data_9DYS
# 
_entry.id   9DYS 
# 
_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   9DYS         pdb_00009dys 10.2210/pdb9dys/pdb 
WWPDB D_1000289079 ?            ?                   
# 
_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                        9DYS 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        
'Same protein, lower resolution with PEG molecule bound on a different portion of the active site.' 
_pdbx_database_related.db_id          9CXR 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_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 
'Capra, N.'    1 0000-0002-2898-6479 
'Meilleur, F.' 2 0000-0001-9313-8989 
# 
_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    2   ? ? ? ? 
4 non-polymer syn 'TETRAETHYLENE GLYCOL'                    194.226   1   ? ? ? ? 
5 water       nat water                                     18.015    203 ? ? ? ? 
# 
_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                 A,B 
_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 'TETRAETHYLENE GLYCOL' PG4 
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          ? 
_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  
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL' ?                 'C8 H18 O5'      194.226 
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 A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   THR 3   3   3   THR THR A . n 
A 1 4   ASP 4   4   4   ASP ASP A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ARG 9   9   9   ARG ARG A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  ASP 15  15  15  ASP ASP A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  MET 19  19  19  MET MET A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  GLY 39  39  39  GLY GLY A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  MET 56  56  56  MET MET A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  MET 63  63  63  MET MET A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  TYR 81  81  81  TYR TYR A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  GLN 85  85  85  GLN GLN A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  TYR 89  89  89  TYR TYR A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 MET 120 120 120 MET MET A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 CYS 125 125 125 CYS CYS A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 ARG 153 153 153 ARG ARG A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 THR 188 188 188 THR THR A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 LYS 197 197 197 LYS LYS A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 MET 223 223 223 MET MET A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
A 1 225 MET 225 225 ?   ?   ?   A . n 
A 1 226 ASN 226 226 ?   ?   ?   A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 CYS 236 236 236 CYS CYS A . n 
A 1 237 ARG 237 237 237 ARG ARG A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 THR 239 239 239 THR THR A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 MET 246 246 246 MET MET A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 CYS 259 259 259 CYS CYS A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 HIS 262 262 262 HIS HIS A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 ASN 264 264 264 ASN ASN A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 GLY 274 274 274 GLY GLY A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 GLN 276 276 276 GLN GLN A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ASP 285 285 285 ASP ASP A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 ALA 295 295 295 ALA ALA A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 LEU 297 297 297 LEU LEU A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 CYS 299 299 299 CYS CYS A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ASP 301 301 301 ASP ASP A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 MET 304 304 304 MET MET A . n 
A 1 305 GLN 305 305 305 GLN GLN A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   LEU 2   2   2   LEU LEU B . n 
B 1 3   THR 3   3   3   THR THR B . n 
B 1 4   ASP 4   4   4   ASP ASP B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   ASP 6   6   6   ASP ASP B . n 
B 1 7   GLY 7   7   7   GLY GLY B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   ARG 9   9   9   ARG ARG B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  ALA 13  13  13  ALA ALA B . n 
B 1 14  THR 14  14  14  THR THR B . n 
B 1 15  ASP 15  15  15  ASP ASP B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  ARG 17  17  17  ARG ARG B . n 
B 1 18  ALA 18  18  18  ALA ALA B . n 
B 1 19  MET 19  19  19  MET MET B . n 
B 1 20  THR 20  20  20  THR THR B . n 
B 1 21  GLY 21  21  21  GLY GLY B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  THR 23  23  23  THR THR B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  VAL 37  37  37  VAL VAL B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  GLY 39  39  39  GLY GLY B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  ASN 41  41  41  ASN ASN B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  ILE 45  45  45  ILE ILE B . n 
B 1 46  TYR 46  46  46  TYR TYR B . n 
B 1 47  THR 47  47  47  THR THR B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  MET 56  56  56  MET MET B . n 
B 1 57  PRO 57  57  57  PRO PRO B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  ILE 62  62  62  ILE ILE B . n 
B 1 63  MET 63  63  63  MET MET B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  GLY 66  66  66  GLY GLY B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  TYR 81  81  81  TYR TYR B . n 
B 1 82  PHE 82  82  82  PHE PHE B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  GLN 85  85  85  GLN GLN B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  TYR 89  89  89  TYR TYR B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  LYS 95  95  95  LYS LYS B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 ASP 106 106 106 ASP ASP B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 ASP 111 111 111 ASP ASP B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 PRO 116 116 116 PRO PRO B . n 
B 1 117 ASP 117 117 117 ASP ASP B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 MET 120 120 120 MET MET B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 CYS 125 125 125 CYS CYS B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 PRO 130 130 130 PRO PRO B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 GLU 134 134 134 GLU GLU B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 ARG 137 137 137 ARG ARG B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 THR 145 145 145 THR THR B . n 
B 1 146 VAL 146 146 146 VAL VAL B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 GLY 151 151 151 GLY GLY B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 ARG 153 153 153 ARG ARG B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 PRO 157 157 157 PRO PRO B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 THR 164 164 164 THR THR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 TYR 168 168 168 TYR TYR B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 ILE 171 171 171 ILE ILE B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 VAL 179 179 179 VAL VAL B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 PHE 182 182 182 PHE PHE B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 THR 188 188 188 THR THR B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 ARG 191 191 191 ARG ARG B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 LYS 197 197 197 LYS LYS B . n 
B 1 198 TYR 198 198 198 TYR TYR B . n 
B 1 199 GLU 199 199 199 GLU GLU B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 THR 206 206 206 THR THR B . n 
B 1 207 TYR 207 207 207 TYR TYR B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 MET 210 210 210 MET MET B . n 
B 1 211 LYS 211 211 211 LYS LYS B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 GLY 213 213 213 GLY GLY B . n 
B 1 214 ASP 214 214 214 ASP ASP B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 GLN 217 217 217 GLN GLN B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 MET 223 223 223 MET MET B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 MET 225 225 ?   ?   ?   B . n 
B 1 226 ASN 226 226 ?   ?   ?   B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 SER 233 233 233 SER SER B . n 
B 1 234 THR 234 234 234 THR THR B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 CYS 236 236 236 CYS CYS B . n 
B 1 237 ARG 237 237 237 ARG ARG B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 THR 239 239 239 THR THR B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 GLU 242 242 242 GLU GLU B . n 
B 1 243 ALA 243 243 243 ALA ALA B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 MET 246 246 246 MET MET B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 LEU 249 249 249 LEU LEU B . n 
B 1 250 ALA 250 250 250 ALA ALA B . n 
B 1 251 HIS 251 251 251 HIS HIS B . n 
B 1 252 ASN 252 252 252 ASN ASN B . n 
B 1 253 GLY 253 253 253 GLY GLY B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 CYS 259 259 259 CYS CYS B . n 
B 1 260 PRO 260 260 260 PRO PRO B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 HIS 262 262 262 HIS HIS B . n 
B 1 263 THR 263 263 263 THR THR B . n 
B 1 264 ASN 264 264 264 ASN ASN B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 ASP 268 268 268 ASP ASP B . n 
B 1 269 THR 269 269 269 THR THR B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 ALA 272 272 272 ALA ALA B . n 
B 1 273 THR 273 273 273 THR THR B . n 
B 1 274 GLY 274 274 274 GLY GLY B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 GLN 276 276 276 GLN GLN B . n 
B 1 277 LYS 277 277 277 LYS LYS B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 THR 281 281 281 THR THR B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 PRO 283 283 283 PRO PRO B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 ASP 285 285 285 ASP ASP B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLY 288 288 288 GLY GLY B . n 
B 1 289 THR 289 289 289 THR THR B . n 
B 1 290 ALA 290 290 290 ALA ALA B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 ALA 294 294 294 ALA ALA B . n 
B 1 295 ALA 295 295 295 ALA ALA B . n 
B 1 296 MET 296 296 296 MET MET B . n 
B 1 297 LEU 297 297 297 LEU LEU B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 CYS 299 299 299 CYS CYS B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ASP 301 301 301 ASP ASP B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 MET 304 304 304 MET MET B . n 
B 1 305 GLN 305 305 305 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 EDO 1   401 402 EDO EDO A . 
D 3 NA  1   402 2   NA  NA  A . 
E 4 PG4 1   401 401 PG4 PG4 B . 
F 3 NA  1   402 1   NA  NA  B . 
G 5 HOH 1   501 205 HOH HOH A . 
G 5 HOH 2   502 3   HOH HOH A . 
G 5 HOH 3   503 113 HOH HOH A . 
G 5 HOH 4   504 163 HOH HOH A . 
G 5 HOH 5   505 177 HOH HOH A . 
G 5 HOH 6   506 170 HOH HOH A . 
G 5 HOH 7   507 22  HOH HOH A . 
G 5 HOH 8   508 47  HOH HOH A . 
G 5 HOH 9   509 118 HOH HOH A . 
G 5 HOH 10  510 71  HOH HOH A . 
G 5 HOH 11  511 187 HOH HOH A . 
G 5 HOH 12  512 104 HOH HOH A . 
G 5 HOH 13  513 145 HOH HOH A . 
G 5 HOH 14  514 124 HOH HOH A . 
G 5 HOH 15  515 133 HOH HOH A . 
G 5 HOH 16  516 119 HOH HOH A . 
G 5 HOH 17  517 169 HOH HOH A . 
G 5 HOH 18  518 28  HOH HOH A . 
G 5 HOH 19  519 16  HOH HOH A . 
G 5 HOH 20  520 189 HOH HOH A . 
G 5 HOH 21  521 107 HOH HOH A . 
G 5 HOH 22  522 44  HOH HOH A . 
G 5 HOH 23  523 137 HOH HOH A . 
G 5 HOH 24  524 33  HOH HOH A . 
G 5 HOH 25  525 69  HOH HOH A . 
G 5 HOH 26  526 48  HOH HOH A . 
G 5 HOH 27  527 72  HOH HOH A . 
G 5 HOH 28  528 55  HOH HOH A . 
G 5 HOH 29  529 182 HOH HOH A . 
G 5 HOH 30  530 68  HOH HOH A . 
G 5 HOH 31  531 147 HOH HOH A . 
G 5 HOH 32  532 58  HOH HOH A . 
G 5 HOH 33  533 90  HOH HOH A . 
G 5 HOH 34  534 96  HOH HOH A . 
G 5 HOH 35  535 158 HOH HOH A . 
G 5 HOH 36  536 39  HOH HOH A . 
G 5 HOH 37  537 75  HOH HOH A . 
G 5 HOH 38  538 192 HOH HOH A . 
G 5 HOH 39  539 88  HOH HOH A . 
G 5 HOH 40  540 116 HOH HOH A . 
G 5 HOH 41  541 7   HOH HOH A . 
G 5 HOH 42  542 14  HOH HOH A . 
G 5 HOH 43  543 109 HOH HOH A . 
G 5 HOH 44  544 183 HOH HOH A . 
G 5 HOH 45  545 35  HOH HOH A . 
G 5 HOH 46  546 160 HOH HOH A . 
G 5 HOH 47  547 185 HOH HOH A . 
G 5 HOH 48  548 32  HOH HOH A . 
G 5 HOH 49  549 13  HOH HOH A . 
G 5 HOH 50  550 165 HOH HOH A . 
G 5 HOH 51  551 20  HOH HOH A . 
G 5 HOH 52  552 25  HOH HOH A . 
G 5 HOH 53  553 178 HOH HOH A . 
G 5 HOH 54  554 62  HOH HOH A . 
G 5 HOH 55  555 23  HOH HOH A . 
G 5 HOH 56  556 17  HOH HOH A . 
G 5 HOH 57  557 49  HOH HOH A . 
G 5 HOH 58  558 66  HOH HOH A . 
G 5 HOH 59  559 149 HOH HOH A . 
G 5 HOH 60  560 175 HOH HOH A . 
G 5 HOH 61  561 162 HOH HOH A . 
G 5 HOH 62  562 136 HOH HOH A . 
G 5 HOH 63  563 80  HOH HOH A . 
G 5 HOH 64  564 29  HOH HOH A . 
G 5 HOH 65  565 171 HOH HOH A . 
G 5 HOH 66  566 174 HOH HOH A . 
G 5 HOH 67  567 79  HOH HOH A . 
G 5 HOH 68  568 98  HOH HOH A . 
G 5 HOH 69  569 114 HOH HOH A . 
G 5 HOH 70  570 46  HOH HOH A . 
G 5 HOH 71  571 2   HOH HOH A . 
G 5 HOH 72  572 115 HOH HOH A . 
G 5 HOH 73  573 50  HOH HOH A . 
G 5 HOH 74  574 121 HOH HOH A . 
G 5 HOH 75  575 122 HOH HOH A . 
G 5 HOH 76  576 167 HOH HOH A . 
G 5 HOH 77  577 172 HOH HOH A . 
G 5 HOH 78  578 100 HOH HOH A . 
G 5 HOH 79  579 31  HOH HOH A . 
G 5 HOH 80  580 112 HOH HOH A . 
G 5 HOH 81  581 159 HOH HOH A . 
G 5 HOH 82  582 152 HOH HOH A . 
G 5 HOH 83  583 64  HOH HOH A . 
G 5 HOH 84  584 70  HOH HOH A . 
G 5 HOH 85  585 108 HOH HOH A . 
G 5 HOH 86  586 110 HOH HOH A . 
G 5 HOH 87  587 93  HOH HOH A . 
G 5 HOH 88  588 42  HOH HOH A . 
G 5 HOH 89  589 76  HOH HOH A . 
G 5 HOH 90  590 97  HOH HOH A . 
G 5 HOH 91  591 196 HOH HOH A . 
G 5 HOH 92  592 73  HOH HOH A . 
G 5 HOH 93  593 30  HOH HOH A . 
G 5 HOH 94  594 190 HOH HOH A . 
G 5 HOH 95  595 146 HOH HOH A . 
G 5 HOH 96  596 129 HOH HOH A . 
G 5 HOH 97  597 26  HOH HOH A . 
G 5 HOH 98  598 102 HOH HOH A . 
G 5 HOH 99  599 155 HOH HOH A . 
G 5 HOH 100 600 184 HOH HOH A . 
G 5 HOH 101 601 87  HOH HOH A . 
G 5 HOH 102 602 186 HOH HOH A . 
H 5 HOH 1   501 204 HOH HOH B . 
H 5 HOH 2   502 9   HOH HOH B . 
H 5 HOH 3   503 125 HOH HOH B . 
H 5 HOH 4   504 193 HOH HOH B . 
H 5 HOH 5   505 173 HOH HOH B . 
H 5 HOH 6   506 59  HOH HOH B . 
H 5 HOH 7   507 143 HOH HOH B . 
H 5 HOH 8   508 130 HOH HOH B . 
H 5 HOH 9   509 144 HOH HOH B . 
H 5 HOH 10  510 195 HOH HOH B . 
H 5 HOH 11  511 60  HOH HOH B . 
H 5 HOH 12  512 128 HOH HOH B . 
H 5 HOH 13  513 140 HOH HOH B . 
H 5 HOH 14  514 84  HOH HOH B . 
H 5 HOH 15  515 142 HOH HOH B . 
H 5 HOH 16  516 78  HOH HOH B . 
H 5 HOH 17  517 11  HOH HOH B . 
H 5 HOH 18  518 24  HOH HOH B . 
H 5 HOH 19  519 151 HOH HOH B . 
H 5 HOH 20  520 127 HOH HOH B . 
H 5 HOH 21  521 99  HOH HOH B . 
H 5 HOH 22  522 191 HOH HOH B . 
H 5 HOH 23  523 132 HOH HOH B . 
H 5 HOH 24  524 180 HOH HOH B . 
H 5 HOH 25  525 53  HOH HOH B . 
H 5 HOH 26  526 1   HOH HOH B . 
H 5 HOH 27  527 92  HOH HOH B . 
H 5 HOH 28  528 94  HOH HOH B . 
H 5 HOH 29  529 40  HOH HOH B . 
H 5 HOH 30  530 12  HOH HOH B . 
H 5 HOH 31  531 157 HOH HOH B . 
H 5 HOH 32  532 38  HOH HOH B . 
H 5 HOH 33  533 10  HOH HOH B . 
H 5 HOH 34  534 81  HOH HOH B . 
H 5 HOH 35  535 197 HOH HOH B . 
H 5 HOH 36  536 18  HOH HOH B . 
H 5 HOH 37  537 83  HOH HOH B . 
H 5 HOH 38  538 34  HOH HOH B . 
H 5 HOH 39  539 8   HOH HOH B . 
H 5 HOH 40  540 138 HOH HOH B . 
H 5 HOH 41  541 179 HOH HOH B . 
H 5 HOH 42  542 21  HOH HOH B . 
H 5 HOH 43  543 45  HOH HOH B . 
H 5 HOH 44  544 52  HOH HOH B . 
H 5 HOH 45  545 19  HOH HOH B . 
H 5 HOH 46  546 141 HOH HOH B . 
H 5 HOH 47  547 51  HOH HOH B . 
H 5 HOH 48  548 153 HOH HOH B . 
H 5 HOH 49  549 105 HOH HOH B . 
H 5 HOH 50  550 63  HOH HOH B . 
H 5 HOH 51  551 36  HOH HOH B . 
H 5 HOH 52  552 67  HOH HOH B . 
H 5 HOH 53  553 15  HOH HOH B . 
H 5 HOH 54  554 85  HOH HOH B . 
H 5 HOH 55  555 135 HOH HOH B . 
H 5 HOH 56  556 89  HOH HOH B . 
H 5 HOH 57  557 166 HOH HOH B . 
H 5 HOH 58  558 164 HOH HOH B . 
H 5 HOH 59  559 161 HOH HOH B . 
H 5 HOH 60  560 37  HOH HOH B . 
H 5 HOH 61  561 74  HOH HOH B . 
H 5 HOH 62  562 134 HOH HOH B . 
H 5 HOH 63  563 77  HOH HOH B . 
H 5 HOH 64  564 106 HOH HOH B . 
H 5 HOH 65  565 91  HOH HOH B . 
H 5 HOH 66  566 6   HOH HOH B . 
H 5 HOH 67  567 203 HOH HOH B . 
H 5 HOH 68  568 194 HOH HOH B . 
H 5 HOH 69  569 95  HOH HOH B . 
H 5 HOH 70  570 156 HOH HOH B . 
H 5 HOH 71  571 41  HOH HOH B . 
H 5 HOH 72  572 176 HOH HOH B . 
H 5 HOH 73  573 120 HOH HOH B . 
H 5 HOH 74  574 154 HOH HOH B . 
H 5 HOH 75  575 101 HOH HOH B . 
H 5 HOH 76  576 150 HOH HOH B . 
H 5 HOH 77  577 86  HOH HOH B . 
H 5 HOH 78  578 111 HOH HOH B . 
H 5 HOH 79  579 54  HOH HOH B . 
H 5 HOH 80  580 139 HOH HOH B . 
H 5 HOH 81  581 188 HOH HOH B . 
H 5 HOH 82  582 57  HOH HOH B . 
H 5 HOH 83  583 126 HOH HOH B . 
H 5 HOH 84  584 181 HOH HOH B . 
H 5 HOH 85  585 61  HOH HOH B . 
H 5 HOH 86  586 123 HOH HOH B . 
H 5 HOH 87  587 103 HOH HOH B . 
H 5 HOH 88  588 56  HOH HOH B . 
H 5 HOH 89  589 168 HOH HOH B . 
H 5 HOH 90  590 43  HOH HOH B . 
H 5 HOH 91  591 117 HOH HOH B . 
H 5 HOH 92  592 82  HOH HOH B . 
H 5 HOH 93  593 148 HOH HOH B . 
H 5 HOH 94  594 131 HOH HOH B . 
H 5 HOH 95  595 206 HOH HOH B . 
H 5 HOH 96  596 201 HOH HOH B . 
H 5 HOH 97  597 198 HOH HOH B . 
H 5 HOH 98  598 200 HOH HOH B . 
H 5 HOH 99  599 199 HOH HOH B . 
H 5 HOH 100 600 65  HOH HOH B . 
H 5 HOH 101 601 202 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .        3 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DYS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.879 
_cell.length_a_esd                 ? 
_cell.length_b                     96.511 
_cell.length_b_esd                 ? 
_cell.length_c                     105.188 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9DYS 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_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                   9DYS 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44 
_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              6.9 
_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    'Imidazole 0.1 M pH 6.9, Polyethylene glycol 6,000 20.0% w/v' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_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         2024-10-04 
_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                          22.6 
_reflns.entry_id                                       9DYS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               26.73 
_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                                     47261 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.92 
_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                                0.105 
_reflns.pdbx_Rpim_I_all                                0.038 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.097 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.89 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11136 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2605 
_reflns_shell.percent_possible_obs                          90.7 
_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                               4.3 
_reflns_shell.pdbx_chi_squared                              1.18 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.3 
_reflns_shell.pdbx_Rrim_I_all                               0.751 
_reflns_shell.pdbx_Rpim_I_all                               0.340 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.703 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.662 
_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]                            0.10 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.04 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.14 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.180 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9DYS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             26.73 
_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                     44737 
_refine.ls_number_reflns_R_free                  2470 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.13 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15170 
_refine.ls_R_factor_R_free                       0.17219 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15057 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.119 
_refine.pdbx_overall_ESU_R_Free                  0.104 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             2.346 
_refine.overall_SU_ML                            0.069 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        26.73 
_refine_hist.number_atoms_solvent             203 
_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         19 
_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' ? 0.009  0.012  4458 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4357 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.735  1.796  6036 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.591  1.731  9996 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.555  5.000  609  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.452  5.000  36   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.756 10.000 703  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  713  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  5324 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  964  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.111  1.940  2427 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.104  1.940  2427 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.963  3.473  3030 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.963  3.474  3031 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.103  2.561  2031 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.103  2.563  2032 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.245  4.402  3004 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.547  19.54  4624 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.528  19.28  4608 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.850 
_refine_ls_shell.d_res_low                        1.898 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             159 
_refine_ls_shell.number_reflns_R_work             2966 
_refine_ls_shell.percent_reflns_obs               91.19 
_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                  0.238 
_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   20 
_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                  0.252 
# 
_struct.entry_id                     9DYS 
_struct.title                        
;X-ray Crystallographic Structure of the Poly(Hexamethylene Adipamide) (Nylon66) Hydrolase Nyl50 at Room Temperature bound to tetraethylene glycol
;
_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        9DYS 
_struct_keywords.text            'Nylon hydrolase, Nylon66, nylon hydrolysis, thermostable, 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 4 ? 
F N N 3 ? 
G N N 5 ? 
H 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 9DYS A 1 ? 305 ? A0A522DD61 1 ? 305 ? 1 305 
2 1 9DYS B 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)' 4890  ? 
1 MORE         -39   ? 
1 'SSA (A^2)'  20370 ? 
# 
_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 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration'   ? 
2 1 'light scattering' ? 
# 
_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 A 1   ILE A 5   5 ? 5  
HELX_P HELX_P2  AA2 TYR A 46  ? TYR A 51  ? TYR A 46  TYR A 51  5 ? 6  
HELX_P HELX_P3  AA3 GLY A 67  ? GLY A 71  ? GLY A 67  GLY A 71  5 ? 5  
HELX_P HELX_P4  AA4 LEU A 72  ? GLN A 85  ? LEU A 72  GLN A 85  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 117 ? ALA A 127 ? ASP A 117 ALA A 127 1 ? 11 
HELX_P HELX_P6  AA6 VAL A 138 ? THR A 142 ? VAL A 138 THR A 142 5 ? 5  
HELX_P HELX_P7  AA7 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 5 ? 5  
HELX_P HELX_P8  AA8 TYR A 168 ? GLY A 170 ? TYR A 168 GLY A 170 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 205 ? GLY A 213 ? ASP A 205 GLY A 213 1 ? 9  
HELX_P HELX_P10 AB1 THR A 239 ? ALA A 257 ? THR A 239 ALA A 257 1 ? 19 
HELX_P HELX_P11 AB2 PRO A 283 ? MET A 304 ? PRO A 283 MET A 304 1 ? 22 
HELX_P HELX_P12 AB3 MET B 1   ? ILE B 5   ? MET B 1   ILE B 5   5 ? 5  
HELX_P HELX_P13 AB4 TYR B 46  ? TYR B 51  ? TYR B 46  TYR B 51  5 ? 6  
HELX_P HELX_P14 AB5 GLY B 67  ? GLY B 71  ? GLY B 67  GLY B 71  5 ? 5  
HELX_P HELX_P15 AB6 LEU B 72  ? GLN B 85  ? LEU B 72  GLN B 85  1 ? 14 
HELX_P HELX_P16 AB7 ASP B 117 ? ALA B 127 ? ASP B 117 ALA B 127 1 ? 11 
HELX_P HELX_P17 AB8 VAL B 138 ? THR B 142 ? VAL B 138 THR B 142 5 ? 5  
HELX_P HELX_P18 AB9 GLY B 151 ? SER B 155 ? GLY B 151 SER B 155 5 ? 5  
HELX_P HELX_P19 AC1 TYR B 168 ? GLY B 170 ? TYR B 168 GLY B 170 5 ? 3  
HELX_P HELX_P20 AC2 ASP B 205 ? GLY B 213 ? ASP B 205 GLY B 213 1 ? 9  
HELX_P HELX_P21 AC3 THR B 239 ? ALA B 257 ? THR B 239 ALA B 257 1 ? 19 
HELX_P HELX_P22 AC4 PRO B 283 ? MET B 304 ? PRO B 283 MET B 304 1 ? 22 
# 
_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 THR 227 OG1 ? ? ? 1_555 D NA  . NA ? ? A THR 227 A NA  402 1_555 ? ? ? ? ? ? ? 2.839 ? ? 
metalc2 metalc ? ? B THR 227 OG1 ? ? ? 1_555 F NA  . NA ? ? B THR 227 B NA  402 1_555 ? ? ? ? ? ? ? 2.901 ? ? 
metalc3 metalc ? ? F NA  .   NA  ? ? ? 1_555 H HOH . O  ? ? B NA  402 B HOH 546 1_555 ? ? ? ? ? ? ? 2.745 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OG1 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   B 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   THR 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    227 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    THR 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     227 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   NA 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    NA 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     402 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   H 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    B 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     546 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 77.0 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 A PRO 260 A ? PRO 260 A 1 -8.47  
2 CYS 259 B . ? CYS 259 B PRO 260 B ? PRO 260 B 1 -10.57 
# 
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 A 8   ASP A 15  
AA1 2 THR A 20  ? PHE A 27  ? THR A 20  PHE A 27  
AA1 3 GLY A 61  ? THR A 65  ? GLY A 61  THR A 65  
AA1 4 ALA A 101 ? VAL A 103 ? ALA A 101 VAL A 103 
AA1 5 THR A 44  ? ILE A 45  ? THR A 44  ILE A 45  
AA2 1 VAL A 31  ? VAL A 37  ? VAL A 31  VAL A 37  
AA2 2 THR A 269 ? LEU A 275 ? THR A 269 LEU A 275 
AA2 3 THR A 228 ? ARG A 237 ? THR A 228 ARG A 237 
AA2 4 LYS A 172 ? VAL A 179 ? LYS A 172 VAL A 179 
AA2 5 GLY A 159 ? SER A 166 ? GLY A 159 SER A 166 
AA3 1 TYR A 89  ? ASP A 90  ? TYR A 89  ASP A 90  
AA3 2 LYS A 95  ? ILE A 96  ? LYS A 95  ILE A 96  
AA4 1 THR A 145 ? VAL A 146 ? THR A 145 VAL A 146 
AA4 2 SER A 156 ? PRO A 157 ? SER A 156 PRO A 157 
AA5 1 ILE A 192 ? ALA A 194 ? ILE A 192 ALA A 194 
AA5 2 ASP A 184 ? ARG A 186 ? ASP A 184 ARG A 186 
AA5 3 ILE A 258 ? CYS A 259 ? ILE A 258 CYS A 259 
AA6 1 ILE B 8   ? ASP B 15  ? ILE B 8   ASP B 15  
AA6 2 THR B 20  ? PHE B 27  ? THR B 20  PHE B 27  
AA6 3 GLY B 61  ? THR B 65  ? GLY B 61  THR B 65  
AA6 4 ALA B 101 ? VAL B 103 ? ALA B 101 VAL B 103 
AA6 5 THR B 44  ? ILE B 45  ? THR B 44  ILE B 45  
AA7 1 VAL B 31  ? VAL B 37  ? VAL B 31  VAL B 37  
AA7 2 THR B 269 ? LEU B 275 ? THR B 269 LEU B 275 
AA7 3 THR B 228 ? ARG B 237 ? THR B 228 ARG B 237 
AA7 4 LYS B 172 ? VAL B 179 ? LYS B 172 VAL B 179 
AA7 5 GLY B 159 ? SER B 166 ? GLY B 159 SER B 166 
AA8 1 TYR B 89  ? ASP B 90  ? TYR B 89  ASP B 90  
AA8 2 LYS B 95  ? ILE B 96  ? LYS B 95  ILE B 96  
AA9 1 THR B 145 ? VAL B 146 ? THR B 145 VAL B 146 
AA9 2 SER B 156 ? PRO B 157 ? SER B 156 PRO B 157 
AB1 1 ILE B 192 ? ALA B 194 ? ILE B 192 ALA B 194 
AB1 2 ASP B 184 ? ARG B 186 ? ASP B 184 ARG B 186 
AB1 3 ILE B 258 ? CYS B 259 ? ILE B 258 CYS B 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 A 9   O VAL A 26  ? O VAL A 26  
AA1 2 3 N ALA A 25  ? N ALA A 25  O ILE A 62  ? O ILE A 62  
AA1 3 4 N THR A 65  ? N THR A 65  O ALA A 102 ? O ALA A 102 
AA1 4 5 O ALA A 101 ? O ALA A 101 N ILE A 45  ? N ILE A 45  
AA2 1 2 N VAL A 32  ? N VAL A 32  O GLY A 274 ? O GLY A 274 
AA2 2 3 O PHE A 271 ? O PHE A 271 N VAL A 232 ? N VAL A 232 
AA2 3 4 O ILE A 229 ? O ILE A 229 N VAL A 178 ? N VAL A 178 
AA2 4 5 O VAL A 173 ? O VAL A 173 N VAL A 165 ? N VAL A 165 
AA3 1 2 N TYR A 89  ? N TYR A 89  O ILE A 96  ? O ILE A 96  
AA4 1 2 N VAL A 146 ? N VAL A 146 O SER A 156 ? O SER A 156 
AA5 1 2 O ALA A 194 ? O ALA A 194 N LEU A 185 ? N LEU A 185 
AA5 2 3 N ASP A 184 ? N ASP A 184 O CYS A 259 ? O CYS A 259 
AA6 1 2 N ARG B 9   ? N ARG B 9   O VAL B 26  ? O VAL B 26  
AA6 2 3 N ALA B 25  ? N ALA B 25  O ILE B 62  ? O ILE B 62  
AA6 3 4 N THR B 65  ? N THR B 65  O ALA B 102 ? O ALA B 102 
AA6 4 5 O ALA B 101 ? O ALA B 101 N ILE B 45  ? N ILE B 45  
AA7 1 2 N VAL B 32  ? N VAL B 32  O GLY B 274 ? O GLY B 274 
AA7 2 3 O PHE B 271 ? O PHE B 271 N VAL B 232 ? N VAL B 232 
AA7 3 4 O ILE B 229 ? O ILE B 229 N VAL B 178 ? N VAL B 178 
AA7 4 5 O VAL B 173 ? O VAL B 173 N VAL B 165 ? N VAL B 165 
AA8 1 2 N TYR B 89  ? N TYR B 89  O ILE B 96  ? O ILE B 96  
AA9 1 2 N VAL B 146 ? N VAL B 146 O SER B 156 ? O SER B 156 
AB1 1 2 O ALA B 194 ? O ALA B 194 N LEU B 185 ? N LEU B 185 
AB1 2 3 N ASP B 184 ? N ASP B 184 O CYS B 259 ? O CYS B 259 
# 
_pdbx_entry_details.entry_id                   9DYS 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  B SER 244 ? ? O B HOH 501 ? ? 1.82 
2 1 NH1 A ARG 17  ? ? O A HOH 501 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 19  ? B SD A MET 19  ? B CE  A MET 19  ? B 111.45 100.20 11.25  1.60 N 
2 1 NE A ARG 122 ? ? CZ A ARG 122 ? ? NH1 A ARG 122 ? ? 125.18 120.30 4.88   0.50 N 
3 1 NE A ARG 122 ? ? CZ A ARG 122 ? ? NH2 A ARG 122 ? ? 113.60 120.30 -6.70  0.50 N 
4 1 CD A ARG 123 ? ? NE A ARG 123 ? ? CZ  A ARG 123 ? ? 132.53 123.60 8.93   1.40 N 
5 1 CD A ARG 256 ? ? NE A ARG 256 ? ? CZ  A ARG 256 ? ? 132.60 123.60 9.00   1.40 N 
6 1 N  B VAL 91  ? ? CA B VAL 91  ? ? CB  B VAL 91  ? ? 98.13  111.50 -13.37 2.20 N 
7 1 NE B ARG 122 ? ? CZ B ARG 122 ? ? NH2 B ARG 122 ? ? 116.88 120.30 -3.42  0.50 N 
8 1 CB B ASP 279 ? ? CA B ASP 279 ? ? C   B ASP 279 ? ? 97.75  110.40 -12.65 2.00 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 A 19  ? ? 62.25 62.98   
2 1 MET A 19  ? ? 62.75 62.56   
3 1 SER A 68  ? ? 49.33 -146.17 
4 1 ASP A 205 ? ? 70.49 87.16   
5 1 MET B 19  ? ? 63.78 63.29   
6 1 MET B 19  ? ? 64.04 63.04   
7 1 SER B 68  ? ? 50.94 -144.86 
8 1 ASP B 205 ? ? 72.49 87.87   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 137 ? ? 0.074 'SIDE CHAIN' 
2 1 ARG A 191 ? ? 0.071 'SIDE CHAIN' 
3 1 ARG B 17  ? ? 0.076 'SIDE CHAIN' 
4 1 ARG B 87  ? ? 0.120 'SIDE CHAIN' 
5 1 ARG B 137 ? ? 0.106 'SIDE CHAIN' 
6 1 ARG B 191 ? ? 0.119 'SIDE CHAIN' 
# 
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 A HOH 601 ? G HOH . 
2 1 A HOH 602 ? G HOH . 
3 1 B HOH 600 ? H HOH . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 224 ? A GLY 224 
2 1 Y 1 A MET 225 ? A MET 225 
3 1 Y 1 A ASN 226 ? A ASN 226 
4 1 Y 1 B MET 225 ? B MET 225 
5 1 Y 1 B 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 
PG4 O1   O  N N 261 
PG4 C1   C  N N 262 
PG4 C2   C  N N 263 
PG4 O2   O  N N 264 
PG4 C3   C  N N 265 
PG4 C4   C  N N 266 
PG4 O3   O  N N 267 
PG4 C5   C  N N 268 
PG4 C6   C  N N 269 
PG4 O4   O  N N 270 
PG4 C7   C  N N 271 
PG4 C8   C  N N 272 
PG4 O5   O  N N 273 
PG4 HO1  H  N N 274 
PG4 H11  H  N N 275 
PG4 H12  H  N N 276 
PG4 H21  H  N N 277 
PG4 H22  H  N N 278 
PG4 H31  H  N N 279 
PG4 H32  H  N N 280 
PG4 H41  H  N N 281 
PG4 H42  H  N N 282 
PG4 H51  H  N N 283 
PG4 H52  H  N N 284 
PG4 H61  H  N N 285 
PG4 H62  H  N N 286 
PG4 H71  H  N N 287 
PG4 H72  H  N N 288 
PG4 H81  H  N N 289 
PG4 H82  H  N N 290 
PG4 HO5  H  N N 291 
PHE N    N  N N 292 
PHE CA   C  N S 293 
PHE C    C  N N 294 
PHE O    O  N N 295 
PHE CB   C  N N 296 
PHE CG   C  Y N 297 
PHE CD1  C  Y N 298 
PHE CD2  C  Y N 299 
PHE CE1  C  Y N 300 
PHE CE2  C  Y N 301 
PHE CZ   C  Y N 302 
PHE OXT  O  N N 303 
PHE H    H  N N 304 
PHE H2   H  N N 305 
PHE HA   H  N N 306 
PHE HB2  H  N N 307 
PHE HB3  H  N N 308 
PHE HD1  H  N N 309 
PHE HD2  H  N N 310 
PHE HE1  H  N N 311 
PHE HE2  H  N N 312 
PHE HZ   H  N N 313 
PHE HXT  H  N N 314 
PRO N    N  N N 315 
PRO CA   C  N S 316 
PRO C    C  N N 317 
PRO O    O  N N 318 
PRO CB   C  N N 319 
PRO CG   C  N N 320 
PRO CD   C  N N 321 
PRO OXT  O  N N 322 
PRO H    H  N N 323 
PRO HA   H  N N 324 
PRO HB2  H  N N 325 
PRO HB3  H  N N 326 
PRO HG2  H  N N 327 
PRO HG3  H  N N 328 
PRO HD2  H  N N 329 
PRO HD3  H  N N 330 
PRO HXT  H  N N 331 
SER N    N  N N 332 
SER CA   C  N S 333 
SER C    C  N N 334 
SER O    O  N N 335 
SER CB   C  N N 336 
SER OG   O  N N 337 
SER OXT  O  N N 338 
SER H    H  N N 339 
SER H2   H  N N 340 
SER HA   H  N N 341 
SER HB2  H  N N 342 
SER HB3  H  N N 343 
SER HG   H  N N 344 
SER HXT  H  N N 345 
THR N    N  N N 346 
THR CA   C  N S 347 
THR C    C  N N 348 
THR O    O  N N 349 
THR CB   C  N R 350 
THR OG1  O  N N 351 
THR CG2  C  N N 352 
THR OXT  O  N N 353 
THR H    H  N N 354 
THR H2   H  N N 355 
THR HA   H  N N 356 
THR HB   H  N N 357 
THR HG1  H  N N 358 
THR HG21 H  N N 359 
THR HG22 H  N N 360 
THR HG23 H  N N 361 
THR HXT  H  N N 362 
TYR N    N  N N 363 
TYR CA   C  N S 364 
TYR C    C  N N 365 
TYR O    O  N N 366 
TYR CB   C  N N 367 
TYR CG   C  Y N 368 
TYR CD1  C  Y N 369 
TYR CD2  C  Y N 370 
TYR CE1  C  Y N 371 
TYR CE2  C  Y N 372 
TYR CZ   C  Y N 373 
TYR OH   O  N N 374 
TYR OXT  O  N N 375 
TYR H    H  N N 376 
TYR H2   H  N N 377 
TYR HA   H  N N 378 
TYR HB2  H  N N 379 
TYR HB3  H  N N 380 
TYR HD1  H  N N 381 
TYR HD2  H  N N 382 
TYR HE1  H  N N 383 
TYR HE2  H  N N 384 
TYR HH   H  N N 385 
TYR HXT  H  N N 386 
VAL N    N  N N 387 
VAL CA   C  N S 388 
VAL C    C  N N 389 
VAL O    O  N N 390 
VAL CB   C  N N 391 
VAL CG1  C  N N 392 
VAL CG2  C  N N 393 
VAL OXT  O  N N 394 
VAL H    H  N N 395 
VAL H2   H  N N 396 
VAL HA   H  N N 397 
VAL HB   H  N N 398 
VAL HG11 H  N N 399 
VAL HG12 H  N N 400 
VAL HG13 H  N N 401 
VAL HG21 H  N N 402 
VAL HG22 H  N N 403 
VAL HG23 H  N N 404 
VAL HXT  H  N N 405 
# 
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 
PG4 O1  C1   sing N N 246 
PG4 O1  HO1  sing N N 247 
PG4 C1  C2   sing N N 248 
PG4 C1  H11  sing N N 249 
PG4 C1  H12  sing N N 250 
PG4 C2  O2   sing N N 251 
PG4 C2  H21  sing N N 252 
PG4 C2  H22  sing N N 253 
PG4 O2  C3   sing N N 254 
PG4 C3  C4   sing N N 255 
PG4 C3  H31  sing N N 256 
PG4 C3  H32  sing N N 257 
PG4 C4  O3   sing N N 258 
PG4 C4  H41  sing N N 259 
PG4 C4  H42  sing N N 260 
PG4 O3  C5   sing N N 261 
PG4 C5  C6   sing N N 262 
PG4 C5  H51  sing N N 263 
PG4 C5  H52  sing N N 264 
PG4 C6  O4   sing N N 265 
PG4 C6  H61  sing N N 266 
PG4 C6  H62  sing N N 267 
PG4 O4  C7   sing N N 268 
PG4 C7  C8   sing N N 269 
PG4 C7  H71  sing N N 270 
PG4 C7  H72  sing N N 271 
PG4 C8  O5   sing N N 272 
PG4 C8  H81  sing N N 273 
PG4 C8  H82  sing N N 274 
PG4 O5  HO5  sing N N 275 
PHE N   CA   sing N N 276 
PHE N   H    sing N N 277 
PHE N   H2   sing N N 278 
PHE CA  C    sing N N 279 
PHE CA  CB   sing N N 280 
PHE CA  HA   sing N N 281 
PHE C   O    doub N N 282 
PHE C   OXT  sing N N 283 
PHE CB  CG   sing N N 284 
PHE CB  HB2  sing N N 285 
PHE CB  HB3  sing N N 286 
PHE CG  CD1  doub Y N 287 
PHE CG  CD2  sing Y N 288 
PHE CD1 CE1  sing Y N 289 
PHE CD1 HD1  sing N N 290 
PHE CD2 CE2  doub Y N 291 
PHE CD2 HD2  sing N N 292 
PHE CE1 CZ   doub Y N 293 
PHE CE1 HE1  sing N N 294 
PHE CE2 CZ   sing Y N 295 
PHE CE2 HE2  sing N N 296 
PHE CZ  HZ   sing N N 297 
PHE OXT HXT  sing N N 298 
PRO N   CA   sing N N 299 
PRO N   CD   sing N N 300 
PRO N   H    sing N N 301 
PRO CA  C    sing N N 302 
PRO CA  CB   sing N N 303 
PRO CA  HA   sing N N 304 
PRO C   O    doub N N 305 
PRO C   OXT  sing N N 306 
PRO CB  CG   sing N N 307 
PRO CB  HB2  sing N N 308 
PRO CB  HB3  sing N N 309 
PRO CG  CD   sing N N 310 
PRO CG  HG2  sing N N 311 
PRO CG  HG3  sing N N 312 
PRO CD  HD2  sing N N 313 
PRO CD  HD3  sing N N 314 
PRO OXT HXT  sing N N 315 
SER N   CA   sing N N 316 
SER N   H    sing N N 317 
SER N   H2   sing N N 318 
SER CA  C    sing N N 319 
SER CA  CB   sing N N 320 
SER CA  HA   sing N N 321 
SER C   O    doub N N 322 
SER C   OXT  sing N N 323 
SER CB  OG   sing N N 324 
SER CB  HB2  sing N N 325 
SER CB  HB3  sing N N 326 
SER OG  HG   sing N N 327 
SER OXT HXT  sing N N 328 
THR N   CA   sing N N 329 
THR N   H    sing N N 330 
THR N   H2   sing N N 331 
THR CA  C    sing N N 332 
THR CA  CB   sing N N 333 
THR CA  HA   sing N N 334 
THR C   O    doub N N 335 
THR C   OXT  sing N N 336 
THR CB  OG1  sing N N 337 
THR CB  CG2  sing N N 338 
THR CB  HB   sing N N 339 
THR OG1 HG1  sing N N 340 
THR CG2 HG21 sing N N 341 
THR CG2 HG22 sing N N 342 
THR CG2 HG23 sing N N 343 
THR OXT HXT  sing N N 344 
TYR N   CA   sing N N 345 
TYR N   H    sing N N 346 
TYR N   H2   sing N N 347 
TYR CA  C    sing N N 348 
TYR CA  CB   sing N N 349 
TYR CA  HA   sing N N 350 
TYR C   O    doub N N 351 
TYR C   OXT  sing N N 352 
TYR CB  CG   sing N N 353 
TYR CB  HB2  sing N N 354 
TYR CB  HB3  sing N N 355 
TYR CG  CD1  doub Y N 356 
TYR CG  CD2  sing Y N 357 
TYR CD1 CE1  sing Y N 358 
TYR CD1 HD1  sing N N 359 
TYR CD2 CE2  doub Y N 360 
TYR CD2 HD2  sing N N 361 
TYR CE1 CZ   doub Y N 362 
TYR CE1 HE1  sing N N 363 
TYR CE2 CZ   sing Y N 364 
TYR CE2 HE2  sing N N 365 
TYR CZ  OH   sing N N 366 
TYR OH  HH   sing N N 367 
TYR OXT HXT  sing N N 368 
VAL N   CA   sing N N 369 
VAL N   H    sing N N 370 
VAL N   H2   sing N N 371 
VAL CA  C    sing N N 372 
VAL CA  CB   sing N N 373 
VAL CA  HA   sing N N 374 
VAL C   O    doub N N 375 
VAL C   OXT  sing N N 376 
VAL CB  CG1  sing N N 377 
VAL CB  CG2  sing N N 378 
VAL CB  HB   sing N N 379 
VAL CG1 HG11 sing N N 380 
VAL CG1 HG12 sing N N 381 
VAL CG1 HG13 sing N N 382 
VAL CG2 HG21 sing N N 383 
VAL CG2 HG22 sing N N 384 
VAL CG2 HG23 sing N N 385 
VAL OXT HXT  sing N N 386 
# 
_pdbx_audit_support.funding_organization   'Department of Energy (DOE, United States)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           DE-AC05-00OR22725 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9CXR 
_pdbx_initial_refinement_model.details          'Nyl50 structure solved at a slightly lowe resolution (2.2)' 
# 
_atom_sites.entry_id                    9DYS 
_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]   0.018560 
_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]   0.010362 
_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]   0.009507 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . MET A 1 1   ? 3.185   28.108  -3.606  1.00 17.69  ?  1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 2.771   28.489  -2.229  1.00 17.80  ?  1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 2.241   27.241  -1.535  1.00 16.38  ?  1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 1.119   26.807  -1.800  1.00 18.22  ?  1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 1.727   29.632  -2.229  1.00 19.13  ?  1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 1.669   30.379  -0.876  1.00 19.22  ?  1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 3.147   31.329  -0.493  1.00 24.18  ?  1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 3.106   32.563  -1.794  1.00 24.04  ?  1   MET A CE  1 
ATOM   9    N  N   . LEU A 1 2   ? 3.039   26.693  -0.597  1.00 14.93  ?  2   LEU A N   1 
ATOM   10   C  CA  . LEU A 1 2   ? 2.724   25.407  0.004   1.00 15.53  ?  2   LEU A CA  1 
ATOM   11   C  C   . LEU A 1 2   ? 1.374   25.425  0.715   1.00 16.60  ?  2   LEU A C   1 
ATOM   12   O  O   . LEU A 1 2   ? 0.681   24.401  0.770   1.00 17.13  ?  2   LEU A O   1 
ATOM   13   C  CB  . LEU A 1 2   ? 3.841   25.006  0.971   1.00 16.70  ?  2   LEU A CB  1 
ATOM   14   C  CG  . LEU A 1 2   ? 3.774   23.562  1.461   1.00 17.77  ?  2   LEU A CG  1 
ATOM   15   C  CD1 . LEU A 1 2   ? 4.134   22.616  0.304   1.00 19.79  ?  2   LEU A CD1 1 
ATOM   16   C  CD2 . LEU A 1 2   ? 4.679   23.326  2.626   1.00 19.12  ?  2   LEU A CD2 1 
ATOM   17   N  N   . THR A 1 3   ? 0.996   26.587  1.276   1.00 16.64  ?  3   THR A N   1 
ATOM   18   C  CA  . THR A 1 3   ? -0.294  26.737  1.948   1.00 18.21  ?  3   THR A CA  1 
ATOM   19   C  C   . THR A 1 3   ? -1.508  26.682  1.001   1.00 20.58  ?  3   THR A C   1 
ATOM   20   O  O   . THR A 1 3   ? -2.646  26.758  1.467   1.00 19.83  ?  3   THR A O   1 
ATOM   21   C  CB  . THR A 1 3   ? -0.254  28.033  2.760   1.00 17.56  ?  3   THR A CB  1 
ATOM   22   O  OG1 . THR A 1 3   ? 0.100   29.141  1.930   1.00 16.56  ?  3   THR A OG1 1 
ATOM   23   C  CG2 . THR A 1 3   ? 0.693   27.899  3.938   1.00 16.09  ?  3   THR A CG2 1 
ATOM   24   N  N   . ASP A 1 4   ? -1.294  26.557  -0.315  1.00 19.73  ?  4   ASP A N   1 
ATOM   25   C  CA  . ASP A 1 4   ? -2.365  26.248  -1.246  1.00 20.22  ?  4   ASP A CA  1 
ATOM   26   C  C   . ASP A 1 4   ? -2.988  24.876  -0.976  1.00 22.85  ?  4   ASP A C   1 
ATOM   27   O  O   . ASP A 1 4   ? -4.086  24.573  -1.435  1.00 21.32  ?  4   ASP A O   1 
ATOM   28   C  CB  . ASP A 1 4   ? -1.894  26.332  -2.678  1.00 21.22  ?  4   ASP A CB  1 
ATOM   29   C  CG  . ASP A 1 4   ? -1.604  27.710  -3.237  1.00 22.86  ?  4   ASP A CG  1 
ATOM   30   O  OD1 . ASP A 1 4   ? -1.996  28.704  -2.586  1.00 23.77  ?  4   ASP A OD1 1 
ATOM   31   O  OD2 . ASP A 1 4   ? -0.912  27.788  -4.275  1.00 19.13  -1 4   ASP A OD2 1 
ATOM   32   N  N   . ILE A 1 5   ? -2.273  24.008  -0.260  1.00 22.11  ?  5   ILE A N   1 
ATOM   33   C  CA  . ILE A 1 5   ? -2.738  22.662  0.011   1.00 21.91  ?  5   ILE A CA  1 
ATOM   34   C  C   . ILE A 1 5   ? -3.467  22.683  1.352   1.00 21.51  ?  5   ILE A C   1 
ATOM   35   O  O   . ILE A 1 5   ? -2.989  23.256  2.332   1.00 22.54  ?  5   ILE A O   1 
ATOM   36   C  CB  . ILE A 1 5   ? -1.557  21.668  0.025   1.00 22.38  ?  5   ILE A CB  1 
ATOM   37   C  CG1 . ILE A 1 5   ? -0.702  21.742  -1.258  1.00 21.58  ?  5   ILE A CG1 1 
ATOM   38   C  CG2 . ILE A 1 5   ? -2.043  20.255  0.296   1.00 23.31  ?  5   ILE A CG2 1 
ATOM   39   C  CD1 . ILE A 1 5   ? -1.448  21.439  -2.544  1.00 24.18  ?  5   ILE A CD1 1 
ATOM   40   N  N   . ASP A 1 6   ? -4.613  22.027  1.384   1.00 20.95  ?  6   ASP A N   1 
ATOM   41   C  CA  . ASP A 1 6   ? -5.497  22.030  2.532   1.00 23.42  ?  6   ASP A CA  1 
ATOM   42   C  C   . ASP A 1 6   ? -4.740  21.694  3.809   1.00 23.69  ?  6   ASP A C   1 
ATOM   43   O  O   . ASP A 1 6   ? -4.048  20.660  3.922   1.00 23.67  ?  6   ASP A O   1 
ATOM   44   C  CB  . ASP A 1 6   ? -6.576  20.959  2.436   1.00 29.85  ?  6   ASP A CB  1 
ATOM   45   C  CG  . ASP A 1 6   ? -7.410  20.915  1.160   1.00 35.93  ?  6   ASP A CG  1 
ATOM   46   O  OD1 . ASP A 1 6   ? -6.854  21.187  0.065   1.00 38.24  ?  6   ASP A OD1 1 
ATOM   47   O  OD2 . ASP A 1 6   ? -8.577  20.495  1.266   1.00 44.89  -1 6   ASP A OD2 1 
ATOM   48   N  N   . GLY A 1 7   ? -4.945  22.552  4.805   1.00 20.01  ?  7   GLY A N   1 
ATOM   49   C  CA  . GLY A 1 7   ? -4.560  22.225  6.164   1.00 20.48  ?  7   GLY A CA  1 
ATOM   50   C  C   . GLY A 1 7   ? -3.122  22.623  6.504   1.00 18.81  ?  7   GLY A C   1 
ATOM   51   O  O   . GLY A 1 7   ? -2.728  22.491  7.652   1.00 25.29  ?  7   GLY A O   1 
ATOM   52   N  N   . ILE A 1 8   ? -2.360  23.184  5.573   1.00 17.32  ?  8   ILE A N   1 
ATOM   53   C  CA  . ILE A 1 8   ? -0.966  23.497  5.851   1.00 16.85  ?  8   ILE A CA  1 
ATOM   54   C  C   . ILE A 1 8   ? -0.849  24.946  6.357   1.00 19.07  ?  8   ILE A C   1 
ATOM   55   O  O   . ILE A 1 8   ? -1.386  25.852  5.733   1.00 20.44  ?  8   ILE A O   1 
ATOM   56   C  CB  . ILE A 1 8   ? -0.100  23.253  4.602   1.00 16.43  ?  8   ILE A CB  1 
ATOM   57   C  CG1 . ILE A 1 8   ? -0.181  21.752  4.191   1.00 17.30  ?  8   ILE A CG1 1 
ATOM   58   C  CG2 . ILE A 1 8   ? 1.326   23.727  4.851   1.00 15.80  ?  8   ILE A CG2 1 
ATOM   59   C  CD1 . ILE A 1 8   ? 0.709   21.347  3.025   1.00 17.96  ?  8   ILE A CD1 1 
ATOM   60   N  N   . ARG A 1 9   ? -0.109  25.142  7.452   1.00 17.51  ?  9   ARG A N   1 
ATOM   61   C  CA  . ARG A 1 9   ? 0.357   26.453  7.884   1.00 17.94  ?  9   ARG A CA  1 
ATOM   62   C  C   . ARG A 1 9   ? 1.877   26.452  7.875   1.00 17.99  ?  9   ARG A C   1 
ATOM   63   O  O   . ARG A 1 9   ? 2.481   25.406  8.131   1.00 18.64  ?  9   ARG A O   1 
ATOM   64   C  CB  . ARG A 1 9   ? -0.179  26.760  9.294   1.00 18.19  ?  9   ARG A CB  1 
ATOM   65   C  CG  . ARG A 1 9   ? -1.701  26.893  9.298   1.00 21.38  ?  9   ARG A CG  1 
ATOM   66   C  CD  . ARG A 1 9   ? -2.251  27.323  10.681  1.00 22.17  ?  9   ARG A CD  1 
ATOM   67   N  NE  . ARG A 1 9   ? -2.218  26.199  11.625  1.00 23.63  ?  9   ARG A NE  1 
ATOM   68   C  CZ  . ARG A 1 9   ? -1.515  26.117  12.741  1.00 24.82  ?  9   ARG A CZ  1 
ATOM   69   N  NH1 . ARG A 1 9   ? -0.824  27.148  13.192  1.00 28.37  1  9   ARG A NH1 1 
ATOM   70   N  NH2 . ARG A 1 9   ? -1.522  24.993  13.426  1.00 26.21  ?  9   ARG A NH2 1 
ATOM   71   N  N   . VAL A 1 10  ? 2.480   27.604  7.591   1.00 15.59  ?  10  VAL A N   1 
ATOM   72   C  CA  . VAL A 1 10  ? 3.912   27.745  7.523   1.00 15.86  ?  10  VAL A CA  1 
ATOM   73   C  C   . VAL A 1 10  ? 4.360   28.848  8.481   1.00 17.05  ?  10  VAL A C   1 
ATOM   74   O  O   . VAL A 1 10  ? 3.775   29.928  8.483   1.00 18.38  ?  10  VAL A O   1 
ATOM   75   C  CB  . VAL A 1 10  ? 4.377   28.005  6.080   1.00 15.10  ?  10  VAL A CB  1 
ATOM   76   C  CG1 . VAL A 1 10  ? 5.822   28.438  6.024   1.00 15.30  ?  10  VAL A CG1 1 
ATOM   77   C  CG2 . VAL A 1 10  ? 4.194   26.742  5.242   1.00 16.06  ?  10  VAL A CG2 1 
ATOM   78   N  N   . GLY A 1 11  ? 5.408   28.570  9.262   1.00 15.67  ?  11  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 11  ? 5.981   29.548  10.170  1.00 16.38  ?  11  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 11  ? 7.481   29.611  9.996   1.00 16.62  ?  11  GLY A C   1 
ATOM   81   O  O   . GLY A 1 11  ? 8.118   28.571  9.859   1.00 16.00  ?  11  GLY A O   1 
ATOM   82   N  N   . HIS A 1 12  ? 8.024   30.828  10.011  1.00 15.33  ?  12  HIS A N   1 
ATOM   83   C  CA  . HIS A 1 12  ? 9.462   31.043  10.008  1.00 16.78  ?  12  HIS A CA  1 
ATOM   84   C  C   . HIS A 1 12  ? 9.943   31.577  11.347  1.00 17.83  ?  12  HIS A C   1 
ATOM   85   O  O   . HIS A 1 12  ? 9.203   32.293  12.011  1.00 17.09  ?  12  HIS A O   1 
ATOM   86   C  CB  . HIS A 1 12  ? 9.801   32.103  8.953   1.00 16.76  ?  12  HIS A CB  1 
ATOM   87   C  CG  . HIS A 1 12  ? 9.445   31.790  7.541   1.00 18.87  ?  12  HIS A CG  1 
ATOM   88   N  ND1 . HIS A 1 12  ? 9.793   30.614  6.896   1.00 17.20  ?  12  HIS A ND1 1 
ATOM   89   C  CD2 . HIS A 1 12  ? 8.825   32.557  6.622   1.00 17.57  ?  12  HIS A CD2 1 
ATOM   90   C  CE1 . HIS A 1 12  ? 9.359   30.680  5.640   1.00 17.24  ?  12  HIS A CE1 1 
ATOM   91   N  NE2 . HIS A 1 12  ? 8.744   31.847  5.451   1.00 17.02  ?  12  HIS A NE2 1 
ATOM   92   N  N   . ALA A 1 13  ? 11.193  31.271  11.688  1.00 18.27  ?  13  ALA A N   1 
ATOM   93   C  CA  . ALA A 1 13  ? 11.946  31.988  12.696  1.00 20.37  ?  13  ALA A CA  1 
ATOM   94   C  C   . ALA A 1 13  ? 13.281  32.344  12.074  1.00 22.20  ?  13  ALA A C   1 
ATOM   95   O  O   . ALA A 1 13  ? 13.955  31.502  11.482  1.00 19.91  ?  13  ALA A O   1 
ATOM   96   C  CB  . ALA A 1 13  ? 12.143  31.176  13.956  1.00 20.98  ?  13  ALA A CB  1 
ATOM   97   N  N   . THR A 1 14  ? 13.645  33.628  12.191  1.00 20.33  ?  14  THR A N   1 
ATOM   98   C  CA  . THR A 1 14  ? 14.695  34.216  11.377  1.00 21.71  ?  14  THR A CA  1 
ATOM   99   C  C   . THR A 1 14  ? 15.635  34.967  12.307  1.00 23.35  ?  14  THR A C   1 
ATOM   100  O  O   . THR A 1 14  ? 15.173  35.793  13.079  1.00 23.42  ?  14  THR A O   1 
ATOM   101  C  CB  . THR A 1 14  ? 14.101  35.149  10.320  1.00 22.59  ?  14  THR A CB  1 
ATOM   102  O  OG1 . THR A 1 14  ? 13.224  34.424  9.467   1.00 21.78  ?  14  THR A OG1 1 
ATOM   103  C  CG2 . THR A 1 14  ? 15.170  35.863  9.512   1.00 22.43  ?  14  THR A CG2 1 
ATOM   104  N  N   . ASP A 1 15  ? 16.929  34.684  12.223  1.00 23.71  ?  15  ASP A N   1 
ATOM   105  C  CA  . ASP A 1 15  ? 17.943  35.505  12.859  1.00 23.21  ?  15  ASP A CA  1 
ATOM   106  C  C   . ASP A 1 15  ? 18.829  36.084  11.765  1.00 23.94  ?  15  ASP A C   1 
ATOM   107  O  O   . ASP A 1 15  ? 19.778  35.437  11.303  1.00 22.51  ?  15  ASP A O   1 
ATOM   108  C  CB  . ASP A 1 15  ? 18.713  34.759  13.929  1.00 23.12  ?  15  ASP A CB  1 
ATOM   109  C  CG  . ASP A 1 15  ? 19.735  35.604  14.704  1.00 25.35  ?  15  ASP A CG  1 
ATOM   110  O  OD1 . ASP A 1 15  ? 20.175  36.655  14.182  1.00 24.04  ?  15  ASP A OD1 1 
ATOM   111  O  OD2 . ASP A 1 15  ? 20.120  35.184  15.811  1.00 26.41  -1 15  ASP A OD2 1 
ATOM   112  N  N   . ALA A 1 16  ? 18.527  37.344  11.403  1.00 26.83  ?  16  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 16  ? 19.177  38.043  10.300  1.00 29.19  ?  16  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 16  ? 20.605  38.476  10.621  1.00 28.32  ?  16  ALA A C   1 
ATOM   115  O  O   . ALA A 1 16  ? 21.406  38.607  9.701   1.00 33.69  ?  16  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 16  ? 18.329  39.213  9.853   1.00 33.67  ?  16  ALA A CB  1 
ATOM   117  N  N   . ARG A 1 17  ? 20.975  38.559  11.905  1.00 28.17  ?  17  ARG A N   1 
ATOM   118  C  CA  . ARG A 1 17  ? 22.333  38.895  12.299  1.00 27.66  ?  17  ARG A CA  1 
ATOM   119  C  C   . ARG A 1 17  ? 23.233  37.659  12.249  1.00 24.78  ?  17  ARG A C   1 
ATOM   120  O  O   . ARG A 1 17  ? 24.337  37.693  11.695  1.00 25.64  ?  17  ARG A O   1 
ATOM   121  C  CB  . ARG A 1 17  ? 22.368  39.480  13.726  1.00 34.25  ?  17  ARG A CB  1 
ATOM   122  C  CG  . ARG A 1 17  ? 23.724  40.064  14.147  1.00 43.43  ?  17  ARG A CG  1 
ATOM   123  C  CD  . ARG A 1 17  ? 24.188  39.843  15.610  1.00 48.99  ?  17  ARG A CD  1 
ATOM   124  N  NE  . ARG A 1 17  ? 24.995  38.643  15.909  1.00 55.63  ?  17  ARG A NE  1 
ATOM   125  C  CZ  . ARG A 1 17  ? 24.695  37.700  16.822  1.00 59.39  ?  17  ARG A CZ  1 
ATOM   126  N  NH1 . ARG A 1 17  ? 23.577  37.792  17.527  1.00 70.53  1  17  ARG A NH1 1 
ATOM   127  N  NH2 . ARG A 1 17  ? 25.502  36.677  17.044  1.00 52.68  ?  17  ARG A NH2 1 
ATOM   128  N  N   . ALA A 1 18  ? 22.796  36.549  12.876  1.00 24.24  ?  18  ALA A N   1 
ATOM   129  C  CA  . ALA A 1 18  ? 23.571  35.315  12.830  1.00 21.68  ?  18  ALA A CA  1 
ATOM   130  C  C   . ALA A 1 18  ? 23.476  34.630  11.458  1.00 19.54  ?  18  ALA A C   1 
ATOM   131  O  O   . ALA A 1 18  ? 24.315  33.783  11.153  1.00 21.20  ?  18  ALA A O   1 
ATOM   132  C  CB  . ALA A 1 18  ? 23.091  34.392  13.932  1.00 25.11  ?  18  ALA A CB  1 
ATOM   133  N  N   . MET A 1 19  ? 22.467  34.990  10.664  1.00 18.69  ?  19  MET A N   1 
ATOM   134  C  CA  A MET A 1 19  ? 22.229  34.406  9.351   0.50 19.26  ?  19  MET A CA  1 
ATOM   135  C  CA  B MET A 1 19  ? 22.236  34.405  9.348   0.50 20.78  ?  19  MET A CA  1 
ATOM   136  C  C   . MET A 1 19  ? 21.944  32.906  9.506   1.00 18.44  ?  19  MET A C   1 
ATOM   137  O  O   . MET A 1 19  ? 22.717  32.046  9.041   1.00 18.08  ?  19  MET A O   1 
ATOM   138  C  CB  A MET A 1 19  ? 23.390  34.691  8.390   0.50 19.83  ?  19  MET A CB  1 
ATOM   139  C  CB  B MET A 1 19  ? 23.415  34.636  8.389   0.50 23.71  ?  19  MET A CB  1 
ATOM   140  C  CG  A MET A 1 19  ? 23.566  36.186  8.107   0.50 21.25  ?  19  MET A CG  1 
ATOM   141  C  CG  B MET A 1 19  ? 23.708  36.098  8.069   0.50 28.15  ?  19  MET A CG  1 
ATOM   142  S  SD  A MET A 1 19  ? 24.808  36.546  6.857   0.50 21.08  ?  19  MET A SD  1 
ATOM   143  S  SD  B MET A 1 19  ? 22.295  36.910  7.310   0.50 33.53  ?  19  MET A SD  1 
ATOM   144  C  CE  A MET A 1 19  ? 23.842  36.254  5.376   0.50 23.47  ?  19  MET A CE  1 
ATOM   145  C  CE  B MET A 1 19  ? 21.962  36.253  5.669   0.50 32.46  ?  19  MET A CE  1 
ATOM   146  N  N   . THR A 1 20  ? 20.843  32.618  10.207  1.00 18.88  ?  20  THR A N   1 
ATOM   147  C  CA  . THR A 1 20  ? 20.326  31.278  10.361  1.00 17.89  ?  20  THR A CA  1 
ATOM   148  C  C   . THR A 1 20  ? 18.856  31.414  10.693  1.00 16.61  ?  20  THR A C   1 
ATOM   149  O  O   . THR A 1 20  ? 18.375  32.501  10.982  1.00 17.39  ?  20  THR A O   1 
ATOM   150  C  CB  . THR A 1 20  ? 21.087  30.477  11.426  1.00 17.58  ?  20  THR A CB  1 
ATOM   151  O  OG1 . THR A 1 20  ? 20.790  29.088  11.264  1.00 17.70  ?  20  THR A OG1 1 
ATOM   152  C  CG2 . THR A 1 20  ? 20.709  30.869  12.837  1.00 19.16  ?  20  THR A CG2 1 
ATOM   153  N  N   . GLY A 1 21  ? 18.162  30.270  10.696  1.00 16.37  ?  21  GLY A N   1 
ATOM   154  C  CA  . GLY A 1 21  ? 16.751  30.208  11.003  1.00 15.48  ?  21  GLY A CA  1 
ATOM   155  C  C   . GLY A 1 21  ? 16.195  28.818  10.704  1.00 14.83  ?  21  GLY A C   1 
ATOM   156  O  O   . GLY A 1 21  ? 16.952  27.923  10.317  1.00 15.92  ?  21  GLY A O   1 
ATOM   157  N  N   . CYS A 1 22  ? 14.874  28.685  10.838  1.00 14.69  ?  22  CYS A N   1 
ATOM   158  C  CA  . CYS A 1 22  ? 14.185  27.444  10.566  1.00 15.31  ?  22  CYS A CA  1 
ATOM   159  C  C   . CYS A 1 22  ? 12.762  27.784  10.138  1.00 15.42  ?  22  CYS A C   1 
ATOM   160  O  O   . CYS A 1 22  ? 12.240  28.876  10.414  1.00 16.41  ?  22  CYS A O   1 
ATOM   161  C  CB  . CYS A 1 22  ? 14.229  26.504  11.770  1.00 16.46  ?  22  CYS A CB  1 
ATOM   162  S  SG  . CYS A 1 22  ? 13.450  27.183  13.268  1.00 19.25  ?  22  CYS A SG  1 
ATOM   163  N  N   . THR A 1 23  ? 12.179  26.856  9.378   1.00 14.39  ?  23  THR A N   1 
ATOM   164  C  CA  . THR A 1 23  ? 10.833  26.959  8.850   1.00 14.06  ?  23  THR A CA  1 
ATOM   165  C  C   . THR A 1 23  ? 10.070  25.668  9.171   1.00 15.03  ?  23  THR A C   1 
ATOM   166  O  O   . THR A 1 23  ? 10.607  24.572  8.971   1.00 14.05  ?  23  THR A O   1 
ATOM   167  C  CB  . THR A 1 23  ? 10.913  27.196  7.342   1.00 14.41  ?  23  THR A CB  1 
ATOM   168  O  OG1 . THR A 1 23  ? 11.553  28.437  7.072   1.00 15.42  ?  23  THR A OG1 1 
ATOM   169  C  CG2 . THR A 1 23  ? 9.541   27.169  6.698   1.00 15.11  ?  23  THR A CG2 1 
ATOM   170  N  N   . ILE A 1 24  ? 8.808   25.786  9.613   1.00 16.35  ?  24  ILE A N   1 
ATOM   171  C  CA  . ILE A 1 24  ? 8.013   24.603  9.850   1.00 16.25  ?  24  ILE A CA  1 
ATOM   172  C  C   . ILE A 1 24  ? 6.750   24.653  9.005   1.00 16.55  ?  24  ILE A C   1 
ATOM   173  O  O   . ILE A 1 24  ? 6.155   25.722  8.820   1.00 16.99  ?  24  ILE A O   1 
ATOM   174  C  CB  . ILE A 1 24  ? 7.707   24.374  11.344  1.00 16.08  ?  24  ILE A CB  1 
ATOM   175  C  CG1 . ILE A 1 24  ? 7.076   22.988  11.511  1.00 16.40  ?  24  ILE A CG1 1 
ATOM   176  C  CG2 . ILE A 1 24  ? 6.836   25.481  11.920  1.00 18.15  ?  24  ILE A CG2 1 
ATOM   177  C  CD1 . ILE A 1 24  ? 7.149   22.427  12.893  1.00 19.41  ?  24  ILE A CD1 1 
ATOM   178  N  N   . ALA A 1 25  ? 6.424   23.504  8.395   1.00 13.16  ?  25  ALA A N   1 
ATOM   179  C  CA  . ALA A 1 25  ? 5.128   23.254  7.819   1.00 14.51  ?  25  ALA A CA  1 
ATOM   180  C  C   . ALA A 1 25  ? 4.297   22.459  8.828   1.00 16.22  ?  25  ALA A C   1 
ATOM   181  O  O   . ALA A 1 25  ? 4.668   21.356  9.229   1.00 15.53  ?  25  ALA A O   1 
ATOM   182  C  CB  . ALA A 1 25  ? 5.270   22.486  6.506   1.00 16.64  ?  25  ALA A CB  1 
ATOM   183  N  N   . VAL A 1 26  ? 3.153   23.009  9.229   1.00 15.37  ?  26  VAL A N   1 
ATOM   184  C  CA  . VAL A 1 26  ? 2.297   22.395  10.229  1.00 15.74  ?  26  VAL A CA  1 
ATOM   185  C  C   . VAL A 1 26  ? 1.079   21.806  9.518   1.00 15.46  ?  26  VAL A C   1 
ATOM   186  O  O   . VAL A 1 26  ? 0.507   22.456  8.653   1.00 16.81  ?  26  VAL A O   1 
ATOM   187  C  CB  . VAL A 1 26  ? 1.898   23.392  11.331  1.00 17.56  ?  26  VAL A CB  1 
ATOM   188  C  CG1 . VAL A 1 26  ? 1.043   22.695  12.366  1.00 18.39  ?  26  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A 1 26  ? 3.103   24.044  11.976  1.00 18.44  ?  26  VAL A CG2 1 
ATOM   190  N  N   . PHE A 1 27  ? 0.704   20.556  9.865   1.00 15.56  ?  27  PHE A N   1 
ATOM   191  C  CA  . PHE A 1 27  ? -0.368  19.867  9.169   1.00 17.34  ?  27  PHE A CA  1 
ATOM   192  C  C   . PHE A 1 27  ? -1.607  19.776  10.059  1.00 20.60  ?  27  PHE A C   1 
ATOM   193  O  O   . PHE A 1 27  ? -1.624  18.984  10.984  1.00 20.51  ?  27  PHE A O   1 
ATOM   194  C  CB  . PHE A 1 27  ? 0.019   18.458  8.688   1.00 18.31  ?  27  PHE A CB  1 
ATOM   195  C  CG  . PHE A 1 27  ? 1.259   18.495  7.819   1.00 17.54  ?  27  PHE A CG  1 
ATOM   196  C  CD1 . PHE A 1 27  ? 1.185   18.939  6.509   1.00 19.60  ?  27  PHE A CD1 1 
ATOM   197  C  CD2 . PHE A 1 27  ? 2.475   18.044  8.289   1.00 21.14  ?  27  PHE A CD2 1 
ATOM   198  C  CE1 . PHE A 1 27  ? 2.308   19.014  5.723   1.00 21.08  ?  27  PHE A CE1 1 
ATOM   199  C  CE2 . PHE A 1 27  ? 3.594   18.140  7.487   1.00 21.57  ?  27  PHE A CE2 1 
ATOM   200  C  CZ  . PHE A 1 27  ? 3.506   18.659  6.232   1.00 21.71  ?  27  PHE A CZ  1 
ATOM   201  N  N   . ASP A 1 28  ? -2.626  20.593  9.761   1.00 19.12  ?  28  ASP A N   1 
ATOM   202  C  CA  . ASP A 1 28  ? -3.857  20.632  10.532  1.00 22.01  ?  28  ASP A CA  1 
ATOM   203  C  C   . ASP A 1 28  ? -4.816  19.549  10.043  1.00 25.65  ?  28  ASP A C   1 
ATOM   204  O  O   . ASP A 1 28  ? -5.724  19.171  10.786  1.00 24.36  ?  28  ASP A O   1 
ATOM   205  C  CB  . ASP A 1 28  ? -4.501  22.011  10.478  1.00 23.78  ?  28  ASP A CB  1 
ATOM   206  C  CG  . ASP A 1 28  ? -3.780  23.074  11.296  1.00 24.09  ?  28  ASP A CG  1 
ATOM   207  O  OD1 . ASP A 1 28  ? -3.011  22.719  12.218  1.00 21.42  ?  28  ASP A OD1 1 
ATOM   208  O  OD2 . ASP A 1 28  ? -3.953  24.253  10.979  1.00 29.43  -1 28  ASP A OD2 1 
ATOM   209  N  N   . GLU A 1 29  ? -4.633  19.068  8.812   1.00 21.03  ?  29  GLU A N   1 
ATOM   210  C  CA  . GLU A 1 29  ? -5.324  17.879  8.326   1.00 26.64  ?  29  GLU A CA  1 
ATOM   211  C  C   . GLU A 1 29  ? -4.324  16.729  8.253   1.00 25.78  ?  29  GLU A C   1 
ATOM   212  O  O   . GLU A 1 29  ? -3.204  16.933  7.787   1.00 24.38  ?  29  GLU A O   1 
ATOM   213  C  CB  . GLU A 1 29  ? -5.859  18.086  6.907   1.00 30.75  ?  29  GLU A CB  1 
ATOM   214  C  CG  . GLU A 1 29  ? -7.176  18.865  6.851   1.00 45.00  ?  29  GLU A CG  1 
ATOM   215  C  CD  . GLU A 1 29  ? -8.344  17.898  7.009   1.00 51.52  ?  29  GLU A CD  1 
ATOM   216  O  OE1 . GLU A 1 29  ? -8.412  16.989  6.129   1.00 61.39  ?  29  GLU A OE1 1 
ATOM   217  O  OE2 . GLU A 1 29  ? -9.089  17.963  8.022   1.00 55.78  -1 29  GLU A OE2 1 
ATOM   218  N  N   . PRO A 1 30  ? -4.680  15.508  8.693   1.00 24.60  ?  30  PRO A N   1 
ATOM   219  C  CA  . PRO A 1 30  ? -3.726  14.400  8.704   1.00 22.97  ?  30  PRO A CA  1 
ATOM   220  C  C   . PRO A 1 30  ? -3.152  14.061  7.320   1.00 18.38  ?  30  PRO A C   1 
ATOM   221  O  O   . PRO A 1 30  ? -3.875  14.071  6.322   1.00 18.03  ?  30  PRO A O   1 
ATOM   222  C  CB  . PRO A 1 30  ? -4.508  13.203  9.239   1.00 25.38  ?  30  PRO A CB  1 
ATOM   223  C  CG  . PRO A 1 30  ? -5.845  13.764  9.724   1.00 27.38  ?  30  PRO A CG  1 
ATOM   224  C  CD  . PRO A 1 30  ? -6.015  15.149  9.199   1.00 25.86  ?  30  PRO A CD  1 
ATOM   225  N  N   . VAL A 1 31  ? -1.836  13.785  7.281   1.00 16.97  ?  31  VAL A N   1 
ATOM   226  C  CA  . VAL A 1 31  ? -1.138  13.510  6.042   1.00 16.52  ?  31  VAL A CA  1 
ATOM   227  C  C   . VAL A 1 31  ? -0.567  12.096  6.025   1.00 16.90  ?  31  VAL A C   1 
ATOM   228  O  O   . VAL A 1 31  ? -0.383  11.437  7.064   1.00 17.41  ?  31  VAL A O   1 
ATOM   229  C  CB  . VAL A 1 31  ? -0.032  14.550  5.781   1.00 16.88  ?  31  VAL A CB  1 
ATOM   230  C  CG1 . VAL A 1 31  ? -0.610  15.938  5.524   1.00 18.41  ?  31  VAL A CG1 1 
ATOM   231  C  CG2 . VAL A 1 31  ? 1.005   14.615  6.881   1.00 18.24  ?  31  VAL A CG2 1 
ATOM   232  N  N   . VAL A 1 32  ? -0.274  11.651  4.798   1.00 16.31  ?  32  VAL A N   1 
ATOM   233  C  CA  . VAL A 1 32  ? 0.462   10.418  4.528   1.00 16.64  ?  32  VAL A CA  1 
ATOM   234  C  C   . VAL A 1 32  ? 1.850   10.820  4.032   1.00 16.22  ?  32  VAL A C   1 
ATOM   235  O  O   . VAL A 1 32  ? 1.978   11.487  2.995   1.00 16.97  ?  32  VAL A O   1 
ATOM   236  C  CB  . VAL A 1 32  ? -0.253  9.589   3.451   1.00 19.43  ?  32  VAL A CB  1 
ATOM   237  C  CG1 . VAL A 1 32  ? 0.527   8.320   3.106   1.00 21.41  ?  32  VAL A CG1 1 
ATOM   238  C  CG2 . VAL A 1 32  ? -1.683  9.237   3.855   1.00 19.74  ?  32  VAL A CG2 1 
ATOM   239  N  N   . PRO A 1 33  ? 2.931   10.453  4.736   1.00 14.90  ?  33  PRO A N   1 
ATOM   240  C  CA  . PRO A 1 33  ? 4.246   10.966  4.390   1.00 14.80  ?  33  PRO A CA  1 
ATOM   241  C  C   . PRO A 1 33  ? 5.180   9.973   3.713   1.00 15.83  ?  33  PRO A C   1 
ATOM   242  O  O   . PRO A 1 33  ? 5.044   8.760   3.857   1.00 15.44  ?  33  PRO A O   1 
ATOM   243  C  CB  . PRO A 1 33  ? 4.788   11.293  5.756   1.00 16.05  ?  33  PRO A CB  1 
ATOM   244  C  CG  . PRO A 1 33  ? 4.266   10.122  6.578   1.00 16.30  ?  33  PRO A CG  1 
ATOM   245  C  CD  . PRO A 1 33  ? 2.941   9.732   6.014   1.00 14.98  ?  33  PRO A CD  1 
ATOM   246  N  N   . GLY A 1 34  ? 6.166   10.543  3.024   1.00 13.97  ?  34  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 34  ? 7.236   9.806   2.395   1.00 13.13  ?  34  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 34  ? 8.489   10.663  2.386   1.00 13.01  ?  34  GLY A C   1 
ATOM   249  O  O   . GLY A 1 34  ? 8.439   11.876  2.634   1.00 11.95  ?  34  GLY A O   1 
ATOM   250  N  N   . VAL A 1 35  ? 9.627   10.038  2.076   1.00 13.62  ?  35  VAL A N   1 
ATOM   251  C  CA  . VAL A 1 35  ? 10.869  10.779  2.061   1.00 11.80  ?  35  VAL A CA  1 
ATOM   252  C  C   . VAL A 1 35  ? 11.836  10.108  1.092   1.00 12.59  ?  35  VAL A C   1 
ATOM   253  O  O   . VAL A 1 35  ? 11.765  8.894   0.833   1.00 12.01  ?  35  VAL A O   1 
ATOM   254  C  CB  . VAL A 1 35  ? 11.442  10.846  3.484   1.00 12.44  ?  35  VAL A CB  1 
ATOM   255  C  CG1 . VAL A 1 35  ? 11.889  9.462   3.972   1.00 14.18  ?  35  VAL A CG1 1 
ATOM   256  C  CG2 . VAL A 1 35  ? 12.608  11.828  3.583   1.00 12.97  ?  35  VAL A CG2 1 
ATOM   257  N  N   . ASP A 1 36  ? 12.749  10.911  0.541   1.00 12.01  ?  36  ASP A N   1 
ATOM   258  C  CA  . ASP A 1 36  ? 13.880  10.396  -0.230  1.00 12.90  ?  36  ASP A CA  1 
ATOM   259  C  C   . ASP A 1 36  ? 15.093  11.253  0.091   1.00 12.35  ?  36  ASP A C   1 
ATOM   260  O  O   . ASP A 1 36  ? 15.111  12.456  -0.208  1.00 12.42  ?  36  ASP A O   1 
ATOM   261  C  CB  . ASP A 1 36  ? 13.600  10.369  -1.727  1.00 14.11  ?  36  ASP A CB  1 
ATOM   262  C  CG  . ASP A 1 36  ? 14.718  9.760   -2.586  1.00 18.32  ?  36  ASP A CG  1 
ATOM   263  O  OD1 . ASP A 1 36  ? 15.884  9.907   -2.221  1.00 19.66  ?  36  ASP A OD1 1 
ATOM   264  O  OD2 . ASP A 1 36  ? 14.431  9.231   -3.653  1.00 18.81  -1 36  ASP A OD2 1 
ATOM   265  N  N   . VAL A 1 37  ? 16.019  10.652  0.826   1.00 13.29  ?  37  VAL A N   1 
ATOM   266  C  CA  . VAL A 1 37  ? 17.287  11.250  1.166   1.00 13.46  ?  37  VAL A CA  1 
ATOM   267  C  C   . VAL A 1 37  ? 18.295  10.839  0.101   1.00 15.00  ?  37  VAL A C   1 
ATOM   268  O  O   . VAL A 1 37  ? 18.716  9.702   0.055   1.00 15.31  ?  37  VAL A O   1 
ATOM   269  C  CB  . VAL A 1 37  ? 17.818  10.832  2.545   1.00 15.89  ?  37  VAL A CB  1 
ATOM   270  C  CG1 . VAL A 1 37  ? 19.152  11.506  2.829   1.00 16.22  ?  37  VAL A CG1 1 
ATOM   271  C  CG2 . VAL A 1 37  ? 16.814  11.094  3.646   1.00 16.24  ?  37  VAL A CG2 1 
ATOM   272  N  N   . ARG A 1 38  ? 18.670  11.752  -0.779  1.00 13.76  ?  38  ARG A N   1 
ATOM   273  C  CA  . ARG A 1 38  ? 19.513  11.395  -1.911  1.00 15.70  ?  38  ARG A CA  1 
ATOM   274  C  C   . ARG A 1 38  ? 20.935  11.915  -1.777  1.00 16.45  ?  38  ARG A C   1 
ATOM   275  O  O   . ARG A 1 38  ? 21.864  11.370  -2.395  1.00 17.79  ?  38  ARG A O   1 
ATOM   276  C  CB  . ARG A 1 38  ? 18.865  11.948  -3.178  1.00 15.52  ?  38  ARG A CB  1 
ATOM   277  C  CG  . ARG A 1 38  ? 19.476  11.403  -4.444  1.00 18.70  ?  38  ARG A CG  1 
ATOM   278  C  CD  . ARG A 1 38  ? 19.053  10.007  -4.737  1.00 20.13  ?  38  ARG A CD  1 
ATOM   279  N  NE  . ARG A 1 38  ? 17.609  9.911   -5.004  1.00 17.47  ?  38  ARG A NE  1 
ATOM   280  C  CZ  . ARG A 1 38  ? 16.946  10.257  -6.091  1.00 19.17  ?  38  ARG A CZ  1 
ATOM   281  N  NH1 . ARG A 1 38  ? 17.558  10.676  -7.184  1.00 20.52  1  38  ARG A NH1 1 
ATOM   282  N  NH2 . ARG A 1 38  ? 15.636  10.143  -6.125  1.00 19.44  ?  38  ARG A NH2 1 
ATOM   283  N  N   . GLY A 1 39  ? 21.135  13.010  -1.036  1.00 15.73  ?  39  GLY A N   1 
ATOM   284  C  CA  . GLY A 1 39  ? 22.496  13.513  -0.888  1.00 16.79  ?  39  GLY A CA  1 
ATOM   285  C  C   . GLY A 1 39  ? 23.320  12.576  0.004   1.00 17.51  ?  39  GLY A C   1 
ATOM   286  O  O   . GLY A 1 39  ? 22.777  11.762  0.770   1.00 17.64  ?  39  GLY A O   1 
ATOM   287  N  N   . ALA A 1 40  ? 24.640  12.693  -0.091  1.00 15.47  ?  40  ALA A N   1 
ATOM   288  C  CA  . ALA A 1 40  ? 25.547  11.800  0.601   1.00 17.25  ?  40  ALA A CA  1 
ATOM   289  C  C   . ALA A 1 40  ? 25.966  12.371  1.959   1.00 16.60  ?  40  ALA A C   1 
ATOM   290  O  O   . ALA A 1 40  ? 26.705  11.731  2.682   1.00 17.47  ?  40  ALA A O   1 
ATOM   291  C  CB  . ALA A 1 40  ? 26.769  11.534  -0.296  1.00 18.24  ?  40  ALA A CB  1 
ATOM   292  N  N   . ASN A 1 41  ? 25.491  13.565  2.323   1.00 15.43  ?  41  ASN A N   1 
ATOM   293  C  CA  . ASN A 1 41  ? 25.881  14.205  3.569   1.00 16.26  ?  41  ASN A CA  1 
ATOM   294  C  C   . ASN A 1 41  ? 24.665  14.815  4.290   1.00 16.60  ?  41  ASN A C   1 
ATOM   295  O  O   . ASN A 1 41  ? 24.645  16.036  4.511   1.00 21.50  ?  41  ASN A O   1 
ATOM   296  C  CB  . ASN A 1 41  ? 26.934  15.252  3.215   1.00 20.62  ?  41  ASN A CB  1 
ATOM   297  C  CG  . ASN A 1 41  ? 27.772  15.683  4.382   1.00 30.11  ?  41  ASN A CG  1 
ATOM   298  O  OD1 . ASN A 1 41  ? 27.426  15.426  5.530   1.00 27.48  ?  41  ASN A OD1 1 
ATOM   299  N  ND2 . ASN A 1 41  ? 28.910  16.295  4.095   1.00 42.02  ?  41  ASN A ND2 1 
ATOM   300  N  N   . ALA A 1 42  ? 23.618  14.030  4.541   1.00 14.87  ?  42  ALA A N   1 
ATOM   301  C  CA  . ALA A 1 42  ? 22.375  14.517  5.117   1.00 15.64  ?  42  ALA A CA  1 
ATOM   302  C  C   . ALA A 1 42  ? 22.342  14.317  6.634   1.00 18.35  ?  42  ALA A C   1 
ATOM   303  O  O   . ALA A 1 42  ? 22.802  13.290  7.112   1.00 19.72  ?  42  ALA A O   1 
ATOM   304  C  CB  . ALA A 1 42  ? 21.198  13.846  4.467   1.00 15.24  ?  42  ALA A CB  1 
ATOM   305  N  N   . ALA A 1 43  ? 21.755  15.261  7.378   1.00 14.40  ?  43  ALA A N   1 
ATOM   306  C  CA  . ALA A 1 43  ? 21.479  15.070  8.804   1.00 15.09  ?  43  ALA A CA  1 
ATOM   307  C  C   . ALA A 1 43  ? 19.969  15.251  9.016   1.00 13.66  ?  43  ALA A C   1 
ATOM   308  O  O   . ALA A 1 43  ? 19.426  16.299  8.681   1.00 10.53  ?  43  ALA A O   1 
ATOM   309  C  CB  . ALA A 1 43  ? 22.288  16.028  9.652   1.00 16.33  ?  43  ALA A CB  1 
ATOM   310  N  N   . THR A 1 44  ? 19.304  14.172  9.426   1.00 10.90  ?  44  THR A N   1 
ATOM   311  C  CA  . THR A 1 44  ? 17.861  14.176  9.568   1.00 12.35  ?  44  THR A CA  1 
ATOM   312  C  C   . THR A 1 44  ? 17.454  13.563  10.904  1.00 11.23  ?  44  THR A C   1 
ATOM   313  O  O   . THR A 1 44  ? 18.256  12.912  11.570  1.00 11.25  ?  44  THR A O   1 
ATOM   314  C  CB  . THR A 1 44  ? 17.181  13.454  8.397   1.00 13.30  ?  44  THR A CB  1 
ATOM   315  O  OG1 . THR A 1 44  ? 17.410  12.064  8.529   1.00 12.98  ?  44  THR A OG1 1 
ATOM   316  C  CG2 . THR A 1 44  ? 17.669  13.934  7.042   1.00 14.04  ?  44  THR A CG2 1 
ATOM   317  N  N   . ILE A 1 45  ? 16.179  13.741  11.241  1.00 10.85  ?  45  ILE A N   1 
ATOM   318  C  CA  . ILE A 1 45  ? 15.583  13.128  12.421  1.00 12.62  ?  45  ILE A CA  1 
ATOM   319  C  C   . ILE A 1 45  ? 14.193  12.607  12.080  1.00 12.27  ?  45  ILE A C   1 
ATOM   320  O  O   . ILE A 1 45  ? 13.506  13.212  11.266  1.00 12.88  ?  45  ILE A O   1 
ATOM   321  C  CB  . ILE A 1 45  ? 15.540  14.123  13.601  1.00 12.98  ?  45  ILE A CB  1 
ATOM   322  C  CG1 . ILE A 1 45  ? 15.160  13.465  14.908  1.00 14.10  ?  45  ILE A CG1 1 
ATOM   323  C  CG2 . ILE A 1 45  ? 14.647  15.326  13.286  1.00 12.38  ?  45  ILE A CG2 1 
ATOM   324  C  CD1 . ILE A 1 45  ? 15.206  14.393  16.110  1.00 14.74  ?  45  ILE A CD1 1 
ATOM   325  N  N   . TYR A 1 46  ? 13.853  11.440  12.656  1.00 12.34  ?  46  TYR A N   1 
ATOM   326  C  CA  . TYR A 1 46  ? 12.563  10.751  12.540  1.00 13.46  ?  46  TYR A CA  1 
ATOM   327  C  C   . TYR A 1 46  ? 12.241  10.265  11.124  1.00 17.67  ?  46  TYR A C   1 
ATOM   328  O  O   . TYR A 1 46  ? 11.073  10.014  10.827  1.00 22.72  ?  46  TYR A O   1 
ATOM   329  C  CB  . TYR A 1 46  ? 11.409  11.622  13.016  1.00 14.10  ?  46  TYR A CB  1 
ATOM   330  C  CG  . TYR A 1 46  ? 11.501  12.173  14.437  1.00 14.54  ?  46  TYR A CG  1 
ATOM   331  C  CD1 . TYR A 1 46  ? 11.706  11.331  15.534  1.00 14.82  ?  46  TYR A CD1 1 
ATOM   332  C  CD2 . TYR A 1 46  ? 11.339  13.522  14.711  1.00 14.56  ?  46  TYR A CD2 1 
ATOM   333  C  CE1 . TYR A 1 46  ? 11.777  11.814  16.825  1.00 13.29  ?  46  TYR A CE1 1 
ATOM   334  C  CE2 . TYR A 1 46  ? 11.397  14.010  16.001  1.00 14.76  ?  46  TYR A CE2 1 
ATOM   335  C  CZ  . TYR A 1 46  ? 11.607  13.157  17.070  1.00 15.36  ?  46  TYR A CZ  1 
ATOM   336  O  OH  . TYR A 1 46  ? 11.653  13.645  18.350  1.00 16.64  ?  46  TYR A OH  1 
ATOM   337  N  N   . THR A 1 47  ? 13.221  10.112  10.228  1.00 15.28  ?  47  THR A N   1 
ATOM   338  C  CA  . THR A 1 47  ? 12.874  9.714   8.864   1.00 14.98  ?  47  THR A CA  1 
ATOM   339  C  C   . THR A 1 47  ? 12.460  8.234   8.758   1.00 16.00  ?  47  THR A C   1 
ATOM   340  O  O   . THR A 1 47  ? 11.767  7.865   7.817   1.00 12.51  ?  47  THR A O   1 
ATOM   341  C  CB  . THR A 1 47  ? 13.977  10.024  7.864   1.00 15.44  ?  47  THR A CB  1 
ATOM   342  O  OG1 . THR A 1 47  ? 15.135  9.296   8.259   1.00 16.98  ?  47  THR A OG1 1 
ATOM   343  C  CG2 . THR A 1 47  ? 14.177  11.513  7.709   1.00 17.66  ?  47  THR A CG2 1 
ATOM   344  N  N   . ASP A 1 48  ? 12.822  7.365   9.713   1.00 17.71  ?  48  ASP A N   1 
ATOM   345  C  CA  . ASP A 1 48  ? 12.496  5.942   9.572   1.00 19.69  ?  48  ASP A CA  1 
ATOM   346  C  C   . ASP A 1 48  ? 11.004  5.636   9.488   1.00 18.35  ?  48  ASP A C   1 
ATOM   347  O  O   . ASP A 1 48  ? 10.619  4.668   8.827   1.00 17.42  ?  48  ASP A O   1 
ATOM   348  C  CB  . ASP A 1 48  ? 13.103  5.105   10.674  1.00 22.17  ?  48  ASP A CB  1 
ATOM   349  C  CG  . ASP A 1 48  ? 14.629  5.155   10.666  1.00 23.75  ?  48  ASP A CG  1 
ATOM   350  O  OD1 . ASP A 1 48  ? 15.250  4.586   9.687   1.00 20.07  ?  48  ASP A OD1 1 
ATOM   351  O  OD2 . ASP A 1 48  ? 15.133  5.797   11.618  1.00 26.74  -1 48  ASP A OD2 1 
ATOM   352  N  N   . LEU A 1 49  ? 10.185  6.430   10.172  1.00 16.65  ?  49  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 49  ? 8.749   6.256   10.146  1.00 19.59  ?  49  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 49  ? 8.124   6.727   8.843   1.00 19.14  ?  49  LEU A C   1 
ATOM   355  O  O   . LEU A 1 49  ? 6.932   6.550   8.666   1.00 22.00  ?  49  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 49  ? 8.200   7.039   11.339  1.00 25.00  ?  49  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 49  ? 8.481   6.414   12.708  1.00 29.95  ?  49  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 49  ? 8.276   7.379   13.889  1.00 35.53  ?  49  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 49  ? 7.621   5.170   12.804  1.00 31.29  ?  49  LEU A CD2 1 
ATOM   360  N  N   . LEU A 1 50  ? 8.913   7.304   7.933   1.00 16.65  ?  50  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 50  ? 8.383   7.868   6.707   1.00 16.96  ?  50  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 50  ? 8.602   6.917   5.533   1.00 19.00  ?  50  LEU A C   1 
ATOM   363  O  O   . LEU A 1 50  ? 8.411   7.306   4.382   1.00 22.75  ?  50  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 50  ? 9.069   9.207   6.448   1.00 18.44  ?  50  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 50  ? 8.498   10.451  7.119   1.00 22.17  ?  50  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 50  ? 8.001   10.229  8.464   1.00 19.84  ?  50  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 50  ? 9.475   11.635  7.054   1.00 21.42  ?  50  LEU A CD2 1 
ATOM   368  N  N   . TYR A 1 51  ? 9.135   5.726   5.776   1.00 19.01  ?  51  TYR A N   1 
ATOM   369  C  CA  . TYR A 1 51  ? 9.318   4.798   4.666   1.00 18.88  ?  51  TYR A CA  1 
ATOM   370  C  C   . TYR A 1 51  ? 8.117   3.872   4.583   1.00 17.31  ?  51  TYR A C   1 
ATOM   371  O  O   . TYR A 1 51  ? 7.439   3.685   5.582   1.00 16.69  ?  51  TYR A O   1 
ATOM   372  C  CB  . TYR A 1 51  ? 10.579  3.964   4.894   1.00 20.67  ?  51  TYR A CB  1 
ATOM   373  C  CG  . TYR A 1 51  ? 11.821  4.812   4.714   1.00 20.72  ?  51  TYR A CG  1 
ATOM   374  C  CD1 . TYR A 1 51  ? 12.269  5.144   3.442   1.00 24.32  ?  51  TYR A CD1 1 
ATOM   375  C  CD2 . TYR A 1 51  ? 12.490  5.337   5.804   1.00 21.92  ?  51  TYR A CD2 1 
ATOM   376  C  CE1 . TYR A 1 51  ? 13.385  5.950   3.265   1.00 23.46  ?  51  TYR A CE1 1 
ATOM   377  C  CE2 . TYR A 1 51  ? 13.613  6.126   5.643   1.00 22.98  ?  51  TYR A CE2 1 
ATOM   378  C  CZ  . TYR A 1 51  ? 14.076  6.416   4.369   1.00 24.89  ?  51  TYR A CZ  1 
ATOM   379  O  OH  . TYR A 1 51  ? 15.190  7.180   4.205   1.00 24.22  ?  51  TYR A OH  1 
ATOM   380  N  N   . PRO A 1 52  ? 7.875   3.211   3.424   1.00 19.26  ?  52  PRO A N   1 
ATOM   381  C  CA  . PRO A 1 52  ? 6.655   2.431   3.230   1.00 21.17  ?  52  PRO A CA  1 
ATOM   382  C  C   . PRO A 1 52  ? 6.509   1.228   4.153   1.00 21.54  ?  52  PRO A C   1 
ATOM   383  O  O   . PRO A 1 52  ? 5.387   0.811   4.435   1.00 22.60  ?  52  PRO A O   1 
ATOM   384  C  CB  . PRO A 1 52  ? 6.766   1.935   1.785   1.00 23.18  ?  52  PRO A CB  1 
ATOM   385  C  CG  . PRO A 1 52  ? 7.743   2.894   1.130   1.00 22.62  ?  52  PRO A CG  1 
ATOM   386  C  CD  . PRO A 1 52  ? 8.717   3.265   2.207   1.00 21.81  ?  52  PRO A CD  1 
ATOM   387  N  N   . ASP A 1 53  ? 7.637   0.666   4.597   1.00 21.90  ?  53  ASP A N   1 
ATOM   388  C  CA  . ASP A 1 53  ? 7.586   -0.548  5.417   1.00 25.88  ?  53  ASP A CA  1 
ATOM   389  C  C   . ASP A 1 53  ? 7.496   -0.265  6.914   1.00 25.42  ?  53  ASP A C   1 
ATOM   390  O  O   . ASP A 1 53  ? 7.502   -1.201  7.698   1.00 30.04  ?  53  ASP A O   1 
ATOM   391  C  CB  . ASP A 1 53  ? 8.728   -1.513  5.118   1.00 29.77  ?  53  ASP A CB  1 
ATOM   392  C  CG  . ASP A 1 53  ? 10.114  -0.924  5.219   1.00 34.42  ?  53  ASP A CG  1 
ATOM   393  O  OD1 . ASP A 1 53  ? 10.236  0.323   5.194   1.00 39.62  ?  53  ASP A OD1 1 
ATOM   394  O  OD2 . ASP A 1 53  ? 11.058  -1.715  5.344   1.00 50.42  -1 53  ASP A OD2 1 
ATOM   395  N  N   A SER A 1 54  ? 7.386   1.017   7.302   0.74 21.84  ?  54  SER A N   1 
ATOM   396  N  N   B SER A 1 54  ? 7.396   1.017   7.302   0.26 22.43  ?  54  SER A N   1 
ATOM   397  C  CA  A SER A 1 54  ? 7.158   1.404   8.679   0.74 18.67  ?  54  SER A CA  1 
ATOM   398  C  CA  B SER A 1 54  ? 7.157   1.400   8.682   0.26 19.76  ?  54  SER A CA  1 
ATOM   399  C  C   A SER A 1 54  ? 5.663   1.603   8.876   0.74 17.41  ?  54  SER A C   1 
ATOM   400  C  C   B SER A 1 54  ? 5.659   1.611   8.872   0.26 18.55  ?  54  SER A C   1 
ATOM   401  O  O   A SER A 1 54  ? 4.974   1.831   7.892   0.74 16.61  ?  54  SER A O   1 
ATOM   402  O  O   B SER A 1 54  ? 4.954   1.808   7.888   0.26 18.21  ?  54  SER A O   1 
ATOM   403  C  CB  A SER A 1 54  ? 7.919   2.671   8.977   0.74 19.97  ?  54  SER A CB  1 
ATOM   404  C  CB  B SER A 1 54  ? 7.932   2.648   9.025   0.26 19.78  ?  54  SER A CB  1 
ATOM   405  O  OG  A SER A 1 54  ? 9.308   2.412   9.084   0.74 19.98  ?  54  SER A OG  1 
ATOM   406  O  OG  B SER A 1 54  ? 7.575   3.715   8.165   0.26 18.74  ?  54  SER A OG  1 
ATOM   407  N  N   . VAL A 1 55  ? 5.198   1.610   10.130  1.00 16.96  ?  55  VAL A N   1 
ATOM   408  C  CA  . VAL A 1 55  ? 3.804   1.907   10.442  1.00 19.27  ?  55  VAL A CA  1 
ATOM   409  C  C   . VAL A 1 55  ? 3.454   3.332   10.018  1.00 19.76  ?  55  VAL A C   1 
ATOM   410  O  O   . VAL A 1 55  ? 4.320   4.139   9.695   1.00 19.31  ?  55  VAL A O   1 
ATOM   411  C  CB  . VAL A 1 55  ? 3.504   1.729   11.939  1.00 21.90  ?  55  VAL A CB  1 
ATOM   412  C  CG1 . VAL A 1 55  ? 3.752   0.295   12.382  1.00 23.57  ?  55  VAL A CG1 1 
ATOM   413  C  CG2 . VAL A 1 55  ? 4.300   2.735   12.794  1.00 23.88  ?  55  VAL A CG2 1 
ATOM   414  N  N   . MET A 1 56  ? 2.158   3.652   10.042  1.00 19.69  ?  56  MET A N   1 
ATOM   415  C  CA  . MET A 1 56  ? 1.698   4.959   9.607   1.00 21.58  ?  56  MET A CA  1 
ATOM   416  C  C   . MET A 1 56  ? 1.857   5.868   10.811  1.00 23.10  ?  56  MET A C   1 
ATOM   417  O  O   . MET A 1 56  ? 1.200   5.663   11.832  1.00 23.11  ?  56  MET A O   1 
ATOM   418  C  CB  . MET A 1 56  ? 0.220   4.954   9.184   1.00 23.60  ?  56  MET A CB  1 
ATOM   419  C  CG  . MET A 1 56  ? -0.320  6.343   8.842   1.00 28.61  ?  56  MET A CG  1 
ATOM   420  S  SD  . MET A 1 56  ? 0.300   6.940   7.251   1.00 28.30  ?  56  MET A SD  1 
ATOM   421  C  CE  . MET A 1 56  ? -0.581  5.848   6.126   1.00 34.74  ?  56  MET A CE  1 
ATOM   422  N  N   . PRO A 1 57  ? 2.760   6.858   10.786  1.00 21.87  ?  57  PRO A N   1 
ATOM   423  C  CA  . PRO A 1 57  ? 2.884   7.756   11.927  1.00 22.57  ?  57  PRO A CA  1 
ATOM   424  C  C   . PRO A 1 57  ? 1.872   8.894   11.871  1.00 22.46  ?  57  PRO A C   1 
ATOM   425  O  O   . PRO A 1 57  ? 1.161   9.068   10.876  1.00 21.09  ?  57  PRO A O   1 
ATOM   426  C  CB  . PRO A 1 57  ? 4.303   8.327   11.760  1.00 24.23  ?  57  PRO A CB  1 
ATOM   427  C  CG  . PRO A 1 57  ? 4.444   8.397   10.233  1.00 22.37  ?  57  PRO A CG  1 
ATOM   428  C  CD  . PRO A 1 57  ? 3.629   7.240   9.658   1.00 23.45  ?  57  PRO A CD  1 
ATOM   429  N  N   . SER A 1 58  ? 1.909   9.708   12.914  1.00 24.49  ?  58  SER A N   1 
ATOM   430  C  CA  . SER A 1 58  ? 1.121   10.919  12.995  1.00 26.47  ?  58  SER A CA  1 
ATOM   431  C  C   . SER A 1 58  ? 2.086   12.108  12.946  1.00 22.01  ?  58  SER A C   1 
ATOM   432  O  O   . SER A 1 58  ? 2.584   12.595  13.963  1.00 22.20  ?  58  SER A O   1 
ATOM   433  C  CB  . SER A 1 58  ? 0.225   10.906  14.241  1.00 26.06  ?  58  SER A CB  1 
ATOM   434  O  OG  . SER A 1 58  ? -0.520  12.110  14.229  1.00 28.78  ?  58  SER A OG  1 
ATOM   435  N  N   . VAL A 1 59  ? 2.371   12.558  11.725  1.00 18.37  ?  59  VAL A N   1 
ATOM   436  C  CA  . VAL A 1 59  ? 3.258   13.680  11.495  1.00 18.05  ?  59  VAL A CA  1 
ATOM   437  C  C   . VAL A 1 59  ? 2.547   14.995  11.840  1.00 15.89  ?  59  VAL A C   1 
ATOM   438  O  O   . VAL A 1 59  ? 1.572   15.366  11.195  1.00 16.34  ?  59  VAL A O   1 
ATOM   439  C  CB  . VAL A 1 59  ? 3.759   13.651  10.039  1.00 20.28  ?  59  VAL A CB  1 
ATOM   440  C  CG1 . VAL A 1 59  ? 4.608   14.863  9.713   1.00 20.09  ?  59  VAL A CG1 1 
ATOM   441  C  CG2 . VAL A 1 59  ? 4.535   12.377  9.718   1.00 22.16  ?  59  VAL A CG2 1 
ATOM   442  N  N   . THR A 1 60  ? 3.091   15.714  12.815  1.00 15.57  ?  60  THR A N   1 
ATOM   443  C  CA  . THR A 1 60  ? 2.520   16.960  13.299  1.00 16.42  ?  60  THR A CA  1 
ATOM   444  C  C   . THR A 1 60  ? 2.987   18.113  12.408  1.00 16.85  ?  60  THR A C   1 
ATOM   445  O  O   . THR A 1 60  ? 2.213   19.011  12.087  1.00 16.19  ?  60  THR A O   1 
ATOM   446  C  CB  . THR A 1 60  ? 2.921   17.164  14.764  1.00 19.23  ?  60  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 60  ? 2.889   15.910  15.460  1.00 20.07  ?  60  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 60  ? 1.966   18.134  15.445  1.00 23.39  ?  60  THR A CG2 1 
ATOM   449  N  N   . GLY A 1 61  ? 4.275   18.109  12.030  1.00 14.16  ?  61  GLY A N   1 
ATOM   450  C  CA  . GLY A 1 61  ? 4.795   19.054  11.077  1.00 14.34  ?  61  GLY A CA  1 
ATOM   451  C  C   . GLY A 1 61  ? 6.159   18.563  10.575  1.00 14.98  ?  61  GLY A C   1 
ATOM   452  O  O   . GLY A 1 61  ? 6.657   17.552  11.056  1.00 16.43  ?  61  GLY A O   1 
ATOM   453  N  N   . ILE A 1 62  ? 6.737   19.272  9.613   1.00 13.54  ?  62  ILE A N   1 
ATOM   454  C  CA  . ILE A 1 62  ? 8.061   18.960  9.077   1.00 14.29  ?  62  ILE A CA  1 
ATOM   455  C  C   . ILE A 1 62  ? 8.843   20.253  9.063   1.00 13.64  ?  62  ILE A C   1 
ATOM   456  O  O   . ILE A 1 62  ? 8.310   21.272  8.631   1.00 15.11  ?  62  ILE A O   1 
ATOM   457  C  CB  . ILE A 1 62  ? 7.954   18.304  7.680   1.00 14.92  ?  62  ILE A CB  1 
ATOM   458  C  CG1 . ILE A 1 62  ? 7.271   16.947  7.754   1.00 14.58  ?  62  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A 1 62  ? 9.321   18.187  6.988   1.00 15.83  ?  62  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A 1 62  ? 6.928   16.378  6.387   1.00 16.00  ?  62  ILE A CD1 1 
ATOM   461  N  N   . MET A 1 63  ? 10.116  20.180  9.484   1.00 14.02  ?  63  MET A N   1 
ATOM   462  C  CA  . MET A 1 63  ? 10.962  21.334  9.620   1.00 14.75  ?  63  MET A CA  1 
ATOM   463  C  C   . MET A 1 63  ? 12.153  21.279  8.668   1.00 14.26  ?  63  MET A C   1 
ATOM   464  O  O   . MET A 1 63  ? 12.776  20.239  8.484   1.00 12.48  ?  63  MET A O   1 
ATOM   465  C  CB  . MET A 1 63  ? 11.418  21.460  11.085  1.00 16.16  ?  63  MET A CB  1 
ATOM   466  C  CG  . MET A 1 63  ? 12.296  22.637  11.321  1.00 18.45  ?  63  MET A CG  1 
ATOM   467  S  SD  . MET A 1 63  ? 12.759  22.807  13.064  1.00 23.92  ?  63  MET A SD  1 
ATOM   468  C  CE  . MET A 1 63  ? 11.148  23.399  13.601  1.00 21.33  ?  63  MET A CE  1 
ATOM   469  N  N   . LEU A 1 64  ? 12.469  22.436  8.084   1.00 13.08  ?  64  LEU A N   1 
ATOM   470  C  CA  . LEU A 1 64  ? 13.681  22.678  7.324   1.00 13.40  ?  64  LEU A CA  1 
ATOM   471  C  C   . LEU A 1 64  ? 14.481  23.704  8.114   1.00 14.62  ?  64  LEU A C   1 
ATOM   472  O  O   . LEU A 1 64  ? 13.981  24.807  8.321   1.00 14.13  ?  64  LEU A O   1 
ATOM   473  C  CB  . LEU A 1 64  ? 13.282  23.233  5.956   1.00 12.91  ?  64  LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 64  ? 12.228  22.435  5.166   1.00 13.35  ?  64  LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 64  ? 11.839  23.179  3.908   1.00 16.14  ?  64  LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 64  ? 12.681  21.010  4.858   1.00 14.04  ?  64  LEU A CD2 1 
ATOM   477  N  N   . THR A 1 65  ? 15.694  23.367  8.531   1.00 13.29  ?  65  THR A N   1 
ATOM   478  C  CA  . THR A 1 65  ? 16.409  24.204  9.493   1.00 12.94  ?  65  THR A CA  1 
ATOM   479  C  C   . THR A 1 65  ? 17.859  24.367  9.078   1.00 14.34  ?  65  THR A C   1 
ATOM   480  O  O   . THR A 1 65  ? 18.426  23.513  8.431   1.00 13.02  ?  65  THR A O   1 
ATOM   481  C  CB  . THR A 1 65  ? 16.279  23.631  10.899  1.00 15.63  ?  65  THR A CB  1 
ATOM   482  O  OG1 . THR A 1 65  ? 16.965  24.506  11.777  1.00 16.56  ?  65  THR A OG1 1 
ATOM   483  C  CG2 . THR A 1 65  ? 16.920  22.262  11.024  1.00 15.48  ?  65  THR A CG2 1 
ATOM   484  N  N   . GLY A 1 66  ? 18.437  25.522  9.433   1.00 14.99  ?  66  GLY A N   1 
ATOM   485  C  CA  . GLY A 1 66  ? 19.866  25.711  9.419   1.00 13.91  ?  66  GLY A CA  1 
ATOM   486  C  C   . GLY A 1 66  ? 20.512  25.149  10.676  1.00 14.93  ?  66  GLY A C   1 
ATOM   487  O  O   . GLY A 1 66  ? 19.887  24.425  11.453  1.00 13.93  ?  66  GLY A O   1 
ATOM   488  N  N   . GLY A 1 67  ? 21.798  25.472  10.841  1.00 15.09  ?  67  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 67  ? 22.542  25.059  12.023  1.00 15.78  ?  67  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 67  ? 23.314  23.766  11.884  1.00 15.16  ?  67  GLY A C   1 
ATOM   491  O  O   . GLY A 1 67  ? 23.852  23.276  12.874  1.00 16.06  ?  67  GLY A O   1 
ATOM   492  N  N   . SER A 1 68  ? 23.402  23.197  10.674  1.00 16.17  ?  68  SER A N   1 
ATOM   493  C  CA  . SER A 1 68  ? 24.015  21.890  10.496  1.00 16.08  ?  68  SER A CA  1 
ATOM   494  C  C   . SER A 1 68  ? 23.444  20.895  11.496  1.00 15.36  ?  68  SER A C   1 
ATOM   495  O  O   . SER A 1 68  ? 22.264  20.965  11.858  1.00 16.15  ?  68  SER A O   1 
ATOM   496  C  CB  . SER A 1 68  ? 25.535  22.018  10.528  1.00 17.49  ?  68  SER A CB  1 
ATOM   497  O  OG  . SER A 1 68  ? 26.203  20.816  10.176  1.00 17.15  ?  68  SER A OG  1 
ATOM   498  N  N   . ALA A 1 69  ? 24.259  19.958  11.959  1.00 15.62  ?  69  ALA A N   1 
ATOM   499  C  CA  . ALA A 1 69  ? 23.788  18.919  12.862  1.00 15.79  ?  69  ALA A CA  1 
ATOM   500  C  C   . ALA A 1 69  ? 23.149  19.469  14.140  1.00 15.97  ?  69  ALA A C   1 
ATOM   501  O  O   . ALA A 1 69  ? 22.274  18.825  14.726  1.00 16.86  ?  69  ALA A O   1 
ATOM   502  C  CB  . ALA A 1 69  ? 24.936  18.002  13.206  1.00 16.76  ?  69  ALA A CB  1 
ATOM   503  N  N   . PHE A 1 70  ? 23.609  20.645  14.606  1.00 15.56  ?  70  PHE A N   1 
ATOM   504  C  CA  . PHE A 1 70  ? 23.081  21.277  15.805  1.00 15.56  ?  70  PHE A CA  1 
ATOM   505  C  C   . PHE A 1 70  ? 21.607  21.630  15.664  1.00 14.51  ?  70  PHE A C   1 
ATOM   506  O  O   . PHE A 1 70  ? 20.866  21.576  16.654  1.00 15.76  ?  70  PHE A O   1 
ATOM   507  C  CB  . PHE A 1 70  ? 23.842  22.563  16.132  1.00 15.94  ?  70  PHE A CB  1 
ATOM   508  C  CG  . PHE A 1 70  ? 25.323  22.333  16.322  1.00 15.55  ?  70  PHE A CG  1 
ATOM   509  C  CD1 . PHE A 1 70  ? 25.806  21.752  17.494  1.00 16.29  ?  70  PHE A CD1 1 
ATOM   510  C  CD2 . PHE A 1 70  ? 26.217  22.749  15.355  1.00 16.97  ?  70  PHE A CD2 1 
ATOM   511  C  CE1 . PHE A 1 70  ? 27.173  21.541  17.657  1.00 15.63  ?  70  PHE A CE1 1 
ATOM   512  C  CE2 . PHE A 1 70  ? 27.572  22.558  15.535  1.00 16.31  ?  70  PHE A CE2 1 
ATOM   513  C  CZ  . PHE A 1 70  ? 28.035  21.945  16.685  1.00 16.76  ?  70  PHE A CZ  1 
ATOM   514  N  N   . GLY A 1 71  ? 21.206  21.996  14.439  1.00 13.87  ?  71  GLY A N   1 
ATOM   515  C  CA  . GLY A 1 71  ? 19.911  22.583  14.175  1.00 13.06  ?  71  GLY A CA  1 
ATOM   516  C  C   . GLY A 1 71  ? 18.739  21.631  14.360  1.00 13.28  ?  71  GLY A C   1 
ATOM   517  O  O   . GLY A 1 71  ? 17.613  22.099  14.457  1.00 14.00  ?  71  GLY A O   1 
ATOM   518  N  N   . LEU A 1 72  ? 18.999  20.309  14.439  1.00 12.77  ?  72  LEU A N   1 
ATOM   519  C  CA  . LEU A 1 72  ? 17.922  19.381  14.716  1.00 14.25  ?  72  LEU A CA  1 
ATOM   520  C  C   . LEU A 1 72  ? 17.314  19.598  16.109  1.00 14.37  ?  72  LEU A C   1 
ATOM   521  O  O   . LEU A 1 72  ? 16.198  19.174  16.355  1.00 14.24  ?  72  LEU A O   1 
ATOM   522  C  CB  . LEU A 1 72  ? 18.378  17.950  14.475  1.00 13.04  ?  72  LEU A CB  1 
ATOM   523  C  CG  . LEU A 1 72  ? 18.695  17.615  13.028  1.00 13.64  ?  72  LEU A CG  1 
ATOM   524  C  CD1 . LEU A 1 72  ? 19.195  16.203  12.936  1.00 14.53  ?  72  LEU A CD1 1 
ATOM   525  C  CD2 . LEU A 1 72  ? 17.481  17.777  12.164  1.00 14.93  ?  72  LEU A CD2 1 
ATOM   526  N  N   . GLU A 1 73  ? 18.022  20.292  17.014  1.00 14.00  ?  73  GLU A N   1 
ATOM   527  C  CA  . GLU A 1 73  ? 17.430  20.656  18.294  1.00 14.67  ?  73  GLU A CA  1 
ATOM   528  C  C   . GLU A 1 73  ? 16.123  21.437  18.114  1.00 13.58  ?  73  GLU A C   1 
ATOM   529  O  O   . GLU A 1 73  ? 15.204  21.306  18.929  1.00 13.99  ?  73  GLU A O   1 
ATOM   530  C  CB  . GLU A 1 73  ? 18.469  21.445  19.086  1.00 14.73  ?  73  GLU A CB  1 
ATOM   531  C  CG  . GLU A 1 73  ? 18.013  21.763  20.501  1.00 16.21  ?  73  GLU A CG  1 
ATOM   532  C  CD  . GLU A 1 73  ? 19.075  22.491  21.316  1.00 17.85  ?  73  GLU A CD  1 
ATOM   533  O  OE1 . GLU A 1 73  ? 20.246  22.019  21.385  1.00 20.03  ?  73  GLU A OE1 1 
ATOM   534  O  OE2 . GLU A 1 73  ? 18.685  23.511  21.912  1.00 18.22  -1 73  GLU A OE2 1 
ATOM   535  N  N   . ALA A 1 74  ? 16.017  22.289  17.073  1.00 14.22  ?  74  ALA A N   1 
ATOM   536  C  CA  . ALA A 1 74  ? 14.808  23.037  16.833  1.00 14.27  ?  74  ALA A CA  1 
ATOM   537  C  C   . ALA A 1 74  ? 13.606  22.113  16.595  1.00 14.83  ?  74  ALA A C   1 
ATOM   538  O  O   . ALA A 1 74  ? 12.461  22.476  16.876  1.00 13.88  ?  74  ALA A O   1 
ATOM   539  C  CB  . ALA A 1 74  ? 15.006  23.967  15.657  1.00 15.31  ?  74  ALA A CB  1 
ATOM   540  N  N   . ALA A 1 75  ? 13.829  20.925  15.993  1.00 14.13  ?  75  ALA A N   1 
ATOM   541  C  CA  . ALA A 1 75  ? 12.740  19.990  15.812  1.00 13.92  ?  75  ALA A CA  1 
ATOM   542  C  C   . ALA A 1 75  ? 12.179  19.539  17.166  1.00 13.65  ?  75  ALA A C   1 
ATOM   543  O  O   . ALA A 1 75  ? 10.957  19.386  17.316  1.00 13.57  ?  75  ALA A O   1 
ATOM   544  C  CB  . ALA A 1 75  ? 13.213  18.802  14.952  1.00 13.40  ?  75  ALA A CB  1 
ATOM   545  N  N   . LEU A 1 76  ? 13.059  19.288  18.141  1.00 14.00  ?  76  LEU A N   1 
ATOM   546  C  CA  . LEU A 1 76  ? 12.609  18.920  19.475  1.00 15.25  ?  76  LEU A CA  1 
ATOM   547  C  C   . LEU A 1 76  ? 11.902  20.079  20.174  1.00 17.40  ?  76  LEU A C   1 
ATOM   548  O  O   . LEU A 1 76  ? 10.965  19.832  20.922  1.00 17.07  ?  76  LEU A O   1 
ATOM   549  C  CB  . LEU A 1 76  ? 13.775  18.353  20.273  1.00 18.00  ?  76  LEU A CB  1 
ATOM   550  C  CG  . LEU A 1 76  ? 14.068  16.954  19.707  1.00 23.13  ?  76  LEU A CG  1 
ATOM   551  C  CD1 . LEU A 1 76  ? 15.495  16.645  19.554  1.00 26.60  ?  76  LEU A CD1 1 
ATOM   552  C  CD2 . LEU A 1 76  ? 13.267  15.969  20.581  1.00 22.94  ?  76  LEU A CD2 1 
ATOM   553  N  N   . GLY A 1 77  ? 12.296  21.315  19.866  1.00 16.18  ?  77  GLY A N   1 
ATOM   554  C  CA  . GLY A 1 77  ? 11.562  22.482  20.362  1.00 15.59  ?  77  GLY A CA  1 
ATOM   555  C  C   . GLY A 1 77  ? 10.120  22.523  19.868  1.00 16.31  ?  77  GLY A C   1 
ATOM   556  O  O   . GLY A 1 77  ? 9.173   22.800  20.628  1.00 15.91  ?  77  GLY A O   1 
ATOM   557  N  N   . ALA A 1 78  ? 9.933   22.139  18.601  1.00 14.47  ?  78  ALA A N   1 
ATOM   558  C  CA  . ALA A 1 78  ? 8.618   22.027  17.995  1.00 15.75  ?  78  ALA A CA  1 
ATOM   559  C  C   . ALA A 1 78  ? 7.823   20.893  18.629  1.00 15.90  ?  78  ALA A C   1 
ATOM   560  O  O   . ALA A 1 78  ? 6.621   21.056  18.865  1.00 15.70  ?  78  ALA A O   1 
ATOM   561  C  CB  . ALA A 1 78  ? 8.719   21.868  16.477  1.00 16.53  ?  78  ALA A CB  1 
ATOM   562  N  N   . VAL A 1 79  ? 8.476   19.737  18.876  1.00 14.82  ?  79  VAL A N   1 
ATOM   563  C  CA  . VAL A 1 79  ? 7.808   18.614  19.531  1.00 17.44  ?  79  VAL A CA  1 
ATOM   564  C  C   . VAL A 1 79  ? 7.257   19.051  20.898  1.00 19.38  ?  79  VAL A C   1 
ATOM   565  O  O   . VAL A 1 79  ? 6.107   18.766  21.216  1.00 17.48  ?  79  VAL A O   1 
ATOM   566  C  CB  . VAL A 1 79  ? 8.776   17.419  19.665  1.00 18.36  ?  79  VAL A CB  1 
ATOM   567  C  CG1 . VAL A 1 79  ? 8.284   16.365  20.631  1.00 20.71  ?  79  VAL A CG1 1 
ATOM   568  C  CG2 . VAL A 1 79  ? 9.033   16.771  18.314  1.00 18.55  ?  79  VAL A CG2 1 
ATOM   569  N  N   . ARG A 1 80  ? 8.084   19.741  21.689  1.00 19.41  ?  80  ARG A N   1 
ATOM   570  C  CA  . ARG A 1 80  ? 7.671   20.257  22.999  1.00 21.15  ?  80  ARG A CA  1 
ATOM   571  C  C   . ARG A 1 80  ? 6.478   21.210  22.879  1.00 22.79  ?  80  ARG A C   1 
ATOM   572  O  O   . ARG A 1 80  ? 5.482   21.083  23.607  1.00 23.25  ?  80  ARG A O   1 
ATOM   573  C  CB  . ARG A 1 80  ? 8.836   20.951  23.706  1.00 19.85  ?  80  ARG A CB  1 
ATOM   574  C  CG  . ARG A 1 80  ? 9.879   20.010  24.288  1.00 22.60  ?  80  ARG A CG  1 
ATOM   575  C  CD  . ARG A 1 80  ? 11.019  20.858  24.847  1.00 24.83  ?  80  ARG A CD  1 
ATOM   576  N  NE  . ARG A 1 80  ? 11.982  20.041  25.578  1.00 24.93  ?  80  ARG A NE  1 
ATOM   577  C  CZ  . ARG A 1 80  ? 11.861  19.749  26.863  1.00 28.88  ?  80  ARG A CZ  1 
ATOM   578  N  NH1 . ARG A 1 80  ? 10.855  20.248  27.569  1.00 28.21  1  80  ARG A NH1 1 
ATOM   579  N  NH2 . ARG A 1 80  ? 12.788  19.022  27.448  1.00 27.97  ?  80  ARG A NH2 1 
ATOM   580  N  N   . TYR A 1 81  ? 6.539   22.150  21.935  1.00 19.39  ?  81  TYR A N   1 
ATOM   581  C  CA  . TYR A 1 81  ? 5.407   23.050  21.680  1.00 19.79  ?  81  TYR A CA  1 
ATOM   582  C  C   . TYR A 1 81  ? 4.114   22.288  21.405  1.00 20.91  ?  81  TYR A C   1 
ATOM   583  O  O   . TYR A 1 81  ? 3.061   22.600  21.970  1.00 21.12  ?  81  TYR A O   1 
ATOM   584  C  CB  . TYR A 1 81  ? 5.729   24.055  20.561  1.00 19.20  ?  81  TYR A CB  1 
ATOM   585  C  CG  . TYR A 1 81  ? 4.552   24.920  20.155  1.00 21.22  ?  81  TYR A CG  1 
ATOM   586  C  CD1 . TYR A 1 81  ? 4.308   26.122  20.820  1.00 22.96  ?  81  TYR A CD1 1 
ATOM   587  C  CD2 . TYR A 1 81  ? 3.686   24.553  19.131  1.00 21.95  ?  81  TYR A CD2 1 
ATOM   588  C  CE1 . TYR A 1 81  ? 3.247   26.941  20.450  1.00 24.07  ?  81  TYR A CE1 1 
ATOM   589  C  CE2 . TYR A 1 81  ? 2.628   25.369  18.755  1.00 22.24  ?  81  TYR A CE2 1 
ATOM   590  C  CZ  . TYR A 1 81  ? 2.420   26.565  19.413  1.00 22.31  ?  81  TYR A CZ  1 
ATOM   591  O  OH  . TYR A 1 81  ? 1.372   27.367  19.093  1.00 25.06  ?  81  TYR A OH  1 
ATOM   592  N  N   . PHE A 1 82  ? 4.171   21.298  20.493  1.00 18.31  ?  82  PHE A N   1 
ATOM   593  C  CA  . PHE A 1 82  ? 2.989   20.576  20.063  1.00 17.28  ?  82  PHE A CA  1 
ATOM   594  C  C   . PHE A 1 82  ? 2.423   19.728  21.205  1.00 19.04  ?  82  PHE A C   1 
ATOM   595  O  O   . PHE A 1 82  ? 1.201   19.608  21.336  1.00 18.92  ?  82  PHE A O   1 
ATOM   596  C  CB  . PHE A 1 82  ? 3.259   19.707  18.826  1.00 18.45  ?  82  PHE A CB  1 
ATOM   597  C  CG  . PHE A 1 82  ? 3.403   20.518  17.551  1.00 21.43  ?  82  PHE A CG  1 
ATOM   598  C  CD1 . PHE A 1 82  ? 2.436   21.449  17.183  1.00 24.72  ?  82  PHE A CD1 1 
ATOM   599  C  CD2 . PHE A 1 82  ? 4.511   20.345  16.725  1.00 23.10  ?  82  PHE A CD2 1 
ATOM   600  C  CE1 . PHE A 1 82  ? 2.599   22.211  16.033  1.00 26.28  ?  82  PHE A CE1 1 
ATOM   601  C  CE2 . PHE A 1 82  ? 4.646   21.083  15.571  1.00 24.75  ?  82  PHE A CE2 1 
ATOM   602  C  CZ  . PHE A 1 82  ? 3.705   22.035  15.247  1.00 25.75  ?  82  PHE A CZ  1 
ATOM   603  N  N   . GLU A 1 83  ? 3.291   19.137  22.025  1.00 19.64  ?  83  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 83  ? 2.808   18.421  23.204  1.00 20.84  ?  83  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 83  ? 2.027   19.364  24.135  1.00 21.78  ?  83  GLU A C   1 
ATOM   606  O  O   . GLU A 1 83  ? 0.979   18.984  24.625  1.00 23.86  ?  83  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 83  ? 3.923   17.754  23.997  1.00 23.26  ?  83  GLU A CB  1 
ATOM   608  C  CG  . GLU A 1 83  ? 3.356   16.800  25.046  1.00 23.63  ?  83  GLU A CG  1 
ATOM   609  C  CD  . GLU A 1 83  ? 4.373   16.295  26.057  1.00 23.64  ?  83  GLU A CD  1 
ATOM   610  O  OE1 . GLU A 1 83  ? 5.514   16.785  26.062  1.00 23.72  ?  83  GLU A OE1 1 
ATOM   611  O  OE2 . GLU A 1 83  ? 4.006   15.412  26.856  1.00 26.15  -1 83  GLU A OE2 1 
ATOM   612  N  N   . GLU A 1 84  ? 2.515   20.573  24.368  1.00 25.37  ?  84  GLU A N   1 
ATOM   613  C  CA  . GLU A 1 84  ? 1.807   21.543  25.199  1.00 28.81  ?  84  GLU A CA  1 
ATOM   614  C  C   . GLU A 1 84  ? 0.449   21.909  24.611  1.00 27.59  ?  84  GLU A C   1 
ATOM   615  O  O   . GLU A 1 84  ? -0.483  22.138  25.355  1.00 25.94  ?  84  GLU A O   1 
ATOM   616  C  CB  . GLU A 1 84  ? 2.536   22.866  25.382  1.00 31.05  ?  84  GLU A CB  1 
ATOM   617  C  CG  . GLU A 1 84  ? 3.780   22.711  26.228  1.00 39.76  ?  84  GLU A CG  1 
ATOM   618  C  CD  . GLU A 1 84  ? 4.512   24.031  26.341  1.00 46.30  ?  84  GLU A CD  1 
ATOM   619  O  OE1 . GLU A 1 84  ? 3.868   25.088  26.129  1.00 43.84  ?  84  GLU A OE1 1 
ATOM   620  O  OE2 . GLU A 1 84  ? 5.730   23.974  26.625  1.00 50.72  -1 84  GLU A OE2 1 
ATOM   621  N  N   . GLN A 1 85  ? 0.332   21.954  23.285  1.00 28.93  ?  85  GLN A N   1 
ATOM   622  C  CA  . GLN A 1 85  ? -0.930  22.263  22.625  1.00 32.54  ?  85  GLN A CA  1 
ATOM   623  C  C   . GLN A 1 85  ? -1.830  21.027  22.565  1.00 29.03  ?  85  GLN A C   1 
ATOM   624  O  O   . GLN A 1 85  ? -2.907  21.092  21.997  1.00 36.78  ?  85  GLN A O   1 
ATOM   625  C  CB  . GLN A 1 85  ? -0.742  22.838  21.218  1.00 35.23  ?  85  GLN A CB  1 
ATOM   626  C  CG  . GLN A 1 85  ? 0.070   24.130  21.136  1.00 39.89  ?  85  GLN A CG  1 
ATOM   627  C  CD  . GLN A 1 85  ? -0.589  25.333  21.781  1.00 53.70  ?  85  GLN A CD  1 
ATOM   628  O  OE1 . GLN A 1 85  ? -1.620  25.838  21.323  1.00 54.60  ?  85  GLN A OE1 1 
ATOM   629  N  NE2 . GLN A 1 85  ? 0.063   25.885  22.795  1.00 58.12  ?  85  GLN A NE2 1 
ATOM   630  N  N   . GLY A 1 86  ? -1.394  19.864  23.046  1.00 29.20  ?  86  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 86  ? -2.239  18.675  23.036  1.00 25.91  ?  86  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 86  ? -2.286  17.929  21.692  1.00 31.86  ?  86  GLY A C   1 
ATOM   633  O  O   . GLY A 1 86  ? -3.204  17.137  21.442  1.00 27.26  ?  86  GLY A O   1 
ATOM   634  N  N   . ARG A 1 87  ? -1.265  18.102  20.829  1.00 29.43  ?  87  ARG A N   1 
ATOM   635  C  CA  . ARG A 1 87  ? -1.216  17.352  19.587  1.00 25.40  ?  87  ARG A CA  1 
ATOM   636  C  C   . ARG A 1 87  ? -0.300  16.139  19.694  1.00 24.90  ?  87  ARG A C   1 
ATOM   637  O  O   . ARG A 1 87  ? 0.655   16.119  20.469  1.00 29.08  ?  87  ARG A O   1 
ATOM   638  C  CB  . ARG A 1 87  ? -0.673  18.251  18.480  1.00 26.89  ?  87  ARG A CB  1 
ATOM   639  C  CG  . ARG A 1 87  ? -1.577  19.450  18.239  1.00 31.02  ?  87  ARG A CG  1 
ATOM   640  C  CD  . ARG A 1 87  ? -1.474  19.835  16.783  1.00 37.38  ?  87  ARG A CD  1 
ATOM   641  N  NE  . ARG A 1 87  ? -2.328  20.985  16.498  1.00 41.83  ?  87  ARG A NE  1 
ATOM   642  C  CZ  . ARG A 1 87  ? -2.523  21.507  15.292  1.00 40.08  ?  87  ARG A CZ  1 
ATOM   643  N  NH1 . ARG A 1 87  ? -1.812  21.125  14.254  1.00 33.89  1  87  ARG A NH1 1 
ATOM   644  N  NH2 . ARG A 1 87  ? -3.489  22.391  15.124  1.00 43.46  ?  87  ARG A NH2 1 
ATOM   645  N  N   . GLY A 1 88  ? -0.543  15.164  18.835  1.00 23.79  ?  88  GLY A N   1 
ATOM   646  C  CA  . GLY A 1 88  ? 0.338   14.015  18.716  1.00 25.08  ?  88  GLY A CA  1 
ATOM   647  C  C   . GLY A 1 88  ? -0.414  12.718  18.957  1.00 28.40  ?  88  GLY A C   1 
ATOM   648  O  O   . GLY A 1 88  ? -1.596  12.750  19.292  1.00 27.91  ?  88  GLY A O   1 
ATOM   649  N  N   . TYR A 1 89  ? 0.289   11.596  18.764  1.00 26.46  ?  89  TYR A N   1 
ATOM   650  C  CA  . TYR A 1 89  ? -0.303  10.280  18.902  1.00 28.84  ?  89  TYR A CA  1 
ATOM   651  C  C   . TYR A 1 89  ? -0.602  10.024  20.378  1.00 26.62  ?  89  TYR A C   1 
ATOM   652  O  O   . TYR A 1 89  ? 0.239   10.248  21.247  1.00 22.55  ?  89  TYR A O   1 
ATOM   653  C  CB  . TYR A 1 89  ? 0.602   9.204   18.290  1.00 30.79  ?  89  TYR A CB  1 
ATOM   654  C  CG  . TYR A 1 89  ? 0.031   7.798   18.392  1.00 40.89  ?  89  TYR A CG  1 
ATOM   655  C  CD1 . TYR A 1 89  ? -0.952  7.327   17.516  1.00 49.48  ?  89  TYR A CD1 1 
ATOM   656  C  CD2 . TYR A 1 89  ? 0.472   6.935   19.388  1.00 50.39  ?  89  TYR A CD2 1 
ATOM   657  C  CE1 . TYR A 1 89  ? -1.466  6.038   17.632  1.00 53.60  ?  89  TYR A CE1 1 
ATOM   658  C  CE2 . TYR A 1 89  ? -0.042  5.655   19.520  1.00 56.77  ?  89  TYR A CE2 1 
ATOM   659  C  CZ  . TYR A 1 89  ? -1.008  5.197   18.639  1.00 59.35  ?  89  TYR A CZ  1 
ATOM   660  O  OH  . TYR A 1 89  ? -1.441  3.905   18.831  1.00 67.29  ?  89  TYR A OH  1 
ATOM   661  N  N   . ASP A 1 90  ? -1.809  9.524   20.660  1.00 28.10  ?  90  ASP A N   1 
ATOM   662  C  CA  . ASP A 1 90  ? -2.280  9.432   22.039  1.00 28.23  ?  90  ASP A CA  1 
ATOM   663  C  C   . ASP A 1 90  ? -1.967  8.051   22.583  1.00 26.05  ?  90  ASP A C   1 
ATOM   664  O  O   . ASP A 1 90  ? -2.483  7.071   22.080  1.00 31.27  ?  90  ASP A O   1 
ATOM   665  C  CB  . ASP A 1 90  ? -3.774  9.714   22.153  1.00 35.18  ?  90  ASP A CB  1 
ATOM   666  C  CG  . ASP A 1 90  ? -4.296  9.906   23.576  1.00 36.21  ?  90  ASP A CG  1 
ATOM   667  O  OD1 . ASP A 1 90  ? -3.625  9.489   24.522  1.00 32.58  ?  90  ASP A OD1 1 
ATOM   668  O  OD2 . ASP A 1 90  ? -5.376  10.500  23.732  1.00 44.77  -1 90  ASP A OD2 1 
ATOM   669  N  N   . VAL A 1 91  ? -1.134  7.981   23.616  1.00 28.03  ?  91  VAL A N   1 
ATOM   670  C  CA  . VAL A 1 91  ? -0.806  6.697   24.236  1.00 29.41  ?  91  VAL A CA  1 
ATOM   671  C  C   . VAL A 1 91  ? -1.420  6.621   25.627  1.00 27.92  ?  91  VAL A C   1 
ATOM   672  O  O   . VAL A 1 91  ? -0.978  5.831   26.445  1.00 35.45  ?  91  VAL A O   1 
ATOM   673  C  CB  . VAL A 1 91  ? 0.707   6.404   24.320  1.00 29.83  ?  91  VAL A CB  1 
ATOM   674  C  CG1 . VAL A 1 91  ? 1.285   6.137   22.948  1.00 33.61  ?  91  VAL A CG1 1 
ATOM   675  C  CG2 . VAL A 1 91  ? 1.497   7.474   25.065  1.00 29.23  ?  91  VAL A CG2 1 
ATOM   676  N  N   . GLY A 1 92  ? -2.381  7.497   25.922  1.00 31.12  ?  92  GLY A N   1 
ATOM   677  C  CA  . GLY A 1 92  ? -3.069  7.485   27.205  1.00 31.98  ?  92  GLY A CA  1 
ATOM   678  C  C   . GLY A 1 92  ? -2.323  8.288   28.259  1.00 31.73  ?  92  GLY A C   1 
ATOM   679  O  O   . GLY A 1 92  ? -2.879  9.230   28.807  1.00 33.98  ?  92  GLY A O   1 
ATOM   680  N  N   . VAL A 1 93  ? -1.051  7.926   28.510  1.00 27.81  ?  93  VAL A N   1 
ATOM   681  C  CA  . VAL A 1 93  ? -0.269  8.593   29.536  1.00 27.82  ?  93  VAL A CA  1 
ATOM   682  C  C   . VAL A 1 93  ? 0.390   9.854   28.976  1.00 28.11  ?  93  VAL A C   1 
ATOM   683  O  O   . VAL A 1 93  ? 0.972   10.621  29.731  1.00 27.54  ?  93  VAL A O   1 
ATOM   684  C  CB  . VAL A 1 93  ? 0.808   7.674   30.146  1.00 28.23  ?  93  VAL A CB  1 
ATOM   685  C  CG1 . VAL A 1 93  ? 0.176   6.523   30.912  1.00 30.40  ?  93  VAL A CG1 1 
ATOM   686  C  CG2 . VAL A 1 93  ? 1.777   7.133   29.092  1.00 28.18  ?  93  VAL A CG2 1 
ATOM   687  N  N   . ALA A 1 94  ? 0.382   10.011  27.648  1.00 28.90  ?  94  ALA A N   1 
ATOM   688  C  CA  . ALA A 1 94  ? 0.994   11.170  27.005  1.00 26.15  ?  94  ALA A CA  1 
ATOM   689  C  C   . ALA A 1 94  ? 0.490   11.233  25.572  1.00 23.84  ?  94  ALA A C   1 
ATOM   690  O  O   . ALA A 1 94  ? -0.101  10.272  25.073  1.00 24.60  ?  94  ALA A O   1 
ATOM   691  C  CB  . ALA A 1 94  ? 2.515   11.084  27.040  1.00 26.01  ?  94  ALA A CB  1 
ATOM   692  N  N   . LYS A 1 95  ? 0.762   12.371  24.941  1.00 22.70  ?  95  LYS A N   1 
ATOM   693  C  CA  . LYS A 1 95  ? 0.609   12.539  23.501  1.00 25.01  ?  95  LYS A CA  1 
ATOM   694  C  C   . LYS A 1 95  ? 2.007   12.748  22.914  1.00 22.15  ?  95  LYS A C   1 
ATOM   695  O  O   . LYS A 1 95  ? 2.807   13.489  23.485  1.00 21.58  ?  95  LYS A O   1 
ATOM   696  C  CB  . LYS A 1 95  ? -0.262  13.760  23.181  1.00 29.62  ?  95  LYS A CB  1 
ATOM   697  C  CG  . LYS A 1 95  ? -1.662  13.683  23.770  1.00 35.35  ?  95  LYS A CG  1 
ATOM   698  C  CD  . LYS A 1 95  ? -2.725  14.393  22.941  1.00 48.19  ?  95  LYS A CD  1 
ATOM   699  C  CE  . LYS A 1 95  ? -4.136  14.119  23.420  1.00 52.04  ?  95  LYS A CE  1 
ATOM   700  N  NZ  . LYS A 1 95  ? -4.236  14.449  24.847  1.00 60.42  1  95  LYS A NZ  1 
ATOM   701  N  N   . ILE A 1 96  ? 2.306   12.076  21.794  1.00 22.74  ?  96  ILE A N   1 
ATOM   702  C  CA  . ILE A 1 96  ? 3.667   12.086  21.263  1.00 20.60  ?  96  ILE A CA  1 
ATOM   703  C  C   . ILE A 1 96  ? 3.637   12.709  19.874  1.00 19.44  ?  96  ILE A C   1 
ATOM   704  O  O   . ILE A 1 96  ? 3.212   12.063  18.921  1.00 16.59  ?  96  ILE A O   1 
ATOM   705  C  CB  . ILE A 1 96  ? 4.280   10.683  21.209  1.00 21.10  ?  96  ILE A CB  1 
ATOM   706  C  CG1 . ILE A 1 96  ? 4.088   9.954   22.549  1.00 23.91  ?  96  ILE A CG1 1 
ATOM   707  C  CG2 . ILE A 1 96  ? 5.760   10.808  20.824  1.00 21.15  ?  96  ILE A CG2 1 
ATOM   708  C  CD1 . ILE A 1 96  ? 4.551   8.523   22.525  1.00 26.00  ?  96  ILE A CD1 1 
ATOM   709  N  N   . PRO A 1 97  ? 3.995   13.995  19.734  1.00 19.48  ?  97  PRO A N   1 
ATOM   710  C  CA  . PRO A 1 97  ? 4.079   14.598  18.407  1.00 19.49  ?  97  PRO A CA  1 
ATOM   711  C  C   . PRO A 1 97  ? 5.318   14.099  17.664  1.00 19.57  ?  97  PRO A C   1 
ATOM   712  O  O   . PRO A 1 97  ? 6.203   13.531  18.306  1.00 18.50  ?  97  PRO A O   1 
ATOM   713  C  CB  . PRO A 1 97  ? 4.136   16.093  18.690  1.00 21.33  ?  97  PRO A CB  1 
ATOM   714  C  CG  . PRO A 1 97  ? 4.113   16.250  20.197  1.00 21.30  ?  97  PRO A CG  1 
ATOM   715  C  CD  . PRO A 1 97  ? 4.376   14.909  20.809  1.00 21.03  ?  97  PRO A CD  1 
ATOM   716  N  N   . LEU A 1 98  ? 5.330   14.270  16.334  1.00 17.52  ?  98  LEU A N   1 
ATOM   717  C  CA  . LEU A 1 98  ? 6.465   13.882  15.503  1.00 17.76  ?  98  LEU A CA  1 
ATOM   718  C  C   . LEU A 1 98  ? 6.742   15.007  14.510  1.00 14.68  ?  98  LEU A C   1 
ATOM   719  O  O   . LEU A 1 98  ? 5.817   15.414  13.821  1.00 14.67  ?  98  LEU A O   1 
ATOM   720  C  CB  . LEU A 1 98  ? 6.158   12.565  14.794  1.00 20.80  ?  98  LEU A CB  1 
ATOM   721  C  CG  . LEU A 1 98  ? 7.372   11.778  14.291  1.00 25.56  ?  98  LEU A CG  1 
ATOM   722  C  CD1 . LEU A 1 98  ? 8.022   11.075  15.479  1.00 26.22  ?  98  LEU A CD1 1 
ATOM   723  C  CD2 . LEU A 1 98  ? 6.953   10.789  13.237  1.00 29.19  ?  98  LEU A CD2 1 
ATOM   724  N  N   . VAL A 1 99  ? 8.000   15.482  14.499  1.00 14.07  ?  99  VAL A N   1 
ATOM   725  C  CA  . VAL A 1 99  ? 8.430   16.575  13.629  1.00 13.18  ?  99  VAL A CA  1 
ATOM   726  C  C   . VAL A 1 99  ? 9.710   16.140  12.925  1.00 12.84  ?  99  VAL A C   1 
ATOM   727  O  O   . VAL A 1 99  ? 10.835  16.428  13.380  1.00 13.74  ?  99  VAL A O   1 
ATOM   728  C  CB  . VAL A 1 99  ? 8.601   17.909  14.376  1.00 13.86  ?  99  VAL A CB  1 
ATOM   729  C  CG1 . VAL A 1 99  ? 9.032   19.018  13.451  1.00 14.36  ?  99  VAL A CG1 1 
ATOM   730  C  CG2 . VAL A 1 99  ? 7.292   18.279  15.092  1.00 16.56  ?  99  VAL A CG2 1 
ATOM   731  N  N   . PRO A 1 100 ? 9.590   15.392  11.813  1.00 11.67  ?  100 PRO A N   1 
ATOM   732  C  CA  . PRO A 1 100 ? 10.759  15.077  11.012  1.00 12.50  ?  100 PRO A CA  1 
ATOM   733  C  C   . PRO A 1 100 ? 11.385  16.363  10.469  1.00 12.79  ?  100 PRO A C   1 
ATOM   734  O  O   . PRO A 1 100 ? 10.694  17.363  10.305  1.00 12.37  ?  100 PRO A O   1 
ATOM   735  C  CB  . PRO A 1 100 ? 10.239  14.152  9.904   1.00 12.12  ?  100 PRO A CB  1 
ATOM   736  C  CG  . PRO A 1 100 ? 8.842   13.747  10.349  1.00 12.32  ?  100 PRO A CG  1 
ATOM   737  C  CD  . PRO A 1 100 ? 8.336   14.857  11.233  1.00 12.45  ?  100 PRO A CD  1 
ATOM   738  N  N   . ALA A 1 101 ? 12.695  16.323  10.242  1.00 12.82  ?  101 ALA A N   1 
ATOM   739  C  CA  . ALA A 1 101 ? 13.438  17.512  9.876   1.00 12.98  ?  101 ALA A CA  1 
ATOM   740  C  C   . ALA A 1 101 ? 14.732  17.112  9.169   1.00 12.90  ?  101 ALA A C   1 
ATOM   741  O  O   . ALA A 1 101 ? 15.253  15.997  9.338   1.00 12.18  ?  101 ALA A O   1 
ATOM   742  C  CB  . ALA A 1 101 ? 13.759  18.358  11.100  1.00 12.93  ?  101 ALA A CB  1 
ATOM   743  N  N   . ALA A 1 102 ? 15.194  18.032  8.337   1.00 12.93  ?  102 ALA A N   1 
ATOM   744  C  CA  . ALA A 1 102 ? 16.495  17.957  7.684   1.00 13.28  ?  102 ALA A CA  1 
ATOM   745  C  C   . ALA A 1 102 ? 17.183  19.322  7.791   1.00 13.14  ?  102 ALA A C   1 
ATOM   746  O  O   . ALA A 1 102 ? 16.505  20.330  7.972   1.00 13.53  ?  102 ALA A O   1 
ATOM   747  C  CB  . ALA A 1 102 ? 16.352  17.551  6.229   1.00 13.33  ?  102 ALA A CB  1 
ATOM   748  N  N   . VAL A 1 103 ? 18.522  19.341  7.647   1.00 13.20  ?  103 VAL A N   1 
ATOM   749  C  CA  . VAL A 1 103 ? 19.301  20.542  7.873   1.00 13.34  ?  103 VAL A CA  1 
ATOM   750  C  C   . VAL A 1 103 ? 20.060  20.981  6.612   1.00 12.84  ?  103 VAL A C   1 
ATOM   751  O  O   . VAL A 1 103 ? 20.344  20.177  5.707   1.00 10.91  ?  103 VAL A O   1 
ATOM   752  C  CB  . VAL A 1 103 ? 20.288  20.327  9.048   1.00 14.30  ?  103 VAL A CB  1 
ATOM   753  C  CG1 . VAL A 1 103 ? 19.612  19.673  10.252  1.00 15.64  ?  103 VAL A CG1 1 
ATOM   754  C  CG2 . VAL A 1 103 ? 21.516  19.537  8.638   1.00 13.37  ?  103 VAL A CG2 1 
ATOM   755  N  N   . ILE A 1 104 ? 20.432  22.277  6.618   1.00 12.50  ?  104 ILE A N   1 
ATOM   756  C  CA  . ILE A 1 104 ? 21.494  22.798  5.777   1.00 13.24  ?  104 ILE A CA  1 
ATOM   757  C  C   . ILE A 1 104 ? 22.645  23.274  6.662   1.00 13.47  ?  104 ILE A C   1 
ATOM   758  O  O   . ILE A 1 104 ? 22.472  23.641  7.834   1.00 14.99  ?  104 ILE A O   1 
ATOM   759  C  CB  . ILE A 1 104 ? 20.997  23.927  4.871   1.00 15.53  ?  104 ILE A CB  1 
ATOM   760  C  CG1 . ILE A 1 104 ? 20.645  25.207  5.684   1.00 16.14  ?  104 ILE A CG1 1 
ATOM   761  C  CG2 . ILE A 1 104 ? 19.850  23.487  3.971   1.00 15.88  ?  104 ILE A CG2 1 
ATOM   762  C  CD1 . ILE A 1 104 ? 20.616  26.487  4.869   1.00 18.58  ?  104 ILE A CD1 1 
ATOM   763  N  N   . TYR A 1 105 ? 23.828  23.358  6.061   1.00 14.84  ?  105 TYR A N   1 
ATOM   764  C  CA  . TYR A 1 105 ? 24.995  23.966  6.672   1.00 16.36  ?  105 TYR A CA  1 
ATOM   765  C  C   . TYR A 1 105 ? 25.036  25.457  6.324   1.00 16.86  ?  105 TYR A C   1 
ATOM   766  O  O   . TYR A 1 105 ? 25.192  25.822  5.145   1.00 16.68  ?  105 TYR A O   1 
ATOM   767  C  CB  . TYR A 1 105 ? 26.270  23.295  6.177   1.00 17.36  ?  105 TYR A CB  1 
ATOM   768  C  CG  . TYR A 1 105 ? 27.531  23.940  6.724   1.00 17.50  ?  105 TYR A CG  1 
ATOM   769  C  CD1 . TYR A 1 105 ? 28.053  23.545  7.943   1.00 19.22  ?  105 TYR A CD1 1 
ATOM   770  C  CD2 . TYR A 1 105 ? 28.148  25.005  6.068   1.00 19.62  ?  105 TYR A CD2 1 
ATOM   771  C  CE1 . TYR A 1 105 ? 29.212  24.109  8.453   1.00 20.27  ?  105 TYR A CE1 1 
ATOM   772  C  CE2 . TYR A 1 105 ? 29.284  25.618  6.597   1.00 19.29  ?  105 TYR A CE2 1 
ATOM   773  C  CZ  . TYR A 1 105 ? 29.830  25.152  7.779   1.00 21.36  ?  105 TYR A CZ  1 
ATOM   774  O  OH  . TYR A 1 105 ? 30.930  25.755  8.333   1.00 20.77  ?  105 TYR A OH  1 
ATOM   775  N  N   . ASP A 1 106 ? 24.985  26.291  7.374   1.00 16.42  ?  106 ASP A N   1 
ATOM   776  C  CA  . ASP A 1 106 ? 24.920  27.741  7.221   1.00 13.65  ?  106 ASP A CA  1 
ATOM   777  C  C   . ASP A 1 106 ? 25.826  28.423  8.255   1.00 16.23  ?  106 ASP A C   1 
ATOM   778  O  O   . ASP A 1 106 ? 25.680  29.614  8.491   1.00 15.57  ?  106 ASP A O   1 
ATOM   779  C  CB  . ASP A 1 106 ? 23.492  28.245  7.324   1.00 13.77  ?  106 ASP A CB  1 
ATOM   780  C  CG  . ASP A 1 106 ? 22.781  27.964  8.642   1.00 15.53  ?  106 ASP A CG  1 
ATOM   781  O  OD1 . ASP A 1 106 ? 23.401  27.309  9.520   1.00 15.94  ?  106 ASP A OD1 1 
ATOM   782  O  OD2 . ASP A 1 106 ? 21.630  28.399  8.783   1.00 16.62  -1 106 ASP A OD2 1 
ATOM   783  N  N   . LEU A 1 107 ? 26.812  27.697  8.789   1.00 17.09  ?  107 LEU A N   1 
ATOM   784  C  CA  . LEU A 1 107 ? 27.660  28.211  9.850   1.00 19.38  ?  107 LEU A CA  1 
ATOM   785  C  C   . LEU A 1 107 ? 28.767  29.132  9.304   1.00 20.23  ?  107 LEU A C   1 
ATOM   786  O  O   . LEU A 1 107 ? 29.372  29.836  10.099  1.00 22.18  ?  107 LEU A O   1 
ATOM   787  C  CB  . LEU A 1 107 ? 28.287  27.073  10.642  1.00 19.90  ?  107 LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 107 ? 27.357  26.054  11.309  1.00 25.18  ?  107 LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 107 ? 28.168  25.273  12.361  1.00 25.55  ?  107 LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 107 ? 26.174  26.657  11.923  1.00 26.38  ?  107 LEU A CD2 1 
ATOM   791  N  N   . SER A 1 108 ? 29.038  29.132  7.990   1.00 18.83  ?  108 SER A N   1 
ATOM   792  C  CA  . SER A 1 108 ? 30.155  29.882  7.433   1.00 21.86  ?  108 SER A CA  1 
ATOM   793  C  C   . SER A 1 108 ? 29.751  31.293  7.012   1.00 22.52  ?  108 SER A C   1 
ATOM   794  O  O   . SER A 1 108 ? 30.590  32.004  6.480   1.00 23.20  ?  108 SER A O   1 
ATOM   795  C  CB  . SER A 1 108 ? 30.822  29.149  6.287   1.00 22.53  ?  108 SER A CB  1 
ATOM   796  O  OG  . SER A 1 108 ? 31.575  28.061  6.781   1.00 24.19  ?  108 SER A OG  1 
ATOM   797  N  N   . VAL A 1 109 ? 28.493  31.681  7.234   1.00 22.64  ?  109 VAL A N   1 
ATOM   798  C  CA  . VAL A 1 109 ? 28.067  33.060  7.075   1.00 24.69  ?  109 VAL A CA  1 
ATOM   799  C  C   . VAL A 1 109 ? 27.401  33.491  8.379   1.00 21.70  ?  109 VAL A C   1 
ATOM   800  O  O   . VAL A 1 109 ? 26.788  32.677  9.062   1.00 20.67  ?  109 VAL A O   1 
ATOM   801  C  CB  . VAL A 1 109 ? 27.122  33.285  5.863   1.00 30.65  ?  109 VAL A CB  1 
ATOM   802  C  CG1 . VAL A 1 109 ? 27.807  32.947  4.545   1.00 31.19  ?  109 VAL A CG1 1 
ATOM   803  C  CG2 . VAL A 1 109 ? 25.835  32.486  5.962   1.00 30.72  ?  109 VAL A CG2 1 
ATOM   804  N  N   . GLY A 1 110 ? 27.618  34.754  8.767   1.00 19.94  ?  110 GLY A N   1 
ATOM   805  C  CA  . GLY A 1 110 ? 27.103  35.299  10.018  1.00 21.67  ?  110 GLY A CA  1 
ATOM   806  C  C   . GLY A 1 110 ? 27.886  34.782  11.217  1.00 21.71  ?  110 GLY A C   1 
ATOM   807  O  O   . GLY A 1 110 ? 29.119  34.711  11.205  1.00 24.38  ?  110 GLY A O   1 
ATOM   808  N  N   . ASP A 1 111 ? 27.146  34.257  12.193  1.00 21.91  ?  111 ASP A N   1 
ATOM   809  C  CA  . ASP A 1 111 ? 27.721  33.830  13.460  1.00 22.21  ?  111 ASP A CA  1 
ATOM   810  C  C   . ASP A 1 111 ? 27.617  32.307  13.607  1.00 18.23  ?  111 ASP A C   1 
ATOM   811  O  O   . ASP A 1 111 ? 26.513  31.802  13.763  1.00 21.79  ?  111 ASP A O   1 
ATOM   812  C  CB  . ASP A 1 111 ? 27.036  34.600  14.585  1.00 22.61  ?  111 ASP A CB  1 
ATOM   813  C  CG  . ASP A 1 111 ? 27.614  34.388  15.972  1.00 25.84  ?  111 ASP A CG  1 
ATOM   814  O  OD1 . ASP A 1 111 ? 28.392  33.421  16.148  1.00 26.85  ?  111 ASP A OD1 1 
ATOM   815  O  OD2 . ASP A 1 111 ? 27.264  35.196  16.877  1.00 27.50  -1 111 ASP A OD2 1 
ATOM   816  N  N   . ALA A 1 112 ? 28.771  31.610  13.600  1.00 17.15  ?  112 ALA A N   1 
ATOM   817  C  CA  . ALA A 1 112 ? 28.823  30.159  13.631  1.00 20.52  ?  112 ALA A CA  1 
ATOM   818  C  C   . ALA A 1 112 ? 28.291  29.575  14.938  1.00 24.44  ?  112 ALA A C   1 
ATOM   819  O  O   . ALA A 1 112 ? 28.002  28.371  14.995  1.00 22.75  ?  112 ALA A O   1 
ATOM   820  C  CB  . ALA A 1 112 ? 30.219  29.674  13.389  1.00 21.60  ?  112 ALA A CB  1 
ATOM   821  N  N   . ASN A 1 113 ? 28.216  30.409  15.987  1.00 21.40  ?  113 ASN A N   1 
ATOM   822  C  CA  . ASN A 1 113 ? 27.930  29.941  17.331  1.00 25.09  ?  113 ASN A CA  1 
ATOM   823  C  C   . ASN A 1 113 ? 26.429  29.995  17.604  1.00 22.94  ?  113 ASN A C   1 
ATOM   824  O  O   . ASN A 1 113 ? 25.983  29.519  18.641  1.00 23.87  ?  113 ASN A O   1 
ATOM   825  C  CB  . ASN A 1 113 ? 28.730  30.744  18.354  1.00 27.39  ?  113 ASN A CB  1 
ATOM   826  C  CG  . ASN A 1 113 ? 30.214  30.519  18.168  1.00 32.02  ?  113 ASN A CG  1 
ATOM   827  O  OD1 . ASN A 1 113 ? 30.667  29.373  18.138  1.00 38.96  ?  113 ASN A OD1 1 
ATOM   828  N  ND2 . ASN A 1 113 ? 30.984  31.563  17.936  1.00 38.33  ?  113 ASN A ND2 1 
ATOM   829  N  N   . VAL A 1 114 ? 25.644  30.575  16.698  1.00 20.15  ?  114 VAL A N   1 
ATOM   830  C  CA  . VAL A 1 114 ? 24.203  30.631  16.883  1.00 21.45  ?  114 VAL A CA  1 
ATOM   831  C  C   . VAL A 1 114 ? 23.531  29.669  15.907  1.00 20.17  ?  114 VAL A C   1 
ATOM   832  O  O   . VAL A 1 114 ? 23.727  29.787  14.694  1.00 18.03  ?  114 VAL A O   1 
ATOM   833  C  CB  . VAL A 1 114 ? 23.673  32.058  16.675  1.00 23.84  ?  114 VAL A CB  1 
ATOM   834  C  CG1 . VAL A 1 114 ? 22.149  32.124  16.780  1.00 23.31  ?  114 VAL A CG1 1 
ATOM   835  C  CG2 . VAL A 1 114 ? 24.351  33.047  17.613  1.00 25.82  ?  114 VAL A CG2 1 
ATOM   836  N  N   . ARG A 1 115 ? 22.735  28.735  16.447  1.00 18.69  ?  115 ARG A N   1 
ATOM   837  C  CA  . ARG A 1 115 ? 22.025  27.767  15.626  1.00 16.65  ?  115 ARG A CA  1 
ATOM   838  C  C   . ARG A 1 115 ? 20.600  27.624  16.131  1.00 17.58  ?  115 ARG A C   1 
ATOM   839  O  O   . ARG A 1 115 ? 20.305  27.940  17.285  1.00 19.46  ?  115 ARG A O   1 
ATOM   840  C  CB  . ARG A 1 115 ? 22.699  26.391  15.698  1.00 16.98  ?  115 ARG A CB  1 
ATOM   841  C  CG  . ARG A 1 115 ? 24.186  26.357  15.398  1.00 17.21  ?  115 ARG A CG  1 
ATOM   842  C  CD  . ARG A 1 115 ? 24.987  26.339  16.641  1.00 19.52  ?  115 ARG A CD  1 
ATOM   843  N  NE  . ARG A 1 115 ? 26.427  26.356  16.373  1.00 21.61  ?  115 ARG A NE  1 
ATOM   844  C  CZ  . ARG A 1 115 ? 27.329  25.790  17.171  1.00 23.65  ?  115 ARG A CZ  1 
ATOM   845  N  NH1 . ARG A 1 115 ? 26.963  25.076  18.234  1.00 23.35  1  115 ARG A NH1 1 
ATOM   846  N  NH2 . ARG A 1 115 ? 28.611  25.961  16.905  1.00 23.91  ?  115 ARG A NH2 1 
ATOM   847  N  N   . PRO A 1 116 ? 19.649  27.171  15.286  1.00 17.14  ?  116 PRO A N   1 
ATOM   848  C  CA  . PRO A 1 116 ? 18.301  26.909  15.750  1.00 16.67  ?  116 PRO A CA  1 
ATOM   849  C  C   . PRO A 1 116 ? 18.323  25.897  16.892  1.00 16.99  ?  116 PRO A C   1 
ATOM   850  O  O   . PRO A 1 116 ? 19.024  24.883  16.828  1.00 19.54  ?  116 PRO A O   1 
ATOM   851  C  CB  . PRO A 1 116 ? 17.577  26.455  14.489  1.00 18.37  ?  116 PRO A CB  1 
ATOM   852  C  CG  . PRO A 1 116 ? 18.389  27.078  13.364  1.00 16.43  ?  116 PRO A CG  1 
ATOM   853  C  CD  . PRO A 1 116 ? 19.789  26.979  13.831  1.00 16.02  ?  116 PRO A CD  1 
ATOM   854  N  N   . ASP A 1 117 ? 17.629  26.265  17.972  1.00 15.23  ?  117 ASP A N   1 
ATOM   855  C  CA  . ASP A 1 117 ? 17.659  25.564  19.245  1.00 15.30  ?  117 ASP A CA  1 
ATOM   856  C  C   . ASP A 1 117 ? 16.219  25.317  19.677  1.00 14.79  ?  117 ASP A C   1 
ATOM   857  O  O   . ASP A 1 117 ? 15.277  25.549  18.912  1.00 15.17  ?  117 ASP A O   1 
ATOM   858  C  CB  . ASP A 1 117 ? 18.476  26.343  20.261  1.00 17.31  ?  117 ASP A CB  1 
ATOM   859  C  CG  . ASP A 1 117 ? 17.941  27.749  20.560  1.00 19.25  ?  117 ASP A CG  1 
ATOM   860  O  OD1 . ASP A 1 117 ? 16.899  28.146  19.992  1.00 17.38  ?  117 ASP A OD1 1 
ATOM   861  O  OD2 . ASP A 1 117 ? 18.589  28.431  21.361  1.00 21.77  -1 117 ASP A OD2 1 
ATOM   862  N  N   . LEU A 1 118 ? 16.037  24.785  20.893  1.00 16.66  ?  118 LEU A N   1 
ATOM   863  C  CA  . LEU A 1 118 ? 14.698  24.501  21.410  1.00 17.47  ?  118 LEU A CA  1 
ATOM   864  C  C   . LEU A 1 118 ? 13.773  25.706  21.299  1.00 17.45  ?  118 LEU A C   1 
ATOM   865  O  O   . LEU A 1 118 ? 12.621  25.573  20.861  1.00 17.73  ?  118 LEU A O   1 
ATOM   866  C  CB  . LEU A 1 118 ? 14.722  24.038  22.873  1.00 17.14  ?  118 LEU A CB  1 
ATOM   867  C  CG  . LEU A 1 118 ? 15.326  22.663  23.143  1.00 17.19  ?  118 LEU A CG  1 
ATOM   868  C  CD1 . LEU A 1 118 ? 15.310  22.485  24.644  1.00 19.42  ?  118 LEU A CD1 1 
ATOM   869  C  CD2 . LEU A 1 118 ? 14.605  21.536  22.447  1.00 18.09  ?  118 LEU A CD2 1 
ATOM   870  N  N   . ALA A 1 119 ? 14.287  26.871  21.708  1.00 18.57  ?  119 ALA A N   1 
ATOM   871  C  CA  . ALA A 1 119 ? 13.481  28.101  21.714  1.00 17.50  ?  119 ALA A CA  1 
ATOM   872  C  C   . ALA A 1 119 ? 13.120  28.526  20.291  1.00 16.67  ?  119 ALA A C   1 
ATOM   873  O  O   . ALA A 1 119 ? 11.991  28.934  20.012  1.00 16.71  ?  119 ALA A O   1 
ATOM   874  C  CB  . ALA A 1 119 ? 14.249  29.216  22.434  1.00 19.19  ?  119 ALA A CB  1 
ATOM   875  N  N   . MET A 1 120 ? 14.082  28.458  19.364  1.00 18.57  ?  120 MET A N   1 
ATOM   876  C  CA  . MET A 1 120 ? 13.808  28.929  18.015  1.00 18.56  ?  120 MET A CA  1 
ATOM   877  C  C   . MET A 1 120 ? 12.792  28.027  17.310  1.00 16.57  ?  120 MET A C   1 
ATOM   878  O  O   . MET A 1 120 ? 11.986  28.496  16.505  1.00 16.53  ?  120 MET A O   1 
ATOM   879  C  CB  . MET A 1 120 ? 15.093  29.057  17.187  1.00 20.27  ?  120 MET A CB  1 
ATOM   880  C  CG  . MET A 1 120 ? 14.892  29.965  15.992  1.00 25.71  ?  120 MET A CG  1 
ATOM   881  S  SD  . MET A 1 120 ? 16.302  30.051  14.881  1.00 26.70  ?  120 MET A SD  1 
ATOM   882  C  CE  . MET A 1 120 ? 17.479  30.920  15.907  1.00 31.94  ?  120 MET A CE  1 
ATOM   883  N  N   . GLY A 1 121 ? 12.833  26.711  17.593  1.00 16.14  ?  121 GLY A N   1 
ATOM   884  C  CA  . GLY A 1 121 ? 11.858  25.820  16.982  1.00 15.98  ?  121 GLY A CA  1 
ATOM   885  C  C   . GLY A 1 121 ? 10.448  26.128  17.458  1.00 16.11  ?  121 GLY A C   1 
ATOM   886  O  O   . GLY A 1 121 ? 9.487   26.098  16.696  1.00 15.18  ?  121 GLY A O   1 
ATOM   887  N  N   . ARG A 1 122 ? 10.330  26.415  18.754  1.00 18.43  ?  122 ARG A N   1 
ATOM   888  C  CA  . ARG A 1 122 ? 9.049   26.807  19.310  1.00 19.12  ?  122 ARG A CA  1 
ATOM   889  C  C   . ARG A 1 122 ? 8.554   28.096  18.657  1.00 17.41  ?  122 ARG A C   1 
ATOM   890  O  O   . ARG A 1 122 ? 7.358   28.194  18.367  1.00 17.86  ?  122 ARG A O   1 
ATOM   891  C  CB  . ARG A 1 122 ? 9.206   26.987  20.830  1.00 20.95  ?  122 ARG A CB  1 
ATOM   892  C  CG  . ARG A 1 122 ? 7.943   27.482  21.499  1.00 25.40  ?  122 ARG A CG  1 
ATOM   893  C  CD  . ARG A 1 122 ? 8.317   27.887  22.893  1.00 30.51  ?  122 ARG A CD  1 
ATOM   894  N  NE  . ARG A 1 122 ? 7.468   27.086  23.757  1.00 39.27  ?  122 ARG A NE  1 
ATOM   895  C  CZ  . ARG A 1 122 ? 6.168   27.286  23.958  1.00 38.37  ?  122 ARG A CZ  1 
ATOM   896  N  NH1 . ARG A 1 122 ? 5.457   28.333  23.479  1.00 37.84  1  122 ARG A NH1 1 
ATOM   897  N  NH2 . ARG A 1 122 ? 5.604   26.361  24.677  1.00 36.52  ?  122 ARG A NH2 1 
ATOM   898  N  N   . ARG A 1 123 ? 9.440   29.090  18.488  1.00 18.02  ?  123 ARG A N   1 
ATOM   899  C  CA  . ARG A 1 123 ? 9.077   30.349  17.848  1.00 21.50  ?  123 ARG A CA  1 
ATOM   900  C  C   . ARG A 1 123 ? 8.523   30.132  16.442  1.00 20.42  ?  123 ARG A C   1 
ATOM   901  O  O   . ARG A 1 123 ? 7.590   30.809  16.044  1.00 18.43  ?  123 ARG A O   1 
ATOM   902  C  CB  . ARG A 1 123 ? 10.254  31.342  17.812  1.00 26.03  ?  123 ARG A CB  1 
ATOM   903  C  CG  . ARG A 1 123 ? 10.008  32.593  16.960  1.00 40.58  ?  123 ARG A CG  1 
ATOM   904  C  CD  . ARG A 1 123 ? 11.011  33.823  16.994  1.00 50.10  ?  123 ARG A CD  1 
ATOM   905  N  NE  . ARG A 1 123 ? 11.429  34.471  15.720  1.00 55.34  ?  123 ARG A NE  1 
ATOM   906  C  CZ  . ARG A 1 123 ? 10.768  34.704  14.531  1.00 55.10  ?  123 ARG A CZ  1 
ATOM   907  N  NH1 . ARG A 1 123 ? 9.501   34.287  14.305  1.00 45.18  1  123 ARG A NH1 1 
ATOM   908  N  NH2 . ARG A 1 123 ? 11.416  35.343  13.535  1.00 38.19  ?  123 ARG A NH2 1 
ATOM   909  N  N   . ALA A 1 124 ? 9.111   29.220  15.641  1.00 17.74  ?  124 ALA A N   1 
ATOM   910  C  CA  . ALA A 1 124 ? 8.589   28.975  14.307  1.00 15.90  ?  124 ALA A CA  1 
ATOM   911  C  C   . ALA A 1 124 ? 7.186   28.407  14.371  1.00 15.92  ?  124 ALA A C   1 
ATOM   912  O  O   . ALA A 1 124 ? 6.350   28.746  13.536  1.00 18.20  ?  124 ALA A O   1 
ATOM   913  C  CB  . ALA A 1 124 ? 9.528   28.060  13.518  1.00 17.05  ?  124 ALA A CB  1 
ATOM   914  N  N   . CYS A 1 125 ? 6.899   27.540  15.353  1.00 16.49  ?  125 CYS A N   1 
ATOM   915  C  CA  . CYS A 1 125 ? 5.551   27.002  15.497  1.00 16.50  ?  125 CYS A CA  1 
ATOM   916  C  C   . CYS A 1 125 ? 4.562   28.103  15.888  1.00 17.20  ?  125 CYS A C   1 
ATOM   917  O  O   . CYS A 1 125 ? 3.443   28.139  15.397  1.00 17.34  ?  125 CYS A O   1 
ATOM   918  C  CB  . CYS A 1 125 ? 5.501   25.943  16.583  1.00 18.46  ?  125 CYS A CB  1 
ATOM   919  S  SG  . CYS A 1 125 ? 6.506   24.478  16.205  1.00 20.66  ?  125 CYS A SG  1 
ATOM   920  N  N   . GLU A 1 126 ? 4.970   28.990  16.804  1.00 17.69  ?  126 GLU A N   1 
ATOM   921  C  CA  . GLU A 1 126 ? 4.142   30.123  17.244  1.00 19.57  ?  126 GLU A CA  1 
ATOM   922  C  C   . GLU A 1 126 ? 3.766   31.014  16.060  1.00 19.22  ?  126 GLU A C   1 
ATOM   923  O  O   . GLU A 1 126 ? 2.648   31.527  15.980  1.00 21.54  ?  126 GLU A O   1 
ATOM   924  C  CB  . GLU A 1 126 ? 4.901   30.944  18.296  1.00 20.15  ?  126 GLU A CB  1 
ATOM   925  C  CG  . GLU A 1 126 ? 5.046   30.212  19.635  1.00 24.83  ?  126 GLU A CG  1 
ATOM   926  C  CD  . GLU A 1 126 ? 5.756   31.019  20.713  1.00 26.45  ?  126 GLU A CD  1 
ATOM   927  O  OE1 . GLU A 1 126 ? 6.061   32.186  20.443  1.00 28.26  ?  126 GLU A OE1 1 
ATOM   928  O  OE2 . GLU A 1 126 ? 5.969   30.502  21.815  1.00 28.05  -1 126 GLU A OE2 1 
ATOM   929  N  N   . ALA A 1 127 ? 4.703   31.168  15.115  1.00 19.19  ?  127 ALA A N   1 
ATOM   930  C  CA  . ALA A 1 127 ? 4.524   32.005  13.943  1.00 17.16  ?  127 ALA A CA  1 
ATOM   931  C  C   . ALA A 1 127 ? 3.736   31.358  12.816  1.00 19.40  ?  127 ALA A C   1 
ATOM   932  O  O   . ALA A 1 127 ? 3.468   32.033  11.832  1.00 18.70  ?  127 ALA A O   1 
ATOM   933  C  CB  . ALA A 1 127 ? 5.867   32.423  13.442  1.00 17.62  ?  127 ALA A CB  1 
ATOM   934  N  N   . ALA A 1 128 ? 3.374   30.069  12.912  1.00 17.26  ?  128 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 128 ? 2.834   29.369  11.753  1.00 19.37  ?  128 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 128 ? 1.418   29.826  11.438  1.00 20.33  ?  128 ALA A C   1 
ATOM   937  O  O   . ALA A 1 128 ? 0.541   29.820  12.299  1.00 21.92  ?  128 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 128 ? 2.873   27.855  11.975  1.00 19.97  ?  128 ALA A CB  1 
ATOM   939  N  N   . LYS A 1 129 ? 1.177   30.205  10.199  1.00 18.94  ?  129 LYS A N   1 
ATOM   940  C  CA  . LYS A 1 129 ? -0.139  30.675  9.829   1.00 21.23  ?  129 LYS A CA  1 
ATOM   941  C  C   . LYS A 1 129 ? -0.508  30.227  8.425   1.00 21.31  ?  129 LYS A C   1 
ATOM   942  O  O   . LYS A 1 129 ? 0.348   29.837  7.637   1.00 19.11  ?  129 LYS A O   1 
ATOM   943  C  CB  . LYS A 1 129 ? -0.158  32.202  9.969   1.00 23.87  ?  129 LYS A CB  1 
ATOM   944  C  CG  . LYS A 1 129 ? 0.828   32.951  9.127   1.00 29.12  ?  129 LYS A CG  1 
ATOM   945  C  CD  . LYS A 1 129 ? 0.812   34.450  9.397   1.00 34.22  ?  129 LYS A CD  1 
ATOM   946  C  CE  . LYS A 1 129 ? 1.494   35.239  8.335   1.00 36.29  ?  129 LYS A CE  1 
ATOM   947  N  NZ  . LYS A 1 129 ? 2.946   35.165  8.466   1.00 43.98  1  129 LYS A NZ  1 
ATOM   948  N  N   . PRO A 1 130 ? -1.814  30.303  8.087   1.00 21.99  ?  130 PRO A N   1 
ATOM   949  C  CA  . PRO A 1 130 ? -2.273  30.054  6.730   1.00 22.24  ?  130 PRO A CA  1 
ATOM   950  C  C   . PRO A 1 130 ? -1.976  31.229  5.814   1.00 23.73  ?  130 PRO A C   1 
ATOM   951  O  O   . PRO A 1 130 ? -1.427  32.224  6.258   1.00 23.23  ?  130 PRO A O   1 
ATOM   952  C  CB  . PRO A 1 130 ? -3.761  29.770  6.870   1.00 23.14  ?  130 PRO A CB  1 
ATOM   953  C  CG  . PRO A 1 130 ? -4.134  30.526  8.127   1.00 24.95  ?  130 PRO A CG  1 
ATOM   954  C  CD  . PRO A 1 130 ? -2.916  30.654  9.004   1.00 24.46  ?  130 PRO A CD  1 
ATOM   955  N  N   . GLY A 1 131 ? -2.249  31.029  4.526   1.00 22.95  ?  131 GLY A N   1 
ATOM   956  C  CA  . GLY A 1 131 ? -2.115  32.082  3.543   1.00 24.26  ?  131 GLY A CA  1 
ATOM   957  C  C   . GLY A 1 131 ? -0.677  32.223  3.068   1.00 25.13  ?  131 GLY A C   1 
ATOM   958  O  O   . GLY A 1 131 ? 0.186   31.394  3.394   1.00 23.61  ?  131 GLY A O   1 
ATOM   959  N  N   . PRO A 1 132 ? -0.375  33.315  2.327   1.00 26.58  ?  132 PRO A N   1 
ATOM   960  C  CA  . PRO A 1 132 ? 0.955   33.509  1.762   1.00 27.01  ?  132 PRO A CA  1 
ATOM   961  C  C   . PRO A 1 132 ? 2.016   33.697  2.835   1.00 24.52  ?  132 PRO A C   1 
ATOM   962  O  O   . PRO A 1 132 ? 1.748   34.248  3.881   1.00 22.11  ?  132 PRO A O   1 
ATOM   963  C  CB  . PRO A 1 132 ? 0.813   34.702  0.814   1.00 29.07  ?  132 PRO A CB  1 
ATOM   964  C  CG  . PRO A 1 132 ? -0.482  35.363  1.234   1.00 31.39  ?  132 PRO A CG  1 
ATOM   965  C  CD  . PRO A 1 132 ? -1.325  34.392  1.989   1.00 31.13  ?  132 PRO A CD  1 
ATOM   966  N  N   . PHE A 1 133 ? 3.218   33.190  2.564   1.00 22.06  ?  133 PHE A N   1 
ATOM   967  C  CA  . PHE A 1 133 ? 4.334   33.371  3.466   1.00 19.71  ?  133 PHE A CA  1 
ATOM   968  C  C   . PHE A 1 133 ? 5.464   34.031  2.691   1.00 19.52  ?  133 PHE A C   1 
ATOM   969  O  O   . PHE A 1 133 ? 5.522   33.974  1.466   1.00 19.68  ?  133 PHE A O   1 
ATOM   970  C  CB  . PHE A 1 133 ? 4.785   32.043  4.097   1.00 19.86  ?  133 PHE A CB  1 
ATOM   971  C  CG  . PHE A 1 133 ? 5.058   30.893  3.126   1.00 16.66  ?  133 PHE A CG  1 
ATOM   972  C  CD1 . PHE A 1 133 ? 6.307   30.722  2.546   1.00 16.95  ?  133 PHE A CD1 1 
ATOM   973  C  CD2 . PHE A 1 133 ? 4.062   29.977  2.832   1.00 17.03  ?  133 PHE A CD2 1 
ATOM   974  C  CE1 . PHE A 1 133 ? 6.556   29.682  1.666   1.00 16.79  ?  133 PHE A CE1 1 
ATOM   975  C  CE2 . PHE A 1 133 ? 4.319   28.924  1.965   1.00 17.85  ?  133 PHE A CE2 1 
ATOM   976  C  CZ  . PHE A 1 133 ? 5.557   28.788  1.375   1.00 17.87  ?  133 PHE A CZ  1 
ATOM   977  N  N   . GLU A 1 134 ? 6.400   34.590  3.439   1.00 19.79  ?  134 GLU A N   1 
ATOM   978  C  CA  . GLU A 1 134 ? 7.530   35.263  2.838   1.00 21.00  ?  134 GLU A CA  1 
ATOM   979  C  C   . GLU A 1 134 ? 8.512   34.233  2.286   1.00 19.50  ?  134 GLU A C   1 
ATOM   980  O  O   . GLU A 1 134 ? 8.657   33.141  2.844   1.00 19.52  ?  134 GLU A O   1 
ATOM   981  C  CB  . GLU A 1 134 ? 8.259   36.091  3.897   1.00 28.78  ?  134 GLU A CB  1 
ATOM   982  C  CG  . GLU A 1 134 ? 7.470   37.230  4.534   1.00 39.71  ?  134 GLU A CG  1 
ATOM   983  C  CD  . GLU A 1 134 ? 8.389   37.902  5.567   1.00 53.74  ?  134 GLU A CD  1 
ATOM   984  O  OE1 . GLU A 1 134 ? 7.939   37.987  6.732   1.00 67.11  ?  134 GLU A OE1 1 
ATOM   985  O  OE2 . GLU A 1 134 ? 9.554   38.295  5.232   1.00 54.70  -1 134 GLU A OE2 1 
ATOM   986  N  N   . ARG A 1 135 ? 9.255   34.635  1.256   1.00 19.07  ?  135 ARG A N   1 
ATOM   987  C  CA  . ARG A 1 135 ? 10.265  33.821  0.593   1.00 18.52  ?  135 ARG A CA  1 
ATOM   988  C  C   . ARG A 1 135 ? 11.556  34.612  0.546   1.00 20.44  ?  135 ARG A C   1 
ATOM   989  O  O   . ARG A 1 135 ? 11.577  35.752  0.991   1.00 20.57  ?  135 ARG A O   1 
ATOM   990  C  CB  . ARG A 1 135 ? 9.790   33.394  -0.805  1.00 19.12  ?  135 ARG A CB  1 
ATOM   991  C  CG  . ARG A 1 135 ? 8.520   32.551  -0.709  1.00 17.09  ?  135 ARG A CG  1 
ATOM   992  C  CD  . ARG A 1 135 ? 7.311   33.210  -1.332  1.00 19.68  ?  135 ARG A CD  1 
ATOM   993  N  NE  . ARG A 1 135 ? 7.456   33.361  -2.777  1.00 20.75  ?  135 ARG A NE  1 
ATOM   994  C  CZ  . ARG A 1 135 ? 6.829   34.277  -3.534  1.00 30.24  ?  135 ARG A CZ  1 
ATOM   995  N  NH1 . ARG A 1 135 ? 5.895   35.056  -3.000  1.00 28.65  1  135 ARG A NH1 1 
ATOM   996  N  NH2 . ARG A 1 135 ? 7.098   34.377  -4.832  1.00 28.62  ?  135 ARG A NH2 1 
ATOM   997  N  N   . GLY A 1 136 ? 12.633  33.980  0.091   1.00 18.38  ?  136 GLY A N   1 
ATOM   998  C  CA  . GLY A 1 136 ? 13.962  34.565  0.055   1.00 18.94  ?  136 GLY A CA  1 
ATOM   999  C  C   . GLY A 1 136 ? 14.798  34.140  1.252   1.00 19.50  ?  136 GLY A C   1 
ATOM   1000 O  O   . GLY A 1 136 ? 14.730  33.000  1.717   1.00 18.79  ?  136 GLY A O   1 
ATOM   1001 N  N   . ARG A 1 137 ? 15.573  35.087  1.790   1.00 17.90  ?  137 ARG A N   1 
ATOM   1002 C  CA  . ARG A 1 137 ? 16.453  34.822  2.912   1.00 20.63  ?  137 ARG A CA  1 
ATOM   1003 C  C   . ARG A 1 137 ? 15.680  35.009  4.216   1.00 21.10  ?  137 ARG A C   1 
ATOM   1004 O  O   . ARG A 1 137 ? 15.830  36.007  4.894   1.00 19.51  ?  137 ARG A O   1 
ATOM   1005 C  CB  . ARG A 1 137 ? 17.691  35.709  2.781   1.00 25.10  ?  137 ARG A CB  1 
ATOM   1006 C  CG  . ARG A 1 137 ? 18.481  35.138  1.619   1.00 33.72  ?  137 ARG A CG  1 
ATOM   1007 C  CD  . ARG A 1 137 ? 19.897  35.627  1.584   1.00 41.67  ?  137 ARG A CD  1 
ATOM   1008 N  NE  . ARG A 1 137 ? 20.063  37.046  1.254   1.00 53.98  ?  137 ARG A NE  1 
ATOM   1009 C  CZ  . ARG A 1 137 ? 19.552  37.723  0.230   1.00 63.60  ?  137 ARG A CZ  1 
ATOM   1010 N  NH1 . ARG A 1 137 ? 18.525  37.250  -0.468  1.00 65.99  1  137 ARG A NH1 1 
ATOM   1011 N  NH2 . ARG A 1 137 ? 20.070  38.907  -0.064  1.00 64.78  ?  137 ARG A NH2 1 
ATOM   1012 N  N   . VAL A 1 138 ? 14.832  34.030  4.527   1.00 18.09  ?  138 VAL A N   1 
ATOM   1013 C  CA  . VAL A 1 138 ? 13.987  34.018  5.697   1.00 18.09  ?  138 VAL A CA  1 
ATOM   1014 C  C   . VAL A 1 138 ? 13.901  32.578  6.202   1.00 19.77  ?  138 VAL A C   1 
ATOM   1015 O  O   . VAL A 1 138 ? 14.078  31.638  5.420   1.00 17.52  ?  138 VAL A O   1 
ATOM   1016 C  CB  . VAL A 1 138 ? 12.628  34.592  5.277   1.00 22.29  ?  138 VAL A CB  1 
ATOM   1017 C  CG1 . VAL A 1 138 ? 11.870  33.665  4.339   1.00 22.89  ?  138 VAL A CG1 1 
ATOM   1018 C  CG2 . VAL A 1 138 ? 11.806  34.953  6.491   1.00 30.42  ?  138 VAL A CG2 1 
ATOM   1019 N  N   . GLY A 1 139 ? 13.596  32.406  7.495   1.00 19.31  ?  139 GLY A N   1 
ATOM   1020 C  CA  . GLY A 1 139 ? 13.425  31.088  8.079   1.00 15.71  ?  139 GLY A CA  1 
ATOM   1021 C  C   . GLY A 1 139 ? 14.637  30.207  7.791   1.00 15.98  ?  139 GLY A C   1 
ATOM   1022 O  O   . GLY A 1 139 ? 15.785  30.622  7.960   1.00 15.81  ?  139 GLY A O   1 
ATOM   1023 N  N   . GLY A 1 140 ? 14.364  28.976  7.314   1.00 16.94  ?  140 GLY A N   1 
ATOM   1024 C  CA  . GLY A 1 140 ? 15.438  28.054  7.033   1.00 17.12  ?  140 GLY A CA  1 
ATOM   1025 C  C   . GLY A 1 140 ? 16.359  28.495  5.903   1.00 16.42  ?  140 GLY A C   1 
ATOM   1026 O  O   . GLY A 1 140 ? 17.445  27.960  5.791   1.00 16.90  ?  140 GLY A O   1 
ATOM   1027 N  N   . GLY A 1 141 ? 15.930  29.460  5.087   1.00 17.10  ?  141 GLY A N   1 
ATOM   1028 C  CA  . GLY A 1 141 ? 16.751  29.980  4.007   1.00 16.11  ?  141 GLY A CA  1 
ATOM   1029 C  C   . GLY A 1 141 ? 17.575  31.227  4.343   1.00 16.80  ?  141 GLY A C   1 
ATOM   1030 O  O   . GLY A 1 141 ? 18.299  31.716  3.463   1.00 15.83  ?  141 GLY A O   1 
ATOM   1031 N  N   . THR A 1 142 ? 17.550  31.693  5.612   1.00 17.80  ?  142 THR A N   1 
ATOM   1032 C  CA  . THR A 1 142 ? 18.160  32.979  5.994   1.00 15.61  ?  142 THR A CA  1 
ATOM   1033 C  C   . THR A 1 142 ? 19.645  32.989  5.645   1.00 17.38  ?  142 THR A C   1 
ATOM   1034 O  O   . THR A 1 142 ? 20.150  33.973  5.094   1.00 16.90  ?  142 THR A O   1 
ATOM   1035 C  CB  . THR A 1 142 ? 17.970  33.257  7.488   1.00 15.86  ?  142 THR A CB  1 
ATOM   1036 O  OG1 . THR A 1 142 ? 16.566  33.247  7.750   1.00 13.84  ?  142 THR A OG1 1 
ATOM   1037 C  CG2 . THR A 1 142 ? 18.544  34.619  7.859   1.00 17.03  ?  142 THR A CG2 1 
ATOM   1038 N  N   . GLY A 1 143 ? 20.355  31.896  5.956   1.00 15.76  ?  143 GLY A N   1 
ATOM   1039 C  CA  . GLY A 1 143 ? 21.797  31.805  5.759   1.00 16.45  ?  143 GLY A CA  1 
ATOM   1040 C  C   . GLY A 1 143 ? 22.237  30.978  4.543   1.00 16.42  ?  143 GLY A C   1 
ATOM   1041 O  O   . GLY A 1 143 ? 23.412  30.618  4.435   1.00 17.47  ?  143 GLY A O   1 
ATOM   1042 N  N   . ALA A 1 144 ? 21.288  30.656  3.645   1.00 15.49  ?  144 ALA A N   1 
ATOM   1043 C  CA  . ALA A 1 144 ? 21.542  29.833  2.462   1.00 15.24  ?  144 ALA A CA  1 
ATOM   1044 C  C   . ALA A 1 144 ? 22.412  30.546  1.418   1.00 16.46  ?  144 ALA A C   1 
ATOM   1045 O  O   . ALA A 1 144 ? 22.262  31.751  1.180   1.00 16.14  ?  144 ALA A O   1 
ATOM   1046 C  CB  . ALA A 1 144 ? 20.221  29.441  1.879   1.00 15.96  ?  144 ALA A CB  1 
ATOM   1047 N  N   . THR A 1 145 ? 23.345  29.777  0.849   1.00 14.38  ?  145 THR A N   1 
ATOM   1048 C  CA  . THR A 1 145 ? 24.206  30.186  -0.240  1.00 15.84  ?  145 THR A CA  1 
ATOM   1049 C  C   . THR A 1 145 ? 24.227  29.097  -1.327  1.00 17.08  ?  145 THR A C   1 
ATOM   1050 O  O   . THR A 1 145 ? 24.047  27.913  -1.051  1.00 14.62  ?  145 THR A O   1 
ATOM   1051 C  CB  . THR A 1 145 ? 25.613  30.447  0.307   1.00 18.27  ?  145 THR A CB  1 
ATOM   1052 O  OG1 . THR A 1 145 ? 26.035  29.288  1.027   1.00 19.97  ?  145 THR A OG1 1 
ATOM   1053 C  CG2 . THR A 1 145 ? 25.645  31.632  1.267   1.00 20.23  ?  145 THR A CG2 1 
ATOM   1054 N  N   . VAL A 1 146 ? 24.549  29.526  -2.554  1.00 16.55  ?  146 VAL A N   1 
ATOM   1055 C  CA  . VAL A 1 146 ? 24.634  28.673  -3.735  1.00 15.85  ?  146 VAL A CA  1 
ATOM   1056 C  C   . VAL A 1 146 ? 25.983  28.838  -4.423  1.00 16.32  ?  146 VAL A C   1 
ATOM   1057 O  O   . VAL A 1 146 ? 26.360  29.962  -4.760  1.00 17.93  ?  146 VAL A O   1 
ATOM   1058 C  CB  . VAL A 1 146 ? 23.483  29.126  -4.645  1.00 17.58  ?  146 VAL A CB  1 
ATOM   1059 C  CG1 . VAL A 1 146 ? 23.535  28.464  -5.998  1.00 18.12  ?  146 VAL A CG1 1 
ATOM   1060 C  CG2 . VAL A 1 146 ? 22.126  28.848  -3.992  1.00 19.40  ?  146 VAL A CG2 1 
ATOM   1061 N  N   . GLY A 1 147 ? 26.644  27.718  -4.689  1.00 15.10  ?  147 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 147 ? 27.822  27.682  -5.524  1.00 15.93  ?  147 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 147 ? 29.095  27.844  -4.699  1.00 17.28  ?  147 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 147 ? 29.709  28.921  -4.697  1.00 18.89  ?  147 GLY A O   1 
ATOM   1065 N  N   . LYS A 1 148 ? 29.543  26.752  -4.073  1.00 17.09  ?  148 LYS A N   1 
ATOM   1066 C  CA  . LYS A 1 148 ? 30.596  26.813  -3.068  1.00 16.15  ?  148 LYS A CA  1 
ATOM   1067 C  C   . LYS A 1 148 ? 31.910  26.174  -3.517  1.00 17.85  ?  148 LYS A C   1 
ATOM   1068 O  O   . LYS A 1 148 ? 32.752  25.875  -2.680  1.00 17.06  ?  148 LYS A O   1 
ATOM   1069 C  CB  . LYS A 1 148 ? 30.052  26.169  -1.785  1.00 18.66  ?  148 LYS A CB  1 
ATOM   1070 C  CG  . LYS A 1 148 ? 29.253  27.249  -1.095  1.00 22.01  ?  148 LYS A CG  1 
ATOM   1071 C  CD  . LYS A 1 148 ? 28.239  26.838  -0.070  1.00 25.70  ?  148 LYS A CD  1 
ATOM   1072 C  CE  . LYS A 1 148 ? 26.996  26.432  -0.795  1.00 23.53  ?  148 LYS A CE  1 
ATOM   1073 N  NZ  . LYS A 1 148 ? 26.027  26.274  0.269   1.00 20.17  1  148 LYS A NZ  1 
ATOM   1074 N  N   . LEU A 1 149 ? 32.099  25.949  -4.816  1.00 16.92  ?  149 LEU A N   1 
ATOM   1075 C  CA  . LEU A 1 149 ? 33.358  25.398  -5.310  1.00 18.01  ?  149 LEU A CA  1 
ATOM   1076 C  C   . LEU A 1 149 ? 34.575  26.106  -4.695  1.00 17.13  ?  149 LEU A C   1 
ATOM   1077 O  O   . LEU A 1 149 ? 35.569  25.462  -4.355  1.00 16.62  ?  149 LEU A O   1 
ATOM   1078 C  CB  . LEU A 1 149 ? 33.405  25.496  -6.840  1.00 20.57  ?  149 LEU A CB  1 
ATOM   1079 C  CG  . LEU A 1 149 ? 34.692  24.974  -7.501  1.00 21.55  ?  149 LEU A CG  1 
ATOM   1080 C  CD1 . LEU A 1 149 ? 34.875  23.496  -7.266  1.00 21.65  ?  149 LEU A CD1 1 
ATOM   1081 C  CD2 . LEU A 1 149 ? 34.704  25.264  -9.002  1.00 24.40  ?  149 LEU A CD2 1 
ATOM   1082 N  N   . TYR A 1 150 ? 34.533  27.436  -4.642  1.00 19.65  ?  150 TYR A N   1 
ATOM   1083 C  CA  . TYR A 1 150 ? 35.666  28.231  -4.153  1.00 22.40  ?  150 TYR A CA  1 
ATOM   1084 C  C   . TYR A 1 150 ? 35.423  28.726  -2.731  1.00 27.06  ?  150 TYR A C   1 
ATOM   1085 O  O   . TYR A 1 150 ? 36.049  29.674  -2.311  1.00 26.55  ?  150 TYR A O   1 
ATOM   1086 C  CB  . TYR A 1 150 ? 35.817  29.432  -5.085  1.00 22.42  ?  150 TYR A CB  1 
ATOM   1087 C  CG  . TYR A 1 150 ? 36.151  29.064  -6.521  1.00 20.67  ?  150 TYR A CG  1 
ATOM   1088 C  CD1 . TYR A 1 150 ? 37.137  28.140  -6.812  1.00 18.68  ?  150 TYR A CD1 1 
ATOM   1089 C  CD2 . TYR A 1 150 ? 35.412  29.581  -7.576  1.00 21.44  ?  150 TYR A CD2 1 
ATOM   1090 C  CE1 . TYR A 1 150 ? 37.421  27.787  -8.121  1.00 22.17  ?  150 TYR A CE1 1 
ATOM   1091 C  CE2 . TYR A 1 150 ? 35.683  29.237  -8.895  1.00 21.69  ?  150 TYR A CE2 1 
ATOM   1092 C  CZ  . TYR A 1 150 ? 36.684  28.330  -9.167  1.00 22.15  ?  150 TYR A CZ  1 
ATOM   1093 O  OH  . TYR A 1 150 ? 36.961  27.965  -10.452 1.00 23.59  ?  150 TYR A OH  1 
ATOM   1094 N  N   . GLY A 1 151 ? 34.481  28.112  -2.003  1.00 21.88  ?  151 GLY A N   1 
ATOM   1095 C  CA  . GLY A 1 151 ? 34.135  28.595  -0.690  1.00 24.18  ?  151 GLY A CA  1 
ATOM   1096 C  C   . GLY A 1 151 ? 33.020  29.625  -0.746  1.00 21.75  ?  151 GLY A C   1 
ATOM   1097 O  O   . GLY A 1 151 ? 32.619  30.118  -1.799  1.00 23.53  ?  151 GLY A O   1 
ATOM   1098 N  N   . VAL A 1 152 ? 32.542  29.954  0.455   1.00 23.08  ?  152 VAL A N   1 
ATOM   1099 C  CA  . VAL A 1 152 ? 31.366  30.772  0.629   1.00 21.17  ?  152 VAL A CA  1 
ATOM   1100 C  C   . VAL A 1 152 ? 31.620  32.206  0.183   1.00 20.84  ?  152 VAL A C   1 
ATOM   1101 O  O   . VAL A 1 152 ? 30.692  32.893  -0.206  1.00 21.62  ?  152 VAL A O   1 
ATOM   1102 C  CB  . VAL A 1 152 ? 30.907  30.662  2.098   1.00 25.30  ?  152 VAL A CB  1 
ATOM   1103 C  CG1 . VAL A 1 152 ? 31.793  31.446  3.051   1.00 26.05  ?  152 VAL A CG1 1 
ATOM   1104 C  CG2 . VAL A 1 152 ? 29.462  31.070  2.221   1.00 27.67  ?  152 VAL A CG2 1 
ATOM   1105 N  N   . ARG A 1 153 ? 32.883  32.636  0.170   1.00 23.90  ?  153 ARG A N   1 
ATOM   1106 C  CA  . ARG A 1 153 ? 33.174  34.018  -0.193  1.00 30.77  ?  153 ARG A CA  1 
ATOM   1107 C  C   . ARG A 1 153 ? 32.872  34.291  -1.670  1.00 28.13  ?  153 ARG A C   1 
ATOM   1108 O  O   . ARG A 1 153 ? 32.527  35.421  -2.039  1.00 26.39  ?  153 ARG A O   1 
ATOM   1109 C  CB  . ARG A 1 153 ? 34.624  34.341  0.195   1.00 42.37  ?  153 ARG A CB  1 
ATOM   1110 C  CG  . ARG A 1 153 ? 34.982  35.823  0.259   1.00 62.74  ?  153 ARG A CG  1 
ATOM   1111 C  CD  . ARG A 1 153 ? 33.860  36.880  0.537   1.00 84.42  ?  153 ARG A CD  1 
ATOM   1112 N  NE  . ARG A 1 153 ? 32.751  36.508  1.436   1.00 106.04 ?  153 ARG A NE  1 
ATOM   1113 C  CZ  . ARG A 1 153 ? 31.436  36.709  1.206   1.00 100.42 ?  153 ARG A CZ  1 
ATOM   1114 N  NH1 . ARG A 1 153 ? 31.035  37.488  0.209   1.00 96.40  1  153 ARG A NH1 1 
ATOM   1115 N  NH2 . ARG A 1 153 ? 30.529  36.145  1.995   1.00 85.84  ?  153 ARG A NH2 1 
ATOM   1116 N  N   . GLN A 1 154 ? 32.925  33.248  -2.517  1.00 23.00  ?  154 GLN A N   1 
ATOM   1117 C  CA  . GLN A 1 154 ? 32.629  33.408  -3.936  1.00 21.37  ?  154 GLN A CA  1 
ATOM   1118 C  C   . GLN A 1 154 ? 31.275  32.822  -4.331  1.00 19.85  ?  154 GLN A C   1 
ATOM   1119 O  O   . GLN A 1 154 ? 30.996  32.636  -5.527  1.00 19.27  ?  154 GLN A O   1 
ATOM   1120 C  CB  . GLN A 1 154 ? 33.835  32.898  -4.719  1.00 23.59  ?  154 GLN A CB  1 
ATOM   1121 C  CG  . GLN A 1 154 ? 35.040  33.831  -4.575  1.00 26.62  ?  154 GLN A CG  1 
ATOM   1122 C  CD  . GLN A 1 154 ? 36.326  33.239  -5.079  1.00 34.93  ?  154 GLN A CD  1 
ATOM   1123 O  OE1 . GLN A 1 154 ? 37.350  33.210  -4.378  1.00 40.70  ?  154 GLN A OE1 1 
ATOM   1124 N  NE2 . GLN A 1 154 ? 36.301  32.799  -6.329  1.00 42.79  ?  154 GLN A NE2 1 
ATOM   1125 N  N   . SER A 1 155 ? 30.389  32.648  -3.349  1.00 19.64  ?  155 SER A N   1 
ATOM   1126 C  CA  . SER A 1 155 ? 29.069  32.091  -3.601  1.00 19.51  ?  155 SER A CA  1 
ATOM   1127 C  C   . SER A 1 155 ? 28.052  33.173  -3.916  1.00 20.06  ?  155 SER A C   1 
ATOM   1128 O  O   . SER A 1 155 ? 28.302  34.364  -3.751  1.00 19.76  ?  155 SER A O   1 
ATOM   1129 C  CB  . SER A 1 155 ? 28.599  31.247  -2.412  1.00 21.41  ?  155 SER A CB  1 
ATOM   1130 O  OG  . SER A 1 155 ? 28.369  32.046  -1.264  1.00 21.24  ?  155 SER A OG  1 
ATOM   1131 N  N   . SER A 1 156 ? 26.868  32.737  -4.345  1.00 16.72  ?  156 SER A N   1 
ATOM   1132 C  CA  . SER A 1 156 ? 25.724  33.606  -4.520  1.00 17.95  ?  156 SER A CA  1 
ATOM   1133 C  C   . SER A 1 156 ? 24.765  33.388  -3.360  1.00 19.78  ?  156 SER A C   1 
ATOM   1134 O  O   . SER A 1 156 ? 24.801  32.324  -2.747  1.00 18.00  ?  156 SER A O   1 
ATOM   1135 C  CB  . SER A 1 156 ? 25.021  33.377  -5.856  1.00 18.10  ?  156 SER A CB  1 
ATOM   1136 O  OG  . SER A 1 156 ? 25.907  33.584  -6.963  1.00 18.19  ?  156 SER A OG  1 
ATOM   1137 N  N   . PRO A 1 157 ? 23.872  34.357  -3.045  1.00 20.86  ?  157 PRO A N   1 
ATOM   1138 C  CA  . PRO A 1 157 ? 22.790  34.119  -2.106  1.00 22.34  ?  157 PRO A CA  1 
ATOM   1139 C  C   . PRO A 1 157 ? 21.839  33.012  -2.551  1.00 21.74  ?  157 PRO A C   1 
ATOM   1140 O  O   . PRO A 1 157 ? 21.508  32.917  -3.726  1.00 22.61  ?  157 PRO A O   1 
ATOM   1141 C  CB  . PRO A 1 157 ? 22.044  35.455  -2.008  1.00 24.97  ?  157 PRO A CB  1 
ATOM   1142 C  CG  . PRO A 1 157 ? 22.941  36.470  -2.681  1.00 24.61  ?  157 PRO A CG  1 
ATOM   1143 C  CD  . PRO A 1 157 ? 23.867  35.731  -3.582  1.00 23.37  ?  157 PRO A CD  1 
ATOM   1144 N  N   . GLY A 1 158 ? 21.418  32.181  -1.587  1.00 19.63  ?  158 GLY A N   1 
ATOM   1145 C  CA  . GLY A 1 158 ? 20.357  31.221  -1.819  1.00 17.52  ?  158 GLY A CA  1 
ATOM   1146 C  C   . GLY A 1 158 ? 19.077  31.714  -1.153  1.00 17.67  ?  158 GLY A C   1 
ATOM   1147 O  O   . GLY A 1 158 ? 18.891  32.914  -0.974  1.00 18.54  ?  158 GLY A O   1 
ATOM   1148 N  N   . GLY A 1 159 ? 18.212  30.787  -0.743  1.00 14.81  ?  159 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 159 ? 16.994  31.175  -0.043  1.00 15.44  ?  159 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 159 ? 15.982  30.059  0.009   1.00 15.30  ?  159 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 159 ? 16.294  28.933  -0.351  1.00 16.40  ?  159 GLY A O   1 
ATOM   1152 N  N   . LEU A 1 160 ? 14.772  30.445  0.411   1.00 14.98  ?  160 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 160 ? 13.604  29.598  0.488   1.00 15.53  ?  160 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 160 ? 12.617  30.067  -0.580  1.00 16.12  ?  160 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 160 ? 12.369  31.276  -0.720  1.00 16.49  ?  160 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 160 ? 13.034  29.694  1.907   1.00 16.19  ?  160 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 160 ? 11.739  28.904  2.173   1.00 17.41  ?  160 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 160 ? 11.687  28.438  3.624   1.00 18.33  ?  160 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 160 ? 10.482  29.614  1.835   1.00 17.86  ?  160 LEU A CD2 1 
ATOM   1160 N  N   . GLY A 1 161 ? 12.120  29.107  -1.369  1.00 14.16  ?  161 GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 161 ? 11.175  29.373  -2.438  1.00 14.81  ?  161 GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 161 ? 9.992   28.430  -2.417  1.00 14.87  ?  161 GLY A C   1 
ATOM   1163 O  O   . GLY A 1 161 ? 9.996   27.399  -1.757  1.00 14.57  ?  161 GLY A O   1 
ATOM   1164 N  N   . THR A 1 162 ? 8.962   28.764  -3.183  1.00 13.64  ?  162 THR A N   1 
ATOM   1165 C  CA  . THR A 1 162 ? 7.767   27.938  -3.208  1.00 15.12  ?  162 THR A CA  1 
ATOM   1166 C  C   . THR A 1 162 ? 7.121   28.070  -4.583  1.00 15.93  ?  162 THR A C   1 
ATOM   1167 O  O   . THR A 1 162 ? 7.327   29.067  -5.278  1.00 16.39  ?  162 THR A O   1 
ATOM   1168 C  CB  . THR A 1 162 ? 6.844   28.354  -2.052  1.00 15.37  ?  162 THR A CB  1 
ATOM   1169 O  OG1 . THR A 1 162 ? 5.784   27.401  -1.910  1.00 14.71  ?  162 THR A OG1 1 
ATOM   1170 C  CG2 . THR A 1 162 ? 6.242   29.731  -2.284  1.00 17.79  ?  162 THR A CG2 1 
ATOM   1171 N  N   . ALA A 1 163 ? 6.334   27.059  -4.981  1.00 15.55  ?  163 ALA A N   1 
ATOM   1172 C  CA  . ALA A 1 163 ? 5.572   27.087  -6.224  1.00 15.23  ?  163 ALA A CA  1 
ATOM   1173 C  C   . ALA A 1 163 ? 4.421   26.100  -6.120  1.00 15.88  ?  163 ALA A C   1 
ATOM   1174 O  O   . ALA A 1 163 ? 4.501   25.146  -5.343  1.00 15.79  ?  163 ALA A O   1 
ATOM   1175 C  CB  . ALA A 1 163 ? 6.452   26.755  -7.416  1.00 15.80  ?  163 ALA A CB  1 
ATOM   1176 N  N   . THR A 1 164 ? 3.350   26.351  -6.881  1.00 15.37  ?  164 THR A N   1 
ATOM   1177 C  CA  . THR A 1 164 ? 2.214   25.458  -6.991  1.00 15.97  ?  164 THR A CA  1 
ATOM   1178 C  C   . THR A 1 164 ? 1.987   25.158  -8.472  1.00 17.26  ?  164 THR A C   1 
ATOM   1179 O  O   . THR A 1 164 ? 2.020   26.070  -9.293  1.00 17.11  ?  164 THR A O   1 
ATOM   1180 C  CB  . THR A 1 164 ? 0.959   26.097  -6.392  1.00 18.62  ?  164 THR A CB  1 
ATOM   1181 O  OG1 . THR A 1 164 ? 1.172   26.230  -4.992  1.00 18.52  ?  164 THR A OG1 1 
ATOM   1182 C  CG2 . THR A 1 164 ? -0.278  25.246  -6.611  1.00 20.95  ?  164 THR A CG2 1 
ATOM   1183 N  N   . VAL A 1 165 ? 1.810   23.871  -8.794  1.00 16.82  ?  165 VAL A N   1 
ATOM   1184 C  CA  . VAL A 1 165 ? 1.416   23.403  -10.097 1.00 18.64  ?  165 VAL A CA  1 
ATOM   1185 C  C   . VAL A 1 165 ? -0.031  22.902  -9.992  1.00 18.61  ?  165 VAL A C   1 
ATOM   1186 O  O   . VAL A 1 165 ? -0.363  22.070  -9.151  1.00 18.00  ?  165 VAL A O   1 
ATOM   1187 C  CB  . VAL A 1 165 ? 2.391   22.303  -10.579 1.00 18.31  ?  165 VAL A CB  1 
ATOM   1188 C  CG1 . VAL A 1 165 ? 1.926   21.614  -11.841 1.00 19.13  ?  165 VAL A CG1 1 
ATOM   1189 C  CG2 . VAL A 1 165 ? 3.803   22.840  -10.757 1.00 20.61  ?  165 VAL A CG2 1 
ATOM   1190 N  N   A SER A 1 166 ? -0.870  23.368  -10.915 0.99 19.43  ?  166 SER A N   1 
ATOM   1191 C  CA  A SER A 1 166 ? -2.274  22.974  -11.017 0.99 22.29  ?  166 SER A CA  1 
ATOM   1192 C  C   A SER A 1 166 ? -2.446  21.944  -12.126 0.99 20.50  ?  166 SER A C   1 
ATOM   1193 O  O   A SER A 1 166 ? -1.930  22.141  -13.207 0.99 24.35  ?  166 SER A O   1 
ATOM   1194 C  CB  A SER A 1 166 ? -3.128  24.169  -11.366 0.99 24.18  ?  166 SER A CB  1 
ATOM   1195 O  OG  A SER A 1 166 ? -3.201  24.993  -10.223 0.99 33.08  ?  166 SER A OG  1 
ATOM   1196 N  N   . LEU A 1 167 ? -3.142  20.864  -11.825 1.00 19.52  ?  167 LEU A N   1 
ATOM   1197 C  CA  . LEU A 1 167 ? -3.500  19.851  -12.793 1.00 22.83  ?  167 LEU A CA  1 
ATOM   1198 C  C   . LEU A 1 167 ? -5.019  19.922  -12.993 1.00 22.89  ?  167 LEU A C   1 
ATOM   1199 O  O   . LEU A 1 167 ? -5.666  20.779  -12.423 1.00 25.58  ?  167 LEU A O   1 
ATOM   1200 C  CB  . LEU A 1 167 ? -3.091  18.463  -12.297 1.00 23.20  ?  167 LEU A CB  1 
ATOM   1201 C  CG  . LEU A 1 167 ? -1.618  18.268  -11.902 1.00 30.90  ?  167 LEU A CG  1 
ATOM   1202 C  CD1 . LEU A 1 167 ? -1.365  16.774  -11.722 1.00 34.83  ?  167 LEU A CD1 1 
ATOM   1203 C  CD2 . LEU A 1 167 ? -0.787  18.835  -12.992 1.00 33.40  ?  167 LEU A CD2 1 
ATOM   1204 N  N   . TYR A 1 168 ? -5.583  18.973  -13.731 1.00 24.71  ?  168 TYR A N   1 
ATOM   1205 C  CA  . TYR A 1 168 ? -7.026  18.876  -13.933 1.00 24.58  ?  168 TYR A CA  1 
ATOM   1206 C  C   . TYR A 1 168 ? -7.754  18.545  -12.633 1.00 26.22  ?  168 TYR A C   1 
ATOM   1207 O  O   . TYR A 1 168 ? -7.205  17.952  -11.701 1.00 24.86  ?  168 TYR A O   1 
ATOM   1208 C  CB  . TYR A 1 168 ? -7.284  17.807  -15.010 1.00 23.82  ?  168 TYR A CB  1 
ATOM   1209 C  CG  . TYR A 1 168 ? -6.928  16.381  -14.606 1.00 23.13  ?  168 TYR A CG  1 
ATOM   1210 C  CD1 . TYR A 1 168 ? -7.792  15.583  -13.862 1.00 23.32  ?  168 TYR A CD1 1 
ATOM   1211 C  CD2 . TYR A 1 168 ? -5.669  15.874  -14.879 1.00 25.16  ?  168 TYR A CD2 1 
ATOM   1212 C  CE1 . TYR A 1 168 ? -7.442  14.295  -13.477 1.00 22.02  ?  168 TYR A CE1 1 
ATOM   1213 C  CE2 . TYR A 1 168 ? -5.299  14.597  -14.488 1.00 24.95  ?  168 TYR A CE2 1 
ATOM   1214 C  CZ  . TYR A 1 168 ? -6.182  13.808  -13.791 1.00 24.95  ?  168 TYR A CZ  1 
ATOM   1215 O  OH  . TYR A 1 168 ? -5.732  12.573  -13.432 1.00 23.24  ?  168 TYR A OH  1 
ATOM   1216 N  N   . GLY A 1 169 ? -9.047  18.901  -12.582 1.00 24.81  ?  169 GLY A N   1 
ATOM   1217 C  CA  . GLY A 1 169 ? -9.954  18.391  -11.575 1.00 25.04  ?  169 GLY A CA  1 
ATOM   1218 C  C   . GLY A 1 169 ? -9.692  18.873  -10.153 1.00 23.62  ?  169 GLY A C   1 
ATOM   1219 O  O   . GLY A 1 169 ? -10.046 18.182  -9.195  1.00 27.99  ?  169 GLY A O   1 
ATOM   1220 N  N   . GLY A 1 170 ? -9.100  20.049  -10.016 1.00 22.13  ?  170 GLY A N   1 
ATOM   1221 C  CA  . GLY A 1 170 ? -8.826  20.635  -8.713  1.00 21.92  ?  170 GLY A CA  1 
ATOM   1222 C  C   . GLY A 1 170 ? -7.557  20.079  -8.060  1.00 21.73  ?  170 GLY A C   1 
ATOM   1223 O  O   . GLY A 1 170 ? -7.293  20.384  -6.909  1.00 21.68  ?  170 GLY A O   1 
ATOM   1224 N  N   . ILE A 1 171 ? -6.802  19.239  -8.779  1.00 20.51  ?  171 ILE A N   1 
ATOM   1225 C  CA  . ILE A 1 171 ? -5.593  18.642  -8.211  1.00 20.69  ?  171 ILE A CA  1 
ATOM   1226 C  C   . ILE A 1 171 ? -4.506  19.715  -8.157  1.00 18.22  ?  171 ILE A C   1 
ATOM   1227 O  O   . ILE A 1 171 ? -4.324  20.485  -9.106  1.00 17.07  ?  171 ILE A O   1 
ATOM   1228 C  CB  . ILE A 1 171 ? -5.167  17.398  -9.009  1.00 21.84  ?  171 ILE A CB  1 
ATOM   1229 C  CG1 . ILE A 1 171 ? -6.163  16.265  -8.833  1.00 24.41  ?  171 ILE A CG1 1 
ATOM   1230 C  CG2 . ILE A 1 171 ? -3.776  16.931  -8.584  1.00 21.75  ?  171 ILE A CG2 1 
ATOM   1231 C  CD1 . ILE A 1 171 ? -6.051  15.207  -9.913  1.00 24.93  ?  171 ILE A CD1 1 
ATOM   1232 N  N   . LYS A 1 172 ? -3.741  19.733  -7.057  1.00 21.55  ?  172 LYS A N   1 
ATOM   1233 C  CA  . LYS A 1 172 ? -2.595  20.628  -6.919  1.00 20.20  ?  172 LYS A CA  1 
ATOM   1234 C  C   . LYS A 1 172 ? -1.396  19.888  -6.334  1.00 16.06  ?  172 LYS A C   1 
ATOM   1235 O  O   . LYS A 1 172 ? -1.539  18.998  -5.521  1.00 14.46  ?  172 LYS A O   1 
ATOM   1236 C  CB  . LYS A 1 172 ? -2.888  21.789  -5.953  1.00 23.94  ?  172 LYS A CB  1 
ATOM   1237 C  CG  . LYS A 1 172 ? -3.812  22.848  -6.478  1.00 30.74  ?  172 LYS A CG  1 
ATOM   1238 C  CD  . LYS A 1 172 ? -4.516  23.601  -5.354  1.00 38.83  ?  172 LYS A CD  1 
ATOM   1239 C  CE  . LYS A 1 172 ? -5.030  24.950  -5.781  1.00 44.69  ?  172 LYS A CE  1 
ATOM   1240 N  NZ  . LYS A 1 172 ? -5.423  24.963  -7.193  1.00 47.90  1  172 LYS A NZ  1 
ATOM   1241 N  N   . VAL A 1 173 ? -0.205  20.324  -6.739  1.00 16.34  ?  173 VAL A N   1 
ATOM   1242 C  CA  . VAL A 1 173 ? 1.034   19.862  -6.140  1.00 16.51  ?  173 VAL A CA  1 
ATOM   1243 C  C   . VAL A 1 173 ? 1.883   21.102  -5.891  1.00 14.86  ?  173 VAL A C   1 
ATOM   1244 O  O   . VAL A 1 173 ? 2.094   21.888  -6.829  1.00 16.19  ?  173 VAL A O   1 
ATOM   1245 C  CB  . VAL A 1 173 ? 1.734   18.906  -7.116  1.00 18.86  ?  173 VAL A CB  1 
ATOM   1246 C  CG1 . VAL A 1 173 ? 3.067   18.457  -6.537  1.00 19.99  ?  173 VAL A CG1 1 
ATOM   1247 C  CG2 . VAL A 1 173 ? 0.856   17.708  -7.480  1.00 19.39  ?  173 VAL A CG2 1 
ATOM   1248 N  N   . SER A 1 174 ? 2.330   21.306  -4.642  1.00 14.39  ?  174 SER A N   1 
ATOM   1249 C  CA  . SER A 1 174 ? 3.092   22.479  -4.279  1.00 14.31  ?  174 SER A CA  1 
ATOM   1250 C  C   . SER A 1 174 ? 4.412   22.059  -3.660  1.00 13.64  ?  174 SER A C   1 
ATOM   1251 O  O   . SER A 1 174 ? 4.514   20.982  -3.109  1.00 15.09  ?  174 SER A O   1 
ATOM   1252 C  CB  . SER A 1 174 ? 2.355   23.392  -3.287  1.00 17.71  ?  174 SER A CB  1 
ATOM   1253 O  OG  . SER A 1 174 ? 1.068   23.722  -3.767  1.00 24.27  ?  174 SER A OG  1 
ATOM   1254 N  N   . ALA A 1 175 ? 5.374   22.952  -3.691  1.00 12.75  ?  175 ALA A N   1 
ATOM   1255 C  CA  . ALA A 1 175 ? 6.683   22.675  -3.133  1.00 13.32  ?  175 ALA A CA  1 
ATOM   1256 C  C   . ALA A 1 175 ? 7.145   23.874  -2.328  1.00 14.14  ?  175 ALA A C   1 
ATOM   1257 O  O   . ALA A 1 175 ? 6.827   25.008  -2.678  1.00 14.12  ?  175 ALA A O   1 
ATOM   1258 C  CB  . ALA A 1 175 ? 7.676   22.364  -4.253  1.00 14.12  ?  175 ALA A CB  1 
ATOM   1259 N  N   . MET A 1 176 ? 8.016   23.591  -1.342  1.00 13.55  ?  176 MET A N   1 
ATOM   1260 C  CA  . MET A 1 176 ? 8.724   24.603  -0.575  1.00 13.68  ?  176 MET A CA  1 
ATOM   1261 C  C   . MET A 1 176 ? 10.133  24.070  -0.389  1.00 13.00  ?  176 MET A C   1 
ATOM   1262 O  O   . MET A 1 176 ? 10.304  22.967  0.145   1.00 13.85  ?  176 MET A O   1 
ATOM   1263 C  CB  . MET A 1 176 ? 8.059   24.858  0.795   1.00 14.65  ?  176 MET A CB  1 
ATOM   1264 C  CG  . MET A 1 176 ? 8.773   25.905  1.646   1.00 16.75  ?  176 MET A CG  1 
ATOM   1265 S  SD  . MET A 1 176 ? 7.882   26.384  3.158   1.00 18.15  ?  176 MET A SD  1 
ATOM   1266 C  CE  . MET A 1 176 ? 8.142   24.898  4.146   1.00 19.39  ?  176 MET A CE  1 
ATOM   1267 N  N   . ILE A 1 177 ? 11.107  24.814  -0.892  1.00 12.79  ?  177 ILE A N   1 
ATOM   1268 C  CA  . ILE A 1 177 ? 12.488  24.348  -1.031  1.00 14.12  ?  177 ILE A CA  1 
ATOM   1269 C  C   . ILE A 1 177 ? 13.428  25.367  -0.387  1.00 13.64  ?  177 ILE A C   1 
ATOM   1270 O  O   . ILE A 1 177 ? 13.285  26.560  -0.613  1.00 15.18  ?  177 ILE A O   1 
ATOM   1271 C  CB  . ILE A 1 177 ? 12.835  24.144  -2.527  1.00 15.79  ?  177 ILE A CB  1 
ATOM   1272 C  CG1 . ILE A 1 177 ? 11.887  23.208  -3.272  1.00 16.94  ?  177 ILE A CG1 1 
ATOM   1273 C  CG2 . ILE A 1 177 ? 14.308  23.729  -2.726  1.00 17.03  ?  177 ILE A CG2 1 
ATOM   1274 C  CD1 . ILE A 1 177 ? 11.937  21.745  -2.875  1.00 21.00  ?  177 ILE A CD1 1 
ATOM   1275 N  N   . VAL A 1 178 ? 14.443  24.888  0.341   1.00 13.13  ?  178 VAL A N   1 
ATOM   1276 C  CA  . VAL A 1 178 ? 15.553  25.712  0.765   1.00 13.60  ?  178 VAL A CA  1 
ATOM   1277 C  C   . VAL A 1 178 ? 16.742  25.345  -0.119  1.00 14.00  ?  178 VAL A C   1 
ATOM   1278 O  O   . VAL A 1 178 ? 17.168  24.183  -0.128  1.00 12.85  ?  178 VAL A O   1 
ATOM   1279 C  CB  . VAL A 1 178 ? 15.886  25.520  2.261   1.00 14.49  ?  178 VAL A CB  1 
ATOM   1280 C  CG1 . VAL A 1 178 ? 17.160  26.254  2.641   1.00 16.44  ?  178 VAL A CG1 1 
ATOM   1281 C  CG2 . VAL A 1 178 ? 14.748  25.979  3.153   1.00 16.11  ?  178 VAL A CG2 1 
ATOM   1282 N  N   . VAL A 1 179 ? 17.238  26.310  -0.902  1.00 13.38  ?  179 VAL A N   1 
ATOM   1283 C  CA  . VAL A 1 179 ? 18.360  26.089  -1.806  1.00 13.96  ?  179 VAL A CA  1 
ATOM   1284 C  C   . VAL A 1 179 ? 19.649  26.585  -1.157  1.00 14.57  ?  179 VAL A C   1 
ATOM   1285 O  O   . VAL A 1 179 ? 19.814  27.792  -0.995  1.00 15.35  ?  179 VAL A O   1 
ATOM   1286 C  CB  . VAL A 1 179 ? 18.140  26.794  -3.150  1.00 18.00  ?  179 VAL A CB  1 
ATOM   1287 C  CG1 . VAL A 1 179 ? 19.280  26.459  -4.108  1.00 19.77  ?  179 VAL A CG1 1 
ATOM   1288 C  CG2 . VAL A 1 179 ? 16.781  26.436  -3.732  1.00 20.91  ?  179 VAL A CG2 1 
ATOM   1289 N  N   . ASN A 1 180 ? 20.532  25.647  -0.795  1.00 13.09  ?  180 ASN A N   1 
ATOM   1290 C  CA  . ASN A 1 180 ? 21.850  25.905  -0.226  1.00 12.57  ?  180 ASN A CA  1 
ATOM   1291 C  C   . ASN A 1 180 ? 22.874  25.073  -0.997  1.00 11.60  ?  180 ASN A C   1 
ATOM   1292 O  O   . ASN A 1 180 ? 23.799  24.512  -0.440  1.00 12.86  ?  180 ASN A O   1 
ATOM   1293 C  CB  . ASN A 1 180 ? 21.859  25.604  1.264   1.00 13.13  ?  180 ASN A CB  1 
ATOM   1294 C  CG  . ASN A 1 180 ? 23.107  26.039  1.999   1.00 15.96  ?  180 ASN A CG  1 
ATOM   1295 O  OD1 . ASN A 1 180 ? 23.440  27.221  2.070   1.00 15.74  ?  180 ASN A OD1 1 
ATOM   1296 N  ND2 . ASN A 1 180 ? 23.798  25.113  2.639   1.00 17.34  ?  180 ASN A ND2 1 
ATOM   1297 N  N   . SER A 1 181 ? 22.663  24.948  -2.302  1.00 12.73  ?  181 SER A N   1 
ATOM   1298 C  CA  . SER A 1 181 ? 23.304  23.913  -3.103  1.00 13.33  ?  181 SER A CA  1 
ATOM   1299 C  C   . SER A 1 181 ? 24.797  24.184  -3.260  1.00 13.68  ?  181 SER A C   1 
ATOM   1300 O  O   . SER A 1 181 ? 25.229  25.323  -3.399  1.00 14.04  ?  181 SER A O   1 
ATOM   1301 C  CB  . SER A 1 181 ? 22.637  23.821  -4.425  1.00 15.15  ?  181 SER A CB  1 
ATOM   1302 O  OG  . SER A 1 181 ? 22.679  25.075  -5.091  1.00 18.74  ?  181 SER A OG  1 
ATOM   1303 N  N   . PHE A 1 182 ? 25.574  23.111  -3.271  1.00 14.17  ?  182 PHE A N   1 
ATOM   1304 C  CA  . PHE A 1 182 ? 26.963  23.182  -3.679  1.00 13.87  ?  182 PHE A CA  1 
ATOM   1305 C  C   . PHE A 1 182 ? 27.072  23.679  -5.121  1.00 15.16  ?  182 PHE A C   1 
ATOM   1306 O  O   . PHE A 1 182 ? 27.924  24.515  -5.424  1.00 15.14  ?  182 PHE A O   1 
ATOM   1307 C  CB  . PHE A 1 182 ? 27.633  21.813  -3.551  1.00 15.15  ?  182 PHE A CB  1 
ATOM   1308 C  CG  . PHE A 1 182 ? 29.028  21.840  -4.166  1.00 14.82  ?  182 PHE A CG  1 
ATOM   1309 C  CD1 . PHE A 1 182 ? 30.084  22.432  -3.501  1.00 17.85  ?  182 PHE A CD1 1 
ATOM   1310 C  CD2 . PHE A 1 182 ? 29.240  21.325  -5.432  1.00 16.89  ?  182 PHE A CD2 1 
ATOM   1311 C  CE1 . PHE A 1 182 ? 31.352  22.478  -4.080  1.00 19.57  ?  182 PHE A CE1 1 
ATOM   1312 C  CE2 . PHE A 1 182 ? 30.497  21.367  -6.009  1.00 19.94  ?  182 PHE A CE2 1 
ATOM   1313 C  CZ  . PHE A 1 182 ? 31.558  21.911  -5.322  1.00 19.81  ?  182 PHE A CZ  1 
ATOM   1314 N  N   . GLY A 1 183 ? 26.186  23.178  -5.999  1.00 14.78  ?  183 GLY A N   1 
ATOM   1315 C  CA  . GLY A 1 183 ? 26.228  23.463  -7.418  1.00 15.09  ?  183 GLY A CA  1 
ATOM   1316 C  C   . GLY A 1 183 ? 25.530  24.784  -7.773  1.00 16.16  ?  183 GLY A C   1 
ATOM   1317 O  O   . GLY A 1 183 ? 25.029  25.503  -6.894  1.00 15.04  ?  183 GLY A O   1 
ATOM   1318 N  N   . ASP A 1 184 ? 25.502  25.069  -9.083  1.00 14.97  ?  184 ASP A N   1 
ATOM   1319 C  CA  . ASP A 1 184 ? 24.927  26.282  -9.646  1.00 16.23  ?  184 ASP A CA  1 
ATOM   1320 C  C   . ASP A 1 184 ? 23.461  26.020  -10.001 1.00 15.58  ?  184 ASP A C   1 
ATOM   1321 O  O   . ASP A 1 184 ? 23.067  24.898  -10.282 1.00 16.65  ?  184 ASP A O   1 
ATOM   1322 C  CB  . ASP A 1 184 ? 25.655  26.677  -10.921 1.00 15.54  ?  184 ASP A CB  1 
ATOM   1323 C  CG  . ASP A 1 184 ? 27.147  26.941  -10.808 1.00 15.96  ?  184 ASP A CG  1 
ATOM   1324 O  OD1 . ASP A 1 184 ? 27.595  27.280  -9.709  1.00 15.37  ?  184 ASP A OD1 1 
ATOM   1325 O  OD2 . ASP A 1 184 ? 27.849  26.674  -11.814 1.00 17.08  -1 184 ASP A OD2 1 
ATOM   1326 N  N   . LEU A 1 185 ? 22.664  27.083  -10.005 1.00 14.81  ?  185 LEU A N   1 
ATOM   1327 C  CA  . LEU A 1 185 ? 21.259  27.070  -10.373 1.00 16.85  ?  185 LEU A CA  1 
ATOM   1328 C  C   . LEU A 1 185 ? 21.158  27.719  -11.753 1.00 16.60  ?  185 LEU A C   1 
ATOM   1329 O  O   . LEU A 1 185 ? 21.740  28.787  -11.979 1.00 16.52  ?  185 LEU A O   1 
ATOM   1330 C  CB  . LEU A 1 185 ? 20.571  27.860  -9.270  1.00 19.24  ?  185 LEU A CB  1 
ATOM   1331 C  CG  . LEU A 1 185 ? 19.055  27.992  -9.290  1.00 25.89  ?  185 LEU A CG  1 
ATOM   1332 C  CD1 . LEU A 1 185 ? 18.326  26.671  -9.268  1.00 30.88  ?  185 LEU A CD1 1 
ATOM   1333 C  CD2 . LEU A 1 185 ? 18.626  28.835  -8.055  1.00 31.69  ?  185 LEU A CD2 1 
ATOM   1334 N  N   . ARG A 1 186 ? 20.458  27.029  -12.656 1.00 17.11  ?  186 ARG A N   1 
ATOM   1335 C  CA  . ARG A 1 186 ? 20.148  27.493  -13.997 1.00 19.72  ?  186 ARG A CA  1 
ATOM   1336 C  C   . ARG A 1 186 ? 18.644  27.638  -14.170 1.00 20.52  ?  186 ARG A C   1 
ATOM   1337 O  O   . ARG A 1 186 ? 17.873  26.915  -13.556 1.00 20.34  ?  186 ARG A O   1 
ATOM   1338 C  CB  . ARG A 1 186 ? 20.635  26.489  -15.045 1.00 20.74  ?  186 ARG A CB  1 
ATOM   1339 C  CG  . ARG A 1 186 ? 22.144  26.560  -15.225 1.00 25.27  ?  186 ARG A CG  1 
ATOM   1340 C  CD  . ARG A 1 186 ? 22.655  25.453  -16.109 1.00 29.09  ?  186 ARG A CD  1 
ATOM   1341 N  NE  . ARG A 1 186 ? 24.053  25.723  -16.444 1.00 33.62  ?  186 ARG A NE  1 
ATOM   1342 C  CZ  . ARG A 1 186 ? 25.125  25.214  -15.818 1.00 37.93  ?  186 ARG A CZ  1 
ATOM   1343 N  NH1 . ARG A 1 186 ? 25.037  24.639  -14.618 1.00 31.28  1  186 ARG A NH1 1 
ATOM   1344 N  NH2 . ARG A 1 186 ? 26.305  25.332  -16.398 1.00 37.42  ?  186 ARG A NH2 1 
ATOM   1345 N  N   . ASP A 1 187 ? 18.247  28.619  -14.992 1.00 21.38  ?  187 ASP A N   1 
ATOM   1346 C  CA  . ASP A 1 187 ? 16.846  28.794  -15.376 1.00 21.57  ?  187 ASP A CA  1 
ATOM   1347 C  C   . ASP A 1 187 ? 16.478  27.798  -16.479 1.00 23.28  ?  187 ASP A C   1 
ATOM   1348 O  O   . ASP A 1 187 ? 17.238  26.883  -16.799 1.00 23.18  ?  187 ASP A O   1 
ATOM   1349 C  CB  . ASP A 1 187 ? 16.568  30.244  -15.720 1.00 22.77  ?  187 ASP A CB  1 
ATOM   1350 C  CG  . ASP A 1 187 ? 17.191  30.761  -17.018 1.00 24.41  ?  187 ASP A CG  1 
ATOM   1351 O  OD1 . ASP A 1 187 ? 17.668  29.934  -17.831 1.00 26.33  ?  187 ASP A OD1 1 
ATOM   1352 O  OD2 . ASP A 1 187 ? 17.228  31.978  -17.159 1.00 28.54  -1 187 ASP A OD2 1 
ATOM   1353 N  N   . THR A 1 188 ? 15.260  27.920  -17.029 1.00 29.71  ?  188 THR A N   1 
ATOM   1354 C  CA  . THR A 1 188 ? 14.721  26.890  -17.920 1.00 31.01  ?  188 THR A CA  1 
ATOM   1355 C  C   . THR A 1 188 ? 15.370  26.973  -19.305 1.00 35.34  ?  188 THR A C   1 
ATOM   1356 O  O   . THR A 1 188 ? 15.351  25.992  -20.049 1.00 41.22  ?  188 THR A O   1 
ATOM   1357 C  CB  . THR A 1 188 ? 13.193  26.992  -18.018 1.00 32.20  ?  188 THR A CB  1 
ATOM   1358 O  OG1 . THR A 1 188 ? 12.848  28.371  -18.155 1.00 30.61  ?  188 THR A OG1 1 
ATOM   1359 C  CG2 . THR A 1 188 ? 12.528  26.458  -16.759 1.00 32.61  ?  188 THR A CG2 1 
ATOM   1360 N  N   . ALA A 1 189 ? 15.954  28.131  -19.633 1.00 37.24  ?  189 ALA A N   1 
ATOM   1361 C  CA  . ALA A 1 189 ? 16.739  28.315  -20.854 1.00 37.75  ?  189 ALA A CA  1 
ATOM   1362 C  C   . ALA A 1 189 ? 18.150  27.744  -20.703 1.00 43.85  ?  189 ALA A C   1 
ATOM   1363 O  O   . ALA A 1 189 ? 18.845  27.552  -21.696 1.00 45.63  ?  189 ALA A O   1 
ATOM   1364 C  CB  . ALA A 1 189 ? 16.806  29.793  -21.185 1.00 35.90  ?  189 ALA A CB  1 
ATOM   1365 N  N   . GLY A 1 190 ? 18.599  27.529  -19.455 1.00 35.79  ?  190 GLY A N   1 
ATOM   1366 C  CA  . GLY A 1 190 ? 19.921  26.973  -19.180 1.00 32.46  ?  190 GLY A CA  1 
ATOM   1367 C  C   . GLY A 1 190 ? 20.959  28.038  -18.852 1.00 28.10  ?  190 GLY A C   1 
ATOM   1368 O  O   . GLY A 1 190 ? 22.140  27.739  -18.875 1.00 29.79  ?  190 GLY A O   1 
ATOM   1369 N  N   . ARG A 1 191 ? 20.533  29.276  -18.527 1.00 27.79  ?  191 ARG A N   1 
ATOM   1370 C  CA  . ARG A 1 191 ? 21.428  30.323  -18.068 1.00 26.96  ?  191 ARG A CA  1 
ATOM   1371 C  C   . ARG A 1 191 ? 21.726  30.203  -16.569 1.00 24.24  ?  191 ARG A C   1 
ATOM   1372 O  O   . ARG A 1 191 ? 20.810  30.012  -15.762 1.00 21.11  ?  191 ARG A O   1 
ATOM   1373 C  CB  . ARG A 1 191 ? 20.770  31.694  -18.198 1.00 29.10  ?  191 ARG A CB  1 
ATOM   1374 C  CG  . ARG A 1 191 ? 20.292  32.033  -19.596 1.00 39.50  ?  191 ARG A CG  1 
ATOM   1375 C  CD  . ARG A 1 191 ? 19.697  33.438  -19.556 1.00 43.60  ?  191 ARG A CD  1 
ATOM   1376 N  NE  . ARG A 1 191 ? 18.349  33.316  -20.118 1.00 57.44  ?  191 ARG A NE  1 
ATOM   1377 C  CZ  . ARG A 1 191 ? 17.228  33.854  -19.646 1.00 69.64  ?  191 ARG A CZ  1 
ATOM   1378 N  NH1 . ARG A 1 191 ? 17.263  34.866  -18.785 1.00 75.56  1  191 ARG A NH1 1 
ATOM   1379 N  NH2 . ARG A 1 191 ? 16.073  33.408  -20.109 1.00 69.69  ?  191 ARG A NH2 1 
ATOM   1380 N  N   . ILE A 1 192 ? 22.979  30.487  -16.168 1.00 23.05  ?  192 ILE A N   1 
ATOM   1381 C  CA  . ILE A 1 192 ? 23.332  30.450  -14.757 1.00 20.24  ?  192 ILE A CA  1 
ATOM   1382 C  C   . ILE A 1 192 ? 22.736  31.673  -14.080 1.00 21.44  ?  192 ILE A C   1 
ATOM   1383 O  O   . ILE A 1 192 ? 23.011  32.764  -14.533 1.00 21.25  ?  192 ILE A O   1 
ATOM   1384 C  CB  . ILE A 1 192 ? 24.851  30.405  -14.547 1.00 20.05  ?  192 ILE A CB  1 
ATOM   1385 C  CG1 . ILE A 1 192 ? 25.427  29.119  -15.147 1.00 22.78  ?  192 ILE A CG1 1 
ATOM   1386 C  CG2 . ILE A 1 192 ? 25.147  30.515  -13.033 1.00 22.86  ?  192 ILE A CG2 1 
ATOM   1387 C  CD1 . ILE A 1 192 ? 26.948  29.011  -15.079 1.00 23.33  ?  192 ILE A CD1 1 
ATOM   1388 N  N   . VAL A 1 193 ? 21.917  31.499  -13.040 1.00 19.09  ?  193 VAL A N   1 
ATOM   1389 C  CA  . VAL A 1 193 ? 21.346  32.638  -12.346 1.00 19.70  ?  193 VAL A CA  1 
ATOM   1390 C  C   . VAL A 1 193 ? 21.940  32.802  -10.958 1.00 19.72  ?  193 VAL A C   1 
ATOM   1391 O  O   . VAL A 1 193 ? 21.852  33.876  -10.394 1.00 21.10  ?  193 VAL A O   1 
ATOM   1392 C  CB  . VAL A 1 193 ? 19.815  32.631  -12.301 1.00 24.43  ?  193 VAL A CB  1 
ATOM   1393 C  CG1 . VAL A 1 193 ? 19.248  32.722  -13.713 1.00 28.12  ?  193 VAL A CG1 1 
ATOM   1394 C  CG2 . VAL A 1 193 ? 19.278  31.426  -11.583 1.00 27.38  ?  193 VAL A CG2 1 
ATOM   1395 N  N   . ALA A 1 194 ? 22.525  31.739  -10.401 1.00 17.26  ?  194 ALA A N   1 
ATOM   1396 C  CA  . ALA A 1 194 ? 23.172  31.812  -9.109  1.00 17.81  ?  194 ALA A CA  1 
ATOM   1397 C  C   . ALA A 1 194 ? 24.231  30.725  -9.089  1.00 16.92  ?  194 ALA A C   1 
ATOM   1398 O  O   . ALA A 1 194 ? 23.964  29.635  -9.568  1.00 18.71  ?  194 ALA A O   1 
ATOM   1399 C  CB  . ALA A 1 194 ? 22.156  31.657  -8.015  1.00 19.13  ?  194 ALA A CB  1 
ATOM   1400 N  N   . GLY A 1 195 ? 25.383  30.983  -8.487  1.00 15.43  ?  195 GLY A N   1 
ATOM   1401 C  CA  . GLY A 1 195 ? 26.462  30.017  -8.558  1.00 15.88  ?  195 GLY A CA  1 
ATOM   1402 C  C   . GLY A 1 195 ? 27.819  30.588  -8.153  1.00 15.55  ?  195 GLY A C   1 
ATOM   1403 O  O   . GLY A 1 195 ? 27.915  31.751  -7.740  1.00 16.77  ?  195 GLY A O   1 
ATOM   1404 N  N   . ALA A 1 196 ? 28.842  29.733  -8.228  1.00 14.66  ?  196 ALA A N   1 
ATOM   1405 C  CA  . ALA A 1 196 ? 30.211  30.109  -7.904  1.00 16.12  ?  196 ALA A CA  1 
ATOM   1406 C  C   . ALA A 1 196 ? 30.705  31.201  -8.863  1.00 18.16  ?  196 ALA A C   1 
ATOM   1407 O  O   . ALA A 1 196 ? 30.466  31.118  -10.065 1.00 16.33  ?  196 ALA A O   1 
ATOM   1408 C  CB  . ALA A 1 196 ? 31.098  28.912  -7.967  1.00 16.52  ?  196 ALA A CB  1 
ATOM   1409 N  N   . LYS A 1 197 ? 31.436  32.181  -8.329  1.00 20.52  ?  197 LYS A N   1 
ATOM   1410 C  CA  . LYS A 1 197 ? 31.978  33.302  -9.109  1.00 23.96  ?  197 LYS A CA  1 
ATOM   1411 C  C   . LYS A 1 197 ? 33.507  33.286  -9.078  1.00 23.21  ?  197 LYS A C   1 
ATOM   1412 O  O   . LYS A 1 197 ? 34.094  32.898  -8.071  1.00 22.24  ?  197 LYS A O   1 
ATOM   1413 C  CB  . LYS A 1 197 ? 31.447  34.631  -8.565  1.00 27.40  ?  197 LYS A CB  1 
ATOM   1414 C  CG  . LYS A 1 197 ? 29.946  34.833  -8.890  1.00 31.07  ?  197 LYS A CG  1 
ATOM   1415 C  CD  . LYS A 1 197 ? 29.097  35.587  -7.867  1.00 41.42  ?  197 LYS A CD  1 
ATOM   1416 C  CE  . LYS A 1 197 ? 29.765  36.703  -7.161  1.00 49.47  ?  197 LYS A CE  1 
ATOM   1417 N  NZ  . LYS A 1 197 ? 28.843  37.314  -6.191  1.00 58.38  1  197 LYS A NZ  1 
ATOM   1418 N  N   . TYR A 1 198 ? 34.131  33.610  -10.231 1.00 23.18  ?  198 TYR A N   1 
ATOM   1419 C  CA  . TYR A 1 198 ? 35.558  33.883  -10.284 1.00 25.82  ?  198 TYR A CA  1 
ATOM   1420 C  C   . TYR A 1 198 ? 35.838  35.146  -9.469  1.00 27.82  ?  198 TYR A C   1 
ATOM   1421 O  O   . TYR A 1 198 ? 34.935  35.973  -9.273  1.00 30.03  ?  198 TYR A O   1 
ATOM   1422 C  CB  . TYR A 1 198 ? 35.992  34.213  -11.712 1.00 26.94  ?  198 TYR A CB  1 
ATOM   1423 C  CG  . TYR A 1 198 ? 36.125  33.067  -12.690 1.00 26.35  ?  198 TYR A CG  1 
ATOM   1424 C  CD1 . TYR A 1 198 ? 36.924  31.975  -12.416 1.00 27.23  ?  198 TYR A CD1 1 
ATOM   1425 C  CD2 . TYR A 1 198 ? 35.435  33.088  -13.895 1.00 28.83  ?  198 TYR A CD2 1 
ATOM   1426 C  CE1 . TYR A 1 198 ? 37.053  30.934  -13.324 1.00 28.73  ?  198 TYR A CE1 1 
ATOM   1427 C  CE2 . TYR A 1 198 ? 35.535  32.049  -14.808 1.00 29.04  ?  198 TYR A CE2 1 
ATOM   1428 C  CZ  . TYR A 1 198 ? 36.363  30.977  -14.528 1.00 29.81  ?  198 TYR A CZ  1 
ATOM   1429 O  OH  . TYR A 1 198 ? 36.511  29.958  -15.415 1.00 28.43  ?  198 TYR A OH  1 
ATOM   1430 N  N   . GLU A 1 199 ? 37.096  35.316  -9.050  1.00 32.51  ?  199 GLU A N   1 
ATOM   1431 C  CA  . GLU A 1 199 ? 37.490  36.529  -8.330  1.00 40.11  ?  199 GLU A CA  1 
ATOM   1432 C  C   . GLU A 1 199 ? 37.242  37.763  -9.200  1.00 37.54  ?  199 GLU A C   1 
ATOM   1433 O  O   . GLU A 1 199 ? 36.703  38.750  -8.724  1.00 36.61  ?  199 GLU A O   1 
ATOM   1434 C  CB  . GLU A 1 199 ? 38.930  36.418  -7.817  1.00 47.93  ?  199 GLU A CB  1 
ATOM   1435 C  CG  . GLU A 1 199 ? 39.019  35.404  -6.673  1.00 66.75  ?  199 GLU A CG  1 
ATOM   1436 C  CD  . GLU A 1 199 ? 40.249  35.433  -5.782  1.00 76.82  ?  199 GLU A CD  1 
ATOM   1437 O  OE1 . GLU A 1 199 ? 41.349  35.223  -6.336  1.00 78.19  ?  199 GLU A OE1 1 
ATOM   1438 O  OE2 . GLU A 1 199 ? 40.100  35.639  -4.550  1.00 79.28  -1 199 GLU A OE2 1 
ATOM   1439 N  N   . GLY A 1 200 ? 37.502  37.650  -10.507 1.00 43.09  ?  200 GLY A N   1 
ATOM   1440 C  CA  . GLY A 1 200 ? 37.293  38.739  -11.458 1.00 44.19  ?  200 GLY A CA  1 
ATOM   1441 C  C   . GLY A 1 200 ? 35.827  39.092  -11.729 1.00 43.28  ?  200 GLY A C   1 
ATOM   1442 O  O   . GLY A 1 200 ? 35.592  40.148  -12.336 1.00 37.75  ?  200 GLY A O   1 
ATOM   1443 N  N   . GLY A 1 201 ? 34.882  38.204  -11.346 1.00 35.87  ?  201 GLY A N   1 
ATOM   1444 C  CA  . GLY A 1 201 ? 33.496  38.580  -11.065 1.00 35.44  ?  201 GLY A CA  1 
ATOM   1445 C  C   . GLY A 1 201 ? 32.413  37.718  -11.745 1.00 28.12  ?  201 GLY A C   1 
ATOM   1446 O  O   . GLY A 1 201 ? 31.270  37.695  -11.289 1.00 30.91  ?  201 GLY A O   1 
ATOM   1447 N  N   . GLU A 1 202 ? 32.701  37.081  -12.883 1.00 26.61  ?  202 GLU A N   1 
ATOM   1448 C  CA  . GLU A 1 202 ? 31.642  36.353  -13.607 1.00 24.55  ?  202 GLU A CA  1 
ATOM   1449 C  C   . GLU A 1 202 ? 31.374  34.982  -12.957 1.00 21.99  ?  202 GLU A C   1 
ATOM   1450 O  O   . GLU A 1 202 ? 32.256  34.418  -12.287 1.00 17.81  ?  202 GLU A O   1 
ATOM   1451 C  CB  . GLU A 1 202 ? 32.036  36.144  -15.072 1.00 28.87  ?  202 GLU A CB  1 
ATOM   1452 C  CG  . GLU A 1 202 ? 32.217  37.450  -15.859 1.00 34.24  ?  202 GLU A CG  1 
ATOM   1453 C  CD  . GLU A 1 202 ? 31.032  38.414  -15.854 1.00 33.05  ?  202 GLU A CD  1 
ATOM   1454 O  OE1 . GLU A 1 202 ? 29.910  37.928  -15.732 1.00 40.65  ?  202 GLU A OE1 1 
ATOM   1455 O  OE2 . GLU A 1 202 ? 31.204  39.648  -15.895 1.00 29.44  -1 202 GLU A OE2 1 
ATOM   1456 N  N   . PHE A 1 203 ? 30.191  34.401  -13.231 1.00 18.17  ?  203 PHE A N   1 
ATOM   1457 C  CA  . PHE A 1 203 ? 29.964  32.990  -12.916 1.00 18.01  ?  203 PHE A CA  1 
ATOM   1458 C  C   . PHE A 1 203 ? 31.027  32.114  -13.561 1.00 18.70  ?  203 PHE A C   1 
ATOM   1459 O  O   . PHE A 1 203 ? 31.298  32.237  -14.760 1.00 21.12  ?  203 PHE A O   1 
ATOM   1460 C  CB  . PHE A 1 203 ? 28.566  32.575  -13.368 1.00 18.77  ?  203 PHE A CB  1 
ATOM   1461 C  CG  . PHE A 1 203 ? 27.427  33.235  -12.610 1.00 18.06  ?  203 PHE A CG  1 
ATOM   1462 C  CD1 . PHE A 1 203 ? 27.392  33.230  -11.221 1.00 19.31  ?  203 PHE A CD1 1 
ATOM   1463 C  CD2 . PHE A 1 203 ? 26.374  33.853  -13.283 1.00 19.79  ?  203 PHE A CD2 1 
ATOM   1464 C  CE1 . PHE A 1 203 ? 26.331  33.829  -10.525 1.00 19.67  ?  203 PHE A CE1 1 
ATOM   1465 C  CE2 . PHE A 1 203 ? 25.336  34.457  -12.579 1.00 21.07  ?  203 PHE A CE2 1 
ATOM   1466 C  CZ  . PHE A 1 203 ? 25.335  34.490  -11.205 1.00 21.04  ?  203 PHE A CZ  1 
ATOM   1467 N  N   . ALA A 1 204 ? 31.565  31.175  -12.784 1.00 16.11  ?  204 ALA A N   1 
ATOM   1468 C  CA  . ALA A 1 204 ? 32.635  30.325  -13.241 1.00 18.12  ?  204 ALA A CA  1 
ATOM   1469 C  C   . ALA A 1 204 ? 32.130  29.137  -14.032 1.00 18.33  ?  204 ALA A C   1 
ATOM   1470 O  O   . ALA A 1 204 ? 32.902  28.601  -14.805 1.00 16.33  ?  204 ALA A O   1 
ATOM   1471 C  CB  . ALA A 1 204 ? 33.457  29.853  -12.080 1.00 19.15  ?  204 ALA A CB  1 
ATOM   1472 N  N   . ASP A 1 205 ? 30.877  28.695  -13.802 1.00 16.58  ?  205 ASP A N   1 
ATOM   1473 C  CA  . ASP A 1 205 ? 30.371  27.408  -14.290 1.00 17.17  ?  205 ASP A CA  1 
ATOM   1474 C  C   . ASP A 1 205 ? 31.032  26.253  -13.531 1.00 16.39  ?  205 ASP A C   1 
ATOM   1475 O  O   . ASP A 1 205 ? 32.079  25.704  -13.939 1.00 15.43  ?  205 ASP A O   1 
ATOM   1476 C  CB  . ASP A 1 205 ? 30.437  27.273  -15.810 1.00 20.91  ?  205 ASP A CB  1 
ATOM   1477 C  CG  . ASP A 1 205 ? 29.710  26.053  -16.380 1.00 22.14  ?  205 ASP A CG  1 
ATOM   1478 O  OD1 . ASP A 1 205 ? 29.422  25.090  -15.628 1.00 19.67  ?  205 ASP A OD1 1 
ATOM   1479 O  OD2 . ASP A 1 205 ? 29.520  26.011  -17.602 1.00 24.85  -1 205 ASP A OD2 1 
ATOM   1480 N  N   . THR A 1 206 ? 30.427  25.893  -12.388 1.00 13.78  ?  206 THR A N   1 
ATOM   1481 C  CA  . THR A 1 206 ? 31.040  24.952  -11.468 1.00 14.51  ?  206 THR A CA  1 
ATOM   1482 C  C   . THR A 1 206 ? 31.413  23.653  -12.172 1.00 15.39  ?  206 THR A C   1 
ATOM   1483 O  O   . THR A 1 206 ? 32.519  23.144  -12.015 1.00 15.83  ?  206 THR A O   1 
ATOM   1484 C  CB  . THR A 1 206 ? 30.107  24.706  -10.284 1.00 15.37  ?  206 THR A CB  1 
ATOM   1485 O  OG1 . THR A 1 206 ? 30.036  25.891  -9.502  1.00 14.31  ?  206 THR A OG1 1 
ATOM   1486 C  CG2 . THR A 1 206 ? 30.597  23.594  -9.375  1.00 16.07  ?  206 THR A CG2 1 
ATOM   1487 N  N   . TYR A 1 207 ? 30.467  23.070  -12.908 1.00 13.84  ?  207 TYR A N   1 
ATOM   1488 C  CA  . TYR A 1 207 ? 30.738  21.761  -13.507 1.00 15.88  ?  207 TYR A CA  1 
ATOM   1489 C  C   . TYR A 1 207 ? 31.883  21.837  -14.530 1.00 16.67  ?  207 TYR A C   1 
ATOM   1490 O  O   . TYR A 1 207 ? 32.766  20.970  -14.555 1.00 15.90  ?  207 TYR A O   1 
ATOM   1491 C  CB  . TYR A 1 207 ? 29.431  21.234  -14.111 1.00 16.22  ?  207 TYR A CB  1 
ATOM   1492 C  CG  . TYR A 1 207 ? 29.584  19.916  -14.867 1.00 16.18  ?  207 TYR A CG  1 
ATOM   1493 C  CD1 . TYR A 1 207 ? 30.276  18.846  -14.319 1.00 16.79  ?  207 TYR A CD1 1 
ATOM   1494 C  CD2 . TYR A 1 207 ? 29.057  19.767  -16.144 1.00 17.46  ?  207 TYR A CD2 1 
ATOM   1495 C  CE1 . TYR A 1 207 ? 30.438  17.661  -15.015 1.00 19.01  ?  207 TYR A CE1 1 
ATOM   1496 C  CE2 . TYR A 1 207 ? 29.196  18.575  -16.839 1.00 18.37  ?  207 TYR A CE2 1 
ATOM   1497 C  CZ  . TYR A 1 207 ? 29.903  17.529  -16.283 1.00 18.46  ?  207 TYR A CZ  1 
ATOM   1498 O  OH  . TYR A 1 207 ? 30.051  16.392  -17.005 1.00 19.13  ?  207 TYR A OH  1 
ATOM   1499 N  N   . ALA A 1 208 ? 31.866  22.876  -15.375 1.00 16.53  ?  208 ALA A N   1 
ATOM   1500 C  CA  . ALA A 1 208 ? 32.935  23.061  -16.360 1.00 18.03  ?  208 ALA A CA  1 
ATOM   1501 C  C   . ALA A 1 208 ? 34.300  23.138  -15.667 1.00 16.25  ?  208 ALA A C   1 
ATOM   1502 O  O   . ALA A 1 208 ? 35.269  22.520  -16.105 1.00 16.37  ?  208 ALA A O   1 
ATOM   1503 C  CB  . ALA A 1 208 ? 32.683  24.307  -17.208 1.00 18.64  ?  208 ALA A CB  1 
ATOM   1504 N  N   . ARG A 1 209 ? 34.383  23.873  -14.553 1.00 17.37  ?  209 ARG A N   1 
ATOM   1505 C  CA  . ARG A 1 209 ? 35.623  24.045  -13.815 1.00 15.89  ?  209 ARG A CA  1 
ATOM   1506 C  C   . ARG A 1 209 ? 36.075  22.738  -13.173 1.00 17.99  ?  209 ARG A C   1 
ATOM   1507 O  O   . ARG A 1 209 ? 37.276  22.406  -13.129 1.00 17.66  ?  209 ARG A O   1 
ATOM   1508 C  CB  . ARG A 1 209 ? 35.475  25.103  -12.718 1.00 17.27  ?  209 ARG A CB  1 
ATOM   1509 C  CG  . ARG A 1 209 ? 35.238  26.520  -13.216 1.00 20.87  ?  209 ARG A CG  1 
ATOM   1510 C  CD  . ARG A 1 209 ? 36.233  26.982  -14.293 1.00 23.96  ?  209 ARG A CD  1 
ATOM   1511 N  NE  . ARG A 1 209 ? 37.620  26.813  -13.839 1.00 27.30  ?  209 ARG A NE  1 
ATOM   1512 C  CZ  . ARG A 1 209 ? 38.735  27.059  -14.549 1.00 34.77  ?  209 ARG A CZ  1 
ATOM   1513 N  NH1 . ARG A 1 209 ? 38.686  27.666  -15.718 1.00 36.64  1  209 ARG A NH1 1 
ATOM   1514 N  NH2 . ARG A 1 209 ? 39.911  26.653  -14.086 1.00 34.68  ?  209 ARG A NH2 1 
ATOM   1515 N  N   . MET A 1 210 ? 35.122  21.987  -12.625 1.00 15.96  ?  210 MET A N   1 
ATOM   1516 C  CA  . MET A 1 210 ? 35.473  20.687  -12.080 1.00 20.49  ?  210 MET A CA  1 
ATOM   1517 C  C   . MET A 1 210 ? 36.026  19.735  -13.151 1.00 19.04  ?  210 MET A C   1 
ATOM   1518 O  O   . MET A 1 210 ? 36.945  18.961  -12.851 1.00 19.45  ?  210 MET A O   1 
ATOM   1519 C  CB  . MET A 1 210 ? 34.280  20.076  -11.326 1.00 20.14  ?  210 MET A CB  1 
ATOM   1520 C  CG  . MET A 1 210 ? 33.928  20.892  -10.079 1.00 21.71  ?  210 MET A CG  1 
ATOM   1521 S  SD  . MET A 1 210 ? 32.511  20.188  -9.195  1.00 25.79  ?  210 MET A SD  1 
ATOM   1522 C  CE  . MET A 1 210 ? 33.302  18.851  -8.301  1.00 31.49  ?  210 MET A CE  1 
ATOM   1523 N  N   . LYS A 1 211 ? 35.459  19.752  -14.372 1.00 17.95  ?  211 LYS A N   1 
ATOM   1524 C  CA  . LYS A 1 211 ? 35.957  18.914  -15.464 1.00 19.82  ?  211 LYS A CA  1 
ATOM   1525 C  C   . LYS A 1 211 ? 37.402  19.277  -15.847 1.00 22.98  ?  211 LYS A C   1 
ATOM   1526 O  O   . LYS A 1 211 ? 38.162  18.423  -16.287 1.00 24.16  ?  211 LYS A O   1 
ATOM   1527 C  CB  . LYS A 1 211 ? 35.071  19.019  -16.711 1.00 22.26  ?  211 LYS A CB  1 
ATOM   1528 C  CG  . LYS A 1 211 ? 33.729  18.278  -16.626 1.00 24.65  ?  211 LYS A CG  1 
ATOM   1529 C  CD  . LYS A 1 211 ? 32.718  18.684  -17.710 1.00 27.91  ?  211 LYS A CD  1 
ATOM   1530 C  CE  . LYS A 1 211 ? 32.880  18.069  -18.994 1.00 32.41  ?  211 LYS A CE  1 
ATOM   1531 N  NZ  . LYS A 1 211 ? 31.812  18.527  -19.892 1.00 28.51  1  211 LYS A NZ  1 
ATOM   1532 N  N   . LEU A 1 212 ? 37.773  20.541  -15.686 1.00 23.63  ?  212 LEU A N   1 
ATOM   1533 C  CA  . LEU A 1 212 ? 39.115  21.056  -15.950 1.00 28.38  ?  212 LEU A CA  1 
ATOM   1534 C  C   . LEU A 1 212 ? 40.079  20.711  -14.820 1.00 27.43  ?  212 LEU A C   1 
ATOM   1535 O  O   . LEU A 1 212 ? 41.279  20.805  -15.003 1.00 30.22  ?  212 LEU A O   1 
ATOM   1536 C  CB  . LEU A 1 212 ? 39.115  22.572  -16.138 1.00 28.54  ?  212 LEU A CB  1 
ATOM   1537 C  CG  . LEU A 1 212 ? 38.954  23.135  -17.553 1.00 39.83  ?  212 LEU A CG  1 
ATOM   1538 C  CD1 . LEU A 1 212 ? 39.412  22.164  -18.630 1.00 40.71  ?  212 LEU A CD1 1 
ATOM   1539 C  CD2 . LEU A 1 212 ? 37.586  23.675  -17.840 1.00 42.11  ?  212 LEU A CD2 1 
ATOM   1540 N  N   . GLY A 1 213 ? 39.576  20.397  -13.631 1.00 25.55  ?  213 GLY A N   1 
ATOM   1541 C  CA  . GLY A 1 213 ? 40.431  19.982  -12.532 1.00 25.06  ?  213 GLY A CA  1 
ATOM   1542 C  C   . GLY A 1 213 ? 40.378  20.844  -11.268 1.00 27.92  ?  213 GLY A C   1 
ATOM   1543 O  O   . GLY A 1 213 ? 41.079  20.509  -10.308 1.00 28.43  ?  213 GLY A O   1 
ATOM   1544 N  N   . ASP A 1 214 ? 39.540  21.896  -11.213 1.00 25.48  ?  214 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 214 ? 39.413  22.681  -9.991  1.00 27.04  ?  214 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 214 ? 38.776  21.811  -8.916  1.00 32.03  ?  214 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 214 ? 37.799  21.118  -9.184  1.00 28.99  ?  214 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 214 ? 38.540  23.921  -10.111 1.00 25.83  ?  214 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 214 ? 39.103  24.994  -11.030 1.00 28.87  ?  214 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 214 ? 40.160  24.745  -11.593 1.00 31.54  ?  214 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 214 ? 38.484  26.055  -11.168 1.00 25.97  -1 214 ASP A OD2 1 
ATOM   1552 N  N   . LYS A 1 215 ? 39.311  21.943  -7.703  1.00 30.52  ?  215 LYS A N   1 
ATOM   1553 C  CA  . LYS A 1 215 ? 38.994  21.071  -6.584  1.00 36.17  ?  215 LYS A CA  1 
ATOM   1554 C  C   . LYS A 1 215 ? 38.066  21.795  -5.617  1.00 34.80  ?  215 LYS A C   1 
ATOM   1555 O  O   . LYS A 1 215 ? 38.160  23.007  -5.427  1.00 31.90  ?  215 LYS A O   1 
ATOM   1556 C  CB  . LYS A 1 215 ? 40.298  20.673  -5.874  1.00 45.90  ?  215 LYS A CB  1 
ATOM   1557 C  CG  . LYS A 1 215 ? 40.688  19.188  -5.933  1.00 57.13  ?  215 LYS A CG  1 
ATOM   1558 C  CD  . LYS A 1 215 ? 40.748  18.486  -7.294  1.00 64.96  ?  215 LYS A CD  1 
ATOM   1559 C  CE  . LYS A 1 215 ? 40.286  17.037  -7.215  1.00 66.04  ?  215 LYS A CE  1 
ATOM   1560 N  NZ  . LYS A 1 215 ? 39.845  16.574  -8.533  1.00 72.21  1  215 LYS A NZ  1 
ATOM   1561 N  N   . ASN A 1 216 ? 37.188  21.009  -4.992  1.00 33.06  ?  216 ASN A N   1 
ATOM   1562 C  CA  . ASN A 1 216 ? 36.172  21.506  -4.088  1.00 31.29  ?  216 ASN A CA  1 
ATOM   1563 C  C   . ASN A 1 216 ? 36.849  22.064  -2.833  1.00 33.22  ?  216 ASN A C   1 
ATOM   1564 O  O   . ASN A 1 216 ? 37.464  21.332  -2.080  1.00 34.68  ?  216 ASN A O   1 
ATOM   1565 C  CB  . ASN A 1 216 ? 35.189  20.376  -3.803  1.00 33.50  ?  216 ASN A CB  1 
ATOM   1566 C  CG  . ASN A 1 216 ? 34.086  20.765  -2.841  1.00 35.30  ?  216 ASN A CG  1 
ATOM   1567 O  OD1 . ASN A 1 216 ? 34.048  21.878  -2.289  1.00 29.29  ?  216 ASN A OD1 1 
ATOM   1568 N  ND2 . ASN A 1 216 ? 33.156  19.845  -2.654  1.00 34.93  ?  216 ASN A ND2 1 
ATOM   1569 N  N   . GLN A 1 217 ? 36.677  23.360  -2.565  1.00 31.37  ?  217 GLN A N   1 
ATOM   1570 C  CA  . GLN A 1 217 ? 37.263  23.993  -1.396  1.00 34.26  ?  217 GLN A CA  1 
ATOM   1571 C  C   . GLN A 1 217 ? 36.204  24.385  -0.365  1.00 32.87  ?  217 GLN A C   1 
ATOM   1572 O  O   . GLN A 1 217 ? 36.476  25.228  0.488   1.00 33.75  ?  217 GLN A O   1 
ATOM   1573 C  CB  . GLN A 1 217 ? 37.988  25.273  -1.806  1.00 40.44  ?  217 GLN A CB  1 
ATOM   1574 C  CG  . GLN A 1 217 ? 39.073  25.041  -2.848  1.00 48.47  ?  217 GLN A CG  1 
ATOM   1575 C  CD  . GLN A 1 217 ? 40.022  26.209  -2.954  1.00 61.22  ?  217 GLN A CD  1 
ATOM   1576 O  OE1 . GLN A 1 217 ? 41.117  26.173  -2.386  1.00 76.65  ?  217 GLN A OE1 1 
ATOM   1577 N  NE2 . GLN A 1 217 ? 39.598  27.263  -3.642  1.00 67.50  ?  217 GLN A NE2 1 
ATOM   1578 N  N   . SER A 1 218 ? 34.998  23.802  -0.436  1.00 30.81  ?  218 SER A N   1 
ATOM   1579 C  CA  . SER A 1 218 ? 33.972  24.169  0.533   1.00 30.76  ?  218 SER A CA  1 
ATOM   1580 C  C   . SER A 1 218 ? 34.308  23.547  1.894   1.00 33.09  ?  218 SER A C   1 
ATOM   1581 O  O   . SER A 1 218 ? 35.032  22.554  1.983   1.00 30.34  ?  218 SER A O   1 
ATOM   1582 C  CB  . SER A 1 218 ? 32.598  23.767  0.083   1.00 28.80  ?  218 SER A CB  1 
ATOM   1583 O  OG  . SER A 1 218 ? 32.490  22.359  0.066   1.00 29.80  ?  218 SER A OG  1 
ATOM   1584 N  N   . ALA A 1 219 ? 33.720  24.115  2.951   1.00 35.22  ?  219 ALA A N   1 
ATOM   1585 C  CA  . ALA A 1 219 ? 34.036  23.719  4.321   1.00 36.16  ?  219 ALA A CA  1 
ATOM   1586 C  C   . ALA A 1 219 ? 33.826  22.222  4.549   1.00 33.61  ?  219 ALA A C   1 
ATOM   1587 O  O   . ALA A 1 219 ? 34.550  21.639  5.359   1.00 36.53  ?  219 ALA A O   1 
ATOM   1588 C  CB  . ALA A 1 219 ? 33.227  24.555  5.300   1.00 35.84  ?  219 ALA A CB  1 
ATOM   1589 N  N   . LEU A 1 220 ? 32.862  21.584  3.855   1.00 29.05  ?  220 LEU A N   1 
ATOM   1590 C  CA  . LEU A 1 220 ? 32.576  20.176  4.114   1.00 34.39  ?  220 LEU A CA  1 
ATOM   1591 C  C   . LEU A 1 220 ? 33.377  19.239  3.198   1.00 33.46  ?  220 LEU A C   1 
ATOM   1592 O  O   . LEU A 1 220 ? 33.217  18.021  3.279   1.00 33.69  ?  220 LEU A O   1 
ATOM   1593 C  CB  . LEU A 1 220 ? 31.070  19.941  3.974   1.00 37.31  ?  220 LEU A CB  1 
ATOM   1594 C  CG  . LEU A 1 220 ? 30.158  20.710  4.945   1.00 41.27  ?  220 LEU A CG  1 
ATOM   1595 C  CD1 . LEU A 1 220 ? 28.718  20.588  4.509   1.00 39.56  ?  220 LEU A CD1 1 
ATOM   1596 C  CD2 . LEU A 1 220 ? 30.259  20.208  6.365   1.00 37.82  ?  220 LEU A CD2 1 
ATOM   1597 N  N   . ALA A 1 221 ? 34.254  19.793  2.353   1.00 32.86  ?  221 ALA A N   1 
ATOM   1598 C  CA  . ALA A 1 221 ? 34.867  19.027  1.270   1.00 39.80  ?  221 ALA A CA  1 
ATOM   1599 C  C   . ALA A 1 221 ? 35.754  17.879  1.757   1.00 41.09  ?  221 ALA A C   1 
ATOM   1600 O  O   . ALA A 1 221 ? 35.914  16.912  1.022   1.00 37.09  ?  221 ALA A O   1 
ATOM   1601 C  CB  . ALA A 1 221 ? 35.647  19.931  0.355   1.00 38.47  ?  221 ALA A CB  1 
ATOM   1602 N  N   . ARG A 1 222 ? 36.300  17.942  2.984   1.00 41.90  ?  222 ARG A N   1 
ATOM   1603 C  CA  . ARG A 1 222 ? 37.250  16.921  3.442   1.00 54.05  ?  222 ARG A CA  1 
ATOM   1604 C  C   . ARG A 1 222 ? 36.592  15.564  3.741   1.00 56.57  ?  222 ARG A C   1 
ATOM   1605 O  O   . ARG A 1 222 ? 37.293  14.576  3.921   1.00 63.05  ?  222 ARG A O   1 
ATOM   1606 C  CB  . ARG A 1 222 ? 38.055  17.351  4.678   1.00 58.11  ?  222 ARG A CB  1 
ATOM   1607 C  CG  . ARG A 1 222 ? 38.993  18.541  4.510   1.00 67.50  ?  222 ARG A CG  1 
ATOM   1608 C  CD  . ARG A 1 222 ? 39.274  19.258  5.844   1.00 82.86  ?  222 ARG A CD  1 
ATOM   1609 N  NE  . ARG A 1 222 ? 39.361  20.725  5.763   1.00 99.61  ?  222 ARG A NE  1 
ATOM   1610 C  CZ  . ARG A 1 222 ? 38.357  21.580  5.499   1.00 107.27 ?  222 ARG A CZ  1 
ATOM   1611 N  NH1 . ARG A 1 222 ? 37.151  21.135  5.188   1.00 114.79 1  222 ARG A NH1 1 
ATOM   1612 N  NH2 . ARG A 1 222 ? 38.562  22.888  5.532   1.00 98.66  ?  222 ARG A NH2 1 
ATOM   1613 N  N   . MET A 1 223 ? 35.257  15.461  3.753   1.00 59.99  ?  223 MET A N   1 
ATOM   1614 C  CA  . MET A 1 223 ? 34.594  14.233  4.176   1.00 59.57  ?  223 MET A CA  1 
ATOM   1615 C  C   . MET A 1 223 ? 34.583  13.175  3.045   1.00 60.43  ?  223 MET A C   1 
ATOM   1616 O  O   . MET A 1 223 ? 34.295  13.541  1.866   1.00 50.13  ?  223 MET A O   1 
ATOM   1617 C  CB  . MET A 1 223 ? 33.171  14.554  4.643   1.00 62.66  ?  223 MET A CB  1 
ATOM   1618 C  CG  . MET A 1 223 ? 33.110  15.599  5.742   1.00 66.97  ?  223 MET A CG  1 
ATOM   1619 S  SD  . MET A 1 223 ? 31.466  15.793  6.459   1.00 71.76  ?  223 MET A SD  1 
ATOM   1620 C  CE  . MET A 1 223 ? 31.364  14.279  7.417   1.00 74.30  ?  223 MET A CE  1 
ATOM   1621 N  N   . THR A 1 227 ? 23.592  21.605  -0.131  1.00 12.79  ?  227 THR A N   1 
ATOM   1622 C  CA  . THR A 1 227 ? 22.324  20.883  0.203   1.00 12.38  ?  227 THR A CA  1 
ATOM   1623 C  C   . THR A 1 227 ? 21.111  21.645  -0.299  1.00 13.03  ?  227 THR A C   1 
ATOM   1624 O  O   . THR A 1 227 ? 21.037  22.873  -0.158  1.00 12.77  ?  227 THR A O   1 
ATOM   1625 C  CB  . THR A 1 227 ? 22.226  20.752  1.718   1.00 12.54  ?  227 THR A CB  1 
ATOM   1626 O  OG1 . THR A 1 227 ? 23.387  20.050  2.151   1.00 14.40  ?  227 THR A OG1 1 
ATOM   1627 C  CG2 . THR A 1 227 ? 20.965  20.067  2.194   1.00 12.94  ?  227 THR A CG2 1 
ATOM   1628 N  N   . THR A 1 228 ? 20.119  20.897  -0.796  1.00 12.55  ?  228 THR A N   1 
ATOM   1629 C  CA  . THR A 1 228 ? 18.807  21.420  -1.118  1.00 12.42  ?  228 THR A CA  1 
ATOM   1630 C  C   . THR A 1 228 ? 17.782  20.550  -0.417  1.00 13.54  ?  228 THR A C   1 
ATOM   1631 O  O   . THR A 1 228 ? 17.796  19.350  -0.625  1.00 13.82  ?  228 THR A O   1 
ATOM   1632 C  CB  . THR A 1 228 ? 18.660  21.436  -2.638  1.00 14.41  ?  228 THR A CB  1 
ATOM   1633 O  OG1 . THR A 1 228 ? 19.685  22.291  -3.149  1.00 14.36  ?  228 THR A OG1 1 
ATOM   1634 C  CG2 . THR A 1 228 ? 17.371  22.035  -3.132  1.00 15.26  ?  228 THR A CG2 1 
ATOM   1635 N  N   . ILE A 1 229 ? 16.906  21.136  0.411   1.00 12.96  ?  229 ILE A N   1 
ATOM   1636 C  CA  . ILE A 1 229 ? 15.939  20.335  1.158   1.00 12.24  ?  229 ILE A CA  1 
ATOM   1637 C  C   . ILE A 1 229 ? 14.564  20.930  0.912   1.00 13.11  ?  229 ILE A C   1 
ATOM   1638 O  O   . ILE A 1 229 ? 14.420  22.141  0.686   1.00 13.72  ?  229 ILE A O   1 
ATOM   1639 C  CB  . ILE A 1 229 ? 16.238  20.239  2.663   1.00 12.67  ?  229 ILE A CB  1 
ATOM   1640 C  CG1 . ILE A 1 229 ? 16.346  21.621  3.312   1.00 12.61  ?  229 ILE A CG1 1 
ATOM   1641 C  CG2 . ILE A 1 229 ? 17.476  19.391  2.912   1.00 13.37  ?  229 ILE A CG2 1 
ATOM   1642 C  CD1 . ILE A 1 229 ? 16.629  21.625  4.803   1.00 14.24  ?  229 ILE A CD1 1 
ATOM   1643 N  N   . GLY A 1 230 ? 13.548  20.105  0.986   1.00 11.05  ?  230 GLY A N   1 
ATOM   1644 C  CA  . GLY A 1 230 ? 12.237  20.646  0.725   1.00 11.84  ?  230 GLY A CA  1 
ATOM   1645 C  C   . GLY A 1 230 ? 11.122  19.676  1.006   1.00 11.80  ?  230 GLY A C   1 
ATOM   1646 O  O   . GLY A 1 230 ? 11.371  18.519  1.341   1.00 12.99  ?  230 GLY A O   1 
ATOM   1647 N  N   . ILE A 1 231 ? 9.912   20.199  0.827   1.00 12.21  ?  231 ILE A N   1 
ATOM   1648 C  CA  . ILE A 1 231 ? 8.666   19.488  1.003   1.00 13.44  ?  231 ILE A CA  1 
ATOM   1649 C  C   . ILE A 1 231 ? 7.862   19.640  -0.286  1.00 13.65  ?  231 ILE A C   1 
ATOM   1650 O  O   . ILE A 1 231 ? 7.731   20.745  -0.785  1.00 15.70  ?  231 ILE A O   1 
ATOM   1651 C  CB  . ILE A 1 231 ? 7.844   20.040  2.193   1.00 15.98  ?  231 ILE A CB  1 
ATOM   1652 C  CG1 . ILE A 1 231 ? 8.629   20.030  3.509   1.00 16.96  ?  231 ILE A CG1 1 
ATOM   1653 C  CG2 . ILE A 1 231 ? 6.544   19.243  2.351   1.00 17.62  ?  231 ILE A CG2 1 
ATOM   1654 C  CD1 . ILE A 1 231 ? 8.025   20.922  4.570   1.00 19.02  ?  231 ILE A CD1 1 
ATOM   1655 N  N   . VAL A 1 232 ? 7.292   18.553  -0.780  1.00 12.54  ?  232 VAL A N   1 
ATOM   1656 C  CA  . VAL A 1 232 ? 6.311   18.584  -1.856  1.00 13.43  ?  232 VAL A CA  1 
ATOM   1657 C  C   . VAL A 1 232 ? 5.027   17.982  -1.284  1.00 12.94  ?  232 VAL A C   1 
ATOM   1658 O  O   . VAL A 1 232 ? 5.039   16.931  -0.638  1.00 13.96  ?  232 VAL A O   1 
ATOM   1659 C  CB  . VAL A 1 232 ? 6.786   17.869  -3.152  1.00 15.29  ?  232 VAL A CB  1 
ATOM   1660 C  CG1 . VAL A 1 232 ? 8.030   18.502  -3.735  1.00 19.30  ?  232 VAL A CG1 1 
ATOM   1661 C  CG2 . VAL A 1 232 ? 7.072   16.392  -2.972  1.00 17.92  ?  232 VAL A CG2 1 
ATOM   1662 N  N   . SER A 1 233 ? 3.896   18.623  -1.582  1.00 14.04  ?  233 SER A N   1 
ATOM   1663 C  CA  . SER A 1 233 ? 2.630   18.273  -0.970  1.00 13.92  ?  233 SER A CA  1 
ATOM   1664 C  C   . SER A 1 233 ? 1.528   18.304  -2.025  1.00 14.81  ?  233 SER A C   1 
ATOM   1665 O  O   . SER A 1 233 ? 1.562   19.164  -2.918  1.00 15.69  ?  233 SER A O   1 
ATOM   1666 C  CB  . SER A 1 233 ? 2.319   19.251  0.182   1.00 15.07  ?  233 SER A CB  1 
ATOM   1667 O  OG  . SER A 1 233 ? 3.203   19.103  1.281   1.00 15.46  ?  233 SER A OG  1 
ATOM   1668 N  N   . THR A 1 234 ? 0.567   17.377  -1.902  1.00 14.37  ?  234 THR A N   1 
ATOM   1669 C  CA  . THR A 1 234 ? -0.579  17.345  -2.808  1.00 14.24  ?  234 THR A CA  1 
ATOM   1670 C  C   . THR A 1 234 ? -1.864  17.196  -1.986  1.00 14.56  ?  234 THR A C   1 
ATOM   1671 O  O   . THR A 1 234 ? -1.875  16.690  -0.865  1.00 15.98  ?  234 THR A O   1 
ATOM   1672 C  CB  . THR A 1 234 ? -0.458  16.222  -3.828  1.00 14.45  ?  234 THR A CB  1 
ATOM   1673 O  OG1 . THR A 1 234 ? -1.529  16.248  -4.762  1.00 15.54  ?  234 THR A OG1 1 
ATOM   1674 C  CG2 . THR A 1 234 ? -0.443  14.842  -3.199  1.00 15.21  ?  234 THR A CG2 1 
ATOM   1675 N  N   . ASN A 1 235 ? -2.973  17.670  -2.585  1.00 16.22  ?  235 ASN A N   1 
ATOM   1676 C  CA  . ASN A 1 235 ? -4.293  17.496  -2.012  1.00 18.43  ?  235 ASN A CA  1 
ATOM   1677 C  C   . ASN A 1 235 ? -4.923  16.158  -2.434  1.00 19.11  ?  235 ASN A C   1 
ATOM   1678 O  O   . ASN A 1 235 ? -6.054  15.863  -2.002  1.00 19.63  ?  235 ASN A O   1 
ATOM   1679 C  CB  . ASN A 1 235 ? -5.194  18.679  -2.359  1.00 18.81  ?  235 ASN A CB  1 
ATOM   1680 C  CG  . ASN A 1 235 ? -5.331  18.924  -3.853  1.00 21.28  ?  235 ASN A CG  1 
ATOM   1681 O  OD1 . ASN A 1 235 ? -4.649  18.333  -4.707  1.00 18.86  ?  235 ASN A OD1 1 
ATOM   1682 N  ND2 . ASN A 1 235 ? -6.186  19.866  -4.210  1.00 25.18  ?  235 ASN A ND2 1 
ATOM   1683 N  N   . CYS A 1 236 ? -4.210  15.321  -3.227  1.00 17.85  ?  236 CYS A N   1 
ATOM   1684 C  CA  . CYS A 1 236 ? -4.630  13.947  -3.466  1.00 17.12  ?  236 CYS A CA  1 
ATOM   1685 C  C   . CYS A 1 236 ? -4.417  13.057  -2.260  1.00 17.45  ?  236 CYS A C   1 
ATOM   1686 O  O   . CYS A 1 236 ? -3.511  13.271  -1.458  1.00 18.06  ?  236 CYS A O   1 
ATOM   1687 C  CB  . CYS A 1 236 ? -3.922  13.321  -4.661  1.00 20.64  ?  236 CYS A CB  1 
ATOM   1688 S  SG  . CYS A 1 236 ? -4.385  14.115  -6.214  1.00 22.62  ?  236 CYS A SG  1 
ATOM   1689 N  N   . ARG A 1 237 ? -5.251  12.019  -2.156  1.00 18.49  ?  237 ARG A N   1 
ATOM   1690 C  CA  . ARG A 1 237 ? -5.010  10.930  -1.220  1.00 20.88  ?  237 ARG A CA  1 
ATOM   1691 C  C   . ARG A 1 237 ? -3.893  10.027  -1.752  1.00 20.28  ?  237 ARG A C   1 
ATOM   1692 O  O   . ARG A 1 237 ? -3.955  9.630   -2.898  1.00 20.44  ?  237 ARG A O   1 
ATOM   1693 C  CB  . ARG A 1 237 ? -6.270  10.070  -1.078  1.00 24.60  ?  237 ARG A CB  1 
ATOM   1694 C  CG  . ARG A 1 237 ? -6.237  9.063   0.068   1.00 32.15  ?  237 ARG A CG  1 
ATOM   1695 C  CD  . ARG A 1 237 ? -7.581  8.308   0.220   1.00 38.96  ?  237 ARG A CD  1 
ATOM   1696 N  NE  . ARG A 1 237 ? -7.876  7.402   -0.902  1.00 46.11  ?  237 ARG A NE  1 
ATOM   1697 C  CZ  . ARG A 1 237 ? -8.781  7.532   -1.886  1.00 53.98  ?  237 ARG A CZ  1 
ATOM   1698 N  NH1 . ARG A 1 237 ? -9.659  8.529   -1.931  1.00 59.75  1  237 ARG A NH1 1 
ATOM   1699 N  NH2 . ARG A 1 237 ? -8.794  6.627   -2.850  1.00 54.11  ?  237 ARG A NH2 1 
ATOM   1700 N  N   . LEU A 1 238 ? -2.915  9.663   -0.905  1.00 20.16  ?  238 LEU A N   1 
ATOM   1701 C  CA  . LEU A 1 238 ? -1.819  8.780   -1.301  1.00 18.13  ?  238 LEU A CA  1 
ATOM   1702 C  C   . LEU A 1 238 ? -1.731  7.642   -0.303  1.00 16.36  ?  238 LEU A C   1 
ATOM   1703 O  O   . LEU A 1 238 ? -2.088  7.823   0.847   1.00 17.97  ?  238 LEU A O   1 
ATOM   1704 C  CB  . LEU A 1 238 ? -0.492  9.546   -1.315  1.00 18.24  ?  238 LEU A CB  1 
ATOM   1705 C  CG  . LEU A 1 238 ? -0.365  10.781  -2.203  1.00 18.18  ?  238 LEU A CG  1 
ATOM   1706 C  CD1 . LEU A 1 238 ? 1.047   11.413  -2.052  1.00 19.73  ?  238 LEU A CD1 1 
ATOM   1707 C  CD2 . LEU A 1 238 ? -0.640  10.436  -3.644  1.00 21.54  ?  238 LEU A CD2 1 
ATOM   1708 N  N   . THR A 1 239 ? -1.203  6.495   -0.733  1.00 15.94  ?  239 THR A N   1 
ATOM   1709 C  CA  . THR A 1 239 ? -0.677  5.483   0.180   1.00 15.27  ?  239 THR A CA  1 
ATOM   1710 C  C   . THR A 1 239 ? 0.762   5.857   0.542   1.00 15.34  ?  239 THR A C   1 
ATOM   1711 O  O   . THR A 1 239 ? 1.346   6.718   -0.117  1.00 13.76  ?  239 THR A O   1 
ATOM   1712 C  CB  . THR A 1 239 ? -0.719  4.096   -0.480  1.00 16.13  ?  239 THR A CB  1 
ATOM   1713 O  OG1 . THR A 1 239 ? 0.194   4.061   -1.591  1.00 17.70  ?  239 THR A OG1 1 
ATOM   1714 C  CG2 . THR A 1 239 ? -2.132  3.710   -0.882  1.00 21.20  ?  239 THR A CG2 1 
ATOM   1715 N  N   . LYS A 1 240 ? 1.319   5.180   1.556   1.00 16.48  ?  240 LYS A N   1 
ATOM   1716 C  CA  . LYS A 1 240 ? 2.700   5.407   1.961   1.00 17.41  ?  240 LYS A CA  1 
ATOM   1717 C  C   . LYS A 1 240 ? 3.668   5.151   0.799   1.00 17.09  ?  240 LYS A C   1 
ATOM   1718 O  O   . LYS A 1 240 ? 4.600   5.923   0.615   1.00 17.06  ?  240 LYS A O   1 
ATOM   1719 C  CB  . LYS A 1 240 ? 3.153   4.610   3.195   1.00 21.84  ?  240 LYS A CB  1 
ATOM   1720 C  CG  . LYS A 1 240 ? 2.854   5.335   4.493   1.00 25.36  ?  240 LYS A CG  1 
ATOM   1721 C  CD  . LYS A 1 240 ? 3.499   4.726   5.730   1.00 27.33  ?  240 LYS A CD  1 
ATOM   1722 C  CE  . LYS A 1 240 ? 4.637   5.578   6.143   1.00 25.02  ?  240 LYS A CE  1 
ATOM   1723 N  NZ  . LYS A 1 240 ? 5.335   4.838   7.191   1.00 23.08  1  240 LYS A NZ  1 
ATOM   1724 N  N   . VAL A 1 241 ? 3.446   4.070   0.034   1.00 15.25  ?  241 VAL A N   1 
ATOM   1725 C  CA  . VAL A 1 241 ? 4.290   3.712   -1.101  1.00 16.57  ?  241 VAL A CA  1 
ATOM   1726 C  C   . VAL A 1 241 ? 4.255   4.830   -2.125  1.00 14.77  ?  241 VAL A C   1 
ATOM   1727 O  O   . VAL A 1 241 ? 5.272   5.240   -2.682  1.00 14.11  ?  241 VAL A O   1 
ATOM   1728 C  CB  . VAL A 1 241 ? 3.843   2.384   -1.760  1.00 20.86  ?  241 VAL A CB  1 
ATOM   1729 C  CG1 . VAL A 1 241 ? 4.309   2.281   -3.210  1.00 26.83  ?  241 VAL A CG1 1 
ATOM   1730 C  CG2 . VAL A 1 241 ? 4.353   1.216   -0.981  1.00 25.57  ?  241 VAL A CG2 1 
ATOM   1731 N  N   . GLU A 1 242 ? 3.074   5.370   -2.368  1.00 13.89  ?  242 GLU A N   1 
ATOM   1732 C  CA  . GLU A 1 242 ? 2.948   6.459   -3.334  1.00 14.19  ?  242 GLU A CA  1 
ATOM   1733 C  C   . GLU A 1 242 ? 3.636   7.758   -2.862  1.00 14.71  ?  242 GLU A C   1 
ATOM   1734 O  O   . GLU A 1 242 ? 4.175   8.493   -3.692  1.00 13.02  ?  242 GLU A O   1 
ATOM   1735 C  CB  . GLU A 1 242 ? 1.484   6.734   -3.657  1.00 15.37  ?  242 GLU A CB  1 
ATOM   1736 C  CG  . GLU A 1 242 ? 0.839   5.606   -4.446  1.00 18.39  ?  242 GLU A CG  1 
ATOM   1737 C  CD  . GLU A 1 242 ? -0.680  5.788   -4.630  1.00 20.52  ?  242 GLU A CD  1 
ATOM   1738 O  OE1 . GLU A 1 242 ? -1.350  6.266   -3.705  1.00 18.59  ?  242 GLU A OE1 1 
ATOM   1739 O  OE2 . GLU A 1 242 ? -1.175  5.512   -5.720  1.00 24.22  -1 242 GLU A OE2 1 
ATOM   1740 N  N   . ALA A 1 243 ? 3.510   8.110   -1.577  1.00 13.84  ?  243 ALA A N   1 
ATOM   1741 C  CA  . ALA A 1 243 ? 4.157   9.304   -1.081  1.00 14.23  ?  243 ALA A CA  1 
ATOM   1742 C  C   . ALA A 1 243 ? 5.683   9.166   -1.235  1.00 13.77  ?  243 ALA A C   1 
ATOM   1743 O  O   . ALA A 1 243 ? 6.345   10.118  -1.621  1.00 13.51  ?  243 ALA A O   1 
ATOM   1744 C  CB  . ALA A 1 243 ? 3.784   9.504   0.345   1.00 14.71  ?  243 ALA A CB  1 
ATOM   1745 N  N   . SER A 1 244 ? 6.235   7.967   -0.983  1.00 13.75  ?  244 SER A N   1 
ATOM   1746 C  CA  . SER A 1 244 ? 7.677   7.785   -1.147  1.00 17.76  ?  244 SER A CA  1 
ATOM   1747 C  C   . SER A 1 244 ? 8.094   7.854   -2.619  1.00 14.57  ?  244 SER A C   1 
ATOM   1748 O  O   . SER A 1 244 ? 9.135   8.416   -2.932  1.00 13.22  ?  244 SER A O   1 
ATOM   1749 C  CB  . SER A 1 244 ? 8.200   6.537   -0.445  1.00 21.41  ?  244 SER A CB  1 
ATOM   1750 O  OG  . SER A 1 244 ? 8.485   6.918   0.924   1.00 32.57  ?  244 SER A OG  1 
ATOM   1751 N  N   . ARG A 1 245 ? 7.263   7.344   -3.534  1.00 14.46  ?  245 ARG A N   1 
ATOM   1752 C  CA  . ARG A 1 245 ? 7.529   7.468   -4.958  1.00 15.60  ?  245 ARG A CA  1 
ATOM   1753 C  C   . ARG A 1 245 ? 7.476   8.935   -5.420  1.00 15.56  ?  245 ARG A C   1 
ATOM   1754 O  O   . ARG A 1 245 ? 8.293   9.368   -6.236  1.00 13.47  ?  245 ARG A O   1 
ATOM   1755 C  CB  . ARG A 1 245 ? 6.571   6.578   -5.755  1.00 17.42  ?  245 ARG A CB  1 
ATOM   1756 C  CG  . ARG A 1 245 ? 6.849   6.535   -7.251  1.00 21.72  ?  245 ARG A CG  1 
ATOM   1757 C  CD  . ARG A 1 245 ? 8.134   5.697   -7.498  1.00 24.41  ?  245 ARG A CD  1 
ATOM   1758 N  NE  . ARG A 1 245 ? 8.423   5.525   -8.928  1.00 24.89  ?  245 ARG A NE  1 
ATOM   1759 C  CZ  . ARG A 1 245 ? 9.547   4.958   -9.367  1.00 28.23  ?  245 ARG A CZ  1 
ATOM   1760 N  NH1 . ARG A 1 245 ? 10.492  4.539   -8.507  1.00 28.34  1  245 ARG A NH1 1 
ATOM   1761 N  NH2 . ARG A 1 245 ? 9.751   4.863   -10.659 1.00 22.92  ?  245 ARG A NH2 1 
ATOM   1762 N  N   . MET A 1 246 ? 6.532   9.713   -4.886  1.00 14.28  ?  246 MET A N   1 
ATOM   1763 C  CA  . MET A 1 246 ? 6.464   11.131  -5.200  1.00 15.43  ?  246 MET A CA  1 
ATOM   1764 C  C   . MET A 1 246 ? 7.735   11.864  -4.766  1.00 13.33  ?  246 MET A C   1 
ATOM   1765 O  O   . MET A 1 246 ? 8.244   12.683  -5.526  1.00 15.14  ?  246 MET A O   1 
ATOM   1766 C  CB  . MET A 1 246 ? 5.247   11.781  -4.534  1.00 16.35  ?  246 MET A CB  1 
ATOM   1767 C  CG  . MET A 1 246 ? 4.919   13.134  -5.107  1.00 21.01  ?  246 MET A CG  1 
ATOM   1768 S  SD  . MET A 1 246 ? 3.302   13.763  -4.563  1.00 25.04  ?  246 MET A SD  1 
ATOM   1769 C  CE  . MET A 1 246 ? 3.621   14.087  -2.851  1.00 28.19  ?  246 MET A CE  1 
ATOM   1770 N  N   . ALA A 1 247 ? 8.230   11.579  -3.559  1.00 12.78  ?  247 ALA A N   1 
ATOM   1771 C  CA  . ALA A 1 247 ? 9.476   12.178  -3.081  1.00 13.01  ?  247 ALA A CA  1 
ATOM   1772 C  C   . ALA A 1 247 ? 10.658  11.823  -3.997  1.00 13.76  ?  247 ALA A C   1 
ATOM   1773 O  O   . ALA A 1 247 ? 11.480  12.667  -4.292  1.00 15.34  ?  247 ALA A O   1 
ATOM   1774 C  CB  . ALA A 1 247 ? 9.709   11.711  -1.655  1.00 12.32  ?  247 ALA A CB  1 
ATOM   1775 N  N   . THR A 1 248 ? 10.743  10.554  -4.442  1.00 13.70  ?  248 THR A N   1 
ATOM   1776 C  CA  . THR A 1 248 ? 11.803  10.098  -5.322  1.00 13.51  ?  248 THR A CA  1 
ATOM   1777 C  C   . THR A 1 248 ? 11.750  10.847  -6.650  1.00 13.78  ?  248 THR A C   1 
ATOM   1778 O  O   . THR A 1 248 ? 12.783  11.300  -7.146  1.00 13.02  ?  248 THR A O   1 
ATOM   1779 C  CB  . THR A 1 248 ? 11.727  8.576   -5.500  1.00 14.91  ?  248 THR A CB  1 
ATOM   1780 O  OG1 . THR A 1 248 ? 11.983  8.023   -4.204  1.00 12.70  ?  248 THR A OG1 1 
ATOM   1781 C  CG2 . THR A 1 248 ? 12.663  8.023   -6.564  1.00 15.85  ?  248 THR A CG2 1 
ATOM   1782 N  N   . LEU A 1 249 ? 10.569  10.970  -7.258  1.00 12.92  ?  249 LEU A N   1 
ATOM   1783 C  CA  . LEU A 1 249 ? 10.438  11.630  -8.542  1.00 13.03  ?  249 LEU A CA  1 
ATOM   1784 C  C   . LEU A 1 249 ? 10.684  13.134  -8.464  1.00 14.11  ?  249 LEU A C   1 
ATOM   1785 O  O   . LEU A 1 249 ? 11.185  13.704  -9.435  1.00 12.59  ?  249 LEU A O   1 
ATOM   1786 C  CB  . LEU A 1 249 ? 9.058   11.331  -9.138  1.00 15.18  ?  249 LEU A CB  1 
ATOM   1787 C  CG  . LEU A 1 249 ? 8.797   9.865   -9.503  1.00 20.45  ?  249 LEU A CG  1 
ATOM   1788 C  CD1 . LEU A 1 249 ? 7.349   9.576   -10.006 1.00 19.99  ?  249 LEU A CD1 1 
ATOM   1789 C  CD2 . LEU A 1 249 ? 9.761   9.445   -10.528 1.00 22.87  ?  249 LEU A CD2 1 
ATOM   1790 N  N   . ALA A 1 250 ? 10.403  13.760  -7.315  1.00 12.01  ?  250 ALA A N   1 
ATOM   1791 C  CA  . ALA A 1 250 ? 10.629  15.184  -7.145  1.00 13.35  ?  250 ALA A CA  1 
ATOM   1792 C  C   . ALA A 1 250 ? 12.105  15.550  -7.316  1.00 13.15  ?  250 ALA A C   1 
ATOM   1793 O  O   . ALA A 1 250 ? 12.424  16.647  -7.757  1.00 12.97  ?  250 ALA A O   1 
ATOM   1794 C  CB  . ALA A 1 250 ? 10.113  15.633  -5.779  1.00 14.17  ?  250 ALA A CB  1 
ATOM   1795 N  N   . HIS A 1 251 ? 13.023  14.652  -6.944  1.00 12.70  ?  251 HIS A N   1 
ATOM   1796 C  CA  . HIS A 1 251 ? 14.446  14.933  -7.122  1.00 13.00  ?  251 HIS A CA  1 
ATOM   1797 C  C   . HIS A 1 251 ? 14.813  15.196  -8.586  1.00 13.21  ?  251 HIS A C   1 
ATOM   1798 O  O   . HIS A 1 251 ? 15.836  15.810  -8.846  1.00 13.66  ?  251 HIS A O   1 
ATOM   1799 C  CB  . HIS A 1 251 ? 15.312  13.802  -6.576  1.00 12.58  ?  251 HIS A CB  1 
ATOM   1800 C  CG  . HIS A 1 251 ? 15.509  13.869  -5.104  1.00 13.92  ?  251 HIS A CG  1 
ATOM   1801 N  ND1 . HIS A 1 251 ? 16.461  14.673  -4.507  1.00 13.50  ?  251 HIS A ND1 1 
ATOM   1802 C  CD2 . HIS A 1 251 ? 14.892  13.194  -4.105  1.00 13.18  ?  251 HIS A CD2 1 
ATOM   1803 C  CE1 . HIS A 1 251 ? 16.433  14.453  -3.197  1.00 14.97  ?  251 HIS A CE1 1 
ATOM   1804 N  NE2 . HIS A 1 251 ? 15.466  13.580  -2.935  1.00 14.58  ?  251 HIS A NE2 1 
ATOM   1805 N  N   . ASN A 1 252 ? 14.013  14.692  -9.538  1.00 12.61  ?  252 ASN A N   1 
ATOM   1806 C  CA  . ASN A 1 252 ? 14.276  14.938  -10.944 1.00 14.24  ?  252 ASN A CA  1 
ATOM   1807 C  C   . ASN A 1 252 ? 14.194  16.441  -11.247 1.00 13.81  ?  252 ASN A C   1 
ATOM   1808 O  O   . ASN A 1 252 ? 14.893  16.927  -12.119 1.00 13.00  ?  252 ASN A O   1 
ATOM   1809 C  CB  . ASN A 1 252 ? 13.344  14.116  -11.802 1.00 14.25  ?  252 ASN A CB  1 
ATOM   1810 C  CG  . ASN A 1 252 ? 13.633  12.641  -11.724 1.00 13.53  ?  252 ASN A CG  1 
ATOM   1811 O  OD1 . ASN A 1 252 ? 14.744  12.209  -11.422 1.00 13.07  ?  252 ASN A OD1 1 
ATOM   1812 N  ND2 . ASN A 1 252 ? 12.673  11.832  -12.092 1.00 15.58  ?  252 ASN A ND2 1 
ATOM   1813 N  N   . GLY A 1 253 ? 13.339  17.145  -10.503 1.00 12.92  ?  253 GLY A N   1 
ATOM   1814 C  CA  . GLY A 1 253 ? 13.216  18.599  -10.622 1.00 14.57  ?  253 GLY A CA  1 
ATOM   1815 C  C   . GLY A 1 253 ? 14.449  19.338  -10.118 1.00 14.84  ?  253 GLY A C   1 
ATOM   1816 O  O   . GLY A 1 253 ? 14.899  20.310  -10.741 1.00 15.05  ?  253 GLY A O   1 
ATOM   1817 N  N   . LEU A 1 254 ? 15.028  18.837  -9.013  1.00 14.67  ?  254 LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 254 ? 16.267  19.387  -8.504  1.00 16.05  ?  254 LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 254 ? 17.372  19.208  -9.539  1.00 15.59  ?  254 LEU A C   1 
ATOM   1820 O  O   . LEU A 1 254 ? 18.113  20.157  -9.779  1.00 15.94  ?  254 LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 254 ? 16.660  18.803  -7.153  1.00 17.15  ?  254 LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 254 ? 15.634  18.961  -6.029  1.00 18.72  ?  254 LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 254 ? 16.330  18.546  -4.730  1.00 18.22  ?  254 LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 254 ? 15.028  20.316  -5.926  1.00 21.59  ?  254 LEU A CD2 1 
ATOM   1825 N  N   . ALA A 1 255 ? 17.444  18.022  -10.182 1.00 14.30  ?  255 ALA A N   1 
ATOM   1826 C  CA  . ALA A 1 255 ? 18.452  17.739  -11.199 1.00 14.99  ?  255 ALA A CA  1 
ATOM   1827 C  C   . ALA A 1 255 ? 18.336  18.668  -12.417 1.00 16.81  ?  255 ALA A C   1 
ATOM   1828 O  O   . ALA A 1 255 ? 19.344  19.001  -13.033 1.00 17.09  ?  255 ALA A O   1 
ATOM   1829 C  CB  . ALA A 1 255 ? 18.382  16.296  -11.643 1.00 17.78  ?  255 ALA A CB  1 
ATOM   1830 N  N   . ARG A 1 256 ? 17.126  19.101  -12.771 1.00 15.15  ?  256 ARG A N   1 
ATOM   1831 C  CA  . ARG A 1 256 ? 16.930  20.003  -13.894 1.00 17.40  ?  256 ARG A CA  1 
ATOM   1832 C  C   . ARG A 1 256 ? 17.403  21.422  -13.581 1.00 18.57  ?  256 ARG A C   1 
ATOM   1833 O  O   . ARG A 1 256 ? 17.850  22.113  -14.490 1.00 21.97  ?  256 ARG A O   1 
ATOM   1834 C  CB  . ARG A 1 256 ? 15.470  19.962  -14.373 1.00 20.25  ?  256 ARG A CB  1 
ATOM   1835 C  CG  . ARG A 1 256 ? 15.076  18.633  -14.992 1.00 23.05  ?  256 ARG A CG  1 
ATOM   1836 C  CD  . ARG A 1 256 ? 13.535  18.491  -15.234 1.00 27.59  ?  256 ARG A CD  1 
ATOM   1837 N  NE  . ARG A 1 256 ? 13.299  17.141  -15.789 1.00 33.78  ?  256 ARG A NE  1 
ATOM   1838 C  CZ  . ARG A 1 256 ? 12.316  16.221  -15.588 1.00 36.90  ?  256 ARG A CZ  1 
ATOM   1839 N  NH1 . ARG A 1 256 ? 12.274  15.114  -16.383 1.00 28.14  1  256 ARG A NH1 1 
ATOM   1840 N  NH2 . ARG A 1 256 ? 11.397  16.416  -14.633 1.00 35.37  ?  256 ARG A NH2 1 
ATOM   1841 N  N   . ALA A 1 257 ? 17.333  21.854  -12.315 1.00 17.40  ?  257 ALA A N   1 
ATOM   1842 C  CA  . ALA A 1 257 ? 17.687  23.208  -11.933 1.00 17.55  ?  257 ALA A CA  1 
ATOM   1843 C  C   . ALA A 1 257 ? 19.142  23.327  -11.474 1.00 16.83  ?  257 ALA A C   1 
ATOM   1844 O  O   . ALA A 1 257 ? 19.742  24.377  -11.670 1.00 17.39  ?  257 ALA A O   1 
ATOM   1845 C  CB  . ALA A 1 257 ? 16.761  23.672  -10.851 1.00 19.35  ?  257 ALA A CB  1 
ATOM   1846 N  N   . ILE A 1 258 ? 19.692  22.298  -10.832 1.00 16.27  ?  258 ILE A N   1 
ATOM   1847 C  CA  . ILE A 1 258 ? 20.924  22.462  -10.074 1.00 14.82  ?  258 ILE A CA  1 
ATOM   1848 C  C   . ILE A 1 258 ? 21.983  21.523  -10.630 1.00 14.92  ?  258 ILE A C   1 
ATOM   1849 O  O   . ILE A 1 258 ? 21.723  20.325  -10.792 1.00 14.76  ?  258 ILE A O   1 
ATOM   1850 C  CB  . ILE A 1 258 ? 20.652  22.193  -8.577  1.00 16.63  ?  258 ILE A CB  1 
ATOM   1851 C  CG1 . ILE A 1 258 ? 19.631  23.152  -7.972  1.00 18.91  ?  258 ILE A CG1 1 
ATOM   1852 C  CG2 . ILE A 1 258 ? 21.947  22.192  -7.757  1.00 17.92  ?  258 ILE A CG2 1 
ATOM   1853 C  CD1 . ILE A 1 258 ? 19.181  22.764  -6.579  1.00 21.86  ?  258 ILE A CD1 1 
ATOM   1854 N  N   . CYS A 1 259 ? 23.230  22.007  -10.803 1.00 15.30  ?  259 CYS A N   1 
ATOM   1855 C  CA  . CYS A 1 259 ? 24.268  21.137  -11.340 1.00 15.60  ?  259 CYS A CA  1 
ATOM   1856 C  C   . CYS A 1 259 ? 25.641  21.604  -10.862 1.00 16.94  ?  259 CYS A C   1 
ATOM   1857 O  O   . CYS A 1 259 ? 25.942  22.792  -10.940 1.00 18.37  ?  259 CYS A O   1 
ATOM   1858 C  CB  . CYS A 1 259 ? 24.248  21.054  -12.867 1.00 19.26  ?  259 CYS A CB  1 
ATOM   1859 S  SG  . CYS A 1 259 ? 25.563  19.986  -13.538 1.00 23.92  ?  259 CYS A SG  1 
ATOM   1860 N  N   . PRO A 1 260 ? 26.486  20.744  -10.270 1.00 15.16  ?  260 PRO A N   1 
ATOM   1861 C  CA  . PRO A 1 260 ? 26.144  19.383  -9.868  1.00 16.18  ?  260 PRO A CA  1 
ATOM   1862 C  C   . PRO A 1 260 ? 25.128  19.317  -8.730  1.00 15.50  ?  260 PRO A C   1 
ATOM   1863 O  O   . PRO A 1 260 ? 24.981  20.278  -7.969  1.00 12.86  ?  260 PRO A O   1 
ATOM   1864 C  CB  . PRO A 1 260 ? 27.446  18.792  -9.317  1.00 16.34  ?  260 PRO A CB  1 
ATOM   1865 C  CG  . PRO A 1 260 ? 28.496  19.821  -9.545  1.00 18.34  ?  260 PRO A CG  1 
ATOM   1866 C  CD  . PRO A 1 260 ? 27.873  21.096  -9.972  1.00 17.69  ?  260 PRO A CD  1 
ATOM   1867 N  N   . ILE A 1 261 ? 24.527  18.127  -8.556  1.00 15.91  ?  261 ILE A N   1 
ATOM   1868 C  CA  . ILE A 1 261 ? 23.513  17.900  -7.515  1.00 14.06  ?  261 ILE A CA  1 
ATOM   1869 C  C   . ILE A 1 261 ? 23.835  16.559  -6.847  1.00 13.84  ?  261 ILE A C   1 
ATOM   1870 O  O   . ILE A 1 261 ? 24.535  15.757  -7.437  1.00 14.08  ?  261 ILE A O   1 
ATOM   1871 C  CB  . ILE A 1 261 ? 22.111  17.920  -8.168  1.00 15.82  ?  261 ILE A CB  1 
ATOM   1872 C  CG1 . ILE A 1 261 ? 20.965  17.838  -7.167  1.00 17.01  ?  261 ILE A CG1 1 
ATOM   1873 C  CG2 . ILE A 1 261 ? 21.980  16.816  -9.214  1.00 16.55  ?  261 ILE A CG2 1 
ATOM   1874 C  CD1 . ILE A 1 261 ? 20.877  18.992  -6.221  1.00 17.81  ?  261 ILE A CD1 1 
ATOM   1875 N  N   . HIS A 1 262 ? 23.345  16.319  -5.627  1.00 12.00  ?  262 HIS A N   1 
ATOM   1876 C  CA  . HIS A 1 262 ? 23.500  15.054  -4.920  1.00 13.23  ?  262 HIS A CA  1 
ATOM   1877 C  C   . HIS A 1 262 ? 24.985  14.730  -4.736  1.00 14.83  ?  262 HIS A C   1 
ATOM   1878 O  O   . HIS A 1 262 ? 25.377  13.563  -4.822  1.00 15.71  ?  262 HIS A O   1 
ATOM   1879 C  CB  . HIS A 1 262 ? 22.804  13.925  -5.715  1.00 15.29  ?  262 HIS A CB  1 
ATOM   1880 C  CG  . HIS A 1 262 ? 21.342  14.136  -6.005  1.00 14.60  ?  262 HIS A CG  1 
ATOM   1881 N  ND1 . HIS A 1 262 ? 20.685  13.788  -7.185  1.00 15.03  ?  262 HIS A ND1 1 
ATOM   1882 C  CD2 . HIS A 1 262 ? 20.407  14.688  -5.214  1.00 14.57  ?  262 HIS A CD2 1 
ATOM   1883 C  CE1 . HIS A 1 262 ? 19.390  14.143  -7.083  1.00 14.23  ?  262 HIS A CE1 1 
ATOM   1884 N  NE2 . HIS A 1 262 ? 19.204  14.673  -5.891  1.00 14.23  ?  262 HIS A NE2 1 
ATOM   1885 N  N   . THR A 1 263 ? 25.817  15.764  -4.492  1.00 13.56  ?  263 THR A N   1 
ATOM   1886 C  CA  . THR A 1 263 ? 27.259  15.587  -4.366  1.00 14.56  ?  263 THR A CA  1 
ATOM   1887 C  C   . THR A 1 263 ? 27.589  15.051  -2.962  1.00 16.47  ?  263 THR A C   1 
ATOM   1888 O  O   . THR A 1 263 ? 26.732  14.968  -2.083  1.00 14.05  ?  263 THR A O   1 
ATOM   1889 C  CB  . THR A 1 263 ? 28.028  16.888  -4.642  1.00 15.45  ?  263 THR A CB  1 
ATOM   1890 O  OG1 . THR A 1 263 ? 27.807  17.763  -3.534  1.00 14.83  ?  263 THR A OG1 1 
ATOM   1891 C  CG2 . THR A 1 263 ? 27.660  17.532  -5.967  1.00 16.29  ?  263 THR A CG2 1 
ATOM   1892 N  N   . ASN A 1 264 ? 28.881  14.820  -2.704  1.00 16.64  ?  264 ASN A N   1 
ATOM   1893 C  CA  . ASN A 1 264 ? 29.326  14.351  -1.401  1.00 17.66  ?  264 ASN A CA  1 
ATOM   1894 C  C   . ASN A 1 264 ? 29.223  15.442  -0.339  1.00 17.12  ?  264 ASN A C   1 
ATOM   1895 O  O   . ASN A 1 264 ? 29.406  15.124  0.823   1.00 18.31  ?  264 ASN A O   1 
ATOM   1896 C  CB  . ASN A 1 264 ? 30.769  13.847  -1.430  1.00 19.23  ?  264 ASN A CB  1 
ATOM   1897 C  CG  . ASN A 1 264 ? 30.883  12.583  -2.247  1.00 24.15  ?  264 ASN A CG  1 
ATOM   1898 O  OD1 . ASN A 1 264 ? 29.889  11.888  -2.502  1.00 28.97  ?  264 ASN A OD1 1 
ATOM   1899 N  ND2 . ASN A 1 264 ? 32.085  12.259  -2.663  1.00 29.51  ?  264 ASN A ND2 1 
ATOM   1900 N  N   . VAL A 1 265 ? 29.008  16.710  -0.695  1.00 14.66  ?  265 VAL A N   1 
ATOM   1901 C  CA  . VAL A 1 265 ? 28.814  17.723  0.326   1.00 16.32  ?  265 VAL A CA  1 
ATOM   1902 C  C   . VAL A 1 265 ? 27.356  18.119  0.442   1.00 16.13  ?  265 VAL A C   1 
ATOM   1903 O  O   . VAL A 1 265 ? 27.022  19.008  1.226   1.00 17.83  ?  265 VAL A O   1 
ATOM   1904 C  CB  . VAL A 1 265 ? 29.698  18.976  0.135   1.00 19.13  ?  265 VAL A CB  1 
ATOM   1905 C  CG1 . VAL A 1 265 ? 31.167  18.584  0.261   1.00 20.25  ?  265 VAL A CG1 1 
ATOM   1906 C  CG2 . VAL A 1 265 ? 29.416  19.682  -1.178  1.00 19.11  ?  265 VAL A CG2 1 
ATOM   1907 N  N   . ASP A 1 266 ? 26.464  17.435  -0.286  1.00 14.92  ?  266 ASP A N   1 
ATOM   1908 C  CA  . ASP A 1 266 ? 25.054  17.814  -0.263  1.00 12.70  ?  266 ASP A CA  1 
ATOM   1909 C  C   . ASP A 1 266 ? 24.256  16.837  0.588   1.00 14.33  ?  266 ASP A C   1 
ATOM   1910 O  O   . ASP A 1 266 ? 24.432  15.625  0.463   1.00 14.03  ?  266 ASP A O   1 
ATOM   1911 C  CB  . ASP A 1 266 ? 24.486  17.864  -1.668  1.00 12.41  ?  266 ASP A CB  1 
ATOM   1912 C  CG  . ASP A 1 266 ? 24.973  19.031  -2.519  1.00 12.40  ?  266 ASP A CG  1 
ATOM   1913 O  OD1 . ASP A 1 266 ? 24.955  20.181  -2.017  1.00 12.42  ?  266 ASP A OD1 1 
ATOM   1914 O  OD2 . ASP A 1 266 ? 25.379  18.761  -3.665  1.00 15.09  -1 266 ASP A OD2 1 
ATOM   1915 N  N   . GLY A 1 267 ? 23.328  17.373  1.394   1.00 13.20  ?  267 GLY A N   1 
ATOM   1916 C  CA  . GLY A 1 267 ? 22.414  16.562  2.188   1.00 13.46  ?  267 GLY A CA  1 
ATOM   1917 C  C   . GLY A 1 267 ? 20.980  16.559  1.633   1.00 12.50  ?  267 GLY A C   1 
ATOM   1918 O  O   . GLY A 1 267 ? 20.035  16.431  2.402   1.00 13.06  ?  267 GLY A O   1 
ATOM   1919 N  N   . ASP A 1 268 ? 20.859  16.554  0.304   1.00 11.74  ?  268 ASP A N   1 
ATOM   1920 C  CA  . ASP A 1 268 ? 19.609  16.771  -0.395  1.00 11.91  ?  268 ASP A CA  1 
ATOM   1921 C  C   . ASP A 1 268 ? 18.553  15.767  0.039   1.00 11.93  ?  268 ASP A C   1 
ATOM   1922 O  O   . ASP A 1 268 ? 18.779  14.569  -0.064  1.00 11.06  ?  268 ASP A O   1 
ATOM   1923 C  CB  . ASP A 1 268 ? 19.852  16.643  -1.884  1.00 13.11  ?  268 ASP A CB  1 
ATOM   1924 C  CG  . ASP A 1 268 ? 20.931  17.547  -2.456  1.00 12.55  ?  268 ASP A CG  1 
ATOM   1925 O  OD1 . ASP A 1 268 ? 21.186  18.606  -1.865  1.00 12.38  ?  268 ASP A OD1 1 
ATOM   1926 O  OD2 . ASP A 1 268 ? 21.539  17.124  -3.436  1.00 13.82  -1 268 ASP A OD2 1 
ATOM   1927 N  N   . THR A 1 269 ? 17.397  16.288  0.469   1.00 11.94  ?  269 THR A N   1 
ATOM   1928 C  CA  . THR A 1 269 ? 16.324  15.503  1.061   1.00 12.57  ?  269 THR A CA  1 
ATOM   1929 C  C   . THR A 1 269 ? 15.008  16.120  0.615   1.00 12.23  ?  269 THR A C   1 
ATOM   1930 O  O   . THR A 1 269 ? 14.877  17.357  0.671   1.00 11.69  ?  269 THR A O   1 
ATOM   1931 C  CB  . THR A 1 269 ? 16.382  15.500  2.584   1.00 13.75  ?  269 THR A CB  1 
ATOM   1932 O  OG1 . THR A 1 269 ? 17.607  14.957  3.035   1.00 13.19  ?  269 THR A OG1 1 
ATOM   1933 C  CG2 . THR A 1 269 ? 15.217  14.741  3.202   1.00 14.31  ?  269 THR A CG2 1 
ATOM   1934 N  N   . ILE A 1 270 ? 14.090  15.286  0.110   1.00 11.74  ?  270 ILE A N   1 
ATOM   1935 C  CA  . ILE A 1 270 ? 12.734  15.720  -0.185  1.00 13.31  ?  270 ILE A CA  1 
ATOM   1936 C  C   . ILE A 1 270 ? 11.769  14.908  0.668   1.00 12.76  ?  270 ILE A C   1 
ATOM   1937 O  O   . ILE A 1 270 ? 11.777  13.677  0.631   1.00 11.29  ?  270 ILE A O   1 
ATOM   1938 C  CB  . ILE A 1 270 ? 12.349  15.601  -1.666  1.00 13.94  ?  270 ILE A CB  1 
ATOM   1939 C  CG1 . ILE A 1 270 ? 13.200  16.485  -2.561  1.00 16.49  ?  270 ILE A CG1 1 
ATOM   1940 C  CG2 . ILE A 1 270 ? 10.858  15.887  -1.898  1.00 14.10  ?  270 ILE A CG2 1 
ATOM   1941 C  CD1 . ILE A 1 270 ? 12.899  17.941  -2.428  1.00 20.55  ?  270 ILE A CD1 1 
ATOM   1942 N  N   . PHE A 1 271 ? 10.892  15.629  1.378   1.00 10.05  ?  271 PHE A N   1 
ATOM   1943 C  CA  . PHE A 1 271 ? 9.750   15.042  2.057   1.00 10.68  ?  271 PHE A CA  1 
ATOM   1944 C  C   . PHE A 1 271 ? 8.531   15.220  1.160   1.00 11.60  ?  271 PHE A C   1 
ATOM   1945 O  O   . PHE A 1 271 ? 8.402   16.263  0.500   1.00 14.70  ?  271 PHE A O   1 
ATOM   1946 C  CB  . PHE A 1 271 ? 9.472   15.748  3.397   1.00 11.01  ?  271 PHE A CB  1 
ATOM   1947 C  CG  . PHE A 1 271 ? 10.604  15.710  4.411   1.00 11.00  ?  271 PHE A CG  1 
ATOM   1948 C  CD1 . PHE A 1 271 ? 10.709  14.667  5.321   1.00 11.56  ?  271 PHE A CD1 1 
ATOM   1949 C  CD2 . PHE A 1 271 ? 11.526  16.740  4.469   1.00 12.66  ?  271 PHE A CD2 1 
ATOM   1950 C  CE1 . PHE A 1 271 ? 11.750  14.649  6.245   1.00 12.34  ?  271 PHE A CE1 1 
ATOM   1951 C  CE2 . PHE A 1 271 ? 12.533  16.744  5.421   1.00 12.70  ?  271 PHE A CE2 1 
ATOM   1952 C  CZ  . PHE A 1 271 ? 12.634  15.694  6.308   1.00 13.05  ?  271 PHE A CZ  1 
ATOM   1953 N  N   . ALA A 1 272 ? 7.622   14.240  1.140   1.00 12.18  ?  272 ALA A N   1 
ATOM   1954 C  CA  . ALA A 1 272 ? 6.384   14.337  0.372   1.00 12.40  ?  272 ALA A CA  1 
ATOM   1955 C  C   . ALA A 1 272 ? 5.188   14.041  1.276   1.00 13.47  ?  272 ALA A C   1 
ATOM   1956 O  O   . ALA A 1 272 ? 5.262   13.178  2.171   1.00 14.06  ?  272 ALA A O   1 
ATOM   1957 C  CB  . ALA A 1 272 ? 6.390   13.392  -0.804  1.00 13.57  ?  272 ALA A CB  1 
ATOM   1958 N  N   . THR A 1 273 ? 4.069   14.734  1.017   1.00 12.61  ?  273 THR A N   1 
ATOM   1959 C  CA  . THR A 1 273 ? 2.839   14.456  1.741   1.00 13.67  ?  273 THR A CA  1 
ATOM   1960 C  C   . THR A 1 273 ? 1.655   14.388  0.780   1.00 12.81  ?  273 THR A C   1 
ATOM   1961 O  O   . THR A 1 273 ? 1.600   15.105  -0.218  1.00 14.83  ?  273 THR A O   1 
ATOM   1962 C  CB  . THR A 1 273 ? 2.536   15.471  2.859   1.00 14.89  ?  273 THR A CB  1 
ATOM   1963 O  OG1 . THR A 1 273 ? 2.240   16.731  2.282   1.00 14.65  ?  273 THR A OG1 1 
ATOM   1964 C  CG2 . THR A 1 273 ? 3.645   15.592  3.893   1.00 15.82  ?  273 THR A CG2 1 
ATOM   1965 N  N   . GLY A 1 274 ? 0.720   13.492  1.103   1.00 13.31  ?  274 GLY A N   1 
ATOM   1966 C  CA  . GLY A 1 274 ? -0.644  13.556  0.581   1.00 13.00  ?  274 GLY A CA  1 
ATOM   1967 C  C   . GLY A 1 274 ? -1.622  13.550  1.749   1.00 15.88  ?  274 GLY A C   1 
ATOM   1968 O  O   . GLY A 1 274 ? -1.206  13.434  2.892   1.00 14.78  ?  274 GLY A O   1 
ATOM   1969 N  N   . LEU A 1 275 ? -2.907  13.761  1.467   1.00 17.92  ?  275 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 275 ? -3.935  13.824  2.517   1.00 20.07  ?  275 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 275 ? -4.444  12.415  2.789   1.00 21.55  ?  275 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 275 ? -4.496  11.591  1.880   1.00 27.43  ?  275 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 275 ? -5.067  14.748  2.057   1.00 22.41  ?  275 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 275 ? -4.740  16.236  2.006   1.00 25.21  ?  275 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 275 ? -5.943  17.050  1.477   1.00 28.03  ?  275 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 275 ? -4.351  16.719  3.385   1.00 29.36  ?  275 LEU A CD2 1 
ATOM   1977 N  N   . GLN A 1 276 ? -4.700  12.085  4.058   1.00 20.19  ?  276 GLN A N   1 
ATOM   1978 C  CA  . GLN A 1 276 ? -5.279  10.801  4.399   1.00 21.25  ?  276 GLN A CA  1 
ATOM   1979 C  C   . GLN A 1 276 ? -6.735  10.736  3.938   1.00 23.55  ?  276 GLN A C   1 
ATOM   1980 O  O   . GLN A 1 276 ? -7.170  9.686   3.486   1.00 26.31  ?  276 GLN A O   1 
ATOM   1981 C  CB  . GLN A 1 276 ? -5.249  10.552  5.900   1.00 23.88  ?  276 GLN A CB  1 
ATOM   1982 C  CG  . GLN A 1 276 ? -3.854  10.289  6.440   1.00 26.32  ?  276 GLN A CG  1 
ATOM   1983 C  CD  . GLN A 1 276 ? -3.848  9.866   7.887   1.00 33.58  ?  276 GLN A CD  1 
ATOM   1984 O  OE1 . GLN A 1 276 ? -4.870  9.439   8.445   1.00 32.76  ?  276 GLN A OE1 1 
ATOM   1985 N  NE2 . GLN A 1 276 ? -2.682  9.988   8.502   1.00 30.50  ?  276 GLN A NE2 1 
ATOM   1986 N  N   . LYS A 1 277 ? -7.445  11.855  4.060   1.00 22.43  ?  277 LYS A N   1 
ATOM   1987 C  CA  . LYS A 1 277 ? -8.861  11.939  3.724   1.00 33.33  ?  277 LYS A CA  1 
ATOM   1988 C  C   . LYS A 1 277 ? -9.016  12.914  2.564   1.00 30.75  ?  277 LYS A C   1 
ATOM   1989 O  O   . LYS A 1 277 ? -8.899  14.123  2.719   1.00 38.55  ?  277 LYS A O   1 
ATOM   1990 C  CB  . LYS A 1 277 ? -9.639  12.449  4.945   1.00 43.33  ?  277 LYS A CB  1 
ATOM   1991 C  CG  . LYS A 1 277 ? -10.191 11.395  5.901   1.00 57.96  ?  277 LYS A CG  1 
ATOM   1992 C  CD  . LYS A 1 277 ? -9.197  10.480  6.617   1.00 72.43  ?  277 LYS A CD  1 
ATOM   1993 C  CE  . LYS A 1 277 ? -9.783  9.657   7.758   1.00 75.44  ?  277 LYS A CE  1 
ATOM   1994 N  NZ  . LYS A 1 277 ? -11.055 8.979   7.456   1.00 72.28  1  277 LYS A NZ  1 
ATOM   1995 N  N   . SER A 1 278 ? -9.205  12.388  1.376   1.00 29.40  ?  278 SER A N   1 
ATOM   1996 C  CA  . SER A 1 278 ? -9.431  13.241  0.229   1.00 29.05  ?  278 SER A CA  1 
ATOM   1997 C  C   . SER A 1 278 ? -10.105 12.353  -0.785  1.00 29.19  ?  278 SER A C   1 
ATOM   1998 O  O   . SER A 1 278 ? -9.834  11.161  -0.791  1.00 32.92  ?  278 SER A O   1 
ATOM   1999 C  CB  . SER A 1 278 ? -8.129  13.828  -0.321  1.00 28.00  ?  278 SER A CB  1 
ATOM   2000 O  OG  . SER A 1 278 ? -8.290  14.406  -1.610  1.00 23.88  ?  278 SER A OG  1 
ATOM   2001 N  N   . ASP A 1 279 ? -10.945 12.959  -1.612  1.00 30.11  ?  279 ASP A N   1 
ATOM   2002 C  CA  . ASP A 1 279 ? -11.621 12.256  -2.680  1.00 38.77  ?  279 ASP A CA  1 
ATOM   2003 C  C   . ASP A 1 279 ? -10.840 12.395  -3.985  1.00 33.54  ?  279 ASP A C   1 
ATOM   2004 O  O   . ASP A 1 279 ? -11.276 11.823  -4.957  1.00 34.38  ?  279 ASP A O   1 
ATOM   2005 C  CB  . ASP A 1 279 ? -13.115 12.579  -2.726  1.00 47.91  ?  279 ASP A CB  1 
ATOM   2006 C  CG  . ASP A 1 279 ? -13.539 14.030  -2.936  1.00 60.41  ?  279 ASP A CG  1 
ATOM   2007 O  OD1 . ASP A 1 279 ? -12.751 14.810  -3.521  1.00 65.65  ?  279 ASP A OD1 1 
ATOM   2008 O  OD2 . ASP A 1 279 ? -14.662 14.375  -2.494  1.00 62.92  -1 279 ASP A OD2 1 
ATOM   2009 N  N   . LEU A 1 280 ? -9.721  13.140  -4.031  1.00 25.62  ?  280 LEU A N   1 
ATOM   2010 C  CA  . LEU A 1 280 ? -8.981  13.323  -5.265  1.00 24.74  ?  280 LEU A CA  1 
ATOM   2011 C  C   . LEU A 1 280 ? -7.894  12.264  -5.341  1.00 24.81  ?  280 LEU A C   1 
ATOM   2012 O  O   . LEU A 1 280 ? -7.176  12.081  -4.361  1.00 21.82  ?  280 LEU A O   1 
ATOM   2013 C  CB  . LEU A 1 280 ? -8.344  14.704  -5.304  1.00 27.93  ?  280 LEU A CB  1 
ATOM   2014 C  CG  . LEU A 1 280 ? -9.302  15.895  -5.268  1.00 31.40  ?  280 LEU A CG  1 
ATOM   2015 C  CD1 . LEU A 1 280 ? -8.559  17.218  -5.257  1.00 31.51  ?  280 LEU A CD1 1 
ATOM   2016 C  CD2 . LEU A 1 280 ? -10.195 15.815  -6.471  1.00 32.56  ?  280 LEU A CD2 1 
ATOM   2017 N  N   . THR A 1 281 ? -7.826  11.538  -6.456  1.00 27.27  ?  281 THR A N   1 
ATOM   2018 C  CA  . THR A 1 281 ? -6.731  10.624  -6.718  1.00 27.13  ?  281 THR A CA  1 
ATOM   2019 C  C   . THR A 1 281 ? -6.220  10.854  -8.134  1.00 26.38  ?  281 THR A C   1 
ATOM   2020 O  O   . THR A 1 281 ? -6.907  11.368  -9.002  1.00 23.89  ?  281 THR A O   1 
ATOM   2021 C  CB  . THR A 1 281 ? -7.097  9.155   -6.483  1.00 31.55  ?  281 THR A CB  1 
ATOM   2022 O  OG1 . THR A 1 281 ? -8.123  8.822   -7.403  1.00 33.82  ?  281 THR A OG1 1 
ATOM   2023 C  CG2 . THR A 1 281 ? -7.567  8.854   -5.068  1.00 32.69  ?  281 THR A CG2 1 
ATOM   2024 N  N   . ALA A 1 282 ? -4.952  10.496  -8.369  1.00 21.26  ?  282 ALA A N   1 
ATOM   2025 C  CA  . ALA A 1 282 ? -4.381  10.605  -9.695  1.00 20.99  ?  282 ALA A CA  1 
ATOM   2026 C  C   . ALA A 1 282 ? -3.207  9.636   -9.763  1.00 20.81  ?  282 ALA A C   1 
ATOM   2027 O  O   . ALA A 1 282 ? -2.719  9.249   -8.713  1.00 17.86  ?  282 ALA A O   1 
ATOM   2028 C  CB  . ALA A 1 282 ? -3.967  12.038  -9.957  1.00 20.79  ?  282 ALA A CB  1 
ATOM   2029 N  N   . PRO A 1 283 ? -2.745  9.169   -10.941 1.00 22.17  ?  283 PRO A N   1 
ATOM   2030 C  CA  . PRO A 1 283 ? -1.595  8.273   -10.974 1.00 22.81  ?  283 PRO A CA  1 
ATOM   2031 C  C   . PRO A 1 283 ? -0.363  8.944   -10.364 1.00 19.10  ?  283 PRO A C   1 
ATOM   2032 O  O   . PRO A 1 283 ? -0.113  10.133  -10.574 1.00 18.68  ?  283 PRO A O   1 
ATOM   2033 C  CB  . PRO A 1 283 ? -1.376  7.946   -12.449 1.00 24.43  ?  283 PRO A CB  1 
ATOM   2034 C  CG  . PRO A 1 283 ? -2.565  8.532   -13.178 1.00 25.59  ?  283 PRO A CG  1 
ATOM   2035 C  CD  . PRO A 1 283 ? -3.286  9.496   -12.262 1.00 26.14  ?  283 PRO A CD  1 
ATOM   2036 N  N   . VAL A 1 284 ? 0.421   8.174   -9.642  1.00 19.02  ?  284 VAL A N   1 
ATOM   2037 C  CA  . VAL A 1 284 ? 1.525   8.712   -8.868  1.00 20.47  ?  284 VAL A CA  1 
ATOM   2038 C  C   . VAL A 1 284 ? 2.659   9.176   -9.790  1.00 18.62  ?  284 VAL A C   1 
ATOM   2039 O  O   . VAL A 1 284 ? 3.406   10.089  -9.435  1.00 18.65  ?  284 VAL A O   1 
ATOM   2040 C  CB  . VAL A 1 284 ? 2.033   7.700   -7.817  1.00 22.10  ?  284 VAL A CB  1 
ATOM   2041 C  CG1 . VAL A 1 284 ? 2.754   6.495   -8.430  1.00 23.95  ?  284 VAL A CG1 1 
ATOM   2042 C  CG2 . VAL A 1 284 ? 2.949   8.400   -6.836  1.00 22.69  ?  284 VAL A CG2 1 
ATOM   2043 N  N   . ASP A 1 285 ? 2.762   8.617   -11.000 1.00 17.67  ?  285 ASP A N   1 
ATOM   2044 C  CA  . ASP A 1 285 ? 3.800   9.034   -11.929 1.00 19.80  ?  285 ASP A CA  1 
ATOM   2045 C  C   . ASP A 1 285 ? 3.514   10.426  -12.482 1.00 19.24  ?  285 ASP A C   1 
ATOM   2046 O  O   . ASP A 1 285 ? 4.451   11.201  -12.678 1.00 21.54  ?  285 ASP A O   1 
ATOM   2047 C  CB  . ASP A 1 285 ? 4.127   7.998   -13.000 1.00 20.77  ?  285 ASP A CB  1 
ATOM   2048 C  CG  . ASP A 1 285 ? 2.939   7.447   -13.772 1.00 21.83  ?  285 ASP A CG  1 
ATOM   2049 O  OD1 . ASP A 1 285 ? 1.771   7.880   -13.483 1.00 22.26  ?  285 ASP A OD1 1 
ATOM   2050 O  OD2 . ASP A 1 285 ? 3.181   6.537   -14.581 1.00 20.26  -1 285 ASP A OD2 1 
ATOM   2051 N  N   . LEU A 1 286 ? 2.229   10.774  -12.675 1.00 16.93  ?  286 LEU A N   1 
ATOM   2052 C  CA  . LEU A 1 286 ? 1.867   12.143  -13.013 1.00 18.41  ?  286 LEU A CA  1 
ATOM   2053 C  C   . LEU A 1 286 ? 2.127   13.086  -11.836 1.00 15.69  ?  286 LEU A C   1 
ATOM   2054 O  O   . LEU A 1 286 ? 2.676   14.159  -12.039 1.00 18.84  ?  286 LEU A O   1 
ATOM   2055 C  CB  . LEU A 1 286 ? 0.397   12.186  -13.421 1.00 20.17  ?  286 LEU A CB  1 
ATOM   2056 C  CG  . LEU A 1 286 ? -0.142  13.577  -13.729 1.00 23.54  ?  286 LEU A CG  1 
ATOM   2057 C  CD1 . LEU A 1 286 ? 0.674   14.236  -14.816 1.00 22.56  ?  286 LEU A CD1 1 
ATOM   2058 C  CD2 . LEU A 1 286 ? -1.606  13.504  -14.127 1.00 27.05  ?  286 LEU A CD2 1 
ATOM   2059 N  N   . LEU A 1 287 ? 1.716   12.703  -10.613 1.00 15.29  ?  287 LEU A N   1 
ATOM   2060 C  CA  . LEU A 1 287 ? 1.905   13.557  -9.444  1.00 15.09  ?  287 LEU A CA  1 
ATOM   2061 C  C   . LEU A 1 287 ? 3.401   13.818  -9.224  1.00 15.44  ?  287 LEU A C   1 
ATOM   2062 O  O   . LEU A 1 287 ? 3.817   14.914  -8.835  1.00 15.62  ?  287 LEU A O   1 
ATOM   2063 C  CB  . LEU A 1 287 ? 1.278   12.931  -8.211  1.00 17.59  ?  287 LEU A CB  1 
ATOM   2064 C  CG  . LEU A 1 287 ? -0.253  12.850  -8.233  1.00 17.99  ?  287 LEU A CG  1 
ATOM   2065 C  CD1 . LEU A 1 287 ? -0.786  12.185  -6.980  1.00 19.75  ?  287 LEU A CD1 1 
ATOM   2066 C  CD2 . LEU A 1 287 ? -0.892  14.222  -8.367  1.00 20.84  ?  287 LEU A CD2 1 
ATOM   2067 N  N   . GLY A 1 288 ? 4.200   12.777  -9.405  1.00 14.09  ?  288 GLY A N   1 
ATOM   2068 C  CA  . GLY A 1 288 ? 5.643   12.876  -9.236  1.00 14.70  ?  288 GLY A CA  1 
ATOM   2069 C  C   . GLY A 1 288 ? 6.299   13.789  -10.258 1.00 14.82  ?  288 GLY A C   1 
ATOM   2070 O  O   . GLY A 1 288 ? 7.240   14.497  -9.918  1.00 16.00  ?  288 GLY A O   1 
ATOM   2071 N  N   . THR A 1 289 ? 5.835   13.748  -11.512 1.00 15.81  ?  289 THR A N   1 
ATOM   2072 C  CA  . THR A 1 289 ? 6.298   14.654  -12.553 1.00 17.02  ?  289 THR A CA  1 
ATOM   2073 C  C   . THR A 1 289 ? 5.945   16.104  -12.206 1.00 15.48  ?  289 THR A C   1 
ATOM   2074 O  O   . THR A 1 289 ? 6.754   17.033  -12.379 1.00 15.08  ?  289 THR A O   1 
ATOM   2075 C  CB  . THR A 1 289 ? 5.732   14.255  -13.923 1.00 16.91  ?  289 THR A CB  1 
ATOM   2076 O  OG1 . THR A 1 289 ? 6.031   12.867  -14.092 1.00 18.64  ?  289 THR A OG1 1 
ATOM   2077 C  CG2 . THR A 1 289 ? 6.340   15.078  -15.035 1.00 17.93  ?  289 THR A CG2 1 
ATOM   2078 N  N   . ALA A 1 290 ? 4.725   16.303  -11.729 1.00 14.24  ?  290 ALA A N   1 
ATOM   2079 C  CA  . ALA A 1 290 ? 4.318   17.617  -11.258 1.00 15.03  ?  290 ALA A CA  1 
ATOM   2080 C  C   . ALA A 1 290 ? 5.123   18.050  -10.035 1.00 15.18  ?  290 ALA A C   1 
ATOM   2081 O  O   . ALA A 1 290 ? 5.379   19.235  -9.889  1.00 15.54  ?  290 ALA A O   1 
ATOM   2082 C  CB  . ALA A 1 290 ? 2.812   17.632  -10.987 1.00 14.72  ?  290 ALA A CB  1 
ATOM   2083 N  N   . ALA A 1 291 ? 5.431   17.121  -9.116  1.00 14.24  ?  291 ALA A N   1 
ATOM   2084 C  CA  . ALA A 1 291 ? 6.255   17.459  -7.964  1.00 14.53  ?  291 ALA A CA  1 
ATOM   2085 C  C   . ALA A 1 291 ? 7.636   17.945  -8.427  1.00 14.54  ?  291 ALA A C   1 
ATOM   2086 O  O   . ALA A 1 291 ? 8.193   18.900  -7.872  1.00 13.43  ?  291 ALA A O   1 
ATOM   2087 C  CB  . ALA A 1 291 ? 6.361   16.276  -7.021  1.00 15.99  ?  291 ALA A CB  1 
ATOM   2088 N  N   . ALA A 1 292 ? 8.188   17.277  -9.442  1.00 13.14  ?  292 ALA A N   1 
ATOM   2089 C  CA  . ALA A 1 292 ? 9.452   17.697  -10.043 1.00 13.43  ?  292 ALA A CA  1 
ATOM   2090 C  C   . ALA A 1 292 ? 9.357   19.117  -10.602 1.00 13.40  ?  292 ALA A C   1 
ATOM   2091 O  O   . ALA A 1 292 ? 10.244  19.943  -10.402 1.00 13.49  ?  292 ALA A O   1 
ATOM   2092 C  CB  . ALA A 1 292 ? 9.877   16.749  -11.128 1.00 13.92  ?  292 ALA A CB  1 
ATOM   2093 N  N   . GLU A 1 293 ? 8.274   19.419  -11.315 1.00 14.42  ?  293 GLU A N   1 
ATOM   2094 C  CA  . GLU A 1 293 ? 8.117   20.749  -11.877 1.00 15.23  ?  293 GLU A CA  1 
ATOM   2095 C  C   . GLU A 1 293 ? 8.017   21.798  -10.766 1.00 13.60  ?  293 GLU A C   1 
ATOM   2096 O  O   . GLU A 1 293 ? 8.704   22.809  -10.804 1.00 15.76  ?  293 GLU A O   1 
ATOM   2097 C  CB  . GLU A 1 293 ? 6.889   20.816  -12.793 1.00 16.04  ?  293 GLU A CB  1 
ATOM   2098 C  CG  . GLU A 1 293 ? 6.721   22.197  -13.429 1.00 18.81  ?  293 GLU A CG  1 
ATOM   2099 C  CD  . GLU A 1 293 ? 5.475   22.383  -14.282 1.00 21.12  ?  293 GLU A CD  1 
ATOM   2100 O  OE1 . GLU A 1 293 ? 4.529   21.581  -14.305 1.00 19.88  ?  293 GLU A OE1 1 
ATOM   2101 O  OE2 . GLU A 1 293 ? 5.492   23.412  -14.936 1.00 25.16  -1 293 GLU A OE2 1 
ATOM   2102 N  N   . ALA A 1 294 ? 7.174   21.535  -9.750  1.00 15.63  ?  294 ALA A N   1 
ATOM   2103 C  CA  . ALA A 1 294 ? 7.020   22.438  -8.603  1.00 14.54  ?  294 ALA A CA  1 
ATOM   2104 C  C   . ALA A 1 294 ? 8.353   22.646  -7.882  1.00 14.39  ?  294 ALA A C   1 
ATOM   2105 O  O   . ALA A 1 294 ? 8.668   23.767  -7.527  1.00 13.95  ?  294 ALA A O   1 
ATOM   2106 C  CB  . ALA A 1 294 ? 5.988   21.916  -7.646  1.00 14.61  ?  294 ALA A CB  1 
ATOM   2107 N  N   . ALA A 1 295 ? 9.126   21.580  -7.674  1.00 15.36  ?  295 ALA A N   1 
ATOM   2108 C  CA  . ALA A 1 295 ? 10.406  21.693  -6.997  1.00 15.03  ?  295 ALA A CA  1 
ATOM   2109 C  C   . ALA A 1 295 ? 11.349  22.583  -7.794  1.00 15.67  ?  295 ALA A C   1 
ATOM   2110 O  O   . ALA A 1 295 ? 12.054  23.429  -7.227  1.00 16.08  ?  295 ALA A O   1 
ATOM   2111 C  CB  . ALA A 1 295 ? 10.982  20.310  -6.752  1.00 16.40  ?  295 ALA A CB  1 
ATOM   2112 N  N   . MET A 1 296 ? 11.412  22.370  -9.109  1.00 14.56  ?  296 MET A N   1 
ATOM   2113 C  CA  . MET A 1 296 ? 12.279  23.164  -9.970  1.00 16.36  ?  296 MET A CA  1 
ATOM   2114 C  C   . MET A 1 296 ? 11.889  24.644  -9.930  1.00 14.98  ?  296 MET A C   1 
ATOM   2115 O  O   . MET A 1 296 ? 12.749  25.511  -9.743  1.00 16.58  ?  296 MET A O   1 
ATOM   2116 C  CB  . MET A 1 296 ? 12.228  22.646  -11.409 1.00 18.47  ?  296 MET A CB  1 
ATOM   2117 C  CG  . MET A 1 296 ? 13.074  23.422  -12.405 1.00 22.26  ?  296 MET A CG  1 
ATOM   2118 S  SD  . MET A 1 296 ? 12.754  22.815  -14.078 1.00 33.10  ?  296 MET A SD  1 
ATOM   2119 C  CE  . MET A 1 296 ? 11.077  23.413  -14.361 1.00 38.84  ?  296 MET A CE  1 
ATOM   2120 N  N   . LEU A 1 297 ? 10.590  24.939  -10.014 1.00 14.72  ?  297 LEU A N   1 
ATOM   2121 C  CA  . LEU A 1 297 ? 10.123  26.323  -9.967  1.00 16.14  ?  297 LEU A CA  1 
ATOM   2122 C  C   . LEU A 1 297 ? 10.398  26.978  -8.605  1.00 15.66  ?  297 LEU A C   1 
ATOM   2123 O  O   . LEU A 1 297 ? 10.728  28.164  -8.542  1.00 15.91  ?  297 LEU A O   1 
ATOM   2124 C  CB  . LEU A 1 297 ? 8.628   26.405  -10.315 1.00 17.78  ?  297 LEU A CB  1 
ATOM   2125 C  CG  . LEU A 1 297 ? 8.232   26.037  -11.743 1.00 22.10  ?  297 LEU A CG  1 
ATOM   2126 C  CD1 . LEU A 1 297 ? 6.702   25.927  -11.904 1.00 24.14  ?  297 LEU A CD1 1 
ATOM   2127 C  CD2 . LEU A 1 297 ? 8.822   27.039  -12.705 1.00 23.45  ?  297 LEU A CD2 1 
ATOM   2128 N  N   . ALA A 1 298 ? 10.254  26.231  -7.497  1.00 15.51  ?  298 ALA A N   1 
ATOM   2129 C  CA  . ALA A 1 298 ? 10.541  26.724  -6.166  1.00 14.05  ?  298 ALA A CA  1 
ATOM   2130 C  C   . ALA A 1 298 ? 12.015  27.073  -5.990  1.00 15.02  ?  298 ALA A C   1 
ATOM   2131 O  O   . ALA A 1 298 ? 12.335  28.006  -5.253  1.00 15.13  ?  298 ALA A O   1 
ATOM   2132 C  CB  . ALA A 1 298 ? 10.054  25.711  -5.134  1.00 15.59  ?  298 ALA A CB  1 
ATOM   2133 N  N   . CYS A 1 299 ? 12.907  26.311  -6.624  1.00 14.05  ?  299 CYS A N   1 
ATOM   2134 C  CA  . CYS A 1 299 ? 14.337  26.597  -6.581  1.00 16.08  ?  299 CYS A CA  1 
ATOM   2135 C  C   . CYS A 1 299 ? 14.623  27.989  -7.162  1.00 16.11  ?  299 CYS A C   1 
ATOM   2136 O  O   . CYS A 1 299 ? 15.390  28.768  -6.591  1.00 16.81  ?  299 CYS A O   1 
ATOM   2137 C  CB  . CYS A 1 299 ? 15.157  25.560  -7.340  1.00 15.99  ?  299 CYS A CB  1 
ATOM   2138 S  SG  . CYS A 1 299 ? 15.283  23.931  -6.553  1.00 20.49  ?  299 CYS A SG  1 
ATOM   2139 N  N   . LEU A 1 300 ? 13.981  28.310  -8.298  1.00 17.46  ?  300 LEU A N   1 
ATOM   2140 C  CA  . LEU A 1 300 ? 14.150  29.603  -8.951  1.00 18.64  ?  300 LEU A CA  1 
ATOM   2141 C  C   . LEU A 1 300 ? 13.505  30.709  -8.117  1.00 19.82  ?  300 LEU A C   1 
ATOM   2142 O  O   . LEU A 1 300 ? 14.052  31.809  -8.013  1.00 19.56  ?  300 LEU A O   1 
ATOM   2143 C  CB  . LEU A 1 300 ? 13.582  29.558  -10.371 1.00 21.34  ?  300 LEU A CB  1 
ATOM   2144 C  CG  . LEU A 1 300 ? 14.362  28.625  -11.310 1.00 25.93  ?  300 LEU A CG  1 
ATOM   2145 C  CD1 . LEU A 1 300 ? 13.575  28.397  -12.619 1.00 30.45  ?  300 LEU A CD1 1 
ATOM   2146 C  CD2 . LEU A 1 300 ? 15.744  29.208  -11.546 1.00 27.14  ?  300 LEU A CD2 1 
ATOM   2147 N  N   . ASP A 1 301 ? 12.341  30.418  -7.536  1.00 16.97  ?  301 ASP A N   1 
ATOM   2148 C  CA  . ASP A 1 301 ? 11.645  31.356  -6.672  1.00 17.35  ?  301 ASP A CA  1 
ATOM   2149 C  C   . ASP A 1 301 ? 12.529  31.826  -5.508  1.00 19.43  ?  301 ASP A C   1 
ATOM   2150 O  O   . ASP A 1 301 ? 12.452  32.988  -5.091  1.00 18.85  ?  301 ASP A O   1 
ATOM   2151 C  CB  . ASP A 1 301 ? 10.325  30.798  -6.193  1.00 17.54  ?  301 ASP A CB  1 
ATOM   2152 C  CG  . ASP A 1 301 ? 9.482   31.773  -5.371  1.00 20.34  ?  301 ASP A CG  1 
ATOM   2153 O  OD1 . ASP A 1 301 ? 9.078   32.771  -5.972  1.00 20.19  ?  301 ASP A OD1 1 
ATOM   2154 O  OD2 . ASP A 1 301 ? 9.226   31.542  -4.148  1.00 14.45  -1 301 ASP A OD2 1 
ATOM   2155 N  N   . ALA A 1 302 ? 13.338  30.913  -4.968  1.00 18.39  ?  302 ALA A N   1 
ATOM   2156 C  CA  . ALA A 1 302 ? 14.174  31.174  -3.821  1.00 18.95  ?  302 ALA A CA  1 
ATOM   2157 C  C   . ALA A 1 302 ? 15.136  32.323  -4.105  1.00 22.85  ?  302 ALA A C   1 
ATOM   2158 O  O   . ALA A 1 302 ? 15.487  33.022  -3.165  1.00 21.55  ?  302 ALA A O   1 
ATOM   2159 C  CB  . ALA A 1 302 ? 14.933  29.928  -3.422  1.00 17.89  ?  302 ALA A CB  1 
ATOM   2160 N  N   . VAL A 1 303 ? 15.598  32.449  -5.351  1.00 22.23  ?  303 VAL A N   1 
ATOM   2161 C  CA  . VAL A 1 303 ? 16.603  33.447  -5.701  1.00 30.00  ?  303 VAL A CA  1 
ATOM   2162 C  C   . VAL A 1 303 ? 16.021  34.663  -6.421  1.00 32.27  ?  303 VAL A C   1 
ATOM   2163 O  O   . VAL A 1 303 ? 16.724  35.640  -6.507  1.00 34.92  ?  303 VAL A O   1 
ATOM   2164 C  CB  . VAL A 1 303 ? 17.784  32.863  -6.495  1.00 27.42  ?  303 VAL A CB  1 
ATOM   2165 C  CG1 . VAL A 1 303 ? 18.475  31.762  -5.713  1.00 30.61  ?  303 VAL A CG1 1 
ATOM   2166 C  CG2 . VAL A 1 303 ? 17.379  32.317  -7.852  1.00 29.25  ?  303 VAL A CG2 1 
ATOM   2167 N  N   . MET A 1 304 ? 14.750  34.666  -6.841  1.00 40.39  ?  304 MET A N   1 
ATOM   2168 C  CA  . MET A 1 304 ? 14.124  35.832  -7.457  1.00 46.04  ?  304 MET A CA  1 
ATOM   2169 C  C   . MET A 1 304 ? 13.587  36.790  -6.386  1.00 53.96  ?  304 MET A C   1 
ATOM   2170 O  O   . MET A 1 304 ? 12.852  37.715  -6.709  1.00 66.11  ?  304 MET A O   1 
ATOM   2171 C  CB  . MET A 1 304 ? 12.914  35.438  -8.321  1.00 52.35  ?  304 MET A CB  1 
ATOM   2172 C  CG  . MET A 1 304 ? 13.148  34.436  -9.439  1.00 59.61  ?  304 MET A CG  1 
ATOM   2173 S  SD  . MET A 1 304 ? 14.648  34.701  -10.408 1.00 77.91  ?  304 MET A SD  1 
ATOM   2174 C  CE  . MET A 1 304 ? 14.763  33.303  -11.537 1.00 61.55  ?  304 MET A CE  1 
ATOM   2175 N  N   . GLN A 1 305 ? 13.912  36.559  -5.105  1.00 63.06  ?  305 GLN A N   1 
ATOM   2176 C  CA  . GLN A 1 305 ? 13.510  37.428  -4.005  1.00 70.88  ?  305 GLN A CA  1 
ATOM   2177 C  C   . GLN A 1 305 ? 14.753  38.164  -3.463  1.00 80.86  ?  305 GLN A C   1 
ATOM   2178 O  O   . GLN A 1 305 ? 15.034  39.256  -4.004  1.00 85.91  ?  305 GLN A O   1 
ATOM   2179 C  CB  . GLN A 1 305 ? 12.830  36.649  -2.874  1.00 67.84  ?  305 GLN A CB  1 
ATOM   2180 C  CG  . GLN A 1 305 ? 11.368  37.014  -2.618  1.00 63.24  ?  305 GLN A CG  1 
ATOM   2181 C  CD  . GLN A 1 305 ? 10.362  36.247  -3.447  1.00 58.60  ?  305 GLN A CD  1 
ATOM   2182 O  OE1 . GLN A 1 305 ? 10.673  35.258  -4.119  1.00 49.63  ?  305 GLN A OE1 1 
ATOM   2183 N  NE2 . GLN A 1 305 ? 9.121   36.702  -3.391  1.00 61.70  ?  305 GLN A NE2 1 
ATOM   2184 N  N   . MET B 1 1   ? 31.117  -7.169  27.347  1.00 16.67  ?  1   MET B N   1 
ATOM   2185 C  CA  . MET B 1 1   ? 31.519  -5.864  27.917  1.00 17.09  ?  1   MET B CA  1 
ATOM   2186 C  C   . MET B 1 1   ? 32.102  -5.015  26.778  1.00 18.11  ?  1   MET B C   1 
ATOM   2187 O  O   . MET B 1 1   ? 33.211  -5.256  26.284  1.00 18.71  ?  1   MET B O   1 
ATOM   2188 C  CB  . MET B 1 1   ? 32.555  -6.053  29.034  1.00 18.16  ?  1   MET B CB  1 
ATOM   2189 C  CG  . MET B 1 1   ? 32.649  -4.806  29.942  1.00 18.70  ?  1   MET B CG  1 
ATOM   2190 S  SD  . MET B 1 1   ? 31.204  -4.537  30.973  1.00 25.26  ?  1   MET B SD  1 
ATOM   2191 C  CE  . MET B 1 1   ? 31.336  -5.951  32.070  1.00 26.92  ?  1   MET B CE  1 
ATOM   2192 N  N   . LEU B 1 2   ? 31.306  -4.038  26.325  1.00 17.37  ?  2   LEU B N   1 
ATOM   2193 C  CA  . LEU B 1 2   ? 31.594  -3.264  25.142  1.00 15.02  ?  2   LEU B CA  1 
ATOM   2194 C  C   . LEU B 1 2   ? 32.947  -2.563  25.238  1.00 15.75  ?  2   LEU B C   1 
ATOM   2195 O  O   . LEU B 1 2   ? 33.609  -2.363  24.212  1.00 14.60  ?  2   LEU B O   1 
ATOM   2196 C  CB  . LEU B 1 2   ? 30.476  -2.265  24.879  1.00 15.12  ?  2   LEU B CB  1 
ATOM   2197 C  CG  . LEU B 1 2   ? 30.526  -1.603  23.500  1.00 16.22  ?  2   LEU B CG  1 
ATOM   2198 C  CD1 . LEU B 1 2   ? 30.154  -2.615  22.411  1.00 17.45  ?  2   LEU B CD1 1 
ATOM   2199 C  CD2 . LEU B 1 2   ? 29.604  -0.432  23.416  1.00 17.56  ?  2   LEU B CD2 1 
ATOM   2200 N  N   . THR B 1 3   ? 33.341  -2.168  26.457  1.00 15.45  ?  3   THR B N   1 
ATOM   2201 C  CA  . THR B 1 3   ? 34.626  -1.512  26.693  1.00 16.65  ?  3   THR B CA  1 
ATOM   2202 C  C   . THR B 1 3   ? 35.830  -2.435  26.506  1.00 18.97  ?  3   THR B C   1 
ATOM   2203 O  O   . THR B 1 3   ? 36.973  -1.967  26.604  1.00 18.56  ?  3   THR B O   1 
ATOM   2204 C  CB  . THR B 1 3   ? 34.609  -0.916  28.095  1.00 17.30  ?  3   THR B CB  1 
ATOM   2205 O  OG1 . THR B 1 3   ? 34.205  -1.894  29.063  1.00 18.13  ?  3   THR B OG1 1 
ATOM   2206 C  CG2 . THR B 1 3   ? 33.687  0.278   28.147  1.00 18.24  ?  3   THR B CG2 1 
ATOM   2207 N  N   . ASP B 1 4   ? 35.610  -3.721  26.232  1.00 18.88  ?  4   ASP B N   1 
ATOM   2208 C  CA  . ASP B 1 4   ? 36.689  -4.594  25.799  1.00 20.87  ?  4   ASP B CA  1 
ATOM   2209 C  C   . ASP B 1 4   ? 37.279  -4.147  24.456  1.00 22.95  ?  4   ASP B C   1 
ATOM   2210 O  O   . ASP B 1 4   ? 38.385  -4.559  24.089  1.00 18.74  ?  4   ASP B O   1 
ATOM   2211 C  CB  . ASP B 1 4   ? 36.216  -6.035  25.706  1.00 20.38  ?  4   ASP B CB  1 
ATOM   2212 C  CG  . ASP B 1 4   ? 35.899  -6.771  27.004  1.00 20.88  ?  4   ASP B CG  1 
ATOM   2213 O  OD1 . ASP B 1 4   ? 36.246  -6.280  28.076  1.00 22.93  ?  4   ASP B OD1 1 
ATOM   2214 O  OD2 . ASP B 1 4   ? 35.256  -7.820  26.935  1.00 20.11  -1 4   ASP B OD2 1 
ATOM   2215 N  N   . ILE B 1 5   ? 36.534  -3.342  23.685  1.00 20.35  ?  5   ILE B N   1 
ATOM   2216 C  CA  . ILE B 1 5   ? 36.989  -2.896  22.378  1.00 21.30  ?  5   ILE B CA  1 
ATOM   2217 C  C   . ILE B 1 5   ? 37.715  -1.576  22.540  1.00 20.49  ?  5   ILE B C   1 
ATOM   2218 O  O   . ILE B 1 5   ? 37.262  -0.681  23.258  1.00 21.01  ?  5   ILE B O   1 
ATOM   2219 C  CB  . ILE B 1 5   ? 35.821  -2.759  21.388  1.00 21.02  ?  5   ILE B CB  1 
ATOM   2220 C  CG1 . ILE B 1 5   ? 34.982  -4.040  21.307  1.00 20.84  ?  5   ILE B CG1 1 
ATOM   2221 C  CG2 . ILE B 1 5   ? 36.295  -2.290  20.019  1.00 21.29  ?  5   ILE B CG2 1 
ATOM   2222 C  CD1 . ILE B 1 5   ? 35.721  -5.265  20.850  1.00 22.38  ?  5   ILE B CD1 1 
ATOM   2223 N  N   . ASP B 1 6   ? 38.870  -1.489  21.879  1.00 23.25  ?  6   ASP B N   1 
ATOM   2224 C  CA  . ASP B 1 6   ? 39.778  -0.357  22.021  1.00 23.20  ?  6   ASP B CA  1 
ATOM   2225 C  C   . ASP B 1 6   ? 39.056  0.969   21.856  1.00 23.93  ?  6   ASP B C   1 
ATOM   2226 O  O   . ASP B 1 6   ? 38.375  1.212   20.862  1.00 27.06  ?  6   ASP B O   1 
ATOM   2227 C  CB  . ASP B 1 6   ? 40.850  -0.346  20.932  1.00 30.32  ?  6   ASP B CB  1 
ATOM   2228 C  CG  . ASP B 1 6   ? 41.658  -1.635  20.750  1.00 35.31  ?  6   ASP B CG  1 
ATOM   2229 O  OD1 . ASP B 1 6   ? 41.092  -2.735  20.934  1.00 43.71  ?  6   ASP B OD1 1 
ATOM   2230 O  OD2 . ASP B 1 6   ? 42.828  -1.549  20.352  1.00 45.59  -1 6   ASP B OD2 1 
ATOM   2231 N  N   . GLY B 1 7   ? 39.257  1.857   22.818  1.00 22.21  ?  7   GLY B N   1 
ATOM   2232 C  CA  . GLY B 1 7   ? 38.857  3.239   22.661  1.00 21.15  ?  7   GLY B CA  1 
ATOM   2233 C  C   . GLY B 1 7   ? 37.433  3.530   23.144  1.00 22.02  ?  7   GLY B C   1 
ATOM   2234 O  O   . GLY B 1 7   ? 37.041  4.687   23.171  1.00 22.95  ?  7   GLY B O   1 
ATOM   2235 N  N   . ILE B 1 8   ? 36.659  2.527   23.558  1.00 18.65  ?  8   ILE B N   1 
ATOM   2236 C  CA  . ILE B 1 8   ? 35.265  2.773   23.902  1.00 17.88  ?  8   ILE B CA  1 
ATOM   2237 C  C   . ILE B 1 8   ? 35.133  3.051   25.397  1.00 17.94  ?  8   ILE B C   1 
ATOM   2238 O  O   . ILE B 1 8   ? 35.684  2.309   26.215  1.00 19.12  ?  8   ILE B O   1 
ATOM   2239 C  CB  . ILE B 1 8   ? 34.395  1.572   23.480  1.00 18.69  ?  8   ILE B CB  1 
ATOM   2240 C  CG1 . ILE B 1 8   ? 34.496  1.304   21.972  1.00 19.33  ?  8   ILE B CG1 1 
ATOM   2241 C  CG2 . ILE B 1 8   ? 32.955  1.772   23.969  1.00 19.20  ?  8   ILE B CG2 1 
ATOM   2242 C  CD1 . ILE B 1 8   ? 33.553  0.224   21.454  1.00 18.80  ?  8   ILE B CD1 1 
ATOM   2243 N  N   . ARG B 1 9   ? 34.424  4.142   25.746  1.00 16.11  ?  9   ARG B N   1 
ATOM   2244 C  CA  . ARG B 1 9   ? 33.986  4.366   27.095  1.00 17.02  ?  9   ARG B CA  1 
ATOM   2245 C  C   . ARG B 1 9   ? 32.464  4.353   27.114  1.00 16.70  ?  9   ARG B C   1 
ATOM   2246 O  O   . ARG B 1 9   ? 31.848  4.752   26.139  1.00 17.93  ?  9   ARG B O   1 
ATOM   2247 C  CB  . ARG B 1 9   ? 34.542  5.703   27.596  1.00 17.55  ?  9   ARG B CB  1 
ATOM   2248 C  CG  . ARG B 1 9   ? 36.060  5.701   27.705  1.00 20.56  ?  9   ARG B CG  1 
ATOM   2249 C  CD  . ARG B 1 9   ? 36.525  7.030   28.316  1.00 22.01  ?  9   ARG B CD  1 
ATOM   2250 N  NE  . ARG B 1 9   ? 36.555  8.092   27.305  1.00 20.00  ?  9   ARG B NE  1 
ATOM   2251 C  CZ  . ARG B 1 9   ? 35.843  9.225   27.350  1.00 22.03  ?  9   ARG B CZ  1 
ATOM   2252 N  NH1 . ARG B 1 9   ? 35.119  9.555   28.397  1.00 24.82  1  9   ARG B NH1 1 
ATOM   2253 N  NH2 . ARG B 1 9   ? 35.916  10.083  26.369  1.00 26.03  ?  9   ARG B NH2 1 
ATOM   2254 N  N   . VAL B 1 10  ? 31.882  3.911   28.225  1.00 16.39  ?  10  VAL B N   1 
ATOM   2255 C  CA  . VAL B 1 10  ? 30.434  3.853   28.370  1.00 16.24  ?  10  VAL B CA  1 
ATOM   2256 C  C   . VAL B 1 10  ? 30.006  4.628   29.605  1.00 17.34  ?  10  VAL B C   1 
ATOM   2257 O  O   . VAL B 1 10  ? 30.606  4.493   30.667  1.00 17.04  ?  10  VAL B O   1 
ATOM   2258 C  CB  . VAL B 1 10  ? 29.967  2.388   28.451  1.00 16.90  ?  10  VAL B CB  1 
ATOM   2259 C  CG1 . VAL B 1 10  ? 28.521  2.272   28.899  1.00 16.03  ?  10  VAL B CG1 1 
ATOM   2260 C  CG2 . VAL B 1 10  ? 30.142  1.682   27.116  1.00 16.77  ?  10  VAL B CG2 1 
ATOM   2261 N  N   . GLY B 1 11  ? 28.966  5.434   29.454  1.00 15.14  ?  11  GLY B N   1 
ATOM   2262 C  CA  . GLY B 1 11  ? 28.410  6.204   30.552  1.00 16.23  ?  11  GLY B CA  1 
ATOM   2263 C  C   . GLY B 1 11  ? 26.899  6.027   30.582  1.00 15.88  ?  11  GLY B C   1 
ATOM   2264 O  O   . GLY B 1 11  ? 26.262  6.060   29.542  1.00 16.37  ?  11  GLY B O   1 
ATOM   2265 N  N   . HIS B 1 12  ? 26.339  5.886   31.784  1.00 15.02  ?  12  HIS B N   1 
ATOM   2266 C  CA  . HIS B 1 12  ? 24.907  5.882   32.006  1.00 15.60  ?  12  HIS B CA  1 
ATOM   2267 C  C   . HIS B 1 12  ? 24.463  7.158   32.720  1.00 17.99  ?  12  HIS B C   1 
ATOM   2268 O  O   . HIS B 1 12  ? 25.202  7.714   33.508  1.00 16.81  ?  12  HIS B O   1 
ATOM   2269 C  CB  . HIS B 1 12  ? 24.520  4.729   32.931  1.00 16.21  ?  12  HIS B CB  1 
ATOM   2270 C  CG  . HIS B 1 12  ? 24.882  3.366   32.448  1.00 17.67  ?  12  HIS B CG  1 
ATOM   2271 N  ND1 . HIS B 1 12  ? 24.540  2.861   31.212  1.00 17.15  ?  12  HIS B ND1 1 
ATOM   2272 C  CD2 . HIS B 1 12  ? 25.508  2.356   33.113  1.00 18.45  ?  12  HIS B CD2 1 
ATOM   2273 C  CE1 . HIS B 1 12  ? 24.948  1.608   31.136  1.00 19.44  ?  12  HIS B CE1 1 
ATOM   2274 N  NE2 . HIS B 1 12  ? 25.573  1.277   32.256  1.00 18.90  ?  12  HIS B NE2 1 
ATOM   2275 N  N   . ALA B 1 13  ? 23.231  7.569   32.456  1.00 17.21  ?  13  ALA B N   1 
ATOM   2276 C  CA  . ALA B 1 13  ? 22.471  8.446   33.318  1.00 16.75  ?  13  ALA B CA  1 
ATOM   2277 C  C   . ALA B 1 13  ? 21.150  7.755   33.596  1.00 18.40  ?  13  ALA B C   1 
ATOM   2278 O  O   . ALA B 1 13  ? 20.487  7.263   32.671  1.00 19.75  ?  13  ALA B O   1 
ATOM   2279 C  CB  . ALA B 1 13  ? 22.252  9.775   32.666  1.00 17.06  ?  13  ALA B CB  1 
ATOM   2280 N  N   . THR B 1 14  ? 20.774  7.715   34.874  1.00 19.26  ?  14  THR B N   1 
ATOM   2281 C  CA  . THR B 1 14  ? 19.706  6.854   35.361  1.00 20.67  ?  14  THR B CA  1 
ATOM   2282 C  C   . THR B 1 14  ? 18.773  7.667   36.239  1.00 20.87  ?  14  THR B C   1 
ATOM   2283 O  O   . THR B 1 14  ? 19.236  8.331   37.149  1.00 20.23  ?  14  THR B O   1 
ATOM   2284 C  CB  . THR B 1 14  ? 20.300  5.693   36.163  1.00 20.00  ?  14  THR B CB  1 
ATOM   2285 O  OG1 . THR B 1 14  ? 21.199  4.925   35.360  1.00 19.45  ?  14  THR B OG1 1 
ATOM   2286 C  CG2 . THR B 1 14  ? 19.212  4.793   36.738  1.00 19.73  ?  14  THR B CG2 1 
ATOM   2287 N  N   . ASP B 1 15  ? 17.483  7.644   35.942  1.00 21.08  ?  15  ASP B N   1 
ATOM   2288 C  CA  . ASP B 1 15  ? 16.479  8.210   36.821  1.00 24.29  ?  15  ASP B CA  1 
ATOM   2289 C  C   . ASP B 1 15  ? 15.586  7.072   37.311  1.00 24.88  ?  15  ASP B C   1 
ATOM   2290 O  O   . ASP B 1 15  ? 14.635  6.690   36.635  1.00 21.87  ?  15  ASP B O   1 
ATOM   2291 C  CB  . ASP B 1 15  ? 15.691  9.338   36.172  1.00 26.11  ?  15  ASP B CB  1 
ATOM   2292 C  CG  . ASP B 1 15  ? 14.683  10.043  37.076  1.00 27.18  ?  15  ASP B CG  1 
ATOM   2293 O  OD1 . ASP B 1 15  ? 14.272  9.446   38.088  1.00 25.64  ?  15  ASP B OD1 1 
ATOM   2294 O  OD2 . ASP B 1 15  ? 14.324  11.188  36.771  1.00 28.57  -1 15  ASP B OD2 1 
ATOM   2295 N  N   . ALA B 1 16  ? 15.883  6.626   38.548  1.00 25.82  ?  16  ALA B N   1 
ATOM   2296 C  CA  . ALA B 1 16  ? 15.250  5.480   39.183  1.00 30.76  ?  16  ALA B CA  1 
ATOM   2297 C  C   . ALA B 1 16  ? 13.832  5.797   39.648  1.00 29.64  ?  16  ALA B C   1 
ATOM   2298 O  O   . ALA B 1 16  ? 13.017  4.890   39.735  1.00 34.79  ?  16  ALA B O   1 
ATOM   2299 C  CB  . ALA B 1 16  ? 16.126  4.983   40.332  1.00 32.71  ?  16  ALA B CB  1 
ATOM   2300 N  N   . ARG B 1 17  ? 13.476  7.078   39.794  1.00 28.52  ?  17  ARG B N   1 
ATOM   2301 C  CA  . ARG B 1 17  ? 12.113  7.429   40.189  1.00 29.74  ?  17  ARG B CA  1 
ATOM   2302 C  C   . ARG B 1 17  ? 11.193  7.511   38.977  1.00 26.03  ?  17  ARG B C   1 
ATOM   2303 O  O   . ARG B 1 17  ? 10.083  6.986   38.989  1.00 26.75  ?  17  ARG B O   1 
ATOM   2304 C  CB  . ARG B 1 17  ? 12.153  8.774   40.932  1.00 38.95  ?  17  ARG B CB  1 
ATOM   2305 C  CG  . ARG B 1 17  ? 10.946  9.110   41.794  1.00 46.41  ?  17  ARG B CG  1 
ATOM   2306 C  CD  . ARG B 1 17  ? 9.815   9.844   41.109  1.00 59.85  ?  17  ARG B CD  1 
ATOM   2307 N  NE  . ARG B 1 17  ? 10.279  11.022  40.363  1.00 67.44  ?  17  ARG B NE  1 
ATOM   2308 C  CZ  . ARG B 1 17  ? 9.547   11.679  39.473  1.00 61.90  ?  17  ARG B CZ  1 
ATOM   2309 N  NH1 . ARG B 1 17  ? 8.234   11.533  39.438  1.00 63.56  1  17  ARG B NH1 1 
ATOM   2310 N  NH2 . ARG B 1 17  ? 10.125  12.530  38.654  1.00 62.54  ?  17  ARG B NH2 1 
ATOM   2311 N  N   . ALA B 1 18  ? 11.617  8.235   37.927  1.00 22.72  ?  18  ALA B N   1 
ATOM   2312 C  CA  . ALA B 1 18  ? 10.829  8.319   36.701  1.00 21.78  ?  18  ALA B CA  1 
ATOM   2313 C  C   . ALA B 1 18  ? 10.905  7.016   35.887  1.00 19.44  ?  18  ALA B C   1 
ATOM   2314 O  O   . ALA B 1 18  ? 10.047  6.798   35.015  1.00 18.49  ?  18  ALA B O   1 
ATOM   2315 C  CB  . ALA B 1 18  ? 11.290  9.480   35.835  1.00 20.46  ?  18  ALA B CB  1 
ATOM   2316 N  N   . MET B 1 19  ? 11.944  6.193   36.134  1.00 18.86  ?  19  MET B N   1 
ATOM   2317 C  CA  A MET B 1 19  ? 12.149  4.957   35.379  0.50 20.01  ?  19  MET B CA  1 
ATOM   2318 C  CA  B MET B 1 19  ? 12.145  4.957   35.379  0.50 20.63  ?  19  MET B CA  1 
ATOM   2319 C  C   . MET B 1 19  ? 12.416  5.280   33.903  1.00 17.91  ?  19  MET B C   1 
ATOM   2320 O  O   . MET B 1 19  ? 11.631  4.941   33.004  1.00 16.38  ?  19  MET B O   1 
ATOM   2321 C  CB  A MET B 1 19  ? 10.991  3.965   35.569  0.50 22.19  ?  19  MET B CB  1 
ATOM   2322 C  CB  B MET B 1 19  ? 10.960  3.995   35.545  0.50 23.72  ?  19  MET B CB  1 
ATOM   2323 C  CG  A MET B 1 19  ? 10.859  3.538   37.045  0.50 24.34  ?  19  MET B CG  1 
ATOM   2324 C  CG  B MET B 1 19  ? 10.734  3.592   37.000  0.50 27.24  ?  19  MET B CG  1 
ATOM   2325 S  SD  A MET B 1 19  ? 9.676   2.220   37.370  0.50 28.28  ?  19  MET B SD  1 
ATOM   2326 S  SD  B MET B 1 19  ? 12.160  2.723   37.679  0.50 33.48  ?  19  MET B SD  1 
ATOM   2327 C  CE  A MET B 1 19  ? 10.409  0.782   36.573  0.50 28.02  ?  19  MET B CE  1 
ATOM   2328 C  CE  B MET B 1 19  ? 11.957  1.186   36.768  0.50 32.54  ?  19  MET B CE  1 
ATOM   2329 N  N   . THR B 1 20  ? 13.538  5.987   33.677  1.00 15.56  ?  20  THR B N   1 
ATOM   2330 C  CA  . THR B 1 20  ? 14.038  6.288   32.348  1.00 16.17  ?  20  THR B CA  1 
ATOM   2331 C  C   . THR B 1 20  ? 15.520  6.588   32.502  1.00 15.43  ?  20  THR B C   1 
ATOM   2332 O  O   . THR B 1 20  ? 16.027  6.729   33.601  1.00 16.93  ?  20  THR B O   1 
ATOM   2333 C  CB  . THR B 1 20  ? 13.263  7.439   31.696  1.00 17.03  ?  20  THR B CB  1 
ATOM   2334 O  OG1 . THR B 1 20  ? 13.501  7.505   30.291  1.00 16.71  ?  20  THR B OG1 1 
ATOM   2335 C  CG2 . THR B 1 20  ? 13.629  8.810   32.240  1.00 18.27  ?  20  THR B CG2 1 
ATOM   2336 N  N   . GLY B 1 21  ? 16.204  6.723   31.382  1.00 15.02  ?  21  GLY B N   1 
ATOM   2337 C  CA  . GLY B 1 21  ? 17.623  7.030   31.364  1.00 15.29  ?  21  GLY B CA  1 
ATOM   2338 C  C   . GLY B 1 21  ? 18.180  6.928   29.946  1.00 14.44  ?  21  GLY B C   1 
ATOM   2339 O  O   . GLY B 1 21  ? 17.439  6.657   29.007  1.00 15.26  ?  21  GLY B O   1 
ATOM   2340 N  N   . CYS B 1 22  ? 19.504  7.035   29.843  1.00 14.58  ?  22  CYS B N   1 
ATOM   2341 C  CA  . CYS B 1 22  ? 20.179  6.941   28.561  1.00 15.09  ?  22  CYS B CA  1 
ATOM   2342 C  C   . CYS B 1 22  ? 21.588  6.444   28.833  1.00 14.47  ?  22  CYS B C   1 
ATOM   2343 O  O   . CYS B 1 22  ? 22.119  6.595   29.943  1.00 14.53  ?  22  CYS B O   1 
ATOM   2344 C  CB  . CYS B 1 22  ? 20.117  8.254   27.783  1.00 16.35  ?  22  CYS B CB  1 
ATOM   2345 S  SG  . CYS B 1 22  ? 20.908  9.648   28.654  1.00 18.89  ?  22  CYS B SG  1 
ATOM   2346 N  N   . THR B 1 23  ? 22.160  5.835   27.804  1.00 14.49  ?  23  THR B N   1 
ATOM   2347 C  CA  . THR B 1 23  ? 23.493  5.277   27.835  1.00 13.54  ?  23  THR B CA  1 
ATOM   2348 C  C   . THR B 1 23  ? 24.238  5.751   26.597  1.00 15.46  ?  23  THR B C   1 
ATOM   2349 O  O   . THR B 1 23  ? 23.682  5.727   25.486  1.00 15.18  ?  23  THR B O   1 
ATOM   2350 C  CB  . THR B 1 23  ? 23.401  3.757   27.888  1.00 13.94  ?  23  THR B CB  1 
ATOM   2351 O  OG1 . THR B 1 23  ? 22.727  3.295   29.055  1.00 13.52  ?  23  THR B OG1 1 
ATOM   2352 C  CG2 . THR B 1 23  ? 24.774  3.119   27.800  1.00 14.38  ?  23  THR B CG2 1 
ATOM   2353 N  N   . ILE B 1 24  ? 25.496  6.174   26.761  1.00 13.75  ?  24  ILE B N   1 
ATOM   2354 C  CA  . ILE B 1 24  ? 26.277  6.557   25.608  1.00 14.20  ?  24  ILE B CA  1 
ATOM   2355 C  C   . ILE B 1 24  ? 27.541  5.722   25.565  1.00 14.42  ?  24  ILE B C   1 
ATOM   2356 O  O   . ILE B 1 24  ? 28.152  5.471   26.615  1.00 14.37  ?  24  ILE B O   1 
ATOM   2357 C  CB  . ILE B 1 24  ? 26.598  8.068   25.559  1.00 16.52  ?  24  ILE B CB  1 
ATOM   2358 C  CG1 . ILE B 1 24  ? 27.220  8.408   24.196  1.00 16.51  ?  24  ILE B CG1 1 
ATOM   2359 C  CG2 . ILE B 1 24  ? 27.484  8.527   26.721  1.00 18.33  ?  24  ILE B CG2 1 
ATOM   2360 C  CD1 . ILE B 1 24  ? 27.214  9.868   23.846  1.00 21.56  ?  24  ILE B CD1 1 
ATOM   2361 N  N   . ALA B 1 25  ? 27.873  5.265   24.338  1.00 13.32  ?  25  ALA B N   1 
ATOM   2362 C  CA  . ALA B 1 25  ? 29.188  4.744   24.028  1.00 13.15  ?  25  ALA B CA  1 
ATOM   2363 C  C   . ALA B 1 25  ? 29.988  5.848   23.330  1.00 14.30  ?  25  ALA B C   1 
ATOM   2364 O  O   . ALA B 1 25  ? 29.610  6.397   22.292  1.00 15.08  ?  25  ALA B O   1 
ATOM   2365 C  CB  . ALA B 1 25  ? 29.027  3.498   23.188  1.00 14.54  ?  25  ALA B CB  1 
ATOM   2366 N  N   . VAL B 1 26  ? 31.133  6.202   23.906  1.00 14.71  ?  26  VAL B N   1 
ATOM   2367 C  CA  . VAL B 1 26  ? 31.978  7.260   23.400  1.00 15.10  ?  26  VAL B CA  1 
ATOM   2368 C  C   . VAL B 1 26  ? 33.195  6.627   22.730  1.00 16.31  ?  26  VAL B C   1 
ATOM   2369 O  O   . VAL B 1 26  ? 33.784  5.694   23.269  1.00 17.63  ?  26  VAL B O   1 
ATOM   2370 C  CB  . VAL B 1 26  ? 32.419  8.205   24.533  1.00 17.20  ?  26  VAL B CB  1 
ATOM   2371 C  CG1 . VAL B 1 26  ? 33.321  9.316   24.026  1.00 19.23  ?  26  VAL B CG1 1 
ATOM   2372 C  CG2 . VAL B 1 26  ? 31.240  8.764   25.299  1.00 17.32  ?  26  VAL B CG2 1 
ATOM   2373 N  N   . PHE B 1 27  ? 33.575  7.139   21.540  1.00 15.57  ?  27  PHE B N   1 
ATOM   2374 C  CA  . PHE B 1 27  ? 34.641  6.532   20.768  1.00 17.19  ?  27  PHE B CA  1 
ATOM   2375 C  C   . PHE B 1 27  ? 35.876  7.427   20.823  1.00 17.76  ?  27  PHE B C   1 
ATOM   2376 O  O   . PHE B 1 27  ? 35.884  8.462   20.193  1.00 19.61  ?  27  PHE B O   1 
ATOM   2377 C  CB  . PHE B 1 27  ? 34.214  6.269   19.315  1.00 17.97  ?  27  PHE B CB  1 
ATOM   2378 C  CG  . PHE B 1 27  ? 32.981  5.384   19.242  1.00 18.07  ?  27  PHE B CG  1 
ATOM   2379 C  CD1 . PHE B 1 27  ? 33.058  4.029   19.527  1.00 18.64  ?  27  PHE B CD1 1 
ATOM   2380 C  CD2 . PHE B 1 27  ? 31.769  5.898   18.848  1.00 19.45  ?  27  PHE B CD2 1 
ATOM   2381 C  CE1 . PHE B 1 27  ? 31.940  3.227   19.499  1.00 20.26  ?  27  PHE B CE1 1 
ATOM   2382 C  CE2 . PHE B 1 27  ? 30.651  5.086   18.822  1.00 20.66  ?  27  PHE B CE2 1 
ATOM   2383 C  CZ  . PHE B 1 27  ? 30.734  3.771   19.194  1.00 19.03  ?  27  PHE B CZ  1 
ATOM   2384 N  N   . ASP B 1 28  ? 36.890  7.013   21.571  1.00 18.09  ?  28  ASP B N   1 
ATOM   2385 C  CA  . ASP B 1 28  ? 38.136  7.772   21.689  1.00 21.86  ?  28  ASP B CA  1 
ATOM   2386 C  C   . ASP B 1 28  ? 39.060  7.458   20.528  1.00 24.09  ?  28  ASP B C   1 
ATOM   2387 O  O   . ASP B 1 28  ? 39.981  8.222   20.290  1.00 27.87  ?  28  ASP B O   1 
ATOM   2388 C  CB  . ASP B 1 28  ? 38.827  7.520   23.024  1.00 20.28  ?  28  ASP B CB  1 
ATOM   2389 C  CG  . ASP B 1 28  ? 38.145  8.196   24.202  1.00 21.23  ?  28  ASP B CG  1 
ATOM   2390 O  OD1 . ASP B 1 28  ? 37.462  9.201   23.983  1.00 21.52  ?  28  ASP B OD1 1 
ATOM   2391 O  OD2 . ASP B 1 28  ? 38.310  7.718   25.324  1.00 27.09  -1 28  ASP B OD2 1 
ATOM   2392 N  N   . GLU B 1 29  ? 38.870  6.311   19.880  1.00 21.63  ?  29  GLU B N   1 
ATOM   2393 C  CA  . GLU B 1 29  ? 39.573  6.001   18.643  1.00 25.88  ?  29  GLU B CA  1 
ATOM   2394 C  C   . GLU B 1 29  ? 38.570  6.099   17.489  1.00 26.51  ?  29  GLU B C   1 
ATOM   2395 O  O   . GLU B 1 29  ? 37.425  5.657   17.621  1.00 26.54  ?  29  GLU B O   1 
ATOM   2396 C  CB  . GLU B 1 29  ? 40.083  4.559   18.614  1.00 28.24  ?  29  GLU B CB  1 
ATOM   2397 C  CG  . GLU B 1 29  ? 40.786  4.139   19.886  1.00 40.46  ?  29  GLU B CG  1 
ATOM   2398 C  CD  . GLU B 1 29  ? 42.275  4.181   19.758  1.00 51.10  ?  29  GLU B CD  1 
ATOM   2399 O  OE1 . GLU B 1 29  ? 42.786  5.223   19.269  1.00 46.88  ?  29  GLU B OE1 1 
ATOM   2400 O  OE2 . GLU B 1 29  ? 42.864  3.149   20.179  1.00 60.92  -1 29  GLU B OE2 1 
ATOM   2401 N  N   . PRO B 1 30  ? 38.956  6.639   16.321  1.00 24.55  ?  30  PRO B N   1 
ATOM   2402 C  CA  . PRO B 1 30  ? 38.005  6.792   15.210  1.00 22.80  ?  30  PRO B CA  1 
ATOM   2403 C  C   . PRO B 1 30  ? 37.391  5.472   14.743  1.00 19.10  ?  30  PRO B C   1 
ATOM   2404 O  O   . PRO B 1 30  ? 38.092  4.462   14.625  1.00 17.24  ?  30  PRO B O   1 
ATOM   2405 C  CB  . PRO B 1 30  ? 38.846  7.413   14.101  1.00 23.31  ?  30  PRO B CB  1 
ATOM   2406 C  CG  . PRO B 1 30  ? 40.115  7.919   14.801  1.00 25.72  ?  30  PRO B CG  1 
ATOM   2407 C  CD  . PRO B 1 30  ? 40.310  7.137   16.014  1.00 25.12  ?  30  PRO B CD  1 
ATOM   2408 N  N   . VAL B 1 31  ? 36.071  5.486   14.482  1.00 17.63  ?  31  VAL B N   1 
ATOM   2409 C  CA  . VAL B 1 31  ? 35.354  4.283   14.088  1.00 16.67  ?  31  VAL B CA  1 
ATOM   2410 C  C   . VAL B 1 31  ? 34.777  4.431   12.683  1.00 16.63  ?  31  VAL B C   1 
ATOM   2411 O  O   . VAL B 1 31  ? 34.629  5.523   12.150  1.00 15.58  ?  31  VAL B O   1 
ATOM   2412 C  CB  . VAL B 1 31  ? 34.237  3.918   15.077  1.00 18.13  ?  31  VAL B CB  1 
ATOM   2413 C  CG1 . VAL B 1 31  ? 34.792  3.497   16.421  1.00 19.31  ?  31  VAL B CG1 1 
ATOM   2414 C  CG2 . VAL B 1 31  ? 33.201  5.012   15.232  1.00 19.04  ?  31  VAL B CG2 1 
ATOM   2415 N  N   . VAL B 1 32  ? 34.509  3.267   12.079  1.00 16.42  ?  32  VAL B N   1 
ATOM   2416 C  CA  . VAL B 1 32  ? 33.740  3.141   10.844  1.00 15.67  ?  32  VAL B CA  1 
ATOM   2417 C  C   . VAL B 1 32  ? 32.361  2.596   11.201  1.00 14.72  ?  32  VAL B C   1 
ATOM   2418 O  O   . VAL B 1 32  ? 32.232  1.469   11.706  1.00 14.25  ?  32  VAL B O   1 
ATOM   2419 C  CB  . VAL B 1 32  ? 34.445  2.172   9.886   1.00 17.05  ?  32  VAL B CB  1 
ATOM   2420 C  CG1 . VAL B 1 32  ? 33.684  2.007   8.574   1.00 17.40  ?  32  VAL B CG1 1 
ATOM   2421 C  CG2 . VAL B 1 32  ? 35.870  2.664   9.585   1.00 20.43  ?  32  VAL B CG2 1 
ATOM   2422 N  N   . PRO B 1 33  ? 31.285  3.325   10.909  1.00 14.16  ?  33  PRO B N   1 
ATOM   2423 C  CA  . PRO B 1 33  ? 29.969  2.919   11.394  1.00 13.88  ?  33  PRO B CA  1 
ATOM   2424 C  C   . PRO B 1 33  ? 29.027  2.399   10.317  1.00 15.05  ?  33  PRO B C   1 
ATOM   2425 O  O   . PRO B 1 33  ? 29.192  2.685   9.133   1.00 16.70  ?  33  PRO B O   1 
ATOM   2426 C  CB  . PRO B 1 33  ? 29.456  4.230   11.948  1.00 14.78  ?  33  PRO B CB  1 
ATOM   2427 C  CG  . PRO B 1 33  ? 29.926  5.215   10.887  1.00 15.60  ?  33  PRO B CG  1 
ATOM   2428 C  CD  . PRO B 1 33  ? 31.261  4.699   10.375  1.00 15.67  ?  33  PRO B CD  1 
ATOM   2429 N  N   . GLY B 1 34  ? 28.034  1.635   10.782  1.00 13.19  ?  34  GLY B N   1 
ATOM   2430 C  CA  . GLY B 1 34  ? 26.960  1.107   9.971   1.00 12.28  ?  34  GLY B CA  1 
ATOM   2431 C  C   . GLY B 1 34  ? 25.695  0.979   10.807  1.00 10.75  ?  34  GLY B C   1 
ATOM   2432 O  O   . GLY B 1 34  ? 25.728  1.090   12.036  1.00 10.78  ?  34  GLY B O   1 
ATOM   2433 N  N   . VAL B 1 35  ? 24.568  0.762   10.147  1.00 11.54  ?  35  VAL B N   1 
ATOM   2434 C  CA  . VAL B 1 35  ? 23.320  0.676   10.886  1.00 12.97  ?  35  VAL B CA  1 
ATOM   2435 C  C   . VAL B 1 35  ? 22.340  -0.211  10.109  1.00 11.76  ?  35  VAL B C   1 
ATOM   2436 O  O   . VAL B 1 35  ? 22.447  -0.317  8.897   1.00 12.16  ?  35  VAL B O   1 
ATOM   2437 C  CB  . VAL B 1 35  ? 22.729  2.076   11.115  1.00 13.84  ?  35  VAL B CB  1 
ATOM   2438 C  CG1 . VAL B 1 35  ? 22.264  2.701   9.807   1.00 15.16  ?  35  VAL B CG1 1 
ATOM   2439 C  CG2 . VAL B 1 35  ? 21.574  2.035   12.118  1.00 15.07  ?  35  VAL B CG2 1 
ATOM   2440 N  N   . ASP B 1 36  ? 21.448  -0.875  10.835  1.00 11.39  ?  36  ASP B N   1 
ATOM   2441 C  CA  . ASP B 1 36  ? 20.311  -1.566  10.245  1.00 12.34  ?  36  ASP B CA  1 
ATOM   2442 C  C   . ASP B 1 36  ? 19.100  -1.343  11.144  1.00 12.05  ?  36  ASP B C   1 
ATOM   2443 O  O   . ASP B 1 36  ? 19.061  -1.820  12.288  1.00 12.74  ?  36  ASP B O   1 
ATOM   2444 C  CB  . ASP B 1 36  ? 20.592  -3.038  9.988   1.00 13.23  ?  36  ASP B CB  1 
ATOM   2445 C  CG  . ASP B 1 36  ? 19.458  -3.805  9.289   1.00 17.35  ?  36  ASP B CG  1 
ATOM   2446 O  OD1 . ASP B 1 36  ? 18.286  -3.473  9.512   1.00 18.39  ?  36  ASP B OD1 1 
ATOM   2447 O  OD2 . ASP B 1 36  ? 19.731  -4.791  8.597   1.00 19.43  -1 36  ASP B OD2 1 
ATOM   2448 N  N   . VAL B 1 37  ? 18.154  -0.582  10.608  1.00 13.01  ?  37  VAL B N   1 
ATOM   2449 C  CA  . VAL B 1 37  ? 16.899  -0.288  11.271  1.00 13.77  ?  37  VAL B CA  1 
ATOM   2450 C  C   . VAL B 1 37  ? 15.874  -1.271  10.738  1.00 14.09  ?  37  VAL B C   1 
ATOM   2451 O  O   . VAL B 1 37  ? 15.462  -1.160  9.594   1.00 15.35  ?  37  VAL B O   1 
ATOM   2452 C  CB  . VAL B 1 37  ? 16.402  1.148   11.017  1.00 14.57  ?  37  VAL B CB  1 
ATOM   2453 C  CG1 . VAL B 1 37  ? 15.097  1.376   11.774  1.00 15.75  ?  37  VAL B CG1 1 
ATOM   2454 C  CG2 . VAL B 1 37  ? 17.433  2.197   11.388  1.00 14.76  ?  37  VAL B CG2 1 
ATOM   2455 N  N   . ARG B 1 38  ? 15.531  -2.296  11.520  1.00 14.68  ?  38  ARG B N   1 
ATOM   2456 C  CA  . ARG B 1 38  ? 14.694  -3.356  11.011  1.00 16.19  ?  38  ARG B CA  1 
ATOM   2457 C  C   . ARG B 1 38  ? 13.270  -3.273  11.554  1.00 16.60  ?  38  ARG B C   1 
ATOM   2458 O  O   . ARG B 1 38  ? 12.370  -3.807  10.933  1.00 18.07  ?  38  ARG B O   1 
ATOM   2459 C  CB  . ARG B 1 38  ? 15.353  -4.665  11.417  1.00 17.04  ?  38  ARG B CB  1 
ATOM   2460 C  CG  . ARG B 1 38  ? 14.743  -5.898  10.785  1.00 18.63  ?  38  ARG B CG  1 
ATOM   2461 C  CD  . ARG B 1 38  ? 15.106  -6.008  9.323   1.00 19.81  ?  38  ARG B CD  1 
ATOM   2462 N  NE  . ARG B 1 38  ? 16.556  -6.224  9.137   1.00 20.51  ?  38  ARG B NE  1 
ATOM   2463 C  CZ  . ARG B 1 38  ? 17.230  -7.346  9.332   1.00 20.48  ?  38  ARG B CZ  1 
ATOM   2464 N  NH1 . ARG B 1 38  ? 16.594  -8.478  9.642   1.00 21.46  1  38  ARG B NH1 1 
ATOM   2465 N  NH2 . ARG B 1 38  ? 18.554  -7.343  9.197   1.00 20.74  ?  38  ARG B NH2 1 
ATOM   2466 N  N   . GLY B 1 39  ? 13.068  -2.649  12.724  1.00 15.06  ?  39  GLY B N   1 
ATOM   2467 C  CA  . GLY B 1 39  ? 11.731  -2.574  13.286  1.00 15.31  ?  39  GLY B CA  1 
ATOM   2468 C  C   . GLY B 1 39  ? 10.865  -1.596  12.494  1.00 15.82  ?  39  GLY B C   1 
ATOM   2469 O  O   . GLY B 1 39  ? 11.381  -0.762  11.762  1.00 16.94  ?  39  GLY B O   1 
ATOM   2470 N  N   . ALA B 1 40  ? 9.541   -1.730  12.609  1.00 14.81  ?  40  ALA B N   1 
ATOM   2471 C  CA  . ALA B 1 40  ? 8.635   -0.897  11.833  1.00 17.54  ?  40  ALA B CA  1 
ATOM   2472 C  C   . ALA B 1 40  ? 8.239   0.385   12.571  1.00 17.13  ?  40  ALA B C   1 
ATOM   2473 O  O   . ALA B 1 40  ? 7.500   1.183   12.023  1.00 18.26  ?  40  ALA B O   1 
ATOM   2474 C  CB  . ALA B 1 40  ? 7.399   -1.706  11.486  1.00 19.05  ?  40  ALA B CB  1 
ATOM   2475 N  N   . ASN B 1 41  ? 8.745   0.598   13.804  1.00 15.83  ?  41  ASN B N   1 
ATOM   2476 C  CA  . ASN B 1 41  ? 8.339   1.746   14.588  1.00 17.46  ?  41  ASN B CA  1 
ATOM   2477 C  C   . ASN B 1 41  ? 9.559   2.362   15.278  1.00 17.12  ?  41  ASN B C   1 
ATOM   2478 O  O   . ASN B 1 41  ? 9.570   2.425   16.511  1.00 17.78  ?  41  ASN B O   1 
ATOM   2479 C  CB  . ASN B 1 41  ? 7.298   1.267   15.603  1.00 20.74  ?  41  ASN B CB  1 
ATOM   2480 C  CG  . ASN B 1 41  ? 6.446   2.387   16.142  1.00 31.67  ?  41  ASN B CG  1 
ATOM   2481 O  OD1 . ASN B 1 41  ? 6.759   3.567   15.979  1.00 24.87  ?  41  ASN B OD1 1 
ATOM   2482 N  ND2 . ASN B 1 41  ? 5.326   2.029   16.759  1.00 45.27  ?  41  ASN B ND2 1 
ATOM   2483 N  N   . ALA B 1 42  ? 10.594  2.722   14.515  1.00 13.46  ?  42  ALA B N   1 
ATOM   2484 C  CA  . ALA B 1 42  ? 11.847  3.214   15.085  1.00 15.81  ?  42  ALA B CA  1 
ATOM   2485 C  C   . ALA B 1 42  ? 11.881  4.747   15.076  1.00 17.37  ?  42  ALA B C   1 
ATOM   2486 O  O   . ALA B 1 42  ? 11.349  5.369   14.165  1.00 20.66  ?  42  ALA B O   1 
ATOM   2487 C  CB  . ALA B 1 42  ? 13.021  2.670   14.278  1.00 16.23  ?  42  ALA B CB  1 
ATOM   2488 N  N   . ALA B 1 43  ? 12.489  5.354   16.092  1.00 14.21  ?  43  ALA B N   1 
ATOM   2489 C  CA  . ALA B 1 43  ? 12.782  6.783   16.081  1.00 12.35  ?  43  ALA B CA  1 
ATOM   2490 C  C   . ALA B 1 43  ? 14.275  6.937   16.302  1.00 11.64  ?  43  ALA B C   1 
ATOM   2491 O  O   . ALA B 1 43  ? 14.791  6.469   17.308  1.00 11.81  ?  43  ALA B O   1 
ATOM   2492 C  CB  . ALA B 1 43  ? 11.984  7.498   17.144  1.00 12.38  ?  43  ALA B CB  1 
ATOM   2493 N  N   . THR B 1 44  ? 14.954  7.555   15.332  1.00 11.89  ?  44  THR B N   1 
ATOM   2494 C  CA  . THR B 1 44  ? 16.398  7.671   15.344  1.00 11.72  ?  44  THR B CA  1 
ATOM   2495 C  C   . THR B 1 44  ? 16.797  9.067   14.881  1.00 10.94  ?  44  THR B C   1 
ATOM   2496 O  O   . THR B 1 44  ? 16.013  9.822   14.317  1.00 10.98  ?  44  THR B O   1 
ATOM   2497 C  CB  . THR B 1 44  ? 17.049  6.606   14.435  1.00 13.64  ?  44  THR B CB  1 
ATOM   2498 O  OG1 . THR B 1 44  ? 16.772  6.923   13.082  1.00 13.70  ?  44  THR B OG1 1 
ATOM   2499 C  CG2 . THR B 1 44  ? 16.528  5.207   14.701  1.00 13.19  ?  44  THR B CG2 1 
ATOM   2500 N  N   . ILE B 1 45  ? 18.075  9.361   15.058  1.00 10.45  ?  45  ILE B N   1 
ATOM   2501 C  CA  . ILE B 1 45  ? 18.668  10.608  14.591  1.00 11.22  ?  45  ILE B CA  1 
ATOM   2502 C  C   . ILE B 1 45  ? 20.056  10.328  14.017  1.00 11.12  ?  45  ILE B C   1 
ATOM   2503 O  O   . ILE B 1 45  ? 20.745  9.421   14.500  1.00 11.31  ?  45  ILE B O   1 
ATOM   2504 C  CB  . ILE B 1 45  ? 18.730  11.612  15.756  1.00 11.42  ?  45  ILE B CB  1 
ATOM   2505 C  CG1 . ILE B 1 45  ? 19.131  13.012  15.261  1.00 11.99  ?  45  ILE B CG1 1 
ATOM   2506 C  CG2 . ILE B 1 45  ? 19.639  11.118  16.885  1.00 11.91  ?  45  ILE B CG2 1 
ATOM   2507 C  CD1 . ILE B 1 45  ? 19.108  14.061  16.350  1.00 13.56  ?  45  ILE B CD1 1 
ATOM   2508 N  N   . TYR B 1 46  ? 20.384  11.047  12.922  1.00 12.27  ?  46  TYR B N   1 
ATOM   2509 C  CA  . TYR B 1 46  ? 21.684  11.014  12.249  1.00 12.32  ?  46  TYR B CA  1 
ATOM   2510 C  C   . TYR B 1 46  ? 21.974  9.670   11.578  1.00 16.14  ?  46  TYR B C   1 
ATOM   2511 O  O   . TYR B 1 46  ? 23.140  9.414   11.286  1.00 19.45  ?  46  TYR B O   1 
ATOM   2512 C  CB  . TYR B 1 46  ? 22.864  11.347  13.172  1.00 12.60  ?  46  TYR B CB  1 
ATOM   2513 C  CG  . TYR B 1 46  ? 22.781  12.699  13.878  1.00 13.02  ?  46  TYR B CG  1 
ATOM   2514 C  CD1 . TYR B 1 46  ? 22.602  13.892  13.154  1.00 13.06  ?  46  TYR B CD1 1 
ATOM   2515 C  CD2 . TYR B 1 46  ? 22.942  12.799  15.246  1.00 12.51  ?  46  TYR B CD2 1 
ATOM   2516 C  CE1 . TYR B 1 46  ? 22.507  15.114  13.807  1.00 13.40  ?  46  TYR B CE1 1 
ATOM   2517 C  CE2 . TYR B 1 46  ? 22.865  14.016  15.904  1.00 14.05  ?  46  TYR B CE2 1 
ATOM   2518 C  CZ  . TYR B 1 46  ? 22.669  15.183  15.185  1.00 15.05  ?  46  TYR B CZ  1 
ATOM   2519 O  OH  . TYR B 1 46  ? 22.558  16.374  15.856  1.00 16.63  ?  46  TYR B OH  1 
ATOM   2520 N  N   . THR B 1 47  ? 20.984  8.816   11.308  1.00 13.34  ?  47  THR B N   1 
ATOM   2521 C  CA  . THR B 1 47  ? 21.317  7.518   10.713  1.00 15.50  ?  47  THR B CA  1 
ATOM   2522 C  C   . THR B 1 47  ? 21.701  7.606   9.230   1.00 16.62  ?  47  THR B C   1 
ATOM   2523 O  O   . THR B 1 47  ? 22.364  6.700   8.736   1.00 14.22  ?  47  THR B O   1 
ATOM   2524 C  CB  . THR B 1 47  ? 20.201  6.499   10.904  1.00 16.87  ?  47  THR B CB  1 
ATOM   2525 O  OG1 . THR B 1 47  ? 19.042  6.971   10.234  1.00 16.60  ?  47  THR B OG1 1 
ATOM   2526 C  CG2 . THR B 1 47  ? 19.994  6.149   12.361  1.00 18.64  ?  47  THR B CG2 1 
ATOM   2527 N  N   . ASP B 1 48  ? 21.382  8.685   8.483   1.00 17.05  ?  48  ASP B N   1 
ATOM   2528 C  CA  . ASP B 1 48  ? 21.673  8.653   7.050   1.00 17.30  ?  48  ASP B CA  1 
ATOM   2529 C  C   . ASP B 1 48  ? 23.172  8.621   6.745   1.00 17.97  ?  48  ASP B C   1 
ATOM   2530 O  O   . ASP B 1 48  ? 23.594  8.090   5.720   1.00 17.27  ?  48  ASP B O   1 
ATOM   2531 C  CB  . ASP B 1 48  ? 21.063  9.793   6.266   1.00 19.79  ?  48  ASP B CB  1 
ATOM   2532 C  CG  . ASP B 1 48  ? 19.551  9.843   6.352   1.00 23.47  ?  48  ASP B CG  1 
ATOM   2533 O  OD1 . ASP B 1 48  ? 18.912  8.971   5.728   1.00 20.46  ?  48  ASP B OD1 1 
ATOM   2534 O  OD2 . ASP B 1 48  ? 19.063  10.707  7.128   1.00 24.81  -1 48  ASP B OD2 1 
ATOM   2535 N  N   . LEU B 1 49  ? 23.973  9.216   7.615   1.00 15.71  ?  49  LEU B N   1 
ATOM   2536 C  CA  . LEU B 1 49  ? 25.422  9.224   7.472   1.00 17.87  ?  49  LEU B CA  1 
ATOM   2537 C  C   . LEU B 1 49  ? 26.044  7.873   7.777   1.00 17.17  ?  49  LEU B C   1 
ATOM   2538 O  O   . LEU B 1 49  ? 27.246  7.727   7.604   1.00 20.59  ?  49  LEU B O   1 
ATOM   2539 C  CB  . LEU B 1 49  ? 25.962  10.298  8.415   1.00 21.58  ?  49  LEU B CB  1 
ATOM   2540 C  CG  . LEU B 1 49  ? 25.650  11.730  7.963   1.00 26.46  ?  49  LEU B CG  1 
ATOM   2541 C  CD1 . LEU B 1 49  ? 25.823  12.787  9.052   1.00 29.68  ?  49  LEU B CD1 1 
ATOM   2542 C  CD2 . LEU B 1 49  ? 26.531  12.042  6.772   1.00 27.96  ?  49  LEU B CD2 1 
ATOM   2543 N  N   . LEU B 1 50  ? 25.253  6.919   8.258   1.00 15.84  ?  50  LEU B N   1 
ATOM   2544 C  CA  A LEU B 1 50  ? 25.772  5.621   8.658   0.50 17.43  ?  50  LEU B CA  1 
ATOM   2545 C  CA  B LEU B 1 50  ? 25.798  5.632   8.643   0.50 15.98  ?  50  LEU B CA  1 
ATOM   2546 C  C   . LEU B 1 50  ? 25.555  4.576   7.560   1.00 18.35  ?  50  LEU B C   1 
ATOM   2547 O  O   . LEU B 1 50  ? 25.791  3.402   7.779   1.00 23.34  ?  50  LEU B O   1 
ATOM   2548 C  CB  A LEU B 1 50  ? 25.112  5.203   9.970   0.50 17.53  ?  50  LEU B CB  1 
ATOM   2549 C  CB  B LEU B 1 50  ? 25.136  5.271   9.964   0.50 14.26  ?  50  LEU B CB  1 
ATOM   2550 C  CG  A LEU B 1 50  ? 25.814  5.667   11.249  0.50 18.24  ?  50  LEU B CG  1 
ATOM   2551 C  CG  B LEU B 1 50  ? 25.153  6.354   11.044  0.50 12.89  ?  50  LEU B CG  1 
ATOM   2552 C  CD1 A LEU B 1 50  ? 25.887  7.166   11.202  0.50 18.02  ?  50  LEU B CD1 1 
ATOM   2553 C  CD1 B LEU B 1 50  ? 24.368  5.775   12.213  0.50 13.69  ?  50  LEU B CD1 1 
ATOM   2554 C  CD2 A LEU B 1 50  ? 25.165  5.175   12.527  0.50 18.19  ?  50  LEU B CD2 1 
ATOM   2555 C  CD2 B LEU B 1 50  ? 26.606  6.722   11.405  0.50 12.37  ?  50  LEU B CD2 1 
ATOM   2556 N  N   . TYR B 1 51  ? 25.035  4.975   6.404   1.00 16.85  ?  51  TYR B N   1 
ATOM   2557 C  CA  . TYR B 1 51  ? 24.875  4.010   5.332   1.00 17.49  ?  51  TYR B CA  1 
ATOM   2558 C  C   . TYR B 1 51  ? 26.084  4.042   4.418   1.00 16.59  ?  51  TYR B C   1 
ATOM   2559 O  O   . TYR B 1 51  ? 26.783  5.050   4.343   1.00 17.15  ?  51  TYR B O   1 
ATOM   2560 C  CB  . TYR B 1 51  ? 23.614  4.300   4.515   1.00 17.53  ?  51  TYR B CB  1 
ATOM   2561 C  CG  . TYR B 1 51  ? 22.374  4.006   5.336   1.00 19.39  ?  51  TYR B CG  1 
ATOM   2562 C  CD1 . TYR B 1 51  ? 21.926  2.708   5.519   1.00 22.11  ?  51  TYR B CD1 1 
ATOM   2563 C  CD2 . TYR B 1 51  ? 21.677  5.025   5.958   1.00 19.75  ?  51  TYR B CD2 1 
ATOM   2564 C  CE1 . TYR B 1 51  ? 20.774  2.439   6.236   1.00 24.63  ?  51  TYR B CE1 1 
ATOM   2565 C  CE2 . TYR B 1 51  ? 20.537  4.771   6.703   1.00 21.63  ?  51  TYR B CE2 1 
ATOM   2566 C  CZ  . TYR B 1 51  ? 20.077  3.477   6.830   1.00 22.66  ?  51  TYR B CZ  1 
ATOM   2567 O  OH  . TYR B 1 51  ? 18.957  3.201   7.538   1.00 25.02  ?  51  TYR B OH  1 
ATOM   2568 N  N   . PRO B 1 52  ? 26.302  2.989   3.611   1.00 17.58  ?  52  PRO B N   1 
ATOM   2569 C  CA  . PRO B 1 52  ? 27.525  2.900   2.817   1.00 20.88  ?  52  PRO B CA  1 
ATOM   2570 C  C   . PRO B 1 52  ? 27.669  3.933   1.702   1.00 20.13  ?  52  PRO B C   1 
ATOM   2571 O  O   . PRO B 1 52  ? 28.791  4.250   1.306   1.00 23.99  ?  52  PRO B O   1 
ATOM   2572 C  CB  . PRO B 1 52  ? 27.447  1.500   2.204   1.00 22.82  ?  52  PRO B CB  1 
ATOM   2573 C  CG  . PRO B 1 52  ? 26.404  0.757   3.020   1.00 23.62  ?  52  PRO B CG  1 
ATOM   2574 C  CD  . PRO B 1 52  ? 25.442  1.798   3.483   1.00 21.95  ?  52  PRO B CD  1 
ATOM   2575 N  N   . ASP B 1 53  ? 26.552  4.421   1.170   1.00 19.59  ?  53  ASP B N   1 
ATOM   2576 C  CA  . ASP B 1 53  ? 26.608  5.410   0.090   1.00 25.18  ?  53  ASP B CA  1 
ATOM   2577 C  C   . ASP B 1 53  ? 26.666  6.859   0.594   1.00 24.45  ?  53  ASP B C   1 
ATOM   2578 O  O   . ASP B 1 53  ? 26.652  7.770   -0.226  1.00 31.20  ?  53  ASP B O   1 
ATOM   2579 C  CB  . ASP B 1 53  ? 25.459  5.256   -0.894  1.00 27.01  ?  53  ASP B CB  1 
ATOM   2580 C  CG  . ASP B 1 53  ? 24.068  5.278   -0.301  1.00 33.44  ?  53  ASP B CG  1 
ATOM   2581 O  OD1 . ASP B 1 53  ? 23.950  5.084   0.929   1.00 37.00  ?  53  ASP B OD1 1 
ATOM   2582 O  OD2 . ASP B 1 53  ? 23.114  5.482   -1.071  1.00 48.05  -1 53  ASP B OD2 1 
ATOM   2583 N  N   . SER B 1 54  ? 26.811  7.072   1.906   1.00 17.77  ?  54  SER B N   1 
ATOM   2584 C  CA  . SER B 1 54  ? 27.035  8.386   2.481   1.00 17.53  ?  54  SER B CA  1 
ATOM   2585 C  C   . SER B 1 54  ? 28.535  8.548   2.706   1.00 18.95  ?  54  SER B C   1 
ATOM   2586 O  O   . SER B 1 54  ? 29.227  7.552   2.770   1.00 20.71  ?  54  SER B O   1 
ATOM   2587 C  CB  . SER B 1 54  ? 26.282  8.544   3.780   1.00 19.47  ?  54  SER B CB  1 
ATOM   2588 O  OG  . SER B 1 54  ? 24.901  8.723   3.515   1.00 26.53  ?  54  SER B OG  1 
ATOM   2589 N  N   . VAL B 1 55  ? 28.994  9.782   2.892   1.00 16.48  ?  55  VAL B N   1 
ATOM   2590 C  CA  . VAL B 1 55  ? 30.380  10.066  3.234   1.00 20.28  ?  55  VAL B CA  1 
ATOM   2591 C  C   . VAL B 1 55  ? 30.729  9.447   4.587   1.00 20.58  ?  55  VAL B C   1 
ATOM   2592 O  O   . VAL B 1 55  ? 29.851  9.058   5.361   1.00 18.44  ?  55  VAL B O   1 
ATOM   2593 C  CB  . VAL B 1 55  ? 30.672  11.571  3.271   1.00 23.76  ?  55  VAL B CB  1 
ATOM   2594 C  CG1 . VAL B 1 55  ? 30.393  12.193  1.916   1.00 26.24  ?  55  VAL B CG1 1 
ATOM   2595 C  CG2 . VAL B 1 55  ? 29.908  12.299  4.374   1.00 25.85  ?  55  VAL B CG2 1 
ATOM   2596 N  N   . MET B 1 56  ? 32.028  9.405   4.882   1.00 21.04  ?  56  MET B N   1 
ATOM   2597 C  CA  . MET B 1 56  ? 32.509  8.859   6.146   1.00 22.84  ?  56  MET B CA  1 
ATOM   2598 C  C   . MET B 1 56  ? 32.331  9.946   7.189   1.00 23.78  ?  56  MET B C   1 
ATOM   2599 O  O   . MET B 1 56  ? 32.950  11.008  7.095   1.00 24.69  ?  56  MET B O   1 
ATOM   2600 C  CB  . MET B 1 56  ? 33.991  8.491   6.080   1.00 22.87  ?  56  MET B CB  1 
ATOM   2601 C  CG  . MET B 1 56  ? 34.534  7.947   7.390   1.00 27.17  ?  56  MET B CG  1 
ATOM   2602 S  SD  . MET B 1 56  ? 33.914  6.291   7.779   1.00 29.60  ?  56  MET B SD  1 
ATOM   2603 C  CE  . MET B 1 56  ? 34.811  5.345   6.538   1.00 35.68  ?  56  MET B CE  1 
ATOM   2604 N  N   . PRO B 1 57  ? 31.420  9.785   8.178   1.00 21.65  ?  57  PRO B N   1 
ATOM   2605 C  CA  . PRO B 1 57  ? 31.264  10.814  9.200   1.00 20.59  ?  57  PRO B CA  1 
ATOM   2606 C  C   . PRO B 1 57  ? 32.326  10.684  10.288  1.00 20.24  ?  57  PRO B C   1 
ATOM   2607 O  O   . PRO B 1 57  ? 33.112  9.734   10.290  1.00 21.68  ?  57  PRO B O   1 
ATOM   2608 C  CB  . PRO B 1 57  ? 29.899  10.526  9.784   1.00 20.72  ?  57  PRO B CB  1 
ATOM   2609 C  CG  . PRO B 1 57  ? 29.828  8.997   9.650   1.00 22.02  ?  57  PRO B CG  1 
ATOM   2610 C  CD  . PRO B 1 57  ? 30.575  8.603   8.411   1.00 23.68  ?  57  PRO B CD  1 
ATOM   2611 N  N   . SER B 1 58  ? 32.337  11.661  11.186  1.00 21.17  ?  58  SER B N   1 
ATOM   2612 C  CA  . SER B 1 58  ? 33.119  11.569  12.409  1.00 25.08  ?  58  SER B CA  1 
ATOM   2613 C  C   . SER B 1 58  ? 32.184  11.285  13.592  1.00 20.14  ?  58  SER B C   1 
ATOM   2614 O  O   . SER B 1 58  ? 31.662  12.197  14.208  1.00 19.39  ?  58  SER B O   1 
ATOM   2615 C  CB  . SER B 1 58  ? 33.950  12.821  12.598  1.00 27.09  ?  58  SER B CB  1 
ATOM   2616 O  OG  . SER B 1 58  ? 34.727  12.685  13.778  1.00 35.13  ?  58  SER B OG  1 
ATOM   2617 N  N   . VAL B 1 59  ? 31.938  10.003  13.876  1.00 17.86  ?  59  VAL B N   1 
ATOM   2618 C  CA  . VAL B 1 59  ? 31.016  9.638   14.948  1.00 16.71  ?  59  VAL B CA  1 
ATOM   2619 C  C   . VAL B 1 59  ? 31.706  9.773   16.302  1.00 15.77  ?  59  VAL B C   1 
ATOM   2620 O  O   . VAL B 1 59  ? 32.677  9.085   16.579  1.00 16.67  ?  59  VAL B O   1 
ATOM   2621 C  CB  . VAL B 1 59  ? 30.457  8.215   14.732  1.00 18.34  ?  59  VAL B CB  1 
ATOM   2622 C  CG1 . VAL B 1 59  ? 29.627  7.732   15.901  1.00 18.12  ?  59  VAL B CG1 1 
ATOM   2623 C  CG2 . VAL B 1 59  ? 29.611  8.165   13.477  1.00 19.69  ?  59  VAL B CG2 1 
ATOM   2624 N  N   . THR B 1 60  ? 31.164  10.653  17.145  1.00 15.84  ?  60  THR B N   1 
ATOM   2625 C  CA  . THR B 1 60  ? 31.738  10.973  18.432  1.00 17.13  ?  60  THR B CA  1 
ATOM   2626 C  C   . THR B 1 60  ? 31.284  9.943   19.469  1.00 17.45  ?  60  THR B C   1 
ATOM   2627 O  O   . THR B 1 60  ? 32.049  9.530   20.329  1.00 14.02  ?  60  THR B O   1 
ATOM   2628 C  CB  . THR B 1 60  ? 31.300  12.385  18.819  1.00 21.58  ?  60  THR B CB  1 
ATOM   2629 O  OG1 . THR B 1 60  ? 31.317  13.243  17.677  1.00 23.51  ?  60  THR B OG1 1 
ATOM   2630 C  CG2 . THR B 1 60  ? 32.283  12.961  19.815  1.00 25.24  ?  60  THR B CG2 1 
ATOM   2631 N  N   . GLY B 1 61  ? 29.997  9.569   19.417  1.00 14.39  ?  61  GLY B N   1 
ATOM   2632 C  CA  . GLY B 1 61  ? 29.450  8.557   20.289  1.00 14.24  ?  61  GLY B CA  1 
ATOM   2633 C  C   . GLY B 1 61  ? 28.119  8.078   19.693  1.00 14.16  ?  61  GLY B C   1 
ATOM   2634 O  O   . GLY B 1 61  ? 27.645  8.674   18.742  1.00 12.98  ?  61  GLY B O   1 
ATOM   2635 N  N   . ILE B 1 62  ? 27.553  7.021   20.261  1.00 12.92  ?  62  ILE B N   1 
ATOM   2636 C  CA  . ILE B 1 62  ? 26.220  6.540   19.896  1.00 13.20  ?  62  ILE B CA  1 
ATOM   2637 C  C   . ILE B 1 62  ? 25.456  6.359   21.199  1.00 12.63  ?  62  ILE B C   1 
ATOM   2638 O  O   . ILE B 1 62  ? 25.988  5.777   22.146  1.00 13.36  ?  62  ILE B O   1 
ATOM   2639 C  CB  . ILE B 1 62  ? 26.330  5.221   19.084  1.00 13.38  ?  62  ILE B CB  1 
ATOM   2640 C  CG1 . ILE B 1 62  ? 26.964  5.478   17.745  1.00 14.34  ?  62  ILE B CG1 1 
ATOM   2641 C  CG2 . ILE B 1 62  ? 24.938  4.577   18.892  1.00 14.16  ?  62  ILE B CG2 1 
ATOM   2642 C  CD1 . ILE B 1 62  ? 27.306  4.239   16.949  1.00 16.20  ?  62  ILE B CD1 1 
ATOM   2643 N  N   . MET B 1 63  ? 24.178  6.758   21.195  1.00 12.47  ?  63  MET B N   1 
ATOM   2644 C  CA  . MET B 1 63  ? 23.346  6.770   22.365  1.00 12.92  ?  63  MET B CA  1 
ATOM   2645 C  C   . MET B 1 63  ? 22.127  5.849   22.204  1.00 14.85  ?  63  MET B C   1 
ATOM   2646 O  O   . MET B 1 63  ? 21.491  5.782   21.151  1.00 13.21  ?  63  MET B O   1 
ATOM   2647 C  CB  . MET B 1 63  ? 22.894  8.207   22.659  1.00 15.25  ?  63  MET B CB  1 
ATOM   2648 C  CG  . MET B 1 63  ? 22.021  8.286   23.878  1.00 18.34  ?  63  MET B CG  1 
ATOM   2649 S  SD  . MET B 1 63  ? 21.598  9.982   24.283  1.00 22.58  ?  63  MET B SD  1 
ATOM   2650 C  CE  . MET B 1 63  ? 23.198  10.432  24.962  1.00 22.24  ?  63  MET B CE  1 
ATOM   2651 N  N   . LEU B 1 64  ? 21.829  5.110   23.295  1.00 13.85  ?  64  LEU B N   1 
ATOM   2652 C  CA  . LEU B 1 64  ? 20.591  4.358   23.438  1.00 13.80  ?  64  LEU B CA  1 
ATOM   2653 C  C   . LEU B 1 64  ? 19.809  5.033   24.553  1.00 13.57  ?  64  LEU B C   1 
ATOM   2654 O  O   . LEU B 1 64  ? 20.299  5.077   25.684  1.00 14.57  ?  64  LEU B O   1 
ATOM   2655 C  CB  . LEU B 1 64  ? 20.952  2.919   23.772  1.00 14.53  ?  64  LEU B CB  1 
ATOM   2656 C  CG  . LEU B 1 64  ? 21.996  2.240   22.859  1.00 16.07  ?  64  LEU B CG  1 
ATOM   2657 C  CD1 . LEU B 1 64  ? 22.362  0.869   23.418  1.00 18.83  ?  64  LEU B CD1 1 
ATOM   2658 C  CD2 . LEU B 1 64  ? 21.547  2.077   21.467  1.00 15.61  ?  64  LEU B CD2 1 
ATOM   2659 N  N   . THR B 1 65  ? 18.609  5.526   24.266  1.00 12.72  ?  65  THR B N   1 
ATOM   2660 C  CA  . THR B 1 65  ? 17.899  6.321   25.250  1.00 14.98  ?  65  THR B CA  1 
ATOM   2661 C  C   . THR B 1 65  ? 16.461  5.867   25.364  1.00 15.34  ?  65  THR B C   1 
ATOM   2662 O  O   . THR B 1 65  ? 15.887  5.386   24.386  1.00 15.53  ?  65  THR B O   1 
ATOM   2663 C  CB  . THR B 1 65  ? 18.014  7.794   24.844  1.00 17.09  ?  65  THR B CB  1 
ATOM   2664 O  OG1 . THR B 1 65  ? 17.343  8.538   25.843  1.00 16.29  ?  65  THR B OG1 1 
ATOM   2665 C  CG2 . THR B 1 65  ? 17.352  8.093   23.506  1.00 16.84  ?  65  THR B CG2 1 
ATOM   2666 N  N   . GLY B 1 66  ? 15.889  6.084   26.551  1.00 15.09  ?  66  GLY B N   1 
ATOM   2667 C  CA  . GLY B 1 66  ? 14.453  6.062   26.716  1.00 15.18  ?  66  GLY B CA  1 
ATOM   2668 C  C   . GLY B 1 66  ? 13.802  7.381   26.320  1.00 16.90  ?  66  GLY B C   1 
ATOM   2669 O  O   . GLY B 1 66  ? 14.416  8.267   25.726  1.00 16.18  ?  66  GLY B O   1 
ATOM   2670 N  N   . GLY B 1 67  ? 12.518  7.496   26.661  1.00 15.29  ?  67  GLY B N   1 
ATOM   2671 C  CA  . GLY B 1 67  ? 11.770  8.708   26.431  1.00 15.45  ?  67  GLY B CA  1 
ATOM   2672 C  C   . GLY B 1 67  ? 10.990  8.738   25.136  1.00 13.94  ?  67  GLY B C   1 
ATOM   2673 O  O   . GLY B 1 67  ? 10.435  9.770   24.790  1.00 14.67  ?  67  GLY B O   1 
ATOM   2674 N  N   . SER B 1 68  ? 10.904  7.608   24.418  1.00 15.15  ?  68  SER B N   1 
ATOM   2675 C  CA  . SER B 1 68  ? 10.258  7.598   23.116  1.00 15.71  ?  68  SER B CA  1 
ATOM   2676 C  C   . SER B 1 68  ? 10.829  8.717   22.236  1.00 15.17  ?  68  SER B C   1 
ATOM   2677 O  O   . SER B 1 68  ? 11.998  9.060   22.345  1.00 16.04  ?  68  SER B O   1 
ATOM   2678 C  CB  . SER B 1 68  ? 8.728   7.645   23.281  1.00 16.47  ?  68  SER B CB  1 
ATOM   2679 O  OG  . SER B 1 68  ? 8.072   7.510   22.030  1.00 15.55  ?  68  SER B OG  1 
ATOM   2680 N  N   . ALA B 1 69  ? 10.010  9.338   21.392  1.00 14.10  ?  69  ALA B N   1 
ATOM   2681 C  CA  . ALA B 1 69  ? 10.495  10.339  20.463  1.00 15.58  ?  69  ALA B CA  1 
ATOM   2682 C  C   . ALA B 1 69  ? 11.155  11.520  21.188  1.00 17.74  ?  69  ALA B C   1 
ATOM   2683 O  O   . ALA B 1 69  ? 12.012  12.202  20.614  1.00 18.11  ?  69  ALA B O   1 
ATOM   2684 C  CB  . ALA B 1 69  ? 9.345   10.836  19.583  1.00 16.70  ?  69  ALA B CB  1 
ATOM   2685 N  N   . PHE B 1 70  ? 10.687  11.817  22.416  1.00 15.45  ?  70  PHE B N   1 
ATOM   2686 C  CA  . PHE B 1 70  ? 11.223  12.928  23.201  1.00 15.85  ?  70  PHE B CA  1 
ATOM   2687 C  C   . PHE B 1 70  ? 12.692  12.735  23.534  1.00 13.69  ?  70  PHE B C   1 
ATOM   2688 O  O   . PHE B 1 70  ? 13.452  13.703  23.601  1.00 15.64  ?  70  PHE B O   1 
ATOM   2689 C  CB  . PHE B 1 70  ? 10.463  13.108  24.515  1.00 17.16  ?  70  PHE B CB  1 
ATOM   2690 C  CG  . PHE B 1 70  ? 8.975   13.296  24.308  1.00 16.05  ?  70  PHE B CG  1 
ATOM   2691 C  CD1 . PHE B 1 70  ? 8.475   14.509  23.855  1.00 18.28  ?  70  PHE B CD1 1 
ATOM   2692 C  CD2 . PHE B 1 70  ? 8.078   12.284  24.643  1.00 18.52  ?  70  PHE B CD2 1 
ATOM   2693 C  CE1 . PHE B 1 70  ? 7.110   14.688  23.717  1.00 18.43  ?  70  PHE B CE1 1 
ATOM   2694 C  CE2 . PHE B 1 70  ? 6.709   12.482  24.488  1.00 20.24  ?  70  PHE B CE2 1 
ATOM   2695 C  CZ  . PHE B 1 70  ? 6.246   13.663  23.994  1.00 18.64  ?  70  PHE B CZ  1 
ATOM   2696 N  N   . GLY B 1 71  ? 13.123  11.479  23.686  1.00 13.00  ?  71  GLY B N   1 
ATOM   2697 C  CA  . GLY B 1 71  ? 14.433  11.189  24.254  1.00 12.89  ?  71  GLY B CA  1 
ATOM   2698 C  C   . GLY B 1 71  ? 15.606  11.494  23.339  1.00 13.31  ?  71  GLY B C   1 
ATOM   2699 O  O   . GLY B 1 71  ? 16.767  11.516  23.813  1.00 13.75  ?  71  GLY B O   1 
ATOM   2700 N  N   . LEU B 1 72  ? 15.343  11.685  22.021  1.00 12.59  ?  72  LEU B N   1 
ATOM   2701 C  CA  . LEU B 1 72  ? 16.412  12.119  21.126  1.00 12.89  ?  72  LEU B CA  1 
ATOM   2702 C  C   . LEU B 1 72  ? 16.995  13.481  21.540  1.00 13.50  ?  72  LEU B C   1 
ATOM   2703 O  O   . LEU B 1 72  ? 18.093  13.822  21.125  1.00 13.46  ?  72  LEU B O   1 
ATOM   2704 C  CB  . LEU B 1 72  ? 15.963  12.123  19.669  1.00 12.90  ?  72  LEU B CB  1 
ATOM   2705 C  CG  . LEU B 1 72  ? 15.591  10.728  19.138  1.00 13.42  ?  72  LEU B CG  1 
ATOM   2706 C  CD1 . LEU B 1 72  ? 15.046  10.867  17.751  1.00 15.59  ?  72  LEU B CD1 1 
ATOM   2707 C  CD2 . LEU B 1 72  ? 16.739  9.808   19.136  1.00 14.81  ?  72  LEU B CD2 1 
ATOM   2708 N  N   . GLU B 1 73  ? 16.302  14.260  22.373  1.00 14.52  ?  73  GLU B N   1 
ATOM   2709 C  CA  . GLU B 1 73  ? 16.872  15.493  22.906  1.00 13.38  ?  73  GLU B CA  1 
ATOM   2710 C  C   . GLU B 1 73  ? 18.172  15.214  23.671  1.00 13.07  ?  73  GLU B C   1 
ATOM   2711 O  O   . GLU B 1 73  ? 19.093  16.006  23.611  1.00 14.77  ?  73  GLU B O   1 
ATOM   2712 C  CB  . GLU B 1 73  ? 15.809  16.214  23.744  1.00 15.27  ?  73  GLU B CB  1 
ATOM   2713 C  CG  . GLU B 1 73  ? 16.288  17.570  24.266  1.00 15.17  ?  73  GLU B CG  1 
ATOM   2714 C  CD  . GLU B 1 73  ? 15.272  18.244  25.156  1.00 17.11  ?  73  GLU B CD  1 
ATOM   2715 O  OE1 . GLU B 1 73  ? 14.074  18.293  24.796  1.00 18.83  ?  73  GLU B OE1 1 
ATOM   2716 O  OE2 . GLU B 1 73  ? 15.721  18.733  26.221  1.00 17.91  -1 73  GLU B OE2 1 
ATOM   2717 N  N   . ALA B 1 74  ? 18.320  14.048  24.337  1.00 12.98  ?  74  ALA B N   1 
ATOM   2718 C  CA  . ALA B 1 74  ? 19.559  13.719  25.029  1.00 13.32  ?  74  ALA B CA  1 
ATOM   2719 C  C   . ALA B 1 74  ? 20.727  13.582  24.056  1.00 14.98  ?  74  ALA B C   1 
ATOM   2720 O  O   . ALA B 1 74  ? 21.886  13.803  24.432  1.00 15.07  ?  74  ALA B O   1 
ATOM   2721 C  CB  . ALA B 1 74  ? 19.400  12.419  25.830  1.00 15.07  ?  74  ALA B CB  1 
ATOM   2722 N  N   . ALA B 1 75  ? 20.456  13.146  22.808  1.00 14.46  ?  75  ALA B N   1 
ATOM   2723 C  CA  . ALA B 1 75  ? 21.531  13.070  21.818  1.00 14.51  ?  75  ALA B CA  1 
ATOM   2724 C  C   . ALA B 1 75  ? 22.085  14.469  21.499  1.00 13.45  ?  75  ALA B C   1 
ATOM   2725 O  O   . ALA B 1 75  ? 23.298  14.636  21.329  1.00 14.17  ?  75  ALA B O   1 
ATOM   2726 C  CB  . ALA B 1 75  ? 21.031  12.350  20.579  1.00 15.05  ?  75  ALA B CB  1 
ATOM   2727 N  N   . LEU B 1 76  ? 21.194  15.468  21.402  1.00 14.25  ?  76  LEU B N   1 
ATOM   2728 C  CA  . LEU B 1 76  ? 21.612  16.847  21.189  1.00 16.85  ?  76  LEU B CA  1 
ATOM   2729 C  C   . LEU B 1 76  ? 22.378  17.360  22.406  1.00 15.81  ?  76  LEU B C   1 
ATOM   2730 O  O   . LEU B 1 76  ? 23.316  18.143  22.234  1.00 17.30  ?  76  LEU B O   1 
ATOM   2731 C  CB  . LEU B 1 76  ? 20.446  17.788  20.868  1.00 18.47  ?  76  LEU B CB  1 
ATOM   2732 C  CG  . LEU B 1 76  ? 19.899  17.770  19.436  1.00 22.91  ?  76  LEU B CG  1 
ATOM   2733 C  CD1 . LEU B 1 76  ? 20.991  18.128  18.468  1.00 23.46  ?  76  LEU B CD1 1 
ATOM   2734 C  CD2 . LEU B 1 76  ? 19.254  16.505  18.983  1.00 25.87  ?  76  LEU B CD2 1 
ATOM   2735 N  N   . GLY B 1 77  ? 22.011  16.893  23.618  1.00 16.03  ?  77  GLY B N   1 
ATOM   2736 C  CA  . GLY B 1 77  ? 22.764  17.251  24.826  1.00 16.73  ?  77  GLY B CA  1 
ATOM   2737 C  C   . GLY B 1 77  ? 24.207  16.779  24.756  1.00 17.07  ?  77  GLY B C   1 
ATOM   2738 O  O   . GLY B 1 77  ? 25.133  17.511  25.103  1.00 15.96  ?  77  GLY B O   1 
ATOM   2739 N  N   . ALA B 1 78  ? 24.394  15.552  24.231  1.00 13.91  ?  78  ALA B N   1 
ATOM   2740 C  CA  . ALA B 1 78  ? 25.701  14.985  24.028  1.00 14.65  ?  78  ALA B CA  1 
ATOM   2741 C  C   . ALA B 1 78  ? 26.471  15.751  22.955  1.00 15.09  ?  78  ALA B C   1 
ATOM   2742 O  O   . ALA B 1 78  ? 27.671  15.956  23.125  1.00 16.01  ?  78  ALA B O   1 
ATOM   2743 C  CB  . ALA B 1 78  ? 25.600  13.496  23.688  1.00 15.17  ?  78  ALA B CB  1 
ATOM   2744 N  N   . VAL B 1 79  ? 25.805  16.123  21.849  1.00 14.26  ?  79  VAL B N   1 
ATOM   2745 C  CA  . VAL B 1 79  ? 26.414  16.930  20.802  1.00 16.80  ?  79  VAL B CA  1 
ATOM   2746 C  C   . VAL B 1 79  ? 26.994  18.223  21.383  1.00 16.65  ?  79  VAL B C   1 
ATOM   2747 O  O   . VAL B 1 79  ? 28.167  18.554  21.118  1.00 17.42  ?  79  VAL B O   1 
ATOM   2748 C  CB  . VAL B 1 79  ? 25.432  17.193  19.632  1.00 18.39  ?  79  VAL B CB  1 
ATOM   2749 C  CG1 . VAL B 1 79  ? 25.914  18.277  18.674  1.00 20.26  ?  79  VAL B CG1 1 
ATOM   2750 C  CG2 . VAL B 1 79  ? 25.233  15.915  18.830  1.00 19.81  ?  79  VAL B CG2 1 
ATOM   2751 N  N   . ARG B 1 80  ? 26.172  18.940  22.152  1.00 16.52  ?  80  ARG B N   1 
ATOM   2752 C  CA  . ARG B 1 80  ? 26.624  20.183  22.804  1.00 18.43  ?  80  ARG B CA  1 
ATOM   2753 C  C   . ARG B 1 80  ? 27.834  19.930  23.721  1.00 21.35  ?  80  ARG B C   1 
ATOM   2754 O  O   . ARG B 1 80  ? 28.819  20.671  23.682  1.00 21.87  ?  80  ARG B O   1 
ATOM   2755 C  CB  . ARG B 1 80  ? 25.500  20.802  23.638  1.00 20.18  ?  80  ARG B CB  1 
ATOM   2756 C  CG  . ARG B 1 80  ? 24.437  21.494  22.793  1.00 22.60  ?  80  ARG B CG  1 
ATOM   2757 C  CD  . ARG B 1 80  ? 23.333  21.899  23.757  1.00 23.92  ?  80  ARG B CD  1 
ATOM   2758 N  NE  . ARG B 1 80  ? 22.350  22.751  23.082  1.00 26.33  ?  80  ARG B NE  1 
ATOM   2759 C  CZ  . ARG B 1 80  ? 22.464  24.062  22.961  1.00 28.33  ?  80  ARG B CZ  1 
ATOM   2760 N  NH1 . ARG B 1 80  ? 23.501  24.704  23.473  1.00 30.03  1  80  ARG B NH1 1 
ATOM   2761 N  NH2 . ARG B 1 80  ? 21.505  24.717  22.354  1.00 27.90  ?  80  ARG B NH2 1 
ATOM   2762 N  N   . TYR B 1 81  ? 27.781  18.892  24.553  1.00 18.07  ?  81  TYR B N   1 
ATOM   2763 C  CA  . TYR B 1 81  ? 28.904  18.558  25.427  1.00 18.25  ?  81  TYR B CA  1 
ATOM   2764 C  C   . TYR B 1 81  ? 30.194  18.346  24.625  1.00 20.09  ?  81  TYR B C   1 
ATOM   2765 O  O   . TYR B 1 81  ? 31.264  18.864  24.994  1.00 18.41  ?  81  TYR B O   1 
ATOM   2766 C  CB  . TYR B 1 81  ? 28.554  17.322  26.281  1.00 18.25  ?  81  TYR B CB  1 
ATOM   2767 C  CG  . TYR B 1 81  ? 29.730  16.792  27.088  1.00 20.33  ?  81  TYR B CG  1 
ATOM   2768 C  CD1 . TYR B 1 81  ? 30.079  17.335  28.328  1.00 24.23  ?  81  TYR B CD1 1 
ATOM   2769 C  CD2 . TYR B 1 81  ? 30.547  15.795  26.582  1.00 20.74  ?  81  TYR B CD2 1 
ATOM   2770 C  CE1 . TYR B 1 81  ? 31.166  16.854  29.041  1.00 24.39  ?  81  TYR B CE1 1 
ATOM   2771 C  CE2 . TYR B 1 81  ? 31.657  15.335  27.269  1.00 24.33  ?  81  TYR B CE2 1 
ATOM   2772 C  CZ  . TYR B 1 81  ? 31.956  15.861  28.508  1.00 25.59  ?  81  TYR B CZ  1 
ATOM   2773 O  OH  . TYR B 1 81  ? 33.032  15.363  29.151  1.00 31.53  ?  81  TYR B OH  1 
ATOM   2774 N  N   . PHE B 1 82  ? 30.126  17.539  23.543  1.00 16.03  ?  82  PHE B N   1 
ATOM   2775 C  CA  . PHE B 1 82  ? 31.299  17.205  22.766  1.00 18.17  ?  82  PHE B CA  1 
ATOM   2776 C  C   . PHE B 1 82  ? 31.880  18.446  22.069  1.00 18.08  ?  82  PHE B C   1 
ATOM   2777 O  O   . PHE B 1 82  ? 33.104  18.568  21.959  1.00 18.87  ?  82  PHE B O   1 
ATOM   2778 C  CB  . PHE B 1 82  ? 31.025  16.079  21.762  1.00 18.66  ?  82  PHE B CB  1 
ATOM   2779 C  CG  . PHE B 1 82  ? 30.896  14.717  22.437  1.00 20.13  ?  82  PHE B CG  1 
ATOM   2780 C  CD1 . PHE B 1 82  ? 31.885  14.249  23.303  1.00 21.59  ?  82  PHE B CD1 1 
ATOM   2781 C  CD2 . PHE B 1 82  ? 29.762  13.931  22.246  1.00 20.98  ?  82  PHE B CD2 1 
ATOM   2782 C  CE1 . PHE B 1 82  ? 31.749  13.019  23.939  1.00 24.58  ?  82  PHE B CE1 1 
ATOM   2783 C  CE2 . PHE B 1 82  ? 29.670  12.680  22.832  1.00 22.40  ?  82  PHE B CE2 1 
ATOM   2784 C  CZ  . PHE B 1 82  ? 30.637  12.242  23.699  1.00 22.11  ?  82  PHE B CZ  1 
ATOM   2785 N  N   . GLU B 1 83  ? 31.018  19.336  21.600  1.00 19.22  ?  83  GLU B N   1 
ATOM   2786 C  CA  . GLU B 1 83  ? 31.473  20.571  20.989  1.00 19.94  ?  83  GLU B CA  1 
ATOM   2787 C  C   . GLU B 1 83  ? 32.255  21.397  22.018  1.00 20.55  ?  83  GLU B C   1 
ATOM   2788 O  O   . GLU B 1 83  ? 33.326  21.885  21.682  1.00 22.42  ?  83  GLU B O   1 
ATOM   2789 C  CB  . GLU B 1 83  ? 30.348  21.417  20.411  1.00 20.22  ?  83  GLU B CB  1 
ATOM   2790 C  CG  . GLU B 1 83  ? 30.878  22.668  19.719  1.00 21.08  ?  83  GLU B CG  1 
ATOM   2791 C  CD  . GLU B 1 83  ? 29.882  23.716  19.338  1.00 21.51  ?  83  GLU B CD  1 
ATOM   2792 O  OE1 . GLU B 1 83  ? 28.761  23.673  19.809  1.00 22.94  ?  83  GLU B OE1 1 
ATOM   2793 O  OE2 . GLU B 1 83  ? 30.265  24.613  18.554  1.00 26.98  -1 83  GLU B OE2 1 
ATOM   2794 N  N   . GLU B 1 84  ? 31.770  21.492  23.262  1.00 22.79  ?  84  GLU B N   1 
ATOM   2795 C  CA  . GLU B 1 84  ? 32.481  22.228  24.300  1.00 27.50  ?  84  GLU B CA  1 
ATOM   2796 C  C   . GLU B 1 84  ? 33.834  21.603  24.585  1.00 31.01  ?  84  GLU B C   1 
ATOM   2797 O  O   . GLU B 1 84  ? 34.787  22.339  24.815  1.00 33.94  ?  84  GLU B O   1 
ATOM   2798 C  CB  . GLU B 1 84  ? 31.730  22.300  25.620  1.00 29.55  ?  84  GLU B CB  1 
ATOM   2799 C  CG  . GLU B 1 84  ? 30.505  23.187  25.508  1.00 34.36  ?  84  GLU B CG  1 
ATOM   2800 C  CD  . GLU B 1 84  ? 29.661  23.170  26.769  1.00 38.88  ?  84  GLU B CD  1 
ATOM   2801 O  OE1 . GLU B 1 84  ? 30.211  22.764  27.830  1.00 42.01  ?  84  GLU B OE1 1 
ATOM   2802 O  OE2 . GLU B 1 84  ? 28.463  23.545  26.654  1.00 43.78  -1 84  GLU B OE2 1 
ATOM   2803 N  N   . GLN B 1 85  ? 33.945  20.271  24.504  1.00 27.75  ?  85  GLN B N   1 
ATOM   2804 C  CA  . GLN B 1 85  ? 35.210  19.589  24.734  1.00 26.16  ?  85  GLN B CA  1 
ATOM   2805 C  C   . GLN B 1 85  ? 36.109  19.635  23.500  1.00 26.33  ?  85  GLN B C   1 
ATOM   2806 O  O   . GLN B 1 85  ? 37.206  19.105  23.532  1.00 31.82  ?  85  GLN B O   1 
ATOM   2807 C  CB  . GLN B 1 85  ? 35.023  18.120  25.148  1.00 28.45  ?  85  GLN B CB  1 
ATOM   2808 C  CG  . GLN B 1 85  ? 34.219  17.900  26.427  1.00 33.16  ?  85  GLN B CG  1 
ATOM   2809 C  CD  . GLN B 1 85  ? 34.961  18.431  27.634  1.00 36.84  ?  85  GLN B CD  1 
ATOM   2810 O  OE1 . GLN B 1 85  ? 36.170  18.226  27.761  1.00 37.08  ?  85  GLN B OE1 1 
ATOM   2811 N  NE2 . GLN B 1 85  ? 34.311  19.301  28.384  1.00 35.53  ?  85  GLN B NE2 1 
ATOM   2812 N  N   . GLY B 1 86  ? 35.637  20.173  22.371  1.00 26.31  ?  86  GLY B N   1 
ATOM   2813 C  CA  . GLY B 1 86  ? 36.491  20.320  21.204  1.00 25.98  ?  86  GLY B CA  1 
ATOM   2814 C  C   . GLY B 1 86  ? 36.590  19.063  20.343  1.00 25.60  ?  86  GLY B C   1 
ATOM   2815 O  O   . GLY B 1 86  ? 37.531  18.921  19.581  1.00 29.45  ?  86  GLY B O   1 
ATOM   2816 N  N   . ARG B 1 87  ? 35.578  18.198  20.376  1.00 23.65  ?  87  ARG B N   1 
ATOM   2817 C  CA  . ARG B 1 87  ? 35.515  17.051  19.480  1.00 24.50  ?  87  ARG B CA  1 
ATOM   2818 C  C   . ARG B 1 87  ? 34.577  17.313  18.308  1.00 25.22  ?  87  ARG B C   1 
ATOM   2819 O  O   . ARG B 1 87  ? 33.609  18.057  18.428  1.00 27.58  ?  87  ARG B O   1 
ATOM   2820 C  CB  . ARG B 1 87  ? 35.026  15.830  20.262  1.00 27.94  ?  87  ARG B CB  1 
ATOM   2821 C  CG  . ARG B 1 87  ? 36.190  15.487  21.177  1.00 33.83  ?  87  ARG B CG  1 
ATOM   2822 C  CD  . ARG B 1 87  ? 35.828  14.632  22.324  1.00 39.82  ?  87  ARG B CD  1 
ATOM   2823 N  NE  . ARG B 1 87  ? 36.135  13.259  21.973  1.00 44.27  ?  87  ARG B NE  1 
ATOM   2824 C  CZ  . ARG B 1 87  ? 36.644  12.387  22.823  1.00 41.59  ?  87  ARG B CZ  1 
ATOM   2825 N  NH1 . ARG B 1 87  ? 37.415  12.745  23.826  1.00 47.57  1  87  ARG B NH1 1 
ATOM   2826 N  NH2 . ARG B 1 87  ? 36.447  11.134  22.582  1.00 29.77  ?  87  ARG B NH2 1 
ATOM   2827 N  N   . GLY B 1 88  ? 34.815  16.596  17.210  1.00 23.85  ?  88  GLY B N   1 
ATOM   2828 C  CA  . GLY B 1 88  ? 33.924  16.674  16.062  1.00 23.28  ?  88  GLY B CA  1 
ATOM   2829 C  C   . GLY B 1 88  ? 34.663  17.093  14.804  1.00 24.07  ?  88  GLY B C   1 
ATOM   2830 O  O   . GLY B 1 88  ? 35.871  17.349  14.861  1.00 23.71  ?  88  GLY B O   1 
ATOM   2831 N  N   . TYR B 1 89  ? 33.931  17.136  13.678  1.00 22.09  ?  89  TYR B N   1 
ATOM   2832 C  CA  . TYR B 1 89  ? 34.525  17.429  12.389  1.00 25.67  ?  89  TYR B CA  1 
ATOM   2833 C  C   . TYR B 1 89  ? 34.867  18.921  12.372  1.00 21.85  ?  89  TYR B C   1 
ATOM   2834 O  O   . TYR B 1 89  ? 34.055  19.772  12.716  1.00 18.68  ?  89  TYR B O   1 
ATOM   2835 C  CB  . TYR B 1 89  ? 33.647  16.976  11.214  1.00 30.58  ?  89  TYR B CB  1 
ATOM   2836 C  CG  . TYR B 1 89  ? 34.180  17.389  9.843   1.00 33.76  ?  89  TYR B CG  1 
ATOM   2837 C  CD1 . TYR B 1 89  ? 35.170  16.672  9.165   1.00 41.97  ?  89  TYR B CD1 1 
ATOM   2838 C  CD2 . TYR B 1 89  ? 33.665  18.511  9.222   1.00 39.03  ?  89  TYR B CD2 1 
ATOM   2839 C  CE1 . TYR B 1 89  ? 35.633  17.079  7.916   1.00 43.99  ?  89  TYR B CE1 1 
ATOM   2840 C  CE2 . TYR B 1 89  ? 34.119  18.934  7.980   1.00 48.86  ?  89  TYR B CE2 1 
ATOM   2841 C  CZ  . TYR B 1 89  ? 35.104  18.218  7.317   1.00 50.29  ?  89  TYR B CZ  1 
ATOM   2842 O  OH  . TYR B 1 89  ? 35.476  18.747  6.091   1.00 49.30  ?  89  TYR B OH  1 
ATOM   2843 N  N   . ASP B 1 90  ? 36.101  19.233  11.948  1.00 23.75  ?  90  ASP B N   1 
ATOM   2844 C  CA  . ASP B 1 90  ? 36.590  20.595  12.037  1.00 27.30  ?  90  ASP B CA  1 
ATOM   2845 C  C   . ASP B 1 90  ? 36.270  21.325  10.740  1.00 28.29  ?  90  ASP B C   1 
ATOM   2846 O  O   . ASP B 1 90  ? 36.801  20.985  9.689   1.00 29.41  ?  90  ASP B O   1 
ATOM   2847 C  CB  . ASP B 1 90  ? 38.092  20.673  12.303  1.00 31.29  ?  90  ASP B CB  1 
ATOM   2848 C  CG  . ASP B 1 90  ? 38.604  22.062  12.688  1.00 32.47  ?  90  ASP B CG  1 
ATOM   2849 O  OD1 . ASP B 1 90  ? 37.899  23.065  12.445  1.00 30.37  ?  90  ASP B OD1 1 
ATOM   2850 O  OD2 . ASP B 1 90  ? 39.680  22.130  13.299  1.00 40.85  -1 90  ASP B OD2 1 
ATOM   2851 N  N   . VAL B 1 91  ? 35.408  22.327  10.853  1.00 24.80  ?  91  VAL B N   1 
ATOM   2852 C  CA  . VAL B 1 91  ? 34.990  23.124  9.712   1.00 31.58  ?  91  VAL B CA  1 
ATOM   2853 C  C   . VAL B 1 91  ? 35.605  24.531  9.802   1.00 31.11  ?  91  VAL B C   1 
ATOM   2854 O  O   . VAL B 1 91  ? 35.218  25.442  9.078   1.00 36.48  ?  91  VAL B O   1 
ATOM   2855 C  CB  . VAL B 1 91  ? 33.460  22.987  9.898   1.00 33.88  ?  91  VAL B CB  1 
ATOM   2856 C  CG1 . VAL B 1 91  ? 32.790  24.220  10.462  1.00 32.92  ?  91  VAL B CG1 1 
ATOM   2857 C  CG2 . VAL B 1 91  ? 32.763  22.421  8.680   1.00 34.28  ?  91  VAL B CG2 1 
ATOM   2858 N  N   . GLY B 1 92  ? 36.579  24.716  10.704  1.00 31.31  ?  92  GLY B N   1 
ATOM   2859 C  CA  . GLY B 1 92  ? 37.289  25.982  10.850  1.00 30.83  ?  92  GLY B CA  1 
ATOM   2860 C  C   . GLY B 1 92  ? 36.582  26.922  11.810  1.00 30.37  ?  92  GLY B C   1 
ATOM   2861 O  O   . GLY B 1 92  ? 37.132  27.324  12.829  1.00 31.59  ?  92  GLY B O   1 
ATOM   2862 N  N   . VAL B 1 93  ? 35.332  27.254  11.492  1.00 28.59  ?  93  VAL B N   1 
ATOM   2863 C  CA  . VAL B 1 93  ? 34.571  28.169  12.332  1.00 27.53  ?  93  VAL B CA  1 
ATOM   2864 C  C   . VAL B 1 93  ? 33.888  27.418  13.476  1.00 25.62  ?  93  VAL B C   1 
ATOM   2865 O  O   . VAL B 1 93  ? 33.330  28.045  14.354  1.00 24.23  ?  93  VAL B O   1 
ATOM   2866 C  CB  . VAL B 1 93  ? 33.521  28.932  11.497  1.00 31.37  ?  93  VAL B CB  1 
ATOM   2867 C  CG1 . VAL B 1 93  ? 34.171  29.880  10.491  1.00 34.58  ?  93  VAL B CG1 1 
ATOM   2868 C  CG2 . VAL B 1 93  ? 32.561  27.990  10.766  1.00 31.45  ?  93  VAL B CG2 1 
ATOM   2869 N  N   . ALA B 1 94  ? 33.896  26.078  13.440  1.00 23.66  ?  94  ALA B N   1 
ATOM   2870 C  CA  . ALA B 1 94  ? 33.288  25.278  14.482  1.00 21.08  ?  94  ALA B CA  1 
ATOM   2871 C  C   . ALA B 1 94  ? 33.808  23.850  14.371  1.00 20.50  ?  94  ALA B C   1 
ATOM   2872 O  O   . ALA B 1 94  ? 34.385  23.458  13.354  1.00 20.47  ?  94  ALA B O   1 
ATOM   2873 C  CB  . ALA B 1 94  ? 31.767  25.326  14.376  1.00 20.96  ?  94  ALA B CB  1 
ATOM   2874 N  N   . LYS B 1 95  ? 33.502  23.068  15.403  1.00 22.15  ?  95  LYS B N   1 
ATOM   2875 C  CA  . LYS B 1 95  ? 33.634  21.620  15.369  1.00 23.17  ?  95  LYS B CA  1 
ATOM   2876 C  C   . LYS B 1 95  ? 32.229  21.032  15.460  1.00 23.32  ?  95  LYS B C   1 
ATOM   2877 O  O   . LYS B 1 95  ? 31.437  21.495  16.286  1.00 22.70  ?  95  LYS B O   1 
ATOM   2878 C  CB  . LYS B 1 95  ? 34.501  21.122  16.526  1.00 28.91  ?  95  LYS B CB  1 
ATOM   2879 C  CG  . LYS B 1 95  ? 35.947  21.580  16.353  1.00 38.11  ?  95  LYS B CG  1 
ATOM   2880 C  CD  . LYS B 1 95  ? 37.005  20.704  17.004  1.00 50.57  ?  95  LYS B CD  1 
ATOM   2881 C  CE  . LYS B 1 95  ? 38.402  21.205  16.762  1.00 53.91  ?  95  LYS B CE  1 
ATOM   2882 N  NZ  . LYS B 1 95  ? 38.529  22.626  17.115  1.00 55.97  1  95  LYS B NZ  1 
ATOM   2883 N  N   . ILE B 1 96  ? 31.957  20.004  14.651  1.00 18.93  ?  96  ILE B N   1 
ATOM   2884 C  CA  . ILE B 1 96  ? 30.603  19.474  14.553  1.00 21.63  ?  96  ILE B CA  1 
ATOM   2885 C  C   . ILE B 1 96  ? 30.630  18.010  14.974  1.00 18.07  ?  96  ILE B C   1 
ATOM   2886 O  O   . ILE B 1 96  ? 31.050  17.164  14.202  1.00 17.08  ?  96  ILE B O   1 
ATOM   2887 C  CB  . ILE B 1 96  ? 30.030  19.624  13.133  1.00 22.24  ?  96  ILE B CB  1 
ATOM   2888 C  CG1 . ILE B 1 96  ? 30.136  21.059  12.648  1.00 22.38  ?  96  ILE B CG1 1 
ATOM   2889 C  CG2 . ILE B 1 96  ? 28.585  19.117  13.079  1.00 21.73  ?  96  ILE B CG2 1 
ATOM   2890 C  CD1 . ILE B 1 96  ? 29.706  21.263  11.209  1.00 24.15  ?  96  ILE B CD1 1 
ATOM   2891 N  N   . PRO B 1 97  ? 30.277  17.680  16.230  1.00 18.96  ?  97  PRO B N   1 
ATOM   2892 C  CA  . PRO B 1 97  ? 30.194  16.286  16.643  1.00 18.37  ?  97  PRO B CA  1 
ATOM   2893 C  C   . PRO B 1 97  ? 28.941  15.620  16.062  1.00 18.73  ?  97  PRO B C   1 
ATOM   2894 O  O   . PRO B 1 97  ? 28.075  16.318  15.581  1.00 19.20  ?  97  PRO B O   1 
ATOM   2895 C  CB  . PRO B 1 97  ? 30.130  16.380  18.167  1.00 17.61  ?  97  PRO B CB  1 
ATOM   2896 C  CG  . PRO B 1 97  ? 30.159  17.820  18.517  1.00 18.84  ?  97  PRO B CG  1 
ATOM   2897 C  CD  . PRO B 1 97  ? 29.874  18.602  17.295  1.00 18.80  ?  97  PRO B CD  1 
ATOM   2898 N  N   . LEU B 1 98  ? 28.886  14.282  16.112  1.00 18.06  ?  98  LEU B N   1 
ATOM   2899 C  CA  . LEU B 1 98  ? 27.756  13.500  15.649  1.00 18.24  ?  98  LEU B CA  1 
ATOM   2900 C  C   . LEU B 1 98  ? 27.508  12.382  16.657  1.00 15.22  ?  98  LEU B C   1 
ATOM   2901 O  O   . LEU B 1 98  ? 28.437  11.650  16.956  1.00 14.19  ?  98  LEU B O   1 
ATOM   2902 C  CB  . LEU B 1 98  ? 28.055  12.932  14.262  1.00 21.56  ?  98  LEU B CB  1 
ATOM   2903 C  CG  . LEU B 1 98  ? 26.820  12.614  13.422  1.00 25.31  ?  98  LEU B CG  1 
ATOM   2904 C  CD1 . LEU B 1 98  ? 26.229  13.904  12.833  1.00 24.46  ?  98  LEU B CD1 1 
ATOM   2905 C  CD2 . LEU B 1 98  ? 27.170  11.621  12.327  1.00 32.15  ?  98  LEU B CD2 1 
ATOM   2906 N  N   . VAL B 1 99  ? 26.272  12.302  17.159  1.00 14.07  ?  99  VAL B N   1 
ATOM   2907 C  CA  . VAL B 1 99  ? 25.858  11.314  18.143  1.00 13.83  ?  99  VAL B CA  1 
ATOM   2908 C  C   . VAL B 1 99  ? 24.564  10.671  17.646  1.00 13.78  ?  99  VAL B C   1 
ATOM   2909 O  O   . VAL B 1 99  ? 23.456  11.029  18.064  1.00 14.47  ?  99  VAL B O   1 
ATOM   2910 C  CB  . VAL B 1 99  ? 25.700  11.920  19.553  1.00 14.52  ?  99  VAL B CB  1 
ATOM   2911 C  CG1 . VAL B 1 99  ? 25.274  10.848  20.533  1.00 15.46  ?  99  VAL B CG1 1 
ATOM   2912 C  CG2 . VAL B 1 99  ? 27.002  12.591  19.997  1.00 16.95  ?  99  VAL B CG2 1 
ATOM   2913 N  N   . PRO B 1 100 ? 24.661  9.687   16.726  1.00 13.39  ?  100 PRO B N   1 
ATOM   2914 C  CA  . PRO B 1 100 ? 23.485  8.912   16.347  1.00 13.91  ?  100 PRO B CA  1 
ATOM   2915 C  C   . PRO B 1 100 ? 22.850  8.261   17.566  1.00 12.46  ?  100 PRO B C   1 
ATOM   2916 O  O   . PRO B 1 100 ? 23.535  7.956   18.561  1.00 11.53  ?  100 PRO B O   1 
ATOM   2917 C  CB  . PRO B 1 100 ? 23.991  7.867   15.347  1.00 13.28  ?  100 PRO B CB  1 
ATOM   2918 C  CG  . PRO B 1 100 ? 25.367  8.366   14.946  1.00 14.94  ?  100 PRO B CG  1 
ATOM   2919 C  CD  . PRO B 1 100 ? 25.897  9.161   16.124  1.00 13.55  ?  100 PRO B CD  1 
ATOM   2920 N  N   . ALA B 1 101 ? 21.528  8.099   17.505  1.00 11.92  ?  101 ALA B N   1 
ATOM   2921 C  CA  . ALA B 1 101 ? 20.803  7.522   18.610  1.00 12.19  ?  101 ALA B CA  1 
ATOM   2922 C  C   . ALA B 1 101 ? 19.517  6.845   18.134  1.00 11.99  ?  101 ALA B C   1 
ATOM   2923 O  O   . ALA B 1 101 ? 18.974  7.176   17.089  1.00 11.34  ?  101 ALA B O   1 
ATOM   2924 C  CB  . ALA B 1 101 ? 20.470  8.597   19.615  1.00 12.44  ?  101 ALA B CB  1 
ATOM   2925 N  N   . ALA B 1 102 ? 19.069  5.879   18.951  1.00 11.26  ?  102 ALA B N   1 
ATOM   2926 C  CA  . ALA B 1 102 ? 17.767  5.265   18.788  1.00 11.57  ?  102 ALA B CA  1 
ATOM   2927 C  C   . ALA B 1 102 ? 17.094  5.226   20.162  1.00 11.42  ?  102 ALA B C   1 
ATOM   2928 O  O   . ALA B 1 102 ? 17.774  5.339   21.187  1.00 12.03  ?  102 ALA B O   1 
ATOM   2929 C  CB  . ALA B 1 102 ? 17.912  3.899   18.187  1.00 11.29  ?  102 ALA B CB  1 
ATOM   2930 N  N   . VAL B 1 103 ? 15.759  5.130   20.167  1.00 12.72  ?  103 VAL B N   1 
ATOM   2931 C  CA  . VAL B 1 103 ? 14.978  5.219   21.390  1.00 13.24  ?  103 VAL B CA  1 
ATOM   2932 C  C   . VAL B 1 103 ? 14.230  3.900   21.685  1.00 13.82  ?  103 VAL B C   1 
ATOM   2933 O  O   . VAL B 1 103 ? 13.934  3.113   20.774  1.00 13.14  ?  103 VAL B O   1 
ATOM   2934 C  CB  . VAL B 1 103 ? 13.978  6.383   21.302  1.00 14.09  ?  103 VAL B CB  1 
ATOM   2935 C  CG1 . VAL B 1 103 ? 14.645  7.653   20.770  1.00 14.00  ?  103 VAL B CG1 1 
ATOM   2936 C  CG2 . VAL B 1 103 ? 12.737  6.059   20.476  1.00 14.44  ?  103 VAL B CG2 1 
ATOM   2937 N  N   . ILE B 1 104 ? 13.859  3.741   22.973  1.00 13.11  ?  104 ILE B N   1 
ATOM   2938 C  CA  . ILE B 1 104 ? 12.773  2.859   23.367  1.00 13.35  ?  104 ILE B CA  1 
ATOM   2939 C  C   . ILE B 1 104 ? 11.622  3.672   23.940  1.00 15.03  ?  104 ILE B C   1 
ATOM   2940 O  O   . ILE B 1 104 ? 11.833  4.750   24.487  1.00 16.85  ?  104 ILE B O   1 
ATOM   2941 C  CB  . ILE B 1 104 ? 13.233  1.803   24.384  1.00 13.71  ?  104 ILE B CB  1 
ATOM   2942 C  CG1 . ILE B 1 104 ? 13.621  2.438   25.766  1.00 13.74  ?  104 ILE B CG1 1 
ATOM   2943 C  CG2 . ILE B 1 104 ? 14.348  0.935   23.792  1.00 14.30  ?  104 ILE B CG2 1 
ATOM   2944 C  CD1 . ILE B 1 104 ? 13.695  1.446   26.891  1.00 15.08  ?  104 ILE B CD1 1 
ATOM   2945 N  N   . TYR B 1 105 ? 10.429  3.065   23.960  1.00 16.03  ?  105 TYR B N   1 
ATOM   2946 C  CA  . TYR B 1 105 ? 9.286   3.595   24.698  1.00 16.09  ?  105 TYR B CA  1 
ATOM   2947 C  C   . TYR B 1 105 ? 9.260   3.033   26.122  1.00 16.35  ?  105 TYR B C   1 
ATOM   2948 O  O   . TYR B 1 105 ? 9.062   1.831   26.310  1.00 16.89  ?  105 TYR B O   1 
ATOM   2949 C  CB  . TYR B 1 105 ? 8.024   3.242   23.906  1.00 17.73  ?  105 TYR B CB  1 
ATOM   2950 C  CG  . TYR B 1 105 ? 6.763   3.673   24.638  1.00 18.24  ?  105 TYR B CG  1 
ATOM   2951 C  CD1 . TYR B 1 105 ? 6.184   2.874   25.617  1.00 20.41  ?  105 TYR B CD1 1 
ATOM   2952 C  CD2 . TYR B 1 105 ? 6.170   4.897   24.357  1.00 19.06  ?  105 TYR B CD2 1 
ATOM   2953 C  CE1 . TYR B 1 105 ? 5.047   3.275   26.300  1.00 19.74  ?  105 TYR B CE1 1 
ATOM   2954 C  CE2 . TYR B 1 105 ? 5.025   5.293   25.018  1.00 18.78  ?  105 TYR B CE2 1 
ATOM   2955 C  CZ  . TYR B 1 105 ? 4.484   4.506   26.014  1.00 21.16  ?  105 TYR B CZ  1 
ATOM   2956 O  OH  . TYR B 1 105 ? 3.371   4.961   26.678  1.00 21.04  ?  105 TYR B OH  1 
ATOM   2957 N  N   . ASP B 1 106 ? 9.372   3.934   27.107  1.00 15.89  ?  106 ASP B N   1 
ATOM   2958 C  CA  . ASP B 1 106 ? 9.428   3.595   28.517  1.00 16.47  ?  106 ASP B CA  1 
ATOM   2959 C  C   . ASP B 1 106 ? 8.527   4.541   29.330  1.00 18.33  ?  106 ASP B C   1 
ATOM   2960 O  O   . ASP B 1 106 ? 8.719   4.663   30.534  1.00 19.08  ?  106 ASP B O   1 
ATOM   2961 C  CB  . ASP B 1 106 ? 10.862  3.624   29.037  1.00 16.92  ?  106 ASP B CB  1 
ATOM   2962 C  CG  . ASP B 1 106 ? 11.579  4.965   28.904  1.00 17.60  ?  106 ASP B CG  1 
ATOM   2963 O  OD1 . ASP B 1 106 ? 10.961  5.893   28.353  1.00 15.91  ?  106 ASP B OD1 1 
ATOM   2964 O  OD2 . ASP B 1 106 ? 12.732  5.064   29.384  1.00 17.13  -1 106 ASP B OD2 1 
ATOM   2965 N  N   . LEU B 1 107 ? 7.526   5.148   28.687  1.00 16.64  ?  107 LEU B N   1 
ATOM   2966 C  CA  . LEU B 1 107 ? 6.699   6.160   29.317  1.00 20.46  ?  107 LEU B CA  1 
ATOM   2967 C  C   . LEU B 1 107 ? 5.582   5.520   30.154  1.00 21.92  ?  107 LEU B C   1 
ATOM   2968 O  O   . LEU B 1 107 ? 4.946   6.230   30.929  1.00 23.24  ?  107 LEU B O   1 
ATOM   2969 C  CB  . LEU B 1 107 ? 6.057   7.083   28.275  1.00 21.73  ?  107 LEU B CB  1 
ATOM   2970 C  CG  . LEU B 1 107 ? 6.984   7.854   27.332  1.00 24.10  ?  107 LEU B CG  1 
ATOM   2971 C  CD1 . LEU B 1 107 ? 6.206   9.015   26.727  1.00 24.79  ?  107 LEU B CD1 1 
ATOM   2972 C  CD2 . LEU B 1 107 ? 8.185   8.362   28.011  1.00 24.83  ?  107 LEU B CD2 1 
ATOM   2973 N  N   . SER B 1 108 ? 5.308   4.219   29.983  1.00 20.67  ?  108 SER B N   1 
ATOM   2974 C  CA  . SER B 1 108 ? 4.200   3.572   30.686  1.00 23.23  ?  108 SER B CA  1 
ATOM   2975 C  C   . SER B 1 108 ? 4.648   2.962   32.016  1.00 24.70  ?  108 SER B C   1 
ATOM   2976 O  O   . SER B 1 108 ? 3.841   2.326   32.682  1.00 25.79  ?  108 SER B O   1 
ATOM   2977 C  CB  . SER B 1 108 ? 3.509   2.543   29.820  1.00 22.18  ?  108 SER B CB  1 
ATOM   2978 O  OG  . SER B 1 108 ? 2.725   3.207   28.838  1.00 27.25  ?  108 SER B OG  1 
ATOM   2979 N  N   . VAL B 1 109 ? 5.910   3.143   32.409  1.00 23.65  ?  109 VAL B N   1 
ATOM   2980 C  CA  . VAL B 1 109 ? 6.346   2.806   33.758  1.00 25.64  ?  109 VAL B CA  1 
ATOM   2981 C  C   . VAL B 1 109 ? 6.998   4.049   34.366  1.00 25.12  ?  109 VAL B C   1 
ATOM   2982 O  O   . VAL B 1 109 ? 7.580   4.842   33.637  1.00 21.32  ?  109 VAL B O   1 
ATOM   2983 C  CB  . VAL B 1 109 ? 7.271   1.577   33.842  1.00 29.84  ?  109 VAL B CB  1 
ATOM   2984 C  CG1 . VAL B 1 109 ? 6.612   0.321   33.303  1.00 35.12  ?  109 VAL B CG1 1 
ATOM   2985 C  CG2 . VAL B 1 109 ? 8.554   1.794   33.081  1.00 28.38  ?  109 VAL B CG2 1 
ATOM   2986 N  N   . GLY B 1 110 ? 6.801   4.263   35.684  1.00 23.44  ?  110 GLY B N   1 
ATOM   2987 C  CA  . GLY B 1 110 ? 7.272   5.457   36.367  1.00 24.35  ?  110 GLY B CA  1 
ATOM   2988 C  C   . GLY B 1 110 ? 6.462   6.684   35.955  1.00 24.98  ?  110 GLY B C   1 
ATOM   2989 O  O   . GLY B 1 110 ? 5.229   6.655   35.896  1.00 27.81  ?  110 GLY B O   1 
ATOM   2990 N  N   . ASP B 1 111 ? 7.179   7.728   35.531  1.00 24.10  ?  111 ASP B N   1 
ATOM   2991 C  CA  . ASP B 1 111 ? 6.586   9.037   35.293  1.00 22.62  ?  111 ASP B CA  1 
ATOM   2992 C  C   . ASP B 1 111 ? 6.728   9.385   33.808  1.00 20.40  ?  111 ASP B C   1 
ATOM   2993 O  O   . ASP B 1 111 ? 7.838   9.634   33.330  1.00 20.70  ?  111 ASP B O   1 
ATOM   2994 C  CB  . ASP B 1 111 ? 7.276   10.061  36.179  1.00 26.38  ?  111 ASP B CB  1 
ATOM   2995 C  CG  . ASP B 1 111 ? 6.688   11.467  36.166  1.00 25.74  ?  111 ASP B CG  1 
ATOM   2996 O  OD1 . ASP B 1 111 ? 5.905   11.776  35.261  1.00 23.57  ?  111 ASP B OD1 1 
ATOM   2997 O  OD2 . ASP B 1 111 ? 7.064   12.242  37.062  1.00 29.92  -1 111 ASP B OD2 1 
ATOM   2998 N  N   . ALA B 1 112 ? 5.606   9.444   33.111  1.00 18.64  ?  112 ALA B N   1 
ATOM   2999 C  CA  . ALA B 1 112 ? 5.573   9.686   31.664  1.00 21.97  ?  112 ALA B CA  1 
ATOM   3000 C  C   . ALA B 1 112 ? 6.065   11.079  31.266  1.00 23.64  ?  112 ALA B C   1 
ATOM   3001 O  O   . ALA B 1 112 ? 6.347   11.303  30.078  1.00 23.20  ?  112 ALA B O   1 
ATOM   3002 C  CB  . ALA B 1 112 ? 4.161   9.490   31.164  1.00 22.92  ?  112 ALA B CB  1 
ATOM   3003 N  N   . ASN B 1 113 ? 6.129   12.009  32.234  1.00 21.27  ?  113 ASN B N   1 
ATOM   3004 C  CA  . ASN B 1 113 ? 6.414   13.404  31.948  1.00 23.25  ?  113 ASN B CA  1 
ATOM   3005 C  C   . ASN B 1 113 ? 7.910   13.672  32.016  1.00 23.38  ?  113 ASN B C   1 
ATOM   3006 O  O   . ASN B 1 113 ? 8.342   14.759  31.647  1.00 24.92  ?  113 ASN B O   1 
ATOM   3007 C  CB  . ASN B 1 113 ? 5.640   14.325  32.888  1.00 28.51  ?  113 ASN B CB  1 
ATOM   3008 C  CG  . ASN B 1 113 ? 4.153   14.206  32.648  1.00 32.76  ?  113 ASN B CG  1 
ATOM   3009 O  OD1 . ASN B 1 113 ? 3.687   14.292  31.518  1.00 33.95  ?  113 ASN B OD1 1 
ATOM   3010 N  ND2 . ASN B 1 113 ? 3.388   13.898  33.679  1.00 43.54  ?  113 ASN B ND2 1 
ATOM   3011 N  N   . VAL B 1 114 ? 8.711   12.705  32.494  1.00 17.50  ?  114 VAL B N   1 
ATOM   3012 C  CA  . VAL B 1 114 ? 10.142  12.905  32.570  1.00 19.01  ?  114 VAL B CA  1 
ATOM   3013 C  C   . VAL B 1 114 ? 10.811  12.039  31.503  1.00 19.29  ?  114 VAL B C   1 
ATOM   3014 O  O   . VAL B 1 114 ? 10.627  10.811  31.503  1.00 18.42  ?  114 VAL B O   1 
ATOM   3015 C  CB  . VAL B 1 114 ? 10.678  12.575  33.972  1.00 19.96  ?  114 VAL B CB  1 
ATOM   3016 C  CG1 . VAL B 1 114 ? 12.187  12.718  34.062  1.00 20.63  ?  114 VAL B CG1 1 
ATOM   3017 C  CG2 . VAL B 1 114 ? 10.004  13.448  35.031  1.00 27.05  ?  114 VAL B CG2 1 
ATOM   3018 N  N   . ARG B 1 115 ? 11.623  12.672  30.651  1.00 17.55  ?  115 ARG B N   1 
ATOM   3019 C  CA  . ARG B 1 115 ? 12.311  11.960  29.586  1.00 17.27  ?  115 ARG B CA  1 
ATOM   3020 C  C   . ARG B 1 115 ? 13.747  12.456  29.500  1.00 16.64  ?  115 ARG B C   1 
ATOM   3021 O  O   . ARG B 1 115 ? 14.042  13.555  29.967  1.00 16.39  ?  115 ARG B O   1 
ATOM   3022 C  CB  . ARG B 1 115 ? 11.638  12.182  28.230  1.00 16.97  ?  115 ARG B CB  1 
ATOM   3023 C  CG  . ARG B 1 115 ? 10.147  11.884  28.139  1.00 19.19  ?  115 ARG B CG  1 
ATOM   3024 C  CD  . ARG B 1 115 ? 9.345   13.156  28.305  1.00 19.86  ?  115 ARG B CD  1 
ATOM   3025 N  NE  . ARG B 1 115 ? 7.907   12.965  28.285  1.00 19.32  ?  115 ARG B NE  1 
ATOM   3026 C  CZ  . ARG B 1 115 ? 6.995   13.828  27.845  1.00 21.04  ?  115 ARG B CZ  1 
ATOM   3027 N  NH1 . ARG B 1 115 ? 7.350   14.955  27.251  1.00 21.09  1  115 ARG B NH1 1 
ATOM   3028 N  NH2 . ARG B 1 115 ? 5.704   13.540  27.983  1.00 21.16  ?  115 ARG B NH2 1 
ATOM   3029 N  N   . PRO B 1 116 ? 14.697  11.669  28.948  1.00 14.75  ?  116 PRO B N   1 
ATOM   3030 C  CA  . PRO B 1 116 ? 16.053  12.151  28.733  1.00 15.45  ?  116 PRO B CA  1 
ATOM   3031 C  C   . PRO B 1 116 ? 16.055  13.414  27.889  1.00 15.55  ?  116 PRO B C   1 
ATOM   3032 O  O   . PRO B 1 116 ? 15.342  13.501  26.875  1.00 15.97  ?  116 PRO B O   1 
ATOM   3033 C  CB  . PRO B 1 116 ? 16.796  10.945  28.127  1.00 16.71  ?  116 PRO B CB  1 
ATOM   3034 C  CG  . PRO B 1 116 ? 15.961  9.777   28.633  1.00 16.15  ?  116 PRO B CG  1 
ATOM   3035 C  CD  . PRO B 1 116 ? 14.562  10.265  28.539  1.00 15.69  ?  116 PRO B CD  1 
ATOM   3036 N  N   . ASP B 1 117 ? 16.743  14.428  28.415  1.00 14.81  ?  117 ASP B N   1 
ATOM   3037 C  CA  . ASP B 1 117 ? 16.714  15.784  27.881  1.00 14.30  ?  117 ASP B CA  1 
ATOM   3038 C  C   . ASP B 1 117 ? 18.153  16.228  27.662  1.00 14.58  ?  117 ASP B C   1 
ATOM   3039 O  O   . ASP B 1 117 ? 19.104  15.429  27.800  1.00 16.00  ?  117 ASP B O   1 
ATOM   3040 C  CB  . ASP B 1 117 ? 15.916  16.700  28.795  1.00 16.20  ?  117 ASP B CB  1 
ATOM   3041 C  CG  . ASP B 1 117 ? 16.456  16.796  30.227  1.00 17.32  ?  117 ASP B CG  1 
ATOM   3042 O  OD1 . ASP B 1 117 ? 17.511  16.201  30.524  1.00 15.98  ?  117 ASP B OD1 1 
ATOM   3043 O  OD2 . ASP B 1 117 ? 15.819  17.497  31.012  1.00 19.91  -1 117 ASP B OD2 1 
ATOM   3044 N  N   . LEU B 1 118 ? 18.342  17.511  27.311  1.00 15.96  ?  118 LEU B N   1 
ATOM   3045 C  CA  . LEU B 1 118 ? 19.692  18.024  27.056  1.00 15.77  ?  118 LEU B CA  1 
ATOM   3046 C  C   . LEU B 1 118 ? 20.625  17.722  28.228  1.00 14.81  ?  118 LEU B C   1 
ATOM   3047 O  O   . LEU B 1 118 ? 21.774  17.293  28.038  1.00 15.46  ?  118 LEU B O   1 
ATOM   3048 C  CB  . LEU B 1 118 ? 19.688  19.530  26.797  1.00 17.37  ?  118 LEU B CB  1 
ATOM   3049 C  CG  . LEU B 1 118 ? 19.032  20.012  25.499  1.00 17.54  ?  118 LEU B CG  1 
ATOM   3050 C  CD1 . LEU B 1 118 ? 19.085  21.558  25.515  1.00 18.07  ?  118 LEU B CD1 1 
ATOM   3051 C  CD2 . LEU B 1 118 ? 19.693  19.463  24.260  1.00 18.30  ?  118 LEU B CD2 1 
ATOM   3052 N  N   . ALA B 1 119 ? 20.142  18.020  29.443  1.00 16.01  ?  119 ALA B N   1 
ATOM   3053 C  CA  . ALA B 1 119 ? 20.954  17.874  30.650  1.00 17.90  ?  119 ALA B CA  1 
ATOM   3054 C  C   . ALA B 1 119 ? 21.294  16.401  30.916  1.00 16.28  ?  119 ALA B C   1 
ATOM   3055 O  O   . ALA B 1 119 ? 22.428  16.072  31.253  1.00 16.17  ?  119 ALA B O   1 
ATOM   3056 C  CB  . ALA B 1 119 ? 20.250  18.490  31.848  1.00 18.63  ?  119 ALA B CB  1 
ATOM   3057 N  N   . MET B 1 120 ? 20.339  15.496  30.721  1.00 15.84  ?  120 MET B N   1 
ATOM   3058 C  CA  . MET B 1 120 ? 20.602  14.089  30.970  1.00 16.58  ?  120 MET B CA  1 
ATOM   3059 C  C   . MET B 1 120 ? 21.628  13.509  29.993  1.00 16.34  ?  120 MET B C   1 
ATOM   3060 O  O   . MET B 1 120 ? 22.450  12.672  30.371  1.00 16.28  ?  120 MET B O   1 
ATOM   3061 C  CB  . MET B 1 120 ? 19.314  13.261  30.999  1.00 17.88  ?  120 MET B CB  1 
ATOM   3062 C  CG  . MET B 1 120 ? 19.508  11.984  31.760  1.00 21.43  ?  120 MET B CG  1 
ATOM   3063 S  SD  . MET B 1 120 ? 18.080  10.896  31.703  1.00 23.97  ?  120 MET B SD  1 
ATOM   3064 C  CE  . MET B 1 120 ? 16.838  11.733  32.680  1.00 30.35  ?  120 MET B CE  1 
ATOM   3065 N  N   . GLY B 1 121 ? 21.589  13.943  28.731  1.00 16.30  ?  121 GLY B N   1 
ATOM   3066 C  CA  . GLY B 1 121 ? 22.580  13.518  27.763  1.00 15.66  ?  121 GLY B CA  1 
ATOM   3067 C  C   . GLY B 1 121 ? 23.986  13.981  28.134  1.00 16.02  ?  121 GLY B C   1 
ATOM   3068 O  O   . GLY B 1 121 ? 24.948  13.225  28.041  1.00 15.23  ?  121 GLY B O   1 
ATOM   3069 N  N   . ARG B 1 122 ? 24.098  15.207  28.633  1.00 16.45  ?  122 ARG B N   1 
ATOM   3070 C  CA  . ARG B 1 122 ? 25.372  15.670  29.147  1.00 17.03  ?  122 ARG B CA  1 
ATOM   3071 C  C   . ARG B 1 122 ? 25.864  14.828  30.328  1.00 14.67  ?  122 ARG B C   1 
ATOM   3072 O  O   . ARG B 1 122 ? 27.060  14.507  30.391  1.00 16.16  ?  122 ARG B O   1 
ATOM   3073 C  CB  . ARG B 1 122 ? 25.270  17.153  29.532  1.00 21.18  ?  122 ARG B CB  1 
ATOM   3074 C  CG  . ARG B 1 122 ? 26.588  17.664  30.104  1.00 25.13  ?  122 ARG B CG  1 
ATOM   3075 C  CD  . ARG B 1 122 ? 26.432  19.102  30.577  1.00 30.94  ?  122 ARG B CD  1 
ATOM   3076 N  NE  . ARG B 1 122 ? 26.140  19.963  29.428  1.00 35.78  ?  122 ARG B NE  1 
ATOM   3077 C  CZ  . ARG B 1 122 ? 27.004  20.728  28.761  1.00 39.21  ?  122 ARG B CZ  1 
ATOM   3078 N  NH1 . ARG B 1 122 ? 28.298  20.786  29.088  1.00 33.76  1  122 ARG B NH1 1 
ATOM   3079 N  NH2 . ARG B 1 122 ? 26.519  21.442  27.752  1.00 38.03  ?  122 ARG B NH2 1 
ATOM   3080 N  N   . ARG B 1 123 ? 24.978  14.525  31.280  1.00 15.36  ?  123 ARG B N   1 
ATOM   3081 C  CA  . ARG B 1 123 ? 25.329  13.707  32.439  1.00 16.40  ?  123 ARG B CA  1 
ATOM   3082 C  C   . ARG B 1 123 ? 25.902  12.344  32.039  1.00 16.88  ?  123 ARG B C   1 
ATOM   3083 O  O   . ARG B 1 123 ? 26.937  11.915  32.596  1.00 16.92  ?  123 ARG B O   1 
ATOM   3084 C  CB  . ARG B 1 123 ? 24.152  13.445  33.385  1.00 17.74  ?  123 ARG B CB  1 
ATOM   3085 C  CG  . ARG B 1 123 ? 23.595  14.623  34.160  1.00 18.88  ?  123 ARG B CG  1 
ATOM   3086 C  CD  . ARG B 1 123 ? 24.575  15.243  35.135  1.00 19.80  ?  123 ARG B CD  1 
ATOM   3087 N  NE  . ARG B 1 123 ? 25.485  16.253  34.577  1.00 21.09  ?  123 ARG B NE  1 
ATOM   3088 C  CZ  . ARG B 1 123 ? 25.124  17.495  34.277  1.00 22.53  ?  123 ARG B CZ  1 
ATOM   3089 N  NH1 . ARG B 1 123 ? 23.841  17.866  34.322  1.00 27.10  1  123 ARG B NH1 1 
ATOM   3090 N  NH2 . ARG B 1 123 ? 26.044  18.331  33.873  1.00 24.52  ?  123 ARG B NH2 1 
ATOM   3091 N  N   . ALA B 1 124 ? 25.293  11.679  31.019  1.00 17.16  ?  124 ALA B N   1 
ATOM   3092 C  CA  . ALA B 1 124 ? 25.829  10.400  30.555  1.00 15.73  ?  124 ALA B CA  1 
ATOM   3093 C  C   . ALA B 1 124 ? 27.225  10.560  29.973  1.00 14.98  ?  124 ALA B C   1 
ATOM   3094 O  O   . ALA B 1 124 ? 28.084  9.713   30.206  1.00 14.82  ?  124 ALA B O   1 
ATOM   3095 C  CB  . ALA B 1 124 ? 24.881  9.775   29.524  1.00 16.26  ?  124 ALA B CB  1 
ATOM   3096 N  N   . CYS B 1 125 ? 27.468  11.653  29.225  1.00 14.57  ?  125 CYS B N   1 
ATOM   3097 C  CA  . CYS B 1 125 ? 28.786  11.890  28.661  1.00 15.06  ?  125 CYS B CA  1 
ATOM   3098 C  C   . CYS B 1 125 ? 29.847  12.094  29.757  1.00 15.41  ?  125 CYS B C   1 
ATOM   3099 O  O   . CYS B 1 125 ? 30.967  11.623  29.657  1.00 16.06  ?  125 CYS B O   1 
ATOM   3100 C  CB  . CYS B 1 125 ? 28.797  13.114  27.760  1.00 17.39  ?  125 CYS B CB  1 
ATOM   3101 S  SG  . CYS B 1 125 ? 27.808  12.888  26.249  1.00 20.00  ?  125 CYS B SG  1 
ATOM   3102 N  N   . GLU B 1 126 ? 29.505  12.872  30.773  1.00 18.25  ?  126 GLU B N   1 
ATOM   3103 C  CA  . GLU B 1 126 ? 30.399  13.173  31.894  1.00 19.05  ?  126 GLU B CA  1 
ATOM   3104 C  C   . GLU B 1 126 ? 30.801  11.882  32.608  1.00 21.39  ?  126 GLU B C   1 
ATOM   3105 O  O   . GLU B 1 126 ? 31.929  11.739  33.056  1.00 19.77  ?  126 GLU B O   1 
ATOM   3106 C  CB  . GLU B 1 126 ? 29.731  14.146  32.867  1.00 18.85  ?  126 GLU B CB  1 
ATOM   3107 C  CG  . GLU B 1 126 ? 29.574  15.551  32.292  1.00 23.28  ?  126 GLU B CG  1 
ATOM   3108 C  CD  . GLU B 1 126 ? 28.974  16.566  33.296  1.00 28.46  ?  126 GLU B CD  1 
ATOM   3109 O  OE1 . GLU B 1 126 ? 28.559  16.174  34.405  1.00 28.70  ?  126 GLU B OE1 1 
ATOM   3110 O  OE2 . GLU B 1 126 ? 28.902  17.749  32.938  1.00 28.78  -1 126 GLU B OE2 1 
ATOM   3111 N  N   . ALA B 1 127 ? 29.859  10.950  32.707  1.00 20.53  ?  127 ALA B N   1 
ATOM   3112 C  CA  . ALA B 1 127 ? 30.039  9.697   33.421  1.00 21.66  ?  127 ALA B CA  1 
ATOM   3113 C  C   . ALA B 1 127 ? 30.761  8.616   32.625  1.00 23.68  ?  127 ALA B C   1 
ATOM   3114 O  O   . ALA B 1 127 ? 30.995  7.543   33.179  1.00 21.16  ?  127 ALA B O   1 
ATOM   3115 C  CB  . ALA B 1 127 ? 28.693  9.196   33.847  1.00 20.00  ?  127 ALA B CB  1 
ATOM   3116 N  N   . ALA B 1 128 ? 31.078  8.849   31.340  1.00 19.66  ?  128 ALA B N   1 
ATOM   3117 C  CA  . ALA B 1 128 ? 31.561  7.789   30.481  1.00 19.61  ?  128 ALA B CA  1 
ATOM   3118 C  C   . ALA B 1 128 ? 32.984  7.385   30.884  1.00 21.43  ?  128 ALA B C   1 
ATOM   3119 O  O   . ALA B 1 128 ? 33.883  8.206   30.906  1.00 21.39  ?  128 ALA B O   1 
ATOM   3120 C  CB  . ALA B 1 128 ? 31.487  8.217   29.015  1.00 19.85  ?  128 ALA B CB  1 
ATOM   3121 N  N   . LYS B 1 129 ? 33.213  6.102   31.115  1.00 19.34  ?  129 LYS B N   1 
ATOM   3122 C  CA  . LYS B 1 129 ? 34.532  5.645   31.521  1.00 21.20  ?  129 LYS B CA  1 
ATOM   3123 C  C   . LYS B 1 129 ? 34.883  4.308   30.889  1.00 19.97  ?  129 LYS B C   1 
ATOM   3124 O  O   . LYS B 1 129 ? 34.005  3.599   30.410  1.00 16.83  ?  129 LYS B O   1 
ATOM   3125 C  CB  . LYS B 1 129 ? 34.587  5.617   33.044  1.00 28.04  ?  129 LYS B CB  1 
ATOM   3126 C  CG  . LYS B 1 129 ? 33.616  4.745   33.742  1.00 37.64  ?  129 LYS B CG  1 
ATOM   3127 C  CD  . LYS B 1 129 ? 33.558  5.106   35.235  1.00 53.04  ?  129 LYS B CD  1 
ATOM   3128 C  CE  . LYS B 1 129 ? 32.323  4.639   35.986  1.00 62.55  ?  129 LYS B CE  1 
ATOM   3129 N  NZ  . LYS B 1 129 ? 32.286  3.178   36.148  1.00 67.35  1  129 LYS B NZ  1 
ATOM   3130 N  N   . PRO B 1 130 ? 36.190  3.966   30.850  1.00 20.50  ?  130 PRO B N   1 
ATOM   3131 C  CA  . PRO B 1 130 ? 36.637  2.644   30.462  1.00 21.66  ?  130 PRO B CA  1 
ATOM   3132 C  C   . PRO B 1 130 ? 36.344  1.609   31.541  1.00 20.94  ?  130 PRO B C   1 
ATOM   3133 O  O   . PRO B 1 130 ? 35.782  1.935   32.576  1.00 20.09  ?  130 PRO B O   1 
ATOM   3134 C  CB  . PRO B 1 130 ? 38.156  2.785   30.250  1.00 24.04  ?  130 PRO B CB  1 
ATOM   3135 C  CG  . PRO B 1 130 ? 38.515  3.970   31.150  1.00 23.60  ?  130 PRO B CG  1 
ATOM   3136 C  CD  . PRO B 1 130 ? 37.301  4.829   31.326  1.00 22.45  ?  130 PRO B CD  1 
ATOM   3137 N  N   . GLY B 1 131 ? 36.660  0.354   31.227  1.00 23.06  ?  131 GLY B N   1 
ATOM   3138 C  CA  . GLY B 1 131 ? 36.473  -0.755  32.142  1.00 25.51  ?  131 GLY B CA  1 
ATOM   3139 C  C   . GLY B 1 131 ? 35.014  -1.178  32.270  1.00 24.56  ?  131 GLY B C   1 
ATOM   3140 O  O   . GLY B 1 131 ? 34.154  -0.754  31.492  1.00 24.33  ?  131 GLY B O   1 
ATOM   3141 N  N   . PRO B 1 132 ? 34.713  -2.030  33.272  1.00 25.36  ?  132 PRO B N   1 
ATOM   3142 C  CA  . PRO B 1 132 ? 33.389  -2.615  33.413  1.00 25.59  ?  132 PRO B CA  1 
ATOM   3143 C  C   . PRO B 1 132 ? 32.333  -1.566  33.733  1.00 26.13  ?  132 PRO B C   1 
ATOM   3144 O  O   . PRO B 1 132 ? 32.604  -0.592  34.409  1.00 22.45  ?  132 PRO B O   1 
ATOM   3145 C  CB  . PRO B 1 132 ? 33.564  -3.665  34.510  1.00 29.17  ?  132 PRO B CB  1 
ATOM   3146 C  CG  . PRO B 1 132 ? 34.828  -3.289  35.243  1.00 31.29  ?  132 PRO B CG  1 
ATOM   3147 C  CD  . PRO B 1 132 ? 35.682  -2.513  34.276  1.00 28.64  ?  132 PRO B CD  1 
ATOM   3148 N  N   . PHE B 1 133 ? 31.122  -1.750  33.209  1.00 23.49  ?  133 PHE B N   1 
ATOM   3149 C  CA  . PHE B 1 133 ? 30.015  -0.864  33.501  1.00 22.27  ?  133 PHE B CA  1 
ATOM   3150 C  C   . PHE B 1 133 ? 28.869  -1.706  34.035  1.00 19.42  ?  133 PHE B C   1 
ATOM   3151 O  O   . PHE B 1 133 ? 28.819  -2.911  33.841  1.00 19.81  ?  133 PHE B O   1 
ATOM   3152 C  CB  . PHE B 1 133 ? 29.608  -0.064  32.252  1.00 22.49  ?  133 PHE B CB  1 
ATOM   3153 C  CG  . PHE B 1 133 ? 29.322  -0.888  30.993  1.00 19.73  ?  133 PHE B CG  1 
ATOM   3154 C  CD1 . PHE B 1 133 ? 28.073  -1.456  30.758  1.00 18.70  ?  133 PHE B CD1 1 
ATOM   3155 C  CD2 . PHE B 1 133 ? 30.303  -1.064  30.038  1.00 18.80  ?  133 PHE B CD2 1 
ATOM   3156 C  CE1 . PHE B 1 133 ? 27.839  -2.209  29.612  1.00 18.58  ?  133 PHE B CE1 1 
ATOM   3157 C  CE2 . PHE B 1 133 ? 30.050  -1.810  28.893  1.00 19.30  ?  133 PHE B CE2 1 
ATOM   3158 C  CZ  . PHE B 1 133 ? 28.830  -2.368  28.677  1.00 17.66  ?  133 PHE B CZ  1 
ATOM   3159 N  N   . GLU B 1 134 ? 27.916  -1.053  34.671  1.00 20.27  ?  134 GLU B N   1 
ATOM   3160 C  CA  . GLU B 1 134 ? 26.790  -1.738  35.282  1.00 23.44  ?  134 GLU B CA  1 
ATOM   3161 C  C   . GLU B 1 134 ? 25.822  -2.178  34.188  1.00 19.96  ?  134 GLU B C   1 
ATOM   3162 O  O   . GLU B 1 134 ? 25.693  -1.475  33.180  1.00 18.46  ?  134 GLU B O   1 
ATOM   3163 C  CB  . GLU B 1 134 ? 26.076  -0.770  36.233  1.00 29.31  ?  134 GLU B CB  1 
ATOM   3164 C  CG  . GLU B 1 134 ? 25.778  -1.329  37.622  1.00 46.54  ?  134 GLU B CG  1 
ATOM   3165 C  CD  . GLU B 1 134 ? 26.925  -1.943  38.431  1.00 52.35  ?  134 GLU B CD  1 
ATOM   3166 O  OE1 . GLU B 1 134 ? 28.016  -1.342  38.594  1.00 59.47  ?  134 GLU B OE1 1 
ATOM   3167 O  OE2 . GLU B 1 134 ? 26.710  -3.072  38.924  1.00 65.27  -1 134 GLU B OE2 1 
ATOM   3168 N  N   . ARG B 1 135 ? 25.095  -3.279  34.456  1.00 19.16  ?  135 ARG B N   1 
ATOM   3169 C  CA  . ARG B 1 135 ? 24.060  -3.798  33.564  1.00 17.40  ?  135 ARG B CA  1 
ATOM   3170 C  C   . ARG B 1 135 ? 22.760  -3.937  34.326  1.00 17.44  ?  135 ARG B C   1 
ATOM   3171 O  O   . ARG B 1 135 ? 22.731  -3.708  35.516  1.00 20.47  ?  135 ARG B O   1 
ATOM   3172 C  CB  . ARG B 1 135 ? 24.539  -5.092  32.916  1.00 18.68  ?  135 ARG B CB  1 
ATOM   3173 C  CG  . ARG B 1 135 ? 25.820  -4.904  32.111  1.00 19.48  ?  135 ARG B CG  1 
ATOM   3174 C  CD  . ARG B 1 135 ? 27.018  -5.643  32.691  1.00 21.21  ?  135 ARG B CD  1 
ATOM   3175 N  NE  . ARG B 1 135 ? 26.849  -7.104  32.596  1.00 20.40  ?  135 ARG B NE  1 
ATOM   3176 C  CZ  . ARG B 1 135 ? 27.673  -7.998  33.148  1.00 32.04  ?  135 ARG B CZ  1 
ATOM   3177 N  NH1 . ARG B 1 135 ? 28.682  -7.612  33.908  1.00 30.96  1  135 ARG B NH1 1 
ATOM   3178 N  NH2 . ARG B 1 135 ? 27.490  -9.296  32.963  1.00 31.67  ?  135 ARG B NH2 1 
ATOM   3179 N  N   . GLY B 1 136 ? 21.679  -4.285  33.634  1.00 16.58  ?  136 GLY B N   1 
ATOM   3180 C  CA  . GLY B 1 136 ? 20.353  -4.412  34.226  1.00 16.58  ?  136 GLY B CA  1 
ATOM   3181 C  C   . GLY B 1 136 ? 19.528  -3.148  34.001  1.00 17.92  ?  136 GLY B C   1 
ATOM   3182 O  O   . GLY B 1 136 ? 19.595  -2.530  32.938  1.00 15.37  ?  136 GLY B O   1 
ATOM   3183 N  N   . ARG B 1 137 ? 18.804  -2.718  35.044  1.00 18.64  ?  137 ARG B N   1 
ATOM   3184 C  CA  . ARG B 1 137 ? 17.891  -1.588  34.924  1.00 21.52  ?  137 ARG B CA  1 
ATOM   3185 C  C   . ARG B 1 137 ? 18.652  -0.311  35.257  1.00 21.44  ?  137 ARG B C   1 
ATOM   3186 O  O   . ARG B 1 137 ? 18.504  0.270   36.334  1.00 18.33  ?  137 ARG B O   1 
ATOM   3187 C  CB  . ARG B 1 137 ? 16.664  -1.811  35.815  1.00 24.93  ?  137 ARG B CB  1 
ATOM   3188 C  CG  . ARG B 1 137 ? 16.017  -3.152  35.488  1.00 33.18  ?  137 ARG B CG  1 
ATOM   3189 C  CD  . ARG B 1 137 ? 14.732  -3.047  34.810  1.00 39.28  ?  137 ARG B CD  1 
ATOM   3190 N  NE  . ARG B 1 137 ? 13.699  -2.784  35.816  1.00 47.01  ?  137 ARG B NE  1 
ATOM   3191 C  CZ  . ARG B 1 137 ? 12.431  -2.447  35.530  1.00 52.04  ?  137 ARG B CZ  1 
ATOM   3192 N  NH1 . ARG B 1 137 ? 12.126  -1.863  34.365  1.00 41.41  1  137 ARG B NH1 1 
ATOM   3193 N  NH2 . ARG B 1 137 ? 11.490  -2.639  36.458  1.00 47.82  ?  137 ARG B NH2 1 
ATOM   3194 N  N   . VAL B 1 138 ? 19.487  0.106   34.306  1.00 18.40  ?  138 VAL B N   1 
ATOM   3195 C  CA  . VAL B 1 138 ? 20.337  1.266   34.447  1.00 18.48  ?  138 VAL B CA  1 
ATOM   3196 C  C   . VAL B 1 138 ? 20.442  1.930   33.074  1.00 18.35  ?  138 VAL B C   1 
ATOM   3197 O  O   . VAL B 1 138 ? 20.258  1.275   32.035  1.00 15.50  ?  138 VAL B O   1 
ATOM   3198 C  CB  . VAL B 1 138 ? 21.684  0.762   34.978  1.00 22.80  ?  138 VAL B CB  1 
ATOM   3199 C  CG1 . VAL B 1 138 ? 22.451  -0.070  33.948  1.00 21.28  ?  138 VAL B CG1 1 
ATOM   3200 C  CG2 . VAL B 1 138 ? 22.541  1.900   35.454  1.00 29.38  ?  138 VAL B CG2 1 
ATOM   3201 N  N   . GLY B 1 139 ? 20.730  3.243   33.077  1.00 15.61  ?  139 GLY B N   1 
ATOM   3202 C  CA  . GLY B 1 139 ? 20.918  3.971   31.835  1.00 14.84  ?  139 GLY B CA  1 
ATOM   3203 C  C   . GLY B 1 139 ? 19.701  3.815   30.924  1.00 14.92  ?  139 GLY B C   1 
ATOM   3204 O  O   . GLY B 1 139 ? 18.550  3.952   31.359  1.00 15.26  ?  139 GLY B O   1 
ATOM   3205 N  N   . GLY B 1 140 ? 19.962  3.507   29.642  1.00 13.48  ?  140 GLY B N   1 
ATOM   3206 C  CA  . GLY B 1 140 ? 18.893  3.340   28.674  1.00 13.94  ?  140 GLY B CA  1 
ATOM   3207 C  C   . GLY B 1 140 ? 17.942  2.191   29.019  1.00 12.77  ?  140 GLY B C   1 
ATOM   3208 O  O   . GLY B 1 140 ? 16.825  2.188   28.549  1.00 14.41  ?  140 GLY B O   1 
ATOM   3209 N  N   . GLY B 1 141 ? 18.364  1.256   29.868  1.00 13.39  ?  141 GLY B N   1 
ATOM   3210 C  CA  . GLY B 1 141 ? 17.544  0.122   30.257  1.00 14.98  ?  141 GLY B CA  1 
ATOM   3211 C  C   . GLY B 1 141 ? 16.715  0.310   31.540  1.00 16.23  ?  141 GLY B C   1 
ATOM   3212 O  O   . GLY B 1 141 ? 16.013  -0.614  31.928  1.00 16.82  ?  141 GLY B O   1 
ATOM   3213 N  N   . THR B 1 142 ? 16.736  1.517   32.159  1.00 14.98  ?  142 THR B N   1 
ATOM   3214 C  CA  . THR B 1 142 ? 16.150  1.727   33.473  1.00 15.52  ?  142 THR B CA  1 
ATOM   3215 C  C   . THR B 1 142 ? 14.667  1.383   33.462  1.00 16.13  ?  142 THR B C   1 
ATOM   3216 O  O   . THR B 1 142 ? 14.173  0.722   34.389  1.00 17.40  ?  142 THR B O   1 
ATOM   3217 C  CB  . THR B 1 142 ? 16.369  3.174   33.929  1.00 15.23  ?  142 THR B CB  1 
ATOM   3218 O  OG1 . THR B 1 142 ? 17.776  3.414   33.939  1.00 14.84  ?  142 THR B OG1 1 
ATOM   3219 C  CG2 . THR B 1 142 ? 15.806  3.398   35.323  1.00 15.96  ?  142 THR B CG2 1 
ATOM   3220 N  N   . GLY B 1 143 ? 13.939  1.859   32.446  1.00 14.75  ?  143 GLY B N   1 
ATOM   3221 C  CA  . GLY B 1 143 ? 12.505  1.622   32.373  1.00 15.06  ?  143 GLY B CA  1 
ATOM   3222 C  C   . GLY B 1 143 ? 12.075  0.554   31.365  1.00 14.79  ?  143 GLY B C   1 
ATOM   3223 O  O   . GLY B 1 143 ? 10.901  0.503   31.005  1.00 18.72  ?  143 GLY B O   1 
ATOM   3224 N  N   . ALA B 1 144 ? 12.998  -0.311  30.931  1.00 16.07  ?  144 ALA B N   1 
ATOM   3225 C  CA  . ALA B 1 144 ? 12.750  -1.335  29.929  1.00 14.36  ?  144 ALA B CA  1 
ATOM   3226 C  C   . ALA B 1 144 ? 11.893  -2.463  30.514  1.00 16.94  ?  144 ALA B C   1 
ATOM   3227 O  O   . ALA B 1 144 ? 12.085  -2.861  31.669  1.00 17.04  ?  144 ALA B O   1 
ATOM   3228 C  CB  . ALA B 1 144 ? 14.085  -1.894  29.432  1.00 14.24  ?  144 ALA B CB  1 
ATOM   3229 N  N   . THR B 1 145 ? 10.977  -2.962  29.678  1.00 16.40  ?  145 THR B N   1 
ATOM   3230 C  CA  . THR B 1 145 ? 10.089  -4.078  29.954  1.00 16.70  ?  145 THR B CA  1 
ATOM   3231 C  C   . THR B 1 145 ? 10.051  -5.017  28.745  1.00 16.25  ?  145 THR B C   1 
ATOM   3232 O  O   . THR B 1 145 ? 10.260  -4.575  27.600  1.00 13.52  ?  145 THR B O   1 
ATOM   3233 C  CB  . THR B 1 145 ? 8.692   -3.583  30.295  1.00 15.90  ?  145 THR B CB  1 
ATOM   3234 O  OG1 . THR B 1 145 ? 8.230   -2.753  29.244  1.00 18.72  ?  145 THR B OG1 1 
ATOM   3235 C  CG2 . THR B 1 145 ? 8.682   -2.773  31.579  1.00 19.74  ?  145 THR B CG2 1 
ATOM   3236 N  N   . VAL B 1 146 ? 9.748   -6.292  29.020  1.00 14.01  ?  146 VAL B N   1 
ATOM   3237 C  CA  . VAL B 1 146 ? 9.680   -7.354  28.028  1.00 15.76  ?  146 VAL B CA  1 
ATOM   3238 C  C   . VAL B 1 146 ? 8.342   -8.071  28.117  1.00 16.14  ?  146 VAL B C   1 
ATOM   3239 O  O   . VAL B 1 146 ? 7.981   -8.522  29.208  1.00 17.43  ?  146 VAL B O   1 
ATOM   3240 C  CB  . VAL B 1 146 ? 10.814  -8.330  28.332  1.00 16.78  ?  146 VAL B CB  1 
ATOM   3241 C  CG1 . VAL B 1 146 ? 10.735  -9.581  27.488  1.00 17.92  ?  146 VAL B CG1 1 
ATOM   3242 C  CG2 . VAL B 1 146 ? 12.157  -7.627  28.137  1.00 19.49  ?  146 VAL B CG2 1 
ATOM   3243 N  N   . GLY B 1 147 ? 7.686   -8.241  26.961  1.00 13.32  ?  147 GLY B N   1 
ATOM   3244 C  CA  . GLY B 1 147 ? 6.513   -9.084  26.854  1.00 14.87  ?  147 GLY B CA  1 
ATOM   3245 C  C   . GLY B 1 147 ? 5.233   -8.303  27.147  1.00 16.02  ?  147 GLY B C   1 
ATOM   3246 O  O   . GLY B 1 147 ? 4.647   -8.432  28.230  1.00 17.39  ?  147 GLY B O   1 
ATOM   3247 N  N   . LYS B 1 148 ? 4.783   -7.513  26.157  1.00 18.18  ?  148 LYS B N   1 
ATOM   3248 C  CA  . LYS B 1 148 ? 3.718   -6.548  26.374  1.00 18.41  ?  148 LYS B CA  1 
ATOM   3249 C  C   . LYS B 1 148 ? 2.399   -6.914  25.698  1.00 19.07  ?  148 LYS B C   1 
ATOM   3250 O  O   . LYS B 1 148 ? 1.542   -6.055  25.572  1.00 18.32  ?  148 LYS B O   1 
ATOM   3251 C  CB  . LYS B 1 148 ? 4.219   -5.182  25.896  1.00 20.23  ?  148 LYS B CB  1 
ATOM   3252 C  CG  . LYS B 1 148 ? 5.018   -4.613  27.064  1.00 23.14  ?  148 LYS B CG  1 
ATOM   3253 C  CD  . LYS B 1 148 ? 6.036   -3.575  26.671  1.00 25.51  ?  148 LYS B CD  1 
ATOM   3254 C  CE  . LYS B 1 148 ? 7.277   -4.218  26.201  1.00 22.77  ?  148 LYS B CE  1 
ATOM   3255 N  NZ  . LYS B 1 148 ? 8.221   -3.115  26.163  1.00 21.32  1  148 LYS B NZ  1 
ATOM   3256 N  N   . LEU B 1 149 ? 2.215   -8.177  25.315  1.00 17.42  ?  149 LEU B N   1 
ATOM   3257 C  CA  . LEU B 1 149 ? 0.960   -8.618  24.725  1.00 18.42  ?  149 LEU B CA  1 
ATOM   3258 C  C   . LEU B 1 149 ? -0.253  -8.168  25.550  1.00 19.69  ?  149 LEU B C   1 
ATOM   3259 O  O   . LEU B 1 149 ? -1.277  -7.772  24.964  1.00 21.03  ?  149 LEU B O   1 
ATOM   3260 C  CB  . LEU B 1 149 ? 0.969   -10.134 24.545  1.00 19.65  ?  149 LEU B CB  1 
ATOM   3261 C  CG  . LEU B 1 149 ? -0.338  -10.760 24.020  1.00 21.37  ?  149 LEU B CG  1 
ATOM   3262 C  CD1 . LEU B 1 149 ? -0.603  -10.347 22.595  1.00 22.32  ?  149 LEU B CD1 1 
ATOM   3263 C  CD2 . LEU B 1 149 ? -0.351  -12.265 24.138  1.00 21.40  ?  149 LEU B CD2 1 
ATOM   3264 N  N   . TYR B 1 150 ? -0.162  -8.261  26.878  1.00 20.45  ?  150 TYR B N   1 
ATOM   3265 C  CA  . TYR B 1 150 ? -1.284  -7.922  27.754  1.00 22.01  ?  150 TYR B CA  1 
ATOM   3266 C  C   . TYR B 1 150 ? -1.059  -6.579  28.443  1.00 26.78  ?  150 TYR B C   1 
ATOM   3267 O  O   . TYR B 1 150 ? -1.644  -6.328  29.485  1.00 27.39  ?  150 TYR B O   1 
ATOM   3268 C  CB  . TYR B 1 150 ? -1.437  -9.009  28.819  1.00 22.75  ?  150 TYR B CB  1 
ATOM   3269 C  CG  . TYR B 1 150 ? -1.792  -10.373 28.254  1.00 20.57  ?  150 TYR B CG  1 
ATOM   3270 C  CD1 . TYR B 1 150 ? -2.779  -10.531 27.294  1.00 23.11  ?  150 TYR B CD1 1 
ATOM   3271 C  CD2 . TYR B 1 150 ? -1.066  -11.481 28.605  1.00 20.86  ?  150 TYR B CD2 1 
ATOM   3272 C  CE1 . TYR B 1 150 ? -3.074  -11.773 26.754  1.00 24.06  ?  150 TYR B CE1 1 
ATOM   3273 C  CE2 . TYR B 1 150 ? -1.346  -12.727 28.074  1.00 22.74  ?  150 TYR B CE2 1 
ATOM   3274 C  CZ  . TYR B 1 150 ? -2.355  -12.880 27.150  1.00 24.87  ?  150 TYR B CZ  1 
ATOM   3275 O  OH  . TYR B 1 150 ? -2.632  -14.134 26.638  1.00 28.27  ?  150 TYR B OH  1 
ATOM   3276 N  N   . GLY B 1 151 ? -0.180  -5.731  27.896  1.00 25.24  ?  151 GLY B N   1 
ATOM   3277 C  CA  . GLY B 1 151 ? 0.115   -4.472  28.558  1.00 23.76  ?  151 GLY B CA  1 
ATOM   3278 C  C   . GLY B 1 151 ? 1.293   -4.589  29.512  1.00 22.97  ?  151 GLY B C   1 
ATOM   3279 O  O   . GLY B 1 151 ? 1.746   -5.694  29.873  1.00 21.62  ?  151 GLY B O   1 
ATOM   3280 N  N   . VAL B 1 152 ? 1.810   -3.416  29.900  1.00 22.33  ?  152 VAL B N   1 
ATOM   3281 C  CA  . VAL B 1 152 ? 3.002   -3.333  30.724  1.00 24.43  ?  152 VAL B CA  1 
ATOM   3282 C  C   . VAL B 1 152 ? 2.788   -3.936  32.110  1.00 22.00  ?  152 VAL B C   1 
ATOM   3283 O  O   . VAL B 1 152 ? 3.729   -4.384  32.762  1.00 19.28  ?  152 VAL B O   1 
ATOM   3284 C  CB  . VAL B 1 152 ? 3.469   -1.868  30.771  1.00 30.24  ?  152 VAL B CB  1 
ATOM   3285 C  CG1 . VAL B 1 152 ? 2.579   -1.001  31.639  1.00 32.59  ?  152 VAL B CG1 1 
ATOM   3286 C  CG2 . VAL B 1 152 ? 4.905   -1.790  31.216  1.00 34.76  ?  152 VAL B CG2 1 
ATOM   3287 N  N   . ARG B 1 153 ? 1.537   -3.969  32.563  1.00 22.43  ?  153 ARG B N   1 
ATOM   3288 C  CA  . ARG B 1 153 ? 1.239   -4.483  33.887  1.00 28.70  ?  153 ARG B CA  1 
ATOM   3289 C  C   . ARG B 1 153 ? 1.564   -5.983  34.009  1.00 22.82  ?  153 ARG B C   1 
ATOM   3290 O  O   . ARG B 1 153 ? 1.892   -6.461  35.078  1.00 23.29  ?  153 ARG B O   1 
ATOM   3291 C  CB  . ARG B 1 153 ? -0.243  -4.153  34.149  1.00 38.16  ?  153 ARG B CB  1 
ATOM   3292 C  CG  . ARG B 1 153 ? -0.554  -3.652  35.551  1.00 54.05  ?  153 ARG B CG  1 
ATOM   3293 C  CD  . ARG B 1 153 ? -0.490  -4.767  36.597  1.00 69.88  ?  153 ARG B CD  1 
ATOM   3294 N  NE  . ARG B 1 153 ? -1.496  -5.820  36.385  1.00 81.57  ?  153 ARG B NE  1 
ATOM   3295 C  CZ  . ARG B 1 153 ? -2.695  -5.887  36.974  1.00 82.12  ?  153 ARG B CZ  1 
ATOM   3296 N  NH1 . ARG B 1 153 ? -3.103  -4.930  37.792  1.00 76.95  1  153 ARG B NH1 1 
ATOM   3297 N  NH2 . ARG B 1 153 ? -3.499  -6.907  36.724  1.00 81.73  ?  153 ARG B NH2 1 
ATOM   3298 N  N   . GLN B 1 154 ? 1.501   -6.733  32.914  1.00 20.08  ?  154 GLN B N   1 
ATOM   3299 C  CA  . GLN B 1 154 ? 1.794   -8.167  32.934  1.00 19.02  ?  154 GLN B CA  1 
ATOM   3300 C  C   . GLN B 1 154 ? 3.119   -8.489  32.231  1.00 19.36  ?  154 GLN B C   1 
ATOM   3301 O  O   . GLN B 1 154 ? 3.369   -9.641  31.827  1.00 19.98  ?  154 GLN B O   1 
ATOM   3302 C  CB  . GLN B 1 154 ? 0.574   -8.866  32.313  1.00 23.65  ?  154 GLN B CB  1 
ATOM   3303 C  CG  . GLN B 1 154 ? -0.638  -8.834  33.246  1.00 27.93  ?  154 GLN B CG  1 
ATOM   3304 C  CD  . GLN B 1 154 ? -1.886  -9.470  32.669  1.00 30.83  ?  154 GLN B CD  1 
ATOM   3305 O  OE1 . GLN B 1 154 ? -2.966  -8.875  32.667  1.00 36.90  ?  154 GLN B OE1 1 
ATOM   3306 N  NE2 . GLN B 1 154 ? -1.783  -10.696 32.173  1.00 33.48  ?  154 GLN B NE2 1 
ATOM   3307 N  N   . SER B 1 155 ? 4.005   -7.496  32.154  1.00 18.60  ?  155 SER B N   1 
ATOM   3308 C  CA  . SER B 1 155 ? 5.298   -7.679  31.514  1.00 17.75  ?  155 SER B CA  1 
ATOM   3309 C  C   . SER B 1 155 ? 6.337   -8.124  32.523  1.00 18.23  ?  155 SER B C   1 
ATOM   3310 O  O   . SER B 1 155 ? 6.117   -8.053  33.728  1.00 20.23  ?  155 SER B O   1 
ATOM   3311 C  CB  . SER B 1 155 ? 5.751   -6.405  30.803  1.00 19.84  ?  155 SER B CB  1 
ATOM   3312 O  OG  . SER B 1 155 ? 5.996   -5.364  31.747  1.00 19.42  ?  155 SER B OG  1 
ATOM   3313 N  N   . SER B 1 156 ? 7.512   -8.507  32.011  1.00 16.21  ?  156 SER B N   1 
ATOM   3314 C  CA  . SER B 1 156 ? 8.664   -8.803  32.821  1.00 16.70  ?  156 SER B CA  1 
ATOM   3315 C  C   . SER B 1 156 ? 9.623   -7.620  32.731  1.00 20.11  ?  156 SER B C   1 
ATOM   3316 O  O   . SER B 1 156 ? 9.570   -6.857  31.768  1.00 17.27  ?  156 SER B O   1 
ATOM   3317 C  CB  . SER B 1 156 ? 9.364   -10.062 32.355  1.00 18.19  ?  156 SER B CB  1 
ATOM   3318 O  OG  . SER B 1 156 ? 8.536   -11.205 32.469  1.00 19.88  ?  156 SER B OG  1 
ATOM   3319 N  N   . PRO B 1 157 ? 10.539  -7.436  33.718  1.00 21.23  ?  157 PRO B N   1 
ATOM   3320 C  CA  . PRO B 1 157 ? 11.554  -6.402  33.603  1.00 21.62  ?  157 PRO B CA  1 
ATOM   3321 C  C   . PRO B 1 157 ? 12.521  -6.689  32.459  1.00 20.49  ?  157 PRO B C   1 
ATOM   3322 O  O   . PRO B 1 157 ? 12.876  -7.849  32.223  1.00 18.50  ?  157 PRO B O   1 
ATOM   3323 C  CB  . PRO B 1 157 ? 12.290  -6.447  34.939  1.00 25.92  ?  157 PRO B CB  1 
ATOM   3324 C  CG  . PRO B 1 157 ? 11.267  -7.141  35.870  1.00 26.11  ?  157 PRO B CG  1 
ATOM   3325 C  CD  . PRO B 1 157 ? 10.585  -8.150  35.007  1.00 22.59  ?  157 PRO B CD  1 
ATOM   3326 N  N   . GLY B 1 158 ? 12.906  -5.625  31.729  1.00 17.82  ?  158 GLY B N   1 
ATOM   3327 C  CA  . GLY B 1 158 ? 13.964  -5.711  30.748  1.00 16.50  ?  158 GLY B CA  1 
ATOM   3328 C  C   . GLY B 1 158 ? 15.259  -5.147  31.324  1.00 17.08  ?  158 GLY B C   1 
ATOM   3329 O  O   . GLY B 1 158 ? 15.452  -5.169  32.527  1.00 17.34  ?  158 GLY B O   1 
ATOM   3330 N  N   . GLY B 1 159 ? 16.114  -4.605  30.468  1.00 14.26  ?  159 GLY B N   1 
ATOM   3331 C  CA  . GLY B 1 159 ? 17.350  -4.017  30.919  1.00 13.96  ?  159 GLY B CA  1 
ATOM   3332 C  C   . GLY B 1 159 ? 18.339  -3.815  29.780  1.00 14.40  ?  159 GLY B C   1 
ATOM   3333 O  O   . GLY B 1 159 ? 18.028  -3.996  28.598  1.00 15.30  ?  159 GLY B O   1 
ATOM   3334 N  N   . LEU B 1 160 ? 19.538  -3.479  30.217  1.00 14.18  ?  160 LEU B N   1 
ATOM   3335 C  CA  . LEU B 1 160 ? 20.697  -3.271  29.382  1.00 14.45  ?  160 LEU B CA  1 
ATOM   3336 C  C   . LEU B 1 160 ? 21.676  -4.397  29.689  1.00 15.03  ?  160 LEU B C   1 
ATOM   3337 O  O   . LEU B 1 160 ? 21.923  -4.694  30.858  1.00 15.73  ?  160 LEU B O   1 
ATOM   3338 C  CB  . LEU B 1 160 ? 21.290  -1.880  29.645  1.00 15.05  ?  160 LEU B CB  1 
ATOM   3339 C  CG  . LEU B 1 160 ? 22.581  -1.548  28.876  1.00 16.89  ?  160 LEU B CG  1 
ATOM   3340 C  CD1 . LEU B 1 160 ? 22.641  -0.093  28.582  1.00 19.44  ?  160 LEU B CD1 1 
ATOM   3341 C  CD2 . LEU B 1 160 ? 23.846  -1.986  29.590  1.00 17.68  ?  160 LEU B CD2 1 
ATOM   3342 N  N   . GLY B 1 161 ? 22.141  -5.070  28.639  1.00 13.38  ?  161 GLY B N   1 
ATOM   3343 C  CA  . GLY B 1 161 ? 23.078  -6.171  28.758  1.00 14.30  ?  161 GLY B CA  1 
ATOM   3344 C  C   . GLY B 1 161 ? 24.274  -6.029  27.822  1.00 14.09  ?  161 GLY B C   1 
ATOM   3345 O  O   . GLY B 1 161 ? 24.291  -5.205  26.918  1.00 13.72  ?  161 GLY B O   1 
ATOM   3346 N  N   . THR B 1 162 ? 25.304  -6.827  28.074  1.00 13.20  ?  162 THR B N   1 
ATOM   3347 C  CA  . THR B 1 162 ? 26.499  -6.774  27.253  1.00 13.80  ?  162 THR B CA  1 
ATOM   3348 C  C   . THR B 1 162 ? 27.148  -8.158  27.215  1.00 15.07  ?  162 THR B C   1 
ATOM   3349 O  O   . THR B 1 162 ? 26.952  -8.958  28.144  1.00 15.41  ?  162 THR B O   1 
ATOM   3350 C  CB  . THR B 1 162 ? 27.430  -5.682  27.777  1.00 13.27  ?  162 THR B CB  1 
ATOM   3351 O  OG1 . THR B 1 162 ? 28.490  -5.433  26.858  1.00 13.10  ?  162 THR B OG1 1 
ATOM   3352 C  CG2 . THR B 1 162 ? 28.049  -6.060  29.102  1.00 14.08  ?  162 THR B CG2 1 
ATOM   3353 N  N   . ALA B 1 163 ? 27.957  -8.413  26.180  1.00 13.91  ?  163 ALA B N   1 
ATOM   3354 C  CA  . ALA B 1 163 ? 28.724  -9.649  26.039  1.00 14.64  ?  163 ALA B CA  1 
ATOM   3355 C  C   . ALA B 1 163 ? 29.871  -9.424  25.052  1.00 14.42  ?  163 ALA B C   1 
ATOM   3356 O  O   . ALA B 1 163 ? 29.801  -8.538  24.209  1.00 14.30  ?  163 ALA B O   1 
ATOM   3357 C  CB  . ALA B 1 163 ? 27.836  -10.774 25.545  1.00 15.55  ?  163 ALA B CB  1 
ATOM   3358 N  N   . THR B 1 164 ? 30.946  -10.178 25.214  1.00 15.75  ?  164 THR B N   1 
ATOM   3359 C  CA  . THR B 1 164 ? 32.073  -10.180 24.291  1.00 15.52  ?  164 THR B CA  1 
ATOM   3360 C  C   . THR B 1 164 ? 32.272  -11.603 23.780  1.00 17.45  ?  164 THR B C   1 
ATOM   3361 O  O   . THR B 1 164 ? 32.246  -12.529 24.565  1.00 16.74  ?  164 THR B O   1 
ATOM   3362 C  CB  . THR B 1 164 ? 33.330  -9.689  25.005  1.00 16.80  ?  164 THR B CB  1 
ATOM   3363 O  OG1 . THR B 1 164 ? 33.134  -8.307  25.317  1.00 16.48  ?  164 THR B OG1 1 
ATOM   3364 C  CG2 . THR B 1 164 ? 34.562  -9.816  24.125  1.00 18.66  ?  164 THR B CG2 1 
ATOM   3365 N  N   . VAL B 1 165 ? 32.450  -11.745 22.463  1.00 17.86  ?  165 VAL B N   1 
ATOM   3366 C  CA  . VAL B 1 165 ? 32.857  -12.988 21.821  1.00 18.90  ?  165 VAL B CA  1 
ATOM   3367 C  C   . VAL B 1 165 ? 34.297  -12.832 21.335  1.00 18.82  ?  165 VAL B C   1 
ATOM   3368 O  O   . VAL B 1 165 ? 34.633  -11.872 20.629  1.00 18.44  ?  165 VAL B O   1 
ATOM   3369 C  CB  . VAL B 1 165 ? 31.901  -13.325 20.664  1.00 20.79  ?  165 VAL B CB  1 
ATOM   3370 C  CG1 . VAL B 1 165 ? 32.355  -14.534 19.862  1.00 24.87  ?  165 VAL B CG1 1 
ATOM   3371 C  CG2 . VAL B 1 165 ? 30.466  -13.524 21.156  1.00 19.19  ?  165 VAL B CG2 1 
ATOM   3372 N  N   . SER B 1 166 ? 35.142  -13.796 21.700  1.00 19.27  ?  166 SER B N   1 
ATOM   3373 C  CA  . SER B 1 166 ? 36.549  -13.834 21.292  1.00 20.29  ?  166 SER B CA  1 
ATOM   3374 C  C   . SER B 1 166 ? 36.736  -14.783 20.123  1.00 22.12  ?  166 SER B C   1 
ATOM   3375 O  O   . SER B 1 166 ? 36.243  -15.908 20.145  1.00 23.98  ?  166 SER B O   1 
ATOM   3376 C  CB  . SER B 1 166 ? 37.455  -14.291 22.400  1.00 23.82  ?  166 SER B CB  1 
ATOM   3377 O  OG  . SER B 1 166 ? 37.307  -13.447 23.508  1.00 30.94  ?  166 SER B OG  1 
ATOM   3378 N  N   . LEU B 1 167 ? 37.450  -14.312 19.102  1.00 20.01  ?  167 LEU B N   1 
ATOM   3379 C  CA  . LEU B 1 167 ? 37.824  -15.126 17.964  1.00 24.18  ?  167 LEU B CA  1 
ATOM   3380 C  C   . LEU B 1 167 ? 39.346  -15.315 18.049  1.00 23.35  ?  167 LEU B C   1 
ATOM   3381 O  O   . LEU B 1 167 ? 39.974  -14.853 18.986  1.00 24.61  ?  167 LEU B O   1 
ATOM   3382 C  CB  . LEU B 1 167 ? 37.424  -14.474 16.640  1.00 23.36  ?  167 LEU B CB  1 
ATOM   3383 C  CG  . LEU B 1 167 ? 35.969  -14.028 16.500  1.00 30.97  ?  167 LEU B CG  1 
ATOM   3384 C  CD1 . LEU B 1 167 ? 35.663  -13.618 15.057  1.00 35.52  ?  167 LEU B CD1 1 
ATOM   3385 C  CD2 . LEU B 1 167 ? 35.070  -15.104 16.947  1.00 32.69  ?  167 LEU B CD2 1 
ATOM   3386 N  N   . TYR B 1 168 ? 39.921  -15.938 17.036  1.00 25.02  ?  168 TYR B N   1 
ATOM   3387 C  CA  . TYR B 1 168 ? 41.369  -16.127 16.930  1.00 26.60  ?  168 TYR B CA  1 
ATOM   3388 C  C   . TYR B 1 168 ? 42.088  -14.791 16.771  1.00 26.13  ?  168 TYR B C   1 
ATOM   3389 O  O   . TYR B 1 168 ? 41.538  -13.799 16.297  1.00 26.29  ?  168 TYR B O   1 
ATOM   3390 C  CB  . TYR B 1 168 ? 41.614  -17.049 15.729  1.00 24.47  ?  168 TYR B CB  1 
ATOM   3391 C  CG  . TYR B 1 168 ? 41.239  -16.463 14.370  1.00 24.93  ?  168 TYR B CG  1 
ATOM   3392 C  CD1 . TYR B 1 168 ? 42.111  -15.658 13.651  1.00 25.75  ?  168 TYR B CD1 1 
ATOM   3393 C  CD2 . TYR B 1 168 ? 39.973  -16.686 13.826  1.00 25.82  ?  168 TYR B CD2 1 
ATOM   3394 C  CE1 . TYR B 1 168 ? 41.747  -15.107 12.428  1.00 24.65  ?  168 TYR B CE1 1 
ATOM   3395 C  CE2 . TYR B 1 168 ? 39.607  -16.158 12.607  1.00 25.04  ?  168 TYR B CE2 1 
ATOM   3396 C  CZ  . TYR B 1 168 ? 40.497  -15.374 11.903  1.00 26.03  ?  168 TYR B CZ  1 
ATOM   3397 O  OH  . TYR B 1 168 ? 40.080  -14.846 10.713  1.00 25.82  ?  168 TYR B OH  1 
ATOM   3398 N  N   . GLY B 1 169 ? 43.380  -14.777 17.132  1.00 25.01  ?  169 GLY B N   1 
ATOM   3399 C  CA  . GLY B 1 169 ? 44.265  -13.699 16.731  1.00 25.46  ?  169 GLY B CA  1 
ATOM   3400 C  C   . GLY B 1 169 ? 44.011  -12.361 17.423  1.00 23.61  ?  169 GLY B C   1 
ATOM   3401 O  O   . GLY B 1 169 ? 44.389  -11.328 16.891  1.00 26.19  ?  169 GLY B O   1 
ATOM   3402 N  N   . GLY B 1 170 ? 43.360  -12.370 18.588  1.00 19.56  ?  170 GLY B N   1 
ATOM   3403 C  CA  . GLY B 1 170 ? 43.103  -11.150 19.324  1.00 20.68  ?  170 GLY B CA  1 
ATOM   3404 C  C   . GLY B 1 170 ? 41.839  -10.430 18.842  1.00 19.56  ?  170 GLY B C   1 
ATOM   3405 O  O   . GLY B 1 170 ? 41.544  -9.343  19.306  1.00 19.49  ?  170 GLY B O   1 
ATOM   3406 N  N   . ILE B 1 171 ? 41.088  -11.048 17.941  1.00 17.55  ?  171 ILE B N   1 
ATOM   3407 C  CA  . ILE B 1 171 ? 39.889  -10.429 17.386  1.00 17.83  ?  171 ILE B CA  1 
ATOM   3408 C  C   . ILE B 1 171 ? 38.780  -10.549 18.429  1.00 16.59  ?  171 ILE B C   1 
ATOM   3409 O  O   . ILE B 1 171 ? 38.619  -11.601 19.054  1.00 17.92  ?  171 ILE B O   1 
ATOM   3410 C  CB  . ILE B 1 171 ? 39.491  -11.069 16.038  1.00 18.44  ?  171 ILE B CB  1 
ATOM   3411 C  CG1 . ILE B 1 171 ? 40.507  -10.774 14.962  1.00 18.90  ?  171 ILE B CG1 1 
ATOM   3412 C  CG2 . ILE B 1 171 ? 38.110  -10.595 15.592  1.00 19.81  ?  171 ILE B CG2 1 
ATOM   3413 C  CD1 . ILE B 1 171 ? 40.472  -11.758 13.818  1.00 21.43  ?  171 ILE B CD1 1 
ATOM   3414 N  N   . LYS B 1 172 ? 38.017  -9.465  18.624  1.00 17.02  ?  172 LYS B N   1 
ATOM   3415 C  CA  . LYS B 1 172 ? 36.882  -9.457  19.542  1.00 17.57  ?  172 LYS B CA  1 
ATOM   3416 C  C   . LYS B 1 172 ? 35.673  -8.821  18.840  1.00 15.51  ?  172 LYS B C   1 
ATOM   3417 O  O   . LYS B 1 172 ? 35.808  -7.912  18.038  1.00 15.17  ?  172 LYS B O   1 
ATOM   3418 C  CB  . LYS B 1 172 ? 37.186  -8.687  20.829  1.00 21.54  ?  172 LYS B CB  1 
ATOM   3419 C  CG  . LYS B 1 172 ? 38.275  -9.316  21.712  1.00 27.77  ?  172 LYS B CG  1 
ATOM   3420 C  CD  . LYS B 1 172 ? 38.673  -8.518  22.937  1.00 36.81  ?  172 LYS B CD  1 
ATOM   3421 C  CE  . LYS B 1 172 ? 39.871  -9.125  23.609  1.00 44.86  ?  172 LYS B CE  1 
ATOM   3422 N  NZ  . LYS B 1 172 ? 39.799  -10.593 23.688  1.00 52.50  1  172 LYS B NZ  1 
ATOM   3423 N  N   . VAL B 1 173 ? 34.494  -9.286  19.215  1.00 15.76  ?  173 VAL B N   1 
ATOM   3424 C  CA  . VAL B 1 173 ? 33.251  -8.643  18.840  1.00 15.93  ?  173 VAL B CA  1 
ATOM   3425 C  C   . VAL B 1 173 ? 32.392  -8.532  20.091  1.00 13.75  ?  173 VAL B C   1 
ATOM   3426 O  O   . VAL B 1 173 ? 32.220  -9.535  20.765  1.00 15.46  ?  173 VAL B O   1 
ATOM   3427 C  CB  . VAL B 1 173 ? 32.547  -9.473  17.751  1.00 17.20  ?  173 VAL B CB  1 
ATOM   3428 C  CG1 . VAL B 1 173 ? 31.225  -8.827  17.387  1.00 18.80  ?  173 VAL B CG1 1 
ATOM   3429 C  CG2 . VAL B 1 173 ? 33.402  -9.643  16.507  1.00 17.06  ?  173 VAL B CG2 1 
ATOM   3430 N  N   . SER B 1 174 ? 31.952  -7.318  20.445  1.00 14.02  ?  174 SER B N   1 
ATOM   3431 C  CA  . SER B 1 174 ? 31.194  -7.110  21.669  1.00 14.85  ?  174 SER B CA  1 
ATOM   3432 C  C   . SER B 1 174 ? 29.848  -6.476  21.338  1.00 15.11  ?  174 SER B C   1 
ATOM   3433 O  O   . SER B 1 174 ? 29.717  -5.780  20.323  1.00 15.62  ?  174 SER B O   1 
ATOM   3434 C  CB  . SER B 1 174 ? 31.925  -6.261  22.700  1.00 17.90  ?  174 SER B CB  1 
ATOM   3435 O  OG  . SER B 1 174 ? 33.218  -6.790  22.961  1.00 23.65  ?  174 SER B OG  1 
ATOM   3436 N  N   . ALA B 1 175 ? 28.900  -6.617  22.260  1.00 12.64  ?  175 ALA B N   1 
ATOM   3437 C  CA  . ALA B 1 175 ? 27.606  -6.002  22.047  1.00 13.67  ?  175 ALA B CA  1 
ATOM   3438 C  C   . ALA B 1 175 ? 27.147  -5.347  23.339  1.00 14.44  ?  175 ALA B C   1 
ATOM   3439 O  O   . ALA B 1 175 ? 27.471  -5.851  24.413  1.00 15.88  ?  175 ALA B O   1 
ATOM   3440 C  CB  . ALA B 1 175 ? 26.586  -7.029  21.590  1.00 14.03  ?  175 ALA B CB  1 
ATOM   3441 N  N   . MET B 1 176 ? 26.310  -4.324  23.185  1.00 13.74  ?  176 MET B N   1 
ATOM   3442 C  CA  . MET B 1 176 ? 25.563  -3.696  24.261  1.00 13.06  ?  176 MET B CA  1 
ATOM   3443 C  C   . MET B 1 176 ? 24.140  -3.471  23.757  1.00 12.05  ?  176 MET B C   1 
ATOM   3444 O  O   . MET B 1 176 ? 23.948  -2.790  22.756  1.00 12.84  ?  176 MET B O   1 
ATOM   3445 C  CB  . MET B 1 176 ? 26.224  -2.387  24.727  1.00 14.98  ?  176 MET B CB  1 
ATOM   3446 C  CG  . MET B 1 176 ? 25.488  -1.662  25.848  1.00 17.01  ?  176 MET B CG  1 
ATOM   3447 S  SD  . MET B 1 176 ? 26.451  -0.278  26.508  1.00 19.26  ?  176 MET B SD  1 
ATOM   3448 C  CE  . MET B 1 176 ? 26.201  0.889   25.173  1.00 22.21  ?  176 MET B CE  1 
ATOM   3449 N  N   . ILE B 1 177 ? 23.158  -4.012  24.472  1.00 11.96  ?  177 ILE B N   1 
ATOM   3450 C  CA  . ILE B 1 177 ? 21.782  -4.103  23.983  1.00 12.96  ?  177 ILE B CA  1 
ATOM   3451 C  C   . ILE B 1 177 ? 20.837  -3.614  25.082  1.00 13.88  ?  177 ILE B C   1 
ATOM   3452 O  O   . ILE B 1 177 ? 20.972  -4.007  26.244  1.00 15.31  ?  177 ILE B O   1 
ATOM   3453 C  CB  . ILE B 1 177 ? 21.423  -5.557  23.579  1.00 16.22  ?  177 ILE B CB  1 
ATOM   3454 C  CG1 . ILE B 1 177 ? 22.400  -6.210  22.554  1.00 18.82  ?  177 ILE B CG1 1 
ATOM   3455 C  CG2 . ILE B 1 177 ? 19.969  -5.690  23.120  1.00 16.36  ?  177 ILE B CG2 1 
ATOM   3456 C  CD1 . ILE B 1 177 ? 22.354  -5.647  21.163  1.00 21.78  ?  177 ILE B CD1 1 
ATOM   3457 N  N   . VAL B 1 178 ? 19.846  -2.795  24.712  1.00 12.97  ?  178 VAL B N   1 
ATOM   3458 C  CA  . VAL B 1 178 ? 18.721  -2.507  25.574  1.00 13.22  ?  178 VAL B CA  1 
ATOM   3459 C  C   . VAL B 1 178 ? 17.532  -3.348  25.104  1.00 13.52  ?  178 VAL B C   1 
ATOM   3460 O  O   . VAL B 1 178 ? 17.099  -3.190  23.971  1.00 13.99  ?  178 VAL B O   1 
ATOM   3461 C  CB  . VAL B 1 178 ? 18.403  -0.999  25.571  1.00 14.73  ?  178 VAL B CB  1 
ATOM   3462 C  CG1 . VAL B 1 178 ? 17.106  -0.692  26.308  1.00 15.69  ?  178 VAL B CG1 1 
ATOM   3463 C  CG2 . VAL B 1 178 ? 19.544  -0.191  26.168  1.00 15.05  ?  178 VAL B CG2 1 
ATOM   3464 N  N   . VAL B 1 179 ? 17.018  -4.228  25.962  1.00 13.57  ?  179 VAL B N   1 
ATOM   3465 C  CA  . VAL B 1 179 ? 15.911  -5.107  25.633  1.00 15.26  ?  179 VAL B CA  1 
ATOM   3466 C  C   . VAL B 1 179 ? 14.628  -4.534  26.223  1.00 14.54  ?  179 VAL B C   1 
ATOM   3467 O  O   . VAL B 1 179 ? 14.474  -4.562  27.431  1.00 13.61  ?  179 VAL B O   1 
ATOM   3468 C  CB  . VAL B 1 179 ? 16.120  -6.551  26.129  1.00 19.54  ?  179 VAL B CB  1 
ATOM   3469 C  CG1 . VAL B 1 179 ? 14.974  -7.445  25.659  1.00 19.87  ?  179 VAL B CG1 1 
ATOM   3470 C  CG2 . VAL B 1 179 ? 17.445  -7.103  25.648  1.00 23.49  ?  179 VAL B CG2 1 
ATOM   3471 N  N   . ASN B 1 180 ? 13.713  -4.107  25.339  1.00 14.47  ?  180 ASN B N   1 
ATOM   3472 C  CA  . ASN B 1 180 ? 12.402  -3.569  25.687  1.00 14.33  ?  180 ASN B CA  1 
ATOM   3473 C  C   . ASN B 1 180 ? 11.365  -4.216  24.775  1.00 12.70  ?  180 ASN B C   1 
ATOM   3474 O  O   . ASN B 1 180 ? 10.446  -3.575  24.278  1.00 12.13  ?  180 ASN B O   1 
ATOM   3475 C  CB  . ASN B 1 180 ? 12.412  -2.026  25.586  1.00 15.28  ?  180 ASN B CB  1 
ATOM   3476 C  CG  . ASN B 1 180 ? 11.163  -1.337  26.120  1.00 15.64  ?  180 ASN B CG  1 
ATOM   3477 O  OD1 . ASN B 1 180 ? 10.823  -1.423  27.304  1.00 16.20  ?  180 ASN B OD1 1 
ATOM   3478 N  ND2 . ASN B 1 180 ? 10.468  -0.586  25.292  1.00 15.45  ?  180 ASN B ND2 1 
ATOM   3479 N  N   . SER B 1 181 ? 11.574  -5.497  24.482  1.00 13.34  ?  181 SER B N   1 
ATOM   3480 C  CA  . SER B 1 181 ? 10.949  -6.144  23.350  1.00 12.75  ?  181 SER B CA  1 
ATOM   3481 C  C   . SER B 1 181 ? 9.458   -6.329  23.610  1.00 14.03  ?  181 SER B C   1 
ATOM   3482 O  O   . SER B 1 181 ? 9.039   -6.601  24.746  1.00 13.10  ?  181 SER B O   1 
ATOM   3483 C  CB  . SER B 1 181 ? 11.619  -7.473  23.077  1.00 15.08  ?  181 SER B CB  1 
ATOM   3484 O  OG  . SER B 1 181 ? 11.613  -8.299  24.238  1.00 16.77  ?  181 SER B OG  1 
ATOM   3485 N  N   . PHE B 1 182 ? 8.677   -6.214  22.537  1.00 13.12  ?  182 PHE B N   1 
ATOM   3486 C  CA  . PHE B 1 182 ? 7.282   -6.626  22.581  1.00 13.72  ?  182 PHE B CA  1 
ATOM   3487 C  C   . PHE B 1 182 ? 7.202   -8.128  22.913  1.00 13.88  ?  182 PHE B C   1 
ATOM   3488 O  O   . PHE B 1 182 ? 6.379   -8.555  23.731  1.00 13.15  ?  182 PHE B O   1 
ATOM   3489 C  CB  . PHE B 1 182 ? 6.598   -6.320  21.250  1.00 13.91  ?  182 PHE B CB  1 
ATOM   3490 C  CG  . PHE B 1 182 ? 5.215   -6.961  21.213  1.00 15.96  ?  182 PHE B CG  1 
ATOM   3491 C  CD1 . PHE B 1 182 ? 4.160   -6.394  21.914  1.00 17.28  ?  182 PHE B CD1 1 
ATOM   3492 C  CD2 . PHE B 1 182 ? 5.000   -8.157  20.540  1.00 16.50  ?  182 PHE B CD2 1 
ATOM   3493 C  CE1 . PHE B 1 182 ? 2.904   -7.017  21.929  1.00 18.82  ?  182 PHE B CE1 1 
ATOM   3494 C  CE2 . PHE B 1 182 ? 3.748   -8.771  20.587  1.00 20.19  ?  182 PHE B CE2 1 
ATOM   3495 C  CZ  . PHE B 1 182 ? 2.705   -8.169  21.233  1.00 17.05  ?  182 PHE B CZ  1 
ATOM   3496 N  N   . GLY B 1 183 ? 8.079   -8.916  22.283  1.00 13.50  ?  183 GLY B N   1 
ATOM   3497 C  CA  . GLY B 1 183 ? 8.060   -10.361 22.368  1.00 14.00  ?  183 GLY B CA  1 
ATOM   3498 C  C   . GLY B 1 183 ? 8.764   -10.907 23.614  1.00 15.14  ?  183 GLY B C   1 
ATOM   3499 O  O   . GLY B 1 183 ? 9.274   -10.138 24.440  1.00 15.62  ?  183 GLY B O   1 
ATOM   3500 N  N   . ASP B 1 184 ? 8.766   -12.255 23.718  1.00 14.18  ?  184 ASP B N   1 
ATOM   3501 C  CA  . ASP B 1 184 ? 9.371   -12.963 24.828  1.00 14.67  ?  184 ASP B CA  1 
ATOM   3502 C  C   . ASP B 1 184 ? 10.831  -13.281 24.509  1.00 15.44  ?  184 ASP B C   1 
ATOM   3503 O  O   . ASP B 1 184 ? 11.211  -13.409 23.354  1.00 16.84  ?  184 ASP B O   1 
ATOM   3504 C  CB  . ASP B 1 184 ? 8.665   -14.293 25.056  1.00 15.29  ?  184 ASP B CB  1 
ATOM   3505 C  CG  . ASP B 1 184 ? 7.174   -14.217 25.382  1.00 15.84  ?  184 ASP B CG  1 
ATOM   3506 O  OD1 . ASP B 1 184 ? 6.744   -13.196 25.898  1.00 16.17  ?  184 ASP B OD1 1 
ATOM   3507 O  OD2 . ASP B 1 184 ? 6.471   -15.157 25.002  1.00 17.24  -1 184 ASP B OD2 1 
ATOM   3508 N  N   . LEU B 1 185 ? 11.630  -13.424 25.548  1.00 15.70  ?  185 LEU B N   1 
ATOM   3509 C  CA  . LEU B 1 185 ? 13.038  -13.768 25.465  1.00 18.44  ?  185 LEU B CA  1 
ATOM   3510 C  C   . LEU B 1 185 ? 13.175  -15.212 25.934  1.00 19.36  ?  185 LEU B C   1 
ATOM   3511 O  O   . LEU B 1 185 ? 12.603  -15.583 26.970  1.00 19.19  ?  185 LEU B O   1 
ATOM   3512 C  CB  . LEU B 1 185 ? 13.727  -12.758 26.366  1.00 21.76  ?  185 LEU B CB  1 
ATOM   3513 C  CG  . LEU B 1 185 ? 15.250  -12.728 26.368  1.00 31.42  ?  185 LEU B CG  1 
ATOM   3514 C  CD1 . LEU B 1 185 ? 15.705  -12.095 25.095  1.00 32.98  ?  185 LEU B CD1 1 
ATOM   3515 C  CD2 . LEU B 1 185 ? 15.771  -11.933 27.561  1.00 35.43  ?  185 LEU B CD2 1 
ATOM   3516 N  N   . ARG B 1 186 ? 13.859  -16.011 25.129  1.00 19.91  ?  186 ARG B N   1 
ATOM   3517 C  CA  . ARG B 1 186 ? 14.094  -17.432 25.345  1.00 25.21  ?  186 ARG B CA  1 
ATOM   3518 C  C   . ARG B 1 186 ? 15.600  -17.709 25.400  1.00 26.56  ?  186 ARG B C   1 
ATOM   3519 O  O   . ARG B 1 186 ? 16.402  -16.991 24.798  1.00 25.65  ?  186 ARG B O   1 
ATOM   3520 C  CB  . ARG B 1 186 ? 13.564  -18.246 24.161  1.00 28.65  ?  186 ARG B CB  1 
ATOM   3521 C  CG  . ARG B 1 186 ? 12.051  -18.372 24.203  1.00 35.15  ?  186 ARG B CG  1 
ATOM   3522 C  CD  . ARG B 1 186 ? 11.503  -19.081 22.963  1.00 38.98  ?  186 ARG B CD  1 
ATOM   3523 N  NE  . ARG B 1 186 ? 10.107  -18.667 22.750  1.00 49.25  ?  186 ARG B NE  1 
ATOM   3524 C  CZ  . ARG B 1 186 ? 9.028   -19.283 23.189  1.00 51.35  ?  186 ARG B CZ  1 
ATOM   3525 N  NH1 . ARG B 1 186 ? 9.132   -20.404 23.888  1.00 60.66  1  186 ARG B NH1 1 
ATOM   3526 N  NH2 . ARG B 1 186 ? 7.841   -18.762 22.930  1.00 51.87  ?  186 ARG B NH2 1 
ATOM   3527 N  N   . ASP B 1 187 ? 15.975  -18.760 26.124  1.00 29.83  ?  187 ASP B N   1 
ATOM   3528 C  CA  . ASP B 1 187 ? 17.359  -19.249 26.110  1.00 35.78  ?  187 ASP B CA  1 
ATOM   3529 C  C   . ASP B 1 187 ? 17.589  -20.140 24.886  1.00 45.58  ?  187 ASP B C   1 
ATOM   3530 O  O   . ASP B 1 187 ? 16.743  -20.218 23.982  1.00 41.55  ?  187 ASP B O   1 
ATOM   3531 C  CB  . ASP B 1 187 ? 17.734  -19.914 27.425  1.00 37.93  ?  187 ASP B CB  1 
ATOM   3532 C  CG  . ASP B 1 187 ? 16.972  -21.189 27.736  1.00 35.81  ?  187 ASP B CG  1 
ATOM   3533 O  OD1 . ASP B 1 187 ? 16.422  -21.808 26.773  1.00 44.94  ?  187 ASP B OD1 1 
ATOM   3534 O  OD2 . ASP B 1 187 ? 16.804  -21.446 28.933  1.00 34.36  -1 187 ASP B OD2 1 
ATOM   3535 N  N   . THR B 1 188 ? 18.763  -20.794 24.834  1.00 50.83  ?  188 THR B N   1 
ATOM   3536 C  CA  . THR B 1 188 ? 19.196  -21.493 23.625  1.00 58.99  ?  188 THR B CA  1 
ATOM   3537 C  C   . THR B 1 188 ? 18.432  -22.806 23.452  1.00 54.89  ?  188 THR B C   1 
ATOM   3538 O  O   . THR B 1 188 ? 18.313  -23.298 22.330  1.00 58.76  ?  188 THR B O   1 
ATOM   3539 C  CB  . THR B 1 188 ? 20.712  -21.714 23.637  1.00 64.82  ?  188 THR B CB  1 
ATOM   3540 O  OG1 . THR B 1 188 ? 21.083  -22.146 24.944  1.00 61.42  ?  188 THR B OG1 1 
ATOM   3541 C  CG2 . THR B 1 188 ? 21.474  -20.435 23.335  1.00 64.94  ?  188 THR B CG2 1 
ATOM   3542 N  N   . ALA B 1 189 ? 17.895  -23.338 24.561  1.00 53.94  ?  189 ALA B N   1 
ATOM   3543 C  CA  . ALA B 1 189 ? 17.023  -24.504 24.540  1.00 55.83  ?  189 ALA B CA  1 
ATOM   3544 C  C   . ALA B 1 189 ? 15.599  -24.147 24.104  1.00 55.84  ?  189 ALA B C   1 
ATOM   3545 O  O   . ALA B 1 189 ? 14.833  -25.046 23.770  1.00 51.34  ?  189 ALA B O   1 
ATOM   3546 C  CB  . ALA B 1 189 ? 16.990  -25.117 25.923  1.00 58.38  ?  189 ALA B CB  1 
ATOM   3547 N  N   . GLY B 1 190 ? 15.222  -22.861 24.188  1.00 53.13  ?  190 GLY B N   1 
ATOM   3548 C  CA  . GLY B 1 190 ? 13.879  -22.425 23.827  1.00 47.84  ?  190 GLY B CA  1 
ATOM   3549 C  C   . GLY B 1 190 ? 12.937  -22.261 25.030  1.00 39.13  ?  190 GLY B C   1 
ATOM   3550 O  O   . GLY B 1 190 ? 11.730  -22.167 24.844  1.00 40.28  ?  190 GLY B O   1 
ATOM   3551 N  N   . ARG B 1 191 ? 13.461  -22.171 26.256  1.00 34.97  ?  191 ARG B N   1 
ATOM   3552 C  CA  . ARG B 1 191 ? 12.651  -21.841 27.426  1.00 36.00  ?  191 ARG B CA  1 
ATOM   3553 C  C   . ARG B 1 191 ? 12.465  -20.322 27.611  1.00 29.68  ?  191 ARG B C   1 
ATOM   3554 O  O   . ARG B 1 191 ? 13.421  -19.569 27.523  1.00 27.95  ?  191 ARG B O   1 
ATOM   3555 C  CB  . ARG B 1 191 ? 13.426  -22.336 28.640  1.00 40.94  ?  191 ARG B CB  1 
ATOM   3556 C  CG  . ARG B 1 191 ? 12.781  -22.412 30.012  1.00 52.63  ?  191 ARG B CG  1 
ATOM   3557 C  CD  . ARG B 1 191 ? 13.762  -23.066 31.006  1.00 61.47  ?  191 ARG B CD  1 
ATOM   3558 N  NE  . ARG B 1 191 ? 14.646  -24.013 30.308  1.00 74.57  ?  191 ARG B NE  1 
ATOM   3559 C  CZ  . ARG B 1 191 ? 15.989  -24.073 30.352  1.00 75.40  ?  191 ARG B CZ  1 
ATOM   3560 N  NH1 . ARG B 1 191 ? 16.658  -23.666 31.429  1.00 69.42  1  191 ARG B NH1 1 
ATOM   3561 N  NH2 . ARG B 1 191 ? 16.644  -24.613 29.324  1.00 56.35  ?  191 ARG B NH2 1 
ATOM   3562 N  N   . ILE B 1 192 ? 11.282  -19.897 28.048  1.00 25.84  ?  192 ILE B N   1 
ATOM   3563 C  CA  . ILE B 1 192 ? 10.994  -18.477 28.226  1.00 27.00  ?  192 ILE B CA  1 
ATOM   3564 C  C   . ILE B 1 192 ? 11.625  -18.013 29.524  1.00 25.41  ?  192 ILE B C   1 
ATOM   3565 O  O   . ILE B 1 192 ? 11.347  -18.600 30.546  1.00 27.28  ?  192 ILE B O   1 
ATOM   3566 C  CB  . ILE B 1 192 ? 9.480   -18.212 28.238  1.00 23.27  ?  192 ILE B CB  1 
ATOM   3567 C  CG1 . ILE B 1 192 ? 8.882   -18.576 26.908  1.00 28.31  ?  192 ILE B CG1 1 
ATOM   3568 C  CG2 . ILE B 1 192 ? 9.206   -16.768 28.625  1.00 23.14  ?  192 ILE B CG2 1 
ATOM   3569 C  CD1 . ILE B 1 192 ? 7.373   -18.639 26.877  1.00 26.25  ?  192 ILE B CD1 1 
ATOM   3570 N  N   . VAL B 1 193 ? 12.454  -16.957 29.495  1.00 22.65  ?  193 VAL B N   1 
ATOM   3571 C  CA  . VAL B 1 193 ? 13.043  -16.451 30.717  1.00 23.04  ?  193 VAL B CA  1 
ATOM   3572 C  C   . VAL B 1 193 ? 12.476  -15.097 31.088  1.00 24.78  ?  193 VAL B C   1 
ATOM   3573 O  O   . VAL B 1 193 ? 12.593  -14.678 32.239  1.00 24.46  ?  193 VAL B O   1 
ATOM   3574 C  CB  . VAL B 1 193 ? 14.584  -16.435 30.647  1.00 28.87  ?  193 VAL B CB  1 
ATOM   3575 C  CG1 . VAL B 1 193 ? 15.143  -17.824 30.351  1.00 33.26  ?  193 VAL B CG1 1 
ATOM   3576 C  CG2 . VAL B 1 193 ? 15.112  -15.461 29.628  1.00 28.19  ?  193 VAL B CG2 1 
ATOM   3577 N  N   . ALA B 1 194 ? 11.889  -14.389 30.118  1.00 20.49  ?  194 ALA B N   1 
ATOM   3578 C  CA  . ALA B 1 194 ? 11.229  -13.125 30.400  1.00 20.52  ?  194 ALA B CA  1 
ATOM   3579 C  C   . ALA B 1 194 ? 10.179  -12.923 29.329  1.00 18.03  ?  194 ALA B C   1 
ATOM   3580 O  O   . ALA B 1 194 ? 10.407  -13.283 28.178  1.00 17.49  ?  194 ALA B O   1 
ATOM   3581 C  CB  . ALA B 1 194 ? 12.245  -11.998 30.395  1.00 21.40  ?  194 ALA B CB  1 
ATOM   3582 N  N   . GLY B 1 195 ? 9.020   -12.414 29.694  1.00 17.24  ?  195 GLY B N   1 
ATOM   3583 C  CA  . GLY B 1 195 ? 7.925   -12.392 28.750  1.00 17.00  ?  195 GLY B CA  1 
ATOM   3584 C  C   . GLY B 1 195 ? 6.597   -12.040 29.396  1.00 15.95  ?  195 GLY B C   1 
ATOM   3585 O  O   . GLY B 1 195 ? 6.533   -11.741 30.584  1.00 17.59  ?  195 GLY B O   1 
ATOM   3586 N  N   . ALA B 1 196 ? 5.553   -12.045 28.570  1.00 14.67  ?  196 ALA B N   1 
ATOM   3587 C  CA  . ALA B 1 196 ? 4.207   -11.777 29.038  1.00 15.88  ?  196 ALA B CA  1 
ATOM   3588 C  C   . ALA B 1 196 ? 3.753   -12.864 30.014  1.00 15.75  ?  196 ALA B C   1 
ATOM   3589 O  O   . ALA B 1 196 ? 4.002   -14.060 29.802  1.00 16.94  ?  196 ALA B O   1 
ATOM   3590 C  CB  . ALA B 1 196 ? 3.271   -11.719 27.874  1.00 16.90  ?  196 ALA B CB  1 
ATOM   3591 N  N   . LYS B 1 197 ? 3.110   -12.411 31.093  1.00 17.74  ?  197 LYS B N   1 
ATOM   3592 C  CA  . LYS B 1 197 ? 2.724   -13.266 32.203  1.00 19.04  ?  197 LYS B CA  1 
ATOM   3593 C  C   . LYS B 1 197 ? 1.204   -13.205 32.331  1.00 18.74  ?  197 LYS B C   1 
ATOM   3594 O  O   . LYS B 1 197 ? 0.567   -12.186 32.071  1.00 17.02  ?  197 LYS B O   1 
ATOM   3595 C  CB  . LYS B 1 197 ? 3.409   -12.847 33.512  1.00 21.08  ?  197 LYS B CB  1 
ATOM   3596 C  CG  . LYS B 1 197 ? 4.899   -13.091 33.549  1.00 27.00  ?  197 LYS B CG  1 
ATOM   3597 C  CD  . LYS B 1 197 ? 5.692   -12.585 34.756  1.00 33.86  ?  197 LYS B CD  1 
ATOM   3598 C  CE  . LYS B 1 197 ? 5.326   -11.167 35.134  1.00 46.00  ?  197 LYS B CE  1 
ATOM   3599 N  NZ  . LYS B 1 197 ? 6.310   -10.432 35.949  1.00 52.50  1  197 LYS B NZ  1 
ATOM   3600 N  N   . TYR B 1 198 ? 0.619   -14.339 32.741  1.00 19.36  ?  198 TYR B N   1 
ATOM   3601 C  CA  . TYR B 1 198 ? -0.727  -14.342 33.272  1.00 19.25  ?  198 TYR B CA  1 
ATOM   3602 C  C   . TYR B 1 198 ? -0.729  -13.607 34.604  1.00 20.87  ?  198 TYR B C   1 
ATOM   3603 O  O   . TYR B 1 198 ? 0.305   -13.446 35.267  1.00 21.79  ?  198 TYR B O   1 
ATOM   3604 C  CB  . TYR B 1 198 ? -1.212  -15.788 33.407  1.00 19.64  ?  198 TYR B CB  1 
ATOM   3605 C  CG  . TYR B 1 198 ? -1.496  -16.503 32.096  1.00 18.57  ?  198 TYR B CG  1 
ATOM   3606 C  CD1 . TYR B 1 198 ? -2.328  -15.941 31.130  1.00 19.59  ?  198 TYR B CD1 1 
ATOM   3607 C  CD2 . TYR B 1 198 ? -0.902  -17.723 31.818  1.00 18.33  ?  198 TYR B CD2 1 
ATOM   3608 C  CE1 . TYR B 1 198 ? -2.621  -16.613 29.967  1.00 21.21  ?  198 TYR B CE1 1 
ATOM   3609 C  CE2 . TYR B 1 198 ? -1.182  -18.395 30.648  1.00 21.69  ?  198 TYR B CE2 1 
ATOM   3610 C  CZ  . TYR B 1 198 ? -2.047  -17.847 29.723  1.00 20.37  ?  198 TYR B CZ  1 
ATOM   3611 O  OH  . TYR B 1 198 ? -2.321  -18.507 28.555  1.00 22.52  ?  198 TYR B OH  1 
ATOM   3612 N  N   . GLU B 1 199 ? -1.948  -13.272 35.040  1.00 25.23  ?  199 GLU B N   1 
ATOM   3613 C  CA  . GLU B 1 199 ? -2.163  -12.528 36.276  1.00 27.77  ?  199 GLU B CA  1 
ATOM   3614 C  C   . GLU B 1 199 ? -1.340  -13.097 37.431  1.00 25.60  ?  199 GLU B C   1 
ATOM   3615 O  O   . GLU B 1 199 ? -0.768  -12.336 38.190  1.00 26.24  ?  199 GLU B O   1 
ATOM   3616 C  CB  . GLU B 1 199 ? -3.662  -12.489 36.569  1.00 33.30  ?  199 GLU B CB  1 
ATOM   3617 C  CG  . GLU B 1 199 ? -4.038  -11.546 37.712  1.00 46.69  ?  199 GLU B CG  1 
ATOM   3618 C  CD  . GLU B 1 199 ? -5.416  -11.840 38.303  1.00 55.22  ?  199 GLU B CD  1 
ATOM   3619 O  OE1 . GLU B 1 199 ? -6.409  -11.958 37.529  1.00 60.67  ?  199 GLU B OE1 1 
ATOM   3620 O  OE2 . GLU B 1 199 ? -5.484  -11.970 39.554  1.00 59.34  -1 199 GLU B OE2 1 
ATOM   3621 N  N   . GLY B 1 200 ? -1.281  -14.431 37.577  1.00 24.76  ?  200 GLY B N   1 
ATOM   3622 C  CA  . GLY B 1 200 ? -0.643  -15.034 38.727  1.00 24.85  ?  200 GLY B CA  1 
ATOM   3623 C  C   . GLY B 1 200 ? 0.859   -15.247 38.563  1.00 27.85  ?  200 GLY B C   1 
ATOM   3624 O  O   . GLY B 1 200 ? 1.523   -15.733 39.478  1.00 24.95  ?  200 GLY B O   1 
ATOM   3625 N  N   . GLY B 1 201 ? 1.385   -14.975 37.358  1.00 25.81  ?  201 GLY B N   1 
ATOM   3626 C  CA  . GLY B 1 201 ? 2.819   -14.918 37.170  1.00 24.56  ?  201 GLY B CA  1 
ATOM   3627 C  C   . GLY B 1 201 ? 3.409   -15.981 36.251  1.00 24.23  ?  201 GLY B C   1 
ATOM   3628 O  O   . GLY B 1 201 ? 4.592   -15.879 35.947  1.00 24.38  ?  201 GLY B O   1 
ATOM   3629 N  N   . GLU B 1 202 ? 2.659   -16.997 35.790  1.00 22.73  ?  202 GLU B N   1 
ATOM   3630 C  CA  . GLU B 1 202 ? 3.231   -17.943 34.837  1.00 23.23  ?  202 GLU B CA  1 
ATOM   3631 C  C   . GLU B 1 202 ? 3.350   -17.290 33.438  1.00 19.31  ?  202 GLU B C   1 
ATOM   3632 O  O   . GLU B 1 202 ? 2.523   -16.455 33.078  1.00 17.93  ?  202 GLU B O   1 
ATOM   3633 C  CB  . GLU B 1 202 ? 2.389   -19.213 34.664  1.00 27.66  ?  202 GLU B CB  1 
ATOM   3634 C  CG  . GLU B 1 202 ? 2.416   -20.185 35.846  1.00 37.57  ?  202 GLU B CG  1 
ATOM   3635 C  CD  . GLU B 1 202 ? 1.652   -21.486 35.585  1.00 43.33  ?  202 GLU B CD  1 
ATOM   3636 O  OE1 . GLU B 1 202 ? 0.556   -21.429 34.989  1.00 47.74  ?  202 GLU B OE1 1 
ATOM   3637 O  OE2 . GLU B 1 202 ? 2.146   -22.568 35.963  1.00 58.29  -1 202 GLU B OE2 1 
ATOM   3638 N  N   . PHE B 1 203 ? 4.335   -17.724 32.648  1.00 19.40  ?  203 PHE B N   1 
ATOM   3639 C  CA  . PHE B 1 203 ? 4.493   -17.187 31.303  1.00 20.83  ?  203 PHE B CA  1 
ATOM   3640 C  C   . PHE B 1 203 ? 3.374   -17.699 30.395  1.00 20.89  ?  203 PHE B C   1 
ATOM   3641 O  O   . PHE B 1 203 ? 3.041   -18.869 30.396  1.00 19.43  ?  203 PHE B O   1 
ATOM   3642 C  CB  . PHE B 1 203 ? 5.863   -17.548 30.735  1.00 20.09  ?  203 PHE B CB  1 
ATOM   3643 C  CG  . PHE B 1 203 ? 6.997   -16.831 31.440  1.00 23.13  ?  203 PHE B CG  1 
ATOM   3644 C  CD1 . PHE B 1 203 ? 6.992   -15.447 31.598  1.00 21.17  ?  203 PHE B CD1 1 
ATOM   3645 C  CD2 . PHE B 1 203 ? 8.068   -17.547 31.961  1.00 24.44  ?  203 PHE B CD2 1 
ATOM   3646 C  CE1 . PHE B 1 203 ? 8.042   -14.809 32.249  1.00 23.41  ?  203 PHE B CE1 1 
ATOM   3647 C  CE2 . PHE B 1 203 ? 9.108   -16.895 32.605  1.00 25.73  ?  203 PHE B CE2 1 
ATOM   3648 C  CZ  . PHE B 1 203 ? 9.085   -15.544 32.757  1.00 24.10  ?  203 PHE B CZ  1 
ATOM   3649 N  N   . ALA B 1 204 ? 2.822   -16.800 29.593  1.00 17.65  ?  204 ALA B N   1 
ATOM   3650 C  CA  . ALA B 1 204 ? 1.717   -17.118 28.715  1.00 17.40  ?  204 ALA B CA  1 
ATOM   3651 C  C   . ALA B 1 204 ? 2.179   -17.726 27.391  1.00 19.04  ?  204 ALA B C   1 
ATOM   3652 O  O   . ALA B 1 204 ? 1.373   -18.398 26.753  1.00 18.87  ?  204 ALA B O   1 
ATOM   3653 C  CB  . ALA B 1 204 ? 0.952   -15.855 28.454  1.00 18.51  ?  204 ALA B CB  1 
ATOM   3654 N  N   . ASP B 1 205 ? 3.403   -17.403 26.942  1.00 15.88  ?  205 ASP B N   1 
ATOM   3655 C  CA  . ASP B 1 205 ? 3.884   -17.719 25.595  1.00 17.40  ?  205 ASP B CA  1 
ATOM   3656 C  C   . ASP B 1 205 ? 3.212   -16.835 24.541  1.00 17.54  ?  205 ASP B C   1 
ATOM   3657 O  O   . ASP B 1 205 ? 2.178   -17.190 23.952  1.00 16.79  ?  205 ASP B O   1 
ATOM   3658 C  CB  . ASP B 1 205 ? 3.836   -19.204 25.268  1.00 17.76  ?  205 ASP B CB  1 
ATOM   3659 C  CG  . ASP B 1 205 ? 4.598   -19.610 24.013  1.00 20.66  ?  205 ASP B CG  1 
ATOM   3660 O  OD1 . ASP B 1 205 ? 4.758   -18.782 23.101  1.00 20.17  ?  205 ASP B OD1 1 
ATOM   3661 O  OD2 . ASP B 1 205 ? 5.029   -20.747 23.931  1.00 24.66  -1 205 ASP B OD2 1 
ATOM   3662 N  N   . THR B 1 206 ? 3.825   -15.665 24.306  1.00 16.42  ?  206 THR B N   1 
ATOM   3663 C  CA  . THR B 1 206 ? 3.227   -14.642 23.471  1.00 15.78  ?  206 THR B CA  1 
ATOM   3664 C  C   . THR B 1 206 ? 2.836   -15.222 22.112  1.00 17.14  ?  206 THR B C   1 
ATOM   3665 O  O   . THR B 1 206 ? 1.706   -15.013 21.639  1.00 16.08  ?  206 THR B O   1 
ATOM   3666 C  CB  . THR B 1 206 ? 4.162   -13.442 23.323  1.00 15.51  ?  206 THR B CB  1 
ATOM   3667 O  OG1 . THR B 1 206 ? 4.278   -12.855 24.615  1.00 14.55  ?  206 THR B OG1 1 
ATOM   3668 C  CG2 . THR B 1 206 ? 3.610   -12.430 22.335  1.00 15.93  ?  206 THR B CG2 1 
ATOM   3669 N  N   . TYR B 1 207 ? 3.785   -15.861 21.435  1.00 15.75  ?  207 TYR B N   1 
ATOM   3670 C  CA  . TYR B 1 207 ? 3.518   -16.316 20.077  1.00 17.04  ?  207 TYR B CA  1 
ATOM   3671 C  C   . TYR B 1 207 ? 2.388   -17.349 20.050  1.00 16.93  ?  207 TYR B C   1 
ATOM   3672 O  O   . TYR B 1 207 ? 1.524   -17.283 19.173  1.00 17.35  ?  207 TYR B O   1 
ATOM   3673 C  CB  . TYR B 1 207 ? 4.827   -16.834 19.455  1.00 17.41  ?  207 TYR B CB  1 
ATOM   3674 C  CG  . TYR B 1 207 ? 4.658   -17.401 18.046  1.00 18.29  ?  207 TYR B CG  1 
ATOM   3675 C  CD1 . TYR B 1 207 ? 3.975   -16.701 17.054  1.00 20.40  ?  207 TYR B CD1 1 
ATOM   3676 C  CD2 . TYR B 1 207 ? 5.169   -18.653 17.721  1.00 21.41  ?  207 TYR B CD2 1 
ATOM   3677 C  CE1 . TYR B 1 207 ? 3.810   -17.232 15.779  1.00 22.27  ?  207 TYR B CE1 1 
ATOM   3678 C  CE2 . TYR B 1 207 ? 5.054   -19.175 16.435  1.00 22.00  ?  207 TYR B CE2 1 
ATOM   3679 C  CZ  . TYR B 1 207 ? 4.374   -18.461 15.461  1.00 22.43  ?  207 TYR B CZ  1 
ATOM   3680 O  OH  . TYR B 1 207 ? 4.227   -19.027 14.224  1.00 22.33  ?  207 TYR B OH  1 
ATOM   3681 N  N   . ALA B 1 208 ? 2.411   -18.325 20.960  1.00 18.11  ?  208 ALA B N   1 
ATOM   3682 C  CA  . ALA B 1 208 ? 1.347   -19.324 21.030  1.00 19.65  ?  208 ALA B CA  1 
ATOM   3683 C  C   . ALA B 1 208 ? -0.026  -18.669 21.190  1.00 19.17  ?  208 ALA B C   1 
ATOM   3684 O  O   . ALA B 1 208 ? -0.982  -19.046 20.512  1.00 17.93  ?  208 ALA B O   1 
ATOM   3685 C  CB  . ALA B 1 208 ? 1.626   -20.315 22.155  1.00 19.74  ?  208 ALA B CB  1 
ATOM   3686 N  N   . ARG B 1 209 ? -0.120  -17.655 22.053  1.00 19.08  ?  209 ARG B N   1 
ATOM   3687 C  CA  . ARG B 1 209 ? -1.378  -16.955 22.306  1.00 17.41  ?  209 ARG B CA  1 
ATOM   3688 C  C   . ARG B 1 209 ? -1.821  -16.158 21.086  1.00 18.59  ?  209 ARG B C   1 
ATOM   3689 O  O   . ARG B 1 209 ? -3.022  -16.065 20.774  1.00 20.05  ?  209 ARG B O   1 
ATOM   3690 C  CB  . ARG B 1 209 ? -1.278  -15.961 23.472  1.00 18.06  ?  209 ARG B CB  1 
ATOM   3691 C  CG  . ARG B 1 209 ? -1.028  -16.630 24.818  1.00 19.78  ?  209 ARG B CG  1 
ATOM   3692 C  CD  . ARG B 1 209 ? -1.986  -17.780 25.147  1.00 22.93  ?  209 ARG B CD  1 
ATOM   3693 N  NE  . ARG B 1 209 ? -3.380  -17.319 25.030  1.00 27.51  ?  209 ARG B NE  1 
ATOM   3694 C  CZ  . ARG B 1 209 ? -4.460  -18.116 25.010  1.00 34.19  ?  209 ARG B CZ  1 
ATOM   3695 N  NH1 . ARG B 1 209 ? -4.358  -19.431 25.189  1.00 38.76  1  209 ARG B NH1 1 
ATOM   3696 N  NH2 . ARG B 1 209 ? -5.638  -17.574 24.796  1.00 35.45  ?  209 ARG B NH2 1 
ATOM   3697 N  N   . MET B 1 210 ? -0.858  -15.535 20.403  1.00 18.39  ?  210 MET B N   1 
ATOM   3698 C  CA  . MET B 1 210 ? -1.196  -14.794 19.197  1.00 19.96  ?  210 MET B CA  1 
ATOM   3699 C  C   . MET B 1 210 ? -1.717  -15.732 18.107  1.00 19.47  ?  210 MET B C   1 
ATOM   3700 O  O   . MET B 1 210 ? -2.616  -15.331 17.359  1.00 20.50  ?  210 MET B O   1 
ATOM   3701 C  CB  . MET B 1 210 ? 0.012   -13.985 18.694  1.00 21.61  ?  210 MET B CB  1 
ATOM   3702 C  CG  . MET B 1 210 ? 0.346   -12.817 19.611  1.00 24.29  ?  210 MET B CG  1 
ATOM   3703 S  SD  . MET B 1 210 ? 1.722   -11.808 19.008  1.00 28.62  ?  210 MET B SD  1 
ATOM   3704 C  CE  . MET B 1 210 ? 0.691   -10.782 17.948  1.00 35.04  ?  210 MET B CE  1 
ATOM   3705 N  N   . LYS B 1 211 ? -1.155  -16.942 17.979  1.00 19.44  ?  211 LYS B N   1 
ATOM   3706 C  CA  . LYS B 1 211 ? -1.651  -17.913 16.998  1.00 22.34  ?  211 LYS B CA  1 
ATOM   3707 C  C   . LYS B 1 211 ? -3.105  -18.319 17.274  1.00 25.40  ?  211 LYS B C   1 
ATOM   3708 O  O   . LYS B 1 211 ? -3.840  -18.650 16.340  1.00 24.90  ?  211 LYS B O   1 
ATOM   3709 C  CB  . LYS B 1 211 ? -0.775  -19.165 16.944  1.00 24.31  ?  211 LYS B CB  1 
ATOM   3710 C  CG  . LYS B 1 211 ? 0.559   -18.945 16.186  1.00 27.12  ?  211 LYS B CG  1 
ATOM   3711 C  CD  . LYS B 1 211 ? 1.572   -20.074 16.377  1.00 31.12  ?  211 LYS B CD  1 
ATOM   3712 C  CE  . LYS B 1 211 ? 1.314   -21.380 15.788  1.00 31.37  ?  211 LYS B CE  1 
ATOM   3713 N  NZ  . LYS B 1 211 ? 2.490   -22.206 16.050  1.00 28.99  1  211 LYS B NZ  1 
ATOM   3714 N  N   . LEU B 1 212 ? -3.480  -18.358 18.561  1.00 27.18  ?  212 LEU B N   1 
ATOM   3715 C  CA  . LEU B 1 212 ? -4.824  -18.731 19.003  1.00 27.76  ?  212 LEU B CA  1 
ATOM   3716 C  C   . LEU B 1 212 ? -5.793  -17.562 18.890  1.00 27.90  ?  212 LEU B C   1 
ATOM   3717 O  O   . LEU B 1 212 ? -6.987  -17.774 19.056  1.00 31.55  ?  212 LEU B O   1 
ATOM   3718 C  CB  . LEU B 1 212 ? -4.811  -19.239 20.437  1.00 27.16  ?  212 LEU B CB  1 
ATOM   3719 C  CG  . LEU B 1 212 ? -4.097  -20.576 20.623  1.00 35.31  ?  212 LEU B CG  1 
ATOM   3720 C  CD1 . LEU B 1 212 ? -3.883  -20.892 22.092  1.00 35.21  ?  212 LEU B CD1 1 
ATOM   3721 C  CD2 . LEU B 1 212 ? -4.864  -21.698 19.924  1.00 37.61  ?  212 LEU B CD2 1 
ATOM   3722 N  N   . GLY B 1 213 ? -5.311  -16.339 18.687  1.00 27.40  ?  213 GLY B N   1 
ATOM   3723 C  CA  . GLY B 1 213 ? -6.185  -15.195 18.472  1.00 28.16  ?  213 GLY B CA  1 
ATOM   3724 C  C   . GLY B 1 213 ? -6.099  -14.039 19.486  1.00 29.11  ?  213 GLY B C   1 
ATOM   3725 O  O   . GLY B 1 213 ? -6.789  -13.047 19.313  1.00 27.48  ?  213 GLY B O   1 
ATOM   3726 N  N   . ASP B 1 214 ? -5.270  -14.107 20.540  1.00 27.21  ?  214 ASP B N   1 
ATOM   3727 C  CA  . ASP B 1 214 ? -5.143  -12.962 21.449  1.00 28.90  ?  214 ASP B CA  1 
ATOM   3728 C  C   . ASP B 1 214 ? -4.491  -11.776 20.740  1.00 32.07  ?  214 ASP B C   1 
ATOM   3729 O  O   . ASP B 1 214 ? -3.505  -11.939 20.015  1.00 30.85  ?  214 ASP B O   1 
ATOM   3730 C  CB  . ASP B 1 214 ? -4.280  -13.258 22.667  1.00 30.01  ?  214 ASP B CB  1 
ATOM   3731 C  CG  . ASP B 1 214 ? -4.872  -14.285 23.618  1.00 31.37  ?  214 ASP B CG  1 
ATOM   3732 O  OD1 . ASP B 1 214 ? -5.940  -14.806 23.294  1.00 34.02  ?  214 ASP B OD1 1 
ATOM   3733 O  OD2 . ASP B 1 214 ? -4.263  -14.546 24.659  1.00 31.56  -1 214 ASP B OD2 1 
ATOM   3734 N  N   . LYS B 1 215 ? -5.014  -10.586 21.017  1.00 31.35  ?  215 LYS B N   1 
ATOM   3735 C  CA  . LYS B 1 215 ? -4.667  -9.374  20.288  1.00 42.90  ?  215 LYS B CA  1 
ATOM   3736 C  C   . LYS B 1 215 ? -3.775  -8.480  21.148  1.00 39.83  ?  215 LYS B C   1 
ATOM   3737 O  O   . LYS B 1 215 ? -3.898  -8.437  22.368  1.00 36.22  ?  215 LYS B O   1 
ATOM   3738 C  CB  . LYS B 1 215 ? -5.909  -8.587  19.841  1.00 49.09  ?  215 LYS B CB  1 
ATOM   3739 C  CG  . LYS B 1 215 ? -6.627  -9.132  18.608  1.00 61.63  ?  215 LYS B CG  1 
ATOM   3740 C  CD  . LYS B 1 215 ? -5.834  -9.053  17.301  1.00 73.60  ?  215 LYS B CD  1 
ATOM   3741 C  CE  . LYS B 1 215 ? -6.296  -10.016 16.224  1.00 72.70  ?  215 LYS B CE  1 
ATOM   3742 N  NZ  . LYS B 1 215 ? -5.197  -10.435 15.343  1.00 71.48  1  215 LYS B NZ  1 
ATOM   3743 N  N   . ASN B 1 216 ? -2.878  -7.767  20.469  1.00 39.02  ?  216 ASN B N   1 
ATOM   3744 C  CA  . ASN B 1 216 ? -1.876  -6.915  21.075  1.00 40.86  ?  216 ASN B CA  1 
ATOM   3745 C  C   . ASN B 1 216 ? -2.551  -5.754  21.810  1.00 41.58  ?  216 ASN B C   1 
ATOM   3746 O  O   . ASN B 1 216 ? -3.196  -4.923  21.191  1.00 38.46  ?  216 ASN B O   1 
ATOM   3747 C  CB  . ASN B 1 216 ? -0.927  -6.454  19.968  1.00 38.82  ?  216 ASN B CB  1 
ATOM   3748 C  CG  . ASN B 1 216 ? 0.161   -5.519  20.439  1.00 40.00  ?  216 ASN B CG  1 
ATOM   3749 O  OD1 . ASN B 1 216 ? 0.219   -5.122  21.608  1.00 35.71  ?  216 ASN B OD1 1 
ATOM   3750 N  ND2 . ASN B 1 216 ? 1.065   -5.186  19.538  1.00 43.35  ?  216 ASN B ND2 1 
ATOM   3751 N  N   . GLN B 1 217 ? -2.349  -5.664  23.127  1.00 47.09  ?  217 GLN B N   1 
ATOM   3752 C  CA  . GLN B 1 217 ? -2.920  -4.575  23.913  1.00 50.89  ?  217 GLN B CA  1 
ATOM   3753 C  C   . GLN B 1 217 ? -1.857  -3.596  24.418  1.00 50.73  ?  217 GLN B C   1 
ATOM   3754 O  O   . GLN B 1 217 ? -2.109  -2.871  25.381  1.00 44.43  ?  217 GLN B O   1 
ATOM   3755 C  CB  . GLN B 1 217 ? -3.643  -5.130  25.140  1.00 54.48  ?  217 GLN B CB  1 
ATOM   3756 C  CG  . GLN B 1 217 ? -4.732  -6.141  24.810  1.00 58.67  ?  217 GLN B CG  1 
ATOM   3757 C  CD  . GLN B 1 217 ? -5.151  -6.911  26.039  1.00 71.34  ?  217 GLN B CD  1 
ATOM   3758 O  OE1 . GLN B 1 217 ? -4.953  -6.463  27.176  1.00 78.02  ?  217 GLN B OE1 1 
ATOM   3759 N  NE2 . GLN B 1 217 ? -5.717  -8.088  25.820  1.00 78.94  ?  217 GLN B NE2 1 
ATOM   3760 N  N   . SER B 1 218 ? -0.666  -3.570  23.797  1.00 45.59  ?  218 SER B N   1 
ATOM   3761 C  CA  . SER B 1 218 ? 0.361   -2.637  24.246  1.00 46.46  ?  218 SER B CA  1 
ATOM   3762 C  C   . SER B 1 218 ? -0.002  -1.212  23.809  1.00 41.65  ?  218 SER B C   1 
ATOM   3763 O  O   . SER B 1 218 ? -0.767  -1.006  22.858  1.00 38.67  ?  218 SER B O   1 
ATOM   3764 C  CB  . SER B 1 218 ? 1.721   -3.020  23.737  1.00 45.29  ?  218 SER B CB  1 
ATOM   3765 O  OG  . SER B 1 218 ? 1.809   -2.821  22.332  1.00 41.97  ?  218 SER B OG  1 
ATOM   3766 N  N   . ALA B 1 219 ? 0.592   -0.230  24.493  1.00 44.52  ?  219 ALA B N   1 
ATOM   3767 C  CA  . ALA B 1 219 ? 0.261   1.179   24.281  1.00 44.99  ?  219 ALA B CA  1 
ATOM   3768 C  C   . ALA B 1 219 ? 0.409   1.606   22.814  1.00 43.80  ?  219 ALA B C   1 
ATOM   3769 O  O   . ALA B 1 219 ? -0.316  2.490   22.368  1.00 40.09  ?  219 ALA B O   1 
ATOM   3770 C  CB  . ALA B 1 219 ? 1.093   2.049   25.195  1.00 41.05  ?  219 ALA B CB  1 
ATOM   3771 N  N   . LEU B 1 220 ? 1.338   0.998   22.053  1.00 43.74  ?  220 LEU B N   1 
ATOM   3772 C  CA  . LEU B 1 220 ? 1.608   1.452   20.692  1.00 42.85  ?  220 LEU B CA  1 
ATOM   3773 C  C   . LEU B 1 220 ? 0.805   0.638   19.666  1.00 44.13  ?  220 LEU B C   1 
ATOM   3774 O  O   . LEU B 1 220 ? 0.943   0.876   18.458  1.00 40.95  ?  220 LEU B O   1 
ATOM   3775 C  CB  . LEU B 1 220 ? 3.103   1.415   20.354  1.00 46.31  ?  220 LEU B CB  1 
ATOM   3776 C  CG  . LEU B 1 220 ? 4.060   2.013   21.391  1.00 49.69  ?  220 LEU B CG  1 
ATOM   3777 C  CD1 . LEU B 1 220 ? 4.440   0.899   22.357  1.00 57.47  ?  220 LEU B CD1 1 
ATOM   3778 C  CD2 . LEU B 1 220 ? 5.303   2.674   20.807  1.00 48.93  ?  220 LEU B CD2 1 
ATOM   3779 N  N   . ALA B 1 221 ? -0.040  -0.299  20.131  1.00 41.12  ?  221 ALA B N   1 
ATOM   3780 C  CA  . ALA B 1 221 ? -0.657  -1.289  19.250  1.00 44.71  ?  221 ALA B CA  1 
ATOM   3781 C  C   . ALA B 1 221 ? -1.528  -0.665  18.147  1.00 47.67  ?  221 ALA B C   1 
ATOM   3782 O  O   . ALA B 1 221 ? -1.676  -1.280  17.090  1.00 44.47  ?  221 ALA B O   1 
ATOM   3783 C  CB  . ALA B 1 221 ? -1.468  -2.274  20.071  1.00 44.56  ?  221 ALA B CB  1 
ATOM   3784 N  N   . ARG B 1 222 ? -2.110  0.533   18.371  1.00 47.61  ?  222 ARG B N   1 
ATOM   3785 C  CA  . ARG B 1 222 ? -3.104  1.078   17.450  1.00 61.21  ?  222 ARG B CA  1 
ATOM   3786 C  C   . ARG B 1 222 ? -2.477  1.603   16.149  1.00 72.19  ?  222 ARG B C   1 
ATOM   3787 O  O   . ARG B 1 222 ? -3.203  1.812   15.178  1.00 79.74  ?  222 ARG B O   1 
ATOM   3788 C  CB  . ARG B 1 222 ? -4.004  2.135   18.107  1.00 61.78  ?  222 ARG B CB  1 
ATOM   3789 C  CG  . ARG B 1 222 ? -5.117  1.539   18.961  1.00 72.54  ?  222 ARG B CG  1 
ATOM   3790 C  CD  . ARG B 1 222 ? -6.198  2.543   19.368  1.00 83.44  ?  222 ARG B CD  1 
ATOM   3791 N  NE  . ARG B 1 222 ? -5.692  3.624   20.227  1.00 101.86 ?  222 ARG B NE  1 
ATOM   3792 C  CZ  . ARG B 1 222 ? -6.420  4.458   20.984  1.00 103.41 ?  222 ARG B CZ  1 
ATOM   3793 N  NH1 . ARG B 1 222 ? -7.738  4.332   21.059  1.00 98.03  1  222 ARG B NH1 1 
ATOM   3794 N  NH2 . ARG B 1 222 ? -5.816  5.410   21.682  1.00 100.12 ?  222 ARG B NH2 1 
ATOM   3795 N  N   . MET B 1 223 ? -1.158  1.837   16.108  1.00 74.41  ?  223 MET B N   1 
ATOM   3796 C  CA  . MET B 1 223 ? -0.523  2.255   14.860  1.00 74.06  ?  223 MET B CA  1 
ATOM   3797 C  C   . MET B 1 223 ? -0.113  1.005   14.073  1.00 76.81  ?  223 MET B C   1 
ATOM   3798 O  O   . MET B 1 223 ? 0.453   0.067   14.639  1.00 69.96  ?  223 MET B O   1 
ATOM   3799 C  CB  . MET B 1 223 ? 0.631   3.246   15.097  1.00 71.46  ?  223 MET B CB  1 
ATOM   3800 C  CG  . MET B 1 223 ? 1.623   2.885   16.196  1.00 74.29  ?  223 MET B CG  1 
ATOM   3801 S  SD  . MET B 1 223 ? 2.577   4.276   16.852  1.00 77.52  ?  223 MET B SD  1 
ATOM   3802 C  CE  . MET B 1 223 ? 2.908   5.279   15.398  1.00 60.55  ?  223 MET B CE  1 
ATOM   3803 N  N   . GLY B 1 224 ? -0.447  0.988   12.769  1.00 77.76  ?  224 GLY B N   1 
ATOM   3804 C  CA  . GLY B 1 224 ? -0.249  -0.176  11.912  1.00 73.70  ?  224 GLY B CA  1 
ATOM   3805 C  C   . GLY B 1 224 ? -0.075  0.200   10.441  1.00 68.63  ?  224 GLY B C   1 
ATOM   3806 O  O   . GLY B 1 224 ? 0.400   1.337   10.166  1.00 42.57  ?  224 GLY B O   1 
ATOM   3807 N  N   . THR B 1 227 ? 10.666  -2.937  21.418  1.00 13.21  ?  227 THR B N   1 
ATOM   3808 C  CA  . THR B 1 227 ? 11.923  -2.488  20.760  1.00 12.51  ?  227 THR B CA  1 
ATOM   3809 C  C   . THR B 1 227 ? 13.141  -3.089  21.442  1.00 11.67  ?  227 THR B C   1 
ATOM   3810 O  O   . THR B 1 227 ? 13.221  -3.122  22.666  1.00 12.57  ?  227 THR B O   1 
ATOM   3811 C  CB  . THR B 1 227 ? 12.017  -0.966  20.836  1.00 13.05  ?  227 THR B CB  1 
ATOM   3812 O  OG1 . THR B 1 227 ? 10.874  -0.482  20.167  1.00 14.82  ?  227 THR B OG1 1 
ATOM   3813 C  CG2 . THR B 1 227 ? 13.274  -0.418  20.185  1.00 13.23  ?  227 THR B CG2 1 
ATOM   3814 N  N   . THR B 1 228 ? 14.164  -3.453  20.631  1.00 10.96  ?  228 THR B N   1 
ATOM   3815 C  CA  . THR B 1 228 ? 15.451  -3.860  21.148  1.00 11.61  ?  228 THR B CA  1 
ATOM   3816 C  C   . THR B 1 228 ? 16.470  -3.057  20.335  1.00 13.40  ?  228 THR B C   1 
ATOM   3817 O  O   . THR B 1 228 ? 16.427  -3.088  19.099  1.00 13.11  ?  228 THR B O   1 
ATOM   3818 C  CB  . THR B 1 228 ? 15.595  -5.377  20.969  1.00 13.07  ?  228 THR B CB  1 
ATOM   3819 O  OG1 . THR B 1 228 ? 14.543  -6.006  21.690  1.00 13.28  ?  228 THR B OG1 1 
ATOM   3820 C  CG2 . THR B 1 228 ? 16.914  -5.915  21.444  1.00 13.63  ?  228 THR B CG2 1 
ATOM   3821 N  N   . ILE B 1 229 ? 17.336  -2.308  21.007  1.00 11.94  ?  229 ILE B N   1 
ATOM   3822 C  CA  . ILE B 1 229 ? 18.282  -1.442  20.289  1.00 12.65  ?  229 ILE B CA  1 
ATOM   3823 C  C   . ILE B 1 229 ? 19.669  -1.731  20.831  1.00 12.03  ?  229 ILE B C   1 
ATOM   3824 O  O   . ILE B 1 229 ? 19.830  -2.110  22.001  1.00 13.71  ?  229 ILE B O   1 
ATOM   3825 C  CB  . ILE B 1 229 ? 17.930  0.056   20.423  1.00 12.81  ?  229 ILE B CB  1 
ATOM   3826 C  CG1 . ILE B 1 229 ? 17.844  0.488   21.871  1.00 13.70  ?  229 ILE B CG1 1 
ATOM   3827 C  CG2 . ILE B 1 229 ? 16.681  0.405   19.619  1.00 14.82  ?  229 ILE B CG2 1 
ATOM   3828 C  CD1 . ILE B 1 229 ? 17.603  1.981   22.112  1.00 13.83  ?  229 ILE B CD1 1 
ATOM   3829 N  N   . GLY B 1 230 ? 20.683  -1.527  20.008  1.00 10.54  ?  230 GLY B N   1 
ATOM   3830 C  CA  . GLY B 1 230 ? 21.984  -1.886  20.506  1.00 10.28  ?  230 GLY B CA  1 
ATOM   3831 C  C   . GLY B 1 230 ? 23.105  -1.514  19.574  1.00 11.28  ?  230 GLY B C   1 
ATOM   3832 O  O   . GLY B 1 230 ? 22.871  -1.068  18.464  1.00 12.32  ?  230 GLY B O   1 
ATOM   3833 N  N   B ILE B 1 231 ? 24.313  -1.745  20.071  1.00 11.25  ?  231 ILE B N   1 
ATOM   3834 C  CA  B ILE B 1 231 ? 25.573  -1.500  19.385  1.00 12.34  ?  231 ILE B CA  1 
ATOM   3835 C  C   B ILE B 1 231 ? 26.367  -2.796  19.361  1.00 12.59  ?  231 ILE B C   1 
ATOM   3836 O  O   B ILE B 1 231 ? 26.494  -3.451  20.391  1.00 14.51  ?  231 ILE B O   1 
ATOM   3837 C  CB  B ILE B 1 231 ? 26.396  -0.418  20.105  1.00 15.20  ?  231 ILE B CB  1 
ATOM   3838 C  CG1 B ILE B 1 231 ? 25.590  0.892   20.270  1.00 18.03  ?  231 ILE B CG1 1 
ATOM   3839 C  CG2 B ILE B 1 231 ? 27.717  -0.152  19.348  1.00 16.01  ?  231 ILE B CG2 1 
ATOM   3840 C  CD1 B ILE B 1 231 ? 26.193  1.842   21.288  1.00 20.87  ?  231 ILE B CD1 1 
ATOM   3841 N  N   . VAL B 1 232 ? 26.945  -3.128  18.208  1.00 12.56  ?  232 VAL B N   1 
ATOM   3842 C  CA  . VAL B 1 232 ? 27.918  -4.199  18.099  1.00 13.54  ?  232 VAL B CA  1 
ATOM   3843 C  C   . VAL B 1 232 ? 29.216  -3.583  17.572  1.00 13.31  ?  232 VAL B C   1 
ATOM   3844 O  O   . VAL B 1 232 ? 29.194  -2.798  16.628  1.00 12.12  ?  232 VAL B O   1 
ATOM   3845 C  CB  . VAL B 1 232 ? 27.437  -5.386  17.226  1.00 15.84  ?  232 VAL B CB  1 
ATOM   3846 C  CG1 . VAL B 1 232 ? 26.231  -6.082  17.809  1.00 16.50  ?  232 VAL B CG1 1 
ATOM   3847 C  CG2 . VAL B 1 232 ? 27.145  -5.001  15.797  1.00 17.34  ?  232 VAL B CG2 1 
ATOM   3848 N  N   . SER B 1 233 ? 30.341  -3.945  18.194  1.00 13.36  ?  233 SER B N   1 
ATOM   3849 C  CA  . SER B 1 233 ? 31.626  -3.316  17.940  1.00 13.06  ?  233 SER B CA  1 
ATOM   3850 C  C   . SER B 1 233 ? 32.720  -4.363  17.821  1.00 14.86  ?  233 SER B C   1 
ATOM   3851 O  O   . SER B 1 233 ? 32.701  -5.362  18.557  1.00 15.64  ?  233 SER B O   1 
ATOM   3852 C  CB  . SER B 1 233 ? 31.943  -2.323  19.063  1.00 14.00  ?  233 SER B CB  1 
ATOM   3853 O  OG  . SER B 1 233 ? 31.031  -1.238  19.071  1.00 15.24  ?  233 SER B OG  1 
ATOM   3854 N  N   . THR B 1 234 ? 33.671  -4.136  16.900  1.00 14.39  ?  234 THR B N   1 
ATOM   3855 C  CA  . THR B 1 234 ? 34.835  -5.006  16.763  1.00 14.47  ?  234 THR B CA  1 
ATOM   3856 C  C   . THR B 1 234 ? 36.112  -4.156  16.717  1.00 14.83  ?  234 THR B C   1 
ATOM   3857 O  O   . THR B 1 234 ? 36.106  -2.969  16.356  1.00 15.52  ?  234 THR B O   1 
ATOM   3858 C  CB  . THR B 1 234 ? 34.699  -5.876  15.505  1.00 16.38  ?  234 THR B CB  1 
ATOM   3859 O  OG1 . THR B 1 234 ? 35.802  -6.789  15.432  1.00 17.80  ?  234 THR B OG1 1 
ATOM   3860 C  CG2 . THR B 1 234 ? 34.651  -5.046  14.232  1.00 15.46  ?  234 THR B CG2 1 
ATOM   3861 N  N   . ASN B 1 235 ? 37.224  -4.793  17.082  1.00 15.93  ?  235 ASN B N   1 
ATOM   3862 C  CA  . ASN B 1 235 ? 38.541  -4.185  16.986  1.00 17.25  ?  235 ASN B CA  1 
ATOM   3863 C  C   . ASN B 1 235 ? 39.165  -4.447  15.601  1.00 18.40  ?  235 ASN B C   1 
ATOM   3864 O  O   . ASN B 1 235 ? 40.305  -4.034  15.352  1.00 21.10  ?  235 ASN B O   1 
ATOM   3865 C  CB  . ASN B 1 235 ? 39.428  -4.673  18.141  1.00 16.90  ?  235 ASN B CB  1 
ATOM   3866 C  CG  . ASN B 1 235 ? 39.595  -6.177  18.191  1.00 19.05  ?  235 ASN B CG  1 
ATOM   3867 O  OD1 . ASN B 1 235 ? 38.922  -6.969  17.507  1.00 17.10  ?  235 ASN B OD1 1 
ATOM   3868 N  ND2 . ASN B 1 235 ? 40.512  -6.601  19.041  1.00 20.74  ?  235 ASN B ND2 1 
ATOM   3869 N  N   . CYS B 1 236 ? 38.455  -5.116  14.680  1.00 17.45  ?  236 CYS B N   1 
ATOM   3870 C  CA  . CYS B 1 236 ? 38.865  -5.187  13.284  1.00 17.15  ?  236 CYS B CA  1 
ATOM   3871 C  C   . CYS B 1 236 ? 38.640  -3.874  12.550  1.00 18.80  ?  236 CYS B C   1 
ATOM   3872 O  O   . CYS B 1 236 ? 37.727  -3.101  12.869  1.00 17.89  ?  236 CYS B O   1 
ATOM   3873 C  CB  . CYS B 1 236 ? 38.148  -6.290  12.511  1.00 20.08  ?  236 CYS B CB  1 
ATOM   3874 S  SG  . CYS B 1 236 ? 38.667  -7.916  13.089  1.00 21.85  ?  236 CYS B SG  1 
ATOM   3875 N  N   . ARG B 1 237 ? 39.491  -3.630  11.530  1.00 17.27  ?  237 ARG B N   1 
ATOM   3876 C  CA  . ARG B 1 237 ? 39.254  -2.567  10.570  1.00 19.96  ?  237 ARG B CA  1 
ATOM   3877 C  C   . ARG B 1 237 ? 38.149  -2.998  9.600   1.00 18.16  ?  237 ARG B C   1 
ATOM   3878 O  O   . ARG B 1 237 ? 38.190  -4.102  9.070   1.00 21.35  ?  237 ARG B O   1 
ATOM   3879 C  CB  . ARG B 1 237 ? 40.539  -2.305  9.760   1.00 23.28  ?  237 ARG B CB  1 
ATOM   3880 C  CG  . ARG B 1 237 ? 40.509  -1.121  8.807   1.00 29.87  ?  237 ARG B CG  1 
ATOM   3881 C  CD  . ARG B 1 237 ? 41.928  -0.882  8.190   1.00 35.82  ?  237 ARG B CD  1 
ATOM   3882 N  NE  . ARG B 1 237 ? 42.229  -1.899  7.177   1.00 44.11  ?  237 ARG B NE  1 
ATOM   3883 C  CZ  . ARG B 1 237 ? 43.117  -2.895  7.199   1.00 48.83  ?  237 ARG B CZ  1 
ATOM   3884 N  NH1 . ARG B 1 237 ? 43.943  -3.084  8.217   1.00 49.81  1  237 ARG B NH1 1 
ATOM   3885 N  NH2 . ARG B 1 237 ? 43.169  -3.725  6.168   1.00 52.52  ?  237 ARG B NH2 1 
ATOM   3886 N  N   . LEU B 1 238 ? 37.185  -2.111  9.344   1.00 19.82  ?  238 LEU B N   1 
ATOM   3887 C  CA  . LEU B 1 238 ? 36.065  -2.371  8.436   1.00 17.95  ?  238 LEU B CA  1 
ATOM   3888 C  C   . LEU B 1 238 ? 35.983  -1.229  7.426   1.00 18.51  ?  238 LEU B C   1 
ATOM   3889 O  O   . LEU B 1 238 ? 36.330  -0.107  7.751   1.00 18.89  ?  238 LEU B O   1 
ATOM   3890 C  CB  . LEU B 1 238 ? 34.756  -2.416  9.238   1.00 18.06  ?  238 LEU B CB  1 
ATOM   3891 C  CG  . LEU B 1 238 ? 34.604  -3.517  10.284  1.00 20.46  ?  238 LEU B CG  1 
ATOM   3892 C  CD1 . LEU B 1 238 ? 33.224  -3.435  10.959  1.00 22.57  ?  238 LEU B CD1 1 
ATOM   3893 C  CD2 . LEU B 1 238 ? 34.808  -4.904  9.704   1.00 20.71  ?  238 LEU B CD2 1 
ATOM   3894 N  N   . THR B 1 239 ? 35.418  -1.502  6.252   1.00 17.47  ?  239 THR B N   1 
ATOM   3895 C  CA  . THR B 1 239 ? 34.893  -0.477  5.365   1.00 18.73  ?  239 THR B CA  1 
ATOM   3896 C  C   . THR B 1 239 ? 33.446  -0.190  5.777   1.00 17.47  ?  239 THR B C   1 
ATOM   3897 O  O   . THR B 1 239 ? 32.862  -0.931  6.564   1.00 15.76  ?  239 THR B O   1 
ATOM   3898 C  CB  . THR B 1 239 ? 34.948  -0.955  3.912   1.00 21.33  ?  239 THR B CB  1 
ATOM   3899 O  OG1 . THR B 1 239 ? 34.017  -2.027  3.742   1.00 20.68  ?  239 THR B OG1 1 
ATOM   3900 C  CG2 . THR B 1 239 ? 36.338  -1.413  3.479   1.00 23.33  ?  239 THR B CG2 1 
ATOM   3901 N  N   . LYS B 1 240 ? 32.875  0.883   5.215   1.00 17.76  ?  240 LYS B N   1 
ATOM   3902 C  CA  . LYS B 1 240 ? 31.508  1.264   5.532   1.00 17.99  ?  240 LYS B CA  1 
ATOM   3903 C  C   . LYS B 1 240 ? 30.528  0.153   5.145   1.00 17.43  ?  240 LYS B C   1 
ATOM   3904 O  O   . LYS B 1 240 ? 29.600  -0.139  5.910   1.00 16.42  ?  240 LYS B O   1 
ATOM   3905 C  CB  . LYS B 1 240 ? 31.120  2.593   4.878   1.00 20.97  ?  240 LYS B CB  1 
ATOM   3906 C  CG  . LYS B 1 240 ? 31.389  3.764   5.774   1.00 24.38  ?  240 LYS B CG  1 
ATOM   3907 C  CD  . LYS B 1 240 ? 30.731  5.074   5.379   1.00 25.37  ?  240 LYS B CD  1 
ATOM   3908 C  CE  . LYS B 1 240 ? 29.568  5.333   6.285   1.00 22.47  ?  240 LYS B CE  1 
ATOM   3909 N  NZ  . LYS B 1 240 ? 28.863  6.473   5.714   1.00 23.28  1  240 LYS B NZ  1 
ATOM   3910 N  N   . VAL B 1 241 ? 30.746  -0.476  3.986   1.00 17.45  ?  241 VAL B N   1 
ATOM   3911 C  CA  . VAL B 1 241 ? 29.887  -1.541  3.479   1.00 19.28  ?  241 VAL B CA  1 
ATOM   3912 C  C   . VAL B 1 241 ? 29.926  -2.695  4.463   1.00 15.91  ?  241 VAL B C   1 
ATOM   3913 O  O   . VAL B 1 241 ? 28.899  -3.278  4.800   1.00 14.49  ?  241 VAL B O   1 
ATOM   3914 C  CB  . VAL B 1 241 ? 30.327  -2.030  2.080   1.00 25.65  ?  241 VAL B CB  1 
ATOM   3915 C  CG1 . VAL B 1 241 ? 29.859  -3.447  1.767   1.00 33.57  ?  241 VAL B CG1 1 
ATOM   3916 C  CG2 . VAL B 1 241 ? 29.838  -1.106  1.006   1.00 28.22  ?  241 VAL B CG2 1 
ATOM   3917 N  N   . GLU B 1 242 ? 31.126  -3.025  4.949   1.00 12.94  ?  242 GLU B N   1 
ATOM   3918 C  CA  . GLU B 1 242 ? 31.252  -4.123  5.895   1.00 13.64  ?  242 GLU B CA  1 
ATOM   3919 C  C   . GLU B 1 242 ? 30.595  -3.813  7.256   1.00 13.67  ?  242 GLU B C   1 
ATOM   3920 O  O   . GLU B 1 242 ? 30.055  -4.719  7.893   1.00 15.02  ?  242 GLU B O   1 
ATOM   3921 C  CB  . GLU B 1 242 ? 32.729  -4.478  6.130   1.00 13.48  ?  242 GLU B CB  1 
ATOM   3922 C  CG  . GLU B 1 242 ? 33.401  -5.034  4.874   1.00 16.76  ?  242 GLU B CG  1 
ATOM   3923 C  CD  . GLU B 1 242 ? 34.893  -5.287  5.055   1.00 19.92  ?  242 GLU B CD  1 
ATOM   3924 O  OE1 . GLU B 1 242 ? 35.553  -4.435  5.678   1.00 17.48  ?  242 GLU B OE1 1 
ATOM   3925 O  OE2 . GLU B 1 242 ? 35.383  -6.336  4.598   1.00 23.97  -1 242 GLU B OE2 1 
ATOM   3926 N  N   . ALA B 1 243 ? 30.699  -2.582  7.750   1.00 12.83  ?  243 ALA B N   1 
ATOM   3927 C  CA  . ALA B 1 243 ? 30.053  -2.251  9.020   1.00 12.45  ?  243 ALA B CA  1 
ATOM   3928 C  C   . ALA B 1 243 ? 28.527  -2.369  8.895   1.00 12.96  ?  243 ALA B C   1 
ATOM   3929 O  O   . ALA B 1 243 ? 27.902  -2.893  9.799   1.00 13.47  ?  243 ALA B O   1 
ATOM   3930 C  CB  . ALA B 1 243 ? 30.438  -0.874  9.433   1.00 13.89  ?  243 ALA B CB  1 
ATOM   3931 N  N   . SER B 1 244 ? 27.951  -1.976  7.753   1.00 13.92  ?  244 SER B N   1 
ATOM   3932 C  CA  . SER B 1 244 ? 26.505  -2.111  7.555   1.00 15.47  ?  244 SER B CA  1 
ATOM   3933 C  C   . SER B 1 244 ? 26.119  -3.578  7.410   1.00 15.11  ?  244 SER B C   1 
ATOM   3934 O  O   . SER B 1 244 ? 25.094  -3.961  7.926   1.00 14.74  ?  244 SER B O   1 
ATOM   3935 C  CB  . SER B 1 244 ? 25.941  -1.293  6.424   1.00 19.92  ?  244 SER B CB  1 
ATOM   3936 O  OG  . SER B 1 244 ? 25.723  0.043   6.924   1.00 27.29  ?  244 SER B OG  1 
ATOM   3937 N  N   . ARG B 1 245 ? 26.962  -4.412  6.800   1.00 15.51  ?  245 ARG B N   1 
ATOM   3938 C  CA  . ARG B 1 245 ? 26.699  -5.830  6.710   1.00 15.04  ?  245 ARG B CA  1 
ATOM   3939 C  C   . ARG B 1 245 ? 26.733  -6.481  8.096   1.00 15.67  ?  245 ARG B C   1 
ATOM   3940 O  O   . ARG B 1 245 ? 25.903  -7.342  8.412   1.00 12.80  ?  245 ARG B O   1 
ATOM   3941 C  CB  . ARG B 1 245 ? 27.656  -6.481  5.702   1.00 17.35  ?  245 ARG B CB  1 
ATOM   3942 C  CG  . ARG B 1 245 ? 27.382  -7.949  5.422   1.00 20.29  ?  245 ARG B CG  1 
ATOM   3943 C  CD  . ARG B 1 245 ? 26.111  -8.108  4.567   1.00 23.96  ?  245 ARG B CD  1 
ATOM   3944 N  NE  . ARG B 1 245 ? 25.810  -9.506  4.225   1.00 22.56  ?  245 ARG B NE  1 
ATOM   3945 C  CZ  . ARG B 1 245 ? 24.661  -9.891  3.668   1.00 25.34  ?  245 ARG B CZ  1 
ATOM   3946 N  NH1 . ARG B 1 245 ? 23.674  -9.007  3.440   1.00 23.87  1  245 ARG B NH1 1 
ATOM   3947 N  NH2 . ARG B 1 245 ? 24.462  -11.177 3.407   1.00 22.60  ?  245 ARG B NH2 1 
ATOM   3948 N  N   . MET B 1 246 ? 27.677  -6.057  8.936   1.00 13.49  ?  246 MET B N   1 
ATOM   3949 C  CA  . MET B 1 246 ? 27.742  -6.555  10.296  1.00 14.87  ?  246 MET B CA  1 
ATOM   3950 C  C   . MET B 1 246 ? 26.476  -6.223  11.084  1.00 14.07  ?  246 MET B C   1 
ATOM   3951 O  O   . MET B 1 246 ? 25.954  -7.064  11.803  1.00 14.58  ?  246 MET B O   1 
ATOM   3952 C  CB  . MET B 1 246 ? 28.999  -5.993  10.979  1.00 15.45  ?  246 MET B CB  1 
ATOM   3953 C  CG  . MET B 1 246 ? 29.291  -6.680  12.308  1.00 20.61  ?  246 MET B CG  1 
ATOM   3954 S  SD  . MET B 1 246 ? 30.925  -6.222  12.963  1.00 25.53  ?  246 MET B SD  1 
ATOM   3955 C  CE  . MET B 1 246 ? 30.625  -4.541  13.440  1.00 30.33  ?  246 MET B CE  1 
ATOM   3956 N  N   . ALA B 1 247 ? 25.981  -4.985  10.951  1.00 12.39  ?  247 ALA B N   1 
ATOM   3957 C  CA  . ALA B 1 247 ? 24.740  -4.577  11.606  1.00 12.22  ?  247 ALA B CA  1 
ATOM   3958 C  C   . ALA B 1 247 ? 23.558  -5.432  11.135  1.00 13.67  ?  247 ALA B C   1 
ATOM   3959 O  O   . ALA B 1 247 ? 22.731  -5.839  11.966  1.00 12.42  ?  247 ALA B O   1 
ATOM   3960 C  CB  . ALA B 1 247 ? 24.504  -3.113  11.352  1.00 11.83  ?  247 ALA B CB  1 
ATOM   3961 N  N   . THR B 1 248 ? 23.477  -5.697  9.819   1.00 12.57  ?  248 THR B N   1 
ATOM   3962 C  CA  . THR B 1 248 ? 22.417  -6.515  9.235   1.00 13.72  ?  248 THR B CA  1 
ATOM   3963 C  C   . THR B 1 248 ? 22.464  -7.931  9.813   1.00 14.39  ?  248 THR B C   1 
ATOM   3964 O  O   . THR B 1 248 ? 21.439  -8.463  10.219  1.00 14.12  ?  248 THR B O   1 
ATOM   3965 C  CB  . THR B 1 248 ? 22.507  -6.514  7.703   1.00 15.40  ?  248 THR B CB  1 
ATOM   3966 O  OG1 . THR B 1 248 ? 22.222  -5.176  7.332   1.00 15.49  ?  248 THR B OG1 1 
ATOM   3967 C  CG2 . THR B 1 248 ? 21.546  -7.488  7.056   1.00 15.24  ?  248 THR B CG2 1 
ATOM   3968 N  N   . LEU B 1 249 ? 23.644  -8.560  9.858   1.00 12.41  ?  249 LEU B N   1 
ATOM   3969 C  CA  . LEU B 1 249 ? 23.762  -9.927  10.341  1.00 13.60  ?  249 LEU B CA  1 
ATOM   3970 C  C   . LEU B 1 249 ? 23.509  -10.038 11.842  1.00 13.00  ?  249 LEU B C   1 
ATOM   3971 O  O   . LEU B 1 249 ? 23.022  -11.055 12.291  1.00 14.09  ?  249 LEU B O   1 
ATOM   3972 C  CB  . LEU B 1 249 ? 25.145  -10.471 9.974   1.00 15.30  ?  249 LEU B CB  1 
ATOM   3973 C  CG  . LEU B 1 249 ? 25.399  -10.661 8.474   1.00 20.79  ?  249 LEU B CG  1 
ATOM   3974 C  CD1 . LEU B 1 249 ? 26.840  -11.147 8.151   1.00 22.47  ?  249 LEU B CD1 1 
ATOM   3975 C  CD2 . LEU B 1 249 ? 24.412  -11.637 7.960   1.00 22.29  ?  249 LEU B CD2 1 
ATOM   3976 N  N   . ALA B 1 250 ? 23.778  -8.975  12.619  1.00 11.51  ?  250 ALA B N   1 
ATOM   3977 C  CA  . ALA B 1 250 ? 23.602  -9.000  14.045  1.00 12.10  ?  250 ALA B CA  1 
ATOM   3978 C  C   . ALA B 1 250 ? 22.130  -9.190  14.411  1.00 12.19  ?  250 ALA B C   1 
ATOM   3979 O  O   . ALA B 1 250 ? 21.852  -9.770  15.447  1.00 13.33  ?  250 ALA B O   1 
ATOM   3980 C  CB  . ALA B 1 250 ? 24.125  -7.708  14.658  1.00 13.00  ?  250 ALA B CB  1 
ATOM   3981 N  N   . HIS B 1 251 ? 21.203  -8.708  13.566  1.00 10.56  ?  251 HIS B N   1 
ATOM   3982 C  CA  . HIS B 1 251 ? 19.775  -8.941  13.821  1.00 11.40  ?  251 HIS B CA  1 
ATOM   3983 C  C   . HIS B 1 251 ? 19.409  -10.427 13.916  1.00 12.35  ?  251 HIS B C   1 
ATOM   3984 O  O   . HIS B 1 251 ? 18.369  -10.769 14.492  1.00 13.51  ?  251 HIS B O   1 
ATOM   3985 C  CB  . HIS B 1 251 ? 18.895  -8.279  12.759  1.00 10.86  ?  251 HIS B CB  1 
ATOM   3986 C  CG  . HIS B 1 251 ? 18.673  -6.829  13.018  1.00 12.15  ?  251 HIS B CG  1 
ATOM   3987 N  ND1 . HIS B 1 251 ? 17.735  -6.337  13.909  1.00 12.63  ?  251 HIS B ND1 1 
ATOM   3988 C  CD2 . HIS B 1 251 ? 19.298  -5.778  12.493  1.00 11.76  ?  251 HIS B CD2 1 
ATOM   3989 C  CE1 . HIS B 1 251 ? 17.782  -5.009  13.869  1.00 13.35  ?  251 HIS B CE1 1 
ATOM   3990 N  NE2 . HIS B 1 251 ? 18.751  -4.649  13.050  1.00 13.18  ?  251 HIS B NE2 1 
ATOM   3991 N  N   . ASN B 1 252 ? 20.187  -11.289 13.268  1.00 12.52  ?  252 ASN B N   1 
ATOM   3992 C  CA  . ASN B 1 252 ? 19.936  -12.725 13.370  1.00 13.65  ?  252 ASN B CA  1 
ATOM   3993 C  C   . ASN B 1 252 ? 20.041  -13.202 14.801  1.00 13.06  ?  252 ASN B C   1 
ATOM   3994 O  O   . ASN B 1 252 ? 19.347  -14.153 15.193  1.00 14.20  ?  252 ASN B O   1 
ATOM   3995 C  CB  . ASN B 1 252 ? 20.862  -13.521 12.475  1.00 15.14  ?  252 ASN B CB  1 
ATOM   3996 C  CG  . ASN B 1 252 ? 20.591  -13.276 11.011  1.00 16.47  ?  252 ASN B CG  1 
ATOM   3997 O  OD1 . ASN B 1 252 ? 19.490  -12.869 10.605  1.00 15.02  ?  252 ASN B OD1 1 
ATOM   3998 N  ND2 . ASN B 1 252 ? 21.613  -13.531 10.233  1.00 15.82  ?  252 ASN B ND2 1 
ATOM   3999 N  N   . GLY B 1 253 ? 20.895  -12.548 15.594  1.00 13.73  ?  253 GLY B N   1 
ATOM   4000 C  CA  . GLY B 1 253 ? 21.041  -12.886 16.992  1.00 13.98  ?  253 GLY B CA  1 
ATOM   4001 C  C   . GLY B 1 253 ? 19.798  -12.496 17.787  1.00 15.00  ?  253 GLY B C   1 
ATOM   4002 O  O   . GLY B 1 253 ? 19.399  -13.221 18.698  1.00 15.61  ?  253 GLY B O   1 
ATOM   4003 N  N   . LEU B 1 254 ? 19.239  -11.321 17.484  1.00 14.26  ?  254 LEU B N   1 
ATOM   4004 C  CA  . LEU B 1 254 ? 17.987  -10.910 18.091  1.00 16.13  ?  254 LEU B CA  1 
ATOM   4005 C  C   . LEU B 1 254 ? 16.888  -11.917 17.786  1.00 16.56  ?  254 LEU B C   1 
ATOM   4006 O  O   . LEU B 1 254 ? 16.143  -12.265 18.701  1.00 18.43  ?  254 LEU B O   1 
ATOM   4007 C  CB  . LEU B 1 254 ? 17.562  -9.507  17.686  1.00 16.90  ?  254 LEU B CB  1 
ATOM   4008 C  CG  . LEU B 1 254 ? 18.557  -8.379  17.966  1.00 20.68  ?  254 LEU B CG  1 
ATOM   4009 C  CD1 . LEU B 1 254 ? 17.857  -7.056  17.733  1.00 20.39  ?  254 LEU B CD1 1 
ATOM   4010 C  CD2 . LEU B 1 254 ? 19.179  -8.448  19.303  1.00 21.41  ?  254 LEU B CD2 1 
ATOM   4011 N  N   . ALA B 1 255 ? 16.789  -12.378 16.519  1.00 16.33  ?  255 ALA B N   1 
ATOM   4012 C  CA  . ALA B 1 255 ? 15.796  -13.364 16.097  1.00 16.50  ?  255 ALA B CA  1 
ATOM   4013 C  C   . ALA B 1 255 ? 15.905  -14.674 16.866  1.00 18.38  ?  255 ALA B C   1 
ATOM   4014 O  O   . ALA B 1 255 ? 14.884  -15.300 17.123  1.00 18.77  ?  255 ALA B O   1 
ATOM   4015 C  CB  . ALA B 1 255 ? 15.906  -13.649 14.620  1.00 16.86  ?  255 ALA B CB  1 
ATOM   4016 N  N   . ARG B 1 256 ? 17.125  -15.098 17.214  1.00 17.18  ?  256 ARG B N   1 
ATOM   4017 C  CA  . ARG B 1 256 ? 17.321  -16.338 17.946  1.00 18.99  ?  256 ARG B CA  1 
ATOM   4018 C  C   . ARG B 1 256 ? 16.886  -16.204 19.412  1.00 19.02  ?  256 ARG B C   1 
ATOM   4019 O  O   . ARG B 1 256 ? 16.481  -17.184 20.011  1.00 22.80  ?  256 ARG B O   1 
ATOM   4020 C  CB  . ARG B 1 256 ? 18.782  -16.797 17.841  1.00 20.77  ?  256 ARG B CB  1 
ATOM   4021 C  CG  . ARG B 1 256 ? 19.155  -17.251 16.438  1.00 26.74  ?  256 ARG B CG  1 
ATOM   4022 C  CD  . ARG B 1 256 ? 20.633  -17.492 16.152  1.00 34.20  ?  256 ARG B CD  1 
ATOM   4023 N  NE  . ARG B 1 256 ? 21.290  -18.299 17.190  1.00 49.02  ?  256 ARG B NE  1 
ATOM   4024 C  CZ  . ARG B 1 256 ? 21.032  -19.559 17.610  1.00 70.32  ?  256 ARG B CZ  1 
ATOM   4025 N  NH1 . ARG B 1 256 ? 20.042  -20.287 17.100  1.00 69.45  1  256 ARG B NH1 1 
ATOM   4026 N  NH2 . ARG B 1 256 ? 21.780  -20.083 18.580  1.00 76.16  ?  256 ARG B NH2 1 
ATOM   4027 N  N   . ALA B 1 257 ? 16.958  -15.017 20.008  1.00 18.58  ?  257 ALA B N   1 
ATOM   4028 C  CA  . ALA B 1 257 ? 16.629  -14.828 21.413  1.00 18.51  ?  257 ALA B CA  1 
ATOM   4029 C  C   . ALA B 1 257 ? 15.177  -14.377 21.625  1.00 17.12  ?  257 ALA B C   1 
ATOM   4030 O  O   . ALA B 1 257 ? 14.627  -14.623 22.685  1.00 17.69  ?  257 ALA B O   1 
ATOM   4031 C  CB  . ALA B 1 257 ? 17.559  -13.785 22.016  1.00 20.74  ?  257 ALA B CB  1 
ATOM   4032 N  N   . ILE B 1 258 ? 14.601  -13.618 20.691  1.00 15.16  ?  258 ILE B N   1 
ATOM   4033 C  CA  . ILE B 1 258 ? 13.357  -12.900 20.949  1.00 15.70  ?  258 ILE B CA  1 
ATOM   4034 C  C   . ILE B 1 258 ? 12.287  -13.358 19.959  1.00 16.15  ?  258 ILE B C   1 
ATOM   4035 O  O   . ILE B 1 258 ? 12.556  -13.410 18.760  1.00 16.11  ?  258 ILE B O   1 
ATOM   4036 C  CB  . ILE B 1 258 ? 13.597  -11.378 20.875  1.00 15.45  ?  258 ILE B CB  1 
ATOM   4037 C  CG1 . ILE B 1 258 ? 14.622  -10.885 21.906  1.00 18.09  ?  258 ILE B CG1 1 
ATOM   4038 C  CG2 . ILE B 1 258 ? 12.285  -10.608 21.022  1.00 16.01  ?  258 ILE B CG2 1 
ATOM   4039 C  CD1 . ILE B 1 258 ? 15.120  -9.474  21.646  1.00 18.74  ?  258 ILE B CD1 1 
ATOM   4040 N  N   . CYS B 1 259 ? 11.047  -13.572 20.432  1.00 14.90  ?  259 CYS B N   1 
ATOM   4041 C  CA  . CYS B 1 259 ? 9.979   -13.979 19.529  1.00 17.01  ?  259 CYS B CA  1 
ATOM   4042 C  C   . CYS B 1 259 ? 8.617   -13.540 20.080  1.00 17.24  ?  259 CYS B C   1 
ATOM   4043 O  O   . CYS B 1 259 ? 8.294   -13.798 21.232  1.00 17.26  ?  259 CYS B O   1 
ATOM   4044 C  CB  . CYS B 1 259 ? 9.999   -15.492 19.302  1.00 20.76  ?  259 CYS B CB  1 
ATOM   4045 S  SG  . CYS B 1 259 ? 8.699   -16.005 18.139  1.00 26.52  ?  259 CYS B SG  1 
ATOM   4046 N  N   . PRO B 1 260 ? 7.748   -12.852 19.316  1.00 16.18  ?  260 PRO B N   1 
ATOM   4047 C  CA  . PRO B 1 260 ? 8.093   -12.282 18.022  1.00 16.29  ?  260 PRO B CA  1 
ATOM   4048 C  C   . PRO B 1 260 ? 9.082   -11.109 18.115  1.00 15.54  ?  260 PRO B C   1 
ATOM   4049 O  O   . PRO B 1 260 ? 9.231   -10.489 19.155  1.00 13.83  ?  260 PRO B O   1 
ATOM   4050 C  CB  . PRO B 1 260 ? 6.793   -11.726 17.469  1.00 17.15  ?  260 PRO B CB  1 
ATOM   4051 C  CG  . PRO B 1 260 ? 5.745   -12.047 18.509  1.00 18.89  ?  260 PRO B CG  1 
ATOM   4052 C  CD  . PRO B 1 260 ? 6.374   -12.529 19.743  1.00 17.14  ?  260 PRO B CD  1 
ATOM   4053 N  N   . ILE B 1 261 ? 9.699   -10.799 16.983  1.00 15.79  ?  261 ILE B N   1 
ATOM   4054 C  CA  . ILE B 1 261 ? 10.707  -9.760  16.845  1.00 14.70  ?  261 ILE B CA  1 
ATOM   4055 C  C   . ILE B 1 261 ? 10.362  -8.952  15.601  1.00 14.36  ?  261 ILE B C   1 
ATOM   4056 O  O   . ILE B 1 261 ? 9.664   -9.446  14.702  1.00 14.47  ?  261 ILE B O   1 
ATOM   4057 C  CB  . ILE B 1 261 ? 12.100  -10.422 16.789  1.00 15.32  ?  261 ILE B CB  1 
ATOM   4058 C  CG1 . ILE B 1 261 ? 13.250  -9.439  16.822  1.00 17.64  ?  261 ILE B CG1 1 
ATOM   4059 C  CG2 . ILE B 1 261 ? 12.198  -11.324 15.571  1.00 17.31  ?  261 ILE B CG2 1 
ATOM   4060 C  CD1 . ILE B 1 261 ? 13.301  -8.579  18.080  1.00 17.77  ?  261 ILE B CD1 1 
ATOM   4061 N  N   . HIS B 1 262 ? 10.895  -7.732  15.500  1.00 12.44  ?  262 HIS B N   1 
ATOM   4062 C  CA  . HIS B 1 262 ? 10.718  -6.887  14.326  1.00 12.43  ?  262 HIS B CA  1 
ATOM   4063 C  C   . HIS B 1 262 ? 9.234   -6.635  14.042  1.00 13.65  ?  262 HIS B C   1 
ATOM   4064 O  O   . HIS B 1 262 ? 8.839   -6.597  12.876  1.00 15.95  ?  262 HIS B O   1 
ATOM   4065 C  CB  . HIS B 1 262 ? 11.408  -7.511  13.112  1.00 13.45  ?  262 HIS B CB  1 
ATOM   4066 C  CG  . HIS B 1 262 ? 12.855  -7.877  13.271  1.00 14.42  ?  262 HIS B CG  1 
ATOM   4067 N  ND1 . HIS B 1 262 ? 13.791  -7.113  13.937  1.00 17.55  ?  262 HIS B ND1 1 
ATOM   4068 C  CD2 . HIS B 1 262 ? 13.538  -8.907  12.730  1.00 13.05  ?  262 HIS B CD2 1 
ATOM   4069 C  CE1 . HIS B 1 262 ? 15.001  -7.654  13.794  1.00 14.22  ?  262 HIS B CE1 1 
ATOM   4070 N  NE2 . HIS B 1 262 ? 14.859  -8.762  13.091  1.00 17.69  ?  262 HIS B NE2 1 
ATOM   4071 N  N   . THR B 1 263 ? 8.426   -6.507  15.099  1.00 13.85  ?  263 THR B N   1 
ATOM   4072 C  CA  . THR B 1 263 ? 6.976   -6.358  14.942  1.00 14.39  ?  263 THR B CA  1 
ATOM   4073 C  C   . THR B 1 263 ? 6.631   -4.901  14.630  1.00 14.41  ?  263 THR B C   1 
ATOM   4074 O  O   . THR B 1 263 ? 7.483   -4.014  14.618  1.00 14.88  ?  263 THR B O   1 
ATOM   4075 C  CB  . THR B 1 263 ? 6.228   -6.798  16.205  1.00 15.89  ?  263 THR B CB  1 
ATOM   4076 O  OG1 . THR B 1 263 ? 6.436   -5.822  17.223  1.00 15.65  ?  263 THR B OG1 1 
ATOM   4077 C  CG2 . THR B 1 263 ? 6.591   -8.213  16.646  1.00 17.46  ?  263 THR B CG2 1 
ATOM   4078 N  N   . ASN B 1 264 ? 5.336   -4.620  14.415  1.00 15.18  ?  264 ASN B N   1 
ATOM   4079 C  CA  . ASN B 1 264 ? 4.895   -3.261  14.108  1.00 15.82  ?  264 ASN B CA  1 
ATOM   4080 C  C   . ASN B 1 264 ? 5.017   -2.317  15.298  1.00 16.71  ?  264 ASN B C   1 
ATOM   4081 O  O   . ASN B 1 264 ? 4.828   -1.116  15.126  1.00 20.83  ?  264 ASN B O   1 
ATOM   4082 C  CB  . ASN B 1 264 ? 3.465   -3.234  13.603  1.00 19.27  ?  264 ASN B CB  1 
ATOM   4083 C  CG  . ASN B 1 264 ? 3.371   -3.885  12.239  1.00 25.43  ?  264 ASN B CG  1 
ATOM   4084 O  OD1 . ASN B 1 264 ? 4.372   -4.077  11.539  1.00 28.82  ?  264 ASN B OD1 1 
ATOM   4085 N  ND2 . ASN B 1 264 ? 2.157   -4.133  11.800  1.00 30.42  ?  264 ASN B ND2 1 
ATOM   4086 N  N   . VAL B 1 265 ? 5.239   -2.824  16.517  1.00 14.85  ?  265 VAL B N   1 
ATOM   4087 C  CA  . VAL B 1 265 ? 5.410   -1.948  17.656  1.00 15.39  ?  265 VAL B CA  1 
ATOM   4088 C  C   . VAL B 1 265 ? 6.873   -1.915  18.072  1.00 15.98  ?  265 VAL B C   1 
ATOM   4089 O  O   . VAL B 1 265 ? 7.210   -1.184  18.993  1.00 16.41  ?  265 VAL B O   1 
ATOM   4090 C  CB  . VAL B 1 265 ? 4.521   -2.267  18.876  1.00 18.03  ?  265 VAL B CB  1 
ATOM   4091 C  CG1 . VAL B 1 265 ? 3.043   -2.156  18.484  1.00 19.94  ?  265 VAL B CG1 1 
ATOM   4092 C  CG2 . VAL B 1 265 ? 4.796   -3.622  19.477  1.00 18.89  ?  265 VAL B CG2 1 
ATOM   4093 N  N   . ASP B 1 266 ? 7.753   -2.570  17.323  1.00 13.65  ?  266 ASP B N   1 
ATOM   4094 C  CA  . ASP B 1 266 ? 9.170   -2.574  17.681  1.00 13.43  ?  266 ASP B CA  1 
ATOM   4095 C  C   . ASP B 1 266 ? 9.962   -1.601  16.795  1.00 13.44  ?  266 ASP B C   1 
ATOM   4096 O  O   . ASP B 1 266 ? 9.762   -1.566  15.572  1.00 14.96  ?  266 ASP B O   1 
ATOM   4097 C  CB  . ASP B 1 266 ? 9.744   -3.971  17.531  1.00 13.07  ?  266 ASP B CB  1 
ATOM   4098 C  CG  . ASP B 1 266 ? 9.256   -4.970  18.583  1.00 13.60  ?  266 ASP B CG  1 
ATOM   4099 O  OD1 . ASP B 1 266 ? 9.309   -4.632  19.793  1.00 14.82  ?  266 ASP B OD1 1 
ATOM   4100 O  OD2 . ASP B 1 266 ? 8.873   -6.088  18.186  1.00 15.03  -1 266 ASP B OD2 1 
ATOM   4101 N  N   . GLY B 1 267 ? 10.903  -0.870  17.423  1.00 13.06  ?  267 GLY B N   1 
ATOM   4102 C  CA  . GLY B 1 267 ? 11.802  0.038   16.704  1.00 13.84  ?  267 GLY B CA  1 
ATOM   4103 C  C   . GLY B 1 267 ? 13.230  -0.516  16.604  1.00 13.53  ?  267 GLY B C   1 
ATOM   4104 O  O   . GLY B 1 267 ? 14.172  0.262   16.552  1.00 13.46  ?  267 GLY B O   1 
ATOM   4105 N  N   . ASP B 1 268 ? 13.362  -1.849  16.424  1.00 12.15  ?  268 ASP B N   1 
ATOM   4106 C  CA  . ASP B 1 268 ? 14.622  -2.556  16.542  1.00 12.29  ?  268 ASP B CA  1 
ATOM   4107 C  C   . ASP B 1 268 ? 15.664  -1.952  15.609  1.00 11.49  ?  268 ASP B C   1 
ATOM   4108 O  O   . ASP B 1 268 ? 15.437  -1.860  14.391  1.00 11.28  ?  268 ASP B O   1 
ATOM   4109 C  CB  . ASP B 1 268 ? 14.430  -4.043  16.271  1.00 12.51  ?  268 ASP B CB  1 
ATOM   4110 C  CG  . ASP B 1 268 ? 13.289  -4.679  17.070  1.00 14.08  ?  268 ASP B CG  1 
ATOM   4111 O  OD1 . ASP B 1 268 ? 13.064  -4.239  18.225  1.00 13.80  ?  268 ASP B OD1 1 
ATOM   4112 O  OD2 . ASP B 1 268 ? 12.667  -5.627  16.541  1.00 14.34  -1 268 ASP B OD2 1 
ATOM   4113 N  N   . THR B 1 269 ? 16.830  -1.624  16.186  1.00 11.45  ?  269 THR B N   1 
ATOM   4114 C  CA  . THR B 1 269 ? 17.900  -0.928  15.489  1.00 11.90  ?  269 THR B CA  1 
ATOM   4115 C  C   . THR B 1 269 ? 19.223  -1.426  16.048  1.00 11.73  ?  269 THR B C   1 
ATOM   4116 O  O   . THR B 1 269 ? 19.364  -1.507  17.271  1.00 11.86  ?  269 THR B O   1 
ATOM   4117 C  CB  . THR B 1 269 ? 17.829  0.583   15.710  1.00 12.60  ?  269 THR B CB  1 
ATOM   4118 O  OG1 . THR B 1 269 ? 16.628  1.123   15.174  1.00 12.68  ?  269 THR B OG1 1 
ATOM   4119 C  CG2 . THR B 1 269 ? 18.952  1.319   14.995  1.00 12.85  ?  269 THR B CG2 1 
ATOM   4120 N  N   . ILE B 1 270 ? 20.143  -1.792  15.158  1.00 10.95  ?  270 ILE B N   1 
ATOM   4121 C  CA  . ILE B 1 270 ? 21.497  -2.152  15.539  1.00 12.11  ?  270 ILE B CA  1 
ATOM   4122 C  C   . ILE B 1 270 ? 22.450  -1.207  14.821  1.00 12.00  ?  270 ILE B C   1 
ATOM   4123 O  O   . ILE B 1 270 ? 22.422  -1.083  13.609  1.00 12.97  ?  270 ILE B O   1 
ATOM   4124 C  CB  . ILE B 1 270 ? 21.864  -3.609  15.207  1.00 14.72  ?  270 ILE B CB  1 
ATOM   4125 C  CG1 . ILE B 1 270 ? 21.016  -4.621  15.950  1.00 16.86  ?  270 ILE B CG1 1 
ATOM   4126 C  CG2 . ILE B 1 270 ? 23.366  -3.880  15.406  1.00 15.56  ?  270 ILE B CG2 1 
ATOM   4127 C  CD1 . ILE B 1 270 ? 21.288  -4.687  17.428  1.00 21.19  ?  270 ILE B CD1 1 
ATOM   4128 N  N   . PHE B 1 271 ? 23.328  -0.584  15.600  1.00 12.89  ?  271 PHE B N   1 
ATOM   4129 C  CA  . PHE B 1 271 ? 24.479  0.149   15.103  1.00 12.46  ?  271 PHE B CA  1 
ATOM   4130 C  C   . PHE B 1 271 ? 25.688  -0.779  15.159  1.00 12.91  ?  271 PHE B C   1 
ATOM   4131 O  O   . PHE B 1 271 ? 25.840  -1.550  16.108  1.00 13.77  ?  271 PHE B O   1 
ATOM   4132 C  CB  . PHE B 1 271 ? 24.761  1.375   16.002  1.00 12.79  ?  271 PHE B CB  1 
ATOM   4133 C  CG  . PHE B 1 271 ? 23.637  2.393   16.098  1.00 13.15  ?  271 PHE B CG  1 
ATOM   4134 C  CD1 . PHE B 1 271 ? 23.478  3.378   15.145  1.00 13.33  ?  271 PHE B CD1 1 
ATOM   4135 C  CD2 . PHE B 1 271 ? 22.715  2.318   17.125  1.00 14.33  ?  271 PHE B CD2 1 
ATOM   4136 C  CE1 . PHE B 1 271 ? 22.439  4.285   15.236  1.00 15.85  ?  271 PHE B CE1 1 
ATOM   4137 C  CE2 . PHE B 1 271 ? 21.701  3.232   17.224  1.00 15.73  ?  271 PHE B CE2 1 
ATOM   4138 C  CZ  . PHE B 1 271 ? 21.567  4.224   16.286  1.00 14.73  ?  271 PHE B CZ  1 
ATOM   4139 N  N   . ALA B 1 272 ? 26.608  -0.677  14.185  1.00 13.86  ?  272 ALA B N   1 
ATOM   4140 C  CA  . ALA B 1 272 ? 27.828  -1.459  14.201  1.00 13.36  ?  272 ALA B CA  1 
ATOM   4141 C  C   . ALA B 1 272 ? 29.023  -0.532  14.018  1.00 13.24  ?  272 ALA B C   1 
ATOM   4142 O  O   . ALA B 1 272 ? 28.914  0.476   13.318  1.00 13.11  ?  272 ALA B O   1 
ATOM   4143 C  CB  . ALA B 1 272 ? 27.806  -2.517  13.098  1.00 13.71  ?  272 ALA B CB  1 
ATOM   4144 N  N   . THR B 1 273 ? 30.138  -0.862  14.684  1.00 12.92  ?  273 THR B N   1 
ATOM   4145 C  CA  . THR B 1 273 ? 31.380  -0.113  14.500  1.00 13.96  ?  273 THR B CA  1 
ATOM   4146 C  C   . THR B 1 273 ? 32.558  -1.063  14.331  1.00 12.69  ?  273 THR B C   1 
ATOM   4147 O  O   . THR B 1 273 ? 32.590  -2.155  14.911  1.00 13.67  ?  273 THR B O   1 
ATOM   4148 C  CB  . THR B 1 273 ? 31.690  0.841   15.669  1.00 15.68  ?  273 THR B CB  1 
ATOM   4149 O  OG1 . THR B 1 273 ? 31.992  0.082   16.844  1.00 16.22  ?  273 THR B OG1 1 
ATOM   4150 C  CG2 . THR B 1 273 ? 30.584  1.861   15.857  1.00 18.34  ?  273 THR B CG2 1 
ATOM   4151 N  N   . GLY B 1 274 ? 33.488  -0.645  13.479  1.00 13.18  ?  274 GLY B N   1 
ATOM   4152 C  CA  . GLY B 1 274 ? 34.856  -1.161  13.448  1.00 13.64  ?  274 GLY B CA  1 
ATOM   4153 C  C   . GLY B 1 274 ? 35.838  0.002   13.609  1.00 15.57  ?  274 GLY B C   1 
ATOM   4154 O  O   . GLY B 1 274 ? 35.437  1.149   13.646  1.00 13.91  ?  274 GLY B O   1 
ATOM   4155 N  N   . LEU B 1 275 ? 37.147  -0.296  13.741  1.00 17.98  ?  275 LEU B N   1 
ATOM   4156 C  CA  . LEU B 1 275 ? 38.160  0.748   13.882  1.00 20.02  ?  275 LEU B CA  1 
ATOM   4157 C  C   . LEU B 1 275 ? 38.628  1.214   12.501  1.00 19.76  ?  275 LEU B C   1 
ATOM   4158 O  O   . LEU B 1 275 ? 38.684  0.436   11.556  1.00 25.90  ?  275 LEU B O   1 
ATOM   4159 C  CB  . LEU B 1 275 ? 39.333  0.226   14.712  1.00 20.27  ?  275 LEU B CB  1 
ATOM   4160 C  CG  . LEU B 1 275 ? 39.047  -0.074  16.180  1.00 23.30  ?  275 LEU B CG  1 
ATOM   4161 C  CD1 . LEU B 1 275 ? 40.254  -0.705  16.886  1.00 27.12  ?  275 LEU B CD1 1 
ATOM   4162 C  CD2 . LEU B 1 275 ? 38.639  1.213   16.878  1.00 25.38  ?  275 LEU B CD2 1 
ATOM   4163 N  N   . GLN B 1 276 ? 38.909  2.510   12.350  1.00 20.34  ?  276 GLN B N   1 
ATOM   4164 C  CA  . GLN B 1 276 ? 39.469  3.013   11.101  1.00 21.40  ?  276 GLN B CA  1 
ATOM   4165 C  C   . GLN B 1 276 ? 40.922  2.564   10.967  1.00 24.69  ?  276 GLN B C   1 
ATOM   4166 O  O   . GLN B 1 276 ? 41.340  2.202   9.883   1.00 27.86  ?  276 GLN B O   1 
ATOM   4167 C  CB  . GLN B 1 276 ? 39.465  4.532   10.997  1.00 25.27  ?  276 GLN B CB  1 
ATOM   4168 C  CG  . GLN B 1 276 ? 38.063  5.102   10.877  1.00 30.28  ?  276 GLN B CG  1 
ATOM   4169 C  CD  . GLN B 1 276 ? 38.051  6.594   10.643  1.00 35.50  ?  276 GLN B CD  1 
ATOM   4170 O  OE1 . GLN B 1 276 ? 39.065  7.191   10.262  1.00 37.86  ?  276 GLN B OE1 1 
ATOM   4171 N  NE2 . GLN B 1 276 ? 36.889  7.193   10.864  1.00 30.54  ?  276 GLN B NE2 1 
ATOM   4172 N  N   . LYS B 1 277 ? 41.638  2.549   12.090  1.00 23.64  ?  277 LYS B N   1 
ATOM   4173 C  CA  . LYS B 1 277 ? 43.050  2.199   12.133  1.00 33.83  ?  277 LYS B CA  1 
ATOM   4174 C  C   . LYS B 1 277 ? 43.202  0.950   12.993  1.00 29.07  ?  277 LYS B C   1 
ATOM   4175 O  O   . LYS B 1 277 ? 43.091  0.984   14.201  1.00 37.81  ?  277 LYS B O   1 
ATOM   4176 C  CB  . LYS B 1 277 ? 43.875  3.331   12.762  1.00 40.65  ?  277 LYS B CB  1 
ATOM   4177 C  CG  . LYS B 1 277 ? 44.288  4.488   11.846  1.00 57.16  ?  277 LYS B CG  1 
ATOM   4178 C  CD  . LYS B 1 277 ? 45.252  4.126   10.713  1.00 65.07  ?  277 LYS B CD  1 
ATOM   4179 C  CE  . LYS B 1 277 ? 45.650  5.309   9.846   1.00 73.26  ?  277 LYS B CE  1 
ATOM   4180 N  NZ  . LYS B 1 277 ? 46.682  4.950   8.864   1.00 73.59  1  277 LYS B NZ  1 
ATOM   4181 N  N   . SER B 1 278 ? 43.407  -0.177  12.363  1.00 26.15  ?  278 SER B N   1 
ATOM   4182 C  CA  . SER B 1 278 ? 43.661  -1.400  13.085  1.00 24.98  ?  278 SER B CA  1 
ATOM   4183 C  C   . SER B 1 278 ? 44.382  -2.294  12.103  1.00 28.54  ?  278 SER B C   1 
ATOM   4184 O  O   . SER B 1 278 ? 44.138  -2.167  10.911  1.00 31.50  ?  278 SER B O   1 
ATOM   4185 C  CB  . SER B 1 278 ? 42.370  -2.034  13.590  1.00 24.47  ?  278 SER B CB  1 
ATOM   4186 O  OG  . SER B 1 278 ? 42.522  -3.388  13.998  1.00 22.37  ?  278 SER B OG  1 
ATOM   4187 N  N   . ASP B 1 279 ? 45.224  -3.176  12.644  1.00 34.10  ?  279 ASP B N   1 
ATOM   4188 C  CA  . ASP B 1 279 ? 45.941  -4.220  11.951  1.00 38.08  ?  279 ASP B CA  1 
ATOM   4189 C  C   . ASP B 1 279 ? 45.060  -5.425  11.666  1.00 34.82  ?  279 ASP B C   1 
ATOM   4190 O  O   . ASP B 1 279 ? 45.405  -6.219  10.818  1.00 35.02  ?  279 ASP B O   1 
ATOM   4191 C  CB  . ASP B 1 279 ? 46.923  -4.902  12.895  1.00 51.10  ?  279 ASP B CB  1 
ATOM   4192 C  CG  . ASP B 1 279 ? 48.195  -4.160  13.261  1.00 66.66  ?  279 ASP B CG  1 
ATOM   4193 O  OD1 . ASP B 1 279 ? 48.508  -3.157  12.578  1.00 67.72  ?  279 ASP B OD1 1 
ATOM   4194 O  OD2 . ASP B 1 279 ? 48.870  -4.618  14.221  1.00 72.71  -1 279 ASP B OD2 1 
ATOM   4195 N  N   . LEU B 1 280 ? 43.985  -5.606  12.439  1.00 26.13  ?  280 LEU B N   1 
ATOM   4196 C  CA  . LEU B 1 280 ? 43.260  -6.856  12.443  1.00 24.90  ?  280 LEU B CA  1 
ATOM   4197 C  C   . LEU B 1 280 ? 42.145  -6.786  11.408  1.00 22.67  ?  280 LEU B C   1 
ATOM   4198 O  O   . LEU B 1 280 ? 41.450  -5.784  11.352  1.00 18.23  ?  280 LEU B O   1 
ATOM   4199 C  CB  . LEU B 1 280 ? 42.650  -7.082  13.824  1.00 27.54  ?  280 LEU B CB  1 
ATOM   4200 C  CG  . LEU B 1 280 ? 43.609  -7.187  15.004  1.00 31.85  ?  280 LEU B CG  1 
ATOM   4201 C  CD1 . LEU B 1 280 ? 42.832  -7.357  16.286  1.00 34.19  ?  280 LEU B CD1 1 
ATOM   4202 C  CD2 . LEU B 1 280 ? 44.525  -8.353  14.774  1.00 31.39  ?  280 LEU B CD2 1 
ATOM   4203 N  N   . THR B 1 281 ? 42.022  -7.832  10.594  1.00 23.27  ?  281 THR B N   1 
ATOM   4204 C  CA  . THR B 1 281 ? 40.933  -7.965  9.637   1.00 24.11  ?  281 THR B CA  1 
ATOM   4205 C  C   . THR B 1 281 ? 40.467  -9.414  9.672   1.00 23.99  ?  281 THR B C   1 
ATOM   4206 O  O   . THR B 1 281 ? 41.178  -10.325 10.120  1.00 21.38  ?  281 THR B O   1 
ATOM   4207 C  CB  . THR B 1 281 ? 41.313  -7.566  8.201   1.00 26.64  ?  281 THR B CB  1 
ATOM   4208 O  OG1 . THR B 1 281 ? 42.350  -8.435  7.763   1.00 31.71  ?  281 THR B OG1 1 
ATOM   4209 C  CG2 . THR B 1 281 ? 41.811  -6.147  8.057   1.00 30.13  ?  281 THR B CG2 1 
ATOM   4210 N  N   . ALA B 1 282 ? 39.210  -9.609  9.244   1.00 20.96  ?  282 ALA B N   1 
ATOM   4211 C  CA  . ALA B 1 282 ? 38.643  -10.934 9.158   1.00 20.10  ?  282 ALA B CA  1 
ATOM   4212 C  C   . ALA B 1 282 ? 37.452  -10.854 8.211   1.00 21.00  ?  282 ALA B C   1 
ATOM   4213 O  O   . ALA B 1 282 ? 36.981  -9.759  7.943   1.00 16.92  ?  282 ALA B O   1 
ATOM   4214 C  CB  . ALA B 1 282 ? 38.261  -11.421 10.522  1.00 20.57  ?  282 ALA B CB  1 
ATOM   4215 N  N   . PRO B 1 283 ? 36.965  -11.974 7.637   1.00 23.74  ?  283 PRO B N   1 
ATOM   4216 C  CA  . PRO B 1 283 ? 35.826  -11.886 6.728   1.00 23.42  ?  283 PRO B CA  1 
ATOM   4217 C  C   . PRO B 1 283 ? 34.596  -11.349 7.447   1.00 18.97  ?  283 PRO B C   1 
ATOM   4218 O  O   . PRO B 1 283 ? 34.335  -11.731 8.597   1.00 15.81  ?  283 PRO B O   1 
ATOM   4219 C  CB  . PRO B 1 283 ? 35.598  -13.318 6.256   1.00 23.49  ?  283 PRO B CB  1 
ATOM   4220 C  CG  . PRO B 1 283 ? 36.887  -14.020 6.632   1.00 27.87  ?  283 PRO B CG  1 
ATOM   4221 C  CD  . PRO B 1 283 ? 37.458  -13.348 7.837   1.00 24.49  ?  283 PRO B CD  1 
ATOM   4222 N  N   . VAL B 1 284 ? 33.814  -10.533 6.744   1.00 17.93  ?  284 VAL B N   1 
ATOM   4223 C  CA  . VAL B 1 284 ? 32.698  -9.862  7.384   1.00 18.58  ?  284 VAL B CA  1 
ATOM   4224 C  C   . VAL B 1 284 ? 31.587  -10.843 7.754   1.00 18.23  ?  284 VAL B C   1 
ATOM   4225 O  O   . VAL B 1 284 ? 30.833  -10.597 8.700   1.00 17.61  ?  284 VAL B O   1 
ATOM   4226 C  CB  . VAL B 1 284 ? 32.166  -8.701  6.531   1.00 22.35  ?  284 VAL B CB  1 
ATOM   4227 C  CG1 . VAL B 1 284 ? 31.412  -9.134  5.273   1.00 24.49  ?  284 VAL B CG1 1 
ATOM   4228 C  CG2 . VAL B 1 284 ? 31.300  -7.804  7.383   1.00 21.89  ?  284 VAL B CG2 1 
ATOM   4229 N  N   . ASP B 1 285 ? 31.450  -11.954 7.011   1.00 19.09  ?  285 ASP B N   1 
ATOM   4230 C  CA  . ASP B 1 285 ? 30.408  -12.931 7.331   1.00 17.52  ?  285 ASP B CA  1 
ATOM   4231 C  C   . ASP B 1 285 ? 30.701  -13.654 8.656   1.00 17.02  ?  285 ASP B C   1 
ATOM   4232 O  O   . ASP B 1 285 ? 29.789  -13.962 9.410   1.00 18.31  ?  285 ASP B O   1 
ATOM   4233 C  CB  . ASP B 1 285 ? 30.089  -13.848 6.151   1.00 18.88  ?  285 ASP B CB  1 
ATOM   4234 C  CG  . ASP B 1 285 ? 31.278  -14.585 5.542   1.00 20.25  ?  285 ASP B CG  1 
ATOM   4235 O  OD1 . ASP B 1 285 ? 32.434  -14.319 5.981   1.00 22.09  ?  285 ASP B OD1 1 
ATOM   4236 O  OD2 . ASP B 1 285 ? 31.061  -15.281 4.543   1.00 18.48  -1 285 ASP B OD2 1 
ATOM   4237 N  N   . LEU B 1 286 ? 31.982  -13.883 8.975   1.00 18.17  ?  286 LEU B N   1 
ATOM   4238 C  CA  . LEU B 1 286 ? 32.385  -14.367 10.286  1.00 17.11  ?  286 LEU B CA  1 
ATOM   4239 C  C   . LEU B 1 286 ? 32.122  -13.335 11.390  1.00 16.00  ?  286 LEU B C   1 
ATOM   4240 O  O   . LEU B 1 286 ? 31.571  -13.696 12.443  1.00 17.02  ?  286 LEU B O   1 
ATOM   4241 C  CB  . LEU B 1 286 ? 33.855  -14.757 10.281  1.00 18.75  ?  286 LEU B CB  1 
ATOM   4242 C  CG  . LEU B 1 286 ? 34.414  -15.248 11.611  1.00 22.97  ?  286 LEU B CG  1 
ATOM   4243 C  CD1 . LEU B 1 286 ? 33.607  -16.439 12.030  1.00 26.28  ?  286 LEU B CD1 1 
ATOM   4244 C  CD2 . LEU B 1 286 ? 35.925  -15.564 11.512  1.00 27.15  ?  286 LEU B CD2 1 
ATOM   4245 N  N   . LEU B 1 287 ? 32.530  -12.077 11.162  1.00 16.38  ?  287 LEU B N   1 
ATOM   4246 C  CA  . LEU B 1 287 ? 32.336  -11.019 12.141  1.00 16.65  ?  287 LEU B CA  1 
ATOM   4247 C  C   . LEU B 1 287 ? 30.847  -10.834 12.428  1.00 16.71  ?  287 LEU B C   1 
ATOM   4248 O  O   . LEU B 1 287 ? 30.423  -10.622 13.578  1.00 15.59  ?  287 LEU B O   1 
ATOM   4249 C  CB  . LEU B 1 287 ? 32.993  -9.727  11.665  1.00 16.94  ?  287 LEU B CB  1 
ATOM   4250 C  CG  . LEU B 1 287 ? 34.529  -9.748  11.627  1.00 17.95  ?  287 LEU B CG  1 
ATOM   4251 C  CD1 . LEU B 1 287 ? 35.056  -8.445  11.085  1.00 18.16  ?  287 LEU B CD1 1 
ATOM   4252 C  CD2 . LEU B 1 287 ? 35.122  -10.087 12.999  1.00 18.61  ?  287 LEU B CD2 1 
ATOM   4253 N  N   . GLY B 1 288 ? 30.046  -10.910 11.352  1.00 16.56  ?  288 GLY B N   1 
ATOM   4254 C  CA  . GLY B 1 288 ? 28.605  -10.756 11.484  1.00 14.68  ?  288 GLY B CA  1 
ATOM   4255 C  C   . GLY B 1 288 ? 27.949  -11.875 12.272  1.00 14.99  ?  288 GLY B C   1 
ATOM   4256 O  O   . GLY B 1 288 ? 26.990  -11.621 13.014  1.00 16.58  ?  288 GLY B O   1 
ATOM   4257 N  N   . THR B 1 289 ? 28.404  -13.113 12.063  1.00 13.27  ?  289 THR B N   1 
ATOM   4258 C  CA  . THR B 1 289 ? 27.933  -14.252 12.833  1.00 13.91  ?  289 THR B CA  1 
ATOM   4259 C  C   . THR B 1 289 ? 28.280  -14.106 14.313  1.00 13.51  ?  289 THR B C   1 
ATOM   4260 O  O   . THR B 1 289 ? 27.473  -14.377 15.213  1.00 15.19  ?  289 THR B O   1 
ATOM   4261 C  CB  . THR B 1 289 ? 28.470  -15.559 12.249  1.00 16.17  ?  289 THR B CB  1 
ATOM   4262 O  OG1 . THR B 1 289 ? 28.142  -15.571 10.861  1.00 16.87  ?  289 THR B OG1 1 
ATOM   4263 C  CG2 . THR B 1 289 ? 27.783  -16.750 12.899  1.00 16.84  ?  289 THR B CG2 1 
ATOM   4264 N  N   . ALA B 1 290 ? 29.507  -13.673 14.593  1.00 13.86  ?  290 ALA B N   1 
ATOM   4265 C  CA  . ALA B 1 290 ? 29.908  -13.391 15.955  1.00 15.08  ?  290 ALA B CA  1 
ATOM   4266 C  C   . ALA B 1 290 ? 29.129  -12.217 16.538  1.00 15.43  ?  290 ALA B C   1 
ATOM   4267 O  O   . ALA B 1 290 ? 28.855  -12.225 17.729  1.00 14.78  ?  290 ALA B O   1 
ATOM   4268 C  CB  . ALA B 1 290 ? 31.414  -13.124 16.000  1.00 15.36  ?  290 ALA B CB  1 
ATOM   4269 N  N   . ALA B 1 291 ? 28.840  -11.175 15.749  1.00 14.12  ?  291 ALA B N   1 
ATOM   4270 C  CA  . ALA B 1 291 ? 27.996  -10.088 16.240  1.00 14.28  ?  291 ALA B CA  1 
ATOM   4271 C  C   . ALA B 1 291 ? 26.604  -10.602 16.633  1.00 14.28  ?  291 ALA B C   1 
ATOM   4272 O  O   . ALA B 1 291 ? 26.031  -10.161 17.638  1.00 13.29  ?  291 ALA B O   1 
ATOM   4273 C  CB  . ALA B 1 291 ? 27.888  -9.001  15.183  1.00 15.21  ?  291 ALA B CB  1 
ATOM   4274 N  N   . ALA B 1 292 ? 26.072  -11.566 15.866  1.00 13.76  ?  292 ALA B N   1 
ATOM   4275 C  CA  . ALA B 1 292 ? 24.791  -12.185 16.180  1.00 14.51  ?  292 ALA B CA  1 
ATOM   4276 C  C   . ALA B 1 292 ? 24.870  -12.937 17.516  1.00 15.02  ?  292 ALA B C   1 
ATOM   4277 O  O   . ALA B 1 292 ? 23.978  -12.826 18.366  1.00 13.75  ?  292 ALA B O   1 
ATOM   4278 C  CB  . ALA B 1 292 ? 24.366  -13.136 15.088  1.00 15.29  ?  292 ALA B CB  1 
ATOM   4279 N  N   . GLU B 1 293 ? 25.964  -13.678 17.719  1.00 14.87  ?  293 GLU B N   1 
ATOM   4280 C  CA  . GLU B 1 293 ? 26.137  -14.396 18.968  1.00 15.39  ?  293 GLU B CA  1 
ATOM   4281 C  C   . GLU B 1 293 ? 26.249  -13.402 20.139  1.00 14.71  ?  293 GLU B C   1 
ATOM   4282 O  O   . GLU B 1 293 ? 25.580  -13.557 21.153  1.00 15.07  ?  293 GLU B O   1 
ATOM   4283 C  CB  . GLU B 1 293 ? 27.332  -15.336 18.928  1.00 16.19  ?  293 GLU B CB  1 
ATOM   4284 C  CG  . GLU B 1 293 ? 27.504  -16.090 20.233  1.00 17.54  ?  293 GLU B CG  1 
ATOM   4285 C  CD  . GLU B 1 293 ? 28.753  -16.967 20.340  1.00 21.68  ?  293 GLU B CD  1 
ATOM   4286 O  OE1 . GLU B 1 293 ? 29.699  -16.914 19.546  1.00 20.20  ?  293 GLU B OE1 1 
ATOM   4287 O  OE2 . GLU B 1 293 ? 28.741  -17.701 21.333  1.00 25.88  -1 293 GLU B OE2 1 
ATOM   4288 N  N   . ALA B 1 294 ? 27.076  -12.369 19.985  1.00 16.42  ?  294 ALA B N   1 
ATOM   4289 C  CA  . ALA B 1 294 ? 27.243  -11.339 21.014  1.00 16.61  ?  294 ALA B CA  1 
ATOM   4290 C  C   . ALA B 1 294 ? 25.920  -10.664 21.348  1.00 14.74  ?  294 ALA B C   1 
ATOM   4291 O  O   . ALA B 1 294 ? 25.612  -10.488 22.523  1.00 15.45  ?  294 ALA B O   1 
ATOM   4292 C  CB  . ALA B 1 294 ? 28.310  -10.328 20.609  1.00 16.58  ?  294 ALA B CB  1 
ATOM   4293 N  N   . ALA B 1 295 ? 25.142  -10.289 20.335  1.00 14.97  ?  295 ALA B N   1 
ATOM   4294 C  CA  . ALA B 1 295 ? 23.859  -9.664  20.559  1.00 14.64  ?  295 ALA B CA  1 
ATOM   4295 C  C   . ALA B 1 295 ? 22.919  -10.587 21.324  1.00 14.71  ?  295 ALA B C   1 
ATOM   4296 O  O   . ALA B 1 295 ? 22.235  -10.136 22.228  1.00 13.98  ?  295 ALA B O   1 
ATOM   4297 C  CB  . ALA B 1 295 ? 23.252  -9.228  19.242  1.00 15.69  ?  295 ALA B CB  1 
ATOM   4298 N  N   . MET B 1 296 ? 22.886  -11.887 20.968  1.00 14.02  ?  296 MET B N   1 
ATOM   4299 C  CA  . MET B 1 296 ? 22.026  -12.857 21.630  1.00 16.28  ?  296 MET B CA  1 
ATOM   4300 C  C   . MET B 1 296 ? 22.399  -12.986 23.097  1.00 16.20  ?  296 MET B C   1 
ATOM   4301 O  O   . MET B 1 296 ? 21.526  -12.929 23.957  1.00 16.56  ?  296 MET B O   1 
ATOM   4302 C  CB  . MET B 1 296 ? 22.066  -14.232 20.930  1.00 18.76  ?  296 MET B CB  1 
ATOM   4303 C  CG  . MET B 1 296 ? 21.208  -15.298 21.592  1.00 24.90  ?  296 MET B CG  1 
ATOM   4304 S  SD  . MET B 1 296 ? 21.518  -16.922 20.863  1.00 36.87  ?  296 MET B SD  1 
ATOM   4305 C  CE  . MET B 1 296 ? 23.196  -17.228 21.445  1.00 40.55  ?  296 MET B CE  1 
ATOM   4306 N  N   . LEU B 1 297 ? 23.698  -13.131 23.389  1.00 15.95  ?  297 LEU B N   1 
ATOM   4307 C  CA  . LEU B 1 297 ? 24.172  -13.242 24.756  1.00 16.25  ?  297 LEU B CA  1 
ATOM   4308 C  C   . LEU B 1 297 ? 23.888  -11.968 25.575  1.00 15.17  ?  297 LEU B C   1 
ATOM   4309 O  O   . LEU B 1 297 ? 23.510  -12.060 26.746  1.00 16.36  ?  297 LEU B O   1 
ATOM   4310 C  CB  . LEU B 1 297 ? 25.668  -13.580 24.726  1.00 16.46  ?  297 LEU B CB  1 
ATOM   4311 C  CG  . LEU B 1 297 ? 26.069  -14.954 24.171  1.00 18.50  ?  297 LEU B CG  1 
ATOM   4312 C  CD1 . LEU B 1 297 ? 27.593  -15.062 24.063  1.00 20.09  ?  297 LEU B CD1 1 
ATOM   4313 C  CD2 . LEU B 1 297 ? 25.534  -16.039 25.071  1.00 20.78  ?  297 LEU B CD2 1 
ATOM   4314 N  N   . ALA B 1 298 ? 24.060  -10.774 24.974  1.00 14.88  ?  298 ALA B N   1 
ATOM   4315 C  CA  . ALA B 1 298 ? 23.762  -9.510  25.625  1.00 13.41  ?  298 ALA B CA  1 
ATOM   4316 C  C   . ALA B 1 298 ? 22.267  -9.384  25.958  1.00 14.46  ?  298 ALA B C   1 
ATOM   4317 O  O   . ALA B 1 298 ? 21.935  -8.775  26.974  1.00 14.38  ?  298 ALA B O   1 
ATOM   4318 C  CB  . ALA B 1 298 ? 24.226  -8.350  24.780  1.00 14.21  ?  298 ALA B CB  1 
ATOM   4319 N  N   . CYS B 1 299 ? 21.371  -9.920  25.102  1.00 13.69  ?  299 CYS B N   1 
ATOM   4320 C  CA  . CYS B 1 299 ? 19.946  -9.930  25.402  1.00 15.65  ?  299 CYS B CA  1 
ATOM   4321 C  C   . CYS B 1 299 ? 19.642  -10.674 26.714  1.00 16.52  ?  299 CYS B C   1 
ATOM   4322 O  O   . CYS B 1 299 ? 18.873  -10.191 27.552  1.00 16.45  ?  299 CYS B O   1 
ATOM   4323 C  CB  . CYS B 1 299 ? 19.140  -10.533 24.253  1.00 16.22  ?  299 CYS B CB  1 
ATOM   4324 S  SG  . CYS B 1 299 ? 19.020  -9.486  22.774  1.00 18.18  ?  299 CYS B SG  1 
ATOM   4325 N  N   . LEU B 1 300 ? 20.258  -11.850 26.891  1.00 17.46  ?  300 LEU B N   1 
ATOM   4326 C  CA  . LEU B 1 300 ? 20.085  -12.646 28.101  1.00 19.70  ?  300 LEU B CA  1 
ATOM   4327 C  C   . LEU B 1 300 ? 20.702  -11.959 29.312  1.00 19.46  ?  300 LEU B C   1 
ATOM   4328 O  O   . LEU B 1 300 ? 20.113  -11.958 30.396  1.00 21.59  ?  300 LEU B O   1 
ATOM   4329 C  CB  . LEU B 1 300 ? 20.680  -14.042 27.913  1.00 23.08  ?  300 LEU B CB  1 
ATOM   4330 C  CG  . LEU B 1 300 ? 19.956  -14.917 26.880  1.00 27.62  ?  300 LEU B CG  1 
ATOM   4331 C  CD1 . LEU B 1 300 ? 20.716  -16.200 26.635  1.00 31.07  ?  300 LEU B CD1 1 
ATOM   4332 C  CD2 . LEU B 1 300 ? 18.560  -15.236 27.324  1.00 30.00  ?  300 LEU B CD2 1 
ATOM   4333 N  N   . ASP B 1 301 ? 21.887  -11.366 29.117  1.00 16.82  ?  301 ASP B N   1 
ATOM   4334 C  CA  . ASP B 1 301 ? 22.562  -10.625 30.158  1.00 17.93  ?  301 ASP B CA  1 
ATOM   4335 C  C   . ASP B 1 301 ? 21.667  -9.526  30.741  1.00 18.07  ?  301 ASP B C   1 
ATOM   4336 O  O   . ASP B 1 301 ? 21.705  -9.271  31.940  1.00 17.77  ?  301 ASP B O   1 
ATOM   4337 C  CB  . ASP B 1 301 ? 23.895  -10.069 29.671  1.00 18.07  ?  301 ASP B CB  1 
ATOM   4338 C  CG  . ASP B 1 301 ? 24.728  -9.403  30.753  1.00 19.98  ?  301 ASP B CG  1 
ATOM   4339 O  OD1 . ASP B 1 301 ? 25.143  -10.140 31.656  1.00 20.24  ?  301 ASP B OD1 1 
ATOM   4340 O  OD2 . ASP B 1 301 ? 24.959  -8.168  30.713  1.00 17.15  -1 301 ASP B OD2 1 
ATOM   4341 N  N   . ALA B 1 302 ? 20.904  -8.854  29.879  1.00 17.72  ?  302 ALA B N   1 
ATOM   4342 C  CA  . ALA B 1 302 ? 20.067  -7.740  30.269  1.00 18.30  ?  302 ALA B CA  1 
ATOM   4343 C  C   . ALA B 1 302 ? 19.062  -8.137  31.331  1.00 21.81  ?  302 ALA B C   1 
ATOM   4344 O  O   . ALA B 1 302 ? 18.711  -7.292  32.140  1.00 22.20  ?  302 ALA B O   1 
ATOM   4345 C  CB  . ALA B 1 302 ? 19.351  -7.179  29.062  1.00 18.65  ?  302 ALA B CB  1 
ATOM   4346 N  N   . VAL B 1 303 ? 18.568  -9.387  31.293  1.00 24.33  ?  303 VAL B N   1 
ATOM   4347 C  CA  . VAL B 1 303 ? 17.494  -9.804  32.185  1.00 27.55  ?  303 VAL B CA  1 
ATOM   4348 C  C   . VAL B 1 303 ? 17.989  -10.662 33.352  1.00 32.12  ?  303 VAL B C   1 
ATOM   4349 O  O   . VAL B 1 303 ? 17.211  -10.920 34.243  1.00 35.92  ?  303 VAL B O   1 
ATOM   4350 C  CB  . VAL B 1 303 ? 16.348  -10.490 31.427  1.00 28.19  ?  303 VAL B CB  1 
ATOM   4351 C  CG1 . VAL B 1 303 ? 15.742  -9.560  30.392  1.00 30.57  ?  303 VAL B CG1 1 
ATOM   4352 C  CG2 . VAL B 1 303 ? 16.768  -11.803 30.760  1.00 31.57  ?  303 VAL B CG2 1 
ATOM   4353 N  N   . MET B 1 304 ? 19.261  -11.067 33.395  1.00 39.40  ?  304 MET B N   1 
ATOM   4354 C  CA  . MET B 1 304 ? 19.810  -11.824 34.512  1.00 43.21  ?  304 MET B CA  1 
ATOM   4355 C  C   . MET B 1 304 ? 20.705  -10.972 35.421  1.00 50.44  ?  304 MET B C   1 
ATOM   4356 O  O   . MET B 1 304 ? 21.403  -11.519 36.264  1.00 49.72  ?  304 MET B O   1 
ATOM   4357 C  CB  . MET B 1 304 ? 20.606  -13.019 33.973  1.00 48.82  ?  304 MET B CB  1 
ATOM   4358 C  CG  . MET B 1 304 ? 19.680  -14.137 33.510  1.00 55.73  ?  304 MET B CG  1 
ATOM   4359 S  SD  . MET B 1 304 ? 20.342  -15.257 32.263  1.00 67.41  ?  304 MET B SD  1 
ATOM   4360 C  CE  . MET B 1 304 ? 18.784  -16.057 31.855  1.00 70.65  ?  304 MET B CE  1 
ATOM   4361 N  N   . GLN B 1 305 ? 20.740  -9.647  35.219  1.00 52.71  ?  305 GLN B N   1 
ATOM   4362 C  CA  . GLN B 1 305 ? 21.584  -8.754  36.011  1.00 52.83  ?  305 GLN B CA  1 
ATOM   4363 C  C   . GLN B 1 305 ? 20.679  -7.811  36.816  1.00 47.34  ?  305 GLN B C   1 
ATOM   4364 O  O   . GLN B 1 305 ? 19.551  -7.600  36.323  1.00 56.21  ?  305 GLN B O   1 
ATOM   4365 C  CB  . GLN B 1 305 ? 22.576  -7.915  35.188  1.00 48.47  ?  305 GLN B CB  1 
ATOM   4366 C  CG  . GLN B 1 305 ? 23.654  -8.717  34.460  1.00 46.84  ?  305 GLN B CG  1 
ATOM   4367 C  CD  . GLN B 1 305 ? 24.702  -9.300  35.388  1.00 61.89  ?  305 GLN B CD  1 
ATOM   4368 O  OE1 . GLN B 1 305 ? 24.679  -10.493 35.723  1.00 63.77  ?  305 GLN B OE1 1 
ATOM   4369 N  NE2 . GLN B 1 305 ? 25.655  -8.469  35.796  1.00 71.81  ?  305 GLN B NE2 1 
HETATM 4370 C  C1  . EDO C 2 .   ? 25.410  18.335  7.129   1.00 44.10  ?  401 EDO A C1  1 
HETATM 4371 O  O1  . EDO C 2 .   ? 25.381  19.700  7.673   1.00 32.85  ?  401 EDO A O1  1 
HETATM 4372 C  C2  . EDO C 2 .   ? 25.919  17.264  8.085   1.00 46.60  ?  401 EDO A C2  1 
HETATM 4373 O  O2  . EDO C 2 .   ? 27.349  17.133  8.222   1.00 53.68  ?  401 EDO A O2  1 
HETATM 4374 NA NA  . NA  D 3 .   ? 24.871  22.246  3.168   1.00 17.27  ?  402 NA  A NA  1 
HETATM 4375 O  O1  A PG4 E 4 .   ? 10.167  2.995   19.665  0.50 38.92  ?  401 PG4 B O1  1 
HETATM 4376 O  O1  B PG4 E 4 .   ? 8.791   5.414   20.901  0.50 24.83  ?  401 PG4 B O1  1 
HETATM 4377 C  C1  A PG4 E 4 .   ? 9.263   3.767   20.450  0.50 45.01  ?  401 PG4 B C1  1 
HETATM 4378 C  C1  B PG4 E 4 .   ? 9.302   4.170   20.498  0.50 35.51  ?  401 PG4 B C1  1 
HETATM 4379 C  C2  A PG4 E 4 .   ? 8.900   5.087   19.819  0.50 45.73  ?  401 PG4 B C2  1 
HETATM 4380 C  C2  B PG4 E 4 .   ? 9.354   4.050   19.017  0.50 40.76  ?  401 PG4 B C2  1 
HETATM 4381 O  O2  A PG4 E 4 .   ? 8.947   4.969   18.401  0.50 51.05  ?  401 PG4 B O2  1 
HETATM 4382 O  O2  B PG4 E 4 .   ? 8.277   4.796   18.461  0.50 51.02  ?  401 PG4 B O2  1 
HETATM 4383 C  C3  A PG4 E 4 .   ? 8.636   6.174   17.709  0.50 54.77  ?  401 PG4 B C3  1 
HETATM 4384 C  C3  B PG4 E 4 .   ? 8.704   5.921   17.700  0.50 56.26  ?  401 PG4 B C3  1 
HETATM 4385 C  C4  A PG4 E 4 .   ? 7.408   6.817   18.286  0.50 59.60  ?  401 PG4 B C4  1 
HETATM 4386 C  C4  B PG4 E 4 .   ? 7.582   6.908   17.609  0.50 62.69  ?  401 PG4 B C4  1 
HETATM 4387 O  O3  A PG4 E 4 .   ? 6.234   6.243   17.718  0.50 61.23  ?  401 PG4 B O3  1 
HETATM 4388 O  O3  B PG4 E 4 .   ? 6.346   6.217   17.451  0.50 67.21  ?  401 PG4 B O3  1 
HETATM 4389 C  C5  A PG4 E 4 .   ? 5.072   7.031   17.954  0.50 60.70  ?  401 PG4 B C5  1 
HETATM 4390 C  C5  B PG4 E 4 .   ? 5.243   6.950   17.969  0.50 70.61  ?  401 PG4 B C5  1 
HETATM 4391 C  C6  A PG4 E 4 .   ? 5.138   8.289   17.134  0.50 58.90  ?  401 PG4 B C6  1 
HETATM 4392 C  C6  B PG4 E 4 .   ? 5.153   8.260   17.254  0.50 71.76  ?  401 PG4 B C6  1 
HETATM 4393 O  O4  A PG4 E 4 .   ? 4.461   8.103   15.891  0.50 55.20  ?  401 PG4 B O4  1 
HETATM 4394 O  O4  B PG4 E 4 .   ? 4.598   8.061   15.957  0.50 72.71  ?  401 PG4 B O4  1 
HETATM 4395 C  C7  A PG4 E 4 .   ? 3.602   9.194   15.563  0.50 45.72  ?  401 PG4 B C7  1 
HETATM 4396 C  C7  B PG4 E 4 .   ? 3.696   9.101   15.591  0.50 66.60  ?  401 PG4 B C7  1 
HETATM 4397 C  C8  A PG4 E 4 .   ? 3.674   10.250  16.644  0.50 46.05  ?  401 PG4 B C8  1 
HETATM 4398 C  C8  B PG4 E 4 .   ? 3.747   10.198  16.621  0.50 67.96  ?  401 PG4 B C8  1 
HETATM 4399 O  O5  A PG4 E 4 .   ? 2.808   11.365  16.417  0.50 37.55  ?  401 PG4 B O5  1 
HETATM 4400 O  O5  B PG4 E 4 .   ? 2.823   11.252  16.365  0.50 60.84  ?  401 PG4 B O5  1 
HETATM 4401 NA NA  . NA  F 3 .   ? 9.373   0.345   22.508  1.00 18.33  ?  402 NA  B NA  1 
HETATM 4402 O  O   . HOH G 5 .   ? 22.167  36.195  17.029  1.00 39.18  ?  501 HOH A O   1 
HETATM 4403 O  O   A HOH G 5 .   ? 24.879  31.461  9.876   0.50 2.36   ?  502 HOH A O   1 
HETATM 4404 O  O   B HOH G 5 .   ? 24.935  30.443  11.916  0.50 10.80  ?  502 HOH A O   1 
HETATM 4405 O  O   . HOH G 5 .   ? 7.481   24.785  24.878  1.00 37.74  ?  503 HOH A O   1 
HETATM 4406 O  O   . HOH G 5 .   ? 12.276  7.052   -0.795  1.00 34.58  ?  504 HOH A O   1 
HETATM 4407 O  O   . HOH G 5 .   ? 28.878  16.441  10.100  1.00 70.42  ?  505 HOH A O   1 
HETATM 4408 O  O   . HOH G 5 .   ? 1.635   14.543  27.032  1.00 28.75  ?  506 HOH A O   1 
HETATM 4409 O  O   . HOH G 5 .   ? 13.521  7.437   12.691  1.00 18.20  ?  507 HOH A O   1 
HETATM 4410 O  O   . HOH G 5 .   ? 4.928   35.619  -0.378  1.00 29.20  ?  508 HOH A O   1 
HETATM 4411 O  O   . HOH G 5 .   ? 28.519  35.900  -15.007 1.00 25.30  ?  509 HOH A O   1 
HETATM 4412 O  O   . HOH G 5 .   ? 17.539  5.320   8.773   1.00 26.64  ?  510 HOH A O   1 
HETATM 4413 O  O   . HOH G 5 .   ? -7.282  11.266  -11.841 1.00 35.14  ?  511 HOH A O   1 
HETATM 4414 O  O   . HOH G 5 .   ? 43.773  20.067  -14.991 1.00 27.73  ?  512 HOH A O   1 
HETATM 4415 O  O   . HOH G 5 .   ? -0.552  5.575   -8.265  1.00 36.42  ?  513 HOH A O   1 
HETATM 4416 O  O   . HOH G 5 .   ? 17.597  7.921   -2.162  1.00 29.99  ?  514 HOH A O   1 
HETATM 4417 O  O   . HOH G 5 .   ? 22.091  34.023  2.484   1.00 40.13  ?  515 HOH A O   1 
HETATM 4418 O  O   . HOH G 5 .   ? 10.900  35.595  9.839   1.00 30.22  ?  516 HOH A O   1 
HETATM 4419 O  O   . HOH G 5 .   ? 0.254   30.417  15.930  1.00 27.29  ?  517 HOH A O   1 
HETATM 4420 O  O   . HOH G 5 .   ? 1.173   11.162  9.265   1.00 22.84  ?  518 HOH A O   1 
HETATM 4421 O  O   A HOH G 5 .   ? 14.628  10.703  -8.941  0.50 12.92  ?  519 HOH A O   1 
HETATM 4422 O  O   B HOH G 5 .   ? 13.747  9.096   -9.680  0.50 16.30  ?  519 HOH A O   1 
HETATM 4423 O  O   . HOH G 5 .   ? 2.839   1.138   3.811   1.00 37.21  ?  520 HOH A O   1 
HETATM 4424 O  O   . HOH G 5 .   ? 30.587  32.172  10.375  1.00 24.93  ?  521 HOH A O   1 
HETATM 4425 O  O   . HOH G 5 .   ? 37.675  18.657  -10.176 1.00 27.99  ?  522 HOH A O   1 
HETATM 4426 O  O   . HOH G 5 .   ? 16.095  10.230  10.555  1.00 25.66  ?  523 HOH A O   1 
HETATM 4427 O  O   . HOH G 5 .   ? 16.897  12.109  -9.864  1.00 35.38  ?  524 HOH A O   1 
HETATM 4428 O  O   . HOH G 5 .   ? -3.683  25.982  4.389   1.00 35.71  ?  525 HOH A O   1 
HETATM 4429 O  O   . HOH G 5 .   ? 25.286  28.912  3.607   1.00 20.51  ?  526 HOH A O   1 
HETATM 4430 O  O   . HOH G 5 .   ? -0.369  19.032  13.353  1.00 29.98  ?  527 HOH A O   1 
HETATM 4431 O  O   . HOH G 5 .   ? 6.471   6.303   2.584   1.00 19.31  ?  528 HOH A O   1 
HETATM 4432 O  O   . HOH G 5 .   ? 13.196  30.088  -16.123 1.00 38.76  ?  529 HOH A O   1 
HETATM 4433 O  O   . HOH G 5 .   ? 16.544  7.846   6.430   1.00 23.99  ?  530 HOH A O   1 
HETATM 4434 O  O   . HOH G 5 .   ? 26.970  34.598  19.482  1.00 35.25  ?  531 HOH A O   1 
HETATM 4435 O  O   . HOH G 5 .   ? 30.036  25.652  -6.815  1.00 18.01  ?  532 HOH A O   1 
HETATM 4436 O  O   . HOH G 5 .   ? 28.525  23.151  -17.292 1.00 31.65  ?  533 HOH A O   1 
HETATM 4437 O  O   . HOH G 5 .   ? 21.268  34.622  -5.822  1.00 28.77  ?  534 HOH A O   1 
HETATM 4438 O  O   . HOH G 5 .   ? 0.174   1.929   -3.273  1.00 35.90  ?  535 HOH A O   1 
HETATM 4439 O  O   . HOH G 5 .   ? 19.631  29.410  7.230   1.00 18.69  ?  536 HOH A O   1 
HETATM 4440 O  O   . HOH G 5 .   ? 32.417  29.514  -4.460  1.00 17.63  ?  537 HOH A O   1 
HETATM 4441 O  O   . HOH G 5 .   ? 31.213  27.618  -19.032 1.00 32.06  ?  538 HOH A O   1 
HETATM 4442 O  O   . HOH G 5 .   ? 0.451   14.674  15.278  1.00 31.01  ?  539 HOH A O   1 
HETATM 4443 O  O   . HOH G 5 .   ? 21.911  18.114  -12.670 1.00 22.42  ?  540 HOH A O   1 
HETATM 4444 O  O   . HOH G 5 .   ? 24.440  20.833  -5.207  1.00 10.62  ?  541 HOH A O   1 
HETATM 4445 O  O   . HOH G 5 .   ? 22.034  20.747  -3.370  1.00 14.07  ?  542 HOH A O   1 
HETATM 4446 O  O   . HOH G 5 .   ? 3.353   30.199  -5.390  1.00 30.20  ?  543 HOH A O   1 
HETATM 4447 O  O   . HOH G 5 .   ? 21.092  27.690  22.253  1.00 31.55  ?  544 HOH A O   1 
HETATM 4448 O  O   A HOH G 5 .   ? 8.646   12.010  -14.323 0.50 7.59   ?  545 HOH A O   1 
HETATM 4449 O  O   B HOH G 5 .   ? 9.724   13.552  -14.918 0.50 17.55  ?  545 HOH A O   1 
HETATM 4450 O  O   . HOH G 5 .   ? 18.364  25.006  24.215  1.00 25.91  ?  546 HOH A O   1 
HETATM 4451 O  O   . HOH G 5 .   ? 31.174  32.983  13.520  1.00 43.05  ?  547 HOH A O   1 
HETATM 4452 O  O   . HOH G 5 .   ? -6.568  14.036  5.668   1.00 25.19  ?  548 HOH A O   1 
HETATM 4453 O  O   . HOH G 5 .   ? 29.004  29.409  -11.696 1.00 17.51  ?  549 HOH A O   1 
HETATM 4454 O  O   . HOH G 5 .   ? 16.756  30.920  20.124  1.00 30.89  ?  550 HOH A O   1 
HETATM 4455 O  O   . HOH G 5 .   ? 6.673   5.778   -11.077 1.00 21.37  ?  551 HOH A O   1 
HETATM 4456 O  O   . HOH G 5 .   ? -3.716  28.855  3.569   1.00 32.03  ?  552 HOH A O   1 
HETATM 4457 O  O   . HOH G 5 .   ? 6.302   26.387  27.911  1.00 38.96  ?  553 HOH A O   1 
HETATM 4458 O  O   . HOH G 5 .   ? 22.063  22.178  19.263  1.00 22.57  ?  554 HOH A O   1 
HETATM 4459 O  O   . HOH G 5 .   ? 20.438  17.394  5.360   1.00 17.19  ?  555 HOH A O   1 
HETATM 4460 O  O   . HOH G 5 .   ? -0.495  16.962  1.682   1.00 16.83  ?  556 HOH A O   1 
HETATM 4461 O  O   . HOH G 5 .   ? 32.426  31.502  -17.238 1.00 22.83  ?  557 HOH A O   1 
HETATM 4462 O  O   . HOH G 5 .   ? -0.627  14.095  9.955   1.00 29.51  ?  558 HOH A O   1 
HETATM 4463 O  O   . HOH G 5 .   ? 30.488  36.290  -3.801  1.00 47.47  ?  559 HOH A O   1 
HETATM 4464 O  O   . HOH G 5 .   ? 22.680  35.146  -7.999  1.00 36.73  ?  560 HOH A O   1 
HETATM 4465 O  O   . HOH G 5 .   ? -6.521  24.887  4.444   1.00 42.02  ?  561 HOH A O   1 
HETATM 4466 O  O   . HOH G 5 .   ? 21.209  24.728  18.646  1.00 28.98  ?  562 HOH A O   1 
HETATM 4467 O  O   . HOH G 5 .   ? -1.870  29.956  0.042   1.00 29.57  ?  563 HOH A O   1 
HETATM 4468 O  O   . HOH G 5 .   ? 27.611  24.138  -13.095 1.00 18.06  ?  564 HOH A O   1 
HETATM 4469 O  O   . HOH G 5 .   ? -2.446  19.206  6.235   1.00 30.12  ?  565 HOH A O   1 
HETATM 4470 O  O   . HOH G 5 .   ? -0.247  16.761  25.934  1.00 45.40  ?  566 HOH A O   1 
HETATM 4471 O  O   . HOH G 5 .   ? 4.068   32.576  7.443   1.00 28.57  ?  567 HOH A O   1 
HETATM 4472 O  O   . HOH G 5 .   ? 1.942   31.371  5.819   1.00 25.65  ?  568 HOH A O   1 
HETATM 4473 O  O   . HOH G 5 .   ? 34.101  17.506  -21.306 1.00 35.67  ?  569 HOH A O   1 
HETATM 4474 O  O   . HOH G 5 .   ? 15.754  7.796   1.445   1.00 16.63  ?  570 HOH A O   1 
HETATM 4475 O  O   . HOH G 5 .   ? 23.489  28.176  12.306  1.00 32.27  ?  571 HOH A O   1 
HETATM 4476 O  O   . HOH G 5 .   ? 5.772   33.771  22.861  1.00 45.87  ?  572 HOH A O   1 
HETATM 4477 O  O   . HOH G 5 .   ? -3.753  9.782   -5.818  1.00 22.27  ?  573 HOH A O   1 
HETATM 4478 O  O   . HOH G 5 .   ? 8.448   36.913  -0.364  1.00 33.34  ?  574 HOH A O   1 
HETATM 4479 O  O   . HOH G 5 .   ? 14.387  2.544   7.787   1.00 32.24  ?  575 HOH A O   1 
HETATM 4480 O  O   . HOH G 5 .   ? 19.334  30.430  18.465  1.00 40.20  ?  576 HOH A O   1 
HETATM 4481 O  O   . HOH G 5 .   ? -3.868  9.333   18.583  1.00 39.24  ?  577 HOH A O   1 
HETATM 4482 O  O   . HOH G 5 .   ? 9.640   30.345  -10.178 1.00 36.63  ?  578 HOH A O   1 
HETATM 4483 O  O   . HOH G 5 .   ? 10.864  2.123   11.559  1.00 19.28  ?  579 HOH A O   1 
HETATM 4484 O  O   . HOH G 5 .   ? 3.251   28.982  -8.202  1.00 31.51  ?  580 HOH A O   1 
HETATM 4485 O  O   . HOH G 5 .   ? 35.324  22.278  -19.042 1.00 37.07  ?  581 HOH A O   1 
HETATM 4486 O  O   . HOH G 5 .   ? -5.333  25.319  8.597   1.00 40.14  ?  582 HOH A O   1 
HETATM 4487 O  O   . HOH G 5 .   ? -1.889  18.645  3.635   1.00 29.75  ?  583 HOH A O   1 
HETATM 4488 O  O   . HOH G 5 .   ? 6.064   33.079  9.836   1.00 24.68  ?  584 HOH A O   1 
HETATM 4489 O  O   . HOH G 5 .   ? 0.114   25.381  -12.927 1.00 32.74  ?  585 HOH A O   1 
HETATM 4490 O  O   . HOH G 5 .   ? -0.499  3.349   3.113   1.00 25.37  ?  586 HOH A O   1 
HETATM 4491 O  O   . HOH G 5 .   ? 10.099  13.370  -12.488 1.00 26.90  ?  587 HOH A O   1 
HETATM 4492 O  O   . HOH G 5 .   ? 5.839   34.565  6.420   1.00 22.05  ?  588 HOH A O   1 
HETATM 4493 O  O   . HOH G 5 .   ? 22.344  24.137  -13.309 1.00 33.25  ?  589 HOH A O   1 
HETATM 4494 O  O   . HOH G 5 .   ? 24.366  24.274  19.616  1.00 28.44  ?  590 HOH A O   1 
HETATM 4495 O  O   . HOH G 5 .   ? 27.169  24.637  2.581   1.00 33.14  ?  591 HOH A O   1 
HETATM 4496 O  O   . HOH G 5 .   ? 27.740  28.473  5.256   1.00 22.71  ?  592 HOH A O   1 
HETATM 4497 O  O   . HOH G 5 .   ? 1.619   1.822   1.201   1.00 24.39  ?  593 HOH A O   1 
HETATM 4498 O  O   . HOH G 5 .   ? 25.008  36.500  -7.710  1.00 42.39  ?  594 HOH A O   1 
HETATM 4499 O  O   . HOH G 5 .   ? 5.259   -3.293  8.386   1.00 43.96  ?  595 HOH A O   1 
HETATM 4500 O  O   . HOH G 5 .   ? 16.745  27.056  23.713  1.00 27.08  ?  596 HOH A O   1 
HETATM 4501 O  O   . HOH G 5 .   ? 32.160  26.891  2.331   1.00 26.62  ?  597 HOH A O   1 
HETATM 4502 O  O   . HOH G 5 .   ? 34.225  28.476  2.811   1.00 35.58  ?  598 HOH A O   1 
HETATM 4503 O  O   . HOH G 5 .   ? 22.661  27.161  19.466  1.00 46.67  ?  599 HOH A O   1 
HETATM 4504 O  O   . HOH G 5 .   ? 14.584  26.830  26.048  1.00 47.55  ?  600 HOH A O   1 
HETATM 4505 O  O   . HOH G 5 .   ? 0.178   0.000   0.000   0.50 33.60  ?  601 HOH A O   1 
HETATM 4506 O  O   . HOH G 5 .   ? -1.856  0.000   0.000   0.50 51.17  ?  602 HOH A O   1 
HETATM 4507 O  O   . HOH H 5 .   ? 24.099  0.806   7.225   1.00 40.80  ?  501 HOH B O   1 
HETATM 4508 O  O   A HOH H 5 .   ? 9.562   5.752   32.524  0.50 2.26   ?  502 HOH B O   1 
HETATM 4509 O  O   B HOH H 5 .   ? 9.277   7.902   31.712  0.50 10.69  ?  502 HOH B O   1 
HETATM 4510 O  O   . HOH H 5 .   ? 29.468  19.254  31.186  1.00 41.46  ?  503 HOH B O   1 
HETATM 4511 O  O   . HOH H 5 .   ? 12.508  12.411  38.128  1.00 38.99  ?  504 HOH B O   1 
HETATM 4512 O  O   . HOH H 5 .   ? 41.364  7.400   11.076  1.00 47.62  ?  505 HOH B O   1 
HETATM 4513 O  O   . HOH H 5 .   ? 32.668  24.774  17.780  1.00 29.69  ?  506 HOH B O   1 
HETATM 4514 O  O   . HOH H 5 .   ? 18.191  9.015   11.472  1.00 22.54  ?  507 HOH B O   1 
HETATM 4515 O  O   . HOH H 5 .   ? 34.544  10.625  20.430  1.00 30.00  ?  508 HOH B O   1 
HETATM 4516 O  O   . HOH H 5 .   ? 15.588  12.960  35.419  1.00 36.44  ?  509 HOH B O   1 
HETATM 4517 O  O   . HOH H 5 .   ? 34.438  -9.491  28.710  1.00 27.86  ?  510 HOH B O   1 
HETATM 4518 O  O   . HOH H 5 .   ? 25.695  -15.749 10.038  1.00 25.70  ?  511 HOH B O   1 
HETATM 4519 O  O   . HOH H 5 .   ? 23.508  5.661   36.318  1.00 32.39  ?  512 HOH B O   1 
HETATM 4520 O  O   . HOH H 5 .   ? 2.478   -18.140 39.814  1.00 30.93  ?  513 HOH B O   1 
HETATM 4521 O  O   . HOH H 5 .   ? 38.142  -4.316  6.000   1.00 27.67  ?  514 HOH B O   1 
HETATM 4522 O  O   . HOH H 5 .   ? 36.394  9.749   10.653  1.00 33.75  ?  515 HOH B O   1 
HETATM 4523 O  O   . HOH H 5 .   ? -0.969  -21.577 19.843  1.00 39.49  ?  516 HOH B O   1 
HETATM 4524 O  O   . HOH H 5 .   ? 9.007   0.015   29.257  1.00 18.76  ?  517 HOH B O   1 
HETATM 4525 O  O   . HOH H 5 .   ? 29.491  -5.102  35.150  1.00 24.46  ?  518 HOH B O   1 
HETATM 4526 O  O   . HOH H 5 .   ? 37.882  0.840   26.400  1.00 34.56  ?  519 HOH B O   1 
HETATM 4527 O  O   . HOH H 5 .   ? 13.231  -10.045 33.683  1.00 27.62  ?  520 HOH B O   1 
HETATM 4528 O  O   . HOH H 5 .   ? 12.302  16.325  24.492  1.00 24.41  ?  521 HOH B O   1 
HETATM 4529 O  O   . HOH H 5 .   ? 38.162  1.206   6.323   1.00 38.84  ?  522 HOH B O   1 
HETATM 4530 O  O   . HOH H 5 .   ? 15.883  20.823  27.887  1.00 28.41  ?  523 HOH B O   1 
HETATM 4531 O  O   . HOH H 5 .   ? 18.596  -17.533 23.338  1.00 43.15  ?  524 HOH B O   1 
HETATM 4532 O  O   . HOH H 5 .   ? 27.746  1.765   6.498   1.00 22.02  ?  525 HOH B O   1 
HETATM 4533 O  O   . HOH H 5 .   ? 4.222   -10.164 24.672  1.00 15.59  ?  526 HOH B O   1 
HETATM 4534 O  O   . HOH H 5 .   ? 3.722   6.366   33.324  1.00 30.04  ?  527 HOH B O   1 
HETATM 4535 O  O   . HOH H 5 .   ? -3.568  -12.740 17.441  1.00 28.15  ?  528 HOH B O   1 
HETATM 4536 O  O   . HOH H 5 .   ? 14.736  3.435   30.174  1.00 16.42  ?  529 HOH B O   1 
HETATM 4537 O  O   . HOH H 5 .   ? 33.135  7.774   12.256  1.00 23.54  ?  530 HOH B O   1 
HETATM 4538 O  O   . HOH H 5 .   ? 32.507  1.754   31.735  1.00 25.78  ?  531 HOH B O   1 
HETATM 4539 O  O   . HOH H 5 .   ? 20.795  11.649  9.006   1.00 17.66  ?  532 HOH B O   1 
HETATM 4540 O  O   . HOH H 5 .   ? 12.238  -5.952  20.177  1.00 14.51  ?  533 HOH B O   1 
HETATM 4541 O  O   . HOH H 5 .   ? 27.496  -11.658 4.222   1.00 20.86  ?  534 HOH B O   1 
HETATM 4542 O  O   . HOH H 5 .   ? 34.223  -3.356  1.358   1.00 37.53  ?  535 HOH B O   1 
HETATM 4543 O  O   . HOH H 5 .   ? 1.977   -8.225  28.841  1.00 18.14  ?  536 HOH B O   1 
HETATM 4544 O  O   . HOH H 5 .   ? -9.490  -17.323 18.018  1.00 29.13  ?  537 HOH B O   1 
HETATM 4545 O  O   . HOH H 5 .   ? 38.085  -0.320  28.959  1.00 33.10  ?  538 HOH B O   1 
HETATM 4546 O  O   . HOH H 5 .   ? 9.879   -7.901  20.021  1.00 12.74  ?  539 HOH B O   1 
HETATM 4547 O  O   . HOH H 5 .   ? 16.411  -3.171  7.497   1.00 29.61  ?  540 HOH B O   1 
HETATM 4548 O  O   . HOH H 5 .   ? 40.792  3.827   14.620  1.00 29.04  ?  541 HOH B O   1 
HETATM 4549 O  O   . HOH H 5 .   ? 34.710  -0.469  16.988  1.00 14.06  ?  542 HOH B O   1 
HETATM 4550 O  O   . HOH H 5 .   ? 24.029  -13.967 11.538  1.00 26.43  ?  543 HOH B O   1 
HETATM 4551 O  O   . HOH H 5 .   ? 36.252  -3.959  29.607  1.00 24.02  ?  544 HOH B O   1 
HETATM 4552 O  O   . HOH H 5 .   ? 18.362  0.504   7.894   1.00 17.95  ?  545 HOH B O   1 
HETATM 4553 O  O   . HOH H 5 .   ? 7.958   -1.824  21.599  1.00 35.46  ?  546 HOH B O   1 
HETATM 4554 O  O   . HOH H 5 .   ? 5.366   -15.503 27.847  1.00 18.09  ?  547 HOH B O   1 
HETATM 4555 O  O   . HOH H 5 .   ? 26.458  -18.967 22.313  1.00 47.76  ?  548 HOH B O   1 
HETATM 4556 O  O   . HOH H 5 .   ? 10.120  -21.016 31.264  1.00 40.04  ?  549 HOH B O   1 
HETATM 4557 O  O   . HOH H 5 .   ? 34.896  8.110   15.167  1.00 25.63  ?  550 HOH B O   1 
HETATM 4558 O  O   . HOH H 5 .   ? 37.992  -6.896  8.829   1.00 22.63  ?  551 HOH B O   1 
HETATM 4559 O  O   . HOH H 5 .   ? 19.823  7.490   3.507   1.00 34.41  ?  552 HOH B O   1 
HETATM 4560 O  O   A HOH H 5 .   ? 19.549  -10.344 9.297   0.50 15.38  ?  553 HOH B O   1 
HETATM 4561 O  O   B HOH H 5 .   ? 20.442  -10.744 7.862   0.50 15.25  ?  553 HOH B O   1 
HETATM 4562 O  O   . HOH H 5 .   ? 6.664   -16.256 22.362  1.00 20.96  ?  554 HOH B O   1 
HETATM 4563 O  O   . HOH H 5 .   ? 28.102  -11.209 29.439  1.00 37.70  ?  555 HOH B O   1 
HETATM 4564 O  O   . HOH H 5 .   ? 13.124  15.276  26.901  1.00 25.31  ?  556 HOH B O   1 
HETATM 4565 O  O   . HOH H 5 .   ? 10.855  8.685   29.623  1.00 36.23  ?  557 HOH B O   1 
HETATM 4566 O  O   . HOH H 5 .   ? 36.763  14.515  17.452  1.00 41.72  ?  558 HOH B O   1 
HETATM 4567 O  O   . HOH H 5 .   ? 5.837   -19.928 33.699  1.00 33.18  ?  559 HOH B O   1 
HETATM 4568 O  O   . HOH H 5 .   ? 13.764  2.998   17.909  1.00 18.51  ?  560 HOH B O   1 
HETATM 4569 O  O   . HOH H 5 .   ? 34.796  -9.144  4.426   1.00 34.98  ?  561 HOH B O   1 
HETATM 4570 O  O   . HOH H 5 .   ? 6.995   -0.778  25.022  1.00 33.18  ?  562 HOH B O   1 
HETATM 4571 O  O   . HOH H 5 .   ? 42.473  -14.613 20.397  1.00 41.38  ?  563 HOH B O   1 
HETATM 4572 O  O   . HOH H 5 .   ? 30.964  -11.766 27.625  1.00 30.57  ?  564 HOH B O   1 
HETATM 4573 O  O   . HOH H 5 .   ? 40.357  -12.586 21.141  1.00 26.47  ?  565 HOH B O   1 
HETATM 4574 O  O   . HOH H 5 .   ? 23.342  11.174  3.565   1.00 16.74  ?  566 HOH B O   1 
HETATM 4575 O  O   . HOH H 5 .   ? 30.388  3.239   33.281  1.00 36.42  ?  567 HOH B O   1 
HETATM 4576 O  O   . HOH H 5 .   ? 5.174   2.345   37.151  1.00 42.59  ?  568 HOH B O   1 
HETATM 4577 O  O   . HOH H 5 .   ? 26.036  -4.865  36.731  1.00 33.13  ?  569 HOH B O   1 
HETATM 4578 O  O   . HOH H 5 .   ? 29.878  27.059  20.091  1.00 37.11  ?  570 HOH B O   1 
HETATM 4579 O  O   . HOH H 5 .   ? 36.828  3.813   19.798  1.00 22.42  ?  571 HOH B O   1 
HETATM 4580 O  O   . HOH H 5 .   ? 25.847  -16.716 15.851  1.00 36.49  ?  572 HOH B O   1 
HETATM 4581 O  O   . HOH H 5 .   ? 24.551  -14.085 28.574  1.00 39.59  ?  573 HOH B O   1 
HETATM 4582 O  O   . HOH H 5 .   ? 2.995   8.811   34.280  1.00 40.68  ?  574 HOH B O   1 
HETATM 4583 O  O   . HOH H 5 .   ? -4.363  -13.826 33.456  1.00 30.54  ?  575 HOH B O   1 
HETATM 4584 O  O   . HOH H 5 .   ? 38.125  17.144  11.478  1.00 29.74  ?  576 HOH B O   1 
HETATM 4585 O  O   . HOH H 5 .   ? 28.160  5.431   34.071  1.00 28.10  ?  577 HOH B O   1 
HETATM 4586 O  O   . HOH H 5 .   ? 5.701   -20.388 20.797  1.00 32.93  ?  578 HOH B O   1 
HETATM 4587 O  O   . HOH H 5 .   ? 34.738  2.530   3.588   1.00 25.83  ?  579 HOH B O   1 
HETATM 4588 O  O   . HOH H 5 .   ? 19.361  -4.033  37.670  1.00 29.49  ?  580 HOH B O   1 
HETATM 4589 O  O   . HOH H 5 .   ? 30.498  13.993  10.827  1.00 45.60  ?  581 HOH B O   1 
HETATM 4590 O  O   . HOH H 5 .   ? 28.471  1.850   35.148  1.00 22.69  ?  582 HOH B O   1 
HETATM 4591 O  O   . HOH H 5 .   ? 8.664   -2.981  35.461  1.00 43.60  ?  583 HOH B O   1 
HETATM 4592 O  O   . HOH H 5 .   ? 34.006  -16.206 23.116  1.00 33.02  ?  584 HOH B O   1 
HETATM 4593 O  O   . HOH H 5 .   ? 27.225  12.536  35.553  1.00 26.36  ?  585 HOH B O   1 
HETATM 4594 O  O   . HOH H 5 .   ? 33.910  9.921   2.549   1.00 33.84  ?  586 HOH B O   1 
HETATM 4595 O  O   . HOH H 5 .   ? 34.867  12.968  26.588  1.00 34.41  ?  587 HOH B O   1 
HETATM 4596 O  O   . HOH H 5 .   ? 6.634   1.610   29.007  1.00 21.19  ?  588 HOH B O   1 
HETATM 4597 O  O   . HOH H 5 .   ? 35.967  1.182   18.901  1.00 30.00  ?  589 HOH B O   1 
HETATM 4598 O  O   . HOH H 5 .   ? 32.608  0.959   1.951   1.00 23.94  ?  590 HOH B O   1 
HETATM 4599 O  O   . HOH H 5 .   ? 2.176   -1.424  26.936  1.00 32.25  ?  591 HOH B O   1 
HETATM 4600 O  O   . HOH H 5 .   ? 10.041  16.389  26.441  1.00 25.56  ?  592 HOH B O   1 
HETATM 4601 O  O   . HOH H 5 .   ? 17.661  19.952  29.910  1.00 23.45  ?  593 HOH B O   1 
HETATM 4602 O  O   . HOH H 5 .   ? 0.486   -0.940  28.393  1.00 35.76  ?  594 HOH B O   1 
HETATM 4603 O  O   . HOH H 5 .   ? 21.044  -21.470 14.267  1.00 33.29  ?  595 HOH B O   1 
HETATM 4604 O  O   . HOH H 5 .   ? 3.919   -22.242 19.183  1.00 45.33  ?  596 HOH B O   1 
HETATM 4605 O  O   . HOH H 5 .   ? 30.390  25.529  22.478  1.00 45.17  ?  597 HOH B O   1 
HETATM 4606 O  O   . HOH H 5 .   ? 3.294   -1.960  8.430   1.00 42.41  ?  598 HOH B O   1 
HETATM 4607 O  O   . HOH H 5 .   ? 19.838  14.495  34.483  1.00 27.81  ?  599 HOH B O   1 
HETATM 4608 O  O   . HOH H 5 .   ? 34.025  0.000   0.000   0.50 42.43  ?  600 HOH B O   1 
HETATM 4609 O  O   . HOH H 5 .   ? 18.470  12.796  36.017  1.00 42.84  ?  601 HOH B O   1 
# 
