data_9CXR
# 
_entry.id   9CXR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9CXR         pdb_00009cxr 10.2210/pdb9cxr/pdb 
WWPDB D_1000286500 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CXR 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              meilleurf@ornl.gov 
_pdbx_contact_author.name_first         Flora 
_pdbx_contact_author.name_last          Meilleur 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9313-8989 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Meilleur, F.'   1 0000-0001-9313-8989 
'Williams, A.N.' 2 ?                   
'Drufva, E.E.'   3 ?                   
'Parks, J.M.'    4 0000-0002-3103-9333 
'Chen, S.H.'     5 ?                   
'Michener, J.K.' 6 0000-0003-2302-8180 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Identification and characterization of substrate- and product-selective nylon hydrolases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.11.14.623603 
_citation.pdbx_database_id_PubMed   39605696 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Drufva, E.E.'          1  ?                   
primary 'Cahill, J.F.'          2  0000-0002-9866-4010 
primary 'Saint-Vincent, P.M.B.' 3  0000-0001-6360-8206 
primary 'Williams, A.N.'        4  0000-0002-5283-5822 
primary 'Bocharova, V.'         5  0000-0003-4270-3866 
primary 'Capra, N.'             6  0000-0002-2898-6479 
primary 'Meilleur, F.'          7  0000-0001-9313-8989 
primary 'Carper, D.L.'          8  0000-0002-4758-8054 
primary 'Bourgery, C.'          9  0000-0002-7318-2218 
primary 'Miyazaki, K.'          10 ?                   
primary 'Yonemura, M.'          11 ?                   
primary 'Shiraishi, Y.'         12 ?                   
primary 'Parks, J.M.'           13 0000-0002-3103-9333 
primary 'Zhou, M.'              14 0000-0001-8265-0215 
primary 'Dishner, I.T.'         15 0000-0002-7333-9182 
primary 'Foster, J.C.'          16 0000-0002-9097-8680 
primary 'Koehler, S.J.'         17 ?                   
primary 'Valentino, H.R.'       18 0009-0008-3117-3541 
primary 'Sedova, A.'            19 0000-0002-8233-3057 
primary 'Kertesz, V.'           20 0000-0003-0186-5797 
primary 'Vasileva, D.P.'        21 0000-0002-7919-7883 
primary 'Hochanadel, L.H.'      22 ?                   
primary 'Figg, C.A.'            23 0000-0003-3514-7750 
primary 'Negoro, S.'            24 0000-0002-9132-6860 
primary 'Kato, D.I.'            25 0000-0002-8255-8790 
primary 'Chen, S.H.'            26 0000-0002-6535-6812 
primary 'Michener, J.K.'        27 0000-0003-2302-8180 
# 
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 'Poly(hexamethylene adipamide) hydrolase' 31410.898 2   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                            62.068    1   ? ? ? ? 
3 non-polymer syn 'SODIUM ION'                              22.990    4   ? ? ? ? 
4 non-polymer syn 'TRIETHYLENE GLYCOL'                      150.173   1   ? ? ? ? 
5 water       nat water                                     18.015    204 ? ? ? ? 
# 
_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       
;MLTDIDGIRVGHATDARAMTGCTIAVFDEPVVPGVDVRGANAATIYTDLLYPDSVMPSVTGIMLTGGSAFGLEAALGAVR
YFEEQGRGYDVGVAKIPLVPAAVIYDLSVGDANVRPDLAMGRRACEAAKPGPFERGRVGGGTGATVGKLYGVRQSSPGGL
GTATVSLYGGIKVSAMIVVNSFGDLRDTAGRIVAGAKYEGGEFADTYARMKLGDKNQSALARMGMNTTIGIVSTNCRLTK
VEASRMATLAHNGLARAICPIHTNVDGDTIFATGLQKSDLTAPVDLLGTAAAEAAMLACLDAVMQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLTDIDGIRVGHATDARAMTGCTIAVFDEPVVPGVDVRGANAATIYTDLLYPDSVMPSVTGIMLTGGSAFGLEAALGAVR
YFEEQGRGYDVGVAKIPLVPAAVIYDLSVGDANVRPDLAMGRRACEAAKPGPFERGRVGGGTGATVGKLYGVRQSSPGGL
GTATVSLYGGIKVSAMIVVNSFGDLRDTAGRIVAGAKYEGGEFADTYARMKLGDKNQSALARMGMNTTIGIVSTNCRLTK
VEASRMATLAHNGLARAICPIHTNVDGDTIFATGLQKSDLTAPVDLLGTAAAEAAMLACLDAVMQ
;
_entity_poly.pdbx_strand_id                 AA,BA 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL       EDO 
3 'SODIUM ION'         NA  
4 'TRIETHYLENE GLYCOL' PGE 
5 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   LEU n 
1 3   THR n 
1 4   ASP n 
1 5   ILE n 
1 6   ASP n 
1 7   GLY n 
1 8   ILE n 
1 9   ARG n 
1 10  VAL n 
1 11  GLY n 
1 12  HIS n 
1 13  ALA n 
1 14  THR n 
1 15  ASP n 
1 16  ALA n 
1 17  ARG n 
1 18  ALA n 
1 19  MET n 
1 20  THR n 
1 21  GLY n 
1 22  CYS n 
1 23  THR n 
1 24  ILE n 
1 25  ALA n 
1 26  VAL n 
1 27  PHE n 
1 28  ASP n 
1 29  GLU n 
1 30  PRO n 
1 31  VAL n 
1 32  VAL n 
1 33  PRO n 
1 34  GLY n 
1 35  VAL n 
1 36  ASP n 
1 37  VAL n 
1 38  ARG n 
1 39  GLY n 
1 40  ALA n 
1 41  ASN n 
1 42  ALA n 
1 43  ALA n 
1 44  THR n 
1 45  ILE n 
1 46  TYR n 
1 47  THR n 
1 48  ASP n 
1 49  LEU n 
1 50  LEU n 
1 51  TYR n 
1 52  PRO n 
1 53  ASP n 
1 54  SER n 
1 55  VAL n 
1 56  MET n 
1 57  PRO n 
1 58  SER n 
1 59  VAL n 
1 60  THR n 
1 61  GLY n 
1 62  ILE n 
1 63  MET n 
1 64  LEU n 
1 65  THR n 
1 66  GLY n 
1 67  GLY n 
1 68  SER n 
1 69  ALA n 
1 70  PHE n 
1 71  GLY n 
1 72  LEU n 
1 73  GLU n 
1 74  ALA n 
1 75  ALA n 
1 76  LEU n 
1 77  GLY n 
1 78  ALA n 
1 79  VAL n 
1 80  ARG n 
1 81  TYR n 
1 82  PHE n 
1 83  GLU n 
1 84  GLU n 
1 85  GLN n 
1 86  GLY n 
1 87  ARG n 
1 88  GLY n 
1 89  TYR n 
1 90  ASP n 
1 91  VAL n 
1 92  GLY n 
1 93  VAL n 
1 94  ALA n 
1 95  LYS n 
1 96  ILE n 
1 97  PRO n 
1 98  LEU n 
1 99  VAL n 
1 100 PRO n 
1 101 ALA n 
1 102 ALA n 
1 103 VAL n 
1 104 ILE n 
1 105 TYR n 
1 106 ASP n 
1 107 LEU n 
1 108 SER n 
1 109 VAL n 
1 110 GLY n 
1 111 ASP n 
1 112 ALA n 
1 113 ASN n 
1 114 VAL n 
1 115 ARG n 
1 116 PRO n 
1 117 ASP n 
1 118 LEU n 
1 119 ALA n 
1 120 MET n 
1 121 GLY n 
1 122 ARG n 
1 123 ARG n 
1 124 ALA n 
1 125 CYS n 
1 126 GLU n 
1 127 ALA n 
1 128 ALA n 
1 129 LYS n 
1 130 PRO n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 GLU n 
1 135 ARG n 
1 136 GLY n 
1 137 ARG n 
1 138 VAL n 
1 139 GLY n 
1 140 GLY n 
1 141 GLY n 
1 142 THR n 
1 143 GLY n 
1 144 ALA n 
1 145 THR n 
1 146 VAL n 
1 147 GLY n 
1 148 LYS n 
1 149 LEU n 
1 150 TYR n 
1 151 GLY n 
1 152 VAL n 
1 153 ARG n 
1 154 GLN n 
1 155 SER n 
1 156 SER n 
1 157 PRO n 
1 158 GLY n 
1 159 GLY n 
1 160 LEU n 
1 161 GLY n 
1 162 THR n 
1 163 ALA n 
1 164 THR n 
1 165 VAL n 
1 166 SER n 
1 167 LEU n 
1 168 TYR n 
1 169 GLY n 
1 170 GLY n 
1 171 ILE n 
1 172 LYS n 
1 173 VAL n 
1 174 SER n 
1 175 ALA n 
1 176 MET n 
1 177 ILE n 
1 178 VAL n 
1 179 VAL n 
1 180 ASN n 
1 181 SER n 
1 182 PHE n 
1 183 GLY n 
1 184 ASP n 
1 185 LEU n 
1 186 ARG n 
1 187 ASP n 
1 188 THR n 
1 189 ALA n 
1 190 GLY n 
1 191 ARG n 
1 192 ILE n 
1 193 VAL n 
1 194 ALA n 
1 195 GLY n 
1 196 ALA n 
1 197 LYS n 
1 198 TYR n 
1 199 GLU n 
1 200 GLY n 
1 201 GLY n 
1 202 GLU n 
1 203 PHE n 
1 204 ALA n 
1 205 ASP n 
1 206 THR n 
1 207 TYR n 
1 208 ALA n 
1 209 ARG n 
1 210 MET n 
1 211 LYS n 
1 212 LEU n 
1 213 GLY n 
1 214 ASP n 
1 215 LYS n 
1 216 ASN n 
1 217 GLN n 
1 218 SER n 
1 219 ALA n 
1 220 LEU n 
1 221 ALA n 
1 222 ARG n 
1 223 MET n 
1 224 GLY n 
1 225 MET n 
1 226 ASN n 
1 227 THR n 
1 228 THR n 
1 229 ILE n 
1 230 GLY n 
1 231 ILE n 
1 232 VAL n 
1 233 SER n 
1 234 THR n 
1 235 ASN n 
1 236 CYS n 
1 237 ARG n 
1 238 LEU n 
1 239 THR n 
1 240 LYS n 
1 241 VAL n 
1 242 GLU n 
1 243 ALA n 
1 244 SER n 
1 245 ARG n 
1 246 MET n 
1 247 ALA n 
1 248 THR n 
1 249 LEU n 
1 250 ALA n 
1 251 HIS n 
1 252 ASN n 
1 253 GLY n 
1 254 LEU n 
1 255 ALA n 
1 256 ARG n 
1 257 ALA n 
1 258 ILE n 
1 259 CYS n 
1 260 PRO n 
1 261 ILE n 
1 262 HIS n 
1 263 THR n 
1 264 ASN n 
1 265 VAL n 
1 266 ASP n 
1 267 GLY n 
1 268 ASP n 
1 269 THR n 
1 270 ILE n 
1 271 PHE n 
1 272 ALA n 
1 273 THR n 
1 274 GLY n 
1 275 LEU n 
1 276 GLN n 
1 277 LYS n 
1 278 SER n 
1 279 ASP n 
1 280 LEU n 
1 281 THR n 
1 282 ALA n 
1 283 PRO n 
1 284 VAL n 
1 285 ASP n 
1 286 LEU n 
1 287 LEU n 
1 288 GLY n 
1 289 THR n 
1 290 ALA n 
1 291 ALA n 
1 292 ALA n 
1 293 GLU n 
1 294 ALA n 
1 295 ALA n 
1 296 MET n 
1 297 LEU n 
1 298 ALA n 
1 299 CYS n 
1 300 LEU n 
1 301 ASP n 
1 302 ALA n 
1 303 VAL n 
1 304 MET n 
1 305 GLN 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                   305 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 EPN97_01225 
_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      'Alphaproteobacteria bacterium' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1913988 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      '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          'pET-28a(+)' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE              ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE             ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE           ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE             ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL       'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE            ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE            ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ?                 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'         ?                 'Na 1'           22.990  
PGE non-polymer         . 'TRIETHYLENE GLYCOL' ?                 'C6 H14 O4'      150.173 
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 
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   1   1   MET MET AA . n 
A 1 2   LEU 2   2   2   LEU LEU AA . n 
A 1 3   THR 3   3   3   THR THR AA . n 
A 1 4   ASP 4   4   4   ASP ASP AA . n 
A 1 5   ILE 5   5   5   ILE ILE AA . n 
A 1 6   ASP 6   6   6   ASP ASP AA . n 
A 1 7   GLY 7   7   7   GLY GLY AA . n 
A 1 8   ILE 8   8   8   ILE ILE AA . n 
A 1 9   ARG 9   9   9   ARG ARG AA . n 
A 1 10  VAL 10  10  10  VAL VAL AA . n 
A 1 11  GLY 11  11  11  GLY GLY AA . n 
A 1 12  HIS 12  12  12  HIS HIS AA . n 
A 1 13  ALA 13  13  13  ALA ALA AA . n 
A 1 14  THR 14  14  14  THR THR AA . n 
A 1 15  ASP 15  15  15  ASP ASP AA . n 
A 1 16  ALA 16  16  16  ALA ALA AA . n 
A 1 17  ARG 17  17  17  ARG ARG AA . n 
A 1 18  ALA 18  18  18  ALA ALA AA . n 
A 1 19  MET 19  19  19  MET MET AA . n 
A 1 20  THR 20  20  20  THR THR AA . n 
A 1 21  GLY 21  21  21  GLY GLY AA . n 
A 1 22  CYS 22  22  22  CYS CYS AA . n 
A 1 23  THR 23  23  23  THR THR AA . n 
A 1 24  ILE 24  24  24  ILE ILE AA . n 
A 1 25  ALA 25  25  25  ALA ALA AA . n 
A 1 26  VAL 26  26  26  VAL VAL AA . n 
A 1 27  PHE 27  27  27  PHE PHE AA . n 
A 1 28  ASP 28  28  28  ASP ASP AA . n 
A 1 29  GLU 29  29  29  GLU GLU AA . n 
A 1 30  PRO 30  30  30  PRO PRO AA . n 
A 1 31  VAL 31  31  31  VAL VAL AA . n 
A 1 32  VAL 32  32  32  VAL VAL AA . n 
A 1 33  PRO 33  33  33  PRO PRO AA . n 
A 1 34  GLY 34  34  34  GLY GLY AA . n 
A 1 35  VAL 35  35  35  VAL VAL AA . n 
A 1 36  ASP 36  36  36  ASP ASP AA . n 
A 1 37  VAL 37  37  37  VAL VAL AA . n 
A 1 38  ARG 38  38  38  ARG ARG AA . n 
A 1 39  GLY 39  39  39  GLY GLY AA . n 
A 1 40  ALA 40  40  40  ALA ALA AA . n 
A 1 41  ASN 41  41  41  ASN ASN AA . n 
A 1 42  ALA 42  42  42  ALA ALA AA . n 
A 1 43  ALA 43  43  43  ALA ALA AA . n 
A 1 44  THR 44  44  44  THR THR AA . n 
A 1 45  ILE 45  45  45  ILE ILE AA . n 
A 1 46  TYR 46  46  46  TYR TYR AA . n 
A 1 47  THR 47  47  47  THR THR AA . n 
A 1 48  ASP 48  48  48  ASP ASP AA . n 
A 1 49  LEU 49  49  49  LEU LEU AA . n 
A 1 50  LEU 50  50  50  LEU LEU AA . n 
A 1 51  TYR 51  51  51  TYR TYR AA . n 
A 1 52  PRO 52  52  52  PRO PRO AA . n 
A 1 53  ASP 53  53  53  ASP ASP AA . n 
A 1 54  SER 54  54  54  SER SER AA . n 
A 1 55  VAL 55  55  55  VAL VAL AA . n 
A 1 56  MET 56  56  56  MET MET AA . n 
A 1 57  PRO 57  57  57  PRO PRO AA . n 
A 1 58  SER 58  58  58  SER SER AA . n 
A 1 59  VAL 59  59  59  VAL VAL AA . n 
A 1 60  THR 60  60  60  THR THR AA . n 
A 1 61  GLY 61  61  61  GLY GLY AA . n 
A 1 62  ILE 62  62  62  ILE ILE AA . n 
A 1 63  MET 63  63  63  MET MET AA . n 
A 1 64  LEU 64  64  64  LEU LEU AA . n 
A 1 65  THR 65  65  65  THR THR AA . n 
A 1 66  GLY 66  66  66  GLY GLY AA . n 
A 1 67  GLY 67  67  67  GLY GLY AA . n 
A 1 68  SER 68  68  68  SER SER AA . n 
A 1 69  ALA 69  69  69  ALA ALA AA . n 
A 1 70  PHE 70  70  70  PHE PHE AA . n 
A 1 71  GLY 71  71  71  GLY GLY AA . n 
A 1 72  LEU 72  72  72  LEU LEU AA . n 
A 1 73  GLU 73  73  73  GLU GLU AA . n 
A 1 74  ALA 74  74  74  ALA ALA AA . n 
A 1 75  ALA 75  75  75  ALA ALA AA . n 
A 1 76  LEU 76  76  76  LEU LEU AA . n 
A 1 77  GLY 77  77  77  GLY GLY AA . n 
A 1 78  ALA 78  78  78  ALA ALA AA . n 
A 1 79  VAL 79  79  79  VAL VAL AA . n 
A 1 80  ARG 80  80  80  ARG ARG AA . n 
A 1 81  TYR 81  81  81  TYR TYR AA . n 
A 1 82  PHE 82  82  82  PHE PHE AA . n 
A 1 83  GLU 83  83  83  GLU GLU AA . n 
A 1 84  GLU 84  84  84  GLU GLU AA . n 
A 1 85  GLN 85  85  85  GLN GLN AA . n 
A 1 86  GLY 86  86  86  GLY GLY AA . n 
A 1 87  ARG 87  87  87  ARG ARG AA . n 
A 1 88  GLY 88  88  88  GLY GLY AA . n 
A 1 89  TYR 89  89  89  TYR TYR AA . n 
A 1 90  ASP 90  90  90  ASP ASP AA . n 
A 1 91  VAL 91  91  91  VAL VAL AA . n 
A 1 92  GLY 92  92  92  GLY GLY AA . n 
A 1 93  VAL 93  93  93  VAL VAL AA . n 
A 1 94  ALA 94  94  94  ALA ALA AA . n 
A 1 95  LYS 95  95  95  LYS LYS AA . n 
A 1 96  ILE 96  96  96  ILE ILE AA . n 
A 1 97  PRO 97  97  97  PRO PRO AA . n 
A 1 98  LEU 98  98  98  LEU LEU AA . n 
A 1 99  VAL 99  99  99  VAL VAL AA . n 
A 1 100 PRO 100 100 100 PRO PRO AA . n 
A 1 101 ALA 101 101 101 ALA ALA AA . n 
A 1 102 ALA 102 102 102 ALA ALA AA . n 
A 1 103 VAL 103 103 103 VAL VAL AA . n 
A 1 104 ILE 104 104 104 ILE ILE AA . n 
A 1 105 TYR 105 105 105 TYR TYR AA . n 
A 1 106 ASP 106 106 106 ASP ASP AA . n 
A 1 107 LEU 107 107 107 LEU LEU AA . n 
A 1 108 SER 108 108 108 SER SER AA . n 
A 1 109 VAL 109 109 109 VAL VAL AA . n 
A 1 110 GLY 110 110 110 GLY GLY AA . n 
A 1 111 ASP 111 111 111 ASP ASP AA . n 
A 1 112 ALA 112 112 112 ALA ALA AA . n 
A 1 113 ASN 113 113 113 ASN ASN AA . n 
A 1 114 VAL 114 114 114 VAL VAL AA . n 
A 1 115 ARG 115 115 115 ARG ARG AA . n 
A 1 116 PRO 116 116 116 PRO PRO AA . n 
A 1 117 ASP 117 117 117 ASP ASP AA . n 
A 1 118 LEU 118 118 118 LEU LEU AA . n 
A 1 119 ALA 119 119 119 ALA ALA AA . n 
A 1 120 MET 120 120 120 MET MET AA . n 
A 1 121 GLY 121 121 121 GLY GLY AA . n 
A 1 122 ARG 122 122 122 ARG ARG AA . n 
A 1 123 ARG 123 123 123 ARG ARG AA . n 
A 1 124 ALA 124 124 124 ALA ALA AA . n 
A 1 125 CYS 125 125 125 CYS CYS AA . n 
A 1 126 GLU 126 126 126 GLU GLU AA . n 
A 1 127 ALA 127 127 127 ALA ALA AA . n 
A 1 128 ALA 128 128 128 ALA ALA AA . n 
A 1 129 LYS 129 129 129 LYS LYS AA . n 
A 1 130 PRO 130 130 130 PRO PRO AA . n 
A 1 131 GLY 131 131 131 GLY GLY AA . n 
A 1 132 PRO 132 132 132 PRO PRO AA . n 
A 1 133 PHE 133 133 133 PHE PHE AA . n 
A 1 134 GLU 134 134 134 GLU GLU AA . n 
A 1 135 ARG 135 135 135 ARG ARG AA . n 
A 1 136 GLY 136 136 136 GLY GLY AA . n 
A 1 137 ARG 137 137 137 ARG ARG AA . n 
A 1 138 VAL 138 138 138 VAL VAL AA . n 
A 1 139 GLY 139 139 139 GLY GLY AA . n 
A 1 140 GLY 140 140 140 GLY GLY AA . n 
A 1 141 GLY 141 141 141 GLY GLY AA . n 
A 1 142 THR 142 142 142 THR THR AA . n 
A 1 143 GLY 143 143 143 GLY GLY AA . n 
A 1 144 ALA 144 144 144 ALA ALA AA . n 
A 1 145 THR 145 145 145 THR THR AA . n 
A 1 146 VAL 146 146 146 VAL VAL AA . n 
A 1 147 GLY 147 147 147 GLY GLY AA . n 
A 1 148 LYS 148 148 148 LYS LYS AA . n 
A 1 149 LEU 149 149 149 LEU LEU AA . n 
A 1 150 TYR 150 150 150 TYR TYR AA . n 
A 1 151 GLY 151 151 151 GLY GLY AA . n 
A 1 152 VAL 152 152 152 VAL VAL AA . n 
A 1 153 ARG 153 153 153 ARG ARG AA . n 
A 1 154 GLN 154 154 154 GLN GLN AA . n 
A 1 155 SER 155 155 155 SER SER AA . n 
A 1 156 SER 156 156 156 SER SER AA . n 
A 1 157 PRO 157 157 157 PRO PRO AA . n 
A 1 158 GLY 158 158 158 GLY GLY AA . n 
A 1 159 GLY 159 159 159 GLY GLY AA . n 
A 1 160 LEU 160 160 160 LEU LEU AA . n 
A 1 161 GLY 161 161 161 GLY GLY AA . n 
A 1 162 THR 162 162 162 THR THR AA . n 
A 1 163 ALA 163 163 163 ALA ALA AA . n 
A 1 164 THR 164 164 164 THR THR AA . n 
A 1 165 VAL 165 165 165 VAL VAL AA . n 
A 1 166 SER 166 166 166 SER SER AA . n 
A 1 167 LEU 167 167 167 LEU LEU AA . n 
A 1 168 TYR 168 168 168 TYR TYR AA . n 
A 1 169 GLY 169 169 169 GLY GLY AA . n 
A 1 170 GLY 170 170 170 GLY GLY AA . n 
A 1 171 ILE 171 171 171 ILE ILE AA . n 
A 1 172 LYS 172 172 172 LYS LYS AA . n 
A 1 173 VAL 173 173 173 VAL VAL AA . n 
A 1 174 SER 174 174 174 SER SER AA . n 
A 1 175 ALA 175 175 175 ALA ALA AA . n 
A 1 176 MET 176 176 176 MET MET AA . n 
A 1 177 ILE 177 177 177 ILE ILE AA . n 
A 1 178 VAL 178 178 178 VAL VAL AA . n 
A 1 179 VAL 179 179 179 VAL VAL AA . n 
A 1 180 ASN 180 180 180 ASN ASN AA . n 
A 1 181 SER 181 181 181 SER SER AA . n 
A 1 182 PHE 182 182 182 PHE PHE AA . n 
A 1 183 GLY 183 183 183 GLY GLY AA . n 
A 1 184 ASP 184 184 184 ASP ASP AA . n 
A 1 185 LEU 185 185 185 LEU LEU AA . n 
A 1 186 ARG 186 186 186 ARG ARG AA . n 
A 1 187 ASP 187 187 187 ASP ASP AA . n 
A 1 188 THR 188 188 188 THR THR AA . n 
A 1 189 ALA 189 189 189 ALA ALA AA . n 
A 1 190 GLY 190 190 190 GLY GLY AA . n 
A 1 191 ARG 191 191 191 ARG ARG AA . n 
A 1 192 ILE 192 192 192 ILE ILE AA . n 
A 1 193 VAL 193 193 193 VAL VAL AA . n 
A 1 194 ALA 194 194 194 ALA ALA AA . n 
A 1 195 GLY 195 195 195 GLY GLY AA . n 
A 1 196 ALA 196 196 196 ALA ALA AA . n 
A 1 197 LYS 197 197 197 LYS LYS AA . n 
A 1 198 TYR 198 198 198 TYR TYR AA . n 
A 1 199 GLU 199 199 199 GLU GLU AA . n 
A 1 200 GLY 200 200 200 GLY GLY AA . n 
A 1 201 GLY 201 201 201 GLY GLY AA . n 
A 1 202 GLU 202 202 202 GLU GLU AA . n 
A 1 203 PHE 203 203 203 PHE PHE AA . n 
A 1 204 ALA 204 204 204 ALA ALA AA . n 
A 1 205 ASP 205 205 205 ASP ASP AA . n 
A 1 206 THR 206 206 206 THR THR AA . n 
A 1 207 TYR 207 207 207 TYR TYR AA . n 
A 1 208 ALA 208 208 208 ALA ALA AA . n 
A 1 209 ARG 209 209 209 ARG ARG AA . n 
A 1 210 MET 210 210 210 MET MET AA . n 
A 1 211 LYS 211 211 211 LYS LYS AA . n 
A 1 212 LEU 212 212 212 LEU LEU AA . n 
A 1 213 GLY 213 213 213 GLY GLY AA . n 
A 1 214 ASP 214 214 214 ASP ASP AA . n 
A 1 215 LYS 215 215 215 LYS LYS AA . n 
A 1 216 ASN 216 216 216 ASN ASN AA . n 
A 1 217 GLN 217 217 217 GLN GLN AA . n 
A 1 218 SER 218 218 218 SER SER AA . n 
A 1 219 ALA 219 219 219 ALA ALA AA . n 
A 1 220 LEU 220 220 220 LEU LEU AA . n 
A 1 221 ALA 221 221 221 ALA ALA AA . n 
A 1 222 ARG 222 222 222 ARG ARG AA . n 
A 1 223 MET 223 223 223 MET MET AA . n 
A 1 224 GLY 224 224 ?   ?   ?   AA . n 
A 1 225 MET 225 225 ?   ?   ?   AA . n 
A 1 226 ASN 226 226 ?   ?   ?   AA . n 
A 1 227 THR 227 227 227 THR THR AA . n 
A 1 228 THR 228 228 228 THR THR AA . n 
A 1 229 ILE 229 229 229 ILE ILE AA . n 
A 1 230 GLY 230 230 230 GLY GLY AA . n 
A 1 231 ILE 231 231 231 ILE ILE AA . n 
A 1 232 VAL 232 232 232 VAL VAL AA . n 
A 1 233 SER 233 233 233 SER SER AA . n 
A 1 234 THR 234 234 234 THR THR AA . n 
A 1 235 ASN 235 235 235 ASN ASN AA . n 
A 1 236 CYS 236 236 236 CYS CYS AA . n 
A 1 237 ARG 237 237 237 ARG ARG AA . n 
A 1 238 LEU 238 238 238 LEU LEU AA . n 
A 1 239 THR 239 239 239 THR THR AA . n 
A 1 240 LYS 240 240 240 LYS LYS AA . n 
A 1 241 VAL 241 241 241 VAL VAL AA . n 
A 1 242 GLU 242 242 242 GLU GLU AA . n 
A 1 243 ALA 243 243 243 ALA ALA AA . n 
A 1 244 SER 244 244 244 SER SER AA . n 
A 1 245 ARG 245 245 245 ARG ARG AA . n 
A 1 246 MET 246 246 246 MET MET AA . n 
A 1 247 ALA 247 247 247 ALA ALA AA . n 
A 1 248 THR 248 248 248 THR THR AA . n 
A 1 249 LEU 249 249 249 LEU LEU AA . n 
A 1 250 ALA 250 250 250 ALA ALA AA . n 
A 1 251 HIS 251 251 251 HIS HIS AA . n 
A 1 252 ASN 252 252 252 ASN ASN AA . n 
A 1 253 GLY 253 253 253 GLY GLY AA . n 
A 1 254 LEU 254 254 254 LEU LEU AA . n 
A 1 255 ALA 255 255 255 ALA ALA AA . n 
A 1 256 ARG 256 256 256 ARG ARG AA . n 
A 1 257 ALA 257 257 257 ALA ALA AA . n 
A 1 258 ILE 258 258 258 ILE ILE AA . n 
A 1 259 CYS 259 259 259 CYS CYS AA . n 
A 1 260 PRO 260 260 260 PRO PRO AA . n 
A 1 261 ILE 261 261 261 ILE ILE AA . n 
A 1 262 HIS 262 262 262 HIS HIS AA . n 
A 1 263 THR 263 263 263 THR THR AA . n 
A 1 264 ASN 264 264 264 ASN ASN AA . n 
A 1 265 VAL 265 265 265 VAL VAL AA . n 
A 1 266 ASP 266 266 266 ASP ASP AA . n 
A 1 267 GLY 267 267 267 GLY GLY AA . n 
A 1 268 ASP 268 268 268 ASP ASP AA . n 
A 1 269 THR 269 269 269 THR THR AA . n 
A 1 270 ILE 270 270 270 ILE ILE AA . n 
A 1 271 PHE 271 271 271 PHE PHE AA . n 
A 1 272 ALA 272 272 272 ALA ALA AA . n 
A 1 273 THR 273 273 273 THR THR AA . n 
A 1 274 GLY 274 274 274 GLY GLY AA . n 
A 1 275 LEU 275 275 275 LEU LEU AA . n 
A 1 276 GLN 276 276 276 GLN GLN AA . n 
A 1 277 LYS 277 277 277 LYS LYS AA . n 
A 1 278 SER 278 278 278 SER SER AA . n 
A 1 279 ASP 279 279 279 ASP ASP AA . n 
A 1 280 LEU 280 280 280 LEU LEU AA . n 
A 1 281 THR 281 281 281 THR THR AA . n 
A 1 282 ALA 282 282 282 ALA ALA AA . n 
A 1 283 PRO 283 283 283 PRO PRO AA . n 
A 1 284 VAL 284 284 284 VAL VAL AA . n 
A 1 285 ASP 285 285 285 ASP ASP AA . n 
A 1 286 LEU 286 286 286 LEU LEU AA . n 
A 1 287 LEU 287 287 287 LEU LEU AA . n 
A 1 288 GLY 288 288 288 GLY GLY AA . n 
A 1 289 THR 289 289 289 THR THR AA . n 
A 1 290 ALA 290 290 290 ALA ALA AA . n 
A 1 291 ALA 291 291 291 ALA ALA AA . n 
A 1 292 ALA 292 292 292 ALA ALA AA . n 
A 1 293 GLU 293 293 293 GLU GLU AA . n 
A 1 294 ALA 294 294 294 ALA ALA AA . n 
A 1 295 ALA 295 295 295 ALA ALA AA . n 
A 1 296 MET 296 296 296 MET MET AA . n 
A 1 297 LEU 297 297 297 LEU LEU AA . n 
A 1 298 ALA 298 298 298 ALA ALA AA . n 
A 1 299 CYS 299 299 299 CYS CYS AA . n 
A 1 300 LEU 300 300 300 LEU LEU AA . n 
A 1 301 ASP 301 301 301 ASP ASP AA . n 
A 1 302 ALA 302 302 302 ALA ALA AA . n 
A 1 303 VAL 303 303 303 VAL VAL AA . n 
A 1 304 MET 304 304 304 MET MET AA . n 
A 1 305 GLN 305 305 305 GLN GLN AA . n 
B 1 1   MET 1   1   1   MET MET BA . n 
B 1 2   LEU 2   2   2   LEU LEU BA . n 
B 1 3   THR 3   3   3   THR THR BA . n 
B 1 4   ASP 4   4   4   ASP ASP BA . n 
B 1 5   ILE 5   5   5   ILE ILE BA . n 
B 1 6   ASP 6   6   6   ASP ASP BA . n 
B 1 7   GLY 7   7   7   GLY GLY BA . n 
B 1 8   ILE 8   8   8   ILE ILE BA . n 
B 1 9   ARG 9   9   9   ARG ARG BA . n 
B 1 10  VAL 10  10  10  VAL VAL BA . n 
B 1 11  GLY 11  11  11  GLY GLY BA . n 
B 1 12  HIS 12  12  12  HIS HIS BA . n 
B 1 13  ALA 13  13  13  ALA ALA BA . n 
B 1 14  THR 14  14  14  THR THR BA . n 
B 1 15  ASP 15  15  15  ASP ASP BA . n 
B 1 16  ALA 16  16  16  ALA ALA BA . n 
B 1 17  ARG 17  17  17  ARG ARG BA . n 
B 1 18  ALA 18  18  18  ALA ALA BA . n 
B 1 19  MET 19  19  19  MET MET BA . n 
B 1 20  THR 20  20  20  THR THR BA . n 
B 1 21  GLY 21  21  21  GLY GLY BA . n 
B 1 22  CYS 22  22  22  CYS CYS BA . n 
B 1 23  THR 23  23  23  THR THR BA . n 
B 1 24  ILE 24  24  24  ILE ILE BA . n 
B 1 25  ALA 25  25  25  ALA ALA BA . n 
B 1 26  VAL 26  26  26  VAL VAL BA . n 
B 1 27  PHE 27  27  27  PHE PHE BA . n 
B 1 28  ASP 28  28  28  ASP ASP BA . n 
B 1 29  GLU 29  29  29  GLU GLU BA . n 
B 1 30  PRO 30  30  30  PRO PRO BA . n 
B 1 31  VAL 31  31  31  VAL VAL BA . n 
B 1 32  VAL 32  32  32  VAL VAL BA . n 
B 1 33  PRO 33  33  33  PRO PRO BA . n 
B 1 34  GLY 34  34  34  GLY GLY BA . n 
B 1 35  VAL 35  35  35  VAL VAL BA . n 
B 1 36  ASP 36  36  36  ASP ASP BA . n 
B 1 37  VAL 37  37  37  VAL VAL BA . n 
B 1 38  ARG 38  38  38  ARG ARG BA . n 
B 1 39  GLY 39  39  39  GLY GLY BA . n 
B 1 40  ALA 40  40  40  ALA ALA BA . n 
B 1 41  ASN 41  41  41  ASN ASN BA . n 
B 1 42  ALA 42  42  42  ALA ALA BA . n 
B 1 43  ALA 43  43  43  ALA ALA BA . n 
B 1 44  THR 44  44  44  THR THR BA . n 
B 1 45  ILE 45  45  45  ILE ILE BA . n 
B 1 46  TYR 46  46  46  TYR TYR BA . n 
B 1 47  THR 47  47  47  THR THR BA . n 
B 1 48  ASP 48  48  48  ASP ASP BA . n 
B 1 49  LEU 49  49  49  LEU LEU BA . n 
B 1 50  LEU 50  50  50  LEU LEU BA . n 
B 1 51  TYR 51  51  51  TYR TYR BA . n 
B 1 52  PRO 52  52  52  PRO PRO BA . n 
B 1 53  ASP 53  53  53  ASP ASP BA . n 
B 1 54  SER 54  54  54  SER SER BA . n 
B 1 55  VAL 55  55  55  VAL VAL BA . n 
B 1 56  MET 56  56  56  MET MET BA . n 
B 1 57  PRO 57  57  57  PRO PRO BA . n 
B 1 58  SER 58  58  58  SER SER BA . n 
B 1 59  VAL 59  59  59  VAL VAL BA . n 
B 1 60  THR 60  60  60  THR THR BA . n 
B 1 61  GLY 61  61  61  GLY GLY BA . n 
B 1 62  ILE 62  62  62  ILE ILE BA . n 
B 1 63  MET 63  63  63  MET MET BA . n 
B 1 64  LEU 64  64  64  LEU LEU BA . n 
B 1 65  THR 65  65  65  THR THR BA . n 
B 1 66  GLY 66  66  66  GLY GLY BA . n 
B 1 67  GLY 67  67  67  GLY GLY BA . n 
B 1 68  SER 68  68  68  SER SER BA . n 
B 1 69  ALA 69  69  69  ALA ALA BA . n 
B 1 70  PHE 70  70  70  PHE PHE BA . n 
B 1 71  GLY 71  71  71  GLY GLY BA . n 
B 1 72  LEU 72  72  72  LEU LEU BA . n 
B 1 73  GLU 73  73  73  GLU GLU BA . n 
B 1 74  ALA 74  74  74  ALA ALA BA . n 
B 1 75  ALA 75  75  75  ALA ALA BA . n 
B 1 76  LEU 76  76  76  LEU LEU BA . n 
B 1 77  GLY 77  77  77  GLY GLY BA . n 
B 1 78  ALA 78  78  78  ALA ALA BA . n 
B 1 79  VAL 79  79  79  VAL VAL BA . n 
B 1 80  ARG 80  80  80  ARG ARG BA . n 
B 1 81  TYR 81  81  81  TYR TYR BA . n 
B 1 82  PHE 82  82  82  PHE PHE BA . n 
B 1 83  GLU 83  83  83  GLU GLU BA . n 
B 1 84  GLU 84  84  84  GLU GLU BA . n 
B 1 85  GLN 85  85  85  GLN GLN BA . n 
B 1 86  GLY 86  86  86  GLY GLY BA . n 
B 1 87  ARG 87  87  87  ARG ARG BA . n 
B 1 88  GLY 88  88  88  GLY GLY BA . n 
B 1 89  TYR 89  89  89  TYR TYR BA . n 
B 1 90  ASP 90  90  90  ASP ASP BA . n 
B 1 91  VAL 91  91  91  VAL VAL BA . n 
B 1 92  GLY 92  92  92  GLY GLY BA . n 
B 1 93  VAL 93  93  93  VAL VAL BA . n 
B 1 94  ALA 94  94  94  ALA ALA BA . n 
B 1 95  LYS 95  95  95  LYS LYS BA . n 
B 1 96  ILE 96  96  96  ILE ILE BA . n 
B 1 97  PRO 97  97  97  PRO PRO BA . n 
B 1 98  LEU 98  98  98  LEU LEU BA . n 
B 1 99  VAL 99  99  99  VAL VAL BA . n 
B 1 100 PRO 100 100 100 PRO PRO BA . n 
B 1 101 ALA 101 101 101 ALA ALA BA . n 
B 1 102 ALA 102 102 102 ALA ALA BA . n 
B 1 103 VAL 103 103 103 VAL VAL BA . n 
B 1 104 ILE 104 104 104 ILE ILE BA . n 
B 1 105 TYR 105 105 105 TYR TYR BA . n 
B 1 106 ASP 106 106 106 ASP ASP BA . n 
B 1 107 LEU 107 107 107 LEU LEU BA . n 
B 1 108 SER 108 108 108 SER SER BA . n 
B 1 109 VAL 109 109 109 VAL VAL BA . n 
B 1 110 GLY 110 110 110 GLY GLY BA . n 
B 1 111 ASP 111 111 111 ASP ASP BA . n 
B 1 112 ALA 112 112 112 ALA ALA BA . n 
B 1 113 ASN 113 113 113 ASN ASN BA . n 
B 1 114 VAL 114 114 114 VAL VAL BA . n 
B 1 115 ARG 115 115 115 ARG ARG BA . n 
B 1 116 PRO 116 116 116 PRO PRO BA . n 
B 1 117 ASP 117 117 117 ASP ASP BA . n 
B 1 118 LEU 118 118 118 LEU LEU BA . n 
B 1 119 ALA 119 119 119 ALA ALA BA . n 
B 1 120 MET 120 120 120 MET MET BA . n 
B 1 121 GLY 121 121 121 GLY GLY BA . n 
B 1 122 ARG 122 122 122 ARG ARG BA . n 
B 1 123 ARG 123 123 123 ARG ARG BA . n 
B 1 124 ALA 124 124 124 ALA ALA BA . n 
B 1 125 CYS 125 125 125 CYS CYS BA . n 
B 1 126 GLU 126 126 126 GLU GLU BA . n 
B 1 127 ALA 127 127 127 ALA ALA BA . n 
B 1 128 ALA 128 128 128 ALA ALA BA . n 
B 1 129 LYS 129 129 129 LYS LYS BA . n 
B 1 130 PRO 130 130 130 PRO PRO BA . n 
B 1 131 GLY 131 131 131 GLY GLY BA . n 
B 1 132 PRO 132 132 132 PRO PRO BA . n 
B 1 133 PHE 133 133 133 PHE PHE BA . n 
B 1 134 GLU 134 134 134 GLU GLU BA . n 
B 1 135 ARG 135 135 135 ARG ARG BA . n 
B 1 136 GLY 136 136 136 GLY GLY BA . n 
B 1 137 ARG 137 137 137 ARG ARG BA . n 
B 1 138 VAL 138 138 138 VAL VAL BA . n 
B 1 139 GLY 139 139 139 GLY GLY BA . n 
B 1 140 GLY 140 140 140 GLY GLY BA . n 
B 1 141 GLY 141 141 141 GLY GLY BA . n 
B 1 142 THR 142 142 142 THR THR BA . n 
B 1 143 GLY 143 143 143 GLY GLY BA . n 
B 1 144 ALA 144 144 144 ALA ALA BA . n 
B 1 145 THR 145 145 145 THR THR BA . n 
B 1 146 VAL 146 146 146 VAL VAL BA . n 
B 1 147 GLY 147 147 147 GLY GLY BA . n 
B 1 148 LYS 148 148 148 LYS LYS BA . n 
B 1 149 LEU 149 149 149 LEU LEU BA . n 
B 1 150 TYR 150 150 150 TYR TYR BA . n 
B 1 151 GLY 151 151 151 GLY GLY BA . n 
B 1 152 VAL 152 152 152 VAL VAL BA . n 
B 1 153 ARG 153 153 153 ARG ARG BA . n 
B 1 154 GLN 154 154 154 GLN GLN BA . n 
B 1 155 SER 155 155 155 SER SER BA . n 
B 1 156 SER 156 156 156 SER SER BA . n 
B 1 157 PRO 157 157 157 PRO PRO BA . n 
B 1 158 GLY 158 158 158 GLY GLY BA . n 
B 1 159 GLY 159 159 159 GLY GLY BA . n 
B 1 160 LEU 160 160 160 LEU LEU BA . n 
B 1 161 GLY 161 161 161 GLY GLY BA . n 
B 1 162 THR 162 162 162 THR THR BA . n 
B 1 163 ALA 163 163 163 ALA ALA BA . n 
B 1 164 THR 164 164 164 THR THR BA . n 
B 1 165 VAL 165 165 165 VAL VAL BA . n 
B 1 166 SER 166 166 166 SER SER BA . n 
B 1 167 LEU 167 167 167 LEU LEU BA . n 
B 1 168 TYR 168 168 168 TYR TYR BA . n 
B 1 169 GLY 169 169 169 GLY GLY BA . n 
B 1 170 GLY 170 170 170 GLY GLY BA . n 
B 1 171 ILE 171 171 171 ILE ILE BA . n 
B 1 172 LYS 172 172 172 LYS LYS BA . n 
B 1 173 VAL 173 173 173 VAL VAL BA . n 
B 1 174 SER 174 174 174 SER SER BA . n 
B 1 175 ALA 175 175 175 ALA ALA BA . n 
B 1 176 MET 176 176 176 MET MET BA . n 
B 1 177 ILE 177 177 177 ILE ILE BA . n 
B 1 178 VAL 178 178 178 VAL VAL BA . n 
B 1 179 VAL 179 179 179 VAL VAL BA . n 
B 1 180 ASN 180 180 180 ASN ASN BA . n 
B 1 181 SER 181 181 181 SER SER BA . n 
B 1 182 PHE 182 182 182 PHE PHE BA . n 
B 1 183 GLY 183 183 183 GLY GLY BA . n 
B 1 184 ASP 184 184 184 ASP ASP BA . n 
B 1 185 LEU 185 185 185 LEU LEU BA . n 
B 1 186 ARG 186 186 186 ARG ARG BA . n 
B 1 187 ASP 187 187 187 ASP ASP BA . n 
B 1 188 THR 188 188 188 THR THR BA . n 
B 1 189 ALA 189 189 189 ALA ALA BA . n 
B 1 190 GLY 190 190 190 GLY GLY BA . n 
B 1 191 ARG 191 191 191 ARG ARG BA . n 
B 1 192 ILE 192 192 192 ILE ILE BA . n 
B 1 193 VAL 193 193 193 VAL VAL BA . n 
B 1 194 ALA 194 194 194 ALA ALA BA . n 
B 1 195 GLY 195 195 195 GLY GLY BA . n 
B 1 196 ALA 196 196 196 ALA ALA BA . n 
B 1 197 LYS 197 197 197 LYS LYS BA . n 
B 1 198 TYR 198 198 198 TYR TYR BA . n 
B 1 199 GLU 199 199 199 GLU GLU BA . n 
B 1 200 GLY 200 200 200 GLY GLY BA . n 
B 1 201 GLY 201 201 201 GLY GLY BA . n 
B 1 202 GLU 202 202 202 GLU GLU BA . n 
B 1 203 PHE 203 203 203 PHE PHE BA . n 
B 1 204 ALA 204 204 204 ALA ALA BA . n 
B 1 205 ASP 205 205 205 ASP ASP BA . n 
B 1 206 THR 206 206 206 THR THR BA . n 
B 1 207 TYR 207 207 207 TYR TYR BA . n 
B 1 208 ALA 208 208 208 ALA ALA BA . n 
B 1 209 ARG 209 209 209 ARG ARG BA . n 
B 1 210 MET 210 210 210 MET MET BA . n 
B 1 211 LYS 211 211 211 LYS LYS BA . n 
B 1 212 LEU 212 212 212 LEU LEU BA . n 
B 1 213 GLY 213 213 213 GLY GLY BA . n 
B 1 214 ASP 214 214 214 ASP ASP BA . n 
B 1 215 LYS 215 215 215 LYS LYS BA . n 
B 1 216 ASN 216 216 216 ASN ASN BA . n 
B 1 217 GLN 217 217 217 GLN GLN BA . n 
B 1 218 SER 218 218 218 SER SER BA . n 
B 1 219 ALA 219 219 219 ALA ALA BA . n 
B 1 220 LEU 220 220 220 LEU LEU BA . n 
B 1 221 ALA 221 221 221 ALA ALA BA . n 
B 1 222 ARG 222 222 222 ARG ARG BA . n 
B 1 223 MET 223 223 223 MET MET BA . n 
B 1 224 GLY 224 224 224 GLY GLY BA . n 
B 1 225 MET 225 225 ?   ?   ?   BA . n 
B 1 226 ASN 226 226 ?   ?   ?   BA . n 
B 1 227 THR 227 227 227 THR THR BA . n 
B 1 228 THR 228 228 228 THR THR BA . n 
B 1 229 ILE 229 229 229 ILE ILE BA . n 
B 1 230 GLY 230 230 230 GLY GLY BA . n 
B 1 231 ILE 231 231 231 ILE ILE BA . n 
B 1 232 VAL 232 232 232 VAL VAL BA . n 
B 1 233 SER 233 233 233 SER SER BA . n 
B 1 234 THR 234 234 234 THR THR BA . n 
B 1 235 ASN 235 235 235 ASN ASN BA . n 
B 1 236 CYS 236 236 236 CYS CYS BA . n 
B 1 237 ARG 237 237 237 ARG ARG BA . n 
B 1 238 LEU 238 238 238 LEU LEU BA . n 
B 1 239 THR 239 239 239 THR THR BA . n 
B 1 240 LYS 240 240 240 LYS LYS BA . n 
B 1 241 VAL 241 241 241 VAL VAL BA . n 
B 1 242 GLU 242 242 242 GLU GLU BA . n 
B 1 243 ALA 243 243 243 ALA ALA BA . n 
B 1 244 SER 244 244 244 SER SER BA . n 
B 1 245 ARG 245 245 245 ARG ARG BA . n 
B 1 246 MET 246 246 246 MET MET BA . n 
B 1 247 ALA 247 247 247 ALA ALA BA . n 
B 1 248 THR 248 248 248 THR THR BA . n 
B 1 249 LEU 249 249 249 LEU LEU BA . n 
B 1 250 ALA 250 250 250 ALA ALA BA . n 
B 1 251 HIS 251 251 251 HIS HIS BA . n 
B 1 252 ASN 252 252 252 ASN ASN BA . n 
B 1 253 GLY 253 253 253 GLY GLY BA . n 
B 1 254 LEU 254 254 254 LEU LEU BA . n 
B 1 255 ALA 255 255 255 ALA ALA BA . n 
B 1 256 ARG 256 256 256 ARG ARG BA . n 
B 1 257 ALA 257 257 257 ALA ALA BA . n 
B 1 258 ILE 258 258 258 ILE ILE BA . n 
B 1 259 CYS 259 259 259 CYS CYS BA . n 
B 1 260 PRO 260 260 260 PRO PRO BA . n 
B 1 261 ILE 261 261 261 ILE ILE BA . n 
B 1 262 HIS 262 262 262 HIS HIS BA . n 
B 1 263 THR 263 263 263 THR THR BA . n 
B 1 264 ASN 264 264 264 ASN ASN BA . n 
B 1 265 VAL 265 265 265 VAL VAL BA . n 
B 1 266 ASP 266 266 266 ASP ASP BA . n 
B 1 267 GLY 267 267 267 GLY GLY BA . n 
B 1 268 ASP 268 268 268 ASP ASP BA . n 
B 1 269 THR 269 269 269 THR THR BA . n 
B 1 270 ILE 270 270 270 ILE ILE BA . n 
B 1 271 PHE 271 271 271 PHE PHE BA . n 
B 1 272 ALA 272 272 272 ALA ALA BA . n 
B 1 273 THR 273 273 273 THR THR BA . n 
B 1 274 GLY 274 274 274 GLY GLY BA . n 
B 1 275 LEU 275 275 275 LEU LEU BA . n 
B 1 276 GLN 276 276 276 GLN GLN BA . n 
B 1 277 LYS 277 277 277 LYS LYS BA . n 
B 1 278 SER 278 278 278 SER SER BA . n 
B 1 279 ASP 279 279 279 ASP ASP BA . n 
B 1 280 LEU 280 280 280 LEU LEU BA . n 
B 1 281 THR 281 281 281 THR THR BA . n 
B 1 282 ALA 282 282 282 ALA ALA BA . n 
B 1 283 PRO 283 283 283 PRO PRO BA . n 
B 1 284 VAL 284 284 284 VAL VAL BA . n 
B 1 285 ASP 285 285 285 ASP ASP BA . n 
B 1 286 LEU 286 286 286 LEU LEU BA . n 
B 1 287 LEU 287 287 287 LEU LEU BA . n 
B 1 288 GLY 288 288 288 GLY GLY BA . n 
B 1 289 THR 289 289 289 THR THR BA . n 
B 1 290 ALA 290 290 290 ALA ALA BA . n 
B 1 291 ALA 291 291 291 ALA ALA BA . n 
B 1 292 ALA 292 292 292 ALA ALA BA . n 
B 1 293 GLU 293 293 293 GLU GLU BA . n 
B 1 294 ALA 294 294 294 ALA ALA BA . n 
B 1 295 ALA 295 295 295 ALA ALA BA . n 
B 1 296 MET 296 296 296 MET MET BA . n 
B 1 297 LEU 297 297 297 LEU LEU BA . n 
B 1 298 ALA 298 298 298 ALA ALA BA . n 
B 1 299 CYS 299 299 299 CYS CYS BA . n 
B 1 300 LEU 300 300 300 LEU LEU BA . n 
B 1 301 ASP 301 301 301 ASP ASP BA . n 
B 1 302 ALA 302 302 302 ALA ALA BA . n 
B 1 303 VAL 303 303 303 VAL VAL BA . n 
B 1 304 MET 304 304 304 MET MET BA . n 
B 1 305 GLN 305 305 305 GLN GLN BA . 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 EDO 1   401 401 EDO EDO AA . 
D 3 NA  1   402 1   NA  NA  AA . 
E 3 NA  1   403 4   NA  NA  AA . 
F 4 PGE 1   401 401 PGE PGE BA . 
G 3 NA  1   402 2   NA  NA  BA . 
H 3 NA  1   403 3   NA  NA  BA . 
I 5 HOH 1   501 49  HOH HOH AA . 
I 5 HOH 2   502 20  HOH HOH AA . 
I 5 HOH 3   503 166 HOH HOH AA . 
I 5 HOH 4   504 16  HOH HOH AA . 
I 5 HOH 5   505 34  HOH HOH AA . 
I 5 HOH 6   506 195 HOH HOH AA . 
I 5 HOH 7   507 196 HOH HOH AA . 
I 5 HOH 8   508 217 HOH HOH AA . 
I 5 HOH 9   509 69  HOH HOH AA . 
I 5 HOH 10  510 239 HOH HOH AA . 
I 5 HOH 11  511 212 HOH HOH AA . 
I 5 HOH 12  512 36  HOH HOH AA . 
I 5 HOH 13  513 39  HOH HOH AA . 
I 5 HOH 14  514 43  HOH HOH AA . 
I 5 HOH 15  515 40  HOH HOH AA . 
I 5 HOH 16  516 186 HOH HOH AA . 
I 5 HOH 17  517 19  HOH HOH AA . 
I 5 HOH 18  518 56  HOH HOH AA . 
I 5 HOH 19  519 109 HOH HOH AA . 
I 5 HOH 20  520 78  HOH HOH AA . 
I 5 HOH 21  521 241 HOH HOH AA . 
I 5 HOH 22  522 79  HOH HOH AA . 
I 5 HOH 23  523 30  HOH HOH AA . 
I 5 HOH 24  524 185 HOH HOH AA . 
I 5 HOH 25  525 216 HOH HOH AA . 
I 5 HOH 26  526 45  HOH HOH AA . 
I 5 HOH 27  527 24  HOH HOH AA . 
I 5 HOH 28  528 114 HOH HOH AA . 
I 5 HOH 29  529 105 HOH HOH AA . 
I 5 HOH 30  530 123 HOH HOH AA . 
I 5 HOH 31  531 155 HOH HOH AA . 
I 5 HOH 32  532 7   HOH HOH AA . 
I 5 HOH 33  533 145 HOH HOH AA . 
I 5 HOH 34  534 46  HOH HOH AA . 
I 5 HOH 35  535 246 HOH HOH AA . 
I 5 HOH 36  536 150 HOH HOH AA . 
I 5 HOH 37  537 227 HOH HOH AA . 
I 5 HOH 38  538 158 HOH HOH AA . 
I 5 HOH 39  539 173 HOH HOH AA . 
I 5 HOH 40  540 61  HOH HOH AA . 
I 5 HOH 41  541 210 HOH HOH AA . 
I 5 HOH 42  542 103 HOH HOH AA . 
I 5 HOH 43  543 149 HOH HOH AA . 
I 5 HOH 44  544 76  HOH HOH AA . 
I 5 HOH 45  545 29  HOH HOH AA . 
I 5 HOH 46  546 28  HOH HOH AA . 
I 5 HOH 47  547 181 HOH HOH AA . 
I 5 HOH 48  548 138 HOH HOH AA . 
I 5 HOH 49  549 17  HOH HOH AA . 
I 5 HOH 50  550 11  HOH HOH AA . 
I 5 HOH 51  551 163 HOH HOH AA . 
I 5 HOH 52  552 133 HOH HOH AA . 
I 5 HOH 53  553 238 HOH HOH AA . 
I 5 HOH 54  554 95  HOH HOH AA . 
I 5 HOH 55  555 13  HOH HOH AA . 
I 5 HOH 56  556 104 HOH HOH AA . 
I 5 HOH 57  557 32  HOH HOH AA . 
I 5 HOH 58  558 18  HOH HOH AA . 
I 5 HOH 59  559 25  HOH HOH AA . 
I 5 HOH 60  560 83  HOH HOH AA . 
I 5 HOH 61  561 73  HOH HOH AA . 
I 5 HOH 62  562 107 HOH HOH AA . 
I 5 HOH 63  563 5   HOH HOH AA . 
I 5 HOH 64  564 15  HOH HOH AA . 
I 5 HOH 65  565 94  HOH HOH AA . 
I 5 HOH 66  566 89  HOH HOH AA . 
I 5 HOH 67  567 127 HOH HOH AA . 
I 5 HOH 68  568 33  HOH HOH AA . 
I 5 HOH 69  569 92  HOH HOH AA . 
I 5 HOH 70  570 98  HOH HOH AA . 
I 5 HOH 71  571 218 HOH HOH AA . 
I 5 HOH 72  572 220 HOH HOH AA . 
I 5 HOH 73  573 121 HOH HOH AA . 
I 5 HOH 74  574 242 HOH HOH AA . 
I 5 HOH 75  575 23  HOH HOH AA . 
I 5 HOH 76  576 182 HOH HOH AA . 
I 5 HOH 77  577 128 HOH HOH AA . 
I 5 HOH 78  578 64  HOH HOH AA . 
I 5 HOH 79  579 137 HOH HOH AA . 
I 5 HOH 80  580 236 HOH HOH AA . 
I 5 HOH 81  581 151 HOH HOH AA . 
I 5 HOH 82  582 68  HOH HOH AA . 
I 5 HOH 83  583 170 HOH HOH AA . 
I 5 HOH 84  584 167 HOH HOH AA . 
I 5 HOH 85  585 47  HOH HOH AA . 
I 5 HOH 86  586 169 HOH HOH AA . 
I 5 HOH 87  587 77  HOH HOH AA . 
I 5 HOH 88  588 250 HOH HOH AA . 
I 5 HOH 89  589 66  HOH HOH AA . 
I 5 HOH 90  590 86  HOH HOH AA . 
I 5 HOH 91  591 199 HOH HOH AA . 
I 5 HOH 92  592 51  HOH HOH AA . 
I 5 HOH 93  593 80  HOH HOH AA . 
I 5 HOH 94  594 60  HOH HOH AA . 
I 5 HOH 95  595 53  HOH HOH AA . 
I 5 HOH 96  596 207 HOH HOH AA . 
I 5 HOH 97  597 84  HOH HOH AA . 
I 5 HOH 98  598 226 HOH HOH AA . 
I 5 HOH 99  599 203 HOH HOH AA . 
I 5 HOH 100 600 162 HOH HOH AA . 
I 5 HOH 101 601 38  HOH HOH AA . 
I 5 HOH 102 602 178 HOH HOH AA . 
I 5 HOH 103 603 117 HOH HOH AA . 
I 5 HOH 104 604 237 HOH HOH AA . 
I 5 HOH 105 605 58  HOH HOH AA . 
I 5 HOH 106 606 248 HOH HOH AA . 
I 5 HOH 107 607 240 HOH HOH AA . 
I 5 HOH 108 608 247 HOH HOH AA . 
I 5 HOH 109 609 243 HOH HOH AA . 
I 5 HOH 110 610 188 HOH HOH AA . 
I 5 HOH 111 611 90  HOH HOH AA . 
I 5 HOH 112 612 244 HOH HOH AA . 
J 5 HOH 1   501 41  HOH HOH BA . 
J 5 HOH 2   502 115 HOH HOH BA . 
J 5 HOH 3   503 102 HOH HOH BA . 
J 5 HOH 4   504 50  HOH HOH BA . 
J 5 HOH 5   505 146 HOH HOH BA . 
J 5 HOH 6   506 97  HOH HOH BA . 
J 5 HOH 7   507 82  HOH HOH BA . 
J 5 HOH 8   508 193 HOH HOH BA . 
J 5 HOH 9   509 129 HOH HOH BA . 
J 5 HOH 10  510 136 HOH HOH BA . 
J 5 HOH 11  511 143 HOH HOH BA . 
J 5 HOH 12  512 22  HOH HOH BA . 
J 5 HOH 13  513 37  HOH HOH BA . 
J 5 HOH 14  514 171 HOH HOH BA . 
J 5 HOH 15  515 27  HOH HOH BA . 
J 5 HOH 16  516 52  HOH HOH BA . 
J 5 HOH 17  517 232 HOH HOH BA . 
J 5 HOH 18  518 4   HOH HOH BA . 
J 5 HOH 19  519 59  HOH HOH BA . 
J 5 HOH 20  520 93  HOH HOH BA . 
J 5 HOH 21  521 131 HOH HOH BA . 
J 5 HOH 22  522 152 HOH HOH BA . 
J 5 HOH 23  523 26  HOH HOH BA . 
J 5 HOH 24  524 108 HOH HOH BA . 
J 5 HOH 25  525 42  HOH HOH BA . 
J 5 HOH 26  526 8   HOH HOH BA . 
J 5 HOH 27  527 180 HOH HOH BA . 
J 5 HOH 28  528 10  HOH HOH BA . 
J 5 HOH 29  529 124 HOH HOH BA . 
J 5 HOH 30  530 174 HOH HOH BA . 
J 5 HOH 31  531 213 HOH HOH BA . 
J 5 HOH 32  532 91  HOH HOH BA . 
J 5 HOH 33  533 21  HOH HOH BA . 
J 5 HOH 34  534 3   HOH HOH BA . 
J 5 HOH 35  535 209 HOH HOH BA . 
J 5 HOH 36  536 231 HOH HOH BA . 
J 5 HOH 37  537 63  HOH HOH BA . 
J 5 HOH 38  538 6   HOH HOH BA . 
J 5 HOH 39  539 229 HOH HOH BA . 
J 5 HOH 40  540 35  HOH HOH BA . 
J 5 HOH 41  541 144 HOH HOH BA . 
J 5 HOH 42  542 159 HOH HOH BA . 
J 5 HOH 43  543 132 HOH HOH BA . 
J 5 HOH 44  544 112 HOH HOH BA . 
J 5 HOH 45  545 31  HOH HOH BA . 
J 5 HOH 46  546 88  HOH HOH BA . 
J 5 HOH 47  547 202 HOH HOH BA . 
J 5 HOH 48  548 122 HOH HOH BA . 
J 5 HOH 49  549 99  HOH HOH BA . 
J 5 HOH 50  550 14  HOH HOH BA . 
J 5 HOH 51  551 71  HOH HOH BA . 
J 5 HOH 52  552 48  HOH HOH BA . 
J 5 HOH 53  553 135 HOH HOH BA . 
J 5 HOH 54  554 233 HOH HOH BA . 
J 5 HOH 55  555 249 HOH HOH BA . 
J 5 HOH 56  556 176 HOH HOH BA . 
J 5 HOH 57  557 111 HOH HOH BA . 
J 5 HOH 58  558 156 HOH HOH BA . 
J 5 HOH 59  559 62  HOH HOH BA . 
J 5 HOH 60  560 234 HOH HOH BA . 
J 5 HOH 61  561 228 HOH HOH BA . 
J 5 HOH 62  562 87  HOH HOH BA . 
J 5 HOH 63  563 85  HOH HOH BA . 
J 5 HOH 64  564 223 HOH HOH BA . 
J 5 HOH 65  565 67  HOH HOH BA . 
J 5 HOH 66  566 116 HOH HOH BA . 
J 5 HOH 67  567 175 HOH HOH BA . 
J 5 HOH 68  568 194 HOH HOH BA . 
J 5 HOH 69  569 70  HOH HOH BA . 
J 5 HOH 70  570 221 HOH HOH BA . 
J 5 HOH 71  571 225 HOH HOH BA . 
J 5 HOH 72  572 154 HOH HOH BA . 
J 5 HOH 73  573 140 HOH HOH BA . 
J 5 HOH 74  574 125 HOH HOH BA . 
J 5 HOH 75  575 192 HOH HOH BA . 
J 5 HOH 76  576 57  HOH HOH BA . 
J 5 HOH 77  577 113 HOH HOH BA . 
J 5 HOH 78  578 142 HOH HOH BA . 
J 5 HOH 79  579 222 HOH HOH BA . 
J 5 HOH 80  580 65  HOH HOH BA . 
J 5 HOH 81  581 190 HOH HOH BA . 
J 5 HOH 82  582 74  HOH HOH BA . 
J 5 HOH 83  583 224 HOH HOH BA . 
J 5 HOH 84  584 101 HOH HOH BA . 
J 5 HOH 85  585 230 HOH HOH BA . 
J 5 HOH 86  586 120 HOH HOH BA . 
J 5 HOH 87  587 75  HOH HOH BA . 
J 5 HOH 88  588 147 HOH HOH BA . 
J 5 HOH 89  589 126 HOH HOH BA . 
J 5 HOH 90  590 130 HOH HOH BA . 
J 5 HOH 91  591 200 HOH HOH BA . 
J 5 HOH 92  592 165 HOH HOH BA . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.19.2_4158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CXR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.014 
_cell.length_a_esd                 ? 
_cell.length_b                     96.643 
_cell.length_b_esd                 ? 
_cell.length_c                     105.212 
_cell.length_c_esd                 ? 
_cell.volume                       549217.013 
_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                         9CXR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9CXR 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.21 
_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          'BATCH MODE' 
_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    'Hampton Research PEGRx HT-D2 (Imidazole 0.1 M, Polyethylene glycol 6,000 20.0 w/v)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'Osmic VariMax' 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          15.42 
_reflns.entry_id                                       9CXR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               25.38 
_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                                     28405 
_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                           98.63 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.98 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.2012 
_reflns.pdbx_Rpim_I_all                                0.0930 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.94 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1775 
_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                                    2.2 
_reflns_shell.d_res_low                                     2.28 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2797 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.5717 
_reflns_shell.pdbx_Rpim_I_all                               0.2630 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.798 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.47 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.5051 
_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                               18.16 
_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                                 9CXR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             25.38 
_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                     28317 
_refine.ls_number_reflns_R_free                  1307 
_refine.ls_number_reflns_R_work                  27010 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.72 
_refine.ls_percent_reflns_R_free                 4.62 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1605 
_refine.ls_R_factor_R_free                       0.2057 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1582 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.3270 
_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                            0.2093 
_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                       2.20 
_refine_hist.d_res_low                        25.38 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               4570 
_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        4348 
_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' ? 0.0023  ? 4532 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4915  ? 6157 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0420  ? 723  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0033  ? 813  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.4804 ? 1637 ? f_dihedral_angle_d ? ? 
# 
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' 2.20 2.29  . . 146 2961 99.39 . . . . 0.1759 . . . . . . . . . . . 0.2510 
'X-RAY DIFFRACTION' 2.29 2.39  . . 151 2946 98.66 . . . . 0.1866 . . . . . . . . . . . 0.2914 
'X-RAY DIFFRACTION' 2.39 2.52  . . 168 2946 99.08 . . . . 0.1919 . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 2.52 2.68  . . 126 2976 98.73 . . . . 0.1838 . . . . . . . . . . . 0.2968 
'X-RAY DIFFRACTION' 2.68 2.88  . . 127 3015 99.30 . . . . 0.1736 . . . . . . . . . . . 0.2161 
'X-RAY DIFFRACTION' 2.88 3.17  . . 140 3012 99.03 . . . . 0.1652 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 3.17 3.63  . . 153 3000 99.18 . . . . 0.1413 . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 3.63 4.57  . . 149 3052 99.04 . . . . 0.1149 . . . . . . . . . . . 0.1456 
'X-RAY DIFFRACTION' 4.57 25.38 . . 147 3102 96.24 . . . . 0.1599 . . . . . . . . . . . 0.1628 
# 
_struct.entry_id                     9CXR 
_struct.title                        
'X-ray Crystallographic Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 at Room Temperature' 
_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        9CXR 
_struct_keywords.text            'NYLON OLIGOMER, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 3 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A522DD61_9PROT 
_struct_ref.pdbx_db_accession          A0A522DD61 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLTDIDGIRVGHATDARAMTGCTIAVFDEPVVPGVDVRGANAATIYTDLLYPDSVMPSVTGIMLTGGSAFGLEAALGAVR
YFEEQGRGYDVGVAKIPLVPAAVIYDLSVGDANVRPDLAMGRRACEAAKPGPFERGRVGGGTGATVGKLYGVRQSSPGGL
GTATVSLYGGIKVSAMIVVNSFGDLRDTAGRIVAGAKYEGGEFADTYARMKLGDKNQSALARMGMNTTIGIVSTNCRLTK
VEASRMATLAHNGLARAICPIHTNVDGDTIFATGLQKSDLTAPVDLLGTAAAEAAMLACLDAVMQ
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CXR AA 1 ? 305 ? A0A522DD61 1 ? 305 ? 1 305 
2 1 9CXR BA 1 ? 305 ? A0A522DD61 1 ? 305 ? 1 305 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5040  ? 
1 MORE         -62   ? 
1 'SSA (A^2)'  20560 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'equilibrium centrifugation' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 MET A 1   ? ILE A 5   ? MET AA 1   ILE AA 5   5 ? 5  
HELX_P HELX_P2  AA2 THR A 47  ? TYR A 51  ? THR AA 47  TYR AA 51  5 ? 5  
HELX_P HELX_P3  AA3 GLY A 67  ? GLY A 71  ? GLY AA 67  GLY AA 71  5 ? 5  
HELX_P HELX_P4  AA4 LEU A 72  ? GLN A 85  ? LEU AA 72  GLN AA 85  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 117 ? ALA A 127 ? ASP AA 117 ALA AA 127 1 ? 11 
HELX_P HELX_P6  AA6 VAL A 138 ? THR A 142 ? VAL AA 138 THR AA 142 5 ? 5  
HELX_P HELX_P7  AA7 GLY A 151 ? SER A 155 ? GLY AA 151 SER AA 155 5 ? 5  
HELX_P HELX_P8  AA8 TYR A 168 ? GLY A 170 ? TYR AA 168 GLY AA 170 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 205 ? GLY A 213 ? ASP AA 205 GLY AA 213 1 ? 9  
HELX_P HELX_P10 AB1 THR A 239 ? ALA A 257 ? THR AA 239 ALA AA 257 1 ? 19 
HELX_P HELX_P11 AB2 PRO A 283 ? MET A 304 ? PRO AA 283 MET AA 304 1 ? 22 
HELX_P HELX_P12 AB3 MET B 1   ? ILE B 5   ? MET BA 1   ILE BA 5   5 ? 5  
HELX_P HELX_P13 AB4 THR B 47  ? TYR B 51  ? THR BA 47  TYR BA 51  5 ? 5  
HELX_P HELX_P14 AB5 GLY B 67  ? GLY B 71  ? GLY BA 67  GLY BA 71  5 ? 5  
HELX_P HELX_P15 AB6 LEU B 72  ? GLN B 85  ? LEU BA 72  GLN BA 85  1 ? 14 
HELX_P HELX_P16 AB7 ASP B 117 ? ALA B 127 ? ASP BA 117 ALA BA 127 1 ? 11 
HELX_P HELX_P17 AB8 VAL B 138 ? THR B 142 ? VAL BA 138 THR BA 142 5 ? 5  
HELX_P HELX_P18 AB9 GLY B 151 ? SER B 155 ? GLY BA 151 SER BA 155 5 ? 5  
HELX_P HELX_P19 AC1 TYR B 168 ? GLY B 170 ? TYR BA 168 GLY BA 170 5 ? 3  
HELX_P HELX_P20 AC2 ASP B 205 ? GLY B 213 ? ASP BA 205 GLY BA 213 1 ? 9  
HELX_P HELX_P21 AC3 THR B 239 ? ALA B 257 ? THR BA 239 ALA BA 257 1 ? 19 
HELX_P HELX_P22 AC4 PRO B 283 ? GLN B 305 ? PRO BA 283 GLN BA 305 1 ? 23 
# 
_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 ALA 18  O   ? ? ? 1_555 E NA  . NA ? ? AA ALA 18  AA NA  403 1_555 ? ? ? ? ? ? ? 2.713 ? ? 
metalc2  metalc ? ? A MET 19  O   A ? ? 1_555 E NA  . NA ? ? AA MET 19  AA NA  403 1_555 ? ? ? ? ? ? ? 2.678 ? ? 
metalc3  metalc ? ? A MET 19  O   B ? ? 1_555 E NA  . NA ? ? AA MET 19  AA NA  403 1_555 ? ? ? ? ? ? ? 2.683 ? ? 
metalc4  metalc ? ? A ASP 106 O   ? ? ? 1_555 E NA  . NA ? ? AA ASP 106 AA NA  403 1_555 ? ? ? ? ? ? ? 2.575 ? ? 
metalc5  metalc ? ? A VAL 109 O   A ? ? 1_555 E NA  . NA ? ? AA VAL 109 AA NA  403 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc6  metalc ? ? A VAL 109 O   B ? ? 1_555 E NA  . NA ? ? AA VAL 109 AA NA  403 1_555 ? ? ? ? ? ? ? 2.493 ? ? 
metalc7  metalc ? ? A THR 227 OG1 ? ? ? 1_555 D NA  . NA ? ? AA THR 227 AA NA  402 1_555 ? ? ? ? ? ? ? 2.737 ? ? 
metalc8  metalc ? ? D NA  .   NA  ? ? ? 1_555 I HOH . O  ? ? AA NA  402 AA HOH 535 1_555 ? ? ? ? ? ? ? 2.658 ? ? 
metalc9  metalc ? ? B ALA 18  O   ? ? ? 1_555 H NA  . NA ? ? BA ALA 18  BA NA  403 1_555 ? ? ? ? ? ? ? 2.815 ? ? 
metalc10 metalc ? ? B MET 19  O   A ? ? 1_555 H NA  . NA ? ? BA MET 19  BA NA  403 1_555 ? ? ? ? ? ? ? 2.581 ? ? 
metalc11 metalc ? ? B MET 19  O   B ? ? 1_555 H NA  . NA ? ? BA MET 19  BA NA  403 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc12 metalc ? ? B ASP 106 O   ? ? ? 1_555 H NA  . NA ? ? BA ASP 106 BA NA  403 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc13 metalc ? ? B VAL 109 O   A ? ? 1_555 H NA  . NA ? ? BA VAL 109 BA NA  403 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc14 metalc ? ? B VAL 109 O   B ? ? 1_555 H NA  . NA ? ? BA VAL 109 BA NA  403 1_555 ? ? ? ? ? ? ? 2.440 ? ? 
metalc15 metalc ? ? B THR 227 OG1 ? ? ? 1_555 G NA  . NA ? ? BA THR 227 BA NA  402 1_555 ? ? ? ? ? ? ? 2.722 ? ? 
metalc16 metalc ? ? G NA  .   NA  ? ? ? 1_555 J HOH . O  ? ? BA NA  402 BA HOH 555 1_555 ? ? ? ? ? ? ? 2.661 ? ? 
# 
_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 ALA 18  ? AA ALA 18  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O A A MET 19  ? AA MET 19  ? 1_555 72.9  ? 
2  O   ? A ALA 18  ? AA ALA 18  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A MET 19  ? AA MET 19  ? 1_555 73.0  ? 
3  O   A A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A MET 19  ? AA MET 19  ? 1_555 0.1   ? 
4  O   ? A ALA 18  ? AA ALA 18  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O ? A ASP 106 ? AA ASP 106 ? 1_555 159.4 ? 
5  O   A A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O ? A ASP 106 ? AA ASP 106 ? 1_555 97.6  ? 
6  O   B A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O ? A ASP 106 ? AA ASP 106 ? 1_555 97.5  ? 
7  O   ? A ALA 18  ? AA ALA 18  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O A A VAL 109 ? AA VAL 109 ? 1_555 84.5  ? 
8  O   A A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O A A VAL 109 ? AA VAL 109 ? 1_555 104.5 ? 
9  O   B A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O A A VAL 109 ? AA VAL 109 ? 1_555 104.5 ? 
10 O   ? A ASP 106 ? AA ASP 106 ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O A A VAL 109 ? AA VAL 109 ? 1_555 80.3  ? 
11 O   ? A ALA 18  ? AA ALA 18  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A VAL 109 ? AA VAL 109 ? 1_555 84.9  ? 
12 O   A A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A VAL 109 ? AA VAL 109 ? 1_555 106.0 ? 
13 O   B A MET 19  ? AA MET 19  ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A VAL 109 ? AA VAL 109 ? 1_555 106.0 ? 
14 O   ? A ASP 106 ? AA ASP 106 ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A VAL 109 ? AA VAL 109 ? 1_555 80.2  ? 
15 O   A A VAL 109 ? AA VAL 109 ? 1_555 NA ? E NA . ? AA NA 403 ? 1_555 O B A VAL 109 ? AA VAL 109 ? 1_555 1.6   ? 
16 OG1 ? A THR 227 ? AA THR 227 ? 1_555 NA ? D NA . ? AA NA 402 ? 1_555 O ? I HOH .   ? AA HOH 535 ? 1_555 75.7  ? 
17 O   ? B ALA 18  ? BA ALA 18  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O A B MET 19  ? BA MET 19  ? 1_555 72.1  ? 
18 O   ? B ALA 18  ? BA ALA 18  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B MET 19  ? BA MET 19  ? 1_555 72.0  ? 
19 O   A B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B MET 19  ? BA MET 19  ? 1_555 0.2   ? 
20 O   ? B ALA 18  ? BA ALA 18  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O ? B ASP 106 ? BA ASP 106 ? 1_555 161.1 ? 
21 O   A B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O ? B ASP 106 ? BA ASP 106 ? 1_555 102.0 ? 
22 O   B B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O ? B ASP 106 ? BA ASP 106 ? 1_555 101.9 ? 
23 O   ? B ALA 18  ? BA ALA 18  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O A B VAL 109 ? BA VAL 109 ? 1_555 83.3  ? 
24 O   A B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O A B VAL 109 ? BA VAL 109 ? 1_555 107.7 ? 
25 O   B B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O A B VAL 109 ? BA VAL 109 ? 1_555 107.5 ? 
26 O   ? B ASP 106 ? BA ASP 106 ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O A B VAL 109 ? BA VAL 109 ? 1_555 81.6  ? 
27 O   ? B ALA 18  ? BA ALA 18  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B VAL 109 ? BA VAL 109 ? 1_555 82.8  ? 
28 O   A B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B VAL 109 ? BA VAL 109 ? 1_555 105.5 ? 
29 O   B B MET 19  ? BA MET 19  ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B VAL 109 ? BA VAL 109 ? 1_555 105.3 ? 
30 O   ? B ASP 106 ? BA ASP 106 ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B VAL 109 ? BA VAL 109 ? 1_555 81.6  ? 
31 O   A B VAL 109 ? BA VAL 109 ? 1_555 NA ? H NA . ? BA NA 403 ? 1_555 O B B VAL 109 ? BA VAL 109 ? 1_555 2.3   ? 
32 OG1 ? B THR 227 ? BA THR 227 ? 1_555 NA ? G NA . ? BA NA 402 ? 1_555 O ? J HOH .   ? BA HOH 555 ? 1_555 83.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 CYS 259 A . ? CYS 259 AA PRO 260 A ? PRO 260 AA 1 -3.59 
2 CYS 259 B . ? CYS 259 BA PRO 260 B ? PRO 260 BA 1 -2.42 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 3 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? 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 ILE A 8   ? ASP A 15  ? ILE AA 8   ASP AA 15  
AA1 2 THR A 20  ? PHE A 27  ? THR AA 20  PHE AA 27  
AA1 3 GLY A 61  ? THR A 65  ? GLY AA 61  THR AA 65  
AA1 4 ALA A 101 ? VAL A 103 ? ALA AA 101 VAL AA 103 
AA1 5 THR A 44  ? ILE A 45  ? THR AA 44  ILE AA 45  
AA2 1 VAL A 31  ? VAL A 37  ? VAL AA 31  VAL AA 37  
AA2 2 THR A 269 ? LEU A 275 ? THR AA 269 LEU AA 275 
AA2 3 THR A 228 ? ARG A 237 ? THR AA 228 ARG AA 237 
AA2 4 LYS A 172 ? VAL A 179 ? LYS AA 172 VAL AA 179 
AA2 5 GLY A 159 ? SER A 166 ? GLY AA 159 SER AA 166 
AA3 1 TYR A 89  ? ASP A 90  ? TYR AA 89  ASP AA 90  
AA3 2 LYS A 95  ? ILE A 96  ? LYS AA 95  ILE AA 96  
AA4 1 THR A 145 ? VAL A 146 ? THR AA 145 VAL AA 146 
AA4 2 SER A 156 ? PRO A 157 ? SER AA 156 PRO AA 157 
AA5 1 ILE A 192 ? ALA A 194 ? ILE AA 192 ALA AA 194 
AA5 2 ASP A 184 ? ARG A 186 ? ASP AA 184 ARG AA 186 
AA5 3 ILE A 258 ? CYS A 259 ? ILE AA 258 CYS AA 259 
AA6 1 ILE B 8   ? ASP B 15  ? ILE BA 8   ASP BA 15  
AA6 2 THR B 20  ? PHE B 27  ? THR BA 20  PHE BA 27  
AA6 3 GLY B 61  ? THR B 65  ? GLY BA 61  THR BA 65  
AA6 4 ALA B 101 ? VAL B 103 ? ALA BA 101 VAL BA 103 
AA6 5 THR B 44  ? ILE B 45  ? THR BA 44  ILE BA 45  
AA7 1 VAL B 31  ? VAL B 37  ? VAL BA 31  VAL BA 37  
AA7 2 THR B 269 ? LEU B 275 ? THR BA 269 LEU BA 275 
AA7 3 THR B 228 ? ARG B 237 ? THR BA 228 ARG BA 237 
AA7 4 LYS B 172 ? VAL B 179 ? LYS BA 172 VAL BA 179 
AA7 5 GLY B 159 ? SER B 166 ? GLY BA 159 SER BA 166 
AA8 1 TYR B 89  ? ASP B 90  ? TYR BA 89  ASP BA 90  
AA8 2 LYS B 95  ? ILE B 96  ? LYS BA 95  ILE BA 96  
AA9 1 THR B 145 ? VAL B 146 ? THR BA 145 VAL BA 146 
AA9 2 SER B 156 ? PRO B 157 ? SER BA 156 PRO BA 157 
AB1 1 ILE B 192 ? ALA B 194 ? ILE BA 192 ALA BA 194 
AB1 2 ASP B 184 ? ARG B 186 ? ASP BA 184 ARG BA 186 
AB1 3 ILE B 258 ? CYS B 259 ? ILE BA 258 CYS BA 259 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ARG A 9   ? N ARG AA 9   O VAL A 26  ? O VAL AA 26  
AA1 2 3 N THR A 23  ? N THR AA 23  O LEU A 64  ? O LEU AA 64  
AA1 3 4 N THR A 65  ? N THR AA 65  O ALA A 102 ? O ALA AA 102 
AA1 4 5 O ALA A 101 ? O ALA AA 101 N ILE A 45  ? N ILE AA 45  
AA2 1 2 N VAL A 32  ? N VAL AA 32  O GLY A 274 ? O GLY AA 274 
AA2 2 3 O PHE A 271 ? O PHE AA 271 N VAL A 232 ? N VAL AA 232 
AA2 3 4 O ILE A 229 ? O ILE AA 229 N VAL A 178 ? N VAL AA 178 
AA2 4 5 O VAL A 173 ? O VAL AA 173 N VAL A 165 ? N VAL AA 165 
AA3 1 2 N TYR A 89  ? N TYR AA 89  O ILE A 96  ? O ILE AA 96  
AA4 1 2 N VAL A 146 ? N VAL AA 146 O SER A 156 ? O SER AA 156 
AA5 1 2 O ALA A 194 ? O ALA AA 194 N LEU A 185 ? N LEU AA 185 
AA5 2 3 N ASP A 184 ? N ASP AA 184 O CYS A 259 ? O CYS AA 259 
AA6 1 2 N ARG B 9   ? N ARG BA 9   O VAL B 26  ? O VAL BA 26  
AA6 2 3 N THR B 23  ? N THR BA 23  O LEU B 64  ? O LEU BA 64  
AA6 3 4 N THR B 65  ? N THR BA 65  O ALA B 102 ? O ALA BA 102 
AA6 4 5 O ALA B 101 ? O ALA BA 101 N ILE B 45  ? N ILE BA 45  
AA7 1 2 N VAL B 32  ? N VAL BA 32  O GLY B 274 ? O GLY BA 274 
AA7 2 3 O PHE B 271 ? O PHE BA 271 N VAL B 232 ? N VAL BA 232 
AA7 3 4 O SER B 233 ? O SER BA 233 N SER B 174 ? N SER BA 174 
AA7 4 5 O VAL B 173 ? O VAL BA 173 N VAL B 165 ? N VAL BA 165 
AA8 1 2 N TYR B 89  ? N TYR BA 89  O ILE B 96  ? O ILE BA 96  
AA9 1 2 N VAL B 146 ? N VAL BA 146 O SER B 156 ? O SER BA 156 
AB1 1 2 O ALA B 194 ? O ALA BA 194 N LEU B 185 ? N LEU BA 185 
AB1 2 3 N ASP B 184 ? N ASP BA 184 O CYS B 259 ? O CYS BA 259 
# 
_pdbx_entry_details.entry_id                   9CXR 
_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 MET AA 19  ? A 60.40   62.68   
2  1 MET AA 19  ? B 60.33   62.47   
3  1 ASN AA 41  ? ? -143.03 58.54   
4  1 SER AA 68  ? ? 56.98   -141.22 
5  1 ASP AA 117 ? ? -124.06 -168.92 
6  1 LEU AA 167 ? ? -116.71 -162.95 
7  1 ASP AA 205 ? ? 60.95   91.74   
8  1 MET BA 19  ? A 61.05   65.59   
9  1 MET BA 19  ? B 60.93   65.65   
10 1 ASN BA 41  ? ? -141.43 58.55   
11 1 SER BA 68  ? ? 56.25   -142.06 
12 1 ASP BA 117 ? ? -127.06 -164.08 
13 1 LEU BA 167 ? ? -110.99 -165.82 
14 1 ASP BA 205 ? ? 61.41   92.89   
# 
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 AA HOH 611 ? I HOH . 
2 1 BA HOH 588 ? J HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x,-y,-z         
3 -x,y+1/2,-z+1/2 
4 -x,-y+1/2,z+1/2 
# 
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 AA GLY 224 ? A GLY 224 
2 1 Y 1 AA MET 225 ? A MET 225 
3 1 Y 1 AA ASN 226 ? A ASN 226 
4 1 Y 1 BA MET 225 ? B MET 225 
5 1 Y 1 BA ASN 226 ? B ASN 226 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
NA  NA   NA N N 260 
PGE C1   C  N N 261 
PGE O1   O  N N 262 
PGE C2   C  N N 263 
PGE O2   O  N N 264 
PGE C3   C  N N 265 
PGE C4   C  N N 266 
PGE O4   O  N N 267 
PGE C6   C  N N 268 
PGE C5   C  N N 269 
PGE O3   O  N N 270 
PGE H1   H  N N 271 
PGE H12  H  N N 272 
PGE HO1  H  N N 273 
PGE H2   H  N N 274 
PGE H22  H  N N 275 
PGE H3   H  N N 276 
PGE H32  H  N N 277 
PGE H4   H  N N 278 
PGE H42  H  N N 279 
PGE HO4  H  N N 280 
PGE H6   H  N N 281 
PGE H62  H  N N 282 
PGE H5   H  N N 283 
PGE H52  H  N N 284 
PHE N    N  N N 285 
PHE CA   C  N S 286 
PHE C    C  N N 287 
PHE O    O  N N 288 
PHE CB   C  N N 289 
PHE CG   C  Y N 290 
PHE CD1  C  Y N 291 
PHE CD2  C  Y N 292 
PHE CE1  C  Y N 293 
PHE CE2  C  Y N 294 
PHE CZ   C  Y N 295 
PHE OXT  O  N N 296 
PHE H    H  N N 297 
PHE H2   H  N N 298 
PHE HA   H  N N 299 
PHE HB2  H  N N 300 
PHE HB3  H  N N 301 
PHE HD1  H  N N 302 
PHE HD2  H  N N 303 
PHE HE1  H  N N 304 
PHE HE2  H  N N 305 
PHE HZ   H  N N 306 
PHE HXT  H  N N 307 
PRO N    N  N N 308 
PRO CA   C  N S 309 
PRO C    C  N N 310 
PRO O    O  N N 311 
PRO CB   C  N N 312 
PRO CG   C  N N 313 
PRO CD   C  N N 314 
PRO OXT  O  N N 315 
PRO H    H  N N 316 
PRO HA   H  N N 317 
PRO HB2  H  N N 318 
PRO HB3  H  N N 319 
PRO HG2  H  N N 320 
PRO HG3  H  N N 321 
PRO HD2  H  N N 322 
PRO HD3  H  N N 323 
PRO HXT  H  N N 324 
SER N    N  N N 325 
SER CA   C  N S 326 
SER C    C  N N 327 
SER O    O  N N 328 
SER CB   C  N N 329 
SER OG   O  N N 330 
SER OXT  O  N N 331 
SER H    H  N N 332 
SER H2   H  N N 333 
SER HA   H  N N 334 
SER HB2  H  N N 335 
SER HB3  H  N N 336 
SER HG   H  N N 337 
SER HXT  H  N N 338 
THR N    N  N N 339 
THR CA   C  N S 340 
THR C    C  N N 341 
THR O    O  N N 342 
THR CB   C  N R 343 
THR OG1  O  N N 344 
THR CG2  C  N N 345 
THR OXT  O  N N 346 
THR H    H  N N 347 
THR H2   H  N N 348 
THR HA   H  N N 349 
THR HB   H  N N 350 
THR HG1  H  N N 351 
THR HG21 H  N N 352 
THR HG22 H  N N 353 
THR HG23 H  N N 354 
THR HXT  H  N N 355 
TYR N    N  N N 356 
TYR CA   C  N S 357 
TYR C    C  N N 358 
TYR O    O  N N 359 
TYR CB   C  N N 360 
TYR CG   C  Y N 361 
TYR CD1  C  Y N 362 
TYR CD2  C  Y N 363 
TYR CE1  C  Y N 364 
TYR CE2  C  Y N 365 
TYR CZ   C  Y N 366 
TYR OH   O  N N 367 
TYR OXT  O  N N 368 
TYR H    H  N N 369 
TYR H2   H  N N 370 
TYR HA   H  N N 371 
TYR HB2  H  N N 372 
TYR HB3  H  N N 373 
TYR HD1  H  N N 374 
TYR HD2  H  N N 375 
TYR HE1  H  N N 376 
TYR HE2  H  N N 377 
TYR HH   H  N N 378 
TYR HXT  H  N N 379 
VAL N    N  N N 380 
VAL CA   C  N S 381 
VAL C    C  N N 382 
VAL O    O  N N 383 
VAL CB   C  N N 384 
VAL CG1  C  N N 385 
VAL CG2  C  N N 386 
VAL OXT  O  N N 387 
VAL H    H  N N 388 
VAL H2   H  N N 389 
VAL HA   H  N N 390 
VAL HB   H  N N 391 
VAL HG11 H  N N 392 
VAL HG12 H  N N 393 
VAL HG13 H  N N 394 
VAL HG21 H  N N 395 
VAL HG22 H  N N 396 
VAL HG23 H  N N 397 
VAL HXT  H  N N 398 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PGE C1  O1   sing N N 246 
PGE C1  C2   sing N N 247 
PGE C1  H1   sing N N 248 
PGE C1  H12  sing N N 249 
PGE O1  HO1  sing N N 250 
PGE C2  O2   sing N N 251 
PGE C2  H2   sing N N 252 
PGE C2  H22  sing N N 253 
PGE O2  C3   sing N N 254 
PGE C3  C4   sing N N 255 
PGE C3  H3   sing N N 256 
PGE C3  H32  sing N N 257 
PGE C4  O3   sing N N 258 
PGE C4  H4   sing N N 259 
PGE C4  H42  sing N N 260 
PGE O4  C6   sing N N 261 
PGE O4  HO4  sing N N 262 
PGE C6  C5   sing N N 263 
PGE C6  H6   sing N N 264 
PGE C6  H62  sing N N 265 
PGE C5  O3   sing N N 266 
PGE C5  H5   sing N N 267 
PGE C5  H52  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   'Department of Energy (DOE, United States)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 2 21 21' 
_space_group.name_Hall        'P 2 2ab (z,x,y)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CXR 
_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]   0.018514 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010347 
_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]   0.009505 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . MET A 1 1   ? 3.31900   28.42500  -3.37100  1.000 12.09907  ? 1   MET AA N   1 
ATOM   2    C  CA  . MET A 1 1   ? 2.71800   28.60600  -2.05400  1.000 17.30511  ? 1   MET AA CA  1 
ATOM   3    C  C   . MET A 1 1   ? 2.27100   27.26700  -1.48000  1.000 16.99678  ? 1   MET AA C   1 
ATOM   4    O  O   . MET A 1 1   ? 1.21200   26.75300  -1.84300  1.000 11.86744  ? 1   MET AA O   1 
ATOM   5    C  CB  . MET A 1 1   ? 1.53200   29.57200  -2.12600  1.000 18.93232  ? 1   MET AA CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 1.48600   30.61200  -1.01100  1.000 15.47433  ? 1   MET AA CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 3.09200   31.29900  -0.55200  1.000 20.25045  ? 1   MET AA SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 3.19300   32.69800  -1.66700  1.000 18.41889  ? 1   MET AA CE  1 
ATOM   9    N  N   . LEU A 1 2   ? 3.08800   26.71300  -0.57900  1.000 11.41814  ? 2   LEU AA N   1 
ATOM   10   C  CA  . LEU A 1 2   ? 2.77100   25.42400  0.03000   1.000 8.17094   ? 2   LEU AA CA  1 
ATOM   11   C  C   . LEU A 1 2   ? 1.42000   25.44400  0.73200   1.000 11.78182  ? 2   LEU AA C   1 
ATOM   12   O  O   . LEU A 1 2   ? 0.73600   24.41500  0.79000   1.000 10.27815  ? 2   LEU AA O   1 
ATOM   13   C  CB  . LEU A 1 2   ? 3.87100   25.02500  1.01500   1.000 6.47136   ? 2   LEU AA CB  1 
ATOM   14   C  CG  . LEU A 1 2   ? 3.86800   23.57700  1.51000   1.000 8.99792   ? 2   LEU AA CG  1 
ATOM   15   C  CD1 . LEU A 1 2   ? 4.11800   22.61200  0.36200   1.000 11.28383  ? 2   LEU AA CD1 1 
ATOM   16   C  CD2 . LEU A 1 2   ? 4.90200   23.38400  2.61200   1.000 10.18378  ? 2   LEU AA CD2 1 
ATOM   17   N  N   . THR A 1 3   ? 1.01400   26.59800  1.26200   1.000 16.44675  ? 3   THR AA N   1 
ATOM   18   C  CA  . THR A 1 3   ? -0.27000  26.70000  1.94700   1.000 19.19058  ? 3   THR AA CA  1 
ATOM   19   C  C   . THR A 1 3   ? -1.46200  26.62400  0.99700   1.000 20.49183  ? 3   THR AA C   1 
ATOM   20   O  O   . THR A 1 3   ? -2.60000  26.78300  1.45300   1.000 9.91252   ? 3   THR AA O   1 
ATOM   21   C  CB  . THR A 1 3   ? -0.33400  27.99700  2.75900   1.000 12.88409  ? 3   THR AA CB  1 
ATOM   22   O  OG1 . THR A 1 3   ? 0.00800   29.10900  1.92300   1.000 10.17463  ? 3   THR AA OG1 1 
ATOM   23   C  CG2 . THR A 1 3   ? 0.63700   27.93900  3.93100   1.000 6.82100   ? 3   THR AA CG2 1 
ATOM   24   N  N   . ASP A 1 4   ? -1.23800  26.39200  -0.30100  1.000 14.90171  ? 4   ASP AA N   1 
ATOM   25   C  CA  . ASP A 1 4   ? -2.34500  26.13000  -1.21400  1.000 13.38461  ? 4   ASP AA CA  1 
ATOM   26   C  C   . ASP A 1 4   ? -3.00600  24.78500  -0.94100  1.000 21.74057  ? 4   ASP AA C   1 
ATOM   27   O  O   . ASP A 1 4   ? -4.15300  24.57700  -1.35000  1.000 28.64397  ? 4   ASP AA O   1 
ATOM   28   C  CB  . ASP A 1 4   ? -1.86500  26.18000  -2.66600  1.000 11.14436  ? 4   ASP AA CB  1 
ATOM   29   C  CG  . ASP A 1 4   ? -1.62100  27.59400  -3.15500  1.000 23.92636  ? 4   ASP AA CG  1 
ATOM   30   O  OD1 . ASP A 1 4   ? -2.13200  28.54300  -2.52600  1.000 27.13056  ? 4   ASP AA OD1 1 
ATOM   31   O  OD2 . ASP A 1 4   ? -0.91900  27.75500  -4.17600  1.000 11.68011  ? 4   ASP AA OD2 1 
ATOM   32   N  N   . ILE A 1 5   ? -2.31000  23.87300  -0.26900  1.000 16.76687  ? 5   ILE AA N   1 
ATOM   33   C  CA  . ILE A 1 5   ? -2.84300  22.55800  0.06500   1.000 21.47190  ? 5   ILE AA CA  1 
ATOM   34   C  C   . ILE A 1 5   ? -3.60000  22.65300  1.38100   1.000 14.21964  ? 5   ILE AA C   1 
ATOM   35   O  O   . ILE A 1 5   ? -3.21900  23.41300  2.28000   1.000 26.03687  ? 5   ILE AA O   1 
ATOM   36   C  CB  . ILE A 1 5   ? -1.71300  21.51400  0.13600   1.000 18.25508  ? 5   ILE AA CB  1 
ATOM   37   C  CG1 . ILE A 1 5   ? -0.75900  21.68500  -1.04900  1.000 12.49163  ? 5   ILE AA CG1 1 
ATOM   38   C  CG2 . ILE A 1 5   ? -2.28100  20.10300  0.16400   1.000 22.82068  ? 5   ILE AA CG2 1 
ATOM   39   C  CD1 . ILE A 1 5   ? -1.41100  21.44900  -2.39900  1.000 12.99910  ? 5   ILE AA CD1 1 
ATOM   40   N  N   . ASP A 1 6   ? -4.67400  21.87300  1.49700   1.000 13.19095  ? 6   ASP AA N   1 
ATOM   41   C  CA  . ASP A 1 6   ? -5.56500  21.96600  2.64800   1.000 18.67784  ? 6   ASP AA CA  1 
ATOM   42   C  C   . ASP A 1 6   ? -4.83300  21.66400  3.95100   1.000 20.77821  ? 6   ASP AA C   1 
ATOM   43   O  O   . ASP A 1 6   ? -4.10100  20.67600  4.05600   1.000 19.81535  ? 6   ASP AA O   1 
ATOM   44   C  CB  . ASP A 1 6   ? -6.74000  21.00100  2.48000   1.000 21.25074  ? 6   ASP AA CB  1 
ATOM   45   C  CG  . ASP A 1 6   ? -7.32700  21.03000  1.08200   1.000 36.42257  ? 6   ASP AA CG  1 
ATOM   46   O  OD1 . ASP A 1 6   ? -6.55300  20.94800  0.10500   1.000 30.92351  ? 6   ASP AA OD1 1 
ATOM   47   O  OD2 . ASP A 1 6   ? -8.56700  21.12400  0.96000   1.000 53.70179  ? 6   ASP AA OD2 1 
ATOM   48   N  N   . GLY A 1 7   ? -5.03800  22.52500  4.94600   1.000 20.46536  ? 7   GLY AA N   1 
ATOM   49   C  CA  . GLY A 1 7   ? -4.59700  22.26300  6.30100   1.000 15.97001  ? 7   GLY AA CA  1 
ATOM   50   C  C   . GLY A 1 7   ? -3.15200  22.58100  6.60700   1.000 20.32819  ? 7   GLY AA C   1 
ATOM   51   O  O   . GLY A 1 7   ? -2.68600  22.25000  7.70300   1.000 24.05148  ? 7   GLY AA O   1 
ATOM   52   N  N   . ILE A 1 8   ? -2.42800  23.21800  5.69100   1.000 11.10865  ? 8   ILE AA N   1 
ATOM   53   C  CA  . ILE A 1 8   ? -1.00400  23.48300  5.86000   1.000 13.99722  ? 8   ILE AA CA  1 
ATOM   54   C  C   . ILE A 1 8   ? -0.81400  24.92400  6.31700   1.000 23.00441  ? 8   ILE AA C   1 
ATOM   55   O  O   . ILE A 1 8   ? -1.34900  25.85600  5.70300   1.000 14.56168  ? 8   ILE AA O   1 
ATOM   56   C  CB  . ILE A 1 8   ? -0.22900  23.21300  4.55900   1.000 12.58511  ? 8   ILE AA CB  1 
ATOM   57   C  CG1 . ILE A 1 8   ? -0.12200  21.70700  4.30500   1.000 11.08034  ? 8   ILE AA CG1 1 
ATOM   58   C  CG2 . ILE A 1 8   ? 1.15500   23.84100  4.61700   1.000 3.99895   ? 8   ILE AA CG2 1 
ATOM   59   C  CD1 . ILE A 1 8   ? 0.61400   21.35400  3.03200   1.000 14.63052  ? 8   ILE AA CD1 1 
ATOM   60   N  N   . ARG A 1 9   ? -0.05800  25.10500  7.39800   1.000 8.79878   ? 9   ARG AA N   1 
ATOM   61   C  CA  . ARG A 1 9   ? 0.37000   26.41500  7.86200   1.000 17.40629  ? 9   ARG AA CA  1 
ATOM   62   C  C   . ARG A 1 9   ? 1.89200   26.44700  7.91800   1.000 12.94475  ? 9   ARG AA C   1 
ATOM   63   O  O   . ARG A 1 9   ? 2.53700   25.42500  8.16900   1.000 18.13932  ? 9   ARG AA O   1 
ATOM   64   C  CB  . ARG A 1 9   ? -0.21800  26.74300  9.24200   1.000 10.95070  ? 9   ARG AA CB  1 
ATOM   65   C  CG  . ARG A 1 9   ? -1.72400  26.97100  9.23600   1.000 13.34843  ? 9   ARG AA CG  1 
ATOM   66   C  CD  . ARG A 1 9   ? -2.24500  27.30100  10.62800  1.000 20.31187  ? 9   ARG AA CD  1 
ATOM   67   N  NE  . ARG A 1 9   ? -2.27000  26.12800  11.49500  1.000 18.76485  ? 9   ARG AA NE  1 
ATOM   68   C  CZ  . ARG A 1 9   ? -1.58600  26.01800  12.62500  1.000 20.92054  ? 9   ARG AA CZ  1 
ATOM   69   N  NH1 . ARG A 1 9   ? -0.81400  26.99900  13.06500  1.000 24.18294  ? 9   ARG AA NH1 1 
ATOM   70   N  NH2 . ARG A 1 9   ? -1.67900  24.89600  13.33300  1.000 17.22530  ? 9   ARG AA NH2 1 
ATOM   71   N  N   . VAL A 1 10  ? 2.46700   27.62600  7.68200   1.000 12.97858  ? 10  VAL AA N   1 
ATOM   72   C  CA  . VAL A 1 10  ? 3.91300   27.78700  7.56800   1.000 14.36410  ? 10  VAL AA CA  1 
ATOM   73   C  C   . VAL A 1 10  ? 4.36200   28.93200  8.46700   1.000 12.09429  ? 10  VAL AA C   1 
ATOM   74   O  O   . VAL A 1 10  ? 3.77600   30.01900  8.43200   1.000 14.68892  ? 10  VAL AA O   1 
ATOM   75   C  CB  . VAL A 1 10  ? 4.34200   28.04400  6.11000   1.000 7.77322   ? 10  VAL AA CB  1 
ATOM   76   C  CG1 . VAL A 1 10  ? 5.79600   28.48600  6.04700   1.000 10.11258  ? 10  VAL AA CG1 1 
ATOM   77   C  CG2 . VAL A 1 10  ? 4.12300   26.79800  5.26600   1.000 10.04295  ? 10  VAL AA CG2 1 
ATOM   78   N  N   . GLY A 1 11  ? 5.39700   28.69000  9.25600   1.000 11.91101  ? 11  GLY AA N   1 
ATOM   79   C  CA  . GLY A 1 11  ? 5.95800   29.71900  10.11800  1.000 10.21599  ? 11  GLY AA CA  1 
ATOM   80   C  C   . GLY A 1 11  ? 7.46400   29.78200  10.00700  1.000 15.55395  ? 11  GLY AA C   1 
ATOM   81   O  O   . GLY A 1 11  ? 8.13400   28.75500  9.89800   1.000 11.04997  ? 11  GLY AA O   1 
ATOM   82   N  N   . HIS A 1 12  ? 7.99100   31.00300  10.03300  1.000 9.47216   ? 12  HIS AA N   1 
ATOM   83   C  CA  . HIS A 1 12  ? 9.42300   31.25600  9.96600   1.000 10.59855  ? 12  HIS AA CA  1 
ATOM   84   C  C   . HIS A 1 12  ? 9.94400   31.72500  11.31900  1.000 15.31184  ? 12  HIS AA C   1 
ATOM   85   O  O   . HIS A 1 12  ? 9.22400   32.35500  12.09900  1.000 12.10750  ? 12  HIS AA O   1 
ATOM   86   C  CB  . HIS A 1 12  ? 9.75800   32.32300  8.91600   1.000 17.30483  ? 12  HIS AA CB  1 
ATOM   87   C  CG  . HIS A 1 12  ? 9.44600   31.92100  7.50900   1.000 16.99976  ? 12  HIS AA CG  1 
ATOM   88   N  ND1 . HIS A 1 12  ? 9.88600   30.73800  6.95400   1.000 13.27615  ? 12  HIS AA ND1 1 
ATOM   89   C  CD2 . HIS A 1 12  ? 8.75500   32.55900  6.53500   1.000 11.23712  ? 12  HIS AA CD2 1 
ATOM   90   C  CE1 . HIS A 1 12  ? 9.46900   30.66000  5.70300   1.000 15.86371  ? 12  HIS AA CE1 1 
ATOM   91   N  NE2 . HIS A 1 12  ? 8.78100   31.75300  5.42300   1.000 12.46226  ? 12  HIS AA NE2 1 
ATOM   92   N  N   . ALA A 1 13  ? 11.21200  31.41700  11.58300  1.000 14.17844  ? 13  ALA AA N   1 
ATOM   93   C  CA  . ALA A 1 13  ? 11.96100  31.99100  12.69800  1.000 12.50528  ? 13  ALA AA CA  1 
ATOM   94   C  C   . ALA A 1 13  ? 13.31200  32.42100  12.14300  1.000 19.75840  ? 13  ALA AA C   1 
ATOM   95   O  O   . ALA A 1 13  ? 14.10400  31.57700  11.71400  1.000 15.85408  ? 13  ALA AA O   1 
ATOM   96   C  CB  . ALA A 1 13  ? 12.12300  30.99400  13.84400  1.000 12.58941  ? 13  ALA AA CB  1 
ATOM   97   N  N   . THR A 1 14  ? 13.57200  33.72600  12.13800  1.000 16.47647  ? 14  THR AA N   1 
ATOM   98   C  CA  . THR A 1 14  ? 14.68600  34.29900  11.39400  1.000 10.42106  ? 14  THR AA CA  1 
ATOM   99   C  C   . THR A 1 14  ? 15.60900  35.07700  12.31900  1.000 15.59109  ? 14  THR AA C   1 
ATOM   100  O  O   . THR A 1 14  ? 15.15200  35.92900  13.08800  1.000 20.55254  ? 14  THR AA O   1 
ATOM   101  C  CB  . THR A 1 14  ? 14.17600  35.21700  10.27900  1.000 11.22261  ? 14  THR AA CB  1 
ATOM   102  O  OG1 . THR A 1 14  ? 13.30800  34.47800  9.41100   1.000 14.57977  ? 14  THR AA OG1 1 
ATOM   103  C  CG2 . THR A 1 14  ? 15.33600  35.78500  9.47500   1.000 9.91455   ? 14  THR AA CG2 1 
ATOM   104  N  N   . ASP A 1 15  ? 16.90400  34.78600  12.23600  1.000 11.83150  ? 15  ASP AA N   1 
ATOM   105  C  CA  . ASP A 1 15  ? 17.95300  35.57700  12.87700  1.000 10.87603  ? 15  ASP AA CA  1 
ATOM   106  C  C   . ASP A 1 15  ? 18.79200  36.18600  11.75600  1.000 15.39216  ? 15  ASP AA C   1 
ATOM   107  O  O   . ASP A 1 15  ? 19.72000  35.55900  11.24200  1.000 17.18757  ? 15  ASP AA O   1 
ATOM   108  C  CB  . ASP A 1 15  ? 18.80100  34.72800  13.82200  1.000 12.77586  ? 15  ASP AA CB  1 
ATOM   109  C  CG  . ASP A 1 15  ? 19.71200  35.56800  14.70700  1.000 25.84540  ? 15  ASP AA CG  1 
ATOM   110  O  OD1 . ASP A 1 15  ? 20.16700  36.64200  14.25900  1.000 19.48915  ? 15  ASP AA OD1 1 
ATOM   111  O  OD2 . ASP A 1 15  ? 19.97300  35.15400  15.85700  1.000 19.63527  ? 15  ASP AA OD2 1 
ATOM   112  N  N   . ALA A 1 16  ? 18.45800  37.42300  11.38100  1.000 17.04060  ? 16  ALA AA N   1 
ATOM   113  C  CA  . ALA A 1 16  ? 19.16800  38.09400  10.30000  1.000 18.02459  ? 16  ALA AA CA  1 
ATOM   114  C  C   . ALA A 1 16  ? 20.58200  38.50300  10.69300  1.000 19.01072  ? 16  ALA AA C   1 
ATOM   115  O  O   . ALA A 1 16  ? 21.41100  38.74100  9.80900   1.000 25.79071  ? 16  ALA AA O   1 
ATOM   116  C  CB  . ALA A 1 16  ? 18.38200  39.32000  9.83500   1.000 18.56285  ? 16  ALA AA CB  1 
ATOM   117  N  N   . ARG A 1 17  ? 20.87900  38.59200  11.99100  1.000 18.42148  ? 17  ARG AA N   1 
ATOM   118  C  CA  . ARG A 1 17  ? 22.23200  38.94300  12.41100  1.000 17.85344  ? 17  ARG AA CA  1 
ATOM   119  C  C   . ARG A 1 17  ? 23.16500  37.74200  12.33100  1.000 18.24842  ? 17  ARG AA C   1 
ATOM   120  O  O   . ARG A 1 17  ? 24.23600  37.81700  11.72000  1.000 27.56962  ? 17  ARG AA O   1 
ATOM   121  C  CB  . ARG A 1 17  ? 22.21600  39.51400  13.83000  1.000 25.57290  ? 17  ARG AA CB  1 
ATOM   122  C  CG  . ARG A 1 17  ? 23.37900  40.44700  14.12700  1.000 32.52783  ? 17  ARG AA CG  1 
ATOM   123  C  CD  . ARG A 1 17  ? 23.88900  40.25700  15.54500  1.000 55.93316  ? 17  ARG AA CD  1 
ATOM   124  N  NE  . ARG A 1 17  ? 24.82200  39.14100  15.64700  1.000 55.68846  ? 17  ARG AA NE  1 
ATOM   125  C  CZ  . ARG A 1 17  ? 24.71100  38.15300  16.52500  1.000 69.44788  ? 17  ARG AA CZ  1 
ATOM   126  N  NH1 . ARG A 1 17  ? 23.70400  38.10000  17.38200  1.000 64.57845  ? 17  ARG AA NH1 1 
ATOM   127  N  NH2 . ARG A 1 17  ? 25.63200  37.19300  16.54200  1.000 47.54635  ? 17  ARG AA NH2 1 
ATOM   128  N  N   . ALA A 1 18  ? 22.77500  36.62500  12.94500  1.000 17.14956  ? 18  ALA AA N   1 
ATOM   129  C  CA  . ALA A 1 18  ? 23.57300  35.40900  12.89100  1.000 16.77849  ? 18  ALA AA CA  1 
ATOM   130  C  C   . ALA A 1 18  ? 23.47000  34.69000  11.55400  1.000 14.08359  ? 18  ALA AA C   1 
ATOM   131  O  O   . ALA A 1 18  ? 24.27700  33.78900  11.29600  1.000 17.29957  ? 18  ALA AA O   1 
ATOM   132  C  CB  . ALA A 1 18  ? 23.15400  34.45800  14.01300  1.000 20.28870  ? 18  ALA AA CB  1 
ATOM   133  N  N   A MET A 1 19  ? 22.50500  35.06400  10.71200  0.550 13.55461  ? 19  MET AA N   1 
ATOM   134  N  N   B MET A 1 19  ? 22.50800  35.06500  10.70900  0.450 13.59741  ? 19  MET AA N   1 
ATOM   135  C  CA  A MET A 1 19  ? 22.29200  34.45000  9.40200   0.550 15.28872  ? 19  MET AA CA  1 
ATOM   136  C  CA  B MET A 1 19  ? 22.29500  34.44800  9.39900   0.450 15.28971  ? 19  MET AA CA  1 
ATOM   137  C  C   A MET A 1 19  ? 21.98700  32.95600  9.54200   0.550 14.68115  ? 19  MET AA C   1 
ATOM   138  C  C   B MET A 1 19  ? 21.98600  32.95500  9.54000   0.450 14.66607  ? 19  MET AA C   1 
ATOM   139  O  O   A MET A 1 19  ? 22.72600  32.08900  9.07000   0.550 12.72783  ? 19  MET AA O   1 
ATOM   140  O  O   B MET A 1 19  ? 22.72200  32.08700  9.06500   0.450 12.73415  ? 19  MET AA O   1 
ATOM   141  C  CB  A MET A 1 19  ? 23.49000  34.69500  8.47700   0.550 15.20331  ? 19  MET AA CB  1 
ATOM   142  C  CB  B MET A 1 19  ? 23.49500  34.68500  8.47300   0.450 15.21146  ? 19  MET AA CB  1 
ATOM   143  C  CG  A MET A 1 19  ? 23.80900  36.16800  8.26300   0.550 18.37389  ? 19  MET AA CG  1 
ATOM   144  C  CG  B MET A 1 19  ? 23.73900  36.14800  8.12800   0.450 18.32703  ? 19  MET AA CG  1 
ATOM   145  S  SD  A MET A 1 19  ? 24.75600  36.48300  6.76200   0.550 16.20735  ? 19  MET AA SD  1 
ATOM   146  S  SD  B MET A 1 19  ? 22.31900  36.94600  7.35200   0.450 26.51590  ? 19  MET AA SD  1 
ATOM   147  C  CE  A MET A 1 19  ? 23.47100  36.38700  5.51800   0.550 30.82274  ? 19  MET AA CE  1 
ATOM   148  C  CE  B MET A 1 19  ? 22.46700  36.35400  5.66800   0.450 29.80588  ? 19  MET AA CE  1 
ATOM   149  N  N   . THR A 1 20  ? 20.87200  32.67300  10.21100  1.000 9.73237   ? 20  THR AA N   1 
ATOM   150  C  CA  . THR A 1 20  ? 20.37700  31.31100  10.36300  1.000 8.19359   ? 20  THR AA CA  1 
ATOM   151  C  C   . THR A 1 20  ? 18.90400  31.38600  10.73900  1.000 11.84132  ? 20  THR AA C   1 
ATOM   152  O  O   . THR A 1 20  ? 18.37300  32.45900  11.03400  1.000 14.00399  ? 20  THR AA O   1 
ATOM   153  C  CB  . THR A 1 20  ? 21.16800  30.52000  11.41200  1.000 14.00169  ? 20  THR AA CB  1 
ATOM   154  O  OG1 . THR A 1 20  ? 20.81400  29.13400  11.33000  1.000 12.45710  ? 20  THR AA OG1 1 
ATOM   155  C  CG2 . THR A 1 20  ? 20.86200  31.02900  12.81000  1.000 12.24321  ? 20  THR AA CG2 1 
ATOM   156  N  N   . GLY A 1 21  ? 18.25000  30.23100  10.72400  1.000 13.20345  ? 21  GLY AA N   1 
ATOM   157  C  CA  . GLY A 1 21  ? 16.84300  30.17300  11.06100  1.000 11.95311  ? 21  GLY AA CA  1 
ATOM   158  C  C   . GLY A 1 21  ? 16.27000  28.80800  10.73800  1.000 13.27849  ? 21  GLY AA C   1 
ATOM   159  O  O   . GLY A 1 21  ? 16.99800  27.87300  10.39800  1.000 10.28444  ? 21  GLY AA O   1 
ATOM   160  N  N   . CYS A 1 22  ? 14.94500  28.71500  10.85300  1.000 9.19668   ? 22  CYS AA N   1 
ATOM   161  C  CA  . CYS A 1 22  ? 14.24500  27.47000  10.57400  1.000 10.87102  ? 22  CYS AA CA  1 
ATOM   162  C  C   . CYS A 1 22  ? 12.81500  27.77200  10.15000  1.000 13.57752  ? 22  CYS AA C   1 
ATOM   163  O  O   . CYS A 1 22  ? 12.25500  28.82300  10.47200  1.000 12.91160  ? 22  CYS AA O   1 
ATOM   164  C  CB  . CYS A 1 22  ? 14.25500  26.53000  11.78800  1.000 10.50305  ? 22  CYS AA CB  1 
ATOM   165  S  SG  . CYS A 1 22  ? 13.48500  27.20300  13.27600  1.000 14.85222  ? 22  CYS AA SG  1 
ATOM   166  N  N   . THR A 1 23  ? 12.22900  26.82400  9.42000   1.000 10.13827  ? 23  THR AA N   1 
ATOM   167  C  CA  . THR A 1 23  ? 10.87200  26.93000  8.90200   1.000 7.91845   ? 23  THR AA CA  1 
ATOM   168  C  C   . THR A 1 23  ? 10.14300  25.61700  9.14500   1.000 9.13750   ? 23  THR AA C   1 
ATOM   169  O  O   . THR A 1 23  ? 10.70700  24.54100  8.93000   1.000 8.58249   ? 23  THR AA O   1 
ATOM   170  C  CB  . THR A 1 23  ? 10.87300  27.25500  7.39900   1.000 8.71035   ? 23  THR AA CB  1 
ATOM   171  O  OG1 . THR A 1 23  ? 11.60900  28.46200  7.16700   1.000 7.68417   ? 23  THR AA OG1 1 
ATOM   172  C  CG2 . THR A 1 23  ? 9.45400   27.42600  6.88700   1.000 14.18682  ? 23  THR AA CG2 1 
ATOM   173  N  N   . ILE A 1 24  ? 8.89300   25.70100  9.59600   1.000 6.40485   ? 24  ILE AA N   1 
ATOM   174  C  CA  . ILE A 1 24  ? 8.08200   24.51700  9.85100   1.000 16.11419  ? 24  ILE AA CA  1 
ATOM   175  C  C   . ILE A 1 24  ? 6.79300   24.61000  9.04600   1.000 16.53856  ? 24  ILE AA C   1 
ATOM   176  O  O   . ILE A 1 24  ? 6.21100   25.69100  8.90100   1.000 13.18696  ? 24  ILE AA O   1 
ATOM   177  C  CB  . ILE A 1 24  ? 7.77900   24.33200  11.35600  1.000 13.09472  ? 24  ILE AA CB  1 
ATOM   178  C  CG1 . ILE A 1 24  ? 7.03600   23.01200  11.58900  1.000 6.05846   ? 24  ILE AA CG1 1 
ATOM   179  C  CG2 . ILE A 1 24  ? 6.97500   25.50300  11.90500  1.000 7.44061   ? 24  ILE AA CG2 1 
ATOM   180  C  CD1 . ILE A 1 24  ? 7.19700   22.45100  12.98100  1.000 14.54368  ? 24  ILE AA CD1 1 
ATOM   181  N  N   . ALA A 1 25  ? 6.36700   23.47400  8.50200   1.000 6.75355   ? 25  ALA AA N   1 
ATOM   182  C  CA  . ALA A 1 25  ? 5.05300   23.32100  7.89400   1.000 8.25958   ? 25  ALA AA CA  1 
ATOM   183  C  C   . ALA A 1 25  ? 4.20000   22.47700  8.83100   1.000 16.32456  ? 25  ALA AA C   1 
ATOM   184  O  O   . ALA A 1 25  ? 4.53000   21.31500  9.09300   1.000 15.04677  ? 25  ALA AA O   1 
ATOM   185  C  CB  . ALA A 1 25  ? 5.15400   22.67100  6.51400   1.000 10.66384  ? 25  ALA AA CB  1 
ATOM   186  N  N   . VAL A 1 26  ? 3.12100   23.06300  9.34300   1.000 12.04573  ? 26  VAL AA N   1 
ATOM   187  C  CA  . VAL A 1 26  ? 2.23000   22.39800  10.28800  1.000 8.62682   ? 26  VAL AA CA  1 
ATOM   188  C  C   . VAL A 1 26  ? 1.05000   21.82400  9.52000   1.000 16.93307  ? 26  VAL AA C   1 
ATOM   189  O  O   . VAL A 1 26  ? 0.43700   22.51700  8.69800   1.000 8.14443   ? 26  VAL AA O   1 
ATOM   190  C  CB  . VAL A 1 26  ? 1.75600   23.36900  11.38300  1.000 13.82980  ? 26  VAL AA CB  1 
ATOM   191  C  CG1 . VAL A 1 26  ? 0.94300   22.62700  12.43600  1.000 7.44407   ? 26  VAL AA CG1 1 
ATOM   192  C  CG2 . VAL A 1 26  ? 2.94600   24.07800  12.01700  1.000 5.36066   ? 26  VAL AA CG2 1 
ATOM   193  N  N   . PHE A 1 27  ? 0.72500   20.56000  9.78600   1.000 10.01648  ? 27  PHE AA N   1 
ATOM   194  C  CA  . PHE A 1 27  ? -0.35300  19.86000  9.08900   1.000 16.46640  ? 27  PHE AA CA  1 
ATOM   195  C  C   . PHE A 1 27  ? -1.56100  19.77800  10.01500  1.000 22.28384  ? 27  PHE AA C   1 
ATOM   196  O  O   . PHE A 1 27  ? -1.61700  18.93000  10.91000  1.000 22.08166  ? 27  PHE AA O   1 
ATOM   197  C  CB  . PHE A 1 27  ? 0.10500   18.47800  8.63700   1.000 10.72018  ? 27  PHE AA CB  1 
ATOM   198  C  CG  . PHE A 1 27  ? 1.33300   18.50500  7.77500   1.000 15.54747  ? 27  PHE AA CG  1 
ATOM   199  C  CD1 . PHE A 1 27  ? 1.26600   18.96200  6.47000   1.000 8.93856   ? 27  PHE AA CD1 1 
ATOM   200  C  CD2 . PHE A 1 27  ? 2.55400   18.08200  8.27100   1.000 13.04191  ? 27  PHE AA CD2 1 
ATOM   201  C  CE1 . PHE A 1 27  ? 2.39200   18.99500  5.67600   1.000 15.08709  ? 27  PHE AA CE1 1 
ATOM   202  C  CE2 . PHE A 1 27  ? 3.68600   18.11200  7.48000   1.000 18.61016  ? 27  PHE AA CE2 1 
ATOM   203  C  CZ  . PHE A 1 27  ? 3.60400   18.56900  6.18100   1.000 14.25855  ? 27  PHE AA CZ  1 
ATOM   204  N  N   . ASP A 1 28  ? -2.53200  20.66500  9.79400   1.000 15.45006  ? 28  ASP AA N   1 
ATOM   205  C  CA  . ASP A 1 28  ? -3.76900  20.63300  10.56300  1.000 16.09915  ? 28  ASP AA CA  1 
ATOM   206  C  C   . ASP A 1 28  ? -4.71300  19.53400  10.09500  1.000 21.74511  ? 28  ASP AA C   1 
ATOM   207  O  O   . ASP A 1 28  ? -5.63100  19.16500  10.83600  1.000 23.23046  ? 28  ASP AA O   1 
ATOM   208  C  CB  . ASP A 1 28  ? -4.46200  21.99400  10.49100  1.000 17.55847  ? 28  ASP AA CB  1 
ATOM   209  C  CG  . ASP A 1 28  ? -3.73800  23.05700  11.29600  1.000 14.88185  ? 28  ASP AA CG  1 
ATOM   210  O  OD1 . ASP A 1 28  ? -2.94100  22.69100  12.18700  1.000 13.49485  ? 28  ASP AA OD1 1 
ATOM   211  O  OD2 . ASP A 1 28  ? -3.95800  24.25800  11.03800  1.000 17.18042  ? 28  ASP AA OD2 1 
ATOM   212  N  N   . GLU A 1 29  ? -4.50900  19.00800  8.88600   1.000 17.82545  ? 29  GLU AA N   1 
ATOM   213  C  CA  . GLU A 1 29  ? -5.20100  17.84000  8.37300   1.000 23.57476  ? 29  GLU AA CA  1 
ATOM   214  C  C   . GLU A 1 29  ? -4.23700  16.66200  8.29200   1.000 24.62088  ? 29  GLU AA C   1 
ATOM   215  O  O   . GLU A 1 29  ? -3.06800  16.84900  7.93400   1.000 18.89920  ? 29  GLU AA O   1 
ATOM   216  C  CB  . GLU A 1 29  ? -5.79500  18.10800  6.98400   1.000 28.22912  ? 29  GLU AA CB  1 
ATOM   217  C  CG  . GLU A 1 29  ? -7.10500  18.87900  7.00900   1.000 47.00682  ? 29  GLU AA CG  1 
ATOM   218  C  CD  . GLU A 1 29  ? -8.30100  17.98400  7.27100   1.000 47.49467  ? 29  GLU AA CD  1 
ATOM   219  O  OE1 . GLU A 1 29  ? -8.48800  17.00500  6.51900   1.000 54.23437  ? 29  GLU AA OE1 1 
ATOM   220  O  OE2 . GLU A 1 29  ? -9.05100  18.25800  8.23200   1.000 38.13925  ? 29  GLU AA OE2 1 
ATOM   221  N  N   . PRO A 1 30  ? -4.68700  15.45100  8.62500   1.000 14.61563  ? 30  PRO AA N   1 
ATOM   222  C  CA  . PRO A 1 30  ? -3.77200  14.30100  8.63400   1.000 15.76901  ? 30  PRO AA CA  1 
ATOM   223  C  C   . PRO A 1 30  ? -3.17200  14.04900  7.25800   1.000 19.69257  ? 30  PRO AA C   1 
ATOM   224  O  O   . PRO A 1 30  ? -3.85000  14.15500  6.23300   1.000 14.51749  ? 30  PRO AA O   1 
ATOM   225  C  CB  . PRO A 1 30  ? -4.66800  13.13800  9.08000   1.000 22.79663  ? 30  PRO AA CB  1 
ATOM   226  C  CG  . PRO A 1 30  ? -5.82100  13.78400  9.78000   1.000 16.79317  ? 30  PRO AA CG  1 
ATOM   227  C  CD  . PRO A 1 30  ? -6.04000  15.09100  9.08100   1.000 27.03056  ? 30  PRO AA CD  1 
ATOM   228  N  N   . VAL A 1 31  ? -1.88300  13.71100  7.24400   1.000 9.86476   ? 31  VAL AA N   1 
ATOM   229  C  CA  . VAL A 1 31  ? -1.13600  13.53800  6.00700   1.000 14.03412  ? 31  VAL AA CA  1 
ATOM   230  C  C   . VAL A 1 31  ? -0.53000  12.14000  5.96300   1.000 14.51584  ? 31  VAL AA C   1 
ATOM   231  O  O   . VAL A 1 31  ? -0.37600  11.46400  6.98400   1.000 11.36291  ? 31  VAL AA O   1 
ATOM   232  C  CB  . VAL A 1 31  ? -0.03600  14.60700  5.84100   1.000 12.07590  ? 31  VAL AA CB  1 
ATOM   233  C  CG1 . VAL A 1 31  ? -0.65700  15.98400  5.67000   1.000 13.56390  ? 31  VAL AA CG1 1 
ATOM   234  C  CG2 . VAL A 1 31  ? 0.91400   14.58700  7.03100   1.000 10.53026  ? 31  VAL AA CG2 1 
ATOM   235  N  N   . VAL A 1 32  ? -0.18900  11.71500  4.75400   1.000 9.10364   ? 32  VAL AA N   1 
ATOM   236  C  CA  . VAL A 1 32  ? 0.53200   10.47200  4.49600   1.000 9.77311   ? 32  VAL AA CA  1 
ATOM   237  C  C   . VAL A 1 32  ? 1.94800   10.84300  4.06800   1.000 21.09251  ? 32  VAL AA C   1 
ATOM   238  O  O   . VAL A 1 32  ? 2.12300   11.46400  3.01200   1.000 18.28961  ? 32  VAL AA O   1 
ATOM   239  C  CB  . VAL A 1 32  ? -0.16100  9.62200   3.42000   1.000 15.53265  ? 32  VAL AA CB  1 
ATOM   240  C  CG1 . VAL A 1 32  ? 0.71400   8.43700   3.04100   1.000 18.67952  ? 32  VAL AA CG1 1 
ATOM   241  C  CG2 . VAL A 1 32  ? -1.51900  9.15000   3.90700   1.000 14.95782  ? 32  VAL AA CG2 1 
ATOM   242  N  N   . PRO A 1 33  ? 2.97600   10.49100  4.83900   1.000 17.48255  ? 33  PRO AA N   1 
ATOM   243  C  CA  . PRO A 1 33  ? 4.31400   11.02900  4.56800   1.000 8.32656   ? 33  PRO AA CA  1 
ATOM   244  C  C   . PRO A 1 33  ? 5.23000   10.09300  3.79400   1.000 16.26866  ? 33  PRO AA C   1 
ATOM   245  O  O   . PRO A 1 33  ? 5.11700   8.86500   3.87900   1.000 16.03285  ? 33  PRO AA O   1 
ATOM   246  C  CB  . PRO A 1 33  ? 4.85900   11.28300  5.97600   1.000 10.43195  ? 33  PRO AA CB  1 
ATOM   247  C  CG  . PRO A 1 33  ? 4.20700   10.20000  6.81600   1.000 14.78155  ? 33  PRO AA CG  1 
ATOM   248  C  CD  . PRO A 1 33  ? 2.93200   9.75800   6.11500   1.000 8.03443   ? 33  PRO AA CD  1 
ATOM   249  N  N   . GLY A 1 34  ? 6.15200   10.68800  3.03100   1.000 8.87090   ? 34  GLY AA N   1 
ATOM   250  C  CA  . GLY A 1 34  ? 7.22600   9.94700   2.40600   1.000 4.92441   ? 34  GLY AA CA  1 
ATOM   251  C  C   . GLY A 1 34  ? 8.49600   10.77400  2.43500   1.000 7.90900   ? 34  GLY AA C   1 
ATOM   252  O  O   . GLY A 1 34  ? 8.47100   11.96100  2.76500   1.000 7.48222   ? 34  GLY AA O   1 
ATOM   253  N  N   . VAL A 1 35  ? 9.61300   10.13300  2.08800   1.000 11.58830  ? 35  VAL AA N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 10.90300  10.81400  2.11700   1.000 9.14036   ? 35  VAL AA CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 11.85500  10.11900  1.15600   1.000 10.17254  ? 35  VAL AA C   1 
ATOM   256  O  O   . VAL A 1 35  ? 11.74400  8.91500   0.90600   1.000 6.95429   ? 35  VAL AA O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 11.47900  10.86500  3.55600   1.000 6.54158   ? 35  VAL AA CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 12.00300  9.49900   3.98100   1.000 4.57258   ? 35  VAL AA CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 12.57200  11.92400  3.65900   1.000 9.97001   ? 35  VAL AA CG2 1 
ATOM   260  N  N   . ASP A 1 36  ? 12.78900  10.89300  0.60600   1.000 5.92820   ? 36  ASP AA N   1 
ATOM   261  C  CA  . ASP A 1 36  ? 13.89800  10.36800  -0.18600  1.000 5.83980   ? 36  ASP AA CA  1 
ATOM   262  C  C   . ASP A 1 36  ? 15.13000  11.18800  0.16800   1.000 7.69084   ? 36  ASP AA C   1 
ATOM   263  O  O   . ASP A 1 36  ? 15.21100  12.37100  -0.17600  1.000 8.58087   ? 36  ASP AA O   1 
ATOM   264  C  CB  . ASP A 1 36  ? 13.60400  10.43400  -1.68900  1.000 5.49971   ? 36  ASP AA CB  1 
ATOM   265  C  CG  . ASP A 1 36  ? 14.66700  9.73000   -2.53200  1.000 10.41815  ? 36  ASP AA CG  1 
ATOM   266  O  OD1 . ASP A 1 36  ? 15.84800  9.70000   -2.12700  1.000 9.81454   ? 36  ASP AA OD1 1 
ATOM   267  O  OD2 . ASP A 1 36  ? 14.32400  9.20600   -3.61000  1.000 13.49263  ? 36  ASP AA OD2 1 
ATOM   268  N  N   . VAL A 1 37  ? 16.07900  10.56500  0.85800   1.000 11.88174  ? 37  VAL AA N   1 
ATOM   269  C  CA  . VAL A 1 37  ? 17.35800  11.19300  1.17000   1.000 6.20510   ? 37  VAL AA CA  1 
ATOM   270  C  C   . VAL A 1 37  ? 18.34400  10.78800  0.08000   1.000 13.70518  ? 37  VAL AA C   1 
ATOM   271  O  O   . VAL A 1 37  ? 18.82000  9.65000   0.05300   1.000 11.93590  ? 37  VAL AA O   1 
ATOM   272  C  CB  . VAL A 1 37  ? 17.86200  10.78600  2.55900   1.000 9.51202   ? 37  VAL AA CB  1 
ATOM   273  C  CG1 . VAL A 1 37  ? 19.17300  11.49000  2.87000   1.000 5.16410   ? 37  VAL AA CG1 1 
ATOM   274  C  CG2 . VAL A 1 37  ? 16.81600  11.09600  3.61900   1.000 9.87632   ? 37  VAL AA CG2 1 
ATOM   275  N  N   . ARG A 1 38  ? 18.65000  11.71700  -0.82400  1.000 10.01959  ? 38  ARG AA N   1 
ATOM   276  C  CA  . ARG A 1 38  ? 19.52100  11.42500  -1.95700  1.000 10.84544  ? 38  ARG AA CA  1 
ATOM   277  C  C   . ARG A 1 38  ? 20.94500  11.93100  -1.77900  1.000 10.60581  ? 38  ARG AA C   1 
ATOM   278  O  O   . ARG A 1 38  ? 21.87400  11.33200  -2.33200  1.000 10.81455  ? 38  ARG AA O   1 
ATOM   279  C  CB  . ARG A 1 38  ? 18.93800  12.02100  -3.24300  1.000 9.98350   ? 38  ARG AA CB  1 
ATOM   280  C  CG  . ARG A 1 38  ? 19.52700  11.43500  -4.51700  1.000 13.53013  ? 38  ARG AA CG  1 
ATOM   281  C  CD  . ARG A 1 38  ? 19.06400  10.00100  -4.74300  1.000 12.09966  ? 38  ARG AA CD  1 
ATOM   282  N  NE  . ARG A 1 38  ? 17.62100  9.91100   -4.92700  1.000 14.65126  ? 38  ARG AA NE  1 
ATOM   283  C  CZ  . ARG A 1 38  ? 16.99300  10.18800  -6.06200  1.000 17.17176  ? 38  ARG AA CZ  1 
ATOM   284  N  NH1 . ARG A 1 38  ? 17.65400  10.57700  -7.14000  1.000 14.74489  ? 38  ARG AA NH1 1 
ATOM   285  N  NH2 . ARG A 1 38  ? 15.66900  10.07400  -6.11500  1.000 18.00705  ? 38  ARG AA NH2 1 
ATOM   286  N  N   . GLY A 1 39  ? 21.14300  13.01700  -1.03400  1.000 12.96172  ? 39  GLY AA N   1 
ATOM   287  C  CA  . GLY A 1 39  ? 22.48200  13.51600  -0.80900  1.000 9.15020   ? 39  GLY AA CA  1 
ATOM   288  C  C   . GLY A 1 39  ? 23.32200  12.56400  0.02000   1.000 13.49541  ? 39  GLY AA C   1 
ATOM   289  O  O   . GLY A 1 39  ? 22.81900  11.73000  0.77300   1.000 13.83818  ? 39  GLY AA O   1 
ATOM   290  N  N   . ALA A 1 40  ? 24.63700  12.69400  -0.12800  1.000 9.83600   ? 40  ALA AA N   1 
ATOM   291  C  CA  . ALA A 1 40  ? 25.58500  11.84100  0.57600   1.000 12.33225  ? 40  ALA AA CA  1 
ATOM   292  C  C   . ALA A 1 40  ? 26.01800  12.41200  1.92000   1.000 13.99686  ? 40  ALA AA C   1 
ATOM   293  O  O   . ALA A 1 40  ? 26.84500  11.79500  2.60000   1.000 14.79263  ? 40  ALA AA O   1 
ATOM   294  C  CB  . ALA A 1 40  ? 26.81900  11.59500  -0.29800  1.000 11.44104  ? 40  ALA AA CB  1 
ATOM   295  N  N   . ASN A 1 41  ? 25.47700  13.56100  2.32400   1.000 13.34628  ? 41  ASN AA N   1 
ATOM   296  C  CA  . ASN A 1 41  ? 25.91400  14.26100  3.52700   1.000 13.76758  ? 41  ASN AA CA  1 
ATOM   297  C  C   . ASN A 1 41  ? 24.70800  14.89600  4.22500   1.000 14.61157  ? 41  ASN AA C   1 
ATOM   298  O  O   . ASN A 1 41  ? 24.63800  16.10100  4.44300   1.000 12.40001  ? 41  ASN AA O   1 
ATOM   299  C  CB  . ASN A 1 41  ? 26.96600  15.31100  3.17500   1.000 11.87382  ? 41  ASN AA CB  1 
ATOM   300  C  CG  . ASN A 1 41  ? 27.93200  15.57800  4.30900   1.000 22.03880  ? 41  ASN AA CG  1 
ATOM   301  O  OD1 . ASN A 1 41  ? 27.55200  15.56700  5.47900   1.000 26.13759  ? 41  ASN AA OD1 1 
ATOM   302  N  ND2 . ASN A 1 41  ? 29.19100  15.82800  3.96700   1.000 36.79894  ? 41  ASN AA ND2 1 
ATOM   303  N  N   . ALA A 1 42  ? 23.73500  14.06900  4.59400   1.000 10.46060  ? 42  ALA AA N   1 
ATOM   304  C  CA  . ALA A 1 42  ? 22.48800  14.54600  5.17000   1.000 11.29908  ? 42  ALA AA CA  1 
ATOM   305  C  C   . ALA A 1 42  ? 22.42800  14.26100  6.66500   1.000 16.69793  ? 42  ALA AA C   1 
ATOM   306  O  O   . ALA A 1 42  ? 22.94900  13.25100  7.14700   1.000 19.07568  ? 42  ALA AA O   1 
ATOM   307  C  CB  . ALA A 1 42  ? 21.28200  13.90700  4.47800   1.000 6.22492   ? 42  ALA AA CB  1 
ATOM   308  N  N   . ALA A 1 43  ? 21.78100  15.17000  7.39200   1.000 10.68634  ? 43  ALA AA N   1 
ATOM   309  C  CA  . ALA A 1 43  ? 21.50100  15.00600  8.81300   1.000 12.34975  ? 43  ALA AA CA  1 
ATOM   310  C  C   . ALA A 1 43  ? 20.00800  15.20800  9.01800   1.000 10.90899  ? 43  ALA AA C   1 
ATOM   311  O  O   . ALA A 1 43  ? 19.48500  16.29600  8.75200   1.000 8.22458   ? 43  ALA AA O   1 
ATOM   312  C  CB  . ALA A 1 43  ? 22.30600  15.99500  9.66000   1.000 2.58936   ? 43  ALA AA CB  1 
ATOM   313  N  N   . THR A 1 44  ? 19.32000  14.15700  9.46600   1.000 4.24881   ? 44  THR AA N   1 
ATOM   314  C  CA  . THR A 1 44  ? 17.86900  14.17300  9.58500   1.000 6.22671   ? 44  THR AA CA  1 
ATOM   315  C  C   . THR A 1 44  ? 17.45600  13.54800  10.91100  1.000 6.22930   ? 44  THR AA C   1 
ATOM   316  O  O   . THR A 1 44  ? 18.27700  12.99000  11.64600  1.000 7.08209   ? 44  THR AA O   1 
ATOM   317  C  CB  . THR A 1 44  ? 17.19100  13.42300  8.42700   1.000 9.95161   ? 44  THR AA CB  1 
ATOM   318  O  OG1 . THR A 1 44  ? 17.47800  12.02400  8.53000   1.000 6.84837   ? 44  THR AA OG1 1 
ATOM   319  C  CG2 . THR A 1 44  ? 17.67400  13.94000  7.07500   1.000 6.11537   ? 44  THR AA CG2 1 
ATOM   320  N  N   . ILE A 1 45  ? 16.16000  13.63700  11.20500  1.000 2.08167   ? 45  ILE AA N   1 
ATOM   321  C  CA  . ILE A 1 45  ? 15.57900  13.04800  12.40700  1.000 3.35796   ? 45  ILE AA CA  1 
ATOM   322  C  C   . ILE A 1 45  ? 14.17700  12.54800  12.07500  1.000 8.38407   ? 45  ILE AA C   1 
ATOM   323  O  O   . ILE A 1 45  ? 13.45500  13.16700  11.28600  1.000 7.99974   ? 45  ILE AA O   1 
ATOM   324  C  CB  . ILE A 1 45  ? 15.55700  14.05900  13.57600  1.000 6.67855   ? 45  ILE AA CB  1 
ATOM   325  C  CG1 . ILE A 1 45  ? 15.13200  13.38000  14.88100  1.000 7.34910   ? 45  ILE AA CG1 1 
ATOM   326  C  CG2 . ILE A 1 45  ? 14.65200  15.24500  13.26200  1.000 4.77236   ? 45  ILE AA CG2 1 
ATOM   327  C  CD1 . ILE A 1 45  ? 15.12200  14.31200  16.07700  1.000 7.82292   ? 45  ILE AA CD1 1 
ATOM   328  N  N   . TYR A 1 46  ? 13.81000  11.40000  12.65700  1.000 7.02298   ? 46  TYR AA N   1 
ATOM   329  C  CA  . TYR A 1 46  ? 12.47600  10.80500  12.53400  1.000 4.00838   ? 46  TYR AA CA  1 
ATOM   330  C  C   . TYR A 1 46  ? 12.15200  10.34300  11.11200  1.000 13.41714  ? 46  TYR AA C   1 
ATOM   331  O  O   . TYR A 1 46  ? 10.97900  10.26100  10.74300  1.000 20.54453  ? 46  TYR AA O   1 
ATOM   332  C  CB  . TYR A 1 46  ? 11.37800  11.76400  13.01200  1.000 4.76657   ? 46  TYR AA CB  1 
ATOM   333  C  CG  . TYR A 1 46  ? 11.48900  12.24000  14.44400  1.000 9.62134   ? 46  TYR AA CG  1 
ATOM   334  C  CD1 . TYR A 1 46  ? 11.66700  11.34300  15.49000  1.000 12.52199  ? 46  TYR AA CD1 1 
ATOM   335  C  CD2 . TYR A 1 46  ? 11.38600  13.59100  14.74900  1.000 6.41568   ? 46  TYR AA CD2 1 
ATOM   336  C  CE1 . TYR A 1 46  ? 11.75400  11.78600  16.80000  1.000 4.57795   ? 46  TYR AA CE1 1 
ATOM   337  C  CE2 . TYR A 1 46  ? 11.47200  14.04300  16.04900  1.000 11.07728  ? 46  TYR AA CE2 1 
ATOM   338  C  CZ  . TYR A 1 46  ? 11.65600  13.13800  17.07100  1.000 13.92314  ? 46  TYR AA CZ  1 
ATOM   339  O  OH  . TYR A 1 46  ? 11.74100  13.59200  18.36700  1.000 9.08672   ? 46  TYR AA OH  1 
ATOM   340  N  N   . THR A 1 47  ? 13.15700  10.02200  10.29400  1.000 8.89995   ? 47  THR AA N   1 
ATOM   341  C  CA  . THR A 1 47  ? 12.86200  9.64400   8.91300   1.000 13.20839  ? 47  THR AA CA  1 
ATOM   342  C  C   . THR A 1 47  ? 12.48300  8.17500   8.75500   1.000 11.98936  ? 47  THR AA C   1 
ATOM   343  O  O   . THR A 1 47  ? 11.87500  7.81900   7.73900   1.000 11.37765  ? 47  THR AA O   1 
ATOM   344  C  CB  . THR A 1 47  ? 14.04900  9.95200   7.99500   1.000 7.71488   ? 47  THR AA CB  1 
ATOM   345  O  OG1 . THR A 1 47  ? 15.25200  9.41400   8.55500   1.000 14.96062  ? 47  THR AA OG1 1 
ATOM   346  C  CG2 . THR A 1 47  ? 14.20200  11.45300  7.80200   1.000 8.92875   ? 47  THR AA CG2 1 
ATOM   347  N  N   . ASP A 1 48  ? 12.81700  7.31800   9.72500   1.000 13.56896  ? 48  ASP AA N   1 
ATOM   348  C  CA  . ASP A 1 48  ? 12.53700  5.89100   9.57400   1.000 19.32910  ? 48  ASP AA CA  1 
ATOM   349  C  C   . ASP A 1 48  ? 11.04300  5.60800   9.48700   1.000 12.74144  ? 48  ASP AA C   1 
ATOM   350  O  O   . ASP A 1 48  ? 10.62800  4.68300   8.77900   1.000 17.19975  ? 48  ASP AA O   1 
ATOM   351  C  CB  . ASP A 1 48  ? 13.15200  5.10300   10.72800  1.000 12.95158  ? 48  ASP AA CB  1 
ATOM   352  C  CG  . ASP A 1 48  ? 14.66400  5.17500   10.74300  1.000 27.42233  ? 48  ASP AA CG  1 
ATOM   353  O  OD1 . ASP A 1 48  ? 15.29500  4.70600   9.77000   1.000 10.16409  ? 48  ASP AA OD1 1 
ATOM   354  O  OD2 . ASP A 1 48  ? 15.22000  5.70000   11.73000  1.000 18.84592  ? 48  ASP AA OD2 1 
ATOM   355  N  N   . LEU A 1 49  ? 10.22200  6.38300   10.19100  1.000 10.83008  ? 49  LEU AA N   1 
ATOM   356  C  CA  . LEU A 1 49  ? 8.77700   6.19700   10.13500  1.000 9.83969   ? 49  LEU AA CA  1 
ATOM   357  C  C   . LEU A 1 49  ? 8.15500   6.75200   8.86300   1.000 11.42189  ? 49  LEU AA C   1 
ATOM   358  O  O   . LEU A 1 49  ? 6.93100   6.67800   8.71100   1.000 12.15183  ? 49  LEU AA O   1 
ATOM   359  C  CB  . LEU A 1 49  ? 8.11200   6.84300   11.35200  1.000 15.54123  ? 49  LEU AA CB  1 
ATOM   360  C  CG  . LEU A 1 49  ? 8.53400   6.28500   12.71000  1.000 23.02460  ? 49  LEU AA CG  1 
ATOM   361  C  CD1 . LEU A 1 49  ? 8.63700   7.39200   13.75200  1.000 33.47810  ? 49  LEU AA CD1 1 
ATOM   362  C  CD2 . LEU A 1 49  ? 7.56700   5.19800   13.15500  1.000 17.31328  ? 49  LEU AA CD2 1 
ATOM   363  N  N   . LEU A 1 50  ? 8.95500   7.29700   7.95100   1.000 9.70251   ? 50  LEU AA N   1 
ATOM   364  C  CA  . LEU A 1 50  ? 8.44700   7.88800   6.72400   1.000 8.64970   ? 50  LEU AA CA  1 
ATOM   365  C  C   . LEU A 1 50  ? 8.58800   6.96300   5.52300   1.000 19.25746  ? 50  LEU AA C   1 
ATOM   366  O  O   . LEU A 1 50  ? 8.21000   7.34800   4.41200   1.000 21.86874  ? 50  LEU AA O   1 
ATOM   367  C  CB  . LEU A 1 50  ? 9.16200   9.21700   6.44800   1.000 10.82961  ? 50  LEU AA CB  1 
ATOM   368  C  CG  . LEU A 1 50  ? 8.48500   10.49800  6.94800   1.000 16.71813  ? 50  LEU AA CG  1 
ATOM   369  C  CD1 . LEU A 1 50  ? 7.92100   10.32300  8.35300   1.000 15.70988  ? 50  LEU AA CD1 1 
ATOM   370  C  CD2 . LEU A 1 50  ? 9.45300   11.67400  6.90500   1.000 8.75815   ? 50  LEU AA CD2 1 
ATOM   371  N  N   . TYR A 1 51  ? 9.11300   5.75600   5.71900   1.000 19.63759  ? 51  TYR AA N   1 
ATOM   372  C  CA  . TYR A 1 51  ? 9.32500   4.78100   4.66100   1.000 12.83030  ? 51  TYR AA CA  1 
ATOM   373  C  C   . TYR A 1 51  ? 8.13700   3.83100   4.56500   1.000 17.68253  ? 51  TYR AA C   1 
ATOM   374  O  O   . TYR A 1 51  ? 7.40900   3.62900   5.54200   1.000 12.84936  ? 51  TYR AA O   1 
ATOM   375  C  CB  . TYR A 1 51  ? 10.61300  4.00400   4.92400   1.000 15.87032  ? 51  TYR AA CB  1 
ATOM   376  C  CG  . TYR A 1 51  ? 11.86400  4.84100   4.76000   1.000 13.72135  ? 51  TYR AA CG  1 
ATOM   377  C  CD1 . TYR A 1 51  ? 12.35600  5.15100   3.49900   1.000 11.57285  ? 51  TYR AA CD1 1 
ATOM   378  C  CD2 . TYR A 1 51  ? 12.54800  5.32800   5.86700   1.000 18.36767  ? 51  TYR AA CD2 1 
ATOM   379  C  CE1 . TYR A 1 51  ? 13.49800  5.91700   3.34400   1.000 21.41661  ? 51  TYR AA CE1 1 
ATOM   380  C  CE2 . TYR A 1 51  ? 13.69100  6.09500   5.72200   1.000 19.74231  ? 51  TYR AA CE2 1 
ATOM   381  C  CZ  . TYR A 1 51  ? 14.16100  6.38600   4.45800   1.000 18.36528  ? 51  TYR AA CZ  1 
ATOM   382  O  OH  . TYR A 1 51  ? 15.29700  7.14900   4.30900   1.000 16.53078  ? 51  TYR AA OH  1 
ATOM   383  N  N   . PRO A 1 52  ? 7.90800   3.23000   3.39000   1.000 18.80910  ? 52  PRO AA N   1 
ATOM   384  C  CA  . PRO A 1 52  ? 6.69500   2.41100   3.21500   1.000 13.91169  ? 52  PRO AA CA  1 
ATOM   385  C  C   . PRO A 1 52  ? 6.63100   1.19800   4.12600   1.000 20.55837  ? 52  PRO AA C   1 
ATOM   386  O  O   . PRO A 1 52  ? 5.52800   0.77200   4.49200   1.000 17.57031  ? 52  PRO AA O   1 
ATOM   387  C  CB  . PRO A 1 52  ? 6.76200   1.99600   1.73700   1.000 8.99462   ? 52  PRO AA CB  1 
ATOM   388  C  CG  . PRO A 1 52  ? 7.67500   2.98200   1.09400   1.000 11.75137  ? 52  PRO AA CG  1 
ATOM   389  C  CD  . PRO A 1 52  ? 8.67900   3.34500   2.14100   1.000 16.99449  ? 52  PRO AA CD  1 
ATOM   390  N  N   . ASP A 1 53  ? 7.77300   0.62900   4.50700   1.000 15.80292  ? 53  ASP AA N   1 
ATOM   391  C  CA  . ASP A 1 53  ? 7.79300   -0.56200  5.34600   1.000 25.41138  ? 53  ASP AA CA  1 
ATOM   392  C  C   . ASP A 1 53  ? 7.58400   -0.26000  6.82500   1.000 27.44422  ? 53  ASP AA C   1 
ATOM   393  O  O   . ASP A 1 53  ? 7.63800   -1.18500  7.64200   1.000 24.05333  ? 53  ASP AA O   1 
ATOM   394  C  CB  . ASP A 1 53  ? 9.11200   -1.31600  5.15200   1.000 19.12423  ? 53  ASP AA CB  1 
ATOM   395  C  CG  . ASP A 1 53  ? 10.32000  -0.47600  5.51100   1.000 33.24064  ? 53  ASP AA CG  1 
ATOM   396  O  OD1 . ASP A 1 53  ? 10.82900  0.24500   4.62700   1.000 49.51983  ? 53  ASP AA OD1 1 
ATOM   397  O  OD2 . ASP A 1 53  ? 10.75600  -0.53300  6.68000   1.000 75.09184  ? 53  ASP AA OD2 1 
ATOM   398  N  N   A SER A 1 54  ? 7.34800   0.99600   7.18800   0.742 19.53439  ? 54  SER AA N   1 
ATOM   399  N  N   B SER A 1 54  ? 7.35200   0.99600   7.18800   0.258 19.55032  ? 54  SER AA N   1 
ATOM   400  C  CA  A SER A 1 54  ? 7.09200   1.38400   8.56600   0.742 18.19054  ? 54  SER AA CA  1 
ATOM   401  C  CA  B SER A 1 54  ? 7.09200   1.37800   8.56700   0.258 18.19390  ? 54  SER AA CA  1 
ATOM   402  C  C   A SER A 1 54  ? 5.60500   1.64700   8.77500   0.742 17.27152  ? 54  SER AA C   1 
ATOM   403  C  C   B SER A 1 54  ? 5.60100   1.62200   8.77400   0.258 17.28362  ? 54  SER AA C   1 
ATOM   404  O  O   A SER A 1 54  ? 4.83700   1.80700   7.82300   0.742 16.56024  ? 54  SER AA O   1 
ATOM   405  O  O   B SER A 1 54  ? 4.82400   1.74200   7.82500   0.258 16.62962  ? 54  SER AA O   1 
ATOM   406  C  CB  A SER A 1 54  ? 7.90100   2.62900   8.94200   0.742 18.22301  ? 54  SER AA CB  1 
ATOM   407  C  CB  B SER A 1 54  ? 7.89800   2.62600   8.94200   0.258 18.14098  ? 54  SER AA CB  1 
ATOM   408  O  OG  A SER A 1 54  ? 9.26400   2.30600   9.15700   0.742 15.32742  ? 54  SER AA OG  1 
ATOM   409  O  OG  B SER A 1 54  ? 7.75300   3.63900   7.96200   0.258 13.81299  ? 54  SER AA OG  1 
ATOM   410  N  N   . VAL A 1 55  ? 5.20700   1.69500   10.04400  1.000 13.75109  ? 55  VAL AA N   1 
ATOM   411  C  CA  . VAL A 1 55  ? 3.81000   1.92400   10.39600  1.000 15.95604  ? 55  VAL AA CA  1 
ATOM   412  C  C   . VAL A 1 55  ? 3.42000   3.35400   10.04200  1.000 20.21874  ? 55  VAL AA C   1 
ATOM   413  O  O   . VAL A 1 55  ? 4.28100   4.20100   9.77800   1.000 15.02650  ? 55  VAL AA O   1 
ATOM   414  C  CB  . VAL A 1 55  ? 3.55300   1.63200   11.88500  1.000 21.44010  ? 55  VAL AA CB  1 
ATOM   415  C  CG1 . VAL A 1 55  ? 3.81300   0.16400   12.18600  1.000 18.12520  ? 55  VAL AA CG1 1 
ATOM   416  C  CG2 . VAL A 1 55  ? 4.42000   2.52400   12.75800  1.000 24.17495  ? 55  VAL AA CG2 1 
ATOM   417  N  N   . MET A 1 56  ? 2.12200   3.61800   10.02100  1.000 19.65004  ? 56  MET AA N   1 
ATOM   418  C  CA  . MET A 1 56  ? 1.57300   4.94300   9.76200   1.000 15.84178  ? 56  MET AA CA  1 
ATOM   419  C  C   . MET A 1 56  ? 1.82200   5.84900   10.96000  1.000 19.32650  ? 56  MET AA C   1 
ATOM   420  O  O   . MET A 1 56  ? 1.22300   5.62500   12.02100  1.000 25.08743  ? 56  MET AA O   1 
ATOM   421  C  CB  . MET A 1 56  ? 0.07100   4.83900   9.49400   1.000 19.14522  ? 56  MET AA CB  1 
ATOM   422  C  CG  . MET A 1 56  ? -0.57400  6.04300   8.82000   1.000 21.07082  ? 56  MET AA CG  1 
ATOM   423  S  SD  . MET A 1 56  ? 0.45700   6.97900   7.67800   1.000 29.16064  ? 56  MET AA SD  1 
ATOM   424  C  CE  . MET A 1 56  ? -0.04500  6.24400   6.12700   1.000 19.54730  ? 56  MET AA CE  1 
ATOM   425  N  N   . PRO A 1 57  ? 2.67300   6.86100   10.85400  1.000 24.91401  ? 57  PRO AA N   1 
ATOM   426  C  CA  . PRO A 1 57  ? 2.87900   7.78200   11.97100  1.000 16.35836  ? 57  PRO AA CA  1 
ATOM   427  C  C   . PRO A 1 57  ? 1.90400   8.95300   11.90000  1.000 16.40614  ? 57  PRO AA C   1 
ATOM   428  O  O   . PRO A 1 57  ? 1.15200   9.11800   10.93900  1.000 17.98104  ? 57  PRO AA O   1 
ATOM   429  C  CB  . PRO A 1 57  ? 4.32000   8.25400   11.75700  1.000 13.84730  ? 57  PRO AA CB  1 
ATOM   430  C  CG  . PRO A 1 57  ? 4.48000   8.24200   10.25400  1.000 20.64683  ? 57  PRO AA CG  1 
ATOM   431  C  CD  . PRO A 1 57  ? 3.50000   7.22500   9.69000   1.000 16.47028  ? 57  PRO AA CD  1 
ATOM   432  N  N   A SER A 1 58  ? 1.93200   9.76500   12.95200  0.425 18.38855  ? 58  SER AA N   1 
ATOM   433  N  N   B SER A 1 58  ? 1.93300   9.76500   12.95200  0.540 18.40257  ? 58  SER AA N   1 
ATOM   434  N  N   C SER A 1 58  ? 1.94000   9.77300   12.94800  0.035 18.35397  ? 58  SER AA N   1 
ATOM   435  C  CA  A SER A 1 58  ? 1.12500   10.97900  13.04700  0.425 18.66854  ? 58  SER AA CA  1 
ATOM   436  C  CA  B SER A 1 58  ? 1.12500   10.97800  13.04800  0.540 18.68617  ? 58  SER AA CA  1 
ATOM   437  C  CA  C SER A 1 58  ? 1.12300   10.98000  13.04300  0.035 18.59902  ? 58  SER AA CA  1 
ATOM   438  C  C   A SER A 1 58  ? 2.07800   12.16800  12.95400  0.425 18.25717  ? 58  SER AA C   1 
ATOM   439  C  C   B SER A 1 58  ? 2.07900   12.16700  12.95400  0.540 18.28370  ? 58  SER AA C   1 
ATOM   440  C  C   C SER A 1 58  ? 2.05900   12.18300  12.95400  0.035 18.13920  ? 58  SER AA C   1 
ATOM   441  O  O   A SER A 1 58  ? 2.53100   12.70300  13.96700  0.425 15.24192  ? 58  SER AA O   1 
ATOM   442  O  O   B SER A 1 58  ? 2.53600   12.70000  13.96700  0.540 15.22601  ? 58  SER AA O   1 
ATOM   443  O  O   C SER A 1 58  ? 2.48500   12.74600  13.96400  0.035 15.35345  ? 58  SER AA O   1 
ATOM   444  C  CB  A SER A 1 58  ? 0.31100   11.00400  14.33700  0.425 17.64048  ? 58  SER AA CB  1 
ATOM   445  C  CB  B SER A 1 58  ? 0.31400   11.00200  14.34100  0.540 17.62075  ? 58  SER AA CB  1 
ATOM   446  C  CB  C SER A 1 58  ? 0.30100   10.99000  14.33900  0.035 17.69587  ? 58  SER AA CB  1 
ATOM   447  O  OG  A SER A 1 58  ? -0.79700  10.12600  14.25200  0.425 19.66126  ? 58  SER AA OG  1 
ATOM   448  O  OG  B SER A 1 58  ? -0.59700  12.08700  14.34700  0.540 14.31853  ? 58  SER AA OG  1 
ATOM   449  O  OG  C SER A 1 58  ? 1.12100   11.25100  15.46400  0.035 18.68189  ? 58  SER AA OG  1 
ATOM   450  N  N   . VAL A 1 59  ? 2.38100   12.57400  11.72300  1.000 15.91512  ? 59  VAL AA N   1 
ATOM   451  C  CA  . VAL A 1 59  ? 3.29600   13.68600  11.49600  1.000 16.83475  ? 59  VAL AA CA  1 
ATOM   452  C  C   . VAL A 1 59  ? 2.58900   14.99000  11.84000  1.000 9.95122   ? 59  VAL AA C   1 
ATOM   453  O  O   . VAL A 1 59  ? 1.60900   15.37400  11.19100  1.000 16.55955  ? 59  VAL AA O   1 
ATOM   454  C  CB  . VAL A 1 59  ? 3.80200   13.69100  10.04900  1.000 20.50261  ? 59  VAL AA CB  1 
ATOM   455  C  CG1 . VAL A 1 59  ? 4.70900   14.88700  9.80700   1.000 13.25847  ? 59  VAL AA CG1 1 
ATOM   456  C  CG2 . VAL A 1 59  ? 4.52900   12.39100  9.74000   1.000 13.68886  ? 59  VAL AA CG2 1 
ATOM   457  N  N   . THR A 1 60  ? 3.08400   15.67500  12.87200  1.000 10.57599  ? 60  THR AA N   1 
ATOM   458  C  CA  . THR A 1 60  ? 2.49900   16.95100  13.26700  1.000 12.70749  ? 60  THR AA CA  1 
ATOM   459  C  C   . THR A 1 60  ? 3.02000   18.09000  12.40100  1.000 16.89784  ? 60  THR AA C   1 
ATOM   460  O  O   . THR A 1 60  ? 2.28100   19.03300  12.09400  1.000 17.08164  ? 60  THR AA O   1 
ATOM   461  C  CB  . THR A 1 60  ? 2.79200   17.22600  14.74100  1.000 17.01034  ? 60  THR AA CB  1 
ATOM   462  O  OG1 . THR A 1 60  ? 2.75700   15.99400  15.47000  1.000 20.60993  ? 60  THR AA OG1 1 
ATOM   463  C  CG2 . THR A 1 60  ? 1.75700   18.17800  15.32200  1.000 14.88341  ? 60  THR AA CG2 1 
ATOM   464  N  N   . GLY A 1 61  ? 4.28500   18.01600  12.00300  1.000 10.72365  ? 61  GLY AA N   1 
ATOM   465  C  CA  . GLY A 1 61  ? 4.87900   19.01400  11.13400  1.000 7.31504   ? 61  GLY AA CA  1 
ATOM   466  C  C   . GLY A 1 61  ? 6.21600   18.52400  10.62900  1.000 9.33514   ? 61  GLY AA C   1 
ATOM   467  O  O   . GLY A 1 61  ? 6.75700   17.52400  11.10700  1.000 15.76012  ? 61  GLY AA O   1 
ATOM   468  N  N   . ILE A 1 62  ? 6.74300   19.24500  9.64200   1.000 7.37227   ? 62  ILE AA N   1 
ATOM   469  C  CA  . ILE A 1 62  ? 8.05600   18.96500  9.07500   1.000 8.45234   ? 62  ILE AA CA  1 
ATOM   470  C  C   . ILE A 1 62  ? 8.85300   20.26000  9.06300   1.000 9.41975   ? 62  ILE AA C   1 
ATOM   471  O  O   . ILE A 1 62  ? 8.32700   21.31900  8.70300   1.000 6.26534   ? 62  ILE AA O   1 
ATOM   472  C  CB  . ILE A 1 62  ? 7.95200   18.36100  7.65700   1.000 7.08597   ? 62  ILE AA CB  1 
ATOM   473  C  CG1 . ILE A 1 62  ? 7.30500   16.97600  7.71700   1.000 6.40151   ? 62  ILE AA CG1 1 
ATOM   474  C  CG2 . ILE A 1 62  ? 9.32000   18.27700  6.99800   1.000 7.69645   ? 62  ILE AA CG2 1 
ATOM   475  C  CD1 . ILE A 1 62  ? 6.85500   16.45400  6.37000   1.000 11.07158  ? 62  ILE AA CD1 1 
ATOM   476  N  N   . MET A 1 63  ? 10.11900  20.17800  9.46400   1.000 6.89882   ? 63  MET AA N   1 
ATOM   477  C  CA  . MET A 1 63  ? 10.96400  21.35000  9.63700   1.000 10.53346  ? 63  MET AA CA  1 
ATOM   478  C  C   . MET A 1 63  ? 12.13400  21.33700  8.66400   1.000 9.74344   ? 63  MET AA C   1 
ATOM   479  O  O   . MET A 1 63  ? 12.76100  20.29800  8.43600   1.000 9.81378   ? 63  MET AA O   1 
ATOM   480  C  CB  . MET A 1 63  ? 11.50100  21.43600  11.06900  1.000 10.33742  ? 63  MET AA CB  1 
ATOM   481  C  CG  . MET A 1 63  ? 11.92100  22.83600  11.47900  1.000 15.69297  ? 63  MET AA CG  1 
ATOM   482  S  SD  . MET A 1 63  ? 12.48500  22.92800  13.18700  1.000 22.21276  ? 63  MET AA SD  1 
ATOM   483  C  CE  . MET A 1 63  ? 11.03800  23.63800  13.96600  1.000 12.67991  ? 63  MET AA CE  1 
ATOM   484  N  N   . LEU A 1 64  ? 12.42100  22.50800  8.10000   1.000 14.37710  ? 64  LEU AA N   1 
ATOM   485  C  CA  . LEU A 1 64  ? 13.63900  22.76300  7.34200   1.000 10.72660  ? 64  LEU AA CA  1 
ATOM   486  C  C   . LEU A 1 64  ? 14.43300  23.80800  8.10900   1.000 9.62650   ? 64  LEU AA C   1 
ATOM   487  O  O   . LEU A 1 64  ? 13.96900  24.94000  8.27900   1.000 8.45125   ? 64  LEU AA O   1 
ATOM   488  C  CB  . LEU A 1 64  ? 13.32000  23.24700  5.92600   1.000 4.90156   ? 64  LEU AA CB  1 
ATOM   489  C  CG  . LEU A 1 64  ? 12.18700  22.50700  5.21300   1.000 9.84044   ? 64  LEU AA CG  1 
ATOM   490  C  CD1 . LEU A 1 64  ? 11.78400  23.23600  3.94100   1.000 7.30345   ? 64  LEU AA CD1 1 
ATOM   491  C  CD2 . LEU A 1 64  ? 12.58800  21.07100  4.90900   1.000 6.32189   ? 64  LEU AA CD2 1 
ATOM   492  N  N   . THR A 1 65  ? 15.61700  23.43100  8.58400   1.000 7.42572   ? 65  THR AA N   1 
ATOM   493  C  CA  . THR A 1 65  ? 16.35500  24.25400  9.52900   1.000 9.97921   ? 65  THR AA CA  1 
ATOM   494  C  C   . THR A 1 65  ? 17.81000  24.38900  9.11100   1.000 13.35416  ? 65  THR AA C   1 
ATOM   495  O  O   . THR A 1 65  ? 18.37100  23.51600  8.44500   1.000 11.90815  ? 65  THR AA O   1 
ATOM   496  C  CB  . THR A 1 65  ? 16.28700  23.66900  10.95100  1.000 8.61564   ? 65  THR AA CB  1 
ATOM   497  O  OG1 . THR A 1 65  ? 16.98700  24.52900  11.85700  1.000 15.72079  ? 65  THR AA OG1 1 
ATOM   498  C  CG2 . THR A 1 65  ? 16.91500  22.28300  10.99300  1.000 10.22122  ? 65  THR AA CG2 1 
ATOM   499  N  N   . GLY A 1 66  ? 18.41500  25.50700  9.50600   1.000 14.86183  ? 66  GLY AA N   1 
ATOM   500  C  CA  . GLY A 1 66  ? 19.84600  25.68300  9.41300   1.000 8.84781   ? 66  GLY AA CA  1 
ATOM   501  C  C   . GLY A 1 66  ? 20.54100  25.16000  10.65500  1.000 10.11019  ? 66  GLY AA C   1 
ATOM   502  O  O   . GLY A 1 66  ? 19.96400  24.44300  11.47400  1.000 7.01760   ? 66  GLY AA O   1 
ATOM   503  N  N   . GLY A 1 67  ? 21.80900  25.53400  10.79000  1.000 12.44512  ? 67  GLY AA N   1 
ATOM   504  C  CA  . GLY A 1 67  ? 22.58600  25.15900  11.95300  1.000 9.39664   ? 67  GLY AA CA  1 
ATOM   505  C  C   . GLY A 1 67  ? 23.35900  23.86500  11.83500  1.000 12.75080  ? 67  GLY AA C   1 
ATOM   506  O  O   . GLY A 1 67  ? 23.95400  23.43200  12.82900  1.000 11.98011  ? 67  GLY AA O   1 
ATOM   507  N  N   . SER A 1 68  ? 23.37200  23.24100  10.66300  1.000 5.23038   ? 68  SER AA N   1 
ATOM   508  C  CA  . SER A 1 68  ? 24.07700  21.96700  10.42300  1.000 10.04513  ? 68  SER AA CA  1 
ATOM   509  C  C   . SER A 1 68  ? 23.53600  20.93700  11.42200  1.000 9.08771   ? 68  SER AA C   1 
ATOM   510  O  O   . SER A 1 68  ? 22.33000  20.93300  11.71300  1.000 8.93022   ? 68  SER AA O   1 
ATOM   511  C  CB  . SER A 1 68  ? 25.57400  22.19000  10.47300  1.000 8.56542   ? 68  SER AA CB  1 
ATOM   512  O  OG  . SER A 1 68  ? 26.27600  20.98700  10.21400  1.000 7.15203   ? 68  SER AA OG  1 
ATOM   513  N  N   . ALA A 1 69  ? 24.39100  20.07100  11.97400  1.000 7.61010   ? 69  ALA AA N   1 
ATOM   514  C  CA  . ALA A 1 69  ? 23.91000  19.00300  12.84600  1.000 11.81468  ? 69  ALA AA CA  1 
ATOM   515  C  C   . ALA A 1 69  ? 23.28400  19.54400  14.12600  1.000 14.15712  ? 69  ALA AA C   1 
ATOM   516  O  O   . ALA A 1 69  ? 22.42100  18.88500  14.71800  1.000 13.21848  ? 69  ALA AA O   1 
ATOM   517  C  CB  . ALA A 1 69  ? 25.05400  18.04600  13.18100  1.000 13.35251  ? 69  ALA AA CB  1 
ATOM   518  N  N   . PHE A 1 70  ? 23.70300  20.73100  14.57400  1.000 10.84688  ? 70  PHE AA N   1 
ATOM   519  C  CA  . PHE A 1 70  ? 23.14000  21.29600  15.79700  1.000 9.21303   ? 70  PHE AA CA  1 
ATOM   520  C  C   . PHE A 1 70  ? 21.67300  21.66900  15.62500  1.000 11.82188  ? 70  PHE AA C   1 
ATOM   521  O  O   . PHE A 1 70  ? 20.90700  21.62900  16.59500  1.000 10.74079  ? 70  PHE AA O   1 
ATOM   522  C  CB  . PHE A 1 70  ? 23.93100  22.53100  16.23000  1.000 14.47173  ? 70  PHE AA CB  1 
ATOM   523  C  CG  . PHE A 1 70  ? 25.40900  22.29700  16.37200  1.000 13.21933  ? 70  PHE AA CG  1 
ATOM   524  C  CD1 . PHE A 1 70  ? 25.92800  21.74200  17.53100  1.000 15.22270  ? 70  PHE AA CD1 1 
ATOM   525  C  CD2 . PHE A 1 70  ? 26.28000  22.65400  15.35700  1.000 11.55799  ? 70  PHE AA CD2 1 
ATOM   526  C  CE1 . PHE A 1 70  ? 27.28900  21.53400  17.66700  1.000 15.73353  ? 70  PHE AA CE1 1 
ATOM   527  C  CE2 . PHE A 1 70  ? 27.64000  22.44900  15.48700  1.000 15.18920  ? 70  PHE AA CE2 1 
ATOM   528  C  CZ  . PHE A 1 70  ? 28.14500  21.88800  16.64500  1.000 15.40939  ? 70  PHE AA CZ  1 
ATOM   529  N  N   . GLY A 1 71  ? 21.26500  22.02400  14.40300  1.000 4.39125   ? 71  GLY AA N   1 
ATOM   530  C  CA  . GLY A 1 71  ? 19.95300  22.60700  14.17400  1.000 5.82138   ? 71  GLY AA CA  1 
ATOM   531  C  C   . GLY A 1 71  ? 18.79100  21.66300  14.39100  1.000 11.06872  ? 71  GLY AA C   1 
ATOM   532  O  O   . GLY A 1 71  ? 17.65100  22.12400  14.51400  1.000 10.97118  ? 71  GLY AA O   1 
ATOM   533  N  N   . LEU A 1 72  ? 19.04500  20.35300  14.43700  1.000 6.75391   ? 72  LEU AA N   1 
ATOM   534  C  CA  . LEU A 1 72  ? 17.97100  19.40700  14.71200  1.000 8.53618   ? 72  LEU AA CA  1 
ATOM   535  C  C   . LEU A 1 72  ? 17.37500  19.59400  16.10200  1.000 7.59660   ? 72  LEU AA C   1 
ATOM   536  O  O   . LEU A 1 72  ? 16.29200  19.06200  16.37200  1.000 7.85029   ? 72  LEU AA O   1 
ATOM   537  C  CB  . LEU A 1 72  ? 18.48100  17.97400  14.53900  1.000 6.24291   ? 72  LEU AA CB  1 
ATOM   538  C  CG  . LEU A 1 72  ? 18.68000  17.54900  13.08100  1.000 3.69863   ? 72  LEU AA CG  1 
ATOM   539  C  CD1 . LEU A 1 72  ? 19.22000  16.13300  12.98100  1.000 5.44929   ? 72  LEU AA CD1 1 
ATOM   540  C  CD2 . LEU A 1 72  ? 17.38000  17.68900  12.30100  1.000 9.76890   ? 72  LEU AA CD2 1 
ATOM   541  N  N   . GLU A 1 73  ? 18.05100  20.33900  16.98100  1.000 5.90202   ? 73  GLU AA N   1 
ATOM   542  C  CA  . GLU A 1 73  ? 17.47100  20.68400  18.27400  1.000 9.39722   ? 73  GLU AA CA  1 
ATOM   543  C  C   . GLU A 1 73  ? 16.17300  21.46500  18.11400  1.000 12.19403  ? 73  GLU AA C   1 
ATOM   544  O  O   . GLU A 1 73  ? 15.25200  21.31300  18.92600  1.000 8.72717   ? 73  GLU AA O   1 
ATOM   545  C  CB  . GLU A 1 73  ? 18.48200  21.48800  19.09400  1.000 4.86462   ? 73  GLU AA CB  1 
ATOM   546  C  CG  . GLU A 1 73  ? 18.01200  21.85600  20.49000  1.000 12.51584  ? 73  GLU AA CG  1 
ATOM   547  C  CD  . GLU A 1 73  ? 19.10000  22.51700  21.31800  1.000 13.02131  ? 73  GLU AA CD  1 
ATOM   548  O  OE1 . GLU A 1 73  ? 20.25800  22.05100  21.26800  1.000 17.14244  ? 73  GLU AA OE1 1 
ATOM   549  O  OE2 . GLU A 1 73  ? 18.79700  23.50200  22.02200  1.000 11.74330  ? 73  GLU AA OE2 1 
ATOM   550  N  N   . ALA A 1 74  ? 16.07700  22.30000  17.07500  1.000 7.01658   ? 74  ALA AA N   1 
ATOM   551  C  CA  . ALA A 1 74  ? 14.85500  23.06500  16.85000  1.000 8.78714   ? 74  ALA AA CA  1 
ATOM   552  C  C   . ALA A 1 74  ? 13.66600  22.15800  16.56800  1.000 13.46899  ? 74  ALA AA C   1 
ATOM   553  O  O   . ALA A 1 74  ? 12.52400  22.52100  16.87200  1.000 14.88775  ? 74  ALA AA O   1 
ATOM   554  C  CB  . ALA A 1 74  ? 15.05500  24.04800  15.69700  1.000 6.25518   ? 74  ALA AA CB  1 
ATOM   555  N  N   . ALA A 1 75  ? 13.90900  20.98200  15.98300  1.000 10.45386  ? 75  ALA AA N   1 
ATOM   556  C  CA  . ALA A 1 75  ? 12.82400  20.03200  15.76400  1.000 7.78905   ? 75  ALA AA CA  1 
ATOM   557  C  C   . ALA A 1 75  ? 12.24700  19.55000  17.08800  1.000 15.72143  ? 75  ALA AA C   1 
ATOM   558  O  O   . ALA A 1 75  ? 11.02900  19.38500  17.22200  1.000 6.51360   ? 75  ALA AA O   1 
ATOM   559  C  CB  . ALA A 1 75  ? 13.31900  18.85000  14.93100  1.000 3.76442   ? 75  ALA AA CB  1 
ATOM   560  N  N   . LEU A 1 76  ? 13.10900  19.32400  18.08300  1.000 4.44183   ? 76  LEU AA N   1 
ATOM   561  C  CA  . LEU A 1 76  ? 12.62400  18.91200  19.39400  1.000 14.64020  ? 76  LEU AA CA  1 
ATOM   562  C  C   . LEU A 1 76  ? 11.94500  20.06100  20.12700  1.000 13.47236  ? 76  LEU AA C   1 
ATOM   563  O  O   . LEU A 1 76  ? 11.02900  19.82800  20.92400  1.000 12.01746  ? 76  LEU AA O   1 
ATOM   564  C  CB  . LEU A 1 76  ? 13.77400  18.34400  20.22200  1.000 14.48184  ? 76  LEU AA CB  1 
ATOM   565  C  CG  . LEU A 1 76  ? 14.12600  16.90900  19.82800  1.000 16.14358  ? 76  LEU AA CG  1 
ATOM   566  C  CD1 . LEU A 1 76  ? 15.63000  16.72500  19.71600  1.000 18.93886  ? 76  LEU AA CD1 1 
ATOM   567  C  CD2 . LEU A 1 76  ? 13.52700  15.92200  20.81900  1.000 14.83814  ? 76  LEU AA CD2 1 
ATOM   568  N  N   . GLY A 1 77  ? 12.37600  21.29900  19.87700  1.000 8.04443   ? 77  GLY AA N   1 
ATOM   569  C  CA  . GLY A 1 77  ? 11.63000  22.43700  20.38600  1.000 8.47101   ? 77  GLY AA CA  1 
ATOM   570  C  C   . GLY A 1 77  ? 10.21000  22.47000  19.85500  1.000 12.66942  ? 77  GLY AA C   1 
ATOM   571  O  O   . GLY A 1 77  ? 9.27500   22.83400  20.57200  1.000 9.81470   ? 77  GLY AA O   1 
ATOM   572  N  N   . ALA A 1 78  ? 10.02900  22.07200  18.59300  1.000 8.64009   ? 78  ALA AA N   1 
ATOM   573  C  CA  . ALA A 1 78  ? 8.69200   22.00600  18.01400  1.000 9.25992   ? 78  ALA AA CA  1 
ATOM   574  C  C   . ALA A 1 78  ? 7.87800   20.87900  18.63500  1.000 17.23208  ? 78  ALA AA C   1 
ATOM   575  O  O   . ALA A 1 78  ? 6.67200   21.03000  18.86500  1.000 11.88706  ? 78  ALA AA O   1 
ATOM   576  C  CB  . ALA A 1 78  ? 8.78800   21.82600  16.50000  1.000 4.77948   ? 78  ALA AA CB  1 
ATOM   577  N  N   . VAL A 1 79  ? 8.52100   19.73900  18.90400  1.000 9.23458   ? 79  VAL AA N   1 
ATOM   578  C  CA  . VAL A 1 79  ? 7.83400   18.62400  19.55100  1.000 16.03867  ? 79  VAL AA CA  1 
ATOM   579  C  C   . VAL A 1 79  ? 7.31000   19.04400  20.91700  1.000 12.37966  ? 79  VAL AA C   1 
ATOM   580  O  O   . VAL A 1 79  ? 6.16900   18.73500  21.28300  1.000 16.84951  ? 79  VAL AA O   1 
ATOM   581  C  CB  . VAL A 1 79  ? 8.77400   17.40700  19.65600  1.000 10.45308  ? 79  VAL AA CB  1 
ATOM   582  C  CG1 . VAL A 1 79  ? 8.17900   16.35000  20.57100  1.000 11.06840  ? 79  VAL AA CG1 1 
ATOM   583  C  CG2 . VAL A 1 79  ? 9.05200   16.82800  18.27800  1.000 7.55695   ? 79  VAL AA CG2 1 
ATOM   584  N  N   . ARG A 1 80  ? 8.13200   19.75900  21.69100  1.000 11.03644  ? 80  ARG AA N   1 
ATOM   585  C  CA  . ARG A 1 80  ? 7.70100   20.22200  23.00700  1.000 21.10598  ? 80  ARG AA CA  1 
ATOM   586  C  C   . ARG A 1 80  ? 6.50400   21.15800  22.89700  1.000 28.72121  ? 80  ARG AA C   1 
ATOM   587  O  O   . ARG A 1 80  ? 5.55700   21.06300  23.68700  1.000 18.56679  ? 80  ARG AA O   1 
ATOM   588  C  CB  . ARG A 1 80  ? 8.85600   20.91900  23.72300  1.000 11.12178  ? 80  ARG AA CB  1 
ATOM   589  C  CG  . ARG A 1 80  ? 9.87700   19.97600  24.33600  1.000 15.68141  ? 80  ARG AA CG  1 
ATOM   590  C  CD  . ARG A 1 80  ? 11.11400  20.73600  24.78900  1.000 15.56352  ? 80  ARG AA CD  1 
ATOM   591  N  NE  . ARG A 1 80  ? 12.01100  19.90400  25.58100  1.000 14.65836  ? 80  ARG AA NE  1 
ATOM   592  C  CZ  . ARG A 1 80  ? 11.90900  19.73100  26.89200  1.000 31.05451  ? 80  ARG AA CZ  1 
ATOM   593  N  NH1 . ARG A 1 80  ? 10.95300  20.31700  27.59300  1.000 15.06572  ? 80  ARG AA NH1 1 
ATOM   594  N  NH2 . ARG A 1 80  ? 12.78900  18.95100  27.51400  1.000 8.67813   ? 80  ARG AA NH2 1 
ATOM   595  N  N   . TYR A 1 81  ? 6.53000   22.06900  21.92100  1.000 10.12945  ? 81  TYR AA N   1 
ATOM   596  C  CA  . TYR A 1 81  ? 5.41200   22.98700  21.72700  1.000 15.11599  ? 81  TYR AA CA  1 
ATOM   597  C  C   . TYR A 1 81  ? 4.13100   22.23000  21.40100  1.000 19.64810  ? 81  TYR AA C   1 
ATOM   598  O  O   . TYR A 1 81  ? 3.06500   22.52000  21.95600  1.000 15.31539  ? 81  TYR AA O   1 
ATOM   599  C  CB  . TYR A 1 81  ? 5.74700   23.98700  20.61900  1.000 8.46689   ? 81  TYR AA CB  1 
ATOM   600  C  CG  . TYR A 1 81  ? 4.58800   24.86800  20.20400  1.000 14.92479  ? 81  TYR AA CG  1 
ATOM   601  C  CD1 . TYR A 1 81  ? 4.33900   26.07100  20.85300  1.000 20.08006  ? 81  TYR AA CD1 1 
ATOM   602  C  CD2 . TYR A 1 81  ? 3.74800   24.50100  19.16000  1.000 13.71137  ? 81  TYR AA CD2 1 
ATOM   603  C  CE1 . TYR A 1 81  ? 3.28400   26.88200  20.47700  1.000 19.04233  ? 81  TYR AA CE1 1 
ATOM   604  C  CE2 . TYR A 1 81  ? 2.68900   25.30600  18.77600  1.000 19.51448  ? 81  TYR AA CE2 1 
ATOM   605  C  CZ  . TYR A 1 81  ? 2.46300   26.49500  19.43800  1.000 18.16055  ? 81  TYR AA CZ  1 
ATOM   606  O  OH  . TYR A 1 81  ? 1.41100   27.29800  19.06000  1.000 18.38384  ? 81  TYR AA OH  1 
ATOM   607  N  N   . PHE A 1 82  ? 4.22000   21.24900  20.49900  1.000 14.98469  ? 82  PHE AA N   1 
ATOM   608  C  CA  . PHE A 1 82  ? 3.02300   20.53900  20.05900  1.000 13.06727  ? 82  PHE AA CA  1 
ATOM   609  C  C   . PHE A 1 82  ? 2.41700   19.70800  21.18300  1.000 11.40255  ? 82  PHE AA C   1 
ATOM   610  O  O   . PHE A 1 82  ? 1.19100   19.57700  21.26800  1.000 19.77841  ? 82  PHE AA O   1 
ATOM   611  C  CB  . PHE A 1 82  ? 3.34900   19.66300  18.84900  1.000 8.36539   ? 82  PHE AA CB  1 
ATOM   612  C  CG  . PHE A 1 82  ? 3.45500   20.42900  17.55900  1.000 22.72944  ? 82  PHE AA CG  1 
ATOM   613  C  CD1 . PHE A 1 82  ? 2.48000   21.34500  17.20300  1.000 16.53684  ? 82  PHE AA CD1 1 
ATOM   614  C  CD2 . PHE A 1 82  ? 4.53100   20.23800  16.70800  1.000 10.21850  ? 82  PHE AA CD2 1 
ATOM   615  C  CE1 . PHE A 1 82  ? 2.57300   22.05500  16.01900  1.000 26.59861  ? 82  PHE AA CE1 1 
ATOM   616  C  CE2 . PHE A 1 82  ? 4.63100   20.94400  15.52300  1.000 19.75356  ? 82  PHE AA CE2 1 
ATOM   617  C  CZ  . PHE A 1 82  ? 3.65000   21.85500  15.17800  1.000 14.50058  ? 82  PHE AA CZ  1 
ATOM   618  N  N   . GLU A 1 83  ? 3.25200   19.13800  22.05600  1.000 11.84829  ? 83  GLU AA N   1 
ATOM   619  C  CA  . GLU A 1 83  ? 2.71400   18.38500  23.18500  1.000 18.79361  ? 83  GLU AA CA  1 
ATOM   620  C  C   . GLU A 1 83  ? 1.97000   19.30100  24.14900  1.000 18.32745  ? 83  GLU AA C   1 
ATOM   621  O  O   . GLU A 1 83  ? 0.96200   18.89900  24.74200  1.000 19.08299  ? 83  GLU AA O   1 
ATOM   622  C  CB  . GLU A 1 83  ? 3.83000   17.63700  23.91400  1.000 18.39279  ? 83  GLU AA CB  1 
ATOM   623  C  CG  . GLU A 1 83  ? 3.31900   16.73300  25.03100  1.000 18.84167  ? 83  GLU AA CG  1 
ATOM   624  C  CD  . GLU A 1 83  ? 4.39900   16.34100  26.02200  1.000 19.30172  ? 83  GLU AA CD  1 
ATOM   625  O  OE1 . GLU A 1 83  ? 5.51700   16.89200  25.94300  1.000 20.94648  ? 83  GLU AA OE1 1 
ATOM   626  O  OE2 . GLU A 1 83  ? 4.12400   15.48100  26.88600  1.000 19.00389  ? 83  GLU AA OE2 1 
ATOM   627  N  N   . GLU A 1 84  ? 2.45100   20.53500  24.31600  1.000 16.27759  ? 84  GLU AA N   1 
ATOM   628  C  CA  . GLU A 1 84  ? 1.74300   21.49800  25.15300  1.000 28.94152  ? 84  GLU AA CA  1 
ATOM   629  C  C   . GLU A 1 84  ? 0.37100   21.82200  24.57500  1.000 22.37174  ? 84  GLU AA C   1 
ATOM   630  O  O   . GLU A 1 84  ? -0.59700  22.01200  25.32000  1.000 24.96345  ? 84  GLU AA O   1 
ATOM   631  C  CB  . GLU A 1 84  ? 2.57200   22.77200  25.30200  1.000 21.68825  ? 84  GLU AA CB  1 
ATOM   632  C  CG  . GLU A 1 84  ? 3.80300   22.61900  26.17700  1.000 35.59048  ? 84  GLU AA CG  1 
ATOM   633  C  CD  . GLU A 1 84  ? 4.51500   23.93800  26.40500  1.000 53.53539  ? 84  GLU AA CD  1 
ATOM   634  O  OE1 . GLU A 1 84  ? 3.83700   24.98700  26.39800  1.000 51.29246  ? 84  GLU AA OE1 1 
ATOM   635  O  OE2 . GLU A 1 84  ? 5.75100   23.92500  26.58800  1.000 43.45379  ? 84  GLU AA OE2 1 
ATOM   636  N  N   . GLN A 1 85  ? 0.26900   21.88500  23.24700  1.000 19.13385  ? 85  GLN AA N   1 
ATOM   637  C  CA  . GLN A 1 85  ? -0.99700  22.16700  22.58300  1.000 23.21633  ? 85  GLN AA CA  1 
ATOM   638  C  C   . GLN A 1 85  ? -1.92700  20.96300  22.54300  1.000 20.98173  ? 85  GLN AA C   1 
ATOM   639  O  O   . GLN A 1 85  ? -3.08200  21.10800  22.12800  1.000 37.95235  ? 85  GLN AA O   1 
ATOM   640  C  CB  . GLN A 1 85  ? -0.74900  22.66300  21.15400  1.000 26.19588  ? 85  GLN AA CB  1 
ATOM   641  C  CG  . GLN A 1 85  ? -0.02900  24.00800  21.03700  1.000 31.86164  ? 85  GLN AA CG  1 
ATOM   642  C  CD  . GLN A 1 85  ? -0.00800  24.80100  22.33300  1.000 50.75085  ? 85  GLN AA CD  1 
ATOM   643  O  OE1 . GLN A 1 85  ? -0.98300  25.46700  22.68000  1.000 60.84167  ? 85  GLN AA OE1 1 
ATOM   644  N  NE2 . GLN A 1 85  ? 1.11400   24.74900  23.04300  1.000 53.51959  ? 85  GLN AA NE2 1 
ATOM   645  N  N   . GLY A 1 86  ? -1.45900  19.78700  22.95300  1.000 19.30045  ? 86  GLY AA N   1 
ATOM   646  C  CA  . GLY A 1 86  ? -2.28900  18.60000  22.95600  1.000 17.20733  ? 86  GLY AA CA  1 
ATOM   647  C  C   . GLY A 1 86  ? -2.26600  17.78800  21.68300  1.000 30.23154  ? 86  GLY AA C   1 
ATOM   648  O  O   . GLY A 1 86  ? -3.14700  16.94200  21.49200  1.000 24.07303  ? 86  GLY AA O   1 
ATOM   649  N  N   . ARG A 1 87  ? -1.29300  18.01200  20.80600  1.000 24.36520  ? 87  ARG AA N   1 
ATOM   650  C  CA  . ARG A 1 87  ? -1.19800  17.28000  19.55300  1.000 21.03009  ? 87  ARG AA CA  1 
ATOM   651  C  C   . ARG A 1 87  ? -0.27300  16.07500  19.69800  1.000 16.41434  ? 87  ARG AA C   1 
ATOM   652  O  O   . ARG A 1 87  ? 0.57300   16.01000  20.59300  1.000 24.44309  ? 87  ARG AA O   1 
ATOM   653  C  CB  . ARG A 1 87  ? -0.69400  18.19100  18.43400  1.000 17.49540  ? 87  ARG AA CB  1 
ATOM   654  C  CG  . ARG A 1 87  ? -1.55200  19.42400  18.19800  1.000 22.25003  ? 87  ARG AA CG  1 
ATOM   655  C  CD  . ARG A 1 87  ? -1.69200  19.71300  16.71500  1.000 25.12467  ? 87  ARG AA CD  1 
ATOM   656  N  NE  . ARG A 1 87  ? -2.47100  20.91900  16.46200  1.000 39.86215  ? 87  ARG AA NE  1 
ATOM   657  C  CZ  . ARG A 1 87  ? -2.52600  21.54300  15.29400  1.000 31.31358  ? 87  ARG AA CZ  1 
ATOM   658  N  NH1 . ARG A 1 87  ? -1.85300  21.10300  14.24300  1.000 16.49335  ? 87  ARG AA NH1 1 
ATOM   659  N  NH2 . ARG A 1 87  ? -3.27400  22.63600  15.17600  1.000 31.07269  ? 87  ARG AA NH2 1 
ATOM   660  N  N   . GLY A 1 88  ? -0.44300  15.11700  18.79800  1.000 21.31336  ? 88  GLY AA N   1 
ATOM   661  C  CA  . GLY A 1 88  ? 0.38100   13.92700  18.76100  1.000 20.97217  ? 88  GLY AA CA  1 
ATOM   662  C  C   . GLY A 1 88  ? -0.42800  12.66200  18.99000  1.000 19.15078  ? 88  GLY AA C   1 
ATOM   663  O  O   . GLY A 1 88  ? -1.60500  12.68900  19.34700  1.000 25.99766  ? 88  GLY AA O   1 
ATOM   664  N  N   A TYR A 1 89  ? 0.24700   11.53700  18.76800  0.453 23.50949  ? 89  TYR AA N   1 
ATOM   665  N  N   B TYR A 1 89  ? 0.24900   11.53700  18.77500  0.547 23.53487  ? 89  TYR AA N   1 
ATOM   666  C  CA  A TYR A 1 89  ? -0.38500  10.23800  18.95500  0.453 22.34194  ? 89  TYR AA CA  1 
ATOM   667  C  CA  B TYR A 1 89  ? -0.37400  10.23200  18.95500  0.547 22.33547  ? 89  TYR AA CA  1 
ATOM   668  C  C   A TYR A 1 89  ? -0.65400  9.99400   20.43400  0.453 21.67235  ? 89  TYR AA C   1 
ATOM   669  C  C   B TYR A 1 89  ? -0.64600  9.97700   20.43300  0.547 21.64981  ? 89  TYR AA C   1 
ATOM   670  O  O   A TYR A 1 89  ? 0.22600   10.18800  21.27800  0.453 23.15111  ? 89  TYR AA O   1 
ATOM   671  O  O   B TYR A 1 89  ? 0.23900   10.14800  21.27700  0.547 23.11902  ? 89  TYR AA O   1 
ATOM   672  C  CB  A TYR A 1 89  ? 0.49500   9.12900   18.38300  0.453 20.69057  ? 89  TYR AA CB  1 
ATOM   673  C  CB  B TYR A 1 89  ? 0.52600   9.14000   18.37700  0.547 20.63205  ? 89  TYR AA CB  1 
ATOM   674  C  CG  A TYR A 1 89  ? -0.29400  7.96300   17.83400  0.453 32.58079  ? 89  TYR AA CG  1 
ATOM   675  C  CG  B TYR A 1 89  ? 0.06500   7.72900   18.66600  0.547 28.31432  ? 89  TYR AA CG  1 
ATOM   676  C  CD1 A TYR A 1 89  ? -0.78100  7.98100   16.53400  0.453 26.15865  ? 89  TYR AA CD1 1 
ATOM   677  C  CD1 B TYR A 1 89  ? -1.05900  7.20100   18.04200  0.547 36.79830  ? 89  TYR AA CD1 1 
ATOM   678  C  CD2 A TYR A 1 89  ? -0.56300  6.85000   18.62000  0.453 33.82206  ? 89  TYR AA CD2 1 
ATOM   679  C  CD2 B TYR A 1 89  ? 0.75900   6.92200   19.55600  0.547 24.49468  ? 89  TYR AA CD2 1 
ATOM   680  C  CE1 A TYR A 1 89  ? -1.50700  6.92100   16.02900  0.453 32.11179  ? 89  TYR AA CE1 1 
ATOM   681  C  CE1 B TYR A 1 89  ? -1.48000  5.90900   18.30300  0.547 32.08416  ? 89  TYR AA CE1 1 
ATOM   682  C  CE2 A TYR A 1 89  ? -1.28900  5.78500   18.12300  0.453 31.63206  ? 89  TYR AA CE2 1 
ATOM   683  C  CE2 B TYR A 1 89  ? 0.34600   5.63100   19.82100  0.547 29.24384  ? 89  TYR AA CE2 1 
ATOM   684  C  CZ  A TYR A 1 89  ? -1.75800  5.82600   16.82800  0.453 30.71212  ? 89  TYR AA CZ  1 
ATOM   685  C  CZ  B TYR A 1 89  ? -0.77200  5.13000   19.19400  0.547 37.92345  ? 89  TYR AA CZ  1 
ATOM   686  O  OH  A TYR A 1 89  ? -2.48200  4.76900   16.32800  0.453 53.64654  ? 89  TYR AA OH  1 
ATOM   687  O  OH  B TYR A 1 89  ? -1.18000  3.84400   19.46300  0.547 42.47174  ? 89  TYR AA OH  1 
ATOM   688  N  N   . ASP A 1 90  ? -1.87400  9.56500   20.74400  1.000 19.98987  ? 90  ASP AA N   1 
ATOM   689  C  CA  . ASP A 1 90  ? -2.31400  9.38300   22.12400  1.000 27.46433  ? 90  ASP AA CA  1 
ATOM   690  C  C   . ASP A 1 90  ? -1.98900  7.97400   22.60700  1.000 21.27806  ? 90  ASP AA C   1 
ATOM   691  O  O   . ASP A 1 90  ? -2.53800  6.99300   22.09300  1.000 38.20623  ? 90  ASP AA O   1 
ATOM   692  C  CB  . ASP A 1 90  ? -3.81500  9.64900   22.23900  1.000 32.66111  ? 90  ASP AA CB  1 
ATOM   693  C  CG  . ASP A 1 90  ? -4.25000  9.95500   23.66200  1.000 29.33801  ? 90  ASP AA CG  1 
ATOM   694  O  OD1 . ASP A 1 90  ? -3.55100  9.53600   24.60900  1.000 29.07453  ? 90  ASP AA OD1 1 
ATOM   695  O  OD2 . ASP A 1 90  ? -5.29600  10.61400  23.83200  1.000 43.17836  ? 90  ASP AA OD2 1 
ATOM   696  N  N   . VAL A 1 91  ? -1.11000  7.87700   23.60700  1.000 25.28505  ? 91  VAL AA N   1 
ATOM   697  C  CA  . VAL A 1 91  ? -0.82500  6.61100   24.27300  1.000 23.14169  ? 91  VAL AA CA  1 
ATOM   698  C  C   . VAL A 1 91  ? -1.52400  6.51400   25.62500  1.000 32.61444  ? 91  VAL AA C   1 
ATOM   699  O  O   . VAL A 1 91  ? -1.28100  5.56600   26.37800  1.000 37.09399  ? 91  VAL AA O   1 
ATOM   700  C  CB  . VAL A 1 91  ? 0.68900   6.38500   24.43200  1.000 21.82241  ? 91  VAL AA CB  1 
ATOM   701  C  CG1 . VAL A 1 91  ? 1.29700   5.90000   23.13000  1.000 32.98914  ? 91  VAL AA CG1 1 
ATOM   702  C  CG2 . VAL A 1 91  ? 1.37700   7.65100   24.91000  1.000 20.36753  ? 91  VAL AA CG2 1 
ATOM   703  N  N   . GLY A 1 92  ? -2.38300  7.47600   25.95400  1.000 28.23032  ? 92  GLY AA N   1 
ATOM   704  C  CA  . GLY A 1 92  ? -3.08800  7.45800   27.22000  1.000 29.89339  ? 92  GLY AA CA  1 
ATOM   705  C  C   . GLY A 1 92  ? -2.39300  8.26000   28.30000  1.000 27.70312  ? 92  GLY AA C   1 
ATOM   706  O  O   . GLY A 1 92  ? -2.97900  9.18200   28.87400  1.000 32.51123  ? 92  GLY AA O   1 
ATOM   707  N  N   . VAL A 1 93  ? -1.13500  7.91500   28.58800  1.000 24.21873  ? 93  VAL AA N   1 
ATOM   708  C  CA  . VAL A 1 93  ? -0.37300  8.63700   29.60500  1.000 19.84718  ? 93  VAL AA CA  1 
ATOM   709  C  C   . VAL A 1 93  ? 0.29300   9.89000   29.06400  1.000 24.78566  ? 93  VAL AA C   1 
ATOM   710  O  O   . VAL A 1 93  ? 0.80900   10.69200  29.85300  1.000 22.04274  ? 93  VAL AA O   1 
ATOM   711  C  CB  . VAL A 1 93  ? 0.70100   7.73000   30.23600  1.000 22.86121  ? 93  VAL AA CB  1 
ATOM   712  C  CG1 . VAL A 1 93  ? 0.04900   6.65000   31.08500  1.000 18.99040  ? 93  VAL AA CG1 1 
ATOM   713  C  CG2 . VAL A 1 93  ? 1.57600   7.11100   29.15800  1.000 13.22404  ? 93  VAL AA CG2 1 
ATOM   714  N  N   . ALA A 1 94  ? 0.29300   10.08500  27.74700  1.000 19.76322  ? 94  ALA AA N   1 
ATOM   715  C  CA  . ALA A 1 94  ? 0.91700   11.24700  27.12500  1.000 18.92928  ? 94  ALA AA CA  1 
ATOM   716  C  C   . ALA A 1 94  ? 0.48700   11.29800  25.66600  1.000 21.99237  ? 94  ALA AA C   1 
ATOM   717  O  O   . ALA A 1 94  ? -0.16900  10.38500  25.15700  1.000 19.38634  ? 94  ALA AA O   1 
ATOM   718  C  CB  . ALA A 1 94  ? 2.44300   11.20000  27.23600  1.000 17.05720  ? 94  ALA AA CB  1 
ATOM   719  N  N   . LYS A 1 95  ? 0.85900   12.39000  25.00100  1.000 18.49243  ? 95  LYS AA N   1 
ATOM   720  C  CA  . LYS A 1 95  ? 0.70200   12.54000  23.56100  1.000 27.01503  ? 95  LYS AA CA  1 
ATOM   721  C  C   . LYS A 1 95  ? 2.08000   12.71900  22.94400  1.000 23.50050  ? 95  LYS AA C   1 
ATOM   722  O  O   . LYS A 1 95  ? 2.89400   13.49600  23.45300  1.000 22.98344  ? 95  LYS AA O   1 
ATOM   723  C  CB  . LYS A 1 95  ? -0.20100  13.72800  23.21500  1.000 21.76598  ? 95  LYS AA CB  1 
ATOM   724  C  CG  . LYS A 1 95  ? -1.36000  13.92300  24.17400  1.000 39.23898  ? 95  LYS AA CG  1 
ATOM   725  C  CD  . LYS A 1 95  ? -2.67800  14.06000  23.42900  1.000 31.64774  ? 95  LYS AA CD  1 
ATOM   726  C  CE  . LYS A 1 95  ? -3.79200  14.49800  24.36800  1.000 55.29470  ? 95  LYS AA CE  1 
ATOM   727  N  NZ  . LYS A 1 95  ? -3.80100  15.97400  24.57600  1.000 71.64923  ? 95  LYS AA NZ  1 
ATOM   728  N  N   . ILE A 1 96  ? 2.34300   11.99700  21.85900  1.000 19.35259  ? 96  ILE AA N   1 
ATOM   729  C  CA  . ILE A 1 96  ? 3.66800   11.99700  21.24500  1.000 16.08658  ? 96  ILE AA CA  1 
ATOM   730  C  C   . ILE A 1 96  ? 3.60400   12.63400  19.86200  1.000 19.01653  ? 96  ILE AA C   1 
ATOM   731  O  O   . ILE A 1 96  ? 3.19200   11.97600  18.89600  1.000 18.56746  ? 96  ILE AA O   1 
ATOM   732  C  CB  . ILE A 1 96  ? 4.24200   10.57400  21.16600  1.000 17.21433  ? 96  ILE AA CB  1 
ATOM   733  C  CG1 . ILE A 1 96  ? 3.95600   9.81100   22.46200  1.000 15.59948  ? 96  ILE AA CG1 1 
ATOM   734  C  CG2 . ILE A 1 96  ? 5.73500   10.62000  20.88400  1.000 14.66005  ? 96  ILE AA CG2 1 
ATOM   735  C  CD1 . ILE A 1 96  ? 4.54400   8.41600   22.49200  1.000 17.13898  ? 96  ILE AA CD1 1 
ATOM   736  N  N   . PRO A 1 97  ? 3.99600   13.89600  19.71700  1.000 18.44373  ? 97  PRO AA N   1 
ATOM   737  C  CA  . PRO A 1 97  ? 4.08600   14.49700  18.38400  1.000 14.42761  ? 97  PRO AA CA  1 
ATOM   738  C  C   . PRO A 1 97  ? 5.34900   14.04600  17.66400  1.000 17.23066  ? 97  PRO AA C   1 
ATOM   739  O  O   . PRO A 1 97  ? 6.28500   13.51100  18.25900  1.000 9.75938   ? 97  PRO AA O   1 
ATOM   740  C  CB  . PRO A 1 97  ? 4.12200   16.00700  18.66400  1.000 15.47305  ? 97  PRO AA CB  1 
ATOM   741  C  CG  . PRO A 1 97  ? 3.98900   16.16300  20.16800  1.000 17.60238  ? 97  PRO AA CG  1 
ATOM   742  C  CD  . PRO A 1 97  ? 4.35300   14.85000  20.77700  1.000 19.09376  ? 97  PRO AA CD  1 
ATOM   743  N  N   . LEU A 1 98  ? 5.35900   14.27500  16.35200  1.000 10.44144  ? 98  LEU AA N   1 
ATOM   744  C  CA  . LEU A 1 98  ? 6.47900   13.87500  15.50800  1.000 11.36722  ? 98  LEU AA CA  1 
ATOM   745  C  C   . LEU A 1 98  ? 6.79200   15.00300  14.53900  1.000 11.75806  ? 98  LEU AA C   1 
ATOM   746  O  O   . LEU A 1 98  ? 5.92000   15.41800  13.76900  1.000 11.21755  ? 98  LEU AA O   1 
ATOM   747  C  CB  . LEU A 1 98  ? 6.16200   12.58500  14.74500  1.000 15.12500  ? 98  LEU AA CB  1 
ATOM   748  C  CG  . LEU A 1 98  ? 7.36500   11.76900  14.27000  1.000 18.32234  ? 98  LEU AA CG  1 
ATOM   749  C  CD1 . LEU A 1 98  ? 8.03100   11.06500  15.44200  1.000 16.61976  ? 98  LEU AA CD1 1 
ATOM   750  C  CD2 . LEU A 1 98  ? 6.95300   10.77000  13.20000  1.000 18.12392  ? 98  LEU AA CD2 1 
ATOM   751  N  N   . VAL A 1 99  ? 8.02700   15.49600  14.57700  1.000 6.14876   ? 99  VAL AA N   1 
ATOM   752  C  CA  . VAL A 1 99  ? 8.46700   16.54900  13.66300  1.000 7.19177   ? 99  VAL AA CA  1 
ATOM   753  C  C   . VAL A 1 99  ? 9.73500   16.10000  12.94300  1.000 12.72365  ? 99  VAL AA C   1 
ATOM   754  O  O   . VAL A 1 99  ? 10.84700  16.36200  13.42600  1.000 9.91030   ? 99  VAL AA O   1 
ATOM   755  C  CB  . VAL A 1 99  ? 8.69400   17.87900  14.40100  1.000 13.30761  ? 99  VAL AA CB  1 
ATOM   756  C  CG1 . VAL A 1 99  ? 9.05900   18.98200  13.41300  1.000 1.24984   ? 99  VAL AA CG1 1 
ATOM   757  C  CG2 . VAL A 1 99  ? 7.45400   18.27100  15.19500  1.000 8.49958   ? 99  VAL AA CG2 1 
ATOM   758  N  N   . PRO A 1 100 ? 9.62300   15.41700  11.80500  1.000 11.13553  ? 100 PRO AA N   1 
ATOM   759  C  CA  . PRO A 1 100 ? 10.82100  15.10400  11.01600  1.000 7.17900   ? 100 PRO AA CA  1 
ATOM   760  C  C   . PRO A 1 100 ? 11.45200  16.37200  10.46300  1.000 7.76926   ? 100 PRO AA C   1 
ATOM   761  O  O   . PRO A 1 100 ? 10.77100  17.36400  10.19000  1.000 7.72231   ? 100 PRO AA O   1 
ATOM   762  C  CB  . PRO A 1 100 ? 10.28700  14.21000  9.88900   1.000 10.05710  ? 100 PRO AA CB  1 
ATOM   763  C  CG  . PRO A 1 100 ? 8.93900   13.73800  10.36000  1.000 9.02868   ? 100 PRO AA CG  1 
ATOM   764  C  CD  . PRO A 1 100 ? 8.40400   14.82900  11.22800  1.000 3.91202   ? 100 PRO AA CD  1 
ATOM   765  N  N   . ALA A 1 101 ? 12.77300  16.33300  10.29600  1.000 7.61910   ? 101 ALA AA N   1 
ATOM   766  C  CA  . ALA A 1 101 ? 13.50100  17.52600  9.89100   1.000 10.38843  ? 101 ALA AA CA  1 
ATOM   767  C  C   . ALA A 1 101 ? 14.78000  17.14500  9.16100   1.000 13.42712  ? 101 ALA AA C   1 
ATOM   768  O  O   . ALA A 1 101 ? 15.31700  16.04700  9.33000   1.000 10.20709  ? 101 ALA AA O   1 
ATOM   769  C  CB  . ALA A 1 101 ? 13.82900  18.41500  11.09700  1.000 8.46787   ? 101 ALA AA CB  1 
ATOM   770  N  N   . ALA A 1 102 ? 15.25800  18.08000  8.34000   1.000 5.18478   ? 102 ALA AA N   1 
ATOM   771  C  CA  . ALA A 1 102 ? 16.55600  17.99300  7.68700   1.000 8.32828   ? 102 ALA AA CA  1 
ATOM   772  C  C   . ALA A 1 102 ? 17.23200  19.35300  7.79100   1.000 13.51093  ? 102 ALA AA C   1 
ATOM   773  O  O   . ALA A 1 102 ? 16.57100  20.38000  7.96700   1.000 7.18552   ? 102 ALA AA O   1 
ATOM   774  C  CB  . ALA A 1 102 ? 16.43300  17.56000  6.22000   1.000 4.88163   ? 102 ALA AA CB  1 
ATOM   775  N  N   . VAL A 1 103 ? 18.56300  19.36000  7.68000   1.000 6.21541   ? 103 VAL AA N   1 
ATOM   776  C  CA  . VAL A 1 103 ? 19.34400  20.56100  7.94600   1.000 10.01320  ? 103 VAL AA CA  1 
ATOM   777  C  C   . VAL A 1 103 ? 20.13500  20.97600  6.71100   1.000 14.11869  ? 103 VAL AA C   1 
ATOM   778  O  O   . VAL A 1 103 ? 20.36500  20.19300  5.78400   1.000 6.02956   ? 103 VAL AA O   1 
ATOM   779  C  CB  . VAL A 1 103 ? 20.30100  20.38000  9.14400   1.000 9.65562   ? 103 VAL AA CB  1 
ATOM   780  C  CG1 . VAL A 1 103 ? 19.60100  19.67100  10.28400  1.000 7.75512   ? 103 VAL AA CG1 1 
ATOM   781  C  CG2 . VAL A 1 103 ? 21.55100  19.62100  8.71800   1.000 4.42278   ? 103 VAL AA CG2 1 
ATOM   782  N  N   . ILE A 1 104 ? 20.54600  22.24400  6.71300   1.000 5.60110   ? 104 ILE AA N   1 
ATOM   783  C  CA  . ILE A 1 104 ? 21.55500  22.76600  5.80400   1.000 7.71905   ? 104 ILE AA CA  1 
ATOM   784  C  C   . ILE A 1 104 ? 22.70500  23.30400  6.64700   1.000 12.95756  ? 104 ILE AA C   1 
ATOM   785  O  O   . ILE A 1 104 ? 22.54700  23.61900  7.82900   1.000 13.63167  ? 104 ILE AA O   1 
ATOM   786  C  CB  . ILE A 1 104 ? 21.01000  23.86800  4.87000   1.000 10.82802  ? 104 ILE AA CB  1 
ATOM   787  C  CG1 . ILE A 1 104 ? 20.56700  25.08900  5.68100   1.000 13.50077  ? 104 ILE AA CG1 1 
ATOM   788  C  CG2 . ILE A 1 104 ? 19.86700  23.33800  4.01700   1.000 6.84662   ? 104 ILE AA CG2 1 
ATOM   789  C  CD1 . ILE A 1 104 ? 20.66800  26.39700  4.92200   1.000 13.76369  ? 104 ILE AA CD1 1 
ATOM   790  N  N   . TYR A 1 105 ? 23.87500  23.40500  6.02200   1.000 11.43624  ? 105 TYR AA N   1 
ATOM   791  C  CA  . TYR A 1 105 ? 25.04800  23.98500  6.66600   1.000 18.09139  ? 105 TYR AA CA  1 
ATOM   792  C  C   . TYR A 1 105 ? 25.08800  25.48100  6.37100   1.000 18.68313  ? 105 TYR AA C   1 
ATOM   793  O  O   . TYR A 1 105 ? 25.24300  25.88600  5.21400   1.000 14.51517  ? 105 TYR AA O   1 
ATOM   794  C  CB  . TYR A 1 105 ? 26.32900  23.30600  6.18000   1.000 9.83294   ? 105 TYR AA CB  1 
ATOM   795  C  CG  . TYR A 1 105 ? 27.59700  23.94000  6.71100   1.000 13.01363  ? 105 TYR AA CG  1 
ATOM   796  C  CD1 . TYR A 1 105 ? 28.13900  23.54300  7.92700   1.000 20.95712  ? 105 TYR AA CD1 1 
ATOM   797  C  CD2 . TYR A 1 105 ? 28.25000  24.94200  6.00000   1.000 17.56747  ? 105 TYR AA CD2 1 
ATOM   798  C  CE1 . TYR A 1 105 ? 29.29700  24.12200  8.41800   1.000 18.83838  ? 105 TYR AA CE1 1 
ATOM   799  C  CE2 . TYR A 1 105 ? 29.40500  25.52800  6.48400   1.000 14.99293  ? 105 TYR AA CE2 1 
ATOM   800  C  CZ  . TYR A 1 105 ? 29.92500  25.11300  7.69300   1.000 18.51204  ? 105 TYR AA CZ  1 
ATOM   801  O  OH  . TYR A 1 105 ? 31.07500  25.69400  8.17700   1.000 17.98006  ? 105 TYR AA OH  1 
ATOM   802  N  N   . ASP A 1 106 ? 24.95700  26.30200  7.41800   1.000 9.14347   ? 106 ASP AA N   1 
ATOM   803  C  CA  . ASP A 1 106 ? 24.99900  27.75200  7.26700   1.000 5.91976   ? 106 ASP AA CA  1 
ATOM   804  C  C   . ASP A 1 106 ? 25.91900  28.40600  8.29300   1.000 10.58263  ? 106 ASP AA C   1 
ATOM   805  O  O   . ASP A 1 106 ? 25.75100  29.59000  8.60100   1.000 12.29924  ? 106 ASP AA O   1 
ATOM   806  C  CB  . ASP A 1 106 ? 23.59100  28.35000  7.36200   1.000 6.08789   ? 106 ASP AA CB  1 
ATOM   807  C  CG  . ASP A 1 106 ? 22.86500  27.95100  8.63600   1.000 9.24255   ? 106 ASP AA CG  1 
ATOM   808  O  OD1 . ASP A 1 106 ? 23.46300  27.24700  9.47700   1.000 9.74028   ? 106 ASP AA OD1 1 
ATOM   809  O  OD2 . ASP A 1 106 ? 21.69000  28.34400  8.79600   1.000 10.95401  ? 106 ASP AA OD2 1 
ATOM   810  N  N   . LEU A 1 107 ? 26.89000  27.66100  8.82400   1.000 18.43154  ? 107 LEU AA N   1 
ATOM   811  C  CA  . LEU A 1 107 ? 27.76300  28.18400  9.86800   1.000 15.33794  ? 107 LEU AA CA  1 
ATOM   812  C  C   . LEU A 1 107 ? 28.85700  29.09600  9.32900   1.000 18.86271  ? 107 LEU AA C   1 
ATOM   813  O  O   . LEU A 1 107 ? 29.41500  29.88800  10.09700  1.000 17.79819  ? 107 LEU AA O   1 
ATOM   814  C  CB  . LEU A 1 107 ? 28.40400  27.03200  10.64500  1.000 15.07588  ? 107 LEU AA CB  1 
ATOM   815  C  CG  . LEU A 1 107 ? 27.46900  25.97700  11.23900  1.000 21.45300  ? 107 LEU AA CG  1 
ATOM   816  C  CD1 . LEU A 1 107 ? 28.25900  24.99600  12.08900  1.000 27.66235  ? 107 LEU AA CD1 1 
ATOM   817  C  CD2 . LEU A 1 107 ? 26.36700  26.63000  12.05600  1.000 18.24170  ? 107 LEU AA CD2 1 
ATOM   818  N  N   . SER A 1 108 ? 29.18000  29.00600  8.04000   1.000 12.27479  ? 108 SER AA N   1 
ATOM   819  C  CA  . SER A 1 108 ? 30.25800  29.80200  7.46700   1.000 20.58153  ? 108 SER AA CA  1 
ATOM   820  C  C   . SER A 1 108 ? 29.82600  31.21600  7.09900   1.000 13.42409  ? 108 SER AA C   1 
ATOM   821  O  O   . SER A 1 108 ? 30.64900  31.98300  6.58800   1.000 17.53352  ? 108 SER AA O   1 
ATOM   822  C  CB  . SER A 1 108 ? 30.83800  29.09600  6.24000   1.000 17.88941  ? 108 SER AA CB  1 
ATOM   823  O  OG  . SER A 1 108 ? 31.74300  28.07900  6.63300   1.000 20.51418  ? 108 SER AA OG  1 
ATOM   824  N  N   A VAL A 1 109 ? 28.56600  31.57500  7.33600   0.364 17.04984  ? 109 VAL AA N   1 
ATOM   825  N  N   B VAL A 1 109 ? 28.56700  31.57300  7.33200   0.636 17.09199  ? 109 VAL AA N   1 
ATOM   826  C  CA  A VAL A 1 109 ? 28.07400  32.93200  7.13500   0.364 14.94871  ? 109 VAL AA CA  1 
ATOM   827  C  CA  B VAL A 1 109 ? 28.07600  32.93000  7.14100   0.636 14.92600  ? 109 VAL AA CA  1 
ATOM   828  C  C   A VAL A 1 109 ? 27.44900  33.40900  8.43800   0.364 12.67061  ? 109 VAL AA C   1 
ATOM   829  C  C   B VAL A 1 109 ? 27.46700  33.40300  8.45300   0.636 12.53870  ? 109 VAL AA C   1 
ATOM   830  O  O   A VAL A 1 109 ? 26.76700  32.64200  9.12600   0.364 16.67272  ? 109 VAL AA O   1 
ATOM   831  O  O   B VAL A 1 109 ? 26.82300  32.62400  9.16400   0.636 16.70879  ? 109 VAL AA O   1 
ATOM   832  C  CB  A VAL A 1 109 ? 27.05200  33.01600  5.98000   0.364 17.19292  ? 109 VAL AA CB  1 
ATOM   833  C  CB  B VAL A 1 109 ? 27.04400  33.01900  5.99600   0.636 17.25679  ? 109 VAL AA CB  1 
ATOM   834  C  CG1 A VAL A 1 109 ? 27.25700  34.29500  5.18400   0.364 15.18746  ? 109 VAL AA CG1 1 
ATOM   835  C  CG1 B VAL A 1 109 ? 27.74100  32.94000  4.64700   0.636 15.32657  ? 109 VAL AA CG1 1 
ATOM   836  C  CG2 A VAL A 1 109 ? 27.15400  31.79600  5.07500   0.364 15.17105  ? 109 VAL AA CG2 1 
ATOM   837  C  CG2 B VAL A 1 109 ? 25.99800  31.92100  6.12800   0.636 12.90870  ? 109 VAL AA CG2 1 
ATOM   838  N  N   . GLY A 1 110 ? 27.68300  34.67500  8.77600   1.000 12.81723  ? 110 GLY AA N   1 
ATOM   839  C  CA  . GLY A 1 110 ? 27.13100  35.21400  10.00900  1.000 18.00043  ? 110 GLY AA CA  1 
ATOM   840  C  C   . GLY A 1 110 ? 27.85200  34.67900  11.23300  1.000 17.87241  ? 110 GLY AA C   1 
ATOM   841  O  O   . GLY A 1 110 ? 29.07800  34.52100  11.24800  1.000 16.81375  ? 110 GLY AA O   1 
ATOM   842  N  N   . ASP A 1 111 ? 27.07700  34.39100  12.27700  1.000 17.31646  ? 111 ASP AA N   1 
ATOM   843  C  CA  . ASP A 1 111 ? 27.61400  33.92200  13.55100  1.000 16.93905  ? 111 ASP AA CA  1 
ATOM   844  C  C   . ASP A 1 111 ? 27.57500  32.39700  13.57500  1.000 14.15954  ? 111 ASP AA C   1 
ATOM   845  O  O   . ASP A 1 111 ? 26.49600  31.79600  13.58500  1.000 18.61591  ? 111 ASP AA O   1 
ATOM   846  C  CB  . ASP A 1 111 ? 26.82100  34.51200  14.71400  1.000 11.85046  ? 111 ASP AA CB  1 
ATOM   847  C  CG  . ASP A 1 111 ? 27.60800  34.53600  16.00900  1.000 22.33665  ? 111 ASP AA CG  1 
ATOM   848  O  OD1 . ASP A 1 111 ? 28.56900  33.74800  16.14100  1.000 26.82569  ? 111 ASP AA OD1 1 
ATOM   849  O  OD2 . ASP A 1 111 ? 27.26400  35.34400  16.89800  1.000 29.32253  ? 111 ASP AA OD2 1 
ATOM   850  N  N   . ALA A 1 112 ? 28.75600  31.77300  13.59600  1.000 14.58987  ? 112 ALA AA N   1 
ATOM   851  C  CA  . ALA A 1 112 ? 28.83700  30.31700  13.57000  1.000 12.25578  ? 112 ALA AA CA  1 
ATOM   852  C  C   . ALA A 1 112 ? 28.36300  29.67800  14.86700  1.000 24.92077  ? 112 ALA AA C   1 
ATOM   853  O  O   . ALA A 1 112 ? 28.02600  28.48900  14.86800  1.000 15.39898  ? 112 ALA AA O   1 
ATOM   854  C  CB  . ALA A 1 112 ? 30.27000  29.87400  13.27600  1.000 9.99996   ? 112 ALA AA CB  1 
ATOM   855  N  N   . ASN A 1 113 ? 28.32800  30.42800  15.96500  1.000 18.21438  ? 113 ASN AA N   1 
ATOM   856  C  CA  . ASN A 1 113 ? 27.97800  29.87800  17.26700  1.000 24.94836  ? 113 ASN AA CA  1 
ATOM   857  C  C   . ASN A 1 113 ? 26.49300  29.99500  17.59000  1.000 24.04635  ? 113 ASN AA C   1 
ATOM   858  O  O   . ASN A 1 113 ? 26.08000  29.58600  18.68100  1.000 23.23328  ? 113 ASN AA O   1 
ATOM   859  C  CB  . ASN A 1 113 ? 28.80300  30.56300  18.36000  1.000 23.56724  ? 113 ASN AA CB  1 
ATOM   860  C  CG  . ASN A 1 113 ? 30.29400  30.36100  18.17100  1.000 24.82790  ? 113 ASN AA CG  1 
ATOM   861  O  OD1 . ASN A 1 113 ? 30.79000  29.23500  18.21500  1.000 47.88883  ? 113 ASN AA OD1 1 
ATOM   862  N  ND2 . ASN A 1 113 ? 31.01700  31.45300  17.95000  1.000 27.77412  ? 113 ASN AA ND2 1 
ATOM   863  N  N   . VAL A 1 114 ? 25.68600  30.53200  16.68000  1.000 15.03914  ? 114 VAL AA N   1 
ATOM   864  C  CA  . VAL A 1 114 ? 24.24300  30.64700  16.86600  1.000 14.26435  ? 114 VAL AA CA  1 
ATOM   865  C  C   . VAL A 1 114 ? 23.56800  29.66900  15.91300  1.000 17.94645  ? 114 VAL AA C   1 
ATOM   866  O  O   . VAL A 1 114 ? 23.75100  29.75300  14.69200  1.000 10.43560  ? 114 VAL AA O   1 
ATOM   867  C  CB  . VAL A 1 114 ? 23.75000  32.08100  16.62300  1.000 25.71832  ? 114 VAL AA CB  1 
ATOM   868  C  CG1 . VAL A 1 114 ? 22.24000  32.16100  16.79800  1.000 21.26882  ? 114 VAL AA CG1 1 
ATOM   869  C  CG2 . VAL A 1 114 ? 24.45900  33.05500  17.55500  1.000 17.36851  ? 114 VAL AA CG2 1 
ATOM   870  N  N   . ARG A 1 115 ? 22.79600  28.74600  16.46600  1.000 15.02666  ? 115 ARG AA N   1 
ATOM   871  C  CA  . ARG A 1 115 ? 22.09300  27.72700  15.70400  1.000 16.13530  ? 115 ARG AA CA  1 
ATOM   872  C  C   . ARG A 1 115 ? 20.66700  27.61700  16.21500  1.000 17.37728  ? 115 ARG AA C   1 
ATOM   873  O  O   . ARG A 1 115 ? 20.37400  28.01100  17.35000  1.000 10.44680  ? 115 ARG AA O   1 
ATOM   874  C  CB  . ARG A 1 115 ? 22.78900  26.36100  15.82000  1.000 12.16688  ? 115 ARG AA CB  1 
ATOM   875  C  CG  . ARG A 1 115 ? 24.24800  26.35800  15.39900  1.000 16.84324  ? 115 ARG AA CG  1 
ATOM   876  C  CD  . ARG A 1 115 ? 25.15600  26.28800  16.61700  1.000 13.61226  ? 115 ARG AA CD  1 
ATOM   877  N  NE  . ARG A 1 115 ? 26.56800  26.31000  16.25600  1.000 24.84910  ? 115 ARG AA NE  1 
ATOM   878  C  CZ  . ARG A 1 115 ? 27.53800  25.79200  16.99800  1.000 22.38236  ? 115 ARG AA CZ  1 
ATOM   879  N  NH1 . ARG A 1 115 ? 27.28000  25.18600  18.14600  1.000 19.32842  ? 115 ARG AA NH1 1 
ATOM   880  N  NH2 . ARG A 1 115 ? 28.79600  25.88500  16.57800  1.000 20.15058  ? 115 ARG AA NH2 1 
ATOM   881  N  N   . PRO A 1 116 ? 19.75100  27.10400  15.39500  1.000 16.75987  ? 116 PRO AA N   1 
ATOM   882  C  CA  . PRO A 1 116 ? 18.39200  26.84000  15.88400  1.000 9.52201   ? 116 PRO AA CA  1 
ATOM   883  C  C   . PRO A 1 116 ? 18.39700  25.87200  17.05900  1.000 17.58759  ? 116 PRO AA C   1 
ATOM   884  O  O   . PRO A 1 116 ? 18.99800  24.79500  17.00200  1.000 15.12559  ? 116 PRO AA O   1 
ATOM   885  C  CB  . PRO A 1 116 ? 17.68400  26.25700  14.65700  1.000 12.40743  ? 116 PRO AA CB  1 
ATOM   886  C  CG  . PRO A 1 116 ? 18.41600  26.86100  13.50100  1.000 14.07053  ? 116 PRO AA CG  1 
ATOM   887  C  CD  . PRO A 1 116 ? 19.85400  26.93400  13.93500  1.000 6.48535   ? 116 PRO AA CD  1 
ATOM   888  N  N   . ASP A 1 117 ? 17.72700  26.27200  18.13300  1.000 9.52066   ? 117 ASP AA N   1 
ATOM   889  C  CA  . ASP A 1 117 ? 17.67000  25.51100  19.37200  1.000 12.57555  ? 117 ASP AA CA  1 
ATOM   890  C  C   . ASP A 1 117 ? 16.20900  25.24700  19.73700  1.000 12.93202  ? 117 ASP AA C   1 
ATOM   891  O  O   . ASP A 1 117 ? 15.29700  25.47500  18.93600  1.000 10.02750  ? 117 ASP AA O   1 
ATOM   892  C  CB  . ASP A 1 117 ? 18.41600  26.25100  20.48800  1.000 14.66287  ? 117 ASP AA CB  1 
ATOM   893  C  CG  . ASP A 1 117 ? 17.95700  27.69500  20.65100  1.000 16.07379  ? 117 ASP AA CG  1 
ATOM   894  O  OD1 . ASP A 1 117 ? 16.97200  28.10000  20.00000  1.000 9.40311   ? 117 ASP AA OD1 1 
ATOM   895  O  OD2 . ASP A 1 117 ? 18.58800  28.42900  21.44100  1.000 16.47899  ? 117 ASP AA OD2 1 
ATOM   896  N  N   . LEU A 1 118 ? 15.99600  24.76100  20.96300  1.000 6.81388   ? 118 LEU AA N   1 
ATOM   897  C  CA  . LEU A 1 118 ? 14.64000  24.48100  21.42800  1.000 12.17146  ? 118 LEU AA CA  1 
ATOM   898  C  C   . LEU A 1 118 ? 13.76400  25.72600  21.36500  1.000 6.71813   ? 118 LEU AA C   1 
ATOM   899  O  O   . LEU A 1 118 ? 12.58900  25.64900  20.98800  1.000 9.66641   ? 118 LEU AA O   1 
ATOM   900  C  CB  . LEU A 1 118 ? 14.67200  23.93500  22.85700  1.000 7.05221   ? 118 LEU AA CB  1 
ATOM   901  C  CG  . LEU A 1 118 ? 15.36200  22.59600  23.11800  1.000 10.74076  ? 118 LEU AA CG  1 
ATOM   902  C  CD1 . LEU A 1 118 ? 15.44300  22.32700  24.61300  1.000 8.73988   ? 118 LEU AA CD1 1 
ATOM   903  C  CD2 . LEU A 1 118 ? 14.63200  21.46700  22.40800  1.000 9.06828   ? 118 LEU AA CD2 1 
ATOM   904  N  N   . ALA A 1 119 ? 14.32300  26.88500  21.72200  1.000 14.46909  ? 119 ALA AA N   1 
ATOM   905  C  CA  . ALA A 1 119 ? 13.52800  28.10800  21.78700  1.000 10.48632  ? 119 ALA AA CA  1 
ATOM   906  C  C   . ALA A 1 119 ? 13.09600  28.56600  20.40000  1.000 11.92778  ? 119 ALA AA C   1 
ATOM   907  O  O   . ALA A 1 119 ? 11.91200  28.83100  20.16700  1.000 11.67800  ? 119 ALA AA O   1 
ATOM   908  C  CB  . ALA A 1 119 ? 14.31600  29.21000  22.49500  1.000 9.26150   ? 119 ALA AA CB  1 
ATOM   909  N  N   . MET A 1 120 ? 14.04400  28.68000  19.46600  1.000 9.79218   ? 120 MET AA N   1 
ATOM   910  C  CA  . MET A 1 120 ? 13.68200  29.16600  18.13700  1.000 13.92137  ? 120 MET AA CA  1 
ATOM   911  C  C   . MET A 1 120 ? 12.88000  28.13500  17.35100  1.000 17.36654  ? 120 MET AA C   1 
ATOM   912  O  O   . MET A 1 120 ? 12.07700  28.50900  16.48900  1.000 11.42414  ? 120 MET AA O   1 
ATOM   913  C  CB  . MET A 1 120 ? 14.93400  29.64300  17.38700  1.000 15.98090  ? 120 MET AA CB  1 
ATOM   914  C  CG  . MET A 1 120 ? 14.89100  29.51800  15.87000  1.000 18.81217  ? 120 MET AA CG  1 
ATOM   915  S  SD  . MET A 1 120 ? 16.14500  30.51900  15.03000  1.000 28.57410  ? 120 MET AA SD  1 
ATOM   916  C  CE  . MET A 1 120 ? 17.63000  30.17100  15.95400  1.000 32.99780  ? 120 MET AA CE  1 
ATOM   917  N  N   . GLY A 1 121 ? 13.03900  26.84800  17.65900  1.000 19.18194  ? 121 GLY AA N   1 
ATOM   918  C  CA  . GLY A 1 121 ? 12.11100  25.86400  17.12600  1.000 9.36685   ? 121 GLY AA CA  1 
ATOM   919  C  C   . GLY A 1 121 ? 10.68800  26.10300  17.60000  1.000 13.98375  ? 121 GLY AA C   1 
ATOM   920  O  O   . GLY A 1 121 ? 9.73300   25.97000  16.83000  1.000 14.73593  ? 121 GLY AA O   1 
ATOM   921  N  N   . ARG A 1 122 ? 10.52900  26.46400  18.87600  1.000 18.98136  ? 122 ARG AA N   1 
ATOM   922  C  CA  . ARG A 1 122 ? 9.20700   26.79500  19.40100  1.000 16.57112  ? 122 ARG AA CA  1 
ATOM   923  C  C   . ARG A 1 122 ? 8.66200   28.06700  18.76300  1.000 14.41613  ? 122 ARG AA C   1 
ATOM   924  O  O   . ARG A 1 122 ? 7.47100   28.14400  18.43700  1.000 11.24368  ? 122 ARG AA O   1 
ATOM   925  C  CB  . ARG A 1 122 ? 9.27500   26.94500  20.92100  1.000 11.87581  ? 122 ARG AA CB  1 
ATOM   926  C  CG  . ARG A 1 122 ? 7.96200   27.34600  21.57800  1.000 17.99745  ? 122 ARG AA CG  1 
ATOM   927  C  CD  . ARG A 1 122 ? 8.09500   27.37900  23.09300  1.000 14.40715  ? 122 ARG AA CD  1 
ATOM   928  N  NE  . ARG A 1 122 ? 6.97300   26.72400  23.75300  1.000 39.84580  ? 122 ARG AA NE  1 
ATOM   929  C  CZ  . ARG A 1 122 ? 5.79700   27.29500  23.97300  1.000 47.08314  ? 122 ARG AA CZ  1 
ATOM   930  N  NH1 . ARG A 1 122 ? 5.55100   28.54100  23.59900  1.000 36.63616  ? 122 ARG AA NH1 1 
ATOM   931  N  NH2 . ARG A 1 122 ? 4.84000   26.59700  24.57900  1.000 59.85899  ? 122 ARG AA NH2 1 
ATOM   932  N  N   . ARG A 1 123 ? 9.52000   29.07400  18.57800  1.000 12.55082  ? 123 ARG AA N   1 
ATOM   933  C  CA  . ARG A 1 123 ? 9.07400   30.33400  17.99100  1.000 18.20787  ? 123 ARG AA CA  1 
ATOM   934  C  C   . ARG A 1 123 ? 8.53900   30.12700  16.57800  1.000 21.36099  ? 123 ARG AA C   1 
ATOM   935  O  O   . ARG A 1 123 ? 7.57100   30.78100  16.17100  1.000 17.13105  ? 123 ARG AA O   1 
ATOM   936  C  CB  . ARG A 1 123 ? 10.22200  31.34600  17.99500  1.000 21.15970  ? 123 ARG AA CB  1 
ATOM   937  C  CG  . ARG A 1 123 ? 10.06100  32.48600  16.99900  1.000 53.49032  ? 123 ARG AA CG  1 
ATOM   938  C  CD  . ARG A 1 123 ? 10.97200  33.65900  17.33400  1.000 66.54368  ? 123 ARG AA CD  1 
ATOM   939  N  NE  . ARG A 1 123 ? 11.67400  34.16500  16.15900  1.000 84.11125  ? 123 ARG AA NE  1 
ATOM   940  C  CZ  . ARG A 1 123 ? 11.12100  34.92000  15.21800  1.000 88.07628  ? 123 ARG AA CZ  1 
ATOM   941  N  NH1 . ARG A 1 123 ? 9.84600   35.27300  15.27400  1.000 69.14547  ? 123 ARG AA NH1 1 
ATOM   942  N  NH2 . ARG A 1 123 ? 11.86500  35.33100  14.19500  1.000 38.21001  ? 123 ARG AA NH2 1 
ATOM   943  N  N   . ALA A 1 124 ? 9.15000   29.21200  15.82100  1.000 17.36324  ? 124 ALA AA N   1 
ATOM   944  C  CA  . ALA A 1 124 ? 8.68800   28.95100  14.46100  1.000 14.57959  ? 124 ALA AA CA  1 
ATOM   945  C  C   . ALA A 1 124 ? 7.27000   28.39400  14.45500  1.000 13.81985  ? 124 ALA AA C   1 
ATOM   946  O  O   . ALA A 1 124 ? 6.47700   28.70700  13.56000  1.000 14.50782  ? 124 ALA AA O   1 
ATOM   947  C  CB  . ALA A 1 124 ? 9.64700   27.99100  13.75600  1.000 12.20214  ? 124 ALA AA CB  1 
ATOM   948  N  N   . CYS A 1 125 ? 6.93400   27.56200  15.44500  1.000 10.02848  ? 125 CYS AA N   1 
ATOM   949  C  CA  . CYS A 1 125 ? 5.57000   27.05000  15.54600  1.000 7.46809   ? 125 CYS AA CA  1 
ATOM   950  C  C   . CYS A 1 125 ? 4.59300   28.15100  15.93600  1.000 14.76273  ? 125 CYS AA C   1 
ATOM   951  O  O   . CYS A 1 125 ? 3.44400   28.16000  15.47700  1.000 14.77081  ? 125 CYS AA O   1 
ATOM   952  C  CB  . CYS A 1 125 ? 5.50800   25.90800  16.55800  1.000 13.20602  ? 125 CYS AA CB  1 
ATOM   953  S  SG  . CYS A 1 125 ? 6.59800   24.52100  16.20400  1.000 16.77807  ? 125 CYS AA SG  1 
ATOM   954  N  N   . GLU A 1 126 ? 5.02800   29.08300  16.78800  1.000 14.17048  ? 126 GLU AA N   1 
ATOM   955  C  CA  . GLU A 1 126 ? 4.15700   30.18200  17.18900  1.000 19.38024  ? 126 GLU AA CA  1 
ATOM   956  C  C   . GLU A 1 126 ? 3.81800   31.08900  16.01200  1.000 18.87738  ? 126 GLU AA C   1 
ATOM   957  O  O   . GLU A 1 126 ? 2.74400   31.70200  15.99300  1.000 15.88416  ? 126 GLU AA O   1 
ATOM   958  C  CB  . GLU A 1 126 ? 4.81200   30.98900  18.31200  1.000 8.56483   ? 126 GLU AA CB  1 
ATOM   959  C  CG  . GLU A 1 126 ? 4.94300   30.23300  19.62800  1.000 17.36524  ? 126 GLU AA CG  1 
ATOM   960  C  CD  . GLU A 1 126 ? 5.68200   31.02800  20.69000  1.000 19.27223  ? 126 GLU AA CD  1 
ATOM   961  O  OE1 . GLU A 1 126 ? 6.03100   32.19700  20.42400  1.000 18.27801  ? 126 GLU AA OE1 1 
ATOM   962  O  OE2 . GLU A 1 126 ? 5.90900   30.48600  21.79200  1.000 16.15318  ? 126 GLU AA OE2 1 
ATOM   963  N  N   . ALA A 1 127 ? 4.70600   31.17600  15.02100  1.000 12.07227  ? 127 ALA AA N   1 
ATOM   964  C  CA  . ALA A 1 127 ? 4.50400   32.04100  13.86700  1.000 12.01337  ? 127 ALA AA CA  1 
ATOM   965  C  C   . ALA A 1 127 ? 3.73500   31.37100  12.73500  1.000 12.52588  ? 127 ALA AA C   1 
ATOM   966  O  O   . ALA A 1 127 ? 3.42400   32.03900  11.74200  1.000 16.45546  ? 127 ALA AA O   1 
ATOM   967  C  CB  . ALA A 1 127 ? 5.85500   32.53200  13.33800  1.000 10.22680  ? 127 ALA AA CB  1 
ATOM   968  N  N   . ALA A 1 128 ? 3.42000   30.08300  12.85600  1.000 15.03949  ? 128 ALA AA N   1 
ATOM   969  C  CA  . ALA A 1 128 ? 2.77600   29.35900  11.76700  1.000 11.48859  ? 128 ALA AA CA  1 
ATOM   970  C  C   . ALA A 1 128 ? 1.37700   29.90400  11.51200  1.000 14.31697  ? 128 ALA AA C   1 
ATOM   971  O  O   . ALA A 1 128 ? 0.56600   30.02100  12.43600  1.000 15.34146  ? 128 ALA AA O   1 
ATOM   972  C  CB  . ALA A 1 128 ? 2.71500   27.86700  12.08600  1.000 9.74816   ? 128 ALA AA CB  1 
ATOM   973  N  N   . LYS A 1 129 ? 1.09400   30.23400  10.25700  1.000 13.27776  ? 129 LYS AA N   1 
ATOM   974  C  CA  . LYS A 1 129 ? -0.18200  30.82000  9.88100   1.000 21.56095  ? 129 LYS AA CA  1 
ATOM   975  C  C   . LYS A 1 129 ? -0.53100  30.36700  8.47300   1.000 26.68589  ? 129 LYS AA C   1 
ATOM   976  O  O   . LYS A 1 129 ? 0.36100   30.01600  7.69000   1.000 14.21605  ? 129 LYS AA O   1 
ATOM   977  C  CB  . LYS A 1 129 ? -0.13800  32.35200  9.95600   1.000 14.52409  ? 129 LYS AA CB  1 
ATOM   978  C  CG  . LYS A 1 129 ? 0.93500   32.98900  9.09100   1.000 16.80722  ? 129 LYS AA CG  1 
ATOM   979  C  CD  . LYS A 1 129 ? 1.07200   34.47200  9.39800   1.000 22.48837  ? 129 LYS AA CD  1 
ATOM   980  C  CE  . LYS A 1 129 ? 1.71300   35.22400  8.24300   1.000 24.89499  ? 129 LYS AA CE  1 
ATOM   981  N  NZ  . LYS A 1 129 ? 3.18700   35.34400  8.41000   1.000 34.92791  ? 129 LYS AA NZ  1 
ATOM   982  N  N   . PRO A 1 130 ? -1.81200  30.35300  8.12200   1.000 18.46239  ? 130 PRO AA N   1 
ATOM   983  C  CA  . PRO A 1 130 ? -2.21700  30.02500  6.75300   1.000 16.78783  ? 130 PRO AA CA  1 
ATOM   984  C  C   . PRO A 1 130 ? -1.94500  31.19700  5.81400   1.000 16.37698  ? 130 PRO AA C   1 
ATOM   985  O  O   . PRO A 1 130 ? -1.41900  32.23600  6.20700   1.000 18.67785  ? 130 PRO AA O   1 
ATOM   986  C  CB  . PRO A 1 130 ? -3.71600  29.74700  6.88800   1.000 11.41246  ? 130 PRO AA CB  1 
ATOM   987  C  CG  . PRO A 1 130 ? -4.13900  30.54300  8.06900   1.000 17.96098  ? 130 PRO AA CG  1 
ATOM   988  C  CD  . PRO A 1 130 ? -2.97100  30.55100  9.01200   1.000 17.98332  ? 130 PRO AA CD  1 
ATOM   989  N  N   . GLY A 1 131 ? -2.31500  31.00900  4.55100   1.000 14.28928  ? 131 GLY AA N   1 
ATOM   990  C  CA  . GLY A 1 131 ? -2.15300  32.03800  3.55300   1.000 12.86204  ? 131 GLY AA CA  1 
ATOM   991  C  C   . GLY A 1 131 ? -0.72200  32.16400  3.07200   1.000 17.33132  ? 131 GLY AA C   1 
ATOM   992  O  O   . GLY A 1 131 ? 0.11200   31.27600  3.28000   1.000 15.43862  ? 131 GLY AA O   1 
ATOM   993  N  N   . PRO A 1 132 ? -0.40700  33.28300  2.42500   1.000 17.99519  ? 132 PRO AA N   1 
ATOM   994  C  CA  . PRO A 1 132 ? 0.93700   33.45300  1.86300   1.000 22.72261  ? 132 PRO AA CA  1 
ATOM   995  C  C   . PRO A 1 132 ? 1.97700   33.66200  2.95000   1.000 15.04196  ? 132 PRO AA C   1 
ATOM   996  O  O   . PRO A 1 132 ? 1.70200   34.23300  4.00800   1.000 17.39163  ? 132 PRO AA O   1 
ATOM   997  C  CB  . PRO A 1 132 ? 0.80600   34.70100  0.97700   1.000 14.22788  ? 132 PRO AA CB  1 
ATOM   998  C  CG  . PRO A 1 132 ? -0.64200  35.12900  1.05300   1.000 14.27741  ? 132 PRO AA CG  1 
ATOM   999  C  CD  . PRO A 1 132 ? -1.23400  34.48800  2.26100   1.000 21.91937  ? 132 PRO AA CD  1 
ATOM   1000 N  N   . PHE A 1 133 ? 3.18800   33.18400  2.67700   1.000 16.61154  ? 133 PHE AA N   1 
ATOM   1001 C  CA  . PHE A 1 133 ? 4.31600   33.36800  3.57600   1.000 14.07631  ? 133 PHE AA CA  1 
ATOM   1002 C  C   . PHE A 1 133 ? 5.47300   33.99900  2.81400   1.000 20.08021  ? 133 PHE AA C   1 
ATOM   1003 O  O   . PHE A 1 133 ? 5.53300   33.95500  1.58200   1.000 18.13097  ? 133 PHE AA O   1 
ATOM   1004 C  CB  . PHE A 1 133 ? 4.76000   32.04200  4.22400   1.000 10.32073  ? 133 PHE AA CB  1 
ATOM   1005 C  CG  . PHE A 1 133 ? 5.01900   30.93200  3.24000   1.000 14.05993  ? 133 PHE AA CG  1 
ATOM   1006 C  CD1 . PHE A 1 133 ? 6.27400   30.76700  2.67400   1.000 9.81088   ? 133 PHE AA CD1 1 
ATOM   1007 C  CD2 . PHE A 1 133 ? 4.01000   30.04700  2.89100   1.000 8.56300   ? 133 PHE AA CD2 1 
ATOM   1008 C  CE1 . PHE A 1 133 ? 6.51700   29.74500  1.77200   1.000 15.82974  ? 133 PHE AA CE1 1 
ATOM   1009 C  CE2 . PHE A 1 133 ? 4.24600   29.02300  1.98900   1.000 14.29386  ? 133 PHE AA CE2 1 
ATOM   1010 C  CZ  . PHE A 1 133 ? 5.50100   28.87200  1.43000   1.000 14.46886  ? 133 PHE AA CZ  1 
ATOM   1011 N  N   . GLU A 1 134 ? 6.39300   34.59200  3.56800   1.000 13.58759  ? 134 GLU AA N   1 
ATOM   1012 C  CA  . GLU A 1 134 ? 7.54200   35.25600  2.97300   1.000 16.60999  ? 134 GLU AA CA  1 
ATOM   1013 C  C   . GLU A 1 134 ? 8.50300   34.24000  2.36700   1.000 14.87940  ? 134 GLU AA C   1 
ATOM   1014 O  O   . GLU A 1 134 ? 8.60700   33.09700  2.82300   1.000 19.63867  ? 134 GLU AA O   1 
ATOM   1015 C  CB  . GLU A 1 134 ? 8.27200   36.09500  4.02200   1.000 11.28186  ? 134 GLU AA CB  1 
ATOM   1016 C  CG  . GLU A 1 134 ? 7.59100   37.40800  4.36300   1.000 40.11975  ? 134 GLU AA CG  1 
ATOM   1017 C  CD  . GLU A 1 134 ? 8.49600   38.34100  5.14400   1.000 68.00620  ? 134 GLU AA CD  1 
ATOM   1018 O  OE1 . GLU A 1 134 ? 8.64200   38.14100  6.36800   1.000 72.20561  ? 134 GLU AA OE1 1 
ATOM   1019 O  OE2 . GLU A 1 134 ? 9.06600   39.27000  4.53300   1.000 106.31444 ? 134 GLU AA OE2 1 
ATOM   1020 N  N   . ARG A 1 135 ? 9.21800   34.67200  1.33100   1.000 15.10181  ? 135 ARG AA N   1 
ATOM   1021 C  CA  . ARG A 1 135 ? 10.22300  33.85700  0.66300   1.000 17.22841  ? 135 ARG AA CA  1 
ATOM   1022 C  C   . ARG A 1 135 ? 11.54400  34.61600  0.64500   1.000 15.75895  ? 135 ARG AA C   1 
ATOM   1023 O  O   . ARG A 1 135 ? 11.63000  35.76800  1.08000   1.000 13.12977  ? 135 ARG AA O   1 
ATOM   1024 C  CB  . ARG A 1 135 ? 9.78300   33.48500  -0.75800  1.000 18.26433  ? 135 ARG AA CB  1 
ATOM   1025 C  CG  . ARG A 1 135 ? 8.58400   32.55500  -0.81100  1.000 10.62882  ? 135 ARG AA CG  1 
ATOM   1026 C  CD  . ARG A 1 135 ? 7.37700   33.25800  -1.40900  1.000 12.99472  ? 135 ARG AA CD  1 
ATOM   1027 N  NE  . ARG A 1 135 ? 7.46400   33.33400  -2.86200  1.000 11.31947  ? 135 ARG AA NE  1 
ATOM   1028 C  CZ  . ARG A 1 135 ? 6.86700   34.25900  -3.60100  1.000 31.75862  ? 135 ARG AA CZ  1 
ATOM   1029 N  NH1 . ARG A 1 135 ? 6.12400   35.20800  -3.05500  1.000 17.53196  ? 135 ARG AA NH1 1 
ATOM   1030 N  NH2 . ARG A 1 135 ? 7.02300   34.23400  -4.92200  1.000 16.72711  ? 135 ARG AA NH2 1 
ATOM   1031 N  N   . GLY A 1 136 ? 12.58400  33.96200  0.13200   1.000 17.38350  ? 136 GLY AA N   1 
ATOM   1032 C  CA  . GLY A 1 136 ? 13.90600  34.55700  0.08600   1.000 7.71221   ? 136 GLY AA CA  1 
ATOM   1033 C  C   . GLY A 1 136 ? 14.78200  34.14500  1.25100   1.000 9.56391   ? 136 GLY AA C   1 
ATOM   1034 O  O   . GLY A 1 136 ? 14.71400  33.00200  1.71400   1.000 14.59415  ? 136 GLY AA O   1 
ATOM   1035 N  N   . ARG A 1 137 ? 15.61100  35.06900  1.73900   1.000 11.01121  ? 137 ARG AA N   1 
ATOM   1036 C  CA  . ARG A 1 137 ? 16.50100  34.79600  2.86800   1.000 9.76247   ? 137 ARG AA CA  1 
ATOM   1037 C  C   . ARG A 1 137 ? 15.72800  34.98400  4.17500   1.000 18.41100  ? 137 ARG AA C   1 
ATOM   1038 O  O   . ARG A 1 137 ? 15.90100  35.95100  4.92000   1.000 11.54753  ? 137 ARG AA O   1 
ATOM   1039 C  CB  . ARG A 1 137 ? 17.73200  35.68800  2.80500   1.000 12.06733  ? 137 ARG AA CB  1 
ATOM   1040 C  CG  . ARG A 1 137 ? 18.58400  35.47000  1.56600   1.000 25.80493  ? 137 ARG AA CG  1 
ATOM   1041 C  CD  . ARG A 1 137 ? 20.00800  35.96900  1.77800   1.000 32.43143  ? 137 ARG AA CD  1 
ATOM   1042 N  NE  . ARG A 1 137 ? 20.13500  37.41700  1.64000   1.000 57.04739  ? 137 ARG AA NE  1 
ATOM   1043 C  CZ  . ARG A 1 137 ? 19.84200  38.11400  0.54800   1.000 59.92143  ? 137 ARG AA CZ  1 
ATOM   1044 N  NH1 . ARG A 1 137 ? 19.44000  37.52500  -0.56600  1.000 76.54920  ? 137 ARG AA NH1 1 
ATOM   1045 N  NH2 . ARG A 1 137 ? 19.97100  39.43800  0.57100   1.000 59.48622  ? 137 ARG AA NH2 1 
ATOM   1046 N  N   . VAL A 1 138 ? 14.85400  34.01700  4.44400   1.000 13.15212  ? 138 VAL AA N   1 
ATOM   1047 C  CA  . VAL A 1 138 ? 14.00400  34.02500  5.62600   1.000 14.33654  ? 138 VAL AA CA  1 
ATOM   1048 C  C   . VAL A 1 138 ? 13.89700  32.59400  6.13600   1.000 15.33664  ? 138 VAL AA C   1 
ATOM   1049 O  O   . VAL A 1 138 ? 14.05400  31.63300  5.37600   1.000 15.63247  ? 138 VAL AA O   1 
ATOM   1050 C  CB  . VAL A 1 138 ? 12.60700  34.61700  5.31600   1.000 13.20333  ? 138 VAL AA CB  1 
ATOM   1051 C  CG1 . VAL A 1 138 ? 11.79900  33.66300  4.44300   1.000 11.16032  ? 138 VAL AA CG1 1 
ATOM   1052 C  CG2 . VAL A 1 138 ? 11.85900  34.96000  6.59400   1.000 35.90290  ? 138 VAL AA CG2 1 
ATOM   1053 N  N   . GLY A 1 139 ? 13.64900  32.45700  7.43700   1.000 13.84060  ? 139 GLY AA N   1 
ATOM   1054 C  CA  . GLY A 1 139 ? 13.46400  31.13500  8.01400   1.000 10.62492  ? 139 GLY AA CA  1 
ATOM   1055 C  C   . GLY A 1 139 ? 14.67400  30.25000  7.78500   1.000 15.04805  ? 139 GLY AA C   1 
ATOM   1056 O  O   . GLY A 1 139 ? 15.82200  30.65700  7.99600   1.000 15.22031  ? 139 GLY AA O   1 
ATOM   1057 N  N   . GLY A 1 140 ? 14.41700  29.02200  7.32700   1.000 11.78105  ? 140 GLY AA N   1 
ATOM   1058 C  CA  . GLY A 1 140 ? 15.48800  28.06800  7.09400   1.000 9.83331   ? 140 GLY AA CA  1 
ATOM   1059 C  C   . GLY A 1 140 ? 16.45900  28.48100  6.00700   1.000 10.10823  ? 140 GLY AA C   1 
ATOM   1060 O  O   . GLY A 1 140 ? 17.59900  28.00600  5.99200   1.000 13.11114  ? 140 GLY AA O   1 
ATOM   1061 N  N   . GLY A 1 141 ? 16.03500  29.34700  5.09100   1.000 11.88228  ? 141 GLY AA N   1 
ATOM   1062 C  CA  . GLY A 1 141 ? 16.89100  29.86600  4.04600   1.000 16.83241  ? 141 GLY AA CA  1 
ATOM   1063 C  C   . GLY A 1 141 ? 17.60300  31.16100  4.37600   1.000 12.54824  ? 141 GLY AA C   1 
ATOM   1064 O  O   . GLY A 1 141 ? 18.16500  31.78400  3.46800   1.000 14.46476  ? 141 GLY AA O   1 
ATOM   1065 N  N   . THR A 1 142 ? 17.60800  31.58300  5.64600   1.000 16.38060  ? 142 THR AA N   1 
ATOM   1066 C  CA  . THR A 1 142 ? 18.20100  32.86900  6.00700   1.000 11.59950  ? 142 THR AA CA  1 
ATOM   1067 C  C   . THR A 1 142 ? 19.69200  32.90900  5.69200   1.000 16.32337  ? 142 THR AA C   1 
ATOM   1068 O  O   . THR A 1 142 ? 20.19800  33.91500  5.18000   1.000 10.86452  ? 142 THR AA O   1 
ATOM   1069 C  CB  . THR A 1 142 ? 17.95600  33.15800  7.48900   1.000 11.32766  ? 142 THR AA CB  1 
ATOM   1070 O  OG1 . THR A 1 142 ? 16.54700  33.28400  7.72400   1.000 11.55576  ? 142 THR AA OG1 1 
ATOM   1071 C  CG2 . THR A 1 142 ? 18.64800  34.44900  7.91500   1.000 11.87519  ? 142 THR AA CG2 1 
ATOM   1072 N  N   . GLY A 1 143 ? 20.41100  31.82500  5.97600   1.000 12.25122  ? 143 GLY AA N   1 
ATOM   1073 C  CA  . GLY A 1 143 ? 21.84100  31.79200  5.73600   1.000 8.33541   ? 143 GLY AA CA  1 
ATOM   1074 C  C   . GLY A 1 143 ? 22.25700  30.93400  4.55700   1.000 6.29206   ? 143 GLY AA C   1 
ATOM   1075 O  O   . GLY A 1 143 ? 23.42300  30.54100  4.44900   1.000 12.77840  ? 143 GLY AA O   1 
ATOM   1076 N  N   . ALA A 1 144 ? 21.31500  30.64700  3.66200   1.000 6.71966   ? 144 ALA AA N   1 
ATOM   1077 C  CA  . ALA A 1 144 ? 21.59000  29.75500  2.54200   1.000 11.53278  ? 144 ALA AA CA  1 
ATOM   1078 C  C   . ALA A 1 144 ? 22.44800  30.44400  1.48700   1.000 11.30971  ? 144 ALA AA C   1 
ATOM   1079 O  O   . ALA A 1 144 ? 22.26400  31.62800  1.18700   1.000 14.85348  ? 144 ALA AA O   1 
ATOM   1080 C  CB  . ALA A 1 144 ? 20.28300  29.27000  1.91800   1.000 6.26895   ? 144 ALA AA CB  1 
ATOM   1081 N  N   . THR A 1 145 ? 23.38800  29.68900  0.92000   1.000 10.43696  ? 145 THR AA N   1 
ATOM   1082 C  CA  . THR A 1 145 ? 24.27500  30.16800  -0.13100  1.000 14.55699  ? 145 THR AA CA  1 
ATOM   1083 C  C   . THR A 1 145 ? 24.32000  29.14300  -1.25700  1.000 11.77422  ? 145 THR AA C   1 
ATOM   1084 O  O   . THR A 1 145 ? 24.03500  27.96000  -1.05700  1.000 5.47350   ? 145 THR AA O   1 
ATOM   1085 C  CB  . THR A 1 145 ? 25.69300  30.42600  0.40100   1.000 15.80600  ? 145 THR AA CB  1 
ATOM   1086 O  OG1 . THR A 1 145 ? 26.13100  29.29100  1.15800   1.000 14.79718  ? 145 THR AA OG1 1 
ATOM   1087 C  CG2 . THR A 1 145 ? 25.71400  31.66100  1.29300   1.000 11.87808  ? 145 THR AA CG2 1 
ATOM   1088 N  N   . VAL A 1 146 ? 24.69200  29.60500  -2.45100  1.000 9.47122   ? 146 VAL AA N   1 
ATOM   1089 C  CA  . VAL A 1 146 ? 24.67800  28.78000  -3.65500  1.000 13.77322  ? 146 VAL AA CA  1 
ATOM   1090 C  C   . VAL A 1 146 ? 26.02600  28.89700  -4.35600  1.000 11.99377  ? 146 VAL AA C   1 
ATOM   1091 O  O   . VAL A 1 146 ? 26.51800  30.00800  -4.58200  1.000 20.38452  ? 146 VAL AA O   1 
ATOM   1092 C  CB  . VAL A 1 146 ? 23.54000  29.19100  -4.61000  1.000 15.37278  ? 146 VAL AA CB  1 
ATOM   1093 C  CG1 . VAL A 1 146 ? 23.64200  28.43300  -5.92600  1.000 7.07633   ? 146 VAL AA CG1 1 
ATOM   1094 C  CG2 . VAL A 1 146 ? 22.18900  28.95600  -3.95700  1.000 17.61587  ? 146 VAL AA CG2 1 
ATOM   1095 N  N   . GLY A 1 147 ? 26.61300  27.75300  -4.70800  1.000 12.00694  ? 147 GLY AA N   1 
ATOM   1096 C  CA  . GLY A 1 147 ? 27.83200  27.72700  -5.49700  1.000 10.29978  ? 147 GLY AA CA  1 
ATOM   1097 C  C   . GLY A 1 147 ? 29.09600  27.88800  -4.67900  1.000 19.04657  ? 147 GLY AA C   1 
ATOM   1098 O  O   . GLY A 1 147 ? 29.69700  28.96600  -4.66800  1.000 15.65586  ? 147 GLY AA O   1 
ATOM   1099 N  N   . LYS A 1 148 ? 29.52600  26.81800  -4.00900  1.000 10.57701  ? 148 LYS AA N   1 
ATOM   1100 C  CA  . LYS A 1 148 ? 30.60400  26.88500  -3.02900  1.000 13.60447  ? 148 LYS AA CA  1 
ATOM   1101 C  C   . LYS A 1 148 ? 31.87600  26.17800  -3.49700  1.000 17.25158  ? 148 LYS AA C   1 
ATOM   1102 O  O   . LYS A 1 148 ? 32.63800  25.66000  -2.67800  1.000 17.65288  ? 148 LYS AA O   1 
ATOM   1103 C  CB  . LYS A 1 148 ? 30.13300  26.30600  -1.69500  1.000 9.67287   ? 148 LYS AA CB  1 
ATOM   1104 C  CG  . LYS A 1 148 ? 29.40400  27.31100  -0.81500  1.000 17.37905  ? 148 LYS AA CG  1 
ATOM   1105 C  CD  . LYS A 1 148 ? 28.34500  26.64500  0.04700   1.000 29.23308  ? 148 LYS AA CD  1 
ATOM   1106 C  CE  . LYS A 1 148 ? 27.00600  26.57800  -0.66700  1.000 13.59212  ? 148 LYS AA CE  1 
ATOM   1107 N  NZ  . LYS A 1 148 ? 25.91200  26.16800  0.25600   1.000 14.90753  ? 148 LYS AA NZ  1 
ATOM   1108 N  N   . LEU A 1 149 ? 32.12500  26.16300  -4.81000  1.000 13.44215  ? 149 LEU AA N   1 
ATOM   1109 C  CA  . LEU A 1 149 ? 33.33400  25.52600  -5.32800  1.000 12.18976  ? 149 LEU AA CA  1 
ATOM   1110 C  C   . LEU A 1 149 ? 34.59200  26.19300  -4.78200  1.000 15.80588  ? 149 LEU AA C   1 
ATOM   1111 O  O   . LEU A 1 149 ? 35.55600  25.51100  -4.41300  1.000 10.20083  ? 149 LEU AA O   1 
ATOM   1112 C  CB  . LEU A 1 149 ? 33.33100  25.56200  -6.85700  1.000 15.74722  ? 149 LEU AA CB  1 
ATOM   1113 C  CG  . LEU A 1 149 ? 34.62900  25.17100  -7.57100  1.000 22.37529  ? 149 LEU AA CG  1 
ATOM   1114 C  CD1 . LEU A 1 149 ? 34.93400  23.69200  -7.38300  1.000 14.98591  ? 149 LEU AA CD1 1 
ATOM   1115 C  CD2 . LEU A 1 149 ? 34.55700  25.52300  -9.05100  1.000 18.52597  ? 149 LEU AA CD2 1 
ATOM   1116 N  N   . TYR A 1 150 ? 34.60100  27.52500  -4.72100  1.000 10.48982  ? 150 TYR AA N   1 
ATOM   1117 C  CA  . TYR A 1 150 ? 35.73300  28.28700  -4.21000  1.000 20.10723  ? 150 TYR AA CA  1 
ATOM   1118 C  C   . TYR A 1 150 ? 35.48800  28.80800  -2.79800  1.000 24.27938  ? 150 TYR AA C   1 
ATOM   1119 O  O   . TYR A 1 150 ? 36.06200  29.82800  -2.40300  1.000 21.17961  ? 150 TYR AA O   1 
ATOM   1120 C  CB  . TYR A 1 150 ? 36.05600  29.44800  -5.15000  1.000 18.18564  ? 150 TYR AA CB  1 
ATOM   1121 C  CG  . TYR A 1 150 ? 36.30600  29.03200  -6.58000  1.000 24.73206  ? 150 TYR AA CG  1 
ATOM   1122 C  CD1 . TYR A 1 150 ? 37.28000  28.09200  -6.88900  1.000 16.52423  ? 150 TYR AA CD1 1 
ATOM   1123 C  CD2 . TYR A 1 150 ? 35.57000  29.58000  -7.62200  1.000 18.04176  ? 150 TYR AA CD2 1 
ATOM   1124 C  CE1 . TYR A 1 150 ? 37.51400  27.70900  -8.19500  1.000 27.23536  ? 150 TYR AA CE1 1 
ATOM   1125 C  CE2 . TYR A 1 150 ? 35.79700  29.20400  -8.93200  1.000 20.38714  ? 150 TYR AA CE2 1 
ATOM   1126 C  CZ  . TYR A 1 150 ? 36.77000  28.26800  -9.21300  1.000 16.13142  ? 150 TYR AA CZ  1 
ATOM   1127 O  OH  . TYR A 1 150 ? 36.99900  27.89000  -10.51400 1.000 22.57017  ? 150 TYR AA OH  1 
ATOM   1128 N  N   . GLY A 1 151 ? 34.64500  28.12800  -2.02900  1.000 22.57806  ? 151 GLY AA N   1 
ATOM   1129 C  CA  . GLY A 1 151 ? 34.29200  28.58300  -0.70300  1.000 17.90731  ? 151 GLY AA CA  1 
ATOM   1130 C  C   . GLY A 1 151 ? 33.12700  29.55500  -0.71700  1.000 19.83727  ? 151 GLY AA C   1 
ATOM   1131 O  O   . GLY A 1 151 ? 32.68600  30.04700  -1.75900  1.000 12.72906  ? 151 GLY AA O   1 
ATOM   1132 N  N   . VAL A 1 152 ? 32.63100  29.84800  0.48700   1.000 16.14403  ? 152 VAL AA N   1 
ATOM   1133 C  CA  . VAL A 1 152 ? 31.41100  30.63500  0.61900   1.000 19.91871  ? 152 VAL AA CA  1 
ATOM   1134 C  C   . VAL A 1 152 ? 31.60200  32.08700  0.19100   1.000 12.97519  ? 152 VAL AA C   1 
ATOM   1135 O  O   . VAL A 1 152 ? 30.61500  32.77800  -0.08400  1.000 17.56971  ? 152 VAL AA O   1 
ATOM   1136 C  CB  . VAL A 1 152 ? 30.88400  30.55700  2.06600   1.000 20.35951  ? 152 VAL AA CB  1 
ATOM   1137 C  CG1 . VAL A 1 152 ? 31.55000  31.60700  2.94400   1.000 18.29228  ? 152 VAL AA CG1 1 
ATOM   1138 C  CG2 . VAL A 1 152 ? 29.37300  30.71000  2.09000   1.000 23.13486  ? 152 VAL AA CG2 1 
ATOM   1139 N  N   . ARG A 1 153 ? 32.84100  32.57500  0.10900   1.000 14.60932  ? 153 ARG AA N   1 
ATOM   1140 C  CA  . ARG A 1 153 ? 33.04000  33.97900  -0.23200  1.000 24.44680  ? 153 ARG AA CA  1 
ATOM   1141 C  C   . ARG A 1 153 ? 32.85900  34.25200  -1.72200  1.000 17.88349  ? 153 ARG AA C   1 
ATOM   1142 O  O   . ARG A 1 153 ? 32.53500  35.38300  -2.09700  1.000 20.08996  ? 153 ARG AA O   1 
ATOM   1143 C  CB  . ARG A 1 153 ? 34.42300  34.44700  0.24800   1.000 34.03457  ? 153 ARG AA CB  1 
ATOM   1144 C  CG  . ARG A 1 153 ? 34.76400  35.96000  0.11400   1.000 56.26951  ? 153 ARG AA CG  1 
ATOM   1145 C  CD  . ARG A 1 153 ? 33.60200  36.96700  0.29100   1.000 81.29875  ? 153 ARG AA CD  1 
ATOM   1146 N  NE  . ARG A 1 153 ? 32.53000  36.52600  1.17700   1.000 110.55751 ? 153 ARG AA NE  1 
ATOM   1147 C  CZ  . ARG A 1 153 ? 31.25600  36.87000  1.03800   1.000 91.86270  ? 153 ARG AA CZ  1 
ATOM   1148 N  NH1 . ARG A 1 153 ? 30.85700  37.66000  0.05500   1.000 69.25184  ? 153 ARG AA NH1 1 
ATOM   1149 N  NH2 . ARG A 1 153 ? 30.35900  36.39900  1.90000   1.000 61.36150  ? 153 ARG AA NH2 1 
ATOM   1150 N  N   . GLN A 1 154 ? 33.02600  33.24500  -2.57900  1.000 15.06775  ? 154 GLN AA N   1 
ATOM   1151 C  CA  . GLN A 1 154 ? 32.76900  33.39800  -4.00500  1.000 12.29390  ? 154 GLN AA CA  1 
ATOM   1152 C  C   . GLN A 1 154 ? 31.42800  32.79500  -4.41400  1.000 19.51588  ? 154 GLN AA C   1 
ATOM   1153 O  O   . GLN A 1 154 ? 31.24300  32.40600  -5.57200  1.000 16.10899  ? 154 GLN AA O   1 
ATOM   1154 C  CB  . GLN A 1 154 ? 33.91400  32.79200  -4.81400  1.000 12.70596  ? 154 GLN AA CB  1 
ATOM   1155 C  CG  . GLN A 1 154 ? 35.11700  33.72000  -4.91600  1.000 22.47236  ? 154 GLN AA CG  1 
ATOM   1156 C  CD  . GLN A 1 154 ? 36.37900  33.01100  -5.36100  1.000 36.54374  ? 154 GLN AA CD  1 
ATOM   1157 O  OE1 . GLN A 1 154 ? 37.29400  32.79700  -4.56500  1.000 43.28662  ? 154 GLN AA OE1 1 
ATOM   1158 N  NE2 . GLN A 1 154 ? 36.44200  32.65300  -6.63800  1.000 33.47047  ? 154 GLN AA NE2 1 
ATOM   1159 N  N   . SER A 1 155 ? 30.48200  32.73000  -3.48300  1.000 16.05787  ? 155 SER AA N   1 
ATOM   1160 C  CA  . SER A 1 155 ? 29.17400  32.14000  -3.72100  1.000 14.44718  ? 155 SER AA CA  1 
ATOM   1161 C  C   . SER A 1 155 ? 28.12100  33.22300  -3.94100  1.000 18.21667  ? 155 SER AA C   1 
ATOM   1162 O  O   . SER A 1 155 ? 28.36600  34.41800  -3.76700  1.000 17.24448  ? 155 SER AA O   1 
ATOM   1163 C  CB  . SER A 1 155 ? 28.77100  31.24200  -2.54700  1.000 18.51183  ? 155 SER AA CB  1 
ATOM   1164 O  OG  . SER A 1 155 ? 28.50600  32.01100  -1.38500  1.000 12.58177  ? 155 SER AA OG  1 
ATOM   1165 N  N   . SER A 1 156 ? 26.93400  32.77800  -4.33000  1.000 12.63026  ? 156 SER AA N   1 
ATOM   1166 C  CA  . SER A 1 156 ? 25.75700  33.61100  -4.49300  1.000 12.85002  ? 156 SER AA CA  1 
ATOM   1167 C  C   . SER A 1 156 ? 24.76500  33.34300  -3.36600  1.000 16.12091  ? 156 SER AA C   1 
ATOM   1168 O  O   . SER A 1 156 ? 24.78500  32.27200  -2.75200  1.000 12.61029  ? 156 SER AA O   1 
ATOM   1169 C  CB  . SER A 1 156 ? 25.08600  33.34100  -5.84800  1.000 15.02217  ? 156 SER AA CB  1 
ATOM   1170 O  OG  . SER A 1 156 ? 25.99200  33.54400  -6.91900  1.000 11.97328  ? 156 SER AA OG  1 
ATOM   1171 N  N   . PRO A 1 157 ? 23.88500  34.29600  -3.05700  1.000 17.05011  ? 157 PRO AA N   1 
ATOM   1172 C  CA  . PRO A 1 157 ? 22.89400  34.04800  -2.00400  1.000 19.14619  ? 157 PRO AA CA  1 
ATOM   1173 C  C   . PRO A 1 157 ? 21.83100  33.06200  -2.46300  1.000 16.09164  ? 157 PRO AA C   1 
ATOM   1174 O  O   . PRO A 1 157 ? 21.36500  33.10500  -3.60400  1.000 16.83814  ? 157 PRO AA O   1 
ATOM   1175 C  CB  . PRO A 1 157 ? 22.29100  35.43200  -1.72600  1.000 17.22490  ? 157 PRO AA CB  1 
ATOM   1176 C  CG  . PRO A 1 157 ? 22.78600  36.34300  -2.78900  1.000 9.51181   ? 157 PRO AA CG  1 
ATOM   1177 C  CD  . PRO A 1 157 ? 23.74200  35.62400  -3.68000  1.000 11.76477  ? 157 PRO AA CD  1 
ATOM   1178 N  N   . GLY A 1 158 ? 21.46400  32.16000  -1.56300  1.000 15.02626  ? 158 GLY AA N   1 
ATOM   1179 C  CA  . GLY A 1 158 ? 20.35000  31.25500  -1.74400  1.000 12.77628  ? 158 GLY AA CA  1 
ATOM   1180 C  C   . GLY A 1 158 ? 19.09300  31.78600  -1.08900  1.000 19.52618  ? 158 GLY AA C   1 
ATOM   1181 O  O   . GLY A 1 158 ? 18.90600  33.00000  -0.94500  1.000 20.29546  ? 158 GLY AA O   1 
ATOM   1182 N  N   . GLY A 1 159 ? 18.22200  30.87500  -0.68000  1.000 6.13493   ? 159 GLY AA N   1 
ATOM   1183 C  CA  . GLY A 1 159 ? 17.03300  31.27100  0.04500   1.000 11.75510  ? 159 GLY AA CA  1 
ATOM   1184 C  C   . GLY A 1 159 ? 15.99300  30.16700  0.06100   1.000 8.69649   ? 159 GLY AA C   1 
ATOM   1185 O  O   . GLY A 1 159 ? 16.27100  29.01300  -0.26100  1.000 12.13857  ? 159 GLY AA O   1 
ATOM   1186 N  N   . LEU A 1 160 ? 14.78700  30.56100  0.45800   1.000 8.54261   ? 160 LEU AA N   1 
ATOM   1187 C  CA  . LEU A 1 160 ? 13.62900  29.68100  0.51600   1.000 12.24180  ? 160 LEU AA CA  1 
ATOM   1188 C  C   . LEU A 1 160 ? 12.65100  30.08600  -0.57800  1.000 13.61470  ? 160 LEU AA C   1 
ATOM   1189 O  O   . LEU A 1 160 ? 12.32300  31.26900  -0.71400  1.000 11.78530  ? 160 LEU AA O   1 
ATOM   1190 C  CB  . LEU A 1 160 ? 12.95700  29.75600  1.89100   1.000 10.34240  ? 160 LEU AA CB  1 
ATOM   1191 C  CG  . LEU A 1 160 ? 11.74500  28.85600  2.15500   1.000 15.88237  ? 160 LEU AA CG  1 
ATOM   1192 C  CD1 . LEU A 1 160 ? 11.79500  28.29600  3.56800   1.000 8.32536   ? 160 LEU AA CD1 1 
ATOM   1193 C  CD2 . LEU A 1 160 ? 10.43700  29.60400  1.92200   1.000 7.52643   ? 160 LEU AA CD2 1 
ATOM   1194 N  N   . GLY A 1 161 ? 12.18800  29.10300  -1.35700  1.000 7.11315   ? 161 GLY AA N   1 
ATOM   1195 C  CA  . GLY A 1 161 ? 11.27100  29.36000  -2.44300  1.000 9.40727   ? 161 GLY AA CA  1 
ATOM   1196 C  C   . GLY A 1 161 ? 10.06400  28.44200  -2.37000  1.000 8.48940   ? 161 GLY AA C   1 
ATOM   1197 O  O   . GLY A 1 161 ? 10.02600  27.48800  -1.59000  1.000 11.41338  ? 161 GLY AA O   1 
ATOM   1198 N  N   . THR A 1 162 ? 9.07500   28.74700  -3.20700  1.000 5.61834   ? 162 THR AA N   1 
ATOM   1199 C  CA  . THR A 1 162 ? 7.84000   27.97600  -3.22500  1.000 10.54038  ? 162 THR AA CA  1 
ATOM   1200 C  C   . THR A 1 162 ? 7.17000   28.13900  -4.58200  1.000 14.05245  ? 162 THR AA C   1 
ATOM   1201 O  O   . THR A 1 162 ? 7.39100   29.12400  -5.29100  1.000 11.55315  ? 162 THR AA O   1 
ATOM   1202 C  CB  . THR A 1 162 ? 6.89400   28.40400  -2.09500  1.000 9.74441   ? 162 THR AA CB  1 
ATOM   1203 O  OG1 . THR A 1 162 ? 5.76900   27.51900  -2.04700  1.000 9.23488   ? 162 THR AA OG1 1 
ATOM   1204 C  CG2 . THR A 1 162 ? 6.40600   29.83100  -2.31000  1.000 13.03922  ? 162 THR AA CG2 1 
ATOM   1205 N  N   . ALA A 1 163 ? 6.35100   27.14800  -4.93300  1.000 14.78571  ? 163 ALA AA N   1 
ATOM   1206 C  CA  . ALA A 1 163 ? 5.61900   27.15900  -6.19300  1.000 6.23919   ? 163 ALA AA CA  1 
ATOM   1207 C  C   . ALA A 1 163 ? 4.46200   26.17600  -6.09600  1.000 11.20822  ? 163 ALA AA C   1 
ATOM   1208 O  O   . ALA A 1 163 ? 4.48200   25.24400  -5.28800  1.000 11.94818  ? 163 ALA AA O   1 
ATOM   1209 C  CB  . ALA A 1 163 ? 6.52600   26.80700  -7.37800  1.000 10.52652  ? 163 ALA AA CB  1 
ATOM   1210 N  N   . THR A 1 164 ? 3.45100   26.39900  -6.93400  1.000 6.45037   ? 164 THR AA N   1 
ATOM   1211 C  CA  . THR A 1 164 ? 2.27700   25.53800  -7.00500  1.000 9.01427   ? 164 THR AA CA  1 
ATOM   1212 C  C   . THR A 1 164 ? 2.00300   25.18400  -8.45800  1.000 13.69990  ? 164 THR AA C   1 
ATOM   1213 O  O   . THR A 1 164 ? 1.99200   26.06500  -9.32400  1.000 16.50172  ? 164 THR AA O   1 
ATOM   1214 C  CB  . THR A 1 164 ? 1.04500   26.21400  -6.38600  1.000 12.07834  ? 164 THR AA CB  1 
ATOM   1215 O  OG1 . THR A 1 164 ? 1.21000   26.30700  -4.96500  1.000 8.75168   ? 164 THR AA OG1 1 
ATOM   1216 C  CG2 . THR A 1 164 ? -0.21800  25.41500  -6.69200  1.000 7.65378   ? 164 THR AA CG2 1 
ATOM   1217 N  N   . VAL A 1 165 ? 1.79000   23.89700  -8.72300  1.000 9.70669   ? 165 VAL AA N   1 
ATOM   1218 C  CA  . VAL A 1 165 ? 1.43800   23.40000  -10.04700 1.000 8.34218   ? 165 VAL AA CA  1 
ATOM   1219 C  C   . VAL A 1 165 ? -0.00300  22.91200  -10.00000 1.000 18.70156  ? 165 VAL AA C   1 
ATOM   1220 O  O   . VAL A 1 165 ? -0.36800  22.11600  -9.12700  1.000 16.82486  ? 165 VAL AA O   1 
ATOM   1221 C  CB  . VAL A 1 165 ? 2.38800   22.27700  -10.50000 1.000 11.58257  ? 165 VAL AA CB  1 
ATOM   1222 C  CG1 . VAL A 1 165 ? 1.88300   21.63200  -11.78300 1.000 11.67064  ? 165 VAL AA CG1 1 
ATOM   1223 C  CG2 . VAL A 1 165 ? 3.79400   22.82200  -10.69200 1.000 13.83857  ? 165 VAL AA CG2 1 
ATOM   1224 N  N   A SER A 1 166 ? -0.81700  23.39100  -10.93800 0.993 15.44050  ? 166 SER AA N   1 
ATOM   1225 C  CA  A SER A 1 166 ? -2.22800  23.04000  -11.02100 0.993 18.56226  ? 166 SER AA CA  1 
ATOM   1226 C  C   A SER A 1 166 ? -2.44300  22.02200  -12.13200 0.993 16.41736  ? 166 SER AA C   1 
ATOM   1227 O  O   A SER A 1 166 ? -1.93700  22.19400  -13.24600 0.993 27.51074  ? 166 SER AA O   1 
ATOM   1228 C  CB  A SER A 1 166 ? -3.08400  24.28100  -11.27900 0.993 15.99959  ? 166 SER AA CB  1 
ATOM   1229 O  OG  A SER A 1 166 ? -3.67800  24.74700  -10.08100 0.993 45.13904  ? 166 SER AA OG  1 
ATOM   1230 N  N   . LEU A 1 167 ? -3.19100  20.96400  -11.82500 1.000 13.80496  ? 167 LEU AA N   1 
ATOM   1231 C  CA  . LEU A 1 167 ? -3.56300  19.97500  -12.82400 1.000 21.11552  ? 167 LEU AA CA  1 
ATOM   1232 C  C   . LEU A 1 167 ? -5.08200  19.97100  -12.99200 1.000 25.48587  ? 167 LEU AA C   1 
ATOM   1233 O  O   . LEU A 1 167 ? -5.76400  20.91900  -12.58100 1.000 24.45077  ? 167 LEU AA O   1 
ATOM   1234 C  CB  . LEU A 1 167 ? -3.00300  18.60000  -12.44200 1.000 12.88542  ? 167 LEU AA CB  1 
ATOM   1235 C  CG  . LEU A 1 167 ? -1.64200  18.55100  -11.74300 1.000 29.98329  ? 167 LEU AA CG  1 
ATOM   1236 C  CD1 . LEU A 1 167 ? -1.44800  17.22700  -11.02000 1.000 38.93604  ? 167 LEU AA CD1 1 
ATOM   1237 C  CD2 . LEU A 1 167 ? -0.51600  18.78400  -12.73500 1.000 28.82299  ? 167 LEU AA CD2 1 
ATOM   1238 N  N   . TYR A 1 168 ? -5.61300  18.90900  -13.59200 1.000 18.96279  ? 168 TYR AA N   1 
ATOM   1239 C  CA  . TYR A 1 168 ? -7.03800  18.82100  -13.86500 1.000 18.27625  ? 168 TYR AA CA  1 
ATOM   1240 C  C   . TYR A 1 168 ? -7.81600  18.49300  -12.59400 1.000 21.76128  ? 168 TYR AA C   1 
ATOM   1241 O  O   . TYR A 1 168 ? -7.26700  18.00400  -11.60300 1.000 18.77114  ? 168 TYR AA O   1 
ATOM   1242 C  CB  . TYR A 1 168 ? -7.31900  17.76000  -14.93200 1.000 11.07894  ? 168 TYR AA CB  1 
ATOM   1243 C  CG  . TYR A 1 168 ? -6.90600  16.35500  -14.53500 1.000 20.86871  ? 168 TYR AA CG  1 
ATOM   1244 C  CD1 . TYR A 1 168 ? -7.78200  15.51500  -13.85600 1.000 10.92571  ? 168 TYR AA CD1 1 
ATOM   1245 C  CD2 . TYR A 1 168 ? -5.64200  15.86800  -14.84300 1.000 16.04444  ? 168 TYR AA CD2 1 
ATOM   1246 C  CE1 . TYR A 1 168 ? -7.40800  14.23500  -13.49000 1.000 13.75303  ? 168 TYR AA CE1 1 
ATOM   1247 C  CE2 . TYR A 1 168 ? -5.26000  14.58700  -14.48200 1.000 15.06943  ? 168 TYR AA CE2 1 
ATOM   1248 C  CZ  . TYR A 1 168 ? -6.14800  13.77600  -13.80600 1.000 16.84551  ? 168 TYR AA CZ  1 
ATOM   1249 O  OH  . TYR A 1 168 ? -5.77600  12.50300  -13.44300 1.000 13.58486  ? 168 TYR AA OH  1 
ATOM   1250 N  N   . GLY A 1 169 ? -9.11800  18.77000  -12.63900 1.000 23.33448  ? 169 GLY AA N   1 
ATOM   1251 C  CA  . GLY A 1 169 ? -10.02900 18.34100  -11.58800 1.000 16.73180  ? 169 GLY AA CA  1 
ATOM   1252 C  C   . GLY A 1 169 ? -9.73500  18.90500  -10.21700 1.000 18.79212  ? 169 GLY AA C   1 
ATOM   1253 O  O   . GLY A 1 169 ? -10.07700 18.27400  -9.21000  1.000 23.43980  ? 169 GLY AA O   1 
ATOM   1254 N  N   . GLY A 1 170 ? -9.11200  20.07800  -10.14500 1.000 11.02868  ? 170 GLY AA N   1 
ATOM   1255 C  CA  . GLY A 1 170 ? -8.80900  20.68000  -8.86300  1.000 9.92388   ? 170 GLY AA CA  1 
ATOM   1256 C  C   . GLY A 1 170 ? -7.63000  20.07700  -8.13600  1.000 23.93787  ? 170 GLY AA C   1 
ATOM   1257 O  O   . GLY A 1 170 ? -7.47800  20.30400  -6.93200  1.000 22.70714  ? 170 GLY AA O   1 
ATOM   1258 N  N   . ILE A 1 171 ? -6.78900  19.31500  -8.82700  1.000 15.33387  ? 171 ILE AA N   1 
ATOM   1259 C  CA  . ILE A 1 171 ? -5.61100  18.71900  -8.21000  1.000 14.72792  ? 171 ILE AA CA  1 
ATOM   1260 C  C   . ILE A 1 171 ? -4.49800  19.75700  -8.14300  1.000 20.74594  ? 171 ILE AA C   1 
ATOM   1261 O  O   . ILE A 1 171 ? -4.28300  20.52500  -9.09000  1.000 15.31953  ? 171 ILE AA O   1 
ATOM   1262 C  CB  . ILE A 1 171 ? -5.16900  17.46800  -8.99100  1.000 17.11564  ? 171 ILE AA CB  1 
ATOM   1263 C  CG1 . ILE A 1 171 ? -6.25400  16.39100  -8.93200  1.000 25.58449  ? 171 ILE AA CG1 1 
ATOM   1264 C  CG2 . ILE A 1 171 ? -3.86500  16.92200  -8.44000  1.000 15.16710  ? 171 ILE AA CG2 1 
ATOM   1265 C  CD1 . ILE A 1 171 ? -6.07100  15.28800  -9.95300  1.000 21.46119  ? 171 ILE AA CD1 1 
ATOM   1266 N  N   . LYS A 1 172 ? -3.78900  19.78800  -7.01700  1.000 18.49188  ? 172 LYS AA N   1 
ATOM   1267 C  CA  . LYS A 1 172 ? -2.67900  20.70800  -6.81900  1.000 18.77835  ? 172 LYS AA CA  1 
ATOM   1268 C  C   . LYS A 1 172 ? -1.47400  19.96300  -6.26400  1.000 11.21760  ? 172 LYS AA C   1 
ATOM   1269 O  O   . LYS A 1 172 ? -1.61500  19.05200  -5.44300  1.000 13.51709  ? 172 LYS AA O   1 
ATOM   1270 C  CB  . LYS A 1 172 ? -3.05800  21.85000  -5.86800  1.000 17.93395  ? 172 LYS AA CB  1 
ATOM   1271 C  CG  . LYS A 1 172 ? -3.78000  23.00600  -6.53800  1.000 24.11838  ? 172 LYS AA CG  1 
ATOM   1272 C  CD  . LYS A 1 172 ? -4.53400  23.84600  -5.52000  1.000 29.49344  ? 172 LYS AA CD  1 
ATOM   1273 C  CE  . LYS A 1 172 ? -5.39400  24.89700  -6.20100  1.000 35.79454  ? 172 LYS AA CE  1 
ATOM   1274 N  NZ  . LYS A 1 172 ? -5.44700  24.70300  -7.67700  1.000 47.77474  ? 172 LYS AA NZ  1 
ATOM   1275 N  N   . VAL A 1 173 ? -0.29000  20.35500  -6.72700  1.000 13.29592  ? 173 VAL AA N   1 
ATOM   1276 C  CA  . VAL A 1 173 ? 0.97900   19.88400  -6.18700  1.000 11.39088  ? 173 VAL AA CA  1 
ATOM   1277 C  C   . VAL A 1 173 ? 1.82300   21.11500  -5.89600  1.000 10.00663  ? 173 VAL AA C   1 
ATOM   1278 O  O   . VAL A 1 173 ? 2.08600   21.91700  -6.80100  1.000 10.77613  ? 173 VAL AA O   1 
ATOM   1279 C  CB  . VAL A 1 173 ? 1.71300   18.93800  -7.15300  1.000 10.29217  ? 173 VAL AA CB  1 
ATOM   1280 C  CG1 . VAL A 1 173 ? 3.03400   18.48900  -6.54800  1.000 12.16951  ? 173 VAL AA CG1 1 
ATOM   1281 C  CG2 . VAL A 1 173 ? 0.84500   17.73700  -7.48900  1.000 6.62668   ? 173 VAL AA CG2 1 
ATOM   1282 N  N   A SER A 1 174 ? 2.23400   21.27300  -4.64200  0.305 10.08979  ? 174 SER AA N   1 
ATOM   1283 N  N   B SER A 1 174 ? 2.24500   21.26500  -4.64500  0.695 10.02639  ? 174 SER AA N   1 
ATOM   1284 C  CA  A SER A 1 174 ? 2.99800   22.43100  -4.21100  0.305 10.34248  ? 174 SER AA CA  1 
ATOM   1285 C  CA  B SER A 1 174 ? 2.99700   22.43000  -4.20800  0.695 10.28030  ? 174 SER AA CA  1 
ATOM   1286 C  C   A SER A 1 174 ? 4.32700   21.98800  -3.61600  0.305 13.47195  ? 174 SER AA C   1 
ATOM   1287 C  C   B SER A 1 174 ? 4.31700   21.99900  -3.58300  0.695 13.61430  ? 174 SER AA C   1 
ATOM   1288 O  O   A SER A 1 174 ? 4.49000   20.84400  -3.18300  0.305 14.56344  ? 174 SER AA O   1 
ATOM   1289 O  O   B SER A 1 174 ? 4.46300   20.87400  -3.09800  0.695 14.73108  ? 174 SER AA O   1 
ATOM   1290 C  CB  A SER A 1 174 ? 2.21500   23.26500  -3.18800  0.305 12.42866  ? 174 SER AA CB  1 
ATOM   1291 C  CB  B SER A 1 174 ? 2.18800   23.26600  -3.20600  0.695 12.52825  ? 174 SER AA CB  1 
ATOM   1292 O  OG  A SER A 1 174 ? 2.66100   24.60900  -3.17900  0.305 10.75582  ? 174 SER AA OG  1 
ATOM   1293 O  OG  B SER A 1 174 ? 1.03800   23.81900  -3.82200  0.695 11.70259  ? 174 SER AA OG  1 
ATOM   1294 N  N   . ALA A 1 175 ? 5.28100   22.91600  -3.59700  1.000 9.44696   ? 175 ALA AA N   1 
ATOM   1295 C  CA  . ALA A 1 175 ? 6.61200   22.64500  -3.07900  1.000 13.90620  ? 175 ALA AA CA  1 
ATOM   1296 C  C   . ALA A 1 175 ? 7.12500   23.85500  -2.31400  1.000 9.04582   ? 175 ALA AA C   1 
ATOM   1297 O  O   . ALA A 1 175 ? 6.75900   24.99600  -2.60400  1.000 10.66205  ? 175 ALA AA O   1 
ATOM   1298 C  CB  . ALA A 1 175 ? 7.59500   22.28600  -4.20400  1.000 9.00388   ? 175 ALA AA CB  1 
ATOM   1299 N  N   . MET A 1 176 ? 7.97500   23.58800  -1.32600  1.000 8.85300   ? 176 MET AA N   1 
ATOM   1300 C  CA  . MET A 1 176 ? 8.70100   24.63000  -0.61000  1.000 4.58063   ? 176 MET AA CA  1 
ATOM   1301 C  C   . MET A 1 176 ? 10.11500  24.12400  -0.38700  1.000 7.34078   ? 176 MET AA C   1 
ATOM   1302 O  O   . MET A 1 176 ? 10.30500  23.07100  0.22700   1.000 8.52365   ? 176 MET AA O   1 
ATOM   1303 C  CB  . MET A 1 176 ? 8.01900   24.98500  0.71700   1.000 6.30683   ? 176 MET AA CB  1 
ATOM   1304 C  CG  . MET A 1 176 ? 8.87100   25.82900  1.65100   1.000 10.40996  ? 176 MET AA CG  1 
ATOM   1305 S  SD  . MET A 1 176 ? 7.98000   26.32300  3.14300   1.000 12.22101  ? 176 MET AA SD  1 
ATOM   1306 C  CE  . MET A 1 176 ? 8.61700   25.12100  4.30800   1.000 17.15336  ? 176 MET AA CE  1 
ATOM   1307 N  N   . ILE A 1 177 ? 11.09800  24.86300  -0.89500  1.000 6.24530   ? 177 ILE AA N   1 
ATOM   1308 C  CA  . ILE A 1 177 ? 12.46600  24.37900  -1.03200  1.000 7.07020   ? 177 ILE AA CA  1 
ATOM   1309 C  C   . ILE A 1 177 ? 13.42700  25.38800  -0.41800  1.000 6.74362   ? 177 ILE AA C   1 
ATOM   1310 O  O   . ILE A 1 177 ? 13.27300  26.59900  -0.60600  1.000 10.62706  ? 177 ILE AA O   1 
ATOM   1311 C  CB  . ILE A 1 177 ? 12.81900  24.13300  -2.51600  1.000 6.06009   ? 177 ILE AA CB  1 
ATOM   1312 C  CG1 . ILE A 1 177 ? 11.82400  23.16000  -3.15600  1.000 6.13122   ? 177 ILE AA CG1 1 
ATOM   1313 C  CG2 . ILE A 1 177 ? 14.24100  23.62900  -2.66200  1.000 6.32903   ? 177 ILE AA CG2 1 
ATOM   1314 C  CD1 . ILE A 1 177 ? 12.02000  21.71800  -2.74200  1.000 9.47353   ? 177 ILE AA CD1 1 
ATOM   1315 N  N   . VAL A 1 178 ? 14.42100  24.88600  0.31200   1.000 8.77239   ? 178 VAL AA N   1 
ATOM   1316 C  CA  . VAL A 1 178 ? 15.53500  25.69100  0.80100   1.000 3.52824   ? 178 VAL AA CA  1 
ATOM   1317 C  C   . VAL A 1 178 ? 16.75000  25.36900  -0.05800  1.000 11.10786  ? 178 VAL AA C   1 
ATOM   1318 O  O   . VAL A 1 178 ? 17.23600  24.23200  -0.05900  1.000 7.59257   ? 178 VAL AA O   1 
ATOM   1319 C  CB  . VAL A 1 178 ? 15.82200  25.42000  2.28600   1.000 10.95959  ? 178 VAL AA CB  1 
ATOM   1320 C  CG1 . VAL A 1 178 ? 17.14000  26.06400  2.69500   1.000 3.89773   ? 178 VAL AA CG1 1 
ATOM   1321 C  CG2 . VAL A 1 178 ? 14.68100  25.93100  3.15200   1.000 6.99011   ? 178 VAL AA CG2 1 
ATOM   1322 N  N   . VAL A 1 179 ? 17.24500  26.36200  -0.78900  1.000 7.26475   ? 179 VAL AA N   1 
ATOM   1323 C  CA  . VAL A 1 179 ? 18.31200  26.15700  -1.76100  1.000 6.25670   ? 179 VAL AA CA  1 
ATOM   1324 C  C   . VAL A 1 179 ? 19.62100  26.62300  -1.13200  1.000 7.90118   ? 179 VAL AA C   1 
ATOM   1325 O  O   . VAL A 1 179 ? 19.86100  27.82600  -0.98100  1.000 9.88208   ? 179 VAL AA O   1 
ATOM   1326 C  CB  . VAL A 1 179 ? 18.02200  26.89100  -3.07600  1.000 11.17506  ? 179 VAL AA CB  1 
ATOM   1327 C  CG1 . VAL A 1 179 ? 19.23300  26.84100  -3.99500  1.000 9.62728   ? 179 VAL AA CG1 1 
ATOM   1328 C  CG2 . VAL A 1 179 ? 16.80100  26.29000  -3.75600  1.000 20.55286  ? 179 VAL AA CG2 1 
ATOM   1329 N  N   . ASN A 1 180 ? 20.46600  25.66000  -0.76000  1.000 7.50174   ? 180 ASN AA N   1 
ATOM   1330 C  CA  . ASN A 1 180 ? 21.80100  25.89000  -0.21800  1.000 5.42803   ? 180 ASN AA CA  1 
ATOM   1331 C  C   . ASN A 1 180 ? 22.81900  25.06600  -1.00200  1.000 9.74520   ? 180 ASN AA C   1 
ATOM   1332 O  O   . ASN A 1 180 ? 23.79900  24.56500  -0.44500  1.000 5.06804   ? 180 ASN AA O   1 
ATOM   1333 C  CB  . ASN A 1 180 ? 21.83600  25.55300  1.27600   1.000 4.76754   ? 180 ASN AA CB  1 
ATOM   1334 C  CG  . ASN A 1 180 ? 23.15000  25.92500  1.94500   1.000 10.38425  ? 180 ASN AA CG  1 
ATOM   1335 O  OD1 . ASN A 1 180 ? 23.50900  27.09800  2.04000   1.000 11.32585  ? 180 ASN AA OD1 1 
ATOM   1336 N  ND2 . ASN A 1 180 ? 23.86900  24.91600  2.42500   1.000 9.51485   ? 180 ASN AA ND2 1 
ATOM   1337 N  N   . SER A 1 181 ? 22.58900  24.92300  -2.30500  1.000 13.03088  ? 181 SER AA N   1 
ATOM   1338 C  CA  . SER A 1 181 ? 23.26400  23.90700  -3.09800  1.000 6.96288   ? 181 SER AA CA  1 
ATOM   1339 C  C   . SER A 1 181 ? 24.74300  24.22000  -3.29000  1.000 15.10910  ? 181 SER AA C   1 
ATOM   1340 O  O   . SER A 1 181 ? 25.15700  25.38000  -3.36500  1.000 7.46176   ? 181 SER AA O   1 
ATOM   1341 C  CB  . SER A 1 181 ? 22.59400  23.77500  -4.46400  1.000 9.38327   ? 181 SER AA CB  1 
ATOM   1342 O  OG  . SER A 1 181 ? 22.75400  24.96400  -5.21900  1.000 10.31608  ? 181 SER AA OG  1 
ATOM   1343 N  N   . PHE A 1 182 ? 25.54200  23.15400  -3.38100  1.000 12.37373  ? 182 PHE AA N   1 
ATOM   1344 C  CA  . PHE A 1 182 ? 26.94400  23.31200  -3.74800  1.000 10.08928  ? 182 PHE AA CA  1 
ATOM   1345 C  C   . PHE A 1 182 ? 27.08300  23.75900  -5.19800  1.000 13.22382  ? 182 PHE AA C   1 
ATOM   1346 O  O   . PHE A 1 182 ? 27.96300  24.56400  -5.52100  1.000 8.49431   ? 182 PHE AA O   1 
ATOM   1347 C  CB  . PHE A 1 182 ? 27.70000  22.00200  -3.51600  1.000 6.91279   ? 182 PHE AA CB  1 
ATOM   1348 C  CG  . PHE A 1 182 ? 29.08600  21.99100  -4.09900  1.000 12.85814  ? 182 PHE AA CG  1 
ATOM   1349 C  CD1 . PHE A 1 182 ? 30.15000  22.52700  -3.39000  1.000 16.49971  ? 182 PHE AA CD1 1 
ATOM   1350 C  CD2 . PHE A 1 182 ? 29.32900  21.43900  -5.34800  1.000 13.91005  ? 182 PHE AA CD2 1 
ATOM   1351 C  CE1 . PHE A 1 182 ? 31.42700  22.52300  -3.92000  1.000 17.20599  ? 182 PHE AA CE1 1 
ATOM   1352 C  CE2 . PHE A 1 182 ? 30.60600  21.43100  -5.88300  1.000 19.76441  ? 182 PHE AA CE2 1 
ATOM   1353 C  CZ  . PHE A 1 182 ? 31.65700  21.97300  -5.16700  1.000 14.79764  ? 182 PHE AA CZ  1 
ATOM   1354 N  N   . GLY A 1 183 ? 26.22700  23.24500  -6.08400  1.000 12.25009  ? 183 GLY AA N   1 
ATOM   1355 C  CA  . GLY A 1 183 ? 26.30900  23.55100  -7.49500  1.000 12.30674  ? 183 GLY AA CA  1 
ATOM   1356 C  C   . GLY A 1 183 ? 25.58200  24.83200  -7.86600  1.000 18.38272  ? 183 GLY AA C   1 
ATOM   1357 O  O   . GLY A 1 183 ? 25.02200  25.54000  -7.03000  1.000 11.51026  ? 183 GLY AA O   1 
ATOM   1358 N  N   . ASP A 1 184 ? 25.59900  25.12500  -9.16300  1.000 12.60393  ? 184 ASP AA N   1 
ATOM   1359 C  CA  . ASP A 1 184 ? 24.99100  26.33700  -9.68800  1.000 6.89315   ? 184 ASP AA CA  1 
ATOM   1360 C  C   . ASP A 1 184 ? 23.52200  26.10800  -10.01800 1.000 14.92095  ? 184 ASP AA C   1 
ATOM   1361 O  O   . ASP A 1 184 ? 23.09400  24.98800  -10.30900 1.000 11.19269  ? 184 ASP AA O   1 
ATOM   1362 C  CB  . ASP A 1 184 ? 25.72700  26.82100  -10.93800 1.000 11.20720  ? 184 ASP AA CB  1 
ATOM   1363 C  CG  . ASP A 1 184 ? 27.22800  26.88100  -10.74800 1.000 12.54015  ? 184 ASP AA CG  1 
ATOM   1364 O  OD1 . ASP A 1 184 ? 27.67700  27.16900  -9.61800  1.000 12.65359  ? 184 ASP AA OD1 1 
ATOM   1365 O  OD2 . ASP A 1 184 ? 27.95900  26.64500  -11.73200 1.000 10.97381  ? 184 ASP AA OD2 1 
ATOM   1366 N  N   . LEU A 1 185 ? 22.75600  27.19200  -9.97300  1.000 12.37755  ? 185 LEU AA N   1 
ATOM   1367 C  CA  . LEU A 1 185 ? 21.34100  27.18300  -10.31800 1.000 9.82164   ? 185 LEU AA CA  1 
ATOM   1368 C  C   . LEU A 1 185 ? 21.16500  27.76500  -11.71500 1.000 15.06017  ? 185 LEU AA C   1 
ATOM   1369 O  O   . LEU A 1 185 ? 21.75300  28.80300  -12.03800 1.000 14.97090  ? 185 LEU AA O   1 
ATOM   1370 C  CB  . LEU A 1 185 ? 20.53600  27.99000  -9.29800  1.000 7.83317   ? 185 LEU AA CB  1 
ATOM   1371 C  CG  . LEU A 1 185 ? 19.00900  27.95100  -9.36100  1.000 16.44325  ? 185 LEU AA CG  1 
ATOM   1372 C  CD1 . LEU A 1 185 ? 18.49400  26.52400  -9.31100  1.000 22.90501  ? 185 LEU AA CD1 1 
ATOM   1373 C  CD2 . LEU A 1 185 ? 18.41500  28.77900  -8.23100  1.000 27.33387  ? 185 LEU AA CD2 1 
ATOM   1374 N  N   . ARG A 1 186 ? 20.36500  27.09500  -12.54100 1.000 8.22909   ? 186 ARG AA N   1 
ATOM   1375 C  CA  . ARG A 1 186 ? 20.07800  27.54000  -13.89600 1.000 14.10378  ? 186 ARG AA CA  1 
ATOM   1376 C  C   . ARG A 1 186 ? 18.57400  27.66100  -14.09800 1.000 19.58207  ? 186 ARG AA C   1 
ATOM   1377 O  O   . ARG A 1 186 ? 17.78600  26.98100  -13.43300 1.000 16.88322  ? 186 ARG AA O   1 
ATOM   1378 C  CB  . ARG A 1 186 ? 20.65400  26.57400  -14.93900 1.000 11.11412  ? 186 ARG AA CB  1 
ATOM   1379 C  CG  . ARG A 1 186 ? 22.08300  26.86700  -15.36000 1.000 17.88174  ? 186 ARG AA CG  1 
ATOM   1380 C  CD  . ARG A 1 186 ? 22.73700  25.61800  -15.92700 1.000 19.72900  ? 186 ARG AA CD  1 
ATOM   1381 N  NE  . ARG A 1 186 ? 24.06200  25.87800  -16.47500 1.000 24.51404  ? 186 ARG AA NE  1 
ATOM   1382 C  CZ  . ARG A 1 186 ? 25.19100  25.44100  -15.93500 1.000 50.44701  ? 186 ARG AA CZ  1 
ATOM   1383 N  NH1 . ARG A 1 186 ? 25.19700  24.75300  -14.80400 1.000 16.91736  ? 186 ARG AA NH1 1 
ATOM   1384 N  NH2 . ARG A 1 186 ? 26.34500  25.70300  -16.54300 1.000 39.91584  ? 186 ARG AA NH2 1 
ATOM   1385 N  N   . ASP A 1 187 ? 18.17700  28.52900  -15.02700 1.000 16.90371  ? 187 ASP AA N   1 
ATOM   1386 C  CA  . ASP A 1 187 ? 16.76800  28.68700  -15.35500 1.000 18.59207  ? 187 ASP AA CA  1 
ATOM   1387 C  C   . ASP A 1 187 ? 16.38500  27.69500  -16.45500 1.000 27.78429  ? 187 ASP AA C   1 
ATOM   1388 O  O   . ASP A 1 187 ? 17.17300  26.82800  -16.84400 1.000 18.41365  ? 187 ASP AA O   1 
ATOM   1389 C  CB  . ASP A 1 187 ? 16.45900  30.13600  -15.73700 1.000 14.78150  ? 187 ASP AA CB  1 
ATOM   1390 C  CG  . ASP A 1 187 ? 17.28400  30.63600  -16.91700 1.000 31.43141  ? 187 ASP AA CG  1 
ATOM   1391 O  OD1 . ASP A 1 187 ? 17.89400  29.81900  -17.63900 1.000 24.73926  ? 187 ASP AA OD1 1 
ATOM   1392 O  OD2 . ASP A 1 187 ? 17.31200  31.86600  -17.12500 1.000 16.05221  ? 187 ASP AA OD2 1 
ATOM   1393 N  N   . THR A 1 188 ? 15.16400  27.82800  -16.98100 1.000 34.59414  ? 188 THR AA N   1 
ATOM   1394 C  CA  . THR A 1 188 ? 14.63700  26.84900  -17.92600 1.000 35.58581  ? 188 THR AA CA  1 
ATOM   1395 C  C   . THR A 1 188 ? 15.36200  26.86300  -19.26600 1.000 37.35356  ? 188 THR AA C   1 
ATOM   1396 O  O   . THR A 1 188 ? 15.23500  25.90000  -20.03000 1.000 47.02205  ? 188 THR AA O   1 
ATOM   1397 C  CB  . THR A 1 188 ? 13.14200  27.08600  -18.14800 1.000 25.54644  ? 188 THR AA CB  1 
ATOM   1398 O  OG1 . THR A 1 188 ? 12.90500  28.48400  -18.35300 1.000 36.16734  ? 188 THR AA OG1 1 
ATOM   1399 C  CG2 . THR A 1 188 ? 12.34600  26.61500  -16.94000 1.000 32.34044  ? 188 THR AA CG2 1 
ATOM   1400 N  N   . ALA A 1 189 ? 16.11100  27.92000  -19.57300 1.000 36.51544  ? 189 ALA AA N   1 
ATOM   1401 C  CA  . ALA A 1 189 ? 16.85300  28.00000  -20.82300 1.000 44.26272  ? 189 ALA AA CA  1 
ATOM   1402 C  C   . ALA A 1 189 ? 18.33500  27.69700  -20.65800 1.000 49.46378  ? 189 ALA AA C   1 
ATOM   1403 O  O   . ALA A 1 189 ? 19.06300  27.67100  -21.65600 1.000 48.48788  ? 189 ALA AA O   1 
ATOM   1404 C  CB  . ALA A 1 189 ? 16.67800  29.38200  -21.45700 1.000 29.77922  ? 189 ALA AA CB  1 
ATOM   1405 N  N   . GLY A 1 190 ? 18.80000  27.47200  -19.43400 1.000 42.62446  ? 190 GLY AA N   1 
ATOM   1406 C  CA  . GLY A 1 190 ? 20.18300  27.12200  -19.19500 1.000 19.06452  ? 190 GLY AA CA  1 
ATOM   1407 C  C   . GLY A 1 190 ? 21.09100  28.25700  -18.78400 1.000 21.75528  ? 190 GLY AA C   1 
ATOM   1408 O  O   . GLY A 1 190 ? 22.30600  28.04400  -18.68800 1.000 32.98251  ? 190 GLY AA O   1 
ATOM   1409 N  N   . ARG A 1 191 ? 20.55600  29.45300  -18.54500 1.000 22.80314  ? 191 ARG AA N   1 
ATOM   1410 C  CA  . ARG A 1 191 ? 21.38600  30.54400  -18.05700 1.000 21.89372  ? 191 ARG AA CA  1 
ATOM   1411 C  C   . ARG A 1 191 ? 21.70800  30.33800  -16.58200 1.000 19.87754  ? 191 ARG AA C   1 
ATOM   1412 O  O   . ARG A 1 191 ? 20.84100  29.96900  -15.78600 1.000 20.67008  ? 191 ARG AA O   1 
ATOM   1413 C  CB  . ARG A 1 191 ? 20.69000  31.89300  -18.23900 1.000 17.65583  ? 191 ARG AA CB  1 
ATOM   1414 C  CG  . ARG A 1 191 ? 20.20200  32.19200  -19.64300 1.000 37.85366  ? 191 ARG AA CG  1 
ATOM   1415 C  CD  . ARG A 1 191 ? 18.93800  33.03900  -19.59100 1.000 32.06305  ? 191 ARG AA CD  1 
ATOM   1416 N  NE  . ARG A 1 191 ? 18.38300  33.30500  -20.91200 1.000 85.74847  ? 191 ARG AA NE  1 
ATOM   1417 C  CZ  . ARG A 1 191 ? 17.15300  32.98200  -21.28600 1.000 79.84390  ? 191 ARG AA CZ  1 
ATOM   1418 N  NH1 . ARG A 1 191 ? 16.30400  32.40900  -20.44800 1.000 72.97496  ? 191 ARG AA NH1 1 
ATOM   1419 N  NH2 . ARG A 1 191 ? 16.76000  33.25000  -22.52800 1.000 62.95053  ? 191 ARG AA NH2 1 
ATOM   1420 N  N   . ILE A 1 192 ? 22.96400  30.58200  -16.21600 1.000 23.98053  ? 192 ILE AA N   1 
ATOM   1421 C  CA  . ILE A 1 192 ? 23.34500  30.55700  -14.80900 1.000 19.25408  ? 192 ILE AA CA  1 
ATOM   1422 C  C   . ILE A 1 192 ? 22.79000  31.80500  -14.13600 1.000 17.53731  ? 192 ILE AA C   1 
ATOM   1423 O  O   . ILE A 1 192 ? 23.11200  32.93300  -14.52600 1.000 19.62297  ? 192 ILE AA O   1 
ATOM   1424 C  CB  . ILE A 1 192 ? 24.86800  30.47200  -14.65000 1.000 11.75018  ? 192 ILE AA CB  1 
ATOM   1425 C  CG1 . ILE A 1 192 ? 25.40400  29.17500  -15.25900 1.000 20.40288  ? 192 ILE AA CG1 1 
ATOM   1426 C  CG2 . ILE A 1 192 ? 25.25200  30.56100  -13.18100 1.000 14.17986  ? 192 ILE AA CG2 1 
ATOM   1427 C  CD1 . ILE A 1 192 ? 26.91000  29.03400  -15.15900 1.000 15.49969  ? 192 ILE AA CD1 1 
ATOM   1428 N  N   . VAL A 1 193 ? 21.94300  31.61000  -13.12700 1.000 15.69998  ? 193 VAL AA N   1 
ATOM   1429 C  CA  . VAL A 1 193 ? 21.39000  32.72300  -12.36700 1.000 10.48901  ? 193 VAL AA CA  1 
ATOM   1430 C  C   . VAL A 1 193 ? 22.00900  32.84700  -10.97900 1.000 13.05915  ? 193 VAL AA C   1 
ATOM   1431 O  O   . VAL A 1 193 ? 21.94100  33.93500  -10.38600 1.000 14.33560  ? 193 VAL AA O   1 
ATOM   1432 C  CB  . VAL A 1 193 ? 19.85300  32.62400  -12.25900 1.000 19.15568  ? 193 VAL AA CB  1 
ATOM   1433 C  CG1 . VAL A 1 193 ? 19.22700  32.52700  -13.64400 1.000 22.91737  ? 193 VAL AA CG1 1 
ATOM   1434 C  CG2 . VAL A 1 193 ? 19.44900  31.43900  -11.40100 1.000 17.07433  ? 193 VAL AA CG2 1 
ATOM   1435 N  N   . ALA A 1 194 ? 22.60900  31.78600  -10.44700 1.000 12.35199  ? 194 ALA AA N   1 
ATOM   1436 C  CA  . ALA A 1 194 ? 23.28200  31.83900  -9.15900  1.000 16.23560  ? 194 ALA AA CA  1 
ATOM   1437 C  C   . ALA A 1 194 ? 24.28600  30.70000  -9.10000  1.000 10.01214  ? 194 ALA AA C   1 
ATOM   1438 O  O   . ALA A 1 194 ? 24.00000  29.59500  -9.56800  1.000 12.02429  ? 194 ALA AA O   1 
ATOM   1439 C  CB  . ALA A 1 194 ? 22.28700  31.73800  -7.99600  1.000 9.18180   ? 194 ALA AA CB  1 
ATOM   1440 N  N   . GLY A 1 195 ? 25.45500  30.97300  -8.53300  1.000 7.70596   ? 195 GLY AA N   1 
ATOM   1441 C  CA  . GLY A 1 195 ? 26.47600  29.95200  -8.42600  1.000 15.87640  ? 195 GLY AA CA  1 
ATOM   1442 C  C   . GLY A 1 195 ? 27.81600  30.55700  -8.05600  1.000 11.21332  ? 195 GLY AA C   1 
ATOM   1443 O  O   . GLY A 1 195 ? 27.91600  31.73700  -7.71200  1.000 12.40923  ? 195 GLY AA O   1 
ATOM   1444 N  N   . ALA A 1 196 ? 28.84400  29.71300  -8.12900  1.000 8.74566   ? 196 ALA AA N   1 
ATOM   1445 C  CA  . ALA A 1 196 ? 30.19800  30.15500  -7.82600  1.000 12.23898  ? 196 ALA AA CA  1 
ATOM   1446 C  C   . ALA A 1 196 ? 30.65800  31.19600  -8.83800  1.000 17.58933  ? 196 ALA AA C   1 
ATOM   1447 O  O   . ALA A 1 196 ? 30.37700  31.09300  -10.03500 1.000 17.87674  ? 196 ALA AA O   1 
ATOM   1448 C  CB  . ALA A 1 196 ? 31.15600  28.96300  -7.82400  1.000 5.42876   ? 196 ALA AA CB  1 
ATOM   1449 N  N   A LYS A 1 197 ? 31.37700  32.20100  -8.34500  0.600 17.26515  ? 197 LYS AA N   1 
ATOM   1450 N  N   B LYS A 1 197 ? 31.36900  32.20900  -8.35200  0.400 17.28188  ? 197 LYS AA N   1 
ATOM   1451 C  CA  A LYS A 1 197 ? 31.87600  33.29500  -9.16200  0.600 22.22775  ? 197 LYS AA CA  1 
ATOM   1452 C  CA  B LYS A 1 197 ? 31.86700  33.28000  -9.19900  0.400 22.15648  ? 197 LYS AA CA  1 
ATOM   1453 C  C   A LYS A 1 197 ? 33.39600  33.34900  -9.09200  0.600 23.59794  ? 197 LYS AA C   1 
ATOM   1454 C  C   B LYS A 1 197 ? 33.38200  33.37900  -9.08500  0.400 23.54400  ? 197 LYS AA C   1 
ATOM   1455 O  O   A LYS A 1 197 ? 34.00700  32.89900  -8.11800  0.600 18.27764  ? 197 LYS AA O   1 
ATOM   1456 O  O   B LYS A 1 197 ? 33.97500  32.98300  -8.07700  0.400 18.34636  ? 197 LYS AA O   1 
ATOM   1457 C  CB  A LYS A 1 197 ? 31.29000  34.63900  -8.71000  0.600 18.77409  ? 197 LYS AA CB  1 
ATOM   1458 C  CB  B LYS A 1 197 ? 31.22600  34.62800  -8.83800  0.400 18.95828  ? 197 LYS AA CB  1 
ATOM   1459 C  CG  A LYS A 1 197 ? 29.79300  34.77200  -8.93100  0.600 15.97715  ? 197 LYS AA CG  1 
ATOM   1460 C  CG  B LYS A 1 197 ? 31.47400  35.08600  -7.41000  0.400 18.28647  ? 197 LYS AA CG  1 
ATOM   1461 C  CD  A LYS A 1 197 ? 29.07600  35.14800  -7.64600  0.600 23.07113  ? 197 LYS AA CD  1 
ATOM   1462 C  CD  B LYS A 1 197 ? 30.33300  35.95300  -6.88900  0.400 15.49913  ? 197 LYS AA CD  1 
ATOM   1463 C  CE  A LYS A 1 197 ? 28.93800  36.65600  -7.51200  0.600 28.56322  ? 197 LYS AA CE  1 
ATOM   1464 C  CE  B LYS A 1 197 ? 29.00000  35.58100  -7.52600  0.400 23.19644  ? 197 LYS AA CE  1 
ATOM   1465 N  NZ  A LYS A 1 197 ? 29.01900  37.09800  -6.09100  0.600 24.47758  ? 197 LYS AA NZ  1 
ATOM   1466 N  NZ  B LYS A 1 197 ? 27.92200  36.54800  -7.17600  0.400 22.30018  ? 197 LYS AA NZ  1 
ATOM   1467 N  N   . TYR A 1 198 ? 34.00100  33.91100  -10.13500 1.000 32.18011  ? 198 TYR AA N   1 
ATOM   1468 C  CA  . TYR A 1 198 ? 35.44500  34.07000  -10.17200 1.000 26.10982  ? 198 TYR AA CA  1 
ATOM   1469 C  C   . TYR A 1 198 ? 35.89100  35.11200  -9.14600  1.000 31.59251  ? 198 TYR AA C   1 
ATOM   1470 O  O   . TYR A 1 198 ? 35.07900  35.81600  -8.53700  1.000 38.51250  ? 198 TYR AA O   1 
ATOM   1471 C  CB  . TYR A 1 198 ? 35.90100  34.47100  -11.57500 1.000 24.58529  ? 198 TYR AA CB  1 
ATOM   1472 C  CG  . TYR A 1 198 ? 36.08200  33.30500  -12.52300 1.000 25.80277  ? 198 TYR AA CG  1 
ATOM   1473 C  CD1 . TYR A 1 198 ? 36.89900  32.23300  -12.19200 1.000 19.69312  ? 198 TYR AA CD1 1 
ATOM   1474 C  CD2 . TYR A 1 198 ? 35.43800  33.28100  -13.75400 1.000 28.95051  ? 198 TYR AA CD2 1 
ATOM   1475 C  CE1 . TYR A 1 198 ? 37.06900  31.16800  -13.05800 1.000 24.22143  ? 198 TYR AA CE1 1 
ATOM   1476 C  CE2 . TYR A 1 198 ? 35.60000  32.22100  -14.62600 1.000 24.02358  ? 198 TYR AA CE2 1 
ATOM   1477 C  CZ  . TYR A 1 198 ? 36.41700  31.16800  -14.27300 1.000 27.01779  ? 198 TYR AA CZ  1 
ATOM   1478 O  OH  . TYR A 1 198 ? 36.58100  30.11000  -15.13800 1.000 29.68111  ? 198 TYR AA OH  1 
ATOM   1479 N  N   . GLU A 1 199 ? 37.21200  35.20500  -8.96300  1.000 37.02306  ? 199 GLU AA N   1 
ATOM   1480 C  CA  . GLU A 1 199 ? 37.76600  36.10300  -7.95200  1.000 53.91323  ? 199 GLU AA CA  1 
ATOM   1481 C  C   . GLU A 1 199 ? 37.31000  37.54000  -8.17200  1.000 51.78532  ? 199 GLU AA C   1 
ATOM   1482 O  O   . GLU A 1 199 ? 37.04200  38.26900  -7.21000  1.000 83.00511  ? 199 GLU AA O   1 
ATOM   1483 C  CB  . GLU A 1 199 ? 39.29200  36.01900  -7.95800  1.000 38.12001  ? 199 GLU AA CB  1 
ATOM   1484 C  CG  . GLU A 1 199 ? 39.83100  34.60000  -7.89500  1.000 84.84506  ? 199 GLU AA CG  1 
ATOM   1485 C  CD  . GLU A 1 199 ? 41.31500  34.55400  -7.59500  1.000 110.73479 ? 199 GLU AA CD  1 
ATOM   1486 O  OE1 . GLU A 1 199 ? 42.04900  35.44100  -8.07900  1.000 101.50921 ? 199 GLU AA OE1 1 
ATOM   1487 O  OE2 . GLU A 1 199 ? 41.74900  33.62900  -6.87600  1.000 119.43934 ? 199 GLU AA OE2 1 
ATOM   1488 N  N   . GLY A 1 200 ? 37.21300  37.96100  -9.42800  1.000 36.01975  ? 200 GLY AA N   1 
ATOM   1489 C  CA  . GLY A 1 200 ? 36.71900  39.28500  -9.74400  1.000 57.05262  ? 200 GLY AA CA  1 
ATOM   1490 C  C   . GLY A 1 200 ? 36.01200  39.32500  -11.08100 1.000 68.58629  ? 200 GLY AA C   1 
ATOM   1491 O  O   . GLY A 1 200 ? 36.45600  40.01500  -12.00400 1.000 43.66133  ? 200 GLY AA O   1 
ATOM   1492 N  N   . GLY A 1 201 ? 34.91300  38.58500  -11.20400 1.000 36.57090  ? 201 GLY AA N   1 
ATOM   1493 C  CA  . GLY A 1 201 ? 34.20000  38.55300  -12.46300 1.000 60.14963  ? 201 GLY AA CA  1 
ATOM   1494 C  C   . GLY A 1 201 ? 32.91300  37.75500  -12.48000 1.000 39.16452  ? 201 GLY AA C   1 
ATOM   1495 O  O   . GLY A 1 201 ? 32.12300  37.79400  -11.53100 1.000 20.01620  ? 201 GLY AA O   1 
ATOM   1496 N  N   . GLU A 1 202 ? 32.70400  37.01600  -13.56600 1.000 32.86962  ? 202 GLU AA N   1 
ATOM   1497 C  CA  . GLU A 1 202 ? 31.42400  36.39900  -13.86700 1.000 38.35674  ? 202 GLU AA CA  1 
ATOM   1498 C  C   . GLU A 1 202 ? 31.28400  35.04400  -13.17500 1.000 27.79702  ? 202 GLU AA C   1 
ATOM   1499 O  O   . GLU A 1 202 ? 32.14200  34.61200  -12.40000 1.000 16.92882  ? 202 GLU AA O   1 
ATOM   1500 C  CB  . GLU A 1 202 ? 31.26400  36.25800  -15.38000 1.000 36.25094  ? 202 GLU AA CB  1 
ATOM   1501 C  CG  . GLU A 1 202 ? 31.79700  37.44500  -16.16000 1.000 32.90977  ? 202 GLU AA CG  1 
ATOM   1502 C  CD  . GLU A 1 202 ? 30.96500  38.69200  -15.95000 1.000 27.96405  ? 202 GLU AA CD  1 
ATOM   1503 O  OE1 . GLU A 1 202 ? 29.72100  38.57900  -15.93200 1.000 40.06572  ? 202 GLU AA OE1 1 
ATOM   1504 O  OE2 . GLU A 1 202 ? 31.55300  39.78400  -15.79700 1.000 36.96973  ? 202 GLU AA OE2 1 
ATOM   1505 N  N   . PHE A 1 203 ? 30.17200  34.36800  -13.45500 1.000 20.78653  ? 203 PHE AA N   1 
ATOM   1506 C  CA  . PHE A 1 203 ? 29.98400  33.00800  -12.97700 1.000 11.57347  ? 203 PHE AA CA  1 
ATOM   1507 C  C   . PHE A 1 203 ? 31.04100  32.09300  -13.58100 1.000 16.40775  ? 203 PHE AA C   1 
ATOM   1508 O  O   . PHE A 1 203 ? 31.37300  32.19500  -14.76500 1.000 15.50012  ? 203 PHE AA O   1 
ATOM   1509 C  CB  . PHE A 1 203 ? 28.58300  32.51000  -13.33000 1.000 13.87336  ? 203 PHE AA CB  1 
ATOM   1510 C  CG  . PHE A 1 203 ? 27.48700  33.17600  -12.54800 1.000 16.32043  ? 203 PHE AA CG  1 
ATOM   1511 C  CD1 . PHE A 1 203 ? 27.46400  33.10400  -11.16400 1.000 17.36836  ? 203 PHE AA CD1 1 
ATOM   1512 C  CD2 . PHE A 1 203 ? 26.47900  33.87400  -13.19400 1.000 8.36076   ? 203 PHE AA CD2 1 
ATOM   1513 C  CE1 . PHE A 1 203 ? 26.45400  33.71400  -10.43800 1.000 15.79943  ? 203 PHE AA CE1 1 
ATOM   1514 C  CE2 . PHE A 1 203 ? 25.46800  34.48600  -12.47500 1.000 12.95522  ? 203 PHE AA CE2 1 
ATOM   1515 C  CZ  . PHE A 1 203 ? 25.45700  34.40600  -11.09500 1.000 11.24086  ? 203 PHE AA CZ  1 
ATOM   1516 N  N   . ALA A 1 204 ? 31.57600  31.19600  -12.75400 1.000 9.44894   ? 204 ALA AA N   1 
ATOM   1517 C  CA  . ALA A 1 204 ? 32.67800  30.35000  -13.18900 1.000 11.42617  ? 204 ALA AA CA  1 
ATOM   1518 C  C   . ALA A 1 204 ? 32.21700  29.08200  -13.89200 1.000 11.52453  ? 204 ALA AA C   1 
ATOM   1519 O  O   . ALA A 1 204 ? 33.04000  28.42600  -14.54000 1.000 17.40285  ? 204 ALA AA O   1 
ATOM   1520 C  CB  . ALA A 1 204 ? 33.55500  29.97600  -11.99200 1.000 16.11570  ? 204 ALA AA CB  1 
ATOM   1521 N  N   . ASP A 1 205 ? 30.92900  28.73800  -13.79300 1.000 13.77164  ? 205 ASP AA N   1 
ATOM   1522 C  CA  . ASP A 1 205 ? 30.40700  27.44500  -14.23000 1.000 12.33977  ? 205 ASP AA CA  1 
ATOM   1523 C  C   . ASP A 1 205 ? 31.08200  26.33400  -13.43600 1.000 9.13141   ? 205 ASP AA C   1 
ATOM   1524 O  O   . ASP A 1 205 ? 32.14100  25.83400  -13.83100 1.000 10.66626  ? 205 ASP AA O   1 
ATOM   1525 C  CB  . ASP A 1 205 ? 30.60100  27.24500  -15.73900 1.000 10.85375  ? 205 ASP AA CB  1 
ATOM   1526 C  CG  . ASP A 1 205 ? 29.77700  26.09200  -16.29100 1.000 15.80599  ? 205 ASP AA CG  1 
ATOM   1527 O  OD1 . ASP A 1 205 ? 29.30100  25.25000  -15.50000 1.000 13.81606  ? 205 ASP AA OD1 1 
ATOM   1528 O  OD2 . ASP A 1 205 ? 29.60300  26.02800  -17.52500 1.000 13.89091  ? 205 ASP AA OD2 1 
ATOM   1529 N  N   . THR A 1 206 ? 30.46300  25.94500  -12.31700 1.000 7.00162   ? 206 THR AA N   1 
ATOM   1530 C  CA  . THR A 1 206 ? 31.08400  24.99600  -11.39500 1.000 7.09396   ? 206 THR AA CA  1 
ATOM   1531 C  C   . THR A 1 206 ? 31.43800  23.68800  -12.09400 1.000 8.34962   ? 206 THR AA C   1 
ATOM   1532 O  O   . THR A 1 206 ? 32.56100  23.18700  -11.96500 1.000 10.97381  ? 206 THR AA O   1 
ATOM   1533 C  CB  . THR A 1 206 ? 30.15300  24.73300  -10.20900 1.000 9.58744   ? 206 THR AA CB  1 
ATOM   1534 O  OG1 . THR A 1 206 ? 30.03800  25.91700  -9.41000  1.000 7.80729   ? 206 THR AA OG1 1 
ATOM   1535 C  CG2 . THR A 1 206 ? 30.68800  23.59800  -9.34800  1.000 8.60581   ? 206 THR AA CG2 1 
ATOM   1536 N  N   . TYR A 1 207 ? 30.49200  23.12400  -12.84600 1.000 7.38345   ? 207 TYR AA N   1 
ATOM   1537 C  CA  . TYR A 1 207 ? 30.72400  21.83100  -13.48300 1.000 6.56939   ? 207 TYR AA CA  1 
ATOM   1538 C  C   . TYR A 1 207 ? 31.87800  21.90100  -14.47600 1.000 7.70566   ? 207 TYR AA C   1 
ATOM   1539 O  O   . TYR A 1 207 ? 32.74800  21.02100  -14.49700 1.000 11.01178  ? 207 TYR AA O   1 
ATOM   1540 C  CB  . TYR A 1 207 ? 29.44600  21.34800  -14.16900 1.000 14.34922  ? 207 TYR AA CB  1 
ATOM   1541 C  CG  . TYR A 1 207 ? 29.60300  20.03100  -14.89700 1.000 18.55764  ? 207 TYR AA CG  1 
ATOM   1542 C  CD1 . TYR A 1 207 ? 30.31800  18.98200  -14.33100 1.000 9.79146   ? 207 TYR AA CD1 1 
ATOM   1543 C  CD2 . TYR A 1 207 ? 29.03200  19.83600  -16.14700 1.000 15.53902  ? 207 TYR AA CD2 1 
ATOM   1544 C  CE1 . TYR A 1 207 ? 30.46600  17.77800  -14.99500 1.000 12.14752  ? 207 TYR AA CE1 1 
ATOM   1545 C  CE2 . TYR A 1 207 ? 29.17200  18.63600  -16.81700 1.000 17.02585  ? 207 TYR AA CE2 1 
ATOM   1546 C  CZ  . TYR A 1 207 ? 29.88800  17.61100  -16.23600 1.000 20.33385  ? 207 TYR AA CZ  1 
ATOM   1547 O  OH  . TYR A 1 207 ? 30.02900  16.41800  -16.90200 1.000 12.95502  ? 207 TYR AA OH  1 
ATOM   1548 N  N   . ALA A 1 208 ? 31.90400  22.94300  -15.31100 1.000 12.65500  ? 208 ALA AA N   1 
ATOM   1549 C  CA  . ALA A 1 208 ? 32.99300  23.08700  -16.27100 1.000 10.99037  ? 208 ALA AA CA  1 
ATOM   1550 C  C   . ALA A 1 208 ? 34.33800  23.24800  -15.57500 1.000 10.16765  ? 208 ALA AA C   1 
ATOM   1551 O  O   . ALA A 1 208 ? 35.35400  22.74900  -16.07000 1.000 12.34114  ? 208 ALA AA O   1 
ATOM   1552 C  CB  . ALA A 1 208 ? 32.72500  24.27300  -17.19800 1.000 12.28541  ? 208 ALA AA CB  1 
ATOM   1553 N  N   . ARG A 1 209 ? 34.36500  23.92300  -14.42300 1.000 11.48405  ? 209 ARG AA N   1 
ATOM   1554 C  CA  . ARG A 1 209 ? 35.62600  24.11200  -13.71200 1.000 11.90106  ? 209 ARG AA CA  1 
ATOM   1555 C  C   . ARG A 1 209 ? 36.13900  22.80100  -13.12700 1.000 22.42582  ? 209 ARG AA C   1 
ATOM   1556 O  O   . ARG A 1 209 ? 37.33800  22.50700  -13.21500 1.000 16.63697  ? 209 ARG AA O   1 
ATOM   1557 C  CB  . ARG A 1 209 ? 35.46400  25.16300  -12.61400 1.000 13.99667  ? 209 ARG AA CB  1 
ATOM   1558 C  CG  . ARG A 1 209 ? 35.27300  26.58500  -13.12800 1.000 14.69045  ? 209 ARG AA CG  1 
ATOM   1559 C  CD  . ARG A 1 209 ? 36.25700  26.93000  -14.24300 1.000 18.46614  ? 209 ARG AA CD  1 
ATOM   1560 N  NE  . ARG A 1 209 ? 37.64400  26.72700  -13.84100 1.000 24.55155  ? 209 ARG AA NE  1 
ATOM   1561 C  CZ  . ARG A 1 209 ? 38.69600  27.03200  -14.58900 1.000 38.35199  ? 209 ARG AA CZ  1 
ATOM   1562 N  NH1 . ARG A 1 209 ? 38.55700  27.57200  -15.78900 1.000 28.16748  ? 209 ARG AA NH1 1 
ATOM   1563 N  NH2 . ARG A 1 209 ? 39.91700  26.78900  -14.12200 1.000 29.26474  ? 209 ARG AA NH2 1 
ATOM   1564 N  N   . MET A 1 210 ? 35.25600  21.99800  -12.52500 1.000 8.44027   ? 210 MET AA N   1 
ATOM   1565 C  CA  . MET A 1 210 ? 35.70600  20.71900  -11.98100 1.000 24.09893  ? 210 MET AA CA  1 
ATOM   1566 C  C   . MET A 1 210 ? 36.12800  19.75200  -13.07900 1.000 7.30631   ? 210 MET AA C   1 
ATOM   1567 O  O   . MET A 1 210 ? 36.98800  18.89600  -12.84600 1.000 15.56686  ? 210 MET AA O   1 
ATOM   1568 C  CB  . MET A 1 210 ? 34.62600  20.08900  -11.09600 1.000 12.59991  ? 210 MET AA CB  1 
ATOM   1569 C  CG  . MET A 1 210 ? 33.98400  21.04800  -10.10400 1.000 14.80894  ? 210 MET AA CG  1 
ATOM   1570 S  SD  . MET A 1 210 ? 32.51400  20.37900  -9.29700  1.000 21.67213  ? 210 MET AA SD  1 
ATOM   1571 C  CE  . MET A 1 210 ? 32.88400  18.62800  -9.28700  1.000 25.32272  ? 210 MET AA CE  1 
ATOM   1572 N  N   . LYS A 1 211 ? 35.54400  19.86900  -14.27400 1.000 10.83142  ? 211 LYS AA N   1 
ATOM   1573 C  CA  . LYS A 1 211 ? 36.03000  19.08000  -15.40200 1.000 18.23563  ? 211 LYS AA CA  1 
ATOM   1574 C  C   . LYS A 1 211 ? 37.45700  19.46000  -15.77000 1.000 19.05596  ? 211 LYS AA C   1 
ATOM   1575 O  O   . LYS A 1 211 ? 38.23400  18.60600  -16.21200 1.000 23.87758  ? 211 LYS AA O   1 
ATOM   1576 C  CB  . LYS A 1 211 ? 35.11200  19.25800  -16.61200 1.000 16.35807  ? 211 LYS AA CB  1 
ATOM   1577 C  CG  . LYS A 1 211 ? 33.86800  18.38700  -16.59200 1.000 21.94594  ? 211 LYS AA CG  1 
ATOM   1578 C  CD  . LYS A 1 211 ? 32.76000  19.00500  -17.42700 1.000 25.61788  ? 211 LYS AA CD  1 
ATOM   1579 C  CE  . LYS A 1 211 ? 32.89000  18.62600  -18.89000 1.000 29.66017  ? 211 LYS AA CE  1 
ATOM   1580 N  NZ  . LYS A 1 211 ? 31.59000  18.73100  -19.60700 1.000 19.21985  ? 211 LYS AA NZ  1 
ATOM   1581 N  N   . LEU A 1 212 ? 37.81900  20.73300  -15.59800 1.000 17.35919  ? 212 LEU AA N   1 
ATOM   1582 C  CA  . LEU A 1 212 ? 39.17400  21.19300  -15.87300 1.000 25.64791  ? 212 LEU AA CA  1 
ATOM   1583 C  C   . LEU A 1 212 ? 40.15000  20.86900  -14.75000 1.000 21.15228  ? 212 LEU AA C   1 
ATOM   1584 O  O   . LEU A 1 212 ? 41.36100  21.01100  -14.94600 1.000 29.93433  ? 212 LEU AA O   1 
ATOM   1585 C  CB  . LEU A 1 212 ? 39.18200  22.70400  -16.14000 1.000 14.98019  ? 212 LEU AA CB  1 
ATOM   1586 C  CG  . LEU A 1 212 ? 38.89400  23.22600  -17.55400 1.000 33.94941  ? 212 LEU AA CG  1 
ATOM   1587 C  CD1 . LEU A 1 212 ? 40.12500  23.06600  -18.43200 1.000 42.54858  ? 212 LEU AA CD1 1 
ATOM   1588 C  CD2 . LEU A 1 212 ? 37.69900  22.54600  -18.20000 1.000 32.41050  ? 212 LEU AA CD2 1 
ATOM   1589 N  N   . GLY A 1 213 ? 39.66200  20.44100  -13.58700 1.000 19.79726  ? 213 GLY AA N   1 
ATOM   1590 C  CA  . GLY A 1 213 ? 40.52000  20.02800  -12.49500 1.000 13.81601  ? 213 GLY AA CA  1 
ATOM   1591 C  C   . GLY A 1 213 ? 40.45400  20.89000  -11.25300 1.000 19.39125  ? 213 GLY AA C   1 
ATOM   1592 O  O   . GLY A 1 213 ? 41.20600  20.63000  -10.30700 1.000 22.67524  ? 213 GLY AA O   1 
ATOM   1593 N  N   . ASP A 1 214 ? 39.59200  21.90600  -11.22000 1.000 13.30766  ? 214 ASP AA N   1 
ATOM   1594 C  CA  . ASP A 1 214 ? 39.44900  22.72600  -10.02300 1.000 22.19036  ? 214 ASP AA CA  1 
ATOM   1595 C  C   . ASP A 1 214 ? 38.94100  21.87700  -8.86300  1.000 25.21965  ? 214 ASP AA C   1 
ATOM   1596 O  O   . ASP A 1 214 ? 37.98300  21.11300  -9.01000  1.000 27.58667  ? 214 ASP AA O   1 
ATOM   1597 C  CB  . ASP A 1 214 ? 38.49500  23.89300  -10.28800 1.000 17.13832  ? 214 ASP AA CB  1 
ATOM   1598 C  CG  . ASP A 1 214 ? 39.14300  25.01000  -11.08800 1.000 26.91691  ? 214 ASP AA CG  1 
ATOM   1599 O  OD1 . ASP A 1 214 ? 40.18800  24.76200  -11.72500 1.000 25.91768  ? 214 ASP AA OD1 1 
ATOM   1600 O  OD2 . ASP A 1 214 ? 38.60800  26.14000  -11.07600 1.000 21.22495  ? 214 ASP AA OD2 1 
ATOM   1601 N  N   . LYS A 1 215 ? 39.58700  22.01300  -7.70900  1.000 29.72479  ? 215 LYS AA N   1 
ATOM   1602 C  CA  . LYS A 1 215 ? 39.27800  21.19000  -6.55000  1.000 29.92765  ? 215 LYS AA CA  1 
ATOM   1603 C  C   . LYS A 1 215 ? 38.26000  21.87200  -5.64400  1.000 29.81084  ? 215 LYS AA C   1 
ATOM   1604 O  O   . LYS A 1 215 ? 38.24200  23.09800  -5.50200  1.000 29.75396  ? 215 LYS AA O   1 
ATOM   1605 C  CB  . LYS A 1 215 ? 40.54800  20.87500  -5.75800  1.000 45.41601  ? 215 LYS AA CB  1 
ATOM   1606 C  CG  . LYS A 1 215 ? 41.07000  19.45700  -5.95500  1.000 56.76136  ? 215 LYS AA CG  1 
ATOM   1607 C  CD  . LYS A 1 215 ? 41.26500  19.13600  -7.42900  1.000 36.25208  ? 215 LYS AA CD  1 
ATOM   1608 C  CE  . LYS A 1 215 ? 40.79100  17.72900  -7.76000  1.000 53.64930  ? 215 LYS AA CE  1 
ATOM   1609 N  NZ  . LYS A 1 215 ? 41.27000  17.28600  -9.09900  1.000 43.94980  ? 215 LYS AA NZ  1 
ATOM   1610 N  N   . ASN A 1 216 ? 37.41200  21.05300  -5.02400  1.000 28.28392  ? 216 ASN AA N   1 
ATOM   1611 C  CA  . ASN A 1 216 ? 36.37900  21.54900  -4.12300  1.000 18.65096  ? 216 ASN AA CA  1 
ATOM   1612 C  C   . ASN A 1 216 ? 37.01800  22.15900  -2.88000  1.000 26.49479  ? 216 ASN AA C   1 
ATOM   1613 O  O   . ASN A 1 216 ? 37.78000  21.49200  -2.17100  1.000 26.66525  ? 216 ASN AA O   1 
ATOM   1614 C  CB  . ASN A 1 216 ? 35.43200  20.41100  -3.74600  1.000 27.51986  ? 216 ASN AA CB  1 
ATOM   1615 C  CG  . ASN A 1 216 ? 34.22900  20.87900  -2.94200  1.000 28.17655  ? 216 ASN AA CG  1 
ATOM   1616 O  OD1 . ASN A 1 216 ? 34.15500  22.03100  -2.51200  1.000 28.59807  ? 216 ASN AA OD1 1 
ATOM   1617 N  ND2 . ASN A 1 216 ? 33.27300  19.97900  -2.74000  1.000 23.03692  ? 216 ASN AA ND2 1 
ATOM   1618 N  N   . GLN A 1 217 ? 36.69900  23.42400  -2.61100  1.000 20.86931  ? 217 GLN AA N   1 
ATOM   1619 C  CA  . GLN A 1 217 ? 37.24700  24.15000  -1.47300  1.000 23.19320  ? 217 GLN AA CA  1 
ATOM   1620 C  C   . GLN A 1 217 ? 36.20100  24.44300  -0.40500  1.000 33.26250  ? 217 GLN AA C   1 
ATOM   1621 O  O   . GLN A 1 217 ? 36.46100  25.24400  0.49900   1.000 23.68246  ? 217 GLN AA O   1 
ATOM   1622 C  CB  . GLN A 1 217 ? 37.89300  25.45400  -1.94400  1.000 27.46053  ? 217 GLN AA CB  1 
ATOM   1623 C  CG  . GLN A 1 217 ? 39.16100  25.26100  -2.75800  1.000 39.87835  ? 217 GLN AA CG  1 
ATOM   1624 C  CD  . GLN A 1 217 ? 40.16200  26.38200  -2.55300  1.000 73.96458  ? 217 GLN AA CD  1 
ATOM   1625 O  OE1 . GLN A 1 217 ? 41.10900  26.25100  -1.77700  1.000 75.70802  ? 217 GLN AA OE1 1 
ATOM   1626 N  NE2 . GLN A 1 217 ? 39.95500  27.49400  -3.25100  1.000 54.51349  ? 217 GLN AA NE2 1 
ATOM   1627 N  N   . SER A 1 218 ? 35.02700  23.82000  -0.48700  1.000 21.82202  ? 218 SER AA N   1 
ATOM   1628 C  CA  . SER A 1 218 ? 33.98900  24.05100  0.50500   1.000 35.45956  ? 218 SER AA CA  1 
ATOM   1629 C  C   . SER A 1 218 ? 34.40500  23.48200  1.86000   1.000 20.05251  ? 218 SER AA C   1 
ATOM   1630 O  O   . SER A 1 218 ? 35.29200  22.63100  1.96500   1.000 21.10097  ? 218 SER AA O   1 
ATOM   1631 C  CB  . SER A 1 218 ? 32.66500  23.43700  0.04900   1.000 18.09908  ? 218 SER AA CB  1 
ATOM   1632 O  OG  . SER A 1 218 ? 32.79300  22.04300  -0.16300  1.000 33.03400  ? 218 SER AA OG  1 
ATOM   1633 N  N   . ALA A 1 219 ? 33.73600  23.96500  2.91100   1.000 29.28930  ? 219 ALA AA N   1 
ATOM   1634 C  CA  . ALA A 1 219 ? 34.14600  23.63500  4.27200   1.000 26.54623  ? 219 ALA AA CA  1 
ATOM   1635 C  C   . ALA A 1 219 ? 33.97800  22.15200  4.58000   1.000 21.55785  ? 219 ALA AA C   1 
ATOM   1636 O  O   . ALA A 1 219 ? 34.69300  21.61400  5.43300   1.000 30.15119  ? 219 ALA AA O   1 
ATOM   1637 C  CB  . ALA A 1 219 ? 33.35800  24.47800  5.27300   1.000 17.71091  ? 219 ALA AA CB  1 
ATOM   1638 N  N   . LEU A 1 220 ? 33.04900  21.47500  3.90700   1.000 24.09682  ? 220 LEU AA N   1 
ATOM   1639 C  CA  . LEU A 1 220 ? 32.79700  20.06000  4.14000   1.000 30.42610  ? 220 LEU AA CA  1 
ATOM   1640 C  C   . LEU A 1 220 ? 33.47500  19.16000  3.11400   1.000 22.24098  ? 220 LEU AA C   1 
ATOM   1641 O  O   . LEU A 1 220 ? 33.16200  17.96700  3.04900   1.000 36.53536  ? 220 LEU AA O   1 
ATOM   1642 C  CB  . LEU A 1 220 ? 31.29100  19.78600  4.15300   1.000 31.05822  ? 220 LEU AA CB  1 
ATOM   1643 C  CG  . LEU A 1 220 ? 30.40500  20.77200  4.91900   1.000 38.33875  ? 220 LEU AA CG  1 
ATOM   1644 C  CD1 . LEU A 1 220 ? 29.02700  20.86700  4.27900   1.000 37.13002  ? 220 LEU AA CD1 1 
ATOM   1645 C  CD2 . LEU A 1 220 ? 30.29600  20.36800  6.38100   1.000 29.81020  ? 220 LEU AA CD2 1 
ATOM   1646 N  N   . ALA A 1 221 ? 34.40300  19.69900  2.32000   1.000 29.08928  ? 221 ALA AA N   1 
ATOM   1647 C  CA  . ALA A 1 221 ? 34.99700  18.92700  1.23300   1.000 32.94661  ? 221 ALA AA CA  1 
ATOM   1648 C  C   . ALA A 1 221 ? 35.93600  17.83300  1.72400   1.000 40.10946  ? 221 ALA AA C   1 
ATOM   1649 O  O   . ALA A 1 221 ? 36.22900  16.90300  0.96500   1.000 36.32545  ? 221 ALA AA O   1 
ATOM   1650 C  CB  . ALA A 1 221 ? 35.74500  19.85900  0.27900   1.000 21.89901  ? 221 ALA AA CB  1 
ATOM   1651 N  N   . ARG A 1 222 ? 36.41300  17.91400  2.96900   1.000 33.72512  ? 222 ARG AA N   1 
ATOM   1652 C  CA  . ARG A 1 222 ? 37.37600  16.93200  3.45700   1.000 34.19130  ? 222 ARG AA CA  1 
ATOM   1653 C  C   . ARG A 1 222 ? 36.74900  15.56500  3.70400   1.000 38.32698  ? 222 ARG AA C   1 
ATOM   1654 O  O   . ARG A 1 222 ? 37.47800  14.56900  3.77400   1.000 54.43806  ? 222 ARG AA O   1 
ATOM   1655 C  CB  . ARG A 1 222 ? 38.03900  17.43500  4.74000   1.000 46.82136  ? 222 ARG AA CB  1 
ATOM   1656 C  CG  . ARG A 1 222 ? 38.70100  18.79800  4.61000   1.000 41.94523  ? 222 ARG AA CG  1 
ATOM   1657 C  CD  . ARG A 1 222 ? 39.07400  19.35600  5.97500   1.000 62.15508  ? 222 ARG AA CD  1 
ATOM   1658 N  NE  . ARG A 1 222 ? 39.41800  20.77200  5.91500   1.000 85.84711  ? 222 ARG AA NE  1 
ATOM   1659 C  CZ  . ARG A 1 222 ? 38.53900  21.76200  5.99200   1.000 86.28934  ? 222 ARG AA CZ  1 
ATOM   1660 N  NH1 . ARG A 1 222 ? 37.24400  21.52700  6.12500   1.000 65.89728  ? 222 ARG AA NH1 1 
ATOM   1661 N  NH2 . ARG A 1 222 ? 38.96900  23.01900  5.93300   1.000 80.51557  ? 222 ARG AA NH2 1 
ATOM   1662 N  N   . MET A 1 223 ? 35.42900  15.48900  3.83800   1.000 44.56294  ? 223 MET AA N   1 
ATOM   1663 C  CA  . MET A 1 223 ? 34.76400  14.21700  4.10300   1.000 43.11878  ? 223 MET AA CA  1 
ATOM   1664 C  C   . MET A 1 223 ? 34.59800  13.39900  2.82400   1.000 44.29332  ? 223 MET AA C   1 
ATOM   1665 O  O   . MET A 1 223 ? 34.17600  13.91900  1.79100   1.000 32.77430  ? 223 MET AA O   1 
ATOM   1666 C  CB  . MET A 1 223 ? 33.40000  14.45200  4.75700   1.000 45.50932  ? 223 MET AA CB  1 
ATOM   1667 C  CG  . MET A 1 223 ? 33.38700  15.58000  5.77600   1.000 51.70113  ? 223 MET AA CG  1 
ATOM   1668 S  SD  . MET A 1 223 ? 31.77500  15.80700  6.55500   1.000 58.02375  ? 223 MET AA SD  1 
ATOM   1669 C  CE  . MET A 1 223 ? 31.46400  14.15800  7.18000   1.000 39.25523  ? 223 MET AA CE  1 
ATOM   1670 N  N   . THR A 1 227 ? 23.58800  21.60500  -0.19200  1.000 2.79608   ? 227 THR AA N   1 
ATOM   1671 C  CA  . THR A 1 227 ? 22.39300  20.89500  0.25700   1.000 8.12586   ? 227 THR AA CA  1 
ATOM   1672 C  C   . THR A 1 227 ? 21.12700  21.59800  -0.22100  1.000 6.10155   ? 227 THR AA C   1 
ATOM   1673 O  O   . THR A 1 227 ? 21.02800  22.82100  -0.15900  1.000 7.71125   ? 227 THR AA O   1 
ATOM   1674 C  CB  . THR A 1 227 ? 22.35200  20.77400  1.79700   1.000 5.96512   ? 227 THR AA CB  1 
ATOM   1675 O  OG1 . THR A 1 227 ? 23.48200  20.01900  2.24800   1.000 4.45127   ? 227 THR AA OG1 1 
ATOM   1676 C  CG2 . THR A 1 227 ? 21.07400  20.08200  2.25500   1.000 1.91029   ? 227 THR AA CG2 1 
ATOM   1677 N  N   . THR A 1 228 ? 20.16100  20.82200  -0.70300  1.000 9.24803   ? 228 THR AA N   1 
ATOM   1678 C  CA  . THR A 1 228 ? 18.85400  21.34100  -1.09400  1.000 6.33467   ? 228 THR AA CA  1 
ATOM   1679 C  C   . THR A 1 228 ? 17.78900  20.45400  -0.46100  1.000 11.87962  ? 228 THR AA C   1 
ATOM   1680 O  O   . THR A 1 228 ? 17.67900  19.27400  -0.80500  1.000 10.50458  ? 228 THR AA O   1 
ATOM   1681 C  CB  . THR A 1 228 ? 18.70500  21.38100  -2.61500  1.000 5.82659   ? 228 THR AA CB  1 
ATOM   1682 O  OG1 . THR A 1 228 ? 19.67000  22.28600  -3.16700  1.000 7.95961   ? 228 THR AA OG1 1 
ATOM   1683 C  CG2 . THR A 1 228 ? 17.31600  21.84500  -2.99800  1.000 11.50537  ? 228 THR AA CG2 1 
ATOM   1684 N  N   . ILE A 1 229 ? 17.01500  21.01500  0.46600   1.000 10.02930  ? 229 ILE AA N   1 
ATOM   1685 C  CA  . ILE A 1 229 ? 15.98100  20.27300  1.17700   1.000 8.40540   ? 229 ILE AA CA  1 
ATOM   1686 C  C   . ILE A 1 229 ? 14.63900  20.95200  0.95000   1.000 7.39013   ? 229 ILE AA C   1 
ATOM   1687 O  O   . ILE A 1 229 ? 14.56600  22.16600  0.73400   1.000 11.75368  ? 229 ILE AA O   1 
ATOM   1688 C  CB  . ILE A 1 229 ? 16.28700  20.16000  2.68700   1.000 1.18158   ? 229 ILE AA CB  1 
ATOM   1689 C  CG1 . ILE A 1 229 ? 16.47100  21.54900  3.30200   1.000 7.21640   ? 229 ILE AA CG1 1 
ATOM   1690 C  CG2 . ILE A 1 229 ? 17.51400  19.29800  2.91600   1.000 5.11263   ? 229 ILE AA CG2 1 
ATOM   1691 C  CD1 . ILE A 1 229 ? 16.73800  21.52700  4.79600   1.000 6.26495   ? 229 ILE AA CD1 1 
ATOM   1692 N  N   . GLY A 1 230 ? 13.57000  20.16300  1.00100   1.000 6.12628   ? 230 GLY AA N   1 
ATOM   1693 C  CA  . GLY A 1 230 ? 12.26200  20.74800  0.77400   1.000 4.20971   ? 230 GLY AA CA  1 
ATOM   1694 C  C   . GLY A 1 230 ? 11.13700  19.76200  0.99100   1.000 8.66447   ? 230 GLY AA C   1 
ATOM   1695 O  O   . GLY A 1 230 ? 11.35200  18.57300  1.24400   1.000 7.14911   ? 230 GLY AA O   1 
ATOM   1696 N  N   . ILE A 1 231 ? 9.91800   20.28900  0.88000   1.000 6.44825   ? 231 ILE AA N   1 
ATOM   1697 C  CA  . ILE A 1 231 ? 8.68400   19.53000  1.03500   1.000 7.69983   ? 231 ILE AA CA  1 
ATOM   1698 C  C   . ILE A 1 231 ? 7.86700   19.67000  -0.24100  1.000 11.54001  ? 231 ILE AA C   1 
ATOM   1699 O  O   . ILE A 1 231 ? 7.73900   20.77100  -0.78700  1.000 14.25729  ? 231 ILE AA O   1 
ATOM   1700 C  CB  . ILE A 1 231 ? 7.86200   20.02000  2.24800   1.000 12.49831  ? 231 ILE AA CB  1 
ATOM   1701 C  CG1 . ILE A 1 231 ? 8.72300   20.06800  3.51200   1.000 10.83622  ? 231 ILE AA CG1 1 
ATOM   1702 C  CG2 . ILE A 1 231 ? 6.62800   19.14700  2.45500   1.000 9.07512   ? 231 ILE AA CG2 1 
ATOM   1703 C  CD1 . ILE A 1 231 ? 8.09800   20.86900  4.63400   1.000 12.26025  ? 231 ILE AA CD1 1 
ATOM   1704 N  N   . VAL A 1 232 ? 7.31300   18.55700  -0.71400  1.000 5.83101   ? 232 VAL AA N   1 
ATOM   1705 C  CA  . VAL A 1 232 ? 6.34400   18.55700  -1.80400  1.000 6.64710   ? 232 VAL AA CA  1 
ATOM   1706 C  C   . VAL A 1 232 ? 5.04200   17.97800  -1.26700  1.000 10.75367  ? 232 VAL AA C   1 
ATOM   1707 O  O   . VAL A 1 232 ? 5.04900   16.93100  -0.60900  1.000 10.66691  ? 232 VAL AA O   1 
ATOM   1708 C  CB  . VAL A 1 232 ? 6.84800   17.76700  -3.02800  1.000 10.61781  ? 232 VAL AA CB  1 
ATOM   1709 C  CG1 . VAL A 1 232 ? 7.95000   18.53900  -3.73600  1.000 4.65984   ? 232 VAL AA CG1 1 
ATOM   1710 C  CG2 . VAL A 1 232 ? 7.35200   16.39000  -2.62300  1.000 15.07042  ? 232 VAL AA CG2 1 
ATOM   1711 N  N   . SER A 1 233 ? 3.93100   18.66500  -1.52800  1.000 5.87095   ? 233 SER AA N   1 
ATOM   1712 C  CA  . SER A 1 233 ? 2.64400   18.27200  -0.97100  1.000 10.67513  ? 233 SER AA CA  1 
ATOM   1713 C  C   . SER A 1 233 ? 1.56800   18.33400  -2.04500  1.000 17.30853  ? 233 SER AA C   1 
ATOM   1714 O  O   . SER A 1 233 ? 1.62700   19.15800  -2.96100  1.000 8.57875   ? 233 SER AA O   1 
ATOM   1715 C  CB  . SER A 1 233 ? 2.24500   19.16600  0.21200   1.000 11.66038  ? 233 SER AA CB  1 
ATOM   1716 O  OG  . SER A 1 233 ? 3.26600   19.20700  1.19300   1.000 14.29404  ? 233 SER AA OG  1 
ATOM   1717 N  N   . THR A 1 234 ? 0.57600   17.45600  -1.91200  1.000 11.58395  ? 234 THR AA N   1 
ATOM   1718 C  CA  . THR A 1 234 ? -0.56100  17.41200  -2.81900  1.000 7.58142   ? 234 THR AA CA  1 
ATOM   1719 C  C   . THR A 1 234 ? -1.84000  17.23700  -2.01200  1.000 14.61577  ? 234 THR AA C   1 
ATOM   1720 O  O   . THR A 1 234 ? -1.82000  16.71400  -0.89500  1.000 8.59557   ? 234 THR AA O   1 
ATOM   1721 C  CB  . THR A 1 234 ? -0.43000  16.27500  -3.84600  1.000 8.03296   ? 234 THR AA CB  1 
ATOM   1722 O  OG1 . THR A 1 234 ? -1.53200  16.32100  -4.76100  1.000 7.87468   ? 234 THR AA OG1 1 
ATOM   1723 C  CG2 . THR A 1 234 ? -0.41400  14.92100  -3.15000  1.000 10.96568  ? 234 THR AA CG2 1 
ATOM   1724 N  N   . ASN A 1 235 ? -2.95300  17.69200  -2.58200  1.000 18.44082  ? 235 ASN AA N   1 
ATOM   1725 C  CA  . ASN A 1 235 ? -4.25600  17.48900  -1.96400  1.000 13.46045  ? 235 ASN AA CA  1 
ATOM   1726 C  C   . ASN A 1 235 ? -4.87300  16.14600  -2.33300  1.000 19.74784  ? 235 ASN AA C   1 
ATOM   1727 O  O   . ASN A 1 235 ? -6.00000  15.86100  -1.91600  1.000 16.53841  ? 235 ASN AA O   1 
ATOM   1728 C  CB  . ASN A 1 235 ? -5.21500  18.62700  -2.34100  1.000 8.79658   ? 235 ASN AA CB  1 
ATOM   1729 C  CG  . ASN A 1 235 ? -5.31100  18.84700  -3.83900  1.000 18.41276  ? 235 ASN AA CG  1 
ATOM   1730 O  OD1 . ASN A 1 235 ? -4.67000  18.15300  -4.62700  1.000 14.65481  ? 235 ASN AA OD1 1 
ATOM   1731 N  ND2 . ASN A 1 235 ? -6.12200  19.82000  -4.24000  1.000 11.97586  ? 235 ASN AA ND2 1 
ATOM   1732 N  N   . CYS A 1 236 ? -4.16100  15.32000  -3.09700  1.000 10.04335  ? 236 CYS AA N   1 
ATOM   1733 C  CA  . CYS A 1 236 ? -4.63000  13.98900  -3.44100  1.000 9.88508   ? 236 CYS AA CA  1 
ATOM   1734 C  C   . CYS A 1 236 ? -4.43300  13.03000  -2.27200  1.000 14.76654  ? 236 CYS AA C   1 
ATOM   1735 O  O   . CYS A 1 236 ? -3.58800  13.23600  -1.39600  1.000 18.06044  ? 236 CYS AA O   1 
ATOM   1736 C  CB  . CYS A 1 236 ? -3.89000  13.45200  -4.66700  1.000 10.97992  ? 236 CYS AA CB  1 
ATOM   1737 S  SG  . CYS A 1 236 ? -4.39200  14.17200  -6.24200  1.000 17.49434  ? 236 CYS AA SG  1 
ATOM   1738 N  N   . ARG A 1 237 ? -5.23000  11.96400  -2.27100  1.000 12.95410  ? 237 ARG AA N   1 
ATOM   1739 C  CA  . ARG A 1 237 ? -5.04200  10.87600  -1.32400  1.000 19.10997  ? 237 ARG AA CA  1 
ATOM   1740 C  C   . ARG A 1 237 ? -3.93700  9.95400   -1.82600  1.000 16.09662  ? 237 ARG AA C   1 
ATOM   1741 O  O   . ARG A 1 237 ? -3.91800  9.58000   -3.00200  1.000 15.25584  ? 237 ARG AA O   1 
ATOM   1742 C  CB  . ARG A 1 237 ? -6.34400  10.09700  -1.13600  1.000 19.97094  ? 237 ARG AA CB  1 
ATOM   1743 C  CG  . ARG A 1 237 ? -6.29100  9.05600   -0.03000  1.000 30.73579  ? 237 ARG AA CG  1 
ATOM   1744 C  CD  . ARG A 1 237 ? -7.63600  8.36500   0.14600   1.000 34.09657  ? 237 ARG AA CD  1 
ATOM   1745 N  NE  . ARG A 1 237 ? -7.82100  7.27900   -0.80800  1.000 27.92428  ? 237 ARG AA NE  1 
ATOM   1746 C  CZ  . ARG A 1 237 ? -8.68700  7.30200   -1.81200  1.000 56.52326  ? 237 ARG AA CZ  1 
ATOM   1747 N  NH1 . ARG A 1 237 ? -9.47700  8.34200   -2.02000  1.000 48.98093  ? 237 ARG AA NH1 1 
ATOM   1748 N  NH2 . ARG A 1 237 ? -8.76300  6.25300   -2.62700  1.000 44.88339  ? 237 ARG AA NH2 1 
ATOM   1749 N  N   . LEU A 1 238 ? -3.01400  9.59400   -0.93700  1.000 16.89369  ? 238 LEU AA N   1 
ATOM   1750 C  CA  . LEU A 1 238 ? -1.88500  8.74700   -1.29000  1.000 12.55108  ? 238 LEU AA CA  1 
ATOM   1751 C  C   . LEU A 1 238 ? -1.68500  7.66900   -0.23500  1.000 10.37946  ? 238 LEU AA C   1 
ATOM   1752 O  O   . LEU A 1 238 ? -1.96000  7.87800   0.95000   1.000 17.55264  ? 238 LEU AA O   1 
ATOM   1753 C  CB  . LEU A 1 238 ? -0.58400  9.55700   -1.42500  1.000 8.55008   ? 238 LEU AA CB  1 
ATOM   1754 C  CG  . LEU A 1 238 ? -0.52200  10.74200  -2.38900  1.000 19.35360  ? 238 LEU AA CG  1 
ATOM   1755 C  CD1 . LEU A 1 238 ? 0.78500   11.49900  -2.19900  1.000 12.83711  ? 238 LEU AA CD1 1 
ATOM   1756 C  CD2 . LEU A 1 238 ? -0.66800  10.27600  -3.82700  1.000 15.93587  ? 238 LEU AA CD2 1 
ATOM   1757 N  N   . THR A 1 239 ? -1.20400  6.51100   -0.67900  1.000 11.37226  ? 239 THR AA N   1 
ATOM   1758 C  CA  . THR A 1 239 ? -0.67600  5.51700   0.24000   1.000 12.93471  ? 239 THR AA CA  1 
ATOM   1759 C  C   . THR A 1 239 ? 0.77400   5.85700   0.58300   1.000 9.86492   ? 239 THR AA C   1 
ATOM   1760 O  O   . THR A 1 239 ? 1.37200   6.77700   0.02000   1.000 8.82459   ? 239 THR AA O   1 
ATOM   1761 C  CB  . THR A 1 239 ? -0.76800  4.11400   -0.36000  1.000 14.04337  ? 239 THR AA CB  1 
ATOM   1762 O  OG1 . THR A 1 239 ? 0.05200   4.03800   -1.53400  1.000 15.56912  ? 239 THR AA OG1 1 
ATOM   1763 C  CG2 . THR A 1 239 ? -2.20700  3.78600   -0.73100  1.000 15.58629  ? 239 THR AA CG2 1 
ATOM   1764 N  N   . LYS A 1 240 ? 1.34400   5.09900   1.52500   1.000 11.60759  ? 240 LYS AA N   1 
ATOM   1765 C  CA  . LYS A 1 240 ? 2.72500   5.35100   1.92800   1.000 11.82008  ? 240 LYS AA CA  1 
ATOM   1766 C  C   . LYS A 1 240 ? 3.69300   5.11900   0.77400   1.000 10.21843  ? 240 LYS AA C   1 
ATOM   1767 O  O   . LYS A 1 240 ? 4.67700   5.85300   0.62500   1.000 10.29465  ? 240 LYS AA O   1 
ATOM   1768 C  CB  . LYS A 1 240 ? 3.10000   4.47500   3.12200   1.000 14.97965  ? 240 LYS AA CB  1 
ATOM   1769 C  CG  . LYS A 1 240 ? 2.87700   5.14300   4.46500   1.000 23.37456  ? 240 LYS AA CG  1 
ATOM   1770 C  CD  . LYS A 1 240 ? 3.72700   4.51000   5.55200   1.000 28.49039  ? 240 LYS AA CD  1 
ATOM   1771 C  CE  . LYS A 1 240 ? 4.79700   5.47200   6.04300   1.000 15.94177  ? 240 LYS AA CE  1 
ATOM   1772 N  NZ  . LYS A 1 240 ? 5.56600   4.90000   7.18200   1.000 16.28698  ? 240 LYS AA NZ  1 
ATOM   1773 N  N   . VAL A 1 241 ? 3.42900   4.10600   -0.05600  1.000 8.71689   ? 241 VAL AA N   1 
ATOM   1774 C  CA  . VAL A 1 241 ? 4.29500   3.83200   -1.20100  1.000 9.66286   ? 241 VAL AA CA  1 
ATOM   1775 C  C   . VAL A 1 241 ? 4.27400   4.99900   -2.17500  1.000 11.12105  ? 241 VAL AA C   1 
ATOM   1776 O  O   . VAL A 1 241 ? 5.32000   5.45400   -2.65100  1.000 7.72617   ? 241 VAL AA O   1 
ATOM   1777 C  CB  . VAL A 1 241 ? 3.87500   2.52700   -1.89800  1.000 16.82982  ? 241 VAL AA CB  1 
ATOM   1778 C  CG1 . VAL A 1 241 ? 4.83000   2.20400   -3.03700  1.000 22.86157  ? 241 VAL AA CG1 1 
ATOM   1779 C  CG2 . VAL A 1 241 ? 3.84800   1.41200   -0.91200  1.000 17.14023  ? 241 VAL AA CG2 1 
ATOM   1780 N  N   . GLU A 1 242 ? 3.07600   5.49300   -2.49400  1.000 9.46735   ? 242 GLU AA N   1 
ATOM   1781 C  CA  . GLU A 1 242 ? 2.96100   6.57400   -3.46600  1.000 12.16155  ? 242 GLU AA CA  1 
ATOM   1782 C  C   . GLU A 1 242 ? 3.60400   7.85500   -2.94800  1.000 8.58912   ? 242 GLU AA C   1 
ATOM   1783 O  O   . GLU A 1 242 ? 4.19000   8.61800   -3.72500  1.000 11.67053  ? 242 GLU AA O   1 
ATOM   1784 C  CB  . GLU A 1 242 ? 1.49200   6.80500   -3.81800  1.000 5.85432   ? 242 GLU AA CB  1 
ATOM   1785 C  CG  . GLU A 1 242 ? 0.82500   5.61000   -4.48200  1.000 9.48714   ? 242 GLU AA CG  1 
ATOM   1786 C  CD  . GLU A 1 242 ? -0.67100  5.79700   -4.65400  1.000 14.69129  ? 242 GLU AA CD  1 
ATOM   1787 O  OE1 . GLU A 1 242 ? -1.32500  6.27900   -3.70500  1.000 19.37029  ? 242 GLU AA OE1 1 
ATOM   1788 O  OE2 . GLU A 1 242 ? -1.19000  5.46900   -5.74200  1.000 18.98606  ? 242 GLU AA OE2 1 
ATOM   1789 N  N   . ALA A 1 243 ? 3.50800   8.10600   -1.64100  1.000 2.00700   ? 243 ALA AA N   1 
ATOM   1790 C  CA  . ALA A 1 243 ? 4.16300   9.27800   -1.06900  1.000 6.15099   ? 243 ALA AA CA  1 
ATOM   1791 C  C   . ALA A 1 243 ? 5.67600   9.18800   -1.22200  1.000 4.51059   ? 243 ALA AA C   1 
ATOM   1792 O  O   . ALA A 1 243 ? 6.32900   10.16800  -1.59900  1.000 12.50585  ? 243 ALA AA O   1 
ATOM   1793 C  CB  . ALA A 1 243 ? 3.77600   9.43200   0.40100   1.000 3.18289   ? 243 ALA AA CB  1 
ATOM   1794 N  N   . SER A 1 244 ? 6.25000   8.01500   -0.94300  1.000 7.65840   ? 244 SER AA N   1 
ATOM   1795 C  CA  . SER A 1 244 ? 7.69000   7.84300   -1.10200  1.000 13.70124  ? 244 SER AA CA  1 
ATOM   1796 C  C   . SER A 1 244 ? 8.09100   7.88900   -2.57100  1.000 10.15230  ? 244 SER AA C   1 
ATOM   1797 O  O   . SER A 1 244 ? 9.16600   8.39700   -2.91000  1.000 10.48870  ? 244 SER AA O   1 
ATOM   1798 C  CB  . SER A 1 244 ? 8.13600   6.52900   -0.46100  1.000 15.39061  ? 244 SER AA CB  1 
ATOM   1799 O  OG  . SER A 1 244 ? 8.55100   6.73600   0.87900   1.000 24.12613  ? 244 SER AA OG  1 
ATOM   1800 N  N   . ARG A 1 245 ? 7.23700   7.37100   -3.45700  1.000 6.58868   ? 245 ARG AA N   1 
ATOM   1801 C  CA  . ARG A 1 245 ? 7.51400   7.45900   -4.88700  1.000 8.18514   ? 245 ARG AA CA  1 
ATOM   1802 C  C   . ARG A 1 245 ? 7.45500   8.90200   -5.37200  1.000 12.23151  ? 245 ARG AA C   1 
ATOM   1803 O  O   . ARG A 1 245 ? 8.23500   9.30000   -6.24700  1.000 9.94164   ? 245 ARG AA O   1 
ATOM   1804 C  CB  . ARG A 1 245 ? 6.53100   6.58600   -5.66900  1.000 9.53800   ? 245 ARG AA CB  1 
ATOM   1805 C  CG  . ARG A 1 245 ? 6.85700   6.46000   -7.15300  1.000 14.60233  ? 245 ARG AA CG  1 
ATOM   1806 C  CD  . ARG A 1 245 ? 8.07500   5.57800   -7.37700  1.000 13.50589  ? 245 ARG AA CD  1 
ATOM   1807 N  NE  . ARG A 1 245 ? 8.40300   5.43700   -8.79100  1.000 17.49517  ? 245 ARG AA NE  1 
ATOM   1808 C  CZ  . ARG A 1 245 ? 9.51600   4.88200   -9.25000  1.000 30.82094  ? 245 ARG AA CZ  1 
ATOM   1809 N  NH1 . ARG A 1 245 ? 10.43800  4.40000   -8.43100  1.000 24.64959  ? 245 ARG AA NH1 1 
ATOM   1810 N  NH2 . ARG A 1 245 ? 9.71000   4.80600   -10.56400 1.000 15.05643  ? 245 ARG AA NH2 1 
ATOM   1811 N  N   . MET A 1 246 ? 6.53800   9.70200   -4.81900  1.000 7.69677   ? 246 MET AA N   1 
ATOM   1812 C  CA  . MET A 1 246 ? 6.48400   11.11700  -5.17500  1.000 11.76562  ? 246 MET AA CA  1 
ATOM   1813 C  C   . MET A 1 246 ? 7.76400   11.83600  -4.77100  1.000 12.68387  ? 246 MET AA C   1 
ATOM   1814 O  O   . MET A 1 246 ? 8.27800   12.67500  -5.52000  1.000 8.38400   ? 246 MET AA O   1 
ATOM   1815 C  CB  . MET A 1 246 ? 5.27300   11.78500  -4.52200  1.000 12.68802  ? 246 MET AA CB  1 
ATOM   1816 C  CG  . MET A 1 246 ? 4.72300   12.96200  -5.31700  1.000 16.78448  ? 246 MET AA CG  1 
ATOM   1817 S  SD  . MET A 1 246 ? 3.25300   13.71700  -4.59100  1.000 18.07314  ? 246 MET AA SD  1 
ATOM   1818 C  CE  . MET A 1 246 ? 3.96200   14.54100  -3.17100  1.000 20.14908  ? 246 MET AA CE  1 
ATOM   1819 N  N   . ALA A 1 247 ? 8.29200   11.52400  -3.58500  1.000 8.46043   ? 247 ALA AA N   1 
ATOM   1820 C  CA  . ALA A 1 247 ? 9.52700   12.15700  -3.13600  1.000 9.23294   ? 247 ALA AA CA  1 
ATOM   1821 C  C   . ALA A 1 247 ? 10.69400  11.78700  -4.04100  1.000 10.39723  ? 247 ALA AA C   1 
ATOM   1822 O  O   . ALA A 1 247 ? 11.55600  12.62500  -4.33000  1.000 10.34457  ? 247 ALA AA O   1 
ATOM   1823 C  CB  . ALA A 1 247 ? 9.82200   11.76200  -1.69000  1.000 1.82159   ? 247 ALA AA CB  1 
ATOM   1824 N  N   . THR A 1 248 ? 10.73600  10.53500  -4.50100  1.000 11.97202  ? 248 THR AA N   1 
ATOM   1825 C  CA  . THR A 1 248 ? 11.82900  10.09600  -5.36100  1.000 8.65100   ? 248 THR AA CA  1 
ATOM   1826 C  C   . THR A 1 248 ? 11.78900  10.80200  -6.70900  1.000 8.32196   ? 248 THR AA C   1 
ATOM   1827 O  O   . THR A 1 248 ? 12.82700  11.24200  -7.21800  1.000 13.49976  ? 248 THR AA O   1 
ATOM   1828 C  CB  . THR A 1 248 ? 11.77200  8.57900   -5.54400  1.000 13.35660  ? 248 THR AA CB  1 
ATOM   1829 O  OG1 . THR A 1 248 ? 11.94800  7.94000   -4.27300  1.000 7.23852   ? 248 THR AA OG1 1 
ATOM   1830 C  CG2 . THR A 1 248 ? 12.86300  8.11000   -6.49600  1.000 8.23367   ? 248 THR AA CG2 1 
ATOM   1831 N  N   . LEU A 1 249 ? 10.59900  10.93000  -7.29800  1.000 11.99379  ? 249 LEU AA N   1 
ATOM   1832 C  CA  . LEU A 1 249 ? 10.48000  11.60700  -8.58400  1.000 7.31058   ? 249 LEU AA CA  1 
ATOM   1833 C  C   . LEU A 1 249 ? 10.72800  13.10500  -8.46000  1.000 12.92109  ? 249 LEU AA C   1 
ATOM   1834 O  O   . LEU A 1 249 ? 11.18500  13.73500  -9.42000  1.000 9.23242   ? 249 LEU AA O   1 
ATOM   1835 C  CB  . LEU A 1 249 ? 9.10100   11.33900  -9.18600  1.000 5.98480   ? 249 LEU AA CB  1 
ATOM   1836 C  CG  . LEU A 1 249 ? 8.94900   9.95200   -9.81400  1.000 23.59591  ? 249 LEU AA CG  1 
ATOM   1837 C  CD1 . LEU A 1 249 ? 7.48500   9.56100   -9.95300  1.000 11.65098  ? 249 LEU AA CD1 1 
ATOM   1838 C  CD2 . LEU A 1 249 ? 9.64300   9.91900   -11.16200 1.000 19.93680  ? 249 LEU AA CD2 1 
ATOM   1839 N  N   . ALA A 1 250 ? 10.44100  13.68800  -7.29100  1.000 7.86990   ? 250 ALA AA N   1 
ATOM   1840 C  CA  . ALA A 1 250 ? 10.65800  15.11900  -7.09900  1.000 10.35889  ? 250 ALA AA CA  1 
ATOM   1841 C  C   . ALA A 1 250 ? 12.12700  15.49700  -7.25500  1.000 11.01068  ? 250 ALA AA C   1 
ATOM   1842 O  O   . ALA A 1 250 ? 12.43700  16.63100  -7.64000  1.000 5.70997   ? 250 ALA AA O   1 
ATOM   1843 C  CB  . ALA A 1 250 ? 10.14600  15.54900  -5.72300  1.000 6.89336   ? 250 ALA AA CB  1 
ATOM   1844 N  N   . HIS A 1 251 ? 13.04300  14.57000  -6.96300  1.000 8.63964   ? 251 HIS AA N   1 
ATOM   1845 C  CA  . HIS A 1 251 ? 14.46400  14.85800  -7.11600  1.000 9.16434   ? 251 HIS AA CA  1 
ATOM   1846 C  C   . HIS A 1 251 ? 14.84400  15.13100  -8.56500  1.000 13.72737  ? 251 HIS AA C   1 
ATOM   1847 O  O   . HIS A 1 251 ? 15.84500  15.81300  -8.81300  1.000 5.56032   ? 251 HIS AA O   1 
ATOM   1848 C  CB  . HIS A 1 251 ? 15.30100  13.70100  -6.56400  1.000 4.94867   ? 251 HIS AA CB  1 
ATOM   1849 C  CG  . HIS A 1 251 ? 15.54000  13.78000  -5.08900  1.000 12.83551  ? 251 HIS AA CG  1 
ATOM   1850 N  ND1 . HIS A 1 251 ? 16.48000  14.62000  -4.53100  1.000 8.74480   ? 251 HIS AA ND1 1 
ATOM   1851 C  CD2 . HIS A 1 251 ? 14.96200  13.12300  -4.05500  1.000 8.99296   ? 251 HIS AA CD2 1 
ATOM   1852 C  CE1 . HIS A 1 251 ? 16.47100  14.47800  -3.21800  1.000 16.19201  ? 251 HIS AA CE1 1 
ATOM   1853 N  NE2 . HIS A 1 251 ? 15.55900  13.57500  -2.90200  1.000 9.44998   ? 251 HIS AA NE2 1 
ATOM   1854 N  N   . ASN A 1 252 ? 14.07200  14.61600  -9.52600  1.000 7.04350   ? 252 ASN AA N   1 
ATOM   1855 C  CA  . ASN A 1 252 ? 14.34500  14.91300  -10.92800 1.000 14.85961  ? 252 ASN AA CA  1 
ATOM   1856 C  C   . ASN A 1 252 ? 14.20100  16.40000  -11.22000 1.000 17.32163  ? 252 ASN AA C   1 
ATOM   1857 O  O   . ASN A 1 252 ? 14.90600  16.93400  -12.08400 1.000 9.19788   ? 252 ASN AA O   1 
ATOM   1858 C  CB  . ASN A 1 252 ? 13.41500  14.10300  -11.83100 1.000 3.51766   ? 252 ASN AA CB  1 
ATOM   1859 C  CG  . ASN A 1 252 ? 13.69400  12.61500  -11.76800 1.000 5.20684   ? 252 ASN AA CG  1 
ATOM   1860 O  OD1 . ASN A 1 252 ? 14.81000  12.19500  -11.46400 1.000 11.30029  ? 252 ASN AA OD1 1 
ATOM   1861 N  ND2 . ASN A 1 252 ? 12.67800  11.80900  -12.05000 1.000 9.92022   ? 252 ASN AA ND2 1 
ATOM   1862 N  N   . GLY A 1 253 ? 13.29700  17.08300  -10.51600 1.000 8.91070   ? 253 GLY AA N   1 
ATOM   1863 C  CA  . GLY A 1 253 ? 13.19500  18.52400  -10.67100 1.000 14.06003  ? 253 GLY AA CA  1 
ATOM   1864 C  C   . GLY A 1 253 ? 14.40900  19.24800  -10.12200 1.000 16.44389  ? 253 GLY AA C   1 
ATOM   1865 O  O   . GLY A 1 253 ? 14.84900  20.25600  -10.68400 1.000 9.06846   ? 253 GLY AA O   1 
ATOM   1866 N  N   . LEU A 1 254 ? 14.96600  18.74600  -9.01800  1.000 8.03166   ? 254 LEU AA N   1 
ATOM   1867 C  CA  . LEU A 1 254 ? 16.20900  19.30500  -8.49800  1.000 5.10632   ? 254 LEU AA CA  1 
ATOM   1868 C  C   . LEU A 1 254 ? 17.34300  19.12500  -9.49700  1.000 11.83027  ? 254 LEU AA C   1 
ATOM   1869 O  O   . LEU A 1 254 ? 18.18000  20.02000  -9.66900  1.000 10.26112  ? 254 LEU AA O   1 
ATOM   1870 C  CB  . LEU A 1 254 ? 16.56000  18.64600  -7.16300  1.000 13.81660  ? 254 LEU AA CB  1 
ATOM   1871 C  CG  . LEU A 1 254 ? 15.65300  18.94200  -5.96400  1.000 10.10954  ? 254 LEU AA CG  1 
ATOM   1872 C  CD1 . LEU A 1 254 ? 16.37900  18.66100  -4.65500  1.000 8.67273   ? 254 LEU AA CD1 1 
ATOM   1873 C  CD2 . LEU A 1 254 ? 15.14000  20.37300  -6.00100  1.000 15.47293  ? 254 LEU AA CD2 1 
ATOM   1874 N  N   . ALA A 1 255 ? 17.38000  17.97400  -10.17800 1.000 8.85857   ? 255 ALA AA N   1 
ATOM   1875 C  CA  . ALA A 1 255 ? 18.43900  17.71300  -11.14800 1.000 8.82528   ? 255 ALA AA CA  1 
ATOM   1876 C  C   . ALA A 1 255 ? 18.31500  18.60500  -12.37600 1.000 12.66874  ? 255 ALA AA C   1 
ATOM   1877 O  O   . ALA A 1 255 ? 19.31600  18.87100  -13.05100 1.000 15.81475  ? 255 ALA AA O   1 
ATOM   1878 C  CB  . ALA A 1 255 ? 18.42200  16.24100  -11.55800 1.000 15.76740  ? 255 ALA AA CB  1 
ATOM   1879 N  N   . ARG A 1 256 ? 17.10600  19.07400  -12.68400 1.000 8.78981   ? 256 ARG AA N   1 
ATOM   1880 C  CA  . ARG A 1 256 ? 16.92600  19.96800  -13.82200 1.000 13.82477  ? 256 ARG AA CA  1 
ATOM   1881 C  C   . ARG A 1 256 ? 17.40800  21.38200  -13.52100 1.000 17.64197  ? 256 ARG AA C   1 
ATOM   1882 O  O   . ARG A 1 256 ? 17.81700  22.10100  -14.44000 1.000 17.16332  ? 256 ARG AA O   1 
ATOM   1883 C  CB  . ARG A 1 256 ? 15.45500  19.99400  -14.24100 1.000 11.10051  ? 256 ARG AA CB  1 
ATOM   1884 C  CG  . ARG A 1 256 ? 15.15100  19.19600  -15.49800 1.000 35.17696  ? 256 ARG AA CG  1 
ATOM   1885 C  CD  . ARG A 1 256 ? 14.12500  18.10100  -15.24000 1.000 25.72361  ? 256 ARG AA CD  1 
ATOM   1886 N  NE  . ARG A 1 256 ? 12.77700  18.63400  -15.07400 1.000 54.28628  ? 256 ARG AA NE  1 
ATOM   1887 C  CZ  . ARG A 1 256 ? 11.73900  17.92700  -14.64700 1.000 78.45502  ? 256 ARG AA CZ  1 
ATOM   1888 N  NH1 . ARG A 1 256 ? 11.85300  16.64200  -14.34900 1.000 38.05621  ? 256 ARG AA NH1 1 
ATOM   1889 N  NH2 . ARG A 1 256 ? 10.55600  18.52300  -14.52000 1.000 36.53838  ? 256 ARG AA NH2 1 
ATOM   1890 N  N   . ALA A 1 257 ? 17.38300  21.79300  -12.25400 1.000 16.97699  ? 257 ALA AA N   1 
ATOM   1891 C  CA  . ALA A 1 257 ? 17.69900  23.16400  -11.87500 1.000 18.07787  ? 257 ALA AA CA  1 
ATOM   1892 C  C   . ALA A 1 257 ? 19.12400  23.35400  -11.37300 1.000 20.86808  ? 257 ALA AA C   1 
ATOM   1893 O  O   . ALA A 1 257 ? 19.71100  24.41400  -11.60900 1.000 22.39287  ? 257 ALA AA O   1 
ATOM   1894 C  CB  . ALA A 1 257 ? 16.72500  23.64800  -10.79400 1.000 16.65883  ? 257 ALA AA CB  1 
ATOM   1895 N  N   . ILE A 1 258 ? 19.69800  22.36300  -10.69300 1.000 14.06237  ? 258 ILE AA N   1 
ATOM   1896 C  CA  . ILE A 1 258 ? 20.98200  22.50700  -10.01700 1.000 9.94672   ? 258 ILE AA CA  1 
ATOM   1897 C  C   . ILE A 1 258 ? 21.97000  21.50100  -10.59300 1.000 14.48846  ? 258 ILE AA C   1 
ATOM   1898 O  O   . ILE A 1 258 ? 21.62100  20.34000  -10.82800 1.000 11.25403  ? 258 ILE AA O   1 
ATOM   1899 C  CB  . ILE A 1 258 ? 20.83300  22.31800  -8.49300  1.000 10.87864  ? 258 ILE AA CB  1 
ATOM   1900 C  CG1 . ILE A 1 258 ? 19.87300  23.36100  -7.91800  1.000 11.10796  ? 258 ILE AA CG1 1 
ATOM   1901 C  CG2 . ILE A 1 258 ? 22.18600  22.39700  -7.80200  1.000 12.39823  ? 258 ILE AA CG2 1 
ATOM   1902 C  CD1 . ILE A 1 258 ? 19.12300  22.89100  -6.68900  1.000 14.28026  ? 258 ILE AA CD1 1 
ATOM   1903 N  N   . CYS A 1 259 ? 23.21100  21.95100  -10.81300 1.000 10.56802  ? 259 CYS AA N   1 
ATOM   1904 C  CA  . CYS A 1 259 ? 24.27800  21.09500  -11.31700 1.000 15.92923  ? 259 CYS AA CA  1 
ATOM   1905 C  C   . CYS A 1 259 ? 25.62200  21.62900  -10.83300 1.000 11.73068  ? 259 CYS AA C   1 
ATOM   1906 O  O   . CYS A 1 259 ? 25.90400  22.82200  -11.02900 1.000 15.51103  ? 259 CYS AA O   1 
ATOM   1907 C  CB  . CYS A 1 259 ? 24.26900  21.01500  -12.84500 1.000 12.96922  ? 259 CYS AA CB  1 
ATOM   1908 S  SG  . CYS A 1 259 ? 25.59800  20.00400  -13.54900 1.000 15.66203  ? 259 CYS AA SG  1 
ATOM   1909 N  N   . PRO A 1 260 ? 26.46100  20.79500  -10.19200 1.000 7.71686   ? 260 PRO AA N   1 
ATOM   1910 C  CA  . PRO A 1 260 ? 26.18500  19.39900  -9.83300  1.000 11.74400  ? 260 PRO AA CA  1 
ATOM   1911 C  C   . PRO A 1 260 ? 25.18300  19.27600  -8.68900  1.000 11.39035  ? 260 PRO AA C   1 
ATOM   1912 O  O   . PRO A 1 260 ? 24.95200  20.24200  -7.96200  1.000 9.22298   ? 260 PRO AA O   1 
ATOM   1913 C  CB  . PRO A 1 260 ? 27.55900  18.85800  -9.40300  1.000 14.51030  ? 260 PRO AA CB  1 
ATOM   1914 C  CG  . PRO A 1 260 ? 28.55900  19.89700  -9.81900  1.000 13.61957  ? 260 PRO AA CG  1 
ATOM   1915 C  CD  . PRO A 1 260 ? 27.82600  21.19400  -9.81600  1.000 11.37350  ? 260 PRO AA CD  1 
ATOM   1916 N  N   . ILE A 1 261 ? 24.59700  18.09000  -8.54200  1.000 10.76615  ? 261 ILE AA N   1 
ATOM   1917 C  CA  . ILE A 1 261 ? 23.57900  17.82500  -7.53600  1.000 7.79936   ? 261 ILE AA CA  1 
ATOM   1918 C  C   . ILE A 1 261 ? 23.90900  16.49900  -6.86500  1.000 10.19395  ? 261 ILE AA C   1 
ATOM   1919 O  O   . ILE A 1 261 ? 24.58000  15.64100  -7.44800  1.000 9.12891   ? 261 ILE AA O   1 
ATOM   1920 C  CB  . ILE A 1 261 ? 22.16000  17.80700  -8.16200  1.000 11.31690  ? 261 ILE AA CB  1 
ATOM   1921 C  CG1 . ILE A 1 261 ? 21.07300  17.69400  -7.08800  1.000 11.82324  ? 261 ILE AA CG1 1 
ATOM   1922 C  CG2 . ILE A 1 261 ? 22.03700  16.68200  -9.18500  1.000 7.35227   ? 261 ILE AA CG2 1 
ATOM   1923 C  CD1 . ILE A 1 261 ? 20.84400  18.96600  -6.30000  1.000 9.86247   ? 261 ILE AA CD1 1 
ATOM   1924 N  N   . HIS A 1 262 ? 23.45800  16.34900  -5.61600  1.000 5.06431   ? 262 HIS AA N   1 
ATOM   1925 C  CA  . HIS A 1 262 ? 23.62200  15.10600  -4.85600  1.000 12.96880  ? 262 HIS AA CA  1 
ATOM   1926 C  C   . HIS A 1 262 ? 25.09600  14.75100  -4.67000  1.000 10.78014  ? 262 HIS AA C   1 
ATOM   1927 O  O   . HIS A 1 262 ? 25.48200  13.58200  -4.73900  1.000 15.64818  ? 262 HIS AA O   1 
ATOM   1928 C  CB  . HIS A 1 262 ? 22.87000  13.94600  -5.51700  1.000 6.42232   ? 262 HIS AA CB  1 
ATOM   1929 C  CG  . HIS A 1 262 ? 21.42100  14.22400  -5.77600  1.000 14.43251  ? 262 HIS AA CG  1 
ATOM   1930 N  ND1 . HIS A 1 262 ? 20.79900  13.88400  -6.95800  1.000 11.98990  ? 262 HIS AA ND1 1 
ATOM   1931 C  CD2 . HIS A 1 262 ? 20.46800  14.79300  -5.00000  1.000 6.48955   ? 262 HIS AA CD2 1 
ATOM   1932 C  CE1 . HIS A 1 262 ? 19.52800  14.24000  -6.90300  1.000 9.98558   ? 262 HIS AA CE1 1 
ATOM   1933 N  NE2 . HIS A 1 262 ? 19.30200  14.79400  -5.72500  1.000 8.35229   ? 262 HIS AA NE2 1 
ATOM   1934 N  N   . THR A 1 263 ? 25.92700  15.76300  -4.42800  1.000 5.16803   ? 263 THR AA N   1 
ATOM   1935 C  CA  . THR A 1 263 ? 27.35600  15.54400  -4.25600  1.000 6.79948   ? 263 THR AA CA  1 
ATOM   1936 C  C   . THR A 1 263 ? 27.65400  15.05700  -2.83600  1.000 11.76002  ? 263 THR AA C   1 
ATOM   1937 O  O   . THR A 1 263 ? 26.75500  14.84100  -2.01900  1.000 13.05183  ? 263 THR AA O   1 
ATOM   1938 C  CB  . THR A 1 263 ? 28.13400  16.82100  -4.57200  1.000 12.36145  ? 263 THR AA CB  1 
ATOM   1939 O  OG1 . THR A 1 263 ? 27.89200  17.79700  -3.55100  1.000 5.56577   ? 263 THR AA OG1 1 
ATOM   1940 C  CG2 . THR A 1 263 ? 27.71100  17.38700  -5.92400  1.000 7.99848   ? 263 THR AA CG2 1 
ATOM   1941 N  N   . ASN A 1 264 ? 28.94400  14.88500  -2.53600  1.000 10.63804  ? 264 ASN AA N   1 
ATOM   1942 C  CA  . ASN A 1 264 ? 29.37700  14.40100  -1.22900  1.000 10.19385  ? 264 ASN AA CA  1 
ATOM   1943 C  C   . ASN A 1 264 ? 29.27300  15.45700  -0.13900  1.000 15.62137  ? 264 ASN AA C   1 
ATOM   1944 O  O   . ASN A 1 264 ? 29.41400  15.11700  1.04000   1.000 18.43379  ? 264 ASN AA O   1 
ATOM   1945 C  CB  . ASN A 1 264 ? 30.81900  13.88800  -1.29900  1.000 16.15150  ? 264 ASN AA CB  1 
ATOM   1946 C  CG  . ASN A 1 264 ? 30.94100  12.59100  -2.08000  1.000 18.20534  ? 264 ASN AA CG  1 
ATOM   1947 O  OD1 . ASN A 1 264 ? 29.97300  11.84400  -2.22000  1.000 29.82477  ? 264 ASN AA OD1 1 
ATOM   1948 N  ND2 . ASN A 1 264 ? 32.13200  12.32400  -2.60500  1.000 17.80601  ? 264 ASN AA ND2 1 
ATOM   1949 N  N   . VAL A 1 265 ? 29.04600  16.72100  -0.49400  1.000 9.16962   ? 265 VAL AA N   1 
ATOM   1950 C  CA  . VAL A 1 265 ? 28.82100  17.77800  0.48500   1.000 14.88498  ? 265 VAL AA CA  1 
ATOM   1951 C  C   . VAL A 1 265 ? 27.36200  18.18600  0.56500   1.000 8.59744   ? 265 VAL AA C   1 
ATOM   1952 O  O   . VAL A 1 265 ? 27.03000  19.11200  1.32000   1.000 11.41786  ? 265 VAL AA O   1 
ATOM   1953 C  CB  . VAL A 1 265 ? 29.70400  19.00900  0.20000   1.000 13.40631  ? 265 VAL AA CB  1 
ATOM   1954 C  CG1 . VAL A 1 265 ? 31.17600  18.62000  0.19600   1.000 12.13215  ? 265 VAL AA CG1 1 
ATOM   1955 C  CG2 . VAL A 1 265 ? 29.30800  19.65900  -1.11600  1.000 14.59218  ? 265 VAL AA CG2 1 
ATOM   1956 N  N   . ASP A 1 266 ? 26.48000  17.52800  -0.18100  1.000 10.37164  ? 266 ASP AA N   1 
ATOM   1957 C  CA  . ASP A 1 266 ? 25.06200  17.85800  -0.20500  1.000 11.45545  ? 266 ASP AA CA  1 
ATOM   1958 C  C   . ASP A 1 266 ? 24.27500  16.87900  0.65400   1.000 10.27189  ? 266 ASP AA C   1 
ATOM   1959 O  O   . ASP A 1 266 ? 24.51100  15.66800  0.61000   1.000 7.20349   ? 266 ASP AA O   1 
ATOM   1960 C  CB  . ASP A 1 266 ? 24.51600  17.83200  -1.63400  1.000 10.06466  ? 266 ASP AA CB  1 
ATOM   1961 C  CG  . ASP A 1 266 ? 24.96200  19.02500  -2.45200  1.000 9.76888   ? 266 ASP AA CG  1 
ATOM   1962 O  OD1 . ASP A 1 266 ? 24.92300  20.15800  -1.92900  1.000 7.40339   ? 266 ASP AA OD1 1 
ATOM   1963 O  OD2 . ASP A 1 266 ? 25.34400  18.82600  -3.62500  1.000 12.29448  ? 266 ASP AA OD2 1 
ATOM   1964 N  N   . GLY A 1 267 ? 23.33300  17.40900  1.42800   1.000 5.62496   ? 267 GLY AA N   1 
ATOM   1965 C  CA  . GLY A 1 267 ? 22.42600  16.57300  2.18700   1.000 6.60099   ? 267 GLY AA CA  1 
ATOM   1966 C  C   . GLY A 1 267 ? 21.02100  16.59900  1.62200   1.000 13.70379  ? 267 GLY AA C   1 
ATOM   1967 O  O   . GLY A 1 267 ? 20.04100  16.59800  2.37500   1.000 5.08295   ? 267 GLY AA O   1 
ATOM   1968 N  N   . ASP A 1 268 ? 20.92300  16.61200  0.29200   1.000 5.06630   ? 268 ASP AA N   1 
ATOM   1969 C  CA  . ASP A 1 268 ? 19.65100  16.78400  -0.40200  1.000 4.46807   ? 268 ASP AA CA  1 
ATOM   1970 C  C   . ASP A 1 268 ? 18.60600  15.78900  0.08300   1.000 8.85308   ? 268 ASP AA C   1 
ATOM   1971 O  O   . ASP A 1 268 ? 18.82300  14.57400  0.04900   1.000 4.94947   ? 268 ASP AA O   1 
ATOM   1972 C  CB  . ASP A 1 268 ? 19.86200  16.64100  -1.91100  1.000 7.91371   ? 268 ASP AA CB  1 
ATOM   1973 C  CG  . ASP A 1 268 ? 20.99900  17.50600  -2.42600  1.000 9.46326   ? 268 ASP AA CG  1 
ATOM   1974 O  OD1 . ASP A 1 268 ? 21.30500  18.53800  -1.79200  1.000 6.61462   ? 268 ASP AA OD1 1 
ATOM   1975 O  OD2 . ASP A 1 268 ? 21.58300  17.15900  -3.47100  1.000 10.81473  ? 268 ASP AA OD2 1 
ATOM   1976 N  N   . THR A 1 269 ? 17.46800  16.31700  0.53200   1.000 2.12187   ? 269 THR AA N   1 
ATOM   1977 C  CA  . THR A 1 269 ? 16.37400  15.52100  1.07000   1.000 5.98773   ? 269 THR AA CA  1 
ATOM   1978 C  C   . THR A 1 269 ? 15.05300  16.14100  0.63900   1.000 7.98672   ? 269 THR AA C   1 
ATOM   1979 O  O   . THR A 1 269 ? 14.90000  17.36400  0.66400   1.000 10.10882  ? 269 THR AA O   1 
ATOM   1980 C  CB  . THR A 1 269 ? 16.43600  15.44600  2.60400   1.000 6.36600   ? 269 THR AA CB  1 
ATOM   1981 O  OG1 . THR A 1 269 ? 17.68000  14.86200  3.01000   1.000 6.14477   ? 269 THR AA OG1 1 
ATOM   1982 C  CG2 . THR A 1 269 ? 15.28100  14.61300  3.15500   1.000 2.29498   ? 269 THR AA CG2 1 
ATOM   1983 N  N   . ILE A 1 270 ? 14.10100  15.29900  0.24500   1.000 6.27541   ? 270 ILE AA N   1 
ATOM   1984 C  CA  . ILE A 1 270 ? 12.76600  15.74700  -0.13400  1.000 9.33013   ? 270 ILE AA CA  1 
ATOM   1985 C  C   . ILE A 1 270 ? 11.74700  14.98800  0.70400   1.000 10.23747  ? 270 ILE AA C   1 
ATOM   1986 O  O   . ILE A 1 270 ? 11.73900  13.75000  0.71000   1.000 5.46599   ? 270 ILE AA O   1 
ATOM   1987 C  CB  . ILE A 1 270 ? 12.49200  15.54600  -1.63400  1.000 15.02592  ? 270 ILE AA CB  1 
ATOM   1988 C  CG1 . ILE A 1 270 ? 13.43700  16.41000  -2.47400  1.000 14.85974  ? 270 ILE AA CG1 1 
ATOM   1989 C  CG2 . ILE A 1 270 ? 11.03600  15.86800  -1.95200  1.000 7.81295   ? 270 ILE AA CG2 1 
ATOM   1990 C  CD1 . ILE A 1 270 ? 13.00100  17.85500  -2.59600  1.000 12.34978  ? 270 ILE AA CD1 1 
ATOM   1991 N  N   . PHE A 1 271 ? 10.89800  15.73000  1.41600   1.000 10.06560  ? 271 PHE AA N   1 
ATOM   1992 C  CA  . PHE A 1 271 ? 9.73400   15.17000  2.08800   1.000 6.71123   ? 271 PHE AA CA  1 
ATOM   1993 C  C   . PHE A 1 271 ? 8.51800   15.30000  1.17900   1.000 10.70512  ? 271 PHE AA C   1 
ATOM   1994 O  O   . PHE A 1 271 ? 8.37100   16.29400  0.46200   1.000 15.67896  ? 271 PHE AA O   1 
ATOM   1995 C  CB  . PHE A 1 271 ? 9.45900   15.88700  3.41400   1.000 6.24668   ? 271 PHE AA CB  1 
ATOM   1996 C  CG  . PHE A 1 271 ? 10.58500  15.80000  4.40800   1.000 11.48852  ? 271 PHE AA CG  1 
ATOM   1997 C  CD1 . PHE A 1 271 ? 10.68200  14.72400  5.27400   1.000 6.13830   ? 271 PHE AA CD1 1 
ATOM   1998 C  CD2 . PHE A 1 271 ? 11.53400  16.80700  4.49000   1.000 10.39207  ? 271 PHE AA CD2 1 
ATOM   1999 C  CE1 . PHE A 1 271 ? 11.71300  14.64600  6.19500   1.000 8.73868   ? 271 PHE AA CE1 1 
ATOM   2000 C  CE2 . PHE A 1 271 ? 12.56700  16.73600  5.41000   1.000 6.57969   ? 271 PHE AA CE2 1 
ATOM   2001 C  CZ  . PHE A 1 271 ? 12.65700  15.65400  6.26200   1.000 7.67560   ? 271 PHE AA CZ  1 
ATOM   2002 N  N   . ALA A 1 272 ? 7.64300   14.29800  1.21700   1.000 11.14279  ? 272 ALA AA N   1 
ATOM   2003 C  CA  . ALA A 1 272 ? 6.42200   14.30500  0.42200   1.000 8.04339   ? 272 ALA AA CA  1 
ATOM   2004 C  C   . ALA A 1 272 ? 5.23400   13.94300  1.30000   1.000 15.52942  ? 272 ALA AA C   1 
ATOM   2005 O  O   . ALA A 1 272 ? 5.32200   13.03600  2.13300   1.000 8.21269   ? 272 ALA AA O   1 
ATOM   2006 C  CB  . ALA A 1 272 ? 6.51500   13.33100  -0.75700  1.000 7.44713   ? 272 ALA AA CB  1 
ATOM   2007 N  N   . THR A 1 273 ? 4.12200   14.65900  1.11500   1.000 7.54226   ? 273 THR AA N   1 
ATOM   2008 C  CA  . THR A 1 273 ? 2.89700   14.38600  1.85400   1.000 15.30919  ? 273 THR AA CA  1 
ATOM   2009 C  C   . THR A 1 273 ? 1.70300   14.33300  0.91200   1.000 8.95275   ? 273 THR AA C   1 
ATOM   2010 O  O   . THR A 1 273 ? 1.63700   15.07500  -0.07300  1.000 15.72654  ? 273 THR AA O   1 
ATOM   2011 C  CB  . THR A 1 273 ? 2.61600   15.44300  2.94100   1.000 14.49381  ? 273 THR AA CB  1 
ATOM   2012 O  OG1 . THR A 1 273 ? 2.16200   16.65600  2.32800   1.000 10.02204  ? 273 THR AA OG1 1 
ATOM   2013 C  CG2 . THR A 1 273 ? 3.85900   15.72400  3.78000   1.000 13.65525  ? 273 THR AA CG2 1 
ATOM   2014 N  N   . GLY A 1 274 ? 0.76400   13.43700  1.22600   1.000 10.64120  ? 274 GLY AA N   1 
ATOM   2015 C  CA  . GLY A 1 274 ? -0.55800  13.47600  0.64600   1.000 7.69706   ? 274 GLY AA CA  1 
ATOM   2016 C  C   . GLY A 1 274 ? -1.59300  13.47100  1.75700   1.000 13.28092  ? 274 GLY AA C   1 
ATOM   2017 O  O   . GLY A 1 274 ? -1.27700  13.21400  2.92000   1.000 14.22407  ? 274 GLY AA O   1 
ATOM   2018 N  N   . LEU A 1 275 ? -2.83500  13.76400  1.38500   1.000 12.74092  ? 275 LEU AA N   1 
ATOM   2019 C  CA  . LEU A 1 275 ? -3.90900  13.83500  2.36600   1.000 13.16407  ? 275 LEU AA CA  1 
ATOM   2020 C  C   . LEU A 1 275 ? -4.42300  12.44100  2.70300   1.000 21.04611  ? 275 LEU AA C   1 
ATOM   2021 O  O   . LEU A 1 275 ? -4.57400  11.58800  1.82300   1.000 25.97120  ? 275 LEU AA O   1 
ATOM   2022 C  CB  . LEU A 1 275 ? -5.05400  14.70600  1.84700   1.000 16.78861  ? 275 LEU AA CB  1 
ATOM   2023 C  CG  . LEU A 1 275 ? -4.84900  16.22000  1.92700   1.000 19.35250  ? 275 LEU AA CG  1 
ATOM   2024 C  CD1 . LEU A 1 275 ? -6.06600  16.95900  1.39000   1.000 17.97076  ? 275 LEU AA CD1 1 
ATOM   2025 C  CD2 . LEU A 1 275 ? -4.54500  16.64900  3.35400   1.000 19.52484  ? 275 LEU AA CD2 1 
ATOM   2026 N  N   . GLN A 1 276 ? -4.68800  12.21100  3.99100   1.000 16.96971  ? 276 GLN AA N   1 
ATOM   2027 C  CA  . GLN A 1 276 ? -5.24000  10.92800  4.41600   1.000 14.41798  ? 276 GLN AA CA  1 
ATOM   2028 C  C   . GLN A 1 276 ? -6.69500  10.79000  3.98300   1.000 23.56837  ? 276 GLN AA C   1 
ATOM   2029 O  O   . GLN A 1 276 ? -7.10000  9.75200   3.44800   1.000 22.99672  ? 276 GLN AA O   1 
ATOM   2030 C  CB  . GLN A 1 276 ? -5.11600  10.77800  5.93300   1.000 25.83783  ? 276 GLN AA CB  1 
ATOM   2031 C  CG  . GLN A 1 276 ? -3.79400  10.19300  6.39600   1.000 20.26813  ? 276 GLN AA CG  1 
ATOM   2032 C  CD  . GLN A 1 276 ? -3.81500  9.77400   7.85200   1.000 34.30450  ? 276 GLN AA CD  1 
ATOM   2033 O  OE1 . GLN A 1 276 ? -4.79600  9.20900   8.33500   1.000 29.33614  ? 276 GLN AA OE1 1 
ATOM   2034 N  NE2 . GLN A 1 276 ? -2.72400  10.04800  8.56200   1.000 19.36601  ? 276 GLN AA NE2 1 
ATOM   2035 N  N   . LYS A 1 277 ? -7.49300  11.82900  4.20600   1.000 18.92103  ? 277 LYS AA N   1 
ATOM   2036 C  CA  . LYS A 1 277 ? -8.90800  11.84400  3.84400   1.000 24.88860  ? 277 LYS AA CA  1 
ATOM   2037 C  C   . LYS A 1 277 ? -9.08900  12.83400  2.69800   1.000 19.68532  ? 277 LYS AA C   1 
ATOM   2038 O  O   . LYS A 1 277 ? -9.06400  14.05100  2.90500   1.000 34.18652  ? 277 LYS AA O   1 
ATOM   2039 C  CB  . LYS A 1 277 ? -9.77400  12.21500  5.04500   1.000 28.25873  ? 277 LYS AA CB  1 
ATOM   2040 C  CG  . LYS A 1 277 ? -10.56200 11.05500  5.64300   1.000 74.07197  ? 277 LYS AA CG  1 
ATOM   2041 C  CD  . LYS A 1 277 ? -9.75200  9.76700   5.65400   1.000 79.41067  ? 277 LYS AA CD  1 
ATOM   2042 C  CE  . LYS A 1 277 ? -10.10400 8.90300   6.85700   1.000 70.42022  ? 277 LYS AA CE  1 
ATOM   2043 N  NZ  . LYS A 1 277 ? -11.52000 8.44000   6.81900   1.000 57.02872  ? 277 LYS AA NZ  1 
ATOM   2044 N  N   . SER A 1 278 ? -9.26600  12.30700  1.49000   1.000 22.54438  ? 278 SER AA N   1 
ATOM   2045 C  CA  . SER A 1 278 ? -9.51000  13.13000  0.31600   1.000 16.18445  ? 278 SER AA CA  1 
ATOM   2046 C  C   . SER A 1 278 ? -10.11000 12.24900  -0.76700  1.000 22.01071  ? 278 SER AA C   1 
ATOM   2047 O  O   . SER A 1 278 ? -9.82100  11.05200  -0.83900  1.000 26.00954  ? 278 SER AA O   1 
ATOM   2048 C  CB  . SER A 1 278 ? -8.22400  13.79900  -0.18500  1.000 20.39923  ? 278 SER AA CB  1 
ATOM   2049 O  OG  . SER A 1 278 ? -8.41400  14.38300  -1.46200  1.000 21.05287  ? 278 SER AA OG  1 
ATOM   2050 N  N   . ASP A 1 279 ? -10.95500 12.85000  -1.60100  1.000 22.04290  ? 279 ASP AA N   1 
ATOM   2051 C  CA  . ASP A 1 279 ? -11.57600 12.14500  -2.71300  1.000 35.72350  ? 279 ASP AA CA  1 
ATOM   2052 C  C   . ASP A 1 279 ? -10.84500 12.36400  -4.03100  1.000 27.43401  ? 279 ASP AA C   1 
ATOM   2053 O  O   . ASP A 1 279 ? -11.30200 11.87000  -5.06600  1.000 38.34560  ? 279 ASP AA O   1 
ATOM   2054 C  CB  . ASP A 1 279 ? -13.04300 12.56600  -2.85600  1.000 46.57625  ? 279 ASP AA CB  1 
ATOM   2055 C  CG  . ASP A 1 279 ? -13.23800 14.06200  -2.71400  1.000 58.96872  ? 279 ASP AA CG  1 
ATOM   2056 O  OD1 . ASP A 1 279 ? -12.24500 14.77000  -2.44500  1.000 63.06965  ? 279 ASP AA OD1 1 
ATOM   2057 O  OD2 . ASP A 1 279 ? -14.38600 14.53000  -2.87000  1.000 53.35142  ? 279 ASP AA OD2 1 
ATOM   2058 N  N   . LEU A 1 280 ? -9.72800  13.08600  -4.01800  1.000 17.97632  ? 280 LEU AA N   1 
ATOM   2059 C  CA  . LEU A 1 280 ? -8.94900  13.33400  -5.22200  1.000 19.27682  ? 280 LEU AA CA  1 
ATOM   2060 C  C   . LEU A 1 280 ? -7.85400  12.28400  -5.34800  1.000 27.87612  ? 280 LEU AA C   1 
ATOM   2061 O  O   . LEU A 1 280 ? -7.07300  12.07700  -4.41400  1.000 22.01471  ? 280 LEU AA O   1 
ATOM   2062 C  CB  . LEU A 1 280 ? -8.33600  14.73400  -5.19100  1.000 18.85378  ? 280 LEU AA CB  1 
ATOM   2063 C  CG  . LEU A 1 280 ? -9.31900  15.90400  -5.15300  1.000 30.19111  ? 280 LEU AA CG  1 
ATOM   2064 C  CD1 . LEU A 1 280 ? -8.58200  17.21700  -4.92700  1.000 22.15069  ? 280 LEU AA CD1 1 
ATOM   2065 C  CD2 . LEU A 1 280 ? -10.13700 15.95500  -6.43300  1.000 31.18356  ? 280 LEU AA CD2 1 
ATOM   2066 N  N   . THR A 1 281 ? -7.81200  11.61000  -6.49600  1.000 15.40619  ? 281 THR AA N   1 
ATOM   2067 C  CA  . THR A 1 281 ? -6.78600  10.62300  -6.79500  1.000 17.44017  ? 281 THR AA CA  1 
ATOM   2068 C  C   . THR A 1 281 ? -6.24000  10.86600  -8.19500  1.000 22.05028  ? 281 THR AA C   1 
ATOM   2069 O  O   . THR A 1 281 ? -6.91100  11.43900  -9.05700  1.000 19.73703  ? 281 THR AA O   1 
ATOM   2070 C  CB  . THR A 1 281 ? -7.31600  9.18100   -6.69200  1.000 16.68758  ? 281 THR AA CB  1 
ATOM   2071 O  OG1 . THR A 1 281 ? -8.14800  8.89100   -7.82200  1.000 29.07940  ? 281 THR AA OG1 1 
ATOM   2072 C  CG2 . THR A 1 281 ? -8.10700  8.97400   -5.40600  1.000 42.15006  ? 281 THR AA CG2 1 
ATOM   2073 N  N   . ALA A 1 282 ? -5.00800  10.41700  -8.40900  1.000 18.30393  ? 282 ALA AA N   1 
ATOM   2074 C  CA  . ALA A 1 282 ? -4.32400  10.57400  -9.68500  1.000 15.94220  ? 282 ALA AA CA  1 
ATOM   2075 C  C   . ALA A 1 282 ? -3.15300  9.60300   -9.71800  1.000 15.27790  ? 282 ALA AA C   1 
ATOM   2076 O  O   . ALA A 1 282 ? -2.68300  9.16300   -8.66200  1.000 8.60960   ? 282 ALA AA O   1 
ATOM   2077 C  CB  . ALA A 1 282 ? -3.84000  12.02000  -9.88300  1.000 9.77261   ? 282 ALA AA CB  1 
ATOM   2078 N  N   . PRO A 1 283 ? -2.67500  9.23300   -10.90700 1.000 14.06798  ? 283 PRO AA N   1 
ATOM   2079 C  CA  . PRO A 1 283 ? -1.50100  8.35300   -10.98100 1.000 14.72848  ? 283 PRO AA CA  1 
ATOM   2080 C  C   . PRO A 1 283 ? -0.29300  8.99400   -10.31300 1.000 9.83054   ? 283 PRO AA C   1 
ATOM   2081 O  O   . PRO A 1 283 ? -0.03200  10.18800  -10.47300 1.000 14.74100  ? 283 PRO AA O   1 
ATOM   2082 C  CB  . PRO A 1 283 ? -1.28400  8.17400   -12.48800 1.000 13.46867  ? 283 PRO AA CB  1 
ATOM   2083 C  CG  . PRO A 1 283 ? -2.61000  8.46900   -13.10400 1.000 16.60385  ? 283 PRO AA CG  1 
ATOM   2084 C  CD  . PRO A 1 283 ? -3.23800  9.51800   -12.23900 1.000 15.71141  ? 283 PRO AA CD  1 
ATOM   2085 N  N   . VAL A 1 284 ? 0.45000   8.18100   -9.55800  1.000 12.67930  ? 284 VAL AA N   1 
ATOM   2086 C  CA  . VAL A 1 284 ? 1.56200   8.71600   -8.78000  1.000 16.34991  ? 284 VAL AA CA  1 
ATOM   2087 C  C   . VAL A 1 284 ? 2.69200   9.19500   -9.68600  1.000 14.40069  ? 284 VAL AA C   1 
ATOM   2088 O  O   . VAL A 1 284 ? 3.40100   10.15100  -9.34800  1.000 13.62165  ? 284 VAL AA O   1 
ATOM   2089 C  CB  . VAL A 1 284 ? 2.05300   7.67600   -7.75100  1.000 25.64648  ? 284 VAL AA CB  1 
ATOM   2090 C  CG1 . VAL A 1 284 ? 2.57800   6.41800   -8.44100  1.000 11.74871  ? 284 VAL AA CG1 1 
ATOM   2091 C  CG2 . VAL A 1 284 ? 3.11400   8.28400   -6.84300  1.000 9.12993   ? 284 VAL AA CG2 1 
ATOM   2092 N  N   A ASP A 1 285 ? 2.88000   8.56500   -10.85000 0.946 11.00991  ? 285 ASP AA N   1 
ATOM   2093 N  N   B ASP A 1 285 ? 2.88000   8.54900   -10.84200 0.054 11.33843  ? 285 ASP AA N   1 
ATOM   2094 C  CA  A ASP A 1 285 ? 3.95000   9.02100   -11.73300 0.946 14.45593  ? 285 ASP AA CA  1 
ATOM   2095 C  CA  B ASP A 1 285 ? 3.91700   8.98400   -11.77100 0.054 14.23041  ? 285 ASP AA CA  1 
ATOM   2096 C  C   A ASP A 1 285 ? 3.61900   10.36900  -12.36300 0.946 12.43729  ? 285 ASP AA C   1 
ATOM   2097 C  C   B ASP A 1 285 ? 3.61300   10.36400  -12.33800 0.054 12.52402  ? 285 ASP AA C   1 
ATOM   2098 O  O   A ASP A 1 285 ? 4.53000   11.13900  -12.68500 0.946 15.82303  ? 285 ASP AA O   1 
ATOM   2099 O  O   B ASP A 1 285 ? 4.53600   11.14500  -12.59500 0.054 15.47900  ? 285 ASP AA O   1 
ATOM   2100 C  CB  A ASP A 1 285 ? 4.25600   7.97300   -12.80800 0.946 8.62882   ? 285 ASP AA CB  1 
ATOM   2101 C  CB  B ASP A 1 285 ? 4.07500   7.96600   -12.90100 0.054 9.93509   ? 285 ASP AA CB  1 
ATOM   2102 C  CG  A ASP A 1 285 ? 3.02300   7.52000   -13.56500 0.946 14.98561  ? 285 ASP AA CG  1 
ATOM   2103 C  CG  B ASP A 1 285 ? 2.75300   7.60900   -13.55500 0.054 14.68662  ? 285 ASP AA CG  1 
ATOM   2104 O  OD1 A ASP A 1 285 ? 1.91700   8.03000   -13.28800 0.946 24.49705  ? 285 ASP AA OD1 1 
ATOM   2105 O  OD1 B ASP A 1 285 ? 1.98800   6.82000   -12.96200 0.054 14.97817  ? 285 ASP AA OD1 1 
ATOM   2106 O  OD2 A ASP A 1 285 ? 3.16700   6.64200   -14.44200 0.946 11.66085  ? 285 ASP AA OD2 1 
ATOM   2107 O  OD2 B ASP A 1 285 ? 2.48100   8.11700   -14.66300 0.054 13.81236  ? 285 ASP AA OD2 1 
ATOM   2108 N  N   . LEU A 1 286 ? 2.33200   10.68000  -12.53700 1.000 10.54423  ? 286 LEU AA N   1 
ATOM   2109 C  CA  . LEU A 1 286 ? 1.96300   12.02400  -12.97000 1.000 10.65985  ? 286 LEU AA CA  1 
ATOM   2110 C  C   . LEU A 1 286 ? 2.15800   13.02900  -11.84100 1.000 13.01550  ? 286 LEU AA C   1 
ATOM   2111 O  O   . LEU A 1 286 ? 2.67800   14.12900  -12.06400 1.000 12.92342  ? 286 LEU AA O   1 
ATOM   2112 C  CB  . LEU A 1 286 ? 0.51700   12.04200  -13.46400 1.000 12.59736  ? 286 LEU AA CB  1 
ATOM   2113 C  CG  . LEU A 1 286 ? -0.13100  13.41800  -13.64000 1.000 18.48291  ? 286 LEU AA CG  1 
ATOM   2114 C  CD1 . LEU A 1 286 ? 0.54300   14.18900  -14.76400 1.000 9.99306   ? 286 LEU AA CD1 1 
ATOM   2115 C  CD2 . LEU A 1 286 ? -1.62600  13.28300  -13.89800 1.000 19.10744  ? 286 LEU AA CD2 1 
ATOM   2116 N  N   . LEU A 1 287 ? 1.75100   12.66700  -10.61900 1.000 9.05843   ? 287 LEU AA N   1 
ATOM   2117 C  CA  . LEU A 1 287 ? 1.96600   13.54500  -9.47300  1.000 8.71236   ? 287 LEU AA CA  1 
ATOM   2118 C  C   . LEU A 1 287 ? 3.44900   13.74500  -9.19200  1.000 10.99389  ? 287 LEU AA C   1 
ATOM   2119 O  O   . LEU A 1 287 ? 3.85900   14.83100  -8.76500  1.000 11.10351  ? 287 LEU AA O   1 
ATOM   2120 C  CB  . LEU A 1 287 ? 1.26400   12.98300  -8.23600  1.000 12.42270  ? 287 LEU AA CB  1 
ATOM   2121 C  CG  . LEU A 1 287 ? -0.26300  12.90000  -8.27800  1.000 11.61168  ? 287 LEU AA CG  1 
ATOM   2122 C  CD1 . LEU A 1 287 ? -0.79200  12.18600  -7.04400  1.000 11.42168  ? 287 LEU AA CD1 1 
ATOM   2123 C  CD2 . LEU A 1 287 ? -0.87300  14.28700  -8.39900  1.000 18.17939  ? 287 LEU AA CD2 1 
ATOM   2124 N  N   . GLY A 1 288 ? 4.26500   12.71400  -9.42100  1.000 9.10687   ? 288 GLY AA N   1 
ATOM   2125 C  CA  . GLY A 1 288 ? 5.69800   12.85900  -9.23500  1.000 9.71588   ? 288 GLY AA CA  1 
ATOM   2126 C  C   . GLY A 1 288 ? 6.34500   13.76100  -10.26600 1.000 9.92137   ? 288 GLY AA C   1 
ATOM   2127 O  O   . GLY A 1 288 ? 7.31000   14.46700  -9.95700  1.000 9.73737   ? 288 GLY AA O   1 
ATOM   2128 N  N   . THR A 1 289 ? 5.83400   13.75100  -11.50000 1.000 10.97418  ? 289 THR AA N   1 
ATOM   2129 C  CA  . THR A 1 289 ? 6.34800   14.66300  -12.51600 1.000 10.75435  ? 289 THR AA CA  1 
ATOM   2130 C  C   . THR A 1 289 ? 5.97500   16.10500  -12.19500 1.000 10.56024  ? 289 THR AA C   1 
ATOM   2131 O  O   . THR A 1 289 ? 6.80500   17.01200  -12.32900 1.000 13.36942  ? 289 THR AA O   1 
ATOM   2132 C  CB  . THR A 1 289 ? 5.82400   14.26800  -13.89800 1.000 9.00603   ? 289 THR AA CB  1 
ATOM   2133 O  OG1 . THR A 1 289 ? 6.07200   12.87500  -14.12400 1.000 11.59527  ? 289 THR AA OG1 1 
ATOM   2134 C  CG2 . THR A 1 289 ? 6.51500   15.07600  -14.98100 1.000 3.90572   ? 289 THR AA CG2 1 
ATOM   2135 N  N   . ALA A 1 290 ? 4.73100   16.33500  -11.76900 1.000 6.95390   ? 290 ALA AA N   1 
ATOM   2136 C  CA  . ALA A 1 290 ? 4.33700   17.67000  -11.33500 1.000 9.88588   ? 290 ALA AA CA  1 
ATOM   2137 C  C   . ALA A 1 290 ? 5.12200   18.09800  -10.10200 1.000 13.86178  ? 290 ALA AA C   1 
ATOM   2138 O  O   . ALA A 1 290 ? 5.47400   19.27400  -9.95900  1.000 11.26784  ? 290 ALA AA O   1 
ATOM   2139 C  CB  . ALA A 1 290 ? 2.83500   17.71400  -11.05900 1.000 12.29537  ? 290 ALA AA CB  1 
ATOM   2140 N  N   . ALA A 1 291 ? 5.40400   17.15400  -9.19900  1.000 8.69067   ? 291 ALA AA N   1 
ATOM   2141 C  CA  . ALA A 1 291 ? 6.23400   17.46600  -8.04000  1.000 8.32232   ? 291 ALA AA CA  1 
ATOM   2142 C  C   . ALA A 1 291 ? 7.62400   17.91900  -8.46700  1.000 9.48414   ? 291 ALA AA C   1 
ATOM   2143 O  O   . ALA A 1 291 ? 8.19900   18.83700  -7.86900  1.000 7.74130   ? 291 ALA AA O   1 
ATOM   2144 C  CB  . ALA A 1 291 ? 6.32400   16.25300  -7.11400  1.000 9.25951   ? 291 ALA AA CB  1 
ATOM   2145 N  N   . ALA A 1 292 ? 8.17800   17.29000  -9.50800  1.000 5.72168   ? 292 ALA AA N   1 
ATOM   2146 C  CA  . ALA A 1 292 ? 9.48100   17.70600  -10.01400 1.000 6.91358   ? 292 ALA AA CA  1 
ATOM   2147 C  C   . ALA A 1 292 ? 9.42500   19.11700  -10.58700 1.000 6.82086   ? 292 ALA AA C   1 
ATOM   2148 O  O   . ALA A 1 292 ? 10.33900  19.92000  -10.36600 1.000 7.27856   ? 292 ALA AA O   1 
ATOM   2149 C  CB  . ALA A 1 292 ? 9.97700   16.71600  -11.06700 1.000 3.22504   ? 292 ALA AA CB  1 
ATOM   2150 N  N   . GLU A 1 293 ? 8.35700   19.44200  -11.32200 1.000 10.57443  ? 293 GLU AA N   1 
ATOM   2151 C  CA  . GLU A 1 293 ? 8.22200   20.79000  -11.86700 1.000 9.24484   ? 293 GLU AA CA  1 
ATOM   2152 C  C   . GLU A 1 293 ? 8.06900   21.81700  -10.75100 1.000 10.70478  ? 293 GLU AA C   1 
ATOM   2153 O  O   . GLU A 1 293 ? 8.72300   22.86600  -10.76300 1.000 8.38315   ? 293 GLU AA O   1 
ATOM   2154 C  CB  . GLU A 1 293 ? 7.03300   20.86200  -12.82900 1.000 10.05343  ? 293 GLU AA CB  1 
ATOM   2155 C  CG  . GLU A 1 293 ? 6.66400   22.29000  -13.22100 1.000 19.66765  ? 293 GLU AA CG  1 
ATOM   2156 C  CD  . GLU A 1 293 ? 5.55000   22.36600  -14.25100 1.000 11.46663  ? 293 GLU AA CD  1 
ATOM   2157 O  OE1 . GLU A 1 293 ? 4.59900   21.56000  -14.17600 1.000 10.71921  ? 293 GLU AA OE1 1 
ATOM   2158 O  OE2 . GLU A 1 293 ? 5.62600   23.24300  -15.13700 1.000 20.82998  ? 293 GLU AA OE2 1 
ATOM   2159 N  N   . ALA A 1 294 ? 7.20500   21.52800  -9.77300  1.000 10.40299  ? 294 ALA AA N   1 
ATOM   2160 C  CA  . ALA A 1 294 ? 7.00400   22.45200  -8.66100  1.000 7.38875   ? 294 ALA AA CA  1 
ATOM   2161 C  C   . ALA A 1 294 ? 8.29400   22.66600  -7.88000  1.000 8.74470   ? 294 ALA AA C   1 
ATOM   2162 O  O   . ALA A 1 294 ? 8.58600   23.78500  -7.44200  1.000 12.45822  ? 294 ALA AA O   1 
ATOM   2163 C  CB  . ALA A 1 294 ? 5.90000   21.93400  -7.73900  1.000 10.49535  ? 294 ALA AA CB  1 
ATOM   2164 N  N   . ALA A 1 295 ? 9.08500   21.60400  -7.70300  1.000 9.60953   ? 295 ALA AA N   1 
ATOM   2165 C  CA  . ALA A 1 295 ? 10.34200  21.73500  -6.97400  1.000 5.37601   ? 295 ALA AA CA  1 
ATOM   2166 C  C   . ALA A 1 295 ? 11.34500  22.57700  -7.75100  1.000 9.96798   ? 295 ALA AA C   1 
ATOM   2167 O  O   . ALA A 1 295 ? 12.08200  23.37700  -7.16200  1.000 7.36988   ? 295 ALA AA O   1 
ATOM   2168 C  CB  . ALA A 1 295 ? 10.92000  20.35300  -6.67000  1.000 8.54701   ? 295 ALA AA CB  1 
ATOM   2169 N  N   . MET A 1 296 ? 11.38500  22.41600  -9.07600  1.000 6.84802   ? 296 MET AA N   1 
ATOM   2170 C  CA  . MET A 1 296 ? 12.30900  23.20000  -9.88600  1.000 8.67027   ? 296 MET AA CA  1 
ATOM   2171 C  C   . MET A 1 296 ? 11.91800  24.67400  -9.89600  1.000 9.73477   ? 296 MET AA C   1 
ATOM   2172 O  O   . MET A 1 296 ? 12.77900  25.55000  -9.75100  1.000 9.63393   ? 296 MET AA O   1 
ATOM   2173 C  CB  . MET A 1 296 ? 12.36500  22.63600  -11.30700 1.000 11.10364  ? 296 MET AA CB  1 
ATOM   2174 C  CG  . MET A 1 296 ? 13.02300  23.55100  -12.32800 1.000 11.64373  ? 296 MET AA CG  1 
ATOM   2175 S  SD  . MET A 1 296 ? 12.71200  23.00900  -14.02100 1.000 32.25354  ? 296 MET AA SD  1 
ATOM   2176 C  CE  . MET A 1 296 ? 11.11400  23.75900  -14.33600 1.000 29.52888  ? 296 MET AA CE  1 
ATOM   2177 N  N   . LEU A 1 297 ? 10.62300  24.96500  -10.04900 1.000 5.66473   ? 297 LEU AA N   1 
ATOM   2178 C  CA  . LEU A 1 297 ? 10.16700  26.35100  -10.00500 1.000 9.59938   ? 297 LEU AA CA  1 
ATOM   2179 C  C   . LEU A 1 297 ? 10.40300  26.97800  -8.63800  1.000 10.60556  ? 297 LEU AA C   1 
ATOM   2180 O  O   . LEU A 1 297 ? 10.69900  28.17600  -8.54700  1.000 15.79821  ? 297 LEU AA O   1 
ATOM   2181 C  CB  . LEU A 1 297 ? 8.68400   26.43000  -10.37200 1.000 8.12293   ? 297 LEU AA CB  1 
ATOM   2182 C  CG  . LEU A 1 297 ? 8.31300   26.08700  -11.81600 1.000 18.94914  ? 297 LEU AA CG  1 
ATOM   2183 C  CD1 . LEU A 1 297 ? 6.80300   25.99900  -11.97500 1.000 14.30901  ? 297 LEU AA CD1 1 
ATOM   2184 C  CD2 . LEU A 1 297 ? 8.89700   27.11500  -12.77200 1.000 10.00909  ? 297 LEU AA CD2 1 
ATOM   2185 N  N   . ALA A 1 298 ? 10.27400  26.19400  -7.56500  1.000 11.20940  ? 298 ALA AA N   1 
ATOM   2186 C  CA  . ALA A 1 298 ? 10.51800  26.72900  -6.23000  1.000 6.99344   ? 298 ALA AA CA  1 
ATOM   2187 C  C   . ALA A 1 298 ? 11.98600  27.07500  -6.02400  1.000 11.95134  ? 298 ALA AA C   1 
ATOM   2188 O  O   . ALA A 1 298 ? 12.30100  28.01300  -5.28300  1.000 9.92008   ? 298 ALA AA O   1 
ATOM   2189 C  CB  . ALA A 1 298 ? 10.05100  25.73200  -5.16900  1.000 10.60509  ? 298 ALA AA CB  1 
ATOM   2190 N  N   . CYS A 1 299 ? 12.89200  26.33100  -6.66600  1.000 8.92806   ? 299 CYS AA N   1 
ATOM   2191 C  CA  . CYS A 1 299 ? 14.31400  26.65100  -6.58700  1.000 8.23751   ? 299 CYS AA CA  1 
ATOM   2192 C  C   . CYS A 1 299 ? 14.59200  28.03900  -7.15000  1.000 17.31820  ? 299 CYS AA C   1 
ATOM   2193 O  O   . CYS A 1 299 ? 15.30700  28.84000  -6.53700  1.000 14.46809  ? 299 CYS AA O   1 
ATOM   2194 C  CB  . CYS A 1 299 ? 15.13300  25.59800  -7.33600  1.000 10.03864  ? 299 CYS AA CB  1 
ATOM   2195 S  SG  . CYS A 1 299 ? 15.23800  23.99400  -6.51900  1.000 15.82161  ? 299 CYS AA SG  1 
ATOM   2196 N  N   . LEU A 1 300 ? 14.03300  28.33900  -8.32500  1.000 12.75300  ? 300 LEU AA N   1 
ATOM   2197 C  CA  . LEU A 1 300 ? 14.23400  29.65200  -8.92600  1.000 7.03385   ? 300 LEU AA CA  1 
ATOM   2198 C  C   . LEU A 1 300 ? 13.55500  30.74400  -8.11000  1.000 19.80723  ? 300 LEU AA C   1 
ATOM   2199 O  O   . LEU A 1 300 ? 14.06900  31.86400  -8.01600  1.000 13.86503  ? 300 LEU AA O   1 
ATOM   2200 C  CB  . LEU A 1 300 ? 13.72000  29.65300  -10.36400 1.000 14.07732  ? 300 LEU AA CB  1 
ATOM   2201 C  CG  . LEU A 1 300 ? 14.38500  28.63300  -11.28900 1.000 24.16371  ? 300 LEU AA CG  1 
ATOM   2202 C  CD1 . LEU A 1 300 ? 13.54800  28.40100  -12.53900 1.000 26.21225  ? 300 LEU AA CD1 1 
ATOM   2203 C  CD2 . LEU A 1 300 ? 15.78700  29.09300  -11.65400 1.000 24.91409  ? 300 LEU AA CD2 1 
ATOM   2204 N  N   . ASP A 1 301 ? 12.40100  30.43600  -7.51300  1.000 7.69038   ? 301 ASP AA N   1 
ATOM   2205 C  CA  . ASP A 1 301 ? 11.70600  31.41900  -6.68900  1.000 11.38378  ? 301 ASP AA CA  1 
ATOM   2206 C  C   . ASP A 1 301 ? 12.55700  31.85500  -5.50300  1.000 12.42855  ? 301 ASP AA C   1 
ATOM   2207 O  O   . ASP A 1 301 ? 12.48500  33.01500  -5.08100  1.000 14.63733  ? 301 ASP AA O   1 
ATOM   2208 C  CB  . ASP A 1 301 ? 10.37300  30.84400  -6.20600  1.000 13.79959  ? 301 ASP AA CB  1 
ATOM   2209 C  CG  . ASP A 1 301 ? 9.56800   31.83900  -5.39600  1.000 20.82304  ? 301 ASP AA CG  1 
ATOM   2210 O  OD1 . ASP A 1 301 ? 9.27900   32.93500  -5.92000  1.000 17.59668  ? 301 ASP AA OD1 1 
ATOM   2211 O  OD2 . ASP A 1 301 ? 9.22400   31.52600  -4.23600  1.000 13.16137  ? 301 ASP AA OD2 1 
ATOM   2212 N  N   . ALA A 1 302 ? 13.37900  30.94800  -4.96800  1.000 14.91755  ? 302 ALA AA N   1 
ATOM   2213 C  CA  . ALA A 1 302 ? 14.17800  31.26400  -3.78900  1.000 16.60688  ? 302 ALA AA CA  1 
ATOM   2214 C  C   . ALA A 1 302 ? 15.19000  32.36800  -4.06100  1.000 14.76916  ? 302 ALA AA C   1 
ATOM   2215 O  O   . ALA A 1 302 ? 15.55900  33.10800  -3.14200  1.000 23.01864  ? 302 ALA AA O   1 
ATOM   2216 C  CB  . ALA A 1 302 ? 14.89100  30.00700  -3.29000  1.000 11.18896  ? 302 ALA AA CB  1 
ATOM   2217 N  N   . VAL A 1 303 ? 15.65400  32.49800  -5.30800  1.000 15.31566  ? 303 VAL AA N   1 
ATOM   2218 C  CA  . VAL A 1 303 ? 16.65600  33.50600  -5.64600  1.000 21.19032  ? 303 VAL AA CA  1 
ATOM   2219 C  C   . VAL A 1 303 ? 16.05800  34.74000  -6.31000  1.000 24.53732  ? 303 VAL AA C   1 
ATOM   2220 O  O   . VAL A 1 303 ? 16.76900  35.74400  -6.47300  1.000 29.89430  ? 303 VAL AA O   1 
ATOM   2221 C  CB  . VAL A 1 303 ? 17.76600  32.91700  -6.54400  1.000 18.84430  ? 303 VAL AA CB  1 
ATOM   2222 C  CG1 . VAL A 1 303 ? 18.39000  31.69800  -5.88100  1.000 19.65357  ? 303 VAL AA CG1 1 
ATOM   2223 C  CG2 . VAL A 1 303 ? 17.21400  32.56400  -7.91300  1.000 22.48366  ? 303 VAL AA CG2 1 
ATOM   2224 N  N   . MET A 1 304 ? 14.78200  34.70400  -6.69500  1.000 24.96716  ? 304 MET AA N   1 
ATOM   2225 C  CA  . MET A 1 304 ? 14.12000  35.88900  -7.22400  1.000 32.04283  ? 304 MET AA CA  1 
ATOM   2226 C  C   . MET A 1 304 ? 13.70200  36.86900  -6.13500  1.000 35.84926  ? 304 MET AA C   1 
ATOM   2227 O  O   . MET A 1 304 ? 13.24200  37.96900  -6.45900  1.000 66.17227  ? 304 MET AA O   1 
ATOM   2228 C  CB  . MET A 1 304 ? 12.89100  35.49200  -8.04600  1.000 54.45628  ? 304 MET AA CB  1 
ATOM   2229 C  CG  . MET A 1 304 ? 13.19500  34.67900  -9.29700  1.000 54.77015  ? 304 MET AA CG  1 
ATOM   2230 S  SD  . MET A 1 304 ? 14.86900  34.91200  -9.92600  1.000 74.83634  ? 304 MET AA SD  1 
ATOM   2231 C  CE  . MET A 1 304 ? 15.03600  33.46800  -10.97300 1.000 37.86585  ? 304 MET AA CE  1 
ATOM   2232 N  N   . GLN A 1 305 ? 13.84500  36.50100  -4.86500  1.000 55.24012  ? 305 GLN AA N   1 
ATOM   2233 C  CA  . GLN A 1 305 ? 13.49400  37.38600  -3.76000  1.000 62.70642  ? 305 GLN AA CA  1 
ATOM   2234 C  C   . GLN A 1 305 ? 14.74100  37.85300  -3.01600  1.000 71.03070  ? 305 GLN AA C   1 
ATOM   2235 O  O   . GLN A 1 305 ? 15.84100  37.35400  -3.25400  1.000 75.17078  ? 305 GLN AA O   1 
ATOM   2236 C  CB  . GLN A 1 305 ? 12.53600  36.68700  -2.79200  1.000 46.02434  ? 305 GLN AA CB  1 
ATOM   2237 C  CG  . GLN A 1 305 ? 11.07600  37.05700  -2.99100  1.000 46.69373  ? 305 GLN AA CG  1 
ATOM   2238 C  CD  . GLN A 1 305 ? 10.39200  36.20600  -4.04400  1.000 49.77345  ? 305 GLN AA CD  1 
ATOM   2239 O  OE1 . GLN A 1 305 ? 11.03700  35.43500  -4.75400  1.000 58.58687  ? 305 GLN AA OE1 1 
ATOM   2240 N  NE2 . GLN A 1 305 ? 9.07900   36.35300  -4.15600  1.000 60.99024  ? 305 GLN AA NE2 1 
ATOM   2241 N  N   . MET B 1 1   ? 31.13700  -7.18200  27.45700  1.000 10.34981  ? 1   MET BA N   1 
ATOM   2242 C  CA  . MET B 1 1   ? 31.62800  -5.90200  27.95100  1.000 14.45928  ? 1   MET BA CA  1 
ATOM   2243 C  C   . MET B 1 1   ? 32.12900  -5.06500  26.77400  1.000 18.30400  ? 1   MET BA C   1 
ATOM   2244 O  O   . MET B 1 1   ? 33.22000  -5.31000  26.25500  1.000 14.93533  ? 1   MET BA O   1 
ATOM   2245 C  CB  . MET B 1 1   ? 32.74500  -6.11300  28.97700  1.000 14.73154  ? 1   MET BA CB  1 
ATOM   2246 C  CG  . MET B 1 1   ? 33.01400  -4.91200  29.86800  1.000 15.41026  ? 1   MET BA CG  1 
ATOM   2247 S  SD  . MET B 1 1   ? 31.51800  -4.36000  30.71600  1.000 23.67065  ? 1   MET BA SD  1 
ATOM   2248 C  CE  . MET B 1 1   ? 31.33400  -5.62300  31.96400  1.000 17.47476  ? 1   MET BA CE  1 
ATOM   2249 N  N   . LEU B 1 2   ? 31.32600  -4.08000  26.35700  1.000 10.32042  ? 2   LEU BA N   1 
ATOM   2250 C  CA  . LEU B 1 2   ? 31.64900  -3.31300  25.15700  1.000 10.54872  ? 2   LEU BA CA  1 
ATOM   2251 C  C   . LEU B 1 2   ? 32.98600  -2.59400  25.27800  1.000 7.18760   ? 2   LEU BA C   1 
ATOM   2252 O  O   . LEU B 1 2   ? 33.66500  -2.37500  24.26800  1.000 11.41017  ? 2   LEU BA O   1 
ATOM   2253 C  CB  . LEU B 1 2   ? 30.53800  -2.30700  24.85600  1.000 5.69718   ? 2   LEU BA CB  1 
ATOM   2254 C  CG  . LEU B 1 2   ? 30.60600  -1.66800  23.46600  1.000 6.17883   ? 2   LEU BA CG  1 
ATOM   2255 C  CD1 . LEU B 1 2   ? 30.34000  -2.71000  22.38800  1.000 10.75737  ? 2   LEU BA CD1 1 
ATOM   2256 C  CD2 . LEU B 1 2   ? 29.63100  -0.50800  23.34800  1.000 8.02922   ? 2   LEU BA CD2 1 
ATOM   2257 N  N   . THR B 1 3   ? 33.38800  -2.22900  26.49600  1.000 6.54513   ? 3   THR BA N   1 
ATOM   2258 C  CA  . THR B 1 3   ? 34.66200  -1.55100  26.69800  1.000 9.70082   ? 3   THR BA CA  1 
ATOM   2259 C  C   . THR B 1 3   ? 35.86300  -2.45300  26.44000  1.000 15.98469  ? 3   THR BA C   1 
ATOM   2260 O  O   . THR B 1 3   ? 36.99800  -1.96700  26.50000  1.000 8.96788   ? 3   THR BA O   1 
ATOM   2261 C  CB  . THR B 1 3   ? 34.73500  -0.98200  28.11600  1.000 14.60860  ? 3   THR BA CB  1 
ATOM   2262 O  OG1 . THR B 1 3   ? 34.22200  -1.94400  29.04600  1.000 17.42679  ? 3   THR BA OG1 1 
ATOM   2263 C  CG2 . THR B 1 3   ? 33.91000  0.29100   28.21500  1.000 9.10262   ? 3   THR BA CG2 1 
ATOM   2264 N  N   . ASP B 1 4   ? 35.64900  -3.74300  26.15900  1.000 10.54493  ? 4   ASP BA N   1 
ATOM   2265 C  CA  . ASP B 1 4   ? 36.74500  -4.60800  25.73700  1.000 10.76604  ? 4   ASP BA CA  1 
ATOM   2266 C  C   . ASP B 1 4   ? 37.34900  -4.15400  24.41600  1.000 11.98616  ? 4   ASP BA C   1 
ATOM   2267 O  O   . ASP B 1 4   ? 38.50700  -4.47800  24.13000  1.000 15.79339  ? 4   ASP BA O   1 
ATOM   2268 C  CB  . ASP B 1 4   ? 36.26000  -6.05300  25.60600  1.000 10.82521  ? 4   ASP BA CB  1 
ATOM   2269 C  CG  . ASP B 1 4   ? 36.04500  -6.72500  26.94800  1.000 18.57117  ? 4   ASP BA CG  1 
ATOM   2270 O  OD1 . ASP B 1 4   ? 36.42900  -6.13800  27.98200  1.000 19.38359  ? 4   ASP BA OD1 1 
ATOM   2271 O  OD2 . ASP B 1 4   ? 35.48500  -7.84000  26.96900  1.000 14.18970  ? 4   ASP BA OD2 1 
ATOM   2272 N  N   . ILE B 1 5   ? 36.59200  -3.42300  23.60300  1.000 9.62033   ? 5   ILE BA N   1 
ATOM   2273 C  CA  . ILE B 1 5   ? 37.09600  -2.91100  22.33500  1.000 15.79183  ? 5   ILE BA CA  1 
ATOM   2274 C  C   . ILE B 1 5   ? 37.86100  -1.62200  22.59200  1.000 14.22853  ? 5   ILE BA C   1 
ATOM   2275 O  O   . ILE B 1 5   ? 37.44600  -0.78800  23.40700  1.000 15.67551  ? 5   ILE BA O   1 
ATOM   2276 C  CB  . ILE B 1 5   ? 35.94000  -2.69800  21.34200  1.000 13.39084  ? 5   ILE BA CB  1 
ATOM   2277 C  CG1 . ILE B 1 5   ? 35.00200  -3.90700  21.35200  1.000 15.96456  ? 5   ILE BA CG1 1 
ATOM   2278 C  CG2 . ILE B 1 5   ? 36.47400  -2.45100  19.93800  1.000 15.14575  ? 5   ILE BA CG2 1 
ATOM   2279 C  CD1 . ILE B 1 5   ? 35.66200  -5.19700  20.90700  1.000 11.52698  ? 5   ILE BA CD1 1 
ATOM   2280 N  N   . ASP B 1 6   ? 38.98400  -1.45700  21.89600  1.000 12.63370  ? 6   ASP BA N   1 
ATOM   2281 C  CA  . ASP B 1 6   ? 39.88100  -0.33700  22.15900  1.000 18.92433  ? 6   ASP BA CA  1 
ATOM   2282 C  C   . ASP B 1 6   ? 39.18100  1.00100   21.95200  1.000 17.97446  ? 6   ASP BA C   1 
ATOM   2283 O  O   . ASP B 1 6   ? 38.44700  1.19700   20.98100  1.000 28.73570  ? 6   ASP BA O   1 
ATOM   2284 C  CB  . ASP B 1 6   ? 41.11200  -0.42200  21.25500  1.000 27.33624  ? 6   ASP BA CB  1 
ATOM   2285 C  CG  . ASP B 1 6   ? 41.67100  -1.82800  21.15700  1.000 41.76166  ? 6   ASP BA CG  1 
ATOM   2286 O  OD1 . ASP B 1 6   ? 40.90100  -2.75800  20.83600  1.000 52.88598  ? 6   ASP BA OD1 1 
ATOM   2287 O  OD2 . ASP B 1 6   ? 42.88300  -2.00300  21.40100  1.000 58.92128  ? 6   ASP BA OD2 1 
ATOM   2288 N  N   . GLY B 1 7   ? 39.41500  1.92400   22.88400  1.000 20.82135  ? 7   GLY BA N   1 
ATOM   2289 C  CA  . GLY B 1 7   ? 38.95300  3.29000   22.76200  1.000 13.40864  ? 7   GLY BA CA  1 
ATOM   2290 C  C   . GLY B 1 7   ? 37.51000  3.54000   23.14200  1.000 24.64809  ? 7   GLY BA C   1 
ATOM   2291 O  O   . GLY B 1 7   ? 37.04800  4.68100   23.01800  1.000 23.98765  ? 7   GLY BA O   1 
ATOM   2292 N  N   . ILE B 1 8   ? 36.78200  2.52900   23.60800  1.000 15.17533  ? 8   ILE BA N   1 
ATOM   2293 C  CA  . ILE B 1 8   ? 35.36100  2.66100   23.90800  1.000 13.57030  ? 8   ILE BA CA  1 
ATOM   2294 C  C   . ILE B 1 8   ? 35.18500  2.93800   25.39400  1.000 14.95338  ? 8   ILE BA C   1 
ATOM   2295 O  O   . ILE B 1 8   ? 35.72500  2.21300   26.24000  1.000 15.69458  ? 8   ILE BA O   1 
ATOM   2296 C  CB  . ILE B 1 8   ? 34.58300  1.40400   23.48700  1.000 17.68267  ? 8   ILE BA CB  1 
ATOM   2297 C  CG1 . ILE B 1 8   ? 34.61000  1.24900   21.96400  1.000 11.63150  ? 8   ILE BA CG1 1 
ATOM   2298 C  CG2 . ILE B 1 8   ? 33.14800  1.47300   23.99200  1.000 8.57534   ? 8   ILE BA CG2 1 
ATOM   2299 C  CD1 . ILE B 1 8   ? 33.63600  0.21700   21.43400  1.000 8.29500   ? 8   ILE BA CD1 1 
ATOM   2300 N  N   . ARG B 1 9   ? 34.43300  3.99000   25.71100  1.000 7.05365   ? 9   ARG BA N   1 
ATOM   2301 C  CA  . ARG B 1 9   ? 34.00500  4.29300   27.06700  1.000 9.96370   ? 9   ARG BA CA  1 
ATOM   2302 C  C   . ARG B 1 9   ? 32.48300  4.33200   27.11000  1.000 16.45376  ? 9   ARG BA C   1 
ATOM   2303 O  O   . ARG B 1 9   ? 31.83100  4.73600   26.14200  1.000 14.02336  ? 9   ARG BA O   1 
ATOM   2304 C  CB  . ARG B 1 9   ? 34.58000  5.62800   27.55100  1.000 15.11624  ? 9   ARG BA CB  1 
ATOM   2305 C  CG  . ARG B 1 9   ? 36.09100  5.62900   27.71200  1.000 15.73182  ? 9   ARG BA CG  1 
ATOM   2306 C  CD  . ARG B 1 9   ? 36.58200  6.94300   28.29800  1.000 15.20025  ? 9   ARG BA CD  1 
ATOM   2307 N  NE  . ARG B 1 9   ? 36.68000  7.98500   27.28300  1.000 18.06016  ? 9   ARG BA NE  1 
ATOM   2308 C  CZ  . ARG B 1 9   ? 35.93400  9.08100   27.25800  1.000 17.26219  ? 9   ARG BA CZ  1 
ATOM   2309 N  NH1 . ARG B 1 9   ? 35.02900  9.32200   28.19200  1.000 17.08690  ? 9   ARG BA NH1 1 
ATOM   2310 N  NH2 . ARG B 1 9   ? 36.09900  9.95600   26.27000  1.000 17.24398  ? 9   ARG BA NH2 1 
ATOM   2311 N  N   . VAL B 1 10  ? 31.91800  3.90900   28.23800  1.000 10.37546  ? 10  VAL BA N   1 
ATOM   2312 C  CA  . VAL B 1 10  ? 30.47400  3.79000   28.40100  1.000 10.24143  ? 10  VAL BA CA  1 
ATOM   2313 C  C   . VAL B 1 10  ? 30.04900  4.59300   29.62300  1.000 12.83550  ? 10  VAL BA C   1 
ATOM   2314 O  O   . VAL B 1 10  ? 30.67500  4.49400   30.68500  1.000 16.06325  ? 10  VAL BA O   1 
ATOM   2315 C  CB  . VAL B 1 10  ? 30.03500  2.31900   28.54300  1.000 13.37520  ? 10  VAL BA CB  1 
ATOM   2316 C  CG1 . VAL B 1 10  ? 28.55400  2.23100   28.87000  1.000 6.09481   ? 10  VAL BA CG1 1 
ATOM   2317 C  CG2 . VAL B 1 10  ? 30.34700  1.54700   27.26900  1.000 8.02256   ? 10  VAL BA CG2 1 
ATOM   2318 N  N   . GLY B 1 11  ? 28.99400  5.37900   29.47400  1.000 5.40425   ? 11  GLY BA N   1 
ATOM   2319 C  CA  . GLY B 1 11  ? 28.46100  6.15900   30.57900  1.000 9.26585   ? 11  GLY BA CA  1 
ATOM   2320 C  C   . GLY B 1 11  ? 26.95400  6.05500   30.66000  1.000 9.34425   ? 11  GLY BA C   1 
ATOM   2321 O  O   . GLY B 1 11  ? 26.26100  6.10800   29.64500  1.000 11.57988  ? 11  GLY BA O   1 
ATOM   2322 N  N   . HIS B 1 12  ? 26.45400  5.90500   31.88200  1.000 9.89867   ? 12  HIS BA N   1 
ATOM   2323 C  CA  . HIS B 1 12  ? 25.02700  5.81600   32.14600  1.000 10.34306  ? 12  HIS BA CA  1 
ATOM   2324 C  C   . HIS B 1 12  ? 24.52300  7.11300   32.76300  1.000 11.74992  ? 12  HIS BA C   1 
ATOM   2325 O  O   . HIS B 1 12  ? 25.26800  7.83500   33.43200  1.000 9.44579   ? 12  HIS BA O   1 
ATOM   2326 C  CB  . HIS B 1 12  ? 24.70500  4.66000   33.10100  1.000 8.59018   ? 12  HIS BA CB  1 
ATOM   2327 C  CG  . HIS B 1 12  ? 24.98400  3.30200   32.53800  1.000 21.73898  ? 12  HIS BA CG  1 
ATOM   2328 N  ND1 . HIS B 1 12  ? 24.54100  2.90300   31.29600  1.000 12.73474  ? 12  HIS BA ND1 1 
ATOM   2329 C  CD2 . HIS B 1 12  ? 25.65100  2.24400   33.05800  1.000 9.99845   ? 12  HIS BA CD2 1 
ATOM   2330 C  CE1 . HIS B 1 12  ? 24.92900  1.66000   31.07100  1.000 14.77255  ? 12  HIS BA CE1 1 
ATOM   2331 N  NE2 . HIS B 1 12  ? 25.60400  1.23700   32.12500  1.000 8.87213   ? 12  HIS BA NE2 1 
ATOM   2332 N  N   . ALA B 1 13  ? 23.24600  7.39900   32.52700  1.000 9.95121   ? 13  ALA BA N   1 
ATOM   2333 C  CA  . ALA B 1 13  ? 22.49500  8.39600   33.28100  1.000 18.37464  ? 13  ALA BA CA  1 
ATOM   2334 C  C   . ALA B 1 13  ? 21.15900  7.76600   33.63900  1.000 16.87882  ? 13  ALA BA C   1 
ATOM   2335 O  O   . ALA B 1 13  ? 20.41200  7.35300   32.74700  1.000 17.38043  ? 13  ALA BA O   1 
ATOM   2336 C  CB  . ALA B 1 13  ? 22.29800  9.68500   32.47900  1.000 17.24798  ? 13  ALA BA CB  1 
ATOM   2337 N  N   . THR B 1 14  ? 20.86600  7.67900   34.93400  1.000 22.50891  ? 14  THR BA N   1 
ATOM   2338 C  CA  . THR B 1 14  ? 19.74700  6.88800   35.42500  1.000 19.51776  ? 14  THR BA CA  1 
ATOM   2339 C  C   . THR B 1 14  ? 18.83300  7.73300   36.30000  1.000 22.09995  ? 14  THR BA C   1 
ATOM   2340 O  O   . THR B 1 14  ? 19.30100  8.49000   37.15500  1.000 20.28980  ? 14  THR BA O   1 
ATOM   2341 C  CB  . THR B 1 14  ? 20.24300  5.67200   36.22200  1.000 12.88694  ? 14  THR BA CB  1 
ATOM   2342 O  OG1 . THR B 1 14  ? 21.19900  4.94600   35.43900  1.000 12.93422  ? 14  THR BA OG1 1 
ATOM   2343 C  CG2 . THR B 1 14  ? 19.08500  4.75100   36.59000  1.000 14.00361  ? 14  THR BA CG2 1 
ATOM   2344 N  N   . ASP B 1 15  ? 17.52800  7.59500   36.07900  1.000 18.15330  ? 15  ASP BA N   1 
ATOM   2345 C  CA  . ASP B 1 15  ? 16.49900  8.19700   36.92500  1.000 16.65094  ? 15  ASP BA CA  1 
ATOM   2346 C  C   . ASP B 1 15  ? 15.64400  7.05300   37.46000  1.000 18.94936  ? 15  ASP BA C   1 
ATOM   2347 O  O   . ASP B 1 15  ? 14.71300  6.59600   36.78800  1.000 14.21810  ? 15  ASP BA O   1 
ATOM   2348 C  CB  . ASP B 1 15  ? 15.66600  9.21400   36.14900  1.000 20.13042  ? 15  ASP BA CB  1 
ATOM   2349 C  CG  . ASP B 1 15  ? 14.77200  10.05300  37.05000  1.000 21.61093  ? 15  ASP BA CG  1 
ATOM   2350 O  OD1 . ASP B 1 15  ? 14.33800  9.55200   38.10800  1.000 19.67950  ? 15  ASP BA OD1 1 
ATOM   2351 O  OD2 . ASP B 1 15  ? 14.50100  11.21900  36.69700  1.000 25.07507  ? 15  ASP BA OD2 1 
ATOM   2352 N  N   . ALA B 1 16  ? 15.96100  6.59400   38.67400  1.000 18.83676  ? 16  ALA BA N   1 
ATOM   2353 C  CA  . ALA B 1 16  ? 15.26300  5.44400   39.24000  1.000 23.52542  ? 16  ALA BA CA  1 
ATOM   2354 C  C   . ALA B 1 16  ? 13.82200  5.77200   39.60600  1.000 21.50025  ? 16  ALA BA C   1 
ATOM   2355 O  O   . ALA B 1 16  ? 12.96400  4.88100   39.59000  1.000 35.78877  ? 16  ALA BA O   1 
ATOM   2356 C  CB  . ALA B 1 16  ? 16.01400  4.92400   40.46500  1.000 24.38659  ? 16  ALA BA CB  1 
ATOM   2357 N  N   . ARG B 1 17  ? 13.53300  7.03100   39.93600  1.000 20.97118  ? 17  ARG BA N   1 
ATOM   2358 C  CA  . ARG B 1 17  ? 12.17600  7.40400   40.32200  1.000 18.29954  ? 17  ARG BA CA  1 
ATOM   2359 C  C   . ARG B 1 17  ? 11.25300  7.47800   39.11100  1.000 19.39340  ? 17  ARG BA C   1 
ATOM   2360 O  O   . ARG B 1 17  ? 10.15100  6.91900   39.12500  1.000 19.32384  ? 17  ARG BA O   1 
ATOM   2361 C  CB  . ARG B 1 17  ? 12.19400  8.73800   41.07200  1.000 21.30911  ? 17  ARG BA CB  1 
ATOM   2362 C  CG  . ARG B 1 17  ? 10.89700  9.07500   41.79000  1.000 35.88244  ? 17  ARG BA CG  1 
ATOM   2363 C  CD  . ARG B 1 17  ? 10.09600  10.11300  41.02100  1.000 61.29819  ? 17  ARG BA CD  1 
ATOM   2364 N  NE  . ARG B 1 17  ? 10.46800  11.47300  41.39000  1.000 73.72196  ? 17  ARG BA NE  1 
ATOM   2365 C  CZ  . ARG B 1 17  ? 10.39500  12.51600  40.57400  1.000 97.90591  ? 17  ARG BA CZ  1 
ATOM   2366 N  NH1 . ARG B 1 17  ? 9.96800   12.39000  39.32800  1.000 69.60121  ? 17  ARG BA NH1 1 
ATOM   2367 N  NH2 . ARG B 1 17  ? 10.76100  13.71500  41.01900  1.000 91.36724  ? 17  ARG BA NH2 1 
ATOM   2368 N  N   . ALA B 1 18  ? 11.68600  8.16600   38.05300  1.000 19.19847  ? 18  ALA BA N   1 
ATOM   2369 C  CA  . ALA B 1 18  ? 10.87900  8.27200   36.84400  1.000 17.49663  ? 18  ALA BA CA  1 
ATOM   2370 C  C   . ALA B 1 18  ? 10.97100  7.03200   35.96700  1.000 16.90144  ? 18  ALA BA C   1 
ATOM   2371 O  O   . ALA B 1 18  ? 10.14400  6.87000   35.06100  1.000 14.97162  ? 18  ALA BA O   1 
ATOM   2372 C  CB  . ALA B 1 18  ? 11.29800  9.50500   36.04000  1.000 14.57186  ? 18  ALA BA CB  1 
ATOM   2373 N  N   A MET B 1 19  ? 11.95000  6.15900   36.21600  0.518 12.11487  ? 19  MET BA N   1 
ATOM   2374 N  N   B MET B 1 19  ? 11.95300  6.16200   36.21600  0.482 12.13288  ? 19  MET BA N   1 
ATOM   2375 C  CA  A MET B 1 19  ? 12.16500  4.93400   35.44300  0.518 14.60748  ? 19  MET BA CA  1 
ATOM   2376 C  CA  B MET B 1 19  ? 12.17300  4.93600   35.44900  0.482 14.60426  ? 19  MET BA CA  1 
ATOM   2377 C  C   A MET B 1 19  ? 12.45700  5.26300   33.97500  0.518 14.23484  ? 19  MET BA C   1 
ATOM   2378 C  C   B MET B 1 19  ? 12.46000  5.25900   33.97800  0.482 14.22797  ? 19  MET BA C   1 
ATOM   2379 O  O   A MET B 1 19  ? 11.69400  4.94600   33.06000  0.518 11.36126  ? 19  MET BA O   1 
ATOM   2380 O  O   B MET B 1 19  ? 11.69600  4.93500   33.06600  0.482 11.38705  ? 19  MET BA O   1 
ATOM   2381 C  CB  A MET B 1 19  ? 10.97000  3.98100   35.57700  0.518 12.68661  ? 19  MET BA CB  1 
ATOM   2382 C  CB  B MET B 1 19  ? 10.98400  3.97800   35.59400  0.482 12.70745  ? 19  MET BA CB  1 
ATOM   2383 C  CG  A MET B 1 19  ? 10.70100  3.51900   37.00000  0.518 15.77967  ? 19  MET BA CG  1 
ATOM   2384 C  CG  B MET B 1 19  ? 10.67100  3.59900   37.03200  0.482 15.79053  ? 19  MET BA CG  1 
ATOM   2385 S  SD  A MET B 1 19  ? 12.01500  2.47100   37.64800  0.518 21.48490  ? 19  MET BA SD  1 
ATOM   2386 S  SD  B MET B 1 19  ? 9.47500   2.25700   37.14700  0.482 20.18479  ? 19  MET BA SD  1 
ATOM   2387 C  CE  A MET B 1 19  ? 11.73700  0.97000   36.71200  0.518 17.63543  ? 19  MET BA CE  1 
ATOM   2388 C  CE  B MET B 1 19  ? 10.50300  0.85000   36.73200  0.482 18.17809  ? 19  MET BA CE  1 
ATOM   2389 N  N   . THR B 1 20  ? 13.60000  5.91700   33.78200  1.000 12.49380  ? 20  THR BA N   1 
ATOM   2390 C  CA  . THR B 1 20  ? 14.08600  6.25100   32.44900  1.000 10.16248  ? 20  THR BA CA  1 
ATOM   2391 C  C   . THR B 1 20  ? 15.56900  6.56900   32.55700  1.000 14.36188  ? 20  THR BA C   1 
ATOM   2392 O  O   . THR B 1 20  ? 16.12100  6.68900   33.65300  1.000 11.14858  ? 20  THR BA O   1 
ATOM   2393 C  CB  . THR B 1 20  ? 13.31800  7.42700   31.83200  1.000 12.05643  ? 20  THR BA CB  1 
ATOM   2394 O  OG1 . THR B 1 20  ? 13.58100  7.48000   30.42300  1.000 13.93850  ? 20  THR BA OG1 1 
ATOM   2395 C  CG2 . THR B 1 20  ? 13.74200  8.74300   32.47000  1.000 9.30241   ? 20  THR BA CG2 1 
ATOM   2396 N  N   . GLY B 1 21  ? 16.20900  6.70200   31.40300  1.000 10.79501  ? 21  GLY BA N   1 
ATOM   2397 C  CA  . GLY B 1 21  ? 17.62100  7.01900   31.37300  1.000 10.02949  ? 21  GLY BA CA  1 
ATOM   2398 C  C   . GLY B 1 21  ? 18.17400  6.86800   29.97400  1.000 15.61893  ? 21  GLY BA C   1 
ATOM   2399 O  O   . GLY B 1 21  ? 17.44500  6.61000   29.01100  1.000 10.58567  ? 21  GLY BA O   1 
ATOM   2400 N  N   . CYS B 1 22  ? 19.49200  7.03800   29.88000  1.000 10.26851  ? 22  CYS BA N   1 
ATOM   2401 C  CA  . CYS B 1 22  ? 20.17800  6.92300   28.60300  1.000 7.74056   ? 22  CYS BA CA  1 
ATOM   2402 C  C   . CYS B 1 22  ? 21.58600  6.39400   28.83200  1.000 10.97957  ? 22  CYS BA C   1 
ATOM   2403 O  O   . CYS B 1 22  ? 22.14100  6.48800   29.93100  1.000 11.26307  ? 22  CYS BA O   1 
ATOM   2404 C  CB  . CYS B 1 22  ? 20.22100  8.26300   27.85700  1.000 9.53423   ? 22  CYS BA CB  1 
ATOM   2405 S  SG  . CYS B 1 22  ? 21.00400  9.61600   28.76100  1.000 15.51765  ? 22  CYS BA SG  1 
ATOM   2406 N  N   . THR B 1 23  ? 22.15500  5.83100   27.77000  1.000 8.72302   ? 23  THR BA N   1 
ATOM   2407 C  CA  . THR B 1 23  ? 23.49200  5.25700   27.79600  1.000 7.10275   ? 23  THR BA CA  1 
ATOM   2408 C  C   . THR B 1 23  ? 24.21500  5.67600   26.52700  1.000 12.64544  ? 23  THR BA C   1 
ATOM   2409 O  O   . THR B 1 23  ? 23.64200  5.59900   25.43600  1.000 9.93421   ? 23  THR BA O   1 
ATOM   2410 C  CB  . THR B 1 23  ? 23.43700  3.72800   27.89300  1.000 7.37564   ? 23  THR BA CB  1 
ATOM   2411 O  OG1 . THR B 1 23  ? 22.72000  3.34700   29.07400  1.000 5.67785   ? 23  THR BA OG1 1 
ATOM   2412 C  CG2 . THR B 1 23  ? 24.84000  3.14200   27.94200  1.000 7.61684   ? 23  THR BA CG2 1 
ATOM   2413 N  N   . ILE B 1 24  ? 25.46000  6.12400   26.66300  1.000 5.14735   ? 24  ILE BA N   1 
ATOM   2414 C  CA  . ILE B 1 24  ? 26.26500  6.53000   25.51900  1.000 6.58547   ? 24  ILE BA CA  1 
ATOM   2415 C  C   . ILE B 1 24  ? 27.55600  5.72500   25.51400  1.000 8.18179   ? 24  ILE BA C   1 
ATOM   2416 O  O   . ILE B 1 24  ? 28.14000  5.45200   26.56800  1.000 5.04448   ? 24  ILE BA O   1 
ATOM   2417 C  CB  . ILE B 1 24  ? 26.56000  8.04600   25.52100  1.000 6.85365   ? 24  ILE BA CB  1 
ATOM   2418 C  CG1 . ILE B 1 24  ? 27.24500  8.45600   24.21400  1.000 6.97376   ? 24  ILE BA CG1 1 
ATOM   2419 C  CG2 . ILE B 1 24  ? 27.41300  8.44500   26.72200  1.000 9.41878   ? 24  ILE BA CG2 1 
ATOM   2420 C  CD1 . ILE B 1 24  ? 27.13900  9.93500   23.89900  1.000 13.52949  ? 24  ILE BA CD1 1 
ATOM   2421 N  N   . ALA B 1 25  ? 27.98000  5.32500   24.32000  1.000 7.53975   ? 25  ALA BA N   1 
ATOM   2422 C  CA  . ALA B 1 25  ? 29.29600  4.74600   24.09400  1.000 10.33958  ? 25  ALA BA CA  1 
ATOM   2423 C  C   . ALA B 1 25  ? 30.14200  5.79300   23.38300  1.000 8.44779   ? 25  ALA BA C   1 
ATOM   2424 O  O   . ALA B 1 25  ? 29.77500  6.25400   22.29800  1.000 12.35655  ? 25  ALA BA O   1 
ATOM   2425 C  CB  . ALA B 1 25  ? 29.20300  3.46400   23.26800  1.000 8.53541   ? 25  ALA BA CB  1 
ATOM   2426 N  N   . VAL B 1 26  ? 31.25200  6.17900   24.00000  1.000 12.31546  ? 26  VAL BA N   1 
ATOM   2427 C  CA  . VAL B 1 26  ? 32.13900  7.20300   23.45900  1.000 7.06797   ? 26  VAL BA CA  1 
ATOM   2428 C  C   . VAL B 1 26  ? 33.33100  6.52100   22.80700  1.000 13.21623  ? 26  VAL BA C   1 
ATOM   2429 O  O   . VAL B 1 26  ? 33.90000  5.57200   23.36100  1.000 12.03808  ? 26  VAL BA O   1 
ATOM   2430 C  CB  . VAL B 1 26  ? 32.59100  8.18500   24.55700  1.000 19.51067  ? 26  VAL BA CB  1 
ATOM   2431 C  CG1 . VAL B 1 26  ? 33.44800  9.29700   23.96300  1.000 11.07315  ? 26  VAL BA CG1 1 
ATOM   2432 C  CG2 . VAL B 1 26  ? 31.38000  8.76300   25.27400  1.000 9.36386   ? 26  VAL BA CG2 1 
ATOM   2433 N  N   . PHE B 1 27  ? 33.71000  7.00100   21.62500  1.000 5.57206   ? 27  PHE BA N   1 
ATOM   2434 C  CA  . PHE B 1 27  ? 34.79600  6.41700   20.84200  1.000 17.81632  ? 27  PHE BA CA  1 
ATOM   2435 C  C   . PHE B 1 27  ? 35.99300  7.36000   20.89300  1.000 12.77984  ? 27  PHE BA C   1 
ATOM   2436 O  O   . PHE B 1 27  ? 36.01500  8.38800   20.21100  1.000 21.87504  ? 27  PHE BA O   1 
ATOM   2437 C  CB  . PHE B 1 27  ? 34.34600  6.15400   19.40800  1.000 11.79906  ? 27  PHE BA CB  1 
ATOM   2438 C  CG  . PHE B 1 27  ? 33.12100  5.29300   19.31000  1.000 16.95821  ? 27  PHE BA CG  1 
ATOM   2439 C  CD1 . PHE B 1 27  ? 33.19600  3.93200   19.55700  1.000 21.13945  ? 27  PHE BA CD1 1 
ATOM   2440 C  CD2 . PHE B 1 27  ? 31.89400  5.84400   18.98400  1.000 14.98698  ? 27  PHE BA CD2 1 
ATOM   2441 C  CE1 . PHE B 1 27  ? 32.07100  3.13500   19.47400  1.000 12.75053  ? 27  PHE BA CE1 1 
ATOM   2442 C  CE2 . PHE B 1 27  ? 30.76500  5.05100   18.90000  1.000 18.35390  ? 27  PHE BA CE2 1 
ATOM   2443 C  CZ  . PHE B 1 27  ? 30.85500  3.69500   19.14600  1.000 11.66926  ? 27  PHE BA CZ  1 
ATOM   2444 N  N   . ASP B 1 28  ? 36.98500  7.00600   21.71100  1.000 19.53015  ? 28  ASP BA N   1 
ATOM   2445 C  CA  . ASP B 1 28  ? 38.21700  7.78000   21.77800  1.000 21.19067  ? 28  ASP BA CA  1 
ATOM   2446 C  C   . ASP B 1 28  ? 39.12100  7.53100   20.58100  1.000 17.79208  ? 28  ASP BA C   1 
ATOM   2447 O  O   . ASP B 1 28  ? 40.06100  8.30100   20.35800  1.000 23.58974  ? 28  ASP BA O   1 
ATOM   2448 C  CB  . ASP B 1 28  ? 38.96600  7.46300   23.07300  1.000 12.40702  ? 28  ASP BA CB  1 
ATOM   2449 C  CG  . ASP B 1 28  ? 38.32500  8.10700   24.28600  1.000 15.71047  ? 28  ASP BA CG  1 
ATOM   2450 O  OD1 . ASP B 1 28  ? 37.60600  9.11400   24.11300  1.000 15.26913  ? 28  ASP BA OD1 1 
ATOM   2451 O  OD2 . ASP B 1 28  ? 38.53300  7.60600   25.41000  1.000 18.72630  ? 28  ASP BA OD2 1 
ATOM   2452 N  N   . GLU B 1 29  ? 38.85900  6.47300   19.81300  1.000 17.62747  ? 29  GLU BA N   1 
ATOM   2453 C  CA  . GLU B 1 29  ? 39.54400  6.18400   18.56900  1.000 27.64700  ? 29  GLU BA CA  1 
ATOM   2454 C  C   . GLU B 1 29  ? 38.55400  6.23600   17.41200  1.000 24.95834  ? 29  GLU BA C   1 
ATOM   2455 O  O   . GLU B 1 29  ? 37.42200  5.76000   17.54900  1.000 22.42495  ? 29  GLU BA O   1 
ATOM   2456 C  CB  . GLU B 1 29  ? 40.21400  4.80300   18.61300  1.000 16.41748  ? 29  GLU BA CB  1 
ATOM   2457 C  CG  . GLU B 1 29  ? 40.92700  4.50900   19.92200  1.000 32.49127  ? 29  GLU BA CG  1 
ATOM   2458 C  CD  . GLU B 1 29  ? 42.38700  4.16200   19.72500  1.000 54.64620  ? 29  GLU BA CD  1 
ATOM   2459 O  OE1 . GLU B 1 29  ? 43.06600  4.87600   18.95700  1.000 38.85980  ? 29  GLU BA OE1 1 
ATOM   2460 O  OE2 . GLU B 1 29  ? 42.85400  3.18000   20.34100  1.000 36.92010  ? 29  GLU BA OE2 1 
ATOM   2461 N  N   . PRO B 1 30  ? 38.94200  6.81300   16.27400  1.000 30.08134  ? 30  PRO BA N   1 
ATOM   2462 C  CA  . PRO B 1 30  ? 37.99800  6.94600   15.15500  1.000 20.66900  ? 30  PRO BA CA  1 
ATOM   2463 C  C   . PRO B 1 30  ? 37.46600  5.59100   14.70800  1.000 16.59276  ? 30  PRO BA C   1 
ATOM   2464 O  O   . PRO B 1 30  ? 38.20200  4.60500   14.63600  1.000 16.51034  ? 30  PRO BA O   1 
ATOM   2465 C  CB  . PRO B 1 30  ? 38.83400  7.61700   14.05700  1.000 20.17536  ? 30  PRO BA CB  1 
ATOM   2466 C  CG  . PRO B 1 30  ? 40.26100  7.47100   14.48500  1.000 16.69890  ? 30  PRO BA CG  1 
ATOM   2467 C  CD  . PRO B 1 30  ? 40.26000  7.39400   15.97300  1.000 14.91108  ? 30  PRO BA CD  1 
ATOM   2468 N  N   . VAL B 1 31  ? 36.16700  5.55100   14.41100  1.000 12.71898  ? 31  VAL BA N   1 
ATOM   2469 C  CA  . VAL B 1 31  ? 35.48600  4.30800   14.07700  1.000 10.61378  ? 31  VAL BA CA  1 
ATOM   2470 C  C   . VAL B 1 31  ? 34.85100  4.42100   12.69600  1.000 16.63197  ? 31  VAL BA C   1 
ATOM   2471 O  O   . VAL B 1 31  ? 34.65400  5.51300   12.15500  1.000 8.48688   ? 31  VAL BA O   1 
ATOM   2472 C  CB  . VAL B 1 31  ? 34.42000  3.92800   15.12600  1.000 18.30412  ? 31  VAL BA CB  1 
ATOM   2473 C  CG1 . VAL B 1 31  ? 35.07700  3.56600   16.45200  1.000 18.38279  ? 31  VAL BA CG1 1 
ATOM   2474 C  CG2 . VAL B 1 31  ? 33.41800  5.06100   15.30500  1.000 16.45380  ? 31  VAL BA CG2 1 
ATOM   2475 N  N   . VAL B 1 32  ? 34.53100  3.26400   12.13100  1.000 14.22658  ? 32  VAL BA N   1 
ATOM   2476 C  CA  . VAL B 1 32  ? 33.79700  3.13600   10.87500  1.000 8.24162   ? 32  VAL BA CA  1 
ATOM   2477 C  C   . VAL B 1 32  ? 32.39200  2.64700   11.21200  1.000 11.40845  ? 32  VAL BA C   1 
ATOM   2478 O  O   . VAL B 1 32  ? 32.24100  1.52900   11.72200  1.000 10.82742  ? 32  VAL BA O   1 
ATOM   2479 C  CB  . VAL B 1 32  ? 34.49800  2.17500   9.90200   1.000 10.71792  ? 32  VAL BA CB  1 
ATOM   2480 C  CG1 . VAL B 1 32  ? 33.63800  1.94800   8.66900   1.000 10.49228  ? 32  VAL BA CG1 1 
ATOM   2481 C  CG2 . VAL B 1 32  ? 35.86500  2.71700   9.51000   1.000 13.24395  ? 32  VAL BA CG2 1 
ATOM   2482 N  N   . PRO B 1 33  ? 31.34700  3.43400   10.95900  1.000 9.22830   ? 33  PRO BA N   1 
ATOM   2483 C  CA  . PRO B 1 33  ? 30.01700  3.07200   11.46200  1.000 10.36573  ? 33  PRO BA CA  1 
ATOM   2484 C  C   . PRO B 1 33  ? 29.10800  2.42200   10.43000  1.000 13.82594  ? 33  PRO BA C   1 
ATOM   2485 O  O   . PRO B 1 33  ? 29.27400  2.60900   9.22000   1.000 12.05861  ? 33  PRO BA O   1 
ATOM   2486 C  CB  . PRO B 1 33  ? 29.45600  4.42500   11.91000  1.000 8.46159   ? 33  PRO BA CB  1 
ATOM   2487 C  CG  . PRO B 1 33  ? 30.04300  5.39200   10.90300  1.000 11.13936  ? 33  PRO BA CG  1 
ATOM   2488 C  CD  . PRO B 1 33  ? 31.36700  4.80600   10.42000  1.000 8.90159   ? 33  PRO BA CD  1 
ATOM   2489 N  N   . GLY B 1 34  ? 28.13100  1.65600   10.92000  1.000 8.07218   ? 34  GLY BA N   1 
ATOM   2490 C  CA  . GLY B 1 34  ? 27.09300  1.07400   10.09200  1.000 6.76621   ? 34  GLY BA CA  1 
ATOM   2491 C  C   . GLY B 1 34  ? 25.82100  0.96300   10.90500  1.000 12.31205  ? 34  GLY BA C   1 
ATOM   2492 O  O   . GLY B 1 34  ? 25.83400  1.09400   12.13100  1.000 8.09918   ? 34  GLY BA O   1 
ATOM   2493 N  N   . VAL B 1 35  ? 24.71000  0.71800   10.21100  1.000 3.59786   ? 35  VAL BA N   1 
ATOM   2494 C  CA  . VAL B 1 35  ? 23.40700  0.69200   10.86600  1.000 13.97085  ? 35  VAL BA CA  1 
ATOM   2495 C  C   . VAL B 1 35  ? 22.44900  -0.18100  10.06600  1.000 8.45459   ? 35  VAL BA C   1 
ATOM   2496 O  O   . VAL B 1 35  ? 22.57200  -0.32300  8.84600   1.000 11.65947  ? 35  VAL BA O   1 
ATOM   2497 C  CB  . VAL B 1 35  ? 22.84400  2.12500   11.05100  1.000 12.76664  ? 35  VAL BA CB  1 
ATOM   2498 C  CG1 . VAL B 1 35  ? 22.24300  2.65000   9.75400   1.000 7.50153   ? 35  VAL BA CG1 1 
ATOM   2499 C  CG2 . VAL B 1 35  ? 21.82200  2.16000   12.18000  1.000 4.99302   ? 35  VAL BA CG2 1 
ATOM   2500 N  N   . ASP B 1 36  ? 21.49600  -0.78300  10.77700  1.000 6.89003   ? 36  ASP BA N   1 
ATOM   2501 C  CA  . ASP B 1 36  ? 20.40500  -1.54200  10.17000  1.000 8.86332   ? 36  ASP BA CA  1 
ATOM   2502 C  C   . ASP B 1 36  ? 19.17100  -1.33600  11.03500  1.000 9.09385   ? 36  ASP BA C   1 
ATOM   2503 O  O   . ASP B 1 36  ? 19.09700  -1.86400  12.14900  1.000 7.77862   ? 36  ASP BA O   1 
ATOM   2504 C  CB  . ASP B 1 36  ? 20.74600  -3.03000  10.04900  1.000 5.08224   ? 36  ASP BA CB  1 
ATOM   2505 C  CG  . ASP B 1 36  ? 19.70200  -3.81200  9.25100   1.000 15.24254  ? 36  ASP BA CG  1 
ATOM   2506 O  OD1 . ASP B 1 36  ? 18.49300  -3.69000  9.54000   1.000 16.69065  ? 36  ASP BA OD1 1 
ATOM   2507 O  OD2 . ASP B 1 36  ? 20.09200  -4.55700  8.33100   1.000 20.28406  ? 36  ASP BA OD2 1 
ATOM   2508 N  N   . VAL B 1 37  ? 18.20800  -0.57500  10.52600  1.000 6.12222   ? 37  VAL BA N   1 
ATOM   2509 C  CA  . VAL B 1 37  ? 16.94000  -0.33400  11.20600  1.000 5.40563   ? 37  VAL BA CA  1 
ATOM   2510 C  C   . VAL B 1 37  ? 15.93500  -1.34200  10.66500  1.000 10.84599  ? 37  VAL BA C   1 
ATOM   2511 O  O   . VAL B 1 37  ? 15.46800  -1.21800  9.52800   1.000 13.60084  ? 37  VAL BA O   1 
ATOM   2512 C  CB  . VAL B 1 37  ? 16.45400  1.10600   11.00100  1.000 5.68554   ? 37  VAL BA CB  1 
ATOM   2513 C  CG1 . VAL B 1 37  ? 15.18400  1.35000   11.79200  1.000 5.21726   ? 37  VAL BA CG1 1 
ATOM   2514 C  CG2 . VAL B 1 37  ? 17.53700  2.09800   11.40300  1.000 6.35213   ? 37  VAL BA CG2 1 
ATOM   2515 N  N   . ARG B 1 38  ? 15.60100  -2.34600  11.47500  1.000 14.79318  ? 38  ARG BA N   1 
ATOM   2516 C  CA  . ARG B 1 38  ? 14.70700  -3.41700  11.05200  1.000 12.88093  ? 38  ARG BA CA  1 
ATOM   2517 C  C   . ARG B 1 38  ? 13.29500  -3.28300  11.60500  1.000 17.50443  ? 38  ARG BA C   1 
ATOM   2518 O  O   . ARG B 1 38  ? 12.35200  -3.78500  10.98400  1.000 13.99765  ? 38  ARG BA O   1 
ATOM   2519 C  CB  . ARG B 1 38  ? 15.28000  -4.77800  11.46600  1.000 11.90454  ? 38  ARG BA CB  1 
ATOM   2520 C  CG  . ARG B 1 38  ? 14.68400  -5.96300  10.71800  1.000 12.27079  ? 38  ARG BA CG  1 
ATOM   2521 C  CD  . ARG B 1 38  ? 15.20700  -6.04700  9.28900   1.000 15.38830  ? 38  ARG BA CD  1 
ATOM   2522 N  NE  . ARG B 1 38  ? 16.65600  -6.20400  9.23900   1.000 10.80844  ? 38  ARG BA NE  1 
ATOM   2523 C  CZ  . ARG B 1 38  ? 17.29000  -7.36000  9.38500   1.000 18.64017  ? 38  ARG BA CZ  1 
ATOM   2524 N  NH1 . ARG B 1 38  ? 16.63000  -8.48900  9.59100   1.000 14.07882  ? 38  ARG BA NH1 1 
ATOM   2525 N  NH2 . ARG B 1 38  ? 18.61900  -7.38500  9.32200   1.000 15.56211  ? 38  ARG BA NH2 1 
ATOM   2526 N  N   . GLY B 1 39  ? 13.12400  -2.62800  12.75100  1.000 11.36709  ? 39  GLY BA N   1 
ATOM   2527 C  CA  . GLY B 1 39  ? 11.79700  -2.47200  13.31400  1.000 12.17150  ? 39  GLY BA CA  1 
ATOM   2528 C  C   . GLY B 1 39  ? 10.93800  -1.53000  12.49200  1.000 14.91111  ? 39  GLY BA C   1 
ATOM   2529 O  O   . GLY B 1 39  ? 11.42900  -0.63400  11.80600  1.000 8.90335   ? 39  GLY BA O   1 
ATOM   2530 N  N   . ALA B 1 40  ? 9.62600   -1.74200  12.56500  1.000 9.96484   ? 40  ALA BA N   1 
ATOM   2531 C  CA  . ALA B 1 40  ? 8.67100   -0.94000  11.81200  1.000 14.37618  ? 40  ALA BA CA  1 
ATOM   2532 C  C   . ALA B 1 40  ? 8.23300   0.31900   12.55000  1.000 11.54905  ? 40  ALA BA C   1 
ATOM   2533 O  O   . ALA B 1 40  ? 7.42100   1.08100   12.01500  1.000 17.32087  ? 40  ALA BA O   1 
ATOM   2534 C  CB  . ALA B 1 40  ? 7.43900   -1.78200  11.46000  1.000 13.16625  ? 40  ALA BA CB  1 
ATOM   2535 N  N   . ASN B 1 41  ? 8.75100   0.56000   13.75500  1.000 10.31389  ? 41  ASN BA N   1 
ATOM   2536 C  CA  . ASN B 1 41  ? 8.33300   1.68900   14.57800  1.000 12.32414  ? 41  ASN BA CA  1 
ATOM   2537 C  C   . ASN B 1 41  ? 9.54900   2.28100   15.29400  1.000 14.68738  ? 41  ASN BA C   1 
ATOM   2538 O  O   . ASN B 1 41  ? 9.61300   2.36200   16.51700  1.000 15.46748  ? 41  ASN BA O   1 
ATOM   2539 C  CB  . ASN B 1 41  ? 7.25800   1.25700   15.57400  1.000 11.82854  ? 41  ASN BA CB  1 
ATOM   2540 C  CG  . ASN B 1 41  ? 6.34900   2.39900   15.98700  1.000 23.93423  ? 41  ASN BA CG  1 
ATOM   2541 O  OD1 . ASN B 1 41  ? 6.72500   3.56800   15.90200  1.000 18.67523  ? 41  ASN BA OD1 1 
ATOM   2542 N  ND2 . ASN B 1 41  ? 5.14600   2.06400   16.43900  1.000 34.72665  ? 41  ASN BA ND2 1 
ATOM   2543 N  N   . ALA B 1 42  ? 10.53700  2.71200   14.51700  1.000 12.53072  ? 42  ALA BA N   1 
ATOM   2544 C  CA  . ALA B 1 42  ? 11.78900  3.21100   15.06300  1.000 10.51266  ? 42  ALA BA CA  1 
ATOM   2545 C  C   . ALA B 1 42  ? 11.84500  4.73200   15.00800  1.000 8.57870   ? 42  ALA BA C   1 
ATOM   2546 O  O   . ALA B 1 42  ? 11.28800  5.36200   14.10700  1.000 20.77602  ? 42  ALA BA O   1 
ATOM   2547 C  CB  . ALA B 1 42  ? 12.98300  2.62400   14.30900  1.000 7.62628   ? 42  ALA BA CB  1 
ATOM   2548 N  N   . ALA B 1 43  ? 12.52900  5.31500   15.99100  1.000 9.21120   ? 43  ALA BA N   1 
ATOM   2549 C  CA  . ALA B 1 43  ? 12.80400  6.74800   16.03300  1.000 6.60411   ? 43  ALA BA CA  1 
ATOM   2550 C  C   . ALA B 1 43  ? 14.29800  6.91800   16.26300  1.000 8.86454   ? 43  ALA BA C   1 
ATOM   2551 O  O   . ALA B 1 43  ? 14.80900  6.54300   17.32300  1.000 7.84005   ? 43  ALA BA O   1 
ATOM   2552 C  CB  . ALA B 1 43  ? 11.99500  7.44100   17.12900  1.000 2.20063   ? 43  ALA BA CB  1 
ATOM   2553 N  N   . THR B 1 44  ? 14.99900  7.46100   15.27000  1.000 13.18673  ? 44  THR BA N   1 
ATOM   2554 C  CA  . THR B 1 44  ? 16.44900  7.59700   15.31400  1.000 9.99762   ? 44  THR BA CA  1 
ATOM   2555 C  C   . THR B 1 44  ? 16.84900  9.00300   14.88000  1.000 8.76412   ? 44  THR BA C   1 
ATOM   2556 O  O   . THR B 1 44  ? 16.01300  9.82600   14.49100  1.000 5.09538   ? 44  THR BA O   1 
ATOM   2557 C  CB  . THR B 1 44  ? 17.14300  6.55800   14.42100  1.000 7.68823   ? 44  THR BA CB  1 
ATOM   2558 O  OG1 . THR B 1 44  ? 16.91500  6.88500   13.04600  1.000 8.45381   ? 44  THR BA OG1 1 
ATOM   2559 C  CG2 . THR B 1 44  ? 16.62700  5.15000   14.70200  1.000 5.72247   ? 44  THR BA CG2 1 
ATOM   2560 N  N   . ILE B 1 45  ? 18.15100  9.26800   14.93700  1.000 9.51110   ? 45  ILE BA N   1 
ATOM   2561 C  CA  . ILE B 1 45  ? 18.71500  10.54100  14.50000  1.000 8.87877   ? 45  ILE BA CA  1 
ATOM   2562 C  C   . ILE B 1 45  ? 20.12300  10.28300  13.97800  1.000 7.02876   ? 45  ILE BA C   1 
ATOM   2563 O  O   . ILE B 1 45  ? 20.83800  9.41600   14.49000  1.000 8.08110   ? 45  ILE BA O   1 
ATOM   2564 C  CB  . ILE B 1 45  ? 18.70100  11.58000  15.64600  1.000 8.64307   ? 45  ILE BA CB  1 
ATOM   2565 C  CG1 . ILE B 1 45  ? 19.12700  12.96100  15.13900  1.000 6.82301   ? 45  ILE BA CG1 1 
ATOM   2566 C  CG2 . ILE B 1 45  ? 19.57500  11.12000  16.81100  1.000 5.11358   ? 45  ILE BA CG2 1 
ATOM   2567 C  CD1 . ILE B 1 45  ? 19.24100  14.00500  16.23500  1.000 12.50164  ? 45  ILE BA CD1 1 
ATOM   2568 N  N   . TYR B 1 46  ? 20.50200  11.01900  12.92900  1.000 7.10158   ? 46  TYR BA N   1 
ATOM   2569 C  CA  . TYR B 1 46  ? 21.82900  10.97500  12.31100  1.000 7.04993   ? 46  TYR BA CA  1 
ATOM   2570 C  C   . TYR B 1 46  ? 22.14800  9.64300   11.63800  1.000 13.95950  ? 46  TYR BA C   1 
ATOM   2571 O  O   . TYR B 1 46  ? 23.32500  9.32900   11.43200  1.000 19.12245  ? 46  TYR BA O   1 
ATOM   2572 C  CB  . TYR B 1 46  ? 22.94200  11.29500  13.31900  1.000 5.12003   ? 46  TYR BA CB  1 
ATOM   2573 C  CG  . TYR B 1 46  ? 22.84300  12.64600  13.98800  1.000 15.09703  ? 46  TYR BA CG  1 
ATOM   2574 C  CD1 . TYR B 1 46  ? 22.64200  13.80300  13.24500  1.000 9.48882   ? 46  TYR BA CD1 1 
ATOM   2575 C  CD2 . TYR B 1 46  ? 22.96800  12.76500  15.36600  1.000 13.60658  ? 46  TYR BA CD2 1 
ATOM   2576 C  CE1 . TYR B 1 46  ? 22.56000  15.03900  13.85900  1.000 9.78195   ? 46  TYR BA CE1 1 
ATOM   2577 C  CE2 . TYR B 1 46  ? 22.88600  13.99500  15.98900  1.000 12.48868  ? 46  TYR BA CE2 1 
ATOM   2578 C  CZ  . TYR B 1 46  ? 22.68200  15.12800  15.23100  1.000 14.06784  ? 46  TYR BA CZ  1 
ATOM   2579 O  OH  . TYR B 1 46  ? 22.60000  16.35200  15.85200  1.000 8.25624   ? 46  TYR BA OH  1 
ATOM   2580 N  N   . THR B 1 47  ? 21.14500  8.84000   11.27500  1.000 6.71406   ? 47  THR BA N   1 
ATOM   2581 C  CA  . THR B 1 47  ? 21.44900  7.53000   10.70600  1.000 11.05375  ? 47  THR BA CA  1 
ATOM   2582 C  C   . THR B 1 47  ? 21.79900  7.58300   9.22300   1.000 11.76226  ? 47  THR BA C   1 
ATOM   2583 O  O   . THR B 1 47  ? 22.37700  6.61900   8.70900   1.000 10.86779  ? 47  THR BA O   1 
ATOM   2584 C  CB  . THR B 1 47  ? 20.28200  6.55900   10.90700  1.000 7.67457   ? 47  THR BA CB  1 
ATOM   2585 O  OG1 . THR B 1 47  ? 19.06700  7.15700   10.44200  1.000 13.44479  ? 47  THR BA OG1 1 
ATOM   2586 C  CG2 . THR B 1 47  ? 20.14200  6.18700   12.37600  1.000 10.33268  ? 47  THR BA CG2 1 
ATOM   2587 N  N   . ASP B 1 48  ? 21.47100  8.67500   8.52500   1.000 10.90934  ? 48  ASP BA N   1 
ATOM   2588 C  CA  . ASP B 1 48  ? 21.72700  8.73100   7.08800   1.000 14.63824  ? 48  ASP BA CA  1 
ATOM   2589 C  C   . ASP B 1 48  ? 23.21700  8.69000   6.77200   1.000 13.89018  ? 48  ASP BA C   1 
ATOM   2590 O  O   . ASP B 1 48  ? 23.61700  8.14500   5.73600   1.000 17.54748  ? 48  ASP BA O   1 
ATOM   2591 C  CB  . ASP B 1 48  ? 21.09400  9.98400   6.48600   1.000 12.93986  ? 48  ASP BA CB  1 
ATOM   2592 C  CG  . ASP B 1 48  ? 19.58400  9.90100   6.42800   1.000 22.04369  ? 48  ASP BA CG  1 
ATOM   2593 O  OD1 . ASP B 1 48  ? 19.06400  9.02100   5.70900   1.000 17.41588  ? 48  ASP BA OD1 1 
ATOM   2594 O  OD2 . ASP B 1 48  ? 18.91700  10.71300  7.10200   1.000 20.12843  ? 48  ASP BA OD2 1 
ATOM   2595 N  N   . LEU B 1 49  ? 24.05100  9.25700   7.64100   1.000 11.36750  ? 49  LEU BA N   1 
ATOM   2596 C  CA  . LEU B 1 49  ? 25.49500  9.22200   7.44600   1.000 15.81403  ? 49  LEU BA CA  1 
ATOM   2597 C  C   . LEU B 1 49  ? 26.10900  7.87400   7.80000   1.000 15.25060  ? 49  LEU BA C   1 
ATOM   2598 O  O   . LEU B 1 49  ? 27.31900  7.69700   7.62100   1.000 17.45937  ? 49  LEU BA O   1 
ATOM   2599 C  CB  . LEU B 1 49  ? 26.15900  10.32600  8.27200   1.000 18.04790  ? 49  LEU BA CB  1 
ATOM   2600 C  CG  . LEU B 1 49  ? 25.86700  11.75400  7.80900   1.000 25.43988  ? 49  LEU BA CG  1 
ATOM   2601 C  CD1 . LEU B 1 49  ? 25.63100  12.67300  8.99800   1.000 24.68752  ? 49  LEU BA CD1 1 
ATOM   2602 C  CD2 . LEU B 1 49  ? 27.00200  12.27200  6.94200   1.000 17.36055  ? 49  LEU BA CD2 1 
ATOM   2603 N  N   . LEU B 1 50  ? 25.31300  6.92500   8.28700   1.000 12.43918  ? 50  LEU BA N   1 
ATOM   2604 C  CA  . LEU B 1 50  ? 25.80400  5.61900   8.69900   1.000 19.86216  ? 50  LEU BA CA  1 
ATOM   2605 C  C   . LEU B 1 50  ? 25.63200  4.55900   7.61500   1.000 17.26101  ? 50  LEU BA C   1 
ATOM   2606 O  O   . LEU B 1 50  ? 25.89700  3.37900   7.86700   1.000 23.64674  ? 50  LEU BA O   1 
ATOM   2607 C  CB  . LEU B 1 50  ? 25.09800  5.17700   9.98400   1.000 7.87016   ? 50  LEU BA CB  1 
ATOM   2608 C  CG  . LEU B 1 50  ? 25.75500  5.51300   11.32800  1.000 18.69301  ? 50  LEU BA CG  1 
ATOM   2609 C  CD1 . LEU B 1 50  ? 26.37200  6.90600   11.32500  1.000 16.53933  ? 50  LEU BA CD1 1 
ATOM   2610 C  CD2 . LEU B 1 50  ? 24.74600  5.37900   12.45800  1.000 14.75421  ? 50  LEU BA CD2 1 
ATOM   2611 N  N   . TYR B 1 51  ? 25.20200  4.95100   6.42500   1.000 11.52306  ? 51  TYR BA N   1 
ATOM   2612 C  CA  . TYR B 1 51  ? 24.96800  4.04400   5.31400   1.000 13.81300  ? 51  TYR BA CA  1 
ATOM   2613 C  C   . TYR B 1 51  ? 26.15800  4.03700   4.36300   1.000 18.27955  ? 51  TYR BA C   1 
ATOM   2614 O  O   . TYR B 1 51  ? 26.93900  4.99200   4.31800   1.000 12.52945  ? 51  TYR BA O   1 
ATOM   2615 C  CB  . TYR B 1 51  ? 23.69300  4.45000   4.56700   1.000 12.57494  ? 51  TYR BA CB  1 
ATOM   2616 C  CG  . TYR B 1 51  ? 22.43000  4.13200   5.33600   1.000 18.16181  ? 51  TYR BA CG  1 
ATOM   2617 C  CD1 . TYR B 1 51  ? 21.96700  2.82600   5.44100   1.000 21.98308  ? 51  TYR BA CD1 1 
ATOM   2618 C  CD2 . TYR B 1 51  ? 21.70800  5.13500   5.96900   1.000 17.15332  ? 51  TYR BA CD2 1 
ATOM   2619 C  CE1 . TYR B 1 51  ? 20.81600  2.53000   6.14700   1.000 25.69574  ? 51  TYR BA CE1 1 
ATOM   2620 C  CE2 . TYR B 1 51  ? 20.55600  4.84800   6.67800   1.000 17.08743  ? 51  TYR BA CE2 1 
ATOM   2621 C  CZ  . TYR B 1 51  ? 20.11600  3.54500   6.76400   1.000 22.57744  ? 51  TYR BA CZ  1 
ATOM   2622 O  OH  . TYR B 1 51  ? 18.97000  3.25600   7.46800   1.000 19.80712  ? 51  TYR BA OH  1 
ATOM   2623 N  N   . PRO B 1 52  ? 26.33500  2.96000   3.58900   1.000 12.24386  ? 52  PRO BA N   1 
ATOM   2624 C  CA  . PRO B 1 52  ? 27.53500  2.86300   2.73900   1.000 15.41568  ? 52  PRO BA CA  1 
ATOM   2625 C  C   . PRO B 1 52  ? 27.61700  3.92300   1.65300   1.000 12.18074  ? 52  PRO BA C   1 
ATOM   2626 O  O   . PRO B 1 52  ? 28.72800  4.31600   1.27500   1.000 28.23814  ? 52  PRO BA O   1 
ATOM   2627 C  CB  . PRO B 1 52  ? 27.42600  1.45400   2.13800   1.000 18.26760  ? 52  PRO BA CB  1 
ATOM   2628 C  CG  . PRO B 1 52  ? 26.52900  0.70600   3.06500   1.000 16.83106  ? 52  PRO BA CG  1 
ATOM   2629 C  CD  . PRO B 1 52  ? 25.54900  1.71400   3.57500   1.000 20.83334  ? 52  PRO BA CD  1 
ATOM   2630 N  N   . ASP B 1 53  ? 26.48600  4.39700   1.13300   1.000 11.56932  ? 53  ASP BA N   1 
ATOM   2631 C  CA  . ASP B 1 53  ? 26.50500  5.39600   0.07100   1.000 25.65380  ? 53  ASP BA CA  1 
ATOM   2632 C  C   . ASP B 1 53  ? 26.69600  6.81600   0.59000   1.000 28.83417  ? 53  ASP BA C   1 
ATOM   2633 O  O   . ASP B 1 53  ? 26.72700  7.75200   -0.21500  1.000 30.79882  ? 53  ASP BA O   1 
ATOM   2634 C  CB  . ASP B 1 53  ? 25.21700  5.31600   -0.75300  1.000 14.63478  ? 53  ASP BA CB  1 
ATOM   2635 C  CG  . ASP B 1 53  ? 23.97200  5.36600   0.10700   1.000 24.16935  ? 53  ASP BA CG  1 
ATOM   2636 O  OD1 . ASP B 1 53  ? 24.01400  4.85000   1.24400   1.000 34.60870  ? 53  ASP BA OD1 1 
ATOM   2637 O  OD2 . ASP B 1 53  ? 22.95100  5.91600   -0.35500  1.000 57.16318  ? 53  ASP BA OD2 1 
ATOM   2638 N  N   . SER B 1 54  ? 26.82000  6.99700   1.90000   1.000 20.89462  ? 54  SER BA N   1 
ATOM   2639 C  CA  . SER B 1 54  ? 27.09200  8.29400   2.49800   1.000 14.31865  ? 54  SER BA CA  1 
ATOM   2640 C  C   . SER B 1 54  ? 28.59100  8.45500   2.72700   1.000 17.70905  ? 54  SER BA C   1 
ATOM   2641 O  O   . SER B 1 54  ? 29.35200  7.48400   2.71100   1.000 13.45791  ? 54  SER BA O   1 
ATOM   2642 C  CB  . SER B 1 54  ? 26.33200  8.45000   3.82000   1.000 11.50329  ? 54  SER BA CB  1 
ATOM   2643 O  OG  . SER B 1 54  ? 24.98500  8.83500   3.59300   1.000 26.21908  ? 54  SER BA OG  1 
ATOM   2644 N  N   . VAL B 1 55  ? 29.01000  9.70300   2.93500   1.000 9.11456   ? 55  VAL BA N   1 
ATOM   2645 C  CA  . VAL B 1 55  ? 30.41100  10.01100  3.21100   1.000 19.52641  ? 55  VAL BA CA  1 
ATOM   2646 C  C   . VAL B 1 55  ? 30.78500  9.47300   4.58600   1.000 22.17452  ? 55  VAL BA C   1 
ATOM   2647 O  O   . VAL B 1 55  ? 29.91100  9.13500   5.39500   1.000 15.61624  ? 55  VAL BA O   1 
ATOM   2648 C  CB  . VAL B 1 55  ? 30.68500  11.52500  3.12600   1.000 21.42449  ? 55  VAL BA CB  1 
ATOM   2649 C  CG1 . VAL B 1 55  ? 30.30100  12.06200  1.75600   1.000 22.88435  ? 55  VAL BA CG1 1 
ATOM   2650 C  CG2 . VAL B 1 55  ? 29.93800  12.26500  4.22200   1.000 22.86487  ? 55  VAL BA CG2 1 
ATOM   2651 N  N   . MET B 1 56  ? 32.08600  9.39100   4.86300   1.000 20.06672  ? 56  MET BA N   1 
ATOM   2652 C  CA  . MET B 1 56  ? 32.57000  8.92500   6.15700   1.000 15.48380  ? 56  MET BA CA  1 
ATOM   2653 C  C   . MET B 1 56  ? 32.40200  10.02200  7.20100   1.000 24.16978  ? 56  MET BA C   1 
ATOM   2654 O  O   . MET B 1 56  ? 33.07600  11.05700  7.13000   1.000 24.26912  ? 56  MET BA O   1 
ATOM   2655 C  CB  . MET B 1 56  ? 34.03500  8.49400   6.06000   1.000 13.16682  ? 56  MET BA CB  1 
ATOM   2656 C  CG  . MET B 1 56  ? 34.61600  7.94200   7.35200   1.000 25.70511  ? 56  MET BA CG  1 
ATOM   2657 S  SD  . MET B 1 56  ? 34.03300  6.27300   7.70500   1.000 23.32758  ? 56  MET BA SD  1 
ATOM   2658 C  CE  . MET B 1 56  ? 35.10400  5.31400   6.63400   1.000 27.73242  ? 56  MET BA CE  1 
ATOM   2659 N  N   . PRO B 1 57  ? 31.52100  9.83800   8.17800   1.000 22.53292  ? 57  PRO BA N   1 
ATOM   2660 C  CA  . PRO B 1 57  ? 31.32700  10.86300  9.20500   1.000 15.64041  ? 57  PRO BA CA  1 
ATOM   2661 C  C   . PRO B 1 57  ? 32.36300  10.73200  10.31400  1.000 12.26556  ? 57  PRO BA C   1 
ATOM   2662 O  O   . PRO B 1 57  ? 33.16900  9.80100   10.35200  1.000 13.34156  ? 57  PRO BA O   1 
ATOM   2663 C  CB  . PRO B 1 57  ? 29.91900  10.56700  9.72200   1.000 21.12667  ? 57  PRO BA CB  1 
ATOM   2664 C  CG  . PRO B 1 57  ? 29.78700  9.07600   9.57500   1.000 22.28312  ? 57  PRO BA CG  1 
ATOM   2665 C  CD  . PRO B 1 57  ? 30.67900  8.65200   8.42000   1.000 18.53833  ? 57  PRO BA CD  1 
ATOM   2666 N  N   . SER B 1 58  ? 32.32700  11.69600  11.22600  1.000 11.67198  ? 58  SER BA N   1 
ATOM   2667 C  CA  . SER B 1 58  ? 33.15900  11.68700  12.42600  1.000 16.24100  ? 58  SER BA CA  1 
ATOM   2668 C  C   . SER B 1 58  ? 32.23300  11.38900  13.60300  1.000 14.73214  ? 58  SER BA C   1 
ATOM   2669 O  O   . SER B 1 58  ? 31.72100  12.29800  14.25900  1.000 15.89543  ? 58  SER BA O   1 
ATOM   2670 C  CB  . SER B 1 58  ? 33.89600  13.01400  12.59900  1.000 19.29394  ? 58  SER BA CB  1 
ATOM   2671 O  OG  . SER B 1 58  ? 34.86100  12.92800  13.63200  1.000 36.02055  ? 58  SER BA OG  1 
ATOM   2672 N  N   . VAL B 1 59  ? 32.01200  10.10300  13.85900  1.000 12.26417  ? 59  VAL BA N   1 
ATOM   2673 C  CA  . VAL B 1 59  ? 31.06700  9.67100   14.88500  1.000 14.79012  ? 59  VAL BA CA  1 
ATOM   2674 C  C   . VAL B 1 59  ? 31.74100  9.79900   16.24700  1.000 14.73957  ? 59  VAL BA C   1 
ATOM   2675 O  O   . VAL B 1 59  ? 32.68300  9.06600   16.55800  1.000 14.56811  ? 59  VAL BA O   1 
ATOM   2676 C  CB  . VAL B 1 59  ? 30.58100  8.23900   14.63500  1.000 15.07694  ? 59  VAL BA CB  1 
ATOM   2677 C  CG1 . VAL B 1 59  ? 29.73700  7.75400   15.80300  1.000 5.55921   ? 59  VAL BA CG1 1 
ATOM   2678 C  CG2 . VAL B 1 59  ? 29.78900  8.17200   13.33600  1.000 11.36445  ? 59  VAL BA CG2 1 
ATOM   2679 N  N   . THR B 1 60  ? 31.25400  10.73600  17.06400  1.000 15.54514  ? 60  THR BA N   1 
ATOM   2680 C  CA  . THR B 1 60  ? 31.81900  10.95900  18.39100  1.000 9.84086   ? 60  THR BA CA  1 
ATOM   2681 C  C   . THR B 1 60  ? 31.31100  9.94200   19.40400  1.000 16.18882  ? 60  THR BA C   1 
ATOM   2682 O  O   . THR B 1 60  ? 32.05300  9.55200   20.31300  1.000 10.22742  ? 60  THR BA O   1 
ATOM   2683 C  CB  . THR B 1 60  ? 31.48600  12.37400  18.86800  1.000 17.00191  ? 60  THR BA CB  1 
ATOM   2684 O  OG1 . THR B 1 60  ? 31.30900  13.23000  17.73200  1.000 25.63652  ? 60  THR BA OG1 1 
ATOM   2685 C  CG2 . THR B 1 60  ? 32.60500  12.92500  19.73500  1.000 25.57843  ? 60  THR BA CG2 1 
ATOM   2686 N  N   . GLY B 1 61  ? 30.06300  9.51400   19.26700  1.000 10.26942  ? 61  GLY BA N   1 
ATOM   2687 C  CA  . GLY B 1 61  ? 29.49700  8.52400   20.16000  1.000 7.87037   ? 61  GLY BA CA  1 
ATOM   2688 C  C   . GLY B 1 61  ? 28.13200  8.10600   19.66800  1.000 13.69835  ? 61  GLY BA C   1 
ATOM   2689 O  O   . GLY B 1 61  ? 27.53900  8.75400   18.79900  1.000 10.34357  ? 61  GLY BA O   1 
ATOM   2690 N  N   . ILE B 1 62  ? 27.64300  7.00200   20.22600  1.000 5.00426   ? 62  ILE BA N   1 
ATOM   2691 C  CA  . ILE B 1 62  ? 26.31900  6.48100   19.91000  1.000 8.63745   ? 62  ILE BA CA  1 
ATOM   2692 C  C   . ILE B 1 62  ? 25.55800  6.28800   21.21300  1.000 10.21341  ? 62  ILE BA C   1 
ATOM   2693 O  O   . ILE B 1 62  ? 26.12000  5.81300   22.20700  1.000 8.60602   ? 62  ILE BA O   1 
ATOM   2694 C  CB  . ILE B 1 62  ? 26.39300  5.16200   19.11100  1.000 8.77801   ? 62  ILE BA CB  1 
ATOM   2695 C  CG1 . ILE B 1 62  ? 27.08600  5.39500   17.76700  1.000 7.64919   ? 62  ILE BA CG1 1 
ATOM   2696 C  CG2 . ILE B 1 62  ? 25.00300  4.59200   18.87900  1.000 7.95069   ? 62  ILE BA CG2 1 
ATOM   2697 C  CD1 . ILE B 1 62  ? 27.31700  4.12900   16.97300  1.000 18.61256  ? 62  ILE BA CD1 1 
ATOM   2698 N  N   . MET B 1 63  ? 24.28000  6.65900   21.21200  1.000 5.49398   ? 63  MET BA N   1 
ATOM   2699 C  CA  . MET B 1 63  ? 23.47700  6.68100   22.42300  1.000 9.05682   ? 63  MET BA CA  1 
ATOM   2700 C  C   . MET B 1 63  ? 22.24500  5.80000   22.27800  1.000 14.37577  ? 63  MET BA C   1 
ATOM   2701 O  O   . MET B 1 63  ? 21.57800  5.80700   21.23800  1.000 11.71830  ? 63  MET BA O   1 
ATOM   2702 C  CB  . MET B 1 63  ? 23.05800  8.11200   22.76500  1.000 3.01166   ? 63  MET BA CB  1 
ATOM   2703 C  CG  . MET B 1 63  ? 22.21100  8.23000   24.01500  1.000 15.68642  ? 63  MET BA CG  1 
ATOM   2704 S  SD  . MET B 1 63  ? 21.61900  9.90700   24.26500  1.000 19.09492  ? 63  MET BA SD  1 
ATOM   2705 C  CE  . MET B 1 63  ? 22.95800  10.57000  25.24700  1.000 6.03685   ? 63  MET BA CE  1 
ATOM   2706 N  N   . LEU B 1 64  ? 21.95700  5.03500   23.32500  1.000 12.26086  ? 64  LEU BA N   1 
ATOM   2707 C  CA  . LEU B 1 64  ? 20.70400  4.30600   23.46800  1.000 8.90206   ? 64  LEU BA CA  1 
ATOM   2708 C  C   . LEU B 1 64  ? 19.94200  4.94100   24.62300  1.000 17.32847  ? 64  LEU BA C   1 
ATOM   2709 O  O   . LEU B 1 64  ? 20.43000  4.94900   25.75800  1.000 11.10321  ? 64  LEU BA O   1 
ATOM   2710 C  CB  . LEU B 1 64  ? 20.95200  2.82100   23.72800  1.000 10.12512  ? 64  LEU BA CB  1 
ATOM   2711 C  CG  . LEU B 1 64  ? 22.03300  2.14600   22.88000  1.000 17.27983  ? 64  LEU BA CG  1 
ATOM   2712 C  CD1 . LEU B 1 64  ? 22.37200  0.77300   23.44100  1.000 8.89621   ? 64  LEU BA CD1 1 
ATOM   2713 C  CD2 . LEU B 1 64  ? 21.60200  2.04000   21.42500  1.000 4.66220   ? 64  LEU BA CD2 1 
ATOM   2714 N  N   . THR B 1 65  ? 18.75900  5.47800   24.33700  1.000 4.49512   ? 65  THR BA N   1 
ATOM   2715 C  CA  . THR B 1 65  ? 18.04300  6.29900   25.30100  1.000 11.84835  ? 65  THR BA CA  1 
ATOM   2716 C  C   . THR B 1 65  ? 16.58000  5.88900   25.38600  1.000 19.77033  ? 65  THR BA C   1 
ATOM   2717 O  O   . THR B 1 65  ? 16.01200  5.33500   24.44100  1.000 15.09086  ? 65  THR BA O   1 
ATOM   2718 C  CB  . THR B 1 65  ? 18.13400  7.78800   24.93500  1.000 12.51731  ? 65  THR BA CB  1 
ATOM   2719 O  OG1 . THR B 1 65  ? 17.40300  8.56300   25.89200  1.000 10.29061  ? 65  THR BA OG1 1 
ATOM   2720 C  CG2 . THR B 1 65  ? 17.56200  8.03200   23.54400  1.000 10.37409  ? 65  THR BA CG2 1 
ATOM   2721 N  N   . GLY B 1 66  ? 15.97500  6.17000   26.54000  1.000 13.20918  ? 66  GLY BA N   1 
ATOM   2722 C  CA  . GLY B 1 66  ? 14.54800  6.02600   26.71800  1.000 6.79205   ? 66  GLY BA CA  1 
ATOM   2723 C  C   . GLY B 1 66  ? 13.81400  7.31100   26.38300  1.000 11.68408  ? 66  GLY BA C   1 
ATOM   2724 O  O   . GLY B 1 66  ? 14.37300  8.26200   25.83500  1.000 10.56351  ? 66  GLY BA O   1 
ATOM   2725 N  N   . GLY B 1 67  ? 12.52900  7.33000   26.72200  1.000 10.47928  ? 67  GLY BA N   1 
ATOM   2726 C  CA  . GLY B 1 67  ? 11.72000  8.51600   26.54100  1.000 9.03152   ? 67  GLY BA CA  1 
ATOM   2727 C  C   . GLY B 1 67  ? 10.99100  8.62300   25.22200  1.000 8.59847   ? 67  GLY BA C   1 
ATOM   2728 O  O   . GLY B 1 67  ? 10.45400  9.69500   24.92200  1.000 9.90811   ? 67  GLY BA O   1 
ATOM   2729 N  N   . SER B 1 68  ? 10.95300  7.55600   24.43200  1.000 11.70504  ? 68  SER BA N   1 
ATOM   2730 C  CA  . SER B 1 68  ? 10.25800  7.52200   23.13100  1.000 15.36617  ? 68  SER BA CA  1 
ATOM   2731 C  C   . SER B 1 68  ? 10.82000  8.65400   22.26200  1.000 10.30083  ? 68  SER BA C   1 
ATOM   2732 O  O   . SER B 1 68  ? 12.02900  8.92900   22.31500  1.000 15.74390  ? 68  SER BA O   1 
ATOM   2733 C  CB  . SER B 1 68  ? 8.75900   7.56500   23.34400  1.000 18.49312  ? 68  SER BA CB  1 
ATOM   2734 O  OG  . SER B 1 68  ? 8.07100   7.41000   22.11300  1.000 9.83021   ? 68  SER BA OG  1 
ATOM   2735 N  N   . ALA B 1 69  ? 9.98100   9.32800   21.47000  1.000 8.54555   ? 69  ALA BA N   1 
ATOM   2736 C  CA  . ALA B 1 69  ? 10.47600  10.33300  20.53500  1.000 7.31763   ? 69  ALA BA CA  1 
ATOM   2737 C  C   . ALA B 1 69  ? 11.13500  11.50600  21.24700  1.000 14.69662  ? 69  ALA BA C   1 
ATOM   2738 O  O   . ALA B 1 69  ? 12.02900  12.14800  20.68300  1.000 9.60391   ? 69  ALA BA O   1 
ATOM   2739 C  CB  . ALA B 1 69  ? 9.33500   10.83200  19.64700  1.000 4.58587   ? 69  ALA BA CB  1 
ATOM   2740 N  N   . PHE B 1 70  ? 10.70800  11.80700  22.47800  1.000 8.18064   ? 70  PHE BA N   1 
ATOM   2741 C  CA  . PHE B 1 70  ? 11.29400  12.92900  23.20600  1.000 16.26474  ? 70  PHE BA CA  1 
ATOM   2742 C  C   . PHE B 1 70  ? 12.74600  12.66600  23.58100  1.000 7.23037   ? 70  PHE BA C   1 
ATOM   2743 O  O   . PHE B 1 70  ? 13.52600  13.61400  23.72900  1.000 11.72055  ? 70  PHE BA O   1 
ATOM   2744 C  CB  . PHE B 1 70  ? 10.48800  13.22700  24.47200  1.000 13.76704  ? 70  PHE BA CB  1 
ATOM   2745 C  CG  . PHE B 1 70  ? 9.00800   13.34600  24.24400  1.000 12.05011  ? 70  PHE BA CG  1 
ATOM   2746 C  CD1 . PHE B 1 70  ? 8.46400   14.51100  23.73000  1.000 10.66833  ? 70  PHE BA CD1 1 
ATOM   2747 C  CD2 . PHE B 1 70  ? 8.16000   12.29800  24.56200  1.000 9.70126   ? 70  PHE BA CD2 1 
ATOM   2748 C  CE1 . PHE B 1 70  ? 7.10200   14.62400  23.52600  1.000 12.94375  ? 70  PHE BA CE1 1 
ATOM   2749 C  CE2 . PHE B 1 70  ? 6.79600   12.40500  24.36000  1.000 14.79719  ? 70  PHE BA CE2 1 
ATOM   2750 C  CZ  . PHE B 1 70  ? 6.26700   13.56900  23.84200  1.000 16.98077  ? 70  PHE BA CZ  1 
ATOM   2751 N  N   . GLY B 1 71  ? 13.12700  11.39600  23.73300  1.000 10.93239  ? 71  GLY BA N   1 
ATOM   2752 C  CA  . GLY B 1 71  ? 14.43900  11.05500  24.25700  1.000 9.08583   ? 71  GLY BA CA  1 
ATOM   2753 C  C   . GLY B 1 71  ? 15.60000  11.42700  23.35800  1.000 6.94439   ? 71  GLY BA C   1 
ATOM   2754 O  O   . GLY B 1 71  ? 16.73700  11.50400  23.83600  1.000 10.54029  ? 71  GLY BA O   1 
ATOM   2755 N  N   . LEU B 1 72  ? 15.34600  11.65800  22.06700  1.000 6.80575   ? 72  LEU BA N   1 
ATOM   2756 C  CA  . LEU B 1 72  ? 16.42100  12.06700  21.16900  1.000 8.67144   ? 72  LEU BA CA  1 
ATOM   2757 C  C   . LEU B 1 72  ? 17.03300  13.40300  21.57300  1.000 9.12199   ? 72  LEU BA C   1 
ATOM   2758 O  O   . LEU B 1 72  ? 18.12800  13.73600  21.10800  1.000 13.66512  ? 72  LEU BA O   1 
ATOM   2759 C  CB  . LEU B 1 72  ? 15.90600  12.13600  19.73100  1.000 0.47606   ? 72  LEU BA CB  1 
ATOM   2760 C  CG  . LEU B 1 72  ? 15.59800  10.78400  19.08400  1.000 6.60441   ? 72  LEU BA CG  1 
ATOM   2761 C  CD1 . LEU B 1 72  ? 15.05300  10.96600  17.67800  1.000 14.47110  ? 72  LEU BA CD1 1 
ATOM   2762 C  CD2 . LEU B 1 72  ? 16.83800  9.90500   19.07000  1.000 5.77921   ? 72  LEU BA CD2 1 
ATOM   2763 N  N   . GLU B 1 73  ? 16.35200  14.17400  22.42700  1.000 5.58459   ? 73  GLU BA N   1 
ATOM   2764 C  CA  . GLU B 1 73  ? 16.92800  15.41600  22.93100  1.000 6.95322   ? 73  GLU BA CA  1 
ATOM   2765 C  C   . GLU B 1 73  ? 18.22500  15.16600  23.69100  1.000 8.88188   ? 73  GLU BA C   1 
ATOM   2766 O  O   . GLU B 1 73  ? 19.10300  16.03600  23.72000  1.000 12.45521  ? 73  GLU BA O   1 
ATOM   2767 C  CB  . GLU B 1 73  ? 15.91900  16.13700  23.82700  1.000 12.66114  ? 73  GLU BA CB  1 
ATOM   2768 C  CG  . GLU B 1 73  ? 16.28000  17.58100  24.13400  1.000 11.56554  ? 73  GLU BA CG  1 
ATOM   2769 C  CD  . GLU B 1 73  ? 15.29900  18.23900  25.08500  1.000 15.16674  ? 73  GLU BA CD  1 
ATOM   2770 O  OE1 . GLU B 1 73  ? 14.08600  18.23800  24.78500  1.000 15.51928  ? 73  GLU BA OE1 1 
ATOM   2771 O  OE2 . GLU B 1 73  ? 15.74000  18.75700  26.13200  1.000 17.14842  ? 73  GLU BA OE2 1 
ATOM   2772 N  N   . ALA B 1 74  ? 18.36600  13.98900  24.30800  1.000 9.55501   ? 74  ALA BA N   1 
ATOM   2773 C  CA  . ALA B 1 74  ? 19.60800  13.66700  25.00300  1.000 12.06819  ? 74  ALA BA CA  1 
ATOM   2774 C  C   . ALA B 1 74  ? 20.77000  13.52100  24.03200  1.000 11.27649  ? 74  ALA BA C   1 
ATOM   2775 O  O   . ALA B 1 74  ? 21.92200  13.76600  24.40600  1.000 11.36081  ? 74  ALA BA O   1 
ATOM   2776 C  CB  . ALA B 1 74  ? 19.44000  12.39000  25.82700  1.000 6.94927   ? 74  ALA BA CB  1 
ATOM   2777 N  N   . ALA B 1 75  ? 20.49300  13.12300  22.78800  1.000 7.20344   ? 75  ALA BA N   1 
ATOM   2778 C  CA  . ALA B 1 75  ? 21.55000  13.06400  21.78400  1.000 12.03513  ? 75  ALA BA CA  1 
ATOM   2779 C  C   . ALA B 1 75  ? 22.09500  14.45400  21.48200  1.000 8.79019   ? 75  ALA BA C   1 
ATOM   2780 O  O   . ALA B 1 75  ? 23.30900  14.63500  21.33400  1.000 6.47210   ? 75  ALA BA O   1 
ATOM   2781 C  CB  . ALA B 1 75  ? 21.02900  12.40000  20.50900  1.000 12.50895  ? 75  ALA BA CB  1 
ATOM   2782 N  N   . LEU B 1 76  ? 21.21000  15.45100  21.39100  1.000 3.30754   ? 76  LEU BA N   1 
ATOM   2783 C  CA  . LEU B 1 76  ? 21.66400  16.81900  21.16600  1.000 7.29204   ? 76  LEU BA CA  1 
ATOM   2784 C  C   . LEU B 1 76  ? 22.44400  17.34600  22.36200  1.000 9.55856   ? 76  LEU BA C   1 
ATOM   2785 O  O   . LEU B 1 76  ? 23.38200  18.13300  22.19000  1.000 11.71575  ? 76  LEU BA O   1 
ATOM   2786 C  CB  . LEU B 1 76  ? 20.47500  17.73100  20.86100  1.000 8.52887   ? 76  LEU BA CB  1 
ATOM   2787 C  CG  . LEU B 1 76  ? 20.05100  17.86500  19.39400  1.000 17.34221  ? 76  LEU BA CG  1 
ATOM   2788 C  CD1 . LEU B 1 76  ? 21.24100  18.18300  18.50200  1.000 13.40366  ? 76  LEU BA CD1 1 
ATOM   2789 C  CD2 . LEU B 1 76  ? 19.34000  16.61100  18.91200  1.000 9.07789   ? 76  LEU BA CD2 1 
ATOM   2790 N  N   . GLY B 1 77  ? 22.07500  16.92700  23.57500  1.000 10.56928  ? 77  GLY BA N   1 
ATOM   2791 C  CA  . GLY B 1 77  ? 22.86000  17.29200  24.74200  1.000 12.96664  ? 77  GLY BA CA  1 
ATOM   2792 C  C   . GLY B 1 77  ? 24.27000  16.74000  24.68300  1.000 13.97885  ? 77  GLY BA C   1 
ATOM   2793 O  O   . GLY B 1 77  ? 25.22500  17.39900  25.10200  1.000 12.56454  ? 77  GLY BA O   1 
ATOM   2794 N  N   . ALA B 1 78  ? 24.42100  15.52200  24.15600  1.000 10.94850  ? 78  ALA BA N   1 
ATOM   2795 C  CA  . ALA B 1 78  ? 25.75300  14.96300  23.95400  1.000 10.06742  ? 78  ALA BA CA  1 
ATOM   2796 C  C   . ALA B 1 78  ? 26.52200  15.74600  22.89800  1.000 11.64914  ? 78  ALA BA C   1 
ATOM   2797 O  O   . ALA B 1 78  ? 27.73300  15.96100  23.03700  1.000 14.25664  ? 78  ALA BA O   1 
ATOM   2798 C  CB  . ALA B 1 78  ? 25.64900  13.49000  23.56000  1.000 12.34219  ? 78  ALA BA CB  1 
ATOM   2799 N  N   . VAL B 1 79  ? 25.83500  16.18200  21.83900  1.000 14.32118  ? 79  VAL BA N   1 
ATOM   2800 C  CA  . VAL B 1 79  ? 26.48600  16.96600  20.79100  1.000 20.14246  ? 79  VAL BA CA  1 
ATOM   2801 C  C   . VAL B 1 79  ? 27.02800  18.27100  21.36300  1.000 12.49542  ? 79  VAL BA C   1 
ATOM   2802 O  O   . VAL B 1 79  ? 28.17600  18.65200  21.10600  1.000 14.20863  ? 79  VAL BA O   1 
ATOM   2803 C  CB  . VAL B 1 79  ? 25.51000  17.21800  19.62600  1.000 12.80244  ? 79  VAL BA CB  1 
ATOM   2804 C  CG1 . VAL B 1 79  ? 26.00400  18.35600  18.74700  1.000 8.38023   ? 79  VAL BA CG1 1 
ATOM   2805 C  CG2 . VAL B 1 79  ? 25.32800  15.95100  18.80100  1.000 7.45916   ? 79  VAL BA CG2 1 
ATOM   2806 N  N   . ARG B 1 80  ? 26.20800  18.97200  22.15300  1.000 10.98890  ? 80  ARG BA N   1 
ATOM   2807 C  CA  . ARG B 1 80  ? 26.65800  20.21300  22.77700  1.000 10.40098  ? 80  ARG BA CA  1 
ATOM   2808 C  C   . ARG B 1 80  ? 27.86200  19.97300  23.68100  1.000 23.22973  ? 80  ARG BA C   1 
ATOM   2809 O  O   . ARG B 1 80  ? 28.82400  20.75000  23.66600  1.000 21.60430  ? 80  ARG BA O   1 
ATOM   2810 C  CB  . ARG B 1 80  ? 25.52000  20.84900  23.57800  1.000 9.22876   ? 80  ARG BA CB  1 
ATOM   2811 C  CG  . ARG B 1 80  ? 24.43300  21.50700  22.74500  1.000 15.16856  ? 80  ARG BA CG  1 
ATOM   2812 C  CD  . ARG B 1 80  ? 23.25600  21.90400  23.62900  1.000 17.03264  ? 80  ARG BA CD  1 
ATOM   2813 N  NE  . ARG B 1 80  ? 22.33600  22.82000  22.96600  1.000 18.24337  ? 80  ARG BA NE  1 
ATOM   2814 C  CZ  . ARG B 1 80  ? 22.52200  24.13000  22.86600  1.000 32.26864  ? 80  ARG BA CZ  1 
ATOM   2815 N  NH1 . ARG B 1 80  ? 23.59900  24.71500  23.36600  1.000 19.04404  ? 80  ARG BA NH1 1 
ATOM   2816 N  NH2 . ARG B 1 80  ? 21.60500  24.87100  22.25100  1.000 16.99324  ? 80  ARG BA NH2 1 
ATOM   2817 N  N   . TYR B 1 81  ? 27.82600  18.90100  24.47700  1.000 13.31964  ? 81  TYR BA N   1 
ATOM   2818 C  CA  . TYR B 1 81  ? 28.93200  18.61100  25.38400  1.000 12.99163  ? 81  TYR BA CA  1 
ATOM   2819 C  C   . TYR B 1 81  ? 30.21800  18.34900  24.61100  1.000 22.09970  ? 81  TYR BA C   1 
ATOM   2820 O  O   . TYR B 1 81  ? 31.28600  18.86400  24.96200  1.000 14.84905  ? 81  TYR BA O   1 
ATOM   2821 C  CB  . TYR B 1 81  ? 28.58000  17.41400  26.27300  1.000 10.51545  ? 81  TYR BA CB  1 
ATOM   2822 C  CG  . TYR B 1 81  ? 29.76300  16.79600  26.99600  1.000 8.36962   ? 81  TYR BA CG  1 
ATOM   2823 C  CD1 . TYR B 1 81  ? 30.51100  15.77700  26.41600  1.000 12.57492  ? 81  TYR BA CD1 1 
ATOM   2824 C  CD2 . TYR B 1 81  ? 30.12700  17.23200  28.26500  1.000 17.98997  ? 81  TYR BA CD2 1 
ATOM   2825 C  CE1 . TYR B 1 81  ? 31.58900  15.21500  27.07600  1.000 14.65355  ? 81  TYR BA CE1 1 
ATOM   2826 C  CE2 . TYR B 1 81  ? 31.20300  16.67500  28.93300  1.000 16.83947  ? 81  TYR BA CE2 1 
ATOM   2827 C  CZ  . TYR B 1 81  ? 31.93000  15.66800  28.33400  1.000 23.37232  ? 81  TYR BA CZ  1 
ATOM   2828 O  OH  . TYR B 1 81  ? 32.99900  15.11300  28.99800  1.000 28.37510  ? 81  TYR BA OH  1 
ATOM   2829 N  N   . PHE B 1 82  ? 30.13400  17.54000  23.55100  1.000 11.11618  ? 82  PHE BA N   1 
ATOM   2830 C  CA  . PHE B 1 82  ? 31.32800  17.17700  22.79800  1.000 18.17009  ? 82  PHE BA CA  1 
ATOM   2831 C  C   . PHE B 1 82  ? 31.91400  18.36700  22.05000  1.000 17.22897  ? 82  PHE BA C   1 
ATOM   2832 O  O   . PHE B 1 82  ? 33.13500  18.44100  21.87400  1.000 16.74614  ? 82  PHE BA O   1 
ATOM   2833 C  CB  . PHE B 1 82  ? 31.01000  16.03400  21.83400  1.000 13.12355  ? 82  PHE BA CB  1 
ATOM   2834 C  CG  . PHE B 1 82  ? 30.96200  14.68300  22.49300  1.000 14.93720  ? 82  PHE BA CG  1 
ATOM   2835 C  CD1 . PHE B 1 82  ? 32.00100  14.25800  23.30500  1.000 14.42740  ? 82  PHE BA CD1 1 
ATOM   2836 C  CD2 . PHE B 1 82  ? 29.87600  13.84400  22.30900  1.000 6.63806   ? 82  PHE BA CD2 1 
ATOM   2837 C  CE1 . PHE B 1 82  ? 31.96100  13.01700  23.91600  1.000 18.89719  ? 82  PHE BA CE1 1 
ATOM   2838 C  CE2 . PHE B 1 82  ? 29.82900  12.60300  22.91500  1.000 16.97529  ? 82  PHE BA CE2 1 
ATOM   2839 C  CZ  . PHE B 1 82  ? 30.87300  12.18900  23.72100  1.000 17.39169  ? 82  PHE BA CZ  1 
ATOM   2840 N  N   . GLU B 1 83  ? 31.07200  19.30500  21.60200  1.000 18.27604  ? 83  GLU BA N   1 
ATOM   2841 C  CA  . GLU B 1 83  ? 31.60200  20.51700  20.98400  1.000 15.80149  ? 83  GLU BA CA  1 
ATOM   2842 C  C   . GLU B 1 83  ? 32.39000  21.33900  21.99400  1.000 16.18681  ? 83  GLU BA C   1 
ATOM   2843 O  O   . GLU B 1 83  ? 33.44300  21.89800  21.66500  1.000 12.64354  ? 83  GLU BA O   1 
ATOM   2844 C  CB  . GLU B 1 83  ? 30.47400  21.35600  20.38100  1.000 12.24689  ? 83  GLU BA CB  1 
ATOM   2845 C  CG  . GLU B 1 83  ? 30.98200  22.58400  19.63000  1.000 10.95550  ? 83  GLU BA CG  1 
ATOM   2846 C  CD  . GLU B 1 83  ? 29.90900  23.62900  19.38700  1.000 15.61271  ? 83  GLU BA CD  1 
ATOM   2847 O  OE1 . GLU B 1 83  ? 28.78600  23.47400  19.90800  1.000 21.50194  ? 83  GLU BA OE1 1 
ATOM   2848 O  OE2 . GLU B 1 83  ? 30.19500  24.61300  18.67200  1.000 24.01767  ? 83  GLU BA OE2 1 
ATOM   2849 N  N   . GLU B 1 84  ? 31.89500  21.41900  23.23100  1.000 13.50901  ? 84  GLU BA N   1 
ATOM   2850 C  CA  . GLU B 1 84  ? 32.62200  22.12400  24.28100  1.000 19.49126  ? 84  GLU BA CA  1 
ATOM   2851 C  C   . GLU B 1 84  ? 33.98500  21.49100  24.53000  1.000 26.71491  ? 84  GLU BA C   1 
ATOM   2852 O  O   . GLU B 1 84  ? 34.97400  22.19800  24.75000  1.000 42.98426  ? 84  GLU BA O   1 
ATOM   2853 C  CB  . GLU B 1 84  ? 31.79900  22.14000  25.56800  1.000 22.01078  ? 84  GLU BA CB  1 
ATOM   2854 C  CG  . GLU B 1 84  ? 30.77600  23.25700  25.64000  1.000 22.21288  ? 84  GLU BA CG  1 
ATOM   2855 C  CD  . GLU B 1 84  ? 29.97600  23.22300  26.92600  1.000 41.54770  ? 84  GLU BA CD  1 
ATOM   2856 O  OE1 . GLU B 1 84  ? 30.56800  22.93300  27.98800  1.000 36.73118  ? 84  GLU BA OE1 1 
ATOM   2857 O  OE2 . GLU B 1 84  ? 28.75700  23.48900  26.87600  1.000 46.80713  ? 84  GLU BA OE2 1 
ATOM   2858 N  N   . GLN B 1 85  ? 34.06100  20.16100  24.49000  1.000 21.89861  ? 85  GLN BA N   1 
ATOM   2859 C  CA  . GLN B 1 85  ? 35.31800  19.46100  24.72100  1.000 17.75617  ? 85  GLN BA CA  1 
ATOM   2860 C  C   . GLN B 1 85  ? 36.26400  19.52100  23.52800  1.000 26.56307  ? 85  GLN BA C   1 
ATOM   2861 O  O   . GLN B 1 85  ? 37.39800  19.04300  23.63500  1.000 34.40664  ? 85  GLN BA O   1 
ATOM   2862 C  CB  . GLN B 1 85  ? 35.04600  18.00000  25.08900  1.000 18.04671  ? 85  GLN BA CB  1 
ATOM   2863 C  CG  . GLN B 1 85  ? 34.34800  17.81700  26.42800  1.000 30.56750  ? 85  GLN BA CG  1 
ATOM   2864 C  CD  . GLN B 1 85  ? 35.07400  18.51000  27.56500  1.000 43.46036  ? 85  GLN BA CD  1 
ATOM   2865 O  OE1 . GLN B 1 85  ? 36.27900  18.33100  27.74800  1.000 37.45490  ? 85  GLN BA OE1 1 
ATOM   2866 N  NE2 . GLN B 1 85  ? 34.34300  19.30600  28.33600  1.000 32.14088  ? 85  GLN BA NE2 1 
ATOM   2867 N  N   . GLY B 1 86  ? 35.83500  20.08700  22.40400  1.000 24.59121  ? 86  GLY BA N   1 
ATOM   2868 C  CA  . GLY B 1 86  ? 36.69800  20.22100  21.24900  1.000 28.21108  ? 86  GLY BA CA  1 
ATOM   2869 C  C   . GLY B 1 86  ? 36.70500  19.04400  20.30500  1.000 16.78801  ? 86  GLY BA C   1 
ATOM   2870 O  O   . GLY B 1 86  ? 37.65500  18.89900  19.52800  1.000 29.18648  ? 86  GLY BA O   1 
ATOM   2871 N  N   . ARG B 1 87  ? 35.68200  18.20000  20.34300  1.000 21.11270  ? 87  ARG BA N   1 
ATOM   2872 C  CA  . ARG B 1 87  ? 35.59000  17.04600  19.46400  1.000 18.51071  ? 87  ARG BA CA  1 
ATOM   2873 C  C   . ARG B 1 87  ? 34.59900  17.31400  18.33700  1.000 18.16099  ? 87  ARG BA C   1 
ATOM   2874 O  O   . ARG B 1 87  ? 33.69100  18.13900  18.45600  1.000 20.65927  ? 87  ARG BA O   1 
ATOM   2875 C  CB  . ARG B 1 87  ? 35.17600  15.80000  20.25100  1.000 17.92815  ? 87  ARG BA CB  1 
ATOM   2876 C  CG  . ARG B 1 87  ? 36.29300  15.21600  21.10000  1.000 26.44509  ? 87  ARG BA CG  1 
ATOM   2877 C  CD  . ARG B 1 87  ? 35.74700  14.41700  22.26800  1.000 31.04436  ? 87  ARG BA CD  1 
ATOM   2878 N  NE  . ARG B 1 87  ? 35.94500  12.98400  22.08800  1.000 40.64944  ? 87  ARG BA NE  1 
ATOM   2879 C  CZ  . ARG B 1 87  ? 36.67800  12.22300  22.88900  1.000 28.97484  ? 87  ARG BA CZ  1 
ATOM   2880 N  NH1 . ARG B 1 87  ? 37.31200  12.72900  23.93400  1.000 38.63521  ? 87  ARG BA NH1 1 
ATOM   2881 N  NH2 . ARG B 1 87  ? 36.77900  10.92200  22.63500  1.000 30.41921  ? 87  ARG BA NH2 1 
ATOM   2882 N  N   . GLY B 1 88  ? 34.79300  16.60600  17.23400  1.000 16.21944  ? 88  GLY BA N   1 
ATOM   2883 C  CA  . GLY B 1 88  ? 33.94700  16.73600  16.06600  1.000 18.26890  ? 88  GLY BA CA  1 
ATOM   2884 C  C   . GLY B 1 88  ? 34.73700  17.12600  14.83000  1.000 18.83113  ? 88  GLY BA C   1 
ATOM   2885 O  O   . GLY B 1 88  ? 35.90900  17.49300  14.88700  1.000 21.18578  ? 88  GLY BA O   1 
ATOM   2886 N  N   . TYR B 1 89  ? 34.05000  17.03200  13.69200  1.000 17.12742  ? 89  TYR BA N   1 
ATOM   2887 C  CA  . TYR B 1 89  ? 34.67200  17.35300  12.41400  1.000 17.90853  ? 89  TYR BA CA  1 
ATOM   2888 C  C   . TYR B 1 89  ? 35.05800  18.82600  12.36900  1.000 20.37958  ? 89  TYR BA C   1 
ATOM   2889 O  O   . TYR B 1 89  ? 34.22500  19.70700  12.59900  1.000 6.96513   ? 89  TYR BA O   1 
ATOM   2890 C  CB  . TYR B 1 89  ? 33.72000  17.01300  11.26600  1.000 20.34332  ? 89  TYR BA CB  1 
ATOM   2891 C  CG  . TYR B 1 89  ? 34.19700  17.48000  9.90800   1.000 24.81263  ? 89  TYR BA CG  1 
ATOM   2892 C  CD1 . TYR B 1 89  ? 35.22600  16.82200  9.24700   1.000 31.44948  ? 89  TYR BA CD1 1 
ATOM   2893 C  CD2 . TYR B 1 89  ? 33.61400  18.57700  9.28600   1.000 37.99065  ? 89  TYR BA CD2 1 
ATOM   2894 C  CE1 . TYR B 1 89  ? 35.66400  17.24500  8.00400   1.000 35.82836  ? 89  TYR BA CE1 1 
ATOM   2895 C  CE2 . TYR B 1 89  ? 34.04400  19.00800  8.04400   1.000 34.71867  ? 89  TYR BA CE2 1 
ATOM   2896 C  CZ  . TYR B 1 89  ? 35.06900  18.33900  7.40800   1.000 47.77875  ? 89  TYR BA CZ  1 
ATOM   2897 O  OH  . TYR B 1 89  ? 35.49900  18.76600  6.17200   1.000 39.17998  ? 89  TYR BA OH  1 
ATOM   2898 N  N   . ASP B 1 90  ? 36.33100  19.08900  12.08000  1.000 18.39036  ? 90  ASP BA N   1 
ATOM   2899 C  CA  . ASP B 1 90  ? 36.85100  20.45300  12.05300  1.000 22.18648  ? 90  ASP BA CA  1 
ATOM   2900 C  C   . ASP B 1 90  ? 36.38000  21.14000  10.77900  1.000 21.46112  ? 90  ASP BA C   1 
ATOM   2901 O  O   . ASP B 1 90  ? 36.86100  20.83400  9.68300   1.000 27.29082  ? 90  ASP BA O   1 
ATOM   2902 C  CB  . ASP B 1 90  ? 38.37400  20.45000  12.14400  1.000 29.92098  ? 90  ASP BA CB  1 
ATOM   2903 C  CG  . ASP B 1 90  ? 38.93100  21.77400  12.63200  1.000 35.04535  ? 90  ASP BA CG  1 
ATOM   2904 O  OD1 . ASP B 1 90  ? 38.27300  22.81500  12.41700  1.000 22.76597  ? 90  ASP BA OD1 1 
ATOM   2905 O  OD2 . ASP B 1 90  ? 40.02700  21.77700  13.23000  1.000 51.37880  ? 90  ASP BA OD2 1 
ATOM   2906 N  N   . VAL B 1 91  ? 35.44000  22.07600  10.92200  1.000 18.88379  ? 91  VAL BA N   1 
ATOM   2907 C  CA  . VAL B 1 91  ? 34.92600  22.83500  9.79100   1.000 26.31155  ? 91  VAL BA CA  1 
ATOM   2908 C  C   . VAL B 1 91  ? 35.56700  24.21100  9.68600   1.000 32.55366  ? 91  VAL BA C   1 
ATOM   2909 O  O   . VAL B 1 91  ? 35.27300  24.95800  8.74100   1.000 35.18475  ? 91  VAL BA O   1 
ATOM   2910 C  CB  . VAL B 1 91  ? 33.38800  22.95000  9.87000   1.000 20.31510  ? 91  VAL BA CB  1 
ATOM   2911 C  CG1 . VAL B 1 91  ? 32.96700  24.15200  10.71400  1.000 15.67787  ? 91  VAL BA CG1 1 
ATOM   2912 C  CG2 . VAL B 1 91  ? 32.77500  22.99000  8.48300   1.000 23.99330  ? 91  VAL BA CG2 1 
ATOM   2913 N  N   . GLY B 1 92  ? 36.44800  24.56400  10.62000  1.000 25.93809  ? 92  GLY BA N   1 
ATOM   2914 C  CA  . GLY B 1 92  ? 37.11200  25.85100  10.59900  1.000 25.46955  ? 92  GLY BA CA  1 
ATOM   2915 C  C   . GLY B 1 92  ? 36.52400  26.82600  11.59600  1.000 30.59034  ? 92  GLY BA C   1 
ATOM   2916 O  O   . GLY B 1 92  ? 37.19300  27.22900  12.55300  1.000 27.16067  ? 92  GLY BA O   1 
ATOM   2917 N  N   . VAL B 1 93  ? 35.26300  27.21500  11.37800  1.000 36.30224  ? 93  VAL BA N   1 
ATOM   2918 C  CA  . VAL B 1 93  ? 34.57700  28.12900  12.28300  1.000 26.36492  ? 93  VAL BA CA  1 
ATOM   2919 C  C   . VAL B 1 93  ? 33.90800  27.40700  13.44200  1.000 24.26075  ? 93  VAL BA C   1 
ATOM   2920 O  O   . VAL B 1 93  ? 33.35100  28.06500  14.33100  1.000 20.84961  ? 93  VAL BA O   1 
ATOM   2921 C  CB  . VAL B 1 93  ? 33.52900  28.96800  11.52100  1.000 46.69251  ? 93  VAL BA CB  1 
ATOM   2922 C  CG1 . VAL B 1 93  ? 34.21500  29.94100  10.57400  1.000 19.45967  ? 93  VAL BA CG1 1 
ATOM   2923 C  CG2 . VAL B 1 93  ? 32.57300  28.05800  10.76000  1.000 26.37038  ? 93  VAL BA CG2 1 
ATOM   2924 N  N   . ALA B 1 94  ? 33.94300  26.07700  13.46200  1.000 27.07714  ? 94  ALA BA N   1 
ATOM   2925 C  CA  . ALA B 1 94  ? 33.33800  25.29900  14.53500  1.000 20.71924  ? 94  ALA BA CA  1 
ATOM   2926 C  C   . ALA B 1 94  ? 33.81100  23.85700  14.41700  1.000 21.51492  ? 94  ALA BA C   1 
ATOM   2927 O  O   . ALA B 1 94  ? 34.47400  23.47200  13.44900  1.000 14.32967  ? 94  ALA BA O   1 
ATOM   2928 C  CB  . ALA B 1 94  ? 31.80800  25.36500  14.49300  1.000 11.11825  ? 94  ALA BA CB  1 
ATOM   2929 N  N   . LYS B 1 95  ? 33.46500  23.06700  15.42700  1.000 18.24788  ? 95  LYS BA N   1 
ATOM   2930 C  CA  . LYS B 1 95  ? 33.64200  21.62300  15.41400  1.000 21.30382  ? 95  LYS BA CA  1 
ATOM   2931 C  C   . LYS B 1 95  ? 32.26400  20.98600  15.50200  1.000 21.26376  ? 95  LYS BA C   1 
ATOM   2932 O  O   . LYS B 1 95  ? 31.43400  21.41200  16.31300  1.000 15.42571  ? 95  LYS BA O   1 
ATOM   2933 C  CB  . LYS B 1 95  ? 34.53100  21.16200  16.57300  1.000 15.36853  ? 95  LYS BA CB  1 
ATOM   2934 C  CG  . LYS B 1 95  ? 36.01300  21.11400  16.23700  1.000 28.91314  ? 95  LYS BA CG  1 
ATOM   2935 C  CD  . LYS B 1 95  ? 36.83800  21.79300  17.31900  1.000 38.99115  ? 95  LYS BA CD  1 
ATOM   2936 C  CE  . LYS B 1 95  ? 38.28700  21.95900  16.89300  1.000 44.29659  ? 95  LYS BA CE  1 
ATOM   2937 N  NZ  . LYS B 1 95  ? 38.43000  23.00000  15.83700  1.000 53.15307  ? 95  LYS BA NZ  1 
ATOM   2938 N  N   . ILE B 1 96  ? 32.01700  19.98700  14.66600  1.000 13.87082  ? 96  ILE BA N   1 
ATOM   2939 C  CA  . ILE B 1 96  ? 30.70200  19.37800  14.53200  1.000 17.32195  ? 96  ILE BA CA  1 
ATOM   2940 C  C   . ILE B 1 96  ? 30.79400  17.92400  14.97500  1.000 13.22789  ? 96  ILE BA C   1 
ATOM   2941 O  O   . ILE B 1 96  ? 31.23400  17.05800  14.21800  1.000 12.79203  ? 96  ILE BA O   1 
ATOM   2942 C  CB  . ILE B 1 96  ? 30.17400  19.48700  13.09000  1.000 19.81082  ? 96  ILE BA CB  1 
ATOM   2943 C  CG1 . ILE B 1 96  ? 30.25300  20.93800  12.60600  1.000 11.82045  ? 96  ILE BA CG1 1 
ATOM   2944 C  CG2 . ILE B 1 96  ? 28.74500  18.97400  13.00400  1.000 13.36965  ? 96  ILE BA CG2 1 
ATOM   2945 C  CD1 . ILE B 1 96  ? 29.82500  21.12100  11.16700  1.000 17.84192  ? 96  ILE BA CD1 1 
ATOM   2946 N  N   . PRO B 1 97  ? 30.39100  17.61800  16.20400  1.000 19.53063  ? 97  PRO BA N   1 
ATOM   2947 C  CA  . PRO B 1 97  ? 30.30200  16.22100  16.63200  1.000 16.33447  ? 97  PRO BA CA  1 
ATOM   2948 C  C   . PRO B 1 97  ? 29.03000  15.57000  16.10700  1.000 14.31074  ? 97  PRO BA C   1 
ATOM   2949 O  O   . PRO B 1 97  ? 28.08600  16.23400  15.67800  1.000 15.03920  ? 97  PRO BA O   1 
ATOM   2950 C  CB  . PRO B 1 97  ? 30.28700  16.30900  18.16500  1.000 12.45033  ? 97  PRO BA CB  1 
ATOM   2951 C  CG  . PRO B 1 97  ? 30.25900  17.79000  18.50800  1.000 14.25999  ? 97  PRO BA CG  1 
ATOM   2952 C  CD  . PRO B 1 97  ? 29.96400  18.54800  17.25800  1.000 11.94201  ? 97  PRO BA CD  1 
ATOM   2953 N  N   . LEU B 1 98  ? 29.02400  14.23900  16.14800  1.000 14.96738  ? 98  LEU BA N   1 
ATOM   2954 C  CA  . LEU B 1 98  ? 27.90700  13.44300  15.65200  1.000 10.57555  ? 98  LEU BA CA  1 
ATOM   2955 C  C   . LEU B 1 98  ? 27.58700  12.36200  16.67200  1.000 9.67293   ? 98  LEU BA C   1 
ATOM   2956 O  O   . LEU B 1 98  ? 28.46200  11.56800  17.03100  1.000 6.65033   ? 98  LEU BA O   1 
ATOM   2957 C  CB  . LEU B 1 98  ? 28.23600  12.81800  14.29400  1.000 18.82594  ? 98  LEU BA CB  1 
ATOM   2958 C  CG  . LEU B 1 98  ? 27.07600  12.64900  13.31100  1.000 22.16436  ? 98  LEU BA CG  1 
ATOM   2959 C  CD1 . LEU B 1 98  ? 26.32800  13.95900  13.11300  1.000 16.80673  ? 98  LEU BA CD1 1 
ATOM   2960 C  CD2 . LEU B 1 98  ? 27.59000  12.11600  11.98800  1.000 39.97274  ? 98  LEU BA CD2 1 
ATOM   2961 N  N   . VAL B 1 99  ? 26.34200  12.33500  17.14100  1.000 12.33406  ? 99  VAL BA N   1 
ATOM   2962 C  CA  . VAL B 1 99  ? 25.90600  11.33600  18.11500  1.000 6.84613   ? 99  VAL BA CA  1 
ATOM   2963 C  C   . VAL B 1 99  ? 24.63300  10.66000  17.61500  1.000 15.59021  ? 99  VAL BA C   1 
ATOM   2964 O  O   . VAL B 1 99  ? 23.52600  11.06300  18.00300  1.000 6.54114   ? 99  VAL BA O   1 
ATOM   2965 C  CB  . VAL B 1 99  ? 25.69000  11.96100  19.50400  1.000 11.06644  ? 99  VAL BA CB  1 
ATOM   2966 C  CG1 . VAL B 1 99  ? 25.37600  10.87900  20.53200  1.000 13.33945  ? 99  VAL BA CG1 1 
ATOM   2967 C  CG2 . VAL B 1 99  ? 26.91600  12.75800  19.93300  1.000 11.20716  ? 99  VAL BA CG2 1 
ATOM   2968 N  N   . PRO B 1 100 ? 24.73500  9.64500   16.75400  1.000 10.71087  ? 100 PRO BA N   1 
ATOM   2969 C  CA  . PRO B 1 100 ? 23.53800  8.88400   16.37200  1.000 7.55812   ? 100 PRO BA CA  1 
ATOM   2970 C  C   . PRO B 1 100 ? 22.90200  8.23000   17.58900  1.000 6.50331   ? 100 PRO BA C   1 
ATOM   2971 O  O   . PRO B 1 100 ? 23.57200  7.93100   18.58000  1.000 7.19341   ? 100 PRO BA O   1 
ATOM   2972 C  CB  . PRO B 1 100 ? 24.07800  7.83500   15.39000  1.000 7.42224   ? 100 PRO BA CB  1 
ATOM   2973 C  CG  . PRO B 1 100 ? 25.38300  8.38800   14.90800  1.000 14.03730  ? 100 PRO BA CG  1 
ATOM   2974 C  CD  . PRO B 1 100 ? 25.94200  9.17600   16.05400  1.000 8.34367   ? 100 PRO BA CD  1 
ATOM   2975 N  N   . ALA B 1 101 ? 21.59100  8.01300   17.51200  1.000 4.58130   ? 101 ALA BA N   1 
ATOM   2976 C  CA  . ALA B 1 101 ? 20.87300  7.46100   18.65200  1.000 7.96374   ? 101 ALA BA CA  1 
ATOM   2977 C  C   . ALA B 1 101 ? 19.57800  6.81000   18.19000  1.000 14.65241  ? 101 ALA BA C   1 
ATOM   2978 O  O   . ALA B 1 101 ? 19.03100  7.14400   17.13600  1.000 7.21466   ? 101 ALA BA O   1 
ATOM   2979 C  CB  . ALA B 1 101 ? 20.57900  8.53900   19.70200  1.000 15.74920  ? 101 ALA BA CB  1 
ATOM   2980 N  N   . ALA B 1 102 ? 19.10300  5.86600   19.00400  1.000 4.31465   ? 102 ALA BA N   1 
ATOM   2981 C  CA  . ALA B 1 102 ? 17.79500  5.24800   18.85100  1.000 11.10905  ? 102 ALA BA CA  1 
ATOM   2982 C  C   . ALA B 1 102 ? 17.12200  5.19000   20.21800  1.000 10.19632  ? 102 ALA BA C   1 
ATOM   2983 O  O   . ALA B 1 102 ? 17.78600  5.22900   21.25700  1.000 9.08818   ? 102 ALA BA O   1 
ATOM   2984 C  CB  . ALA B 1 102 ? 17.89800  3.84300   18.24200  1.000 3.72667   ? 102 ALA BA CB  1 
ATOM   2985 N  N   . VAL B 1 103 ? 15.79100  5.09700   20.21600  1.000 3.18415   ? 103 VAL BA N   1 
ATOM   2986 C  CA  . VAL B 1 103 ? 15.01800  5.20300   21.44700  1.000 6.95587   ? 103 VAL BA CA  1 
ATOM   2987 C  C   . VAL B 1 103 ? 14.23300  3.92100   21.69900  1.000 12.32350  ? 103 VAL BA C   1 
ATOM   2988 O  O   . VAL B 1 103 ? 14.00600  3.10500   20.80100  1.000 5.72266   ? 103 VAL BA O   1 
ATOM   2989 C  CB  . VAL B 1 103 ? 14.05600  6.41200   21.43200  1.000 9.76722   ? 103 VAL BA CB  1 
ATOM   2990 C  CG1 . VAL B 1 103 ? 14.75200  7.64500   20.89000  1.000 7.30248   ? 103 VAL BA CG1 1 
ATOM   2991 C  CG2 . VAL B 1 103 ? 12.80500  6.09100   20.62200  1.000 8.80378   ? 103 VAL BA CG2 1 
ATOM   2992 N  N   . ILE B 1 104 ? 13.82200  3.75600   22.95700  1.000 6.46312   ? 104 ILE BA N   1 
ATOM   2993 C  CA  . ILE B 1 104 ? 12.81100  2.78800   23.35500  1.000 6.05619   ? 104 ILE BA CA  1 
ATOM   2994 C  C   . ILE B 1 104 ? 11.66200  3.54900   24.00500  1.000 14.93669  ? 104 ILE BA C   1 
ATOM   2995 O  O   . ILE B 1 104 ? 11.83100  4.65600   24.52300  1.000 15.09412  ? 104 ILE BA O   1 
ATOM   2996 C  CB  . ILE B 1 104 ? 13.35200  1.71000   24.32000  1.000 11.33828  ? 104 ILE BA CB  1 
ATOM   2997 C  CG1 . ILE B 1 104 ? 13.77200  2.34400   25.65000  1.000 11.58649  ? 104 ILE BA CG1 1 
ATOM   2998 C  CG2 . ILE B 1 104 ? 14.50200  0.94000   23.68700  1.000 8.26094   ? 104 ILE BA CG2 1 
ATOM   2999 C  CD1 . ILE B 1 104 ? 13.80600  1.36800   26.81500  1.000 11.14431  ? 104 ILE BA CD1 1 
ATOM   3000 N  N   . TYR B 1 105 ? 10.48000  2.94000   23.97200  1.000 7.30369   ? 105 TYR BA N   1 
ATOM   3001 C  CA  . TYR B 1 105 ? 9.30500   3.49000   24.63900  1.000 12.93706  ? 105 TYR BA CA  1 
ATOM   3002 C  C   . TYR B 1 105 ? 9.28500   2.98400   26.07700  1.000 21.88682  ? 105 TYR BA C   1 
ATOM   3003 O  O   . TYR B 1 105 ? 9.11800   1.78300   26.31700  1.000 12.14126  ? 105 TYR BA O   1 
ATOM   3004 C  CB  . TYR B 1 105 ? 8.02700   3.09700   23.90100  1.000 14.24227  ? 105 TYR BA CB  1 
ATOM   3005 C  CG  . TYR B 1 105 ? 6.75900   3.57000   24.58100  1.000 18.13211  ? 105 TYR BA CG  1 
ATOM   3006 C  CD1 . TYR B 1 105 ? 6.21900   4.81800   24.29900  1.000 19.22788  ? 105 TYR BA CD1 1 
ATOM   3007 C  CD2 . TYR B 1 105 ? 6.10400   2.76700   25.50800  1.000 18.83317  ? 105 TYR BA CD2 1 
ATOM   3008 C  CE1 . TYR B 1 105 ? 5.06300   5.25300   24.92100  1.000 17.38139  ? 105 TYR BA CE1 1 
ATOM   3009 C  CE2 . TYR B 1 105 ? 4.95000   3.19300   26.13600  1.000 14.32084  ? 105 TYR BA CE2 1 
ATOM   3010 C  CZ  . TYR B 1 105 ? 4.43300   4.43500   25.83800  1.000 22.14398  ? 105 TYR BA CZ  1 
ATOM   3011 O  OH  . TYR B 1 105 ? 3.28200   4.85900   26.46200  1.000 15.41064  ? 105 TYR BA OH  1 
ATOM   3012 N  N   . ASP B 1 106 ? 9.44900   3.90000   27.03600  1.000 14.76148  ? 106 ASP BA N   1 
ATOM   3013 C  CA  . ASP B 1 106 ? 9.41200   3.54800   28.45100  1.000 11.67548  ? 106 ASP BA CA  1 
ATOM   3014 C  C   . ASP B 1 106 ? 8.47900   4.46000   29.24200  1.000 19.93200  ? 106 ASP BA C   1 
ATOM   3015 O  O   . ASP B 1 106 ? 8.62200   4.57400   30.46300  1.000 16.86745  ? 106 ASP BA O   1 
ATOM   3016 C  CB  . ASP B 1 106 ? 10.82000  3.57800   29.05600  1.000 12.12558  ? 106 ASP BA CB  1 
ATOM   3017 C  CG  . ASP B 1 106 ? 11.50100  4.93000   28.89900  1.000 18.48935  ? 106 ASP BA CG  1 
ATOM   3018 O  OD1 . ASP B 1 106 ? 10.89700  5.84800   28.30400  1.000 13.39061  ? 106 ASP BA OD1 1 
ATOM   3019 O  OD2 . ASP B 1 106 ? 12.64700  5.07500   29.37700  1.000 9.62932   ? 106 ASP BA OD2 1 
ATOM   3020 N  N   . LEU B 1 107 ? 7.52000   5.10500   28.57400  1.000 14.61934  ? 107 LEU BA N   1 
ATOM   3021 C  CA  . LEU B 1 107 ? 6.66500   6.08000   29.24000  1.000 12.66545  ? 107 LEU BA CA  1 
ATOM   3022 C  C   . LEU B 1 107 ? 5.57400   5.44100   30.08900  1.000 20.75207  ? 107 LEU BA C   1 
ATOM   3023 O  O   . LEU B 1 107 ? 5.02000   6.11500   30.96400  1.000 21.34842  ? 107 LEU BA O   1 
ATOM   3024 C  CB  . LEU B 1 107 ? 6.02000   7.01000   28.20900  1.000 14.54310  ? 107 LEU BA CB  1 
ATOM   3025 C  CG  . LEU B 1 107 ? 6.93700   7.69700   27.19200  1.000 22.90366  ? 107 LEU BA CG  1 
ATOM   3026 C  CD1 . LEU B 1 107 ? 6.17800   8.78900   26.45300  1.000 15.11405  ? 107 LEU BA CD1 1 
ATOM   3027 C  CD2 . LEU B 1 107 ? 8.18200   8.26200   27.86000  1.000 14.30173  ? 107 LEU BA CD2 1 
ATOM   3028 N  N   . SER B 1 108 ? 5.25000   4.16900   29.85900  1.000 16.25093  ? 108 SER BA N   1 
ATOM   3029 C  CA  . SER B 1 108 ? 4.17300   3.51600   30.59500  1.000 19.23609  ? 108 SER BA CA  1 
ATOM   3030 C  C   . SER B 1 108 ? 4.60000   3.01600   31.97000  1.000 26.60156  ? 108 SER BA C   1 
ATOM   3031 O  O   . SER B 1 108 ? 3.76500   2.46800   32.69700  1.000 22.12819  ? 108 SER BA O   1 
ATOM   3032 C  CB  . SER B 1 108 ? 3.60400   2.35500   29.77600  1.000 13.09234  ? 108 SER BA CB  1 
ATOM   3033 O  OG  . SER B 1 108 ? 2.71800   2.83200   28.77800  1.000 27.75993  ? 108 SER BA OG  1 
ATOM   3034 N  N   A VAL B 1 109 ? 5.86800   3.18100   32.33800  0.733 18.09232  ? 109 VAL BA N   1 
ATOM   3035 N  N   B VAL B 1 109 ? 5.86600   3.18500   32.34400  0.267 18.17340  ? 109 VAL BA N   1 
ATOM   3036 C  CA  A VAL B 1 109 ? 6.36800   2.81600   33.65700  0.733 17.93789  ? 109 VAL BA CA  1 
ATOM   3037 C  CA  B VAL B 1 109 ? 6.36000   2.81100   33.66300  0.267 18.03006  ? 109 VAL BA CA  1 
ATOM   3038 C  C   A VAL B 1 109 ? 6.97600   4.05800   34.29400  0.733 17.17340  ? 109 VAL BA C   1 
ATOM   3039 C  C   B VAL B 1 109 ? 6.99600   4.03700   34.30100  0.267 17.26015  ? 109 VAL BA C   1 
ATOM   3040 O  O   A VAL B 1 109 ? 7.67000   4.83400   33.62700  0.733 19.43115  ? 109 VAL BA O   1 
ATOM   3041 O  O   B VAL B 1 109 ? 7.74400   4.77200   33.64600  0.267 19.37838  ? 109 VAL BA O   1 
ATOM   3042 C  CB  A VAL B 1 109 ? 7.39500   1.66400   33.58200  0.733 24.17240  ? 109 VAL BA CB  1 
ATOM   3043 C  CB  B VAL B 1 109 ? 7.36800   1.64400   33.59400  0.267 23.92723  ? 109 VAL BA CB  1 
ATOM   3044 C  CG1 A VAL B 1 109 ? 8.50900   1.99100   32.59500  0.733 16.15658  ? 109 VAL BA CG1 1 
ATOM   3045 C  CG1 B VAL B 1 109 ? 7.19800   0.72800   34.79500  0.267 24.84260  ? 109 VAL BA CG1 1 
ATOM   3046 C  CG2 A VAL B 1 109 ? 7.96600   1.35400   34.96100  0.733 25.11677  ? 109 VAL BA CG2 1 
ATOM   3047 C  CG2 B VAL B 1 109 ? 7.20400   0.86300   32.29800  0.267 18.06287  ? 109 VAL BA CG2 1 
ATOM   3048 N  N   . GLY B 1 110 ? 6.69400   4.25800   35.57800  1.000 16.80464  ? 110 GLY BA N   1 
ATOM   3049 C  CA  . GLY B 1 110 ? 7.20700   5.41800   36.28100  1.000 19.34335  ? 110 GLY BA CA  1 
ATOM   3050 C  C   . GLY B 1 110 ? 6.50100   6.70100   35.89100  1.000 18.74427  ? 110 GLY BA C   1 
ATOM   3051 O  O   . GLY B 1 110 ? 5.27300   6.72700   35.77000  1.000 15.57196  ? 110 GLY BA O   1 
ATOM   3052 N  N   . ASP B 1 111 ? 7.26700   7.77100   35.68500  1.000 21.63136  ? 111 ASP BA N   1 
ATOM   3053 C  CA  . ASP B 1 111 ? 6.72100   9.08900   35.37200  1.000 18.15305  ? 111 ASP BA CA  1 
ATOM   3054 C  C   . ASP B 1 111 ? 6.80700   9.32000   33.86600  1.000 19.92432  ? 111 ASP BA C   1 
ATOM   3055 O  O   . ASP B 1 111 ? 7.90400   9.43400   33.30800  1.000 18.85700  ? 111 ASP BA O   1 
ATOM   3056 C  CB  . ASP B 1 111 ? 7.47000   10.17800  36.13700  1.000 20.17438  ? 111 ASP BA CB  1 
ATOM   3057 C  CG  . ASP B 1 111 ? 6.69100   11.47900  36.22000  1.000 28.26028  ? 111 ASP BA CG  1 
ATOM   3058 O  OD1 . ASP B 1 111 ? 5.81000   11.70900  35.36500  1.000 19.67815  ? 111 ASP BA OD1 1 
ATOM   3059 O  OD2 . ASP B 1 111 ? 6.96200   12.27500  37.14300  1.000 30.83747  ? 111 ASP BA OD2 1 
ATOM   3060 N  N   . ALA B 1 112 ? 5.64600   9.40900   33.21400  1.000 14.58546  ? 112 ALA BA N   1 
ATOM   3061 C  CA  . ALA B 1 112 ? 5.59700   9.60000   31.76900  1.000 20.13571  ? 112 ALA BA CA  1 
ATOM   3062 C  C   . ALA B 1 112 ? 6.02300   10.99600  31.33300  1.000 21.95890  ? 112 ALA BA C   1 
ATOM   3063 O  O   . ALA B 1 112 ? 6.27000   11.20100  30.14000  1.000 17.15903  ? 112 ALA BA O   1 
ATOM   3064 C  CB  . ALA B 1 112 ? 4.18600   9.31200   31.25200  1.000 14.58911  ? 112 ALA BA CB  1 
ATOM   3065 N  N   . ASN B 1 113 ? 6.11900   11.95200  32.25300  1.000 14.72325  ? 113 ASN BA N   1 
ATOM   3066 C  CA  . ASN B 1 113 ? 6.45500   13.32600  31.90300  1.000 19.86391  ? 113 ASN BA CA  1 
ATOM   3067 C  C   . ASN B 1 113 ? 7.94200   13.63400  32.02700  1.000 14.68659  ? 113 ASN BA C   1 
ATOM   3068 O  O   . ASN B 1 113 ? 8.35300   14.75400  31.71200  1.000 21.98957  ? 113 ASN BA O   1 
ATOM   3069 C  CB  . ASN B 1 113 ? 5.65300   14.30000  32.77300  1.000 21.72066  ? 113 ASN BA CB  1 
ATOM   3070 C  CG  . ASN B 1 113 ? 4.16100   14.04300  32.70700  1.000 29.06672  ? 113 ASN BA CG  1 
ATOM   3071 O  OD1 . ASN B 1 113 ? 3.48200   14.50000  31.78800  1.000 27.89385  ? 113 ASN BA OD1 1 
ATOM   3072 N  ND2 . ASN B 1 113 ? 3.64100   13.30900  33.68500  1.000 45.31893  ? 113 ASN BA ND2 1 
ATOM   3073 N  N   . VAL B 1 114 ? 8.75400   12.68000  32.47200  1.000 13.56103  ? 114 VAL BA N   1 
ATOM   3074 C  CA  . VAL B 1 114 ? 10.19600  12.86400  32.60300  1.000 13.17321  ? 114 VAL BA CA  1 
ATOM   3075 C  C   . VAL B 1 114 ? 10.88000  11.99300  31.55800  1.000 19.23079  ? 114 VAL BA C   1 
ATOM   3076 O  O   . VAL B 1 114 ? 10.68200  10.77200  31.53000  1.000 16.03100  ? 114 VAL BA O   1 
ATOM   3077 C  CB  . VAL B 1 114 ? 10.68600  12.52300  34.01700  1.000 14.49983  ? 114 VAL BA CB  1 
ATOM   3078 C  CG1 . VAL B 1 114 ? 12.20000  12.68100  34.10700  1.000 13.30513  ? 114 VAL BA CG1 1 
ATOM   3079 C  CG2 . VAL B 1 114 ? 9.98800   13.40300  35.04400  1.000 25.05375  ? 114 VAL BA CG2 1 
ATOM   3080 N  N   . ARG B 1 115 ? 11.68100  12.61800  30.70500  1.000 13.24578  ? 115 ARG BA N   1 
ATOM   3081 C  CA  . ARG B 1 115 ? 12.38300  11.95000  29.62000  1.000 12.95898  ? 115 ARG BA CA  1 
ATOM   3082 C  C   . ARG B 1 115 ? 13.81200  12.46000  29.57700  1.000 15.29779  ? 115 ARG BA C   1 
ATOM   3083 O  O   . ARG B 1 115 ? 14.09700  13.56800  30.05000  1.000 13.38272  ? 115 ARG BA O   1 
ATOM   3084 C  CB  . ARG B 1 115 ? 11.70000  12.20000  28.26700  1.000 7.54583   ? 115 ARG BA CB  1 
ATOM   3085 C  CG  . ARG B 1 115 ? 10.21200  11.88400  28.24100  1.000 7.23415   ? 115 ARG BA CG  1 
ATOM   3086 C  CD  . ARG B 1 115 ? 9.39800   13.14100  27.98400  1.000 17.25283  ? 115 ARG BA CD  1 
ATOM   3087 N  NE  . ARG B 1 115 ? 7.96900   12.92500  28.17400  1.000 10.60992  ? 115 ARG BA NE  1 
ATOM   3088 C  CZ  . ARG B 1 115 ? 7.03200   13.80900  27.85900  1.000 21.53477  ? 115 ARG BA CZ  1 
ATOM   3089 N  NH1 . ARG B 1 115 ? 7.34000   14.98800  27.34300  1.000 9.33154   ? 115 ARG BA NH1 1 
ATOM   3090 N  NH2 . ARG B 1 115 ? 5.75400   13.50000  28.06000  1.000 16.04601  ? 115 ARG BA NH2 1 
ATOM   3091 N  N   . PRO B 1 116 ? 14.74100  11.67500  29.02900  1.000 10.90097  ? 116 PRO BA N   1 
ATOM   3092 C  CA  . PRO B 1 116 ? 16.11600  12.16500  28.87200  1.000 11.83680  ? 116 PRO BA CA  1 
ATOM   3093 C  C   . PRO B 1 116 ? 16.15200  13.40900  27.99600  1.000 11.80365  ? 116 PRO BA C   1 
ATOM   3094 O  O   . PRO B 1 116 ? 15.57100  13.44000  26.90800  1.000 7.95402   ? 116 PRO BA O   1 
ATOM   3095 C  CB  . PRO B 1 116 ? 16.84200  10.98300  28.21900  1.000 11.30446  ? 116 PRO BA CB  1 
ATOM   3096 C  CG  . PRO B 1 116 ? 16.03300  9.78800   28.60500  1.000 16.57865  ? 116 PRO BA CG  1 
ATOM   3097 C  CD  . PRO B 1 116 ? 14.61100  10.26200  28.63200  1.000 14.06115  ? 116 PRO BA CD  1 
ATOM   3098 N  N   . ASP B 1 117 ? 16.83500  14.43900  28.48200  1.000 7.90132   ? 117 ASP BA N   1 
ATOM   3099 C  CA  . ASP B 1 117 ? 16.84200  15.74400  27.83100  1.000 11.12796  ? 117 ASP BA CA  1 
ATOM   3100 C  C   . ASP B 1 117 ? 18.29000  16.17800  27.61000  1.000 9.55181   ? 117 ASP BA C   1 
ATOM   3101 O  O   . ASP B 1 117 ? 19.23000  15.37700  27.69100  1.000 15.59791  ? 117 ASP BA O   1 
ATOM   3102 C  CB  . ASP B 1 117 ? 16.04300  16.75100  28.66600  1.000 9.68764   ? 117 ASP BA CB  1 
ATOM   3103 C  CG  . ASP B 1 117 ? 16.48900  16.79100  30.11900  1.000 11.96416  ? 117 ASP BA CG  1 
ATOM   3104 O  OD1 . ASP B 1 117 ? 17.44200  16.06600  30.47800  1.000 11.10879  ? 117 ASP BA OD1 1 
ATOM   3105 O  OD2 . ASP B 1 117 ? 15.88200  17.54600  30.90500  1.000 16.40522  ? 117 ASP BA OD2 1 
ATOM   3106 N  N   . LEU B 1 118 ? 18.48100  17.47200  27.33200  1.000 8.62229   ? 118 LEU BA N   1 
ATOM   3107 C  CA  . LEU B 1 118 ? 19.82500  18.00000  27.10700  1.000 13.34428  ? 118 LEU BA CA  1 
ATOM   3108 C  C   . LEU B 1 118 ? 20.72400  17.74500  28.31000  1.000 10.05529  ? 118 LEU BA C   1 
ATOM   3109 O  O   . LEU B 1 118 ? 21.87700  17.32300  28.16100  1.000 11.90714  ? 118 LEU BA O   1 
ATOM   3110 C  CB  . LEU B 1 118 ? 19.76100  19.49800  26.80000  1.000 17.11913  ? 118 LEU BA CB  1 
ATOM   3111 C  CG  . LEU B 1 118 ? 19.08300  19.95800  25.50900  1.000 12.69593  ? 118 LEU BA CG  1 
ATOM   3112 C  CD1 . LEU B 1 118 ? 19.06900  21.47800  25.43400  1.000 12.61739  ? 118 LEU BA CD1 1 
ATOM   3113 C  CD2 . LEU B 1 118 ? 19.78000  19.36700  24.29400  1.000 10.86614  ? 118 LEU BA CD2 1 
ATOM   3114 N  N   . ALA B 1 119 ? 20.20800  17.99600  29.51500  1.000 11.19901  ? 119 ALA BA N   1 
ATOM   3115 C  CA  . ALA B 1 119 ? 21.01300  17.81700  30.71800  1.000 15.87673  ? 119 ALA BA CA  1 
ATOM   3116 C  C   . ALA B 1 119 ? 21.36000  16.35000  30.94400  1.000 8.87923   ? 119 ALA BA C   1 
ATOM   3117 O  O   . ALA B 1 119 ? 22.51200  16.02200  31.25000  1.000 15.09772  ? 119 ALA BA O   1 
ATOM   3118 C  CB  . ALA B 1 119 ? 20.28000  18.38900  31.93100  1.000 5.78016   ? 119 ALA BA CB  1 
ATOM   3119 N  N   . MET B 1 120 ? 20.38100  15.45300  30.79200  1.000 9.50955   ? 120 MET BA N   1 
ATOM   3120 C  CA  . MET B 1 120 ? 20.63900  14.03700  31.03800  1.000 20.65473  ? 120 MET BA CA  1 
ATOM   3121 C  C   . MET B 1 120 ? 21.63700  13.47300  30.03400  1.000 16.25707  ? 120 MET BA C   1 
ATOM   3122 O  O   . MET B 1 120 ? 22.48000  12.64000  30.39000  1.000 12.67964  ? 120 MET BA O   1 
ATOM   3123 C  CB  . MET B 1 120 ? 19.33200  13.24500  31.00200  1.000 9.80415   ? 120 MET BA CB  1 
ATOM   3124 C  CG  . MET B 1 120 ? 19.51500  11.75200  31.23700  1.000 19.50435  ? 120 MET BA CG  1 
ATOM   3125 S  SD  . MET B 1 120 ? 18.01300  10.91800  31.77700  1.000 18.76122  ? 120 MET BA SD  1 
ATOM   3126 C  CE  . MET B 1 120 ? 17.51500  11.95400  33.14700  1.000 35.39370  ? 120 MET BA CE  1 
ATOM   3127 N  N   . GLY B 1 121 ? 21.56200  13.91500  28.77600  1.000 11.27573  ? 121 GLY BA N   1 
ATOM   3128 C  CA  . GLY B 1 121 ? 22.55700  13.49900  27.80100  1.000 5.91714   ? 121 GLY BA CA  1 
ATOM   3129 C  C   . GLY B 1 121 ? 23.95500  13.95400  28.17400  1.000 15.54878  ? 121 GLY BA C   1 
ATOM   3130 O  O   . GLY B 1 121 ? 24.93400  13.23800  27.94700  1.000 11.86641  ? 121 GLY BA O   1 
ATOM   3131 N  N   . ARG B 1 122 ? 24.06600  15.14700  28.76000  1.000 13.80642  ? 122 ARG BA N   1 
ATOM   3132 C  CA  . ARG B 1 122 ? 25.36500  15.62800  29.21400  1.000 14.08238  ? 122 ARG BA CA  1 
ATOM   3133 C  C   . ARG B 1 122 ? 25.87800  14.80700  30.39200  1.000 11.71259  ? 122 ARG BA C   1 
ATOM   3134 O  O   . ARG B 1 122 ? 27.07000  14.48300  30.45400  1.000 10.10252  ? 122 ARG BA O   1 
ATOM   3135 C  CB  . ARG B 1 122 ? 25.27500  17.10700  29.59000  1.000 16.50483  ? 122 ARG BA CB  1 
ATOM   3136 C  CG  . ARG B 1 122 ? 26.58500  17.69700  30.08500  1.000 20.24984  ? 122 ARG BA CG  1 
ATOM   3137 C  CD  . ARG B 1 122 ? 26.45500  19.18400  30.37500  1.000 22.52623  ? 122 ARG BA CD  1 
ATOM   3138 N  NE  . ARG B 1 122 ? 26.28800  19.96800  29.15600  1.000 24.24636  ? 122 ARG BA NE  1 
ATOM   3139 C  CZ  . ARG B 1 122 ? 27.21600  20.76700  28.64600  1.000 48.60905  ? 122 ARG BA CZ  1 
ATOM   3140 N  NH1 . ARG B 1 122 ? 28.40300  20.90100  29.21500  1.000 23.94717  ? 122 ARG BA NH1 1 
ATOM   3141 N  NH2 . ARG B 1 122 ? 26.94500  21.44600  27.53500  1.000 34.41863  ? 122 ARG BA NH2 1 
ATOM   3142 N  N   . ARG B 1 123 ? 24.99200  14.45900  31.33200  1.000 9.13517   ? 123 ARG BA N   1 
ATOM   3143 C  CA  . ARG B 1 123 ? 25.40700  13.68200  32.49800  1.000 12.45960  ? 123 ARG BA CA  1 
ATOM   3144 C  C   . ARG B 1 123 ? 25.99100  12.33600  32.08900  1.000 14.26244  ? 123 ARG BA C   1 
ATOM   3145 O  O   . ARG B 1 123 ? 26.98100  11.87900  32.67200  1.000 11.03816  ? 123 ARG BA O   1 
ATOM   3146 C  CB  . ARG B 1 123 ? 24.22700  13.47700  33.44800  1.000 10.78712  ? 123 ARG BA CB  1 
ATOM   3147 C  CG  . ARG B 1 123 ? 23.76900  14.73600  34.16600  1.000 24.37908  ? 123 ARG BA CG  1 
ATOM   3148 C  CD  . ARG B 1 123 ? 24.80900  15.23500  35.16300  1.000 20.47650  ? 123 ARG BA CD  1 
ATOM   3149 N  NE  . ARG B 1 123 ? 25.65500  16.28700  34.61000  1.000 20.74076  ? 123 ARG BA NE  1 
ATOM   3150 C  CZ  . ARG B 1 123 ? 25.24500  17.52000  34.34000  1.000 23.25213  ? 123 ARG BA CZ  1 
ATOM   3151 N  NH1 . ARG B 1 123 ? 23.99400  17.89700  34.55000  1.000 26.42071  ? 123 ARG BA NH1 1 
ATOM   3152 N  NH2 . ARG B 1 123 ? 26.11400  18.39900  33.84700  1.000 20.01097  ? 123 ARG BA NH2 1 
ATOM   3153 N  N   . ALA B 1 124 ? 25.38700  11.68400  31.09100  1.000 6.98282   ? 124 ALA BA N   1 
ATOM   3154 C  CA  . ALA B 1 124 ? 25.91100  10.40500  30.62100  1.000 6.94564   ? 124 ALA BA CA  1 
ATOM   3155 C  C   . ALA B 1 124 ? 27.30400  10.56600  30.02500  1.000 10.01690  ? 124 ALA BA C   1 
ATOM   3156 O  O   . ALA B 1 124 ? 28.17400  9.70900   30.22300  1.000 6.45183   ? 124 ALA BA O   1 
ATOM   3157 C  CB  . ALA B 1 124 ? 24.95600  9.79000   29.59700  1.000 8.18992   ? 124 ALA BA CB  1 
ATOM   3158 N  N   . CYS B 1 125 ? 27.53400  11.65800  29.29200  1.000 8.96019   ? 125 CYS BA N   1 
ATOM   3159 C  CA  . CYS B 1 125 ? 28.85400  11.90200  28.71900  1.000 6.43297   ? 125 CYS BA CA  1 
ATOM   3160 C  C   . CYS B 1 125 ? 29.89800  12.10800  29.80800  1.000 10.09287  ? 125 CYS BA C   1 
ATOM   3161 O  O   . CYS B 1 125 ? 31.01300  11.58200  29.71700  1.000 6.96826   ? 125 CYS BA O   1 
ATOM   3162 C  CB  . CYS B 1 125 ? 28.80700  13.11400  27.79200  1.000 14.70534  ? 125 CYS BA CB  1 
ATOM   3163 S  SG  . CYS B 1 125 ? 27.86500  12.86500  26.27500  1.000 16.61476  ? 125 CYS BA SG  1 
ATOM   3164 N  N   . GLU B 1 126 ? 29.55400  12.87200  30.84800  1.000 11.84538  ? 126 GLU BA N   1 
ATOM   3165 C  CA  . GLU B 1 126 ? 30.49500  13.11400  31.93600  1.000 16.90973  ? 126 GLU BA CA  1 
ATOM   3166 C  C   . GLU B 1 126 ? 30.86400  11.82400  32.65900  1.000 17.07302  ? 126 GLU BA C   1 
ATOM   3167 O  O   . GLU B 1 126 ? 31.97600  11.70600  33.18800  1.000 12.03358  ? 126 GLU BA O   1 
ATOM   3168 C  CB  . GLU B 1 126 ? 29.90500  14.12400  32.92200  1.000 9.11857   ? 126 GLU BA CB  1 
ATOM   3169 C  CG  . GLU B 1 126 ? 29.94900  15.56500  32.44000  1.000 21.93975  ? 126 GLU BA CG  1 
ATOM   3170 C  CD  . GLU B 1 126 ? 29.12300  16.50000  33.30700  1.000 29.46184  ? 126 GLU BA CD  1 
ATOM   3171 O  OE1 . GLU B 1 126 ? 28.50800  16.02500  34.28400  1.000 26.96311  ? 126 GLU BA OE1 1 
ATOM   3172 O  OE2 . GLU B 1 126 ? 29.08900  17.71300  33.00800  1.000 21.27964  ? 126 GLU BA OE2 1 
ATOM   3173 N  N   . ALA B 1 127 ? 29.95800  10.85000  32.68300  1.000 14.64053  ? 127 ALA BA N   1 
ATOM   3174 C  CA  . ALA B 1 127 ? 30.16900  9.59700   33.39500  1.000 13.44591  ? 127 ALA BA CA  1 
ATOM   3175 C  C   . ALA B 1 127 ? 30.84200  8.52500   32.54700  1.000 15.85466  ? 127 ALA BA C   1 
ATOM   3176 O  O   . ALA B 1 127 ? 31.12900  7.44100   33.06600  1.000 20.49141  ? 127 ALA BA O   1 
ATOM   3177 C  CB  . ALA B 1 127 ? 28.83200  9.06400   33.92200  1.000 13.53805  ? 127 ALA BA CB  1 
ATOM   3178 N  N   . ALA B 1 128 ? 31.10000  8.79400   31.26800  1.000 8.76804   ? 128 ALA BA N   1 
ATOM   3179 C  CA  . ALA B 1 128 ? 31.68200  7.79100   30.38300  1.000 12.79686  ? 128 ALA BA CA  1 
ATOM   3180 C  C   . ALA B 1 128 ? 33.11000  7.47500   30.81300  1.000 9.89574   ? 128 ALA BA C   1 
ATOM   3181 O  O   . ALA B 1 128 ? 33.95700  8.37200   30.88300  1.000 18.24690  ? 128 ALA BA O   1 
ATOM   3182 C  CB  . ALA B 1 128 ? 31.65100  8.28000   28.93700  1.000 10.78263  ? 128 ALA BA CB  1 
ATOM   3183 N  N   . LYS B 1 129 ? 33.37800  6.20600   31.08900  1.000 13.23688  ? 129 LYS BA N   1 
ATOM   3184 C  CA  . LYS B 1 129 ? 34.66900  5.76200   31.58900  1.000 13.14890  ? 129 LYS BA CA  1 
ATOM   3185 C  C   . LYS B 1 129 ? 34.99000  4.39100   31.01200  1.000 20.63133  ? 129 LYS BA C   1 
ATOM   3186 O  O   . LYS B 1 129 ? 34.08800  3.66300   30.58700  1.000 9.82061   ? 129 LYS BA O   1 
ATOM   3187 C  CB  . LYS B 1 129 ? 34.68000  5.70800   33.12300  1.000 21.23490  ? 129 LYS BA CB  1 
ATOM   3188 C  CG  . LYS B 1 129 ? 33.71800  4.69800   33.72800  1.000 27.21132  ? 129 LYS BA CG  1 
ATOM   3189 C  CD  . LYS B 1 129 ? 33.88900  4.62800   35.24000  1.000 47.57546  ? 129 LYS BA CD  1 
ATOM   3190 C  CE  . LYS B 1 129 ? 32.94600  3.61200   35.86800  1.000 36.01198  ? 129 LYS BA CE  1 
ATOM   3191 N  NZ  . LYS B 1 129 ? 32.87600  2.34800   35.08200  1.000 43.54851  ? 129 LYS BA NZ  1 
ATOM   3192 N  N   . PRO B 1 130 ? 36.27600  4.01700   30.97400  1.000 22.12684  ? 130 PRO BA N   1 
ATOM   3193 C  CA  . PRO B 1 130 ? 36.63100  2.66600   30.51900  1.000 16.64769  ? 130 PRO BA CA  1 
ATOM   3194 C  C   . PRO B 1 130 ? 36.33200  1.60900   31.57000  1.000 14.64266  ? 130 PRO BA C   1 
ATOM   3195 O  O   . PRO B 1 130 ? 35.72300  1.90300   32.60300  1.000 13.38632  ? 130 PRO BA O   1 
ATOM   3196 C  CB  . PRO B 1 130 ? 38.13600  2.77400   30.24500  1.000 19.05183  ? 130 PRO BA CB  1 
ATOM   3197 C  CG  . PRO B 1 130 ? 38.60000  3.84600   31.17300  1.000 13.94554  ? 130 PRO BA CG  1 
ATOM   3198 C  CD  . PRO B 1 130 ? 37.46900  4.83600   31.26000  1.000 19.61979  ? 130 PRO BA CD  1 
ATOM   3199 N  N   . GLY B 1 131 ? 36.75600  0.37500   31.31500  1.000 12.54702  ? 131 GLY BA N   1 
ATOM   3200 C  CA  . GLY B 1 131 ? 36.55400  -0.70400  32.25100  1.000 23.35738  ? 131 GLY BA CA  1 
ATOM   3201 C  C   . GLY B 1 131 ? 35.12400  -1.20200  32.26100  1.000 20.88774  ? 131 GLY BA C   1 
ATOM   3202 O  O   . GLY B 1 131 ? 34.31600  -0.86800  31.38900  1.000 21.93144  ? 131 GLY BA O   1 
ATOM   3203 N  N   . PRO B 1 132 ? 34.77900  -2.00600  33.26400  1.000 16.40546  ? 132 PRO BA N   1 
ATOM   3204 C  CA  . PRO B 1 132 ? 33.43900  -2.60200  33.30100  1.000 13.95755  ? 132 PRO BA CA  1 
ATOM   3205 C  C   . PRO B 1 132 ? 32.38800  -1.59700  33.74200  1.000 19.09944  ? 132 PRO BA C   1 
ATOM   3206 O  O   . PRO B 1 132 ? 32.63200  -0.74100  34.59500  1.000 17.67527  ? 132 PRO BA O   1 
ATOM   3207 C  CB  . PRO B 1 132 ? 33.58100  -3.74200  34.31900  1.000 18.59097  ? 132 PRO BA CB  1 
ATOM   3208 C  CG  . PRO B 1 132 ? 34.87200  -3.48400  35.06400  1.000 19.77883  ? 132 PRO BA CG  1 
ATOM   3209 C  CD  . PRO B 1 132 ? 35.54900  -2.27800  34.48700  1.000 11.93577  ? 132 PRO BA CD  1 
ATOM   3210 N  N   . PHE B 1 133 ? 31.20500  -1.70900  33.14400  1.000 14.59948  ? 133 PHE BA N   1 
ATOM   3211 C  CA  . PHE B 1 133 ? 30.08300  -0.84500  33.46900  1.000 16.16094  ? 133 PHE BA CA  1 
ATOM   3212 C  C   . PHE B 1 133 ? 28.93900  -1.67200  34.04000  1.000 12.96190  ? 133 PHE BA C   1 
ATOM   3213 O  O   . PHE B 1 133 ? 28.89000  -2.89600  33.89100  1.000 12.87583  ? 133 PHE BA O   1 
ATOM   3214 C  CB  . PHE B 1 133 ? 29.60400  -0.05300  32.24100  1.000 11.94236  ? 133 PHE BA CB  1 
ATOM   3215 C  CG  . PHE B 1 133 ? 29.38400  -0.89400  31.01000  1.000 13.62471  ? 133 PHE BA CG  1 
ATOM   3216 C  CD1 . PHE B 1 133 ? 28.18300  -1.55700  30.80900  1.000 10.75256  ? 133 PHE BA CD1 1 
ATOM   3217 C  CD2 . PHE B 1 133 ? 30.37000  -1.00100  30.04300  1.000 10.28844  ? 133 PHE BA CD2 1 
ATOM   3218 C  CE1 . PHE B 1 133 ? 27.97700  -2.32500  29.67300  1.000 13.94460  ? 133 PHE BA CE1 1 
ATOM   3219 C  CE2 . PHE B 1 133 ? 30.16900  -1.76400  28.90400  1.000 11.47283  ? 133 PHE BA CE2 1 
ATOM   3220 C  CZ  . PHE B 1 133 ? 28.97200  -2.42800  28.72000  1.000 9.46762   ? 133 PHE BA CZ  1 
ATOM   3221 N  N   . GLU B 1 134 ? 28.01700  -0.98300  34.70400  1.000 10.55139  ? 134 GLU BA N   1 
ATOM   3222 C  CA  . GLU B 1 134 ? 26.87200  -1.64700  35.30800  1.000 17.33737  ? 134 GLU BA CA  1 
ATOM   3223 C  C   . GLU B 1 134 ? 25.89400  -2.11000  34.23300  1.000 17.83574  ? 134 GLU BA C   1 
ATOM   3224 O  O   . GLU B 1 134 ? 25.77900  -1.50800  33.16200  1.000 10.58299  ? 134 GLU BA O   1 
ATOM   3225 C  CB  . GLU B 1 134 ? 26.17100  -0.70600  36.28700  1.000 13.73815  ? 134 GLU BA CB  1 
ATOM   3226 C  CG  . GLU B 1 134 ? 25.39000  -1.40400  37.38800  1.000 43.68231  ? 134 GLU BA CG  1 
ATOM   3227 C  CD  . GLU B 1 134 ? 24.92700  -0.44100  38.46700  1.000 72.78384  ? 134 GLU BA CD  1 
ATOM   3228 O  OE1 . GLU B 1 134 ? 25.72900  0.42600   38.87500  1.000 60.52735  ? 134 GLU BA OE1 1 
ATOM   3229 O  OE2 . GLU B 1 134 ? 23.76100  -0.54800  38.90500  1.000 51.01466  ? 134 GLU BA OE2 1 
ATOM   3230 N  N   . ARG B 1 135 ? 25.18600  -3.19600  34.53000  1.000 11.64423  ? 135 ARG BA N   1 
ATOM   3231 C  CA  . ARG B 1 135 ? 24.19800  -3.76100  33.62500  1.000 9.11987   ? 135 ARG BA CA  1 
ATOM   3232 C  C   . ARG B 1 135 ? 22.88200  -3.94400  34.36800  1.000 13.04836  ? 135 ARG BA C   1 
ATOM   3233 O  O   . ARG B 1 135 ? 22.80800  -3.81700  35.59200  1.000 14.76663  ? 135 ARG BA O   1 
ATOM   3234 C  CB  . ARG B 1 135 ? 24.67700  -5.09400  33.03500  1.000 9.76414   ? 135 ARG BA CB  1 
ATOM   3235 C  CG  . ARG B 1 135 ? 25.87700  -4.96200  32.11200  1.000 11.11047  ? 135 ARG BA CG  1 
ATOM   3236 C  CD  . ARG B 1 135 ? 27.07400  -5.71700  32.66200  1.000 19.32397  ? 135 ARG BA CD  1 
ATOM   3237 N  NE  . ARG B 1 135 ? 26.87000  -7.16000  32.62200  1.000 18.61159  ? 135 ARG BA NE  1 
ATOM   3238 C  CZ  . ARG B 1 135 ? 27.63800  -8.04300  33.24600  1.000 36.53708  ? 135 ARG BA CZ  1 
ATOM   3239 N  NH1 . ARG B 1 135 ? 28.67500  -7.66400  33.97500  1.000 27.23567  ? 135 ARG BA NH1 1 
ATOM   3240 N  NH2 . ARG B 1 135 ? 27.35600  -9.33800  33.13900  1.000 27.33054  ? 135 ARG BA NH2 1 
ATOM   3241 N  N   . GLY B 1 136 ? 21.83200  -4.24500  33.60900  1.000 19.10373  ? 136 GLY BA N   1 
ATOM   3242 C  CA  . GLY B 1 136 ? 20.50900  -4.39100  34.18300  1.000 16.73553  ? 136 GLY BA CA  1 
ATOM   3243 C  C   . GLY B 1 136 ? 19.64200  -3.16700  33.97500  1.000 16.34116  ? 136 GLY BA C   1 
ATOM   3244 O  O   . GLY B 1 136 ? 19.73800  -2.49900  32.94100  1.000 12.20595  ? 136 GLY BA O   1 
ATOM   3245 N  N   . ARG B 1 137 ? 18.79200  -2.85700  34.95600  1.000 14.94011  ? 137 ARG BA N   1 
ATOM   3246 C  CA  . ARG B 1 137 ? 17.88300  -1.71400  34.86900  1.000 19.52224  ? 137 ARG BA CA  1 
ATOM   3247 C  C   . ARG B 1 137 ? 18.64700  -0.43200  35.20300  1.000 17.56326  ? 137 ARG BA C   1 
ATOM   3248 O  O   . ARG B 1 137 ? 18.48500  0.18500   36.25900  1.000 11.34587  ? 137 ARG BA O   1 
ATOM   3249 C  CB  . ARG B 1 137 ? 16.68700  -1.91400  35.78900  1.000 19.27053  ? 137 ARG BA CB  1 
ATOM   3250 C  CG  . ARG B 1 137 ? 15.94200  -3.21500  35.54700  1.000 25.35390  ? 137 ARG BA CG  1 
ATOM   3251 C  CD  . ARG B 1 137 ? 14.57800  -2.95100  34.94400  1.000 24.97350  ? 137 ARG BA CD  1 
ATOM   3252 N  NE  . ARG B 1 137 ? 13.52800  -2.94900  35.95400  1.000 49.18655  ? 137 ARG BA NE  1 
ATOM   3253 C  CZ  . ARG B 1 137 ? 12.27900  -2.56100  35.73400  1.000 58.00123  ? 137 ARG BA CZ  1 
ATOM   3254 N  NH1 . ARG B 1 137 ? 11.89100  -2.12200  34.54700  1.000 31.36479  ? 137 ARG BA NH1 1 
ATOM   3255 N  NH2 . ARG B 1 137 ? 11.39900  -2.61100  36.73000  1.000 34.10838  ? 137 ARG BA NH2 1 
ATOM   3256 N  N   . VAL B 1 138 ? 19.49700  -0.03100  34.26100  1.000 11.03331  ? 138 VAL BA N   1 
ATOM   3257 C  CA  . VAL B 1 138 ? 20.35700  1.13400   34.42300  1.000 5.06853   ? 138 VAL BA CA  1 
ATOM   3258 C  C   . VAL B 1 138 ? 20.49900  1.82300   33.07200  1.000 20.20514  ? 138 VAL BA C   1 
ATOM   3259 O  O   . VAL B 1 138 ? 20.39300  1.19000   32.01600  1.000 11.15564  ? 138 VAL BA O   1 
ATOM   3260 C  CB  . VAL B 1 138 ? 21.73600  0.74000   35.00300  1.000 10.83065  ? 138 VAL BA CB  1 
ATOM   3261 C  CG1 . VAL B 1 138 ? 22.61500  0.10300   33.93200  1.000 12.33493  ? 138 VAL BA CG1 1 
ATOM   3262 C  CG2 . VAL B 1 138 ? 22.42000  1.94100   35.63400  1.000 23.38339  ? 138 VAL BA CG2 1 
ATOM   3263 N  N   . GLY B 1 139 ? 20.72200  3.13700   33.11400  1.000 11.98866  ? 139 GLY BA N   1 
ATOM   3264 C  CA  . GLY B 1 139 ? 20.90900  3.89700   31.88800  1.000 7.23559   ? 139 GLY BA CA  1 
ATOM   3265 C  C   . GLY B 1 139 ? 19.70500  3.77900   30.97300  1.000 15.99910  ? 139 GLY BA C   1 
ATOM   3266 O  O   . GLY B 1 139 ? 18.55400  3.95400   31.39100  1.000 8.85878   ? 139 GLY BA O   1 
ATOM   3267 N  N   . GLY B 1 140 ? 19.97000  3.45900   29.70400  1.000 6.15129   ? 140 GLY BA N   1 
ATOM   3268 C  CA  . GLY B 1 140 ? 18.90200  3.30700   28.73000  1.000 5.46652   ? 140 GLY BA CA  1 
ATOM   3269 C  C   . GLY B 1 140 ? 17.94800  2.16800   29.02900  1.000 4.69955   ? 140 GLY BA C   1 
ATOM   3270 O  O   . GLY B 1 140 ? 16.83200  2.15100   28.50000  1.000 4.39465   ? 140 GLY BA O   1 
ATOM   3271 N  N   . GLY B 1 141 ? 18.35900  1.21300   29.85700  1.000 6.98207   ? 141 GLY BA N   1 
ATOM   3272 C  CA  . GLY B 1 141 ? 17.51800  0.09800   30.24000  1.000 11.61891  ? 141 GLY BA CA  1 
ATOM   3273 C  C   . GLY B 1 141 ? 16.75500  0.27300   31.53600  1.000 8.25518   ? 141 GLY BA C   1 
ATOM   3274 O  O   . GLY B 1 141 ? 16.17400  -0.70300  32.02600  1.000 12.15664  ? 141 GLY BA O   1 
ATOM   3275 N  N   . THR B 1 142 ? 16.72100  1.48500   32.10200  1.000 9.43939   ? 142 THR BA N   1 
ATOM   3276 C  CA  . THR B 1 142 ? 16.12400  1.67900   33.42200  1.000 11.14713  ? 142 THR BA CA  1 
ATOM   3277 C  C   . THR B 1 142 ? 14.63400  1.35600   33.41900  1.000 12.25138  ? 142 THR BA C   1 
ATOM   3278 O  O   . THR B 1 142 ? 14.13600  0.68800   34.33300  1.000 17.61422  ? 142 THR BA O   1 
ATOM   3279 C  CB  . THR B 1 142 ? 16.35900  3.11300   33.89800  1.000 15.30565  ? 142 THR BA CB  1 
ATOM   3280 O  OG1 . THR B 1 142 ? 17.76600  3.39300   33.89200  1.000 11.00775  ? 142 THR BA OG1 1 
ATOM   3281 C  CG2 . THR B 1 142 ? 15.82100  3.30700   35.31300  1.000 10.33165  ? 142 THR BA CG2 1 
ATOM   3282 N  N   . GLY B 1 143 ? 13.90800  1.81000   32.40000  1.000 12.92269  ? 143 GLY BA N   1 
ATOM   3283 C  CA  . GLY B 1 143 ? 12.48000  1.56800   32.33100  1.000 11.30148  ? 143 GLY BA CA  1 
ATOM   3284 C  C   . GLY B 1 143 ? 12.08100  0.53100   31.30100  1.000 16.63635  ? 143 GLY BA C   1 
ATOM   3285 O  O   . GLY B 1 143 ? 10.94000  0.52400   30.82700  1.000 18.70080  ? 143 GLY BA O   1 
ATOM   3286 N  N   . ALA B 1 144 ? 13.00800  -0.35700  30.95000  1.000 14.74519  ? 144 ALA BA N   1 
ATOM   3287 C  CA  . ALA B 1 144 ? 12.75100  -1.35600  29.92200  1.000 13.78630  ? 144 ALA BA CA  1 
ATOM   3288 C  C   . ALA B 1 144 ? 11.87400  -2.48000  30.46000  1.000 19.23052  ? 144 ALA BA C   1 
ATOM   3289 O  O   . ALA B 1 144 ? 12.00400  -2.89300  31.61700  1.000 15.98562  ? 144 ALA BA O   1 
ATOM   3290 C  CB  . ALA B 1 144 ? 14.06800  -1.92700  29.39400  1.000 7.14575   ? 144 ALA BA CB  1 
ATOM   3291 N  N   . THR B 1 145 ? 10.97300  -2.97000  29.61000  1.000 14.10329  ? 145 THR BA N   1 
ATOM   3292 C  CA  . THR B 1 145 ? 10.08700  -4.07600  29.94800  1.000 13.60410  ? 145 THR BA CA  1 
ATOM   3293 C  C   . THR B 1 145 ? 10.05600  -5.05600  28.78200  1.000 18.40227  ? 145 THR BA C   1 
ATOM   3294 O  O   . THR B 1 145 ? 10.35000  -4.69800  27.64000  1.000 11.16137  ? 145 THR BA O   1 
ATOM   3295 C  CB  . THR B 1 145 ? 8.66500   -3.59500  30.27000  1.000 8.78426   ? 145 THR BA CB  1 
ATOM   3296 O  OG1 . THR B 1 145 ? 8.20600   -2.72300  29.22900  1.000 11.98308  ? 145 THR BA OG1 1 
ATOM   3297 C  CG2 . THR B 1 145 ? 8.63600   -2.85400  31.59900  1.000 10.43902  ? 145 THR BA CG2 1 
ATOM   3298 N  N   . VAL B 1 146 ? 9.68600   -6.30100  29.07800  1.000 10.69659  ? 146 VAL BA N   1 
ATOM   3299 C  CA  . VAL B 1 146 ? 9.72300   -7.38600  28.10400  1.000 7.96587   ? 146 VAL BA CA  1 
ATOM   3300 C  C   . VAL B 1 146 ? 8.38800   -8.11900  28.12500  1.000 15.42571  ? 146 VAL BA C   1 
ATOM   3301 O  O   . VAL B 1 146 ? 7.89500   -8.48800  29.19700  1.000 15.68906  ? 146 VAL BA O   1 
ATOM   3302 C  CB  . VAL B 1 146 ? 10.88000  -8.36300  28.38900  1.000 8.04144   ? 146 VAL BA CB  1 
ATOM   3303 C  CG1 . VAL B 1 146 ? 10.75400  -9.61200  27.53000  1.000 8.02952   ? 146 VAL BA CG1 1 
ATOM   3304 C  CG2 . VAL B 1 146 ? 12.21900  -7.68000  28.15100  1.000 12.80097  ? 146 VAL BA CG2 1 
ATOM   3305 N  N   . GLY B 1 147 ? 7.81000   -8.33200  26.94400  1.000 6.89678   ? 147 GLY BA N   1 
ATOM   3306 C  CA  . GLY B 1 147 ? 6.57500   -9.08500  26.82300  1.000 10.65588  ? 147 GLY BA CA  1 
ATOM   3307 C  C   . GLY B 1 147 ? 5.34100   -8.28200  27.17700  1.000 15.34402  ? 147 GLY BA C   1 
ATOM   3308 O  O   . GLY B 1 147 ? 4.83900   -8.37200  28.30100  1.000 13.77753  ? 147 GLY BA O   1 
ATOM   3309 N  N   . LYS B 1 148 ? 4.83000   -7.50300  26.22200  1.000 9.66927   ? 148 LYS BA N   1 
ATOM   3310 C  CA  . LYS B 1 148 ? 3.73900   -6.57000  26.47600  1.000 13.31067  ? 148 LYS BA CA  1 
ATOM   3311 C  C   . LYS B 1 148 ? 2.46500   -6.93300  25.71600  1.000 17.37501  ? 148 LYS BA C   1 
ATOM   3312 O  O   . LYS B 1 148 ? 1.65700   -6.05500  25.40000  1.000 13.75860  ? 148 LYS BA O   1 
ATOM   3313 C  CB  . LYS B 1 148 ? 4.17500   -5.14700  26.13600  1.000 10.34994  ? 148 LYS BA CB  1 
ATOM   3314 C  CG  . LYS B 1 148 ? 4.94800   -4.46900  27.25600  1.000 23.27695  ? 148 LYS BA CG  1 
ATOM   3315 C  CD  . LYS B 1 148 ? 6.00600   -3.52400  26.71800  1.000 19.26185  ? 148 LYS BA CD  1 
ATOM   3316 C  CE  . LYS B 1 148 ? 7.28600   -4.25600  26.35900  1.000 16.11363  ? 148 LYS BA CE  1 
ATOM   3317 N  NZ  . LYS B 1 148 ? 8.41300   -3.30500  26.15000  1.000 15.61617  ? 148 LYS BA NZ  1 
ATOM   3318 N  N   . LEU B 1 149 ? 2.26700   -8.22200  25.42600  1.000 14.42468  ? 149 LEU BA N   1 
ATOM   3319 C  CA  . LEU B 1 149 ? 1.04900   -8.65200  24.74400  1.000 9.68301   ? 149 LEU BA CA  1 
ATOM   3320 C  C   . LEU B 1 149 ? -0.19600  -8.26400  25.53500  1.000 16.80822  ? 149 LEU BA C   1 
ATOM   3321 O  O   . LEU B 1 149 ? -1.20700  -7.85200  24.95400  1.000 15.84978  ? 149 LEU BA O   1 
ATOM   3322 C  CB  . LEU B 1 149 ? 1.08400   -10.16200 24.50800  1.000 14.19120  ? 149 LEU BA CB  1 
ATOM   3323 C  CG  . LEU B 1 149 ? -0.23100  -10.81100 24.06700  1.000 16.29092  ? 149 LEU BA CG  1 
ATOM   3324 C  CD1 . LEU B 1 149 ? -0.61500  -10.35500 22.66600  1.000 16.43518  ? 149 LEU BA CD1 1 
ATOM   3325 C  CD2 . LEU B 1 149 ? -0.13900  -12.32800 24.13600  1.000 10.17505  ? 149 LEU BA CD2 1 
ATOM   3326 N  N   . TYR B 1 150 ? -0.14000  -8.38700  26.86100  1.000 17.44645  ? 150 TYR BA N   1 
ATOM   3327 C  CA  . TYR B 1 150 ? -1.24100  -8.01000  27.73600  1.000 16.71521  ? 150 TYR BA CA  1 
ATOM   3328 C  C   . TYR B 1 150 ? -1.00100  -6.67400  28.42900  1.000 23.35711  ? 150 TYR BA C   1 
ATOM   3329 O  O   . TYR B 1 150 ? -1.57400  -6.42200  29.49500  1.000 18.72177  ? 150 TYR BA O   1 
ATOM   3330 C  CB  . TYR B 1 150 ? -1.48700  -9.10500  28.77600  1.000 21.45469  ? 150 TYR BA CB  1 
ATOM   3331 C  CG  . TYR B 1 150 ? -1.78400  -10.46300 28.18100  1.000 13.40467  ? 150 TYR BA CG  1 
ATOM   3332 C  CD1 . TYR B 1 150 ? -2.82700  -10.63600 27.28100  1.000 17.41759  ? 150 TYR BA CD1 1 
ATOM   3333 C  CD2 . TYR B 1 150 ? -1.02100  -11.57200 28.51900  1.000 16.53742  ? 150 TYR BA CD2 1 
ATOM   3334 C  CE1 . TYR B 1 150 ? -3.10400  -11.87600 26.73500  1.000 12.03048  ? 150 TYR BA CE1 1 
ATOM   3335 C  CE2 . TYR B 1 150 ? -1.28900  -12.81600 27.97700  1.000 12.42532  ? 150 TYR BA CE2 1 
ATOM   3336 C  CZ  . TYR B 1 150 ? -2.33100  -12.96200 27.08700  1.000 15.01017  ? 150 TYR BA CZ  1 
ATOM   3337 O  OH  . TYR B 1 150 ? -2.60000  -14.19900 26.54600  1.000 16.02724  ? 150 TYR BA OH  1 
ATOM   3338 N  N   . GLY B 1 151 ? -0.16800  -5.81400  27.85100  1.000 20.22935  ? 151 GLY BA N   1 
ATOM   3339 C  CA  . GLY B 1 151 ? 0.16100   -4.54500  28.46000  1.000 15.55510  ? 151 GLY BA CA  1 
ATOM   3340 C  C   . GLY B 1 151 ? 1.34300   -4.64400  29.40800  1.000 22.44957  ? 151 GLY BA C   1 
ATOM   3341 O  O   . GLY B 1 151 ? 1.79900   -5.72500  29.78900  1.000 18.94376  ? 151 GLY BA O   1 
ATOM   3342 N  N   . VAL B 1 152 ? 1.84300   -3.46900  29.80200  1.000 17.36391  ? 152 VAL BA N   1 
ATOM   3343 C  CA  . VAL B 1 152 ? 3.03200   -3.40800  30.64300  1.000 26.28731  ? 152 VAL BA CA  1 
ATOM   3344 C  C   . VAL B 1 152 ? 2.77100   -3.95100  32.04300  1.000 19.90450  ? 152 VAL BA C   1 
ATOM   3345 O  O   . VAL B 1 152 ? 3.71900   -4.32900  32.74200  1.000 17.82603  ? 152 VAL BA O   1 
ATOM   3346 C  CB  . VAL B 1 152 ? 3.56600   -1.96300  30.70400  1.000 21.14866  ? 152 VAL BA CB  1 
ATOM   3347 C  CG1 . VAL B 1 152 ? 2.85400   -1.16600  31.78800  1.000 20.42291  ? 152 VAL BA CG1 1 
ATOM   3348 C  CG2 . VAL B 1 152 ? 5.07000   -1.95900  30.92900  1.000 30.18971  ? 152 VAL BA CG2 1 
ATOM   3349 N  N   . ARG B 1 153 ? 1.50500   -4.01500  32.46700  1.000 20.95163  ? 153 ARG BA N   1 
ATOM   3350 C  CA  . ARG B 1 153 ? 1.19300   -4.49700  33.81000  1.000 31.28922  ? 153 ARG BA CA  1 
ATOM   3351 C  C   . ARG B 1 153 ? 1.55300   -5.96800  33.98000  1.000 23.00799  ? 153 ARG BA C   1 
ATOM   3352 O  O   . ARG B 1 153 ? 1.95100   -6.38400  35.07400  1.000 19.34093  ? 153 ARG BA O   1 
ATOM   3353 C  CB  . ARG B 1 153 ? -0.29000  -4.27200  34.11200  1.000 34.95597  ? 153 ARG BA CB  1 
ATOM   3354 C  CG  . ARG B 1 153 ? -0.59000  -3.76400  35.51900  1.000 60.02057  ? 153 ARG BA CG  1 
ATOM   3355 C  CD  . ARG B 1 153 ? -0.36300  -4.84000  36.57000  1.000 70.10096  ? 153 ARG BA CD  1 
ATOM   3356 N  NE  . ARG B 1 153 ? -1.35700  -5.90400  36.48800  1.000 90.64558  ? 153 ARG BA NE  1 
ATOM   3357 C  CZ  . ARG B 1 153 ? -2.42100  -6.00100  37.27400  1.000 93.41076  ? 153 ARG BA CZ  1 
ATOM   3358 N  NH1 . ARG B 1 153 ? -2.66400  -5.11100  38.22200  1.000 72.90465  ? 153 ARG BA NH1 1 
ATOM   3359 N  NH2 . ARG B 1 153 ? -3.26300  -7.01700  37.10400  1.000 79.41704  ? 153 ARG BA NH2 1 
ATOM   3360 N  N   . GLN B 1 154 ? 1.42900   -6.76500  32.92000  1.000 19.36845  ? 154 GLN BA N   1 
ATOM   3361 C  CA  . GLN B 1 154 ? 1.72600   -8.18900  32.96900  1.000 15.21644  ? 154 GLN BA CA  1 
ATOM   3362 C  C   . GLN B 1 154 ? 3.06300   -8.52800  32.31700  1.000 27.52508  ? 154 GLN BA C   1 
ATOM   3363 O  O   . GLN B 1 154 ? 3.27200   -9.67200  31.89900  1.000 22.47595  ? 154 GLN BA O   1 
ATOM   3364 C  CB  . GLN B 1 154 ? 0.59600   -8.98300  32.31200  1.000 14.72234  ? 154 GLN BA CB  1 
ATOM   3365 C  CG  . GLN B 1 154 ? -0.59800  -9.22300  33.22400  1.000 22.76651  ? 154 GLN BA CG  1 
ATOM   3366 C  CD  . GLN B 1 154 ? -1.80500  -9.76100  32.48100  1.000 30.07841  ? 154 GLN BA CD  1 
ATOM   3367 O  OE1 . GLN B 1 154 ? -2.78500  -9.04800  32.26500  1.000 31.48017  ? 154 GLN BA OE1 1 
ATOM   3368 N  NE2 . GLN B 1 154 ? -1.74000  -11.02800 32.08500  1.000 24.71920  ? 154 GLN BA NE2 1 
ATOM   3369 N  N   . SER B 1 155 ? 3.97200   -7.56300  32.23000  1.000 15.39973  ? 155 SER BA N   1 
ATOM   3370 C  CA  . SER B 1 155 ? 5.25000   -7.77200  31.57100  1.000 20.83167  ? 155 SER BA CA  1 
ATOM   3371 C  C   . SER B 1 155 ? 6.33000   -8.15300  32.58100  1.000 19.20830  ? 155 SER BA C   1 
ATOM   3372 O  O   . SER B 1 155 ? 6.14400   -8.07700  33.79700  1.000 20.08822  ? 155 SER BA O   1 
ATOM   3373 C  CB  . SER B 1 155 ? 5.66400   -6.51700  30.80200  1.000 21.05053  ? 155 SER BA CB  1 
ATOM   3374 O  OG  . SER B 1 155 ? 6.00900   -5.46600  31.69000  1.000 15.54474  ? 155 SER BA OG  1 
ATOM   3375 N  N   . SER B 1 156 ? 7.47600   -8.57500  32.05100  1.000 14.79887  ? 156 SER BA N   1 
ATOM   3376 C  CA  . SER B 1 156 ? 8.69600   -8.85700  32.78600  1.000 12.37196  ? 156 SER BA CA  1 
ATOM   3377 C  C   . SER B 1 156 ? 9.66700   -7.68800  32.66100  1.000 16.75561  ? 156 SER BA C   1 
ATOM   3378 O  O   . SER B 1 156 ? 9.60800   -6.92700  31.69100  1.000 15.32592  ? 156 SER BA O   1 
ATOM   3379 C  CB  . SER B 1 156 ? 9.36500   -10.13300 32.26200  1.000 9.80064   ? 156 SER BA CB  1 
ATOM   3380 O  OG  . SER B 1 156 ? 8.51400   -11.25600 32.41400  1.000 19.12380  ? 156 SER BA OG  1 
ATOM   3381 N  N   . PRO B 1 157 ? 10.56400  -7.50300  33.62700  1.000 13.52110  ? 157 PRO BA N   1 
ATOM   3382 C  CA  . PRO B 1 157 ? 11.52400  -6.39800  33.52500  1.000 15.34830  ? 157 PRO BA CA  1 
ATOM   3383 C  C   . PRO B 1 157 ? 12.55100  -6.65200  32.43200  1.000 14.86143  ? 157 PRO BA C   1 
ATOM   3384 O  O   . PRO B 1 157 ? 13.03400  -7.77300  32.25400  1.000 12.30145  ? 157 PRO BA O   1 
ATOM   3385 C  CB  . PRO B 1 157 ? 12.18300  -6.36300  34.91000  1.000 15.49830  ? 157 PRO BA CB  1 
ATOM   3386 C  CG  . PRO B 1 157 ? 11.31000  -7.20500  35.79500  1.000 16.43351  ? 157 PRO BA CG  1 
ATOM   3387 C  CD  . PRO B 1 157 ? 10.68800  -8.22400  34.90400  1.000 14.32768  ? 157 PRO BA CD  1 
ATOM   3388 N  N   . GLY B 1 158 ? 12.87300  -5.59400  31.69200  1.000 16.16420  ? 158 GLY BA N   1 
ATOM   3389 C  CA  . GLY B 1 158 ? 13.95800  -5.61200  30.73500  1.000 15.03576  ? 158 GLY BA CA  1 
ATOM   3390 C  C   . GLY B 1 158 ? 15.24800  -5.13100  31.36500  1.000 16.32125  ? 158 GLY BA C   1 
ATOM   3391 O  O   . GLY B 1 158 ? 15.44700  -5.21600  32.57900  1.000 13.01964  ? 158 GLY BA O   1 
ATOM   3392 N  N   . GLY B 1 159 ? 16.13600  -4.61300  30.52500  1.000 7.13848   ? 159 GLY BA N   1 
ATOM   3393 C  CA  . GLY B 1 159 ? 17.36300  -4.03600  31.03000  1.000 6.21776   ? 159 GLY BA CA  1 
ATOM   3394 C  C   . GLY B 1 159 ? 18.39100  -3.86000  29.93000  1.000 17.24116  ? 159 GLY BA C   1 
ATOM   3395 O  O   . GLY B 1 159 ? 18.09500  -3.98900  28.73900  1.000 8.79325   ? 159 GLY BA O   1 
ATOM   3396 N  N   . LEU B 1 160 ? 19.60800  -3.54800  30.36600  1.000 10.01336  ? 160 LEU BA N   1 
ATOM   3397 C  CA  . LEU B 1 160 ? 20.75700  -3.36800  29.49000  1.000 10.85602  ? 160 LEU BA CA  1 
ATOM   3398 C  C   . LEU B 1 160 ? 21.73400  -4.51100  29.72800  1.000 13.46756  ? 160 LEU BA C   1 
ATOM   3399 O  O   . LEU B 1 160 ? 22.07200  -4.81000  30.87800  1.000 10.54649  ? 160 LEU BA O   1 
ATOM   3400 C  CB  . LEU B 1 160 ? 21.43500  -2.01900  29.75100  1.000 17.93012  ? 160 LEU BA CB  1 
ATOM   3401 C  CG  . LEU B 1 160 ? 22.65800  -1.62700  28.91400  1.000 10.20327  ? 160 LEU BA CG  1 
ATOM   3402 C  CD1 . LEU B 1 160 ? 22.61200  -0.14600  28.57900  1.000 11.35659  ? 160 LEU BA CD1 1 
ATOM   3403 C  CD2 . LEU B 1 160 ? 23.96400  -1.97300  29.62700  1.000 2.82201   ? 160 LEU BA CD2 1 
ATOM   3404 N  N   . GLY B 1 161 ? 22.18000  -5.15200  28.64300  1.000 7.70681   ? 161 GLY BA N   1 
ATOM   3405 C  CA  . GLY B 1 161 ? 23.10500  -6.25900  28.74000  1.000 5.82071   ? 161 GLY BA CA  1 
ATOM   3406 C  C   . GLY B 1 161 ? 24.28400  -6.06900  27.80300  1.000 6.90104   ? 161 GLY BA C   1 
ATOM   3407 O  O   . GLY B 1 161 ? 24.25700  -5.23400  26.89600  1.000 10.44153  ? 161 GLY BA O   1 
ATOM   3408 N  N   . THR B 1 162 ? 25.32600  -6.86500  28.03800  1.000 7.89014   ? 162 THR BA N   1 
ATOM   3409 C  CA  . THR B 1 162 ? 26.54300  -6.78100  27.24400  1.000 6.96812   ? 162 THR BA CA  1 
ATOM   3410 C  C   . THR B 1 162 ? 27.22800  -8.14100  27.22700  1.000 12.44676  ? 162 THR BA C   1 
ATOM   3411 O  O   . THR B 1 162 ? 27.01800  -8.97500  28.11200  1.000 8.48673   ? 162 THR BA O   1 
ATOM   3412 C  CB  . THR B 1 162 ? 27.49600  -5.70200  27.78000  1.000 6.43175   ? 162 THR BA CB  1 
ATOM   3413 O  OG1 . THR B 1 162 ? 28.55900  -5.48900  26.84500  1.000 7.88236   ? 162 THR BA OG1 1 
ATOM   3414 C  CG2 . THR B 1 162 ? 28.08200  -6.12000  29.12000  1.000 9.86419   ? 162 THR BA CG2 1 
ATOM   3415 N  N   . ALA B 1 163 ? 28.05400  -8.35400  26.20300  1.000 10.10441  ? 163 ALA BA N   1 
ATOM   3416 C  CA  . ALA B 1 163 ? 28.76800  -9.61300  26.03800  1.000 10.46670  ? 163 ALA BA CA  1 
ATOM   3417 C  C   . ALA B 1 163 ? 29.90100  -9.41800  25.04200  1.000 11.36928  ? 163 ALA BA C   1 
ATOM   3418 O  O   . ALA B 1 163 ? 29.82700  -8.55900  24.16000  1.000 16.28706  ? 163 ALA BA O   1 
ATOM   3419 C  CB  . ALA B 1 163 ? 27.83400  -10.73400 25.56700  1.000 6.35663   ? 163 ALA BA CB  1 
ATOM   3420 N  N   . THR B 1 164 ? 30.94700  -10.22900 25.19100  1.000 7.57768   ? 164 THR BA N   1 
ATOM   3421 C  CA  . THR B 1 164 ? 32.10600  -10.19500 24.30800  1.000 9.25305   ? 164 THR BA CA  1 
ATOM   3422 C  C   . THR B 1 164 ? 32.36500  -11.59400 23.77000  1.000 8.79917   ? 164 THR BA C   1 
ATOM   3423 O  O   . THR B 1 164 ? 32.37000  -12.56400 24.53400  1.000 8.57350   ? 164 THR BA O   1 
ATOM   3424 C  CB  . THR B 1 164 ? 33.35300  -9.67500  25.03600  1.000 9.19050   ? 164 THR BA CB  1 
ATOM   3425 O  OG1 . THR B 1 164 ? 33.17400  -8.29400  25.37400  1.000 13.25089  ? 164 THR BA OG1 1 
ATOM   3426 C  CG2 . THR B 1 164 ? 34.58900  -9.81900  24.15800  1.000 10.12552  ? 164 THR BA CG2 1 
ATOM   3427 N  N   . VAL B 1 165 ? 32.57300  -11.69300 22.45900  1.000 10.98278  ? 165 VAL BA N   1 
ATOM   3428 C  CA  . VAL B 1 165 ? 32.92100  -12.94400 21.79500  1.000 9.65349   ? 165 VAL BA CA  1 
ATOM   3429 C  C   . VAL B 1 165 ? 34.35200  -12.82900 21.28800  1.000 13.77001  ? 165 VAL BA C   1 
ATOM   3430 O  O   . VAL B 1 165 ? 34.69000  -11.87100 20.58100  1.000 19.92412  ? 165 VAL BA O   1 
ATOM   3431 C  CB  . VAL B 1 165 ? 31.95100  -13.26100 20.64400  1.000 12.88684  ? 165 VAL BA CB  1 
ATOM   3432 C  CG1 . VAL B 1 165 ? 32.42100  -14.48200 19.87000  1.000 14.18478  ? 165 VAL BA CG1 1 
ATOM   3433 C  CG2 . VAL B 1 165 ? 30.54500  -13.47000 21.18000  1.000 14.32008  ? 165 VAL BA CG2 1 
ATOM   3434 N  N   . SER B 1 166 ? 35.18800  -13.79900 21.64500  1.000 11.50803  ? 166 SER BA N   1 
ATOM   3435 C  CA  . SER B 1 166 ? 36.59500  -13.79500 21.26700  1.000 15.52011  ? 166 SER BA CA  1 
ATOM   3436 C  C   . SER B 1 166 ? 36.82300  -14.74400 20.09800  1.000 11.19925  ? 166 SER BA C   1 
ATOM   3437 O  O   . SER B 1 166 ? 36.33000  -15.87700 20.10400  1.000 21.57052  ? 166 SER BA O   1 
ATOM   3438 C  CB  . SER B 1 166 ? 37.48200  -14.19500 22.44800  1.000 12.17196  ? 166 SER BA CB  1 
ATOM   3439 O  OG  . SER B 1 166 ? 37.27300  -13.33500 23.55400  1.000 41.91688  ? 166 SER BA OG  1 
ATOM   3440 N  N   . LEU B 1 167 ? 37.56200  -14.27400 19.10000  1.000 14.52671  ? 167 LEU BA N   1 
ATOM   3441 C  CA  . LEU B 1 167 ? 37.96300  -15.07300 17.95500  1.000 20.06845  ? 167 LEU BA CA  1 
ATOM   3442 C  C   . LEU B 1 167 ? 39.47000  -15.31400 18.01700  1.000 16.60777  ? 167 LEU BA C   1 
ATOM   3443 O  O   . LEU B 1 167 ? 40.11800  -15.08300 19.04500  1.000 19.89570  ? 167 LEU BA O   1 
ATOM   3444 C  CB  . LEU B 1 167 ? 37.55100  -14.38000 16.65200  1.000 12.80680  ? 167 LEU BA CB  1 
ATOM   3445 C  CG  . LEU B 1 167 ? 36.10400  -13.89400 16.53600  1.000 32.29959  ? 167 LEU BA CG  1 
ATOM   3446 C  CD1 . LEU B 1 167 ? 35.81000  -13.41700 15.12100  1.000 28.63825  ? 167 LEU BA CD1 1 
ATOM   3447 C  CD2 . LEU B 1 167 ? 35.13000  -14.98400 16.94700  1.000 25.81874  ? 167 LEU BA CD2 1 
ATOM   3448 N  N   . TYR B 1 168 ? 40.03300  -15.77200 16.90500  1.000 17.94124  ? 168 TYR BA N   1 
ATOM   3449 C  CA  . TYR B 1 168 ? 41.46200  -16.02800 16.83700  1.000 20.04041  ? 168 TYR BA CA  1 
ATOM   3450 C  C   . TYR B 1 168 ? 42.24200  -14.72500 16.67400  1.000 20.73557  ? 168 TYR BA C   1 
ATOM   3451 O  O   . TYR B 1 168 ? 41.70500  -13.69000 16.26700  1.000 19.74193  ? 168 TYR BA O   1 
ATOM   3452 C  CB  . TYR B 1 168 ? 41.78100  -16.97300 15.67700  1.000 19.24021  ? 168 TYR BA CB  1 
ATOM   3453 C  CG  . TYR B 1 168 ? 41.35200  -16.44500 14.32600  1.000 18.84367  ? 168 TYR BA CG  1 
ATOM   3454 C  CD1 . TYR B 1 168 ? 40.07500  -16.68900 13.83600  1.000 19.61157  ? 168 TYR BA CD1 1 
ATOM   3455 C  CD2 . TYR B 1 168 ? 42.22300  -15.69900 13.54000  1.000 18.13248  ? 168 TYR BA CD2 1 
ATOM   3456 C  CE1 . TYR B 1 168 ? 39.67800  -16.20700 12.60300  1.000 16.30585  ? 168 TYR BA CE1 1 
ATOM   3457 C  CE2 . TYR B 1 168 ? 41.83400  -15.21300 12.30600  1.000 14.56554  ? 168 TYR BA CE2 1 
ATOM   3458 C  CZ  . TYR B 1 168 ? 40.56100  -15.47100 11.84300  1.000 20.48300  ? 168 TYR BA CZ  1 
ATOM   3459 O  OH  . TYR B 1 168 ? 40.16800  -14.99100 10.61500  1.000 21.07397  ? 168 TYR BA OH  1 
ATOM   3460 N  N   . GLY B 1 169 ? 43.52900  -14.79100 17.00600  1.000 17.20224  ? 169 GLY BA N   1 
ATOM   3461 C  CA  . GLY B 1 169 ? 44.44900  -13.70000 16.71900  1.000 16.59246  ? 169 GLY BA CA  1 
ATOM   3462 C  C   . GLY B 1 169 ? 44.14400  -12.39900 17.42500  1.000 16.63323  ? 169 GLY BA C   1 
ATOM   3463 O  O   . GLY B 1 169 ? 44.50800  -11.33000 16.92100  1.000 19.78515  ? 169 GLY BA O   1 
ATOM   3464 N  N   . GLY B 1 170 ? 43.49200  -12.45400 18.58300  1.000 15.98042  ? 170 GLY BA N   1 
ATOM   3465 C  CA  . GLY B 1 170 ? 43.15100  -11.24400 19.30100  1.000 14.35908  ? 170 GLY BA CA  1 
ATOM   3466 C  C   . GLY B 1 170 ? 41.93400  -10.51300 18.78500  1.000 22.29196  ? 170 GLY BA C   1 
ATOM   3467 O  O   . GLY B 1 170 ? 41.67400  -9.38700  19.22600  1.000 14.10765  ? 170 GLY BA O   1 
ATOM   3468 N  N   . ILE B 1 171 ? 41.18500  -11.10800 17.86300  1.000 13.58730  ? 171 ILE BA N   1 
ATOM   3469 C  CA  . ILE B 1 171 ? 39.97100  -10.48900 17.34600  1.000 14.62580  ? 171 ILE BA CA  1 
ATOM   3470 C  C   . ILE B 1 171 ? 38.86600  -10.61600 18.38400  1.000 9.67563   ? 171 ILE BA C   1 
ATOM   3471 O  O   . ILE B 1 171 ? 38.67700  -11.68000 18.98700  1.000 10.66663  ? 171 ILE BA O   1 
ATOM   3472 C  CB  . ILE B 1 171 ? 39.56100  -11.13700 16.01100  1.000 17.93918  ? 171 ILE BA CB  1 
ATOM   3473 C  CG1 . ILE B 1 171 ? 40.63100  -10.89100 14.94500  1.000 11.66114  ? 171 ILE BA CG1 1 
ATOM   3474 C  CG2 . ILE B 1 171 ? 38.21700  -10.60100 15.54600  1.000 13.29920  ? 171 ILE BA CG2 1 
ATOM   3475 C  CD1 . ILE B 1 171 ? 40.54900  -11.84100 13.77300  1.000 16.64341  ? 171 ILE BA CD1 1 
ATOM   3476 N  N   . LYS B 1 172 ? 38.13200  -9.52800  18.60100  1.000 9.61189   ? 172 LYS BA N   1 
ATOM   3477 C  CA  . LYS B 1 172 ? 37.02700  -9.51100  19.54600  1.000 16.51315  ? 172 LYS BA CA  1 
ATOM   3478 C  C   . LYS B 1 172 ? 35.81600  -8.84500  18.90900  1.000 23.98559  ? 172 LYS BA C   1 
ATOM   3479 O  O   . LYS B 1 172 ? 35.94400  -7.90700  18.11700  1.000 8.94616   ? 172 LYS BA O   1 
ATOM   3480 C  CB  . LYS B 1 172 ? 37.40300  -8.77600  20.83900  1.000 16.84581  ? 172 LYS BA CB  1 
ATOM   3481 C  CG  . LYS B 1 172 ? 38.25000  -9.59900  21.79400  1.000 15.66991  ? 172 LYS BA CG  1 
ATOM   3482 C  CD  . LYS B 1 172 ? 38.70100  -8.76900  22.98400  1.000 28.50595  ? 172 LYS BA CD  1 
ATOM   3483 C  CE  . LYS B 1 172 ? 40.01900  -9.27900  23.54300  1.000 47.53384  ? 172 LYS BA CE  1 
ATOM   3484 N  NZ  . LYS B 1 172 ? 40.10700  -10.76500 23.48800  1.000 51.61816  ? 172 LYS BA NZ  1 
ATOM   3485 N  N   . VAL B 1 173 ? 34.63500  -9.34600  19.25800  1.000 7.03820   ? 173 VAL BA N   1 
ATOM   3486 C  CA  . VAL B 1 173 ? 33.36900  -8.75700  18.84100  1.000 9.18162   ? 173 VAL BA CA  1 
ATOM   3487 C  C   . VAL B 1 173 ? 32.49200  -8.64200  20.07700  1.000 12.46833  ? 173 VAL BA C   1 
ATOM   3488 O  O   . VAL B 1 173 ? 32.20300  -9.65100  20.73200  1.000 11.49862  ? 173 VAL BA O   1 
ATOM   3489 C  CB  . VAL B 1 173 ? 32.66900  -9.58500  17.75000  1.000 7.08395   ? 173 VAL BA CB  1 
ATOM   3490 C  CG1 . VAL B 1 173 ? 31.30400  -8.99700  17.44500  1.000 14.15447  ? 173 VAL BA CG1 1 
ATOM   3491 C  CG2 . VAL B 1 173 ? 33.51900  -9.63600  16.48900  1.000 12.12727  ? 173 VAL BA CG2 1 
ATOM   3492 N  N   . SER B 1 174 ? 32.07700  -7.42100  20.40100  1.000 2.96639   ? 174 SER BA N   1 
ATOM   3493 C  CA  . SER B 1 174 ? 31.31800  -7.14700  21.60900  1.000 5.68103   ? 174 SER BA CA  1 
ATOM   3494 C  C   . SER B 1 174 ? 29.98800  -6.49500  21.25800  1.000 10.34068  ? 174 SER BA C   1 
ATOM   3495 O  O   . SER B 1 174 ? 29.82200  -5.90500  20.18800  1.000 12.45795  ? 174 SER BA O   1 
ATOM   3496 C  CB  . SER B 1 174 ? 32.10400  -6.24100  22.56600  1.000 8.93125   ? 174 SER BA CB  1 
ATOM   3497 O  OG  . SER B 1 174 ? 33.23400  -6.91500  23.09000  1.000 23.63974  ? 174 SER BA OG  1 
ATOM   3498 N  N   . ALA B 1 175 ? 29.03800  -6.60400  22.18400  1.000 8.02176   ? 175 ALA BA N   1 
ATOM   3499 C  CA  . ALA B 1 175 ? 27.71100  -6.04000  21.99900  1.000 13.72921  ? 175 ALA BA CA  1 
ATOM   3500 C  C   . ALA B 1 175 ? 27.22700  -5.43600  23.30800  1.000 12.45293  ? 175 ALA BA C   1 
ATOM   3501 O  O   . ALA B 1 175 ? 27.60300  -5.88500  24.39400  1.000 10.63204  ? 175 ALA BA O   1 
ATOM   3502 C  CB  . ALA B 1 175 ? 26.71100  -7.09800  21.51000  1.000 11.26609  ? 175 ALA BA CB  1 
ATOM   3503 N  N   . MET B 1 176 ? 26.40000  -4.39900  23.19300  1.000 10.86591  ? 176 MET BA N   1 
ATOM   3504 C  CA  . MET B 1 176 ? 25.68500  -3.83800  24.33500  1.000 9.29209   ? 176 MET BA CA  1 
ATOM   3505 C  C   . MET B 1 176 ? 24.26800  -3.53500  23.87700  1.000 11.25945  ? 176 MET BA C   1 
ATOM   3506 O  O   . MET B 1 176 ? 24.07300  -2.80700  22.89900  1.000 7.11617   ? 176 MET BA O   1 
ATOM   3507 C  CB  . MET B 1 176 ? 26.38100  -2.58600  24.88100  1.000 13.33589  ? 176 MET BA CB  1 
ATOM   3508 C  CG  . MET B 1 176 ? 25.47600  -1.64900  25.66500  1.000 8.89595   ? 176 MET BA CG  1 
ATOM   3509 S  SD  . MET B 1 176 ? 26.37500  -0.23600  26.34300  1.000 13.73153  ? 176 MET BA SD  1 
ATOM   3510 C  CE  . MET B 1 176 ? 25.94700  1.03500   25.15400  1.000 21.62609  ? 176 MET BA CE  1 
ATOM   3511 N  N   . ILE B 1 177 ? 23.28500  -4.10700  24.57000  1.000 4.94513   ? 177 ILE BA N   1 
ATOM   3512 C  CA  . ILE B 1 177 ? 21.91200  -4.18500  24.08400  1.000 7.52599   ? 177 ILE BA CA  1 
ATOM   3513 C  C   . ILE B 1 177 ? 20.95700  -3.72400  25.17700  1.000 9.93092   ? 177 ILE BA C   1 
ATOM   3514 O  O   . ILE B 1 177 ? 21.10700  -4.09900  26.34500  1.000 6.97343   ? 177 ILE BA O   1 
ATOM   3515 C  CB  . ILE B 1 177 ? 21.56000  -5.62200  23.63600  1.000 12.13474  ? 177 ILE BA CB  1 
ATOM   3516 C  CG1 . ILE B 1 177 ? 22.57200  -6.14000  22.60700  1.000 12.28006  ? 177 ILE BA CG1 1 
ATOM   3517 C  CG2 . ILE B 1 177 ? 20.14200  -5.69200  23.09700  1.000 9.93343   ? 177 ILE BA CG2 1 
ATOM   3518 C  CD1 . ILE B 1 177 ? 22.33700  -5.64100  21.19900  1.000 12.50877  ? 177 ILE BA CD1 1 
ATOM   3519 N  N   . VAL B 1 178 ? 19.97200  -2.91500  24.79400  1.000 6.33510   ? 178 VAL BA N   1 
ATOM   3520 C  CA  . VAL B 1 178 ? 18.84900  -2.56300  25.65700  1.000 6.59751   ? 178 VAL BA CA  1 
ATOM   3521 C  C   . VAL B 1 178 ? 17.63600  -3.34900  25.17800  1.000 14.23457  ? 178 VAL BA C   1 
ATOM   3522 O  O   . VAL B 1 178 ? 17.19700  -3.18700  24.03200  1.000 11.31608  ? 178 VAL BA O   1 
ATOM   3523 C  CB  . VAL B 1 178 ? 18.57100  -1.05200  25.63900  1.000 10.48764  ? 178 VAL BA CB  1 
ATOM   3524 C  CG1 . VAL B 1 178 ? 17.28100  -0.74400  26.38800  1.000 2.67402   ? 178 VAL BA CG1 1 
ATOM   3525 C  CG2 . VAL B 1 178 ? 19.74000  -0.28600  26.23600  1.000 9.23332   ? 178 VAL BA CG2 1 
ATOM   3526 N  N   . VAL B 1 179 ? 17.09200  -4.19800  26.04300  1.000 8.68616   ? 179 VAL BA N   1 
ATOM   3527 C  CA  . VAL B 1 179 ? 15.99500  -5.08900  25.68100  1.000 11.08830  ? 179 VAL BA CA  1 
ATOM   3528 C  C   . VAL B 1 179 ? 14.70100  -4.51300  26.24200  1.000 10.53890  ? 179 VAL BA C   1 
ATOM   3529 O  O   . VAL B 1 179 ? 14.49300  -4.48700  27.46000  1.000 7.72132   ? 179 VAL BA O   1 
ATOM   3530 C  CB  . VAL B 1 179 ? 16.23400  -6.51800  26.18600  1.000 16.38497  ? 179 VAL BA CB  1 
ATOM   3531 C  CG1 . VAL B 1 179 ? 15.14200  -7.44500  25.67100  1.000 9.40055   ? 179 VAL BA CG1 1 
ATOM   3532 C  CG2 . VAL B 1 179 ? 17.60200  -7.01000  25.74700  1.000 16.96583  ? 179 VAL BA CG2 1 
ATOM   3533 N  N   . ASN B 1 180 ? 13.83000  -4.05700  25.34500  1.000 5.58163   ? 180 ASN BA N   1 
ATOM   3534 C  CA  . ASN B 1 180 ? 12.49300  -3.55700  25.64600  1.000 12.81366  ? 180 ASN BA CA  1 
ATOM   3535 C  C   . ASN B 1 180 ? 11.48300  -4.22300  24.72000  1.000 11.26702  ? 180 ASN BA C   1 
ATOM   3536 O  O   . ASN B 1 180 ? 10.51800  -3.60600  24.25800  1.000 9.12522   ? 180 ASN BA O   1 
ATOM   3537 C  CB  . ASN B 1 180 ? 12.44500  -2.03400  25.52000  1.000 4.47984   ? 180 ASN BA CB  1 
ATOM   3538 C  CG  . ASN B 1 180 ? 11.15300  -1.43400  26.05600  1.000 10.56539  ? 180 ASN BA CG  1 
ATOM   3539 O  OD1 . ASN B 1 180 ? 10.77500  -1.66100  27.20400  1.000 5.95665   ? 180 ASN BA OD1 1 
ATOM   3540 N  ND2 . ASN B 1 180 ? 10.47000  -0.66300  25.21600  1.000 6.04852   ? 180 ASN BA ND2 1 
ATOM   3541 N  N   . SER B 1 181 ? 11.70300  -5.50400  24.43600  1.000 6.65889   ? 181 SER BA N   1 
ATOM   3542 C  CA  . SER B 1 181 ? 11.03900  -6.16500  23.32300  1.000 8.29416   ? 181 SER BA CA  1 
ATOM   3543 C  C   . SER B 1 181 ? 9.56600   -6.42200  23.61500  1.000 12.91704  ? 181 SER BA C   1 
ATOM   3544 O  O   . SER B 1 181 ? 9.16400   -6.66500  24.75700  1.000 11.08080  ? 181 SER BA O   1 
ATOM   3545 C  CB  . SER B 1 181 ? 11.73300  -7.48800  23.00600  1.000 12.19050  ? 181 SER BA CB  1 
ATOM   3546 O  OG  . SER B 1 181 ? 11.62200  -8.38600  24.09700  1.000 12.87825  ? 181 SER BA OG  1 
ATOM   3547 N  N   . PHE B 1 182 ? 8.75800   -6.37300  22.55400  1.000 10.71218  ? 182 PHE BA N   1 
ATOM   3548 C  CA  . PHE B 1 182 ? 7.36000   -6.76500  22.67900  1.000 14.73121  ? 182 PHE BA CA  1 
ATOM   3549 C  C   . PHE B 1 182 ? 7.23000   -8.26100  22.94000  1.000 13.44897  ? 182 PHE BA C   1 
ATOM   3550 O  O   . PHE B 1 182 ? 6.36100   -8.68800  23.70900  1.000 12.00861  ? 182 PHE BA O   1 
ATOM   3551 C  CB  . PHE B 1 182 ? 6.58700   -6.37300  21.41800  1.000 8.59425   ? 182 PHE BA CB  1 
ATOM   3552 C  CG  . PHE B 1 182 ? 5.23900   -7.02900  21.30700  1.000 20.37865  ? 182 PHE BA CG  1 
ATOM   3553 C  CD1 . PHE B 1 182 ? 4.15500   -6.53300  22.01300  1.000 12.07705  ? 182 PHE BA CD1 1 
ATOM   3554 C  CD2 . PHE B 1 182 ? 5.05500   -8.14400  20.50500  1.000 8.92272   ? 182 PHE BA CD2 1 
ATOM   3555 C  CE1 . PHE B 1 182 ? 2.91200   -7.13300  21.92100  1.000 15.96905  ? 182 PHE BA CE1 1 
ATOM   3556 C  CE2 . PHE B 1 182 ? 3.81400   -8.75100  20.41000  1.000 18.34007  ? 182 PHE BA CE2 1 
ATOM   3557 C  CZ  . PHE B 1 182 ? 2.74100   -8.24200  21.11900  1.000 9.76555   ? 182 PHE BA CZ  1 
ATOM   3558 N  N   . GLY B 1 183 ? 8.08500   -9.07200  22.31200  1.000 6.23064   ? 183 GLY BA N   1 
ATOM   3559 C  CA  . GLY B 1 183 ? 8.01100   -10.51200 22.43900  1.000 9.52185   ? 183 GLY BA CA  1 
ATOM   3560 C  C   . GLY B 1 183 ? 8.75100   -11.04400 23.65400  1.000 9.81651   ? 183 GLY BA C   1 
ATOM   3561 O  O   . GLY B 1 183 ? 9.26400   -10.30300 24.49100  1.000 8.64290   ? 183 GLY BA O   1 
ATOM   3562 N  N   . ASP B 1 184 ? 8.80300   -12.37200 23.73800  1.000 3.24577   ? 184 ASP BA N   1 
ATOM   3563 C  CA  . ASP B 1 184 ? 9.43800   -13.06200 24.85100  1.000 6.39670   ? 184 ASP BA CA  1 
ATOM   3564 C  C   . ASP B 1 184 ? 10.91800  -13.31200 24.57400  1.000 8.03550   ? 184 ASP BA C   1 
ATOM   3565 O  O   . ASP B 1 184 ? 11.36400  -13.36500 23.42600  1.000 12.66559  ? 184 ASP BA O   1 
ATOM   3566 C  CB  . ASP B 1 184 ? 8.74600   -14.39800 25.13600  1.000 8.80910   ? 184 ASP BA CB  1 
ATOM   3567 C  CG  . ASP B 1 184 ? 7.25700   -14.25100 25.36900  1.000 12.06926  ? 184 ASP BA CG  1 
ATOM   3568 O  OD1 . ASP B 1 184 ? 6.83500   -13.21000 25.91400  1.000 10.96001  ? 184 ASP BA OD1 1 
ATOM   3569 O  OD2 . ASP B 1 184 ? 6.50800   -15.18600 25.01500  1.000 9.83971   ? 184 ASP BA OD2 1 
ATOM   3570 N  N   . LEU B 1 185 ? 11.67400  -13.47900 25.65600  1.000 8.64573   ? 185 LEU BA N   1 
ATOM   3571 C  CA  . LEU B 1 185 ? 13.08900  -13.82300 25.59800  1.000 4.85453   ? 185 LEU BA CA  1 
ATOM   3572 C  C   . LEU B 1 185 ? 13.26100  -15.29900 25.92900  1.000 14.78009  ? 185 LEU BA C   1 
ATOM   3573 O  O   . LEU B 1 185 ? 12.75500  -15.77200 26.95300  1.000 14.55042  ? 185 LEU BA O   1 
ATOM   3574 C  CB  . LEU B 1 185 ? 13.90000  -12.97500 26.57700  1.000 13.01160  ? 185 LEU BA CB  1 
ATOM   3575 C  CG  . LEU B 1 185 ? 15.22200  -12.37900 26.08900  1.000 24.16331  ? 185 LEU BA CG  1 
ATOM   3576 C  CD1 . LEU B 1 185 ? 14.97300  -11.32600 25.03400  1.000 33.22494  ? 185 LEU BA CD1 1 
ATOM   3577 C  CD2 . LEU B 1 185 ? 16.01500  -11.80100 27.24800  1.000 33.23108  ? 185 LEU BA CD2 1 
ATOM   3578 N  N   . ARG B 1 186 ? 13.98100  -16.01900 25.07300  1.000 11.70597  ? 186 ARG BA N   1 
ATOM   3579 C  CA  . ARG B 1 186 ? 14.24100  -17.43700 25.26300  1.000 17.90818  ? 186 ARG BA CA  1 
ATOM   3580 C  C   . ARG B 1 186 ? 15.74200  -17.69800 25.27800  1.000 33.23075  ? 186 ARG BA C   1 
ATOM   3581 O  O   . ARG B 1 186 ? 16.53500  -16.93000 24.72400  1.000 19.61046  ? 186 ARG BA O   1 
ATOM   3582 C  CB  . ARG B 1 186 ? 13.58100  -18.27700 24.16100  1.000 29.83459  ? 186 ARG BA CB  1 
ATOM   3583 C  CG  . ARG B 1 186 ? 12.09000  -18.48600 24.34600  1.000 30.80649  ? 186 ARG BA CG  1 
ATOM   3584 C  CD  . ARG B 1 186 ? 11.50000  -19.27400 23.18900  1.000 28.21018  ? 186 ARG BA CD  1 
ATOM   3585 N  NE  . ARG B 1 186 ? 10.15000  -18.82900 22.86300  1.000 40.10838  ? 186 ARG BA NE  1 
ATOM   3586 C  CZ  . ARG B 1 186 ? 9.04400   -19.45200 23.24200  1.000 39.03249  ? 186 ARG BA CZ  1 
ATOM   3587 N  NH1 . ARG B 1 186 ? 9.08700   -20.55900 23.96500  1.000 44.64164  ? 186 ARG BA NH1 1 
ATOM   3588 N  NH2 . ARG B 1 186 ? 7.86300   -18.95200 22.88700  1.000 32.28621  ? 186 ARG BA NH2 1 
ATOM   3589 N  N   . ASP B 1 187 ? 16.12700  -18.79700 25.92100  1.000 27.77418  ? 187 ASP BA N   1 
ATOM   3590 C  CA  . ASP B 1 187 ? 17.52000  -19.21500 25.93900  1.000 30.98065  ? 187 ASP BA CA  1 
ATOM   3591 C  C   . ASP B 1 187 ? 17.80100  -20.08600 24.71400  1.000 46.03237  ? 187 ASP BA C   1 
ATOM   3592 O  O   . ASP B 1 187 ? 16.98000  -20.19600 23.79900  1.000 34.62117  ? 187 ASP BA O   1 
ATOM   3593 C  CB  . ASP B 1 187 ? 17.85400  -19.93500 27.24700  1.000 30.99172  ? 187 ASP BA CB  1 
ATOM   3594 C  CG  . ASP B 1 187 ? 16.87600  -21.05200 27.57700  1.000 44.59946  ? 187 ASP BA CG  1 
ATOM   3595 O  OD1 . ASP B 1 187 ? 16.22500  -21.58700 26.65400  1.000 45.40741  ? 187 ASP BA OD1 1 
ATOM   3596 O  OD2 . ASP B 1 187 ? 16.76700  -21.40400 28.77000  1.000 25.35570  ? 187 ASP BA OD2 1 
ATOM   3597 N  N   . THR B 1 188 ? 18.97500  -20.72200 24.69100  1.000 51.71892  ? 188 THR BA N   1 
ATOM   3598 C  CA  . THR B 1 188 ? 19.34600  -21.55000 23.54900  1.000 51.31531  ? 188 THR BA CA  1 
ATOM   3599 C  C   . THR B 1 188 ? 18.46800  -22.79000 23.44000  1.000 41.10869  ? 188 THR BA C   1 
ATOM   3600 O  O   . THR B 1 188 ? 18.27900  -23.31900 22.33900  1.000 53.10676  ? 188 THR BA O   1 
ATOM   3601 C  CB  . THR B 1 188 ? 20.81700  -21.95000 23.64700  1.000 68.12858  ? 188 THR BA CB  1 
ATOM   3602 O  OG1 . THR B 1 188 ? 21.05700  -22.58100 24.91100  1.000 66.72988  ? 188 THR BA OG1 1 
ATOM   3603 C  CG2 . THR B 1 188 ? 21.71000  -20.72200 23.52400  1.000 50.49107  ? 188 THR BA CG2 1 
ATOM   3604 N  N   . ALA B 1 189 ? 17.92400  -23.26600 24.56200  1.000 50.81563  ? 189 ALA BA N   1 
ATOM   3605 C  CA  . ALA B 1 189 ? 17.03700  -24.42300 24.52000  1.000 56.29215  ? 189 ALA BA CA  1 
ATOM   3606 C  C   . ALA B 1 189 ? 15.67800  -24.05100 23.94400  1.000 52.71854  ? 189 ALA BA C   1 
ATOM   3607 O  O   . ALA B 1 189 ? 15.19000  -24.69400 23.00700  1.000 64.17384  ? 189 ALA BA O   1 
ATOM   3608 C  CB  . ALA B 1 189 ? 16.88000  -25.01600 25.91900  1.000 48.58329  ? 189 ALA BA CB  1 
ATOM   3609 N  N   . GLY B 1 190 ? 15.04900  -23.01600 24.49500  1.000 36.00079  ? 190 GLY BA N   1 
ATOM   3610 C  CA  . GLY B 1 190 ? 13.74000  -22.59800 24.04000  1.000 34.92280  ? 190 GLY BA CA  1 
ATOM   3611 C  C   . GLY B 1 190 ? 12.80400  -22.25200 25.17900  1.000 30.11350  ? 190 GLY BA C   1 
ATOM   3612 O  O   . GLY B 1 190 ? 11.62000  -21.98600 24.95700  1.000 32.21163  ? 190 GLY BA O   1 
ATOM   3613 N  N   . ARG B 1 191 ? 13.32100  -22.25600 26.40500  1.000 32.45711  ? 191 ARG BA N   1 
ATOM   3614 C  CA  . ARG B 1 191 ? 12.51100  -21.91200 27.56400  1.000 33.52540  ? 191 ARG BA CA  1 
ATOM   3615 C  C   . ARG B 1 191 ? 12.42500  -20.40000 27.71700  1.000 31.58709  ? 191 ARG BA C   1 
ATOM   3616 O  O   . ARG B 1 191 ? 13.38800  -19.67500 27.44900  1.000 22.75711  ? 191 ARG BA O   1 
ATOM   3617 C  CB  . ARG B 1 191 ? 13.09100  -22.53200 28.83500  1.000 28.21148  ? 191 ARG BA CB  1 
ATOM   3618 C  CG  . ARG B 1 191 ? 14.06500  -23.66600 28.58500  1.000 61.93830  ? 191 ARG BA CG  1 
ATOM   3619 C  CD  . ARG B 1 191 ? 14.72400  -24.11200 29.87700  1.000 72.32692  ? 191 ARG BA CD  1 
ATOM   3620 N  NE  . ARG B 1 191 ? 16.06900  -24.62200 29.64500  1.000 71.17644  ? 191 ARG BA NE  1 
ATOM   3621 C  CZ  . ARG B 1 191 ? 16.99400  -24.74900 30.58700  1.000 81.89671  ? 191 ARG BA CZ  1 
ATOM   3622 N  NH1 . ARG B 1 191 ? 16.74200  -24.44400 31.85000  1.000 59.29439  ? 191 ARG BA NH1 1 
ATOM   3623 N  NH2 . ARG B 1 191 ? 18.20400  -25.18800 30.25200  1.000 88.29665  ? 191 ARG BA NH2 1 
ATOM   3624 N  N   . ILE B 1 192 ? 11.26300  -19.93000 28.15600  1.000 24.72513  ? 192 ILE BA N   1 
ATOM   3625 C  CA  . ILE B 1 192 ? 11.02100  -18.50200 28.32600  1.000 26.33567  ? 192 ILE BA CA  1 
ATOM   3626 C  C   . ILE B 1 192 ? 11.65800  -18.04600 29.63100  1.000 21.11317  ? 192 ILE BA C   1 
ATOM   3627 O  O   . ILE B 1 192 ? 11.31300  -18.54200 30.70900  1.000 33.39373  ? 192 ILE BA O   1 
ATOM   3628 C  CB  . ILE B 1 192 ? 9.51700   -18.19400 28.30900  1.000 15.74902  ? 192 ILE BA CB  1 
ATOM   3629 C  CG1 . ILE B 1 192 ? 8.91500   -18.57000 26.95300  1.000 15.90585  ? 192 ILE BA CG1 1 
ATOM   3630 C  CG2 . ILE B 1 192 ? 9.26800   -16.72700 28.63600  1.000 15.75750  ? 192 ILE BA CG2 1 
ATOM   3631 C  CD1 . ILE B 1 192 ? 7.40800   -18.71700 26.97300  1.000 18.53058  ? 192 ILE BA CD1 1 
ATOM   3632 N  N   . VAL B 1 193 ? 12.59200  -17.10000 29.53800  1.000 17.45851  ? 193 VAL BA N   1 
ATOM   3633 C  CA  . VAL B 1 193 ? 13.19800  -16.51000 30.72600  1.000 9.42813   ? 193 VAL BA CA  1 
ATOM   3634 C  C   . VAL B 1 193 ? 12.57300  -15.16700 31.09000  1.000 18.74599  ? 193 VAL BA C   1 
ATOM   3635 O  O   . VAL B 1 193 ? 12.67900  -14.74300 32.25100  1.000 20.22342  ? 193 VAL BA O   1 
ATOM   3636 C  CB  . VAL B 1 193 ? 14.72400  -16.36100 30.55300  1.000 20.62155  ? 193 VAL BA CB  1 
ATOM   3637 C  CG1 . VAL B 1 193 ? 15.35600  -17.70900 30.24700  1.000 27.04710  ? 193 VAL BA CG1 1 
ATOM   3638 C  CG2 . VAL B 1 193 ? 15.04400  -15.36100 29.45400  1.000 24.91420  ? 193 VAL BA CG2 1 
ATOM   3639 N  N   . ALA B 1 194 ? 11.92500  -14.49100 30.14300  1.000 19.12578  ? 194 ALA BA N   1 
ATOM   3640 C  CA  . ALA B 1 194 ? 11.24800  -13.23000 30.40500  1.000 12.21335  ? 194 ALA BA CA  1 
ATOM   3641 C  C   . ALA B 1 194 ? 10.23300  -12.99600 29.29700  1.000 14.65605  ? 194 ALA BA C   1 
ATOM   3642 O  O   . ALA B 1 194 ? 10.50600  -13.29600 28.13200  1.000 12.60197  ? 194 ALA BA O   1 
ATOM   3643 C  CB  . ALA B 1 194 ? 12.23800  -12.06200 30.48100  1.000 9.88773   ? 194 ALA BA CB  1 
ATOM   3644 N  N   . GLY B 1 195 ? 9.07000   -12.47300 29.66300  1.000 8.96864   ? 195 GLY BA N   1 
ATOM   3645 C  CA  . GLY B 1 195 ? 8.04300   -12.20400 28.67400  1.000 13.63127  ? 195 GLY BA CA  1 
ATOM   3646 C  C   . GLY B 1 195 ? 6.69600   -11.96100 29.33600  1.000 12.36293  ? 195 GLY BA C   1 
ATOM   3647 O  O   . GLY B 1 195 ? 6.61400   -11.71000 30.53700  1.000 14.84770  ? 195 GLY BA O   1 
ATOM   3648 N  N   . ALA B 1 196 ? 5.65300   -12.04200 28.51400  1.000 9.07554   ? 196 ALA BA N   1 
ATOM   3649 C  CA  . ALA B 1 196 ? 4.29800   -11.79300 28.98700  1.000 11.76495  ? 196 ALA BA CA  1 
ATOM   3650 C  C   . ALA B 1 196 ? 3.86200   -12.88200 29.95800  1.000 8.92078   ? 196 ALA BA C   1 
ATOM   3651 O  O   . ALA B 1 196 ? 4.11000   -14.07100 29.73800  1.000 14.61889  ? 196 ALA BA O   1 
ATOM   3652 C  CB  . ALA B 1 196 ? 3.33000   -11.71800 27.80800  1.000 14.04050  ? 196 ALA BA CB  1 
ATOM   3653 N  N   . LYS B 1 197 ? 3.20400   -12.46800 31.03600  1.000 13.32158  ? 197 LYS BA N   1 
ATOM   3654 C  CA  . LYS B 1 197 ? 2.82800   -13.36200 32.11900  1.000 16.37630  ? 197 LYS BA CA  1 
ATOM   3655 C  C   . LYS B 1 197 ? 1.32900   -13.29400 32.36500  1.000 21.83871  ? 197 LYS BA C   1 
ATOM   3656 O  O   . LYS B 1 197 ? 0.68900   -12.26300 32.13400  1.000 11.73577  ? 197 LYS BA O   1 
ATOM   3657 C  CB  . LYS B 1 197 ? 3.57400   -13.00700 33.41300  1.000 13.64081  ? 197 LYS BA CB  1 
ATOM   3658 C  CG  . LYS B 1 197 ? 5.03500   -13.41800 33.41800  1.000 25.15944  ? 197 LYS BA CG  1 
ATOM   3659 C  CD  . LYS B 1 197 ? 5.77400   -12.87800 34.63600  1.000 28.58358  ? 197 LYS BA CD  1 
ATOM   3660 C  CE  . LYS B 1 197 ? 5.39300   -11.43500 34.92900  1.000 43.35534  ? 197 LYS BA CE  1 
ATOM   3661 N  NZ  . LYS B 1 197 ? 6.06100   -10.92500 36.15900  1.000 44.36365  ? 197 LYS BA NZ  1 
ATOM   3662 N  N   . TYR B 1 198 ? 0.77400   -14.40700 32.83900  1.000 21.31770  ? 198 TYR BA N   1 
ATOM   3663 C  CA  . TYR B 1 198 ? -0.60000  -14.41000 33.30900  1.000 19.77357  ? 198 TYR BA CA  1 
ATOM   3664 C  C   . TYR B 1 198 ? -0.70000  -13.62500 34.61700  1.000 24.85079  ? 198 TYR BA C   1 
ATOM   3665 O  O   . TYR B 1 198 ? 0.30300   -13.19900 35.19900  1.000 13.60044  ? 198 TYR BA O   1 
ATOM   3666 C  CB  . TYR B 1 198 ? -1.09900  -15.84100 33.50200  1.000 13.00078  ? 198 TYR BA CB  1 
ATOM   3667 C  CG  . TYR B 1 198 ? -1.40700  -16.56300 32.21000  1.000 18.92845  ? 198 TYR BA CG  1 
ATOM   3668 C  CD1 . TYR B 1 198 ? -2.27100  -16.01300 31.27100  1.000 20.32571  ? 198 TYR BA CD1 1 
ATOM   3669 C  CD2 . TYR B 1 198 ? -0.83000  -17.79400 31.92700  1.000 18.91611  ? 198 TYR BA CD2 1 
ATOM   3670 C  CE1 . TYR B 1 198 ? -2.55400  -16.67000 30.08700  1.000 19.55565  ? 198 TYR BA CE1 1 
ATOM   3671 C  CE2 . TYR B 1 198 ? -1.10600  -18.45900 30.74400  1.000 17.63752  ? 198 TYR BA CE2 1 
ATOM   3672 C  CZ  . TYR B 1 198 ? -1.96900  -17.89300 29.82900  1.000 22.37249  ? 198 TYR BA CZ  1 
ATOM   3673 O  OH  . TYR B 1 198 ? -2.24700  -18.55100 28.65100  1.000 22.08812  ? 198 TYR BA OH  1 
ATOM   3674 N  N   . GLU B 1 199 ? -1.93900  -13.43900 35.08100  1.000 22.35149  ? 199 GLU BA N   1 
ATOM   3675 C  CA  . GLU B 1 199 ? -2.17100  -12.67500 36.30400  1.000 21.60657  ? 199 GLU BA CA  1 
ATOM   3676 C  C   . GLU B 1 199 ? -1.40700  -13.25500 37.48900  1.000 25.89463  ? 199 GLU BA C   1 
ATOM   3677 O  O   . GLU B 1 199 ? -0.93600  -12.50300 38.35000  1.000 22.47085  ? 199 GLU BA O   1 
ATOM   3678 C  CB  . GLU B 1 199 ? -3.67000  -12.62400 36.60600  1.000 20.03235  ? 199 GLU BA CB  1 
ATOM   3679 C  CG  . GLU B 1 199 ? -4.03900  -11.82600 37.84600  1.000 37.00920  ? 199 GLU BA CG  1 
ATOM   3680 C  CD  . GLU B 1 199 ? -5.40300  -12.20200 38.39300  1.000 61.31242  ? 199 GLU BA CD  1 
ATOM   3681 O  OE1 . GLU B 1 199 ? -6.34600  -12.35200 37.58600  1.000 62.82579  ? 199 GLU BA OE1 1 
ATOM   3682 O  OE2 . GLU B 1 199 ? -5.53400  -12.34900 39.62600  1.000 52.94106  ? 199 GLU BA OE2 1 
ATOM   3683 N  N   . GLY B 1 200 ? -1.25700  -14.57900 37.54100  1.000 22.54795  ? 200 GLY BA N   1 
ATOM   3684 C  CA  . GLY B 1 200 ? -0.57400  -15.22100 38.64800  1.000 20.96968  ? 200 GLY BA CA  1 
ATOM   3685 C  C   . GLY B 1 200 ? 0.93400   -15.28400 38.54100  1.000 23.52876  ? 200 GLY BA C   1 
ATOM   3686 O  O   . GLY B 1 200 ? 1.59100   -15.64900 39.52000  1.000 24.73332  ? 200 GLY BA O   1 
ATOM   3687 N  N   . GLY B 1 201 ? 1.50100   -14.94900 37.38600  1.000 20.38813  ? 201 GLY BA N   1 
ATOM   3688 C  CA  . GLY B 1 201 ? 2.94200   -14.94400 37.20200  1.000 14.66218  ? 201 GLY BA CA  1 
ATOM   3689 C  C   . GLY B 1 201 ? 3.47900   -15.97600 36.23000  1.000 18.98406  ? 201 GLY BA C   1 
ATOM   3690 O  O   . GLY B 1 201 ? 4.65500   -15.88500 35.84900  1.000 28.78138  ? 201 GLY BA O   1 
ATOM   3691 N  N   . GLU B 1 202 ? 2.68500   -16.95600 35.80700  1.000 15.67968  ? 202 GLU BA N   1 
ATOM   3692 C  CA  . GLU B 1 202 ? 3.17200   -17.95400 34.86300  1.000 14.21545  ? 202 GLU BA CA  1 
ATOM   3693 C  C   . GLU B 1 202 ? 3.32400   -17.34800 33.47100  1.000 23.55823  ? 202 GLU BA C   1 
ATOM   3694 O  O   . GLU B 1 202 ? 2.53700   -16.49100 33.06000  1.000 11.53425  ? 202 GLU BA O   1 
ATOM   3695 C  CB  . GLU B 1 202 ? 2.21900   -19.14800 34.81500  1.000 13.92657  ? 202 GLU BA CB  1 
ATOM   3696 C  CG  . GLU B 1 202 ? 2.59900   -20.28900 35.74700  1.000 39.78446  ? 202 GLU BA CG  1 
ATOM   3697 C  CD  . GLU B 1 202 ? 1.82800   -21.56200 35.45400  1.000 44.08741  ? 202 GLU BA CD  1 
ATOM   3698 O  OE1 . GLU B 1 202 ? 0.64800   -21.46400 35.05400  1.000 44.97731  ? 202 GLU BA OE1 1 
ATOM   3699 O  OE2 . GLU B 1 202 ? 2.39800   -22.66000 35.62600  1.000 45.58541  ? 202 GLU BA OE2 1 
ATOM   3700 N  N   . PHE B 1 203 ? 4.34600   -17.79700 32.74500  1.000 8.08920   ? 203 PHE BA N   1 
ATOM   3701 C  CA  . PHE B 1 203 ? 4.56100   -17.31900 31.38600  1.000 16.50508  ? 203 PHE BA CA  1 
ATOM   3702 C  C   . PHE B 1 203 ? 3.48300   -17.86300 30.45600  1.000 21.86937  ? 203 PHE BA C   1 
ATOM   3703 O  O   . PHE B 1 203 ? 3.11300   -19.03800 30.52600  1.000 14.17079  ? 203 PHE BA O   1 
ATOM   3704 C  CB  . PHE B 1 203 ? 5.94600   -17.73100 30.88600  1.000 13.46263  ? 203 PHE BA CB  1 
ATOM   3705 C  CG  . PHE B 1 203 ? 7.07400   -16.98400 31.54100  1.000 21.69566  ? 203 PHE BA CG  1 
ATOM   3706 C  CD1 . PHE B 1 203 ? 7.06200   -15.60100 31.60300  1.000 15.74493  ? 203 PHE BA CD1 1 
ATOM   3707 C  CD2 . PHE B 1 203 ? 8.14400   -17.66500 32.09600  1.000 17.78114  ? 203 PHE BA CD2 1 
ATOM   3708 C  CE1 . PHE B 1 203 ? 8.09800   -14.91100 32.20500  1.000 24.70809  ? 203 PHE BA CE1 1 
ATOM   3709 C  CE2 . PHE B 1 203 ? 9.18300   -16.98000 32.69900  1.000 18.14883  ? 203 PHE BA CE2 1 
ATOM   3710 C  CZ  . PHE B 1 203 ? 9.15900   -15.60100 32.75300  1.000 14.10555  ? 203 PHE BA CZ  1 
ATOM   3711 N  N   . ALA B 1 204 ? 2.98200   -16.99900 29.57400  1.000 15.00715  ? 204 ALA BA N   1 
ATOM   3712 C  CA  . ALA B 1 204 ? 1.85700   -17.33600 28.71300  1.000 14.03335  ? 204 ALA BA CA  1 
ATOM   3713 C  C   . ALA B 1 204 ? 2.26400   -17.76700 27.30900  1.000 19.17779  ? 204 ALA BA C   1 
ATOM   3714 O  O   . ALA B 1 204 ? 1.40500   -18.25000 26.56300  1.000 24.80092  ? 204 ALA BA O   1 
ATOM   3715 C  CB  . ALA B 1 204 ? 0.89700   -16.14500 28.61200  1.000 15.17489  ? 204 ALA BA CB  1 
ATOM   3716 N  N   . ASP B 1 205 ? 3.53900   -17.61200 26.94000  1.000 10.88700  ? 205 ASP BA N   1 
ATOM   3717 C  CA  . ASP B 1 205 ? 4.01800   -17.85900 25.58100  1.000 11.04001  ? 205 ASP BA CA  1 
ATOM   3718 C  C   . ASP B 1 205 ? 3.32200   -16.92000 24.60300  1.000 11.07593  ? 205 ASP BA C   1 
ATOM   3719 O  O   . ASP B 1 205 ? 2.24100   -17.23300 24.09400  1.000 11.33743  ? 205 ASP BA O   1 
ATOM   3720 C  CB  . ASP B 1 205 ? 3.80700   -19.32300 25.17400  1.000 10.85816  ? 205 ASP BA CB  1 
ATOM   3721 C  CG  . ASP B 1 205 ? 4.69300   -19.74400 24.01500  1.000 10.26283  ? 205 ASP BA CG  1 
ATOM   3722 O  OD1 . ASP B 1 205 ? 4.89100   -18.93700 23.08400  1.000 19.55637  ? 205 ASP BA OD1 1 
ATOM   3723 O  OD2 . ASP B 1 205 ? 5.18600   -20.89100 24.03100  1.000 24.71425  ? 205 ASP BA OD2 1 
ATOM   3724 N  N   . THR B 1 206 ? 3.94700   -15.77100 24.33400  1.000 13.31246  ? 206 THR BA N   1 
ATOM   3725 C  CA  . THR B 1 206 ? 3.30900   -14.73900 23.52100  1.000 12.08602  ? 206 THR BA CA  1 
ATOM   3726 C  C   . THR B 1 206 ? 2.91000   -15.27500 22.15100  1.000 12.72490  ? 206 THR BA C   1 
ATOM   3727 O  O   . THR B 1 206 ? 1.75000   -15.16000 21.74300  1.000 9.58368   ? 206 THR BA O   1 
ATOM   3728 C  CB  . THR B 1 206 ? 4.24100   -13.53400 23.38200  1.000 9.97405   ? 206 THR BA CB  1 
ATOM   3729 O  OG1 . THR B 1 206 ? 4.34100   -12.85700 24.64100  1.000 11.21837  ? 206 THR BA OG1 1 
ATOM   3730 C  CG2 . THR B 1 206 ? 3.71300   -12.56500 22.33200  1.000 6.40464   ? 206 THR BA CG2 1 
ATOM   3731 N  N   . TYR B 1 207 ? 3.85800   -15.88500 21.43500  1.000 9.40481   ? 207 TYR BA N   1 
ATOM   3732 C  CA  . TYR B 1 207 ? 3.58700   -16.34200 20.07300  1.000 16.13569  ? 207 TYR BA CA  1 
ATOM   3733 C  C   . TYR B 1 207 ? 2.46200   -17.37000 20.03900  1.000 10.00358  ? 207 TYR BA C   1 
ATOM   3734 O  O   . TYR B 1 207 ? 1.60900   -17.33600 19.14400  1.000 14.50891  ? 207 TYR BA O   1 
ATOM   3735 C  CB  . TYR B 1 207 ? 4.86300   -16.91700 19.45500  1.000 9.10617   ? 207 TYR BA CB  1 
ATOM   3736 C  CG  . TYR B 1 207 ? 4.69100   -17.48200 18.05900  1.000 13.39760  ? 207 TYR BA CG  1 
ATOM   3737 C  CD1 . TYR B 1 207 ? 3.99200   -16.78300 17.08200  1.000 10.54917  ? 207 TYR BA CD1 1 
ATOM   3738 C  CD2 . TYR B 1 207 ? 5.24000   -18.71100 17.71800  1.000 13.78659  ? 207 TYR BA CD2 1 
ATOM   3739 C  CE1 . TYR B 1 207 ? 3.84000   -17.29800 15.80400  1.000 6.13711   ? 207 TYR BA CE1 1 
ATOM   3740 C  CE2 . TYR B 1 207 ? 5.09400   -19.23200 16.44700  1.000 19.62765  ? 207 TYR BA CE2 1 
ATOM   3741 C  CZ  . TYR B 1 207 ? 4.39600   -18.52200 15.49400  1.000 23.21615  ? 207 TYR BA CZ  1 
ATOM   3742 O  OH  . TYR B 1 207 ? 4.25200   -19.04800 14.23100  1.000 19.12951  ? 207 TYR BA OH  1 
ATOM   3743 N  N   . ALA B 1 208 ? 2.43900   -18.29000 21.00600  1.000 9.99213   ? 208 ALA BA N   1 
ATOM   3744 C  CA  . ALA B 1 208 ? 1.38000   -19.29300 21.04200  1.000 12.49760  ? 208 ALA BA CA  1 
ATOM   3745 C  C   . ALA B 1 208 ? 0.01700   -18.64900 21.26000  1.000 10.38183  ? 208 ALA BA C   1 
ATOM   3746 O  O   . ALA B 1 208 ? -0.99200  -19.11600 20.71800  1.000 13.06187  ? 208 ALA BA O   1 
ATOM   3747 C  CB  . ALA B 1 208 ? 1.66700   -20.32400 22.13300  1.000 15.91018  ? 208 ALA BA CB  1 
ATOM   3748 N  N   . ARG B 1 209 ? -0.03200  -17.56800 22.04300  1.000 14.12001  ? 209 ARG BA N   1 
ATOM   3749 C  CA  . ARG B 1 209 ? -1.30100  -16.89100 22.29300  1.000 9.48500   ? 209 ARG BA CA  1 
ATOM   3750 C  C   . ARG B 1 209 ? -1.77900  -16.12500 21.06300  1.000 17.56067  ? 209 ARG BA C   1 
ATOM   3751 O  O   . ARG B 1 209 ? -2.97800  -16.11600 20.76200  1.000 14.54490  ? 209 ARG BA O   1 
ATOM   3752 C  CB  . ARG B 1 209 ? -1.17200  -15.95400 23.49500  1.000 12.29324  ? 209 ARG BA CB  1 
ATOM   3753 C  CG  . ARG B 1 209 ? -0.95800  -16.66400 24.82800  1.000 18.25962  ? 209 ARG BA CG  1 
ATOM   3754 C  CD  . ARG B 1 209 ? -2.00600  -17.74800 25.06900  1.000 16.89718  ? 209 ARG BA CD  1 
ATOM   3755 N  NE  . ARG B 1 209 ? -3.36600  -17.25400 24.88600  1.000 26.69574  ? 209 ARG BA NE  1 
ATOM   3756 C  CZ  . ARG B 1 209 ? -4.45100  -18.01800 24.88900  1.000 25.42679  ? 209 ARG BA CZ  1 
ATOM   3757 N  NH1 . ARG B 1 209 ? -4.37500  -19.32700 25.07300  1.000 23.64646  ? 209 ARG BA NH1 1 
ATOM   3758 N  NH2 . ARG B 1 209 ? -5.64100  -17.45500 24.70300  1.000 25.12077  ? 209 ARG BA NH2 1 
ATOM   3759 N  N   . MET B 1 210 ? -0.86300  -15.46800 20.34200  1.000 16.42922  ? 210 MET BA N   1 
ATOM   3760 C  CA  . MET B 1 210 ? -1.26500  -14.74900 19.13400  1.000 14.37854  ? 210 MET BA CA  1 
ATOM   3761 C  C   . MET B 1 210 ? -1.77700  -15.70300 18.06400  1.000 10.09681  ? 210 MET BA C   1 
ATOM   3762 O  O   . MET B 1 210 ? -2.69800  -15.36300 17.31100  1.000 15.14555  ? 210 MET BA O   1 
ATOM   3763 C  CB  . MET B 1 210 ? -0.10700  -13.91000 18.58900  1.000 16.31532  ? 210 MET BA CB  1 
ATOM   3764 C  CG  . MET B 1 210 ? 0.76300   -13.25200 19.64200  1.000 18.33335  ? 210 MET BA CG  1 
ATOM   3765 S  SD  . MET B 1 210 ? 1.64400   -11.79700 19.04200  1.000 22.31899  ? 210 MET BA SD  1 
ATOM   3766 C  CE  . MET B 1 210 ? 0.34900   -10.95500 18.13500  1.000 14.62448  ? 210 MET BA CE  1 
ATOM   3767 N  N   . LYS B 1 211 ? -1.19200  -16.90000 17.97700  1.000 7.06054   ? 211 LYS BA N   1 
ATOM   3768 C  CA  . LYS B 1 211 ? -1.68100  -17.88700 17.02200  1.000 13.39524  ? 211 LYS BA CA  1 
ATOM   3769 C  C   . LYS B 1 211 ? -3.11400  -18.29500 17.33000  1.000 12.50929  ? 211 LYS BA C   1 
ATOM   3770 O  O   . LYS B 1 211 ? -3.86700  -18.65800 16.41900  1.000 16.38917  ? 211 LYS BA O   1 
ATOM   3771 C  CB  . LYS B 1 211 ? -0.77100  -19.11700 17.01900  1.000 12.96271  ? 211 LYS BA CB  1 
ATOM   3772 C  CG  . LYS B 1 211 ? 0.47600   -18.96900 16.16300  1.000 24.50072  ? 211 LYS BA CG  1 
ATOM   3773 C  CD  . LYS B 1 211 ? 1.54800   -19.96700 16.57000  1.000 21.98058  ? 211 LYS BA CD  1 
ATOM   3774 C  CE  . LYS B 1 211 ? 1.45300   -21.24900 15.76300  1.000 20.29818  ? 211 LYS BA CE  1 
ATOM   3775 N  NZ  . LYS B 1 211 ? 2.37000   -22.29600 16.29100  1.000 21.39485  ? 211 LYS BA NZ  1 
ATOM   3776 N  N   . LEU B 1 212 ? -3.50900  -18.23600 18.60100  1.000 22.01455  ? 212 LEU BA N   1 
ATOM   3777 C  CA  . LEU B 1 212 ? -4.85700  -18.59000 19.02200  1.000 27.85705  ? 212 LEU BA CA  1 
ATOM   3778 C  C   . LEU B 1 212 ? -5.84200  -17.43500 18.90600  1.000 21.39544  ? 212 LEU BA C   1 
ATOM   3779 O  O   . LEU B 1 212 ? -7.04500  -17.65000 19.08200  1.000 36.54076  ? 212 LEU BA O   1 
ATOM   3780 C  CB  . LEU B 1 212 ? -4.83700  -19.10300 20.46600  1.000 21.66281  ? 212 LEU BA CB  1 
ATOM   3781 C  CG  . LEU B 1 212 ? -4.32100  -20.53000 20.66100  1.000 24.13886  ? 212 LEU BA CG  1 
ATOM   3782 C  CD1 . LEU B 1 212 ? -4.30400  -20.89800 22.13500  1.000 36.69636  ? 212 LEU BA CD1 1 
ATOM   3783 C  CD2 . LEU B 1 212 ? -5.16500  -21.51600 19.87100  1.000 33.57608  ? 212 LEU BA CD2 1 
ATOM   3784 N  N   . GLY B 1 213 ? -5.36900  -16.22500 18.62000  1.000 19.88465  ? 213 GLY BA N   1 
ATOM   3785 C  CA  . GLY B 1 213 ? -6.24400  -15.08000 18.43100  1.000 15.31090  ? 213 GLY BA CA  1 
ATOM   3786 C  C   . GLY B 1 213 ? -6.08500  -13.96300 19.44400  1.000 27.71774  ? 213 GLY BA C   1 
ATOM   3787 O  O   . GLY B 1 213 ? -6.78600  -12.94800 19.32500  1.000 19.04172  ? 213 GLY BA O   1 
ATOM   3788 N  N   . ASP B 1 214 ? -5.20700  -14.08800 20.43800  1.000 18.28996  ? 214 ASP BA N   1 
ATOM   3789 C  CA  . ASP B 1 214 ? -5.00800  -13.01000 21.40000  1.000 24.49728  ? 214 ASP BA CA  1 
ATOM   3790 C  C   . ASP B 1 214 ? -4.46500  -11.77000 20.69800  1.000 35.82685  ? 214 ASP BA C   1 
ATOM   3791 O  O   . ASP B 1 214 ? -3.51400  -11.85000 19.91500  1.000 23.51310  ? 214 ASP BA O   1 
ATOM   3792 C  CB  . ASP B 1 214 ? -4.05200  -13.45800 22.50500  1.000 21.15133  ? 214 ASP BA CB  1 
ATOM   3793 C  CG  . ASP B 1 214 ? -4.74600  -14.26400 23.58900  1.000 23.97369  ? 214 ASP BA CG  1 
ATOM   3794 O  OD1 . ASP B 1 214 ? -5.84900  -14.79100 23.33200  1.000 25.62970  ? 214 ASP BA OD1 1 
ATOM   3795 O  OD2 . ASP B 1 214 ? -4.18700  -14.37400 24.69900  1.000 28.08897  ? 214 ASP BA OD2 1 
ATOM   3796 N  N   . LYS B 1 215 ? -5.07400  -10.62300 20.97900  1.000 22.71516  ? 215 LYS BA N   1 
ATOM   3797 C  CA  . LYS B 1 215 ? -4.75600  -9.38200  20.28900  1.000 45.15571  ? 215 LYS BA CA  1 
ATOM   3798 C  C   . LYS B 1 215 ? -3.76200  -8.54900  21.09000  1.000 40.32500  ? 215 LYS BA C   1 
ATOM   3799 O  O   . LYS B 1 215 ? -3.68500  -8.64400  22.31800  1.000 38.30168  ? 215 LYS BA O   1 
ATOM   3800 C  CB  . LYS B 1 215 ? -6.02500  -8.56800  20.02700  1.000 45.05600  ? 215 LYS BA CB  1 
ATOM   3801 C  CG  . LYS B 1 215 ? -6.79000  -8.99900  18.78300  1.000 44.06619  ? 215 LYS BA CG  1 
ATOM   3802 C  CD  . LYS B 1 215 ? -5.89900  -8.97500  17.54900  1.000 53.67489  ? 215 LYS BA CD  1 
ATOM   3803 C  CE  . LYS B 1 215 ? -6.48100  -9.82400  16.42800  1.000 49.32462  ? 215 LYS BA CE  1 
ATOM   3804 N  NZ  . LYS B 1 215 ? -5.42300  -10.50600 15.63000  1.000 42.22055  ? 215 LYS BA NZ  1 
ATOM   3805 N  N   . ASN B 1 216 ? -3.00200  -7.72400  20.37300  1.000 38.62690  ? 216 ASN BA N   1 
ATOM   3806 C  CA  . ASN B 1 216 ? -1.99900  -6.86800  20.99700  1.000 30.80862  ? 216 ASN BA CA  1 
ATOM   3807 C  C   . ASN B 1 216 ? -2.67800  -5.77100  21.80700  1.000 26.56232  ? 216 ASN BA C   1 
ATOM   3808 O  O   . ASN B 1 216 ? -3.46200  -4.98400  21.26600  1.000 28.47721  ? 216 ASN BA O   1 
ATOM   3809 C  CB  . ASN B 1 216 ? -1.09000  -6.26300  19.92900  1.000 29.24710  ? 216 ASN BA CB  1 
ATOM   3810 C  CG  . ASN B 1 216 ? 0.14300   -5.59900  20.51500  1.000 28.74444  ? 216 ASN BA CG  1 
ATOM   3811 O  OD1 . ASN B 1 216 ? 0.24900   -5.41300  21.72700  1.000 32.72665  ? 216 ASN BA OD1 1 
ATOM   3812 N  ND2 . ASN B 1 216 ? 1.08500   -5.23800  19.65200  1.000 23.81248  ? 216 ASN BA ND2 1 
ATOM   3813 N  N   A GLN B 1 217 ? -2.37600  -5.71600  23.10500  0.472 24.01607  ? 217 GLN BA N   1 
ATOM   3814 N  N   B GLN B 1 217 ? -2.37300  -5.71700  23.10400  0.528 23.98688  ? 217 GLN BA N   1 
ATOM   3815 C  CA  A GLN B 1 217 ? -2.93100  -4.70800  23.99900  0.472 28.03480  ? 217 GLN BA CA  1 
ATOM   3816 C  CA  B GLN B 1 217 ? -2.92700  -4.71400  24.00300  0.528 28.02241  ? 217 GLN BA CA  1 
ATOM   3817 C  C   A GLN B 1 217 ? -1.86900  -3.73700  24.50600  0.472 36.91224  ? 217 GLN BA C   1 
ATOM   3818 C  C   B GLN B 1 217 ? -1.86400  -3.74500  24.51200  0.528 36.95246  ? 217 GLN BA C   1 
ATOM   3819 O  O   A GLN B 1 217 ? -2.03800  -3.14000  25.57500  0.472 33.33454  ? 217 GLN BA O   1 
ATOM   3820 O  O   B GLN B 1 217 ? -2.02800  -3.15700  25.58600  0.528 33.34883  ? 217 GLN BA O   1 
ATOM   3821 C  CB  A GLN B 1 217 ? -3.64300  -5.37400  25.17700  0.472 28.46546  ? 217 GLN BA CB  1 
ATOM   3822 C  CB  B GLN B 1 217 ? -3.63800  -5.39200  25.17500  0.528 28.45152  ? 217 GLN BA CB  1 
ATOM   3823 C  CG  A GLN B 1 217 ? -4.35800  -6.66900  24.82500  0.472 37.05424  ? 217 GLN BA CG  1 
ATOM   3824 C  CG  B GLN B 1 217 ? -4.76300  -6.32400  24.75100  0.528 37.91415  ? 217 GLN BA CG  1 
ATOM   3825 C  CD  A GLN B 1 217 ? -5.60400  -6.44500  23.99000  0.472 34.78422  ? 217 GLN BA CD  1 
ATOM   3826 C  CD  B GLN B 1 217 ? -5.41700  -7.02800  25.92300  0.528 32.51299  ? 217 GLN BA CD  1 
ATOM   3827 O  OE1 A GLN B 1 217 ? -6.15500  -5.34400  23.95700  0.472 43.30216  ? 217 GLN BA OE1 1 
ATOM   3828 O  OE1 B GLN B 1 217 ? -4.89800  -7.01700  27.03900  0.528 31.64996  ? 217 GLN BA OE1 1 
ATOM   3829 N  NE2 A GLN B 1 217 ? -6.05400  -7.49100  23.30900  0.472 36.32422  ? 217 GLN BA NE2 1 
ATOM   3830 N  NE2 B GLN B 1 217 ? -6.56300  -7.65000  25.67300  0.528 50.65151  ? 217 GLN BA NE2 1 
ATOM   3831 N  N   . SER B 1 218 ? -0.78000  -3.56700  23.76200  1.000 33.51480  ? 218 SER BA N   1 
ATOM   3832 C  CA  . SER B 1 218 ? 0.27800   -2.65400  24.16200  1.000 42.82436  ? 218 SER BA CA  1 
ATOM   3833 C  C   . SER B 1 218 ? -0.10400  -1.21300  23.82000  1.000 44.43832  ? 218 SER BA C   1 
ATOM   3834 O  O   . SER B 1 218 ? -1.07200  -0.94800  23.10100  1.000 31.63167  ? 218 SER BA O   1 
ATOM   3835 C  CB  . SER B 1 218 ? 1.59800   -3.04100  23.49400  1.000 28.02305  ? 218 SER BA CB  1 
ATOM   3836 O  OG  . SER B 1 218 ? 1.60800   -2.68100  22.12400  1.000 45.80773  ? 218 SER BA OG  1 
ATOM   3837 N  N   . ALA B 1 219 ? 0.68600   -0.27100  24.34400  1.000 40.90770  ? 219 ALA BA N   1 
ATOM   3838 C  CA  . ALA B 1 219 ? 0.34800   1.14400   24.21400  1.000 41.42160  ? 219 ALA BA CA  1 
ATOM   3839 C  C   . ALA B 1 219 ? 0.38900   1.61900   22.76700  1.000 32.92411  ? 219 ALA BA C   1 
ATOM   3840 O  O   . ALA B 1 219 ? -0.37300  2.51800   22.39300  1.000 38.80409  ? 219 ALA BA O   1 
ATOM   3841 C  CB  . ALA B 1 219 ? 1.29000   1.99100   25.07100  1.000 30.63402  ? 219 ALA BA CB  1 
ATOM   3842 N  N   . LEU B 1 220 ? 1.25800   1.03800   21.94200  1.000 39.30813  ? 220 LEU BA N   1 
ATOM   3843 C  CA  . LEU B 1 220 ? 1.42800   1.47000   20.56100  1.000 37.83338  ? 220 LEU BA CA  1 
ATOM   3844 C  C   . LEU B 1 220 ? 0.76100   0.53600   19.55800  1.000 32.89678  ? 220 LEU BA C   1 
ATOM   3845 O  O   . LEU B 1 220 ? 1.03500   0.63500   18.35700  1.000 34.66422  ? 220 LEU BA O   1 
ATOM   3846 C  CB  . LEU B 1 220 ? 2.91600   1.60700   20.23300  1.000 34.32680  ? 220 LEU BA CB  1 
ATOM   3847 C  CG  . LEU B 1 220 ? 3.74000   2.47100   21.18900  1.000 45.83010  ? 220 LEU BA CG  1 
ATOM   3848 C  CD1 . LEU B 1 220 ? 4.77600   1.62500   21.90600  1.000 37.02224  ? 220 LEU BA CD1 1 
ATOM   3849 C  CD2 . LEU B 1 220 ? 4.39900   3.62000   20.44400  1.000 47.76809  ? 220 LEU BA CD2 1 
ATOM   3850 N  N   . ALA B 1 221 ? -0.11600  -0.35900  20.01600  1.000 36.99765  ? 221 ALA BA N   1 
ATOM   3851 C  CA  . ALA B 1 221 ? -0.74000  -1.32700  19.12200  1.000 39.63102  ? 221 ALA BA CA  1 
ATOM   3852 C  C   . ALA B 1 221 ? -1.73400  -0.69800  18.15400  1.000 45.98257  ? 221 ALA BA C   1 
ATOM   3853 O  O   . ALA B 1 221 ? -2.13300  -1.36200  17.19100  1.000 35.55821  ? 221 ALA BA O   1 
ATOM   3854 C  CB  . ALA B 1 221 ? -1.44000  -2.41700  19.93700  1.000 28.03665  ? 221 ALA BA CB  1 
ATOM   3855 N  N   . ARG B 1 222 ? -2.13800  0.55500   18.37600  1.000 35.70688  ? 222 ARG BA N   1 
ATOM   3856 C  CA  . ARG B 1 222 ? -3.16100  1.15800   17.52700  1.000 51.20552  ? 222 ARG BA CA  1 
ATOM   3857 C  C   . ARG B 1 222 ? -2.61700  1.48900   16.14300  1.000 56.86752  ? 222 ARG BA C   1 
ATOM   3858 O  O   . ARG B 1 222 ? -3.28400  1.23700   15.13300  1.000 68.47798  ? 222 ARG BA O   1 
ATOM   3859 C  CB  . ARG B 1 222 ? -3.72800  2.41000   18.19400  1.000 61.20861  ? 222 ARG BA CB  1 
ATOM   3860 C  CG  . ARG B 1 222 ? -5.04500  2.18900   18.92000  1.000 54.16578  ? 222 ARG BA CG  1 
ATOM   3861 C  CD  . ARG B 1 222 ? -5.58600  3.49300   19.48700  1.000 82.66564  ? 222 ARG BA CD  1 
ATOM   3862 N  NE  . ARG B 1 222 ? -4.81200  3.96000   20.63100  1.000 81.68579  ? 222 ARG BA NE  1 
ATOM   3863 C  CZ  . ARG B 1 222 ? -5.20600  4.91300   21.46500  1.000 86.48048  ? 222 ARG BA CZ  1 
ATOM   3864 N  NH1 . ARG B 1 222 ? -6.36900  5.52600   21.31300  1.000 82.14345  ? 222 ARG BA NH1 1 
ATOM   3865 N  NH2 . ARG B 1 222 ? -4.41500  5.26000   22.47500  1.000 69.52620  ? 222 ARG BA NH2 1 
ATOM   3866 N  N   . MET B 1 223 ? -1.41400  2.05300   16.07100  1.000 58.86419  ? 223 MET BA N   1 
ATOM   3867 C  CA  . MET B 1 223 ? -0.83300  2.42400   14.78900  1.000 60.61418  ? 223 MET BA CA  1 
ATOM   3868 C  C   . MET B 1 223 ? -0.28500  1.19600   14.07300  1.000 63.46680  ? 223 MET BA C   1 
ATOM   3869 O  O   . MET B 1 223 ? 0.27200   0.28800   14.69900  1.000 63.78902  ? 223 MET BA O   1 
ATOM   3870 C  CB  . MET B 1 223 ? 0.27000   3.46700   14.97800  1.000 44.15349  ? 223 MET BA CB  1 
ATOM   3871 C  CG  . MET B 1 223 ? 1.44300   3.00700   15.82900  1.000 50.15146  ? 223 MET BA CG  1 
ATOM   3872 S  SD  . MET B 1 223 ? 2.18400   4.35200   16.77700  1.000 58.55652  ? 223 MET BA SD  1 
ATOM   3873 C  CE  . MET B 1 223 ? 3.28300   5.06500   15.55500  1.000 35.01665  ? 223 MET BA CE  1 
ATOM   3874 N  N   . GLY B 1 224 ? -0.45500  1.16900   12.75500  1.000 59.43486  ? 224 GLY BA N   1 
ATOM   3875 C  CA  . GLY B 1 224 ? 0.00500   0.05400   11.94900  1.000 56.05453  ? 224 GLY BA CA  1 
ATOM   3876 C  C   . GLY B 1 224 ? 0.27000   0.42900   10.50400  1.000 55.24681  ? 224 GLY BA C   1 
ATOM   3877 O  O   . GLY B 1 224 ? 0.21200   1.60300   10.13800  1.000 37.97837  ? 224 GLY BA O   1 
ATOM   3878 N  N   . THR B 1 227 ? 10.72600  -3.08300  21.38600  1.000 13.38331  ? 227 THR BA N   1 
ATOM   3879 C  CA  . THR B 1 227 ? 11.91200  -2.51900  20.75200  1.000 10.65714  ? 227 THR BA CA  1 
ATOM   3880 C  C   . THR B 1 227 ? 13.18600  -3.05900  21.39200  1.000 14.72850  ? 227 THR BA C   1 
ATOM   3881 O  O   . THR B 1 227 ? 13.29000  -3.13500  22.61300  1.000 13.24087  ? 227 THR BA O   1 
ATOM   3882 C  CB  . THR B 1 227 ? 11.91800  -0.98000  20.83800  1.000 6.98799   ? 227 THR BA CB  1 
ATOM   3883 O  OG1 . THR B 1 227 ? 10.80900  -0.45500  20.10000  1.000 7.14913   ? 227 THR BA OG1 1 
ATOM   3884 C  CG2 . THR B 1 227 ? 13.21200  -0.40900  20.27200  1.000 5.06591   ? 227 THR BA CG2 1 
ATOM   3885 N  N   . THR B 1 228 ? 14.15300  -3.44200  20.56200  1.000 9.28694   ? 228 THR BA N   1 
ATOM   3886 C  CA  . THR B 1 228 ? 15.46600  -3.87000  21.02800  1.000 4.33406   ? 228 THR BA CA  1 
ATOM   3887 C  C   . THR B 1 228 ? 16.52000  -3.13700  20.21400  1.000 12.08069  ? 228 THR BA C   1 
ATOM   3888 O  O   . THR B 1 228 ? 16.61900  -3.34000  19.00000  1.000 12.40164  ? 228 THR BA O   1 
ATOM   3889 C  CB  . THR B 1 228 ? 15.63700  -5.38600  20.89600  1.000 8.11051   ? 228 THR BA CB  1 
ATOM   3890 O  OG1 . THR B 1 228 ? 14.71500  -6.04900  21.77000  1.000 8.00260   ? 228 THR BA OG1 1 
ATOM   3891 C  CG2 . THR B 1 228 ? 17.05300  -5.79400  21.26100  1.000 3.50005   ? 228 THR BA CG2 1 
ATOM   3892 N  N   . ILE B 1 229 ? 17.29400  -2.27900  20.87600  1.000 8.43986   ? 229 ILE BA N   1 
ATOM   3893 C  CA  . ILE B 1 229 ? 18.32900  -1.48800  20.22200  1.000 15.98554  ? 229 ILE BA CA  1 
ATOM   3894 C  C   . ILE B 1 229 ? 19.66700  -1.81400  20.86600  1.000 11.10304  ? 229 ILE BA C   1 
ATOM   3895 O  O   . ILE B 1 229 ? 19.73200  -2.21200  22.03400  1.000 11.44698  ? 229 ILE BA O   1 
ATOM   3896 C  CB  . ILE B 1 229 ? 18.03500  0.02600   20.30200  1.000 7.46348   ? 229 ILE BA CB  1 
ATOM   3897 C  CG1 . ILE B 1 229 ? 17.99000  0.49100   21.75800  1.000 9.98709   ? 229 ILE BA CG1 1 
ATOM   3898 C  CG2 . ILE B 1 229 ? 16.72900  0.35400   19.59700  1.000 5.68478   ? 229 ILE BA CG2 1 
ATOM   3899 C  CD1 . ILE B 1 229 ? 17.61400  1.95400   21.92400  1.000 8.90868   ? 229 ILE BA CD1 1 
ATOM   3900 N  N   . GLY B 1 230 ? 20.74000  -1.64800  20.10300  1.000 4.92446   ? 230 GLY BA N   1 
ATOM   3901 C  CA  . GLY B 1 230 ? 22.04900  -2.00000  20.62400  1.000 8.30809   ? 230 GLY BA CA  1 
ATOM   3902 C  C   . GLY B 1 230 ? 23.16300  -1.62700  19.67200  1.000 7.38878   ? 230 GLY BA C   1 
ATOM   3903 O  O   . GLY B 1 230 ? 22.93300  -1.17800  18.54300  1.000 11.99914  ? 230 GLY BA O   1 
ATOM   3904 N  N   B ILE B 1 231 ? 24.38500  -1.82300  20.16000  1.000 6.51060   ? 231 ILE BA N   1 
ATOM   3905 C  CA  B ILE B 1 231 ? 25.61300  -1.53700  19.43300  1.000 4.98764   ? 231 ILE BA CA  1 
ATOM   3906 C  C   B ILE B 1 231 ? 26.45100  -2.80500  19.40100  1.000 11.43701  ? 231 ILE BA C   1 
ATOM   3907 O  O   B ILE B 1 231 ? 26.57200  -3.49900  20.41600  1.000 12.24380  ? 231 ILE BA O   1 
ATOM   3908 C  CB  B ILE B 1 231 ? 26.40500  -0.38700  20.09200  1.000 14.18742  ? 231 ILE BA CB  1 
ATOM   3909 C  CG1 B ILE B 1 231 ? 25.53300  0.86200   20.23000  1.000 12.39614  ? 231 ILE BA CG1 1 
ATOM   3910 C  CG2 B ILE B 1 231 ? 27.68200  -0.08700  19.31100  1.000 10.23333  ? 231 ILE BA CG2 1 
ATOM   3911 C  CD1 B ILE B 1 231 ? 26.02200  1.82800   21.29000  1.000 13.83460  ? 231 ILE BA CD1 1 
ATOM   3912 N  N   . VAL B 1 232 ? 27.02100  -3.11300  18.23900  1.000 7.40482   ? 232 VAL BA N   1 
ATOM   3913 C  CA  . VAL B 1 232 ? 27.98300  -4.20100  18.09800  1.000 14.60393  ? 232 VAL BA CA  1 
ATOM   3914 C  C   . VAL B 1 232 ? 29.29400  -3.60100  17.60800  1.000 10.48180  ? 232 VAL BA C   1 
ATOM   3915 O  O   . VAL B 1 232 ? 29.30900  -2.83600  16.63600  1.000 12.17297  ? 232 VAL BA O   1 
ATOM   3916 C  CB  . VAL B 1 232 ? 27.48600  -5.30400  17.14400  1.000 15.78508  ? 232 VAL BA CB  1 
ATOM   3917 C  CG1 . VAL B 1 232 ? 26.44100  -6.17300  17.83200  1.000 5.72693   ? 232 VAL BA CG1 1 
ATOM   3918 C  CG2 . VAL B 1 232 ? 26.93300  -4.70900  15.85900  1.000 14.75786  ? 232 VAL BA CG2 1 
ATOM   3919 N  N   . SER B 1 233 ? 30.39000  -3.93700  18.28500  1.000 12.66509  ? 233 SER BA N   1 
ATOM   3920 C  CA  . SER B 1 233 ? 31.68900  -3.34500  18.00100  1.000 7.12655   ? 233 SER BA CA  1 
ATOM   3921 C  C   . SER B 1 233 ? 32.74900  -4.42900  17.89200  1.000 13.38158  ? 233 SER BA C   1 
ATOM   3922 O  O   . SER B 1 233 ? 32.70800  -5.42700  18.61900  1.000 13.86417  ? 233 SER BA O   1 
ATOM   3923 C  CB  . SER B 1 233 ? 32.08900  -2.33700  19.08800  1.000 7.28460   ? 233 SER BA CB  1 
ATOM   3924 O  OG  . SER B 1 233 ? 31.12900  -1.30000  19.20200  1.000 7.48402   ? 233 SER BA OG  1 
ATOM   3925 N  N   . THR B 1 234 ? 33.69800  -4.22500  16.98000  1.000 8.38989   ? 234 THR BA N   1 
ATOM   3926 C  CA  . THR B 1 234 ? 34.84300  -5.10800  16.81900  1.000 10.31664  ? 234 THR BA CA  1 
ATOM   3927 C  C   . THR B 1 234 ? 36.11400  -4.27300  16.75300  1.000 9.23920   ? 234 THR BA C   1 
ATOM   3928 O  O   . THR B 1 234 ? 36.08600  -3.08600  16.41900  1.000 10.49893  ? 234 THR BA O   1 
ATOM   3929 C  CB  . THR B 1 234 ? 34.72500  -5.97500  15.55700  1.000 9.30790   ? 234 THR BA CB  1 
ATOM   3930 O  OG1 . THR B 1 234 ? 35.85900  -6.84500  15.46700  1.000 10.95062  ? 234 THR BA OG1 1 
ATOM   3931 C  CG2 . THR B 1 234 ? 34.66800  -5.10100  14.31200  1.000 8.88511   ? 234 THR BA CG2 1 
ATOM   3932 N  N   . ASN B 1 235 ? 37.23900  -4.90500  17.08400  1.000 13.63524  ? 235 ASN BA N   1 
ATOM   3933 C  CA  . ASN B 1 235 ? 38.53700  -4.25300  16.98500  1.000 7.63715   ? 235 ASN BA CA  1 
ATOM   3934 C  C   . ASN B 1 235 ? 39.18600  -4.45000  15.62100  1.000 14.45696  ? 235 ASN BA C   1 
ATOM   3935 O  O   . ASN B 1 235 ? 40.34200  -4.05700  15.43200  1.000 17.45604  ? 235 ASN BA O   1 
ATOM   3936 C  CB  . ASN B 1 235 ? 39.47300  -4.75200  18.09200  1.000 12.86364  ? 235 ASN BA CB  1 
ATOM   3937 C  CG  . ASN B 1 235 ? 39.59200  -6.26500  18.12500  1.000 15.93430  ? 235 ASN BA CG  1 
ATOM   3938 O  OD1 . ASN B 1 235 ? 38.86400  -6.97500  17.43400  1.000 12.63064  ? 235 ASN BA OD1 1 
ATOM   3939 N  ND2 . ASN B 1 235 ? 40.52000  -6.76400  18.93500  1.000 13.76660  ? 235 ASN BA ND2 1 
ATOM   3940 N  N   . CYS B 1 236 ? 38.47100  -5.04400  14.67000  1.000 9.31784   ? 236 CYS BA N   1 
ATOM   3941 C  CA  . CYS B 1 236 ? 38.97700  -5.19500  13.31800  1.000 8.76548   ? 236 CYS BA CA  1 
ATOM   3942 C  C   . CYS B 1 236 ? 38.76900  -3.91200  12.52000  1.000 17.27622  ? 236 CYS BA C   1 
ATOM   3943 O  O   . CYS B 1 236 ? 37.91400  -3.08000  12.83600  1.000 12.19332  ? 236 CYS BA O   1 
ATOM   3944 C  CB  . CYS B 1 236 ? 38.28400  -6.35700  12.60500  1.000 13.45713  ? 236 CYS BA CB  1 
ATOM   3945 S  SG  . CYS B 1 236 ? 38.78900  -7.99400  13.15800  1.000 18.26895  ? 236 CYS BA SG  1 
ATOM   3946 N  N   . ARG B 1 237 ? 39.57200  -3.76000  11.47000  1.000 11.37893  ? 237 ARG BA N   1 
ATOM   3947 C  CA  . ARG B 1 237 ? 39.36900  -2.68700  10.50900  1.000 12.39653  ? 237 ARG BA CA  1 
ATOM   3948 C  C   . ARG B 1 237 ? 38.25800  -3.07900  9.54300   1.000 11.98655  ? 237 ARG BA C   1 
ATOM   3949 O  O   . ARG B 1 237 ? 38.22600  -4.21000  9.05000   1.000 15.14833  ? 237 ARG BA O   1 
ATOM   3950 C  CB  . ARG B 1 237 ? 40.66100  -2.39700  9.74600   1.000 16.28432  ? 237 ARG BA CB  1 
ATOM   3951 C  CG  . ARG B 1 237 ? 40.70800  -1.02800  9.08900   1.000 21.93666  ? 237 ARG BA CG  1 
ATOM   3952 C  CD  . ARG B 1 237 ? 42.01800  -0.82500  8.34400   1.000 28.46029  ? 237 ARG BA CD  1 
ATOM   3953 N  NE  . ARG B 1 237 ? 42.11600  -1.68600  7.17100   1.000 42.78918  ? 237 ARG BA NE  1 
ATOM   3954 C  CZ  . ARG B 1 237 ? 43.01900  -2.64500  7.01900   1.000 44.59421  ? 237 ARG BA CZ  1 
ATOM   3955 N  NH1 . ARG B 1 237 ? 43.92100  -2.90000  7.95200   1.000 36.58392  ? 237 ARG BA NH1 1 
ATOM   3956 N  NH2 . ARG B 1 237 ? 43.01600  -3.36800  5.90200   1.000 45.76305  ? 237 ARG BA NH2 1 
ATOM   3957 N  N   . LEU B 1 238 ? 37.34500  -2.14700  9.27900   1.000 13.01505  ? 238 LEU BA N   1 
ATOM   3958 C  CA  . LEU B 1 238 ? 36.20200  -2.40200  8.41600   1.000 16.37219  ? 238 LEU BA CA  1 
ATOM   3959 C  C   . LEU B 1 238 ? 36.01900  -1.25400  7.43400   1.000 15.48730  ? 238 LEU BA C   1 
ATOM   3960 O  O   . LEU B 1 238 ? 36.36900  -0.10700  7.72200   1.000 13.26207  ? 238 LEU BA O   1 
ATOM   3961 C  CB  . LEU B 1 238 ? 34.90400  -2.57500  9.22500   1.000 9.08327   ? 238 LEU BA CB  1 
ATOM   3962 C  CG  . LEU B 1 238 ? 34.81200  -3.68200  10.27500  1.000 14.32325  ? 238 LEU BA CG  1 
ATOM   3963 C  CD1 . LEU B 1 238 ? 33.49100  -3.57900  11.02100  1.000 12.56676  ? 238 LEU BA CD1 1 
ATOM   3964 C  CD2 . LEU B 1 238 ? 34.95800  -5.04900  9.63400   1.000 9.09653   ? 238 LEU BA CD2 1 
ATOM   3965 N  N   . THR B 1 239 ? 35.46900  -1.57500  6.26700   1.000 7.70609   ? 239 THR BA N   1 
ATOM   3966 C  CA  . THR B 1 239 ? 34.94400  -0.55200  5.38000   1.000 12.90923  ? 239 THR BA CA  1 
ATOM   3967 C  C   . THR B 1 239 ? 33.50400  -0.23300  5.77300   1.000 17.01092  ? 239 THR BA C   1 
ATOM   3968 O  O   . THR B 1 239 ? 32.89800  -0.90800  6.60900   1.000 10.74925  ? 239 THR BA O   1 
ATOM   3969 C  CB  . THR B 1 239 ? 35.01500  -0.99800  3.91800   1.000 15.74407  ? 239 THR BA CB  1 
ATOM   3970 O  OG1 . THR B 1 239 ? 34.11600  -2.09300  3.70300   1.000 16.32124  ? 239 THR BA OG1 1 
ATOM   3971 C  CG2 . THR B 1 239 ? 36.43100  -1.42700  3.55500   1.000 13.35342  ? 239 THR BA CG2 1 
ATOM   3972 N  N   . LYS B 1 240 ? 32.95300  0.81700   5.16100   1.000 13.81583  ? 240 LYS BA N   1 
ATOM   3973 C  CA  . LYS B 1 240 ? 31.58300  1.20800   5.47700   1.000 9.26584   ? 240 LYS BA CA  1 
ATOM   3974 C  C   . LYS B 1 240 ? 30.59600  0.10000   5.12400   1.000 15.62075  ? 240 LYS BA C   1 
ATOM   3975 O  O   . LYS B 1 240 ? 29.66100  -0.17100  5.88700   1.000 13.70126  ? 240 LYS BA O   1 
ATOM   3976 C  CB  . LYS B 1 240 ? 31.22700  2.50300   4.75000   1.000 20.77017  ? 240 LYS BA CB  1 
ATOM   3977 C  CG  . LYS B 1 240 ? 31.44100  3.75500   5.58400   1.000 26.09037  ? 240 LYS BA CG  1 
ATOM   3978 C  CD  . LYS B 1 240 ? 30.51800  4.87700   5.14400   1.000 24.14199  ? 240 LYS BA CD  1 
ATOM   3979 C  CE  . LYS B 1 240 ? 29.55700  5.27000   6.25400   1.000 11.61747  ? 240 LYS BA CE  1 
ATOM   3980 N  NZ  . LYS B 1 240 ? 28.77000  6.48300   5.89400   1.000 16.06750  ? 240 LYS BA NZ  1 
ATOM   3981 N  N   . VAL B 1 241 ? 30.79800  -0.55800  3.97900   1.000 10.56949  ? 241 VAL BA N   1 
ATOM   3982 C  CA  . VAL B 1 241 ? 29.93300  -1.67000  3.58200   1.000 15.86946  ? 241 VAL BA CA  1 
ATOM   3983 C  C   . VAL B 1 241 ? 29.98100  -2.78300  4.61500   1.000 7.49542   ? 241 VAL BA C   1 
ATOM   3984 O  O   . VAL B 1 241 ? 28.94700  -3.33700  5.00500   1.000 8.60205   ? 241 VAL BA O   1 
ATOM   3985 C  CB  . VAL B 1 241 ? 30.33400  -2.19800  2.19600   1.000 24.25562  ? 241 VAL BA CB  1 
ATOM   3986 C  CG1 . VAL B 1 241 ? 29.42300  -3.34200  1.78000   1.000 30.57310  ? 241 VAL BA CG1 1 
ATOM   3987 C  CG2 . VAL B 1 241 ? 30.26100  -1.10500  1.21100   1.000 17.82542  ? 241 VAL BA CG2 1 
ATOM   3988 N  N   . GLU B 1 242 ? 31.18800  -3.14700  5.05200   1.000 5.53163   ? 242 GLU BA N   1 
ATOM   3989 C  CA  . GLU B 1 242 ? 31.32300  -4.24900  5.99700   1.000 8.78075   ? 242 GLU BA CA  1 
ATOM   3990 C  C   . GLU B 1 242 ? 30.66300  -3.91700  7.32800   1.000 10.66407  ? 242 GLU BA C   1 
ATOM   3991 O  O   . GLU B 1 242 ? 30.06800  -4.79200  7.96900   1.000 6.77561   ? 242 GLU BA O   1 
ATOM   3992 C  CB  . GLU B 1 242 ? 32.80000  -4.59800  6.18700   1.000 11.52791  ? 242 GLU BA CB  1 
ATOM   3993 C  CG  . GLU B 1 242 ? 33.48300  -5.08100  4.91300   1.000 13.64765  ? 242 GLU BA CG  1 
ATOM   3994 C  CD  . GLU B 1 242 ? 34.97000  -5.31900  5.09500   1.000 14.10853  ? 242 GLU BA CD  1 
ATOM   3995 O  OE1 . GLU B 1 242 ? 35.63100  -4.49500  5.76200   1.000 13.84587  ? 242 GLU BA OE1 1 
ATOM   3996 O  OE2 . GLU B 1 242 ? 35.47900  -6.33400  4.57600   1.000 22.79739  ? 242 GLU BA OE2 1 
ATOM   3997 N  N   . ALA B 1 243 ? 30.74500  -2.65400  7.75500   1.000 8.70231   ? 243 ALA BA N   1 
ATOM   3998 C  CA  . ALA B 1 243 ? 30.09600  -2.25000  8.99800   1.000 7.36063   ? 243 ALA BA CA  1 
ATOM   3999 C  C   . ALA B 1 243 ? 28.58500  -2.42200  8.90500   1.000 6.89619   ? 243 ALA BA C   1 
ATOM   4000 O  O   . ALA B 1 243 ? 27.95400  -2.97000  9.81600   1.000 10.76945  ? 243 ALA BA O   1 
ATOM   4001 C  CB  . ALA B 1 243 ? 30.45900  -0.80400  9.33500   1.000 8.63697   ? 243 ALA BA CB  1 
ATOM   4002 N  N   . SER B 1 244 ? 27.98700  -1.96800  7.80000   1.000 4.56773   ? 244 SER BA N   1 
ATOM   4003 C  CA  . SER B 1 244 ? 26.54500  -2.12000  7.62600   1.000 6.94966   ? 244 SER BA CA  1 
ATOM   4004 C  C   . SER B 1 244 ? 26.15700  -3.58600  7.47500   1.000 8.83225   ? 244 SER BA C   1 
ATOM   4005 O  O   . SER B 1 244 ? 25.12300  -4.01600  7.99900   1.000 6.01626   ? 244 SER BA O   1 
ATOM   4006 C  CB  . SER B 1 244 ? 26.07100  -1.31000  6.41900   1.000 14.48993  ? 244 SER BA CB  1 
ATOM   4007 O  OG  . SER B 1 244 ? 25.59800  -0.03400  6.82100   1.000 24.21119  ? 244 SER BA OG  1 
ATOM   4008 N  N   . ARG B 1 245 ? 26.97200  -4.36900  6.76400   1.000 4.01574   ? 245 ARG BA N   1 
ATOM   4009 C  CA  . ARG B 1 245 ? 26.71500  -5.80200  6.66900   1.000 7.50258   ? 245 ARG BA CA  1 
ATOM   4010 C  C   . ARG B 1 245 ? 26.79700  -6.46200  8.03900   1.000 14.50422  ? 245 ARG BA C   1 
ATOM   4011 O  O   . ARG B 1 245 ? 25.99600  -7.34800  8.36200   1.000 11.62004  ? 245 ARG BA O   1 
ATOM   4012 C  CB  . ARG B 1 245 ? 27.70400  -6.45100  5.70000   1.000 12.36035  ? 245 ARG BA CB  1 
ATOM   4013 C  CG  . ARG B 1 245 ? 27.40800  -7.91100  5.39700   1.000 15.73308  ? 245 ARG BA CG  1 
ATOM   4014 C  CD  . ARG B 1 245 ? 26.24700  -8.04600  4.42300   1.000 23.04013  ? 245 ARG BA CD  1 
ATOM   4015 N  NE  . ARG B 1 245 ? 25.92900  -9.44100  4.13900   1.000 20.60558  ? 245 ARG BA NE  1 
ATOM   4016 C  CZ  . ARG B 1 245 ? 24.76300  -9.86200  3.66800   1.000 22.94758  ? 245 ARG BA CZ  1 
ATOM   4017 N  NH1 . ARG B 1 245 ? 23.77600  -9.01900  3.41000   1.000 26.10931  ? 245 ARG BA NH1 1 
ATOM   4018 N  NH2 . ARG B 1 245 ? 24.58200  -11.16200 3.45100   1.000 20.08076  ? 245 ARG BA NH2 1 
ATOM   4019 N  N   . MET B 1 246 ? 27.76200  -6.03800  8.85900   1.000 9.03596   ? 246 MET BA N   1 
ATOM   4020 C  CA  . MET B 1 246 ? 27.86000  -6.54500  10.22300  1.000 13.91594  ? 246 MET BA CA  1 
ATOM   4021 C  C   . MET B 1 246 ? 26.59800  -6.23000  11.01500  1.000 11.06738  ? 246 MET BA C   1 
ATOM   4022 O  O   . MET B 1 246 ? 26.08700  -7.08200  11.75200  1.000 5.41342   ? 246 MET BA O   1 
ATOM   4023 C  CB  . MET B 1 246 ? 29.08600  -5.94400  10.91000  1.000 5.07590   ? 246 MET BA CB  1 
ATOM   4024 C  CG  . MET B 1 246 ? 29.21300  -6.27900  12.38500  1.000 20.04048  ? 246 MET BA CG  1 
ATOM   4025 S  SD  . MET B 1 246 ? 30.93700  -6.29700  12.92100  1.000 17.76938  ? 246 MET BA SD  1 
ATOM   4026 C  CE  . MET B 1 246 ? 30.81600  -5.38200  14.45400  1.000 14.77355  ? 246 MET BA CE  1 
ATOM   4027 N  N   . ALA B 1 247 ? 26.08000  -5.00500  10.87500  1.000 3.98234   ? 247 ALA BA N   1 
ATOM   4028 C  CA  . ALA B 1 247 ? 24.86300  -4.62800  11.58600  1.000 10.27009  ? 247 ALA BA CA  1 
ATOM   4029 C  C   . ALA B 1 247 ? 23.66800  -5.44100  11.10700  1.000 13.48638  ? 247 ALA BA C   1 
ATOM   4030 O  O   . ALA B 1 247 ? 22.78700  -5.79000  11.90200  1.000 9.51619   ? 247 ALA BA O   1 
ATOM   4031 C  CB  . ALA B 1 247 ? 24.59500  -3.13300  11.41500  1.000 4.38986   ? 247 ALA BA CB  1 
ATOM   4032 N  N   . THR B 1 248 ? 23.62100  -5.75300  9.80900   1.000 11.09915  ? 248 THR BA N   1 
ATOM   4033 C  CA  . THR B 1 248 ? 22.50900  -6.53300  9.27200   1.000 9.03134   ? 248 THR BA CA  1 
ATOM   4034 C  C   . THR B 1 248 ? 22.52700  -7.96100  9.80400   1.000 9.10882   ? 248 THR BA C   1 
ATOM   4035 O  O   . THR B 1 248 ? 21.48700  -8.49200  10.21100  1.000 11.61612  ? 248 THR BA O   1 
ATOM   4036 C  CB  . THR B 1 248 ? 22.55400  -6.52800  7.74200   1.000 8.99518   ? 248 THR BA CB  1 
ATOM   4037 O  OG1 . THR B 1 248 ? 22.27200  -5.20800  7.25900   1.000 10.40397  ? 248 THR BA OG1 1 
ATOM   4038 C  CG2 . THR B 1 248 ? 21.52800  -7.49900  7.16900   1.000 1.90718   ? 248 THR BA CG2 1 
ATOM   4039 N  N   . LEU B 1 249 ? 23.70100  -8.59600  9.81600   1.000 8.02437   ? 249 LEU BA N   1 
ATOM   4040 C  CA  . LEU B 1 249 ? 23.78500  -9.97100  10.29400  1.000 7.32864   ? 249 LEU BA CA  1 
ATOM   4041 C  C   . LEU B 1 249 ? 23.55600  -10.06100 11.79700  1.000 7.97595   ? 249 LEU BA C   1 
ATOM   4042 O  O   . LEU B 1 249 ? 23.09000  -11.09400 12.28800  1.000 7.14846   ? 249 LEU BA O   1 
ATOM   4043 C  CB  . LEU B 1 249 ? 25.13800  -10.57400 9.92300   1.000 5.60612   ? 249 LEU BA CB  1 
ATOM   4044 C  CG  . LEU B 1 249 ? 25.37600  -10.74500 8.42100   1.000 21.87539  ? 249 LEU BA CG  1 
ATOM   4045 C  CD1 . LEU B 1 249 ? 26.86400  -10.75900 8.09500   1.000 18.88387  ? 249 LEU BA CD1 1 
ATOM   4046 C  CD2 . LEU B 1 249 ? 24.70200  -12.00700 7.91800   1.000 27.62975  ? 249 LEU BA CD2 1 
ATOM   4047 N  N   . ALA B 1 250 ? 23.87100  -8.99400  12.53800  1.000 8.23642   ? 250 ALA BA N   1 
ATOM   4048 C  CA  . ALA B 1 250 ? 23.67300  -9.00600  13.98300  1.000 9.17420   ? 250 ALA BA CA  1 
ATOM   4049 C  C   . ALA B 1 250 ? 22.20700  -9.19900  14.35200  1.000 11.09584  ? 250 ALA BA C   1 
ATOM   4050 O  O   . ALA B 1 250 ? 21.90500  -9.74400  15.42000  1.000 5.86599   ? 250 ALA BA O   1 
ATOM   4051 C  CB  . ALA B 1 250 ? 24.20600  -7.71100  14.59700  1.000 7.40952   ? 250 ALA BA CB  1 
ATOM   4052 N  N   . HIS B 1 251 ? 21.28700  -8.76700  13.48600  1.000 4.66818   ? 251 HIS BA N   1 
ATOM   4053 C  CA  . HIS B 1 251 ? 19.86500  -8.95000  13.75200  1.000 9.78406   ? 251 HIS BA CA  1 
ATOM   4054 C  C   . HIS B 1 251 ? 19.47200  -10.41900 13.82400  1.000 7.27845   ? 251 HIS BA C   1 
ATOM   4055 O  O   . HIS B 1 251 ? 18.44900  -10.74600 14.43600  1.000 7.19378   ? 251 HIS BA O   1 
ATOM   4056 C  CB  . HIS B 1 251 ? 19.03400  -8.24100  12.68300  1.000 2.98410   ? 251 HIS BA CB  1 
ATOM   4057 C  CG  . HIS B 1 251 ? 18.80200  -6.79000  12.96700  1.000 11.83379  ? 251 HIS BA CG  1 
ATOM   4058 N  ND1 . HIS B 1 251 ? 17.81800  -6.34900  13.82500  1.000 7.87926   ? 251 HIS BA ND1 1 
ATOM   4059 C  CD2 . HIS B 1 251 ? 19.43000  -5.68000  12.51200  1.000 7.01882   ? 251 HIS BA CD2 1 
ATOM   4060 C  CE1 . HIS B 1 251 ? 17.84700  -5.02900  13.88400  1.000 12.20721  ? 251 HIS BA CE1 1 
ATOM   4061 N  NE2 . HIS B 1 251 ? 18.81600  -4.59800  13.09600  1.000 7.71237   ? 251 HIS BA NE2 1 
ATOM   4062 N  N   . ASN B 1 252 ? 20.25500  -11.31100 13.21100  1.000 5.50052   ? 252 ASN BA N   1 
ATOM   4063 C  CA  . ASN B 1 252 ? 19.97900  -12.73800 13.33600  1.000 10.26869  ? 252 ASN BA CA  1 
ATOM   4064 C  C   . ASN B 1 252 ? 20.09600  -13.20100 14.78000  1.000 9.54972   ? 252 ASN BA C   1 
ATOM   4065 O  O   . ASN B 1 252 ? 19.40500  -14.14200 15.18800  1.000 8.91397   ? 252 ASN BA O   1 
ATOM   4066 C  CB  . ASN B 1 252 ? 20.92500  -13.53700 12.44000  1.000 8.97113   ? 252 ASN BA CB  1 
ATOM   4067 C  CG  . ASN B 1 252 ? 20.70100  -13.26400 10.96700  1.000 10.76055  ? 252 ASN BA CG  1 
ATOM   4068 O  OD1 . ASN B 1 252 ? 19.59800  -12.90900 10.55100  1.000 7.77633   ? 252 ASN BA OD1 1 
ATOM   4069 N  ND2 . ASN B 1 252 ? 21.74900  -13.42700 10.16800  1.000 6.36985   ? 252 ASN BA ND2 1 
ATOM   4070 N  N   . GLY B 1 253 ? 20.95900  -12.55600 15.56700  1.000 5.36100   ? 253 GLY BA N   1 
ATOM   4071 C  CA  . GLY B 1 253 ? 21.05600  -12.90000 16.97600  1.000 7.55584   ? 253 GLY BA CA  1 
ATOM   4072 C  C   . GLY B 1 253 ? 19.81100  -12.51700 17.75300  1.000 13.27372  ? 253 GLY BA C   1 
ATOM   4073 O  O   . GLY B 1 253 ? 19.41300  -13.21700 18.68800  1.000 12.07851  ? 253 GLY BA O   1 
ATOM   4074 N  N   . LEU B 1 254 ? 19.18200  -11.39900 17.38200  1.000 6.52723   ? 254 LEU BA N   1 
ATOM   4075 C  CA  . LEU B 1 254 ? 17.93200  -11.00600 18.02400  1.000 10.16798  ? 254 LEU BA CA  1 
ATOM   4076 C  C   . LEU B 1 254 ? 16.82500  -12.01000 17.72800  1.000 17.80696  ? 254 LEU BA C   1 
ATOM   4077 O  O   . LEU B 1 254 ? 16.00600  -12.31900 18.60200  1.000 15.21091  ? 254 LEU BA O   1 
ATOM   4078 C  CB  . LEU B 1 254 ? 17.52100  -9.60500  17.57100  1.000 4.67305   ? 254 LEU BA CB  1 
ATOM   4079 C  CG  . LEU B 1 254 ? 18.49900  -8.46100  17.85100  1.000 11.85049  ? 254 LEU BA CG  1 
ATOM   4080 C  CD1 . LEU B 1 254 ? 17.82500  -7.11700  17.62700  1.000 8.63451   ? 254 LEU BA CD1 1 
ATOM   4081 C  CD2 . LEU B 1 254 ? 19.05100  -8.55300  19.26200  1.000 6.46444   ? 254 LEU BA CD2 1 
ATOM   4082 N  N   . ALA B 1 255 ? 16.78300  -12.53100 16.49900  1.000 12.38133  ? 255 ALA BA N   1 
ATOM   4083 C  CA  . ALA B 1 255 ? 15.80400  -13.55600 16.15700  1.000 10.59936  ? 255 ALA BA CA  1 
ATOM   4084 C  C   . ALA B 1 255 ? 16.03700  -14.84900 16.92700  1.000 17.29393  ? 255 ALA BA C   1 
ATOM   4085 O  O   . ALA B 1 255 ? 15.10000  -15.63700 17.08800  1.000 19.16455  ? 255 ALA BA O   1 
ATOM   4086 C  CB  . ALA B 1 255 ? 15.83200  -13.83100 14.65300  1.000 12.86588  ? 255 ALA BA CB  1 
ATOM   4087 N  N   . ARG B 1 256 ? 17.26200  -15.07600 17.40400  1.000 14.15196  ? 256 ARG BA N   1 
ATOM   4088 C  CA  . ARG B 1 256 ? 17.55500  -16.26000 18.20500  1.000 21.20070  ? 256 ARG BA CA  1 
ATOM   4089 C  C   . ARG B 1 256 ? 16.82100  -16.21900 19.53900  1.000 17.70056  ? 256 ARG BA C   1 
ATOM   4090 O  O   . ARG B 1 256 ? 16.21300  -17.21100 19.95800  1.000 28.53719  ? 256 ARG BA O   1 
ATOM   4091 C  CB  . ARG B 1 256 ? 19.06000  -16.36200 18.44300  1.000 37.00612  ? 256 ARG BA CB  1 
ATOM   4092 C  CG  . ARG B 1 256 ? 19.89800  -16.56800 17.20100  1.000 36.57150  ? 256 ARG BA CG  1 
ATOM   4093 C  CD  . ARG B 1 256 ? 19.54000  -17.85800 16.51300  1.000 27.47624  ? 256 ARG BA CD  1 
ATOM   4094 N  NE  . ARG B 1 256 ? 20.73700  -18.64700 16.25700  1.000 55.76122  ? 256 ARG BA NE  1 
ATOM   4095 C  CZ  . ARG B 1 256 ? 20.97600  -19.83500 16.79500  1.000 78.46544  ? 256 ARG BA CZ  1 
ATOM   4096 N  NH1 . ARG B 1 256 ? 20.11700  -20.40100 17.62700  1.000 44.68554  ? 256 ARG BA NH1 1 
ATOM   4097 N  NH2 . ARG B 1 256 ? 22.10900  -20.46500 16.50000  1.000 80.83947  ? 256 ARG BA NH2 1 
ATOM   4098 N  N   . ALA B 1 257 ? 16.87100  -15.07600 20.22100  1.000 16.67497  ? 257 ALA BA N   1 
ATOM   4099 C  CA  . ALA B 1 257 ? 16.42700  -14.97400 21.60500  1.000 18.55265  ? 257 ALA BA CA  1 
ATOM   4100 C  C   . ALA B 1 257 ? 15.02900  -14.39900 21.76600  1.000 9.48597   ? 257 ALA BA C   1 
ATOM   4101 O  O   . ALA B 1 257 ? 14.37900  -14.67500 22.77900  1.000 21.47868  ? 257 ALA BA O   1 
ATOM   4102 C  CB  . ALA B 1 257 ? 17.41000  -14.11400 22.40700  1.000 17.07819  ? 257 ALA BA CB  1 
ATOM   4103 N  N   . ILE B 1 258 ? 14.54800  -13.61200 20.80700  1.000 9.90952   ? 258 ILE BA N   1 
ATOM   4104 C  CA  . ILE B 1 258 ? 13.30700  -12.85900 20.94800  1.000 10.02581  ? 258 ILE BA CA  1 
ATOM   4105 C  C   . ILE B 1 258 ? 12.28200  -13.37300 19.94800  1.000 11.36259  ? 258 ILE BA C   1 
ATOM   4106 O  O   . ILE B 1 258 ? 12.60100  -13.59100 18.77300  1.000 7.63059   ? 258 ILE BA O   1 
ATOM   4107 C  CB  . ILE B 1 258 ? 13.54800  -11.34900 20.75600  1.000 9.02649   ? 258 ILE BA CB  1 
ATOM   4108 C  CG1 . ILE B 1 258 ? 14.74300  -10.89500 21.59500  1.000 13.24084  ? 258 ILE BA CG1 1 
ATOM   4109 C  CG2 . ILE B 1 258 ? 12.30000  -10.56000 21.11400  1.000 8.92743   ? 258 ILE BA CG2 1 
ATOM   4110 C  CD1 . ILE B 1 258 ? 15.11200  -9.44000  21.41400  1.000 12.77075  ? 258 ILE BA CD1 1 
ATOM   4111 N  N   . CYS B 1 259 ? 11.04200  -13.55500 20.41600  1.000 8.51068   ? 259 CYS BA N   1 
ATOM   4112 C  CA  . CYS B 1 259 ? 9.94400   -13.97400 19.55200  1.000 11.24288  ? 259 CYS BA CA  1 
ATOM   4113 C  C   . CYS B 1 259 ? 8.60300   -13.53200 20.12800  1.000 10.38501  ? 259 CYS BA C   1 
ATOM   4114 O  O   . CYS B 1 259 ? 8.27200   -13.88400 21.26800  1.000 11.51549  ? 259 CYS BA O   1 
ATOM   4115 C  CB  . CYS B 1 259 ? 9.95800   -15.49000 19.35500  1.000 14.55418  ? 259 CYS BA CB  1 
ATOM   4116 S  SG  . CYS B 1 259 ? 8.78100   -16.07900 18.11500  1.000 17.93225  ? 259 CYS BA SG  1 
ATOM   4117 N  N   . PRO B 1 260 ? 7.79600   -12.76300 19.37700  1.000 10.66596  ? 260 PRO BA N   1 
ATOM   4118 C  CA  . PRO B 1 260 ? 8.11800   -12.25700 18.03800  1.000 10.43930  ? 260 PRO BA CA  1 
ATOM   4119 C  C   . PRO B 1 260 ? 9.11200   -11.10100 18.06800  1.000 9.08936   ? 260 PRO BA C   1 
ATOM   4120 O  O   . PRO B 1 260 ? 9.30600   -10.47600 19.11100  1.000 8.43255   ? 260 PRO BA O   1 
ATOM   4121 C  CB  . PRO B 1 260 ? 6.76000   -11.78300 17.49300  1.000 13.99918  ? 260 PRO BA CB  1 
ATOM   4122 C  CG  . PRO B 1 260 ? 5.72900   -12.25900 18.47600  1.000 15.43891  ? 260 PRO BA CG  1 
ATOM   4123 C  CD  . PRO B 1 260 ? 6.42900   -12.39900 19.78200  1.000 7.87299   ? 260 PRO BA CD  1 
ATOM   4124 N  N   . ILE B 1 261 ? 9.73300   -10.83300 16.92000  1.000 9.39236   ? 261 ILE BA N   1 
ATOM   4125 C  CA  . ILE B 1 261 ? 10.73200  -9.78600  16.77100  1.000 8.02909   ? 261 ILE BA CA  1 
ATOM   4126 C  C   . ILE B 1 261 ? 10.40000  -9.00500  15.50500  1.000 14.59553  ? 261 ILE BA C   1 
ATOM   4127 O  O   . ILE B 1 261 ? 9.71400   -9.50000  14.60700  1.000 15.30354  ? 261 ILE BA O   1 
ATOM   4128 C  CB  . ILE B 1 261 ? 12.16700  -10.36800 16.71700  1.000 9.18203   ? 261 ILE BA CB  1 
ATOM   4129 C  CG1 . ILE B 1 261 ? 13.23000  -9.26500  16.76000  1.000 8.41896   ? 261 ILE BA CG1 1 
ATOM   4130 C  CG2 . ILE B 1 261 ? 12.34300  -11.25600 15.49300  1.000 9.28718   ? 261 ILE BA CG2 1 
ATOM   4131 C  CD1 . ILE B 1 261 ? 13.38800  -8.62100  18.12000  1.000 9.01766   ? 261 ILE BA CD1 1 
ATOM   4132 N  N   . HIS B 1 262 ? 10.87600  -7.75800  15.45600  1.000 11.81797  ? 262 HIS BA N   1 
ATOM   4133 C  CA  . HIS B 1 262 ? 10.66500  -6.86700  14.31000  1.000 7.40827   ? 262 HIS BA CA  1 
ATOM   4134 C  C   . HIS B 1 262 ? 9.17900   -6.61800  14.05700  1.000 12.34392  ? 262 HIS BA C   1 
ATOM   4135 O  O   . HIS B 1 262 ? 8.74300   -6.49000  12.91100  1.000 12.90756  ? 262 HIS BA O   1 
ATOM   4136 C  CB  . HIS B 1 262 ? 11.33200  -7.40900  13.04100  1.000 9.68107   ? 262 HIS BA CB  1 
ATOM   4137 C  CG  . HIS B 1 262 ? 12.77100  -7.78900  13.21200  1.000 15.79543  ? 262 HIS BA CG  1 
ATOM   4138 N  ND1 . HIS B 1 262 ? 13.65000  -7.06300  13.98600  1.000 17.76083  ? 262 HIS BA ND1 1 
ATOM   4139 C  CD2 . HIS B 1 262 ? 13.48700  -8.81300  12.69000  1.000 16.37024  ? 262 HIS BA CD2 1 
ATOM   4140 C  CE1 . HIS B 1 262 ? 14.84400  -7.62900  13.94100  1.000 12.45590  ? 262 HIS BA CE1 1 
ATOM   4141 N  NE2 . HIS B 1 262 ? 14.77200  -8.69200  13.16100  1.000 12.47227  ? 262 HIS BA NE2 1 
ATOM   4142 N  N   . THR B 1 263 ? 8.39100   -6.54400  15.12800  1.000 7.21940   ? 263 THR BA N   1 
ATOM   4143 C  CA  . THR B 1 263 ? 6.95500   -6.34900  14.98700  1.000 8.32213   ? 263 THR BA CA  1 
ATOM   4144 C  C   . THR B 1 263 ? 6.63800   -4.88400  14.68700  1.000 11.53233  ? 263 THR BA C   1 
ATOM   4145 O  O   . THR B 1 263 ? 7.52200   -4.02600  14.61400  1.000 11.61188  ? 263 THR BA O   1 
ATOM   4146 C  CB  . THR B 1 263 ? 6.22100   -6.81300  16.24300  1.000 9.92992   ? 263 THR BA CB  1 
ATOM   4147 O  OG1 . THR B 1 263 ? 6.52800   -5.93400  17.33300  1.000 8.71062   ? 263 THR BA OG1 1 
ATOM   4148 C  CG2 . THR B 1 263 ? 6.62700   -8.23400  16.60300  1.000 8.16300   ? 263 THR BA CG2 1 
ATOM   4149 N  N   . ASN B 1 264 ? 5.34700   -4.59300  14.51300  1.000 15.88549  ? 264 ASN BA N   1 
ATOM   4150 C  CA  . ASN B 1 264 ? 4.91000   -3.24000  14.18900  1.000 6.21922   ? 264 ASN BA CA  1 
ATOM   4151 C  C   . ASN B 1 264 ? 5.04800   -2.27200  15.35700  1.000 11.08702  ? 264 ASN BA C   1 
ATOM   4152 O  O   . ASN B 1 264 ? 4.95900   -1.05900  15.14200  1.000 18.86580  ? 264 ASN BA O   1 
ATOM   4153 C  CB  . ASN B 1 264 ? 3.45900   -3.25500  13.70300  1.000 14.44928  ? 264 ASN BA CB  1 
ATOM   4154 C  CG  . ASN B 1 264 ? 3.31900   -3.80800  12.29600  1.000 24.74766  ? 264 ASN BA CG  1 
ATOM   4155 O  OD1 . ASN B 1 264 ? 4.28700   -3.85700  11.53600  1.000 21.81970  ? 264 ASN BA OD1 1 
ATOM   4156 N  ND2 . ASN B 1 264 ? 2.10700   -4.22000  11.93900  1.000 28.50422  ? 264 ASN BA ND2 1 
ATOM   4157 N  N   . VAL B 1 265 ? 5.25300   -2.76700  16.58100  1.000 6.32480   ? 265 VAL BA N   1 
ATOM   4158 C  CA  . VAL B 1 265 ? 5.49600   -1.90000  17.72700  1.000 11.62993  ? 265 VAL BA CA  1 
ATOM   4159 C  C   . VAL B 1 265 ? 6.96100   -1.87500  18.13400  1.000 12.51884  ? 265 VAL BA C   1 
ATOM   4160 O  O   . VAL B 1 265 ? 7.30400   -1.24200  19.14100  1.000 11.55814  ? 265 VAL BA O   1 
ATOM   4161 C  CB  . VAL B 1 265 ? 4.62000   -2.30200  18.93200  1.000 10.49411  ? 265 VAL BA CB  1 
ATOM   4162 C  CG1 . VAL B 1 265 ? 3.14700   -2.31100  18.54400  1.000 12.03344  ? 265 VAL BA CG1 1 
ATOM   4163 C  CG2 . VAL B 1 265 ? 5.04400   -3.65600  19.47100  1.000 11.72386  ? 265 VAL BA CG2 1 
ATOM   4164 N  N   . ASP B 1 266 ? 7.83500   -2.54000  17.38300  1.000 13.06408  ? 266 ASP BA N   1 
ATOM   4165 C  CA  . ASP B 1 266 ? 9.25700   -2.59700  17.69300  1.000 7.70678   ? 266 ASP BA CA  1 
ATOM   4166 C  C   . ASP B 1 266 ? 10.03100  -1.62500  16.81200  1.000 10.46118  ? 266 ASP BA C   1 
ATOM   4167 O  O   . ASP B 1 266 ? 9.76000   -1.50500  15.61300  1.000 8.12874   ? 266 ASP BA O   1 
ATOM   4168 C  CB  . ASP B 1 266 ? 9.80600   -4.01200  17.49800  1.000 6.73782   ? 266 ASP BA CB  1 
ATOM   4169 C  CG  . ASP B 1 266 ? 9.34100   -4.97400  18.56900  1.000 18.58584  ? 266 ASP BA CG  1 
ATOM   4170 O  OD1 . ASP B 1 266 ? 9.40600   -4.61600  19.76500  1.000 9.85695   ? 266 ASP BA OD1 1 
ATOM   4171 O  OD2 . ASP B 1 266 ? 8.91800   -6.09500  18.21000  1.000 11.36297  ? 266 ASP BA OD2 1 
ATOM   4172 N  N   . GLY B 1 267 ? 10.99900  -0.93700  17.41200  1.000 12.32751  ? 267 GLY BA N   1 
ATOM   4173 C  CA  . GLY B 1 267 ? 11.88900  -0.07200  16.66400  1.000 8.05586   ? 267 GLY BA CA  1 
ATOM   4174 C  C   . GLY B 1 267 ? 13.30200  -0.61800  16.62100  1.000 15.38319  ? 267 GLY BA C   1 
ATOM   4175 O  O   . GLY B 1 267 ? 14.27300  0.13500   16.74600  1.000 9.12052   ? 267 GLY BA O   1 
ATOM   4176 N  N   . ASP B 1 268 ? 13.41600  -1.93300  16.43100  1.000 3.89527   ? 268 ASP BA N   1 
ATOM   4177 C  CA  . ASP B 1 268 ? 14.69600  -2.62200  16.55400  1.000 8.51890   ? 268 ASP BA CA  1 
ATOM   4178 C  C   . ASP B 1 268 ? 15.75100  -2.01500  15.63500  1.000 10.83206  ? 268 ASP BA C   1 
ATOM   4179 O  O   . ASP B 1 268 ? 15.54200  -1.88500  14.42500  1.000 15.31962  ? 268 ASP BA O   1 
ATOM   4180 C  CB  . ASP B 1 268 ? 14.51300  -4.11000  16.25000  1.000 4.30516   ? 268 ASP BA CB  1 
ATOM   4181 C  CG  . ASP B 1 268 ? 13.38000  -4.73300  17.05100  1.000 15.49237  ? 268 ASP BA CG  1 
ATOM   4182 O  OD1 . ASP B 1 268 ? 13.12400  -4.27100  18.18400  1.000 8.38419   ? 268 ASP BA OD1 1 
ATOM   4183 O  OD2 . ASP B 1 268 ? 12.74700  -5.68600  16.55100  1.000 8.87825   ? 268 ASP BA OD2 1 
ATOM   4184 N  N   . THR B 1 269 ? 16.89000  -1.64800  16.22100  1.000 7.22345   ? 269 THR BA N   1 
ATOM   4185 C  CA  . THR B 1 269 ? 17.97000  -0.96500  15.51800  1.000 5.22544   ? 269 THR BA CA  1 
ATOM   4186 C  C   . THR B 1 269 ? 19.30400  -1.46000  16.05300  1.000 7.84617   ? 269 THR BA C   1 
ATOM   4187 O  O   . THR B 1 269 ? 19.48500  -1.56000  17.26900  1.000 11.20815  ? 269 THR BA O   1 
ATOM   4188 C  CB  . THR B 1 269 ? 17.87100  0.55600   15.69900  1.000 5.81477   ? 269 THR BA CB  1 
ATOM   4189 O  OG1 . THR B 1 269 ? 16.65900  1.03500   15.10700  1.000 9.71982   ? 269 THR BA OG1 1 
ATOM   4190 C  CG2 . THR B 1 269 ? 19.06100  1.25600   15.05600  1.000 4.27546   ? 269 THR BA CG2 1 
ATOM   4191 N  N   . ILE B 1 270 ? 20.23600  -1.76300  15.15300  1.000 7.54706   ? 270 ILE BA N   1 
ATOM   4192 C  CA  . ILE B 1 270 ? 21.57800  -2.19900  15.52800  1.000 8.27563   ? 270 ILE BA CA  1 
ATOM   4193 C  C   . ILE B 1 270 ? 22.58900  -1.28100  14.85600  1.000 7.63681   ? 270 ILE BA C   1 
ATOM   4194 O  O   . ILE B 1 270 ? 22.63400  -1.19500  13.62200  1.000 13.61493  ? 270 ILE BA O   1 
ATOM   4195 C  CB  . ILE B 1 270 ? 21.83800  -3.66500  15.14700  1.000 8.48136   ? 270 ILE BA CB  1 
ATOM   4196 C  CG1 . ILE B 1 270 ? 21.00400  -4.60400  16.01800  1.000 9.06893   ? 270 ILE BA CG1 1 
ATOM   4197 C  CG2 . ILE B 1 270 ? 23.31900  -3.99300  15.28800  1.000 7.35683   ? 270 ILE BA CG2 1 
ATOM   4198 C  CD1 . ILE B 1 270 ? 21.33300  -4.51900  17.49300  1.000 17.15439  ? 270 ILE BA CD1 1 
ATOM   4199 N  N   . PHE B 1 271 ? 23.38800  -0.59300  15.66600  1.000 11.59590  ? 271 PHE BA N   1 
ATOM   4200 C  CA  . PHE B 1 271 ? 24.55800  0.12400   15.18400  1.000 3.90899   ? 271 PHE BA CA  1 
ATOM   4201 C  C   . PHE B 1 271 ? 25.77000  -0.79900  15.21900  1.000 9.75863   ? 271 PHE BA C   1 
ATOM   4202 O  O   . PHE B 1 271 ? 25.88700  -1.66700  16.08800  1.000 14.57542  ? 271 PHE BA O   1 
ATOM   4203 C  CB  . PHE B 1 271 ? 24.83500  1.36400   16.03900  1.000 8.18077   ? 271 PHE BA CB  1 
ATOM   4204 C  CG  . PHE B 1 271 ? 23.69500  2.34200   16.09200  1.000 10.19271  ? 271 PHE BA CG  1 
ATOM   4205 C  CD1 . PHE B 1 271 ? 23.58900  3.35600   15.15500  1.000 6.37673   ? 271 PHE BA CD1 1 
ATOM   4206 C  CD2 . PHE B 1 271 ? 22.73700  2.25400   17.08900  1.000 8.05431   ? 271 PHE BA CD2 1 
ATOM   4207 C  CE1 . PHE B 1 271 ? 22.54300  4.26000   15.20600  1.000 12.15195  ? 271 PHE BA CE1 1 
ATOM   4208 C  CE2 . PHE B 1 271 ? 21.69000  3.15400   17.14600  1.000 13.70269  ? 271 PHE BA CE2 1 
ATOM   4209 C  CZ  . PHE B 1 271 ? 21.59300  4.15800   16.20300  1.000 12.87287  ? 271 PHE BA CZ  1 
ATOM   4210 N  N   . ALA B 1 272 ? 26.67700  -0.60600  14.26600  1.000 6.93630   ? 272 ALA BA N   1 
ATOM   4211 C  CA  . ALA B 1 272 ? 27.90000  -1.39200  14.19700  1.000 6.56035   ? 272 ALA BA CA  1 
ATOM   4212 C  C   . ALA B 1 272 ? 29.08500  -0.46700  13.97500  1.000 8.63071   ? 272 ALA BA C   1 
ATOM   4213 O  O   . ALA B 1 272 ? 28.97600  0.52900   13.25400  1.000 12.22483  ? 272 ALA BA O   1 
ATOM   4214 C  CB  . ALA B 1 272 ? 27.83400  -2.44000  13.07900  1.000 5.96336   ? 272 ALA BA CB  1 
ATOM   4215 N  N   . THR B 1 273 ? 30.21500  -0.79300  14.60500  1.000 5.52808   ? 273 THR BA N   1 
ATOM   4216 C  CA  . THR B 1 273 ? 31.43400  -0.00900  14.45800  1.000 9.25236   ? 273 THR BA CA  1 
ATOM   4217 C  C   . THR B 1 273 ? 32.63500  -0.92700  14.28800  1.000 13.12982  ? 273 THR BA C   1 
ATOM   4218 O  O   . THR B 1 273 ? 32.72600  -1.97700  14.93100  1.000 9.66506   ? 273 THR BA O   1 
ATOM   4219 C  CB  . THR B 1 273 ? 31.68900  0.91100   15.66600  1.000 8.78603   ? 273 THR BA CB  1 
ATOM   4220 O  OG1 . THR B 1 273 ? 31.88800  0.11900   16.84400  1.000 13.50151  ? 273 THR BA OG1 1 
ATOM   4221 C  CG2 . THR B 1 273 ? 30.52800  1.87000   15.88600  1.000 6.89804   ? 273 THR BA CG2 1 
ATOM   4222 N  N   . GLY B 1 274 ? 33.54800  -0.52000  13.40600  1.000 14.02205  ? 274 GLY BA N   1 
ATOM   4223 C  CA  . GLY B 1 274 ? 34.88900  -1.05400  13.35600  1.000 10.11770  ? 274 GLY BA CA  1 
ATOM   4224 C  C   . GLY B 1 274 ? 35.89100  0.07200   13.55700  1.000 13.64385  ? 274 GLY BA C   1 
ATOM   4225 O  O   . GLY B 1 274 ? 35.52700  1.24300   13.67100  1.000 9.54422   ? 274 GLY BA O   1 
ATOM   4226 N  N   . LEU B 1 275 ? 37.16300  -0.30500  13.60100  1.000 11.88108  ? 275 LEU BA N   1 
ATOM   4227 C  CA  . LEU B 1 275 ? 38.22800  0.67200   13.78300  1.000 16.55616  ? 275 LEU BA CA  1 
ATOM   4228 C  C   . LEU B 1 275 ? 38.77000  1.11900   12.43100  1.000 16.78857  ? 275 LEU BA C   1 
ATOM   4229 O  O   . LEU B 1 275 ? 38.97200  0.30200   11.52900  1.000 19.68116  ? 275 LEU BA O   1 
ATOM   4230 C  CB  . LEU B 1 275 ? 39.35600  0.09200   14.63700  1.000 14.83350  ? 275 LEU BA CB  1 
ATOM   4231 C  CG  . LEU B 1 275 ? 39.05200  -0.03600  16.13200  1.000 24.60257  ? 275 LEU BA CG  1 
ATOM   4232 C  CD1 . LEU B 1 275 ? 40.18800  -0.74500  16.85600  1.000 27.91757  ? 275 LEU BA CD1 1 
ATOM   4233 C  CD2 . LEU B 1 275 ? 38.78600  1.33000   16.75000  1.000 20.50803  ? 275 LEU BA CD2 1 
ATOM   4234 N  N   . GLN B 1 276 ? 38.99200  2.42900   12.28900  1.000 19.89744  ? 276 GLN BA N   1 
ATOM   4235 C  CA  . GLN B 1 276 ? 39.58600  2.93100   11.05300  1.000 12.40307  ? 276 GLN BA CA  1 
ATOM   4236 C  C   . GLN B 1 276 ? 41.04400  2.50500   10.93100  1.000 17.14020  ? 276 GLN BA C   1 
ATOM   4237 O  O   . GLN B 1 276 ? 41.48500  2.08400   9.85600   1.000 30.52109  ? 276 GLN BA O   1 
ATOM   4238 C  CB  . GLN B 1 276 ? 39.46500  4.45400   10.97800  1.000 21.37564  ? 276 GLN BA CB  1 
ATOM   4239 C  CG  . GLN B 1 276 ? 38.07400  4.99700   11.26300  1.000 27.81959  ? 276 GLN BA CG  1 
ATOM   4240 C  CD  . GLN B 1 276 ? 37.91700  6.44200   10.82800  1.000 29.31475  ? 276 GLN BA CD  1 
ATOM   4241 O  OE1 . GLN B 1 276 ? 38.88500  7.08700   10.42300  1.000 37.52856  ? 276 GLN BA OE1 1 
ATOM   4242 N  NE2 . GLN B 1 276 ? 36.69500  6.95700   10.90300  1.000 21.76246  ? 276 GLN BA NE2 1 
ATOM   4243 N  N   . LYS B 1 277 ? 41.80300  2.60200   12.01900  1.000 10.98988  ? 277 LYS BA N   1 
ATOM   4244 C  CA  . LYS B 1 277 ? 43.21000  2.21600   12.04600  1.000 26.94026  ? 277 LYS BA CA  1 
ATOM   4245 C  C   . LYS B 1 277 ? 43.34900  0.97400   12.91800  1.000 18.95967  ? 277 LYS BA C   1 
ATOM   4246 O  O   . LYS B 1 277 ? 43.21500  1.05000   14.14400  1.000 25.52090  ? 277 LYS BA O   1 
ATOM   4247 C  CB  . LYS B 1 277 ? 44.07800  3.35700   12.57200  1.000 30.81082  ? 277 LYS BA CB  1 
ATOM   4248 C  CG  . LYS B 1 277 ? 44.81800  4.12800   11.48900  1.000 59.54270  ? 277 LYS BA CG  1 
ATOM   4249 C  CD  . LYS B 1 277 ? 46.00200  3.33800   10.95400  1.000 75.57354  ? 277 LYS BA CD  1 
ATOM   4250 C  CE  . LYS B 1 277 ? 46.65200  4.04700   9.77600   1.000 73.85536  ? 277 LYS BA CE  1 
ATOM   4251 N  NZ  . LYS B 1 277 ? 48.11000  3.75900   9.68700   1.000 74.76771  ? 277 LYS BA NZ  1 
ATOM   4252 N  N   . SER B 1 278 ? 43.61500  -0.16700  12.28600  1.000 17.77623  ? 278 SER BA N   1 
ATOM   4253 C  CA  . SER B 1 278 ? 43.80500  -1.41400  13.01200  1.000 18.09237  ? 278 SER BA CA  1 
ATOM   4254 C  C   . SER B 1 278 ? 44.49200  -2.41400  12.09700  1.000 22.20045  ? 278 SER BA C   1 
ATOM   4255 O  O   . SER B 1 278 ? 44.32400  -2.37600  10.87600  1.000 27.17979  ? 278 SER BA O   1 
ATOM   4256 C  CB  . SER B 1 278 ? 42.47500  -1.98200  13.52000  1.000 15.96704  ? 278 SER BA CB  1 
ATOM   4257 O  OG  . SER B 1 278 ? 42.58000  -3.37200  13.77600  1.000 15.56387  ? 278 SER BA OG  1 
ATOM   4258 N  N   . ASP B 1 279 ? 45.26700  -3.31000  12.70600  1.000 24.67652  ? 279 ASP BA N   1 
ATOM   4259 C  CA  . ASP B 1 279 ? 45.95500  -4.35900  11.96700  1.000 28.67818  ? 279 ASP BA CA  1 
ATOM   4260 C  C   . ASP B 1 279 ? 45.11500  -5.61600  11.80200  1.000 32.08149  ? 279 ASP BA C   1 
ATOM   4261 O  O   . ASP B 1 279 ? 45.42200  -6.44100  10.93400  1.000 33.35330  ? 279 ASP BA O   1 
ATOM   4262 C  CB  . ASP B 1 279 ? 47.27000  -4.72400  12.66400  1.000 42.60979  ? 279 ASP BA CB  1 
ATOM   4263 C  CG  . ASP B 1 279 ? 48.21800  -3.54800  12.77100  1.000 71.63065  ? 279 ASP BA CG  1 
ATOM   4264 O  OD1 . ASP B 1 279 ? 48.26400  -2.73200  11.82600  1.000 77.10857  ? 279 ASP BA OD1 1 
ATOM   4265 O  OD2 . ASP B 1 279 ? 48.91600  -3.43800  13.80100  1.000 69.52041  ? 279 ASP BA OD2 1 
ATOM   4266 N  N   . LEU B 1 280 ? 44.06900  -5.78100  12.60700  1.000 15.66682  ? 280 LEU BA N   1 
ATOM   4267 C  CA  . LEU B 1 280 ? 43.26000  -6.99000  12.57000  1.000 24.27181  ? 280 LEU BA CA  1 
ATOM   4268 C  C   . LEU B 1 280 ? 42.21300  -6.89800  11.46600  1.000 16.57948  ? 280 LEU BA C   1 
ATOM   4269 O  O   . LEU B 1 280 ? 41.48900  -5.90200  11.36500  1.000 14.41904  ? 280 LEU BA O   1 
ATOM   4270 C  CB  . LEU B 1 280 ? 42.58600  -7.21700  13.92200  1.000 26.49824  ? 280 LEU BA CB  1 
ATOM   4271 C  CG  . LEU B 1 280 ? 43.52400  -7.19600  15.13100  1.000 26.72443  ? 280 LEU BA CG  1 
ATOM   4272 C  CD1 . LEU B 1 280 ? 42.75400  -7.39900  16.42700  1.000 21.32054  ? 280 LEU BA CD1 1 
ATOM   4273 C  CD2 . LEU B 1 280 ? 44.60200  -8.25500  14.97500  1.000 24.54665  ? 280 LEU BA CD2 1 
ATOM   4274 N  N   . THR B 1 281 ? 42.15100  -7.93300  10.62800  1.000 21.45908  ? 281 THR BA N   1 
ATOM   4275 C  CA  . THR B 1 281 ? 41.13800  -8.06400  9.59000   1.000 24.05285  ? 281 THR BA CA  1 
ATOM   4276 C  C   . THR B 1 281 ? 40.58800  -9.48300  9.60600   1.000 20.33288  ? 281 THR BA C   1 
ATOM   4277 O  O   . THR B 1 281 ? 41.26700  -10.42400 10.02800  1.000 23.19453  ? 281 THR BA O   1 
ATOM   4278 C  CB  . THR B 1 281 ? 41.69000  -7.74600  8.18400   1.000 21.30345  ? 281 THR BA CB  1 
ATOM   4279 O  OG1 . THR B 1 281 ? 42.40200  -8.88100  7.67700   1.000 31.92770  ? 281 THR BA OG1 1 
ATOM   4280 C  CG2 . THR B 1 281 ? 42.61300  -6.53400  8.20800   1.000 34.46780  ? 281 THR BA CG2 1 
ATOM   4281 N  N   . ALA B 1 282 ? 39.35200  -9.62800  9.13900   1.000 20.62625  ? 282 ALA BA N   1 
ATOM   4282 C  CA  . ALA B 1 282 ? 38.67800  -10.91900 9.10700   1.000 12.46150  ? 282 ALA BA CA  1 
ATOM   4283 C  C   . ALA B 1 282 ? 37.49300  -10.81500 8.15800   1.000 17.26427  ? 282 ALA BA C   1 
ATOM   4284 O  O   . ALA B 1 282 ? 36.97800  -9.71500  7.92500   1.000 16.55473  ? 282 ALA BA O   1 
ATOM   4285 C  CB  . ALA B 1 282 ? 38.21600  -11.34100 10.51200  1.000 13.51810  ? 282 ALA BA CB  1 
ATOM   4286 N  N   . PRO B 1 283 ? 37.04500  -11.93600 7.58800   1.000 17.18801  ? 283 PRO BA N   1 
ATOM   4287 C  CA  . PRO B 1 283 ? 35.88800  -11.89000 6.68600   1.000 18.59310  ? 283 PRO BA CA  1 
ATOM   4288 C  C   . PRO B 1 283 ? 34.65200  -11.35200 7.39400   1.000 16.81760  ? 283 PRO BA C   1 
ATOM   4289 O  O   . PRO B 1 283 ? 34.44100  -11.58100 8.58700   1.000 12.67592  ? 283 PRO BA O   1 
ATOM   4290 C  CB  . PRO B 1 283 ? 35.70200  -13.35300 6.27000   1.000 12.47390  ? 283 PRO BA CB  1 
ATOM   4291 C  CG  . PRO B 1 283 ? 37.03500  -13.98200 6.48400   1.000 22.02473  ? 283 PRO BA CG  1 
ATOM   4292 C  CD  . PRO B 1 283 ? 37.62400  -13.28800 7.67300   1.000 12.62349  ? 283 PRO BA CD  1 
ATOM   4293 N  N   . VAL B 1 284 ? 33.82500  -10.62900 6.63500   1.000 13.08308  ? 284 VAL BA N   1 
ATOM   4294 C  CA  . VAL B 1 284 ? 32.68600  -9.94700  7.23900   1.000 14.84773  ? 284 VAL BA CA  1 
ATOM   4295 C  C   . VAL B 1 284 ? 31.59300  -10.92500 7.66200   1.000 16.62347  ? 284 VAL BA C   1 
ATOM   4296 O  O   . VAL B 1 284 ? 30.81000  -10.62000 8.57000   1.000 13.80802  ? 284 VAL BA O   1 
ATOM   4297 C  CB  . VAL B 1 284 ? 32.13800  -8.86400  6.28600   1.000 17.99357  ? 284 VAL BA CB  1 
ATOM   4298 C  CG1 . VAL B 1 284 ? 31.34300  -9.48100  5.14100   1.000 17.13072  ? 284 VAL BA CG1 1 
ATOM   4299 C  CG2 . VAL B 1 284 ? 31.29100  -7.85900  7.05400   1.000 11.27450  ? 284 VAL BA CG2 1 
ATOM   4300 N  N   A ASP B 1 285 ? 31.50700  -12.09000 7.01100   0.220 15.77136  ? 285 ASP BA N   1 
ATOM   4301 N  N   B ASP B 1 285 ? 31.52800  -12.11300 7.05400   0.780 15.86224  ? 285 ASP BA N   1 
ATOM   4302 C  CA  A ASP B 1 285 ? 30.54100  -13.10200 7.42700   0.220 13.87992  ? 285 ASP BA CA  1 
ATOM   4303 C  CA  B ASP B 1 285 ? 30.49200  -13.06600 7.44100   0.780 13.76813  ? 285 ASP BA CA  1 
ATOM   4304 C  C   A ASP B 1 285 ? 30.82000  -13.56200 8.84600   0.220 13.00068  ? 285 ASP BA C   1 
ATOM   4305 C  C   B ASP B 1 285 ? 30.79600  -13.74500 8.77300   0.780 12.49689  ? 285 ASP BA C   1 
ATOM   4306 O  O   A ASP B 1 285 ? 29.91700  -13.61500 9.68800   0.220 14.35351  ? 285 ASP BA O   1 
ATOM   4307 O  O   B ASP B 1 285 ? 29.86400  -14.12000 9.49200   0.780 15.28498  ? 285 ASP BA O   1 
ATOM   4308 C  CB  A ASP B 1 285 ? 30.58700  -14.30200 6.48800   0.220 16.42103  ? 285 ASP BA CB  1 
ATOM   4309 C  CB  B ASP B 1 285 ? 30.28700  -14.11500 6.34400   0.780 15.71192  ? 285 ASP BA CB  1 
ATOM   4310 C  CG  A ASP B 1 285 ? 30.32500  -13.93200 5.06300   0.220 13.50556  ? 285 ASP BA CG  1 
ATOM   4311 C  CG  B ASP B 1 285 ? 31.58300  -14.54800 5.69200   0.780 12.11306  ? 285 ASP BA CG  1 
ATOM   4312 O  OD1 A ASP B 1 285 ? 29.82500  -12.81500 4.81900   0.220 19.56119  ? 285 ASP BA OD1 1 
ATOM   4313 O  OD1 B ASP B 1 285 ? 32.66100  -14.27100 6.25700   0.780 16.71739  ? 285 ASP BA OD1 1 
ATOM   4314 O  OD2 A ASP B 1 285 ? 30.61900  -14.77000 4.18900   0.220 14.26154  ? 285 ASP BA OD2 1 
ATOM   4315 O  OD2 B ASP B 1 285 ? 31.52000  -15.17600 4.61500   0.780 15.23074  ? 285 ASP BA OD2 1 
ATOM   4316 N  N   . LEU B 1 286 ? 32.07600  -13.91400 9.12000   1.000 16.79356  ? 286 LEU BA N   1 
ATOM   4317 C  CA  . LEU B 1 286 ? 32.42800  -14.44400 10.43200  1.000 19.72452  ? 286 LEU BA CA  1 
ATOM   4318 C  C   . LEU B 1 286 ? 32.18700  -13.40600 11.52000  1.000 17.30870  ? 286 LEU BA C   1 
ATOM   4319 O  O   . LEU B 1 286 ? 31.60900  -13.71200 12.56900  1.000 17.51554  ? 286 LEU BA O   1 
ATOM   4320 C  CB  . LEU B 1 286 ? 33.88600  -14.90600 10.43000  1.000 12.60916  ? 286 LEU BA CB  1 
ATOM   4321 C  CG  . LEU B 1 286 ? 34.44900  -15.42400 11.75300  1.000 25.00334  ? 286 LEU BA CG  1 
ATOM   4322 C  CD1 . LEU B 1 286 ? 33.63000  -16.60100 12.25900  1.000 19.64342  ? 286 LEU BA CD1 1 
ATOM   4323 C  CD2 . LEU B 1 286 ? 35.91100  -15.81200 11.58900  1.000 22.77426  ? 286 LEU BA CD2 1 
ATOM   4324 N  N   . LEU B 1 287 ? 32.61800  -12.16400 11.27900  1.000 12.31641  ? 287 LEU BA N   1 
ATOM   4325 C  CA  . LEU B 1 287 ? 32.35200  -11.09000 12.23000  1.000 17.06494  ? 287 LEU BA CA  1 
ATOM   4326 C  C   . LEU B 1 287 ? 30.85600  -10.87600 12.41100  1.000 12.49466  ? 287 LEU BA C   1 
ATOM   4327 O  O   . LEU B 1 287 ? 30.38400  -10.64700 13.53200  1.000 12.66170  ? 287 LEU BA O   1 
ATOM   4328 C  CB  . LEU B 1 287 ? 33.02200  -9.79700  11.76500  1.000 13.43986  ? 287 LEU BA CB  1 
ATOM   4329 C  CG  . LEU B 1 287 ? 34.54800  -9.79800  11.66500  1.000 19.29007  ? 287 LEU BA CG  1 
ATOM   4330 C  CD1 . LEU B 1 287 ? 35.04000  -8.48700  11.07300  1.000 14.81216  ? 287 LEU BA CD1 1 
ATOM   4331 C  CD2 . LEU B 1 287 ? 35.18200  -10.05100 13.02600  1.000 9.15619   ? 287 LEU BA CD2 1 
ATOM   4332 N  N   . GLY B 1 288 ? 30.09300  -10.94900 11.31700  1.000 9.01896   ? 288 GLY BA N   1 
ATOM   4333 C  CA  . GLY B 1 288 ? 28.65000  -10.80800 11.42200  1.000 7.87505   ? 288 GLY BA CA  1 
ATOM   4334 C  C   . GLY B 1 288 ? 28.01000  -11.93300 12.21100  1.000 8.55641   ? 288 GLY BA C   1 
ATOM   4335 O  O   . GLY B 1 288 ? 27.07300  -11.70900 12.98100  1.000 11.00109  ? 288 GLY BA O   1 
ATOM   4336 N  N   . THR B 1 289 ? 28.50300  -13.16100 12.02800  1.000 7.15654   ? 289 THR BA N   1 
ATOM   4337 C  CA  . THR B 1 289 ? 28.01300  -14.27700 12.83000  1.000 11.78808  ? 289 THR BA CA  1 
ATOM   4338 C  C   . THR B 1 289 ? 28.42000  -14.12100 14.29000  1.000 10.76976  ? 289 THR BA C   1 
ATOM   4339 O  O   . THR B 1 289 ? 27.63400  -14.42300 15.19600  1.000 12.45825  ? 289 THR BA O   1 
ATOM   4340 C  CB  . THR B 1 289 ? 28.53000  -15.60200 12.26800  1.000 10.13548  ? 289 THR BA CB  1 
ATOM   4341 O  OG1 . THR B 1 289 ? 28.36000  -15.62100 10.84600  1.000 7.56670   ? 289 THR BA OG1 1 
ATOM   4342 C  CG2 . THR B 1 289 ? 27.76800  -16.77000 12.87300  1.000 9.28031   ? 289 THR BA CG2 1 
ATOM   4343 N  N   . ALA B 1 290 ? 29.64400  -13.64500 14.53600  1.000 6.19196   ? 290 ALA BA N   1 
ATOM   4344 C  CA  . ALA B 1 290 ? 30.07700  -13.39300 15.90600  1.000 8.87011   ? 290 ALA BA CA  1 
ATOM   4345 C  C   . ALA B 1 290 ? 29.29300  -12.24600 16.53000  1.000 14.38657  ? 290 ALA BA C   1 
ATOM   4346 O  O   . ALA B 1 290 ? 29.01000  -12.26200 17.73400  1.000 11.31379  ? 290 ALA BA O   1 
ATOM   4347 C  CB  . ALA B 1 290 ? 31.57600  -13.10100 15.93800  1.000 13.16068  ? 290 ALA BA CB  1 
ATOM   4348 N  N   . ALA B 1 291 ? 28.93700  -11.23800 15.72900  1.000 7.50839   ? 291 ALA BA N   1 
ATOM   4349 C  CA  . ALA B 1 291 ? 28.10100  -10.15500 16.23500  1.000 7.11473   ? 291 ALA BA CA  1 
ATOM   4350 C  C   . ALA B 1 291 ? 26.72300  -10.66600 16.63000  1.000 12.63445  ? 291 ALA BA C   1 
ATOM   4351 O  O   . ALA B 1 291 ? 26.14500  -10.21000 17.62400  1.000 5.84771   ? 291 ALA BA O   1 
ATOM   4352 C  CB  . ALA B 1 291 ? 27.98400  -9.04700  15.18800  1.000 10.20110  ? 291 ALA BA CB  1 
ATOM   4353 N  N   . ALA B 1 292 ? 26.18100  -11.61700 15.86400  1.000 5.62607   ? 292 ALA BA N   1 
ATOM   4354 C  CA  . ALA B 1 292 ? 24.88000  -12.18600 16.19900  1.000 8.59118   ? 292 ALA BA CA  1 
ATOM   4355 C  C   . ALA B 1 292 ? 24.93200  -12.93800 17.52300  1.000 13.07643  ? 292 ALA BA C   1 
ATOM   4356 O  O   . ALA B 1 292 ? 24.01500  -12.82700 18.34500  1.000 9.56468   ? 292 ALA BA O   1 
ATOM   4357 C  CB  . ALA B 1 292 ? 24.40300  -13.10300 15.07400  1.000 3.69328   ? 292 ALA BA CB  1 
ATOM   4358 N  N   . GLU B 1 293 ? 26.00000  -13.70800 17.75100  1.000 10.25324  ? 293 GLU BA N   1 
ATOM   4359 C  CA  . GLU B 1 293 ? 26.14600  -14.40000 19.02700  1.000 12.79649  ? 293 GLU BA CA  1 
ATOM   4360 C  C   . GLU B 1 293 ? 26.29900  -13.40500 20.17000  1.000 7.72850   ? 293 GLU BA C   1 
ATOM   4361 O  O   . GLU B 1 293 ? 25.64000  -13.53000 21.20900  1.000 11.79804  ? 293 GLU BA O   1 
ATOM   4362 C  CB  . GLU B 1 293 ? 27.34100  -15.35500 18.98400  1.000 10.52371  ? 293 GLU BA CB  1 
ATOM   4363 C  CG  . GLU B 1 293 ? 27.44500  -16.24300 20.21500  1.000 10.56644  ? 293 GLU BA CG  1 
ATOM   4364 C  CD  . GLU B 1 293 ? 28.73700  -17.03800 20.27100  1.000 17.97290  ? 293 GLU BA CD  1 
ATOM   4365 O  OE1 . GLU B 1 293 ? 29.64800  -16.76800 19.46100  1.000 14.12190  ? 293 GLU BA OE1 1 
ATOM   4366 O  OE2 . GLU B 1 293 ? 28.84200  -17.93600 21.13300  1.000 26.57084  ? 293 GLU BA OE2 1 
ATOM   4367 N  N   . ALA B 1 294 ? 27.16400  -12.40300 19.99000  1.000 8.11927   ? 294 ALA BA N   1 
ATOM   4368 C  CA  . ALA B 1 294 ? 27.36300  -11.39600 21.02800  1.000 14.12874  ? 294 ALA BA CA  1 
ATOM   4369 C  C   . ALA B 1 294 ? 26.06200  -10.67700 21.35500  1.000 9.90558   ? 294 ALA BA C   1 
ATOM   4370 O  O   . ALA B 1 294 ? 25.76300  -10.42200 22.52800  1.000 11.81169  ? 294 ALA BA O   1 
ATOM   4371 C  CB  . ALA B 1 294 ? 28.43400  -10.39600 20.59300  1.000 11.37219  ? 294 ALA BA CB  1 
ATOM   4372 N  N   . ALA B 1 295 ? 25.26900  -10.35200 20.33200  1.000 6.20691   ? 295 ALA BA N   1 
ATOM   4373 C  CA  . ALA B 1 295 ? 23.98900  -9.69500  20.57200  1.000 7.94826   ? 295 ALA BA CA  1 
ATOM   4374 C  C   . ALA B 1 295 ? 23.01900  -10.62200 21.29300  1.000 10.47386  ? 295 ALA BA C   1 
ATOM   4375 O  O   . ALA B 1 295 ? 22.26000  -10.17900 22.16300  1.000 11.48881  ? 295 ALA BA O   1 
ATOM   4376 C  CB  . ALA B 1 295 ? 23.39100  -9.21100  19.25100  1.000 7.80783   ? 295 ALA BA CB  1 
ATOM   4377 N  N   . MET B 1 296 ? 23.02600  -11.91100 20.94300  1.000 14.12518  ? 296 MET BA N   1 
ATOM   4378 C  CA  . MET B 1 296 ? 22.13700  -12.86100 21.60500  1.000 10.79044  ? 296 MET BA CA  1 
ATOM   4379 C  C   . MET B 1 296 ? 22.52200  -13.04800 23.06800  1.000 10.68766  ? 296 MET BA C   1 
ATOM   4380 O  O   . MET B 1 296 ? 21.65200  -13.08700 23.94500  1.000 18.30361  ? 296 MET BA O   1 
ATOM   4381 C  CB  . MET B 1 296 ? 22.15500  -14.19800 20.86200  1.000 9.45831   ? 296 MET BA CB  1 
ATOM   4382 C  CG  . MET B 1 296 ? 21.58400  -15.36600 21.65200  1.000 23.36450  ? 296 MET BA CG  1 
ATOM   4383 S  SD  . MET B 1 296 ? 21.72200  -16.93400 20.76800  1.000 37.56830  ? 296 MET BA SD  1 
ATOM   4384 C  CE  . MET B 1 296 ? 23.33600  -17.49500 21.30900  1.000 21.88094  ? 296 MET BA CE  1 
ATOM   4385 N  N   . LEU B 1 297 ? 23.82200  -13.15800 23.35000  1.000 11.17704  ? 297 LEU BA N   1 
ATOM   4386 C  CA  . LEU B 1 297 ? 24.26900  -13.30400 24.73200  1.000 10.31129  ? 297 LEU BA CA  1 
ATOM   4387 C  C   . LEU B 1 297 ? 23.99000  -12.04200 25.54000  1.000 11.40260  ? 297 LEU BA C   1 
ATOM   4388 O  O   . LEU B 1 297 ? 23.65600  -12.12200 26.72800  1.000 9.67409   ? 297 LEU BA O   1 
ATOM   4389 C  CB  . LEU B 1 297 ? 25.75800  -13.64600 24.76500  1.000 7.57159   ? 297 LEU BA CB  1 
ATOM   4390 C  CG  . LEU B 1 297 ? 26.14600  -14.98700 24.14200  1.000 11.74164  ? 297 LEU BA CG  1 
ATOM   4391 C  CD1 . LEU B 1 297 ? 27.65900  -15.13300 24.07400  1.000 8.02347   ? 297 LEU BA CD1 1 
ATOM   4392 C  CD2 . LEU B 1 297 ? 25.52600  -16.13300 24.92700  1.000 8.62637   ? 297 LEU BA CD2 1 
ATOM   4393 N  N   . ALA B 1 298 ? 24.11800  -10.86900 24.91200  1.000 9.94473   ? 298 ALA BA N   1 
ATOM   4394 C  CA  . ALA B 1 298 ? 23.85400  -9.62100  25.62000  1.000 9.84903   ? 298 ALA BA CA  1 
ATOM   4395 C  C   . ALA B 1 298 ? 22.37500  -9.45600  25.94400  1.000 17.66629  ? 298 ALA BA C   1 
ATOM   4396 O  O   . ALA B 1 298 ? 22.03000  -8.79800  26.93300  1.000 11.36136  ? 298 ALA BA O   1 
ATOM   4397 C  CB  . ALA B 1 298 ? 24.35200  -8.43400  24.79700  1.000 5.25586   ? 298 ALA BA CB  1 
ATOM   4398 N  N   . CYS B 1 299 ? 21.49100  -10.03500 25.12700  1.000 9.36643   ? 299 CYS BA N   1 
ATOM   4399 C  CA  . CYS B 1 299 ? 20.06200  -9.97600  25.42000  1.000 9.70856   ? 299 CYS BA CA  1 
ATOM   4400 C  C   . CYS B 1 299 ? 19.74200  -10.71700 26.71300  1.000 18.05063  ? 299 CYS BA C   1 
ATOM   4401 O  O   . CYS B 1 299 ? 19.01700  -10.20500 27.57400  1.000 13.83890  ? 299 CYS BA O   1 
ATOM   4402 C  CB  . CYS B 1 299 ? 19.26400  -10.55800 24.25200  1.000 13.64199  ? 299 CYS BA CB  1 
ATOM   4403 S  SG  . CYS B 1 299 ? 19.07700  -9.44700  22.83700  1.000 15.74293  ? 299 CYS BA SG  1 
ATOM   4404 N  N   . LEU B 1 300 ? 20.28300  -11.92900 26.86700  1.000 19.33078  ? 300 LEU BA N   1 
ATOM   4405 C  CA  . LEU B 1 300 ? 20.07200  -12.68800 28.09600  1.000 12.68595  ? 300 LEU BA CA  1 
ATOM   4406 C  C   . LEU B 1 300 ? 20.73800  -12.01100 29.28600  1.000 17.86178  ? 300 LEU BA C   1 
ATOM   4407 O  O   . LEU B 1 300 ? 20.20600  -12.04300 30.40200  1.000 21.03443  ? 300 LEU BA O   1 
ATOM   4408 C  CB  . LEU B 1 300 ? 20.59900  -14.11400 27.93200  1.000 14.62843  ? 300 LEU BA CB  1 
ATOM   4409 C  CG  . LEU B 1 300 ? 19.94600  -14.98300 26.85500  1.000 18.97838  ? 300 LEU BA CG  1 
ATOM   4410 C  CD1 . LEU B 1 300 ? 20.75700  -16.25000 26.63400  1.000 16.97327  ? 300 LEU BA CD1 1 
ATOM   4411 C  CD2 . LEU B 1 300 ? 18.51400  -15.32100 27.23300  1.000 17.06462  ? 300 LEU BA CD2 1 
ATOM   4412 N  N   . ASP B 1 301 ? 21.90400  -11.39700 29.06900  1.000 10.87515  ? 301 ASP BA N   1 
ATOM   4413 C  CA  . ASP B 1 301 ? 22.58300  -10.69000 30.15000  1.000 17.43973  ? 301 ASP BA CA  1 
ATOM   4414 C  C   . ASP B 1 301 ? 21.73400  -9.55100  30.69700  1.000 13.40641  ? 301 ASP BA C   1 
ATOM   4415 O  O   . ASP B 1 301 ? 21.84900  -9.20200  31.87700  1.000 13.93359  ? 301 ASP BA O   1 
ATOM   4416 C  CB  . ASP B 1 301 ? 23.93000  -10.15600 29.66000  1.000 11.94720  ? 301 ASP BA CB  1 
ATOM   4417 C  CG  . ASP B 1 301 ? 24.75100  -9.53500  30.77400  1.000 14.11352  ? 301 ASP BA CG  1 
ATOM   4418 O  OD1 . ASP B 1 301 ? 25.21900  -10.28500 31.65500  1.000 23.70376  ? 301 ASP BA OD1 1 
ATOM   4419 O  OD2 . ASP B 1 301 ? 24.92900  -8.29900  30.76900  1.000 11.37044  ? 301 ASP BA OD2 1 
ATOM   4420 N  N   . ALA B 1 302 ? 20.86600  -8.97300  29.86300  1.000 14.91421  ? 302 ALA BA N   1 
ATOM   4421 C  CA  . ALA B 1 302 ? 20.08400  -7.81700  30.28400  1.000 11.80644  ? 302 ALA BA CA  1 
ATOM   4422 C  C   . ALA B 1 302 ? 19.04000  -8.17800  31.33400  1.000 16.72389  ? 302 ALA BA C   1 
ATOM   4423 O  O   . ALA B 1 302 ? 18.65300  -7.32100  32.13600  1.000 19.11895  ? 302 ALA BA O   1 
ATOM   4424 C  CB  . ALA B 1 302 ? 19.41200  -7.17200  29.07300  1.000 9.74674   ? 302 ALA BA CB  1 
ATOM   4425 N  N   . VAL B 1 303 ? 18.57300  -9.42600  31.34900  1.000 19.81037  ? 303 VAL BA N   1 
ATOM   4426 C  CA  . VAL B 1 303 ? 17.51200  -9.84300  32.26300  1.000 15.77762  ? 303 VAL BA CA  1 
ATOM   4427 C  C   . VAL B 1 303 ? 18.02300  -10.67700 33.42700  1.000 24.99171  ? 303 VAL BA C   1 
ATOM   4428 O  O   . VAL B 1 303 ? 17.26500  -10.89700 34.38600  1.000 25.11785  ? 303 VAL BA O   1 
ATOM   4429 C  CB  . VAL B 1 303 ? 16.39400  -10.60700 31.52300  1.000 19.29134  ? 303 VAL BA CB  1 
ATOM   4430 C  CG1 . VAL B 1 303 ? 15.64300  -9.67200  30.58800  1.000 17.60570  ? 303 VAL BA CG1 1 
ATOM   4431 C  CG2 . VAL B 1 303 ? 16.96800  -11.79100 30.76100  1.000 30.17684  ? 303 VAL BA CG2 1 
ATOM   4432 N  N   . MET B 1 304 ? 19.26600  -11.15000 33.38300  1.000 28.56880  ? 304 MET BA N   1 
ATOM   4433 C  CA  . MET B 1 304 ? 19.85000  -11.89700 34.48900  1.000 36.99637  ? 304 MET BA CA  1 
ATOM   4434 C  C   . MET B 1 304 ? 20.76800  -11.04700 35.35600  1.000 39.16970  ? 304 MET BA C   1 
ATOM   4435 O  O   . MET B 1 304 ? 21.35700  -11.56900 36.30700  1.000 42.02450  ? 304 MET BA O   1 
ATOM   4436 C  CB  . MET B 1 304 ? 20.61800  -13.11400 33.96100  1.000 27.55297  ? 304 MET BA CB  1 
ATOM   4437 C  CG  . MET B 1 304 ? 19.73300  -14.18000 33.33000  1.000 40.26663  ? 304 MET BA CG  1 
ATOM   4438 S  SD  . MET B 1 304 ? 20.44000  -14.88700 31.83000  1.000 64.76922  ? 304 MET BA SD  1 
ATOM   4439 C  CE  . MET B 1 304 ? 19.62200  -16.48000 31.78800  1.000 40.40194  ? 304 MET BA CE  1 
ATOM   4440 N  N   . GLN B 1 305 ? 20.90000  -9.75900  35.05600  1.000 56.43912  ? 305 GLN BA N   1 
ATOM   4441 C  CA  . GLN B 1 305 ? 21.76700  -8.87200  35.82200  1.000 52.89811  ? 305 GLN BA CA  1 
ATOM   4442 C  C   . GLN B 1 305 ? 20.94000  -7.91700  36.67600  1.000 47.91271  ? 305 GLN BA C   1 
ATOM   4443 O  O   . GLN B 1 305 ? 19.88000  -7.45600  36.25400  1.000 45.29495  ? 305 GLN BA O   1 
ATOM   4444 C  CB  . GLN B 1 305 ? 22.68800  -8.08300  34.88700  1.000 35.82722  ? 305 GLN BA CB  1 
ATOM   4445 C  CG  . GLN B 1 305 ? 23.98200  -8.80000  34.53200  1.000 30.87726  ? 305 GLN BA CG  1 
ATOM   4446 C  CD  . GLN B 1 305 ? 24.80000  -9.17300  35.75400  1.000 67.43683  ? 305 GLN BA CD  1 
ATOM   4447 O  OE1 . GLN B 1 305 ? 24.84500  -10.33700 36.15500  1.000 51.74266  ? 305 GLN BA OE1 1 
ATOM   4448 N  NE2 . GLN B 1 305 ? 25.45600  -8.18400  36.35200  1.000 64.03770  ? 305 GLN BA NE2 1 
HETATM 4449 C  C1  . EDO C 2 .   ? 3.39700   8.90200   15.82700  0.652 20.66568  ? 401 EDO AA C1  1 
HETATM 4450 O  O1  . EDO C 2 .   ? 3.17700   10.27000  16.19200  0.652 23.02152  ? 401 EDO AA O1  1 
HETATM 4451 C  C2  . EDO C 2 .   ? 4.81400   8.49800   16.21300  0.652 27.59967  ? 401 EDO AA C2  1 
HETATM 4452 O  O2  . EDO C 2 .   ? 5.01700   8.77300   17.60300  0.652 25.89859  ? 401 EDO AA O2  1 
HETATM 4453 NA NA  . NA  D 3 .   ? 24.80000  22.16500  3.32000   1.000 15.85186  ? 402 NA  AA NA  1 
HETATM 4454 NA NA  . NA  E 3 .   ? 24.99300  31.36900  10.30100  1.000 15.63941  ? 403 NA  AA NA  1 
HETATM 4455 C  C1  . PGE F 4 .   ? 7.18200   -0.54100  24.74400  0.762 18.32778  ? 401 PGE BA C1  1 
HETATM 4456 O  O1  . PGE F 4 .   ? 7.22200   -0.55700  26.16300  0.762 25.16208  ? 401 PGE BA O1  1 
HETATM 4457 C  C2  . PGE F 4 .   ? 5.77800   -0.88600  24.29700  0.762 34.04568  ? 401 PGE BA C2  1 
HETATM 4458 O  O2  . PGE F 4 .   ? 4.86400   -0.21400  25.13800  0.762 50.40200  ? 401 PGE BA O2  1 
HETATM 4459 C  C3  . PGE F 4 .   ? 3.72600   -0.98700  25.45300  0.762 27.55100  ? 401 PGE BA C3  1 
HETATM 4460 C  C4  . PGE F 4 .   ? 3.22000   -0.59400  26.82600  0.762 30.21225  ? 401 PGE BA C4  1 
HETATM 4461 O  O4  . PGE F 4 .   ? -0.83700  -0.62500  29.29200  0.762 46.48279  ? 401 PGE BA O4  1 
HETATM 4462 C  C6  . PGE F 4 .   ? -0.21200  -0.98600  28.06700  0.762 28.62268  ? 401 PGE BA C6  1 
HETATM 4463 C  C5  . PGE F 4 .   ? 1.25800   -0.63000  28.14400  0.762 29.67562  ? 401 PGE BA C5  1 
HETATM 4464 O  O3  . PGE F 4 .   ? 1.91200   -1.10700  26.98600  0.762 34.30082  ? 401 PGE BA O3  1 
HETATM 4465 NA NA  . NA  G 3 .   ? 9.53600   0.38000   22.35700  1.000 15.04633  ? 402 NA  BA NA  1 
HETATM 4466 NA NA  . NA  H 3 .   ? 9.44400   6.05800   32.45800  1.000 19.53155  ? 403 NA  BA NA  1 
HETATM 4467 O  O   . HOH I 5 .   ? 10.73900  35.39600  12.10300  1.000 45.30885  ? 501 HOH AA O   1 
HETATM 4468 O  O   . HOH I 5 .   ? 16.05100  10.17200  10.68000  1.000 13.41197  ? 502 HOH AA O   1 
HETATM 4469 O  O   . HOH I 5 .   ? 34.07700  28.48300  6.08000   1.000 37.09671  ? 503 HOH AA O   1 
HETATM 4470 O  O   . HOH I 5 .   ? 29.99900  25.77300  -6.92700  1.000 13.11868  ? 504 HOH AA O   1 
HETATM 4471 O  O   . HOH I 5 .   ? 17.53000  5.39700   8.89100   1.000 21.16998  ? 505 HOH AA O   1 
HETATM 4472 O  O   . HOH I 5 .   ? 17.72000  8.04100   -1.99800  1.000 17.59069  ? 506 HOH AA O   1 
HETATM 4473 O  O   . HOH I 5 .   ? 14.55800  39.91200  -5.58100  1.000 44.60057  ? 507 HOH AA O   1 
HETATM 4474 O  O   . HOH I 5 .   ? 13.27900  29.71700  -16.20200 1.000 30.06985  ? 508 HOH AA O   1 
HETATM 4475 O  O   . HOH I 5 .   ? -1.39200  8.25900   -6.70000  1.000 30.85725  ? 509 HOH AA O   1 
HETATM 4476 O  O   . HOH I 5 .   ? 39.23200  25.22000  -6.42800  1.000 35.99675  ? 510 HOH AA O   1 
HETATM 4477 O  O   . HOH I 5 .   ? 13.68600  7.43700   12.71600  1.000 11.71891  ? 511 HOH AA O   1 
HETATM 4478 O  O   . HOH I 5 .   ? 5.04500   35.46900  -0.38200  1.000 23.35073  ? 512 HOH AA O   1 
HETATM 4479 O  O   . HOH I 5 .   ? -0.69800  18.96700  13.29700  1.000 27.81250  ? 513 HOH AA O   1 
HETATM 4480 O  O   . HOH I 5 .   ? -7.29900  11.32600  -11.74300 1.000 26.04777  ? 514 HOH AA O   1 
HETATM 4481 O  O   . HOH I 5 .   ? 16.61400  7.83400   6.42700   1.000 20.26354  ? 515 HOH AA O   1 
HETATM 4482 O  O   . HOH I 5 .   ? 25.48100  37.31800  -6.78400  1.000 34.54247  ? 516 HOH AA O   1 
HETATM 4483 O  O   . HOH I 5 .   ? 6.99600   5.81800   -10.93400 1.000 14.27372  ? 517 HOH AA O   1 
HETATM 4484 O  O   . HOH I 5 .   ? 37.76200  18.83300  -10.25400 1.000 24.76918  ? 518 HOH AA O   1 
HETATM 4485 O  O   . HOH I 5 .   ? 18.76500  33.60500  17.57800  1.000 32.97894  ? 519 HOH AA O   1 
HETATM 4486 O  O   . HOH I 5 .   ? 21.20500  34.74400  -5.63100  1.000 24.26330  ? 520 HOH AA O   1 
HETATM 4487 O  O   . HOH I 5 .   ? 10.91000  5.80400   -3.18300  1.000 29.93245  ? 521 HOH AA O   1 
HETATM 4488 O  O   . HOH I 5 .   ? 8.27000   31.42500  22.41800  1.000 31.40189  ? 522 HOH AA O   1 
HETATM 4489 O  O   . HOH I 5 .   ? 19.70800  29.33400  7.38600   1.000 14.62612  ? 523 HOH AA O   1 
HETATM 4490 O  O   . HOH I 5 .   ? 2.318     27.037    27.029    1.000 40.12725  ? 524 HOH AA O   1 
HETATM 4491 O  O   . HOH I 5 .   ? 1.09200   11.27800  9.42200   1.000 22.38746  ? 525 HOH AA O   1 
HETATM 4492 O  O   . HOH I 5 .   ? -3.66600  28.86900  3.78900   1.000 23.65160  ? 526 HOH AA O   1 
HETATM 4493 O  O   . HOH I 5 .   ? 6.44200   6.37400   2.53000   1.000 12.16068  ? 527 HOH AA O   1 
HETATM 4494 O  O   . HOH I 5 .   ? 17.049    11.923    -10.072   1.000 29.14885  ? 528 HOH AA O   1 
HETATM 4495 O  O   . HOH I 5 .   ? 1.66300   14.51200  27.10200  1.000 27.80316  ? 529 HOH AA O   1 
HETATM 4496 O  O   . HOH I 5 .   ? 19.760    10.437    -8.754    1.000 24.86956  ? 530 HOH AA O   1 
HETATM 4497 O  O   . HOH I 5 .   ? 30.52800  32.42700  10.47600  1.000 17.92954  ? 531 HOH AA O   1 
HETATM 4498 O  O   . HOH I 5 .   ? 32.55700  29.64200  -4.38900  1.000 13.37558  ? 532 HOH AA O   1 
HETATM 4499 O  O   . HOH I 5 .   ? 0.45900   14.69200  15.11400  1.000 25.62916  ? 533 HOH AA O   1 
HETATM 4500 O  O   . HOH I 5 .   ? 25.39400  28.79200  3.68200   1.000 10.78532  ? 534 HOH AA O   1 
HETATM 4501 O  O   . HOH I 5 .   ? 26.13300  21.62600  1.08400   1.000 34.02482  ? 535 HOH AA O   1 
HETATM 4502 O  O   . HOH I 5 .   ? -3.70700  26.29200  4.50400   1.000 31.33303  ? 536 HOH AA O   1 
HETATM 4503 O  O   . HOH I 5 .   ? 23.85100  28.72200  12.20200  1.000 32.76579  ? 537 HOH AA O   1 
HETATM 4504 O  O   . HOH I 5 .   ? 10.96500  35.78500  9.71500   1.000 28.38700  ? 538 HOH AA O   1 
HETATM 4505 O  O   . HOH I 5 .   ? 25.73800  15.55800  -9.89400  1.000 11.99323  ? 539 HOH AA O   1 
HETATM 4506 O  O   . HOH I 5 .   ? -6.52400  14.08000  5.78200   1.000 24.11408  ? 540 HOH AA O   1 
HETATM 4507 O  O   . HOH I 5 .   ? 29.01800  29.46200  -11.72700 1.000 12.89018  ? 541 HOH AA O   1 
HETATM 4508 O  O   . HOH I 5 .   ? 19.70900  30.38100  18.50200  1.000 34.11742  ? 542 HOH AA O   1 
HETATM 4509 O  O   . HOH I 5 .   ? 30.90700  27.80500  -19.12200 1.000 31.70337  ? 543 HOH AA O   1 
HETATM 4510 O  O   . HOH I 5 .   ? 8.68600   12.03400  -14.22300 1.000 19.38147  ? 544 HOH AA O   1 
HETATM 4511 O  O   . HOH I 5 .   ? 27.71900  24.25600  -13.07100 1.000 14.34886  ? 545 HOH AA O   1 
HETATM 4512 O  O   . HOH I 5 .   ? 32.421    31.483    -17.211   1.000 17.27496  ? 546 HOH AA O   1 
HETATM 4513 O  O   . HOH I 5 .   ? 4.11400   32.58000  7.47500   1.000 23.30210  ? 547 HOH AA O   1 
HETATM 4514 O  O   . HOH I 5 .   ? 25.04300  27.70800  -18.73100 1.000 25.89202  ? 548 HOH AA O   1 
HETATM 4515 O  O   . HOH I 5 .   ? -0.48100  16.91500  1.56300   1.000 13.50501  ? 549 HOH AA O   1 
HETATM 4516 O  O   . HOH I 5 .   ? 23.44500  11.27100  3.43600   1.000 7.93569   ? 550 HOH AA O   1 
HETATM 4517 O  O   . HOH I 5 .   ? 4.84600   16.48200  29.37200  1.000 40.45143  ? 551 HOH AA O   1 
HETATM 4518 O  O   . HOH I 5 .   ? -0.50600  34.82300  5.78400   1.000 29.84785  ? 552 HOH AA O   1 
HETATM 4519 O  O   . HOH I 5 .   ? 37.34700  27.23500  2.22000   1.000 36.73505  ? 553 HOH AA O   1 
HETATM 4520 O  O   . HOH I 5 .   ? -0.64400  5.67500   -8.45800  1.000 29.48882  ? 554 HOH AA O   1 
HETATM 4521 O  O   . HOH I 5 .   ? 24.47400  20.94400  -5.20200  1.000 6.90664   ? 555 HOH AA O   1 
HETATM 4522 O  O   . HOH I 5 .   ? 17.62300  35.17100  -2.13200  1.000 38.62099  ? 556 HOH AA O   1 
HETATM 4523 O  O   . HOH I 5 .   ? 22.12600  22.12600  19.18300  1.000 15.41528  ? 557 HOH AA O   1 
HETATM 4524 O  O   . HOH I 5 .   ? -3.74700  9.90100   -5.77900  1.000 13.41458  ? 558 HOH AA O   1 
HETATM 4525 O  O   . HOH I 5 .   ? 20.44100  17.43700  5.28300   1.000 12.82311  ? 559 HOH AA O   1 
HETATM 4526 O  O   . HOH I 5 .   ? 12.60300  6.90500   -0.84800  1.000 30.68169  ? 560 HOH AA O   1 
HETATM 4527 O  O   . HOH I 5 .   ? 10.35900  13.31000  -12.53200 1.000 17.16677  ? 561 HOH AA O   1 
HETATM 4528 O  O   . HOH I 5 .   ? 21.22500  24.62900  18.70000  1.000 20.83182  ? 562 HOH AA O   1 
HETATM 4529 O  O   . HOH I 5 .   ? 22.15100  20.77900  -3.28000  1.000 8.81013   ? 563 HOH AA O   1 
HETATM 4530 O  O   . HOH I 5 .   ? 44.000    19.996    -15.043   1.000 14.33196  ? 564 HOH AA O   1 
HETATM 4531 O  O   . HOH I 5 .   ? -2.06900  29.96600  0.19600   1.000 25.41352  ? 565 HOH AA O   1 
HETATM 4532 O  O   . HOH I 5 .   ? 3.40900   30.18700  -5.59600  1.000 17.49448  ? 566 HOH AA O   1 
HETATM 4533 O  O   . HOH I 5 .   ? -6.15600  22.49600  -9.91800  1.000 22.56511  ? 567 HOH AA O   1 
HETATM 4534 O  O   . HOH I 5 .   ? 1.97300   31.39400  5.79500   1.000 19.84740  ? 568 HOH AA O   1 
HETATM 4535 O  O   . HOH I 5 .   ? 15.85400  7.66100   1.56500   1.000 19.21838  ? 569 HOH AA O   1 
HETATM 4536 O  O   . HOH I 5 .   ? 35.13900  31.39500  1.37700   1.000 30.64245  ? 570 HOH AA O   1 
HETATM 4537 O  O   . HOH I 5 .   ? 28.19900  35.90600  -14.88200 1.000 16.25398  ? 571 HOH AA O   1 
HETATM 4538 O  O   . HOH I 5 .   ? 14.18800  10.06700  -9.60700  1.000 30.87572  ? 572 HOH AA O   1 
HETATM 4539 O  O   . HOH I 5 .   ? 5.85700   34.53600  6.41500   1.000 16.97145  ? 573 HOH AA O   1 
HETATM 4540 O  O   . HOH I 5 .   ? 5.91200   33.01800  9.82500   1.000 25.67899  ? 574 HOH AA O   1 
HETATM 4541 O  O   . HOH I 5 .   ? -0.67400  14.14300  9.87000   1.000 23.42226  ? 575 HOH AA O   1 
HETATM 4542 O  O   . HOH I 5 .   ? -0.13000  25.44700  -12.90900 1.000 27.88882  ? 576 HOH AA O   1 
HETATM 4543 O  O   . HOH I 5 .   ? 15.44500  25.50300  -14.40800 1.000 24.85536  ? 577 HOH AA O   1 
HETATM 4544 O  O   . HOH I 5 .   ? 14.65200  2.77500   7.64600   1.000 22.76958  ? 578 HOH AA O   1 
HETATM 4545 O  O   . HOH I 5 .   ? 2.69600   1.23500   3.84300   1.000 23.46482  ? 579 HOH AA O   1 
HETATM 4546 O  O   . HOH I 5 .   ? 27.13200  24.67500  2.50400   1.000 33.01027  ? 580 HOH AA O   1 
HETATM 4547 O  O   . HOH I 5 .   ? -0.04000  1.67200   -3.31500  1.000 28.09529  ? 581 HOH AA O   1 
HETATM 4548 O  O   . HOH I 5 .   ? 25.57100  19.47900  7.75700   1.000 19.25283  ? 582 HOH AA O   1 
HETATM 4549 O  O   . HOH I 5 .   ? 22.63000  35.27000  -7.82400  1.000 34.28850  ? 583 HOH AA O   1 
HETATM 4550 O  O   . HOH I 5 .   ? 7.97400   34.99800  11.56000  1.000 34.62637  ? 584 HOH AA O   1 
HETATM 4551 O  O   . HOH I 5 .   ? -2.39000  19.23500  6.29000   1.000 28.98656  ? 585 HOH AA O   1 
HETATM 4552 O  O   . HOH I 5 .   ? 8.10600   24.64600  -16.01300 1.000 35.46442  ? 586 HOH AA O   1 
HETATM 4553 O  O   . HOH I 5 .   ? 4.36700   34.44600  19.33500  1.000 18.50162  ? 587 HOH AA O   1 
HETATM 4554 O  O   . HOH I 5 .   ? 22.24400  24.07300  -13.18800 1.000 23.98803  ? 588 HOH AA O   1 
HETATM 4555 O  O   . HOH I 5 .   ? 9.50300   30.51100  -10.02300 1.000 18.98694  ? 589 HOH AA O   1 
HETATM 4556 O  O   . HOH I 5 .   ? 10.85000  30.71500  22.26800  1.000 29.82602  ? 590 HOH AA O   1 
HETATM 4557 O  O   . HOH I 5 .   ? 8.32400   36.95500  -0.43300  1.000 36.60597  ? 591 HOH AA O   1 
HETATM 4558 O  O   . HOH I 5 .   ? -6.55700  25.06000  4.31100   1.000 32.54677  ? 592 HOH AA O   1 
HETATM 4559 O  O   . HOH I 5 .   ? -0.33300  3.29200   3.29200   1.000 21.28970  ? 593 HOH AA O   1 
HETATM 4560 O  O   . HOH I 5 .   ? 3.18300   29.11800  -8.28500  1.000 24.37670  ? 594 HOH AA O   1 
HETATM 4561 O  O   . HOH I 5 .   ? 34.63800  22.27000  -19.01200 1.000 37.81532  ? 595 HOH AA O   1 
HETATM 4562 O  O   . HOH I 5 .   ? 30.37500  21.54600  -19.56600 1.000 39.25659  ? 596 HOH AA O   1 
HETATM 4563 O  O   . HOH I 5 .   ? -1.84000  18.63900  3.61500   1.000 20.19861  ? 597 HOH AA O   1 
HETATM 4564 O  O   . HOH I 5 .   ? 22.20900  17.84600  -12.68900 1.000 32.64532  ? 598 HOH AA O   1 
HETATM 4565 O  O   . HOH I 5 .   ? 5.89100   33.75400  23.10600  1.000 33.71098  ? 599 HOH AA O   1 
HETATM 4566 O  O   . HOH I 5 .   ? 26.58200  17.08000  8.04100   1.000 33.12043  ? 600 HOH AA O   1 
HETATM 4567 O  O   . HOH I 5 .   ? 1.63200   1.97600   1.38700   1.000 20.43113  ? 601 HOH AA O   1 
HETATM 4568 O  O   . HOH I 5 .   ? 27.80700  28.19000  5.33100   1.000 18.17134  ? 602 HOH AA O   1 
HETATM 4569 O  O   . HOH I 5 .   ? 35.652    36.865    -14.689   1.000 36.40071  ? 603 HOH AA O   1 
HETATM 4570 O  O   . HOH I 5 .   ? 34.41900  28.45900  2.80300   1.000 36.89921  ? 604 HOH AA O   1 
HETATM 4571 O  O   A HOH I 5 .   ? 5.01700   -2.94100  8.43800   0.489 14.82500  ? 605 HOH AA O   1 
HETATM 4572 O  O   B HOH I 5 .   ? 2.92700   -2.64000  7.12500   0.511 16.58705  ? 605 HOH AA O   1 
HETATM 4573 O  O   . HOH I 5 .   ? 32.13600  26.75900  2.35100   1.000 28.57697  ? 606 HOH AA O   1 
HETATM 4574 O  O   . HOH I 5 .   ? 24.40200  24.11400  19.36000  1.000 24.32521  ? 607 HOH AA O   1 
HETATM 4575 O  O   . HOH I 5 .   ? 30.17900  23.01800  2.03700   1.000 35.52614  ? 608 HOH AA O   1 
HETATM 4576 O  O   . HOH I 5 .   ? 24.367    16.212    -11.583   1.000 29.60617  ? 609 HOH AA O   1 
HETATM 4577 O  O   . HOH I 5 .   ? 29.39200  29.05700  21.74000  1.000 39.73203  ? 610 HOH AA O   1 
HETATM 4578 O  O   . HOH I 5 .   ? -0.27700  0.00000   0.00000   0.50  29.93921  ? 611 HOH AA O   1 
HETATM 4579 O  O   . HOH I 5 .   ? 29.52200  26.56800  3.21700   1.000 33.91715  ? 612 HOH AA O   1 
HETATM 4580 O  O   . HOH J 5 .   ? 27.03300  23.40700  21.43000  1.000 35.22492  ? 501 HOH BA O   1 
HETATM 4581 O  O   . HOH J 5 .   ? 18.14200  8.98400   11.66400  1.000 16.33819  ? 502 HOH BA O   1 
HETATM 4582 O  O   . HOH J 5 .   ? 26.84100  -18.64300 22.36200  1.000 32.11936  ? 503 HOH BA O   1 
HETATM 4583 O  O   . HOH J 5 .   ? -3.33300  -12.56600 17.53800  1.000 24.70511  ? 504 HOH BA O   1 
HETATM 4584 O  O   . HOH J 5 .   ? 29.51800  19.57300  31.02800  1.000 22.12713  ? 505 HOH BA O   1 
HETATM 4585 O  O   . HOH J 5 .   ? 41.66100  -13.32100 9.44900   1.000 29.51942  ? 506 HOH BA O   1 
HETATM 4586 O  O   . HOH J 5 .   ? 4.00700   6.21600   33.63300  1.000 18.29315  ? 507 HOH BA O   1 
HETATM 4587 O  O   . HOH J 5 .   ? 15.19400  14.04700  32.28800  1.000 38.83795  ? 508 HOH BA O   1 
HETATM 4588 O  O   . HOH J 5 .   ? 32.76600  1.75100   31.65200  1.000 19.02652  ? 509 HOH BA O   1 
HETATM 4589 O  O   . HOH J 5 .   ? 37.87300  0.75200   26.37800  1.000 25.20154  ? 510 HOH BA O   1 
HETATM 4590 O  O   . HOH J 5 .   ? -0.43400  -20.30600 27.97500  1.000 36.37665  ? 511 HOH BA O   1 
HETATM 4591 O  O   . HOH J 5 .   ? 27.83800  1.62200   6.43200   1.000 15.20767  ? 512 HOH BA O   1 
HETATM 4592 O  O   . HOH J 5 .   ? 36.20300  -4.11200  29.62100  1.000 15.35342  ? 513 HOH BA O   1 
HETATM 4593 O  O   . HOH J 5 .   ? 32.63400  -16.92500 3.01000   1.000 28.84274  ? 514 HOH BA O   1 
HETATM 4594 O  O   . HOH J 5 .   ? 27.59000  -11.58100 4.21200   1.000 15.89230  ? 515 HOH BA O   1 
HETATM 4595 O  O   . HOH J 5 .   ? 29.42600  -4.98000  35.39900  1.000 20.41258  ? 516 HOH BA O   1 
HETATM 4596 O  O   . HOH J 5 .   ? 5.34500   -15.44700 27.85400  1.000 20.39952  ? 517 HOH BA O   1 
HETATM 4597 O  O   . HOH J 5 .   ? 4.32500   -10.21800 24.70300  1.000 13.09424  ? 518 HOH BA O   1 
HETATM 4598 O  O   . HOH J 5 .   ? 32.67900  24.77400  17.77700  1.000 24.38110  ? 519 HOH BA O   1 
HETATM 4599 O  O   . HOH J 5 .   ? 15.43400  13.39500  35.49000  1.000 32.06712  ? 520 HOH BA O   1 
HETATM 4600 O  O   . HOH J 5 .   ? 12.25000  -14.84500 16.45400  1.000 16.01074  ? 521 HOH BA O   1 
HETATM 4601 O  O   . HOH J 5 .   ? 13.58800  -17.40200 19.57000  1.000 34.68922  ? 522 HOH BA O   1 
HETATM 4602 O  O   . HOH J 5 .   ? 14.59300  3.40100   30.08400  1.000 10.70048  ? 523 HOH BA O   1 
HETATM 4603 O  O   . HOH J 5 .   ? 34.77700  10.71000  20.65200  1.000 23.55290  ? 524 HOH BA O   1 
HETATM 4604 O  O   . HOH J 5 .   ? 12.33100  16.23100  24.59000  1.000 14.38350  ? 525 HOH BA O   1 
HETATM 4605 O  O   . HOH J 5 .   ? 8.99400   -0.13700  29.10900  1.000 14.39480  ? 526 HOH BA O   1 
HETATM 4606 O  O   . HOH J 5 .   ? 36.79500  12.11200  19.70000  1.000 46.68679  ? 527 HOH BA O   1 
HETATM 4607 O  O   . HOH J 5 .   ? 10.76300  1.96000   11.62700  1.000 14.69032  ? 528 HOH BA O   1 
HETATM 4608 O  O   . HOH J 5 .   ? 38.30900  -4.38700  5.96700   1.000 17.63742  ? 529 HOH BA O   1 
HETATM 4609 O  O   . HOH J 5 .   ? 36.91900  3.99200   19.51200  1.000 21.69552  ? 530 HOH BA O   1 
HETATM 4610 O  O   . HOH J 5 .   ? 33.43800  8.07300   12.41500  1.000 19.90875  ? 531 HOH BA O   1 
HETATM 4611 O  O   . HOH J 5 .   ? 24.19600  19.60400  27.47900  1.000 32.97834  ? 532 HOH BA O   1 
HETATM 4612 O  O   . HOH J 5 .   ? 18.39200  0.63400   7.81300   1.000 14.32544  ? 533 HOH BA O   1 
HETATM 4613 O  O   . HOH J 5 .   ? 12.33000  -6.03500  20.08900  1.000 4.49575   ? 534 HOH BA O   1 
HETATM 4614 O  O   . HOH J 5 .   ? 9.96300   -8.03300  20.10100  1.000 6.34646   ? 535 HOH BA O   1 
HETATM 4615 O  O   . HOH J 5 .   ? 38.31300  17.27300  11.47400  1.000 30.11657  ? 536 HOH BA O   1 
HETATM 4616 O  O   . HOH J 5 .   ? 44.38800  -17.22900 17.98100  1.000 25.14657  ? 537 HOH BA O   1 
HETATM 4617 O  O   . HOH J 5 .   ? 1.92600   -8.31800  28.83600  1.000 12.65883  ? 538 HOH BA O   1 
HETATM 4618 O  O   . HOH J 5 .   ? 40.77400  3.54900   14.56500  1.000 25.12732  ? 539 HOH BA O   1 
HETATM 4619 O  O   . HOH J 5 .   ? 38.03100  -6.98100  8.82600   1.000 16.44623  ? 540 HOH BA O   1 
HETATM 4620 O  O   . HOH J 5 .   ? 31.42800  3.71500   1.64600   1.000 32.59440  ? 541 HOH BA O   1 
HETATM 4621 O  O   . HOH J 5 .   ? 28.10200  5.53600   34.10500  1.000 22.77649  ? 542 HOH BA O   1 
HETATM 4622 O  O   . HOH J 5 .   ? 35.24700  -9.12200  4.60800   1.000 27.29247  ? 543 HOH BA O   1 
HETATM 4623 O  O   . HOH J 5 .   ? 35.52500  -7.38700  7.37700   1.000 32.79955  ? 544 HOH BA O   1 
HETATM 4624 O  O   . HOH J 5 .   ? 34.80900  -0.65300  16.95200  1.000 11.36685  ? 545 HOH BA O   1 
HETATM 4625 O  O   . HOH J 5 .   ? 2.68300   -18.20600 39.86600  1.000 27.81245  ? 546 HOH BA O   1 
HETATM 4626 O  O   . HOH J 5 .   ? 34.284    -16.467   5.620     1.000 25.33986  ? 547 HOH BA O   1 
HETATM 4627 O  O   . HOH J 5 .   ? 16.00700  20.86100  27.97700  1.000 22.97585  ? 548 HOH BA O   1 
HETATM 4628 O  O   . HOH J 5 .   ? 13.83700  2.94600   17.99500  1.000 13.54665  ? 549 HOH BA O   1 
HETATM 4629 O  O   . HOH J 5 .   ? 20.66100  11.67800  9.10400   1.000 16.13193  ? 550 HOH BA O   1 
HETATM 4630 O  O   . HOH J 5 .   ? 34.70400  2.54100   3.76500   1.000 19.35327  ? 551 HOH BA O   1 
HETATM 4631 O  O   . HOH J 5 .   ? 34.81100  7.97000   15.05300  1.000 16.11998  ? 552 HOH BA O   1 
HETATM 4632 O  O   . HOH J 5 .   ? 26.01100  -4.70400  36.81200  1.000 29.07017  ? 553 HOH BA O   1 
HETATM 4633 O  O   . HOH J 5 .   ? 6.73400   -16.25300 22.36600  1.000 21.73445  ? 554 HOH BA O   1 
HETATM 4634 O  O   . HOH J 5 .   ? 7.98000   -1.72700  21.88900  1.000 30.43273  ? 555 HOH BA O   1 
HETATM 4635 O  O   . HOH J 5 .   ? 16.78900  -3.15200  7.28800   1.000 30.07321  ? 556 HOH BA O   1 
HETATM 4636 O  O   . HOH J 5 .   ? 23.85500  5.46600   36.41400  1.000 32.36813  ? 557 HOH BA O   1 
HETATM 4637 O  O   . HOH J 5 .   ? 34.11300  -3.08500  0.98700   1.000 33.67646  ? 558 HOH BA O   1 
HETATM 4638 O  O   . HOH J 5 .   ? 31.07300  -9.24500  29.49200  1.000 31.26653  ? 559 HOH BA O   1 
HETATM 4639 O  O   . HOH J 5 .   ? 5.81400   -20.58600 20.87800  1.000 22.40179  ? 560 HOH BA O   1 
HETATM 4640 O  O   . HOH J 5 .   ? 8.79200   5.15400   20.42400  1.000 23.33582  ? 561 HOH BA O   1 
HETATM 4641 O  O   . HOH J 5 .   ? 31.25700  -11.80300 27.61800  1.000 27.14394  ? 562 HOH BA O   1 
HETATM 4642 O  O   . HOH J 5 .   ? 40.42200  -12.64000 21.11200  1.000 23.40036  ? 563 HOH BA O   1 
HETATM 4643 O  O   . HOH J 5 .   ? -0.69400  -21.91700 19.97700  1.000 22.61044  ? 564 HOH BA O   1 
HETATM 4644 O  O   . HOH J 5 .   ? 29.98400  27.12400  20.14100  1.000 22.71904  ? 565 HOH BA O   1 
HETATM 4645 O  O   . HOH J 5 .   ? 33.86900  9.88400   2.59500   1.000 31.77654  ? 566 HOH BA O   1 
HETATM 4646 O  O   . HOH J 5 .   ? 19.92300  7.22600   3.54400   1.000 31.09242  ? 567 HOH BA O   1 
HETATM 4647 O  O   . HOH J 5 .   ? 41.80800  1.42500   24.53800  1.000 39.95681  ? 568 HOH BA O   1 
HETATM 4648 O  O   . HOH J 5 .   ? 28.45000  1.91400   35.14400  1.000 15.44393  ? 569 HOH BA O   1 
HETATM 4649 O  O   . HOH J 5 .   ? 30.46700  3.36800   33.61800  1.000 34.04042  ? 570 HOH BA O   1 
HETATM 4650 O  O   . HOH J 5 .   ? 27.29100  12.36900  35.62300  1.000 18.25974  ? 571 HOH BA O   1 
HETATM 4651 O  O   . HOH J 5 .   ? -4.233    -12.068   30.732    1.000 33.28677  ? 572 HOH BA O   1 
HETATM 4652 O  O   . HOH J 5 .   ? 34.12100  -16.01400 23.40200  1.000 27.22779  ? 573 HOH BA O   1 
HETATM 4653 O  O   . HOH J 5 .   ? 38.00100  -7.81500  5.34400   1.000 40.22563  ? 574 HOH BA O   1 
HETATM 4654 O  O   . HOH J 5 .   ? 24.37000  -13.84300 11.64000  1.000 21.37527  ? 575 HOH BA O   1 
HETATM 4655 O  O   . HOH J 5 .   ? -6.686    -21.268   24.637    1.000 38.64530  ? 576 HOH BA O   1 
HETATM 4656 O  O   . HOH J 5 .   ? 13.20800  15.36600  26.79500  1.000 20.88013  ? 577 HOH BA O   1 
HETATM 4657 O  O   . HOH J 5 .   ? 17.86300  15.64000  33.48800  1.000 20.09376  ? 578 HOH BA O   1 
HETATM 4658 O  O   . HOH J 5 .   ? 19.32800  -4.16800  37.70200  1.000 20.69582  ? 579 HOH BA O   1 
HETATM 4659 O  O   . HOH J 5 .   ? 6.69900   1.56300   28.98500  1.000 25.48464  ? 580 HOH BA O   1 
HETATM 4660 O  O   . HOH J 5 .   ? 25.68200  -16.71100 15.99300  1.000 24.93905  ? 581 HOH BA O   1 
HETATM 4661 O  O   . HOH J 5 .   ? 10.02900  16.35300  26.45200  1.000 23.90744  ? 582 HOH BA O   1 
HETATM 4662 O  O   . HOH J 5 .   ? 44.912    -11.353   13.774    1.000 38.73457  ? 583 HOH BA O   1 
HETATM 4663 O  O   . HOH J 5 .   ? 17.87400  20.14200  29.82600  1.000 24.51058  ? 584 HOH BA O   1 
HETATM 4664 O  O   . HOH J 5 .   ? 24.82700  -14.45700 28.57700  1.000 26.95792  ? 585 HOH BA O   1 
HETATM 4665 O  O   . HOH J 5 .   ? 32.73900  1.02400   1.83200   1.000 21.24444  ? 586 HOH BA O   1 
HETATM 4666 O  O   . HOH J 5 .   ? 19.98100  14.47200  34.75500  1.000 17.99007  ? 587 HOH BA O   1 
HETATM 4667 O  O   . HOH J 5 .   ? 34.46500  0.00000   -0.00000  0.777 36.90379  ? 588 HOH BA O   1 
HETATM 4668 O  O   . HOH J 5 .   ? 18.41200  13.00900  36.07500  1.000 24.76743  ? 589 HOH BA O   1 
HETATM 4669 O  O   . HOH J 5 .   ? 19.91500  22.31700  30.01900  1.000 33.13066  ? 590 HOH BA O   1 
HETATM 4670 O  O   . HOH J 5 .   ? 17.83600  -3.19900  4.37100   1.000 45.24672  ? 591 HOH BA O   1 
HETATM 4671 O  O   . HOH J 5 .   ? 34.10200  8.67900   0.47300   1.000 40.70531  ? 592 HOH BA O   1 
# 
