . n 
A 1 66  ALA 66  4541 4541 ALA ALA A . n 
A 1 67  GLY 67  4542 4542 GLY GLY A . n 
A 1 68  THR 68  4543 4543 THR THR A . n 
A 1 69  VAL 69  4544 4544 VAL VAL A . n 
A 1 70  ASN 70  4545 4545 ASN ASN A . n 
A 1 71  ILE 71  4546 4546 ILE ILE A . n 
A 1 72  PHE 72  4547 4547 PHE PHE A . n 
A 1 73  LEU 73  4548 4548 LEU LEU A . n 
A 1 74  VAL 74  4549 4549 VAL VAL A . n 
A 1 75  ASP 75  4550 4550 ASP ASP A . n 
A 1 76  PHE 76  4551 4551 PHE PHE A . n 
A 1 77  ASP 77  4552 4552 ASP ASP A . n 
A 1 78  THR 78  4553 4553 THR THR A . n 
A 1 79  LEU 79  4554 4554 LEU LEU A . n 
A 1 80  ALA 80  4555 4555 ALA ALA A . n 
A 1 81  ASN 81  4556 4556 ASN ASN A . n 
A 1 82  LYS 82  4557 4557 LYS LYS A . n 
A 1 83  SER 83  4558 4558 SER SER A . n 
A 1 84  VAL 84  4559 4559 VAL VAL A . n 
A 1 85  SER 85  4560 4560 SER SER A . n 
A 1 86  VAL 86  4561 4561 VAL VAL A . n 
A 1 87  ASN 87  4562 4562 ASN ASN A . n 
A 1 88  LEU 88  4563 4563 LEU LEU A . n 
A 1 89  LYS 89  4564 4564 LYS LYS A . n 
A 1 90  ASP 90  4565 4565 ASP ASP A . n 
A 1 91  SER 91  4566 4566 SER SER A . n 
A 1 92  ASN 92  4567 4567 ASN ASN A . n 
A 1 93  ALA 93  4568 4568 ALA ALA A . n 
A 1 94  LEU 94  4569 4569 LEU LEU A . n 
A 1 95  SER 95  4570 4570 SER SER A . n 
A 1 96  GLN 96  4571 4571 GLN GLN A . n 
A 1 97  LEU 97  4572 4572 LEU LEU A . n 
A 1 98  GLN 98  4573 4573 GLN GLN A . n 
A 1 99  ALA 99  4574 4574 ALA ALA A . n 
A 1 100 ILE 100 4575 4575 ILE ILE A . n 
A 1 101 LEU 101 4576 4576 LEU LEU A . n 
A 1 102 ASP 102 4577 4577 ASP ASP A . n 
A 1 103 SER 103 4578 4578 SER SER A . n 
A 1 104 MET 104 4579 4579 MET MET A . n 
A 1 105 ASP 105 4580 4580 ASP ASP A . n 
A 1 106 GLY 106 4581 4581 GLY GLY A . n 
A 1 107 SER 107 4582 4582 SER SER A . n 
A 1 108 THR 108 4583 4583 THR THR A . n 
A 1 109 ASN 109 4584 4584 ASN ASN A . n 
A 1 110 SER 110 4585 4585 SER SER A . n 
A 1 111 GLY 111 4586 4586 GLY GLY A . n 
A 1 112 GLY 112 4587 4587 GLY GLY A . n 
A 1 113 GLY 113 4588 4588 GLY GLY A . n 
A 1 114 THR 114 4589 4589 THR THR A . n 
A 1 115 ASN 115 4590 4590 ASN ASN A . n 
A 1 116 TYR 116 4591 4591 TYR TYR A . n 
A 1 117 GLU 117 4592 4592 GLU GLU A . n 
A 1 118 ASP 118 4593 4593 ASP ASP A . n 
A 1 119 VAL 119 4594 4594 VAL VAL A . n 
A 1 120 PHE 120 4595 4595 PHE PHE A . n 
A 1 121 LYS 121 4596 4596 LYS LYS A . n 
A 1 122 THR 122 4597 4597 THR THR A . n 
A 1 123 THR 123 4598 4598 THR THR A . n 
A 1 124 ALA 124 4599 4599 ALA ALA A . n 
A 1 125 ASN 125 4600 4600 ASN ASN A . n 
A 1 126 TRP 126 4601 4601 TRP TRP A . n 
A 1 127 PHE 127 4602 4602 PHE PHE A . n 
A 1 128 ASN 128 4603 4603 ASN ASN A . n 
A 1 129 SER 129 4604 4604 SER SER A . n 
A 1 130 SER 130 4605 4605 SER SER A . n 
A 1 131 THR 131 4606 4606 THR THR A . n 
A 1 132 VAL 132 4607 4607 VAL VAL A . n 
A 1 133 GLN 133 4608 4608 GLN GLN A . n 
A 1 134 GLY 134 4609 4609 GLY GLY A . n 
A 1 135 ASN 135 4610 4610 ASN ASN A . n 
A 1 136 THR 136 4611 4611 THR THR A . n 
A 1 137 ASN 137 4612 4612 ASN ASN A . n 
A 1 138 ALA 138 4613 4613 ALA ALA A . n 
A 1 139 LYS 139 4614 4614 LYS LYS A . n 
A 1 140 ASN 140 4615 4615 ASN ASN A . n 
A 1 141 LEU 141 4616 4616 LEU LEU A . n 
A 1 142 THR 142 4617 4617 THR THR A . n 
A 1 143 TYR 143 4618 4618 TYR TYR A . n 
A 1 144 PHE 144 4619 4619 PHE PHE A . n 
A 1 145 ILE 145 4620 4620 ILE ILE A . n 
A 1 146 THR 146 4621 4621 THR THR A . n 
A 1 147 ASP 147 4622 4622 ASP ASP A . n 
A 1 148 GLY 148 4623 4623 GLY GLY A . n 
A 1 149 GLN 149 4624 4624 GLN GLN A . n 
A 1 150 PRO 150 4625 4625 PRO PRO A . n 
A 1 151 THR 151 4626 4626 THR THR A . n 
A 1 152 PHE 152 4627 4627 PHE PHE A . n 
A 1 153 TYR 153 4628 4628 TYR TYR A . n 
A 1 154 LEU 154 4629 4629 LEU LEU A . n 
A 1 155 GLU 155 4630 4630 GLU GLU A . n 
A 1 156 ASN 156 4631 4631 ASN ASN A . n 
A 1 157 GLU 157 4632 4632 GLU GLU A . n 
A 1 158 GLY 158 4633 4633 GLY GLY A . n 
A 1 159 SER 159 4634 4634 SER SER A . n 
A 1 160 ASP 160 4635 4635 ASP ASP A . n 
A 1 161 PRO 161 4636 4636 PRO PRO A . n 
A 1 162 MET 162 4637 4637 MET MET A . n 
A 1 163 ILE 163 4638 4638 ILE ILE A . n 
A 1 164 ARG 164 4639 4639 ARG ARG A . n 
A 1 165 ASP 165 4640 4640 ASP ASP A . n 
A 1 166 ARG 166 4641 4641 ARG ARG A . n 
A 1 167 SER 167 4642 4642 SER SER A . n 
A 1 168 GLY 168 4643 4643 GLY GLY A . n 
A 1 169 THR 169 4644 4644 THR THR A . n 
A 1 170 VAL 170 4645 4645 VAL VAL A . n 
A 1 171 ASN 171 4646 4646 ASN ASN A . n 
A 1 172 ASP 172 4647 4647 ASP ASP A . n 
A 1 173 VAL 173 4648 4648 VAL VAL A . n 
A 1 174 TYR 174 4649 4649 TYR TYR A . n 
A 1 175 LEU 175 4650 4650 LEU LEU A . n 
A 1 176 SER 176 4651 4651 SER SER A . n 
A 1 177 ASN 177 4652 4652 ASN ASN A . n 
A 1 178 VAL 178 4653 4653 VAL VAL A . n 
A 1 179 ILE 179 4654 4654 ILE ILE A . n 
A 1 180 GLY 180 4655 4655 GLY GLY A . n 
A 1 181 THR 181 4656 4656 THR THR A . n 
A 1 182 SER 182 4657 4657 SER SER A . n 
A 1 183 TYR 183 4658 4658 TYR TYR A . n 
A 1 184 THR 184 4659 4659 THR THR A . n 
A 1 185 TYR 185 4660 4660 TYR TYR A . n 
A 1 186 GLY 186 4661 4661 GLY GLY A . n 
A 1 187 GLN 187 4662 4662 GLN GLN A . n 
A 1 188 THR 188 4663 4663 THR THR A . n 
A 1 189 TYR 189 4664 4664 TYR TYR A . n 
A 1 190 SER 190 4665 4665 SER SER A . n 
A 1 191 VAL 191 4666 4666 VAL VAL A . n 
A 1 192 ASN 192 4667 4667 ASN ASN A . n 
A 1 193 GLY 193 4668 4668 GLY GLY A . n 
A 1 194 ARG 194 4669 4669 ARG ARG A . n 
A 1 195 THR 195 4670 4670 THR THR A . n 
A 1 196 VAL 196 4671 4671 VAL VAL A . n 
A 1 197 VAL 197 4672 4672 VAL VAL A . n 
A 1 198 ASN 198 4673 4673 ASN ASN A . n 
A 1 199 GLY 199 4674 4674 GLY GLY A . n 
A 1 200 ASN 200 4675 4675 ASN ASN A . n 
A 1 201 GLY 201 4676 4676 GLY GLY A . n 
A 1 202 VAL 202 4677 4677 VAL VAL A . n 
A 1 203 VAL 203 4678 4678 VAL VAL A . n 
A 1 204 TYR 204 4679 4679 TYR TYR A . n 
A 1 205 ASP 205 4680 4680 ASP ASP A . n 
A 1 206 TYR 206 4681 4681 TYR TYR A . n 
A 1 207 ASN 207 4682 4682 ASN ASN A . n 
A 1 208 GLY 208 4683 4683 GLY GLY A . n 
A 1 209 ASN 209 4684 4684 ASN ASN A . n 
A 1 210 GLN 210 4685 4685 GLN GLN A . n 
A 1 211 ILE 211 4686 4686 ILE ILE A . n 
A 1 212 GLY 212 4687 4687 GLY GLY A . n 
A 1 213 TYR 213 4688 4688 TYR TYR A . n 
A 1 214 MET 214 4689 4689 MET MET A . n 
A 1 215 ARG 215 4690 4690 ARG ARG A . n 
A 1 216 PRO 216 4691 4691 PRO PRO A . n 
A 1 217 ASP 217 4692 4692 ASP ASP A . n 
A 1 218 GLY 218 4693 4693 GLY GLY A . n 
A 1 219 ALA 219 4694 4694 ALA ALA A . n 
A 1 220 GLY 220 4695 4695 GLY GLY A . n 
A 1 221 ARG 221 4696 4696 ARG ARG A . n 
A 1 222 TYR 222 4697 4697 TYR TYR A . n 
A 1 223 VAL 223 4698 4698 VAL VAL A . n 
A 1 224 TYR 224 4699 4699 TYR TYR A . n 
A 1 225 ALA 225 4700 4700 ALA ALA A . n 
A 1 226 THR 226 4701 4701 THR THR A . n 
A 1 227 LEU 227 4702 4702 LEU LEU A . n 
A 1 228 ALA 228 4703 4703 ALA ALA A . n 
A 1 229 GLY 229 4704 4704 GLY GLY A . n 
A 1 230 THR 230 4705 4705 THR THR A . n 
A 1 231 GLY 231 4706 4706 GLY GLY A . n 
A 1 232 ASN 232 4707 4707 ASN ASN A . n 
A 1 233 SER 233 4708 4708 SER SER A . n 
A 1 234 THR 234 4709 4709 THR THR A . n 
A 1 235 SER 235 4710 4710 SER SER A . n 
A 1 236 SER 236 4711 4711 SER SER A . n 
A 1 237 THR 237 4712 4712 THR THR A . n 
A 1 238 THR 238 4713 4713 THR THR A . n 
A 1 239 ILE 239 4714 4714 ILE ILE A . n 
A 1 240 ALA 240 4715 4715 ALA ALA A . n 
A 1 241 ASN 241 4716 4716 ASN ASN A . n 
A 1 242 SER 242 4717 4717 SER SER A . n 
A 1 243 VAL 243 4718 4718 VAL VAL A . n 
A 1 244 ALA 244 4719 4719 ALA ALA A . n 
A 1 245 GLY 245 4720 4720 GLY GLY A . n 
A 1 246 PHE 246 4721 4721 PHE PHE A . n 
A 1 247 GLY 247 4722 4722 GLY GLY A . n 
A 1 248 LEU 248 4723 4723 LEU LEU A . n 
A 1 249 LEU 249 4724 4724 LEU LEU A . n 
A 1 250 THR 250 4725 4725 THR THR A . n 
A 1 251 GLY 251 4726 4726 GLY GLY A . n 
A 1 252 MET 252 4727 4727 MET MET A . n 
A 1 253 GLY 253 4728 4728 GLY GLY A . n 
A 1 254 VAL 254 4729 4729 VAL VAL A . n 
A 1 255 THR 255 4730 4730 THR THR A . n 
A 1 256 VAL 256 4731 4731 VAL VAL A . n 
A 1 257 GLU 257 4732 4732 GLU GLU A . n 
A 1 258 ALA 258 4733 4733 ALA ALA A . n 
A 1 259 ILE 259 4734 4734 ILE ILE A . n 
A 1 260 GLY 260 4735 4735 GLY GLY A . n 
A 1 261 LEU 261 4736 4736 LEU LEU A . n 
A 1 262 GLY 262 4737 4737 GLY GLY A . n 
A 1 263 ALA 263 4738 4738 ALA ALA A . n 
A 1 264 ASN 264 4739 4739 ASN ASN A . n 
A 1 265 ILE 265 4740 4740 ILE ILE A . n 
A 1 266 SER 266 4741 4741 SER SER A . n 
A 1 267 TYR 267 4742 4742 TYR TYR A . n 
A 1 268 ASN 268 4743 4743 ASN ASN A . n 
A 1 269 ASP 269 4744 4744 ASP ASP A . n 
A 1 270 LEU 270 4745 4745 LEU LEU A . n 
A 1 271 LYS 271 4746 4746 LYS LYS A . n 
A 1 272 SER 272 4747 4747 SER SER A . n 
A 1 273 TYR 273 4748 4748 TYR TYR A . n 
A 1 274 ASP 274 4749 4749 ASP ASP A . n 
A 1 275 SER 275 4750 4750 SER SER A . n 
A 1 276 ASP 276 4751 4751 ASP ASP A . n 
A 1 277 GLY 277 4752 4752 GLY GLY A . n 
A 1 278 VAL 278 4753 4753 VAL VAL A . n 
A 1 279 ILE 279 4754 4754 ILE ILE A . n 
A 1 280 MET 280 4755 4755 MET MET A . n 
A 1 281 THR 281 4756 4756 THR THR A . n 
A 1 282 GLY 282 4757 4757 GLY GLY A . n 
A 1 283 VAL 283 4758 4758 VAL VAL A . n 
A 1 284 ASN 284 4759 4759 ASN ASN A . n 
A 1 285 ALA 285 4760 4760 ALA ALA A . n 
A 1 286 SER 286 4761 4761 SER SER A . n 
A 1 287 ASP 287 4762 4762 ASP ASP A . n 
A 1 288 LEU 288 4763 4763 LEU LEU A . n 
A 1 289 ALA 289 4764 4764 ALA ALA A . n 
A 1 290 ASN 290 4765 4765 ASN ASN A . n 
A 1 291 ALA 291 4766 4766 ALA ALA A . n 
A 1 292 ILE 292 4767 4767 ILE ILE A . n 
A 1 293 LEU 293 4768 4768 LEU LEU A . n 
A 1 294 GLY 294 4769 4769 GLY GLY A . n 
A 1 295 THR 295 4770 4770 THR THR A . n 
A 1 296 SER 296 4771 ?    ?   ?   A . n 
A 1 297 VAL 297 4772 ?    ?   ?   A . n 
A 1 298 ASN 298 4773 ?    ?   ?   A . n 
A 1 299 ASN 299 4774 ?    ?   ?   A . n 
A 1 300 LEU 300 4775 ?    ?   ?   A . n 
A 1 301 PRO 301 4776 ?    ?   ?   A . n 
B 1 1   MET 1   4476 ?    ?   ?   B . n 
B 1 2   ALA 2   4477 ?    ?   ?   B . n 
B 1 3   SER 3   4478 ?    ?   ?   B . n 
B 1 4   SER 4   4479 ?    ?   ?   B . n 
B 1 5   HIS 5   4480 ?    ?   ?   B . n 
B 1 6   HIS 6   4481 ?    ?   ?   B . n 
B 1 7   HIS 7   4482 ?    ?   ?   B . n 
B 1 8   HIS 8   4483 ?    ?   ?   B . n 
B 1 9   HIS 9   4484 ?    ?   ?   B . n 
B 1 10  HIS 10  4485 ?    ?   ?   B . n 
B 1 11  SER 11  4486 ?    ?   ?   B . n 
B 1 12  SER 12  4487 ?    ?   ?   B . n 
B 1 13  GLY 13  4488 ?    ?   ?   B . n 
B 1 14  LEU 14  4489 ?    ?   ?   B . n 
B 1 15  VAL 15  4490 ?    ?   ?   B . n 
B 1 16  PRO 16  4491 ?    ?   ?   B . n 
B 1 17  ARG 17  4492 ?    ?   ?   B . n 
B 1 18  GLY 18  4493 ?    ?   ?   B . n 
B 1 19  SER 19  4494 ?    ?   ?   B . n 
B 1 20  HIS 20  4495 ?    ?   ?   B . n 
B 1 21  MET 21  4496 ?    ?   ?   B . n 
B 1 22  PRO 22  4497 4497 PRO PRO B . n 
B 1 23  GLY 23  4498 4498 GLY GLY B . n 
B 1 24  GLN 24  4499 4499 GLN GLN B . n 
B 1 25  ASN 25  4500 4500 ASN ASN B . n 
B 1 26  TYR 26  4501 4501 TYR TYR B . n 
B 1 27  ASN 27  4502 4502 ASN ASN B . n 
B 1 28  ILE 28  4503 4503 ILE ILE B . n 
B 1 29  ALA 29  4504 4504 ALA ALA B . n 
B 1 30  PHE 30  4505 4505 PHE PHE B . n 
B 1 31  MET 31  4506 4506 MET MET B . n 
B 1 32  VAL 32  4507 4507 VAL VAL B . n 
B 1 33  ASP 33  4508 4508 ASP ASP B . n 
B 1 34  SER 34  4509 4509 SER SER B . n 
B 1 35  SER 35  4510 4510 SER SER B . n 
B 1 36  GLY 36  4511 4511 GLY GLY B . n 
B 1 37  SER 37  4512 4512 SER SER B . n 
B 1 38  ILE 38  4513 4513 ILE ILE B . n 
B 1 39  GLY 39  4514 4514 GLY GLY B . n 
B 1 40  SER 40  4515 4515 SER SER B . n 
B 1 41  SER 41  4516 4516 SER SER B . n 
B 1 42  ALA 42  4517 4517 ALA ALA B . n 
B 1 43  MET 43  4518 4518 MET MET B . n 
B 1 44  ASN 44  4519 4519 ASN ASN B . n 
B 1 45  THR 45  4520 4520 THR THR B . n 
B 1 46  ILE 46  4521 4521 ILE ILE B . n 
B 1 47  LYS 47  4522 4522 LYS LYS B . n 
B 1 48  SER 48  4523 4523 SER SER B . n 
B 1 49  GLN 49  4524 4524 GLN GLN B . n 
B 1 50  LEU 50  4525 4525 LEU LEU B . n 
B 1 51  ALA 51  4526 4526 ALA ALA B . n 
B 1 52  GLN 52  4527 4527 GLN GLN B . n 
B 1 53  VAL 53  4528 4528 VAL VAL B . n 
B 1 54  PHE 54  4529 4529 PHE PHE B . n 
B 1 55  SER 55  4530 4530 SER SER B . n 
B 1 56  SER 56  4531 4531 SER SER B . n 
B 1 57  LEU 57  4532 4532 LEU LEU B . n 
B 1 58  LYS 58  4533 4533 LYS LYS B . n 
B 1 59  ALA 59  4534 4534 ALA ALA B . n 
B 1 60  SER 60  4535 4535 SER SER B . n 
B 1 61  ALA 61  4536 4536 ALA ALA B . n 
B 1 62  GLY 62  4537 4537 GLY GLY B . n 
B 1 63  THR 63  4538 4538 THR THR B . n 
B 1 64  ASP 64  4539 4539 ASP ASP B . n 
B 1 65  GLY 65  4540 4540 GLY GLY B . n 
B 1 66  ALA 66  4541 4541 ALA ALA B . n 
B 1 67  GLY 67  4542 4542 GLY GLY B . n 
B 1 68  THR 68  4543 4543 THR THR B . n 
B 1 69  VAL 69  4544 4544 VAL VAL B . n 
B 1 70  ASN 70  4545 4545 ASN ASN B . n 
B 1 71  ILE 71  4546 4546 ILE ILE B . n 
B 1 72  PHE 72  4547 4547 PHE PHE B . n 
B 1 73  LEU 73  4548 4548 LEU LEU B . n 
B 1 74  VAL 74  4549 4549 VAL VAL B . n 
B 1 75  ASP 75  4550 4550 ASP ASP B . n 
B 1 76  PHE 76  4551 4551 PHE PHE B . n 
B 1 77  ASP 77  4552 4552 ASP ASP B . n 
B 1 78  THR 78  4553 4553 THR THR B . n 
B 1 79  LEU 79  4554 4554 LEU LEU B . n 
B 1 80  ALA 80  4555 4555 ALA ALA B . n 
B 1 81  ASN 81  4556 4556 ASN ASN B . n 
B 1 82  LYS 82  4557 4557 LYS LYS B . n 
B 1 83  SER 83  4558 4558 SER SER B . n 
B 1 84  VAL 84  4559 4559 VAL VAL B . n 
B 1 85  SER 85  4560 4560 SER SER B . n 
B 1 86  VAL 86  4561 4561 VAL VAL B . n 
B 1 87  ASN 87  4562 4562 ASN ASN B . n 
B 1 88  LEU 88  4563 4563 LEU LEU B . n 
B 1 89  LYS 89  4564 4564 LYS LYS B . n 
B 1 90  ASP 90  4565 4565 ASP ASP B . n 
B 1 91  SER 91  4566 4566 SER SER B . n 
B 1 92  ASN 92  4567 4567 ASN ASN B . n 
B 1 93  ALA 93  4568 4568 ALA ALA B . n 
B 1 94  LEU 94  4569 4569 LEU LEU B . n 
B 1 95  SER 95  4570 4570 SER SER B . n 
B 1 96  GLN 96  4571 4571 GLN GLN B . n 
B 1 97  LEU 97  4572 4572 LEU LEU B . n 
B 1 98  GLN 98  4573 4573 GLN GLN B . n 
B 1 99  ALA 99  4574 4574 ALA ALA B . n 
B 1 100 ILE 100 4575 4575 ILE ILE B . n 
B 1 101 LEU 101 4576 4576 LEU LEU B . n 
B 1 102 ASP 102 4577 4577 ASP ASP B . n 
B 1 103 SER 103 4578 4578 SER SER B . n 
B 1 104 MET 104 4579 4579 MET MET B . n 
B 1 105 ASP 105 4580 4580 ASP ASP B . n 
B 1 106 GLY 106 4581 4581 GLY GLY B . n 
B 1 107 SER 107 4582 4582 SER SER B . n 
B 1 108 THR 108 4583 4583 THR THR B . n 
B 1 109 ASN 109 4584 4584 ASN ASN B . n 
B 1 110 SER 110 4585 4585 SER SER B . n 
B 1 111 GLY 111 4586 4586 GLY GLY B . n 
B 1 112 GLY 112 4587 4587 GLY GLY B . n 
B 1 113 GLY 113 4588 4588 GLY GLY B . n 
B 1 114 THR 114 4589 4589 THR THR B . n 
B 1 115 ASN 115 4590 4590 ASN ASN B . n 
B 1 116 TYR 116 4591 4591 TYR TYR B . n 
B 1 117 GLU 117 4592 4592 GLU GLU B . n 
B 1 118 ASP 118 4593 4593 ASP ASP B . n 
B 1 119 VAL 119 4594 4594 VAL VAL B . n 
B 1 120 PHE 120 4595 4595 PHE PHE B . n 
B 1 121 LYS 121 4596 4596 LYS LYS B . n 
B 1 122 THR 122 4597 4597 THR THR B . n 
B 1 123 THR 123 4598 4598 THR THR B . n 
B 1 124 ALA 124 4599 4599 ALA ALA B . n 
B 1 125 ASN 125 4600 4600 ASN ASN B . n 
B 1 126 TRP 126 4601 4601 TRP TRP B . n 
B 1 127 PHE 127 4602 4602 PHE PHE B . n 
B 1 128 ASN 128 4603 4603 ASN ASN B . n 
B 1 129 SER 129 4604 4604 SER SER B . n 
B 1 130 SER 130 4605 4605 SER SER B . n 
B 1 131 THR 131 4606 4606 THR THR B . n 
B 1 132 VAL 132 4607 4607 VAL VAL B . n 
B 1 133 GLN 133 4608 4608 GLN GLN B . n 
B 1 134 GLY 134 4609 4609 GLY GLY B . n 
B 1 135 ASN 135 4610 4610 ASN ASN B . n 
B 1 136 THR 136 4611 4611 THR THR B . n 
B 1 137 ASN 137 4612 4612 ASN ASN B . n 
B 1 138 ALA 138 4613 4613 ALA ALA B . n 
B 1 139 LYS 139 4614 4614 LYS LYS B . n 
B 1 140 ASN 140 4615 4615 ASN ASN B . n 
B 1 141 LEU 141 4616 4616 LEU LEU B . n 
B 1 142 THR 142 4617 4617 THR THR B . n 
B 1 143 TYR 143 4618 4618 TYR TYR B . n 
B 1 144 PHE 144 4619 4619 PHE PHE B . n 
B 1 145 ILE 145 4620 4620 ILE ILE B . n 
B 1 146 THR 146 4621 4621 THR THR B . n 
B 1 147 ASP 147 4622 4622 ASP ASP B . n 
B 1 148 GLY 148 4623 4623 GLY GLY B . n 
B 1 149 GLN 149 4624 4624 GLN GLN B . n 
B 1 150 PRO 150 4625 4625 PRO PRO B . n 
B 1 151 THR 151 4626 4626 THR THR B . n 
B 1 152 PHE 152 4627 4627 PHE PHE B . n 
B 1 153 TYR 153 4628 4628 TYR TYR B . n 
B 1 154 LEU 154 4629 4629 LEU LEU B . n 
B 1 155 GLU 155 4630 4630 GLU GLU B . n 
B 1 156 ASN 156 4631 4631 ASN ASN B . n 
B 1 157 GLU 157 4632 4632 GLU GLU B . n 
B 1 158 GLY 158 4633 4633 GLY GLY B . n 
B 1 159 SER 159 4634 4634 SER SER B . n 
B 1 160 ASP 160 4635 4635 ASP ASP B . n 
B 1 161 PRO 161 4636 4636 PRO PRO B . n 
B 1 162 MET 162 4637 4637 MET MET B . n 
B 1 163 ILE 163 4638 4638 ILE ILE B . n 
B 1 164 ARG 164 4639 4639 ARG ARG B . n 
B 1 165 ASP 165 4640 4640 ASP ASP B . n 
B 1 166 ARG 166 4641 4641 ARG ARG B . n 
B 1 167 SER 167 4642 4642 SER SER B . n 
B 1 168 GLY 168 4643 4643 GLY GLY B . n 
B 1 169 THR 169 4644 4644 THR THR B . n 
B 1 170 VAL 170 4645 4645 VAL VAL B . n 
B 1 171 ASN 171 4646 4646 ASN ASN B . n 
B 1 172 ASP 172 4647 4647 ASP ASP B . n 
B 1 173 VAL 173 4648 4648 VAL VAL B . n 
B 1 174 TYR 174 4649 4649 TYR TYR B . n 
B 1 175 LEU 175 4650 4650 LEU LEU B . n 
B 1 176 SER 176 4651 4651 SER SER B . n 
B 1 177 ASN 177 4652 4652 ASN ASN B . n 
B 1 178 VAL 178 4653 4653 VAL VAL B . n 
B 1 179 ILE 179 4654 4654 ILE ILE B . n 
B 1 180 GLY 180 4655 4655 GLY GLY B . n 
B 1 181 THR 181 4656 4656 THR THR B . n 
B 1 182 SER 182 4657 4657 SER SER B . n 
B 1 183 TYR 183 4658 4658 TYR TYR B . n 
B 1 184 THR 184 4659 4659 THR THR B . n 
B 1 185 TYR 185 4660 4660 TYR TYR B . n 
B 1 186 GLY 186 4661 4661 GLY GLY B . n 
B 1 187 GLN 187 4662 4662 GLN GLN B . n 
B 1 188 THR 188 4663 4663 THR THR B . n 
B 1 189 TYR 189 4664 4664 TYR TYR B . n 
B 1 190 SER 190 4665 4665 SER SER B . n 
B 1 191 VAL 191 4666 4666 VAL VAL B . n 
B 1 192 ASN 192 4667 4667 ASN ASN B . n 
B 1 193 GLY 193 4668 4668 GLY GLY B . n 
B 1 194 ARG 194 4669 4669 ARG ARG B . n 
B 1 195 THR 195 4670 4670 THR THR B . n 
B 1 196 VAL 196 4671 4671 VAL VAL B . n 
B 1 197 VAL 197 4672 4672 VAL VAL B . n 
B 1 198 ASN 198 4673 4673 ASN ASN B . n 
B 1 199 GLY 199 4674 4674 GLY GLY B . n 
B 1 200 ASN 200 4675 4675 ASN ASN B . n 
B 1 201 GLY 201 4676 4676 GLY GLY B . n 
B 1 202 VAL 202 4677 4677 VAL VAL B . n 
B 1 203 VAL 203 4678 4678 VAL VAL B . n 
B 1 204 TYR 204 4679 4679 TYR TYR B . n 
B 1 205 ASP 205 4680 4680 ASP ASP B . n 
B 1 206 TYR 206 4681 4681 TYR TYR B . n 
B 1 207 ASN 207 4682 4682 ASN ASN B . n 
B 1 208 GLY 208 4683 4683 GLY GLY B . n 
B 1 209 ASN 209 4684 4684 ASN ASN B . n 
B 1 210 GLN 210 4685 4685 GLN GLN B . n 
B 1 211 ILE 211 4686 4686 ILE ILE B . n 
B 1 212 GLY 212 4687 4687 GLY GLY B . n 
B 1 213 TYR 213 4688 4688 TYR TYR B . n 
B 1 214 MET 214 4689 4689 MET MET B . n 
B 1 215 ARG 215 4690 4690 ARG ARG B . n 
B 1 216 PRO 216 4691 4691 PRO PRO B . n 
B 1 217 ASP 217 4692 4692 ASP ASP B . n 
B 1 218 GLY 218 4693 4693 GLY GLY B . n 
B 1 219 ALA 219 4694 4694 ALA ALA B . n 
B 1 220 GLY 220 4695 4695 GLY GLY B . n 
B 1 221 ARG 221 4696 4696 ARG ARG B . n 
B 1 222 TYR 222 4697 4697 TYR TYR B . n 
B 1 223 VAL 223 4698 4698 VAL VAL B . n 
B 1 224 TYR 224 4699 4699 TYR TYR B . n 
B 1 225 ALA 225 4700 4700 ALA ALA B . n 
B 1 226 THR 226 4701 4701 THR THR B . n 
B 1 227 LEU 227 4702 4702 LEU LEU B . n 
B 1 228 ALA 228 4703 4703 ALA ALA B . n 
B 1 229 GLY 229 4704 4704 GLY GLY B . n 
B 1 230 THR 230 4705 4705 THR THR B . n 
B 1 231 GLY 231 4706 4706 GLY GLY B . n 
B 1 232 ASN 232 4707 4707 ASN ASN B . n 
B 1 233 SER 233 4708 4708 SER SER B . n 
B 1 234 THR 234 4709 4709 THR THR B . n 
B 1 235 SER 235 4710 4710 SER SER B . n 
B 1 236 SER 236 4711 4711 SER SER B . n 
B 1 237 THR 237 4712 4712 THR THR B . n 
B 1 238 THR 238 4713 4713 THR THR B . n 
B 1 239 ILE 239 4714 4714 ILE ILE B . n 
B 1 240 ALA 240 4715 4715 ALA ALA B . n 
B 1 241 ASN 241 4716 4716 ASN ASN B . n 
B 1 242 SER 242 4717 4717 SER SER B . n 
B 1 243 VAL 243 4718 4718 VAL VAL B . n 
B 1 244 ALA 244 4719 4719 ALA ALA B . n 
B 1 245 GLY 245 4720 4720 GLY GLY B . n 
B 1 246 PHE 246 4721 4721 PHE PHE B . n 
B 1 247 GLY 247 4722 4722 GLY GLY B . n 
B 1 248 LEU 248 4723 4723 LEU LEU B . n 
B 1 249 LEU 249 4724 4724 LEU LEU B . n 
B 1 250 THR 250 4725 4725 THR THR B . n 
B 1 251 GLY 251 4726 4726 GLY GLY B . n 
B 1 252 MET 252 4727 4727 MET MET B . n 
B 1 253 GLY 253 4728 4728 GLY GLY B . n 
B 1 254 VAL 254 4729 4729 VAL VAL B . n 
B 1 255 THR 255 4730 4730 THR THR B . n 
B 1 256 VAL 256 4731 4731 VAL VAL B . n 
B 1 257 GLU 257 4732 4732 GLU GLU B . n 
B 1 258 ALA 258 4733 4733 ALA ALA B . n 
B 1 259 ILE 259 4734 4734 ILE ILE B . n 
B 1 260 GLY 260 4735 4735 GLY GLY B . n 
B 1 261 LEU 261 4736 4736 LEU LEU B . n 
B 1 262 GLY 262 4737 4737 GLY GLY B . n 
B 1 263 ALA 263 4738 4738 ALA ALA B . n 
B 1 264 ASN 264 4739 4739 ASN ASN B . n 
B 1 265 ILE 265 4740 4740 ILE ILE B . n 
B 1 266 SER 266 4741 4741 SER SER B . n 
B 1 267 TYR 267 4742 4742 TYR TYR B . n 
B 1 268 ASN 268 4743 4743 ASN ASN B . n 
B 1 269 ASP 269 4744 4744 ASP ASP B . n 
B 1 270 LEU 270 4745 4745 LEU LEU B . n 
B 1 271 LYS 271 4746 4746 LYS LYS B . n 
B 1 272 SER 272 4747 4747 SER SER B . n 
B 1 273 TYR 273 4748 4748 TYR TYR B . n 
B 1 274 ASP 274 4749 4749 ASP ASP B . n 
B 1 275 SER 275 4750 4750 SER SER B . n 
B 1 276 ASP 276 4751 4751 ASP ASP B . n 
B 1 277 GLY 277 4752 4752 GLY GLY B . n 
B 1 278 VAL 278 4753 4753 VAL VAL B . n 
B 1 279 ILE 279 4754 4754 ILE ILE B . n 
B 1 280 MET 280 4755 4755 MET MET B . n 
B 1 281 THR 281 4756 4756 THR THR B . n 
B 1 282 GLY 282 4757 4757 GLY GLY B . n 
B 1 283 VAL 283 4758 4758 VAL VAL B . n 
B 1 284 ASN 284 4759 4759 ASN ASN B . n 
B 1 285 ALA 285 4760 4760 ALA ALA B . n 
B 1 286 SER 286 4761 4761 SER SER B . n 
B 1 287 ASP 287 4762 4762 ASP ASP B . n 
B 1 288 LEU 288 4763 4763 LEU LEU B . n 
B 1 289 ALA 289 4764 4764 ALA ALA B . n 
B 1 290 ASN 290 4765 4765 ASN ASN B . n 
B 1 291 ALA 291 4766 4766 ALA ALA B . n 
B 1 292 ILE 292 4767 4767 ILE ILE B . n 
B 1 293 LEU 293 4768 4768 LEU LEU B . n 
B 1 294 GLY 294 4769 4769 GLY GLY B . n 
B 1 295 THR 295 4770 4770 THR THR B . n 
B 1 296 SER 296 4771 4771 SER SER B . n 
B 1 297 VAL 297 4772 4772 VAL VAL B . n 
B 1 298 ASN 298 4773 4773 ASN ASN B . n 
B 1 299 ASN 299 4774 ?    ?   ?   B . n 
B 1 300 LEU 300 4775 ?    ?   ?   B . n 
B 1 301 PRO 301 4776 ?    ?   ?   B . 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 
C 2 CA  1   4801 1   CA  CA  A . 
D 2 CA  1   4802 2   CA  CA  A . 
E 2 CA  1   4803 3   CA  CA  A . 
F 2 CA  1   4804 4   CA  CA  A . 
G 2 CA  1   4805 6   CA  CA  A . 
H 2 CA  1   4806 7   CA  CA  A . 
I 2 CA  1   4801 5   CA  CA  B . 
J 2 CA  1   4802 8   CA  CA  B . 
K 2 CA  1   4803 9   CA  CA  B . 
L 2 CA  1   4804 10  CA  CA  B . 
M 2 CA  1   4805 11  CA  CA  B . 
N 2 CA  1   4806 12  CA  CA  B . 
O 3 GOL 1   4807 1   GOL GOL B . 
P 4 HOH 1   4901 250 HOH HOH A . 
P 4 HOH 2   4902 225 HOH HOH A . 
P 4 HOH 3   4903 2   HOH HOH A . 
P 4 HOH 4   4904 60  HOH HOH A . 
P 4 HOH 5   4905 242 HOH HOH A . 
P 4 HOH 6   4906 120 HOH HOH A . 
P 4 HOH 7   4907 255 HOH HOH A . 
P 4 HOH 8   4908 239 HOH HOH A . 
P 4 HOH 9   4909 80  HOH HOH A . 
P 4 HOH 10  4910 10  HOH HOH A . 
P 4 HOH 11  4911 97  HOH HOH A . 
P 4 HOH 12  4912 88  HOH HOH A . 
P 4 HOH 13  4913 23  HOH HOH A . 
P 4 HOH 14  4914 229 HOH HOH A . 
P 4 HOH 15  4915 42  HOH HOH A . 
P 4 HOH 16  4916 246 HOH HOH A . 
P 4 HOH 17  4917 240 HOH HOH A . 
P 4 HOH 18  4918 72  HOH HOH A . 
P 4 HOH 19  4919 176 HOH HOH A . 
P 4 HOH 20  4920 53  HOH HOH A . 
P 4 HOH 21  4921 241 HOH HOH A . 
P 4 HOH 22  4922 95  HOH HOH A . 
P 4 HOH 23  4923 36  HOH HOH A . 
P 4 HOH 24  4924 125 HOH HOH A . 
P 4 HOH 25  4925 217 HOH HOH A . 
P 4 HOH 26  4926 27  HOH HOH A . 
P 4 HOH 27  4927 115 HOH HOH A . 
P 4 HOH 28  4928 45  HOH HOH A . 
P 4 HOH 29  4929 226 HOH HOH A . 
P 4 HOH 30  4930 85  HOH HOH A . 
P 4 HOH 31  4931 91  HOH HOH A . 
P 4 HOH 32  4932 30  HOH HOH A . 
P 4 HOH 33  4933 215 HOH HOH A . 
P 4 HOH 34  4934 3   HOH HOH A . 
P 4 HOH 35  4935 24  HOH HOH A . 
P 4 HOH 36  4936 210 HOH HOH A . 
P 4 HOH 37  4937 216 HOH HOH A . 
P 4 HOH 38  4938 121 HOH HOH A . 
P 4 HOH 39  4939 96  HOH HOH A . 
P 4 HOH 40  4940 75  HOH HOH A . 
P 4 HOH 41  4941 117 HOH HOH A . 
P 4 HOH 42  4942 126 HOH HOH A . 
P 4 HOH 43  4943 32  HOH HOH A . 
P 4 HOH 44  4944 48  HOH HOH A . 
P 4 HOH 45  4945 73  HOH HOH A . 
P 4 HOH 46  4946 76  HOH HOH A . 
P 4 HOH 47  4947 40  HOH HOH A . 
P 4 HOH 48  4948 211 HOH HOH A . 
P 4 HOH 49  4949 209 HOH HOH A . 
P 4 HOH 50  4950 208 HOH HOH A . 
P 4 HOH 51  4951 69  HOH HOH A . 
P 4 HOH 52  4952 21  HOH HOH A . 
P 4 HOH 53  4953 234 HOH HOH A . 
P 4 HOH 54  4954 99  HOH HOH A . 
P 4 HOH 55  4955 119 HOH HOH A . 
P 4 HOH 56  4956 56  HOH HOH A . 
P 4 HOH 57  4957 105 HOH HOH A . 
P 4 HOH 58  4958 251 HOH HOH A . 
P 4 HOH 59  4959 67  HOH HOH A . 
P 4 HOH 60  4960 31  HOH HOH A . 
P 4 HOH 61  4961 11  HOH HOH A . 
P 4 HOH 62  4962 103 HOH HOH A . 
P 4 HOH 63  4963 6   HOH HOH A . 
P 4 HOH 64  4964 18  HOH HOH A . 
P 4 HOH 65  4965 243 HOH HOH A . 
P 4 HOH 66  4966 57  HOH HOH A . 
P 4 HOH 67  4967 233 HOH HOH A . 
P 4 HOH 68  4968 118 HOH HOH A . 
P 4 HOH 69  4969 213 HOH HOH A . 
P 4 HOH 70  4970 123 HOH HOH A . 
P 4 HOH 71  4971 59  HOH HOH A . 
P 4 HOH 72  4972 81  HOH HOH A . 
P 4 HOH 73  4973 100 HOH HOH A . 
P 4 HOH 74  4974 248 HOH HOH A . 
P 4 HOH 75  4975 235 HOH HOH A . 
P 4 HOH 76  4976 86  HOH HOH A . 
P 4 HOH 77  4977 29  HOH HOH A . 
P 4 HOH 78  4978 104 HOH HOH A . 
P 4 HOH 79  4979 22  HOH HOH A . 
P 4 HOH 80  4980 70  HOH HOH A . 
P 4 HOH 81  4981 54  HOH HOH A . 
P 4 HOH 82  4982 112 HOH HOH A . 
P 4 HOH 83  4983 228 HOH HOH A . 
P 4 HOH 84  4984 238 HOH HOH A . 
P 4 HOH 85  4985 16  HOH HOH A . 
P 4 HOH 86  4986 1   HOH HOH A . 
P 4 HOH 87  4987 124 HOH HOH A . 
P 4 HOH 88  4988 38  HOH HOH A . 
P 4 HOH 89  4989 218 HOH HOH A . 
P 4 HOH 90  4990 92  HOH HOH A . 
P 4 HOH 91  4991 114 HOH HOH A . 
P 4 HOH 92  4992 52  HOH HOH A . 
P 4 HOH 93  4993 55  HOH HOH A . 
P 4 HOH 94  4994 51  HOH HOH A . 
P 4 HOH 95  4995 98  HOH HOH A . 
P 4 HOH 96  4996 102 HOH HOH A . 
P 4 HOH 97  4997 58  HOH HOH A . 
P 4 HOH 98  4998 26  HOH HOH A . 
P 4 HOH 99  4999 221 HOH HOH A . 
P 4 HOH 100 5000 110 HOH HOH A . 
P 4 HOH 101 5001 249 HOH HOH A . 
P 4 HOH 102 5002 107 HOH HOH A . 
P 4 HOH 103 5003 116 HOH HOH A . 
P 4 HOH 104 5004 17  HOH HOH A . 
P 4 HOH 105 5005 219 HOH HOH A . 
P 4 HOH 106 5006 50  HOH HOH A . 
P 4 HOH 107 5007 8   HOH HOH A . 
P 4 HOH 108 5008 212 HOH HOH A . 
P 4 HOH 109 5009 206 HOH HOH A . 
P 4 HOH 110 5010 220 HOH HOH A . 
P 4 HOH 111 5011 35  HOH HOH A . 
P 4 HOH 112 5012 122 HOH HOH A . 
P 4 HOH 113 5013 49  HOH HOH A . 
P 4 HOH 114 5014 74  HOH HOH A . 
P 4 HOH 115 5015 25  HOH HOH A . 
P 4 HOH 116 5016 257 HOH HOH A . 
P 4 HOH 117 5017 46  HOH HOH A . 
P 4 HOH 118 5018 222 HOH HOH A . 
P 4 HOH 119 5019 254 HOH HOH A . 
P 4 HOH 120 5020 237 HOH HOH A . 
P 4 HOH 121 5021 89  HOH HOH A . 
P 4 HOH 122 5022 44  HOH HOH A . 
P 4 HOH 123 5023 61  HOH HOH A . 
P 4 HOH 124 5024 20  HOH HOH A . 
P 4 HOH 125 5025 84  HOH HOH A . 
P 4 HOH 126 5026 207 HOH HOH A . 
P 4 HOH 127 5027 33  HOH HOH A . 
P 4 HOH 128 5028 230 HOH HOH A . 
P 4 HOH 129 5029 68  HOH HOH A . 
P 4 HOH 130 5030 78  HOH HOH A . 
P 4 HOH 131 5031 41  HOH HOH A . 
P 4 HOH 132 5032 15  HOH HOH A . 
P 4 HOH 133 5033 34  HOH HOH A . 
P 4 HOH 134 5034 12  HOH HOH A . 
P 4 HOH 135 5035 7   HOH HOH A . 
P 4 HOH 136 5036 83  HOH HOH A . 
P 4 HOH 137 5037 9   HOH HOH A . 
P 4 HOH 138 5038 214 HOH HOH A . 
P 4 HOH 139 5039 252 HOH HOH A . 
P 4 HOH 140 5040 87  HOH HOH A . 
P 4 HOH 141 5041 106 HOH HOH A . 
P 4 HOH 142 5042 236 HOH HOH A . 
P 4 HOH 143 5043 28  HOH HOH A . 
P 4 HOH 144 5044 109 HOH HOH A . 
P 4 HOH 145 5045 4   HOH HOH A . 
P 4 HOH 146 5046 13  HOH HOH A . 
P 4 HOH 147 5047 101 HOH HOH A . 
P 4 HOH 148 5048 5   HOH HOH A . 
P 4 HOH 149 5049 19  HOH HOH A . 
P 4 HOH 150 5050 43  HOH HOH A . 
P 4 HOH 151 5051 71  HOH HOH A . 
P 4 HOH 152 5052 37  HOH HOH A . 
P 4 HOH 153 5053 82  HOH HOH A . 
P 4 HOH 154 5054 253 HOH HOH A . 
P 4 HOH 155 5055 111 HOH HOH A . 
P 4 HOH 156 5056 79  HOH HOH A . 
P 4 HOH 157 5057 168 HOH HOH A . 
P 4 HOH 158 5058 108 HOH HOH A . 
Q 4 HOH 1   4901 184 HOH HOH B . 
Q 4 HOH 2   4902 202 HOH HOH B . 
Q 4 HOH 3   4903 158 HOH HOH B . 
Q 4 HOH 4   4904 198 HOH HOH B . 
Q 4 HOH 5   4905 146 HOH HOH B . 
Q 4 HOH 6   4906 165 HOH HOH B . 
Q 4 HOH 7   4907 47  HOH HOH B . 
Q 4 HOH 8   4908 203 HOH HOH B . 
Q 4 HOH 9   4909 90  HOH HOH B . 
Q 4 HOH 10  4910 113 HOH HOH B . 
Q 4 HOH 11  4911 174 HOH HOH B . 
Q 4 HOH 12  4912 151 HOH HOH B . 
Q 4 HOH 13  4913 128 HOH HOH B . 
Q 4 HOH 14  4914 129 HOH HOH B . 
Q 4 HOH 15  4915 171 HOH HOH B . 
Q 4 HOH 16  4916 195 HOH HOH B . 
Q 4 HOH 17  4917 131 HOH HOH B . 
Q 4 HOH 18  4918 197 HOH HOH B . 
Q 4 HOH 19  4919 150 HOH HOH B . 
Q 4 HOH 20  4920 154 HOH HOH B . 
Q 4 HOH 21  4921 181 HOH HOH B . 
Q 4 HOH 22  4922 143 HOH HOH B . 
Q 4 HOH 23  4923 172 HOH HOH B . 
Q 4 HOH 24  4924 177 HOH HOH B . 
Q 4 HOH 25  4925 205 HOH HOH B . 
Q 4 HOH 26  4926 132 HOH HOH B . 
Q 4 HOH 27  4927 130 HOH HOH B . 
Q 4 HOH 28  4928 194 HOH HOH B . 
Q 4 HOH 29  4929 93  HOH HOH B . 
Q 4 HOH 30  4930 192 HOH HOH B . 
Q 4 HOH 31  4931 14  HOH HOH B . 
Q 4 HOH 32  4932 149 HOH HOH B . 
Q 4 HOH 33  4933 247 HOH HOH B . 
Q 4 HOH 34  4934 142 HOH HOH B . 
Q 4 HOH 35  4935 190 HOH HOH B . 
Q 4 HOH 36  4936 144 HOH HOH B . 
Q 4 HOH 37  4937 260 HOH HOH B . 
Q 4 HOH 38  4938 163 HOH HOH B . 
Q 4 HOH 39  4939 136 HOH HOH B . 
Q 4 HOH 40  4940 201 HOH HOH B . 
Q 4 HOH 41  4941 65  HOH HOH B . 
Q 4 HOH 42  4942 64  HOH HOH B . 
Q 4 HOH 43  4943 66  HOH HOH B . 
Q 4 HOH 44  4944 188 HOH HOH B . 
Q 4 HOH 45  4945 162 HOH HOH B . 
Q 4 HOH 46  4946 137 HOH HOH B . 
Q 4 HOH 47  4947 186 HOH HOH B . 
Q 4 HOH 48  4948 189 HOH HOH B . 
Q 4 HOH 49  4949 127 HOH HOH B . 
Q 4 HOH 50  4950 160 HOH HOH B . 
Q 4 HOH 51  4951 139 HOH HOH B . 
Q 4 HOH 52  4952 185 HOH HOH B . 
Q 4 HOH 53  4953 200 HOH HOH B . 
Q 4 HOH 54  4954 77  HOH HOH B . 
Q 4 HOH 55  4955 164 HOH HOH B . 
Q 4 HOH 56  4956 152 HOH HOH B . 
Q 4 HOH 57  4957 183 HOH HOH B . 
Q 4 HOH 58  4958 39  HOH HOH B . 
Q 4 HOH 59  4959 155 HOH HOH B . 
Q 4 HOH 60  4960 224 HOH HOH B . 
Q 4 HOH 61  4961 199 HOH HOH B . 
Q 4 HOH 62  4962 94  HOH HOH B . 
Q 4 HOH 63  4963 166 HOH HOH B . 
Q 4 HOH 64  4964 259 HOH HOH B . 
Q 4 HOH 65  4965 157 HOH HOH B . 
Q 4 HOH 66  4966 148 HOH HOH B . 
Q 4 HOH 67  4967 178 HOH HOH B . 
Q 4 HOH 68  4968 156 HOH HOH B . 
Q 4 HOH 69  4969 191 HOH HOH B . 
Q 4 HOH 70  4970 196 HOH HOH B . 
Q 4 HOH 71  4971 256 HOH HOH B . 
Q 4 HOH 72  4972 227 HOH HOH B . 
Q 4 HOH 73  4973 147 HOH HOH B . 
Q 4 HOH 74  4974 258 HOH HOH B . 
Q 4 HOH 75  4975 173 HOH HOH B . 
Q 4 HOH 76  4976 133 HOH HOH B . 
Q 4 HOH 77  4977 134 HOH HOH B . 
Q 4 HOH 78  4978 245 HOH HOH B . 
Q 4 HOH 79  4979 135 HOH HOH B . 
Q 4 HOH 80  4980 159 HOH HOH B . 
Q 4 HOH 81  4981 170 HOH HOH B . 
Q 4 HOH 82  4982 179 HOH HOH B . 
Q 4 HOH 83  4983 138 HOH HOH B . 
Q 4 HOH 84  4984 62  HOH HOH B . 
Q 4 HOH 85  4985 261 HOH HOH B . 
Q 4 HOH 86  4986 244 HOH HOH B . 
Q 4 HOH 87  4987 193 HOH HOH B . 
Q 4 HOH 88  4988 141 HOH HOH B . 
Q 4 HOH 89  4989 180 HOH HOH B . 
Q 4 HOH 90  4990 140 HOH HOH B . 
Q 4 HOH 91  4991 63  HOH HOH B . 
Q 4 HOH 92  4992 145 HOH HOH B . 
Q 4 HOH 93  4993 187 HOH HOH B . 
Q 4 HOH 94  4994 262 HOH HOH B . 
Q 4 HOH 95  4995 231 HOH HOH B . 
Q 4 HOH 96  4996 232 HOH HOH B . 
Q 4 HOH 97  4997 175 HOH HOH B . 
Q 4 HOH 98  4998 167 HOH HOH B . 
Q 4 HOH 99  4999 223 HOH HOH B . 
Q 4 HOH 100 5000 204 HOH HOH B . 
Q 4 HOH 101 5001 182 HOH HOH B . 
Q 4 HOH 102 5002 169 HOH HOH B . 
Q 4 HOH 103 5003 153 HOH HOH B . 
Q 4 HOH 104 5004 161 HOH HOH B . 
# 
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_5207: 000)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AutoSol ? ? ? .                  4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? .                  5 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .                  6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.23 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DAS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.235 
_cell.length_a_esd                 ? 
_cell.length_b                     156.288 
_cell.length_b_esd                 ? 
_cell.length_c                     57.496 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9DAS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 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                   9DAS 
_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             2.51 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.07 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG3350, 0.2M CaCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
loop_
_diffrn.ambient_environment 
_diffrn.ambient_temp 
_diffrn.ambient_temp_details 
_diffrn.ambient_temp_esd 
_diffrn.crystal_id 
_diffrn.crystal_support 
_diffrn.crystal_treatment 
_diffrn.details 
_diffrn.id 
_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 
? 100 ? ? 1 ? ? ? 1 ? ? ? ? ? ? N 
? 100 ? ? 1 ? ? ? 2 ? ? ? ? ? ? N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    2 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-04-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
loop_
_diffrn_radiation.collimation 
_diffrn_radiation.diffrn_id 
_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 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l 
_diffrn_radiation.pdbx_wavelength_list 
_diffrn_radiation.pdbx_wavelength 
_diffrn_radiation.pdbx_diffrn_protocol 
_diffrn_radiation.pdbx_analyzer 
_diffrn_radiation.pdbx_scattering_type 
? 1 ? ? ?         ? ? ? ? ? 1 M ? ? 'SINGLE WAVELENGTH' ? x-ray 
? 2 ? ? 'Si(111)' ? ? ? ? ? 2 M ? ? 'SINGLE WAVELENGTH' ? x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 1.03318 1.0 
2 .       1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   2 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03318 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          15.063 
_reflns.entry_id                                       9DAS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.4 
_reflns.d_resolution_low                               45.95 
_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                                     119428 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_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                                0.08 
_reflns.pdbx_Rpim_I_all                                0.029 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 2 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.075 
_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                                    1.4 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5790 
_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                               7.6 
_reflns_shell.pdbx_chi_squared                              0.99 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.746 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                2 
_reflns_shell.pdbx_CC_half                                  0.446 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97 
_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                                 9DAS 
_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                            1.40 
_refine.ls_d_res_low                             45.97 
_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                     118765 
_refine.ls_number_reflns_R_free                  5948 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.43 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1920 
_refine.ls_R_factor_R_free                       0.2069 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1912 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          SAD 
_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                 22.03 
_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                            0.19 
_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.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        45.97 
_refine_hist.number_atoms_solvent             262 
_refine_hist.number_atoms_total               4306 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4026 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.006  ? 4094 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.808  ? 5565 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.121 ? 1405 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.077  ? 646  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 734  ? 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' 1.40 1.42 . . 214 3599 95.00  . . . . 0.3733 . . . . . . . . . . . 0.3809 
'X-RAY DIFFRACTION' 1.42 1.44 . . 163 3713 96.00  . . . . 0.3518 . . . . . . . . . . . 0.3681 
'X-RAY DIFFRACTION' 1.44 1.45 . . 196 3735 98.00  . . . . 0.3249 . . . . . . . . . . . 0.3586 
'X-RAY DIFFRACTION' 1.45 1.47 . . 208 3641 97.00  . . . . 0.3020 . . . . . . . . . . . 0.3361 
'X-RAY DIFFRACTION' 1.47 1.49 . . 192 3735 98.00  . . . . 0.2873 . . . . . . . . . . . 0.2913 
'X-RAY DIFFRACTION' 1.49 1.51 . . 208 3690 97.00  . . . . 0.2628 . . . . . . . . . . . 0.2897 
'X-RAY DIFFRACTION' 1.51 1.53 . . 189 3699 98.00  . . . . 0.2507 . . . . . . . . . . . 0.2690 
'X-RAY DIFFRACTION' 1.53 1.56 . . 203 3724 97.00  . . . . 0.2334 . . . . . . . . . . . 0.2592 
'X-RAY DIFFRACTION' 1.56 1.58 . . 196 3721 98.00  . . . . 0.2301 . . . . . . . . . . . 0.2383 
'X-RAY DIFFRACTION' 1.58 1.61 . . 178 3718 97.00  . . . . 0.2293 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 1.61 1.63 . . 178 3801 98.00  . . . . 0.2233 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 1.63 1.66 . . 191 3749 98.00  . . . . 0.2245 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 1.66 1.70 . . 207 3740 98.00  . . . . 0.2258 . . . . . . . . . . . 0.2518 
'X-RAY DIFFRACTION' 1.70 1.73 . . 194 3732 99.00  . . . . 0.2159 . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 1.73 1.77 . . 212 3729 98.00  . . . . 0.2028 . . . . . . . . . . . 0.2316 
'X-RAY DIFFRACTION' 1.77 1.81 . . 159 3819 98.00  . . . . 0.1991 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 1.81 1.85 . . 196 3765 99.00  . . . . 0.1867 . . . . . . . . . . . 0.1928 
'X-RAY DIFFRACTION' 1.85 1.90 . . 183 3832 99.00  . . . . 0.1871 . . . . . . . . . . . 0.2069 
'X-RAY DIFFRACTION' 1.90 1.96 . . 193 3759 99.00  . . . . 0.1857 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 1.96 2.02 . . 232 3735 99.00  . . . . 0.1911 . . . . . . . . . . . 0.2095 
'X-RAY DIFFRACTION' 2.02 2.10 . . 207 3818 99.00  . . . . 0.1845 . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 2.10 2.18 . . 190 3777 99.00  . . . . 0.1906 . . . . . . . . . . . 0.2242 
'X-RAY DIFFRACTION' 2.18 2.28 . . 194 3820 99.00  . . . . 0.1816 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.28 2.40 . . 211 3812 99.00  . . . . 0.1819 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 2.40 2.55 . . 202 3793 100.00 . . . . 0.1818 . . . . . . . . . . . 0.1842 
'X-RAY DIFFRACTION' 2.55 2.75 . . 218 3811 100.00 . . . . 0.1895 . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 2.75 3.02 . . 224 3818 100.00 . . . . 0.1884 . . . . . . . . . . . 0.2075 
'X-RAY DIFFRACTION' 3.02 3.46 . . 216 3797 100.00 . . . . 0.1764 . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 3.46 4.36 . . 197 3841 100.00 . . . . 0.1614 . . . . . . . . . . . 0.1731 
'X-RAY DIFFRACTION' 4.36 4.60 . . 197 3894 100.00 . . . . 0.1649 . . . . . . . . . . . 0.1657 
# 
_struct.entry_id                     9DAS 
_struct.title                        'Crystal structure of vWFA domain from large adhesion protein of Aeromonas hydrophila' 
_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        9DAS 
_struct_keywords.text            'RTX adhesin, Gram-negative bacteria, Biofilm, Putative ligand-binding domain, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 2 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0KNW4_AERHH 
_struct_ref.pdbx_db_accession          A0KNW4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PGQNYNIAFMVDSSGSIGSSAMNTIKSQLAQVFSSLKASAGTDGAGTVNIFLVDFDTLANKSVSVNLKDSNALSQLQAIL
DSMDGSTNSGGGTNYEDVFKTTANWFNSSTVQGNTNAKNLTYFITDGQPTFYLENEGSDPMIRDRSGTVNDVYLSNVIGT
SYTYGQTYSVNGRTVVNGNGVVYDYNGNQIGYMRPDGAGRYVYATLAGTGNSTSSTTIANSVAGFGLLTGMGVTVEAIGL
GANISYNDLKSYDSDGVIMTGVNASDLANAILGTSVNNLP
;
_struct_ref.pdbx_align_begin           4496 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DAS A 22 ? 301 ? A0KNW4 4496 ? 4775 ? 4497 4776 
2 1 9DAS B 22 ? 301 ? A0KNW4 4496 ? 4775 ? 4497 4776 
# 
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 9DAS MET A 1  ? UNP A0KNW4 ? ? 'initiating methionine' 4476 1  
1 9DAS ALA A 2  ? UNP A0KNW4 ? ? 'expression tag'        4477 2  
1 9DAS SER A 3  ? UNP A0KNW4 ? ? 'expression tag'        4478 3  
1 9DAS SER A 4  ? UNP A0KNW4 ? ? 'expression tag'        4479 4  
1 9DAS HIS A 5  ? UNP A0KNW4 ? ? 'expression tag'        4480 5  
1 9DAS HIS A 6  ? UNP A0KNW4 ? ? 'expression tag'        4481 6  
1 9DAS HIS A 7  ? UNP A0KNW4 ? ? 'expression tag'        4482 7  
1 9DAS HIS A 8  ? UNP A0KNW4 ? ? 'expression tag'        4483 8  
1 9DAS HIS A 9  ? UNP A0KNW4 ? ? 'expression tag'        4484 9  
1 9DAS HIS A 10 ? UNP A0KNW4 ? ? 'expression tag'        4485 10 
1 9DAS SER A 11 ? UNP A0KNW4 ? ? 'expression tag'        4486 11 
1 9DAS SER A 12 ? UNP A0KNW4 ? ? 'expression tag'        4487 12 
1 9DAS GLY A 13 ? UNP A0KNW4 ? ? 'expression tag'        4488 13 
1 9DAS LEU A 14 ? UNP A0KNW4 ? ? 'expression tag'        4489 14 
1 9DAS VAL A 15 ? UNP A0KNW4 ? ? 'expression tag'        4490 15 
1 9DAS PRO A 16 ? UNP A0KNW4 ? ? 'expression tag'        4491 16 
1 9DAS ARG A 17 ? UNP A0KNW4 ? ? 'expression tag'        4492 17 
1 9DAS GLY A 18 ? UNP A0KNW4 ? ? 'expression tag'        4493 18 
1 9DAS SER A 19 ? UNP A0KNW4 ? ? 'expression tag'        4494 19 
1 9DAS HIS A 20 ? UNP A0KNW4 ? ? 'expression tag'        4495 20 
1 9DAS MET A 21 ? UNP A0KNW4 ? ? 'expression tag'        4496 21 
2 9DAS MET B 1  ? UNP A0KNW4 ? ? 'initiating methionine' 4476 22 
2 9DAS ALA B 2  ? UNP A0KNW4 ? ? 'expression tag'        4477 23 
2 9DAS SER B 3  ? UNP A0KNW4 ? ? 'expression tag'        4478 24 
2 9DAS SER B 4  ? UNP A0KNW4 ? ? 'expression tag'        4479 25 
2 9DAS HIS B 5  ? UNP A0KNW4 ? ? 'expression tag'        4480 26 
2 9DAS HIS B 6  ? UNP A0KNW4 ? ? 'expression tag'        4481 27 
2 9DAS HIS B 7  ? UNP A0KNW4 ? ? 'expression tag'        4482 28 
2 9DAS HIS B 8  ? UNP A0KNW4 ? ? 'expression tag'        4483 29 
2 9DAS HIS B 9  ? UNP A0KNW4 ? ? 'expression tag'        4484 30 
2 9DAS HIS B 10 ? UNP A0KNW4 ? ? 'expression tag'        4485 31 
2 9DAS SER B 11 ? UNP A0KNW4 ? ? 'expression tag'        4486 32 
2 9DAS SER B 12 ? UNP A0KNW4 ? ? 'expression tag'        4487 33 
2 9DAS GLY B 13 ? UNP A0KNW4 ? ? 'expression tag'        4488 34 
2 9DAS LEU B 14 ? UNP A0KNW4 ? ? 'expression tag'        4489 35 
2 9DAS VAL B 15 ? UNP A0KNW4 ? ? 'expression tag'        4490 36 
2 9DAS PRO B 16 ? UNP A0KNW4 ? ? 'expression tag'        4491 37 
2 9DAS ARG B 17 ? UNP A0KNW4 ? ? 'expression tag'        4492 38 
2 9DAS GLY B 18 ? UNP A0KNW4 ? ? 'expression tag'        4493 39 
2 9DAS SER B 19 ? UNP A0KNW4 ? ? 'expression tag'        4494 40 
2 9DAS HIS B 20 ? UNP A0KNW4 ? ? 'expression tag'        4495 41 
2 9DAS MET B 21 ? UNP A0KNW4 ? ? 'expression tag'        4496 42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,P   
2 1 B,I,J,K,L,M,N,O,Q 
# 
_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                PDBePISA 
# 
_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 GLY A 39  ? GLY A 62  ? GLY A 4514 GLY A 4537 1 ? 24 
HELX_P HELX_P2  AA2 ASN A 92  ? MET A 104 ? ASN A 4567 MET A 4579 1 ? 13 
HELX_P HELX_P3  AA3 ASN A 115 ? ASN A 128 ? ASN A 4590 ASN A 4603 1 ? 14 
HELX_P HELX_P4  AA4 SER A 129 ? ASN A 135 ? SER A 4604 ASN A 4610 1 ? 7  
HELX_P HELX_P5  AA5 LEU A 175 ? GLY A 180 ? LEU A 4650 GLY A 4655 1 ? 6  
HELX_P HELX_P6  AA6 SER A 235 ? GLY A 251 ? SER A 4710 GLY A 4726 1 ? 17 
HELX_P HELX_P7  AA7 SER A 266 ? LYS A 271 ? SER A 4741 LYS A 4746 1 ? 6  
HELX_P HELX_P8  AA8 SER A 272 ? ASP A 274 ? SER A 4747 ASP A 4749 5 ? 3  
HELX_P HELX_P9  AA9 ASN A 284 ? SER A 286 ? ASN A 4759 SER A 4761 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 287 ? GLY A 294 ? ASP A 4762 GLY A 4769 1 ? 8  
HELX_P HELX_P11 AB2 GLY B 39  ? ASP B 64  ? GLY B 4514 ASP B 4539 1 ? 26 
HELX_P HELX_P12 AB3 ASN B 92  ? MET B 104 ? ASN B 4567 MET B 4579 1 ? 13 
HELX_P HELX_P13 AB4 ASN B 115 ? ASN B 128 ? ASN B 4590 ASN B 4603 1 ? 14 
HELX_P HELX_P14 AB5 SER B 129 ? ASN B 135 ? SER B 4604 ASN B 4610 1 ? 7  
HELX_P HELX_P15 AB6 LEU B 175 ? GLY B 180 ? LEU B 4650 GLY B 4655 1 ? 6  
HELX_P HELX_P16 AB7 SER B 235 ? GLY B 251 ? SER B 4710 GLY B 4726 1 ? 17 
HELX_P HELX_P17 AB8 SER B 266 ? LYS B 271 ? SER B 4741 LYS B 4746 1 ? 6  
HELX_P HELX_P18 AB9 SER B 272 ? ASP B 274 ? SER B 4747 ASP B 4749 5 ? 3  
HELX_P HELX_P19 AC1 ASN B 284 ? SER B 286 ? ASN B 4759 SER B 4761 5 ? 3  
HELX_P HELX_P20 AC2 ASP B 287 ? GLY B 294 ? ASP B 4762 GLY B 4769 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 34  O   ? ? ? 1_555 C CA  .   CA ? ? A SER 4509 A CA  4801 1_555 ? ? ? ? ? ? ? 2.423 ? ? 
metalc2  metalc ? ? A SER 34  OG  ? ? ? 1_555 C CA  .   CA ? ? A SER 4509 A CA  4801 1_555 ? ? ? ? ? ? ? 2.415 ? ? 
metalc3  metalc ? ? A SER 35  OG  ? ? ? 1_555 D CA  .   CA ? ? A SER 4510 A CA  4802 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc4  metalc ? ? A SER 37  OG  ? ? ? 1_555 D CA  .   CA ? ? A SER 4512 A CA  4802 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc5  metalc ? ? A SER 37  O   ? ? ? 1_555 E CA  .   CA ? ? A SER 4512 A CA  4803 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc6  metalc ? ? A ASP 77  OD2 ? ? ? 1_555 C CA  .   CA ? ? A ASP 4552 A CA  4801 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc7  metalc ? ? A ASP 105 O   ? ? ? 1_555 C CA  .   CA ? ? A ASP 4580 A CA  4801 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc8  metalc ? ? A GLY 111 O   ? ? ? 1_555 C CA  .   CA ? ? A GLY 4586 A CA  4801 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc9  metalc ? ? A THR 114 OG1 ? ? ? 1_555 D CA  .   CA ? ? A THR 4589 A CA  4802 1_555 ? ? ? ? ? ? ? 2.394 ? ? 
metalc10 metalc ? ? A GLU 117 OE1 ? ? ? 1_555 F CA  .   CA ? ? A GLU 4592 A CA  4804 1_555 ? ? ? ? ? ? ? 2.674 ? ? 
metalc11 metalc ? ? A GLU 117 OE2 ? ? ? 1_555 F CA  .   CA ? ? A GLU 4592 A CA  4804 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc12 metalc ? ? A ASP 147 OD2 ? ? ? 1_555 E CA  .   CA ? ? A ASP 4622 A CA  4803 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc13 metalc ? ? A LEU 154 O   ? ? ? 1_555 F CA  .   CA ? ? A LEU 4629 A CA  4804 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc14 metalc ? ? A GLU 157 OE2 ? ? ? 1_555 F CA  .   CA ? ? A GLU 4632 A CA  4804 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc15 metalc ? ? A ASP 165 OD1 ? ? ? 1_555 G CA  .   CA ? ? A ASP 4640 A CA  4805 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc16 metalc ? ? A ARG 166 O   ? ? ? 1_555 G CA  .   CA ? ? A ARG 4641 A CA  4805 1_555 ? ? ? ? ? ? ? 2.354 ? ? 
metalc17 metalc ? ? A GLY 168 O   ? ? ? 1_555 G CA  .   CA ? ? A GLY 4643 A CA  4805 1_555 ? ? ? ? ? ? ? 2.245 ? ? 
metalc18 metalc ? ? A ASP 172 OD1 ? ? ? 1_555 G CA  .   CA ? ? A ASP 4647 A CA  4805 1_555 ? ? ? ? ? ? ? 2.555 ? ? 
metalc19 metalc ? ? A ASP 172 OD2 ? ? ? 1_555 G CA  .   CA ? ? A ASP 4647 A CA  4805 1_555 ? ? ? ? ? ? ? 2.553 ? ? 
metalc20 metalc ? ? A GLU 257 OE1 ? ? ? 1_555 H CA  .   CA ? ? A GLU 4732 A CA  4806 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc21 metalc ? ? A ASP 274 OD1 ? ? ? 1_555 H CA  .   CA ? ? A ASP 4749 A CA  4806 1_555 ? ? ? ? ? ? ? 2.535 ? ? 
metalc22 metalc ? ? A ASP 274 OD2 ? ? ? 1_555 H CA  .   CA ? ? A ASP 4749 A CA  4806 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc23 metalc ? ? A ASP 276 OD1 ? ? ? 1_555 H CA  .   CA ? ? A ASP 4751 A CA  4806 1_555 ? ? ? ? ? ? ? 2.447 ? ? 
metalc24 metalc ? ? A VAL 278 O   ? ? ? 1_555 H CA  .   CA ? ? A VAL 4753 A CA  4806 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc25 metalc ? ? C CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4801 A HOH 4934 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
metalc26 metalc ? ? C CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4801 A HOH 4986 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc27 metalc ? ? D CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4802 A HOH 4903 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc28 metalc ? ? D CA  .   CA  ? ? ? 4_555 B ASN 298 O  ? ? A CA  4802 B ASN 4773 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc29 metalc ? ? E CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4803 A HOH 4961 1_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc30 metalc ? ? E CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4803 A HOH 5007 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc31 metalc ? ? E CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4803 A HOH 5034 1_555 ? ? ? ? ? ? ? 2.499 ? ? 
metalc32 metalc ? ? E CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4803 A HOH 5035 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc33 metalc ? ? E CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4803 A HOH 5046 1_555 ? ? ? ? ? ? ? 2.559 ? ? 
metalc34 metalc ? ? F CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4804 A HOH 4915 1_555 ? ? ? ? ? ? ? 2.436 ? ? 
metalc35 metalc ? ? F CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4804 A HOH 5031 1_555 ? ? ? ? ? ? ? 2.369 ? ? 
metalc36 metalc ? ? G CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4805 A HOH 5025 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc37 metalc ? ? G CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4805 A HOH 5036 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc38 metalc ? ? H CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4806 A HOH 4955 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc39 metalc ? ? H CA  .   CA  ? ? ? 1_555 P HOH .   O  ? ? A CA  4806 A HOH 4968 1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc40 metalc ? ? B SER 34  O   ? ? ? 1_555 K CA  .   CA ? ? B SER 4509 B CA  4803 1_555 ? ? ? ? ? ? ? 2.475 ? ? 
metalc41 metalc ? ? B SER 34  OG  ? ? ? 1_555 K CA  .   CA ? ? B SER 4509 B CA  4803 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc42 metalc ? ? B SER 35  OG  ? ? ? 1_555 J CA  .   CA ? ? B SER 4510 B CA  4802 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc43 metalc ? ? B SER 37  OG  ? ? ? 1_555 J CA  .   CA ? ? B SER 4512 B CA  4802 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc44 metalc ? ? B ASP 77  OD2 ? ? ? 1_555 K CA  .   CA ? ? B ASP 4552 B CA  4803 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
metalc45 metalc ? ? B ASP 105 O   ? ? ? 1_555 K CA  .   CA ? ? B ASP 4580 B CA  4803 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc46 metalc ? ? B GLY 111 O   ? ? ? 1_555 K CA  .   CA ? ? B GLY 4586 B CA  4803 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc47 metalc ? ? B GLU 117 OE1 ? ? ? 1_555 L CA  .   CA ? ? B GLU 4592 B CA  4804 1_555 ? ? ? ? ? ? ? 2.736 ? ? 
metalc48 metalc ? ? B GLU 117 OE2 ? ? ? 1_555 L CA  .   CA ? ? B GLU 4592 B CA  4804 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
metalc49 metalc ? ? B ASP 147 OD1 ? ? ? 1_555 J CA  .   CA ? ? B ASP 4622 B CA  4802 1_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc50 metalc ? ? B LEU 154 O   ? ? ? 1_555 L CA  .   CA ? ? B LEU 4629 B CA  4804 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc51 metalc ? ? B GLU 157 OE2 ? ? ? 1_555 L CA  .   CA ? ? B GLU 4632 B CA  4804 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc52 metalc ? ? B ASP 165 OD1 ? ? ? 1_555 I CA  .   CA ? ? B ASP 4640 B CA  4801 1_555 ? ? ? ? ? ? ? 2.290 ? ? 
metalc53 metalc ? ? B ARG 166 O   ? ? ? 1_555 I CA  .   CA ? ? B ARG 4641 B CA  4801 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc54 metalc ? ? B GLY 168 O   ? ? ? 1_555 I CA  .   CA ? ? B GLY 4643 B CA  4801 1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc55 metalc ? ? B ASP 172 OD1 ? ? ? 1_555 I CA  .   CA ? ? B ASP 4647 B CA  4801 1_555 ? ? ? ? ? ? ? 2.539 ? ? 
metalc56 metalc ? ? B ASP 172 OD2 ? ? ? 1_555 I CA  .   CA ? ? B ASP 4647 B CA  4801 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc57 metalc ? ? B ASN 241 OD1 ? ? ? 1_555 L CA  .   CA ? ? B ASN 4716 B CA  4804 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc58 metalc ? ? B GLU 257 OE1 ? ? ? 1_555 M CA  .   CA ? ? B GLU 4732 B CA  4805 1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc59 metalc ? ? B ASP 274 OD1 ? ? ? 1_555 M CA  .   CA ? ? B ASP 4749 B CA  4805 1_555 ? ? ? ? ? ? ? 2.476 ? ? 
metalc60 metalc ? ? B ASP 274 OD2 ? ? ? 1_555 M CA  .   CA ? ? B ASP 4749 B CA  4805 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc61 metalc ? ? B SER 275 O   ? ? ? 1_555 N CA  .   CA ? ? B SER 4750 B CA  4806 1_555 ? ? ? ? ? ? ? 2.631 ? ? 
metalc62 metalc ? ? B SER 275 O   ? ? ? 1_555 N CA  .   CA ? ? B SER 4750 B CA  4806 2_655 ? ? ? ? ? ? ? 2.632 ? ? 
metalc63 metalc ? ? B ASP 276 OD1 ? ? ? 1_555 M CA  .   CA ? ? B ASP 4751 B CA  4805 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc64 metalc ? ? B VAL 278 O   ? ? ? 1_555 M CA  .   CA ? ? B VAL 4753 B CA  4805 1_555 ? ? ? ? ? ? ? 2.455 ? ? 
metalc65 metalc ? ? I CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4801 B HOH 4984 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc66 metalc ? ? I CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4801 B HOH 4991 1_555 ? ? ? ? ? ? ? 2.424 ? ? 
metalc67 metalc ? ? J CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4802 B HOH 4917 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc68 metalc ? ? J CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4802 B HOH 4994 1_555 ? ? ? ? ? ? ? 2.672 ? ? 
metalc69 metalc ? ? K CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4803 B HOH 4913 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc70 metalc ? ? K CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4803 B HOH 4949 1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc71 metalc ? ? L CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4804 B HOH 4936 1_555 ? ? ? ? ? ? ? 2.433 ? ? 
metalc72 metalc ? ? L CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4804 B HOH 4992 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc73 metalc ? ? M CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4805 B HOH 4904 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc74 metalc ? ? M CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4805 B HOH 4916 1_555 ? ? ? ? ? ? ? 2.527 ? ? 
metalc75 metalc ? ? N CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4806 B HOH 4995 1_555 ? ? ? ? ? ? ? 2.466 ? ? 
metalc76 metalc ? ? N CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4806 B HOH 4995 2_655 ? ? ? ? ? ? ? 2.466 ? ? 
metalc77 metalc ? ? N CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4806 B HOH 4996 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc78 metalc ? ? N CA  .   CA  ? ? ? 1_555 Q HOH .   O  ? ? B CA  4806 B HOH 4996 2_655 ? ? ? ? ? ? ? 2.344 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 OG  ? A SER 34  ? A SER 4509 ? 1_555 71.2  ? 
2   O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 111.8 ? 
3   OG  ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 88.3  ? 
4   O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A ASP 105 ? A ASP 4580 ? 1_555 75.6  ? 
5   OG  ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A ASP 105 ? A ASP 4580 ? 1_555 99.1  ? 
6   OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A ASP 105 ? A ASP 4580 ? 1_555 171.1 ? 
7   O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A GLY 111 ? A GLY 4586 ? 1_555 73.2  ? 
8   OG  ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A GLY 111 ? A GLY 4586 ? 1_555 131.9 ? 
9   OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A GLY 111 ? A GLY 4586 ? 1_555 75.9  ? 
10  O   ? A ASP 105 ? A ASP 4580 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? A GLY 111 ? A GLY 4586 ? 1_555 102.4 ? 
11  O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4934 ? 1_555 138.9 ? 
12  OG  ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4934 ? 1_555 73.9  ? 
13  OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4934 ? 1_555 88.1  ? 
14  O   ? A ASP 105 ? A ASP 4580 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4934 ? 1_555 89.1  ? 
15  O   ? A GLY 111 ? A GLY 4586 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4934 ? 1_555 147.9 ? 
16  O   ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 137.6 ? 
17  OG  ? A SER 34  ? A SER 4509 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 149.4 ? 
18  OD2 ? A ASP 77  ? A ASP 4552 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 87.9  ? 
19  O   ? A ASP 105 ? A ASP 4580 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 83.2  ? 
20  O   ? A GLY 111 ? A GLY 4586 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 76.2  ? 
21  O   ? P HOH .   ? A HOH 4934 ? 1_555 CA ? C CA . ? A CA 4801 ? 1_555 O   ? P HOH .   ? A HOH 4986 ? 1_555 75.6  ? 
22  OG  ? A SER 35  ? A SER 4510 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 OG  ? A SER 37  ? A SER 4512 ? 1_555 81.2  ? 
23  OG  ? A SER 35  ? A SER 4510 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 OG1 ? A THR 114 ? A THR 4589 ? 1_555 82.0  ? 
24  OG  ? A SER 37  ? A SER 4512 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 OG1 ? A THR 114 ? A THR 4589 ? 1_555 161.7 ? 
25  OG  ? A SER 35  ? A SER 4510 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? P HOH .   ? A HOH 4903 ? 1_555 78.9  ? 
26  OG  ? A SER 37  ? A SER 4512 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? P HOH .   ? A HOH 4903 ? 1_555 82.3  ? 
27  OG1 ? A THR 114 ? A THR 4589 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? P HOH .   ? A HOH 4903 ? 1_555 101.4 ? 
28  OG  ? A SER 35  ? A SER 4510 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? B ASN 298 ? B ASN 4773 ? 1_555 79.1  ? 
29  OG  ? A SER 37  ? A SER 4512 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? B ASN 298 ? B ASN 4773 ? 1_555 124.4 ? 
30  OG1 ? A THR 114 ? A THR 4589 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? B ASN 298 ? B ASN 4773 ? 1_555 58.6  ? 
31  O   ? P HOH .   ? A HOH 4903 ? 1_555 CA ? D CA . ? A CA 4802 ? 1_555 O   ? B ASN 298 ? B ASN 4773 ? 1_555 43.1  ? 
32  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 78.4  ? 
33  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 4961 ? 1_555 78.0  ? 
34  OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 4961 ? 1_555 94.2  ? 
35  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5007 ? 1_555 110.3 ? 
36  OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5007 ? 1_555 75.7  ? 
37  O   ? P HOH .   ? A HOH 4961 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5007 ? 1_555 164.7 ? 
38  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5034 ? 1_555 80.9  ? 
39  OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5034 ? 1_555 133.6 ? 
40  O   ? P HOH .   ? A HOH 4961 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5034 ? 1_555 121.3 ? 
41  O   ? P HOH .   ? A HOH 5007 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5034 ? 1_555 73.4  ? 
42  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5035 ? 1_555 158.3 ? 
43  OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5035 ? 1_555 85.6  ? 
44  O   ? P HOH .   ? A HOH 4961 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5035 ? 1_555 88.9  ? 
45  O   ? P HOH .   ? A HOH 5007 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5035 ? 1_555 79.1  ? 
46  O   ? P HOH .   ? A HOH 5034 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5035 ? 1_555 120.8 ? 
47  O   ? A SER 37  ? A SER 4512 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 114.2 ? 
48  OD2 ? A ASP 147 ? A ASP 4622 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 154.9 ? 
49  O   ? P HOH .   ? A HOH 4961 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 69.1  ? 
50  O   ? P HOH .   ? A HOH 5007 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 116.2 ? 
51  O   ? P HOH .   ? A HOH 5034 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 71.3  ? 
52  O   ? P HOH .   ? A HOH 5035 ? 1_555 CA ? E CA . ? A CA 4803 ? 1_555 O   ? P HOH .   ? A HOH 5046 ? 1_555 75.9  ? 
53  OE1 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 OE2 ? A GLU 117 ? A GLU 4592 ? 1_555 50.7  ? 
54  OE1 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? A LEU 154 ? A LEU 4629 ? 1_555 77.1  ? 
55  OE2 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? A LEU 154 ? A LEU 4629 ? 1_555 106.3 ? 
56  OE1 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 OE2 ? A GLU 157 ? A GLU 4632 ? 1_555 112.4 ? 
57  OE2 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 OE2 ? A GLU 157 ? A GLU 4632 ? 1_555 75.2  ? 
58  O   ? A LEU 154 ? A LEU 4629 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 OE2 ? A GLU 157 ? A GLU 4632 ? 1_555 84.1  ? 
59  OE1 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 4915 ? 1_555 161.3 ? 
60  OE2 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 4915 ? 1_555 147.0 ? 
61  O   ? A LEU 154 ? A LEU 4629 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 4915 ? 1_555 88.5  ? 
62  OE2 ? A GLU 157 ? A GLU 4632 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 4915 ? 1_555 77.3  ? 
63  OE1 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 5031 ? 1_555 103.7 ? 
64  OE2 ? A GLU 117 ? A GLU 4592 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 5031 ? 1_555 80.6  ? 
65  O   ? A LEU 154 ? A LEU 4629 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 5031 ? 1_555 170.8 ? 
66  OE2 ? A GLU 157 ? A GLU 4632 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 5031 ? 1_555 103.8 ? 
67  O   ? P HOH .   ? A HOH 4915 ? 1_555 CA ? F CA . ? A CA 4804 ? 1_555 O   ? P HOH .   ? A HOH 5031 ? 1_555 88.6  ? 
68  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? A ARG 166 ? A ARG 4641 ? 1_555 89.7  ? 
69  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? A GLY 168 ? A GLY 4643 ? 1_555 172.4 ? 
70  O   ? A ARG 166 ? A ARG 4641 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? A GLY 168 ? A GLY 4643 ? 1_555 82.7  ? 
71  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 86.6  ? 
72  O   ? A ARG 166 ? A ARG 4641 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 77.0  ? 
73  O   ? A GLY 168 ? A GLY 4643 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 91.4  ? 
74  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 95.4  ? 
75  O   ? A ARG 166 ? A ARG 4641 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 127.3 ? 
76  O   ? A GLY 168 ? A GLY 4643 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 89.1  ? 
77  OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 51.1  ? 
78  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5025 ? 1_555 86.1  ? 
79  O   ? A ARG 166 ? A ARG 4641 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5025 ? 1_555 78.7  ? 
80  O   ? A GLY 168 ? A GLY 4643 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5025 ? 1_555 92.6  ? 
81  OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5025 ? 1_555 154.7 ? 
82  OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5025 ? 1_555 153.9 ? 
83  OD1 ? A ASP 165 ? A ASP 4640 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 96.4  ? 
84  O   ? A ARG 166 ? A ARG 4641 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 153.1 ? 
85  O   ? A GLY 168 ? A GLY 4643 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 90.5  ? 
86  OD1 ? A ASP 172 ? A ASP 4647 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 129.4 ? 
87  OD2 ? A ASP 172 ? A ASP 4647 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 78.4  ? 
88  O   ? P HOH .   ? A HOH 5025 ? 1_555 CA ? G CA . ? A CA 4805 ? 1_555 O   ? P HOH .   ? A HOH 5036 ? 1_555 75.6  ? 
89  OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 132.2 ? 
90  OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 80.5  ? 
91  OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 51.8  ? 
92  OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 153.6 ? 
93  OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 72.3  ? 
94  OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 123.4 ? 
95  OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? A VAL 278 ? A VAL 4753 ? 1_555 98.6  ? 
96  OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? A VAL 278 ? A VAL 4753 ? 1_555 90.2  ? 
97  OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? A VAL 278 ? A VAL 4753 ? 1_555 97.7  ? 
98  OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? A VAL 278 ? A VAL 4753 ? 1_555 89.7  ? 
99  OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4955 ? 1_555 78.4  ? 
100 OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4955 ? 1_555 148.3 ? 
101 OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4955 ? 1_555 157.6 ? 
102 OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4955 ? 1_555 76.2  ? 
103 O   ? A VAL 278 ? A VAL 4753 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4955 ? 1_555 92.6  ? 
104 OE1 ? A GLU 257 ? A GLU 4732 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 90.0  ? 
105 OD1 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 85.2  ? 
106 OD2 ? A ASP 274 ? A ASP 4749 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 85.3  ? 
107 OD1 ? A ASP 276 ? A ASP 4751 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 81.8  ? 
108 O   ? A VAL 278 ? A VAL 4753 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 171.2 ? 
109 O   ? P HOH .   ? A HOH 4955 ? 1_555 CA ? H CA . ? A CA 4806 ? 1_555 O   ? P HOH .   ? A HOH 4968 ? 1_555 87.4  ? 
110 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 OG  ? B SER 34  ? B SER 4509 ? 1_555 70.1  ? 
111 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 113.0 ? 
112 OG  ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 89.6  ? 
113 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B ASP 105 ? B ASP 4580 ? 1_555 75.6  ? 
114 OG  ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B ASP 105 ? B ASP 4580 ? 1_555 98.2  ? 
115 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B ASP 105 ? B ASP 4580 ? 1_555 170.1 ? 
116 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B GLY 111 ? B GLY 4586 ? 1_555 73.7  ? 
117 OG  ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B GLY 111 ? B GLY 4586 ? 1_555 132.7 ? 
118 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B GLY 111 ? B GLY 4586 ? 1_555 77.6  ? 
119 O   ? B ASP 105 ? B ASP 4580 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? B GLY 111 ? B GLY 4586 ? 1_555 101.2 ? 
120 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4913 ? 1_555 133.2 ? 
121 OG  ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4913 ? 1_555 154.8 ? 
122 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4913 ? 1_555 88.2  ? 
123 O   ? B ASP 105 ? B ASP 4580 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4913 ? 1_555 82.1  ? 
124 O   ? B GLY 111 ? B GLY 4586 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4913 ? 1_555 71.0  ? 
125 O   ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 138.8 ? 
126 OG  ? B SER 34  ? B SER 4509 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 75.8  ? 
127 OD2 ? B ASP 77  ? B ASP 4552 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 88.7  ? 
128 O   ? B ASP 105 ? B ASP 4580 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 87.3  ? 
129 O   ? B GLY 111 ? B GLY 4586 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 147.2 ? 
130 O   ? Q HOH .   ? B HOH 4913 ? 1_555 CA ? K CA . ? B CA 4803 ? 1_555 O   ? Q HOH .   ? B HOH 4949 ? 1_555 79.0  ? 
131 OG  ? B SER 35  ? B SER 4510 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 OG  ? B SER 37  ? B SER 4512 ? 1_555 95.8  ? 
132 OG  ? B SER 35  ? B SER 4510 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 OD1 ? B ASP 147 ? B ASP 4622 ? 1_555 86.1  ? 
133 OG  ? B SER 37  ? B SER 4512 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 OD1 ? B ASP 147 ? B ASP 4622 ? 1_555 71.8  ? 
134 OG  ? B SER 35  ? B SER 4510 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4917 ? 1_555 81.0  ? 
135 OG  ? B SER 37  ? B SER 4512 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4917 ? 1_555 146.1 ? 
136 OD1 ? B ASP 147 ? B ASP 4622 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4917 ? 1_555 74.3  ? 
137 OG  ? B SER 35  ? B SER 4510 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4994 ? 1_555 85.5  ? 
138 OG  ? B SER 37  ? B SER 4512 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4994 ? 1_555 87.1  ? 
139 OD1 ? B ASP 147 ? B ASP 4622 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4994 ? 1_555 156.3 ? 
140 O   ? Q HOH .   ? B HOH 4917 ? 1_555 CA ? J CA . ? B CA 4802 ? 1_555 O   ? Q HOH .   ? B HOH 4994 ? 1_555 125.9 ? 
141 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 50.2  ? 
142 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? B LEU 154 ? B LEU 4629 ? 1_555 78.9  ? 
143 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? B LEU 154 ? B LEU 4629 ? 1_555 106.2 ? 
144 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 115.2 ? 
145 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 77.5  ? 
146 O   ? B LEU 154 ? B LEU 4629 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 83.3  ? 
147 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 84.2  ? 
148 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 123.2 ? 
149 O   ? B LEU 154 ? B LEU 4629 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 93.2  ? 
150 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 159.0 ? 
151 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4936 ? 1_555 156.0 ? 
152 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4936 ? 1_555 153.3 ? 
153 O   ? B LEU 154 ? B LEU 4629 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4936 ? 1_555 85.0  ? 
154 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4936 ? 1_555 80.0  ? 
155 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4936 ? 1_555 79.1  ? 
156 OE1 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 110.3 ? 
157 OE2 ? B GLU 117 ? B GLU 4592 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 82.4  ? 
158 O   ? B LEU 154 ? B LEU 4629 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 170.5 ? 
159 OE2 ? B GLU 157 ? B GLU 4632 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 94.7  ? 
160 OD1 ? B ASN 241 ? B ASN 4716 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 85.4  ? 
161 O   ? Q HOH .   ? B HOH 4936 ? 1_555 CA ? L CA . ? B CA 4804 ? 1_555 O   ? Q HOH .   ? B HOH 4992 ? 1_555 85.5  ? 
162 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? B ARG 166 ? B ARG 4641 ? 1_555 92.6  ? 
163 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? B GLY 168 ? B GLY 4643 ? 1_555 171.5 ? 
164 O   ? B ARG 166 ? B ARG 4641 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? B GLY 168 ? B GLY 4643 ? 1_555 79.4  ? 
165 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 86.0  ? 
166 O   ? B ARG 166 ? B ARG 4641 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 75.8  ? 
167 O   ? B GLY 168 ? B GLY 4643 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 94.6  ? 
168 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 96.4  ? 
169 O   ? B ARG 166 ? B ARG 4641 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 125.4 ? 
170 O   ? B GLY 168 ? B GLY 4643 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 90.5  ? 
171 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 51.5  ? 
172 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4984 ? 1_555 84.2  ? 
173 O   ? B ARG 166 ? B ARG 4641 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4984 ? 1_555 79.1  ? 
174 O   ? B GLY 168 ? B GLY 4643 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4984 ? 1_555 91.6  ? 
175 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4984 ? 1_555 152.5 ? 
176 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4984 ? 1_555 155.3 ? 
177 OD1 ? B ASP 165 ? B ASP 4640 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 93.9  ? 
178 O   ? B ARG 166 ? B ARG 4641 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 153.9 ? 
179 O   ? B GLY 168 ? B GLY 4643 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 92.2  ? 
180 OD1 ? B ASP 172 ? B ASP 4647 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 129.8 ? 
181 OD2 ? B ASP 172 ? B ASP 4647 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 78.9  ? 
182 O   ? Q HOH .   ? B HOH 4984 ? 1_555 CA ? I CA . ? B CA 4801 ? 1_555 O   ? Q HOH .   ? B HOH 4991 ? 1_555 76.5  ? 
183 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 138.3 ? 
184 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 88.1  ? 
185 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 53.8  ? 
186 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 142.0 ? 
187 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 70.9  ? 
188 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 124.7 ? 
189 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? B VAL 278 ? B VAL 4753 ? 1_555 109.4 ? 
190 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? B VAL 278 ? B VAL 4753 ? 1_555 90.3  ? 
191 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? B VAL 278 ? B VAL 4753 ? 1_555 92.2  ? 
192 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? B VAL 278 ? B VAL 4753 ? 1_555 89.8  ? 
193 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4904 ? 1_555 67.6  ? 
194 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4904 ? 1_555 149.0 ? 
195 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4904 ? 1_555 155.7 ? 
196 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4904 ? 1_555 78.6  ? 
197 O   ? B VAL 278 ? B VAL 4753 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4904 ? 1_555 95.1  ? 
198 OE1 ? B GLU 257 ? B GLU 4732 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 80.8  ? 
199 OD1 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 80.9  ? 
200 OD2 ? B ASP 274 ? B ASP 4749 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 86.8  ? 
201 OD1 ? B ASP 276 ? B ASP 4751 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 82.4  ? 
202 O   ? B VAL 278 ? B VAL 4753 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 169.8 ? 
203 O   ? Q HOH .   ? B HOH 4904 ? 1_555 CA ? M CA . ? B CA 4805 ? 1_555 O   ? Q HOH .   ? B HOH 4916 ? 1_555 90.0  ? 
204 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? B SER 275 ? B SER 4750 ? 1_555 0.0   ? 
205 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4995 ? 1_555 85.7  ? 
206 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4995 ? 1_555 85.7  ? 
207 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4995 ? 2_655 95.2  ? 
208 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4995 ? 2_655 95.2  ? 
209 O   ? Q HOH .   ? B HOH 4995 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4995 ? 2_655 147.4 ? 
210 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 1_555 91.6  ? 
211 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 1_555 91.6  ? 
212 O   ? Q HOH .   ? B HOH 4995 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 1_555 73.7  ? 
213 O   ? Q HOH .   ? B HOH 4995 ? 2_655 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 1_555 73.7  ? 
214 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 2_655 91.6  ? 
215 O   ? B SER 275 ? B SER 4750 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 2_655 91.6  ? 
216 O   ? Q HOH .   ? B HOH 4995 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 2_655 73.7  ? 
217 O   ? Q HOH .   ? B HOH 4995 ? 2_655 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 2_655 73.7  ? 
218 O   ? Q HOH .   ? B HOH 4996 ? 1_555 CA ? N CA . ? B CA 4806 ? 1_555 O   ? Q HOH .   ? B HOH 4996 ? 2_655 0.0   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? 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 ALA A 80  ? ASN A 87  ? ALA A 4555 ASN A 4562 
AA1 2 VAL A 69  ? PHE A 76  ? VAL A 4544 PHE A 4551 
AA1 3 TYR A 26  ? ASP A 33  ? TYR A 4501 ASP A 4508 
AA1 4 LYS A 139 ? THR A 146 ? LYS A 4614 THR A 4621 
AA1 5 THR A 255 ? LEU A 261 ? THR A 4730 LEU A 4736 
AA1 6 MET A 280 ? VAL A 283 ? MET A 4755 VAL A 4758 
AA2 1 TYR A 153 ? GLU A 155 ? TYR A 4628 GLU A 4630 
AA2 2 TYR A 222 ? ALA A 228 ? TYR A 4697 ALA A 4703 
AA2 3 GLN A 210 ? PRO A 216 ? GLN A 4685 PRO A 4691 
AA2 4 VAL A 202 ? TYR A 204 ? VAL A 4677 TYR A 4679 
AA3 1 MET A 162 ? ARG A 164 ? MET A 4637 ARG A 4639 
AA3 2 VAL A 173 ? TYR A 174 ? VAL A 4648 TYR A 4649 
AA4 1 TYR A 189 ? VAL A 191 ? TYR A 4664 VAL A 4666 
AA4 2 ARG A 194 ? VAL A 197 ? ARG A 4669 VAL A 4672 
AA5 1 ALA B 80  ? ASN B 87  ? ALA B 4555 ASN B 4562 
AA5 2 VAL B 69  ? PHE B 76  ? VAL B 4544 PHE B 4551 
AA5 3 TYR B 26  ? ASP B 33  ? TYR B 4501 ASP B 4508 
AA5 4 LYS B 139 ? THR B 146 ? LYS B 4614 THR B 4621 
AA5 5 THR B 255 ? LEU B 261 ? THR B 4730 LEU B 4736 
AA5 6 MET B 280 ? VAL B 283 ? MET B 4755 VAL B 4758 
AA6 1 TYR B 153 ? GLU B 155 ? TYR B 4628 GLU B 4630 
AA6 2 TYR B 222 ? ALA B 228 ? TYR B 4697 ALA B 4703 
AA6 3 GLN B 210 ? PRO B 216 ? GLN B 4685 PRO B 4691 
AA6 4 VAL B 202 ? TYR B 204 ? VAL B 4677 TYR B 4679 
AA7 1 MET B 162 ? ARG B 164 ? MET B 4637 ARG B 4639 
AA7 2 VAL B 173 ? TYR B 174 ? VAL B 4648 TYR B 4649 
AA8 1 TYR B 189 ? VAL B 191 ? TYR B 4664 VAL B 4666 
AA8 2 ARG B 194 ? VAL B 197 ? ARG B 4669 VAL B 4672 
# 
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 ASN A 81  ? O ASN A 4556 N ASP A 75  ? N ASP A 4550 
AA1 2 3 O ASN A 70  ? O ASN A 4545 N ILE A 28  ? N ILE A 4503 
AA1 3 4 N ALA A 29  ? N ALA A 4504 O TYR A 143 ? O TYR A 4618 
AA1 4 5 N THR A 142 ? N THR A 4617 O GLU A 257 ? O GLU A 4732 
AA1 5 6 N GLY A 260 ? N GLY A 4735 O MET A 280 ? O MET A 4755 
AA2 1 2 N TYR A 153 ? N TYR A 4628 O ALA A 228 ? O ALA A 4703 
AA2 2 3 O VAL A 223 ? O VAL A 4698 N ARG A 215 ? N ARG A 4690 
AA2 3 4 O ILE A 211 ? O ILE A 4686 N VAL A 203 ? N VAL A 4678 
AA3 1 2 N ILE A 163 ? N ILE A 4638 O VAL A 173 ? O VAL A 4648 
AA4 1 2 N TYR A 189 ? N TYR A 4664 O VAL A 196 ? O VAL A 4671 
AA5 1 2 O ASN B 81  ? O ASN B 4556 N ASP B 75  ? N ASP B 4550 
AA5 2 3 O ASN B 70  ? O ASN B 4545 N ILE B 28  ? N ILE B 4503 
AA5 3 4 N MET B 31  ? N MET B 4506 O TYR B 143 ? O TYR B 4618 
AA5 4 5 N THR B 142 ? N THR B 4617 O GLU B 257 ? O GLU B 4732 
AA5 5 6 N GLY B 260 ? N GLY B 4735 O MET B 280 ? O MET B 4755 
AA6 1 2 N GLU B 155 ? N GLU B 4630 O THR B 226 ? O THR B 4701 
AA6 2 3 O VAL B 223 ? O VAL B 4698 N ARG B 215 ? N ARG B 4690 
AA6 3 4 O ILE B 211 ? O ILE B 4686 N VAL B 203 ? N VAL B 4678 
AA7 1 2 N ILE B 163 ? N ILE B 4638 O VAL B 173 ? O VAL B 4648 
AA8 1 2 N TYR B 189 ? N TYR B 4664 O VAL B 196 ? O VAL B 4671 
# 
_pdbx_entry_details.entry_id                   9DAS 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   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 ASP A 4552 ? ? -146.04 -103.47 
2 1 ASN A 4556 ? ? -105.04 -123.54 
3 1 ASP B 4552 ? ? -142.90 -106.15 
4 1 ASN B 4556 ? ? -105.12 -121.79 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B CA  4806 ? N CA  . 
2 1 B HOH 4996 ? Q HOH . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 4476 ? A MET 1   
2  1 Y 1 A ALA 4477 ? A ALA 2   
3  1 Y 1 A SER 4478 ? A SER 3   
4  1 Y 1 A SER 4479 ? A SER 4   
5  1 Y 1 A HIS 4480 ? A HIS 5   
6  1 Y 1 A HIS 4481 ? A HIS 6   
7  1 Y 1 A HIS 4482 ? A HIS 7   
8  1 Y 1 A HIS 4483 ? A HIS 8   
9  1 Y 1 A HIS 4484 ? A HIS 9   
10 1 Y 1 A HIS 4485 ? A HIS 10  
11 1 Y 1 A SER 4486 ? A SER 11  
12 1 Y 1 A SER 4487 ? A SER 12  
13 1 Y 1 A GLY 4488 ? A GLY 13  
14 1 Y 1 A LEU 4489 ? A LEU 14  
15 1 Y 1 A VAL 4490 ? A VAL 15  
16 1 Y 1 A PRO 4491 ? A PRO 16  
17 1 Y 1 A ARG 4492 ? A ARG 17  
18 1 Y 1 A GLY 4493 ? A GLY 18  
19 1 Y 1 A SER 4494 ? A SER 19  
20 1 Y 1 A HIS 4495 ? A HIS 20  
21 1 Y 1 A MET 4496 ? A MET 21  
22 1 Y 1 A PRO 4497 ? A PRO 22  
23 1 Y 1 A SER 4771 ? A SER 296 
24 1 Y 1 A VAL 4772 ? A VAL 297 
25 1 Y 1 A ASN 4773 ? A ASN 298 
26 1 Y 1 A ASN 4774 ? A ASN 299 
27 1 Y 1 A LEU 4775 ? A LEU 300 
28 1 Y 1 A PRO 4776 ? A PRO 301 
29 1 Y 1 B MET 4476 ? B MET 1   
30 1 Y 1 B ALA 4477 ? B ALA 2   
31 1 Y 1 B SER 4478 ? B SER 3   
32 1 Y 1 B SER 4479 ? B SER 4   
33 1 Y 1 B HIS 4480 ? B HIS 5   
34 1 Y 1 B HIS 4481 ? B HIS 6   
35 1 Y 1 B HIS 4482 ? B HIS 7   
36 1 Y 1 B HIS 4483 ? B HIS 8   
37 1 Y 1 B HIS 4484 ? B HIS 9   
38 1 Y 1 B HIS 4485 ? B HIS 10  
39 1 Y 1 B SER 4486 ? B SER 11  
40 1 Y 1 B SER 4487 ? B SER 12  
41 1 Y 1 B GLY 4488 ? B GLY 13  
42 1 Y 1 B LEU 4489 ? B LEU 14  
43 1 Y 1 B VAL 4490 ? B VAL 15  
44 1 Y 1 B PRO 4491 ? B PRO 16  
45 1 Y 1 B ARG 4492 ? B ARG 17  
46 1 Y 1 B GLY 4493 ? B GLY 18  
47 1 Y 1 B SER 4494 ? B SER 19  
48 1 Y 1 B HIS 4495 ? B HIS 20  
49 1 Y 1 B MET 4496 ? B MET 21  
50 1 Y 1 B ASN 4774 ? B ASN 299 
51 1 Y 1 B LEU 4775 ? B LEU 300 
52 1 Y 1 B PRO 4776 ? B PRO 301 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
GOL C1   C  N N 124 
GOL O1   O  N N 125 
GOL C2   C  N N 126 
GOL O2   O  N N 127 
GOL C3   C  N N 128 
GOL O3   O  N N 129 
GOL H11  H  N N 130 
GOL H12  H  N N 131 
GOL HO1  H  N N 132 
GOL H2   H  N N 133 
GOL HO2  H  N N 134 
GOL H31  H  N N 135 
GOL H32  H  N N 136 
GOL HO3  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
GOL C1  O1   sing N N 116 
GOL C1  C2   sing N N 117 
GOL C1  H11  sing N N 118 
GOL C1  H12  sing N N 119 
GOL O1  HO1  sing N N 120 
GOL C2  O2   sing N N 121 
GOL C2  C3   sing N N 122 
GOL C2  H2   sing N N 123 
GOL O2  HO2  sing N N 124 
GOL C3  O3   sing N N 125 
GOL C3  H31  sing N N 126 
GOL C3  H32  sing N N 127 
GOL O3  HO3  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Canadian Institutes of Health Research (CIHR)'                     Canada 'FRN 148422'     1 
'Natural Sciences and Engineering Research Council (NSERC, Canada)' Canada RGPIN-2016-04810 2 
# 
_atom_sites.entry_id                    9DAS 
_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]   0.014038 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002281 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006398 
_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]   0.017621 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 23  ? 1.561   7.340   15.590  1.00 35.63 ?  4498 GLY A N   1 
ATOM   2    C  CA  . GLY A 1 23  ? 1.418   7.491   14.153  1.00 31.62 ?  4498 GLY A CA  1 
ATOM   3    C  C   . GLY A 1 23  ? 2.621   6.994   13.373  1.00 29.13 ?  4498 GLY A C   1 
ATOM   4    O  O   . GLY A 1 23  ? 2.686   7.151   12.151  1.00 32.73 ?  4498 GLY A O   1 
ATOM   5    N  N   . GLN A 1 24  ? 3.576   6.392   14.075  1.00 30.44 ?  4499 GLN A N   1 
ATOM   6    C  CA  . GLN A 1 24  ? 4.792   5.918   13.425  1.00 26.03 ?  4499 GLN A CA  1 
ATOM   7    C  C   . GLN A 1 24  ? 4.490   4.712   12.540  1.00 22.30 ?  4499 GLN A C   1 
ATOM   8    O  O   . GLN A 1 24  ? 3.898   3.731   13.000  1.00 24.82 ?  4499 GLN A O   1 
ATOM   9    C  CB  . GLN A 1 24  ? 5.827   5.534   14.480  1.00 28.51 ?  4499 GLN A CB  1 
ATOM   10   C  CG  . GLN A 1 24  ? 7.121   4.962   13.914  1.00 26.79 ?  4499 GLN A CG  1 
ATOM   11   C  CD  . GLN A 1 24  ? 7.946   5.986   13.164  1.00 30.21 ?  4499 GLN A CD  1 
ATOM   12   O  OE1 . GLN A 1 24  ? 8.349   7.009   13.725  1.00 33.83 ?  4499 GLN A OE1 1 
ATOM   13   N  NE2 . GLN A 1 24  ? 8.205   5.719   11.891  1.00 27.93 ?  4499 GLN A NE2 1 
ATOM   14   N  N   . ASN A 1 25  ? 4.900   4.792   11.273  1.00 23.22 ?  4500 ASN A N   1 
ATOM   15   C  CA  . ASN A 1 25  ? 4.783   3.668   10.351  1.00 20.44 ?  4500 ASN A CA  1 
ATOM   16   C  C   . ASN A 1 25  ? 5.964   2.717   10.536  1.00 22.21 ?  4500 ASN A C   1 
ATOM   17   O  O   . ASN A 1 25  ? 7.082   3.141   10.831  1.00 21.24 ?  4500 ASN A O   1 
ATOM   18   C  CB  . ASN A 1 25  ? 4.783   4.170   8.908   1.00 21.88 ?  4500 ASN A CB  1 
ATOM   19   C  CG  . ASN A 1 25  ? 3.550   4.987   8.565   1.00 23.29 ?  4500 ASN A CG  1 
ATOM   20   O  OD1 . ASN A 1 25  ? 2.491   4.801   9.156   1.00 24.06 ?  4500 ASN A OD1 1 
ATOM   21   N  ND2 . ASN A 1 25  ? 3.689   5.897   7.599   1.00 24.25 ?  4500 ASN A ND2 1 
ATOM   22   N  N   . TYR A 1 26  ? 5.705   1.416   10.359  1.00 18.87 ?  4501 TYR A N   1 
ATOM   23   C  CA  . TYR A 1 26  ? 6.734   0.390   10.518  1.00 16.62 ?  4501 TYR A CA  1 
ATOM   24   C  C   . TYR A 1 26  ? 6.633   -0.637  9.402   1.00 15.54 ?  4501 TYR A C   1 
ATOM   25   O  O   . TYR A 1 26  ? 5.532   -1.035  9.008   1.00 16.41 ?  4501 TYR A O   1 
ATOM   26   C  CB  . TYR A 1 26  ? 6.584   -0.388  11.830  1.00 18.77 ?  4501 TYR A CB  1 
ATOM   27   C  CG  . TYR A 1 26  ? 6.873   0.391   13.086  1.00 24.20 ?  4501 TYR A CG  1 
ATOM   28   C  CD1 . TYR A 1 26  ? 8.155   0.430   13.625  1.00 23.42 ?  4501 TYR A CD1 1 
ATOM   29   C  CD2 . TYR A 1 26  ? 5.859   1.065   13.749  1.00 25.48 ?  4501 TYR A CD2 1 
ATOM   30   C  CE1 . TYR A 1 26  ? 8.416   1.143   14.797  1.00 26.20 ?  4501 TYR A CE1 1 
ATOM   31   C  CE2 . TYR A 1 26  ? 6.108   1.768   14.913  1.00 26.73 ?  4501 TYR A CE2 1 
ATOM   32   C  CZ  . TYR A 1 26  ? 7.382   1.802   15.427  1.00 27.43 ?  4501 TYR A CZ  1 
ATOM   33   O  OH  . TYR A 1 26  ? 7.618   2.517   16.584  1.00 34.40 ?  4501 TYR A OH  1 
ATOM   34   N  N   . ASN A 1 27  ? 7.792   -1.087  8.913   1.00 15.05 ?  4502 ASN A N   1 
ATOM   35   C  CA  . ASN A 1 27  ? 7.887   -2.312  8.119   1.00 15.11 ?  4502 ASN A CA  1 
ATOM   36   C  C   . ASN A 1 27  ? 8.797   -3.251  8.898   1.00 13.17 ?  4502 ASN A C   1 
ATOM   37   O  O   . ASN A 1 27  ? 10.001  -2.982  9.025   1.00 14.07 ?  4502 ASN A O   1 
ATOM   38   C  CB  . ASN A 1 27  ? 8.492   -2.026  6.747   1.00 15.82 ?  4502 ASN A CB  1 
ATOM   39   C  CG  . ASN A 1 27  ? 7.669   -1.052  5.943   1.00 14.92 ?  4502 ASN A CG  1 
ATOM   40   O  OD1 . ASN A 1 27  ? 6.459   -1.247  5.759   1.00 15.74 ?  4502 ASN A OD1 1 
ATOM   41   N  ND2 . ASN A 1 27  ? 8.296   0.006   5.481   1.00 17.09 ?  4502 ASN A ND2 1 
ATOM   42   N  N   . ILE A 1 28  ? 8.240   -4.352  9.401   1.00 12.77 ?  4503 ILE A N   1 
ATOM   43   C  CA  . ILE A 1 28  ? 8.955   -5.243  10.312  1.00 12.56 ?  4503 ILE A CA  1 
ATOM   44   C  C   . ILE A 1 28  ? 9.042   -6.632  9.693   1.00 12.57 ?  4503 ILE A C   1 
ATOM   45   O  O   . ILE A 1 28  ? 8.016   -7.267  9.433   1.00 14.02 ?  4503 ILE A O   1 
ATOM   46   C  CB  . ILE A 1 28  ? 8.269   -5.316  11.681  1.00 14.55 ?  4503 ILE A CB  1 
ATOM   47   C  CG1 . ILE A 1 28  ? 7.987   -3.909  12.217  1.00 16.23 ?  4503 ILE A CG1 1 
ATOM   48   C  CG2 . ILE A 1 28  ? 9.148   -6.098  12.656  1.00 14.92 ?  4503 ILE A CG2 1 
ATOM   49   C  CD1 . ILE A 1 28  ? 7.290   -3.897  13.572  1.00 15.80 ?  4503 ILE A CD1 1 
ATOM   50   N  N   . ALA A 1 29  ? 10.263  -7.109  9.469   1.00 10.36 ?  4504 ALA A N   1 
ATOM   51   C  CA  . ALA A 1 29  ? 10.467  -8.458  8.955   1.00 11.13 ?  4504 ALA A CA  1 
ATOM   52   C  C   . ALA A 1 29  ? 10.954  -9.404  10.050  1.00 11.48 ?  4504 ALA A C   1 
ATOM   53   O  O   . ALA A 1 29  ? 11.651  -9.006  10.996  1.00 13.16 ?  4504 ALA A O   1 
ATOM   54   C  CB  . ALA A 1 29  ? 11.511  -8.424  7.840   1.00 12.74 ?  4504 ALA A CB  1 
ATOM   55   N  N   . PHE A 1 30  ? 10.597  -10.677 9.898   1.00 11.15 ?  4505 PHE A N   1 
ATOM   56   C  CA  . PHE A 1 30  ? 11.025  -11.742 10.788  1.00 11.50 ?  4505 PHE A CA  1 
ATOM   57   C  C   . PHE A 1 30  ? 11.618  -12.843 9.932   1.00 13.55 ?  4505 PHE A C   1 
ATOM   58   O  O   . PHE A 1 30  ? 10.923  -13.433 9.095   1.00 13.18 ?  4505 PHE A O   1 
ATOM   59   C  CB  . PHE A 1 30  ? 9.841   -12.297 11.576  1.00 12.31 ?  4505 PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 30  ? 9.274   -11.322 12.553  1.00 11.57 ?  4505 PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 30  ? 8.371   -10.349 12.132  1.00 11.68 ?  4505 PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 30  ? 9.679   -11.356 13.874  1.00 13.25 ?  4505 PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 30  ? 7.853   -9.421  13.059  1.00 12.68 ?  4505 PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 30  ? 9.186   -10.446 14.787  1.00 15.69 ?  4505 PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 30  ? 8.278   -9.481  14.384  1.00 15.10 ?  4505 PHE A CZ  1 
ATOM   66   N  N   . MET A 1 31  ? 12.901  -13.100 10.122  1.00 11.36 ?  4506 MET A N   1 
ATOM   67   C  CA  . MET A 1 31  ? 13.613  -14.124 9.366   1.00 11.22 ?  4506 MET A CA  1 
ATOM   68   C  C   . MET A 1 31  ? 13.865  -15.256 10.347  1.00 10.55 ?  4506 MET A C   1 
ATOM   69   O  O   . MET A 1 31  ? 14.653  -15.094 11.289  1.00 10.31 ?  4506 MET A O   1 
ATOM   70   C  CB  . MET A 1 31  ? 14.933  -13.567 8.839   1.00 9.98  ?  4506 MET A CB  1 
ATOM   71   C  CG  . MET A 1 31  ? 14.775  -12.348 7.955   1.00 10.44 ?  4506 MET A CG  1 
ATOM   72   S  SD  . MET A 1 31  ? 16.303  -11.772 7.160   1.00 12.03 ?  4506 MET A SD  1 
ATOM   73   C  CE  . MET A 1 31  ? 17.341  -11.450 8.598   1.00 13.75 ?  4506 MET A CE  1 
ATOM   74   N  N   . VAL A 1 32  ? 13.222  -16.401 10.139  1.00 10.80 ?  4507 VAL A N   1 
ATOM   75   C  CA  . VAL A 1 32  ? 13.112  -17.431 11.164  1.00 11.30 ?  4507 VAL A CA  1 
ATOM   76   C  C   . VAL A 1 32  ? 13.766  -18.719 10.676  1.00 10.53 ?  4507 VAL A C   1 
ATOM   77   O  O   . VAL A 1 32  ? 13.296  -19.334 9.716   1.00 12.68 ?  4507 VAL A O   1 
ATOM   78   C  CB  . VAL A 1 32  ? 11.645  -17.667 11.547  1.00 10.80 ?  4507 VAL A CB  1 
ATOM   79   C  CG1 . VAL A 1 32  ? 11.568  -18.743 12.644  1.00 14.71 ?  4507 VAL A CG1 1 
ATOM   80   C  CG2 . VAL A 1 32  ? 11.006  -16.358 12.010  1.00 13.75 ?  4507 VAL A CG2 1 
ATOM   81   N  N   . ASP A 1 33  ? 14.816  -19.104 11.388  1.00 10.99 ?  4508 ASP A N   1 
ATOM   82   C  CA  . ASP A 1 33  ? 15.568  -20.339 11.105  1.00 11.76 ?  4508 ASP A CA  1 
ATOM   83   C  C   . ASP A 1 33  ? 14.747  -21.576 11.466  1.00 12.85 ?  4508 ASP A C   1 
ATOM   84   O  O   . ASP A 1 33  ? 14.324  -21.704 12.602  1.00 13.61 ?  4508 ASP A O   1 
ATOM   85   C  CB  . ASP A 1 33  ? 16.854  -20.257 11.905  1.00 13.00 ?  4508 ASP A CB  1 
ATOM   86   C  CG  . ASP A 1 33  ? 17.850  -21.397 11.814  1.00 14.75 ?  4508 ASP A CG  1 
ATOM   87   O  OD1 . ASP A 1 33  ? 17.491  -22.462 11.293  1.00 14.05 ?  4508 ASP A OD1 1 
ATOM   88   O  OD2 . ASP A 1 33  ? 18.974  -21.192 12.297  1.00 18.75 -1 4508 ASP A OD2 1 
ATOM   89   N  N   . SER A 1 34  ? 14.474  -22.408 10.479  1.00 10.87 ?  4509 SER A N   1 
ATOM   90   C  CA  . SER A 1 34  ? 13.869  -23.706 10.723  1.00 12.34 ?  4509 SER A CA  1 
ATOM   91   C  C   . SER A 1 34  ? 14.759  -24.832 10.222  1.00 11.09 ?  4509 SER A C   1 
ATOM   92   O  O   . SER A 1 34  ? 14.282  -25.872 9.766   1.00 11.21 ?  4509 SER A O   1 
ATOM   93   C  CB  . SER A 1 34  ? 12.470  -23.801 10.131  1.00 11.56 ?  4509 SER A CB  1 
ATOM   94   O  OG  . SER A 1 34  ? 12.531  -23.939 8.699   1.00 12.04 ?  4509 SER A OG  1 
ATOM   95   N  N   . SER A 1 35  ? 16.070  -24.653 10.371  1.00 11.85 ?  4510 SER A N   1 
ATOM   96   C  CA  . SER A 1 35  ? 17.025  -25.683 10.003  1.00 12.06 ?  4510 SER A CA  1 
ATOM   97   C  C   . SER A 1 35  ? 16.957  -26.854 10.981  1.00 14.27 ?  4510 SER A C   1 
ATOM   98   O  O   . SER A 1 35  ? 16.390  -26.759 12.073  1.00 14.23 ?  4510 SER A O   1 
ATOM   99   C  CB  . SER A 1 35  ? 18.448  -25.116 9.934   1.00 11.36 ?  4510 SER A CB  1 
ATOM   100  O  OG  . SER A 1 35  ? 18.952  -24.723 11.209  1.00 13.70 ?  4510 SER A OG  1 
ATOM   101  N  N   . GLY A 1 36  ? 17.564  -27.972 10.584  1.00 13.39 ?  4511 GLY A N   1 
ATOM   102  C  CA  . GLY A 1 36  ? 17.470  -29.186 11.384  1.00 12.65 ?  4511 GLY A CA  1 
ATOM   103  C  C   . GLY A 1 36  ? 18.111  -29.094 12.755  1.00 16.88 ?  4511 GLY A C   1 
ATOM   104  O  O   . GLY A 1 36  ? 17.782  -29.906 13.633  1.00 16.36 ?  4511 GLY A O   1 
ATOM   105  N  N   . SER A 1 37  ? 19.022  -28.135 12.965  1.00 14.72 ?  4512 SER A N   1 
ATOM   106  C  CA  . SER A 1 37  ? 19.600  -27.940 14.296  1.00 14.20 ?  4512 SER A CA  1 
ATOM   107  C  C   . SER A 1 37  ? 18.589  -27.411 15.312  1.00 13.18 ?  4512 SER A C   1 
ATOM   108  O  O   . SER A 1 37  ? 18.849  -27.513 16.517  1.00 15.57 ?  4512 SER A O   1 
ATOM   109  C  CB  . SER A 1 37  ? 20.822  -27.019 14.232  1.00 15.57 ?  4512 SER A CB  1 
ATOM   110  O  OG  . SER A 1 37  ? 20.505  -25.724 13.722  1.00 14.45 ?  4512 SER A OG  1 
ATOM   111  N  N   . ILE A 1 38  ? 17.474  -26.833 14.855  1.00 14.49 ?  4513 ILE A N   1 
ATOM   112  C  CA  . ILE A 1 38  ? 16.476  -26.286 15.777  1.00 14.71 ?  4513 ILE A CA  1 
ATOM   113  C  C   . ILE A 1 38  ? 15.822  -27.408 16.573  1.00 14.98 ?  4513 ILE A C   1 
ATOM   114  O  O   . ILE A 1 38  ? 15.767  -27.365 17.811  1.00 15.04 ?  4513 ILE A O   1 
ATOM   115  C  CB  . ILE A 1 38  ? 15.426  -25.467 15.000  1.00 15.35 ?  4513 ILE A CB  1 
ATOM   116  C  CG1 . ILE A 1 38  ? 16.071  -24.276 14.252  1.00 17.91 ?  4513 ILE A CG1 1 
ATOM   117  C  CG2 . ILE A 1 38  ? 14.283  -25.004 15.928  1.00 17.11 ?  4513 ILE A CG2 1 
ATOM   118  C  CD1 . ILE A 1 38  ? 16.378  -23.093 15.142  1.00 18.81 ?  4513 ILE A CD1 1 
ATOM   119  N  N   . GLY A 1 39  ? 15.307  -28.419 15.875  1.00 14.52 ?  4514 GLY A N   1 
ATOM   120  C  CA  . GLY A 1 39  ? 14.536  -29.495 16.492  1.00 13.91 ?  4514 GLY A CA  1 
ATOM   121  C  C   . GLY A 1 39  ? 13.078  -29.113 16.656  1.00 15.24 ?  4514 GLY A C   1 
ATOM   122  O  O   . GLY A 1 39  ? 12.715  -27.942 16.779  1.00 14.76 ?  4514 GLY A O   1 
ATOM   123  N  N   . SER A 1 40  ? 12.215  -30.127 16.648  1.00 14.11 ?  4515 SER A N   1 
ATOM   124  C  CA  . SER A 1 40  ? 10.781  -29.849 16.674  1.00 15.33 ?  4515 SER A CA  1 
ATOM   125  C  C   . SER A 1 40  ? 10.310  -29.233 17.988  1.00 17.71 ?  4515 SER A C   1 
ATOM   126  O  O   . SER A 1 40  ? 9.353   -28.457 17.973  1.00 17.11 ?  4515 SER A O   1 
ATOM   127  C  CB  . SER A 1 40  ? 9.981   -31.099 16.338  1.00 15.64 ?  4515 SER A CB  1 
ATOM   128  O  OG  . SER A 1 40  ? 10.234  -31.462 14.988  1.00 17.06 ?  4515 SER A OG  1 
ATOM   129  N  N   . SER A 1 41  ? 10.933  -29.566 19.124  1.00 15.22 ?  4516 SER A N   1 
ATOM   130  C  CA  . SER A 1 41  ? 10.496  -28.957 20.384  1.00 15.23 ?  4516 SER A CA  1 
ATOM   131  C  C   . SER A 1 41  ? 10.701  -27.453 20.357  1.00 16.86 ?  4516 SER A C   1 
ATOM   132  O  O   . SER A 1 41  ? 9.773   -26.680 20.620  1.00 16.47 ?  4516 SER A O   1 
ATOM   133  C  CB  . SER A 1 41  ? 11.258  -29.558 21.561  1.00 18.58 ?  4516 SER A CB  1 
ATOM   134  O  OG  . SER A 1 41  ? 10.694  -30.793 21.915  1.00 22.19 ?  4516 SER A OG  1 
ATOM   135  N  N   . ALA A 1 42  ? 11.922  -27.013 20.049  1.00 13.28 ?  4517 ALA A N   1 
ATOM   136  C  CA  . ALA A 1 42  ? 12.164  -25.579 19.972  1.00 12.82 ?  4517 ALA A CA  1 
ATOM   137  C  C   . ALA A 1 42  ? 11.331  -24.943 18.869  1.00 11.85 ?  4517 ALA A C   1 
ATOM   138  O  O   . ALA A 1 42  ? 10.848  -23.814 19.018  1.00 13.99 ?  4517 ALA A O   1 
ATOM   139  C  CB  . ALA A 1 42  ? 13.655  -25.302 19.759  1.00 15.03 ?  4517 ALA A CB  1 
ATOM   140  N  N   . MET A 1 43  ? 11.181  -25.636 17.738  1.00 12.95 ?  4518 MET A N   1 
ATOM   141  C  CA  . MET A 1 43  ? 10.423  -25.046 16.645  1.00 12.03 ?  4518 MET A CA  1 
ATOM   142  C  C   . MET A 1 43  ? 8.982   -24.803 17.066  1.00 12.90 ?  4518 MET A C   1 
ATOM   143  O  O   . MET A 1 43  ? 8.416   -23.748 16.773  1.00 13.49 ?  4518 MET A O   1 
ATOM   144  C  CB  . MET A 1 43  ? 10.468  -25.958 15.425  1.00 14.67 ?  4518 MET A CB  1 
ATOM   145  C  CG  . MET A 1 43  ? 9.870   -25.300 14.167  1.00 13.82 ?  4518 MET A CG  1 
ATOM   146  S  SD  . MET A 1 43  ? 11.078  -24.240 13.307  1.00 17.36 ?  4518 MET A SD  1 
ATOM   147  C  CE  . MET A 1 43  ? 10.745  -22.590 13.919  1.00 18.33 ?  4518 MET A CE  1 
ATOM   148  N  N   . ASN A 1 44  ? 8.396   -25.750 17.794  1.00 14.66 ?  4519 ASN A N   1 
ATOM   149  C  CA  . ASN A 1 44  ? 7.017   -25.578 18.241  1.00 15.58 ?  4519 ASN A CA  1 
ATOM   150  C  C   . ASN A 1 44  ? 6.892   -24.413 19.216  1.00 15.32 ?  4519 ASN A C   1 
ATOM   151  O  O   . ASN A 1 44  ? 5.954   -23.620 19.120  1.00 15.88 ?  4519 ASN A O   1 
ATOM   152  C  CB  . ASN A 1 44  ? 6.497   -26.888 18.821  1.00 16.51 ?  4519 ASN A CB  1 
ATOM   153  C  CG  . ASN A 1 44  ? 6.117   -27.857 17.736  1.00 23.40 ?  4519 ASN A CG  1 
ATOM   154  O  OD1 . ASN A 1 44  ? 5.611   -27.445 16.689  1.00 28.05 ?  4519 ASN A OD1 1 
ATOM   155  N  ND2 . ASN A 1 44  ? 6.372   -29.145 17.957  1.00 28.73 ?  4519 ASN A ND2 1 
ATOM   156  N  N   . THR A 1 45  ? 7.858   -24.263 20.120  1.00 14.70 ?  4520 THR A N   1 
ATOM   157  C  CA  . THR A 1 45  ? 7.838   -23.115 21.023  1.00 14.91 ?  4520 THR A CA  1 
ATOM   158  C  C   . THR A 1 45  ? 8.018   -21.816 20.250  1.00 13.54 ?  4520 THR A C   1 
ATOM   159  O  O   . THR A 1 45  ? 7.338   -20.821 20.520  1.00 14.91 ?  4520 THR A O   1 
ATOM   160  C  CB  . THR A 1 45  ? 8.941   -23.264 22.058  1.00 14.50 ?  4520 THR A CB  1 
ATOM   161  O  OG1 . THR A 1 45  ? 8.734   -24.480 22.782  1.00 17.56 ?  4520 THR A OG1 1 
ATOM   162  C  CG2 . THR A 1 45  ? 8.930   -22.090 23.019  1.00 15.51 ?  4520 THR A CG2 1 
ATOM   163  N  N   . ILE A 1 46  ? 8.956   -21.794 19.293  1.00 13.55 ?  4521 ILE A N   1 
ATOM   164  C  CA  . ILE A 1 46  ? 9.165   -20.602 18.477  1.00 13.66 ?  4521 ILE A CA  1 
ATOM   165  C  C   . ILE A 1 46  ? 7.873   -20.190 17.776  1.00 13.48 ?  4521 ILE A C   1 
ATOM   166  O  O   . ILE A 1 46  ? 7.531   -19.004 17.739  1.00 13.34 ?  4521 ILE A O   1 
ATOM   167  C  CB  . ILE A 1 46  ? 10.316  -20.842 17.488  1.00 13.42 ?  4521 ILE A CB  1 
ATOM   168  C  CG1 . ILE A 1 46  ? 11.649  -20.916 18.231  1.00 14.50 ?  4521 ILE A CG1 1 
ATOM   169  C  CG2 . ILE A 1 46  ? 10.332  -19.801 16.353  1.00 14.35 ?  4521 ILE A CG2 1 
ATOM   170  C  CD1 . ILE A 1 46  ? 12.733  -21.579 17.383  1.00 15.97 ?  4521 ILE A CD1 1 
ATOM   171  N  N   . LYS A 1 47  ? 7.159   -21.162 17.183  1.00 15.22 ?  4522 LYS A N   1 
ATOM   172  C  CA  . LYS A 1 47  ? 5.895   -20.863 16.507  1.00 15.25 ?  4522 LYS A CA  1 
ATOM   173  C  C   . LYS A 1 47  ? 4.883   -20.243 17.461  1.00 14.91 ?  4522 LYS A C   1 
ATOM   174  O  O   . LYS A 1 47  ? 4.195   -19.277 17.104  1.00 17.60 ?  4522 LYS A O   1 
ATOM   175  C  CB  . LYS A 1 47  ? 5.296   -22.130 15.911  1.00 16.18 ?  4522 LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 47  ? 6.044   -22.683 14.715  1.00 16.43 ?  4522 LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 47  ? 5.392   -23.990 14.333  1.00 20.27 ?  4522 LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 47  ? 6.175   -24.731 13.302  1.00 25.49 ?  4522 LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 47  ? 5.436   -25.945 12.857  1.00 30.23 ?  4522 LYS A NZ  1 
ATOM   180  N  N   . SER A 1 48  ? 4.766   -20.809 18.664  1.00 16.36 ?  4523 SER A N   1 
ATOM   181  C  CA  . SER A 1 48  ? 3.836   -20.284 19.658  1.00 16.03 ?  4523 SER A CA  1 
ATOM   182  C  C   . SER A 1 48  ? 4.242   -18.886 20.101  1.00 16.57 ?  4523 SER A C   1 
ATOM   183  O  O   . SER A 1 48  ? 3.404   -17.985 20.213  1.00 15.99 ?  4523 SER A O   1 
ATOM   184  C  CB  . SER A 1 48  ? 3.810   -21.225 20.858  1.00 17.08 ?  4523 SER A CB  1 
ATOM   185  O  OG  . SER A 1 48  ? 3.012   -20.682 21.903  1.00 28.69 ?  4523 SER A OG  1 
ATOM   186  N  N   . GLN A 1 49  ? 5.540   -18.672 20.328  1.00 13.90 ?  4524 GLN A N   1 
ATOM   187  C  CA  . GLN A 1 49  ? 5.997   -17.354 20.749  1.00 12.76 ?  4524 GLN A CA  1 
ATOM   188  C  C   . GLN A 1 49  ? 5.791   -16.308 19.661  1.00 12.37 ?  4524 GLN A C   1 
ATOM   189  O  O   . GLN A 1 49  ? 5.428   -15.168 19.955  1.00 13.45 ?  4524 GLN A O   1 
ATOM   190  C  CB  . GLN A 1 49  ? 7.476   -17.410 21.146  1.00 13.60 ?  4524 GLN A CB  1 
ATOM   191  C  CG  . GLN A 1 49  ? 7.754   -18.322 22.317  1.00 16.06 ?  4524 GLN A CG  1 
ATOM   192  C  CD  . GLN A 1 49  ? 7.526   -17.631 23.626  1.00 14.94 ?  4524 GLN A CD  1 
ATOM   193  O  OE1 . GLN A 1 49  ? 8.022   -16.523 23.855  1.00 16.17 ?  4524 GLN A OE1 1 
ATOM   194  N  NE2 . GLN A 1 49  ? 6.759   -18.271 24.496  1.00 20.41 ?  4524 GLN A NE2 1 
ATOM   195  N  N   . LEU A 1 50  ? 6.068   -16.654 18.400  1.00 13.36 ?  4525 LEU A N   1 
ATOM   196  C  CA  . LEU A 1 50  ? 5.898   -15.669 17.334  1.00 12.53 ?  4525 LEU A CA  1 
ATOM   197  C  C   . LEU A 1 50  ? 4.432   -15.305 17.134  1.00 13.53 ?  4525 LEU A C   1 
ATOM   198  O  O   . LEU A 1 50  ? 4.116   -14.135 16.879  1.00 13.19 ?  4525 LEU A O   1 
ATOM   199  C  CB  . LEU A 1 50  ? 6.490   -16.206 16.032  1.00 13.53 ?  4525 LEU A CB  1 
ATOM   200  C  CG  . LEU A 1 50  ? 8.021   -16.180 16.050  1.00 13.29 ?  4525 LEU A CG  1 
ATOM   201  C  CD1 . LEU A 1 50  ? 8.548   -16.886 14.811  1.00 14.57 ?  4525 LEU A CD1 1 
ATOM   202  C  CD2 . LEU A 1 50  ? 8.569   -14.771 16.200  1.00 16.22 ?  4525 LEU A CD2 1 
ATOM   203  N  N   . ALA A 1 51  ? 3.527   -16.284 17.258  1.00 14.01 ?  4526 ALA A N   1 
ATOM   204  C  CA  . ALA A 1 51  ? 2.102   -15.962 17.185  1.00 14.31 ?  4526 ALA A CA  1 
ATOM   205  C  C   . ALA A 1 51  ? 1.717   -14.970 18.278  1.00 16.49 ?  4526 ALA A C   1 
ATOM   206  O  O   . ALA A 1 51  ? 0.939   -14.044 18.034  1.00 17.67 ?  4526 ALA A O   1 
ATOM   207  C  CB  . ALA A 1 51  ? 1.255   -17.231 17.257  1.00 16.38 ?  4526 ALA A CB  1 
ATOM   208  N  N   . GLN A 1 52  ? 2.311   -15.105 19.467  1.00 15.94 ?  4527 GLN A N   1 
ATOM   209  C  CA  . GLN A 1 52  ? 2.059   -14.120 20.522  1.00 14.83 ?  4527 GLN A CA  1 
ATOM   210  C  C   . GLN A 1 52  ? 2.600   -12.752 20.147  1.00 17.12 ?  4527 GLN A C   1 
ATOM   211  O  O   . GLN A 1 52  ? 1.974   -11.723 20.435  1.00 16.86 ?  4527 GLN A O   1 
ATOM   212  C  CB  . GLN A 1 52  ? 2.687   -14.574 21.835  1.00 17.87 ?  4527 GLN A CB  1 
ATOM   213  C  CG  . GLN A 1 52  ? 1.997   -15.738 22.479  1.00 22.38 ?  4527 GLN A CG  1 
ATOM   214  C  CD  . GLN A 1 52  ? 2.794   -16.287 23.644  1.00 27.57 ?  4527 GLN A CD  1 
ATOM   215  O  OE1 . GLN A 1 52  ? 3.438   -15.531 24.376  1.00 31.68 ?  4527 GLN A OE1 1 
ATOM   216  N  NE2 . GLN A 1 52  ? 2.786   -17.613 23.802  1.00 28.57 ?  4527 GLN A NE2 1 
ATOM   217  N  N   . VAL A 1 53  ? 3.792   -12.708 19.543  1.00 13.84 ?  4528 VAL A N   1 
ATOM   218  C  CA  . VAL A 1 53  ? 4.327   -11.436 19.078  1.00 13.15 ?  4528 VAL A CA  1 
ATOM   219  C  C   . VAL A 1 53  ? 3.367   -10.790 18.084  1.00 13.78 ?  4528 VAL A C   1 
ATOM   220  O  O   . VAL A 1 53  ? 3.093   -9.587  18.152  1.00 15.11 ?  4528 VAL A O   1 
ATOM   221  C  CB  . VAL A 1 53  ? 5.722   -11.648 18.451  1.00 15.06 ?  4528 VAL A CB  1 
ATOM   222  C  CG1 . VAL A 1 53  ? 6.170   -10.407 17.692  1.00 18.32 ?  4528 VAL A CG1 1 
ATOM   223  C  CG2 . VAL A 1 53  ? 6.747   -12.041 19.525  1.00 16.27 ?  4528 VAL A CG2 1 
ATOM   224  N  N   . PHE A 1 54  ? 2.874   -11.578 17.123  1.00 15.29 ?  4529 PHE A N   1 
ATOM   225  C  CA  . PHE A 1 54  ? 2.047   -11.006 16.067  1.00 14.56 ?  4529 PHE A CA  1 
ATOM   226  C  C   . PHE A 1 54  ? 0.715   -10.524 16.626  1.00 14.48 ?  4529 PHE A C   1 
ATOM   227  O  O   . PHE A 1 54  ? 0.206   -9.481  16.206  1.00 15.48 ?  4529 PHE A O   1 
ATOM   228  C  CB  . PHE A 1 54  ? 1.824   -12.029 14.945  1.00 13.97 ?  4529 PHE A CB  1 
ATOM   229  C  CG  . PHE A 1 54  ? 3.093   -12.538 14.304  1.00 12.91 ?  4529 PHE A CG  1 
ATOM   230  C  CD1 . PHE A 1 54  ? 4.234   -11.754 14.221  1.00 14.04 ?  4529 PHE A CD1 1 
ATOM   231  C  CD2 . PHE A 1 54  ? 3.120   -13.804 13.762  1.00 12.16 ?  4529 PHE A CD2 1 
ATOM   232  C  CE1 . PHE A 1 54  ? 5.399   -12.255 13.618  1.00 14.33 ?  4529 PHE A CE1 1 
ATOM   233  C  CE2 . PHE A 1 54  ? 4.271   -14.302 13.184  1.00 13.82 ?  4529 PHE A CE2 1 
ATOM   234  C  CZ  . PHE A 1 54  ? 5.404   -13.532 13.114  1.00 15.35 ?  4529 PHE A CZ  1 
ATOM   235  N  N   . SER A 1 55  ? 0.176   -11.249 17.608  1.00 16.23 ?  4530 SER A N   1 
ATOM   236  C  CA  . SER A 1 55  ? -1.056  -10.824 18.261  1.00 17.63 ?  4530 SER A CA  1 
ATOM   237  C  C   . SER A 1 55  ? -0.849  -9.520  19.027  1.00 18.19 ?  4530 SER A C   1 
ATOM   238  O  O   . SER A 1 55  ? -1.700  -8.628  18.985  1.00 18.63 ?  4530 SER A O   1 
ATOM   239  C  CB  . SER A 1 55  ? -1.531  -11.935 19.188  1.00 19.83 ?  4530 SER A CB  1 
ATOM   240  O  OG  . SER A 1 55  ? -2.685  -11.527 19.907  1.00 27.84 ?  4530 SER A OG  1 
ATOM   241  N  N   . SER A 1 56  ? 0.290   -9.379  19.714  1.00 15.83 ?  4531 SER A N   1 
ATOM   242  C  CA  . SER A 1 56  ? 0.585   -8.124  20.403  1.00 17.25 ?  4531 SER A CA  1 
ATOM   243  C  C   . SER A 1 56  ? 0.697   -6.970  19.414  1.00 20.12 ?  4531 SER A C   1 
ATOM   244  O  O   . SER A 1 56  ? 0.144   -5.886  19.633  1.00 18.92 ?  4531 SER A O   1 
ATOM   245  C  CB  . SER A 1 56  ? 1.876   -8.267  21.215  1.00 18.28 ?  4531 SER A CB  1 
ATOM   246  O  OG  . SER A 1 56  ? 2.205   -7.044  21.868  1.00 22.18 ?  4531 SER A OG  1 
ATOM   247  N  N   . LEU A 1 57  ? 1.425   -7.187  18.314  1.00 16.19 ?  4532 LEU A N   1 
ATOM   248  C  CA  . LEU A 1 57  ? 1.600   -6.144  17.308  1.00 17.10 ?  4532 LEU A CA  1 
ATOM   249  C  C   . LEU A 1 57  ? 0.277   -5.785  16.646  1.00 16.78 ?  4532 LEU A C   1 
ATOM   250  O  O   . LEU A 1 57  ? 0.048   -4.618  16.307  1.00 19.39 ?  4532 LEU A O   1 
ATOM   251  C  CB  . LEU A 1 57  ? 2.605   -6.605  16.251  1.00 17.71 ?  4532 LEU A CB  1 
ATOM   252  C  CG  . LEU A 1 57  ? 4.046   -6.715  16.745  1.00 18.99 ?  4532 LEU A CG  1 
ATOM   253  C  CD1 . LEU A 1 57  ? 4.906   -7.338  15.673  1.00 16.61 ?  4532 LEU A CD1 1 
ATOM   254  C  CD2 . LEU A 1 57  ? 4.579   -5.341  17.079  1.00 22.23 ?  4532 LEU A CD2 1 
ATOM   255  N  N   . LYS A 1 58  ? -0.583  -6.781  16.431  1.00 18.11 ?  4533 LYS A N   1 
ATOM   256  C  CA  . LYS A 1 58  ? -1.930  -6.527  15.920  1.00 19.03 ?  4533 LYS A CA  1 
ATOM   257  C  C   . LYS A 1 58  ? -2.680  -5.569  16.839  1.00 19.42 ?  4533 LYS A C   1 
ATOM   258  O  O   . LYS A 1 58  ? -3.279  -4.588  16.383  1.00 22.01 ?  4533 LYS A O   1 
ATOM   259  C  CB  . LYS A 1 58  ? -2.675  -7.856  15.794  1.00 19.07 ?  4533 LYS A CB  1 
ATOM   260  C  CG  . LYS A 1 58  ? -4.157  -7.748  15.439  1.00 23.58 ?  4533 LYS A CG  1 
ATOM   261  C  CD  . LYS A 1 58  ? -4.371  -7.650  13.952  1.00 21.09 ?  4533 LYS A CD  1 
ATOM   262  C  CE  . LYS A 1 58  ? -5.861  -7.490  13.638  1.00 18.70 ?  4533 LYS A CE  1 
ATOM   263  N  NZ  . LYS A 1 58  ? -6.048  -7.463  12.180  1.00 21.38 ?  4533 LYS A NZ  1 
ATOM   264  N  N   . ALA A 1 59  ? -2.639  -5.833  18.145  1.00 19.02 ?  4534 ALA A N   1 
ATOM   265  C  CA  . ALA A 1 59  ? -3.316  -4.959  19.099  1.00 21.85 ?  4534 ALA A CA  1 
ATOM   266  C  C   . ALA A 1 59  ? -2.756  -3.543  19.038  1.00 24.95 ?  4534 ALA A C   1 
ATOM   267  O  O   . ALA A 1 59  ? -3.511  -2.564  18.994  1.00 28.33 ?  4534 ALA A O   1 
ATOM   268  C  CB  . ALA A 1 59  ? -3.196  -5.553  20.506  1.00 23.83 ?  4534 ALA A CB  1 
ATOM   269  N  N   . SER A 1 60  ? -1.429  -3.414  19.002  1.00 21.44 ?  4535 SER A N   1 
ATOM   270  C  CA  . SER A 1 60  ? -0.811  -2.093  18.908  1.00 25.67 ?  4535 SER A CA  1 
ATOM   271  C  C   . SER A 1 60  ? -1.214  -1.377  17.625  1.00 26.49 ?  4535 SER A C   1 
ATOM   272  O  O   . SER A 1 60  ? -1.454  -0.162  17.630  1.00 27.58 ?  4535 SER A O   1 
ATOM   273  C  CB  . SER A 1 60  ? 0.711   -2.225  18.987  1.00 28.04 ?  4535 SER A CB  1 
ATOM   274  O  OG  . SER A 1 60  ? 1.115   -2.736  20.246  1.00 32.79 ?  4535 SER A OG  1 
ATOM   275  N  N   . ALA A 1 61  ? -1.296  -2.114  16.513  1.00 22.41 ?  4536 ALA A N   1 
ATOM   276  C  CA  . ALA A 1 61  ? -1.646  -1.503  15.234  1.00 24.07 ?  4536 ALA A CA  1 
ATOM   277  C  C   . ALA A 1 61  ? -3.115  -1.106  15.166  1.00 26.21 ?  4536 ALA A C   1 
ATOM   278  O  O   . ALA A 1 61  ? -3.494  -0.323  14.287  1.00 25.20 ?  4536 ALA A O   1 
ATOM   279  C  CB  . ALA A 1 61  ? -1.318  -2.472  14.092  1.00 23.97 ?  4536 ALA A CB  1 
ATOM   280  N  N   . GLY A 1 62  ? -3.943  -1.628  16.061  1.00 25.53 ?  4537 GLY A N   1 
ATOM   281  C  CA  . GLY A 1 62  ? -5.352  -1.305  16.087  1.00 26.86 ?  4537 GLY A CA  1 
ATOM   282  C  C   . GLY A 1 62  ? -5.730  -0.183  17.021  1.00 31.48 ?  4537 GLY A C   1 
ATOM   283  O  O   . GLY A 1 62  ? -6.916  0.150   17.129  1.00 32.05 ?  4537 GLY A O   1 
ATOM   284  N  N   . THR A 1 63  ? -4.761  0.414   17.703  1.00 28.41 ?  4538 THR A N   1 
ATOM   285  C  CA  . THR A 1 63  ? -5.078  1.477   18.642  1.00 31.95 ?  4538 THR A CA  1 
ATOM   286  C  C   . THR A 1 63  ? -5.265  2.793   17.898  1.00 34.85 ?  4538 THR A C   1 
ATOM   287  O  O   . THR A 1 63  ? -4.855  2.949   16.746  1.00 34.79 ?  4538 THR A O   1 
ATOM   288  C  CB  . THR A 1 63  ? -3.981  1.609   19.700  1.00 33.67 ?  4538 THR A CB  1 
ATOM   289  O  OG1 . THR A 1 63  ? -2.736  1.918   19.065  1.00 36.45 ?  4538 THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 63  ? -3.834  0.313   20.469  1.00 33.66 ?  4538 THR A CG2 1 
ATOM   291  N  N   . ASP A 1 64  ? -5.902  3.746   18.573  1.00 35.39 ?  4539 ASP A N   1 
ATOM   292  C  CA  . ASP A 1 64  ? -6.193  5.035   17.958  1.00 38.15 ?  4539 ASP A CA  1 
ATOM   293  C  C   . ASP A 1 64  ? -4.902  5.780   17.642  1.00 32.83 ?  4539 ASP A C   1 
ATOM   294  O  O   . ASP A 1 64  ? -3.992  5.853   18.473  1.00 41.56 ?  4539 ASP A O   1 
ATOM   295  C  CB  . ASP A 1 64  ? -7.065  5.865   18.897  1.00 40.10 ?  4539 ASP A CB  1 
ATOM   296  C  CG  . ASP A 1 64  ? -8.522  5.460   18.841  1.00 46.45 ?  4539 ASP A CG  1 
ATOM   297  O  OD1 . ASP A 1 64  ? -9.232  5.930   17.927  1.00 50.36 ?  4539 ASP A OD1 1 
ATOM   298  O  OD2 . ASP A 1 64  ? -8.952  4.655   19.697  1.00 49.75 -1 4539 ASP A OD2 1 
ATOM   299  N  N   . GLY A 1 65  ? -4.823  6.331   16.434  1.00 36.94 ?  4540 GLY A N   1 
ATOM   300  C  CA  . GLY A 1 65  ? -3.642  7.042   16.000  1.00 36.37 ?  4540 GLY A CA  1 
ATOM   301  C  C   . GLY A 1 65  ? -2.476  6.176   15.576  1.00 35.77 ?  4540 GLY A C   1 
ATOM   302  O  O   . GLY A 1 65  ? -1.399  6.716   15.296  1.00 36.09 ?  4540 GLY A O   1 
ATOM   303  N  N   . ALA A 1 66  ? -2.645  4.857   15.517  1.00 35.81 ?  4541 ALA A N   1 
ATOM   304  C  CA  . ALA A 1 66  ? -1.552  3.988   15.101  1.00 31.89 ?  4541 ALA A CA  1 
ATOM   305  C  C   . ALA A 1 66  ? -1.235  4.196   13.627  1.00 31.18 ?  4541 ALA A C   1 
ATOM   306  O  O   . ALA A 1 66  ? -2.133  4.383   12.801  1.00 28.55 ?  4541 ALA A O   1 
ATOM   307  C  CB  . ALA A 1 66  ? -1.925  2.524   15.332  1.00 30.83 ?  4541 ALA A CB  1 
ATOM   308  N  N   . GLY A 1 67  ? 0.056   4.164   13.300  1.00 28.01 ?  4542 GLY A N   1 
ATOM   309  C  CA  . GLY A 1 67  ? 0.486   4.166   11.921  1.00 23.73 ?  4542 GLY A CA  1 
ATOM   310  C  C   . GLY A 1 67  ? 0.319   2.804   11.269  1.00 22.95 ?  4542 GLY A C   1 
ATOM   311  O  O   . GLY A 1 67  ? -0.205  1.856   11.852  1.00 27.45 ?  4542 GLY A O   1 
ATOM   312  N  N   . THR A 1 68  ? 0.773   2.721   10.022  1.00 20.68 ?  4543 THR A N   1 
ATOM   313  C  CA  . THR A 1 68  ? 0.679   1.488   9.251   1.00 22.83 ?  4543 THR A CA  1 
ATOM   314  C  C   . THR A 1 68  ? 1.817   0.555   9.636   1.00 19.86 ?  4543 THR A C   1 
ATOM   315  O  O   . THR A 1 68  ? 2.988   0.962   9.648   1.00 20.68 ?  4543 THR A O   1 
ATOM   316  C  CB  . THR A 1 68  ? 0.760   1.804   7.759   1.00 23.38 ?  4543 THR A CB  1 
ATOM   317  O  OG1 . THR A 1 68  ? -0.435  2.483   7.353   1.00 26.35 ?  4543 THR A OG1 1 
ATOM   318  C  CG2 . THR A 1 68  ? 0.906   0.529   6.939   1.00 20.82 ?  4543 THR A CG2 1 
ATOM   319  N  N   . VAL A 1 69  ? 1.472   -0.685  9.965   1.00 18.62 ?  4544 VAL A N   1 
ATOM   320  C  CA  . VAL A 1 69  ? 2.445   -1.704  10.351  1.00 17.38 ?  4544 VAL A CA  1 
ATOM   321  C  C   . VAL A 1 69  ? 2.338   -2.860  9.369   1.00 17.20 ?  4544 VAL A C   1 
ATOM   322  O  O   . VAL A 1 69  ? 1.348   -3.606  9.378   1.00 17.50 ?  4544 VAL A O   1 
ATOM   323  C  CB  . VAL A 1 69  ? 2.243   -2.202  11.784  1.00 18.30 ?  4544 VAL A CB  1 
ATOM   324  C  CG1 . VAL A 1 69  ? 3.310   -3.227  12.124  1.00 20.12 ?  4544 VAL A CG1 1 
ATOM   325  C  CG2 . VAL A 1 69  ? 2.303   -1.046  12.777  1.00 22.46 ?  4544 VAL A CG2 1 
ATOM   326  N  N   . ASN A 1 70  ? 3.352   -3.008  8.526   1.00 15.34 ?  4545 ASN A N   1 
ATOM   327  C  CA  . ASN A 1 70  ? 3.487   -4.174  7.665   1.00 14.43 ?  4545 ASN A CA  1 
ATOM   328  C  C   . ASN A 1 70  ? 4.414   -5.186  8.320   1.00 15.47 ?  4545 ASN A C   1 
ATOM   329  O  O   . ASN A 1 70  ? 5.464   -4.817  8.859   1.00 16.45 ?  4545 ASN A O   1 
ATOM   330  C  CB  . ASN A 1 70  ? 4.083   -3.784  6.312   1.00 15.69 ?  4545 ASN A CB  1 
ATOM   331  C  CG  . ASN A 1 70  ? 3.156   -2.921  5.500   1.00 17.27 ?  4545 ASN A CG  1 
ATOM   332  O  OD1 . ASN A 1 70  ? 1.965   -3.235  5.359   1.00 20.33 ?  4545 ASN A OD1 1 
ATOM   333  N  ND2 . ASN A 1 70  ? 3.679   -1.827  4.965   1.00 16.95 ?  4545 ASN A ND2 1 
ATOM   334  N  N   . ILE A 1 71  ? 4.020   -6.455  8.293   1.00 14.83 ?  4546 ILE A N   1 
ATOM   335  C  CA  . ILE A 1 71  ? 4.832   -7.546  8.822   1.00 13.87 ?  4546 ILE A CA  1 
ATOM   336  C  C   . ILE A 1 71  ? 5.194   -8.485  7.681   1.00 12.81 ?  4546 ILE A C   1 
ATOM   337  O  O   . ILE A 1 71  ? 4.316   -8.935  6.941   1.00 14.47 ?  4546 ILE A O   1 
ATOM   338  C  CB  . ILE A 1 71  ? 4.092   -8.328  9.922   1.00 14.92 ?  4546 ILE A CB  1 
ATOM   339  C  CG1 . ILE A 1 71  ? 3.635   -7.392  11.056  1.00 16.84 ?  4546 ILE A CG1 1 
ATOM   340  C  CG2 . ILE A 1 71  ? 4.954   -9.537  10.406  1.00 15.94 ?  4546 ILE A CG2 1 
ATOM   341  C  CD1 . ILE A 1 71  ? 4.752   -6.601  11.739  1.00 18.40 ?  4546 ILE A CD1 1 
ATOM   342  N  N   . PHE A 1 72  ? 6.475   -8.819  7.570   1.00 12.77 ?  4547 PHE A N   1 
ATOM   343  C  CA  . PHE A 1 72  ? 6.943   -9.835  6.644   1.00 11.83 ?  4547 PHE A CA  1 
ATOM   344  C  C   . PHE A 1 72  ? 7.494   -10.989 7.469   1.00 11.54 ?  4547 PHE A C   1 
ATOM   345  O  O   . PHE A 1 72  ? 8.248   -10.760 8.421   1.00 13.33 ?  4547 PHE A O   1 
ATOM   346  C  CB  . PHE A 1 72  ? 8.043   -9.245  5.757   1.00 13.17 ?  4547 PHE A CB  1 
ATOM   347  C  CG  . PHE A 1 72  ? 8.618   -10.211 4.755   1.00 13.18 ?  4547 PHE A CG  1 
ATOM   348  C  CD1 . PHE A 1 72  ? 7.904   -10.556 3.629   1.00 14.17 ?  4547 PHE A CD1 1 
ATOM   349  C  CD2 . PHE A 1 72  ? 9.892   -10.726 4.915   1.00 13.54 ?  4547 PHE A CD2 1 
ATOM   350  C  CE1 . PHE A 1 72  ? 8.429   -11.419 2.687   1.00 14.10 ?  4547 PHE A CE1 1 
ATOM   351  C  CE2 . PHE A 1 72  ? 10.423  -11.598 3.971   1.00 13.98 ?  4547 PHE A CE2 1 
ATOM   352  C  CZ  . PHE A 1 72  ? 9.694   -11.935 2.860   1.00 13.18 ?  4547 PHE A CZ  1 
ATOM   353  N  N   . LEU A 1 73  ? 7.117   -12.212 7.130   1.00 10.78 ?  4548 LEU A N   1 
ATOM   354  C  CA  . LEU A 1 73  ? 7.569   -13.397 7.842   1.00 11.04 ?  4548 LEU A CA  1 
ATOM   355  C  C   . LEU A 1 73  ? 8.092   -14.384 6.814   1.00 12.56 ?  4548 LEU A C   1 
ATOM   356  O  O   . LEU A 1 73  ? 7.400   -14.680 5.836   1.00 12.44 ?  4548 LEU A O   1 
ATOM   357  C  CB  . LEU A 1 73  ? 6.417   -14.050 8.622   1.00 11.33 ?  4548 LEU A CB  1 
ATOM   358  C  CG  . LEU A 1 73  ? 6.719   -15.396 9.271   1.00 10.60 ?  4548 LEU A CG  1 
ATOM   359  C  CD1 . LEU A 1 73  ? 7.886   -15.267 10.255  1.00 13.20 ?  4548 LEU A CD1 1 
ATOM   360  C  CD2 . LEU A 1 73  ? 5.481   -15.940 9.968   1.00 15.05 ?  4548 LEU A CD2 1 
ATOM   361  N  N   . VAL A 1 74  ? 9.323   -14.858 7.000   1.00 11.49 ?  4549 VAL A N   1 
ATOM   362  C  CA  . VAL A 1 74  ? 9.926   -15.825 6.084   1.00 10.83 ?  4549 VAL A CA  1 
ATOM   363  C  C   . VAL A 1 74  ? 10.554  -16.946 6.898   1.00 10.48 ?  4549 VAL A C   1 
ATOM   364  O  O   . VAL A 1 74  ? 11.315  -16.691 7.846   1.00 11.91 ?  4549 VAL A O   1 
ATOM   365  C  CB  . VAL A 1 74  ? 10.926  -15.174 5.107   1.00 10.74 ?  4549 VAL A CB  1 
ATOM   366  C  CG1 . VAL A 1 74  ? 12.039  -14.413 5.839   1.00 12.06 ?  4549 VAL A CG1 1 
ATOM   367  C  CG2 . VAL A 1 74  ? 11.518  -16.215 4.153   1.00 11.33 ?  4549 VAL A CG2 1 
ATOM   368  N  N   . ASP A 1 75  ? 10.233  -18.176 6.517   1.00 11.81 ?  4550 ASP A N   1 
ATOM   369  C  CA  . ASP A 1 75  ? 10.850  -19.378 7.042   1.00 12.31 ?  4550 ASP A CA  1 
ATOM   370  C  C   . ASP A 1 75  ? 12.062  -19.684 6.175   1.00 12.64 ?  4550 ASP A C   1 
ATOM   371  O  O   . ASP A 1 75  ? 11.991  -19.564 4.948   1.00 14.50 ?  4550 ASP A O   1 
ATOM   372  C  CB  . ASP A 1 75  ? 9.847   -20.519 6.860   1.00 14.98 ?  4550 ASP A CB  1 
ATOM   373  C  CG  . ASP A 1 75  ? 10.426  -21.864 7.196   1.00 15.11 ?  4550 ASP A CG  1 
ATOM   374  O  OD1 . ASP A 1 75  ? 11.194  -21.935 8.154   1.00 16.67 ?  4550 ASP A OD1 1 
ATOM   375  O  OD2 . ASP A 1 75  ? 10.109  -22.858 6.516   1.00 16.52 -1 4550 ASP A OD2 1 
ATOM   376  N  N   . PHE A 1 76  ? 13.170  -20.082 6.792   1.00 11.68 ?  4551 PHE A N   1 
ATOM   377  C  CA  . PHE A 1 76  ? 14.301  -20.478 5.955   1.00 12.19 ?  4551 PHE A CA  1 
ATOM   378  C  C   . PHE A 1 76  ? 15.044  -21.676 6.518   1.00 11.75 ?  4551 PHE A C   1 
ATOM   379  O  O   . PHE A 1 76  ? 15.126  -21.889 7.731   1.00 13.37 ?  4551 PHE A O   1 
ATOM   380  C  CB  . PHE A 1 76  ? 15.296  -19.334 5.683   1.00 11.80 ?  4551 PHE A CB  1 
ATOM   381  C  CG  . PHE A 1 76  ? 16.279  -19.090 6.802   1.00 12.00 ?  4551 PHE A CG  1 
ATOM   382  C  CD1 . PHE A 1 76  ? 15.926  -18.298 7.894   1.00 11.33 ?  4551 PHE A CD1 1 
ATOM   383  C  CD2 . PHE A 1 76  ? 17.569  -19.602 6.732   1.00 12.68 ?  4551 PHE A CD2 1 
ATOM   384  C  CE1 . PHE A 1 76  ? 16.838  -18.052 8.916   1.00 13.67 ?  4551 PHE A CE1 1 
ATOM   385  C  CE2 . PHE A 1 76  ? 18.483  -19.375 7.732   1.00 16.03 ?  4551 PHE A CE2 1 
ATOM   386  C  CZ  . PHE A 1 76  ? 18.134  -18.590 8.834   1.00 14.11 ?  4551 PHE A CZ  1 
ATOM   387  N  N   . ASP A 1 77  ? 15.607  -22.462 5.604   1.00 11.19 ?  4552 ASP A N   1 
ATOM   388  C  CA  . ASP A 1 77  ? 16.618  -23.432 5.981   1.00 12.83 ?  4552 ASP A CA  1 
ATOM   389  C  C   . ASP A 1 77  ? 17.624  -23.546 4.836   1.00 12.18 ?  4552 ASP A C   1 
ATOM   390  O  O   . ASP A 1 77  ? 18.429  -22.633 4.653   1.00 12.99 ?  4552 ASP A O   1 
ATOM   391  C  CB  . ASP A 1 77  ? 16.024  -24.771 6.492   1.00 11.92 ?  4552 ASP A CB  1 
ATOM   392  C  CG  . ASP A 1 77  ? 14.946  -25.345 5.577   1.00 13.95 ?  4552 ASP A CG  1 
ATOM   393  O  OD1 . ASP A 1 77  ? 15.285  -25.951 4.518   1.00 14.25 ?  4552 ASP A OD1 1 
ATOM   394  O  OD2 . ASP A 1 77  ? 13.744  -25.249 5.913   1.00 13.53 -1 4552 ASP A OD2 1 
ATOM   395  N  N   . THR A 1 78  ? 17.558  -24.610 4.038   1.00 12.32 ?  4553 THR A N   1 
ATOM   396  C  CA  . THR A 1 78  ? 18.467  -24.749 2.902   1.00 11.52 ?  4553 THR A CA  1 
ATOM   397  C  C   . THR A 1 78  ? 18.311  -23.582 1.946   1.00 10.76 ?  4553 THR A C   1 
ATOM   398  O  O   . THR A 1 78  ? 19.296  -23.103 1.372   1.00 12.96 ?  4553 THR A O   1 
ATOM   399  C  CB  . THR A 1 78  ? 18.171  -26.067 2.202   1.00 12.55 ?  4553 THR A CB  1 
ATOM   400  O  OG1 . THR A 1 78  ? 18.471  -27.130 3.096   1.00 14.62 ?  4553 THR A OG1 1 
ATOM   401  C  CG2 . THR A 1 78  ? 19.010  -26.241 0.935   1.00 14.55 ?  4553 THR A CG2 1 
ATOM   402  N  N   . LEU A 1 79  ? 17.075  -23.145 1.734   1.00 11.41 ?  4554 LEU A N   1 
ATOM   403  C  CA  . LEU A 1 79  ? 16.740  -21.882 1.110   1.00 12.08 ?  4554 LEU A CA  1 
ATOM   404  C  C   . LEU A 1 79  ? 15.647  -21.240 1.946   1.00 12.45 ?  4554 LEU A C   1 
ATOM   405  O  O   . LEU A 1 79  ? 15.062  -21.880 2.825   1.00 12.54 ?  4554 LEU A O   1 
ATOM   406  C  CB  . LEU A 1 79  ? 16.197  -22.107 -0.306  1.00 13.91 ?  4554 LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 79  ? 17.194  -22.667 -1.316  1.00 14.43 ?  4554 LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 79  ? 16.460  -23.110 -2.592  1.00 14.90 ?  4554 LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 79  ? 18.269  -21.631 -1.631  1.00 13.54 ?  4554 LEU A CD2 1 
ATOM   410  N  N   . ALA A 1 80  ? 15.369  -19.970 1.678   1.00 11.87 ?  4555 ALA A N   1 
ATOM   411  C  CA  . ALA A 1 80  ? 14.117  -19.403 2.146   1.00 11.15 ?  4555 ALA A CA  1 
ATOM   412  C  C   . ALA A 1 80  ? 12.961  -20.170 1.529   1.00 14.68 ?  4555 ALA A C   1 
ATOM   413  O  O   . ALA A 1 80  ? 12.987  -20.530 0.347   1.00 15.73 ?  4555 ALA A O   1 
ATOM   414  C  CB  . ALA A 1 80  ? 14.015  -17.921 1.783   1.00 13.23 ?  4555 ALA A CB  1 
ATOM   415  N  N   . ASN A 1 81  ? 11.955  -20.453 2.353   1.00 12.67 ?  4556 ASN A N   1 
ATOM   416  C  CA  . ASN A 1 81  ? 10.799  -21.241 1.939   1.00 12.45 ?  4556 ASN A CA  1 
ATOM   417  C  C   . ASN A 1 81  ? 9.622   -20.306 1.749   1.00 13.71 ?  4556 ASN A C   1 
ATOM   418  O  O   . ASN A 1 81  ? 9.710   -19.360 0.957   1.00 16.96 ?  4556 ASN A O   1 
ATOM   419  C  CB  . ASN A 1 81  ? 10.517  -22.323 2.974   1.00 14.79 ?  4556 ASN A CB  1 
ATOM   420  C  CG  . ASN A 1 81  ? 11.688  -23.253 3.142   1.00 16.28 ?  4556 ASN A CG  1 
ATOM   421  O  OD1 . ASN A 1 81  ? 12.292  -23.680 2.149   1.00 16.21 ?  4556 ASN A OD1 1 
ATOM   422  N  ND2 . ASN A 1 81  ? 12.043  -23.556 4.380   1.00 16.12 ?  4556 ASN A ND2 1 
ATOM   423  N  N   . LYS A 1 82  ? 8.520   -20.554 2.442   1.00 12.99 ?  4557 LYS A N   1 
ATOM   424  C  CA  . LYS A 1 82  ? 7.357   -19.701 2.287   1.00 14.59 ?  4557 LYS A CA  1 
ATOM   425  C  C   . LYS A 1 82  ? 7.548   -18.385 3.030   1.00 12.74 ?  4557 LYS A C   1 
ATOM   426  O  O   . LYS A 1 82  ? 8.261   -18.301 4.046   1.00 13.59 ?  4557 LYS A O   1 
ATOM   427  C  CB  . LYS A 1 82  ? 6.089   -20.408 2.773   1.00 17.89 ?  4557 LYS A CB  1 
ATOM   428  C  CG  . LYS A 1 82  ? 5.778   -21.658 1.937   1.00 16.93 ?  4557 LYS A CG  1 
ATOM   429  C  CD  . LYS A 1 82  ? 4.437   -22.273 2.278   1.00 26.37 ?  4557 LYS A CD  1 
ATOM   430  C  CE  . LYS A 1 82  ? 4.086   -23.368 1.274   1.00 32.84 ?  4557 LYS A CE  1 
ATOM   431  N  NZ  . LYS A 1 82  ? 2.970   -24.216 1.766   1.00 37.44 ?  4557 LYS A NZ  1 
ATOM   432  N  N   . SER A 1 83  ? 6.926   -17.349 2.493   1.00 12.22 ?  4558 SER A N   1 
ATOM   433  C  CA  . SER A 1 83  ? 6.932   -16.044 3.134   1.00 13.33 ?  4558 SER A CA  1 
ATOM   434  C  C   . SER A 1 83  ? 5.600   -15.355 2.876   1.00 14.04 ?  4558 SER A C   1 
ATOM   435  O  O   . SER A 1 83  ? 4.869   -15.703 1.937   1.00 15.42 ?  4558 SER A O   1 
ATOM   436  C  CB  . SER A 1 83  ? 8.091   -15.173 2.631   1.00 16.51 ?  4558 SER A CB  1 
ATOM   437  O  OG  . SER A 1 83  ? 7.977   -14.945 1.238   1.00 16.77 ?  4558 SER A OG  1 
ATOM   438  N  N   . VAL A 1 84  ? 5.290   -14.354 3.701   1.00 13.06 ?  4559 VAL A N   1 
ATOM   439  C  CA  . VAL A 1 84  ? 4.099   -13.549 3.470   1.00 13.18 ?  4559 VAL A CA  1 
ATOM   440  C  C   . VAL A 1 84  ? 4.325   -12.148 4.013   1.00 14.22 ?  4559 VAL A C   1 
ATOM   441  O  O   . VAL A 1 84  ? 5.079   -11.946 4.968   1.00 13.49 ?  4559 VAL A O   1 
ATOM   442  C  CB  . VAL A 1 84  ? 2.839   -14.197 4.081   1.00 15.76 ?  4559 VAL A CB  1 
ATOM   443  C  CG1 . VAL A 1 84  ? 2.810   -13.991 5.596   1.00 14.04 ?  4559 VAL A CG1 1 
ATOM   444  C  CG2 . VAL A 1 84  ? 1.591   -13.640 3.412   1.00 17.03 ?  4559 VAL A CG2 1 
ATOM   445  N  N   . SER A 1 85  ? 3.658   -11.184 3.396   1.00 13.18 ?  4560 SER A N   1 
ATOM   446  C  CA  . SER A 1 85  ? 3.631   -9.794  3.814   1.00 13.42 ?  4560 SER A CA  1 
ATOM   447  C  C   . SER A 1 85  ? 2.179   -9.423  4.115   1.00 13.99 ?  4560 SER A C   1 
ATOM   448  O  O   . SER A 1 85  ? 1.294   -9.656  3.281   1.00 17.14 ?  4560 SER A O   1 
ATOM   449  C  CB  . SER A 1 85  ? 4.131   -8.933  2.647   1.00 16.33 ?  4560 SER A CB  1 
ATOM   450  O  OG  . SER A 1 85  ? 4.050   -7.548  2.922   1.00 20.08 ?  4560 SER A OG  1 
ATOM   451  N  N   . VAL A 1 86  ? 1.934   -8.834  5.289   1.00 14.58 ?  4561 VAL A N   1 
ATOM   452  C  CA  . VAL A 1 86  ? 0.582   -8.460  5.702   1.00 13.88 ?  4561 VAL A CA  1 
ATOM   453  C  C   . VAL A 1 86  ? 0.584   -7.062  6.300   1.00 15.73 ?  4561 VAL A C   1 
ATOM   454  O  O   . VAL A 1 86  ? 1.580   -6.594  6.860   1.00 15.89 ?  4561 VAL A O   1 
ATOM   455  C  CB  . VAL A 1 86  ? -0.060  -9.437  6.716   1.00 14.06 ?  4561 VAL A CB  1 
ATOM   456  C  CG1 . VAL A 1 86  ? -0.045  -10.873 6.180   1.00 14.82 ?  4561 VAL A CG1 1 
ATOM   457  C  CG2 . VAL A 1 86  ? 0.627   -9.330  8.094   1.00 16.05 ?  4561 VAL A CG2 1 
ATOM   458  N  N   . ASN A 1 87  ? -0.564  -6.407  6.209   1.00 14.40 ?  4562 ASN A N   1 
ATOM   459  C  CA  . ASN A 1 87  ? -0.809  -5.150  6.897   1.00 14.08 ?  4562 ASN A CA  1 
ATOM   460  C  C   . ASN A 1 87  ? -1.717  -5.504  8.064   1.00 14.29 ?  4562 ASN A C   1 
ATOM   461  O  O   . ASN A 1 87  ? -2.759  -6.135  7.869   1.00 16.80 ?  4562 ASN A O   1 
ATOM   462  C  CB  . ASN A 1 87  ? -1.460  -4.149  5.936   1.00 14.36 ?  4562 ASN A CB  1 
ATOM   463  C  CG  . ASN A 1 87  ? -1.820  -2.824  6.596   1.00 15.26 ?  4562 ASN A CG  1 
ATOM   464  O  OD1 . ASN A 1 87  ? -2.336  -2.787  7.711   1.00 17.09 ?  4562 ASN A OD1 1 
ATOM   465  N  ND2 . ASN A 1 87  ? -1.583  -1.726  5.883   1.00 19.03 ?  4562 ASN A ND2 1 
ATOM   466  N  N   . LEU A 1 88  ? -1.290  -5.158  9.278   1.00 15.23 ?  4563 LEU A N   1 
ATOM   467  C  CA  . LEU A 1 88  ? -2.003  -5.620  10.464  1.00 15.48 ?  4563 LEU A CA  1 
ATOM   468  C  C   . LEU A 1 88  ? -3.406  -5.037  10.623  1.00 18.35 ?  4563 LEU A C   1 
ATOM   469  O  O   . LEU A 1 88  ? -4.151  -5.510  11.490  1.00 20.11 ?  4563 LEU A O   1 
ATOM   470  C  CB  . LEU A 1 88  ? -1.157  -5.384  11.713  1.00 16.02 ?  4563 LEU A CB  1 
ATOM   471  C  CG  . LEU A 1 88  ? 0.079   -6.274  11.829  1.00 17.97 ?  4563 LEU A CG  1 
ATOM   472  C  CD1 . LEU A 1 88  ? 0.864   -5.884  13.085  1.00 17.70 ?  4563 LEU A CD1 1 
ATOM   473  C  CD2 . LEU A 1 88  ? -0.295  -7.742  11.861  1.00 19.70 ?  4563 LEU A CD2 1 
ATOM   474  N  N   . LYS A 1 89  ? -3.796  -4.053  9.817   1.00 16.86 ?  4564 LYS A N   1 
ATOM   475  C  CA  . LYS A 1 89  ? -5.190  -3.611  9.825   1.00 17.79 ?  4564 LYS A CA  1 
ATOM   476  C  C   . LYS A 1 89  ? -6.129  -4.657  9.246   1.00 19.84 ?  4564 LYS A C   1 
ATOM   477  O  O   . LYS A 1 89  ? -7.325  -4.625  9.552   1.00 22.17 ?  4564 LYS A O   1 
ATOM   478  C  CB  . LYS A 1 89  ? -5.353  -2.341  8.999   1.00 18.55 ?  4564 LYS A CB  1 
ATOM   479  C  CG  . LYS A 1 89  ? -4.767  -1.092  9.609   1.00 24.51 ?  4564 LYS A CG  1 
ATOM   480  C  CD  . LYS A 1 89  ? -4.893  0.072   8.633   1.00 26.00 ?  4564 LYS A CD  1 
ATOM   481  C  CE  . LYS A 1 89  ? -4.564  1.414   9.286   1.00 33.80 ?  4564 LYS A CE  1 
ATOM   482  N  NZ  . LYS A 1 89  ? -3.110  1.684   9.357   1.00 33.54 ?  4564 LYS A NZ  1 
ATOM   483  N  N   . ASP A 1 90  ? -5.632  -5.575  8.419   1.00 16.56 ?  4565 ASP A N   1 
ATOM   484  C  CA  . ASP A 1 90  ? -6.511  -6.490  7.699   1.00 15.49 ?  4565 ASP A CA  1 
ATOM   485  C  C   . ASP A 1 90  ? -6.914  -7.677  8.569   1.00 15.68 ?  4565 ASP A C   1 
ATOM   486  O  O   . ASP A 1 90  ? -6.116  -8.185  9.362   1.00 17.57 ?  4565 ASP A O   1 
ATOM   487  C  CB  . ASP A 1 90  ? -5.824  -6.950  6.414   1.00 14.97 ?  4565 ASP A CB  1 
ATOM   488  C  CG  . ASP A 1 90  ? -5.692  -5.823  5.397   1.00 18.45 ?  4565 ASP A CG  1 
ATOM   489  O  OD1 . ASP A 1 90  ? -6.635  -4.996  5.277   1.00 18.87 ?  4565 ASP A OD1 1 
ATOM   490  O  OD2 . ASP A 1 90  ? -4.642  -5.750  4.719   1.00 18.98 -1 4565 ASP A OD2 1 
ATOM   491  N  N   . SER A 1 91  ? -8.165  -8.120  8.420   1.00 17.26 ?  4566 SER A N   1 
ATOM   492  C  CA  . SER A 1 91  ? -8.722  -9.117  9.328   1.00 15.38 ?  4566 SER A CA  1 
ATOM   493  C  C   . SER A 1 91  ? -8.245  -10.526 9.036   1.00 17.12 ?  4566 SER A C   1 
ATOM   494  O  O   . SER A 1 91  ? -8.633  -11.458 9.746   1.00 19.98 ?  4566 SER A O   1 
ATOM   495  C  CB  . SER A 1 91  ? -10.251 -9.105  9.243   1.00 17.98 ?  4566 SER A CB  1 
ATOM   496  O  OG  . SER A 1 91  ? -10.645 -9.497  7.939   1.00 22.00 ?  4566 SER A OG  1 
ATOM   497  N  N   . ASN A 1 92  ? -7.440  -10.730 7.996   1.00 15.72 ?  4567 ASN A N   1 
ATOM   498  C  CA  . ASN A 1 92  ? -6.825  -12.023 7.741   1.00 16.16 ?  4567 ASN A CA  1 
ATOM   499  C  C   . ASN A 1 92  ? -5.315  -11.969 7.927   1.00 13.86 ?  4567 ASN A C   1 
ATOM   500  O  O   . ASN A 1 92  ? -4.622  -12.916 7.543   1.00 16.04 ?  4567 ASN A O   1 
ATOM   501  C  CB  . ASN A 1 92  ? -7.177  -12.547 6.340   1.00 15.36 ?  4567 ASN A CB  1 
ATOM   502  C  CG  . ASN A 1 92  ? -6.640  -11.661 5.229   1.00 14.93 ?  4567 ASN A CG  1 
ATOM   503  O  OD1 . ASN A 1 92  ? -6.314  -10.496 5.447   1.00 18.09 ?  4567 ASN A OD1 1 
ATOM   504  N  ND2 . ASN A 1 92  ? -6.591  -12.209 4.015   1.00 20.38 ?  4567 ASN A ND2 1 
ATOM   505  N  N   . ALA A 1 93  ? -4.811  -10.888 8.527   1.00 12.95 ?  4568 ALA A N   1 
ATOM   506  C  CA  . ALA A 1 93  ? -3.361  -10.720 8.678   1.00 14.74 ?  4568 ALA A CA  1 
ATOM   507  C  C   . ALA A 1 93  ? -2.763  -11.828 9.533   1.00 15.25 ?  4568 ALA A C   1 
ATOM   508  O  O   . ALA A 1 93  ? -1.765  -12.457 9.154   1.00 14.89 ?  4568 ALA A O   1 
ATOM   509  C  CB  . ALA A 1 93  ? -3.052  -9.358  9.296   1.00 17.35 ?  4568 ALA A CB  1 
ATOM   510  N  N   . LEU A 1 94  ? -3.343  -12.067 10.710  1.00 13.49 ?  4569 LEU A N   1 
ATOM   511  C  CA  . LEU A 1 94  ? -2.790  -13.091 11.591  1.00 12.79 ?  4569 LEU A CA  1 
ATOM   512  C  C   . LEU A 1 94  ? -2.935  -14.484 11.000  1.00 15.28 ?  4569 LEU A C   1 
ATOM   513  O  O   . LEU A 1 94  ? -2.074  -15.343 11.227  1.00 15.62 ?  4569 LEU A O   1 
ATOM   514  C  CB  . LEU A 1 94  ? -3.387  -13.009 13.007  1.00 15.29 ?  4569 LEU A CB  1 
ATOM   515  C  CG  . LEU A 1 94  ? -3.113  -11.703 13.740  1.00 15.23 ?  4569 LEU A CG  1 
ATOM   516  C  CD1 . LEU A 1 94  ? -3.748  -11.699 15.110  1.00 17.04 ?  4569 LEU A CD1 1 
ATOM   517  C  CD2 . LEU A 1 94  ? -1.610  -11.478 13.865  1.00 17.72 ?  4569 LEU A CD2 1 
ATOM   518  N  N   . SER A 1 95  ? -3.999  -14.721 10.224  1.00 15.13 ?  4570 SER A N   1 
ATOM   519  C  CA  . SER A 1 95  ? -4.159  -16.017 9.576   1.00 13.11 ?  4570 SER A CA  1 
ATOM   520  C  C   . SER A 1 95  ? -3.074  -16.253 8.533   1.00 14.00 ?  4570 SER A C   1 
ATOM   521  O  O   . SER A 1 95  ? -2.573  -17.373 8.388   1.00 14.39 ?  4570 SER A O   1 
ATOM   522  C  CB  . SER A 1 95  ? -5.555  -16.137 8.955   1.00 17.76 ?  4570 SER A CB  1 
ATOM   523  O  OG  . SER A 1 95  ? -5.579  -17.144 7.970   1.00 23.70 ?  4570 SER A OG  1 
ATOM   524  N  N   . GLN A 1 96  ? -2.727  -15.218 7.777   1.00 13.89 ?  4571 GLN A N   1 
ATOM   525  C  CA  . GLN A 1 96  ? -1.689  -15.394 6.772   1.00 14.53 ?  4571 GLN A CA  1 
ATOM   526  C  C   . GLN A 1 96  ? -0.342  -15.642 7.421   1.00 13.76 ?  4571 GLN A C   1 
ATOM   527  O  O   . GLN A 1 96  ? 0.421   -16.487 6.949   1.00 14.27 ?  4571 GLN A O   1 
ATOM   528  C  CB  . GLN A 1 96  ? -1.630  -14.182 5.864   1.00 13.51 ?  4571 GLN A CB  1 
ATOM   529  C  CG  . GLN A 1 96  ? -2.848  -14.060 4.949   1.00 16.54 ?  4571 GLN A CG  1 
ATOM   530  C  CD  . GLN A 1 96  ? -2.485  -13.309 3.704   1.00 18.83 ?  4571 GLN A CD  1 
ATOM   531  O  OE1 . GLN A 1 96  ? -2.582  -12.086 3.653   1.00 25.67 ?  4571 GLN A OE1 1 
ATOM   532  N  NE2 . GLN A 1 96  ? -2.015  -14.037 2.699   1.00 21.42 ?  4571 GLN A NE2 1 
ATOM   533  N  N   . LEU A 1 97  ? -0.038  -14.914 8.501   1.00 13.41 ?  4572 LEU A N   1 
ATOM   534  C  CA  . LEU A 1 97  ? 1.189   -15.201 9.241   1.00 13.61 ?  4572 LEU A CA  1 
ATOM   535  C  C   . LEU A 1 97  ? 1.144   -16.600 9.828   1.00 13.01 ?  4572 LEU A C   1 
ATOM   536  O  O   . LEU A 1 97  ? 2.148   -17.318 9.807   1.00 14.38 ?  4572 LEU A O   1 
ATOM   537  C  CB  . LEU A 1 97  ? 1.360   -14.168 10.348  1.00 11.79 ?  4572 LEU A CB  1 
ATOM   538  C  CG  . LEU A 1 97  ? 1.612   -12.768 9.811   1.00 10.57 ?  4572 LEU A CG  1 
ATOM   539  C  CD1 . LEU A 1 97  ? 1.510   -11.770 10.935  1.00 13.82 ?  4572 LEU A CD1 1 
ATOM   540  C  CD2 . LEU A 1 97  ? 2.978   -12.670 9.122   1.00 13.16 ?  4572 LEU A CD2 1 
ATOM   541  N  N   . GLN A 1 98  ? -0.022  -17.013 10.345  1.00 12.84 ?  4573 GLN A N   1 
ATOM   542  C  CA  . GLN A 1 98  ? -0.138  -18.345 10.932  1.00 13.37 ?  4573 GLN A CA  1 
ATOM   543  C  C   . GLN A 1 98  ? 0.148   -19.442 9.913   1.00 15.57 ?  4573 GLN A C   1 
ATOM   544  O  O   . GLN A 1 98  ? 0.741   -20.473 10.254  1.00 15.47 ?  4573 GLN A O   1 
ATOM   545  C  CB  . GLN A 1 98  ? -1.531  -18.545 11.544  1.00 16.10 ?  4573 GLN A CB  1 
ATOM   546  C  CG  . GLN A 1 98  ? -1.593  -19.790 12.431  1.00 15.87 ?  4573 GLN A CG  1 
ATOM   547  C  CD  . GLN A 1 98  ? -0.672  -19.665 13.634  1.00 17.01 ?  4573 GLN A CD  1 
ATOM   548  O  OE1 . GLN A 1 98  ? -0.612  -18.612 14.267  1.00 19.31 ?  4573 GLN A OE1 1 
ATOM   549  N  NE2 . GLN A 1 98  ? 0.072   -20.725 13.928  1.00 20.28 ?  4573 GLN A NE2 1 
ATOM   550  N  N   . ALA A 1 99  ? -0.284  -19.254 8.661   1.00 14.59 ?  4574 ALA A N   1 
ATOM   551  C  CA  . ALA A 1 99  ? -0.015  -20.271 7.648   1.00 13.48 ?  4574 ALA A CA  1 
ATOM   552  C  C   . ALA A 1 99  ? 1.483   -20.436 7.434   1.00 15.07 ?  4574 ALA A C   1 
ATOM   553  O  O   . ALA A 1 99  ? 1.964   -21.553 7.202   1.00 15.62 ?  4574 ALA A O   1 
ATOM   554  C  CB  . ALA A 1 99  ? -0.711  -19.900 6.337   1.00 16.39 ?  4574 ALA A CB  1 
ATOM   555  N  N   . ILE A 1 100 ? 2.233   -19.337 7.496   1.00 13.76 ?  4575 ILE A N   1 
ATOM   556  C  CA  . ILE A 1 100 ? 3.686   -19.449 7.381   1.00 14.09 ?  4575 ILE A CA  1 
ATOM   557  C  C   . ILE A 1 100 ? 4.265   -20.174 8.589   1.00 14.81 ?  4575 ILE A C   1 
ATOM   558  O  O   . ILE A 1 100 ? 5.092   -21.078 8.440   1.00 15.92 ?  4575 ILE A O   1 
ATOM   559  C  CB  . ILE A 1 100 ? 4.356   -18.086 7.143   1.00 15.33 ?  4575 ILE A CB  1 
ATOM   560  C  CG1 . ILE A 1 100 ? 3.779   -17.375 5.921   1.00 16.11 ?  4575 ILE A CG1 1 
ATOM   561  C  CG2 . ILE A 1 100 ? 5.870   -18.279 6.987   1.00 17.20 ?  4575 ILE A CG2 1 
ATOM   562  C  CD1 . ILE A 1 100 ? 3.904   -18.136 4.618   1.00 19.04 ?  4575 ILE A CD1 1 
ATOM   563  N  N   . LEU A 1 101 ? 3.849   -19.787 9.803   1.00 12.51 ?  4576 LEU A N   1 
ATOM   564  C  CA  . LEU A 1 101 ? 4.318   -20.512 10.982  1.00 13.23 ?  4576 LEU A CA  1 
ATOM   565  C  C   . LEU A 1 101 ? 4.031   -22.001 10.860  1.00 14.54 ?  4576 LEU A C   1 
ATOM   566  O  O   . LEU A 1 101 ? 4.888   -22.835 11.160  1.00 16.69 ?  4576 LEU A O   1 
ATOM   567  C  CB  . LEU A 1 101 ? 3.674   -19.960 12.258  1.00 13.22 ?  4576 LEU A CB  1 
ATOM   568  C  CG  . LEU A 1 101 ? 3.956   -18.504 12.603  1.00 12.62 ?  4576 LEU A CG  1 
ATOM   569  C  CD1 . LEU A 1 101 ? 3.145   -18.075 13.832  1.00 15.32 ?  4576 LEU A CD1 1 
ATOM   570  C  CD2 . LEU A 1 101 ? 5.456   -18.289 12.868  1.00 16.37 ?  4576 LEU A CD2 1 
ATOM   571  N  N   . ASP A 1 102 ? 2.812   -22.354 10.427  1.00 15.07 ?  4577 ASP A N   1 
ATOM   572  C  CA  . ASP A 1 102 ? 2.435   -23.763 10.368  1.00 17.20 ?  4577 ASP A CA  1 
ATOM   573  C  C   . ASP A 1 102 ? 3.275   -24.531 9.360   1.00 18.79 ?  4577 ASP A C   1 
ATOM   574  O  O   . ASP A 1 102 ? 3.465   -25.744 9.509   1.00 20.79 ?  4577 ASP A O   1 
ATOM   575  C  CB  . ASP A 1 102 ? 0.947   -23.907 10.024  1.00 19.30 ?  4577 ASP A CB  1 
ATOM   576  C  CG  . ASP A 1 102 ? 0.034   -23.465 11.153  1.00 23.38 ?  4577 ASP A CG  1 
ATOM   577  O  OD1 . ASP A 1 102 ? 0.500   -23.347 12.302  1.00 23.41 ?  4577 ASP A OD1 1 
ATOM   578  O  OD2 . ASP A 1 102 ? -1.164  -23.245 10.869  1.00 26.96 -1 4577 ASP A OD2 1 
ATOM   579  N  N   . SER A 1 103 ? 3.784   -23.849 8.333   1.00 15.00 ?  4578 SER A N   1 
ATOM   580  C  CA  . SER A 1 103 ? 4.622   -24.494 7.328   1.00 15.18 ?  4578 SER A CA  1 
ATOM   581  C  C   . SER A 1 103 ? 6.034   -24.777 7.820   1.00 19.07 ?  4578 SER A C   1 
ATOM   582  O  O   . SER A 1 103 ? 6.772   -25.496 7.138   1.00 21.16 ?  4578 SER A O   1 
ATOM   583  C  CB  . SER A 1 103 ? 4.685   -23.652 6.041   1.00 17.40 ?  4578 SER A CB  1 
ATOM   584  O  OG  . SER A 1 103 ? 5.561   -22.548 6.188   1.00 17.04 ?  4578 SER A OG  1 
ATOM   585  N  N   . MET A 1 104 ? 6.432   -24.238 8.969   1.00 15.55 ?  4579 MET A N   1 
ATOM   586  C  CA  . MET A 1 104 ? 7.809   -24.382 9.417   1.00 16.85 ?  4579 MET A CA  1 
ATOM   587  C  C   . MET A 1 104 ? 8.043   -25.779 9.969   1.00 18.17 ?  4579 MET A C   1 
ATOM   588  O  O   . MET A 1 104 ? 7.336   -26.229 10.877  1.00 20.80 ?  4579 MET A O   1 
ATOM   589  C  CB  . MET A 1 104 ? 8.126   -23.354 10.495  1.00 17.02 ?  4579 MET A CB  1 
ATOM   590  C  CG  . MET A 1 104 ? 8.045   -21.931 9.992   1.00 14.85 ?  4579 MET A CG  1 
ATOM   591  S  SD  . MET A 1 104 ? 8.325   -20.794 11.353  1.00 20.67 ?  4579 MET A SD  1 
ATOM   592  C  CE  . MET A 1 104 ? 8.404   -19.266 10.449  1.00 19.33 ?  4579 MET A CE  1 
ATOM   593  N  N   . ASP A 1 105 ? 9.052   -26.449 9.439   1.00 16.58 ?  4580 ASP A N   1 
ATOM   594  C  CA  . ASP A 1 105 ? 9.479   -27.769 9.881   1.00 16.66 ?  4580 ASP A CA  1 
ATOM   595  C  C   . ASP A 1 105 ? 10.919  -27.601 10.345  1.00 15.07 ?  4580 ASP A C   1 
ATOM   596  O  O   . ASP A 1 105 ? 11.812  -27.337 9.523   1.00 13.66 ?  4580 ASP A O   1 
ATOM   597  C  CB  . ASP A 1 105 ? 9.368   -28.732 8.697   1.00 15.69 ?  4580 ASP A CB  1 
ATOM   598  C  CG  . ASP A 1 105 ? 9.993   -30.106 8.955   1.00 19.68 ?  4580 ASP A CG  1 
ATOM   599  O  OD1 . ASP A 1 105 ? 10.631  -30.357 9.994   1.00 17.78 ?  4580 ASP A OD1 1 
ATOM   600  O  OD2 . ASP A 1 105 ? 9.841   -30.963 8.056   1.00 26.59 -1 4580 ASP A OD2 1 
ATOM   601  N  N   . GLY A 1 106 ? 11.142  -27.745 11.656  1.00 13.11 ?  4581 GLY A N   1 
ATOM   602  C  CA  . GLY A 1 106 ? 12.461  -27.615 12.239  1.00 14.52 ?  4581 GLY A CA  1 
ATOM   603  C  C   . GLY A 1 106 ? 12.976  -28.936 12.779  1.00 15.05 ?  4581 GLY A C   1 
ATOM   604  O  O   . GLY A 1 106 ? 13.907  -28.973 13.598  1.00 14.72 ?  4581 GLY A O   1 
ATOM   605  N  N   . SER A 1 107 ? 12.415  -30.034 12.282  1.00 15.01 ?  4582 SER A N   1 
ATOM   606  C  CA  . SER A 1 107 ? 12.797  -31.333 12.812  1.00 16.07 ?  4582 SER A CA  1 
ATOM   607  C  C   . SER A 1 107 ? 14.244  -31.661 12.454  1.00 15.70 ?  4582 SER A C   1 
ATOM   608  O  O   . SER A 1 107 ? 14.788  -31.195 11.453  1.00 18.41 ?  4582 SER A O   1 
ATOM   609  C  CB  . SER A 1 107 ? 11.877  -32.421 12.270  1.00 15.75 ?  4582 SER A CB  1 
ATOM   610  O  OG  . SER A 1 107 ? 12.071  -32.634 10.880  1.00 19.15 ?  4582 SER A OG  1 
ATOM   611  N  N   . THR A 1 108 ? 14.867  -32.498 13.275  1.00 18.99 ?  4583 THR A N   1 
ATOM   612  C  CA  . THR A 1 108 ? 16.245  -32.886 12.991  1.00 20.03 ?  4583 THR A CA  1 
ATOM   613  C  C   . THR A 1 108 ? 16.368  -33.533 11.617  1.00 23.92 ?  4583 THR A C   1 
ATOM   614  O  O   . THR A 1 108 ? 17.325  -33.263 10.883  1.00 26.48 ?  4583 THR A O   1 
ATOM   615  C  CB  . THR A 1 108 ? 16.767  -33.829 14.078  1.00 23.88 ?  4583 THR A CB  1 
ATOM   616  O  OG1 . THR A 1 108 ? 16.030  -35.055 14.029  1.00 31.73 ?  4583 THR A OG1 1 
ATOM   617  C  CG2 . THR A 1 108 ? 16.596  -33.210 15.450  1.00 22.21 ?  4583 THR A CG2 1 
ATOM   618  N  N   . ASN A 1 109 ? 15.385  -34.342 11.223  1.00 19.99 ?  4584 ASN A N   1 
ATOM   619  C  CA  . ASN A 1 109 ? 15.531  -35.150 10.018  1.00 21.32 ?  4584 ASN A CA  1 
ATOM   620  C  C   . ASN A 1 109 ? 15.084  -34.455 8.733   1.00 25.15 ?  4584 ASN A C   1 
ATOM   621  O  O   . ASN A 1 109 ? 15.565  -34.820 7.653   1.00 23.35 ?  4584 ASN A O   1 
ATOM   622  C  CB  . ASN A 1 109 ? 14.820  -36.495 10.190  1.00 29.23 ?  4584 ASN A CB  1 
ATOM   623  C  CG  . ASN A 1 109 ? 13.378  -36.447 9.745   1.00 34.51 ?  4584 ASN A CG  1 
ATOM   624  O  OD1 . ASN A 1 109 ? 12.518  -35.882 10.429  1.00 42.97 ?  4584 ASN A OD1 1 
ATOM   625  N  ND2 . ASN A 1 109 ? 13.097  -37.051 8.584   1.00 37.35 ?  4584 ASN A ND2 1 
ATOM   626  N  N   . SER A 1 110 ? 14.176  -33.480 8.800   1.00 19.42 ?  4585 SER A N   1 
ATOM   627  C  CA  . SER A 1 110 ? 13.715  -32.805 7.591   1.00 19.71 ?  4585 SER A CA  1 
ATOM   628  C  C   . SER A 1 110 ? 13.737  -31.286 7.716   1.00 16.32 ?  4585 SER A C   1 
ATOM   629  O  O   . SER A 1 110 ? 13.180  -30.592 6.854   1.00 18.24 ?  4585 SER A O   1 
ATOM   630  C  CB  . SER A 1 110 ? 12.334  -33.300 7.136   1.00 25.26 ?  4585 SER A CB  1 
ATOM   631  O  OG  . SER A 1 110 ? 11.341  -33.115 8.129   1.00 25.17 ?  4585 SER A OG  1 
ATOM   632  N  N   . GLY A 1 111 ? 14.379  -30.756 8.758   1.00 16.44 ?  4586 GLY A N   1 
ATOM   633  C  CA  . GLY A 1 111 ? 14.416  -29.314 8.940   1.00 15.35 ?  4586 GLY A CA  1 
ATOM   634  C  C   . GLY A 1 111 ? 15.190  -28.590 7.853   1.00 13.79 ?  4586 GLY A C   1 
ATOM   635  O  O   . GLY A 1 111 ? 14.809  -27.493 7.442   1.00 13.00 ?  4586 GLY A O   1 
ATOM   636  N  N   . GLY A 1 112 ? 16.313  -29.162 7.411   1.00 14.42 ?  4587 GLY A N   1 
ATOM   637  C  CA  . GLY A 1 112 ? 17.101  -28.589 6.329   1.00 13.07 ?  4587 GLY A CA  1 
ATOM   638  C  C   . GLY A 1 112 ? 18.405  -27.968 6.816   1.00 14.69 ?  4587 GLY A C   1 
ATOM   639  O  O   . GLY A 1 112 ? 18.753  -28.017 7.997   1.00 13.89 ?  4587 GLY A O   1 
ATOM   640  N  N   . GLY A 1 113 ? 19.127  -27.360 5.859   1.00 15.02 ?  4588 GLY A N   1 
ATOM   641  C  CA  . GLY A 1 113 ? 20.383  -26.682 6.141   1.00 12.39 ?  4588 GLY A CA  1 
ATOM   642  C  C   . GLY A 1 113 ? 20.135  -25.252 6.599   1.00 13.07 ?  4588 GLY A C   1 
ATOM   643  O  O   . GLY A 1 113 ? 19.014  -24.876 6.914   1.00 13.07 ?  4588 GLY A O   1 
ATOM   644  N  N   . THR A 1 114 ? 21.195  -24.435 6.620   1.00 11.94 ?  4589 THR A N   1 
ATOM   645  C  CA  . THR A 1 114 ? 21.119  -23.099 7.236   1.00 11.63 ?  4589 THR A CA  1 
ATOM   646  C  C   . THR A 1 114 ? 21.689  -22.068 6.258   1.00 11.57 ?  4589 THR A C   1 
ATOM   647  O  O   . THR A 1 114 ? 22.891  -21.801 6.269   1.00 12.56 ?  4589 THR A O   1 
ATOM   648  C  CB  . THR A 1 114 ? 21.840  -23.067 8.604   1.00 10.94 ?  4589 THR A CB  1 
ATOM   649  O  OG1 . THR A 1 114 ? 21.482  -24.216 9.380   1.00 12.39 ?  4589 THR A OG1 1 
ATOM   650  C  CG2 . THR A 1 114 ? 21.468  -21.833 9.356   1.00 13.12 ?  4589 THR A CG2 1 
ATOM   651  N  N   . ASN A 1 115 ? 20.832  -21.443 5.459   1.00 10.89 ?  4590 ASN A N   1 
ATOM   652  C  CA  . ASN A 1 115 ? 21.284  -20.547 4.385   1.00 9.81  ?  4590 ASN A CA  1 
ATOM   653  C  C   . ASN A 1 115 ? 20.948  -19.104 4.750   1.00 12.39 ?  4590 ASN A C   1 
ATOM   654  O  O   . ASN A 1 115 ? 19.895  -18.578 4.376   1.00 11.83 ?  4590 ASN A O   1 
ATOM   655  C  CB  . ASN A 1 115 ? 20.655  -20.950 3.053   1.00 12.58 ?  4590 ASN A CB  1 
ATOM   656  C  CG  . ASN A 1 115 ? 21.365  -20.358 1.864   1.00 12.23 ?  4590 ASN A CG  1 
ATOM   657  O  OD1 . ASN A 1 115 ? 21.951  -19.291 1.941   1.00 12.39 ?  4590 ASN A OD1 1 
ATOM   658  N  ND2 . ASN A 1 115 ? 21.299  -21.071 0.736   1.00 12.12 ?  4590 ASN A ND2 1 
ATOM   659  N  N   . TYR A 1 116 ? 21.867  -18.454 5.464   1.00 11.16 ?  4591 TYR A N   1 
ATOM   660  C  CA  . TYR A 1 116 ? 21.694  -17.037 5.782   1.00 10.38 ?  4591 TYR A CA  1 
ATOM   661  C  C   . TYR A 1 116 ? 21.582  -16.203 4.515   1.00 12.14 ?  4591 TYR A C   1 
ATOM   662  O  O   . TYR A 1 116 ? 20.752  -15.289 4.432   1.00 12.13 ?  4591 TYR A O   1 
ATOM   663  C  CB  . TYR A 1 116 ? 22.891  -16.517 6.574   1.00 11.21 ?  4591 TYR A CB  1 
ATOM   664  C  CG  . TYR A 1 116 ? 23.006  -16.860 8.045   1.00 10.89 ?  4591 TYR A CG  1 
ATOM   665  C  CD1 . TYR A 1 116 ? 22.355  -17.956 8.628   1.00 12.03 ?  4591 TYR A CD1 1 
ATOM   666  C  CD2 . TYR A 1 116 ? 23.834  -16.085 8.847   1.00 10.69 ?  4591 TYR A CD2 1 
ATOM   667  C  CE1 . TYR A 1 116 ? 22.524  -18.243 9.991   1.00 11.82 ?  4591 TYR A CE1 1 
ATOM   668  C  CE2 . TYR A 1 116 ? 24.013  -16.366 10.188  1.00 11.89 ?  4591 TYR A CE2 1 
ATOM   669  C  CZ  . TYR A 1 116 ? 23.377  -17.446 10.747  1.00 13.33 ?  4591 TYR A CZ  1 
ATOM   670  O  OH  . TYR A 1 116 ? 23.562  -17.707 12.102  1.00 13.54 ?  4591 TYR A OH  1 
ATOM   671  N  N   . GLU A 1 117 ? 22.465  -16.448 3.536   1.00 11.19 ?  4592 GLU A N   1 
ATOM   672  C  CA  . GLU A 1 117 ? 22.506  -15.572 2.368   1.00 11.31 ?  4592 GLU A CA  1 
ATOM   673  C  C   . GLU A 1 117 ? 21.150  -15.523 1.678   1.00 10.17 ?  4592 GLU A C   1 
ATOM   674  O  O   . GLU A 1 117 ? 20.671  -14.454 1.300   1.00 11.35 ?  4592 GLU A O   1 
ATOM   675  C  CB  . GLU A 1 117 ? 23.586  -16.045 1.393   1.00 11.46 ?  4592 GLU A CB  1 
ATOM   676  C  CG  . GLU A 1 117 ? 23.733  -15.078 0.241   1.00 12.71 ?  4592 GLU A CG  1 
ATOM   677  C  CD  . GLU A 1 117 ? 24.762  -15.483 -0.794  1.00 14.34 ?  4592 GLU A CD  1 
ATOM   678  O  OE1 . GLU A 1 117 ? 25.514  -16.444 -0.584  1.00 12.91 ?  4592 GLU A OE1 1 
ATOM   679  O  OE2 . GLU A 1 117 ? 24.817  -14.788 -1.828  1.00 17.23 -1 4592 GLU A OE2 1 
ATOM   680  N  N   . ASP A 1 118 ? 20.544  -16.685 1.459   1.00 11.52 ?  4593 ASP A N   1 
ATOM   681  C  CA  . ASP A 1 118 ? 19.274  -16.695 0.744   1.00 10.44 ?  4593 ASP A CA  1 
ATOM   682  C  C   . ASP A 1 118 ? 18.170  -15.968 1.507   1.00 12.15 ?  4593 ASP A C   1 
ATOM   683  O  O   . ASP A 1 118 ? 17.362  -15.256 0.899   1.00 12.14 ?  4593 ASP A O   1 
ATOM   684  C  CB  . ASP A 1 118 ? 18.867  -18.111 0.368   1.00 11.41 ?  4593 ASP A CB  1 
ATOM   685  C  CG  . ASP A 1 118 ? 17.729  -18.126 -0.631  1.00 14.80 ?  4593 ASP A CG  1 
ATOM   686  O  OD1 . ASP A 1 118 ? 17.960  -17.805 -1.825  1.00 14.11 ?  4593 ASP A OD1 1 
ATOM   687  O  OD2 . ASP A 1 118 ? 16.589  -18.424 -0.220  1.00 15.44 -1 4593 ASP A OD2 1 
ATOM   688  N  N   . VAL A 1 119 ? 18.125  -16.114 2.834   1.00 10.80 ?  4594 VAL A N   1 
ATOM   689  C  CA  . VAL A 1 119 ? 17.051  -15.447 3.568   1.00 11.50 ?  4594 VAL A CA  1 
ATOM   690  C  C   . VAL A 1 119 ? 17.294  -13.942 3.619   1.00 11.46 ?  4594 VAL A C   1 
ATOM   691  O  O   . VAL A 1 119 ? 16.353  -13.151 3.532   1.00 10.94 ?  4594 VAL A O   1 
ATOM   692  C  CB  . VAL A 1 119 ? 16.771  -16.085 4.942   1.00 10.80 ?  4594 VAL A CB  1 
ATOM   693  C  CG1 . VAL A 1 119 ? 17.829  -15.722 5.973   1.00 13.34 ?  4594 VAL A CG1 1 
ATOM   694  C  CG2 . VAL A 1 119 ? 15.390  -15.621 5.445   1.00 12.51 ?  4594 VAL A CG2 1 
ATOM   695  N  N   . PHE A 1 120 ? 18.560  -13.528 3.719   1.00 10.53 ?  4595 PHE A N   1 
ATOM   696  C  CA  . PHE A 1 120 ? 18.863  -12.100 3.699   1.00 9.95  ?  4595 PHE A CA  1 
ATOM   697  C  C   . PHE A 1 120 ? 18.441  -11.473 2.368   1.00 11.85 ?  4595 PHE A C   1 
ATOM   698  O  O   . PHE A 1 120 ? 17.881  -10.365 2.334   1.00 11.69 ?  4595 PHE A O   1 
ATOM   699  C  CB  . PHE A 1 120 ? 20.366  -11.861 3.910   1.00 12.11 ?  4595 PHE A CB  1 
ATOM   700  C  CG  . PHE A 1 120 ? 20.901  -12.251 5.265   1.00 11.41 ?  4595 PHE A CG  1 
ATOM   701  C  CD1 . PHE A 1 120 ? 20.102  -12.322 6.399   1.00 12.40 ?  4595 PHE A CD1 1 
ATOM   702  C  CD2 . PHE A 1 120 ? 22.263  -12.503 5.394   1.00 11.00 ?  4595 PHE A CD2 1 
ATOM   703  C  CE1 . PHE A 1 120 ? 20.677  -12.687 7.652   1.00 12.33 ?  4595 PHE A CE1 1 
ATOM   704  C  CE2 . PHE A 1 120 ? 22.823  -12.848 6.613   1.00 11.83 ?  4595 PHE A CE2 1 
ATOM   705  C  CZ  . PHE A 1 120 ? 22.046  -12.919 7.738   1.00 12.65 ?  4595 PHE A CZ  1 
ATOM   706  N  N   . LYS A 1 121 ? 18.756  -12.145 1.249   1.00 11.77 ?  4596 LYS A N   1 
ATOM   707  C  CA  . LYS A 1 121 ? 18.376  -11.610 -0.061  1.00 10.44 ?  4596 LYS A CA  1 
ATOM   708  C  C   . LYS A 1 121 ? 16.871  -11.635 -0.264  1.00 9.90  ?  4596 LYS A C   1 
ATOM   709  O  O   . LYS A 1 121 ? 16.321  -10.701 -0.860  1.00 11.11 ?  4596 LYS A O   1 
ATOM   710  C  CB  . LYS A 1 121 ? 19.068  -12.391 -1.182  1.00 11.75 ?  4596 LYS A CB  1 
ATOM   711  C  CG  . LYS A 1 121 ? 20.569  -12.070 -1.290  1.00 12.59 ?  4596 LYS A CG  1 
ATOM   712  C  CD  . LYS A 1 121 ? 21.243  -12.963 -2.321  1.00 12.24 ?  4596 LYS A CD  1 
ATOM   713  C  CE  . LYS A 1 121 ? 22.588  -12.394 -2.735  1.00 16.72 ?  4596 LYS A CE  1 
ATOM   714  N  NZ  . LYS A 1 121 ? 23.320  -13.342 -3.645  1.00 15.56 ?  4596 LYS A NZ  1 
ATOM   715  N  N   . THR A 1 122 ? 16.206  -12.707 0.186   1.00 10.09 ?  4597 THR A N   1 
ATOM   716  C  CA  . THR A 1 122 ? 14.747  -12.749 0.125   1.00 10.70 ?  4597 THR A CA  1 
ATOM   717  C  C   . THR A 1 122 ? 14.141  -11.574 0.876   1.00 12.07 ?  4597 THR A C   1 
ATOM   718  O  O   . THR A 1 122 ? 13.215  -10.913 0.386   1.00 12.53 ?  4597 THR A O   1 
ATOM   719  C  CB  . THR A 1 122 ? 14.254  -14.065 0.718   1.00 11.44 ?  4597 THR A CB  1 
ATOM   720  O  OG1 . THR A 1 122 ? 14.663  -15.144 -0.123  1.00 13.58 ?  4597 THR A OG1 1 
ATOM   721  C  CG2 . THR A 1 122 ? 12.724  -14.087 0.798   1.00 14.22 ?  4597 THR A CG2 1 
ATOM   722  N  N   . THR A 1 123 ? 14.660  -11.291 2.073   1.00 12.08 ?  4598 THR A N   1 
ATOM   723  C  CA  . THR A 1 123 ? 14.121  -10.211 2.878   1.00 11.47 ?  4598 THR A CA  1 
ATOM   724  C  C   . THR A 1 123 ? 14.504  -8.849  2.309   1.00 11.33 ?  4598 THR A C   1 
ATOM   725  O  O   . THR A 1 123 ? 13.696  -7.912  2.330   1.00 12.36 ?  4598 THR A O   1 
ATOM   726  C  CB  . THR A 1 123 ? 14.591  -10.390 4.323   1.00 11.21 ?  4598 THR A CB  1 
ATOM   727  O  OG1 . THR A 1 123 ? 14.244  -11.712 4.777   1.00 11.37 ?  4598 THR A OG1 1 
ATOM   728  C  CG2 . THR A 1 123 ? 13.937  -9.367  5.231   1.00 13.18 ?  4598 THR A CG2 1 
ATOM   729  N  N   . ALA A 1 124 ? 15.732  -8.717  1.789   1.00 11.61 ?  4599 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 124 ? 16.080  -7.491  1.081   1.00 11.22 ?  4599 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 124 ? 15.128  -7.237  -0.084  1.00 12.88 ?  4599 ALA A C   1 
ATOM   732  O  O   . ALA A 1 124 ? 14.737  -6.091  -0.330  1.00 13.12 ?  4599 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 124 ? 17.541  -7.536  0.624   1.00 11.59 ?  4599 ALA A CB  1 
ATOM   734  N  N   . ASN A 1 125 ? 14.726  -8.299  -0.794  1.00 12.01 ?  4600 ASN A N   1 
ATOM   735  C  CA  . ASN A 1 125 ? 13.736  -8.133  -1.856  1.00 11.88 ?  4600 ASN A CA  1 
ATOM   736  C  C   . ASN A 1 125 ? 12.439  -7.542  -1.313  1.00 13.47 ?  4600 ASN A C   1 
ATOM   737  O  O   . ASN A 1 125 ? 11.832  -6.680  -1.952  1.00 14.98 ?  4600 ASN A O   1 
ATOM   738  C  CB  . ASN A 1 125 ? 13.459  -9.462  -2.566  1.00 12.67 ?  4600 ASN A CB  1 
ATOM   739  C  CG  . ASN A 1 125 ? 14.312  -9.668  -3.813  1.00 14.86 ?  4600 ASN A CG  1 
ATOM   740  O  OD1 . ASN A 1 125 ? 15.423  -9.145  -3.919  1.00 14.23 ?  4600 ASN A OD1 1 
ATOM   741  N  ND2 . ASN A 1 125 ? 13.796  -10.454 -4.764  1.00 14.98 ?  4600 ASN A ND2 1 
ATOM   742  N  N   . TRP A 1 126 ? 12.006  -7.979  -0.129  1.00 12.82 ?  4601 TRP A N   1 
ATOM   743  C  CA  . TRP A 1 126 ? 10.789  -7.398  0.443   1.00 11.78 ?  4601 TRP A CA  1 
ATOM   744  C  C   . TRP A 1 126 ? 10.976  -5.913  0.720   1.00 12.99 ?  4601 TRP A C   1 
ATOM   745  O  O   . TRP A 1 126 ? 10.079  -5.109  0.471   1.00 13.77 ?  4601 TRP A O   1 
ATOM   746  C  CB  . TRP A 1 126 ? 10.379  -8.119  1.731   1.00 12.08 ?  4601 TRP A CB  1 
ATOM   747  C  CG  . TRP A 1 126 ? 9.065   -7.600  2.260   1.00 12.61 ?  4601 TRP A CG  1 
ATOM   748  C  CD1 . TRP A 1 126 ? 7.860   -7.684  1.637   1.00 15.09 ?  4601 TRP A CD1 1 
ATOM   749  C  CD2 . TRP A 1 126 ? 8.831   -6.887  3.486   1.00 12.57 ?  4601 TRP A CD2 1 
ATOM   750  N  NE1 . TRP A 1 126 ? 6.889   -7.089  2.393   1.00 15.36 ?  4601 TRP A NE1 1 
ATOM   751  C  CE2 . TRP A 1 126 ? 7.448   -6.609  3.546   1.00 14.32 ?  4601 TRP A CE2 1 
ATOM   752  C  CE3 . TRP A 1 126 ? 9.646   -6.494  4.558   1.00 13.61 ?  4601 TRP A CE3 1 
ATOM   753  C  CZ2 . TRP A 1 126 ? 6.853   -5.943  4.628   1.00 14.23 ?  4601 TRP A CZ2 1 
ATOM   754  C  CZ3 . TRP A 1 126 ? 9.054   -5.834  5.642   1.00 13.36 ?  4601 TRP A CZ3 1 
ATOM   755  C  CH2 . TRP A 1 126 ? 7.672   -5.568  5.667   1.00 13.40 ?  4601 TRP A CH2 1 
ATOM   756  N  N   . PHE A 1 127 ? 12.156  -5.521  1.195   1.00 12.36 ?  4602 PHE A N   1 
ATOM   757  C  CA  . PHE A 1 127 ? 12.347  -4.097  1.436   1.00 12.99 ?  4602 PHE A CA  1 
ATOM   758  C  C   . PHE A 1 127 ? 12.458  -3.274  0.159   1.00 15.79 ?  4602 PHE A C   1 
ATOM   759  O  O   . PHE A 1 127 ? 12.396  -2.042  0.245   1.00 21.06 ?  4602 PHE A O   1 
ATOM   760  C  CB  . PHE A 1 127 ? 13.514  -3.877  2.413   1.00 14.58 ?  4602 PHE A CB  1 
ATOM   761  C  CG  . PHE A 1 127 ? 13.150  -4.163  3.843   1.00 13.72 ?  4602 PHE A CG  1 
ATOM   762  C  CD1 . PHE A 1 127 ? 12.424  -3.234  4.589   1.00 13.17 ?  4602 PHE A CD1 1 
ATOM   763  C  CD2 . PHE A 1 127 ? 13.507  -5.361  4.443   1.00 13.69 ?  4602 PHE A CD2 1 
ATOM   764  C  CE1 . PHE A 1 127 ? 12.080  -3.497  5.896   1.00 12.72 ?  4602 PHE A CE1 1 
ATOM   765  C  CE2 . PHE A 1 127 ? 13.163  -5.629  5.751   1.00 13.13 ?  4602 PHE A CE2 1 
ATOM   766  C  CZ  . PHE A 1 127 ? 12.442  -4.686  6.491   1.00 14.09 ?  4602 PHE A CZ  1 
ATOM   767  N  N   . ASN A 1 128 ? 12.594  -3.915  -1.000  1.00 13.17 ?  4603 ASN A N   1 
ATOM   768  C  CA  . ASN A 1 128 ? 12.478  -3.269  -2.305  1.00 16.28 ?  4603 ASN A CA  1 
ATOM   769  C  C   . ASN A 1 128 ? 11.049  -3.263  -2.837  1.00 17.52 ?  4603 ASN A C   1 
ATOM   770  O  O   . ASN A 1 128 ? 10.811  -2.711  -3.923  1.00 21.16 ?  4603 ASN A O   1 
ATOM   771  C  CB  . ASN A 1 128 ? 13.326  -4.027  -3.338  1.00 18.38 ?  4603 ASN A CB  1 
ATOM   772  C  CG  . ASN A 1 128 ? 14.778  -3.663  -3.288  1.00 21.08 ?  4603 ASN A CG  1 
ATOM   773  O  OD1 . ASN A 1 128 ? 15.216  -2.747  -3.988  1.00 24.13 ?  4603 ASN A OD1 1 
ATOM   774  N  ND2 . ASN A 1 128 ? 15.550  -4.384  -2.476  1.00 20.44 ?  4603 ASN A ND2 1 
ATOM   775  N  N   . SER A 1 129 ? 10.111  -3.888  -2.132  1.00 15.35 ?  4604 SER A N   1 
ATOM   776  C  CA  . SER A 1 129 ? 8.771   -4.149  -2.647  1.00 17.64 ?  4604 SER A CA  1 
ATOM   777  C  C   . SER A 1 129 ? 7.874   -2.923  -2.550  1.00 16.66 ?  4604 SER A C   1 
ATOM   778  O  O   . SER A 1 129 ? 8.124   -1.977  -1.796  1.00 15.61 ?  4604 SER A O   1 
ATOM   779  C  CB  . SER A 1 129 ? 8.107   -5.298  -1.884  1.00 16.81 ?  4604 SER A CB  1 
ATOM   780  O  OG  . SER A 1 129 ? 7.644   -4.862  -0.614  1.00 19.27 ?  4604 SER A OG  1 
ATOM   781  N  N   . SER A 1 130 ? 6.778   -2.974  -3.313  1.00 17.04 ?  4605 SER A N   1 
ATOM   782  C  CA  . SER A 1 130 ? 5.811   -1.881  -3.297  1.00 17.49 ?  4605 SER A CA  1 
ATOM   783  C  C   . SER A 1 130 ? 5.187   -1.693  -1.918  1.00 17.65 ?  4605 SER A C   1 
ATOM   784  O  O   . SER A 1 130 ? 4.894   -0.554  -1.528  1.00 18.62 ?  4605 SER A O   1 
ATOM   785  C  CB  . SER A 1 130 ? 4.736   -2.139  -4.354  1.00 18.47 ?  4605 SER A CB  1 
ATOM   786  O  OG  . SER A 1 130 ? 3.997   -3.297  -4.011  1.00 21.10 ?  4605 SER A OG  1 
ATOM   787  N  N   . THR A 1 131 ? 4.994   -2.786  -1.166  1.00 18.24 ?  4606 THR A N   1 
ATOM   788  C  CA  . THR A 1 131 ? 4.454   -2.693  0.189   1.00 19.07 ?  4606 THR A CA  1 
ATOM   789  C  C   . THR A 1 131 ? 5.331   -1.807  1.059   1.00 16.81 ?  4606 THR A C   1 
ATOM   790  O  O   . THR A 1 131 ? 4.840   -0.912  1.761   1.00 19.70 ?  4606 THR A O   1 
ATOM   791  C  CB  . THR A 1 131 ? 4.379   -4.092  0.801   1.00 18.52 ?  4606 THR A CB  1 
ATOM   792  O  OG1 . THR A 1 131 ? 3.367   -4.844  0.121   1.00 26.29 ?  4606 THR A OG1 1 
ATOM   793  C  CG2 . THR A 1 131 ? 4.058   -4.023  2.300   1.00 21.60 ?  4606 THR A CG2 1 
ATOM   794  N  N   . VAL A 1 132 ? 6.643   -2.038  1.014   1.00 15.53 ?  4607 VAL A N   1 
ATOM   795  C  CA  . VAL A 1 132 ? 7.551   -1.296  1.882   1.00 17.55 ?  4607 VAL A CA  1 
ATOM   796  C  C   . VAL A 1 132 ? 7.716   0.130   1.385   1.00 17.98 ?  4607 VAL A C   1 
ATOM   797  O  O   . VAL A 1 132 ? 7.654   1.089   2.168   1.00 17.63 ?  4607 VAL A O   1 
ATOM   798  C  CB  . VAL A 1 132 ? 8.896   -2.030  1.990   1.00 17.18 ?  4607 VAL A CB  1 
ATOM   799  C  CG1 . VAL A 1 132 ? 9.982   -1.080  2.496   1.00 19.79 ?  4607 VAL A CG1 1 
ATOM   800  C  CG2 . VAL A 1 132 ? 8.750   -3.243  2.892   1.00 16.68 ?  4607 VAL A CG2 1 
ATOM   801  N  N   . GLN A 1 133 ? 7.938   0.292   0.080   1.00 19.50 ?  4608 GLN A N   1 
ATOM   802  C  CA  . GLN A 1 133 ? 8.173   1.624   -0.462  1.00 21.66 ?  4608 GLN A CA  1 
ATOM   803  C  C   . GLN A 1 133 ? 6.943   2.507   -0.324  1.00 23.23 ?  4608 GLN A C   1 
ATOM   804  O  O   . GLN A 1 133 ? 7.073   3.727   -0.170  1.00 27.86 ?  4608 GLN A O   1 
ATOM   805  C  CB  . GLN A 1 133 ? 8.624   1.529   -1.921  1.00 23.32 ?  4608 GLN A CB  1 
ATOM   806  C  CG  . GLN A 1 133 ? 9.909   0.723   -2.130  1.00 26.46 ?  4608 GLN A CG  1 
ATOM   807  C  CD  . GLN A 1 133 ? 11.152  1.397   -1.556  1.00 33.26 ?  4608 GLN A CD  1 
ATOM   808  O  OE1 . GLN A 1 133 ? 11.415  2.571   -1.824  1.00 40.02 ?  4608 GLN A OE1 1 
ATOM   809  N  NE2 . GLN A 1 133 ? 11.925  0.652   -0.765  1.00 32.65 ?  4608 GLN A NE2 1 
ATOM   810  N  N   . GLY A 1 134 ? 5.750   1.914   -0.352  1.00 19.82 ?  4609 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 134 ? 4.527   2.685   -0.189  1.00 26.17 ?  4609 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 134 ? 4.243   3.133   1.229   1.00 27.50 ?  4609 GLY A C   1 
ATOM   813  O  O   . GLY A 1 134 ? 3.407   4.019   1.431   1.00 26.95 ?  4609 GLY A O   1 
ATOM   814  N  N   . ASN A 1 135 ? 4.905   2.533   2.219   1.00 21.87 ?  4610 ASN A N   1 
ATOM   815  C  CA  . ASN A 1 135 ? 4.708   2.880   3.627   1.00 20.35 ?  4610 ASN A CA  1 
ATOM   816  C  C   . ASN A 1 135 ? 5.749   3.937   3.965   1.00 25.66 ?  4610 ASN A C   1 
ATOM   817  O  O   . ASN A 1 135 ? 6.845   3.638   4.442   1.00 28.37 ?  4610 ASN A O   1 
ATOM   818  C  CB  . ASN A 1 135 ? 4.845   1.635   4.496   1.00 21.07 ?  4610 ASN A CB  1 
ATOM   819  C  CG  . ASN A 1 135 ? 4.322   1.839   5.908   1.00 22.15 ?  4610 ASN A CG  1 
ATOM   820  O  OD1 . ASN A 1 135 ? 3.621   2.817   6.192   1.00 22.27 ?  4610 ASN A OD1 1 
ATOM   821  N  ND2 . ASN A 1 135 ? 4.644   0.901   6.801   1.00 20.49 ?  4610 ASN A ND2 1 
ATOM   822  N  N   . THR A 1 136 ? 5.408   5.192   3.700   1.00 28.36 ?  4611 THR A N   1 
ATOM   823  C  CA  . THR A 1 136 ? 6.422   6.237   3.680   1.00 31.87 ?  4611 THR A CA  1 
ATOM   824  C  C   . THR A 1 136 ? 6.853   6.624   5.090   1.00 27.83 ?  4611 THR A C   1 
ATOM   825  O  O   . THR A 1 136 ? 6.095   6.501   6.056   1.00 27.67 ?  4611 THR A O   1 
ATOM   826  C  CB  . THR A 1 136 ? 5.898   7.463   2.937   1.00 31.35 ?  4611 THR A CB  1 
ATOM   827  O  OG1 . THR A 1 136 ? 4.710   7.932   3.583   1.00 36.63 ?  4611 THR A OG1 1 
ATOM   828  C  CG2 . THR A 1 136 ? 5.573   7.103   1.496   1.00 34.89 ?  4611 THR A CG2 1 
ATOM   829  N  N   . ASN A 1 137 ? 8.098   7.093   5.191   1.00 28.23 ?  4612 ASN A N   1 
ATOM   830  C  CA  . ASN A 1 137 ? 8.675   7.569   6.450   1.00 29.30 ?  4612 ASN A CA  1 
ATOM   831  C  C   . ASN A 1 137 ? 8.568   6.515   7.541   1.00 25.05 ?  4612 ASN A C   1 
ATOM   832  O  O   . ASN A 1 137 ? 8.301   6.811   8.706   1.00 28.51 ?  4612 ASN A O   1 
ATOM   833  C  CB  . ASN A 1 137 ? 8.071   8.903   6.894   1.00 31.62 ?  4612 ASN A CB  1 
ATOM   834  C  CG  . ASN A 1 137 ? 8.329   10.016  5.900   1.00 34.59 ?  4612 ASN A CG  1 
ATOM   835  O  OD1 . ASN A 1 137 ? 7.424   10.764  5.548   1.00 42.91 ?  4612 ASN A OD1 1 
ATOM   836  N  ND2 . ASN A 1 137 ? 9.568   10.123  5.433   1.00 36.24 ?  4612 ASN A ND2 1 
ATOM   837  N  N   . ALA A 1 138 ? 8.757   5.261   7.156   1.00 25.25 ?  4613 ALA A N   1 
ATOM   838  C  CA  . ALA A 1 138 ? 8.605   4.171   8.101   1.00 24.96 ?  4613 ALA A CA  1 
ATOM   839  C  C   . ALA A 1 138 ? 9.952   3.795   8.709   1.00 22.32 ?  4613 ALA A C   1 
ATOM   840  O  O   . ALA A 1 138 ? 11.012  4.031   8.126   1.00 24.64 ?  4613 ALA A O   1 
ATOM   841  C  CB  . ALA A 1 138 ? 7.981   2.952   7.413   1.00 23.13 ?  4613 ALA A CB  1 
ATOM   842  N  N   . LYS A 1 139 ? 9.885   3.209   9.899   1.00 20.29 ?  4614 LYS A N   1 
ATOM   843  C  CA  . LYS A 1 139 ? 11.024  2.526   10.502  1.00 21.43 ?  4614 LYS A CA  1 
ATOM   844  C  C   . LYS A 1 139 ? 11.073  1.112   9.937   1.00 21.00 ?  4614 LYS A C   1 
ATOM   845  O  O   . LYS A 1 139 ? 10.101  0.360   10.072  1.00 18.12 ?  4614 LYS A O   1 
ATOM   846  C  CB  . LYS A 1 139 ? 10.847  2.444   12.016  1.00 25.07 ?  4614 LYS A CB  1 
ATOM   847  C  CG  . LYS A 1 139 ? 10.957  3.767   12.769  1.00 31.96 ?  4614 LYS A CG  1 
ATOM   848  C  CD  . LYS A 1 139 ? 12.295  3.890   13.499  1.00 36.70 ?  4614 LYS A CD  1 
ATOM   849  C  CE  . LYS A 1 139 ? 12.327  5.111   14.421  1.00 37.08 ?  4614 LYS A CE  1 
ATOM   850  N  NZ  . LYS A 1 139 ? 11.603  4.876   15.707  1.00 39.69 ?  4614 LYS A NZ  1 
ATOM   851  N  N   . ASN A 1 140 ? 12.192  0.759   9.306   1.00 18.08 ?  4615 ASN A N   1 
ATOM   852  C  CA  . ASN A 1 140 ? 12.403  -0.561  8.718   1.00 16.95 ?  4615 ASN A CA  1 
ATOM   853  C  C   . ASN A 1 140 ? 13.195  -1.406  9.706   1.00 15.19 ?  4615 ASN A C   1 
ATOM   854  O  O   . ASN A 1 140 ? 14.354  -1.083  10.018  1.00 17.20 ?  4615 ASN A O   1 
ATOM   855  C  CB  . ASN A 1 140 ? 13.186  -0.437  7.412   1.00 17.85 ?  4615 ASN A CB  1 
ATOM   856  C  CG  . ASN A 1 140 ? 12.361  0.133   6.285   1.00 17.95 ?  4615 ASN A CG  1 
ATOM   857  O  OD1 . ASN A 1 140 ? 11.136  0.030   6.287   1.00 18.17 ?  4615 ASN A OD1 1 
ATOM   858  N  ND2 . ASN A 1 140 ? 13.036  0.695   5.282   1.00 25.51 ?  4615 ASN A ND2 1 
ATOM   859  N  N   . LEU A 1 141 ? 12.580  -2.475  10.197  1.00 14.46 ?  4616 LEU A N   1 
ATOM   860  C  CA  . LEU A 1 141 ? 13.165  -3.318  11.233  1.00 13.58 ?  4616 LEU A CA  1 
ATOM   861  C  C   . LEU A 1 141 ? 13.127  -4.762  10.774  1.00 14.89 ?  4616 LEU A C   1 
ATOM   862  O  O   . LEU A 1 141 ? 12.149  -5.197  10.164  1.00 16.60 ?  4616 LEU A O   1 
ATOM   863  C  CB  . LEU A 1 141 ? 12.370  -3.252  12.534  1.00 17.36 ?  4616 LEU A CB  1 
ATOM   864  C  CG  . LEU A 1 141 ? 12.166  -1.920  13.237  1.00 22.70 ?  4616 LEU A CG  1 
ATOM   865  C  CD1 . LEU A 1 141 ? 11.462  -2.174  14.560  1.00 26.09 ?  4616 LEU A CD1 1 
ATOM   866  C  CD2 . LEU A 1 141 ? 13.496  -1.217  13.459  1.00 25.72 ?  4616 LEU A CD2 1 
ATOM   867  N  N   . THR A 1 142 ? 14.162  -5.522  11.119  1.00 13.17 ?  4617 THR A N   1 
ATOM   868  C  CA  . THR A 1 142 ? 14.156  -6.962  10.899  1.00 13.04 ?  4617 THR A CA  1 
ATOM   869  C  C   . THR A 1 142 ? 14.654  -7.675  12.143  1.00 14.67 ?  4617 THR A C   1 
ATOM   870  O  O   . THR A 1 142 ? 15.673  -7.279  12.724  1.00 15.39 ?  4617 THR A O   1 
ATOM   871  C  CB  . THR A 1 142 ? 15.041  -7.314  9.703   1.00 13.07 ?  4617 THR A CB  1 
ATOM   872  O  OG1 . THR A 1 142 ? 14.469  -6.748  8.523   1.00 13.69 ?  4617 THR A OG1 1 
ATOM   873  C  CG2 . THR A 1 142 ? 15.121  -8.811  9.506   1.00 12.36 ?  4617 THR A CG2 1 
ATOM   874  N  N   . TYR A 1 143 ? 13.943  -8.728  12.536  1.00 11.87 ?  4618 TYR A N   1 
ATOM   875  C  CA  . TYR A 1 143 ? 14.380  -9.656  13.568  1.00 11.87 ?  4618 TYR A CA  1 
ATOM   876  C  C   . TYR A 1 143 ? 14.936  -10.900 12.895  1.00 13.85 ?  4618 TYR A C   1 
ATOM   877  O  O   . TYR A 1 143 ? 14.251  -11.521 12.080  1.00 14.85 ?  4618 TYR A O   1 
ATOM   878  C  CB  . TYR A 1 143 ? 13.197  -10.034 14.462  1.00 11.57 ?  4618 TYR A CB  1 
ATOM   879  C  CG  . TYR A 1 143 ? 12.775  -8.867  15.303  1.00 12.54 ?  4618 TYR A CG  1 
ATOM   880  C  CD1 . TYR A 1 143 ? 13.386  -8.615  16.537  1.00 13.89 ?  4618 TYR A CD1 1 
ATOM   881  C  CD2 . TYR A 1 143 ? 11.789  -7.986  14.854  1.00 13.68 ?  4618 TYR A CD2 1 
ATOM   882  C  CE1 . TYR A 1 143 ? 13.024  -7.509  17.301  1.00 14.99 ?  4618 TYR A CE1 1 
ATOM   883  C  CE2 . TYR A 1 143 ? 11.422  -6.887  15.609  1.00 16.31 ?  4618 TYR A CE2 1 
ATOM   884  C  CZ  . TYR A 1 143 ? 12.037  -6.662  16.832  1.00 15.90 ?  4618 TYR A CZ  1 
ATOM   885  O  OH  . TYR A 1 143 ? 11.664  -5.564  17.573  1.00 19.47 ?  4618 TYR A OH  1 
ATOM   886  N  N   . PHE A 1 144 ? 16.180  -11.258 13.221  1.00 11.99 ?  4619 PHE A N   1 
ATOM   887  C  CA  . PHE A 1 144 ? 16.838  -12.432 12.657  1.00 12.71 ?  4619 PHE A CA  1 
ATOM   888  C  C   . PHE A 1 144 ? 16.967  -13.421 13.802  1.00 11.80 ?  4619 PHE A C   1 
ATOM   889  O  O   . PHE A 1 144 ? 17.682  -13.153 14.771  1.00 13.53 ?  4619 PHE A O   1 
ATOM   890  C  CB  . PHE A 1 144 ? 18.212  -12.010 12.153  1.00 12.99 ?  4619 PHE A CB  1 
ATOM   891  C  CG  . PHE A 1 144 ? 19.047  -13.120 11.580  1.00 12.48 ?  4619 PHE A CG  1 
ATOM   892  C  CD1 . PHE A 1 144 ? 18.473  -14.180 10.902  1.00 14.04 ?  4619 PHE A CD1 1 
ATOM   893  C  CD2 . PHE A 1 144 ? 20.432  -13.072 11.706  1.00 13.80 ?  4619 PHE A CD2 1 
ATOM   894  C  CE1 . PHE A 1 144 ? 19.270  -15.185 10.343  1.00 14.17 ?  4619 PHE A CE1 1 
ATOM   895  C  CE2 . PHE A 1 144 ? 21.235  -14.066 11.164  1.00 14.51 ?  4619 PHE A CE2 1 
ATOM   896  C  CZ  . PHE A 1 144 ? 20.658  -15.121 10.483  1.00 13.20 ?  4619 PHE A CZ  1 
ATOM   897  N  N   . ILE A 1 145 ? 16.295  -14.553 13.706  1.00 11.12 ?  4620 ILE A N   1 
ATOM   898  C  CA  . ILE A 1 145 ? 16.165  -15.491 14.809  1.00 11.37 ?  4620 ILE A CA  1 
ATOM   899  C  C   . ILE A 1 145 ? 16.804  -16.806 14.379  1.00 11.91 ?  4620 ILE A C   1 
ATOM   900  O  O   . ILE A 1 145 ? 16.295  -17.480 13.478  1.00 13.75 ?  4620 ILE A O   1 
ATOM   901  C  CB  . ILE A 1 145 ? 14.693  -15.692 15.183  1.00 12.49 ?  4620 ILE A CB  1 
ATOM   902  C  CG1 . ILE A 1 145 ? 14.073  -14.353 15.578  1.00 14.70 ?  4620 ILE A CG1 1 
ATOM   903  C  CG2 . ILE A 1 145 ? 14.585  -16.669 16.340  1.00 14.78 ?  4620 ILE A CG2 1 
ATOM   904  C  CD1 . ILE A 1 145 ? 12.555  -14.328 15.486  1.00 15.61 ?  4620 ILE A CD1 1 
ATOM   905  N  N   . THR A 1 146 ? 17.899  -17.193 15.034  1.00 11.91 ?  4621 THR A N   1 
ATOM   906  C  CA  . THR A 1 146 ? 18.667  -18.349 14.593  1.00 11.89 ?  4621 THR A CA  1 
ATOM   907  C  C   . THR A 1 146 ? 19.297  -19.062 15.783  1.00 12.78 ?  4621 THR A C   1 
ATOM   908  O  O   . THR A 1 146 ? 19.530  -18.463 16.831  1.00 12.68 ?  4621 THR A O   1 
ATOM   909  C  CB  . THR A 1 146 ? 19.738  -17.914 13.570  1.00 13.90 ?  4621 THR A CB  1 
ATOM   910  O  OG1 . THR A 1 146 ? 20.456  -19.070 13.094  1.00 13.37 ?  4621 THR A OG1 1 
ATOM   911  C  CG2 . THR A 1 146 ? 20.697  -16.884 14.158  1.00 15.85 ?  4621 THR A CG2 1 
ATOM   912  N  N   . ASP A 1 147 ? 19.566  -20.362 15.613  1.00 12.95 ?  4622 ASP A N   1 
ATOM   913  C  CA  . ASP A 1 147 ? 20.251  -21.149 16.629  1.00 13.86 ?  4622 ASP A CA  1 
ATOM   914  C  C   . ASP A 1 147 ? 21.620  -21.644 16.185  1.00 14.05 ?  4622 ASP A C   1 
ATOM   915  O  O   . ASP A 1 147 ? 22.241  -22.427 16.905  1.00 15.96 ?  4622 ASP A O   1 
ATOM   916  C  CB  . ASP A 1 147 ? 19.373  -22.291 17.167  1.00 12.59 ?  4622 ASP A CB  1 
ATOM   917  C  CG  . ASP A 1 147 ? 19.522  -23.606 16.414  1.00 18.41 ?  4622 ASP A CG  1 
ATOM   918  O  OD1 . ASP A 1 147 ? 19.821  -23.589 15.210  1.00 17.98 ?  4622 ASP A OD1 1 
ATOM   919  O  OD2 . ASP A 1 147 ? 19.335  -24.675 17.043  1.00 19.18 -1 4622 ASP A OD2 1 
ATOM   920  N  N   . GLY A 1 148 ? 22.130  -21.203 15.037  1.00 14.13 ?  4623 GLY A N   1 
ATOM   921  C  CA  . GLY A 1 148 ? 23.403  -21.752 14.604  1.00 13.96 ?  4623 GLY A CA  1 
ATOM   922  C  C   . GLY A 1 148 ? 23.961  -21.006 13.421  1.00 13.14 ?  4623 GLY A C   1 
ATOM   923  O  O   . GLY A 1 148 ? 23.260  -20.239 12.758  1.00 13.76 ?  4623 GLY A O   1 
ATOM   924  N  N   . GLN A 1 149 ? 25.248  -21.246 13.175  1.00 12.13 ?  4624 GLN A N   1 
ATOM   925  C  CA  . GLN A 1 149 ? 25.965  -20.640 12.059  1.00 13.68 ?  4624 GLN A CA  1 
ATOM   926  C  C   . GLN A 1 149 ? 25.437  -21.136 10.719  1.00 12.78 ?  4624 GLN A C   1 
ATOM   927  O  O   . GLN A 1 149 ? 24.849  -22.217 10.625  1.00 14.36 ?  4624 GLN A O   1 
ATOM   928  C  CB  . GLN A 1 149 ? 27.440  -21.004 12.153  1.00 15.91 ?  4624 GLN A CB  1 
ATOM   929  C  CG  . GLN A 1 149 ? 28.175  -20.295 13.258  1.00 16.70 ?  4624 GLN A CG  1 
ATOM   930  C  CD  . GLN A 1 149 ? 29.592  -20.790 13.332  1.00 24.16 ?  4624 GLN A CD  1 
ATOM   931  O  OE1 . GLN A 1 149 ? 29.858  -21.846 13.896  1.00 33.20 ?  4624 GLN A OE1 1 
ATOM   932  N  NE2 . GLN A 1 149 ? 30.506  -20.052 12.726  1.00 22.05 ?  4624 GLN A NE2 1 
ATOM   933  N  N   . PRO A 1 150 ? 25.681  -20.383 9.654   1.00 12.76 ?  4625 PRO A N   1 
ATOM   934  C  CA  . PRO A 1 150 ? 25.229  -20.831 8.337   1.00 11.77 ?  4625 PRO A CA  1 
ATOM   935  C  C   . PRO A 1 150 ? 26.020  -22.037 7.864   1.00 12.50 ?  4625 PRO A C   1 
ATOM   936  O  O   . PRO A 1 150 ? 27.210  -22.182 8.156   1.00 13.39 ?  4625 PRO A O   1 
ATOM   937  C  CB  . PRO A 1 150 ? 25.504  -19.617 7.447   1.00 13.32 ?  4625 PRO A CB  1 
ATOM   938  C  CG  . PRO A 1 150 ? 26.668  -18.944 8.103   1.00 13.38 ?  4625 PRO A CG  1 
ATOM   939  C  CD  . PRO A 1 150 ? 26.369  -19.082 9.589   1.00 12.45 ?  4625 PRO A CD  1 
ATOM   940  N  N   . THR A 1 151 ? 25.341  -22.898 7.107   1.00 11.40 ?  4626 THR A N   1 
ATOM   941  C  CA  . THR A 1 151 ? 25.934  -24.101 6.538   1.00 13.12 ?  4626 THR A CA  1 
ATOM   942  C  C   . THR A 1 151 ? 25.755  -24.209 5.032   1.00 15.03 ?  4626 THR A C   1 
ATOM   943  O  O   . THR A 1 151 ? 26.366  -25.099 4.417   1.00 14.96 ?  4626 THR A O   1 
ATOM   944  C  CB  . THR A 1 151 ? 25.368  -25.365 7.201   1.00 12.82 ?  4626 THR A CB  1 
ATOM   945  O  OG1 . THR A 1 151 ? 23.962  -25.468 6.931   1.00 14.34 ?  4626 THR A OG1 1 
ATOM   946  C  CG2 . THR A 1 151 ? 25.610  -25.339 8.724   1.00 14.09 ?  4626 THR A CG2 1 
ATOM   947  N  N   . PHE A 1 152 ? 24.940  -23.350 4.421   1.00 13.16 ?  4627 PHE A N   1 
ATOM   948  C  CA  . PHE A 1 152 ? 24.817  -23.246 2.976   1.00 10.88 ?  4627 PHE A CA  1 
ATOM   949  C  C   . PHE A 1 152 ? 24.909  -21.775 2.610   1.00 10.56 ?  4627 PHE A C   1 
ATOM   950  O  O   . PHE A 1 152 ? 24.728  -20.892 3.457   1.00 11.20 ?  4627 PHE A O   1 
ATOM   951  C  CB  . PHE A 1 152 ? 23.441  -23.742 2.489   1.00 12.69 ?  4627 PHE A CB  1 
ATOM   952  C  CG  . PHE A 1 152 ? 23.292  -25.244 2.372   1.00 15.09 ?  4627 PHE A CG  1 
ATOM   953  C  CD1 . PHE A 1 152 ? 24.194  -26.005 1.638   1.00 13.85 ?  4627 PHE A CD1 1 
ATOM   954  C  CD2 . PHE A 1 152 ? 22.201  -25.897 2.969   1.00 15.66 ?  4627 PHE A CD2 1 
ATOM   955  C  CE1 . PHE A 1 152 ? 24.025  -27.373 1.495   1.00 17.06 ?  4627 PHE A CE1 1 
ATOM   956  C  CE2 . PHE A 1 152 ? 22.027  -27.269 2.834   1.00 15.96 ?  4627 PHE A CE2 1 
ATOM   957  C  CZ  . PHE A 1 152 ? 22.942  -28.011 2.089   1.00 15.99 ?  4627 PHE A CZ  1 
ATOM   958  N  N   . TYR A 1 153 ? 25.179  -21.516 1.331   1.00 11.34 ?  4628 TYR A N   1 
ATOM   959  C  CA  . TYR A 1 153 ? 25.157  -20.161 0.776   1.00 11.28 ?  4628 TYR A CA  1 
ATOM   960  C  C   . TYR A 1 153 ? 24.866  -20.298 -0.714  1.00 9.70  ?  4628 TYR A C   1 
ATOM   961  O  O   . TYR A 1 153 ? 24.588  -21.392 -1.199  1.00 12.98 ?  4628 TYR A O   1 
ATOM   962  C  CB  . TYR A 1 153 ? 26.469  -19.420 1.087   1.00 12.17 ?  4628 TYR A CB  1 
ATOM   963  C  CG  . TYR A 1 153 ? 27.729  -20.056 0.511   1.00 13.09 ?  4628 TYR A CG  1 
ATOM   964  C  CD1 . TYR A 1 153 ? 28.350  -21.145 1.143   1.00 14.54 ?  4628 TYR A CD1 1 
ATOM   965  C  CD2 . TYR A 1 153 ? 28.288  -19.566 -0.661  1.00 14.87 ?  4628 TYR A CD2 1 
ATOM   966  C  CE1 . TYR A 1 153 ? 29.507  -21.728 0.601   1.00 17.87 ?  4628 TYR A CE1 1 
ATOM   967  C  CE2 . TYR A 1 153 ? 29.442  -20.122 -1.186  1.00 17.81 ?  4628 TYR A CE2 1 
ATOM   968  C  CZ  . TYR A 1 153 ? 30.035  -21.193 -0.556  1.00 19.68 ?  4628 TYR A CZ  1 
ATOM   969  O  OH  . TYR A 1 153 ? 31.176  -21.746 -1.124  1.00 21.75 ?  4628 TYR A OH  1 
ATOM   970  N  N   . LEU A 1 154 ? 24.921  -19.187 -1.438  1.00 11.75 ?  4629 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 154 ? 24.685  -19.189 -2.878  1.00 12.26 ?  4629 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 154 ? 25.925  -18.720 -3.619  1.00 13.70 ?  4629 LEU A C   1 
ATOM   973  O  O   . LEU A 1 154 ? 26.639  -17.824 -3.163  1.00 12.69 ?  4629 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 154 ? 23.519  -18.297 -3.266  1.00 15.08 ?  4629 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 154 ? 22.230  -18.692 -2.552  1.00 15.56 ?  4629 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 154 ? 21.184  -17.690 -2.769  1.00 20.91 ?  4629 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 154 ? 21.758  -20.049 -2.987  1.00 16.55 ?  4629 LEU A CD2 1 
ATOM   978  N  N   . GLU A 1 155 ? 26.149  -19.312 -4.791  1.00 13.42 ?  4630 GLU A N   1 
ATOM   979  C  CA  . GLU A 1 155 ? 27.240  -18.853 -5.633  1.00 14.26 ?  4630 GLU A CA  1 
ATOM   980  C  C   . GLU A 1 155 ? 26.766  -18.818 -7.070  1.00 12.32 ?  4630 GLU A C   1 
ATOM   981  O  O   . GLU A 1 155 ? 25.605  -19.122 -7.378  1.00 12.39 ?  4630 GLU A O   1 
ATOM   982  C  CB  . GLU A 1 155 ? 28.510  -19.690 -5.476  1.00 17.69 ?  4630 GLU A CB  1 
ATOM   983  C  CG  . GLU A 1 155 ? 28.382  -21.111 -5.881  1.00 19.36 ?  4630 GLU A CG  1 
ATOM   984  C  CD  . GLU A 1 155 ? 29.667  -21.886 -5.617  1.00 23.80 ?  4630 GLU A CD  1 
ATOM   985  O  OE1 . GLU A 1 155 ? 30.705  -21.230 -5.365  1.00 26.04 ?  4630 GLU A OE1 1 
ATOM   986  O  OE2 . GLU A 1 155 ? 29.639  -23.136 -5.658  1.00 29.88 -1 4630 GLU A OE2 1 
ATOM   987  N  N   . ASN A 1 156 ? 27.667  -18.384 -7.951  1.00 13.66 ?  4631 ASN A N   1 
ATOM   988  C  CA  . ASN A 1 156 ? 27.401  -18.356 -9.388  1.00 15.35 ?  4631 ASN A CA  1 
ATOM   989  C  C   . ASN A 1 156 ? 26.189  -17.500 -9.718  1.00 14.62 ?  4631 ASN A C   1 
ATOM   990  O  O   . ASN A 1 156 ? 25.481  -17.754 -10.696 1.00 14.51 ?  4631 ASN A O   1 
ATOM   991  C  CB  . ASN A 1 156 ? 27.250  -19.767 -9.981  1.00 13.19 ?  4631 ASN A CB  1 
ATOM   992  C  CG  . ASN A 1 156 ? 28.496  -20.580 -9.826  1.00 16.80 ?  4631 ASN A CG  1 
ATOM   993  O  OD1 . ASN A 1 156 ? 29.584  -20.113 -10.149 1.00 17.63 ?  4631 ASN A OD1 1 
ATOM   994  N  ND2 . ASN A 1 156 ? 28.359  -21.799 -9.309  1.00 16.96 ?  4631 ASN A ND2 1 
ATOM   995  N  N   . GLU A 1 157 ? 25.950  -16.458 -8.927  1.00 13.39 ?  4632 GLU A N   1 
ATOM   996  C  CA  . GLU A 1 157 ? 24.734  -15.681 -9.113  1.00 13.43 ?  4632 GLU A CA  1 
ATOM   997  C  C   . GLU A 1 157 ? 24.727  -14.969 -10.456 1.00 13.76 ?  4632 GLU A C   1 
ATOM   998  O  O   . GLU A 1 157 ? 25.696  -14.300 -10.834 1.00 16.28 ?  4632 GLU A O   1 
ATOM   999  C  CB  . GLU A 1 157 ? 24.572  -14.673 -7.978  1.00 15.04 ?  4632 GLU A CB  1 
ATOM   1000 C  CG  . GLU A 1 157 ? 24.399  -15.329 -6.621  1.00 16.82 ?  4632 GLU A CG  1 
ATOM   1001 C  CD  . GLU A 1 157 ? 25.680  -15.371 -5.825  1.00 17.10 ?  4632 GLU A CD  1 
ATOM   1002 O  OE1 . GLU A 1 157 ? 26.784  -15.526 -6.420  1.00 17.06 ?  4632 GLU A OE1 1 
ATOM   1003 O  OE2 . GLU A 1 157 ? 25.572  -15.233 -4.595  1.00 17.15 -1 4632 GLU A OE2 1 
ATOM   1004 N  N   . GLY A 1 158 ? 23.613  -15.113 -11.163 1.00 13.22 ?  4633 GLY A N   1 
ATOM   1005 C  CA  . GLY A 1 158 ? 23.460  -14.502 -12.463 1.00 12.68 ?  4633 GLY A CA  1 
ATOM   1006 C  C   . GLY A 1 158 ? 24.239  -15.150 -13.573 1.00 12.68 ?  4633 GLY A C   1 
ATOM   1007 O  O   . GLY A 1 158 ? 24.226  -14.626 -14.693 1.00 15.51 ?  4633 GLY A O   1 
ATOM   1008 N  N   . SER A 1 159 ? 24.911  -16.259 -13.305 1.00 12.56 ?  4634 SER A N   1 
ATOM   1009 C  CA  . SER A 1 159 ? 25.696  -16.912 -14.338 1.00 12.82 ?  4634 SER A CA  1 
ATOM   1010 C  C   . SER A 1 159 ? 24.780  -17.615 -15.323 1.00 13.52 ?  4634 SER A C   1 
ATOM   1011 O  O   . SER A 1 159 ? 23.570  -17.742 -15.121 1.00 14.37 ?  4634 SER A O   1 
ATOM   1012 C  CB  . SER A 1 159 ? 26.682  -17.890 -13.724 1.00 12.76 ?  4634 SER A CB  1 
ATOM   1013 O  OG  . SER A 1 159 ? 26.000  -18.966 -13.100 1.00 13.80 ?  4634 SER A OG  1 
ATOM   1014 N  N   . ASP A 1 160 ? 25.389  -18.086 -16.406 1.00 13.57 ?  4635 ASP A N   1 
ATOM   1015 C  CA  . ASP A 1 160 ? 24.679  -18.616 -17.566 1.00 13.11 ?  4635 ASP A CA  1 
ATOM   1016 C  C   . ASP A 1 160 ? 25.084  -20.072 -17.775 1.00 14.58 ?  4635 ASP A C   1 
ATOM   1017 O  O   . ASP A 1 160 ? 25.992  -20.366 -18.573 1.00 15.98 ?  4635 ASP A O   1 
ATOM   1018 C  CB  . ASP A 1 160 ? 25.009  -17.778 -18.801 1.00 14.57 ?  4635 ASP A CB  1 
ATOM   1019 C  CG  . ASP A 1 160 ? 24.094  -18.082 -19.955 1.00 17.72 ?  4635 ASP A CG  1 
ATOM   1020 O  OD1 . ASP A 1 160 ? 23.038  -18.700 -19.737 1.00 16.17 ?  4635 ASP A OD1 1 
ATOM   1021 O  OD2 . ASP A 1 160 ? 24.416  -17.668 -21.080 1.00 16.96 -1 4635 ASP A OD2 1 
ATOM   1022 N  N   . PRO A 1 161 ? 24.442  -21.010 -17.077 1.00 13.84 ?  4636 PRO A N   1 
ATOM   1023 C  CA  . PRO A 1 161 ? 24.839  -22.416 -17.183 1.00 13.51 ?  4636 PRO A CA  1 
ATOM   1024 C  C   . PRO A 1 161 ? 24.401  -23.035 -18.495 1.00 13.38 ?  4636 PRO A C   1 
ATOM   1025 O  O   . PRO A 1 161 ? 23.404  -22.641 -19.097 1.00 14.31 ?  4636 PRO A O   1 
ATOM   1026 C  CB  . PRO A 1 161 ? 24.111  -23.080 -16.009 1.00 16.48 ?  4636 PRO A CB  1 
ATOM   1027 C  CG  . PRO A 1 161 ? 22.894  -22.260 -15.827 1.00 14.72 ?  4636 PRO A CG  1 
ATOM   1028 C  CD  . PRO A 1 161 ? 23.361  -20.826 -16.088 1.00 15.35 ?  4636 PRO A CD  1 
ATOM   1029 N  N   . MET A 1 162 ? 25.161  -24.046 -18.897 1.00 15.58 ?  4637 MET A N   1 
ATOM   1030 C  CA  . MET A 1 162 ? 24.798  -24.922 -20.000 1.00 17.31 ?  4637 MET A CA  1 
ATOM   1031 C  C   . MET A 1 162 ? 23.588  -25.757 -19.608 1.00 15.31 ?  4637 MET A C   1 
ATOM   1032 O  O   . MET A 1 162 ? 23.587  -26.403 -18.552 1.00 19.53 ?  4637 MET A O   1 
ATOM   1033 C  CB  . MET A 1 162 ? 25.977  -25.856 -20.258 1.00 18.89 ?  4637 MET A CB  1 
ATOM   1034 C  CG  . MET A 1 162 ? 25.718  -26.884 -21.315 1.00 20.02 ?  4637 MET A CG  1 
ATOM   1035 S  SD  . MET A 1 162 ? 25.693  -26.087 -22.925 1.00 24.12 ?  4637 MET A SD  1 
ATOM   1036 C  CE  . MET A 1 162 ? 27.439  -25.866 -23.174 1.00 19.62 ?  4637 MET A CE  1 
ATOM   1037 N  N   . ILE A 1 163 ? 22.558  -25.730 -20.445 1.00 13.90 ?  4638 ILE A N   1 
ATOM   1038 C  CA  . ILE A 1 163 ? 21.367  -26.556 -20.263 1.00 15.03 ?  4638 ILE A CA  1 
ATOM   1039 C  C   . ILE A 1 163 ? 21.431  -27.821 -21.121 1.00 15.19 ?  4638 ILE A C   1 
ATOM   1040 O  O   . ILE A 1 163 ? 21.211  -28.926 -20.627 1.00 17.29 ?  4638 ILE A O   1 
ATOM   1041 C  CB  . ILE A 1 163 ? 20.084  -25.729 -20.523 1.00 15.41 ?  4638 ILE A CB  1 
ATOM   1042 C  CG1 . ILE A 1 163 ? 20.006  -24.529 -19.559 1.00 14.70 ?  4638 ILE A CG1 1 
ATOM   1043 C  CG2 . ILE A 1 163 ? 18.823  -26.602 -20.405 1.00 17.22 ?  4638 ILE A CG2 1 
ATOM   1044 C  CD1 . ILE A 1 163 ? 20.039  -24.915 -18.079 1.00 16.62 ?  4638 ILE A CD1 1 
ATOM   1045 N  N   . ARG A 1 164 ? 21.777  -27.683 -22.403 1.00 15.23 ?  4639 ARG A N   1 
ATOM   1046 C  CA  . ARG A 1 164 ? 21.941  -28.830 -23.297 1.00 17.06 ?  4639 ARG A CA  1 
ATOM   1047 C  C   . ARG A 1 164 ? 23.233  -28.664 -24.084 1.00 15.68 ?  4639 ARG A C   1 
ATOM   1048 O  O   . ARG A 1 164 ? 23.371  -27.718 -24.869 1.00 16.64 ?  4639 ARG A O   1 
ATOM   1049 C  CB  . ARG A 1 164 ? 20.748  -28.980 -24.245 1.00 17.96 ?  4639 ARG A CB  1 
ATOM   1050 C  CG  . ARG A 1 164 ? 20.798  -30.247 -25.085 1.00 18.62 ?  4639 ARG A CG  1 
ATOM   1051 C  CD  . ARG A 1 164 ? 19.661  -30.294 -26.070 1.00 25.83 ?  4639 ARG A CD  1 
ATOM   1052 N  NE  . ARG A 1 164 ? 19.682  -31.562 -26.792 1.00 25.43 ?  4639 ARG A NE  1 
ATOM   1053 C  CZ  . ARG A 1 164 ? 18.867  -31.876 -27.787 1.00 23.86 ?  4639 ARG A CZ  1 
ATOM   1054 N  NH1 . ARG A 1 164 ? 17.948  -31.030 -28.221 1.00 24.94 ?  4639 ARG A NH1 1 
ATOM   1055 N  NH2 . ARG A 1 164 ? 18.986  -33.066 -28.366 1.00 29.33 ?  4639 ARG A NH2 1 
ATOM   1056 N  N   . ASP A 1 165 ? 24.170  -29.576 -23.863 1.00 17.34 ?  4640 ASP A N   1 
ATOM   1057 C  CA  . ASP A 1 165 ? 25.475  -29.544 -24.509 1.00 17.79 ?  4640 ASP A CA  1 
ATOM   1058 C  C   . ASP A 1 165 ? 25.462  -30.540 -25.658 1.00 18.59 ?  4640 ASP A C   1 
ATOM   1059 O  O   . ASP A 1 165 ? 25.290  -31.744 -25.439 1.00 22.62 ?  4640 ASP A O   1 
ATOM   1060 C  CB  . ASP A 1 165 ? 26.561  -29.915 -23.502 1.00 19.49 ?  4640 ASP A CB  1 
ATOM   1061 C  CG  . ASP A 1 165 ? 27.954  -29.529 -23.965 1.00 23.72 ?  4640 ASP A CG  1 
ATOM   1062 O  OD1 . ASP A 1 165 ? 28.111  -29.052 -25.112 1.00 20.66 ?  4640 ASP A OD1 1 
ATOM   1063 O  OD2 . ASP A 1 165 ? 28.904  -29.685 -23.168 1.00 27.79 -1 4640 ASP A OD2 1 
ATOM   1064 N  N   . ARG A 1 166 ? 25.631  -30.034 -26.873 1.00 16.11 ?  4641 ARG A N   1 
ATOM   1065 C  CA  . ARG A 1 166 ? 25.703  -30.842 -28.087 1.00 18.86 ?  4641 ARG A CA  1 
ATOM   1066 C  C   . ARG A 1 166 ? 27.082  -30.699 -28.709 1.00 16.01 ?  4641 ARG A C   1 
ATOM   1067 O  O   . ARG A 1 166 ? 27.915  -29.929 -28.241 1.00 18.71 ?  4641 ARG A O   1 
ATOM   1068 C  CB  . ARG A 1 166 ? 24.592  -30.438 -29.056 1.00 18.87 ?  4641 ARG A CB  1 
ATOM   1069 C  CG  . ARG A 1 166 ? 23.230  -30.667 -28.414 1.00 20.45 ?  4641 ARG A CG  1 
ATOM   1070 C  CD  . ARG A 1 166 ? 22.103  -30.305 -29.295 1.00 21.44 ?  4641 ARG A CD  1 
ATOM   1071 N  NE  . ARG A 1 166 ? 22.083  -31.118 -30.508 1.00 24.48 ?  4641 ARG A NE  1 
ATOM   1072 C  CZ  . ARG A 1 166 ? 21.209  -30.935 -31.484 1.00 24.51 ?  4641 ARG A CZ  1 
ATOM   1073 N  NH1 . ARG A 1 166 ? 20.274  -30.002 -31.401 1.00 21.37 ?  4641 ARG A NH1 1 
ATOM   1074 N  NH2 . ARG A 1 166 ? 21.286  -31.690 -32.578 1.00 22.26 ?  4641 ARG A NH2 1 
ATOM   1075 N  N   . SER A 1 167 ? 27.332  -31.475 -29.765 1.00 19.74 ?  4642 SER A N   1 
ATOM   1076 C  CA  . SER A 1 167 ? 28.624  -31.405 -30.433 1.00 23.12 ?  4642 SER A CA  1 
ATOM   1077 C  C   . SER A 1 167 ? 28.868  -30.000 -30.974 1.00 17.56 ?  4642 SER A C   1 
ATOM   1078 O  O   . SER A 1 167 ? 27.959  -29.353 -31.505 1.00 20.20 ?  4642 SER A O   1 
ATOM   1079 C  CB  . SER A 1 167 ? 28.683  -32.412 -31.580 1.00 23.68 ?  4642 SER A CB  1 
ATOM   1080 O  OG  . SER A 1 167 ? 29.951  -32.344 -32.203 1.00 32.50 ?  4642 SER A OG  1 
ATOM   1081 N  N   . GLY A 1 168 ? 30.100  -29.527 -30.834 1.00 19.08 ?  4643 GLY A N   1 
ATOM   1082 C  CA  . GLY A 1 168 ? 30.373  -28.164 -31.251 1.00 18.18 ?  4643 GLY A CA  1 
ATOM   1083 C  C   . GLY A 1 168 ? 29.761  -27.180 -30.265 1.00 16.42 ?  4643 GLY A C   1 
ATOM   1084 O  O   . GLY A 1 168 ? 29.529  -27.496 -29.087 1.00 18.29 ?  4643 GLY A O   1 
ATOM   1085 N  N   . THR A 1 169 ? 29.533  -25.956 -30.747 1.00 14.90 ?  4644 THR A N   1 
ATOM   1086 C  CA  . THR A 1 169 ? 28.872  -24.949 -29.936 1.00 15.56 ?  4644 THR A CA  1 
ATOM   1087 C  C   . THR A 1 169 ? 27.568  -24.431 -30.524 1.00 16.68 ?  4644 THR A C   1 
ATOM   1088 O  O   . THR A 1 169 ? 26.744  -23.923 -29.766 1.00 15.27 ?  4644 THR A O   1 
ATOM   1089 C  CB  . THR A 1 169 ? 29.794  -23.750 -29.653 1.00 14.72 ?  4644 THR A CB  1 
ATOM   1090 O  OG1 . THR A 1 169 ? 30.095  -23.054 -30.873 1.00 16.51 ?  4644 THR A OG1 1 
ATOM   1091 C  CG2 . THR A 1 169 ? 31.123  -24.196 -28.994 1.00 17.57 ?  4644 THR A CG2 1 
ATOM   1092 N  N   . VAL A 1 170 ? 27.347  -24.541 -31.838 1.00 13.72 ?  4645 VAL A N   1 
ATOM   1093 C  CA  . VAL A 1 170 ? 26.260  -23.788 -32.456 1.00 14.10 ?  4645 VAL A CA  1 
ATOM   1094 C  C   . VAL A 1 170 ? 24.881  -24.255 -32.009 1.00 14.73 ?  4645 VAL A C   1 
ATOM   1095 O  O   . VAL A 1 170 ? 23.915  -23.485 -32.084 1.00 15.49 ?  4645 VAL A O   1 
ATOM   1096 C  CB  . VAL A 1 170 ? 26.398  -23.855 -33.987 1.00 13.34 ?  4645 VAL A CB  1 
ATOM   1097 C  CG1 . VAL A 1 170 ? 26.109  -25.246 -34.513 1.00 15.04 ?  4645 VAL A CG1 1 
ATOM   1098 C  CG2 . VAL A 1 170 ? 25.512  -22.815 -34.667 1.00 16.87 ?  4645 VAL A CG2 1 
ATOM   1099 N  N   . ASN A 1 171 ? 24.765  -25.505 -31.558 1.00 13.95 ?  4646 ASN A N   1 
ATOM   1100 C  CA  . ASN A 1 171 ? 23.493  -26.067 -31.121 1.00 12.41 ?  4646 ASN A CA  1 
ATOM   1101 C  C   . ASN A 1 171 ? 23.396  -26.156 -29.604 1.00 14.08 ?  4646 ASN A C   1 
ATOM   1102 O  O   . ASN A 1 171 ? 22.438  -26.742 -29.088 1.00 15.71 ?  4646 ASN A O   1 
ATOM   1103 C  CB  . ASN A 1 171 ? 23.290  -27.451 -31.745 1.00 14.30 ?  4646 ASN A CB  1 
ATOM   1104 C  CG  . ASN A 1 171 ? 23.185  -27.397 -33.257 1.00 16.45 ?  4646 ASN A CG  1 
ATOM   1105 O  OD1 . ASN A 1 171 ? 23.835  -28.172 -33.975 1.00 19.55 ?  4646 ASN A OD1 1 
ATOM   1106 N  ND2 . ASN A 1 171 ? 22.362  -26.496 -33.744 1.00 14.04 ?  4646 ASN A ND2 1 
ATOM   1107 N  N   . ASP A 1 172 ? 24.385  -25.636 -28.884 1.00 13.28 ?  4647 ASP A N   1 
ATOM   1108 C  CA  . ASP A 1 172 ? 24.313  -25.656 -27.432 1.00 12.71 ?  4647 ASP A CA  1 
ATOM   1109 C  C   . ASP A 1 172 ? 23.168  -24.759 -26.964 1.00 14.25 ?  4647 ASP A C   1 
ATOM   1110 O  O   . ASP A 1 172 ? 22.820  -23.764 -27.613 1.00 15.99 ?  4647 ASP A O   1 
ATOM   1111 C  CB  . ASP A 1 172 ? 25.636  -25.173 -26.832 1.00 15.16 ?  4647 ASP A CB  1 
ATOM   1112 C  CG  . ASP A 1 172 ? 26.761  -26.187 -26.980 1.00 14.54 ?  4647 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A 1 172 ? 26.509  -27.329 -27.444 1.00 14.80 ?  4647 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A 1 172 ? 27.910  -25.835 -26.637 1.00 15.86 -1 4647 ASP A OD2 1 
ATOM   1115 N  N   . VAL A 1 173 ? 22.565  -25.130 -25.839 1.00 15.21 ?  4648 VAL A N   1 
ATOM   1116 C  CA  . VAL A 1 173 ? 21.497  -24.340 -25.224 1.00 15.64 ?  4648 VAL A CA  1 
ATOM   1117 C  C   . VAL A 1 173 ? 21.969  -23.909 -23.845 1.00 11.69 ?  4648 VAL A C   1 
ATOM   1118 O  O   . VAL A 1 173 ? 22.212  -24.754 -22.983 1.00 14.05 ?  4648 VAL A O   1 
ATOM   1119 C  CB  . VAL A 1 173 ? 20.191  -25.141 -25.130 1.00 16.30 ?  4648 VAL A CB  1 
ATOM   1120 C  CG1 . VAL A 1 173 ? 19.071  -24.251 -24.607 1.00 17.99 ?  4648 VAL A CG1 1 
ATOM   1121 C  CG2 . VAL A 1 173 ? 19.813  -25.673 -26.516 1.00 18.80 ?  4648 VAL A CG2 1 
ATOM   1122 N  N   . TYR A 1 174 ? 22.088  -22.602 -23.642 1.00 12.71 ?  4649 TYR A N   1 
ATOM   1123 C  CA  . TYR A 1 174 ? 22.384  -22.028 -22.337 1.00 13.35 ?  4649 TYR A CA  1 
ATOM   1124 C  C   . TYR A 1 174 ? 21.095  -21.560 -21.696 1.00 15.19 ?  4649 TYR A C   1 
ATOM   1125 O  O   . TYR A 1 174 ? 20.084  -21.384 -22.361 1.00 14.58 ?  4649 TYR A O   1 
ATOM   1126 C  CB  . TYR A 1 174 ? 23.325  -20.829 -22.488 1.00 16.08 ?  4649 TYR A CB  1 
ATOM   1127 C  CG  . TYR A 1 174 ? 24.736  -21.241 -22.836 1.00 16.53 ?  4649 TYR A CG  1 
ATOM   1128 C  CD1 . TYR A 1 174 ? 25.118  -21.455 -24.156 1.00 15.10 ?  4649 TYR A CD1 1 
ATOM   1129 C  CD2 . TYR A 1 174 ? 25.671  -21.449 -21.850 1.00 16.34 ?  4649 TYR A CD2 1 
ATOM   1130 C  CE1 . TYR A 1 174 ? 26.411  -21.840 -24.467 1.00 16.04 ?  4649 TYR A CE1 1 
ATOM   1131 C  CE2 . TYR A 1 174 ? 26.956  -21.842 -22.144 1.00 16.71 ?  4649 TYR A CE2 1 
ATOM   1132 C  CZ  . TYR A 1 174 ? 27.318  -22.033 -23.454 1.00 18.13 ?  4649 TYR A CZ  1 
ATOM   1133 O  OH  . TYR A 1 174 ? 28.610  -22.407 -23.720 1.00 18.28 ?  4649 TYR A OH  1 
ATOM   1134 N  N   . LEU A 1 175 ? 21.146  -21.347 -20.380 1.00 13.72 ?  4650 LEU A N   1 
ATOM   1135 C  CA  . LEU A 1 175 ? 19.987  -20.780 -19.698 1.00 15.17 ?  4650 LEU A CA  1 
ATOM   1136 C  C   . LEU A 1 175 ? 19.536  -19.476 -20.347 1.00 16.52 ?  4650 LEU A C   1 
ATOM   1137 O  O   . LEU A 1 175 ? 18.330  -19.225 -20.478 1.00 15.57 ?  4650 LEU A O   1 
ATOM   1138 C  CB  . LEU A 1 175 ? 20.304  -20.585 -18.212 1.00 13.53 ?  4650 LEU A CB  1 
ATOM   1139 C  CG  . LEU A 1 175 ? 19.118  -20.106 -17.375 1.00 13.29 ?  4650 LEU A CG  1 
ATOM   1140 C  CD1 . LEU A 1 175 ? 17.971  -21.105 -17.356 1.00 17.31 ?  4650 LEU A CD1 1 
ATOM   1141 C  CD2 . LEU A 1 175 ? 19.636  -19.843 -15.968 1.00 16.16 ?  4650 LEU A CD2 1 
ATOM   1142 N  N   . SER A 1 176 ? 20.491  -18.656 -20.810 1.00 15.84 ?  4651 SER A N   1 
ATOM   1143 C  CA  . SER A 1 176 ? 20.151  -17.394 -21.457 1.00 15.55 ?  4651 SER A CA  1 
ATOM   1144 C  C   . SER A 1 176 ? 19.344  -17.603 -22.735 1.00 18.04 ?  4651 SER A C   1 
ATOM   1145 O  O   . SER A 1 176 ? 18.574  -16.724 -23.123 1.00 21.64 ?  4651 SER A O   1 
ATOM   1146 C  CB  . SER A 1 176 ? 21.417  -16.588 -21.745 1.00 18.37 ?  4651 SER A CB  1 
ATOM   1147 O  OG  . SER A 1 176 ? 22.288  -17.301 -22.607 1.00 16.31 ?  4651 SER A OG  1 
ATOM   1148 N  N   . ASN A 1 177 ? 19.510  -18.743 -23.405 1.00 15.38 ?  4652 ASN A N   1 
ATOM   1149 C  CA  . ASN A 1 177 ? 18.698  -19.036 -24.577 1.00 16.17 ?  4652 ASN A CA  1 
ATOM   1150 C  C   . ASN A 1 177 ? 17.290  -19.443 -24.197 1.00 18.77 ?  4652 ASN A C   1 
ATOM   1151 O  O   . ASN A 1 177 ? 16.388  -19.381 -25.043 1.00 23.45 ?  4652 ASN A O   1 
ATOM   1152 C  CB  . ASN A 1 177 ? 19.323  -20.173 -25.393 1.00 14.43 ?  4652 ASN A CB  1 
ATOM   1153 C  CG  . ASN A 1 177 ? 20.700  -19.815 -25.922 1.00 14.69 ?  4652 ASN A CG  1 
ATOM   1154 O  OD1 . ASN A 1 177 ? 21.687  -20.485 -25.614 1.00 16.76 ?  4652 ASN A OD1 1 
ATOM   1155 N  ND2 . ASN A 1 177 ? 20.772  -18.750 -26.716 1.00 18.09 ?  4652 ASN A ND2 1 
ATOM   1156 N  N   . VAL A 1 178 ? 17.098  -19.880 -22.958 1.00 18.08 ?  4653 VAL A N   1 
ATOM   1157 C  CA  . VAL A 1 178 ? 15.794  -20.311 -22.475 1.00 19.12 ?  4653 VAL A CA  1 
ATOM   1158 C  C   . VAL A 1 178 ? 15.019  -19.140 -21.900 1.00 16.95 ?  4653 VAL A C   1 
ATOM   1159 O  O   . VAL A 1 178 ? 13.860  -18.916 -22.258 1.00 20.69 ?  4653 VAL A O   1 
ATOM   1160 C  CB  . VAL A 1 178 ? 15.973  -21.443 -21.442 1.00 19.70 ?  4653 VAL A CB  1 
ATOM   1161 C  CG1 . VAL A 1 178 ? 14.627  -21.857 -20.885 1.00 22.08 ?  4653 VAL A CG1 1 
ATOM   1162 C  CG2 . VAL A 1 178 ? 16.685  -22.646 -22.068 1.00 20.00 ?  4653 VAL A CG2 1 
ATOM   1163 N  N   . ILE A 1 179 ? 15.659  -18.355 -21.034 1.00 18.34 ?  4654 ILE A N   1 
ATOM   1164 C  CA  . ILE A 1 179 ? 14.966  -17.302 -20.301 1.00 18.98 ?  4654 ILE A CA  1 
ATOM   1165 C  C   . ILE A 1 179 ? 15.178  -15.910 -20.890 1.00 22.01 ?  4654 ILE A C   1 
ATOM   1166 O  O   . ILE A 1 179 ? 14.408  -14.991 -20.565 1.00 22.75 ?  4654 ILE A O   1 
ATOM   1167 C  CB  . ILE A 1 179 ? 15.312  -17.311 -18.794 1.00 17.10 ?  4654 ILE A CB  1 
ATOM   1168 C  CG1 . ILE A 1 179 ? 16.790  -16.944 -18.575 1.00 17.62 ?  4654 ILE A CG1 1 
ATOM   1169 C  CG2 . ILE A 1 179 ? 14.967  -18.661 -18.154 1.00 19.41 ?  4654 ILE A CG2 1 
ATOM   1170 C  CD1 . ILE A 1 179 ? 17.183  -16.708 -17.106 1.00 17.42 ?  4654 ILE A CD1 1 
ATOM   1171 N  N   . GLY A 1 180 ? 16.198  -15.718 -21.722 1.00 20.69 ?  4655 GLY A N   1 
ATOM   1172 C  CA  . GLY A 1 180 ? 16.359  -14.415 -22.353 1.00 20.16 ?  4655 GLY A CA  1 
ATOM   1173 C  C   . GLY A 1 180 ? 16.669  -13.315 -21.356 1.00 23.25 ?  4655 GLY A C   1 
ATOM   1174 O  O   . GLY A 1 180 ? 17.272  -13.535 -20.298 1.00 23.09 ?  4655 GLY A O   1 
ATOM   1175 N  N   . THR A 1 181 ? 16.263  -12.096 -21.713 1.00 20.32 ?  4656 THR A N   1 
ATOM   1176 C  CA  . THR A 1 181 ? 16.442  -10.927 -20.860 1.00 19.28 ?  4656 THR A CA  1 
ATOM   1177 C  C   . THR A 1 181 ? 15.186  -10.571 -20.091 1.00 20.97 ?  4656 THR A C   1 
ATOM   1178 O  O   . THR A 1 181 ? 15.096  -9.462  -19.549 1.00 23.11 ?  4656 THR A O   1 
ATOM   1179 C  CB  . THR A 1 181 ? 16.881  -9.729  -21.692 1.00 21.79 ?  4656 THR A CB  1 
ATOM   1180 O  OG1 . THR A 1 181 ? 15.966  -9.569  -22.789 1.00 24.80 ?  4656 THR A OG1 1 
ATOM   1181 C  CG2 . THR A 1 181 ? 18.292  -9.928  -22.208 1.00 22.12 ?  4656 THR A CG2 1 
ATOM   1182 N  N   . SER A 1 182 ? 14.217  -11.480 -20.022 1.00 20.39 ?  4657 SER A N   1 
ATOM   1183 C  CA  . SER A 1 182 ? 12.926  -11.145 -19.431 1.00 25.70 ?  4657 SER A CA  1 
ATOM   1184 C  C   . SER A 1 182 ? 12.405  -12.281 -18.565 1.00 21.22 ?  4657 SER A C   1 
ATOM   1185 O  O   . SER A 1 182 ? 11.207  -12.579 -18.571 1.00 24.63 ?  4657 SER A O   1 
ATOM   1186 C  CB  . SER A 1 182 ? 11.907  -10.807 -20.514 1.00 25.23 ?  4657 SER A CB  1 
ATOM   1187 O  OG  . SER A 1 182 ? 11.856  -11.863 -21.455 1.00 32.75 ?  4657 SER A OG  1 
ATOM   1188 N  N   . TYR A 1 183 ? 13.275  -12.904 -17.775 1.00 16.43 ?  4658 TYR A N   1 
ATOM   1189 C  CA  . TYR A 1 183 ? 12.832  -13.989 -16.907 1.00 15.82 ?  4658 TYR A CA  1 
ATOM   1190 C  C   . TYR A 1 183 ? 11.696  -13.521 -16.002 1.00 17.37 ?  4658 TYR A C   1 
ATOM   1191 O  O   . TYR A 1 183 ? 11.784  -12.463 -15.371 1.00 19.75 ?  4658 TYR A O   1 
ATOM   1192 C  CB  . TYR A 1 183 ? 13.983  -14.506 -16.039 1.00 15.54 ?  4658 TYR A CB  1 
ATOM   1193 C  CG  . TYR A 1 183 ? 13.492  -15.518 -15.015 1.00 15.06 ?  4658 TYR A CG  1 
ATOM   1194 C  CD1 . TYR A 1 183 ? 13.000  -16.758 -15.423 1.00 16.81 ?  4658 TYR A CD1 1 
ATOM   1195 C  CD2 . TYR A 1 183 ? 13.458  -15.213 -13.651 1.00 15.94 ?  4658 TYR A CD2 1 
ATOM   1196 C  CE1 . TYR A 1 183 ? 12.523  -17.677 -14.506 1.00 14.91 ?  4658 TYR A CE1 1 
ATOM   1197 C  CE2 . TYR A 1 183 ? 12.990  -16.125 -12.730 1.00 15.77 ?  4658 TYR A CE2 1 
ATOM   1198 C  CZ  . TYR A 1 183 ? 12.523  -17.354 -13.157 1.00 13.87 ?  4658 TYR A CZ  1 
ATOM   1199 O  OH  . TYR A 1 183 ? 12.041  -18.257 -12.245 1.00 14.37 ?  4658 TYR A OH  1 
ATOM   1200 N  N   . THR A 1 184 ? 10.620  -14.304 -15.946 1.00 17.47 ?  4659 THR A N   1 
ATOM   1201 C  CA  . THR A 1 184 ? 9.507   -14.046 -15.033 1.00 17.82 ?  4659 THR A CA  1 
ATOM   1202 C  C   . THR A 1 184 ? 9.463   -15.163 -14.004 1.00 15.59 ?  4659 THR A C   1 
ATOM   1203 O  O   . THR A 1 184 ? 9.258   -16.332 -14.350 1.00 16.26 ?  4659 THR A O   1 
ATOM   1204 C  CB  . THR A 1 184 ? 8.183   -13.957 -15.794 1.00 18.84 ?  4659 THR A CB  1 
ATOM   1205 O  OG1 . THR A 1 184 ? 8.216   -12.811 -16.642 1.00 22.58 ?  4659 THR A OG1 1 
ATOM   1206 C  CG2 . THR A 1 184 ? 7.006   -13.822 -14.813 1.00 22.56 ?  4659 THR A CG2 1 
ATOM   1207 N  N   . TYR A 1 185 ? 9.671   -14.811 -12.734 1.00 15.22 ?  4660 TYR A N   1 
ATOM   1208 C  CA  . TYR A 1 185 ? 9.601   -15.817 -11.689 1.00 15.82 ?  4660 TYR A CA  1 
ATOM   1209 C  C   . TYR A 1 185 ? 8.203   -16.427 -11.667 1.00 16.42 ?  4660 TYR A C   1 
ATOM   1210 O  O   . TYR A 1 185 ? 7.200   -15.709 -11.751 1.00 17.91 ?  4660 TYR A O   1 
ATOM   1211 C  CB  . TYR A 1 185 ? 9.945   -15.175 -10.343 1.00 15.51 ?  4660 TYR A CB  1 
ATOM   1212 C  CG  . TYR A 1 185 ? 9.879   -16.136 -9.191  1.00 16.30 ?  4660 TYR A CG  1 
ATOM   1213 C  CD1 . TYR A 1 185 ? 10.708  -17.247 -9.136  1.00 16.54 ?  4660 TYR A CD1 1 
ATOM   1214 C  CD2 . TYR A 1 185 ? 8.997   -15.925 -8.147  1.00 18.41 ?  4660 TYR A CD2 1 
ATOM   1215 C  CE1 . TYR A 1 185 ? 10.654  -18.131 -8.086  1.00 17.77 ?  4660 TYR A CE1 1 
ATOM   1216 C  CE2 . TYR A 1 185 ? 8.938   -16.800 -7.086  1.00 19.53 ?  4660 TYR A CE2 1 
ATOM   1217 C  CZ  . TYR A 1 185 ? 9.763   -17.900 -7.063  1.00 22.45 ?  4660 TYR A CZ  1 
ATOM   1218 O  OH  . TYR A 1 185 ? 9.688   -18.765 -6.001  1.00 28.80 ?  4660 TYR A OH  1 
ATOM   1219 N  N   . GLY A 1 186 ? 8.143   -17.760 -11.613 1.00 18.65 ?  4661 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 186 ? 6.889   -18.487 -11.623 1.00 17.13 ?  4661 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 186 ? 6.447   -18.980 -12.986 1.00 19.43 ?  4661 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 186 ? 5.556   -19.836 -13.054 1.00 23.73 ?  4661 GLY A O   1 
ATOM   1223 N  N   . GLN A 1 187 ? 7.021   -18.449 -14.066 1.00 16.46 ?  4662 GLN A N   1 
ATOM   1224 C  CA  . GLN A 1 187 ? 6.762   -18.971 -15.403 1.00 19.16 ?  4662 GLN A CA  1 
ATOM   1225 C  C   . GLN A 1 187 ? 7.567   -20.247 -15.622 1.00 18.67 ?  4662 GLN A C   1 
ATOM   1226 O  O   . GLN A 1 187 ? 8.729   -20.338 -15.233 1.00 18.16 ?  4662 GLN A O   1 
ATOM   1227 C  CB  . GLN A 1 187 ? 7.143   -17.921 -16.450 1.00 19.25 ?  4662 GLN A CB  1 
ATOM   1228 C  CG  . GLN A 1 187 ? 7.020   -18.393 -17.911 1.00 21.05 ?  4662 GLN A CG  1 
ATOM   1229 C  CD  . GLN A 1 187 ? 7.331   -17.303 -18.928 1.00 22.19 ?  4662 GLN A CD  1 
ATOM   1230 O  OE1 . GLN A 1 187 ? 7.234   -16.107 -18.636 1.00 29.99 ?  4662 GLN A OE1 1 
ATOM   1231 N  NE2 . GLN A 1 187 ? 7.715   -17.714 -20.135 1.00 27.57 ?  4662 GLN A NE2 1 
ATOM   1232 N  N   . THR A 1 188 ? 6.947   -21.250 -16.234 1.00 20.06 ?  4663 THR A N   1 
ATOM   1233 C  CA  . THR A 1 188 ? 7.655   -22.485 -16.554 1.00 17.97 ?  4663 THR A CA  1 
ATOM   1234 C  C   . THR A 1 188 ? 8.334   -22.330 -17.910 1.00 20.35 ?  4663 THR A C   1 
ATOM   1235 O  O   . THR A 1 188 ? 7.732   -21.812 -18.852 1.00 20.57 ?  4663 THR A O   1 
ATOM   1236 C  CB  . THR A 1 188 ? 6.684   -23.668 -16.562 1.00 21.47 ?  4663 THR A CB  1 
ATOM   1237 O  OG1 . THR A 1 188 ? 6.165   -23.859 -15.238 1.00 22.59 ?  4663 THR A OG1 1 
ATOM   1238 C  CG2 . THR A 1 188 ? 7.389   -24.947 -16.997 1.00 21.25 ?  4663 THR A CG2 1 
ATOM   1239 N  N   . TYR A 1 189 ? 9.604   -22.728 -17.988 1.00 17.32 ?  4664 TYR A N   1 
ATOM   1240 C  CA  . TYR A 1 189 ? 10.373  -22.680 -19.223 1.00 19.69 ?  4664 TYR A CA  1 
ATOM   1241 C  C   . TYR A 1 189 ? 10.813  -24.086 -19.593 1.00 16.24 ?  4664 TYR A C   1 
ATOM   1242 O  O   . TYR A 1 189 ? 11.186  -24.882 -18.727 1.00 17.95 ?  4664 TYR A O   1 
ATOM   1243 C  CB  . TYR A 1 189 ? 11.612  -21.808 -19.064 1.00 17.42 ?  4664 TYR A CB  1 
ATOM   1244 C  CG  . TYR A 1 189 ? 11.319  -20.352 -18.848 1.00 15.70 ?  4664 TYR A CG  1 
ATOM   1245 C  CD1 . TYR A 1 189 ? 10.967  -19.883 -17.583 1.00 17.10 ?  4664 TYR A CD1 1 
ATOM   1246 C  CD2 . TYR A 1 189 ? 11.383  -19.442 -19.897 1.00 17.92 ?  4664 TYR A CD2 1 
ATOM   1247 C  CE1 . TYR A 1 189 ? 10.693  -18.553 -17.380 1.00 16.75 ?  4664 TYR A CE1 1 
ATOM   1248 C  CE2 . TYR A 1 189 ? 11.130  -18.109 -19.701 1.00 18.22 ?  4664 TYR A CE2 1 
ATOM   1249 C  CZ  . TYR A 1 189 ? 10.784  -17.664 -18.434 1.00 18.50 ?  4664 TYR A CZ  1 
ATOM   1250 O  OH  . TYR A 1 189 ? 10.524  -16.334 -18.228 1.00 19.95 ?  4664 TYR A OH  1 
ATOM   1251 N  N   . SER A 1 190 ? 10.791  -24.382 -20.898 1.00 21.83 ?  4665 SER A N   1 
ATOM   1252 C  CA  . SER A 1 190 ? 11.037  -25.739 -21.362 1.00 21.16 ?  4665 SER A CA  1 
ATOM   1253 C  C   . SER A 1 190 ? 11.925  -25.726 -22.602 1.00 21.23 ?  4665 SER A C   1 
ATOM   1254 O  O   . SER A 1 190 ? 11.999  -24.732 -23.331 1.00 24.96 ?  4665 SER A O   1 
ATOM   1255 C  CB  . SER A 1 190 ? 9.715   -26.469 -21.668 1.00 24.48 ?  4665 SER A CB  1 
ATOM   1256 O  OG  . SER A 1 190 ? 8.860   -25.644 -22.435 1.00 34.86 ?  4665 SER A OG  1 
ATOM   1257 N  N   . VAL A 1 191 ? 12.606  -26.849 -22.817 1.00 22.81 ?  4666 VAL A N   1 
ATOM   1258 C  CA  . VAL A 1 191 ? 13.366  -27.118 -24.036 1.00 24.76 ?  4666 VAL A CA  1 
ATOM   1259 C  C   . VAL A 1 191 ? 12.882  -28.457 -24.570 1.00 23.09 ?  4666 VAL A C   1 
ATOM   1260 O  O   . VAL A 1 191 ? 13.026  -29.480 -23.894 1.00 23.05 ?  4666 VAL A O   1 
ATOM   1261 C  CB  . VAL A 1 191 ? 14.879  -27.168 -23.772 1.00 23.62 ?  4666 VAL A CB  1 
ATOM   1262 C  CG1 . VAL A 1 191 ? 15.631  -27.681 -25.012 1.00 28.28 ?  4666 VAL A CG1 1 
ATOM   1263 C  CG2 . VAL A 1 191 ? 15.376  -25.795 -23.373 1.00 23.95 ?  4666 VAL A CG2 1 
ATOM   1264 N  N   . ASN A 1 192 ? 12.303  -28.452 -25.774 1.00 32.32 ?  4667 ASN A N   1 
ATOM   1265 C  CA  . ASN A 1 192 ? 11.764  -29.677 -26.382 1.00 31.20 ?  4667 ASN A CA  1 
ATOM   1266 C  C   . ASN A 1 192 ? 10.788  -30.383 -25.449 1.00 31.62 ?  4667 ASN A C   1 
ATOM   1267 O  O   . ASN A 1 192 ? 10.833  -31.604 -25.278 1.00 34.53 ?  4667 ASN A O   1 
ATOM   1268 C  CB  . ASN A 1 192 ? 12.873  -30.638 -26.805 1.00 34.51 ?  4667 ASN A CB  1 
ATOM   1269 C  CG  . ASN A 1 192 ? 13.765  -30.058 -27.862 1.00 33.97 ?  4667 ASN A CG  1 
ATOM   1270 O  OD1 . ASN A 1 192 ? 13.346  -29.199 -28.640 1.00 40.89 ?  4667 ASN A OD1 1 
ATOM   1271 N  ND2 . ASN A 1 192 ? 15.011  -30.522 -27.902 1.00 35.34 ?  4667 ASN A ND2 1 
ATOM   1272 N  N   . GLY A 1 193 ? 9.915   -29.605 -24.814 1.00 30.96 ?  4668 GLY A N   1 
ATOM   1273 C  CA  . GLY A 1 193 ? 8.970   -30.158 -23.870 1.00 31.97 ?  4668 GLY A CA  1 
ATOM   1274 C  C   . GLY A 1 193 ? 9.556   -30.617 -22.553 1.00 29.86 ?  4668 GLY A C   1 
ATOM   1275 O  O   . GLY A 1 193 ? 8.805   -31.113 -21.706 1.00 35.03 ?  4668 GLY A O   1 
ATOM   1276 N  N   . ARG A 1 194 ? 10.866  -30.480 -22.347 1.00 25.81 ?  4669 ARG A N   1 
ATOM   1277 C  CA  . ARG A 1 194 ? 11.489  -30.841 -21.081 1.00 24.39 ?  4669 ARG A CA  1 
ATOM   1278 C  C   . ARG A 1 194 ? 11.574  -29.596 -20.211 1.00 22.03 ?  4669 ARG A C   1 
ATOM   1279 O  O   . ARG A 1 194 ? 12.025  -28.544 -20.673 1.00 23.05 ?  4669 ARG A O   1 
ATOM   1280 C  CB  . ARG A 1 194 ? 12.897  -31.386 -21.297 1.00 25.96 ?  4669 ARG A CB  1 
ATOM   1281 C  CG  . ARG A 1 194 ? 12.954  -32.601 -22.215 1.00 25.87 ?  4669 ARG A CG  1 
ATOM   1282 C  CD  . ARG A 1 194 ? 14.269  -33.319 -22.068 1.00 25.99 ?  4669 ARG A CD  1 
ATOM   1283 N  NE  . ARG A 1 194 ? 14.332  -34.453 -22.986 1.00 27.20 ?  4669 ARG A NE  1 
ATOM   1284 C  CZ  . ARG A 1 194 ? 15.292  -35.367 -22.994 1.00 28.08 ?  4669 ARG A CZ  1 
ATOM   1285 N  NH1 . ARG A 1 194 ? 16.306  -35.312 -22.150 1.00 27.42 ?  4669 ARG A NH1 1 
ATOM   1286 N  NH2 . ARG A 1 194 ? 15.226  -36.369 -23.874 1.00 32.66 ?  4669 ARG A NH2 1 
ATOM   1287 N  N   . THR A 1 195 ? 11.127  -29.716 -18.967 1.00 22.61 ?  4670 THR A N   1 
ATOM   1288 C  CA  . THR A 1 195 ? 11.126  -28.566 -18.075 1.00 19.82 ?  4670 THR A CA  1 
ATOM   1289 C  C   . THR A 1 195 ? 12.552  -28.211 -17.676 1.00 17.93 ?  4670 THR A C   1 
ATOM   1290 O  O   . THR A 1 195 ? 13.304  -29.060 -17.183 1.00 20.56 ?  4670 THR A O   1 
ATOM   1291 C  CB  . THR A 1 195 ? 10.281  -28.871 -16.840 1.00 19.87 ?  4670 THR A CB  1 
ATOM   1292 O  OG1 . THR A 1 195 ? 8.915   -29.011 -17.239 1.00 27.56 ?  4670 THR A OG1 1 
ATOM   1293 C  CG2 . THR A 1 195 ? 10.383  -27.734 -15.814 1.00 21.10 ?  4670 THR A CG2 1 
ATOM   1294 N  N   . VAL A 1 196 ? 12.909  -26.948 -17.892 1.00 17.05 ?  4671 VAL A N   1 
ATOM   1295 C  CA  . VAL A 1 196 ? 14.225  -26.430 -17.557 1.00 18.02 ?  4671 VAL A CA  1 
ATOM   1296 C  C   . VAL A 1 196 ? 14.172  -25.479 -16.369 1.00 16.98 ?  4671 VAL A C   1 
ATOM   1297 O  O   . VAL A 1 196 ? 15.098  -25.451 -15.558 1.00 16.72 ?  4671 VAL A O   1 
ATOM   1298 C  CB  . VAL A 1 196 ? 14.888  -25.767 -18.782 1.00 20.00 ?  4671 VAL A CB  1 
ATOM   1299 C  CG1 . VAL A 1 196 ? 16.154  -25.025 -18.373 1.00 21.58 ?  4671 VAL A CG1 1 
ATOM   1300 C  CG2 . VAL A 1 196 ? 15.192  -26.828 -19.814 1.00 25.05 ?  4671 VAL A CG2 1 
ATOM   1301 N  N   . VAL A 1 197 ? 13.105  -24.690 -16.255 1.00 16.17 ?  4672 VAL A N   1 
ATOM   1302 C  CA  . VAL A 1 197 ? 12.851  -23.874 -15.068 1.00 14.37 ?  4672 VAL A CA  1 
ATOM   1303 C  C   . VAL A 1 197 ? 11.396  -24.097 -14.696 1.00 16.38 ?  4672 VAL A C   1 
ATOM   1304 O  O   . VAL A 1 197 ? 10.498  -23.791 -15.493 1.00 16.98 ?  4672 VAL A O   1 
ATOM   1305 C  CB  . VAL A 1 197 ? 13.112  -22.375 -15.293 1.00 14.19 ?  4672 VAL A CB  1 
ATOM   1306 C  CG1 . VAL A 1 197 ? 13.009  -21.626 -13.938 1.00 16.04 ?  4672 VAL A CG1 1 
ATOM   1307 C  CG2 . VAL A 1 197 ? 14.475  -22.132 -15.972 1.00 17.07 ?  4672 VAL A CG2 1 
ATOM   1308 N  N   . ASN A 1 198 ? 11.162  -24.613 -13.489 1.00 17.24 ?  4673 ASN A N   1 
ATOM   1309 C  CA  . ASN A 1 198 ? 9.802   -24.850 -13.035 1.00 17.47 ?  4673 ASN A CA  1 
ATOM   1310 C  C   . ASN A 1 198 ? 9.238   -23.605 -12.347 1.00 17.29 ?  4673 ASN A C   1 
ATOM   1311 O  O   . ASN A 1 198 ? 9.904   -22.576 -12.211 1.00 17.11 ?  4673 ASN A O   1 
ATOM   1312 C  CB  . ASN A 1 198 ? 9.696   -26.157 -12.239 1.00 17.56 ?  4673 ASN A CB  1 
ATOM   1313 C  CG  . ASN A 1 198 ? 10.258  -26.068 -10.825 1.00 18.43 ?  4673 ASN A CG  1 
ATOM   1314 O  OD1 . ASN A 1 198 ? 10.532  -24.991 -10.298 1.00 19.25 ?  4673 ASN A OD1 1 
ATOM   1315 N  ND2 . ASN A 1 198 ? 10.410  -27.224 -10.199 1.00 19.65 ?  4673 ASN A ND2 1 
ATOM   1316 N  N   . GLY A 1 199 ? 7.963   -23.682 -11.954 1.00 19.53 ?  4674 GLY A N   1 
ATOM   1317 C  CA  . GLY A 1 199 ? 7.294   -22.524 -11.394 1.00 19.19 ?  4674 GLY A CA  1 
ATOM   1318 C  C   . GLY A 1 199 ? 7.862   -22.071 -10.070 1.00 17.61 ?  4674 GLY A C   1 
ATOM   1319 O  O   . GLY A 1 199 ? 7.686   -20.904 -9.703  1.00 22.04 ?  4674 GLY A O   1 
ATOM   1320 N  N   . ASN A 1 200 ? 8.540   -22.959 -9.350  1.00 16.96 ?  4675 ASN A N   1 
ATOM   1321 C  CA  . ASN A 1 200 ? 9.219   -22.580 -8.114  1.00 17.60 ?  4675 ASN A CA  1 
ATOM   1322 C  C   . ASN A 1 200 ? 10.635  -22.078 -8.349  1.00 19.85 ?  4675 ASN A C   1 
ATOM   1323 O  O   . ASN A 1 200 ? 11.360  -21.804 -7.382  1.00 18.26 ?  4675 ASN A O   1 
ATOM   1324 C  CB  . ASN A 1 200 ? 9.226   -23.746 -7.132  1.00 18.83 ?  4675 ASN A CB  1 
ATOM   1325 C  CG  . ASN A 1 200 ? 7.835   -24.106 -6.666  1.00 27.04 ?  4675 ASN A CG  1 
ATOM   1326 O  OD1 . ASN A 1 200 ? 6.953   -23.254 -6.627  1.00 28.24 ?  4675 ASN A OD1 1 
ATOM   1327 N  ND2 . ASN A 1 200 ? 7.624   -25.372 -6.347  1.00 31.58 ?  4675 ASN A ND2 1 
ATOM   1328 N  N   . GLY A 1 201 ? 11.041  -21.971 -9.611  1.00 17.03 ?  4676 GLY A N   1 
ATOM   1329 C  CA  . GLY A 1 201 ? 12.346  -21.463 -9.959  1.00 16.21 ?  4676 GLY A CA  1 
ATOM   1330 C  C   . GLY A 1 201 ? 13.455  -22.479 -9.925  1.00 15.02 ?  4676 GLY A C   1 
ATOM   1331 O  O   . GLY A 1 201 ? 14.620  -22.087 -10.063 1.00 16.11 ?  4676 GLY A O   1 
ATOM   1332 N  N   . VAL A 1 202 ? 13.149  -23.773 -9.777  1.00 15.16 ?  4677 VAL A N   1 
ATOM   1333 C  CA  . VAL A 1 202 ? 14.203  -24.781 -9.826  1.00 14.86 ?  4677 VAL A CA  1 
ATOM   1334 C  C   . VAL A 1 202 ? 14.664  -24.947 -11.268 1.00 15.97 ?  4677 VAL A C   1 
ATOM   1335 O  O   . VAL A 1 202 ? 13.845  -25.031 -12.194 1.00 15.19 ?  4677 VAL A O   1 
ATOM   1336 C  CB  . VAL A 1 202 ? 13.738  -26.117 -9.237  1.00 17.26 ?  4677 VAL A CB  1 
ATOM   1337 C  CG1 . VAL A 1 202 ? 14.923  -27.053 -9.117  1.00 17.78 ?  4677 VAL A CG1 1 
ATOM   1338 C  CG2 . VAL A 1 202 ? 13.125  -25.907 -7.859  1.00 17.37 ?  4677 VAL A CG2 1 
ATOM   1339 N  N   . VAL A 1 203 ? 15.982  -24.969 -11.465 1.00 13.86 ?  4678 VAL A N   1 
ATOM   1340 C  CA  . VAL A 1 203 ? 16.590  -25.037 -12.795 1.00 15.60 ?  4678 VAL A CA  1 
ATOM   1341 C  C   . VAL A 1 203 ? 17.182  -26.424 -12.994 1.00 15.08 ?  4678 VAL A C   1 
ATOM   1342 O  O   . VAL A 1 203 ? 17.919  -26.925 -12.136 1.00 15.01 ?  4678 VAL A O   1 
ATOM   1343 C  CB  . VAL A 1 203 ? 17.655  -23.946 -12.968 1.00 14.54 ?  4678 VAL A CB  1 
ATOM   1344 C  CG1 . VAL A 1 203 ? 18.225  -23.981 -14.369 1.00 14.96 ?  4678 VAL A CG1 1 
ATOM   1345 C  CG2 . VAL A 1 203 ? 17.056  -22.587 -12.657 1.00 15.15 ?  4678 VAL A CG2 1 
ATOM   1346 N  N   . TYR A 1 204 ? 16.865  -27.037 -14.136 1.00 15.16 ?  4679 TYR A N   1 
ATOM   1347 C  CA  . TYR A 1 204 ? 17.335  -28.367 -14.497 1.00 16.48 ?  4679 TYR A CA  1 
ATOM   1348 C  C   . TYR A 1 204 ? 18.062  -28.293 -15.834 1.00 15.31 ?  4679 TYR A C   1 
ATOM   1349 O  O   . TYR A 1 204 ? 17.713  -27.486 -16.700 1.00 17.15 ?  4679 TYR A O   1 
ATOM   1350 C  CB  . TYR A 1 204 ? 16.139  -29.320 -14.680 1.00 18.10 ?  4679 TYR A CB  1 
ATOM   1351 C  CG  . TYR A 1 204 ? 15.245  -29.441 -13.460 1.00 17.85 ?  4679 TYR A CG  1 
ATOM   1352 C  CD1 . TYR A 1 204 ? 14.189  -28.562 -13.268 1.00 19.23 ?  4679 TYR A CD1 1 
ATOM   1353 C  CD2 . TYR A 1 204 ? 15.462  -30.428 -12.506 1.00 19.21 ?  4679 TYR A CD2 1 
ATOM   1354 C  CE1 . TYR A 1 204 ? 13.365  -28.659 -12.156 1.00 20.45 ?  4679 TYR A CE1 1 
ATOM   1355 C  CE2 . TYR A 1 204 ? 14.641  -30.530 -11.375 1.00 21.26 ?  4679 TYR A CE2 1 
ATOM   1356 C  CZ  . TYR A 1 204 ? 13.604  -29.637 -11.223 1.00 23.20 ?  4679 TYR A CZ  1 
ATOM   1357 O  OH  . TYR A 1 204 ? 12.781  -29.717 -10.121 1.00 25.62 ?  4679 TYR A OH  1 
ATOM   1358 N  N   . ASP A 1 205 ? 19.055  -29.165 -16.007 1.00 15.82 ?  4680 ASP A N   1 
ATOM   1359 C  CA  . ASP A 1 205 ? 19.620  -29.338 -17.340 1.00 15.29 ?  4680 ASP A CA  1 
ATOM   1360 C  C   . ASP A 1 205 ? 18.694  -30.196 -18.201 1.00 18.74 ?  4680 ASP A C   1 
ATOM   1361 O  O   . ASP A 1 205 ? 17.638  -30.665 -17.763 1.00 19.98 ?  4680 ASP A O   1 
ATOM   1362 C  CB  . ASP A 1 205 ? 21.079  -29.807 -17.270 1.00 16.63 ?  4680 ASP A CB  1 
ATOM   1363 C  CG  . ASP A 1 205 ? 21.244  -31.252 -16.792 1.00 20.85 ?  4680 ASP A CG  1 
ATOM   1364 O  OD1 . ASP A 1 205 ? 20.282  -32.042 -16.810 1.00 20.73 ?  4680 ASP A OD1 1 
ATOM   1365 O  OD2 . ASP A 1 205 ? 22.373  -31.598 -16.402 1.00 24.18 -1 4680 ASP A OD2 1 
ATOM   1366 N  N   . TYR A 1 206 ? 19.097  -30.398 -19.455 1.00 19.14 ?  4681 TYR A N   1 
ATOM   1367 C  CA  . TYR A 1 206 ? 18.254  -31.113 -20.407 1.00 19.69 ?  4681 TYR A CA  1 
ATOM   1368 C  C   . TYR A 1 206 ? 18.050  -32.570 -20.006 1.00 20.75 ?  4681 TYR A C   1 
ATOM   1369 O  O   . TYR A 1 206 ? 17.022  -33.167 -20.346 1.00 25.69 ?  4681 TYR A O   1 
ATOM   1370 C  CB  . TYR A 1 206 ? 18.870  -31.000 -21.804 1.00 19.91 ?  4681 TYR A CB  1 
ATOM   1371 C  CG  . TYR A 1 206 ? 17.989  -31.501 -22.918 1.00 22.41 ?  4681 TYR A CG  1 
ATOM   1372 C  CD1 . TYR A 1 206 ? 16.870  -30.782 -23.316 1.00 25.00 ?  4681 TYR A CD1 1 
ATOM   1373 C  CD2 . TYR A 1 206 ? 18.292  -32.681 -23.594 1.00 23.25 ?  4681 TYR A CD2 1 
ATOM   1374 C  CE1 . TYR A 1 206 ? 16.062  -31.223 -24.348 1.00 28.67 ?  4681 TYR A CE1 1 
ATOM   1375 C  CE2 . TYR A 1 206 ? 17.485  -33.133 -24.632 1.00 24.54 ?  4681 TYR A CE2 1 
ATOM   1376 C  CZ  . TYR A 1 206 ? 16.376  -32.398 -25.003 1.00 25.15 ?  4681 TYR A CZ  1 
ATOM   1377 O  OH  . TYR A 1 206 ? 15.557  -32.824 -26.027 1.00 28.03 ?  4681 TYR A OH  1 
ATOM   1378 N  N   . ASN A 1 207 ? 18.993  -33.146 -19.271 1.00 19.97 ?  4682 ASN A N   1 
ATOM   1379 C  CA  . ASN A 1 207 ? 18.876  -34.529 -18.810 1.00 22.70 ?  4682 ASN A CA  1 
ATOM   1380 C  C   . ASN A 1 207 ? 18.054  -34.664 -17.537 1.00 25.25 ?  4682 ASN A C   1 
ATOM   1381 O  O   . ASN A 1 207 ? 17.872  -35.788 -17.050 1.00 25.36 ?  4682 ASN A O   1 
ATOM   1382 C  CB  . ASN A 1 207 ? 20.264  -35.145 -18.619 1.00 22.80 ?  4682 ASN A CB  1 
ATOM   1383 C  CG  . ASN A 1 207 ? 20.987  -35.347 -19.935 1.00 28.35 ?  4682 ASN A CG  1 
ATOM   1384 O  OD1 . ASN A 1 207 ? 20.357  -35.537 -20.972 1.00 31.09 ?  4682 ASN A OD1 1 
ATOM   1385 N  ND2 . ASN A 1 207 ? 22.309  -35.296 -19.900 1.00 33.29 ?  4682 ASN A ND2 1 
ATOM   1386 N  N   . GLY A 1 208 ? 17.549  -33.560 -16.995 1.00 22.27 ?  4683 GLY A N   1 
ATOM   1387 C  CA  . GLY A 1 208 ? 16.737  -33.603 -15.800 1.00 22.06 ?  4683 GLY A CA  1 
ATOM   1388 C  C   . GLY A 1 208 ? 17.500  -33.485 -14.504 1.00 22.81 ?  4683 GLY A C   1 
ATOM   1389 O  O   . GLY A 1 208 ? 16.895  -33.632 -13.437 1.00 24.85 ?  4683 GLY A O   1 
ATOM   1390 N  N   . ASN A 1 209 ? 18.806  -33.240 -14.550 1.00 24.66 ?  4684 ASN A N   1 
ATOM   1391 C  CA  . ASN A 1 209 ? 19.568  -33.015 -13.331 1.00 23.68 ?  4684 ASN A CA  1 
ATOM   1392 C  C   . ASN A 1 209 ? 19.303  -31.600 -12.828 1.00 20.91 ?  4684 ASN A C   1 
ATOM   1393 O  O   . ASN A 1 209 ? 19.370  -30.634 -13.596 1.00 18.98 ?  4684 ASN A O   1 
ATOM   1394 C  CB  . ASN A 1 209 ? 21.066  -33.196 -13.577 1.00 24.60 ?  4684 ASN A CB  1 
ATOM   1395 C  CG  . ASN A 1 209 ? 21.412  -34.562 -14.147 1.00 30.60 ?  4684 ASN A CG  1 
ATOM   1396 O  OD1 . ASN A 1 209 ? 21.218  -35.589 -13.493 1.00 33.93 ?  4684 ASN A OD1 1 
ATOM   1397 N  ND2 . ASN A 1 209 ? 21.957  -34.577 -15.363 1.00 30.62 ?  4684 ASN A ND2 1 
ATOM   1398 N  N   . GLN A 1 210 ? 18.977  -31.480 -11.545 1.00 20.64 ?  4685 GLN A N   1 
ATOM   1399 C  CA  . GLN A 1 210 ? 18.833  -30.161 -10.940 1.00 18.16 ?  4685 GLN A CA  1 
ATOM   1400 C  C   . GLN A 1 210 ? 20.203  -29.496 -10.852 1.00 19.66 ?  4685 GLN A C   1 
ATOM   1401 O  O   . GLN A 1 210 ? 21.174  -30.110 -10.392 1.00 21.36 ?  4685 GLN A O   1 
ATOM   1402 C  CB  . GLN A 1 210 ? 18.217  -30.299 -9.547  1.00 18.27 ?  4685 GLN A CB  1 
ATOM   1403 C  CG  . GLN A 1 210 ? 17.905  -28.957 -8.880  1.00 19.67 ?  4685 GLN A CG  1 
ATOM   1404 C  CD  . GLN A 1 210 ? 19.051  -28.436 -8.030  1.00 20.47 ?  4685 GLN A CD  1 
ATOM   1405 O  OE1 . GLN A 1 210 ? 19.803  -29.212 -7.432  1.00 27.97 ?  4685 GLN A OE1 1 
ATOM   1406 N  NE2 . GLN A 1 210 ? 19.191  -27.116 -7.967  1.00 19.99 ?  4685 GLN A NE2 1 
ATOM   1407 N  N   . ILE A 1 211 ? 20.291  -28.237 -11.300 1.00 16.03 ?  4686 ILE A N   1 
ATOM   1408 C  CA  . ILE A 1 211 ? 21.585  -27.556 -11.318 1.00 15.68 ?  4686 ILE A CA  1 
ATOM   1409 C  C   . ILE A 1 211 ? 21.596  -26.290 -10.467 1.00 16.20 ?  4686 ILE A C   1 
ATOM   1410 O  O   . ILE A 1 211 ? 22.644  -25.897 -9.949  1.00 17.42 ?  4686 ILE A O   1 
ATOM   1411 C  CB  . ILE A 1 211 ? 22.095  -27.274 -12.748 1.00 16.56 ?  4686 ILE A CB  1 
ATOM   1412 C  CG1 . ILE A 1 211 ? 21.077  -26.467 -13.559 1.00 16.70 ?  4686 ILE A CG1 1 
ATOM   1413 C  CG2 . ILE A 1 211 ? 22.462  -28.592 -13.450 1.00 19.20 ?  4686 ILE A CG2 1 
ATOM   1414 C  CD1 . ILE A 1 211 ? 21.641  -25.858 -14.879 1.00 17.46 ?  4686 ILE A CD1 1 
ATOM   1415 N  N   . GLY A 1 212 ? 20.450  -25.641 -10.317 1.00 15.67 ?  4687 GLY A N   1 
ATOM   1416 C  CA  . GLY A 1 212 ? 20.417  -24.417 -9.543  1.00 14.79 ?  4687 GLY A CA  1 
ATOM   1417 C  C   . GLY A 1 212 ? 19.003  -23.938 -9.334  1.00 13.52 ?  4687 GLY A C   1 
ATOM   1418 O  O   . GLY A 1 212 ? 18.048  -24.703 -9.467  1.00 14.28 ?  4687 GLY A O   1 
ATOM   1419 N  N   . TYR A 1 213 ? 18.883  -22.649 -8.995  1.00 12.72 ?  4688 TYR A N   1 
ATOM   1420 C  CA  . TYR A 1 213 ? 17.600  -22.070 -8.609  1.00 13.32 ?  4688 TYR A CA  1 
ATOM   1421 C  C   . TYR A 1 213 ? 17.572  -20.612 -9.035  1.00 14.34 ?  4688 TYR A C   1 
ATOM   1422 O  O   . TYR A 1 213 ? 18.604  -19.936 -9.035  1.00 18.19 ?  4688 TYR A O   1 
ATOM   1423 C  CB  . TYR A 1 213 ? 17.417  -22.078 -7.076  1.00 12.11 ?  4688 TYR A CB  1 
ATOM   1424 C  CG  . TYR A 1 213 ? 17.465  -23.427 -6.420  1.00 12.78 ?  4688 TYR A CG  1 
ATOM   1425 C  CD1 . TYR A 1 213 ? 16.303  -24.166 -6.239  1.00 14.68 ?  4688 TYR A CD1 1 
ATOM   1426 C  CD2 . TYR A 1 213 ? 18.662  -23.942 -5.944  1.00 14.46 ?  4688 TYR A CD2 1 
ATOM   1427 C  CE1 . TYR A 1 213 ? 16.338  -25.413 -5.632  1.00 18.02 ?  4688 TYR A CE1 1 
ATOM   1428 C  CE2 . TYR A 1 213 ? 18.711  -25.200 -5.327  1.00 17.79 ?  4688 TYR A CE2 1 
ATOM   1429 C  CZ  . TYR A 1 213 ? 17.538  -25.913 -5.176  1.00 17.71 ?  4688 TYR A CZ  1 
ATOM   1430 O  OH  . TYR A 1 213 ? 17.541  -27.155 -4.563  1.00 21.98 ?  4688 TYR A OH  1 
ATOM   1431 N  N   . MET A 1 214 ? 16.375  -20.117 -9.369  1.00 12.23 ?  4689 MET A N   1 
ATOM   1432 C  CA  . MET A 1 214 ? 16.163  -18.690 -9.595  1.00 12.05 ?  4689 MET A CA  1 
ATOM   1433 C  C   . MET A 1 214 ? 15.769  -18.116 -8.239  1.00 14.06 ?  4689 MET A C   1 
ATOM   1434 O  O   . MET A 1 214 ? 14.672  -18.394 -7.743  1.00 15.57 ?  4689 MET A O   1 
ATOM   1435 C  CB  . MET A 1 214 ? 15.084  -18.453 -10.654 1.00 14.75 ?  4689 MET A CB  1 
ATOM   1436 C  CG  . MET A 1 214 ? 15.334  -19.180 -12.001 1.00 14.09 ?  4689 MET A CG  1 
ATOM   1437 S  SD  . MET A 1 214 ? 16.910  -18.754 -12.811 1.00 14.43 ?  4689 MET A SD  1 
ATOM   1438 C  CE  . MET A 1 214 ? 16.593  -17.086 -13.333 1.00 14.21 ?  4689 MET A CE  1 
ATOM   1439 N  N   . ARG A 1 215 ? 16.677  -17.374 -7.608  1.00 11.70 ?  4690 ARG A N   1 
ATOM   1440 C  CA  . ARG A 1 215 ? 16.517  -16.915 -6.235  1.00 12.88 ?  4690 ARG A CA  1 
ATOM   1441 C  C   . ARG A 1 215 ? 16.456  -15.396 -6.167  1.00 12.70 ?  4690 ARG A C   1 
ATOM   1442 O  O   . ARG A 1 215 ? 17.040  -14.701 -7.003  1.00 12.37 ?  4690 ARG A O   1 
ATOM   1443 C  CB  . ARG A 1 215 ? 17.715  -17.371 -5.382  1.00 13.90 ?  4690 ARG A CB  1 
ATOM   1444 C  CG  . ARG A 1 215 ? 17.879  -18.868 -5.225  1.00 12.16 ?  4690 ARG A CG  1 
ATOM   1445 C  CD  . ARG A 1 215 ? 16.558  -19.535 -4.864  1.00 13.96 ?  4690 ARG A CD  1 
ATOM   1446 N  NE  . ARG A 1 215 ? 16.056  -19.058 -3.580  1.00 13.95 ?  4690 ARG A NE  1 
ATOM   1447 C  CZ  . ARG A 1 215 ? 14.817  -19.260 -3.160  1.00 15.74 ?  4690 ARG A CZ  1 
ATOM   1448 N  NH1 . ARG A 1 215 ? 13.931  -19.892 -3.910  1.00 18.91 ?  4690 ARG A NH1 1 
ATOM   1449 N  NH2 . ARG A 1 215 ? 14.453  -18.807 -1.964  1.00 15.71 ?  4690 ARG A NH2 1 
ATOM   1450 N  N   . PRO A 1 216 ? 15.839  -14.842 -5.124  1.00 11.69 ?  4691 PRO A N   1 
ATOM   1451 C  CA  . PRO A 1 216 ? 15.942  -13.400 -4.904  1.00 11.14 ?  4691 PRO A CA  1 
ATOM   1452 C  C   . PRO A 1 216 ? 17.393  -12.947 -4.924  1.00 10.60 ?  4691 PRO A C   1 
ATOM   1453 O  O   . PRO A 1 216 ? 18.284  -13.618 -4.404  1.00 14.13 ?  4691 PRO A O   1 
ATOM   1454 C  CB  . PRO A 1 216 ? 15.322  -13.223 -3.513  1.00 12.70 ?  4691 PRO A CB  1 
ATOM   1455 C  CG  . PRO A 1 216 ? 14.311  -14.321 -3.464  1.00 14.63 ?  4691 PRO A CG  1 
ATOM   1456 C  CD  . PRO A 1 216 ? 14.983  -15.498 -4.118  1.00 13.43 ?  4691 PRO A CD  1 
ATOM   1457 N  N   . ASP A 1 217 ? 17.630  -11.785 -5.528  1.00 12.24 ?  4692 ASP A N   1 
ATOM   1458 C  CA  . ASP A 1 217 ? 18.989  -11.265 -5.573  1.00 13.42 ?  4692 ASP A CA  1 
ATOM   1459 C  C   . ASP A 1 217 ? 19.251  -10.185 -4.536  1.00 14.63 ?  4692 ASP A C   1 
ATOM   1460 O  O   . ASP A 1 217 ? 20.391  -9.736  -4.410  1.00 15.69 ?  4692 ASP A O   1 
ATOM   1461 C  CB  . ASP A 1 217 ? 19.388  -10.800 -6.991  1.00 14.91 ?  4692 ASP A CB  1 
ATOM   1462 C  CG  . ASP A 1 217 ? 18.669  -9.537  -7.445  1.00 15.08 ?  4692 ASP A CG  1 
ATOM   1463 O  OD1 . ASP A 1 217 ? 17.682  -9.103  -6.815  1.00 14.86 ?  4692 ASP A OD1 1 
ATOM   1464 O  OD2 . ASP A 1 217 ? 19.111  -8.974  -8.476  1.00 17.31 -1 4692 ASP A OD2 1 
ATOM   1465 N  N   . GLY A 1 218 ? 18.245  -9.784  -3.765  1.00 13.01 ?  4693 GLY A N   1 
ATOM   1466 C  CA  . GLY A 1 218 ? 18.425  -8.726  -2.803  1.00 14.12 ?  4693 GLY A CA  1 
ATOM   1467 C  C   . GLY A 1 218 ? 18.261  -7.346  -3.374  1.00 13.22 ?  4693 GLY A C   1 
ATOM   1468 O  O   . GLY A 1 218 ? 18.390  -6.363  -2.628  1.00 17.17 ?  4693 GLY A O   1 
ATOM   1469 N  N   . ALA A 1 219 ? 17.950  -7.237  -4.668  1.00 14.35 ?  4694 ALA A N   1 
ATOM   1470 C  CA  . ALA A 1 219 ? 17.697  -5.954  -5.314  1.00 14.02 ?  4694 ALA A CA  1 
ATOM   1471 C  C   . ALA A 1 219 ? 16.316  -5.918  -5.955  1.00 16.60 ?  4694 ALA A C   1 
ATOM   1472 O  O   . ALA A 1 219 ? 16.022  -5.024  -6.757  1.00 21.49 ?  4694 ALA A O   1 
ATOM   1473 C  CB  . ALA A 1 219 ? 18.784  -5.649  -6.342  1.00 16.57 ?  4694 ALA A CB  1 
ATOM   1474 N  N   . GLY A 1 220 ? 15.460  -6.873  -5.605  1.00 15.89 ?  4695 GLY A N   1 
ATOM   1475 C  CA  . GLY A 1 220 ? 14.101  -6.900  -6.106  1.00 15.63 ?  4695 GLY A CA  1 
ATOM   1476 C  C   . GLY A 1 220 ? 13.858  -7.853  -7.254  1.00 15.76 ?  4695 GLY A C   1 
ATOM   1477 O  O   . GLY A 1 220 ? 12.747  -7.857  -7.800  1.00 18.47 ?  4695 GLY A O   1 
ATOM   1478 N  N   . ARG A 1 221 ? 14.848  -8.652  -7.643  1.00 13.72 ?  4696 ARG A N   1 
ATOM   1479 C  CA  . ARG A 1 221 ? 14.767  -9.510  -8.812  1.00 14.83 ?  4696 ARG A CA  1 
ATOM   1480 C  C   . ARG A 1 221 ? 14.992  -10.957 -8.406  1.00 13.15 ?  4696 ARG A C   1 
ATOM   1481 O  O   . ARG A 1 221 ? 15.305  -11.268 -7.254  1.00 13.55 ?  4696 ARG A O   1 
ATOM   1482 C  CB  . ARG A 1 221 ? 15.818  -9.072  -9.842  1.00 17.10 ?  4696 ARG A CB  1 
ATOM   1483 C  CG  . ARG A 1 221 ? 15.604  -7.611  -10.181 1.00 22.09 ?  4696 ARG A CG  1 
ATOM   1484 C  CD  . ARG A 1 221 ? 16.747  -6.989  -10.885 1.00 25.71 ?  4696 ARG A CD  1 
ATOM   1485 N  NE  . ARG A 1 221 ? 17.994  -6.976  -10.126 1.00 20.76 ?  4696 ARG A NE  1 
ATOM   1486 C  CZ  . ARG A 1 221 ? 18.988  -6.153  -10.422 1.00 19.04 ?  4696 ARG A CZ  1 
ATOM   1487 N  NH1 . ARG A 1 221 ? 18.808  -5.133  -11.249 1.00 20.71 ?  4696 ARG A NH1 1 
ATOM   1488 N  NH2 . ARG A 1 221 ? 20.194  -6.375  -9.911  1.00 24.80 ?  4696 ARG A NH2 1 
ATOM   1489 N  N   . TYR A 1 222 ? 14.825  -11.850 -9.379  1.00 13.19 ?  4697 TYR A N   1 
ATOM   1490 C  CA  . TYR A 1 222 ? 15.068  -13.277 -9.217  1.00 13.17 ?  4697 TYR A CA  1 
ATOM   1491 C  C   . TYR A 1 222 ? 16.096  -13.665 -10.258 1.00 15.13 ?  4697 TYR A C   1 
ATOM   1492 O  O   . TYR A 1 222 ? 15.900  -13.390 -11.446 1.00 15.33 ?  4697 TYR A O   1 
ATOM   1493 C  CB  . TYR A 1 222 ? 13.789  -14.085 -9.477  1.00 15.09 ?  4697 TYR A CB  1 
ATOM   1494 C  CG  . TYR A 1 222 ? 12.836  -13.996 -8.317  1.00 13.95 ?  4697 TYR A CG  1 
ATOM   1495 C  CD1 . TYR A 1 222 ? 12.024  -12.899 -8.169  1.00 17.18 ?  4697 TYR A CD1 1 
ATOM   1496 C  CD2 . TYR A 1 222 ? 12.783  -14.995 -7.362  1.00 14.82 ?  4697 TYR A CD2 1 
ATOM   1497 C  CE1 . TYR A 1 222 ? 11.152  -12.789 -7.102  1.00 17.87 ?  4697 TYR A CE1 1 
ATOM   1498 C  CE2 . TYR A 1 222 ? 11.913  -14.903 -6.272  1.00 16.71 ?  4697 TYR A CE2 1 
ATOM   1499 C  CZ  . TYR A 1 222 ? 11.109  -13.789 -6.160  1.00 17.51 ?  4697 TYR A CZ  1 
ATOM   1500 O  OH  . TYR A 1 222 ? 10.239  -13.642 -5.100  1.00 20.61 ?  4697 TYR A OH  1 
ATOM   1501 N  N   . VAL A 1 223 ? 17.183  -14.286 -9.813  1.00 12.99 ?  4698 VAL A N   1 
ATOM   1502 C  CA  . VAL A 1 223 ? 18.372  -14.491 -10.627 1.00 13.18 ?  4698 VAL A CA  1 
ATOM   1503 C  C   . VAL A 1 223 ? 18.940  -15.874 -10.334 1.00 11.88 ?  4698 VAL A C   1 
ATOM   1504 O  O   . VAL A 1 223 ? 18.878  -16.369 -9.202  1.00 13.17 ?  4698 VAL A O   1 
ATOM   1505 C  CB  . VAL A 1 223 ? 19.402  -13.381 -10.311 1.00 18.48 ?  4698 VAL A CB  1 
ATOM   1506 C  CG1 . VAL A 1 223 ? 20.677  -13.633 -10.990 1.00 20.80 ?  4698 VAL A CG1 1 
ATOM   1507 C  CG2 . VAL A 1 223 ? 18.879  -12.019 -10.736 1.00 18.28 ?  4698 VAL A CG2 1 
ATOM   1508 N  N   . TYR A 1 224 ? 19.513  -16.503 -11.363 1.00 13.67 ?  4699 TYR A N   1 
ATOM   1509 C  CA  . TYR A 1 224 ? 20.088  -17.829 -11.207 1.00 11.89 ?  4699 TYR A CA  1 
ATOM   1510 C  C   . TYR A 1 224 ? 21.150  -17.838 -10.109 1.00 11.91 ?  4699 TYR A C   1 
ATOM   1511 O  O   . TYR A 1 224 ? 21.957  -16.906 -9.986  1.00 13.81 ?  4699 TYR A O   1 
ATOM   1512 C  CB  . TYR A 1 224 ? 20.732  -18.272 -12.531 1.00 13.69 ?  4699 TYR A CB  1 
ATOM   1513 C  CG  . TYR A 1 224 ? 21.325  -19.646 -12.462 1.00 11.99 ?  4699 TYR A CG  1 
ATOM   1514 C  CD1 . TYR A 1 224 ? 20.507  -20.759 -12.435 1.00 15.79 ?  4699 TYR A CD1 1 
ATOM   1515 C  CD2 . TYR A 1 224 ? 22.711  -19.843 -12.435 1.00 12.52 ?  4699 TYR A CD2 1 
ATOM   1516 C  CE1 . TYR A 1 224 ? 21.019  -22.025 -12.356 1.00 13.60 ?  4699 TYR A CE1 1 
ATOM   1517 C  CE2 . TYR A 1 224 ? 23.244  -21.123 -12.359 1.00 14.33 ?  4699 TYR A CE2 1 
ATOM   1518 C  CZ  . TYR A 1 224 ? 22.393  -22.209 -12.338 1.00 13.67 ?  4699 TYR A CZ  1 
ATOM   1519 O  OH  . TYR A 1 224 ? 22.858  -23.508 -12.271 1.00 14.89 ?  4699 TYR A OH  1 
ATOM   1520 N  N   . ALA A 1 225 ? 21.166  -18.919 -9.335  1.00 12.22 ?  4700 ALA A N   1 
ATOM   1521 C  CA  . ALA A 1 225 ? 22.235  -19.155 -8.374  1.00 12.41 ?  4700 ALA A CA  1 
ATOM   1522 C  C   . ALA A 1 225 ? 22.335  -20.653 -8.115  1.00 12.13 ?  4700 ALA A C   1 
ATOM   1523 O  O   . ALA A 1 225 ? 21.397  -21.409 -8.365  1.00 14.88 ?  4700 ALA A O   1 
ATOM   1524 C  CB  . ALA A 1 225 ? 21.974  -18.413 -7.057  1.00 15.12 ?  4700 ALA A CB  1 
ATOM   1525 N  N   . THR A 1 226 ? 23.496  -21.077 -7.626  1.00 12.21 ?  4701 THR A N   1 
ATOM   1526 C  CA  . THR A 1 226 ? 23.686  -22.467 -7.245  1.00 13.34 ?  4701 THR A CA  1 
ATOM   1527 C  C   . THR A 1 226 ? 23.897  -22.564 -5.741  1.00 12.16 ?  4701 THR A C   1 
ATOM   1528 O  O   . THR A 1 226 ? 24.459  -21.662 -5.106  1.00 13.76 ?  4701 THR A O   1 
ATOM   1529 C  CB  . THR A 1 226 ? 24.852  -23.123 -7.997  1.00 14.82 ?  4701 THR A CB  1 
ATOM   1530 O  OG1 . THR A 1 226 ? 26.073  -22.459 -7.668  1.00 16.94 ?  4701 THR A OG1 1 
ATOM   1531 C  CG2 . THR A 1 226 ? 24.610  -23.054 -9.525  1.00 17.65 ?  4701 THR A CG2 1 
ATOM   1532 N  N   . LEU A 1 227 ? 23.425  -23.663 -5.176  1.00 12.50 ?  4702 LEU A N   1 
ATOM   1533 C  CA  . LEU A 1 227 ? 23.595  -23.896 -3.755  1.00 12.23 ?  4702 LEU A CA  1 
ATOM   1534 C  C   . LEU A 1 227 ? 25.030  -24.329 -3.488  1.00 15.60 ?  4702 LEU A C   1 
ATOM   1535 O  O   . LEU A 1 227 ? 25.578  -25.181 -4.197  1.00 16.56 ?  4702 LEU A O   1 
ATOM   1536 C  CB  . LEU A 1 227 ? 22.621  -24.977 -3.303  1.00 15.47 ?  4702 LEU A CB  1 
ATOM   1537 C  CG  . LEU A 1 227 ? 22.491  -25.236 -1.807  1.00 15.36 ?  4702 LEU A CG  1 
ATOM   1538 C  CD1 . LEU A 1 227 ? 21.876  -24.033 -1.079  1.00 13.86 ?  4702 LEU A CD1 1 
ATOM   1539 C  CD2 . LEU A 1 227 ? 21.663  -26.483 -1.614  1.00 16.99 ?  4702 LEU A CD2 1 
ATOM   1540 N  N   . ALA A 1 228 ? 25.648  -23.752 -2.468  1.00 13.51 ?  4703 ALA A N   1 
ATOM   1541 C  CA  . ALA A 1 228 ? 27.024  -24.080 -2.137  1.00 14.92 ?  4703 ALA A CA  1 
ATOM   1542 C  C   . ALA A 1 228 ? 27.136  -24.335 -0.643  1.00 15.06 ?  4703 ALA A C   1 
ATOM   1543 O  O   . ALA A 1 228 ? 26.286  -23.915 0.141   1.00 14.25 ?  4703 ALA A O   1 
ATOM   1544 C  CB  . ALA A 1 228 ? 27.970  -22.953 -2.553  1.00 19.05 ?  4703 ALA A CB  1 
ATOM   1545 N  N   . GLY A 1 229 ? 28.217  -24.987 -0.248  1.00 16.42 ?  4704 GLY A N   1 
ATOM   1546 C  CA  . GLY A 1 229 ? 28.437  -25.339 1.138   1.00 16.72 ?  4704 GLY A CA  1 
ATOM   1547 C  C   . GLY A 1 229 ? 28.092  -26.789 1.415   1.00 15.86 ?  4704 GLY A C   1 
ATOM   1548 O  O   . GLY A 1 229 ? 27.458  -27.484 0.617   1.00 17.65 ?  4704 GLY A O   1 
ATOM   1549 N  N   . THR A 1 230 ? 28.511  -27.250 2.597   1.00 16.08 ?  4705 THR A N   1 
ATOM   1550 C  CA  . THR A 1 230 ? 28.282  -28.647 2.937   1.00 18.29 ?  4705 THR A CA  1 
ATOM   1551 C  C   . THR A 1 230 ? 26.892  -28.905 3.494   1.00 19.63 ?  4705 THR A C   1 
ATOM   1552 O  O   . THR A 1 230 ? 26.414  -30.045 3.442   1.00 20.22 ?  4705 THR A O   1 
ATOM   1553 C  CB  . THR A 1 230 ? 29.281  -29.098 3.994   1.00 21.78 ?  4705 THR A CB  1 
ATOM   1554 O  OG1 . THR A 1 230 ? 29.029  -28.368 5.203   1.00 18.56 ?  4705 THR A OG1 1 
ATOM   1555 C  CG2 . THR A 1 230 ? 30.709  -28.838 3.530   1.00 22.27 ?  4705 THR A CG2 1 
ATOM   1556 N  N   . GLY A 1 231 ? 26.250  -27.892 4.065   1.00 16.19 ?  4706 GLY A N   1 
ATOM   1557 C  CA  . GLY A 1 231 ? 24.971  -28.096 4.702   1.00 16.19 ?  4706 GLY A CA  1 
ATOM   1558 C  C   . GLY A 1 231 ? 25.046  -28.570 6.133   1.00 16.90 ?  4706 GLY A C   1 
ATOM   1559 O  O   . GLY A 1 231 ? 24.011  -28.618 6.804   1.00 17.48 ?  4706 GLY A O   1 
ATOM   1560 N  N   . ASN A 1 232 ? 26.232  -28.917 6.628   1.00 16.57 ?  4707 ASN A N   1 
ATOM   1561 C  CA  . ASN A 1 232 ? 26.352  -29.422 7.990   1.00 17.91 ?  4707 ASN A CA  1 
ATOM   1562 C  C   . ASN A 1 232 ? 27.597  -28.896 8.692   1.00 19.37 ?  4707 ASN A C   1 
ATOM   1563 O  O   . ASN A 1 232 ? 27.913  -29.364 9.796   1.00 24.58 ?  4707 ASN A O   1 
ATOM   1564 C  CB  . ASN A 1 232 ? 26.336  -30.953 7.996   1.00 20.08 ?  4707 ASN A CB  1 
ATOM   1565 C  CG  . ASN A 1 232 ? 27.384  -31.538 7.070   1.00 24.84 ?  4707 ASN A CG  1 
ATOM   1566 O  OD1 . ASN A 1 232 ? 28.507  -31.042 7.000   1.00 26.40 ?  4707 ASN A OD1 1 
ATOM   1567 N  ND2 . ASN A 1 232 ? 27.011  -32.580 6.329   1.00 31.67 ?  4707 ASN A ND2 1 
ATOM   1568 N  N   . SER A 1 233 ? 28.300  -27.940 8.095   1.00 20.64 ?  4708 SER A N   1 
ATOM   1569 C  CA  . SER A 1 233 ? 29.462  -27.305 8.690   1.00 18.53 ?  4708 SER A CA  1 
ATOM   1570 C  C   . SER A 1 233 ? 29.568  -25.901 8.108   1.00 16.34 ?  4708 SER A C   1 
ATOM   1571 O  O   . SER A 1 233 ? 28.864  -25.546 7.154   1.00 16.46 ?  4708 SER A O   1 
ATOM   1572 C  CB  . SER A 1 233 ? 30.742  -28.107 8.434   1.00 22.05 ?  4708 SER A CB  1 
ATOM   1573 O  OG  . SER A 1 233 ? 31.015  -28.165 7.050   1.00 22.78 ?  4708 SER A OG  1 
ATOM   1574 N  N   . THR A 1 234 ? 30.456  -25.108 8.696   1.00 16.99 ?  4709 THR A N   1 
ATOM   1575 C  CA  . THR A 1 234 ? 30.594  -23.692 8.364   1.00 15.60 ?  4709 THR A CA  1 
ATOM   1576 C  C   . THR A 1 234 ? 32.040  -23.400 8.007   1.00 18.26 ?  4709 THR A C   1 
ATOM   1577 O  O   . THR A 1 234 ? 32.954  -23.744 8.761   1.00 23.98 ?  4709 THR A O   1 
ATOM   1578 C  CB  . THR A 1 234 ? 30.185  -22.802 9.550   1.00 17.14 ?  4709 THR A CB  1 
ATOM   1579 O  OG1 . THR A 1 234 ? 28.865  -23.153 9.974   1.00 21.85 ?  4709 THR A OG1 1 
ATOM   1580 C  CG2 . THR A 1 234 ? 30.197  -21.327 9.138   1.00 17.01 ?  4709 THR A CG2 1 
ATOM   1581 N  N   . SER A 1 235 ? 32.245  -22.735 6.880   1.00 17.09 ?  4710 SER A N   1 
ATOM   1582 C  CA  . SER A 1 235 ? 33.571  -22.333 6.452   1.00 19.37 ?  4710 SER A CA  1 
ATOM   1583 C  C   . SER A 1 235 ? 33.656  -20.815 6.384   1.00 17.21 ?  4710 SER A C   1 
ATOM   1584 O  O   . SER A 1 235 ? 32.651  -20.101 6.445   1.00 16.86 ?  4710 SER A O   1 
ATOM   1585 C  CB  . SER A 1 235 ? 33.881  -22.896 5.063   1.00 17.79 ?  4710 SER A CB  1 
ATOM   1586 O  OG  . SER A 1 235 ? 33.015  -22.326 4.093   1.00 19.25 ?  4710 SER A OG  1 
ATOM   1587 N  N   . SER A 1 236 ? 34.882  -20.327 6.234   1.00 17.53 ?  4711 SER A N   1 
ATOM   1588 C  CA  . SER A 1 236 ? 35.092  -18.898 6.039   1.00 15.92 ?  4711 SER A CA  1 
ATOM   1589 C  C   . SER A 1 236 ? 34.316  -18.397 4.826   1.00 16.32 ?  4711 SER A C   1 
ATOM   1590 O  O   . SER A 1 236 ? 33.790  -17.279 4.832   1.00 17.24 ?  4711 SER A O   1 
ATOM   1591 C  CB  . SER A 1 236 ? 36.589  -18.633 5.864   1.00 20.02 ?  4711 SER A CB  1 
ATOM   1592 O  OG  . SER A 1 236 ? 37.253  -18.767 7.112   1.00 27.56 ?  4711 SER A OG  1 
ATOM   1593 N  N   . THR A 1 237 ? 34.255  -19.207 3.768   1.00 16.76 ?  4712 THR A N   1 
ATOM   1594 C  CA  . THR A 1 237 ? 33.517  -18.808 2.574   1.00 12.34 ?  4712 THR A CA  1 
ATOM   1595 C  C   . THR A 1 237 ? 32.020  -18.731 2.854   1.00 13.82 ?  4712 THR A C   1 
ATOM   1596 O  O   . THR A 1 237 ? 31.348  -17.808 2.380   1.00 14.12 ?  4712 THR A O   1 
ATOM   1597 C  CB  . THR A 1 237 ? 33.815  -19.791 1.447   1.00 13.37 ?  4712 THR A CB  1 
ATOM   1598 O  OG1 . THR A 1 237 ? 35.219  -19.727 1.180   1.00 18.81 ?  4712 THR A OG1 1 
ATOM   1599 C  CG2 . THR A 1 237 ? 33.051  -19.451 0.165   1.00 16.81 ?  4712 THR A CG2 1 
ATOM   1600 N  N   . THR A 1 238 ? 31.484  -19.697 3.613   1.00 14.83 ?  4713 THR A N   1 
ATOM   1601 C  CA  . THR A 1 238 ? 30.070  -19.625 3.974   1.00 15.11 ?  4713 THR A CA  1 
ATOM   1602 C  C   . THR A 1 238 ? 29.778  -18.319 4.690   1.00 14.52 ?  4713 THR A C   1 
ATOM   1603 O  O   . THR A 1 238 ? 28.792  -17.631 4.381   1.00 15.33 ?  4713 THR A O   1 
ATOM   1604 C  CB  . THR A 1 238 ? 29.685  -20.784 4.886   1.00 15.22 ?  4713 THR A CB  1 
ATOM   1605 O  OG1 . THR A 1 238 ? 30.048  -22.020 4.271   1.00 20.98 ?  4713 THR A OG1 1 
ATOM   1606 C  CG2 . THR A 1 238 ? 28.170  -20.786 5.088   1.00 15.36 ?  4713 THR A CG2 1 
ATOM   1607 N  N   . ILE A 1 239 ? 30.636  -17.963 5.648   1.00 15.48 ?  4714 ILE A N   1 
ATOM   1608 C  CA  . ILE A 1 239 ? 30.447  -16.738 6.417   1.00 15.86 ?  4714 ILE A CA  1 
ATOM   1609 C  C   . ILE A 1 239 ? 30.572  -15.515 5.519   1.00 15.93 ?  4714 ILE A C   1 
ATOM   1610 O  O   . ILE A 1 239 ? 29.759  -14.589 5.599   1.00 15.57 ?  4714 ILE A O   1 
ATOM   1611 C  CB  . ILE A 1 239 ? 31.420  -16.687 7.608   1.00 17.65 ?  4714 ILE A CB  1 
ATOM   1612 C  CG1 . ILE A 1 239 ? 31.089  -17.810 8.592   1.00 17.51 ?  4714 ILE A CG1 1 
ATOM   1613 C  CG2 . ILE A 1 239 ? 31.349  -15.324 8.292   1.00 19.00 ?  4714 ILE A CG2 1 
ATOM   1614 C  CD1 . ILE A 1 239 ? 32.153  -18.029 9.649   1.00 22.01 ?  4714 ILE A CD1 1 
ATOM   1615 N  N   . ALA A 1 240 ? 31.598  -15.485 4.649   1.00 14.75 ?  4715 ALA A N   1 
ATOM   1616 C  CA  . ALA A 1 240 ? 31.797  -14.303 3.815   1.00 14.11 ?  4715 ALA A CA  1 
ATOM   1617 C  C   . ALA A 1 240 ? 30.593  -14.065 2.913   1.00 14.70 ?  4715 ALA A C   1 
ATOM   1618 O  O   . ALA A 1 240 ? 30.173  -12.918 2.707   1.00 14.73 ?  4715 ALA A O   1 
ATOM   1619 C  CB  . ALA A 1 240 ? 33.091  -14.438 3.007   1.00 15.83 ?  4715 ALA A CB  1 
ATOM   1620 N  N   . ASN A 1 241 ? 30.013  -15.145 2.384   1.00 13.00 ?  4716 ASN A N   1 
ATOM   1621 C  CA  . ASN A 1 241 ? 28.837  -15.006 1.536   1.00 13.30 ?  4716 ASN A CA  1 
ATOM   1622 C  C   . ASN A 1 241 ? 27.632  -14.548 2.332   1.00 14.28 ?  4716 ASN A C   1 
ATOM   1623 O  O   . ASN A 1 241 ? 26.795  -13.790 1.810   1.00 14.11 ?  4716 ASN A O   1 
ATOM   1624 C  CB  . ASN A 1 241 ? 28.542  -16.334 0.851   1.00 11.69 ?  4716 ASN A CB  1 
ATOM   1625 C  CG  . ASN A 1 241 ? 29.392  -16.528 -0.382  1.00 13.07 ?  4716 ASN A CG  1 
ATOM   1626 O  OD1 . ASN A 1 241 ? 30.570  -16.949 -0.301  1.00 16.88 ?  4716 ASN A OD1 1 
ATOM   1627 N  ND2 . ASN A 1 241 ? 28.830  -16.192 -1.526  1.00 11.94 ?  4716 ASN A ND2 1 
ATOM   1628 N  N   . SER A 1 242 ? 27.520  -15.030 3.581   1.00 13.61 ?  4717 SER A N   1 
ATOM   1629 C  CA  . SER A 1 242 ? 26.435  -14.616 4.464   1.00 12.80 ?  4717 SER A CA  1 
ATOM   1630 C  C   . SER A 1 242 ? 26.534  -13.130 4.772   1.00 14.03 ?  4717 SER A C   1 
ATOM   1631 O  O   . SER A 1 242 ? 25.532  -12.415 4.737   1.00 13.56 ?  4717 SER A O   1 
ATOM   1632 C  CB  . SER A 1 242 ? 26.505  -15.417 5.753   1.00 12.10 ?  4717 SER A CB  1 
ATOM   1633 O  OG  . SER A 1 242 ? 26.395  -16.795 5.487   1.00 14.05 ?  4717 SER A OG  1 
ATOM   1634 N  N   . VAL A 1 243 ? 27.748  -12.649 5.059   1.00 13.39 ?  4718 VAL A N   1 
ATOM   1635 C  CA  . VAL A 1 243 ? 27.936  -11.233 5.361   1.00 16.30 ?  4718 VAL A CA  1 
ATOM   1636 C  C   . VAL A 1 243 ? 27.646  -10.380 4.129   1.00 15.08 ?  4718 VAL A C   1 
ATOM   1637 O  O   . VAL A 1 243 ? 27.067  -9.294  4.230   1.00 16.74 ?  4718 VAL A O   1 
ATOM   1638 C  CB  . VAL A 1 243 ? 29.352  -11.004 5.927   1.00 16.83 ?  4718 VAL A CB  1 
ATOM   1639 C  CG1 . VAL A 1 243 ? 29.673  -9.520  6.008   1.00 21.11 ?  4718 VAL A CG1 1 
ATOM   1640 C  CG2 . VAL A 1 243 ? 29.485  -11.639 7.296   1.00 17.00 ?  4718 VAL A CG2 1 
ATOM   1641 N  N   . ALA A 1 244 ? 28.010  -10.870 2.940   1.00 16.51 ?  4719 ALA A N   1 
ATOM   1642 C  CA  . ALA A 1 244 ? 27.720  -10.114 1.725   1.00 14.83 ?  4719 ALA A CA  1 
ATOM   1643 C  C   . ALA A 1 244 ? 26.217  -9.984  1.505   1.00 16.26 ?  4719 ALA A C   1 
ATOM   1644 O  O   . ALA A 1 244 ? 25.713  -8.902  1.176   1.00 19.21 ?  4719 ALA A O   1 
ATOM   1645 C  CB  . ALA A 1 244 ? 28.392  -10.789 0.525   1.00 18.26 ?  4719 ALA A CB  1 
ATOM   1646 N  N   . GLY A 1 245 ? 25.487  -11.089 1.658   1.00 15.56 ?  4720 GLY A N   1 
ATOM   1647 C  CA  . GLY A 1 245 ? 24.038  -11.017 1.577   1.00 14.07 ?  4720 GLY A CA  1 
ATOM   1648 C  C   . GLY A 1 245 ? 23.454  -10.061 2.595   1.00 16.28 ?  4720 GLY A C   1 
ATOM   1649 O  O   . GLY A 1 245 ? 22.513  -9.325  2.298   1.00 16.69 ?  4720 GLY A O   1 
ATOM   1650 N  N   . PHE A 1 246 ? 23.990  -10.079 3.818   1.00 15.53 ?  4721 PHE A N   1 
ATOM   1651 C  CA  . PHE A 1 246 ? 23.483  -9.208  4.867   1.00 13.61 ?  4721 PHE A CA  1 
ATOM   1652 C  C   . PHE A 1 246 ? 23.595  -7.747  4.467   1.00 15.41 ?  4721 PHE A C   1 
ATOM   1653 O  O   . PHE A 1 246 ? 22.718  -6.944  4.789   1.00 14.15 ?  4721 PHE A O   1 
ATOM   1654 C  CB  . PHE A 1 246 ? 24.247  -9.457  6.162   1.00 14.18 ?  4721 PHE A CB  1 
ATOM   1655 C  CG  . PHE A 1 246 ? 23.647  -8.766  7.348   1.00 14.36 ?  4721 PHE A CG  1 
ATOM   1656 C  CD1 . PHE A 1 246 ? 22.453  -9.228  7.911   1.00 15.59 ?  4721 PHE A CD1 1 
ATOM   1657 C  CD2 . PHE A 1 246 ? 24.248  -7.641  7.877   1.00 14.18 ?  4721 PHE A CD2 1 
ATOM   1658 C  CE1 . PHE A 1 246 ? 21.898  -8.587  9.010   1.00 17.57 ?  4721 PHE A CE1 1 
ATOM   1659 C  CE2 . PHE A 1 246 ? 23.685  -6.981  8.982   1.00 15.89 ?  4721 PHE A CE2 1 
ATOM   1660 C  CZ  . PHE A 1 246 ? 22.503  -7.462  9.537   1.00 16.73 ?  4721 PHE A CZ  1 
ATOM   1661 N  N   . GLY A 1 247 ? 24.683  -7.380  3.788   1.00 15.31 ?  4722 GLY A N   1 
ATOM   1662 C  CA  . GLY A 1 247 ? 24.855  -5.988  3.398   1.00 15.33 ?  4722 GLY A CA  1 
ATOM   1663 C  C   . GLY A 1 247 ? 23.804  -5.499  2.421   1.00 16.38 ?  4722 GLY A C   1 
ATOM   1664 O  O   . GLY A 1 247 ? 23.514  -4.303  2.365   1.00 17.07 ?  4722 GLY A O   1 
ATOM   1665 N  N   . LEU A 1 248 ? 23.239  -6.401  1.620   1.00 15.26 ?  4723 LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 248 ? 22.130  -6.004  0.755   1.00 15.80 ?  4723 LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 248 ? 20.893  -5.654  1.565   1.00 15.29 ?  4723 LEU A C   1 
ATOM   1668 O  O   . LEU A 1 248 ? 20.130  -4.759  1.191   1.00 16.78 ?  4723 LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 248 ? 21.800  -7.133  -0.221  1.00 14.27 ?  4723 LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 248 ? 22.938  -7.492  -1.179  1.00 18.09 ?  4723 LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 248 ? 22.654  -8.803  -1.909  1.00 18.14 ?  4723 LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 248 ? 23.115  -6.352  -2.150  1.00 20.16 ?  4723 LEU A CD2 1 
ATOM   1673 N  N   . LEU A 1 249 ? 20.670  -6.364  2.671   1.00 14.33 ?  4724 LEU A N   1 
ATOM   1674 C  CA  . LEU A 1 249 ? 19.533  -6.069  3.533   1.00 13.57 ?  4724 LEU A CA  1 
ATOM   1675 C  C   . LEU A 1 249 ? 19.724  -4.747  4.270   1.00 15.50 ?  4724 LEU A C   1 
ATOM   1676 O  O   . LEU A 1 249 ? 18.854  -3.867  4.219   1.00 17.42 ?  4724 LEU A O   1 
ATOM   1677 C  CB  . LEU A 1 249 ? 19.324  -7.232  4.508   1.00 14.13 ?  4724 LEU A CB  1 
ATOM   1678 C  CG  . LEU A 1 249 ? 18.250  -7.032  5.563   1.00 12.85 ?  4724 LEU A CG  1 
ATOM   1679 C  CD1 . LEU A 1 249 ? 16.865  -6.816  4.916   1.00 15.11 ?  4724 LEU A CD1 1 
ATOM   1680 C  CD2 . LEU A 1 249 ? 18.248  -8.254  6.468   1.00 14.56 ?  4724 LEU A CD2 1 
ATOM   1681 N  N   . THR A 1 250 ? 20.856  -4.576  4.965   1.00 14.17 ?  4725 THR A N   1 
ATOM   1682 C  CA  . THR A 1 250 ? 21.047  -3.307  5.661   1.00 17.54 ?  4725 THR A CA  1 
ATOM   1683 C  C   . THR A 1 250 ? 21.145  -2.154  4.680   1.00 18.88 ?  4725 THR A C   1 
ATOM   1684 O  O   . THR A 1 250 ? 20.744  -1.027  5.005   1.00 18.44 ?  4725 THR A O   1 
ATOM   1685 C  CB  . THR A 1 250 ? 22.260  -3.349  6.588   1.00 19.29 ?  4725 THR A CB  1 
ATOM   1686 O  OG1 . THR A 1 250 ? 23.438  -3.703  5.851   1.00 20.22 ?  4725 THR A OG1 1 
ATOM   1687 C  CG2 . THR A 1 250 ? 22.031  -4.357  7.706   1.00 21.18 ?  4725 THR A CG2 1 
ATOM   1688 N  N   . GLY A 1 251 ? 21.653  -2.424  3.476   1.00 16.90 ?  4726 GLY A N   1 
ATOM   1689 C  CA  . GLY A 1 251 ? 21.791  -1.402  2.455   1.00 17.84 ?  4726 GLY A CA  1 
ATOM   1690 C  C   . GLY A 1 251 ? 20.477  -0.806  1.996   1.00 18.59 ?  4726 GLY A C   1 
ATOM   1691 O  O   . GLY A 1 251 ? 20.474  0.273   1.395   1.00 23.23 ?  4726 GLY A O   1 
ATOM   1692 N  N   . MET A 1 252 ? 19.364  -1.488  2.241   1.00 19.04 ?  4727 MET A N   1 
ATOM   1693 C  CA  . MET A 1 252 ? 18.049  -0.927  1.977   1.00 19.42 ?  4727 MET A CA  1 
ATOM   1694 C  C   . MET A 1 252 ? 17.620  0.070   3.044   1.00 21.28 ?  4727 MET A C   1 
ATOM   1695 O  O   . MET A 1 252 ? 16.517  0.618   2.944   1.00 25.90 ?  4727 MET A O   1 
ATOM   1696 C  CB  . MET A 1 252 ? 16.997  -2.038  1.864   1.00 18.96 ?  4727 MET A CB  1 
ATOM   1697 C  CG  . MET A 1 252 ? 17.201  -3.024  0.702   1.00 17.88 ?  4727 MET A CG  1 
ATOM   1698 S  SD  . MET A 1 252 ? 17.423  -2.175  -0.898  1.00 23.57 ?  4727 MET A SD  1 
ATOM   1699 C  CE  . MET A 1 252 ? 15.893  -1.279  -1.046  1.00 23.14 ?  4727 MET A CE  1 
ATOM   1700 N  N   . GLY A 1 253 ? 18.456  0.310   4.054   1.00 18.93 ?  4728 GLY A N   1 
ATOM   1701 C  CA  . GLY A 1 253 ? 18.090  1.153   5.178   1.00 20.14 ?  4728 GLY A CA  1 
ATOM   1702 C  C   . GLY A 1 253 ? 17.229  0.410   6.177   1.00 20.09 ?  4728 GLY A C   1 
ATOM   1703 O  O   . GLY A 1 253 ? 16.102  0.826   6.472   1.00 22.21 ?  4728 GLY A O   1 
ATOM   1704 N  N   . VAL A 1 254 ? 17.751  -0.705  6.687   1.00 16.24 ?  4729 VAL A N   1 
ATOM   1705 C  CA  . VAL A 1 254 ? 17.032  -1.606  7.582   1.00 14.69 ?  4729 VAL A CA  1 
ATOM   1706 C  C   . VAL A 1 254 ? 17.872  -1.814  8.830   1.00 14.80 ?  4729 VAL A C   1 
ATOM   1707 O  O   . VAL A 1 254 ? 19.077  -2.081  8.732   1.00 17.54 ?  4729 VAL A O   1 
ATOM   1708 C  CB  . VAL A 1 254 ? 16.781  -2.967  6.901   1.00 14.09 ?  4729 VAL A CB  1 
ATOM   1709 C  CG1 . VAL A 1 254 ? 16.056  -3.905  7.856   1.00 15.08 ?  4729 VAL A CG1 1 
ATOM   1710 C  CG2 . VAL A 1 254 ? 15.987  -2.784  5.613   1.00 16.78 ?  4729 VAL A CG2 1 
ATOM   1711 N  N   . THR A 1 255 ? 17.242  -1.699  9.993   1.00 15.49 ?  4730 THR A N   1 
ATOM   1712 C  CA  . THR A 1 255 ? 17.878  -2.019  11.264  1.00 15.10 ?  4730 THR A CA  1 
ATOM   1713 C  C   . THR A 1 255 ? 17.582  -3.476  11.574  1.00 15.28 ?  4730 THR A C   1 
ATOM   1714 O  O   . THR A 1 255 ? 16.417  -3.897  11.552  1.00 16.49 ?  4730 THR A O   1 
ATOM   1715 C  CB  . THR A 1 255 ? 17.281  -1.149  12.366  1.00 16.06 ?  4730 THR A CB  1 
ATOM   1716 O  OG1 . THR A 1 255 ? 17.589  0.225   12.092  1.00 19.92 ?  4730 THR A OG1 1 
ATOM   1717 C  CG2 . THR A 1 255 ? 17.842  -1.539  13.726  1.00 17.84 ?  4730 THR A CG2 1 
ATOM   1718 N  N   . VAL A 1 256 ? 18.620  -4.247  11.870  1.00 14.19 ?  4731 VAL A N   1 
ATOM   1719 C  CA  . VAL A 1 256 ? 18.473  -5.674  12.124  1.00 12.92 ?  4731 VAL A CA  1 
ATOM   1720 C  C   . VAL A 1 256 ? 18.794  -5.965  13.584  1.00 12.66 ?  4731 VAL A C   1 
ATOM   1721 O  O   . VAL A 1 256 ? 19.855  -5.567  14.087  1.00 14.94 ?  4731 VAL A O   1 
ATOM   1722 C  CB  . VAL A 1 256 ? 19.351  -6.511  11.178  1.00 13.88 ?  4731 VAL A CB  1 
ATOM   1723 C  CG1 . VAL A 1 256 ? 19.161  -8.009  11.455  1.00 14.60 ?  4731 VAL A CG1 1 
ATOM   1724 C  CG2 . VAL A 1 256 ? 19.061  -6.146  9.707   1.00 14.88 ?  4731 VAL A CG2 1 
ATOM   1725 N  N   . GLU A 1 257 ? 17.900  -6.689  14.246  1.00 13.85 ?  4732 GLU A N   1 
ATOM   1726 C  CA  . GLU A 1 257 ? 18.110  -7.212  15.585  1.00 12.93 ?  4732 GLU A CA  1 
ATOM   1727 C  C   . GLU A 1 257 ? 18.299  -8.723  15.471  1.00 13.51 ?  4732 GLU A C   1 
ATOM   1728 O  O   . GLU A 1 257 ? 17.378  -9.431  15.060  1.00 14.94 ?  4732 GLU A O   1 
ATOM   1729 C  CB  . GLU A 1 257 ? 16.898  -6.874  16.455  1.00 14.02 ?  4732 GLU A CB  1 
ATOM   1730 C  CG  . GLU A 1 257 ? 16.800  -7.647  17.764  1.00 15.88 ?  4732 GLU A CG  1 
ATOM   1731 C  CD  . GLU A 1 257 ? 17.791  -7.203  18.848  1.00 20.96 ?  4732 GLU A CD  1 
ATOM   1732 O  OE1 . GLU A 1 257 ? 18.873  -6.666  18.511  1.00 20.20 ?  4732 GLU A OE1 1 
ATOM   1733 O  OE2 . GLU A 1 257 ? 17.472  -7.409  20.045  1.00 23.30 -1 4732 GLU A OE2 1 
ATOM   1734 N  N   . ALA A 1 258 ? 19.490  -9.211  15.804  1.00 12.29 ?  4733 ALA A N   1 
ATOM   1735 C  CA  . ALA A 1 258 ? 19.774  -10.640 15.763  1.00 11.78 ?  4733 ALA A CA  1 
ATOM   1736 C  C   . ALA A 1 258 ? 19.571  -11.230 17.149  1.00 15.30 ?  4733 ALA A C   1 
ATOM   1737 O  O   . ALA A 1 258 ? 20.042  -10.665 18.147  1.00 18.22 ?  4733 ALA A O   1 
ATOM   1738 C  CB  . ALA A 1 258 ? 21.218  -10.891 15.326  1.00 13.04 ?  4733 ALA A CB  1 
ATOM   1739 N  N   . ILE A 1 259 ? 18.875  -12.358 17.216  1.00 12.27 ?  4734 ILE A N   1 
ATOM   1740 C  CA  . ILE A 1 259 ? 18.572  -13.043 18.466  1.00 11.23 ?  4734 ILE A CA  1 
ATOM   1741 C  C   . ILE A 1 259 ? 19.092  -14.462 18.325  1.00 13.08 ?  4734 ILE A C   1 
ATOM   1742 O  O   . ILE A 1 259 ? 18.686  -15.193 17.410  1.00 13.57 ?  4734 ILE A O   1 
ATOM   1743 C  CB  . ILE A 1 259 ? 17.061  -13.047 18.739  1.00 12.24 ?  4734 ILE A CB  1 
ATOM   1744 C  CG1 . ILE A 1 259 ? 16.563  -11.600 18.847  1.00 14.92 ?  4734 ILE A CG1 1 
ATOM   1745 C  CG2 . ILE A 1 259 ? 16.773  -13.817 20.027  1.00 15.87 ?  4734 ILE A CG2 1 
ATOM   1746 C  CD1 . ILE A 1 259 ? 15.063  -11.503 19.069  1.00 17.45 ?  4734 ILE A CD1 1 
ATOM   1747 N  N   . GLY A 1 260 ? 20.051  -14.826 19.178  1.00 12.78 ?  4735 GLY A N   1 
ATOM   1748 C  CA  . GLY A 1 260 ? 20.636  -16.141 19.165  1.00 13.69 ?  4735 GLY A CA  1 
ATOM   1749 C  C   . GLY A 1 260 ? 19.969  -17.038 20.185  1.00 14.68 ?  4735 GLY A C   1 
ATOM   1750 O  O   . GLY A 1 260 ? 20.035  -16.780 21.396  1.00 15.65 ?  4735 GLY A O   1 
ATOM   1751 N  N   . LEU A 1 261 ? 19.354  -18.107 19.698  1.00 11.95 ?  4736 LEU A N   1 
ATOM   1752 C  CA  . LEU A 1 261 ? 18.687  -19.084 20.553  1.00 13.31 ?  4736 LEU A CA  1 
ATOM   1753 C  C   . LEU A 1 261 ? 19.632  -20.219 20.912  1.00 15.88 ?  4736 LEU A C   1 
ATOM   1754 O  O   . LEU A 1 261 ? 20.352  -20.744 20.059  1.00 14.68 ?  4736 LEU A O   1 
ATOM   1755 C  CB  . LEU A 1 261 ? 17.474  -19.691 19.843  1.00 15.07 ?  4736 LEU A CB  1 
ATOM   1756 C  CG  . LEU A 1 261 ? 16.404  -18.716 19.383  1.00 16.10 ?  4736 LEU A CG  1 
ATOM   1757 C  CD1 . LEU A 1 261 ? 15.269  -19.468 18.705  1.00 19.09 ?  4736 LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A 1 261 ? 15.897  -17.886 20.549  1.00 18.90 ?  4736 LEU A CD2 1 
ATOM   1759 N  N   . GLY A 1 262 ? 19.609  -20.612 22.179  1.00 14.69 ?  4737 GLY A N   1 
ATOM   1760 C  CA  . GLY A 1 262 ? 20.308  -21.815 22.590  1.00 15.48 ?  4737 GLY A CA  1 
ATOM   1761 C  C   . GLY A 1 262 ? 21.813  -21.646 22.754  1.00 14.00 ?  4737 GLY A C   1 
ATOM   1762 O  O   . GLY A 1 262 ? 22.368  -20.546 22.734  1.00 15.31 ?  4737 GLY A O   1 
ATOM   1763 N  N   . ALA A 1 263 ? 22.477  -22.788 22.907  1.00 13.93 ?  4738 ALA A N   1 
ATOM   1764 C  CA  . ALA A 1 263 ? 23.857  -22.816 23.378  1.00 15.51 ?  4738 ALA A CA  1 
ATOM   1765 C  C   . ALA A 1 263 ? 24.887  -22.824 22.261  1.00 18.35 ?  4738 ALA A C   1 
ATOM   1766 O  O   . ALA A 1 263 ? 26.091  -22.757 22.546  1.00 21.07 ?  4738 ALA A O   1 
ATOM   1767 C  CB  . ALA A 1 263 ? 24.083  -24.054 24.255  1.00 18.67 ?  4738 ALA A CB  1 
ATOM   1768 N  N   . ASN A 1 264 ? 24.468  -22.899 21.007  1.00 15.24 ?  4739 ASN A N   1 
ATOM   1769 C  CA  . ASN A 1 264 ? 25.411  -23.149 19.923  1.00 16.33 ?  4739 ASN A CA  1 
ATOM   1770 C  C   . ASN A 1 264 ? 25.558  -21.950 18.994  1.00 16.18 ?  4739 ASN A C   1 
ATOM   1771 O  O   . ASN A 1 264 ? 25.951  -22.103 17.829  1.00 19.04 ?  4739 ASN A O   1 
ATOM   1772 C  CB  . ASN A 1 264 ? 25.005  -24.391 19.143  1.00 17.80 ?  4739 ASN A CB  1 
ATOM   1773 C  CG  . ASN A 1 264 ? 24.971  -25.611 20.022  1.00 22.14 ?  4739 ASN A CG  1 
ATOM   1774 O  OD1 . ASN A 1 264 ? 25.953  -25.925 20.696  1.00 26.81 ?  4739 ASN A OD1 1 
ATOM   1775 N  ND2 . ASN A 1 264 ? 23.829  -26.281 20.067  1.00 26.53 ?  4739 ASN A ND2 1 
ATOM   1776 N  N   . ILE A 1 265 ? 25.268  -20.749 19.489  1.00 14.25 ?  4740 ILE A N   1 
ATOM   1777 C  CA  . ILE A 1 265 ? 25.446  -19.541 18.703  1.00 17.36 ?  4740 ILE A CA  1 
ATOM   1778 C  C   . ILE A 1 265 ? 25.962  -18.468 19.657  1.00 18.82 ?  4740 ILE A C   1 
ATOM   1779 O  O   . ILE A 1 265 ? 25.324  -18.170 20.673  1.00 20.22 ?  4740 ILE A O   1 
ATOM   1780 C  CB  . ILE A 1 265 ? 24.173  -19.098 17.956  1.00 19.99 ?  4740 ILE A CB  1 
ATOM   1781 C  CG1 . ILE A 1 265 ? 24.459  -17.849 17.139  1.00 22.96 ?  4740 ILE A CG1 1 
ATOM   1782 C  CG2 . ILE A 1 265 ? 22.961  -19.007 18.841  1.00 22.18 ?  4740 ILE A CG2 1 
ATOM   1783 C  CD1 . ILE A 1 265 ? 24.694  -18.188 15.685  1.00 23.88 ?  4740 ILE A CD1 1 
ATOM   1784 N  N   . SER A 1 266 ? 27.154  -17.956 19.378  1.00 15.94 ?  4741 SER A N   1 
ATOM   1785 C  CA  . SER A 1 266 ? 27.861  -17.040 20.262  1.00 15.62 ?  4741 SER A CA  1 
ATOM   1786 C  C   . SER A 1 266 ? 27.595  -15.604 19.828  1.00 14.70 ?  4741 SER A C   1 
ATOM   1787 O  O   . SER A 1 266 ? 27.124  -15.336 18.716  1.00 15.49 ?  4741 SER A O   1 
ATOM   1788 C  CB  . SER A 1 266 ? 29.364  -17.329 20.205  1.00 17.88 ?  4741 SER A CB  1 
ATOM   1789 O  OG  . SER A 1 266 ? 29.913  -16.962 18.952  1.00 19.55 ?  4741 SER A OG  1 
ATOM   1790 N  N   . TYR A 1 267 ? 27.912  -14.660 20.723  1.00 14.73 ?  4742 TYR A N   1 
ATOM   1791 C  CA  . TYR A 1 267 ? 27.868  -13.248 20.355  1.00 15.31 ?  4742 TYR A CA  1 
ATOM   1792 C  C   . TYR A 1 267 ? 28.642  -13.007 19.066  1.00 13.86 ?  4742 TYR A C   1 
ATOM   1793 O  O   . TYR A 1 267 ? 28.172  -12.315 18.153  1.00 15.16 ?  4742 TYR A O   1 
ATOM   1794 C  CB  . TYR A 1 267 ? 28.450  -12.376 21.480  1.00 16.40 ?  4742 TYR A CB  1 
ATOM   1795 C  CG  . TYR A 1 267 ? 28.486  -10.903 21.125  1.00 12.82 ?  4742 TYR A CG  1 
ATOM   1796 C  CD1 . TYR A 1 267 ? 29.540  -10.360 20.390  1.00 14.23 ?  4742 TYR A CD1 1 
ATOM   1797 C  CD2 . TYR A 1 267 ? 27.439  -10.066 21.496  1.00 15.57 ?  4742 TYR A CD2 1 
ATOM   1798 C  CE1 . TYR A 1 267 ? 29.543  -9.016  20.030  1.00 15.12 ?  4742 TYR A CE1 1 
ATOM   1799 C  CE2 . TYR A 1 267 ? 27.446  -8.729  21.174  1.00 15.49 ?  4742 TYR A CE2 1 
ATOM   1800 C  CZ  . TYR A 1 267 ? 28.503  -8.206  20.434  1.00 16.65 ?  4742 TYR A CZ  1 
ATOM   1801 O  OH  . TYR A 1 267 ? 28.524  -6.869  20.089  1.00 20.71 ?  4742 TYR A OH  1 
ATOM   1802 N  N   . ASN A 1 268 ? 29.848  -13.564 18.975  1.00 14.02 ?  4743 ASN A N   1 
ATOM   1803 C  CA  . ASN A 1 268 ? 30.664  -13.311 17.797  1.00 12.86 ?  4743 ASN A CA  1 
ATOM   1804 C  C   . ASN A 1 268 ? 30.059  -13.910 16.536  1.00 16.02 ?  4743 ASN A C   1 
ATOM   1805 O  O   . ASN A 1 268 ? 30.322  -13.405 15.442  1.00 16.65 ?  4743 ASN A O   1 
ATOM   1806 C  CB  . ASN A 1 268 ? 32.089  -13.829 18.008  1.00 14.82 ?  4743 ASN A CB  1 
ATOM   1807 C  CG  . ASN A 1 268 ? 32.909  -12.929 18.895  1.00 17.74 ?  4743 ASN A CG  1 
ATOM   1808 O  OD1 . ASN A 1 268 ? 32.585  -11.745 19.074  1.00 18.87 ?  4743 ASN A OD1 1 
ATOM   1809 N  ND2 . ASN A 1 268 ? 33.996  -13.475 19.452  1.00 18.36 ?  4743 ASN A ND2 1 
ATOM   1810 N  N   . ASP A 1 269 ? 29.254  -14.975 16.665  1.00 15.60 ?  4744 ASP A N   1 
ATOM   1811 C  CA  . ASP A 1 269 ? 28.576  -15.539 15.497  1.00 15.06 ?  4744 ASP A CA  1 
ATOM   1812 C  C   . ASP A 1 269 ? 27.466  -14.638 14.977  1.00 16.11 ?  4744 ASP A C   1 
ATOM   1813 O  O   . ASP A 1 269 ? 27.059  -14.782 13.818  1.00 16.30 ?  4744 ASP A O   1 
ATOM   1814 C  CB  . ASP A 1 269 ? 27.955  -16.893 15.820  1.00 16.24 ?  4744 ASP A CB  1 
ATOM   1815 C  CG  . ASP A 1 269 ? 28.974  -17.949 16.126  1.00 19.14 ?  4744 ASP A CG  1 
ATOM   1816 O  OD1 . ASP A 1 269 ? 30.012  -17.991 15.442  1.00 19.78 ?  4744 ASP A OD1 1 
ATOM   1817 O  OD2 . ASP A 1 269 ? 28.715  -18.746 17.055  1.00 21.50 -1 4744 ASP A OD2 1 
ATOM   1818 N  N   . LEU A 1 270 ? 26.977  -13.698 15.781  1.00 15.45 ?  4745 LEU A N   1 
ATOM   1819 C  CA  . LEU A 1 270 ? 25.917  -12.805 15.331  1.00 13.95 ?  4745 LEU A CA  1 
ATOM   1820 C  C   . LEU A 1 270 ? 26.377  -11.368 15.178  1.00 13.74 ?  4745 LEU A C   1 
ATOM   1821 O  O   . LEU A 1 270 ? 25.607  -10.530 14.704  1.00 14.49 ?  4745 LEU A O   1 
ATOM   1822 C  CB  . LEU A 1 270 ? 24.728  -12.862 16.286  1.00 14.97 ?  4745 LEU A CB  1 
ATOM   1823 C  CG  . LEU A 1 270 ? 23.967  -14.183 16.207  1.00 16.75 ?  4745 LEU A CG  1 
ATOM   1824 C  CD1 . LEU A 1 270 ? 22.781  -14.134 17.156  1.00 17.26 ?  4745 LEU A CD1 1 
ATOM   1825 C  CD2 . LEU A 1 270 ? 23.515  -14.482 14.769  1.00 16.80 ?  4745 LEU A CD2 1 
ATOM   1826 N  N   . LYS A 1 271 ? 27.635  -11.078 15.525  1.00 13.94 ?  4746 LYS A N   1 
ATOM   1827 C  CA  . LYS A 1 271 ? 28.152  -9.715  15.504  1.00 15.70 ?  4746 LYS A CA  1 
ATOM   1828 C  C   . LYS A 1 271 ? 28.007  -9.084  14.125  1.00 13.65 ?  4746 LYS A C   1 
ATOM   1829 O  O   . LYS A 1 271 ? 27.743  -7.879  14.003  1.00 16.89 ?  4746 LYS A O   1 
ATOM   1830 C  CB  . LYS A 1 271 ? 29.627  -9.770  15.912  1.00 18.59 ?  4746 LYS A CB  1 
ATOM   1831 C  CG  . LYS A 1 271 ? 30.298  -8.461  16.207  1.00 24.73 ?  4746 LYS A CG  1 
ATOM   1832 C  CD  . LYS A 1 271 ? 31.774  -8.737  16.529  1.00 21.92 ?  4746 LYS A CD  1 
ATOM   1833 C  CE  . LYS A 1 271 ? 32.490  -7.475  16.938  1.00 27.89 ?  4746 LYS A CE  1 
ATOM   1834 N  NZ  . LYS A 1 271 ? 32.520  -6.506  15.808  1.00 27.81 ?  4746 LYS A NZ  1 
ATOM   1835 N  N   . SER A 1 272 ? 28.180  -9.874  13.068  1.00 14.42 ?  4747 SER A N   1 
ATOM   1836 C  CA  . SER A 1 272 ? 28.116  -9.307  11.732  1.00 15.78 ?  4747 SER A CA  1 
ATOM   1837 C  C   . SER A 1 272 ? 26.698  -9.087  11.243  1.00 17.01 ?  4747 SER A C   1 
ATOM   1838 O  O   . SER A 1 272 ? 26.522  -8.492  10.175  1.00 18.52 ?  4747 SER A O   1 
ATOM   1839 C  CB  . SER A 1 272 ? 28.806  -10.241 10.744  1.00 16.02 ?  4747 SER A CB  1 
ATOM   1840 O  OG  . SER A 1 272 ? 30.209  -10.270 10.966  1.00 20.15 ?  4747 SER A OG  1 
ATOM   1841 N  N   . TYR A 1 273 ? 25.696  -9.551  11.985  1.00 15.18 ?  4748 TYR A N   1 
ATOM   1842 C  CA  . TYR A 1 273 ? 24.316  -9.562  11.515  1.00 14.67 ?  4748 TYR A CA  1 
ATOM   1843 C  C   . TYR A 1 273 ? 23.408  -8.762  12.432  1.00 15.18 ?  4748 TYR A C   1 
ATOM   1844 O  O   . TYR A 1 273 ? 22.196  -9.023  12.497  1.00 15.34 ?  4748 TYR A O   1 
ATOM   1845 C  CB  . TYR A 1 273 ? 23.813  -10.996 11.387  1.00 13.82 ?  4748 TYR A CB  1 
ATOM   1846 C  CG  . TYR A 1 273 ? 24.797  -11.918 10.705  1.00 13.34 ?  4748 TYR A CG  1 
ATOM   1847 C  CD1 . TYR A 1 273 ? 25.038  -11.822 9.330   1.00 15.37 ?  4748 TYR A CD1 1 
ATOM   1848 C  CD2 . TYR A 1 273 ? 25.484  -12.888 11.424  1.00 15.58 ?  4748 TYR A CD2 1 
ATOM   1849 C  CE1 . TYR A 1 273 ? 25.935  -12.671 8.706   1.00 15.79 ?  4748 TYR A CE1 1 
ATOM   1850 C  CE2 . TYR A 1 273 ? 26.392  -13.744 10.797  1.00 15.12 ?  4748 TYR A CE2 1 
ATOM   1851 C  CZ  . TYR A 1 273 ? 26.608  -13.626 9.444   1.00 16.48 ?  4748 TYR A CZ  1 
ATOM   1852 O  OH  . TYR A 1 273 ? 27.502  -14.470 8.840   1.00 19.37 ?  4748 TYR A OH  1 
ATOM   1853 N  N   . ASP A 1 274 ? 23.960  -7.801  13.158  1.00 15.28 ?  4749 ASP A N   1 
ATOM   1854 C  CA  . ASP A 1 274 ? 23.175  -7.017  14.094  1.00 16.26 ?  4749 ASP A CA  1 
ATOM   1855 C  C   . ASP A 1 274 ? 23.604  -5.561  13.988  1.00 17.38 ?  4749 ASP A C   1 
ATOM   1856 O  O   . ASP A 1 274 ? 24.799  -5.259  13.990  1.00 19.14 ?  4749 ASP A O   1 
ATOM   1857 C  CB  . ASP A 1 274 ? 23.363  -7.540  15.517  1.00 15.89 ?  4749 ASP A CB  1 
ATOM   1858 C  CG  . ASP A 1 274 ? 22.513  -6.805  16.516  1.00 18.38 ?  4749 ASP A CG  1 
ATOM   1859 O  OD1 . ASP A 1 274 ? 22.977  -5.772  17.021  1.00 17.20 ?  4749 ASP A OD1 1 
ATOM   1860 O  OD2 . ASP A 1 274 ? 21.378  -7.231  16.787  1.00 15.13 -1 4749 ASP A OD2 1 
ATOM   1861 N  N   . SER A 1 275 ? 22.622  -4.666  13.937  1.00 18.76 ?  4750 SER A N   1 
ATOM   1862 C  CA  . SER A 1 275 ? 22.892  -3.268  13.615  1.00 17.12 ?  4750 SER A CA  1 
ATOM   1863 C  C   . SER A 1 275 ? 23.621  -2.524  14.733  1.00 20.37 ?  4750 SER A C   1 
ATOM   1864 O  O   . SER A 1 275 ? 24.478  -1.685  14.446  1.00 25.80 ?  4750 SER A O   1 
ATOM   1865 C  CB  . SER A 1 275 ? 21.596  -2.558  13.220  1.00 17.05 ?  4750 SER A CB  1 
ATOM   1866 O  OG  . SER A 1 275 ? 21.192  -3.002  11.949  1.00 19.20 ?  4750 SER A OG  1 
ATOM   1867 N  N   . ASP A 1 276 ? 23.293  -2.774  15.997  1.00 17.83 ?  4751 ASP A N   1 
ATOM   1868 C  CA  . ASP A 1 276 ? 23.878  -1.955  17.060  1.00 20.83 ?  4751 ASP A CA  1 
ATOM   1869 C  C   . ASP A 1 276 ? 24.883  -2.683  17.943  1.00 20.77 ?  4751 ASP A C   1 
ATOM   1870 O  O   . ASP A 1 276 ? 25.435  -2.066  18.863  1.00 23.59 ?  4751 ASP A O   1 
ATOM   1871 C  CB  . ASP A 1 276 ? 22.796  -1.262  17.896  1.00 21.50 ?  4751 ASP A CB  1 
ATOM   1872 C  CG  . ASP A 1 276 ? 21.979  -2.232  18.724  1.00 21.23 ?  4751 ASP A CG  1 
ATOM   1873 O  OD1 . ASP A 1 276 ? 22.245  -3.455  18.678  1.00 19.44 ?  4751 ASP A OD1 1 
ATOM   1874 O  OD2 . ASP A 1 276 ? 21.061  -1.779  19.442  1.00 24.83 -1 4751 ASP A OD2 1 
ATOM   1875 N  N   . GLY A 1 277 ? 25.142  -3.964  17.700  1.00 18.06 ?  4752 GLY A N   1 
ATOM   1876 C  CA  . GLY A 1 277 ? 26.063  -4.697  18.549  1.00 19.99 ?  4752 GLY A CA  1 
ATOM   1877 C  C   . GLY A 1 277 ? 25.529  -5.081  19.911  1.00 19.58 ?  4752 GLY A C   1 
ATOM   1878 O  O   . GLY A 1 277 ? 26.269  -5.676  20.702  1.00 21.76 ?  4752 GLY A O   1 
ATOM   1879 N  N   . VAL A 1 278 ? 24.289  -4.732  20.235  1.00 16.32 ?  4753 VAL A N   1 
ATOM   1880 C  CA  . VAL A 1 278 ? 23.620  -5.243  21.423  1.00 18.42 ?  4753 VAL A CA  1 
ATOM   1881 C  C   . VAL A 1 278 ? 22.862  -6.488  20.977  1.00 18.42 ?  4753 VAL A C   1 
ATOM   1882 O  O   . VAL A 1 278 ? 21.915  -6.393  20.192  1.00 17.62 ?  4753 VAL A O   1 
ATOM   1883 C  CB  . VAL A 1 278 ? 22.677  -4.198  22.028  1.00 22.28 ?  4753 VAL A CB  1 
ATOM   1884 C  CG1 . VAL A 1 278 ? 22.112  -4.711  23.330  1.00 22.48 ?  4753 VAL A CG1 1 
ATOM   1885 C  CG2 . VAL A 1 278 ? 23.414  -2.883  22.244  1.00 23.38 ?  4753 VAL A CG2 1 
ATOM   1886 N  N   . ILE A 1 279 ? 23.276  -7.654  21.463  1.00 17.48 ?  4754 ILE A N   1 
ATOM   1887 C  CA  . ILE A 1 279 ? 22.820  -8.929  20.913  1.00 16.93 ?  4754 ILE A CA  1 
ATOM   1888 C  C   . ILE A 1 279 ? 22.530  -9.871  22.067  1.00 17.59 ?  4754 ILE A C   1 
ATOM   1889 O  O   . ILE A 1 279 ? 23.421  -10.139 22.882  1.00 19.82 ?  4754 ILE A O   1 
ATOM   1890 C  CB  . ILE A 1 279 ? 23.888  -9.558  20.009  1.00 16.57 ?  4754 ILE A CB  1 
ATOM   1891 C  CG1 . ILE A 1 279 ? 24.312  -8.584  18.913  1.00 16.12 ?  4754 ILE A CG1 1 
ATOM   1892 C  CG2 . ILE A 1 279 ? 23.371  -10.872 19.419  1.00 17.74 ?  4754 ILE A CG2 1 
ATOM   1893 C  CD1 . ILE A 1 279 ? 25.446  -9.128  18.053  1.00 17.17 ?  4754 ILE A CD1 1 
ATOM   1894 N  N   . MET A 1 280 ? 21.301  -10.389 22.131  1.00 15.90 ?  4755 MET A N   1 
ATOM   1895 C  CA  . MET A 1 280 ? 20.956  -11.438 23.077  1.00 17.02 ?  4755 MET A CA  1 
ATOM   1896 C  C   . MET A 1 280 ? 21.306  -12.797 22.481  1.00 16.59 ?  4755 MET A C   1 
ATOM   1897 O  O   . MET A 1 280 ? 20.859  -13.125 21.374  1.00 17.76 ?  4755 MET A O   1 
ATOM   1898 C  CB  . MET A 1 280 ? 19.466  -11.382 23.380  1.00 19.54 ?  4755 MET A CB  1 
ATOM   1899 C  CG  . MET A 1 280 ? 19.074  -10.189 24.217  1.00 20.07 ?  4755 MET A CG  1 
ATOM   1900 S  SD  . MET A 1 280 ? 17.284  -10.092 24.392  1.00 23.04 ?  4755 MET A SD  1 
ATOM   1901 C  CE  . MET A 1 280 ? 16.815  -9.269  22.892  1.00 21.83 ?  4755 MET A CE  1 
ATOM   1902 N  N   . THR A 1 281 ? 22.111  -13.573 23.196  1.00 16.07 ?  4756 THR A N   1 
ATOM   1903 C  CA  . THR A 1 281 ? 22.417  -14.945 22.821  1.00 17.12 ?  4756 THR A CA  1 
ATOM   1904 C  C   . THR A 1 281 ? 22.145  -15.853 24.009  1.00 16.70 ?  4756 THR A C   1 
ATOM   1905 O  O   . THR A 1 281 ? 22.026  -15.402 25.153  1.00 19.36 ?  4756 THR A O   1 
ATOM   1906 C  CB  . THR A 1 281 ? 23.880  -15.139 22.376  1.00 17.35 ?  4756 THR A CB  1 
ATOM   1907 O  OG1 . THR A 1 281 ? 24.759  -14.805 23.457  1.00 22.74 ?  4756 THR A OG1 1 
ATOM   1908 C  CG2 . THR A 1 281 ? 24.218  -14.279 21.189  1.00 18.70 ?  4756 THR A CG2 1 
ATOM   1909 N  N   . GLY A 1 282 ? 22.078  -17.148 23.731  1.00 16.44 ?  4757 GLY A N   1 
ATOM   1910 C  CA  . GLY A 1 282 ? 21.697  -18.099 24.749  1.00 17.00 ?  4757 GLY A CA  1 
ATOM   1911 C  C   . GLY A 1 282 ? 20.240  -18.010 25.129  1.00 16.15 ?  4757 GLY A C   1 
ATOM   1912 O  O   . GLY A 1 282 ? 19.848  -18.528 26.190  1.00 17.37 ?  4757 GLY A O   1 
ATOM   1913 N  N   . VAL A 1 283 ? 19.427  -17.366 24.289  1.00 15.75 ?  4758 VAL A N   1 
ATOM   1914 C  CA  . VAL A 1 283 ? 18.022  -17.138 24.583  1.00 14.86 ?  4758 VAL A CA  1 
ATOM   1915 C  C   . VAL A 1 283 ? 17.270  -18.452 24.503  1.00 14.97 ?  4758 VAL A C   1 
ATOM   1916 O  O   . VAL A 1 283 ? 17.406  -19.228 23.552  1.00 15.22 ?  4758 VAL A O   1 
ATOM   1917 C  CB  . VAL A 1 283 ? 17.437  -16.083 23.632  1.00 16.36 ?  4758 VAL A CB  1 
ATOM   1918 C  CG1 . VAL A 1 283 ? 15.931  -15.903 23.849  1.00 18.05 ?  4758 VAL A CG1 1 
ATOM   1919 C  CG2 . VAL A 1 283 ? 18.165  -14.765 23.795  1.00 18.45 ?  4758 VAL A CG2 1 
ATOM   1920 N  N   . ASN A 1 284 ? 16.490  -18.711 25.533  1.00 16.43 ?  4759 ASN A N   1 
ATOM   1921 C  CA  . ASN A 1 284 ? 15.605  -19.845 25.600  1.00 17.25 ?  4759 ASN A CA  1 
ATOM   1922 C  C   . ASN A 1 284 ? 14.420  -19.609 24.661  1.00 17.05 ?  4759 ASN A C   1 
ATOM   1923 O  O   . ASN A 1 284 ? 13.966  -18.474 24.503  1.00 16.54 ?  4759 ASN A O   1 
ATOM   1924 C  CB  . ASN A 1 284 ? 15.149  -19.844 27.056  1.00 22.48 ?  4759 ASN A CB  1 
ATOM   1925 C  CG  . ASN A 1 284 ? 14.334  -21.005 27.415  1.00 21.20 ?  4759 ASN A CG  1 
ATOM   1926 O  OD1 . ASN A 1 284 ? 13.158  -21.067 27.071  1.00 23.27 ?  4759 ASN A OD1 1 
ATOM   1927 N  ND2 . ASN A 1 284 ? 14.930  -21.948 28.146  1.00 23.62 ?  4759 ASN A ND2 1 
ATOM   1928 N  N   . ALA A 1 285 ? 13.931  -20.672 24.015  1.00 15.35 ?  4760 ALA A N   1 
ATOM   1929 C  CA  . ALA A 1 285 ? 12.815  -20.480 23.086  1.00 16.15 ?  4760 ALA A CA  1 
ATOM   1930 C  C   . ALA A 1 285 ? 11.600  -19.882 23.782  1.00 17.11 ?  4760 ALA A C   1 
ATOM   1931 O  O   . ALA A 1 285 ? 10.869  -19.092 23.174  1.00 16.61 ?  4760 ALA A O   1 
ATOM   1932 C  CB  . ALA A 1 285 ? 12.450  -21.784 22.395  1.00 17.16 ?  4760 ALA A CB  1 
ATOM   1933 N  N   . SER A 1 286 ? 11.406  -20.208 25.063  1.00 16.63 ?  4761 SER A N   1 
ATOM   1934 C  CA  . SER A 1 286 ? 10.260  -19.713 25.817  1.00 16.66 ?  4761 SER A CA  1 
ATOM   1935 C  C   . SER A 1 286 ? 10.365  -18.237 26.157  1.00 16.61 ?  4761 SER A C   1 
ATOM   1936 O  O   . SER A 1 286 ? 9.376   -17.668 26.646  1.00 18.05 ?  4761 SER A O   1 
ATOM   1937 C  CB  . SER A 1 286 ? 10.092  -20.518 27.108  1.00 18.26 ?  4761 SER A CB  1 
ATOM   1938 O  OG  . SER A 1 286 ? 9.815   -21.873 26.812  1.00 22.27 ?  4761 SER A OG  1 
ATOM   1939 N  N   . ASP A 1 287 ? 11.518  -17.603 25.923  1.00 15.15 ?  4762 ASP A N   1 
ATOM   1940 C  CA  . ASP A 1 287 ? 11.687  -16.175 26.155  1.00 15.73 ?  4762 ASP A CA  1 
ATOM   1941 C  C   . ASP A 1 287 ? 11.647  -15.345 24.889  1.00 11.38 ?  4762 ASP A C   1 
ATOM   1942 O  O   . ASP A 1 287 ? 11.829  -14.129 24.962  1.00 15.13 ?  4762 ASP A O   1 
ATOM   1943 C  CB  . ASP A 1 287 ? 12.997  -15.885 26.882  1.00 16.05 ?  4762 ASP A CB  1 
ATOM   1944 C  CG  . ASP A 1 287 ? 12.922  -16.229 28.336  1.00 22.53 ?  4762 ASP A CG  1 
ATOM   1945 O  OD1 . ASP A 1 287 ? 11.938  -15.813 28.988  1.00 22.37 ?  4762 ASP A OD1 1 
ATOM   1946 O  OD2 . ASP A 1 287 ? 13.832  -16.928 28.808  1.00 21.67 -1 4762 ASP A OD2 1 
ATOM   1947 N  N   . LEU A 1 288 ? 11.341  -15.964 23.749  1.00 14.12 ?  4763 LEU A N   1 
ATOM   1948 C  CA  . LEU A 1 288 ? 11.462  -15.273 22.470  1.00 13.09 ?  4763 LEU A CA  1 
ATOM   1949 C  C   . LEU A 1 288 ? 10.505  -14.089 22.360  1.00 11.74 ?  4763 LEU A C   1 
ATOM   1950 O  O   . LEU A 1 288 ? 10.896  -13.011 21.902  1.00 13.38 ?  4763 LEU A O   1 
ATOM   1951 C  CB  . LEU A 1 288 ? 11.259  -16.257 21.321  1.00 14.66 ?  4763 LEU A CB  1 
ATOM   1952 C  CG  . LEU A 1 288 ? 11.356  -15.670 19.914  1.00 13.28 ?  4763 LEU A CG  1 
ATOM   1953 C  CD1 . LEU A 1 288 ? 12.724  -15.060 19.708  1.00 15.84 ?  4763 LEU A CD1 1 
ATOM   1954 C  CD2 . LEU A 1 288 ? 11.082  -16.759 18.886  1.00 14.85 ?  4763 LEU A CD2 1 
ATOM   1955 N  N   . ALA A 1 289 ? 9.228   -14.291 22.719  1.00 13.33 ?  4764 ALA A N   1 
ATOM   1956 C  CA  . ALA A 1 289 ? 8.272   -13.202 22.567  1.00 13.96 ?  4764 ALA A CA  1 
ATOM   1957 C  C   . ALA A 1 289 ? 8.655   -12.007 23.431  1.00 12.91 ?  4764 ALA A C   1 
ATOM   1958 O  O   . ALA A 1 289 ? 8.651   -10.866 22.956  1.00 15.05 ?  4764 ALA A O   1 
ATOM   1959 C  CB  . ALA A 1 289 ? 6.856   -13.679 22.911  1.00 14.92 ?  4764 ALA A CB  1 
ATOM   1960 N  N   . ASN A 1 290 ? 9.047   -12.263 24.683  1.00 17.86 ?  4765 ASN A N   1 
ATOM   1961 C  CA  . ASN A 1 290 ? 9.492   -11.177 25.559  1.00 19.21 ?  4765 ASN A CA  1 
ATOM   1962 C  C   . ASN A 1 290 ? 10.739  -10.503 25.016  1.00 17.39 ?  4765 ASN A C   1 
ATOM   1963 O  O   . ASN A 1 290 ? 10.859  -9.270  25.062  1.00 17.71 ?  4765 ASN A O   1 
ATOM   1964 C  CB  . ASN A 1 290 ? 9.818   -11.709 26.951  1.00 19.85 ?  4765 ASN A CB  1 
ATOM   1965 C  CG  . ASN A 1 290 ? 8.591   -12.081 27.746  1.00 28.55 ?  4765 ASN A CG  1 
ATOM   1966 O  OD1 . ASN A 1 290 ? 7.477   -11.650 27.448  1.00 28.89 ?  4765 ASN A OD1 1 
ATOM   1967 N  ND2 . ASN A 1 290 ? 8.794   -12.887 28.781  1.00 33.13 ?  4765 ASN A ND2 1 
ATOM   1968 N  N   . ALA A 1 291 ? 11.678  -11.298 24.486  1.00 15.97 ?  4766 ALA A N   1 
ATOM   1969 C  CA  . ALA A 1 291 ? 12.905  -10.735 23.933  1.00 15.20 ?  4766 ALA A CA  1 
ATOM   1970 C  C   . ALA A 1 291 ? 12.599  -9.762  22.802  1.00 17.37 ?  4766 ALA A C   1 
ATOM   1971 O  O   . ALA A 1 291 ? 13.260  -8.728  22.666  1.00 17.33 ?  4766 ALA A O   1 
ATOM   1972 C  CB  . ALA A 1 291 ? 13.825  -11.854 23.445  1.00 16.84 ?  4766 ALA A CB  1 
ATOM   1973 N  N   . ILE A 1 292 ? 11.586  -10.074 21.988  1.00 15.74 ?  4767 ILE A N   1 
ATOM   1974 C  CA  . ILE A 1 292 ? 11.209  -9.194  20.884  1.00 16.87 ?  4767 ILE A CA  1 
ATOM   1975 C  C   . ILE A 1 292 ? 10.387  -8.007  21.382  1.00 17.58 ?  4767 ILE A C   1 
ATOM   1976 O  O   . ILE A 1 292 ? 10.697  -6.849  21.079  1.00 21.06 ?  4767 ILE A O   1 
ATOM   1977 C  CB  . ILE A 1 292 ? 10.449  -10.007 19.818  1.00 14.26 ?  4767 ILE A CB  1 
ATOM   1978 C  CG1 . ILE A 1 292 ? 11.382  -11.014 19.139  1.00 14.49 ?  4767 ILE A CG1 1 
ATOM   1979 C  CG2 . ILE A 1 292 ? 9.834   -9.081  18.752  1.00 16.46 ?  4767 ILE A CG2 1 
ATOM   1980 C  CD1 . ILE A 1 292 ? 10.630  -12.020 18.331  1.00 16.15 ?  4767 ILE A CD1 1 
ATOM   1981 N  N   . LEU A 1 293 ? 9.329   -8.276  22.143  1.00 17.73 ?  4768 LEU A N   1 
ATOM   1982 C  CA  . LEU A 1 293 ? 8.358   -7.233  22.486  1.00 18.23 ?  4768 LEU A CA  1 
ATOM   1983 C  C   . LEU A 1 293 ? 8.888   -6.270  23.541  1.00 24.73 ?  4768 LEU A C   1 
ATOM   1984 O  O   . LEU A 1 293 ? 8.540   -5.079  23.527  1.00 25.02 ?  4768 LEU A O   1 
ATOM   1985 C  CB  . LEU A 1 293 ? 7.060   -7.878  22.974  1.00 19.18 ?  4768 LEU A CB  1 
ATOM   1986 C  CG  . LEU A 1 293 ? 6.273   -8.703  21.943  1.00 18.89 ?  4768 LEU A CG  1 
ATOM   1987 C  CD1 . LEU A 1 293 ? 5.190   -9.546  22.600  1.00 21.57 ?  4768 LEU A CD1 1 
ATOM   1988 C  CD2 . LEU A 1 293 ? 5.668   -7.787  20.902  1.00 18.44 ?  4768 LEU A CD2 1 
ATOM   1989 N  N   . GLY A 1 294 ? 9.708   -6.756  24.465  1.00 20.83 ?  4769 GLY A N   1 
ATOM   1990 C  CA  . GLY A 1 294 ? 10.157  -5.948  25.579  1.00 22.98 ?  4769 GLY A CA  1 
ATOM   1991 C  C   . GLY A 1 294 ? 11.499  -5.271  25.406  1.00 25.89 ?  4769 GLY A C   1 
ATOM   1992 O  O   . GLY A 1 294 ? 12.004  -4.689  26.374  1.00 28.67 ?  4769 GLY A O   1 
ATOM   1993 N  N   . THR A 1 295 ? 12.093  -5.296  24.214  1.00 24.55 ?  4770 THR A N   1 
ATOM   1994 C  CA  . THR A 1 295 ? 13.462  -4.826  24.035  1.00 27.31 ?  4770 THR A CA  1 
ATOM   1995 C  C   . THR A 1 295 ? 13.523  -3.539  23.224  1.00 34.52 ?  4770 THR A C   1 
ATOM   1996 O  O   . THR A 1 295 ? 12.908  -3.445  22.154  1.00 33.67 ?  4770 THR A O   1 
ATOM   1997 C  CB  . THR A 1 295 ? 14.330  -5.892  23.372  1.00 26.37 ?  4770 THR A CB  1 
ATOM   1998 O  OG1 . THR A 1 295 ? 14.460  -7.009  24.262  1.00 20.33 ?  4770 THR A OG1 1 
ATOM   1999 C  CG2 . THR A 1 295 ? 15.710  -5.330  23.052  1.00 28.84 ?  4770 THR A CG2 1 
ATOM   2000 N  N   . PRO B 1 22  ? 31.530  45.717  -19.306 1.00 35.18 ?  4497 PRO B N   1 
ATOM   2001 C  CA  . PRO B 1 22  ? 30.789  45.471  -20.550 1.00 32.21 ?  4497 PRO B CA  1 
ATOM   2002 C  C   . PRO B 1 22  ? 31.336  44.262  -21.296 1.00 33.61 ?  4497 PRO B C   1 
ATOM   2003 O  O   . PRO B 1 22  ? 32.551  44.109  -21.418 1.00 37.49 ?  4497 PRO B O   1 
ATOM   2004 C  CB  . PRO B 1 22  ? 31.045  46.740  -21.365 1.00 35.84 ?  4497 PRO B CB  1 
ATOM   2005 C  CG  . PRO B 1 22  ? 31.331  47.786  -20.350 1.00 32.70 ?  4497 PRO B CG  1 
ATOM   2006 C  CD  . PRO B 1 22  ? 32.072  47.085  -19.247 1.00 33.34 ?  4497 PRO B CD  1 
ATOM   2007 N  N   . GLY B 1 23  ? 30.443  43.415  -21.798 1.00 30.79 ?  4498 GLY B N   1 
ATOM   2008 C  CA  . GLY B 1 23  ? 30.875  42.193  -22.436 1.00 30.76 ?  4498 GLY B CA  1 
ATOM   2009 C  C   . GLY B 1 23  ? 31.279  41.098  -21.476 1.00 30.26 ?  4498 GLY B C   1 
ATOM   2010 O  O   . GLY B 1 23  ? 31.937  40.140  -21.895 1.00 31.24 ?  4498 GLY B O   1 
ATOM   2011 N  N   . GLN B 1 24  ? 30.907  41.211  -20.199 1.00 29.12 ?  4499 GLN B N   1 
ATOM   2012 C  CA  . GLN B 1 24  ? 31.245  40.195  -19.204 1.00 27.31 ?  4499 GLN B CA  1 
ATOM   2013 C  C   . GLN B 1 24  ? 30.625  38.855  -19.584 1.00 24.59 ?  4499 GLN B C   1 
ATOM   2014 O  O   . GLN B 1 24  ? 29.410  38.752  -19.778 1.00 24.24 ?  4499 GLN B O   1 
ATOM   2015 C  CB  . GLN B 1 24  ? 30.736  40.631  -17.831 1.00 30.38 ?  4499 GLN B CB  1 
ATOM   2016 C  CG  . GLN B 1 24  ? 30.972  39.603  -16.729 1.00 31.05 ?  4499 GLN B CG  1 
ATOM   2017 C  CD  . GLN B 1 24  ? 32.441  39.326  -16.499 1.00 31.91 ?  4499 GLN B CD  1 
ATOM   2018 O  OE1 . GLN B 1 24  ? 33.198  40.213  -16.106 1.00 36.02 ?  4499 GLN B OE1 1 
ATOM   2019 N  NE2 . GLN B 1 24  ? 32.858  38.089  -16.747 1.00 32.54 ?  4499 GLN B NE2 1 
ATOM   2020 N  N   . ASN B 1 25  ? 31.459  37.829  -19.693 1.00 27.47 ?  4500 ASN B N   1 
ATOM   2021 C  CA  . ASN B 1 25  ? 30.974  36.494  -20.016 1.00 26.92 ?  4500 ASN B CA  1 
ATOM   2022 C  C   . ASN B 1 25  ? 30.544  35.779  -18.739 1.00 26.67 ?  4500 ASN B C   1 
ATOM   2023 O  O   . ASN B 1 25  ? 31.096  36.018  -17.664 1.00 27.52 ?  4500 ASN B O   1 
ATOM   2024 C  CB  . ASN B 1 25  ? 32.063  35.690  -20.724 1.00 28.56 ?  4500 ASN B CB  1 
ATOM   2025 C  CG  . ASN B 1 25  ? 32.382  36.228  -22.111 1.00 25.94 ?  4500 ASN B CG  1 
ATOM   2026 O  OD1 . ASN B 1 25  ? 31.493  36.673  -22.837 1.00 28.91 ?  4500 ASN B OD1 1 
ATOM   2027 N  ND2 . ASN B 1 25  ? 33.655  36.169  -22.490 1.00 30.67 ?  4500 ASN B ND2 1 
ATOM   2028 N  N   . TYR B 1 26  ? 29.534  34.913  -18.865 1.00 24.24 ?  4501 TYR B N   1 
ATOM   2029 C  CA  . TYR B 1 26  ? 29.007  34.151  -17.736 1.00 25.10 ?  4501 TYR B CA  1 
ATOM   2030 C  C   . TYR B 1 26  ? 28.743  32.708  -18.139 1.00 23.60 ?  4501 TYR B C   1 
ATOM   2031 O  O   . TYR B 1 26  ? 28.241  32.439  -19.233 1.00 23.92 ?  4501 TYR B O   1 
ATOM   2032 C  CB  . TYR B 1 26  ? 27.670  34.709  -17.238 1.00 24.11 ?  4501 TYR B CB  1 
ATOM   2033 C  CG  . TYR B 1 26  ? 27.752  36.078  -16.618 1.00 30.98 ?  4501 TYR B CG  1 
ATOM   2034 C  CD1 . TYR B 1 26  ? 27.639  37.222  -17.398 1.00 28.85 ?  4501 TYR B CD1 1 
ATOM   2035 C  CD2 . TYR B 1 26  ? 27.929  36.229  -15.252 1.00 30.73 ?  4501 TYR B CD2 1 
ATOM   2036 C  CE1 . TYR B 1 26  ? 27.704  38.481  -16.832 1.00 31.78 ?  4501 TYR B CE1 1 
ATOM   2037 C  CE2 . TYR B 1 26  ? 27.995  37.486  -14.675 1.00 31.62 ?  4501 TYR B CE2 1 
ATOM   2038 C  CZ  . TYR B 1 26  ? 27.884  38.606  -15.472 1.00 33.82 ?  4501 TYR B CZ  1 
ATOM   2039 O  OH  . TYR B 1 26  ? 27.952  39.859  -14.906 1.00 35.67 ?  4501 TYR B OH  1 
ATOM   2040 N  N   . ASN B 1 27  ? 29.046  31.789  -17.221 1.00 21.93 ?  4502 ASN B N   1 
ATOM   2041 C  CA  . ASN B 1 27  ? 28.629  30.390  -17.308 1.00 25.48 ?  4502 ASN B CA  1 
ATOM   2042 C  C   . ASN B 1 27  ? 27.916  30.082  -16.001 1.00 20.62 ?  4502 ASN B C   1 
ATOM   2043 O  O   . ASN B 1 27  ? 28.560  29.997  -14.950 1.00 22.57 ?  4502 ASN B O   1 
ATOM   2044 C  CB  . ASN B 1 27  ? 29.839  29.474  -17.472 1.00 23.88 ?  4502 ASN B CB  1 
ATOM   2045 C  CG  . ASN B 1 27  ? 30.587  29.719  -18.762 1.00 21.69 ?  4502 ASN B CG  1 
ATOM   2046 O  OD1 . ASN B 1 27  ? 30.010  29.662  -19.853 1.00 25.17 ?  4502 ASN B OD1 1 
ATOM   2047 N  ND2 . ASN B 1 27  ? 31.883  29.974  -18.649 1.00 27.90 ?  4502 ASN B ND2 1 
ATOM   2048 N  N   . ILE B 1 28  ? 26.595  29.940  -16.052 1.00 21.54 ?  4503 ILE B N   1 
ATOM   2049 C  CA  . ILE B 1 28  ? 25.764  29.837  -14.859 1.00 22.66 ?  4503 ILE B CA  1 
ATOM   2050 C  C   . ILE B 1 28  ? 25.008  28.511  -14.883 1.00 22.79 ?  4503 ILE B C   1 
ATOM   2051 O  O   . ILE B 1 28  ? 24.205  28.264  -15.792 1.00 23.13 ?  4503 ILE B O   1 
ATOM   2052 C  CB  . ILE B 1 28  ? 24.783  31.013  -14.748 1.00 23.23 ?  4503 ILE B CB  1 
ATOM   2053 C  CG1 . ILE B 1 28  ? 25.524  32.347  -14.856 1.00 25.83 ?  4503 ILE B CG1 1 
ATOM   2054 C  CG2 . ILE B 1 28  ? 24.018  30.936  -13.428 1.00 24.66 ?  4503 ILE B CG2 1 
ATOM   2055 C  CD1 . ILE B 1 28  ? 24.602  33.550  -14.803 1.00 27.32 ?  4503 ILE B CD1 1 
ATOM   2056 N  N   . ALA B 1 29  ? 25.220  27.686  -13.858 1.00 23.08 ?  4504 ALA B N   1 
ATOM   2057 C  CA  . ALA B 1 29  ? 24.563  26.391  -13.744 1.00 23.57 ?  4504 ALA B CA  1 
ATOM   2058 C  C   . ALA B 1 29  ? 23.521  26.414  -12.632 1.00 20.62 ?  4504 ALA B C   1 
ATOM   2059 O  O   . ALA B 1 29  ? 23.672  27.116  -11.625 1.00 22.36 ?  4504 ALA B O   1 
ATOM   2060 C  CB  . ALA B 1 29  ? 25.585  25.283  -13.462 1.00 24.26 ?  4504 ALA B CB  1 
ATOM   2061 N  N   . PHE B 1 30  ? 22.450  25.650  -12.833 1.00 21.56 ?  4505 PHE B N   1 
ATOM   2062 C  CA  . PHE B 1 30  ? 21.410  25.453  -11.832 1.00 18.20 ?  4505 PHE B CA  1 
ATOM   2063 C  C   . PHE B 1 30  ? 21.263  23.959  -11.587 1.00 21.79 ?  4505 PHE B C   1 
ATOM   2064 O  O   . PHE B 1 30  ? 20.935  23.211  -12.513 1.00 21.84 ?  4505 PHE B O   1 
ATOM   2065 C  CB  . PHE B 1 30  ? 20.082  26.036  -12.308 1.00 21.53 ?  4505 PHE B CB  1 
ATOM   2066 C  CG  . PHE B 1 30  ? 20.084  27.539  -12.423 1.00 26.90 ?  4505 PHE B CG  1 
ATOM   2067 C  CD1 . PHE B 1 30  ? 20.608  28.166  -13.545 1.00 22.98 ?  4505 PHE B CD1 1 
ATOM   2068 C  CD2 . PHE B 1 30  ? 19.560  28.323  -11.407 1.00 28.73 ?  4505 PHE B CD2 1 
ATOM   2069 C  CE1 . PHE B 1 30  ? 20.613  29.557  -13.653 1.00 25.19 ?  4505 PHE B CE1 1 
ATOM   2070 C  CE2 . PHE B 1 30  ? 19.561  29.714  -11.506 1.00 27.43 ?  4505 PHE B CE2 1 
ATOM   2071 C  CZ  . PHE B 1 30  ? 20.090  30.327  -12.633 1.00 27.24 ?  4505 PHE B CZ  1 
ATOM   2072 N  N   . MET B 1 31  ? 21.516  23.530  -10.351 1.00 19.88 ?  4506 MET B N   1 
ATOM   2073 C  CA  . MET B 1 31  ? 21.365  22.138  -9.930  1.00 19.70 ?  4506 MET B CA  1 
ATOM   2074 C  C   . MET B 1 31  ? 20.140  22.096  -9.031  1.00 20.30 ?  4506 MET B C   1 
ATOM   2075 O  O   . MET B 1 31  ? 20.164  22.641  -7.921  1.00 20.70 ?  4506 MET B O   1 
ATOM   2076 C  CB  . MET B 1 31  ? 22.608  21.679  -9.174  1.00 20.18 ?  4506 MET B CB  1 
ATOM   2077 C  CG  . MET B 1 31  ? 23.896  21.916  -9.923  1.00 19.43 ?  4506 MET B CG  1 
ATOM   2078 S  SD  . MET B 1 31  ? 25.351  21.299  -9.045  1.00 31.05 ?  4506 MET B SD  1 
ATOM   2079 C  CE  . MET B 1 31  ? 25.246  22.183  -7.471  1.00 20.99 ?  4506 MET B CE  1 
ATOM   2080 N  N   . VAL B 1 32  ? 19.071  21.462  -9.508  1.00 21.81 ?  4507 VAL B N   1 
ATOM   2081 C  CA  . VAL B 1 32  ? 17.751  21.561  -8.895  1.00 22.54 ?  4507 VAL B CA  1 
ATOM   2082 C  C   . VAL B 1 32  ? 17.313  20.198  -8.371  1.00 26.31 ?  4507 VAL B C   1 
ATOM   2083 O  O   . VAL B 1 32  ? 17.086  19.268  -9.155  1.00 23.97 ?  4507 VAL B O   1 
ATOM   2084 C  CB  . VAL B 1 32  ? 16.712  22.134  -9.870  1.00 25.79 ?  4507 VAL B CB  1 
ATOM   2085 C  CG1 . VAL B 1 32  ? 15.388  22.339  -9.146  1.00 24.85 ?  4507 VAL B CG1 1 
ATOM   2086 C  CG2 . VAL B 1 32  ? 17.209  23.443  -10.480 1.00 26.56 ?  4507 VAL B CG2 1 
ATOM   2087 N  N   . ASP B 1 33  ? 17.170  20.107  -7.049  1.00 23.82 ?  4508 ASP B N   1 
ATOM   2088 C  CA  . ASP B 1 33  ? 16.650  18.935  -6.354  1.00 24.29 ?  4508 ASP B CA  1 
ATOM   2089 C  C   . ASP B 1 33  ? 15.179  18.731  -6.699  1.00 26.86 ?  4508 ASP B C   1 
ATOM   2090 O  O   . ASP B 1 33  ? 14.362  19.643  -6.543  1.00 28.50 ?  4508 ASP B O   1 
ATOM   2091 C  CB  . ASP B 1 33  ? 16.796  19.220  -4.853  1.00 25.77 ?  4508 ASP B CB  1 
ATOM   2092 C  CG  . ASP B 1 33  ? 16.318  18.094  -3.946  1.00 30.61 ?  4508 ASP B CG  1 
ATOM   2093 O  OD1 . ASP B 1 33  ? 15.522  17.223  -4.357  1.00 32.18 ?  4508 ASP B OD1 1 
ATOM   2094 O  OD2 . ASP B 1 33  ? 16.737  18.117  -2.765  1.00 29.97 -1 4508 ASP B OD2 1 
ATOM   2095 N  N   . SER B 1 34  ? 14.835  17.527  -7.157  1.00 24.18 ?  4509 SER B N   1 
ATOM   2096 C  CA  . SER B 1 34  ? 13.441  17.133  -7.344  1.00 25.12 ?  4509 SER B CA  1 
ATOM   2097 C  C   . SER B 1 34  ? 13.150  15.814  -6.642  1.00 26.97 ?  4509 SER B C   1 
ATOM   2098 O  O   . SER B 1 34  ? 12.424  14.962  -7.162  1.00 27.86 ?  4509 SER B O   1 
ATOM   2099 C  CB  . SER B 1 34  ? 13.059  17.064  -8.820  1.00 26.65 ?  4509 SER B CB  1 
ATOM   2100 O  OG  . SER B 1 34  ? 13.694  15.975  -9.474  1.00 26.85 ?  4509 SER B OG  1 
ATOM   2101 N  N   . SER B 1 35  ? 13.706  15.632  -5.445  1.00 27.05 ?  4510 SER B N   1 
ATOM   2102 C  CA  . SER B 1 35  ? 13.435  14.446  -4.643  1.00 28.03 ?  4510 SER B CA  1 
ATOM   2103 C  C   . SER B 1 35  ? 11.977  14.430  -4.184  1.00 33.72 ?  4510 SER B C   1 
ATOM   2104 O  O   . SER B 1 35  ? 11.251  15.421  -4.286  1.00 35.12 ?  4510 SER B O   1 
ATOM   2105 C  CB  . SER B 1 35  ? 14.375  14.380  -3.437  1.00 30.41 ?  4510 SER B CB  1 
ATOM   2106 O  OG  . SER B 1 35  ? 14.221  15.506  -2.584  1.00 29.98 ?  4510 SER B OG  1 
ATOM   2107 N  N   . GLY B 1 36  ? 11.558  13.278  -3.652  1.00 31.03 ?  4511 GLY B N   1 
ATOM   2108 C  CA  . GLY B 1 36  ? 10.162  13.060  -3.304  1.00 35.62 ?  4511 GLY B CA  1 
ATOM   2109 C  C   . GLY B 1 36  ? 9.663   13.869  -2.125  1.00 34.82 ?  4511 GLY B C   1 
ATOM   2110 O  O   . GLY B 1 36  ? 8.446   13.995  -1.950  1.00 36.52 ?  4511 GLY B O   1 
ATOM   2111 N  N   . SER B 1 37  ? 10.569  14.418  -1.313  1.00 35.66 ?  4512 SER B N   1 
ATOM   2112 C  CA  . SER B 1 37  ? 10.162  15.249  -0.185  1.00 35.06 ?  4512 SER B CA  1 
ATOM   2113 C  C   . SER B 1 37  ? 9.649   16.614  -0.625  1.00 37.72 ?  4512 SER B C   1 
ATOM   2114 O  O   . SER B 1 37  ? 8.973   17.288  0.160   1.00 39.44 ?  4512 SER B O   1 
ATOM   2115 C  CB  . SER B 1 37  ? 11.336  15.432  0.772   1.00 33.45 ?  4512 SER B CB  1 
ATOM   2116 O  OG  . SER B 1 37  ? 12.336  16.220  0.169   1.00 35.06 ?  4512 SER B OG  1 
ATOM   2117 N  N   . ILE B 1 38  ? 9.964   17.040  -1.850  1.00 39.09 ?  4513 ILE B N   1 
ATOM   2118 C  CA  . ILE B 1 38  ? 9.457   18.313  -2.362  1.00 36.85 ?  4513 ILE B CA  1 
ATOM   2119 C  C   . ILE B 1 38  ? 7.935   18.276  -2.455  1.00 40.04 ?  4513 ILE B C   1 
ATOM   2120 O  O   . ILE B 1 38  ? 7.236   19.121  -1.884  1.00 41.31 ?  4513 ILE B O   1 
ATOM   2121 C  CB  . ILE B 1 38  ? 10.103  18.643  -3.720  1.00 37.56 ?  4513 ILE B CB  1 
ATOM   2122 C  CG1 . ILE B 1 38  ? 11.627  18.743  -3.586  1.00 35.74 ?  4513 ILE B CG1 1 
ATOM   2123 C  CG2 . ILE B 1 38  ? 9.521   19.927  -4.313  1.00 37.94 ?  4513 ILE B CG2 1 
ATOM   2124 C  CD1 . ILE B 1 38  ? 12.121  20.105  -3.144  1.00 38.99 ?  4513 ILE B CD1 1 
ATOM   2125 N  N   . GLY B 1 39  ? 7.404   17.282  -3.151  1.00 36.79 ?  4514 GLY B N   1 
ATOM   2126 C  CA  . GLY B 1 39  ? 5.974   17.274  -3.424  1.00 37.85 ?  4514 GLY B CA  1 
ATOM   2127 C  C   . GLY B 1 39  ? 5.646   17.963  -4.733  1.00 37.04 ?  4514 GLY B C   1 
ATOM   2128 O  O   . GLY B 1 39  ? 6.323   18.894  -5.171  1.00 38.34 ?  4514 GLY B O   1 
ATOM   2129 N  N   . SER B 1 40  ? 4.572   17.490  -5.371  1.00 38.18 ?  4515 SER B N   1 
ATOM   2130 C  CA  . SER B 1 40  ? 4.243   17.947  -6.719  1.00 36.88 ?  4515 SER B CA  1 
ATOM   2131 C  C   . SER B 1 40  ? 3.850   19.420  -6.751  1.00 39.23 ?  4515 SER B C   1 
ATOM   2132 O  O   . SER B 1 40  ? 4.131   20.112  -7.737  1.00 38.55 ?  4515 SER B O   1 
ATOM   2133 C  CB  . SER B 1 40  ? 3.122   17.090  -7.299  1.00 38.86 ?  4515 SER B CB  1 
ATOM   2134 O  OG  . SER B 1 40  ? 3.438   15.715  -7.184  1.00 44.06 ?  4515 SER B OG  1 
ATOM   2135 N  N   . SER B 1 41  ? 3.192   19.912  -5.700  1.00 41.71 ?  4516 SER B N   1 
ATOM   2136 C  CA  . SER B 1 41  ? 2.784   21.314  -5.679  1.00 38.83 ?  4516 SER B CA  1 
ATOM   2137 C  C   . SER B 1 41  ? 3.991   22.232  -5.555  1.00 37.95 ?  4516 SER B C   1 
ATOM   2138 O  O   . SER B 1 41  ? 4.137   23.189  -6.324  1.00 38.24 ?  4516 SER B O   1 
ATOM   2139 C  CB  . SER B 1 41  ? 1.794   21.561  -4.542  1.00 38.86 ?  4516 SER B CB  1 
ATOM   2140 O  OG  . SER B 1 41  ? 0.587   20.860  -4.770  1.00 46.13 ?  4516 SER B OG  1 
ATOM   2141 N  N   . ALA B 1 42  ? 4.866   21.959  -4.584  1.00 39.18 ?  4517 ALA B N   1 
ATOM   2142 C  CA  . ALA B 1 42  ? 6.091   22.740  -4.460  1.00 38.14 ?  4517 ALA B CA  1 
ATOM   2143 C  C   . ALA B 1 42  ? 6.939   22.638  -5.722  1.00 38.28 ?  4517 ALA B C   1 
ATOM   2144 O  O   . ALA B 1 42  ? 7.573   23.618  -6.133  1.00 35.83 ?  4517 ALA B O   1 
ATOM   2145 C  CB  . ALA B 1 42  ? 6.884   22.291  -3.233  1.00 40.03 ?  4517 ALA B CB  1 
ATOM   2146 N  N   . MET B 1 43  ? 6.955   21.462  -6.359  1.00 37.10 ?  4518 MET B N   1 
ATOM   2147 C  CA  . MET B 1 43  ? 7.756   21.302  -7.568  1.00 37.87 ?  4518 MET B CA  1 
ATOM   2148 C  C   . MET B 1 43  ? 7.260   22.214  -8.681  1.00 37.16 ?  4518 MET B C   1 
ATOM   2149 O  O   . MET B 1 43  ? 8.063   22.862  -9.364  1.00 37.47 ?  4518 MET B O   1 
ATOM   2150 C  CB  . MET B 1 43  ? 7.755   19.842  -8.025  1.00 35.35 ?  4518 MET B CB  1 
ATOM   2151 C  CG  . MET B 1 43  ? 8.782   19.530  -9.103  1.00 35.17 ?  4518 MET B CG  1 
ATOM   2152 S  SD  . MET B 1 43  ? 10.453  19.341  -8.444  1.00 41.20 ?  4518 MET B SD  1 
ATOM   2153 C  CE  . MET B 1 43  ? 11.109  21.002  -8.602  1.00 35.62 ?  4518 MET B CE  1 
ATOM   2154 N  N   . ASN B 1 44  ? 5.939   22.284  -8.875  1.00 38.29 ?  4519 ASN B N   1 
ATOM   2155 C  CA  . ASN B 1 44  ? 5.389   23.169  -9.898  1.00 38.68 ?  4519 ASN B CA  1 
ATOM   2156 C  C   . ASN B 1 44  ? 5.690   24.628  -9.584  1.00 36.12 ?  4519 ASN B C   1 
ATOM   2157 O  O   . ASN B 1 44  ? 5.956   25.424  -10.492 1.00 35.15 ?  4519 ASN B O   1 
ATOM   2158 C  CB  . ASN B 1 44  ? 3.883   22.946  -10.038 1.00 39.02 ?  4519 ASN B CB  1 
ATOM   2159 C  CG  . ASN B 1 44  ? 3.552   21.618  -10.687 1.00 43.76 ?  4519 ASN B CG  1 
ATOM   2160 O  OD1 . ASN B 1 44  ? 4.362   21.057  -11.428 1.00 42.48 ?  4519 ASN B OD1 1 
ATOM   2161 N  ND2 . ASN B 1 44  ? 2.354   21.107  -10.416 1.00 45.06 ?  4519 ASN B ND2 1 
ATOM   2162 N  N   . THR B 1 45  ? 5.652   24.998  -8.304  1.00 36.96 ?  4520 THR B N   1 
ATOM   2163 C  CA  . THR B 1 45  ? 6.035   26.354  -7.922  1.00 35.98 ?  4520 THR B CA  1 
ATOM   2164 C  C   . THR B 1 45  ? 7.504   26.605  -8.233  1.00 37.58 ?  4520 THR B C   1 
ATOM   2165 O  O   . THR B 1 45  ? 7.864   27.644  -8.801  1.00 35.33 ?  4520 THR B O   1 
ATOM   2166 C  CB  . THR B 1 45  ? 5.742   26.581  -6.438  1.00 38.89 ?  4520 THR B CB  1 
ATOM   2167 O  OG1 . THR B 1 45  ? 4.334   26.439  -6.203  1.00 39.18 ?  4520 THR B OG1 1 
ATOM   2168 C  CG2 . THR B 1 45  ? 6.182   27.973  -6.017  1.00 36.94 ?  4520 THR B CG2 1 
ATOM   2169 N  N   . ILE B 1 46  ? 8.370   25.651  -7.877  1.00 35.41 ?  4521 ILE B N   1 
ATOM   2170 C  CA  . ILE B 1 46  ? 9.789   25.769  -8.199  1.00 34.71 ?  4521 ILE B CA  1 
ATOM   2171 C  C   . ILE B 1 46  ? 9.986   25.950  -9.699  1.00 32.92 ?  4521 ILE B C   1 
ATOM   2172 O  O   . ILE B 1 46  ? 10.807  26.764  -10.140 1.00 31.66 ?  4521 ILE B O   1 
ATOM   2173 C  CB  . ILE B 1 46  ? 10.558  24.549  -7.658  1.00 34.00 ?  4521 ILE B CB  1 
ATOM   2174 C  CG1 . ILE B 1 46  ? 10.596  24.582  -6.130  1.00 34.25 ?  4521 ILE B CG1 1 
ATOM   2175 C  CG2 . ILE B 1 46  ? 11.964  24.499  -8.240  1.00 35.21 ?  4521 ILE B CG2 1 
ATOM   2176 C  CD1 . ILE B 1 46  ? 11.029  23.272  -5.500  1.00 36.17 ?  4521 ILE B CD1 1 
ATOM   2177 N  N   . LYS B 1 47  ? 9.231   25.201  -10.506 1.00 34.85 ?  4522 LYS B N   1 
ATOM   2178 C  CA  . LYS B 1 47  ? 9.393   25.282  -11.954 1.00 33.22 ?  4522 LYS B CA  1 
ATOM   2179 C  C   . LYS B 1 47  ? 9.006   26.657  -12.485 1.00 33.59 ?  4522 LYS B C   1 
ATOM   2180 O  O   . LYS B 1 47  ? 9.711   27.222  -13.327 1.00 34.11 ?  4522 LYS B O   1 
ATOM   2181 C  CB  . LYS B 1 47  ? 8.584   24.183  -12.639 1.00 35.23 ?  4522 LYS B CB  1 
ATOM   2182 C  CG  . LYS B 1 47  ? 9.109   22.782  -12.381 1.00 36.22 ?  4522 LYS B CG  1 
ATOM   2183 C  CD  . LYS B 1 47  ? 7.971   21.785  -12.396 1.00 39.81 ?  4522 LYS B CD  1 
ATOM   2184 C  CE  . LYS B 1 47  ? 7.245   21.836  -13.727 1.00 39.94 ?  4522 LYS B CE  1 
ATOM   2185 N  NZ  . LYS B 1 47  ? 5.815   21.440  -13.588 1.00 44.19 ?  4522 LYS B NZ  1 
ATOM   2186 N  N   . SER B 1 48  ? 7.893   27.214  -12.006 1.00 34.07 ?  4523 SER B N   1 
ATOM   2187 C  CA  . SER B 1 48  ? 7.488   28.541  -12.462 1.00 35.67 ?  4523 SER B CA  1 
ATOM   2188 C  C   . SER B 1 48  ? 8.439   29.616  -11.945 1.00 33.94 ?  4523 SER B C   1 
ATOM   2189 O  O   . SER B 1 48  ? 8.726   30.589  -12.652 1.00 34.33 ?  4523 SER B O   1 
ATOM   2190 C  CB  . SER B 1 48  ? 6.056   28.829  -12.023 1.00 35.22 ?  4523 SER B CB  1 
ATOM   2191 O  OG  . SER B 1 48  ? 5.956   28.769  -10.614 1.00 42.11 ?  4523 SER B OG  1 
ATOM   2192 N  N   . GLN B 1 49  ? 8.937   29.459  -10.715 1.00 34.25 ?  4524 GLN B N   1 
ATOM   2193 C  CA  . GLN B 1 49  ? 9.926   30.398  -10.194 1.00 32.22 ?  4524 GLN B CA  1 
ATOM   2194 C  C   . GLN B 1 49  ? 11.191  30.400  -11.046 1.00 33.98 ?  4524 GLN B C   1 
ATOM   2195 O  O   . GLN B 1 49  ? 11.730  31.465  -11.371 1.00 30.18 ?  4524 GLN B O   1 
ATOM   2196 C  CB  . GLN B 1 49  ? 10.251  30.058  -8.739  1.00 36.93 ?  4524 GLN B CB  1 
ATOM   2197 C  CG  . GLN B 1 49  ? 9.111   30.338  -7.767  1.00 37.30 ?  4524 GLN B CG  1 
ATOM   2198 C  CD  . GLN B 1 49  ? 8.929   31.819  -7.504  1.00 39.04 ?  4524 GLN B CD  1 
ATOM   2199 O  OE1 . GLN B 1 49  ? 9.832   32.481  -6.997  1.00 39.54 ?  4524 GLN B OE1 1 
ATOM   2200 N  NE2 . GLN B 1 49  ? 7.760   32.346  -7.848  1.00 41.24 ?  4524 GLN B NE2 1 
ATOM   2201 N  N   . LEU B 1 50  ? 11.675  29.215  -11.427 1.00 29.69 ?  4525 LEU B N   1 
ATOM   2202 C  CA  . LEU B 1 50  ? 12.892  29.141  -12.232 1.00 31.04 ?  4525 LEU B CA  1 
ATOM   2203 C  C   . LEU B 1 50  ? 12.662  29.684  -13.636 1.00 29.01 ?  4525 LEU B C   1 
ATOM   2204 O  O   . LEU B 1 50  ? 13.553  30.314  -14.219 1.00 30.34 ?  4525 LEU B O   1 
ATOM   2205 C  CB  . LEU B 1 50  ? 13.411  27.702  -12.277 1.00 27.87 ?  4525 LEU B CB  1 
ATOM   2206 C  CG  . LEU B 1 50  ? 14.030  27.193  -10.973 1.00 28.17 ?  4525 LEU B CG  1 
ATOM   2207 C  CD1 . LEU B 1 50  ? 14.310  25.695  -11.062 1.00 30.49 ?  4525 LEU B CD1 1 
ATOM   2208 C  CD2 . LEU B 1 50  ? 15.306  27.967  -10.661 1.00 33.37 ?  4525 LEU B CD2 1 
ATOM   2209 N  N   . ALA B 1 51  ? 11.479  29.443  -14.202 1.00 30.37 ?  4526 ALA B N   1 
ATOM   2210 C  CA  . ALA B 1 51  ? 11.165  30.014  -15.507 1.00 30.49 ?  4526 ALA B CA  1 
ATOM   2211 C  C   . ALA B 1 51  ? 11.220  31.538  -15.466 1.00 30.51 ?  4526 ALA B C   1 
ATOM   2212 O  O   . ALA B 1 51  ? 11.691  32.174  -16.414 1.00 30.66 ?  4526 ALA B O   1 
ATOM   2213 C  CB  . ALA B 1 51  ? 9.796   29.523  -15.981 1.00 33.04 ?  4526 ALA B CB  1 
ATOM   2214 N  N   . GLN B 1 52  ? 10.767  32.138  -14.362 1.00 32.04 ?  4527 GLN B N   1 
ATOM   2215 C  CA  . GLN B 1 52  ? 10.902  33.584  -14.197 1.00 32.64 ?  4527 GLN B CA  1 
ATOM   2216 C  C   . GLN B 1 52  ? 12.366  33.999  -14.129 1.00 34.00 ?  4527 GLN B C   1 
ATOM   2217 O  O   . GLN B 1 52  ? 12.758  35.015  -14.717 1.00 31.03 ?  4527 GLN B O   1 
ATOM   2218 C  CB  . GLN B 1 52  ? 10.167  34.040  -12.937 1.00 35.00 ?  4527 GLN B CB  1 
ATOM   2219 C  CG  . GLN B 1 52  ? 8.665   34.196  -13.112 1.00 42.03 ?  4527 GLN B CG  1 
ATOM   2220 C  CD  . GLN B 1 52  ? 7.935   34.332  -11.786 1.00 46.57 ?  4527 GLN B CD  1 
ATOM   2221 O  OE1 . GLN B 1 52  ? 8.358   35.080  -10.903 1.00 46.96 ?  4527 GLN B OE1 1 
ATOM   2222 N  NE2 . GLN B 1 52  ? 6.839   33.593  -11.640 1.00 47.61 ?  4527 GLN B NE2 1 
ATOM   2223 N  N   . VAL B 1 53  ? 13.185  33.230  -13.404 1.00 30.34 ?  4528 VAL B N   1 
ATOM   2224 C  CA  . VAL B 1 53  ? 14.609  33.542  -13.297 1.00 29.62 ?  4528 VAL B CA  1 
ATOM   2225 C  C   . VAL B 1 53  ? 15.257  33.566  -14.676 1.00 30.13 ?  4528 VAL B C   1 
ATOM   2226 O  O   . VAL B 1 53  ? 15.982  34.505  -15.022 1.00 28.11 ?  4528 VAL B O   1 
ATOM   2227 C  CB  . VAL B 1 53  ? 15.311  32.553  -12.350 1.00 29.05 ?  4528 VAL B CB  1 
ATOM   2228 C  CG1 . VAL B 1 53  ? 16.822  32.779  -12.363 1.00 28.39 ?  4528 VAL B CG1 1 
ATOM   2229 C  CG2 . VAL B 1 53  ? 14.759  32.683  -10.948 1.00 30.97 ?  4528 VAL B CG2 1 
ATOM   2230 N  N   . PHE B 1 54  ? 15.000  32.532  -15.488 1.00 27.21 ?  4529 PHE B N   1 
ATOM   2231 C  CA  . PHE B 1 54  ? 15.634  32.450  -16.799 1.00 29.18 ?  4529 PHE B CA  1 
ATOM   2232 C  C   . PHE B 1 54  ? 15.185  33.599  -17.691 1.00 27.94 ?  4529 PHE B C   1 
ATOM   2233 O  O   . PHE B 1 54  ? 15.990  34.168  -18.435 1.00 25.67 ?  4529 PHE B O   1 
ATOM   2234 C  CB  . PHE B 1 54  ? 15.313  31.105  -17.461 1.00 28.79 ?  4529 PHE B CB  1 
ATOM   2235 C  CG  . PHE B 1 54  ? 15.702  29.897  -16.635 1.00 29.56 ?  4529 PHE B CG  1 
ATOM   2236 C  CD1 . PHE B 1 54  ? 16.765  29.951  -15.741 1.00 28.01 ?  4529 PHE B CD1 1 
ATOM   2237 C  CD2 . PHE B 1 54  ? 14.998  28.704  -16.759 1.00 27.95 ?  4529 PHE B CD2 1 
ATOM   2238 C  CE1 . PHE B 1 54  ? 17.117  28.839  -14.977 1.00 28.21 ?  4529 PHE B CE1 1 
ATOM   2239 C  CE2 . PHE B 1 54  ? 15.344  27.587  -15.999 1.00 28.18 ?  4529 PHE B CE2 1 
ATOM   2240 C  CZ  . PHE B 1 54  ? 16.405  27.657  -15.111 1.00 28.10 ?  4529 PHE B CZ  1 
ATOM   2241 N  N   . SER B 1 55  ? 13.901  33.953  -17.620 1.00 28.23 ?  4530 SER B N   1 
ATOM   2242 C  CA  . SER B 1 55  ? 13.388  35.085  -18.383 1.00 31.40 ?  4530 SER B CA  1 
ATOM   2243 C  C   . SER B 1 55  ? 14.057  36.385  -17.943 1.00 30.62 ?  4530 SER B C   1 
ATOM   2244 O  O   . SER B 1 55  ? 14.496  37.185  -18.779 1.00 30.40 ?  4530 SER B O   1 
ATOM   2245 C  CB  . SER B 1 55  ? 11.870  35.159  -18.208 1.00 31.92 ?  4530 SER B CB  1 
ATOM   2246 O  OG  . SER B 1 55  ? 11.274  35.944  -19.221 1.00 42.19 ?  4530 SER B OG  1 
ATOM   2247 N  N   . SER B 1 56  ? 14.168  36.595  -16.626 1.00 30.89 ?  4531 SER B N   1 
ATOM   2248 C  CA  . SER B 1 56  ? 14.834  37.791  -16.112 1.00 30.16 ?  4531 SER B CA  1 
ATOM   2249 C  C   . SER B 1 56  ? 16.286  37.851  -16.565 1.00 32.61 ?  4531 SER B C   1 
ATOM   2250 O  O   . SER B 1 56  ? 16.778  38.916  -16.957 1.00 32.35 ?  4531 SER B O   1 
ATOM   2251 C  CB  . SER B 1 56  ? 14.769  37.820  -14.584 1.00 30.96 ?  4531 SER B CB  1 
ATOM   2252 O  OG  . SER B 1 56  ? 13.443  37.637  -14.118 1.00 38.56 ?  4531 SER B OG  1 
ATOM   2253 N  N   . LEU B 1 57  ? 16.991  36.716  -16.511 1.00 26.02 ?  4532 LEU B N   1 
ATOM   2254 C  CA  . LEU B 1 57  ? 18.404  36.702  -16.875 1.00 29.27 ?  4532 LEU B CA  1 
ATOM   2255 C  C   . LEU B 1 57  ? 18.601  36.970  -18.361 1.00 30.97 ?  4532 LEU B C   1 
ATOM   2256 O  O   . LEU B 1 57  ? 19.593  37.594  -18.757 1.00 29.47 ?  4532 LEU B O   1 
ATOM   2257 C  CB  . LEU B 1 57  ? 19.038  35.368  -16.482 1.00 27.44 ?  4532 LEU B CB  1 
ATOM   2258 C  CG  . LEU B 1 57  ? 19.150  35.058  -14.988 1.00 31.41 ?  4532 LEU B CG  1 
ATOM   2259 C  CD1 . LEU B 1 57  ? 19.715  33.654  -14.775 1.00 30.93 ?  4532 LEU B CD1 1 
ATOM   2260 C  CD2 . LEU B 1 57  ? 19.998  36.100  -14.264 1.00 32.84 ?  4532 LEU B CD2 1 
ATOM   2261 N  N   . LYS B 1 58  ? 17.685  36.490  -19.203 1.00 28.33 ?  4533 LYS B N   1 
ATOM   2262 C  CA  . LYS B 1 58  ? 17.802  36.767  -20.628 1.00 30.35 ?  4533 LYS B CA  1 
ATOM   2263 C  C   . LYS B 1 58  ? 17.622  38.254  -20.900 1.00 29.33 ?  4533 LYS B C   1 
ATOM   2264 O  O   . LYS B 1 58  ? 18.356  38.840  -21.705 1.00 30.51 ?  4533 LYS B O   1 
ATOM   2265 C  CB  . LYS B 1 58  ? 16.789  35.933  -21.413 1.00 32.37 ?  4533 LYS B CB  1 
ATOM   2266 C  CG  . LYS B 1 58  ? 16.881  36.104  -22.919 1.00 31.64 ?  4533 LYS B CG  1 
ATOM   2267 C  CD  . LYS B 1 58  ? 15.967  35.126  -23.647 1.00 36.32 ?  4533 LYS B CD  1 
ATOM   2268 C  CE  . LYS B 1 58  ? 15.951  35.375  -25.158 1.00 35.76 ?  4533 LYS B CE  1 
ATOM   2269 N  NZ  . LYS B 1 58  ? 17.125  34.802  -25.885 1.00 40.92 ?  4533 LYS B NZ  1 
ATOM   2270 N  N   . ALA B 1 59  ? 16.669  38.881  -20.211 1.00 27.67 ?  4534 ALA B N   1 
ATOM   2271 C  CA  . ALA B 1 59  ? 16.485  40.324  -20.338 1.00 30.22 ?  4534 ALA B CA  1 
ATOM   2272 C  C   . ALA B 1 59  ? 17.715  41.073  -19.839 1.00 30.98 ?  4534 ALA B C   1 
ATOM   2273 O  O   . ALA B 1 59  ? 18.259  41.939  -20.539 1.00 27.97 ?  4534 ALA B O   1 
ATOM   2274 C  CB  . ALA B 1 59  ? 15.233  40.751  -19.574 1.00 26.55 ?  4534 ALA B CB  1 
ATOM   2275 N  N   . SER B 1 60  ? 18.184  40.726  -18.636 1.00 28.58 ?  4535 SER B N   1 
ATOM   2276 C  CA  . SER B 1 60  ? 19.325  41.411  -18.036 1.00 29.75 ?  4535 SER B CA  1 
ATOM   2277 C  C   . SER B 1 60  ? 20.590  41.253  -18.865 1.00 28.54 ?  4535 SER B C   1 
ATOM   2278 O  O   . SER B 1 60  ? 21.463  42.128  -18.831 1.00 28.64 ?  4535 SER B O   1 
ATOM   2279 C  CB  . SER B 1 60  ? 19.564  40.874  -16.625 1.00 30.93 ?  4535 SER B CB  1 
ATOM   2280 O  OG  . SER B 1 60  ? 18.386  40.974  -15.847 1.00 39.78 ?  4535 SER B OG  1 
ATOM   2281 N  N   . ALA B 1 61  ? 20.720  40.151  -19.608 1.00 26.77 ?  4536 ALA B N   1 
ATOM   2282 C  CA  . ALA B 1 61  ? 21.930  39.939  -20.394 1.00 26.56 ?  4536 ALA B CA  1 
ATOM   2283 C  C   . ALA B 1 61  ? 22.121  41.060  -21.406 1.00 23.19 ?  4536 ALA B C   1 
ATOM   2284 O  O   . ALA B 1 61  ? 23.252  41.490  -21.662 1.00 30.48 ?  4536 ALA B O   1 
ATOM   2285 C  CB  . ALA B 1 61  ? 21.871  38.588  -21.104 1.00 28.40 ?  4536 ALA B CB  1 
ATOM   2286 N  N   . GLY B 1 62  ? 21.026  41.549  -21.977 1.00 25.23 ?  4537 GLY B N   1 
ATOM   2287 C  CA  . GLY B 1 62  ? 21.093  42.661  -22.907 1.00 27.14 ?  4537 GLY B CA  1 
ATOM   2288 C  C   . GLY B 1 62  ? 21.290  43.989  -22.200 1.00 24.72 ?  4537 GLY B C   1 
ATOM   2289 O  O   . GLY B 1 62  ? 22.275  44.688  -22.453 1.00 24.28 ?  4537 GLY B O   1 
ATOM   2290 N  N   . THR B 1 63  ? 20.370  44.319  -21.285 1.00 24.07 ?  4538 THR B N   1 
ATOM   2291 C  CA  . THR B 1 63  ? 20.389  45.624  -20.622 1.00 22.52 ?  4538 THR B CA  1 
ATOM   2292 C  C   . THR B 1 63  ? 21.669  45.845  -19.825 1.00 23.20 ?  4538 THR B C   1 
ATOM   2293 O  O   . THR B 1 63  ? 22.136  46.984  -19.694 1.00 19.16 ?  4538 THR B O   1 
ATOM   2294 C  CB  . THR B 1 63  ? 19.170  45.749  -19.705 1.00 27.17 ?  4538 THR B CB  1 
ATOM   2295 O  OG1 . THR B 1 63  ? 17.994  45.382  -20.437 1.00 37.06 ?  4538 THR B OG1 1 
ATOM   2296 C  CG2 . THR B 1 63  ? 19.017  47.174  -19.214 1.00 28.83 ?  4538 THR B CG2 1 
ATOM   2297 N  N   . ASP B 1 64  ? 22.231  44.790  -19.255 1.00 19.28 ?  4539 ASP B N   1 
ATOM   2298 C  CA  . ASP B 1 64  ? 23.473  44.904  -18.509 1.00 21.30 ?  4539 ASP B CA  1 
ATOM   2299 C  C   . ASP B 1 64  ? 24.704  44.722  -19.387 1.00 21.56 ?  4539 ASP B C   1 
ATOM   2300 O  O   . ASP B 1 64  ? 25.827  44.790  -18.876 1.00 25.38 ?  4539 ASP B O   1 
ATOM   2301 C  CB  . ASP B 1 64  ? 23.491  43.905  -17.342 1.00 20.30 ?  4539 ASP B CB  1 
ATOM   2302 C  CG  . ASP B 1 64  ? 22.468  44.237  -16.258 1.00 20.63 ?  4539 ASP B CG  1 
ATOM   2303 O  OD1 . ASP B 1 64  ? 22.244  45.431  -15.984 1.00 17.76 ?  4539 ASP B OD1 1 
ATOM   2304 O  OD2 . ASP B 1 64  ? 21.891  43.290  -15.669 1.00 24.01 -1 4539 ASP B OD2 1 
ATOM   2305 N  N   . GLY B 1 65  ? 24.517  44.491  -20.686 1.00 20.79 ?  4540 GLY B N   1 
ATOM   2306 C  CA  . GLY B 1 65  ? 25.612  44.413  -21.645 1.00 24.07 ?  4540 GLY B CA  1 
ATOM   2307 C  C   . GLY B 1 65  ? 26.541  43.238  -21.454 1.00 23.61 ?  4540 GLY B C   1 
ATOM   2308 O  O   . GLY B 1 65  ? 27.763  43.381  -21.615 1.00 26.01 ?  4540 GLY B O   1 
ATOM   2309 N  N   . ALA B 1 66  ? 25.999  42.083  -21.086 1.00 24.43 ?  4541 ALA B N   1 
ATOM   2310 C  CA  . ALA B 1 66  ? 26.840  40.915  -20.924 1.00 24.21 ?  4541 ALA B CA  1 
ATOM   2311 C  C   . ALA B 1 66  ? 27.348  40.447  -22.282 1.00 29.32 ?  4541 ALA B C   1 
ATOM   2312 O  O   . ALA B 1 66  ? 26.785  40.772  -23.333 1.00 28.27 ?  4541 ALA B O   1 
ATOM   2313 C  CB  . ALA B 1 66  ? 26.059  39.790  -20.245 1.00 24.13 ?  4541 ALA B CB  1 
ATOM   2314 N  N   . GLY B 1 67  ? 28.454  39.706  -22.247 1.00 25.92 ?  4542 GLY B N   1 
ATOM   2315 C  CA  . GLY B 1 67  ? 28.955  39.022  -23.421 1.00 23.60 ?  4542 GLY B CA  1 
ATOM   2316 C  C   . GLY B 1 67  ? 28.198  37.727  -23.634 1.00 28.86 ?  4542 GLY B C   1 
ATOM   2317 O  O   . GLY B 1 67  ? 26.967  37.730  -23.731 1.00 32.13 ?  4542 GLY B O   1 
ATOM   2318 N  N   . THR B 1 68  ? 28.915  36.611  -23.687 1.00 26.46 ?  4543 THR B N   1 
ATOM   2319 C  CA  . THR B 1 68  ? 28.276  35.314  -23.873 1.00 25.01 ?  4543 THR B CA  1 
ATOM   2320 C  C   . THR B 1 68  ? 27.802  34.782  -22.523 1.00 23.84 ?  4543 THR B C   1 
ATOM   2321 O  O   . THR B 1 68  ? 28.595  34.667  -21.580 1.00 25.29 ?  4543 THR B O   1 
ATOM   2322 C  CB  . THR B 1 68  ? 29.258  34.348  -24.529 1.00 29.30 ?  4543 THR B CB  1 
ATOM   2323 O  OG1 . THR B 1 68  ? 29.617  34.852  -25.822 1.00 29.59 ?  4543 THR B OG1 1 
ATOM   2324 C  CG2 . THR B 1 68  ? 28.636  32.962  -24.679 1.00 27.40 ?  4543 THR B CG2 1 
ATOM   2325 N  N   . VAL B 1 69  ? 26.511  34.478  -22.427 1.00 24.42 ?  4544 VAL B N   1 
ATOM   2326 C  CA  . VAL B 1 69  ? 25.917  33.907  -21.225 1.00 26.10 ?  4544 VAL B CA  1 
ATOM   2327 C  C   . VAL B 1 69  ? 25.438  32.499  -21.559 1.00 28.04 ?  4544 VAL B C   1 
ATOM   2328 O  O   . VAL B 1 69  ? 24.446  32.323  -22.279 1.00 27.26 ?  4544 VAL B O   1 
ATOM   2329 C  CB  . VAL B 1 69  ? 24.771  34.769  -20.681 1.00 27.03 ?  4544 VAL B CB  1 
ATOM   2330 C  CG1 . VAL B 1 69  ? 24.222  34.163  -19.404 1.00 24.24 ?  4544 VAL B CG1 1 
ATOM   2331 C  CG2 . VAL B 1 69  ? 25.258  36.189  -20.421 1.00 27.89 ?  4544 VAL B CG2 1 
ATOM   2332 N  N   . ASN B 1 70  ? 26.137  31.497  -21.026 1.00 23.73 ?  4545 ASN B N   1 
ATOM   2333 C  CA  . ASN B 1 70  ? 25.710  30.107  -21.112 1.00 24.39 ?  4545 ASN B CA  1 
ATOM   2334 C  C   . ASN B 1 70  ? 24.994  29.720  -19.827 1.00 22.61 ?  4545 ASN B C   1 
ATOM   2335 O  O   . ASN B 1 70  ? 25.450  30.050  -18.723 1.00 24.03 ?  4545 ASN B O   1 
ATOM   2336 C  CB  . ASN B 1 70  ? 26.907  29.176  -21.305 1.00 26.20 ?  4545 ASN B CB  1 
ATOM   2337 C  CG  . ASN B 1 70  ? 27.607  29.385  -22.622 1.00 24.61 ?  4545 ASN B CG  1 
ATOM   2338 O  OD1 . ASN B 1 70  ? 28.833  29.500  -22.673 1.00 29.66 ?  4545 ASN B OD1 1 
ATOM   2339 N  ND2 . ASN B 1 70  ? 26.839  29.416  -23.702 1.00 27.05 ?  4545 ASN B ND2 1 
ATOM   2340 N  N   . ILE B 1 71  ? 23.873  29.019  -19.974 1.00 25.32 ?  4546 ILE B N   1 
ATOM   2341 C  CA  . ILE B 1 71  ? 23.081  28.540  -18.848 1.00 23.83 ?  4546 ILE B CA  1 
ATOM   2342 C  C   . ILE B 1 71  ? 23.008  27.025  -18.922 1.00 24.01 ?  4546 ILE B C   1 
ATOM   2343 O  O   . ILE B 1 71  ? 22.716  26.465  -19.984 1.00 24.69 ?  4546 ILE B O   1 
ATOM   2344 C  CB  . ILE B 1 71  ? 21.663  29.134  -18.852 1.00 23.89 ?  4546 ILE B CB  1 
ATOM   2345 C  CG1 . ILE B 1 71  ? 21.727  30.659  -18.815 1.00 25.65 ?  4546 ILE B CG1 1 
ATOM   2346 C  CG2 . ILE B 1 71  ? 20.864  28.606  -17.667 1.00 25.86 ?  4546 ILE B CG2 1 
ATOM   2347 C  CD1 . ILE B 1 71  ? 22.255  31.213  -17.523 1.00 26.06 ?  4546 ILE B CD1 1 
ATOM   2348 N  N   . PHE B 1 72  ? 23.253  26.369  -17.790 1.00 21.96 ?  4547 PHE B N   1 
ATOM   2349 C  CA  . PHE B 1 72  ? 23.104  24.925  -17.652 1.00 22.80 ?  4547 PHE B CA  1 
ATOM   2350 C  C   . PHE B 1 72  ? 22.055  24.667  -16.583 1.00 22.95 ?  4547 PHE B C   1 
ATOM   2351 O  O   . PHE B 1 72  ? 22.111  25.262  -15.501 1.00 24.15 ?  4547 PHE B O   1 
ATOM   2352 C  CB  . PHE B 1 72  ? 24.442  24.304  -17.246 1.00 23.31 ?  4547 PHE B CB  1 
ATOM   2353 C  CG  . PHE B 1 72  ? 24.414  22.804  -17.095 1.00 21.61 ?  4547 PHE B CG  1 
ATOM   2354 C  CD1 . PHE B 1 72  ? 24.315  21.982  -18.204 1.00 22.84 ?  4547 PHE B CD1 1 
ATOM   2355 C  CD2 . PHE B 1 72  ? 24.520  22.221  -15.843 1.00 22.04 ?  4547 PHE B CD2 1 
ATOM   2356 C  CE1 . PHE B 1 72  ? 24.299  20.600  -18.062 1.00 22.08 ?  4547 PHE B CE1 1 
ATOM   2357 C  CE2 . PHE B 1 72  ? 24.516  20.838  -15.693 1.00 22.95 ?  4547 PHE B CE2 1 
ATOM   2358 C  CZ  . PHE B 1 72  ? 24.407  20.030  -16.806 1.00 21.75 ?  4547 PHE B CZ  1 
ATOM   2359 N  N   . LEU B 1 73  ? 21.092  23.803  -16.884 1.00 20.87 ?  4548 LEU B N   1 
ATOM   2360 C  CA  . LEU B 1 73  ? 20.059  23.432  -15.929 1.00 21.23 ?  4548 LEU B CA  1 
ATOM   2361 C  C   . LEU B 1 73  ? 20.042  21.918  -15.834 1.00 22.38 ?  4548 LEU B C   1 
ATOM   2362 O  O   . LEU B 1 73  ? 19.977  21.243  -16.864 1.00 23.34 ?  4548 LEU B O   1 
ATOM   2363 C  CB  . LEU B 1 73  ? 18.688  23.925  -16.396 1.00 23.61 ?  4548 LEU B CB  1 
ATOM   2364 C  CG  . LEU B 1 73  ? 17.470  23.414  -15.629 1.00 23.53 ?  4548 LEU B CG  1 
ATOM   2365 C  CD1 . LEU B 1 73  ? 17.533  23.786  -14.149 1.00 25.04 ?  4548 LEU B CD1 1 
ATOM   2366 C  CD2 . LEU B 1 73  ? 16.185  23.922  -16.268 1.00 28.52 ?  4548 LEU B CD2 1 
ATOM   2367 N  N   . VAL B 1 74  ? 20.105  21.385  -14.614 1.00 20.21 ?  4549 VAL B N   1 
ATOM   2368 C  CA  . VAL B 1 74  ? 20.062  19.939  -14.410 1.00 21.75 ?  4549 VAL B CA  1 
ATOM   2369 C  C   . VAL B 1 74  ? 19.106  19.611  -13.277 1.00 21.26 ?  4549 VAL B C   1 
ATOM   2370 O  O   . VAL B 1 74  ? 19.186  20.193  -12.188 1.00 22.55 ?  4549 VAL B O   1 
ATOM   2371 C  CB  . VAL B 1 74  ? 21.458  19.319  -14.178 1.00 20.50 ?  4549 VAL B CB  1 
ATOM   2372 C  CG1 . VAL B 1 74  ? 22.162  19.956  -12.975 1.00 21.95 ?  4549 VAL B CG1 1 
ATOM   2373 C  CG2 . VAL B 1 74  ? 21.349  17.791  -14.015 1.00 23.75 ?  4549 VAL B CG2 1 
ATOM   2374 N  N   . ASP B 1 75  ? 18.199  18.679  -13.538 1.00 22.17 ?  4550 ASP B N   1 
ATOM   2375 C  CA  . ASP B 1 75  ? 17.306  18.143  -12.531 1.00 22.00 ?  4550 ASP B CA  1 
ATOM   2376 C  C   . ASP B 1 75  ? 17.988  16.938  -11.897 1.00 24.87 ?  4550 ASP B C   1 
ATOM   2377 O  O   . ASP B 1 75  ? 18.660  16.168  -12.586 1.00 22.36 ?  4550 ASP B O   1 
ATOM   2378 C  CB  . ASP B 1 75  ? 16.011  17.712  -13.222 1.00 25.38 ?  4550 ASP B CB  1 
ATOM   2379 C  CG  . ASP B 1 75  ? 15.153  16.825  -12.359 1.00 28.86 ?  4550 ASP B CG  1 
ATOM   2380 O  OD1 . ASP B 1 75  ? 14.964  17.162  -11.176 1.00 28.83 ?  4550 ASP B OD1 1 
ATOM   2381 O  OD2 . ASP B 1 75  ? 14.655  15.793  -12.864 1.00 29.82 -1 4550 ASP B OD2 1 
ATOM   2382 N  N   . PHE B 1 76  ? 17.853  16.791  -10.581 1.00 22.11 ?  4551 PHE B N   1 
ATOM   2383 C  CA  . PHE B 1 76  ? 18.490  15.649  -9.934  1.00 23.12 ?  4551 PHE B CA  1 
ATOM   2384 C  C   . PHE B 1 76  ? 17.645  15.117  -8.788  1.00 23.84 ?  4551 PHE B C   1 
ATOM   2385 O  O   . PHE B 1 76  ? 16.969  15.870  -8.080  1.00 23.02 ?  4551 PHE B O   1 
ATOM   2386 C  CB  . PHE B 1 76  ? 19.937  15.932  -9.484  1.00 21.03 ?  4551 PHE B CB  1 
ATOM   2387 C  CG  . PHE B 1 76  ? 20.057  16.579  -8.120  1.00 22.18 ?  4551 PHE B CG  1 
ATOM   2388 C  CD1 . PHE B 1 76  ? 19.992  17.958  -7.987  1.00 21.10 ?  4551 PHE B CD1 1 
ATOM   2389 C  CD2 . PHE B 1 76  ? 20.267  15.809  -6.981  1.00 22.50 ?  4551 PHE B CD2 1 
ATOM   2390 C  CE1 . PHE B 1 76  ? 20.116  18.557  -6.740  1.00 22.31 ?  4551 PHE B CE1 1 
ATOM   2391 C  CE2 . PHE B 1 76  ? 20.389  16.398  -5.729  1.00 24.04 ?  4551 PHE B CE2 1 
ATOM   2392 C  CZ  . PHE B 1 76  ? 20.312  17.781  -5.611  1.00 23.77 ?  4551 PHE B CZ  1 
ATOM   2393 N  N   . ASP B 1 77  ? 17.699  13.795  -8.620  1.00 22.40 ?  4552 ASP B N   1 
ATOM   2394 C  CA  . ASP B 1 77  ? 17.248  13.148  -7.398  1.00 22.70 ?  4552 ASP B CA  1 
ATOM   2395 C  C   . ASP B 1 77  ? 18.157  11.970  -7.059  1.00 23.31 ?  4552 ASP B C   1 
ATOM   2396 O  O   . ASP B 1 77  ? 19.297  12.181  -6.631  1.00 23.46 ?  4552 ASP B O   1 
ATOM   2397 C  CB  . ASP B 1 77  ? 15.749  12.799  -7.435  1.00 22.69 ?  4552 ASP B CB  1 
ATOM   2398 C  CG  . ASP B 1 77  ? 15.319  12.108  -8.716  1.00 27.54 ?  4552 ASP B CG  1 
ATOM   2399 O  OD1 . ASP B 1 77  ? 15.521  10.877  -8.836  1.00 26.00 ?  4552 ASP B OD1 1 
ATOM   2400 O  OD2 . ASP B 1 77  ? 14.737  12.787  -9.591  1.00 25.13 -1 4552 ASP B OD2 1 
ATOM   2401 N  N   . THR B 1 78  ? 17.683  10.737  -7.263  1.00 23.85 ?  4553 THR B N   1 
ATOM   2402 C  CA  . THR B 1 78  ? 18.534  9.571   -7.023  1.00 24.46 ?  4553 THR B CA  1 
ATOM   2403 C  C   . THR B 1 78  ? 19.788  9.619   -7.889  1.00 22.98 ?  4553 THR B C   1 
ATOM   2404 O  O   . THR B 1 78  ? 20.866  9.184   -7.465  1.00 20.62 ?  4553 THR B O   1 
ATOM   2405 C  CB  . THR B 1 78  ? 17.734  8.296   -7.293  1.00 25.50 ?  4553 THR B CB  1 
ATOM   2406 O  OG1 . THR B 1 78  ? 16.564  8.293   -6.471  1.00 25.61 ?  4553 THR B OG1 1 
ATOM   2407 C  CG2 . THR B 1 78  ? 18.561  7.070   -6.975  1.00 25.80 ?  4553 THR B CG2 1 
ATOM   2408 N  N   . LEU B 1 79  ? 19.659  10.136  -9.109  1.00 20.97 ?  4554 LEU B N   1 
ATOM   2409 C  CA  . LEU B 1 79  ? 20.773  10.538  -9.958  1.00 20.37 ?  4554 LEU B CA  1 
ATOM   2410 C  C   . LEU B 1 79  ? 20.408  11.867  -10.600 1.00 19.64 ?  4554 LEU B C   1 
ATOM   2411 O  O   . LEU B 1 79  ? 19.252  12.300  -10.555 1.00 21.22 ?  4554 LEU B O   1 
ATOM   2412 C  CB  . LEU B 1 79  ? 21.024  9.529   -11.081 1.00 22.39 ?  4554 LEU B CB  1 
ATOM   2413 C  CG  . LEU B 1 79  ? 21.605  8.173   -10.695 1.00 20.57 ?  4554 LEU B CG  1 
ATOM   2414 C  CD1 . LEU B 1 79  ? 21.555  7.263   -11.902 1.00 23.17 ?  4554 LEU B CD1 1 
ATOM   2415 C  CD2 . LEU B 1 79  ? 23.028  8.302   -10.195 1.00 20.78 ?  4554 LEU B CD2 1 
ATOM   2416 N  N   . ALA B 1 80  ? 21.390  12.515  -11.220 1.00 20.01 ?  4555 ALA B N   1 
ATOM   2417 C  CA  . ALA B 1 80  ? 21.057  13.616  -12.111 1.00 20.96 ?  4555 ALA B CA  1 
ATOM   2418 C  C   . ALA B 1 80  ? 20.313  13.070  -13.322 1.00 23.96 ?  4555 ALA B C   1 
ATOM   2419 O  O   . ALA B 1 80  ? 20.671  12.022  -13.876 1.00 25.48 ?  4555 ALA B O   1 
ATOM   2420 C  CB  . ALA B 1 80  ? 22.310  14.368  -12.559 1.00 21.59 ?  4555 ALA B CB  1 
ATOM   2421 N  N   . ASN B 1 81  ? 19.260  13.775  -13.721 1.00 23.10 ?  4556 ASN B N   1 
ATOM   2422 C  CA  . ASN B 1 81  ? 18.392  13.291  -14.784 1.00 23.92 ?  4556 ASN B CA  1 
ATOM   2423 C  C   . ASN B 1 81  ? 18.649  14.062  -16.069 1.00 23.07 ?  4556 ASN B C   1 
ATOM   2424 O  O   . ASN B 1 81  ? 19.783  14.080  -16.563 1.00 26.08 ?  4556 ASN B O   1 
ATOM   2425 C  CB  . ASN B 1 81  ? 16.936  13.380  -14.335 1.00 23.39 ?  4556 ASN B CB  1 
ATOM   2426 C  CG  . ASN B 1 81  ? 16.678  12.585  -13.070 1.00 25.04 ?  4556 ASN B CG  1 
ATOM   2427 O  OD1 . ASN B 1 81  ? 17.060  11.418  -12.975 1.00 26.41 ?  4556 ASN B OD1 1 
ATOM   2428 N  ND2 . ASN B 1 81  ? 16.049  13.212  -12.086 1.00 26.12 ?  4556 ASN B ND2 1 
ATOM   2429 N  N   . LYS B 1 82  ? 17.621  14.708  -16.615 1.00 25.69 ?  4557 LYS B N   1 
ATOM   2430 C  CA  . LYS B 1 82  ? 17.787  15.488  -17.832 1.00 25.87 ?  4557 LYS B CA  1 
ATOM   2431 C  C   . LYS B 1 82  ? 18.499  16.806  -17.539 1.00 23.54 ?  4557 LYS B C   1 
ATOM   2432 O  O   . LYS B 1 82  ? 18.391  17.368  -16.442 1.00 25.23 ?  4557 LYS B O   1 
ATOM   2433 C  CB  . LYS B 1 82  ? 16.425  15.764  -18.475 1.00 26.35 ?  4557 LYS B CB  1 
ATOM   2434 C  CG  . LYS B 1 82  ? 15.794  14.555  -19.157 1.00 30.38 ?  4557 LYS B CG  1 
ATOM   2435 C  CD  . LYS B 1 82  ? 14.666  14.983  -20.096 1.00 33.90 ?  4557 LYS B CD  1 
ATOM   2436 C  CE  . LYS B 1 82  ? 14.258  13.855  -21.043 1.00 37.53 ?  4557 LYS B CE  1 
ATOM   2437 N  NZ  . LYS B 1 82  ? 13.000  13.187  -20.614 1.00 40.66 ?  4557 LYS B NZ  1 
ATOM   2438 N  N   . SER B 1 83  ? 19.251  17.284  -18.528 1.00 26.52 ?  4558 SER B N   1 
ATOM   2439 C  CA  . SER B 1 83  ? 19.945  18.561  -18.428 1.00 23.00 ?  4558 SER B CA  1 
ATOM   2440 C  C   . SER B 1 83  ? 19.981  19.216  -19.801 1.00 27.19 ?  4558 SER B C   1 
ATOM   2441 O  O   . SER B 1 83  ? 19.735  18.577  -20.826 1.00 26.27 ?  4558 SER B O   1 
ATOM   2442 C  CB  . SER B 1 83  ? 21.364  18.399  -17.867 1.00 26.55 ?  4558 SER B CB  1 
ATOM   2443 O  OG  . SER B 1 83  ? 22.200  17.695  -18.772 1.00 26.59 ?  4558 SER B OG  1 
ATOM   2444 N  N   . VAL B 1 84  ? 20.294  20.510  -19.818 1.00 25.27 ?  4559 VAL B N   1 
ATOM   2445 C  CA  . VAL B 1 84  ? 20.462  21.227  -21.076 1.00 25.29 ?  4559 VAL B CA  1 
ATOM   2446 C  C   . VAL B 1 84  ? 21.433  22.379  -20.867 1.00 23.87 ?  4559 VAL B C   1 
ATOM   2447 O  O   . VAL B 1 84  ? 21.497  22.978  -19.788 1.00 23.71 ?  4559 VAL B O   1 
ATOM   2448 C  CB  . VAL B 1 84  ? 19.114  21.692  -21.686 1.00 28.10 ?  4559 VAL B CB  1 
ATOM   2449 C  CG1 . VAL B 1 84  ? 18.593  22.942  -20.977 1.00 28.47 ?  4559 VAL B CG1 1 
ATOM   2450 C  CG2 . VAL B 1 84  ? 19.264  21.938  -23.184 1.00 29.68 ?  4559 VAL B CG2 1 
ATOM   2451 N  N   . SER B 1 85  ? 22.214  22.662  -21.906 1.00 24.33 ?  4560 SER B N   1 
ATOM   2452 C  CA  . SER B 1 85  ? 23.116  23.800  -21.953 1.00 25.11 ?  4560 SER B CA  1 
ATOM   2453 C  C   . SER B 1 85  ? 22.652  24.689  -23.094 1.00 28.51 ?  4560 SER B C   1 
ATOM   2454 O  O   . SER B 1 85  ? 22.490  24.214  -24.223 1.00 26.76 ?  4560 SER B O   1 
ATOM   2455 C  CB  . SER B 1 85  ? 24.546  23.325  -22.214 1.00 28.73 ?  4560 SER B CB  1 
ATOM   2456 O  OG  . SER B 1 85  ? 25.440  24.413  -22.330 1.00 28.37 ?  4560 SER B OG  1 
ATOM   2457 N  N   . VAL B 1 86  ? 22.403  25.963  -22.797 1.00 26.71 ?  4561 VAL B N   1 
ATOM   2458 C  CA  . VAL B 1 86  ? 21.922  26.905  -23.802 1.00 25.69 ?  4561 VAL B CA  1 
ATOM   2459 C  C   . VAL B 1 86  ? 22.759  28.174  -23.762 1.00 29.57 ?  4561 VAL B C   1 
ATOM   2460 O  O   . VAL B 1 86  ? 23.319  28.549  -22.725 1.00 29.38 ?  4561 VAL B O   1 
ATOM   2461 C  CB  . VAL B 1 86  ? 20.420  27.259  -23.644 1.00 25.86 ?  4561 VAL B CB  1 
ATOM   2462 C  CG1 . VAL B 1 86  ? 19.556  26.008  -23.593 1.00 31.41 ?  4561 VAL B CG1 1 
ATOM   2463 C  CG2 . VAL B 1 86  ? 20.193  28.139  -22.425 1.00 28.12 ?  4561 VAL B CG2 1 
ATOM   2464 N  N   . ASN B 1 87  ? 22.841  28.835  -24.912 1.00 27.71 ?  4562 ASN B N   1 
ATOM   2465 C  CA  . ASN B 1 87  ? 23.278  30.221  -24.983 1.00 29.38 ?  4562 ASN B CA  1 
ATOM   2466 C  C   . ASN B 1 87  ? 22.028  31.082  -24.860 1.00 32.06 ?  4562 ASN B C   1 
ATOM   2467 O  O   . ASN B 1 87  ? 21.109  30.970  -25.679 1.00 32.43 ?  4562 ASN B O   1 
ATOM   2468 C  CB  . ASN B 1 87  ? 24.004  30.482  -26.302 1.00 31.53 ?  4562 ASN B CB  1 
ATOM   2469 C  CG  . ASN B 1 87  ? 24.572  31.889  -26.389 1.00 32.28 ?  4562 ASN B CG  1 
ATOM   2470 O  OD1 . ASN B 1 87  ? 23.871  32.869  -26.137 1.00 30.97 ?  4562 ASN B OD1 1 
ATOM   2471 N  ND2 . ASN B 1 87  ? 25.853  31.991  -26.738 1.00 33.40 ?  4562 ASN B ND2 1 
ATOM   2472 N  N   . LEU B 1 88  ? 21.994  31.936  -23.831 1.00 30.93 ?  4563 LEU B N   1 
ATOM   2473 C  CA  . LEU B 1 88  ? 20.746  32.589  -23.445 1.00 32.74 ?  4563 LEU B CA  1 
ATOM   2474 C  C   . LEU B 1 88  ? 20.205  33.491  -24.543 1.00 36.91 ?  4563 LEU B C   1 
ATOM   2475 O  O   . LEU B 1 88  ? 18.996  33.748  -24.592 1.00 39.28 ?  4563 LEU B O   1 
ATOM   2476 C  CB  . LEU B 1 88  ? 20.956  33.409  -22.173 1.00 34.28 ?  4563 LEU B CB  1 
ATOM   2477 C  CG  . LEU B 1 88  ? 20.154  33.035  -20.929 1.00 34.59 ?  4563 LEU B CG  1 
ATOM   2478 C  CD1 . LEU B 1 88  ? 20.232  34.168  -19.912 1.00 30.07 ?  4563 LEU B CD1 1 
ATOM   2479 C  CD2 . LEU B 1 88  ? 18.707  32.657  -21.242 1.00 28.76 ?  4563 LEU B CD2 1 
ATOM   2480 N  N   . LYS B 1 89  ? 21.072  33.991  -25.419 1.00 36.04 ?  4564 LYS B N   1 
ATOM   2481 C  CA  . LYS B 1 89  ? 20.635  34.925  -26.447 1.00 38.71 ?  4564 LYS B CA  1 
ATOM   2482 C  C   . LYS B 1 89  ? 20.022  34.238  -27.660 1.00 39.92 ?  4564 LYS B C   1 
ATOM   2483 O  O   . LYS B 1 89  ? 19.501  34.930  -28.541 1.00 42.37 ?  4564 LYS B O   1 
ATOM   2484 C  CB  . LYS B 1 89  ? 21.792  35.847  -26.846 1.00 39.55 ?  4564 LYS B CB  1 
ATOM   2485 C  CG  . LYS B 1 89  ? 22.258  36.745  -25.697 1.00 40.48 ?  4564 LYS B CG  1 
ATOM   2486 C  CD  . LYS B 1 89  ? 23.517  37.518  -26.049 1.00 38.86 ?  4564 LYS B CD  1 
ATOM   2487 C  CE  . LYS B 1 89  ? 23.986  38.360  -24.873 1.00 39.15 ?  4564 LYS B CE  1 
ATOM   2488 N  NZ  . LYS B 1 89  ? 25.155  39.200  -25.248 1.00 38.77 ?  4564 LYS B NZ  1 
ATOM   2489 N  N   . ASP B 1 90  ? 20.060  32.909  -27.723 1.00 37.34 ?  4565 ASP B N   1 
ATOM   2490 C  CA  . ASP B 1 90  ? 19.372  32.187  -28.784 1.00 39.38 ?  4565 ASP B CA  1 
ATOM   2491 C  C   . ASP B 1 90  ? 17.865  32.217  -28.554 1.00 39.18 ?  4565 ASP B C   1 
ATOM   2492 O  O   . ASP B 1 90  ? 17.387  32.245  -27.417 1.00 38.79 ?  4565 ASP B O   1 
ATOM   2493 C  CB  . ASP B 1 90  ? 19.868  30.742  -28.843 1.00 37.50 ?  4565 ASP B CB  1 
ATOM   2494 C  CG  . ASP B 1 90  ? 21.225  30.624  -29.508 1.00 43.90 ?  4565 ASP B CG  1 
ATOM   2495 O  OD1 . ASP B 1 90  ? 21.452  31.337  -30.512 1.00 47.09 ?  4565 ASP B OD1 1 
ATOM   2496 O  OD2 . ASP B 1 90  ? 22.061  29.824  -29.034 1.00 42.43 -1 4565 ASP B OD2 1 
ATOM   2497 N  N   . SER B 1 91  ? 17.108  32.214  -29.657 1.00 40.72 ?  4566 SER B N   1 
ATOM   2498 C  CA  . SER B 1 91  ? 15.660  32.392  -29.563 1.00 39.55 ?  4566 SER B CA  1 
ATOM   2499 C  C   . SER B 1 91  ? 14.955  31.191  -28.941 1.00 40.05 ?  4566 SER B C   1 
ATOM   2500 O  O   . SER B 1 91  ? 13.825  31.335  -28.459 1.00 40.45 ?  4566 SER B O   1 
ATOM   2501 C  CB  . SER B 1 91  ? 15.065  32.712  -30.939 1.00 42.60 ?  4566 SER B CB  1 
ATOM   2502 O  OG  . SER B 1 91  ? 15.163  31.600  -31.812 1.00 44.71 ?  4566 SER B OG  1 
ATOM   2503 N  N   . ASN B 1 92  ? 15.587  30.018  -28.943 1.00 39.54 ?  4567 ASN B N   1 
ATOM   2504 C  CA  . ASN B 1 92  ? 15.023  28.817  -28.343 1.00 38.27 ?  4567 ASN B CA  1 
ATOM   2505 C  C   . ASN B 1 92  ? 15.531  28.567  -26.925 1.00 38.29 ?  4567 ASN B C   1 
ATOM   2506 O  O   . ASN B 1 92  ? 15.217  27.523  -26.343 1.00 36.99 ?  4567 ASN B O   1 
ATOM   2507 C  CB  . ASN B 1 92  ? 15.314  27.600  -29.225 1.00 38.48 ?  4567 ASN B CB  1 
ATOM   2508 C  CG  . ASN B 1 92  ? 16.795  27.438  -29.530 1.00 42.94 ?  4567 ASN B CG  1 
ATOM   2509 O  OD1 . ASN B 1 92  ? 17.640  28.126  -28.955 1.00 44.63 ?  4567 ASN B OD1 1 
ATOM   2510 N  ND2 . ASN B 1 92  ? 17.117  26.527  -30.441 1.00 46.72 ?  4567 ASN B ND2 1 
ATOM   2511 N  N   . ALA B 1 93  ? 16.303  29.501  -26.358 1.00 37.41 ?  4568 ALA B N   1 
ATOM   2512 C  CA  . ALA B 1 93  ? 16.934  29.266  -25.059 1.00 34.52 ?  4568 ALA B CA  1 
ATOM   2513 C  C   . ALA B 1 93  ? 15.899  28.980  -23.975 1.00 34.59 ?  4568 ALA B C   1 
ATOM   2514 O  O   . ALA B 1 93  ? 16.011  27.991  -23.239 1.00 31.55 ?  4568 ALA B O   1 
ATOM   2515 C  CB  . ALA B 1 93  ? 17.816  30.456  -24.675 1.00 34.79 ?  4568 ALA B CB  1 
ATOM   2516 N  N   . LEU B 1 94  ? 14.879  29.834  -23.864 1.00 32.83 ?  4569 LEU B N   1 
ATOM   2517 C  CA  . LEU B 1 94  ? 13.898  29.671  -22.795 1.00 31.70 ?  4569 LEU B CA  1 
ATOM   2518 C  C   . LEU B 1 94  ? 13.063  28.413  -22.987 1.00 31.92 ?  4569 LEU B C   1 
ATOM   2519 O  O   . LEU B 1 94  ? 12.710  27.742  -22.010 1.00 31.26 ?  4569 LEU B O   1 
ATOM   2520 C  CB  . LEU B 1 94  ? 13.012  30.912  -22.687 1.00 30.96 ?  4569 LEU B CB  1 
ATOM   2521 C  CG  . LEU B 1 94  ? 13.758  32.212  -22.376 1.00 34.02 ?  4569 LEU B CG  1 
ATOM   2522 C  CD1 . LEU B 1 94  ? 12.790  33.382  -22.227 1.00 35.01 ?  4569 LEU B CD1 1 
ATOM   2523 C  CD2 . LEU B 1 94  ? 14.600  32.051  -21.117 1.00 31.84 ?  4569 LEU B CD2 1 
ATOM   2524 N  N   . SER B 1 95  ? 12.741  28.068  -24.236 1.00 34.65 ?  4570 SER B N   1 
ATOM   2525 C  CA  . SER B 1 95  ? 11.933  26.876  -24.476 1.00 32.46 ?  4570 SER B CA  1 
ATOM   2526 C  C   . SER B 1 95  ? 12.717  25.605  -24.169 1.00 31.54 ?  4570 SER B C   1 
ATOM   2527 O  O   . SER B 1 95  ? 12.167  24.652  -23.608 1.00 33.33 ?  4570 SER B O   1 
ATOM   2528 C  CB  . SER B 1 95  ? 11.389  26.873  -25.907 1.00 32.33 ?  4570 SER B CB  1 
ATOM   2529 O  OG  . SER B 1 95  ? 12.419  27.084  -26.854 1.00 36.86 ?  4570 SER B OG  1 
ATOM   2530 N  N   . GLN B 1 96  ? 14.007  25.580  -24.510 1.00 34.54 ?  4571 GLN B N   1 
ATOM   2531 C  CA  . GLN B 1 96  ? 14.826  24.418  -24.184 1.00 33.48 ?  4571 GLN B CA  1 
ATOM   2532 C  C   . GLN B 1 96  ? 14.989  24.258  -22.679 1.00 32.93 ?  4571 GLN B C   1 
ATOM   2533 O  O   . GLN B 1 96  ? 14.939  23.137  -22.161 1.00 31.61 ?  4571 GLN B O   1 
ATOM   2534 C  CB  . GLN B 1 96  ? 16.191  24.529  -24.851 1.00 35.30 ?  4571 GLN B CB  1 
ATOM   2535 C  CG  . GLN B 1 96  ? 16.158  24.336  -26.343 1.00 33.57 ?  4571 GLN B CG  1 
ATOM   2536 C  CD  . GLN B 1 96  ? 17.496  23.889  -26.873 1.00 41.67 ?  4571 GLN B CD  1 
ATOM   2537 O  OE1 . GLN B 1 96  ? 18.422  24.690  -27.009 1.00 41.74 ?  4571 GLN B OE1 1 
ATOM   2538 N  NE2 . GLN B 1 96  ? 17.616  22.597  -27.158 1.00 46.04 ?  4571 GLN B NE2 1 
ATOM   2539 N  N   . LEU B 1 97  ? 15.207  25.364  -21.964 1.00 30.74 ?  4572 LEU B N   1 
ATOM   2540 C  CA  . LEU B 1 97  ? 15.222  25.299  -20.507 1.00 32.00 ?  4572 LEU B CA  1 
ATOM   2541 C  C   . LEU B 1 97  ? 13.875  24.837  -19.971 1.00 30.66 ?  4572 LEU B C   1 
ATOM   2542 O  O   . LEU B 1 97  ? 13.812  24.056  -19.015 1.00 30.59 ?  4572 LEU B O   1 
ATOM   2543 C  CB  . LEU B 1 97  ? 15.592  26.663  -19.918 1.00 27.79 ?  4572 LEU B CB  1 
ATOM   2544 C  CG  . LEU B 1 97  ? 17.046  27.106  -20.072 1.00 29.79 ?  4572 LEU B CG  1 
ATOM   2545 C  CD1 . LEU B 1 97  ? 17.184  28.566  -19.689 1.00 28.07 ?  4572 LEU B CD1 1 
ATOM   2546 C  CD2 . LEU B 1 97  ? 17.952  26.244  -19.209 1.00 26.71 ?  4572 LEU B CD2 1 
ATOM   2547 N  N   . GLN B 1 98  ? 12.784  25.308  -20.579 1.00 30.61 ?  4573 GLN B N   1 
ATOM   2548 C  CA  . GLN B 1 98  ? 11.457  24.918  -20.118 1.00 31.82 ?  4573 GLN B CA  1 
ATOM   2549 C  C   . GLN B 1 98  ? 11.235  23.416  -20.270 1.00 33.68 ?  4573 GLN B C   1 
ATOM   2550 O  O   . GLN B 1 98  ? 10.559  22.796  -19.439 1.00 31.98 ?  4573 GLN B O   1 
ATOM   2551 C  CB  . GLN B 1 98  ? 10.389  25.702  -20.885 1.00 33.62 ?  4573 GLN B CB  1 
ATOM   2552 C  CG  . GLN B 1 98  ? 8.978   25.470  -20.379 1.00 31.99 ?  4573 GLN B CG  1 
ATOM   2553 C  CD  . GLN B 1 98  ? 8.752   26.057  -19.006 1.00 35.92 ?  4573 GLN B CD  1 
ATOM   2554 O  OE1 . GLN B 1 98  ? 8.180   25.416  -18.130 1.00 38.84 ?  4573 GLN B OE1 1 
ATOM   2555 N  NE2 . GLN B 1 98  ? 9.201   27.293  -18.813 1.00 35.35 ?  4573 GLN B NE2 1 
ATOM   2556 N  N   . ALA B 1 99  ? 11.799  22.813  -21.322 1.00 32.65 ?  4574 ALA B N   1 
ATOM   2557 C  CA  . ALA B 1 99  ? 11.663  21.369  -21.498 1.00 33.24 ?  4574 ALA B CA  1 
ATOM   2558 C  C   . ALA B 1 99  ? 12.240  20.620  -20.307 1.00 33.49 ?  4574 ALA B C   1 
ATOM   2559 O  O   . ALA B 1 99  ? 11.641  19.654  -19.821 1.00 35.05 ?  4574 ALA B O   1 
ATOM   2560 C  CB  . ALA B 1 99  ? 12.337  20.923  -22.795 1.00 31.65 ?  4574 ALA B CB  1 
ATOM   2561 N  N   . ILE B 1 100 ? 13.397  21.062  -19.809 1.00 31.48 ?  4575 ILE B N   1 
ATOM   2562 C  CA  . ILE B 1 100 ? 13.986  20.417  -18.640 1.00 30.77 ?  4575 ILE B CA  1 
ATOM   2563 C  C   . ILE B 1 100 ? 13.120  20.642  -17.408 1.00 30.10 ?  4575 ILE B C   1 
ATOM   2564 O  O   . ILE B 1 100 ? 12.894  19.719  -16.618 1.00 29.56 ?  4575 ILE B O   1 
ATOM   2565 C  CB  . ILE B 1 100 ? 15.435  20.890  -18.436 1.00 29.79 ?  4575 ILE B CB  1 
ATOM   2566 C  CG1 . ILE B 1 100 ? 16.257  20.591  -19.691 1.00 29.59 ?  4575 ILE B CG1 1 
ATOM   2567 C  CG2 . ILE B 1 100 ? 16.042  20.252  -17.183 1.00 27.11 ?  4575 ILE B CG2 1 
ATOM   2568 C  CD1 . ILE B 1 100 ? 16.178  19.148  -20.157 1.00 29.97 ?  4575 ILE B CD1 1 
ATOM   2569 N  N   . LEU B 1 101 ? 12.621  21.869  -17.223 1.00 29.10 ?  4576 LEU B N   1 
ATOM   2570 C  CA  . LEU B 1 101 ? 11.737  22.146  -16.095 1.00 32.59 ?  4576 LEU B CA  1 
ATOM   2571 C  C   . LEU B 1 101 ? 10.518  21.230  -16.104 1.00 34.40 ?  4576 LEU B C   1 
ATOM   2572 O  O   . LEU B 1 101 ? 10.119  20.701  -15.060 1.00 32.86 ?  4576 LEU B O   1 
ATOM   2573 C  CB  . LEU B 1 101 ? 11.300  23.614  -16.119 1.00 33.48 ?  4576 LEU B CB  1 
ATOM   2574 C  CG  . LEU B 1 101 ? 12.363  24.669  -15.815 1.00 29.18 ?  4576 LEU B CG  1 
ATOM   2575 C  CD1 . LEU B 1 101 ? 11.768  26.065  -15.932 1.00 31.82 ?  4576 LEU B CD1 1 
ATOM   2576 C  CD2 . LEU B 1 101 ? 12.932  24.452  -14.420 1.00 28.25 ?  4576 LEU B CD2 1 
ATOM   2577 N  N   . ASP B 1 102 ? 9.919   21.016  -17.276 1.00 33.57 ?  4577 ASP B N   1 
ATOM   2578 C  CA  . ASP B 1 102 ? 8.703   20.212  -17.333 1.00 36.22 ?  4577 ASP B CA  1 
ATOM   2579 C  C   . ASP B 1 102 ? 8.972   18.744  -17.021 1.00 37.40 ?  4577 ASP B C   1 
ATOM   2580 O  O   . ASP B 1 102 ? 8.071   18.036  -16.555 1.00 39.16 ?  4577 ASP B O   1 
ATOM   2581 C  CB  . ASP B 1 102 ? 8.021   20.382  -18.691 1.00 37.64 ?  4577 ASP B CB  1 
ATOM   2582 C  CG  . ASP B 1 102 ? 7.490   21.792  -18.901 1.00 39.95 ?  4577 ASP B CG  1 
ATOM   2583 O  OD1 . ASP B 1 102 ? 7.187   22.468  -17.894 1.00 44.69 ?  4577 ASP B OD1 1 
ATOM   2584 O  OD2 . ASP B 1 102 ? 7.371   22.223  -20.069 1.00 42.36 -1 4577 ASP B OD2 1 
ATOM   2585 N  N   . SER B 1 103 ? 10.198  18.274  -17.251 1.00 34.73 ?  4578 SER B N   1 
ATOM   2586 C  CA  . SER B 1 103 ? 10.547  16.890  -16.956 1.00 34.08 ?  4578 SER B CA  1 
ATOM   2587 C  C   . SER B 1 103 ? 10.729  16.625  -15.468 1.00 34.96 ?  4578 SER B C   1 
ATOM   2588 O  O   . SER B 1 103 ? 10.779  15.457  -15.066 1.00 34.91 ?  4578 SER B O   1 
ATOM   2589 C  CB  . SER B 1 103 ? 11.820  16.489  -17.708 1.00 32.70 ?  4578 SER B CB  1 
ATOM   2590 O  OG  . SER B 1 103 ? 12.976  17.055  -17.109 1.00 31.94 ?  4578 SER B OG  1 
ATOM   2591 N  N   . MET B 1 104 ? 10.829  17.664  -14.644 1.00 31.84 ?  4579 MET B N   1 
ATOM   2592 C  CA  . MET B 1 104 ? 11.087  17.475  -13.222 1.00 33.89 ?  4579 MET B CA  1 
ATOM   2593 C  C   . MET B 1 104 ? 9.876   16.848  -12.543 1.00 35.56 ?  4579 MET B C   1 
ATOM   2594 O  O   . MET B 1 104 ? 8.763   17.376  -12.630 1.00 37.75 ?  4579 MET B O   1 
ATOM   2595 C  CB  . MET B 1 104 ? 11.427  18.812  -12.573 1.00 31.67 ?  4579 MET B CB  1 
ATOM   2596 C  CG  . MET B 1 104 ? 12.709  19.425  -13.102 1.00 31.26 ?  4579 MET B CG  1 
ATOM   2597 S  SD  . MET B 1 104 ? 13.037  21.057  -12.411 1.00 33.90 ?  4579 MET B SD  1 
ATOM   2598 C  CE  . MET B 1 104 ? 14.697  21.302  -13.036 1.00 31.46 ?  4579 MET B CE  1 
ATOM   2599 N  N   . ASP B 1 105 ? 10.095  15.719  -11.871 1.00 32.57 ?  4580 ASP B N   1 
ATOM   2600 C  CA  . ASP B 1 105 ? 9.062   15.026  -11.107 1.00 33.02 ?  4580 ASP B CA  1 
ATOM   2601 C  C   . ASP B 1 105 ? 9.486   15.061  -9.647  1.00 32.16 ?  4580 ASP B C   1 
ATOM   2602 O  O   . ASP B 1 105 ? 10.481  14.432  -9.271  1.00 29.18 ?  4580 ASP B O   1 
ATOM   2603 C  CB  . ASP B 1 105 ? 8.909   13.586  -11.598 1.00 34.94 ?  4580 ASP B CB  1 
ATOM   2604 C  CG  . ASP B 1 105 ? 7.943   12.758  -10.749 1.00 37.33 ?  4580 ASP B CG  1 
ATOM   2605 O  OD1 . ASP B 1 105 ? 7.253   13.316  -9.870  1.00 37.67 ?  4580 ASP B OD1 1 
ATOM   2606 O  OD2 . ASP B 1 105 ? 7.878   11.527  -10.963 1.00 41.46 -1 4580 ASP B OD2 1 
ATOM   2607 N  N   . GLY B 1 106 ? 8.742   15.801  -8.829  1.00 33.49 ?  4581 GLY B N   1 
ATOM   2608 C  CA  . GLY B 1 106 ? 9.034   15.883  -7.412  1.00 34.40 ?  4581 GLY B CA  1 
ATOM   2609 C  C   . GLY B 1 106 ? 7.967   15.251  -6.539  1.00 37.00 ?  4581 GLY B C   1 
ATOM   2610 O  O   . GLY B 1 106 ? 7.879   15.549  -5.344  1.00 35.88 ?  4581 GLY B O   1 
ATOM   2611 N  N   . SER B 1 107 ? 7.161   14.366  -7.122  1.00 38.43 ?  4582 SER B N   1 
ATOM   2612 C  CA  . SER B 1 107 ? 6.057   13.759  -6.395  1.00 39.02 ?  4582 SER B CA  1 
ATOM   2613 C  C   . SER B 1 107 ? 6.573   12.843  -5.286  1.00 42.71 ?  4582 SER B C   1 
ATOM   2614 O  O   . SER B 1 107 ? 7.716   12.380  -5.300  1.00 39.08 ?  4582 SER B O   1 
ATOM   2615 C  CB  . SER B 1 107 ? 5.162   12.966  -7.350  1.00 39.32 ?  4582 SER B CB  1 
ATOM   2616 O  OG  . SER B 1 107 ? 5.881   11.912  -7.966  1.00 40.39 ?  4582 SER B OG  1 
ATOM   2617 N  N   . THR B 1 108 ? 5.703   12.583  -4.310  1.00 41.16 ?  4583 THR B N   1 
ATOM   2618 C  CA  . THR B 1 108 ? 6.088   11.724  -3.197  1.00 43.59 ?  4583 THR B CA  1 
ATOM   2619 C  C   . THR B 1 108 ? 6.346   10.297  -3.663  1.00 44.09 ?  4583 THR B C   1 
ATOM   2620 O  O   . THR B 1 108 ? 7.250   9.625   -3.156  1.00 44.60 ?  4583 THR B O   1 
ATOM   2621 C  CB  . THR B 1 108 ? 4.997   11.748  -2.125  1.00 45.53 ?  4583 THR B CB  1 
ATOM   2622 O  OG1 . THR B 1 108 ? 4.640   13.106  -1.836  1.00 46.91 ?  4583 THR B OG1 1 
ATOM   2623 C  CG2 . THR B 1 108 ? 5.497   11.079  -0.853  1.00 42.58 ?  4583 THR B CG2 1 
ATOM   2624 N  N   . ASN B 1 109 ? 5.570   9.823   -4.641  1.00 46.17 ?  4584 ASN B N   1 
ATOM   2625 C  CA  . ASN B 1 109 ? 5.684   8.433   -5.072  1.00 46.97 ?  4584 ASN B CA  1 
ATOM   2626 C  C   . ASN B 1 109 ? 6.895   8.179   -5.965  1.00 45.43 ?  4584 ASN B C   1 
ATOM   2627 O  O   . ASN B 1 109 ? 7.510   7.111   -5.868  1.00 46.15 ?  4584 ASN B O   1 
ATOM   2628 C  CB  . ASN B 1 109 ? 4.397   7.980   -5.766  1.00 46.54 ?  4584 ASN B CB  1 
ATOM   2629 C  CG  . ASN B 1 109 ? 3.426   7.313   -4.809  1.00 52.19 ?  4584 ASN B CG  1 
ATOM   2630 O  OD1 . ASN B 1 109 ? 3.259   7.754   -3.670  1.00 53.07 ?  4584 ASN B OD1 1 
ATOM   2631 N  ND2 . ASN B 1 109 ? 2.801   6.232   -5.260  1.00 51.15 ?  4584 ASN B ND2 1 
ATOM   2632 N  N   . SER B 1 110 ? 7.258   9.127   -6.834  1.00 40.41 ?  4585 SER B N   1 
ATOM   2633 C  CA  . SER B 1 110 ? 8.303   8.887   -7.824  1.00 39.79 ?  4585 SER B CA  1 
ATOM   2634 C  C   . SER B 1 110 ? 9.312   10.030  -7.919  1.00 38.28 ?  4585 SER B C   1 
ATOM   2635 O  O   . SER B 1 110 ? 10.024  10.135  -8.926  1.00 37.18 ?  4585 SER B O   1 
ATOM   2636 C  CB  . SER B 1 110 ? 7.701   8.585   -9.198  1.00 40.27 ?  4585 SER B CB  1 
ATOM   2637 O  OG  . SER B 1 110 ? 6.862   9.639   -9.635  1.00 41.50 ?  4585 SER B OG  1 
ATOM   2638 N  N   . GLY B 1 111 ? 9.398   10.878  -6.892  1.00 35.39 ?  4586 GLY B N   1 
ATOM   2639 C  CA  . GLY B 1 111 ? 10.355  11.973  -6.927  1.00 34.00 ?  4586 GLY B CA  1 
ATOM   2640 C  C   . GLY B 1 111 ? 11.796  11.507  -6.842  1.00 30.07 ?  4586 GLY B C   1 
ATOM   2641 O  O   . GLY B 1 111 ? 12.663  12.024  -7.550  1.00 26.52 ?  4586 GLY B O   1 
ATOM   2642 N  N   . GLY B 1 112 ? 12.074  10.536  -5.984  1.00 30.05 ?  4587 GLY B N   1 
ATOM   2643 C  CA  . GLY B 1 112 ? 13.397  9.945   -5.889  1.00 26.85 ?  4587 GLY B CA  1 
ATOM   2644 C  C   . GLY B 1 112 ? 14.136  10.385  -4.637  1.00 27.90 ?  4587 GLY B C   1 
ATOM   2645 O  O   . GLY B 1 112 ? 13.591  11.049  -3.751  1.00 29.33 ?  4587 GLY B O   1 
ATOM   2646 N  N   . GLY B 1 113 ? 15.408  9.988   -4.575  1.00 25.04 ?  4588 GLY B N   1 
ATOM   2647 C  CA  . GLY B 1 113 ? 16.277  10.311  -3.462  1.00 26.33 ?  4588 GLY B CA  1 
ATOM   2648 C  C   . GLY B 1 113 ? 17.078  11.567  -3.733  1.00 23.79 ?  4588 GLY B C   1 
ATOM   2649 O  O   . GLY B 1 113 ? 16.693  12.414  -4.537  1.00 23.30 ?  4588 GLY B O   1 
ATOM   2650 N  N   . THR B 1 114 ? 18.227  11.678  -3.064  1.00 23.68 ?  4589 THR B N   1 
ATOM   2651 C  CA  . THR B 1 114 ? 19.025  12.905  -3.127  1.00 22.09 ?  4589 THR B CA  1 
ATOM   2652 C  C   . THR B 1 114 ? 20.498  12.541  -3.274  1.00 19.58 ?  4589 THR B C   1 
ATOM   2653 O  O   . THR B 1 114 ? 21.142  12.140  -2.305  1.00 22.08 ?  4589 THR B O   1 
ATOM   2654 C  CB  . THR B 1 114 ? 18.792  13.755  -1.886  1.00 23.57 ?  4589 THR B CB  1 
ATOM   2655 O  OG1 . THR B 1 114 ? 17.384  13.981  -1.728  1.00 25.44 ?  4589 THR B OG1 1 
ATOM   2656 C  CG2 . THR B 1 114 ? 19.504  15.088  -2.027  1.00 24.44 ?  4589 THR B CG2 1 
ATOM   2657 N  N   . ASN B 1 115 ? 21.033  12.693  -4.480  1.00 20.19 ?  4590 ASN B N   1 
ATOM   2658 C  CA  . ASN B 1 115 ? 22.412  12.309  -4.773  1.00 19.77 ?  4590 ASN B CA  1 
ATOM   2659 C  C   . ASN B 1 115 ? 23.214  13.571  -5.093  1.00 19.16 ?  4590 ASN B C   1 
ATOM   2660 O  O   . ASN B 1 115 ? 23.300  13.992  -6.245  1.00 19.17 ?  4590 ASN B O   1 
ATOM   2661 C  CB  . ASN B 1 115 ? 22.429  11.325  -5.945  1.00 16.18 ?  4590 ASN B CB  1 
ATOM   2662 C  CG  . ASN B 1 115 ? 23.743  10.602  -6.077  1.00 18.73 ?  4590 ASN B CG  1 
ATOM   2663 O  OD1 . ASN B 1 115 ? 24.813  11.126  -5.740  1.00 18.30 ?  4590 ASN B OD1 1 
ATOM   2664 N  ND2 . ASN B 1 115 ? 23.674  9.364   -6.575  1.00 19.46 ?  4590 ASN B ND2 1 
ATOM   2665 N  N   . TYR B 1 116 ? 23.815  14.167  -4.058  1.00 19.54 ?  4591 TYR B N   1 
ATOM   2666 C  CA  . TYR B 1 116 ? 24.682  15.325  -4.274  1.00 19.89 ?  4591 TYR B CA  1 
ATOM   2667 C  C   . TYR B 1 116 ? 25.855  14.968  -5.170  1.00 18.55 ?  4591 TYR B C   1 
ATOM   2668 O  O   . TYR B 1 116 ? 26.212  15.724  -6.083  1.00 18.57 ?  4591 TYR B O   1 
ATOM   2669 C  CB  . TYR B 1 116 ? 25.244  15.829  -2.947  1.00 19.18 ?  4591 TYR B CB  1 
ATOM   2670 C  CG  . TYR B 1 116 ? 24.314  16.599  -2.042  1.00 20.00 ?  4591 TYR B CG  1 
ATOM   2671 C  CD1 . TYR B 1 116 ? 22.935  16.585  -2.215  1.00 20.35 ?  4591 TYR B CD1 1 
ATOM   2672 C  CD2 . TYR B 1 116 ? 24.833  17.331  -0.988  1.00 20.36 ?  4591 TYR B CD2 1 
ATOM   2673 C  CE1 . TYR B 1 116 ? 22.101  17.288  -1.346  1.00 23.47 ?  4591 TYR B CE1 1 
ATOM   2674 C  CE2 . TYR B 1 116 ? 24.019  18.032  -0.129  1.00 21.17 ?  4591 TYR B CE2 1 
ATOM   2675 C  CZ  . TYR B 1 116 ? 22.658  18.008  -0.311  1.00 22.45 ?  4591 TYR B CZ  1 
ATOM   2676 O  OH  . TYR B 1 116 ? 21.852  18.704  0.564   1.00 24.02 ?  4591 TYR B OH  1 
ATOM   2677 N  N   . GLU B 1 117 ? 26.497  13.827  -4.898  1.00 17.52 ?  4592 GLU B N   1 
ATOM   2678 C  CA  . GLU B 1 117 ? 27.722  13.499  -5.613  1.00 16.73 ?  4592 GLU B CA  1 
ATOM   2679 C  C   . GLU B 1 117 ? 27.491  13.473  -7.118  1.00 16.13 ?  4592 GLU B C   1 
ATOM   2680 O  O   . GLU B 1 117 ? 28.268  14.046  -7.885  1.00 18.14 ?  4592 GLU B O   1 
ATOM   2681 C  CB  . GLU B 1 117 ? 28.292  12.162  -5.141  1.00 16.30 ?  4592 GLU B CB  1 
ATOM   2682 C  CG  . GLU B 1 117 ? 29.551  11.798  -5.909  1.00 17.04 ?  4592 GLU B CG  1 
ATOM   2683 C  CD  . GLU B 1 117 ? 30.121  10.438  -5.546  1.00 16.48 ?  4592 GLU B CD  1 
ATOM   2684 O  OE1 . GLU B 1 117 ? 29.612  9.785   -4.606  1.00 16.12 ?  4592 GLU B OE1 1 
ATOM   2685 O  OE2 . GLU B 1 117 ? 31.103  10.032  -6.198  1.00 20.29 -1 4592 GLU B OE2 1 
ATOM   2686 N  N   . ASP B 1 118 ? 26.401  12.844  -7.555  1.00 17.71 ?  4593 ASP B N   1 
ATOM   2687 C  CA  . ASP B 1 118 ? 26.192  12.694  -8.987  1.00 18.08 ?  4593 ASP B CA  1 
ATOM   2688 C  C   . ASP B 1 118 ? 25.888  14.035  -9.643  1.00 16.32 ?  4593 ASP B C   1 
ATOM   2689 O  O   . ASP B 1 118 ? 26.379  14.310  -10.742 1.00 17.64 ?  4593 ASP B O   1 
ATOM   2690 C  CB  . ASP B 1 118 ? 25.078  11.689  -9.273  1.00 19.05 ?  4593 ASP B CB  1 
ATOM   2691 C  CG  . ASP B 1 118 ? 24.970  11.349  -10.748 1.00 21.98 ?  4593 ASP B CG  1 
ATOM   2692 O  OD1 . ASP B 1 118 ? 25.868  10.651  -11.273 1.00 20.06 ?  4593 ASP B OD1 1 
ATOM   2693 O  OD2 . ASP B 1 118 ? 23.998  11.799  -11.390 1.00 23.02 -1 4593 ASP B OD2 1 
ATOM   2694 N  N   . VAL B 1 119 ? 25.104  14.894  -8.978  1.00 17.80 ?  4594 VAL B N   1 
ATOM   2695 C  CA  . VAL B 1 119 ? 24.781  16.177  -9.607  1.00 18.88 ?  4594 VAL B CA  1 
ATOM   2696 C  C   . VAL B 1 119 ? 25.996  17.104  -9.624  1.00 18.23 ?  4594 VAL B C   1 
ATOM   2697 O  O   . VAL B 1 119 ? 26.210  17.838  -10.595 1.00 16.92 ?  4594 VAL B O   1 
ATOM   2698 C  CB  . VAL B 1 119 ? 23.519  16.831  -9.009  1.00 20.60 ?  4594 VAL B CB  1 
ATOM   2699 C  CG1 . VAL B 1 119 ? 23.802  17.446  -7.644  1.00 19.99 ?  4594 VAL B CG1 1 
ATOM   2700 C  CG2 . VAL B 1 119 ? 22.988  17.913  -9.959  1.00 19.49 ?  4594 VAL B CG2 1 
ATOM   2701 N  N   . PHE B 1 120 ? 26.820  17.072  -8.569  1.00 18.66 ?  4595 PHE B N   1 
ATOM   2702 C  CA  . PHE B 1 120 ? 28.059  17.847  -8.577  1.00 17.63 ?  4595 PHE B CA  1 
ATOM   2703 C  C   . PHE B 1 120 ? 28.972  17.398  -9.710  1.00 18.53 ?  4595 PHE B C   1 
ATOM   2704 O  O   . PHE B 1 120 ? 29.567  18.225  -10.407 1.00 17.75 ?  4595 PHE B O   1 
ATOM   2705 C  CB  . PHE B 1 120 ? 28.813  17.699  -7.255  1.00 17.15 ?  4595 PHE B CB  1 
ATOM   2706 C  CG  . PHE B 1 120 ? 28.085  18.226  -6.047  1.00 19.18 ?  4595 PHE B CG  1 
ATOM   2707 C  CD1 . PHE B 1 120 ? 27.095  19.191  -6.153  1.00 20.12 ?  4595 PHE B CD1 1 
ATOM   2708 C  CD2 . PHE B 1 120 ? 28.418  17.742  -4.783  1.00 20.01 ?  4595 PHE B CD2 1 
ATOM   2709 C  CE1 . PHE B 1 120 ? 26.448  19.670  -5.014  1.00 20.32 ?  4595 PHE B CE1 1 
ATOM   2710 C  CE2 . PHE B 1 120 ? 27.785  18.210  -3.645  1.00 17.97 ?  4595 PHE B CE2 1 
ATOM   2711 C  CZ  . PHE B 1 120 ? 26.786  19.167  -3.753  1.00 20.50 ?  4595 PHE B CZ  1 
ATOM   2712 N  N   . LYS B 1 121 ? 29.100  16.080  -9.915  1.00 17.76 ?  4596 LYS B N   1 
ATOM   2713 C  CA  . LYS B 1 121 ? 29.977  15.588  -10.975 1.00 18.15 ?  4596 LYS B CA  1 
ATOM   2714 C  C   . LYS B 1 121 ? 29.409  15.899  -12.355 1.00 17.57 ?  4596 LYS B C   1 
ATOM   2715 O  O   . LYS B 1 121 ? 30.160  16.263  -13.271 1.00 18.52 ?  4596 LYS B O   1 
ATOM   2716 C  CB  . LYS B 1 121 ? 30.214  14.083  -10.815 1.00 17.63 ?  4596 LYS B CB  1 
ATOM   2717 C  CG  . LYS B 1 121 ? 31.230  13.730  -9.722  1.00 18.20 ?  4596 LYS B CG  1 
ATOM   2718 C  CD  . LYS B 1 121 ? 31.328  12.218  -9.492  1.00 18.90 ?  4596 LYS B CD  1 
ATOM   2719 C  CE  . LYS B 1 121 ? 32.514  11.880  -8.598  1.00 20.01 ?  4596 LYS B CE  1 
ATOM   2720 N  NZ  . LYS B 1 121 ? 32.651  10.391  -8.393  1.00 22.24 ?  4596 LYS B NZ  1 
ATOM   2721 N  N   . THR B 1 122 ? 28.086  15.774  -12.513 1.00 18.54 ?  4597 THR B N   1 
ATOM   2722 C  CA  . THR B 1 122 ? 27.446  16.137  -13.771 1.00 18.66 ?  4597 THR B CA  1 
ATOM   2723 C  C   . THR B 1 122 ? 27.697  17.599  -14.099 1.00 18.92 ?  4597 THR B C   1 
ATOM   2724 O  O   . THR B 1 122 ? 28.042  17.947  -15.236 1.00 18.36 ?  4597 THR B O   1 
ATOM   2725 C  CB  . THR B 1 122 ? 25.947  15.842  -13.685 1.00 20.56 ?  4597 THR B CB  1 
ATOM   2726 O  OG1 . THR B 1 122 ? 25.749  14.420  -13.603 1.00 20.90 ?  4597 THR B OG1 1 
ATOM   2727 C  CG2 . THR B 1 122 ? 25.206  16.367  -14.909 1.00 21.70 ?  4597 THR B CG2 1 
ATOM   2728 N  N   . THR B 1 123 ? 27.578  18.466  -13.096 1.00 18.45 ?  4598 THR B N   1 
ATOM   2729 C  CA  . THR B 1 123 ? 27.748  19.894  -13.343 1.00 17.67 ?  4598 THR B CA  1 
ATOM   2730 C  C   . THR B 1 123 ? 29.216  20.250  -13.542 1.00 19.99 ?  4598 THR B C   1 
ATOM   2731 O  O   . THR B 1 123 ? 29.549  21.084  -14.390 1.00 19.91 ?  4598 THR B O   1 
ATOM   2732 C  CB  . THR B 1 123 ? 27.121  20.662  -12.190 1.00 17.22 ?  4598 THR B CB  1 
ATOM   2733 O  OG1 . THR B 1 123 ? 25.748  20.259  -12.059 1.00 18.53 ?  4598 THR B OG1 1 
ATOM   2734 C  CG2 . THR B 1 123 ? 27.189  22.182  -12.435 1.00 18.49 ?  4598 THR B CG2 1 
ATOM   2735 N  N   . ALA B 1 124 ? 30.116  19.614  -12.794 1.00 18.28 ?  4599 ALA B N   1 
ATOM   2736 C  CA  . ALA B 1 124 ? 31.538  19.796  -13.054 1.00 19.74 ?  4599 ALA B CA  1 
ATOM   2737 C  C   . ALA B 1 124 ? 31.901  19.379  -14.476 1.00 22.98 ?  4599 ALA B C   1 
ATOM   2738 O  O   . ALA B 1 124 ? 32.760  20.002  -15.110 1.00 21.20 ?  4599 ALA B O   1 
ATOM   2739 C  CB  . ALA B 1 124 ? 32.379  19.037  -12.027 1.00 21.00 ?  4599 ALA B CB  1 
ATOM   2740 N  N   . ASN B 1 125 ? 31.255  18.329  -14.999 1.00 20.33 ?  4600 ASN B N   1 
ATOM   2741 C  CA  . ASN B 1 125 ? 31.485  17.949  -16.391 1.00 20.58 ?  4600 ASN B CA  1 
ATOM   2742 C  C   . ASN B 1 125 ? 31.113  19.080  -17.337 1.00 21.48 ?  4600 ASN B C   1 
ATOM   2743 O  O   . ASN B 1 125 ? 31.822  19.329  -18.319 1.00 21.63 ?  4600 ASN B O   1 
ATOM   2744 C  CB  . ASN B 1 125 ? 30.693  16.691  -16.751 1.00 21.70 ?  4600 ASN B CB  1 
ATOM   2745 C  CG  . ASN B 1 125 ? 31.534  15.434  -16.666 1.00 23.49 ?  4600 ASN B CG  1 
ATOM   2746 O  OD1 . ASN B 1 125 ? 32.460  15.342  -15.851 1.00 22.71 ?  4600 ASN B OD1 1 
ATOM   2747 N  ND2 . ASN B 1 125 ? 31.226  14.459  -17.518 1.00 22.47 ?  4600 ASN B ND2 1 
ATOM   2748 N  N   . TRP B 1 126 ? 30.001  19.769  -17.060 1.00 18.81 ?  4601 TRP B N   1 
ATOM   2749 C  CA  . TRP B 1 126 ? 29.612  20.889  -17.910 1.00 22.41 ?  4601 TRP B CA  1 
ATOM   2750 C  C   . TRP B 1 126 ? 30.678  21.974  -17.910 1.00 24.10 ?  4601 TRP B C   1 
ATOM   2751 O  O   . TRP B 1 126 ? 31.012  22.524  -18.965 1.00 23.47 ?  4601 TRP B O   1 
ATOM   2752 C  CB  . TRP B 1 126 ? 28.274  21.473  -17.472 1.00 19.88 ?  4601 TRP B CB  1 
ATOM   2753 C  CG  . TRP B 1 126 ? 27.823  22.578  -18.398 1.00 20.50 ?  4601 TRP B CG  1 
ATOM   2754 C  CD1 . TRP B 1 126 ? 27.466  22.442  -19.708 1.00 21.93 ?  4601 TRP B CD1 1 
ATOM   2755 C  CD2 . TRP B 1 126 ? 27.681  23.973  -18.085 1.00 22.00 ?  4601 TRP B CD2 1 
ATOM   2756 N  NE1 . TRP B 1 126 ? 27.111  23.667  -20.233 1.00 22.28 ?  4601 TRP B NE1 1 
ATOM   2757 C  CE2 . TRP B 1 126 ? 27.229  24.619  -19.255 1.00 24.45 ?  4601 TRP B CE2 1 
ATOM   2758 C  CE3 . TRP B 1 126 ? 27.884  24.737  -16.929 1.00 23.58 ?  4601 TRP B CE3 1 
ATOM   2759 C  CZ2 . TRP B 1 126 ? 26.981  25.994  -19.305 1.00 23.37 ?  4601 TRP B CZ2 1 
ATOM   2760 C  CZ3 . TRP B 1 126 ? 27.635  26.111  -16.982 1.00 22.93 ?  4601 TRP B CZ3 1 
ATOM   2761 C  CH2 . TRP B 1 126 ? 27.189  26.720  -18.164 1.00 23.93 ?  4601 TRP B CH2 1 
ATOM   2762 N  N   . PHE B 1 127 ? 31.233  22.291  -16.740 1.00 22.53 ?  4602 PHE B N   1 
ATOM   2763 C  CA  . PHE B 1 127 ? 32.297  23.287  -16.695 1.00 22.58 ?  4602 PHE B CA  1 
ATOM   2764 C  C   . PHE B 1 127 ? 33.579  22.824  -17.382 1.00 26.78 ?  4602 PHE B C   1 
ATOM   2765 O  O   . PHE B 1 127 ? 34.449  23.654  -17.668 1.00 26.41 ?  4602 PHE B O   1 
ATOM   2766 C  CB  . PHE B 1 127 ? 32.521  23.759  -15.254 1.00 22.40 ?  4602 PHE B CB  1 
ATOM   2767 C  CG  . PHE B 1 127 ? 31.435  24.675  -14.750 1.00 22.08 ?  4602 PHE B CG  1 
ATOM   2768 C  CD1 . PHE B 1 127 ? 31.438  26.028  -15.093 1.00 22.25 ?  4602 PHE B CD1 1 
ATOM   2769 C  CD2 . PHE B 1 127 ? 30.405  24.201  -13.956 1.00 21.10 ?  4602 PHE B CD2 1 
ATOM   2770 C  CE1 . PHE B 1 127 ? 30.439  26.881  -14.649 1.00 21.73 ?  4602 PHE B CE1 1 
ATOM   2771 C  CE2 . PHE B 1 127 ? 29.398  25.050  -13.505 1.00 22.12 ?  4602 PHE B CE2 1 
ATOM   2772 C  CZ  . PHE B 1 127 ? 29.419  26.401  -13.858 1.00 22.29 ?  4602 PHE B CZ  1 
ATOM   2773 N  N   . ASN B 1 128 ? 33.703  21.535  -17.687 1.00 24.61 ?  4603 ASN B N   1 
ATOM   2774 C  CA  . ASN B 1 128 ? 34.795  21.029  -18.509 1.00 26.91 ?  4603 ASN B CA  1 
ATOM   2775 C  C   . ASN B 1 128 ? 34.481  21.026  -19.999 1.00 25.93 ?  4603 ASN B C   1 
ATOM   2776 O  O   . ASN B 1 128 ? 35.370  20.715  -20.797 1.00 30.00 ?  4603 ASN B O   1 
ATOM   2777 C  CB  . ASN B 1 128 ? 35.141  19.592  -18.097 1.00 27.72 ?  4603 ASN B CB  1 
ATOM   2778 C  CG  . ASN B 1 128 ? 36.048  19.539  -16.899 1.00 29.81 ?  4603 ASN B CG  1 
ATOM   2779 O  OD1 . ASN B 1 128 ? 37.273  19.597  -17.032 1.00 33.21 ?  4603 ASN B OD1 1 
ATOM   2780 N  ND2 . ASN B 1 128 ? 35.458  19.424  -15.712 1.00 30.27 ?  4603 ASN B ND2 1 
ATOM   2781 N  N   . SER B 1 129 ? 33.250  21.334  -20.392 1.00 23.98 ?  4604 SER B N   1 
ATOM   2782 C  CA  . SER B 1 129 ? 32.858  21.184  -21.783 1.00 25.26 ?  4604 SER B CA  1 
ATOM   2783 C  C   . SER B 1 129 ? 33.502  22.269  -22.640 1.00 32.29 ?  4604 SER B C   1 
ATOM   2784 O  O   . SER B 1 129 ? 34.020  23.274  -22.144 1.00 29.86 ?  4604 SER B O   1 
ATOM   2785 C  CB  . SER B 1 129 ? 31.341  21.257  -21.925 1.00 26.82 ?  4604 SER B CB  1 
ATOM   2786 O  OG  . SER B 1 129 ? 30.870  22.560  -21.625 1.00 28.94 ?  4604 SER B OG  1 
ATOM   2787 N  N   . SER B 1 130 ? 33.466  22.040  -23.956 1.00 32.84 ?  4605 SER B N   1 
ATOM   2788 C  CA  . SER B 1 130 ? 33.996  23.015  -24.903 1.00 33.15 ?  4605 SER B CA  1 
ATOM   2789 C  C   . SER B 1 130 ? 33.210  24.318  -24.865 1.00 35.64 ?  4605 SER B C   1 
ATOM   2790 O  O   . SER B 1 130 ? 33.785  25.392  -25.077 1.00 36.35 ?  4605 SER B O   1 
ATOM   2791 C  CB  . SER B 1 130 ? 33.961  22.430  -26.314 1.00 36.72 ?  4605 SER B CB  1 
ATOM   2792 O  OG  . SER B 1 130 ? 32.630  22.102  -26.676 1.00 40.26 ?  4605 SER B OG  1 
ATOM   2793 N  N   . THR B 1 131 ? 31.900  24.240  -24.610 1.00 35.21 ?  4606 THR B N   1 
ATOM   2794 C  CA  . THR B 1 131 ? 31.076  25.442  -24.495 1.00 34.51 ?  4606 THR B CA  1 
ATOM   2795 C  C   . THR B 1 131 ? 31.594  26.357  -23.392 1.00 35.38 ?  4606 THR B C   1 
ATOM   2796 O  O   . THR B 1 131 ? 31.804  27.558  -23.605 1.00 32.28 ?  4606 THR B O   1 
ATOM   2797 C  CB  . THR B 1 131 ? 29.631  25.040  -24.190 1.00 34.99 ?  4606 THR B CB  1 
ATOM   2798 O  OG1 . THR B 1 131 ? 29.119  24.225  -25.252 1.00 41.05 ?  4606 THR B OG1 1 
ATOM   2799 C  CG2 . THR B 1 131 ? 28.752  26.267  -24.030 1.00 36.08 ?  4606 THR B CG2 1 
ATOM   2800 N  N   . VAL B 1 132 ? 31.805  25.800  -22.201 1.00 29.49 ?  4607 VAL B N   1 
ATOM   2801 C  CA  . VAL B 1 132 ? 32.219  26.609  -21.061 1.00 29.41 ?  4607 VAL B CA  1 
ATOM   2802 C  C   . VAL B 1 132 ? 33.680  27.013  -21.187 1.00 31.69 ?  4607 VAL B C   1 
ATOM   2803 O  O   . VAL B 1 132 ? 34.043  28.166  -20.925 1.00 30.59 ?  4607 VAL B O   1 
ATOM   2804 C  CB  . VAL B 1 132 ? 31.937  25.866  -19.742 1.00 27.56 ?  4607 VAL B CB  1 
ATOM   2805 C  CG1 . VAL B 1 132 ? 32.601  26.579  -18.578 1.00 28.48 ?  4607 VAL B CG1 1 
ATOM   2806 C  CG2 . VAL B 1 132 ? 30.446  25.750  -19.517 1.00 27.59 ?  4607 VAL B CG2 1 
ATOM   2807 N  N   . GLN B 1 133 ? 34.542  26.077  -21.588 1.00 31.99 ?  4608 GLN B N   1 
ATOM   2808 C  CA  . GLN B 1 133 ? 35.961  26.400  -21.686 1.00 35.31 ?  4608 GLN B CA  1 
ATOM   2809 C  C   . GLN B 1 133 ? 36.234  27.433  -22.774 1.00 34.52 ?  4608 GLN B C   1 
ATOM   2810 O  O   . GLN B 1 133 ? 37.147  28.252  -22.629 1.00 38.85 ?  4608 GLN B O   1 
ATOM   2811 C  CB  . GLN B 1 133 ? 36.787  25.130  -21.888 1.00 36.61 ?  4608 GLN B CB  1 
ATOM   2812 C  CG  . GLN B 1 133 ? 36.816  24.227  -20.661 1.00 38.27 ?  4608 GLN B CG  1 
ATOM   2813 C  CD  . GLN B 1 133 ? 37.484  24.888  -19.465 1.00 41.50 ?  4608 GLN B CD  1 
ATOM   2814 O  OE1 . GLN B 1 133 ? 38.483  25.593  -19.609 1.00 48.60 ?  4608 GLN B OE1 1 
ATOM   2815 N  NE2 . GLN B 1 133 ? 36.929  24.668  -18.277 1.00 38.70 ?  4608 GLN B NE2 1 
ATOM   2816 N  N   . GLY B 1 134 ? 35.449  27.425  -23.852 1.00 33.02 ?  4609 GLY B N   1 
ATOM   2817 C  CA  . GLY B 1 134 ? 35.599  28.435  -24.886 1.00 35.26 ?  4609 GLY B CA  1 
ATOM   2818 C  C   . GLY B 1 134 ? 35.110  29.810  -24.480 1.00 36.88 ?  4609 GLY B C   1 
ATOM   2819 O  O   . GLY B 1 134 ? 35.529  30.808  -25.077 1.00 38.11 ?  4609 GLY B O   1 
ATOM   2820 N  N   . ASN B 1 135 ? 34.232  29.885  -23.479 1.00 32.51 ?  4610 ASN B N   1 
ATOM   2821 C  CA  . ASN B 1 135 ? 33.700  31.157  -22.985 1.00 33.75 ?  4610 ASN B CA  1 
ATOM   2822 C  C   . ASN B 1 135 ? 34.640  31.679  -21.898 1.00 35.90 ?  4610 ASN B C   1 
ATOM   2823 O  O   . ASN B 1 135 ? 34.406  31.531  -20.695 1.00 34.83 ?  4610 ASN B O   1 
ATOM   2824 C  CB  . ASN B 1 135 ? 32.280  30.958  -22.470 1.00 28.83 ?  4610 ASN B CB  1 
ATOM   2825 C  CG  . ASN B 1 135 ? 31.543  32.258  -22.273 1.00 28.89 ?  4610 ASN B CG  1 
ATOM   2826 O  OD1 . ASN B 1 135 ? 31.861  33.262  -22.908 1.00 28.81 ?  4610 ASN B OD1 1 
ATOM   2827 N  ND2 . ASN B 1 135 ? 30.540  32.247  -21.402 1.00 24.40 ?  4610 ASN B ND2 1 
ATOM   2828 N  N   . THR B 1 136 ? 35.720  32.321  -22.340 1.00 38.57 ?  4611 THR B N   1 
ATOM   2829 C  CA  . THR B 1 136 ? 36.837  32.646  -21.463 1.00 37.68 ?  4611 THR B CA  1 
ATOM   2830 C  C   . THR B 1 136 ? 36.560  33.893  -20.626 1.00 37.45 ?  4611 THR B C   1 
ATOM   2831 O  O   . THR B 1 136 ? 35.674  34.698  -20.926 1.00 36.55 ?  4611 THR B O   1 
ATOM   2832 C  CB  . THR B 1 136 ? 38.109  32.863  -22.283 1.00 42.33 ?  4611 THR B CB  1 
ATOM   2833 O  OG1 . THR B 1 136 ? 37.877  33.878  -23.269 1.00 42.18 ?  4611 THR B OG1 1 
ATOM   2834 C  CG2 . THR B 1 136 ? 38.520  31.572  -22.978 1.00 41.24 ?  4611 THR B CG2 1 
ATOM   2835 N  N   . ASN B 1 137 ? 37.359  34.042  -19.564 1.00 37.28 ?  4612 ASN B N   1 
ATOM   2836 C  CA  . ASN B 1 137 ? 37.258  35.164  -18.625 1.00 36.61 ?  4612 ASN B CA  1 
ATOM   2837 C  C   . ASN B 1 137 ? 35.847  35.334  -18.079 1.00 36.77 ?  4612 ASN B C   1 
ATOM   2838 O  O   . ASN B 1 137 ? 35.412  36.443  -17.753 1.00 35.49 ?  4612 ASN B O   1 
ATOM   2839 C  CB  . ASN B 1 137 ? 37.795  36.469  -19.214 1.00 36.64 ?  4612 ASN B CB  1 
ATOM   2840 C  CG  . ASN B 1 137 ? 39.245  36.693  -18.875 1.00 42.93 ?  4612 ASN B CG  1 
ATOM   2841 O  OD1 . ASN B 1 137 ? 40.131  36.431  -19.685 1.00 47.46 ?  4612 ASN B OD1 1 
ATOM   2842 N  ND2 . ASN B 1 137 ? 39.500  37.167  -17.659 1.00 43.51 ?  4612 ASN B ND2 1 
ATOM   2843 N  N   . ALA B 1 138 ? 35.129  34.230  -17.960 1.00 35.28 ?  4613 ALA B N   1 
ATOM   2844 C  CA  . ALA B 1 138 ? 33.744  34.279  -17.539 1.00 30.53 ?  4613 ALA B CA  1 
ATOM   2845 C  C   . ALA B 1 138 ? 33.646  34.233  -16.021 1.00 29.20 ?  4613 ALA B C   1 
ATOM   2846 O  O   . ALA B 1 138 ? 34.578  33.835  -15.319 1.00 34.68 ?  4613 ALA B O   1 
ATOM   2847 C  CB  . ALA B 1 138 ? 32.975  33.105  -18.144 1.00 29.12 ?  4613 ALA B CB  1 
ATOM   2848 N  N   . LYS B 1 139 ? 32.503  34.674  -15.517 1.00 27.85 ?  4614 LYS B N   1 
ATOM   2849 C  CA  . LYS B 1 139 ? 32.127  34.396  -14.142 1.00 30.39 ?  4614 LYS B CA  1 
ATOM   2850 C  C   . LYS B 1 139 ? 31.405  33.055  -14.131 1.00 30.00 ?  4614 LYS B C   1 
ATOM   2851 O  O   . LYS B 1 139 ? 30.357  32.899  -14.770 1.00 26.56 ?  4614 LYS B O   1 
ATOM   2852 C  CB  . LYS B 1 139 ? 31.262  35.518  -13.574 1.00 32.51 ?  4614 LYS B CB  1 
ATOM   2853 C  CG  . LYS B 1 139 ? 31.987  36.863  -13.599 1.00 36.46 ?  4614 LYS B CG  1 
ATOM   2854 C  CD  . LYS B 1 139 ? 31.773  37.676  -12.333 1.00 40.68 ?  4614 LYS B CD  1 
ATOM   2855 C  CE  . LYS B 1 139 ? 30.515  38.523  -12.417 1.00 42.74 ?  4614 LYS B CE  1 
ATOM   2856 N  NZ  . LYS B 1 139 ? 30.616  39.763  -11.589 1.00 42.18 ?  4614 LYS B NZ  1 
ATOM   2857 N  N   . ASN B 1 140 ? 31.993  32.078  -13.450 1.00 26.59 ?  4615 ASN B N   1 
ATOM   2858 C  CA  . ASN B 1 140 ? 31.441  30.732  -13.385 1.00 24.96 ?  4615 ASN B CA  1 
ATOM   2859 C  C   . ASN B 1 140 ? 30.724  30.570  -12.055 1.00 24.60 ?  4615 ASN B C   1 
ATOM   2860 O  O   . ASN B 1 140 ? 31.351  30.630  -10.989 1.00 25.87 ?  4615 ASN B O   1 
ATOM   2861 C  CB  . ASN B 1 140 ? 32.538  29.691  -13.576 1.00 26.13 ?  4615 ASN B CB  1 
ATOM   2862 C  CG  . ASN B 1 140 ? 33.241  29.851  -14.902 1.00 29.27 ?  4615 ASN B CG  1 
ATOM   2863 O  OD1 . ASN B 1 140 ? 32.645  29.647  -15.955 1.00 30.43 ?  4615 ASN B OD1 1 
ATOM   2864 N  ND2 . ASN B 1 140 ? 34.509  30.247  -14.860 1.00 36.38 ?  4615 ASN B ND2 1 
ATOM   2865 N  N   . LEU B 1 141 ? 29.414  30.392  -12.123 1.00 22.85 ?  4616 LEU B N   1 
ATOM   2866 C  CA  . LEU B 1 141 ? 28.543  30.412  -10.963 1.00 25.58 ?  4616 LEU B CA  1 
ATOM   2867 C  C   . LEU B 1 141 ? 27.583  29.235  -11.043 1.00 24.21 ?  4616 LEU B C   1 
ATOM   2868 O  O   . LEU B 1 141 ? 27.125  28.871  -12.128 1.00 24.55 ?  4616 LEU B O   1 
ATOM   2869 C  CB  . LEU B 1 141 ? 27.750  31.726  -10.958 1.00 26.99 ?  4616 LEU B CB  1 
ATOM   2870 C  CG  . LEU B 1 141 ? 26.597  31.923  -9.977  1.00 31.03 ?  4616 LEU B CG  1 
ATOM   2871 C  CD1 . LEU B 1 141 ? 27.110  31.941  -8.539  1.00 32.51 ?  4616 LEU B CD1 1 
ATOM   2872 C  CD2 . LEU B 1 141 ? 25.853  33.212  -10.305 1.00 34.37 ?  4616 LEU B CD2 1 
ATOM   2873 N  N   . THR B 1 142 ? 27.298  28.623  -9.897  1.00 21.32 ?  4617 THR B N   1 
ATOM   2874 C  CA  . THR B 1 142 ? 26.304  27.564  -9.817  1.00 23.47 ?  4617 THR B CA  1 
ATOM   2875 C  C   . THR B 1 142 ? 25.381  27.828  -8.643  1.00 22.05 ?  4617 THR B C   1 
ATOM   2876 O  O   . THR B 1 142 ? 25.843  28.129  -7.538  1.00 23.07 ?  4617 THR B O   1 
ATOM   2877 C  CB  . THR B 1 142 ? 26.965  26.191  -9.655  1.00 22.97 ?  4617 THR B CB  1 
ATOM   2878 O  OG1 . THR B 1 142 ? 27.722  25.886  -10.828 1.00 21.83 ?  4617 THR B OG1 1 
ATOM   2879 C  CG2 . THR B 1 142 ? 25.913  25.108  -9.441  1.00 22.28 ?  4617 THR B CG2 1 
ATOM   2880 N  N   . TYR B 1 143 ? 24.083  27.719  -8.886  1.00 19.86 ?  4618 TYR B N   1 
ATOM   2881 C  CA  . TYR B 1 143 ? 23.084  27.708  -7.835  1.00 20.77 ?  4618 TYR B CA  1 
ATOM   2882 C  C   . TYR B 1 143 ? 22.750  26.264  -7.499  1.00 22.89 ?  4618 TYR B C   1 
ATOM   2883 O  O   . TYR B 1 143 ? 22.445  25.471  -8.398  1.00 23.71 ?  4618 TYR B O   1 
ATOM   2884 C  CB  . TYR B 1 143 ? 21.828  28.446  -8.288  1.00 25.98 ?  4618 TYR B CB  1 
ATOM   2885 C  CG  . TYR B 1 143 ? 22.062  29.929  -8.432  1.00 28.21 ?  4618 TYR B CG  1 
ATOM   2886 C  CD1 . TYR B 1 143 ? 22.005  30.763  -7.327  1.00 30.02 ?  4618 TYR B CD1 1 
ATOM   2887 C  CD2 . TYR B 1 143 ? 22.364  30.494  -9.667  1.00 28.58 ?  4618 TYR B CD2 1 
ATOM   2888 C  CE1 . TYR B 1 143 ? 22.227  32.119  -7.443  1.00 30.39 ?  4618 TYR B CE1 1 
ATOM   2889 C  CE2 . TYR B 1 143 ? 22.586  31.851  -9.794  1.00 31.07 ?  4618 TYR B CE2 1 
ATOM   2890 C  CZ  . TYR B 1 143 ? 22.515  32.657  -8.674  1.00 31.59 ?  4618 TYR B CZ  1 
ATOM   2891 O  OH  . TYR B 1 143 ? 22.738  34.011  -8.790  1.00 34.70 ?  4618 TYR B OH  1 
ATOM   2892 N  N   . PHE B 1 144 ? 22.836  25.927  -6.217  1.00 22.96 ?  4619 PHE B N   1 
ATOM   2893 C  CA  . PHE B 1 144 ? 22.571  24.584  -5.707  1.00 21.05 ?  4619 PHE B CA  1 
ATOM   2894 C  C   . PHE B 1 144 ? 21.314  24.670  -4.853  1.00 24.39 ?  4619 PHE B C   1 
ATOM   2895 O  O   . PHE B 1 144 ? 21.341  25.240  -3.756  1.00 25.03 ?  4619 PHE B O   1 
ATOM   2896 C  CB  . PHE B 1 144 ? 23.765  24.118  -4.882  1.00 20.55 ?  4619 PHE B CB  1 
ATOM   2897 C  CG  . PHE B 1 144 ? 23.598  22.754  -4.268  1.00 22.86 ?  4619 PHE B CG  1 
ATOM   2898 C  CD1 . PHE B 1 144 ? 22.908  21.754  -4.933  1.00 24.05 ?  4619 PHE B CD1 1 
ATOM   2899 C  CD2 . PHE B 1 144 ? 24.144  22.477  -3.023  1.00 21.55 ?  4619 PHE B CD2 1 
ATOM   2900 C  CE1 . PHE B 1 144 ? 22.758  20.496  -4.356  1.00 23.50 ?  4619 PHE B CE1 1 
ATOM   2901 C  CE2 . PHE B 1 144 ? 24.009  21.230  -2.444  1.00 23.59 ?  4619 PHE B CE2 1 
ATOM   2902 C  CZ  . PHE B 1 144 ? 23.312  20.233  -3.116  1.00 20.87 ?  4619 PHE B CZ  1 
ATOM   2903 N  N   . ILE B 1 145 ? 20.216  24.106  -5.351  1.00 23.80 ?  4620 ILE B N   1 
ATOM   2904 C  CA  . ILE B 1 145 ? 18.894  24.273  -4.757  1.00 22.86 ?  4620 ILE B CA  1 
ATOM   2905 C  C   . ILE B 1 145 ? 18.398  22.918  -4.270  1.00 25.65 ?  4620 ILE B C   1 
ATOM   2906 O  O   . ILE B 1 145 ? 18.119  22.026  -5.085  1.00 25.22 ?  4620 ILE B O   1 
ATOM   2907 C  CB  . ILE B 1 145 ? 17.908  24.886  -5.759  1.00 24.72 ?  4620 ILE B CB  1 
ATOM   2908 C  CG1 . ILE B 1 145 ? 18.389  26.281  -6.179  1.00 28.33 ?  4620 ILE B CG1 1 
ATOM   2909 C  CG2 . ILE B 1 145 ? 16.508  24.919  -5.161  1.00 27.28 ?  4620 ILE B CG2 1 
ATOM   2910 C  CD1 . ILE B 1 145 ? 17.836  26.759  -7.506  1.00 28.48 ?  4620 ILE B CD1 1 
ATOM   2911 N  N   . THR B 1 146 ? 18.240  22.772  -2.952  1.00 25.93 ?  4621 THR B N   1 
ATOM   2912 C  CA  . THR B 1 146 ? 17.935  21.472  -2.367  1.00 29.21 ?  4621 THR B CA  1 
ATOM   2913 C  C   . THR B 1 146 ? 17.072  21.640  -1.124  1.00 30.00 ?  4621 THR B C   1 
ATOM   2914 O  O   . THR B 1 146 ? 17.098  22.683  -0.464  1.00 30.50 ?  4621 THR B O   1 
ATOM   2915 C  CB  . THR B 1 146 ? 19.219  20.703  -2.028  1.00 27.63 ?  4621 THR B CB  1 
ATOM   2916 O  OG1 . THR B 1 146 ? 18.882  19.425  -1.481  1.00 27.48 ?  4621 THR B OG1 1 
ATOM   2917 C  CG2 . THR B 1 146 ? 20.064  21.477  -1.021  1.00 28.28 ?  4621 THR B CG2 1 
ATOM   2918 N  N   . ASP B 1 147 ? 16.316  20.587  -0.800  1.00 27.97 ?  4622 ASP B N   1 
ATOM   2919 C  CA  . ASP B 1 147 ? 15.470  20.578  0.392   1.00 31.38 ?  4622 ASP B CA  1 
ATOM   2920 C  C   . ASP B 1 147 ? 15.859  19.506  1.407   1.00 32.04 ?  4622 ASP B C   1 
ATOM   2921 O  O   . ASP B 1 147 ? 15.128  19.295  2.383   1.00 31.62 ?  4622 ASP B O   1 
ATOM   2922 C  CB  . ASP B 1 147 ? 13.981  20.479  0.021   1.00 31.09 ?  4622 ASP B CB  1 
ATOM   2923 C  CG  . ASP B 1 147 ? 13.481  19.040  -0.081  1.00 36.03 ?  4622 ASP B CG  1 
ATOM   2924 O  OD1 . ASP B 1 147 ? 14.270  18.134  -0.433  1.00 32.61 ?  4622 ASP B OD1 1 
ATOM   2925 O  OD2 . ASP B 1 147 ? 12.279  18.813  0.188   1.00 34.78 -1 4622 ASP B OD2 1 
ATOM   2926 N  N   . GLY B 1 148 ? 16.980  18.817  1.212   1.00 29.47 ?  4623 GLY B N   1 
ATOM   2927 C  CA  . GLY B 1 148 ? 17.332  17.741  2.119   1.00 28.60 ?  4623 GLY B CA  1 
ATOM   2928 C  C   . GLY B 1 148 ? 18.790  17.363  2.020   1.00 26.06 ?  4623 GLY B C   1 
ATOM   2929 O  O   . GLY B 1 148 ? 19.489  17.732  1.071   1.00 26.02 ?  4623 GLY B O   1 
ATOM   2930 N  N   . GLN B 1 149 ? 19.247  16.632  3.036   1.00 26.23 ?  4624 GLN B N   1 
ATOM   2931 C  CA  . GLN B 1 149 ? 20.590  16.085  3.045   1.00 25.48 ?  4624 GLN B CA  1 
ATOM   2932 C  C   . GLN B 1 149 ? 20.708  14.989  1.989   1.00 23.16 ?  4624 GLN B C   1 
ATOM   2933 O  O   . GLN B 1 149 ? 19.704  14.407  1.568   1.00 23.04 ?  4624 GLN B O   1 
ATOM   2934 C  CB  . GLN B 1 149 ? 20.886  15.473  4.412   1.00 25.90 ?  4624 GLN B CB  1 
ATOM   2935 C  CG  . GLN B 1 149 ? 21.152  16.482  5.516   1.00 28.90 ?  4624 GLN B CG  1 
ATOM   2936 C  CD  . GLN B 1 149 ? 21.448  15.802  6.836   1.00 35.86 ?  4624 GLN B CD  1 
ATOM   2937 O  OE1 . GLN B 1 149 ? 20.564  15.653  7.678   1.00 42.23 ?  4624 GLN B OE1 1 
ATOM   2938 N  NE2 . GLN B 1 149 ? 22.693  15.370  7.016   1.00 34.25 ?  4624 GLN B NE2 1 
ATOM   2939 N  N   . PRO B 1 150 ? 21.928  14.684  1.550   1.00 22.43 ?  4625 PRO B N   1 
ATOM   2940 C  CA  . PRO B 1 150 ? 22.094  13.610  0.563   1.00 20.12 ?  4625 PRO B CA  1 
ATOM   2941 C  C   . PRO B 1 150 ? 21.787  12.255  1.184   1.00 22.17 ?  4625 PRO B C   1 
ATOM   2942 O  O   . PRO B 1 150 ? 22.134  11.980  2.336   1.00 21.38 ?  4625 PRO B O   1 
ATOM   2943 C  CB  . PRO B 1 150 ? 23.572  13.717  0.177   1.00 19.80 ?  4625 PRO B CB  1 
ATOM   2944 C  CG  . PRO B 1 150 ? 24.217  14.268  1.412   1.00 23.35 ?  4625 PRO B CG  1 
ATOM   2945 C  CD  . PRO B 1 150 ? 23.224  15.264  1.942   1.00 22.17 ?  4625 PRO B CD  1 
ATOM   2946 N  N   . THR B 1 151 ? 21.139  11.399  0.394   1.00 20.83 ?  4626 THR B N   1 
ATOM   2947 C  CA  . THR B 1 151 ? 20.813  10.046  0.824   1.00 22.33 ?  4626 THR B CA  1 
ATOM   2948 C  C   . THR B 1 151 ? 21.307  8.983   -0.141  1.00 22.47 ?  4626 THR B C   1 
ATOM   2949 O  O   . THR B 1 151 ? 21.185  7.788   0.163   1.00 23.42 ?  4626 THR B O   1 
ATOM   2950 C  CB  . THR B 1 151 ? 19.297  9.883   1.005   1.00 23.75 ?  4626 THR B CB  1 
ATOM   2951 O  OG1 . THR B 1 151 ? 18.633  10.199  -0.224  1.00 25.17 ?  4626 THR B OG1 1 
ATOM   2952 C  CG2 . THR B 1 151 ? 18.784  10.806  2.119   1.00 25.83 ?  4626 THR B CG2 1 
ATOM   2953 N  N   . PHE B 1 152 ? 21.850  9.377   -1.286  1.00 19.80 ?  4627 PHE B N   1 
ATOM   2954 C  CA  . PHE B 1 152 ? 22.510  8.473   -2.209  1.00 20.53 ?  4627 PHE B CA  1 
ATOM   2955 C  C   . PHE B 1 152 ? 23.845  9.091   -2.595  1.00 20.73 ?  4627 PHE B C   1 
ATOM   2956 O  O   . PHE B 1 152 ? 24.063  10.299  -2.454  1.00 20.37 ?  4627 PHE B O   1 
ATOM   2957 C  CB  . PHE B 1 152 ? 21.699  8.269   -3.494  1.00 21.02 ?  4627 PHE B CB  1 
ATOM   2958 C  CG  . PHE B 1 152 ? 20.498  7.365   -3.342  1.00 20.44 ?  4627 PHE B CG  1 
ATOM   2959 C  CD1 . PHE B 1 152 ? 20.651  6.008   -3.082  1.00 22.34 ?  4627 PHE B CD1 1 
ATOM   2960 C  CD2 . PHE B 1 152 ? 19.220  7.869   -3.520  1.00 24.09 ?  4627 PHE B CD2 1 
ATOM   2961 C  CE1 . PHE B 1 152 ? 19.541  5.183   -2.974  1.00 23.46 ?  4627 PHE B CE1 1 
ATOM   2962 C  CE2 . PHE B 1 152 ? 18.109  7.054   -3.414  1.00 26.42 ?  4627 PHE B CE2 1 
ATOM   2963 C  CZ  . PHE B 1 152 ? 18.270  5.701   -3.147  1.00 24.53 ?  4627 PHE B CZ  1 
ATOM   2964 N  N   . TYR B 1 153 ? 24.742  8.240   -3.077  1.00 18.58 ?  4628 TYR B N   1 
ATOM   2965 C  CA  . TYR B 1 153 ? 26.021  8.660   -3.636  1.00 16.21 ?  4628 TYR B CA  1 
ATOM   2966 C  C   . TYR B 1 153 ? 26.419  7.623   -4.674  1.00 17.63 ?  4628 TYR B C   1 
ATOM   2967 O  O   . TYR B 1 153 ? 25.604  6.783   -5.056  1.00 19.49 ?  4628 TYR B O   1 
ATOM   2968 C  CB  . TYR B 1 153 ? 27.075  8.893   -2.543  1.00 17.33 ?  4628 TYR B CB  1 
ATOM   2969 C  CG  . TYR B 1 153 ? 27.403  7.692   -1.684  1.00 18.19 ?  4628 TYR B CG  1 
ATOM   2970 C  CD1 . TYR B 1 153 ? 26.558  7.298   -0.654  1.00 21.21 ?  4628 TYR B CD1 1 
ATOM   2971 C  CD2 . TYR B 1 153 ? 28.581  6.982   -1.882  1.00 20.31 ?  4628 TYR B CD2 1 
ATOM   2972 C  CE1 . TYR B 1 153 ? 26.869  6.208   0.144   1.00 21.64 ?  4628 TYR B CE1 1 
ATOM   2973 C  CE2 . TYR B 1 153 ? 28.901  5.883   -1.082  1.00 21.81 ?  4628 TYR B CE2 1 
ATOM   2974 C  CZ  . TYR B 1 153 ? 28.040  5.510   -0.084  1.00 21.57 ?  4628 TYR B CZ  1 
ATOM   2975 O  OH  . TYR B 1 153 ? 28.354  4.426   0.709   1.00 26.89 ?  4628 TYR B OH  1 
ATOM   2976 N  N   . LEU B 1 154 ? 27.657  7.693   -5.151  1.00 17.38 ?  4629 LEU B N   1 
ATOM   2977 C  CA  . LEU B 1 154 ? 28.165  6.725   -6.116  1.00 18.42 ?  4629 LEU B CA  1 
ATOM   2978 C  C   . LEU B 1 154 ? 29.366  5.999   -5.536  1.00 19.70 ?  4629 LEU B C   1 
ATOM   2979 O  O   . LEU B 1 154 ? 30.197  6.599   -4.857  1.00 18.31 ?  4629 LEU B O   1 
ATOM   2980 C  CB  . LEU B 1 154 ? 28.592  7.415   -7.418  1.00 19.24 ?  4629 LEU B CB  1 
ATOM   2981 C  CG  . LEU B 1 154 ? 27.506  8.235   -8.108  1.00 20.89 ?  4629 LEU B CG  1 
ATOM   2982 C  CD1 . LEU B 1 154 ? 28.103  8.979   -9.285  1.00 23.81 ?  4629 LEU B CD1 1 
ATOM   2983 C  CD2 . LEU B 1 154 ? 26.363  7.360   -8.558  1.00 20.57 ?  4629 LEU B CD2 1 
ATOM   2984 N  N   . GLU B 1 155 ? 29.478  4.706   -5.832  1.00 18.58 ?  4630 GLU B N   1 
ATOM   2985 C  CA  . GLU B 1 155 ? 30.664  3.941   -5.469  1.00 19.17 ?  4630 GLU B CA  1 
ATOM   2986 C  C   . GLU B 1 155 ? 31.110  3.106   -6.662  1.00 17.98 ?  4630 GLU B C   1 
ATOM   2987 O  O   . GLU B 1 155 ? 30.503  3.137   -7.740  1.00 17.16 ?  4630 GLU B O   1 
ATOM   2988 C  CB  . GLU B 1 155 ? 30.437  3.063   -4.232  1.00 20.95 ?  4630 GLU B CB  1 
ATOM   2989 C  CG  . GLU B 1 155 ? 29.330  2.069   -4.374  1.00 24.94 ?  4630 GLU B CG  1 
ATOM   2990 C  CD  . GLU B 1 155 ? 29.128  1.246   -3.103  1.00 31.77 ?  4630 GLU B CD  1 
ATOM   2991 O  OE1 . GLU B 1 155 ? 29.670  1.641   -2.045  1.00 35.81 ?  4630 GLU B OE1 1 
ATOM   2992 O  OE2 . GLU B 1 155 ? 28.433  0.208   -3.169  1.00 38.24 -1 4630 GLU B OE2 1 
ATOM   2993 N  N   . ASN B 1 156 ? 32.219  2.393   -6.474  1.00 18.43 ?  4631 ASN B N   1 
ATOM   2994 C  CA  . ASN B 1 156 ? 32.732  1.459   -7.473  1.00 18.18 ?  4631 ASN B CA  1 
ATOM   2995 C  C   . ASN B 1 156 ? 33.099  2.151   -8.776  1.00 18.40 ?  4631 ASN B C   1 
ATOM   2996 O  O   . ASN B 1 156 ? 33.070  1.529   -9.846  1.00 19.49 ?  4631 ASN B O   1 
ATOM   2997 C  CB  . ASN B 1 156 ? 31.754  0.309   -7.727  1.00 18.63 ?  4631 ASN B CB  1 
ATOM   2998 C  CG  . ASN B 1 156 ? 31.576  -0.569  -6.507  1.00 21.14 ?  4631 ASN B CG  1 
ATOM   2999 O  OD1 . ASN B 1 156 ? 32.549  -0.938  -5.855  1.00 25.36 ?  4631 ASN B OD1 1 
ATOM   3000 N  ND2 . ASN B 1 156 ? 30.334  -0.879  -6.173  1.00 22.47 ?  4631 ASN B ND2 1 
ATOM   3001 N  N   . GLU B 1 157 ? 33.456  3.435   -8.701  1.00 17.65 ?  4632 GLU B N   1 
ATOM   3002 C  CA  . GLU B 1 157 ? 33.720  4.200   -9.912  1.00 18.58 ?  4632 GLU B CA  1 
ATOM   3003 C  C   . GLU B 1 157 ? 34.909  3.625   -10.673 1.00 19.65 ?  4632 GLU B C   1 
ATOM   3004 O  O   . GLU B 1 157 ? 35.985  3.402   -10.109 1.00 20.34 ?  4632 GLU B O   1 
ATOM   3005 C  CB  . GLU B 1 157 ? 33.958  5.674   -9.567  1.00 20.96 ?  4632 GLU B CB  1 
ATOM   3006 C  CG  . GLU B 1 157 ? 32.750  6.379   -8.958  1.00 20.25 ?  4632 GLU B CG  1 
ATOM   3007 C  CD  . GLU B 1 157 ? 32.821  6.466   -7.440  1.00 21.23 ?  4632 GLU B CD  1 
ATOM   3008 O  OE1 . GLU B 1 157 ? 33.366  5.531   -6.807  1.00 20.83 ?  4632 GLU B OE1 1 
ATOM   3009 O  OE2 . GLU B 1 157 ? 32.342  7.480   -6.879  1.00 20.19 -1 4632 GLU B OE2 1 
ATOM   3010 N  N   . GLY B 1 158 ? 34.711  3.369   -11.961 1.00 18.82 ?  4633 GLY B N   1 
ATOM   3011 C  CA  . GLY B 1 158 ? 35.783  2.852   -12.791 1.00 20.03 ?  4633 GLY B CA  1 
ATOM   3012 C  C   . GLY B 1 158 ? 35.968  1.361   -12.705 1.00 21.02 ?  4633 GLY B C   1 
ATOM   3013 O  O   . GLY B 1 158 ? 36.864  0.819   -13.374 1.00 21.88 ?  4633 GLY B O   1 
ATOM   3014 N  N   . SER B 1 159 ? 35.156  0.680   -11.909 1.00 19.51 ?  4634 SER B N   1 
ATOM   3015 C  CA  . SER B 1 159 ? 35.260  -0.761  -11.824 1.00 17.80 ?  4634 SER B CA  1 
ATOM   3016 C  C   . SER B 1 159 ? 34.768  -1.394  -13.126 1.00 18.89 ?  4634 SER B C   1 
ATOM   3017 O  O   . SER B 1 159 ? 34.189  -0.737  -14.001 1.00 18.80 ?  4634 SER B O   1 
ATOM   3018 C  CB  . SER B 1 159 ? 34.488  -1.291  -10.617 1.00 18.77 ?  4634 SER B CB  1 
ATOM   3019 O  OG  . SER B 1 159 ? 33.107  -0.984  -10.696 1.00 18.10 ?  4634 SER B OG  1 
ATOM   3020 N  N   . ASP B 1 160 ? 35.013  -2.694  -13.242 1.00 18.64 ?  4635 ASP B N   1 
ATOM   3021 C  CA  . ASP B 1 160 ? 34.786  -3.434  -14.482 1.00 18.79 ?  4635 ASP B CA  1 
ATOM   3022 C  C   . ASP B 1 160 ? 33.896  -4.625  -14.160 1.00 16.04 ?  4635 ASP B C   1 
ATOM   3023 O  O   . ASP B 1 160 ? 34.397  -5.729  -13.914 1.00 17.73 ?  4635 ASP B O   1 
ATOM   3024 C  CB  . ASP B 1 160 ? 36.118  -3.897  -15.067 1.00 18.21 ?  4635 ASP B CB  1 
ATOM   3025 C  CG  . ASP B 1 160 ? 35.967  -4.490  -16.440 1.00 19.24 ?  4635 ASP B CG  1 
ATOM   3026 O  OD1 . ASP B 1 160 ? 34.896  -4.309  -17.054 1.00 17.62 ?  4635 ASP B OD1 1 
ATOM   3027 O  OD2 . ASP B 1 160 ? 36.926  -5.129  -16.910 1.00 21.49 -1 4635 ASP B OD2 1 
ATOM   3028 N  N   . PRO B 1 161 ? 32.572  -4.445  -14.156 1.00 16.41 ?  4636 PRO B N   1 
ATOM   3029 C  CA  . PRO B 1 161 ? 31.677  -5.521  -13.719 1.00 16.66 ?  4636 PRO B CA  1 
ATOM   3030 C  C   . PRO B 1 161 ? 31.570  -6.635  -14.745 1.00 14.65 ?  4636 PRO B C   1 
ATOM   3031 O  O   . PRO B 1 161 ? 31.715  -6.433  -15.952 1.00 15.62 ?  4636 PRO B O   1 
ATOM   3032 C  CB  . PRO B 1 161 ? 30.328  -4.812  -13.545 1.00 16.90 ?  4636 PRO B CB  1 
ATOM   3033 C  CG  . PRO B 1 161 ? 30.397  -3.682  -14.539 1.00 16.08 ?  4636 PRO B CG  1 
ATOM   3034 C  CD  . PRO B 1 161 ? 31.833  -3.211  -14.476 1.00 16.50 ?  4636 PRO B CD  1 
ATOM   3035 N  N   . MET B 1 162 ? 31.297  -7.816  -14.227 1.00 16.09 ?  4637 MET B N   1 
ATOM   3036 C  CA  . MET B 1 162 ? 30.955  -8.960  -15.056 1.00 15.73 ?  4637 MET B CA  1 
ATOM   3037 C  C   . MET B 1 162 ? 29.606  -8.734  -15.728 1.00 17.19 ?  4637 MET B C   1 
ATOM   3038 O  O   . MET B 1 162 ? 28.623  -8.355  -15.078 1.00 19.10 ?  4637 MET B O   1 
ATOM   3039 C  CB  . MET B 1 162 ? 30.858  -10.192 -14.162 1.00 18.16 ?  4637 MET B CB  1 
ATOM   3040 C  CG  . MET B 1 162 ? 30.336  -11.399 -14.893 1.00 21.42 ?  4637 MET B CG  1 
ATOM   3041 S  SD  . MET B 1 162 ? 31.670  -12.205 -15.768 1.00 24.36 ?  4637 MET B SD  1 
ATOM   3042 C  CE  . MET B 1 162 ? 32.444  -13.078 -14.446 1.00 19.78 ?  4637 MET B CE  1 
ATOM   3043 N  N   . ILE B 1 163 ? 29.559  -8.985  -17.032 1.00 13.54 ?  4638 ILE B N   1 
ATOM   3044 C  CA  . ILE B 1 163 ? 28.325  -8.885  -17.799 1.00 14.24 ?  4638 ILE B CA  1 
ATOM   3045 C  C   . ILE B 1 163 ? 27.718  -10.258 -18.063 1.00 14.42 ?  4638 ILE B C   1 
ATOM   3046 O  O   . ILE B 1 163 ? 26.506  -10.439 -17.927 1.00 14.79 ?  4638 ILE B O   1 
ATOM   3047 C  CB  . ILE B 1 163 ? 28.596  -8.125  -19.115 1.00 14.83 ?  4638 ILE B CB  1 
ATOM   3048 C  CG1 . ILE B 1 163 ? 29.115  -6.702  -18.832 1.00 17.29 ?  4638 ILE B CG1 1 
ATOM   3049 C  CG2 . ILE B 1 163 ? 27.348  -8.099  -19.982 1.00 14.92 ?  4638 ILE B CG2 1 
ATOM   3050 C  CD1 . ILE B 1 163 ? 28.171  -5.832  -18.009 1.00 17.04 ?  4638 ILE B CD1 1 
ATOM   3051 N  N   . ARG B 1 164 ? 28.541  -11.224 -18.458 1.00 14.27 ?  4639 ARG B N   1 
ATOM   3052 C  CA  . ARG B 1 164 ? 28.094  -12.593 -18.709 1.00 12.86 ?  4639 ARG B CA  1 
ATOM   3053 C  C   . ARG B 1 164 ? 29.108  -13.561 -18.123 1.00 15.99 ?  4639 ARG B C   1 
ATOM   3054 O  O   . ARG B 1 164 ? 30.258  -13.609 -18.567 1.00 17.59 ?  4639 ARG B O   1 
ATOM   3055 C  CB  . ARG B 1 164 ? 27.890  -12.881 -20.201 1.00 15.03 ?  4639 ARG B CB  1 
ATOM   3056 C  CG  . ARG B 1 164 ? 27.199  -14.228 -20.442 1.00 15.83 ?  4639 ARG B CG  1 
ATOM   3057 C  CD  . ARG B 1 164 ? 27.072  -14.533 -21.909 1.00 18.86 ?  4639 ARG B CD  1 
ATOM   3058 N  NE  . ARG B 1 164 ? 28.389  -14.769 -22.482 1.00 25.08 ?  4639 ARG B NE  1 
ATOM   3059 C  CZ  . ARG B 1 164 ? 28.606  -14.970 -23.771 1.00 31.64 ?  4639 ARG B CZ  1 
ATOM   3060 N  NH1 . ARG B 1 164 ? 27.605  -15.017 -24.635 1.00 30.58 ?  4639 ARG B NH1 1 
ATOM   3061 N  NH2 . ARG B 1 164 ? 29.857  -15.118 -24.202 1.00 33.82 ?  4639 ARG B NH2 1 
ATOM   3062 N  N   . ASP B 1 165 ? 28.680  -14.353 -17.156 1.00 13.96 ?  4640 ASP B N   1 
ATOM   3063 C  CA  . ASP B 1 165 ? 29.537  -15.306 -16.461 1.00 13.73 ?  4640 ASP B CA  1 
ATOM   3064 C  C   . ASP B 1 165 ? 29.170  -16.693 -16.962 1.00 12.74 ?  4640 ASP B C   1 
ATOM   3065 O  O   . ASP B 1 165 ? 28.045  -17.154 -16.743 1.00 14.88 ?  4640 ASP B O   1 
ATOM   3066 C  CB  . ASP B 1 165 ? 29.259  -15.196 -14.965 1.00 13.71 ?  4640 ASP B CB  1 
ATOM   3067 C  CG  . ASP B 1 165 ? 30.146  -16.072 -14.136 1.00 16.25 ?  4640 ASP B CG  1 
ATOM   3068 O  OD1 . ASP B 1 165 ? 31.163  -16.578 -14.662 1.00 15.69 ?  4640 ASP B OD1 1 
ATOM   3069 O  OD2 . ASP B 1 165 ? 29.802  -16.268 -12.946 1.00 18.27 -1 4640 ASP B OD2 1 
ATOM   3070 N  N   . ARG B 1 166 ? 30.100  -17.348 -17.640 1.00 13.90 ?  4641 ARG B N   1 
ATOM   3071 C  CA  . ARG B 1 166 ? 29.903  -18.721 -18.090 1.00 14.52 ?  4641 ARG B CA  1 
ATOM   3072 C  C   . ARG B 1 166 ? 30.928  -19.633 -17.424 1.00 15.66 ?  4641 ARG B C   1 
ATOM   3073 O  O   . ARG B 1 166 ? 31.812  -19.187 -16.702 1.00 16.34 ?  4641 ARG B O   1 
ATOM   3074 C  CB  . ARG B 1 166 ? 29.907  -18.802 -19.621 1.00 17.57 ?  4641 ARG B CB  1 
ATOM   3075 C  CG  . ARG B 1 166 ? 28.548  -18.369 -20.181 1.00 18.48 ?  4641 ARG B CG  1 
ATOM   3076 C  CD  . ARG B 1 166 ? 28.409  -18.563 -21.680 1.00 24.95 ?  4641 ARG B CD  1 
ATOM   3077 N  NE  . ARG B 1 166 ? 27.081  -18.148 -22.133 1.00 21.36 ?  4641 ARG B NE  1 
ATOM   3078 C  CZ  . ARG B 1 166 ? 26.729  -18.030 -23.407 1.00 18.56 ?  4641 ARG B CZ  1 
ATOM   3079 N  NH1 . ARG B 1 166 ? 27.576  -18.321 -24.386 1.00 26.20 ?  4641 ARG B NH1 1 
ATOM   3080 N  NH2 . ARG B 1 166 ? 25.505  -17.616 -23.702 1.00 19.92 ?  4641 ARG B NH2 1 
ATOM   3081 N  N   . SER B 1 167 ? 30.795  -20.931 -17.666 1.00 15.24 ?  4642 SER B N   1 
ATOM   3082 C  CA  . SER B 1 167 ? 31.688  -21.891 -17.028 1.00 17.29 ?  4642 SER B CA  1 
ATOM   3083 C  C   . SER B 1 167 ? 33.142  -21.555 -17.333 1.00 17.62 ?  4642 SER B C   1 
ATOM   3084 O  O   . SER B 1 167 ? 33.480  -21.137 -18.443 1.00 16.76 ?  4642 SER B O   1 
ATOM   3085 C  CB  . SER B 1 167 ? 31.381  -23.286 -17.565 1.00 23.51 ?  4642 SER B CB  1 
ATOM   3086 O  OG  . SER B 1 167 ? 32.191  -24.246 -16.911 1.00 32.18 ?  4642 SER B OG  1 
ATOM   3087 N  N   . GLY B 1 168 ? 34.002  -21.747 -16.340 1.00 18.33 ?  4643 GLY B N   1 
ATOM   3088 C  CA  . GLY B 1 168 ? 35.383  -21.381 -16.525 1.00 19.40 ?  4643 GLY B CA  1 
ATOM   3089 C  C   . GLY B 1 168 ? 35.519  -19.866 -16.514 1.00 20.93 ?  4643 GLY B C   1 
ATOM   3090 O  O   . GLY B 1 168 ? 34.687  -19.137 -15.965 1.00 19.35 ?  4643 GLY B O   1 
ATOM   3091 N  N   . THR B 1 169 ? 36.597  -19.390 -17.129 1.00 21.20 ?  4644 THR B N   1 
ATOM   3092 C  CA  . THR B 1 169 ? 36.874  -17.960 -17.110 1.00 21.59 ?  4644 THR B CA  1 
ATOM   3093 C  C   . THR B 1 169 ? 37.077  -17.445 -18.518 1.00 20.52 ?  4644 THR B C   1 
ATOM   3094 O  O   . THR B 1 169 ? 36.834  -16.267 -18.797 1.00 22.89 ?  4644 THR B O   1 
ATOM   3095 C  CB  . THR B 1 169 ? 38.124  -17.664 -16.281 1.00 21.91 ?  4644 THR B CB  1 
ATOM   3096 O  OG1 . THR B 1 169 ? 39.240  -18.380 -16.837 1.00 27.05 ?  4644 THR B OG1 1 
ATOM   3097 C  CG2 . THR B 1 169 ? 37.928  -18.069 -14.830 1.00 21.87 ?  4644 THR B CG2 1 
ATOM   3098 N  N   . VAL B 1 170 ? 37.517  -18.327 -19.423 1.00 22.79 ?  4645 VAL B N   1 
ATOM   3099 C  CA  . VAL B 1 170 ? 37.973  -17.863 -20.728 1.00 23.17 ?  4645 VAL B CA  1 
ATOM   3100 C  C   . VAL B 1 170 ? 36.873  -17.126 -21.482 1.00 19.49 ?  4645 VAL B C   1 
ATOM   3101 O  O   . VAL B 1 170 ? 37.152  -16.163 -22.206 1.00 27.90 ?  4645 VAL B O   1 
ATOM   3102 C  CB  . VAL B 1 170 ? 38.608  -19.011 -21.542 1.00 22.89 ?  4645 VAL B CB  1 
ATOM   3103 C  CG1 . VAL B 1 170 ? 37.577  -20.085 -21.867 1.00 22.50 ?  4645 VAL B CG1 1 
ATOM   3104 C  CG2 . VAL B 1 170 ? 39.261  -18.472 -22.809 1.00 24.40 ?  4645 VAL B CG2 1 
ATOM   3105 N  N   . ASN B 1 171 ? 35.605  -17.513 -21.276 1.00 21.38 ?  4646 ASN B N   1 
ATOM   3106 C  CA  . ASN B 1 171 ? 34.473  -16.969 -22.018 1.00 17.73 ?  4646 ASN B CA  1 
ATOM   3107 C  C   . ASN B 1 171 ? 33.663  -15.934 -21.239 1.00 20.57 ?  4646 ASN B C   1 
ATOM   3108 O  O   . ASN B 1 171 ? 32.579  -15.552 -21.691 1.00 22.77 ?  4646 ASN B O   1 
ATOM   3109 C  CB  . ASN B 1 171 ? 33.530  -18.094 -22.441 1.00 20.18 ?  4646 ASN B CB  1 
ATOM   3110 C  CG  . ASN B 1 171 ? 34.161  -19.042 -23.433 1.00 22.38 ?  4646 ASN B CG  1 
ATOM   3111 O  OD1 . ASN B 1 171 ? 34.839  -18.615 -24.371 1.00 27.38 ?  4646 ASN B OD1 1 
ATOM   3112 N  ND2 . ASN B 1 171 ? 33.936  -20.336 -23.237 1.00 22.51 ?  4646 ASN B ND2 1 
ATOM   3113 N  N   . ASP B 1 172 ? 34.121  -15.521 -20.063 1.00 17.12 ?  4647 ASP B N   1 
ATOM   3114 C  CA  . ASP B 1 172 ? 33.397  -14.503 -19.303 1.00 15.42 ?  4647 ASP B CA  1 
ATOM   3115 C  C   . ASP B 1 172 ? 33.528  -13.155 -19.989 1.00 16.78 ?  4647 ASP B C   1 
ATOM   3116 O  O   . ASP B 1 172 ? 34.597  -12.809 -20.503 1.00 20.92 ?  4647 ASP B O   1 
ATOM   3117 C  CB  . ASP B 1 172 ? 33.979  -14.391 -17.898 1.00 15.90 ?  4647 ASP B CB  1 
ATOM   3118 C  CG  . ASP B 1 172 ? 33.736  -15.630 -17.061 1.00 14.59 ?  4647 ASP B CG  1 
ATOM   3119 O  OD1 . ASP B 1 172 ? 32.907  -16.472 -17.461 1.00 14.83 ?  4647 ASP B OD1 1 
ATOM   3120 O  OD2 . ASP B 1 172 ? 34.373  -15.763 -16.001 1.00 16.00 -1 4647 ASP B OD2 1 
ATOM   3121 N  N   . VAL B 1 173 ? 32.437  -12.392 -19.998 1.00 14.52 ?  4648 VAL B N   1 
ATOM   3122 C  CA  . VAL B 1 173 ? 32.382  -11.078 -20.628 1.00 14.49 ?  4648 VAL B CA  1 
ATOM   3123 C  C   . VAL B 1 173 ? 32.274  -10.017 -19.546 1.00 14.41 ?  4648 VAL B C   1 
ATOM   3124 O  O   . VAL B 1 173 ? 31.365  -10.070 -18.707 1.00 14.55 ?  4648 VAL B O   1 
ATOM   3125 C  CB  . VAL B 1 173 ? 31.180  -10.984 -21.577 1.00 15.44 ?  4648 VAL B CB  1 
ATOM   3126 C  CG1 . VAL B 1 173 ? 31.162  -9.640  -22.263 1.00 15.14 ?  4648 VAL B CG1 1 
ATOM   3127 C  CG2 . VAL B 1 173 ? 31.238  -12.119 -22.597 1.00 17.75 ?  4648 VAL B CG2 1 
ATOM   3128 N  N   . TYR B 1 174 ? 33.179  -9.042  -19.584 1.00 15.31 ?  4649 TYR B N   1 
ATOM   3129 C  CA  . TYR B 1 174 ? 33.200  -7.918  -18.661 1.00 15.34 ?  4649 TYR B CA  1 
ATOM   3130 C  C   . TYR B 1 174 ? 32.798  -6.658  -19.411 1.00 15.11 ?  4649 TYR B C   1 
ATOM   3131 O  O   . TYR B 1 174 ? 32.775  -6.623  -20.637 1.00 15.04 ?  4649 TYR B O   1 
ATOM   3132 C  CB  . TYR B 1 174 ? 34.607  -7.745  -18.079 1.00 16.07 ?  4649 TYR B CB  1 
ATOM   3133 C  CG  . TYR B 1 174 ? 34.988  -8.841  -17.125 1.00 16.05 ?  4649 TYR B CG  1 
ATOM   3134 C  CD1 . TYR B 1 174 ? 35.526  -10.045 -17.587 1.00 18.73 ?  4649 TYR B CD1 1 
ATOM   3135 C  CD2 . TYR B 1 174 ? 34.803  -8.686  -15.760 1.00 18.50 ?  4649 TYR B CD2 1 
ATOM   3136 C  CE1 . TYR B 1 174 ? 35.872  -11.057 -16.706 1.00 19.00 ?  4649 TYR B CE1 1 
ATOM   3137 C  CE2 . TYR B 1 174 ? 35.144  -9.683  -14.871 1.00 21.57 ?  4649 TYR B CE2 1 
ATOM   3138 C  CZ  . TYR B 1 174 ? 35.682  -10.866 -15.343 1.00 19.98 ?  4649 TYR B CZ  1 
ATOM   3139 O  OH  . TYR B 1 174 ? 36.012  -11.845 -14.435 1.00 23.55 ?  4649 TYR B OH  1 
ATOM   3140 N  N   . LEU B 1 175 ? 32.464  -5.608  -18.665 1.00 14.16 ?  4650 LEU B N   1 
ATOM   3141 C  CA  . LEU B 1 175 ? 32.051  -4.373  -19.321 1.00 13.75 ?  4650 LEU B CA  1 
ATOM   3142 C  C   . LEU B 1 175 ? 33.147  -3.846  -20.238 1.00 14.46 ?  4650 LEU B C   1 
ATOM   3143 O  O   . LEU B 1 175 ? 32.860  -3.295  -21.310 1.00 16.60 ?  4650 LEU B O   1 
ATOM   3144 C  CB  . LEU B 1 175 ? 31.664  -3.334  -18.267 1.00 15.98 ?  4650 LEU B CB  1 
ATOM   3145 C  CG  . LEU B 1 175 ? 31.238  -1.948  -18.759 1.00 15.32 ?  4650 LEU B CG  1 
ATOM   3146 C  CD1 . LEU B 1 175 ? 29.971  -2.051  -19.569 1.00 16.94 ?  4650 LEU B CD1 1 
ATOM   3147 C  CD2 . LEU B 1 175 ? 31.018  -1.022  -17.570 1.00 17.71 ?  4650 LEU B CD2 1 
ATOM   3148 N  N   . SER B 1 176 ? 34.408  -4.030  -19.839 1.00 16.54 ?  4651 SER B N   1 
ATOM   3149 C  CA  . SER B 1 176 ? 35.528  -3.585  -20.661 1.00 18.46 ?  4651 SER B CA  1 
ATOM   3150 C  C   . SER B 1 176 ? 35.553  -4.279  -22.013 1.00 19.80 ?  4651 SER B C   1 
ATOM   3151 O  O   . SER B 1 176 ? 36.029  -3.699  -22.995 1.00 22.19 ?  4651 SER B O   1 
ATOM   3152 C  CB  . SER B 1 176 ? 36.838  -3.848  -19.926 1.00 19.66 ?  4651 SER B CB  1 
ATOM   3153 O  OG  . SER B 1 176 ? 36.888  -5.191  -19.487 1.00 20.35 ?  4651 SER B OG  1 
ATOM   3154 N  N   . ASN B 1 177 ? 35.056  -5.512  -22.086 1.00 16.99 ?  4652 ASN B N   1 
ATOM   3155 C  CA  . ASN B 1 177 ? 34.964  -6.186  -23.379 1.00 16.17 ?  4652 ASN B CA  1 
ATOM   3156 C  C   . ASN B 1 177 ? 33.918  -5.557  -24.276 1.00 18.13 ?  4652 ASN B C   1 
ATOM   3157 O  O   . ASN B 1 177 ? 33.988  -5.718  -25.498 1.00 22.23 ?  4652 ASN B O   1 
ATOM   3158 C  CB  . ASN B 1 177 ? 34.630  -7.665  -23.198 1.00 16.26 ?  4652 ASN B CB  1 
ATOM   3159 C  CG  . ASN B 1 177 ? 35.690  -8.407  -22.431 1.00 18.68 ?  4652 ASN B CG  1 
ATOM   3160 O  OD1 . ASN B 1 177 ? 35.444  -8.929  -21.344 1.00 20.83 ?  4652 ASN B OD1 1 
ATOM   3161 N  ND2 . ASN B 1 177 ? 36.888  -8.475  -23.001 1.00 23.29 ?  4652 ASN B ND2 1 
ATOM   3162 N  N   . VAL B 1 178 ? 32.949  -4.859  -23.700 1.00 16.94 ?  4653 VAL B N   1 
ATOM   3163 C  CA  . VAL B 1 178 ? 31.859  -4.264  -24.457 1.00 18.62 ?  4653 VAL B CA  1 
ATOM   3164 C  C   . VAL B 1 178 ? 32.182  -2.840  -24.870 1.00 21.22 ?  4653 VAL B C   1 
ATOM   3165 O  O   . VAL B 1 178 ? 32.057  -2.477  -26.043 1.00 22.56 ?  4653 VAL B O   1 
ATOM   3166 C  CB  . VAL B 1 178 ? 30.576  -4.327  -23.606 1.00 17.69 ?  4653 VAL B CB  1 
ATOM   3167 C  CG1 . VAL B 1 178 ? 29.388  -3.798  -24.402 1.00 21.92 ?  4653 VAL B CG1 1 
ATOM   3168 C  CG2 . VAL B 1 178 ? 30.349  -5.745  -23.125 1.00 20.20 ?  4653 VAL B CG2 1 
ATOM   3169 N  N   . ILE B 1 179 ? 32.586  -2.008  -23.913 1.00 19.93 ?  4654 ILE B N   1 
ATOM   3170 C  CA  . ILE B 1 179 ? 32.799  -0.589  -24.185 1.00 21.94 ?  4654 ILE B CA  1 
ATOM   3171 C  C   . ILE B 1 179 ? 34.256  -0.238  -24.443 1.00 26.16 ?  4654 ILE B C   1 
ATOM   3172 O  O   . ILE B 1 179 ? 34.529  0.854   -24.963 1.00 28.26 ?  4654 ILE B O   1 
ATOM   3173 C  CB  . ILE B 1 179 ? 32.227  0.317   -23.075 1.00 21.34 ?  4654 ILE B CB  1 
ATOM   3174 C  CG1 . ILE B 1 179 ? 32.996  0.115   -21.765 1.00 20.81 ?  4654 ILE B CG1 1 
ATOM   3175 C  CG2 . ILE B 1 179 ? 30.736  0.060   -22.914 1.00 21.91 ?  4654 ILE B CG2 1 
ATOM   3176 C  CD1 . ILE B 1 179 ? 32.560  1.052   -20.644 1.00 24.99 ?  4654 ILE B CD1 1 
ATOM   3177 N  N   . GLY B 1 180 ? 35.192  -1.109  -24.083 1.00 28.68 ?  4655 GLY B N   1 
ATOM   3178 C  CA  . GLY B 1 180 ? 36.589  -0.799  -24.297 1.00 29.23 ?  4655 GLY B CA  1 
ATOM   3179 C  C   . GLY B 1 180 ? 37.021  0.414   -23.498 1.00 30.92 ?  4655 GLY B C   1 
ATOM   3180 O  O   . GLY B 1 180 ? 36.560  0.665   -22.375 1.00 31.38 ?  4655 GLY B O   1 
ATOM   3181 N  N   . THR B 1 181 ? 37.921  1.193   -24.095 1.00 36.82 ?  4656 THR B N   1 
ATOM   3182 C  CA  . THR B 1 181 ? 38.431  2.400   -23.461 1.00 38.25 ?  4656 THR B CA  1 
ATOM   3183 C  C   . THR B 1 181 ? 37.931  3.673   -24.138 1.00 37.88 ?  4656 THR B C   1 
ATOM   3184 O  O   . THR B 1 181 ? 38.408  4.764   -23.808 1.00 41.25 ?  4656 THR B O   1 
ATOM   3185 C  CB  . THR B 1 181 ? 39.964  2.378   -23.408 1.00 40.06 ?  4656 THR B CB  1 
ATOM   3186 O  OG1 . THR B 1 181 ? 40.496  2.761   -24.681 1.00 43.91 ?  4656 THR B OG1 1 
ATOM   3187 C  CG2 . THR B 1 181 ? 40.467  0.979   -23.069 1.00 39.89 ?  4656 THR B CG2 1 
ATOM   3188 N  N   . SER B 1 182 ? 36.975  3.566   -25.063 1.00 35.48 ?  4657 SER B N   1 
ATOM   3189 C  CA  . SER B 1 182 ? 36.491  4.721   -25.813 1.00 33.79 ?  4657 SER B CA  1 
ATOM   3190 C  C   . SER B 1 182 ? 34.968  4.805   -25.773 1.00 31.23 ?  4657 SER B C   1 
ATOM   3191 O  O   . SER B 1 182 ? 34.312  5.062   -26.784 1.00 34.43 ?  4657 SER B O   1 
ATOM   3192 C  CB  . SER B 1 182 ? 37.026  4.738   -27.243 1.00 37.89 ?  4657 SER B CB  1 
ATOM   3193 O  OG  . SER B 1 182 ? 36.069  4.249   -28.174 1.00 44.77 ?  4657 SER B OG  1 
ATOM   3194 N  N   . TYR B 1 183 ? 34.389  4.615   -24.586 1.00 29.41 ?  4658 TYR B N   1 
ATOM   3195 C  CA  . TYR B 1 183 ? 32.945  4.739   -24.435 1.00 25.17 ?  4658 TYR B CA  1 
ATOM   3196 C  C   . TYR B 1 183 ? 32.469  6.126   -24.853 1.00 26.72 ?  4658 TYR B C   1 
ATOM   3197 O  O   . TYR B 1 183 ? 33.066  7.146   -24.495 1.00 26.91 ?  4658 TYR B O   1 
ATOM   3198 C  CB  . TYR B 1 183 ? 32.533  4.469   -22.985 1.00 25.05 ?  4658 TYR B CB  1 
ATOM   3199 C  CG  . TYR B 1 183 ? 31.089  4.826   -22.696 1.00 21.98 ?  4658 TYR B CG  1 
ATOM   3200 C  CD1 . TYR B 1 183 ? 30.046  4.038   -23.180 1.00 18.93 ?  4658 TYR B CD1 1 
ATOM   3201 C  CD2 . TYR B 1 183 ? 30.763  5.951   -21.943 1.00 19.74 ?  4658 TYR B CD2 1 
ATOM   3202 C  CE1 . TYR B 1 183 ? 28.727  4.353   -22.925 1.00 18.56 ?  4658 TYR B CE1 1 
ATOM   3203 C  CE2 . TYR B 1 183 ? 29.454  6.276   -21.687 1.00 19.01 ?  4658 TYR B CE2 1 
ATOM   3204 C  CZ  . TYR B 1 183 ? 28.432  5.475   -22.174 1.00 17.73 ?  4658 TYR B CZ  1 
ATOM   3205 O  OH  . TYR B 1 183 ? 27.129  5.806   -21.914 1.00 20.19 ?  4658 TYR B OH  1 
ATOM   3206 N  N   . THR B 1 184 ? 31.381  6.155   -25.616 1.00 24.91 ?  4659 THR B N   1 
ATOM   3207 C  CA  . THR B 1 184 ? 30.750  7.388   -26.070 1.00 27.83 ?  4659 THR B CA  1 
ATOM   3208 C  C   . THR B 1 184 ? 29.367  7.462   -25.441 1.00 24.33 ?  4659 THR B C   1 
ATOM   3209 O  O   . THR B 1 184 ? 28.495  6.641   -25.749 1.00 25.84 ?  4659 THR B O   1 
ATOM   3210 C  CB  . THR B 1 184 ? 30.650  7.397   -27.595 1.00 27.28 ?  4659 THR B CB  1 
ATOM   3211 O  OG1 . THR B 1 184 ? 31.967  7.432   -28.159 1.00 33.09 ?  4659 THR B OG1 1 
ATOM   3212 C  CG2 . THR B 1 184 ? 29.853  8.608   -28.073 1.00 29.54 ?  4659 THR B CG2 1 
ATOM   3213 N  N   . TYR B 1 185 ? 29.161  8.441   -24.560 1.00 23.06 ?  4660 TYR B N   1 
ATOM   3214 C  CA  . TYR B 1 185 ? 27.853  8.601   -23.940 1.00 23.82 ?  4660 TYR B CA  1 
ATOM   3215 C  C   . TYR B 1 185 ? 26.771  8.819   -24.989 1.00 26.92 ?  4660 TYR B C   1 
ATOM   3216 O  O   . TYR B 1 185 ? 26.902  9.673   -25.875 1.00 26.56 ?  4660 TYR B O   1 
ATOM   3217 C  CB  . TYR B 1 185 ? 27.851  9.768   -22.951 1.00 27.05 ?  4660 TYR B CB  1 
ATOM   3218 C  CG  . TYR B 1 185 ? 26.479  9.983   -22.345 1.00 25.36 ?  4660 TYR B CG  1 
ATOM   3219 C  CD1 . TYR B 1 185 ? 25.979  9.100   -21.398 1.00 26.19 ?  4660 TYR B CD1 1 
ATOM   3220 C  CD2 . TYR B 1 185 ? 25.674  11.044  -22.735 1.00 25.93 ?  4660 TYR B CD2 1 
ATOM   3221 C  CE1 . TYR B 1 185 ? 24.730  9.272   -20.849 1.00 26.18 ?  4660 TYR B CE1 1 
ATOM   3222 C  CE2 . TYR B 1 185 ? 24.414  11.224  -22.193 1.00 28.45 ?  4660 TYR B CE2 1 
ATOM   3223 C  CZ  . TYR B 1 185 ? 23.952  10.332  -21.245 1.00 28.87 ?  4660 TYR B CZ  1 
ATOM   3224 O  OH  . TYR B 1 185 ? 22.704  10.491  -20.692 1.00 32.68 ?  4660 TYR B OH  1 
ATOM   3225 N  N   . GLY B 1 186 ? 25.679  8.064   -24.863 1.00 23.92 ?  4661 GLY B N   1 
ATOM   3226 C  CA  . GLY B 1 186 ? 24.575  8.113   -25.793 1.00 24.66 ?  4661 GLY B CA  1 
ATOM   3227 C  C   . GLY B 1 186 ? 24.587  7.016   -26.841 1.00 22.96 ?  4661 GLY B C   1 
ATOM   3228 O  O   . GLY B 1 186 ? 23.538  6.736   -27.438 1.00 28.31 ?  4661 GLY B O   1 
ATOM   3229 N  N   . GLN B 1 187 ? 25.744  6.425   -27.111 1.00 21.17 ?  4662 GLN B N   1 
ATOM   3230 C  CA  . GLN B 1 187 ? 25.812  5.278   -28.001 1.00 24.30 ?  4662 GLN B CA  1 
ATOM   3231 C  C   . GLN B 1 187 ? 25.374  4.026   -27.249 1.00 25.19 ?  4662 GLN B C   1 
ATOM   3232 O  O   . GLN B 1 187 ? 25.723  3.835   -26.079 1.00 24.26 ?  4662 GLN B O   1 
ATOM   3233 C  CB  . GLN B 1 187 ? 27.242  5.096   -28.515 1.00 25.73 ?  4662 GLN B CB  1 
ATOM   3234 C  CG  . GLN B 1 187 ? 27.440  3.878   -29.413 1.00 27.75 ?  4662 GLN B CG  1 
ATOM   3235 C  CD  . GLN B 1 187 ? 28.859  3.770   -29.948 1.00 32.73 ?  4662 GLN B CD  1 
ATOM   3236 O  OE1 . GLN B 1 187 ? 29.356  2.674   -30.213 1.00 36.61 ?  4662 GLN B OE1 1 
ATOM   3237 N  NE2 . GLN B 1 187 ? 29.517  4.915   -30.116 1.00 33.82 ?  4662 GLN B NE2 1 
ATOM   3238 N  N   . THR B 1 188 ? 24.599  3.176   -27.922 1.00 21.79 ?  4663 THR B N   1 
ATOM   3239 C  CA  . THR B 1 188 ? 24.150  1.916   -27.335 1.00 20.84 ?  4663 THR B CA  1 
ATOM   3240 C  C   . THR B 1 188 ? 25.177  0.823   -27.610 1.00 20.52 ?  4663 THR B C   1 
ATOM   3241 O  O   . THR B 1 188 ? 25.759  0.761   -28.696 1.00 23.75 ?  4663 THR B O   1 
ATOM   3242 C  CB  . THR B 1 188 ? 22.779  1.526   -27.898 1.00 25.48 ?  4663 THR B CB  1 
ATOM   3243 O  OG1 . THR B 1 188 ? 21.808  2.491   -27.480 1.00 28.51 ?  4663 THR B OG1 1 
ATOM   3244 C  CG2 . THR B 1 188 ? 22.346  0.156   -27.402 1.00 24.87 ?  4663 THR B CG2 1 
ATOM   3245 N  N   . TYR B 1 189 ? 25.424  -0.020  -26.603 1.00 18.52 ?  4664 TYR B N   1 
ATOM   3246 C  CA  . TYR B 1 189 ? 26.387  -1.105  -26.711 1.00 16.25 ?  4664 TYR B CA  1 
ATOM   3247 C  C   . TYR B 1 189 ? 25.690  -2.400  -26.351 1.00 16.98 ?  4664 TYR B C   1 
ATOM   3248 O  O   . TYR B 1 189 ? 24.834  -2.429  -25.461 1.00 17.42 ?  4664 TYR B O   1 
ATOM   3249 C  CB  . TYR B 1 189 ? 27.571  -0.907  -25.757 1.00 17.57 ?  4664 TYR B CB  1 
ATOM   3250 C  CG  . TYR B 1 189 ? 28.438  0.276   -26.103 1.00 18.56 ?  4664 TYR B CG  1 
ATOM   3251 C  CD1 . TYR B 1 189 ? 28.037  1.577   -25.789 1.00 18.55 ?  4664 TYR B CD1 1 
ATOM   3252 C  CD2 . TYR B 1 189 ? 29.669  0.096   -26.721 1.00 20.64 ?  4664 TYR B CD2 1 
ATOM   3253 C  CE1 . TYR B 1 189 ? 28.843  2.668   -26.111 1.00 19.02 ?  4664 TYR B CE1 1 
ATOM   3254 C  CE2 . TYR B 1 189 ? 30.482  1.182   -27.035 1.00 21.19 ?  4664 TYR B CE2 1 
ATOM   3255 C  CZ  . TYR B 1 189 ? 30.056  2.460   -26.726 1.00 24.06 ?  4664 TYR B CZ  1 
ATOM   3256 O  OH  . TYR B 1 189 ? 30.843  3.556   -27.023 1.00 27.46 ?  4664 TYR B OH  1 
ATOM   3257 N  N   . SER B 1 190 ? 26.064  -3.470  -27.046 1.00 16.14 ?  4665 SER B N   1 
ATOM   3258 C  CA  . SER B 1 190 ? 25.368  -4.737  -26.910 1.00 17.13 ?  4665 SER B CA  1 
ATOM   3259 C  C   . SER B 1 190 ? 26.336  -5.909  -27.008 1.00 18.82 ?  4665 SER B C   1 
ATOM   3260 O  O   . SER B 1 190 ? 27.462  -5.788  -27.504 1.00 20.53 ?  4665 SER B O   1 
ATOM   3261 C  CB  . SER B 1 190 ? 24.276  -4.873  -27.977 1.00 17.71 ?  4665 SER B CB  1 
ATOM   3262 O  OG  . SER B 1 190 ? 24.840  -4.764  -29.279 1.00 21.26 ?  4665 SER B OG  1 
ATOM   3263 N  N   . VAL B 1 191 ? 25.873  -7.058  -26.520 1.00 15.78 ?  4666 VAL B N   1 
ATOM   3264 C  CA  . VAL B 1 191 ? 26.574  -8.331  -26.647 1.00 18.83 ?  4666 VAL B CA  1 
ATOM   3265 C  C   . VAL B 1 191 ? 25.554  -9.321  -27.172 1.00 16.27 ?  4666 VAL B C   1 
ATOM   3266 O  O   . VAL B 1 191 ? 24.534  -9.556  -26.517 1.00 16.60 ?  4666 VAL B O   1 
ATOM   3267 C  CB  . VAL B 1 191 ? 27.117  -8.829  -25.298 1.00 21.09 ?  4666 VAL B CB  1 
ATOM   3268 C  CG1 . VAL B 1 191 ? 27.772  -10.194 -25.473 1.00 22.66 ?  4666 VAL B CG1 1 
ATOM   3269 C  CG2 . VAL B 1 191 ? 28.083  -7.832  -24.716 1.00 24.30 ?  4666 VAL B CG2 1 
ATOM   3270 N  N   . ASN B 1 192 ? 25.816  -9.890  -28.356 1.00 16.72 ?  4667 ASN B N   1 
ATOM   3271 C  CA  . ASN B 1 192 ? 24.885  -10.834 -28.987 1.00 17.36 ?  4667 ASN B CA  1 
ATOM   3272 C  C   . ASN B 1 192 ? 23.486  -10.237 -29.086 1.00 16.77 ?  4667 ASN B C   1 
ATOM   3273 O  O   . ASN B 1 192 ? 22.469  -10.918 -28.924 1.00 18.36 ?  4667 ASN B O   1 
ATOM   3274 C  CB  . ASN B 1 192 ? 24.874  -12.190 -28.273 1.00 19.15 ?  4667 ASN B CB  1 
ATOM   3275 C  CG  . ASN B 1 192 ? 26.217  -12.868 -28.315 1.00 22.71 ?  4667 ASN B CG  1 
ATOM   3276 O  OD1 . ASN B 1 192 ? 26.958  -12.725 -29.282 1.00 25.10 ?  4667 ASN B OD1 1 
ATOM   3277 N  ND2 . ASN B 1 192 ? 26.536  -13.631 -27.274 1.00 24.59 ?  4667 ASN B ND2 1 
ATOM   3278 N  N   . GLY B 1 193 ? 23.430  -8.934  -29.325 1.00 16.71 ?  4668 GLY B N   1 
ATOM   3279 C  CA  . GLY B 1 193 ? 22.160  -8.264  -29.466 1.00 18.35 ?  4668 GLY B CA  1 
ATOM   3280 C  C   . GLY B 1 193 ? 21.493  -7.852  -28.176 1.00 19.79 ?  4668 GLY B C   1 
ATOM   3281 O  O   . GLY B 1 193 ? 20.460  -7.181  -28.225 1.00 21.84 ?  4668 GLY B O   1 
ATOM   3282 N  N   . ARG B 1 194 ? 22.039  -8.221  -27.023 1.00 16.96 ?  4669 ARG B N   1 
ATOM   3283 C  CA  . ARG B 1 194 ? 21.464  -7.810  -25.749 1.00 16.64 ?  4669 ARG B CA  1 
ATOM   3284 C  C   . ARG B 1 194 ? 22.074  -6.485  -25.323 1.00 16.63 ?  4669 ARG B C   1 
ATOM   3285 O  O   . ARG B 1 194 ? 23.295  -6.346  -25.285 1.00 16.23 ?  4669 ARG B O   1 
ATOM   3286 C  CB  . ARG B 1 194 ? 21.716  -8.862  -24.677 1.00 18.79 ?  4669 ARG B CB  1 
ATOM   3287 C  CG  . ARG B 1 194 ? 21.191  -10.212 -25.107 1.00 18.13 ?  4669 ARG B CG  1 
ATOM   3288 C  CD  . ARG B 1 194 ? 21.211  -11.180 -23.986 1.00 20.67 ?  4669 ARG B CD  1 
ATOM   3289 N  NE  . ARG B 1 194 ? 20.552  -12.415 -24.394 1.00 19.33 ?  4669 ARG B NE  1 
ATOM   3290 C  CZ  . ARG B 1 194 ? 20.049  -13.305 -23.550 1.00 21.84 ?  4669 ARG B CZ  1 
ATOM   3291 N  NH1 . ARG B 1 194 ? 20.181  -13.167 -22.236 1.00 17.05 ?  4669 ARG B NH1 1 
ATOM   3292 N  NH2 . ARG B 1 194 ? 19.399  -14.360 -24.036 1.00 24.96 ?  4669 ARG B NH2 1 
ATOM   3293 N  N   . THR B 1 195 ? 21.226  -5.531  -24.983 1.00 17.07 ?  4670 THR B N   1 
ATOM   3294 C  CA  . THR B 1 195 ? 21.705  -4.200  -24.626 1.00 15.81 ?  4670 THR B CA  1 
ATOM   3295 C  C   . THR B 1 195 ? 22.447  -4.238  -23.295 1.00 16.15 ?  4670 THR B C   1 
ATOM   3296 O  O   . THR B 1 195 ? 21.904  -4.672  -22.273 1.00 19.32 ?  4670 THR B O   1 
ATOM   3297 C  CB  . THR B 1 195 ? 20.543  -3.220  -24.582 1.00 18.63 ?  4670 THR B CB  1 
ATOM   3298 O  OG1 . THR B 1 195 ? 20.002  -3.089  -25.895 1.00 22.87 ?  4670 THR B OG1 1 
ATOM   3299 C  CG2 . THR B 1 195 ? 21.016  -1.852  -24.095 1.00 20.07 ?  4670 THR B CG2 1 
ATOM   3300 N  N   . VAL B 1 196 ? 23.702  -3.810  -23.329 1.00 14.58 ?  4671 VAL B N   1 
ATOM   3301 C  CA  . VAL B 1 196 ? 24.536  -3.715  -22.138 1.00 16.79 ?  4671 VAL B CA  1 
ATOM   3302 C  C   . VAL B 1 196 ? 24.653  -2.277  -21.641 1.00 14.09 ?  4671 VAL B C   1 
ATOM   3303 O  O   . VAL B 1 196 ? 24.681  -2.036  -20.434 1.00 15.63 ?  4671 VAL B O   1 
ATOM   3304 C  CB  . VAL B 1 196 ? 25.917  -4.350  -22.400 1.00 16.18 ?  4671 VAL B CB  1 
ATOM   3305 C  CG1 . VAL B 1 196 ? 26.859  -4.086  -21.221 1.00 18.92 ?  4671 VAL B CG1 1 
ATOM   3306 C  CG2 . VAL B 1 196 ? 25.771  -5.863  -22.622 1.00 20.46 ?  4671 VAL B CG2 1 
ATOM   3307 N  N   . VAL B 1 197 ? 24.753  -1.303  -22.546 1.00 15.51 ?  4672 VAL B N   1 
ATOM   3308 C  CA  . VAL B 1 197 ? 24.676  0.108   -22.168 1.00 16.81 ?  4672 VAL B CA  1 
ATOM   3309 C  C   . VAL B 1 197 ? 23.647  0.773   -23.075 1.00 18.55 ?  4672 VAL B C   1 
ATOM   3310 O  O   . VAL B 1 197 ? 23.771  0.714   -24.308 1.00 17.42 ?  4672 VAL B O   1 
ATOM   3311 C  CB  . VAL B 1 197 ? 26.036  0.823   -22.251 1.00 15.67 ?  4672 VAL B CB  1 
ATOM   3312 C  CG1 . VAL B 1 197 ? 25.956  2.182   -21.554 1.00 17.41 ?  4672 VAL B CG1 1 
ATOM   3313 C  CG2 . VAL B 1 197 ? 27.141  -0.018  -21.612 1.00 17.98 ?  4672 VAL B CG2 1 
ATOM   3314 N  N   . ASN B 1 198 ? 22.613  1.357   -22.480 1.00 18.28 ?  4673 ASN B N   1 
ATOM   3315 C  CA  . ASN B 1 198 ? 21.614  2.041   -23.289 1.00 17.45 ?  4673 ASN B CA  1 
ATOM   3316 C  C   . ASN B 1 198 ? 22.024  3.492   -23.538 1.00 19.67 ?  4673 ASN B C   1 
ATOM   3317 O  O   . ASN B 1 198 ? 23.097  3.944   -23.131 1.00 18.46 ?  4673 ASN B O   1 
ATOM   3318 C  CB  . ASN B 1 198 ? 20.201  1.865   -22.729 1.00 18.48 ?  4673 ASN B CB  1 
ATOM   3319 C  CG  . ASN B 1 198 ? 19.923  2.715   -21.491 1.00 21.31 ?  4673 ASN B CG  1 
ATOM   3320 O  OD1 . ASN B 1 198 ? 20.719  3.567   -21.090 1.00 20.38 ?  4673 ASN B OD1 1 
ATOM   3321 N  ND2 . ASN B 1 198 ? 18.769  2.479   -20.884 1.00 22.63 ?  4673 ASN B ND2 1 
ATOM   3322 N  N   . GLY B 1 199 ? 21.158  4.223   -24.245 1.00 22.50 ?  4674 GLY B N   1 
ATOM   3323 C  CA  . GLY B 1 199 ? 21.498  5.569   -24.670 1.00 22.03 ?  4674 GLY B CA  1 
ATOM   3324 C  C   . GLY B 1 199 ? 21.547  6.573   -23.544 1.00 25.80 ?  4674 GLY B C   1 
ATOM   3325 O  O   . GLY B 1 199 ? 22.060  7.681   -23.739 1.00 26.53 ?  4674 GLY B O   1 
ATOM   3326 N  N   . ASN B 1 200 ? 21.007  6.221   -22.381 1.00 21.22 ?  4675 ASN B N   1 
ATOM   3327 C  CA  . ASN B 1 200 ? 21.097  7.044   -21.184 1.00 23.05 ?  4675 ASN B CA  1 
ATOM   3328 C  C   . ASN B 1 200 ? 22.219  6.600   -20.262 1.00 22.19 ?  4675 ASN B C   1 
ATOM   3329 O  O   . ASN B 1 200 ? 22.329  7.109   -19.141 1.00 21.77 ?  4675 ASN B O   1 
ATOM   3330 C  CB  . ASN B 1 200 ? 19.768  7.043   -20.439 1.00 25.89 ?  4675 ASN B CB  1 
ATOM   3331 C  CG  . ASN B 1 200 ? 18.665  7.702   -21.233 1.00 32.09 ?  4675 ASN B CG  1 
ATOM   3332 O  OD1 . ASN B 1 200 ? 18.896  8.682   -21.939 1.00 34.56 ?  4675 ASN B OD1 1 
ATOM   3333 N  ND2 . ASN B 1 200 ? 17.460  7.158   -21.134 1.00 32.54 ?  4675 ASN B ND2 1 
ATOM   3334 N  N   . GLY B 1 201 ? 23.051  5.666   -20.704 1.00 18.56 ?  4676 GLY B N   1 
ATOM   3335 C  CA  . GLY B 1 201 ? 24.162  5.209   -19.900 1.00 17.75 ?  4676 GLY B CA  1 
ATOM   3336 C  C   . GLY B 1 201 ? 23.834  4.143   -18.874 1.00 16.35 ?  4676 GLY B C   1 
ATOM   3337 O  O   . GLY B 1 201 ? 24.721  3.777   -18.103 1.00 17.38 ?  4676 GLY B O   1 
ATOM   3338 N  N   . VAL B 1 202 ? 22.601  3.643   -18.827 1.00 17.63 ?  4677 VAL B N   1 
ATOM   3339 C  CA  . VAL B 1 202 ? 22.268  2.583   -17.878 1.00 17.07 ?  4677 VAL B CA  1 
ATOM   3340 C  C   . VAL B 1 202 ? 22.960  1.297   -18.315 1.00 17.07 ?  4677 VAL B C   1 
ATOM   3341 O  O   . VAL B 1 202 ? 22.967  0.950   -19.504 1.00 16.32 ?  4677 VAL B O   1 
ATOM   3342 C  CB  . VAL B 1 202 ? 20.746  2.390   -17.798 1.00 17.49 ?  4677 VAL B CB  1 
ATOM   3343 C  CG1 . VAL B 1 202 ? 20.416  1.399   -16.708 1.00 18.87 ?  4677 VAL B CG1 1 
ATOM   3344 C  CG2 . VAL B 1 202 ? 20.039  3.723   -17.555 1.00 19.83 ?  4677 VAL B CG2 1 
ATOM   3345 N  N   . VAL B 1 203 ? 23.582  0.603   -17.364 1.00 15.67 ?  4678 VAL B N   1 
ATOM   3346 C  CA  . VAL B 1 203 ? 24.347  -0.612  -17.640 1.00 14.18 ?  4678 VAL B CA  1 
ATOM   3347 C  C   . VAL B 1 203 ? 23.559  -1.823  -17.159 1.00 14.21 ?  4678 VAL B C   1 
ATOM   3348 O  O   . VAL B 1 203 ? 23.115  -1.877  -16.001 1.00 15.09 ?  4678 VAL B O   1 
ATOM   3349 C  CB  . VAL B 1 203 ? 25.745  -0.572  -16.995 1.00 14.20 ?  4678 VAL B CB  1 
ATOM   3350 C  CG1 . VAL B 1 203 ? 26.508  -1.845  -17.311 1.00 15.43 ?  4678 VAL B CG1 1 
ATOM   3351 C  CG2 . VAL B 1 203 ? 26.518  0.646   -17.494 1.00 16.60 ?  4678 VAL B CG2 1 
ATOM   3352 N  N   . TYR B 1 204 ? 23.425  -2.815  -18.047 1.00 13.44 ?  4679 TYR B N   1 
ATOM   3353 C  CA  . TYR B 1 204 ? 22.694  -4.041  -17.789 1.00 16.09 ?  4679 TYR B CA  1 
ATOM   3354 C  C   . TYR B 1 204 ? 23.617  -5.225  -17.985 1.00 15.81 ?  4679 TYR B C   1 
ATOM   3355 O  O   . TYR B 1 204 ? 24.499  -5.208  -18.844 1.00 14.79 ?  4679 TYR B O   1 
ATOM   3356 C  CB  . TYR B 1 204 ? 21.539  -4.198  -18.784 1.00 13.16 ?  4679 TYR B CB  1 
ATOM   3357 C  CG  . TYR B 1 204 ? 20.539  -3.072  -18.729 1.00 16.85 ?  4679 TYR B CG  1 
ATOM   3358 C  CD1 . TYR B 1 204 ? 20.697  -1.951  -19.527 1.00 18.91 ?  4679 TYR B CD1 1 
ATOM   3359 C  CD2 . TYR B 1 204 ? 19.436  -3.141  -17.896 1.00 17.37 ?  4679 TYR B CD2 1 
ATOM   3360 C  CE1 . TYR B 1 204 ? 19.785  -0.914  -19.485 1.00 19.84 ?  4679 TYR B CE1 1 
ATOM   3361 C  CE2 . TYR B 1 204 ? 18.513  -2.109  -17.843 1.00 19.66 ?  4679 TYR B CE2 1 
ATOM   3362 C  CZ  . TYR B 1 204 ? 18.700  -0.996  -18.653 1.00 21.65 ?  4679 TYR B CZ  1 
ATOM   3363 O  OH  . TYR B 1 204 ? 17.796  0.048   -18.627 1.00 29.38 ?  4679 TYR B OH  1 
ATOM   3364 N  N   . ASP B 1 205 ? 23.397  -6.262  -17.189 1.00 14.11 ?  4680 ASP B N   1 
ATOM   3365 C  CA  . ASP B 1 205 ? 24.092  -7.514  -17.422 1.00 13.78 ?  4680 ASP B CA  1 
ATOM   3366 C  C   . ASP B 1 205 ? 23.397  -8.304  -18.530 1.00 15.60 ?  4680 ASP B C   1 
ATOM   3367 O  O   . ASP B 1 205 ? 22.359  -7.903  -19.080 1.00 14.85 ?  4680 ASP B O   1 
ATOM   3368 C  CB  . ASP B 1 205 ? 24.271  -8.292  -16.117 1.00 14.72 ?  4680 ASP B CB  1 
ATOM   3369 C  CG  . ASP B 1 205 ? 22.969  -8.810  -15.535 1.00 14.93 ?  4680 ASP B CG  1 
ATOM   3370 O  OD1 . ASP B 1 205 ? 21.935  -8.920  -16.226 1.00 15.84 ?  4680 ASP B OD1 1 
ATOM   3371 O  OD2 . ASP B 1 205 ? 22.972  -9.101  -14.324 1.00 19.25 -1 4680 ASP B OD2 1 
ATOM   3372 N  N   . TYR B 1 206 ? 23.970  -9.464  -18.851 1.00 14.57 ?  4681 TYR B N   1 
ATOM   3373 C  CA  . TYR B 1 206 ? 23.461  -10.274 -19.950 1.00 14.50 ?  4681 TYR B CA  1 
ATOM   3374 C  C   . TYR B 1 206 ? 22.047  -10.794 -19.688 1.00 15.04 ?  4681 TYR B C   1 
ATOM   3375 O  O   . TYR B 1 206 ? 21.338  -11.126 -20.642 1.00 17.01 ?  4681 TYR B O   1 
ATOM   3376 C  CB  . TYR B 1 206 ? 24.434  -11.426 -20.187 1.00 16.13 ?  4681 TYR B CB  1 
ATOM   3377 C  CG  . TYR B 1 206 ? 24.344  -12.117 -21.526 1.00 15.27 ?  4681 TYR B CG  1 
ATOM   3378 C  CD1 . TYR B 1 206 ? 24.822  -11.501 -22.688 1.00 14.93 ?  4681 TYR B CD1 1 
ATOM   3379 C  CD2 . TYR B 1 206 ? 23.831  -13.403 -21.628 1.00 15.90 ?  4681 TYR B CD2 1 
ATOM   3380 C  CE1 . TYR B 1 206 ? 24.764  -12.153 -23.910 1.00 17.31 ?  4681 TYR B CE1 1 
ATOM   3381 C  CE2 . TYR B 1 206 ? 23.767  -14.060 -22.852 1.00 15.87 ?  4681 TYR B CE2 1 
ATOM   3382 C  CZ  . TYR B 1 206 ? 24.231  -13.428 -23.977 1.00 17.52 ?  4681 TYR B CZ  1 
ATOM   3383 O  OH  . TYR B 1 206 ? 24.172  -14.097 -25.191 1.00 21.60 ?  4681 TYR B OH  1 
ATOM   3384 N  N   . ASN B 1 207 ? 21.624  -10.884 -18.429 1.00 14.61 ?  4682 ASN B N   1 
ATOM   3385 C  CA  . ASN B 1 207 ? 20.270  -11.298 -18.079 1.00 15.13 ?  4682 ASN B CA  1 
ATOM   3386 C  C   . ASN B 1 207 ? 19.256  -10.178 -18.202 1.00 16.24 ?  4682 ASN B C   1 
ATOM   3387 O  O   . ASN B 1 207 ? 18.062  -10.415 -17.967 1.00 18.50 ?  4682 ASN B O   1 
ATOM   3388 C  CB  . ASN B 1 207 ? 20.264  -11.849 -16.655 1.00 18.20 ?  4682 ASN B CB  1 
ATOM   3389 C  CG  . ASN B 1 207 ? 21.251  -12.975 -16.478 1.00 20.17 ?  4682 ASN B CG  1 
ATOM   3390 O  OD1 . ASN B 1 207 ? 21.327  -13.876 -17.306 1.00 20.40 ?  4682 ASN B OD1 1 
ATOM   3391 N  ND2 . ASN B 1 207 ? 22.029  -12.916 -15.417 1.00 21.33 ?  4682 ASN B ND2 1 
ATOM   3392 N  N   . GLY B 1 208 ? 19.700  -8.982  -18.551 1.00 16.09 ?  4683 GLY B N   1 
ATOM   3393 C  CA  . GLY B 1 208 ? 18.818  -7.850  -18.677 1.00 15.91 ?  4683 GLY B CA  1 
ATOM   3394 C  C   . GLY B 1 208 ? 18.602  -7.082  -17.402 1.00 16.81 ?  4683 GLY B C   1 
ATOM   3395 O  O   . GLY B 1 208 ? 17.717  -6.227  -17.363 1.00 17.81 ?  4683 GLY B O   1 
ATOM   3396 N  N   . ASN B 1 209 ? 19.366  -7.364  -16.357 1.00 15.01 ?  4684 ASN B N   1 
ATOM   3397 C  CA  . ASN B 1 209 ? 19.173  -6.697  -15.081 1.00 16.40 ?  4684 ASN B CA  1 
ATOM   3398 C  C   . ASN B 1 209 ? 20.129  -5.523  -14.946 1.00 15.44 ?  4684 ASN B C   1 
ATOM   3399 O  O   . ASN B 1 209 ? 21.318  -5.627  -15.271 1.00 15.66 ?  4684 ASN B O   1 
ATOM   3400 C  CB  . ASN B 1 209 ? 19.356  -7.700  -13.942 1.00 17.63 ?  4684 ASN B CB  1 
ATOM   3401 C  CG  . ASN B 1 209 ? 18.239  -8.729  -13.923 1.00 16.76 ?  4684 ASN B CG  1 
ATOM   3402 O  OD1 . ASN B 1 209 ? 17.072  -8.390  -14.172 1.00 20.17 ?  4684 ASN B OD1 1 
ATOM   3403 N  ND2 . ASN B 1 209 ? 18.585  -9.990  -13.677 1.00 19.11 ?  4684 ASN B ND2 1 
ATOM   3404 N  N   . GLN B 1 210 ? 19.603  -4.400  -14.475 1.00 16.57 ?  4685 GLN B N   1 
ATOM   3405 C  CA  . GLN B 1 210 ? 20.427  -3.215  -14.310 1.00 16.97 ?  4685 GLN B CA  1 
ATOM   3406 C  C   . GLN B 1 210 ? 21.440  -3.434  -13.188 1.00 15.32 ?  4685 GLN B C   1 
ATOM   3407 O  O   . GLN B 1 210 ? 21.083  -3.906  -12.106 1.00 17.18 ?  4685 GLN B O   1 
ATOM   3408 C  CB  . GLN B 1 210 ? 19.524  -2.022  -13.998 1.00 17.90 ?  4685 GLN B CB  1 
ATOM   3409 C  CG  . GLN B 1 210 ? 20.260  -0.702  -13.841 1.00 19.06 ?  4685 GLN B CG  1 
ATOM   3410 C  CD  . GLN B 1 210 ? 20.690  -0.421  -12.419 1.00 21.47 ?  4685 GLN B CD  1 
ATOM   3411 O  OE1 . GLN B 1 210 ? 20.042  -0.851  -11.464 1.00 25.46 ?  4685 GLN B OE1 1 
ATOM   3412 N  NE2 . GLN B 1 210 ? 21.804  0.289   -12.269 1.00 20.50 ?  4685 GLN B NE2 1 
ATOM   3413 N  N   . ILE B 1 211 ? 22.705  -3.082  -13.445 1.00 14.60 ?  4686 ILE B N   1 
ATOM   3414 C  CA  . ILE B 1 211 ? 23.788  -3.263  -12.475 1.00 16.66 ?  4686 ILE B CA  1 
ATOM   3415 C  C   . ILE B 1 211 ? 24.464  -1.944  -12.104 1.00 15.08 ?  4686 ILE B C   1 
ATOM   3416 O  O   . ILE B 1 211 ? 24.982  -1.796  -10.993 1.00 18.71 ?  4686 ILE B O   1 
ATOM   3417 C  CB  . ILE B 1 211 ? 24.819  -4.318  -12.933 1.00 15.60 ?  4686 ILE B CB  1 
ATOM   3418 C  CG1 . ILE B 1 211 ? 25.396  -3.974  -14.308 1.00 15.07 ?  4686 ILE B CG1 1 
ATOM   3419 C  CG2 . ILE B 1 211 ? 24.188  -5.707  -12.971 1.00 17.74 ?  4686 ILE B CG2 1 
ATOM   3420 C  CD1 . ILE B 1 211 ? 26.702  -4.737  -14.620 1.00 18.45 ?  4686 ILE B CD1 1 
ATOM   3421 N  N   . GLY B 1 212 ? 24.481  -0.984  -13.017 1.00 16.26 ?  4687 GLY B N   1 
ATOM   3422 C  CA  . GLY B 1 212 ? 25.117  0.280   -12.718 1.00 16.03 ?  4687 GLY B CA  1 
ATOM   3423 C  C   . GLY B 1 212 ? 24.801  1.292   -13.790 1.00 16.04 ?  4687 GLY B C   1 
ATOM   3424 O  O   . GLY B 1 212 ? 23.793  1.175   -14.489 1.00 15.01 ?  4687 GLY B O   1 
ATOM   3425 N  N   . TYR B 1 213 ? 25.667  2.304   -13.894 1.00 14.33 ?  4688 TYR B N   1 
ATOM   3426 C  CA  . TYR B 1 213 ? 25.445  3.418   -14.805 1.00 15.95 ?  4688 TYR B CA  1 
ATOM   3427 C  C   . TYR B 1 213 ? 26.790  3.944   -15.259 1.00 16.37 ?  4688 TYR B C   1 
ATOM   3428 O  O   . TYR B 1 213 ? 27.763  3.938   -14.500 1.00 19.42 ?  4688 TYR B O   1 
ATOM   3429 C  CB  . TYR B 1 213 ? 24.757  4.589   -14.080 1.00 16.98 ?  4688 TYR B CB  1 
ATOM   3430 C  CG  . TYR B 1 213 ? 23.436  4.244   -13.468 1.00 15.15 ?  4688 TYR B CG  1 
ATOM   3431 C  CD1 . TYR B 1 213 ? 22.265  4.360   -14.195 1.00 17.21 ?  4688 TYR B CD1 1 
ATOM   3432 C  CD2 . TYR B 1 213 ? 23.358  3.787   -12.155 1.00 17.94 ?  4688 TYR B CD2 1 
ATOM   3433 C  CE1 . TYR B 1 213 ? 21.050  4.036   -13.639 1.00 20.02 ?  4688 TYR B CE1 1 
ATOM   3434 C  CE2 . TYR B 1 213 ? 22.143  3.450   -11.600 1.00 20.93 ?  4688 TYR B CE2 1 
ATOM   3435 C  CZ  . TYR B 1 213 ? 20.994  3.580   -12.346 1.00 20.30 ?  4688 TYR B CZ  1 
ATOM   3436 O  OH  . TYR B 1 213 ? 19.764  3.254   -11.813 1.00 27.29 ?  4688 TYR B OH  1 
ATOM   3437 N  N   . MET B 1 214 ? 26.834  4.461   -16.485 1.00 15.47 ?  4689 MET B N   1 
ATOM   3438 C  CA  . MET B 1 214 ? 27.954  5.292   -16.908 1.00 15.69 ?  4689 MET B CA  1 
ATOM   3439 C  C   . MET B 1 214 ? 27.600  6.719   -16.496 1.00 17.74 ?  4689 MET B C   1 
ATOM   3440 O  O   . MET B 1 214 ? 26.620  7.281   -16.992 1.00 19.95 ?  4689 MET B O   1 
ATOM   3441 C  CB  . MET B 1 214 ? 28.180  5.190   -18.414 1.00 17.09 ?  4689 MET B CB  1 
ATOM   3442 C  CG  . MET B 1 214 ? 28.356  3.741   -18.907 1.00 18.00 ?  4689 MET B CG  1 
ATOM   3443 S  SD  . MET B 1 214 ? 29.779  2.944   -18.159 1.00 17.58 ?  4689 MET B SD  1 
ATOM   3444 C  CE  . MET B 1 214 ? 31.139  3.927   -18.826 1.00 19.51 ?  4689 MET B CE  1 
ATOM   3445 N  N   . ARG B 1 215 ? 28.356  7.275   -15.553 1.00 18.35 ?  4690 ARG B N   1 
ATOM   3446 C  CA  . ARG B 1 215 ? 28.029  8.573   -14.972 1.00 18.81 ?  4690 ARG B CA  1 
ATOM   3447 C  C   . ARG B 1 215 ? 29.163  9.561   -15.209 1.00 16.39 ?  4690 ARG B C   1 
ATOM   3448 O  O   . ARG B 1 215 ? 30.330  9.172   -15.288 1.00 18.53 ?  4690 ARG B O   1 
ATOM   3449 C  CB  . ARG B 1 215 ? 27.804  8.463   -13.456 1.00 16.01 ?  4690 ARG B CB  1 
ATOM   3450 C  CG  . ARG B 1 215 ? 26.603  7.616   -13.029 1.00 17.62 ?  4690 ARG B CG  1 
ATOM   3451 C  CD  . ARG B 1 215 ? 25.339  7.961   -13.792 1.00 17.96 ?  4690 ARG B CD  1 
ATOM   3452 N  NE  . ARG B 1 215 ? 24.934  9.356   -13.613 1.00 17.38 ?  4690 ARG B NE  1 
ATOM   3453 C  CZ  . ARG B 1 215 ? 24.055  9.990   -14.380 1.00 23.25 ?  4690 ARG B CZ  1 
ATOM   3454 N  NH1 . ARG B 1 215 ? 23.474  9.391   -15.410 1.00 24.08 ?  4690 ARG B NH1 1 
ATOM   3455 N  NH2 . ARG B 1 215 ? 23.763  11.262  -14.118 1.00 25.03 ?  4690 ARG B NH2 1 
ATOM   3456 N  N   . PRO B 1 216 ? 28.854  10.857  -15.261 1.00 19.28 ?  4691 PRO B N   1 
ATOM   3457 C  CA  . PRO B 1 216 ? 29.916  11.867  -15.296 1.00 21.17 ?  4691 PRO B CA  1 
ATOM   3458 C  C   . PRO B 1 216 ? 30.894  11.672  -14.145 1.00 20.70 ?  4691 PRO B C   1 
ATOM   3459 O  O   . PRO B 1 216 ? 30.506  11.337  -13.022 1.00 21.76 ?  4691 PRO B O   1 
ATOM   3460 C  CB  . PRO B 1 216 ? 29.144  13.186  -15.159 1.00 20.40 ?  4691 PRO B CB  1 
ATOM   3461 C  CG  . PRO B 1 216 ? 27.787  12.881  -15.738 1.00 20.65 ?  4691 PRO B CG  1 
ATOM   3462 C  CD  . PRO B 1 216 ? 27.509  11.455  -15.286 1.00 18.50 ?  4691 PRO B CD  1 
ATOM   3463 N  N   . ASP B 1 217 ? 32.183  11.855  -14.435 1.00 22.25 ?  4692 ASP B N   1 
ATOM   3464 C  CA  . ASP B 1 217 ? 33.199  11.729  -13.402 1.00 18.33 ?  4692 ASP B CA  1 
ATOM   3465 C  C   . ASP B 1 217 ? 33.618  13.066  -12.805 1.00 20.82 ?  4692 ASP B C   1 
ATOM   3466 O  O   . ASP B 1 217 ? 34.412  13.082  -11.860 1.00 21.95 ?  4692 ASP B O   1 
ATOM   3467 C  CB  . ASP B 1 217 ? 34.431  10.953  -13.902 1.00 20.68 ?  4692 ASP B CB  1 
ATOM   3468 C  CG  . ASP B 1 217 ? 35.241  11.703  -14.953 1.00 25.44 ?  4692 ASP B CG  1 
ATOM   3469 O  OD1 . ASP B 1 217 ? 34.779  12.741  -15.479 1.00 24.67 ?  4692 ASP B OD1 1 
ATOM   3470 O  OD2 . ASP B 1 217 ? 36.359  11.230  -15.255 1.00 27.00 -1 4692 ASP B OD2 1 
ATOM   3471 N  N   . GLY B 1 218 ? 33.102  14.175  -13.325 1.00 19.68 ?  4693 GLY B N   1 
ATOM   3472 C  CA  . GLY B 1 218 ? 33.502  15.487  -12.850 1.00 22.74 ?  4693 GLY B CA  1 
ATOM   3473 C  C   . GLY B 1 218 ? 34.737  16.041  -13.521 1.00 23.94 ?  4693 GLY B C   1 
ATOM   3474 O  O   . GLY B 1 218 ? 35.178  17.146  -13.162 1.00 27.78 ?  4693 GLY B O   1 
ATOM   3475 N  N   . ALA B 1 219 ? 35.313  15.310  -14.478 1.00 23.92 ?  4694 ALA B N   1 
ATOM   3476 C  CA  . ALA B 1 219 ? 36.487  15.751  -15.223 1.00 25.53 ?  4694 ALA B CA  1 
ATOM   3477 C  C   . ALA B 1 219 ? 36.249  15.708  -16.730 1.00 25.24 ?  4694 ALA B C   1 
ATOM   3478 O  O   . ALA B 1 219 ? 37.210  15.719  -17.508 1.00 31.77 ?  4694 ALA B O   1 
ATOM   3479 C  CB  . ALA B 1 219 ? 37.724  14.938  -14.833 1.00 26.12 ?  4694 ALA B CB  1 
ATOM   3480 N  N   . GLY B 1 220 ? 34.992  15.665  -17.158 1.00 24.69 ?  4695 GLY B N   1 
ATOM   3481 C  CA  . GLY B 1 220 ? 34.659  15.667  -18.565 1.00 25.00 ?  4695 GLY B CA  1 
ATOM   3482 C  C   . GLY B 1 220 ? 34.467  14.308  -19.197 1.00 26.49 ?  4695 GLY B C   1 
ATOM   3483 O  O   . GLY B 1 220 ? 34.322  14.234  -20.421 1.00 29.26 ?  4695 GLY B O   1 
ATOM   3484 N  N   . ARG B 1 221 ? 34.448  13.235  -18.413 1.00 23.85 ?  4696 ARG B N   1 
ATOM   3485 C  CA  . ARG B 1 221 ? 34.255  11.895  -18.949 1.00 25.79 ?  4696 ARG B CA  1 
ATOM   3486 C  C   . ARG B 1 221 ? 33.049  11.231  -18.295 1.00 23.43 ?  4696 ARG B C   1 
ATOM   3487 O  O   . ARG B 1 221 ? 32.439  11.761  -17.361 1.00 22.37 ?  4696 ARG B O   1 
ATOM   3488 C  CB  . ARG B 1 221 ? 35.499  11.028  -18.729 1.00 28.39 ?  4696 ARG B CB  1 
ATOM   3489 C  CG  . ARG B 1 221 ? 36.688  11.411  -19.595 1.00 36.17 ?  4696 ARG B CG  1 
ATOM   3490 C  CD  . ARG B 1 221 ? 37.925  10.648  -19.166 1.00 42.51 ?  4696 ARG B CD  1 
ATOM   3491 N  NE  . ARG B 1 221 ? 38.247  10.909  -17.761 1.00 45.05 ?  4696 ARG B NE  1 
ATOM   3492 C  CZ  . ARG B 1 221 ? 38.953  11.951  -17.344 1.00 47.40 ?  4696 ARG B CZ  1 
ATOM   3493 N  NH1 . ARG B 1 221 ? 39.437  12.842  -18.201 1.00 48.44 ?  4696 ARG B NH1 1 
ATOM   3494 N  NH2 . ARG B 1 221 ? 39.176  12.102  -16.042 1.00 44.78 ?  4696 ARG B NH2 1 
ATOM   3495 N  N   . TYR B 1 222 ? 32.706  10.052  -18.811 1.00 23.25 ?  4697 TYR B N   1 
ATOM   3496 C  CA  . TYR B 1 222 ? 31.704  9.182   -18.217 1.00 20.79 ?  4697 TYR B CA  1 
ATOM   3497 C  C   . TYR B 1 222 ? 32.394  7.887   -17.823 1.00 23.00 ?  4697 TYR B C   1 
ATOM   3498 O  O   . TYR B 1 222 ? 33.118  7.296   -18.633 1.00 24.10 ?  4697 TYR B O   1 
ATOM   3499 C  CB  . TYR B 1 222 ? 30.577  8.877   -19.210 1.00 22.60 ?  4697 TYR B CB  1 
ATOM   3500 C  CG  . TYR B 1 222 ? 29.527  9.954   -19.302 1.00 22.98 ?  4697 TYR B CG  1 
ATOM   3501 C  CD1 . TYR B 1 222 ? 29.784  11.153  -19.963 1.00 25.47 ?  4697 TYR B CD1 1 
ATOM   3502 C  CD2 . TYR B 1 222 ? 28.274  9.772   -18.739 1.00 24.36 ?  4697 TYR B CD2 1 
ATOM   3503 C  CE1 . TYR B 1 222 ? 28.817  12.142  -20.047 1.00 25.69 ?  4697 TYR B CE1 1 
ATOM   3504 C  CE2 . TYR B 1 222 ? 27.305  10.749  -18.814 1.00 27.12 ?  4697 TYR B CE2 1 
ATOM   3505 C  CZ  . TYR B 1 222 ? 27.583  11.932  -19.468 1.00 26.32 ?  4697 TYR B CZ  1 
ATOM   3506 O  OH  . TYR B 1 222 ? 26.608  12.898  -19.538 1.00 31.94 ?  4697 TYR B OH  1 
ATOM   3507 N  N   . VAL B 1 223 ? 32.178  7.463   -16.580 1.00 19.16 ?  4698 VAL B N   1 
ATOM   3508 C  CA  . VAL B 1 223 ? 32.849  6.311   -15.997 1.00 19.68 ?  4698 VAL B CA  1 
ATOM   3509 C  C   . VAL B 1 223 ? 31.800  5.460   -15.294 1.00 18.19 ?  4698 VAL B C   1 
ATOM   3510 O  O   . VAL B 1 223 ? 30.812  5.977   -14.768 1.00 19.00 ?  4698 VAL B O   1 
ATOM   3511 C  CB  . VAL B 1 223 ? 33.944  6.800   -15.021 1.00 24.45 ?  4698 VAL B CB  1 
ATOM   3512 C  CG1 . VAL B 1 223 ? 34.451  5.693   -14.156 1.00 27.71 ?  4698 VAL B CG1 1 
ATOM   3513 C  CG2 . VAL B 1 223 ? 35.096  7.427   -15.788 1.00 26.32 ?  4698 VAL B CG2 1 
ATOM   3514 N  N   . TYR B 1 224 ? 31.996  4.140   -15.311 1.00 16.86 ?  4699 TYR B N   1 
ATOM   3515 C  CA  . TYR B 1 224 ? 31.049  3.251   -14.648 1.00 16.46 ?  4699 TYR B CA  1 
ATOM   3516 C  C   . TYR B 1 224 ? 30.967  3.562   -13.158 1.00 16.20 ?  4699 TYR B C   1 
ATOM   3517 O  O   . TYR B 1 224 ? 31.979  3.842   -12.509 1.00 17.62 ?  4699 TYR B O   1 
ATOM   3518 C  CB  . TYR B 1 224 ? 31.477  1.794   -14.849 1.00 15.88 ?  4699 TYR B CB  1 
ATOM   3519 C  CG  . TYR B 1 224 ? 30.542  0.808   -14.195 1.00 15.69 ?  4699 TYR B CG  1 
ATOM   3520 C  CD1 . TYR B 1 224 ? 29.309  0.536   -14.763 1.00 16.27 ?  4699 TYR B CD1 1 
ATOM   3521 C  CD2 . TYR B 1 224 ? 30.875  0.174   -13.006 1.00 17.27 ?  4699 TYR B CD2 1 
ATOM   3522 C  CE1 . TYR B 1 224 ? 28.436  -0.348  -14.193 1.00 16.70 ?  4699 TYR B CE1 1 
ATOM   3523 C  CE2 . TYR B 1 224 ? 29.997  -0.717  -12.411 1.00 15.35 ?  4699 TYR B CE2 1 
ATOM   3524 C  CZ  . TYR B 1 224 ? 28.773  -0.978  -13.019 1.00 15.39 ?  4699 TYR B CZ  1 
ATOM   3525 O  OH  . TYR B 1 224 ? 27.884  -1.862  -12.451 1.00 18.67 ?  4699 TYR B OH  1 
ATOM   3526 N  N   . ALA B 1 225 ? 29.755  3.485   -12.617 1.00 14.62 ?  4700 ALA B N   1 
ATOM   3527 C  CA  . ALA B 1 225 ? 29.547  3.642   -11.185 1.00 16.76 ?  4700 ALA B CA  1 
ATOM   3528 C  C   . ALA B 1 225 ? 28.306  2.875   -10.761 1.00 16.48 ?  4700 ALA B C   1 
ATOM   3529 O  O   . ALA B 1 225 ? 27.447  2.534   -11.580 1.00 17.73 ?  4700 ALA B O   1 
ATOM   3530 C  CB  . ALA B 1 225 ? 29.370  5.122   -10.831 1.00 18.73 ?  4700 ALA B CB  1 
ATOM   3531 N  N   . THR B 1 226 ? 28.217  2.592   -9.470  1.00 15.61 ?  4701 THR B N   1 
ATOM   3532 C  CA  . THR B 1 226 ? 27.004  2.015   -8.922  1.00 18.19 ?  4701 THR B CA  1 
ATOM   3533 C  C   . THR B 1 226 ? 26.394  2.967   -7.909  1.00 17.82 ?  4701 THR B C   1 
ATOM   3534 O  O   . THR B 1 226 ? 27.099  3.738   -7.246  1.00 19.66 ?  4701 THR B O   1 
ATOM   3535 C  CB  . THR B 1 226 ? 27.243  0.651   -8.267  1.00 18.43 ?  4701 THR B CB  1 
ATOM   3536 O  OG1 . THR B 1 226 ? 28.185  0.790   -7.198  1.00 18.97 ?  4701 THR B OG1 1 
ATOM   3537 C  CG2 . THR B 1 226 ? 27.767  -0.343  -9.288  1.00 20.16 ?  4701 THR B CG2 1 
ATOM   3538 N  N   . LEU B 1 227 ? 25.073  2.911   -7.815  1.00 18.70 ?  4702 LEU B N   1 
ATOM   3539 C  CA  . LEU B 1 227 ? 24.347  3.673   -6.817  1.00 18.66 ?  4702 LEU B CA  1 
ATOM   3540 C  C   . LEU B 1 227 ? 24.609  3.100   -5.432  1.00 21.66 ?  4702 LEU B C   1 
ATOM   3541 O  O   . LEU B 1 227 ? 24.564  1.882   -5.221  1.00 21.48 ?  4702 LEU B O   1 
ATOM   3542 C  CB  . LEU B 1 227 ? 22.858  3.598   -7.123  1.00 19.45 ?  4702 LEU B CB  1 
ATOM   3543 C  CG  . LEU B 1 227 ? 21.914  4.524   -6.368  1.00 22.40 ?  4702 LEU B CG  1 
ATOM   3544 C  CD1 . LEU B 1 227 ? 22.237  5.976   -6.717  1.00 22.68 ?  4702 LEU B CD1 1 
ATOM   3545 C  CD2 . LEU B 1 227 ? 20.488  4.175   -6.734  1.00 24.60 ?  4702 LEU B CD2 1 
ATOM   3546 N  N   . ALA B 1 228 ? 24.870  3.989   -4.481  1.00 20.08 ?  4703 ALA B N   1 
ATOM   3547 C  CA  . ALA B 1 228 ? 25.162  3.612   -3.112  1.00 17.35 ?  4703 ALA B CA  1 
ATOM   3548 C  C   . ALA B 1 228 ? 24.301  4.438   -2.174  1.00 20.83 ?  4703 ALA B C   1 
ATOM   3549 O  O   . ALA B 1 228 ? 23.814  5.513   -2.526  1.00 19.91 ?  4703 ALA B O   1 
ATOM   3550 C  CB  . ALA B 1 228 ? 26.642  3.829   -2.767  1.00 19.35 ?  4703 ALA B CB  1 
ATOM   3551 N  N   . GLY B 1 229 ? 24.122  3.925   -0.967  1.00 19.88 ?  4704 GLY B N   1 
ATOM   3552 C  CA  . GLY B 1 229 ? 23.316  4.608   0.021   1.00 21.86 ?  4704 GLY B CA  1 
ATOM   3553 C  C   . GLY B 1 229 ? 21.918  4.025   0.103   1.00 23.63 ?  4704 GLY B C   1 
ATOM   3554 O  O   . GLY B 1 229 ? 21.469  3.254   -0.750  1.00 24.59 ?  4704 GLY B O   1 
ATOM   3555 N  N   . THR B 1 230 ? 21.218  4.415   1.164   1.00 26.90 ?  4705 THR B N   1 
ATOM   3556 C  CA  . THR B 1 230 ? 19.913  3.839   1.452   1.00 27.19 ?  4705 THR B CA  1 
ATOM   3557 C  C   . THR B 1 230 ? 18.770  4.614   0.826   1.00 29.56 ?  4705 THR B C   1 
ATOM   3558 O  O   . THR B 1 230 ? 17.696  4.043   0.602   1.00 31.73 ?  4705 THR B O   1 
ATOM   3559 C  CB  . THR B 1 230 ? 19.675  3.826   2.960   1.00 26.75 ?  4705 THR B CB  1 
ATOM   3560 O  OG1 . THR B 1 230 ? 19.637  5.180   3.426   1.00 31.38 ?  4705 THR B OG1 1 
ATOM   3561 C  CG2 . THR B 1 230 ? 20.789  3.090   3.673   1.00 26.82 ?  4705 THR B CG2 1 
ATOM   3562 N  N   . GLY B 1 231 ? 18.957  5.906   0.565   1.00 26.57 ?  4706 GLY B N   1 
ATOM   3563 C  CA  . GLY B 1 231 ? 17.868  6.748   0.130   1.00 29.70 ?  4706 GLY B CA  1 
ATOM   3564 C  C   . GLY B 1 231 ? 16.976  7.254   1.244   1.00 32.33 ?  4706 GLY B C   1 
ATOM   3565 O  O   . GLY B 1 231 ? 16.101  8.088   0.979   1.00 33.60 ?  4706 GLY B O   1 
ATOM   3566 N  N   . ASN B 1 232 ? 17.165  6.780   2.480   1.00 32.19 ?  4707 ASN B N   1 
ATOM   3567 C  CA  . ASN B 1 232 ? 16.349  7.194   3.616   1.00 34.80 ?  4707 ASN B CA  1 
ATOM   3568 C  C   . ASN B 1 232 ? 17.185  7.635   4.812   1.00 34.16 ?  4707 ASN B C   1 
ATOM   3569 O  O   . ASN B 1 232 ? 16.654  7.721   5.925   1.00 35.85 ?  4707 ASN B O   1 
ATOM   3570 C  CB  . ASN B 1 232 ? 15.354  6.093   4.029   1.00 33.24 ?  4707 ASN B CB  1 
ATOM   3571 C  CG  . ASN B 1 232 ? 16.035  4.780   4.428   1.00 38.94 ?  4707 ASN B CG  1 
ATOM   3572 O  OD1 . ASN B 1 232 ? 17.125  4.766   5.009   1.00 35.59 ?  4707 ASN B OD1 1 
ATOM   3573 N  ND2 . ASN B 1 232 ? 15.378  3.662   4.115   1.00 38.44 ?  4707 ASN B ND2 1 
ATOM   3574 N  N   . SER B 1 233 ? 18.470  7.912   4.618   1.00 30.39 ?  4708 SER B N   1 
ATOM   3575 C  CA  . SER B 1 233 ? 19.358  8.248   5.720   1.00 29.92 ?  4708 SER B CA  1 
ATOM   3576 C  C   . SER B 1 233 ? 20.652  8.787   5.136   1.00 27.95 ?  4708 SER B C   1 
ATOM   3577 O  O   . SER B 1 233 ? 20.941  8.617   3.947   1.00 24.90 ?  4708 SER B O   1 
ATOM   3578 C  CB  . SER B 1 233 ? 19.643  7.038   6.612   1.00 32.76 ?  4708 SER B CB  1 
ATOM   3579 O  OG  . SER B 1 233 ? 20.269  5.999   5.874   1.00 33.60 ?  4708 SER B OG  1 
ATOM   3580 N  N   . THR B 1 234 ? 21.443  9.413   6.003   1.00 26.01 ?  4709 THR B N   1 
ATOM   3581 C  CA  . THR B 1 234 ? 22.681  10.076  5.622   1.00 26.46 ?  4709 THR B CA  1 
ATOM   3582 C  C   . THR B 1 234 ? 23.770  9.593   6.562   1.00 27.44 ?  4709 THR B C   1 
ATOM   3583 O  O   . THR B 1 234 ? 23.695  9.828   7.773   1.00 33.82 ?  4709 THR B O   1 
ATOM   3584 C  CB  . THR B 1 234 ? 22.536  11.598  5.743   1.00 26.85 ?  4709 THR B CB  1 
ATOM   3585 O  OG1 . THR B 1 234 ? 21.419  12.041  4.962   1.00 24.66 ?  4709 THR B OG1 1 
ATOM   3586 C  CG2 . THR B 1 234 ? 23.806  12.297  5.259   1.00 23.96 ?  4709 THR B CG2 1 
ATOM   3587 N  N   . SER B 1 235 ? 24.775  8.932   6.012   1.00 26.56 ?  4710 SER B N   1 
ATOM   3588 C  CA  . SER B 1 235 ? 25.900  8.445   6.790   1.00 26.23 ?  4710 SER B CA  1 
ATOM   3589 C  C   . SER B 1 235 ? 27.112  9.340   6.574   1.00 26.57 ?  4710 SER B C   1 
ATOM   3590 O  O   . SER B 1 235 ? 27.158  10.167  5.657   1.00 23.27 ?  4710 SER B O   1 
ATOM   3591 C  CB  . SER B 1 235 ? 26.244  7.009   6.391   1.00 25.93 ?  4710 SER B CB  1 
ATOM   3592 O  OG  . SER B 1 235 ? 26.747  6.964   5.061   1.00 30.71 ?  4710 SER B OG  1 
ATOM   3593 N  N   . SER B 1 236 ? 28.107  9.165   7.446   1.00 25.52 ?  4711 SER B N   1 
ATOM   3594 C  CA  . SER B 1 236 ? 29.377  9.852   7.254   1.00 26.22 ?  4711 SER B CA  1 
ATOM   3595 C  C   . SER B 1 236 ? 29.988  9.534   5.892   1.00 22.70 ?  4711 SER B C   1 
ATOM   3596 O  O   . SER B 1 236 ? 30.661  10.388  5.306   1.00 23.76 ?  4711 SER B O   1 
ATOM   3597 C  CB  . SER B 1 236 ? 30.346  9.507   8.387   1.00 28.94 ?  4711 SER B CB  1 
ATOM   3598 O  OG  . SER B 1 236 ? 30.651  8.124   8.387   1.00 32.75 ?  4711 SER B OG  1 
ATOM   3599 N  N   . THR B 1 237 ? 29.769  8.319   5.373   1.00 25.58 ?  4712 THR B N   1 
ATOM   3600 C  CA  . THR B 1 237 ? 30.255  7.980   4.035   1.00 22.97 ?  4712 THR B CA  1 
ATOM   3601 C  C   . THR B 1 237 ? 29.506  8.760   2.958   1.00 21.06 ?  4712 THR B C   1 
ATOM   3602 O  O   . THR B 1 237 ? 30.121  9.260   2.006   1.00 20.56 ?  4712 THR B O   1 
ATOM   3603 C  CB  . THR B 1 237 ? 30.146  6.472   3.799   1.00 25.47 ?  4712 THR B CB  1 
ATOM   3604 O  OG1 . THR B 1 237 ? 30.892  5.782   4.810   1.00 27.31 ?  4712 THR B OG1 1 
ATOM   3605 C  CG2 . THR B 1 237 ? 30.702  6.086   2.428   1.00 23.67 ?  4712 THR B CG2 1 
ATOM   3606 N  N   . THR B 1 238 ? 28.178  8.859   3.079   1.00 20.15 ?  4713 THR B N   1 
ATOM   3607 C  CA  . THR B 1 238 ? 27.402  9.689   2.158   1.00 19.37 ?  4713 THR B CA  1 
ATOM   3608 C  C   . THR B 1 238 ? 27.949  11.108  2.119   1.00 19.62 ?  4713 THR B C   1 
ATOM   3609 O  O   . THR B 1 238 ? 28.126  11.695  1.043   1.00 18.19 ?  4713 THR B O   1 
ATOM   3610 C  CB  . THR B 1 238 ? 25.939  9.732   2.607   1.00 24.80 ?  4713 THR B CB  1 
ATOM   3611 O  OG1 . THR B 1 238 ? 25.478  8.409   2.900   1.00 29.09 ?  4713 THR B OG1 1 
ATOM   3612 C  CG2 . THR B 1 238 ? 25.064  10.342  1.524   1.00 23.01 ?  4713 THR B CG2 1 
ATOM   3613 N  N   . ILE B 1 239 ? 28.228  11.673  3.293   1.00 20.79 ?  4714 ILE B N   1 
ATOM   3614 C  CA  . ILE B 1 239 ? 28.738  13.039  3.353   1.00 21.05 ?  4714 ILE B CA  1 
ATOM   3615 C  C   . ILE B 1 239 ? 30.117  13.131  2.717   1.00 18.50 ?  4714 ILE B C   1 
ATOM   3616 O  O   . ILE B 1 239 ? 30.385  14.031  1.915   1.00 17.62 ?  4714 ILE B O   1 
ATOM   3617 C  CB  . ILE B 1 239 ? 28.731  13.562  4.801   1.00 20.38 ?  4714 ILE B CB  1 
ATOM   3618 C  CG1 . ILE B 1 239 ? 27.285  13.689  5.285   1.00 22.72 ?  4714 ILE B CG1 1 
ATOM   3619 C  CG2 . ILE B 1 239 ? 29.469  14.893  4.879   1.00 22.39 ?  4714 ILE B CG2 1 
ATOM   3620 C  CD1 . ILE B 1 239 ? 27.137  13.795  6.794   1.00 25.54 ?  4714 ILE B CD1 1 
ATOM   3621 N  N   . ALA B 1 240 ? 31.007  12.197  3.051   1.00 18.91 ?  4715 ALA B N   1 
ATOM   3622 C  CA  . ALA B 1 240 ? 32.354  12.250  2.500   1.00 19.52 ?  4715 ALA B CA  1 
ATOM   3623 C  C   . ALA B 1 240 ? 32.324  12.201  0.981   1.00 17.63 ?  4715 ALA B C   1 
ATOM   3624 O  O   . ALA B 1 240 ? 33.063  12.932  0.316   1.00 18.96 ?  4715 ALA B O   1 
ATOM   3625 C  CB  . ALA B 1 240 ? 33.196  11.104  3.058   1.00 19.65 ?  4715 ALA B CB  1 
ATOM   3626 N  N   . ASN B 1 241 ? 31.463  11.357  0.414   1.00 19.29 ?  4716 ASN B N   1 
ATOM   3627 C  CA  . ASN B 1 241 ? 31.370  11.273  -1.039  1.00 19.14 ?  4716 ASN B CA  1 
ATOM   3628 C  C   . ASN B 1 241 ? 30.792  12.551  -1.632  1.00 19.27 ?  4716 ASN B C   1 
ATOM   3629 O  O   . ASN B 1 241 ? 31.200  12.970  -2.724  1.00 19.23 ?  4716 ASN B O   1 
ATOM   3630 C  CB  . ASN B 1 241 ? 30.528  10.065  -1.444  1.00 17.98 ?  4716 ASN B CB  1 
ATOM   3631 C  CG  . ASN B 1 241 ? 31.330  8.779   -1.455  1.00 18.07 ?  4716 ASN B CG  1 
ATOM   3632 O  OD1 . ASN B 1 241 ? 31.861  8.370   -2.498  1.00 17.94 ?  4716 ASN B OD1 1 
ATOM   3633 N  ND2 . ASN B 1 241 ? 31.440  8.136   -0.287  1.00 20.53 ?  4716 ASN B ND2 1 
ATOM   3634 N  N   . SER B 1 242 ? 29.840  13.180  -0.931  1.00 20.49 ?  4717 SER B N   1 
ATOM   3635 C  CA  . SER B 1 242 ? 29.259  14.424  -1.430  1.00 21.02 ?  4717 SER B CA  1 
ATOM   3636 C  C   . SER B 1 242 ? 30.280  15.555  -1.387  1.00 20.70 ?  4717 SER B C   1 
ATOM   3637 O  O   . SER B 1 242 ? 30.406  16.330  -2.345  1.00 18.74 ?  4717 SER B O   1 
ATOM   3638 C  CB  . SER B 1 242 ? 28.029  14.795  -0.597  1.00 20.23 ?  4717 SER B CB  1 
ATOM   3639 O  OG  . SER B 1 242 ? 27.132  13.704  -0.443  1.00 21.59 ?  4717 SER B OG  1 
ATOM   3640 N  N   . VAL B 1 243 ? 31.022  15.657  -0.280  1.00 18.84 ?  4718 VAL B N   1 
ATOM   3641 C  CA  . VAL B 1 243 ? 32.020  16.713  -0.134  1.00 19.46 ?  4718 VAL B CA  1 
ATOM   3642 C  C   . VAL B 1 243 ? 33.153  16.536  -1.141  1.00 20.58 ?  4718 VAL B C   1 
ATOM   3643 O  O   . VAL B 1 243 ? 33.627  17.509  -1.742  1.00 19.62 ?  4718 VAL B O   1 
ATOM   3644 C  CB  . VAL B 1 243 ? 32.519  16.763  1.324   1.00 19.57 ?  4718 VAL B CB  1 
ATOM   3645 C  CG1 . VAL B 1 243 ? 33.761  17.648  1.444   1.00 22.60 ?  4718 VAL B CG1 1 
ATOM   3646 C  CG2 . VAL B 1 243 ? 31.411  17.261  2.241   1.00 20.39 ?  4718 VAL B CG2 1 
ATOM   3647 N  N   . ALA B 1 244 ? 33.601  15.295  -1.357  1.00 20.44 ?  4719 ALA B N   1 
ATOM   3648 C  CA  . ALA B 1 244 ? 34.635  15.074  -2.365  1.00 20.38 ?  4719 ALA B CA  1 
ATOM   3649 C  C   . ALA B 1 244 ? 34.132  15.443  -3.757  1.00 21.60 ?  4719 ALA B C   1 
ATOM   3650 O  O   . ALA B 1 244 ? 34.851  16.085  -4.531  1.00 21.26 ?  4719 ALA B O   1 
ATOM   3651 C  CB  . ALA B 1 244 ? 35.123  13.625  -2.319  1.00 22.73 ?  4719 ALA B CB  1 
ATOM   3652 N  N   . GLY B 1 245 ? 32.894  15.057  -4.087  1.00 19.38 ?  4720 GLY B N   1 
ATOM   3653 C  CA  . GLY B 1 245 ? 32.343  15.425  -5.383  1.00 22.40 ?  4720 GLY B CA  1 
ATOM   3654 C  C   . GLY B 1 245 ? 32.233  16.927  -5.554  1.00 20.23 ?  4720 GLY B C   1 
ATOM   3655 O  O   . GLY B 1 245 ? 32.509  17.461  -6.634  1.00 21.33 ?  4720 GLY B O   1 
ATOM   3656 N  N   . PHE B 1 246 ? 31.844  17.628  -4.483  1.00 19.62 ?  4721 PHE B N   1 
ATOM   3657 C  CA  . PHE B 1 246 ? 31.736  19.083  -4.519  1.00 20.48 ?  4721 PHE B CA  1 
ATOM   3658 C  C   . PHE B 1 246 ? 33.070  19.727  -4.868  1.00 22.67 ?  4721 PHE B C   1 
ATOM   3659 O  O   . PHE B 1 246 ? 33.113  20.718  -5.606  1.00 22.88 ?  4721 PHE B O   1 
ATOM   3660 C  CB  . PHE B 1 246 ? 31.227  19.587  -3.165  1.00 18.66 ?  4721 PHE B CB  1 
ATOM   3661 C  CG  . PHE B 1 246 ? 30.851  21.032  -3.166  1.00 22.37 ?  4721 PHE B CG  1 
ATOM   3662 C  CD1 . PHE B 1 246 ? 29.717  21.465  -3.848  1.00 21.46 ?  4721 PHE B CD1 1 
ATOM   3663 C  CD2 . PHE B 1 246 ? 31.619  21.961  -2.475  1.00 24.20 ?  4721 PHE B CD2 1 
ATOM   3664 C  CE1 . PHE B 1 246 ? 29.368  22.804  -3.858  1.00 24.63 ?  4721 PHE B CE1 1 
ATOM   3665 C  CE2 . PHE B 1 246 ? 31.271  23.300  -2.470  1.00 24.21 ?  4721 PHE B CE2 1 
ATOM   3666 C  CZ  . PHE B 1 246 ? 30.144  23.723  -3.171  1.00 25.30 ?  4721 PHE B CZ  1 
ATOM   3667 N  N   . GLY B 1 247 ? 34.170  19.163  -4.370  1.00 20.88 ?  4722 GLY B N   1 
ATOM   3668 C  CA  . GLY B 1 247 ? 35.485  19.687  -4.688  1.00 22.20 ?  4722 GLY B CA  1 
ATOM   3669 C  C   . GLY B 1 247 ? 35.805  19.642  -6.168  1.00 23.82 ?  4722 GLY B C   1 
ATOM   3670 O  O   . GLY B 1 247 ? 36.581  20.465  -6.661  1.00 24.08 ?  4722 GLY B O   1 
ATOM   3671 N  N   . LEU B 1 248 ? 35.232  18.677  -6.896  1.00 20.67 ?  4723 LEU B N   1 
ATOM   3672 C  CA  . LEU B 1 248 ? 35.437  18.648  -8.342  1.00 21.15 ?  4723 LEU B CA  1 
ATOM   3673 C  C   . LEU B 1 248 ? 34.735  19.815  -9.014  1.00 21.49 ?  4723 LEU B C   1 
ATOM   3674 O  O   . LEU B 1 248 ? 35.233  20.358  -10.006 1.00 22.92 ?  4723 LEU B O   1 
ATOM   3675 C  CB  . LEU B 1 248 ? 34.938  17.332  -8.933  1.00 22.35 ?  4723 LEU B CB  1 
ATOM   3676 C  CG  . LEU B 1 248 ? 35.632  16.104  -8.362  1.00 24.69 ?  4723 LEU B CG  1 
ATOM   3677 C  CD1 . LEU B 1 248 ? 34.974  14.862  -8.909  1.00 24.24 ?  4723 LEU B CD1 1 
ATOM   3678 C  CD2 . LEU B 1 248 ? 37.115  16.138  -8.699  1.00 25.97 ?  4723 LEU B CD2 1 
ATOM   3679 N  N   . LEU B 1 249 ? 33.574  20.203  -8.494  1.00 18.74 ?  4724 LEU B N   1 
ATOM   3680 C  CA  . LEU B 1 249 ? 32.856  21.341  -9.053  1.00 21.52 ?  4724 LEU B CA  1 
ATOM   3681 C  C   . LEU B 1 249 ? 33.569  22.654  -8.733  1.00 23.43 ?  4724 LEU B C   1 
ATOM   3682 O  O   . LEU B 1 249 ? 33.826  23.468  -9.631  1.00 21.53 ?  4724 LEU B O   1 
ATOM   3683 C  CB  . LEU B 1 249 ? 31.420  21.342  -8.532  1.00 20.57 ?  4724 LEU B CB  1 
ATOM   3684 C  CG  . LEU B 1 249 ? 30.518  22.517  -8.920  1.00 21.93 ?  4724 LEU B CG  1 
ATOM   3685 C  CD1 . LEU B 1 249 ? 30.380  22.634  -10.437 1.00 21.02 ?  4724 LEU B CD1 1 
ATOM   3686 C  CD2 . LEU B 1 249 ? 29.151  22.366  -8.268  1.00 20.95 ?  4724 LEU B CD2 1 
ATOM   3687 N  N   . THR B 1 250 ? 33.908  22.883  -7.462  1.00 21.97 ?  4725 THR B N   1 
ATOM   3688 C  CA  . THR B 1 250 ? 34.590  24.130  -7.122  1.00 23.02 ?  4725 THR B CA  1 
ATOM   3689 C  C   . THR B 1 250 ? 35.972  24.205  -7.746  1.00 24.86 ?  4725 THR B C   1 
ATOM   3690 O  O   . THR B 1 250 ? 36.452  25.306  -8.048  1.00 24.22 ?  4725 THR B O   1 
ATOM   3691 C  CB  . THR B 1 250 ? 34.703  24.291  -5.610  1.00 25.33 ?  4725 THR B CB  1 
ATOM   3692 O  OG1 . THR B 1 250 ? 35.405  23.165  -5.058  1.00 25.39 ?  4725 THR B OG1 1 
ATOM   3693 C  CG2 . THR B 1 250 ? 33.328  24.399  -4.995  1.00 24.60 ?  4725 THR B CG2 1 
ATOM   3694 N  N   . GLY B 1 251 ? 36.624  23.059  -7.948  1.00 24.83 ?  4726 GLY B N   1 
ATOM   3695 C  CA  . GLY B 1 251 ? 37.937  23.026  -8.570  1.00 23.41 ?  4726 GLY B CA  1 
ATOM   3696 C  C   . GLY B 1 251 ? 37.939  23.357  -10.047 1.00 23.79 ?  4726 GLY B C   1 
ATOM   3697 O  O   . GLY B 1 251 ? 39.017  23.465  -10.641 1.00 24.44 ?  4726 GLY B O   1 
ATOM   3698 N  N   . MET B 1 252 ? 36.768  23.490  -10.658 1.00 23.79 ?  4727 MET B N   1 
ATOM   3699 C  CA  . MET B 1 252 ? 36.690  24.060  -11.992 1.00 23.60 ?  4727 MET B CA  1 
ATOM   3700 C  C   . MET B 1 252 ? 36.682  25.581  -11.957 1.00 28.56 ?  4727 MET B C   1 
ATOM   3701 O  O   . MET B 1 252 ? 36.462  26.211  -12.996 1.00 28.77 ?  4727 MET B O   1 
ATOM   3702 C  CB  . MET B 1 252 ? 35.456  23.528  -12.731 1.00 25.41 ?  4727 MET B CB  1 
ATOM   3703 C  CG  . MET B 1 252 ? 35.466  22.014  -12.992 1.00 25.20 ?  4727 MET B CG  1 
ATOM   3704 S  SD  . MET B 1 252 ? 36.958  21.452  -13.850 1.00 29.85 ?  4727 MET B SD  1 
ATOM   3705 C  CE  . MET B 1 252 ? 36.951  22.507  -15.296 1.00 29.70 ?  4727 MET B CE  1 
ATOM   3706 N  N   . GLY B 1 253 ? 36.922  26.173  -10.790 1.00 25.13 ?  4728 GLY B N   1 
ATOM   3707 C  CA  . GLY B 1 253 ? 36.855  27.615  -10.642 1.00 28.22 ?  4728 GLY B CA  1 
ATOM   3708 C  C   . GLY B 1 253 ? 35.444  28.149  -10.557 1.00 25.93 ?  4728 GLY B C   1 
ATOM   3709 O  O   . GLY B 1 253 ? 35.149  29.202  -11.138 1.00 31.53 ?  4728 GLY B O   1 
ATOM   3710 N  N   . VAL B 1 254 ? 34.562  27.462  -9.832  1.00 24.66 ?  4729 VAL B N   1 
ATOM   3711 C  CA  . VAL B 1 254 ? 33.133  27.758  -9.815  1.00 20.15 ?  4729 VAL B CA  1 
ATOM   3712 C  C   . VAL B 1 254 ? 32.750  28.266  -8.434  1.00 24.73 ?  4729 VAL B C   1 
ATOM   3713 O  O   . VAL B 1 254 ? 33.091  27.647  -7.419  1.00 24.31 ?  4729 VAL B O   1 
ATOM   3714 C  CB  . VAL B 1 254 ? 32.305  26.514  -10.184 1.00 22.69 ?  4729 VAL B CB  1 
ATOM   3715 C  CG1 . VAL B 1 254 ? 30.819  26.823  -10.079 1.00 21.70 ?  4729 VAL B CG1 1 
ATOM   3716 C  CG2 . VAL B 1 254 ? 32.678  26.011  -11.582 1.00 21.64 ?  4729 VAL B CG2 1 
ATOM   3717 N  N   . THR B 1 255 ? 32.035  29.388  -8.397  1.00 25.13 ?  4730 THR B N   1 
ATOM   3718 C  CA  . THR B 1 255 ? 31.432  29.888  -7.170  1.00 23.32 ?  4730 THR B CA  1 
ATOM   3719 C  C   . THR B 1 255 ? 30.058  29.253  -7.015  1.00 24.51 ?  4730 THR B C   1 
ATOM   3720 O  O   . THR B 1 255 ? 29.228  29.328  -7.924  1.00 26.52 ?  4730 THR B O   1 
ATOM   3721 C  CB  . THR B 1 255 ? 31.280  31.410  -7.238  1.00 24.50 ?  4730 THR B CB  1 
ATOM   3722 O  OG1 . THR B 1 255 ? 32.578  32.013  -7.321  1.00 31.50 ?  4730 THR B OG1 1 
ATOM   3723 C  CG2 . THR B 1 255 ? 30.555  31.923  -6.000  1.00 27.33 ?  4730 THR B CG2 1 
ATOM   3724 N  N   . VAL B 1 256 ? 29.813  28.627  -5.870  1.00 24.12 ?  4731 VAL B N   1 
ATOM   3725 C  CA  . VAL B 1 256 ? 28.564  27.917  -5.635  1.00 21.84 ?  4731 VAL B CA  1 
ATOM   3726 C  C   . VAL B 1 256 ? 27.732  28.665  -4.609  1.00 25.91 ?  4731 VAL B C   1 
ATOM   3727 O  O   . VAL B 1 256 ? 28.218  29.009  -3.521  1.00 23.93 ?  4731 VAL B O   1 
ATOM   3728 C  CB  . VAL B 1 256 ? 28.793  26.459  -5.204  1.00 22.15 ?  4731 VAL B CB  1 
ATOM   3729 C  CG1 . VAL B 1 256 ? 27.449  25.778  -5.005  1.00 23.86 ?  4731 VAL B CG1 1 
ATOM   3730 C  CG2 . VAL B 1 256 ? 29.636  25.732  -6.245  1.00 23.08 ?  4731 VAL B CG2 1 
ATOM   3731 N  N   . GLU B 1 257 ? 26.473  28.876  -4.945  1.00 24.93 ?  4732 GLU B N   1 
ATOM   3732 C  CA  . GLU B 1 257 ? 25.496  29.514  -4.081  1.00 24.12 ?  4732 GLU B CA  1 
ATOM   3733 C  C   . GLU B 1 257 ? 24.444  28.468  -3.731  1.00 28.25 ?  4732 GLU B C   1 
ATOM   3734 O  O   . GLU B 1 257 ? 23.660  28.048  -4.591  1.00 25.24 ?  4732 GLU B O   1 
ATOM   3735 C  CB  . GLU B 1 257 ? 24.893  30.718  -4.803  1.00 29.08 ?  4732 GLU B CB  1 
ATOM   3736 C  CG  . GLU B 1 257 ? 23.717  31.366  -4.097  1.00 34.61 ?  4732 GLU B CG  1 
ATOM   3737 C  CD  . GLU B 1 257 ? 24.061  31.940  -2.722  1.00 40.34 ?  4732 GLU B CD  1 
ATOM   3738 O  OE1 . GLU B 1 257 ? 25.256  32.024  -2.355  1.00 40.97 ?  4732 GLU B OE1 1 
ATOM   3739 O  OE2 . GLU B 1 257 ? 23.111  32.316  -1.999  1.00 42.28 -1 4732 GLU B OE2 1 
ATOM   3740 N  N   . ALA B 1 258 ? 24.447  28.035  -2.472  1.00 24.15 ?  4733 ALA B N   1 
ATOM   3741 C  CA  . ALA B 1 258 ? 23.518  27.025  -1.991  1.00 26.73 ?  4733 ALA B CA  1 
ATOM   3742 C  C   . ALA B 1 258 ? 22.273  27.686  -1.418  1.00 28.24 ?  4733 ALA B C   1 
ATOM   3743 O  O   . ALA B 1 258 ? 22.356  28.694  -0.708  1.00 29.21 ?  4733 ALA B O   1 
ATOM   3744 C  CB  . ALA B 1 258 ? 24.175  26.153  -0.918  1.00 25.31 ?  4733 ALA B CB  1 
ATOM   3745 N  N   . ILE B 1 259 ? 21.118  27.110  -1.734  1.00 27.60 ?  4734 ILE B N   1 
ATOM   3746 C  CA  . ILE B 1 259 ? 19.824  27.621  -1.298  1.00 27.85 ?  4734 ILE B CA  1 
ATOM   3747 C  C   . ILE B 1 259 ? 19.038  26.461  -0.714  1.00 32.27 ?  4734 ILE B C   1 
ATOM   3748 O  O   . ILE B 1 259 ? 18.762  25.475  -1.411  1.00 27.70 ?  4734 ILE B O   1 
ATOM   3749 C  CB  . ILE B 1 259 ? 19.045  28.260  -2.457  1.00 29.53 ?  4734 ILE B CB  1 
ATOM   3750 C  CG1 . ILE B 1 259 ? 19.793  29.471  -3.016  1.00 29.72 ?  4734 ILE B CG1 1 
ATOM   3751 C  CG2 . ILE B 1 259 ? 17.641  28.638  -1.997  1.00 31.51 ?  4734 ILE B CG2 1 
ATOM   3752 C  CD1 . ILE B 1 259 ? 19.100  30.107  -4.203  1.00 33.09 ?  4734 ILE B CD1 1 
ATOM   3753 N  N   . GLY B 1 260 ? 18.670  26.576  0.565   1.00 29.26 ?  4735 GLY B N   1 
ATOM   3754 C  CA  . GLY B 1 260 ? 17.935  25.536  1.245   1.00 30.22 ?  4735 GLY B CA  1 
ATOM   3755 C  C   . GLY B 1 260 ? 16.448  25.826  1.276   1.00 34.22 ?  4735 GLY B C   1 
ATOM   3756 O  O   . GLY B 1 260 ? 16.009  26.809  1.879   1.00 34.09 ?  4735 GLY B O   1 
ATOM   3757 N  N   . LEU B 1 261 ? 15.674  24.956  0.633   1.00 33.19 ?  4736 LEU B N   1 
ATOM   3758 C  CA  . LEU B 1 261 ? 14.222  25.073  0.609   1.00 34.00 ?  4736 LEU B CA  1 
ATOM   3759 C  C   . LEU B 1 261 ? 13.604  24.268  1.743   1.00 36.46 ?  4736 LEU B C   1 
ATOM   3760 O  O   . LEU B 1 261 ? 14.076  23.180  2.079   1.00 37.04 ?  4736 LEU B O   1 
ATOM   3761 C  CB  . LEU B 1 261 ? 13.667  24.555  -0.718  1.00 31.87 ?  4736 LEU B CB  1 
ATOM   3762 C  CG  . LEU B 1 261 ? 14.133  25.258  -1.994  1.00 34.95 ?  4736 LEU B CG  1 
ATOM   3763 C  CD1 . LEU B 1 261 ? 13.318  24.783  -3.184  1.00 34.95 ?  4736 LEU B CD1 1 
ATOM   3764 C  CD2 . LEU B 1 261 ? 14.048  26.767  -1.854  1.00 36.87 ?  4736 LEU B CD2 1 
ATOM   3765 N  N   . GLY B 1 262 ? 12.540  24.811  2.329   1.00 35.38 ?  4737 GLY B N   1 
ATOM   3766 C  CA  . GLY B 1 262 ? 11.746  24.066  3.278   1.00 33.86 ?  4737 GLY B CA  1 
ATOM   3767 C  C   . GLY B 1 262 ? 12.335  24.039  4.675   1.00 38.86 ?  4737 GLY B C   1 
ATOM   3768 O  O   . GLY B 1 262 ? 13.313  24.719  5.000   1.00 39.83 ?  4737 GLY B O   1 
ATOM   3769 N  N   . ALA B 1 263 ? 11.725  23.199  5.511   1.00 40.63 ?  4738 ALA B N   1 
ATOM   3770 C  CA  . ALA B 1 263 ? 12.003  23.173  6.940   1.00 41.78 ?  4738 ALA B CA  1 
ATOM   3771 C  C   . ALA B 1 263 ? 12.953  22.062  7.364   1.00 43.41 ?  4738 ALA B C   1 
ATOM   3772 O  O   . ALA B 1 263 ? 13.274  21.969  8.552   1.00 45.63 ?  4738 ALA B O   1 
ATOM   3773 C  CB  . ALA B 1 263 ? 10.692  23.053  7.726   1.00 44.91 ?  4738 ALA B CB  1 
ATOM   3774 N  N   . ASN B 1 264 ? 13.417  21.223  6.436   1.00 41.96 ?  4739 ASN B N   1 
ATOM   3775 C  CA  . ASN B 1 264 ? 14.207  20.045  6.779   1.00 43.67 ?  4739 ASN B CA  1 
ATOM   3776 C  C   . ASN B 1 264 ? 15.658  20.138  6.316   1.00 42.56 ?  4739 ASN B C   1 
ATOM   3777 O  O   . ASN B 1 264 ? 16.345  19.114  6.238   1.00 40.91 ?  4739 ASN B O   1 
ATOM   3778 C  CB  . ASN B 1 264 ? 13.549  18.778  6.231   1.00 44.33 ?  4739 ASN B CB  1 
ATOM   3779 C  CG  . ASN B 1 264 ? 12.253  18.447  6.937   1.00 45.22 ?  4739 ASN B CG  1 
ATOM   3780 O  OD1 . ASN B 1 264 ? 12.162  18.536  8.162   1.00 48.87 ?  4739 ASN B OD1 1 
ATOM   3781 N  ND2 . ASN B 1 264 ? 11.240  18.069  6.168   1.00 46.02 ?  4739 ASN B ND2 1 
ATOM   3782 N  N   . ILE B 1 265 ? 16.141  21.338  6.005   1.00 37.45 ?  4740 ILE B N   1 
ATOM   3783 C  CA  . ILE B 1 265 ? 17.529  21.544  5.607   1.00 37.04 ?  4740 ILE B CA  1 
ATOM   3784 C  C   . ILE B 1 265 ? 18.065  22.754  6.364   1.00 37.28 ?  4740 ILE B C   1 
ATOM   3785 O  O   . ILE B 1 265 ? 17.500  23.852  6.273   1.00 37.86 ?  4740 ILE B O   1 
ATOM   3786 C  CB  . ILE B 1 265 ? 17.691  21.691  4.079   1.00 36.91 ?  4740 ILE B CB  1 
ATOM   3787 C  CG1 . ILE B 1 265 ? 19.167  21.800  3.694   1.00 36.93 ?  4740 ILE B CG1 1 
ATOM   3788 C  CG2 . ILE B 1 265 ? 16.892  22.862  3.524   1.00 37.30 ?  4740 ILE B CG2 1 
ATOM   3789 C  CD1 . ILE B 1 265 ? 19.818  20.466  3.421   1.00 35.43 ?  4740 ILE B CD1 1 
ATOM   3790 N  N   . SER B 1 266 ? 19.133  22.550  7.128   1.00 34.33 ?  4741 SER B N   1 
ATOM   3791 C  CA  . SER B 1 266 ? 19.674  23.575  8.007   1.00 32.70 ?  4741 SER B CA  1 
ATOM   3792 C  C   . SER B 1 266 ? 20.885  24.247  7.372   1.00 33.87 ?  4741 SER B C   1 
ATOM   3793 O  O   . SER B 1 266 ? 21.461  23.766  6.388   1.00 28.78 ?  4741 SER B O   1 
ATOM   3794 C  CB  . SER B 1 266 ? 20.070  22.957  9.350   1.00 34.84 ?  4741 SER B CB  1 
ATOM   3795 O  OG  . SER B 1 266 ? 21.268  22.202  9.228   1.00 33.45 ?  4741 SER B OG  1 
ATOM   3796 N  N   . TYR B 1 267 ? 21.270  25.386  7.954   1.00 32.39 ?  4742 TYR B N   1 
ATOM   3797 C  CA  . TYR B 1 267 ? 22.527  26.014  7.573   1.00 30.86 ?  4742 TYR B CA  1 
ATOM   3798 C  C   . TYR B 1 267 ? 23.682  25.031  7.707   1.00 31.36 ?  4742 TYR B C   1 
ATOM   3799 O  O   . TYR B 1 267 ? 24.546  24.943  6.826   1.00 28.86 ?  4742 TYR B O   1 
ATOM   3800 C  CB  . TYR B 1 267 ? 22.786  27.264  8.425   1.00 28.67 ?  4742 TYR B CB  1 
ATOM   3801 C  CG  . TYR B 1 267 ? 24.124  27.908  8.123   1.00 28.69 ?  4742 TYR B CG  1 
ATOM   3802 C  CD1 . TYR B 1 267 ? 25.287  27.478  8.755   1.00 28.02 ?  4742 TYR B CD1 1 
ATOM   3803 C  CD2 . TYR B 1 267 ? 24.228  28.930  7.191   1.00 28.15 ?  4742 TYR B CD2 1 
ATOM   3804 C  CE1 . TYR B 1 267 ? 26.509  28.041  8.468   1.00 30.46 ?  4742 TYR B CE1 1 
ATOM   3805 C  CE2 . TYR B 1 267 ? 25.446  29.507  6.903   1.00 28.70 ?  4742 TYR B CE2 1 
ATOM   3806 C  CZ  . TYR B 1 267 ? 26.583  29.062  7.544   1.00 30.20 ?  4742 TYR B CZ  1 
ATOM   3807 O  OH  . TYR B 1 267 ? 27.800  29.635  7.253   1.00 31.72 ?  4742 TYR B OH  1 
ATOM   3808 N  N   . ASN B 1 268 ? 23.707  24.270  8.801   1.00 31.00 ?  4743 ASN B N   1 
ATOM   3809 C  CA  . ASN B 1 268 ? 24.807  23.342  9.019   1.00 30.91 ?  4743 ASN B CA  1 
ATOM   3810 C  C   . ASN B 1 268 ? 24.831  22.245  7.963   1.00 31.42 ?  4743 ASN B C   1 
ATOM   3811 O  O   . ASN B 1 268 ? 25.910  21.767  7.593   1.00 31.28 ?  4743 ASN B O   1 
ATOM   3812 C  CB  . ASN B 1 268 ? 24.720  22.744  10.422  1.00 32.95 ?  4743 ASN B CB  1 
ATOM   3813 C  CG  . ASN B 1 268 ? 26.026  22.121  10.859  1.00 40.32 ?  4743 ASN B CG  1 
ATOM   3814 O  OD1 . ASN B 1 268 ? 26.961  22.825  11.246  1.00 41.84 ?  4743 ASN B OD1 1 
ATOM   3815 N  ND2 . ASN B 1 268 ? 26.105  20.797  10.789  1.00 42.70 ?  4743 ASN B ND2 1 
ATOM   3816 N  N   . ASP B 1 269 ? 23.659  21.841  7.468   1.00 29.89 ?  4744 ASP B N   1 
ATOM   3817 C  CA  . ASP B 1 269 ? 23.602  20.842  6.403   1.00 27.05 ?  4744 ASP B CA  1 
ATOM   3818 C  C   . ASP B 1 269 ? 24.235  21.353  5.113   1.00 30.53 ?  4744 ASP B C   1 
ATOM   3819 O  O   . ASP B 1 269 ? 24.759  20.559  4.323   1.00 28.89 ?  4744 ASP B O   1 
ATOM   3820 C  CB  . ASP B 1 269 ? 22.149  20.441  6.130   1.00 30.82 ?  4744 ASP B CB  1 
ATOM   3821 C  CG  . ASP B 1 269 ? 21.501  19.709  7.299   1.00 35.07 ?  4744 ASP B CG  1 
ATOM   3822 O  OD1 . ASP B 1 269 ? 22.232  19.119  8.127   1.00 36.51 ?  4744 ASP B OD1 1 
ATOM   3823 O  OD2 . ASP B 1 269 ? 20.251  19.714  7.377   1.00 33.98 -1 4744 ASP B OD2 1 
ATOM   3824 N  N   . LEU B 1 270 ? 24.192  22.663  4.873   1.00 26.92 ?  4745 LEU B N   1 
ATOM   3825 C  CA  . LEU B 1 270 ? 24.617  23.224  3.598   1.00 24.69 ?  4745 LEU B CA  1 
ATOM   3826 C  C   . LEU B 1 270 ? 25.967  23.929  3.633   1.00 25.03 ?  4745 LEU B C   1 
ATOM   3827 O  O   . LEU B 1 270 ? 26.448  24.339  2.574   1.00 25.62 ?  4745 LEU B O   1 
ATOM   3828 C  CB  . LEU B 1 270 ? 23.551  24.186  3.048   1.00 26.48 ?  4745 LEU B CB  1 
ATOM   3829 C  CG  . LEU B 1 270 ? 22.315  23.522  2.446   1.00 27.32 ?  4745 LEU B CG  1 
ATOM   3830 C  CD1 . LEU B 1 270 ? 21.319  24.571  1.971   1.00 28.55 ?  4745 LEU B CD1 1 
ATOM   3831 C  CD2 . LEU B 1 270 ? 22.722  22.611  1.284   1.00 26.89 ?  4745 LEU B CD2 1 
ATOM   3832 N  N   . LYS B 1 271 ? 26.598  24.065  4.809   1.00 24.54 ?  4746 LYS B N   1 
ATOM   3833 C  CA  . LYS B 1 271 ? 27.812  24.871  4.915   1.00 26.09 ?  4746 LYS B CA  1 
ATOM   3834 C  C   . LYS B 1 271 ? 28.952  24.331  4.060   1.00 25.45 ?  4746 LYS B C   1 
ATOM   3835 O  O   . LYS B 1 271 ? 29.796  25.105  3.597   1.00 25.88 ?  4746 LYS B O   1 
ATOM   3836 C  CB  . LYS B 1 271 ? 28.246  25.007  6.380   1.00 27.26 ?  4746 LYS B CB  1 
ATOM   3837 C  CG  . LYS B 1 271 ? 28.704  23.694  7.029   1.00 29.39 ?  4746 LYS B CG  1 
ATOM   3838 C  CD  . LYS B 1 271 ? 29.056  23.871  8.507   1.00 29.77 ?  4746 LYS B CD  1 
ATOM   3839 C  CE  . LYS B 1 271 ? 29.424  22.536  9.144   1.00 33.19 ?  4746 LYS B CE  1 
ATOM   3840 N  NZ  . LYS B 1 271 ? 29.712  22.666  10.599  1.00 34.67 ?  4746 LYS B NZ  1 
ATOM   3841 N  N   . SER B 1 272 ? 28.998  23.015  3.830   1.00 25.47 ?  4747 SER B N   1 
ATOM   3842 C  CA  . SER B 1 272 ? 30.072  22.441  3.031   1.00 26.36 ?  4747 SER B CA  1 
ATOM   3843 C  C   . SER B 1 272 ? 29.875  22.648  1.539   1.00 24.43 ?  4747 SER B C   1 
ATOM   3844 O  O   . SER B 1 272 ? 30.799  22.367  0.769   1.00 22.54 ?  4747 SER B O   1 
ATOM   3845 C  CB  . SER B 1 272 ? 30.200  20.939  3.298   1.00 28.11 ?  4747 SER B CB  1 
ATOM   3846 O  OG  . SER B 1 272 ? 30.535  20.690  4.648   1.00 30.69 ?  4747 SER B OG  1 
ATOM   3847 N  N   . TYR B 1 273 ? 28.710  23.144  1.118   1.00 23.16 ?  4748 TYR B N   1 
ATOM   3848 C  CA  . TYR B 1 273 ? 28.349  23.201  -0.294  1.00 23.35 ?  4748 TYR B CA  1 
ATOM   3849 C  C   . TYR B 1 273 ? 28.084  24.626  -0.758  1.00 23.40 ?  4748 TYR B C   1 
ATOM   3850 O  O   . TYR B 1 273 ? 27.321  24.847  -1.699  1.00 22.38 ?  4748 TYR B O   1 
ATOM   3851 C  CB  . TYR B 1 273 ? 27.155  22.293  -0.585  1.00 20.76 ?  4748 TYR B CB  1 
ATOM   3852 C  CG  . TYR B 1 273 ? 27.309  20.934  0.063   1.00 21.97 ?  4748 TYR B CG  1 
ATOM   3853 C  CD1 . TYR B 1 273 ? 28.188  19.988  -0.458  1.00 21.32 ?  4748 TYR B CD1 1 
ATOM   3854 C  CD2 . TYR B 1 273 ? 26.598  20.606  1.207   1.00 21.76 ?  4748 TYR B CD2 1 
ATOM   3855 C  CE1 . TYR B 1 273 ? 28.337  18.742  0.144   1.00 20.07 ?  4748 TYR B CE1 1 
ATOM   3856 C  CE2 . TYR B 1 273 ? 26.743  19.362  1.822   1.00 22.63 ?  4748 TYR B CE2 1 
ATOM   3857 C  CZ  . TYR B 1 273 ? 27.614  18.438  1.280   1.00 23.11 ?  4748 TYR B CZ  1 
ATOM   3858 O  OH  . TYR B 1 273 ? 27.761  17.210  1.889   1.00 22.26 ?  4748 TYR B OH  1 
ATOM   3859 N  N   . ASP B 1 274 ? 28.719  25.603  -0.115  1.00 23.67 ?  4749 ASP B N   1 
ATOM   3860 C  CA  . ASP B 1 274 ? 28.501  27.006  -0.441  1.00 26.53 ?  4749 ASP B CA  1 
ATOM   3861 C  C   . ASP B 1 274 ? 29.817  27.758  -0.309  1.00 27.15 ?  4749 ASP B C   1 
ATOM   3862 O  O   . ASP B 1 274 ? 30.540  27.589  0.675   1.00 27.41 ?  4749 ASP B O   1 
ATOM   3863 C  CB  . ASP B 1 274 ? 27.426  27.613  0.464   1.00 23.61 ?  4749 ASP B CB  1 
ATOM   3864 C  CG  . ASP B 1 274 ? 27.169  29.085  0.171   1.00 31.19 ?  4749 ASP B CG  1 
ATOM   3865 O  OD1 . ASP B 1 274 ? 27.963  29.930  0.648   1.00 28.28 ?  4749 ASP B OD1 1 
ATOM   3866 O  OD2 . ASP B 1 274 ? 26.181  29.391  -0.535  1.00 24.54 -1 4749 ASP B OD2 1 
ATOM   3867 N  N   . SER B 1 275 ? 30.112  28.608  -1.297  1.00 25.65 ?  4750 SER B N   1 
ATOM   3868 C  CA  . SER B 1 275 ? 31.462  29.142  -1.443  1.00 26.45 ?  4750 SER B CA  1 
ATOM   3869 C  C   . SER B 1 275 ? 31.805  30.217  -0.415  1.00 28.97 ?  4750 SER B C   1 
ATOM   3870 O  O   . SER B 1 275 ? 32.989  30.408  -0.113  1.00 30.58 ?  4750 SER B O   1 
ATOM   3871 C  CB  . SER B 1 275 ? 31.662  29.692  -2.852  1.00 26.45 ?  4750 SER B CB  1 
ATOM   3872 O  OG  . SER B 1 275 ? 31.801  28.635  -3.778  1.00 27.07 ?  4750 SER B OG  1 
ATOM   3873 N  N   . ASP B 1 276 ? 30.819  30.946  0.105   1.00 26.60 ?  4751 ASP B N   1 
ATOM   3874 C  CA  . ASP B 1 276 ? 31.111  32.066  1.000   1.00 32.50 ?  4751 ASP B CA  1 
ATOM   3875 C  C   . ASP B 1 276 ? 30.543  31.935  2.407   1.00 33.42 ?  4751 ASP B C   1 
ATOM   3876 O  O   . ASP B 1 276 ? 30.780  32.823  3.236   1.00 33.93 ?  4751 ASP B O   1 
ATOM   3877 C  CB  . ASP B 1 276 ? 30.687  33.411  0.382   1.00 31.22 ?  4751 ASP B CB  1 
ATOM   3878 C  CG  . ASP B 1 276 ? 29.181  33.568  0.269   1.00 33.43 ?  4751 ASP B CG  1 
ATOM   3879 O  OD1 . ASP B 1 276 ? 28.437  32.630  0.601   1.00 31.55 ?  4751 ASP B OD1 1 
ATOM   3880 O  OD2 . ASP B 1 276 ? 28.733  34.654  -0.164  1.00 39.99 -1 4751 ASP B OD2 1 
ATOM   3881 N  N   . GLY B 1 277 ? 29.797  30.877  2.705   1.00 28.19 ?  4752 GLY B N   1 
ATOM   3882 C  CA  . GLY B 1 277 ? 29.246  30.717  4.032   1.00 31.01 ?  4752 GLY B CA  1 
ATOM   3883 C  C   . GLY B 1 277 ? 28.010  31.539  4.332   1.00 32.51 ?  4752 GLY B C   1 
ATOM   3884 O  O   . GLY B 1 277 ? 27.461  31.412  5.436   1.00 31.89 ?  4752 GLY B O   1 
ATOM   3885 N  N   . VAL B 1 278 ? 27.566  32.390  3.412   1.00 30.28 ?  4753 VAL B N   1 
ATOM   3886 C  CA  . VAL B 1 278 ? 26.280  33.064  3.543   1.00 31.41 ?  4753 VAL B CA  1 
ATOM   3887 C  C   . VAL B 1 278 ? 25.252  32.206  2.824   1.00 29.68 ?  4753 VAL B C   1 
ATOM   3888 O  O   . VAL B 1 278 ? 25.333  32.024  1.604   1.00 31.22 ?  4753 VAL B O   1 
ATOM   3889 C  CB  . VAL B 1 278 ? 26.327  34.480  2.951   1.00 34.29 ?  4753 VAL B CB  1 
ATOM   3890 C  CG1 . VAL B 1 278 ? 25.010  35.204  3.206   1.00 32.98 ?  4753 VAL B CG1 1 
ATOM   3891 C  CG2 . VAL B 1 278 ? 27.497  35.249  3.535   1.00 33.31 ?  4753 VAL B CG2 1 
ATOM   3892 N  N   . ILE B 1 279 ? 24.295  31.664  3.574   1.00 31.32 ?  4754 ILE B N   1 
ATOM   3893 C  CA  . ILE B 1 279 ? 23.383  30.651  3.049   1.00 33.40 ?  4754 ILE B CA  1 
ATOM   3894 C  C   . ILE B 1 279 ? 21.976  30.942  3.546   1.00 31.67 ?  4754 ILE B C   1 
ATOM   3895 O  O   . ILE B 1 279 ? 21.744  31.031  4.756   1.00 34.70 ?  4754 ILE B O   1 
ATOM   3896 C  CB  . ILE B 1 279 ? 23.804  29.227  3.468   1.00 26.99 ?  4754 ILE B CB  1 
ATOM   3897 C  CG1 . ILE B 1 279 ? 25.281  28.981  3.140   1.00 29.16 ?  4754 ILE B CG1 1 
ATOM   3898 C  CG2 . ILE B 1 279 ? 22.924  28.202  2.788   1.00 29.20 ?  4754 ILE B CG2 1 
ATOM   3899 C  CD1 . ILE B 1 279 ? 25.853  27.732  3.775   1.00 29.84 ?  4754 ILE B CD1 1 
ATOM   3900 N  N   . MET B 1 280 ? 21.033  31.053  2.615   1.00 32.57 ?  4755 MET B N   1 
ATOM   3901 C  CA  . MET B 1 280 ? 19.622  31.198  2.943   1.00 33.41 ?  4755 MET B CA  1 
ATOM   3902 C  C   . MET B 1 280 ? 19.005  29.814  3.089   1.00 37.11 ?  4755 MET B C   1 
ATOM   3903 O  O   . MET B 1 280 ? 19.059  29.004  2.155   1.00 35.67 ?  4755 MET B O   1 
ATOM   3904 C  CB  . MET B 1 280 ? 18.900  31.964  1.838   1.00 37.50 ?  4755 MET B CB  1 
ATOM   3905 C  CG  . MET B 1 280 ? 19.401  33.380  1.633   1.00 39.74 ?  4755 MET B CG  1 
ATOM   3906 S  SD  . MET B 1 280 ? 18.493  34.237  0.332   1.00 46.84 ?  4755 MET B SD  1 
ATOM   3907 C  CE  . MET B 1 280 ? 16.807  34.032  0.898   1.00 39.24 ?  4755 MET B CE  1 
ATOM   3908 N  N   . THR B 1 281 ? 18.431  29.543  4.257   1.00 34.52 ?  4756 THR B N   1 
ATOM   3909 C  CA  . THR B 1 281 ? 17.720  28.303  4.526   1.00 37.94 ?  4756 THR B CA  1 
ATOM   3910 C  C   . THR B 1 281 ? 16.270  28.621  4.861   1.00 37.92 ?  4756 THR B C   1 
ATOM   3911 O  O   . THR B 1 281 ? 15.902  29.773  5.105   1.00 41.32 ?  4756 THR B O   1 
ATOM   3912 C  CB  . THR B 1 281 ? 18.377  27.510  5.666   1.00 36.30 ?  4756 THR B CB  1 
ATOM   3913 O  OG1 . THR B 1 281 ? 18.575  28.364  6.802   1.00 38.55 ?  4756 THR B OG1 1 
ATOM   3914 C  CG2 . THR B 1 281 ? 19.715  26.949  5.220   1.00 34.69 ?  4756 THR B CG2 1 
ATOM   3915 N  N   . GLY B 1 282 ? 15.442  27.581  4.870   1.00 37.68 ?  4757 GLY B N   1 
ATOM   3916 C  CA  . GLY B 1 282 ? 14.023  27.781  5.079   1.00 37.14 ?  4757 GLY B CA  1 
ATOM   3917 C  C   . GLY B 1 282 ? 13.339  28.587  4.001   1.00 39.41 ?  4757 GLY B C   1 
ATOM   3918 O  O   . GLY B 1 282 ? 12.242  29.104  4.230   1.00 40.58 ?  4757 GLY B O   1 
ATOM   3919 N  N   . VAL B 1 283 ? 13.964  28.720  2.832   1.00 37.20 ?  4758 VAL B N   1 
ATOM   3920 C  CA  . VAL B 1 283 ? 13.369  29.463  1.726   1.00 37.70 ?  4758 VAL B CA  1 
ATOM   3921 C  C   . VAL B 1 283 ? 12.146  28.706  1.229   1.00 40.10 ?  4758 VAL B C   1 
ATOM   3922 O  O   . VAL B 1 283 ? 12.226  27.524  0.876   1.00 40.03 ?  4758 VAL B O   1 
ATOM   3923 C  CB  . VAL B 1 283 ? 14.387  29.668  0.596   1.00 37.70 ?  4758 VAL B CB  1 
ATOM   3924 C  CG1 . VAL B 1 283 ? 13.708  30.274  -0.631  1.00 38.43 ?  4758 VAL B CG1 1 
ATOM   3925 C  CG2 . VAL B 1 283 ? 15.551  30.538  1.067   1.00 37.06 ?  4758 VAL B CG2 1 
ATOM   3926 N  N   . ASN B 1 284 ? 11.003  29.381  1.200   1.00 42.38 ?  4759 ASN B N   1 
ATOM   3927 C  CA  . ASN B 1 284 ? 9.803   28.758  0.672   1.00 41.34 ?  4759 ASN B CA  1 
ATOM   3928 C  C   . ASN B 1 284 ? 9.886   28.685  -0.850  1.00 41.03 ?  4759 ASN B C   1 
ATOM   3929 O  O   . ASN B 1 284 ? 10.548  29.502  -1.496  1.00 41.37 ?  4759 ASN B O   1 
ATOM   3930 C  CB  . ASN B 1 284 ? 8.571   29.555  1.094   1.00 45.33 ?  4759 ASN B CB  1 
ATOM   3931 C  CG  . ASN B 1 284 ? 7.292   28.759  0.957   1.00 48.59 ?  4759 ASN B CG  1 
ATOM   3932 O  OD1 . ASN B 1 284 ? 6.862   28.091  1.898   1.00 53.40 ?  4759 ASN B OD1 1 
ATOM   3933 N  ND2 . ASN B 1 284 ? 6.675   28.823  -0.220  1.00 50.12 ?  4759 ASN B ND2 1 
ATOM   3934 N  N   . ALA B 1 285 ? 9.214   27.678  -1.420  1.00 42.73 ?  4760 ALA B N   1 
ATOM   3935 C  CA  . ALA B 1 285 ? 9.239   27.498  -2.870  1.00 41.30 ?  4760 ALA B CA  1 
ATOM   3936 C  C   . ALA B 1 285 ? 8.756   28.743  -3.600  1.00 41.74 ?  4760 ALA B C   1 
ATOM   3937 O  O   . ALA B 1 285 ? 9.262   29.064  -4.683  1.00 38.53 ?  4760 ALA B O   1 
ATOM   3938 C  CB  . ALA B 1 285 ? 8.393   26.287  -3.269  1.00 41.03 ?  4760 ALA B CB  1 
ATOM   3939 N  N   . SER B 1 286 ? 7.792   29.462  -3.020  1.00 41.76 ?  4761 SER B N   1 
ATOM   3940 C  CA  . SER B 1 286 ? 7.249   30.664  -3.638  1.00 41.52 ?  4761 SER B CA  1 
ATOM   3941 C  C   . SER B 1 286 ? 8.235   31.823  -3.655  1.00 41.67 ?  4761 SER B C   1 
ATOM   3942 O  O   . SER B 1 286 ? 8.004   32.794  -4.384  1.00 40.57 ?  4761 SER B O   1 
ATOM   3943 C  CB  . SER B 1 286 ? 5.980   31.097  -2.903  1.00 41.53 ?  4761 SER B CB  1 
ATOM   3944 O  OG  . SER B 1 286 ? 5.059   30.026  -2.811  1.00 47.27 ?  4761 SER B OG  1 
ATOM   3945 N  N   . ASP B 1 287 ? 9.316   31.748  -2.880  1.00 40.59 ?  4762 ASP B N   1 
ATOM   3946 C  CA  . ASP B 1 287 ? 10.292  32.825  -2.786  1.00 40.60 ?  4762 ASP B CA  1 
ATOM   3947 C  C   . ASP B 1 287 ? 11.602  32.494  -3.488  1.00 40.79 ?  4762 ASP B C   1 
ATOM   3948 O  O   . ASP B 1 287 ? 12.594  33.206  -3.293  1.00 36.65 ?  4762 ASP B O   1 
ATOM   3949 C  CB  . ASP B 1 287 ? 10.556  33.179  -1.320  1.00 42.32 ?  4762 ASP B CB  1 
ATOM   3950 C  CG  . ASP B 1 287 ? 9.277   33.448  -0.538  1.00 46.26 ?  4762 ASP B CG  1 
ATOM   3951 O  OD1 . ASP B 1 287 ? 8.242   33.773  -1.159  1.00 47.12 ?  4762 ASP B OD1 1 
ATOM   3952 O  OD2 . ASP B 1 287 ? 9.313   33.338  0.706   1.00 49.49 -1 4762 ASP B OD2 1 
ATOM   3953 N  N   . LEU B 1 288 ? 11.627  31.438  -4.309  1.00 39.98 ?  4763 LEU B N   1 
ATOM   3954 C  CA  . LEU B 1 288 ? 12.888  30.978  -4.886  1.00 37.35 ?  4763 LEU B CA  1 
ATOM   3955 C  C   . LEU B 1 288 ? 13.494  32.019  -5.819  1.00 35.72 ?  4763 LEU B C   1 
ATOM   3956 O  O   . LEU B 1 288 ? 14.704  32.267  -5.776  1.00 37.69 ?  4763 LEU B O   1 
ATOM   3957 C  CB  . LEU B 1 288 ? 12.686  29.646  -5.611  1.00 34.88 ?  4763 LEU B CB  1 
ATOM   3958 C  CG  . LEU B 1 288 ? 13.922  29.090  -6.322  1.00 35.58 ?  4763 LEU B CG  1 
ATOM   3959 C  CD1 . LEU B 1 288 ? 15.077  28.904  -5.344  1.00 34.01 ?  4763 LEU B CD1 1 
ATOM   3960 C  CD2 . LEU B 1 288 ? 13.592  27.784  -7.032  1.00 32.79 ?  4763 LEU B CD2 1 
ATOM   3961 N  N   . ALA B 1 289 ? 12.672  32.634  -6.674  1.00 36.45 ?  4764 ALA B N   1 
ATOM   3962 C  CA  . ALA B 1 289 ? 13.200  33.627  -7.604  1.00 36.27 ?  4764 ALA B CA  1 
ATOM   3963 C  C   . ALA B 1 289 ? 13.806  34.811  -6.862  1.00 38.12 ?  4764 ALA B C   1 
ATOM   3964 O  O   . ALA B 1 289 ? 14.855  35.332  -7.262  1.00 37.51 ?  4764 ALA B O   1 
ATOM   3965 C  CB  . ALA B 1 289 ? 12.110  34.081  -8.576  1.00 35.88 ?  4764 ALA B CB  1 
ATOM   3966 N  N   . ASN B 1 290 ? 13.170  35.238  -5.769  1.00 38.33 ?  4765 ASN B N   1 
ATOM   3967 C  CA  . ASN B 1 290 ? 13.728  36.326  -4.971  1.00 41.89 ?  4765 ASN B CA  1 
ATOM   3968 C  C   . ASN B 1 290 ? 15.006  35.904  -4.258  1.00 40.17 ?  4765 ASN B C   1 
ATOM   3969 O  O   . ASN B 1 290 ? 15.922  36.716  -4.102  1.00 40.32 ?  4765 ASN B O   1 
ATOM   3970 C  CB  . ASN B 1 290 ? 12.690  36.853  -3.977  1.00 43.25 ?  4765 ASN B CB  1 
ATOM   3971 C  CG  . ASN B 1 290 ? 11.713  37.833  -4.614  1.00 46.08 ?  4765 ASN B CG  1 
ATOM   3972 O  OD1 . ASN B 1 290 ? 11.983  38.393  -5.679  1.00 46.99 ?  4765 ASN B OD1 1 
ATOM   3973 N  ND2 . ASN B 1 290 ? 10.576  38.049  -3.959  1.00 47.07 ?  4765 ASN B ND2 1 
ATOM   3974 N  N   . ALA B 1 291 ? 15.095  34.641  -3.831  1.00 38.99 ?  4766 ALA B N   1 
ATOM   3975 C  CA  . ALA B 1 291 ? 16.337  34.159  -3.236  1.00 38.40 ?  4766 ALA B CA  1 
ATOM   3976 C  C   . ALA B 1 291 ? 17.478  34.154  -4.249  1.00 39.23 ?  4766 ALA B C   1 
ATOM   3977 O  O   . ALA B 1 291 ? 18.639  34.357  -3.876  1.00 37.21 ?  4766 ALA B O   1 
ATOM   3978 C  CB  . ALA B 1 291 ? 16.132  32.765  -2.641  1.00 36.74 ?  4766 ALA B CB  1 
ATOM   3979 N  N   . ILE B 1 292 ? 17.169  33.931  -5.524  1.00 38.33 ?  4767 ILE B N   1 
ATOM   3980 C  CA  . ILE B 1 292 ? 18.189  33.883  -6.570  1.00 37.02 ?  4767 ILE B CA  1 
ATOM   3981 C  C   . ILE B 1 292 ? 18.529  35.274  -7.083  1.00 36.23 ?  4767 ILE B C   1 
ATOM   3982 O  O   . ILE B 1 292 ? 19.703  35.630  -7.217  1.00 38.24 ?  4767 ILE B O   1 
ATOM   3983 C  CB  . ILE B 1 292 ? 17.734  32.952  -7.715  1.00 36.56 ?  4767 ILE B CB  1 
ATOM   3984 C  CG1 . ILE B 1 292 ? 17.566  31.519  -7.210  1.00 37.58 ?  4767 ILE B CG1 1 
ATOM   3985 C  CG2 . ILE B 1 292 ? 18.714  33.012  -8.879  1.00 35.32 ?  4767 ILE B CG2 1 
ATOM   3986 C  CD1 . ILE B 1 292 ? 16.889  30.609  -8.203  1.00 34.32 ?  4767 ILE B CD1 1 
ATOM   3987 N  N   . LEU B 1 293 ? 17.507  36.078  -7.380  1.00 38.83 ?  4768 LEU B N   1 
ATOM   3988 C  CA  . LEU B 1 293 ? 17.698  37.381  -8.003  1.00 38.80 ?  4768 LEU B CA  1 
ATOM   3989 C  C   . LEU B 1 293 ? 17.687  38.538  -7.012  1.00 36.73 ?  4768 LEU B C   1 
ATOM   3990 O  O   . LEU B 1 293 ? 18.231  39.603  -7.325  1.00 38.55 ?  4768 LEU B O   1 
ATOM   3991 C  CB  . LEU B 1 293 ? 16.604  37.625  -9.051  1.00 37.50 ?  4768 LEU B CB  1 
ATOM   3992 C  CG  . LEU B 1 293 ? 16.455  36.605  -10.183 1.00 36.98 ?  4768 LEU B CG  1 
ATOM   3993 C  CD1 . LEU B 1 293 ? 15.133  36.805  -10.901 1.00 36.69 ?  4768 LEU B CD1 1 
ATOM   3994 C  CD2 . LEU B 1 293 ? 17.613  36.708  -11.159 1.00 37.20 ?  4768 LEU B CD2 1 
ATOM   3995 N  N   . GLY B 1 294 ? 17.100  38.354  -5.838  1.00 37.79 ?  4769 GLY B N   1 
ATOM   3996 C  CA  . GLY B 1 294 ? 16.872  39.439  -4.910  1.00 36.25 ?  4769 GLY B CA  1 
ATOM   3997 C  C   . GLY B 1 294 ? 15.457  39.979  -5.024  1.00 37.42 ?  4769 GLY B C   1 
ATOM   3998 O  O   . GLY B 1 294 ? 14.750  39.759  -6.010  1.00 38.16 ?  4769 GLY B O   1 
ATOM   3999 N  N   . THR B 1 295 ? 15.028  40.686  -3.978  1.00 37.93 ?  4770 THR B N   1 
ATOM   4000 C  CA  . THR B 1 295 ? 13.729  41.344  -4.034  1.00 38.52 ?  4770 THR B CA  1 
ATOM   4001 C  C   . THR B 1 295 ? 13.741  42.375  -5.159  1.00 31.12 ?  4770 THR B C   1 
ATOM   4002 O  O   . THR B 1 295 ? 14.754  43.034  -5.417  1.00 31.80 ?  4770 THR B O   1 
ATOM   4003 C  CB  . THR B 1 295 ? 13.400  42.002  -2.692  1.00 37.57 ?  4770 THR B CB  1 
ATOM   4004 O  OG1 . THR B 1 295 ? 13.548  41.037  -1.643  1.00 43.30 ?  4770 THR B OG1 1 
ATOM   4005 C  CG2 . THR B 1 295 ? 11.965  42.502  -2.680  1.00 36.56 ?  4770 THR B CG2 1 
ATOM   4006 N  N   . SER B 1 296 ? 12.629  42.461  -5.877  1.00 30.36 ?  4771 SER B N   1 
ATOM   4007 C  CA  . SER B 1 296 ? 12.583  43.294  -7.069  1.00 27.87 ?  4771 SER B CA  1 
ATOM   4008 C  C   . SER B 1 296 ? 12.492  44.751  -6.644  1.00 26.30 ?  4771 SER B C   1 
ATOM   4009 O  O   . SER B 1 296 ? 11.460  45.194  -6.132  1.00 23.64 ?  4771 SER B O   1 
ATOM   4010 C  CB  . SER B 1 296 ? 11.393  42.905  -7.939  1.00 33.82 ?  4771 SER B CB  1 
ATOM   4011 O  OG  . SER B 1 296 ? 10.178  43.336  -7.357  1.00 39.07 ?  4771 SER B OG  1 
ATOM   4012 N  N   . VAL B 1 297 ? 13.586  45.483  -6.813  1.00 22.22 ?  4772 VAL B N   1 
ATOM   4013 C  CA  . VAL B 1 297 ? 13.564  46.937  -6.744  1.00 20.52 ?  4772 VAL B CA  1 
ATOM   4014 C  C   . VAL B 1 297 ? 14.224  47.467  -8.004  1.00 20.44 ?  4772 VAL B C   1 
ATOM   4015 O  O   . VAL B 1 297 ? 15.135  46.844  -8.560  1.00 19.57 ?  4772 VAL B O   1 
ATOM   4016 C  CB  . VAL B 1 297 ? 14.246  47.506  -5.483  1.00 23.18 ?  4772 VAL B CB  1 
ATOM   4017 C  CG1 . VAL B 1 297 ? 13.524  47.020  -4.233  1.00 24.64 ?  4772 VAL B CG1 1 
ATOM   4018 C  CG2 . VAL B 1 297 ? 15.713  47.124  -5.439  1.00 23.00 ?  4772 VAL B CG2 1 
ATOM   4019 N  N   . ASN B 1 298 ? 13.757  48.621  -8.457  1.00 18.11 ?  4773 ASN B N   1 
ATOM   4020 C  CA  . ASN B 1 298 ? 14.326  49.195  -9.670  1.00 17.04 ?  4773 ASN B CA  1 
ATOM   4021 C  C   . ASN B 1 298 ? 14.221  50.702  -9.751  1.00 21.15 ?  4773 ASN B C   1 
ATOM   4022 O  O   . ASN B 1 298 ? 14.631  51.269  -10.766 1.00 14.12 ?  4773 ASN B O   1 
ATOM   4023 C  CB  . ASN B 1 298 ? 13.716  48.549  -10.917 1.00 18.16 ?  4773 ASN B CB  1 
ATOM   4024 C  CG  . ASN B 1 298 ? 12.212  48.549  -10.892 1.00 20.94 ?  4773 ASN B CG  1 
ATOM   4025 O  OD1 . ASN B 1 298 ? 11.578  49.602  -10.814 1.00 20.83 ?  4773 ASN B OD1 1 
ATOM   4026 N  ND2 . ASN B 1 298 ? 11.618  47.356  -10.958 1.00 25.97 ?  4773 ASN B ND2 1 
HETATM 4027 CA CA  . CA  C 2 .   ? 12.831  -26.180 7.850   1.00 12.04 ?  4801 CA  A CA  1 
HETATM 4028 CA CA  . CA  D 2 .   ? 21.329  -24.855 11.682  1.00 13.71 ?  4802 CA  A CA  1 
HETATM 4029 CA CA  . CA  E 2 .   ? 20.110  -26.544 18.188  1.00 18.50 ?  4803 CA  A CA  1 
HETATM 4030 CA CA  . CA  F 2 .   ? 26.919  -15.558 -2.680  1.00 12.41 ?  4804 CA  A CA  1 
HETATM 4031 CA CA  . CA  G 2 .   ? 28.892  -28.157 -27.038 1.00 17.29 ?  4805 CA  A CA  1 
HETATM 4032 CA CA  . CA  H 2 .   ? 20.879  -5.468  18.411  1.00 16.90 ?  4806 CA  A CA  1 
HETATM 4033 CA CA  . CA  I 2 .   ? 33.040  -17.743 -15.267 1.00 15.88 ?  4801 CA  B CA  1 
HETATM 4034 CA CA  . CA  J 2 .   ? 14.389  15.598  -0.170  1.00 32.48 ?  4802 CA  B CA  1 
HETATM 4035 CA CA  . CA  K 2 .   ? 12.656  13.767  -9.317  1.00 26.90 ?  4803 CA  B CA  1 
HETATM 4036 CA CA  . CA  L 2 .   ? 31.873  8.257   -4.797  1.00 17.27 ?  4804 CA  B CA  1 
HETATM 4037 CA CA  . CA  M 2 .   ? 26.665  31.737  -0.438  1.00 27.34 ?  4805 CA  B CA  1 
HETATM 4038 CA CA  . CA  N 2 .   ? 35.617  30.334  0.000   0.50 30.50 ?  4806 CA  B CA  1 
HETATM 4039 C  C1  . GOL O 3 .   ? 28.298  -20.658 -15.251 1.00 29.14 ?  4807 GOL B C1  1 
HETATM 4040 O  O1  . GOL O 3 .   ? 29.538  -20.180 -14.767 1.00 30.46 ?  4807 GOL B O1  1 
HETATM 4041 C  C2  . GOL O 3 .   ? 27.831  -21.785 -14.370 1.00 26.94 ?  4807 GOL B C2  1 
HETATM 4042 O  O2  . GOL O 3 .   ? 26.527  -21.496 -13.907 1.00 25.11 ?  4807 GOL B O2  1 
HETATM 4043 C  C3  . GOL O 3 .   ? 28.811  -21.966 -13.221 1.00 29.53 ?  4807 GOL B C3  1 
HETATM 4044 O  O3  . GOL O 3 .   ? 29.772  -22.907 -13.652 1.00 35.51 ?  4807 GOL B O3  1 
HETATM 4045 O  O   . HOH P 4 .   ? 10.479  -34.882 9.743   1.00 32.89 ?  4901 HOH A O   1 
HETATM 4046 O  O   . HOH P 4 .   ? 22.512  -18.057 21.573  1.00 26.76 ?  4902 HOH A O   1 
HETATM 4047 O  O   . HOH P 4 .   ? 20.787  -22.845 12.678  1.00 15.96 ?  4903 HOH A O   1 
HETATM 4048 O  O   . HOH P 4 .   ? 27.442  -24.229 -6.135  1.00 21.50 ?  4904 HOH A O   1 
HETATM 4049 O  O   . HOH P 4 .   ? 25.017  -26.873 -10.157 1.00 31.20 ?  4905 HOH A O   1 
HETATM 4050 O  O   . HOH P 4 .   ? 19.295  -9.664  20.405  1.00 19.32 ?  4906 HOH A O   1 
HETATM 4051 O  O   . HOH P 4 .   ? 7.951   -20.270 -20.937 1.00 32.09 ?  4907 HOH A O   1 
HETATM 4052 O  O   . HOH P 4 .   ? 26.825  -6.910  -0.084  1.00 30.17 ?  4908 HOH A O   1 
HETATM 4053 O  O   . HOH P 4 .   ? 24.972  -27.377 -16.554 1.00 27.37 ?  4909 HOH A O   1 
HETATM 4054 O  O   . HOH P 4 .   ? 22.001  -22.714 19.542  1.00 13.85 ?  4910 HOH A O   1 
HETATM 4055 O  O   . HOH P 4 .   ? 4.473   -22.000 -14.082 1.00 23.95 ?  4911 HOH A O   1 
HETATM 4056 O  O   . HOH P 4 .   ? 28.791  -23.382 -26.291 1.00 20.66 ?  4912 HOH A O   1 
HETATM 4057 O  O   . HOH P 4 .   ? -2.460  1.069   6.450   1.00 30.47 ?  4913 HOH A O   1 
HETATM 4058 O  O   . HOH P 4 .   ? 8.692   -17.761 29.186  1.00 27.68 ?  4914 HOH A O   1 
HETATM 4059 O  O   . HOH P 4 .   ? 28.561  -15.444 -4.476  1.00 16.51 ?  4915 HOH A O   1 
HETATM 4060 O  O   . HOH P 4 .   ? -0.928  -10.471 2.095   1.00 31.51 ?  4916 HOH A O   1 
HETATM 4061 O  O   . HOH P 4 .   ? 19.213  -6.632  21.882  1.00 26.80 ?  4917 HOH A O   1 
HETATM 4062 O  O   . HOH P 4 .   ? 16.356  -11.887 -13.582 1.00 17.83 ?  4918 HOH A O   1 
HETATM 4063 O  O   . HOH P 4 .   ? 25.920  -13.839 -16.575 1.00 25.16 ?  4919 HOH A O   1 
HETATM 4064 O  O   . HOH P 4 .   ? 11.129  -11.441 -3.906  1.00 20.08 ?  4920 HOH A O   1 
HETATM 4065 O  O   . HOH P 4 .   ? 33.245  -9.472  20.303  1.00 26.65 ?  4921 HOH A O   1 
HETATM 4066 O  O   . HOH P 4 .   ? 9.933   -19.783 -12.845 1.00 17.06 ?  4922 HOH A O   1 
HETATM 4067 O  O   . HOH P 4 .   ? -5.370  -16.925 5.312   1.00 25.74 ?  4923 HOH A O   1 
HETATM 4068 O  O   . HOH P 4 .   ? 12.784  -5.486  20.003  1.00 25.94 ?  4924 HOH A O   1 
HETATM 4069 O  O   . HOH P 4 .   ? 14.818  -31.159 -17.877 1.00 26.38 ?  4925 HOH A O   1 
HETATM 4070 O  O   . HOH P 4 .   ? -2.660  -7.552  4.615   1.00 15.62 ?  4926 HOH A O   1 
HETATM 4071 O  O   . HOH P 4 .   ? 28.181  -7.182  8.523   1.00 22.05 ?  4927 HOH A O   1 
HETATM 4072 O  O   . HOH P 4 .   ? 32.203  -20.328 -3.330  1.00 22.86 ?  4928 HOH A O   1 
HETATM 4073 O  O   . HOH P 4 .   ? -8.586  -6.710  11.741  1.00 28.85 ?  4929 HOH A O   1 
HETATM 4074 O  O   . HOH P 4 .   ? 26.442  -27.443 -30.380 1.00 15.95 ?  4930 HOH A O   1 
HETATM 4075 O  O   . HOH P 4 .   ? 22.328  -16.079 -25.001 1.00 25.50 ?  4931 HOH A O   1 
HETATM 4076 O  O   . HOH P 4 .   ? 17.869  -29.559 2.111   1.00 25.16 ?  4932 HOH A O   1 
HETATM 4077 O  O   . HOH P 4 .   ? 20.245  -25.185 -32.723 1.00 24.67 ?  4933 HOH A O   1 
HETATM 4078 O  O   . HOH P 4 .   ? 10.621  -25.445 7.063   1.00 13.64 ?  4934 HOH A O   1 
HETATM 4079 O  O   . HOH P 4 .   ? 0.270   -2.121  3.581   1.00 23.81 ?  4935 HOH A O   1 
HETATM 4080 O  O   . HOH P 4 .   ? 19.982  -27.730 -29.606 1.00 24.34 ?  4936 HOH A O   1 
HETATM 4081 O  O   . HOH P 4 .   ? 31.748  -10.715 2.802   1.00 23.79 ?  4937 HOH A O   1 
HETATM 4082 O  O   . HOH P 4 .   ? 29.444  -12.548 13.025  1.00 20.73 ?  4938 HOH A O   1 
HETATM 4083 O  O   . HOH P 4 .   ? 6.557   -25.898 -13.492 1.00 28.57 ?  4939 HOH A O   1 
HETATM 4084 O  O   . HOH P 4 .   ? -10.100 -11.988 11.968  1.00 22.76 ?  4940 HOH A O   1 
HETATM 4085 O  O   . HOH P 4 .   ? 26.856  -5.976  15.725  1.00 21.78 ?  4941 HOH A O   1 
HETATM 4086 O  O   . HOH P 4 .   ? 14.797  -7.607  20.468  1.00 23.39 ?  4942 HOH A O   1 
HETATM 4087 O  O   . HOH P 4 .   ? 13.586  -28.003 3.989   1.00 26.56 ?  4943 HOH A O   1 
HETATM 4088 O  O   . HOH P 4 .   ? 19.315  -15.507 -2.746  1.00 19.68 ?  4944 HOH A O   1 
HETATM 4089 O  O   . HOH P 4 .   ? 13.924  -11.012 -14.535 1.00 23.83 ?  4945 HOH A O   1 
HETATM 4090 O  O   . HOH P 4 .   ? 6.432   -13.323 -10.700 1.00 16.59 ?  4946 HOH A O   1 
HETATM 4091 O  O   . HOH P 4 .   ? 24.573  -18.239 4.044   1.00 13.52 ?  4947 HOH A O   1 
HETATM 4092 O  O   . HOH P 4 .   ? 32.183  -21.333 -30.547 1.00 23.86 ?  4948 HOH A O   1 
HETATM 4093 O  O   . HOH P 4 .   ? 28.167  -21.123 -30.856 1.00 21.60 ?  4949 HOH A O   1 
HETATM 4094 O  O   . HOH P 4 .   ? 36.346  -21.317 3.102   1.00 20.61 ?  4950 HOH A O   1 
HETATM 4095 O  O   . HOH P 4 .   ? 19.741  -14.597 -19.735 1.00 19.81 ?  4951 HOH A O   1 
HETATM 4096 O  O   . HOH P 4 .   ? -2.447  0.272   11.764  1.00 22.59 ?  4952 HOH A O   1 
HETATM 4097 O  O   . HOH P 4 .   ? 25.234  -12.038 23.694  1.00 26.29 ?  4953 HOH A O   1 
HETATM 4098 O  O   . HOH P 4 .   ? 12.159  -20.424 -23.808 1.00 27.53 ?  4954 HOH A O   1 
HETATM 4099 O  O   . HOH P 4 .   ? 19.536  -4.043  19.793  1.00 20.90 ?  4955 HOH A O   1 
HETATM 4100 O  O   . HOH P 4 .   ? 26.370  -17.140 12.575  1.00 16.52 ?  4956 HOH A O   1 
HETATM 4101 O  O   . HOH P 4 .   ? 20.949  -3.045  -0.802  1.00 19.00 ?  4957 HOH A O   1 
HETATM 4102 O  O   . HOH P 4 .   ? 25.250  -2.249  2.961   1.00 32.36 ?  4958 HOH A O   1 
HETATM 4103 O  O   . HOH P 4 .   ? 21.313  -16.282 -15.724 1.00 17.72 ?  4959 HOH A O   1 
HETATM 4104 O  O   . HOH P 4 .   ? 14.692  -25.031 1.989   1.00 16.18 ?  4960 HOH A O   1 
HETATM 4105 O  O   . HOH P 4 .   ? 18.056  -26.936 19.286  1.00 19.85 ?  4961 HOH A O   1 
HETATM 4106 O  O   . HOH P 4 .   ? 22.855  -9.495  -5.623  1.00 25.14 ?  4962 HOH A O   1 
HETATM 4107 O  O   . HOH P 4 .   ? 7.928   -22.564 4.774   1.00 15.98 ?  4963 HOH A O   1 
HETATM 4108 O  O   . HOH P 4 .   ? 3.008   -4.805  20.465  1.00 26.94 ?  4964 HOH A O   1 
HETATM 4109 O  O   . HOH P 4 .   ? 26.217  -27.661 -1.846  1.00 27.88 ?  4965 HOH A O   1 
HETATM 4110 O  O   . HOH P 4 .   ? 28.262  -16.518 10.535  1.00 20.33 ?  4966 HOH A O   1 
HETATM 4111 O  O   . HOH P 4 .   ? 28.405  -25.210 11.767  1.00 28.36 ?  4967 HOH A O   1 
HETATM 4112 O  O   . HOH P 4 .   ? 20.053  -4.240  16.527  1.00 18.46 ?  4968 HOH A O   1 
HETATM 4113 O  O   . HOH P 4 .   ? 17.797  -28.251 -28.074 1.00 27.83 ?  4969 HOH A O   1 
HETATM 4114 O  O   . HOH P 4 .   ? 8.438   -14.819 26.023  1.00 18.62 ?  4970 HOH A O   1 
HETATM 4115 O  O   . HOH P 4 .   ? 29.451  -24.768 4.533   1.00 23.37 ?  4971 HOH A O   1 
HETATM 4116 O  O   . HOH P 4 .   ? 25.593  -23.885 -12.720 1.00 19.22 ?  4972 HOH A O   1 
HETATM 4117 O  O   . HOH P 4 .   ? 13.950  -20.885 -6.672  1.00 16.34 ?  4973 HOH A O   1 
HETATM 4118 O  O   . HOH P 4 .   ? 11.509  -14.886 -20.423 1.00 30.71 ?  4974 HOH A O   1 
HETATM 4119 O  O   . HOH P 4 .   ? 7.705   -27.611 22.277  1.00 26.11 ?  4975 HOH A O   1 
HETATM 4120 O  O   . HOH P 4 .   ? 25.582  -30.138 -32.796 1.00 21.37 ?  4976 HOH A O   1 
HETATM 4121 O  O   . HOH P 4 .   ? -3.511  -10.101 5.423   1.00 21.75 ?  4977 HOH A O   1 
HETATM 4122 O  O   . HOH P 4 .   ? 19.897  -4.050  -3.217  1.00 20.82 ?  4978 HOH A O   1 
HETATM 4123 O  O   . HOH P 4 .   ? -1.242  -1.457  10.052  1.00 21.45 ?  4979 HOH A O   1 
HETATM 4124 O  O   . HOH P 4 .   ? 16.412  -12.837 -17.698 1.00 18.99 ?  4980 HOH A O   1 
HETATM 4125 O  O   . HOH P 4 .   ? 5.933   7.317   10.170  1.00 30.03 ?  4981 HOH A O   1 
HETATM 4126 O  O   . HOH P 4 .   ? 21.552  -9.728  -9.702  1.00 30.79 ?  4982 HOH A O   1 
HETATM 4127 O  O   . HOH P 4 .   ? 8.803   -13.069 -0.726  1.00 28.04 ?  4983 HOH A O   1 
HETATM 4128 O  O   . HOH P 4 .   ? 1.768   -6.008  3.617   1.00 26.92 ?  4984 HOH A O   1 
HETATM 4129 O  O   . HOH P 4 .   ? -1.083  -14.413 16.062  1.00 20.88 ?  4985 HOH A O   1 
HETATM 4130 O  O   . HOH P 4 .   ? 12.040  -28.006 6.491   1.00 15.02 ?  4986 HOH A O   1 
HETATM 4131 O  O   . HOH P 4 .   ? 16.506  -16.812 27.814  1.00 23.54 ?  4987 HOH A O   1 
HETATM 4132 O  O   . HOH P 4 .   ? 0.414   -17.051 4.148   1.00 25.72 ?  4988 HOH A O   1 
HETATM 4133 O  O   . HOH P 4 .   ? 31.714  -25.920 11.132  1.00 27.32 ?  4989 HOH A O   1 
HETATM 4134 O  O   . HOH P 4 .   ? 11.907  -12.980 29.409  1.00 23.83 ?  4990 HOH A O   1 
HETATM 4135 O  O   . HOH P 4 .   ? 19.580  -15.246 -13.942 1.00 16.90 ?  4991 HOH A O   1 
HETATM 4136 O  O   . HOH P 4 .   ? 10.803  -11.477 -1.068  1.00 21.14 ?  4992 HOH A O   1 
HETATM 4137 O  O   . HOH P 4 .   ? 26.637  -22.884 15.147  1.00 24.32 ?  4993 HOH A O   1 
HETATM 4138 O  O   . HOH P 4 .   ? 21.901  -12.960 -6.118  1.00 23.36 ?  4994 HOH A O   1 
HETATM 4139 O  O   . HOH P 4 .   ? 10.047  -22.124 -22.526 1.00 29.21 ?  4995 HOH A O   1 
HETATM 4140 O  O   . HOH P 4 .   ? 12.226  -22.363 -1.744  1.00 34.36 ?  4996 HOH A O   1 
HETATM 4141 O  O   . HOH P 4 .   ? 30.340  -17.119 12.706  1.00 25.90 ?  4997 HOH A O   1 
HETATM 4142 O  O   . HOH P 4 .   ? 1.634   -3.203  -2.339  1.00 29.07 ?  4998 HOH A O   1 
HETATM 4143 O  O   . HOH P 4 .   ? 4.151   -20.909 -16.964 1.00 28.52 ?  4999 HOH A O   1 
HETATM 4144 O  O   . HOH P 4 .   ? 25.268  -11.709 -5.064  1.00 31.82 ?  5000 HOH A O   1 
HETATM 4145 O  O   . HOH P 4 .   ? -10.171 -6.596  6.956   1.00 29.59 ?  5001 HOH A O   1 
HETATM 4146 O  O   . HOH P 4 .   ? 18.062  -2.291  -4.494  1.00 26.31 ?  5002 HOH A O   1 
HETATM 4147 O  O   . HOH P 4 .   ? 27.332  -6.876  5.858   1.00 24.03 ?  5003 HOH A O   1 
HETATM 4148 O  O   . HOH P 4 .   ? -0.451  -15.747 13.686  1.00 18.15 ?  5004 HOH A O   1 
HETATM 4149 O  O   . HOH P 4 .   ? 30.084  -26.054 -2.241  1.00 28.93 ?  5005 HOH A O   1 
HETATM 4150 O  O   . HOH P 4 .   ? 21.425  -15.316 -4.706  1.00 21.45 ?  5006 HOH A O   1 
HETATM 4151 O  O   . HOH P 4 .   ? 22.140  -25.523 17.244  1.00 22.17 ?  5007 HOH A O   1 
HETATM 4152 O  O   . HOH P 4 .   ? 1.689   -20.721 16.388  1.00 23.33 ?  5008 HOH A O   1 
HETATM 4153 O  O   . HOH P 4 .   ? 23.614  -31.736 -21.937 1.00 36.54 ?  5009 HOH A O   1 
HETATM 4154 O  O   . HOH P 4 .   ? 5.144   -20.689 23.997  1.00 28.53 ?  5010 HOH A O   1 
HETATM 4155 O  O   . HOH P 4 .   ? -6.791  -15.125 3.595   1.00 30.31 ?  5011 HOH A O   1 
HETATM 4156 O  O   . HOH P 4 .   ? 25.118  -7.426  23.763  1.00 23.96 ?  5012 HOH A O   1 
HETATM 4157 O  O   . HOH P 4 .   ? 19.985  -14.946 -6.820  1.00 19.53 ?  5013 HOH A O   1 
HETATM 4158 O  O   . HOH P 4 .   ? 13.036  -10.995 -11.578 1.00 20.62 ?  5014 HOH A O   1 
HETATM 4159 O  O   . HOH P 4 .   ? 2.191   -0.223  2.896   1.00 26.61 ?  5015 HOH A O   1 
HETATM 4160 O  O   . HOH P 4 .   ? 0.147   -11.612 22.771  1.00 29.75 ?  5016 HOH A O   1 
HETATM 4161 O  O   . HOH P 4 .   ? 30.395  -17.374 -7.358  1.00 22.77 ?  5017 HOH A O   1 
HETATM 4162 O  O   . HOH P 4 .   ? 29.403  -15.344 23.225  1.00 24.34 ?  5018 HOH A O   1 
HETATM 4163 O  O   . HOH P 4 .   ? 32.193  -30.829 -29.138 1.00 30.74 ?  5019 HOH A O   1 
HETATM 4164 O  O   . HOH P 4 .   ? 14.451  2.714   9.104   0.63 21.66 ?  5020 HOH A O   1 
HETATM 4165 O  O   . HOH P 4 .   ? 27.246  -21.608 -27.920 1.00 21.25 ?  5021 HOH A O   1 
HETATM 4166 O  O   . HOH P 4 .   ? 32.110  -17.691 -2.774  1.00 18.14 ?  5022 HOH A O   1 
HETATM 4167 O  O   . HOH P 4 .   ? 22.078  -25.802 -6.811  1.00 18.23 ?  5023 HOH A O   1 
HETATM 4168 O  O   . HOH P 4 .   ? -0.260  -5.039  22.503  1.00 33.70 ?  5024 HOH A O   1 
HETATM 4169 O  O   . HOH P 4 .   ? 30.630  -29.826 -26.916 1.00 25.14 ?  5025 HOH A O   1 
HETATM 4170 O  O   . HOH P 4 .   ? 31.417  -14.581 21.365  1.00 19.16 ?  5026 HOH A O   1 
HETATM 4171 O  O   . HOH P 4 .   ? 5.645   -18.160 -0.136  1.00 23.24 ?  5027 HOH A O   1 
HETATM 4172 O  O   . HOH P 4 .   ? 22.721  -12.492 25.984  1.00 28.31 ?  5028 HOH A O   1 
HETATM 4173 O  O   . HOH P 4 .   ? 21.057  -16.932 -18.214 1.00 25.76 ?  5029 HOH A O   1 
HETATM 4174 O  O   . HOH P 4 .   ? 27.811  -24.554 -17.445 1.00 20.53 ?  5030 HOH A O   1 
HETATM 4175 O  O   . HOH P 4 .   ? 27.541  -13.361 -2.049  1.00 21.74 ?  5031 HOH A O   1 
HETATM 4176 O  O   . HOH P 4 .   ? 9.009   -29.044 13.480  1.00 12.23 ?  5032 HOH A O   1 
HETATM 4177 O  O   . HOH P 4 .   ? -6.016  -10.553 11.905  1.00 12.60 ?  5033 HOH A O   1 
HETATM 4178 O  O   . HOH P 4 .   ? 21.638  -28.425 17.579  1.00 28.86 ?  5034 HOH A O   1 
HETATM 4179 O  O   . HOH P 4 .   ? 20.667  -25.073 19.852  1.00 20.83 ?  5035 HOH A O   1 
HETATM 4180 O  O   . HOH P 4 .   ? 30.768  -27.000 -26.057 1.00 23.56 ?  5036 HOH A O   1 
HETATM 4181 O  O   . HOH P 4 .   ? 29.879  -25.507 -33.838 1.00 6.34  ?  5037 HOH A O   1 
HETATM 4182 O  O   . HOH P 4 .   ? 9.982   -27.441 -7.075  1.00 28.67 ?  5038 HOH A O   1 
HETATM 4183 O  O   . HOH P 4 .   ? 19.156  -1.753  16.711  1.00 30.50 ?  5039 HOH A O   1 
HETATM 4184 O  O   . HOH P 4 .   ? 24.778  -32.877 -31.619 1.00 22.38 ?  5040 HOH A O   1 
HETATM 4185 O  O   . HOH P 4 .   ? 23.559  -2.605  -0.748  1.00 32.95 ?  5041 HOH A O   1 
HETATM 4186 O  O   . HOH P 4 .   ? 8.931   -9.338  -1.408  1.00 25.18 ?  5042 HOH A O   1 
HETATM 4187 O  O   . HOH P 4 .   ? -1.067  -6.501  2.624   1.00 32.52 ?  5043 HOH A O   1 
HETATM 4188 O  O   . HOH P 4 .   ? 25.842  -11.268 -2.072  1.00 30.04 ?  5044 HOH A O   1 
HETATM 4189 O  O   . HOH P 4 .   ? 9.492   -26.800 5.013   1.00 29.42 ?  5045 HOH A O   1 
HETATM 4190 O  O   . HOH P 4 .   ? 20.443  -28.028 20.246  1.00 26.58 ?  5046 HOH A O   1 
HETATM 4191 O  O   . HOH P 4 .   ? 12.614  -23.637 -4.124  1.00 35.78 ?  5047 HOH A O   1 
HETATM 4192 O  O   . HOH P 4 .   ? 7.692   -24.848 3.329   1.00 24.13 ?  5048 HOH A O   1 
HETATM 4193 O  O   . HOH P 4 .   ? -1.626  -3.171  23.114  1.00 37.19 ?  5049 HOH A O   1 
HETATM 4194 O  O   . HOH P 4 .   ? 31.035  -16.446 -4.891  1.00 23.77 ?  5050 HOH A O   1 
HETATM 4195 O  O   . HOH P 4 .   ? 17.637  -13.717 -15.161 1.00 20.24 ?  5051 HOH A O   1 
HETATM 4196 O  O   . HOH P 4 .   ? -3.152  -18.196 4.334   1.00 29.34 ?  5052 HOH A O   1 
HETATM 4197 O  O   . HOH P 4 .   ? 27.117  -25.481 -11.233 1.00 34.82 ?  5053 HOH A O   1 
HETATM 4198 O  O   . HOH P 4 .   ? 20.355  0.440   15.487  1.00 35.52 ?  5054 HOH A O   1 
HETATM 4199 O  O   . HOH P 4 .   ? 23.012  -11.260 -7.872  1.00 30.47 ?  5055 HOH A O   1 
HETATM 4200 O  O   . HOH P 4 .   ? 25.984  -26.131 -14.332 1.00 30.75 ?  5056 HOH A O   1 
HETATM 4201 O  O   . HOH P 4 .   ? 19.023  -6.657  24.757  1.00 31.05 ?  5057 HOH A O   1 
HETATM 4202 O  O   . HOH P 4 .   ? 21.987  -4.230  -4.942  1.00 27.25 ?  5058 HOH A O   1 
HETATM 4203 O  O   . HOH Q 4 .   ? 33.690  7.378   -22.184 1.00 40.72 ?  4901 HOH B O   1 
HETATM 4204 O  O   . HOH Q 4 .   ? 24.364  18.940  9.348   1.00 40.81 ?  4902 HOH B O   1 
HETATM 4205 O  O   . HOH Q 4 .   ? 26.643  0.407   -4.875  1.00 29.98 ?  4903 HOH B O   1 
HETATM 4206 O  O   . HOH Q 4 .   ? 26.501  34.126  -1.147  1.00 32.91 ?  4904 HOH B O   1 
HETATM 4207 O  O   . HOH Q 4 .   ? 28.664  11.070  -11.334 1.00 30.02 ?  4905 HOH B O   1 
HETATM 4208 O  O   . HOH Q 4 .   ? 29.909  -6.413  -27.728 1.00 33.04 ?  4906 HOH B O   1 
HETATM 4209 O  O   . HOH Q 4 .   ? 28.392  -15.257 -11.072 1.00 23.80 ?  4907 HOH B O   1 
HETATM 4210 O  O   . HOH Q 4 .   ? 29.891  27.658  3.416   1.00 27.41 ?  4908 HOH B O   1 
HETATM 4211 O  O   . HOH Q 4 .   ? 27.029  -18.617 -26.904 1.00 32.22 ?  4909 HOH B O   1 
HETATM 4212 O  O   . HOH Q 4 .   ? 21.392  -10.862 -13.239 1.00 23.33 ?  4910 HOH B O   1 
HETATM 4213 O  O   . HOH Q 4 .   ? 25.440  5.223   -23.878 1.00 22.62 ?  4911 HOH B O   1 
HETATM 4214 O  O   . HOH Q 4 .   ? 28.753  -3.435  -10.542 1.00 21.80 ?  4912 HOH B O   1 
HETATM 4215 O  O   . HOH Q 4 .   ? 11.663  11.728  -10.211 1.00 29.62 ?  4913 HOH B O   1 
HETATM 4216 O  O   . HOH Q 4 .   ? 17.084  9.853   -10.681 1.00 26.85 ?  4914 HOH B O   1 
HETATM 4217 O  O   . HOH Q 4 .   ? 25.346  -7.120  -30.326 1.00 19.51 ?  4915 HOH B O   1 
HETATM 4218 O  O   . HOH Q 4 .   ? 28.366  31.315  -2.259  1.00 28.13 ?  4916 HOH B O   1 
HETATM 4219 O  O   . HOH Q 4 .   ? 16.579  16.285  -0.718  1.00 31.45 ?  4917 HOH B O   1 
HETATM 4220 O  O   . HOH Q 4 .   ? 21.441  31.205  -0.277  1.00 34.87 ?  4918 HOH B O   1 
HETATM 4221 O  O   . HOH Q 4 .   ? 13.605  21.044  3.801   1.00 38.91 ?  4919 HOH B O   1 
HETATM 4222 O  O   . HOH Q 4 .   ? 27.505  -7.971  -12.705 1.00 24.59 ?  4920 HOH B O   1 
HETATM 4223 O  O   . HOH Q 4 .   ? 25.189  -3.596  -9.057  1.00 34.18 ?  4921 HOH B O   1 
HETATM 4224 O  O   . HOH Q 4 .   ? 25.732  12.362  -2.597  1.00 19.29 ?  4922 HOH B O   1 
HETATM 4225 O  O   . HOH Q 4 .   ? 24.606  -2.448  -30.577 1.00 33.39 ?  4923 HOH B O   1 
HETATM 4226 O  O   . HOH Q 4 .   ? 23.699  -14.571 -18.306 1.00 23.67 ?  4924 HOH B O   1 
HETATM 4227 O  O   . HOH Q 4 .   ? 22.377  35.158  -6.410  1.00 38.66 ?  4925 HOH B O   1 
HETATM 4228 O  O   . HOH Q 4 .   ? 17.206  14.080  2.447   1.00 32.11 ?  4926 HOH B O   1 
HETATM 4229 O  O   . HOH Q 4 .   ? 14.622  15.491  -15.699 1.00 29.51 ?  4927 HOH B O   1 
HETATM 4230 O  O   . HOH Q 4 .   ? 35.392  28.033  -6.109  1.00 29.70 ?  4928 HOH B O   1 
HETATM 4231 O  O   . HOH Q 4 .   ? 21.031  -7.069  -21.454 1.00 19.09 ?  4929 HOH B O   1 
HETATM 4232 O  O   . HOH Q 4 .   ? 36.483  30.874  -12.773 1.00 36.48 ?  4930 HOH B O   1 
HETATM 4233 O  O   . HOH Q 4 .   ? 21.308  49.544  -19.901 1.00 16.02 ?  4931 HOH B O   1 
HETATM 4234 O  O   . HOH Q 4 .   ? 30.208  21.753  -25.282 1.00 36.01 ?  4932 HOH B O   1 
HETATM 4235 O  O   . HOH Q 4 .   ? 28.049  0.309   -30.135 1.00 33.31 ?  4933 HOH B O   1 
HETATM 4236 O  O   . HOH Q 4 .   ? 12.576  30.084  -26.408 1.00 36.97 ?  4934 HOH B O   1 
HETATM 4237 O  O   . HOH Q 4 .   ? 38.089  22.806  -5.180  1.00 35.81 ?  4935 HOH B O   1 
HETATM 4238 O  O   . HOH Q 4 .   ? 33.369  6.422   -4.237  1.00 20.35 ?  4936 HOH B O   1 
HETATM 4239 O  O   . HOH Q 4 .   ? 24.311  12.673  -18.097 1.00 32.77 ?  4937 HOH B O   1 
HETATM 4240 O  O   . HOH Q 4 .   ? 38.771  -6.901  -20.460 1.00 25.75 ?  4938 HOH B O   1 
HETATM 4241 O  O   . HOH Q 4 .   ? 24.852  34.945  -24.670 1.00 31.07 ?  4939 HOH B O   1 
HETATM 4242 O  O   . HOH Q 4 .   ? 23.262  18.553  3.232   1.00 25.52 ?  4940 HOH B O   1 
HETATM 4243 O  O   . HOH Q 4 .   ? 33.893  -18.544 -19.196 1.00 16.90 ?  4941 HOH B O   1 
HETATM 4244 O  O   . HOH Q 4 .   ? 36.626  -14.350 -15.363 1.00 21.37 ?  4942 HOH B O   1 
HETATM 4245 O  O   . HOH Q 4 .   ? 32.515  -21.440 -20.985 1.00 21.69 ?  4943 HOH B O   1 
HETATM 4246 O  O   . HOH Q 4 .   ? 37.834  19.833  -10.674 1.00 25.47 ?  4944 HOH B O   1 
HETATM 4247 O  O   . HOH Q 4 .   ? 34.466  -24.696 -18.370 1.00 38.39 ?  4945 HOH B O   1 
HETATM 4248 O  O   . HOH Q 4 .   ? 27.794  29.417  -26.280 1.00 34.97 ?  4946 HOH B O   1 
HETATM 4249 O  O   . HOH Q 4 .   ? 33.513  21.870  0.776   1.00 28.01 ?  4947 HOH B O   1 
HETATM 4250 O  O   . HOH Q 4 .   ? 37.762  17.978  -12.600 1.00 32.00 ?  4948 HOH B O   1 
HETATM 4251 O  O   . HOH Q 4 .   ? 12.640  14.260  -11.678 1.00 28.50 ?  4949 HOH B O   1 
HETATM 4252 O  O   . HOH Q 4 .   ? 38.353  -21.046 -18.544 1.00 26.51 ?  4950 HOH B O   1 
HETATM 4253 O  O   . HOH Q 4 .   ? 23.860  6.874   -16.773 1.00 22.39 ?  4951 HOH B O   1 
HETATM 4254 O  O   . HOH Q 4 .   ? 34.571  20.033  -0.974  1.00 21.96 ?  4952 HOH B O   1 
HETATM 4255 O  O   . HOH Q 4 .   ? 25.640  16.749  3.674   1.00 28.16 ?  4953 HOH B O   1 
HETATM 4256 O  O   . HOH Q 4 .   ? 28.381  -21.927 -18.769 1.00 17.48 ?  4954 HOH B O   1 
HETATM 4257 O  O   . HOH Q 4 .   ? 30.706  -3.902  -28.095 1.00 31.51 ?  4955 HOH B O   1 
HETATM 4258 O  O   . HOH Q 4 .   ? 31.496  -3.275  -10.140 1.00 28.57 ?  4956 HOH B O   1 
HETATM 4259 O  O   . HOH Q 4 .   ? 34.289  3.003   -16.578 1.00 23.77 ?  4957 HOH B O   1 
HETATM 4260 O  O   . HOH Q 4 .   ? 17.979  46.539  -8.521  1.00 21.31 ?  4958 HOH B O   1 
HETATM 4261 O  O   . HOH Q 4 .   ? 31.433  -7.990  -11.366 1.00 27.56 ?  4959 HOH B O   1 
HETATM 4262 O  O   . HOH Q 4 .   ? 27.396  17.379  -17.974 1.00 27.72 ?  4960 HOH B O   1 
HETATM 4263 O  O   . HOH Q 4 .   ? 27.544  20.715  5.021   1.00 25.44 ?  4961 HOH B O   1 
HETATM 4264 O  O   . HOH Q 4 .   ? 18.461  -6.300  -24.744 1.00 28.13 ?  4962 HOH B O   1 
HETATM 4265 O  O   . HOH Q 4 .   ? 28.187  -2.820  -28.897 1.00 22.80 ?  4963 HOH B O   1 
HETATM 4266 O  O   . HOH Q 4 .   ? 22.048  14.804  -18.209 1.00 32.59 ?  4964 HOH B O   1 
HETATM 4267 O  O   . HOH Q 4 .   ? 33.984  2.425   -4.177  1.00 30.31 ?  4965 HOH B O   1 
HETATM 4268 O  O   . HOH Q 4 .   ? 31.341  8.282   -12.715 1.00 25.67 ?  4966 HOH B O   1 
HETATM 4269 O  O   . HOH Q 4 .   ? 15.679  -9.507  -16.570 1.00 28.93 ?  4967 HOH B O   1 
HETATM 4270 O  O   . HOH Q 4 .   ? 36.721  -4.063  -11.328 1.00 28.35 ?  4968 HOH B O   1 
HETATM 4271 O  O   . HOH Q 4 .   ? 34.529  31.672  -9.721  1.00 35.06 ?  4969 HOH B O   1 
HETATM 4272 O  O   . HOH Q 4 .   ? 24.171  32.927  6.206   1.00 39.91 ?  4970 HOH B O   1 
HETATM 4273 O  O   . HOH Q 4 .   ? 35.543  3.392   -22.087 1.00 33.72 ?  4971 HOH B O   1 
HETATM 4274 O  O   . HOH Q 4 .   ? 10.238  9.206   -4.135  1.00 34.65 ?  4972 HOH B O   1 
HETATM 4275 O  O   . HOH Q 4 .   ? 33.212  9.252   -11.031 1.00 24.98 ?  4973 HOH B O   1 
HETATM 4276 O  O   . HOH Q 4 .   ? 22.409  12.650  -16.338 1.00 31.44 ?  4974 HOH B O   1 
HETATM 4277 O  O   . HOH Q 4 .   ? 31.296  10.498  -24.592 1.00 35.24 ?  4975 HOH B O   1 
HETATM 4278 O  O   . HOH Q 4 .   ? 17.576  16.432  5.485   1.00 36.52 ?  4976 HOH B O   1 
HETATM 4279 O  O   . HOH Q 4 .   ? 3.202   14.487  -4.485  1.00 40.49 ?  4977 HOH B O   1 
HETATM 4280 O  O   . HOH Q 4 .   ? 17.023  0.357   -22.030 1.00 35.92 ?  4978 HOH B O   1 
HETATM 4281 O  O   . HOH Q 4 .   ? 6.173   16.924  -9.833  1.00 37.64 ?  4979 HOH B O   1 
HETATM 4282 O  O   . HOH Q 4 .   ? 33.445  -21.874 -13.413 1.00 28.26 ?  4980 HOH B O   1 
HETATM 4283 O  O   . HOH Q 4 .   ? 28.552  -9.222  -29.362 1.00 27.03 ?  4981 HOH B O   1 
HETATM 4284 O  O   . HOH Q 4 .   ? 16.728  -4.317  -13.642 1.00 25.61 ?  4982 HOH B O   1 
HETATM 4285 O  O   . HOH Q 4 .   ? 30.290  29.466  -25.354 1.00 35.58 ?  4983 HOH B O   1 
HETATM 4286 O  O   . HOH Q 4 .   ? 32.220  -19.406 -13.663 1.00 18.23 ?  4984 HOH B O   1 
HETATM 4287 O  O   . HOH Q 4 .   ? 15.829  11.302  -0.103  1.00 31.88 ?  4985 HOH B O   1 
HETATM 4288 O  O   . HOH Q 4 .   ? 17.132  4.498   -19.315 1.00 30.14 ?  4986 HOH B O   1 
HETATM 4289 O  O   . HOH Q 4 .   ? 34.455  32.728  -11.789 1.00 36.01 ?  4987 HOH B O   1 
HETATM 4290 O  O   . HOH Q 4 .   ? 14.720  32.374  -25.700 1.00 35.05 ?  4988 HOH B O   1 
HETATM 4291 O  O   . HOH Q 4 .   ? 23.609  0.715   -9.429  1.00 19.29 ?  4989 HOH B O   1 
HETATM 4292 O  O   . HOH Q 4 .   ? 19.338  15.303  -20.924 1.00 31.10 ?  4990 HOH B O   1 
HETATM 4293 O  O   . HOH Q 4 .   ? 34.233  -17.201 -13.228 1.00 23.01 ?  4991 HOH B O   1 
HETATM 4294 O  O   . HOH Q 4 .   ? 33.840  9.650   -4.660  1.00 29.29 ?  4992 HOH B O   1 
HETATM 4295 O  O   . HOH Q 4 .   ? 39.296  19.601  -8.270  1.00 31.63 ?  4993 HOH B O   1 
HETATM 4296 O  O   . HOH Q 4 .   ? 13.477  13.087  -0.222  1.00 32.76 ?  4994 HOH B O   1 
HETATM 4297 O  O   . HOH Q 4 .   ? 35.313  29.642  2.347   1.00 33.57 ?  4995 HOH B O   1 
HETATM 4298 O  O   . HOH Q 4 .   ? 35.617  27.990  0.000   0.50 31.09 ?  4996 HOH B O   1 
HETATM 4299 O  O   . HOH Q 4 .   ? 23.146  -10.864 -11.205 1.00 30.02 ?  4997 HOH B O   1 
HETATM 4300 O  O   . HOH Q 4 .   ? 27.751  -4.025  -31.306 1.00 35.72 ?  4998 HOH B O   1 
HETATM 4301 O  O   . HOH Q 4 .   ? 18.497  -6.484  -21.948 1.00 26.97 ?  4999 HOH B O   1 
HETATM 4302 O  O   . HOH Q 4 .   ? 31.921  28.555  4.971   1.00 35.56 ?  5000 HOH B O   1 
HETATM 4303 O  O   . HOH Q 4 .   ? 25.821  -2.291  -6.300  1.00 34.86 ?  5001 HOH B O   1 
HETATM 4304 O  O   . HOH Q 4 .   ? 30.091  -7.356  -30.524 1.00 34.38 ?  5002 HOH B O   1 
HETATM 4305 O  O   . HOH Q 4 .   ? 27.806  -6.007  -10.774 1.00 29.89 ?  5003 HOH B O   1 
HETATM 4306 O  O   . HOH Q 4 .   ? 37.274  -23.222 -19.684 1.00 35.16 ?  5004 HOH B O   1 
# 
